data_9BI1
# 
_entry.id   9BI1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9BI1         pdb_00009bi1 10.2210/pdb9bi1/pdb 
WWPDB D_1000283410 ?            ?                   
# 
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 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BI1 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-22 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9BGH unspecified 
PDB . 9BHO unspecified 
PDB . 9BHP unspecified 
PDB . 9BHQ unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              litop@mskcc.org 
_pdbx_contact_author.name_first         Piro 
_pdbx_contact_author.name_last          Lito 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2196-3503 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pourfarjam, Y.'     1 ? 
'Goldgur, Y.'        2 ? 
'Cuevas-Navarro, A.' 3 ? 
'Lito, P.'           4 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nature 
_citation.journal_id_ASTM           NATUAS 
_citation.journal_id_CSD            0006 
_citation.journal_id_ISSN           1476-4687 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            637 
_citation.language                  ? 
_citation.page_first                224 
_citation.page_last                 229 
_citation.title                     'Pharmacological restoration of GTP hydrolysis by mutant RAS.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41586-024-08283-2 
_citation.pdbx_database_id_PubMed   39476862 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cuevas-Navarro, A.' 1  0000-0001-6208-6944 
primary 'Pourfarjam, Y.'     2  0009-0009-8881-6824 
primary 'Hu, F.'             3  0000-0001-9605-7594 
primary 'Rodriguez, D.J.'    4  0000-0002-0053-8674 
primary 'Vides, A.'          5  ?                   
primary 'Sang, B.'           6  ?                   
primary 'Fan, S.'            7  ?                   
primary 'Goldgur, Y.'        8  ?                   
primary 'de Stanchina, E.'   9  ?                   
primary 'Lito, P.'           10 0000-0003-2196-3503 
# 
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' 19386.848 2   3.6.5.2 G12D ? ? 
2 polymer     man 'Peptidyl-prolyl cis-trans isomerase A' 18093.555 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 
;(1R,5S,6r)-N-[(1P,7S,9S,13S,20M)-20-{5-(4-cyclopropylpiperazin-1-yl)-2-[(1S)-1-methoxyethyl]pyridin-3-yl}-21-ethyl-17,17-dimethyl-8,14-dioxo-15-oxa-4-thia-9,21,27,28-tetraazapentacyclo[17.5.2.1~2,5~.1~9,13~.0~22,26~]octacosa-1(24),2,5(28),19,22,25-hexaen-7-yl]-3-oxabicyclo[3.1.0]hexane-6-carboxamide
;
865.094   2   ?       ?    ? ? 
6 water       nat water 18.015    619 ?       ?    ? ? 
# 
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 
;GMTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
;GMTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
A,C ? 
2 'polypeptide(L)' no no 
;GMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;GMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
B,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP 
4 'MAGNESIUM ION' MG  
5 
;(1R,5S,6r)-N-[(1P,7S,9S,13S,20M)-20-{5-(4-cyclopropylpiperazin-1-yl)-2-[(1S)-1-methoxyethyl]pyridin-3-yl}-21-ethyl-17,17-dimethyl-8,14-dioxo-15-oxa-4-thia-9,21,27,28-tetraazapentacyclo[17.5.2.1~2,5~.1~9,13~.0~22,26~]octacosa-1(24),2,5(28),19,22,25-hexaen-7-yl]-3-oxabicyclo[3.1.0]hexane-6-carboxamide
;
ZNI 
6 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY 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  ASP n 
1 14  GLY n 
1 15  VAL n 
1 16  GLY n 
1 17  LYS n 
1 18  SER n 
1 19  ALA n 
1 20  LEU n 
1 21  THR n 
1 22  ILE n 
1 23  GLN n 
1 24  LEU n 
1 25  ILE n 
1 26  GLN n 
1 27  ASN n 
1 28  HIS n 
1 29  PHE n 
1 30  VAL n 
1 31  ASP n 
1 32  GLU n 
1 33  TYR n 
1 34  ASP n 
1 35  PRO n 
1 36  THR n 
1 37  ILE n 
1 38  GLU n 
1 39  ASP n 
1 40  SER n 
1 41  TYR n 
1 42  ARG n 
1 43  LYS n 
1 44  GLN n 
1 45  VAL n 
1 46  VAL n 
1 47  ILE n 
1 48  ASP n 
1 49  GLY n 
1 50  GLU n 
1 51  THR n 
1 52  CYS n 
1 53  LEU n 
1 54  LEU n 
1 55  ASP n 
1 56  ILE n 
1 57  LEU n 
1 58  ASP n 
1 59  THR n 
1 60  ALA n 
1 61  GLY n 
1 62  GLN n 
1 63  GLU n 
1 64  GLU n 
1 65  TYR n 
1 66  SER n 
1 67  ALA n 
1 68  MET n 
1 69  ARG n 
1 70  ASP n 
1 71  GLN n 
1 72  TYR n 
1 73  MET n 
1 74  ARG n 
1 75  THR n 
1 76  GLY n 
1 77  GLU n 
1 78  GLY n 
1 79  PHE n 
1 80  LEU n 
1 81  CYS n 
1 82  VAL n 
1 83  PHE n 
1 84  ALA n 
1 85  ILE n 
1 86  ASN n 
1 87  ASN n 
1 88  THR n 
1 89  LYS n 
1 90  SER n 
1 91  PHE n 
1 92  GLU n 
1 93  ASP n 
1 94  ILE n 
1 95  HIS n 
1 96  HIS n 
1 97  TYR n 
1 98  ARG n 
1 99  GLU n 
1 100 GLN n 
1 101 ILE n 
1 102 LYS n 
1 103 ARG n 
1 104 VAL n 
1 105 LYS n 
1 106 ASP n 
1 107 SER n 
1 108 GLU n 
1 109 ASP n 
1 110 VAL n 
1 111 PRO n 
1 112 MET n 
1 113 VAL n 
1 114 LEU n 
1 115 VAL n 
1 116 GLY n 
1 117 ASN n 
1 118 LYS n 
1 119 CYS n 
1 120 ASP n 
1 121 LEU n 
1 122 PRO n 
1 123 SER n 
1 124 ARG n 
1 125 THR n 
1 126 VAL n 
1 127 ASP n 
1 128 THR n 
1 129 LYS n 
1 130 GLN n 
1 131 ALA n 
1 132 GLN n 
1 133 ASP n 
1 134 LEU n 
1 135 ALA n 
1 136 ARG n 
1 137 SER n 
1 138 TYR n 
1 139 GLY n 
1 140 ILE n 
1 141 PRO n 
1 142 PHE n 
1 143 ILE n 
1 144 GLU n 
1 145 THR n 
1 146 SER n 
1 147 ALA n 
1 148 LYS n 
1 149 THR n 
1 150 ARG n 
1 151 GLN n 
1 152 GLY n 
1 153 VAL n 
1 154 ASP n 
1 155 ASP n 
1 156 ALA n 
1 157 PHE n 
1 158 TYR n 
1 159 THR n 
1 160 LEU n 
1 161 VAL n 
1 162 ARG n 
1 163 GLU n 
1 164 ILE n 
1 165 ARG n 
1 166 LYS n 
1 167 HIS n 
1 168 LYS n 
1 169 GLU n 
1 170 LYS n 
2 1   GLY 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 
ALA 'L-peptide linking' y ALANINE ?        'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ?        'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?        'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?        'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?        'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?        'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?        'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?        'C2 H5 N O2'        75.067  
GNP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ?        'C10 H17 N6 O13 P3' 522.196 
HIS 'L-peptide linking' y HISTIDINE ?        'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?        'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?        'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?        'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?        'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?        'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION' ?        'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE ?        'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?        'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?        'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?        'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?        'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?        'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?        'C5 H11 N O2'       117.146 
ZNI non-polymer         . 
;(1R,5S,6r)-N-[(1P,7S,9S,13S,20M)-20-{5-(4-cyclopropylpiperazin-1-yl)-2-[(1S)-1-methoxyethyl]pyridin-3-yl}-21-ethyl-17,17-dimethyl-8,14-dioxo-15-oxa-4-thia-9,21,27,28-tetraazapentacyclo[17.5.2.1~2,5~.1~9,13~.0~22,26~]octacosa-1(24),2,5(28),19,22,25-hexaen-7-yl]-3-oxabicyclo[3.1.0]hexane-6-carboxamide
;
RMC-7977 'C47 H60 N8 O6 S'   865.094 
# 
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   GLY 1   0   0   GLY GLY 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  ASP 13  12  12  ASP ASP A . n 
A 1 14  GLY 14  13  13  GLY GLY A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLY 16  15  15  GLY GLY A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  ALA 19  18  18  ALA ALA A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  THR 21  20  20  THR THR A . n 
A 1 22  ILE 22  21  21  ILE ILE A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  ILE 25  24  24  ILE ILE A . n 
A 1 26  GLN 26  25  25  GLN GLN A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  HIS 28  27  27  HIS HIS A . n 
A 1 29  PHE 29  28  28  PHE PHE A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  ASP 31  30  30  ASP ASP A . n 
A 1 32  GLU 32  31  31  GLU GLU A . n 
A 1 33  TYR 33  32  32  TYR TYR A . n 
A 1 34  ASP 34  33  33  ASP ASP A . n 
A 1 35  PRO 35  34  34  PRO PRO A . n 
A 1 36  THR 36  35  35  THR THR A . n 
A 1 37  ILE 37  36  36  ILE ILE A . n 
A 1 38  GLU 38  37  37  GLU GLU A . n 
A 1 39  ASP 39  38  38  ASP ASP A . n 
A 1 40  SER 40  39  39  SER SER A . n 
A 1 41  TYR 41  40  40  TYR TYR A . n 
A 1 42  ARG 42  41  41  ARG ARG A . n 
A 1 43  LYS 43  42  42  LYS LYS A . n 
A 1 44  GLN 44  43  43  GLN GLN A . n 
A 1 45  VAL 45  44  44  VAL VAL A . n 
A 1 46  VAL 46  45  45  VAL VAL A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  GLY 49  48  48  GLY GLY A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  THR 51  50  50  THR THR A . n 
A 1 52  CYS 52  51  51  CYS CYS A . n 
A 1 53  LEU 53  52  52  LEU LEU A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  ASP 55  54  54  ASP ASP A . n 
A 1 56  ILE 56  55  55  ILE ILE A . n 
A 1 57  LEU 57  56  56  LEU LEU A . n 
A 1 58  ASP 58  57  57  ASP ASP A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  ALA 60  59  59  ALA ALA A . n 
A 1 61  GLY 61  60  60  GLY GLY A . n 
A 1 62  GLN 62  61  61  GLN GLN A . n 
A 1 63  GLU 63  62  62  GLU GLU A . n 
A 1 64  GLU 64  63  63  GLU GLU A . n 
A 1 65  TYR 65  64  64  TYR TYR A . n 
A 1 66  SER 66  65  65  SER SER A . n 
A 1 67  ALA 67  66  66  ALA ALA A . n 
A 1 68  MET 68  67  67  MET MET A . n 
A 1 69  ARG 69  68  68  ARG ARG A . n 
A 1 70  ASP 70  69  69  ASP ASP A . n 
A 1 71  GLN 71  70  70  GLN GLN A . n 
A 1 72  TYR 72  71  71  TYR TYR A . n 
A 1 73  MET 73  72  72  MET MET A . n 
A 1 74  ARG 74  73  73  ARG ARG A . n 
A 1 75  THR 75  74  74  THR THR A . n 
A 1 76  GLY 76  75  75  GLY GLY A . n 
A 1 77  GLU 77  76  76  GLU GLU A . n 
A 1 78  GLY 78  77  77  GLY GLY A . n 
A 1 79  PHE 79  78  78  PHE PHE A . n 
A 1 80  LEU 80  79  79  LEU LEU A . n 
A 1 81  CYS 81  80  80  CYS CYS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  PHE 83  82  82  PHE PHE A . n 
A 1 84  ALA 84  83  83  ALA ALA A . n 
A 1 85  ILE 85  84  84  ILE ILE A . n 
A 1 86  ASN 86  85  85  ASN ASN A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  THR 88  87  87  THR THR A . n 
A 1 89  LYS 89  88  88  LYS LYS A . n 
A 1 90  SER 90  89  89  SER SER A . n 
A 1 91  PHE 91  90  90  PHE PHE A . n 
A 1 92  GLU 92  91  91  GLU GLU A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  ILE 94  93  93  ILE ILE A . n 
A 1 95  HIS 95  94  94  HIS HIS A . n 
A 1 96  HIS 96  95  95  HIS HIS A . n 
A 1 97  TYR 97  96  96  TYR TYR A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  GLU 99  98  98  GLU GLU A . n 
A 1 100 GLN 100 99  99  GLN GLN A . n 
A 1 101 ILE 101 100 100 ILE ILE A . n 
A 1 102 LYS 102 101 101 LYS LYS A . n 
A 1 103 ARG 103 102 102 ARG ARG A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 LYS 105 104 104 LYS LYS A . n 
A 1 106 ASP 106 105 105 ASP ASP A . n 
A 1 107 SER 107 106 106 SER SER A . n 
A 1 108 GLU 108 107 107 GLU GLU A . n 
A 1 109 ASP 109 108 108 ASP ASP A . n 
A 1 110 VAL 110 109 109 VAL VAL A . n 
A 1 111 PRO 111 110 110 PRO PRO A . n 
A 1 112 MET 112 111 111 MET MET A . n 
A 1 113 VAL 113 112 112 VAL VAL A . n 
A 1 114 LEU 114 113 113 LEU LEU A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 GLY 116 115 115 GLY GLY A . n 
A 1 117 ASN 117 116 116 ASN ASN A . n 
A 1 118 LYS 118 117 117 LYS LYS A . n 
A 1 119 CYS 119 118 118 CYS CYS A . n 
A 1 120 ASP 120 119 119 ASP ASP A . n 
A 1 121 LEU 121 120 120 LEU LEU A . n 
A 1 122 PRO 122 121 121 PRO PRO A . n 
A 1 123 SER 123 122 122 SER SER A . n 
A 1 124 ARG 124 123 123 ARG ARG A . n 
A 1 125 THR 125 124 124 THR THR A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 ASP 127 126 126 ASP ASP A . n 
A 1 128 THR 128 127 127 THR THR A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLN 130 129 129 GLN GLN A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 GLN 132 131 131 GLN GLN A . n 
A 1 133 ASP 133 132 132 ASP ASP A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 ARG 136 135 135 ARG ARG A . n 
A 1 137 SER 137 136 136 SER SER A . n 
A 1 138 TYR 138 137 137 TYR TYR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ILE 140 139 139 ILE ILE A . n 
A 1 141 PRO 141 140 140 PRO PRO A . n 
A 1 142 PHE 142 141 141 PHE PHE A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 GLU 144 143 143 GLU GLU A . n 
A 1 145 THR 145 144 144 THR THR A . n 
A 1 146 SER 146 145 145 SER SER A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 THR 149 148 148 THR THR A . n 
A 1 150 ARG 150 149 149 ARG ARG A . n 
A 1 151 GLN 151 150 150 GLN GLN A . n 
A 1 152 GLY 152 151 151 GLY GLY A . n 
A 1 153 VAL 153 152 152 VAL VAL A . n 
A 1 154 ASP 154 153 153 ASP ASP A . n 
A 1 155 ASP 155 154 154 ASP ASP A . n 
A 1 156 ALA 156 155 155 ALA ALA A . n 
A 1 157 PHE 157 156 156 PHE PHE A . n 
A 1 158 TYR 158 157 157 TYR TYR A . n 
A 1 159 THR 159 158 158 THR THR A . n 
A 1 160 LEU 160 159 159 LEU LEU A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 ARG 162 161 161 ARG ARG A . n 
A 1 163 GLU 163 162 162 GLU GLU A . n 
A 1 164 ILE 164 163 163 ILE ILE A . n 
A 1 165 ARG 165 164 164 ARG ARG A . n 
A 1 166 LYS 166 165 165 LYS LYS A . n 
A 1 167 HIS 167 166 166 HIS HIS A . n 
A 1 168 LYS 168 167 167 LYS LYS A . n 
A 1 169 GLU 169 168 168 GLU GLU A . n 
A 1 170 LYS 170 169 169 LYS LYS A . n 
B 2 1   GLY 1   0   ?   ?   ?   B . n 
B 2 2   MET 2   1   ?   ?   ?   B . n 
B 2 3   VAL 3   2   2   VAL VAL B . n 
B 2 4   ASN 4   3   3   ASN ASN B . n 
B 2 5   PRO 5   4   4   PRO PRO B . n 
B 2 6   THR 6   5   5   THR THR B . n 
B 2 7   VAL 7   6   6   VAL VAL B . n 
B 2 8   PHE 8   7   7   PHE PHE B . n 
B 2 9   PHE 9   8   8   PHE PHE B . n 
B 2 10  ASP 10  9   9   ASP ASP B . n 
B 2 11  ILE 11  10  10  ILE ILE B . n 
B 2 12  ALA 12  11  11  ALA ALA B . n 
B 2 13  VAL 13  12  12  VAL VAL B . n 
B 2 14  ASP 14  13  13  ASP ASP B . n 
B 2 15  GLY 15  14  14  GLY GLY B . n 
B 2 16  GLU 16  15  15  GLU GLU B . n 
B 2 17  PRO 17  16  16  PRO PRO B . n 
B 2 18  LEU 18  17  17  LEU LEU B . n 
B 2 19  GLY 19  18  18  GLY GLY B . n 
B 2 20  ARG 20  19  19  ARG ARG B . n 
B 2 21  VAL 21  20  20  VAL VAL B . n 
B 2 22  SER 22  21  21  SER SER B . n 
B 2 23  PHE 23  22  22  PHE PHE B . n 
B 2 24  GLU 24  23  23  GLU GLU B . n 
B 2 25  LEU 25  24  24  LEU LEU B . n 
B 2 26  PHE 26  25  25  PHE PHE B . n 
B 2 27  ALA 27  26  26  ALA ALA B . n 
B 2 28  ASP 28  27  27  ASP ASP B . n 
B 2 29  LYS 29  28  28  LYS LYS B . n 
B 2 30  VAL 30  29  29  VAL VAL B . n 
B 2 31  PRO 31  30  30  PRO PRO B . n 
B 2 32  LYS 32  31  31  LYS LYS B . n 
B 2 33  THR 33  32  32  THR THR B . n 
B 2 34  ALA 34  33  33  ALA ALA B . n 
B 2 35  GLU 35  34  34  GLU GLU B . n 
B 2 36  ASN 36  35  35  ASN ASN B . n 
B 2 37  PHE 37  36  36  PHE PHE B . n 
B 2 38  ARG 38  37  37  ARG ARG B . n 
B 2 39  ALA 39  38  38  ALA ALA B . n 
B 2 40  LEU 40  39  39  LEU LEU B . n 
B 2 41  SER 41  40  40  SER SER B . n 
B 2 42  THR 42  41  41  THR THR B . n 
B 2 43  GLY 43  42  42  GLY GLY B . n 
B 2 44  GLU 44  43  43  GLU GLU B . n 
B 2 45  LYS 45  44  44  LYS LYS B . n 
B 2 46  GLY 46  45  45  GLY GLY B . n 
B 2 47  PHE 47  46  46  PHE PHE B . n 
B 2 48  GLY 48  47  47  GLY GLY B . n 
B 2 49  TYR 49  48  48  TYR TYR B . n 
B 2 50  LYS 50  49  49  LYS LYS B . n 
B 2 51  GLY 51  50  50  GLY GLY B . n 
B 2 52  SER 52  51  51  SER SER B . n 
B 2 53  CYS 53  52  52  CYS CYS B . n 
B 2 54  PHE 54  53  53  PHE PHE B . n 
B 2 55  HIS 55  54  54  HIS HIS B . n 
B 2 56  ARG 56  55  55  ARG ARG B . n 
B 2 57  ILE 57  56  56  ILE ILE B . n 
B 2 58  ILE 58  57  57  ILE ILE B . n 
B 2 59  PRO 59  58  58  PRO PRO B . n 
B 2 60  GLY 60  59  59  GLY GLY B . n 
B 2 61  PHE 61  60  60  PHE PHE B . n 
B 2 62  MET 62  61  61  MET MET B . n 
B 2 63  CYS 63  62  62  CYS CYS B . n 
B 2 64  GLN 64  63  63  GLN GLN B . n 
B 2 65  GLY 65  64  64  GLY GLY B . n 
B 2 66  GLY 66  65  65  GLY GLY B . n 
B 2 67  ASP 67  66  66  ASP ASP B . n 
B 2 68  PHE 68  67  67  PHE PHE B . n 
B 2 69  THR 69  68  68  THR THR B . n 
B 2 70  ARG 70  69  69  ARG ARG B . n 
B 2 71  HIS 71  70  70  HIS HIS B . n 
B 2 72  ASN 72  71  71  ASN ASN B . n 
B 2 73  GLY 73  72  72  GLY GLY B . n 
B 2 74  THR 74  73  73  THR THR B . n 
B 2 75  GLY 75  74  74  GLY GLY B . n 
B 2 76  GLY 76  75  75  GLY GLY B . n 
B 2 77  LYS 77  76  76  LYS LYS B . n 
B 2 78  SER 78  77  77  SER SER B . n 
B 2 79  ILE 79  78  78  ILE ILE B . n 
B 2 80  TYR 80  79  79  TYR TYR B . n 
B 2 81  GLY 81  80  80  GLY GLY B . n 
B 2 82  GLU 82  81  81  GLU GLU B . n 
B 2 83  LYS 83  82  82  LYS LYS B . n 
B 2 84  PHE 84  83  83  PHE PHE B . n 
B 2 85  GLU 85  84  84  GLU GLU B . n 
B 2 86  ASP 86  85  85  ASP ASP B . n 
B 2 87  GLU 87  86  86  GLU GLU B . n 
B 2 88  ASN 88  87  87  ASN ASN B . n 
B 2 89  PHE 89  88  88  PHE PHE B . n 
B 2 90  ILE 90  89  89  ILE ILE B . n 
B 2 91  LEU 91  90  90  LEU LEU B . n 
B 2 92  LYS 92  91  91  LYS LYS B . n 
B 2 93  HIS 93  92  92  HIS HIS B . n 
B 2 94  THR 94  93  93  THR THR B . n 
B 2 95  GLY 95  94  94  GLY GLY B . n 
B 2 96  PRO 96  95  95  PRO PRO B . n 
B 2 97  GLY 97  96  96  GLY GLY B . n 
B 2 98  ILE 98  97  97  ILE ILE B . n 
B 2 99  LEU 99  98  98  LEU LEU B . n 
B 2 100 SER 100 99  99  SER SER B . n 
B 2 101 MET 101 100 100 MET MET B . n 
B 2 102 ALA 102 101 101 ALA ALA B . n 
B 2 103 ASN 103 102 102 ASN ASN B . n 
B 2 104 ALA 104 103 103 ALA ALA B . n 
B 2 105 GLY 105 104 104 GLY GLY B . n 
B 2 106 PRO 106 105 105 PRO PRO B . n 
B 2 107 ASN 107 106 106 ASN ASN B . n 
B 2 108 THR 108 107 107 THR THR B . n 
B 2 109 ASN 109 108 108 ASN ASN B . n 
B 2 110 GLY 110 109 109 GLY GLY B . n 
B 2 111 SER 111 110 110 SER SER B . n 
B 2 112 GLN 112 111 111 GLN GLN B . n 
B 2 113 PHE 113 112 112 PHE PHE B . n 
B 2 114 PHE 114 113 113 PHE PHE B . n 
B 2 115 ILE 115 114 114 ILE ILE B . n 
B 2 116 CYS 116 115 115 CYS CYS B . n 
B 2 117 THR 117 116 116 THR THR B . n 
B 2 118 ALA 118 117 117 ALA ALA B . n 
B 2 119 LYS 119 118 118 LYS LYS B . n 
B 2 120 THR 120 119 119 THR THR B . n 
B 2 121 GLU 121 120 120 GLU GLU B . n 
B 2 122 TRP 122 121 121 TRP TRP B . n 
B 2 123 LEU 123 122 122 LEU LEU B . n 
B 2 124 ASP 124 123 123 ASP ASP B . n 
B 2 125 GLY 125 124 124 GLY GLY B . n 
B 2 126 LYS 126 125 125 LYS LYS B . n 
B 2 127 HIS 127 126 126 HIS HIS B . n 
B 2 128 VAL 128 127 127 VAL VAL B . n 
B 2 129 VAL 129 128 128 VAL VAL B . n 
B 2 130 PHE 130 129 129 PHE PHE B . n 
B 2 131 GLY 131 130 130 GLY GLY B . n 
B 2 132 LYS 132 131 131 LYS LYS B . n 
B 2 133 VAL 133 132 132 VAL VAL B . n 
B 2 134 LYS 134 133 133 LYS LYS B . n 
B 2 135 GLU 135 134 134 GLU GLU B . n 
B 2 136 GLY 136 135 135 GLY GLY B . n 
B 2 137 MET 137 136 136 MET MET B . n 
B 2 138 ASN 138 137 137 ASN ASN B . n 
B 2 139 ILE 139 138 138 ILE ILE B . n 
B 2 140 VAL 140 139 139 VAL VAL B . n 
B 2 141 GLU 141 140 140 GLU GLU B . n 
B 2 142 ALA 142 141 141 ALA ALA B . n 
B 2 143 MET 143 142 142 MET MET B . n 
B 2 144 GLU 144 143 143 GLU GLU B . n 
B 2 145 ARG 145 144 144 ARG ARG B . n 
B 2 146 PHE 146 145 145 PHE PHE B . n 
B 2 147 GLY 147 146 146 GLY GLY B . n 
B 2 148 SER 148 147 147 SER SER B . n 
B 2 149 ARG 149 148 148 ARG ARG B . n 
B 2 150 ASN 150 149 149 ASN ASN B . n 
B 2 151 GLY 151 150 150 GLY GLY B . n 
B 2 152 LYS 152 151 151 LYS LYS B . n 
B 2 153 THR 153 152 152 THR THR B . n 
B 2 154 SER 154 153 153 SER SER B . n 
B 2 155 LYS 155 154 154 LYS LYS B . n 
B 2 156 LYS 156 155 155 LYS LYS B . n 
B 2 157 ILE 157 156 156 ILE ILE B . n 
B 2 158 THR 158 157 157 THR THR B . n 
B 2 159 ILE 159 158 158 ILE ILE B . n 
B 2 160 ALA 160 159 159 ALA ALA B . n 
B 2 161 ASP 161 160 160 ASP ASP B . n 
B 2 162 CYS 162 161 161 CYS CYS B . n 
B 2 163 GLY 163 162 162 GLY GLY B . n 
B 2 164 GLN 164 163 163 GLN GLN B . n 
B 2 165 LEU 165 164 164 LEU LEU B . n 
B 2 166 GLU 166 165 ?   ?   ?   B . n 
C 2 1   GLY 1   0   ?   ?   ?   D . n 
C 2 2   MET 2   1   ?   ?   ?   D . n 
C 2 3   VAL 3   2   2   VAL VAL D . n 
C 2 4   ASN 4   3   3   ASN ASN D . n 
C 2 5   PRO 5   4   4   PRO PRO D . n 
C 2 6   THR 6   5   5   THR THR D . n 
C 2 7   VAL 7   6   6   VAL VAL D . n 
C 2 8   PHE 8   7   7   PHE PHE D . n 
C 2 9   PHE 9   8   8   PHE PHE D . n 
C 2 10  ASP 10  9   9   ASP ASP D . n 
C 2 11  ILE 11  10  10  ILE ILE D . n 
C 2 12  ALA 12  11  11  ALA ALA D . n 
C 2 13  VAL 13  12  12  VAL VAL D . n 
C 2 14  ASP 14  13  13  ASP ASP D . n 
C 2 15  GLY 15  14  14  GLY GLY D . n 
C 2 16  GLU 16  15  15  GLU GLU D . n 
C 2 17  PRO 17  16  16  PRO PRO D . n 
C 2 18  LEU 18  17  17  LEU LEU D . n 
C 2 19  GLY 19  18  18  GLY GLY D . n 
C 2 20  ARG 20  19  19  ARG ARG D . n 
C 2 21  VAL 21  20  20  VAL VAL D . n 
C 2 22  SER 22  21  21  SER SER D . n 
C 2 23  PHE 23  22  22  PHE PHE D . n 
C 2 24  GLU 24  23  23  GLU GLU D . n 
C 2 25  LEU 25  24  24  LEU LEU D . n 
C 2 26  PHE 26  25  25  PHE PHE D . n 
C 2 27  ALA 27  26  26  ALA ALA D . n 
C 2 28  ASP 28  27  27  ASP ASP D . n 
C 2 29  LYS 29  28  28  LYS LYS D . n 
C 2 30  VAL 30  29  29  VAL VAL D . n 
C 2 31  PRO 31  30  30  PRO PRO D . n 
C 2 32  LYS 32  31  31  LYS LYS D . n 
C 2 33  THR 33  32  32  THR THR D . n 
C 2 34  ALA 34  33  33  ALA ALA D . n 
C 2 35  GLU 35  34  34  GLU GLU D . n 
C 2 36  ASN 36  35  35  ASN ASN D . n 
C 2 37  PHE 37  36  36  PHE PHE D . n 
C 2 38  ARG 38  37  37  ARG ARG D . n 
C 2 39  ALA 39  38  38  ALA ALA D . n 
C 2 40  LEU 40  39  39  LEU LEU D . n 
C 2 41  SER 41  40  40  SER SER D . n 
C 2 42  THR 42  41  41  THR THR D . n 
C 2 43  GLY 43  42  42  GLY GLY D . n 
C 2 44  GLU 44  43  43  GLU GLU D . n 
C 2 45  LYS 45  44  44  LYS LYS D . n 
C 2 46  GLY 46  45  45  GLY GLY D . n 
C 2 47  PHE 47  46  46  PHE PHE D . n 
C 2 48  GLY 48  47  47  GLY GLY D . n 
C 2 49  TYR 49  48  48  TYR TYR D . n 
C 2 50  LYS 50  49  49  LYS LYS D . n 
C 2 51  GLY 51  50  50  GLY GLY D . n 
C 2 52  SER 52  51  51  SER SER D . n 
C 2 53  CYS 53  52  52  CYS CYS D . n 
C 2 54  PHE 54  53  53  PHE PHE D . n 
C 2 55  HIS 55  54  54  HIS HIS D . n 
C 2 56  ARG 56  55  55  ARG ARG D . n 
C 2 57  ILE 57  56  56  ILE ILE D . n 
C 2 58  ILE 58  57  57  ILE ILE D . n 
C 2 59  PRO 59  58  58  PRO PRO D . n 
C 2 60  GLY 60  59  59  GLY GLY D . n 
C 2 61  PHE 61  60  60  PHE PHE D . n 
C 2 62  MET 62  61  61  MET MET D . n 
C 2 63  CYS 63  62  62  CYS CYS D . n 
C 2 64  GLN 64  63  63  GLN GLN D . n 
C 2 65  GLY 65  64  64  GLY GLY D . n 
C 2 66  GLY 66  65  65  GLY GLY D . n 
C 2 67  ASP 67  66  66  ASP ASP D . n 
C 2 68  PHE 68  67  67  PHE PHE D . n 
C 2 69  THR 69  68  68  THR THR D . n 
C 2 70  ARG 70  69  69  ARG ARG D . n 
C 2 71  HIS 71  70  70  HIS HIS D . n 
C 2 72  ASN 72  71  71  ASN ASN D . n 
C 2 73  GLY 73  72  72  GLY GLY D . n 
C 2 74  THR 74  73  73  THR THR D . n 
C 2 75  GLY 75  74  74  GLY GLY D . n 
C 2 76  GLY 76  75  75  GLY GLY D . n 
C 2 77  LYS 77  76  76  LYS LYS D . n 
C 2 78  SER 78  77  77  SER SER D . n 
C 2 79  ILE 79  78  78  ILE ILE D . n 
C 2 80  TYR 80  79  79  TYR TYR D . n 
C 2 81  GLY 81  80  80  GLY GLY D . n 
C 2 82  GLU 82  81  81  GLU GLU D . n 
C 2 83  LYS 83  82  82  LYS LYS D . n 
C 2 84  PHE 84  83  83  PHE PHE D . n 
C 2 85  GLU 85  84  84  GLU GLU D . n 
C 2 86  ASP 86  85  85  ASP ASP D . n 
C 2 87  GLU 87  86  86  GLU GLU D . n 
C 2 88  ASN 88  87  87  ASN ASN D . n 
C 2 89  PHE 89  88  88  PHE PHE D . n 
C 2 90  ILE 90  89  89  ILE ILE D . n 
C 2 91  LEU 91  90  90  LEU LEU D . n 
C 2 92  LYS 92  91  91  LYS LYS D . n 
C 2 93  HIS 93  92  92  HIS HIS D . n 
C 2 94  THR 94  93  93  THR THR D . n 
C 2 95  GLY 95  94  94  GLY GLY D . n 
C 2 96  PRO 96  95  95  PRO PRO D . n 
C 2 97  GLY 97  96  96  GLY GLY D . n 
C 2 98  ILE 98  97  97  ILE ILE D . n 
C 2 99  LEU 99  98  98  LEU LEU D . n 
C 2 100 SER 100 99  99  SER SER D . n 
C 2 101 MET 101 100 100 MET MET D . n 
C 2 102 ALA 102 101 101 ALA ALA D . n 
C 2 103 ASN 103 102 102 ASN ASN D . n 
C 2 104 ALA 104 103 103 ALA ALA D . n 
C 2 105 GLY 105 104 104 GLY GLY D . n 
C 2 106 PRO 106 105 105 PRO PRO D . n 
C 2 107 ASN 107 106 106 ASN ASN D . n 
C 2 108 THR 108 107 107 THR THR D . n 
C 2 109 ASN 109 108 108 ASN ASN D . n 
C 2 110 GLY 110 109 109 GLY GLY D . n 
C 2 111 SER 111 110 110 SER SER D . n 
C 2 112 GLN 112 111 111 GLN GLN D . n 
C 2 113 PHE 113 112 112 PHE PHE D . n 
C 2 114 PHE 114 113 113 PHE PHE D . n 
C 2 115 ILE 115 114 114 ILE ILE D . n 
C 2 116 CYS 116 115 115 CYS CYS D . n 
C 2 117 THR 117 116 116 THR THR D . n 
C 2 118 ALA 118 117 117 ALA ALA D . n 
C 2 119 LYS 119 118 118 LYS LYS D . n 
C 2 120 THR 120 119 119 THR THR D . n 
C 2 121 GLU 121 120 120 GLU GLU D . n 
C 2 122 TRP 122 121 121 TRP TRP D . n 
C 2 123 LEU 123 122 122 LEU LEU D . n 
C 2 124 ASP 124 123 123 ASP ASP D . n 
C 2 125 GLY 125 124 124 GLY GLY D . n 
C 2 126 LYS 126 125 125 LYS LYS D . n 
C 2 127 HIS 127 126 126 HIS HIS D . n 
C 2 128 VAL 128 127 127 VAL VAL D . n 
C 2 129 VAL 129 128 128 VAL VAL D . n 
C 2 130 PHE 130 129 129 PHE PHE D . n 
C 2 131 GLY 131 130 130 GLY GLY D . n 
C 2 132 LYS 132 131 131 LYS LYS D . n 
C 2 133 VAL 133 132 132 VAL VAL D . n 
C 2 134 LYS 134 133 133 LYS LYS D . n 
C 2 135 GLU 135 134 134 GLU GLU D . n 
C 2 136 GLY 136 135 135 GLY GLY D . n 
C 2 137 MET 137 136 136 MET MET D . n 
C 2 138 ASN 138 137 137 ASN ASN D . n 
C 2 139 ILE 139 138 138 ILE ILE D . n 
C 2 140 VAL 140 139 139 VAL VAL D . n 
C 2 141 GLU 141 140 140 GLU GLU D . n 
C 2 142 ALA 142 141 141 ALA ALA D . n 
C 2 143 MET 143 142 142 MET MET D . n 
C 2 144 GLU 144 143 143 GLU GLU D . n 
C 2 145 ARG 145 144 144 ARG ARG D . n 
C 2 146 PHE 146 145 145 PHE PHE D . n 
C 2 147 GLY 147 146 146 GLY GLY D . n 
C 2 148 SER 148 147 147 SER SER D . n 
C 2 149 ARG 149 148 148 ARG ARG D . n 
C 2 150 ASN 150 149 149 ASN ASN D . n 
C 2 151 GLY 151 150 150 GLY GLY D . n 
C 2 152 LYS 152 151 151 LYS LYS D . n 
C 2 153 THR 153 152 152 THR THR D . n 
C 2 154 SER 154 153 153 SER SER D . n 
C 2 155 LYS 155 154 154 LYS LYS D . n 
C 2 156 LYS 156 155 155 LYS LYS D . n 
C 2 157 ILE 157 156 156 ILE ILE D . n 
C 2 158 THR 158 157 157 THR THR D . n 
C 2 159 ILE 159 158 158 ILE ILE D . n 
C 2 160 ALA 160 159 159 ALA ALA D . n 
C 2 161 ASP 161 160 160 ASP ASP D . n 
C 2 162 CYS 162 161 161 CYS CYS D . n 
C 2 163 GLY 163 162 162 GLY GLY D . n 
C 2 164 GLN 164 163 163 GLN GLN D . n 
C 2 165 LEU 165 164 164 LEU LEU D . n 
C 2 166 GLU 166 165 ?   ?   ?   D . n 
D 1 1   GLY 1   0   0   GLY GLY C . n 
D 1 2   MET 2   1   1   MET MET C . n 
D 1 3   THR 3   2   2   THR THR C . n 
D 1 4   GLU 4   3   3   GLU GLU C . n 
D 1 5   TYR 5   4   4   TYR TYR C . n 
D 1 6   LYS 6   5   5   LYS LYS C . n 
D 1 7   LEU 7   6   6   LEU LEU C . n 
D 1 8   VAL 8   7   7   VAL VAL C . n 
D 1 9   VAL 9   8   8   VAL VAL C . n 
D 1 10  VAL 10  9   9   VAL VAL C . n 
D 1 11  GLY 11  10  10  GLY GLY C . n 
D 1 12  ALA 12  11  11  ALA ALA C . n 
D 1 13  ASP 13  12  12  ASP ASP C . n 
D 1 14  GLY 14  13  13  GLY GLY C . n 
D 1 15  VAL 15  14  14  VAL VAL C . n 
D 1 16  GLY 16  15  15  GLY GLY C . n 
D 1 17  LYS 17  16  16  LYS LYS C . n 
D 1 18  SER 18  17  17  SER SER C . n 
D 1 19  ALA 19  18  18  ALA ALA C . n 
D 1 20  LEU 20  19  19  LEU LEU C . n 
D 1 21  THR 21  20  20  THR THR C . n 
D 1 22  ILE 22  21  21  ILE ILE C . n 
D 1 23  GLN 23  22  22  GLN GLN C . n 
D 1 24  LEU 24  23  23  LEU LEU C . n 
D 1 25  ILE 25  24  24  ILE ILE C . n 
D 1 26  GLN 26  25  25  GLN GLN C . n 
D 1 27  ASN 27  26  26  ASN ASN C . n 
D 1 28  HIS 28  27  27  HIS HIS C . n 
D 1 29  PHE 29  28  28  PHE PHE C . n 
D 1 30  VAL 30  29  29  VAL VAL C . n 
D 1 31  ASP 31  30  30  ASP ASP C . n 
D 1 32  GLU 32  31  31  GLU GLU C . n 
D 1 33  TYR 33  32  32  TYR TYR C . n 
D 1 34  ASP 34  33  33  ASP ASP C . n 
D 1 35  PRO 35  34  34  PRO PRO C . n 
D 1 36  THR 36  35  35  THR THR C . n 
D 1 37  ILE 37  36  36  ILE ILE C . n 
D 1 38  GLU 38  37  37  GLU GLU C . n 
D 1 39  ASP 39  38  38  ASP ASP C . n 
D 1 40  SER 40  39  39  SER SER C . n 
D 1 41  TYR 41  40  40  TYR TYR C . n 
D 1 42  ARG 42  41  41  ARG ARG C . n 
D 1 43  LYS 43  42  42  LYS LYS C . n 
D 1 44  GLN 44  43  43  GLN GLN C . n 
D 1 45  VAL 45  44  44  VAL VAL C . n 
D 1 46  VAL 46  45  45  VAL VAL C . n 
D 1 47  ILE 47  46  46  ILE ILE C . n 
D 1 48  ASP 48  47  47  ASP ASP C . n 
D 1 49  GLY 49  48  48  GLY GLY C . n 
D 1 50  GLU 50  49  49  GLU GLU C . n 
D 1 51  THR 51  50  50  THR THR C . n 
D 1 52  CYS 52  51  51  CYS CYS C . n 
D 1 53  LEU 53  52  52  LEU LEU C . n 
D 1 54  LEU 54  53  53  LEU LEU C . n 
D 1 55  ASP 55  54  54  ASP ASP C . n 
D 1 56  ILE 56  55  55  ILE ILE C . n 
D 1 57  LEU 57  56  56  LEU LEU C . n 
D 1 58  ASP 58  57  57  ASP ASP C . n 
D 1 59  THR 59  58  58  THR THR C . n 
D 1 60  ALA 60  59  59  ALA ALA C . n 
D 1 61  GLY 61  60  60  GLY GLY C . n 
D 1 62  GLN 62  61  61  GLN GLN C . n 
D 1 63  GLU 63  62  62  GLU GLU C . n 
D 1 64  GLU 64  63  63  GLU GLU C . n 
D 1 65  TYR 65  64  64  TYR TYR C . n 
D 1 66  SER 66  65  65  SER SER C . n 
D 1 67  ALA 67  66  66  ALA ALA C . n 
D 1 68  MET 68  67  67  MET MET C . n 
D 1 69  ARG 69  68  68  ARG ARG C . n 
D 1 70  ASP 70  69  69  ASP ASP C . n 
D 1 71  GLN 71  70  70  GLN GLN C . n 
D 1 72  TYR 72  71  71  TYR TYR C . n 
D 1 73  MET 73  72  72  MET MET C . n 
D 1 74  ARG 74  73  73  ARG ARG C . n 
D 1 75  THR 75  74  74  THR THR C . n 
D 1 76  GLY 76  75  75  GLY GLY C . n 
D 1 77  GLU 77  76  76  GLU GLU C . n 
D 1 78  GLY 78  77  77  GLY GLY C . n 
D 1 79  PHE 79  78  78  PHE PHE C . n 
D 1 80  LEU 80  79  79  LEU LEU C . n 
D 1 81  CYS 81  80  80  CYS CYS C . n 
D 1 82  VAL 82  81  81  VAL VAL C . n 
D 1 83  PHE 83  82  82  PHE PHE C . n 
D 1 84  ALA 84  83  83  ALA ALA C . n 
D 1 85  ILE 85  84  84  ILE ILE C . n 
D 1 86  ASN 86  85  85  ASN ASN C . n 
D 1 87  ASN 87  86  86  ASN ASN C . n 
D 1 88  THR 88  87  87  THR THR C . n 
D 1 89  LYS 89  88  88  LYS LYS C . n 
D 1 90  SER 90  89  89  SER SER C . n 
D 1 91  PHE 91  90  90  PHE PHE C . n 
D 1 92  GLU 92  91  91  GLU GLU C . n 
D 1 93  ASP 93  92  92  ASP ASP C . n 
D 1 94  ILE 94  93  93  ILE ILE C . n 
D 1 95  HIS 95  94  94  HIS HIS C . n 
D 1 96  HIS 96  95  95  HIS HIS C . n 
D 1 97  TYR 97  96  96  TYR TYR C . n 
D 1 98  ARG 98  97  97  ARG ARG C . n 
D 1 99  GLU 99  98  98  GLU GLU C . n 
D 1 100 GLN 100 99  99  GLN GLN C . n 
D 1 101 ILE 101 100 100 ILE ILE C . n 
D 1 102 LYS 102 101 101 LYS LYS C . n 
D 1 103 ARG 103 102 102 ARG ARG C . n 
D 1 104 VAL 104 103 103 VAL VAL C . n 
D 1 105 LYS 105 104 104 LYS LYS C . n 
D 1 106 ASP 106 105 105 ASP ASP C . n 
D 1 107 SER 107 106 106 SER SER C . n 
D 1 108 GLU 108 107 107 GLU GLU C . n 
D 1 109 ASP 109 108 108 ASP ASP C . n 
D 1 110 VAL 110 109 109 VAL VAL C . n 
D 1 111 PRO 111 110 110 PRO PRO C . n 
D 1 112 MET 112 111 111 MET MET C . n 
D 1 113 VAL 113 112 112 VAL VAL C . n 
D 1 114 LEU 114 113 113 LEU LEU C . n 
D 1 115 VAL 115 114 114 VAL VAL C . n 
D 1 116 GLY 116 115 115 GLY GLY C . n 
D 1 117 ASN 117 116 116 ASN ASN C . n 
D 1 118 LYS 118 117 117 LYS LYS C . n 
D 1 119 CYS 119 118 118 CYS CYS C . n 
D 1 120 ASP 120 119 119 ASP ASP C . n 
D 1 121 LEU 121 120 120 LEU LEU C . n 
D 1 122 PRO 122 121 121 PRO PRO C . n 
D 1 123 SER 123 122 122 SER SER C . n 
D 1 124 ARG 124 123 123 ARG ARG C . n 
D 1 125 THR 125 124 124 THR THR C . n 
D 1 126 VAL 126 125 125 VAL VAL C . n 
D 1 127 ASP 127 126 126 ASP ASP C . n 
D 1 128 THR 128 127 127 THR THR C . n 
D 1 129 LYS 129 128 128 LYS LYS C . n 
D 1 130 GLN 130 129 129 GLN GLN C . n 
D 1 131 ALA 131 130 130 ALA ALA C . n 
D 1 132 GLN 132 131 131 GLN GLN C . n 
D 1 133 ASP 133 132 132 ASP ASP C . n 
D 1 134 LEU 134 133 133 LEU LEU C . n 
D 1 135 ALA 135 134 134 ALA ALA C . n 
D 1 136 ARG 136 135 135 ARG ARG C . n 
D 1 137 SER 137 136 136 SER SER C . n 
D 1 138 TYR 138 137 137 TYR TYR C . n 
D 1 139 GLY 139 138 138 GLY GLY C . n 
D 1 140 ILE 140 139 139 ILE ILE C . n 
D 1 141 PRO 141 140 140 PRO PRO C . n 
D 1 142 PHE 142 141 141 PHE PHE C . n 
D 1 143 ILE 143 142 142 ILE ILE C . n 
D 1 144 GLU 144 143 143 GLU GLU C . n 
D 1 145 THR 145 144 144 THR THR C . n 
D 1 146 SER 146 145 145 SER SER C . n 
D 1 147 ALA 147 146 146 ALA ALA C . n 
D 1 148 LYS 148 147 147 LYS LYS C . n 
D 1 149 THR 149 148 148 THR THR C . n 
D 1 150 ARG 150 149 149 ARG ARG C . n 
D 1 151 GLN 151 150 150 GLN GLN C . n 
D 1 152 GLY 152 151 151 GLY GLY C . n 
D 1 153 VAL 153 152 152 VAL VAL C . n 
D 1 154 ASP 154 153 153 ASP ASP C . n 
D 1 155 ASP 155 154 154 ASP ASP C . n 
D 1 156 ALA 156 155 155 ALA ALA C . n 
D 1 157 PHE 157 156 156 PHE PHE C . n 
D 1 158 TYR 158 157 157 TYR TYR C . n 
D 1 159 THR 159 158 158 THR THR C . n 
D 1 160 LEU 160 159 159 LEU LEU C . n 
D 1 161 VAL 161 160 160 VAL VAL C . n 
D 1 162 ARG 162 161 161 ARG ARG C . n 
D 1 163 GLU 163 162 162 GLU GLU C . n 
D 1 164 ILE 164 163 163 ILE ILE C . n 
D 1 165 ARG 165 164 164 ARG ARG C . n 
D 1 166 LYS 166 165 165 LYS LYS C . n 
D 1 167 HIS 167 166 166 HIS HIS C . n 
D 1 168 LYS 168 167 167 LYS LYS C . n 
D 1 169 GLU 169 168 ?   ?   ?   C . n 
D 1 170 LYS 170 169 ?   ?   ?   C . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ZNI ? ? ZNI ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GNP ? ? GNP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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   202 202 MG  MG  A . 
G 5 ZNI 1   201 201 ZNI ZNI B . 
H 5 ZNI 1   201 201 ZNI ZNI D . 
I 3 GNP 1   201 201 GNP GNP C . 
J 4 MG  1   202 202 MG  MG  C . 
K 6 HOH 1   301 682 HOH HOH A . 
K 6 HOH 2   302 330 HOH HOH A . 
K 6 HOH 3   303 389 HOH HOH A . 
K 6 HOH 4   304 53  HOH HOH A . 
K 6 HOH 5   305 634 HOH HOH A . 
K 6 HOH 6   306 727 HOH HOH A . 
K 6 HOH 7   307 547 HOH HOH A . 
K 6 HOH 8   308 207 HOH HOH A . 
K 6 HOH 9   309 380 HOH HOH A . 
K 6 HOH 10  310 684 HOH HOH A . 
K 6 HOH 11  311 114 HOH HOH A . 
K 6 HOH 12  312 728 HOH HOH A . 
K 6 HOH 13  313 45  HOH HOH A . 
K 6 HOH 14  314 670 HOH HOH A . 
K 6 HOH 15  315 725 HOH HOH A . 
K 6 HOH 16  316 247 HOH HOH A . 
K 6 HOH 17  317 391 HOH HOH A . 
K 6 HOH 18  318 406 HOH HOH A . 
K 6 HOH 19  319 474 HOH HOH A . 
K 6 HOH 20  320 437 HOH HOH A . 
K 6 HOH 21  321 412 HOH HOH A . 
K 6 HOH 22  322 103 HOH HOH A . 
K 6 HOH 23  323 13  HOH HOH A . 
K 6 HOH 24  324 408 HOH HOH A . 
K 6 HOH 25  325 656 HOH HOH A . 
K 6 HOH 26  326 80  HOH HOH A . 
K 6 HOH 27  327 120 HOH HOH A . 
K 6 HOH 28  328 314 HOH HOH A . 
K 6 HOH 29  329 267 HOH HOH A . 
K 6 HOH 30  330 705 HOH HOH A . 
K 6 HOH 31  331 63  HOH HOH A . 
K 6 HOH 32  332 318 HOH HOH A . 
K 6 HOH 33  333 2   HOH HOH A . 
K 6 HOH 34  334 197 HOH HOH A . 
K 6 HOH 35  335 590 HOH HOH A . 
K 6 HOH 36  336 20  HOH HOH A . 
K 6 HOH 37  337 25  HOH HOH A . 
K 6 HOH 38  338 335 HOH HOH A . 
K 6 HOH 39  339 560 HOH HOH A . 
K 6 HOH 40  340 190 HOH HOH A . 
K 6 HOH 41  341 210 HOH HOH A . 
K 6 HOH 42  342 195 HOH HOH A . 
K 6 HOH 43  343 688 HOH HOH A . 
K 6 HOH 44  344 115 HOH HOH A . 
K 6 HOH 45  345 58  HOH HOH A . 
K 6 HOH 46  346 385 HOH HOH A . 
K 6 HOH 47  347 40  HOH HOH A . 
K 6 HOH 48  348 397 HOH HOH A . 
K 6 HOH 49  349 336 HOH HOH A . 
K 6 HOH 50  350 666 HOH HOH A . 
K 6 HOH 51  351 603 HOH HOH A . 
K 6 HOH 52  352 10  HOH HOH A . 
K 6 HOH 53  353 373 HOH HOH A . 
K 6 HOH 54  354 93  HOH HOH A . 
K 6 HOH 55  355 582 HOH HOH A . 
K 6 HOH 56  356 627 HOH HOH A . 
K 6 HOH 57  357 152 HOH HOH A . 
K 6 HOH 58  358 44  HOH HOH A . 
K 6 HOH 59  359 256 HOH HOH A . 
K 6 HOH 60  360 51  HOH HOH A . 
K 6 HOH 61  361 83  HOH HOH A . 
K 6 HOH 62  362 209 HOH HOH A . 
K 6 HOH 63  363 311 HOH HOH A . 
K 6 HOH 64  364 346 HOH HOH A . 
K 6 HOH 65  365 321 HOH HOH A . 
K 6 HOH 66  366 180 HOH HOH A . 
K 6 HOH 67  367 289 HOH HOH A . 
K 6 HOH 68  368 410 HOH HOH A . 
K 6 HOH 69  369 201 HOH HOH A . 
K 6 HOH 70  370 113 HOH HOH A . 
K 6 HOH 71  371 147 HOH HOH A . 
K 6 HOH 72  372 540 HOH HOH A . 
K 6 HOH 73  373 444 HOH HOH A . 
K 6 HOH 74  374 300 HOH HOH A . 
K 6 HOH 75  375 251 HOH HOH A . 
K 6 HOH 76  376 36  HOH HOH A . 
K 6 HOH 77  377 68  HOH HOH A . 
K 6 HOH 78  378 12  HOH HOH A . 
K 6 HOH 79  379 485 HOH HOH A . 
K 6 HOH 80  380 169 HOH HOH A . 
K 6 HOH 81  381 48  HOH HOH A . 
K 6 HOH 82  382 189 HOH HOH A . 
K 6 HOH 83  383 62  HOH HOH A . 
K 6 HOH 84  384 281 HOH HOH A . 
K 6 HOH 85  385 439 HOH HOH A . 
K 6 HOH 86  386 213 HOH HOH A . 
K 6 HOH 87  387 162 HOH HOH A . 
K 6 HOH 88  388 178 HOH HOH A . 
K 6 HOH 89  389 660 HOH HOH A . 
K 6 HOH 90  390 299 HOH HOH A . 
K 6 HOH 91  391 357 HOH HOH A . 
K 6 HOH 92  392 170 HOH HOH A . 
K 6 HOH 93  393 402 HOH HOH A . 
K 6 HOH 94  394 639 HOH HOH A . 
K 6 HOH 95  395 109 HOH HOH A . 
K 6 HOH 96  396 524 HOH HOH A . 
K 6 HOH 97  397 572 HOH HOH A . 
K 6 HOH 98  398 579 HOH HOH A . 
K 6 HOH 99  399 200 HOH HOH A . 
K 6 HOH 100 400 54  HOH HOH A . 
K 6 HOH 101 401 632 HOH HOH A . 
K 6 HOH 102 402 613 HOH HOH A . 
K 6 HOH 103 403 693 HOH HOH A . 
K 6 HOH 104 404 387 HOH HOH A . 
K 6 HOH 105 405 386 HOH HOH A . 
K 6 HOH 106 406 216 HOH HOH A . 
K 6 HOH 107 407 553 HOH HOH A . 
K 6 HOH 108 408 719 HOH HOH A . 
K 6 HOH 109 409 208 HOH HOH A . 
K 6 HOH 110 410 327 HOH HOH A . 
K 6 HOH 111 411 185 HOH HOH A . 
K 6 HOH 112 412 228 HOH HOH A . 
K 6 HOH 113 413 270 HOH HOH A . 
K 6 HOH 114 414 464 HOH HOH A . 
K 6 HOH 115 415 729 HOH HOH A . 
K 6 HOH 116 416 533 HOH HOH A . 
K 6 HOH 117 417 599 HOH HOH A . 
K 6 HOH 118 418 481 HOH HOH A . 
K 6 HOH 119 419 726 HOH HOH A . 
K 6 HOH 120 420 571 HOH HOH A . 
K 6 HOH 121 421 204 HOH HOH A . 
K 6 HOH 122 422 648 HOH HOH A . 
K 6 HOH 123 423 455 HOH HOH A . 
K 6 HOH 124 424 567 HOH HOH A . 
K 6 HOH 125 425 687 HOH HOH A . 
K 6 HOH 126 426 640 HOH HOH A . 
K 6 HOH 127 427 548 HOH HOH A . 
K 6 HOH 128 428 569 HOH HOH A . 
K 6 HOH 129 429 352 HOH HOH A . 
K 6 HOH 130 430 661 HOH HOH A . 
K 6 HOH 131 431 624 HOH HOH A . 
K 6 HOH 132 432 516 HOH HOH A . 
K 6 HOH 133 433 550 HOH HOH A . 
K 6 HOH 134 434 646 HOH HOH A . 
K 6 HOH 135 435 414 HOH HOH A . 
K 6 HOH 136 436 473 HOH HOH A . 
K 6 HOH 137 437 296 HOH HOH A . 
K 6 HOH 138 438 328 HOH HOH A . 
K 6 HOH 139 439 112 HOH HOH A . 
K 6 HOH 140 440 146 HOH HOH A . 
K 6 HOH 141 441 243 HOH HOH A . 
K 6 HOH 142 442 675 HOH HOH A . 
K 6 HOH 143 443 370 HOH HOH A . 
K 6 HOH 144 444 400 HOH HOH A . 
K 6 HOH 145 445 159 HOH HOH A . 
K 6 HOH 146 446 723 HOH HOH A . 
K 6 HOH 147 447 664 HOH HOH A . 
K 6 HOH 148 448 696 HOH HOH A . 
K 6 HOH 149 449 356 HOH HOH A . 
K 6 HOH 150 450 499 HOH HOH A . 
K 6 HOH 151 451 657 HOH HOH A . 
K 6 HOH 152 452 249 HOH HOH A . 
K 6 HOH 153 453 420 HOH HOH A . 
K 6 HOH 154 454 403 HOH HOH A . 
K 6 HOH 155 455 722 HOH HOH A . 
K 6 HOH 156 456 222 HOH HOH A . 
K 6 HOH 157 457 350 HOH HOH A . 
K 6 HOH 158 458 504 HOH HOH A . 
K 6 HOH 159 459 707 HOH HOH A . 
K 6 HOH 160 460 458 HOH HOH A . 
K 6 HOH 161 461 706 HOH HOH A . 
K 6 HOH 162 462 428 HOH HOH A . 
L 6 HOH 1   301 285 HOH HOH B . 
L 6 HOH 2   302 156 HOH HOH B . 
L 6 HOH 3   303 183 HOH HOH B . 
L 6 HOH 4   304 305 HOH HOH B . 
L 6 HOH 5   305 482 HOH HOH B . 
L 6 HOH 6   306 192 HOH HOH B . 
L 6 HOH 7   307 173 HOH HOH B . 
L 6 HOH 8   308 141 HOH HOH B . 
L 6 HOH 9   309 242 HOH HOH B . 
L 6 HOH 10  310 193 HOH HOH B . 
L 6 HOH 11  311 215 HOH HOH B . 
L 6 HOH 12  312 66  HOH HOH B . 
L 6 HOH 13  313 26  HOH HOH B . 
L 6 HOH 14  314 354 HOH HOH B . 
L 6 HOH 15  315 337 HOH HOH B . 
L 6 HOH 16  316 94  HOH HOH B . 
L 6 HOH 17  317 30  HOH HOH B . 
L 6 HOH 18  318 322 HOH HOH B . 
L 6 HOH 19  319 37  HOH HOH B . 
L 6 HOH 20  320 122 HOH HOH B . 
L 6 HOH 21  321 205 HOH HOH B . 
L 6 HOH 22  322 110 HOH HOH B . 
L 6 HOH 23  323 108 HOH HOH B . 
L 6 HOH 24  324 3   HOH HOH B . 
L 6 HOH 25  325 448 HOH HOH B . 
L 6 HOH 26  326 14  HOH HOH B . 
L 6 HOH 27  327 423 HOH HOH B . 
L 6 HOH 28  328 154 HOH HOH B . 
L 6 HOH 29  329 176 HOH HOH B . 
L 6 HOH 30  330 144 HOH HOH B . 
L 6 HOH 31  331 510 HOH HOH B . 
L 6 HOH 32  332 157 HOH HOH B . 
L 6 HOH 33  333 358 HOH HOH B . 
L 6 HOH 34  334 287 HOH HOH B . 
L 6 HOH 35  335 332 HOH HOH B . 
L 6 HOH 36  336 411 HOH HOH B . 
L 6 HOH 37  337 212 HOH HOH B . 
L 6 HOH 38  338 139 HOH HOH B . 
L 6 HOH 39  339 258 HOH HOH B . 
L 6 HOH 40  340 119 HOH HOH B . 
L 6 HOH 41  341 182 HOH HOH B . 
L 6 HOH 42  342 593 HOH HOH B . 
L 6 HOH 43  343 97  HOH HOH B . 
L 6 HOH 44  344 349 HOH HOH B . 
L 6 HOH 45  345 580 HOH HOH B . 
L 6 HOH 46  346 333 HOH HOH B . 
L 6 HOH 47  347 221 HOH HOH B . 
L 6 HOH 48  348 23  HOH HOH B . 
L 6 HOH 49  349 61  HOH HOH B . 
L 6 HOH 50  350 4   HOH HOH B . 
L 6 HOH 51  351 98  HOH HOH B . 
L 6 HOH 52  352 85  HOH HOH B . 
L 6 HOH 53  353 84  HOH HOH B . 
L 6 HOH 54  354 234 HOH HOH B . 
L 6 HOH 55  355 22  HOH HOH B . 
L 6 HOH 56  356 71  HOH HOH B . 
L 6 HOH 57  357 368 HOH HOH B . 
L 6 HOH 58  358 304 HOH HOH B . 
L 6 HOH 59  359 6   HOH HOH B . 
L 6 HOH 60  360 79  HOH HOH B . 
L 6 HOH 61  361 75  HOH HOH B . 
L 6 HOH 62  362 117 HOH HOH B . 
L 6 HOH 63  363 638 HOH HOH B . 
L 6 HOH 64  364 140 HOH HOH B . 
L 6 HOH 65  365 31  HOH HOH B . 
L 6 HOH 66  366 92  HOH HOH B . 
L 6 HOH 67  367 714 HOH HOH B . 
L 6 HOH 68  368 292 HOH HOH B . 
L 6 HOH 69  369 226 HOH HOH B . 
L 6 HOH 70  370 15  HOH HOH B . 
L 6 HOH 71  371 196 HOH HOH B . 
L 6 HOH 72  372 143 HOH HOH B . 
L 6 HOH 73  373 67  HOH HOH B . 
L 6 HOH 74  374 9   HOH HOH B . 
L 6 HOH 75  375 407 HOH HOH B . 
L 6 HOH 76  376 438 HOH HOH B . 
L 6 HOH 77  377 339 HOH HOH B . 
L 6 HOH 78  378 150 HOH HOH B . 
L 6 HOH 79  379 77  HOH HOH B . 
L 6 HOH 80  380 272 HOH HOH B . 
L 6 HOH 81  381 166 HOH HOH B . 
L 6 HOH 82  382 29  HOH HOH B . 
L 6 HOH 83  383 21  HOH HOH B . 
L 6 HOH 84  384 581 HOH HOH B . 
L 6 HOH 85  385 126 HOH HOH B . 
L 6 HOH 86  386 104 HOH HOH B . 
L 6 HOH 87  387 135 HOH HOH B . 
L 6 HOH 88  388 416 HOH HOH B . 
L 6 HOH 89  389 663 HOH HOH B . 
L 6 HOH 90  390 616 HOH HOH B . 
L 6 HOH 91  391 308 HOH HOH B . 
L 6 HOH 92  392 583 HOH HOH B . 
L 6 HOH 93  393 505 HOH HOH B . 
L 6 HOH 94  394 445 HOH HOH B . 
L 6 HOH 95  395 72  HOH HOH B . 
L 6 HOH 96  396 32  HOH HOH B . 
L 6 HOH 97  397 39  HOH HOH B . 
L 6 HOH 98  398 73  HOH HOH B . 
L 6 HOH 99  399 27  HOH HOH B . 
L 6 HOH 100 400 531 HOH HOH B . 
L 6 HOH 101 401 181 HOH HOH B . 
L 6 HOH 102 402 288 HOH HOH B . 
L 6 HOH 103 403 160 HOH HOH B . 
L 6 HOH 104 404 422 HOH HOH B . 
L 6 HOH 105 405 286 HOH HOH B . 
L 6 HOH 106 406 132 HOH HOH B . 
L 6 HOH 107 407 28  HOH HOH B . 
L 6 HOH 108 408 194 HOH HOH B . 
L 6 HOH 109 409 326 HOH HOH B . 
L 6 HOH 110 410 612 HOH HOH B . 
L 6 HOH 111 411 671 HOH HOH B . 
L 6 HOH 112 412 105 HOH HOH B . 
L 6 HOH 113 413 398 HOH HOH B . 
L 6 HOH 114 414 129 HOH HOH B . 
L 6 HOH 115 415 379 HOH HOH B . 
L 6 HOH 116 416 95  HOH HOH B . 
L 6 HOH 117 417 591 HOH HOH B . 
L 6 HOH 118 418 588 HOH HOH B . 
L 6 HOH 119 419 486 HOH HOH B . 
L 6 HOH 120 420 451 HOH HOH B . 
L 6 HOH 121 421 278 HOH HOH B . 
L 6 HOH 122 422 306 HOH HOH B . 
L 6 HOH 123 423 171 HOH HOH B . 
L 6 HOH 124 424 276 HOH HOH B . 
L 6 HOH 125 425 188 HOH HOH B . 
L 6 HOH 126 426 488 HOH HOH B . 
L 6 HOH 127 427 659 HOH HOH B . 
L 6 HOH 128 428 466 HOH HOH B . 
L 6 HOH 129 429 237 HOH HOH B . 
L 6 HOH 130 430 478 HOH HOH B . 
L 6 HOH 131 431 393 HOH HOH B . 
L 6 HOH 132 432 679 HOH HOH B . 
L 6 HOH 133 433 106 HOH HOH B . 
L 6 HOH 134 434 319 HOH HOH B . 
L 6 HOH 135 435 153 HOH HOH B . 
L 6 HOH 136 436 525 HOH HOH B . 
L 6 HOH 137 437 443 HOH HOH B . 
L 6 HOH 138 438 618 HOH HOH B . 
L 6 HOH 139 439 662 HOH HOH B . 
L 6 HOH 140 440 425 HOH HOH B . 
L 6 HOH 141 441 280 HOH HOH B . 
L 6 HOH 142 442 313 HOH HOH B . 
L 6 HOH 143 443 587 HOH HOH B . 
L 6 HOH 144 444 489 HOH HOH B . 
L 6 HOH 145 445 241 HOH HOH B . 
L 6 HOH 146 446 238 HOH HOH B . 
L 6 HOH 147 447 716 HOH HOH B . 
L 6 HOH 148 448 343 HOH HOH B . 
L 6 HOH 149 449 359 HOH HOH B . 
L 6 HOH 150 450 230 HOH HOH B . 
L 6 HOH 151 451 712 HOH HOH B . 
L 6 HOH 152 452 529 HOH HOH B . 
L 6 HOH 153 453 552 HOH HOH B . 
L 6 HOH 154 454 586 HOH HOH B . 
L 6 HOH 155 455 236 HOH HOH B . 
L 6 HOH 156 456 697 HOH HOH B . 
L 6 HOH 157 457 686 HOH HOH B . 
L 6 HOH 158 458 362 HOH HOH B . 
L 6 HOH 159 459 637 HOH HOH B . 
L 6 HOH 160 460 625 HOH HOH B . 
L 6 HOH 161 461 174 HOH HOH B . 
L 6 HOH 162 462 263 HOH HOH B . 
L 6 HOH 163 463 211 HOH HOH B . 
L 6 HOH 164 464 479 HOH HOH B . 
L 6 HOH 165 465 658 HOH HOH B . 
L 6 HOH 166 466 427 HOH HOH B . 
L 6 HOH 167 467 239 HOH HOH B . 
L 6 HOH 168 468 442 HOH HOH B . 
L 6 HOH 169 469 430 HOH HOH B . 
L 6 HOH 170 470 721 HOH HOH B . 
L 6 HOH 171 471 511 HOH HOH B . 
L 6 HOH 172 472 369 HOH HOH B . 
L 6 HOH 173 473 88  HOH HOH B . 
L 6 HOH 174 474 376 HOH HOH B . 
L 6 HOH 175 475 689 HOH HOH B . 
L 6 HOH 176 476 456 HOH HOH B . 
L 6 HOH 177 477 483 HOH HOH B . 
L 6 HOH 178 478 158 HOH HOH B . 
L 6 HOH 179 479 720 HOH HOH B . 
L 6 HOH 180 480 606 HOH HOH B . 
L 6 HOH 181 481 669 HOH HOH B . 
L 6 HOH 182 482 361 HOH HOH B . 
L 6 HOH 183 483 468 HOH HOH B . 
L 6 HOH 184 484 372 HOH HOH B . 
L 6 HOH 185 485 668 HOH HOH B . 
L 6 HOH 186 486 577 HOH HOH B . 
L 6 HOH 187 487 543 HOH HOH B . 
L 6 HOH 188 488 446 HOH HOH B . 
L 6 HOH 189 489 433 HOH HOH B . 
L 6 HOH 190 490 717 HOH HOH B . 
L 6 HOH 191 491 509 HOH HOH B . 
M 6 HOH 1   301 102 HOH HOH D . 
M 6 HOH 2   302 275 HOH HOH D . 
M 6 HOH 3   303 564 HOH HOH D . 
M 6 HOH 4   304 134 HOH HOH D . 
M 6 HOH 5   305 309 HOH HOH D . 
M 6 HOH 6   306 626 HOH HOH D . 
M 6 HOH 7   307 453 HOH HOH D . 
M 6 HOH 8   308 530 HOH HOH D . 
M 6 HOH 9   309 86  HOH HOH D . 
M 6 HOH 10  310 594 HOH HOH D . 
M 6 HOH 11  311 229 HOH HOH D . 
M 6 HOH 12  312 551 HOH HOH D . 
M 6 HOH 13  313 50  HOH HOH D . 
M 6 HOH 14  314 133 HOH HOH D . 
M 6 HOH 15  315 78  HOH HOH D . 
M 6 HOH 16  316 42  HOH HOH D . 
M 6 HOH 17  317 64  HOH HOH D . 
M 6 HOH 18  318 35  HOH HOH D . 
M 6 HOH 19  319 81  HOH HOH D . 
M 6 HOH 20  320 584 HOH HOH D . 
M 6 HOH 21  321 125 HOH HOH D . 
M 6 HOH 22  322 121 HOH HOH D . 
M 6 HOH 23  323 70  HOH HOH D . 
M 6 HOH 24  324 149 HOH HOH D . 
M 6 HOH 25  325 227 HOH HOH D . 
M 6 HOH 26  326 151 HOH HOH D . 
M 6 HOH 27  327 55  HOH HOH D . 
M 6 HOH 28  328 52  HOH HOH D . 
M 6 HOH 29  329 49  HOH HOH D . 
M 6 HOH 30  330 46  HOH HOH D . 
M 6 HOH 31  331 274 HOH HOH D . 
M 6 HOH 32  332 418 HOH HOH D . 
M 6 HOH 33  333 607 HOH HOH D . 
M 6 HOH 34  334 8   HOH HOH D . 
M 6 HOH 35  335 57  HOH HOH D . 
M 6 HOH 36  336 165 HOH HOH D . 
M 6 HOH 37  337 56  HOH HOH D . 
M 6 HOH 38  338 11  HOH HOH D . 
M 6 HOH 39  339 18  HOH HOH D . 
M 6 HOH 40  340 16  HOH HOH D . 
M 6 HOH 41  341 89  HOH HOH D . 
M 6 HOH 42  342 124 HOH HOH D . 
M 6 HOH 43  343 294 HOH HOH D . 
M 6 HOH 44  344 76  HOH HOH D . 
M 6 HOH 45  345 1   HOH HOH D . 
M 6 HOH 46  346 5   HOH HOH D . 
M 6 HOH 47  347 641 HOH HOH D . 
M 6 HOH 48  348 392 HOH HOH D . 
M 6 HOH 49  349 179 HOH HOH D . 
M 6 HOH 50  350 692 HOH HOH D . 
M 6 HOH 51  351 698 HOH HOH D . 
M 6 HOH 52  352 101 HOH HOH D . 
M 6 HOH 53  353 59  HOH HOH D . 
M 6 HOH 54  354 82  HOH HOH D . 
M 6 HOH 55  355 255 HOH HOH D . 
M 6 HOH 56  356 492 HOH HOH D . 
M 6 HOH 57  357 284 HOH HOH D . 
M 6 HOH 58  358 175 HOH HOH D . 
M 6 HOH 59  359 38  HOH HOH D . 
M 6 HOH 60  360 7   HOH HOH D . 
M 6 HOH 61  361 33  HOH HOH D . 
M 6 HOH 62  362 329 HOH HOH D . 
M 6 HOH 63  363 341 HOH HOH D . 
M 6 HOH 64  364 99  HOH HOH D . 
M 6 HOH 65  365 17  HOH HOH D . 
M 6 HOH 66  366 130 HOH HOH D . 
M 6 HOH 67  367 131 HOH HOH D . 
M 6 HOH 68  368 90  HOH HOH D . 
M 6 HOH 69  369 34  HOH HOH D . 
M 6 HOH 70  370 250 HOH HOH D . 
M 6 HOH 71  371 19  HOH HOH D . 
M 6 HOH 72  372 111 HOH HOH D . 
M 6 HOH 73  373 96  HOH HOH D . 
M 6 HOH 74  374 47  HOH HOH D . 
M 6 HOH 75  375 65  HOH HOH D . 
M 6 HOH 76  376 69  HOH HOH D . 
M 6 HOH 77  377 585 HOH HOH D . 
M 6 HOH 78  378 74  HOH HOH D . 
M 6 HOH 79  379 683 HOH HOH D . 
M 6 HOH 80  380 107 HOH HOH D . 
M 6 HOH 81  381 168 HOH HOH D . 
M 6 HOH 82  382 191 HOH HOH D . 
M 6 HOH 83  383 203 HOH HOH D . 
M 6 HOH 84  384 500 HOH HOH D . 
M 6 HOH 85  385 472 HOH HOH D . 
M 6 HOH 86  386 172 HOH HOH D . 
M 6 HOH 87  387 163 HOH HOH D . 
M 6 HOH 88  388 667 HOH HOH D . 
M 6 HOH 89  389 631 HOH HOH D . 
M 6 HOH 90  390 338 HOH HOH D . 
M 6 HOH 91  391 381 HOH HOH D . 
M 6 HOH 92  392 681 HOH HOH D . 
M 6 HOH 93  393 702 HOH HOH D . 
M 6 HOH 94  394 279 HOH HOH D . 
M 6 HOH 95  395 283 HOH HOH D . 
M 6 HOH 96  396 331 HOH HOH D . 
M 6 HOH 97  397 220 HOH HOH D . 
M 6 HOH 98  398 347 HOH HOH D . 
M 6 HOH 99  399 538 HOH HOH D . 
M 6 HOH 100 400 704 HOH HOH D . 
M 6 HOH 101 401 477 HOH HOH D . 
M 6 HOH 102 402 116 HOH HOH D . 
M 6 HOH 103 403 674 HOH HOH D . 
M 6 HOH 104 404 621 HOH HOH D . 
M 6 HOH 105 405 273 HOH HOH D . 
M 6 HOH 106 406 148 HOH HOH D . 
M 6 HOH 107 407 665 HOH HOH D . 
M 6 HOH 108 408 224 HOH HOH D . 
M 6 HOH 109 409 426 HOH HOH D . 
M 6 HOH 110 410 302 HOH HOH D . 
M 6 HOH 111 411 432 HOH HOH D . 
M 6 HOH 112 412 460 HOH HOH D . 
M 6 HOH 113 413 643 HOH HOH D . 
M 6 HOH 114 414 609 HOH HOH D . 
M 6 HOH 115 415 608 HOH HOH D . 
M 6 HOH 116 416 495 HOH HOH D . 
M 6 HOH 117 417 539 HOH HOH D . 
M 6 HOH 118 418 487 HOH HOH D . 
M 6 HOH 119 419 244 HOH HOH D . 
M 6 HOH 120 420 718 HOH HOH D . 
M 6 HOH 121 421 254 HOH HOH D . 
M 6 HOH 122 422 685 HOH HOH D . 
M 6 HOH 123 423 494 HOH HOH D . 
M 6 HOH 124 424 528 HOH HOH D . 
M 6 HOH 125 425 497 HOH HOH D . 
M 6 HOH 126 426 476 HOH HOH D . 
M 6 HOH 127 427 521 HOH HOH D . 
M 6 HOH 128 428 218 HOH HOH D . 
M 6 HOH 129 429 700 HOH HOH D . 
M 6 HOH 130 430 506 HOH HOH D . 
M 6 HOH 131 431 461 HOH HOH D . 
M 6 HOH 132 432 619 HOH HOH D . 
M 6 HOH 133 433 282 HOH HOH D . 
M 6 HOH 134 434 519 HOH HOH D . 
M 6 HOH 135 435 91  HOH HOH D . 
M 6 HOH 136 436 167 HOH HOH D . 
M 6 HOH 137 437 145 HOH HOH D . 
M 6 HOH 138 438 390 HOH HOH D . 
M 6 HOH 139 439 363 HOH HOH D . 
M 6 HOH 140 440 655 HOH HOH D . 
M 6 HOH 141 441 360 HOH HOH D . 
M 6 HOH 142 442 269 HOH HOH D . 
M 6 HOH 143 443 695 HOH HOH D . 
M 6 HOH 144 444 703 HOH HOH D . 
M 6 HOH 145 445 502 HOH HOH D . 
M 6 HOH 146 446 447 HOH HOH D . 
M 6 HOH 147 447 544 HOH HOH D . 
M 6 HOH 148 448 457 HOH HOH D . 
M 6 HOH 149 449 673 HOH HOH D . 
M 6 HOH 150 450 515 HOH HOH D . 
M 6 HOH 151 451 382 HOH HOH D . 
M 6 HOH 152 452 323 HOH HOH D . 
M 6 HOH 153 453 534 HOH HOH D . 
M 6 HOH 154 454 694 HOH HOH D . 
M 6 HOH 155 455 556 HOH HOH D . 
M 6 HOH 156 456 518 HOH HOH D . 
N 6 HOH 1   301 592 HOH HOH C . 
N 6 HOH 2   302 597 HOH HOH C . 
N 6 HOH 3   303 334 HOH HOH C . 
N 6 HOH 4   304 512 HOH HOH C . 
N 6 HOH 5   305 600 HOH HOH C . 
N 6 HOH 6   306 371 HOH HOH C . 
N 6 HOH 7   307 630 HOH HOH C . 
N 6 HOH 8   308 421 HOH HOH C . 
N 6 HOH 9   309 440 HOH HOH C . 
N 6 HOH 10  310 43  HOH HOH C . 
N 6 HOH 11  311 177 HOH HOH C . 
N 6 HOH 12  312 142 HOH HOH C . 
N 6 HOH 13  313 730 HOH HOH C . 
N 6 HOH 14  314 364 HOH HOH C . 
N 6 HOH 15  315 136 HOH HOH C . 
N 6 HOH 16  316 574 HOH HOH C . 
N 6 HOH 17  317 233 HOH HOH C . 
N 6 HOH 18  318 219 HOH HOH C . 
N 6 HOH 19  319 680 HOH HOH C . 
N 6 HOH 20  320 470 HOH HOH C . 
N 6 HOH 21  321 155 HOH HOH C . 
N 6 HOH 22  322 24  HOH HOH C . 
N 6 HOH 23  323 301 HOH HOH C . 
N 6 HOH 24  324 690 HOH HOH C . 
N 6 HOH 25  325 691 HOH HOH C . 
N 6 HOH 26  326 578 HOH HOH C . 
N 6 HOH 27  327 245 HOH HOH C . 
N 6 HOH 28  328 231 HOH HOH C . 
N 6 HOH 29  329 316 HOH HOH C . 
N 6 HOH 30  330 260 HOH HOH C . 
N 6 HOH 31  331 293 HOH HOH C . 
N 6 HOH 32  332 475 HOH HOH C . 
N 6 HOH 33  333 342 HOH HOH C . 
N 6 HOH 34  334 401 HOH HOH C . 
N 6 HOH 35  335 555 HOH HOH C . 
N 6 HOH 36  336 409 HOH HOH C . 
N 6 HOH 37  337 415 HOH HOH C . 
N 6 HOH 38  338 253 HOH HOH C . 
N 6 HOH 39  339 546 HOH HOH C . 
N 6 HOH 40  340 123 HOH HOH C . 
N 6 HOH 41  341 87  HOH HOH C . 
N 6 HOH 42  342 344 HOH HOH C . 
N 6 HOH 43  343 469 HOH HOH C . 
N 6 HOH 44  344 449 HOH HOH C . 
N 6 HOH 45  345 340 HOH HOH C . 
N 6 HOH 46  346 187 HOH HOH C . 
N 6 HOH 47  347 672 HOH HOH C . 
N 6 HOH 48  348 650 HOH HOH C . 
N 6 HOH 49  349 417 HOH HOH C . 
N 6 HOH 50  350 708 HOH HOH C . 
N 6 HOH 51  351 138 HOH HOH C . 
N 6 HOH 52  352 235 HOH HOH C . 
N 6 HOH 53  353 355 HOH HOH C . 
N 6 HOH 54  354 266 HOH HOH C . 
N 6 HOH 55  355 60  HOH HOH C . 
N 6 HOH 56  356 137 HOH HOH C . 
N 6 HOH 57  357 513 HOH HOH C . 
N 6 HOH 58  358 184 HOH HOH C . 
N 6 HOH 59  359 246 HOH HOH C . 
N 6 HOH 60  360 463 HOH HOH C . 
N 6 HOH 61  361 399 HOH HOH C . 
N 6 HOH 62  362 699 HOH HOH C . 
N 6 HOH 63  363 353 HOH HOH C . 
N 6 HOH 64  364 404 HOH HOH C . 
N 6 HOH 65  365 367 HOH HOH C . 
N 6 HOH 66  366 413 HOH HOH C . 
N 6 HOH 67  367 565 HOH HOH C . 
N 6 HOH 68  368 315 HOH HOH C . 
N 6 HOH 69  369 377 HOH HOH C . 
N 6 HOH 70  370 653 HOH HOH C . 
N 6 HOH 71  371 320 HOH HOH C . 
N 6 HOH 72  372 558 HOH HOH C . 
N 6 HOH 73  373 100 HOH HOH C . 
N 6 HOH 74  374 297 HOH HOH C . 
N 6 HOH 75  375 677 HOH HOH C . 
N 6 HOH 76  376 535 HOH HOH C . 
N 6 HOH 77  377 223 HOH HOH C . 
N 6 HOH 78  378 549 HOH HOH C . 
N 6 HOH 79  379 710 HOH HOH C . 
N 6 HOH 80  380 678 HOH HOH C . 
N 6 HOH 81  381 378 HOH HOH C . 
N 6 HOH 82  382 709 HOH HOH C . 
N 6 HOH 83  383 310 HOH HOH C . 
N 6 HOH 84  384 491 HOH HOH C . 
N 6 HOH 85  385 614 HOH HOH C . 
N 6 HOH 86  386 508 HOH HOH C . 
N 6 HOH 87  387 490 HOH HOH C . 
N 6 HOH 88  388 507 HOH HOH C . 
N 6 HOH 89  389 589 HOH HOH C . 
N 6 HOH 90  390 365 HOH HOH C . 
N 6 HOH 91  391 118 HOH HOH C . 
N 6 HOH 92  392 711 HOH HOH C . 
N 6 HOH 93  393 206 HOH HOH C . 
N 6 HOH 94  394 277 HOH HOH C . 
N 6 HOH 95  395 601 HOH HOH C . 
N 6 HOH 96  396 265 HOH HOH C . 
N 6 HOH 97  397 562 HOH HOH C . 
N 6 HOH 98  398 605 HOH HOH C . 
N 6 HOH 99  399 731 HOH HOH C . 
N 6 HOH 100 400 557 HOH HOH C . 
N 6 HOH 101 401 394 HOH HOH C . 
N 6 HOH 102 402 262 HOH HOH C . 
N 6 HOH 103 403 633 HOH HOH C . 
N 6 HOH 104 404 545 HOH HOH C . 
N 6 HOH 105 405 252 HOH HOH C . 
N 6 HOH 106 406 261 HOH HOH C . 
N 6 HOH 107 407 127 HOH HOH C . 
N 6 HOH 108 408 164 HOH HOH C . 
N 6 HOH 109 409 554 HOH HOH C . 
N 6 HOH 110 410 542 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 scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BI1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.519 
_cell.length_a_esd                 ? 
_cell.length_b                     82.052 
_cell.length_b_esd                 ? 
_cell.length_c                     127.902 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BI1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BI1 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.36 
_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    '100 mM Tris-HCl pH 8.5, 24% PEG 10000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97933 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97933 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BI1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               34.53 
_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                                     80063 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.132 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.65 
_reflns_shell.d_res_low                                     1.667 
_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                             2309 
_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                               ? 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.3496 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               ? 
_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                                 9BI1 
_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                            1.65 
_refine.ls_d_res_low                             34.53 
_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                     79807 
_refine.ls_number_reflns_R_free                  4063 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.28 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2203 
_refine.ls_R_factor_R_free                       0.2601 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2182 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 28.13 
_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                            0.27 
_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                       1.65 
_refine_hist.d_res_low                        34.53 
_refine_hist.number_atoms_solvent             619 
_refine_hist.number_atoms_total               6003 
_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        5194 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         190 
_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' ? 0.016  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.265  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.890 ? 770 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.066  ? 790 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.012  ? 949 ? f_plane_restr      ? ? 
# 
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' 1.65 1.67 . . 136 2538 94.00  . . . . 0.4070 . . . . . . . . . . . 0.4366 
'X-RAY DIFFRACTION' 1.67 1.69 . . 146 2611 98.00  . . . . 0.3678 . . . . . . . . . . . 0.4206 
'X-RAY DIFFRACTION' 1.69 1.72 . . 127 2684 99.00  . . . . .      . . . . . . . . . . . 0.3537 
'X-RAY DIFFRACTION' 1.72 1.74 . . 142 2650 100.00 . . . . 0.3381 . . . . . . . . . . . 0.3664 
'X-RAY DIFFRACTION' 1.74 1.76 . . 142 2700 100.00 . . . . 0.3173 . . . . . . . . . . . 0.3889 
'X-RAY DIFFRACTION' 1.76 1.79 . . 133 2684 100.00 . . . . 0.3033 . . . . . . . . . . . 0.3410 
'X-RAY DIFFRACTION' 1.79 1.81 . . 157 2677 100.00 . . . . 0.2940 . . . . . . . . . . . 0.3117 
'X-RAY DIFFRACTION' 1.81 1.84 . . 167 2646 100.00 . . . . 0.2709 . . . . . . . . . . . 0.3324 
'X-RAY DIFFRACTION' 1.84 1.87 . . 164 2682 100.00 . . . . 0.2639 . . . . . . . . . . . 0.3187 
'X-RAY DIFFRACTION' 1.87 1.90 . . 133 2573 100.00 . . . . 0.2618 . . . . . . . . . . . 0.2927 
'X-RAY DIFFRACTION' 1.93 1.94 . . 54  1065 100.00 . . . . .      . . . . . . . . . . . 0.2608 
'X-RAY DIFFRACTION' 1.94 1.98 . . 134 2693 100.00 . . . . 0.2570 . . . . . . . . . . . 0.3054 
'X-RAY DIFFRACTION' 1.98 2.02 . . 148 2691 100.00 . . . . 0.2561 . . . . . . . . . . . 0.3234 
'X-RAY DIFFRACTION' 2.02 2.06 . . 138 2710 100.00 . . . . 0.2492 . . . . . . . . . . . 0.2998 
'X-RAY DIFFRACTION' 2.06 2.11 . . 152 2680 100.00 . . . . 0.2489 . . . . . . . . . . . 0.2742 
'X-RAY DIFFRACTION' 2.11 2.16 . . 127 2703 100.00 . . . . 0.2251 . . . . . . . . . . . 0.2601 
'X-RAY DIFFRACTION' 2.16 2.22 . . 147 2684 100.00 . . . . 0.2206 . . . . . . . . . . . 0.2986 
'X-RAY DIFFRACTION' 2.22 2.29 . . 90  1789 66.00  . . . . 0.2211 . . . . . . . . . . . 0.2364 
'X-RAY DIFFRACTION' 2.29 2.36 . . 153 2698 100.00 . . . . 0.2149 . . . . . . . . . . . 0.2400 
'X-RAY DIFFRACTION' 2.36 2.44 . . 169 2702 100.00 . . . . 0.2169 . . . . . . . . . . . 0.2540 
'X-RAY DIFFRACTION' 2.44 2.54 . . 132 2709 100.00 . . . . 0.2148 . . . . . . . . . . . 0.2449 
'X-RAY DIFFRACTION' 2.54 2.66 . . 133 2726 100.00 . . . . 0.2149 . . . . . . . . . . . 0.2782 
'X-RAY DIFFRACTION' 2.66 2.80 . . 151 2722 100.00 . . . . 0.2183 . . . . . . . . . . . 0.2577 
'X-RAY DIFFRACTION' 2.80 2.97 . . 130 2748 100.00 . . . . 0.2079 . . . . . . . . . . . 0.2470 
'X-RAY DIFFRACTION' 2.97 3.20 . . 148 2735 100.00 . . . . 0.2072 . . . . . . . . . . . 0.2380 
'X-RAY DIFFRACTION' 3.20 3.52 . . 145 2765 100.00 . . . . 0.1945 . . . . . . . . . . . 0.2371 
'X-RAY DIFFRACTION' 3.52 4.03 . . 142 2774 100.00 . . . . 0.1803 . . . . . . . . . . . 0.2317 
'X-RAY DIFFRACTION' 4.03 5.08 . . 151 2801 100.00 . . . . 0.1711 . . . . . . . . . . . 0.1988 
# 
_struct.entry_id                     9BI1 
_struct.title                        'Crystal structure of GMPPNP bound KRAS G12D in complex with CYPA and RMC-7977' 
_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        9BI1 
_struct_keywords.text            'GTPase SIGNALING PROTEIN Isomerase, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
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 2 ? 
D N N 1 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 3 ? 
J N N 4 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP RASK_HUMAN P01116 P01116-2 1 
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
;
1 
2 UNP PPIA_HUMAN P62937 ?        2 
;MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BI1 A 2 ? 170 ? P01116 1 ? 169 ? 1 169 
2 2 9BI1 B 2 ? 166 ? P62937 1 ? 165 ? 1 165 
3 2 9BI1 D 2 ? 166 ? P62937 1 ? 165 ? 1 165 
4 1 9BI1 C 2 ? 170 ? P01116 1 ? 169 ? 1 169 
# 
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 9BI1 GLY A 1  ? UNP P01116 ?   ?  'expression tag' 0  1 
1 9BI1 ASP A 13 ? UNP P01116 GLY 12 variant          12 2 
2 9BI1 GLY B 1  ? UNP P62937 ?   ?  'expression tag' 0  3 
3 9BI1 GLY D 1  ? UNP P62937 ?   ?  'expression tag' 0  4 
4 9BI1 GLY C 1  ? UNP P01116 ?   ?  'expression tag' 0  5 
4 9BI1 ASP C 13 ? UNP P01116 GLY 12 variant          12 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 16  ? ASN A 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2  AA2 GLN A 62  ? MET A 68  ? GLN A 61  MET A 67  5 ? 7  
HELX_P HELX_P3  AA3 ARG A 69  ? GLY A 76  ? ARG A 68  GLY A 75  1 ? 8  
HELX_P HELX_P4  AA4 ASN A 87  ? ASP A 106 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P5  AA5 ASP A 127 ? GLY A 139 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6  AA6 GLY A 152 ? LYS A 168 ? GLY A 151 LYS A 167 1 ? 17 
HELX_P HELX_P7  AA7 VAL B 30  ? GLY B 43  ? VAL B 29  GLY B 42  1 ? 14 
HELX_P HELX_P8  AA8 THR B 120 ? ASP B 124 ? THR B 119 ASP B 123 5 ? 5  
HELX_P HELX_P9  AA9 GLY B 136 ? ARG B 145 ? GLY B 135 ARG B 144 1 ? 10 
HELX_P HELX_P10 AB1 VAL C 30  ? GLY C 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P11 AB2 THR C 120 ? ASP C 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P12 AB3 GLY C 136 ? GLU C 144 ? GLY D 135 GLU D 143 1 ? 9  
HELX_P HELX_P13 AB4 ARG C 145 ? GLY C 147 ? ARG D 144 GLY D 146 5 ? 3  
HELX_P HELX_P14 AB5 GLY D 16  ? ASN D 27  ? GLY C 15  ASN C 26  1 ? 12 
HELX_P HELX_P15 AB6 GLN D 62  ? GLU D 64  ? GLN C 61  GLU C 63  5 ? 3  
HELX_P HELX_P16 AB7 TYR D 65  ? GLY D 76  ? TYR C 64  GLY C 75  1 ? 12 
HELX_P HELX_P17 AB8 ASN D 87  ? ASP D 106 ? ASN C 86  ASP C 105 1 ? 20 
HELX_P HELX_P18 AB9 ASP D 127 ? GLY D 139 ? ASP C 126 GLY C 138 1 ? 13 
HELX_P HELX_P19 AC1 GLY D 152 ? LYS D 168 ? GLY C 151 LYS C 167 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 18 OG  ? ? ? 1_555 F MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc2  metalc ? ? A THR 36 OG1 ? ? ? 1_555 F MG  . MG ? ? A THR 35  A MG  202 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
metalc3  metalc ? ? E GNP .  O1G ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc4  metalc ? ? E GNP .  O1B ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 1.970 ? ? 
metalc5  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 318 1_555 ? ? ? ? ? ? ? 2.150 ? ? 
metalc6  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 346 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc7  metalc ? ? D SER 18 OG  ? ? ? 1_555 J MG  . MG ? ? C SER 17  C MG  202 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc8  metalc ? ? D THR 36 OG1 ? ? ? 1_555 J MG  . MG ? ? C THR 35  C MG  202 1_555 ? ? ? ? ? ? ? 2.248 ? ? 
metalc9  metalc ? ? I GNP .  O1G ? ? ? 1_555 J MG  . MG ? ? C GNP 201 C MG  202 1_555 ? ? ? ? ? ? ? 1.914 ? ? 
metalc10 metalc ? ? I GNP .  O1B ? ? ? 1_555 J MG  . MG ? ? C GNP 201 C MG  202 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc11 metalc ? ? J MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? C MG  202 C HOH 320 1_555 ? ? ? ? ? ? ? 2.189 ? ? 
metalc12 metalc ? ? J MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? C MG  202 C HOH 326 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 OG1 ? A THR 36 ? A THR 35  ? 1_555 80.3  ? 
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_555 170.2 ? 
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 90.0  ? 
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 91.1  ? 
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_555 169.8 ? 
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 98.7  ? 
7  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 318 ? 1_555 85.8  ? 
8  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 318 ? 1_555 87.2  ? 
9  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 318 ? 1_555 92.5  ? 
10 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 318 ? 1_555 97.8  ? 
11 OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 91.3  ? 
12 OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 85.1  ? 
13 O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 89.2  ? 
14 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 89.5  ? 
15 O   ? K HOH .  ? A HOH 318 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 172.2 ? 
16 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 OG1 ? D THR 36 ? C THR 35  ? 1_555 79.6  ? 
17 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O1G ? I GNP .  ? C GNP 201 ? 1_555 152.7 ? 
18 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O1G ? I GNP .  ? C GNP 201 ? 1_555 84.4  ? 
19 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O1B ? I GNP .  ? C GNP 201 ? 1_555 93.2  ? 
20 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O1B ? I GNP .  ? C GNP 201 ? 1_555 166.4 ? 
21 O1G ? I GNP .  ? C GNP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O1B ? I GNP .  ? C GNP 201 ? 1_555 97.6  ? 
22 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 320 ? 1_555 97.8  ? 
23 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 320 ? 1_555 102.9 ? 
24 O1G ? I GNP .  ? C GNP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 320 ? 1_555 107.2 ? 
25 O1B ? I GNP .  ? C GNP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 320 ? 1_555 89.4  ? 
26 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 326 ? 1_555 81.8  ? 
27 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 326 ? 1_555 74.6  ? 
28 O1G ? I GNP .  ? C GNP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 326 ? 1_555 72.6  ? 
29 O1B ? I GNP .  ? C GNP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 326 ? 1_555 93.1  ? 
30 O   ? N HOH .  ? C HOH 320 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? N HOH .  ? C HOH 326 ? 1_555 177.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
AA4 ? 6 ? 
# 
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 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? 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 GLU A 4   ? VAL A 10  ? GLU A 3   VAL A 9   
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 B 55  ILE B 57  
AA2 2 MET B 62  ? GLY B 65  ? MET B 61  GLY B 64  
AA2 3 PHE B 113 ? CYS B 116 ? PHE B 112 CYS B 115 
AA2 4 ILE B 98  ? MET B 101 ? ILE B 97  MET B 100 
AA2 5 VAL B 129 ? GLU B 135 ? VAL B 128 GLU B 134 
AA2 6 GLU B 16  ? LEU B 25  ? GLU B 15  LEU B 24  
AA2 7 THR B 6   ? VAL B 13  ? THR B 5   VAL B 12  
AA2 8 ILE B 157 ? LEU B 165 ? ILE B 156 LEU B 164 
AA3 1 ARG C 56  ? ILE C 58  ? ARG D 55  ILE D 57  
AA3 2 MET C 62  ? GLY C 65  ? MET D 61  GLY D 64  
AA3 3 PHE C 113 ? CYS C 116 ? PHE D 112 CYS D 115 
AA3 4 ILE C 98  ? MET C 101 ? ILE D 97  MET D 100 
AA3 5 VAL C 129 ? VAL C 133 ? VAL D 128 VAL D 132 
AA3 6 GLU C 16  ? LEU C 25  ? GLU D 15  LEU D 24  
AA3 7 THR C 6   ? VAL C 13  ? THR D 5   VAL D 12  
AA3 8 ILE C 157 ? LEU C 165 ? ILE D 156 LEU D 164 
AA4 1 GLU D 38  ? ILE D 47  ? GLU C 37  ILE C 46  
AA4 2 GLU D 50  ? THR D 59  ? GLU C 49  THR C 58  
AA4 3 THR D 3   ? VAL D 10  ? THR C 2   VAL C 9   
AA4 4 GLY D 78  ? ALA D 84  ? GLY C 77  ALA C 83  
AA4 5 MET D 112 ? ASN D 117 ? MET C 111 ASN C 116 
AA4 6 PHE D 142 ? GLU D 144 ? PHE C 141 GLU C 143 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP A 39  ? N ASP A 38  O ASP A 58  ? O ASP A 57  
AA1 2 3 O LEU A 57  ? O LEU A 56  N VAL A 9   ? N VAL A 8   
AA1 3 4 N VAL A 10  ? N VAL A 9   O LEU A 80  ? O LEU A 79  
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 B 55  O GLN B 64  ? O GLN B 63  
AA2 2 3 N CYS B 63  ? N CYS B 62  O ILE B 115 ? O ILE B 114 
AA2 3 4 O PHE B 114 ? O PHE B 113 N SER B 100 ? N SER B 99  
AA2 4 5 N LEU B 99  ? N LEU B 98  O GLY B 131 ? O GLY B 130 
AA2 5 6 O LYS B 134 ? O LYS B 133 N SER B 22  ? N SER B 21  
AA2 6 7 O GLY B 19  ? O GLY B 18  N ILE B 11  ? N ILE B 10  
AA2 7 8 N ASP B 10  ? N ASP B 9   O ASP B 161 ? O ASP B 160 
AA3 1 2 N ARG C 56  ? N ARG D 55  O GLN C 64  ? O GLN D 63  
AA3 2 3 N CYS C 63  ? N CYS D 62  O ILE C 115 ? O ILE D 114 
AA3 3 4 O CYS C 116 ? O CYS D 115 N ILE C 98  ? N ILE D 97  
AA3 4 5 N LEU C 99  ? N LEU D 98  O GLY C 131 ? O GLY D 130 
AA3 5 6 O LYS C 132 ? O LYS D 131 N GLU C 24  ? N GLU D 23  
AA3 6 7 O LEU C 18  ? O LEU D 17  N ILE C 11  ? N ILE D 10  
AA3 7 8 N ASP C 10  ? N ASP D 9   O ASP C 161 ? O ASP D 160 
AA4 1 2 N LYS D 43  ? N LYS C 42  O LEU D 54  ? O LEU C 53  
AA4 2 3 O ASP D 55  ? O ASP C 54  N TYR D 5   ? N TYR C 4   
AA4 3 4 N VAL D 10  ? N VAL C 9   O VAL D 82  ? O VAL C 81  
AA4 4 5 N PHE D 83  ? N PHE C 82  O ASN D 117 ? O ASN C 116 
AA4 5 6 N LEU D 114 ? N LEU C 113 O ILE D 143 ? O ILE C 142 
# 
_pdbx_entry_details.entry_id                   9BI1 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 H    C ILE 139 ? ? O   C HOH 305 ? ? 1.33 
2  1 HZ3  A LYS 88  ? ? O   A HOH 301 ? ? 1.34 
3  1 HE   A ARG 97  ? ? O   A HOH 305 ? ? 1.37 
4  1 H    C ARG 164 ? ? O   C HOH 304 ? ? 1.48 
5  1 HH12 B ARG 144 ? ? O   B HOH 302 ? ? 1.49 
6  1 HH21 C ARG 68  ? ? O   C HOH 309 ? ? 1.51 
7  1 HZ1  C LYS 16  ? ? O2G C GNP 201 ? ? 1.53 
8  1 HH12 D ARG 69  ? ? O   D HOH 305 ? ? 1.55 
9  1 H    C GLY 60  ? ? O   C HOH 302 ? ? 1.56 
10 1 HH   C TYR 40  ? ? O   C HOH 312 ? ? 1.57 
11 1 HZ3  A LYS 104 ? ? O   A HOH 307 ? ? 1.57 
12 1 HZ3  B LYS 91  ? ? O   B HOH 304 ? ? 1.59 
13 1 HZ2  B LYS 91  ? ? O   B HOH 305 ? ? 1.59 
14 1 HH11 C ARG 41  ? ? O   C HOH 301 ? ? 1.59 
15 1 O    A HOH 396 ? ? O   A HOH 412 ? ? 1.62 
16 1 O    B HOH 301 ? ? O   B HOH 423 ? ? 1.67 
17 1 O    D HOH 393 ? ? O   D HOH 444 ? ? 1.71 
18 1 O    B HOH 317 ? ? O   B HOH 453 ? ? 1.73 
19 1 NH1  C ARG 41  ? ? O   C HOH 301 ? ? 1.74 
20 1 O    A HOH 328 ? ? O   A HOH 396 ? ? 1.77 
21 1 O    C HOH 378 ? ? O   C HOH 382 ? ? 1.78 
22 1 O2G  C GNP 201 ? ? O   C HOH 302 ? ? 1.79 
23 1 OD1  C ASN 116 ? ? O   C HOH 303 ? ? 1.80 
24 1 O    A HOH 349 ? ? O   B HOH 417 ? ? 1.82 
25 1 O    B HOH 357 ? ? O   B HOH 417 ? ? 1.83 
26 1 O    D HOH 447 ? ? O   D HOH 454 ? ? 1.84 
27 1 O    C VAL 160 ? ? O   C HOH 304 ? ? 1.85 
28 1 O    C HOH 333 ? ? O   C HOH 404 ? ? 1.85 
29 1 O    A HOH 436 ? ? O   D HOH 430 ? ? 1.86 
30 1 O    A HOH 422 ? ? O   D HOH 422 ? ? 1.88 
31 1 O    A HOH 430 ? ? O   A HOH 445 ? ? 1.91 
32 1 NZ   A LYS 88  ? ? O   A HOH 301 ? ? 1.92 
33 1 O    A HOH 417 ? ? O   B HOH 357 ? ? 1.92 
34 1 O    D HOH 384 ? ? O   D HOH 424 ? ? 1.93 
35 1 O    C ALA 134 ? ? O   C HOH 305 ? ? 1.93 
36 1 O    A HOH 457 ? ? O   A HOH 458 ? ? 1.98 
37 1 O    C HOH 334 ? ? O   C HOH 403 ? ? 1.98 
38 1 O    C HOH 343 ? ? O   C HOH 387 ? ? 1.99 
39 1 N    C ILE 139 ? ? O   C HOH 305 ? ? 2.02 
40 1 O    B HOH 422 ? ? O   B HOH 432 ? ? 2.02 
41 1 O    A HOH 393 ? ? O   A HOH 414 ? ? 2.03 
42 1 O    D HOH 349 ? ? O   D HOH 436 ? ? 2.03 
43 1 OE2  B GLU 81  ? ? O   B HOH 301 ? ? 2.04 
44 1 OD2  A ASP 153 ? ? O   A HOH 302 ? ? 2.05 
45 1 O    C THR 74  ? ? O   C HOH 306 ? ? 2.05 
46 1 O    C HOH 323 ? ? O   C HOH 400 ? ? 2.05 
47 1 O    B HOH 402 ? ? O   B HOH 435 ? ? 2.05 
48 1 O    C GLY 138 ? ? O   C HOH 307 ? ? 2.06 
49 1 NZ   D LYS 31  ? ? OE2 D GLU 84  ? ? 2.07 
50 1 O    A HOH 401 ? ? O   A HOH 402 ? ? 2.08 
51 1 O    D HOH 445 ? ? O   D HOH 449 ? ? 2.10 
52 1 SD   B MET 61  ? ? O   B HOH 427 ? ? 2.10 
53 1 O    D HOH 420 ? ? O   D HOH 444 ? ? 2.12 
54 1 N    C ARG 164 ? ? O   C HOH 304 ? ? 2.12 
55 1 NH1  B ARG 144 ? ? O   B HOH 302 ? ? 2.13 
56 1 O    A HOH 301 ? ? O   A HOH 312 ? ? 2.13 
57 1 O    A HOH 371 ? ? O   A HOH 373 ? ? 2.13 
58 1 O    D VAL 6   ? ? O   D HOH 301 ? ? 2.14 
59 1 O    C HOH 365 ? ? O   C HOH 397 ? ? 2.16 
60 1 O    B HOH 376 ? ? O   B HOH 437 ? ? 2.16 
61 1 OD1  A ASP 12  ? ? O   A HOH 303 ? ? 2.16 
62 1 O    D HOH 439 ? ? O   D HOH 452 ? ? 2.17 
63 1 O    A HOH 328 ? ? O   A HOH 442 ? ? 2.17 
64 1 O    A GLY 60  ? ? O   A HOH 304 ? ? 2.18 
65 1 OD1  C ASP 92  ? ? O   C HOH 308 ? ? 2.18 
66 1 NE   A ARG 97  ? ? O   A HOH 305 ? ? 2.18 
67 1 O    B HOH 333 ? ? O   B HOH 428 ? ? 2.19 
68 1 O    D HOH 383 ? ? O   D HOH 418 ? ? 2.19 
69 1 NH2  C ARG 68  ? ? O   C HOH 309 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1  1 O   A HOH 325 ? ? 1_555 O B HOH 481 ? ? 4_555 1.57 
2  1 O   A HOH 315 ? ? 1_555 O D HOH 456 ? ? 1_455 1.77 
3  1 O   B HOH 488 ? ? 1_555 O D HOH 308 ? ? 3_645 1.80 
4  1 O   A HOH 416 ? ? 1_555 O D HOH 456 ? ? 1_455 1.91 
5  1 OE1 A GLN 150 ? ? 1_555 O B HOH 481 ? ? 4_555 1.93 
6  1 O   A HOH 411 ? ? 1_555 O B HOH 452 ? ? 4_555 1.97 
7  1 O   B HOH 424 ? ? 1_555 O D HOH 425 ? ? 4_455 1.99 
8  1 O   A HOH 459 ? ? 1_555 O B HOH 470 ? ? 4_555 2.01 
9  1 O   B HOH 459 ? ? 1_555 O C HOH 353 ? ? 2_554 2.09 
10 1 O   B HOH 426 ? ? 1_555 O D HOH 425 ? ? 4_455 2.12 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              61 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              61 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              61 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                80.10 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -20.10 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 37  ? ? -170.51 132.63 
2  1 ASP A 105 ? ? 39.45   54.06  
3  1 ARG A 149 ? ? 75.23   -0.27  
4  1 PHE B 60  ? ? -135.11 -65.09 
5  1 LYS B 133 ? ? -95.28  -62.64 
6  1 PHE D 60  ? ? -132.73 -66.11 
7  1 LYS D 133 ? ? -95.33  -68.72 
8  1 ILE C 36  ? ? -95.05  -66.37 
9  1 ARG C 102 ? ? -56.07  -70.94 
10 1 ASP C 105 ? ? 46.32   76.30  
11 1 LYS C 117 ? ? 72.55   30.92  
12 1 CYS C 118 ? ? -64.88  3.08   
13 1 HIS C 166 ? ? -58.31  -9.98  
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 N2  ? B ZNI 201 ? PLANAR       . 
2 1 C10 ? D ZNI 201 ? 'WRONG HAND' . 
3 1 C9  ? D ZNI 201 ? 'WRONG HAND' . 
4 1 N2  ? D ZNI 201 ? PLANAR       . 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     149 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.101 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         19.6742 
_pdbx_refine_tls.origin_y         20.7605 
_pdbx_refine_tls.origin_z         21.5804 
_pdbx_refine_tls.T[1][1]          0.1924 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0208 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0160 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1910 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0046 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1609 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.8686 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.5369 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0324 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9634 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0235 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.5415 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.2308 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1955 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0116 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.2361 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.1273 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0306 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0152 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0131 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0851 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 458 ? 6.04  . 
2  1 O ? A HOH 459 ? 6.10  . 
3  1 O ? A HOH 460 ? 6.16  . 
4  1 O ? A HOH 461 ? 6.32  . 
5  1 O ? A HOH 462 ? 9.36  . 
6  1 O ? B HOH 485 ? 5.92  . 
7  1 O ? B HOH 486 ? 6.68  . 
8  1 O ? B HOH 487 ? 6.82  . 
9  1 O ? B HOH 488 ? 7.30  . 
10 1 O ? B HOH 489 ? 7.75  . 
11 1 O ? B HOH 490 ? 9.37  . 
12 1 O ? B HOH 491 ? 12.14 . 
13 1 O ? D HOH 453 ? 5.87  . 
14 1 O ? D HOH 454 ? 6.36  . 
15 1 O ? D HOH 455 ? 6.56  . 
16 1 O ? D HOH 456 ? 7.44  . 
17 1 O ? C HOH 410 ? 8.39  . 
# 
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 B GLY 0   ? B GLY 1   
2 1 Y 1 B MET 1   ? B MET 2   
3 1 Y 1 B GLU 165 ? B GLU 166 
4 1 Y 1 D GLY 0   ? C GLY 1   
5 1 Y 1 D MET 1   ? C MET 2   
6 1 Y 1 D GLU 165 ? C GLU 166 
7 1 Y 1 C GLU 168 ? D GLU 169 
8 1 Y 1 C LYS 169 ? D LYS 170 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GNP PG     P  N N 137 
GNP O1G    O  N N 138 
GNP O2G    O  N N 139 
GNP O3G    O  N N 140 
GNP N3B    N  N N 141 
GNP PB     P  N R 142 
GNP O1B    O  N N 143 
GNP O2B    O  N N 144 
GNP O3A    O  N N 145 
GNP PA     P  N S 146 
GNP O1A    O  N N 147 
GNP O2A    O  N N 148 
GNP "O5'"  O  N N 149 
GNP "C5'"  C  N N 150 
GNP "C4'"  C  N R 151 
GNP "O4'"  O  N N 152 
GNP "C3'"  C  N S 153 
GNP "O3'"  O  N N 154 
GNP "C2'"  C  N R 155 
GNP "O2'"  O  N N 156 
GNP "C1'"  C  N R 157 
GNP N9     N  Y N 158 
GNP C8     C  Y N 159 
GNP N7     N  Y N 160 
GNP C5     C  Y N 161 
GNP C6     C  Y N 162 
GNP O6     O  N N 163 
GNP N1     N  Y N 164 
GNP C2     C  Y N 165 
GNP N2     N  N N 166 
GNP N3     N  Y N 167 
GNP C4     C  Y N 168 
GNP HOG2   H  N N 169 
GNP HOG3   H  N N 170 
GNP HNB3   H  N N 171 
GNP HOB2   H  N N 172 
GNP HOA2   H  N N 173 
GNP "H5'2" H  N N 174 
GNP "H5'1" H  N N 175 
GNP "H4'"  H  N N 176 
GNP "H3'"  H  N N 177 
GNP "HO3'" H  N N 178 
GNP "H2'"  H  N N 179 
GNP "HO2'" H  N N 180 
GNP "H1'"  H  N N 181 
GNP H8     H  N N 182 
GNP HN1    H  N N 183 
GNP HN21   H  N N 184 
GNP HN22   H  N N 185 
HIS N      N  N N 186 
HIS CA     C  N S 187 
HIS C      C  N N 188 
HIS O      O  N N 189 
HIS CB     C  N N 190 
HIS CG     C  Y N 191 
HIS ND1    N  Y N 192 
HIS CD2    C  Y N 193 
HIS CE1    C  Y N 194 
HIS NE2    N  Y N 195 
HIS OXT    O  N N 196 
HIS H      H  N N 197 
HIS H2     H  N N 198 
HIS HA     H  N N 199 
HIS HB2    H  N N 200 
HIS HB3    H  N N 201 
HIS HD1    H  N N 202 
HIS HD2    H  N N 203 
HIS HE1    H  N N 204 
HIS HE2    H  N N 205 
HIS HXT    H  N N 206 
HOH O      O  N N 207 
HOH H1     H  N N 208 
HOH H2     H  N N 209 
ILE N      N  N N 210 
ILE CA     C  N S 211 
ILE C      C  N N 212 
ILE O      O  N N 213 
ILE CB     C  N S 214 
ILE CG1    C  N N 215 
ILE CG2    C  N N 216 
ILE CD1    C  N N 217 
ILE OXT    O  N N 218 
ILE H      H  N N 219 
ILE H2     H  N N 220 
ILE HA     H  N N 221 
ILE HB     H  N N 222 
ILE HG12   H  N N 223 
ILE HG13   H  N N 224 
ILE HG21   H  N N 225 
ILE HG22   H  N N 226 
ILE HG23   H  N N 227 
ILE HD11   H  N N 228 
ILE HD12   H  N N 229 
ILE HD13   H  N N 230 
ILE HXT    H  N N 231 
LEU N      N  N N 232 
LEU CA     C  N S 233 
LEU C      C  N N 234 
LEU O      O  N N 235 
LEU CB     C  N N 236 
LEU CG     C  N N 237 
LEU CD1    C  N N 238 
LEU CD2    C  N N 239 
LEU OXT    O  N N 240 
LEU H      H  N N 241 
LEU H2     H  N N 242 
LEU HA     H  N N 243 
LEU HB2    H  N N 244 
LEU HB3    H  N N 245 
LEU HG     H  N N 246 
LEU HD11   H  N N 247 
LEU HD12   H  N N 248 
LEU HD13   H  N N 249 
LEU HD21   H  N N 250 
LEU HD22   H  N N 251 
LEU HD23   H  N N 252 
LEU HXT    H  N N 253 
LYS N      N  N N 254 
LYS CA     C  N S 255 
LYS C      C  N N 256 
LYS O      O  N N 257 
LYS CB     C  N N 258 
LYS CG     C  N N 259 
LYS CD     C  N N 260 
LYS CE     C  N N 261 
LYS NZ     N  N N 262 
LYS OXT    O  N N 263 
LYS H      H  N N 264 
LYS H2     H  N N 265 
LYS HA     H  N N 266 
LYS HB2    H  N N 267 
LYS HB3    H  N N 268 
LYS HG2    H  N N 269 
LYS HG3    H  N N 270 
LYS HD2    H  N N 271 
LYS HD3    H  N N 272 
LYS HE2    H  N N 273 
LYS HE3    H  N N 274 
LYS HZ1    H  N N 275 
LYS HZ2    H  N N 276 
LYS HZ3    H  N N 277 
LYS HXT    H  N N 278 
MET N      N  N N 279 
MET CA     C  N S 280 
MET C      C  N N 281 
MET O      O  N N 282 
MET CB     C  N N 283 
MET CG     C  N N 284 
MET SD     S  N N 285 
MET CE     C  N N 286 
MET OXT    O  N N 287 
MET H      H  N N 288 
MET H2     H  N N 289 
MET HA     H  N N 290 
MET HB2    H  N N 291 
MET HB3    H  N N 292 
MET HG2    H  N N 293 
MET HG3    H  N N 294 
MET HE1    H  N N 295 
MET HE2    H  N N 296 
MET HE3    H  N N 297 
MET HXT    H  N N 298 
MG  MG     MG N N 299 
PHE N      N  N N 300 
PHE CA     C  N S 301 
PHE C      C  N N 302 
PHE O      O  N N 303 
PHE CB     C  N N 304 
PHE CG     C  Y N 305 
PHE CD1    C  Y N 306 
PHE CD2    C  Y N 307 
PHE CE1    C  Y N 308 
PHE CE2    C  Y N 309 
PHE CZ     C  Y N 310 
PHE OXT    O  N N 311 
PHE H      H  N N 312 
PHE H2     H  N N 313 
PHE HA     H  N N 314 
PHE HB2    H  N N 315 
PHE HB3    H  N N 316 
PHE HD1    H  N N 317 
PHE HD2    H  N N 318 
PHE HE1    H  N N 319 
PHE HE2    H  N N 320 
PHE HZ     H  N N 321 
PHE HXT    H  N N 322 
PRO N      N  N N 323 
PRO CA     C  N S 324 
PRO C      C  N N 325 
PRO O      O  N N 326 
PRO CB     C  N N 327 
PRO CG     C  N N 328 
PRO CD     C  N N 329 
PRO OXT    O  N N 330 
PRO H      H  N N 331 
PRO HA     H  N N 332 
PRO HB2    H  N N 333 
PRO HB3    H  N N 334 
PRO HG2    H  N N 335 
PRO HG3    H  N N 336 
PRO HD2    H  N N 337 
PRO HD3    H  N N 338 
PRO HXT    H  N N 339 
SER N      N  N N 340 
SER CA     C  N S 341 
SER C      C  N N 342 
SER O      O  N N 343 
SER CB     C  N N 344 
SER OG     O  N N 345 
SER OXT    O  N N 346 
SER H      H  N N 347 
SER H2     H  N N 348 
SER HA     H  N N 349 
SER HB2    H  N N 350 
SER HB3    H  N N 351 
SER HG     H  N N 352 
SER HXT    H  N N 353 
THR N      N  N N 354 
THR CA     C  N S 355 
THR C      C  N N 356 
THR O      O  N N 357 
THR CB     C  N R 358 
THR OG1    O  N N 359 
THR CG2    C  N N 360 
THR OXT    O  N N 361 
THR H      H  N N 362 
THR H2     H  N N 363 
THR HA     H  N N 364 
THR HB     H  N N 365 
THR HG1    H  N N 366 
THR HG21   H  N N 367 
THR HG22   H  N N 368 
THR HG23   H  N N 369 
THR HXT    H  N N 370 
TRP N      N  N N 371 
TRP CA     C  N S 372 
TRP C      C  N N 373 
TRP O      O  N N 374 
TRP CB     C  N N 375 
TRP CG     C  Y N 376 
TRP CD1    C  Y N 377 
TRP CD2    C  Y N 378 
TRP NE1    N  Y N 379 
TRP CE2    C  Y N 380 
TRP CE3    C  Y N 381 
TRP CZ2    C  Y N 382 
TRP CZ3    C  Y N 383 
TRP CH2    C  Y N 384 
TRP OXT    O  N N 385 
TRP H      H  N N 386 
TRP H2     H  N N 387 
TRP HA     H  N N 388 
TRP HB2    H  N N 389 
TRP HB3    H  N N 390 
TRP HD1    H  N N 391 
TRP HE1    H  N N 392 
TRP HE3    H  N N 393 
TRP HZ2    H  N N 394 
TRP HZ3    H  N N 395 
TRP HH2    H  N N 396 
TRP HXT    H  N N 397 
TYR N      N  N N 398 
TYR CA     C  N S 399 
TYR C      C  N N 400 
TYR O      O  N N 401 
TYR CB     C  N N 402 
TYR CG     C  Y N 403 
TYR CD1    C  Y N 404 
TYR CD2    C  Y N 405 
TYR CE1    C  Y N 406 
TYR CE2    C  Y N 407 
TYR CZ     C  Y N 408 
TYR OH     O  N N 409 
TYR OXT    O  N N 410 
TYR H      H  N N 411 
TYR H2     H  N N 412 
TYR HA     H  N N 413 
TYR HB2    H  N N 414 
TYR HB3    H  N N 415 
TYR HD1    H  N N 416 
TYR HD2    H  N N 417 
TYR HE1    H  N N 418 
TYR HE2    H  N N 419 
TYR HH     H  N N 420 
TYR HXT    H  N N 421 
VAL N      N  N N 422 
VAL CA     C  N S 423 
VAL C      C  N N 424 
VAL O      O  N N 425 
VAL CB     C  N N 426 
VAL CG1    C  N N 427 
VAL CG2    C  N N 428 
VAL OXT    O  N N 429 
VAL H      H  N N 430 
VAL H2     H  N N 431 
VAL HA     H  N N 432 
VAL HB     H  N N 433 
VAL HG11   H  N N 434 
VAL HG12   H  N N 435 
VAL HG13   H  N N 436 
VAL HG21   H  N N 437 
VAL HG22   H  N N 438 
VAL HG23   H  N N 439 
VAL HXT    H  N N 440 
ZNI C1     C  N N 441 
ZNI C10    C  N R 442 
ZNI C11    C  N N 443 
ZNI C12    C  N N 444 
ZNI C13    C  N N 445 
ZNI C14    C  Y N 446 
ZNI C15    C  Y N 447 
ZNI C16    C  Y N 448 
ZNI C17    C  Y N 449 
ZNI C18    C  Y N 450 
ZNI C19    C  Y N 451 
ZNI C2     C  N S 452 
ZNI C20    C  Y N 453 
ZNI C21    C  Y N 454 
ZNI C22    C  Y N 455 
ZNI C23    C  N N 456 
ZNI C24    C  N N 457 
ZNI C25    C  Y N 458 
ZNI C26    C  Y N 459 
ZNI C27    C  Y N 460 
ZNI C28    C  N S 461 
ZNI C29    C  N N 462 
ZNI C3     C  N N 463 
ZNI C30    C  N N 464 
ZNI C31    C  Y N 465 
ZNI C32    C  Y N 466 
ZNI C33    C  N N 467 
ZNI C34    C  N N 468 
ZNI C35    C  N N 469 
ZNI C36    C  N N 470 
ZNI C37    C  N N 471 
ZNI C38    C  N N 472 
ZNI C39    C  N N 473 
ZNI C4     C  N N 474 
ZNI C40    C  Y N 475 
ZNI C41    C  Y N 476 
ZNI C42    C  N N 477 
ZNI C43    C  N N 478 
ZNI C44    C  N N 479 
ZNI C45    C  N N 480 
ZNI C46    C  N N 481 
ZNI C47    C  N N 482 
ZNI C5     C  N N 483 
ZNI C6     C  N S 484 
ZNI C7     C  N N 485 
ZNI C8     C  N N 486 
ZNI C9     C  N S 487 
ZNI N1     N  N N 488 
ZNI N2     N  N S 489 
ZNI N3     N  N N 490 
ZNI N4     N  Y N 491 
ZNI N5     N  Y N 492 
ZNI N6     N  Y N 493 
ZNI N7     N  N N 494 
ZNI N8     N  N N 495 
ZNI O1     O  N N 496 
ZNI O2     O  N N 497 
ZNI O3     O  N N 498 
ZNI O4     O  N N 499 
ZNI O5     O  N N 500 
ZNI O6     O  N N 501 
ZNI S1     S  Y N 502 
ZNI H1     H  N N 503 
ZNI H2     H  N N 504 
ZNI H3     H  N N 505 
ZNI H4     H  N N 506 
ZNI H5     H  N N 507 
ZNI H6     H  N N 508 
ZNI H7     H  N N 509 
ZNI H8     H  N N 510 
ZNI H9     H  N N 511 
ZNI H10    H  N N 512 
ZNI H11    H  N N 513 
ZNI H12    H  N N 514 
ZNI H13    H  N N 515 
ZNI H14    H  N N 516 
ZNI H15    H  N N 517 
ZNI H16    H  N N 518 
ZNI H17    H  N N 519 
ZNI H18    H  N N 520 
ZNI H19    H  N N 521 
ZNI H20    H  N N 522 
ZNI H21    H  N N 523 
ZNI H22    H  N N 524 
ZNI H23    H  N N 525 
ZNI H24    H  N N 526 
ZNI H25    H  N N 527 
ZNI H26    H  N N 528 
ZNI H27    H  N N 529 
ZNI H28    H  N N 530 
ZNI H29    H  N N 531 
ZNI H30    H  N N 532 
ZNI H31    H  N N 533 
ZNI H32    H  N N 534 
ZNI H33    H  N N 535 
ZNI H34    H  N N 536 
ZNI H35    H  N N 537 
ZNI H36    H  N N 538 
ZNI H37    H  N N 539 
ZNI H38    H  N N 540 
ZNI H39    H  N N 541 
ZNI H40    H  N N 542 
ZNI H41    H  N N 543 
ZNI H42    H  N N 544 
ZNI H43    H  N N 545 
ZNI H44    H  N N 546 
ZNI H45    H  N N 547 
ZNI H46    H  N N 548 
ZNI H47    H  N N 549 
ZNI H48    H  N N 550 
ZNI H49    H  N N 551 
ZNI H50    H  N N 552 
ZNI H51    H  N N 553 
ZNI H52    H  N N 554 
ZNI H53    H  N N 555 
ZNI H54    H  N N 556 
ZNI H55    H  N N 557 
ZNI H56    H  N N 558 
ZNI H57    H  N N 559 
ZNI H58    H  N N 560 
ZNI H59    H  N N 561 
ZNI H60    H  N N 562 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GNP PG    O1G    doub N N 129 
GNP PG    O2G    sing N N 130 
GNP PG    O3G    sing N N 131 
GNP PG    N3B    sing N N 132 
GNP O2G   HOG2   sing N N 133 
GNP O3G   HOG3   sing N N 134 
GNP N3B   PB     sing N N 135 
GNP N3B   HNB3   sing N N 136 
GNP PB    O1B    doub N N 137 
GNP PB    O2B    sing N N 138 
GNP PB    O3A    sing N N 139 
GNP O2B   HOB2   sing N N 140 
GNP O3A   PA     sing N N 141 
GNP PA    O1A    doub N N 142 
GNP PA    O2A    sing N N 143 
GNP PA    "O5'"  sing N N 144 
GNP O2A   HOA2   sing N N 145 
GNP "O5'" "C5'"  sing N N 146 
GNP "C5'" "C4'"  sing N N 147 
GNP "C5'" "H5'2" sing N N 148 
GNP "C5'" "H5'1" sing N N 149 
GNP "C4'" "O4'"  sing N N 150 
GNP "C4'" "C3'"  sing N N 151 
GNP "C4'" "H4'"  sing N N 152 
GNP "O4'" "C1'"  sing N N 153 
GNP "C3'" "O3'"  sing N N 154 
GNP "C3'" "C2'"  sing N N 155 
GNP "C3'" "H3'"  sing N N 156 
GNP "O3'" "HO3'" sing N N 157 
GNP "C2'" "O2'"  sing N N 158 
GNP "C2'" "C1'"  sing N N 159 
GNP "C2'" "H2'"  sing N N 160 
GNP "O2'" "HO2'" sing N N 161 
GNP "C1'" N9     sing N N 162 
GNP "C1'" "H1'"  sing N N 163 
GNP N9    C8     sing Y N 164 
GNP N9    C4     sing Y N 165 
GNP C8    N7     doub Y N 166 
GNP C8    H8     sing N N 167 
GNP N7    C5     sing Y N 168 
GNP C5    C6     sing Y N 169 
GNP C5    C4     doub Y N 170 
GNP C6    O6     doub N N 171 
GNP C6    N1     sing Y N 172 
GNP N1    C2     sing Y N 173 
GNP N1    HN1    sing N N 174 
GNP C2    N2     sing N N 175 
GNP C2    N3     doub Y N 176 
GNP N2    HN21   sing N N 177 
GNP N2    HN22   sing N N 178 
GNP N3    C4     sing Y N 179 
HIS N     CA     sing N N 180 
HIS N     H      sing N N 181 
HIS N     H2     sing N N 182 
HIS CA    C      sing N N 183 
HIS CA    CB     sing N N 184 
HIS CA    HA     sing N N 185 
HIS C     O      doub N N 186 
HIS C     OXT    sing N N 187 
HIS CB    CG     sing N N 188 
HIS CB    HB2    sing N N 189 
HIS CB    HB3    sing N N 190 
HIS CG    ND1    sing Y N 191 
HIS CG    CD2    doub Y N 192 
HIS ND1   CE1    doub Y N 193 
HIS ND1   HD1    sing N N 194 
HIS CD2   NE2    sing Y N 195 
HIS CD2   HD2    sing N N 196 
HIS CE1   NE2    sing Y N 197 
HIS CE1   HE1    sing N N 198 
HIS NE2   HE2    sing N N 199 
HIS OXT   HXT    sing N N 200 
HOH O     H1     sing N N 201 
HOH O     H2     sing N N 202 
ILE N     CA     sing N N 203 
ILE N     H      sing N N 204 
ILE N     H2     sing N N 205 
ILE CA    C      sing N N 206 
ILE CA    CB     sing N N 207 
ILE CA    HA     sing N N 208 
ILE C     O      doub N N 209 
ILE C     OXT    sing N N 210 
ILE CB    CG1    sing N N 211 
ILE CB    CG2    sing N N 212 
ILE CB    HB     sing N N 213 
ILE CG1   CD1    sing N N 214 
ILE CG1   HG12   sing N N 215 
ILE CG1   HG13   sing N N 216 
ILE CG2   HG21   sing N N 217 
ILE CG2   HG22   sing N N 218 
ILE CG2   HG23   sing N N 219 
ILE CD1   HD11   sing N N 220 
ILE CD1   HD12   sing N N 221 
ILE CD1   HD13   sing N N 222 
ILE OXT   HXT    sing N N 223 
LEU N     CA     sing N N 224 
LEU N     H      sing N N 225 
LEU N     H2     sing N N 226 
LEU CA    C      sing N N 227 
LEU CA    CB     sing N N 228 
LEU CA    HA     sing N N 229 
LEU C     O      doub N N 230 
LEU C     OXT    sing N N 231 
LEU CB    CG     sing N N 232 
LEU CB    HB2    sing N N 233 
LEU CB    HB3    sing N N 234 
LEU CG    CD1    sing N N 235 
LEU CG    CD2    sing N N 236 
LEU CG    HG     sing N N 237 
LEU CD1   HD11   sing N N 238 
LEU CD1   HD12   sing N N 239 
LEU CD1   HD13   sing N N 240 
LEU CD2   HD21   sing N N 241 
LEU CD2   HD22   sing N N 242 
LEU CD2   HD23   sing N N 243 
LEU OXT   HXT    sing N N 244 
LYS N     CA     sing N N 245 
LYS N     H      sing N N 246 
LYS N     H2     sing N N 247 
LYS CA    C      sing N N 248 
LYS CA    CB     sing N N 249 
LYS CA    HA     sing N N 250 
LYS C     O      doub N N 251 
LYS C     OXT    sing N N 252 
LYS CB    CG     sing N N 253 
LYS CB    HB2    sing N N 254 
LYS CB    HB3    sing N N 255 
LYS CG    CD     sing N N 256 
LYS CG    HG2    sing N N 257 
LYS CG    HG3    sing N N 258 
LYS CD    CE     sing N N 259 
LYS CD    HD2    sing N N 260 
LYS CD    HD3    sing N N 261 
LYS CE    NZ     sing N N 262 
LYS CE    HE2    sing N N 263 
LYS CE    HE3    sing N N 264 
LYS NZ    HZ1    sing N N 265 
LYS NZ    HZ2    sing N N 266 
LYS NZ    HZ3    sing N N 267 
LYS OXT   HXT    sing N N 268 
MET N     CA     sing N N 269 
MET N     H      sing N N 270 
MET N     H2     sing N N 271 
MET CA    C      sing N N 272 
MET CA    CB     sing N N 273 
MET CA    HA     sing N N 274 
MET C     O      doub N N 275 
MET C     OXT    sing N N 276 
MET CB    CG     sing N N 277 
MET CB    HB2    sing N N 278 
MET CB    HB3    sing N N 279 
MET CG    SD     sing N N 280 
MET CG    HG2    sing N N 281 
MET CG    HG3    sing N N 282 
MET SD    CE     sing N N 283 
MET CE    HE1    sing N N 284 
MET CE    HE2    sing N N 285 
MET CE    HE3    sing N N 286 
MET OXT   HXT    sing N N 287 
PHE N     CA     sing N N 288 
PHE N     H      sing N N 289 
PHE N     H2     sing N N 290 
PHE CA    C      sing N N 291 
PHE CA    CB     sing N N 292 
PHE CA    HA     sing N N 293 
PHE C     O      doub N N 294 
PHE C     OXT    sing N N 295 
PHE CB    CG     sing N N 296 
PHE CB    HB2    sing N N 297 
PHE CB    HB3    sing N N 298 
PHE CG    CD1    doub Y N 299 
PHE CG    CD2    sing Y N 300 
PHE CD1   CE1    sing Y N 301 
PHE CD1   HD1    sing N N 302 
PHE CD2   CE2    doub Y N 303 
PHE CD2   HD2    sing N N 304 
PHE CE1   CZ     doub Y N 305 
PHE CE1   HE1    sing N N 306 
PHE CE2   CZ     sing Y N 307 
PHE CE2   HE2    sing N N 308 
PHE CZ    HZ     sing N N 309 
PHE OXT   HXT    sing N N 310 
PRO N     CA     sing N N 311 
PRO N     CD     sing N N 312 
PRO N     H      sing N N 313 
PRO CA    C      sing N N 314 
PRO CA    CB     sing N N 315 
PRO CA    HA     sing N N 316 
PRO C     O      doub N N 317 
PRO C     OXT    sing N N 318 
PRO CB    CG     sing N N 319 
PRO CB    HB2    sing N N 320 
PRO CB    HB3    sing N N 321 
PRO CG    CD     sing N N 322 
PRO CG    HG2    sing N N 323 
PRO CG    HG3    sing N N 324 
PRO CD    HD2    sing N N 325 
PRO CD    HD3    sing N N 326 
PRO OXT   HXT    sing N N 327 
SER N     CA     sing N N 328 
SER N     H      sing N N 329 
SER N     H2     sing N N 330 
SER CA    C      sing N N 331 
SER CA    CB     sing N N 332 
SER CA    HA     sing N N 333 
SER C     O      doub N N 334 
SER C     OXT    sing N N 335 
SER CB    OG     sing N N 336 
SER CB    HB2    sing N N 337 
SER CB    HB3    sing N N 338 
SER OG    HG     sing N N 339 
SER OXT   HXT    sing N N 340 
THR N     CA     sing N N 341 
THR N     H      sing N N 342 
THR N     H2     sing N N 343 
THR CA    C      sing N N 344 
THR CA    CB     sing N N 345 
THR CA    HA     sing N N 346 
THR C     O      doub N N 347 
THR C     OXT    sing N N 348 
THR CB    OG1    sing N N 349 
THR CB    CG2    sing N N 350 
THR CB    HB     sing N N 351 
THR OG1   HG1    sing N N 352 
THR CG2   HG21   sing N N 353 
THR CG2   HG22   sing N N 354 
THR CG2   HG23   sing N N 355 
THR OXT   HXT    sing N N 356 
TRP N     CA     sing N N 357 
TRP N     H      sing N N 358 
TRP N     H2     sing N N 359 
TRP CA    C      sing N N 360 
TRP CA    CB     sing N N 361 
TRP CA    HA     sing N N 362 
TRP C     O      doub N N 363 
TRP C     OXT    sing N N 364 
TRP CB    CG     sing N N 365 
TRP CB    HB2    sing N N 366 
TRP CB    HB3    sing N N 367 
TRP CG    CD1    doub Y N 368 
TRP CG    CD2    sing Y N 369 
TRP CD1   NE1    sing Y N 370 
TRP CD1   HD1    sing N N 371 
TRP CD2   CE2    doub Y N 372 
TRP CD2   CE3    sing Y N 373 
TRP NE1   CE2    sing Y N 374 
TRP NE1   HE1    sing N N 375 
TRP CE2   CZ2    sing Y N 376 
TRP CE3   CZ3    doub Y N 377 
TRP CE3   HE3    sing N N 378 
TRP CZ2   CH2    doub Y N 379 
TRP CZ2   HZ2    sing N N 380 
TRP CZ3   CH2    sing Y N 381 
TRP CZ3   HZ3    sing N N 382 
TRP CH2   HH2    sing N N 383 
TRP OXT   HXT    sing N N 384 
TYR N     CA     sing N N 385 
TYR N     H      sing N N 386 
TYR N     H2     sing N N 387 
TYR CA    C      sing N N 388 
TYR CA    CB     sing N N 389 
TYR CA    HA     sing N N 390 
TYR C     O      doub N N 391 
TYR C     OXT    sing N N 392 
TYR CB    CG     sing N N 393 
TYR CB    HB2    sing N N 394 
TYR CB    HB3    sing N N 395 
TYR CG    CD1    doub Y N 396 
TYR CG    CD2    sing Y N 397 
TYR CD1   CE1    sing Y N 398 
TYR CD1   HD1    sing N N 399 
TYR CD2   CE2    doub Y N 400 
TYR CD2   HD2    sing N N 401 
TYR CE1   CZ     doub Y N 402 
TYR CE1   HE1    sing N N 403 
TYR CE2   CZ     sing Y N 404 
TYR CE2   HE2    sing N N 405 
TYR CZ    OH     sing N N 406 
TYR OH    HH     sing N N 407 
TYR OXT   HXT    sing N N 408 
VAL N     CA     sing N N 409 
VAL N     H      sing N N 410 
VAL N     H2     sing N N 411 
VAL CA    C      sing N N 412 
VAL CA    CB     sing N N 413 
VAL CA    HA     sing N N 414 
VAL C     O      doub N N 415 
VAL C     OXT    sing N N 416 
VAL CB    CG1    sing N N 417 
VAL CB    CG2    sing N N 418 
VAL CB    HB     sing N N 419 
VAL CG1   HG11   sing N N 420 
VAL CG1   HG12   sing N N 421 
VAL CG1   HG13   sing N N 422 
VAL CG2   HG21   sing N N 423 
VAL CG2   HG22   sing N N 424 
VAL CG2   HG23   sing N N 425 
VAL OXT   HXT    sing N N 426 
ZNI C30   C28    sing N N 427 
ZNI C44   C43    sing N N 428 
ZNI C29   O4     sing N N 429 
ZNI C28   O4     sing N N 430 
ZNI C28   C27    sing N N 431 
ZNI N6    C27    doub Y N 432 
ZNI N6    C31    sing Y N 433 
ZNI C45   C43    sing N N 434 
ZNI O6    C47    doub N N 435 
ZNI C46   C43    sing N N 436 
ZNI C46   O5     sing N N 437 
ZNI C43   C42    sing N N 438 
ZNI C27   C26    sing Y N 439 
ZNI C31   C32    doub Y N 440 
ZNI C47   O5     sing N N 441 
ZNI C47   C2     sing N N 442 
ZNI C1    C4     sing N N 443 
ZNI C1    C2     sing N N 444 
ZNI C3    C4     sing N N 445 
ZNI C3    N2     sing N N 446 
ZNI C32   N7     sing N N 447 
ZNI C32   C40    sing Y N 448 
ZNI N1    C2     sing N N 449 
ZNI N1    N2     sing N N 450 
ZNI C26   C40    doub Y N 451 
ZNI C26   C25    sing N N 452 
ZNI C39   C38    sing N N 453 
ZNI C39   N7     sing N N 454 
ZNI C42   C41    sing N N 455 
ZNI C38   N8     sing N N 456 
ZNI N7    C33    sing N N 457 
ZNI N2    C5     sing N N 458 
ZNI C25   C41    doub Y N 459 
ZNI C25   N5     sing Y N 460 
ZNI C41   C19    sing Y N 461 
ZNI O2    C7     doub N N 462 
ZNI N5    C23    sing N N 463 
ZNI N5    C20    sing Y N 464 
ZNI C19   C20    doub Y N 465 
ZNI C19   C18    sing Y N 466 
ZNI C23   C24    sing N N 467 
ZNI N8    C35    sing N N 468 
ZNI N8    C34    sing N N 469 
ZNI C5    O1     doub N N 470 
ZNI C5    C6     sing N N 471 
ZNI C35   C37    sing N N 472 
ZNI C35   C36    sing N N 473 
ZNI C33   C34    sing N N 474 
ZNI C20   C21    sing Y N 475 
ZNI C18   C17    doub Y N 476 
ZNI C9    C10    sing N N 477 
ZNI C9    C12    sing N N 478 
ZNI C9    C8     sing N N 479 
ZNI C7    N3     sing N N 480 
ZNI C7    C8     sing N N 481 
ZNI C37   C36    sing N N 482 
ZNI C6    N3     sing N N 483 
ZNI C6    C13    sing N N 484 
ZNI C21   C22    doub Y N 485 
ZNI C10   C8     sing N N 486 
ZNI C10   C11    sing N N 487 
ZNI C17   C22    sing Y N 488 
ZNI C17   C15    sing N N 489 
ZNI C12   O3     sing N N 490 
ZNI N4    C15    sing Y N 491 
ZNI N4    C14    doub Y N 492 
ZNI C15   C16    doub Y N 493 
ZNI C14   C13    sing N N 494 
ZNI C14   S1     sing Y N 495 
ZNI C16   S1     sing Y N 496 
ZNI C11   O3     sing N N 497 
ZNI C1    H1     sing N N 498 
ZNI C1    H2     sing N N 499 
ZNI C10   H3     sing N N 500 
ZNI C11   H4     sing N N 501 
ZNI C11   H5     sing N N 502 
ZNI C12   H6     sing N N 503 
ZNI C12   H7     sing N N 504 
ZNI C13   H8     sing N N 505 
ZNI C13   H9     sing N N 506 
ZNI C16   H10    sing N N 507 
ZNI C18   H11    sing N N 508 
ZNI C2    H12    sing N N 509 
ZNI C21   H13    sing N N 510 
ZNI C22   H14    sing N N 511 
ZNI C23   H15    sing N N 512 
ZNI C23   H16    sing N N 513 
ZNI C24   H17    sing N N 514 
ZNI C24   H18    sing N N 515 
ZNI C24   H19    sing N N 516 
ZNI C28   H20    sing N N 517 
ZNI C29   H21    sing N N 518 
ZNI C29   H22    sing N N 519 
ZNI C29   H23    sing N N 520 
ZNI C3    H24    sing N N 521 
ZNI C3    H25    sing N N 522 
ZNI C30   H26    sing N N 523 
ZNI C30   H27    sing N N 524 
ZNI C30   H28    sing N N 525 
ZNI C31   H29    sing N N 526 
ZNI C33   H30    sing N N 527 
ZNI C33   H31    sing N N 528 
ZNI C34   H32    sing N N 529 
ZNI C34   H33    sing N N 530 
ZNI C35   H34    sing N N 531 
ZNI C36   H35    sing N N 532 
ZNI C36   H36    sing N N 533 
ZNI C37   H37    sing N N 534 
ZNI C37   H38    sing N N 535 
ZNI C38   H39    sing N N 536 
ZNI C38   H40    sing N N 537 
ZNI C39   H41    sing N N 538 
ZNI C39   H42    sing N N 539 
ZNI C4    H43    sing N N 540 
ZNI C4    H44    sing N N 541 
ZNI C40   H45    sing N N 542 
ZNI C42   H46    sing N N 543 
ZNI C42   H47    sing N N 544 
ZNI C44   H48    sing N N 545 
ZNI C44   H49    sing N N 546 
ZNI C44   H50    sing N N 547 
ZNI C45   H51    sing N N 548 
ZNI C45   H52    sing N N 549 
ZNI C45   H53    sing N N 550 
ZNI C46   H54    sing N N 551 
ZNI C46   H55    sing N N 552 
ZNI C6    H56    sing N N 553 
ZNI C8    H57    sing N N 554 
ZNI C9    H58    sing N N 555 
ZNI N1    H59    sing N N 556 
ZNI N3    H60    sing N N 557 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   9BGH 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BI1 
_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]   0.015263 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012187 
_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]   0.007818 
_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 
C  
H  
MG 
N  
O  
P  
S  
# 
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      . GLY A 1 1   ? 28.761  42.645  29.539  1.00 52.46  ? 0   GLY A N      1 
ATOM   2     C  CA     . GLY A 1 1   ? 28.204  41.579  28.644  1.00 50.00  ? 0   GLY A CA     1 
ATOM   3     C  C      . GLY A 1 1   ? 27.537  42.161  27.420  1.00 44.77  ? 0   GLY A C      1 
ATOM   4     O  O      . GLY A 1 1   ? 27.194  43.343  27.394  1.00 48.20  ? 0   GLY A O      1 
ATOM   5     H  H1     . GLY A 1 1   ? 29.650  42.618  29.515  1.00 62.98  ? 0   GLY A H1     1 
ATOM   6     H  H2     . GLY A 1 1   ? 28.481  43.442  29.260  1.00 62.98  ? 0   GLY A H2     1 
ATOM   7     H  H3     . GLY A 1 1   ? 28.482  42.508  30.373  1.00 62.98  ? 0   GLY A H3     1 
ATOM   8     H  HA2    . GLY A 1 1   ? 28.922  40.994  28.355  1.00 60.03  ? 0   GLY A HA2    1 
ATOM   9     H  HA3    . GLY A 1 1   ? 27.549  41.057  29.133  1.00 60.03  ? 0   GLY A HA3    1 
ATOM   10    N  N      . MET A 1 2   ? 27.368  41.347  26.383  1.00 43.20  ? 1   MET A N      1 
ATOM   11    C  CA     . MET A 1 2   ? 26.690  41.820  25.192  1.00 40.64  ? 1   MET A CA     1 
ATOM   12    C  C      . MET A 1 2   ? 25.205  41.558  25.323  1.00 35.44  ? 1   MET A C      1 
ATOM   13    O  O      . MET A 1 2   ? 24.764  40.635  26.007  1.00 40.06  ? 1   MET A O      1 
ATOM   14    C  CB     . MET A 1 2   ? 27.211  41.157  23.907  1.00 38.75  ? 1   MET A CB     1 
ATOM   15    C  CG     . MET A 1 2   ? 27.431  39.671  23.951  1.00 32.35  ? 1   MET A CG     1 
ATOM   16    S  SD     . MET A 1 2   ? 27.865  39.046  22.299  1.00 35.64  ? 1   MET A SD     1 
ATOM   17    C  CE     . MET A 1 2   ? 29.584  38.575  22.511  1.00 34.79  ? 1   MET A CE     1 
ATOM   18    H  H      . MET A 1 2   ? 27.634  40.530  26.350  1.00 51.87  ? 1   MET A H      1 
ATOM   19    H  HA     . MET A 1 2   ? 26.867  42.769  25.101  1.00 48.80  ? 1   MET A HA     1 
ATOM   20    H  HB2    . MET A 1 2   ? 26.569  41.328  23.201  1.00 46.53  ? 1   MET A HB2    1 
ATOM   21    H  HB3    . MET A 1 2   ? 28.064  41.563  23.686  1.00 46.53  ? 1   MET A HB3    1 
ATOM   22    H  HG2    . MET A 1 2   ? 28.158  39.467  24.560  1.00 38.86  ? 1   MET A HG2    1 
ATOM   23    H  HG3    . MET A 1 2   ? 26.619  39.230  24.245  1.00 38.86  ? 1   MET A HG3    1 
ATOM   24    H  HE1    . MET A 1 2   ? 29.923  38.233  21.669  1.00 41.78  ? 1   MET A HE1    1 
ATOM   25    H  HE2    . MET A 1 2   ? 30.094  39.355  22.780  1.00 41.78  ? 1   MET A HE2    1 
ATOM   26    H  HE3    . MET A 1 2   ? 29.641  37.890  23.195  1.00 41.78  ? 1   MET A HE3    1 
ATOM   27    N  N      . THR A 1 3   ? 24.433  42.372  24.643  1.00 38.60  ? 2   THR A N      1 
ATOM   28    C  CA     . THR A 1 3   ? 22.993  42.234  24.689  1.00 33.78  ? 2   THR A CA     1 
ATOM   29    C  C      . THR A 1 3   ? 22.583  41.052  23.824  1.00 36.02  ? 2   THR A C      1 
ATOM   30    O  O      . THR A 1 3   ? 23.164  40.818  22.759  1.00 31.87  ? 2   THR A O      1 
ATOM   31    C  CB     . THR A 1 3   ? 22.349  43.520  24.196  1.00 35.90  ? 2   THR A CB     1 
ATOM   32    O  OG1    . THR A 1 3   ? 22.781  44.602  25.035  1.00 41.44  ? 2   THR A OG1    1 
ATOM   33    C  CG2    . THR A 1 3   ? 20.864  43.401  24.260  1.00 38.01  ? 2   THR A CG2    1 
ATOM   34    H  H      . THR A 1 3   ? 24.715  43.014  24.145  1.00 46.36  ? 2   THR A H      1 
ATOM   35    H  HA     . THR A 1 3   ? 22.680  42.073  25.593  1.00 40.56  ? 2   THR A HA     1 
ATOM   36    H  HB     . THR A 1 3   ? 22.604  43.696  23.277  1.00 43.11  ? 2   THR A HB     1 
ATOM   37    H  HG1    . THR A 1 3   ? 22.438  45.323  24.772  1.00 49.76  ? 2   THR A HG1    1 
ATOM   38    H  HG21   . THR A 1 3   ? 20.457  44.276  24.158  1.00 45.65  ? 2   THR A HG21   1 
ATOM   39    H  HG22   . THR A 1 3   ? 20.547  42.822  23.550  1.00 45.65  ? 2   THR A HG22   1 
ATOM   40    H  HG23   . THR A 1 3   ? 20.598  43.027  25.114  1.00 45.65  ? 2   THR A HG23   1 
ATOM   41    N  N      . GLU A 1 4   ? 21.616  40.291  24.303  1.00 35.00  ? 3   GLU A N      1 
ATOM   42    C  CA     . GLU A 1 4   ? 21.089  39.143  23.575  1.00 35.07  ? 3   GLU A CA     1 
ATOM   43    C  C      . GLU A 1 4   ? 19.745  39.552  22.993  1.00 31.12  ? 3   GLU A C      1 
ATOM   44    O  O      . GLU A 1 4   ? 18.968  40.257  23.630  1.00 31.27  ? 3   GLU A O      1 
ATOM   45    C  CB     . GLU A 1 4   ? 20.956  37.921  24.492  1.00 35.88  ? 3   GLU A CB     1 
ATOM   46    C  CG     . GLU A 1 4   ? 20.311  36.687  23.823  1.00 41.85  ? 3   GLU A CG     1 
ATOM   47    C  CD     . GLU A 1 4   ? 19.526  35.830  24.815  1.00 42.70  ? 3   GLU A CD     1 
ATOM   48    O  OE1    . GLU A 1 4   ? 18.830  34.871  24.387  1.00 38.31  ? 3   GLU A OE1    1 
ATOM   49    O  OE2    . GLU A 1 4   ? 19.635  36.099  26.029  1.00 45.10  ? 3   GLU A OE2    1 
ATOM   50    H  H      . GLU A 1 4   ? 21.238  40.419  25.065  1.00 42.04  ? 3   GLU A H      1 
ATOM   51    H  HA     . GLU A 1 4   ? 21.680  38.876  22.853  1.00 42.12  ? 3   GLU A HA     1 
ATOM   52    H  HB2    . GLU A 1 4   ? 21.841  37.663  24.793  1.00 43.09  ? 3   GLU A HB2    1 
ATOM   53    H  HB3    . GLU A 1 4   ? 20.404  38.164  25.253  1.00 43.09  ? 3   GLU A HB3    1 
ATOM   54    H  HG2    . GLU A 1 4   ? 19.700  36.984  23.131  1.00 50.25  ? 3   GLU A HG2    1 
ATOM   55    H  HG3    . GLU A 1 4   ? 21.009  36.136  23.436  1.00 50.25  ? 3   GLU A HG3    1 
ATOM   56    N  N      . TYR A 1 5   ? 19.483  39.140  21.767  1.00 28.19  ? 4   TYR A N      1 
ATOM   57    C  CA     . TYR A 1 5   ? 18.272  39.522  21.057  1.00 29.72  ? 4   TYR A CA     1 
ATOM   58    C  C      . TYR A 1 5   ? 17.566  38.240  20.634  1.00 29.95  ? 4   TYR A C      1 
ATOM   59    O  O      . TYR A 1 5   ? 18.162  37.403  19.943  1.00 26.61  ? 4   TYR A O      1 
ATOM   60    C  CB     . TYR A 1 5   ? 18.597  40.366  19.830  1.00 29.90  ? 4   TYR A CB     1 
ATOM   61    C  CG     . TYR A 1 5   ? 19.158  41.724  20.149  1.00 30.31  ? 4   TYR A CG     1 
ATOM   62    C  CD1    . TYR A 1 5   ? 18.308  42.779  20.437  1.00 34.93  ? 4   TYR A CD1    1 
ATOM   63    C  CD2    . TYR A 1 5   ? 20.531  41.960  20.151  1.00 32.85  ? 4   TYR A CD2    1 
ATOM   64    C  CE1    . TYR A 1 5   ? 18.795  44.024  20.721  1.00 34.05  ? 4   TYR A CE1    1 
ATOM   65    C  CE2    . TYR A 1 5   ? 21.030  43.233  20.447  1.00 35.36  ? 4   TYR A CE2    1 
ATOM   66    C  CZ     . TYR A 1 5   ? 20.136  44.254  20.738  1.00 34.80  ? 4   TYR A CZ     1 
ATOM   67    O  OH     . TYR A 1 5   ? 20.569  45.534  21.051  1.00 36.47  ? 4   TYR A OH     1 
ATOM   68    H  H      . TYR A 1 5   ? 20.002  38.627  21.313  1.00 33.86  ? 4   TYR A H      1 
ATOM   69    H  HA     . TYR A 1 5   ? 17.693  40.039  21.639  1.00 35.70  ? 4   TYR A HA     1 
ATOM   70    H  HB2    . TYR A 1 5   ? 19.253  39.894  19.294  1.00 35.92  ? 4   TYR A HB2    1 
ATOM   71    H  HB3    . TYR A 1 5   ? 17.783  40.496  19.319  1.00 35.92  ? 4   TYR A HB3    1 
ATOM   72    H  HD1    . TYR A 1 5   ? 17.389  42.637  20.437  1.00 41.95  ? 4   TYR A HD1    1 
ATOM   73    H  HD2    . TYR A 1 5   ? 21.119  41.268  19.954  1.00 39.46  ? 4   TYR A HD2    1 
ATOM   74    H  HE1    . TYR A 1 5   ? 18.205  44.719  20.905  1.00 40.90  ? 4   TYR A HE1    1 
ATOM   75    H  HE2    . TYR A 1 5   ? 21.946  43.393  20.450  1.00 42.47  ? 4   TYR A HE2    1 
ATOM   76    H  HH     . TYR A 1 5   ? 21.407  45.574  20.999  1.00 43.80  ? 4   TYR A HH     1 
ATOM   77    N  N      . LYS A 1 6   ? 16.311  38.087  21.036  1.00 26.85  ? 5   LYS A N      1 
ATOM   78    C  CA     . LYS A 1 6   ? 15.576  36.847  20.808  1.00 27.07  ? 5   LYS A CA     1 
ATOM   79    C  C      . LYS A 1 6   ? 14.720  36.999  19.554  1.00 24.47  ? 5   LYS A C      1 
ATOM   80    O  O      . LYS A 1 6   ? 13.653  37.630  19.571  1.00 24.37  ? 5   LYS A O      1 
ATOM   81    C  CB     . LYS A 1 6   ? 14.748  36.491  22.036  1.00 27.50  ? 5   LYS A CB     1 
ATOM   82    C  CG     . LYS A 1 6   ? 15.577  36.211  23.281  1.00 31.77  ? 5   LYS A CG     1 
ATOM   83    C  CD     . LYS A 1 6   ? 14.652  35.963  24.485  1.00 38.22  ? 5   LYS A CD     1 
ATOM   84    C  CE     . LYS A 1 6   ? 15.278  36.402  25.802  1.00 43.28  ? 5   LYS A CE     1 
ATOM   85    N  NZ     . LYS A 1 6   ? 16.419  35.506  26.148  1.00 50.55  ? 5   LYS A NZ     1 
ATOM   86    H  H      . LYS A 1 6   ? 15.859  38.692  21.447  1.00 32.25  ? 5   LYS A H      1 
ATOM   87    H  HA     . LYS A 1 6   ? 16.205  36.128  20.639  1.00 32.52  ? 5   LYS A HA     1 
ATOM   88    H  HB2    . LYS A 1 6   ? 14.155  37.231  22.237  1.00 33.04  ? 5   LYS A HB2    1 
ATOM   89    H  HB3    . LYS A 1 6   ? 14.230  35.694  21.841  1.00 33.04  ? 5   LYS A HB3    1 
ATOM   90    H  HG2    . LYS A 1 6   ? 16.123  35.421  23.140  1.00 38.16  ? 5   LYS A HG2    1 
ATOM   91    H  HG3    . LYS A 1 6   ? 16.143  36.974  23.476  1.00 38.16  ? 5   LYS A HG3    1 
ATOM   92    H  HD2    . LYS A 1 6   ? 13.830  36.462  24.362  1.00 45.89  ? 5   LYS A HD2    1 
ATOM   93    H  HD3    . LYS A 1 6   ? 14.458  35.014  24.546  1.00 45.89  ? 5   LYS A HD3    1 
ATOM   94    H  HE2    . LYS A 1 6   ? 15.609  37.310  25.720  1.00 51.97  ? 5   LYS A HE2    1 
ATOM   95    H  HE3    . LYS A 1 6   ? 14.617  36.353  26.511  1.00 51.97  ? 5   LYS A HE3    1 
ATOM   96    H  HZ1    . LYS A 1 6   ? 17.031  35.529  25.502  1.00 60.69  ? 5   LYS A HZ1    1 
ATOM   97    H  HZ2    . LYS A 1 6   ? 16.794  35.772  26.910  1.00 60.69  ? 5   LYS A HZ2    1 
ATOM   98    H  HZ3    . LYS A 1 6   ? 16.131  34.670  26.244  1.00 60.69  ? 5   LYS A HZ3    1 
ATOM   99    N  N      . LEU A 1 7   ? 15.238  36.475  18.448  1.00 21.33  ? 6   LEU A N      1 
ATOM   100   C  CA     . LEU A 1 7   ? 14.607  36.544  17.136  1.00 21.94  ? 6   LEU A CA     1 
ATOM   101   C  C      . LEU A 1 7   ? 13.889  35.232  16.852  1.00 21.04  ? 6   LEU A C      1 
ATOM   102   O  O      . LEU A 1 7   ? 14.380  34.161  17.207  1.00 22.20  ? 6   LEU A O      1 
ATOM   103   C  CB     . LEU A 1 7   ? 15.657  36.788  16.055  1.00 21.28  ? 6   LEU A CB     1 
ATOM   104   C  CG     . LEU A 1 7   ? 16.706  37.865  16.355  1.00 24.35  ? 6   LEU A CG     1 
ATOM   105   C  CD1    . LEU A 1 7   ? 17.598  38.127  15.135  1.00 26.57  ? 6   LEU A CD1    1 
ATOM   106   C  CD2    . LEU A 1 7   ? 16.101  39.139  16.821  1.00 24.39  ? 6   LEU A CD2    1 
ATOM   107   H  H      . LEU A 1 7   ? 15.988  36.055  18.432  1.00 25.63  ? 6   LEU A H      1 
ATOM   108   H  HA     . LEU A 1 7   ? 13.962  37.269  17.116  1.00 26.37  ? 6   LEU A HA     1 
ATOM   109   H  HB2    . LEU A 1 7   ? 16.135  35.957  15.906  1.00 25.57  ? 6   LEU A HB2    1 
ATOM   110   H  HB3    . LEU A 1 7   ? 15.198  37.056  15.243  1.00 25.57  ? 6   LEU A HB3    1 
ATOM   111   H  HG     . LEU A 1 7   ? 17.257  37.525  17.077  1.00 29.26  ? 6   LEU A HG     1 
ATOM   112   H  HD11   . LEU A 1 7   ? 18.480  38.390  15.439  1.00 31.92  ? 6   LEU A HD11   1 
ATOM   113   H  HD12   . LEU A 1 7   ? 17.659  37.314  14.608  1.00 31.92  ? 6   LEU A HD12   1 
ATOM   114   H  HD13   . LEU A 1 7   ? 17.205  38.837  14.603  1.00 31.92  ? 6   LEU A HD13   1 
ATOM   115   H  HD21   . LEU A 1 7   ? 16.784  39.827  16.834  1.00 29.30  ? 6   LEU A HD21   1 
ATOM   116   H  HD22   . LEU A 1 7   ? 15.388  39.391  16.213  1.00 29.30  ? 6   LEU A HD22   1 
ATOM   117   H  HD23   . LEU A 1 7   ? 15.743  39.011  17.714  1.00 29.30  ? 6   LEU A HD23   1 
ATOM   118   N  N      . VAL A 1 8   ? 12.723  35.322  16.212  1.00 19.55  ? 7   VAL A N      1 
ATOM   119   C  CA     . VAL A 1 8   ? 11.891  34.166  15.899  1.00 18.53  ? 7   VAL A CA     1 
ATOM   120   C  C      . VAL A 1 8   ? 11.531  34.248  14.419  1.00 18.97  ? 7   VAL A C      1 
ATOM   121   O  O      . VAL A 1 8   ? 11.064  35.301  13.951  1.00 21.44  ? 7   VAL A O      1 
ATOM   122   C  CB     . VAL A 1 8   ? 10.620  34.121  16.752  1.00 21.71  ? 7   VAL A CB     1 
ATOM   123   C  CG1    . VAL A 1 8   ? 9.791   32.909  16.366  1.00 20.48  ? 7   VAL A CG1    1 
ATOM   124   C  CG2    . VAL A 1 8   ? 11.002  34.060  18.252  1.00 21.36  ? 7   VAL A CG2    1 
ATOM   125   H  H      . VAL A 1 8   ? 12.385  36.065  15.943  1.00 23.49  ? 7   VAL A H      1 
ATOM   126   H  HA     . VAL A 1 8   ? 12.392  33.351  16.064  1.00 22.27  ? 7   VAL A HA     1 
ATOM   127   H  HB     . VAL A 1 8   ? 10.089  34.919  16.600  1.00 26.08  ? 7   VAL A HB     1 
ATOM   128   H  HG11   . VAL A 1 8   ? 9.120   32.755  17.049  1.00 24.61  ? 7   VAL A HG11   1 
ATOM   129   H  HG12   . VAL A 1 8   ? 9.362   33.079  15.513  1.00 24.61  ? 7   VAL A HG12   1 
ATOM   130   H  HG13   . VAL A 1 8   ? 10.374  32.137  16.295  1.00 24.61  ? 7   VAL A HG13   1 
ATOM   131   H  HG21   . VAL A 1 8   ? 10.192  33.998  18.782  1.00 25.67  ? 7   VAL A HG21   1 
ATOM   132   H  HG22   . VAL A 1 8   ? 11.559  33.281  18.404  1.00 25.67  ? 7   VAL A HG22   1 
ATOM   133   H  HG23   . VAL A 1 8   ? 11.490  34.866  18.486  1.00 25.67  ? 7   VAL A HG23   1 
ATOM   134   N  N      . VAL A 1 9   ? 11.776  33.164  13.683  1.00 17.63  ? 8   VAL A N      1 
ATOM   135   C  CA     . VAL A 1 9   ? 11.553  33.118  12.242  1.00 17.68  ? 8   VAL A CA     1 
ATOM   136   C  C      . VAL A 1 9   ? 10.260  32.359  12.016  1.00 19.05  ? 8   VAL A C      1 
ATOM   137   O  O      . VAL A 1 9   ? 10.146  31.185  12.399  1.00 18.10  ? 8   VAL A O      1 
ATOM   138   C  CB     . VAL A 1 9   ? 12.730  32.461  11.514  1.00 18.72  ? 8   VAL A CB     1 
ATOM   139   C  CG1    . VAL A 1 9   ? 12.559  32.560  10.042  1.00 17.27  ? 8   VAL A CG1    1 
ATOM   140   C  CG2    . VAL A 1 9   ? 14.022  33.127  11.915  1.00 16.15  ? 8   VAL A CG2    1 
ATOM   141   H  H      . VAL A 1 9   ? 12.080  32.426  14.006  1.00 21.19  ? 8   VAL A H      1 
ATOM   142   H  HA     . VAL A 1 9   ? 11.453  34.016  11.889  1.00 21.25  ? 8   VAL A HA     1 
ATOM   143   H  HB     . VAL A 1 9   ? 12.762  31.523  11.761  1.00 22.50  ? 8   VAL A HB     1 
ATOM   144   H  HG11   . VAL A 1 9   ? 13.327  32.158  9.607   1.00 20.76  ? 8   VAL A HG11   1 
ATOM   145   H  HG12   . VAL A 1 9   ? 11.750  32.089  9.786   1.00 20.76  ? 8   VAL A HG12   1 
ATOM   146   H  HG13   . VAL A 1 9   ? 12.490  33.495  9.795   1.00 20.76  ? 8   VAL A HG13   1 
ATOM   147   H  HG21   . VAL A 1 9   ? 14.743  32.771  11.371  1.00 19.41  ? 8   VAL A HG21   1 
ATOM   148   H  HG22   . VAL A 1 9   ? 13.942  34.083  11.773  1.00 19.41  ? 8   VAL A HG22   1 
ATOM   149   H  HG23   . VAL A 1 9   ? 14.195  32.945  12.852  1.00 19.41  ? 8   VAL A HG23   1 
ATOM   150   N  N      . VAL A 1 10  ? 9.279   33.018  11.389  1.00 21.30  ? 9   VAL A N      1 
ATOM   151   C  CA     . VAL A 1 10  ? 7.974   32.410  11.197  1.00 17.75  ? 9   VAL A CA     1 
ATOM   152   C  C      . VAL A 1 10  ? 7.536   32.551  9.751   1.00 24.40  ? 9   VAL A C      1 
ATOM   153   O  O      . VAL A 1 10  ? 8.019   33.408  8.999   1.00 21.08  ? 9   VAL A O      1 
ATOM   154   C  CB     . VAL A 1 10  ? 6.905   33.055  12.113  1.00 21.96  ? 9   VAL A CB     1 
ATOM   155   C  CG1    . VAL A 1 10  ? 7.397   33.084  13.533  1.00 23.85  ? 9   VAL A CG1    1 
ATOM   156   C  CG2    . VAL A 1 10  ? 6.565   34.498  11.635  1.00 23.65  ? 9   VAL A CG2    1 
ATOM   157   H  H      . VAL A 1 10  ? 9.353   33.814  11.072  1.00 25.59  ? 9   VAL A H      1 
ATOM   158   H  HA     . VAL A 1 10  ? 8.051   31.463  11.393  1.00 21.33  ? 9   VAL A HA     1 
ATOM   159   H  HB     . VAL A 1 10  ? 6.095   32.524  12.069  1.00 26.38  ? 9   VAL A HB     1 
ATOM   160   H  HG11   . VAL A 1 10  ? 6.670   33.361  14.113  1.00 28.65  ? 9   VAL A HG11   1 
ATOM   161   H  HG12   . VAL A 1 10  ? 7.698   32.196  13.781  1.00 28.65  ? 9   VAL A HG12   1 
ATOM   162   H  HG13   . VAL A 1 10  ? 8.132   33.714  13.600  1.00 28.65  ? 9   VAL A HG13   1 
ATOM   163   H  HG21   . VAL A 1 10  ? 6.090   34.960  12.343  1.00 28.41  ? 9   VAL A HG21   1 
ATOM   164   H  HG22   . VAL A 1 10  ? 7.389   34.965  11.430  1.00 28.41  ? 9   VAL A HG22   1 
ATOM   165   H  HG23   . VAL A 1 10  ? 6.008   34.445  10.843  1.00 28.41  ? 9   VAL A HG23   1 
ATOM   166   N  N      . GLY A 1 11  ? 6.561   31.726  9.395   1.00 21.98  ? 10  GLY A N      1 
ATOM   167   C  CA     . GLY A 1 11  ? 5.962   31.744  8.075   1.00 22.35  ? 10  GLY A CA     1 
ATOM   168   C  C      . GLY A 1 11  ? 5.584   30.342  7.646   1.00 23.96  ? 10  GLY A C      1 
ATOM   169   O  O      . GLY A 1 11  ? 5.900   29.340  8.296   1.00 24.30  ? 10  GLY A O      1 
ATOM   170   H  H      . GLY A 1 11  ? 6.221   31.131  9.916   1.00 26.41  ? 10  GLY A H      1 
ATOM   171   H  HA2    . GLY A 1 11  ? 5.164   32.295  8.083   1.00 26.86  ? 10  GLY A HA2    1 
ATOM   172   H  HA3    . GLY A 1 11  ? 6.591   32.109  7.433   1.00 26.86  ? 10  GLY A HA3    1 
ATOM   173   N  N      . ALA A 1 12  ? 4.882   30.282  6.517   1.00 22.18  ? 11  ALA A N      1 
ATOM   174   C  CA     . ALA A 1 12  ? 4.378   29.010  6.029   1.00 24.37  ? 11  ALA A CA     1 
ATOM   175   C  C      . ALA A 1 12  ? 5.495   28.026  5.726   1.00 23.41  ? 11  ALA A C      1 
ATOM   176   O  O      . ALA A 1 12  ? 6.636   28.397  5.484   1.00 24.34  ? 11  ALA A O      1 
ATOM   177   C  CB     . ALA A 1 12  ? 3.581   29.222  4.740   1.00 33.34  ? 11  ALA A CB     1 
ATOM   178   H  H      . ALA A 1 12  ? 4.688   30.958  6.022   1.00 26.65  ? 11  ALA A H      1 
ATOM   179   H  HA     . ALA A 1 12  ? 3.814   28.630  6.720   1.00 29.28  ? 11  ALA A HA     1 
ATOM   180   H  HB1    . ALA A 1 12  ? 3.366   28.358  4.356   1.00 40.04  ? 11  ALA A HB1    1 
ATOM   181   H  HB2    . ALA A 1 12  ? 2.766   29.704  4.949   1.00 40.04  ? 11  ALA A HB2    1 
ATOM   182   H  HB3    . ALA A 1 12  ? 4.119   29.736  4.117   1.00 40.04  ? 11  ALA A HB3    1 
ATOM   183   N  N      . ASP A 1 13  ? 5.135   26.747  5.682   1.00 28.66  ? 12  ASP A N      1 
ATOM   184   C  CA     . ASP A 1 13  ? 6.096   25.707  5.335   1.00 30.43  ? 12  ASP A CA     1 
ATOM   185   C  C      . ASP A 1 13  ? 6.678   25.956  3.948   1.00 25.36  ? 12  ASP A C      1 
ATOM   186   O  O      . ASP A 1 13  ? 5.969   26.367  3.034   1.00 25.80  ? 12  ASP A O      1 
ATOM   187   C  CB     . ASP A 1 13  ? 5.410   24.329  5.369   1.00 39.18  ? 12  ASP A CB     1 
ATOM   188   C  CG     . ASP A 1 13  ? 4.081   24.308  4.626   1.00 43.90  ? 12  ASP A CG     1 
ATOM   189   O  OD1    . ASP A 1 13  ? 3.024   24.420  5.283   1.00 44.61  ? 12  ASP A OD1    1 
ATOM   190   O  OD2    . ASP A 1 13  ? 4.092   24.203  3.372   1.00 46.72  ? 12  ASP A OD2    1 
ATOM   191   H  H      . ASP A 1 13  ? 4.343   26.456  5.849   1.00 34.43  ? 12  ASP A H      1 
ATOM   192   H  HA     . ASP A 1 13  ? 6.821   25.711  5.978   1.00 36.56  ? 12  ASP A HA     1 
ATOM   193   H  HB2    . ASP A 1 13  ? 5.995   23.676  4.955   1.00 47.05  ? 12  ASP A HB2    1 
ATOM   194   H  HB3    . ASP A 1 13  ? 5.240   24.085  6.292   1.00 47.05  ? 12  ASP A HB3    1 
ATOM   195   N  N      . GLY A 1 14  ? 7.983   25.725  3.804   1.00 22.49  ? 13  GLY A N      1 
ATOM   196   C  CA     . GLY A 1 14  ? 8.639   25.739  2.505   1.00 25.38  ? 13  GLY A CA     1 
ATOM   197   C  C      . GLY A 1 14  ? 9.100   27.085  1.992   1.00 20.61  ? 13  GLY A C      1 
ATOM   198   O  O      . GLY A 1 14  ? 9.634   27.154  0.870   1.00 25.52  ? 13  GLY A O      1 
ATOM   199   H  H      . GLY A 1 14  ? 8.516   25.556  4.457   1.00 27.02  ? 13  GLY A H      1 
ATOM   200   H  HA2    . GLY A 1 14  ? 9.421   25.166  2.555   1.00 30.49  ? 13  GLY A HA2    1 
ATOM   201   H  HA3    . GLY A 1 14  ? 8.023   25.376  1.850   1.00 30.49  ? 13  GLY A HA3    1 
ATOM   202   N  N      . VAL A 1 15  ? 8.908   28.160  2.765   1.00 22.23  ? 14  VAL A N      1 
ATOM   203   C  CA     . VAL A 1 15  ? 9.262   29.481  2.281   1.00 20.34  ? 14  VAL A CA     1 
ATOM   204   C  C      . VAL A 1 15  ? 10.757  29.765  2.387   1.00 19.16  ? 14  VAL A C      1 
ATOM   205   O  O      . VAL A 1 15  ? 11.244  30.734  1.772   1.00 21.21  ? 14  VAL A O      1 
ATOM   206   C  CB     . VAL A 1 15  ? 8.497   30.582  3.037   1.00 24.28  ? 14  VAL A CB     1 
ATOM   207   C  CG1    . VAL A 1 15  ? 6.964   30.438  2.840   1.00 24.87  ? 14  VAL A CG1    1 
ATOM   208   C  CG2    . VAL A 1 15  ? 8.831   30.534  4.542   1.00 20.43  ? 14  VAL A CG2    1 
ATOM   209   H  H      . VAL A 1 15  ? 8.580   28.144  3.560   1.00 26.71  ? 14  VAL A H      1 
ATOM   210   H  HA     . VAL A 1 15  ? 9.008   29.511  1.346   1.00 24.44  ? 14  VAL A HA     1 
ATOM   211   H  HB     . VAL A 1 15  ? 8.772   31.439  2.678   1.00 29.17  ? 14  VAL A HB     1 
ATOM   212   H  HG11   . VAL A 1 15  ? 6.515   31.146  3.327   1.00 29.88  ? 14  VAL A HG11   1 
ATOM   213   H  HG12   . VAL A 1 15  ? 6.760   30.507  1.894   1.00 29.88  ? 14  VAL A HG12   1 
ATOM   214   H  HG13   . VAL A 1 15  ? 6.681   29.574  3.177   1.00 29.88  ? 14  VAL A HG13   1 
ATOM   215   H  HG21   . VAL A 1 15  ? 8.256   31.156  5.013   1.00 24.56  ? 14  VAL A HG21   1 
ATOM   216   H  HG22   . VAL A 1 15  ? 8.682   29.633  4.870   1.00 24.56  ? 14  VAL A HG22   1 
ATOM   217   H  HG23   . VAL A 1 15  ? 9.760   30.782  4.667   1.00 24.56  ? 14  VAL A HG23   1 
ATOM   218   N  N      . GLY A 1 16  ? 11.474  28.996  3.206   1.00 18.53  ? 15  GLY A N      1 
ATOM   219   C  CA     . GLY A 1 16  ? 12.889  29.205  3.415   1.00 19.59  ? 15  GLY A CA     1 
ATOM   220   C  C      . GLY A 1 16  ? 13.302  29.756  4.790   1.00 19.24  ? 15  GLY A C      1 
ATOM   221   O  O      . GLY A 1 16  ? 14.369  30.358  4.895   1.00 17.32  ? 15  GLY A O      1 
ATOM   222   H  H      . GLY A 1 16  ? 11.149  28.338  3.654   1.00 22.27  ? 15  GLY A H      1 
ATOM   223   H  HA2    . GLY A 1 16  ? 13.343  28.357  3.295   1.00 23.54  ? 15  GLY A HA2    1 
ATOM   224   H  HA3    . GLY A 1 16  ? 13.207  29.831  2.745   1.00 23.54  ? 15  GLY A HA3    1 
ATOM   225   N  N      . LYS A 1 17  ? 12.484  29.583  5.819   1.00 17.74  ? 16  LYS A N      1 
ATOM   226   C  CA     . LYS A 1 17  ? 12.892  29.999  7.172   1.00 15.38  ? 16  LYS A CA     1 
ATOM   227   C  C      . LYS A 1 17  ? 14.205  29.354  7.568   1.00 17.32  ? 16  LYS A C      1 
ATOM   228   O  O      . LYS A 1 17  ? 15.138  30.020  8.043   1.00 18.41  ? 16  LYS A O      1 
ATOM   229   C  CB     . LYS A 1 17  ? 11.800  29.592  8.186   1.00 17.85  ? 16  LYS A CB     1 
ATOM   230   C  CG     . LYS A 1 17  ? 10.459  30.226  7.940   1.00 20.10  ? 16  LYS A CG     1 
ATOM   231   C  CD     . LYS A 1 17  ? 9.373   29.849  8.951   1.00 21.05  ? 16  LYS A CD     1 
ATOM   232   C  CE     . LYS A 1 17  ? 9.054   28.381  8.947   1.00 21.31  ? 16  LYS A CE     1 
ATOM   233   N  NZ     . LYS A 1 17  ? 8.325   27.924  7.702   1.00 24.06  ? 16  LYS A NZ     1 
ATOM   234   H  H      . LYS A 1 17  ? 11.699  29.235  5.772   1.00 21.32  ? 16  LYS A H      1 
ATOM   235   H  HA     . LYS A 1 17  ? 13.001  30.963  7.182   1.00 18.49  ? 16  LYS A HA     1 
ATOM   236   H  HB2    . LYS A 1 17  ? 11.682  28.630  8.145   1.00 21.45  ? 16  LYS A HB2    1 
ATOM   237   H  HB3    . LYS A 1 17  ? 12.090  29.853  9.074   1.00 21.45  ? 16  LYS A HB3    1 
ATOM   238   H  HG2    . LYS A 1 17  ? 10.563  31.190  7.972   1.00 24.15  ? 16  LYS A HG2    1 
ATOM   239   H  HG3    . LYS A 1 17  ? 10.146  29.954  7.063   1.00 24.15  ? 16  LYS A HG3    1 
ATOM   240   H  HD2    . LYS A 1 17  ? 9.674   30.087  9.842   1.00 25.29  ? 16  LYS A HD2    1 
ATOM   241   H  HD3    . LYS A 1 17  ? 8.560   30.332  8.735   1.00 25.29  ? 16  LYS A HD3    1 
ATOM   242   H  HE2    . LYS A 1 17  ? 9.882   27.880  9.006   1.00 25.61  ? 16  LYS A HE2    1 
ATOM   243   H  HE3    . LYS A 1 17  ? 8.490   28.180  9.711   1.00 25.61  ? 16  LYS A HE3    1 
ATOM   244   H  HZ1    . LYS A 1 17  ? 7.557   28.366  7.620   1.00 28.90  ? 16  LYS A HZ1    1 
ATOM   245   H  HZ2    . LYS A 1 17  ? 8.826   28.078  6.983   1.00 28.90  ? 16  LYS A HZ2    1 
ATOM   246   H  HZ3    . LYS A 1 17  ? 8.152   27.052  7.753   1.00 28.90  ? 16  LYS A HZ3    1 
ATOM   247   N  N      . SER A 1 18  ? 14.284  28.037  7.414   1.00 16.02  ? 17  SER A N      1 
ATOM   248   C  CA     . SER A 1 18  ? 15.479  27.317  7.820   1.00 16.96  ? 17  SER A CA     1 
ATOM   249   C  C      . SER A 1 18  ? 16.650  27.650  6.913   1.00 17.20  ? 17  SER A C      1 
ATOM   250   O  O      . SER A 1 18  ? 17.763  27.861  7.398   1.00 16.65  ? 17  SER A O      1 
ATOM   251   C  CB     . SER A 1 18  ? 15.216  25.823  7.823   1.00 16.19  ? 17  SER A CB     1 
ATOM   252   O  OG     . SER A 1 18  ? 14.167  25.532  8.763   1.00 18.31  ? 17  SER A OG     1 
ATOM   253   H  H      . SER A 1 18  ? 13.665  27.542  7.080   1.00 19.26  ? 17  SER A H      1 
ATOM   254   H  HA     . SER A 1 18  ? 15.710  27.581  8.725   1.00 20.39  ? 17  SER A HA     1 
ATOM   255   H  HB2    . SER A 1 18  ? 14.941  25.541  6.936   1.00 19.46  ? 17  SER A HB2    1 
ATOM   256   H  HB3    . SER A 1 18  ? 16.023  25.353  8.085   1.00 19.46  ? 17  SER A HB3    1 
ATOM   257   N  N      . ALA A 1 19  ? 16.426  27.731  5.603   1.00 18.63  ? 18  ALA A N      1 
ATOM   258   C  CA     . ALA A 1 19  ? 17.541  28.062  4.731   1.00 15.21  ? 18  ALA A CA     1 
ATOM   259   C  C      . ALA A 1 19  ? 18.084  29.448  5.062   1.00 16.31  ? 18  ALA A C      1 
ATOM   260   O  O      . ALA A 1 19  ? 19.307  29.658  5.049   1.00 17.68  ? 18  ALA A O      1 
ATOM   261   C  CB     . ALA A 1 19  ? 17.106  27.967  3.261   1.00 19.51  ? 18  ALA A CB     1 
ATOM   262   H  H      . ALA A 1 19  ? 15.670  27.603  5.214   1.00 22.39  ? 18  ALA A H      1 
ATOM   263   H  HA     . ALA A 1 19  ? 18.257  27.422  4.860   1.00 18.29  ? 18  ALA A HA     1 
ATOM   264   H  HB1    . ALA A 1 19  ? 17.861  28.190  2.694   1.00 23.44  ? 18  ALA A HB1    1 
ATOM   265   H  HB2    . ALA A 1 19  ? 16.810  27.061  3.078   1.00 23.44  ? 18  ALA A HB2    1 
ATOM   266   H  HB3    . ALA A 1 19  ? 16.380  28.590  3.106   1.00 23.44  ? 18  ALA A HB3    1 
ATOM   267   N  N      . LEU A 1 20  ? 17.209  30.397  5.369   1.00 16.49  ? 19  LEU A N      1 
ATOM   268   C  CA     . LEU A 1 20  ? 17.677  31.725  5.774   1.00 16.29  ? 19  LEU A CA     1 
ATOM   269   C  C      . LEU A 1 20  ? 18.521  31.643  7.054   1.00 17.03  ? 19  LEU A C      1 
ATOM   270   O  O      . LEU A 1 20  ? 19.620  32.191  7.115   1.00 18.10  ? 19  LEU A O      1 
ATOM   271   C  CB     . LEU A 1 20  ? 16.515  32.681  5.961   1.00 18.05  ? 19  LEU A CB     1 
ATOM   272   C  CG     . LEU A 1 20  ? 15.845  33.206  4.703   1.00 20.19  ? 19  LEU A CG     1 
ATOM   273   C  CD1    . LEU A 1 20  ? 14.604  34.053  4.972   1.00 19.88  ? 19  LEU A CD1    1 
ATOM   274   C  CD2    . LEU A 1 20  ? 16.794  34.058  3.882   1.00 19.53  ? 19  LEU A CD2    1 
ATOM   275   H  H      . LEU A 1 20  ? 16.354  30.305  5.353   1.00 19.82  ? 19  LEU A H      1 
ATOM   276   H  HA     . LEU A 1 20  ? 18.230  32.081  5.060   1.00 19.58  ? 19  LEU A HA     1 
ATOM   277   H  HB2    . LEU A 1 20  ? 15.833  32.224  6.476   1.00 21.70  ? 19  LEU A HB2    1 
ATOM   278   H  HB3    . LEU A 1 20  ? 16.840  33.453  6.452   1.00 21.70  ? 19  LEU A HB3    1 
ATOM   279   H  HG     . LEU A 1 20  ? 15.577  32.412  4.215   1.00 24.26  ? 19  LEU A HG     1 
ATOM   280   H  HD11   . LEU A 1 20  ? 14.187  34.281  4.126   1.00 23.89  ? 19  LEU A HD11   1 
ATOM   281   H  HD12   . LEU A 1 20  ? 13.985  33.543  5.518   1.00 23.89  ? 19  LEU A HD12   1 
ATOM   282   H  HD13   . LEU A 1 20  ? 14.868  34.862  5.438   1.00 23.89  ? 19  LEU A HD13   1 
ATOM   283   H  HD21   . LEU A 1 20  ? 16.298  34.483  3.166   1.00 23.47  ? 19  LEU A HD21   1 
ATOM   284   H  HD22   . LEU A 1 20  ? 17.190  34.732  4.456   1.00 23.47  ? 19  LEU A HD22   1 
ATOM   285   H  HD23   . LEU A 1 20  ? 17.488  33.490  3.512   1.00 23.47  ? 19  LEU A HD23   1 
ATOM   286   N  N      . THR A 1 21  ? 18.017  30.937  8.061   1.00 15.93  ? 20  THR A N      1 
ATOM   287   C  CA     . THR A 1 21  ? 18.707  30.780  9.338   1.00 17.35  ? 20  THR A CA     1 
ATOM   288   C  C      . THR A 1 21  ? 20.055  30.090  9.168   1.00 18.00  ? 20  THR A C      1 
ATOM   289   O  O      . THR A 1 21  ? 21.061  30.526  9.741   1.00 18.59  ? 20  THR A O      1 
ATOM   290   C  CB     . THR A 1 21  ? 17.795  30.002  10.289  1.00 15.86  ? 20  THR A CB     1 
ATOM   291   O  OG1    . THR A 1 21  ? 16.617  30.780  10.544  1.00 18.33  ? 20  THR A OG1    1 
ATOM   292   C  CG2    . THR A 1 21  ? 18.483  29.745  11.578  1.00 17.88  ? 20  THR A CG2    1 
ATOM   293   H  H      . THR A 1 21  ? 17.260  30.530  8.031   1.00 19.16  ? 20  THR A H      1 
ATOM   294   H  HA     . THR A 1 21  ? 18.888  31.652  9.723   1.00 20.86  ? 20  THR A HA     1 
ATOM   295   H  HB     . THR A 1 21  ? 17.558  29.150  9.890   1.00 19.07  ? 20  THR A HB     1 
ATOM   296   H  HG1    . THR A 1 21  ? 16.251  30.993  9.819   1.00 22.04  ? 20  THR A HG1    1 
ATOM   297   H  HG21   . THR A 1 21  ? 17.840  29.463  12.247  1.00 21.49  ? 20  THR A HG21   1 
ATOM   298   H  HG22   . THR A 1 21  ? 19.148  29.048  11.466  1.00 21.49  ? 20  THR A HG22   1 
ATOM   299   H  HG23   . THR A 1 21  ? 18.924  30.553  11.886  1.00 21.49  ? 20  THR A HG23   1 
ATOM   300   N  N      . ILE A 1 22  ? 20.089  28.977  8.425   1.00 15.44  ? 21  ILE A N      1 
ATOM   301   C  CA     . ILE A 1 22  ? 21.339  28.234  8.236   1.00 19.19  ? 21  ILE A CA     1 
ATOM   302   C  C      . ILE A 1 22  ? 22.336  29.055  7.433   1.00 17.61  ? 21  ILE A C      1 
ATOM   303   O  O      . ILE A 1 22  ? 23.542  29.008  7.700   1.00 18.78  ? 21  ILE A O      1 
ATOM   304   C  CB     . ILE A 1 22  ? 21.058  26.881  7.585   1.00 18.94  ? 21  ILE A CB     1 
ATOM   305   C  CG1    . ILE A 1 22  ? 20.236  25.941  8.491   1.00 21.10  ? 21  ILE A CG1    1 
ATOM   306   C  CG2    . ILE A 1 22  ? 22.375  26.179  7.199   1.00 20.00  ? 21  ILE A CG2    1 
ATOM   307   C  CD1    . ILE A 1 22  ? 20.732  25.837  9.851   1.00 26.73  ? 21  ILE A CD1    1 
ATOM   308   H  H      . ILE A 1 22  ? 19.410  28.635  8.024   1.00 18.56  ? 21  ILE A H      1 
ATOM   309   H  HA     . ILE A 1 22  ? 21.734  28.064  9.106   1.00 23.06  ? 21  ILE A HA     1 
ATOM   310   H  HB     . ILE A 1 22  ? 20.531  27.070  6.793   1.00 22.76  ? 21  ILE A HB     1 
ATOM   311   H  HG12   . ILE A 1 22  ? 19.325  26.272  8.535   1.00 25.36  ? 21  ILE A HG12   1 
ATOM   312   H  HG13   . ILE A 1 22  ? 20.247  25.051  8.106   1.00 25.36  ? 21  ILE A HG13   1 
ATOM   313   H  HG21   . ILE A 1 22  ? 22.192  25.244  7.014   1.00 24.03  ? 21  ILE A HG21   1 
ATOM   314   H  HG22   . ILE A 1 22  ? 22.742  26.607  6.410   1.00 24.03  ? 21  ILE A HG22   1 
ATOM   315   H  HG23   . ILE A 1 22  ? 23.001  26.254  7.936   1.00 24.03  ? 21  ILE A HG23   1 
ATOM   316   H  HD11   . ILE A 1 22  ? 20.353  25.047  10.266  1.00 32.11  ? 21  ILE A HD11   1 
ATOM   317   H  HD12   . ILE A 1 22  ? 21.699  25.769  9.830   1.00 32.11  ? 21  ILE A HD12   1 
ATOM   318   H  HD13   . ILE A 1 22  ? 20.467  26.629  10.345  1.00 32.11  ? 21  ILE A HD13   1 
ATOM   319   N  N      . GLN A 1 23  ? 21.867  29.889  6.508   1.00 16.80  ? 22  GLN A N      1 
ATOM   320   C  CA     . GLN A 1 23  ? 22.812  30.799  5.846   1.00 19.46  ? 22  GLN A CA     1 
ATOM   321   C  C      . GLN A 1 23  ? 23.421  31.760  6.862   1.00 21.14  ? 22  GLN A C      1 
ATOM   322   O  O      . GLN A 1 23  ? 24.633  31.988  6.876   1.00 19.81  ? 22  GLN A O      1 
ATOM   323   C  CB     . GLN A 1 23  ? 22.128  31.619  4.763   1.00 22.19  ? 22  GLN A CB     1 
ATOM   324   C  CG     . GLN A 1 23  ? 22.199  31.116  3.385   1.00 23.74  ? 22  GLN A CG     1 
ATOM   325   C  CD     . GLN A 1 23  ? 23.590  30.884  2.830   1.00 23.85  ? 22  GLN A CD     1 
ATOM   326   O  OE1    . GLN A 1 23  ? 24.640  31.151  3.454   1.00 21.68  ? 22  GLN A OE1    1 
ATOM   327   N  NE2    . GLN A 1 23  ? 23.603  30.414  1.595   1.00 21.01  ? 22  GLN A NE2    1 
ATOM   328   H  H      . GLN A 1 23  ? 21.048  29.949  6.254   1.00 20.19  ? 22  GLN A H      1 
ATOM   329   H  HA     . GLN A 1 23  ? 23.500  30.256  5.431   1.00 23.38  ? 22  GLN A HA     1 
ATOM   330   H  HB2    . GLN A 1 23  ? 21.187  31.684  4.990   1.00 26.66  ? 22  GLN A HB2    1 
ATOM   331   H  HB3    . GLN A 1 23  ? 22.531  32.501  4.761   1.00 26.66  ? 22  GLN A HB3    1 
ATOM   332   H  HG2    . GLN A 1 23  ? 21.731  30.268  3.347   1.00 28.53  ? 22  GLN A HG2    1 
ATOM   333   H  HG3    . GLN A 1 23  ? 21.764  31.761  2.805   1.00 28.53  ? 22  GLN A HG3    1 
ATOM   334   H  HE21   . GLN A 1 23  ? 22.863  30.269  1.183   1.00 25.24  ? 22  GLN A HE21   1 
ATOM   335   H  HE22   . GLN A 1 23  ? 24.352  30.254  1.204   1.00 25.24  ? 22  GLN A HE22   1 
ATOM   336   N  N      . LEU A 1 24  ? 22.582  32.402  7.670   1.00 18.09  ? 23  LEU A N      1 
ATOM   337   C  CA     . LEU A 1 24  ? 23.105  33.300  8.698   1.00 20.57  ? 23  LEU A CA     1 
ATOM   338   C  C      . LEU A 1 24  ? 24.116  32.575  9.567   1.00 21.99  ? 23  LEU A C      1 
ATOM   339   O  O      . LEU A 1 24  ? 25.190  33.097  9.866   1.00 20.35  ? 23  LEU A O      1 
ATOM   340   C  CB     . LEU A 1 24  ? 21.973  33.837  9.559   1.00 21.16  ? 23  LEU A CB     1 
ATOM   341   C  CG     . LEU A 1 24  ? 22.353  34.846  10.662  1.00 21.19  ? 23  LEU A CG     1 
ATOM   342   C  CD1    . LEU A 1 24  ? 22.707  36.203  10.089  1.00 25.46  ? 23  LEU A CD1    1 
ATOM   343   C  CD2    . LEU A 1 24  ? 21.206  34.950  11.664  1.00 23.05  ? 23  LEU A CD2    1 
ATOM   344   H  H      . LEU A 1 24  ? 21.725  32.339  7.645   1.00 21.74  ? 23  LEU A H      1 
ATOM   345   H  HA     . LEU A 1 24  ? 23.538  34.052  8.264   1.00 24.72  ? 23  LEU A HA     1 
ATOM   346   H  HB2    . LEU A 1 24  ? 21.338  34.282  8.976   1.00 25.42  ? 23  LEU A HB2    1 
ATOM   347   H  HB3    . LEU A 1 24  ? 21.548  33.084  9.999   1.00 25.42  ? 23  LEU A HB3    1 
ATOM   348   H  HG     . LEU A 1 24  ? 23.147  34.531  11.122  1.00 25.46  ? 23  LEU A HG     1 
ATOM   349   H  HD11   . LEU A 1 24  ? 22.939  36.802  10.816  1.00 30.59  ? 23  LEU A HD11   1 
ATOM   350   H  HD12   . LEU A 1 24  ? 23.461  36.105  9.487   1.00 30.59  ? 23  LEU A HD12   1 
ATOM   351   H  HD13   . LEU A 1 24  ? 21.941  36.551  9.607   1.00 30.59  ? 23  LEU A HD13   1 
ATOM   352   H  HD21   . LEU A 1 24  ? 21.386  35.681  12.275  1.00 27.69  ? 23  LEU A HD21   1 
ATOM   353   H  HD22   . LEU A 1 24  ? 20.380  35.118  11.182  1.00 27.69  ? 23  LEU A HD22   1 
ATOM   354   H  HD23   . LEU A 1 24  ? 21.138  34.117  12.155  1.00 27.69  ? 23  LEU A HD23   1 
ATOM   355   N  N      . ILE A 1 25  ? 23.764  31.370  10.010  1.00 19.62  ? 24  ILE A N      1 
ATOM   356   C  CA     . ILE A 1 25  ? 24.537  30.744  11.071  1.00 20.38  ? 24  ILE A CA     1 
ATOM   357   C  C      . ILE A 1 25  ? 25.783  30.082  10.498  1.00 22.51  ? 24  ILE A C      1 
ATOM   358   O  O      . ILE A 1 25  ? 26.878  30.172  11.078  1.00 23.11  ? 24  ILE A O      1 
ATOM   359   C  CB     . ILE A 1 25  ? 23.676  29.732  11.844  1.00 21.44  ? 24  ILE A CB     1 
ATOM   360   C  CG1    . ILE A 1 25  ? 22.442  30.401  12.508  1.00 22.50  ? 24  ILE A CG1    1 
ATOM   361   C  CG2    . ILE A 1 25  ? 24.527  29.062  12.899  1.00 24.06  ? 24  ILE A CG2    1 
ATOM   362   C  CD1    . ILE A 1 25  ? 22.747  31.419  13.616  1.00 19.89  ? 24  ILE A CD1    1 
ATOM   363   H  H      . ILE A 1 25  ? 23.100  30.908  9.719   1.00 23.58  ? 24  ILE A H      1 
ATOM   364   H  HA     . ILE A 1 25  ? 24.813  31.434  11.694  1.00 24.49  ? 24  ILE A HA     1 
ATOM   365   H  HB     . ILE A 1 25  ? 23.342  29.077  11.210  1.00 25.77  ? 24  ILE A HB     1 
ATOM   366   H  HG12   . ILE A 1 25  ? 21.942  30.868  11.820  1.00 27.03  ? 24  ILE A HG12   1 
ATOM   367   H  HG13   . ILE A 1 25  ? 21.893  29.705  12.901  1.00 27.03  ? 24  ILE A HG13   1 
ATOM   368   H  HG21   . ILE A 1 25  ? 23.948  28.676  13.574  1.00 28.90  ? 24  ILE A HG21   1 
ATOM   369   H  HG22   . ILE A 1 25  ? 25.058  28.366  12.481  1.00 28.90  ? 24  ILE A HG22   1 
ATOM   370   H  HG23   . ILE A 1 25  ? 25.110  29.725  13.302  1.00 28.90  ? 24  ILE A HG23   1 
ATOM   371   H  HD11   . ILE A 1 25  ? 21.913  31.787  13.945  1.00 23.90  ? 24  ILE A HD11   1 
ATOM   372   H  HD12   . ILE A 1 25  ? 23.218  30.970  14.336  1.00 23.90  ? 24  ILE A HD12   1 
ATOM   373   H  HD13   . ILE A 1 25  ? 23.300  32.127  13.251  1.00 23.90  ? 24  ILE A HD13   1 
ATOM   374   N  N      . GLN A 1 26  ? 25.634  29.380  9.378   1.00 20.18  ? 25  GLN A N      1 
ATOM   375   C  CA     . GLN A 1 26  ? 26.698  28.517  8.871   1.00 20.55  ? 25  GLN A CA     1 
ATOM   376   C  C      . GLN A 1 26  ? 27.208  28.892  7.491   1.00 23.30  ? 25  GLN A C      1 
ATOM   377   O  O      . GLN A 1 26  ? 28.140  28.242  7.012   1.00 25.08  ? 25  GLN A O      1 
ATOM   378   C  CB     . GLN A 1 26  ? 26.209  27.070  8.820   1.00 21.47  ? 25  GLN A CB     1 
ATOM   379   C  CG     . GLN A 1 26  ? 25.780  26.583  10.195  1.00 23.80  ? 25  GLN A CG     1 
ATOM   380   C  CD     . GLN A 1 26  ? 25.246  25.175  10.219  1.00 30.93  ? 25  GLN A CD     1 
ATOM   381   O  OE1    . GLN A 1 26  ? 25.305  24.458  9.226   1.00 33.63  ? 25  GLN A OE1    1 
ATOM   382   N  NE2    . GLN A 1 26  ? 24.719  24.767  11.370  1.00 37.12  ? 25  GLN A NE2    1 
ATOM   383   H  H      . GLN A 1 26  ? 24.925  29.386  8.892   1.00 24.25  ? 25  GLN A H      1 
ATOM   384   H  HA     . GLN A 1 26  ? 27.450  28.575  9.482   1.00 24.69  ? 25  GLN A HA     1 
ATOM   385   H  HB2    . GLN A 1 26  ? 25.447  27.009  8.222   1.00 25.79  ? 25  GLN A HB2    1 
ATOM   386   H  HB3    . GLN A 1 26  ? 26.926  26.499  8.502   1.00 25.79  ? 25  GLN A HB3    1 
ATOM   387   H  HG2    . GLN A 1 26  ? 26.547  26.616  10.788  1.00 28.59  ? 25  GLN A HG2    1 
ATOM   388   H  HG3    . GLN A 1 26  ? 25.080  27.167  10.526  1.00 28.59  ? 25  GLN A HG3    1 
ATOM   389   H  HE21   . GLN A 1 26  ? 24.699  25.299  12.046  1.00 44.58  ? 25  GLN A HE21   1 
ATOM   390   H  HE22   . GLN A 1 26  ? 24.400  23.972  11.440  1.00 44.58  ? 25  GLN A HE22   1 
ATOM   391   N  N      . ASN A 1 27  ? 26.593  29.866  6.824   1.00 20.23  ? 26  ASN A N      1 
ATOM   392   C  CA     . ASN A 1 27  ? 27.045  30.406  5.539   1.00 24.88  ? 26  ASN A CA     1 
ATOM   393   C  C      . ASN A 1 27  ? 27.055  29.341  4.441   1.00 25.70  ? 26  ASN A C      1 
ATOM   394   O  O      . ASN A 1 27  ? 27.957  29.285  3.599   1.00 26.08  ? 26  ASN A O      1 
ATOM   395   C  CB     . ASN A 1 27  ? 28.417  31.091  5.697   1.00 23.39  ? 26  ASN A CB     1 
ATOM   396   C  CG     . ASN A 1 27  ? 28.513  32.426  4.901   1.00 28.18  ? 26  ASN A CG     1 
ATOM   397   O  OD1    . ASN A 1 27  ? 28.292  33.500  5.459   1.00 28.77  ? 26  ASN A OD1    1 
ATOM   398   N  ND2    . ASN A 1 27  ? 28.906  32.345  3.604   1.00 25.00  ? 26  ASN A ND2    1 
ATOM   399   H  H      . ASN A 1 27  ? 25.878  30.251  7.107   1.00 24.31  ? 26  ASN A H      1 
ATOM   400   H  HA     . ASN A 1 27  ? 26.412  31.078  5.242   1.00 29.89  ? 26  ASN A HA     1 
ATOM   401   H  HB2    . ASN A 1 27  ? 28.566  31.289  6.635   1.00 28.11  ? 26  ASN A HB2    1 
ATOM   402   H  HB3    . ASN A 1 27  ? 29.109  30.495  5.370   1.00 28.11  ? 26  ASN A HB3    1 
ATOM   403   H  HD21   . ASN A 1 27  ? 29.089  31.580  3.257   1.00 30.03  ? 26  ASN A HD21   1 
ATOM   404   H  HD22   . ASN A 1 27  ? 28.972  33.060  3.130   1.00 30.03  ? 26  ASN A HD22   1 
ATOM   405   N  N      . HIS A 1 28  ? 26.026  28.500  4.414   1.00 22.99  ? 27  HIS A N      1 
ATOM   406   C  CA     . HIS A 1 28  ? 25.809  27.691  3.226   1.00 30.14  ? 27  HIS A CA     1 
ATOM   407   C  C      . HIS A 1 28  ? 24.321  27.429  3.059   1.00 26.26  ? 27  HIS A C      1 
ATOM   408   O  O      . HIS A 1 28  ? 23.509  27.687  3.958   1.00 22.22  ? 27  HIS A O      1 
ATOM   409   C  CB     . HIS A 1 28  ? 26.570  26.376  3.284   1.00 31.96  ? 27  HIS A CB     1 
ATOM   410   C  CG     . HIS A 1 28  ? 26.038  25.453  4.323   1.00 29.47  ? 27  HIS A CG     1 
ATOM   411   N  ND1    . HIS A 1 28  ? 25.089  24.496  4.043   1.00 36.89  ? 27  HIS A ND1    1 
ATOM   412   C  CD2    . HIS A 1 28  ? 26.279  25.374  5.651   1.00 32.51  ? 27  HIS A CD2    1 
ATOM   413   C  CE1    . HIS A 1 28  ? 24.787  23.843  5.148   1.00 34.59  ? 27  HIS A CE1    1 
ATOM   414   N  NE2    . HIS A 1 28  ? 25.491  24.358  6.141   1.00 39.14  ? 27  HIS A NE2    1 
ATOM   415   H  H      . HIS A 1 28  ? 25.460  28.385  5.051   1.00 27.62  ? 27  HIS A H      1 
ATOM   416   H  HA     . HIS A 1 28  ? 26.122  28.194  2.458   1.00 36.20  ? 27  HIS A HA     1 
ATOM   417   H  HB2    . HIS A 1 28  ? 26.501  25.932  2.424   1.00 38.39  ? 27  HIS A HB2    1 
ATOM   418   H  HB3    . HIS A 1 28  ? 27.500  26.558  3.490   1.00 38.39  ? 27  HIS A HB3    1 
ATOM   419   H  HD2    . HIS A 1 28  ? 26.866  25.904  6.140   1.00 39.05  ? 27  HIS A HD2    1 
ATOM   420   H  HE1    . HIS A 1 28  ? 24.182  23.139  5.217   1.00 41.54  ? 27  HIS A HE1    1 
ATOM   421   H  HE2    . HIS A 1 28  ? 25.461  24.101  6.961   1.00 47.00  ? 27  HIS A HE2    1 
ATOM   422   N  N      . PHE A 1 29  ? 23.970  26.888  1.904   1.00 26.82  ? 28  PHE A N      1 
ATOM   423   C  CA     . PHE A 1 29  ? 22.578  26.815  1.484   1.00 24.99  ? 28  PHE A CA     1 
ATOM   424   C  C      . PHE A 1 29  ? 22.088  25.379  1.524   1.00 33.42  ? 28  PHE A C      1 
ATOM   425   O  O      . PHE A 1 29  ? 22.644  24.512  0.856   1.00 31.94  ? 28  PHE A O      1 
ATOM   426   C  CB     . PHE A 1 29  ? 22.410  27.432  0.104   1.00 25.44  ? 28  PHE A CB     1 
ATOM   427   C  CG     . PHE A 1 29  ? 21.068  27.199  -0.504  1.00 26.31  ? 28  PHE A CG     1 
ATOM   428   C  CD1    . PHE A 1 29  ? 19.925  27.732  0.062   1.00 26.76  ? 28  PHE A CD1    1 
ATOM   429   C  CD2    . PHE A 1 29  ? 20.958  26.446  -1.642  1.00 29.30  ? 28  PHE A CD2    1 
ATOM   430   C  CE1    . PHE A 1 29  ? 18.681  27.507  -0.515  1.00 25.20  ? 28  PHE A CE1    1 
ATOM   431   C  CE2    . PHE A 1 29  ? 19.722  26.220  -2.237  1.00 29.36  ? 28  PHE A CE2    1 
ATOM   432   C  CZ     . PHE A 1 29  ? 18.581  26.749  -1.674  1.00 25.82  ? 28  PHE A CZ     1 
ATOM   433   H  H      . PHE A 1 29  ? 24.526  26.553  1.339   1.00 32.22  ? 28  PHE A H      1 
ATOM   434   H  HA     . PHE A 1 29  ? 22.027  27.308  2.113   1.00 30.02  ? 28  PHE A HA     1 
ATOM   435   H  HB2    . PHE A 1 29  ? 22.539  28.391  0.174   1.00 30.56  ? 28  PHE A HB2    1 
ATOM   436   H  HB3    . PHE A 1 29  ? 23.074  27.050  -0.490  1.00 30.56  ? 28  PHE A HB3    1 
ATOM   437   H  HD1    . PHE A 1 29  ? 19.989  28.245  0.835   1.00 32.14  ? 28  PHE A HD1    1 
ATOM   438   H  HD2    . PHE A 1 29  ? 21.723  26.079  -2.023  1.00 35.20  ? 28  PHE A HD2    1 
ATOM   439   H  HE1    . PHE A 1 29  ? 17.915  27.863  -0.124  1.00 30.28  ? 28  PHE A HE1    1 
ATOM   440   H  HE2    . PHE A 1 29  ? 19.666  25.713  -3.015  1.00 35.27  ? 28  PHE A HE2    1 
ATOM   441   H  HZ     . PHE A 1 29  ? 17.752  26.600  -2.067  1.00 31.01  ? 28  PHE A HZ     1 
ATOM   442   N  N      . VAL A 1 30  ? 21.038  25.139  2.316   1.00 34.07  ? 29  VAL A N      1 
ATOM   443   C  CA     . VAL A 1 30  ? 20.424  23.815  2.426   1.00 36.81  ? 29  VAL A CA     1 
ATOM   444   C  C      . VAL A 1 30  ? 19.522  23.631  1.204   1.00 36.20  ? 29  VAL A C      1 
ATOM   445   O  O      . VAL A 1 30  ? 18.447  24.210  1.110   1.00 33.66  ? 29  VAL A O      1 
ATOM   446   C  CB     . VAL A 1 30  ? 19.648  23.642  3.735   1.00 35.03  ? 29  VAL A CB     1 
ATOM   447   C  CG1    . VAL A 1 30  ? 20.577  23.814  4.931   1.00 35.35  ? 29  VAL A CG1    1 
ATOM   448   C  CG2    . VAL A 1 30  ? 18.470  24.614  3.811   1.00 36.93  ? 29  VAL A CG2    1 
ATOM   449   H  H      . VAL A 1 30  ? 20.659  25.736  2.805   1.00 40.92  ? 29  VAL A H      1 
ATOM   450   H  HA     . VAL A 1 30  ? 21.120  23.141  2.399   1.00 44.20  ? 29  VAL A HA     1 
ATOM   451   H  HB     . VAL A 1 30  ? 19.284  22.743  3.763   1.00 42.07  ? 29  VAL A HB     1 
ATOM   452   H  HG11   . VAL A 1 30  ? 20.077  23.651  5.745   1.00 42.46  ? 29  VAL A HG11   1 
ATOM   453   H  HG12   . VAL A 1 30  ? 21.307  23.180  4.857   1.00 42.46  ? 29  VAL A HG12   1 
ATOM   454   H  HG13   . VAL A 1 30  ? 20.925  24.720  4.932   1.00 42.46  ? 29  VAL A HG13   1 
ATOM   455   H  HG21   . VAL A 1 30  ? 18.240  24.759  4.742   1.00 44.35  ? 29  VAL A HG21   1 
ATOM   456   H  HG22   . VAL A 1 30  ? 18.726  25.454  3.399   1.00 44.35  ? 29  VAL A HG22   1 
ATOM   457   H  HG23   . VAL A 1 30  ? 17.714  24.231  3.340   1.00 44.35  ? 29  VAL A HG23   1 
ATOM   458   N  N      . ASP A 1 31  ? 19.974  22.827  0.260   1.00 31.22  ? 30  ASP A N      1 
ATOM   459   C  CA     . ASP A 1 31  ? 19.213  22.542  -0.946  1.00 36.33  ? 30  ASP A CA     1 
ATOM   460   C  C      . ASP A 1 31  ? 18.099  21.524  -0.709  1.00 35.77  ? 30  ASP A C      1 
ATOM   461   O  O      . ASP A 1 31  ? 17.099  21.548  -1.425  1.00 38.17  ? 30  ASP A O      1 
ATOM   462   C  CB     . ASP A 1 31  ? 20.188  22.068  -2.016  1.00 44.08  ? 30  ASP A CB     1 
ATOM   463   C  CG     . ASP A 1 31  ? 19.614  22.156  -3.384  1.00 46.28  ? 30  ASP A CG     1 
ATOM   464   O  OD1    . ASP A 1 31  ? 20.333  21.795  -4.340  1.00 60.32  ? 30  ASP A OD1    1 
ATOM   465   O  OD2    . ASP A 1 31  ? 18.439  22.572  -3.504  1.00 57.54  ? 30  ASP A OD2    1 
ATOM   466   H  H      . ASP A 1 31  ? 20.734  22.424  0.292   1.00 37.50  ? 30  ASP A H      1 
ATOM   467   H  HA     . ASP A 1 31  ? 18.774  23.342  -1.275  1.00 43.63  ? 30  ASP A HA     1 
ATOM   468   H  HB2    . ASP A 1 31  ? 20.985  22.621  -1.987  1.00 52.93  ? 30  ASP A HB2    1 
ATOM   469   H  HB3    . ASP A 1 31  ? 20.421  21.142  -1.846  1.00 52.93  ? 30  ASP A HB3    1 
ATOM   470   N  N      . GLU A 1 32  ? 18.218  20.691  0.311   1.00 33.02  ? 31  GLU A N      1 
ATOM   471   C  CA     . GLU A 1 32  ? 17.255  19.647  0.634   1.00 30.62  ? 31  GLU A CA     1 
ATOM   472   C  C      . GLU A 1 32  ? 16.146  20.190  1.529   1.00 30.94  ? 31  GLU A C      1 
ATOM   473   O  O      . GLU A 1 32  ? 16.282  21.243  2.159   1.00 29.61  ? 31  GLU A O      1 
ATOM   474   C  CB     . GLU A 1 32  ? 18.002  18.475  1.308   1.00 33.45  ? 31  GLU A CB     1 
ATOM   475   C  CG     . GLU A 1 32  ? 19.076  17.854  0.380   1.00 33.00  ? 31  GLU A CG     1 
ATOM   476   C  CD     . GLU A 1 32  ? 19.989  16.852  1.078   1.00 33.55  ? 31  GLU A CD     1 
ATOM   477   O  OE1    . GLU A 1 32  ? 20.084  16.903  2.313   1.00 33.23  ? 31  GLU A OE1    1 
ATOM   478   O  OE2    . GLU A 1 32  ? 20.619  16.010  0.387   1.00 37.22  ? 31  GLU A OE2    1 
ATOM   479   H  H      . GLU A 1 32  ? 18.879  20.710  0.860   1.00 39.66  ? 31  GLU A H      1 
ATOM   480   H  HA     . GLU A 1 32  ? 16.822  19.315  -0.168  1.00 36.77  ? 31  GLU A HA     1 
ATOM   481   H  HB2    . GLU A 1 32  ? 18.443  18.798  2.108   1.00 40.17  ? 31  GLU A HB2    1 
ATOM   482   H  HB3    . GLU A 1 32  ? 17.363  17.782  1.538   1.00 40.17  ? 31  GLU A HB3    1 
ATOM   483   H  HG2    . GLU A 1 32  ? 18.631  17.391  -0.347  1.00 39.64  ? 31  GLU A HG2    1 
ATOM   484   H  HG3    . GLU A 1 32  ? 19.633  18.566  0.028   1.00 39.64  ? 31  GLU A HG3    1 
ATOM   485   N  N      . TYR A 1 33  ? 15.014  19.475  1.551   1.00 24.67  ? 32  TYR A N      1 
ATOM   486   C  CA     . TYR A 1 33  ? 13.852  19.895  2.329   1.00 24.70  ? 32  TYR A CA     1 
ATOM   487   C  C      . TYR A 1 33  ? 13.776  19.052  3.588   1.00 23.42  ? 32  TYR A C      1 
ATOM   488   O  O      . TYR A 1 33  ? 13.447  17.857  3.523   1.00 20.92  ? 32  TYR A O      1 
ATOM   489   C  CB     . TYR A 1 33  ? 12.562  19.754  1.547   1.00 25.84  ? 32  TYR A CB     1 
ATOM   490   C  CG     . TYR A 1 33  ? 11.328  20.225  2.287   1.00 27.16  ? 32  TYR A CG     1 
ATOM   491   C  CD1    . TYR A 1 33  ? 11.364  21.345  3.110   1.00 27.06  ? 32  TYR A CD1    1 
ATOM   492   C  CD2    . TYR A 1 33  ? 10.128  19.530  2.177   1.00 25.15  ? 32  TYR A CD2    1 
ATOM   493   C  CE1    . TYR A 1 33  ? 10.220  21.780  3.780   1.00 27.32  ? 32  TYR A CE1    1 
ATOM   494   C  CE2    . TYR A 1 33  ? 8.993   19.954  2.838   1.00 28.60  ? 32  TYR A CE2    1 
ATOM   495   C  CZ     . TYR A 1 33  ? 9.050   21.075  3.641   1.00 29.55  ? 32  TYR A CZ     1 
ATOM   496   O  OH     . TYR A 1 33  ? 7.905   21.501  4.290   1.00 33.52  ? 32  TYR A OH     1 
ATOM   497   H  H      . TYR A 1 33  ? 14.899  18.740  1.119   1.00 29.64  ? 32  TYR A H      1 
ATOM   498   H  HA     . TYR A 1 33  ? 13.974  20.828  2.565   1.00 29.67  ? 32  TYR A HA     1 
ATOM   499   H  HB2    . TYR A 1 33  ? 12.634  20.279  0.734   1.00 31.04  ? 32  TYR A HB2    1 
ATOM   500   H  HB3    . TYR A 1 33  ? 12.433  18.818  1.327   1.00 31.04  ? 32  TYR A HB3    1 
ATOM   501   H  HD1    . TYR A 1 33  ? 12.162  21.812  3.216   1.00 32.51  ? 32  TYR A HD1    1 
ATOM   502   H  HD2    . TYR A 1 33  ? 10.090  18.766  1.648   1.00 30.21  ? 32  TYR A HD2    1 
ATOM   503   H  HE1    . TYR A 1 33  ? 10.250  22.539  4.316   1.00 32.82  ? 32  TYR A HE1    1 
ATOM   504   H  HE2    . TYR A 1 33  ? 8.195   19.487  2.743   1.00 34.35  ? 32  TYR A HE2    1 
ATOM   505   H  HH     . TYR A 1 33  ? 8.053   22.225  4.689   1.00 40.25  ? 32  TYR A HH     1 
ATOM   506   N  N      . ASP A 1 34  ? 14.079  19.676  4.744   1.00 26.67  ? 33  ASP A N      1 
ATOM   507   C  CA     . ASP A 1 34  ? 14.060  19.052  6.065   1.00 24.29  ? 33  ASP A CA     1 
ATOM   508   C  C      . ASP A 1 34  ? 13.044  19.856  6.876   1.00 27.57  ? 33  ASP A C      1 
ATOM   509   O  O      . ASP A 1 34  ? 13.408  20.825  7.564   1.00 22.58  ? 33  ASP A O      1 
ATOM   510   C  CB     . ASP A 1 34  ? 15.459  19.090  6.697   1.00 25.33  ? 33  ASP A CB     1 
ATOM   511   C  CG     . ASP A 1 34  ? 15.575  18.300  7.998   1.00 29.25  ? 33  ASP A CG     1 
ATOM   512   O  OD1    . ASP A 1 34  ? 14.640  17.568  8.389   1.00 28.97  ? 33  ASP A OD1    1 
ATOM   513   O  OD2    . ASP A 1 34  ? 16.647  18.408  8.654   1.00 34.45  ? 33  ASP A OD2    1 
ATOM   514   H  H      . ASP A 1 34  ? 14.308  20.504  4.780   1.00 32.04  ? 33  ASP A H      1 
ATOM   515   H  HA     . ASP A 1 34  ? 13.784  18.124  6.027   1.00 29.18  ? 33  ASP A HA     1 
ATOM   516   H  HB2    . ASP A 1 34  ? 16.095  18.715  6.068   1.00 30.43  ? 33  ASP A HB2    1 
ATOM   517   H  HB3    . ASP A 1 34  ? 15.688  20.012  6.891   1.00 30.43  ? 33  ASP A HB3    1 
ATOM   518   N  N      . PRO A 1 35  ? 11.759  19.527  6.774   1.00 23.30  ? 34  PRO A N      1 
ATOM   519   C  CA     . PRO A 1 35  ? 10.755  20.369  7.428   1.00 24.66  ? 34  PRO A CA     1 
ATOM   520   C  C      . PRO A 1 35  ? 11.008  20.378  8.921   1.00 23.48  ? 34  PRO A C      1 
ATOM   521   O  O      . PRO A 1 35  ? 11.265  19.339  9.527   1.00 23.33  ? 34  PRO A O      1 
ATOM   522   C  CB     . PRO A 1 35  ? 9.414   19.701  7.072   1.00 26.74  ? 34  PRO A CB     1 
ATOM   523   C  CG     . PRO A 1 35  ? 9.766   18.340  6.687   1.00 22.25  ? 34  PRO A CG     1 
ATOM   524   C  CD     . PRO A 1 35  ? 11.127  18.404  6.042   1.00 25.11  ? 34  PRO A CD     1 
ATOM   525   H  HA     . PRO A 1 35  ? 10.751  21.271  7.071   1.00 29.62  ? 34  PRO A HA     1 
ATOM   526   H  HB2    . PRO A 1 35  ? 8.828   19.703  7.845   1.00 32.12  ? 34  PRO A HB2    1 
ATOM   527   H  HB3    . PRO A 1 35  ? 8.994   20.173  6.336   1.00 32.12  ? 34  PRO A HB3    1 
ATOM   528   H  HG2    . PRO A 1 35  ? 9.791   17.777  7.476   1.00 26.73  ? 34  PRO A HG2    1 
ATOM   529   H  HG3    . PRO A 1 35  ? 9.109   18.002  6.058   1.00 26.73  ? 34  PRO A HG3    1 
ATOM   530   H  HD2    . PRO A 1 35  ? 11.618  17.578  6.176   1.00 30.17  ? 34  PRO A HD2    1 
ATOM   531   H  HD3    . PRO A 1 35  ? 11.058  18.598  5.095   1.00 30.17  ? 34  PRO A HD3    1 
ATOM   532   N  N      . THR A 1 36  ? 10.917  21.565  9.503   1.00 23.74  ? 35  THR A N      1 
ATOM   533   C  CA     . THR A 1 36  ? 11.400  21.815  10.863  1.00 19.20  ? 35  THR A CA     1 
ATOM   534   C  C      . THR A 1 36  ? 10.420  21.392  11.942  1.00 19.77  ? 35  THR A C      1 
ATOM   535   O  O      . THR A 1 36  ? 9.211   21.594  11.803  1.00 18.37  ? 35  THR A O      1 
ATOM   536   C  CB     . THR A 1 36  ? 11.680  23.321  10.967  1.00 17.30  ? 35  THR A CB     1 
ATOM   537   O  OG1    . THR A 1 36  ? 12.641  23.663  9.962   1.00 18.74  ? 35  THR A OG1    1 
ATOM   538   C  CG2    . THR A 1 36  ? 12.213  23.713  12.357  1.00 21.79  ? 35  THR A CG2    1 
ATOM   539   H  H      . THR A 1 36  ? 10.574  22.259  9.129   1.00 28.52  ? 35  THR A H      1 
ATOM   540   H  HA     . THR A 1 36  ? 12.198  21.290  11.031  1.00 23.08  ? 35  THR A HA     1 
ATOM   541   H  HB     . THR A 1 36  ? 10.858  23.818  10.836  1.00 20.80  ? 35  THR A HB     1 
ATOM   542   H  HG21   . THR A 1 36  ? 12.546  24.624  12.340  1.00 26.18  ? 35  THR A HG21   1 
ATOM   543   H  HG22   . THR A 1 36  ? 11.502  23.649  13.014  1.00 26.18  ? 35  THR A HG22   1 
ATOM   544   H  HG23   . THR A 1 36  ? 12.935  23.119  12.616  1.00 26.18  ? 35  THR A HG23   1 
ATOM   545   N  N      . ILE A 1 37  ? 10.946  20.846  13.048  1.00 18.30  ? 36  ILE A N      1 
ATOM   546   C  CA     . ILE A 1 37  ? 10.151  20.645  14.262  1.00 19.76  ? 36  ILE A CA     1 
ATOM   547   C  C      . ILE A 1 37  ? 10.293  21.945  15.064  1.00 20.85  ? 36  ILE A C      1 
ATOM   548   O  O      . ILE A 1 37  ? 9.350   22.738  15.195  1.00 21.16  ? 36  ILE A O      1 
ATOM   549   C  CB     . ILE A 1 37  ? 10.602  19.448  15.118  1.00 19.43  ? 36  ILE A CB     1 
ATOM   550   C  CG1    . ILE A 1 37  ? 10.623  18.131  14.366  1.00 25.06  ? 36  ILE A CG1    1 
ATOM   551   C  CG2    . ILE A 1 37  ? 9.738   19.375  16.392  1.00 22.09  ? 36  ILE A CG2    1 
ATOM   552   C  CD1    . ILE A 1 37  ? 9.341   17.714  13.908  1.00 22.07  ? 36  ILE A CD1    1 
ATOM   553   H  H      . ILE A 1 37  ? 11.762  20.584  13.117  1.00 22.00  ? 36  ILE A H      1 
ATOM   554   H  HA     . ILE A 1 37  ? 9.232   20.458  14.014  1.00 23.75  ? 36  ILE A HA     1 
ATOM   555   H  HB     . ILE A 1 37  ? 11.528  19.603  15.363  1.00 23.35  ? 36  ILE A HB     1 
ATOM   556   H  HG12   . ILE A 1 37  ? 11.200  18.223  13.591  1.00 30.11  ? 36  ILE A HG12   1 
ATOM   557   H  HG13   . ILE A 1 37  ? 10.967  17.441  14.955  1.00 30.11  ? 36  ILE A HG13   1 
ATOM   558   H  HG21   . ILE A 1 37  ? 9.874   18.514  16.817  1.00 26.54  ? 36  ILE A HG21   1 
ATOM   559   H  HG22   . ILE A 1 37  ? 10.004  20.087  16.995  1.00 26.54  ? 36  ILE A HG22   1 
ATOM   560   H  HG23   . ILE A 1 37  ? 8.805   19.480  16.148  1.00 26.54  ? 36  ILE A HG23   1 
ATOM   561   H  HD11   . ILE A 1 37  ? 9.433   16.874  13.433  1.00 26.52  ? 36  ILE A HD11   1 
ATOM   562   H  HD12   . ILE A 1 37  ? 8.755   17.600  14.672  1.00 26.52  ? 36  ILE A HD12   1 
ATOM   563   H  HD13   . ILE A 1 37  ? 8.982   18.392  13.314  1.00 26.52  ? 36  ILE A HD13   1 
ATOM   564   N  N      . GLU A 1 38  ? 11.516  22.183  15.562  1.00 21.11  ? 37  GLU A N      1 
ATOM   565   C  CA     . GLU A 1 38  ? 11.871  23.432  16.231  1.00 22.65  ? 37  GLU A CA     1 
ATOM   566   C  C      . GLU A 1 38  ? 13.383  23.395  16.424  1.00 20.90  ? 37  GLU A C      1 
ATOM   567   O  O      . GLU A 1 38  ? 13.904  22.361  16.851  1.00 20.93  ? 37  GLU A O      1 
ATOM   568   C  CB     . GLU A 1 38  ? 11.184  23.587  17.592  1.00 21.26  ? 37  GLU A CB     1 
ATOM   569   C  CG     . GLU A 1 38  ? 11.357  25.008  18.153  1.00 24.26  ? 37  GLU A CG     1 
ATOM   570   C  CD     . GLU A 1 38  ? 10.887  25.127  19.589  1.00 33.93  ? 37  GLU A CD     1 
ATOM   571   O  OE1    . GLU A 1 38  ? 9.692   25.359  19.802  1.00 40.22  ? 37  GLU A OE1    1 
ATOM   572   O  OE2    . GLU A 1 38  ? 11.721  24.987  20.500  1.00 36.59  ? 37  GLU A OE2    1 
ATOM   573   H  H      . GLU A 1 38  ? 12.167  21.623  15.522  1.00 25.37  ? 37  GLU A H      1 
ATOM   574   H  HA     . GLU A 1 38  ? 11.582  24.193  15.702  1.00 27.21  ? 37  GLU A HA     1 
ATOM   575   H  HB2    . GLU A 1 38  ? 10.236  23.411  17.495  1.00 25.54  ? 37  GLU A HB2    1 
ATOM   576   H  HB3    . GLU A 1 38  ? 11.576  22.961  18.221  1.00 25.54  ? 37  GLU A HB3    1 
ATOM   577   H  HG2    . GLU A 1 38  ? 12.297  25.248  18.123  1.00 29.15  ? 37  GLU A HG2    1 
ATOM   578   H  HG3    . GLU A 1 38  ? 10.839  25.626  17.614  1.00 29.15  ? 37  GLU A HG3    1 
ATOM   579   N  N      . ASP A 1 39  ? 14.093  24.478  16.085  1.00 19.97  ? 38  ASP A N      1 
ATOM   580   C  CA     . ASP A 1 39  ? 15.540  24.532  16.245  1.00 18.67  ? 38  ASP A CA     1 
ATOM   581   C  C      . ASP A 1 39  ? 15.892  25.910  16.781  1.00 21.34  ? 38  ASP A C      1 
ATOM   582   O  O      . ASP A 1 39  ? 15.293  26.907  16.382  1.00 20.11  ? 38  ASP A O      1 
ATOM   583   C  CB     . ASP A 1 39  ? 16.256  24.279  14.942  1.00 21.08  ? 38  ASP A CB     1 
ATOM   584   C  CG     . ASP A 1 39  ? 16.081  22.822  14.481  1.00 22.98  ? 38  ASP A CG     1 
ATOM   585   O  OD1    . ASP A 1 39  ? 16.617  21.906  15.144  1.00 22.90  ? 38  ASP A OD1    1 
ATOM   586   O  OD2    . ASP A 1 39  ? 15.318  22.618  13.550  1.00 23.32  ? 38  ASP A OD2    1 
ATOM   587   H  H      . ASP A 1 39  ? 13.752  25.196  15.758  1.00 23.99  ? 38  ASP A H      1 
ATOM   588   H  HA     . ASP A 1 39  ? 15.839  23.858  16.876  1.00 22.43  ? 38  ASP A HA     1 
ATOM   589   H  HB2    . ASP A 1 39  ? 15.894  24.863  14.258  1.00 25.33  ? 38  ASP A HB2    1 
ATOM   590   H  HB3    . ASP A 1 39  ? 17.204  24.452  15.058  1.00 25.33  ? 38  ASP A HB3    1 
ATOM   591   N  N      . SER A 1 40  ? 16.930  25.953  17.611  1.00 21.13  ? 39  SER A N      1 
ATOM   592   C  CA     . SER A 1 40  ? 17.467  27.184  18.161  1.00 19.26  ? 39  SER A CA     1 
ATOM   593   C  C      . SER A 1 40  ? 18.953  27.301  17.838  1.00 21.93  ? 39  SER A C      1 
ATOM   594   O  O      . SER A 1 40  ? 19.687  26.312  17.779  1.00 20.88  ? 39  SER A O      1 
ATOM   595   C  CB     . SER A 1 40  ? 17.292  27.265  19.700  1.00 24.29  ? 39  SER A CB     1 
ATOM   596   O  OG     . SER A 1 40  ? 15.954  27.482  20.055  1.00 33.30  ? 39  SER A OG     1 
ATOM   597   H  H      . SER A 1 40  ? 17.353  25.253  17.878  1.00 25.39  ? 39  SER A H      1 
ATOM   598   H  HA     . SER A 1 40  ? 16.992  27.927  17.757  1.00 23.14  ? 39  SER A HA     1 
ATOM   599   H  HB2    . SER A 1 40  ? 17.588  26.429  20.093  1.00 29.18  ? 39  SER A HB2    1 
ATOM   600   H  HB3    . SER A 1 40  ? 17.828  27.999  20.038  1.00 29.18  ? 39  SER A HB3    1 
ATOM   601   H  HG     . SER A 1 40  ? 15.887  27.565  20.888  1.00 39.99  ? 39  SER A HG     1 
ATOM   602   N  N      . TYR A 1 41  ? 19.384  28.537  17.622  1.00 21.41  ? 40  TYR A N      1 
ATOM   603   C  CA     . TYR A 1 41  ? 20.769  28.823  17.241  1.00 20.54  ? 40  TYR A CA     1 
ATOM   604   C  C      . TYR A 1 41  ? 21.244  30.065  17.967  1.00 20.69  ? 40  TYR A C      1 
ATOM   605   O  O      . TYR A 1 41  ? 20.436  30.885  18.410  1.00 20.39  ? 40  TYR A O      1 
ATOM   606   C  CB     . TYR A 1 41  ? 20.913  29.044  15.740  1.00 21.93  ? 40  TYR A CB     1 
ATOM   607   C  CG     . TYR A 1 41  ? 20.407  27.886  14.918  1.00 20.50  ? 40  TYR A CG     1 
ATOM   608   C  CD1    . TYR A 1 41  ? 21.261  26.848  14.567  1.00 22.16  ? 40  TYR A CD1    1 
ATOM   609   C  CD2    . TYR A 1 41  ? 19.091  27.841  14.483  1.00 18.82  ? 40  TYR A CD2    1 
ATOM   610   C  CE1    . TYR A 1 41  ? 20.825  25.788  13.814  1.00 24.08  ? 40  TYR A CE1    1 
ATOM   611   C  CE2    . TYR A 1 41  ? 18.634  26.762  13.709  1.00 20.79  ? 40  TYR A CE2    1 
ATOM   612   C  CZ     . TYR A 1 41  ? 19.515  25.738  13.401  1.00 26.20  ? 40  TYR A CZ     1 
ATOM   613   O  OH     . TYR A 1 41  ? 19.151  24.666  12.636  1.00 24.14  ? 40  TYR A OH     1 
ATOM   614   H  H      . TYR A 1 41  ? 18.890  29.238  17.689  1.00 25.73  ? 40  TYR A H      1 
ATOM   615   H  HA     . TYR A 1 41  ? 21.322  28.070  17.503  1.00 24.69  ? 40  TYR A HA     1 
ATOM   616   H  HB2    . TYR A 1 41  ? 20.408  29.832  15.488  1.00 26.35  ? 40  TYR A HB2    1 
ATOM   617   H  HB3    . TYR A 1 41  ? 21.852  29.171  15.530  1.00 26.35  ? 40  TYR A HB3    1 
ATOM   618   H  HD1    . TYR A 1 41  ? 22.147  26.872  14.849  1.00 26.62  ? 40  TYR A HD1    1 
ATOM   619   H  HD2    . TYR A 1 41  ? 18.507  28.529  14.706  1.00 22.62  ? 40  TYR A HD2    1 
ATOM   620   H  HE1    . TYR A 1 41  ? 21.413  25.106  13.584  1.00 28.93  ? 40  TYR A HE1    1 
ATOM   621   H  HE2    . TYR A 1 41  ? 17.755  26.735  13.407  1.00 24.98  ? 40  TYR A HE2    1 
ATOM   622   H  HH     . TYR A 1 41  ? 18.380  24.784  12.324  1.00 29.00  ? 40  TYR A HH     1 
ATOM   623   N  N      . ARG A 1 42  ? 22.592  30.210  18.038  1.00 21.52  ? 41  ARG A N      1 
ATOM   624   C  CA     . ARG A 1 42  ? 23.248  31.370  18.631  1.00 21.54  ? 41  ARG A CA     1 
ATOM   625   C  C      . ARG A 1 42  ? 24.340  31.873  17.696  1.00 17.39  ? 41  ARG A C      1 
ATOM   626   O  O      . ARG A 1 42  ? 25.090  31.071  17.129  1.00 18.95  ? 41  ARG A O      1 
ATOM   627   C  CB     . ARG A 1 42  ? 23.905  31.029  19.968  1.00 23.03  ? 41  ARG A CB     1 
ATOM   628   C  CG     . ARG A 1 42  ? 22.929  30.815  21.139  1.00 24.67  ? 41  ARG A CG     1 
ATOM   629   C  CD     . ARG A 1 42  ? 22.409  32.124  21.634  1.00 27.25  ? 41  ARG A CD     1 
ATOM   630   N  NE     . ARG A 1 42  ? 21.507  32.030  22.778  1.00 29.54  ? 41  ARG A NE     1 
ATOM   631   C  CZ     . ARG A 1 42  ? 21.897  32.163  24.037  1.00 31.21  ? 41  ARG A CZ     1 
ATOM   632   N  NH1    . ARG A 1 42  ? 23.166  32.102  24.367  1.00 29.18  ? 41  ARG A NH1    1 
ATOM   633   N  NH2    . ARG A 1 42  ? 20.983  32.341  24.992  1.00 35.40  ? 41  ARG A NH2    1 
ATOM   634   H  H      . ARG A 1 42  ? 23.148  29.626  17.739  1.00 25.85  ? 41  ARG A H      1 
ATOM   635   H  HA     . ARG A 1 42  ? 22.582  32.063  18.765  1.00 25.88  ? 41  ARG A HA     1 
ATOM   636   H  HB2    . ARG A 1 42  ? 24.412  30.209  19.860  1.00 27.66  ? 41  ARG A HB2    1 
ATOM   637   H  HB3    . ARG A 1 42  ? 24.497  31.757  20.213  1.00 27.66  ? 41  ARG A HB3    1 
ATOM   638   H  HG2    . ARG A 1 42  ? 22.179  30.277  20.842  1.00 29.64  ? 41  ARG A HG2    1 
ATOM   639   H  HG3    . ARG A 1 42  ? 23.390  30.370  21.868  1.00 29.64  ? 41  ARG A HG3    1 
ATOM   640   H  HD2    . ARG A 1 42  ? 23.161  32.674  21.901  1.00 32.73  ? 41  ARG A HD2    1 
ATOM   641   H  HD3    . ARG A 1 42  ? 21.922  32.554  20.914  1.00 32.73  ? 41  ARG A HD3    1 
ATOM   642   H  HE     . ARG A 1 42  ? 20.674  31.881  22.625  1.00 35.48  ? 41  ARG A HE     1 
ATOM   643   H  HH11   . ARG A 1 42  ? 23.762  31.975  23.760  1.00 35.05  ? 41  ARG A HH11   1 
ATOM   644   H  HH12   . ARG A 1 42  ? 23.401  32.190  25.189  1.00 35.05  ? 41  ARG A HH12   1 
ATOM   645   H  HH21   . ARG A 1 42  ? 20.148  32.370  24.788  1.00 42.51  ? 41  ARG A HH21   1 
ATOM   646   H  HH22   . ARG A 1 42  ? 21.228  32.428  25.812  1.00 42.51  ? 41  ARG A HH22   1 
ATOM   647   N  N      . LYS A 1 43  ? 24.414  33.187  17.516  1.00 19.33  ? 42  LYS A N      1 
ATOM   648   C  CA     . LYS A 1 43  ? 25.493  33.773  16.724  1.00 19.73  ? 42  LYS A CA     1 
ATOM   649   C  C      . LYS A 1 43  ? 25.767  35.183  17.228  1.00 19.63  ? 42  LYS A C      1 
ATOM   650   O  O      . LYS A 1 43  ? 24.845  35.987  17.374  1.00 24.16  ? 42  LYS A O      1 
ATOM   651   C  CB     . LYS A 1 43  ? 25.151  33.833  15.240  1.00 22.00  ? 42  LYS A CB     1 
ATOM   652   C  CG     . LYS A 1 43  ? 26.265  34.474  14.374  1.00 23.42  ? 42  LYS A CG     1 
ATOM   653   C  CD     . LYS A 1 43  ? 25.817  34.846  12.976  1.00 24.33  ? 42  LYS A CD     1 
ATOM   654   C  CE     . LYS A 1 43  ? 27.046  34.857  12.044  1.00 27.68  ? 42  LYS A CE     1 
ATOM   655   N  NZ     . LYS A 1 43  ? 26.745  35.301  10.654  1.00 32.81  ? 42  LYS A NZ     1 
ATOM   656   H  H      . LYS A 1 43  ? 23.857  33.758  17.840  1.00 23.23  ? 42  LYS A H      1 
ATOM   657   H  HA     . LYS A 1 43  ? 26.286  33.226  16.837  1.00 23.71  ? 42  LYS A HA     1 
ATOM   658   H  HB2    . LYS A 1 43  ? 25.004  32.931  14.916  1.00 26.44  ? 42  LYS A HB2    1 
ATOM   659   H  HB3    . LYS A 1 43  ? 24.345  34.362  15.126  1.00 26.44  ? 42  LYS A HB3    1 
ATOM   660   H  HG2    . LYS A 1 43  ? 26.573  35.283  14.810  1.00 28.14  ? 42  LYS A HG2    1 
ATOM   661   H  HG3    . LYS A 1 43  ? 26.997  33.843  14.291  1.00 28.14  ? 42  LYS A HG3    1 
ATOM   662   H  HD2    . LYS A 1 43  ? 25.178  34.194  12.648  1.00 29.23  ? 42  LYS A HD2    1 
ATOM   663   H  HD3    . LYS A 1 43  ? 25.417  35.730  12.981  1.00 29.23  ? 42  LYS A HD3    1 
ATOM   664   H  HE2    . LYS A 1 43  ? 27.710  35.462  12.409  1.00 33.25  ? 42  LYS A HE2    1 
ATOM   665   H  HE3    . LYS A 1 43  ? 27.407  33.958  11.994  1.00 33.25  ? 42  LYS A HE3    1 
ATOM   666   H  HZ1    . LYS A 1 43  ? 27.487  35.285  10.163  1.00 39.40  ? 42  LYS A HZ1    1 
ATOM   667   H  HZ2    . LYS A 1 43  ? 26.143  34.759  10.285  1.00 39.40  ? 42  LYS A HZ2    1 
ATOM   668   H  HZ3    . LYS A 1 43  ? 26.421  36.130  10.663  1.00 39.40  ? 42  LYS A HZ3    1 
ATOM   669   N  N      . GLN A 1 44  ? 27.038  35.507  17.428  1.00 23.35  ? 43  GLN A N      1 
ATOM   670   C  CA     . GLN A 1 44  ? 27.400  36.873  17.772  1.00 24.34  ? 43  GLN A CA     1 
ATOM   671   C  C      . GLN A 1 44  ? 27.755  37.622  16.494  1.00 23.41  ? 43  GLN A C      1 
ATOM   672   O  O      . GLN A 1 44  ? 28.421  37.086  15.596  1.00 26.18  ? 43  GLN A O      1 
ATOM   673   C  CB     . GLN A 1 44  ? 28.561  36.904  18.765  1.00 26.75  ? 43  GLN A CB     1 
ATOM   674   C  CG     . GLN A 1 44  ? 29.852  36.384  18.247  1.00 28.11  ? 43  GLN A CG     1 
ATOM   675   C  CD     . GLN A 1 44  ? 31.018  36.771  19.161  1.00 29.51  ? 43  GLN A CD     1 
ATOM   676   O  OE1    . GLN A 1 44  ? 31.203  37.942  19.479  1.00 26.32  ? 43  GLN A OE1    1 
ATOM   677   N  NE2    . GLN A 1 44  ? 31.758  35.781  19.622  1.00 27.08  ? 43  GLN A NE2    1 
ATOM   678   H  H      . GLN A 1 44  ? 27.699  34.960  17.371  1.00 28.05  ? 43  GLN A H      1 
ATOM   679   H  HA     . GLN A 1 44  ? 26.655  37.321  18.203  1.00 29.24  ? 43  GLN A HA     1 
ATOM   680   H  HB2    . GLN A 1 44  ? 28.708  37.824  19.035  1.00 32.14  ? 43  GLN A HB2    1 
ATOM   681   H  HB3    . GLN A 1 44  ? 28.320  36.366  19.535  1.00 32.14  ? 43  GLN A HB3    1 
ATOM   682   H  HG2    . GLN A 1 44  ? 29.811  35.416  18.197  1.00 33.77  ? 43  GLN A HG2    1 
ATOM   683   H  HG3    . GLN A 1 44  ? 30.017  36.754  17.366  1.00 33.77  ? 43  GLN A HG3    1 
ATOM   684   H  HE21   . GLN A 1 44  ? 31.574  34.969  19.405  1.00 32.53  ? 43  GLN A HE21   1 
ATOM   685   H  HE22   . GLN A 1 44  ? 32.425  35.947  20.139  1.00 32.53  ? 43  GLN A HE22   1 
ATOM   686   N  N      . VAL A 1 45  ? 27.277  38.862  16.402  1.00 22.86  ? 44  VAL A N      1 
ATOM   687   C  CA     . VAL A 1 45  ? 27.511  39.678  15.208  1.00 29.49  ? 44  VAL A CA     1 
ATOM   688   C  C      . VAL A 1 45  ? 27.759  41.120  15.644  1.00 32.41  ? 44  VAL A C      1 
ATOM   689   O  O      . VAL A 1 45  ? 27.351  41.534  16.722  1.00 32.05  ? 44  VAL A O      1 
ATOM   690   C  CB     . VAL A 1 45  ? 26.322  39.665  14.233  1.00 29.84  ? 44  VAL A CB     1 
ATOM   691   C  CG1    . VAL A 1 45  ? 26.002  38.256  13.739  1.00 27.93  ? 44  VAL A CG1    1 
ATOM   692   C  CG2    . VAL A 1 45  ? 25.120  40.253  14.913  1.00 25.44  ? 44  VAL A CG2    1 
ATOM   693   H  H      . VAL A 1 45  ? 26.816  39.253  17.015  1.00 27.47  ? 44  VAL A H      1 
ATOM   694   H  HA     . VAL A 1 45  ? 28.294  39.332  14.753  1.00 35.43  ? 44  VAL A HA     1 
ATOM   695   H  HB     . VAL A 1 45  ? 26.558  40.194  13.455  1.00 35.84  ? 44  VAL A HB     1 
ATOM   696   H  HG11   . VAL A 1 45  ? 25.270  38.303  13.104  1.00 33.55  ? 44  VAL A HG11   1 
ATOM   697   H  HG12   . VAL A 1 45  ? 26.789  37.886  13.310  1.00 33.55  ? 44  VAL A HG12   1 
ATOM   698   H  HG13   . VAL A 1 45  ? 25.748  37.706  14.496  1.00 33.55  ? 44  VAL A HG13   1 
ATOM   699   H  HG21   . VAL A 1 45  ? 24.338  40.101  14.358  1.00 30.57  ? 44  VAL A HG21   1 
ATOM   700   H  HG22   . VAL A 1 45  ? 25.002  39.823  15.774  1.00 30.57  ? 44  VAL A HG22   1 
ATOM   701   H  HG23   . VAL A 1 45  ? 25.260  41.205  15.034  1.00 30.57  ? 44  VAL A HG23   1 
ATOM   702   N  N      . VAL A 1 46  ? 28.376  41.908  14.764  1.00 29.60  ? 45  VAL A N      1 
ATOM   703   C  CA     . VAL A 1 46  ? 28.492  43.348  14.976  1.00 35.98  ? 45  VAL A CA     1 
ATOM   704   C  C      . VAL A 1 46  ? 27.425  44.050  14.148  1.00 36.39  ? 45  VAL A C      1 
ATOM   705   O  O      . VAL A 1 46  ? 27.438  43.958  12.915  1.00 37.65  ? 45  VAL A O      1 
ATOM   706   C  CB     . VAL A 1 46  ? 29.889  43.867  14.601  1.00 39.31  ? 45  VAL A CB     1 
ATOM   707   C  CG1    . VAL A 1 46  ? 29.961  45.361  14.900  1.00 43.30  ? 45  VAL A CG1    1 
ATOM   708   C  CG2    . VAL A 1 46  ? 30.955  43.128  15.347  1.00 39.83  ? 45  VAL A CG2    1 
ATOM   709   H  H      . VAL A 1 46  ? 28.737  41.629  14.035  1.00 35.56  ? 45  VAL A H      1 
ATOM   710   H  HA     . VAL A 1 46  ? 28.329  43.536  15.913  1.00 43.21  ? 45  VAL A HA     1 
ATOM   711   H  HB     . VAL A 1 46  ? 30.046  43.721  13.655  1.00 47.20  ? 45  VAL A HB     1 
ATOM   712   H  HG11   . VAL A 1 46  ? 30.887  45.647  14.857  1.00 51.99  ? 45  VAL A HG11   1 
ATOM   713   H  HG12   . VAL A 1 46  ? 29.436  45.840  14.241  1.00 51.99  ? 45  VAL A HG12   1 
ATOM   714   H  HG13   . VAL A 1 46  ? 29.606  45.522  15.788  1.00 51.99  ? 45  VAL A HG13   1 
ATOM   715   H  HG21   . VAL A 1 46  ? 31.818  43.519  15.135  1.00 47.83  ? 45  VAL A HG21   1 
ATOM   716   H  HG22   . VAL A 1 46  ? 30.783  43.201  16.299  1.00 47.83  ? 45  VAL A HG22   1 
ATOM   717   H  HG23   . VAL A 1 46  ? 30.940  42.196  15.079  1.00 47.83  ? 45  VAL A HG23   1 
ATOM   718   N  N      . ILE A 1 47  ? 26.521  44.762  14.814  1.00 37.05  ? 46  ILE A N      1 
ATOM   719   C  CA     . ILE A 1 47  ? 25.511  45.588  14.156  1.00 37.13  ? 46  ILE A CA     1 
ATOM   720   C  C      . ILE A 1 47  ? 25.729  47.031  14.604  1.00 44.01  ? 46  ILE A C      1 
ATOM   721   O  O      . ILE A 1 47  ? 25.641  47.333  15.797  1.00 44.36  ? 46  ILE A O      1 
ATOM   722   C  CB     . ILE A 1 47  ? 24.086  45.126  14.494  1.00 34.19  ? 46  ILE A CB     1 
ATOM   723   C  CG1    . ILE A 1 47  ? 23.879  43.668  14.036  1.00 32.11  ? 46  ILE A CG1    1 
ATOM   724   C  CG2    . ILE A 1 47  ? 23.051  46.012  13.839  1.00 34.08  ? 46  ILE A CG2    1 
ATOM   725   C  CD1    . ILE A 1 47  ? 22.560  43.046  14.523  1.00 29.12  ? 46  ILE A CD1    1 
ATOM   726   H  H      . ILE A 1 47  ? 26.470  44.783  15.672  1.00 44.49  ? 46  ILE A H      1 
ATOM   727   H  HA     . ILE A 1 47  ? 25.631  45.537  13.195  1.00 44.59  ? 46  ILE A HA     1 
ATOM   728   H  HB     . ILE A 1 47  ? 23.979  45.186  15.456  1.00 41.07  ? 46  ILE A HB     1 
ATOM   729   H  HG12   . ILE A 1 47  ? 23.878  43.643  13.067  1.00 38.56  ? 46  ILE A HG12   1 
ATOM   730   H  HG13   . ILE A 1 47  ? 24.606  43.127  14.381  1.00 38.56  ? 46  ILE A HG13   1 
ATOM   731   H  HG21   . ILE A 1 47  ? 22.168  45.664  14.036  1.00 40.92  ? 46  ILE A HG21   1 
ATOM   732   H  HG22   . ILE A 1 47  ? 23.138  46.912  14.189  1.00 40.92  ? 46  ILE A HG22   1 
ATOM   733   H  HG23   . ILE A 1 47  ? 23.199  46.014  12.880  1.00 40.92  ? 46  ILE A HG23   1 
ATOM   734   H  HD11   . ILE A 1 47  ? 22.584  42.090  14.363  1.00 34.98  ? 46  ILE A HD11   1 
ATOM   735   H  HD12   . ILE A 1 47  ? 22.459  43.221  15.472  1.00 34.98  ? 46  ILE A HD12   1 
ATOM   736   H  HD13   . ILE A 1 47  ? 21.823  43.445  14.034  1.00 34.98  ? 46  ILE A HD13   1 
ATOM   737   N  N      . ASP A 1 48  ? 25.998  47.922  13.656  1.00 41.16  ? 47  ASP A N      1 
ATOM   738   C  CA     . ASP A 1 48  ? 26.216  49.333  13.989  1.00 40.89  ? 47  ASP A CA     1 
ATOM   739   C  C      . ASP A 1 48  ? 27.361  49.477  14.992  1.00 43.54  ? 47  ASP A C      1 
ATOM   740   O  O      . ASP A 1 48  ? 27.265  50.180  15.999  1.00 44.32  ? 47  ASP A O      1 
ATOM   741   C  CB     . ASP A 1 48  ? 24.922  49.967  14.504  1.00 40.39  ? 47  ASP A CB     1 
ATOM   742   C  CG     . ASP A 1 48  ? 23.856  50.033  13.426  1.00 38.49  ? 47  ASP A CG     1 
ATOM   743   O  OD1    . ASP A 1 48  ? 24.247  49.988  12.245  1.00 38.59  ? 47  ASP A OD1    1 
ATOM   744   O  OD2    . ASP A 1 48  ? 22.649  50.105  13.743  1.00 43.41  ? 47  ASP A OD2    1 
ATOM   745   H  H      . ASP A 1 48  ? 26.060  47.738  12.818  1.00 49.43  ? 47  ASP A H      1 
ATOM   746   H  HA     . ASP A 1 48  ? 26.478  49.816  13.189  1.00 49.10  ? 47  ASP A HA     1 
ATOM   747   H  HB2    . ASP A 1 48  ? 24.577  49.437  15.240  1.00 48.50  ? 47  ASP A HB2    1 
ATOM   748   H  HB3    . ASP A 1 48  ? 25.106  50.871  14.805  1.00 48.50  ? 47  ASP A HB3    1 
ATOM   749   N  N      . GLY A 1 49  ? 28.466  48.804  14.696  1.00 43.25  ? 48  GLY A N      1 
ATOM   750   C  CA     . GLY A 1 49  ? 29.616  48.834  15.566  1.00 45.41  ? 48  GLY A CA     1 
ATOM   751   C  C      . GLY A 1 49  ? 29.418  48.243  16.948  1.00 47.05  ? 48  GLY A C      1 
ATOM   752   O  O      . GLY A 1 49  ? 30.357  48.267  17.750  1.00 49.66  ? 48  GLY A O      1 
ATOM   753   H  H      . GLY A 1 49  ? 28.569  48.323  13.991  1.00 51.94  ? 48  GLY A H      1 
ATOM   754   H  HA2    . GLY A 1 49  ? 30.336  48.342  15.141  1.00 54.53  ? 48  GLY A HA2    1 
ATOM   755   H  HA3    . GLY A 1 49  ? 29.890  49.757  15.682  1.00 54.53  ? 48  GLY A HA3    1 
ATOM   756   N  N      . GLU A 1 50  ? 28.232  47.703  17.246  1.00 46.52  ? 49  GLU A N      1 
ATOM   757   C  CA     . GLU A 1 50  ? 27.934  47.104  18.547  1.00 45.91  ? 49  GLU A CA     1 
ATOM   758   C  C      . GLU A 1 50  ? 27.872  45.587  18.396  1.00 45.34  ? 49  GLU A C      1 
ATOM   759   O  O      . GLU A 1 50  ? 27.105  45.072  17.565  1.00 41.48  ? 49  GLU A O      1 
ATOM   760   C  CB     . GLU A 1 50  ? 26.610  47.604  19.119  1.00 46.29  ? 49  GLU A CB     1 
ATOM   761   C  CG     . GLU A 1 50  ? 26.399  49.108  19.070  1.00 54.70  ? 49  GLU A CG     1 
ATOM   762   C  CD     . GLU A 1 50  ? 26.741  49.778  20.390  1.00 63.52  ? 49  GLU A CD     1 
ATOM   763   O  OE1    . GLU A 1 50  ? 25.810  50.027  21.186  1.00 65.69  ? 49  GLU A OE1    1 
ATOM   764   O  OE2    . GLU A 1 50  ? 27.943  50.043  20.633  1.00 64.14  ? 49  GLU A OE2    1 
ATOM   765   H  H      . GLU A 1 50  ? 27.571  47.673  16.696  1.00 55.86  ? 49  GLU A H      1 
ATOM   766   H  HA     . GLU A 1 50  ? 28.648  47.343  19.158  1.00 55.13  ? 49  GLU A HA     1 
ATOM   767   H  HB2    . GLU A 1 50  ? 25.887  47.195  18.617  1.00 55.59  ? 49  GLU A HB2    1 
ATOM   768   H  HB3    . GLU A 1 50  ? 26.560  47.337  20.050  1.00 55.59  ? 49  GLU A HB3    1 
ATOM   769   H  HG2    . GLU A 1 50  ? 26.968  49.487  18.382  1.00 65.67  ? 49  GLU A HG2    1 
ATOM   770   H  HG3    . GLU A 1 50  ? 25.468  49.293  18.870  1.00 65.67  ? 49  GLU A HG3    1 
ATOM   771   N  N      . THR A 1 51  ? 28.679  44.876  19.188  1.00 40.48  ? 50  THR A N      1 
ATOM   772   C  CA     . THR A 1 51  ? 28.614  43.420  19.196  1.00 38.56  ? 50  THR A CA     1 
ATOM   773   C  C      . THR A 1 51  ? 27.425  42.987  20.045  1.00 37.04  ? 50  THR A C      1 
ATOM   774   O  O      . THR A 1 51  ? 27.218  43.521  21.131  1.00 35.27  ? 50  THR A O      1 
ATOM   775   C  CB     . THR A 1 51  ? 29.902  42.811  19.738  1.00 39.45  ? 50  THR A CB     1 
ATOM   776   O  OG1    . THR A 1 51  ? 31.028  43.318  19.011  1.00 41.75  ? 50  THR A OG1    1 
ATOM   777   C  CG2    . THR A 1 51  ? 29.877  41.298  19.591  1.00 37.44  ? 50  THR A CG2    1 
ATOM   778   H  H      . THR A 1 51  ? 29.264  45.212  19.722  1.00 48.61  ? 50  THR A H      1 
ATOM   779   H  HA     . THR A 1 51  ? 28.503  43.092  18.290  1.00 46.31  ? 50  THR A HA     1 
ATOM   780   H  HB     . THR A 1 51  ? 29.987  43.039  20.677  1.00 47.38  ? 50  THR A HB     1 
ATOM   781   H  HG1    . THR A 1 51  ? 31.737  42.972  19.300  1.00 50.14  ? 50  THR A HG1    1 
ATOM   782   H  HG21   . THR A 1 51  ? 30.731  40.925  19.857  1.00 44.97  ? 50  THR A HG21   1 
ATOM   783   H  HG22   . THR A 1 51  ? 29.180  40.922  20.152  1.00 44.97  ? 50  THR A HG22   1 
ATOM   784   H  HG23   . THR A 1 51  ? 29.702  41.057  18.668  1.00 44.97  ? 50  THR A HG23   1 
ATOM   785   N  N      . CYS A 1 52  ? 26.633  42.041  19.528  1.00 31.08  ? 51  CYS A N      1 
ATOM   786   C  CA     . CYS A 1 52  ? 25.521  41.473  20.252  1.00 34.96  ? 51  CYS A CA     1 
ATOM   787   C  C      . CYS A 1 52  ? 25.394  39.987  19.932  1.00 27.22  ? 51  CYS A C      1 
ATOM   788   O  O      . CYS A 1 52  ? 26.060  39.459  19.039  1.00 28.13  ? 51  CYS A O      1 
ATOM   789   C  CB     . CYS A 1 52  ? 24.205  42.183  19.921  1.00 36.03  ? 51  CYS A CB     1 
ATOM   790   S  SG     . CYS A 1 52  ? 23.907  42.143  18.183  1.00 37.53  ? 51  CYS A SG     1 
ATOM   791   H  H      . CYS A 1 52  ? 26.731  41.713  18.740  1.00 37.33  ? 51  CYS A H      1 
ATOM   792   H  HA     . CYS A 1 52  ? 25.702  41.567  21.200  1.00 41.98  ? 51  CYS A HA     1 
ATOM   793   H  HB2    . CYS A 1 52  ? 23.472  41.735  20.373  1.00 43.28  ? 51  CYS A HB2    1 
ATOM   794   H  HB3    . CYS A 1 52  ? 24.254  43.109  20.207  1.00 43.28  ? 51  CYS A HB3    1 
ATOM   795   H  HG     . CYS A 1 52  ? 22.883  42.722  17.948  1.00 45.06  ? 51  CYS A HG     1 
ATOM   796   N  N      . LEU A 1 53  ? 24.521  39.329  20.685  1.00 26.57  ? 52  LEU A N      1 
ATOM   797   C  CA     . LEU A 1 53  ? 24.300  37.891  20.587  1.00 25.29  ? 52  LEU A CA     1 
ATOM   798   C  C      . LEU A 1 53  ? 22.890  37.687  20.051  1.00 23.40  ? 52  LEU A C      1 
ATOM   799   O  O      . LEU A 1 53  ? 21.921  38.183  20.635  1.00 28.26  ? 52  LEU A O      1 
ATOM   800   C  CB     . LEU A 1 53  ? 24.493  37.219  21.947  1.00 28.78  ? 52  LEU A CB     1 
ATOM   801   C  CG     . LEU A 1 53  ? 24.456  35.693  21.993  1.00 28.17  ? 52  LEU A CG     1 
ATOM   802   C  CD1    . LEU A 1 53  ? 25.350  35.042  20.985  1.00 28.33  ? 52  LEU A CD1    1 
ATOM   803   C  CD2    . LEU A 1 53  ? 24.816  35.223  23.422  1.00 32.80  ? 52  LEU A CD2    1 
ATOM   804   H  H      . LEU A 1 53  ? 24.028  39.707  21.280  1.00 31.91  ? 52  LEU A H      1 
ATOM   805   H  HA     . LEU A 1 53  ? 24.929  37.481  19.973  1.00 30.38  ? 52  LEU A HA     1 
ATOM   806   H  HB2    . LEU A 1 53  ? 25.359  37.489  22.291  1.00 34.57  ? 52  LEU A HB2    1 
ATOM   807   H  HB3    . LEU A 1 53  ? 23.789  37.534  22.536  1.00 34.57  ? 52  LEU A HB3    1 
ATOM   808   H  HG     . LEU A 1 53  ? 23.558  35.408  21.763  1.00 33.83  ? 52  LEU A HG     1 
ATOM   809   H  HD11   . LEU A 1 53  ? 25.358  34.085  21.141  1.00 34.03  ? 52  LEU A HD11   1 
ATOM   810   H  HD12   . LEU A 1 53  ? 25.011  35.229  20.095  1.00 34.03  ? 52  LEU A HD12   1 
ATOM   811   H  HD13   . LEU A 1 53  ? 26.246  35.400  21.080  1.00 34.03  ? 52  LEU A HD13   1 
ATOM   812   H  HD21   . LEU A 1 53  ? 24.809  34.254  23.447  1.00 39.40  ? 52  LEU A HD21   1 
ATOM   813   H  HD22   . LEU A 1 53  ? 25.700  35.553  23.649  1.00 39.40  ? 52  LEU A HD22   1 
ATOM   814   H  HD23   . LEU A 1 53  ? 24.161  35.576  24.044  1.00 39.40  ? 52  LEU A HD23   1 
ATOM   815   N  N      . LEU A 1 54  ? 22.796  37.043  18.893  1.00 23.20  ? 53  LEU A N      1 
ATOM   816   C  CA     . LEU A 1 54  ? 21.524  36.659  18.299  1.00 23.76  ? 53  LEU A CA     1 
ATOM   817   C  C      . LEU A 1 54  ? 21.122  35.260  18.773  1.00 23.31  ? 53  LEU A C      1 
ATOM   818   O  O      . LEU A 1 54  ? 21.909  34.314  18.710  1.00 21.23  ? 53  LEU A O      1 
ATOM   819   C  CB     . LEU A 1 54  ? 21.591  36.688  16.779  1.00 24.11  ? 53  LEU A CB     1 
ATOM   820   C  CG     . LEU A 1 54  ? 22.143  37.936  16.095  1.00 24.75  ? 53  LEU A CG     1 
ATOM   821   C  CD1    . LEU A 1 54  ? 21.950  37.852  14.585  1.00 26.30  ? 53  LEU A CD1    1 
ATOM   822   C  CD2    . LEU A 1 54  ? 21.477  39.141  16.588  1.00 27.75  ? 53  LEU A CD2    1 
ATOM   823   H  H      . LEU A 1 54  ? 23.476  36.811  18.419  1.00 27.87  ? 53  LEU A H      1 
ATOM   824   H  HA     . LEU A 1 54  ? 20.846  37.292  18.584  1.00 28.55  ? 53  LEU A HA     1 
ATOM   825   H  HB2    . LEU A 1 54  ? 22.152  35.948  16.498  1.00 28.96  ? 53  LEU A HB2    1 
ATOM   826   H  HB3    . LEU A 1 54  ? 20.689  36.566  16.444  1.00 28.96  ? 53  LEU A HB3    1 
ATOM   827   H  HG     . LEU A 1 54  ? 23.090  37.993  16.294  1.00 29.74  ? 53  LEU A HG     1 
ATOM   828   H  HD11   . LEU A 1 54  ? 22.341  38.638  14.173  1.00 31.60  ? 53  LEU A HD11   1 
ATOM   829   H  HD12   . LEU A 1 54  ? 22.388  37.053  14.255  1.00 31.60  ? 53  LEU A HD12   1 
ATOM   830   H  HD13   . LEU A 1 54  ? 21.001  37.815  14.390  1.00 31.60  ? 53  LEU A HD13   1 
ATOM   831   H  HD21   . LEU A 1 54  ? 21.782  39.904  16.073  1.00 33.34  ? 53  LEU A HD21   1 
ATOM   832   H  HD22   . LEU A 1 54  ? 20.518  39.036  16.488  1.00 33.34  ? 53  LEU A HD22   1 
ATOM   833   H  HD23   . LEU A 1 54  ? 21.700  39.264  17.524  1.00 33.34  ? 53  LEU A HD23   1 
ATOM   834   N  N      . ASP A 1 55  ? 19.908  35.146  19.296  1.00 21.80  ? 54  ASP A N      1 
ATOM   835   C  CA     . ASP A 1 55  ? 19.316  33.872  19.656  1.00 21.71  ? 54  ASP A CA     1 
ATOM   836   C  C      . ASP A 1 55  ? 18.155  33.690  18.695  1.00 21.53  ? 54  ASP A C      1 
ATOM   837   O  O      . ASP A 1 55  ? 17.222  34.507  18.698  1.00 26.00  ? 54  ASP A O      1 
ATOM   838   C  CB     . ASP A 1 55  ? 18.864  33.878  21.111  1.00 25.28  ? 54  ASP A CB     1 
ATOM   839   C  CG     . ASP A 1 55  ? 18.230  32.565  21.514  1.00 30.74  ? 54  ASP A CG     1 
ATOM   840   O  OD1    . ASP A 1 55  ? 17.092  32.316  21.071  1.00 32.46  ? 54  ASP A OD1    1 
ATOM   841   O  OD2    . ASP A 1 55  ? 18.877  31.772  22.236  1.00 33.14  ? 54  ASP A OD2    1 
ATOM   842   H  H      . ASP A 1 55  ? 19.394  35.817  19.455  1.00 26.20  ? 54  ASP A H      1 
ATOM   843   H  HA     . ASP A 1 55  ? 19.943  33.138  19.561  1.00 26.09  ? 54  ASP A HA     1 
ATOM   844   H  HB2    . ASP A 1 55  ? 19.632  34.032  21.682  1.00 30.37  ? 54  ASP A HB2    1 
ATOM   845   H  HB3    . ASP A 1 55  ? 18.209  34.582  21.238  1.00 30.37  ? 54  ASP A HB3    1 
ATOM   846   N  N      . ILE A 1 56  ? 18.273  32.713  17.790  1.00 22.03  ? 55  ILE A N      1 
ATOM   847   C  CA     . ILE A 1 56  ? 17.334  32.542  16.682  1.00 19.61  ? 55  ILE A CA     1 
ATOM   848   C  C      . ILE A 1 56  ? 16.536  31.270  16.935  1.00 18.54  ? 55  ILE A C      1 
ATOM   849   O  O      . ILE A 1 56  ? 17.110  30.184  17.123  1.00 19.77  ? 55  ILE A O      1 
ATOM   850   C  CB     . ILE A 1 56  ? 18.029  32.458  15.317  1.00 20.26  ? 55  ILE A CB     1 
ATOM   851   C  CG1    . ILE A 1 56  ? 19.119  33.515  15.131  1.00 25.97  ? 55  ILE A CG1    1 
ATOM   852   C  CG2    . ILE A 1 56  ? 16.976  32.554  14.210  1.00 20.69  ? 55  ILE A CG2    1 
ATOM   853   C  CD1    . ILE A 1 56  ? 18.539  34.866  15.103  1.00 26.54  ? 55  ILE A CD1    1 
ATOM   854   H  H      . ILE A 1 56  ? 18.902  32.126  17.800  1.00 26.47  ? 55  ILE A H      1 
ATOM   855   H  HA     . ILE A 1 56  ? 16.739  33.309  16.668  1.00 23.57  ? 55  ILE A HA     1 
ATOM   856   H  HB     . ILE A 1 56  ? 18.483  31.602  15.273  1.00 24.35  ? 55  ILE A HB     1 
ATOM   857   H  HG12   . ILE A 1 56  ? 19.747  33.464  15.869  1.00 31.20  ? 55  ILE A HG12   1 
ATOM   858   H  HG13   . ILE A 1 56  ? 19.579  33.359  14.292  1.00 31.20  ? 55  ILE A HG13   1 
ATOM   859   H  HG21   . ILE A 1 56  ? 17.423  32.697  13.361  1.00 24.86  ? 55  ILE A HG21   1 
ATOM   860   H  HG22   . ILE A 1 56  ? 16.471  31.726  14.183  1.00 24.86  ? 55  ILE A HG22   1 
ATOM   861   H  HG23   . ILE A 1 56  ? 16.384  33.297  14.401  1.00 24.86  ? 55  ILE A HG23   1 
ATOM   862   H  HD11   . ILE A 1 56  ? 19.253  35.513  14.994  1.00 31.88  ? 55  ILE A HD11   1 
ATOM   863   H  HD12   . ILE A 1 56  ? 17.920  34.928  14.359  1.00 31.88  ? 55  ILE A HD12   1 
ATOM   864   H  HD13   . ILE A 1 56  ? 18.072  35.026  15.937  1.00 31.88  ? 55  ILE A HD13   1 
ATOM   865   N  N      . LEU A 1 57  ? 15.223  31.403  16.927  1.00 19.14  ? 56  LEU A N      1 
ATOM   866   C  CA     . LEU A 1 57  ? 14.307  30.282  16.985  1.00 16.15  ? 56  LEU A CA     1 
ATOM   867   C  C      . LEU A 1 57  ? 13.711  30.108  15.597  1.00 18.86  ? 56  LEU A C      1 
ATOM   868   O  O      . LEU A 1 57  ? 13.070  31.028  15.071  1.00 17.74  ? 56  LEU A O      1 
ATOM   869   C  CB     . LEU A 1 57  ? 13.209  30.511  18.019  1.00 20.83  ? 56  LEU A CB     1 
ATOM   870   C  CG     . LEU A 1 57  ? 12.316  29.275  18.210  1.00 20.78  ? 56  LEU A CG     1 
ATOM   871   C  CD1    . LEU A 1 57  ? 13.039  28.132  18.859  1.00 24.78  ? 56  LEU A CD1    1 
ATOM   872   C  CD2    . LEU A 1 57  ? 11.103  29.679  19.028  1.00 25.33  ? 56  LEU A CD2    1 
ATOM   873   H  H      . LEU A 1 57  ? 14.823  32.163  16.886  1.00 23.01  ? 56  LEU A H      1 
ATOM   874   H  HA     . LEU A 1 57  ? 14.783  29.476  17.238  1.00 19.42  ? 56  LEU A HA     1 
ATOM   875   H  HB2    . LEU A 1 57  ? 13.617  30.724  18.872  1.00 25.03  ? 56  LEU A HB2    1 
ATOM   876   H  HB3    . LEU A 1 57  ? 12.648  31.247  17.727  1.00 25.03  ? 56  LEU A HB3    1 
ATOM   877   H  HG     . LEU A 1 57  ? 12.038  28.948  17.340  1.00 24.97  ? 56  LEU A HG     1 
ATOM   878   H  HD11   . LEU A 1 57  ? 12.396  27.446  19.098  1.00 29.77  ? 56  LEU A HD11   1 
ATOM   879   H  HD12   . LEU A 1 57  ? 13.688  27.774  18.234  1.00 29.77  ? 56  LEU A HD12   1 
ATOM   880   H  HD13   . LEU A 1 57  ? 13.490  28.455  19.655  1.00 29.77  ? 56  LEU A HD13   1 
ATOM   881   H  HD21   . LEU A 1 57  ? 10.534  28.904  19.154  1.00 30.43  ? 56  LEU A HD21   1 
ATOM   882   H  HD22   . LEU A 1 57  ? 11.400  30.015  19.888  1.00 30.43  ? 56  LEU A HD22   1 
ATOM   883   H  HD23   . LEU A 1 57  ? 10.618  30.371  18.552  1.00 30.43  ? 56  LEU A HD23   1 
ATOM   884   N  N      . ASP A 1 58  ? 13.923  28.934  15.044  1.00 16.80  ? 57  ASP A N      1 
ATOM   885   C  CA     . ASP A 1 58  ? 13.465  28.521  13.728  1.00 17.02  ? 57  ASP A CA     1 
ATOM   886   C  C      . ASP A 1 58  ? 12.275  27.616  13.963  1.00 17.78  ? 57  ASP A C      1 
ATOM   887   O  O      . ASP A 1 58  ? 12.416  26.566  14.610  1.00 19.59  ? 57  ASP A O      1 
ATOM   888   C  CB     . ASP A 1 58  ? 14.589  27.797  12.990  1.00 18.82  ? 57  ASP A CB     1 
ATOM   889   C  CG     . ASP A 1 58  ? 14.220  27.385  11.588  1.00 18.40  ? 57  ASP A CG     1 
ATOM   890   O  OD1    . ASP A 1 58  ? 13.340  28.033  10.991  1.00 19.34  ? 57  ASP A OD1    1 
ATOM   891   O  OD2    . ASP A 1 58  ? 14.910  26.467  11.051  1.00 18.57  ? 57  ASP A OD2    1 
ATOM   892   H  H      . ASP A 1 58  ? 14.364  28.310  15.437  1.00 20.19  ? 57  ASP A H      1 
ATOM   893   H  HA     . ASP A 1 58  ? 13.194  29.272  13.177  1.00 20.46  ? 57  ASP A HA     1 
ATOM   894   H  HB2    . ASP A 1 58  ? 15.357  28.387  12.934  1.00 22.61  ? 57  ASP A HB2    1 
ATOM   895   H  HB3    . ASP A 1 58  ? 14.822  26.995  13.483  1.00 22.61  ? 57  ASP A HB3    1 
ATOM   896   N  N      . THR A 1 59  ? 11.108  28.012  13.447  1.00 18.36  ? 58  THR A N      1 
ATOM   897   C  CA     . THR A 1 59  ? 9.854   27.385  13.855  1.00 19.43  ? 58  THR A CA     1 
ATOM   898   C  C      . THR A 1 59  ? 9.243   26.547  12.741  1.00 22.80  ? 58  THR A C      1 
ATOM   899   O  O      . THR A 1 59  ? 9.610   26.637  11.561  1.00 19.85  ? 58  THR A O      1 
ATOM   900   C  CB     . THR A 1 59  ? 8.840   28.450  14.322  1.00 21.89  ? 58  THR A CB     1 
ATOM   901   O  OG1    . THR A 1 59  ? 8.441   29.247  13.215  1.00 20.75  ? 58  THR A OG1    1 
ATOM   902   C  CG2    . THR A 1 59  ? 9.422   29.373  15.372  1.00 19.63  ? 58  THR A CG2    1 
ATOM   903   H  H      . THR A 1 59  ? 11.021  28.637  12.863  1.00 22.06  ? 58  THR A H      1 
ATOM   904   H  HA     . THR A 1 59  ? 10.051  26.784  14.591  1.00 23.36  ? 58  THR A HA     1 
ATOM   905   H  HB     . THR A 1 59  ? 8.081   27.988  14.710  1.00 26.31  ? 58  THR A HB     1 
ATOM   906   H  HG1    . THR A 1 59  ? 9.106   29.645  12.893  1.00 24.93  ? 58  THR A HG1    1 
ATOM   907   H  HG21   . THR A 1 59  ? 8.737   29.976  15.700  1.00 23.59  ? 58  THR A HG21   1 
ATOM   908   H  HG22   . THR A 1 59  ? 9.767   28.854  16.115  1.00 23.59  ? 58  THR A HG22   1 
ATOM   909   H  HG23   . THR A 1 59  ? 10.145  29.895  14.991  1.00 23.59  ? 58  THR A HG23   1 
ATOM   910   N  N      . ALA A 1 60  ? 8.251   25.753  13.137  1.00 20.03  ? 59  ALA A N      1 
ATOM   911   C  CA     . ALA A 1 60  ? 7.489   24.962  12.180  1.00 24.19  ? 59  ALA A CA     1 
ATOM   912   C  C      . ALA A 1 60  ? 6.340   25.790  11.628  1.00 27.68  ? 59  ALA A C      1 
ATOM   913   O  O      . ALA A 1 60  ? 5.652   26.483  12.382  1.00 27.52  ? 59  ALA A O      1 
ATOM   914   C  CB     . ALA A 1 60  ? 6.910   23.735  12.852  1.00 23.38  ? 59  ALA A CB     1 
ATOM   915   H  H      . ALA A 1 60  ? 8.001   25.657  13.954  1.00 24.08  ? 59  ALA A H      1 
ATOM   916   H  HA     . ALA A 1 60  ? 8.073   24.687  11.456  1.00 29.06  ? 59  ALA A HA     1 
ATOM   917   H  HB1    . ALA A 1 60  ? 6.399   23.230  12.201  1.00 28.09  ? 59  ALA A HB1    1 
ATOM   918   H  HB2    . ALA A 1 60  ? 7.636   23.192  13.197  1.00 28.09  ? 59  ALA A HB2    1 
ATOM   919   H  HB3    . ALA A 1 60  ? 6.333   24.017  13.579  1.00 28.09  ? 59  ALA A HB3    1 
ATOM   920   N  N      . GLY A 1 61  ? 6.131   25.692  10.322  1.00 32.65  ? 60  GLY A N      1 
ATOM   921   C  CA     . GLY A 1 61  ? 4.973   26.309  9.695   1.00 36.15  ? 60  GLY A CA     1 
ATOM   922   C  C      . GLY A 1 61  ? 3.712   25.479  9.693   1.00 37.93  ? 60  GLY A C      1 
ATOM   923   O  O      . GLY A 1 61  ? 2.631   26.004  9.406   1.00 42.03  ? 60  GLY A O      1 
ATOM   924   H  H      . GLY A 1 61  ? 6.647   25.273  9.776   1.00 39.21  ? 60  GLY A H      1 
ATOM   925   H  HA2    . GLY A 1 61  ? 4.778   27.138  10.160  1.00 43.41  ? 60  GLY A HA2    1 
ATOM   926   H  HA3    . GLY A 1 61  ? 5.194   26.509  8.772   1.00 43.41  ? 60  GLY A HA3    1 
ATOM   927   N  N      . GLN A 1 62  ? 3.813   24.212  10.065  1.00 31.33  ? 61  GLN A N      1 
ATOM   928   C  CA     . GLN A 1 62  ? 2.710   23.263  9.964   1.00 35.18  ? 61  GLN A CA     1 
ATOM   929   C  C      . GLN A 1 62  ? 1.407   23.838  10.494  1.00 37.03  ? 61  GLN A C      1 
ATOM   930   O  O      . GLN A 1 62  ? 1.295   24.161  11.681  1.00 36.08  ? 61  GLN A O      1 
ATOM   931   C  CB     . GLN A 1 62  ? 3.051   21.990  10.742  1.00 30.35  ? 61  GLN A CB     1 
ATOM   932   C  CG     . GLN A 1 62  ? 4.344   21.308  10.346  1.00 32.75  ? 61  GLN A CG     1 
ATOM   933   C  CD     . GLN A 1 62  ? 4.222   20.561  9.063   1.00 35.99  ? 61  GLN A CD     1 
ATOM   934   O  OE1    . GLN A 1 62  ? 3.138   20.118  8.691   1.00 42.21  ? 61  GLN A OE1    1 
ATOM   935   N  NE2    . GLN A 1 62  ? 5.331   20.446  8.343   1.00 37.35  ? 61  GLN A NE2    1 
ATOM   936   H  H      . GLN A 1 62  ? 4.529   23.863  10.388  1.00 37.63  ? 61  GLN A H      1 
ATOM   937   H  HA     . GLN A 1 62  ? 2.586   23.050  9.026   1.00 42.25  ? 61  GLN A HA     1 
ATOM   938   H  HB2    . GLN A 1 62  ? 3.121   22.217  11.683  1.00 36.46  ? 61  GLN A HB2    1 
ATOM   939   H  HB3    . GLN A 1 62  ? 2.334   21.350  10.608  1.00 36.46  ? 61  GLN A HB3    1 
ATOM   940   H  HG2    . GLN A 1 62  ? 5.037   21.979  10.240  1.00 39.33  ? 61  GLN A HG2    1 
ATOM   941   H  HG3    . GLN A 1 62  ? 4.595   20.678  11.039  1.00 39.33  ? 61  GLN A HG3    1 
ATOM   942   H  HE21   . GLN A 1 62  ? 6.065   20.793  8.625   1.00 44.85  ? 61  GLN A HE21   1 
ATOM   943   H  HE22   . GLN A 1 62  ? 5.315   20.024  7.594   1.00 44.85  ? 61  GLN A HE22   1 
ATOM   944   N  N      . GLU A 1 63  ? 0.395   23.912  9.627   1.00 38.17  ? 62  GLU A N      1 
ATOM   945   C  CA     . GLU A 1 63  ? -0.871  24.517  10.036  1.00 37.03  ? 62  GLU A CA     1 
ATOM   946   C  C      . GLU A 1 63  ? -1.573  23.711  11.129  1.00 36.65  ? 62  GLU A C      1 
ATOM   947   O  O      . GLU A 1 63  ? -2.319  24.279  11.935  1.00 33.68  ? 62  GLU A O      1 
ATOM   948   C  CB     . GLU A 1 63  ? -1.775  24.678  8.807   1.00 41.31  ? 62  GLU A CB     1 
ATOM   949   C  CG     . GLU A 1 63  ? -1.217  25.666  7.764   1.00 48.39  ? 62  GLU A CG     1 
ATOM   950   C  CD     . GLU A 1 63  ? -2.244  26.077  6.713   1.00 53.97  ? 62  GLU A CD     1 
ATOM   951   O  OE1    . GLU A 1 63  ? -2.046  25.753  5.518   1.00 57.35  ? 62  GLU A OE1    1 
ATOM   952   O  OE2    . GLU A 1 63  ? -3.248  26.731  7.081   1.00 61.34  ? 62  GLU A OE2    1 
ATOM   953   H  H      . GLU A 1 63  ? 0.416   23.625  8.816   1.00 45.84  ? 62  GLU A H      1 
ATOM   954   H  HA     . GLU A 1 63  ? -0.698  25.397  10.406  1.00 44.47  ? 62  GLU A HA     1 
ATOM   955   H  HB2    . GLU A 1 63  ? -1.875  23.815  8.376   1.00 49.60  ? 62  GLU A HB2    1 
ATOM   956   H  HB3    . GLU A 1 63  ? -2.641  25.008  9.096   1.00 49.60  ? 62  GLU A HB3    1 
ATOM   957   H  HG2    . GLU A 1 63  ? -0.920  26.469  8.220   1.00 58.10  ? 62  GLU A HG2    1 
ATOM   958   H  HG3    . GLU A 1 63  ? -0.471  25.249  7.305   1.00 58.10  ? 62  GLU A HG3    1 
ATOM   959   N  N      . GLU A 1 64  ? -1.349  22.397  11.182  1.00 34.49  ? 63  GLU A N      1 
ATOM   960   C  CA     . GLU A 1 64  ? -1.990  21.560  12.194  1.00 35.43  ? 63  GLU A CA     1 
ATOM   961   C  C      . GLU A 1 64  ? -1.645  22.007  13.614  1.00 34.54  ? 63  GLU A C      1 
ATOM   962   O  O      . GLU A 1 64  ? -2.417  21.736  14.541  1.00 35.10  ? 63  GLU A O      1 
ATOM   963   C  CB     . GLU A 1 64  ? -1.590  20.092  11.932  1.00 36.59  ? 63  GLU A CB     1 
ATOM   964   C  CG     . GLU A 1 64  ? -2.031  19.040  12.944  1.00 37.91  ? 63  GLU A CG     1 
ATOM   965   C  CD     . GLU A 1 64  ? -3.492  18.606  12.839  1.00 42.18  ? 63  GLU A CD     1 
ATOM   966   O  OE1    . GLU A 1 64  ? -3.896  18.041  11.794  1.00 46.07  ? 63  GLU A OE1    1 
ATOM   967   O  OE2    . GLU A 1 64  ? -4.226  18.791  13.841  1.00 43.42  ? 63  GLU A OE2    1 
ATOM   968   H  H      . GLU A 1 64  ? -0.833  21.967  10.645  1.00 41.42  ? 63  GLU A H      1 
ATOM   969   H  HA     . GLU A 1 64  ? -2.956  21.618  12.126  1.00 42.55  ? 63  GLU A HA     1 
ATOM   970   H  HB2    . GLU A 1 64  ? -1.967  19.831  11.077  1.00 43.94  ? 63  GLU A HB2    1 
ATOM   971   H  HB3    . GLU A 1 64  ? -0.621  20.052  11.893  1.00 43.94  ? 63  GLU A HB3    1 
ATOM   972   H  HG2    . GLU A 1 64  ? -1.484  18.248  12.820  1.00 45.52  ? 63  GLU A HG2    1 
ATOM   973   H  HG3    . GLU A 1 64  ? -1.898  19.398  13.835  1.00 45.52  ? 63  GLU A HG3    1 
ATOM   974   N  N      . TYR A 1 65  ? -0.524  22.702  13.805  1.00 29.73  ? 64  TYR A N      1 
ATOM   975   C  CA     . TYR A 1 65  ? -0.043  23.072  15.131  1.00 35.38  ? 64  TYR A CA     1 
ATOM   976   C  C      . TYR A 1 65  ? -0.112  24.583  15.360  1.00 33.62  ? 64  TYR A C      1 
ATOM   977   O  O      . TYR A 1 65  ? 0.589   25.119  16.212  1.00 29.22  ? 64  TYR A O      1 
ATOM   978   C  CB     . TYR A 1 65  ? 1.375   22.510  15.329  1.00 29.94  ? 64  TYR A CB     1 
ATOM   979   C  CG     . TYR A 1 65  ? 1.460   21.014  14.985  1.00 27.29  ? 64  TYR A CG     1 
ATOM   980   C  CD1    . TYR A 1 65  ? 0.696   20.094  15.682  1.00 31.01  ? 64  TYR A CD1    1 
ATOM   981   C  CD2    . TYR A 1 65  ? 2.256   20.551  13.931  1.00 25.47  ? 64  TYR A CD2    1 
ATOM   982   C  CE1    . TYR A 1 65  ? 0.736   18.740  15.369  1.00 28.35  ? 64  TYR A CE1    1 
ATOM   983   C  CE2    . TYR A 1 65  ? 2.295   19.199  13.587  1.00 26.04  ? 64  TYR A CE2    1 
ATOM   984   C  CZ     . TYR A 1 65  ? 1.545   18.297  14.335  1.00 21.28  ? 64  TYR A CZ     1 
ATOM   985   O  OH     . TYR A 1 65  ? 1.555   16.963  14.029  1.00 20.15  ? 64  TYR A OH     1 
ATOM   986   H  H      . TYR A 1 65  ? -0.016  22.975  13.168  1.00 35.72  ? 64  TYR A H      1 
ATOM   987   H  HA     . TYR A 1 65  ? -0.609  22.677  15.813  1.00 42.49  ? 64  TYR A HA     1 
ATOM   988   H  HB2    . TYR A 1 65  ? 1.990   22.989  14.752  1.00 35.97  ? 64  TYR A HB2    1 
ATOM   989   H  HB3    . TYR A 1 65  ? 1.635   22.623  16.257  1.00 35.97  ? 64  TYR A HB3    1 
ATOM   990   H  HD1    . TYR A 1 65  ? 0.145   20.387  16.373  1.00 37.24  ? 64  TYR A HD1    1 
ATOM   991   H  HD2    . TYR A 1 65  ? 2.771   21.157  13.449  1.00 30.60  ? 64  TYR A HD2    1 
ATOM   992   H  HE1    . TYR A 1 65  ? 0.222   18.134  15.852  1.00 34.05  ? 64  TYR A HE1    1 
ATOM   993   H  HE2    . TYR A 1 65  ? 2.813   18.907  12.871  1.00 31.28  ? 64  TYR A HE2    1 
ATOM   994   H  HH     . TYR A 1 65  ? 2.049   16.825  13.364  1.00 24.21  ? 64  TYR A HH     1 
ATOM   995   N  N      . SER A 1 66  ? -1.021  25.271  14.659  1.00 35.81  ? 65  SER A N      1 
ATOM   996   C  CA     . SER A 1 66  ? -1.034  26.731  14.727  1.00 35.80  ? 65  SER A CA     1 
ATOM   997   C  C      . SER A 1 66  ? -1.383  27.232  16.119  1.00 36.64  ? 65  SER A C      1 
ATOM   998   O  O      . SER A 1 66  ? -0.946  28.323  16.512  1.00 41.01  ? 65  SER A O      1 
ATOM   999   C  CB     . SER A 1 66  ? -2.011  27.318  13.699  1.00 39.67  ? 65  SER A CB     1 
ATOM   1000  O  OG     . SER A 1 66  ? -3.278  26.676  13.748  1.00 37.30  ? 65  SER A OG     1 
ATOM   1001  H  H      . SER A 1 66  ? -1.623  24.925  14.151  1.00 43.00  ? 65  SER A H      1 
ATOM   1002  H  HA     . SER A 1 66  ? -0.145  27.047  14.504  1.00 42.99  ? 65  SER A HA     1 
ATOM   1003  H  HB2    . SER A 1 66  ? -2.132  28.262  13.888  1.00 47.63  ? 65  SER A HB2    1 
ATOM   1004  H  HB3    . SER A 1 66  ? -1.637  27.203  12.812  1.00 47.63  ? 65  SER A HB3    1 
ATOM   1005  H  HG     . SER A 1 66  ? -3.775  26.975  13.140  1.00 44.80  ? 65  SER A HG     1 
ATOM   1006  N  N      . ALA A 1 67  ? -2.147  26.468  16.890  1.00 39.17  ? 66  ALA A N      1 
ATOM   1007  C  CA     . ALA A 1 67  ? -2.532  26.941  18.211  1.00 38.99  ? 66  ALA A CA     1 
ATOM   1008  C  C      . ALA A 1 67  ? -1.444  26.743  19.251  1.00 40.15  ? 66  ALA A C      1 
ATOM   1009  O  O      . ALA A 1 67  ? -1.590  27.249  20.367  1.00 44.63  ? 66  ALA A O      1 
ATOM   1010  C  CB     . ALA A 1 67  ? -3.803  26.245  18.679  1.00 31.99  ? 66  ALA A CB     1 
ATOM   1011  H  H      . ALA A 1 67  ? -2.447  25.691  16.676  1.00 47.04  ? 66  ALA A H      1 
ATOM   1012  H  HA     . ALA A 1 67  ? -2.721  27.890  18.147  1.00 46.82  ? 66  ALA A HA     1 
ATOM   1013  H  HB1    . ALA A 1 67  ? -4.044  26.584  19.555  1.00 38.42  ? 66  ALA A HB1    1 
ATOM   1014  H  HB2    . ALA A 1 67  ? -4.515  26.428  18.046  1.00 38.42  ? 66  ALA A HB2    1 
ATOM   1015  H  HB3    . ALA A 1 67  ? -3.641  25.290  18.728  1.00 38.42  ? 66  ALA A HB3    1 
ATOM   1016  N  N      . MET A 1 68  ? -0.372  26.027  18.914  1.00 36.58  ? 67  MET A N      1 
ATOM   1017  C  CA     . MET A 1 68  ? 0.759   25.858  19.803  1.00 36.16  ? 67  MET A CA     1 
ATOM   1018  C  C      . MET A 1 68  ? 1.907   26.806  19.492  1.00 37.39  ? 67  MET A C      1 
ATOM   1019  O  O      . MET A 1 68  ? 3.027   26.571  19.959  1.00 37.62  ? 67  MET A O      1 
ATOM   1020  C  CB     . MET A 1 68  ? 1.284   24.434  19.738  1.00 38.47  ? 67  MET A CB     1 
ATOM   1021  C  CG     . MET A 1 68  ? 0.256   23.439  19.307  1.00 41.26  ? 67  MET A CG     1 
ATOM   1022  S  SD     . MET A 1 68  ? 0.833   21.765  19.593  1.00 43.93  ? 67  MET A SD     1 
ATOM   1023  C  CE     . MET A 1 68  ? 1.270   21.820  21.332  1.00 41.75  ? 67  MET A CE     1 
ATOM   1024  H  H      . MET A 1 68  ? -0.282  25.624  18.159  1.00 43.93  ? 67  MET A H      1 
ATOM   1025  H  HA     . MET A 1 68  ? 0.438   26.029  20.703  1.00 43.43  ? 67  MET A HA     1 
ATOM   1026  H  HB2    . MET A 1 68  ? 2.015   24.400  19.102  1.00 46.19  ? 67  MET A HB2    1 
ATOM   1027  H  HB3    . MET A 1 68  ? 1.597   24.176  20.619  1.00 46.19  ? 67  MET A HB3    1 
ATOM   1028  H  HG2    . MET A 1 68  ? -0.559  23.575  19.815  1.00 49.54  ? 67  MET A HG2    1 
ATOM   1029  H  HG3    . MET A 1 68  ? 0.079   23.546  18.360  1.00 49.54  ? 67  MET A HG3    1 
ATOM   1030  H  HE1    . MET A 1 68  ? 1.567   20.939  21.611  1.00 50.14  ? 67  MET A HE1    1 
ATOM   1031  H  HE2    . MET A 1 68  ? 1.983   22.465  21.459  1.00 50.14  ? 67  MET A HE2    1 
ATOM   1032  H  HE3    . MET A 1 68  ? 0.491   22.084  21.846  1.00 50.14  ? 67  MET A HE3    1 
ATOM   1033  N  N      . ARG A 1 69  ? 1.673   27.834  18.676  1.00 37.12  ? 68  ARG A N      1 
ATOM   1034  C  CA     . ARG A 1 69  ? 2.706   28.818  18.413  1.00 35.39  ? 68  ARG A CA     1 
ATOM   1035  C  C      . ARG A 1 69  ? 2.807   29.817  19.537  1.00 36.45  ? 68  ARG A C      1 
ATOM   1036  O  O      . ARG A 1 69  ? 3.822   30.510  19.652  1.00 34.35  ? 68  ARG A O      1 
ATOM   1037  C  CB     . ARG A 1 69  ? 2.422   29.576  17.111  1.00 37.87  ? 68  ARG A CB     1 
ATOM   1038  C  CG     . ARG A 1 69  ? 2.542   28.774  15.843  1.00 38.16  ? 68  ARG A CG     1 
ATOM   1039  C  CD     . ARG A 1 69  ? 1.836   29.526  14.702  1.00 37.04  ? 68  ARG A CD     1 
ATOM   1040  N  NE     . ARG A 1 69  ? 1.681   28.699  13.516  1.00 38.62  ? 68  ARG A NE     1 
ATOM   1041  C  CZ     . ARG A 1 69  ? 0.791   28.927  12.564  1.00 38.78  ? 68  ARG A CZ     1 
ATOM   1042  N  NH1    . ARG A 1 69  ? -0.049  29.951  12.630  1.00 38.88  ? 68  ARG A NH1    1 
ATOM   1043  N  NH2    . ARG A 1 69  ? 0.734   28.104  11.524  1.00 42.73  ? 68  ARG A NH2    1 
ATOM   1044  H  H      . ARG A 1 69  ? 0.929   27.978  18.269  1.00 44.58  ? 68  ARG A H      1 
ATOM   1045  H  HA     . ARG A 1 69  ? 3.553   28.357  18.305  1.00 42.50  ? 68  ARG A HA     1 
ATOM   1046  H  HB2    . ARG A 1 69  ? 1.514   29.916  17.151  1.00 45.48  ? 68  ARG A HB2    1 
ATOM   1047  H  HB3    . ARG A 1 69  ? 3.050   30.312  17.046  1.00 45.48  ? 68  ARG A HB3    1 
ATOM   1048  H  HG2    . ARG A 1 69  ? 3.477   28.658  15.612  1.00 45.82  ? 68  ARG A HG2    1 
ATOM   1049  H  HG3    . ARG A 1 69  ? 2.120   27.908  15.958  1.00 45.82  ? 68  ARG A HG3    1 
ATOM   1050  H  HD2    . ARG A 1 69  ? 0.954   29.799  14.998  1.00 44.48  ? 68  ARG A HD2    1 
ATOM   1051  H  HD3    . ARG A 1 69  ? 2.361   30.305  14.461  1.00 44.48  ? 68  ARG A HD3    1 
ATOM   1052  H  HE     . ARG A 1 69  ? 2.200   28.019  13.428  1.00 46.38  ? 68  ARG A HE     1 
ATOM   1053  H  HH11   . ARG A 1 69  ? -0.023  30.486  13.304  1.00 46.69  ? 68  ARG A HH11   1 
ATOM   1054  H  HH12   . ARG A 1 69  ? -0.620  30.081  12.000  1.00 46.69  ? 68  ARG A HH12   1 
ATOM   1055  H  HH21   . ARG A 1 69  ? 1.271   27.434  11.477  1.00 51.30  ? 68  ARG A HH21   1 
ATOM   1056  H  HH22   . ARG A 1 69  ? 0.160   28.241  10.898  1.00 51.30  ? 68  ARG A HH22   1 
ATOM   1057  N  N      . ASP A 1 70  ? 1.764   29.905  20.356  1.00 37.30  ? 69  ASP A N      1 
ATOM   1058  C  CA     . ASP A 1 70  ? 1.659   30.966  21.336  1.00 40.02  ? 69  ASP A CA     1 
ATOM   1059  C  C      . ASP A 1 70  ? 2.885   31.019  22.234  1.00 40.30  ? 69  ASP A C      1 
ATOM   1060  O  O      . ASP A 1 70  ? 3.405   32.103  22.518  1.00 42.44  ? 69  ASP A O      1 
ATOM   1061  C  CB     . ASP A 1 70  ? 0.384   30.774  22.173  1.00 41.94  ? 69  ASP A CB     1 
ATOM   1062  C  CG     . ASP A 1 70  ? -0.902  30.748  21.319  1.00 45.39  ? 69  ASP A CG     1 
ATOM   1063  O  OD1    . ASP A 1 70  ? -0.840  30.680  20.068  1.00 41.83  ? 69  ASP A OD1    1 
ATOM   1064  O  OD2    . ASP A 1 70  ? -1.990  30.785  21.913  1.00 47.54  ? 69  ASP A OD2    1 
ATOM   1065  H  H      . ASP A 1 70  ? 1.101   29.357  20.361  1.00 44.79  ? 69  ASP A H      1 
ATOM   1066  H  HA     . ASP A 1 70  ? 1.595   31.816  20.874  1.00 48.06  ? 69  ASP A HA     1 
ATOM   1067  H  HB2    . ASP A 1 70  ? 0.444   29.931  22.649  1.00 50.36  ? 69  ASP A HB2    1 
ATOM   1068  H  HB3    . ASP A 1 70  ? 0.309   31.506  22.804  1.00 50.36  ? 69  ASP A HB3    1 
ATOM   1069  N  N      . GLN A 1 71  ? 3.360   29.869  22.713  1.00 39.79  ? 70  GLN A N      1 
ATOM   1070  C  CA     . GLN A 1 71  ? 4.412   29.921  23.733  1.00 42.47  ? 70  GLN A CA     1 
ATOM   1071  C  C      . GLN A 1 71  ? 5.656   30.623  23.198  1.00 37.95  ? 70  GLN A C      1 
ATOM   1072  O  O      . GLN A 1 71  ? 6.259   31.460  23.887  1.00 40.05  ? 70  GLN A O      1 
ATOM   1073  C  CB     . GLN A 1 71  ? 4.778   28.522  24.224  1.00 47.34  ? 70  GLN A CB     1 
ATOM   1074  C  CG     . GLN A 1 71  ? 5.665   28.515  25.501  1.00 51.41  ? 70  GLN A CG     1 
ATOM   1075  C  CD     . GLN A 1 71  ? 5.486   29.740  26.391  1.00 53.96  ? 70  GLN A CD     1 
ATOM   1076  O  OE1    . GLN A 1 71  ? 6.310   30.661  26.391  1.00 53.65  ? 70  GLN A OE1    1 
ATOM   1077  N  NE2    . GLN A 1 71  ? 4.397   29.753  27.171  1.00 53.61  ? 70  GLN A NE2    1 
ATOM   1078  H  H      . GLN A 1 71  ? 3.104   29.083  22.478  1.00 47.79  ? 70  GLN A H      1 
ATOM   1079  H  HA     . GLN A 1 71  ? 4.067   30.417  24.491  1.00 51.00  ? 70  GLN A HA     1 
ATOM   1080  H  HB2    . GLN A 1 71  ? 3.961   28.040  24.428  1.00 56.84  ? 70  GLN A HB2    1 
ATOM   1081  H  HB3    . GLN A 1 71  ? 5.267   28.064  23.522  1.00 56.84  ? 70  GLN A HB3    1 
ATOM   1082  H  HG2    . GLN A 1 71  ? 5.443   27.733  26.029  1.00 61.73  ? 70  GLN A HG2    1 
ATOM   1083  H  HG3    . GLN A 1 71  ? 6.597   28.481  25.232  1.00 61.73  ? 70  GLN A HG3    1 
ATOM   1084  H  HE21   . GLN A 1 71  ? 3.846   29.093  27.150  1.00 64.37  ? 70  GLN A HE21   1 
ATOM   1085  H  HE22   . GLN A 1 71  ? 4.249   30.421  27.692  1.00 64.37  ? 70  GLN A HE22   1 
ATOM   1086  N  N      . TYR A 1 72  ? 6.067   30.306  21.974  1.00 39.07  ? 71  TYR A N      1 
ATOM   1087  C  CA     . TYR A 1 72  ? 7.298   30.924  21.507  1.00 34.50  ? 71  TYR A CA     1 
ATOM   1088  C  C      . TYR A 1 72  ? 7.072   32.365  21.060  1.00 36.98  ? 71  TYR A C      1 
ATOM   1089  O  O      . TYR A 1 72  ? 7.995   33.189  21.134  1.00 31.38  ? 71  TYR A O      1 
ATOM   1090  C  CB     . TYR A 1 72  ? 7.926   30.059  20.425  1.00 33.20  ? 71  TYR A CB     1 
ATOM   1091  C  CG     . TYR A 1 72  ? 7.235   29.997  19.086  1.00 31.97  ? 71  TYR A CG     1 
ATOM   1092  C  CD1    . TYR A 1 72  ? 7.069   31.130  18.311  1.00 33.82  ? 71  TYR A CD1    1 
ATOM   1093  C  CD2    . TYR A 1 72  ? 6.801   28.789  18.585  1.00 31.19  ? 71  TYR A CD2    1 
ATOM   1094  C  CE1    . TYR A 1 72  ? 6.475   31.069  17.078  1.00 30.30  ? 71  TYR A CE1    1 
ATOM   1095  C  CE2    . TYR A 1 72  ? 6.205   28.710  17.355  1.00 34.91  ? 71  TYR A CE2    1 
ATOM   1096  C  CZ     . TYR A 1 72  ? 6.044   29.858  16.603  1.00 34.52  ? 71  TYR A CZ     1 
ATOM   1097  O  OH     . TYR A 1 72  ? 5.455   29.799  15.368  1.00 35.34  ? 71  TYR A OH     1 
ATOM   1098  H  H      . TYR A 1 72  ? 5.675   29.768  21.429  1.00 46.91  ? 71  TYR A H      1 
ATOM   1099  H  HA     . TYR A 1 72  ? 7.947   30.967  22.226  1.00 41.43  ? 71  TYR A HA     1 
ATOM   1100  H  HB2    . TYR A 1 72  ? 8.822   30.394  20.261  1.00 39.87  ? 71  TYR A HB2    1 
ATOM   1101  H  HB3    . TYR A 1 72  ? 7.968   29.150  20.760  1.00 39.87  ? 71  TYR A HB3    1 
ATOM   1102  H  HD1    . TYR A 1 72  ? 7.367   31.950  18.633  1.00 40.62  ? 71  TYR A HD1    1 
ATOM   1103  H  HD2    . TYR A 1 72  ? 6.914   28.016  19.090  1.00 37.46  ? 71  TYR A HD2    1 
ATOM   1104  H  HE1    . TYR A 1 72  ? 6.366   31.840  16.570  1.00 36.40  ? 71  TYR A HE1    1 
ATOM   1105  H  HE2    . TYR A 1 72  ? 5.911   27.890  17.029  1.00 41.93  ? 71  TYR A HE2    1 
ATOM   1106  H  HH     . TYR A 1 72  ? 5.413   29.001  15.108  1.00 42.44  ? 71  TYR A HH     1 
ATOM   1107  N  N      . MET A 1 73  ? 5.860   32.709  20.624  1.00 37.27  ? 72  MET A N      1 
ATOM   1108  C  CA     . MET A 1 73  ? 5.596   34.116  20.364  1.00 33.51  ? 72  MET A CA     1 
ATOM   1109  C  C      . MET A 1 73  ? 5.617   34.897  21.661  1.00 35.96  ? 72  MET A C      1 
ATOM   1110  O  O      . MET A 1 73  ? 6.012   36.067  21.674  1.00 31.81  ? 72  MET A O      1 
ATOM   1111  C  CB     . MET A 1 73  ? 4.281   34.304  19.608  1.00 31.35  ? 72  MET A CB     1 
ATOM   1112  C  CG     . MET A 1 73  ? 4.149   33.442  18.331  1.00 30.81  ? 72  MET A CG     1 
ATOM   1113  S  SD     . MET A 1 73  ? 2.544   33.669  17.482  1.00 33.53  ? 72  MET A SD     1 
ATOM   1114  C  CE     . MET A 1 73  ? 2.869   32.921  15.888  1.00 36.07  ? 72  MET A CE     1 
ATOM   1115  H  H      . MET A 1 73  ? 5.206   32.170  20.478  1.00 44.75  ? 72  MET A H      1 
ATOM   1116  H  HA     . MET A 1 73  ? 6.280   34.465  19.772  1.00 40.25  ? 72  MET A HA     1 
ATOM   1117  H  HB2    . MET A 1 73  ? 3.548   34.068  20.199  1.00 37.65  ? 72  MET A HB2    1 
ATOM   1118  H  HB3    . MET A 1 73  ? 4.207   35.234  19.343  1.00 37.65  ? 72  MET A HB3    1 
ATOM   1119  H  HG2    . MET A 1 73  ? 4.853   33.687  17.711  1.00 37.00  ? 72  MET A HG2    1 
ATOM   1120  H  HG3    . MET A 1 73  ? 4.230   32.506  18.572  1.00 37.00  ? 72  MET A HG3    1 
ATOM   1121  H  HE1    . MET A 1 73  ? 2.056   32.940  15.359  1.00 43.32  ? 72  MET A HE1    1 
ATOM   1122  H  HE2    . MET A 1 73  ? 3.567   33.424  15.440  1.00 43.32  ? 72  MET A HE2    1 
ATOM   1123  H  HE3    . MET A 1 73  ? 3.155   32.004  16.022  1.00 43.32  ? 72  MET A HE3    1 
ATOM   1124  N  N      . ARG A 1 74  ? 5.256   34.250  22.773  1.00 36.39  ? 73  ARG A N      1 
ATOM   1125  C  CA     . ARG A 1 74  ? 5.285   34.933  24.057  1.00 38.30  ? 73  ARG A CA     1 
ATOM   1126  C  C      . ARG A 1 74  ? 6.706   35.368  24.410  1.00 35.21  ? 73  ARG A C      1 
ATOM   1127  O  O      . ARG A 1 74  ? 6.930   36.506  24.835  1.00 36.09  ? 73  ARG A O      1 
ATOM   1128  C  CB     . ARG A 1 74  ? 4.688   34.014  25.136  1.00 42.68  ? 73  ARG A CB     1 
ATOM   1129  C  CG     . ARG A 1 74  ? 4.016   34.766  26.256  1.00 51.19  ? 73  ARG A CG     1 
ATOM   1130  C  CD     . ARG A 1 74  ? 2.690   34.131  26.757  1.00 53.45  ? 73  ARG A CD     1 
ATOM   1131  N  NE     . ARG A 1 74  ? 2.625   32.682  26.573  1.00 54.80  ? 73  ARG A NE     1 
ATOM   1132  C  CZ     . ARG A 1 74  ? 1.623   32.025  25.996  1.00 54.25  ? 73  ARG A CZ     1 
ATOM   1133  N  NH1    . ARG A 1 74  ? 0.539   32.650  25.551  1.00 52.54  ? 73  ARG A NH1    1 
ATOM   1134  N  NH2    . ARG A 1 74  ? 1.712   30.706  25.859  1.00 53.97  ? 73  ARG A NH2    1 
ATOM   1135  H  H      . ARG A 1 74  ? 4.995   33.431  22.805  1.00 43.70  ? 73  ARG A H      1 
ATOM   1136  H  HA     . ARG A 1 74  ? 4.740   35.735  24.015  1.00 46.00  ? 73  ARG A HA     1 
ATOM   1137  H  HB2    . ARG A 1 74  ? 4.025   33.438  24.724  1.00 51.25  ? 73  ARG A HB2    1 
ATOM   1138  H  HB3    . ARG A 1 74  ? 5.399   33.480  25.521  1.00 51.25  ? 73  ARG A HB3    1 
ATOM   1139  H  HG2    . ARG A 1 74  ? 4.624   34.805  27.011  1.00 61.46  ? 73  ARG A HG2    1 
ATOM   1140  H  HG3    . ARG A 1 74  ? 3.811   35.663  25.948  1.00 61.46  ? 73  ARG A HG3    1 
ATOM   1141  H  HD2    . ARG A 1 74  ? 2.595   34.313  27.705  1.00 64.17  ? 73  ARG A HD2    1 
ATOM   1142  H  HD3    . ARG A 1 74  ? 1.951   34.524  26.267  1.00 64.17  ? 73  ARG A HD3    1 
ATOM   1143  H  HE     . ARG A 1 74  ? 3.288   32.216  26.862  1.00 65.79  ? 73  ARG A HE     1 
ATOM   1144  H  HH11   . ARG A 1 74  ? 0.470   33.503  25.633  1.00 63.08  ? 73  ARG A HH11   1 
ATOM   1145  H  HH12   . ARG A 1 74  ? -0.095  32.201  25.182  1.00 63.08  ? 73  ARG A HH12   1 
ATOM   1146  H  HH21   . ARG A 1 74  ? 2.410   30.291  26.142  1.00 64.80  ? 73  ARG A HH21   1 
ATOM   1147  H  HH22   . ARG A 1 74  ? 1.072   30.268  25.488  1.00 64.80  ? 73  ARG A HH22   1 
ATOM   1148  N  N      . THR A 1 75  ? 7.681   34.475  24.220  1.00 35.01  ? 74  THR A N      1 
ATOM   1149  C  CA     . THR A 1 75  ? 9.055   34.725  24.626  1.00 35.73  ? 74  THR A CA     1 
ATOM   1150  C  C      . THR A 1 75  ? 9.877   35.470  23.573  1.00 35.37  ? 74  THR A C      1 
ATOM   1151  O  O      . THR A 1 75  ? 10.858  36.132  23.927  1.00 34.14  ? 74  THR A O      1 
ATOM   1152  C  CB     . THR A 1 75  ? 9.743   33.390  24.954  1.00 39.29  ? 74  THR A CB     1 
ATOM   1153  O  OG1    . THR A 1 75  ? 9.526   32.464  23.881  1.00 42.55  ? 74  THR A OG1    1 
ATOM   1154  C  CG2    . THR A 1 75  ? 9.183   32.784  26.242  1.00 44.57  ? 74  THR A CG2    1 
ATOM   1155  H  H      . THR A 1 75  ? 7.565   33.707  23.851  1.00 42.04  ? 74  THR A H      1 
ATOM   1156  H  HA     . THR A 1 75  ? 9.049   35.274  25.426  1.00 42.91  ? 74  THR A HA     1 
ATOM   1157  H  HB     . THR A 1 75  ? 10.693  33.547  25.075  1.00 47.19  ? 74  THR A HB     1 
ATOM   1158  H  HG1    . THR A 1 75  ? 9.815   32.786  23.161  1.00 51.09  ? 74  THR A HG1    1 
ATOM   1159  H  HG21   . THR A 1 75  ? 9.625   31.941  26.432  1.00 53.52  ? 74  THR A HG21   1 
ATOM   1160  H  HG22   . THR A 1 75  ? 9.329   33.390  26.985  1.00 53.52  ? 74  THR A HG22   1 
ATOM   1161  H  HG23   . THR A 1 75  ? 8.231   32.626  26.147  1.00 53.52  ? 74  THR A HG23   1 
ATOM   1162  N  N      . GLY A 1 76  ? 9.507   35.384  22.299  1.00 31.68  ? 75  GLY A N      1 
ATOM   1163  C  CA     . GLY A 1 76  ? 10.264  36.067  21.266  1.00 25.87  ? 75  GLY A CA     1 
ATOM   1164  C  C      . GLY A 1 76  ? 10.197  37.584  21.367  1.00 30.40  ? 75  GLY A C      1 
ATOM   1165  O  O      . GLY A 1 76  ? 9.160   38.172  21.709  1.00 31.42  ? 75  GLY A O      1 
ATOM   1166  H  H      . GLY A 1 76  ? 8.829   34.939  22.012  1.00 38.05  ? 75  GLY A H      1 
ATOM   1167  H  HA2    . GLY A 1 76  ? 11.195  35.802  21.328  1.00 31.07  ? 75  GLY A HA2    1 
ATOM   1168  H  HA3    . GLY A 1 76  ? 9.919   35.808  20.397  1.00 31.07  ? 75  GLY A HA3    1 
ATOM   1169  N  N      . GLU A 1 77  ? 11.329  38.230  21.048  1.00 23.63  ? 76  GLU A N      1 
ATOM   1170  C  CA     . GLU A 1 77  ? 11.410  39.687  21.106  1.00 26.89  ? 76  GLU A CA     1 
ATOM   1171  C  C      . GLU A 1 77  ? 11.108  40.358  19.768  1.00 27.95  ? 76  GLU A C      1 
ATOM   1172  O  O      . GLU A 1 77  ? 10.573  41.478  19.744  1.00 28.32  ? 76  GLU A O      1 
ATOM   1173  C  CB     . GLU A 1 77  ? 12.791  40.138  21.570  1.00 27.88  ? 76  GLU A CB     1 
ATOM   1174  C  CG     . GLU A 1 77  ? 13.115  39.926  23.042  1.00 33.83  ? 76  GLU A CG     1 
ATOM   1175  C  CD     . GLU A 1 77  ? 14.515  40.426  23.401  1.00 34.21  ? 76  GLU A CD     1 
ATOM   1176  O  OE1    . GLU A 1 77  ? 15.511  39.963  22.802  1.00 31.90  ? 76  GLU A OE1    1 
ATOM   1177  O  OE2    . GLU A 1 77  ? 14.640  41.316  24.262  1.00 43.52  ? 76  GLU A OE2    1 
ATOM   1178  H  H      . GLU A 1 77  ? 12.056  37.845  20.796  1.00 28.39  ? 76  GLU A H      1 
ATOM   1179  H  HA     . GLU A 1 77  ? 10.759  39.991  21.757  1.00 32.30  ? 76  GLU A HA     1 
ATOM   1180  H  HB2    . GLU A 1 77  ? 13.455  39.649  21.059  1.00 33.49  ? 76  GLU A HB2    1 
ATOM   1181  H  HB3    . GLU A 1 77  ? 12.872  41.089  21.395  1.00 33.49  ? 76  GLU A HB3    1 
ATOM   1182  H  HG2    . GLU A 1 77  ? 12.472  40.411  23.583  1.00 40.63  ? 76  GLU A HG2    1 
ATOM   1183  H  HG3    . GLU A 1 77  ? 13.071  38.978  23.245  1.00 40.63  ? 76  GLU A HG3    1 
ATOM   1184  N  N      . GLY A 1 78  ? 11.440  39.697  18.657  1.00 23.35  ? 77  GLY A N      1 
ATOM   1185  C  CA     . GLY A 1 78  ? 11.187  40.253  17.343  1.00 26.42  ? 77  GLY A CA     1 
ATOM   1186  C  C      . GLY A 1 78  ? 10.979  39.097  16.393  1.00 24.91  ? 77  GLY A C      1 
ATOM   1187  O  O      . GLY A 1 78  ? 11.461  37.984  16.634  1.00 21.92  ? 77  GLY A O      1 
ATOM   1188  H  H      . GLY A 1 78  ? 11.814  38.923  18.645  1.00 28.05  ? 77  GLY A H      1 
ATOM   1189  H  HA2    . GLY A 1 78  ? 10.393  40.810  17.357  1.00 31.74  ? 77  GLY A HA2    1 
ATOM   1190  H  HA3    . GLY A 1 78  ? 11.942  40.786  17.048  1.00 31.74  ? 77  GLY A HA3    1 
ATOM   1191  N  N      . PHE A 1 79  ? 10.267  39.367  15.304  1.00 22.43  ? 78  PHE A N      1 
ATOM   1192  C  CA     . PHE A 1 79  ? 9.821   38.280  14.447  1.00 23.30  ? 78  PHE A CA     1 
ATOM   1193  C  C      . PHE A 1 79  ? 10.187  38.563  13.005  1.00 24.12  ? 78  PHE A C      1 
ATOM   1194  O  O      . PHE A 1 79  ? 9.876   39.640  12.488  1.00 22.87  ? 78  PHE A O      1 
ATOM   1195  C  CB     . PHE A 1 79  ? 8.330   38.075  14.573  1.00 25.45  ? 78  PHE A CB     1 
ATOM   1196  C  CG     . PHE A 1 79  ? 7.926   37.715  15.961  1.00 22.52  ? 78  PHE A CG     1 
ATOM   1197  C  CD1    . PHE A 1 79  ? 7.761   38.697  16.920  1.00 27.77  ? 78  PHE A CD1    1 
ATOM   1198  C  CD2    . PHE A 1 79  ? 7.801   36.384  16.322  1.00 26.41  ? 78  PHE A CD2    1 
ATOM   1199  C  CE1    . PHE A 1 79  ? 7.446   38.345  18.199  1.00 24.75  ? 78  PHE A CE1    1 
ATOM   1200  C  CE2    . PHE A 1 79  ? 7.483   36.024  17.592  1.00 26.02  ? 78  PHE A CE2    1 
ATOM   1201  C  CZ     . PHE A 1 79  ? 7.312   36.995  18.541  1.00 24.44  ? 78  PHE A CZ     1 
ATOM   1202  H  H      . PHE A 1 79  ? 10.037  40.155  15.048  1.00 26.95  ? 78  PHE A H      1 
ATOM   1203  H  HA     . PHE A 1 79  ? 10.278  37.465  14.709  1.00 27.99  ? 78  PHE A HA     1 
ATOM   1204  H  HB2    . PHE A 1 79  ? 7.875   38.896  14.329  1.00 30.57  ? 78  PHE A HB2    1 
ATOM   1205  H  HB3    . PHE A 1 79  ? 8.057   37.356  13.982  1.00 30.57  ? 78  PHE A HB3    1 
ATOM   1206  H  HD1    . PHE A 1 79  ? 7.865   39.593  16.694  1.00 33.36  ? 78  PHE A HD1    1 
ATOM   1207  H  HD2    . PHE A 1 79  ? 7.937   35.724  15.681  1.00 31.72  ? 78  PHE A HD2    1 
ATOM   1208  H  HE1    . PHE A 1 79  ? 7.320   39.003  18.844  1.00 29.73  ? 78  PHE A HE1    1 
ATOM   1209  H  HE2    . PHE A 1 79  ? 7.383   35.127  17.815  1.00 31.26  ? 78  PHE A HE2    1 
ATOM   1210  H  HZ     . PHE A 1 79  ? 7.106   36.757  19.416  1.00 29.37  ? 78  PHE A HZ     1 
ATOM   1211  N  N      . LEU A 1 80  ? 10.815  37.579  12.363  1.00 20.71  ? 79  LEU A N      1 
ATOM   1212  C  CA     . LEU A 1 80  ? 11.048  37.589  10.920  1.00 21.19  ? 79  LEU A CA     1 
ATOM   1213  C  C      . LEU A 1 80  ? 9.871   36.880  10.254  1.00 22.92  ? 79  LEU A C      1 
ATOM   1214  O  O      . LEU A 1 80  ? 9.695   35.660  10.422  1.00 23.47  ? 79  LEU A O      1 
ATOM   1215  C  CB     . LEU A 1 80  ? 12.364  36.886  10.588  1.00 20.85  ? 79  LEU A CB     1 
ATOM   1216  C  CG     . LEU A 1 80  ? 13.225  37.465  9.506   1.00 25.77  ? 79  LEU A CG     1 
ATOM   1217  C  CD1    . LEU A 1 80  ? 13.615  38.924  9.843   1.00 26.67  ? 79  LEU A CD1    1 
ATOM   1218  C  CD2    . LEU A 1 80  ? 14.410  36.560  9.291   1.00 22.96  ? 79  LEU A CD2    1 
ATOM   1219  H  H      . LEU A 1 80  ? 11.122  36.876  12.752  1.00 24.89  ? 79  LEU A H      1 
ATOM   1220  H  HA     . LEU A 1 80  ? 11.097  38.502  10.596  1.00 25.46  ? 79  LEU A HA     1 
ATOM   1221  H  HB2    . LEU A 1 80  ? 12.902  36.875  11.395  1.00 25.05  ? 79  LEU A HB2    1 
ATOM   1222  H  HB3    . LEU A 1 80  ? 12.152  35.979  10.318  1.00 25.05  ? 79  LEU A HB3    1 
ATOM   1223  H  HG     . LEU A 1 80  ? 12.745  37.515  8.665   1.00 30.96  ? 79  LEU A HG     1 
ATOM   1224  H  HD11   . LEU A 1 80  ? 14.343  39.198  9.265   1.00 32.04  ? 79  LEU A HD11   1 
ATOM   1225  H  HD12   . LEU A 1 80  ? 12.845  39.498  9.700   1.00 32.04  ? 79  LEU A HD12   1 
ATOM   1226  H  HD13   . LEU A 1 80  ? 13.894  38.970  10.771  1.00 32.04  ? 79  LEU A HD13   1 
ATOM   1227  H  HD21   . LEU A 1 80  ? 14.978  36.941  8.604   1.00 27.58  ? 79  LEU A HD21   1 
ATOM   1228  H  HD22   . LEU A 1 80  ? 14.903  36.482  10.123  1.00 27.58  ? 79  LEU A HD22   1 
ATOM   1229  H  HD23   . LEU A 1 80  ? 14.094  35.686  9.012   1.00 27.58  ? 79  LEU A HD23   1 
ATOM   1230  N  N      . CYS A 1 81  ? 9.040   37.644  9.542   1.00 21.88  ? 80  CYS A N      1 
ATOM   1231  C  CA     . CYS A 1 81  ? 7.806   37.125  8.952   1.00 22.19  ? 80  CYS A CA     1 
ATOM   1232  C  C      . CYS A 1 81  ? 8.069   36.835  7.482   1.00 22.86  ? 80  CYS A C      1 
ATOM   1233  O  O      . CYS A 1 81  ? 8.108   37.759  6.679   1.00 23.49  ? 80  CYS A O      1 
ATOM   1234  C  CB     . CYS A 1 81  ? 6.685   38.136  9.104   1.00 28.15  ? 80  CYS A CB     1 
ATOM   1235  S  SG     . CYS A 1 81  ? 6.131   38.285  10.789  1.00 29.50  ? 80  CYS A SG     1 
ATOM   1236  H  H      . CYS A 1 81  ? 9.172   38.479  9.385   1.00 26.29  ? 80  CYS A H      1 
ATOM   1237  H  HA     . CYS A 1 81  ? 7.560   36.299  9.397   1.00 26.66  ? 80  CYS A HA     1 
ATOM   1238  H  HB2    . CYS A 1 81  ? 7.001   39.006  8.812   1.00 33.82  ? 80  CYS A HB2    1 
ATOM   1239  H  HB3    . CYS A 1 81  ? 5.931   37.857  8.561   1.00 33.82  ? 80  CYS A HB3    1 
ATOM   1240  H  HG     . CYS A 1 81  ? 5.278   39.128  10.847  1.00 35.43  ? 80  CYS A HG     1 
ATOM   1241  N  N      . VAL A 1 82  ? 8.249   35.553  7.139   1.00 21.37  ? 81  VAL A N      1 
ATOM   1242  C  CA     . VAL A 1 82  ? 8.816   35.145  5.851   1.00 22.38  ? 81  VAL A CA     1 
ATOM   1243  C  C      . VAL A 1 82  ? 7.725   34.595  4.931   1.00 25.41  ? 81  VAL A C      1 
ATOM   1244  O  O      . VAL A 1 82  ? 6.969   33.691  5.309   1.00 20.74  ? 81  VAL A O      1 
ATOM   1245  C  CB     . VAL A 1 82  ? 9.922   34.093  6.033   1.00 20.02  ? 81  VAL A CB     1 
ATOM   1246  C  CG1    . VAL A 1 82  ? 10.693  33.913  4.681   1.00 20.67  ? 81  VAL A CG1    1 
ATOM   1247  C  CG2    . VAL A 1 82  ? 10.887  34.442  7.146   1.00 21.45  ? 81  VAL A CG2    1 
ATOM   1248  H  H      . VAL A 1 82  ? 8.046   34.890  7.649   1.00 25.68  ? 81  VAL A H      1 
ATOM   1249  H  HA     . VAL A 1 82  ? 9.179   35.940  5.431   1.00 26.88  ? 81  VAL A HA     1 
ATOM   1250  H  HB     . VAL A 1 82  ? 9.502   33.258  6.291   1.00 24.06  ? 81  VAL A HB     1 
ATOM   1251  H  HG11   . VAL A 1 82  ? 11.433  33.302  4.818   1.00 24.84  ? 81  VAL A HG11   1 
ATOM   1252  H  HG12   . VAL A 1 82  ? 10.085  33.553  4.016   1.00 24.84  ? 81  VAL A HG12   1 
ATOM   1253  H  HG13   . VAL A 1 82  ? 11.026  34.777  4.390   1.00 24.84  ? 81  VAL A HG13   1 
ATOM   1254  H  HG21   . VAL A 1 82  ? 11.605  33.790  7.157   1.00 25.77  ? 81  VAL A HG21   1 
ATOM   1255  H  HG22   . VAL A 1 82  ? 11.248  35.328  6.985   1.00 25.77  ? 81  VAL A HG22   1 
ATOM   1256  H  HG23   . VAL A 1 82  ? 10.413  34.427  7.992   1.00 25.77  ? 81  VAL A HG23   1 
ATOM   1257  N  N      . PHE A 1 83  ? 7.678   35.097  3.701   1.00 25.19  ? 82  PHE A N      1 
ATOM   1258  C  CA     . PHE A 1 83  ? 6.980   34.394  2.622   1.00 26.10  ? 82  PHE A CA     1 
ATOM   1259  C  C      . PHE A 1 83  ? 7.952   34.179  1.468   1.00 23.93  ? 82  PHE A C      1 
ATOM   1260  O  O      . PHE A 1 83  ? 9.048   34.747  1.447   1.00 23.27  ? 82  PHE A O      1 
ATOM   1261  C  CB     . PHE A 1 83  ? 5.744   35.177  2.154   1.00 23.52  ? 82  PHE A CB     1 
ATOM   1262  C  CG     . PHE A 1 83  ? 6.078   36.474  1.478   1.00 27.89  ? 82  PHE A CG     1 
ATOM   1263  C  CD1    . PHE A 1 83  ? 6.388   37.612  2.218   1.00 23.66  ? 82  PHE A CD1    1 
ATOM   1264  C  CD2    . PHE A 1 83  ? 6.094   36.552  0.073   1.00 25.91  ? 82  PHE A CD2    1 
ATOM   1265  C  CE1    . PHE A 1 83  ? 6.720   38.820  1.570   1.00 28.38  ? 82  PHE A CE1    1 
ATOM   1266  C  CE2    . PHE A 1 83  ? 6.423   37.731  -0.572  1.00 28.55  ? 82  PHE A CE2    1 
ATOM   1267  C  CZ     . PHE A 1 83  ? 6.737   38.879  0.170   1.00 28.43  ? 82  PHE A CZ     1 
ATOM   1268  H  H      . PHE A 1 83  ? 8.041   35.840  3.466   1.00 30.26  ? 82  PHE A H      1 
ATOM   1269  H  HA     . PHE A 1 83  ? 6.672   33.529  2.935   1.00 31.36  ? 82  PHE A HA     1 
ATOM   1270  H  HB2    . PHE A 1 83  ? 5.249   34.632  1.523   1.00 28.26  ? 82  PHE A HB2    1 
ATOM   1271  H  HB3    . PHE A 1 83  ? 5.191   35.378  2.925   1.00 28.26  ? 82  PHE A HB3    1 
ATOM   1272  H  HD1    . PHE A 1 83  ? 6.377   37.575  3.147   1.00 28.42  ? 82  PHE A HD1    1 
ATOM   1273  H  HD2    . PHE A 1 83  ? 5.880   35.800  -0.429  1.00 31.12  ? 82  PHE A HD2    1 
ATOM   1274  H  HE1    . PHE A 1 83  ? 6.927   39.576  2.071   1.00 34.09  ? 82  PHE A HE1    1 
ATOM   1275  H  HE2    . PHE A 1 83  ? 6.435   37.763  -1.501  1.00 34.29  ? 82  PHE A HE2    1 
ATOM   1276  H  HZ     . PHE A 1 83  ? 6.955   39.673  -0.264  1.00 34.15  ? 82  PHE A HZ     1 
ATOM   1277  N  N      . ALA A 1 84  ? 7.533   33.368  0.496   1.00 24.61  ? 83  ALA A N      1 
ATOM   1278  C  CA     . ALA A 1 84  ? 8.281   33.147  -0.736  1.00 25.46  ? 83  ALA A CA     1 
ATOM   1279  C  C      . ALA A 1 84  ? 7.633   33.936  -1.876  1.00 29.74  ? 83  ALA A C      1 
ATOM   1280  O  O      . ALA A 1 84  ? 6.401   33.947  -2.018  1.00 27.82  ? 83  ALA A O      1 
ATOM   1281  C  CB     . ALA A 1 84  ? 8.350   31.654  -1.053  1.00 26.05  ? 83  ALA A CB     1 
ATOM   1282  H  H      . ALA A 1 84  ? 6.798   32.923  0.530   1.00 29.57  ? 83  ALA A H      1 
ATOM   1283  H  HA     . ALA A 1 84  ? 9.190   33.472  -0.643  1.00 30.58  ? 83  ALA A HA     1 
ATOM   1284  H  HB1    . ALA A 1 84  ? 8.856   31.527  -1.871  1.00 31.29  ? 83  ALA A HB1    1 
ATOM   1285  H  HB2    . ALA A 1 84  ? 8.787   31.195  -0.319  1.00 31.29  ? 83  ALA A HB2    1 
ATOM   1286  H  HB3    . ALA A 1 84  ? 7.449   31.313  -1.166  1.00 31.29  ? 83  ALA A HB3    1 
ATOM   1287  N  N      . ILE A 1 85  ? 8.466   34.632  -2.660  1.00 24.64  ? 84  ILE A N      1 
ATOM   1288  C  CA     . ILE A 1 85  ? 7.948   35.529  -3.683  1.00 31.96  ? 84  ILE A CA     1 
ATOM   1289  C  C      . ILE A 1 85  ? 7.286   34.782  -4.822  1.00 34.87  ? 84  ILE A C      1 
ATOM   1290  O  O      . ILE A 1 85  ? 6.644   35.409  -5.669  1.00 37.19  ? 84  ILE A O      1 
ATOM   1291  C  CB     . ILE A 1 85  ? 9.045   36.435  -4.279  1.00 32.77  ? 84  ILE A CB     1 
ATOM   1292  C  CG1    . ILE A 1 85  ? 10.229  35.595  -4.767  1.00 32.68  ? 84  ILE A CG1    1 
ATOM   1293  C  CG2    . ILE A 1 85  ? 9.469   37.466  -3.266  1.00 33.35  ? 84  ILE A CG2    1 
ATOM   1294  C  CD1    . ILE A 1 85  ? 10.189  35.272  -6.220  1.00 37.32  ? 84  ILE A CD1    1 
ATOM   1295  H  H      . ILE A 1 85  ? 9.324   34.600  -2.615  1.00 29.60  ? 84  ILE A H      1 
ATOM   1296  H  HA     . ILE A 1 85  ? 7.298   36.098  -3.242  1.00 38.38  ? 84  ILE A HA     1 
ATOM   1297  H  HB     . ILE A 1 85  ? 8.685   36.903  -5.049  1.00 39.35  ? 84  ILE A HB     1 
ATOM   1298  H  HG12   . ILE A 1 85  ? 11.048  36.085  -4.596  1.00 39.25  ? 84  ILE A HG12   1 
ATOM   1299  H  HG13   . ILE A 1 85  ? 10.236  34.757  -4.279  1.00 39.25  ? 84  ILE A HG13   1 
ATOM   1300  H  HG21   . ILE A 1 85  ? 10.142  38.041  -3.664  1.00 40.06  ? 84  ILE A HG21   1 
ATOM   1301  H  HG22   . ILE A 1 85  ? 8.696   37.992  -3.008  1.00 40.06  ? 84  ILE A HG22   1 
ATOM   1302  H  HG23   . ILE A 1 85  ? 9.837   37.015  -2.490  1.00 40.06  ? 84  ILE A HG23   1 
ATOM   1303  H  HD11   . ILE A 1 85  ? 11.039  34.882  -6.480  1.00 44.81  ? 84  ILE A HD11   1 
ATOM   1304  H  HD12   . ILE A 1 85  ? 9.471   34.641  -6.383  1.00 44.81  ? 84  ILE A HD12   1 
ATOM   1305  H  HD13   . ILE A 1 85  ? 10.033  36.088  -6.720  1.00 44.81  ? 84  ILE A HD13   1 
ATOM   1306  N  N      . ASN A 1 86  ? 7.405   33.462  -4.845  1.00 30.38  ? 85  ASN A N      1 
ATOM   1307  C  CA     . ASN A 1 86  ? 6.799   32.618  -5.858  1.00 37.38  ? 85  ASN A CA     1 
ATOM   1308  C  C      . ASN A 1 86  ? 5.661   31.777  -5.303  1.00 37.34  ? 85  ASN A C      1 
ATOM   1309  O  O      . ASN A 1 86  ? 5.244   30.809  -5.942  1.00 35.07  ? 85  ASN A O      1 
ATOM   1310  C  CB     . ASN A 1 86  ? 7.855   31.712  -6.472  1.00 35.71  ? 85  ASN A CB     1 
ATOM   1311  C  CG     . ASN A 1 86  ? 8.341   30.666  -5.506  1.00 36.71  ? 85  ASN A CG     1 
ATOM   1312  O  OD1    . ASN A 1 86  ? 8.312   30.858  -4.279  1.00 34.97  ? 85  ASN A OD1    1 
ATOM   1313  N  ND2    . ASN A 1 86  ? 8.756   29.534  -6.043  1.00 37.28  ? 85  ASN A ND2    1 
ATOM   1314  H  H      . ASN A 1 86  ? 7.851   33.016  -4.260  1.00 36.48  ? 85  ASN A H      1 
ATOM   1315  H  HA     . ASN A 1 86  ? 6.437   33.184  -6.559  1.00 44.89  ? 85  ASN A HA     1 
ATOM   1316  H  HB2    . ASN A 1 86  ? 7.476   31.259  -7.242  1.00 42.88  ? 85  ASN A HB2    1 
ATOM   1317  H  HB3    . ASN A 1 86  ? 8.615   32.249  -6.744  1.00 42.88  ? 85  ASN A HB3    1 
ATOM   1318  H  HD21   . ASN A 1 86  ? 9.046   28.900  -5.539  1.00 44.77  ? 85  ASN A HD21   1 
ATOM   1319  H  HD22   . ASN A 1 86  ? 8.737   29.430  -6.896  1.00 44.77  ? 85  ASN A HD22   1 
ATOM   1320  N  N      . ASN A 1 87  ? 5.173   32.100  -4.112  1.00 36.10  ? 86  ASN A N      1 
ATOM   1321  C  CA     . ASN A 1 87  ? 4.080   31.360  -3.486  1.00 33.97  ? 86  ASN A CA     1 
ATOM   1322  C  C      . ASN A 1 87  ? 3.087   32.375  -2.926  1.00 35.37  ? 86  ASN A C      1 
ATOM   1323  O  O      . ASN A 1 87  ? 3.247   32.901  -1.820  1.00 32.52  ? 86  ASN A O      1 
ATOM   1324  C  CB     . ASN A 1 87  ? 4.579   30.420  -2.403  1.00 36.52  ? 86  ASN A CB     1 
ATOM   1325  C  CG     . ASN A 1 87  ? 3.461   29.537  -1.872  1.00 41.39  ? 86  ASN A CG     1 
ATOM   1326  O  OD1    . ASN A 1 87  ? 2.635   29.985  -1.088  1.00 37.60  ? 86  ASN A OD1    1 
ATOM   1327  N  ND2    . ASN A 1 87  ? 3.431   28.282  -2.311  1.00 45.21  ? 86  ASN A ND2    1 
ATOM   1328  H  H      . ASN A 1 87  ? 5.463   32.756  -3.638  1.00 43.35  ? 86  ASN A H      1 
ATOM   1329  H  HA     . ASN A 1 87  ? 3.635   30.827  -4.163  1.00 40.79  ? 86  ASN A HA     1 
ATOM   1330  H  HB2    . ASN A 1 87  ? 5.271   29.848  -2.768  1.00 43.85  ? 86  ASN A HB2    1 
ATOM   1331  H  HB3    . ASN A 1 87  ? 4.933   30.940  -1.664  1.00 43.85  ? 86  ASN A HB3    1 
ATOM   1332  H  HD21   . ASN A 1 87  ? 2.817   27.746  -2.038  1.00 54.29  ? 86  ASN A HD21   1 
ATOM   1333  H  HD22   . ASN A 1 87  ? 4.026   28.007  -2.868  1.00 54.29  ? 86  ASN A HD22   1 
ATOM   1334  N  N      . THR A 1 88  ? 2.053   32.646  -3.708  1.00 36.83  ? 87  THR A N      1 
ATOM   1335  C  CA     . THR A 1 88  ? 1.065   33.632  -3.299  1.00 38.90  ? 87  THR A CA     1 
ATOM   1336  C  C      . THR A 1 88  ? 0.432   33.282  -1.956  1.00 34.00  ? 87  THR A C      1 
ATOM   1337  O  O      . THR A 1 88  ? 0.171   34.177  -1.144  1.00 37.24  ? 87  THR A O      1 
ATOM   1338  C  CB     . THR A 1 88  ? 0.000   33.748  -4.397  1.00 38.95  ? 87  THR A CB     1 
ATOM   1339  O  OG1    . THR A 1 88  ? 0.608   34.299  -5.565  1.00 42.48  ? 87  THR A OG1    1 
ATOM   1340  C  CG2    . THR A 1 88  ? -1.138  34.632  -3.949  1.00 42.42  ? 87  THR A CG2    1 
ATOM   1341  H  H      . THR A 1 88  ? 1.901   32.279  -4.470  1.00 44.23  ? 87  THR A H      1 
ATOM   1342  H  HA     . THR A 1 88  ? 1.497   34.493  -3.189  1.00 46.71  ? 87  THR A HA     1 
ATOM   1343  H  HB     . THR A 1 88  ? -0.368  32.873  -4.596  1.00 46.77  ? 87  THR A HB     1 
ATOM   1344  H  HG1    . THR A 1 88  ? 0.037   34.379  -6.176  1.00 51.01  ? 87  THR A HG1    1 
ATOM   1345  H  HG21   . THR A 1 88  ? -1.662  34.911  -4.716  1.00 50.94  ? 87  THR A HG21   1 
ATOM   1346  H  HG22   . THR A 1 88  ? -1.712  34.148  -3.335  1.00 50.94  ? 87  THR A HG22   1 
ATOM   1347  H  HG23   . THR A 1 88  ? -0.791  35.419  -3.502  1.00 50.94  ? 87  THR A HG23   1 
ATOM   1348  N  N      . LYS A 1 89  ? 0.163   31.999  -1.704  1.00 35.70  ? 88  LYS A N      1 
ATOM   1349  C  CA     . LYS A 1 89  ? -0.511  31.627  -0.458  1.00 39.04  ? 88  LYS A CA     1 
ATOM   1350  C  C      . LYS A 1 89  ? 0.375   31.911  0.751   1.00 37.09  ? 88  LYS A C      1 
ATOM   1351  O  O      . LYS A 1 89  ? -0.124  32.309  1.804   1.00 32.15  ? 88  LYS A O      1 
ATOM   1352  C  CB     . LYS A 1 89  ? -0.933  30.151  -0.484  1.00 38.48  ? 88  LYS A CB     1 
ATOM   1353  C  CG     . LYS A 1 89  ? -1.610  29.635  0.832   1.00 44.72  ? 88  LYS A CG     1 
ATOM   1354  C  CD     . LYS A 1 89  ? -1.321  28.162  1.165   1.00 49.47  ? 88  LYS A CD     1 
ATOM   1355  C  CE     . LYS A 1 89  ? -1.015  27.941  2.658   1.00 51.89  ? 88  LYS A CE     1 
ATOM   1356  N  NZ     . LYS A 1 89  ? 0.433   28.136  2.913   1.00 47.74  ? 88  LYS A NZ     1 
ATOM   1357  H  H      . LYS A 1 89  ? 0.355   31.341  -2.224  1.00 42.87  ? 88  LYS A H      1 
ATOM   1358  H  HA     . LYS A 1 89  ? -1.319  32.158  -0.378  1.00 46.88  ? 88  LYS A HA     1 
ATOM   1359  H  HB2    . LYS A 1 89  ? -1.567  30.025  -1.206  1.00 46.21  ? 88  LYS A HB2    1 
ATOM   1360  H  HB3    . LYS A 1 89  ? -0.144  29.608  -0.637  1.00 46.21  ? 88  LYS A HB3    1 
ATOM   1361  H  HG2    . LYS A 1 89  ? -1.290  30.170  1.575   1.00 53.70  ? 88  LYS A HG2    1 
ATOM   1362  H  HG3    . LYS A 1 89  ? -2.571  29.731  0.744   1.00 53.70  ? 88  LYS A HG3    1 
ATOM   1363  H  HD2    . LYS A 1 89  ? -2.097  27.627  0.935   1.00 59.40  ? 88  LYS A HD2    1 
ATOM   1364  H  HD3    . LYS A 1 89  ? -0.552  27.867  0.653   1.00 59.40  ? 88  LYS A HD3    1 
ATOM   1365  H  HE2    . LYS A 1 89  ? -1.514  28.579  3.191   1.00 62.31  ? 88  LYS A HE2    1 
ATOM   1366  H  HE3    . LYS A 1 89  ? -1.257  27.036  2.911   1.00 62.31  ? 88  LYS A HE3    1 
ATOM   1367  H  HZ1    . LYS A 1 89  ? 0.608   28.015  3.777   1.00 57.33  ? 88  LYS A HZ1    1 
ATOM   1368  H  HZ2    . LYS A 1 89  ? 0.907   27.553  2.437   1.00 57.33  ? 88  LYS A HZ2    1 
ATOM   1369  H  HZ3    . LYS A 1 89  ? 0.674   28.961  2.682   1.00 57.33  ? 88  LYS A HZ3    1 
ATOM   1370  N  N      . SER A 1 90  ? 1.697   31.726  0.617   1.00 35.92  ? 89  SER A N      1 
ATOM   1371  C  CA     . SER A 1 90  ? 2.602   32.060  1.716   1.00 31.41  ? 89  SER A CA     1 
ATOM   1372  C  C      . SER A 1 90  ? 2.541   33.542  2.038   1.00 32.73  ? 89  SER A C      1 
ATOM   1373  O  O      . SER A 1 90  ? 2.671   33.943  3.201   1.00 32.15  ? 89  SER A O      1 
ATOM   1374  C  CB     . SER A 1 90  ? 4.038   31.653  1.361   1.00 31.67  ? 89  SER A CB     1 
ATOM   1375  O  OG     . SER A 1 90  ? 4.618   32.605  0.492   1.00 31.33  ? 89  SER A OG     1 
ATOM   1376  H  H      . SER A 1 90  ? 2.084   31.416  -0.086  1.00 43.14  ? 89  SER A H      1 
ATOM   1377  H  HA     . SER A 1 90  ? 2.338   31.561  2.505   1.00 37.73  ? 89  SER A HA     1 
ATOM   1378  H  HB2    . SER A 1 90  ? 4.564   31.603  2.175   1.00 38.04  ? 89  SER A HB2    1 
ATOM   1379  H  HB3    . SER A 1 90  ? 4.024   30.788  0.922   1.00 38.04  ? 89  SER A HB3    1 
ATOM   1380  H  HG     . SER A 1 90  ? 4.172   32.655  -0.218  1.00 37.63  ? 89  SER A HG     1 
ATOM   1381  N  N      . PHE A 1 91  ? 2.351   34.377  1.018   1.00 29.67  ? 90  PHE A N      1 
ATOM   1382  C  CA     . PHE A 1 91  ? 2.167   35.802  1.235   1.00 29.75  ? 90  PHE A CA     1 
ATOM   1383  C  C      . PHE A 1 91  ? 0.837   36.089  1.918   1.00 33.95  ? 90  PHE A C      1 
ATOM   1384  O  O      . PHE A 1 91  ? 0.766   36.914  2.832   1.00 30.81  ? 90  PHE A O      1 
ATOM   1385  C  CB     . PHE A 1 91  ? 2.254   36.529  -0.116  1.00 33.94  ? 90  PHE A CB     1 
ATOM   1386  C  CG     . PHE A 1 91  ? 2.071   38.007  -0.029  1.00 31.15  ? 90  PHE A CG     1 
ATOM   1387  C  CD1    . PHE A 1 91  ? 3.056   38.810  0.505   1.00 32.12  ? 90  PHE A CD1    1 
ATOM   1388  C  CD2    . PHE A 1 91  ? 0.917   38.600  -0.494  1.00 34.96  ? 90  PHE A CD2    1 
ATOM   1389  C  CE1    . PHE A 1 91  ? 2.905   40.162  0.600   1.00 32.63  ? 90  PHE A CE1    1 
ATOM   1390  C  CE2    . PHE A 1 91  ? 0.764   39.961  -0.418  1.00 34.93  ? 90  PHE A CE2    1 
ATOM   1391  C  CZ     . PHE A 1 91  ? 1.765   40.750  0.126   1.00 37.93  ? 90  PHE A CZ     1 
ATOM   1392  H  H      . PHE A 1 91  ? 2.325   34.142  0.192   1.00 35.63  ? 90  PHE A H      1 
ATOM   1393  H  HA     . PHE A 1 91  ? 2.870   36.137  1.813   1.00 35.74  ? 90  PHE A HA     1 
ATOM   1394  H  HB2    . PHE A 1 91  ? 3.129   36.363  -0.501  1.00 40.76  ? 90  PHE A HB2    1 
ATOM   1395  H  HB3    . PHE A 1 91  ? 1.563   36.181  -0.701  1.00 40.76  ? 90  PHE A HB3    1 
ATOM   1396  H  HD1    . PHE A 1 91  ? 3.844   38.419  0.808   1.00 38.58  ? 90  PHE A HD1    1 
ATOM   1397  H  HD2    . PHE A 1 91  ? 0.242   38.076  -0.861  1.00 41.98  ? 90  PHE A HD2    1 
ATOM   1398  H  HE1    . PHE A 1 91  ? 3.574   40.682  0.984   1.00 39.19  ? 90  PHE A HE1    1 
ATOM   1399  H  HE2    . PHE A 1 91  ? -0.016  40.357  -0.733  1.00 41.95  ? 90  PHE A HE2    1 
ATOM   1400  H  HZ     . PHE A 1 91  ? 1.662   41.673  0.169   1.00 45.55  ? 90  PHE A HZ     1 
ATOM   1401  N  N      . GLU A 1 92  ? -0.227  35.432  1.475   1.00 33.68  ? 91  GLU A N      1 
ATOM   1402  C  CA     . GLU A 1 92  ? -1.523  35.589  2.134   1.00 35.59  ? 91  GLU A CA     1 
ATOM   1403  C  C      . GLU A 1 92  ? -1.442  35.120  3.587   1.00 37.01  ? 91  GLU A C      1 
ATOM   1404  O  O      . GLU A 1 92  ? -2.015  35.748  4.484   1.00 39.29  ? 91  GLU A O      1 
ATOM   1405  C  CB     . GLU A 1 92  ? -2.570  34.814  1.340   1.00 37.68  ? 91  GLU A CB     1 
ATOM   1406  C  CG     . GLU A 1 92  ? -2.983  35.501  0.028   1.00 40.99  ? 91  GLU A CG     1 
ATOM   1407  C  CD     . GLU A 1 92  ? -3.686  34.546  -0.943  1.00 47.00  ? 91  GLU A CD     1 
ATOM   1408  O  OE1    . GLU A 1 92  ? -3.691  33.315  -0.693  1.00 45.15  ? 91  GLU A OE1    1 
ATOM   1409  O  OE2    . GLU A 1 92  ? -4.229  35.024  -1.964  1.00 46.63  ? 91  GLU A OE2    1 
ATOM   1410  H  H      . GLU A 1 92  ? -0.230  34.895  0.804   1.00 40.45  ? 91  GLU A H      1 
ATOM   1411  H  HA     . GLU A 1 92  ? -1.794  36.520  2.149   1.00 42.74  ? 91  GLU A HA     1 
ATOM   1412  H  HB2    . GLU A 1 92  ? -2.210  33.941  1.118   1.00 45.25  ? 91  GLU A HB2    1 
ATOM   1413  H  HB3    . GLU A 1 92  ? -3.366  34.715  1.887   1.00 45.25  ? 91  GLU A HB3    1 
ATOM   1414  H  HG2    . GLU A 1 92  ? -3.594  36.227  0.230   1.00 49.23  ? 91  GLU A HG2    1 
ATOM   1415  H  HG3    . GLU A 1 92  ? -2.191  35.846  -0.411  1.00 49.23  ? 91  GLU A HG3    1 
ATOM   1416  N  N      . ASP A 1 93  ? -0.655  34.068  3.845   1.00 37.96  ? 92  ASP A N      1 
ATOM   1417  C  CA     . ASP A 1 93  ? -0.523  33.552  5.203   1.00 37.54  ? 92  ASP A CA     1 
ATOM   1418  C  C      . ASP A 1 93  ? 0.094   34.571  6.156   1.00 35.76  ? 92  ASP A C      1 
ATOM   1419  O  O      . ASP A 1 93  ? -0.066  34.449  7.374   1.00 35.63  ? 92  ASP A O      1 
ATOM   1420  C  CB     . ASP A 1 93  ? 0.335   32.288  5.228   1.00 36.39  ? 92  ASP A CB     1 
ATOM   1421  C  CG     . ASP A 1 93  ? -0.397  31.071  4.734   1.00 39.98  ? 92  ASP A CG     1 
ATOM   1422  O  OD1    . ASP A 1 93  ? -1.634  31.159  4.591   1.00 39.21  ? 92  ASP A OD1    1 
ATOM   1423  O  OD2    . ASP A 1 93  ? 0.256   30.019  4.522   1.00 39.07  ? 92  ASP A OD2    1 
ATOM   1424  H  H      . ASP A 1 93  ? -0.194  33.644  3.256   1.00 45.59  ? 92  ASP A H      1 
ATOM   1425  H  HA     . ASP A 1 93  ? -1.414  33.326  5.514   1.00 45.09  ? 92  ASP A HA     1 
ATOM   1426  H  HB2    . ASP A 1 93  ? 1.110   32.422  4.659   1.00 43.70  ? 92  ASP A HB2    1 
ATOM   1427  H  HB3    . ASP A 1 93  ? 0.618   32.117  6.140   1.00 43.70  ? 92  ASP A HB3    1 
ATOM   1428  N  N      . ILE A 1 94  ? 0.809   35.559  5.627   1.00 34.17  ? 93  ILE A N      1 
ATOM   1429  C  CA     . ILE A 1 94  ? 1.478   36.545  6.462   1.00 32.74  ? 93  ILE A CA     1 
ATOM   1430  C  C      . ILE A 1 94  ? 0.488   37.212  7.396   1.00 35.53  ? 93  ILE A C      1 
ATOM   1431  O  O      . ILE A 1 94  ? 0.782   37.427  8.579   1.00 33.58  ? 93  ILE A O      1 
ATOM   1432  C  CB     . ILE A 1 94  ? 2.179   37.597  5.582   1.00 35.26  ? 93  ILE A CB     1 
ATOM   1433  C  CG1    . ILE A 1 94  ? 3.365   36.975  4.865   1.00 30.01  ? 93  ILE A CG1    1 
ATOM   1434  C  CG2    . ILE A 1 94  ? 2.623   38.775  6.433   1.00 34.44  ? 93  ILE A CG2    1 
ATOM   1435  C  CD1    . ILE A 1 94  ? 4.432   36.421  5.808   1.00 29.54  ? 93  ILE A CD1    1 
ATOM   1436  H  H      . ILE A 1 94  ? 0.923   35.681  4.783   1.00 41.04  ? 93  ILE A H      1 
ATOM   1437  H  HA     . ILE A 1 94  ? 2.144   36.084  6.995   1.00 39.32  ? 93  ILE A HA     1 
ATOM   1438  H  HB     . ILE A 1 94  ? 1.552   37.916  4.915   1.00 42.34  ? 93  ILE A HB     1 
ATOM   1439  H  HG12   . ILE A 1 94  ? 3.047   36.243  4.314   1.00 36.05  ? 93  ILE A HG12   1 
ATOM   1440  H  HG13   . ILE A 1 94  ? 3.783   37.652  4.309   1.00 36.05  ? 93  ILE A HG13   1 
ATOM   1441  H  HG21   . ILE A 1 94  ? 3.326   39.254  5.968   1.00 41.37  ? 93  ILE A HG21   1 
ATOM   1442  H  HG22   . ILE A 1 94  ? 1.865   39.362  6.581   1.00 41.37  ? 93  ILE A HG22   1 
ATOM   1443  H  HG23   . ILE A 1 94  ? 2.955   38.444  7.283   1.00 41.37  ? 93  ILE A HG23   1 
ATOM   1444  H  HD11   . ILE A 1 94  ? 5.232   36.219  5.297   1.00 35.48  ? 93  ILE A HD11   1 
ATOM   1445  H  HD12   . ILE A 1 94  ? 4.632   37.086  6.485   1.00 35.48  ? 93  ILE A HD12   1 
ATOM   1446  H  HD13   . ILE A 1 94  ? 4.095   35.614  6.228   1.00 35.48  ? 93  ILE A HD13   1 
ATOM   1447  N  N      . HIS A 1 95  ? -0.680  37.598  6.872   1.00 38.25  ? 94  HIS A N      1 
ATOM   1448  C  CA     . HIS A 1 95  ? -1.666  38.290  7.699   1.00 40.81  ? 94  HIS A CA     1 
ATOM   1449  C  C      . HIS A 1 95  ? -1.960  37.488  8.962   1.00 35.90  ? 94  HIS A C      1 
ATOM   1450  O  O      . HIS A 1 95  ? -1.959  38.028  10.073  1.00 38.49  ? 94  HIS A O      1 
ATOM   1451  C  CB     . HIS A 1 95  ? -2.945  38.544  6.889   1.00 39.48  ? 94  HIS A CB     1 
ATOM   1452  C  CG     . HIS A 1 95  ? -4.074  39.121  7.695   1.00 43.65  ? 94  HIS A CG     1 
ATOM   1453  N  ND1    . HIS A 1 95  ? -5.192  38.390  8.036   1.00 46.44  ? 94  HIS A ND1    1 
ATOM   1454  C  CD2    . HIS A 1 95  ? -4.252  40.352  8.234   1.00 42.01  ? 94  HIS A CD2    1 
ATOM   1455  C  CE1    . HIS A 1 95  ? -6.007  39.141  8.753   1.00 42.36  ? 94  HIS A CE1    1 
ATOM   1456  N  NE2    . HIS A 1 95  ? -5.464  40.339  8.884   1.00 42.74  ? 94  HIS A NE2    1 
ATOM   1457  H  H      . HIS A 1 95  ? -0.921  37.472  6.056   1.00 45.93  ? 94  HIS A H      1 
ATOM   1458  H  HA     . HIS A 1 95  ? -1.316  39.155  7.966   1.00 49.01  ? 94  HIS A HA     1 
ATOM   1459  H  HB2    . HIS A 1 95  ? -2.743  39.169  6.175   1.00 47.41  ? 94  HIS A HB2    1 
ATOM   1460  H  HB3    . HIS A 1 95  ? -3.249  37.702  6.515   1.00 47.41  ? 94  HIS A HB3    1 
ATOM   1461  H  HD2    . HIS A 1 95  ? -3.664  41.070  8.175   1.00 50.44  ? 94  HIS A HD2    1 
ATOM   1462  H  HE1    . HIS A 1 95  ? -6.825  38.873  9.106   1.00 50.87  ? 94  HIS A HE1    1 
ATOM   1463  H  HE2    . HIS A 1 95  ? -5.812  41.002  9.307   1.00 51.32  ? 94  HIS A HE2    1 
ATOM   1464  N  N      . HIS A 1 96  ? -2.168  36.184  8.810   1.00 40.73  ? 95  HIS A N      1 
ATOM   1465  C  CA     . HIS A 1 96  ? -2.518  35.345  9.953   1.00 37.50  ? 95  HIS A CA     1 
ATOM   1466  C  C      . HIS A 1 96  ? -1.399  35.298  10.979  1.00 36.38  ? 95  HIS A C      1 
ATOM   1467  O  O      . HIS A 1 96  ? -1.659  35.319  12.185  1.00 33.89  ? 95  HIS A O      1 
ATOM   1468  C  CB     . HIS A 1 96  ? -2.878  33.940  9.466   1.00 40.28  ? 95  HIS A CB     1 
ATOM   1469  C  CG     . HIS A 1 96  ? -4.054  33.920  8.533   1.00 47.07  ? 95  HIS A CG     1 
ATOM   1470  N  ND1    . HIS A 1 96  ? -3.957  34.288  7.205   1.00 45.31  ? 95  HIS A ND1    1 
ATOM   1471  C  CD2    . HIS A 1 96  ? -5.361  33.628  8.747   1.00 50.03  ? 95  HIS A CD2    1 
ATOM   1472  C  CE1    . HIS A 1 96  ? -5.151  34.203  6.637   1.00 49.37  ? 95  HIS A CE1    1 
ATOM   1473  N  NE2    . HIS A 1 96  ? -6.017  33.800  7.549   1.00 54.56  ? 95  HIS A NE2    1 
ATOM   1474  H  H      . HIS A 1 96  ? -2.114  35.762  8.062   1.00 48.92  ? 95  HIS A H      1 
ATOM   1475  H  HA     . HIS A 1 96  ? -3.296  35.722  10.395  1.00 45.03  ? 95  HIS A HA     1 
ATOM   1476  H  HB2    . HIS A 1 96  ? -2.117  33.566  8.995   1.00 48.37  ? 95  HIS A HB2    1 
ATOM   1477  H  HB3    . HIS A 1 96  ? -3.097  33.388  10.234  1.00 48.37  ? 95  HIS A HB3    1 
ATOM   1478  H  HD2    . HIS A 1 96  ? -5.743  33.362  9.552   1.00 60.07  ? 95  HIS A HD2    1 
ATOM   1479  H  HE1    . HIS A 1 96  ? -5.346  34.395  5.748   1.00 59.28  ? 95  HIS A HE1    1 
ATOM   1480  H  HE2    . HIS A 1 96  ? -6.856  33.665  7.416   1.00 65.51  ? 95  HIS A HE2    1 
ATOM   1481  N  N      . TYR A 1 97  ? -0.145  35.245  10.523  1.00 34.99  ? 96  TYR A N      1 
ATOM   1482  C  CA     . TYR A 1 97  ? 0.963   35.225  11.464  1.00 32.53  ? 96  TYR A CA     1 
ATOM   1483  C  C      . TYR A 1 97  ? 1.039   36.540  12.223  1.00 33.98  ? 96  TYR A C      1 
ATOM   1484  O  O      . TYR A 1 97  ? 1.206   36.549  13.447  1.00 34.52  ? 96  TYR A O      1 
ATOM   1485  C  CB     . TYR A 1 97  ? 2.285   34.954  10.742  1.00 30.06  ? 96  TYR A CB     1 
ATOM   1486  C  CG     . TYR A 1 97  ? 2.552   33.476  10.551  1.00 29.77  ? 96  TYR A CG     1 
ATOM   1487  C  CD1    . TYR A 1 97  ? 3.019   32.703  11.593  1.00 32.40  ? 96  TYR A CD1    1 
ATOM   1488  C  CD2    . TYR A 1 97  ? 2.309   32.859  9.342   1.00 30.35  ? 96  TYR A CD2    1 
ATOM   1489  C  CE1    . TYR A 1 97  ? 3.269   31.353  11.418  1.00 31.33  ? 96  TYR A CE1    1 
ATOM   1490  C  CE2    . TYR A 1 97  ? 2.537   31.529  9.170   1.00 33.01  ? 96  TYR A CE2    1 
ATOM   1491  C  CZ     . TYR A 1 97  ? 3.000   30.784  10.207  1.00 30.84  ? 96  TYR A CZ     1 
ATOM   1492  O  OH     . TYR A 1 97  ? 3.207   29.451  10.029  1.00 38.19  ? 96  TYR A OH     1 
ATOM   1493  H  H      . TYR A 1 97  ? 0.081   35.221  9.694   1.00 42.02  ? 96  TYR A H      1 
ATOM   1494  H  HA     . TYR A 1 97  ? 0.819   34.503  12.095  1.00 39.07  ? 96  TYR A HA     1 
ATOM   1495  H  HB2    . TYR A 1 97  ? 2.259   35.370  9.866   1.00 36.10  ? 96  TYR A HB2    1 
ATOM   1496  H  HB3    . TYR A 1 97  ? 3.013   35.325  11.264  1.00 36.10  ? 96  TYR A HB3    1 
ATOM   1497  H  HD1    . TYR A 1 97  ? 3.168   33.093  12.424  1.00 38.91  ? 96  TYR A HD1    1 
ATOM   1498  H  HD2    . TYR A 1 97  ? 1.983   33.362  8.631   1.00 36.46  ? 96  TYR A HD2    1 
ATOM   1499  H  HE1    . TYR A 1 97  ? 3.615   30.842  12.113  1.00 37.63  ? 96  TYR A HE1    1 
ATOM   1500  H  HE2    . TYR A 1 97  ? 2.377   31.132  8.345   1.00 39.65  ? 96  TYR A HE2    1 
ATOM   1501  H  HH     . TYR A 1 97  ? 2.999   29.231  9.245   1.00 45.86  ? 96  TYR A HH     1 
ATOM   1502  N  N      . ARG A 1 98  ? 0.947   37.663  11.514  1.00 29.38  ? 97  ARG A N      1 
ATOM   1503  C  CA     . ARG A 1 98  ? 1.044   38.948  12.194  1.00 32.45  ? 97  ARG A CA     1 
ATOM   1504  C  C      . ARG A 1 98  ? -0.052  39.081  13.238  1.00 32.72  ? 97  ARG A C      1 
ATOM   1505  O  O      . ARG A 1 98  ? 0.205   39.464  14.383  1.00 36.47  ? 97  ARG A O      1 
ATOM   1506  C  CB     . ARG A 1 98  ? 0.938   40.097  11.196  1.00 39.75  ? 97  ARG A CB     1 
ATOM   1507  C  CG     . ARG A 1 98  ? 1.215   41.459  11.818  1.00 40.38  ? 97  ARG A CG     1 
ATOM   1508  C  CD     . ARG A 1 98  ? 1.216   42.575  10.785  1.00 39.76  ? 97  ARG A CD     1 
ATOM   1509  N  NE     . ARG A 1 98  ? 0.824   43.840  11.390  1.00 43.91  ? 97  ARG A NE     1 
ATOM   1510  C  CZ     . ARG A 1 98  ? 1.622   44.584  12.146  1.00 46.47  ? 97  ARG A CZ     1 
ATOM   1511  N  NH1    . ARG A 1 98  ? 2.879   44.233  12.381  1.00 45.17  ? 97  ARG A NH1    1 
ATOM   1512  N  NH2    . ARG A 1 98  ? 1.146   45.700  12.689  1.00 50.66  ? 97  ARG A NH2    1 
ATOM   1513  H  H      . ARG A 1 98  ? 0.831   37.706  10.663  1.00 35.29  ? 97  ARG A H      1 
ATOM   1514  H  HA     . ARG A 1 98  ? 1.911   39.000  12.625  1.00 38.97  ? 97  ARG A HA     1 
ATOM   1515  H  HB2    . ARG A 1 98  ? 1.584   39.956  10.486  1.00 47.74  ? 97  ARG A HB2    1 
ATOM   1516  H  HB3    . ARG A 1 98  ? 0.041   40.113  10.829  1.00 47.74  ? 97  ARG A HB3    1 
ATOM   1517  H  HG2    . ARG A 1 98  ? 0.527   41.655  12.473  1.00 48.49  ? 97  ARG A HG2    1 
ATOM   1518  H  HG3    . ARG A 1 98  ? 2.085   41.442  12.246  1.00 48.49  ? 97  ARG A HG3    1 
ATOM   1519  H  HD2    . ARG A 1 98  ? 2.108   42.673  10.416  1.00 47.75  ? 97  ARG A HD2    1 
ATOM   1520  H  HD3    . ARG A 1 98  ? 0.586   42.363  10.079  1.00 47.75  ? 97  ARG A HD3    1 
ATOM   1521  H  HE     . ARG A 1 98  ? 0.025   44.124  11.249  1.00 52.73  ? 97  ARG A HE     1 
ATOM   1522  H  HH11   . ARG A 1 98  ? 3.194   43.509  12.041  1.00 54.24  ? 97  ARG A HH11   1 
ATOM   1523  H  HH12   . ARG A 1 98  ? 3.379   44.730  12.874  1.00 54.24  ? 97  ARG A HH12   1 
ATOM   1524  H  HH21   . ARG A 1 98  ? 0.330   45.933  12.549  1.00 60.83  ? 97  ARG A HH21   1 
ATOM   1525  H  HH22   . ARG A 1 98  ? 1.655   46.190  13.181  1.00 60.83  ? 97  ARG A HH22   1 
ATOM   1526  N  N      . GLU A 1 99  ? -1.292  38.797  12.836  1.00 36.94  ? 98  GLU A N      1 
ATOM   1527  C  CA     . GLU A 1 99  ? -2.430  38.882  13.748  1.00 38.76  ? 98  GLU A CA     1 
ATOM   1528  C  C      . GLU A 1 99  ? -2.205  38.028  14.979  1.00 37.88  ? 98  GLU A C      1 
ATOM   1529  O  O      . GLU A 1 99  ? -2.496  38.448  16.103  1.00 33.54  ? 98  GLU A O      1 
ATOM   1530  C  CB     . GLU A 1 99  ? -3.697  38.428  13.029  1.00 36.21  ? 98  GLU A CB     1 
ATOM   1531  C  CG     . GLU A 1 99  ? -4.240  39.467  12.059  1.00 42.27  ? 98  GLU A CG     1 
ATOM   1532  C  CD     . GLU A 1 99  ? -4.389  40.855  12.701  1.00 45.75  ? 98  GLU A CD     1 
ATOM   1533  O  OE1    . GLU A 1 99  ? -5.109  40.987  13.722  1.00 47.73  ? 98  GLU A OE1    1 
ATOM   1534  O  OE2    . GLU A 1 99  ? -3.736  41.806  12.196  1.00 46.11  ? 98  GLU A OE2    1 
ATOM   1535  H  H      . GLU A 1 99  ? -1.501  38.551  12.039  1.00 44.36  ? 98  GLU A H      1 
ATOM   1536  H  HA     . GLU A 1 99  ? -2.541  39.804  14.028  1.00 46.54  ? 98  GLU A HA     1 
ATOM   1537  H  HB2    . GLU A 1 99  ? -3.501  37.622  12.525  1.00 43.49  ? 98  GLU A HB2    1 
ATOM   1538  H  HB3    . GLU A 1 99  ? -4.385  38.247  13.689  1.00 43.49  ? 98  GLU A HB3    1 
ATOM   1539  H  HG2    . GLU A 1 99  ? -3.632  39.547  11.308  1.00 50.76  ? 98  GLU A HG2    1 
ATOM   1540  H  HG3    . GLU A 1 99  ? -5.115  39.184  11.749  1.00 50.76  ? 98  GLU A HG3    1 
ATOM   1541  N  N      . GLN A 1 100 ? -1.708  36.811  14.780  1.00 32.66  ? 99  GLN A N      1 
ATOM   1542  C  CA     . GLN A 1 100 ? -1.455  35.933  15.906  1.00 37.10  ? 99  GLN A CA     1 
ATOM   1543  C  C      . GLN A 1 100 ? -0.395  36.529  16.819  1.00 36.07  ? 99  GLN A C      1 
ATOM   1544  O  O      . GLN A 1 100 ? -0.569  36.569  18.034  1.00 36.05  ? 99  GLN A O      1 
ATOM   1545  C  CB     . GLN A 1 100 ? -1.050  34.560  15.391  1.00 33.38  ? 99  GLN A CB     1 
ATOM   1546  C  CG     . GLN A 1 100 ? -0.950  33.492  16.433  1.00 36.48  ? 99  GLN A CG     1 
ATOM   1547  C  CD     . GLN A 1 100 ? -0.849  32.128  15.798  1.00 40.87  ? 99  GLN A CD     1 
ATOM   1548  O  OE1    . GLN A 1 100 ? -0.357  31.994  14.669  1.00 38.00  ? 99  GLN A OE1    1 
ATOM   1549  N  NE2    . GLN A 1 100 ? -1.294  31.102  16.517  1.00 41.39  ? 99  GLN A NE2    1 
ATOM   1550  H  H      . GLN A 1 100 ? -1.514  36.477  14.012  1.00 39.23  ? 99  GLN A H      1 
ATOM   1551  H  HA     . GLN A 1 100 ? -2.263  35.823  16.431  1.00 44.55  ? 99  GLN A HA     1 
ATOM   1552  H  HB2    . GLN A 1 100 ? -1.709  34.270  14.741  1.00 40.09  ? 99  GLN A HB2    1 
ATOM   1553  H  HB3    . GLN A 1 100 ? -0.179  34.635  14.969  1.00 40.09  ? 99  GLN A HB3    1 
ATOM   1554  H  HG2    . GLN A 1 100 ? -0.158  33.640  16.973  1.00 43.81  ? 99  GLN A HG2    1 
ATOM   1555  H  HG3    . GLN A 1 100 ? -1.742  33.512  16.993  1.00 43.81  ? 99  GLN A HG3    1 
ATOM   1556  H  HE21   . GLN A 1 100 ? -1.619  31.237  17.302  1.00 49.71  ? 99  GLN A HE21   1 
ATOM   1557  H  HE22   . GLN A 1 100 ? -1.257  30.305  16.197  1.00 49.71  ? 99  GLN A HE22   1 
ATOM   1558  N  N      . ILE A 1 101 ? 0.714   37.018  16.252  1.00 32.54  ? 100 ILE A N      1 
ATOM   1559  C  CA     . ILE A 1 101 ? 1.739   37.611  17.099  1.00 30.82  ? 100 ILE A CA     1 
ATOM   1560  C  C      . ILE A 1 101 ? 1.177   38.771  17.918  1.00 37.04  ? 100 ILE A C      1 
ATOM   1561  O  O      . ILE A 1 101 ? 1.502   38.927  19.106  1.00 33.29  ? 100 ILE A O      1 
ATOM   1562  C  CB     . ILE A 1 101 ? 2.945   38.064  16.255  1.00 30.38  ? 100 ILE A CB     1 
ATOM   1563  C  CG1    . ILE A 1 101 ? 3.653   36.861  15.670  1.00 30.46  ? 100 ILE A CG1    1 
ATOM   1564  C  CG2    . ILE A 1 101 ? 3.860   38.834  17.139  1.00 32.84  ? 100 ILE A CG2    1 
ATOM   1565  C  CD1    . ILE A 1 101 ? 4.308   37.181  14.327  1.00 27.55  ? 100 ILE A CD1    1 
ATOM   1566  H  H      . ILE A 1 101 ? 0.887   37.017  15.410  1.00 39.08  ? 100 ILE A H      1 
ATOM   1567  H  HA     . ILE A 1 101 ? 2.038   36.927  17.718  1.00 37.02  ? 100 ILE A HA     1 
ATOM   1568  H  HB     . ILE A 1 101 ? 2.649   38.621  15.517  1.00 36.49  ? 100 ILE A HB     1 
ATOM   1569  H  HG12   . ILE A 1 101 ? 4.346   36.570  16.284  1.00 36.59  ? 100 ILE A HG12   1 
ATOM   1570  H  HG13   . ILE A 1 101 ? 3.010   36.148  15.533  1.00 36.59  ? 100 ILE A HG13   1 
ATOM   1571  H  HG21   . ILE A 1 101 ? 4.749   38.833  16.751  1.00 39.44  ? 100 ILE A HG21   1 
ATOM   1572  H  HG22   . ILE A 1 101 ? 3.533   39.744  17.216  1.00 39.44  ? 100 ILE A HG22   1 
ATOM   1573  H  HG23   . ILE A 1 101 ? 3.880   38.415  18.013  1.00 39.44  ? 100 ILE A HG23   1 
ATOM   1574  H  HD11   . ILE A 1 101 ? 4.748   36.384  13.992  1.00 33.09  ? 100 ILE A HD11   1 
ATOM   1575  H  HD12   . ILE A 1 101 ? 3.623   37.467  13.702  1.00 33.09  ? 100 ILE A HD12   1 
ATOM   1576  H  HD13   . ILE A 1 101 ? 4.958   37.889  14.453  1.00 33.09  ? 100 ILE A HD13   1 
ATOM   1577  N  N      . LYS A 1 102 ? 0.388   39.643  17.288  1.00 37.92  ? 101 LYS A N      1 
ATOM   1578  C  CA     . LYS A 1 102 ? -0.193  40.770  18.021  1.00 36.80  ? 101 LYS A CA     1 
ATOM   1579  C  C      . LYS A 1 102 ? -1.131  40.265  19.112  1.00 37.64  ? 101 LYS A C      1 
ATOM   1580  O  O      . LYS A 1 102 ? -1.115  40.746  20.255  1.00 38.41  ? 101 LYS A O      1 
ATOM   1581  C  CB     . LYS A 1 102 ? -0.970  41.688  17.072  1.00 37.67  ? 101 LYS A CB     1 
ATOM   1582  C  CG     . LYS A 1 102 ? -0.152  42.601  16.196  1.00 40.92  ? 101 LYS A CG     1 
ATOM   1583  C  CD     . LYS A 1 102 ? -1.036  43.628  15.446  1.00 42.88  ? 101 LYS A CD     1 
ATOM   1584  C  CE     . LYS A 1 102 ? -2.144  42.962  14.639  1.00 43.83  ? 101 LYS A CE     1 
ATOM   1585  N  NZ     . LYS A 1 102 ? -2.898  43.939  13.773  1.00 48.34  ? 101 LYS A NZ     1 
ATOM   1586  H  H      . LYS A 1 102 ? 0.177   39.607  16.455  1.00 45.54  ? 101 LYS A H      1 
ATOM   1587  H  HA     . LYS A 1 102 ? 0.530   41.280  18.419  1.00 44.19  ? 101 LYS A HA     1 
ATOM   1588  H  HB2    . LYS A 1 102 ? -1.502  41.130  16.483  1.00 45.24  ? 101 LYS A HB2    1 
ATOM   1589  H  HB3    . LYS A 1 102 ? -1.550  42.252  17.607  1.00 45.24  ? 101 LYS A HB3    1 
ATOM   1590  H  HG2    . LYS A 1 102 ? 0.480   43.090  16.746  1.00 49.14  ? 101 LYS A HG2    1 
ATOM   1591  H  HG3    . LYS A 1 102 ? 0.322   42.071  15.536  1.00 49.14  ? 101 LYS A HG3    1 
ATOM   1592  H  HD2    . LYS A 1 102 ? -1.449  44.223  16.092  1.00 51.49  ? 101 LYS A HD2    1 
ATOM   1593  H  HD3    . LYS A 1 102 ? -0.482  44.137  14.834  1.00 51.49  ? 101 LYS A HD3    1 
ATOM   1594  H  HE2    . LYS A 1 102 ? -1.753  42.287  14.062  1.00 52.63  ? 101 LYS A HE2    1 
ATOM   1595  H  HE3    . LYS A 1 102 ? -2.776  42.551  15.249  1.00 52.63  ? 101 LYS A HE3    1 
ATOM   1596  H  HZ1    . LYS A 1 102 ? -3.274  44.567  14.279  1.00 58.04  ? 101 LYS A HZ1    1 
ATOM   1597  H  HZ2    . LYS A 1 102 ? -2.341  44.327  13.197  1.00 58.04  ? 101 LYS A HZ2    1 
ATOM   1598  H  HZ3    . LYS A 1 102 ? -3.534  43.514  13.318  1.00 58.04  ? 101 LYS A HZ3    1 
ATOM   1599  N  N      . ARG A 1 103 ? -1.996  39.326  18.749  1.00 35.70  ? 102 ARG A N      1 
ATOM   1600  C  CA     . ARG A 1 103 ? -2.952  38.764  19.704  1.00 39.59  ? 102 ARG A CA     1 
ATOM   1601  C  C      . ARG A 1 103 ? -2.216  38.151  20.892  1.00 38.81  ? 102 ARG A C      1 
ATOM   1602  O  O      . ARG A 1 103 ? -2.472  38.512  22.050  1.00 39.62  ? 102 ARG A O      1 
ATOM   1603  C  CB     . ARG A 1 103 ? -3.819  37.757  18.955  1.00 41.34  ? 102 ARG A CB     1 
ATOM   1604  C  CG     . ARG A 1 103 ? -4.937  37.111  19.698  1.00 45.59  ? 102 ARG A CG     1 
ATOM   1605  C  CD     . ARG A 1 103 ? -6.044  36.699  18.720  1.00 50.12  ? 102 ARG A CD     1 
ATOM   1606  N  NE     . ARG A 1 103 ? -5.528  35.951  17.573  1.00 50.81  ? 102 ARG A NE     1 
ATOM   1607  C  CZ     . ARG A 1 103 ? -4.995  34.739  17.641  1.00 52.28  ? 102 ARG A CZ     1 
ATOM   1608  N  NH1    . ARG A 1 103 ? -4.905  34.088  18.793  1.00 51.24  ? 102 ARG A NH1    1 
ATOM   1609  N  NH2    . ARG A 1 103 ? -4.545  34.160  16.524  1.00 51.13  ? 102 ARG A NH2    1 
ATOM   1610  H  H      . ARG A 1 103 ? -2.054  38.995  17.957  1.00 42.87  ? 102 ARG A H      1 
ATOM   1611  H  HA     . ARG A 1 103 ? -3.536  39.446  20.070  1.00 47.54  ? 102 ARG A HA     1 
ATOM   1612  H  HB2    . ARG A 1 103 ? -4.217  38.215  18.197  1.00 49.64  ? 102 ARG A HB2    1 
ATOM   1613  H  HB3    . ARG A 1 103 ? -3.242  37.043  18.644  1.00 49.64  ? 102 ARG A HB3    1 
ATOM   1614  H  HG2    . ARG A 1 103 ? -4.612  36.319  20.153  1.00 54.75  ? 102 ARG A HG2    1 
ATOM   1615  H  HG3    . ARG A 1 103 ? -5.307  37.736  20.341  1.00 54.75  ? 102 ARG A HG3    1 
ATOM   1616  H  HD2    . ARG A 1 103 ? -6.683  36.135  19.183  1.00 60.18  ? 102 ARG A HD2    1 
ATOM   1617  H  HD3    . ARG A 1 103 ? -6.485  37.495  18.385  1.00 60.18  ? 102 ARG A HD3    1 
ATOM   1618  H  HE     . ARG A 1 103 ? -5.574  36.324  16.799  1.00 61.01  ? 102 ARG A HE     1 
ATOM   1619  H  HH11   . ARG A 1 103 ? -5.195  34.452  19.517  1.00 61.52  ? 102 ARG A HH11   1 
ATOM   1620  H  HH12   . ARG A 1 103 ? -4.556  33.303  18.817  1.00 61.52  ? 102 ARG A HH12   1 
ATOM   1621  H  HH21   . ARG A 1 103 ? -4.603  34.573  15.772  1.00 61.39  ? 102 ARG A HH21   1 
ATOM   1622  H  HH22   . ARG A 1 103 ? -4.197  33.374  16.557  1.00 61.39  ? 102 ARG A HH22   1 
ATOM   1623  N  N      . VAL A 1 104 ? -1.216  37.300  20.616  1.00 40.46  ? 103 VAL A N      1 
ATOM   1624  C  CA     . VAL A 1 104 ? -0.508  36.626  21.698  1.00 39.18  ? 103 VAL A CA     1 
ATOM   1625  C  C      . VAL A 1 104 ? 0.278   37.623  22.539  1.00 38.99  ? 103 VAL A C      1 
ATOM   1626  O  O      . VAL A 1 104 ? 0.346   37.503  23.771  1.00 41.60  ? 103 VAL A O      1 
ATOM   1627  C  CB     . VAL A 1 104 ? 0.401   35.516  21.155  1.00 38.59  ? 103 VAL A CB     1 
ATOM   1628  C  CG1    . VAL A 1 104 ? 1.245   34.963  22.282  1.00 40.35  ? 103 VAL A CG1    1 
ATOM   1629  C  CG2    . VAL A 1 104 ? -0.419  34.417  20.485  1.00 42.18  ? 103 VAL A CG2    1 
ATOM   1630  H  H      . VAL A 1 104 ? -0.938  37.104  19.827  1.00 48.58  ? 103 VAL A H      1 
ATOM   1631  H  HA     . VAL A 1 104 ? -1.174  36.212  22.268  1.00 47.04  ? 103 VAL A HA     1 
ATOM   1632  H  HB     . VAL A 1 104 ? 0.990   35.882  20.477  1.00 46.34  ? 103 VAL A HB     1 
ATOM   1633  H  HG11   . VAL A 1 104 ? 1.574   34.086  22.028  1.00 48.46  ? 103 VAL A HG11   1 
ATOM   1634  H  HG12   . VAL A 1 104 ? 1.991   35.562  22.441  1.00 48.46  ? 103 VAL A HG12   1 
ATOM   1635  H  HG13   . VAL A 1 104 ? 0.700   34.893  23.081  1.00 48.46  ? 103 VAL A HG13   1 
ATOM   1636  H  HG21   . VAL A 1 104 ? 0.184   33.741  20.137  1.00 50.65  ? 103 VAL A HG21   1 
ATOM   1637  H  HG22   . VAL A 1 104 ? -1.014  34.022  21.141  1.00 50.65  ? 103 VAL A HG22   1 
ATOM   1638  H  HG23   . VAL A 1 104 ? -0.935  34.805  19.761  1.00 50.65  ? 103 VAL A HG23   1 
ATOM   1639  N  N      . LYS A 1 105 ? 0.879   38.625  21.901  1.00 37.07  ? 104 LYS A N      1 
ATOM   1640  C  CA     . LYS A 1 105 ? 1.609   39.659  22.609  1.00 37.31  ? 104 LYS A CA     1 
ATOM   1641  C  C      . LYS A 1 105 ? 0.699   40.726  23.196  1.00 42.10  ? 104 LYS A C      1 
ATOM   1642  O  O      . LYS A 1 105 ? 1.172   41.568  23.967  1.00 41.62  ? 104 LYS A O      1 
ATOM   1643  C  CB     . LYS A 1 105 ? 2.607   40.300  21.645  1.00 41.91  ? 104 LYS A CB     1 
ATOM   1644  C  CG     . LYS A 1 105 ? 3.768   39.398  21.301  1.00 40.78  ? 104 LYS A CG     1 
ATOM   1645  C  CD     . LYS A 1 105 ? 4.993   39.943  21.970  1.00 43.84  ? 104 LYS A CD     1 
ATOM   1646  C  CE     . LYS A 1 105 ? 6.108   38.983  21.846  1.00 33.31  ? 104 LYS A CE     1 
ATOM   1647  N  NZ     . LYS A 1 105 ? 6.964   39.017  23.040  1.00 32.15  ? 104 LYS A NZ     1 
ATOM   1648  H  H      . LYS A 1 105 ? 0.875   38.725  21.047  1.00 44.51  ? 104 LYS A H      1 
ATOM   1649  H  HA     . LYS A 1 105 ? 2.100   39.265  23.348  1.00 44.80  ? 104 LYS A HA     1 
ATOM   1650  H  HB2    . LYS A 1 105 ? 2.148   40.522  20.820  1.00 50.33  ? 104 LYS A HB2    1 
ATOM   1651  H  HB3    . LYS A 1 105 ? 2.965   41.104  22.052  1.00 50.33  ? 104 LYS A HB3    1 
ATOM   1652  H  HG2    . LYS A 1 105 ? 3.600   38.499  21.625  1.00 48.97  ? 104 LYS A HG2    1 
ATOM   1653  H  HG3    . LYS A 1 105 ? 3.907   39.384  20.341  1.00 48.97  ? 104 LYS A HG3    1 
ATOM   1654  H  HD2    . LYS A 1 105 ? 5.252   40.776  21.547  1.00 52.65  ? 104 LYS A HD2    1 
ATOM   1655  H  HD3    . LYS A 1 105 ? 4.813   40.090  22.911  1.00 52.65  ? 104 LYS A HD3    1 
ATOM   1656  H  HE2    . LYS A 1 105 ? 5.753   38.086  21.747  1.00 40.01  ? 104 LYS A HE2    1 
ATOM   1657  H  HE3    . LYS A 1 105 ? 6.649   39.213  21.074  1.00 40.01  ? 104 LYS A HE3    1 
ATOM   1658  H  HZ1    . LYS A 1 105 ? 6.601   38.527  23.688  1.00 38.61  ? 104 LYS A HZ1    1 
ATOM   1659  H  HZ2    . LYS A 1 105 ? 7.769   38.690  22.847  1.00 38.61  ? 104 LYS A HZ2    1 
ATOM   1660  H  HZ3    . LYS A 1 105 ? 7.053   39.855  23.327  1.00 38.61  ? 104 LYS A HZ3    1 
ATOM   1661  N  N      . ASP A 1 106 ? -0.585  40.689  22.874  1.00 41.91  ? 105 ASP A N      1 
ATOM   1662  C  CA     . ASP A 1 106 ? -1.524  41.781  23.169  1.00 40.78  ? 105 ASP A CA     1 
ATOM   1663  C  C      . ASP A 1 106 ? -0.909  43.166  22.957  1.00 41.18  ? 105 ASP A C      1 
ATOM   1664  O  O      . ASP A 1 106 ? -0.943  44.030  23.835  1.00 41.37  ? 105 ASP A O      1 
ATOM   1665  C  CB     . ASP A 1 106 ? -2.059  41.670  24.589  1.00 42.94  ? 105 ASP A CB     1 
ATOM   1666  C  CG     . ASP A 1 106 ? -3.346  42.421  24.763  1.00 48.45  ? 105 ASP A CG     1 
ATOM   1667  O  OD1    . ASP A 1 106 ? -4.217  42.241  23.887  1.00 46.95  ? 105 ASP A OD1    1 
ATOM   1668  O  OD2    . ASP A 1 106 ? -3.464  43.195  25.737  1.00 49.21  ? 105 ASP A OD2    1 
ATOM   1669  H  H      . ASP A 1 106 ? -0.955  40.025  22.471  1.00 50.32  ? 105 ASP A H      1 
ATOM   1670  H  HA     . ASP A 1 106 ? -2.255  41.691  22.539  1.00 48.97  ? 105 ASP A HA     1 
ATOM   1671  H  HB2    . ASP A 1 106 ? -2.221  40.737  24.797  1.00 51.56  ? 105 ASP A HB2    1 
ATOM   1672  H  HB3    . ASP A 1 106 ? -1.407  42.039  25.206  1.00 51.56  ? 105 ASP A HB3    1 
ATOM   1673  N  N      . SER A 1 107 ? -0.363  43.387  21.747  1.00 40.99  ? 106 SER A N      1 
ATOM   1674  C  CA     . SER A 1 107 ? 0.236   44.665  21.392  1.00 38.60  ? 106 SER A CA     1 
ATOM   1675  C  C      . SER A 1 107 ? 0.165   44.907  19.888  1.00 44.56  ? 106 SER A C      1 
ATOM   1676  O  O      . SER A 1 107 ? 0.312   43.981  19.074  1.00 39.08  ? 106 SER A O      1 
ATOM   1677  C  CB     . SER A 1 107 ? 1.709   44.762  21.817  1.00 40.00  ? 106 SER A CB     1 
ATOM   1678  O  OG     . SER A 1 107 ? 2.212   46.072  21.647  1.00 39.46  ? 106 SER A OG     1 
ATOM   1679  H  H      . SER A 1 107 ? -0.333  42.802  21.117  1.00 49.22  ? 106 SER A H      1 
ATOM   1680  H  HA     . SER A 1 107 ? -0.282  45.350  21.844  1.00 46.36  ? 106 SER A HA     1 
ATOM   1681  H  HB2    . SER A 1 107 ? 1.782   44.518  22.753  1.00 48.03  ? 106 SER A HB2    1 
ATOM   1682  H  HB3    . SER A 1 107 ? 2.233   44.153  21.274  1.00 48.03  ? 106 SER A HB3    1 
ATOM   1683  H  HG     . SER A 1 107 ? 3.025   46.098  21.855  1.00 47.39  ? 106 SER A HG     1 
ATOM   1684  N  N      . GLU A 1 108 ? -0.015  46.171  19.535  1.00 38.14  ? 107 GLU A N      1 
ATOM   1685  C  CA     . GLU A 1 108 ? 0.011   46.615  18.155  1.00 42.75  ? 107 GLU A CA     1 
ATOM   1686  C  C      . GLU A 1 108 ? 1.417   47.002  17.726  1.00 44.45  ? 107 GLU A C      1 
ATOM   1687  O  O      . GLU A 1 108 ? 1.645   47.262  16.538  1.00 46.85  ? 107 GLU A O      1 
ATOM   1688  C  CB     . GLU A 1 108 ? -0.975  47.788  17.998  1.00 47.59  ? 107 GLU A CB     1 
ATOM   1689  C  CG     . GLU A 1 108 ? -1.739  47.749  16.694  1.00 52.04  ? 107 GLU A CG     1 
ATOM   1690  C  CD     . GLU A 1 108 ? -2.870  46.745  16.734  1.00 51.47  ? 107 GLU A CD     1 
ATOM   1691  O  OE1    . GLU A 1 108 ? -3.247  46.330  17.844  1.00 56.91  ? 107 GLU A OE1    1 
ATOM   1692  O  OE2    . GLU A 1 108 ? -3.365  46.334  15.668  1.00 52.51  ? 107 GLU A OE2    1 
ATOM   1693  H  H      . GLU A 1 108 ? -0.158  46.808  20.094  1.00 45.80  ? 107 GLU A H      1 
ATOM   1694  H  HA     . GLU A 1 108 ? -0.286  45.917  17.549  1.00 51.33  ? 107 GLU A HA     1 
ATOM   1695  H  HB2    . GLU A 1 108 ? -1.619  47.756  18.723  1.00 57.14  ? 107 GLU A HB2    1 
ATOM   1696  H  HB3    . GLU A 1 108 ? -0.480  48.621  18.029  1.00 57.14  ? 107 GLU A HB3    1 
ATOM   1697  H  HG2    . GLU A 1 108 ? -2.117  48.625  16.519  1.00 62.48  ? 107 GLU A HG2    1 
ATOM   1698  H  HG3    . GLU A 1 108 ? -1.136  47.498  15.977  1.00 62.48  ? 107 GLU A HG3    1 
ATOM   1699  N  N      . ASP A 1 109 ? 2.372   46.988  18.658  1.00 38.54  ? 108 ASP A N      1 
ATOM   1700  C  CA     . ASP A 1 109 ? 3.712   47.516  18.447  1.00 42.14  ? 108 ASP A CA     1 
ATOM   1701  C  C      . ASP A 1 109 ? 4.729   46.420  18.789  1.00 41.22  ? 108 ASP A C      1 
ATOM   1702  O  O      . ASP A 1 109 ? 5.356   46.442  19.852  1.00 41.07  ? 108 ASP A O      1 
ATOM   1703  C  CB     . ASP A 1 109 ? 3.920   48.759  19.279  1.00 45.89  ? 108 ASP A CB     1 
ATOM   1704  C  CG     . ASP A 1 109 ? 5.189   49.472  18.928  1.00 54.73  ? 108 ASP A CG     1 
ATOM   1705  O  OD1    . ASP A 1 109 ? 5.324   49.873  17.752  1.00 57.22  ? 108 ASP A OD1    1 
ATOM   1706  O  OD2    . ASP A 1 109 ? 6.050   49.630  19.822  1.00 60.11  ? 108 ASP A OD2    1 
ATOM   1707  H  H      . ASP A 1 109 ? 2.258   46.665  19.447  1.00 46.28  ? 108 ASP A H      1 
ATOM   1708  H  HA     . ASP A 1 109 ? 3.823   47.737  17.509  1.00 50.60  ? 108 ASP A HA     1 
ATOM   1709  H  HB2    . ASP A 1 109 ? 3.180   49.369  19.129  1.00 55.10  ? 108 ASP A HB2    1 
ATOM   1710  H  HB3    . ASP A 1 109 ? 3.961   48.512  20.216  1.00 55.10  ? 108 ASP A HB3    1 
ATOM   1711  N  N      . VAL A 1 110 ? 4.906   45.486  17.867  1.00 40.18  ? 109 VAL A N      1 
ATOM   1712  C  CA     . VAL A 1 110 ? 5.790   44.339  18.049  1.00 33.96  ? 109 VAL A CA     1 
ATOM   1713  C  C      . VAL A 1 110 ? 6.898   44.413  17.002  1.00 32.03  ? 109 VAL A C      1 
ATOM   1714  O  O      . VAL A 1 110 ? 6.601   44.555  15.822  1.00 35.24  ? 109 VAL A O      1 
ATOM   1715  C  CB     . VAL A 1 110 ? 5.039   43.007  17.926  1.00 31.03  ? 109 VAL A CB     1 
ATOM   1716  C  CG1    . VAL A 1 110 ? 5.992   41.828  18.173  1.00 31.58  ? 109 VAL A CG1    1 
ATOM   1717  C  CG2    . VAL A 1 110 ? 3.889   42.996  18.877  1.00 36.50  ? 109 VAL A CG2    1 
ATOM   1718  H  H      . VAL A 1 110 ? 4.513   45.493  17.102  1.00 48.25  ? 109 VAL A H      1 
ATOM   1719  H  HA     . VAL A 1 110 ? 6.202   44.390  18.925  1.00 40.79  ? 109 VAL A HA     1 
ATOM   1720  H  HB     . VAL A 1 110 ? 4.688   42.905  17.027  1.00 37.27  ? 109 VAL A HB     1 
ATOM   1721  H  HG11   . VAL A 1 110 ? 5.470   41.017  18.278  1.00 37.93  ? 109 VAL A HG11   1 
ATOM   1722  H  HG12   . VAL A 1 110 ? 6.589   41.741  17.414  1.00 37.93  ? 109 VAL A HG12   1 
ATOM   1723  H  HG13   . VAL A 1 110 ? 6.503   42.000  18.979  1.00 37.93  ? 109 VAL A HG13   1 
ATOM   1724  H  HG21   . VAL A 1 110 ? 3.481   42.116  18.870  1.00 43.84  ? 109 VAL A HG21   1 
ATOM   1725  H  HG22   . VAL A 1 110 ? 4.214   43.203  19.768  1.00 43.84  ? 109 VAL A HG22   1 
ATOM   1726  H  HG23   . VAL A 1 110 ? 3.242   43.663  18.598  1.00 43.84  ? 109 VAL A HG23   1 
ATOM   1727  N  N      . PRO A 1 111 ? 8.159   44.274  17.380  1.00 29.44  ? 110 PRO A N      1 
ATOM   1728  C  CA     . PRO A 1 111 ? 9.230   44.325  16.371  1.00 30.45  ? 110 PRO A CA     1 
ATOM   1729  C  C      . PRO A 1 111 ? 9.073   43.207  15.348  1.00 33.40  ? 110 PRO A C      1 
ATOM   1730  O  O      . PRO A 1 111 ? 9.004   42.032  15.704  1.00 27.58  ? 110 PRO A O      1 
ATOM   1731  C  CB     . PRO A 1 111 ? 10.502  44.164  17.212  1.00 30.39  ? 110 PRO A CB     1 
ATOM   1732  C  CG     . PRO A 1 111 ? 10.117  44.706  18.546  1.00 31.70  ? 110 PRO A CG     1 
ATOM   1733  C  CD     . PRO A 1 111 ? 8.709   44.272  18.748  1.00 32.48  ? 110 PRO A CD     1 
ATOM   1734  H  HA     . PRO A 1 111 ? 9.241   45.181  15.915  1.00 36.57  ? 110 PRO A HA     1 
ATOM   1735  H  HB2    . PRO A 1 111 ? 10.749  43.228  17.271  1.00 36.51  ? 110 PRO A HB2    1 
ATOM   1736  H  HB3    . PRO A 1 111 ? 11.228  44.675  16.822  1.00 36.51  ? 110 PRO A HB3    1 
ATOM   1737  H  HG2    . PRO A 1 111 ? 10.696  44.338  19.231  1.00 38.08  ? 110 PRO A HG2    1 
ATOM   1738  H  HG3    . PRO A 1 111 ? 10.184  45.674  18.541  1.00 38.08  ? 110 PRO A HG3    1 
ATOM   1739  H  HD2    . PRO A 1 111 ? 8.674   43.382  19.134  1.00 39.01  ? 110 PRO A HD2    1 
ATOM   1740  H  HD3    . PRO A 1 111 ? 8.232   44.898  19.314  1.00 39.01  ? 110 PRO A HD3    1 
ATOM   1741  N  N      . MET A 1 112 ? 8.981   43.587  14.068  1.00 29.50  ? 111 MET A N      1 
ATOM   1742  C  CA     . MET A 1 112 ? 8.849   42.600  13.013  1.00 30.52  ? 111 MET A CA     1 
ATOM   1743  C  C      . MET A 1 112 ? 9.441   43.139  11.718  1.00 31.25  ? 111 MET A C      1 
ATOM   1744  O  O      . MET A 1 112 ? 9.454   44.352  11.482  1.00 31.38  ? 111 MET A O      1 
ATOM   1745  C  CB     . MET A 1 112 ? 7.407   42.181  12.662  1.00 27.47  ? 111 MET A CB     1 
ATOM   1746  C  CG     . MET A 1 112 ? 6.482   41.827  13.771  1.00 34.59  ? 111 MET A CG     1 
ATOM   1747  S  SD     . MET A 1 112 ? 4.868   41.442  13.022  1.00 39.26  ? 111 MET A SD     1 
ATOM   1748  C  CE     . MET A 1 112 ? 3.786   41.433  14.465  1.00 39.52  ? 111 MET A CE     1 
ATOM   1749  H  H      . MET A 1 112 ? 8.994   44.403  13.797  1.00 35.44  ? 111 MET A H      1 
ATOM   1750  H  HA     . MET A 1 112 ? 9.323   41.826  13.356  1.00 36.66  ? 111 MET A HA     1 
ATOM   1751  H  HB2    . MET A 1 112 ? 6.995   42.918  12.184  1.00 32.99  ? 111 MET A HB2    1 
ATOM   1752  H  HB3    . MET A 1 112 ? 7.460   41.401  12.087  1.00 32.99  ? 111 MET A HB3    1 
ATOM   1753  H  HG2    . MET A 1 112 ? 6.811   41.050  14.249  1.00 41.54  ? 111 MET A HG2    1 
ATOM   1754  H  HG3    . MET A 1 112 ? 6.386   42.575  14.381  1.00 41.54  ? 111 MET A HG3    1 
ATOM   1755  H  HE1    . MET A 1 112 ? 2.883   41.218  14.182  1.00 47.46  ? 111 MET A HE1    1 
ATOM   1756  H  HE2    . MET A 1 112 ? 4.103   40.766  15.093  1.00 47.46  ? 111 MET A HE2    1 
ATOM   1757  H  HE3    . MET A 1 112 ? 3.803   42.311  14.877  1.00 47.46  ? 111 MET A HE3    1 
ATOM   1758  N  N      . VAL A 1 113 ? 9.889   42.213  10.867  1.00 27.17  ? 112 VAL A N      1 
ATOM   1759  C  CA     . VAL A 1 113 ? 10.380  42.519  9.531   1.00 26.05  ? 112 VAL A CA     1 
ATOM   1760  C  C      . VAL A 1 113 ? 9.684   41.563  8.561   1.00 27.29  ? 112 VAL A C      1 
ATOM   1761  O  O      . VAL A 1 113 ? 9.535   40.364  8.851   1.00 24.00  ? 112 VAL A O      1 
ATOM   1762  C  CB     . VAL A 1 113 ? 11.912  42.393  9.459   1.00 27.69  ? 112 VAL A CB     1 
ATOM   1763  C  CG1    . VAL A 1 113 ? 12.407  42.489  8.011   1.00 25.49  ? 112 VAL A CG1    1 
ATOM   1764  C  CG2    . VAL A 1 113 ? 12.557  43.455  10.354  1.00 28.67  ? 112 VAL A CG2    1 
ATOM   1765  H  H      . VAL A 1 113 ? 9.918   41.373  11.051  1.00 32.64  ? 112 VAL A H      1 
ATOM   1766  H  HA     . VAL A 1 113 ? 10.147  43.426  9.276   1.00 31.29  ? 112 VAL A HA     1 
ATOM   1767  H  HB     . VAL A 1 113 ? 12.182  41.520  9.786   1.00 33.27  ? 112 VAL A HB     1 
ATOM   1768  H  HG11   . VAL A 1 113 ? 13.370  42.606  8.013   1.00 30.63  ? 112 VAL A HG11   1 
ATOM   1769  H  HG12   . VAL A 1 113 ? 12.174  41.672  7.543   1.00 30.63  ? 112 VAL A HG12   1 
ATOM   1770  H  HG13   . VAL A 1 113 ? 11.983  43.249  7.582   1.00 30.63  ? 112 VAL A HG13   1 
ATOM   1771  H  HG21   . VAL A 1 113 ? 13.521  43.361  10.311  1.00 34.43  ? 112 VAL A HG21   1 
ATOM   1772  H  HG22   . VAL A 1 113 ? 12.296  44.335  10.038  1.00 34.43  ? 112 VAL A HG22   1 
ATOM   1773  H  HG23   . VAL A 1 113 ? 12.252  43.327  11.266  1.00 34.43  ? 112 VAL A HG23   1 
ATOM   1774  N  N      . LEU A 1 114 ? 9.182   42.105  7.458   1.00 26.09  ? 113 LEU A N      1 
ATOM   1775  C  CA     . LEU A 1 114 ? 8.576   41.300  6.406   1.00 23.95  ? 113 LEU A CA     1 
ATOM   1776  C  C      . LEU A 1 114 ? 9.668   40.871  5.434   1.00 24.55  ? 113 LEU A C      1 
ATOM   1777  O  O      . LEU A 1 114 ? 10.425  41.712  4.952   1.00 25.32  ? 113 LEU A O      1 
ATOM   1778  C  CB     . LEU A 1 114 ? 7.514   42.097  5.670   1.00 27.98  ? 113 LEU A CB     1 
ATOM   1779  C  CG     . LEU A 1 114 ? 6.774   41.290  4.598   1.00 28.20  ? 113 LEU A CG     1 
ATOM   1780  C  CD1    . LEU A 1 114 ? 5.913   40.191  5.196   1.00 26.23  ? 113 LEU A CD1    1 
ATOM   1781  C  CD2    . LEU A 1 114 ? 5.900   42.263  3.764   1.00 31.71  ? 113 LEU A CD2    1 
ATOM   1782  H  H      . LEU A 1 114 ? 9.180   42.950  7.293   1.00 31.35  ? 113 LEU A H      1 
ATOM   1783  H  HA     . LEU A 1 114 ? 8.155   40.514  6.788   1.00 28.77  ? 113 LEU A HA     1 
ATOM   1784  H  HB2    . LEU A 1 114 ? 6.858   42.410  6.312   1.00 33.61  ? 113 LEU A HB2    1 
ATOM   1785  H  HB3    . LEU A 1 114 ? 7.938   42.853  5.234   1.00 33.61  ? 113 LEU A HB3    1 
ATOM   1786  H  HG     . LEU A 1 114 ? 7.424   40.849  4.028   1.00 33.88  ? 113 LEU A HG     1 
ATOM   1787  H  HD11   . LEU A 1 114 ? 5.414   39.759  4.485   1.00 31.51  ? 113 LEU A HD11   1 
ATOM   1788  H  HD12   . LEU A 1 114 ? 6.487   39.545  5.637   1.00 31.51  ? 113 LEU A HD12   1 
ATOM   1789  H  HD13   . LEU A 1 114 ? 5.302   40.584  5.839   1.00 31.51  ? 113 LEU A HD13   1 
ATOM   1790  H  HD21   . LEU A 1 114 ? 5.415   41.756  3.093   1.00 38.08  ? 113 LEU A HD21   1 
ATOM   1791  H  HD22   . LEU A 1 114 ? 5.275   42.711  4.355   1.00 38.08  ? 113 LEU A HD22   1 
ATOM   1792  H  HD23   . LEU A 1 114 ? 6.475   42.915  3.335   1.00 38.08  ? 113 LEU A HD23   1 
ATOM   1793  N  N      . VAL A 1 115 ? 9.773   39.572  5.178   1.00 21.07  ? 114 VAL A N      1 
ATOM   1794  C  CA     . VAL A 1 115 ? 10.837  39.031  4.328   1.00 22.97  ? 114 VAL A CA     1 
ATOM   1795  C  C      . VAL A 1 115 ? 10.221  38.298  3.143   1.00 22.34  ? 114 VAL A C      1 
ATOM   1796  O  O      . VAL A 1 115 ? 9.517   37.299  3.321   1.00 21.90  ? 114 VAL A O      1 
ATOM   1797  C  CB     . VAL A 1 115 ? 11.776  38.104  5.107   1.00 25.02  ? 114 VAL A CB     1 
ATOM   1798  C  CG1    . VAL A 1 115 ? 12.840  37.508  4.154   1.00 19.71  ? 114 VAL A CG1    1 
ATOM   1799  C  CG2    . VAL A 1 115 ? 12.450  38.880  6.260   1.00 25.12  ? 114 VAL A CG2    1 
ATOM   1800  H  H      . VAL A 1 115 ? 9.236   38.976  5.488   1.00 25.32  ? 114 VAL A H      1 
ATOM   1801  H  HA     . VAL A 1 115 ? 11.348  39.776  3.975   1.00 27.59  ? 114 VAL A HA     1 
ATOM   1802  H  HB     . VAL A 1 115 ? 11.267  37.373  5.491   1.00 30.06  ? 114 VAL A HB     1 
ATOM   1803  H  HG11   . VAL A 1 115 ? 13.554  37.118  4.683   1.00 23.69  ? 114 VAL A HG11   1 
ATOM   1804  H  HG12   . VAL A 1 115 ? 12.425  36.825  3.605   1.00 23.69  ? 114 VAL A HG12   1 
ATOM   1805  H  HG13   . VAL A 1 115 ? 13.193  38.216  3.593   1.00 23.69  ? 114 VAL A HG13   1 
ATOM   1806  H  HG21   . VAL A 1 115 ? 13.136  38.321  6.659   1.00 30.18  ? 114 VAL A HG21   1 
ATOM   1807  H  HG22   . VAL A 1 115 ? 12.849  39.690  5.905   1.00 30.18  ? 114 VAL A HG22   1 
ATOM   1808  H  HG23   . VAL A 1 115 ? 11.780  39.105  6.924   1.00 30.18  ? 114 VAL A HG23   1 
ATOM   1809  N  N      . GLY A 1 116 ? 10.518  38.778  1.929   1.00 24.53  ? 115 GLY A N      1 
ATOM   1810  C  CA     . GLY A 1 116 ? 10.171  38.051  0.722   1.00 25.13  ? 115 GLY A CA     1 
ATOM   1811  C  C      . GLY A 1 116 ? 11.353  37.246  0.221   1.00 24.25  ? 115 GLY A C      1 
ATOM   1812  O  O      . GLY A 1 116 ? 12.308  37.831  -0.314  1.00 22.50  ? 115 GLY A O      1 
ATOM   1813  H  H      . GLY A 1 116 ? 10.921  39.524  1.786   1.00 29.47  ? 115 GLY A H      1 
ATOM   1814  H  HA2    . GLY A 1 116 ? 9.435   37.446  0.905   1.00 30.19  ? 115 GLY A HA2    1 
ATOM   1815  H  HA3    . GLY A 1 116 ? 9.901   38.675  0.030   1.00 30.19  ? 115 GLY A HA3    1 
ATOM   1816  N  N      . ASN A 1 117 ? 11.315  35.927  0.413   1.00 19.78  ? 116 ASN A N      1 
ATOM   1817  C  CA     . ASN A 1 117 ? 12.457  35.052  0.157   1.00 23.91  ? 116 ASN A CA     1 
ATOM   1818  C  C      . ASN A 1 117 ? 12.340  34.368  -1.213  1.00 23.00  ? 116 ASN A C      1 
ATOM   1819  O  O      . ASN A 1 117 ? 11.313  34.451  -1.900  1.00 24.62  ? 116 ASN A O      1 
ATOM   1820  C  CB     . ASN A 1 117 ? 12.600  34.000  1.278   1.00 21.07  ? 116 ASN A CB     1 
ATOM   1821  C  CG     . ASN A 1 117 ? 13.913  33.219  1.167   1.00 18.95  ? 116 ASN A CG     1 
ATOM   1822  O  OD1    . ASN A 1 117 ? 14.966  33.824  1.009   1.00 20.95  ? 116 ASN A OD1    1 
ATOM   1823  N  ND2    . ASN A 1 117 ? 13.847  31.890  1.193   1.00 19.43  ? 116 ASN A ND2    1 
ATOM   1824  H  H      . ASN A 1 117 ? 10.621  35.506  0.698   1.00 23.77  ? 116 ASN A H      1 
ATOM   1825  H  HA     . ASN A 1 117 ? 13.262  35.594  0.145   1.00 28.72  ? 116 ASN A HA     1 
ATOM   1826  H  HB2    . ASN A 1 117 ? 12.585  34.446  2.139   1.00 25.32  ? 116 ASN A HB2    1 
ATOM   1827  H  HB3    . ASN A 1 117 ? 11.866  33.368  1.219   1.00 25.32  ? 116 ASN A HB3    1 
ATOM   1828  H  HD21   . ASN A 1 117 ? 14.566  31.422  1.132   1.00 23.35  ? 116 ASN A HD21   1 
ATOM   1829  H  HD22   . ASN A 1 117 ? 13.085  31.498  1.269   1.00 23.35  ? 116 ASN A HD22   1 
ATOM   1830  N  N      . LYS A 1 118 ? 13.435  33.707  -1.611  1.00 22.51  ? 117 LYS A N      1 
ATOM   1831  C  CA     . LYS A 1 118 ? 13.605  33.056  -2.921  1.00 25.04  ? 117 LYS A CA     1 
ATOM   1832  C  C      . LYS A 1 118 ? 13.639  34.052  -4.086  1.00 26.40  ? 117 LYS A C      1 
ATOM   1833  O  O      . LYS A 1 118 ? 13.157  33.751  -5.176  1.00 23.80  ? 117 LYS A O      1 
ATOM   1834  C  CB     . LYS A 1 118 ? 12.506  32.006  -3.144  1.00 22.15  ? 117 LYS A CB     1 
ATOM   1835  C  CG     . LYS A 1 118 ? 12.257  31.097  -1.955  1.00 24.22  ? 117 LYS A CG     1 
ATOM   1836  C  CD     . LYS A 1 118 ? 11.629  29.792  -2.404  1.00 25.24  ? 117 LYS A CD     1 
ATOM   1837  C  CE     . LYS A 1 118 ? 11.385  28.894  -1.236  1.00 25.45  ? 117 LYS A CE     1 
ATOM   1838  N  NZ     . LYS A 1 118 ? 10.722  27.619  -1.613  1.00 27.18  ? 117 LYS A NZ     1 
ATOM   1839  H  H      . LYS A 1 118 ? 14.131  33.617  -1.114  1.00 27.05  ? 117 LYS A H      1 
ATOM   1840  H  HA     . LYS A 1 118 ? 14.467  32.611  -2.926  1.00 30.08  ? 117 LYS A HA     1 
ATOM   1841  H  HB2    . LYS A 1 118 ? 11.674  32.466  -3.341  1.00 26.61  ? 117 LYS A HB2    1 
ATOM   1842  H  HB3    . LYS A 1 118 ? 12.760  31.446  -3.893  1.00 26.61  ? 117 LYS A HB3    1 
ATOM   1843  H  HG2    . LYS A 1 118 ? 13.099  30.900  -1.515  1.00 29.10  ? 117 LYS A HG2    1 
ATOM   1844  H  HG3    . LYS A 1 118 ? 11.653  31.533  -1.333  1.00 29.10  ? 117 LYS A HG3    1 
ATOM   1845  H  HD2    . LYS A 1 118 ? 10.780  29.973  -2.836  1.00 30.32  ? 117 LYS A HD2    1 
ATOM   1846  H  HD3    . LYS A 1 118 ? 12.226  29.341  -3.021  1.00 30.32  ? 117 LYS A HD3    1 
ATOM   1847  H  HE2    . LYS A 1 118 ? 12.235  28.678  -0.822  1.00 30.57  ? 117 LYS A HE2    1 
ATOM   1848  H  HE3    . LYS A 1 118 ? 10.813  29.352  -0.601  1.00 30.57  ? 117 LYS A HE3    1 
ATOM   1849  H  HZ1    . LYS A 1 118 ? 9.925   27.784  -1.973  1.00 32.65  ? 117 LYS A HZ1    1 
ATOM   1850  H  HZ2    . LYS A 1 118 ? 11.221  27.179  -2.204  1.00 32.65  ? 117 LYS A HZ2    1 
ATOM   1851  H  HZ3    . LYS A 1 118 ? 10.612  27.108  -0.892  1.00 32.65  ? 117 LYS A HZ3    1 
ATOM   1852  N  N      . CYS A 1 119 ? 14.212  35.243  -3.890  1.00 24.83  ? 118 CYS A N      1 
ATOM   1853  C  CA     . CYS A 1 119 ? 14.193  36.247  -4.943  1.00 26.20  ? 118 CYS A CA     1 
ATOM   1854  C  C      . CYS A 1 119 ? 15.169  35.922  -6.061  1.00 28.15  ? 118 CYS A C      1 
ATOM   1855  O  O      . CYS A 1 119 ? 15.238  36.667  -7.066  1.00 31.49  ? 118 CYS A O      1 
ATOM   1856  C  CB     . CYS A 1 119 ? 14.485  37.614  -4.374  1.00 25.40  ? 118 CYS A CB     1 
ATOM   1857  S  SG     . CYS A 1 119 ? 16.170  37.806  -3.806  1.00 35.57  ? 118 CYS A SG     1 
ATOM   1858  H  H      . CYS A 1 119 ? 14.610  35.485  -3.167  1.00 29.83  ? 118 CYS A H      1 
ATOM   1859  H  HA     . CYS A 1 119 ? 13.302  36.286  -5.325  1.00 31.48  ? 118 CYS A HA     1 
ATOM   1860  H  HB2    . CYS A 1 119 ? 14.325  38.279  -5.061  1.00 30.52  ? 118 CYS A HB2    1 
ATOM   1861  H  HB3    . CYS A 1 119 ? 13.898  37.769  -3.618  1.00 30.52  ? 118 CYS A HB3    1 
ATOM   1862  H  HG     . CYS A 1 119 ? 16.321  38.927  -3.407  1.00 42.72  ? 118 CYS A HG     1 
ATOM   1863  N  N      . ASP A 1 120 ? 15.885  34.812  -5.948  1.00 26.13  ? 119 ASP A N      1 
ATOM   1864  C  CA     . ASP A 1 120 ? 16.673  34.318  -7.070  1.00 29.43  ? 119 ASP A CA     1 
ATOM   1865  C  C      . ASP A 1 120 ? 15.825  33.630  -8.131  1.00 32.40  ? 119 ASP A C      1 
ATOM   1866  O  O      . ASP A 1 120 ? 16.331  33.321  -9.212  1.00 34.37  ? 119 ASP A O      1 
ATOM   1867  C  CB     . ASP A 1 120 ? 17.735  33.326  -6.579  1.00 28.31  ? 119 ASP A CB     1 
ATOM   1868  C  CG     . ASP A 1 120 ? 17.134  32.169  -5.822  1.00 29.68  ? 119 ASP A CG     1 
ATOM   1869  O  OD1    . ASP A 1 120 ? 16.739  32.393  -4.651  1.00 23.76  ? 119 ASP A OD1    1 
ATOM   1870  O  OD2    . ASP A 1 120 ? 17.059  31.042  -6.365  1.00 27.81  ? 119 ASP A OD2    1 
ATOM   1871  H  H      . ASP A 1 120 ? 15.930  34.329  -5.238  1.00 31.40  ? 119 ASP A H      1 
ATOM   1872  H  HA     . ASP A 1 120 ? 17.125  35.074  -7.476  1.00 35.34  ? 119 ASP A HA     1 
ATOM   1873  H  HB2    . ASP A 1 120 ? 18.214  32.969  -7.344  1.00 34.00  ? 119 ASP A HB2    1 
ATOM   1874  H  HB3    . ASP A 1 120 ? 18.350  33.786  -5.987  1.00 34.00  ? 119 ASP A HB3    1 
ATOM   1875  N  N      . LEU A 1 121 ? 14.566  33.368  -7.845  1.00 33.82  ? 120 LEU A N      1 
ATOM   1876  C  CA     . LEU A 1 121 ? 13.758  32.503  -8.689  1.00 30.80  ? 120 LEU A CA     1 
ATOM   1877  C  C      . LEU A 1 121 ? 13.019  33.338  -9.726  1.00 37.49  ? 120 LEU A C      1 
ATOM   1878  O  O      . LEU A 1 121 ? 12.588  34.452  -9.424  1.00 40.43  ? 120 LEU A O      1 
ATOM   1879  C  CB     . LEU A 1 121 ? 12.771  31.705  -7.838  1.00 33.26  ? 120 LEU A CB     1 
ATOM   1880  C  CG     . LEU A 1 121 ? 13.377  30.554  -7.042  1.00 33.07  ? 120 LEU A CG     1 
ATOM   1881  C  CD1    . LEU A 1 121 ? 12.247  29.792  -6.360  1.00 36.68  ? 120 LEU A CD1    1 
ATOM   1882  C  CD2    . LEU A 1 121 ? 14.216  29.613  -7.923  1.00 33.80  ? 120 LEU A CD2    1 
ATOM   1883  H  H      . LEU A 1 121 ? 14.146  33.679  -7.162  1.00 40.62  ? 120 LEU A H      1 
ATOM   1884  H  HA     . LEU A 1 121 ? 14.317  31.868  -9.163  1.00 36.99  ? 120 LEU A HA     1 
ATOM   1885  H  HB2    . LEU A 1 121 ? 12.357  32.311  -7.203  1.00 39.94  ? 120 LEU A HB2    1 
ATOM   1886  H  HB3    . LEU A 1 121 ? 12.097  31.329  -8.425  1.00 39.94  ? 120 LEU A HB3    1 
ATOM   1887  H  HG     . LEU A 1 121 ? 13.987  30.909  -6.377  1.00 39.72  ? 120 LEU A HG     1 
ATOM   1888  H  HD11   . LEU A 1 121 ? 12.626  29.075  -5.827  1.00 44.05  ? 120 LEU A HD11   1 
ATOM   1889  H  HD12   . LEU A 1 121 ? 11.754  30.403  -5.790  1.00 44.05  ? 120 LEU A HD12   1 
ATOM   1890  H  HD13   . LEU A 1 121 ? 11.659  29.425  -7.038  1.00 44.05  ? 120 LEU A HD13   1 
ATOM   1891  H  HD21   . LEU A 1 121 ? 14.382  28.790  -7.436  1.00 40.59  ? 120 LEU A HD21   1 
ATOM   1892  H  HD22   . LEU A 1 121 ? 13.726  29.422  -8.738  1.00 40.59  ? 120 LEU A HD22   1 
ATOM   1893  H  HD23   . LEU A 1 121 ? 15.057  30.047  -8.136  1.00 40.59  ? 120 LEU A HD23   1 
ATOM   1894  N  N      . PRO A 1 122 ? 12.913  32.819  -10.953 1.00 43.40  ? 121 PRO A N      1 
ATOM   1895  C  CA     . PRO A 1 122 ? 12.350  33.625  -12.042 1.00 46.46  ? 121 PRO A CA     1 
ATOM   1896  C  C      . PRO A 1 122 ? 10.843  33.701  -12.029 1.00 51.85  ? 121 PRO A C      1 
ATOM   1897  O  O      . PRO A 1 122 ? 10.282  34.658  -12.588 1.00 54.49  ? 121 PRO A O      1 
ATOM   1898  C  CB     . PRO A 1 122 ? 12.827  32.887  -13.296 1.00 49.41  ? 121 PRO A CB     1 
ATOM   1899  C  CG     . PRO A 1 122 ? 12.833  31.448  -12.866 1.00 49.82  ? 121 PRO A CG     1 
ATOM   1900  C  CD     . PRO A 1 122 ? 13.164  31.427  -11.375 1.00 44.33  ? 121 PRO A CD     1 
ATOM   1901  H  HA     . PRO A 1 122 ? 12.723  34.520  -12.020 1.00 55.78  ? 121 PRO A HA     1 
ATOM   1902  H  HB2    . PRO A 1 122 ? 12.211  33.034  -14.029 1.00 59.32  ? 121 PRO A HB2    1 
ATOM   1903  H  HB3    . PRO A 1 122 ? 13.716  33.185  -13.544 1.00 59.32  ? 121 PRO A HB3    1 
ATOM   1904  H  HG2    . PRO A 1 122 ? 11.957  31.061  -13.024 1.00 59.82  ? 121 PRO A HG2    1 
ATOM   1905  H  HG3    . PRO A 1 122 ? 13.505  30.963  -13.369 1.00 59.82  ? 121 PRO A HG3    1 
ATOM   1906  H  HD2    . PRO A 1 122 ? 12.584  30.812  -10.900 1.00 53.23  ? 121 PRO A HD2    1 
ATOM   1907  H  HD3    . PRO A 1 122 ? 14.093  31.185  -11.231 1.00 53.23  ? 121 PRO A HD3    1 
ATOM   1908  N  N      . SER A 1 123 ? 10.182  32.722  -11.428 1.00 57.45  ? 122 SER A N      1 
ATOM   1909  C  CA     . SER A 1 123 ? 8.736   32.553  -11.543 1.00 63.13  ? 122 SER A CA     1 
ATOM   1910  C  C      . SER A 1 123 ? 8.027   33.224  -10.370 1.00 63.09  ? 122 SER A C      1 
ATOM   1911  O  O      . SER A 1 123 ? 7.370   32.595  -9.534  1.00 60.92  ? 122 SER A O      1 
ATOM   1912  C  CB     . SER A 1 123 ? 8.395   31.067  -11.636 1.00 68.55  ? 122 SER A CB     1 
ATOM   1913  O  OG     . SER A 1 123 ? 8.741   30.546  -12.913 1.00 71.72  ? 122 SER A OG     1 
ATOM   1914  H  H      . SER A 1 123 ? 10.556  32.125  -10.934 1.00 68.97  ? 122 SER A H      1 
ATOM   1915  H  HA     . SER A 1 123 ? 8.429   32.983  -12.357 1.00 75.78  ? 122 SER A HA     1 
ATOM   1916  H  HB2    . SER A 1 123 ? 8.891   30.586  -10.954 1.00 82.29  ? 122 SER A HB2    1 
ATOM   1917  H  HB3    . SER A 1 123 ? 7.442   30.952  -11.496 1.00 82.29  ? 122 SER A HB3    1 
ATOM   1918  H  HG     . SER A 1 123 ? 8.595   29.719  -12.935 1.00 86.10  ? 122 SER A HG     1 
ATOM   1919  N  N      . ARG A 1 124 ? 8.165   34.542  -10.332 1.00 50.26  ? 123 ARG A N      1 
ATOM   1920  C  CA     . ARG A 1 124 ? 7.621   35.334  -9.249  1.00 44.04  ? 123 ARG A CA     1 
ATOM   1921  C  C      . ARG A 1 124 ? 6.119   35.507  -9.394  1.00 44.89  ? 123 ARG A C      1 
ATOM   1922  O  O      . ARG A 1 124 ? 5.612   35.735  -10.496 1.00 45.02  ? 123 ARG A O      1 
ATOM   1923  C  CB     . ARG A 1 124 ? 8.294   36.701  -9.222  1.00 41.50  ? 123 ARG A CB     1 
ATOM   1924  C  CG     . ARG A 1 124 ? 7.597   37.679  -8.333  1.00 46.35  ? 123 ARG A CG     1 
ATOM   1925  C  CD     . ARG A 1 124 ? 8.237   39.021  -8.448  1.00 46.01  ? 123 ARG A CD     1 
ATOM   1926  N  NE     . ARG A 1 124 ? 9.583   39.027  -7.894  1.00 47.62  ? 123 ARG A NE     1 
ATOM   1927  C  CZ     . ARG A 1 124 ? 9.910   39.540  -6.715  1.00 43.66  ? 123 ARG A CZ     1 
ATOM   1928  N  NH1    . ARG A 1 124 ? 8.995   39.977  -5.870  1.00 41.85  ? 123 ARG A NH1    1 
ATOM   1929  N  NH2    . ARG A 1 124 ? 11.196  39.633  -6.384  1.00 43.92  ? 123 ARG A NH2    1 
ATOM   1930  H  H      . ARG A 1 124 ? 8.575   35.004  -10.930 1.00 60.35  ? 123 ARG A H      1 
ATOM   1931  H  HA     . ARG A 1 124 ? 7.787   34.880  -8.408  1.00 52.88  ? 123 ARG A HA     1 
ATOM   1932  H  HB2    . ARG A 1 124 ? 9.203   36.598  -8.898  1.00 49.84  ? 123 ARG A HB2    1 
ATOM   1933  H  HB3    . ARG A 1 124 ? 8.302   37.066  -10.120 1.00 49.84  ? 123 ARG A HB3    1 
ATOM   1934  H  HG2    . ARG A 1 124 ? 6.666   37.755  -8.596  1.00 55.65  ? 123 ARG A HG2    1 
ATOM   1935  H  HG3    . ARG A 1 124 ? 7.657   37.384  -7.411  1.00 55.65  ? 123 ARG A HG3    1 
ATOM   1936  H  HD2    . ARG A 1 124 ? 8.293   39.269  -9.384  1.00 55.25  ? 123 ARG A HD2    1 
ATOM   1937  H  HD3    . ARG A 1 124 ? 7.706   39.671  -7.963  1.00 55.25  ? 123 ARG A HD3    1 
ATOM   1938  H  HE     . ARG A 1 124 ? 10.211  38.673  -8.363  1.00 57.18  ? 123 ARG A HE     1 
ATOM   1939  H  HH11   . ARG A 1 124 ? 8.162   39.933  -6.078  1.00 50.25  ? 123 ARG A HH11   1 
ATOM   1940  H  HH12   . ARG A 1 124 ? 9.233   40.305  -5.112  1.00 50.25  ? 123 ARG A HH12   1 
ATOM   1941  H  HH21   . ARG A 1 124 ? 11.802  39.363  -6.932  1.00 52.74  ? 123 ARG A HH21   1 
ATOM   1942  H  HH22   . ARG A 1 124 ? 11.421  39.964  -5.623  1.00 52.74  ? 123 ARG A HH22   1 
ATOM   1943  N  N      . THR A 1 125 ? 5.412   35.447  -8.265  1.00 42.76  ? 124 THR A N      1 
ATOM   1944  C  CA     . THR A 1 125 ? 3.987   35.723  -8.250  1.00 39.88  ? 124 THR A CA     1 
ATOM   1945  C  C      . THR A 1 125 ? 3.587   36.823  -7.291  1.00 41.23  ? 124 THR A C      1 
ATOM   1946  O  O      . THR A 1 125 ? 2.426   37.244  -7.325  1.00 41.87  ? 124 THR A O      1 
ATOM   1947  C  CB     . THR A 1 125 ? 3.182   34.454  -7.911  1.00 42.48  ? 124 THR A CB     1 
ATOM   1948  O  OG1    . THR A 1 125 ? 3.507   34.000  -6.585  1.00 38.30  ? 124 THR A OG1    1 
ATOM   1949  C  CG2    . THR A 1 125 ? 3.471   33.351  -8.943  1.00 42.42  ? 124 THR A CG2    1 
ATOM   1950  H  H      . THR A 1 125 ? 5.741   35.249  -7.496  1.00 51.34  ? 124 THR A H      1 
ATOM   1951  H  HA     . THR A 1 125 ? 3.728   35.999  -9.143  1.00 47.89  ? 124 THR A HA     1 
ATOM   1952  H  HB     . THR A 1 125 ? 2.233   34.652  -7.940  1.00 51.01  ? 124 THR A HB     1 
ATOM   1953  H  HG1    . THR A 1 125 ? 3.057   33.315  -6.397  1.00 46.00  ? 124 THR A HG1    1 
ATOM   1954  H  HG21   . THR A 1 125 ? 2.946   32.561  -8.739  1.00 50.94  ? 124 THR A HG21   1 
ATOM   1955  H  HG22   . THR A 1 125 ? 3.241   33.660  -9.833  1.00 50.94  ? 124 THR A HG22   1 
ATOM   1956  H  HG23   . THR A 1 125 ? 4.412   33.117  -8.924  1.00 50.94  ? 124 THR A HG23   1 
ATOM   1957  N  N      . VAL A 1 126 ? 4.501   37.328  -6.466  1.00 41.54  ? 125 VAL A N      1 
ATOM   1958  C  CA     . VAL A 1 126 ? 4.207   38.430  -5.557  1.00 38.26  ? 125 VAL A CA     1 
ATOM   1959  C  C      . VAL A 1 126 ? 5.096   39.610  -5.915  1.00 44.46  ? 125 VAL A C      1 
ATOM   1960  O  O      . VAL A 1 126 ? 6.330   39.510  -5.844  1.00 43.71  ? 125 VAL A O      1 
ATOM   1961  C  CB     . VAL A 1 126 ? 4.409   38.042  -4.088  1.00 38.67  ? 125 VAL A CB     1 
ATOM   1962  C  CG1    . VAL A 1 126 ? 4.120   39.216  -3.178  1.00 36.41  ? 125 VAL A CG1    1 
ATOM   1963  C  CG2    . VAL A 1 126 ? 3.525   36.856  -3.735  1.00 38.70  ? 125 VAL A CG2    1 
ATOM   1964  H  H      . VAL A 1 126 ? 5.311   37.043  -6.416  1.00 49.88  ? 125 VAL A H      1 
ATOM   1965  H  HA     . VAL A 1 126 ? 3.282   38.691  -5.688  1.00 45.94  ? 125 VAL A HA     1 
ATOM   1966  H  HB     . VAL A 1 126 ? 5.335   37.786  -3.953  1.00 46.44  ? 125 VAL A HB     1 
ATOM   1967  H  HG11   . VAL A 1 126 ? 4.060   38.900  -2.263  1.00 43.72  ? 125 VAL A HG11   1 
ATOM   1968  H  HG12   . VAL A 1 126 ? 4.838   39.863  -3.258  1.00 43.72  ? 125 VAL A HG12   1 
ATOM   1969  H  HG13   . VAL A 1 126 ? 3.279   39.622  -3.443  1.00 43.72  ? 125 VAL A HG13   1 
ATOM   1970  H  HG21   . VAL A 1 126 ? 3.616   36.665  -2.788  1.00 46.47  ? 125 VAL A HG21   1 
ATOM   1971  H  HG22   . VAL A 1 126 ? 2.603   37.077  -3.940  1.00 46.47  ? 125 VAL A HG22   1 
ATOM   1972  H  HG23   . VAL A 1 126 ? 3.805   36.087  -4.256  1.00 46.47  ? 125 VAL A HG23   1 
ATOM   1973  N  N      . ASP A 1 127 ? 4.462   40.733  -6.251  1.00 42.81  ? 126 ASP A N      1 
ATOM   1974  C  CA     . ASP A 1 127 ? 5.178   41.928  -6.652  1.00 43.44  ? 126 ASP A CA     1 
ATOM   1975  C  C      . ASP A 1 127 ? 5.891   42.543  -5.470  1.00 41.82  ? 126 ASP A C      1 
ATOM   1976  O  O      . ASP A 1 127 ? 5.363   42.566  -4.353  1.00 41.41  ? 126 ASP A O      1 
ATOM   1977  C  CB     . ASP A 1 127 ? 4.229   42.994  -7.214  1.00 47.29  ? 126 ASP A CB     1 
ATOM   1978  C  CG     . ASP A 1 127 ? 3.560   42.581  -8.490  1.00 54.56  ? 126 ASP A CG     1 
ATOM   1979  O  OD1    . ASP A 1 127 ? 2.875   43.458  -9.068  1.00 55.03  ? 126 ASP A OD1    1 
ATOM   1980  O  OD2    . ASP A 1 127 ? 3.715   41.406  -8.912  1.00 53.79  ? 126 ASP A OD2    1 
ATOM   1981  H  H      . ASP A 1 127 ? 3.607   40.824  -6.253  1.00 51.40  ? 126 ASP A H      1 
ATOM   1982  H  HA     . ASP A 1 127 ? 5.813   41.671  -7.339  1.00 52.17  ? 126 ASP A HA     1 
ATOM   1983  H  HB2    . ASP A 1 127 ? 3.536   43.173  -6.559  1.00 56.79  ? 126 ASP A HB2    1 
ATOM   1984  H  HB3    . ASP A 1 127 ? 4.735   43.802  -7.392  1.00 56.79  ? 126 ASP A HB3    1 
ATOM   1985  N  N      . THR A 1 128 ? 7.078   43.086  -5.739  1.00 41.73  ? 127 THR A N      1 
ATOM   1986  C  CA     . THR A 1 128 ? 7.777   43.894  -4.747  1.00 43.19  ? 127 THR A CA     1 
ATOM   1987  C  C      . THR A 1 128 ? 6.896   45.018  -4.213  1.00 42.79  ? 127 THR A C      1 
ATOM   1988  O  O      . THR A 1 128 ? 6.903   45.305  -3.013  1.00 43.95  ? 127 THR A O      1 
ATOM   1989  C  CB     . THR A 1 128 ? 9.056   44.464  -5.366  1.00 44.98  ? 127 THR A CB     1 
ATOM   1990  O  OG1    . THR A 1 128 ? 9.894   43.392  -5.810  1.00 41.96  ? 127 THR A OG1    1 
ATOM   1991  C  CG2    . THR A 1 128 ? 9.823   45.328  -4.356  1.00 46.31  ? 127 THR A CG2    1 
ATOM   1992  H  H      . THR A 1 128 ? 7.497   43.002  -6.486  1.00 50.11  ? 127 THR A H      1 
ATOM   1993  H  HA     . THR A 1 128 ? 8.021   43.331  -3.996  1.00 51.86  ? 127 THR A HA     1 
ATOM   1994  H  HB     . THR A 1 128 ? 8.820   45.026  -6.120  1.00 54.02  ? 127 THR A HB     1 
ATOM   1995  H  HG1    . THR A 1 128 ? 10.066  42.877  -5.170  1.00 50.39  ? 127 THR A HG1    1 
ATOM   1996  H  HG21   . THR A 1 128 ? 10.706  45.536  -4.699  1.00 55.61  ? 127 THR A HG21   1 
ATOM   1997  H  HG22   . THR A 1 128 ? 9.344   46.157  -4.197  1.00 55.61  ? 127 THR A HG22   1 
ATOM   1998  H  HG23   . THR A 1 128 ? 9.915   44.853  -3.515  1.00 55.61  ? 127 THR A HG23   1 
ATOM   1999  N  N      . LYS A 1 129 ? 6.143   45.685  -5.086  1.00 44.62  ? 128 LYS A N      1 
ATOM   2000  C  CA     . LYS A 1 129 ? 5.308   46.789  -4.614  1.00 41.59  ? 128 LYS A CA     1 
ATOM   2001  C  C      . LYS A 1 129 ? 4.153   46.257  -3.776  1.00 41.22  ? 128 LYS A C      1 
ATOM   2002  O  O      . LYS A 1 129 ? 3.746   46.885  -2.794  1.00 43.66  ? 128 LYS A O      1 
ATOM   2003  C  CB     . LYS A 1 129 ? 4.829   47.614  -5.818  1.00 45.29  ? 128 LYS A CB     1 
ATOM   2004  C  CG     . LYS A 1 129 ? 3.473   48.274  -5.692  1.00 49.42  ? 128 LYS A CG     1 
ATOM   2005  C  CD     . LYS A 1 129 ? 3.562   49.719  -5.211  1.00 52.24  ? 128 LYS A CD     1 
ATOM   2006  C  CE     . LYS A 1 129 ? 2.489   50.565  -5.879  1.00 53.43  ? 128 LYS A CE     1 
ATOM   2007  N  NZ     . LYS A 1 129 ? 1.121   49.972  -5.724  1.00 53.26  ? 128 LYS A NZ     1 
ATOM   2008  H  H      . LYS A 1 129 ? 6.097   45.524  -5.930  1.00 53.58  ? 128 LYS A H      1 
ATOM   2009  H  HA     . LYS A 1 129 ? 5.820   47.389  -4.049  1.00 49.94  ? 128 LYS A HA     1 
ATOM   2010  H  HB2    . LYS A 1 129 ? 5.475   48.321  -5.974  1.00 54.38  ? 128 LYS A HB2    1 
ATOM   2011  H  HB3    . LYS A 1 129 ? 4.788   47.026  -6.588  1.00 54.38  ? 128 LYS A HB3    1 
ATOM   2012  H  HG2    . LYS A 1 129 ? 3.039   48.272  -6.559  1.00 59.33  ? 128 LYS A HG2    1 
ATOM   2013  H  HG3    . LYS A 1 129 ? 2.938   47.778  -5.052  1.00 59.33  ? 128 LYS A HG3    1 
ATOM   2014  H  HD2    . LYS A 1 129 ? 3.429   49.752  -4.251  1.00 62.72  ? 128 LYS A HD2    1 
ATOM   2015  H  HD3    . LYS A 1 129 ? 4.431   50.085  -5.438  1.00 62.72  ? 128 LYS A HD3    1 
ATOM   2016  H  HE2    . LYS A 1 129 ? 2.483   51.448  -5.477  1.00 64.15  ? 128 LYS A HE2    1 
ATOM   2017  H  HE3    . LYS A 1 129 ? 2.683   50.634  -6.827  1.00 64.15  ? 128 LYS A HE3    1 
ATOM   2018  H  HZ1    . LYS A 1 129 ? 0.517   50.490  -6.125  1.00 63.95  ? 128 LYS A HZ1    1 
ATOM   2019  H  HZ2    . LYS A 1 129 ? 1.096   49.162  -6.093  1.00 63.95  ? 128 LYS A HZ2    1 
ATOM   2020  H  HZ3    . LYS A 1 129 ? 0.915   49.903  -4.861  1.00 63.95  ? 128 LYS A HZ3    1 
ATOM   2021  N  N      . GLN A 1 130 ? 3.607   45.108  -4.159  1.00 40.07  ? 129 GLN A N      1 
ATOM   2022  C  CA     . GLN A 1 130 ? 2.640   44.410  -3.321  1.00 41.20  ? 129 GLN A CA     1 
ATOM   2023  C  C      . GLN A 1 130 ? 3.150   44.289  -1.892  1.00 42.97  ? 129 GLN A C      1 
ATOM   2024  O  O      . GLN A 1 130 ? 2.437   44.606  -0.927  1.00 39.94  ? 129 GLN A O      1 
ATOM   2025  C  CB     . GLN A 1 130 ? 2.404   43.014  -3.890  1.00 47.90  ? 129 GLN A CB     1 
ATOM   2026  C  CG     . GLN A 1 130 ? 0.995   42.508  -3.909  1.00 48.00  ? 129 GLN A CG     1 
ATOM   2027  C  CD     . GLN A 1 130 ? 0.888   41.307  -4.823  1.00 51.93  ? 129 GLN A CD     1 
ATOM   2028  O  OE1    . GLN A 1 130 ? 1.530   41.258  -5.880  1.00 49.92  ? 129 GLN A OE1    1 
ATOM   2029  N  NE2    . GLN A 1 130 ? 0.110   40.310  -4.407  1.00 52.46  ? 129 GLN A NE2    1 
ATOM   2030  H  H      . GLN A 1 130 ? 3.779   44.711  -4.902  1.00 48.12  ? 129 GLN A H      1 
ATOM   2031  H  HA     . GLN A 1 130 ? 1.805   44.905  -3.318  1.00 49.47  ? 129 GLN A HA     1 
ATOM   2032  H  HB2    . GLN A 1 130 ? 2.716   43.010  -4.808  1.00 57.51  ? 129 GLN A HB2    1 
ATOM   2033  H  HB3    . GLN A 1 130 ? 2.921   42.386  -3.361  1.00 57.51  ? 129 GLN A HB3    1 
ATOM   2034  H  HG2    . GLN A 1 130 ? 0.731   42.242  -3.014  1.00 57.63  ? 129 GLN A HG2    1 
ATOM   2035  H  HG3    . GLN A 1 130 ? 0.403   43.203  -4.237  1.00 57.63  ? 129 GLN A HG3    1 
ATOM   2036  H  HE21   . GLN A 1 130 ? -0.300  40.371  -3.653  1.00 62.99  ? 129 GLN A HE21   1 
ATOM   2037  H  HE22   . GLN A 1 130 ? 0.017   39.606  -4.891  1.00 62.99  ? 129 GLN A HE22   1 
ATOM   2038  N  N      . ALA A 1 131 ? 4.391   43.803  -1.747  1.00 42.13  ? 130 ALA A N      1 
ATOM   2039  C  CA     . ALA A 1 131 ? 4.940   43.541  -0.424  1.00 36.26  ? 130 ALA A CA     1 
ATOM   2040  C  C      . ALA A 1 131 ? 5.303   44.832  0.283   1.00 40.27  ? 130 ALA A C      1 
ATOM   2041  O  O      . ALA A 1 131 ? 5.128   44.943  1.505   1.00 40.05  ? 130 ALA A O      1 
ATOM   2042  C  CB     . ALA A 1 131 ? 6.168   42.637  -0.532  1.00 37.37  ? 130 ALA A CB     1 
ATOM   2043  H  H      . ALA A 1 131 ? 4.925   43.619  -2.395  1.00 50.60  ? 130 ALA A H      1 
ATOM   2044  H  HA     . ALA A 1 131 ? 4.269   43.080  0.104   1.00 43.54  ? 130 ALA A HA     1 
ATOM   2045  H  HB1    . ALA A 1 131 ? 6.537   42.497  0.354   1.00 44.88  ? 130 ALA A HB1    1 
ATOM   2046  H  HB2    . ALA A 1 131 ? 5.902   41.788  -0.917  1.00 44.88  ? 130 ALA A HB2    1 
ATOM   2047  H  HB3    . ALA A 1 131 ? 6.827   43.066  -1.100  1.00 44.88  ? 130 ALA A HB3    1 
ATOM   2048  N  N      . GLN A 1 132 ? 5.821   45.813  -0.466  1.00 39.17  ? 131 GLN A N      1 
ATOM   2049  C  CA     . GLN A 1 132 ? 6.185   47.085  0.140   1.00 41.27  ? 131 GLN A CA     1 
ATOM   2050  C  C      . GLN A 1 132 ? 4.955   47.785  0.690   1.00 40.88  ? 131 GLN A C      1 
ATOM   2051  O  O      . GLN A 1 132 ? 4.997   48.376  1.778   1.00 42.13  ? 131 GLN A O      1 
ATOM   2052  C  CB     . GLN A 1 132 ? 6.864   47.999  -0.877  1.00 44.91  ? 131 GLN A CB     1 
ATOM   2053  C  CG     . GLN A 1 132 ? 8.301   47.681  -1.179  1.00 47.22  ? 131 GLN A CG     1 
ATOM   2054  C  CD     . GLN A 1 132 ? 8.793   48.429  -2.405  1.00 51.07  ? 131 GLN A CD     1 
ATOM   2055  O  OE1    . GLN A 1 132 ? 8.008   49.043  -3.125  1.00 52.63  ? 131 GLN A OE1    1 
ATOM   2056  N  NE2    . GLN A 1 132 ? 10.094  48.366  -2.656  1.00 51.23  ? 131 GLN A NE2    1 
ATOM   2057  H  H      . GLN A 1 132 ? 5.967   45.763  -1.312  1.00 47.04  ? 131 GLN A H      1 
ATOM   2058  H  HA     . GLN A 1 132 ? 6.812   46.908  0.859   1.00 49.56  ? 131 GLN A HA     1 
ATOM   2059  H  HB2    . GLN A 1 132 ? 6.375   47.942  -1.712  1.00 53.93  ? 131 GLN A HB2    1 
ATOM   2060  H  HB3    . GLN A 1 132 ? 6.836   48.907  -0.537  1.00 53.93  ? 131 GLN A HB3    1 
ATOM   2061  H  HG2    . GLN A 1 132 ? 8.852   47.938  -0.423  1.00 56.70  ? 131 GLN A HG2    1 
ATOM   2062  H  HG3    . GLN A 1 132 ? 8.390   46.729  -1.346  1.00 56.70  ? 131 GLN A HG3    1 
ATOM   2063  H  HE21   . GLN A 1 132 ? 10.611  47.918  -2.134  1.00 61.51  ? 131 GLN A HE21   1 
ATOM   2064  H  HE22   . GLN A 1 132 ? 10.420  48.773  -3.339  1.00 61.51  ? 131 GLN A HE22   1 
ATOM   2065  N  N      . ASP A 1 133 ? 3.859   47.754  -0.077  1.00 43.11  ? 132 ASP A N      1 
ATOM   2066  C  CA     . ASP A 1 133 ? 2.627   48.416  0.344   1.00 44.88  ? 132 ASP A CA     1 
ATOM   2067  C  C      . ASP A 1 133 ? 2.119   47.802  1.644   1.00 44.08  ? 132 ASP A C      1 
ATOM   2068  O  O      . ASP A 1 133 ? 1.708   48.522  2.565   1.00 45.09  ? 132 ASP A O      1 
ATOM   2069  C  CB     . ASP A 1 133 ? 1.558   48.293  -0.753  1.00 44.79  ? 132 ASP A CB     1 
ATOM   2070  C  CG     . ASP A 1 133 ? 1.853   49.147  -2.000  1.00 46.79  ? 132 ASP A CG     1 
ATOM   2071  O  OD1    . ASP A 1 133 ? 2.692   50.073  -1.959  1.00 48.69  ? 132 ASP A OD1    1 
ATOM   2072  O  OD2    . ASP A 1 133 ? 1.252   48.853  -3.055  1.00 44.67  ? 132 ASP A OD2    1 
ATOM   2073  H  H      . ASP A 1 133 ? 3.806   47.359  -0.839  1.00 51.76  ? 132 ASP A H      1 
ATOM   2074  H  HA     . ASP A 1 133 ? 2.801   49.360  0.484   1.00 53.89  ? 132 ASP A HA     1 
ATOM   2075  H  HB2    . ASP A 1 133 ? 1.503   47.367  -1.034  1.00 53.78  ? 132 ASP A HB2    1 
ATOM   2076  H  HB3    . ASP A 1 133 ? 0.705   48.582  -0.392  1.00 53.78  ? 132 ASP A HB3    1 
ATOM   2077  N  N      . LEU A 1 134 ? 2.159   46.466  1.738   1.00 42.56  ? 133 LEU A N      1 
ATOM   2078  C  CA     . LEU A 1 134 ? 1.708   45.769  2.939   1.00 44.21  ? 133 LEU A CA     1 
ATOM   2079  C  C      . LEU A 1 134 ? 2.612   46.071  4.126   1.00 43.23  ? 133 LEU A C      1 
ATOM   2080  O  O      . LEU A 1 134 ? 2.135   46.399  5.217   1.00 41.32  ? 133 LEU A O      1 
ATOM   2081  C  CB     . LEU A 1 134 ? 1.654   44.264  2.677   1.00 41.42  ? 133 LEU A CB     1 
ATOM   2082  C  CG     . LEU A 1 134 ? 1.243   43.381  3.855   1.00 41.85  ? 133 LEU A CG     1 
ATOM   2083  C  CD1    . LEU A 1 134 ? -0.279  43.444  4.047   1.00 42.51  ? 133 LEU A CD1    1 
ATOM   2084  C  CD2    . LEU A 1 134 ? 1.678   41.963  3.644   1.00 36.88  ? 133 LEU A CD2    1 
ATOM   2085  H  H      . LEU A 1 134 ? 2.444   45.942  1.118   1.00 51.11  ? 133 LEU A H      1 
ATOM   2086  H  HA     . LEU A 1 134 ? 0.814   46.075  3.159   1.00 53.08  ? 133 LEU A HA     1 
ATOM   2087  H  HB2    . LEU A 1 134 ? 1.015   44.106  1.965   1.00 49.73  ? 133 LEU A HB2    1 
ATOM   2088  H  HB3    . LEU A 1 134 ? 2.538   43.976  2.400   1.00 49.73  ? 133 LEU A HB3    1 
ATOM   2089  H  HG     . LEU A 1 134 ? 1.678   43.707  4.659   1.00 50.26  ? 133 LEU A HG     1 
ATOM   2090  H  HD11   . LEU A 1 134 ? -0.538  42.807  4.732   1.00 51.04  ? 133 LEU A HD11   1 
ATOM   2091  H  HD12   . LEU A 1 134 ? -0.527  44.341  4.320   1.00 51.04  ? 133 LEU A HD12   1 
ATOM   2092  H  HD13   . LEU A 1 134 ? -0.713  43.222  3.208   1.00 51.04  ? 133 LEU A HD13   1 
ATOM   2093  H  HD21   . LEU A 1 134 ? 1.380   41.426  4.395   1.00 44.30  ? 133 LEU A HD21   1 
ATOM   2094  H  HD22   . LEU A 1 134 ? 1.284   41.631  2.822   1.00 44.30  ? 133 LEU A HD22   1 
ATOM   2095  H  HD23   . LEU A 1 134 ? 2.646   41.935  3.581   1.00 44.30  ? 133 LEU A HD23   1 
ATOM   2096  N  N      . ALA A 1 135 ? 3.925   45.930  3.941   1.00 41.98  ? 134 ALA A N      1 
ATOM   2097  C  CA     . ALA A 1 135 ? 4.852   46.305  4.998   1.00 39.71  ? 134 ALA A CA     1 
ATOM   2098  C  C      . ALA A 1 135 ? 4.632   47.750  5.417   1.00 40.37  ? 134 ALA A C      1 
ATOM   2099  O  O      . ALA A 1 135 ? 4.677   48.078  6.610   1.00 41.16  ? 134 ALA A O      1 
ATOM   2100  C  CB     . ALA A 1 135 ? 6.286   46.106  4.530   1.00 37.06  ? 134 ALA A CB     1 
ATOM   2101  H  H      . ALA A 1 135 ? 4.295   45.625  3.227   1.00 50.41  ? 134 ALA A H      1 
ATOM   2102  H  HA     . ALA A 1 135 ? 4.704   45.733  5.766   1.00 47.69  ? 134 ALA A HA     1 
ATOM   2103  H  HB1    . ALA A 1 135 ? 6.889   46.350  5.249   1.00 44.51  ? 134 ALA A HB1    1 
ATOM   2104  H  HB2    . ALA A 1 135 ? 6.414   45.174  4.293   1.00 44.51  ? 134 ALA A HB2    1 
ATOM   2105  H  HB3    . ALA A 1 135 ? 6.447   46.669  3.757   1.00 44.51  ? 134 ALA A HB3    1 
ATOM   2106  N  N      . ARG A 1 136 ? 4.427   48.631  4.444   1.00 39.98  ? 135 ARG A N      1 
ATOM   2107  C  CA     . ARG A 1 136 ? 4.128   50.023  4.757   1.00 43.10  ? 135 ARG A CA     1 
ATOM   2108  C  C      . ARG A 1 136 ? 2.878   50.139  5.619   1.00 43.85  ? 135 ARG A C      1 
ATOM   2109  O  O      . ARG A 1 136 ? 2.849   50.919  6.581   1.00 45.38  ? 135 ARG A O      1 
ATOM   2110  C  CB     . ARG A 1 136 ? 3.960   50.808  3.454   1.00 46.55  ? 135 ARG A CB     1 
ATOM   2111  C  CG     . ARG A 1 136 ? 4.134   52.311  3.586   1.00 51.93  ? 135 ARG A CG     1 
ATOM   2112  C  CD     . ARG A 1 136 ? 4.081   53.018  2.215   1.00 54.33  ? 135 ARG A CD     1 
ATOM   2113  N  NE     . ARG A 1 136 ? 5.262   52.740  1.399   1.00 57.56  ? 135 ARG A NE     1 
ATOM   2114  C  CZ     . ARG A 1 136 ? 5.279   51.975  0.309   1.00 53.68  ? 135 ARG A CZ     1 
ATOM   2115  N  NH1    . ARG A 1 136 ? 4.177   51.414  -0.167  1.00 53.22  ? 135 ARG A NH1    1 
ATOM   2116  N  NH2    . ARG A 1 136 ? 6.435   51.772  -0.323  1.00 56.27  ? 135 ARG A NH2    1 
ATOM   2117  H  H      . ARG A 1 136 ? 4.454   48.451  3.603   1.00 48.01  ? 135 ARG A H      1 
ATOM   2118  H  HA     . ARG A 1 136 ? 4.866   50.407  5.255   1.00 51.76  ? 135 ARG A HA     1 
ATOM   2119  H  HB2    . ARG A 1 136 ? 4.622   50.493  2.819   1.00 55.89  ? 135 ARG A HB2    1 
ATOM   2120  H  HB3    . ARG A 1 136 ? 3.068   50.647  3.111   1.00 55.89  ? 135 ARG A HB3    1 
ATOM   2121  H  HG2    . ARG A 1 136 ? 3.422   52.669  4.139   1.00 62.36  ? 135 ARG A HG2    1 
ATOM   2122  H  HG3    . ARG A 1 136 ? 4.995   52.500  3.990   1.00 62.36  ? 135 ARG A HG3    1 
ATOM   2123  H  HD2    . ARG A 1 136 ? 3.300   52.710  1.729   1.00 65.24  ? 135 ARG A HD2    1 
ATOM   2124  H  HD3    . ARG A 1 136 ? 4.029   53.977  2.353   1.00 65.24  ? 135 ARG A HD3    1 
ATOM   2125  H  HE     . ARG A 1 136 ? 6.005   53.099  1.642   1.00 69.10  ? 135 ARG A HE     1 
ATOM   2126  H  HH11   . ARG A 1 136 ? 3.424   51.540  0.230   1.00 63.90  ? 135 ARG A HH11   1 
ATOM   2127  H  HH12   . ARG A 1 136 ? 4.214   50.924  -0.873  1.00 63.90  ? 135 ARG A HH12   1 
ATOM   2128  H  HH21   . ARG A 1 136 ? 7.157   52.133  -0.026  1.00 67.56  ? 135 ARG A HH21   1 
ATOM   2129  H  HH22   . ARG A 1 136 ? 6.458   51.280  -1.028  1.00 67.56  ? 135 ARG A HH22   1 
ATOM   2130  N  N      . SER A 1 137 ? 1.822   49.395  5.275   1.00 44.00  ? 136 SER A N      1 
ATOM   2131  C  CA     . SER A 1 137 ? 0.581   49.495  6.037   1.00 41.98  ? 136 SER A CA     1 
ATOM   2132  C  C      . SER A 1 137 ? 0.785   48.982  7.452   1.00 44.76  ? 136 SER A C      1 
ATOM   2133  O  O      . SER A 1 137 ? 0.204   49.515  8.405   1.00 43.26  ? 136 SER A O      1 
ATOM   2134  C  CB     . SER A 1 137 ? -0.539  48.698  5.364   1.00 46.05  ? 136 SER A CB     1 
ATOM   2135  O  OG     . SER A 1 137 ? -0.483  47.329  5.741   1.00 45.30  ? 136 SER A OG     1 
ATOM   2136  H  H      . SER A 1 137 ? 1.801   48.838  4.620   1.00 52.84  ? 136 SER A H      1 
ATOM   2137  H  HA     . SER A 1 137 ? 0.312   50.426  6.062   1.00 50.41  ? 136 SER A HA     1 
ATOM   2138  H  HB2    . SER A 1 137 ? -1.395  49.065  5.634   1.00 55.30  ? 136 SER A HB2    1 
ATOM   2139  H  HB3    . SER A 1 137 ? -0.439  48.764  4.401   1.00 55.30  ? 136 SER A HB3    1 
ATOM   2140  H  HG     . SER A 1 137 ? 0.243   46.990  5.488   1.00 54.39  ? 136 SER A HG     1 
ATOM   2141  N  N      . TYR A 1 138 ? 1.603   47.931  7.594   1.00 42.61  ? 137 TYR A N      1 
ATOM   2142  C  CA     . TYR A 1 138 ? 1.985   47.404  8.894   1.00 40.29  ? 137 TYR A CA     1 
ATOM   2143  C  C      . TYR A 1 138 ? 2.929   48.326  9.656   1.00 40.78  ? 137 TYR A C      1 
ATOM   2144  O  O      . TYR A 1 138 ? 3.092   48.157  10.865  1.00 41.02  ? 137 TYR A O      1 
ATOM   2145  C  CB     . TYR A 1 138 ? 2.688   46.053  8.727   1.00 39.12  ? 137 TYR A CB     1 
ATOM   2146  C  CG     . TYR A 1 138 ? 1.848   44.896  8.239   1.00 41.10  ? 137 TYR A CG     1 
ATOM   2147  C  CD1    . TYR A 1 138 ? 0.462   44.950  8.224   1.00 41.62  ? 137 TYR A CD1    1 
ATOM   2148  C  CD2    . TYR A 1 138 ? 2.460   43.722  7.806   1.00 38.86  ? 137 TYR A CD2    1 
ATOM   2149  C  CE1    . TYR A 1 138 ? -0.284  43.867  7.780   1.00 40.43  ? 137 TYR A CE1    1 
ATOM   2150  C  CE2    . TYR A 1 138 ? 1.733   42.652  7.364   1.00 39.29  ? 137 TYR A CE2    1 
ATOM   2151  C  CZ     . TYR A 1 138 ? 0.367   42.720  7.346   1.00 40.90  ? 137 TYR A CZ     1 
ATOM   2152  O  OH     . TYR A 1 138 ? -0.329  41.627  6.900   1.00 39.03  ? 137 TYR A OH     1 
ATOM   2153  H  H      . TYR A 1 138 ? 1.954   47.502  6.936   1.00 51.16  ? 137 TYR A H      1 
ATOM   2154  H  HA     . TYR A 1 138 ? 1.172   47.291  9.411   1.00 48.38  ? 137 TYR A HA     1 
ATOM   2155  H  HB2    . TYR A 1 138 ? 3.408   46.168  8.087   1.00 46.98  ? 137 TYR A HB2    1 
ATOM   2156  H  HB3    . TYR A 1 138 ? 3.049   45.795  9.589   1.00 46.98  ? 137 TYR A HB3    1 
ATOM   2157  H  HD1    . TYR A 1 138 ? 0.028   45.720  8.513   1.00 49.97  ? 137 TYR A HD1    1 
ATOM   2158  H  HD2    . TYR A 1 138 ? 3.388   43.665  7.818   1.00 46.66  ? 137 TYR A HD2    1 
ATOM   2159  H  HE1    . TYR A 1 138 ? -1.213  43.910  7.773   1.00 48.54  ? 137 TYR A HE1    1 
ATOM   2160  H  HE2    . TYR A 1 138 ? 2.166   41.880  7.077   1.00 47.19  ? 137 TYR A HE2    1 
ATOM   2161  H  HH     . TYR A 1 138 ? 0.204   41.009  6.698   1.00 46.87  ? 137 TYR A HH     1 
ATOM   2162  N  N      . GLY A 1 139 ? 3.599   49.252  8.980   1.00 39.70  ? 138 GLY A N      1 
ATOM   2163  C  CA     . GLY A 1 139 ? 4.619   50.048  9.636   1.00 36.11  ? 138 GLY A CA     1 
ATOM   2164  C  C      . GLY A 1 139 ? 5.919   49.318  9.925   1.00 36.26  ? 138 GLY A C      1 
ATOM   2165  O  O      . GLY A 1 139 ? 6.624   49.665  10.876  1.00 37.60  ? 138 GLY A O      1 
ATOM   2166  H  H      . GLY A 1 139 ? 3.482   49.435  8.148   1.00 47.67  ? 138 GLY A H      1 
ATOM   2167  H  HA2    . GLY A 1 139 ? 4.828   50.810  9.073   1.00 43.37  ? 138 GLY A HA2    1 
ATOM   2168  H  HA3    . GLY A 1 139 ? 4.266   50.368  10.481  1.00 43.37  ? 138 GLY A HA3    1 
ATOM   2169  N  N      . ILE A 1 140 ? 6.278   48.336  9.111   1.00 34.21  ? 139 ILE A N      1 
ATOM   2170  C  CA     . ILE A 1 140 ? 7.497   47.566  9.366   1.00 35.42  ? 139 ILE A CA     1 
ATOM   2171  C  C      . ILE A 1 140 ? 8.344   47.548  8.105   1.00 33.02  ? 139 ILE A C      1 
ATOM   2172  O  O      . ILE A 1 140 ? 7.838   47.774  6.994   1.00 29.43  ? 139 ILE A O      1 
ATOM   2173  C  CB     . ILE A 1 140 ? 7.183   46.120  9.818   1.00 33.26  ? 139 ILE A CB     1 
ATOM   2174  C  CG1    . ILE A 1 140 ? 6.490   45.344  8.698   1.00 33.39  ? 139 ILE A CG1    1 
ATOM   2175  C  CG2    . ILE A 1 140 ? 6.339   46.127  11.094  1.00 33.36  ? 139 ILE A CG2    1 
ATOM   2176  C  CD1    . ILE A 1 140 ? 6.167   43.916  9.049   1.00 31.49  ? 139 ILE A CD1    1 
ATOM   2177  H  H      . ILE A 1 140 ? 5.840   48.094  8.412   1.00 41.09  ? 139 ILE A H      1 
ATOM   2178  H  HA     . ILE A 1 140 ? 7.998   48.012  10.066  1.00 42.54  ? 139 ILE A HA     1 
ATOM   2179  H  HB     . ILE A 1 140 ? 8.021   45.672  10.016  1.00 39.94  ? 139 ILE A HB     1 
ATOM   2180  H  HG12   . ILE A 1 140 ? 5.656   45.791  8.482   1.00 40.10  ? 139 ILE A HG12   1 
ATOM   2181  H  HG13   . ILE A 1 140 ? 7.072   45.333  7.922   1.00 40.10  ? 139 ILE A HG13   1 
ATOM   2182  H  HG21   . ILE A 1 140 ? 6.279   45.222  11.439  1.00 40.06  ? 139 ILE A HG21   1 
ATOM   2183  H  HG22   . ILE A 1 140 ? 6.762   46.703  11.750  1.00 40.06  ? 139 ILE A HG22   1 
ATOM   2184  H  HG23   . ILE A 1 140 ? 5.452   46.460  10.885  1.00 40.06  ? 139 ILE A HG23   1 
ATOM   2185  H  HD11   . ILE A 1 140 ? 5.840   43.463  8.256   1.00 37.82  ? 139 ILE A HD11   1 
ATOM   2186  H  HD12   . ILE A 1 140 ? 6.971   43.480  9.371   1.00 37.82  ? 139 ILE A HD12   1 
ATOM   2187  H  HD13   . ILE A 1 140 ? 5.486   43.907  9.740   1.00 37.82  ? 139 ILE A HD13   1 
ATOM   2188  N  N      . PRO A 1 141 ? 9.629   47.231  8.242   1.00 31.57  ? 140 PRO A N      1 
ATOM   2189  C  CA     . PRO A 1 141 ? 10.495  47.131  7.064   1.00 32.09  ? 140 PRO A CA     1 
ATOM   2190  C  C      . PRO A 1 141 ? 10.194  45.904  6.220   1.00 34.38  ? 140 PRO A C      1 
ATOM   2191  O  O      . PRO A 1 141 ? 9.601   44.918  6.667   1.00 31.02  ? 140 PRO A O      1 
ATOM   2192  C  CB     . PRO A 1 141 ? 11.901  47.043  7.664   1.00 32.19  ? 140 PRO A CB     1 
ATOM   2193  C  CG     . PRO A 1 141 ? 11.767  47.574  9.060   1.00 30.83  ? 140 PRO A CG     1 
ATOM   2194  C  CD     . PRO A 1 141 ? 10.409  47.105  9.487   1.00 34.17  ? 140 PRO A CD     1 
ATOM   2195  H  HA     . PRO A 1 141 ? 10.408  47.927  6.517   1.00 38.55  ? 140 PRO A HA     1 
ATOM   2196  H  HB2    . PRO A 1 141 ? 12.199  46.120  7.672   1.00 38.66  ? 140 PRO A HB2    1 
ATOM   2197  H  HB3    . PRO A 1 141 ? 12.515  47.586  7.145   1.00 38.66  ? 140 PRO A HB3    1 
ATOM   2198  H  HG2    . PRO A 1 141 ? 12.461  47.205  9.628   1.00 37.03  ? 140 PRO A HG2    1 
ATOM   2199  H  HG3    . PRO A 1 141 ? 11.820  48.542  9.058   1.00 37.03  ? 140 PRO A HG3    1 
ATOM   2200  H  HD2    . PRO A 1 141 ? 10.437  46.184  9.790   1.00 41.04  ? 140 PRO A HD2    1 
ATOM   2201  H  HD3    . PRO A 1 141 ? 10.047  47.673  10.185  1.00 41.04  ? 140 PRO A HD3    1 
ATOM   2202  N  N      . PHE A 1 142 ? 10.633  45.973  4.969   1.00 33.01  ? 141 PHE A N      1 
ATOM   2203  C  CA     . PHE A 1 142 ? 10.471  44.876  4.038   1.00 29.86  ? 141 PHE A CA     1 
ATOM   2204  C  C      . PHE A 1 142 ? 11.792  44.666  3.326   1.00 31.13  ? 141 PHE A C      1 
ATOM   2205  O  O      . PHE A 1 142 ? 12.410  45.629  2.858   1.00 30.05  ? 141 PHE A O      1 
ATOM   2206  C  CB     . PHE A 1 142 ? 9.364   45.140  3.024   1.00 34.26  ? 141 PHE A CB     1 
ATOM   2207  C  CG     . PHE A 1 142 ? 9.373   44.192  1.856   1.00 31.31  ? 141 PHE A CG     1 
ATOM   2208  C  CD1    . PHE A 1 142 ? 9.205   42.823  2.048   1.00 29.15  ? 141 PHE A CD1    1 
ATOM   2209  C  CD2    . PHE A 1 142 ? 9.554   44.664  0.571   1.00 37.10  ? 141 PHE A CD2    1 
ATOM   2210  C  CE1    . PHE A 1 142 ? 9.206   41.950  0.961   1.00 32.37  ? 141 PHE A CE1    1 
ATOM   2211  C  CE2    . PHE A 1 142 ? 9.565   43.807  -0.509  1.00 35.51  ? 141 PHE A CE2    1 
ATOM   2212  C  CZ     . PHE A 1 142 ? 9.386   42.443  -0.318  1.00 33.08  ? 141 PHE A CZ     1 
ATOM   2213  H  H      . PHE A 1 142 ? 11.033  46.657  4.636   1.00 39.65  ? 141 PHE A H      1 
ATOM   2214  H  HA     . PHE A 1 142 ? 10.232  44.070  4.523   1.00 35.86  ? 141 PHE A HA     1 
ATOM   2215  H  HB2    . PHE A 1 142 ? 8.506   45.053  3.469   1.00 41.14  ? 141 PHE A HB2    1 
ATOM   2216  H  HB3    . PHE A 1 142 ? 9.468   46.039  2.676   1.00 41.14  ? 141 PHE A HB3    1 
ATOM   2217  H  HD1    . PHE A 1 142 ? 9.091   42.488  2.908   1.00 35.01  ? 141 PHE A HD1    1 
ATOM   2218  H  HD2    . PHE A 1 142 ? 9.671   45.576  0.431   1.00 44.55  ? 141 PHE A HD2    1 
ATOM   2219  H  HE1    . PHE A 1 142 ? 9.087   41.037  1.096   1.00 38.88  ? 141 PHE A HE1    1 
ATOM   2220  H  HE2    . PHE A 1 142 ? 9.693   44.142  -1.367  1.00 42.64  ? 141 PHE A HE2    1 
ATOM   2221  H  HZ     . PHE A 1 142 ? 9.386   41.864  -1.046  1.00 39.74  ? 141 PHE A HZ     1 
ATOM   2222  N  N      . ILE A 1 143 ? 12.205  43.407  3.236   1.00 28.04  ? 142 ILE A N      1 
ATOM   2223  C  CA     . ILE A 1 143 ? 13.477  43.035  2.630   1.00 27.76  ? 142 ILE A CA     1 
ATOM   2224  C  C      . ILE A 1 143 ? 13.270  41.801  1.788   1.00 29.52  ? 142 ILE A C      1 
ATOM   2225  O  O      . ILE A 1 143 ? 12.772  40.785  2.281   1.00 24.76  ? 142 ILE A O      1 
ATOM   2226  C  CB     . ILE A 1 143 ? 14.559  42.765  3.701   1.00 28.20  ? 142 ILE A CB     1 
ATOM   2227  C  CG1    . ILE A 1 143 ? 14.397  43.833  4.778   1.00 33.50  ? 142 ILE A CG1    1 
ATOM   2228  C  CG2    . ILE A 1 143 ? 15.941  42.625  3.050   1.00 30.90  ? 142 ILE A CG2    1 
ATOM   2229  C  CD1    . ILE A 1 143 ? 15.498  43.909  5.776   1.00 37.37  ? 142 ILE A CD1    1 
ATOM   2230  H  H      . ILE A 1 143 ? 11.754  42.734  3.526   1.00 33.68  ? 142 ILE A H      1 
ATOM   2231  H  HA     . ILE A 1 143 ? 13.776  43.754  2.052   1.00 33.34  ? 142 ILE A HA     1 
ATOM   2232  H  HB     . ILE A 1 143 ? 14.453  41.911  4.149   1.00 33.88  ? 142 ILE A HB     1 
ATOM   2233  H  HG12   . ILE A 1 143 ? 14.341  44.698  4.344   1.00 40.23  ? 142 ILE A HG12   1 
ATOM   2234  H  HG13   . ILE A 1 143 ? 13.578  43.652  5.265   1.00 40.23  ? 142 ILE A HG13   1 
ATOM   2235  H  HG21   . ILE A 1 143 ? 16.595  42.426  3.738   1.00 37.12  ? 142 ILE A HG21   1 
ATOM   2236  H  HG22   . ILE A 1 143 ? 15.913  41.903  2.403   1.00 37.12  ? 142 ILE A HG22   1 
ATOM   2237  H  HG23   . ILE A 1 143 ? 16.168  43.458  2.608   1.00 37.12  ? 142 ILE A HG23   1 
ATOM   2238  H  HD11   . ILE A 1 143 ? 15.301  44.617  6.410   1.00 44.88  ? 142 ILE A HD11   1 
ATOM   2239  H  HD12   . ILE A 1 143 ? 15.564  43.060  6.240   1.00 44.88  ? 142 ILE A HD12   1 
ATOM   2240  H  HD13   . ILE A 1 143 ? 16.329  44.100  5.315   1.00 44.88  ? 142 ILE A HD13   1 
ATOM   2241  N  N      . GLU A 1 144 ? 13.713  41.866  0.536   1.00 28.20  ? 143 GLU A N      1 
ATOM   2242  C  CA     . GLU A 1 144 ? 13.743  40.698  -0.334  1.00 30.22  ? 143 GLU A CA     1 
ATOM   2243  C  C      . GLU A 1 144 ? 15.062  39.973  -0.148  1.00 25.29  ? 143 GLU A C      1 
ATOM   2244  O  O      . GLU A 1 144 ? 16.115  40.596  -0.004  1.00 23.72  ? 143 GLU A O      1 
ATOM   2245  C  CB     . GLU A 1 144 ? 13.544  41.117  -1.793  1.00 31.06  ? 143 GLU A CB     1 
ATOM   2246  C  CG     . GLU A 1 144 ? 12.062  41.430  -2.080  1.00 35.69  ? 143 GLU A CG     1 
ATOM   2247  C  CD     . GLU A 1 144 ? 11.670  41.317  -3.570  1.00 42.55  ? 143 GLU A CD     1 
ATOM   2248  O  OE1    . GLU A 1 144 ? 10.462  41.417  -3.867  1.00 44.56  ? 143 GLU A OE1    1 
ATOM   2249  O  OE2    . GLU A 1 144 ? 12.562  41.178  -4.439  1.00 42.94  ? 143 GLU A OE2    1 
ATOM   2250  H  H      . GLU A 1 144 ? 14.005  42.585  0.164   1.00 33.88  ? 143 GLU A H      1 
ATOM   2251  H  HA     . GLU A 1 144 ? 13.026  40.084  -0.109  1.00 36.30  ? 143 GLU A HA     1 
ATOM   2252  H  HB2    . GLU A 1 144 ? 14.068  41.912  -1.974  1.00 37.30  ? 143 GLU A HB2    1 
ATOM   2253  H  HB3    . GLU A 1 144 ? 13.824  40.394  -2.377  1.00 37.30  ? 143 GLU A HB3    1 
ATOM   2254  H  HG2    . GLU A 1 144 ? 11.510  40.807  -1.582  1.00 42.86  ? 143 GLU A HG2    1 
ATOM   2255  H  HG3    . GLU A 1 144 ? 11.875  42.339  -1.795  1.00 42.86  ? 143 GLU A HG3    1 
ATOM   2256  N  N      . THR A 1 145 ? 14.981  38.654  -0.088  1.00 22.33  ? 144 THR A N      1 
ATOM   2257  C  CA     . THR A 1 145 ? 16.128  37.832  0.239   1.00 20.97  ? 144 THR A CA     1 
ATOM   2258  C  C      . THR A 1 145 ? 16.185  36.638  -0.692  1.00 22.23  ? 144 THR A C      1 
ATOM   2259  O  O      . THR A 1 145 ? 15.208  36.290  -1.354  1.00 22.53  ? 144 THR A O      1 
ATOM   2260  C  CB     . THR A 1 145 ? 16.084  37.311  1.705   1.00 21.29  ? 144 THR A CB     1 
ATOM   2261  O  OG1    . THR A 1 145 ? 14.943  36.447  1.872   1.00 21.25  ? 144 THR A OG1    1 
ATOM   2262  C  CG2    . THR A 1 145 ? 16.014  38.453  2.702   1.00 21.96  ? 144 THR A CG2    1 
ATOM   2263  H  H      . THR A 1 145 ? 14.261  38.207  -0.234  1.00 26.83  ? 144 THR A H      1 
ATOM   2264  H  HA     . THR A 1 145 ? 16.926  38.371  0.117   1.00 25.20  ? 144 THR A HA     1 
ATOM   2265  H  HB     . THR A 1 145 ? 16.898  36.817  1.889   1.00 25.59  ? 144 THR A HB     1 
ATOM   2266  H  HG1    . THR A 1 145 ? 15.047  35.744  1.423   1.00 25.53  ? 144 THR A HG1    1 
ATOM   2267  H  HG21   . THR A 1 145 ? 16.001  38.102  3.607   1.00 26.38  ? 144 THR A HG21   1 
ATOM   2268  H  HG22   . THR A 1 145 ? 16.787  39.030  2.600   1.00 26.38  ? 144 THR A HG22   1 
ATOM   2269  H  HG23   . THR A 1 145 ? 15.210  38.974  2.555   1.00 26.38  ? 144 THR A HG23   1 
ATOM   2270  N  N      . SER A 1 146 ? 17.361  36.000  -0.707  1.00 21.81  ? 145 SER A N      1 
ATOM   2271  C  CA     . SER A 1 146 ? 17.559  34.683  -1.290  1.00 22.27  ? 145 SER A CA     1 
ATOM   2272  C  C      . SER A 1 146 ? 18.509  33.946  -0.359  1.00 23.89  ? 145 SER A C      1 
ATOM   2273  O  O      . SER A 1 146 ? 19.648  34.378  -0.144  1.00 21.29  ? 145 SER A O      1 
ATOM   2274  C  CB     . SER A 1 146 ? 18.135  34.773  -2.723  1.00 22.43  ? 145 SER A CB     1 
ATOM   2275  O  OG     . SER A 1 146 ? 18.609  33.498  -3.090  1.00 22.62  ? 145 SER A OG     1 
ATOM   2276  H  H      . SER A 1 146 ? 18.082  36.328  -0.371  1.00 26.21  ? 145 SER A H      1 
ATOM   2277  H  HA     . SER A 1 146 ? 16.720  34.200  -1.353  1.00 26.76  ? 145 SER A HA     1 
ATOM   2278  H  HB2    . SER A 1 146 ? 17.437  35.051  -3.338  1.00 26.95  ? 145 SER A HB2    1 
ATOM   2279  H  HB3    . SER A 1 146 ? 18.866  35.411  -2.741  1.00 26.95  ? 145 SER A HB3    1 
ATOM   2280  H  HG     . SER A 1 146 ? 17.978  32.944  -3.080  1.00 27.18  ? 145 SER A HG     1 
ATOM   2281  N  N      . ALA A 1 147 ? 18.030  32.856  0.222   1.00 21.48  ? 146 ALA A N      1 
ATOM   2282  C  CA     . ALA A 1 147 ? 18.906  32.004  1.002   1.00 22.44  ? 146 ALA A CA     1 
ATOM   2283  C  C      . ALA A 1 147 ? 19.914  31.303  0.106   1.00 24.61  ? 146 ALA A C      1 
ATOM   2284  O  O      . ALA A 1 147 ? 20.951  30.861  0.598   1.00 23.29  ? 146 ALA A O      1 
ATOM   2285  C  CB     . ALA A 1 147 ? 18.073  30.987  1.771   1.00 21.44  ? 146 ALA A CB     1 
ATOM   2286  H  H      . ALA A 1 147 ? 17.213  32.593  0.180   1.00 25.81  ? 146 ALA A H      1 
ATOM   2287  H  HA     . ALA A 1 147 ? 19.395  32.530  1.654   1.00 26.96  ? 146 ALA A HA     1 
ATOM   2288  H  HB1    . ALA A 1 147 ? 18.667  30.406  2.271   1.00 25.76  ? 146 ALA A HB1    1 
ATOM   2289  H  HB2    . ALA A 1 147 ? 17.482  31.458  2.378   1.00 25.76  ? 146 ALA A HB2    1 
ATOM   2290  H  HB3    . ALA A 1 147 ? 17.553  30.465  1.141   1.00 25.76  ? 146 ALA A HB3    1 
ATOM   2291  N  N      . LYS A 1 148 ? 19.617  31.193  -1.193  1.00 20.77  ? 147 LYS A N      1 
ATOM   2292  C  CA     . LYS A 1 148 ? 20.540  30.535  -2.115  1.00 24.21  ? 147 LYS A CA     1 
ATOM   2293  C  C      . LYS A 1 148 ? 21.725  31.434  -2.476  1.00 21.59  ? 147 LYS A C      1 
ATOM   2294  O  O      . LYS A 1 148 ? 22.880  31.001  -2.404  1.00 24.59  ? 147 LYS A O      1 
ATOM   2295  C  CB     . LYS A 1 148 ? 19.789  30.114  -3.378  1.00 25.90  ? 147 LYS A CB     1 
ATOM   2296  C  CG     . LYS A 1 148 ? 20.591  29.237  -4.337  1.00 28.32  ? 147 LYS A CG     1 
ATOM   2297  C  CD     . LYS A 1 148 ? 19.675  28.736  -5.445  1.00 28.88  ? 147 LYS A CD     1 
ATOM   2298  C  CE     . LYS A 1 148 ? 20.463  27.920  -6.440  1.00 30.74  ? 147 LYS A CE     1 
ATOM   2299  N  NZ     . LYS A 1 148 ? 19.658  27.667  -7.669  1.00 40.45  ? 147 LYS A NZ     1 
ATOM   2300  H  H      . LYS A 1 148 ? 18.896  31.489  -1.559  1.00 24.96  ? 147 LYS A H      1 
ATOM   2301  H  HA     . LYS A 1 148 ? 20.895  29.742  -1.685  1.00 29.08  ? 147 LYS A HA     1 
ATOM   2302  H  HB2    . LYS A 1 148 ? 19.001  29.613  -3.114  1.00 31.11  ? 147 LYS A HB2    1 
ATOM   2303  H  HB3    . LYS A 1 148 ? 19.527  30.913  -3.862  1.00 31.11  ? 147 LYS A HB3    1 
ATOM   2304  H  HG2    . LYS A 1 148 ? 21.310  29.755  -4.733  1.00 34.02  ? 147 LYS A HG2    1 
ATOM   2305  H  HG3    . LYS A 1 148 ? 20.955  28.475  -3.860  1.00 34.02  ? 147 LYS A HG3    1 
ATOM   2306  H  HD2    . LYS A 1 148 ? 18.979  28.177  -5.066  1.00 34.69  ? 147 LYS A HD2    1 
ATOM   2307  H  HD3    . LYS A 1 148 ? 19.278  29.491  -5.907  1.00 34.69  ? 147 LYS A HD3    1 
ATOM   2308  H  HE2    . LYS A 1 148 ? 21.266  28.403  -6.691  1.00 36.92  ? 147 LYS A HE2    1 
ATOM   2309  H  HE3    . LYS A 1 148 ? 20.699  27.066  -6.044  1.00 36.92  ? 147 LYS A HE3    1 
ATOM   2310  H  HZ1    . LYS A 1 148 ? 20.135  27.198  -8.255  1.00 48.58  ? 147 LYS A HZ1    1 
ATOM   2311  H  HZ2    . LYS A 1 148 ? 18.923  27.209  -7.462  1.00 48.58  ? 147 LYS A HZ2    1 
ATOM   2312  H  HZ3    . LYS A 1 148 ? 19.421  28.440  -8.042  1.00 48.58  ? 147 LYS A HZ3    1 
ATOM   2313  N  N      . THR A 1 149 ? 21.472  32.666  -2.896  1.00 21.24  ? 148 THR A N      1 
ATOM   2314  C  CA     . THR A 1 149 ? 22.566  33.589  -3.205  1.00 21.78  ? 148 THR A CA     1 
ATOM   2315  C  C      . THR A 1 149 ? 23.082  34.343  -1.988  1.00 20.67  ? 148 THR A C      1 
ATOM   2316  O  O      . THR A 1 149 ? 24.113  35.016  -2.070  1.00 19.99  ? 148 THR A O      1 
ATOM   2317  C  CB     . THR A 1 149 ? 22.103  34.620  -4.242  1.00 23.99  ? 148 THR A CB     1 
ATOM   2318  O  OG1    . THR A 1 149 ? 21.179  35.493  -3.578  1.00 23.06  ? 148 THR A OG1    1 
ATOM   2319  C  CG2    . THR A 1 149 ? 21.507  33.912  -5.460  1.00 24.51  ? 148 THR A CG2    1 
ATOM   2320  H  H      . THR A 1 149 ? 20.684  32.992  -3.010  1.00 25.52  ? 148 THR A H      1 
ATOM   2321  H  HA     . THR A 1 149 ? 23.298  33.073  -3.577  1.00 26.16  ? 148 THR A HA     1 
ATOM   2322  H  HB     . THR A 1 149 ? 22.830  35.156  -4.596  1.00 28.82  ? 148 THR A HB     1 
ATOM   2323  H  HG1    . THR A 1 149 ? 20.968  36.128  -4.085  1.00 27.71  ? 148 THR A HG1    1 
ATOM   2324  H  HG21   . THR A 1 149 ? 21.463  34.524  -6.211  1.00 29.45  ? 148 THR A HG21   1 
ATOM   2325  H  HG22   . THR A 1 149 ? 22.057  33.152  -5.704  1.00 29.45  ? 148 THR A HG22   1 
ATOM   2326  H  HG23   . THR A 1 149 ? 20.611  33.600  -5.256  1.00 29.45  ? 148 THR A HG23   1 
ATOM   2327  N  N      . ARG A 1 150 ? 22.380  34.283  -0.855  1.00 18.80  ? 149 ARG A N      1 
ATOM   2328  C  CA     . ARG A 1 150 ? 22.647  35.079  0.339   1.00 21.97  ? 149 ARG A CA     1 
ATOM   2329  C  C      . ARG A 1 150 ? 22.219  36.547  0.248   1.00 21.83  ? 149 ARG A C      1 
ATOM   2330  O  O      . ARG A 1 150 ? 22.418  37.272  1.241   1.00 21.30  ? 149 ARG A O      1 
ATOM   2331  C  CB     . ARG A 1 150 ? 24.122  35.086  0.752   1.00 23.49  ? 149 ARG A CB     1 
ATOM   2332  C  CG     . ARG A 1 150 ? 24.760  33.724  0.676   1.00 23.52  ? 149 ARG A CG     1 
ATOM   2333  C  CD     . ARG A 1 150 ? 26.137  33.740  1.283   1.00 25.01  ? 149 ARG A CD     1 
ATOM   2334  N  NE     . ARG A 1 150 ? 26.004  33.436  2.669   1.00 28.85  ? 149 ARG A NE     1 
ATOM   2335  C  CZ     . ARG A 1 150 ? 25.893  34.328  3.635   1.00 29.61  ? 149 ARG A CZ     1 
ATOM   2336  N  NH1    . ARG A 1 150 ? 26.271  35.582  3.465   1.00 31.90  ? 149 ARG A NH1    1 
ATOM   2337  N  NH2    . ARG A 1 150 ? 25.352  33.956  4.785   1.00 27.05  ? 149 ARG A NH2    1 
ATOM   2338  H  H      . ARG A 1 150 ? 21.707  33.758  -0.755  1.00 22.59  ? 149 ARG A H      1 
ATOM   2339  H  HA     . ARG A 1 150 ? 22.110  34.664  1.032   1.00 26.40  ? 149 ARG A HA     1 
ATOM   2340  H  HB2    . ARG A 1 150 ? 24.611  35.679  0.161   1.00 28.22  ? 149 ARG A HB2    1 
ATOM   2341  H  HB3    . ARG A 1 150 ? 24.191  35.398  1.667   1.00 28.22  ? 149 ARG A HB3    1 
ATOM   2342  H  HG2    . ARG A 1 150 ? 24.217  33.086  1.164   1.00 28.26  ? 149 ARG A HG2    1 
ATOM   2343  H  HG3    . ARG A 1 150 ? 24.836  33.454  -0.252  1.00 28.26  ? 149 ARG A HG3    1 
ATOM   2344  H  HD2    . ARG A 1 150 ? 26.697  33.070  0.860   1.00 30.05  ? 149 ARG A HD2    1 
ATOM   2345  H  HD3    . ARG A 1 150 ? 26.538  34.617  1.183   1.00 30.05  ? 149 ARG A HD3    1 
ATOM   2346  H  HE     . ARG A 1 150 ? 25.997  32.606  2.894   1.00 34.66  ? 149 ARG A HE     1 
ATOM   2347  H  HH11   . ARG A 1 150 ? 26.600  35.834  2.712   1.00 38.32  ? 149 ARG A HH11   1 
ATOM   2348  H  HH12   . ARG A 1 150 ? 26.189  36.147  4.109   1.00 38.32  ? 149 ARG A HH12   1 
ATOM   2349  H  HH21   . ARG A 1 150 ? 25.082  33.146  4.891   1.00 32.49  ? 149 ARG A HH21   1 
ATOM   2350  H  HH22   . ARG A 1 150 ? 25.271  34.524  5.426   1.00 32.49  ? 149 ARG A HH22   1 
ATOM   2351  N  N      . GLN A 1 151 ? 21.652  37.009  -0.873  1.00 22.05  ? 150 GLN A N      1 
ATOM   2352  C  CA     . GLN A 1 151 ? 21.119  38.358  -0.959  1.00 21.65  ? 150 GLN A CA     1 
ATOM   2353  C  C      . GLN A 1 151 ? 20.205  38.634  0.232   1.00 22.65  ? 150 GLN A C      1 
ATOM   2354  O  O      . GLN A 1 151 ? 19.275  37.872  0.502   1.00 21.41  ? 150 GLN A O      1 
ATOM   2355  C  CB     . GLN A 1 151 ? 20.327  38.563  -2.257  1.00 24.20  ? 150 GLN A CB     1 
ATOM   2356  C  CG     . GLN A 1 151 ? 19.612  39.900  -2.320  1.00 27.68  ? 150 GLN A CG     1 
ATOM   2357  C  CD     . GLN A 1 151 ? 18.971  40.196  -3.670  1.00 31.24  ? 150 GLN A CD     1 
ATOM   2358  O  OE1    . GLN A 1 151 ? 19.220  39.511  -4.667  1.00 29.96  ? 150 GLN A OE1    1 
ATOM   2359  N  NE2    . GLN A 1 151 ? 18.155  41.251  -3.716  1.00 39.47  ? 150 GLN A NE2    1 
ATOM   2360  H  H      . GLN A 1 151 ? 21.566  36.554  -1.597  1.00 26.49  ? 150 GLN A H      1 
ATOM   2361  H  HA     . GLN A 1 151 ? 21.862  38.981  -0.962  1.00 26.02  ? 150 GLN A HA     1 
ATOM   2362  H  HB2    . GLN A 1 151 ? 20.938  38.516  -3.008  1.00 29.08  ? 150 GLN A HB2    1 
ATOM   2363  H  HB3    . GLN A 1 151 ? 19.658  37.864  -2.329  1.00 29.08  ? 150 GLN A HB3    1 
ATOM   2364  H  HG2    . GLN A 1 151 ? 18.908  39.909  -1.652  1.00 33.25  ? 150 GLN A HG2    1 
ATOM   2365  H  HG3    . GLN A 1 151 ? 20.252  40.604  -2.137  1.00 33.25  ? 150 GLN A HG3    1 
ATOM   2366  H  HE21   . GLN A 1 151 ? 18.018  41.720  -3.008  1.00 47.40  ? 150 GLN A HE21   1 
ATOM   2367  H  HE22   . GLN A 1 151 ? 17.767  41.463  -4.453  1.00 47.40  ? 150 GLN A HE22   1 
ATOM   2368  N  N      . GLY A 1 152 ? 20.477  39.738  0.919   1.00 20.98  ? 151 GLY A N      1 
ATOM   2369  C  CA     . GLY A 1 152 ? 19.625  40.262  1.958   1.00 22.12  ? 151 GLY A CA     1 
ATOM   2370  C  C      . GLY A 1 152 ? 19.608  39.494  3.266   1.00 24.16  ? 151 GLY A C      1 
ATOM   2371  O  O      . GLY A 1 152 ? 18.875  39.910  4.192   1.00 24.49  ? 151 GLY A O      1 
ATOM   2372  H  H      . GLY A 1 152 ? 21.181  40.216  0.791   1.00 25.21  ? 151 GLY A H      1 
ATOM   2373  H  HA2    . GLY A 1 152 ? 19.909  41.167  2.158   1.00 26.58  ? 151 GLY A HA2    1 
ATOM   2374  H  HA3    . GLY A 1 152 ? 18.715  40.283  1.623   1.00 26.58  ? 151 GLY A HA3    1 
ATOM   2375  N  N      . VAL A 1 153 ? 20.377  38.407  3.397   1.00 20.77  ? 152 VAL A N      1 
ATOM   2376  C  CA     . VAL A 1 153 ? 20.252  37.561  4.588   1.00 18.43  ? 152 VAL A CA     1 
ATOM   2377  C  C      . VAL A 1 153 ? 20.684  38.351  5.823   1.00 21.78  ? 152 VAL A C      1 
ATOM   2378  O  O      . VAL A 1 153 ? 19.919  38.546  6.775   1.00 21.53  ? 152 VAL A O      1 
ATOM   2379  C  CB     . VAL A 1 153 ? 21.063  36.262  4.434   1.00 21.58  ? 152 VAL A CB     1 
ATOM   2380  C  CG1    . VAL A 1 153 ? 21.085  35.491  5.765   1.00 22.58  ? 152 VAL A CG1    1 
ATOM   2381  C  CG2    . VAL A 1 153 ? 20.452  35.377  3.333   1.00 21.43  ? 152 VAL A CG2    1 
ATOM   2382  H  H      . VAL A 1 153 ? 20.963  38.144  2.825   1.00 24.96  ? 152 VAL A H      1 
ATOM   2383  H  HA     . VAL A 1 153 ? 19.322  37.307  4.694   1.00 22.15  ? 152 VAL A HA     1 
ATOM   2384  H  HB     . VAL A 1 153 ? 21.973  36.488  4.185   1.00 25.93  ? 152 VAL A HB     1 
ATOM   2385  H  HG11   . VAL A 1 153 ? 21.390  34.585  5.599   1.00 27.13  ? 152 VAL A HG11   1 
ATOM   2386  H  HG12   . VAL A 1 153 ? 21.690  35.937  6.378   1.00 27.13  ? 152 VAL A HG12   1 
ATOM   2387  H  HG13   . VAL A 1 153 ? 20.189  35.476  6.136   1.00 27.13  ? 152 VAL A HG13   1 
ATOM   2388  H  HG21   . VAL A 1 153 ? 20.963  34.556  3.268   1.00 25.75  ? 152 VAL A HG21   1 
ATOM   2389  H  HG22   . VAL A 1 153 ? 19.531  35.176  3.563   1.00 25.75  ? 152 VAL A HG22   1 
ATOM   2390  H  HG23   . VAL A 1 153 ? 20.485  35.855  2.489   1.00 25.75  ? 152 VAL A HG23   1 
ATOM   2391  N  N      . ASP A 1 154 ? 21.907  38.881  5.803   1.00 24.73  ? 153 ASP A N      1 
ATOM   2392  C  CA     . ASP A 1 154 ? 22.340  39.697  6.934   1.00 22.63  ? 153 ASP A CA     1 
ATOM   2393  C  C      . ASP A 1 154 ? 21.398  40.873  7.159   1.00 25.45  ? 153 ASP A C      1 
ATOM   2394  O  O      . ASP A 1 154 ? 21.005  41.156  8.299   1.00 28.76  ? 153 ASP A O      1 
ATOM   2395  C  CB     . ASP A 1 154 ? 23.782  40.183  6.729   1.00 27.28  ? 153 ASP A CB     1 
ATOM   2396  C  CG     . ASP A 1 154 ? 24.825  39.109  7.057   1.00 29.87  ? 153 ASP A CG     1 
ATOM   2397  O  OD1    . ASP A 1 154 ? 24.506  38.082  7.693   1.00 28.49  ? 153 ASP A OD1    1 
ATOM   2398  O  OD2    . ASP A 1 154 ? 25.994  39.302  6.701   1.00 32.47  ? 153 ASP A OD2    1 
ATOM   2399  H  H      . ASP A 1 154 ? 22.482  38.788  5.171   1.00 29.71  ? 153 ASP A H      1 
ATOM   2400  H  HA     . ASP A 1 154 ? 22.327  39.144  7.731   1.00 27.19  ? 153 ASP A HA     1 
ATOM   2401  H  HB2    . ASP A 1 154 ? 23.899  40.441  5.801   1.00 32.77  ? 153 ASP A HB2    1 
ATOM   2402  H  HB3    . ASP A 1 154 ? 23.943  40.944  7.308   1.00 32.77  ? 153 ASP A HB3    1 
ATOM   2403  N  N      . ASP A 1 155 ? 21.031  41.586  6.080   1.00 22.30  ? 154 ASP A N      1 
ATOM   2404  C  CA     . ASP A 1 155 ? 20.185  42.772  6.206   1.00 29.14  ? 154 ASP A CA     1 
ATOM   2405  C  C      . ASP A 1 155 ? 18.892  42.426  6.933   1.00 26.76  ? 154 ASP A C      1 
ATOM   2406  O  O      . ASP A 1 155 ? 18.412  43.197  7.766   1.00 27.41  ? 154 ASP A O      1 
ATOM   2407  C  CB     . ASP A 1 155 ? 19.899  43.334  4.813   1.00 28.91  ? 154 ASP A CB     1 
ATOM   2408  C  CG     . ASP A 1 155 ? 19.218  44.698  4.818   1.00 34.24  ? 154 ASP A CG     1 
ATOM   2409  O  OD1    . ASP A 1 155 ? 19.265  45.464  5.810   1.00 37.19  ? 154 ASP A OD1    1 
ATOM   2410  O  OD2    . ASP A 1 155 ? 18.621  45.003  3.770   1.00 34.72  ? 154 ASP A OD2    1 
ATOM   2411  H  H      . ASP A 1 155 ? 21.259  41.401  5.271   1.00 26.79  ? 154 ASP A H      1 
ATOM   2412  H  HA     . ASP A 1 155 ? 20.642  43.458  6.717   1.00 35.01  ? 154 ASP A HA     1 
ATOM   2413  H  HB2    . ASP A 1 155 ? 20.739  43.427  4.337   1.00 34.73  ? 154 ASP A HB2    1 
ATOM   2414  H  HB3    . ASP A 1 155 ? 19.317  42.717  4.342   1.00 34.73  ? 154 ASP A HB3    1 
ATOM   2415  N  N      . ALA A 1 156 ? 18.312  41.265  6.631   1.00 21.88  ? 155 ALA A N      1 
ATOM   2416  C  CA     . ALA A 1 156 ? 17.023  40.936  7.238   1.00 25.55  ? 155 ALA A CA     1 
ATOM   2417  C  C      . ALA A 1 156 ? 17.170  40.753  8.744   1.00 25.36  ? 155 ALA A C      1 
ATOM   2418  O  O      . ALA A 1 156 ? 16.396  41.314  9.528   1.00 22.87  ? 155 ALA A O      1 
ATOM   2419  C  CB     . ALA A 1 156 ? 16.441  39.670  6.595   1.00 22.10  ? 155 ALA A CB     1 
ATOM   2420  H  H      . ALA A 1 156 ? 18.632  40.671  6.098   1.00 26.29  ? 155 ALA A H      1 
ATOM   2421  H  HA     . ALA A 1 156 ? 16.404  41.664  7.074   1.00 30.69  ? 155 ALA A HA     1 
ATOM   2422  H  HB1    . ALA A 1 156 ? 15.584  39.472  7.005   1.00 26.55  ? 155 ALA A HB1    1 
ATOM   2423  H  HB2    . ALA A 1 156 ? 16.324  39.823  5.644   1.00 26.55  ? 155 ALA A HB2    1 
ATOM   2424  H  HB3    . ALA A 1 156 ? 17.054  38.932  6.738   1.00 26.55  ? 155 ALA A HB3    1 
ATOM   2425  N  N      . PHE A 1 157 ? 18.139  39.945  9.168   1.00 21.22  ? 156 PHE A N      1 
ATOM   2426  C  CA     . PHE A 1 157 ? 18.350  39.722  10.600  1.00 22.81  ? 156 PHE A CA     1 
ATOM   2427  C  C      . PHE A 1 157 ? 18.844  40.973  11.304  1.00 25.87  ? 156 PHE A C      1 
ATOM   2428  O  O      . PHE A 1 157 ? 18.381  41.279  12.412  1.00 23.66  ? 156 PHE A O      1 
ATOM   2429  C  CB     . PHE A 1 157 ? 19.311  38.559  10.804  1.00 22.19  ? 156 PHE A CB     1 
ATOM   2430  C  CG     . PHE A 1 157 ? 18.680  37.229  10.538  1.00 20.34  ? 156 PHE A CG     1 
ATOM   2431  C  CD1    . PHE A 1 157 ? 17.885  36.617  11.489  1.00 20.20  ? 156 PHE A CD1    1 
ATOM   2432  C  CD2    . PHE A 1 157 ? 18.868  36.594  9.316   1.00 21.00  ? 156 PHE A CD2    1 
ATOM   2433  C  CE1    . PHE A 1 157 ? 17.311  35.355  11.225  1.00 18.18  ? 156 PHE A CE1    1 
ATOM   2434  C  CE2    . PHE A 1 157 ? 18.276  35.369  9.037   1.00 18.48  ? 156 PHE A CE2    1 
ATOM   2435  C  CZ     . PHE A 1 157 ? 17.491  34.752  10.006  1.00 21.24  ? 156 PHE A CZ     1 
ATOM   2436  H  H      . PHE A 1 157 ? 18.683  39.518  8.656   1.00 25.50  ? 156 PHE A H      1 
ATOM   2437  H  HA     . PHE A 1 157 ? 17.501  39.485  11.005  1.00 27.41  ? 156 PHE A HA     1 
ATOM   2438  H  HB2    . PHE A 1 157 ? 20.062  38.661  10.199  1.00 26.67  ? 156 PHE A HB2    1 
ATOM   2439  H  HB3    . PHE A 1 157 ? 19.622  38.565  11.723  1.00 26.67  ? 156 PHE A HB3    1 
ATOM   2440  H  HD1    . PHE A 1 157 ? 17.727  37.037  12.304  1.00 24.28  ? 156 PHE A HD1    1 
ATOM   2441  H  HD2    . PHE A 1 157 ? 19.401  36.999  8.670   1.00 25.23  ? 156 PHE A HD2    1 
ATOM   2442  H  HE1    . PHE A 1 157 ? 16.808  34.930  11.881  1.00 21.86  ? 156 PHE A HE1    1 
ATOM   2443  H  HE2    . PHE A 1 157 ? 18.402  34.965  8.209   1.00 22.21  ? 156 PHE A HE2    1 
ATOM   2444  H  HZ     . PHE A 1 157 ? 17.090  33.932  9.828   1.00 25.52  ? 156 PHE A HZ     1 
ATOM   2445  N  N      . TYR A 1 158 ? 19.780  41.708  10.701  1.00 22.59  ? 157 TYR A N      1 
ATOM   2446  C  CA     . TYR A 1 158 ? 20.262  42.932  11.346  1.00 29.26  ? 157 TYR A CA     1 
ATOM   2447  C  C      . TYR A 1 158 ? 19.161  43.983  11.450  1.00 27.57  ? 157 TYR A C      1 
ATOM   2448  O  O      . TYR A 1 158 ? 19.081  44.708  12.450  1.00 28.33  ? 157 TYR A O      1 
ATOM   2449  C  CB     . TYR A 1 158 ? 21.466  43.523  10.600  1.00 25.28  ? 157 TYR A CB     1 
ATOM   2450  C  CG     . TYR A 1 158 ? 22.749  42.723  10.644  1.00 27.51  ? 157 TYR A CG     1 
ATOM   2451  C  CD1    . TYR A 1 158 ? 22.778  41.417  11.099  1.00 23.73  ? 157 TYR A CD1    1 
ATOM   2452  C  CD2    . TYR A 1 158 ? 23.946  43.269  10.163  1.00 29.27  ? 157 TYR A CD2    1 
ATOM   2453  C  CE1    . TYR A 1 158 ? 23.949  40.682  11.098  1.00 29.39  ? 157 TYR A CE1    1 
ATOM   2454  C  CE2    . TYR A 1 158 ? 25.126  42.542  10.174  1.00 31.84  ? 157 TYR A CE2    1 
ATOM   2455  C  CZ     . TYR A 1 158 ? 25.124  41.250  10.638  1.00 31.21  ? 157 TYR A CZ     1 
ATOM   2456  O  OH     . TYR A 1 158 ? 26.285  40.502  10.631  1.00 35.03  ? 157 TYR A OH     1 
ATOM   2457  H  H      . TYR A 1 158 ? 20.143  41.527  9.942   1.00 27.15  ? 157 TYR A H      1 
ATOM   2458  H  HA     . TYR A 1 158 ? 20.554  42.690  12.239  1.00 35.14  ? 157 TYR A HA     1 
ATOM   2459  H  HB2    . TYR A 1 158 ? 21.223  43.619  9.665   1.00 30.37  ? 157 TYR A HB2    1 
ATOM   2460  H  HB3    . TYR A 1 158 ? 21.661  44.393  10.983  1.00 30.37  ? 157 TYR A HB3    1 
ATOM   2461  H  HD1    . TYR A 1 158 ? 21.994  41.025  11.412  1.00 28.51  ? 157 TYR A HD1    1 
ATOM   2462  H  HD2    . TYR A 1 158 ? 23.949  44.138  9.831   1.00 35.15  ? 157 TYR A HD2    1 
ATOM   2463  H  HE1    . TYR A 1 158 ? 23.947  39.805  11.407  1.00 35.30  ? 157 TYR A HE1    1 
ATOM   2464  H  HE2    . TYR A 1 158 ? 25.916  42.927  9.868   1.00 38.24  ? 157 TYR A HE2    1 
ATOM   2465  H  HH     . TYR A 1 158 ? 26.921  40.961  10.329  1.00 42.07  ? 157 TYR A HH     1 
ATOM   2466  N  N      . THR A 1 159 ? 18.288  44.075  10.444  1.00 24.54  ? 158 THR A N      1 
ATOM   2467  C  CA     . THR A 1 159 ? 17.232  45.065  10.479  1.00 26.88  ? 158 THR A CA     1 
ATOM   2468  C  C      . THR A 1 159 ? 16.284  44.743  11.621  1.00 29.44  ? 158 THR A C      1 
ATOM   2469  O  O      . THR A 1 159 ? 15.916  45.623  12.400  1.00 30.79  ? 158 THR A O      1 
ATOM   2470  C  CB     . THR A 1 159 ? 16.482  45.109  9.142   1.00 30.59  ? 158 THR A CB     1 
ATOM   2471  O  OG1    . THR A 1 159 ? 17.347  45.613  8.117   1.00 30.87  ? 158 THR A OG1    1 
ATOM   2472  C  CG2    . THR A 1 159 ? 15.243  46.024  9.203   1.00 28.88  ? 158 THR A CG2    1 
ATOM   2473  H  H      . THR A 1 159 ? 18.293  43.579  9.741   1.00 29.48  ? 158 THR A H      1 
ATOM   2474  H  HA     . THR A 1 159 ? 17.612  45.947  10.613  1.00 32.28  ? 158 THR A HA     1 
ATOM   2475  H  HB     . THR A 1 159 ? 16.189  44.208  8.936   1.00 36.74  ? 158 THR A HB     1 
ATOM   2476  H  HG1    . THR A 1 159 ? 18.015  45.111  8.032   1.00 37.08  ? 158 THR A HG1    1 
ATOM   2477  H  HG21   . THR A 1 159 ? 14.905  46.186  8.308   1.00 34.69  ? 158 THR A HG21   1 
ATOM   2478  H  HG22   . THR A 1 159 ? 14.546  45.604  9.731   1.00 34.69  ? 158 THR A HG22   1 
ATOM   2479  H  HG23   . THR A 1 159 ? 15.477  46.873  9.610   1.00 34.69  ? 158 THR A HG23   1 
ATOM   2480  N  N      . LEU A 1 160 ? 15.955  43.456  11.781  1.00 27.40  ? 159 LEU A N      1 
ATOM   2481  C  CA     . LEU A 1 160 ? 15.094  43.054  12.895  1.00 23.55  ? 159 LEU A CA     1 
ATOM   2482  C  C      . LEU A 1 160 ? 15.699  43.467  14.233  1.00 28.92  ? 159 LEU A C      1 
ATOM   2483  O  O      . LEU A 1 160 ? 14.986  43.998  15.108  1.00 29.89  ? 159 LEU A O      1 
ATOM   2484  C  CB     . LEU A 1 160 ? 14.853  41.538  12.829  1.00 22.25  ? 159 LEU A CB     1 
ATOM   2485  C  CG     . LEU A 1 160 ? 13.942  40.966  13.933  1.00 21.38  ? 159 LEU A CG     1 
ATOM   2486  C  CD1    . LEU A 1 160 ? 12.642  41.766  13.994  1.00 23.66  ? 159 LEU A CD1    1 
ATOM   2487  C  CD2    . LEU A 1 160 ? 13.644  39.472  13.709  1.00 21.22  ? 159 LEU A CD2    1 
ATOM   2488  H  H      . LEU A 1 160 ? 16.210  42.813  11.271  1.00 32.92  ? 159 LEU A H      1 
ATOM   2489  H  HA     . LEU A 1 160 ? 14.234  43.496  12.821  1.00 28.29  ? 159 LEU A HA     1 
ATOM   2490  H  HB2    . LEU A 1 160 ? 14.440  41.331  11.976  1.00 26.73  ? 159 LEU A HB2    1 
ATOM   2491  H  HB3    . LEU A 1 160 ? 15.711  41.089  12.900  1.00 26.73  ? 159 LEU A HB3    1 
ATOM   2492  H  HG     . LEU A 1 160 ? 14.402  41.041  14.784  1.00 25.69  ? 159 LEU A HG     1 
ATOM   2493  H  HD11   . LEU A 1 160 ? 12.000  41.284  14.539  1.00 28.42  ? 159 LEU A HD11   1 
ATOM   2494  H  HD12   . LEU A 1 160 ? 12.823  42.635  14.386  1.00 28.42  ? 159 LEU A HD12   1 
ATOM   2495  H  HD13   . LEU A 1 160 ? 12.295  41.875  13.094  1.00 28.42  ? 159 LEU A HD13   1 
ATOM   2496  H  HD21   . LEU A 1 160 ? 13.130  39.137  14.460  1.00 25.50  ? 159 LEU A HD21   1 
ATOM   2497  H  HD22   . LEU A 1 160 ? 13.135  39.371  12.889  1.00 25.50  ? 159 LEU A HD22   1 
ATOM   2498  H  HD23   . LEU A 1 160 ? 14.482  38.990  13.640  1.00 25.50  ? 159 LEU A HD23   1 
ATOM   2499  N  N      . VAL A 1 161 ? 17.007  43.271  14.411  1.00 25.43  ? 160 VAL A N      1 
ATOM   2500  C  CA     . VAL A 1 161 ? 17.638  43.715  15.654  1.00 29.72  ? 160 VAL A CA     1 
ATOM   2501  C  C      . VAL A 1 161 ? 17.460  45.218  15.828  1.00 34.39  ? 160 VAL A C      1 
ATOM   2502  O  O      . VAL A 1 161 ? 17.050  45.701  16.894  1.00 31.91  ? 160 VAL A O      1 
ATOM   2503  C  CB     . VAL A 1 161 ? 19.120  43.326  15.687  1.00 25.90  ? 160 VAL A CB     1 
ATOM   2504  C  CG1    . VAL A 1 161 ? 19.849  44.029  16.858  1.00 33.11  ? 160 VAL A CG1    1 
ATOM   2505  C  CG2    . VAL A 1 161 ? 19.276  41.825  15.798  1.00 28.54  ? 160 VAL A CG2    1 
ATOM   2506  H  H      . VAL A 1 161 ? 17.535  42.896  13.845  1.00 30.55  ? 160 VAL A H      1 
ATOM   2507  H  HA     . VAL A 1 161 ? 17.197  43.266  16.393  1.00 35.70  ? 160 VAL A HA     1 
ATOM   2508  H  HB     . VAL A 1 161 ? 19.531  43.616  14.858  1.00 31.11  ? 160 VAL A HB     1 
ATOM   2509  H  HG11   . VAL A 1 161 ? 20.685  43.568  17.033  1.00 39.76  ? 160 VAL A HG11   1 
ATOM   2510  H  HG12   . VAL A 1 161 ? 20.026  44.951  16.612  1.00 39.76  ? 160 VAL A HG12   1 
ATOM   2511  H  HG13   . VAL A 1 161 ? 19.284  43.999  17.646  1.00 39.76  ? 160 VAL A HG13   1 
ATOM   2512  H  HG21   . VAL A 1 161 ? 20.221  41.607  15.826  1.00 34.28  ? 160 VAL A HG21   1 
ATOM   2513  H  HG22   . VAL A 1 161 ? 18.843  41.522  16.611  1.00 34.28  ? 160 VAL A HG22   1 
ATOM   2514  H  HG23   . VAL A 1 161 ? 18.862  41.407  15.027  1.00 34.28  ? 160 VAL A HG23   1 
ATOM   2515  N  N      . ARG A 1 162 ? 17.739  45.983  14.773  1.00 30.70  ? 161 ARG A N      1 
ATOM   2516  C  CA     . ARG A 1 162 ? 17.538  47.432  14.867  1.00 34.95  ? 161 ARG A CA     1 
ATOM   2517  C  C      . ARG A 1 162 ? 16.121  47.762  15.305  1.00 36.26  ? 161 ARG A C      1 
ATOM   2518  O  O      . ARG A 1 162 ? 15.920  48.660  16.134  1.00 39.75  ? 161 ARG A O      1 
ATOM   2519  C  CB     . ARG A 1 162 ? 17.879  48.110  13.537  1.00 33.79  ? 161 ARG A CB     1 
ATOM   2520  C  CG     . ARG A 1 162 ? 19.373  48.107  13.249  1.00 34.53  ? 161 ARG A CG     1 
ATOM   2521  C  CD     . ARG A 1 162 ? 19.759  48.976  12.062  1.00 35.24  ? 161 ARG A CD     1 
ATOM   2522  N  NE     . ARG A 1 162 ? 21.148  48.741  11.678  1.00 35.36  ? 161 ARG A NE     1 
ATOM   2523  C  CZ     . ARG A 1 162 ? 21.523  47.976  10.663  1.00 32.60  ? 161 ARG A CZ     1 
ATOM   2524  N  NH1    . ARG A 1 162 ? 20.636  47.374  9.884   1.00 37.96  ? 161 ARG A NH1    1 
ATOM   2525  N  NH2    . ARG A 1 162 ? 22.819  47.786  10.439  1.00 36.76  ? 161 ARG A NH2    1 
ATOM   2526  H  H      . ARG A 1 162 ? 18.036  45.700  14.017  1.00 36.87  ? 161 ARG A H      1 
ATOM   2527  H  HA     . ARG A 1 162 ? 18.146  47.790  15.533  1.00 41.97  ? 161 ARG A HA     1 
ATOM   2528  H  HB2    . ARG A 1 162 ? 17.432  47.637  12.817  1.00 40.58  ? 161 ARG A HB2    1 
ATOM   2529  H  HB3    . ARG A 1 162 ? 17.579  49.032  13.565  1.00 40.58  ? 161 ARG A HB3    1 
ATOM   2530  H  HG2    . ARG A 1 162 ? 19.844  48.441  14.028  1.00 41.47  ? 161 ARG A HG2    1 
ATOM   2531  H  HG3    . ARG A 1 162 ? 19.654  47.199  13.056  1.00 41.47  ? 161 ARG A HG3    1 
ATOM   2532  H  HD2    . ARG A 1 162 ? 19.190  48.762  11.305  1.00 42.33  ? 161 ARG A HD2    1 
ATOM   2533  H  HD3    . ARG A 1 162 ? 19.659  49.911  12.299  1.00 42.33  ? 161 ARG A HD3    1 
ATOM   2534  H  HE     . ARG A 1 162 ? 21.763  49.125  12.141  1.00 42.46  ? 161 ARG A HE     1 
ATOM   2535  H  HH11   . ARG A 1 162 ? 19.795  47.475  10.033  1.00 45.58  ? 161 ARG A HH11   1 
ATOM   2536  H  HH12   . ARG A 1 162 ? 20.901  46.881  9.231   1.00 45.58  ? 161 ARG A HH12   1 
ATOM   2537  H  HH21   . ARG A 1 162 ? 23.403  48.157  10.949  1.00 44.14  ? 161 ARG A HH21   1 
ATOM   2538  H  HH22   . ARG A 1 162 ? 23.074  47.291  9.783   1.00 44.14  ? 161 ARG A HH22   1 
ATOM   2539  N  N      . GLU A 1 163 ? 15.121  47.019  14.806  1.00 35.18  ? 162 GLU A N      1 
ATOM   2540  C  CA     . GLU A 1 163 ? 13.742  47.278  15.226  1.00 37.04  ? 162 GLU A CA     1 
ATOM   2541  C  C      . GLU A 1 163 ? 13.532  46.937  16.700  1.00 38.26  ? 162 GLU A C      1 
ATOM   2542  O  O      . GLU A 1 163 ? 12.795  47.637  17.411  1.00 38.64  ? 162 GLU A O      1 
ATOM   2543  C  CB     . GLU A 1 163 ? 12.745  46.500  14.369  1.00 38.34  ? 162 GLU A CB     1 
ATOM   2544  C  CG     . GLU A 1 163 ? 12.727  46.893  12.891  1.00 33.71  ? 162 GLU A CG     1 
ATOM   2545  C  CD     . GLU A 1 163 ? 12.133  48.264  12.641  1.00 37.20  ? 162 GLU A CD     1 
ATOM   2546  O  OE1    . GLU A 1 163 ? 10.918  48.455  12.860  1.00 39.08  ? 162 GLU A OE1    1 
ATOM   2547  O  OE2    . GLU A 1 163 ? 12.913  49.138  12.223  1.00 41.44  ? 162 GLU A OE2    1 
ATOM   2548  H  H      . GLU A 1 163 ? 15.214  46.379  14.239  1.00 42.24  ? 162 GLU A H      1 
ATOM   2549  H  HA     . GLU A 1 163 ? 13.570  48.224  15.096  1.00 44.48  ? 162 GLU A HA     1 
ATOM   2550  H  HB2    . GLU A 1 163 ? 12.967  45.557  14.418  1.00 46.04  ? 162 GLU A HB2    1 
ATOM   2551  H  HB3    . GLU A 1 163 ? 11.853  46.650  14.721  1.00 46.04  ? 162 GLU A HB3    1 
ATOM   2552  H  HG2    . GLU A 1 163 ? 13.638  46.898  12.557  1.00 40.49  ? 162 GLU A HG2    1 
ATOM   2553  H  HG3    . GLU A 1 163 ? 12.198  46.245  12.401  1.00 40.49  ? 162 GLU A HG3    1 
ATOM   2554  N  N      . ILE A 1 164 ? 14.174  45.877  17.189  1.00 33.71  ? 163 ILE A N      1 
ATOM   2555  C  CA     . ILE A 1 164 ? 14.069  45.567  18.616  1.00 36.74  ? 163 ILE A CA     1 
ATOM   2556  C  C      . ILE A 1 164 ? 14.671  46.698  19.451  1.00 41.65  ? 163 ILE A C      1 
ATOM   2557  O  O      . ILE A 1 164 ? 14.022  47.229  20.362  1.00 45.54  ? 163 ILE A O      1 
ATOM   2558  C  CB     . ILE A 1 164 ? 14.722  44.210  18.926  1.00 33.52  ? 163 ILE A CB     1 
ATOM   2559  C  CG1    . ILE A 1 164 ? 13.964  43.085  18.209  1.00 29.68  ? 163 ILE A CG1    1 
ATOM   2560  C  CG2    . ILE A 1 164 ? 14.698  43.934  20.418  1.00 35.52  ? 163 ILE A CG2    1 
ATOM   2561  C  CD1    . ILE A 1 164 ? 14.606  41.680  18.355  1.00 26.75  ? 163 ILE A CD1    1 
ATOM   2562  H  H      . ILE A 1 164 ? 14.663  45.338  16.732  1.00 40.49  ? 163 ILE A H      1 
ATOM   2563  H  HA     . ILE A 1 164 ? 13.129  45.497  18.849  1.00 44.13  ? 163 ILE A HA     1 
ATOM   2564  H  HB     . ILE A 1 164 ? 15.640  44.244  18.615  1.00 40.26  ? 163 ILE A HB     1 
ATOM   2565  H  HG12   . ILE A 1 164 ? 13.066  43.036  18.573  1.00 35.65  ? 163 ILE A HG12   1 
ATOM   2566  H  HG13   . ILE A 1 164 ? 13.926  43.292  17.262  1.00 35.65  ? 163 ILE A HG13   1 
ATOM   2567  H  HG21   . ILE A 1 164 ? 15.008  43.029  20.577  1.00 42.66  ? 163 ILE A HG21   1 
ATOM   2568  H  HG22   . ILE A 1 164 ? 15.281  44.567  20.866  1.00 42.66  ? 163 ILE A HG22   1 
ATOM   2569  H  HG23   . ILE A 1 164 ? 13.790  44.035  20.743  1.00 42.66  ? 163 ILE A HG23   1 
ATOM   2570  H  HD11   . ILE A 1 164 ? 14.196  41.077  17.715  1.00 32.13  ? 163 ILE A HD11   1 
ATOM   2571  H  HD12   . ILE A 1 164 ? 15.558  41.748  18.183  1.00 32.13  ? 163 ILE A HD12   1 
ATOM   2572  H  HD13   . ILE A 1 164 ? 14.455  41.356  19.257  1.00 32.13  ? 163 ILE A HD13   1 
ATOM   2573  N  N      . ARG A 1 165 ? 15.913  47.094  19.135  1.00 39.04  ? 164 ARG A N      1 
ATOM   2574  C  CA     . ARG A 1 165 ? 16.555  48.211  19.836  1.00 45.10  ? 164 ARG A CA     1 
ATOM   2575  C  C      . ARG A 1 165 ? 15.625  49.415  19.909  1.00 48.68  ? 164 ARG A C      1 
ATOM   2576  O  O      . ARG A 1 165 ? 15.422  50.004  20.976  1.00 54.20  ? 164 ARG A O      1 
ATOM   2577  C  CB     . ARG A 1 165 ? 17.851  48.616  19.127  1.00 41.81  ? 164 ARG A CB     1 
ATOM   2578  C  CG     . ARG A 1 165 ? 18.989  47.632  19.232  1.00 43.84  ? 164 ARG A CG     1 
ATOM   2579  C  CD     . ARG A 1 165 ? 20.193  48.048  18.378  1.00 44.62  ? 164 ARG A CD     1 
ATOM   2580  N  NE     . ARG A 1 165 ? 21.352  47.183  18.609  1.00 46.15  ? 164 ARG A NE     1 
ATOM   2581  C  CZ     . ARG A 1 165 ? 22.501  47.274  17.952  1.00 45.90  ? 164 ARG A CZ     1 
ATOM   2582  N  NH1    . ARG A 1 165 ? 22.693  48.193  17.018  1.00 47.65  ? 164 ARG A NH1    1 
ATOM   2583  N  NH2    . ARG A 1 165 ? 23.488  46.430  18.247  1.00 46.55  ? 164 ARG A NH2    1 
ATOM   2584  H  H      . ARG A 1 165 ? 16.400  46.735  18.524  1.00 46.89  ? 164 ARG A H      1 
ATOM   2585  H  HA     . ARG A 1 165 ? 16.773  47.918  20.734  1.00 54.16  ? 164 ARG A HA     1 
ATOM   2586  H  HB2    . ARG A 1 165 ? 17.658  48.733  18.184  1.00 50.21  ? 164 ARG A HB2    1 
ATOM   2587  H  HB3    . ARG A 1 165 ? 18.159  49.452  19.510  1.00 50.21  ? 164 ARG A HB3    1 
ATOM   2588  H  HG2    . ARG A 1 165 ? 19.279  47.576  20.156  1.00 52.64  ? 164 ARG A HG2    1 
ATOM   2589  H  HG3    . ARG A 1 165 ? 18.688  46.762  18.926  1.00 52.64  ? 164 ARG A HG3    1 
ATOM   2590  H  HD2    . ARG A 1 165 ? 19.954  47.991  17.440  1.00 53.58  ? 164 ARG A HD2    1 
ATOM   2591  H  HD3    . ARG A 1 165 ? 20.444  48.958  18.602  1.00 53.58  ? 164 ARG A HD3    1 
ATOM   2592  H  HE     . ARG A 1 165 ? 21.284  46.574  19.212  1.00 55.41  ? 164 ARG A HE     1 
ATOM   2593  H  HH11   . ARG A 1 165 ? 22.065  48.748  16.825  1.00 57.21  ? 164 ARG A HH11   1 
ATOM   2594  H  HH12   . ARG A 1 165 ? 23.446  48.235  16.604  1.00 57.21  ? 164 ARG A HH12   1 
ATOM   2595  H  HH21   . ARG A 1 165 ? 23.377  45.835  18.857  1.00 55.90  ? 164 ARG A HH21   1 
ATOM   2596  H  HH22   . ARG A 1 165 ? 24.237  46.481  17.827  1.00 55.90  ? 164 ARG A HH22   1 
ATOM   2597  N  N      . LYS A 1 166 ? 15.041  49.777  18.765  1.00 47.47  ? 165 LYS A N      1 
ATOM   2598  C  CA     . LYS A 1 166 ? 14.155  50.929  18.676  1.00 50.23  ? 165 LYS A CA     1 
ATOM   2599  C  C      . LYS A 1 166 ? 12.960  50.793  19.608  1.00 52.69  ? 165 LYS A C      1 
ATOM   2600  O  O      . LYS A 1 166 ? 12.609  51.732  20.326  1.00 58.17  ? 165 LYS A O      1 
ATOM   2601  C  CB     . LYS A 1 166 ? 13.669  51.084  17.237  1.00 46.10  ? 165 LYS A CB     1 
ATOM   2602  C  CG     . LYS A 1 166 ? 14.490  52.037  16.401  1.00 51.05  ? 165 LYS A CG     1 
ATOM   2603  C  CD     . LYS A 1 166 ? 14.189  51.874  14.911  1.00 49.33  ? 165 LYS A CD     1 
ATOM   2604  C  CE     . LYS A 1 166 ? 12.692  52.015  14.613  1.00 52.18  ? 165 LYS A CE     1 
ATOM   2605  N  NZ     . LYS A 1 166 ? 12.375  51.853  13.155  1.00 57.86  ? 165 LYS A NZ     1 
ATOM   2606  H  H      . LYS A 1 166 ? 15.145  49.364  18.017  1.00 57.00  ? 165 LYS A H      1 
ATOM   2607  H  HA     . LYS A 1 166 ? 14.652  51.720  18.937  1.00 60.31  ? 165 LYS A HA     1 
ATOM   2608  H  HB2    . LYS A 1 166 ? 13.698  50.216  16.805  1.00 55.35  ? 165 LYS A HB2    1 
ATOM   2609  H  HB3    . LYS A 1 166 ? 12.758  51.417  17.252  1.00 55.35  ? 165 LYS A HB3    1 
ATOM   2610  H  HG2    . LYS A 1 166 ? 14.283  52.950  16.656  1.00 61.30  ? 165 LYS A HG2    1 
ATOM   2611  H  HG3    . LYS A 1 166 ? 15.433  51.859  16.543  1.00 61.30  ? 165 LYS A HG3    1 
ATOM   2612  H  HD2    . LYS A 1 166 ? 14.663  52.556  14.412  1.00 59.23  ? 165 LYS A HD2    1 
ATOM   2613  H  HD3    . LYS A 1 166 ? 14.473  50.993  14.622  1.00 59.23  ? 165 LYS A HD3    1 
ATOM   2614  H  HE2    . LYS A 1 166 ? 12.205  51.334  15.103  1.00 62.65  ? 165 LYS A HE2    1 
ATOM   2615  H  HE3    . LYS A 1 166 ? 12.396  52.897  14.888  1.00 62.65  ? 165 LYS A HE3    1 
ATOM   2616  H  HZ1    . LYS A 1 166 ? 11.499  51.939  13.022  1.00 69.47  ? 165 LYS A HZ1    1 
ATOM   2617  H  HZ2    . LYS A 1 166 ? 12.801  52.473  12.680  1.00 69.47  ? 165 LYS A HZ2    1 
ATOM   2618  H  HZ3    . LYS A 1 166 ? 12.631  51.048  12.876  1.00 69.47  ? 165 LYS A HZ3    1 
ATOM   2619  N  N      . HIS A 1 167 ? 12.286  49.644  19.564  1.00 51.62  ? 166 HIS A N      1 
ATOM   2620  C  CA     . HIS A 1 167 ? 11.089  49.445  20.373  1.00 54.77  ? 166 HIS A CA     1 
ATOM   2621  C  C      . HIS A 1 167 ? 11.413  49.450  21.861  1.00 57.04  ? 166 HIS A C      1 
ATOM   2622  O  O      . HIS A 1 167 ? 10.557  49.805  22.673  1.00 59.88  ? 166 HIS A O      1 
ATOM   2623  C  CB     . HIS A 1 167 ? 10.422  48.136  19.950  1.00 50.05  ? 166 HIS A CB     1 
ATOM   2624  C  CG     . HIS A 1 167 ? 9.368   47.647  20.887  1.00 50.42  ? 166 HIS A CG     1 
ATOM   2625  N  ND1    . HIS A 1 167 ? 9.662   47.011  22.074  1.00 50.94  ? 166 HIS A ND1    1 
ATOM   2626  C  CD2    . HIS A 1 167 ? 8.018   47.664  20.793  1.00 47.66  ? 166 HIS A CD2    1 
ATOM   2627  C  CE1    . HIS A 1 167 ? 8.537   46.670  22.676  1.00 51.86  ? 166 HIS A CE1    1 
ATOM   2628  N  NE2    . HIS A 1 167 ? 7.525   47.055  21.920  1.00 47.97  ? 166 HIS A NE2    1 
ATOM   2629  H  H      . HIS A 1 167 ? 12.501  48.968  19.078  1.00 61.97  ? 166 HIS A H      1 
ATOM   2630  H  HA     . HIS A 1 167 ? 10.459  50.167  20.220  1.00 65.76  ? 166 HIS A HA     1 
ATOM   2631  H  HB2    . HIS A 1 167 ? 10.006  48.266  19.084  1.00 60.09  ? 166 HIS A HB2    1 
ATOM   2632  H  HB3    . HIS A 1 167 ? 11.103  47.447  19.891  1.00 60.09  ? 166 HIS A HB3    1 
ATOM   2633  H  HD2    . HIS A 1 167 ? 7.518   48.021  20.094  1.00 57.23  ? 166 HIS A HD2    1 
ATOM   2634  H  HE1    . HIS A 1 167 ? 8.469   46.233  23.494  1.00 62.27  ? 166 HIS A HE1    1 
ATOM   2635  H  HE2    . HIS A 1 167 ? 6.692   46.943  22.104  1.00 57.59  ? 166 HIS A HE2    1 
ATOM   2636  N  N      . LYS A 1 168 ? 12.634  49.064  22.232  1.00 57.72  ? 167 LYS A N      1 
ATOM   2637  C  CA     . LYS A 1 168 ? 13.115  49.206  23.599  1.00 62.20  ? 167 LYS A CA     1 
ATOM   2638  C  C      . LYS A 1 168 ? 13.590  50.619  23.918  1.00 69.40  ? 167 LYS A C      1 
ATOM   2639  O  O      . LYS A 1 168 ? 13.912  50.898  25.078  1.00 72.22  ? 167 LYS A O      1 
ATOM   2640  C  CB     . LYS A 1 168 ? 14.267  48.231  23.847  1.00 58.39  ? 167 LYS A CB     1 
ATOM   2641  C  CG     . LYS A 1 168 ? 13.894  46.790  23.604  1.00 57.88  ? 167 LYS A CG     1 
ATOM   2642  C  CD     . LYS A 1 168 ? 14.869  45.825  24.263  1.00 54.10  ? 167 LYS A CD     1 
ATOM   2643  C  CE     . LYS A 1 168 ? 16.128  45.653  23.429  1.00 51.21  ? 167 LYS A CE     1 
ATOM   2644  N  NZ     . LYS A 1 168 ? 17.275  45.050  24.185  1.00 45.92  ? 167 LYS A NZ     1 
ATOM   2645  H  H      . LYS A 1 168 ? 13.210  48.711  21.700  1.00 69.30  ? 167 LYS A H      1 
ATOM   2646  H  HA     . LYS A 1 168 ? 12.389  48.987  24.204  1.00 74.67  ? 167 LYS A HA     1 
ATOM   2647  H  HB2    . LYS A 1 168 ? 14.999  48.453  23.252  1.00 70.10  ? 167 LYS A HB2    1 
ATOM   2648  H  HB3    . LYS A 1 168 ? 14.553  48.313  24.771  1.00 70.10  ? 167 LYS A HB3    1 
ATOM   2649  H  HG2    . LYS A 1 168 ? 13.011  46.623  23.970  1.00 69.49  ? 167 LYS A HG2    1 
ATOM   2650  H  HG3    . LYS A 1 168 ? 13.896  46.616  22.650  1.00 69.49  ? 167 LYS A HG3    1 
ATOM   2651  H  HD2    . LYS A 1 168 ? 15.123  46.169  25.133  1.00 64.95  ? 167 LYS A HD2    1 
ATOM   2652  H  HD3    . LYS A 1 168 ? 14.446  44.957  24.360  1.00 64.95  ? 167 LYS A HD3    1 
ATOM   2653  H  HE2    . LYS A 1 168 ? 15.930  45.071  22.679  1.00 61.48  ? 167 LYS A HE2    1 
ATOM   2654  H  HE3    . LYS A 1 168 ? 16.411  46.524  23.108  1.00 61.48  ? 167 LYS A HE3    1 
ATOM   2655  H  HZ1    . LYS A 1 168 ? 17.985  44.978  23.654  1.00 55.14  ? 167 LYS A HZ1    1 
ATOM   2656  H  HZ2    . LYS A 1 168 ? 17.485  45.564  24.880  1.00 55.14  ? 167 LYS A HZ2    1 
ATOM   2657  H  HZ3    . LYS A 1 168 ? 17.052  44.240  24.481  1.00 55.14  ? 167 LYS A HZ3    1 
ATOM   2658  N  N      . GLU A 1 169 ? 13.645  51.503  22.925  1.00 77.15  ? 168 GLU A N      1 
ATOM   2659  C  CA     . GLU A 1 169 ? 14.169  52.861  23.073  1.00 75.44  ? 168 GLU A CA     1 
ATOM   2660  C  C      . GLU A 1 169 ? 15.555  52.852  23.726  1.00 79.47  ? 168 GLU A C      1 
ATOM   2661  O  O      . GLU A 1 169 ? 15.749  53.298  24.859  1.00 80.64  ? 168 GLU A O      1 
ATOM   2662  C  CB     . GLU A 1 169 ? 13.206  53.740  23.880  1.00 74.78  ? 168 GLU A CB     1 
ATOM   2663  C  CG     . GLU A 1 169 ? 11.906  54.040  23.170  1.00 76.21  ? 168 GLU A CG     1 
ATOM   2664  C  CD     . GLU A 1 169 ? 10.726  53.340  23.812  1.00 80.61  ? 168 GLU A CD     1 
ATOM   2665  O  OE1    . GLU A 1 169 ? 10.665  53.304  25.062  1.00 79.87  ? 168 GLU A OE1    1 
ATOM   2666  O  OE2    . GLU A 1 169 ? 9.875   52.805  23.063  1.00 82.26  ? 168 GLU A OE2    1 
ATOM   2667  H  H      . GLU A 1 169 ? 13.375  51.335  22.126  1.00 92.62  ? 168 GLU A H      1 
ATOM   2668  H  HA     . GLU A 1 169 ? 14.257  53.234  22.183  1.00 90.56  ? 168 GLU A HA     1 
ATOM   2669  H  HB2    . GLU A 1 169 ? 12.991  53.286  24.709  1.00 89.77  ? 168 GLU A HB2    1 
ATOM   2670  H  HB3    . GLU A 1 169 ? 13.641  54.586  24.068  1.00 89.77  ? 168 GLU A HB3    1 
ATOM   2671  H  HG2    . GLU A 1 169 ? 11.741  54.995  23.198  1.00 91.48  ? 168 GLU A HG2    1 
ATOM   2672  H  HG3    . GLU A 1 169 ? 11.970  53.741  22.250  1.00 91.48  ? 168 GLU A HG3    1 
ATOM   2673  N  N      . LYS A 1 170 ? 16.519  52.325  22.970  1.00 74.65  ? 169 LYS A N      1 
ATOM   2674  C  CA     . LYS A 1 170 ? 17.919  52.309  23.407  1.00 74.89  ? 169 LYS A CA     1 
ATOM   2675  C  C      . LYS A 1 170 ? 18.870  52.451  22.215  1.00 72.72  ? 169 LYS A C      1 
ATOM   2676  O  O      . LYS A 1 170 ? 18.986  51.550  21.376  1.00 66.71  ? 169 LYS A O      1 
ATOM   2677  C  CB     . LYS A 1 170 ? 18.226  51.020  24.188  1.00 73.31  ? 169 LYS A CB     1 
ATOM   2678  C  CG     . LYS A 1 170 ? 17.020  50.441  24.932  1.00 71.13  ? 169 LYS A CG     1 
ATOM   2679  C  CD     . LYS A 1 170 ? 17.408  49.367  25.947  1.00 70.72  ? 169 LYS A CD     1 
ATOM   2680  C  CE     . LYS A 1 170 ? 16.353  49.258  27.057  1.00 72.48  ? 169 LYS A CE     1 
ATOM   2681  N  NZ     . LYS A 1 170 ? 16.875  48.679  28.330  1.00 75.61  ? 169 LYS A NZ     1 
ATOM   2682  H  H      . LYS A 1 170 ? 16.390  51.970  22.198  1.00 89.61  ? 169 LYS A H      1 
ATOM   2683  H  HA     . LYS A 1 170 ? 18.073  53.060  24.001  1.00 89.90  ? 169 LYS A HA     1 
ATOM   2684  H  HB2    . LYS A 1 170 ? 18.540  50.347  23.565  1.00 88.01  ? 169 LYS A HB2    1 
ATOM   2685  H  HB3    . LYS A 1 170 ? 18.914  51.211  24.845  1.00 88.01  ? 169 LYS A HB3    1 
ATOM   2686  H  HG2    . LYS A 1 170 ? 16.571  51.155  25.410  1.00 85.38  ? 169 LYS A HG2    1 
ATOM   2687  H  HG3    . LYS A 1 170 ? 16.415  50.040  24.289  1.00 85.38  ? 169 LYS A HG3    1 
ATOM   2688  H  HD2    . LYS A 1 170 ? 17.474  48.508  25.501  1.00 84.90  ? 169 LYS A HD2    1 
ATOM   2689  H  HD3    . LYS A 1 170 ? 18.258  49.596  26.353  1.00 84.90  ? 169 LYS A HD3    1 
ATOM   2690  H  HE2    . LYS A 1 170 ? 16.014  50.145  27.253  1.00 87.01  ? 169 LYS A HE2    1 
ATOM   2691  H  HE3    . LYS A 1 170 ? 15.632  48.688  26.747  1.00 87.01  ? 169 LYS A HE3    1 
ATOM   2692  H  HZ1    . LYS A 1 170 ? 16.226  48.649  28.939  1.00 90.76  ? 169 LYS A HZ1    1 
ATOM   2693  H  HZ2    . LYS A 1 170 ? 17.176  47.854  28.188  1.00 90.76  ? 169 LYS A HZ2    1 
ATOM   2694  H  HZ3    . LYS A 1 170 ? 17.541  49.180  28.641  1.00 90.76  ? 169 LYS A HZ3    1 
ATOM   2695  N  N      . VAL B 2 3   ? -1.213  -14.777 4.070   1.00 64.96  ? 2   VAL B N      1 
ATOM   2696  C  CA     . VAL B 2 3   ? -1.275  -14.170 5.395   1.00 63.77  ? 2   VAL B CA     1 
ATOM   2697  C  C      . VAL B 2 3   ? -0.333  -12.960 5.451   1.00 55.81  ? 2   VAL B C      1 
ATOM   2698  O  O      . VAL B 2 3   ? 0.634   -12.876 4.691   1.00 51.09  ? 2   VAL B O      1 
ATOM   2699  C  CB     . VAL B 2 3   ? -0.939  -15.194 6.491   1.00 62.96  ? 2   VAL B CB     1 
ATOM   2700  C  CG1    . VAL B 2 3   ? -1.455  -14.719 7.834   1.00 60.73  ? 2   VAL B CG1    1 
ATOM   2701  C  CG2    . VAL B 2 3   ? -1.545  -16.546 6.155   1.00 66.23  ? 2   VAL B CG2    1 
ATOM   2702  H  HA     . VAL B 2 3   ? -2.178  -13.859 5.565   1.00 76.55  ? 2   VAL B HA     1 
ATOM   2703  H  HB     . VAL B 2 3   ? 0.025   -15.289 6.544   1.00 75.59  ? 2   VAL B HB     1 
ATOM   2704  H  HG11   . VAL B 2 3   ? -1.289  -15.407 8.498   1.00 72.91  ? 2   VAL B HG11   1 
ATOM   2705  H  HG12   . VAL B 2 3   ? -0.993  -13.903 8.080   1.00 72.91  ? 2   VAL B HG12   1 
ATOM   2706  H  HG13   . VAL B 2 3   ? -2.408  -14.551 7.765   1.00 72.91  ? 2   VAL B HG13   1 
ATOM   2707  H  HG21   . VAL B 2 3   ? -1.504  -17.115 6.939   1.00 79.50  ? 2   VAL B HG21   1 
ATOM   2708  H  HG22   . VAL B 2 3   ? -2.468  -16.420 5.886   1.00 79.50  ? 2   VAL B HG22   1 
ATOM   2709  H  HG23   . VAL B 2 3   ? -1.041  -16.947 5.429   1.00 79.50  ? 2   VAL B HG23   1 
ATOM   2710  N  N      . ASN B 2 4   ? -0.648  -12.023 6.342   1.00 50.08  ? 3   ASN B N      1 
ATOM   2711  C  CA     . ASN B 2 4   ? 0.128   -10.789 6.475   1.00 39.31  ? 3   ASN B CA     1 
ATOM   2712  C  C      . ASN B 2 4   ? 1.578   -11.127 6.792   1.00 40.20  ? 3   ASN B C      1 
ATOM   2713  O  O      . ASN B 2 4   ? 1.830   -11.966 7.669   1.00 44.12  ? 3   ASN B O      1 
ATOM   2714  C  CB     . ASN B 2 4   ? -0.449  -9.928  7.593   1.00 36.21  ? 3   ASN B CB     1 
ATOM   2715  C  CG     . ASN B 2 4   ? -1.683  -9.150  7.165   1.00 31.57  ? 3   ASN B CG     1 
ATOM   2716  O  OD1    . ASN B 2 4   ? -1.974  -9.045  5.989   1.00 34.45  ? 3   ASN B OD1    1 
ATOM   2717  N  ND2    . ASN B 2 4   ? -2.411  -8.610  8.134   1.00 32.31  ? 3   ASN B ND2    1 
ATOM   2718  H  H      . ASN B 2 4   ? -1.312  -12.076 6.886   1.00 60.14  ? 3   ASN B H      1 
ATOM   2719  H  HA     . ASN B 2 4   ? 0.094   -10.290 5.644   1.00 47.20  ? 3   ASN B HA     1 
ATOM   2720  H  HB2    . ASN B 2 4   ? -0.699  -10.501 8.335   1.00 43.49  ? 3   ASN B HB2    1 
ATOM   2721  H  HB3    . ASN B 2 4   ? 0.223   -9.290  7.879   1.00 43.49  ? 3   ASN B HB3    1 
ATOM   2722  H  HD21   . ASN B 2 4   ? -3.118  -8.161  7.940   1.00 38.81  ? 3   ASN B HD21   1 
ATOM   2723  H  HD22   . ASN B 2 4   ? -2.176  -8.710  8.955   1.00 38.81  ? 3   ASN B HD22   1 
ATOM   2724  N  N      . PRO B 2 5   ? 2.547   -10.520 6.117   1.00 35.42  ? 4   PRO B N      1 
ATOM   2725  C  CA     . PRO B 2 5   ? 3.946   -10.832 6.403   1.00 37.28  ? 4   PRO B CA     1 
ATOM   2726  C  C      . PRO B 2 5   ? 4.405   -10.207 7.713   1.00 36.50  ? 4   PRO B C      1 
ATOM   2727  O  O      . PRO B 2 5   ? 3.757   -9.325  8.281   1.00 32.33  ? 4   PRO B O      1 
ATOM   2728  C  CB     . PRO B 2 5   ? 4.690   -10.235 5.208   1.00 35.86  ? 4   PRO B CB     1 
ATOM   2729  C  CG     . PRO B 2 5   ? 3.819   -9.129  4.746   1.00 37.95  ? 4   PRO B CG     1 
ATOM   2730  C  CD     . PRO B 2 5   ? 2.412   -9.618  4.959   1.00 36.19  ? 4   PRO B CD     1 
ATOM   2731  H  HA     . PRO B 2 5   ? 4.091   -11.790 6.433   1.00 44.77  ? 4   PRO B HA     1 
ATOM   2732  H  HB2    . PRO B 2 5   ? 5.557   -9.903  5.488   1.00 43.07  ? 4   PRO B HB2    1 
ATOM   2733  H  HB3    . PRO B 2 5   ? 4.799   -10.906 4.516   1.00 43.07  ? 4   PRO B HB3    1 
ATOM   2734  H  HG2    . PRO B 2 5   ? 3.992   -8.332  5.272   1.00 45.57  ? 4   PRO B HG2    1 
ATOM   2735  H  HG3    . PRO B 2 5   ? 3.985   -8.949  3.807   1.00 45.57  ? 4   PRO B HG3    1 
ATOM   2736  H  HD2    . PRO B 2 5   ? 1.816   -8.881  5.162   1.00 43.47  ? 4   PRO B HD2    1 
ATOM   2737  H  HD3    . PRO B 2 5   ? 2.091   -10.100 4.180   1.00 43.47  ? 4   PRO B HD3    1 
ATOM   2738  N  N      . THR B 2 6   ? 5.546   -10.693 8.196   1.00 33.36  ? 5   THR B N      1 
ATOM   2739  C  CA     . THR B 2 6   ? 6.152   -10.212 9.435   1.00 31.22  ? 5   THR B CA     1 
ATOM   2740  C  C      . THR B 2 6   ? 7.619   -9.909  9.148   1.00 31.90  ? 5   THR B C      1 
ATOM   2741  O  O      . THR B 2 6   ? 8.309   -10.721 8.520   1.00 35.72  ? 5   THR B O      1 
ATOM   2742  C  CB     . THR B 2 6   ? 5.992   -11.249 10.561  1.00 31.87  ? 5   THR B CB     1 
ATOM   2743  O  OG1    . THR B 2 6   ? 4.588   -11.490 10.800  1.00 33.40  ? 5   THR B OG1    1 
ATOM   2744  C  CG2    . THR B 2 6   ? 6.649   -10.733 11.850  1.00 36.24  ? 5   THR B CG2    1 
ATOM   2745  H  H      . THR B 2 6   ? 5.999   -11.317 7.814   1.00 40.06  ? 5   THR B H      1 
ATOM   2746  H  HA     . THR B 2 6   ? 5.728   -9.394  9.740   1.00 37.50  ? 5   THR B HA     1 
ATOM   2747  H  HB     . THR B 2 6   ? 6.421   -12.080 10.305  1.00 38.28  ? 5   THR B HB     1 
ATOM   2748  H  HG1    . THR B 2 6   ? 4.495   -12.073 11.397  1.00 40.11  ? 5   THR B HG1    1 
ATOM   2749  H  HG21   . THR B 2 6   ? 6.551   -11.389 12.558  1.00 43.52  ? 5   THR B HG21   1 
ATOM   2750  H  HG22   . THR B 2 6   ? 7.594   -10.572 11.700  1.00 43.52  ? 5   THR B HG22   1 
ATOM   2751  H  HG23   . THR B 2 6   ? 6.229   -9.905  12.129  1.00 43.52  ? 5   THR B HG23   1 
ATOM   2752  N  N      . VAL B 2 7   ? 8.078   -8.727  9.573   1.00 28.09  ? 6   VAL B N      1 
ATOM   2753  C  CA     . VAL B 2 7   ? 9.457   -8.306  9.401   1.00 28.97  ? 6   VAL B CA     1 
ATOM   2754  C  C      . VAL B 2 7   ? 10.037  -7.958  10.772  1.00 25.74  ? 6   VAL B C      1 
ATOM   2755  O  O      . VAL B 2 7   ? 9.313   -7.664  11.721  1.00 26.44  ? 6   VAL B O      1 
ATOM   2756  C  CB     . VAL B 2 7   ? 9.583   -7.112  8.450   1.00 27.36  ? 6   VAL B CB     1 
ATOM   2757  C  CG1    . VAL B 2 7   ? 9.198   -7.499  7.011   1.00 26.86  ? 6   VAL B CG1    1 
ATOM   2758  C  CG2    . VAL B 2 7   ? 8.701   -6.007  8.897   1.00 28.97  ? 6   VAL B CG2    1 
ATOM   2759  H  H      . VAL B 2 7   ? 7.591   -8.142  9.974   1.00 33.74  ? 6   VAL B H      1 
ATOM   2760  H  HA     . VAL B 2 7   ? 9.968   -9.043  9.031   1.00 34.80  ? 6   VAL B HA     1 
ATOM   2761  H  HB     . VAL B 2 7   ? 10.509  -6.821  8.458   1.00 32.87  ? 6   VAL B HB     1 
ATOM   2762  H  HG11   . VAL B 2 7   ? 9.295   -6.722  6.438   1.00 32.27  ? 6   VAL B HG11   1 
ATOM   2763  H  HG12   . VAL B 2 7   ? 9.786   -8.208  6.707   1.00 32.27  ? 6   VAL B HG12   1 
ATOM   2764  H  HG13   . VAL B 2 7   ? 8.278   -7.804  7.001   1.00 32.27  ? 6   VAL B HG13   1 
ATOM   2765  H  HG21   . VAL B 2 7   ? 8.820   -5.249  8.304   1.00 34.80  ? 6   VAL B HG21   1 
ATOM   2766  H  HG22   . VAL B 2 7   ? 7.779   -6.308  8.868   1.00 34.80  ? 6   VAL B HG22   1 
ATOM   2767  H  HG23   . VAL B 2 7   ? 8.940   -5.759  9.804   1.00 34.80  ? 6   VAL B HG23   1 
ATOM   2768  N  N      . PHE B 2 8   ? 11.350  -7.989  10.860  1.00 27.98  ? 7   PHE B N      1 
ATOM   2769  C  CA     . PHE B 2 8   ? 12.067  -7.699  12.095  1.00 27.61  ? 7   PHE B CA     1 
ATOM   2770  C  C      . PHE B 2 8   ? 13.116  -6.636  11.838  1.00 27.28  ? 7   PHE B C      1 
ATOM   2771  O  O      . PHE B 2 8   ? 13.681  -6.551  10.749  1.00 25.11  ? 7   PHE B O      1 
ATOM   2772  C  CB     . PHE B 2 8   ? 12.766  -8.976  12.686  1.00 26.48  ? 7   PHE B CB     1 
ATOM   2773  C  CG     . PHE B 2 8   ? 13.980  -9.385  11.926  1.00 26.82  ? 7   PHE B CG     1 
ATOM   2774  C  CD1    . PHE B 2 8   ? 15.213  -8.844  12.238  1.00 30.59  ? 7   PHE B CD1    1 
ATOM   2775  C  CD2    . PHE B 2 8   ? 13.900  -10.320 10.900  1.00 32.87  ? 7   PHE B CD2    1 
ATOM   2776  C  CE1    . PHE B 2 8   ? 16.338  -9.200  11.546  1.00 30.97  ? 7   PHE B CE1    1 
ATOM   2777  C  CE2    . PHE B 2 8   ? 15.030  -10.682 10.195  1.00 34.06  ? 7   PHE B CE2    1 
ATOM   2778  C  CZ     . PHE B 2 8   ? 16.257  -10.108 10.518  1.00 31.47  ? 7   PHE B CZ     1 
ATOM   2779  H  H      . PHE B 2 8   ? 11.868  -8.181  10.201  1.00 33.61  ? 7   PHE B H      1 
ATOM   2780  H  HA     . PHE B 2 8   ? 11.436  -7.365  12.752  1.00 33.17  ? 7   PHE B HA     1 
ATOM   2781  H  HB2    . PHE B 2 8   ? 13.034  -8.793  13.600  1.00 31.81  ? 7   PHE B HB2    1 
ATOM   2782  H  HB3    . PHE B 2 8   ? 12.138  -9.715  12.666  1.00 31.81  ? 7   PHE B HB3    1 
ATOM   2783  H  HD1    . PHE B 2 8   ? 15.279  -8.226  12.930  1.00 36.74  ? 7   PHE B HD1    1 
ATOM   2784  H  HD2    . PHE B 2 8   ? 13.079  -10.703 10.686  1.00 39.48  ? 7   PHE B HD2    1 
ATOM   2785  H  HE1    . PHE B 2 8   ? 17.160  -8.827  11.771  1.00 37.19  ? 7   PHE B HE1    1 
ATOM   2786  H  HE2    . PHE B 2 8   ? 14.972  -11.307 9.509   1.00 40.90  ? 7   PHE B HE2    1 
ATOM   2787  H  HZ     . PHE B 2 8   ? 17.020  -10.339 10.039  1.00 37.80  ? 7   PHE B HZ     1 
ATOM   2788  N  N      . PHE B 2 9   ? 13.373  -5.828  12.867  1.00 24.50  ? 8   PHE B N      1 
ATOM   2789  C  CA     . PHE B 2 9   ? 14.516  -4.936  12.949  1.00 22.44  ? 8   PHE B CA     1 
ATOM   2790  C  C      . PHE B 2 9   ? 15.340  -5.381  14.167  1.00 25.97  ? 8   PHE B C      1 
ATOM   2791  O  O      . PHE B 2 9   ? 14.779  -5.540  15.251  1.00 23.77  ? 8   PHE B O      1 
ATOM   2792  C  CB     . PHE B 2 9   ? 14.147  -3.458  13.191  1.00 24.32  ? 8   PHE B CB     1 
ATOM   2793  C  CG     . PHE B 2 9   ? 13.438  -2.741  12.061  1.00 21.65  ? 8   PHE B CG     1 
ATOM   2794  C  CD1    . PHE B 2 9   ? 13.257  -3.302  10.819  1.00 22.59  ? 8   PHE B CD1    1 
ATOM   2795  C  CD2    . PHE B 2 9   ? 12.996  -1.442  12.265  1.00 21.99  ? 8   PHE B CD2    1 
ATOM   2796  C  CE1    . PHE B 2 9   ? 12.573  -2.591  9.797   1.00 22.36  ? 8   PHE B CE1    1 
ATOM   2797  C  CE2    . PHE B 2 9   ? 12.323  -0.730  11.262  1.00 18.37  ? 8   PHE B CE2    1 
ATOM   2798  C  CZ     . PHE B 2 9   ? 12.153  -1.298  10.010  1.00 19.62  ? 8   PHE B CZ     1 
ATOM   2799  H  H      . PHE B 2 9   ? 12.871  -5.782  13.564  1.00 29.43  ? 8   PHE B H      1 
ATOM   2800  H  HA     . PHE B 2 9   ? 14.998  -4.993  12.109  1.00 26.96  ? 8   PHE B HA     1 
ATOM   2801  H  HB2    . PHE B 2 9   ? 13.561  -3.418  13.964  1.00 29.21  ? 8   PHE B HB2    1 
ATOM   2802  H  HB3    . PHE B 2 9   ? 14.965  -2.969  13.368  1.00 29.21  ? 8   PHE B HB3    1 
ATOM   2803  H  HD1    . PHE B 2 9   ? 13.585  -4.155  10.647  1.00 27.14  ? 8   PHE B HD1    1 
ATOM   2804  H  HD2    . PHE B 2 9   ? 13.149  -1.034  13.087  1.00 26.42  ? 8   PHE B HD2    1 
ATOM   2805  H  HE1    . PHE B 2 9   ? 12.409  -3.001  8.979   1.00 26.87  ? 8   PHE B HE1    1 
ATOM   2806  H  HE2    . PHE B 2 9   ? 11.993  0.122   11.437  1.00 22.08  ? 8   PHE B HE2    1 
ATOM   2807  H  HZ     . PHE B 2 9   ? 11.759  -0.812  9.322   1.00 23.58  ? 8   PHE B HZ     1 
ATOM   2808  N  N      . ASP B 2 10  ? 16.643  -5.581  13.994  1.00 24.15  ? 9   ASP B N      1 
ATOM   2809  C  CA     . ASP B 2 10  ? 17.577  -5.695  15.115  1.00 25.11  ? 9   ASP B CA     1 
ATOM   2810  C  C      . ASP B 2 10  ? 18.137  -4.299  15.349  1.00 27.40  ? 9   ASP B C      1 
ATOM   2811  O  O      . ASP B 2 10  ? 18.813  -3.725  14.483  1.00 24.72  ? 9   ASP B O      1 
ATOM   2812  C  CB     . ASP B 2 10  ? 18.669  -6.728  14.834  1.00 26.76  ? 9   ASP B CB     1 
ATOM   2813  C  CG     . ASP B 2 10  ? 18.159  -8.145  14.936  1.00 30.34  ? 9   ASP B CG     1 
ATOM   2814  O  OD1    . ASP B 2 10  ? 17.455  -8.439  15.910  1.00 32.67  ? 9   ASP B OD1    1 
ATOM   2815  O  OD2    . ASP B 2 10  ? 18.424  -8.976  14.047  1.00 34.62  ? 9   ASP B OD2    1 
ATOM   2816  H  H      . ASP B 2 10  ? 17.020  -5.655  13.225  1.00 29.01  ? 9   ASP B H      1 
ATOM   2817  H  HA     . ASP B 2 10  ? 17.121  -5.999  15.915  1.00 30.16  ? 9   ASP B HA     1 
ATOM   2818  H  HB2    . ASP B 2 10  ? 19.010  -6.595  13.936  1.00 32.14  ? 9   ASP B HB2    1 
ATOM   2819  H  HB3    . ASP B 2 10  ? 19.384  -6.618  15.481  1.00 32.14  ? 9   ASP B HB3    1 
ATOM   2820  N  N      . ILE B 2 11  ? 17.802  -3.713  16.518  1.00 24.43  ? 10  ILE B N      1 
ATOM   2821  C  CA     . ILE B 2 11  ? 18.170  -2.344  16.836  1.00 20.24  ? 10  ILE B CA     1 
ATOM   2822  C  C      . ILE B 2 11  ? 19.473  -2.325  17.610  1.00 22.69  ? 10  ILE B C      1 
ATOM   2823  O  O      . ILE B 2 11  ? 19.667  -3.128  18.522  1.00 24.70  ? 10  ILE B O      1 
ATOM   2824  C  CB     . ILE B 2 11  ? 17.072  -1.659  17.673  1.00 23.66  ? 10  ILE B CB     1 
ATOM   2825  C  CG1    . ILE B 2 11  ? 15.692  -1.711  16.976  1.00 22.64  ? 10  ILE B CG1    1 
ATOM   2826  C  CG2    . ILE B 2 11  ? 17.496  -0.223  17.971  1.00 20.87  ? 10  ILE B CG2    1 
ATOM   2827  C  CD1    . ILE B 2 11  ? 15.610  -0.968  15.697  1.00 21.43  ? 10  ILE B CD1    1 
ATOM   2828  H  H      . ILE B 2 11  ? 17.356  -4.104  17.141  1.00 29.36  ? 10  ILE B H      1 
ATOM   2829  H  HA     . ILE B 2 11  ? 18.290  -1.869  15.999  1.00 24.32  ? 10  ILE B HA     1 
ATOM   2830  H  HB     . ILE B 2 11  ? 16.971  -2.145  18.506  1.00 28.42  ? 10  ILE B HB     1 
ATOM   2831  H  HG12   . ILE B 2 11  ? 15.476  -2.638  16.789  1.00 27.20  ? 10  ILE B HG12   1 
ATOM   2832  H  HG13   . ILE B 2 11  ? 15.030  -1.331  17.576  1.00 27.20  ? 10  ILE B HG13   1 
ATOM   2833  H  HG21   . ILE B 2 11  ? 16.716  0.288   18.238  1.00 25.08  ? 10  ILE B HG21   1 
ATOM   2834  H  HG22   . ILE B 2 11  ? 18.149  -0.229  18.689  1.00 25.08  ? 10  ILE B HG22   1 
ATOM   2835  H  HG23   . ILE B 2 11  ? 17.887  0.163   17.172  1.00 25.08  ? 10  ILE B HG23   1 
ATOM   2836  H  HD11   . ILE B 2 11  ? 14.722  -1.079  15.323  1.00 25.75  ? 10  ILE B HD11   1 
ATOM   2837  H  HD12   . ILE B 2 11  ? 15.783  -0.028  15.865  1.00 25.75  ? 10  ILE B HD12   1 
ATOM   2838  H  HD13   . ILE B 2 11  ? 16.273  -1.321  15.083  1.00 25.75  ? 10  ILE B HD13   1 
ATOM   2839  N  N      . ALA B 2 12  ? 20.319  -1.357  17.300  1.00 22.05  ? 11  ALA B N      1 
ATOM   2840  C  CA     . ALA B 2 12  ? 21.573  -1.144  17.998  1.00 24.84  ? 11  ALA B CA     1 
ATOM   2841  C  C      . ALA B 2 12  ? 21.709  0.315   18.399  1.00 25.27  ? 11  ALA B C      1 
ATOM   2842  O  O      . ALA B 2 12  ? 21.146  1.218   17.759  1.00 22.57  ? 11  ALA B O      1 
ATOM   2843  C  CB     . ALA B 2 12  ? 22.764  -1.593  17.119  1.00 25.41  ? 11  ALA B CB     1 
ATOM   2844  H  H      . ALA B 2 12  ? 20.184  -0.792  16.667  1.00 26.49  ? 11  ALA B H      1 
ATOM   2845  H  HA     . ALA B 2 12  ? 21.593  -1.658  18.821  1.00 29.84  ? 11  ALA B HA     1 
ATOM   2846  H  HB1    . ALA B 2 12  ? 23.590  -1.441  17.604  1.00 30.53  ? 11  ALA B HB1    1 
ATOM   2847  H  HB2    . ALA B 2 12  ? 22.669  -2.537  16.916  1.00 30.53  ? 11  ALA B HB2    1 
ATOM   2848  H  HB3    . ALA B 2 12  ? 22.763  -1.077  16.298  1.00 30.53  ? 11  ALA B HB3    1 
ATOM   2849  N  N      . VAL B 2 13  ? 22.453  0.542   19.483  1.00 23.70  ? 12  VAL B N      1 
ATOM   2850  C  CA     . VAL B 2 13  ? 22.687  1.872   20.018  1.00 22.43  ? 12  VAL B CA     1 
ATOM   2851  C  C      . VAL B 2 13  ? 24.185  2.068   20.081  1.00 26.28  ? 12  VAL B C      1 
ATOM   2852  O  O      . VAL B 2 13  ? 24.874  1.336   20.819  1.00 23.67  ? 12  VAL B O      1 
ATOM   2853  C  CB     . VAL B 2 13  ? 22.055  2.051   21.411  1.00 26.55  ? 12  VAL B CB     1 
ATOM   2854  C  CG1    . VAL B 2 13  ? 22.295  3.462   21.922  1.00 25.60  ? 12  VAL B CG1    1 
ATOM   2855  C  CG2    . VAL B 2 13  ? 20.547  1.714   21.349  1.00 23.06  ? 12  VAL B CG2    1 
ATOM   2856  H  H      . VAL B 2 13  ? 22.841  -0.079  19.933  1.00 28.47  ? 12  VAL B H      1 
ATOM   2857  H  HA     . VAL B 2 13  ? 22.304  2.537   19.425  1.00 26.95  ? 12  VAL B HA     1 
ATOM   2858  H  HB     . VAL B 2 13  ? 22.470  1.442   22.042  1.00 31.90  ? 12  VAL B HB     1 
ATOM   2859  H  HG11   . VAL B 2 13  ? 21.767  3.601   22.724  1.00 30.76  ? 12  VAL B HG11   1 
ATOM   2860  H  HG12   . VAL B 2 13  ? 23.238  3.569   22.124  1.00 30.76  ? 12  VAL B HG12   1 
ATOM   2861  H  HG13   . VAL B 2 13  ? 22.029  4.095   21.237  1.00 30.76  ? 12  VAL B HG13   1 
ATOM   2862  H  HG21   . VAL B 2 13  ? 20.139  1.930   22.202  1.00 27.70  ? 12  VAL B HG21   1 
ATOM   2863  H  HG22   . VAL B 2 13  ? 20.135  2.237   20.643  1.00 27.70  ? 12  VAL B HG22   1 
ATOM   2864  H  HG23   . VAL B 2 13  ? 20.442  0.767   21.162  1.00 27.70  ? 12  VAL B HG23   1 
ATOM   2865  N  N      . ASP B 2 14  ? 24.682  3.054   19.326  1.00 26.72  ? 13  ASP B N      1 
ATOM   2866  C  CA     . ASP B 2 14  ? 26.125  3.254   19.168  1.00 28.22  ? 13  ASP B CA     1 
ATOM   2867  C  C      . ASP B 2 14  ? 26.782  1.902   18.958  1.00 31.40  ? 13  ASP B C      1 
ATOM   2868  O  O      . ASP B 2 14  ? 27.831  1.600   19.555  1.00 30.69  ? 13  ASP B O      1 
ATOM   2869  C  CB     . ASP B 2 14  ? 26.706  3.982   20.361  1.00 32.73  ? 13  ASP B CB     1 
ATOM   2870  C  CG     . ASP B 2 14  ? 26.347  5.442   20.363  1.00 32.97  ? 13  ASP B CG     1 
ATOM   2871  O  OD1    . ASP B 2 14  ? 26.011  5.981   19.264  1.00 31.47  ? 13  ASP B OD1    1 
ATOM   2872  O  OD2    . ASP B 2 14  ? 26.417  6.050   21.452  1.00 31.56  ? 13  ASP B OD2    1 
ATOM   2873  H  H      . ASP B 2 14  ? 24.203  3.622   18.894  1.00 32.10  ? 13  ASP B H      1 
ATOM   2874  H  HA     . ASP B 2 14  ? 26.309  3.813   18.397  1.00 33.89  ? 13  ASP B HA     1 
ATOM   2875  H  HB2    . ASP B 2 14  ? 26.362  3.585   21.176  1.00 39.31  ? 13  ASP B HB2    1 
ATOM   2876  H  HB3    . ASP B 2 14  ? 27.673  3.909   20.339  1.00 39.31  ? 13  ASP B HB3    1 
ATOM   2877  N  N      . GLY B 2 15  ? 26.144  1.072   18.126  1.00 26.69  ? 14  GLY B N      1 
ATOM   2878  C  CA     . GLY B 2 15  ? 26.681  -0.205  17.709  1.00 28.05  ? 14  GLY B CA     1 
ATOM   2879  C  C      . GLY B 2 15  ? 26.413  -1.360  18.638  1.00 33.34  ? 14  GLY B C      1 
ATOM   2880  O  O      . GLY B 2 15  ? 26.661  -2.524  18.266  1.00 29.49  ? 14  GLY B O      1 
ATOM   2881  H  H      . GLY B 2 15  ? 25.373  1.241   17.784  1.00 32.06  ? 14  GLY B H      1 
ATOM   2882  H  HA2    . GLY B 2 15  ? 26.302  -0.430  16.845  1.00 33.70  ? 14  GLY B HA2    1 
ATOM   2883  H  HA3    . GLY B 2 15  ? 27.643  -0.119  17.619  1.00 33.70  ? 14  GLY B HA3    1 
ATOM   2884  N  N      . GLU B 2 16  ? 25.920  -1.093  19.809  1.00 28.88  ? 15  GLU B N      1 
ATOM   2885  C  CA     . GLU B 2 16  ? 25.674  -2.089  20.842  1.00 29.26  ? 15  GLU B CA     1 
ATOM   2886  C  C      . GLU B 2 16  ? 24.274  -2.644  20.679  1.00 27.54  ? 15  GLU B C      1 
ATOM   2887  O  O      . GLU B 2 16  ? 23.327  -1.863  20.572  1.00 27.70  ? 15  GLU B O      1 
ATOM   2888  C  CB     . GLU B 2 16  ? 25.817  -1.421  22.193  1.00 33.23  ? 15  GLU B CB     1 
ATOM   2889  C  CG     . GLU B 2 16  ? 26.037  -2.292  23.353  1.00 38.73  ? 15  GLU B CG     1 
ATOM   2890  C  CD     . GLU B 2 16  ? 26.468  -1.445  24.541  1.00 39.66  ? 15  GLU B CD     1 
ATOM   2891  O  OE1    . GLU B 2 16  ? 25.566  -0.929  25.231  1.00 40.29  ? 15  GLU B OE1    1 
ATOM   2892  O  OE2    . GLU B 2 16  ? 27.698  -1.263  24.737  1.00 43.74  ? 15  GLU B OE2    1 
ATOM   2893  H  H      . GLU B 2 16  ? 25.702  -0.300  20.060  1.00 34.69  ? 15  GLU B H      1 
ATOM   2894  H  HA     . GLU B 2 16  ? 26.296  -2.831  20.783  1.00 35.15  ? 15  GLU B HA     1 
ATOM   2895  H  HB2    . GLU B 2 16  ? 26.575  -0.816  22.147  1.00 39.91  ? 15  GLU B HB2    1 
ATOM   2896  H  HB3    . GLU B 2 16  ? 25.004  -0.921  22.366  1.00 39.91  ? 15  GLU B HB3    1 
ATOM   2897  H  HG2    . GLU B 2 16  ? 25.215  -2.754  23.578  1.00 46.51  ? 15  GLU B HG2    1 
ATOM   2898  H  HG3    . GLU B 2 16  ? 26.736  -2.935  23.155  1.00 46.51  ? 15  GLU B HG3    1 
ATOM   2899  N  N      . PRO B 2 17  ? 24.092  -3.960  20.628  1.00 26.83  ? 16  PRO B N      1 
ATOM   2900  C  CA     . PRO B 2 17  ? 22.736  -4.490  20.489  1.00 27.02  ? 16  PRO B CA     1 
ATOM   2901  C  C      . PRO B 2 17  ? 21.808  -4.003  21.594  1.00 29.45  ? 16  PRO B C      1 
ATOM   2902  O  O      . PRO B 2 17  ? 22.145  -4.018  22.777  1.00 24.71  ? 16  PRO B O      1 
ATOM   2903  C  CB     . PRO B 2 17  ? 22.920  -6.006  20.535  1.00 29.01  ? 16  PRO B CB     1 
ATOM   2904  C  CG     . PRO B 2 17  ? 24.352  -6.221  20.066  1.00 31.85  ? 16  PRO B CG     1 
ATOM   2905  C  CD     . PRO B 2 17  ? 25.123  -5.011  20.525  1.00 30.23  ? 16  PRO B CD     1 
ATOM   2906  H  HA     . PRO B 2 17  ? 22.374  -4.230  19.628  1.00 32.46  ? 16  PRO B HA     1 
ATOM   2907  H  HB2    . PRO B 2 17  ? 22.796  -6.330  21.440  1.00 34.85  ? 16  PRO B HB2    1 
ATOM   2908  H  HB3    . PRO B 2 17  ? 22.288  -6.437  19.938  1.00 34.85  ? 16  PRO B HB3    1 
ATOM   2909  H  HG2    . PRO B 2 17  ? 24.709  -7.028  20.468  1.00 38.25  ? 16  PRO B HG2    1 
ATOM   2910  H  HG3    . PRO B 2 17  ? 24.372  -6.294  19.099  1.00 38.25  ? 16  PRO B HG3    1 
ATOM   2911  H  HD2    . PRO B 2 17  ? 25.537  -5.174  21.387  1.00 36.31  ? 16  PRO B HD2    1 
ATOM   2912  H  HD3    . PRO B 2 17  ? 25.799  -4.767  19.873  1.00 36.31  ? 16  PRO B HD3    1 
ATOM   2913  N  N      . LEU B 2 18  ? 20.627  -3.566  21.176  1.00 25.99  ? 17  LEU B N      1 
ATOM   2914  C  CA     . LEU B 2 18  ? 19.507  -3.271  22.056  1.00 26.49  ? 17  LEU B CA     1 
ATOM   2915  C  C      . LEU B 2 18  ? 18.449  -4.367  22.058  1.00 23.44  ? 17  LEU B C      1 
ATOM   2916  O  O      . LEU B 2 18  ? 18.058  -4.833  23.130  1.00 24.17  ? 17  LEU B O      1 
ATOM   2917  C  CB     . LEU B 2 18  ? 18.900  -1.930  21.644  1.00 23.84  ? 17  LEU B CB     1 
ATOM   2918  C  CG     . LEU B 2 18  ? 17.744  -1.461  22.529  1.00 26.89  ? 17  LEU B CG     1 
ATOM   2919  C  CD1    . LEU B 2 18  ? 18.114  -1.335  23.997  1.00 27.44  ? 17  LEU B CD1    1 
ATOM   2920  C  CD2    . LEU B 2 18  ? 17.214  -0.117  22.002  1.00 26.71  ? 17  LEU B CD2    1 
ATOM   2921  H  H      . LEU B 2 18  ? 20.442  -3.427  20.348  1.00 31.22  ? 17  LEU B H      1 
ATOM   2922  H  HA     . LEU B 2 18  ? 19.824  -3.196  22.970  1.00 31.82  ? 17  LEU B HA     1 
ATOM   2923  H  HB2    . LEU B 2 18  ? 19.593  -1.252  21.682  1.00 28.64  ? 17  LEU B HB2    1 
ATOM   2924  H  HB3    . LEU B 2 18  ? 18.564  -2.008  20.738  1.00 28.64  ? 17  LEU B HB3    1 
ATOM   2925  H  HG     . LEU B 2 18  ? 17.051  -2.139  22.488  1.00 32.30  ? 17  LEU B HG     1 
ATOM   2926  H  HD11   . LEU B 2 18  ? 17.371  -0.939  24.478  1.00 32.96  ? 17  LEU B HD11   1 
ATOM   2927  H  HD12   . LEU B 2 18  ? 18.305  -2.217  24.352  1.00 32.96  ? 17  LEU B HD12   1 
ATOM   2928  H  HD13   . LEU B 2 18  ? 18.899  -0.770  24.078  1.00 32.96  ? 17  LEU B HD13   1 
ATOM   2929  H  HD21   . LEU B 2 18  ? 16.483  0.177   22.567  1.00 32.09  ? 17  LEU B HD21   1 
ATOM   2930  H  HD22   . LEU B 2 18  ? 17.932  0.535   22.023  1.00 32.09  ? 17  LEU B HD22   1 
ATOM   2931  H  HD23   . LEU B 2 18  ? 16.902  -0.236  21.092  1.00 32.09  ? 17  LEU B HD23   1 
ATOM   2932  N  N      . GLY B 2 19  ? 17.988  -4.811  20.892  1.00 25.85  ? 18  GLY B N      1 
ATOM   2933  C  CA     . GLY B 2 19  ? 17.025  -5.889  20.816  1.00 21.92  ? 18  GLY B CA     1 
ATOM   2934  C  C      . GLY B 2 19  ? 16.267  -5.872  19.509  1.00 26.15  ? 18  GLY B C      1 
ATOM   2935  O  O      . GLY B 2 19  ? 16.466  -5.013  18.666  1.00 26.15  ? 18  GLY B O      1 
ATOM   2936  H  H      . GLY B 2 19  ? 18.222  -4.498  20.126  1.00 31.05  ? 18  GLY B H      1 
ATOM   2937  H  HA2    . GLY B 2 19  ? 17.484  -6.740  20.895  1.00 26.33  ? 18  GLY B HA2    1 
ATOM   2938  H  HA3    . GLY B 2 19  ? 16.387  -5.806  21.543  1.00 26.33  ? 18  GLY B HA3    1 
ATOM   2939  N  N      . ARG B 2 20  ? 15.374  -6.855  19.368  1.00 24.49  ? 19  ARG B N      1 
ATOM   2940  C  CA     . ARG B 2 20  ? 14.627  -7.056  18.132  1.00 29.12  ? 19  ARG B CA     1 
ATOM   2941  C  C      . ARG B 2 20  ? 13.195  -6.578  18.288  1.00 27.73  ? 19  ARG B C      1 
ATOM   2942  O  O      . ARG B 2 20  ? 12.515  -6.948  19.257  1.00 28.69  ? 19  ARG B O      1 
ATOM   2943  C  CB     . ARG B 2 20  ? 14.609  -8.536  17.752  1.00 29.41  ? 19  ARG B CB     1 
ATOM   2944  C  CG     . ARG B 2 20  ? 13.787  -8.839  16.560  1.00 30.29  ? 19  ARG B CG     1 
ATOM   2945  C  CD     . ARG B 2 20  ? 14.127  -10.225 16.062  1.00 29.66  ? 19  ARG B CD     1 
ATOM   2946  N  NE     . ARG B 2 20  ? 15.458  -10.246 15.481  1.00 31.79  ? 19  ARG B NE     1 
ATOM   2947  C  CZ     . ARG B 2 20  ? 15.926  -11.247 14.752  1.00 33.32  ? 19  ARG B CZ     1 
ATOM   2948  N  NH1    . ARG B 2 20  ? 15.168  -12.284 14.451  1.00 32.85  ? 19  ARG B NH1    1 
ATOM   2949  N  NH2    . ARG B 2 20  ? 17.177  -11.200 14.318  1.00 32.86  ? 19  ARG B NH2    1 
ATOM   2950  H  H      . ARG B 2 20  ? 15.184  -7.424  19.985  1.00 29.42  ? 19  ARG B H      1 
ATOM   2951  H  HA     . ARG B 2 20  ? 15.052  -6.538  17.431  1.00 34.98  ? 19  ARG B HA     1 
ATOM   2952  H  HB2    . ARG B 2 20  ? 15.517  -8.820  17.564  1.00 35.32  ? 19  ARG B HB2    1 
ATOM   2953  H  HB3    . ARG B 2 20  ? 14.249  -9.044  18.496  1.00 35.32  ? 19  ARG B HB3    1 
ATOM   2954  H  HG2    . ARG B 2 20  ? 12.846  -8.809  16.792  1.00 36.38  ? 19  ARG B HG2    1 
ATOM   2955  H  HG3    . ARG B 2 20  ? 13.976  -8.197  15.857  1.00 36.38  ? 19  ARG B HG3    1 
ATOM   2956  H  HD2    . ARG B 2 20  ? 14.103  -10.851 16.803  1.00 35.62  ? 19  ARG B HD2    1 
ATOM   2957  H  HD3    . ARG B 2 20  ? 13.488  -10.492 15.382  1.00 35.62  ? 19  ARG B HD3    1 
ATOM   2958  H  HE     . ARG B 2 20  ? 15.972  -9.570  15.618  1.00 38.19  ? 19  ARG B HE     1 
ATOM   2959  H  HH11   . ARG B 2 20  ? 14.355  -12.318 14.729  1.00 39.45  ? 19  ARG B HH11   1 
ATOM   2960  H  HH12   . ARG B 2 20  ? 15.487  -12.927 13.976  1.00 39.45  ? 19  ARG B HH12   1 
ATOM   2961  H  HH21   . ARG B 2 20  ? 17.674  -10.525 14.511  1.00 39.46  ? 19  ARG B HH21   1 
ATOM   2962  H  HH22   . ARG B 2 20  ? 17.492  -11.844 13.844  1.00 39.46  ? 19  ARG B HH22   1 
ATOM   2963  N  N      . VAL B 2 21  ? 12.710  -5.838  17.300  1.00 24.65  ? 20  VAL B N      1 
ATOM   2964  C  CA     . VAL B 2 21  ? 11.297  -5.529  17.207  1.00 23.86  ? 20  VAL B CA     1 
ATOM   2965  C  C      . VAL B 2 21  ? 10.781  -6.136  15.913  1.00 21.93  ? 20  VAL B C      1 
ATOM   2966  O  O      . VAL B 2 21  ? 11.473  -6.128  14.892  1.00 24.79  ? 20  VAL B O      1 
ATOM   2967  C  CB     . VAL B 2 21  ? 11.035  -4.018  17.271  1.00 27.31  ? 20  VAL B CB     1 
ATOM   2968  C  CG1    . VAL B 2 21  ? 11.889  -3.300  16.340  1.00 27.30  ? 20  VAL B CG1    1 
ATOM   2969  C  CG2    . VAL B 2 21  ? 9.552   -3.724  16.987  1.00 26.63  ? 20  VAL B CG2    1 
ATOM   2970  H  H      . VAL B 2 21  ? 13.187  -5.502  16.668  1.00 29.61  ? 20  VAL B H      1 
ATOM   2971  H  HA     . VAL B 2 21  ? 10.817  -5.932  17.948  1.00 28.67  ? 20  VAL B HA     1 
ATOM   2972  H  HB     . VAL B 2 21  ? 11.246  -3.702  18.164  1.00 32.81  ? 20  VAL B HB     1 
ATOM   2973  H  HG11   . VAL B 2 21  ? 11.613  -2.371  16.310  1.00 32.79  ? 20  VAL B HG11   1 
ATOM   2974  H  HG12   . VAL B 2 21  ? 12.809  -3.362  16.642  1.00 32.79  ? 20  VAL B HG12   1 
ATOM   2975  H  HG13   . VAL B 2 21  ? 11.803  -3.699  15.460  1.00 32.79  ? 20  VAL B HG13   1 
ATOM   2976  H  HG21   . VAL B 2 21  ? 9.347   -2.822  17.278  1.00 31.99  ? 20  VAL B HG21   1 
ATOM   2977  H  HG22   . VAL B 2 21  ? 9.391   -3.809  16.034  1.00 31.99  ? 20  VAL B HG22   1 
ATOM   2978  H  HG23   . VAL B 2 21  ? 9.005   -4.361  17.473  1.00 31.99  ? 20  VAL B HG23   1 
ATOM   2979  N  N      . SER B 2 22  ? 9.616   -6.713  15.976  1.00 23.91  ? 21  SER B N      1 
ATOM   2980  C  CA     . SER B 2 22  ? 8.990   -7.253  14.782  1.00 27.37  ? 21  SER B CA     1 
ATOM   2981  C  C      . SER B 2 22  ? 7.657   -6.570  14.572  1.00 25.30  ? 21  SER B C      1 
ATOM   2982  O  O      . SER B 2 22  ? 7.042   -6.048  15.514  1.00 24.83  ? 21  SER B O      1 
ATOM   2983  C  CB     . SER B 2 22  ? 8.809   -8.760  14.933  1.00 26.96  ? 21  SER B CB     1 
ATOM   2984  O  OG     . SER B 2 22  ? 7.772   -8.973  15.849  1.00 30.08  ? 21  SER B OG     1 
ATOM   2985  H  H      . SER B 2 22  ? 9.157   -6.809  16.697  1.00 28.73  ? 21  SER B H      1 
ATOM   2986  H  HA     . SER B 2 22  ? 9.533   -7.088  13.996  1.00 32.88  ? 21  SER B HA     1 
ATOM   2987  H  HB2    . SER B 2 22  ? 8.575   -9.150  14.076  1.00 32.39  ? 21  SER B HB2    1 
ATOM   2988  H  HB3    . SER B 2 22  ? 9.629   -9.158  15.266  1.00 32.39  ? 21  SER B HB3    1 
ATOM   2989  H  HG     . SER B 2 22  ? 7.675   -9.796  15.987  1.00 36.13  ? 21  SER B HG     1 
ATOM   2990  N  N      . PHE B 2 23  ? 7.216   -6.589  13.306  1.00 24.24  ? 22  PHE B N      1 
ATOM   2991  C  CA     . PHE B 2 23  ? 6.027   -5.887  12.864  1.00 24.62  ? 22  PHE B CA     1 
ATOM   2992  C  C      . PHE B 2 23  ? 5.159   -6.808  12.039  1.00 22.52  ? 22  PHE B C      1 
ATOM   2993  O  O      . PHE B 2 23  ? 5.675   -7.560  11.202  1.00 25.63  ? 22  PHE B O      1 
ATOM   2994  C  CB     . PHE B 2 23  ? 6.373   -4.709  11.977  1.00 20.65  ? 22  PHE B CB     1 
ATOM   2995  C  CG     . PHE B 2 23  ? 7.390   -3.793  12.554  1.00 17.60  ? 22  PHE B CG     1 
ATOM   2996  C  CD1    . PHE B 2 23  ? 7.011   -2.731  13.344  1.00 22.80  ? 22  PHE B CD1    1 
ATOM   2997  C  CD2    . PHE B 2 23  ? 8.720   -3.936  12.266  1.00 22.75  ? 22  PHE B CD2    1 
ATOM   2998  C  CE1    . PHE B 2 23  ? 7.962   -1.872  13.859  1.00 22.54  ? 22  PHE B CE1    1 
ATOM   2999  C  CE2    . PHE B 2 23  ? 9.650   -3.086  12.768  1.00 23.86  ? 22  PHE B CE2    1 
ATOM   3000  C  CZ     . PHE B 2 23  ? 9.267   -2.047  13.569  1.00 22.80  ? 22  PHE B CZ     1 
ATOM   3001  H  H      . PHE B 2 23  ? 7.609   -7.018  12.672  1.00 29.12  ? 22  PHE B H      1 
ATOM   3002  H  HA     . PHE B 2 23  ? 5.547   -5.589  13.652  1.00 29.58  ? 22  PHE B HA     1 
ATOM   3003  H  HB2    . PHE B 2 23  ? 6.723   -5.045  11.137  1.00 24.81  ? 22  PHE B HB2    1 
ATOM   3004  H  HB3    . PHE B 2 23  ? 5.568   -4.193  11.818  1.00 24.81  ? 22  PHE B HB3    1 
ATOM   3005  H  HD1    . PHE B 2 23  ? 6.111   -2.592  13.532  1.00 27.39  ? 22  PHE B HD1    1 
ATOM   3006  H  HD2    . PHE B 2 23  ? 8.992   -4.632  11.713  1.00 27.33  ? 22  PHE B HD2    1 
ATOM   3007  H  HE1    . PHE B 2 23  ? 7.701   -1.169  14.408  1.00 27.08  ? 22  PHE B HE1    1 
ATOM   3008  H  HE2    . PHE B 2 23  ? 10.549  -3.211  12.568  1.00 28.66  ? 22  PHE B HE2    1 
ATOM   3009  H  HZ     . PHE B 2 23  ? 9.903   -1.462  13.912  1.00 27.39  ? 22  PHE B HZ     1 
ATOM   3010  N  N      . GLU B 2 24  ? 3.864   -6.739  12.258  1.00 21.64  ? 23  GLU B N      1 
ATOM   3011  C  CA     . GLU B 2 24  ? 2.904   -7.263  11.290  1.00 26.91  ? 23  GLU B CA     1 
ATOM   3012  C  C      . GLU B 2 24  ? 2.602   -6.142  10.292  1.00 25.85  ? 23  GLU B C      1 
ATOM   3013  O  O      . GLU B 2 24  ? 2.387   -4.989  10.693  1.00 24.11  ? 23  GLU B O      1 
ATOM   3014  C  CB     . GLU B 2 24  ? 1.630   -7.763  11.972  1.00 28.58  ? 23  GLU B CB     1 
ATOM   3015  C  CG     . GLU B 2 24  ? 0.542   -8.081  10.990  1.00 31.95  ? 23  GLU B CG     1 
ATOM   3016  C  CD     . GLU B 2 24  ? -0.643  -8.775  11.600  1.00 35.90  ? 23  GLU B CD     1 
ATOM   3017  O  OE1    . GLU B 2 24  ? -0.607  -9.098  12.807  1.00 38.71  ? 23  GLU B OE1    1 
ATOM   3018  O  OE2    . GLU B 2 24  ? -1.628  -8.982  10.859  1.00 33.43  ? 23  GLU B OE2    1 
ATOM   3019  H  H      . GLU B 2 24  ? 3.507   -6.394  12.960  1.00 26.00  ? 23  GLU B H      1 
ATOM   3020  H  HA     . GLU B 2 24  ? 3.271   -8.028  10.819  1.00 32.33  ? 23  GLU B HA     1 
ATOM   3021  H  HB2    . GLU B 2 24  ? 1.833   -8.570  12.470  1.00 34.33  ? 23  GLU B HB2    1 
ATOM   3022  H  HB3    . GLU B 2 24  ? 1.302   -7.076  12.574  1.00 34.33  ? 23  GLU B HB3    1 
ATOM   3023  H  HG2    . GLU B 2 24  ? 0.227   -7.253  10.594  1.00 38.38  ? 23  GLU B HG2    1 
ATOM   3024  H  HG3    . GLU B 2 24  ? 0.903   -8.662  10.302  1.00 38.38  ? 23  GLU B HG3    1 
ATOM   3025  N  N      . LEU B 2 25  ? 2.624   -6.475  9.000   1.00 23.99  ? 24  LEU B N      1 
ATOM   3026  C  CA     . LEU B 2 25  ? 2.320   -5.546  7.909   1.00 22.91  ? 24  LEU B CA     1 
ATOM   3027  C  C      . LEU B 2 25  ? 0.939   -5.897  7.356   1.00 26.65  ? 24  LEU B C      1 
ATOM   3028  O  O      . LEU B 2 25  ? 0.688   -7.049  6.974   1.00 26.17  ? 24  LEU B O      1 
ATOM   3029  C  CB     . LEU B 2 25  ? 3.367   -5.645  6.810   1.00 25.79  ? 24  LEU B CB     1 
ATOM   3030  C  CG     . LEU B 2 25  ? 4.835   -5.517  7.174   1.00 23.72  ? 24  LEU B CG     1 
ATOM   3031  C  CD1    . LEU B 2 25  ? 5.670   -5.421  5.914   1.00 28.47  ? 24  LEU B CD1    1 
ATOM   3032  C  CD2    . LEU B 2 25  ? 5.062   -4.294  8.119   1.00 22.32  ? 24  LEU B CD2    1 
ATOM   3033  H  H      . LEU B 2 25  ? 2.821   -7.264  8.719   1.00 28.82  ? 24  LEU B H      1 
ATOM   3034  H  HA     . LEU B 2 25  ? 2.307   -4.635  8.243   1.00 27.53  ? 24  LEU B HA     1 
ATOM   3035  H  HB2    . LEU B 2 25  ? 3.264   -6.512  6.389   1.00 30.98  ? 24  LEU B HB2    1 
ATOM   3036  H  HB3    . LEU B 2 25  ? 3.182   -4.940  6.169   1.00 30.98  ? 24  LEU B HB3    1 
ATOM   3037  H  HG     . LEU B 2 25  ? 5.126   -6.304  7.660   1.00 28.50  ? 24  LEU B HG     1 
ATOM   3038  H  HD11   . LEU B 2 25  ? 6.605   -5.348  6.160   1.00 34.19  ? 24  LEU B HD11   1 
ATOM   3039  H  HD12   . LEU B 2 25  ? 5.529   -6.218  5.381   1.00 34.19  ? 24  LEU B HD12   1 
ATOM   3040  H  HD13   . LEU B 2 25  ? 5.397   -4.636  5.414   1.00 34.19  ? 24  LEU B HD13   1 
ATOM   3041  H  HD21   . LEU B 2 25  ? 6.015   -4.165  8.246   1.00 26.82  ? 24  LEU B HD21   1 
ATOM   3042  H  HD22   . LEU B 2 25  ? 4.673   -3.504  7.712   1.00 26.82  ? 24  LEU B HD22   1 
ATOM   3043  H  HD23   . LEU B 2 25  ? 4.635   -4.471  8.972   1.00 26.82  ? 24  LEU B HD23   1 
ATOM   3044  N  N      . PHE B 2 26  ? 0.036   -4.917  7.337   1.00 24.10  ? 25  PHE B N      1 
ATOM   3045  C  CA     . PHE B 2 26  ? -1.367  -5.179  7.029   1.00 25.00  ? 25  PHE B CA     1 
ATOM   3046  C  C      . PHE B 2 26  ? -1.616  -5.226  5.522   1.00 26.19  ? 25  PHE B C      1 
ATOM   3047  O  O      . PHE B 2 26  ? -2.323  -4.391  4.946   1.00 24.62  ? 25  PHE B O      1 
ATOM   3048  C  CB     . PHE B 2 26  ? -2.226  -4.118  7.693   1.00 25.95  ? 25  PHE B CB     1 
ATOM   3049  C  CG     . PHE B 2 26  ? -2.068  -4.059  9.206   1.00 27.56  ? 25  PHE B CG     1 
ATOM   3050  C  CD1    . PHE B 2 26  ? -1.983  -5.218  9.967   1.00 30.26  ? 25  PHE B CD1    1 
ATOM   3051  C  CD2    . PHE B 2 26  ? -2.015  -2.843  9.844   1.00 26.16  ? 25  PHE B CD2    1 
ATOM   3052  C  CE1    . PHE B 2 26  ? -1.857  -5.145  11.337  1.00 29.06  ? 25  PHE B CE1    1 
ATOM   3053  C  CE2    . PHE B 2 26  ? -1.909  -2.774  11.235  1.00 27.51  ? 25  PHE B CE2    1 
ATOM   3054  C  CZ     . PHE B 2 26  ? -1.821  -3.909  11.957  1.00 26.20  ? 25  PHE B CZ     1 
ATOM   3055  H  H      . PHE B 2 26  ? 0.213   -4.091  7.500   1.00 28.95  ? 25  PHE B H      1 
ATOM   3056  H  HA     . PHE B 2 26  ? -1.602  -6.052  7.381   1.00 30.03  ? 25  PHE B HA     1 
ATOM   3057  H  HB2    . PHE B 2 26  ? -1.982  -3.250  7.336   1.00 31.18  ? 25  PHE B HB2    1 
ATOM   3058  H  HB3    . PHE B 2 26  ? -3.158  -4.306  7.500   1.00 31.18  ? 25  PHE B HB3    1 
ATOM   3059  H  HD1    . PHE B 2 26  ? -2.011  -6.048  9.549   1.00 36.34  ? 25  PHE B HD1    1 
ATOM   3060  H  HD2    . PHE B 2 26  ? -2.051  -2.058  9.346   1.00 31.43  ? 25  PHE B HD2    1 
ATOM   3061  H  HE1    . PHE B 2 26  ? -1.796  -5.923  11.842  1.00 34.91  ? 25  PHE B HE1    1 
ATOM   3062  H  HE2    . PHE B 2 26  ? -1.898  -1.948  11.662  1.00 33.04  ? 25  PHE B HE2    1 
ATOM   3063  H  HZ     . PHE B 2 26  ? -1.736  -3.860  12.882  1.00 31.47  ? 25  PHE B HZ     1 
ATOM   3064  N  N      . ALA B 2 27  ? -1.001  -6.213  4.870   1.00 28.36  ? 26  ALA B N      1 
ATOM   3065  C  CA     . ALA B 2 27  ? -1.128  -6.307  3.418   1.00 26.70  ? 26  ALA B CA     1 
ATOM   3066  C  C      . ALA B 2 27  ? -2.565  -6.566  2.990   1.00 28.81  ? 26  ALA B C      1 
ATOM   3067  O  O      . ALA B 2 27  ? -2.922  -6.319  1.820   1.00 29.54  ? 26  ALA B O      1 
ATOM   3068  C  CB     . ALA B 2 27  ? -0.246  -7.425  2.865   1.00 27.38  ? 26  ALA B CB     1 
ATOM   3069  H  H      . ALA B 2 27  ? -0.518  -6.824  5.235   1.00 34.07  ? 26  ALA B H      1 
ATOM   3070  H  HA     . ALA B 2 27  ? -0.826  -5.467  3.039   1.00 32.07  ? 26  ALA B HA     1 
ATOM   3071  H  HB1    . ALA B 2 27  ? -0.368  -7.477  1.904   1.00 32.89  ? 26  ALA B HB1    1 
ATOM   3072  H  HB2    . ALA B 2 27  ? 0.681   -7.227  3.070   1.00 32.89  ? 26  ALA B HB2    1 
ATOM   3073  H  HB3    . ALA B 2 27  ? -0.504  -8.265  3.277   1.00 32.89  ? 26  ALA B HB3    1 
ATOM   3074  N  N      . ASP B 2 28  ? -3.381  -7.090  3.904   1.00 27.19  ? 27  ASP B N      1 
ATOM   3075  C  CA     . ASP B 2 28  ? -4.792  -7.324  3.628   1.00 32.52  ? 27  ASP B CA     1 
ATOM   3076  C  C      . ASP B 2 28  ? -5.549  -6.025  3.402   1.00 31.86  ? 27  ASP B C      1 
ATOM   3077  O  O      . ASP B 2 28  ? -6.537  -6.013  2.670   1.00 32.43  ? 27  ASP B O      1 
ATOM   3078  C  CB     . ASP B 2 28  ? -5.421  -8.093  4.788   1.00 34.81  ? 27  ASP B CB     1 
ATOM   3079  C  CG     . ASP B 2 28  ? -5.252  -7.374  6.108   1.00 37.05  ? 27  ASP B CG     1 
ATOM   3080  O  OD1    . ASP B 2 28  ? -4.198  -6.721  6.287   1.00 34.85  ? 27  ASP B OD1    1 
ATOM   3081  O  OD2    . ASP B 2 28  ? -6.150  -7.465  6.967   1.00 42.53  ? 27  ASP B OD2    1 
ATOM   3082  H  H      . ASP B 2 28  ? -3.139  -7.320  4.696   1.00 32.66  ? 27  ASP B H      1 
ATOM   3083  H  HA     . ASP B 2 28  ? -4.866  -7.858  2.822   1.00 39.06  ? 27  ASP B HA     1 
ATOM   3084  H  HB2    . ASP B 2 28  ? -6.371  -8.200  4.621   1.00 41.80  ? 27  ASP B HB2    1 
ATOM   3085  H  HB3    . ASP B 2 28  ? -4.997  -8.963  4.860   1.00 41.80  ? 27  ASP B HB3    1 
ATOM   3086  N  N      . LYS B 2 29  ? -5.111  -4.926  4.032   1.00 28.02  ? 28  LYS B N      1 
ATOM   3087  C  CA     . LYS B 2 29  ? -5.763  -3.632  3.888   1.00 29.07  ? 28  LYS B CA     1 
ATOM   3088  C  C      . LYS B 2 29  ? -4.940  -2.601  3.112   1.00 25.41  ? 28  LYS B C      1 
ATOM   3089  O  O      . LYS B 2 29  ? -5.540  -1.790  2.417   1.00 24.87  ? 28  LYS B O      1 
ATOM   3090  C  CB     . LYS B 2 29  ? -6.109  -3.049  5.266   1.00 32.99  ? 28  LYS B CB     1 
ATOM   3091  C  CG     . LYS B 2 29  ? -7.317  -3.660  6.005   1.00 36.10  ? 28  LYS B CG     1 
ATOM   3092  C  CD     . LYS B 2 29  ? -8.445  -4.113  5.099   1.00 45.47  ? 28  LYS B CD     1 
ATOM   3093  C  CE     . LYS B 2 29  ? -9.676  -3.184  5.146   1.00 50.48  ? 28  LYS B CE     1 
ATOM   3094  N  NZ     . LYS B 2 29  ? -10.898 -3.889  4.660   1.00 55.29  ? 28  LYS B NZ     1 
ATOM   3095  H  H      . LYS B 2 29  ? -4.429  -4.911  4.554   1.00 33.65  ? 28  LYS B H      1 
ATOM   3096  H  HA     . LYS B 2 29  ? -6.594  -3.765  3.404   1.00 34.92  ? 28  LYS B HA     1 
ATOM   3097  H  HB2    . LYS B 2 29  ? -5.338  -3.166  5.843   1.00 39.62  ? 28  LYS B HB2    1 
ATOM   3098  H  HB3    . LYS B 2 29  ? -6.297  -2.104  5.152   1.00 39.62  ? 28  LYS B HB3    1 
ATOM   3099  H  HG2    . LYS B 2 29  ? -7.015  -4.434  6.505   1.00 43.35  ? 28  LYS B HG2    1 
ATOM   3100  H  HG3    . LYS B 2 29  ? -7.679  -2.994  6.610   1.00 43.35  ? 28  LYS B HG3    1 
ATOM   3101  H  HD2    . LYS B 2 29  ? -8.125  -4.136  4.184   1.00 54.60  ? 28  LYS B HD2    1 
ATOM   3102  H  HD3    . LYS B 2 29  ? -8.731  -4.999  5.373   1.00 54.60  ? 28  LYS B HD3    1 
ATOM   3103  H  HE2    . LYS B 2 29  ? -9.830  -2.898  6.060   1.00 60.61  ? 28  LYS B HE2    1 
ATOM   3104  H  HE3    . LYS B 2 29  ? -9.520  -2.413  4.578   1.00 60.61  ? 28  LYS B HE3    1 
ATOM   3105  H  HZ1    . LYS B 2 29  ? -11.599 -3.341  4.693   1.00 66.38  ? 28  LYS B HZ1    1 
ATOM   3106  H  HZ2    . LYS B 2 29  ? -10.781 -4.157  3.819   1.00 66.38  ? 28  LYS B HZ2    1 
ATOM   3107  H  HZ3    . LYS B 2 29  ? -11.062 -4.600  5.169   1.00 66.38  ? 28  LYS B HZ3    1 
ATOM   3108  N  N      . VAL B 2 30  ? -3.605  -2.609  3.206   1.00 26.51  ? 29  VAL B N      1 
ATOM   3109  C  CA     . VAL B 2 30  ? -2.776  -1.711  2.396   1.00 25.71  ? 29  VAL B CA     1 
ATOM   3110  C  C      . VAL B 2 30  ? -1.673  -2.504  1.716   1.00 22.69  ? 29  VAL B C      1 
ATOM   3111  O  O      . VAL B 2 30  ? -0.501  -2.379  2.079   1.00 24.15  ? 29  VAL B O      1 
ATOM   3112  C  CB     . VAL B 2 30  ? -2.137  -0.584  3.227   1.00 23.31  ? 29  VAL B CB     1 
ATOM   3113  C  CG1    . VAL B 2 30  ? -3.058  0.562   3.413   1.00 24.80  ? 29  VAL B CG1    1 
ATOM   3114  C  CG2    . VAL B 2 30  ? -1.739  -1.119  4.559   1.00 24.05  ? 29  VAL B CG2    1 
ATOM   3115  H  H      . VAL B 2 30  ? -3.158  -3.124  3.730   1.00 31.85  ? 29  VAL B H      1 
ATOM   3116  H  HA     . VAL B 2 30  ? -3.361  -1.321  1.728   1.00 30.89  ? 29  VAL B HA     1 
ATOM   3117  H  HB     . VAL B 2 30  ? -1.359  -0.259  2.748   1.00 28.00  ? 29  VAL B HB     1 
ATOM   3118  H  HG11   . VAL B 2 30  ? -2.614  1.241   3.946   1.00 29.80  ? 29  VAL B HG11   1 
ATOM   3119  H  HG12   . VAL B 2 30  ? -3.291  0.924   2.543   1.00 29.80  ? 29  VAL B HG12   1 
ATOM   3120  H  HG13   . VAL B 2 30  ? -3.858  0.255   3.868   1.00 29.80  ? 29  VAL B HG13   1 
ATOM   3121  H  HG21   . VAL B 2 30  ? -1.222  -0.446  5.028   1.00 28.90  ? 29  VAL B HG21   1 
ATOM   3122  H  HG22   . VAL B 2 30  ? -2.539  -1.334  5.065   1.00 28.90  ? 29  VAL B HG22   1 
ATOM   3123  H  HG23   . VAL B 2 30  ? -1.204  -1.918  4.432   1.00 28.90  ? 29  VAL B HG23   1 
ATOM   3124  N  N      . PRO B 2 31  ? -1.980  -3.289  0.685   1.00 24.11  ? 30  PRO B N      1 
ATOM   3125  C  CA     . PRO B 2 31  ? -0.961  -4.181  0.119   1.00 23.25  ? 30  PRO B CA     1 
ATOM   3126  C  C      . PRO B 2 31  ? 0.227   -3.469  -0.507  1.00 20.90  ? 30  PRO B C      1 
ATOM   3127  O  O      . PRO B 2 31  ? 1.369   -3.957  -0.428  1.00 23.12  ? 30  PRO B O      1 
ATOM   3128  C  CB     . PRO B 2 31  ? -1.768  -4.971  -0.955  1.00 23.95  ? 30  PRO B CB     1 
ATOM   3129  C  CG     . PRO B 2 31  ? -2.981  -4.098  -1.217  1.00 30.79  ? 30  PRO B CG     1 
ATOM   3130  C  CD     . PRO B 2 31  ? -3.314  -3.568  0.144   1.00 27.76  ? 30  PRO B CD     1 
ATOM   3131  H  HA     . PRO B 2 31  ? -0.638  -4.775  0.815   1.00 27.93  ? 30  PRO B HA     1 
ATOM   3132  H  HB2    . PRO B 2 31  ? -1.235  -5.082  -1.758  1.00 28.77  ? 30  PRO B HB2    1 
ATOM   3133  H  HB3    . PRO B 2 31  ? -2.028  -5.838  -0.606  1.00 28.77  ? 30  PRO B HB3    1 
ATOM   3134  H  HG2    . PRO B 2 31  ? -2.756  -3.381  -1.831  1.00 36.98  ? 30  PRO B HG2    1 
ATOM   3135  H  HG3    . PRO B 2 31  ? -3.708  -4.628  -1.579  1.00 36.98  ? 30  PRO B HG3    1 
ATOM   3136  H  HD2    . PRO B 2 31  ? -3.846  -2.759  0.086   1.00 33.35  ? 30  PRO B HD2    1 
ATOM   3137  H  HD3    . PRO B 2 31  ? -3.778  -4.233  0.677   1.00 33.35  ? 30  PRO B HD3    1 
ATOM   3138  N  N      . LYS B 2 32  ? -0.006  -2.344  -1.181  1.00 22.67  ? 31  LYS B N      1 
ATOM   3139  C  CA     . LYS B 2 32  ? 1.105   -1.679  -1.852  1.00 22.37  ? 31  LYS B CA     1 
ATOM   3140  C  C      . LYS B 2 32  ? 2.095   -1.122  -0.837  1.00 21.63  ? 31  LYS B C      1 
ATOM   3141  O  O      . LYS B 2 32  ? 3.310   -1.279  -0.979  1.00 19.59  ? 31  LYS B O      1 
ATOM   3142  C  CB     . LYS B 2 32  ? 0.568   -0.570  -2.748  1.00 23.35  ? 31  LYS B CB     1 
ATOM   3143  C  CG     . LYS B 2 32  ? 1.630   0.047   -3.640  1.00 27.43  ? 31  LYS B CG     1 
ATOM   3144  C  CD     . LYS B 2 32  ? 1.019   0.909   -4.779  1.00 29.95  ? 31  LYS B CD     1 
ATOM   3145  C  CE     . LYS B 2 32  ? 2.140   1.415   -5.667  1.00 30.37  ? 31  LYS B CE     1 
ATOM   3146  N  NZ     . LYS B 2 32  ? 1.598   2.245   -6.770  1.00 33.13  ? 31  LYS B NZ     1 
ATOM   3147  H  H      . LYS B 2 32  ? -0.771  -1.960  -1.262  1.00 27.23  ? 31  LYS B H      1 
ATOM   3148  H  HA     . LYS B 2 32  ? 1.575   -2.318  -2.410  1.00 26.88  ? 31  LYS B HA     1 
ATOM   3149  H  HB2    . LYS B 2 32  ? -0.125  -0.936  -3.320  1.00 28.06  ? 31  LYS B HB2    1 
ATOM   3150  H  HB3    . LYS B 2 32  ? 0.201   0.134   -2.191  1.00 28.06  ? 31  LYS B HB3    1 
ATOM   3151  H  HG2    . LYS B 2 32  ? 2.202   0.618   -3.104  1.00 32.95  ? 31  LYS B HG2    1 
ATOM   3152  H  HG3    . LYS B 2 32  ? 2.154   -0.661  -4.046  1.00 32.95  ? 31  LYS B HG3    1 
ATOM   3153  H  HD2    . LYS B 2 32  ? 0.412   0.372   -5.312  1.00 35.97  ? 31  LYS B HD2    1 
ATOM   3154  H  HD3    . LYS B 2 32  ? 0.547   1.668   -4.403  1.00 35.97  ? 31  LYS B HD3    1 
ATOM   3155  H  HE2    . LYS B 2 32  ? 2.750   1.958   -5.143  1.00 36.48  ? 31  LYS B HE2    1 
ATOM   3156  H  HE3    . LYS B 2 32  ? 2.615   0.661   -6.052  1.00 36.48  ? 31  LYS B HE3    1 
ATOM   3157  H  HZ1    . LYS B 2 32  ? 2.262   2.536   -7.287  1.00 39.79  ? 31  LYS B HZ1    1 
ATOM   3158  H  HZ2    . LYS B 2 32  ? 1.036   1.764   -7.265  1.00 39.79  ? 31  LYS B HZ2    1 
ATOM   3159  H  HZ3    . LYS B 2 32  ? 1.163   2.946   -6.438  1.00 39.79  ? 31  LYS B HZ3    1 
ATOM   3160  N  N      . THR B 2 33  ? 1.570   -0.453  0.186   1.00 21.71  ? 32  THR B N      1 
ATOM   3161  C  CA     . THR B 2 33  ? 2.382   0.129   1.252   1.00 19.49  ? 32  THR B CA     1 
ATOM   3162  C  C      . THR B 2 33  ? 3.067   -0.960  2.070   1.00 20.40  ? 32  THR B C      1 
ATOM   3163  O  O      . THR B 2 33  ? 4.262   -0.876  2.338   1.00 19.85  ? 32  THR B O      1 
ATOM   3164  C  CB     . THR B 2 33  ? 1.478   1.016   2.122   1.00 19.40  ? 32  THR B CB     1 
ATOM   3165  O  OG1    . THR B 2 33  ? 0.704   1.909   1.275   1.00 20.24  ? 32  THR B OG1    1 
ATOM   3166  C  CG2    . THR B 2 33  ? 2.305   1.840   3.114   1.00 16.81  ? 32  THR B CG2    1 
ATOM   3167  H  H      . THR B 2 33  ? 0.727   -0.319  0.291   1.00 26.08  ? 32  THR B H      1 
ATOM   3168  H  HA     . THR B 2 33  ? 3.084   0.686   0.880   1.00 23.42  ? 32  THR B HA     1 
ATOM   3169  H  HB     . THR B 2 33  ? 0.875   0.451   2.632   1.00 23.31  ? 32  THR B HB     1 
ATOM   3170  H  HG1    . THR B 2 33  ? 0.094   1.481   0.888   1.00 24.32  ? 32  THR B HG1    1 
ATOM   3171  H  HG21   . THR B 2 33  ? 1.729   2.448   3.602   1.00 20.21  ? 32  THR B HG21   1 
ATOM   3172  H  HG22   . THR B 2 33  ? 2.749   1.252   3.745   1.00 20.21  ? 32  THR B HG22   1 
ATOM   3173  H  HG23   . THR B 2 33  ? 2.976   2.355   2.639   1.00 20.21  ? 32  THR B HG23   1 
ATOM   3174  N  N      . ALA B 2 34  ? 2.338   -2.009  2.418   1.00 21.91  ? 33  ALA B N      1 
ATOM   3175  C  CA     . ALA B 2 34  ? 2.945   -3.140  3.117   1.00 19.82  ? 33  ALA B CA     1 
ATOM   3176  C  C      . ALA B 2 34  ? 4.096   -3.754  2.316   1.00 22.45  ? 33  ALA B C      1 
ATOM   3177  O  O      . ALA B 2 34  ? 5.143   -4.080  2.882   1.00 23.29  ? 33  ALA B O      1 
ATOM   3178  C  CB     . ALA B 2 34  ? 1.856   -4.171  3.440   1.00 23.62  ? 33  ALA B CB     1 
ATOM   3179  H  H      . ALA B 2 34  ? 1.496   -2.095  2.265   1.00 26.33  ? 33  ALA B H      1 
ATOM   3180  H  HA     . ALA B 2 34  ? 3.330   -2.838  3.955   1.00 23.82  ? 33  ALA B HA     1 
ATOM   3181  H  HB1    . ALA B 2 34  ? 2.255   -4.912  3.921   1.00 28.38  ? 33  ALA B HB1    1 
ATOM   3182  H  HB2    . ALA B 2 34  ? 1.175   -3.749  3.987   1.00 28.38  ? 33  ALA B HB2    1 
ATOM   3183  H  HB3    . ALA B 2 34  ? 1.464   -4.487  2.610   1.00 28.38  ? 33  ALA B HB3    1 
ATOM   3184  N  N      . GLU B 2 35  ? 3.932   -3.935  0.988   1.00 22.38  ? 34  GLU B N      1 
ATOM   3185  C  CA     . GLU B 2 35  ? 4.967   -4.622  0.202   1.00 22.83  ? 34  GLU B CA     1 
ATOM   3186  C  C      . GLU B 2 35  ? 6.219   -3.771  0.069   1.00 22.79  ? 34  GLU B C      1 
ATOM   3187  O  O      . GLU B 2 35  ? 7.335   -4.293  0.068   1.00 23.91  ? 34  GLU B O      1 
ATOM   3188  C  CB     . GLU B 2 35  ? 4.405   -4.979  -1.190  1.00 24.28  ? 34  GLU B CB     1 
ATOM   3189  C  CG     . GLU B 2 35  ? 5.440   -5.397  -2.250  1.00 28.26  ? 34  GLU B CG     1 
ATOM   3190  C  CD     . GLU B 2 35  ? 6.160   -6.677  -1.891  1.00 29.98  ? 34  GLU B CD     1 
ATOM   3191  O  OE1    . GLU B 2 35  ? 5.644   -7.383  -1.005  1.00 28.65  ? 34  GLU B OE1    1 
ATOM   3192  O  OE2    . GLU B 2 35  ? 7.241   -6.955  -2.480  1.00 31.70  ? 34  GLU B OE2    1 
ATOM   3193  H  H      . GLU B 2 35  ? 3.249   -3.675  0.535   1.00 26.89  ? 34  GLU B H      1 
ATOM   3194  H  HA     . GLU B 2 35  ? 5.215   -5.444  0.655   1.00 27.43  ? 34  GLU B HA     1 
ATOM   3195  H  HB2    . GLU B 2 35  ? 3.786   -5.720  -1.086  1.00 29.17  ? 34  GLU B HB2    1 
ATOM   3196  H  HB3    . GLU B 2 35  ? 3.938   -4.203  -1.536  1.00 29.17  ? 34  GLU B HB3    1 
ATOM   3197  H  HG2    . GLU B 2 35  ? 4.987   -5.534  -3.097  1.00 33.94  ? 34  GLU B HG2    1 
ATOM   3198  H  HG3    . GLU B 2 35  ? 6.103   -4.695  -2.338  1.00 33.94  ? 34  GLU B HG3    1 
ATOM   3199  N  N      . ASN B 2 36  ? 6.055   -2.453  -0.041  1.00 22.35  ? 35  ASN B N      1 
ATOM   3200  C  CA     . ASN B 2 36  ? 7.190   -1.552  0.026   1.00 18.99  ? 35  ASN B CA     1 
ATOM   3201  C  C      . ASN B 2 36  ? 8.010   -1.786  1.285   1.00 23.48  ? 35  ASN B C      1 
ATOM   3202  O  O      . ASN B 2 36  ? 9.230   -1.962  1.220   1.00 20.81  ? 35  ASN B O      1 
ATOM   3203  C  CB     . ASN B 2 36  ? 6.673   -0.115  -0.029  1.00 18.93  ? 35  ASN B CB     1 
ATOM   3204  C  CG     . ASN B 2 36  ? 7.755   0.899   -0.029  1.00 20.27  ? 35  ASN B CG     1 
ATOM   3205  O  OD1    . ASN B 2 36  ? 8.638   0.905   -0.888  1.00 18.88  ? 35  ASN B OD1    1 
ATOM   3206  N  ND2    . ASN B 2 36  ? 7.709   1.800   0.964   1.00 21.91  ? 35  ASN B ND2    1 
ATOM   3207  H  H      . ASN B 2 36  ? 5.298   -2.062  -0.155  1.00 26.85  ? 35  ASN B H      1 
ATOM   3208  H  HA     . ASN B 2 36  ? 7.776   -1.706  -0.732  1.00 22.82  ? 35  ASN B HA     1 
ATOM   3209  H  HB2    . ASN B 2 36  ? 6.156   0.002   -0.841  1.00 22.75  ? 35  ASN B HB2    1 
ATOM   3210  H  HB3    . ASN B 2 36  ? 6.113   0.047   0.746   1.00 22.75  ? 35  ASN B HB3    1 
ATOM   3211  H  HD21   . ASN B 2 36  ? 8.310   2.413   1.017   1.00 26.32  ? 35  ASN B HD21   1 
ATOM   3212  H  HD22   . ASN B 2 36  ? 7.078   1.765   1.547   1.00 26.32  ? 35  ASN B HD22   1 
ATOM   3213  N  N      . PHE B 2 37  ? 7.354   -1.779  2.446   1.00 21.09  ? 36  PHE B N      1 
ATOM   3214  C  CA     . PHE B 2 37  ? 8.102   -1.885  3.704   1.00 21.26  ? 36  PHE B CA     1 
ATOM   3215  C  C      . PHE B 2 37  ? 8.766   -3.258  3.821   1.00 20.02  ? 36  PHE B C      1 
ATOM   3216  O  O      . PHE B 2 37  ? 9.918   -3.360  4.270   1.00 21.39  ? 36  PHE B O      1 
ATOM   3217  C  CB     . PHE B 2 37  ? 7.164   -1.608  4.867   1.00 19.05  ? 36  PHE B CB     1 
ATOM   3218  C  CG     . PHE B 2 37  ? 7.859   -1.443  6.187   1.00 18.26  ? 36  PHE B CG     1 
ATOM   3219  C  CD1    . PHE B 2 37  ? 8.311   -0.187  6.584   1.00 17.49  ? 36  PHE B CD1    1 
ATOM   3220  C  CD2    . PHE B 2 37  ? 8.068   -2.533  7.014   1.00 19.32  ? 36  PHE B CD2    1 
ATOM   3221  C  CE1    . PHE B 2 37  ? 8.928   -0.034  7.793   1.00 21.02  ? 36  PHE B CE1    1 
ATOM   3222  C  CE2    . PHE B 2 37  ? 8.705   -2.385  8.243   1.00 23.37  ? 36  PHE B CE2    1 
ATOM   3223  C  CZ     . PHE B 2 37  ? 9.117   -1.119  8.614   1.00 18.61  ? 36  PHE B CZ     1 
ATOM   3224  H  H      . PHE B 2 37  ? 6.501   -1.715  2.534   1.00 25.34  ? 36  PHE B H      1 
ATOM   3225  H  HA     . PHE B 2 37  ? 8.808   -1.221  3.733   1.00 25.55  ? 36  PHE B HA     1 
ATOM   3226  H  HB2    . PHE B 2 37  ? 6.678   -0.789  4.686   1.00 22.89  ? 36  PHE B HB2    1 
ATOM   3227  H  HB3    . PHE B 2 37  ? 6.545   -2.350  4.951   1.00 22.89  ? 36  PHE B HB3    1 
ATOM   3228  H  HD1    . PHE B 2 37  ? 8.192   0.547   6.026   1.00 21.02  ? 36  PHE B HD1    1 
ATOM   3229  H  HD2    . PHE B 2 37  ? 7.779   -3.375  6.746   1.00 23.22  ? 36  PHE B HD2    1 
ATOM   3230  H  HE1    . PHE B 2 37  ? 9.222   0.807   8.060   1.00 25.26  ? 36  PHE B HE1    1 
ATOM   3231  H  HE2    . PHE B 2 37  ? 8.850   -3.117  8.799   1.00 28.08  ? 36  PHE B HE2    1 
ATOM   3232  H  HZ     . PHE B 2 37  ? 9.532   -0.999  9.438   1.00 22.37  ? 36  PHE B HZ     1 
ATOM   3233  N  N      . ARG B 2 38  ? 8.073   -4.308  3.380   1.00 21.87  ? 37  ARG B N      1 
ATOM   3234  C  CA     . ARG B 2 38  ? 8.632   -5.661  3.369   1.00 27.11  ? 37  ARG B CA     1 
ATOM   3235  C  C      . ARG B 2 38  ? 9.910   -5.716  2.551   1.00 26.33  ? 37  ARG B C      1 
ATOM   3236  O  O      . ARG B 2 38  ? 10.954  -6.170  3.020   1.00 26.51  ? 37  ARG B O      1 
ATOM   3237  C  CB     . ARG B 2 38  ? 7.602   -6.655  2.783   1.00 27.39  ? 37  ARG B CB     1 
ATOM   3238  C  CG     . ARG B 2 38  ? 8.001   -8.157  2.948   1.00 26.67  ? 37  ARG B CG     1 
ATOM   3239  C  CD     . ARG B 2 38  ? 7.270   -9.141  1.964   1.00 32.41  ? 37  ARG B CD     1 
ATOM   3240  N  NE     . ARG B 2 38  ? 7.568   -8.861  0.566   1.00 32.40  ? 37  ARG B NE     1 
ATOM   3241  C  CZ     . ARG B 2 38  ? 8.739   -9.081  -0.015  1.00 32.41  ? 37  ARG B CZ     1 
ATOM   3242  N  NH1    . ARG B 2 38  ? 9.718   -9.721  0.607   1.00 29.91  ? 37  ARG B NH1    1 
ATOM   3243  N  NH2    . ARG B 2 38  ? 8.938   -8.648  -1.257  1.00 36.25  ? 37  ARG B NH2    1 
ATOM   3244  H  H      . ARG B 2 38  ? 7.268   -4.265  3.078   1.00 26.28  ? 37  ARG B H      1 
ATOM   3245  H  HA     . ARG B 2 38  ? 8.831   -5.915  4.283   1.00 32.56  ? 37  ARG B HA     1 
ATOM   3246  H  HB2    . ARG B 2 38  ? 6.753   -6.525  3.234   1.00 32.90  ? 37  ARG B HB2    1 
ATOM   3247  H  HB3    . ARG B 2 38  ? 7.504   -6.479  1.835   1.00 32.90  ? 37  ARG B HB3    1 
ATOM   3248  H  HG2    . ARG B 2 38  ? 8.954   -8.243  2.791   1.00 32.04  ? 37  ARG B HG2    1 
ATOM   3249  H  HG3    . ARG B 2 38  ? 7.786   -8.437  3.852   1.00 32.04  ? 37  ARG B HG3    1 
ATOM   3250  H  HD2    . ARG B 2 38  ? 7.554   -10.049 2.155   1.00 38.92  ? 37  ARG B HD2    1 
ATOM   3251  H  HD3    . ARG B 2 38  ? 6.312   -9.061  2.089   1.00 38.92  ? 37  ARG B HD3    1 
ATOM   3252  H  HE     . ARG B 2 38  ? 6.939   -8.528  0.083   1.00 38.92  ? 37  ARG B HE     1 
ATOM   3253  H  HH11   . ARG B 2 38  ? 9.602   -10.006 1.411   1.00 35.92  ? 37  ARG B HH11   1 
ATOM   3254  H  HH12   . ARG B 2 38  ? 10.468  -9.851  0.208   1.00 35.92  ? 37  ARG B HH12   1 
ATOM   3255  H  HH21   . ARG B 2 38  ? 8.310   -8.232  -1.673  1.00 43.54  ? 37  ARG B HH21   1 
ATOM   3256  H  HH22   . ARG B 2 38  ? 9.693   -8.786  -1.645  1.00 43.54  ? 37  ARG B HH22   1 
ATOM   3257  N  N      . ALA B 2 39  ? 9.818   -5.310  1.279   1.00 25.18  ? 38  ALA B N      1 
ATOM   3258  C  CA     . ALA B 2 39  ? 10.982  -5.363  0.401   1.00 23.97  ? 38  ALA B CA     1 
ATOM   3259  C  C      . ALA B 2 39  ? 12.114  -4.504  0.927   1.00 25.78  ? 38  ALA B C      1 
ATOM   3260  O  O      . ALA B 2 39  ? 13.289  -4.864  0.796   1.00 25.48  ? 38  ALA B O      1 
ATOM   3261  C  CB     . ALA B 2 39  ? 10.589  -4.920  -1.007  1.00 23.54  ? 38  ALA B CB     1 
ATOM   3262  H  H      . ALA B 2 39  ? 9.104   -5.006  0.909   1.00 30.24  ? 38  ALA B H      1 
ATOM   3263  H  HA     . ALA B 2 39  ? 11.299  -6.279  0.357   1.00 28.79  ? 38  ALA B HA     1 
ATOM   3264  H  HB1    . ALA B 2 39  ? 11.367  -4.973  -1.584  1.00 28.28  ? 38  ALA B HB1    1 
ATOM   3265  H  HB2    . ALA B 2 39  ? 9.890   -5.506  -1.339  1.00 28.28  ? 38  ALA B HB2    1 
ATOM   3266  H  HB3    . ALA B 2 39  ? 10.265  -4.006  -0.972  1.00 28.28  ? 38  ALA B HB3    1 
ATOM   3267  N  N      . LEU B 2 40  ? 11.796  -3.340  1.501   1.00 24.22  ? 39  LEU B N      1 
ATOM   3268  C  CA     . LEU B 2 40  ? 12.868  -2.505  2.003   1.00 18.05  ? 39  LEU B CA     1 
ATOM   3269  C  C      . LEU B 2 40  ? 13.537  -3.170  3.215   1.00 19.99  ? 39  LEU B C      1 
ATOM   3270  O  O      . LEU B 2 40  ? 14.750  -3.035  3.421   1.00 23.25  ? 39  LEU B O      1 
ATOM   3271  C  CB     . LEU B 2 40  ? 12.334  -1.126  2.349   1.00 22.09  ? 39  LEU B CB     1 
ATOM   3272  C  CG     . LEU B 2 40  ? 11.870  -0.327  1.125   1.00 23.34  ? 39  LEU B CG     1 
ATOM   3273  C  CD1    . LEU B 2 40  ? 11.052  0.852   1.572   1.00 20.55  ? 39  LEU B CD1    1 
ATOM   3274  C  CD2    . LEU B 2 40  ? 13.089  0.082   0.286   1.00 21.54  ? 39  LEU B CD2    1 
ATOM   3275  H  H      . LEU B 2 40  ? 10.999  -3.031  1.605   1.00 29.10  ? 39  LEU B H      1 
ATOM   3276  H  HA     . LEU B 2 40  ? 13.543  -2.379  1.318   1.00 21.69  ? 39  LEU B HA     1 
ATOM   3277  H  HB2    . LEU B 2 40  ? 11.576  -1.225  2.946   1.00 26.55  ? 39  LEU B HB2    1 
ATOM   3278  H  HB3    . LEU B 2 40  ? 13.037  -0.620  2.786   1.00 26.55  ? 39  LEU B HB3    1 
ATOM   3279  H  HG     . LEU B 2 40  ? 11.299  -0.864  0.553   1.00 28.04  ? 39  LEU B HG     1 
ATOM   3280  H  HD11   . LEU B 2 40  ? 10.777  1.359   0.793   1.00 24.70  ? 39  LEU B HD11   1 
ATOM   3281  H  HD12   . LEU B 2 40  ? 10.272  0.531   2.051   1.00 24.70  ? 39  LEU B HD12   1 
ATOM   3282  H  HD13   . LEU B 2 40  ? 11.592  1.408   2.155   1.00 24.70  ? 39  LEU B HD13   1 
ATOM   3283  H  HD21   . LEU B 2 40  ? 12.815  0.742   -0.370  1.00 25.89  ? 39  LEU B HD21   1 
ATOM   3284  H  HD22   . LEU B 2 40  ? 13.764  0.458   0.872   1.00 25.89  ? 39  LEU B HD22   1 
ATOM   3285  H  HD23   . LEU B 2 40  ? 13.441  -0.703  -0.163  1.00 25.89  ? 39  LEU B HD23   1 
ATOM   3286  N  N      . SER B 2 41  ? 12.781  -3.955  3.963   1.00 21.65  ? 40  SER B N      1 
ATOM   3287  C  CA     . SER B 2 41  ? 13.348  -4.679  5.101   1.00 24.67  ? 40  SER B CA     1 
ATOM   3288  C  C      . SER B 2 41  ? 14.254  -5.826  4.654   1.00 26.78  ? 40  SER B C      1 
ATOM   3289  O  O      . SER B 2 41  ? 15.282  -6.074  5.296   1.00 27.69  ? 40  SER B O      1 
ATOM   3290  C  CB     . SER B 2 41  ? 12.201  -5.166  5.994   1.00 24.74  ? 40  SER B CB     1 
ATOM   3291  O  OG     . SER B 2 41  ? 11.472  -4.046  6.528   1.00 23.92  ? 40  SER B OG     1 
ATOM   3292  H  H      . SER B 2 41  ? 11.940  -4.090  3.840   1.00 26.02  ? 40  SER B H      1 
ATOM   3293  H  HA     . SER B 2 41  ? 13.906  -4.086  5.629   1.00 29.64  ? 40  SER B HA     1 
ATOM   3294  H  HB2    . SER B 2 41  ? 11.599  -5.714  5.466   1.00 29.72  ? 40  SER B HB2    1 
ATOM   3295  H  HB3    . SER B 2 41  ? 12.566  -5.685  6.726   1.00 29.72  ? 40  SER B HB3    1 
ATOM   3296  H  HG     . SER B 2 41  ? 11.201  -3.555  5.902   1.00 28.73  ? 40  SER B HG     1 
ATOM   3297  N  N      . THR B 2 42  ? 13.939  -6.483  3.536   1.00 28.48  ? 41  THR B N      1 
ATOM   3298  C  CA     . THR B 2 42  ? 14.805  -7.566  3.055   1.00 29.95  ? 41  THR B CA     1 
ATOM   3299  C  C      . THR B 2 42  ? 16.011  -7.077  2.268   1.00 30.62  ? 41  THR B C      1 
ATOM   3300  O  O      . THR B 2 42  ? 16.966  -7.843  2.083   1.00 34.76  ? 41  THR B O      1 
ATOM   3301  C  CB     . THR B 2 42  ? 14.050  -8.528  2.124   1.00 32.15  ? 41  THR B CB     1 
ATOM   3302  O  OG1    . THR B 2 42  ? 13.668  -7.807  0.924   1.00 31.50  ? 41  THR B OG1    1 
ATOM   3303  C  CG2    . THR B 2 42  ? 12.821  -9.125  2.806   1.00 29.03  ? 41  THR B CG2    1 
ATOM   3304  H  H      . THR B 2 42  ? 13.247  -6.327  3.049   1.00 34.20  ? 41  THR B H      1 
ATOM   3305  H  HA     . THR B 2 42  ? 15.096  -8.042  3.848   1.00 35.98  ? 41  THR B HA     1 
ATOM   3306  H  HB     . THR B 2 42  ? 14.622  -9.275  1.888   1.00 38.61  ? 41  THR B HB     1 
ATOM   3307  H  HG1    . THR B 2 42  ? 13.246  -8.315  0.406   1.00 37.83  ? 41  THR B HG1    1 
ATOM   3308  H  HG21   . THR B 2 42  ? 12.383  -9.753  2.211   1.00 34.87  ? 41  THR B HG21   1 
ATOM   3309  H  HG22   . THR B 2 42  ? 13.083  -9.589  3.616   1.00 34.87  ? 41  THR B HG22   1 
ATOM   3310  H  HG23   . THR B 2 42  ? 12.194  -8.420  3.036   1.00 34.87  ? 41  THR B HG23   1 
ATOM   3311  N  N      . GLY B 2 43  ? 15.964  -5.859  1.737   1.00 26.78  ? 42  GLY B N      1 
ATOM   3312  C  CA     . GLY B 2 43  ? 16.997  -5.377  0.855   1.00 28.94  ? 42  GLY B CA     1 
ATOM   3313  C  C      . GLY B 2 43  ? 16.992  -6.020  -0.514  1.00 29.59  ? 42  GLY B C      1 
ATOM   3314  O  O      . GLY B 2 43  ? 17.941  -5.827  -1.274  1.00 34.79  ? 42  GLY B O      1 
ATOM   3315  H  H      . GLY B 2 43  ? 15.334  -5.291  1.879   1.00 32.17  ? 42  GLY B H      1 
ATOM   3316  H  HA2    . GLY B 2 43  ? 16.886  -4.421  0.737   1.00 34.76  ? 42  GLY B HA2    1 
ATOM   3317  H  HA3    . GLY B 2 43  ? 17.860  -5.547  1.262   1.00 34.76  ? 42  GLY B HA3    1 
ATOM   3318  N  N      . GLU B 2 44  ? 15.944  -6.738  -0.861  1.00 30.98  ? 43  GLU B N      1 
ATOM   3319  C  CA     . GLU B 2 44  ? 15.998  -7.573  -2.063  1.00 35.65  ? 43  GLU B CA     1 
ATOM   3320  C  C      . GLU B 2 44  ? 16.059  -6.767  -3.360  1.00 39.32  ? 43  GLU B C      1 
ATOM   3321  O  O      . GLU B 2 44  ? 16.425  -7.316  -4.412  1.00 36.83  ? 43  GLU B O      1 
ATOM   3322  C  CB     . GLU B 2 44  ? 14.797  -8.505  -2.076  1.00 38.71  ? 43  GLU B CB     1 
ATOM   3323  C  CG     . GLU B 2 44  ? 13.458  -7.833  -2.312  1.00 35.49  ? 43  GLU B CG     1 
ATOM   3324  C  CD     . GLU B 2 44  ? 12.298  -8.757  -1.981  1.00 39.40  ? 43  GLU B CD     1 
ATOM   3325  O  OE1    . GLU B 2 44  ? 12.164  -9.166  -0.800  1.00 35.15  ? 43  GLU B OE1    1 
ATOM   3326  O  OE2    . GLU B 2 44  ? 11.526  -9.086  -2.906  1.00 40.65  ? 43  GLU B OE2    1 
ATOM   3327  H  H      . GLU B 2 44  ? 15.199  -6.765  -0.433  1.00 37.21  ? 43  GLU B H      1 
ATOM   3328  H  HA     . GLU B 2 44  ? 16.808  -8.107  -2.033  1.00 42.81  ? 43  GLU B HA     1 
ATOM   3329  H  HB2    . GLU B 2 44  ? 14.923  -9.156  -2.784  1.00 46.48  ? 43  GLU B HB2    1 
ATOM   3330  H  HB3    . GLU B 2 44  ? 14.748  -8.954  -1.218  1.00 46.48  ? 43  GLU B HB3    1 
ATOM   3331  H  HG2    . GLU B 2 44  ? 13.392  -7.046  -1.748  1.00 42.63  ? 43  GLU B HG2    1 
ATOM   3332  H  HG3    . GLU B 2 44  ? 13.388  -7.578  -3.246  1.00 42.63  ? 43  GLU B HG3    1 
ATOM   3333  N  N      . LYS B 2 45  ? 15.712  -5.490  -3.330  1.00 31.39  ? 44  LYS B N      1 
ATOM   3334  C  CA     . LYS B 2 45  ? 15.805  -4.675  -4.529  1.00 32.20  ? 44  LYS B CA     1 
ATOM   3335  C  C      . LYS B 2 45  ? 17.175  -4.061  -4.688  1.00 35.65  ? 44  LYS B C      1 
ATOM   3336  O  O      . LYS B 2 45  ? 17.375  -3.278  -5.618  1.00 39.77  ? 44  LYS B O      1 
ATOM   3337  C  CB     . LYS B 2 45  ? 14.749  -3.562  -4.506  1.00 30.56  ? 44  LYS B CB     1 
ATOM   3338  C  CG     . LYS B 2 45  ? 13.336  -4.038  -4.227  1.00 30.18  ? 44  LYS B CG     1 
ATOM   3339  C  CD     . LYS B 2 45  ? 12.767  -4.870  -5.372  1.00 33.34  ? 44  LYS B CD     1 
ATOM   3340  C  CE     . LYS B 2 45  ? 11.263  -5.032  -5.220  1.00 36.14  ? 44  LYS B CE     1 
ATOM   3341  N  NZ     . LYS B 2 45  ? 10.673  -5.979  -6.247  1.00 41.36  ? 44  LYS B NZ     1 
ATOM   3342  H  H      . LYS B 2 45  ? 15.422  -5.076  -2.633  1.00 37.70  ? 44  LYS B H      1 
ATOM   3343  H  HA     . LYS B 2 45  ? 15.622  -5.232  -5.301  1.00 38.68  ? 44  LYS B HA     1 
ATOM   3344  H  HB2    . LYS B 2 45  ? 14.986  -2.926  -3.813  1.00 36.71  ? 44  LYS B HB2    1 
ATOM   3345  H  HB3    . LYS B 2 45  ? 14.744  -3.124  -5.371  1.00 36.71  ? 44  LYS B HB3    1 
ATOM   3346  H  HG2    . LYS B 2 45  ? 13.338  -4.588  -3.427  1.00 36.25  ? 44  LYS B HG2    1 
ATOM   3347  H  HG3    . LYS B 2 45  ? 12.761  -3.268  -4.098  1.00 36.25  ? 44  LYS B HG3    1 
ATOM   3348  H  HD2    . LYS B 2 45  ? 12.946  -4.426  -6.215  1.00 40.04  ? 44  LYS B HD2    1 
ATOM   3349  H  HD3    . LYS B 2 45  ? 13.173  -5.751  -5.367  1.00 40.04  ? 44  LYS B HD3    1 
ATOM   3350  H  HE2    . LYS B 2 45  ? 11.069  -5.385  -4.338  1.00 43.41  ? 44  LYS B HE2    1 
ATOM   3351  H  HE3    . LYS B 2 45  ? 10.838  -4.167  -5.332  1.00 43.41  ? 44  LYS B HE3    1 
ATOM   3352  H  HZ1    . LYS B 2 45  ? 10.839  -5.681  -7.068  1.00 49.66  ? 44  LYS B HZ1    1 
ATOM   3353  H  HZ2    . LYS B 2 45  ? 11.032  -6.789  -6.155  1.00 49.66  ? 44  LYS B HZ2    1 
ATOM   3354  H  HZ3    . LYS B 2 45  ? 9.792   -6.040  -6.134  1.00 49.66  ? 44  LYS B HZ3    1 
ATOM   3355  N  N      . GLY B 2 46  ? 18.112  -4.375  -3.786  1.00 33.40  ? 45  GLY B N      1 
ATOM   3356  C  CA     . GLY B 2 46  ? 19.437  -3.788  -3.798  1.00 36.18  ? 45  GLY B CA     1 
ATOM   3357  C  C      . GLY B 2 46  ? 19.615  -2.585  -2.894  1.00 34.65  ? 45  GLY B C      1 
ATOM   3358  O  O      . GLY B 2 46  ? 20.693  -1.969  -2.915  1.00 31.10  ? 45  GLY B O      1 
ATOM   3359  H  H      . GLY B 2 46  ? 17.994  -4.939  -3.147  1.00 40.11  ? 45  GLY B H      1 
ATOM   3360  H  HA2    . GLY B 2 46  ? 20.078  -4.462  -3.521  1.00 43.45  ? 45  GLY B HA2    1 
ATOM   3361  H  HA3    . GLY B 2 46  ? 19.644  -3.509  -4.704  1.00 43.45  ? 45  GLY B HA3    1 
ATOM   3362  N  N      . PHE B 2 47  ? 18.592  -2.226  -2.113  1.00 30.80  ? 46  PHE B N      1 
ATOM   3363  C  CA     . PHE B 2 47  ? 18.642  -1.095  -1.190  1.00 29.56  ? 46  PHE B CA     1 
ATOM   3364  C  C      . PHE B 2 47  ? 17.582  -1.310  -0.121  1.00 28.86  ? 46  PHE B C      1 
ATOM   3365  O  O      . PHE B 2 47  ? 16.681  -2.129  -0.283  1.00 26.20  ? 46  PHE B O      1 
ATOM   3366  C  CB     . PHE B 2 47  ? 18.422  0.243   -1.909  1.00 29.61  ? 46  PHE B CB     1 
ATOM   3367  C  CG     . PHE B 2 47  ? 17.179  0.286   -2.795  1.00 31.34  ? 46  PHE B CG     1 
ATOM   3368  C  CD1    . PHE B 2 47  ? 15.951  0.668   -2.267  1.00 28.40  ? 46  PHE B CD1    1 
ATOM   3369  C  CD2    . PHE B 2 47  ? 17.249  -0.038  -4.154  1.00 33.18  ? 46  PHE B CD2    1 
ATOM   3370  C  CE1    . PHE B 2 47  ? 14.804  0.716   -3.061  1.00 29.27  ? 46  PHE B CE1    1 
ATOM   3371  C  CE2    . PHE B 2 47  ? 16.100  0.015   -4.965  1.00 32.38  ? 46  PHE B CE2    1 
ATOM   3372  C  CZ     . PHE B 2 47  ? 14.879  0.396   -4.419  1.00 32.34  ? 46  PHE B CZ     1 
ATOM   3373  H  H      . PHE B 2 47  ? 17.836  -2.636  -2.099  1.00 36.99  ? 46  PHE B H      1 
ATOM   3374  H  HA     . PHE B 2 47  ? 19.513  -1.062  -0.766  1.00 35.51  ? 46  PHE B HA     1 
ATOM   3375  H  HB2    . PHE B 2 47  ? 18.331  0.942   -1.243  1.00 35.57  ? 46  PHE B HB2    1 
ATOM   3376  H  HB3    . PHE B 2 47  ? 19.191  0.421   -2.474  1.00 35.57  ? 46  PHE B HB3    1 
ATOM   3377  H  HD1    . PHE B 2 47  ? 15.893  0.897   -1.368  1.00 34.11  ? 46  PHE B HD1    1 
ATOM   3378  H  HD2    . PHE B 2 47  ? 18.063  -0.291  -4.526  1.00 39.85  ? 46  PHE B HD2    1 
ATOM   3379  H  HE1    . PHE B 2 47  ? 13.989  0.961   -2.686  1.00 35.15  ? 46  PHE B HE1    1 
ATOM   3380  H  HE2    . PHE B 2 47  ? 16.158  -0.205  -5.867  1.00 38.89  ? 46  PHE B HE2    1 
ATOM   3381  H  HZ     . PHE B 2 47  ? 14.118  0.438   -4.953  1.00 38.84  ? 46  PHE B HZ     1 
ATOM   3382  N  N      . GLY B 2 48  ? 17.712  -0.598  0.998   1.00 26.82  ? 47  GLY B N      1 
ATOM   3383  C  CA     . GLY B 2 48  ? 16.679  -0.757  2.018   1.00 24.31  ? 47  GLY B CA     1 
ATOM   3384  C  C      . GLY B 2 48  ? 17.176  -0.309  3.379   1.00 22.04  ? 47  GLY B C      1 
ATOM   3385  O  O      . GLY B 2 48  ? 18.148  0.414   3.478   1.00 21.24  ? 47  GLY B O      1 
ATOM   3386  H  H      . GLY B 2 48  ? 18.349  -0.050  1.179   1.00 32.22  ? 47  GLY B H      1 
ATOM   3387  H  HA2    . GLY B 2 48  ? 15.903  -0.226  1.782   1.00 29.20  ? 47  GLY B HA2    1 
ATOM   3388  H  HA3    . GLY B 2 48  ? 16.418  -1.690  2.076   1.00 29.20  ? 47  GLY B HA3    1 
ATOM   3389  N  N      . TYR B 2 49  ? 16.460  -0.775  4.411   1.00 23.82  ? 48  TYR B N      1 
ATOM   3390  C  CA     . TYR B 2 49  ? 16.590  -0.227  5.760   1.00 21.42  ? 48  TYR B CA     1 
ATOM   3391  C  C      . TYR B 2 49  ? 17.867  -0.626  6.473   1.00 24.50  ? 48  TYR B C      1 
ATOM   3392  O  O      . TYR B 2 49  ? 18.301  0.098   7.361   1.00 20.03  ? 48  TYR B O      1 
ATOM   3393  C  CB     . TYR B 2 49  ? 15.391  -0.666  6.613   1.00 20.05  ? 48  TYR B CB     1 
ATOM   3394  C  CG     . TYR B 2 49  ? 14.083  -0.036  6.202   1.00 17.41  ? 48  TYR B CG     1 
ATOM   3395  C  CD1    . TYR B 2 49  ? 13.989  1.343   5.948   1.00 20.27  ? 48  TYR B CD1    1 
ATOM   3396  C  CD2    . TYR B 2 49  ? 12.940  -0.809  6.085   1.00 16.31  ? 48  TYR B CD2    1 
ATOM   3397  C  CE1    . TYR B 2 49  ? 12.789  1.920   5.590   1.00 18.15  ? 48  TYR B CE1    1 
ATOM   3398  C  CE2    . TYR B 2 49  ? 11.743  -0.242  5.697   1.00 19.90  ? 48  TYR B CE2    1 
ATOM   3399  C  CZ     . TYR B 2 49  ? 11.666  1.128   5.469   1.00 17.41  ? 48  TYR B CZ     1 
ATOM   3400  O  OH     . TYR B 2 49  ? 10.460  1.662   5.104   1.00 18.67  ? 48  TYR B OH     1 
ATOM   3401  H  H      . TYR B 2 49  ? 15.888  -1.414  4.353   1.00 28.62  ? 48  TYR B H      1 
ATOM   3402  H  HA     . TYR B 2 49  ? 16.603  0.739   5.669   1.00 25.74  ? 48  TYR B HA     1 
ATOM   3403  H  HB2    . TYR B 2 49  ? 15.291  -1.628  6.539   1.00 24.09  ? 48  TYR B HB2    1 
ATOM   3404  H  HB3    . TYR B 2 49  ? 15.559  -0.420  7.536   1.00 24.09  ? 48  TYR B HB3    1 
ATOM   3405  H  HD1    . TYR B 2 49  ? 14.748  1.875   6.023   1.00 24.36  ? 48  TYR B HD1    1 
ATOM   3406  H  HD2    . TYR B 2 49  ? 12.980  -1.719  6.270   1.00 19.60  ? 48  TYR B HD2    1 
ATOM   3407  H  HE1    . TYR B 2 49  ? 12.737  2.835   5.432   1.00 21.82  ? 48  TYR B HE1    1 
ATOM   3408  H  HE2    . TYR B 2 49  ? 10.989  -0.775  5.588   1.00 23.92  ? 48  TYR B HE2    1 
ATOM   3409  H  HH     . TYR B 2 49  ? 10.566  2.448   4.826   1.00 22.44  ? 48  TYR B HH     1 
ATOM   3410  N  N      . LYS B 2 50  ? 18.454  -1.778  6.157   1.00 22.32  ? 49  LYS B N      1 
ATOM   3411  C  CA     . LYS B 2 50  ? 19.607  -2.238  6.936   1.00 22.66  ? 49  LYS B CA     1 
ATOM   3412  C  C      . LYS B 2 50  ? 20.683  -1.161  6.996   1.00 21.92  ? 49  LYS B C      1 
ATOM   3413  O  O      . LYS B 2 50  ? 21.107  -0.635  5.964   1.00 25.44  ? 49  LYS B O      1 
ATOM   3414  C  CB     . LYS B 2 50  ? 20.153  -3.518  6.308   1.00 25.32  ? 49  LYS B CB     1 
ATOM   3415  C  CG     . LYS B 2 50  ? 21.442  -4.035  6.968   1.00 30.87  ? 49  LYS B CG     1 
ATOM   3416  C  CD     . LYS B 2 50  ? 21.819  -5.427  6.469   1.00 32.74  ? 49  LYS B CD     1 
ATOM   3417  C  CE     . LYS B 2 50  ? 22.646  -6.168  7.518   1.00 37.46  ? 49  LYS B CE     1 
ATOM   3418  N  NZ     . LYS B 2 50  ? 23.240  -7.435  6.988   1.00 41.85  ? 49  LYS B NZ     1 
ATOM   3419  H  H      . LYS B 2 50  ? 18.214  -2.298  5.515   1.00 26.82  ? 49  LYS B H      1 
ATOM   3420  H  HA     . LYS B 2 50  ? 19.336  -2.432  7.847   1.00 27.23  ? 49  LYS B HA     1 
ATOM   3421  H  HB2    . LYS B 2 50  ? 19.481  -4.214  6.386   1.00 30.42  ? 49  LYS B HB2    1 
ATOM   3422  H  HB3    . LYS B 2 50  ? 20.347  -3.348  5.374   1.00 30.42  ? 49  LYS B HB3    1 
ATOM   3423  H  HG2    . LYS B 2 50  ? 22.172  -3.431  6.761   1.00 37.07  ? 49  LYS B HG2    1 
ATOM   3424  H  HG3    . LYS B 2 50  ? 21.313  -4.083  7.928   1.00 37.07  ? 49  LYS B HG3    1 
ATOM   3425  H  HD2    . LYS B 2 50  ? 21.014  -5.938  6.293   1.00 39.32  ? 49  LYS B HD2    1 
ATOM   3426  H  HD3    . LYS B 2 50  ? 22.347  -5.349  5.659   1.00 39.32  ? 49  LYS B HD3    1 
ATOM   3427  H  HE2    . LYS B 2 50  ? 23.372  -5.595  7.812   1.00 44.99  ? 49  LYS B HE2    1 
ATOM   3428  H  HE3    . LYS B 2 50  ? 22.076  -6.394  8.269   1.00 44.99  ? 49  LYS B HE3    1 
ATOM   3429  H  HZ1    . LYS B 2 50  ? 23.705  -7.843  7.627   1.00 50.25  ? 49  LYS B HZ1    1 
ATOM   3430  H  HZ2    . LYS B 2 50  ? 22.595  -7.979  6.707   1.00 50.25  ? 49  LYS B HZ2    1 
ATOM   3431  H  HZ3    . LYS B 2 50  ? 23.783  -7.254  6.306   1.00 50.25  ? 49  LYS B HZ3    1 
ATOM   3432  N  N      . GLY B 2 51  ? 21.154  -0.827  8.226   1.00 22.76  ? 50  GLY B N      1 
ATOM   3433  C  CA     . GLY B 2 51  ? 22.188  0.168   8.394   1.00 22.84  ? 50  GLY B CA     1 
ATOM   3434  C  C      . GLY B 2 51  ? 21.742  1.598   8.578   1.00 24.95  ? 50  GLY B C      1 
ATOM   3435  O  O      . GLY B 2 51  ? 22.581  2.456   8.902   1.00 24.79  ? 50  GLY B O      1 
ATOM   3436  H  H      . GLY B 2 51  ? 20.877  -1.175  8.962   1.00 27.34  ? 50  GLY B H      1 
ATOM   3437  H  HA2    . GLY B 2 51  ? 22.713  -0.071  9.174   1.00 27.44  ? 50  GLY B HA2    1 
ATOM   3438  H  HA3    . GLY B 2 51  ? 22.759  0.145   7.610   1.00 27.44  ? 50  GLY B HA3    1 
ATOM   3439  N  N      . SER B 2 52  ? 20.475  1.907   8.310   1.00 20.13  ? 51  SER B N      1 
ATOM   3440  C  CA     . SER B 2 52  ? 19.958  3.243   8.482   1.00 23.17  ? 51  SER B CA     1 
ATOM   3441  C  C      . SER B 2 52  ? 19.603  3.488   9.952   1.00 20.93  ? 51  SER B C      1 
ATOM   3442  O  O      . SER B 2 52  ? 19.607  2.580   10.797  1.00 22.05  ? 51  SER B O      1 
ATOM   3443  C  CB     . SER B 2 52  ? 18.741  3.481   7.587   1.00 18.80  ? 51  SER B CB     1 
ATOM   3444  O  OG     . SER B 2 52  ? 17.700  2.567   7.839   1.00 20.95  ? 51  SER B OG     1 
ATOM   3445  H  H      . SER B 2 52  ? 19.891  1.345   8.022   1.00 24.19  ? 51  SER B H      1 
ATOM   3446  H  HA     . SER B 2 52  ? 20.641  3.881   8.220   1.00 27.84  ? 51  SER B HA     1 
ATOM   3447  H  HB2    . SER B 2 52  ? 18.410  4.378   7.747   1.00 22.60  ? 51  SER B HB2    1 
ATOM   3448  H  HB3    . SER B 2 52  ? 19.015  3.388   6.661   1.00 22.60  ? 51  SER B HB3    1 
ATOM   3449  H  HG     . SER B 2 52  ? 17.964  1.784   7.692   1.00 25.17  ? 51  SER B HG     1 
ATOM   3450  N  N      . CYS B 2 53  ? 19.338  4.730   10.248  1.00 20.26  ? 52  CYS B N      1 
ATOM   3451  C  CA     . CYS B 2 53  ? 19.158  5.145   11.619  1.00 20.61  ? 52  CYS B CA     1 
ATOM   3452  C  C      . CYS B 2 53  ? 17.744  5.645   11.857  1.00 20.01  ? 52  CYS B C      1 
ATOM   3453  O  O      . CYS B 2 53  ? 16.986  5.983   10.936  1.00 18.24  ? 52  CYS B O      1 
ATOM   3454  C  CB     . CYS B 2 53  ? 20.125  6.238   12.010  1.00 25.60  ? 52  CYS B CB     1 
ATOM   3455  S  SG     . CYS B 2 53  ? 19.902  7.795   11.207  1.00 44.37  ? 52  CYS B SG     1 
ATOM   3456  H  H      . CYS B 2 53  ? 19.255  5.361   9.670   1.00 24.34  ? 52  CYS B H      1 
ATOM   3457  H  HA     . CYS B 2 53  ? 19.311  4.370   12.183  1.00 24.76  ? 52  CYS B HA     1 
ATOM   3458  H  HB2    . CYS B 2 53  ? 20.038  6.393   12.964  1.00 30.76  ? 52  CYS B HB2    1 
ATOM   3459  H  HB3    . CYS B 2 53  ? 21.023  5.936   11.804  1.00 30.76  ? 52  CYS B HB3    1 
ATOM   3460  H  HG     . CYS B 2 53  ? 18.797  8.200   11.439  1.00 53.28  ? 52  CYS B HG     1 
ATOM   3461  N  N      . PHE B 2 54  ? 17.382  5.660   13.130  1.00 20.50  ? 53  PHE B N      1 
ATOM   3462  C  CA     . PHE B 2 54  ? 16.192  6.393   13.573  1.00 18.16  ? 53  PHE B CA     1 
ATOM   3463  C  C      . PHE B 2 54  ? 16.656  7.814   13.860  1.00 20.06  ? 53  PHE B C      1 
ATOM   3464  O  O      . PHE B 2 54  ? 17.308  8.084   14.876  1.00 20.92  ? 53  PHE B O      1 
ATOM   3465  C  CB     . PHE B 2 54  ? 15.564  5.726   14.800  1.00 16.35  ? 53  PHE B CB     1 
ATOM   3466  C  CG     . PHE B 2 54  ? 14.723  4.521   14.474  1.00 19.19  ? 53  PHE B CG     1 
ATOM   3467  C  CD1    . PHE B 2 54  ? 15.320  3.300   14.229  1.00 18.67  ? 53  PHE B CD1    1 
ATOM   3468  C  CD2    . PHE B 2 54  ? 13.336  4.604   14.412  1.00 19.35  ? 53  PHE B CD2    1 
ATOM   3469  C  CE1    . PHE B 2 54  ? 14.576  2.189   13.956  1.00 18.94  ? 53  PHE B CE1    1 
ATOM   3470  C  CE2    . PHE B 2 54  ? 12.584  3.481   14.119  1.00 19.52  ? 53  PHE B CE2    1 
ATOM   3471  C  CZ     . PHE B 2 54  ? 13.207  2.274   13.896  1.00 17.60  ? 53  PHE B CZ     1 
ATOM   3472  H  H      . PHE B 2 54  ? 17.806  5.256   13.760  1.00 24.64  ? 53  PHE B H      1 
ATOM   3473  H  HA     . PHE B 2 54  ? 15.514  6.406   12.879  1.00 21.82  ? 53  PHE B HA     1 
ATOM   3474  H  HB2    . PHE B 2 54  ? 16.274  5.440   15.396  1.00 19.65  ? 53  PHE B HB2    1 
ATOM   3475  H  HB3    . PHE B 2 54  ? 14.995  6.372   15.247  1.00 19.65  ? 53  PHE B HB3    1 
ATOM   3476  H  HD1    . PHE B 2 54  ? 16.248  3.234   14.251  1.00 22.44  ? 53  PHE B HD1    1 
ATOM   3477  H  HD2    . PHE B 2 54  ? 12.913  5.418   14.568  1.00 23.25  ? 53  PHE B HD2    1 
ATOM   3478  H  HE1    . PHE B 2 54  ? 14.997  1.373   13.811  1.00 22.76  ? 53  PHE B HE1    1 
ATOM   3479  H  HE2    . PHE B 2 54  ? 11.657  3.542   14.072  1.00 23.46  ? 53  PHE B HE2    1 
ATOM   3480  H  HZ     . PHE B 2 54  ? 12.701  1.517   13.705  1.00 21.16  ? 53  PHE B HZ     1 
ATOM   3481  N  N      . HIS B 2 55  ? 16.358  8.718   12.958  1.00 15.05  ? 54  HIS B N      1 
ATOM   3482  C  CA     . HIS B 2 55  ? 16.894  10.054  13.042  1.00 15.45  ? 54  HIS B CA     1 
ATOM   3483  C  C      . HIS B 2 55  ? 16.092  10.958  13.935  1.00 17.43  ? 54  HIS B C      1 
ATOM   3484  O  O      . HIS B 2 55  ? 16.591  12.024  14.319  1.00 17.73  ? 54  HIS B O      1 
ATOM   3485  C  CB     . HIS B 2 55  ? 17.004  10.686  11.671  1.00 18.57  ? 54  HIS B CB     1 
ATOM   3486  C  CG     . HIS B 2 55  ? 15.714  10.829  10.951  1.00 17.74  ? 54  HIS B CG     1 
ATOM   3487  N  ND1    . HIS B 2 55  ? 15.139  9.796   10.267  1.00 17.35  ? 54  HIS B ND1    1 
ATOM   3488  C  CD2    . HIS B 2 55  ? 14.914  11.902  10.765  1.00 17.42  ? 54  HIS B CD2    1 
ATOM   3489  C  CE1    . HIS B 2 55  ? 14.033  10.214  9.689   1.00 16.08  ? 54  HIS B CE1    1 
ATOM   3490  N  NE2    . HIS B 2 55  ? 13.868  11.492  9.985   1.00 16.61  ? 54  HIS B NE2    1 
ATOM   3491  H  H      . HIS B 2 55  ? 15.844  8.582   12.282  1.00 18.10  ? 54  HIS B H      1 
ATOM   3492  H  HA     . HIS B 2 55  ? 17.791  9.990   13.404  1.00 18.57  ? 54  HIS B HA     1 
ATOM   3493  H  HB2    . HIS B 2 55  ? 17.384  11.573  11.770  1.00 22.32  ? 54  HIS B HB2    1 
ATOM   3494  H  HB3    . HIS B 2 55  ? 17.586  10.135  11.123  1.00 22.32  ? 54  HIS B HB3    1 
ATOM   3495  H  HD1    . HIS B 2 55  ? 15.452  8.996   10.221  1.00 20.85  ? 54  HIS B HD1    1 
ATOM   3496  H  HD2    . HIS B 2 55  ? 15.050  12.757  11.103  1.00 20.94  ? 54  HIS B HD2    1 
ATOM   3497  H  HE1    . HIS B 2 55  ? 13.465  9.699   9.163   1.00 19.33  ? 54  HIS B HE1    1 
ATOM   3498  N  N      . ARG B 2 56  ? 14.840  10.606  14.225  1.00 17.92  ? 55  ARG B N      1 
ATOM   3499  C  CA     . ARG B 2 56  ? 13.972  11.494  14.973  1.00 14.64  ? 55  ARG B CA     1 
ATOM   3500  C  C      . ARG B 2 56  ? 13.186  10.707  16.002  1.00 18.08  ? 55  ARG B C      1 
ATOM   3501  O  O      . ARG B 2 56  ? 12.415  9.813   15.651  1.00 18.22  ? 55  ARG B O      1 
ATOM   3502  C  CB     . ARG B 2 56  ? 12.984  12.216  14.062  1.00 17.16  ? 55  ARG B CB     1 
ATOM   3503  C  CG     . ARG B 2 56  ? 11.928  12.983  14.825  1.00 17.19  ? 55  ARG B CG     1 
ATOM   3504  C  CD     . ARG B 2 56  ? 10.994  13.612  13.824  1.00 16.29  ? 55  ARG B CD     1 
ATOM   3505  N  NE     . ARG B 2 56  ? 11.687  14.692  13.134  1.00 17.71  ? 55  ARG B NE     1 
ATOM   3506  C  CZ     . ARG B 2 56  ? 11.338  15.149  11.944  1.00 20.37  ? 55  ARG B CZ     1 
ATOM   3507  N  NH1    . ARG B 2 56  ? 10.316  14.628  11.281  1.00 18.17  ? 55  ARG B NH1    1 
ATOM   3508  N  NH2    . ARG B 2 56  ? 12.043  16.131  11.398  1.00 20.31  ? 55  ARG B NH2    1 
ATOM   3509  H  H      . ARG B 2 56  ? 14.478  9.860   13.998  1.00 21.53  ? 55  ARG B H      1 
ATOM   3510  H  HA     . ARG B 2 56  ? 14.536  12.139  15.428  1.00 17.60  ? 55  ARG B HA     1 
ATOM   3511  H  HB2    . ARG B 2 56  ? 13.470  12.846  13.507  1.00 20.63  ? 55  ARG B HB2    1 
ATOM   3512  H  HB3    . ARG B 2 56  ? 12.535  11.561  13.504  1.00 20.63  ? 55  ARG B HB3    1 
ATOM   3513  H  HG2    . ARG B 2 56  ? 11.426  12.382  15.397  1.00 20.66  ? 55  ARG B HG2    1 
ATOM   3514  H  HG3    . ARG B 2 56  ? 12.341  13.680  15.358  1.00 20.66  ? 55  ARG B HG3    1 
ATOM   3515  H  HD2    . ARG B 2 56  ? 10.714  12.950  13.173  1.00 19.59  ? 55  ARG B HD2    1 
ATOM   3516  H  HD3    . ARG B 2 56  ? 10.219  13.976  14.280  1.00 19.59  ? 55  ARG B HD3    1 
ATOM   3517  H  HE     . ARG B 2 56  ? 12.363  15.053  13.523  1.00 21.29  ? 55  ARG B HE     1 
ATOM   3518  H  HH11   . ARG B 2 56  ? 9.866   13.981  11.625  1.00 21.84  ? 55  ARG B HH11   1 
ATOM   3519  H  HH12   . ARG B 2 56  ? 10.102  14.938  10.508  1.00 21.84  ? 55  ARG B HH12   1 
ATOM   3520  H  HH21   . ARG B 2 56  ? 12.717  16.462  11.818  1.00 24.40  ? 55  ARG B HH21   1 
ATOM   3521  H  HH22   . ARG B 2 56  ? 11.826  16.437  10.624  1.00 24.40  ? 55  ARG B HH22   1 
ATOM   3522  N  N      . ILE B 2 57  ? 13.395  11.024  17.259  1.00 16.57  ? 56  ILE B N      1 
ATOM   3523  C  CA     . ILE B 2 57  ? 12.780  10.286  18.347  1.00 14.40  ? 56  ILE B CA     1 
ATOM   3524  C  C      . ILE B 2 57  ? 12.268  11.330  19.325  1.00 17.94  ? 56  ILE B C      1 
ATOM   3525  O  O      . ILE B 2 57  ? 13.059  12.078  19.916  1.00 17.07  ? 56  ILE B O      1 
ATOM   3526  C  CB     . ILE B 2 57  ? 13.711  9.307   19.063  1.00 16.07  ? 56  ILE B CB     1 
ATOM   3527  C  CG1    . ILE B 2 57  ? 14.132  8.191   18.113  1.00 18.39  ? 56  ILE B CG1    1 
ATOM   3528  C  CG2    . ILE B 2 57  ? 13.035  8.719   20.315  1.00 18.19  ? 56  ILE B CG2    1 
ATOM   3529  C  CD1    . ILE B 2 57  ? 15.111  7.265   18.683  1.00 20.13  ? 56  ILE B CD1    1 
ATOM   3530  H  H      . ILE B 2 57  ? 13.896  11.674  17.516  1.00 19.92  ? 56  ILE B H      1 
ATOM   3531  H  HA     . ILE B 2 57  ? 12.049  9.755   17.994  1.00 17.32  ? 56  ILE B HA     1 
ATOM   3532  H  HB     . ILE B 2 57  ? 14.500  9.795   19.345  1.00 19.32  ? 56  ILE B HB     1 
ATOM   3533  H  HG12   . ILE B 2 57  ? 13.347  7.676   17.868  1.00 22.10  ? 56  ILE B HG12   1 
ATOM   3534  H  HG13   . ILE B 2 57  ? 14.528  8.588   17.321  1.00 22.10  ? 56  ILE B HG13   1 
ATOM   3535  H  HG21   . ILE B 2 57  ? 13.624  8.056   20.710  1.00 21.86  ? 56  ILE B HG21   1 
ATOM   3536  H  HG22   . ILE B 2 57  ? 12.870  9.434   20.950  1.00 21.86  ? 56  ILE B HG22   1 
ATOM   3537  H  HG23   . ILE B 2 57  ? 12.197  8.305   20.057  1.00 21.86  ? 56  ILE B HG23   1 
ATOM   3538  H  HD11   . ILE B 2 57  ? 15.528  6.764   17.965  1.00 24.19  ? 56  ILE B HD11   1 
ATOM   3539  H  HD12   . ILE B 2 57  ? 15.782  7.773   19.165  1.00 24.19  ? 56  ILE B HD12   1 
ATOM   3540  H  HD13   . ILE B 2 57  ? 14.657  6.659   19.289  1.00 24.19  ? 56  ILE B HD13   1 
ATOM   3541  N  N      . ILE B 2 58  ? 10.957  11.377  19.521  1.00 15.55  ? 57  ILE B N      1 
ATOM   3542  C  CA     . ILE B 2 58  ? 10.349  12.393  20.365  1.00 16.01  ? 57  ILE B CA     1 
ATOM   3543  C  C      . ILE B 2 58  ? 9.561   11.694  21.453  1.00 18.58  ? 57  ILE B C      1 
ATOM   3544  O  O      . ILE B 2 58  ? 8.504   11.105  21.209  1.00 17.68  ? 57  ILE B O      1 
ATOM   3545  C  CB     . ILE B 2 58  ? 9.471   13.365  19.549  1.00 14.78  ? 57  ILE B CB     1 
ATOM   3546  C  CG1    . ILE B 2 58  ? 10.337  14.092  18.513  1.00 15.82  ? 57  ILE B CG1    1 
ATOM   3547  C  CG2    . ILE B 2 58  ? 8.828   14.368  20.516  1.00 18.95  ? 57  ILE B CG2    1 
ATOM   3548  C  CD1    . ILE B 2 58  ? 9.574   15.013  17.660  1.00 20.52  ? 57  ILE B CD1    1 
ATOM   3549  H  H      . ILE B 2 58  ? 10.397  10.826  19.172  1.00 18.70  ? 57  ILE B H      1 
ATOM   3550  H  HA     . ILE B 2 58  ? 11.045  12.916  20.791  1.00 19.25  ? 57  ILE B HA     1 
ATOM   3551  H  HB     . ILE B 2 58  ? 8.777   12.877  19.079  1.00 17.61  ? 57  ILE B HB     1 
ATOM   3552  H  HG12   . ILE B 2 58  ? 11.014  14.608  18.978  1.00 19.02  ? 57  ILE B HG12   1 
ATOM   3553  H  HG13   . ILE B 2 58  ? 10.758  13.433  17.939  1.00 19.02  ? 57  ILE B HG13   1 
ATOM   3554  H  HG21   . ILE B 2 58  ? 8.359   15.045  20.004  1.00 22.78  ? 57  ILE B HG21   1 
ATOM   3555  H  HG22   . ILE B 2 58  ? 8.204   13.897  21.091  1.00 22.78  ? 57  ILE B HG22   1 
ATOM   3556  H  HG23   . ILE B 2 58  ? 9.523   14.780  21.052  1.00 22.78  ? 57  ILE B HG23   1 
ATOM   3557  H  HD11   . ILE B 2 58  ? 10.112  15.246  16.887  1.00 24.66  ? 57  ILE B HD11   1 
ATOM   3558  H  HD12   . ILE B 2 58  ? 8.757   14.575  17.374  1.00 24.66  ? 57  ILE B HD12   1 
ATOM   3559  H  HD13   . ILE B 2 58  ? 9.361   15.811  18.168  1.00 24.66  ? 57  ILE B HD13   1 
ATOM   3560  N  N      . PRO B 2 59  ? 10.074  11.679  22.673  1.00 17.37  ? 58  PRO B N      1 
ATOM   3561  C  CA     . PRO B 2 59  ? 9.399   10.932  23.726  1.00 18.75  ? 58  PRO B CA     1 
ATOM   3562  C  C      . PRO B 2 59  ? 7.986   11.430  23.940  1.00 20.09  ? 58  PRO B C      1 
ATOM   3563  O  O      . PRO B 2 59  ? 7.716   12.639  23.985  1.00 20.01  ? 58  PRO B O      1 
ATOM   3564  C  CB     . PRO B 2 59  ? 10.296  11.178  24.951  1.00 20.21  ? 58  PRO B CB     1 
ATOM   3565  C  CG     . PRO B 2 59  ? 11.635  11.272  24.350  1.00 17.73  ? 58  PRO B CG     1 
ATOM   3566  C  CD     . PRO B 2 59  ? 11.440  12.080  23.086  1.00 19.19  ? 58  PRO B CD     1 
ATOM   3567  H  HA     . PRO B 2 59  ? 9.374   9.983   23.524  1.00 22.53  ? 58  PRO B HA     1 
ATOM   3568  H  HB2    . PRO B 2 59  ? 10.046  12.003  25.395  1.00 24.29  ? 58  PRO B HB2    1 
ATOM   3569  H  HB3    . PRO B 2 59  ? 10.235  10.436  25.572  1.00 24.29  ? 58  PRO B HB3    1 
ATOM   3570  H  HG2    . PRO B 2 59  ? 12.240  11.723  24.960  1.00 21.31  ? 58  PRO B HG2    1 
ATOM   3571  H  HG3    . PRO B 2 59  ? 11.969  10.385  24.146  1.00 21.31  ? 58  PRO B HG3    1 
ATOM   3572  H  HD2    . PRO B 2 59  ? 11.486  13.032  23.269  1.00 23.06  ? 58  PRO B HD2    1 
ATOM   3573  H  HD3    . PRO B 2 59  ? 12.095  11.839  22.412  1.00 23.06  ? 58  PRO B HD3    1 
ATOM   3574  N  N      . GLY B 2 60  ? 7.099   10.471  24.106  1.00 19.43  ? 59  GLY B N      1 
ATOM   3575  C  CA     . GLY B 2 60  ? 5.695   10.749  24.243  1.00 20.35  ? 59  GLY B CA     1 
ATOM   3576  C  C      . GLY B 2 60  ? 4.925   10.688  22.952  1.00 20.27  ? 59  GLY B C      1 
ATOM   3577  O  O      . GLY B 2 60  ? 3.679   10.694  22.995  1.00 20.93  ? 59  GLY B O      1 
ATOM   3578  H  H      . GLY B 2 60  ? 7.294   9.634   24.143  1.00 23.36  ? 59  GLY B H      1 
ATOM   3579  H  HA2    . GLY B 2 60  ? 5.306   10.103  24.853  1.00 24.46  ? 59  GLY B HA2    1 
ATOM   3580  H  HA3    . GLY B 2 60  ? 5.586   11.639  24.613  1.00 24.46  ? 59  GLY B HA3    1 
ATOM   3581  N  N      . PHE B 2 61  ? 5.610   10.538  21.824  1.00 18.83  ? 60  PHE B N      1 
ATOM   3582  C  CA     . PHE B 2 61  ? 4.927   10.567  20.541  1.00 16.42  ? 60  PHE B CA     1 
ATOM   3583  C  C      . PHE B 2 61  ? 5.365   9.465   19.582  1.00 16.50  ? 60  PHE B C      1 
ATOM   3584  O  O      . PHE B 2 61  ? 4.547   8.596   19.237  1.00 16.47  ? 60  PHE B O      1 
ATOM   3585  C  CB     . PHE B 2 61  ? 5.106   11.953  19.925  1.00 19.31  ? 60  PHE B CB     1 
ATOM   3586  C  CG     . PHE B 2 61  ? 4.431   13.042  20.693  1.00 17.38  ? 60  PHE B CG     1 
ATOM   3587  C  CD1    . PHE B 2 61  ? 3.080   13.288  20.557  1.00 23.58  ? 60  PHE B CD1    1 
ATOM   3588  C  CD2    . PHE B 2 61  ? 5.178   13.847  21.558  1.00 21.93  ? 60  PHE B CD2    1 
ATOM   3589  C  CE1    . PHE B 2 61  ? 2.466   14.337  21.321  1.00 24.24  ? 60  PHE B CE1    1 
ATOM   3590  C  CE2    . PHE B 2 61  ? 4.601   14.881  22.275  1.00 24.94  ? 60  PHE B CE2    1 
ATOM   3591  C  CZ     . PHE B 2 61  ? 3.248   15.132  22.147  1.00 26.82  ? 60  PHE B CZ     1 
ATOM   3592  H  H      . PHE B 2 61  ? 6.460   10.420  21.777  1.00 22.63  ? 60  PHE B H      1 
ATOM   3593  H  HA     . PHE B 2 61  ? 3.984   10.395  20.689  1.00 19.53  ? 60  PHE B HA     1 
ATOM   3594  H  HB2    . PHE B 2 61  ? 6.053   12.159  19.888  1.00 23.20  ? 60  PHE B HB2    1 
ATOM   3595  H  HB3    . PHE B 2 61  ? 4.732   11.947  19.029  1.00 23.20  ? 60  PHE B HB3    1 
ATOM   3596  H  HD1    . PHE B 2 61  ? 2.569   12.775  19.973  1.00 28.32  ? 60  PHE B HD1    1 
ATOM   3597  H  HD2    . PHE B 2 61  ? 6.088   13.684  21.654  1.00 26.35  ? 60  PHE B HD2    1 
ATOM   3598  H  HE1    . PHE B 2 61  ? 1.549   14.484  21.262  1.00 29.13  ? 60  PHE B HE1    1 
ATOM   3599  H  HE2    . PHE B 2 61  ? 5.122   15.404  22.841  1.00 29.96  ? 60  PHE B HE2    1 
ATOM   3600  H  HZ     . PHE B 2 61  ? 2.861   15.835  22.616  1.00 32.21  ? 60  PHE B HZ     1 
ATOM   3601  N  N      . MET B 2 62  ? 6.616   9.474   19.134  1.00 16.03  ? 61  MET B N      1 
ATOM   3602  C  CA     . MET B 2 62  ? 7.017   8.473   18.151  1.00 15.34  ? 61  MET B CA     1 
ATOM   3603  C  C      . MET B 2 62  ? 8.513   8.414   17.888  1.00 16.14  ? 61  MET B C      1 
ATOM   3604  O  O      . MET B 2 62  ? 9.296   9.272   18.320  1.00 17.29  ? 61  MET B O      1 
ATOM   3605  C  CB     . MET B 2 62  ? 6.230   8.643   16.820  1.00 18.03  ? 61  MET B CB     1 
ATOM   3606  C  CG     . MET B 2 62  ? 6.021   10.043  16.337  1.00 22.24  ? 61  MET B CG     1 
ATOM   3607  S  SD     . MET B 2 62  ? 7.214   11.286  16.443  1.00 18.82  ? 61  MET B SD     1 
ATOM   3608  C  CE     . MET B 2 62  ? 8.056   10.123  15.098  1.00 21.44  ? 61  MET B CE     1 
ATOM   3609  H  H      . MET B 2 62  ? 7.228   10.028  19.375  1.00 19.27  ? 61  MET B H      1 
ATOM   3610  H  HA     . MET B 2 62  ? 6.811   7.619   18.560  1.00 18.23  ? 61  MET B HA     1 
ATOM   3611  H  HB2    . MET B 2 62  ? 6.713   8.171   16.123  1.00 21.67  ? 61  MET B HB2    1 
ATOM   3612  H  HB3    . MET B 2 62  ? 5.351   8.249   16.938  1.00 21.67  ? 61  MET B HB3    1 
ATOM   3613  H  HG2    . MET B 2 62  ? 5.811   9.977   15.393  1.00 26.72  ? 61  MET B HG2    1 
ATOM   3614  H  HG3    . MET B 2 62  ? 5.256   10.388  16.824  1.00 26.72  ? 61  MET B HG3    1 
ATOM   3615  H  HE1    . MET B 2 62  ? 8.903   10.512  14.830  1.00 25.76  ? 61  MET B HE1    1 
ATOM   3616  H  HE2    . MET B 2 62  ? 8.203   9.246   15.487  1.00 25.76  ? 61  MET B HE2    1 
ATOM   3617  H  HE3    . MET B 2 62  ? 7.467   10.050  14.331  1.00 25.76  ? 61  MET B HE3    1 
ATOM   3618  N  N      . CYS B 2 63  ? 8.904   7.311   17.231  1.00 17.59  ? 62  CYS B N      1 
ATOM   3619  C  CA     . CYS B 2 63  ? 10.250  7.098   16.718  1.00 14.64  ? 62  CYS B CA     1 
ATOM   3620  C  C      . CYS B 2 63  ? 10.165  7.027   15.204  1.00 16.78  ? 62  CYS B C      1 
ATOM   3621  O  O      . CYS B 2 63  ? 9.390   6.223   14.702  1.00 17.72  ? 62  CYS B O      1 
ATOM   3622  C  CB     . CYS B 2 63  ? 10.820  5.774   17.203  1.00 14.99  ? 62  CYS B CB     1 
ATOM   3623  S  SG     . CYS B 2 63  ? 10.962  5.673   19.027  1.00 19.67  ? 62  CYS B SG     1 
ATOM   3624  H  H      . CYS B 2 63  ? 8.379   6.650   17.067  1.00 21.14  ? 62  CYS B H      1 
ATOM   3625  H  HA     . CYS B 2 63  ? 10.824  7.825   17.007  1.00 17.44  ? 62  CYS B HA     1 
ATOM   3626  H  HB2    . CYS B 2 63  ? 10.239  5.056   16.909  1.00 17.86  ? 62  CYS B HB2    1 
ATOM   3627  H  HB3    . CYS B 2 63  ? 11.707  5.659   16.828  1.00 17.86  ? 62  CYS B HB3    1 
ATOM   3628  H  HG     . CYS B 2 63  ? 11.391  4.593   19.326  1.00 23.64  ? 62  CYS B HG     1 
ATOM   3629  N  N      . GLN B 2 64  ? 10.987  7.800   14.508  1.00 14.50  ? 63  GLN B N      1 
ATOM   3630  C  CA     . GLN B 2 64  ? 10.931  7.905   13.045  1.00 16.36  ? 63  GLN B CA     1 
ATOM   3631  C  C      . GLN B 2 64  ? 12.279  7.572   12.426  1.00 17.55  ? 63  GLN B C      1 
ATOM   3632  O  O      . GLN B 2 64  ? 13.338  7.956   12.965  1.00 17.06  ? 63  GLN B O      1 
ATOM   3633  C  CB     . GLN B 2 64  ? 10.486  9.313   12.661  1.00 16.63  ? 63  GLN B CB     1 
ATOM   3634  C  CG     . GLN B 2 64  ? 10.524  9.596   11.160  1.00 16.33  ? 63  GLN B CG     1 
ATOM   3635  C  CD     . GLN B 2 64  ? 9.921   10.910  10.821  1.00 16.22  ? 63  GLN B CD     1 
ATOM   3636  O  OE1    . GLN B 2 64  ? 9.237   11.516  11.635  1.00 16.60  ? 63  GLN B OE1    1 
ATOM   3637  N  NE2    . GLN B 2 64  ? 10.172  11.375  9.571   1.00 16.18  ? 63  GLN B NE2    1 
ATOM   3638  H  H      . GLN B 2 64  ? 11.600  8.287   14.863  1.00 17.44  ? 63  GLN B H      1 
ATOM   3639  H  HA     . GLN B 2 64  ? 10.304  7.260   12.682  1.00 19.67  ? 63  GLN B HA     1 
ATOM   3640  H  HB2    . GLN B 2 64  ? 9.572   9.441   12.961  1.00 19.98  ? 63  GLN B HB2    1 
ATOM   3641  H  HB3    . GLN B 2 64  ? 11.071  9.952   13.096  1.00 19.98  ? 63  GLN B HB3    1 
ATOM   3642  H  HG2    . GLN B 2 64  ? 11.447  9.601   10.861  1.00 19.64  ? 63  GLN B HG2    1 
ATOM   3643  H  HG3    . GLN B 2 64  ? 10.028  8.906   10.693  1.00 19.64  ? 63  GLN B HG3    1 
ATOM   3644  H  HE21   . GLN B 2 64  ? 10.655  10.913  9.029   1.00 19.45  ? 63  GLN B HE21   1 
ATOM   3645  H  HE22   . GLN B 2 64  ? 9.847   12.131  9.320   1.00 19.45  ? 63  GLN B HE22   1 
ATOM   3646  N  N      . GLY B 2 65  ? 12.227  6.838   11.315  1.00 18.85  ? 64  GLY B N      1 
ATOM   3647  C  CA     . GLY B 2 65  ? 13.433  6.414   10.620  1.00 13.79  ? 64  GLY B CA     1 
ATOM   3648  C  C      . GLY B 2 65  ? 13.167  6.209   9.150   1.00 16.67  ? 64  GLY B C      1 
ATOM   3649  O  O      . GLY B 2 65  ? 12.176  6.700   8.608   1.00 16.59  ? 64  GLY B O      1 
ATOM   3650  H  H      . GLY B 2 65  ? 11.499  6.573   10.943  1.00 22.65  ? 64  GLY B H      1 
ATOM   3651  H  HA2    . GLY B 2 65  ? 14.123  7.088   10.721  1.00 16.59  ? 64  GLY B HA2    1 
ATOM   3652  H  HA3    . GLY B 2 65  ? 13.751  5.579   10.998  1.00 16.59  ? 64  GLY B HA3    1 
ATOM   3653  N  N      . GLY B 2 66  ? 14.064  5.468   8.513   1.00 16.71  ? 65  GLY B N      1 
ATOM   3654  C  CA     . GLY B 2 66  ? 13.863  5.030   7.162   1.00 14.18  ? 65  GLY B CA     1 
ATOM   3655  C  C      . GLY B 2 66  ? 14.561  5.798   6.072   1.00 18.66  ? 65  GLY B C      1 
ATOM   3656  O  O      . GLY B 2 66  ? 14.372  5.432   4.886   1.00 20.87  ? 65  GLY B O      1 
ATOM   3657  H  H      . GLY B 2 66  ? 14.807  5.207   8.857   1.00 20.09  ? 65  GLY B H      1 
ATOM   3658  H  HA2    . GLY B 2 66  ? 14.162  4.109   7.098   1.00 17.06  ? 65  GLY B HA2    1 
ATOM   3659  H  HA3    . GLY B 2 66  ? 12.912  5.067   6.973   1.00 17.06  ? 65  GLY B HA3    1 
ATOM   3660  N  N      . ASP B 2 67  ? 15.379  6.810   6.393   1.00 18.38  ? 66  ASP B N      1 
ATOM   3661  C  CA     . ASP B 2 67  ? 16.146  7.510   5.358   1.00 18.82  ? 66  ASP B CA     1 
ATOM   3662  C  C      . ASP B 2 67  ? 17.470  6.780   5.130   1.00 20.06  ? 66  ASP B C      1 
ATOM   3663  O  O      . ASP B 2 67  ? 18.483  7.045   5.783   1.00 20.41  ? 66  ASP B O      1 
ATOM   3664  C  CB     . ASP B 2 67  ? 16.398  8.966   5.727   1.00 19.37  ? 66  ASP B CB     1 
ATOM   3665  C  CG     . ASP B 2 67  ? 17.270  9.701   4.683   1.00 21.94  ? 66  ASP B CG     1 
ATOM   3666  O  OD1    . ASP B 2 67  ? 17.630  9.089   3.644   1.00 23.33  ? 66  ASP B OD1    1 
ATOM   3667  O  OD2    . ASP B 2 67  ? 17.556  10.896  4.914   1.00 20.72  ? 66  ASP B OD2    1 
ATOM   3668  H  H      . ASP B 2 67  ? 15.504  7.103   7.192   1.00 22.09  ? 66  ASP B H      1 
ATOM   3669  H  HA     . ASP B 2 67  ? 15.622  7.478   4.542   1.00 22.62  ? 66  ASP B HA     1 
ATOM   3670  H  HB2    . ASP B 2 67  ? 15.547  9.429   5.787   1.00 23.27  ? 66  ASP B HB2    1 
ATOM   3671  H  HB3    . ASP B 2 67  ? 16.856  9.002   6.581   1.00 23.27  ? 66  ASP B HB3    1 
ATOM   3672  N  N      . PHE B 2 68  ? 17.472  5.860   4.178   1.00 19.01  ? 67  PHE B N      1 
ATOM   3673  C  CA     . PHE B 2 68  ? 18.659  5.092   3.845   1.00 21.03  ? 67  PHE B CA     1 
ATOM   3674  C  C      . PHE B 2 68  ? 19.389  5.646   2.629   1.00 23.29  ? 67  PHE B C      1 
ATOM   3675  O  O      . PHE B 2 68  ? 20.413  5.075   2.224   1.00 25.16  ? 67  PHE B O      1 
ATOM   3676  C  CB     . PHE B 2 68  ? 18.301  3.612   3.632   1.00 23.09  ? 67  PHE B CB     1 
ATOM   3677  C  CG     . PHE B 2 68  ? 17.320  3.391   2.528   1.00 22.35  ? 67  PHE B CG     1 
ATOM   3678  C  CD1    . PHE B 2 68  ? 17.728  3.448   1.214   1.00 24.05  ? 67  PHE B CD1    1 
ATOM   3679  C  CD2    . PHE B 2 68  ? 15.986  3.121   2.790   1.00 22.87  ? 67  PHE B CD2    1 
ATOM   3680  C  CE1    . PHE B 2 68  ? 16.802  3.237   0.175   1.00 25.63  ? 67  PHE B CE1    1 
ATOM   3681  C  CE2    . PHE B 2 68  ? 15.077  2.961   1.772   1.00 21.64  ? 67  PHE B CE2    1 
ATOM   3682  C  CZ     . PHE B 2 68  ? 15.493  2.989   0.465   1.00 21.80  ? 67  PHE B CZ     1 
ATOM   3683  H  H      . PHE B 2 68  ? 16.785  5.659   3.701   1.00 22.85  ? 67  PHE B H      1 
ATOM   3684  H  HA     . PHE B 2 68  ? 19.274  5.125   4.594   1.00 25.26  ? 67  PHE B HA     1 
ATOM   3685  H  HB2    . PHE B 2 68  ? 19.110  3.123   3.414   1.00 27.75  ? 67  PHE B HB2    1 
ATOM   3686  H  HB3    . PHE B 2 68  ? 17.913  3.263   4.450   1.00 27.75  ? 67  PHE B HB3    1 
ATOM   3687  H  HD1    . PHE B 2 68  ? 18.618  3.628   1.012   1.00 28.89  ? 67  PHE B HD1    1 
ATOM   3688  H  HD2    . PHE B 2 68  ? 15.701  3.047   3.672   1.00 27.48  ? 67  PHE B HD2    1 
ATOM   3689  H  HE1    . PHE B 2 68  ? 17.083  3.266   -0.711  1.00 30.79  ? 67  PHE B HE1    1 
ATOM   3690  H  HE2    . PHE B 2 68  ? 14.177  2.833   1.969   1.00 26.00  ? 67  PHE B HE2    1 
ATOM   3691  H  HZ     . PHE B 2 68  ? 14.883  2.839   -0.221  1.00 26.20  ? 67  PHE B HZ     1 
ATOM   3692  N  N      . THR B 2 69  ? 18.929  6.760   2.055   1.00 22.80  ? 68  THR B N      1 
ATOM   3693  C  CA     . THR B 2 69  ? 19.645  7.314   0.903   1.00 25.78  ? 68  THR B CA     1 
ATOM   3694  C  C      . THR B 2 69  ? 20.517  8.510   1.266   1.00 26.48  ? 68  THR B C      1 
ATOM   3695  O  O      . THR B 2 69  ? 21.582  8.692   0.662   1.00 27.91  ? 68  THR B O      1 
ATOM   3696  C  CB     . THR B 2 69  ? 18.683  7.741   -0.211  1.00 25.71  ? 68  THR B CB     1 
ATOM   3697  O  OG1    . THR B 2 69  ? 17.875  8.837   0.243   1.00 25.25  ? 68  THR B OG1    1 
ATOM   3698  C  CG2    . THR B 2 69  ? 17.805  6.541   -0.658  1.00 22.79  ? 68  THR B CG2    1 
ATOM   3699  H  H      . THR B 2 69  ? 18.231  7.197   2.305   1.00 27.39  ? 68  THR B H      1 
ATOM   3700  H  HA     . THR B 2 69  ? 20.207  6.608   0.548   1.00 30.97  ? 68  THR B HA     1 
ATOM   3701  H  HB     . THR B 2 69  ? 19.182  8.037   -0.988  1.00 30.89  ? 68  THR B HB     1 
ATOM   3702  H  HG1    . THR B 2 69  ? 17.409  9.131   -0.391  1.00 30.34  ? 68  THR B HG1    1 
ATOM   3703  H  HG21   . THR B 2 69  ? 17.205  6.816   -1.369  1.00 27.38  ? 68  THR B HG21   1 
ATOM   3704  H  HG22   . THR B 2 69  ? 18.369  5.821   -0.982  1.00 27.38  ? 68  THR B HG22   1 
ATOM   3705  H  HG23   . THR B 2 69  ? 17.280  6.218   0.090   1.00 27.38  ? 68  THR B HG23   1 
ATOM   3706  N  N      . ARG B 2 70  ? 20.072  9.353   2.204   1.00 23.24  ? 69  ARG B N      1 
ATOM   3707  C  CA     . ARG B 2 70  ? 20.826  10.510  2.639   1.00 23.61  ? 69  ARG B CA     1 
ATOM   3708  C  C      . ARG B 2 70  ? 21.247  10.428  4.091   1.00 26.29  ? 69  ARG B C      1 
ATOM   3709  O  O      . ARG B 2 70  ? 22.103  11.214  4.517   1.00 25.91  ? 69  ARG B O      1 
ATOM   3710  C  CB     . ARG B 2 70  ? 20.009  11.788  2.438   1.00 23.09  ? 69  ARG B CB     1 
ATOM   3711  C  CG     . ARG B 2 70  ? 19.656  12.001  0.990   1.00 27.92  ? 69  ARG B CG     1 
ATOM   3712  C  CD     . ARG B 2 70  ? 18.841  13.236  0.832   1.00 30.28  ? 69  ARG B CD     1 
ATOM   3713  N  NE     . ARG B 2 70  ? 18.430  13.406  -0.559  1.00 34.50  ? 69  ARG B NE     1 
ATOM   3714  C  CZ     . ARG B 2 70  ? 17.572  14.331  -0.956  1.00 32.11  ? 69  ARG B CZ     1 
ATOM   3715  N  NH1    . ARG B 2 70  ? 17.027  15.179  -0.094  1.00 26.85  ? 69  ARG B NH1    1 
ATOM   3716  N  NH2    . ARG B 2 70  ? 17.183  14.351  -2.232  1.00 34.28  ? 69  ARG B NH2    1 
ATOM   3717  H  H      . ARG B 2 70  ? 19.317  9.266   2.606   1.00 27.92  ? 69  ARG B H      1 
ATOM   3718  H  HA     . ARG B 2 70  ? 21.625  10.592  2.095   1.00 28.36  ? 69  ARG B HA     1 
ATOM   3719  H  HB2    . ARG B 2 70  ? 19.186  11.724  2.946   1.00 27.75  ? 69  ARG B HB2    1 
ATOM   3720  H  HB3    . ARG B 2 70  ? 20.528  12.549  2.740   1.00 27.75  ? 69  ARG B HB3    1 
ATOM   3721  H  HG2    . ARG B 2 70  ? 20.467  12.096  0.467   1.00 33.54  ? 69  ARG B HG2    1 
ATOM   3722  H  HG3    . ARG B 2 70  ? 19.140  11.246  0.666   1.00 33.54  ? 69  ARG B HG3    1 
ATOM   3723  H  HD2    . ARG B 2 70  ? 18.045  13.173  1.383   1.00 36.37  ? 69  ARG B HD2    1 
ATOM   3724  H  HD3    . ARG B 2 70  ? 19.367  14.008  1.095   1.00 36.37  ? 69  ARG B HD3    1 
ATOM   3725  H  HE     . ARG B 2 70  ? 18.764  12.878  -1.150  1.00 41.44  ? 69  ARG B HE     1 
ATOM   3726  H  HH11   . ARG B 2 70  ? 17.230  15.134  0.741   1.00 32.26  ? 69  ARG B HH11   1 
ATOM   3727  H  HH12   . ARG B 2 70  ? 16.471  15.774  -0.369  1.00 32.26  ? 69  ARG B HH12   1 
ATOM   3728  H  HH21   . ARG B 2 70  ? 17.490  13.767  -2.784  1.00 41.17  ? 69  ARG B HH21   1 
ATOM   3729  H  HH22   . ARG B 2 70  ? 16.626  14.947  -2.502  1.00 41.17  ? 69  ARG B HH22   1 
ATOM   3730  N  N      . HIS B 2 71  ? 20.629  9.549   4.867   1.00 25.04  ? 70  HIS B N      1 
ATOM   3731  C  CA     . HIS B 2 71  ? 20.926  9.395   6.304   1.00 23.86  ? 70  HIS B CA     1 
ATOM   3732  C  C      . HIS B 2 71  ? 20.881  10.724  7.035   1.00 27.41  ? 70  HIS B C      1 
ATOM   3733  O  O      . HIS B 2 71  ? 21.626  10.963  7.998   1.00 30.02  ? 70  HIS B O      1 
ATOM   3734  C  CB     . HIS B 2 71  ? 22.282  8.725   6.523   1.00 27.10  ? 70  HIS B CB     1 
ATOM   3735  C  CG     . HIS B 2 71  ? 22.446  7.442   5.781   1.00 27.64  ? 70  HIS B CG     1 
ATOM   3736  N  ND1    . HIS B 2 71  ? 21.975  6.249   6.272   1.00 26.61  ? 70  HIS B ND1    1 
ATOM   3737  C  CD2    . HIS B 2 71  ? 23.069  7.153   4.613   1.00 24.30  ? 70  HIS B CD2    1 
ATOM   3738  C  CE1    . HIS B 2 71  ? 22.280  5.276   5.430   1.00 28.88  ? 70  HIS B CE1    1 
ATOM   3739  N  NE2    . HIS B 2 71  ? 22.910  5.806   4.394   1.00 25.97  ? 70  HIS B NE2    1 
ATOM   3740  H  H      . HIS B 2 71  ? 20.018  9.012   4.587   1.00 30.08  ? 70  HIS B H      1 
ATOM   3741  H  HA     . HIS B 2 71  ? 20.236  8.827   6.679   1.00 28.67  ? 70  HIS B HA     1 
ATOM   3742  H  HB2    . HIS B 2 71  ? 22.980  9.330   6.227   1.00 32.55  ? 70  HIS B HB2    1 
ATOM   3743  H  HB3    . HIS B 2 71  ? 22.386  8.536   7.469   1.00 32.55  ? 70  HIS B HB3    1 
ATOM   3744  H  HD1    . HIS B 2 71  ? 21.548  6.150   7.012   1.00 31.97  ? 70  HIS B HD1    1 
ATOM   3745  H  HD2    . HIS B 2 71  ? 23.519  7.754   4.063   1.00 29.20  ? 70  HIS B HD2    1 
ATOM   3746  H  HE1    . HIS B 2 71  ? 22.084  4.374   5.546   1.00 34.70  ? 70  HIS B HE1    1 
ATOM   3747  N  N      . ASN B 2 72  ? 19.969  11.595  6.618   1.00 21.65  ? 71  ASN B N      1 
ATOM   3748  C  CA     . ASN B 2 72  ? 19.838  12.857  7.322   1.00 27.83  ? 71  ASN B CA     1 
ATOM   3749  C  C      . ASN B 2 72  ? 18.402  13.298  7.558   1.00 22.27  ? 71  ASN B C      1 
ATOM   3750  O  O      . ASN B 2 72  ? 18.192  14.449  7.954   1.00 26.74  ? 71  ASN B O      1 
ATOM   3751  C  CB     . ASN B 2 72  ? 20.644  13.949  6.576   1.00 26.93  ? 71  ASN B CB     1 
ATOM   3752  C  CG     . ASN B 2 72  ? 20.026  14.392  5.252   1.00 31.44  ? 71  ASN B CG     1 
ATOM   3753  O  OD1    . ASN B 2 72  ? 18.881  14.069  4.914   1.00 22.44  ? 71  ASN B OD1    1 
ATOM   3754  N  ND2    . ASN B 2 72  ? 20.793  15.183  4.506   1.00 29.11  ? 71  ASN B ND2    1 
ATOM   3755  H  H      . ASN B 2 72  ? 19.434  11.480  5.954   1.00 26.01  ? 71  ASN B H      1 
ATOM   3756  H  HA     . ASN B 2 72  ? 20.213  12.758  8.211   1.00 33.42  ? 71  ASN B HA     1 
ATOM   3757  H  HB2    . ASN B 2 72  ? 20.709  14.731  7.146   1.00 32.34  ? 71  ASN B HB2    1 
ATOM   3758  H  HB3    . ASN B 2 72  ? 21.530  13.604  6.384   1.00 32.34  ? 71  ASN B HB3    1 
ATOM   3759  H  HD21   . ASN B 2 72  ? 20.506  15.470  3.747   1.00 34.97  ? 71  ASN B HD21   1 
ATOM   3760  H  HD22   . ASN B 2 72  ? 21.576  15.407  4.781   1.00 34.97  ? 71  ASN B HD22   1 
ATOM   3761  N  N      . GLY B 2 73  ? 17.395  12.419  7.364   1.00 19.89  ? 72  GLY B N      1 
ATOM   3762  C  CA     . GLY B 2 73  ? 16.013  12.798  7.569   1.00 18.75  ? 72  GLY B CA     1 
ATOM   3763  C  C      . GLY B 2 73  ? 15.292  13.402  6.370   1.00 20.57  ? 72  GLY B C      1 
ATOM   3764  O  O      . GLY B 2 73  ? 14.070  13.595  6.435   1.00 20.19  ? 72  GLY B O      1 
ATOM   3765  H  H      . GLY B 2 73  ? 17.505  11.603  7.115   1.00 23.90  ? 72  GLY B H      1 
ATOM   3766  H  HA2    . GLY B 2 73  ? 15.517  12.008  7.837   1.00 22.54  ? 72  GLY B HA2    1 
ATOM   3767  H  HA3    . GLY B 2 73  ? 15.979  13.451  8.285   1.00 22.54  ? 72  GLY B HA3    1 
ATOM   3768  N  N      . THR B 2 74  ? 15.996  13.725  5.272   1.00 20.72  ? 73  THR B N      1 
ATOM   3769  C  CA     . THR B 2 74  ? 15.336  14.292  4.109   1.00 21.61  ? 73  THR B CA     1 
ATOM   3770  C  C      . THR B 2 74  ? 15.122  13.279  2.989   1.00 22.81  ? 73  THR B C      1 
ATOM   3771  O  O      . THR B 2 74  ? 14.391  13.579  2.032   1.00 23.68  ? 73  THR B O      1 
ATOM   3772  C  CB     . THR B 2 74  ? 16.142  15.468  3.542   1.00 24.40  ? 73  THR B CB     1 
ATOM   3773  O  OG1    . THR B 2 74  ? 17.352  14.957  2.976   1.00 25.01  ? 73  THR B OG1    1 
ATOM   3774  C  CG2    . THR B 2 74  ? 16.457  16.520  4.642   1.00 24.89  ? 73  THR B CG2    1 
ATOM   3775  H  H      . THR B 2 74  ? 16.846  13.622  5.188   1.00 24.89  ? 73  THR B H      1 
ATOM   3776  H  HA     . THR B 2 74  ? 14.472  14.629  4.396   1.00 25.97  ? 73  THR B HA     1 
ATOM   3777  H  HB     . THR B 2 74  ? 15.628  15.925  2.857   1.00 29.32  ? 73  THR B HB     1 
ATOM   3778  H  HG1    . THR B 2 74  ? 17.788  14.539  3.560   1.00 30.05  ? 73  THR B HG1    1 
ATOM   3779  H  HG21   . THR B 2 74  ? 16.846  17.313  4.242   1.00 29.90  ? 73  THR B HG21   1 
ATOM   3780  H  HG22   . THR B 2 74  ? 15.643  16.768  5.107   1.00 29.90  ? 73  THR B HG22   1 
ATOM   3781  H  HG23   . THR B 2 74  ? 17.085  16.151  5.283   1.00 29.90  ? 73  THR B HG23   1 
ATOM   3782  N  N      . GLY B 2 75  ? 15.753  12.106  3.072   1.00 19.67  ? 74  GLY B N      1 
ATOM   3783  C  CA     . GLY B 2 75  ? 15.744  11.176  1.960   1.00 22.09  ? 74  GLY B CA     1 
ATOM   3784  C  C      . GLY B 2 75  ? 14.864  9.956   2.102   1.00 22.94  ? 74  GLY B C      1 
ATOM   3785  O  O      . GLY B 2 75  ? 13.826  9.967   2.790   1.00 23.11  ? 74  GLY B O      1 
ATOM   3786  H  H      . GLY B 2 75  ? 16.190  11.833  3.761   1.00 23.64  ? 74  GLY B H      1 
ATOM   3787  H  HA2    . GLY B 2 75  ? 15.449  11.652  1.168   1.00 26.55  ? 74  GLY B HA2    1 
ATOM   3788  H  HA3    . GLY B 2 75  ? 16.651  10.861  1.820   1.00 26.55  ? 74  GLY B HA3    1 
ATOM   3789  N  N      . GLY B 2 76  ? 15.283  8.889   1.435   1.00 21.59  ? 75  GLY B N      1 
ATOM   3790  C  CA     . GLY B 2 76  ? 14.521  7.671   1.336   1.00 21.44  ? 75  GLY B CA     1 
ATOM   3791  C  C      . GLY B 2 76  ? 13.879  7.557   -0.031  1.00 19.80  ? 75  GLY B C      1 
ATOM   3792  O  O      . GLY B 2 76  ? 13.705  8.535   -0.750  1.00 20.73  ? 75  GLY B O      1 
ATOM   3793  H  H      . GLY B 2 76  ? 16.034  8.853   1.019   1.00 25.94  ? 75  GLY B H      1 
ATOM   3794  H  HA2    . GLY B 2 76  ? 15.104  6.908   1.474   1.00 25.76  ? 75  GLY B HA2    1 
ATOM   3795  H  HA3    . GLY B 2 76  ? 13.825  7.663   2.012   1.00 25.76  ? 75  GLY B HA3    1 
ATOM   3796  N  N      . LYS B 2 77  ? 13.553  6.330   -0.409  1.00 20.54  ? 76  LYS B N      1 
ATOM   3797  C  CA     . LYS B 2 77  ? 12.834  6.126   -1.661  1.00 21.75  ? 76  LYS B CA     1 
ATOM   3798  C  C      . LYS B 2 77  ? 12.088  4.818   -1.568  1.00 17.46  ? 76  LYS B C      1 
ATOM   3799  O  O      . LYS B 2 77  ? 12.492  3.931   -0.803  1.00 19.75  ? 76  LYS B O      1 
ATOM   3800  C  CB     . LYS B 2 77  ? 13.799  6.083   -2.838  1.00 22.60  ? 76  LYS B CB     1 
ATOM   3801  C  CG     . LYS B 2 77  ? 14.706  4.844   -2.789  1.00 23.75  ? 76  LYS B CG     1 
ATOM   3802  C  CD     . LYS B 2 77  ? 15.809  4.989   -3.860  1.00 28.38  ? 76  LYS B CD     1 
ATOM   3803  C  CE     . LYS B 2 77  ? 16.770  3.835   -3.893  1.00 30.36  ? 76  LYS B CE     1 
ATOM   3804  N  NZ     . LYS B 2 77  ? 17.738  3.998   -5.053  1.00 34.10  ? 76  LYS B NZ     1 
ATOM   3805  H  H      . LYS B 2 77  ? 13.732  5.613   0.031   1.00 24.68  ? 76  LYS B H      1 
ATOM   3806  H  HA     . LYS B 2 77  ? 12.197  6.844   -1.800  1.00 26.13  ? 76  LYS B HA     1 
ATOM   3807  H  HB2    . LYS B 2 77  ? 13.293  6.058   -3.665  1.00 27.15  ? 76  LYS B HB2    1 
ATOM   3808  H  HB3    . LYS B 2 77  ? 14.362  6.873   -2.818  1.00 27.15  ? 76  LYS B HB3    1 
ATOM   3809  H  HG2    . LYS B 2 77  ? 15.122  4.771   -1.916  1.00 28.53  ? 76  LYS B HG2    1 
ATOM   3810  H  HG3    . LYS B 2 77  ? 14.187  4.046   -2.977  1.00 28.53  ? 76  LYS B HG3    1 
ATOM   3811  H  HD2    . LYS B 2 77  ? 15.392  5.052   -4.734  1.00 34.09  ? 76  LYS B HD2    1 
ATOM   3812  H  HD3    . LYS B 2 77  ? 16.320  5.793   -3.678  1.00 34.09  ? 76  LYS B HD3    1 
ATOM   3813  H  HE2    . LYS B 2 77  ? 17.276  3.807   -3.066  1.00 36.47  ? 76  LYS B HE2    1 
ATOM   3814  H  HE3    . LYS B 2 77  ? 16.280  3.006   -4.010  1.00 36.47  ? 76  LYS B HE3    1 
ATOM   3815  H  HZ1    . LYS B 2 77  ? 18.312  3.318   -5.069  1.00 40.95  ? 76  LYS B HZ1    1 
ATOM   3816  H  HZ2    . LYS B 2 77  ? 17.291  4.017   -5.823  1.00 40.95  ? 76  LYS B HZ2    1 
ATOM   3817  H  HZ3    . LYS B 2 77  ? 18.193  4.758   -4.965  1.00 40.95  ? 76  LYS B HZ3    1 
ATOM   3818  N  N      . SER B 2 78  ? 10.973  4.727   -2.304  1.00 18.91  ? 77  SER B N      1 
ATOM   3819  C  CA     . SER B 2 78  ? 10.174  3.519   -2.296  1.00 19.66  ? 77  SER B CA     1 
ATOM   3820  C  C      . SER B 2 78  ? 10.695  2.572   -3.374  1.00 21.05  ? 77  SER B C      1 
ATOM   3821  O  O      . SER B 2 78  ? 11.568  2.921   -4.177  1.00 23.73  ? 77  SER B O      1 
ATOM   3822  C  CB     . SER B 2 78  ? 8.694   3.806   -2.549  1.00 18.74  ? 77  SER B CB     1 
ATOM   3823  O  OG     . SER B 2 78  ? 8.372   3.840   -3.946  1.00 20.79  ? 77  SER B OG     1 
ATOM   3824  H  H      . SER B 2 78  ? 10.669  5.352   -2.810  1.00 22.72  ? 77  SER B H      1 
ATOM   3825  H  HA     . SER B 2 78  ? 10.241  3.110   -1.419  1.00 23.63  ? 77  SER B HA     1 
ATOM   3826  H  HB2    . SER B 2 78  ? 8.168   3.109   -2.127  1.00 22.53  ? 77  SER B HB2    1 
ATOM   3827  H  HB3    . SER B 2 78  ? 8.476   4.668   -2.161  1.00 22.53  ? 77  SER B HB3    1 
ATOM   3828  H  HG     . SER B 2 78  ? 8.823   4.435   -4.331  1.00 24.98  ? 77  SER B HG     1 
ATOM   3829  N  N      . ILE B 2 79  ? 10.120  1.366   -3.405  1.00 21.35  ? 78  ILE B N      1 
ATOM   3830  C  CA     . ILE B 2 79  ? 10.455  0.413   -4.460  1.00 21.77  ? 78  ILE B CA     1 
ATOM   3831  C  C      . ILE B 2 79  ? 9.736   0.739   -5.759  1.00 23.39  ? 78  ILE B C      1 
ATOM   3832  O  O      . ILE B 2 79  ? 9.907   0.008   -6.761  1.00 24.89  ? 78  ILE B O      1 
ATOM   3833  C  CB     . ILE B 2 79  ? 10.121  -1.026  -4.018  1.00 20.40  ? 78  ILE B CB     1 
ATOM   3834  C  CG1    . ILE B 2 79  ? 8.591   -1.168  -3.894  1.00 21.14  ? 78  ILE B CG1    1 
ATOM   3835  C  CG2    . ILE B 2 79  ? 10.855  -1.408  -2.702  1.00 25.48  ? 78  ILE B CG2    1 
ATOM   3836  C  CD1    . ILE B 2 79  ? 8.117   -2.600  -3.654  1.00 22.04  ? 78  ILE B CD1    1 
ATOM   3837  H  H      . ILE B 2 79  ? 9.543   1.082   -2.834  1.00 25.65  ? 78  ILE B H      1 
ATOM   3838  H  HA     . ILE B 2 79  ? 11.409  0.455   -4.631  1.00 26.16  ? 78  ILE B HA     1 
ATOM   3839  H  HB     . ILE B 2 79  ? 10.439  -1.648  -4.691  1.00 24.52  ? 78  ILE B HB     1 
ATOM   3840  H  HG12   . ILE B 2 79  ? 8.289   -0.628  -3.147  1.00 25.40  ? 78  ILE B HG12   1 
ATOM   3841  H  HG13   . ILE B 2 79  ? 8.183   -0.856  -4.716  1.00 25.40  ? 78  ILE B HG13   1 
ATOM   3842  H  HG21   . ILE B 2 79  ? 10.726  -2.354  -2.532  1.00 30.61  ? 78  ILE B HG21   1 
ATOM   3843  H  HG22   . ILE B 2 79  ? 11.800  -1.215  -2.801  1.00 30.61  ? 78  ILE B HG22   1 
ATOM   3844  H  HG23   . ILE B 2 79  ? 10.485  -0.887  -1.972  1.00 30.61  ? 78  ILE B HG23   1 
ATOM   3845  H  HD11   . ILE B 2 79  ? 7.148   -2.613  -3.639  1.00 26.48  ? 78  ILE B HD11   1 
ATOM   3846  H  HD12   . ILE B 2 79  ? 8.445   -3.165  -4.371  1.00 26.48  ? 78  ILE B HD12   1 
ATOM   3847  H  HD13   . ILE B 2 79  ? 8.466   -2.909  -2.803  1.00 26.48  ? 78  ILE B HD13   1 
ATOM   3848  N  N      . TYR B 2 80  ? 8.878   1.767   -5.749  1.00 24.63  ? 79  TYR B N      1 
ATOM   3849  C  CA     . TYR B 2 80  ? 8.029   2.154   -6.868  1.00 22.79  ? 79  TYR B CA     1 
ATOM   3850  C  C      . TYR B 2 80  ? 8.521   3.401   -7.581  1.00 24.29  ? 79  TYR B C      1 
ATOM   3851  O  O      . TYR B 2 80  ? 7.852   3.880   -8.520  1.00 28.22  ? 79  TYR B O      1 
ATOM   3852  C  CB     . TYR B 2 80  ? 6.597   2.418   -6.373  1.00 21.97  ? 79  TYR B CB     1 
ATOM   3853  C  CG     . TYR B 2 80  ? 5.993   1.279   -5.578  1.00 25.77  ? 79  TYR B CG     1 
ATOM   3854  C  CD1    . TYR B 2 80  ? 5.793   0.043   -6.163  1.00 26.41  ? 79  TYR B CD1    1 
ATOM   3855  C  CD2    . TYR B 2 80  ? 5.651   1.434   -4.233  1.00 24.32  ? 79  TYR B CD2    1 
ATOM   3856  C  CE1    . TYR B 2 80  ? 5.270   -1.008  -5.459  1.00 25.94  ? 79  TYR B CE1    1 
ATOM   3857  C  CE2    . TYR B 2 80  ? 5.113   0.394   -3.517  1.00 21.63  ? 79  TYR B CE2    1 
ATOM   3858  C  CZ     . TYR B 2 80  ? 4.927   -0.841  -4.132  1.00 24.10  ? 79  TYR B CZ     1 
ATOM   3859  O  OH     . TYR B 2 80  ? 4.395   -1.905  -3.443  1.00 25.32  ? 79  TYR B OH     1 
ATOM   3860  H  H      . TYR B 2 80  ? 8.768   2.278   -5.066  1.00 29.59  ? 79  TYR B H      1 
ATOM   3861  H  HA     . TYR B 2 80  ? 8.014   1.421   -7.503  1.00 27.39  ? 79  TYR B HA     1 
ATOM   3862  H  HB2    . TYR B 2 80  ? 6.606   3.202   -5.802  1.00 26.39  ? 79  TYR B HB2    1 
ATOM   3863  H  HB3    . TYR B 2 80  ? 6.027   2.574   -7.142  1.00 26.39  ? 79  TYR B HB3    1 
ATOM   3864  H  HD1    . TYR B 2 80  ? 6.019   -0.078  -7.057  1.00 31.72  ? 79  TYR B HD1    1 
ATOM   3865  H  HD2    . TYR B 2 80  ? 5.791   2.254   -3.817  1.00 29.21  ? 79  TYR B HD2    1 
ATOM   3866  H  HE1    . TYR B 2 80  ? 5.147   -1.832  -5.873  1.00 31.17  ? 79  TYR B HE1    1 
ATOM   3867  H  HE2    . TYR B 2 80  ? 4.875   0.514   -2.626  1.00 25.99  ? 79  TYR B HE2    1 
ATOM   3868  H  HH     . TYR B 2 80  ? 4.268   -1.693  -2.640  1.00 30.42  ? 79  TYR B HH     1 
ATOM   3869  N  N      . GLY B 2 81  ? 9.656   3.934   -7.182  1.00 28.16  ? 80  GLY B N      1 
ATOM   3870  C  CA     . GLY B 2 81  ? 10.060  5.280   -7.516  1.00 26.58  ? 80  GLY B CA     1 
ATOM   3871  C  C      . GLY B 2 81  ? 10.363  6.063   -6.255  1.00 27.43  ? 80  GLY B C      1 
ATOM   3872  O  O      . GLY B 2 81  ? 10.211  5.569   -5.138  1.00 26.01  ? 80  GLY B O      1 
ATOM   3873  H  H      . GLY B 2 81  ? 10.231  3.518   -6.696  1.00 33.82  ? 80  GLY B H      1 
ATOM   3874  H  HA2    . GLY B 2 81  ? 10.855  5.257   -8.071  1.00 31.93  ? 80  GLY B HA2    1 
ATOM   3875  H  HA3    . GLY B 2 81  ? 9.349   5.727   -8.001  1.00 31.93  ? 80  GLY B HA3    1 
ATOM   3876  N  N      . GLU B 2 82  ? 10.823  7.300   -6.445  1.00 25.75  ? 81  GLU B N      1 
ATOM   3877  C  CA     . GLU B 2 82  ? 11.214  8.077   -5.271  1.00 23.70  ? 81  GLU B CA     1 
ATOM   3878  C  C      . GLU B 2 82  ? 10.074  8.148   -4.270  1.00 24.34  ? 81  GLU B C      1 
ATOM   3879  O  O      . GLU B 2 82  ? 10.292  7.987   -3.075  1.00 26.24  ? 81  GLU B O      1 
ATOM   3880  C  CB     . GLU B 2 82  ? 11.631  9.487   -5.622  1.00 25.63  ? 81  GLU B CB     1 
ATOM   3881  C  CG     . GLU B 2 82  ? 12.909  9.604   -6.394  1.00 39.61  ? 81  GLU B CG     1 
ATOM   3882  C  CD     . GLU B 2 82  ? 14.116  9.623   -5.468  1.00 40.14  ? 81  GLU B CD     1 
ATOM   3883  O  OE1    . GLU B 2 82  ? 14.325  10.665  -4.786  1.00 41.79  ? 81  GLU B OE1    1 
ATOM   3884  O  OE2    . GLU B 2 82  ? 14.849  8.597   -5.430  1.00 36.89  ? 81  GLU B OE2    1 
ATOM   3885  H  H      . GLU B 2 82  ? 10.913  7.692   -7.205  1.00 30.93  ? 81  GLU B H      1 
ATOM   3886  H  HA     . GLU B 2 82  ? 11.985  7.632   -4.884  1.00 28.47  ? 81  GLU B HA     1 
ATOM   3887  H  HB2    . GLU B 2 82  ? 10.930  9.887   -6.160  1.00 30.79  ? 81  GLU B HB2    1 
ATOM   3888  H  HB3    . GLU B 2 82  ? 11.743  9.987   -4.799  1.00 30.79  ? 81  GLU B HB3    1 
ATOM   3889  H  HG2    . GLU B 2 82  ? 12.994  8.846   -6.993  1.00 47.57  ? 81  GLU B HG2    1 
ATOM   3890  H  HG3    . GLU B 2 82  ? 12.902  10.430  -6.904  1.00 47.57  ? 81  GLU B HG3    1 
ATOM   3891  N  N      . LYS B 2 83  ? 8.851   8.361   -4.744  1.00 21.91  ? 82  LYS B N      1 
ATOM   3892  C  CA     . LYS B 2 83  ? 7.681   8.517   -3.884  1.00 19.73  ? 82  LYS B CA     1 
ATOM   3893  C  C      . LYS B 2 83  ? 6.494   7.844   -4.562  1.00 23.66  ? 82  LYS B C      1 
ATOM   3894  O  O      . LYS B 2 83  ? 6.508   7.599   -5.764  1.00 25.71  ? 82  LYS B O      1 
ATOM   3895  C  CB     . LYS B 2 83  ? 7.380   9.995   -3.620  1.00 25.54  ? 82  LYS B CB     1 
ATOM   3896  C  CG     . LYS B 2 83  ? 8.464   10.802  -2.807  1.00 25.57  ? 82  LYS B CG     1 
ATOM   3897  C  CD     . LYS B 2 83  ? 9.065   10.048  -1.593  1.00 30.79  ? 82  LYS B CD     1 
ATOM   3898  C  CE     . LYS B 2 83  ? 10.477  10.571  -1.260  1.00 30.63  ? 82  LYS B CE     1 
ATOM   3899  N  NZ     . LYS B 2 83  ? 11.445  9.470   -1.201  1.00 29.67  ? 82  LYS B NZ     1 
ATOM   3900  H  H      . LYS B 2 83  ? 8.667   8.422   -5.582  1.00 26.32  ? 82  LYS B H      1 
ATOM   3901  H  HA     . LYS B 2 83  ? 7.833   8.085   -3.029  1.00 23.71  ? 82  LYS B HA     1 
ATOM   3902  H  HB2    . LYS B 2 83  ? 7.279   10.438  -4.477  1.00 30.68  ? 82  LYS B HB2    1 
ATOM   3903  H  HB3    . LYS B 2 83  ? 6.551   10.048  -3.119  1.00 30.68  ? 82  LYS B HB3    1 
ATOM   3904  H  HG2    . LYS B 2 83  ? 9.197   11.023  -3.403  1.00 30.72  ? 82  LYS B HG2    1 
ATOM   3905  H  HG3    . LYS B 2 83  ? 8.055   11.615  -2.470  1.00 30.72  ? 82  LYS B HG3    1 
ATOM   3906  H  HD2    . LYS B 2 83  ? 8.498   10.180  -0.817  1.00 36.99  ? 82  LYS B HD2    1 
ATOM   3907  H  HD3    . LYS B 2 83  ? 9.129   9.102   -1.800  1.00 36.99  ? 82  LYS B HD3    1 
ATOM   3908  H  HE2    . LYS B 2 83  ? 10.761  11.193  -1.948  1.00 36.79  ? 82  LYS B HE2    1 
ATOM   3909  H  HE3    . LYS B 2 83  ? 10.462  11.013  -0.397  1.00 36.79  ? 82  LYS B HE3    1 
ATOM   3910  H  HZ1    . LYS B 2 83  ? 11.201  8.883   -0.578  1.00 35.63  ? 82  LYS B HZ1    1 
ATOM   3911  H  HZ2    . LYS B 2 83  ? 11.485  9.056   -1.988  1.00 35.63  ? 82  LYS B HZ2    1 
ATOM   3912  H  HZ3    . LYS B 2 83  ? 12.253  9.785   -1.000  1.00 35.63  ? 82  LYS B HZ3    1 
ATOM   3913  N  N      . PHE B 2 84  ? 5.479   7.506   -3.763  1.00 20.35  ? 83  PHE B N      1 
ATOM   3914  C  CA     . PHE B 2 84  ? 4.241   6.961   -4.275  1.00 21.76  ? 83  PHE B CA     1 
ATOM   3915  C  C      . PHE B 2 84  ? 3.053   7.491   -3.478  1.00 21.08  ? 83  PHE B C      1 
ATOM   3916  O  O      . PHE B 2 84  ? 3.173   8.089   -2.390  1.00 20.10  ? 83  PHE B O      1 
ATOM   3917  C  CB     . PHE B 2 84  ? 4.223   5.422   -4.311  1.00 22.05  ? 83  PHE B CB     1 
ATOM   3918  C  CG     . PHE B 2 84  ? 4.266   4.739   -2.966  1.00 22.22  ? 83  PHE B CG     1 
ATOM   3919  C  CD1    . PHE B 2 84  ? 5.445   4.677   -2.276  1.00 19.77  ? 83  PHE B CD1    1 
ATOM   3920  C  CD2    . PHE B 2 84  ? 3.135   4.114   -2.435  1.00 20.48  ? 83  PHE B CD2    1 
ATOM   3921  C  CE1    . PHE B 2 84  ? 5.515   4.025   -1.042  1.00 22.02  ? 83  PHE B CE1    1 
ATOM   3922  C  CE2    . PHE B 2 84  ? 3.188   3.429   -1.212  1.00 22.33  ? 83  PHE B CE2    1 
ATOM   3923  C  CZ     . PHE B 2 84  ? 4.367   3.415   -0.511  1.00 19.23  ? 83  PHE B CZ     1 
ATOM   3924  H  H      . PHE B 2 84  ? 5.494   7.587   -2.907  1.00 24.45  ? 83  PHE B H      1 
ATOM   3925  H  HA     . PHE B 2 84  ? 4.150   7.277   -5.187  1.00 26.15  ? 83  PHE B HA     1 
ATOM   3926  H  HB2    . PHE B 2 84  ? 3.408   5.136   -4.753  1.00 26.50  ? 83  PHE B HB2    1 
ATOM   3927  H  HB3    . PHE B 2 84  ? 4.995   5.119   -4.814  1.00 26.50  ? 83  PHE B HB3    1 
ATOM   3928  H  HD1    . PHE B 2 84  ? 6.208   5.073   -2.631  1.00 23.76  ? 83  PHE B HD1    1 
ATOM   3929  H  HD2    . PHE B 2 84  ? 2.331   4.153   -2.901  1.00 24.61  ? 83  PHE B HD2    1 
ATOM   3930  H  HE1    . PHE B 2 84  ? 6.318   3.994   -0.575  1.00 26.46  ? 83  PHE B HE1    1 
ATOM   3931  H  HE2    . PHE B 2 84  ? 2.437   2.991   -0.882  1.00 26.83  ? 83  PHE B HE2    1 
ATOM   3932  H  HZ     . PHE B 2 84  ? 4.407   3.000   0.321   1.00 23.11  ? 83  PHE B HZ     1 
ATOM   3933  N  N      . GLU B 2 85  ? 1.898   7.269   -4.071  1.00 19.79  ? 84  GLU B N      1 
ATOM   3934  C  CA     . GLU B 2 85  ? 0.657   7.906   -3.656  1.00 21.34  ? 84  GLU B CA     1 
ATOM   3935  C  C      . GLU B 2 85  ? 0.175   7.285   -2.344  1.00 20.28  ? 84  GLU B C      1 
ATOM   3936  O  O      . GLU B 2 85  ? 0.585   6.185   -1.956  1.00 22.58  ? 84  GLU B O      1 
ATOM   3937  C  CB     . GLU B 2 85  ? -0.396  7.793   -4.781  1.00 24.01  ? 84  GLU B CB     1 
ATOM   3938  C  CG     . GLU B 2 85  ? -0.889  6.368   -5.073  1.00 27.27  ? 84  GLU B CG     1 
ATOM   3939  C  CD     . GLU B 2 85  ? 0.168   5.468   -5.738  1.00 29.40  ? 84  GLU B CD     1 
ATOM   3940  O  OE1    . GLU B 2 85  ? 1.097   5.972   -6.420  1.00 25.54  ? 84  GLU B OE1    1 
ATOM   3941  O  OE2    . GLU B 2 85  ? 0.062   4.251   -5.574  1.00 32.23  ? 84  GLU B OE2    1 
ATOM   3942  H  H      . GLU B 2 85  ? 1.797   6.736   -4.739  1.00 23.79  ? 84  GLU B H      1 
ATOM   3943  H  HA     . GLU B 2 85  ? 0.786   8.853   -3.493  1.00 25.64  ? 84  GLU B HA     1 
ATOM   3944  H  HB2    . GLU B 2 85  ? -1.170  8.322   -4.531  1.00 28.85  ? 84  GLU B HB2    1 
ATOM   3945  H  HB3    . GLU B 2 85  ? -0.008  8.139   -5.600  1.00 28.85  ? 84  GLU B HB3    1 
ATOM   3946  H  HG2    . GLU B 2 85  ? -1.149  5.951   -4.236  1.00 32.76  ? 84  GLU B HG2    1 
ATOM   3947  H  HG3    . GLU B 2 85  ? -1.653  6.418   -5.670  1.00 32.76  ? 84  GLU B HG3    1 
ATOM   3948  N  N      . ASP B 2 86  ? -0.695  8.016   -1.651  1.00 20.06  ? 85  ASP B N      1 
ATOM   3949  C  CA     . ASP B 2 86  ? -1.356  7.493   -0.460  1.00 17.53  ? 85  ASP B CA     1 
ATOM   3950  C  C      . ASP B 2 86  ? -2.370  6.406   -0.846  1.00 21.80  ? 85  ASP B C      1 
ATOM   3951  O  O      . ASP B 2 86  ? -3.329  6.662   -1.584  1.00 20.95  ? 85  ASP B O      1 
ATOM   3952  C  CB     . ASP B 2 86  ? -2.072  8.620   0.300   1.00 18.28  ? 85  ASP B CB     1 
ATOM   3953  C  CG     . ASP B 2 86  ? -1.136  9.679   0.829   1.00 19.36  ? 85  ASP B CG     1 
ATOM   3954  O  OD1    . ASP B 2 86  ? -0.085  9.332   1.452   1.00 18.57  ? 85  ASP B OD1    1 
ATOM   3955  O  OD2    . ASP B 2 86  ? -1.496  10.860  0.681   1.00 20.91  ? 85  ASP B OD2    1 
ATOM   3956  H  H      . ASP B 2 86  ? -0.919  8.822   -1.850  1.00 24.11  ? 85  ASP B H      1 
ATOM   3957  H  HA     . ASP B 2 86  ? -0.682  7.104   0.118   1.00 20.86  ? 85  ASP B HA     1 
ATOM   3958  H  HB2    . ASP B 2 86  ? -2.701  9.052   -0.299  1.00 21.97  ? 85  ASP B HB2    1 
ATOM   3959  H  HB3    . ASP B 2 86  ? -2.544  8.237   1.056   1.00 21.97  ? 85  ASP B HB3    1 
ATOM   3960  N  N      . GLU B 2 87  ? -2.173  5.210   -0.315  1.00 18.26  ? 86  GLU B N      1 
ATOM   3961  C  CA     . GLU B 2 87  ? -2.975  4.058   -0.715  1.00 20.97  ? 86  GLU B CA     1 
ATOM   3962  C  C      . GLU B 2 87  ? -4.389  4.145   -0.167  1.00 20.57  ? 86  GLU B C      1 
ATOM   3963  O  O      . GLU B 2 87  ? -5.360  4.034   -0.923  1.00 20.76  ? 86  GLU B O      1 
ATOM   3964  C  CB     . GLU B 2 87  ? -2.269  2.770   -0.294  1.00 22.33  ? 86  GLU B CB     1 
ATOM   3965  C  CG     . GLU B 2 87  ? -2.995  1.486   -0.669  1.00 26.70  ? 86  GLU B CG     1 
ATOM   3966  C  CD     . GLU B 2 87  ? -2.101  0.242   -0.526  1.00 24.38  ? 86  GLU B CD     1 
ATOM   3967  O  OE1    . GLU B 2 87  ? -1.051  0.316   0.184   1.00 19.98  ? 86  GLU B OE1    1 
ATOM   3968  O  OE2    . GLU B 2 87  ? -2.418  -0.793  -1.186  1.00 25.14  ? 86  GLU B OE2    1 
ATOM   3969  H  H      . GLU B 2 87  ? -1.580  5.033   0.282   1.00 21.95  ? 86  GLU B H      1 
ATOM   3970  H  HA     . GLU B 2 87  ? -3.055  4.043   -1.682  1.00 25.20  ? 86  GLU B HA     1 
ATOM   3971  H  HB2    . GLU B 2 87  ? -1.397  2.745   -0.717  1.00 26.83  ? 86  GLU B HB2    1 
ATOM   3972  H  HB3    . GLU B 2 87  ? -2.169  2.776   0.671   1.00 26.83  ? 86  GLU B HB3    1 
ATOM   3973  H  HG2    . GLU B 2 87  ? -3.762  1.374   -0.086  1.00 32.07  ? 86  GLU B HG2    1 
ATOM   3974  H  HG3    . GLU B 2 87  ? -3.285  1.544   -1.592  1.00 32.07  ? 86  GLU B HG3    1 
ATOM   3975  N  N      . ASN B 2 88  ? -4.529  4.329   1.140   1.00 18.91  ? 87  ASN B N      1 
ATOM   3976  C  CA     . ASN B 2 88  ? -5.801  4.612   1.777   1.00 19.34  ? 87  ASN B CA     1 
ATOM   3977  C  C      . ASN B 2 88  ? -5.502  4.976   3.230   1.00 20.57  ? 87  ASN B C      1 
ATOM   3978  O  O      . ASN B 2 88  ? -4.371  4.809   3.731   1.00 19.86  ? 87  ASN B O      1 
ATOM   3979  C  CB     . ASN B 2 88  ? -6.800  3.428   1.693   1.00 20.36  ? 87  ASN B CB     1 
ATOM   3980  C  CG     . ASN B 2 88  ? -6.325  2.223   2.455   1.00 25.20  ? 87  ASN B CG     1 
ATOM   3981  O  OD1    . ASN B 2 88  ? -6.152  2.272   3.672   1.00 20.78  ? 87  ASN B OD1    1 
ATOM   3982  N  ND2    . ASN B 2 88  ? -6.145  1.120   1.744   1.00 23.19  ? 87  ASN B ND2    1 
ATOM   3983  H  H      . ASN B 2 88  ? -3.875  4.294   1.698   1.00 22.52  ? 87  ASN B H      1 
ATOM   3984  H  HA     . ASN B 2 88  ? -6.220  5.366   1.331   1.00 23.04  ? 87  ASN B HA     1 
ATOM   3985  H  HB2    . ASN B 2 88  ? -7.652  3.703   2.066   1.00 24.46  ? 87  ASN B HB2    1 
ATOM   3986  H  HB3    . ASN B 2 88  ? -6.912  3.172   0.764   1.00 24.46  ? 87  ASN B HB3    1 
ATOM   3987  H  HD21   . ASN B 2 88  ? -5.874  0.400   2.129   1.00 27.87  ? 87  ASN B HD21   1 
ATOM   3988  H  HD22   . ASN B 2 88  ? -6.299  1.124   0.898   1.00 27.87  ? 87  ASN B HD22   1 
ATOM   3989  N  N      . PHE B 2 89  ? -6.515  5.513   3.885   1.00 19.41  ? 88  PHE B N      1 
ATOM   3990  C  CA     . PHE B 2 89  ? -6.418  5.942   5.273   1.00 19.20  ? 88  PHE B CA     1 
ATOM   3991  C  C      . PHE B 2 89  ? -7.401  5.166   6.135   1.00 20.09  ? 88  PHE B C      1 
ATOM   3992  O  O      . PHE B 2 89  ? -8.016  5.713   7.035   1.00 22.76  ? 88  PHE B O      1 
ATOM   3993  C  CB     . PHE B 2 89  ? -6.673  7.434   5.371   1.00 21.78  ? 88  PHE B CB     1 
ATOM   3994  C  CG     . PHE B 2 89  ? -5.647  8.267   4.640   1.00 20.13  ? 88  PHE B CG     1 
ATOM   3995  C  CD1    . PHE B 2 89  ? -4.347  8.337   5.097   1.00 19.09  ? 88  PHE B CD1    1 
ATOM   3996  C  CD2    . PHE B 2 89  ? -5.983  8.930   3.474   1.00 22.12  ? 88  PHE B CD2    1 
ATOM   3997  C  CE1    . PHE B 2 89  ? -3.420  9.083   4.460   1.00 21.33  ? 88  PHE B CE1    1 
ATOM   3998  C  CE2    . PHE B 2 89  ? -5.049  9.667   2.806   1.00 22.71  ? 88  PHE B CE2    1 
ATOM   3999  C  CZ     . PHE B 2 89  ? -3.768  9.758   3.284   1.00 21.67  ? 88  PHE B CZ     1 
ATOM   4000  H  H      . PHE B 2 89  ? -7.292  5.644   3.540   1.00 23.32  ? 88  PHE B H      1 
ATOM   4001  H  HA     . PHE B 2 89  ? -5.525  5.771   5.610   1.00 23.07  ? 88  PHE B HA     1 
ATOM   4002  H  HB2    . PHE B 2 89  ? -7.542  7.629   4.989   1.00 26.17  ? 88  PHE B HB2    1 
ATOM   4003  H  HB3    . PHE B 2 89  ? -6.656  7.694   6.306   1.00 26.17  ? 88  PHE B HB3    1 
ATOM   4004  H  HD1    . PHE B 2 89  ? -4.105  7.861   5.859   1.00 22.95  ? 88  PHE B HD1    1 
ATOM   4005  H  HD2    . PHE B 2 89  ? -6.850  8.874   3.143   1.00 26.58  ? 88  PHE B HD2    1 
ATOM   4006  H  HE1    . PHE B 2 89  ? -2.557  9.149   4.801   1.00 25.63  ? 88  PHE B HE1    1 
ATOM   4007  H  HE2    . PHE B 2 89  ? -5.283  10.110  2.022   1.00 27.28  ? 88  PHE B HE2    1 
ATOM   4008  H  HZ     . PHE B 2 89  ? -3.134  10.265  2.830   1.00 26.04  ? 88  PHE B HZ     1 
ATOM   4009  N  N      . ILE B 2 90  ? -7.615  3.909   5.780   1.00 21.01  ? 89  ILE B N      1 
ATOM   4010  C  CA     . ILE B 2 90  ? -8.601  3.090   6.477   1.00 21.12  ? 89  ILE B CA     1 
ATOM   4011  C  C      . ILE B 2 90  ? -8.218  2.958   7.947   1.00 22.00  ? 89  ILE B C      1 
ATOM   4012  O  O      . ILE B 2 90  ? -9.041  3.135   8.852   1.00 23.34  ? 89  ILE B O      1 
ATOM   4013  C  CB     . ILE B 2 90  ? -8.697  1.709   5.800   1.00 20.87  ? 89  ILE B CB     1 
ATOM   4014  C  CG1    . ILE B 2 90  ? -9.331  1.818   4.399   1.00 21.34  ? 89  ILE B CG1    1 
ATOM   4015  C  CG2    . ILE B 2 90  ? -9.548  0.733   6.677   1.00 24.22  ? 89  ILE B CG2    1 
ATOM   4016  C  CD1    . ILE B 2 90  ? -9.205  0.561   3.577   1.00 27.39  ? 89  ILE B CD1    1 
ATOM   4017  H  H      . ILE B 2 90  ? -7.205  3.504   5.141   1.00 25.25  ? 89  ILE B H      1 
ATOM   4018  H  HA     . ILE B 2 90  ? -9.469  3.520   6.427   1.00 25.38  ? 89  ILE B HA     1 
ATOM   4019  H  HB     . ILE B 2 90  ? -7.794  1.367   5.709   1.00 25.08  ? 89  ILE B HB     1 
ATOM   4020  H  HG12   . ILE B 2 90  ? -10.276 2.014   4.499   1.00 25.64  ? 89  ILE B HG12   1 
ATOM   4021  H  HG13   . ILE B 2 90  ? -8.893  2.535   3.914   1.00 25.64  ? 89  ILE B HG13   1 
ATOM   4022  H  HG21   . ILE B 2 90  ? -9.808  -0.031  6.138   1.00 29.10  ? 89  ILE B HG21   1 
ATOM   4023  H  HG22   . ILE B 2 90  ? -9.014  0.438   7.431   1.00 29.10  ? 89  ILE B HG22   1 
ATOM   4024  H  HG23   . ILE B 2 90  ? -10.338 1.199   6.993   1.00 29.10  ? 89  ILE B HG23   1 
ATOM   4025  H  HD11   . ILE B 2 90  ? -9.445  0.760   2.659   1.00 32.90  ? 89  ILE B HD11   1 
ATOM   4026  H  HD12   . ILE B 2 90  ? -8.288  0.247   3.619   1.00 32.90  ? 89  ILE B HD12   1 
ATOM   4027  H  HD13   . ILE B 2 90  ? -9.803  -0.113  3.937   1.00 32.90  ? 89  ILE B HD13   1 
ATOM   4028  N  N      . LEU B 2 91  ? -6.963  2.638   8.196   1.00 22.19  ? 90  LEU B N      1 
ATOM   4029  C  CA     . LEU B 2 91  ? -6.476  2.335   9.533   1.00 19.51  ? 90  LEU B CA     1 
ATOM   4030  C  C      . LEU B 2 91  ? -6.047  3.626   10.247  1.00 23.72  ? 90  LEU B C      1 
ATOM   4031  O  O      . LEU B 2 91  ? -5.516  4.558   9.626   1.00 21.09  ? 90  LEU B O      1 
ATOM   4032  C  CB     . LEU B 2 91  ? -5.301  1.358   9.445   1.00 22.89  ? 90  LEU B CB     1 
ATOM   4033  C  CG     . LEU B 2 91  ? -5.663  -0.003  8.827   1.00 24.44  ? 90  LEU B CG     1 
ATOM   4034  C  CD1    . LEU B 2 91  ? -4.516  -1.031  8.767   1.00 26.61  ? 90  LEU B CD1    1 
ATOM   4035  C  CD2    . LEU B 2 91  ? -6.837  -0.622  9.617   1.00 28.93  ? 90  LEU B CD2    1 
ATOM   4036  H  H      . LEU B 2 91  ? -6.354  2.588   7.591   1.00 26.66  ? 90  LEU B H      1 
ATOM   4037  H  HA     . LEU B 2 91  ? -7.177  1.924   10.062  1.00 23.42  ? 90  LEU B HA     1 
ATOM   4038  H  HB2    . LEU B 2 91  ? -4.607  1.756   8.897   1.00 27.50  ? 90  LEU B HB2    1 
ATOM   4039  H  HB3    . LEU B 2 91  ? -4.965  1.196   10.341  1.00 27.50  ? 90  LEU B HB3    1 
ATOM   4040  H  HG     . LEU B 2 91  ? -5.895  0.180   7.904   1.00 29.36  ? 90  LEU B HG     1 
ATOM   4041  H  HD11   . LEU B 2 91  ? -4.831  -1.829  8.313   1.00 31.96  ? 90  LEU B HD11   1 
ATOM   4042  H  HD12   . LEU B 2 91  ? -3.772  -0.646  8.280   1.00 31.96  ? 90  LEU B HD12   1 
ATOM   4043  H  HD13   . LEU B 2 91  ? -4.242  -1.252  9.671   1.00 31.96  ? 90  LEU B HD13   1 
ATOM   4044  H  HD21   . LEU B 2 91  ? -6.895  -1.567  9.408   1.00 34.75  ? 90  LEU B HD21   1 
ATOM   4045  H  HD22   . LEU B 2 91  ? -6.676  -0.503  10.567  1.00 34.75  ? 90  LEU B HD22   1 
ATOM   4046  H  HD23   . LEU B 2 91  ? -7.659  -0.175  9.362   1.00 34.75  ? 90  LEU B HD23   1 
ATOM   4047  N  N      . LYS B 2 92  ? -6.247  3.651   11.585  1.00 21.91  ? 91  LYS B N      1 
ATOM   4048  C  CA     . LYS B 2 92  ? -6.026  4.833   12.405  1.00 22.60  ? 91  LYS B CA     1 
ATOM   4049  C  C      . LYS B 2 92  ? -4.828  4.673   13.358  1.00 20.91  ? 91  LYS B C      1 
ATOM   4050  O  O      . LYS B 2 92  ? -4.347  3.567   13.636  1.00 23.21  ? 91  LYS B O      1 
ATOM   4051  C  CB     . LYS B 2 92  ? -7.280  5.163   13.233  1.00 23.32  ? 91  LYS B CB     1 
ATOM   4052  C  CG     . LYS B 2 92  ? -8.601  5.089   12.460  1.00 28.34  ? 91  LYS B CG     1 
ATOM   4053  C  CD     . LYS B 2 92  ? -8.623  6.025   11.278  1.00 31.45  ? 91  LYS B CD     1 
ATOM   4054  C  CE     . LYS B 2 92  ? -10.070 6.243   10.801  1.00 34.46  ? 91  LYS B CE     1 
ATOM   4055  N  NZ     . LYS B 2 92  ? -10.071 6.678   9.356   1.00 35.64  ? 91  LYS B NZ     1 
ATOM   4056  H  H      . LYS B 2 92  ? -6.518  2.972   12.037  1.00 26.33  ? 91  LYS B H      1 
ATOM   4057  H  HA     . LYS B 2 92  ? -5.821  5.570   11.807  1.00 27.16  ? 91  LYS B HA     1 
ATOM   4058  H  HB2    . LYS B 2 92  ? -7.337  4.533   13.969  1.00 28.02  ? 91  LYS B HB2    1 
ATOM   4059  H  HB3    . LYS B 2 92  ? -7.193  6.067   13.576  1.00 28.02  ? 91  LYS B HB3    1 
ATOM   4060  H  HG2    . LYS B 2 92  ? -8.728  4.185   12.132  1.00 34.04  ? 91  LYS B HG2    1 
ATOM   4061  H  HG3    . LYS B 2 92  ? -9.330  5.332   13.052  1.00 34.04  ? 91  LYS B HG3    1 
ATOM   4062  H  HD2    . LYS B 2 92  ? -8.248  6.882   11.534  1.00 37.78  ? 91  LYS B HD2    1 
ATOM   4063  H  HD3    . LYS B 2 92  ? -8.110  5.643   10.549  1.00 37.78  ? 91  LYS B HD3    1 
ATOM   4064  H  HE2    . LYS B 2 92  ? -10.568 5.414   10.878  1.00 41.39  ? 91  LYS B HE2    1 
ATOM   4065  H  HE3    . LYS B 2 92  ? -10.491 6.934   11.336  1.00 41.39  ? 91  LYS B HE3    1 
ATOM   4066  H  HZ1    . LYS B 2 92  ? -9.830  5.999   8.834   1.00 42.80  ? 91  LYS B HZ1    1 
ATOM   4067  H  HZ2    . LYS B 2 92  ? -10.885 6.949   9.121   1.00 42.80  ? 91  LYS B HZ2    1 
ATOM   4068  H  HZ3    . LYS B 2 92  ? -9.498  7.349   9.240   1.00 42.80  ? 91  LYS B HZ3    1 
ATOM   4069  N  N      . HIS B 2 93  ? -4.345  5.812   13.849  1.00 20.26  ? 92  HIS B N      1 
ATOM   4070  C  CA     . HIS B 2 93  ? -3.206  5.838   14.774  1.00 20.02  ? 92  HIS B CA     1 
ATOM   4071  C  C      . HIS B 2 93  ? -3.811  5.693   16.171  1.00 20.07  ? 92  HIS B C      1 
ATOM   4072  O  O      . HIS B 2 93  ? -4.065  6.666   16.865  1.00 23.66  ? 92  HIS B O      1 
ATOM   4073  C  CB     . HIS B 2 93  ? -2.397  7.124   14.632  1.00 19.26  ? 92  HIS B CB     1 
ATOM   4074  C  CG     . HIS B 2 93  ? -1.823  7.352   13.258  1.00 19.78  ? 92  HIS B CG     1 
ATOM   4075  N  ND1    . HIS B 2 93  ? -2.583  7.839   12.219  1.00 18.87  ? 92  HIS B ND1    1 
ATOM   4076  C  CD2    . HIS B 2 93  ? -0.577  7.172   12.761  1.00 19.94  ? 92  HIS B CD2    1 
ATOM   4077  C  CE1    . HIS B 2 93  ? -1.825  7.960   11.138  1.00 19.52  ? 92  HIS B CE1    1 
ATOM   4078  N  NE2    . HIS B 2 93  ? -0.606  7.550   11.434  1.00 18.20  ? 92  HIS B NE2    1 
ATOM   4079  H  H      . HIS B 2 93  ? -4.659  6.591   13.661  1.00 24.35  ? 92  HIS B H      1 
ATOM   4080  H  HA     . HIS B 2 93  ? -2.599  5.106   14.587  1.00 24.06  ? 92  HIS B HA     1 
ATOM   4081  H  HB2    . HIS B 2 93  ? -2.974  7.876   14.837  1.00 23.14  ? 92  HIS B HB2    1 
ATOM   4082  H  HB3    . HIS B 2 93  ? -1.656  7.093   15.257  1.00 23.14  ? 92  HIS B HB3    1 
ATOM   4083  H  HD1    . HIS B 2 93  ? -3.419  8.034   12.263  1.00 22.68  ? 92  HIS B HD1    1 
ATOM   4084  H  HD2    . HIS B 2 93  ? 0.162   6.854   13.227  1.00 23.96  ? 92  HIS B HD2    1 
ATOM   4085  H  HE1    . HIS B 2 93  ? -2.106  8.280   10.311  1.00 23.46  ? 92  HIS B HE1    1 
ATOM   4086  N  N      . THR B 2 94  ? -4.086  4.430   16.571  1.00 22.43  ? 93  THR B N      1 
ATOM   4087  C  CA     . THR B 2 94  ? -4.939  4.154   17.728  1.00 23.62  ? 93  THR B CA     1 
ATOM   4088  C  C      . THR B 2 94  ? -4.181  4.079   19.047  1.00 23.55  ? 93  THR B C      1 
ATOM   4089  O  O      . THR B 2 94  ? -4.814  4.126   20.113  1.00 23.72  ? 93  THR B O      1 
ATOM   4090  C  CB     . THR B 2 94  ? -5.681  2.824   17.545  1.00 21.65  ? 93  THR B CB     1 
ATOM   4091  O  OG1    . THR B 2 94  ? -4.756  1.827   17.121  1.00 25.40  ? 93  THR B OG1    1 
ATOM   4092  C  CG2    . THR B 2 94  ? -6.762  2.985   16.493  1.00 26.18  ? 93  THR B CG2    1 
ATOM   4093  H  H      . THR B 2 94  ? -3.787  3.724   16.182  1.00 26.95  ? 93  THR B H      1 
ATOM   4094  H  HA     . THR B 2 94  ? -5.587  4.873   17.786  1.00 28.37  ? 93  THR B HA     1 
ATOM   4095  H  HB     . THR B 2 94  ? -6.093  2.550   18.379  1.00 26.01  ? 93  THR B HB     1 
ATOM   4096  H  HG1    . THR B 2 94  ? -5.154  1.097   17.002  1.00 30.51  ? 93  THR B HG1    1 
ATOM   4097  H  HG21   . THR B 2 94  ? -7.239  2.148   16.377  1.00 31.45  ? 93  THR B HG21   1 
ATOM   4098  H  HG22   . THR B 2 94  ? -7.391  3.670   16.767  1.00 31.45  ? 93  THR B HG22   1 
ATOM   4099  H  HG23   . THR B 2 94  ? -6.365  3.241   15.646  1.00 31.45  ? 93  THR B HG23   1 
ATOM   4100  N  N      . GLY B 2 95  ? -2.859  3.946   18.993  1.00 23.14  ? 94  GLY B N      1 
ATOM   4101  C  CA     . GLY B 2 95  ? -2.077  3.713   20.190  1.00 22.69  ? 94  GLY B CA     1 
ATOM   4102  C  C      . GLY B 2 95  ? -0.641  3.351   19.900  1.00 23.08  ? 94  GLY B C      1 
ATOM   4103  O  O      . GLY B 2 95  ? -0.185  3.281   18.748  1.00 21.33  ? 94  GLY B O      1 
ATOM   4104  H  H      . GLY B 2 95  ? -2.395  3.987   18.270  1.00 27.80  ? 94  GLY B H      1 
ATOM   4105  H  HA2    . GLY B 2 95  ? -2.082  4.516   20.735  1.00 27.26  ? 94  GLY B HA2    1 
ATOM   4106  H  HA3    . GLY B 2 95  ? -2.475  2.987   20.694  1.00 27.26  ? 94  GLY B HA3    1 
ATOM   4107  N  N      . PRO B 2 96  ? 0.113   3.105   20.977  1.00 19.23  ? 95  PRO B N      1 
ATOM   4108  C  CA     . PRO B 2 96  ? 1.500   2.661   20.821  1.00 20.15  ? 95  PRO B CA     1 
ATOM   4109  C  C      . PRO B 2 96  ? 1.599   1.423   19.939  1.00 20.97  ? 95  PRO B C      1 
ATOM   4110  O  O      . PRO B 2 96  ? 0.738   0.532   19.977  1.00 21.25  ? 95  PRO B O      1 
ATOM   4111  C  CB     . PRO B 2 96  ? 1.958   2.362   22.261  1.00 21.90  ? 95  PRO B CB     1 
ATOM   4112  C  CG     . PRO B 2 96  ? 0.966   2.875   23.141  1.00 22.26  ? 95  PRO B CG     1 
ATOM   4113  C  CD     . PRO B 2 96  ? -0.358  3.030   22.368  1.00 25.24  ? 95  PRO B CD     1 
ATOM   4114  H  HA     . PRO B 2 96  ? 2.038   3.376   20.448  1.00 24.22  ? 95  PRO B HA     1 
ATOM   4115  H  HB2    . PRO B 2 96  ? 2.048   1.402   22.375  1.00 26.31  ? 95  PRO B HB2    1 
ATOM   4116  H  HB3    . PRO B 2 96  ? 2.810   2.796   22.422  1.00 26.31  ? 95  PRO B HB3    1 
ATOM   4117  H  HG2    . PRO B 2 96  ? 0.849   2.255   23.878  1.00 26.75  ? 95  PRO B HG2    1 
ATOM   4118  H  HG3    . PRO B 2 96  ? 1.258   3.737   23.475  1.00 26.75  ? 95  PRO B HG3    1 
ATOM   4119  H  HD2    . PRO B 2 96  ? -0.935  2.262   22.502  1.00 30.32  ? 95  PRO B HD2    1 
ATOM   4120  H  HD3    . PRO B 2 96  ? -0.822  3.842   22.626  1.00 30.32  ? 95  PRO B HD3    1 
ATOM   4121  N  N      . GLY B 2 97  ? 2.653   1.391   19.121  1.00 19.84  ? 96  GLY B N      1 
ATOM   4122  C  CA     . GLY B 2 97  ? 2.972   0.261   18.277  1.00 22.54  ? 96  GLY B CA     1 
ATOM   4123  C  C      . GLY B 2 97  ? 2.545   0.425   16.832  1.00 18.81  ? 96  GLY B C      1 
ATOM   4124  O  O      . GLY B 2 97  ? 3.055   -0.301  15.957  1.00 18.94  ? 96  GLY B O      1 
ATOM   4125  H  H      . GLY B 2 97  ? 3.212   2.040   19.042  1.00 23.84  ? 96  GLY B H      1 
ATOM   4126  H  HA2    . GLY B 2 97  ? 3.932   0.120   18.291  1.00 27.08  ? 96  GLY B HA2    1 
ATOM   4127  H  HA3    . GLY B 2 97  ? 2.533   -0.529  18.630  1.00 27.08  ? 96  GLY B HA3    1 
ATOM   4128  N  N      . ILE B 2 98  ? 1.672   1.395   16.570  1.00 18.57  ? 97  ILE B N      1 
ATOM   4129  C  CA     . ILE B 2 98  ? 1.194   1.661   15.210  1.00 18.00  ? 97  ILE B CA     1 
ATOM   4130  C  C      . ILE B 2 98  ? 2.385   2.052   14.325  1.00 18.58  ? 97  ILE B C      1 
ATOM   4131  O  O      . ILE B 2 98  ? 3.219   2.896   14.679  1.00 17.76  ? 97  ILE B O      1 
ATOM   4132  C  CB     . ILE B 2 98  ? 0.094   2.741   15.245  1.00 18.66  ? 97  ILE B CB     1 
ATOM   4133  C  CG1    . ILE B 2 98  ? -1.225  2.237   15.835  1.00 22.07  ? 97  ILE B CG1    1 
ATOM   4134  C  CG2    . ILE B 2 98  ? -0.103  3.337   13.849  1.00 18.81  ? 97  ILE B CG2    1 
ATOM   4135  C  CD1    . ILE B 2 98  ? -1.952  1.264   14.954  1.00 23.32  ? 97  ILE B CD1    1 
ATOM   4136  H  H      . ILE B 2 98  ? 1.337   1.919   17.164  1.00 22.31  ? 97  ILE B H      1 
ATOM   4137  H  HA     . ILE B 2 98  ? 0.804   0.858   14.832  1.00 21.63  ? 97  ILE B HA     1 
ATOM   4138  H  HB     . ILE B 2 98  ? 0.399   3.438   15.847  1.00 22.42  ? 97  ILE B HB     1 
ATOM   4139  H  HG12   . ILE B 2 98  ? -1.040  1.791   16.677  1.00 26.52  ? 97  ILE B HG12   1 
ATOM   4140  H  HG13   . ILE B 2 98  ? -1.810  2.996   15.983  1.00 26.52  ? 97  ILE B HG13   1 
ATOM   4141  H  HG21   . ILE B 2 98  ? -0.957  3.797   13.820  1.00 22.61  ? 97  ILE B HG21   1 
ATOM   4142  H  HG22   . ILE B 2 98  ? 0.616   3.963   13.669  1.00 22.61  ? 97  ILE B HG22   1 
ATOM   4143  H  HG23   . ILE B 2 98  ? -0.090  2.621   13.195  1.00 22.61  ? 97  ILE B HG23   1 
ATOM   4144  H  HD11   . ILE B 2 98  ? -2.650  0.831   15.470  1.00 28.01  ? 97  ILE B HD11   1 
ATOM   4145  H  HD12   . ILE B 2 98  ? -2.343  1.745   14.208  1.00 28.01  ? 97  ILE B HD12   1 
ATOM   4146  H  HD13   . ILE B 2 98  ? -1.323  0.601   14.628  1.00 28.01  ? 97  ILE B HD13   1 
ATOM   4147  N  N      . LEU B 2 99  ? 2.472   1.414   13.160  1.00 16.99  ? 98  LEU B N      1 
ATOM   4148  C  CA     . LEU B 2 99  ? 3.516   1.662   12.172  1.00 16.29  ? 98  LEU B CA     1 
ATOM   4149  C  C      . LEU B 2 99  ? 2.876   2.388   10.981  1.00 17.46  ? 98  LEU B C      1 
ATOM   4150  O  O      . LEU B 2 99  ? 1.917   1.883   10.384  1.00 18.71  ? 98  LEU B O      1 
ATOM   4151  C  CB     . LEU B 2 99  ? 4.134   0.355   11.701  1.00 17.70  ? 98  LEU B CB     1 
ATOM   4152  C  CG     . LEU B 2 99  ? 5.156   0.437   10.594  1.00 18.59  ? 98  LEU B CG     1 
ATOM   4153  C  CD1    . LEU B 2 99  ? 6.391   1.159   11.083  1.00 17.20  ? 98  LEU B CD1    1 
ATOM   4154  C  CD2    . LEU B 2 99  ? 5.509   -0.975  10.118  1.00 19.76  ? 98  LEU B CD2    1 
ATOM   4155  H  H      . LEU B 2 99  ? 1.915   0.808   12.910  1.00 20.42  ? 98  LEU B H      1 
ATOM   4156  H  HA     . LEU B 2 99  ? 4.211   2.217   12.559  1.00 19.38  ? 98  LEU B HA     1 
ATOM   4157  H  HB2    . LEU B 2 99  ? 4.574   -0.058  12.460  1.00 21.27  ? 98  LEU B HB2    1 
ATOM   4158  H  HB3    . LEU B 2 99  ? 3.418   -0.216  11.381  1.00 21.27  ? 98  LEU B HB3    1 
ATOM   4159  H  HG     . LEU B 2 99  ? 4.794   0.934   9.844   1.00 22.34  ? 98  LEU B HG     1 
ATOM   4160  H  HD11   . LEU B 2 99  ? 7.049   1.176   10.370  1.00 20.67  ? 98  LEU B HD11   1 
ATOM   4161  H  HD12   . LEU B 2 99  ? 6.150   2.064   11.332  1.00 20.67  ? 98  LEU B HD12   1 
ATOM   4162  H  HD13   . LEU B 2 99  ? 6.749   0.688   11.851  1.00 20.67  ? 98  LEU B HD13   1 
ATOM   4163  H  HD21   . LEU B 2 99  ? 6.177   -0.915  9.418   1.00 23.75  ? 98  LEU B HD21   1 
ATOM   4164  H  HD22   . LEU B 2 99  ? 5.859   -1.483  10.867  1.00 23.75  ? 98  LEU B HD22   1 
ATOM   4165  H  HD23   . LEU B 2 99  ? 4.708   -1.402  9.775   1.00 23.75  ? 98  LEU B HD23   1 
ATOM   4166  N  N      . SER B 2 100 ? 3.408   3.549   10.627  1.00 15.69  ? 99  SER B N      1 
ATOM   4167  C  CA     . SER B 2 100 ? 2.774   4.459   9.686   1.00 16.64  ? 99  SER B CA     1 
ATOM   4168  C  C      . SER B 2 100 ? 3.825   5.173   8.830   1.00 16.92  ? 99  SER B C      1 
ATOM   4169  O  O      . SER B 2 100 ? 5.017   5.276   9.165   1.00 15.63  ? 99  SER B O      1 
ATOM   4170  C  CB     . SER B 2 100 ? 1.893   5.453   10.430  1.00 17.52  ? 99  SER B CB     1 
ATOM   4171  O  OG     . SER B 2 100 ? 1.194   6.376   9.579   1.00 16.94  ? 99  SER B OG     1 
ATOM   4172  H  H      . SER B 2 100 ? 4.159   3.841   10.928  1.00 18.66  ? 99  SER B H      1 
ATOM   4173  H  HA     . SER B 2 100 ? 2.226   3.957   9.062   1.00 20.00  ? 99  SER B HA     1 
ATOM   4174  H  HB2    . SER B 2 100 ? 1.235   4.952   10.937  1.00 21.06  ? 99  SER B HB2    1 
ATOM   4175  H  HB3    . SER B 2 100 ? 2.456   5.965   11.031  1.00 21.06  ? 99  SER B HB3    1 
ATOM   4176  H  HG     . SER B 2 100 ? 1.089   7.109   9.975   1.00 20.36  ? 99  SER B HG     1 
ATOM   4177  N  N      . MET B 2 101 ? 3.386   5.674   7.696   1.00 15.25  ? 100 MET B N      1 
ATOM   4178  C  CA     . MET B 2 101 ? 4.312   6.230   6.720   1.00 14.91  ? 100 MET B CA     1 
ATOM   4179  C  C      . MET B 2 101 ? 4.532   7.706   7.016   1.00 15.58  ? 100 MET B C      1 
ATOM   4180  O  O      . MET B 2 101 ? 3.574   8.464   7.187   1.00 15.06  ? 100 MET B O      1 
ATOM   4181  C  CB     . MET B 2 101 ? 3.714   6.149   5.301   1.00 16.39  ? 100 MET B CB     1 
ATOM   4182  C  CG     . MET B 2 101 ? 4.008   4.878   4.539   1.00 16.31  ? 100 MET B CG     1 
ATOM   4183  S  SD     . MET B 2 101 ? 5.462   3.986   4.784   1.00 19.07  ? 100 MET B SD     1 
ATOM   4184  C  CE     . MET B 2 101 ? 6.422   4.576   3.367   1.00 21.92  ? 100 MET B CE     1 
ATOM   4185  H  H      . MET B 2 101 ? 2.558   5.706   7.463   1.00 18.33  ? 100 MET B H      1 
ATOM   4186  H  HA     . MET B 2 101 ? 5.140   5.727   6.766   1.00 17.92  ? 100 MET B HA     1 
ATOM   4187  H  HB2    . MET B 2 101 ? 2.750   6.226   5.372   1.00 19.70  ? 100 MET B HB2    1 
ATOM   4188  H  HB3    . MET B 2 101 ? 4.068   6.886   4.779   1.00 19.70  ? 100 MET B HB3    1 
ATOM   4189  H  HG2    . MET B 2 101 ? 3.287   4.259   4.737   1.00 19.61  ? 100 MET B HG2    1 
ATOM   4190  H  HG3    . MET B 2 101 ? 3.999   5.107   3.597   1.00 19.61  ? 100 MET B HG3    1 
ATOM   4191  H  HE1    . MET B 2 101 ? 7.321   4.215   3.422   1.00 26.34  ? 100 MET B HE1    1 
ATOM   4192  H  HE2    . MET B 2 101 ? 5.994   4.277   2.549   1.00 26.34  ? 100 MET B HE2    1 
ATOM   4193  H  HE3    . MET B 2 101 ? 6.453   5.546   3.389   1.00 26.34  ? 100 MET B HE3    1 
ATOM   4194  N  N      . ALA B 2 102 ? 5.773   8.122   7.050   1.00 14.17  ? 101 ALA B N      1 
ATOM   4195  C  CA     . ALA B 2 102 ? 6.051   9.541   7.031   1.00 13.91  ? 101 ALA B CA     1 
ATOM   4196  C  C      . ALA B 2 102 ? 5.851   10.129  5.628   1.00 16.17  ? 101 ALA B C      1 
ATOM   4197  O  O      . ALA B 2 102 ? 5.868   9.427   4.623   1.00 17.22  ? 101 ALA B O      1 
ATOM   4198  C  CB     . ALA B 2 102 ? 7.477   9.784   7.506   1.00 13.85  ? 101 ALA B CB     1 
ATOM   4199  H  H      . ALA B 2 102 ? 6.465   7.613   7.083   1.00 16.83  ? 101 ALA B H      1 
ATOM   4200  H  HA     . ALA B 2 102 ? 5.439   10.003  7.624   1.00 16.53  ? 101 ALA B HA     1 
ATOM   4201  H  HB1    . ALA B 2 102 ? 7.666   10.735  7.465   1.00 16.65  ? 101 ALA B HB1    1 
ATOM   4202  H  HB2    . ALA B 2 102 ? 7.563   9.469   8.420   1.00 16.65  ? 101 ALA B HB2    1 
ATOM   4203  H  HB3    . ALA B 2 102 ? 8.089   9.300   6.930   1.00 16.65  ? 101 ALA B HB3    1 
ATOM   4204  N  N      . ASN B 2 103 ? 5.666   11.447  5.568   1.00 16.66  ? 102 ASN B N      1 
ATOM   4205  C  CA     . ASN B 2 103 ? 5.473   12.091  4.269   1.00 17.04  ? 102 ASN B CA     1 
ATOM   4206  C  C      . ASN B 2 103 ? 5.712   13.590  4.385   1.00 19.49  ? 102 ASN B C      1 
ATOM   4207  O  O      . ASN B 2 103 ? 5.895   14.147  5.475   1.00 19.41  ? 102 ASN B O      1 
ATOM   4208  C  CB     . ASN B 2 103 ? 4.065   11.794  3.728   1.00 17.52  ? 102 ASN B CB     1 
ATOM   4209  C  CG     . ASN B 2 103 ? 2.959   12.417  4.557   1.00 17.46  ? 102 ASN B CG     1 
ATOM   4210  O  OD1    . ASN B 2 103 ? 2.951   13.613  4.829   1.00 17.36  ? 102 ASN B OD1    1 
ATOM   4211  N  ND2    . ASN B 2 103 ? 1.946   11.628  4.858   1.00 18.58  ? 102 ASN B ND2    1 
ATOM   4212  H  H      . ASN B 2 103 ? 5.648   11.976  6.246   1.00 20.02  ? 102 ASN B H      1 
ATOM   4213  H  HA     . ASN B 2 103 ? 6.137   11.749  3.650   1.00 20.48  ? 102 ASN B HA     1 
ATOM   4214  H  HB2    . ASN B 2 103 ? 3.995   12.145  2.826   1.00 21.05  ? 102 ASN B HB2    1 
ATOM   4215  H  HB3    . ASN B 2 103 ? 3.928   10.833  3.721   1.00 21.05  ? 102 ASN B HB3    1 
ATOM   4216  H  HD21   . ASN B 2 103 ? 1.291   11.929  5.326   1.00 22.33  ? 102 ASN B HD21   1 
ATOM   4217  H  HD22   . ASN B 2 103 ? 1.941   10.812  4.586   1.00 22.33  ? 102 ASN B HD22   1 
ATOM   4218  N  N      . ALA B 2 104 ? 5.675   14.245  3.236   1.00 18.46  ? 103 ALA B N      1 
ATOM   4219  C  CA     . ALA B 2 104 ? 5.833   15.682  3.151   1.00 20.62  ? 103 ALA B CA     1 
ATOM   4220  C  C      . ALA B 2 104 ? 4.615   16.308  2.508   1.00 23.31  ? 103 ALA B C      1 
ATOM   4221  O  O      . ALA B 2 104 ? 4.712   17.245  1.719   1.00 27.28  ? 103 ALA B O      1 
ATOM   4222  C  CB     . ALA B 2 104 ? 7.100   16.012  2.378   1.00 21.39  ? 103 ALA B CB     1 
ATOM   4223  H  H      . ALA B 2 104 ? 5.556   13.866  2.474   1.00 22.18  ? 103 ALA B H      1 
ATOM   4224  H  HA     . ALA B 2 104 ? 5.916   16.059  4.040   1.00 24.78  ? 103 ALA B HA     1 
ATOM   4225  H  HB1    . ALA B 2 104 ? 7.192   16.975  2.318   1.00 25.71  ? 103 ALA B HB1    1 
ATOM   4226  H  HB2    . ALA B 2 104 ? 7.862   15.635  2.845   1.00 25.71  ? 103 ALA B HB2    1 
ATOM   4227  H  HB3    . ALA B 2 104 ? 7.036   15.630  1.488   1.00 25.71  ? 103 ALA B HB3    1 
ATOM   4228  N  N      . GLY B 2 105 ? 3.455   15.778  2.853   1.00 22.02  ? 104 GLY B N      1 
ATOM   4229  C  CA     . GLY B 2 105 ? 2.202   16.151  2.254   1.00 20.16  ? 104 GLY B CA     1 
ATOM   4230  C  C      . GLY B 2 105 ? 1.581   15.022  1.465   1.00 20.89  ? 104 GLY B C      1 
ATOM   4231  O  O      . GLY B 2 105 ? 2.090   13.889  1.417   1.00 19.25  ? 104 GLY B O      1 
ATOM   4232  H  H      . GLY B 2 105 ? 3.369   15.174  3.459   1.00 26.46  ? 104 GLY B H      1 
ATOM   4233  H  HA2    . GLY B 2 105 ? 1.580   16.416  2.949   1.00 24.23  ? 104 GLY B HA2    1 
ATOM   4234  H  HA3    . GLY B 2 105 ? 2.344   16.900  1.654   1.00 24.23  ? 104 GLY B HA3    1 
ATOM   4235  N  N      . PRO B 2 106 ? 0.458   15.314  0.822   1.00 21.41  ? 105 PRO B N      1 
ATOM   4236  C  CA     . PRO B 2 106 ? -0.269  14.260  0.100   1.00 22.30  ? 105 PRO B CA     1 
ATOM   4237  C  C      . PRO B 2 106 ? 0.585   13.582  -0.948  1.00 20.25  ? 105 PRO B C      1 
ATOM   4238  O  O      . PRO B 2 106 ? 1.328   14.237  -1.685  1.00 19.60  ? 105 PRO B O      1 
ATOM   4239  C  CB     . PRO B 2 106 ? -1.429  15.017  -0.559  1.00 22.35  ? 105 PRO B CB     1 
ATOM   4240  C  CG     . PRO B 2 106 ? -1.653  16.215  0.336   1.00 28.95  ? 105 PRO B CG     1 
ATOM   4241  C  CD     . PRO B 2 106 ? -0.245  16.608  0.775   1.00 27.09  ? 105 PRO B CD     1 
ATOM   4242  H  HA     . PRO B 2 106 ? -0.597  13.600  0.730   1.00 26.80  ? 105 PRO B HA     1 
ATOM   4243  H  HB2    . PRO B 2 106 ? -1.180  15.291  -1.455  1.00 26.85  ? 105 PRO B HB2    1 
ATOM   4244  H  HB3    . PRO B 2 106 ? -2.217  14.453  -0.591  1.00 26.85  ? 105 PRO B HB3    1 
ATOM   4245  H  HG2    . PRO B 2 106 ? -2.078  16.931  -0.162  1.00 34.77  ? 105 PRO B HG2    1 
ATOM   4246  H  HG3    . PRO B 2 106 ? -2.202  15.969  1.096   1.00 34.77  ? 105 PRO B HG3    1 
ATOM   4247  H  HD2    . PRO B 2 106 ? 0.166   17.202  0.128   1.00 32.55  ? 105 PRO B HD2    1 
ATOM   4248  H  HD3    . PRO B 2 106 ? -0.259  17.027  1.649   1.00 32.55  ? 105 PRO B HD3    1 
ATOM   4249  N  N      . ASN B 2 107 ? 0.450   12.248  -1.009  1.00 16.84  ? 106 ASN B N      1 
ATOM   4250  C  CA     . ASN B 2 107 ? 1.037   11.414  -2.047  1.00 17.83  ? 106 ASN B CA     1 
ATOM   4251  C  C      . ASN B 2 107 ? 2.544   11.571  -2.168  1.00 18.70  ? 106 ASN B C      1 
ATOM   4252  O  O      . ASN B 2 107 ? 3.081   11.666  -3.281  1.00 19.77  ? 106 ASN B O      1 
ATOM   4253  C  CB     . ASN B 2 107 ? 0.347   11.740  -3.380  1.00 17.43  ? 106 ASN B CB     1 
ATOM   4254  C  CG     . ASN B 2 107 ? -1.110  11.513  -3.304  1.00 18.27  ? 106 ASN B CG     1 
ATOM   4255  O  OD1    . ASN B 2 107 ? -1.541  10.450  -2.820  1.00 20.64  ? 106 ASN B OD1    1 
ATOM   4256  N  ND2    . ASN B 2 107 ? -1.907  12.491  -3.753  1.00 21.78  ? 106 ASN B ND2    1 
ATOM   4257  H  H      . ASN B 2 107 ? 0.003   11.792  -0.432  1.00 20.25  ? 106 ASN B H      1 
ATOM   4258  H  HA     . ASN B 2 107 ? 0.900   10.484  -1.808  1.00 21.43  ? 106 ASN B HA     1 
ATOM   4259  H  HB2    . ASN B 2 107 ? 0.501   12.672  -3.602  1.00 20.75  ? 106 ASN B HB2    1 
ATOM   4260  H  HB3    . ASN B 2 107 ? 0.709   11.169  -4.077  1.00 20.75  ? 106 ASN B HB3    1 
ATOM   4261  H  HD21   . ASN B 2 107 ? -2.761  12.396  -3.725  1.00 26.17  ? 106 ASN B HD21   1 
ATOM   4262  H  HD22   . ASN B 2 107 ? -1.564  13.213  -4.069  1.00 26.17  ? 106 ASN B HD22   1 
ATOM   4263  N  N      . THR B 2 108 ? 3.250   11.528  -1.014  1.00 16.17  ? 107 THR B N      1 
ATOM   4264  C  CA     . THR B 2 108 ? 4.705   11.635  -0.987  1.00 18.20  ? 107 THR B CA     1 
ATOM   4265  C  C      . THR B 2 108 ? 5.334   10.566  -0.103  1.00 17.59  ? 107 THR B C      1 
ATOM   4266  O  O      . THR B 2 108 ? 6.346   10.797  0.595   1.00 19.53  ? 107 THR B O      1 
ATOM   4267  C  CB     . THR B 2 108 ? 5.163   13.036  -0.575  1.00 18.32  ? 107 THR B CB     1 
ATOM   4268  O  OG1    . THR B 2 108 ? 4.735   13.339  0.744   1.00 20.67  ? 107 THR B OG1    1 
ATOM   4269  C  CG2    . THR B 2 108 ? 4.586   14.097  -1.503  1.00 18.30  ? 107 THR B CG2    1 
ATOM   4270  H  H      . THR B 2 108 ? 2.893   11.438  -0.236  1.00 19.44  ? 107 THR B H      1 
ATOM   4271  H  HA     . THR B 2 108 ? 5.023   11.475  -1.890  1.00 21.87  ? 107 THR B HA     1 
ATOM   4272  H  HB     . THR B 2 108 ? 6.131   13.055  -0.622  1.00 22.02  ? 107 THR B HB     1 
ATOM   4273  H  HG1    . THR B 2 108 ? 3.896   13.376  0.773   1.00 24.84  ? 107 THR B HG1    1 
ATOM   4274  H  HG21   . THR B 2 108 ? 5.053   14.938  -1.376  1.00 21.99  ? 107 THR B HG21   1 
ATOM   4275  H  HG22   . THR B 2 108 ? 4.684   13.819  -2.427  1.00 21.99  ? 107 THR B HG22   1 
ATOM   4276  H  HG23   . THR B 2 108 ? 3.644   14.229  -1.312  1.00 21.99  ? 107 THR B HG23   1 
ATOM   4277  N  N      . ASN B 2 109 ? 4.786   9.358   -0.151  1.00 17.93  ? 108 ASN B N      1 
ATOM   4278  C  CA     . ASN B 2 109 ? 5.381   8.252   0.587   1.00 17.72  ? 108 ASN B CA     1 
ATOM   4279  C  C      . ASN B 2 109 ? 6.660   7.797   -0.092  1.00 19.54  ? 108 ASN B C      1 
ATOM   4280  O  O      . ASN B 2 109 ? 6.682   7.605   -1.308  1.00 19.91  ? 108 ASN B O      1 
ATOM   4281  C  CB     . ASN B 2 109 ? 4.414   7.098   0.669   1.00 17.74  ? 108 ASN B CB     1 
ATOM   4282  C  CG     . ASN B 2 109 ? 3.129   7.473   1.360   1.00 18.91  ? 108 ASN B CG     1 
ATOM   4283  O  OD1    . ASN B 2 109 ? 3.066   7.618   2.623   1.00 17.73  ? 108 ASN B OD1    1 
ATOM   4284  N  ND2    . ASN B 2 109 ? 2.086   7.688   0.551   1.00 17.23  ? 108 ASN B ND2    1 
ATOM   4285  H  H      . ASN B 2 109 ? 4.080   9.154   -0.598  1.00 21.55  ? 108 ASN B H      1 
ATOM   4286  H  HA     . ASN B 2 109 ? 5.591   8.541   1.489   1.00 21.29  ? 108 ASN B HA     1 
ATOM   4287  H  HB2    . ASN B 2 109 ? 4.197   6.802   -0.229  1.00 21.33  ? 108 ASN B HB2    1 
ATOM   4288  H  HB3    . ASN B 2 109 ? 4.824   6.374   1.167   1.00 21.33  ? 108 ASN B HB3    1 
ATOM   4289  H  HD21   . ASN B 2 109 ? 1.323   7.906   0.882   1.00 20.71  ? 108 ASN B HD21   1 
ATOM   4290  H  HD22   . ASN B 2 109 ? 2.179   7.608   -0.300  1.00 20.71  ? 108 ASN B HD22   1 
ATOM   4291  N  N      . GLY B 2 110 ? 7.681   7.529   0.714   1.00 19.38  ? 109 GLY B N      1 
ATOM   4292  C  CA     . GLY B 2 110 ? 8.935   7.028   0.211   1.00 16.67  ? 109 GLY B CA     1 
ATOM   4293  C  C      . GLY B 2 110 ? 9.325   5.773   0.968   1.00 16.52  ? 109 GLY B C      1 
ATOM   4294  O  O      . GLY B 2 110 ? 8.754   4.703   0.756   1.00 18.36  ? 109 GLY B O      1 
ATOM   4295  H  H      . GLY B 2 110 ? 7.665   7.634   1.567   1.00 23.29  ? 109 GLY B H      1 
ATOM   4296  H  HA2    . GLY B 2 110 ? 8.854   6.816   -0.732  1.00 20.04  ? 109 GLY B HA2    1 
ATOM   4297  H  HA3    . GLY B 2 110 ? 9.629   7.696   0.326   1.00 20.04  ? 109 GLY B HA3    1 
ATOM   4298  N  N      . SER B 2 111 ? 10.286  5.915   1.857   1.00 17.65  ? 110 SER B N      1 
ATOM   4299  C  CA     . SER B 2 111 ? 10.669  4.849   2.772   1.00 17.02  ? 110 SER B CA     1 
ATOM   4300  C  C      . SER B 2 111 ? 10.573  5.252   4.231   1.00 18.92  ? 110 SER B C      1 
ATOM   4301  O  O      . SER B 2 111 ? 10.512  4.366   5.094   1.00 16.50  ? 110 SER B O      1 
ATOM   4302  C  CB     . SER B 2 111 ? 12.109  4.361   2.519   1.00 18.77  ? 110 SER B CB     1 
ATOM   4303  O  OG     . SER B 2 111 ? 13.053  5.422   2.495   1.00 19.10  ? 110 SER B OG     1 
ATOM   4304  H  H      . SER B 2 111 ? 10.745  6.636   1.957   1.00 21.21  ? 110 SER B H      1 
ATOM   4305  H  HA     . SER B 2 111 ? 10.081  4.095   2.607   1.00 20.45  ? 110 SER B HA     1 
ATOM   4306  H  HB2    . SER B 2 111 ? 12.355  3.745   3.227   1.00 22.56  ? 110 SER B HB2    1 
ATOM   4307  H  HB3    . SER B 2 111 ? 12.134  3.907   1.662   1.00 22.56  ? 110 SER B HB3    1 
ATOM   4308  H  HG     . SER B 2 111 ? 13.074  5.804   3.243   1.00 22.95  ? 110 SER B HG     1 
ATOM   4309  N  N      . GLN B 2 112 ? 10.559  6.546   4.538   1.00 17.66  ? 111 GLN B N      1 
ATOM   4310  C  CA     . GLN B 2 112 ? 10.514  6.929   5.958   1.00 16.36  ? 111 GLN B CA     1 
ATOM   4311  C  C      . GLN B 2 112 ? 9.186   6.491   6.562   1.00 15.12  ? 111 GLN B C      1 
ATOM   4312  O  O      . GLN B 2 112 ? 8.127   6.570   5.936   1.00 14.94  ? 111 GLN B O      1 
ATOM   4313  C  CB     . GLN B 2 112 ? 10.678  8.420   6.133   1.00 13.29  ? 111 GLN B CB     1 
ATOM   4314  C  CG     . GLN B 2 112 ? 12.118  8.832   5.939   1.00 15.86  ? 111 GLN B CG     1 
ATOM   4315  C  CD     . GLN B 2 112 ? 12.359  10.264  6.325   1.00 15.77  ? 111 GLN B CD     1 
ATOM   4316  O  OE1    . GLN B 2 112 ? 11.982  10.716  7.425   1.00 16.04  ? 111 GLN B OE1    1 
ATOM   4317  N  NE2    . GLN B 2 112 ? 13.026  10.992  5.439   1.00 17.75  ? 111 GLN B NE2    1 
ATOM   4318  H  H      . GLN B 2 112 ? 10.573  7.196   3.975   1.00 21.23  ? 111 GLN B H      1 
ATOM   4319  H  HA     . GLN B 2 112 ? 11.245  6.500   6.430   1.00 19.67  ? 111 GLN B HA     1 
ATOM   4320  H  HB2    . GLN B 2 112 ? 10.134  8.883   5.476   1.00 15.78  ? 111 GLN B HB2    1 
ATOM   4321  H  HB3    . GLN B 2 112 ? 10.403  8.672   7.028   1.00 15.78  ? 111 GLN B HB3    1 
ATOM   4322  H  HG2    . GLN B 2 112 ? 12.686  8.271   6.490   1.00 19.06  ? 111 GLN B HG2    1 
ATOM   4323  H  HG3    . GLN B 2 112 ? 12.355  8.728   5.004   1.00 19.06  ? 111 GLN B HG3    1 
ATOM   4324  H  HE21   . GLN B 2 112 ? 13.289  10.637  4.701   1.00 21.34  ? 111 GLN B HE21   1 
ATOM   4325  H  HE22   . GLN B 2 112 ? 13.196  11.819  5.602   1.00 21.34  ? 111 GLN B HE22   1 
ATOM   4326  N  N      . PHE B 2 113 ? 9.252   6.140   7.839   1.00 16.56  ? 112 PHE B N      1 
ATOM   4327  C  CA     . PHE B 2 113 ? 8.128   5.580   8.565   1.00 15.36  ? 112 PHE B CA     1 
ATOM   4328  C  C      . PHE B 2 113 ? 8.266   6.034   10.011  1.00 17.73  ? 112 PHE B C      1 
ATOM   4329  O  O      . PHE B 2 113 ? 9.350   6.460   10.445  1.00 15.67  ? 112 PHE B O      1 
ATOM   4330  C  CB     . PHE B 2 113 ? 8.174   4.048   8.491   1.00 16.45  ? 112 PHE B CB     1 
ATOM   4331  C  CG     . PHE B 2 113 ? 9.411   3.496   9.139   1.00 16.85  ? 112 PHE B CG     1 
ATOM   4332  C  CD1    . PHE B 2 113 ? 9.452   3.224   10.494  1.00 16.77  ? 112 PHE B CD1    1 
ATOM   4333  C  CD2    . PHE B 2 113 ? 10.544  3.293   8.393   1.00 17.37  ? 112 PHE B CD2    1 
ATOM   4334  C  CE1    . PHE B 2 113 ? 10.579  2.796   11.081  1.00 17.90  ? 112 PHE B CE1    1 
ATOM   4335  C  CE2    . PHE B 2 113 ? 11.704  2.854   8.994   1.00 19.15  ? 112 PHE B CE2    1 
ATOM   4336  C  CZ     . PHE B 2 113 ? 11.720  2.612   10.336  1.00 18.49  ? 112 PHE B CZ     1 
ATOM   4337  H  H      . PHE B 2 113 ? 9.960   6.220   8.320   1.00 19.91  ? 112 PHE B H      1 
ATOM   4338  H  HA     . PHE B 2 113 ? 7.281   5.890   8.208   1.00 18.46  ? 112 PHE B HA     1 
ATOM   4339  H  HB2    . PHE B 2 113 ? 7.401   3.683   8.949   1.00 19.77  ? 112 PHE B HB2    1 
ATOM   4340  H  HB3    . PHE B 2 113 ? 8.169   3.773   7.561   1.00 19.77  ? 112 PHE B HB3    1 
ATOM   4341  H  HD1    . PHE B 2 113 ? 8.685   3.340   11.008  1.00 20.16  ? 112 PHE B HD1    1 
ATOM   4342  H  HD2    . PHE B 2 113 ? 10.531  3.453   7.477   1.00 20.88  ? 112 PHE B HD2    1 
ATOM   4343  H  HE1    . PHE B 2 113 ? 10.588  2.622   11.994  1.00 21.52  ? 112 PHE B HE1    1 
ATOM   4344  H  HE2    . PHE B 2 113 ? 12.472  2.722   8.487   1.00 23.02  ? 112 PHE B HE2    1 
ATOM   4345  H  HZ     . PHE B 2 113 ? 12.503  2.324   10.748  1.00 22.22  ? 112 PHE B HZ     1 
ATOM   4346  N  N      . PHE B 2 114 ? 7.173   5.932   10.771  1.00 16.40  ? 113 PHE B N      1 
ATOM   4347  C  CA     . PHE B 2 114 ? 7.284   6.127   12.203  1.00 14.44  ? 113 PHE B CA     1 
ATOM   4348  C  C      . PHE B 2 114 ? 6.521   5.049   12.978  1.00 16.31  ? 113 PHE B C      1 
ATOM   4349  O  O      . PHE B 2 114 ? 5.569   4.420   12.497  1.00 15.19  ? 113 PHE B O      1 
ATOM   4350  C  CB     . PHE B 2 114 ? 6.806   7.533   12.633  1.00 15.00  ? 113 PHE B CB     1 
ATOM   4351  C  CG     . PHE B 2 114 ? 5.364   7.845   12.311  1.00 14.71  ? 113 PHE B CG     1 
ATOM   4352  C  CD1    . PHE B 2 114 ? 4.983   8.146   11.024  1.00 15.30  ? 113 PHE B CD1    1 
ATOM   4353  C  CD2    . PHE B 2 114 ? 4.395   7.864   13.305  1.00 14.95  ? 113 PHE B CD2    1 
ATOM   4354  C  CE1    . PHE B 2 114 ? 3.648   8.477   10.736  1.00 14.92  ? 113 PHE B CE1    1 
ATOM   4355  C  CE2    . PHE B 2 114 ? 3.080   8.174   13.038  1.00 16.25  ? 113 PHE B CE2    1 
ATOM   4356  C  CZ     . PHE B 2 114 ? 2.690   8.480   11.755  1.00 16.00  ? 113 PHE B CZ     1 
ATOM   4357  H  H      . PHE B 2 114 ? 6.383   5.755   10.481  1.00 19.71  ? 113 PHE B H      1 
ATOM   4358  H  HA     . PHE B 2 114 ? 8.219   6.032   12.443  1.00 17.32  ? 113 PHE B HA     1 
ATOM   4359  H  HB2    . PHE B 2 114 ? 6.912   7.613   13.594  1.00 18.03  ? 113 PHE B HB2    1 
ATOM   4360  H  HB3    . PHE B 2 114 ? 7.354   8.194   12.182  1.00 18.03  ? 113 PHE B HB3    1 
ATOM   4361  H  HD1    . PHE B 2 114 ? 5.613   8.129   10.340  1.00 18.39  ? 113 PHE B HD1    1 
ATOM   4362  H  HD2    . PHE B 2 114 ? 4.642   7.661   14.178  1.00 17.78  ? 113 PHE B HD2    1 
ATOM   4363  H  HE1    . PHE B 2 114 ? 3.402   8.695   9.867   1.00 17.93  ? 113 PHE B HE1    1 
ATOM   4364  H  HE2    . PHE B 2 114 ? 2.455   8.176   13.727  1.00 19.54  ? 113 PHE B HE2    1 
ATOM   4365  H  HZ     . PHE B 2 114 ? 1.802   8.686   11.568  1.00 19.23  ? 113 PHE B HZ     1 
ATOM   4366  N  N      . ILE B 2 115 ? 6.949   4.854   14.228  1.00 15.09  ? 114 ILE B N      1 
ATOM   4367  C  CA     . ILE B 2 115 ? 6.325   3.914   15.146  1.00 15.60  ? 114 ILE B CA     1 
ATOM   4368  C  C      . ILE B 2 115 ? 5.795   4.761   16.297  1.00 15.77  ? 114 ILE B C      1 
ATOM   4369  O  O      . ILE B 2 115 ? 6.561   5.495   16.942  1.00 16.37  ? 114 ILE B O      1 
ATOM   4370  C  CB     . ILE B 2 115 ? 7.291   2.844   15.671  1.00 16.22  ? 114 ILE B CB     1 
ATOM   4371  C  CG1    . ILE B 2 115 ? 8.032   2.148   14.547  1.00 21.45  ? 114 ILE B CG1    1 
ATOM   4372  C  CG2    . ILE B 2 115 ? 6.547   1.848   16.516  1.00 16.66  ? 114 ILE B CG2    1 
ATOM   4373  C  CD1    . ILE B 2 115 ? 9.294   1.424   15.052  1.00 18.81  ? 114 ILE B CD1    1 
ATOM   4374  H  H      . ILE B 2 115 ? 7.619   5.269   14.571  1.00 17.93  ? 114 ILE B H      1 
ATOM   4375  H  HA     . ILE B 2 115 ? 5.604   3.447   14.697  1.00 18.55  ? 114 ILE B HA     1 
ATOM   4376  H  HB     . ILE B 2 115 ? 7.957   3.291   16.217  1.00 19.49  ? 114 ILE B HB     1 
ATOM   4377  H  HG12   . ILE B 2 115 ? 7.447   1.490   14.140  1.00 25.77  ? 114 ILE B HG12   1 
ATOM   4378  H  HG13   . ILE B 2 115 ? 8.302   2.806   13.888  1.00 25.77  ? 114 ILE B HG13   1 
ATOM   4379  H  HG21   . ILE B 2 115 ? 7.158   1.145   16.788  1.00 20.02  ? 114 ILE B HG21   1 
ATOM   4380  H  HG22   . ILE B 2 115 ? 6.194   2.299   17.299  1.00 20.02  ? 114 ILE B HG22   1 
ATOM   4381  H  HG23   . ILE B 2 115 ? 5.821   1.472   15.995  1.00 20.02  ? 114 ILE B HG23   1 
ATOM   4382  H  HD11   . ILE B 2 115 ? 9.807   1.115   14.289  1.00 22.61  ? 114 ILE B HD11   1 
ATOM   4383  H  HD12   . ILE B 2 115 ? 9.824   2.043   15.577  1.00 22.61  ? 114 ILE B HD12   1 
ATOM   4384  H  HD13   . ILE B 2 115 ? 9.028   0.669   15.599  1.00 22.61  ? 114 ILE B HD13   1 
ATOM   4385  N  N      . CYS B 2 116 ? 4.494   4.760   16.480  1.00 16.11  ? 115 CYS B N      1 
ATOM   4386  C  CA     . CYS B 2 116 ? 3.891   5.523   17.570  1.00 17.31  ? 115 CYS B CA     1 
ATOM   4387  C  C      . CYS B 2 116 ? 4.232   4.941   18.943  1.00 18.20  ? 115 CYS B C      1 
ATOM   4388  O  O      . CYS B 2 116 ? 4.246   3.719   19.150  1.00 17.17  ? 115 CYS B O      1 
ATOM   4389  C  CB     . CYS B 2 116 ? 2.370   5.528   17.452  1.00 16.80  ? 115 CYS B CB     1 
ATOM   4390  S  SG     . CYS B 2 116 ? 1.789   6.308   15.910  1.00 20.48  ? 115 CYS B SG     1 
ATOM   4391  H  H      . CYS B 2 116 ? 3.931   4.329   15.993  1.00 19.16  ? 115 CYS B H      1 
ATOM   4392  H  HA     . CYS B 2 116 ? 4.240   6.425   17.507  1.00 20.80  ? 115 CYS B HA     1 
ATOM   4393  H  HB2    . CYS B 2 116 ? 2.048   4.613   17.465  1.00 20.11  ? 115 CYS B HB2    1 
ATOM   4394  H  HB3    . CYS B 2 116 ? 1.996   6.022   18.198  1.00 20.11  ? 115 CYS B HB3    1 
ATOM   4395  H  HG     . CYS B 2 116 ? 2.171   7.445   15.880  1.00 24.60  ? 115 CYS B HG     1 
ATOM   4396  N  N      . THR B 2 117 ? 4.442   5.834   19.910  1.00 16.94  ? 116 THR B N      1 
ATOM   4397  C  CA     . THR B 2 117 ? 4.565   5.442   21.305  1.00 18.64  ? 116 THR B CA     1 
ATOM   4398  C  C      . THR B 2 117 ? 3.412   5.976   22.115  1.00 20.94  ? 116 THR B C      1 
ATOM   4399  O  O      . THR B 2 117 ? 3.410   5.854   23.353  1.00 20.88  ? 116 THR B O      1 
ATOM   4400  C  CB     . THR B 2 117 ? 5.881   5.926   21.900  1.00 20.31  ? 116 THR B CB     1 
ATOM   4401  O  OG1    . THR B 2 117 ? 5.985   7.338   21.722  1.00 19.33  ? 116 THR B OG1    1 
ATOM   4402  C  CG2    . THR B 2 117 ? 7.059   5.248   21.151  1.00 20.01  ? 116 THR B CG2    1 
ATOM   4403  H  H      . THR B 2 117 ? 4.518   6.680   19.777  1.00 20.16  ? 116 THR B H      1 
ATOM   4404  H  HA     . THR B 2 117 ? 4.573   4.474   21.358  1.00 22.40  ? 116 THR B HA     1 
ATOM   4405  H  HB     . THR B 2 117 ? 5.925   5.709   22.845  1.00 24.40  ? 116 THR B HB     1 
ATOM   4406  H  HG1    . THR B 2 117 ? 6.699   7.619   22.064  1.00 23.23  ? 116 THR B HG1    1 
ATOM   4407  H  HG21   . THR B 2 117 ? 7.903   5.530   21.536  1.00 24.04  ? 116 THR B HG21   1 
ATOM   4408  H  HG22   . THR B 2 117 ? 6.986   4.283   21.223  1.00 24.04  ? 116 THR B HG22   1 
ATOM   4409  H  HG23   . THR B 2 117 ? 7.042   5.495   20.213  1.00 24.04  ? 116 THR B HG23   1 
ATOM   4410  N  N      . ALA B 2 118 ? 2.404   6.501   21.435  1.00 17.97  ? 117 ALA B N      1 
ATOM   4411  C  CA     . ALA B 2 118 ? 1.175   6.992   22.042  1.00 20.18  ? 117 ALA B CA     1 
ATOM   4412  C  C      . ALA B 2 118 ? 0.150   7.099   20.915  1.00 19.54  ? 117 ALA B C      1 
ATOM   4413  O  O      . ALA B 2 118 ? 0.497   7.046   19.740  1.00 21.55  ? 117 ALA B O      1 
ATOM   4414  C  CB     . ALA B 2 118 ? 1.395   8.358   22.681  1.00 21.52  ? 117 ALA B CB     1 
ATOM   4415  H  H      . ALA B 2 118 ? 2.406   6.588   20.579  1.00 21.46  ? 117 ALA B H      1 
ATOM   4416  H  HA     . ALA B 2 118 ? 0.860   6.378   22.724  1.00 24.25  ? 117 ALA B HA     1 
ATOM   4417  H  HB1    . ALA B 2 118 ? 0.558   8.668   23.059  1.00 25.86  ? 117 ALA B HB1    1 
ATOM   4418  H  HB2    . ALA B 2 118 ? 2.063   8.276   23.379  1.00 25.86  ? 117 ALA B HB2    1 
ATOM   4419  H  HB3    . ALA B 2 118 ? 1.701   8.978   22.001  1.00 25.86  ? 117 ALA B HB3    1 
ATOM   4420  N  N      . LYS B 2 119 ? -1.114  7.301   21.286  1.00 21.27  ? 118 LYS B N      1 
ATOM   4421  C  CA     . LYS B 2 119 ? -2.165  7.566   20.304  1.00 20.76  ? 118 LYS B CA     1 
ATOM   4422  C  C      . LYS B 2 119 ? -1.923  8.934   19.683  1.00 21.61  ? 118 LYS B C      1 
ATOM   4423  O  O      . LYS B 2 119 ? -1.742  9.932   20.393  1.00 22.46  ? 118 LYS B O      1 
ATOM   4424  C  CB     . LYS B 2 119 ? -3.534  7.506   20.977  1.00 21.55  ? 118 LYS B CB     1 
ATOM   4425  C  CG     . LYS B 2 119 ? -4.747  7.816   20.076  1.00 26.39  ? 118 LYS B CG     1 
ATOM   4426  C  CD     . LYS B 2 119 ? -6.020  7.833   20.959  1.00 30.35  ? 118 LYS B CD     1 
ATOM   4427  C  CE     . LYS B 2 119 ? -7.304  8.008   20.162  1.00 38.79  ? 118 LYS B CE     1 
ATOM   4428  N  NZ     . LYS B 2 119 ? -8.472  7.823   21.081  1.00 41.21  ? 118 LYS B NZ     1 
ATOM   4429  H  H      . LYS B 2 119 ? -1.389  7.291   22.100  1.00 25.56  ? 118 LYS B H      1 
ATOM   4430  H  HA     . LYS B 2 119 ? -2.156  6.899   19.600  1.00 24.94  ? 118 LYS B HA     1 
ATOM   4431  H  HB2    . LYS B 2 119 ? -3.659  6.610   21.328  1.00 25.89  ? 118 LYS B HB2    1 
ATOM   4432  H  HB3    . LYS B 2 119 ? -3.543  8.150   21.702  1.00 25.89  ? 118 LYS B HB3    1 
ATOM   4433  H  HG2    . LYS B 2 119 ? -4.638  8.685   19.659  1.00 31.71  ? 118 LYS B HG2    1 
ATOM   4434  H  HG3    . LYS B 2 119 ? -4.840  7.131   19.396  1.00 31.71  ? 118 LYS B HG3    1 
ATOM   4435  H  HD2    . LYS B 2 119 ? -6.081  6.992   21.439  1.00 36.45  ? 118 LYS B HD2    1 
ATOM   4436  H  HD3    . LYS B 2 119 ? -5.958  8.569   21.587  1.00 36.45  ? 118 LYS B HD3    1 
ATOM   4437  H  HE2    . LYS B 2 119 ? -7.339  8.899   19.781  1.00 46.58  ? 118 LYS B HE2    1 
ATOM   4438  H  HE3    . LYS B 2 119 ? -7.349  7.344   19.456  1.00 46.58  ? 118 LYS B HE3    1 
ATOM   4439  H  HZ1    . LYS B 2 119 ? -9.233  7.912   20.628  1.00 49.49  ? 118 LYS B HZ1    1 
ATOM   4440  H  HZ2    . LYS B 2 119 ? -8.446  7.012   21.447  1.00 49.49  ? 118 LYS B HZ2    1 
ATOM   4441  H  HZ3    . LYS B 2 119 ? -8.449  8.433   21.728  1.00 49.49  ? 118 LYS B HZ3    1 
ATOM   4442  N  N      . THR B 2 120 ? -1.902  8.992   18.336  1.00 19.51  ? 119 THR B N      1 
ATOM   4443  C  CA     . THR B 2 120 ? -1.642  10.225  17.620  1.00 18.05  ? 119 THR B CA     1 
ATOM   4444  C  C      . THR B 2 120 ? -2.790  10.461  16.610  1.00 21.86  ? 119 THR B C      1 
ATOM   4445  O  O      . THR B 2 120 ? -2.600  10.397  15.385  1.00 20.57  ? 119 THR B O      1 
ATOM   4446  C  CB     . THR B 2 120 ? -0.283  10.199  16.910  1.00 18.72  ? 119 THR B CB     1 
ATOM   4447  O  OG1    . THR B 2 120 ? -0.239  9.126   15.973  1.00 22.06  ? 119 THR B OG1    1 
ATOM   4448  C  CG2    . THR B 2 120 ? 0.877   10.008  17.889  1.00 20.75  ? 119 THR B CG2    1 
ATOM   4449  H  H      . THR B 2 120 ? -2.038  8.315   17.823  1.00 23.45  ? 119 THR B H      1 
ATOM   4450  H  HA     . THR B 2 120 ? -1.636  10.952  18.262  1.00 21.69  ? 119 THR B HA     1 
ATOM   4451  H  HB     . THR B 2 120 ? -0.173  11.052  16.462  1.00 22.50  ? 119 THR B HB     1 
ATOM   4452  H  HG1    . THR B 2 120 ? -0.820  9.241   15.378  1.00 26.51  ? 119 THR B HG1    1 
ATOM   4453  H  HG21   . THR B 2 120 ? 1.721   10.034  17.412  1.00 24.94  ? 119 THR B HG21   1 
ATOM   4454  H  HG22   . THR B 2 120 ? 0.869   10.714  18.554  1.00 24.94  ? 119 THR B HG22   1 
ATOM   4455  H  HG23   . THR B 2 120 ? 0.795   9.152   18.338  1.00 24.94  ? 119 THR B HG23   1 
ATOM   4456  N  N      . GLU B 2 121 ? -3.968  10.767  17.150  1.00 23.74  ? 120 GLU B N      1 
ATOM   4457  C  CA     . GLU B 2 121 ? -5.186  10.702  16.348  1.00 24.80  ? 120 GLU B CA     1 
ATOM   4458  C  C      . GLU B 2 121 ? -5.233  11.800  15.302  1.00 22.52  ? 120 GLU B C      1 
ATOM   4459  O  O      . GLU B 2 121 ? -5.877  11.628  14.265  1.00 22.69  ? 120 GLU B O      1 
ATOM   4460  C  CB     . GLU B 2 121 ? -6.404  10.764  17.273  1.00 24.88  ? 120 GLU B CB     1 
ATOM   4461  C  CG     . GLU B 2 121 ? -6.592  12.117  17.991  1.00 33.61  ? 120 GLU B CG     1 
ATOM   4462  C  CD     . GLU B 2 121 ? -5.680  12.333  19.239  1.00 41.35  ? 120 GLU B CD     1 
ATOM   4463  O  OE1    . GLU B 2 121 ? -5.770  13.453  19.881  1.00 43.58  ? 120 GLU B OE1    1 
ATOM   4464  O  OE2    . GLU B 2 121 ? -4.899  11.418  19.612  1.00 34.05  ? 120 GLU B OE2    1 
ATOM   4465  H  H      . GLU B 2 121 ? -4.088  11.012  17.966  1.00 28.52  ? 120 GLU B H      1 
ATOM   4466  H  HA     . GLU B 2 121 ? -5.214  9.858   15.872  1.00 29.80  ? 120 GLU B HA     1 
ATOM   4467  H  HB2    . GLU B 2 121 ? -7.201  10.598  16.746  1.00 29.89  ? 120 GLU B HB2    1 
ATOM   4468  H  HB3    . GLU B 2 121 ? -6.310  10.080  17.955  1.00 29.89  ? 120 GLU B HB3    1 
ATOM   4469  H  HG2    . GLU B 2 121 ? -6.396  12.828  17.361  1.00 40.37  ? 120 GLU B HG2    1 
ATOM   4470  H  HG3    . GLU B 2 121 ? -7.513  12.182  18.289  1.00 40.37  ? 120 GLU B HG3    1 
ATOM   4471  N  N      . TRP B 2 122 ? -4.550  12.921  15.536  1.00 20.97  ? 121 TRP B N      1 
ATOM   4472  C  CA     . TRP B 2 122 ? -4.579  14.034  14.602  1.00 25.31  ? 121 TRP B CA     1 
ATOM   4473  C  C      . TRP B 2 122 ? -3.807  13.734  13.326  1.00 24.52  ? 121 TRP B C      1 
ATOM   4474  O  O      . TRP B 2 122 ? -3.890  14.504  12.369  1.00 26.38  ? 121 TRP B O      1 
ATOM   4475  C  CB     . TRP B 2 122 ? -4.021  15.282  15.257  1.00 28.80  ? 121 TRP B CB     1 
ATOM   4476  C  CG     . TRP B 2 122 ? -2.592  15.192  15.571  1.00 27.25  ? 121 TRP B CG     1 
ATOM   4477  C  CD1    . TRP B 2 122 ? -1.559  15.637  14.791  1.00 22.91  ? 121 TRP B CD1    1 
ATOM   4478  C  CD2    . TRP B 2 122 ? -1.996  14.645  16.750  1.00 24.75  ? 121 TRP B CD2    1 
ATOM   4479  N  NE1    . TRP B 2 122 ? -0.369  15.389  15.404  1.00 28.75  ? 121 TRP B NE1    1 
ATOM   4480  C  CE2    . TRP B 2 122 ? -0.594  14.770  16.599  1.00 25.13  ? 121 TRP B CE2    1 
ATOM   4481  C  CE3    . TRP B 2 122 ? -2.502  14.051  17.906  1.00 28.19  ? 121 TRP B CE3    1 
ATOM   4482  C  CZ2    . TRP B 2 122 ? 0.298   14.349  17.574  1.00 26.42  ? 121 TRP B CZ2    1 
ATOM   4483  C  CZ3    . TRP B 2 122 ? -1.619  13.620  18.876  1.00 29.19  ? 121 TRP B CZ3    1 
ATOM   4484  C  CH2    . TRP B 2 122 ? -0.232  13.774  18.708  1.00 26.50  ? 121 TRP B CH2    1 
ATOM   4485  H  H      . TRP B 2 122 ? -4.062  13.058  16.230  1.00 25.20  ? 121 TRP B H      1 
ATOM   4486  H  HA     . TRP B 2 122 ? -5.501  14.218  14.363  1.00 30.40  ? 121 TRP B HA     1 
ATOM   4487  H  HB2    . TRP B 2 122 ? -4.145  16.033  14.656  1.00 34.59  ? 121 TRP B HB2    1 
ATOM   4488  H  HB3    . TRP B 2 122 ? -4.497  15.439  16.088  1.00 34.59  ? 121 TRP B HB3    1 
ATOM   4489  H  HD1    . TRP B 2 122 ? -1.656  16.048  13.962  1.00 27.53  ? 121 TRP B HD1    1 
ATOM   4490  H  HE1    . TRP B 2 122 ? 0.405   15.591  15.087  1.00 34.53  ? 121 TRP B HE1    1 
ATOM   4491  H  HE3    . TRP B 2 122 ? -3.419  13.947  18.021  1.00 33.86  ? 121 TRP B HE3    1 
ATOM   4492  H  HZ2    . TRP B 2 122 ? 1.216   14.451  17.466  1.00 31.73  ? 121 TRP B HZ2    1 
ATOM   4493  H  HZ3    . TRP B 2 122 ? -1.946  13.223  19.650  1.00 35.07  ? 121 TRP B HZ3    1 
ATOM   4494  H  HH2    . TRP B 2 122 ? 0.342   13.480  19.379  1.00 31.83  ? 121 TRP B HH2    1 
ATOM   4495  N  N      . LEU B 2 123 ? -3.081  12.639  13.286  1.00 20.79  ? 122 LEU B N      1 
ATOM   4496  C  CA     . LEU B 2 123 ? -2.396  12.183  12.074  1.00 20.41  ? 122 LEU B CA     1 
ATOM   4497  C  C      . LEU B 2 123 ? -3.315  11.323  11.215  1.00 19.71  ? 122 LEU B C      1 
ATOM   4498  O  O      . LEU B 2 123 ? -2.980  11.033  10.069  1.00 19.94  ? 122 LEU B O      1 
ATOM   4499  C  CB     . LEU B 2 123 ? -1.113  11.448  12.482  1.00 18.08  ? 122 LEU B CB     1 
ATOM   4500  C  CG     . LEU B 2 123 ? -0.110  12.357  13.220  1.00 19.45  ? 122 LEU B CG     1 
ATOM   4501  C  CD1    . LEU B 2 123 ? 1.099   11.518  13.545  1.00 19.58  ? 122 LEU B CD1    1 
ATOM   4502  C  CD2    . LEU B 2 123 ? 0.270   13.602  12.434  1.00 21.49  ? 122 LEU B CD2    1 
ATOM   4503  H  H      . LEU B 2 123 ? -2.959  12.121  13.962  1.00 24.98  ? 122 LEU B H      1 
ATOM   4504  H  HA     . LEU B 2 123 ? -2.113  12.923  11.515  1.00 24.53  ? 122 LEU B HA     1 
ATOM   4505  H  HB2    . LEU B 2 123 ? -1.345  10.715  13.073  1.00 21.73  ? 122 LEU B HB2    1 
ATOM   4506  H  HB3    . LEU B 2 123 ? -0.679  11.107  11.685  1.00 21.73  ? 122 LEU B HB3    1 
ATOM   4507  H  HG     . LEU B 2 123 ? -0.518  12.701  14.030  1.00 23.37  ? 122 LEU B HG     1 
ATOM   4508  H  HD11   . LEU B 2 123 ? 1.749   12.068  14.010  1.00 23.53  ? 122 LEU B HD11   1 
ATOM   4509  H  HD12   . LEU B 2 123 ? 0.827   10.778  14.109  1.00 23.53  ? 122 LEU B HD12   1 
ATOM   4510  H  HD13   . LEU B 2 123 ? 1.481   11.181  12.719  1.00 23.53  ? 122 LEU B HD13   1 
ATOM   4511  H  HD21   . LEU B 2 123 ? 1.038   14.019  12.856  1.00 25.82  ? 122 LEU B HD21   1 
ATOM   4512  H  HD22   . LEU B 2 123 ? 0.490   13.347  11.524  1.00 25.82  ? 122 LEU B HD22   1 
ATOM   4513  H  HD23   . LEU B 2 123 ? -0.481  14.216  12.433  1.00 25.82  ? 122 LEU B HD23   1 
ATOM   4514  N  N      . ASP B 2 124 ? -4.486  10.933  11.730  1.00 23.06  ? 123 ASP B N      1 
ATOM   4515  C  CA     . ASP B 2 124 ? -5.421  10.142  10.941  1.00 21.04  ? 123 ASP B CA     1 
ATOM   4516  C  C      . ASP B 2 124 ? -5.835  10.888  9.682   1.00 22.90  ? 123 ASP B C      1 
ATOM   4517  O  O      . ASP B 2 124 ? -6.133  12.092  9.712   1.00 20.86  ? 123 ASP B O      1 
ATOM   4518  C  CB     . ASP B 2 124 ? -6.676  9.824   11.755  1.00 22.28  ? 123 ASP B CB     1 
ATOM   4519  C  CG     . ASP B 2 124 ? -6.394  8.886   12.926  1.00 24.45  ? 123 ASP B CG     1 
ATOM   4520  O  OD1    . ASP B 2 124 ? -5.276  8.364   13.021  1.00 21.49  ? 123 ASP B OD1    1 
ATOM   4521  O  OD2    . ASP B 2 124 ? -7.319  8.660   13.721  1.00 23.57  ? 123 ASP B OD2    1 
ATOM   4522  H  H      . ASP B 2 124 ? -4.756  11.114  12.527  1.00 27.71  ? 123 ASP B H      1 
ATOM   4523  H  HA     . ASP B 2 124 ? -4.985  9.313   10.692  1.00 25.28  ? 123 ASP B HA     1 
ATOM   4524  H  HB2    . ASP B 2 124 ? -7.039  10.650  12.113  1.00 26.78  ? 123 ASP B HB2    1 
ATOM   4525  H  HB3    . ASP B 2 124 ? -7.328  9.397   11.178  1.00 26.78  ? 123 ASP B HB3    1 
ATOM   4526  N  N      . GLY B 2 125 ? -5.865  10.155  8.567   1.00 22.27  ? 124 GLY B N      1 
ATOM   4527  C  CA     . GLY B 2 125 ? -6.180  10.732  7.274   1.00 25.32  ? 124 GLY B CA     1 
ATOM   4528  C  C      . GLY B 2 125 ? -5.068  11.522  6.638   1.00 23.38  ? 124 GLY B C      1 
ATOM   4529  O  O      . GLY B 2 125 ? -5.231  11.992  5.503   1.00 22.95  ? 124 GLY B O      1 
ATOM   4530  H  H      . GLY B 2 125 ? -5.704  9.311   8.540   1.00 26.76  ? 124 GLY B H      1 
ATOM   4531  H  HA2    . GLY B 2 125 ? -6.417  10.015  6.665   1.00 30.42  ? 124 GLY B HA2    1 
ATOM   4532  H  HA3    . GLY B 2 125 ? -6.941  11.324  7.376   1.00 30.42  ? 124 GLY B HA3    1 
ATOM   4533  N  N      . LYS B 2 126 ? -3.923  11.641  7.291   1.00 21.24  ? 125 LYS B N      1 
ATOM   4534  C  CA     . LYS B 2 126 ? -2.759  12.302  6.739   1.00 21.30  ? 125 LYS B CA     1 
ATOM   4535  C  C      . LYS B 2 126 ? -1.582  11.364  6.532   1.00 20.61  ? 125 LYS B C      1 
ATOM   4536  O  O      . LYS B 2 126 ? -0.804  11.580  5.617   1.00 19.83  ? 125 LYS B O      1 
ATOM   4537  C  CB     . LYS B 2 126 ? -2.360  13.477  7.639   1.00 23.69  ? 125 LYS B CB     1 
ATOM   4538  C  CG     . LYS B 2 126 ? -3.325  14.701  7.529   1.00 33.64  ? 125 LYS B CG     1 
ATOM   4539  C  CD     . LYS B 2 126 ? -4.255  14.794  8.737   1.00 34.21  ? 125 LYS B CD     1 
ATOM   4540  C  CE     . LYS B 2 126 ? -5.249  15.991  8.705   1.00 43.52  ? 125 LYS B CE     1 
ATOM   4541  N  NZ     . LYS B 2 126 ? -6.550  15.771  7.971   1.00 44.35  ? 125 LYS B NZ     1 
ATOM   4542  H  H      . LYS B 2 126 ? -3.793  11.334  8.084   1.00 25.52  ? 125 LYS B H      1 
ATOM   4543  H  HA     . LYS B 2 126 ? -2.969  12.675  5.869   1.00 25.60  ? 125 LYS B HA     1 
ATOM   4544  H  HB2    . LYS B 2 126 ? -2.362  13.179  8.562   1.00 28.47  ? 125 LYS B HB2    1 
ATOM   4545  H  HB3    . LYS B 2 126 ? -1.472  13.775  7.388   1.00 28.47  ? 125 LYS B HB3    1 
ATOM   4546  H  HG2    . LYS B 2 126 ? -2.804  15.518  7.483   1.00 40.41  ? 125 LYS B HG2    1 
ATOM   4547  H  HG3    . LYS B 2 126 ? -3.870  14.610  6.732   1.00 40.41  ? 125 LYS B HG3    1 
ATOM   4548  H  HD2    . LYS B 2 126 ? -4.781  13.980  8.784   1.00 41.09  ? 125 LYS B HD2    1 
ATOM   4549  H  HD3    . LYS B 2 126 ? -3.714  14.886  9.536   1.00 41.09  ? 125 LYS B HD3    1 
ATOM   4550  H  HE2    . LYS B 2 126 ? -5.476  16.219  9.620   1.00 52.26  ? 125 LYS B HE2    1 
ATOM   4551  H  HE3    . LYS B 2 126 ? -4.805  16.740  8.277   1.00 52.26  ? 125 LYS B HE3    1 
ATOM   4552  H  HZ1    . LYS B 2 126 ? -7.052  16.505  8.015   1.00 53.25  ? 125 LYS B HZ1    1 
ATOM   4553  H  HZ2    . LYS B 2 126 ? -6.389  15.582  7.116   1.00 53.25  ? 125 LYS B HZ2    1 
ATOM   4554  H  HZ3    . LYS B 2 126 ? -6.996  15.094  8.337   1.00 53.25  ? 125 LYS B HZ3    1 
ATOM   4555  N  N      . HIS B 2 127 ? -1.455  10.305  7.336   1.00 16.36  ? 126 HIS B N      1 
ATOM   4556  C  CA     . HIS B 2 127 ? -0.378  9.343   7.236   1.00 15.97  ? 126 HIS B CA     1 
ATOM   4557  C  C      . HIS B 2 127 ? -1.020  7.982   7.062   1.00 17.94  ? 126 HIS B C      1 
ATOM   4558  O  O      . HIS B 2 127 ? -1.969  7.653   7.786   1.00 19.43  ? 126 HIS B O      1 
ATOM   4559  C  CB     . HIS B 2 127 ? 0.536   9.423   8.510   1.00 17.03  ? 126 HIS B CB     1 
ATOM   4560  C  CG     . HIS B 2 127 ? 1.223   10.763  8.615   1.00 17.17  ? 126 HIS B CG     1 
ATOM   4561  N  ND1    . HIS B 2 127 ? 2.503   10.980  8.149   1.00 16.10  ? 126 HIS B ND1    1 
ATOM   4562  C  CD2    . HIS B 2 127 ? 0.781   11.967  9.072   1.00 15.66  ? 126 HIS B CD2    1 
ATOM   4563  C  CE1    . HIS B 2 127 ? 2.803   12.260  8.277   1.00 15.71  ? 126 HIS B CE1    1 
ATOM   4564  N  NE2    . HIS B 2 127 ? 1.803   12.870  8.891   1.00 16.31  ? 126 HIS B NE2    1 
ATOM   4565  H  H      . HIS B 2 127 ? -2.007  10.124  7.969   1.00 19.46  ? 126 HIS B H      1 
ATOM   4566  H  HA     . HIS B 2 127 ? 0.203   9.499   6.475   1.00 18.99  ? 126 HIS B HA     1 
ATOM   4567  H  HB2    . HIS B 2 127 ? -0.008  9.296   9.303   1.00 20.47  ? 126 HIS B HB2    1 
ATOM   4568  H  HB3    . HIS B 2 127 ? 1.216   8.734   8.461   1.00 20.47  ? 126 HIS B HB3    1 
ATOM   4569  H  HD1    . HIS B 2 127 ? 3.024   10.376  7.826   1.00 19.36  ? 126 HIS B HD1    1 
ATOM   4570  H  HD2    . HIS B 2 127 ? -0.055  12.145  9.438   1.00 18.82  ? 126 HIS B HD2    1 
ATOM   4571  H  HE1    . HIS B 2 127 ? 3.587   12.665  7.983   1.00 18.88  ? 126 HIS B HE1    1 
ATOM   4572  H  HE2    . HIS B 2 127 ? 1.793   13.694  9.137   1.00 19.61  ? 126 HIS B HE2    1 
ATOM   4573  N  N      . VAL B 2 128 ? -0.483  7.202   6.118   1.00 17.29  ? 127 VAL B N      1 
ATOM   4574  C  CA     . VAL B 2 128 ? -0.980  5.849   5.869   1.00 18.33  ? 127 VAL B CA     1 
ATOM   4575  C  C      . VAL B 2 128 ? -0.442  4.899   6.937   1.00 16.52  ? 127 VAL B C      1 
ATOM   4576  O  O      . VAL B 2 128 ? 0.742   4.576   6.966   1.00 17.37  ? 127 VAL B O      1 
ATOM   4577  C  CB     . VAL B 2 128 ? -0.610  5.354   4.468   1.00 16.78  ? 127 VAL B CB     1 
ATOM   4578  C  CG1    . VAL B 2 128 ? -1.116  3.913   4.298   1.00 18.82  ? 127 VAL B CG1    1 
ATOM   4579  C  CG2    . VAL B 2 128 ? -1.232  6.236   3.431   1.00 18.08  ? 127 VAL B CG2    1 
ATOM   4580  H  H      . VAL B 2 128 ? 0.169   7.435   5.610   1.00 20.79  ? 127 VAL B H      1 
ATOM   4581  H  HA     . VAL B 2 128 ? -1.946  5.871   5.951   1.00 22.03  ? 127 VAL B HA     1 
ATOM   4582  H  HB     . VAL B 2 128 ? 0.353   5.376   4.353   1.00 20.18  ? 127 VAL B HB     1 
ATOM   4583  H  HG11   . VAL B 2 128 ? -1.068  3.670   3.360   1.00 22.61  ? 127 VAL B HG11   1 
ATOM   4584  H  HG12   . VAL B 2 128 ? -0.559  3.318   4.824   1.00 22.61  ? 127 VAL B HG12   1 
ATOM   4585  H  HG13   . VAL B 2 128 ? -2.035  3.863   4.606   1.00 22.61  ? 127 VAL B HG13   1 
ATOM   4586  H  HG21   . VAL B 2 128 ? -0.994  5.905   2.551   1.00 21.73  ? 127 VAL B HG21   1 
ATOM   4587  H  HG22   . VAL B 2 128 ? -2.196  6.221   3.541   1.00 21.73  ? 127 VAL B HG22   1 
ATOM   4588  H  HG23   . VAL B 2 128 ? -0.900  7.140   3.545   1.00 21.73  ? 127 VAL B HG23   1 
ATOM   4589  N  N      . VAL B 2 129 ? -1.344  4.375   7.743   1.00 18.18  ? 128 VAL B N      1 
ATOM   4590  C  CA     . VAL B 2 129 ? -1.037  3.312   8.699   1.00 20.25  ? 128 VAL B CA     1 
ATOM   4591  C  C      . VAL B 2 129 ? -1.055  1.982   7.964   1.00 19.91  ? 128 VAL B C      1 
ATOM   4592  O  O      . VAL B 2 129 ? -2.026  1.675   7.268   1.00 20.34  ? 128 VAL B O      1 
ATOM   4593  C  CB     . VAL B 2 129 ? -2.074  3.321   9.833   1.00 19.07  ? 128 VAL B CB     1 
ATOM   4594  C  CG1    . VAL B 2 129 ? -1.883  2.120   10.716  1.00 18.20  ? 128 VAL B CG1    1 
ATOM   4595  C  CG2    . VAL B 2 129 ? -1.997  4.640   10.617  1.00 21.01  ? 128 VAL B CG2    1 
ATOM   4596  H  H      . VAL B 2 129 ? -2.168  4.621   7.763   1.00 21.84  ? 128 VAL B H      1 
ATOM   4597  H  HA     . VAL B 2 129 ? -0.153  3.447   9.074   1.00 24.33  ? 128 VAL B HA     1 
ATOM   4598  H  HB     . VAL B 2 129 ? -2.969  3.265   9.463   1.00 22.92  ? 128 VAL B HB     1 
ATOM   4599  H  HG11   . VAL B 2 129 ? -2.334  2.275   11.561  1.00 21.87  ? 128 VAL B HG11   1 
ATOM   4600  H  HG12   . VAL B 2 129 ? -2.262  1.342   10.277  1.00 21.87  ? 128 VAL B HG12   1 
ATOM   4601  H  HG13   . VAL B 2 129 ? -0.935  1.987   10.866  1.00 21.87  ? 128 VAL B HG13   1 
ATOM   4602  H  HG21   . VAL B 2 129 ? -2.622  4.604   11.358  1.00 25.25  ? 128 VAL B HG21   1 
ATOM   4603  H  HG22   . VAL B 2 129 ? -1.094  4.757   10.950  1.00 25.25  ? 128 VAL B HG22   1 
ATOM   4604  H  HG23   . VAL B 2 129 ? -2.228  5.373   10.025  1.00 25.25  ? 128 VAL B HG23   1 
ATOM   4605  N  N      . PHE B 2 130 ? -0.017  1.169   8.158   1.00 18.02  ? 129 PHE B N      1 
ATOM   4606  C  CA     . PHE B 2 130 ? 0.113   -0.074  7.409   1.00 19.15  ? 129 PHE B CA     1 
ATOM   4607  C  C      . PHE B 2 130 ? 0.658   -1.231  8.243   1.00 20.05  ? 129 PHE B C      1 
ATOM   4608  O  O      . PHE B 2 130 ? 0.911   -2.304  7.683   1.00 21.04  ? 129 PHE B O      1 
ATOM   4609  C  CB     . PHE B 2 130 ? 1.012   0.141   6.198   1.00 20.76  ? 129 PHE B CB     1 
ATOM   4610  C  CG     . PHE B 2 130 ? 2.451   0.446   6.542   1.00 17.61  ? 129 PHE B CG     1 
ATOM   4611  C  CD1    . PHE B 2 130 ? 2.869   1.780   6.753   1.00 16.25  ? 129 PHE B CD1    1 
ATOM   4612  C  CD2    . PHE B 2 130 ? 3.397   -0.536  6.650   1.00 16.75  ? 129 PHE B CD2    1 
ATOM   4613  C  CE1    . PHE B 2 130 ? 4.193   2.091   7.100   1.00 16.08  ? 129 PHE B CE1    1 
ATOM   4614  C  CE2    . PHE B 2 130 ? 4.734   -0.228  6.961   1.00 18.43  ? 129 PHE B CE2    1 
ATOM   4615  C  CZ     . PHE B 2 130 ? 5.131   1.099   7.180   1.00 17.71  ? 129 PHE B CZ     1 
ATOM   4616  H  H      . PHE B 2 130 ? 0.622   1.316   8.715   1.00 21.66  ? 129 PHE B H      1 
ATOM   4617  H  HA     . PHE B 2 130 ? -0.768  -0.337  7.102   1.00 23.01  ? 129 PHE B HA     1 
ATOM   4618  H  HB2    . PHE B 2 130 ? 1.002   -0.664  5.657   1.00 24.95  ? 129 PHE B HB2    1 
ATOM   4619  H  HB3    . PHE B 2 130 ? 0.667   0.889   5.685   1.00 24.95  ? 129 PHE B HB3    1 
ATOM   4620  H  HD1    . PHE B 2 130 ? 2.251   2.469   6.659   1.00 19.54  ? 129 PHE B HD1    1 
ATOM   4621  H  HD2    . PHE B 2 130 ? 3.152   -1.423  6.516   1.00 19.93  ? 129 PHE B HD2    1 
ATOM   4622  H  HE1    . PHE B 2 130 ? 4.432   2.972   7.277   1.00 19.33  ? 129 PHE B HE1    1 
ATOM   4623  H  HE2    . PHE B 2 130 ? 5.362   -0.912  7.021   1.00 22.15  ? 129 PHE B HE2    1 
ATOM   4624  H  HZ     . PHE B 2 130 ? 6.017   1.302   7.376   1.00 21.29  ? 129 PHE B HZ     1 
ATOM   4625  N  N      . GLY B 2 131 ? 0.854   -1.050  9.542   1.00 21.03  ? 130 GLY B N      1 
ATOM   4626  C  CA     . GLY B 2 131 ? 1.389   -2.151  10.322  1.00 19.50  ? 130 GLY B CA     1 
ATOM   4627  C  C      . GLY B 2 131 ? 1.329   -1.871  11.804  1.00 18.73  ? 130 GLY B C      1 
ATOM   4628  O  O      . GLY B 2 131 ? 0.845   -0.827  12.256  1.00 19.54  ? 130 GLY B O      1 
ATOM   4629  H  H      . GLY B 2 131 ? 0.691   -0.326  9.977   1.00 25.26  ? 130 GLY B H      1 
ATOM   4630  H  HA2    . GLY B 2 131 ? 0.877   -2.955  10.141  1.00 23.43  ? 130 GLY B HA2    1 
ATOM   4631  H  HA3    . GLY B 2 131 ? 2.314   -2.304  10.075  1.00 23.43  ? 130 GLY B HA3    1 
ATOM   4632  N  N      . LYS B 2 132 ? 1.839   -2.825  12.560  1.00 19.60  ? 131 LYS B N      1 
ATOM   4633  C  CA     . LYS B 2 132 ? 1.871   -2.659  14.010  1.00 19.95  ? 131 LYS B CA     1 
ATOM   4634  C  C      . LYS B 2 132 ? 2.983   -3.517  14.565  1.00 23.65  ? 131 LYS B C      1 
ATOM   4635  O  O      . LYS B 2 132 ? 3.277   -4.599  14.047  1.00 23.86  ? 131 LYS B O      1 
ATOM   4636  C  CB     . LYS B 2 132 ? 0.532   -3.052  14.641  1.00 25.99  ? 131 LYS B CB     1 
ATOM   4637  C  CG     . LYS B 2 132 ? 0.411   -2.680  16.094  1.00 29.98  ? 131 LYS B CG     1 
ATOM   4638  C  CD     . LYS B 2 132 ? -0.842  -1.864  16.416  1.00 35.78  ? 131 LYS B CD     1 
ATOM   4639  C  CE     . LYS B 2 132 ? -0.898  -1.488  17.907  1.00 35.89  ? 131 LYS B CE     1 
ATOM   4640  N  NZ     . LYS B 2 132 ? -1.557  -2.536  18.739  1.00 44.02  ? 131 LYS B NZ     1 
ATOM   4641  H  H      . LYS B 2 132 ? 2.167   -3.565  12.269  1.00 23.56  ? 131 LYS B H      1 
ATOM   4642  H  HA     . LYS B 2 132 ? 2.056   -1.733  14.231  1.00 23.98  ? 131 LYS B HA     1 
ATOM   4643  H  HB2    . LYS B 2 132 ? -0.182  -2.604  14.161  1.00 31.23  ? 131 LYS B HB2    1 
ATOM   4644  H  HB3    . LYS B 2 132 ? 0.426   -4.013  14.572  1.00 31.23  ? 131 LYS B HB3    1 
ATOM   4645  H  HG2    . LYS B 2 132 ? 0.379   -3.492  16.623  1.00 36.01  ? 131 LYS B HG2    1 
ATOM   4646  H  HG3    . LYS B 2 132 ? 1.182   -2.149  16.347  1.00 36.01  ? 131 LYS B HG3    1 
ATOM   4647  H  HD2    . LYS B 2 132 ? -0.836  -1.046  15.895  1.00 42.97  ? 131 LYS B HD2    1 
ATOM   4648  H  HD3    . LYS B 2 132 ? -1.630  -2.387  16.203  1.00 42.97  ? 131 LYS B HD3    1 
ATOM   4649  H  HE2    . LYS B 2 132 ? 0.006   -1.366  18.237  1.00 43.10  ? 131 LYS B HE2    1 
ATOM   4650  H  HE3    . LYS B 2 132 ? -1.401  -0.664  18.007  1.00 43.10  ? 131 LYS B HE3    1 
ATOM   4651  H  HZ1    . LYS B 2 132 ? -1.570  -2.284  19.593  1.00 52.86  ? 131 LYS B HZ1    1 
ATOM   4652  H  HZ2    . LYS B 2 132 ? -2.394  -2.663  18.463  1.00 52.86  ? 131 LYS B HZ2    1 
ATOM   4653  H  HZ3    . LYS B 2 132 ? -1.112  -3.303  18.672  1.00 52.86  ? 131 LYS B HZ3    1 
ATOM   4654  N  N      . VAL B 2 133 ? 3.587   -3.025  15.640  1.00 20.75  ? 132 VAL B N      1 
ATOM   4655  C  CA     . VAL B 2 133 ? 4.579   -3.818  16.359  1.00 23.03  ? 132 VAL B CA     1 
ATOM   4656  C  C      . VAL B 2 133 ? 3.913   -5.072  16.882  1.00 23.22  ? 132 VAL B C      1 
ATOM   4657  O  O      . VAL B 2 133 ? 2.844   -5.008  17.497  1.00 25.27  ? 132 VAL B O      1 
ATOM   4658  C  CB     . VAL B 2 133 ? 5.201   -3.015  17.509  1.00 21.76  ? 132 VAL B CB     1 
ATOM   4659  C  CG1    . VAL B 2 133 ? 6.050   -3.954  18.384  1.00 22.61  ? 132 VAL B CG1    1 
ATOM   4660  C  CG2    . VAL B 2 133 ? 6.066   -1.883  16.999  1.00 20.15  ? 132 VAL B CG2    1 
ATOM   4661  H  H      . VAL B 2 133 ? 3.443   -2.244  15.971  1.00 24.93  ? 132 VAL B H      1 
ATOM   4662  H  HA     . VAL B 2 133 ? 5.289   -4.058  15.744  1.00 27.67  ? 132 VAL B HA     1 
ATOM   4663  H  HB     . VAL B 2 133 ? 4.484   -2.625  18.033  1.00 26.15  ? 132 VAL B HB     1 
ATOM   4664  H  HG11   . VAL B 2 133 ? 6.680   -3.424  18.897  1.00 27.17  ? 132 VAL B HG11   1 
ATOM   4665  H  HG12   . VAL B 2 133 ? 5.465   -4.443  18.983  1.00 27.17  ? 132 VAL B HG12   1 
ATOM   4666  H  HG13   . VAL B 2 133 ? 6.529   -4.573  17.810  1.00 27.17  ? 132 VAL B HG13   1 
ATOM   4667  H  HG21   . VAL B 2 133 ? 6.389   -1.368  17.754  1.00 24.21  ? 132 VAL B HG21   1 
ATOM   4668  H  HG22   . VAL B 2 133 ? 6.814   -2.254  16.507  1.00 24.21  ? 132 VAL B HG22   1 
ATOM   4669  H  HG23   . VAL B 2 133 ? 5.534   -1.318  16.416  1.00 24.21  ? 132 VAL B HG23   1 
ATOM   4670  N  N      . LYS B 2 134 ? 4.553   -6.219  16.621  1.00 25.28  ? 133 LYS B N      1 
ATOM   4671  C  CA     . LYS B 2 134 ? 4.160   -7.547  17.094  1.00 26.93  ? 133 LYS B CA     1 
ATOM   4672  C  C      . LYS B 2 134 ? 4.903   -7.928  18.369  1.00 31.72  ? 133 LYS B C      1 
ATOM   4673  O  O      . LYS B 2 134 ? 4.295   -8.117  19.423  1.00 33.01  ? 133 LYS B O      1 
ATOM   4674  C  CB     . LYS B 2 134 ? 4.443   -8.558  15.968  1.00 30.39  ? 133 LYS B CB     1 
ATOM   4675  C  CG     . LYS B 2 134 ? 3.906   -9.954  16.182  1.00 37.29  ? 133 LYS B CG     1 
ATOM   4676  C  CD     . LYS B 2 134 ? 3.839   -10.700 14.833  1.00 42.00  ? 133 LYS B CD     1 
ATOM   4677  C  CE     . LYS B 2 134 ? 4.311   -12.138 14.981  1.00 49.71  ? 133 LYS B CE     1 
ATOM   4678  N  NZ     . LYS B 2 134 ? 3.240   -13.054 14.511  1.00 51.20  ? 133 LYS B NZ     1 
ATOM   4679  H  H      . LYS B 2 134 ? 5.265   -6.253  16.140  1.00 30.37  ? 133 LYS B H      1 
ATOM   4680  H  HA     . LYS B 2 134 ? 3.213   -7.564  17.300  1.00 32.35  ? 133 LYS B HA     1 
ATOM   4681  H  HB2    . LYS B 2 134 ? 4.045   -8.220  15.150  1.00 36.50  ? 133 LYS B HB2    1 
ATOM   4682  H  HB3    . LYS B 2 134 ? 5.404   -8.633  15.862  1.00 36.50  ? 133 LYS B HB3    1 
ATOM   4683  H  HG2    . LYS B 2 134 ? 4.493   -10.443 16.780  1.00 44.78  ? 133 LYS B HG2    1 
ATOM   4684  H  HG3    . LYS B 2 134 ? 3.013   -9.908  16.557  1.00 44.78  ? 133 LYS B HG3    1 
ATOM   4685  H  HD2    . LYS B 2 134 ? 2.923   -10.709 14.514  1.00 50.43  ? 133 LYS B HD2    1 
ATOM   4686  H  HD3    . LYS B 2 134 ? 4.411   -10.255 14.189  1.00 50.43  ? 133 LYS B HD3    1 
ATOM   4687  H  HE2    . LYS B 2 134 ? 5.106   -12.281 14.444  1.00 59.68  ? 133 LYS B HE2    1 
ATOM   4688  H  HE3    . LYS B 2 134 ? 4.501   -12.328 15.913  1.00 59.68  ? 133 LYS B HE3    1 
ATOM   4689  H  HZ1    . LYS B 2 134 ? 3.505   -13.899 14.593  1.00 61.47  ? 133 LYS B HZ1    1 
ATOM   4690  H  HZ2    . LYS B 2 134 ? 2.502   -12.934 14.994  1.00 61.47  ? 133 LYS B HZ2    1 
ATOM   4691  H  HZ3    . LYS B 2 134 ? 3.054   -12.891 13.656  1.00 61.47  ? 133 LYS B HZ3    1 
ATOM   4692  N  N      . GLU B 2 135 ? 6.213   -8.033  18.290  1.00 29.05  ? 134 GLU B N      1 
ATOM   4693  C  CA     . GLU B 2 135 ? 7.034   -8.275  19.459  1.00 31.45  ? 134 GLU B CA     1 
ATOM   4694  C  C      . GLU B 2 135 ? 8.057   -7.170  19.605  1.00 25.63  ? 134 GLU B C      1 
ATOM   4695  O  O      . GLU B 2 135 ? 8.423   -6.497  18.636  1.00 28.25  ? 134 GLU B O      1 
ATOM   4696  C  CB     . GLU B 2 135 ? 7.732   -9.627  19.379  1.00 36.28  ? 134 GLU B CB     1 
ATOM   4697  C  CG     . GLU B 2 135 ? 6.792   -10.792 19.186  1.00 42.15  ? 134 GLU B CG     1 
ATOM   4698  C  CD     . GLU B 2 135 ? 6.465   -11.474 20.491  1.00 46.88  ? 134 GLU B CD     1 
ATOM   4699  O  OE1    . GLU B 2 135 ? 5.441   -11.092 21.122  1.00 49.66  ? 134 GLU B OE1    1 
ATOM   4700  O  OE2    . GLU B 2 135 ? 7.252   -12.360 20.909  1.00 55.48  ? 134 GLU B OE2    1 
ATOM   4701  H  H      . GLU B 2 135 ? 6.659   -7.967  17.557  1.00 34.89  ? 134 GLU B H      1 
ATOM   4702  H  HA     . GLU B 2 135 ? 6.475   -8.276  20.252  1.00 37.77  ? 134 GLU B HA     1 
ATOM   4703  H  HB2    . GLU B 2 135 ? 8.347   -9.616  18.629  1.00 43.56  ? 134 GLU B HB2    1 
ATOM   4704  H  HB3    . GLU B 2 135 ? 8.219   -9.775  20.205  1.00 43.56  ? 134 GLU B HB3    1 
ATOM   4705  H  HG2    . GLU B 2 135 ? 5.964   -10.473 18.794  1.00 50.62  ? 134 GLU B HG2    1 
ATOM   4706  H  HG3    . GLU B 2 135 ? 7.207   -11.443 18.599  1.00 50.62  ? 134 GLU B HG3    1 
ATOM   4707  N  N      . GLY B 2 136 ? 8.486   -6.960  20.842  1.00 23.80  ? 135 GLY B N      1 
ATOM   4708  C  CA     . GLY B 2 136 ? 9.543   -6.020  21.100  1.00 25.61  ? 135 GLY B CA     1 
ATOM   4709  C  C      . GLY B 2 136 ? 9.074   -4.598  21.234  1.00 23.42  ? 135 GLY B C      1 
ATOM   4710  O  O      . GLY B 2 136 ? 9.845   -3.687  21.003  1.00 22.58  ? 135 GLY B O      1 
ATOM   4711  H  H      . GLY B 2 136 ? 8.177   -7.352  21.542  1.00 28.60  ? 135 GLY B H      1 
ATOM   4712  H  HA2    . GLY B 2 136 ? 9.989   -6.267  21.924  1.00 30.77  ? 135 GLY B HA2    1 
ATOM   4713  H  HA3    . GLY B 2 136 ? 10.182  -6.057  20.371  1.00 30.77  ? 135 GLY B HA3    1 
ATOM   4714  N  N      . MET B 2 137 ? 7.818   -4.366  21.619  1.00 22.76  ? 136 MET B N      1 
ATOM   4715  C  CA     . MET B 2 137 ? 7.468   -2.967  21.835  1.00 23.77  ? 136 MET B CA     1 
ATOM   4716  C  C      . MET B 2 137 ? 8.346   -2.353  22.919  1.00 21.38  ? 136 MET B C      1 
ATOM   4717  O  O      . MET B 2 137 ? 8.626   -1.151  22.853  1.00 20.60  ? 136 MET B O      1 
ATOM   4718  C  CB     . MET B 2 137 ? 5.980   -2.816  22.140  1.00 25.37  ? 136 MET B CB     1 
ATOM   4719  C  CG     . MET B 2 137 ? 5.594   -1.377  22.510  1.00 27.02  ? 136 MET B CG     1 
ATOM   4720  S  SD     . MET B 2 137 ? 5.425   -0.436  20.903  1.00 22.55  ? 136 MET B SD     1 
ATOM   4721  C  CE     . MET B 2 137 ? 5.696   1.236   21.543  1.00 21.90  ? 136 MET B CE     1 
ATOM   4722  H  H      . MET B 2 137 ? 7.202   -4.952  21.750  1.00 27.35  ? 136 MET B H      1 
ATOM   4723  H  HA     . MET B 2 137 ? 7.611   -2.473  21.012  1.00 28.56  ? 136 MET B HA     1 
ATOM   4724  H  HB2    . MET B 2 137 ? 5.469   -3.072  21.357  1.00 30.47  ? 136 MET B HB2    1 
ATOM   4725  H  HB3    . MET B 2 137 ? 5.751   -3.390  22.888  1.00 30.47  ? 136 MET B HB3    1 
ATOM   4726  H  HG2    . MET B 2 137 ? 4.748   -1.365  22.984  1.00 32.45  ? 136 MET B HG2    1 
ATOM   4727  H  HG3    . MET B 2 137 ? 6.285   -0.970  23.054  1.00 32.45  ? 136 MET B HG3    1 
ATOM   4728  H  HE1    . MET B 2 137 ? 5.589   1.872   20.818  1.00 26.31  ? 136 MET B HE1    1 
ATOM   4729  H  HE2    . MET B 2 137 ? 5.046   1.416   22.240  1.00 26.31  ? 136 MET B HE2    1 
ATOM   4730  H  HE3    . MET B 2 137 ? 6.594   1.294   21.904  1.00 26.31  ? 136 MET B HE3    1 
ATOM   4731  N  N      . ASN B 2 138 ? 8.856   -3.159  23.888  1.00 23.00  ? 137 ASN B N      1 
ATOM   4732  C  CA     . ASN B 2 138 ? 9.693   -2.560  24.925  1.00 23.62  ? 137 ASN B CA     1 
ATOM   4733  C  C      . ASN B 2 138 ? 11.017  -2.042  24.347  1.00 22.08  ? 137 ASN B C      1 
ATOM   4734  O  O      . ASN B 2 138 ? 11.635  -1.171  24.939  1.00 21.93  ? 137 ASN B O      1 
ATOM   4735  C  CB     . ASN B 2 138 ? 9.929   -3.520  26.102  1.00 25.03  ? 137 ASN B CB     1 
ATOM   4736  C  CG     . ASN B 2 138 ? 10.356  -4.909  25.700  1.00 29.52  ? 137 ASN B CG     1 
ATOM   4737  O  OD1    . ASN B 2 138 ? 10.674  -5.191  24.547  1.00 27.07  ? 137 ASN B OD1    1 
ATOM   4738  N  ND2    . ASN B 2 138 ? 10.362  -5.808  26.681  1.00 29.58  ? 137 ASN B ND2    1 
ATOM   4739  H  H      . ASN B 2 138 ? 8.732   -4.008  23.950  1.00 27.63  ? 137 ASN B H      1 
ATOM   4740  H  HA     . ASN B 2 138 ? 9.216   -1.807  25.309  1.00 28.38  ? 137 ASN B HA     1 
ATOM   4741  H  HB2    . ASN B 2 138 ? 10.627  -3.152  26.667  1.00 30.07  ? 137 ASN B HB2    1 
ATOM   4742  H  HB3    . ASN B 2 138 ? 9.104   -3.601  26.606  1.00 30.07  ? 137 ASN B HB3    1 
ATOM   4743  H  HD21   . ASN B 2 138 ? 10.132  -5.578  27.477  1.00 35.53  ? 137 ASN B HD21   1 
ATOM   4744  H  HD22   . ASN B 2 138 ? 10.595  -6.620  26.518  1.00 35.53  ? 137 ASN B HD22   1 
ATOM   4745  N  N      . ILE B 2 139 ? 11.429  -2.532  23.178  1.00 21.75  ? 138 ILE B N      1 
ATOM   4746  C  CA     . ILE B 2 139 ? 12.601  -2.004  22.498  1.00 20.27  ? 138 ILE B CA     1 
ATOM   4747  C  C      . ILE B 2 139 ? 12.316  -0.588  22.016  1.00 20.25  ? 138 ILE B C      1 
ATOM   4748  O  O      . ILE B 2 139 ? 13.157  0.318   22.118  1.00 20.94  ? 138 ILE B O      1 
ATOM   4749  C  CB     . ILE B 2 139 ? 12.965  -2.928  21.313  1.00 25.32  ? 138 ILE B CB     1 
ATOM   4750  C  CG1    . ILE B 2 139 ? 13.110  -4.391  21.751  1.00 24.93  ? 138 ILE B CG1    1 
ATOM   4751  C  CG2    . ILE B 2 139 ? 14.193  -2.437  20.626  1.00 26.62  ? 138 ILE B CG2    1 
ATOM   4752  C  CD1    . ILE B 2 139 ? 14.130  -4.547  22.752  1.00 28.62  ? 138 ILE B CD1    1 
ATOM   4753  H  H      . ILE B 2 139 ? 11.043  -3.174  22.757  1.00 26.14  ? 138 ILE B H      1 
ATOM   4754  H  HA     . ILE B 2 139 ? 13.349  -1.979  23.115  1.00 24.36  ? 138 ILE B HA     1 
ATOM   4755  H  HB     . ILE B 2 139 ? 12.230  -2.897  20.681  1.00 30.41  ? 138 ILE B HB     1 
ATOM   4756  H  HG12   . ILE B 2 139 ? 12.269  -4.698  22.123  1.00 29.95  ? 138 ILE B HG12   1 
ATOM   4757  H  HG13   . ILE B 2 139 ? 13.352  -4.932  20.983  1.00 29.95  ? 138 ILE B HG13   1 
ATOM   4758  H  HG21   . ILE B 2 139 ? 14.527  -3.134  20.040  1.00 31.98  ? 138 ILE B HG21   1 
ATOM   4759  H  HG22   . ILE B 2 139 ? 13.971  -1.647  20.108  1.00 31.98  ? 138 ILE B HG22   1 
ATOM   4760  H  HG23   . ILE B 2 139 ? 14.862  -2.216  21.293  1.00 31.98  ? 138 ILE B HG23   1 
ATOM   4761  H  HD11   . ILE B 2 139 ? 14.271  -5.493  22.913  1.00 34.38  ? 138 ILE B HD11   1 
ATOM   4762  H  HD12   . ILE B 2 139 ? 14.950  -4.139  22.433  1.00 34.38  ? 138 ILE B HD12   1 
ATOM   4763  H  HD13   . ILE B 2 139 ? 13.840  -4.112  23.569  1.00 34.38  ? 138 ILE B HD13   1 
ATOM   4764  N  N      . VAL B 2 140 ? 11.146  -0.397  21.415  1.00 19.15  ? 139 VAL B N      1 
ATOM   4765  C  CA     . VAL B 2 140 ? 10.742  0.931   20.978  1.00 17.63  ? 139 VAL B CA     1 
ATOM   4766  C  C      . VAL B 2 140 ? 10.668  1.882   22.161  1.00 17.94  ? 139 VAL B C      1 
ATOM   4767  O  O      . VAL B 2 140 ? 11.111  3.029   22.068  1.00 18.68  ? 139 VAL B O      1 
ATOM   4768  C  CB     . VAL B 2 140 ? 9.388   0.825   20.243  1.00 18.94  ? 139 VAL B CB     1 
ATOM   4769  C  CG1    . VAL B 2 140 ? 8.965   2.207   19.761  1.00 18.92  ? 139 VAL B CG1    1 
ATOM   4770  C  CG2    . VAL B 2 140 ? 9.516   -0.205  19.093  1.00 19.96  ? 139 VAL B CG2    1 
ATOM   4771  H  H      . VAL B 2 140 ? 10.573  -1.017  21.249  1.00 23.02  ? 139 VAL B H      1 
ATOM   4772  H  HA     . VAL B 2 140 ? 11.405  1.285   20.365  1.00 20.99  ? 139 VAL B HA     1 
ATOM   4773  H  HB     . VAL B 2 140 ? 8.687   0.508   20.834  1.00 22.76  ? 139 VAL B HB     1 
ATOM   4774  H  HG11   . VAL B 2 140 ? 8.210   2.115   19.159  1.00 22.73  ? 139 VAL B HG11   1 
ATOM   4775  H  HG12   . VAL B 2 140 ? 8.713   2.746   20.528  1.00 22.73  ? 139 VAL B HG12   1 
ATOM   4776  H  HG13   . VAL B 2 140 ? 9.710   2.621   19.297  1.00 22.73  ? 139 VAL B HG13   1 
ATOM   4777  H  HG21   . VAL B 2 140 ? 8.740   -0.133  18.517  1.00 23.98  ? 139 VAL B HG21   1 
ATOM   4778  H  HG22   . VAL B 2 140 ? 10.322  -0.016  18.588  1.00 23.98  ? 139 VAL B HG22   1 
ATOM   4779  H  HG23   . VAL B 2 140 ? 9.565   -1.097  19.472  1.00 23.98  ? 139 VAL B HG23   1 
ATOM   4780  N  N      . GLU B 2 141 ? 10.065  1.442   23.265  1.00 19.79  ? 140 GLU B N      1 
ATOM   4781  C  CA     . GLU B 2 141 ? 10.046  2.246   24.493  1.00 18.76  ? 140 GLU B CA     1 
ATOM   4782  C  C      . GLU B 2 141 ? 11.468  2.596   24.923  1.00 19.41  ? 140 GLU B C      1 
ATOM   4783  O  O      . GLU B 2 141 ? 11.790  3.757   25.181  1.00 20.19  ? 140 GLU B O      1 
ATOM   4784  C  CB     . GLU B 2 141 ? 9.324   1.492   25.610  1.00 19.96  ? 140 GLU B CB     1 
ATOM   4785  C  CG     . GLU B 2 141 ? 7.867   1.147   25.255  1.00 21.00  ? 140 GLU B CG     1 
ATOM   4786  C  CD     . GLU B 2 141 ? 7.112   0.240   26.206  1.00 27.80  ? 140 GLU B CD     1 
ATOM   4787  O  OE1    . GLU B 2 141 ? 7.670   -0.216  27.219  1.00 31.77  ? 140 GLU B OE1    1 
ATOM   4788  O  OE2    . GLU B 2 141 ? 5.923   -0.080  25.929  1.00 31.01  ? 140 GLU B OE2    1 
ATOM   4789  H  H      . GLU B 2 141 ? 9.662   0.686   23.332  1.00 23.78  ? 140 GLU B H      1 
ATOM   4790  H  HA     . GLU B 2 141 ? 9.558   3.067   24.323  1.00 22.34  ? 140 GLU B HA     1 
ATOM   4791  H  HB2    . GLU B 2 141 ? 9.795   0.662   25.785  1.00 23.98  ? 140 GLU B HB2    1 
ATOM   4792  H  HB3    . GLU B 2 141 ? 9.316   2.044   26.408  1.00 23.98  ? 140 GLU B HB3    1 
ATOM   4793  H  HG2    . GLU B 2 141 ? 7.368   1.977   25.206  1.00 25.24  ? 140 GLU B HG2    1 
ATOM   4794  H  HG3    . GLU B 2 141 ? 7.867   0.708   24.390  1.00 25.24  ? 140 GLU B HG3    1 
ATOM   4795  N  N      . ALA B 2 142 ? 12.348  1.592   24.926  1.00 20.02  ? 141 ALA B N      1 
ATOM   4796  C  CA     . ALA B 2 142 ? 13.755  1.826   25.231  1.00 21.72  ? 141 ALA B CA     1 
ATOM   4797  C  C      . ALA B 2 142 ? 14.399  2.853   24.317  1.00 20.25  ? 141 ALA B C      1 
ATOM   4798  O  O      . ALA B 2 142 ? 15.291  3.575   24.768  1.00 21.75  ? 141 ALA B O      1 
ATOM   4799  C  CB     . ALA B 2 142 ? 14.512  0.497   25.176  1.00 23.66  ? 141 ALA B CB     1 
ATOM   4800  H  H      . ALA B 2 142 ? 12.155  0.772   24.755  1.00 24.06  ? 141 ALA B H      1 
ATOM   4801  H  HA     . ALA B 2 142 ? 13.818  2.183   26.131  1.00 26.10  ? 141 ALA B HA     1 
ATOM   4802  H  HB1    . ALA B 2 142 ? 15.443  0.655   25.401  1.00 28.43  ? 141 ALA B HB1    1 
ATOM   4803  H  HB2    . ALA B 2 142 ? 14.118  -0.118  25.814  1.00 28.43  ? 141 ALA B HB2    1 
ATOM   4804  H  HB3    . ALA B 2 142 ? 14.445  0.132   24.280  1.00 28.43  ? 141 ALA B HB3    1 
ATOM   4805  N  N      . MET B 2 143 ? 13.954  2.969   23.047  1.00 20.33  ? 142 MET B N      1 
ATOM   4806  C  CA     . MET B 2 143 ? 14.577  3.913   22.131  1.00 18.86  ? 142 MET B CA     1 
ATOM   4807  C  C      . MET B 2 143 ? 14.253  5.360   22.527  1.00 20.50  ? 142 MET B C      1 
ATOM   4808  O  O      . MET B 2 143 ? 15.045  6.252   22.252  1.00 18.41  ? 142 MET B O      1 
ATOM   4809  C  CB     . MET B 2 143 ? 14.103  3.635   20.699  1.00 19.91  ? 142 MET B CB     1 
ATOM   4810  C  CG     . MET B 2 143 ? 14.836  2.469   20.029  1.00 19.98  ? 142 MET B CG     1 
ATOM   4811  S  SD     . MET B 2 143 ? 13.882  1.649   18.691  1.00 28.74  ? 142 MET B SD     1 
ATOM   4812  C  CE     . MET B 2 143 ? 13.926  3.001   17.639  1.00 21.86  ? 142 MET B CE     1 
ATOM   4813  H  H      . MET B 2 143 ? 13.306  2.515   22.708  1.00 24.43  ? 142 MET B H      1 
ATOM   4814  H  HA     . MET B 2 143 ? 15.539  3.790   22.155  1.00 22.67  ? 142 MET B HA     1 
ATOM   4815  H  HB2    . MET B 2 143 ? 13.157  3.420   20.718  1.00 23.93  ? 142 MET B HB2    1 
ATOM   4816  H  HB3    . MET B 2 143 ? 14.252  4.428   20.161  1.00 23.93  ? 142 MET B HB3    1 
ATOM   4817  H  HG2    . MET B 2 143 ? 15.660  2.803   19.640  1.00 24.01  ? 142 MET B HG2    1 
ATOM   4818  H  HG3    . MET B 2 143 ? 15.034  1.799   20.702  1.00 24.01  ? 142 MET B HG3    1 
ATOM   4819  H  HE1    . MET B 2 143 ? 13.440  2.786   16.827  1.00 26.27  ? 142 MET B HE1    1 
ATOM   4820  H  HE2    . MET B 2 143 ? 13.511  3.759   18.081  1.00 26.27  ? 142 MET B HE2    1 
ATOM   4821  H  HE3    . MET B 2 143 ? 14.849  3.207   17.427  1.00 26.27  ? 142 MET B HE3    1 
ATOM   4822  N  N      . GLU B 2 144 ? 13.108  5.606   23.189  1.00 23.90  ? 143 GLU B N      1 
ATOM   4823  C  CA     . GLU B 2 144 ? 12.760  6.968   23.635  1.00 22.56  ? 143 GLU B CA     1 
ATOM   4824  C  C      . GLU B 2 144 ? 13.775  7.562   24.579  1.00 25.84  ? 143 GLU B C      1 
ATOM   4825  O  O      . GLU B 2 144 ? 13.880  8.791   24.686  1.00 28.38  ? 143 GLU B O      1 
ATOM   4826  C  CB     . GLU B 2 144 ? 11.397  6.986   24.356  1.00 25.37  ? 143 GLU B CB     1 
ATOM   4827  C  CG     . GLU B 2 144 ? 10.268  6.781   23.430  1.00 20.23  ? 143 GLU B CG     1 
ATOM   4828  C  CD     . GLU B 2 144 ? 8.917   7.129   24.047  1.00 25.81  ? 143 GLU B CD     1 
ATOM   4829  O  OE1    . GLU B 2 144 ? 8.706   6.740   25.179  1.00 26.99  ? 143 GLU B OE1    1 
ATOM   4830  O  OE2    . GLU B 2 144 ? 8.084   7.793   23.399  1.00 24.01  ? 143 GLU B OE2    1 
ATOM   4831  H  H      . GLU B 2 144 ? 12.522  5.010   23.390  1.00 28.72  ? 143 GLU B H      1 
ATOM   4832  H  HA     . GLU B 2 144 ? 12.717  7.507   22.830  1.00 27.10  ? 143 GLU B HA     1 
ATOM   4833  H  HB2    . GLU B 2 144 ? 11.378  6.276   25.017  1.00 30.48  ? 143 GLU B HB2    1 
ATOM   4834  H  HB3    . GLU B 2 144 ? 11.279  7.845   24.790  1.00 30.48  ? 143 GLU B HB3    1 
ATOM   4835  H  HG2    . GLU B 2 144 ? 10.395  7.344   22.650  1.00 24.31  ? 143 GLU B HG2    1 
ATOM   4836  H  HG3    . GLU B 2 144 ? 10.244  5.848   23.165  1.00 24.31  ? 143 GLU B HG3    1 
ATOM   4837  N  N      . ARG B 2 145 ? 14.478  6.721   25.330  1.00 24.13  ? 144 ARG B N      1 
ATOM   4838  C  CA     . ARG B 2 145 ? 15.490  7.223   26.242  1.00 30.39  ? 144 ARG B CA     1 
ATOM   4839  C  C      . ARG B 2 145 ? 16.523  8.071   25.520  1.00 26.86  ? 144 ARG B C      1 
ATOM   4840  O  O      . ARG B 2 145 ? 17.209  8.872   26.162  1.00 29.69  ? 144 ARG B O      1 
ATOM   4841  C  CB     . ARG B 2 145 ? 16.174  6.060   26.976  1.00 31.75  ? 144 ARG B CB     1 
ATOM   4842  C  CG     . ARG B 2 145 ? 15.216  5.087   27.638  1.00 38.19  ? 144 ARG B CG     1 
ATOM   4843  C  CD     . ARG B 2 145 ? 15.914  3.869   28.281  1.00 40.69  ? 144 ARG B CD     1 
ATOM   4844  N  NE     . ARG B 2 145 ? 16.768  3.083   27.377  1.00 41.19  ? 144 ARG B NE     1 
ATOM   4845  C  CZ     . ARG B 2 145 ? 17.390  1.969   27.762  1.00 45.70  ? 144 ARG B CZ     1 
ATOM   4846  N  NH1    . ARG B 2 145 ? 17.196  1.454   28.968  1.00 42.03  ? 144 ARG B NH1    1 
ATOM   4847  N  NH2    . ARG B 2 145 ? 18.219  1.348   26.918  1.00 38.20  ? 144 ARG B NH2    1 
ATOM   4848  H  H      . ARG B 2 145 ? 14.388  5.866   25.329  1.00 28.99  ? 144 ARG B H      1 
ATOM   4849  H  HA     . ARG B 2 145 ? 15.061  7.775   26.914  1.00 36.51  ? 144 ARG B HA     1 
ATOM   4850  H  HB2    . ARG B 2 145 ? 16.705  5.560   26.336  1.00 38.13  ? 144 ARG B HB2    1 
ATOM   4851  H  HB3    . ARG B 2 145 ? 16.746  6.426   27.668  1.00 38.13  ? 144 ARG B HB3    1 
ATOM   4852  H  HG2    . ARG B 2 145 ? 14.730  5.552   28.337  1.00 45.86  ? 144 ARG B HG2    1 
ATOM   4853  H  HG3    . ARG B 2 145 ? 14.597  4.754   26.969  1.00 45.86  ? 144 ARG B HG3    1 
ATOM   4854  H  HD2    . ARG B 2 145 ? 16.475  4.185   29.006  1.00 48.86  ? 144 ARG B HD2    1 
ATOM   4855  H  HD3    . ARG B 2 145 ? 15.232  3.271   28.626  1.00 48.86  ? 144 ARG B HD3    1 
ATOM   4856  H  HE     . ARG B 2 145 ? 16.869  3.354   26.567  1.00 49.46  ? 144 ARG B HE     1 
ATOM   4857  H  HH11   . ARG B 2 145 ? 16.660  1.840   29.519  1.00 50.47  ? 144 ARG B HH11   1 
ATOM   4858  H  HH12   . ARG B 2 145 ? 17.606  0.735   29.199  1.00 50.47  ? 144 ARG B HH12   1 
ATOM   4859  H  HH21   . ARG B 2 145 ? 18.350  1.668   26.130  1.00 45.88  ? 144 ARG B HH21   1 
ATOM   4860  H  HH22   . ARG B 2 145 ? 18.622  0.629   27.163  1.00 45.88  ? 144 ARG B HH22   1 
ATOM   4861  N  N      . PHE B 2 146 ? 16.651  7.930   24.194  1.00 25.47  ? 145 PHE B N      1 
ATOM   4862  C  CA     . PHE B 2 146 ? 17.684  8.623   23.441  1.00 24.02  ? 145 PHE B CA     1 
ATOM   4863  C  C      . PHE B 2 146 ? 17.142  9.741   22.569  1.00 21.72  ? 145 PHE B C      1 
ATOM   4864  O  O      . PHE B 2 146 ? 17.889  10.311  21.755  1.00 21.05  ? 145 PHE B O      1 
ATOM   4865  C  CB     . PHE B 2 146 ? 18.453  7.595   22.617  1.00 23.20  ? 145 PHE B CB     1 
ATOM   4866  C  CG     . PHE B 2 146 ? 18.954  6.469   23.430  1.00 27.20  ? 145 PHE B CG     1 
ATOM   4867  C  CD1    . PHE B 2 146 ? 19.920  6.706   24.409  1.00 30.85  ? 145 PHE B CD1    1 
ATOM   4868  C  CD2    . PHE B 2 146 ? 18.429  5.193   23.301  1.00 24.91  ? 145 PHE B CD2    1 
ATOM   4869  C  CE1    . PHE B 2 146 ? 20.401  5.664   25.214  1.00 32.21  ? 145 PHE B CE1    1 
ATOM   4870  C  CE2    . PHE B 2 146 ? 18.909  4.155   24.096  1.00 30.36  ? 145 PHE B CE2    1 
ATOM   4871  C  CZ     . PHE B 2 146 ? 19.898  4.398   25.057  1.00 28.48  ? 145 PHE B CZ     1 
ATOM   4872  H  H      . PHE B 2 146 ? 16.142  7.433   23.711  1.00 30.59  ? 145 PHE B H      1 
ATOM   4873  H  HA     . PHE B 2 146 ? 18.303  9.048   24.055  1.00 28.86  ? 145 PHE B HA     1 
ATOM   4874  H  HB2    . PHE B 2 146 ? 17.866  7.234   21.934  1.00 27.87  ? 145 PHE B HB2    1 
ATOM   4875  H  HB3    . PHE B 2 146 ? 19.216  8.029   22.204  1.00 27.87  ? 145 PHE B HB3    1 
ATOM   4876  H  HD1    . PHE B 2 146 ? 20.250  7.568   24.529  1.00 37.05  ? 145 PHE B HD1    1 
ATOM   4877  H  HD2    . PHE B 2 146 ? 17.755  5.029   22.681  1.00 29.92  ? 145 PHE B HD2    1 
ATOM   4878  H  HE1    . PHE B 2 146 ? 21.057  5.830   25.852  1.00 38.69  ? 145 PHE B HE1    1 
ATOM   4879  H  HE2    . PHE B 2 146 ? 18.570  3.296   23.988  1.00 36.46  ? 145 PHE B HE2    1 
ATOM   4880  H  HZ     . PHE B 2 146 ? 20.213  3.702   25.587  1.00 34.21  ? 145 PHE B HZ     1 
ATOM   4881  N  N      . GLY B 2 147 ? 15.864  10.079  22.715  1.00 23.92  ? 146 GLY B N      1 
ATOM   4882  C  CA     . GLY B 2 147 ? 15.284  11.179  21.975  1.00 22.42  ? 146 GLY B CA     1 
ATOM   4883  C  C      . GLY B 2 147 ? 15.284  12.467  22.776  1.00 23.23  ? 146 GLY B C      1 
ATOM   4884  O  O      . GLY B 2 147 ? 15.902  12.584  23.834  1.00 23.42  ? 146 GLY B O      1 
ATOM   4885  H  H      . GLY B 2 147 ? 15.313  9.680   23.242  1.00 28.73  ? 146 GLY B H      1 
ATOM   4886  H  HA2    . GLY B 2 147 ? 15.792  11.324  21.162  1.00 26.94  ? 146 GLY B HA2    1 
ATOM   4887  H  HA3    . GLY B 2 147 ? 14.368  10.963  21.741  1.00 26.94  ? 146 GLY B HA3    1 
ATOM   4888  N  N      . SER B 2 148 ? 14.525  13.436  22.262  1.00 18.54  ? 147 SER B N      1 
ATOM   4889  C  CA     . SER B 2 148 ? 14.465  14.775  22.796  1.00 22.14  ? 147 SER B CA     1 
ATOM   4890  C  C      . SER B 2 148 ? 13.196  15.448  22.296  1.00 20.12  ? 147 SER B C      1 
ATOM   4891  O  O      . SER B 2 148 ? 12.479  14.932  21.416  1.00 20.38  ? 147 SER B O      1 
ATOM   4892  C  CB     . SER B 2 148 ? 15.710  15.576  22.378  1.00 21.63  ? 147 SER B CB     1 
ATOM   4893  O  OG     . SER B 2 148 ? 15.705  15.963  21.007  1.00 21.52  ? 147 SER B OG     1 
ATOM   4894  H  H      . SER B 2 148 ? 14.019  13.328  21.575  1.00 22.28  ? 147 SER B H      1 
ATOM   4895  H  HA     . SER B 2 148 ? 14.421  14.725  23.764  1.00 26.60  ? 147 SER B HA     1 
ATOM   4896  H  HB2    . SER B 2 148 ? 15.752  16.379  22.921  1.00 25.99  ? 147 SER B HB2    1 
ATOM   4897  H  HB3    . SER B 2 148 ? 16.494  15.027  22.537  1.00 25.99  ? 147 SER B HB3    1 
ATOM   4898  H  HG     . SER B 2 148 ? 15.746  15.282  20.517  1.00 25.86  ? 147 SER B HG     1 
ATOM   4899  N  N      . ARG B 2 149 ? 12.988  16.658  22.787  1.00 20.51  ? 148 ARG B N      1 
ATOM   4900  C  CA     . ARG B 2 149 ? 11.797  17.425  22.439  1.00 22.43  ? 148 ARG B CA     1 
ATOM   4901  C  C      . ARG B 2 149 ? 11.678  17.695  20.945  1.00 21.80  ? 148 ARG B C      1 
ATOM   4902  O  O      . ARG B 2 149 ? 10.569  17.589  20.389  1.00 22.96  ? 148 ARG B O      1 
ATOM   4903  C  CB     . ARG B 2 149 ? 11.782  18.746  23.205  1.00 26.96  ? 148 ARG B CB     1 
ATOM   4904  C  CG     . ARG B 2 149 ? 10.635  19.644  22.812  1.00 27.19  ? 148 ARG B CG     1 
ATOM   4905  C  CD     . ARG B 2 149 ? 10.562  20.863  23.781  1.00 32.62  ? 148 ARG B CD     1 
ATOM   4906  N  NE     . ARG B 2 149 ? 9.461   21.751  23.427  1.00 30.36  ? 148 ARG B NE     1 
ATOM   4907  C  CZ     . ARG B 2 149 ? 9.587   22.803  22.634  1.00 31.72  ? 148 ARG B CZ     1 
ATOM   4908  N  NH1    . ARG B 2 149 ? 10.758  23.150  22.143  1.00 35.32  ? 148 ARG B NH1    1 
ATOM   4909  N  NH2    . ARG B 2 149 ? 8.512   23.534  22.350  1.00 37.10  ? 148 ARG B NH2    1 
ATOM   4910  H  H      . ARG B 2 149 ? 13.521  17.064  23.326  1.00 24.65  ? 148 ARG B H      1 
ATOM   4911  H  HA     . ARG B 2 149 ? 11.027  16.894  22.700  1.00 26.95  ? 148 ARG B HA     1 
ATOM   4912  H  HB2    . ARG B 2 149 ? 11.703  18.558  24.154  1.00 32.39  ? 148 ARG B HB2    1 
ATOM   4913  H  HB3    . ARG B 2 149 ? 12.609  19.221  23.029  1.00 32.39  ? 148 ARG B HB3    1 
ATOM   4914  H  HG2    . ARG B 2 149 ? 10.771  19.971  21.909  1.00 32.66  ? 148 ARG B HG2    1 
ATOM   4915  H  HG3    . ARG B 2 149 ? 9.801   19.153  22.866  1.00 32.66  ? 148 ARG B HG3    1 
ATOM   4916  H  HD2    . ARG B 2 149 ? 10.421  20.547  24.687  1.00 39.18  ? 148 ARG B HD2    1 
ATOM   4917  H  HD3    . ARG B 2 149 ? 11.389  21.366  23.729  1.00 39.18  ? 148 ARG B HD3    1 
ATOM   4918  H  HE     . ARG B 2 149 ? 8.683   21.581  23.753  1.00 36.46  ? 148 ARG B HE     1 
ATOM   4919  H  HH11   . ARG B 2 149 ? 11.458  22.691  22.336  1.00 42.42  ? 148 ARG B HH11   1 
ATOM   4920  H  HH12   . ARG B 2 149 ? 10.822  23.837  21.629  1.00 42.42  ? 148 ARG B HH12   1 
ATOM   4921  H  HH21   . ARG B 2 149 ? 7.747   23.321  22.681  1.00 44.56  ? 148 ARG B HH21   1 
ATOM   4922  H  HH22   . ARG B 2 149 ? 8.581   24.220  21.836  1.00 44.56  ? 148 ARG B HH22   1 
ATOM   4923  N  N      . ASN B 2 150 ? 12.777  18.068  20.273  1.00 20.94  ? 149 ASN B N      1 
ATOM   4924  C  CA     . ASN B 2 150 ? 12.700  18.337  18.836  1.00 20.49  ? 149 ASN B CA     1 
ATOM   4925  C  C      . ASN B 2 150 ? 13.118  17.141  17.993  1.00 18.68  ? 149 ASN B C      1 
ATOM   4926  O  O      . ASN B 2 150 ? 13.149  17.255  16.782  1.00 18.32  ? 149 ASN B O      1 
ATOM   4927  C  CB     . ASN B 2 150 ? 13.527  19.563  18.451  1.00 22.07  ? 149 ASN B CB     1 
ATOM   4928  C  CG     . ASN B 2 150 ? 15.006  19.264  18.296  1.00 23.41  ? 149 ASN B CG     1 
ATOM   4929  O  OD1    . ASN B 2 150 ? 15.513  18.232  18.777  1.00 22.06  ? 149 ASN B OD1    1 
ATOM   4930  N  ND2    . ASN B 2 150 ? 15.712  20.168  17.623  1.00 22.35  ? 149 ASN B ND2    1 
ATOM   4931  H  H      . ASN B 2 150 ? 13.556  18.169  20.622  1.00 25.16  ? 149 ASN B H      1 
ATOM   4932  H  HA     . ASN B 2 150 ? 11.778  18.550  18.622  1.00 24.63  ? 149 ASN B HA     1 
ATOM   4933  H  HB2    . ASN B 2 150 ? 13.203  19.906  17.603  1.00 26.52  ? 149 ASN B HB2    1 
ATOM   4934  H  HB3    . ASN B 2 150 ? 13.430  20.237  19.141  1.00 26.52  ? 149 ASN B HB3    1 
ATOM   4935  H  HD21   . ASN B 2 150 ? 16.556  20.052  17.503  1.00 26.86  ? 149 ASN B HD21   1 
ATOM   4936  H  HD22   . ASN B 2 150 ? 15.324  20.867  17.306  1.00 26.86  ? 149 ASN B HD22   1 
ATOM   4937  N  N      . GLY B 2 151 ? 13.417  16.011  18.616  1.00 18.54  ? 150 GLY B N      1 
ATOM   4938  C  CA     . GLY B 2 151 ? 13.600  14.739  17.948  1.00 15.51  ? 150 GLY B CA     1 
ATOM   4939  C  C      . GLY B 2 151 ? 15.043  14.347  17.754  1.00 16.65  ? 150 GLY B C      1 
ATOM   4940  O  O      . GLY B 2 151 ? 15.326  13.189  17.458  1.00 18.22  ? 150 GLY B O      1 
ATOM   4941  H  H      . GLY B 2 151 ? 13.523  15.956  19.468  1.00 22.29  ? 150 GLY B H      1 
ATOM   4942  H  HA2    . GLY B 2 151 ? 13.170  14.045  18.471  1.00 18.64  ? 150 GLY B HA2    1 
ATOM   4943  H  HA3    . GLY B 2 151 ? 13.182  14.781  17.074  1.00 18.64  ? 150 GLY B HA3    1 
ATOM   4944  N  N      . LYS B 2 152 ? 15.968  15.287  17.909  1.00 17.45  ? 151 LYS B N      1 
ATOM   4945  C  CA     . LYS B 2 152 ? 17.379  14.935  17.806  1.00 19.92  ? 151 LYS B CA     1 
ATOM   4946  C  C      . LYS B 2 152 ? 17.724  13.852  18.819  1.00 19.01  ? 151 LYS B C      1 
ATOM   4947  O  O      . LYS B 2 152 ? 17.313  13.900  19.988  1.00 19.89  ? 151 LYS B O      1 
ATOM   4948  C  CB     . LYS B 2 152 ? 18.248  16.177  18.000  1.00 23.09  ? 151 LYS B CB     1 
ATOM   4949  C  CG     . LYS B 2 152 ? 17.926  17.387  17.081  1.00 30.16  ? 151 LYS B CG     1 
ATOM   4950  C  CD     . LYS B 2 152 ? 18.195  17.214  15.553  1.00 35.57  ? 151 LYS B CD     1 
ATOM   4951  C  CE     . LYS B 2 152 ? 18.584  18.570  14.833  1.00 39.93  ? 151 LYS B CE     1 
ATOM   4952  N  NZ     . LYS B 2 152 ? 17.429  19.298  14.109  1.00 39.81  ? 151 LYS B NZ     1 
ATOM   4953  H  H      . LYS B 2 152 ? 15.810  16.117  18.072  1.00 20.97  ? 151 LYS B H      1 
ATOM   4954  H  HA     . LYS B 2 152 ? 17.572  14.586  16.922  1.00 23.94  ? 151 LYS B HA     1 
ATOM   4955  H  HB2    . LYS B 2 152 ? 18.145  16.479  18.916  1.00 27.74  ? 151 LYS B HB2    1 
ATOM   4956  H  HB3    . LYS B 2 152 ? 19.172  15.930  17.834  1.00 27.74  ? 151 LYS B HB3    1 
ATOM   4957  H  HG2    . LYS B 2 152 ? 16.983  17.594  17.177  1.00 36.23  ? 151 LYS B HG2    1 
ATOM   4958  H  HG3    . LYS B 2 152 ? 18.462  18.140  17.376  1.00 36.23  ? 151 LYS B HG3    1 
ATOM   4959  H  HD2    . LYS B 2 152 ? 18.928  16.591  15.431  1.00 42.72  ? 151 LYS B HD2    1 
ATOM   4960  H  HD3    . LYS B 2 152 ? 17.393  16.871  15.129  1.00 42.72  ? 151 LYS B HD3    1 
ATOM   4961  H  HE2    . LYS B 2 152 ? 18.935  19.180  15.501  1.00 47.94  ? 151 LYS B HE2    1 
ATOM   4962  H  HE3    . LYS B 2 152 ? 19.265  18.379  14.169  1.00 47.94  ? 151 LYS B HE3    1 
ATOM   4963  H  HZ1    . LYS B 2 152 ? 17.732  20.041  13.724  1.00 47.81  ? 151 LYS B HZ1    1 
ATOM   4964  H  HZ2    . LYS B 2 152 ? 17.081  18.770  13.484  1.00 47.81  ? 151 LYS B HZ2    1 
ATOM   4965  H  HZ3    . LYS B 2 152 ? 16.792  19.514  14.692  1.00 47.81  ? 151 LYS B HZ3    1 
ATOM   4966  N  N      . THR B 2 153 ? 18.497  12.869  18.372  1.00 17.78  ? 152 THR B N      1 
ATOM   4967  C  CA     . THR B 2 153 ? 18.886  11.773  19.238  1.00 16.28  ? 152 THR B CA     1 
ATOM   4968  C  C      . THR B 2 153 ? 20.258  12.023  19.850  1.00 21.30  ? 152 THR B C      1 
ATOM   4969  O  O      . THR B 2 153 ? 21.096  12.726  19.267  1.00 22.49  ? 152 THR B O      1 
ATOM   4970  C  CB     . THR B 2 153 ? 18.878  10.442  18.496  1.00 21.62  ? 152 THR B CB     1 
ATOM   4971  O  OG1    . THR B 2 153 ? 19.826  10.397  17.428  1.00 21.66  ? 152 THR B OG1    1 
ATOM   4972  C  CG2    . THR B 2 153 ? 17.486  10.229  17.855  1.00 20.20  ? 152 THR B CG2    1 
ATOM   4973  H  H      . THR B 2 153 ? 18.806  12.818  17.571  1.00 21.37  ? 152 THR B H      1 
ATOM   4974  H  HA     . THR B 2 153 ? 18.245  11.710  19.963  1.00 19.57  ? 152 THR B HA     1 
ATOM   4975  H  HB     . THR B 2 153 ? 19.099  9.750   19.138  1.00 25.98  ? 152 THR B HB     1 
ATOM   4976  H  HG1    . THR B 2 153 ? 20.604  10.490  17.731  1.00 26.02  ? 152 THR B HG1    1 
ATOM   4977  H  HG21   . THR B 2 153 ? 17.431  9.341   17.469  1.00 24.28  ? 152 THR B HG21   1 
ATOM   4978  H  HG22   . THR B 2 153 ? 16.793  10.323  18.528  1.00 24.28  ? 152 THR B HG22   1 
ATOM   4979  H  HG23   . THR B 2 153 ? 17.337  10.886  17.157  1.00 24.28  ? 152 THR B HG23   1 
ATOM   4980  N  N      . SER B 2 154 ? 20.476  11.416  21.001  1.00 20.11  ? 153 SER B N      1 
ATOM   4981  C  CA     . SER B 2 154 ? 21.709  11.591  21.789  1.00 24.89  ? 153 SER B CA     1 
ATOM   4982  C  C      . SER B 2 154 ? 22.690  10.450  21.566  1.00 31.50  ? 153 SER B C      1 
ATOM   4983  O  O      . SER B 2 154 ? 23.866  10.577  21.942  1.00 29.71  ? 153 SER B O      1 
ATOM   4984  C  CB     . SER B 2 154 ? 21.408  11.712  23.295  1.00 22.38  ? 153 SER B CB     1 
ATOM   4985  O  OG     . SER B 2 154 ? 20.674  10.611  23.775  1.00 23.18  ? 153 SER B OG     1 
ATOM   4986  H  H      . SER B 2 154 ? 19.914  10.878  21.369  1.00 24.17  ? 153 SER B H      1 
ATOM   4987  H  HA     . SER B 2 154 ? 22.127  12.426  21.525  1.00 29.90  ? 153 SER B HA     1 
ATOM   4988  H  HB2    . SER B 2 154 ? 22.248  11.760  23.778  1.00 26.89  ? 153 SER B HB2    1 
ATOM   4989  H  HB3    . SER B 2 154 ? 20.892  12.520  23.446  1.00 26.89  ? 153 SER B HB3    1 
ATOM   4990  H  HG     . SER B 2 154 ? 20.497  10.717  24.589  1.00 27.85  ? 153 SER B HG     1 
ATOM   4991  N  N      . LYS B 2 155 ? 22.248  9.370   20.918  1.00 25.50  ? 154 LYS B N      1 
ATOM   4992  C  CA     . LYS B 2 155 ? 23.103  8.274   20.485  1.00 27.27  ? 154 LYS B CA     1 
ATOM   4993  C  C      . LYS B 2 155 ? 22.645  7.869   19.083  1.00 27.95  ? 154 LYS B C      1 
ATOM   4994  O  O      . LYS B 2 155 ? 21.538  8.202   18.655  1.00 25.59  ? 154 LYS B O      1 
ATOM   4995  C  CB     . LYS B 2 155 ? 23.036  7.077   21.448  1.00 29.00  ? 154 LYS B CB     1 
ATOM   4996  C  CG     . LYS B 2 155 ? 23.523  7.389   22.893  1.00 29.23  ? 154 LYS B CG     1 
ATOM   4997  C  CD     . LYS B 2 155 ? 23.657  6.129   23.736  1.00 32.02  ? 154 LYS B CD     1 
ATOM   4998  C  CE     . LYS B 2 155 ? 24.076  6.489   25.153  1.00 37.25  ? 154 LYS B CE     1 
ATOM   4999  N  NZ     . LYS B 2 155 ? 25.413  7.179   25.122  1.00 40.89  ? 154 LYS B NZ     1 
ATOM   5000  H  H      . LYS B 2 155 ? 21.422  9.248   20.711  1.00 30.63  ? 154 LYS B H      1 
ATOM   5001  H  HA     . LYS B 2 155 ? 24.030  8.556   20.449  1.00 32.76  ? 154 LYS B HA     1 
ATOM   5002  H  HB2    . LYS B 2 155 ? 22.115  6.779   21.507  1.00 34.83  ? 154 LYS B HB2    1 
ATOM   5003  H  HB3    . LYS B 2 155 ? 23.594  6.366   21.097  1.00 34.83  ? 154 LYS B HB3    1 
ATOM   5004  H  HG2    . LYS B 2 155 ? 24.392  7.819   22.851  1.00 35.10  ? 154 LYS B HG2    1 
ATOM   5005  H  HG3    . LYS B 2 155 ? 22.884  7.976   23.326  1.00 35.10  ? 154 LYS B HG3    1 
ATOM   5006  H  HD2    . LYS B 2 155 ? 22.804  5.668   23.771  1.00 38.46  ? 154 LYS B HD2    1 
ATOM   5007  H  HD3    . LYS B 2 155 ? 24.332  5.548   23.351  1.00 38.46  ? 154 LYS B HD3    1 
ATOM   5008  H  HE2    . LYS B 2 155 ? 23.422  7.088   25.547  1.00 44.73  ? 154 LYS B HE2    1 
ATOM   5009  H  HE3    . LYS B 2 155 ? 24.151  5.683   25.688  1.00 44.73  ? 154 LYS B HE3    1 
ATOM   5010  H  HZ1    . LYS B 2 155 ? 25.711  7.305   25.952  1.00 49.11  ? 154 LYS B HZ1    1 
ATOM   5011  H  HZ2    . LYS B 2 155 ? 26.002  6.682   24.676  1.00 49.11  ? 154 LYS B HZ2    1 
ATOM   5012  H  HZ3    . LYS B 2 155 ? 25.339  7.969   24.719  1.00 49.11  ? 154 LYS B HZ3    1 
ATOM   5013  N  N      . LYS B 2 156 ? 23.503  7.140   18.371  1.00 29.26  ? 155 LYS B N      1 
ATOM   5014  C  CA     . LYS B 2 156 ? 23.175  6.656   17.027  1.00 25.88  ? 155 LYS B CA     1 
ATOM   5015  C  C      . LYS B 2 156 ? 22.327  5.396   17.121  1.00 26.27  ? 155 LYS B C      1 
ATOM   5016  O  O      . LYS B 2 156 ? 22.818  4.329   17.505  1.00 24.37  ? 155 LYS B O      1 
ATOM   5017  C  CB     . LYS B 2 156 ? 24.456  6.380   16.241  1.00 33.23  ? 155 LYS B CB     1 
ATOM   5018  C  CG     . LYS B 2 156 ? 24.749  7.409   15.158  1.00 39.59  ? 155 LYS B CG     1 
ATOM   5019  C  CD     . LYS B 2 156 ? 25.746  6.908   14.103  1.00 42.00  ? 155 LYS B CD     1 
ATOM   5020  C  CE     . LYS B 2 156 ? 25.131  5.900   13.130  1.00 49.42  ? 155 LYS B CE     1 
ATOM   5021  N  NZ     . LYS B 2 156 ? 23.869  6.402   12.465  1.00 45.87  ? 155 LYS B NZ     1 
ATOM   5022  H  H      . LYS B 2 156 ? 24.285  6.910   18.644  1.00 35.14  ? 155 LYS B H      1 
ATOM   5023  H  HA     . LYS B 2 156 ? 22.657  7.336   16.569  1.00 31.09  ? 155 LYS B HA     1 
ATOM   5024  H  HB2    . LYS B 2 156 ? 25.205  6.379   16.858  1.00 39.92  ? 155 LYS B HB2    1 
ATOM   5025  H  HB3    . LYS B 2 156 ? 24.378  5.513   15.813  1.00 39.92  ? 155 LYS B HB3    1 
ATOM   5026  H  HG2    . LYS B 2 156 ? 23.922  7.632   14.703  1.00 47.54  ? 155 LYS B HG2    1 
ATOM   5027  H  HG3    . LYS B 2 156 ? 25.125  8.202   15.570  1.00 47.54  ? 155 LYS B HG3    1 
ATOM   5028  H  HD2    . LYS B 2 156 ? 26.066  7.664   13.587  1.00 50.44  ? 155 LYS B HD2    1 
ATOM   5029  H  HD3    . LYS B 2 156 ? 26.489  6.475   14.551  1.00 50.44  ? 155 LYS B HD3    1 
ATOM   5030  H  HE2    . LYS B 2 156 ? 25.776  5.703   12.432  1.00 59.34  ? 155 LYS B HE2    1 
ATOM   5031  H  HE3    . LYS B 2 156 ? 24.909  5.090   13.615  1.00 59.34  ? 155 LYS B HE3    1 
ATOM   5032  H  HZ1    . LYS B 2 156 ? 23.581  5.806   11.870  1.00 55.08  ? 155 LYS B HZ1    1 
ATOM   5033  H  HZ2    . LYS B 2 156 ? 23.234  6.531   13.076  1.00 55.08  ? 155 LYS B HZ2    1 
ATOM   5034  H  HZ3    . LYS B 2 156 ? 24.030  7.172   12.049  1.00 55.08  ? 155 LYS B HZ3    1 
ATOM   5035  N  N      . ILE B 2 157 ? 21.049  5.490   16.736  1.00 21.60  ? 156 ILE B N      1 
ATOM   5036  C  CA     . ILE B 2 157 ? 20.123  4.381   16.849  1.00 21.60  ? 156 ILE B CA     1 
ATOM   5037  C  C      . ILE B 2 157 ? 19.966  3.758   15.480  1.00 23.57  ? 156 ILE B C      1 
ATOM   5038  O  O      . ILE B 2 157 ? 19.298  4.331   14.603  1.00 19.85  ? 156 ILE B O      1 
ATOM   5039  C  CB     . ILE B 2 157 ? 18.755  4.820   17.381  1.00 21.81  ? 156 ILE B CB     1 
ATOM   5040  C  CG1    . ILE B 2 157 ? 18.911  5.692   18.651  1.00 22.16  ? 156 ILE B CG1    1 
ATOM   5041  C  CG2    . ILE B 2 157 ? 17.919  3.568   17.565  1.00 22.10  ? 156 ILE B CG2    1 
ATOM   5042  C  CD1    . ILE B 2 157 ? 19.700  5.040   19.733  1.00 26.42  ? 156 ILE B CD1    1 
ATOM   5043  H  H      . ILE B 2 157 ? 20.699  6.201   16.403  1.00 25.96  ? 156 ILE B H      1 
ATOM   5044  H  HA     . ILE B 2 157 ? 20.507  3.730   17.457  1.00 25.95  ? 156 ILE B HA     1 
ATOM   5045  H  HB     . ILE B 2 157 ? 18.293  5.399   16.754  1.00 26.20  ? 156 ILE B HB     1 
ATOM   5046  H  HG12   . ILE B 2 157 ? 19.363  6.516   18.411  1.00 26.62  ? 156 ILE B HG12   1 
ATOM   5047  H  HG13   . ILE B 2 157 ? 18.029  5.889   19.005  1.00 26.62  ? 156 ILE B HG13   1 
ATOM   5048  H  HG21   . ILE B 2 157 ? 17.140  3.784   18.102  1.00 26.56  ? 156 ILE B HG21   1 
ATOM   5049  H  HG22   . ILE B 2 157 ? 17.640  3.243   16.694  1.00 26.56  ? 156 ILE B HG22   1 
ATOM   5050  H  HG23   . ILE B 2 157 ? 18.453  2.894   18.013  1.00 26.56  ? 156 ILE B HG23   1 
ATOM   5051  H  HD11   . ILE B 2 157 ? 19.651  5.586   20.532  1.00 31.74  ? 156 ILE B HD11   1 
ATOM   5052  H  HD12   . ILE B 2 157 ? 19.328  4.161   19.909  1.00 31.74  ? 156 ILE B HD12   1 
ATOM   5053  H  HD13   . ILE B 2 157 ? 20.622  4.956   19.444  1.00 31.74  ? 156 ILE B HD13   1 
ATOM   5054  N  N      . THR B 2 158 ? 20.485  2.551   15.310  1.00 22.29  ? 157 THR B N      1 
ATOM   5055  C  CA     . THR B 2 158 ? 20.528  1.957   13.975  1.00 18.93  ? 157 THR B CA     1 
ATOM   5056  C  C      . THR B 2 158 ? 19.722  0.685   13.840  1.00 21.31  ? 157 THR B C      1 
ATOM   5057  O  O      . THR B 2 158 ? 19.492  -0.052  14.795  1.00 21.87  ? 157 THR B O      1 
ATOM   5058  C  CB     . THR B 2 158 ? 21.986  1.669   13.569  1.00 22.51  ? 157 THR B CB     1 
ATOM   5059  O  OG1    . THR B 2 158 ? 22.575  0.853   14.580  1.00 26.45  ? 157 THR B OG1    1 
ATOM   5060  C  CG2    . THR B 2 158 ? 22.744  2.959   13.413  1.00 25.10  ? 157 THR B CG2    1 
ATOM   5061  H  H      . THR B 2 158 ? 20.814  2.064   15.938  1.00 26.78  ? 157 THR B H      1 
ATOM   5062  H  HA     . THR B 2 158 ? 20.115  2.590   13.367  1.00 22.75  ? 157 THR B HA     1 
ATOM   5063  H  HB     . THR B 2 158 ? 22.029  1.207   12.718  1.00 27.05  ? 157 THR B HB     1 
ATOM   5064  H  HG1    . THR B 2 158 ? 23.377  0.695   14.390  1.00 31.77  ? 157 THR B HG1    1 
ATOM   5065  H  HG21   . THR B 2 158 ? 23.653  2.777   13.127  1.00 30.16  ? 157 THR B HG21   1 
ATOM   5066  H  HG22   . THR B 2 158 ? 22.312  3.520   12.750  1.00 30.16  ? 157 THR B HG22   1 
ATOM   5067  H  HG23   . THR B 2 158 ? 22.769  3.434   14.259  1.00 30.16  ? 157 THR B HG23   1 
ATOM   5068  N  N      . ILE B 2 159 ? 19.271  0.432   12.604  1.00 18.32  ? 158 ILE B N      1 
ATOM   5069  C  CA     . ILE B 2 159 ? 18.756  -0.870  12.224  1.00 20.14  ? 158 ILE B CA     1 
ATOM   5070  C  C      . ILE B 2 159 ? 19.985  -1.676  11.815  1.00 25.89  ? 158 ILE B C      1 
ATOM   5071  O  O      . ILE B 2 159 ? 20.448  -1.604  10.688  1.00 24.49  ? 158 ILE B O      1 
ATOM   5072  C  CB     . ILE B 2 159 ? 17.728  -0.767  11.105  1.00 19.09  ? 158 ILE B CB     1 
ATOM   5073  C  CG1    . ILE B 2 159 ? 16.527  0.104   11.572  1.00 19.46  ? 158 ILE B CG1    1 
ATOM   5074  C  CG2    . ILE B 2 159 ? 17.203  -2.116  10.683  1.00 17.92  ? 158 ILE B CG2    1 
ATOM   5075  C  CD1    . ILE B 2 159 ? 15.683  0.581   10.368  1.00 19.67  ? 158 ILE B CD1    1 
ATOM   5076  H  H      . ILE B 2 159 ? 19.258  1.011   11.968  1.00 22.02  ? 158 ILE B H      1 
ATOM   5077  H  HA     . ILE B 2 159 ? 18.330  -1.299  12.983  1.00 24.20  ? 158 ILE B HA     1 
ATOM   5078  H  HB     . ILE B 2 159 ? 18.178  -0.362  10.348  1.00 22.94  ? 158 ILE B HB     1 
ATOM   5079  H  HG12   . ILE B 2 159 ? 15.958  -0.420  12.158  1.00 23.39  ? 158 ILE B HG12   1 
ATOM   5080  H  HG13   . ILE B 2 159 ? 16.859  0.884   12.043  1.00 23.39  ? 158 ILE B HG13   1 
ATOM   5081  H  HG21   . ILE B 2 159 ? 16.572  -1.995  9.957   1.00 21.54  ? 158 ILE B HG21   1 
ATOM   5082  H  HG22   . ILE B 2 159 ? 17.946  -2.665  10.388  1.00 21.54  ? 158 ILE B HG22   1 
ATOM   5083  H  HG23   . ILE B 2 159 ? 16.762  -2.533  11.439  1.00 21.54  ? 158 ILE B HG23   1 
ATOM   5084  H  HD11   . ILE B 2 159 ? 15.038  1.237   10.675  1.00 23.64  ? 158 ILE B HD11   1 
ATOM   5085  H  HD12   . ILE B 2 159 ? 16.272  0.980   9.708   1.00 23.64  ? 158 ILE B HD12   1 
ATOM   5086  H  HD13   . ILE B 2 159 ? 15.223  -0.181  9.983   1.00 23.64  ? 158 ILE B HD13   1 
ATOM   5087  N  N      . ALA B 2 160 ? 20.551  -2.414  12.770  1.00 23.69  ? 159 ALA B N      1 
ATOM   5088  C  CA     . ALA B 2 160 ? 21.788  -3.128  12.502  1.00 25.21  ? 159 ALA B CA     1 
ATOM   5089  C  C      . ALA B 2 160 ? 21.562  -4.280  11.545  1.00 27.94  ? 159 ALA B C      1 
ATOM   5090  O  O      . ALA B 2 160 ? 22.478  -4.650  10.798  1.00 31.87  ? 159 ALA B O      1 
ATOM   5091  C  CB     . ALA B 2 160 ? 22.395  -3.622  13.824  1.00 28.76  ? 159 ALA B CB     1 
ATOM   5092  H  H      . ALA B 2 160 ? 20.242  -2.514  13.566  1.00 28.47  ? 159 ALA B H      1 
ATOM   5093  H  HA     . ALA B 2 160 ? 22.428  -2.525  12.090  1.00 30.29  ? 159 ALA B HA     1 
ATOM   5094  H  HB1    . ALA B 2 160 ? 23.205  -4.120  13.634  1.00 34.55  ? 159 ALA B HB1    1 
ATOM   5095  H  HB2    . ALA B 2 160 ? 22.601  -2.856  14.383  1.00 34.55  ? 159 ALA B HB2    1 
ATOM   5096  H  HB3    . ALA B 2 160 ? 21.752  -4.194  14.272  1.00 34.55  ? 159 ALA B HB3    1 
ATOM   5097  N  N      . ASP B 2 161 ? 20.369  -4.875  11.570  1.00 27.67  ? 160 ASP B N      1 
ATOM   5098  C  CA     . ASP B 2 161 ? 19.970  -5.927  10.650  1.00 29.43  ? 160 ASP B CA     1 
ATOM   5099  C  C      . ASP B 2 161 ? 18.456  -5.906  10.551  1.00 26.31  ? 160 ASP B C      1 
ATOM   5100  O  O      . ASP B 2 161 ? 17.765  -5.383  11.425  1.00 25.72  ? 160 ASP B O      1 
ATOM   5101  C  CB     . ASP B 2 161 ? 20.463  -7.302  11.113  1.00 29.69  ? 160 ASP B CB     1 
ATOM   5102  C  CG     . ASP B 2 161 ? 20.455  -8.349  9.999   1.00 35.06  ? 160 ASP B CG     1 
ATOM   5103  O  OD1    . ASP B 2 161 ? 20.171  -8.021  8.824   1.00 30.30  ? 160 ASP B OD1    1 
ATOM   5104  O  OD2    . ASP B 2 161 ? 20.737  -9.517  10.318  1.00 36.45  ? 160 ASP B OD2    1 
ATOM   5105  H  H      . ASP B 2 161 ? 19.751  -4.676  12.134  1.00 33.23  ? 160 ASP B H      1 
ATOM   5106  H  HA     . ASP B 2 161 ? 20.348  -5.757  9.773   1.00 35.35  ? 160 ASP B HA     1 
ATOM   5107  H  HB2    . ASP B 2 161 ? 21.373  -7.218  11.438  1.00 35.66  ? 160 ASP B HB2    1 
ATOM   5108  H  HB3    . ASP B 2 161 ? 19.885  -7.620  11.825  1.00 35.66  ? 160 ASP B HB3    1 
ATOM   5109  N  N      . CYS B 2 162 ? 17.944  -6.473  9.470   1.00 27.36  ? 161 CYS B N      1 
ATOM   5110  C  CA     . CYS B 2 162 ? 16.506  -6.502  9.273   1.00 29.08  ? 161 CYS B CA     1 
ATOM   5111  C  C      . CYS B 2 162 ? 16.231  -7.487  8.153   1.00 28.82  ? 161 CYS B C      1 
ATOM   5112  O  O      . CYS B 2 162 ? 17.108  -7.793  7.339   1.00 30.95  ? 161 CYS B O      1 
ATOM   5113  C  CB     . CYS B 2 162 ? 15.935  -5.109  8.951   1.00 27.57  ? 161 CYS B CB     1 
ATOM   5114  S  SG     . CYS B 2 162 ? 16.779  -4.202  7.590   1.00 26.43  ? 161 CYS B SG     1 
ATOM   5115  H  H      . CYS B 2 162 ? 18.403  -6.843  8.845   1.00 32.87  ? 161 CYS B H      1 
ATOM   5116  H  HA     . CYS B 2 162 ? 16.062  -6.809  10.079  1.00 34.93  ? 161 CYS B HA     1 
ATOM   5117  H  HB2    . CYS B 2 162 ? 15.005  -5.213  8.696   1.00 33.12  ? 161 CYS B HB2    1 
ATOM   5118  H  HB3    . CYS B 2 162 ? 16.002  -4.561  9.748   1.00 33.12  ? 161 CYS B HB3    1 
ATOM   5119  H  HG     . CYS B 2 162 ? 16.784  -4.889  6.606   1.00 31.75  ? 161 CYS B HG     1 
ATOM   5120  N  N      . GLY B 2 163 ? 15.015  -8.001  8.161   1.00 23.31  ? 162 GLY B N      1 
ATOM   5121  C  CA     . GLY B 2 163 ? 14.565  -8.931  7.151   1.00 29.84  ? 162 GLY B CA     1 
ATOM   5122  C  C      . GLY B 2 163 ? 13.162  -9.402  7.447   1.00 29.03  ? 162 GLY B C      1 
ATOM   5123  O  O      . GLY B 2 163 ? 12.444  -8.824  8.268   1.00 29.09  ? 162 GLY B O      1 
ATOM   5124  H  H      . GLY B 2 163 ? 14.418  -7.823  8.753   1.00 28.00  ? 162 GLY B H      1 
ATOM   5125  H  HA2    . GLY B 2 163 ? 14.573  -8.501  6.282   1.00 35.85  ? 162 GLY B HA2    1 
ATOM   5126  H  HA3    . GLY B 2 163 ? 15.155  -9.701  7.128   1.00 35.85  ? 162 GLY B HA3    1 
ATOM   5127  N  N      . GLN B 2 164 ? 12.766  -10.438 6.716   1.00 28.12  ? 163 GLN B N      1 
ATOM   5128  C  CA     . GLN B 2 164 ? 11.459  -11.062 6.847   1.00 28.24  ? 163 GLN B CA     1 
ATOM   5129  C  C      . GLN B 2 164 ? 11.552  -12.360 7.633   1.00 37.27  ? 163 GLN B C      1 
ATOM   5130  O  O      . GLN B 2 164 ? 12.530  -13.103 7.516   1.00 34.53  ? 163 GLN B O      1 
ATOM   5131  C  CB     . GLN B 2 164 ? 10.864  -11.361 5.464   1.00 32.82  ? 163 GLN B CB     1 
ATOM   5132  C  CG     . GLN B 2 164 ? 9.413   -11.819 5.481   1.00 34.06  ? 163 GLN B CG     1 
ATOM   5133  C  CD     . GLN B 2 164 ? 8.799   -11.846 4.102   1.00 29.90  ? 163 GLN B CD     1 
ATOM   5134  O  OE1    . GLN B 2 164 ? 9.467   -11.562 3.114   1.00 32.97  ? 163 GLN B OE1    1 
ATOM   5135  N  NE2    . GLN B 2 164 ? 7.513   -12.172 4.024   1.00 33.10  ? 163 GLN B NE2    1 
ATOM   5136  H  H      . GLN B 2 164 ? 13.256  -10.809 6.116   1.00 33.77  ? 163 GLN B H      1 
ATOM   5137  H  HA     . GLN B 2 164 ? 10.872  -10.457 7.328   1.00 33.92  ? 163 GLN B HA     1 
ATOM   5138  H  HB2    . GLN B 2 164 ? 10.908  -10.553 4.928   1.00 39.41  ? 163 GLN B HB2    1 
ATOM   5139  H  HB3    . GLN B 2 164 ? 11.387  -12.064 5.048   1.00 39.41  ? 163 GLN B HB3    1 
ATOM   5140  H  HG2    . GLN B 2 164 ? 9.368   -12.716 5.848   1.00 40.90  ? 163 GLN B HG2    1 
ATOM   5141  H  HG3    . GLN B 2 164 ? 8.894   -11.210 6.030   1.00 40.90  ? 163 GLN B HG3    1 
ATOM   5142  H  HE21   . GLN B 2 164 ? 7.072   -12.355 4.739   1.00 39.76  ? 163 GLN B HE21   1 
ATOM   5143  H  HE22   . GLN B 2 164 ? 7.122   -12.201 3.258   1.00 39.76  ? 163 GLN B HE22   1 
ATOM   5144  N  N      . LEU B 2 165 ? 10.520  -12.615 8.423   1.00 33.61  ? 164 LEU B N      1 
ATOM   5145  C  CA     . LEU B 2 165 ? 10.409  -13.794 9.250   1.00 39.50  ? 164 LEU B CA     1 
ATOM   5146  C  C      . LEU B 2 165 ? 9.532   -14.805 8.513   1.00 37.26  ? 164 LEU B C      1 
ATOM   5147  O  O      . LEU B 2 165 ? 8.526   -14.415 7.880   1.00 40.51  ? 164 LEU B O      1 
ATOM   5148  C  CB     . LEU B 2 165 ? 9.825   -13.405 10.608  1.00 33.55  ? 164 LEU B CB     1 
ATOM   5149  C  CG     . LEU B 2 165 ? 10.700  -12.545 11.508  1.00 37.96  ? 164 LEU B CG     1 
ATOM   5150  C  CD1    . LEU B 2 165 ? 9.897   -12.122 12.714  1.00 36.79  ? 164 LEU B CD1    1 
ATOM   5151  C  CD2    . LEU B 2 165 ? 11.953  -13.286 11.974  1.00 35.22  ? 164 LEU B CD2    1 
ATOM   5152  H  H      . LEU B 2 165 ? 9.841   -12.093 8.499   1.00 40.37  ? 164 LEU B H      1 
ATOM   5153  H  HA     . LEU B 2 165 ? 11.268  -14.207 9.428   1.00 47.44  ? 164 LEU B HA     1 
ATOM   5154  H  HB2    . LEU B 2 165 ? 9.006   -12.910 10.451  1.00 40.29  ? 164 LEU B HB2    1 
ATOM   5155  H  HB3    . LEU B 2 165 ? 9.631   -14.221 11.096  1.00 40.29  ? 164 LEU B HB3    1 
ATOM   5156  H  HG     . LEU B 2 165 ? 10.993  -11.770 11.003  1.00 45.59  ? 164 LEU B HG     1 
ATOM   5157  H  HD11   . LEU B 2 165 ? 10.467  -12.149 13.498  1.00 44.18  ? 164 LEU B HD11   1 
ATOM   5158  H  HD12   . LEU B 2 165 ? 9.569   -11.220 12.575  1.00 44.18  ? 164 LEU B HD12   1 
ATOM   5159  H  HD13   . LEU B 2 165 ? 9.151   -12.732 12.826  1.00 44.18  ? 164 LEU B HD13   1 
ATOM   5160  H  HD21   . LEU B 2 165 ? 12.458  -12.710 12.569  1.00 42.30  ? 164 LEU B HD21   1 
ATOM   5161  H  HD22   . LEU B 2 165 ? 11.687  -14.093 12.442  1.00 42.30  ? 164 LEU B HD22   1 
ATOM   5162  H  HD23   . LEU B 2 165 ? 12.491  -13.515 11.199  1.00 42.30  ? 164 LEU B HD23   1 
ATOM   5163  N  N      . VAL C 2 3   ? 61.524  33.680  26.374  1.00 41.53  ? 2   VAL D N      1 
ATOM   5164  C  CA     . VAL C 2 3   ? 60.796  34.149  25.208  1.00 43.80  ? 2   VAL D CA     1 
ATOM   5165  C  C      . VAL C 2 3   ? 59.483  33.394  25.074  1.00 37.07  ? 2   VAL D C      1 
ATOM   5166  O  O      . VAL C 2 3   ? 59.402  32.197  25.338  1.00 37.14  ? 2   VAL D O      1 
ATOM   5167  C  CB     . VAL C 2 3   ? 61.608  33.982  23.918  1.00 47.58  ? 2   VAL D CB     1 
ATOM   5168  C  CG1    . VAL C 2 3   ? 61.404  32.579  23.340  1.00 44.93  ? 2   VAL D CG1    1 
ATOM   5169  C  CG2    . VAL C 2 3   ? 61.179  35.019  22.884  1.00 45.43  ? 2   VAL D CG2    1 
ATOM   5170  H  HA     . VAL C 2 3   ? 60.618  35.094  25.333  1.00 52.60  ? 2   VAL D HA     1 
ATOM   5171  H  HB     . VAL C 2 3   ? 62.547  34.109  24.125  1.00 57.12  ? 2   VAL D HB     1 
ATOM   5172  H  HG11   . VAL C 2 3   ? 62.097  32.404  22.684  1.00 53.96  ? 2   VAL D HG11   1 
ATOM   5173  H  HG12   . VAL C 2 3   ? 61.458  31.930  24.059  1.00 53.96  ? 2   VAL D HG12   1 
ATOM   5174  H  HG13   . VAL C 2 3   ? 60.531  32.535  22.919  1.00 53.96  ? 2   VAL D HG13   1 
ATOM   5175  H  HG21   . VAL C 2 3   ? 61.632  34.835  22.046  1.00 54.55  ? 2   VAL D HG21   1 
ATOM   5176  H  HG22   . VAL C 2 3   ? 60.218  34.964  22.760  1.00 54.55  ? 2   VAL D HG22   1 
ATOM   5177  H  HG23   . VAL C 2 3   ? 61.421  35.903  23.203  1.00 54.55  ? 2   VAL D HG23   1 
ATOM   5178  N  N      . ASN C 2 4   ? 58.470  34.081  24.611  1.00 34.34  ? 3   ASN D N      1 
ATOM   5179  C  CA     . ASN C 2 4   ? 57.160  33.457  24.488  1.00 35.42  ? 3   ASN D CA     1 
ATOM   5180  C  C      . ASN C 2 4   ? 57.121  32.574  23.242  1.00 36.20  ? 3   ASN D C      1 
ATOM   5181  O  O      . ASN C 2 4   ? 57.326  33.075  22.130  1.00 37.80  ? 3   ASN D O      1 
ATOM   5182  C  CB     . ASN C 2 4   ? 56.096  34.536  24.454  1.00 32.05  ? 3   ASN D CB     1 
ATOM   5183  C  CG     . ASN C 2 4   ? 55.882  35.178  25.819  1.00 35.34  ? 3   ASN D CG     1 
ATOM   5184  O  OD1    . ASN C 2 4   ? 56.404  34.689  26.828  1.00 33.26  ? 3   ASN D OD1    1 
ATOM   5185  N  ND2    . ASN C 2 4   ? 55.143  36.292  25.855  1.00 33.85  ? 3   ASN D ND2    1 
ATOM   5186  H  H      . ASN C 2 4   ? 58.504  34.903  24.362  1.00 41.25  ? 3   ASN D H      1 
ATOM   5187  H  HA     . ASN C 2 4   ? 56.976  32.879  25.244  1.00 42.54  ? 3   ASN D HA     1 
ATOM   5188  H  HB2    . ASN C 2 4   ? 56.366  35.229  23.832  1.00 38.49  ? 3   ASN D HB2    1 
ATOM   5189  H  HB3    . ASN C 2 4   ? 55.255  34.144  24.170  1.00 38.49  ? 3   ASN D HB3    1 
ATOM   5190  H  HD21   . ASN C 2 4   ? 54.997  36.687  26.605  1.00 40.66  ? 3   ASN D HD21   1 
ATOM   5191  H  HD22   . ASN C 2 4   ? 54.812  36.612  25.129  1.00 40.66  ? 3   ASN D HD22   1 
ATOM   5192  N  N      . PRO C 2 5   ? 56.905  31.274  23.381  1.00 33.08  ? 4   PRO D N      1 
ATOM   5193  C  CA     . PRO C 2 5   ? 56.799  30.408  22.199  1.00 34.84  ? 4   PRO D CA     1 
ATOM   5194  C  C      . PRO C 2 5   ? 55.450  30.557  21.515  1.00 33.56  ? 4   PRO D C      1 
ATOM   5195  O  O      . PRO C 2 5   ? 54.505  31.103  22.072  1.00 28.90  ? 4   PRO D O      1 
ATOM   5196  C  CB     . PRO C 2 5   ? 56.973  29.001  22.780  1.00 36.66  ? 4   PRO D CB     1 
ATOM   5197  C  CG     . PRO C 2 5   ? 56.404  29.121  24.191  1.00 34.93  ? 4   PRO D CG     1 
ATOM   5198  C  CD     . PRO C 2 5   ? 56.667  30.535  24.636  1.00 31.94  ? 4   PRO D CD     1 
ATOM   5199  H  HA     . PRO C 2 5   ? 57.509  30.595  21.565  1.00 41.84  ? 4   PRO D HA     1 
ATOM   5200  H  HB2    . PRO C 2 5   ? 56.474  28.356  22.254  1.00 44.02  ? 4   PRO D HB2    1 
ATOM   5201  H  HB3    . PRO C 2 5   ? 57.912  28.758  22.799  1.00 44.02  ? 4   PRO D HB3    1 
ATOM   5202  H  HG2    . PRO C 2 5   ? 55.451  28.940  24.174  1.00 41.95  ? 4   PRO D HG2    1 
ATOM   5203  H  HG3    . PRO C 2 5   ? 56.851  28.490  24.777  1.00 41.95  ? 4   PRO D HG3    1 
ATOM   5204  H  HD2    . PRO C 2 5   ? 55.896  30.895  25.102  1.00 38.37  ? 4   PRO D HD2    1 
ATOM   5205  H  HD3    . PRO C 2 5   ? 57.449  30.574  25.208  1.00 38.37  ? 4   PRO D HD3    1 
ATOM   5206  N  N      . THR C 2 6   ? 55.387  30.049  20.275  1.00 31.76  ? 5   THR D N      1 
ATOM   5207  C  CA     . THR C 2 6   ? 54.178  30.060  19.471  1.00 29.59  ? 5   THR D CA     1 
ATOM   5208  C  C      . THR C 2 6   ? 53.881  28.638  19.039  1.00 34.87  ? 5   THR D C      1 
ATOM   5209  O  O      . THR C 2 6   ? 54.782  27.910  18.623  1.00 32.82  ? 5   THR D O      1 
ATOM   5210  C  CB     . THR C 2 6   ? 54.305  30.966  18.258  1.00 32.64  ? 5   THR D CB     1 
ATOM   5211  O  OG1    . THR C 2 6   ? 54.532  32.309  18.692  1.00 33.99  ? 5   THR D OG1    1 
ATOM   5212  C  CG2    . THR C 2 6   ? 53.051  30.928  17.427  1.00 32.92  ? 5   THR D CG2    1 
ATOM   5213  H  H      . THR C 2 6   ? 56.056  29.684  19.876  1.00 38.14  ? 5   THR D H      1 
ATOM   5214  H  HA     . THR C 2 6   ? 53.434  30.394  19.997  1.00 35.55  ? 5   THR D HA     1 
ATOM   5215  H  HB     . THR C 2 6   ? 55.045  30.665  17.709  1.00 39.21  ? 5   THR D HB     1 
ATOM   5216  H  HG1    . THR C 2 6   ? 54.780  32.782  18.044  1.00 40.82  ? 5   THR D HG1    1 
ATOM   5217  H  HG21   . THR C 2 6   ? 53.061  31.649  16.778  1.00 39.53  ? 5   THR D HG21   1 
ATOM   5218  H  HG22   . THR C 2 6   ? 52.990  30.082  16.957  1.00 39.53  ? 5   THR D HG22   1 
ATOM   5219  H  HG23   . THR C 2 6   ? 52.272  31.028  17.997  1.00 39.53  ? 5   THR D HG23   1 
ATOM   5220  N  N      . VAL C 2 7   ? 52.608  28.252  19.134  1.00 31.66  ? 6   VAL D N      1 
ATOM   5221  C  CA     . VAL C 2 7   ? 52.154  26.919  18.771  1.00 29.99  ? 6   VAL D CA     1 
ATOM   5222  C  C      . VAL C 2 7   ? 50.951  27.084  17.853  1.00 31.96  ? 6   VAL D C      1 
ATOM   5223  O  O      . VAL C 2 7   ? 50.378  28.173  17.732  1.00 28.69  ? 6   VAL D O      1 
ATOM   5224  C  CB     . VAL C 2 7   ? 51.824  26.054  20.008  1.00 30.30  ? 6   VAL D CB     1 
ATOM   5225  C  CG1    . VAL C 2 7   ? 53.048  25.970  20.936  1.00 35.75  ? 6   VAL D CG1    1 
ATOM   5226  C  CG2    . VAL C 2 7   ? 50.648  26.604  20.780  1.00 30.39  ? 6   VAL D CG2    1 
ATOM   5227  H  H      . VAL C 2 7   ? 51.975  28.762  19.415  1.00 38.03  ? 6   VAL D H      1 
ATOM   5228  H  HA     . VAL C 2 7   ? 52.844  26.446  18.280  1.00 36.02  ? 6   VAL D HA     1 
ATOM   5229  H  HB     . VAL C 2 7   ? 51.588  25.166  19.696  1.00 36.39  ? 6   VAL D HB     1 
ATOM   5230  H  HG11   . VAL C 2 7   ? 52.841  25.383  21.679  1.00 42.94  ? 6   VAL D HG11   1 
ATOM   5231  H  HG12   . VAL C 2 7   ? 53.800  25.618  20.435  1.00 42.94  ? 6   VAL D HG12   1 
ATOM   5232  H  HG13   . VAL C 2 7   ? 53.257  26.859  21.264  1.00 42.94  ? 6   VAL D HG13   1 
ATOM   5233  H  HG21   . VAL C 2 7   ? 50.574  26.129  21.623  1.00 36.50  ? 6   VAL D HG21   1 
ATOM   5234  H  HG22   . VAL C 2 7   ? 50.792  27.549  20.944  1.00 36.50  ? 6   VAL D HG22   1 
ATOM   5235  H  HG23   . VAL C 2 7   ? 49.841  26.478  20.257  1.00 36.50  ? 6   VAL D HG23   1 
ATOM   5236  N  N      . PHE C 2 8   ? 50.623  26.011  17.142  1.00 30.63  ? 7   PHE D N      1 
ATOM   5237  C  CA     . PHE C 2 8   ? 49.539  26.041  16.173  1.00 29.73  ? 7   PHE D CA     1 
ATOM   5238  C  C      . PHE C 2 8   ? 48.685  24.793  16.308  1.00 28.20  ? 7   PHE D C      1 
ATOM   5239  O  O      . PHE C 2 8   ? 49.183  23.718  16.656  1.00 28.48  ? 7   PHE D O      1 
ATOM   5240  C  CB     . PHE C 2 8   ? 50.071  26.140  14.735  1.00 33.11  ? 7   PHE D CB     1 
ATOM   5241  C  CG     . PHE C 2 8   ? 50.683  24.858  14.227  1.00 34.35  ? 7   PHE D CG     1 
ATOM   5242  C  CD1    . PHE C 2 8   ? 49.885  23.877  13.646  1.00 34.35  ? 7   PHE D CD1    1 
ATOM   5243  C  CD2    . PHE C 2 8   ? 52.044  24.629  14.331  1.00 34.81  ? 7   PHE D CD2    1 
ATOM   5244  C  CE1    . PHE C 2 8   ? 50.452  22.681  13.189  1.00 35.86  ? 7   PHE D CE1    1 
ATOM   5245  C  CE2    . PHE C 2 8   ? 52.609  23.456  13.868  1.00 36.78  ? 7   PHE D CE2    1 
ATOM   5246  C  CZ     . PHE C 2 8   ? 51.799  22.476  13.291  1.00 33.91  ? 7   PHE D CZ     1 
ATOM   5247  H  H      . PHE C 2 8   ? 51.017  25.249  17.206  1.00 36.79  ? 7   PHE D H      1 
ATOM   5248  H  HA     . PHE C 2 8   ? 48.977  26.810  16.354  1.00 35.71  ? 7   PHE D HA     1 
ATOM   5249  H  HB2    . PHE C 2 8   ? 49.336  26.372  14.145  1.00 39.77  ? 7   PHE D HB2    1 
ATOM   5250  H  HB3    . PHE C 2 8   ? 50.753  26.829  14.701  1.00 39.77  ? 7   PHE D HB3    1 
ATOM   5251  H  HD1    . PHE C 2 8   ? 48.970  24.017  13.560  1.00 41.25  ? 7   PHE D HD1    1 
ATOM   5252  H  HD2    . PHE C 2 8   ? 52.588  25.276  14.718  1.00 41.80  ? 7   PHE D HD2    1 
ATOM   5253  H  HE1    . PHE C 2 8   ? 49.911  22.025  12.814  1.00 43.06  ? 7   PHE D HE1    1 
ATOM   5254  H  HE2    . PHE C 2 8   ? 53.526  23.320  13.941  1.00 44.17  ? 7   PHE D HE2    1 
ATOM   5255  H  HZ     . PHE C 2 8   ? 52.176  21.686  12.978  1.00 40.72  ? 7   PHE D HZ     1 
ATOM   5256  N  N      . PHE C 2 9   ? 47.384  24.980  16.063  1.00 25.55  ? 8   PHE D N      1 
ATOM   5257  C  CA     . PHE C 2 9   ? 46.421  23.921  15.823  1.00 27.84  ? 8   PHE D CA     1 
ATOM   5258  C  C      . PHE C 2 9   ? 45.956  24.024  14.367  1.00 30.17  ? 8   PHE D C      1 
ATOM   5259  O  O      . PHE C 2 9   ? 45.553  25.102  13.918  1.00 25.60  ? 8   PHE D O      1 
ATOM   5260  C  CB     . PHE C 2 9   ? 45.150  24.039  16.663  1.00 26.27  ? 8   PHE D CB     1 
ATOM   5261  C  CG     . PHE C 2 9   ? 45.327  23.884  18.160  1.00 24.19  ? 8   PHE D CG     1 
ATOM   5262  C  CD1    . PHE C 2 9   ? 46.487  23.408  18.721  1.00 24.05  ? 8   PHE D CD1    1 
ATOM   5263  C  CD2    . PHE C 2 9   ? 44.260  24.178  18.981  1.00 28.64  ? 8   PHE D CD2    1 
ATOM   5264  C  CE1    . PHE C 2 9   ? 46.611  23.285  20.084  1.00 26.98  ? 8   PHE D CE1    1 
ATOM   5265  C  CE2    . PHE C 2 9   ? 44.358  24.040  20.366  1.00 27.04  ? 8   PHE D CE2    1 
ATOM   5266  C  CZ     . PHE C 2 9   ? 45.546  23.590  20.911  1.00 24.70  ? 8   PHE D CZ     1 
ATOM   5267  H  H      . PHE C 2 9   ? 47.023  25.759  16.030  1.00 30.69  ? 8   PHE D H      1 
ATOM   5268  H  HA     . PHE C 2 9   ? 46.865  23.084  16.031  1.00 33.45  ? 8   PHE D HA     1 
ATOM   5269  H  HB2    . PHE C 2 9   ? 44.765  24.916  16.509  1.00 31.56  ? 8   PHE D HB2    1 
ATOM   5270  H  HB3    . PHE C 2 9   ? 44.532  23.349  16.375  1.00 31.56  ? 8   PHE D HB3    1 
ATOM   5271  H  HD1    . PHE C 2 9   ? 47.198  23.166  18.171  1.00 28.90  ? 8   PHE D HD1    1 
ATOM   5272  H  HD2    . PHE C 2 9   ? 43.462  24.474  18.606  1.00 34.40  ? 8   PHE D HD2    1 
ATOM   5273  H  HE1    . PHE C 2 9   ? 47.415  22.994  20.452  1.00 32.41  ? 8   PHE D HE1    1 
ATOM   5274  H  HE2    . PHE C 2 9   ? 43.635  24.248  20.913  1.00 32.48  ? 8   PHE D HE2    1 
ATOM   5275  H  HZ     . PHE C 2 9   ? 45.629  23.494  21.833  1.00 29.68  ? 8   PHE D HZ     1 
ATOM   5276  N  N      . ASP C 2 10  ? 45.937  22.918  13.649  1.00 29.34  ? 9   ASP D N      1 
ATOM   5277  C  CA     . ASP C 2 10  ? 45.184  22.847  12.395  1.00 31.54  ? 9   ASP D CA     1 
ATOM   5278  C  C      . ASP C 2 10  ? 43.814  22.249  12.695  1.00 25.87  ? 9   ASP D C      1 
ATOM   5279  O  O      . ASP C 2 10  ? 43.717  21.115  13.170  1.00 31.06  ? 9   ASP D O      1 
ATOM   5280  C  CB     . ASP C 2 10  ? 45.942  22.023  11.363  1.00 28.62  ? 9   ASP D CB     1 
ATOM   5281  C  CG     . ASP C 2 10  ? 47.120  22.766  10.786  1.00 31.48  ? 9   ASP D CG     1 
ATOM   5282  O  OD1    . ASP C 2 10  ? 47.026  23.995  10.615  1.00 34.07  ? 9   ASP D OD1    1 
ATOM   5283  O  OD2    . ASP C 2 10  ? 48.136  22.118  10.498  1.00 37.12  ? 9   ASP D OD2    1 
ATOM   5284  H  H      . ASP C 2 10  ? 46.350  22.194  13.860  1.00 35.24  ? 9   ASP D H      1 
ATOM   5285  H  HA     . ASP C 2 10  ? 45.054  23.734  12.025  1.00 37.89  ? 9   ASP D HA     1 
ATOM   5286  H  HB2    . ASP C 2 10  ? 46.273  21.214  11.784  1.00 34.37  ? 9   ASP D HB2    1 
ATOM   5287  H  HB3    . ASP C 2 10  ? 45.342  21.797  10.635  1.00 34.37  ? 9   ASP D HB3    1 
ATOM   5288  N  N      . ILE C 2 11  ? 42.759  23.001  12.426  1.00 26.35  ? 10  ILE D N      1 
ATOM   5289  C  CA     . ILE C 2 11  ? 41.419  22.634  12.835  1.00 23.49  ? 10  ILE D CA     1 
ATOM   5290  C  C      . ILE C 2 11  ? 40.716  21.955  11.674  1.00 27.29  ? 10  ILE D C      1 
ATOM   5291  O  O      . ILE C 2 11  ? 40.812  22.426  10.526  1.00 26.10  ? 10  ILE D O      1 
ATOM   5292  C  CB     . ILE C 2 11  ? 40.617  23.867  13.293  1.00 23.01  ? 10  ILE D CB     1 
ATOM   5293  C  CG1    . ILE C 2 11  ? 41.320  24.577  14.464  1.00 24.80  ? 10  ILE D CG1    1 
ATOM   5294  C  CG2    . ILE C 2 11  ? 39.200  23.468  13.600  1.00 27.01  ? 10  ILE D CG2    1 
ATOM   5295  C  CD1    . ILE C 2 11  ? 41.398  23.741  15.697  1.00 26.45  ? 10  ILE D CD1    1 
ATOM   5296  H  H      . ILE C 2 11  ? 42.798  23.746  11.999  1.00 31.65  ? 10  ILE D H      1 
ATOM   5297  H  HA     . ILE C 2 11  ? 41.481  22.009  13.575  1.00 28.22  ? 10  ILE D HA     1 
ATOM   5298  H  HB     . ILE C 2 11  ? 40.582  24.516  12.573  1.00 27.64  ? 10  ILE D HB     1 
ATOM   5299  H  HG12   . ILE C 2 11  ? 42.225  24.801  14.197  1.00 29.79  ? 10  ILE D HG12   1 
ATOM   5300  H  HG13   . ILE C 2 11  ? 40.829  25.384  14.682  1.00 29.79  ? 10  ILE D HG13   1 
ATOM   5301  H  HG21   . ILE C 2 11  ? 38.792  24.155  14.151  1.00 32.45  ? 10  ILE D HG21   1 
ATOM   5302  H  HG22   . ILE C 2 11  ? 38.710  23.377  12.768  1.00 32.45  ? 10  ILE D HG22   1 
ATOM   5303  H  HG23   . ILE C 2 11  ? 39.206  22.623  14.076  1.00 32.45  ? 10  ILE D HG23   1 
ATOM   5304  H  HD11   . ILE C 2 11  ? 41.787  24.268  16.412  1.00 31.78  ? 10  ILE D HD11   1 
ATOM   5305  H  HD12   . ILE C 2 11  ? 40.504  23.457  15.944  1.00 31.78  ? 10  ILE D HD12   1 
ATOM   5306  H  HD13   . ILE C 2 11  ? 41.953  22.965  15.518  1.00 31.78  ? 10  ILE D HD13   1 
ATOM   5307  N  N      . ALA C 2 12  ? 39.993  20.880  11.967  1.00 23.84  ? 11  ALA D N      1 
ATOM   5308  C  CA     . ALA C 2 12  ? 39.143  20.239  10.964  1.00 30.13  ? 11  ALA D CA     1 
ATOM   5309  C  C      . ALA C 2 12  ? 37.690  20.125  11.419  1.00 31.05  ? 11  ALA D C      1 
ATOM   5310  O  O      . ALA C 2 12  ? 37.388  20.034  12.619  1.00 26.40  ? 11  ALA D O      1 
ATOM   5311  C  CB     . ALA C 2 12  ? 39.671  18.842  10.613  1.00 30.41  ? 11  ALA D CB     1 
ATOM   5312  H  H      . ALA C 2 12  ? 39.976  20.502  12.740  1.00 28.64  ? 11  ALA D H      1 
ATOM   5313  H  HA     . ALA C 2 12  ? 39.144  20.799  10.173  1.00 36.19  ? 11  ALA D HA     1 
ATOM   5314  H  HB1    . ALA C 2 12  ? 39.096  18.447  9.939   1.00 36.52  ? 11  ALA D HB1    1 
ATOM   5315  H  HB2    . ALA C 2 12  ? 40.575  18.923  10.269  1.00 36.52  ? 11  ALA D HB2    1 
ATOM   5316  H  HB3    . ALA C 2 12  ? 39.669  18.293  11.412  1.00 36.52  ? 11  ALA D HB3    1 
ATOM   5317  N  N      . VAL C 2 13  ? 36.780  20.126  10.431  1.00 27.13  ? 12  VAL D N      1 
ATOM   5318  C  CA     . VAL C 2 13  ? 35.346  19.984  10.638  1.00 30.47  ? 12  VAL D CA     1 
ATOM   5319  C  C      . VAL C 2 13  ? 34.895  18.709  9.941   1.00 35.20  ? 12  VAL D C      1 
ATOM   5320  O  O      . VAL C 2 13  ? 34.962  18.622  8.707   1.00 33.22  ? 12  VAL D O      1 
ATOM   5321  C  CB     . VAL C 2 13  ? 34.575  21.193  10.100  1.00 30.60  ? 12  VAL D CB     1 
ATOM   5322  C  CG1    . VAL C 2 13  ? 33.095  20.967  10.236  1.00 30.76  ? 12  VAL D CG1    1 
ATOM   5323  C  CG2    . VAL C 2 13  ? 35.023  22.448  10.840  1.00 29.30  ? 12  VAL D CG2    1 
ATOM   5324  H  H      . VAL C 2 13  ? 36.987  20.211  9.601   1.00 32.59  ? 12  VAL D H      1 
ATOM   5325  H  HA     . VAL C 2 13  ? 35.170  19.890  11.588  1.00 36.60  ? 12  VAL D HA     1 
ATOM   5326  H  HB     . VAL C 2 13  ? 34.762  21.315  9.156   1.00 36.75  ? 12  VAL D HB     1 
ATOM   5327  H  HG11   . VAL C 2 13  ? 32.637  21.818  10.151  1.00 36.94  ? 12  VAL D HG11   1 
ATOM   5328  H  HG12   . VAL C 2 13  ? 32.802  20.362  9.537   1.00 36.94  ? 12  VAL D HG12   1 
ATOM   5329  H  HG13   . VAL C 2 13  ? 32.914  20.580  11.107  1.00 36.94  ? 12  VAL D HG13   1 
ATOM   5330  H  HG21   . VAL C 2 13  ? 34.483  23.198  10.544  1.00 35.19  ? 12  VAL D HG21   1 
ATOM   5331  H  HG22   . VAL C 2 13  ? 34.905  22.312  11.793  1.00 35.19  ? 12  VAL D HG22   1 
ATOM   5332  H  HG23   . VAL C 2 13  ? 35.958  22.615  10.642  1.00 35.19  ? 12  VAL D HG23   1 
ATOM   5333  N  N      . ASP C 2 14  ? 34.430  17.726  10.723  1.00 29.40  ? 13  ASP D N      1 
ATOM   5334  C  CA     . ASP C 2 14  ? 34.134  16.373  10.245  1.00 35.74  ? 13  ASP D CA     1 
ATOM   5335  C  C      . ASP C 2 14  ? 35.200  15.859  9.287   1.00 39.87  ? 13  ASP D C      1 
ATOM   5336  O  O      . ASP C 2 14  ? 34.889  15.247  8.247   1.00 38.65  ? 13  ASP D O      1 
ATOM   5337  C  CB     . ASP C 2 14  ? 32.754  16.342  9.589   1.00 36.29  ? 13  ASP D CB     1 
ATOM   5338  C  CG     . ASP C 2 14  ? 31.652  16.391  10.599  1.00 31.77  ? 13  ASP D CG     1 
ATOM   5339  O  OD1    . ASP C 2 14  ? 31.896  16.006  11.770  1.00 32.71  ? 13  ASP D OD1    1 
ATOM   5340  O  OD2    . ASP C 2 14  ? 30.529  16.797  10.227  1.00 31.84  ? 13  ASP D OD2    1 
ATOM   5341  H  H      . ASP C 2 14  ? 34.272  17.823  11.563  1.00 35.31  ? 13  ASP D H      1 
ATOM   5342  H  HA     . ASP C 2 14  ? 34.129  15.771  11.006  1.00 42.93  ? 13  ASP D HA     1 
ATOM   5343  H  HB2    . ASP C 2 14  ? 32.662  17.110  9.003   1.00 43.58  ? 13  ASP D HB2    1 
ATOM   5344  H  HB3    . ASP C 2 14  ? 32.662  15.522  9.079   1.00 43.58  ? 13  ASP D HB3    1 
ATOM   5345  N  N      . GLY C 2 15  ? 36.453  16.090  9.656   1.00 34.19  ? 14  GLY D N      1 
ATOM   5346  C  CA     . GLY C 2 15  ? 37.601  15.650  8.909   1.00 36.38  ? 14  GLY D CA     1 
ATOM   5347  C  C      . GLY C 2 15  ? 38.053  16.594  7.821   1.00 37.82  ? 14  GLY D C      1 
ATOM   5348  O  O      . GLY C 2 15  ? 39.115  16.364  7.228   1.00 41.12  ? 14  GLY D O      1 
ATOM   5349  H  H      . GLY C 2 15  ? 36.665  16.522  10.369  1.00 41.06  ? 14  GLY D H      1 
ATOM   5350  H  HA2    . GLY C 2 15  ? 38.342  15.528  9.522   1.00 43.69  ? 14  GLY D HA2    1 
ATOM   5351  H  HA3    . GLY C 2 15  ? 37.392  14.798  8.493   1.00 43.69  ? 14  GLY D HA3    1 
ATOM   5352  N  N      . GLU C 2 16  ? 37.307  17.610  7.541   1.00 34.58  ? 15  GLU D N      1 
ATOM   5353  C  CA     . GLU C 2 16  ? 37.617  18.565  6.484   1.00 38.73  ? 15  GLU D CA     1 
ATOM   5354  C  C      . GLU C 2 16  ? 38.448  19.707  7.056   1.00 32.72  ? 15  GLU D C      1 
ATOM   5355  O  O      . GLU C 2 16  ? 38.027  20.335  8.021   1.00 34.02  ? 15  GLU D O      1 
ATOM   5356  C  CB     . GLU C 2 16  ? 36.335  19.115  5.876   1.00 37.09  ? 15  GLU D CB     1 
ATOM   5357  C  CG     . GLU C 2 16  ? 36.562  19.978  4.636   1.00 45.22  ? 15  GLU D CG     1 
ATOM   5358  C  CD     . GLU C 2 16  ? 36.696  19.141  3.368   1.00 47.94  ? 15  GLU D CD     1 
ATOM   5359  O  OE1    . GLU C 2 16  ? 35.869  18.224  3.149   1.00 55.91  ? 15  GLU D OE1    1 
ATOM   5360  O  OE2    . GLU C 2 16  ? 37.656  19.378  2.603   1.00 50.38  ? 15  GLU D OE2    1 
ATOM   5361  H  H      . GLU C 2 16  ? 36.578  17.795  7.957   1.00 41.53  ? 15  GLU D H      1 
ATOM   5362  H  HA     . GLU C 2 16  ? 38.127  18.133  5.781   1.00 46.51  ? 15  GLU D HA     1 
ATOM   5363  H  HB2    . GLU C 2 16  ? 35.767  18.372  5.620   1.00 44.54  ? 15  GLU D HB2    1 
ATOM   5364  H  HB3    . GLU C 2 16  ? 35.886  19.662  6.540   1.00 44.54  ? 15  GLU D HB3    1 
ATOM   5365  H  HG2    . GLU C 2 16  ? 35.809  20.578  4.524   1.00 54.29  ? 15  GLU D HG2    1 
ATOM   5366  H  HG3    . GLU C 2 16  ? 37.379  20.489  4.749   1.00 54.29  ? 15  GLU D HG3    1 
ATOM   5367  N  N      . PRO C 2 17  ? 39.616  20.007  6.490   1.00 35.58  ? 16  PRO D N      1 
ATOM   5368  C  CA     . PRO C 2 17  ? 40.425  21.095  7.045   1.00 32.18  ? 16  PRO D CA     1 
ATOM   5369  C  C      . PRO C 2 17  ? 39.630  22.390  7.048   1.00 35.95  ? 16  PRO D C      1 
ATOM   5370  O  O      . PRO C 2 17  ? 38.915  22.712  6.096   1.00 35.06  ? 16  PRO D O      1 
ATOM   5371  C  CB     . PRO C 2 17  ? 41.645  21.176  6.123   1.00 37.88  ? 16  PRO D CB     1 
ATOM   5372  C  CG     . PRO C 2 17  ? 41.544  20.080  5.154   1.00 38.95  ? 16  PRO D CG     1 
ATOM   5373  C  CD     . PRO C 2 17  ? 40.287  19.286  5.393   1.00 38.28  ? 16  PRO D CD     1 
ATOM   5374  H  HA     . PRO C 2 17  ? 40.730  20.880  7.940   1.00 38.64  ? 16  PRO D HA     1 
ATOM   5375  H  HB2    . PRO C 2 17  ? 41.643  22.032  5.666   1.00 45.49  ? 16  PRO D HB2    1 
ATOM   5376  H  HB3    . PRO C 2 17  ? 42.452  21.085  6.653   1.00 45.49  ? 16  PRO D HB3    1 
ATOM   5377  H  HG2    . PRO C 2 17  ? 41.528  20.458  4.261   1.00 46.77  ? 16  PRO D HG2    1 
ATOM   5378  H  HG3    . PRO C 2 17  ? 42.319  19.505  5.257   1.00 46.77  ? 16  PRO D HG3    1 
ATOM   5379  H  HD2    . PRO C 2 17  ? 39.732  19.276  4.598   1.00 45.97  ? 16  PRO D HD2    1 
ATOM   5380  H  HD3    . PRO C 2 17  ? 40.501  18.378  5.659   1.00 45.97  ? 16  PRO D HD3    1 
ATOM   5381  N  N      . LEU C 2 18  ? 39.720  23.110  8.166   1.00 30.87  ? 17  LEU D N      1 
ATOM   5382  C  CA     . LEU C 2 18  ? 39.086  24.405  8.317   1.00 28.09  ? 17  LEU D CA     1 
ATOM   5383  C  C      . LEU C 2 18  ? 40.115  25.524  8.236   1.00 31.22  ? 17  LEU D C      1 
ATOM   5384  O  O      . LEU C 2 18  ? 39.962  26.465  7.456   1.00 31.39  ? 17  LEU D O      1 
ATOM   5385  C  CB     . LEU C 2 18  ? 38.346  24.464  9.649   1.00 26.75  ? 17  LEU D CB     1 
ATOM   5386  C  CG     . LEU C 2 18  ? 37.578  25.741  9.910   1.00 25.07  ? 17  LEU D CG     1 
ATOM   5387  C  CD1    . LEU C 2 18  ? 36.504  25.936  8.854   1.00 33.27  ? 17  LEU D CD1    1 
ATOM   5388  C  CD2    . LEU C 2 18  ? 36.958  25.726  11.303  1.00 25.99  ? 17  LEU D CD2    1 
ATOM   5389  H  H      . LEU C 2 18  ? 40.156  22.859  8.863   1.00 37.07  ? 17  LEU D H      1 
ATOM   5390  H  HA     . LEU C 2 18  ? 38.429  24.537  7.616   1.00 33.74  ? 17  LEU D HA     1 
ATOM   5391  H  HB2    . LEU C 2 18  ? 37.710  23.732  9.676   1.00 32.13  ? 17  LEU D HB2    1 
ATOM   5392  H  HB3    . LEU C 2 18  ? 38.995  24.366  10.363  1.00 32.13  ? 17  LEU D HB3    1 
ATOM   5393  H  HG     . LEU C 2 18  ? 38.191  26.491  9.864   1.00 30.12  ? 17  LEU D HG     1 
ATOM   5394  H  HD11   . LEU C 2 18  ? 35.919  26.659  9.129   1.00 39.95  ? 17  LEU D HD11   1 
ATOM   5395  H  HD12   . LEU C 2 18  ? 36.927  26.154  8.009   1.00 39.95  ? 17  LEU D HD12   1 
ATOM   5396  H  HD13   . LEU C 2 18  ? 35.995  25.114  8.767   1.00 39.95  ? 17  LEU D HD13   1 
ATOM   5397  H  HD21   . LEU C 2 18  ? 36.492  26.563  11.450  1.00 31.22  ? 17  LEU D HD21   1 
ATOM   5398  H  HD22   . LEU C 2 18  ? 36.334  24.985  11.363  1.00 31.22  ? 17  LEU D HD22   1 
ATOM   5399  H  HD23   . LEU C 2 18  ? 37.663  25.619  11.961  1.00 31.22  ? 17  LEU D HD23   1 
ATOM   5400  N  N      . GLY C 2 19  ? 41.168  25.431  9.028   1.00 26.48  ? 18  GLY D N      1 
ATOM   5401  C  CA     . GLY C 2 19  ? 42.209  26.431  8.983   1.00 27.33  ? 18  GLY D CA     1 
ATOM   5402  C  C      . GLY C 2 19  ? 43.061  26.294  10.220  1.00 29.03  ? 18  GLY D C      1 
ATOM   5403  O  O      . GLY C 2 19  ? 42.795  25.464  11.089  1.00 26.82  ? 18  GLY D O      1 
ATOM   5404  H  H      . GLY C 2 19  ? 41.301  24.800  9.597   1.00 31.81  ? 18  GLY D H      1 
ATOM   5405  H  HA2    . GLY C 2 19  ? 42.763  26.305  8.196   1.00 32.83  ? 18  GLY D HA2    1 
ATOM   5406  H  HA3    . GLY C 2 19  ? 41.821  27.319  8.956   1.00 32.83  ? 18  GLY D HA3    1 
ATOM   5407  N  N      . ARG C 2 20  ? 44.091  27.127  10.269  1.00 28.21  ? 19  ARG D N      1 
ATOM   5408  C  CA     . ARG C 2 20  ? 45.123  27.077  11.294  1.00 24.23  ? 19  ARG D CA     1 
ATOM   5409  C  C      . ARG C 2 20  ? 44.921  28.212  12.280  1.00 28.37  ? 19  ARG D C      1 
ATOM   5410  O  O      . ARG C 2 20  ? 44.710  29.362  11.876  1.00 26.39  ? 19  ARG D O      1 
ATOM   5411  C  CB     . ARG C 2 20  ? 46.516  27.195  10.696  1.00 25.32  ? 19  ARG D CB     1 
ATOM   5412  C  CG     . ARG C 2 20  ? 47.665  27.320  11.731  1.00 27.60  ? 19  ARG D CG     1 
ATOM   5413  C  CD     . ARG C 2 20  ? 49.037  27.009  11.135  1.00 32.55  ? 19  ARG D CD     1 
ATOM   5414  N  NE     . ARG C 2 20  ? 49.140  25.631  10.677  1.00 35.24  ? 19  ARG D NE     1 
ATOM   5415  C  CZ     . ARG C 2 20  ? 50.255  25.067  10.241  1.00 34.13  ? 19  ARG D CZ     1 
ATOM   5416  N  NH1    . ARG C 2 20  ? 51.391  25.738  10.187  1.00 36.70  ? 19  ARG D NH1    1 
ATOM   5417  N  NH2    . ARG C 2 20  ? 50.231  23.791  9.868   1.00 36.81  ? 19  ARG D NH2    1 
ATOM   5418  H  H      . ARG C 2 20  ? 44.218  27.756  9.696   1.00 33.89  ? 19  ARG D H      1 
ATOM   5419  H  HA     . ARG C 2 20  ? 45.049  26.228  11.758  1.00 29.11  ? 19  ARG D HA     1 
ATOM   5420  H  HB2    . ARG C 2 20  ? 46.690  26.403  10.164  1.00 30.42  ? 19  ARG D HB2    1 
ATOM   5421  H  HB3    . ARG C 2 20  ? 46.543  27.985  10.135  1.00 30.42  ? 19  ARG D HB3    1 
ATOM   5422  H  HG2    . ARG C 2 20  ? 47.686  28.228  12.072  1.00 33.15  ? 19  ARG D HG2    1 
ATOM   5423  H  HG3    . ARG C 2 20  ? 47.507  26.697  12.457  1.00 33.15  ? 19  ARG D HG3    1 
ATOM   5424  H  HD2    . ARG C 2 20  ? 49.193  27.592  10.375  1.00 39.09  ? 19  ARG D HD2    1 
ATOM   5425  H  HD3    . ARG C 2 20  ? 49.718  27.155  11.810  1.00 39.09  ? 19  ARG D HD3    1 
ATOM   5426  H  HE     . ARG C 2 20  ? 48.427  25.150  10.691  1.00 42.33  ? 19  ARG D HE     1 
ATOM   5427  H  HH11   . ARG C 2 20  ? 51.418  26.560  10.438  1.00 44.08  ? 19  ARG D HH11   1 
ATOM   5428  H  HH12   . ARG C 2 20  ? 52.104  25.352  9.900   1.00 44.08  ? 19  ARG D HH12   1 
ATOM   5429  H  HH21   . ARG C 2 20  ? 49.498  23.344  9.912   1.00 44.20  ? 19  ARG D HH21   1 
ATOM   5430  H  HH22   . ARG C 2 20  ? 50.949  23.413  9.583   1.00 44.20  ? 19  ARG D HH22   1 
ATOM   5431  N  N      . VAL C 2 21  ? 45.008  27.892  13.568  1.00 26.93  ? 20  VAL D N      1 
ATOM   5432  C  CA     . VAL C 2 21  ? 44.990  28.886  14.631  1.00 24.48  ? 20  VAL D CA     1 
ATOM   5433  C  C      . VAL C 2 21  ? 46.339  28.815  15.325  1.00 25.58  ? 20  VAL D C      1 
ATOM   5434  O  O      . VAL C 2 21  ? 46.792  27.721  15.656  1.00 26.42  ? 20  VAL D O      1 
ATOM   5435  C  CB     . VAL C 2 21  ? 43.861  28.624  15.641  1.00 23.67  ? 20  VAL D CB     1 
ATOM   5436  C  CG1    . VAL C 2 21  ? 43.874  29.746  16.668  1.00 24.65  ? 20  VAL D CG1    1 
ATOM   5437  C  CG2    . VAL C 2 21  ? 42.509  28.495  14.936  1.00 26.44  ? 20  VAL D CG2    1 
ATOM   5438  H  H      . VAL C 2 21  ? 45.079  27.085  13.855  1.00 32.35  ? 20  VAL D H      1 
ATOM   5439  H  HA     . VAL C 2 21  ? 44.860  29.770  14.254  1.00 29.41  ? 20  VAL D HA     1 
ATOM   5440  H  HB     . VAL C 2 21  ? 43.999  27.780  16.098  1.00 28.43  ? 20  VAL D HB     1 
ATOM   5441  H  HG11   . VAL C 2 21  ? 43.055  29.710  17.186  1.00 29.61  ? 20  VAL D HG11   1 
ATOM   5442  H  HG12   . VAL C 2 21  ? 44.640  29.631  17.252  1.00 29.61  ? 20  VAL D HG12   1 
ATOM   5443  H  HG13   . VAL C 2 21  ? 43.935  30.597  16.206  1.00 29.61  ? 20  VAL D HG13   1 
ATOM   5444  H  HG21   . VAL C 2 21  ? 41.829  28.287  15.595  1.00 31.77  ? 20  VAL D HG21   1 
ATOM   5445  H  HG22   . VAL C 2 21  ? 42.300  29.335  14.499  1.00 31.77  ? 20  VAL D HG22   1 
ATOM   5446  H  HG23   . VAL C 2 21  ? 42.563  27.784  14.279  1.00 31.77  ? 20  VAL D HG23   1 
ATOM   5447  N  N      . SER C 2 22  ? 46.996  29.965  15.511  1.00 24.57  ? 21  SER D N      1 
ATOM   5448  C  CA     . SER C 2 22  ? 48.293  30.022  16.169  1.00 24.92  ? 21  SER D CA     1 
ATOM   5449  C  C      . SER C 2 22  ? 48.113  30.787  17.472  1.00 26.35  ? 21  SER D C      1 
ATOM   5450  O  O      . SER C 2 22  ? 47.257  31.673  17.562  1.00 24.27  ? 21  SER D O      1 
ATOM   5451  C  CB     . SER C 2 22  ? 49.377  30.694  15.304  1.00 30.78  ? 21  SER D CB     1 
ATOM   5452  O  OG     . SER C 2 22  ? 49.257  32.108  15.196  1.00 28.91  ? 21  SER D OG     1 
ATOM   5453  H  H      . SER C 2 22  ? 46.701  30.733  15.260  1.00 29.52  ? 21  SER D H      1 
ATOM   5454  H  HA     . SER C 2 22  ? 48.616  29.124  16.344  1.00 29.94  ? 21  SER D HA     1 
ATOM   5455  H  HB2    . SER C 2 22  ? 50.241  30.495  15.696  1.00 36.97  ? 21  SER D HB2    1 
ATOM   5456  H  HB3    . SER C 2 22  ? 49.324  30.319  14.411  1.00 36.97  ? 21  SER D HB3    1 
ATOM   5457  H  HG     . SER C 2 22  ? 49.891  32.416  14.740  1.00 34.72  ? 21  SER D HG     1 
ATOM   5458  N  N      . PHE C 2 23  ? 48.904  30.433  18.475  1.00 23.00  ? 22  PHE D N      1 
ATOM   5459  C  CA     . PHE C 2 23  ? 48.838  31.078  19.776  1.00 27.30  ? 22  PHE D CA     1 
ATOM   5460  C  C      . PHE C 2 23  ? 50.210  31.526  20.259  1.00 25.45  ? 22  PHE D C      1 
ATOM   5461  O  O      . PHE C 2 23  ? 51.171  30.758  20.185  1.00 28.34  ? 22  PHE D O      1 
ATOM   5462  C  CB     . PHE C 2 23  ? 48.314  30.113  20.844  1.00 23.04  ? 22  PHE D CB     1 
ATOM   5463  C  CG     . PHE C 2 23  ? 47.043  29.400  20.475  1.00 26.64  ? 22  PHE D CG     1 
ATOM   5464  C  CD1    . PHE C 2 23  ? 47.070  28.157  19.827  1.00 26.76  ? 22  PHE D CD1    1 
ATOM   5465  C  CD2    . PHE C 2 23  ? 45.811  29.955  20.786  1.00 22.14  ? 22  PHE D CD2    1 
ATOM   5466  C  CE1    . PHE C 2 23  ? 45.871  27.516  19.503  1.00 24.33  ? 22  PHE D CE1    1 
ATOM   5467  C  CE2    . PHE C 2 23  ? 44.631  29.318  20.482  1.00 22.89  ? 22  PHE D CE2    1 
ATOM   5468  C  CZ     . PHE C 2 23  ? 44.645  28.097  19.855  1.00 25.15  ? 22  PHE D CZ     1 
ATOM   5469  H  H      . PHE C 2 23  ? 49.496  29.811  18.425  1.00 27.63  ? 22  PHE D H      1 
ATOM   5470  H  HA     . PHE C 2 23  ? 48.264  31.853  19.674  1.00 32.80  ? 22  PHE D HA     1 
ATOM   5471  H  HB2    . PHE C 2 23  ? 48.991  29.439  21.009  1.00 27.68  ? 22  PHE D HB2    1 
ATOM   5472  H  HB3    . PHE C 2 23  ? 48.141  30.616  21.655  1.00 27.68  ? 22  PHE D HB3    1 
ATOM   5473  H  HD1    . PHE C 2 23  ? 47.884  27.760  19.612  1.00 32.15  ? 22  PHE D HD1    1 
ATOM   5474  H  HD2    . PHE C 2 23  ? 45.782  30.781  21.211  1.00 26.60  ? 22  PHE D HD2    1 
ATOM   5475  H  HE1    . PHE C 2 23  ? 45.886  26.703  19.053  1.00 29.24  ? 22  PHE D HE1    1 
ATOM   5476  H  HE2    . PHE C 2 23  ? 43.819  29.716  20.702  1.00 27.51  ? 22  PHE D HE2    1 
ATOM   5477  H  HZ     . PHE C 2 23  ? 43.847  27.659  19.666  1.00 30.21  ? 22  PHE D HZ     1 
ATOM   5478  N  N      . GLU C 2 24  ? 50.286  32.749  20.804  1.00 23.61  ? 23  GLU D N      1 
ATOM   5479  C  CA     . GLU C 2 24  ? 51.402  33.159  21.630  1.00 24.97  ? 23  GLU D CA     1 
ATOM   5480  C  C      . GLU C 2 24  ? 51.165  32.675  23.044  1.00 25.05  ? 23  GLU D C      1 
ATOM   5481  O  O      . GLU C 2 24  ? 50.059  32.828  23.579  1.00 24.59  ? 23  GLU D O      1 
ATOM   5482  C  CB     . GLU C 2 24  ? 51.554  34.676  21.624  1.00 25.88  ? 23  GLU D CB     1 
ATOM   5483  C  CG     . GLU C 2 24  ? 52.617  35.182  22.572  1.00 28.65  ? 23  GLU D CG     1 
ATOM   5484  C  CD     . GLU C 2 24  ? 52.771  36.692  22.499  1.00 32.82  ? 23  GLU D CD     1 
ATOM   5485  O  OE1    . GLU C 2 24  ? 52.100  37.335  21.642  1.00 32.43  ? 23  GLU D OE1    1 
ATOM   5486  O  OE2    . GLU C 2 24  ? 53.590  37.206  23.266  1.00 34.91  ? 23  GLU D OE2    1 
ATOM   5487  H  H      . GLU C 2 24  ? 49.690  33.360  20.702  1.00 28.16  ? 23  GLU D H      1 
ATOM   5488  H  HA     . GLU C 2 24  ? 52.223  32.776  21.285  1.00 30.00  ? 23  GLU D HA     1 
ATOM   5489  H  HB2    . GLU C 2 24  ? 51.794  34.962  20.729  1.00 31.09  ? 23  GLU D HB2    1 
ATOM   5490  H  HB3    . GLU C 2 24  ? 50.709  35.075  21.885  1.00 31.09  ? 23  GLU D HB3    1 
ATOM   5491  H  HG2    . GLU C 2 24  ? 52.373  34.945  23.480  1.00 34.41  ? 23  GLU D HG2    1 
ATOM   5492  H  HG3    . GLU C 2 24  ? 53.468  34.778  22.341  1.00 34.41  ? 23  GLU D HG3    1 
ATOM   5493  N  N      . LEU C 2 25  ? 52.170  32.049  23.637  1.00 27.88  ? 24  LEU D N      1 
ATOM   5494  C  CA     . LEU C 2 25  ? 52.052  31.493  24.985  1.00 27.81  ? 24  LEU D CA     1 
ATOM   5495  C  C      . LEU C 2 25  ? 52.848  32.371  25.949  1.00 28.73  ? 24  LEU D C      1 
ATOM   5496  O  O      . LEU C 2 25  ? 54.054  32.606  25.758  1.00 29.06  ? 24  LEU D O      1 
ATOM   5497  C  CB     . LEU C 2 25  ? 52.523  30.038  25.030  1.00 27.50  ? 24  LEU D CB     1 
ATOM   5498  C  CG     . LEU C 2 25  ? 51.794  29.059  24.115  1.00 26.45  ? 24  LEU D CG     1 
ATOM   5499  C  CD1    . LEU C 2 25  ? 52.308  27.636  24.349  1.00 29.47  ? 24  LEU D CD1    1 
ATOM   5500  C  CD2    . LEU C 2 25  ? 50.286  29.127  24.321  1.00 28.06  ? 24  LEU D CD2    1 
ATOM   5501  H  H      . LEU C 2 25  ? 52.942  31.931  23.277  1.00 33.49  ? 24  LEU D H      1 
ATOM   5502  H  HA     . LEU C 2 25  ? 51.123  31.507  25.264  1.00 33.41  ? 24  LEU D HA     1 
ATOM   5503  H  HB2    . LEU C 2 25  ? 53.461  30.018  24.781  1.00 33.04  ? 24  LEU D HB2    1 
ATOM   5504  H  HB3    . LEU C 2 25  ? 52.415  29.715  25.938  1.00 33.04  ? 24  LEU D HB3    1 
ATOM   5505  H  HG     . LEU C 2 25  ? 51.971  29.303  23.193  1.00 31.77  ? 24  LEU D HG     1 
ATOM   5506  H  HD11   . LEU C 2 25  ? 51.844  27.031  23.750  1.00 35.40  ? 24  LEU D HD11   1 
ATOM   5507  H  HD12   . LEU C 2 25  ? 53.261  27.612  24.173  1.00 35.40  ? 24  LEU D HD12   1 
ATOM   5508  H  HD13   . LEU C 2 25  ? 52.135  27.386  25.271  1.00 35.40  ? 24  LEU D HD13   1 
ATOM   5509  H  HD21   . LEU C 2 25  ? 49.867  28.402  23.832  1.00 33.71  ? 24  LEU D HD21   1 
ATOM   5510  H  HD22   . LEU C 2 25  ? 50.092  29.043  25.268  1.00 33.71  ? 24  LEU D HD22   1 
ATOM   5511  H  HD23   . LEU C 2 25  ? 49.960  29.979  23.991  1.00 33.71  ? 24  LEU D HD23   1 
ATOM   5512  N  N      . PHE C 2 26  ? 52.186  32.856  27.004  1.00 27.76  ? 25  PHE D N      1 
ATOM   5513  C  CA     . PHE C 2 26  ? 52.842  33.858  27.869  1.00 30.11  ? 25  PHE D CA     1 
ATOM   5514  C  C      . PHE C 2 26  ? 53.757  33.206  28.909  1.00 32.79  ? 25  PHE D C      1 
ATOM   5515  O  O      . PHE C 2 26  ? 53.560  33.280  30.133  1.00 31.34  ? 25  PHE D O      1 
ATOM   5516  C  CB     . PHE C 2 26  ? 51.780  34.713  28.533  1.00 30.25  ? 25  PHE D CB     1 
ATOM   5517  C  CG     . PHE C 2 26  ? 50.865  35.396  27.560  1.00 29.40  ? 25  PHE D CG     1 
ATOM   5518  C  CD1    . PHE C 2 26  ? 51.359  36.063  26.452  1.00 31.51  ? 25  PHE D CD1    1 
ATOM   5519  C  CD2    . PHE C 2 26  ? 49.502  35.358  27.752  1.00 26.64  ? 25  PHE D CD2    1 
ATOM   5520  C  CE1    . PHE C 2 26  ? 50.488  36.678  25.554  1.00 32.21  ? 25  PHE D CE1    1 
ATOM   5521  C  CE2    . PHE C 2 26  ? 48.656  35.982  26.882  1.00 27.69  ? 25  PHE D CE2    1 
ATOM   5522  C  CZ     . PHE C 2 26  ? 49.144  36.637  25.774  1.00 29.89  ? 25  PHE D CZ     1 
ATOM   5523  H  H      . PHE C 2 26  ? 51.389  32.632  27.235  1.00 33.34  ? 25  PHE D H      1 
ATOM   5524  H  HA     . PHE C 2 26  ? 53.414  34.405  27.308  1.00 36.16  ? 25  PHE D HA     1 
ATOM   5525  H  HB2    . PHE C 2 26  ? 51.238  34.148  29.105  1.00 36.34  ? 25  PHE D HB2    1 
ATOM   5526  H  HB3    . PHE C 2 26  ? 52.217  35.399  29.061  1.00 36.34  ? 25  PHE D HB3    1 
ATOM   5527  H  HD1    . PHE C 2 26  ? 52.277  36.102  26.306  1.00 37.85  ? 25  PHE D HD1    1 
ATOM   5528  H  HD2    . PHE C 2 26  ? 49.154  34.903  28.485  1.00 32.00  ? 25  PHE D HD2    1 
ATOM   5529  H  HE1    . PHE C 2 26  ? 50.824  37.116  24.805  1.00 38.69  ? 25  PHE D HE1    1 
ATOM   5530  H  HE2    . PHE C 2 26  ? 47.739  35.964  27.039  1.00 33.26  ? 25  PHE D HE2    1 
ATOM   5531  H  HZ     . PHE C 2 26  ? 48.560  37.049  25.179  1.00 35.90  ? 25  PHE D HZ     1 
ATOM   5532  N  N      . ALA C 2 27  ? 54.829  32.581  28.404  1.00 33.81  ? 26  ALA D N      1 
ATOM   5533  C  CA     . ALA C 2 27  ? 55.773  31.958  29.312  1.00 34.16  ? 26  ALA D CA     1 
ATOM   5534  C  C      . ALA C 2 27  ? 56.481  32.997  30.168  1.00 32.56  ? 26  ALA D C      1 
ATOM   5535  O  O      . ALA C 2 27  ? 57.098  32.637  31.176  1.00 33.70  ? 26  ALA D O      1 
ATOM   5536  C  CB     . ALA C 2 27  ? 56.831  31.146  28.572  1.00 36.97  ? 26  ALA D CB     1 
ATOM   5537  H  H      . ALA C 2 27  ? 55.017  32.511  27.568  1.00 40.61  ? 26  ALA D H      1 
ATOM   5538  H  HA     . ALA C 2 27  ? 55.276  31.340  29.871  1.00 41.02  ? 26  ALA D HA     1 
ATOM   5539  H  HB1    . ALA C 2 27  ? 57.434  30.748  29.219  1.00 44.39  ? 26  ALA D HB1    1 
ATOM   5540  H  HB2    . ALA C 2 27  ? 56.393  30.451  28.057  1.00 44.39  ? 26  ALA D HB2    1 
ATOM   5541  H  HB3    . ALA C 2 27  ? 57.324  31.736  27.980  1.00 44.39  ? 26  ALA D HB3    1 
ATOM   5542  N  N      . ASP C 2 28  ? 56.439  34.273  29.764  1.00 33.45  ? 27  ASP D N      1 
ATOM   5543  C  CA     . ASP C 2 28  ? 57.077  35.309  30.577  1.00 37.65  ? 27  ASP D CA     1 
ATOM   5544  C  C      . ASP C 2 28  ? 56.278  35.643  31.837  1.00 33.56  ? 27  ASP D C      1 
ATOM   5545  O  O      . ASP C 2 28  ? 56.837  36.286  32.724  1.00 38.72  ? 27  ASP D O      1 
ATOM   5546  C  CB     . ASP C 2 28  ? 57.309  36.574  29.741  1.00 36.06  ? 27  ASP D CB     1 
ATOM   5547  C  CG     . ASP C 2 28  ? 56.043  37.104  29.125  1.00 40.02  ? 27  ASP D CG     1 
ATOM   5548  O  OD1    . ASP C 2 28  ? 54.976  36.500  29.335  1.00 35.50  ? 27  ASP D OD1    1 
ATOM   5549  O  OD2    . ASP C 2 28  ? 56.126  38.107  28.391  1.00 44.86  ? 27  ASP D OD2    1 
ATOM   5550  H  H      . ASP C 2 28  ? 56.059  34.553  29.046  1.00 40.18  ? 27  ASP D H      1 
ATOM   5551  H  HA     . ASP C 2 28  ? 57.948  34.990  30.860  1.00 45.21  ? 27  ASP D HA     1 
ATOM   5552  H  HB2    . ASP C 2 28  ? 57.678  37.267  30.311  1.00 43.31  ? 27  ASP D HB2    1 
ATOM   5553  H  HB3    . ASP C 2 28  ? 57.929  36.370  29.024  1.00 43.31  ? 27  ASP D HB3    1 
ATOM   5554  N  N      . LYS C 2 29  ? 55.007  35.232  31.947  1.00 32.70  ? 28  LYS D N      1 
ATOM   5555  C  CA     . LYS C 2 29  ? 54.255  35.403  33.194  1.00 36.81  ? 28  LYS D CA     1 
ATOM   5556  C  C      . LYS C 2 29  ? 53.806  34.102  33.836  1.00 33.16  ? 28  LYS D C      1 
ATOM   5557  O  O      . LYS C 2 29  ? 53.715  34.042  35.061  1.00 34.03  ? 28  LYS D O      1 
ATOM   5558  C  CB     . LYS C 2 29  ? 52.983  36.248  32.993  1.00 36.37  ? 28  LYS D CB     1 
ATOM   5559  C  CG     . LYS C 2 29  ? 53.117  37.458  32.095  1.00 39.18  ? 28  LYS D CG     1 
ATOM   5560  C  CD     . LYS C 2 29  ? 53.231  38.747  32.861  1.00 37.03  ? 28  LYS D CD     1 
ATOM   5561  C  CE     . LYS C 2 29  ? 54.094  39.734  32.105  1.00 41.68  ? 28  LYS D CE     1 
ATOM   5562  N  NZ     . LYS C 2 29  ? 53.345  40.645  31.216  1.00 41.53  ? 28  LYS D NZ     1 
ATOM   5563  H  H      . LYS C 2 29  ? 54.564  34.852  31.316  1.00 39.07  ? 28  LYS D H      1 
ATOM   5564  H  HA     . LYS C 2 29  ? 54.845  35.878  33.800  1.00 44.21  ? 28  LYS D HA     1 
ATOM   5565  H  HB2    . LYS C 2 29  ? 52.300  35.679  32.604  1.00 43.67  ? 28  LYS D HB2    1 
ATOM   5566  H  HB3    . LYS C 2 29  ? 52.692  36.568  33.862  1.00 43.67  ? 28  LYS D HB3    1 
ATOM   5567  H  HG2    . LYS C 2 29  ? 53.916  37.362  31.552  1.00 47.05  ? 28  LYS D HG2    1 
ATOM   5568  H  HG3    . LYS C 2 29  ? 52.334  37.518  31.525  1.00 47.05  ? 28  LYS D HG3    1 
ATOM   5569  H  HD2    . LYS C 2 29  ? 52.350  39.134  32.981  1.00 44.47  ? 28  LYS D HD2    1 
ATOM   5570  H  HD3    . LYS C 2 29  ? 53.639  38.577  33.725  1.00 44.47  ? 28  LYS D HD3    1 
ATOM   5571  H  HE2    . LYS C 2 29  ? 54.574  40.281  32.747  1.00 50.05  ? 28  LYS D HE2    1 
ATOM   5572  H  HE3    . LYS C 2 29  ? 54.722  39.239  31.556  1.00 50.05  ? 28  LYS D HE3    1 
ATOM   5573  H  HZ1    . LYS C 2 29  ? 53.907  41.196  30.801  1.00 49.87  ? 28  LYS D HZ1    1 
ATOM   5574  H  HZ2    . LYS C 2 29  ? 52.898  40.175  30.606  1.00 49.87  ? 28  LYS D HZ2    1 
ATOM   5575  H  HZ3    . LYS C 2 29  ? 52.766  41.126  31.691  1.00 49.87  ? 28  LYS D HZ3    1 
ATOM   5576  N  N      . VAL C 2 30  ? 53.517  33.074  33.054  1.00 32.36  ? 29  VAL D N      1 
ATOM   5577  C  CA     . VAL C 2 30  ? 53.025  31.787  33.557  1.00 33.45  ? 29  VAL D CA     1 
ATOM   5578  C  C      . VAL C 2 30  ? 53.851  30.692  32.891  1.00 32.51  ? 29  VAL D C      1 
ATOM   5579  O  O      . VAL C 2 30  ? 53.341  29.934  32.063  1.00 32.06  ? 29  VAL D O      1 
ATOM   5580  C  CB     . VAL C 2 30  ? 51.523  31.593  33.301  1.00 31.19  ? 29  VAL D CB     1 
ATOM   5581  C  CG1    . VAL C 2 30  ? 50.680  32.320  34.380  1.00 32.37  ? 29  VAL D CG1    1 
ATOM   5582  C  CG2    . VAL C 2 30  ? 51.086  32.057  31.904  1.00 29.93  ? 29  VAL D CG2    1 
ATOM   5583  H  H      . VAL C 2 30  ? 53.597  33.090  32.198  1.00 38.67  ? 29  VAL D H      1 
ATOM   5584  H  HA     . VAL C 2 30  ? 53.151  31.750  34.518  1.00 40.17  ? 29  VAL D HA     1 
ATOM   5585  H  HB     . VAL C 2 30  ? 51.357  30.639  33.349  1.00 37.26  ? 29  VAL D HB     1 
ATOM   5586  H  HG11   . VAL C 2 30  ? 49.739  32.183  34.190  1.00 38.87  ? 29  VAL D HG11   1 
ATOM   5587  H  HG12   . VAL C 2 30  ? 50.900  31.955  35.251  1.00 38.87  ? 29  VAL D HG12   1 
ATOM   5588  H  HG13   . VAL C 2 30  ? 50.888  33.268  34.357  1.00 38.87  ? 29  VAL D HG13   1 
ATOM   5589  H  HG21   . VAL C 2 30  ? 50.143  31.864  31.787  1.00 35.74  ? 29  VAL D HG21   1 
ATOM   5590  H  HG22   . VAL C 2 30  ? 51.240  33.012  31.825  1.00 35.74  ? 29  VAL D HG22   1 
ATOM   5591  H  HG23   . VAL C 2 30  ? 51.606  31.582  31.236  1.00 35.74  ? 29  VAL D HG23   1 
ATOM   5592  N  N      . PRO C 2 31  ? 55.137  30.596  33.216  1.00 33.69  ? 30  PRO D N      1 
ATOM   5593  C  CA     . PRO C 2 31  ? 56.016  29.664  32.492  1.00 33.91  ? 30  PRO D CA     1 
ATOM   5594  C  C      . PRO C 2 31  ? 55.608  28.214  32.607  1.00 33.82  ? 30  PRO D C      1 
ATOM   5595  O  O      . PRO C 2 31  ? 55.727  27.486  31.615  1.00 33.38  ? 30  PRO D O      1 
ATOM   5596  C  CB     . PRO C 2 31  ? 57.393  29.911  33.147  1.00 35.45  ? 30  PRO D CB     1 
ATOM   5597  C  CG     . PRO C 2 31  ? 57.050  30.427  34.540  1.00 36.16  ? 30  PRO D CG     1 
ATOM   5598  C  CD     . PRO C 2 31  ? 55.857  31.314  34.288  1.00 34.99  ? 30  PRO D CD     1 
ATOM   5599  H  HA     . PRO C 2 31  ? 56.039  29.913  31.555  1.00 40.52  ? 30  PRO D HA     1 
ATOM   5600  H  HB2    . PRO C 2 31  ? 57.895  29.083  33.193  1.00 42.37  ? 30  PRO D HB2    1 
ATOM   5601  H  HB3    . PRO C 2 31  ? 57.891  30.573  32.640  1.00 42.37  ? 30  PRO D HB3    1 
ATOM   5602  H  HG2    . PRO C 2 31  ? 56.825  29.690  35.128  1.00 43.23  ? 30  PRO D HG2    1 
ATOM   5603  H  HG3    . PRO C 2 31  ? 57.793  30.930  34.908  1.00 43.23  ? 30  PRO D HG3    1 
ATOM   5604  H  HD2    . PRO C 2 31  ? 55.308  31.391  35.084  1.00 41.82  ? 30  PRO D HD2    1 
ATOM   5605  H  HD3    . PRO C 2 31  ? 56.135  32.194  33.990  1.00 41.82  ? 30  PRO D HD3    1 
ATOM   5606  N  N      . LYS C 2 32  ? 55.181  27.760  33.788  1.00 34.39  ? 31  LYS D N      1 
ATOM   5607  C  CA     . LYS C 2 32  ? 54.810  26.356  33.933  1.00 35.54  ? 31  LYS D CA     1 
ATOM   5608  C  C      . LYS C 2 32  ? 53.600  26.029  33.056  1.00 34.30  ? 31  LYS D C      1 
ATOM   5609  O  O      . LYS C 2 32  ? 53.536  24.957  32.446  1.00 34.18  ? 31  LYS D O      1 
ATOM   5610  C  CB     . LYS C 2 32  ? 54.476  25.990  35.391  1.00 35.31  ? 31  LYS D CB     1 
ATOM   5611  C  CG     . LYS C 2 32  ? 55.589  25.996  36.423  1.00 45.53  ? 31  LYS D CG     1 
ATOM   5612  C  CD     . LYS C 2 32  ? 55.382  24.929  37.565  1.00 49.80  ? 31  LYS D CD     1 
ATOM   5613  C  CE     . LYS C 2 32  ? 53.990  24.259  37.623  1.00 48.37  ? 31  LYS D CE     1 
ATOM   5614  N  NZ     . LYS C 2 32  ? 53.854  23.269  38.756  1.00 53.41  ? 31  LYS D NZ     1 
ATOM   5615  H  H      . LYS C 2 32  ? 55.099  28.234  34.501  1.00 41.10  ? 31  LYS D H      1 
ATOM   5616  H  HA     . LYS C 2 32  ? 55.577  25.826  33.667  1.00 42.68  ? 31  LYS D HA     1 
ATOM   5617  H  HB2    . LYS C 2 32  ? 53.810  26.622  35.704  1.00 42.20  ? 31  LYS D HB2    1 
ATOM   5618  H  HB3    . LYS C 2 32  ? 54.109  25.093  35.389  1.00 42.20  ? 31  LYS D HB3    1 
ATOM   5619  H  HG2    . LYS C 2 32  ? 56.430  25.799  35.981  1.00 54.68  ? 31  LYS D HG2    1 
ATOM   5620  H  HG3    . LYS C 2 32  ? 55.629  26.871  36.838  1.00 54.68  ? 31  LYS D HG3    1 
ATOM   5621  H  HD2    . LYS C 2 32  ? 56.034  24.221  37.442  1.00 59.80  ? 31  LYS D HD2    1 
ATOM   5622  H  HD3    . LYS C 2 32  ? 55.524  25.366  38.419  1.00 59.80  ? 31  LYS D HD3    1 
ATOM   5623  H  HE2    . LYS C 2 32  ? 53.315  24.945  37.745  1.00 58.08  ? 31  LYS D HE2    1 
ATOM   5624  H  HE3    . LYS C 2 32  ? 53.834  23.784  36.792  1.00 58.08  ? 31  LYS D HE3    1 
ATOM   5625  H  HZ1    . LYS C 2 32  ? 54.003  23.674  39.534  1.00 64.13  ? 31  LYS D HZ1    1 
ATOM   5626  H  HZ2    . LYS C 2 32  ? 54.443  22.609  38.656  1.00 64.13  ? 31  LYS D HZ2    1 
ATOM   5627  H  HZ3    . LYS C 2 32  ? 53.033  22.925  38.762  1.00 64.13  ? 31  LYS D HZ3    1 
ATOM   5628  N  N      . THR C 2 33  ? 52.610  26.928  33.028  1.00 32.16  ? 32  THR D N      1 
ATOM   5629  C  CA     . THR C 2 33  ? 51.363  26.678  32.298  1.00 32.57  ? 32  THR D CA     1 
ATOM   5630  C  C      . THR C 2 33  ? 51.594  26.786  30.799  1.00 29.78  ? 32  THR D C      1 
ATOM   5631  O  O      . THR C 2 33  ? 51.019  26.027  30.014  1.00 29.92  ? 32  THR D O      1 
ATOM   5632  C  CB     . THR C 2 33  ? 50.289  27.673  32.770  1.00 32.66  ? 32  THR D CB     1 
ATOM   5633  O  OG1    . THR C 2 33  ? 50.181  27.611  34.197  1.00 33.52  ? 32  THR D OG1    1 
ATOM   5634  C  CG2    . THR C 2 33  ? 48.911  27.383  32.139  1.00 28.85  ? 32  THR D CG2    1 
ATOM   5635  H  H      . THR C 2 33  ? 52.635  27.691  33.424  1.00 38.63  ? 32  THR D H      1 
ATOM   5636  H  HA     . THR C 2 33  ? 51.041  25.783  32.486  1.00 39.12  ? 32  THR D HA     1 
ATOM   5637  H  HB     . THR C 2 33  ? 50.550  28.566  32.492  1.00 39.22  ? 32  THR D HB     1 
ATOM   5638  H  HG1    . THR C 2 33  ? 50.909  27.836  34.550  1.00 40.25  ? 32  THR D HG1    1 
ATOM   5639  H  HG21   . THR C 2 33  ? 48.249  28.000  32.490  1.00 34.45  ? 32  THR D HG21   1 
ATOM   5640  H  HG22   . THR C 2 33  ? 48.958  27.487  31.176  1.00 34.45  ? 32  THR D HG22   1 
ATOM   5641  H  HG23   . THR C 2 33  ? 48.636  26.476  32.345  1.00 34.45  ? 32  THR D HG23   1 
ATOM   5642  N  N      . ALA C 2 34  ? 52.452  27.714  30.391  1.00 30.78  ? 33  ALA D N      1 
ATOM   5643  C  CA     . ALA C 2 34  ? 52.814  27.825  28.989  1.00 29.40  ? 33  ALA D CA     1 
ATOM   5644  C  C      . ALA C 2 34  ? 53.560  26.589  28.518  1.00 31.15  ? 33  ALA D C      1 
ATOM   5645  O  O      . ALA C 2 34  ? 53.298  26.080  27.419  1.00 30.42  ? 33  ALA D O      1 
ATOM   5646  C  CB     . ALA C 2 34  ? 53.645  29.084  28.755  1.00 30.54  ? 33  ALA D CB     1 
ATOM   5647  H  H      . ALA C 2 34  ? 52.836  28.288  30.904  1.00 36.96  ? 33  ALA D H      1 
ATOM   5648  H  HA     . ALA C 2 34  ? 52.003  27.904  28.461  1.00 35.11  ? 33  ALA D HA     1 
ATOM   5649  H  HB1    . ALA C 2 34  ? 53.875  29.141  27.815  1.00 36.68  ? 33  ALA D HB1    1 
ATOM   5650  H  HB2    . ALA C 2 34  ? 53.124  29.860  29.016  1.00 36.68  ? 33  ALA D HB2    1 
ATOM   5651  H  HB3    . ALA C 2 34  ? 54.452  29.033  29.291  1.00 36.68  ? 33  ALA D HB3    1 
ATOM   5652  N  N      . GLU C 2 35  ? 54.494  26.086  29.332  1.00 32.43  ? 34  GLU D N      1 
ATOM   5653  C  CA     . GLU C 2 35  ? 55.260  24.912  28.930  1.00 35.21  ? 34  GLU D CA     1 
ATOM   5654  C  C      . GLU C 2 35  ? 54.350  23.708  28.738  1.00 33.25  ? 34  GLU D C      1 
ATOM   5655  O  O      . GLU C 2 35  ? 54.496  22.951  27.773  1.00 36.08  ? 34  GLU D O      1 
ATOM   5656  C  CB     . GLU C 2 35  ? 56.342  24.619  29.978  1.00 35.35  ? 34  GLU D CB     1 
ATOM   5657  C  CG     . GLU C 2 35  ? 57.059  23.296  29.803  1.00 39.80  ? 34  GLU D CG     1 
ATOM   5658  C  CD     . GLU C 2 35  ? 57.768  23.185  28.457  1.00 42.05  ? 34  GLU D CD     1 
ATOM   5659  O  OE1    . GLU C 2 35  ? 57.882  24.198  27.734  1.00 40.14  ? 34  GLU D OE1    1 
ATOM   5660  O  OE2    . GLU C 2 35  ? 58.205  22.075  28.113  1.00 44.86  ? 34  GLU D OE2    1 
ATOM   5661  H  H      . GLU C 2 35  ? 54.696  26.402  30.106  1.00 38.95  ? 34  GLU D H      1 
ATOM   5662  H  HA     . GLU C 2 35  ? 55.700  25.089  28.084  1.00 42.29  ? 34  GLU D HA     1 
ATOM   5663  H  HB2    . GLU C 2 35  ? 57.011  25.321  29.934  1.00 42.46  ? 34  GLU D HB2    1 
ATOM   5664  H  HB3    . GLU C 2 35  ? 55.927  24.612  30.855  1.00 42.46  ? 34  GLU D HB3    1 
ATOM   5665  H  HG2    . GLU C 2 35  ? 57.725  23.201  30.502  1.00 47.80  ? 34  GLU D HG2    1 
ATOM   5666  H  HG3    . GLU C 2 35  ? 56.412  22.575  29.862  1.00 47.80  ? 34  GLU D HG3    1 
ATOM   5667  N  N      . ASN C 2 36  ? 53.412  23.508  29.651  1.00 33.17  ? 35  ASN D N      1 
ATOM   5668  C  CA     . ASN C 2 36  ? 52.484  22.399  29.530  1.00 30.71  ? 35  ASN D CA     1 
ATOM   5669  C  C      . ASN C 2 36  ? 51.753  22.439  28.188  1.00 31.72  ? 35  ASN D C      1 
ATOM   5670  O  O      . ASN C 2 36  ? 51.733  21.451  27.444  1.00 33.67  ? 35  ASN D O      1 
ATOM   5671  C  CB     . ASN C 2 36  ? 51.489  22.455  30.681  1.00 33.11  ? 35  ASN D CB     1 
ATOM   5672  C  CG     . ASN C 2 36  ? 50.531  21.295  30.672  1.00 32.68  ? 35  ASN D CG     1 
ATOM   5673  O  OD1    . ASN C 2 36  ? 50.965  20.150  30.596  1.00 34.49  ? 35  ASN D OD1    1 
ATOM   5674  N  ND2    . ASN C 2 36  ? 49.222  21.579  30.743  1.00 31.38  ? 35  ASN D ND2    1 
ATOM   5675  H  H      . ASN C 2 36  ? 53.293  23.998  30.347  1.00 39.83  ? 35  ASN D H      1 
ATOM   5676  H  HA     . ASN C 2 36  ? 52.973  21.563  29.578  1.00 36.89  ? 35  ASN D HA     1 
ATOM   5677  H  HB2    . ASN C 2 36  ? 51.975  22.438  31.521  1.00 39.76  ? 35  ASN D HB2    1 
ATOM   5678  H  HB3    . ASN C 2 36  ? 50.972  23.273  30.614  1.00 39.76  ? 35  ASN D HB3    1 
ATOM   5679  H  HD21   . ASN C 2 36  ? 48.643  20.943  30.741  1.00 37.68  ? 35  ASN D HD21   1 
ATOM   5680  H  HD22   . ASN C 2 36  ? 48.962  22.397  30.792  1.00 37.68  ? 35  ASN D HD22   1 
ATOM   5681  N  N      . PHE C 2 37  ? 51.128  23.568  27.876  1.00 28.90  ? 36  PHE D N      1 
ATOM   5682  C  CA     . PHE C 2 37  ? 50.426  23.690  26.602  1.00 30.59  ? 36  PHE D CA     1 
ATOM   5683  C  C      . PHE C 2 37  ? 51.371  23.537  25.416  1.00 31.96  ? 36  PHE D C      1 
ATOM   5684  O  O      . PHE C 2 37  ? 51.026  22.893  24.408  1.00 31.26  ? 36  PHE D O      1 
ATOM   5685  C  CB     . PHE C 2 37  ? 49.717  25.031  26.542  1.00 27.24  ? 36  PHE D CB     1 
ATOM   5686  C  CG     . PHE C 2 37  ? 48.663  25.116  25.467  1.00 27.58  ? 36  PHE D CG     1 
ATOM   5687  C  CD1    . PHE C 2 37  ? 48.985  25.589  24.212  1.00 24.58  ? 36  PHE D CD1    1 
ATOM   5688  C  CD2    . PHE C 2 37  ? 47.362  24.753  25.739  1.00 26.65  ? 36  PHE D CD2    1 
ATOM   5689  C  CE1    . PHE C 2 37  ? 48.017  25.706  23.254  1.00 26.56  ? 36  PHE D CE1    1 
ATOM   5690  C  CE2    . PHE C 2 37  ? 46.378  24.841  24.776  1.00 28.60  ? 36  PHE D CE2    1 
ATOM   5691  C  CZ     . PHE C 2 37  ? 46.703  25.323  23.550  1.00 25.68  ? 36  PHE D CZ     1 
ATOM   5692  H  H      . PHE C 2 37  ? 51.095  24.268  28.375  1.00 34.72  ? 36  PHE D H      1 
ATOM   5693  H  HA     . PHE C 2 37  ? 49.765  22.983  26.542  1.00 36.74  ? 36  PHE D HA     1 
ATOM   5694  H  HB2    . PHE C 2 37  ? 49.283  25.193  27.394  1.00 32.72  ? 36  PHE D HB2    1 
ATOM   5695  H  HB3    . PHE C 2 37  ? 50.374  25.723  26.367  1.00 32.72  ? 36  PHE D HB3    1 
ATOM   5696  H  HD1    . PHE C 2 37  ? 49.862  25.829  24.017  1.00 29.53  ? 36  PHE D HD1    1 
ATOM   5697  H  HD2    . PHE C 2 37  ? 47.143  24.444  26.588  1.00 32.01  ? 36  PHE D HD2    1 
ATOM   5698  H  HE1    . PHE C 2 37  ? 48.229  26.038  22.412  1.00 31.90  ? 36  PHE D HE1    1 
ATOM   5699  H  HE2    . PHE C 2 37  ? 45.507  24.574  24.965  1.00 34.36  ? 36  PHE D HE2    1 
ATOM   5700  H  HZ     . PHE C 2 37  ? 46.044  25.400  22.898  1.00 30.85  ? 36  PHE D HZ     1 
ATOM   5701  N  N      . ARG C 2 38  ? 52.550  24.144  25.500  1.00 31.35  ? 37  ARG D N      1 
ATOM   5702  C  CA     . ARG C 2 38  ? 53.547  23.974  24.452  1.00 35.21  ? 37  ARG D CA     1 
ATOM   5703  C  C      . ARG C 2 38  ? 53.846  22.501  24.228  1.00 33.61  ? 37  ARG D C      1 
ATOM   5704  O  O      . ARG C 2 38  ? 53.698  21.991  23.112  1.00 34.12  ? 37  ARG D O      1 
ATOM   5705  C  CB     . ARG C 2 38  ? 54.816  24.735  24.819  1.00 33.04  ? 37  ARG D CB     1 
ATOM   5706  C  CG     . ARG C 2 38  ? 55.853  24.782  23.700  1.00 35.66  ? 37  ARG D CG     1 
ATOM   5707  C  CD     . ARG C 2 38  ? 57.251  25.014  24.247  1.00 32.80  ? 37  ARG D CD     1 
ATOM   5708  N  NE     . ARG C 2 38  ? 57.733  23.880  25.022  1.00 38.10  ? 37  ARG D NE     1 
ATOM   5709  C  CZ     . ARG C 2 38  ? 58.069  22.701  24.508  1.00 38.07  ? 37  ARG D CZ     1 
ATOM   5710  N  NH1    . ARG C 2 38  ? 58.001  22.464  23.203  1.00 37.70  ? 37  ARG D NH1    1 
ATOM   5711  N  NH2    . ARG C 2 38  ? 58.492  21.736  25.318  1.00 36.13  ? 37  ARG D NH2    1 
ATOM   5712  H  H      . ARG C 2 38  ? 52.795  24.654  26.147  1.00 37.66  ? 37  ARG D H      1 
ATOM   5713  H  HA     . ARG C 2 38  ? 53.205  24.342  23.622  1.00 42.29  ? 37  ARG D HA     1 
ATOM   5714  H  HB2    . ARG C 2 38  ? 54.579  25.649  25.040  1.00 39.68  ? 37  ARG D HB2    1 
ATOM   5715  H  HB3    . ARG C 2 38  ? 55.227  24.304  25.585  1.00 39.68  ? 37  ARG D HB3    1 
ATOM   5716  H  HG2    . ARG C 2 38  ? 55.849  23.938  23.222  1.00 42.83  ? 37  ARG D HG2    1 
ATOM   5717  H  HG3    . ARG C 2 38  ? 55.639  25.508  23.093  1.00 42.83  ? 37  ARG D HG3    1 
ATOM   5718  H  HD2    . ARG C 2 38  ? 57.863  25.156  23.507  1.00 39.39  ? 37  ARG D HD2    1 
ATOM   5719  H  HD3    . ARG C 2 38  ? 57.242  25.793  24.824  1.00 39.39  ? 37  ARG D HD3    1 
ATOM   5720  H  HE     . ARG C 2 38  ? 57.806  23.980  25.873  1.00 45.76  ? 37  ARG D HE     1 
ATOM   5721  H  HH11   . ARG C 2 38  ? 57.735  23.082  22.667  1.00 45.27  ? 37  ARG D HH11   1 
ATOM   5722  H  HH12   . ARG C 2 38  ? 58.224  21.693  22.894  1.00 45.27  ? 37  ARG D HH12   1 
ATOM   5723  H  HH21   . ARG C 2 38  ? 58.546  21.878  26.165  1.00 43.40  ? 37  ARG D HH21   1 
ATOM   5724  H  HH22   . ARG C 2 38  ? 58.711  20.969  24.996  1.00 43.40  ? 37  ARG D HH22   1 
ATOM   5725  N  N      . ALA C 2 39  ? 54.220  21.788  25.291  1.00 31.86  ? 38  ALA D N      1 
ATOM   5726  C  CA     . ALA C 2 39  ? 54.632  20.394  25.126  1.00 35.90  ? 38  ALA D CA     1 
ATOM   5727  C  C      . ALA C 2 39  ? 53.485  19.510  24.659  1.00 34.49  ? 38  ALA D C      1 
ATOM   5728  O  O      . ALA C 2 39  ? 53.725  18.582  23.872  1.00 34.68  ? 38  ALA D O      1 
ATOM   5729  C  CB     . ALA C 2 39  ? 55.235  19.840  26.429  1.00 35.22  ? 38  ALA D CB     1 
ATOM   5730  H  H      . ALA C 2 39  ? 54.243  22.080  26.099  1.00 38.26  ? 38  ALA D H      1 
ATOM   5731  H  HA     . ALA C 2 39  ? 55.326  20.369  24.449  1.00 43.11  ? 38  ALA D HA     1 
ATOM   5732  H  HB1    . ALA C 2 39  ? 55.484  18.913  26.292  1.00 42.30  ? 38  ALA D HB1    1 
ATOM   5733  H  HB2    . ALA C 2 39  ? 56.020  20.362  26.661  1.00 42.30  ? 38  ALA D HB2    1 
ATOM   5734  H  HB3    . ALA C 2 39  ? 54.574  19.905  27.135  1.00 42.30  ? 38  ALA D HB3    1 
ATOM   5735  N  N      . LEU C 2 40  ? 52.239  19.787  25.097  1.00 30.81  ? 39  LEU D N      1 
ATOM   5736  C  CA     . LEU C 2 40  ? 51.097  19.004  24.638  1.00 33.25  ? 39  LEU D CA     1 
ATOM   5737  C  C      . LEU C 2 40  ? 50.752  19.281  23.177  1.00 34.61  ? 39  LEU D C      1 
ATOM   5738  O  O      . LEU C 2 40  ? 50.119  18.447  22.519  1.00 33.83  ? 39  LEU D O      1 
ATOM   5739  C  CB     . LEU C 2 40  ? 49.869  19.288  25.497  1.00 28.00  ? 39  LEU D CB     1 
ATOM   5740  C  CG     . LEU C 2 40  ? 49.893  18.849  26.960  1.00 36.06  ? 39  LEU D CG     1 
ATOM   5741  C  CD1    . LEU C 2 40  ? 48.717  19.487  27.680  1.00 31.43  ? 39  LEU D CD1    1 
ATOM   5742  C  CD2    . LEU C 2 40  ? 49.856  17.350  27.032  1.00 38.39  ? 39  LEU D CD2    1 
ATOM   5743  H  H      . LEU C 2 40  ? 52.040  20.415  25.651  1.00 37.00  ? 39  LEU D H      1 
ATOM   5744  H  HA     . LEU C 2 40  ? 51.334  18.067  24.728  1.00 39.94  ? 39  LEU D HA     1 
ATOM   5745  H  HB2    . LEU C 2 40  ? 49.727  20.248  25.497  1.00 33.63  ? 39  LEU D HB2    1 
ATOM   5746  H  HB3    . LEU C 2 40  ? 49.113  18.841  25.085  1.00 33.63  ? 39  LEU D HB3    1 
ATOM   5747  H  HG     . LEU C 2 40  ? 50.705  19.137  27.405  1.00 43.31  ? 39  LEU D HG     1 
ATOM   5748  H  HD11   . LEU C 2 40  ? 48.709  19.185  28.602  1.00 37.75  ? 39  LEU D HD11   1 
ATOM   5749  H  HD12   . LEU C 2 40  ? 48.814  20.452  27.650  1.00 37.75  ? 39  LEU D HD12   1 
ATOM   5750  H  HD13   . LEU C 2 40  ? 47.895  19.223  27.239  1.00 37.75  ? 39  LEU D HD13   1 
ATOM   5751  H  HD21   . LEU C 2 40  ? 49.844  17.079  27.963  1.00 46.11  ? 39  LEU D HD21   1 
ATOM   5752  H  HD22   . LEU C 2 40  ? 49.056  17.032  26.585  1.00 46.11  ? 39  LEU D HD22   1 
ATOM   5753  H  HD23   . LEU C 2 40  ? 50.644  16.993  26.593  1.00 46.11  ? 39  LEU D HD23   1 
ATOM   5754  N  N      . SER C 2 41  ? 51.108  20.463  22.668  1.00 32.82  ? 40  SER D N      1 
ATOM   5755  C  CA     . SER C 2 41  ? 50.885  20.762  21.254  1.00 32.47  ? 40  SER D CA     1 
ATOM   5756  C  C      . SER C 2 41  ? 51.937  20.101  20.363  1.00 32.73  ? 40  SER D C      1 
ATOM   5757  O  O      . SER C 2 41  ? 51.654  19.807  19.200  1.00 31.33  ? 40  SER D O      1 
ATOM   5758  C  CB     . SER C 2 41  ? 50.903  22.273  21.007  1.00 31.02  ? 40  SER D CB     1 
ATOM   5759  O  OG     . SER C 2 41  ? 49.974  22.969  21.815  1.00 29.72  ? 40  SER D OG     1 
ATOM   5760  H  H      . SER C 2 41  ? 51.476  21.099  23.114  1.00 39.42  ? 40  SER D H      1 
ATOM   5761  H  HA     . SER C 2 41  ? 50.007  20.429  21.013  1.00 39.00  ? 40  SER D HA     1 
ATOM   5762  H  HB2    . SER C 2 41  ? 51.793  22.607  21.202  1.00 37.26  ? 40  SER D HB2    1 
ATOM   5763  H  HB3    . SER C 2 41  ? 50.685  22.435  20.076  1.00 37.26  ? 40  SER D HB3    1 
ATOM   5764  H  HG     . SER C 2 41  ? 50.122  22.808  22.626  1.00 35.70  ? 40  SER D HG     1 
ATOM   5765  N  N      . THR C 2 42  ? 53.160  19.887  20.867  1.00 34.17  ? 41  THR D N      1 
ATOM   5766  C  CA     . THR C 2 42  ? 54.147  19.164  20.070  1.00 35.93  ? 41  THR D CA     1 
ATOM   5767  C  C      . THR C 2 42  ? 54.033  17.642  20.205  1.00 39.16  ? 41  THR D C      1 
ATOM   5768  O  O      . THR C 2 42  ? 54.564  16.917  19.345  1.00 37.32  ? 41  THR D O      1 
ATOM   5769  C  CB     . THR C 2 42  ? 55.578  19.580  20.425  1.00 37.90  ? 41  THR D CB     1 
ATOM   5770  O  OG1    . THR C 2 42  ? 55.914  19.134  21.750  1.00 37.08  ? 41  THR D OG1    1 
ATOM   5771  C  CG2    . THR C 2 42  ? 55.746  21.103  20.303  1.00 35.83  ? 41  THR D CG2    1 
ATOM   5772  H  H      . THR C 2 42  ? 53.430  20.144  21.642  1.00 41.04  ? 41  THR D H      1 
ATOM   5773  H  HA     . THR C 2 42  ? 53.992  19.407  19.144  1.00 43.15  ? 41  THR D HA     1 
ATOM   5774  H  HB     . THR C 2 42  ? 56.198  19.166  19.804  1.00 45.52  ? 41  THR D HB     1 
ATOM   5775  H  HG1    . THR C 2 42  ? 56.700  19.361  21.939  1.00 44.53  ? 41  THR D HG1    1 
ATOM   5776  H  HG21   . THR C 2 42  ? 56.666  21.351  20.483  1.00 43.03  ? 41  THR D HG21   1 
ATOM   5777  H  HG22   . THR C 2 42  ? 55.511  21.392  19.407  1.00 43.03  ? 41  THR D HG22   1 
ATOM   5778  H  HG23   . THR C 2 42  ? 55.168  21.552  20.940  1.00 43.03  ? 41  THR D HG23   1 
ATOM   5779  N  N      . GLY C 2 43  ? 53.344  17.145  21.235  1.00 34.05  ? 42  GLY D N      1 
ATOM   5780  C  CA     . GLY C 2 43  ? 53.296  15.717  21.506  1.00 37.76  ? 42  GLY D CA     1 
ATOM   5781  C  C      . GLY C 2 43  ? 54.618  15.119  21.948  1.00 40.86  ? 42  GLY D C      1 
ATOM   5782  O  O      . GLY C 2 43  ? 54.768  13.887  21.960  1.00 39.22  ? 42  GLY D O      1 
ATOM   5783  H  H      . GLY C 2 43  ? 52.895  17.621  21.793  1.00 40.89  ? 42  GLY D H      1 
ATOM   5784  H  HA2    . GLY C 2 43  ? 52.645  15.553  22.206  1.00 45.35  ? 42  GLY D HA2    1 
ATOM   5785  H  HA3    . GLY C 2 43  ? 53.015  15.255  20.700  1.00 45.35  ? 42  GLY D HA3    1 
ATOM   5786  N  N      . GLU C 2 44  ? 55.581  15.955  22.341  1.00 39.75  ? 43  GLU D N      1 
ATOM   5787  C  CA     . GLU C 2 44  ? 56.936  15.470  22.565  1.00 38.75  ? 43  GLU D CA     1 
ATOM   5788  C  C      . GLU C 2 44  ? 57.086  14.581  23.794  1.00 40.14  ? 43  GLU D C      1 
ATOM   5789  O  O      . GLU C 2 44  ? 58.107  13.899  23.909  1.00 41.95  ? 43  GLU D O      1 
ATOM   5790  C  CB     . GLU C 2 44  ? 57.892  16.658  22.652  1.00 41.63  ? 43  GLU D CB     1 
ATOM   5791  C  CG     . GLU C 2 44  ? 57.688  17.573  23.842  1.00 42.67  ? 43  GLU D CG     1 
ATOM   5792  C  CD     . GLU C 2 44  ? 58.525  18.826  23.696  1.00 39.73  ? 43  GLU D CD     1 
ATOM   5793  O  OE1    . GLU C 2 44  ? 58.309  19.552  22.697  1.00 34.21  ? 43  GLU D OE1    1 
ATOM   5794  O  OE2    . GLU C 2 44  ? 59.423  19.061  24.539  1.00 39.02  ? 43  GLU D OE2    1 
ATOM   5795  H  H      . GLU C 2 44  ? 55.473  16.797  22.483  1.00 47.73  ? 43  GLU D H      1 
ATOM   5796  H  HA     . GLU C 2 44  ? 57.186  14.921  21.805  1.00 46.54  ? 43  GLU D HA     1 
ATOM   5797  H  HB2    . GLU C 2 44  ? 58.799  16.316  22.702  1.00 49.99  ? 43  GLU D HB2    1 
ATOM   5798  H  HB3    . GLU C 2 44  ? 57.785  17.195  21.852  1.00 49.99  ? 43  GLU D HB3    1 
ATOM   5799  H  HG2    . GLU C 2 44  ? 56.754  17.830  23.898  1.00 51.24  ? 43  GLU D HG2    1 
ATOM   5800  H  HG3    . GLU C 2 44  ? 57.955  17.115  24.654  1.00 51.24  ? 43  GLU D HG3    1 
ATOM   5801  N  N      . LYS C 2 45  ? 56.118  14.563  24.708  1.00 39.88  ? 44  LYS D N      1 
ATOM   5802  C  CA     . LYS C 2 45  ? 56.141  13.648  25.847  1.00 41.46  ? 44  LYS D CA     1 
ATOM   5803  C  C      . LYS C 2 45  ? 55.366  12.354  25.576  1.00 45.73  ? 44  LYS D C      1 
ATOM   5804  O  O      . LYS C 2 45  ? 55.069  11.614  26.520  1.00 47.41  ? 44  LYS D O      1 
ATOM   5805  C  CB     . LYS C 2 45  ? 55.540  14.316  27.091  1.00 45.63  ? 44  LYS D CB     1 
ATOM   5806  C  CG     . LYS C 2 45  ? 56.061  15.699  27.450  1.00 42.67  ? 44  LYS D CG     1 
ATOM   5807  C  CD     . LYS C 2 45  ? 57.539  15.742  27.749  1.00 47.19  ? 44  LYS D CD     1 
ATOM   5808  C  CE     . LYS C 2 45  ? 57.921  17.097  28.332  1.00 48.57  ? 44  LYS D CE     1 
ATOM   5809  N  NZ     . LYS C 2 45  ? 59.385  17.272  28.375  1.00 48.64  ? 44  LYS D NZ     1 
ATOM   5810  H  H      . LYS C 2 45  ? 55.429  15.077  24.690  1.00 47.89  ? 44  LYS D H      1 
ATOM   5811  H  HA     . LYS C 2 45  ? 57.068  13.431  26.031  1.00 49.79  ? 44  LYS D HA     1 
ATOM   5812  H  HB2    . LYS C 2 45  ? 54.584  14.402  26.952  1.00 54.79  ? 44  LYS D HB2    1 
ATOM   5813  H  HB3    . LYS C 2 45  ? 55.715  13.742  27.853  1.00 54.79  ? 44  LYS D HB3    1 
ATOM   5814  H  HG2    . LYS C 2 45  ? 55.895  16.298  26.705  1.00 51.24  ? 44  LYS D HG2    1 
ATOM   5815  H  HG3    . LYS C 2 45  ? 55.592  16.014  28.239  1.00 51.24  ? 44  LYS D HG3    1 
ATOM   5816  H  HD2    . LYS C 2 45  ? 57.761  15.053  28.394  1.00 56.67  ? 44  LYS D HD2    1 
ATOM   5817  H  HD3    . LYS C 2 45  ? 58.041  15.604  26.930  1.00 56.67  ? 44  LYS D HD3    1 
ATOM   5818  H  HE2    . LYS C 2 45  ? 57.545  17.802  27.782  1.00 58.32  ? 44  LYS D HE2    1 
ATOM   5819  H  HE3    . LYS C 2 45  ? 57.579  17.165  29.238  1.00 58.32  ? 44  LYS D HE3    1 
ATOM   5820  H  HZ1    . LYS C 2 45  ? 59.586  18.070  28.715  1.00 58.41  ? 44  LYS D HZ1    1 
ATOM   5821  H  HZ2    . LYS C 2 45  ? 59.752  16.641  28.882  1.00 58.41  ? 44  LYS D HZ2    1 
ATOM   5822  H  HZ3    . LYS C 2 45  ? 59.722  17.215  27.553  1.00 58.41  ? 44  LYS D HZ3    1 
ATOM   5823  N  N      . GLY C 2 46  ? 54.974  12.102  24.327  1.00 42.50  ? 45  GLY D N      1 
ATOM   5824  C  CA     . GLY C 2 46  ? 54.250  10.900  23.972  1.00 40.91  ? 45  GLY D CA     1 
ATOM   5825  C  C      . GLY C 2 46  ? 52.734  10.988  24.032  1.00 43.35  ? 45  GLY D C      1 
ATOM   5826  O  O      . GLY C 2 46  ? 52.061  9.984   23.757  1.00 44.87  ? 45  GLY D O      1 
ATOM   5827  H  H      . GLY C 2 46  ? 55.122  12.625  23.661  1.00 51.03  ? 45  GLY D H      1 
ATOM   5828  H  HA2    . GLY C 2 46  ? 54.491  10.655  23.064  1.00 49.12  ? 45  GLY D HA2    1 
ATOM   5829  H  HA3    . GLY C 2 46  ? 54.524  10.190  24.573  1.00 49.12  ? 45  GLY D HA3    1 
ATOM   5830  N  N      . PHE C 2 47  ? 52.175  12.154  24.368  1.00 42.16  ? 46  PHE D N      1 
ATOM   5831  C  CA     . PHE C 2 47  ? 50.734  12.367  24.421  1.00 41.72  ? 46  PHE D CA     1 
ATOM   5832  C  C      . PHE C 2 47  ? 50.488  13.851  24.206  1.00 38.10  ? 46  PHE D C      1 
ATOM   5833  O  O      . PHE C 2 47  ? 51.411  14.667  24.301  1.00 39.10  ? 46  PHE D O      1 
ATOM   5834  C  CB     . PHE C 2 47  ? 50.150  11.884  25.749  1.00 41.39  ? 46  PHE D CB     1 
ATOM   5835  C  CG     . PHE C 2 47  ? 50.827  12.464  26.952  1.00 43.09  ? 46  PHE D CG     1 
ATOM   5836  C  CD1    . PHE C 2 47  ? 50.542  13.746  27.379  1.00 41.85  ? 46  PHE D CD1    1 
ATOM   5837  C  CD2    . PHE C 2 47  ? 51.776  11.730  27.651  1.00 45.76  ? 46  PHE D CD2    1 
ATOM   5838  C  CE1    . PHE C 2 47  ? 51.178  14.284  28.489  1.00 40.66  ? 46  PHE D CE1    1 
ATOM   5839  C  CE2    . PHE C 2 47  ? 52.428  12.274  28.764  1.00 43.86  ? 46  PHE D CE2    1 
ATOM   5840  C  CZ     . PHE C 2 47  ? 52.126  13.545  29.180  1.00 43.98  ? 46  PHE D CZ     1 
ATOM   5841  H  H      . PHE C 2 47  ? 52.626  12.856  24.576  1.00 50.63  ? 46  PHE D H      1 
ATOM   5842  H  HA     . PHE C 2 47  ? 50.283  11.876  23.716  1.00 50.10  ? 46  PHE D HA     1 
ATOM   5843  H  HB2    . PHE C 2 47  ? 49.213  12.134  25.787  1.00 49.70  ? 46  PHE D HB2    1 
ATOM   5844  H  HB3    . PHE C 2 47  ? 50.238  10.919  25.796  1.00 49.70  ? 46  PHE D HB3    1 
ATOM   5845  H  HD1    . PHE C 2 47  ? 49.916  14.255  26.917  1.00 50.26  ? 46  PHE D HD1    1 
ATOM   5846  H  HD2    . PHE C 2 47  ? 51.981  10.865  27.377  1.00 54.95  ? 46  PHE D HD2    1 
ATOM   5847  H  HE1    . PHE C 2 47  ? 50.967  15.145  28.771  1.00 48.82  ? 46  PHE D HE1    1 
ATOM   5848  H  HE2    . PHE C 2 47  ? 53.065  11.774  29.221  1.00 52.66  ? 46  PHE D HE2    1 
ATOM   5849  H  HZ     . PHE C 2 47  ? 52.555  13.909  29.920  1.00 52.81  ? 46  PHE D HZ     1 
ATOM   5850  N  N      . GLY C 2 48  ? 49.257  14.196  23.859  1.00 38.16  ? 47  GLY D N      1 
ATOM   5851  C  CA     . GLY C 2 48  ? 48.933  15.601  23.711  1.00 31.65  ? 47  GLY D CA     1 
ATOM   5852  C  C      . GLY C 2 48  ? 47.706  15.791  22.836  1.00 35.89  ? 47  GLY D C      1 
ATOM   5853  O  O      . GLY C 2 48  ? 46.892  14.880  22.667  1.00 32.61  ? 47  GLY D O      1 
ATOM   5854  H  H      . GLY C 2 48  ? 48.610  13.649  23.708  1.00 45.82  ? 47  GLY D H      1 
ATOM   5855  H  HA2    . GLY C 2 48  ? 48.756  15.989  24.582  1.00 38.01  ? 47  GLY D HA2    1 
ATOM   5856  H  HA3    . GLY C 2 48  ? 49.680  16.067  23.303  1.00 38.01  ? 47  GLY D HA3    1 
ATOM   5857  N  N      . TYR C 2 49  ? 47.632  16.994  22.252  1.00 33.15  ? 48  TYR D N      1 
ATOM   5858  C  CA     . TYR C 2 49  ? 46.393  17.479  21.691  1.00 32.60  ? 48  TYR D CA     1 
ATOM   5859  C  C      . TYR C 2 49  ? 46.096  16.903  20.319  1.00 31.44  ? 48  TYR D C      1 
ATOM   5860  O  O      . TYR C 2 49  ? 44.941  16.913  19.904  1.00 29.83  ? 48  TYR D O      1 
ATOM   5861  C  CB     . TYR C 2 49  ? 46.428  19.002  21.597  1.00 26.76  ? 48  TYR D CB     1 
ATOM   5862  C  CG     . TYR C 2 49  ? 46.386  19.739  22.943  1.00 28.86  ? 48  TYR D CG     1 
ATOM   5863  C  CD1    . TYR C 2 49  ? 45.400  19.462  23.892  1.00 28.44  ? 48  TYR D CD1    1 
ATOM   5864  C  CD2    . TYR C 2 49  ? 47.303  20.735  23.224  1.00 32.19  ? 48  TYR D CD2    1 
ATOM   5865  C  CE1    . TYR C 2 49  ? 45.348  20.165  25.111  1.00 31.87  ? 48  TYR D CE1    1 
ATOM   5866  C  CE2    . TYR C 2 49  ? 47.269  21.431  24.420  1.00 30.34  ? 48  TYR D CE2    1 
ATOM   5867  C  CZ     . TYR C 2 49  ? 46.296  21.150  25.351  1.00 26.19  ? 48  TYR D CZ     1 
ATOM   5868  O  OH     . TYR C 2 49  ? 46.290  21.864  26.514  1.00 29.41  ? 48  TYR D OH     1 
ATOM   5869  H  H      . TYR C 2 49  ? 48.292  17.539  22.175  1.00 39.81  ? 48  TYR D H      1 
ATOM   5870  H  HA     . TYR C 2 49  ? 45.668  17.222  22.282  1.00 39.15  ? 48  TYR D HA     1 
ATOM   5871  H  HB2    . TYR C 2 49  ? 47.249  19.262  21.149  1.00 32.14  ? 48  TYR D HB2    1 
ATOM   5872  H  HB3    . TYR C 2 49  ? 45.661  19.295  21.081  1.00 32.14  ? 48  TYR D HB3    1 
ATOM   5873  H  HD1    . TYR C 2 49  ? 44.768  18.803  23.716  1.00 34.17  ? 48  TYR D HD1    1 
ATOM   5874  H  HD2    . TYR C 2 49  ? 47.958  20.941  22.596  1.00 38.66  ? 48  TYR D HD2    1 
ATOM   5875  H  HE1    . TYR C 2 49  ? 44.693  19.973  25.742  1.00 38.28  ? 48  TYR D HE1    1 
ATOM   5876  H  HE2    . TYR C 2 49  ? 47.904  22.089  24.594  1.00 36.44  ? 48  TYR D HE2    1 
ATOM   5877  H  HH     . TYR C 2 49  ? 45.691  21.574  27.027  1.00 35.33  ? 48  TYR D HH     1 
ATOM   5878  N  N      . LYS C 2 50  ? 47.100  16.414  19.600  1.00 29.98  ? 49  LYS D N      1 
ATOM   5879  C  CA     . LYS C 2 50  ? 46.811  15.961  18.236  1.00 32.33  ? 49  LYS D CA     1 
ATOM   5880  C  C      . LYS C 2 50  ? 45.685  14.921  18.244  1.00 33.02  ? 49  LYS D C      1 
ATOM   5881  O  O      . LYS C 2 50  ? 45.708  13.963  19.017  1.00 36.59  ? 49  LYS D O      1 
ATOM   5882  C  CB     . LYS C 2 50  ? 48.084  15.396  17.602  1.00 34.63  ? 49  LYS D CB     1 
ATOM   5883  C  CG     . LYS C 2 50  ? 47.883  14.889  16.159  1.00 35.62  ? 49  LYS D CG     1 
ATOM   5884  C  CD     . LYS C 2 50  ? 49.233  14.684  15.504  1.00 40.96  ? 49  LYS D CD     1 
ATOM   5885  C  CE     . LYS C 2 50  ? 49.127  14.032  14.135  1.00 42.53  ? 49  LYS D CE     1 
ATOM   5886  N  NZ     . LYS C 2 50  ? 50.507  13.881  13.553  1.00 46.40  ? 49  LYS D NZ     1 
ATOM   5887  H  H      . LYS C 2 50  ? 47.915  16.335  19.861  1.00 36.01  ? 49  LYS D H      1 
ATOM   5888  H  HA     . LYS C 2 50  ? 46.513  16.709  17.694  1.00 38.83  ? 49  LYS D HA     1 
ATOM   5889  H  HB2    . LYS C 2 50  ? 48.758  16.093  17.581  1.00 41.60  ? 49  LYS D HB2    1 
ATOM   5890  H  HB3    . LYS C 2 50  ? 48.395  14.650  18.138  1.00 41.60  ? 49  LYS D HB3    1 
ATOM   5891  H  HG2    . LYS C 2 50  ? 47.408  14.043  16.170  1.00 42.78  ? 49  LYS D HG2    1 
ATOM   5892  H  HG3    . LYS C 2 50  ? 47.383  15.544  15.647  1.00 42.78  ? 49  LYS D HG3    1 
ATOM   5893  H  HD2    . LYS C 2 50  ? 49.665  15.545  15.393  1.00 49.18  ? 49  LYS D HD2    1 
ATOM   5894  H  HD3    . LYS C 2 50  ? 49.775  14.111  16.068  1.00 49.18  ? 49  LYS D HD3    1 
ATOM   5895  H  HE2    . LYS C 2 50  ? 48.723  13.154  14.217  1.00 51.07  ? 49  LYS D HE2    1 
ATOM   5896  H  HE3    . LYS C 2 50  ? 48.596  14.588  13.544  1.00 51.07  ? 49  LYS D HE3    1 
ATOM   5897  H  HZ1    . LYS C 2 50  ? 50.460  13.492  12.754  1.00 55.71  ? 49  LYS D HZ1    1 
ATOM   5898  H  HZ2    . LYS C 2 50  ? 50.889  14.680  13.464  1.00 55.71  ? 49  LYS D HZ2    1 
ATOM   5899  H  HZ3    . LYS C 2 50  ? 51.010  13.379  14.089  1.00 55.71  ? 49  LYS D HZ3    1 
ATOM   5900  N  N      . GLY C 2 51  ? 44.693  15.106  17.378  1.00 31.65  ? 50  GLY D N      1 
ATOM   5901  C  CA     . GLY C 2 51  ? 43.587  14.186  17.304  1.00 34.29  ? 50  GLY D CA     1 
ATOM   5902  C  C      . GLY C 2 51  ? 42.438  14.481  18.240  1.00 31.05  ? 50  GLY D C      1 
ATOM   5903  O  O      . GLY C 2 51  ? 41.330  13.986  18.006  1.00 35.31  ? 50  GLY D O      1 
ATOM   5904  H  H      . GLY C 2 51  ? 44.646  15.763  16.825  1.00 38.02  ? 50  GLY D H      1 
ATOM   5905  H  HA2    . GLY C 2 51  ? 43.238  14.195  16.399  1.00 41.18  ? 50  GLY D HA2    1 
ATOM   5906  H  HA3    . GLY C 2 51  ? 43.911  13.296  17.509  1.00 41.18  ? 50  GLY D HA3    1 
ATOM   5907  N  N      . SER C 2 52  ? 42.637  15.305  19.256  1.00 33.56  ? 51  SER D N      1 
ATOM   5908  C  CA     . SER C 2 52  ? 41.537  15.561  20.180  1.00 31.91  ? 51  SER D CA     1 
ATOM   5909  C  C      . SER C 2 52  ? 40.544  16.550  19.568  1.00 30.16  ? 51  SER D C      1 
ATOM   5910  O  O      . SER C 2 52  ? 40.795  17.148  18.519  1.00 30.76  ? 51  SER D O      1 
ATOM   5911  C  CB     . SER C 2 52  ? 42.063  16.075  21.520  1.00 31.44  ? 51  SER D CB     1 
ATOM   5912  O  OG     . SER C 2 52  ? 42.682  17.350  21.396  1.00 30.55  ? 51  SER D OG     1 
ATOM   5913  H  H      . SER C 2 52  ? 43.373  15.715  19.430  1.00 40.31  ? 51  SER D H      1 
ATOM   5914  H  HA     . SER C 2 52  ? 41.066  14.730  20.349  1.00 38.33  ? 51  SER D HA     1 
ATOM   5915  H  HB2    . SER C 2 52  ? 41.319  16.149  22.138  1.00 37.77  ? 51  SER D HB2    1 
ATOM   5916  H  HB3    . SER C 2 52  ? 42.716  15.444  21.861  1.00 37.77  ? 51  SER D HB3    1 
ATOM   5917  H  HG     . SER C 2 52  ? 43.348  17.298  20.888  1.00 36.70  ? 51  SER D HG     1 
ATOM   5918  N  N      . CYS C 2 53  ? 39.390  16.717  20.231  1.00 29.10  ? 52  CYS D N      1 
ATOM   5919  C  CA     . CYS C 2 53  ? 38.344  17.582  19.702  1.00 29.91  ? 52  CYS D CA     1 
ATOM   5920  C  C      . CYS C 2 53  ? 37.959  18.742  20.620  1.00 29.08  ? 52  CYS D C      1 
ATOM   5921  O  O      . CYS C 2 53  ? 38.300  18.791  21.799  1.00 28.07  ? 52  CYS D O      1 
ATOM   5922  C  CB     . CYS C 2 53  ? 37.069  16.781  19.382  1.00 37.30  ? 52  CYS D CB     1 
ATOM   5923  S  SG     . CYS C 2 53  ? 36.144  16.253  20.845  1.00 48.62  ? 52  CYS D SG     1 
ATOM   5924  H  H      . CYS C 2 53  ? 39.199  16.341  20.980  1.00 34.96  ? 52  CYS D H      1 
ATOM   5925  H  HA     . CYS C 2 53  ? 38.717  17.983  18.901  1.00 35.93  ? 52  CYS D HA     1 
ATOM   5926  H  HB2    . CYS C 2 53  ? 36.480  17.336  18.845  1.00 44.79  ? 52  CYS D HB2    1 
ATOM   5927  H  HB3    . CYS C 2 53  ? 37.317  15.985  18.886  1.00 44.79  ? 52  CYS D HB3    1 
ATOM   5928  H  HG     . CYS C 2 53  ? 35.782  17.224  21.451  1.00 58.38  ? 52  CYS D HG     1 
ATOM   5929  N  N      . PHE C 2 54  ? 37.272  19.717  20.035  1.00 25.34  ? 53  PHE D N      1 
ATOM   5930  C  CA     . PHE C 2 54  ? 36.652  20.804  20.783  1.00 24.86  ? 53  PHE D CA     1 
ATOM   5931  C  C      . PHE C 2 54  ? 35.247  20.357  21.155  1.00 27.17  ? 53  PHE D C      1 
ATOM   5932  O  O      . PHE C 2 54  ? 34.361  20.327  20.294  1.00 25.79  ? 53  PHE D O      1 
ATOM   5933  C  CB     . PHE C 2 54  ? 36.590  22.094  19.970  1.00 24.41  ? 53  PHE D CB     1 
ATOM   5934  C  CG     . PHE C 2 54  ? 37.876  22.883  19.984  1.00 24.53  ? 53  PHE D CG     1 
ATOM   5935  C  CD1    . PHE C 2 54  ? 38.925  22.535  19.165  1.00 22.76  ? 53  PHE D CD1    1 
ATOM   5936  C  CD2    . PHE C 2 54  ? 38.018  23.972  20.825  1.00 25.58  ? 53  PHE D CD2    1 
ATOM   5937  C  CE1    . PHE C 2 54  ? 40.138  23.261  19.180  1.00 23.66  ? 53  PHE D CE1    1 
ATOM   5938  C  CE2    . PHE C 2 54  ? 39.224  24.704  20.847  1.00 23.41  ? 53  PHE D CE2    1 
ATOM   5939  C  CZ     . PHE C 2 54  ? 40.277  24.333  20.015  1.00 25.45  ? 53  PHE D CZ     1 
ATOM   5940  H  H      . PHE C 2 54  ? 37.147  19.772  19.186  1.00 30.44  ? 53  PHE D H      1 
ATOM   5941  H  HA     . PHE C 2 54  ? 37.178  20.980  21.578  1.00 29.87  ? 53  PHE D HA     1 
ATOM   5942  H  HB2    . PHE C 2 54  ? 36.388  21.872  19.047  1.00 29.32  ? 53  PHE D HB2    1 
ATOM   5943  H  HB3    . PHE C 2 54  ? 35.891  22.660  20.335  1.00 29.32  ? 53  PHE D HB3    1 
ATOM   5944  H  HD1    . PHE C 2 54  ? 38.835  21.809  18.590  1.00 27.34  ? 53  PHE D HD1    1 
ATOM   5945  H  HD2    . PHE C 2 54  ? 37.314  24.224  21.378  1.00 30.73  ? 53  PHE D HD2    1 
ATOM   5946  H  HE1    . PHE C 2 54  ? 40.839  23.010  18.624  1.00 28.43  ? 53  PHE D HE1    1 
ATOM   5947  H  HE2    . PHE C 2 54  ? 39.317  25.433  21.418  1.00 28.13  ? 53  PHE D HE2    1 
ATOM   5948  H  HZ     . PHE C 2 54  ? 41.073  24.813  20.028  1.00 30.58  ? 53  PHE D HZ     1 
ATOM   5949  N  N      . HIS C 2 55  ? 35.046  20.001  22.418  1.00 25.99  ? 54  HIS D N      1 
ATOM   5950  C  CA     . HIS C 2 55  ? 33.801  19.366  22.819  1.00 24.47  ? 54  HIS D CA     1 
ATOM   5951  C  C      . HIS C 2 55  ? 32.720  20.347  23.209  1.00 30.10  ? 54  HIS D C      1 
ATOM   5952  O  O      . HIS C 2 55  ? 31.539  19.974  23.214  1.00 28.25  ? 54  HIS D O      1 
ATOM   5953  C  CB     . HIS C 2 55  ? 34.040  18.397  23.971  1.00 26.41  ? 54  HIS D CB     1 
ATOM   5954  C  CG     . HIS C 2 55  ? 34.636  19.040  25.189  1.00 27.09  ? 54  HIS D CG     1 
ATOM   5955  N  ND1    . HIS C 2 55  ? 35.994  19.270  25.317  1.00 26.97  ? 54  HIS D ND1    1 
ATOM   5956  C  CD2    . HIS C 2 55  ? 34.067  19.470  26.342  1.00 26.72  ? 54  HIS D CD2    1 
ATOM   5957  C  CE1    . HIS C 2 55  ? 36.226  19.837  26.487  1.00 27.91  ? 54  HIS D CE1    1 
ATOM   5958  N  NE2    . HIS C 2 55  ? 35.077  19.969  27.127  1.00 25.83  ? 54  HIS D NE2    1 
ATOM   5959  H  H      . HIS C 2 55  ? 35.611  20.116  23.055  1.00 31.22  ? 54  HIS D H      1 
ATOM   5960  H  HA     . HIS C 2 55  ? 33.470  18.853  22.065  1.00 29.40  ? 54  HIS D HA     1 
ATOM   5961  H  HB2    . HIS C 2 55  ? 33.192  18.004  24.228  1.00 31.72  ? 54  HIS D HB2    1 
ATOM   5962  H  HB3    . HIS C 2 55  ? 34.651  17.705  23.673  1.00 31.72  ? 54  HIS D HB3    1 
ATOM   5963  H  HD2    . HIS C 2 55  ? 33.163  19.434  26.559  1.00 32.10  ? 54  HIS D HD2    1 
ATOM   5964  H  HE1    . HIS C 2 55  ? 37.059  20.098  26.807  1.00 33.53  ? 54  HIS D HE1    1 
ATOM   5965  H  HE2    . HIS C 2 55  ? 34.978  20.312  27.909  1.00 31.02  ? 54  HIS D HE2    1 
ATOM   5966  N  N      . ARG C 2 56  ? 33.080  21.601  23.488  1.00 23.34  ? 55  ARG D N      1 
ATOM   5967  C  CA     . ARG C 2 56  ? 32.117  22.592  23.944  1.00 20.30  ? 55  ARG D CA     1 
ATOM   5968  C  C      . ARG C 2 56  ? 32.376  23.891  23.210  1.00 25.83  ? 55  ARG D C      1 
ATOM   5969  O  O      . ARG C 2 56  ? 33.437  24.496  23.386  1.00 23.88  ? 55  ARG D O      1 
ATOM   5970  C  CB     . ARG C 2 56  ? 32.229  22.807  25.466  1.00 24.65  ? 55  ARG D CB     1 
ATOM   5971  C  CG     . ARG C 2 56  ? 31.398  23.960  26.010  1.00 24.32  ? 55  ARG D CG     1 
ATOM   5972  C  CD     . ARG C 2 56  ? 31.544  24.055  27.552  1.00 25.88  ? 55  ARG D CD     1 
ATOM   5973  N  NE     . ARG C 2 56  ? 31.074  22.824  28.179  1.00 30.05  ? 55  ARG D NE     1 
ATOM   5974  C  CZ     . ARG C 2 56  ? 31.472  22.381  29.365  1.00 31.24  ? 55  ARG D CZ     1 
ATOM   5975  N  NH1    . ARG C 2 56  ? 32.456  22.967  30.023  1.00 29.99  ? 55  ARG D NH1    1 
ATOM   5976  N  NH2    . ARG C 2 56  ? 30.874  21.317  29.898  1.00 30.76  ? 55  ARG D NH2    1 
ATOM   5977  H  H      . ARG C 2 56  ? 33.883  21.900  23.419  1.00 28.05  ? 55  ARG D H      1 
ATOM   5978  H  HA     . ARG C 2 56  ? 31.218  22.292  23.736  1.00 24.39  ? 55  ARG D HA     1 
ATOM   5979  H  HB2    . ARG C 2 56  ? 31.934  21.998  25.914  1.00 29.61  ? 55  ARG D HB2    1 
ATOM   5980  H  HB3    . ARG C 2 56  ? 33.157  22.987  25.684  1.00 29.61  ? 55  ARG D HB3    1 
ATOM   5981  H  HG2    . ARG C 2 56  ? 31.704  24.794  25.619  1.00 29.22  ? 55  ARG D HG2    1 
ATOM   5982  H  HG3    . ARG C 2 56  ? 30.463  23.817  25.796  1.00 29.22  ? 55  ARG D HG3    1 
ATOM   5983  H  HD2    . ARG C 2 56  ? 32.477  24.184  27.784  1.00 31.09  ? 55  ARG D HD2    1 
ATOM   5984  H  HD3    . ARG C 2 56  ? 31.014  24.795  27.885  1.00 31.09  ? 55  ARG D HD3    1 
ATOM   5985  H  HE     . ARG C 2 56  ? 30.498  22.351  27.749  1.00 36.10  ? 55  ARG D HE     1 
ATOM   5986  H  HH11   . ARG C 2 56  ? 32.853  23.651  29.683  1.00 36.02  ? 55  ARG D HH11   1 
ATOM   5987  H  HH12   . ARG C 2 56  ? 32.700  22.666  30.790  1.00 36.02  ? 55  ARG D HH12   1 
ATOM   5988  H  HH21   . ARG C 2 56  ? 30.237  20.924  29.475  1.00 36.95  ? 55  ARG D HH21   1 
ATOM   5989  H  HH22   . ARG C 2 56  ? 31.125  21.022  30.666  1.00 36.95  ? 55  ARG D HH22   1 
ATOM   5990  N  N      . ILE C 2 57  ? 31.400  24.331  22.417  1.00 23.27  ? 56  ILE D N      1 
ATOM   5991  C  CA     . ILE C 2 57  ? 31.488  25.606  21.689  1.00 23.17  ? 56  ILE D CA     1 
ATOM   5992  C  C      . ILE C 2 57  ? 30.196  26.361  21.972  1.00 19.46  ? 56  ILE D C      1 
ATOM   5993  O  O      . ILE C 2 57  ? 29.108  25.921  21.572  1.00 21.61  ? 56  ILE D O      1 
ATOM   5994  C  CB     . ILE C 2 57  ? 31.704  25.415  20.193  1.00 19.59  ? 56  ILE D CB     1 
ATOM   5995  C  CG1    . ILE C 2 57  ? 32.960  24.587  19.898  1.00 23.17  ? 56  ILE D CG1    1 
ATOM   5996  C  CG2    . ILE C 2 57  ? 31.791  26.765  19.460  1.00 21.39  ? 56  ILE D CG2    1 
ATOM   5997  C  CD1    . ILE C 2 57  ? 33.089  24.265  18.416  1.00 25.90  ? 56  ILE D CD1    1 
ATOM   5998  H  H      . ILE C 2 57  ? 30.665  23.905  22.279  1.00 27.96  ? 56  ILE D H      1 
ATOM   5999  H  HA     . ILE C 2 57  ? 32.232  26.127  22.027  1.00 27.84  ? 56  ILE D HA     1 
ATOM   6000  H  HB     . ILE C 2 57  ? 30.931  24.928  19.866  1.00 23.54  ? 56  ILE D HB     1 
ATOM   6001  H  HG12   . ILE C 2 57  ? 33.745  25.088  20.170  1.00 27.83  ? 56  ILE D HG12   1 
ATOM   6002  H  HG13   . ILE C 2 57  ? 32.914  23.751  20.388  1.00 27.83  ? 56  ILE D HG13   1 
ATOM   6003  H  HG21   . ILE C 2 57  ? 31.844  26.604  18.505  1.00 25.70  ? 56  ILE D HG21   1 
ATOM   6004  H  HG22   . ILE C 2 57  ? 31.000  27.287  19.664  1.00 25.70  ? 56  ILE D HG22   1 
ATOM   6005  H  HG23   . ILE C 2 57  ? 32.584  27.237  19.760  1.00 25.70  ? 56  ILE D HG23   1 
ATOM   6006  H  HD11   . ILE C 2 57  ? 33.760  23.574  18.300  1.00 31.11  ? 56  ILE D HD11   1 
ATOM   6007  H  HD12   . ILE C 2 57  ? 32.232  23.953  18.085  1.00 31.11  ? 56  ILE D HD12   1 
ATOM   6008  H  HD13   . ILE C 2 57  ? 33.355  25.068  17.941  1.00 31.11  ? 56  ILE D HD13   1 
ATOM   6009  N  N      . ILE C 2 58  ? 30.310  27.485  22.656  1.00 19.38  ? 57  ILE D N      1 
ATOM   6010  C  CA     . ILE C 2 58  ? 29.180  28.321  23.040  1.00 19.20  ? 57  ILE D CA     1 
ATOM   6011  C  C      . ILE C 2 58  ? 29.364  29.676  22.366  1.00 21.05  ? 57  ILE D C      1 
ATOM   6012  O  O      . ILE C 2 58  ? 30.149  30.512  22.815  1.00 20.39  ? 57  ILE D O      1 
ATOM   6013  C  CB     . ILE C 2 58  ? 29.052  28.447  24.570  1.00 20.05  ? 57  ILE D CB     1 
ATOM   6014  C  CG1    . ILE C 2 58  ? 28.796  27.085  25.215  1.00 20.23  ? 57  ILE D CG1    1 
ATOM   6015  C  CG2    . ILE C 2 58  ? 27.906  29.369  24.968  1.00 23.54  ? 57  ILE D CG2    1 
ATOM   6016  C  CD1    . ILE C 2 58  ? 28.844  27.109  26.769  1.00 25.16  ? 57  ILE D CD1    1 
ATOM   6017  H  H      . ILE C 2 58  ? 31.064  27.801  22.922  1.00 23.29  ? 57  ILE D H      1 
ATOM   6018  H  HA     . ILE C 2 58  ? 28.355  27.928  22.715  1.00 23.07  ? 57  ILE D HA     1 
ATOM   6019  H  HB     . ILE C 2 58  ? 29.894  28.816  24.879  1.00 24.09  ? 57  ILE D HB     1 
ATOM   6020  H  HG12   . ILE C 2 58  ? 27.915  26.776  24.951  1.00 24.31  ? 57  ILE D HG12   1 
ATOM   6021  H  HG13   . ILE C 2 58  ? 29.472  26.462  24.908  1.00 24.31  ? 57  ILE D HG13   1 
ATOM   6022  H  HG21   . ILE C 2 58  ? 27.887  29.450  25.934  1.00 28.28  ? 57  ILE D HG21   1 
ATOM   6023  H  HG22   . ILE C 2 58  ? 28.048  30.240  24.566  1.00 28.28  ? 57  ILE D HG22   1 
ATOM   6024  H  HG23   . ILE C 2 58  ? 27.071  28.990  24.651  1.00 28.28  ? 57  ILE D HG23   1 
ATOM   6025  H  HD11   . ILE C 2 58  ? 28.869  26.196  27.098  1.00 30.22  ? 57  ILE D HD11   1 
ATOM   6026  H  HD12   . ILE C 2 58  ? 29.639  27.585  27.053  1.00 30.22  ? 57  ILE D HD12   1 
ATOM   6027  H  HD13   . ILE C 2 58  ? 28.052  27.559  27.102  1.00 30.22  ? 57  ILE D HD13   1 
ATOM   6028  N  N      . PRO C 2 59  ? 28.649  29.926  21.260  1.00 20.59  ? 58  PRO D N      1 
ATOM   6029  C  CA     . PRO C 2 59  ? 28.813  31.187  20.517  1.00 21.09  ? 58  PRO D CA     1 
ATOM   6030  C  C      . PRO C 2 59  ? 28.582  32.404  21.404  1.00 20.60  ? 58  PRO D C      1 
ATOM   6031  O  O      . PRO C 2 59  ? 27.613  32.496  22.162  1.00 22.15  ? 58  PRO D O      1 
ATOM   6032  C  CB     . PRO C 2 59  ? 27.733  31.091  19.419  1.00 21.85  ? 58  PRO D CB     1 
ATOM   6033  C  CG     . PRO C 2 59  ? 27.421  29.658  19.305  1.00 19.18  ? 58  PRO D CG     1 
ATOM   6034  C  CD     . PRO C 2 59  ? 27.595  29.076  20.692  1.00 21.45  ? 58  PRO D CD     1 
ATOM   6035  H  HA     . PRO C 2 59  ? 29.698  31.234  20.123  1.00 25.35  ? 58  PRO D HA     1 
ATOM   6036  H  HB2    . PRO C 2 59  ? 26.949  31.597  19.683  1.00 26.25  ? 58  PRO D HB2    1 
ATOM   6037  H  HB3    . PRO C 2 59  ? 28.083  31.436  18.582  1.00 26.25  ? 58  PRO D HB3    1 
ATOM   6038  H  HG2    . PRO C 2 59  ? 26.506  29.547  19.000  1.00 23.05  ? 58  PRO D HG2    1 
ATOM   6039  H  HG3    . PRO C 2 59  ? 28.032  29.240  18.679  1.00 23.05  ? 58  PRO D HG3    1 
ATOM   6040  H  HD2    . PRO C 2 59  ? 26.775  29.148  21.206  1.00 25.78  ? 58  PRO D HD2    1 
ATOM   6041  H  HD3    . PRO C 2 59  ? 27.880  28.150  20.648  1.00 25.78  ? 58  PRO D HD3    1 
ATOM   6042  N  N      . GLY C 2 60  ? 29.453  33.383  21.259  1.00 21.39  ? 59  GLY D N      1 
ATOM   6043  C  CA     . GLY C 2 60  ? 29.401  34.552  22.099  1.00 20.83  ? 59  GLY D CA     1 
ATOM   6044  C  C      . GLY C 2 60  ? 30.261  34.475  23.329  1.00 22.62  ? 59  GLY D C      1 
ATOM   6045  O  O      . GLY C 2 60  ? 30.416  35.497  24.036  1.00 25.11  ? 59  GLY D O      1 
ATOM   6046  H  H      . GLY C 2 60  ? 30.086  33.390  20.676  1.00 25.70  ? 59  GLY D H      1 
ATOM   6047  H  HA2    . GLY C 2 60  ? 29.690  35.321  21.582  1.00 25.02  ? 59  GLY D HA2    1 
ATOM   6048  H  HA3    . GLY C 2 60  ? 28.485  34.691  22.384  1.00 25.02  ? 59  GLY D HA3    1 
ATOM   6049  N  N      . PHE C 2 61  ? 30.819  33.309  23.623  1.00 22.21  ? 60  PHE D N      1 
ATOM   6050  C  CA     . PHE C 2 61  ? 31.605  33.157  24.840  1.00 22.41  ? 60  PHE D CA     1 
ATOM   6051  C  C      . PHE C 2 61  ? 32.937  32.464  24.617  1.00 20.63  ? 60  PHE D C      1 
ATOM   6052  O  O      . PHE C 2 61  ? 33.969  33.112  24.797  1.00 21.38  ? 60  PHE D O      1 
ATOM   6053  C  CB     . PHE C 2 61  ? 30.797  32.387  25.888  1.00 23.12  ? 60  PHE D CB     1 
ATOM   6054  C  CG     . PHE C 2 61  ? 29.580  33.099  26.337  1.00 23.28  ? 60  PHE D CG     1 
ATOM   6055  C  CD1    . PHE C 2 61  ? 28.368  32.934  25.662  1.00 23.38  ? 60  PHE D CD1    1 
ATOM   6056  C  CD2    . PHE C 2 61  ? 29.642  33.957  27.429  1.00 25.52  ? 60  PHE D CD2    1 
ATOM   6057  C  CE1    . PHE C 2 61  ? 27.233  33.601  26.105  1.00 26.83  ? 60  PHE D CE1    1 
ATOM   6058  C  CE2    . PHE C 2 61  ? 28.536  34.623  27.865  1.00 27.40  ? 60  PHE D CE2    1 
ATOM   6059  C  CZ     . PHE C 2 61  ? 27.323  34.452  27.207  1.00 26.03  ? 60  PHE D CZ     1 
ATOM   6060  H  H      . PHE C 2 61  ? 30.758  32.600  23.141  1.00 26.69  ? 60  PHE D H      1 
ATOM   6061  H  HA     . PHE C 2 61  ? 31.808  34.048  25.165  1.00 26.92  ? 60  PHE D HA     1 
ATOM   6062  H  HB2    . PHE C 2 61  ? 30.522  31.538  25.508  1.00 27.78  ? 60  PHE D HB2    1 
ATOM   6063  H  HB3    . PHE C 2 61  ? 31.357  32.236  26.665  1.00 27.78  ? 60  PHE D HB3    1 
ATOM   6064  H  HD1    . PHE C 2 61  ? 28.321  32.379  24.918  1.00 28.08  ? 60  PHE D HD1    1 
ATOM   6065  H  HD2    . PHE C 2 61  ? 30.452  34.078  27.869  1.00 30.66  ? 60  PHE D HD2    1 
ATOM   6066  H  HE1    . PHE C 2 61  ? 26.419  33.481  25.671  1.00 32.23  ? 60  PHE D HE1    1 
ATOM   6067  H  HE2    . PHE C 2 61  ? 28.593  35.189  28.601  1.00 32.91  ? 60  PHE D HE2    1 
ATOM   6068  H  HZ     . PHE C 2 61  ? 26.568  34.908  27.503  1.00 31.27  ? 60  PHE D HZ     1 
ATOM   6069  N  N      . MET C 2 62  ? 32.950  31.169  24.237  1.00 20.28  ? 61  MET D N      1 
ATOM   6070  C  CA     . MET C 2 62  ? 34.229  30.500  24.114  1.00 23.74  ? 61  MET D CA     1 
ATOM   6071  C  C      . MET C 2 62  ? 34.133  29.149  23.414  1.00 23.12  ? 61  MET D C      1 
ATOM   6072  O  O      . MET C 2 62  ? 33.045  28.587  23.213  1.00 22.15  ? 61  MET D O      1 
ATOM   6073  C  CB     . MET C 2 62  ? 34.884  30.288  25.492  1.00 21.29  ? 61  MET D CB     1 
ATOM   6074  C  CG     . MET C 2 62  ? 33.963  30.194  26.704  1.00 29.15  ? 61  MET D CG     1 
ATOM   6075  S  SD     . MET C 2 62  ? 32.805  28.820  26.653  1.00 25.85  ? 61  MET D SD     1 
ATOM   6076  C  CE     . MET C 2 62  ? 33.987  27.475  26.437  1.00 30.10  ? 61  MET D CE     1 
ATOM   6077  H  H      . MET C 2 62  ? 32.257  30.694  24.057  1.00 24.37  ? 61  MET D H      1 
ATOM   6078  H  HA     . MET C 2 62  ? 34.767  31.077  23.550  1.00 28.52  ? 61  MET D HA     1 
ATOM   6079  H  HB2    . MET C 2 62  ? 35.387  29.459  25.457  1.00 25.58  ? 61  MET D HB2    1 
ATOM   6080  H  HB3    . MET C 2 62  ? 35.484  31.033  25.653  1.00 25.58  ? 61  MET D HB3    1 
ATOM   6081  H  HG2    . MET C 2 62  ? 34.507  30.089  27.500  1.00 35.01  ? 61  MET D HG2    1 
ATOM   6082  H  HG3    . MET C 2 62  ? 33.444  31.012  26.763  1.00 35.01  ? 61  MET D HG3    1 
ATOM   6083  H  HE1    . MET C 2 62  ? 33.510  26.631  26.448  1.00 36.16  ? 61  MET D HE1    1 
ATOM   6084  H  HE2    . MET C 2 62  ? 34.442  27.588  25.588  1.00 36.16  ? 61  MET D HE2    1 
ATOM   6085  H  HE3    . MET C 2 62  ? 34.630  27.500  27.163  1.00 36.16  ? 61  MET D HE3    1 
ATOM   6086  N  N      . CYS C 2 63  ? 35.304  28.668  23.017  1.00 20.22  ? 62  CYS D N      1 
ATOM   6087  C  CA     . CYS C 2 63  ? 35.519  27.336  22.463  1.00 21.55  ? 62  CYS D CA     1 
ATOM   6088  C  C      . CYS C 2 63  ? 36.400  26.566  23.420  1.00 24.72  ? 62  CYS D C      1 
ATOM   6089  O  O      . CYS C 2 63  ? 37.526  27.013  23.692  1.00 22.16  ? 62  CYS D O      1 
ATOM   6090  C  CB     . CYS C 2 63  ? 36.259  27.395  21.129  1.00 21.71  ? 62  CYS D CB     1 
ATOM   6091  S  SG     . CYS C 2 63  ? 35.299  28.218  19.826  1.00 23.40  ? 62  CYS D SG     1 
ATOM   6092  H  H      . CYS C 2 63  ? 36.033  29.121  23.062  1.00 24.29  ? 62  CYS D H      1 
ATOM   6093  H  HA     . CYS C 2 63  ? 34.655  26.910  22.348  1.00 25.89  ? 62  CYS D HA     1 
ATOM   6094  H  HB2    . CYS C 2 63  ? 37.086  27.888  21.249  1.00 26.09  ? 62  CYS D HB2    1 
ATOM   6095  H  HB3    . CYS C 2 63  ? 36.451  26.491  20.835  1.00 26.09  ? 62  CYS D HB3    1 
ATOM   6096  H  HG     . CYS C 2 63  ? 35.945  28.232  18.815  1.00 28.11  ? 62  CYS D HG     1 
ATOM   6097  N  N      . GLN C 2 64  ? 35.934  25.394  23.878  1.00 22.45  ? 63  GLN D N      1 
ATOM   6098  C  CA     . GLN C 2 64  ? 36.690  24.623  24.872  1.00 22.93  ? 63  GLN D CA     1 
ATOM   6099  C  C      . GLN C 2 64  ? 37.040  23.242  24.320  1.00 25.35  ? 63  GLN D C      1 
ATOM   6100  O  O      . GLN C 2 64  ? 36.207  22.594  23.660  1.00 26.93  ? 63  GLN D O      1 
ATOM   6101  C  CB     . GLN C 2 64  ? 35.895  24.516  26.165  1.00 22.60  ? 63  GLN D CB     1 
ATOM   6102  C  CG     . GLN C 2 64  ? 36.561  23.654  27.214  1.00 26.32  ? 63  GLN D CG     1 
ATOM   6103  C  CD     . GLN C 2 64  ? 35.766  23.583  28.485  1.00 25.65  ? 63  GLN D CD     1 
ATOM   6104  O  OE1    . GLN C 2 64  ? 34.856  24.398  28.714  1.00 25.42  ? 63  GLN D OE1    1 
ATOM   6105  N  NE2    . GLN C 2 64  ? 36.113  22.608  29.341  1.00 26.38  ? 63  GLN D NE2    1 
ATOM   6106  H  H      . GLN C 2 64  ? 35.195  25.032  23.629  1.00 26.97  ? 63  GLN D H      1 
ATOM   6107  H  HA     . GLN C 2 64  ? 37.532  25.063  25.069  1.00 27.55  ? 63  GLN D HA     1 
ATOM   6108  H  HB2    . GLN C 2 64  ? 35.783  25.404  26.538  1.00 27.15  ? 63  GLN D HB2    1 
ATOM   6109  H  HB3    . GLN C 2 64  ? 35.029  24.127  25.968  1.00 27.15  ? 63  GLN D HB3    1 
ATOM   6110  H  HG2    . GLN C 2 64  ? 36.660  22.753  26.869  1.00 31.61  ? 63  GLN D HG2    1 
ATOM   6111  H  HG3    . GLN C 2 64  ? 37.432  24.026  27.424  1.00 31.61  ? 63  GLN D HG3    1 
ATOM   6112  H  HE21   . GLN C 2 64  ? 36.756  22.072  29.145  1.00 31.69  ? 63  GLN D HE21   1 
ATOM   6113  H  HE22   . GLN C 2 64  ? 35.691  22.520  30.086  1.00 31.69  ? 63  GLN D HE22   1 
ATOM   6114  N  N      . GLY C 2 65  ? 38.278  22.810  24.589  1.00 25.87  ? 64  GLY D N      1 
ATOM   6115  C  CA     . GLY C 2 65  ? 38.775  21.494  24.220  1.00 25.07  ? 64  GLY D CA     1 
ATOM   6116  C  C      . GLY C 2 65  ? 39.860  20.975  25.153  1.00 24.89  ? 64  GLY D C      1 
ATOM   6117  O  O      . GLY C 2 65  ? 39.950  21.403  26.305  1.00 23.92  ? 64  GLY D O      1 
ATOM   6118  H  H      . GLY C 2 65  ? 38.867  23.284  25.000  1.00 31.08  ? 64  GLY D H      1 
ATOM   6119  H  HA2    . GLY C 2 65  ? 38.039  20.863  24.233  1.00 30.12  ? 64  GLY D HA2    1 
ATOM   6120  H  HA3    . GLY C 2 65  ? 39.141  21.534  23.323  1.00 30.12  ? 64  GLY D HA3    1 
ATOM   6121  N  N      . GLY C 2 66  ? 40.662  20.031  24.657  1.00 26.07  ? 65  GLY D N      1 
ATOM   6122  C  CA     . GLY C 2 66  ? 41.859  19.554  25.312  1.00 26.15  ? 65  GLY D CA     1 
ATOM   6123  C  C      . GLY C 2 66  ? 41.781  18.191  25.956  1.00 29.20  ? 65  GLY D C      1 
ATOM   6124  O  O      . GLY C 2 66  ? 42.784  17.754  26.536  1.00 34.37  ? 65  GLY D O      1 
ATOM   6125  H  H      . GLY C 2 66  ? 40.518  19.639  23.905  1.00 31.32  ? 65  GLY D H      1 
ATOM   6126  H  HA2    . GLY C 2 66  ? 42.571  19.522  24.654  1.00 31.41  ? 65  GLY D HA2    1 
ATOM   6127  H  HA3    . GLY C 2 66  ? 42.098  20.188  26.006  1.00 31.41  ? 65  GLY D HA3    1 
ATOM   6128  N  N      . ASP C 2 67  ? 40.645  17.497  25.903  1.00 31.47  ? 66  ASP D N      1 
ATOM   6129  C  CA     . ASP C 2 67  ? 40.555  16.201  26.578  1.00 31.71  ? 66  ASP D CA     1 
ATOM   6130  C  C      . ASP C 2 67  ? 40.980  15.089  25.625  1.00 35.44  ? 66  ASP D C      1 
ATOM   6131  O  O      . ASP C 2 67  ? 40.178  14.533  24.882  1.00 35.35  ? 66  ASP D O      1 
ATOM   6132  C  CB     . ASP C 2 67  ? 39.152  15.958  27.109  1.00 34.51  ? 66  ASP D CB     1 
ATOM   6133  C  CG     . ASP C 2 67  ? 38.987  14.555  27.697  1.00 38.47  ? 66  ASP D CG     1 
ATOM   6134  O  OD1    . ASP C 2 67  ? 40.000  13.818  27.778  1.00 35.59  ? 66  ASP D OD1    1 
ATOM   6135  O  OD2    . ASP C 2 67  ? 37.849  14.191  28.063  1.00 37.79  ? 66  ASP D OD2    1 
ATOM   6136  H  H      . ASP C 2 67  ? 39.931  17.747  25.493  1.00 37.80  ? 66  ASP D H      1 
ATOM   6137  H  HA     . ASP C 2 67  ? 41.180  16.212  27.320  1.00 38.09  ? 66  ASP D HA     1 
ATOM   6138  H  HB2    . ASP C 2 67  ? 38.961  16.603  27.808  1.00 41.45  ? 66  ASP D HB2    1 
ATOM   6139  H  HB3    . ASP C 2 67  ? 38.516  16.058  26.383  1.00 41.45  ? 66  ASP D HB3    1 
ATOM   6140  N  N      . PHE C 2 68  ? 42.249  14.724  25.688  1.00 35.52  ? 67  PHE D N      1 
ATOM   6141  C  CA     . PHE C 2 68  ? 42.799  13.692  24.820  1.00 37.89  ? 67  PHE D CA     1 
ATOM   6142  C  C      . PHE C 2 68  ? 42.948  12.334  25.500  1.00 38.84  ? 67  PHE D C      1 
ATOM   6143  O  O      . PHE C 2 68  ? 43.517  11.424  24.892  1.00 39.31  ? 67  PHE D O      1 
ATOM   6144  C  CB     . PHE C 2 68  ? 44.162  14.150  24.288  1.00 34.39  ? 67  PHE D CB     1 
ATOM   6145  C  CG     . PHE C 2 68  ? 45.169  14.415  25.364  1.00 35.74  ? 67  PHE D CG     1 
ATOM   6146  C  CD1    . PHE C 2 68  ? 45.839  13.368  25.980  1.00 37.96  ? 67  PHE D CD1    1 
ATOM   6147  C  CD2    . PHE C 2 68  ? 45.454  15.720  25.760  1.00 37.11  ? 67  PHE D CD2    1 
ATOM   6148  C  CE1    . PHE C 2 68  ? 46.777  13.618  26.985  1.00 38.74  ? 67  PHE D CE1    1 
ATOM   6149  C  CE2    . PHE C 2 68  ? 46.378  15.971  26.744  1.00 37.01  ? 67  PHE D CE2    1 
ATOM   6150  C  CZ     . PHE C 2 68  ? 47.037  14.917  27.366  1.00 37.28  ? 67  PHE D CZ     1 
ATOM   6151  H  H      . PHE C 2 68  ? 42.822  15.062  26.233  1.00 42.66  ? 67  PHE D H      1 
ATOM   6152  H  HA     . PHE C 2 68  ? 42.197  13.568  24.070  1.00 45.50  ? 67  PHE D HA     1 
ATOM   6153  H  HB2    . PHE C 2 68  ? 44.521  13.458  23.710  1.00 41.30  ? 67  PHE D HB2    1 
ATOM   6154  H  HB3    . PHE C 2 68  ? 44.042  14.971  23.786  1.00 41.30  ? 67  PHE D HB3    1 
ATOM   6155  H  HD1    . PHE C 2 68  ? 45.663  12.492  25.723  1.00 45.58  ? 67  PHE D HD1    1 
ATOM   6156  H  HD2    . PHE C 2 68  ? 45.012  16.430  25.353  1.00 44.57  ? 67  PHE D HD2    1 
ATOM   6157  H  HE1    . PHE C 2 68  ? 47.222  12.912  27.395  1.00 46.52  ? 67  PHE D HE1    1 
ATOM   6158  H  HE2    . PHE C 2 68  ? 46.564  16.848  26.994  1.00 44.45  ? 67  PHE D HE2    1 
ATOM   6159  H  HZ     . PHE C 2 68  ? 47.655  15.088  28.040  1.00 44.77  ? 67  PHE D HZ     1 
ATOM   6160  N  N      . THR C 2 69  ? 42.501  12.184  26.748  1.00 38.66  ? 68  THR D N      1 
ATOM   6161  C  CA     . THR C 2 69  ? 42.574  10.897  27.432  1.00 41.43  ? 68  THR D CA     1 
ATOM   6162  C  C      . THR C 2 69  ? 41.248  10.153  27.381  1.00 42.32  ? 68  THR D C      1 
ATOM   6163  O  O      . THR C 2 69  ? 41.235  8.925   27.257  1.00 44.63  ? 68  THR D O      1 
ATOM   6164  C  CB     . THR C 2 69  ? 43.013  11.042  28.904  1.00 39.37  ? 68  THR D CB     1 
ATOM   6165  O  OG1    . THR C 2 69  ? 42.095  11.843  29.663  1.00 39.91  ? 68  THR D OG1    1 
ATOM   6166  C  CG2    . THR C 2 69  ? 44.413  11.650  29.019  1.00 40.74  ? 68  THR D CG2    1 
ATOM   6167  H  H      . THR C 2 69  ? 42.151  12.813  27.218  1.00 46.43  ? 68  THR D H      1 
ATOM   6168  H  HA     . THR C 2 69  ? 43.260  10.362  27.003  1.00 49.75  ? 68  THR D HA     1 
ATOM   6169  H  HB     . THR C 2 69  ? 43.029  10.149  29.284  1.00 47.28  ? 68  THR D HB     1 
ATOM   6170  H  HG1    . THR C 2 69  ? 42.330  11.864  30.469  1.00 47.92  ? 68  THR D HG1    1 
ATOM   6171  H  HG21   . THR C 2 69  ? 44.665  11.730  29.952  1.00 48.93  ? 68  THR D HG21   1 
ATOM   6172  H  HG22   . THR C 2 69  ? 45.058  11.085  28.566  1.00 48.93  ? 68  THR D HG22   1 
ATOM   6173  H  HG23   . THR C 2 69  ? 44.426  12.531  28.613  1.00 48.93  ? 68  THR D HG23   1 
ATOM   6174  N  N      . ARG C 2 70  ? 40.144  10.892  27.412  1.00 40.52  ? 69  ARG D N      1 
ATOM   6175  C  CA     . ARG C 2 70  ? 38.798  10.332  27.410  1.00 41.09  ? 69  ARG D CA     1 
ATOM   6176  C  C      . ARG C 2 70  ? 37.983  10.771  26.220  1.00 44.54  ? 69  ARG D C      1 
ATOM   6177  O  O      . ARG C 2 70  ? 37.014  10.081  25.861  1.00 44.39  ? 69  ARG D O      1 
ATOM   6178  C  CB     . ARG C 2 70  ? 38.060  10.739  28.689  1.00 38.14  ? 69  ARG D CB     1 
ATOM   6179  C  CG     . ARG C 2 70  ? 38.781  10.284  29.966  1.00 42.87  ? 69  ARG D CG     1 
ATOM   6180  C  CD     . ARG C 2 70  ? 37.848  10.495  31.157  1.00 45.79  ? 69  ARG D CD     1 
ATOM   6181  N  NE     . ARG C 2 70  ? 38.408  10.099  32.441  1.00 49.76  ? 69  ARG D NE     1 
ATOM   6182  C  CZ     . ARG C 2 70  ? 37.934  10.511  33.611  1.00 50.53  ? 69  ARG D CZ     1 
ATOM   6183  N  NH1    . ARG C 2 70  ? 36.893  11.321  33.685  1.00 46.09  ? 69  ARG D NH1    1 
ATOM   6184  N  NH2    . ARG C 2 70  ? 38.532  10.115  34.733  1.00 51.62  ? 69  ARG D NH2    1 
ATOM   6185  H  H      . ARG C 2 70  ? 40.149  11.751  27.435  1.00 48.66  ? 69  ARG D H      1 
ATOM   6186  H  HA     . ARG C 2 70  ? 38.850  9.363   27.398  1.00 49.34  ? 69  ARG D HA     1 
ATOM   6187  H  HB2    . ARG C 2 70  ? 37.985  11.706  28.715  1.00 45.80  ? 69  ARG D HB2    1 
ATOM   6188  H  HB3    . ARG C 2 70  ? 37.177  10.338  28.684  1.00 45.80  ? 69  ARG D HB3    1 
ATOM   6189  H  HG2    . ARG C 2 70  ? 39.005  9.343   29.903  1.00 51.48  ? 69  ARG D HG2    1 
ATOM   6190  H  HG3    . ARG C 2 70  ? 39.586  10.809  30.098  1.00 51.48  ? 69  ARG D HG3    1 
ATOM   6191  H  HD2    . ARG C 2 70  ? 37.627  11.438  31.213  1.00 54.98  ? 69  ARG D HD2    1 
ATOM   6192  H  HD3    . ARG C 2 70  ? 37.043  9.973   31.016  1.00 54.98  ? 69  ARG D HD3    1 
ATOM   6193  H  HE     . ARG C 2 70  ? 39.084  9.567   32.442  1.00 59.75  ? 69  ARG D HE     1 
ATOM   6194  H  HH11   . ARG C 2 70  ? 36.508  11.593  32.966  1.00 55.34  ? 69  ARG D HH11   1 
ATOM   6195  H  HH12   . ARG C 2 70  ? 36.601  11.576  34.452  1.00 55.34  ? 69  ARG D HH12   1 
ATOM   6196  H  HH21   . ARG C 2 70  ? 39.218  9.597   34.696  1.00 61.98  ? 69  ARG D HH21   1 
ATOM   6197  H  HH22   . ARG C 2 70  ? 38.232  10.377  35.496  1.00 61.98  ? 69  ARG D HH22   1 
ATOM   6198  N  N      . HIS C 2 71  ? 38.339  11.895  25.599  1.00 38.83  ? 70  HIS D N      1 
ATOM   6199  C  CA     . HIS C 2 71  ? 37.617  12.394  24.434  1.00 41.69  ? 70  HIS D CA     1 
ATOM   6200  C  C      . HIS C 2 71  ? 36.121  12.524  24.703  1.00 40.76  ? 70  HIS D C      1 
ATOM   6201  O  O      . HIS C 2 71  ? 35.297  12.273  23.824  1.00 40.52  ? 70  HIS D O      1 
ATOM   6202  C  CB     . HIS C 2 71  ? 37.856  11.491  23.230  1.00 43.07  ? 70  HIS D CB     1 
ATOM   6203  C  CG     . HIS C 2 71  ? 39.301  11.285  22.921  1.00 41.98  ? 70  HIS D CG     1 
ATOM   6204  N  ND1    . HIS C 2 71  ? 40.035  12.182  22.170  1.00 43.84  ? 70  HIS D ND1    1 
ATOM   6205  C  CD2    . HIS C 2 71  ? 40.157  10.299  23.278  1.00 44.58  ? 70  HIS D CD2    1 
ATOM   6206  C  CE1    . HIS C 2 71  ? 41.279  11.746  22.059  1.00 40.89  ? 70  HIS D CE1    1 
ATOM   6207  N  NE2    . HIS C 2 71  ? 41.382  10.613  22.736  1.00 48.08  ? 70  HIS D NE2    1 
ATOM   6208  H  H      . HIS C 2 71  ? 39.001  12.389  25.836  1.00 46.63  ? 70  HIS D H      1 
ATOM   6209  H  HA     . HIS C 2 71  ? 37.952  13.283  24.236  1.00 50.07  ? 70  HIS D HA     1 
ATOM   6210  H  HB2    . HIS C 2 71  ? 37.463  10.622  23.408  1.00 51.72  ? 70  HIS D HB2    1 
ATOM   6211  H  HB3    . HIS C 2 71  ? 37.439  11.891  22.451  1.00 51.72  ? 70  HIS D HB3    1 
ATOM   6212  H  HD2    . HIS C 2 71  ? 39.956  9.551   23.794  1.00 53.54  ? 70  HIS D HD2    1 
ATOM   6213  H  HE1    . HIS C 2 71  ? 41.964  12.163  21.588  1.00 49.10  ? 70  HIS D HE1    1 
ATOM   6214  H  HE2    . HIS C 2 71  ? 42.100  10.147  22.822  1.00 57.73  ? 70  HIS D HE2    1 
ATOM   6215  N  N      . ASN C 2 72  ? 35.765  12.938  25.920  1.00 39.24  ? 71  ASN D N      1 
ATOM   6216  C  CA     . ASN C 2 72  ? 34.369  13.243  26.207  1.00 40.03  ? 71  ASN D CA     1 
ATOM   6217  C  C      . ASN C 2 72  ? 34.156  14.482  27.076  1.00 41.17  ? 71  ASN D C      1 
ATOM   6218  O  O      . ASN C 2 72  ? 33.024  14.716  27.520  1.00 40.76  ? 71  ASN D O      1 
ATOM   6219  C  CB     . ASN C 2 72  ? 33.704  12.058  26.904  1.00 42.15  ? 71  ASN D CB     1 
ATOM   6220  C  CG     . ASN C 2 72  ? 34.476  11.607  28.122  1.00 44.03  ? 71  ASN D CG     1 
ATOM   6221  O  OD1    . ASN C 2 72  ? 34.816  12.413  29.007  1.00 42.15  ? 71  ASN D OD1    1 
ATOM   6222  N  ND2    . ASN C 2 72  ? 34.765  10.315  28.182  1.00 43.99  ? 71  ASN D ND2    1 
ATOM   6223  H  H      . ASN C 2 72  ? 36.304  13.048  26.581  1.00 47.13  ? 71  ASN D H      1 
ATOM   6224  H  HA     . ASN C 2 72  ? 33.937  13.412  25.355  1.00 48.07  ? 71  ASN D HA     1 
ATOM   6225  H  HB2    . ASN C 2 72  ? 32.813  12.315  27.188  1.00 50.61  ? 71  ASN D HB2    1 
ATOM   6226  H  HB3    . ASN C 2 72  ? 33.653  11.313  26.285  1.00 50.61  ? 71  ASN D HB3    1 
ATOM   6227  H  HD21   . ASN C 2 72  ? 34.515  9.789   27.549  1.00 52.83  ? 71  ASN D HD21   1 
ATOM   6228  H  HD22   . ASN C 2 72  ? 35.203  10.003  28.853  1.00 52.83  ? 71  ASN D HD22   1 
ATOM   6229  N  N      . GLY C 2 73  ? 35.192  15.283  27.354  1.00 37.58  ? 72  GLY D N      1 
ATOM   6230  C  CA     . GLY C 2 73  ? 34.991  16.506  28.103  1.00 33.12  ? 72  GLY D CA     1 
ATOM   6231  C  C      . GLY C 2 73  ? 35.231  16.401  29.593  1.00 37.44  ? 72  GLY D C      1 
ATOM   6232  O  O      . GLY C 2 73  ? 35.067  17.408  30.301  1.00 36.49  ? 72  GLY D O      1 
ATOM   6233  H  H      . GLY C 2 73  ? 36.006  15.133  27.118  1.00 45.14  ? 72  GLY D H      1 
ATOM   6234  H  HA2    . GLY C 2 73  ? 35.593  17.183  27.756  1.00 39.78  ? 72  GLY D HA2    1 
ATOM   6235  H  HA3    . GLY C 2 73  ? 34.076  16.800  27.973  1.00 39.78  ? 72  GLY D HA3    1 
ATOM   6236  N  N      . THR C 2 74  ? 35.589  15.219  30.103  1.00 34.75  ? 73  THR D N      1 
ATOM   6237  C  CA     . THR C 2 74  ? 35.914  15.065  31.519  1.00 38.96  ? 73  THR D CA     1 
ATOM   6238  C  C      . THR C 2 74  ? 37.377  14.764  31.772  1.00 37.46  ? 73  THR D C      1 
ATOM   6239  O  O      . THR C 2 74  ? 37.787  14.718  32.923  1.00 38.92  ? 73  THR D O      1 
ATOM   6240  C  CB     . THR C 2 74  ? 35.104  13.917  32.162  1.00 40.60  ? 73  THR D CB     1 
ATOM   6241  O  OG1    . THR C 2 74  ? 35.615  12.659  31.684  1.00 41.87  ? 73  THR D OG1    1 
ATOM   6242  C  CG2    . THR C 2 74  ? 33.622  14.032  31.816  1.00 41.37  ? 73  THR D CG2    1 
ATOM   6243  H  H      . THR C 2 74  ? 35.650  14.493  29.647  1.00 41.73  ? 73  THR D H      1 
ATOM   6244  H  HA     . THR C 2 74  ? 35.672  15.897  31.955  1.00 46.79  ? 73  THR D HA     1 
ATOM   6245  H  HB     . THR C 2 74  ? 35.186  13.961  33.127  1.00 48.76  ? 73  THR D HB     1 
ATOM   6246  H  HG1    . THR C 2 74  ? 35.536  12.616  30.849  1.00 50.27  ? 73  THR D HG1    1 
ATOM   6247  H  HG21   . THR C 2 74  ? 33.113  13.374  32.315  1.00 49.68  ? 73  THR D HG21   1 
ATOM   6248  H  HG22   . THR C 2 74  ? 33.297  14.918  32.041  1.00 49.68  ? 73  THR D HG22   1 
ATOM   6249  H  HG23   . THR C 2 74  ? 33.490  13.879  30.867  1.00 49.68  ? 73  THR D HG23   1 
ATOM   6250  N  N      . GLY C 2 75  ? 38.165  14.504  30.744  1.00 39.67  ? 74  GLY D N      1 
ATOM   6251  C  CA     . GLY C 2 75  ? 39.505  14.018  30.956  1.00 40.13  ? 74  GLY D CA     1 
ATOM   6252  C  C      . GLY C 2 75  ? 40.567  15.073  30.736  1.00 39.35  ? 74  GLY D C      1 
ATOM   6253  O  O      . GLY C 2 75  ? 40.343  16.275  30.929  1.00 36.11  ? 74  GLY D O      1 
ATOM   6254  H  H      . GLY C 2 75  ? 37.941  14.602  29.919  1.00 47.63  ? 74  GLY D H      1 
ATOM   6255  H  HA2    . GLY C 2 75  ? 39.585  13.695  31.867  1.00 48.19  ? 74  GLY D HA2    1 
ATOM   6256  H  HA3    . GLY C 2 75  ? 39.678  13.285  30.344  1.00 48.19  ? 74  GLY D HA3    1 
ATOM   6257  N  N      . GLY C 2 76  ? 41.730  14.615  30.329  1.00 36.85  ? 75  GLY D N      1 
ATOM   6258  C  CA     . GLY C 2 76  ? 42.871  15.496  30.251  1.00 39.16  ? 75  GLY D CA     1 
ATOM   6259  C  C      . GLY C 2 76  ? 43.851  15.250  31.377  1.00 40.58  ? 75  GLY D C      1 
ATOM   6260  O  O      . GLY C 2 76  ? 43.481  14.877  32.500  1.00 38.22  ? 75  GLY D O      1 
ATOM   6261  H  H      . GLY C 2 76  ? 41.884  13.802  30.095  1.00 44.26  ? 75  GLY D H      1 
ATOM   6262  H  HA2    . GLY C 2 76  ? 43.329  15.357  29.407  1.00 47.03  ? 75  GLY D HA2    1 
ATOM   6263  H  HA3    . GLY C 2 76  ? 42.571  16.418  30.299  1.00 47.03  ? 75  GLY D HA3    1 
ATOM   6264  N  N      . LYS C 2 77  ? 45.127  15.461  31.070  1.00 38.53  ? 76  LYS D N      1 
ATOM   6265  C  CA     . LYS C 2 77  ? 46.173  15.421  32.069  1.00 37.64  ? 76  LYS D CA     1 
ATOM   6266  C  C      . LYS C 2 77  ? 47.267  16.374  31.616  1.00 39.06  ? 76  LYS D C      1 
ATOM   6267  O  O      . LYS C 2 77  ? 47.400  16.664  30.423  1.00 37.04  ? 76  LYS D O      1 
ATOM   6268  C  CB     . LYS C 2 77  ? 46.734  14.008  32.259  1.00 40.71  ? 76  LYS D CB     1 
ATOM   6269  C  CG     . LYS C 2 77  ? 47.420  13.450  31.021  1.00 43.85  ? 76  LYS D CG     1 
ATOM   6270  C  CD     . LYS C 2 77  ? 48.093  12.106  31.311  1.00 47.94  ? 76  LYS D CD     1 
ATOM   6271  C  CE     . LYS C 2 77  ? 48.395  11.343  30.027  1.00 46.90  ? 76  LYS D CE     1 
ATOM   6272  N  NZ     . LYS C 2 77  ? 49.113  10.069  30.316  1.00 51.78  ? 76  LYS D NZ     1 
ATOM   6273  H  H      . LYS C 2 77  ? 45.411  15.632  30.276  1.00 46.27  ? 76  LYS D H      1 
ATOM   6274  H  HA     . LYS C 2 77  ? 45.826  15.710  32.928  1.00 45.21  ? 76  LYS D HA     1 
ATOM   6275  H  HB2    . LYS C 2 77  ? 47.387  14.025  32.976  1.00 48.88  ? 76  LYS D HB2    1 
ATOM   6276  H  HB3    . LYS C 2 77  ? 46.005  13.411  32.488  1.00 48.88  ? 76  LYS D HB3    1 
ATOM   6277  H  HG2    . LYS C 2 77  ? 46.762  13.316  30.321  1.00 52.65  ? 76  LYS D HG2    1 
ATOM   6278  H  HG3    . LYS C 2 77  ? 48.100  14.073  30.722  1.00 52.65  ? 76  LYS D HG3    1 
ATOM   6279  H  HD2    . LYS C 2 77  ? 48.930  12.260  31.777  1.00 57.57  ? 76  LYS D HD2    1 
ATOM   6280  H  HD3    . LYS C 2 77  ? 47.504  11.563  31.857  1.00 57.57  ? 76  LYS D HD3    1 
ATOM   6281  H  HE2    . LYS C 2 77  ? 47.564  11.130  29.575  1.00 56.32  ? 76  LYS D HE2    1 
ATOM   6282  H  HE3    . LYS C 2 77  ? 48.956  11.887  29.452  1.00 56.32  ? 76  LYS D HE3    1 
ATOM   6283  H  HZ1    . LYS C 2 77  ? 49.284  9.637   29.557  1.00 62.17  ? 76  LYS D HZ1    1 
ATOM   6284  H  HZ2    . LYS C 2 77  ? 49.882  10.240  30.730  1.00 62.17  ? 76  LYS D HZ2    1 
ATOM   6285  H  HZ3    . LYS C 2 77  ? 48.614  9.550   30.838  1.00 62.17  ? 76  LYS D HZ3    1 
ATOM   6286  N  N      . SER C 2 78  ? 48.066  16.839  32.572  1.00 37.92  ? 77  SER D N      1 
ATOM   6287  C  CA     . SER C 2 78  ? 49.184  17.719  32.280  1.00 41.96  ? 77  SER D CA     1 
ATOM   6288  C  C      . SER C 2 78  ? 50.456  16.907  32.105  1.00 38.90  ? 77  SER D C      1 
ATOM   6289  O  O      . SER C 2 78  ? 50.486  15.697  32.320  1.00 42.74  ? 77  SER D O      1 
ATOM   6290  C  CB     . SER C 2 78  ? 49.370  18.752  33.391  1.00 39.38  ? 77  SER D CB     1 
ATOM   6291  O  OG     . SER C 2 78  ? 49.968  18.199  34.548  1.00 45.17  ? 77  SER D OG     1 
ATOM   6292  H  H      . SER C 2 78  ? 47.977  16.654  33.408  1.00 45.53  ? 77  SER D H      1 
ATOM   6293  H  HA     . SER C 2 78  ? 49.000  18.197  31.457  1.00 50.38  ? 77  SER D HA     1 
ATOM   6294  H  HB2    . SER C 2 78  ? 49.939  19.464  33.059  1.00 47.29  ? 77  SER D HB2    1 
ATOM   6295  H  HB3    . SER C 2 78  ? 48.500  19.107  33.632  1.00 47.29  ? 77  SER D HB3    1 
ATOM   6296  H  HG     . SER C 2 78  ? 49.472  17.603  34.870  1.00 54.23  ? 77  SER D HG     1 
ATOM   6297  N  N      . ILE C 2 79  ? 51.523  17.589  31.730  1.00 41.71  ? 78  ILE D N      1 
ATOM   6298  C  CA     . ILE C 2 79  ? 52.838  16.968  31.669  1.00 40.52  ? 78  ILE D CA     1 
ATOM   6299  C  C      . ILE C 2 79  ? 53.440  16.793  33.065  1.00 42.65  ? 78  ILE D C      1 
ATOM   6300  O  O      . ILE C 2 79  ? 54.524  16.221  33.205  1.00 44.40  ? 78  ILE D O      1 
ATOM   6301  C  CB     . ILE C 2 79  ? 53.786  17.776  30.767  1.00 40.33  ? 78  ILE D CB     1 
ATOM   6302  C  CG1    . ILE C 2 79  ? 53.980  19.188  31.323  1.00 38.69  ? 78  ILE D CG1    1 
ATOM   6303  C  CG2    . ILE C 2 79  ? 53.251  17.882  29.327  1.00 39.95  ? 78  ILE D CG2    1 
ATOM   6304  C  CD1    . ILE C 2 79  ? 55.135  19.946  30.665  1.00 38.88  ? 78  ILE D CD1    1 
ATOM   6305  H  H      . ILE C 2 79  ? 51.514  18.418  31.503  1.00 50.09  ? 78  ILE D H      1 
ATOM   6306  H  HA     . ILE C 2 79  ? 52.723  16.079  31.300  1.00 48.65  ? 78  ILE D HA     1 
ATOM   6307  H  HB     . ILE C 2 79  ? 54.632  17.302  30.756  1.00 48.43  ? 78  ILE D HB     1 
ATOM   6308  H  HG12   . ILE C 2 79  ? 53.168  19.697  31.176  1.00 46.46  ? 78  ILE D HG12   1 
ATOM   6309  H  HG13   . ILE C 2 79  ? 54.167  19.128  32.273  1.00 46.46  ? 78  ILE D HG13   1 
ATOM   6310  H  HG21   . ILE C 2 79  ? 53.932  18.286  28.766  1.00 47.97  ? 78  ILE D HG21   1 
ATOM   6311  H  HG22   . ILE C 2 79  ? 53.041  16.993  29.002  1.00 47.97  ? 78  ILE D HG22   1 
ATOM   6312  H  HG23   . ILE C 2 79  ? 52.453  18.433  29.326  1.00 47.97  ? 78  ILE D HG23   1 
ATOM   6313  H  HD11   . ILE C 2 79  ? 55.271  20.784  31.134  1.00 46.69  ? 78  ILE D HD11   1 
ATOM   6314  H  HD12   . ILE C 2 79  ? 55.938  19.404  30.715  1.00 46.69  ? 78  ILE D HD12   1 
ATOM   6315  H  HD13   . ILE C 2 79  ? 54.911  20.119  29.737  1.00 46.69  ? 78  ILE D HD13   1 
ATOM   6316  N  N      . TYR C 2 80  ? 52.741  17.282  34.095  1.00 42.19  ? 79  TYR D N      1 
ATOM   6317  C  CA     . TYR C 2 80  ? 53.229  17.276  35.476  1.00 43.57  ? 79  TYR D CA     1 
ATOM   6318  C  C      . TYR C 2 80  ? 52.540  16.229  36.335  1.00 44.56  ? 79  TYR D C      1 
ATOM   6319  O  O      . TYR C 2 80  ? 52.855  16.108  37.522  1.00 52.50  ? 79  TYR D O      1 
ATOM   6320  C  CB     . TYR C 2 80  ? 53.022  18.659  36.107  1.00 41.58  ? 79  TYR D CB     1 
ATOM   6321  C  CG     . TYR C 2 80  ? 53.606  19.788  35.290  1.00 40.89  ? 79  TYR D CG     1 
ATOM   6322  C  CD1    . TYR C 2 80  ? 54.961  19.839  35.005  1.00 41.28  ? 79  TYR D CD1    1 
ATOM   6323  C  CD2    . TYR C 2 80  ? 52.794  20.791  34.785  1.00 36.98  ? 79  TYR D CD2    1 
ATOM   6324  C  CE1    . TYR C 2 80  ? 55.496  20.878  34.248  1.00 40.55  ? 79  TYR D CE1    1 
ATOM   6325  C  CE2    . TYR C 2 80  ? 53.312  21.816  34.018  1.00 37.70  ? 79  TYR D CE2    1 
ATOM   6326  C  CZ     . TYR C 2 80  ? 54.659  21.860  33.746  1.00 41.62  ? 79  TYR D CZ     1 
ATOM   6327  O  OH     . TYR C 2 80  ? 55.151  22.898  32.979  1.00 38.81  ? 79  TYR D OH     1 
ATOM   6328  H  H      . TYR C 2 80  ? 51.960  17.633  34.016  1.00 50.67  ? 79  TYR D H      1 
ATOM   6329  H  HA     . TYR C 2 80  ? 54.179  17.083  35.470  1.00 52.32  ? 79  TYR D HA     1 
ATOM   6330  H  HB2    . TYR C 2 80  ? 52.070  18.821  36.200  1.00 49.93  ? 79  TYR D HB2    1 
ATOM   6331  H  HB3    . TYR C 2 80  ? 53.447  18.672  36.979  1.00 49.93  ? 79  TYR D HB3    1 
ATOM   6332  H  HD1    . TYR C 2 80  ? 55.522  19.170  35.325  1.00 49.57  ? 79  TYR D HD1    1 
ATOM   6333  H  HD2    . TYR C 2 80  ? 51.882  20.773  34.965  1.00 44.40  ? 79  TYR D HD2    1 
ATOM   6334  H  HE1    . TYR C 2 80  ? 56.410  20.912  34.079  1.00 48.69  ? 79  TYR D HE1    1 
ATOM   6335  H  HE2    . TYR C 2 80  ? 52.749  22.477  33.686  1.00 45.28  ? 79  TYR D HE2    1 
ATOM   6336  H  HH     . TYR C 2 80  ? 54.523  23.406  32.746  1.00 46.60  ? 79  TYR D HH     1 
ATOM   6337  N  N      . GLY C 2 81  ? 51.595  15.486  35.774  1.00 47.96  ? 80  GLY D N      1 
ATOM   6338  C  CA     . GLY C 2 81  ? 50.721  14.609  36.511  1.00 48.90  ? 80  GLY D CA     1 
ATOM   6339  C  C      . GLY C 2 81  ? 49.301  14.856  36.109  1.00 50.35  ? 80  GLY D C      1 
ATOM   6340  O  O      . GLY C 2 81  ? 49.014  15.498  35.087  1.00 47.40  ? 80  GLY D O      1 
ATOM   6341  H  H      . GLY C 2 81  ? 51.441  15.478  34.928  1.00 57.58  ? 80  GLY D H      1 
ATOM   6342  H  HA2    . GLY C 2 81  ? 50.946  13.684  36.326  1.00 58.71  ? 80  GLY D HA2    1 
ATOM   6343  H  HA3    . GLY C 2 81  ? 50.813  14.772  37.463  1.00 58.71  ? 80  GLY D HA3    1 
ATOM   6344  N  N      . GLU C 2 82  ? 48.368  14.354  36.917  1.00 50.99  ? 81  GLU D N      1 
ATOM   6345  C  CA     . GLU C 2 82  ? 46.969  14.503  36.534  1.00 51.20  ? 81  GLU D CA     1 
ATOM   6346  C  C      . GLU C 2 82  ? 46.511  15.952  36.605  1.00 46.99  ? 81  GLU D C      1 
ATOM   6347  O  O      . GLU C 2 82  ? 45.629  16.369  35.833  1.00 45.25  ? 81  GLU D O      1 
ATOM   6348  C  CB     . GLU C 2 82  ? 46.086  13.627  37.415  1.00 58.96  ? 81  GLU D CB     1 
ATOM   6349  C  CG     . GLU C 2 82  ? 45.847  12.251  36.829  1.00 65.80  ? 81  GLU D CG     1 
ATOM   6350  C  CD     . GLU C 2 82  ? 44.634  11.577  37.424  1.00 74.89  ? 81  GLU D CD     1 
ATOM   6351  O  OE1    . GLU C 2 82  ? 43.776  12.290  37.993  1.00 75.14  ? 81  GLU D OE1    1 
ATOM   6352  O  OE2    . GLU C 2 82  ? 44.538  10.333  37.325  1.00 80.40  ? 81  GLU D OE2    1 
ATOM   6353  H  H      . GLU C 2 82  ? 48.512  13.943  37.658  1.00 61.22  ? 81  GLU D H      1 
ATOM   6354  H  HA     . GLU C 2 82  ? 46.870  14.205  35.617  1.00 61.47  ? 81  GLU D HA     1 
ATOM   6355  H  HB2    . GLU C 2 82  ? 46.515  13.514  38.278  1.00 70.79  ? 81  GLU D HB2    1 
ATOM   6356  H  HB3    . GLU C 2 82  ? 45.225  14.059  37.526  1.00 70.79  ? 81  GLU D HB3    1 
ATOM   6357  H  HG2    . GLU C 2 82  ? 45.708  12.333  35.873  1.00 79.00  ? 81  GLU D HG2    1 
ATOM   6358  H  HG3    . GLU C 2 82  ? 46.620  11.692  37.006  1.00 79.00  ? 81  GLU D HG3    1 
ATOM   6359  N  N      . LYS C 2 83  ? 47.078  16.731  37.515  1.00 43.10  ? 82  LYS D N      1 
ATOM   6360  C  CA     . LYS C 2 83  ? 46.614  18.083  37.790  1.00 42.10  ? 82  LYS D CA     1 
ATOM   6361  C  C      . LYS C 2 83  ? 47.772  18.902  38.341  1.00 41.61  ? 82  LYS D C      1 
ATOM   6362  O  O      . LYS C 2 83  ? 48.670  18.365  38.995  1.00 43.44  ? 82  LYS D O      1 
ATOM   6363  C  CB     . LYS C 2 83  ? 45.444  18.042  38.785  1.00 41.38  ? 82  LYS D CB     1 
ATOM   6364  C  CG     . LYS C 2 83  ? 44.141  17.496  38.192  1.00 50.09  ? 82  LYS D CG     1 
ATOM   6365  C  CD     . LYS C 2 83  ? 42.974  17.525  39.198  1.00 50.66  ? 82  LYS D CD     1 
ATOM   6366  C  CE     . LYS C 2 83  ? 41.744  16.752  38.678  1.00 51.81  ? 82  LYS D CE     1 
ATOM   6367  N  NZ     . LYS C 2 83  ? 41.305  15.656  39.616  1.00 60.06  ? 82  LYS D NZ     1 
ATOM   6368  H  H      . LYS C 2 83  ? 47.748  16.494  37.999  1.00 51.75  ? 82  LYS D H      1 
ATOM   6369  H  HA     . LYS C 2 83  ? 46.318  18.519  36.975  1.00 50.55  ? 82  LYS D HA     1 
ATOM   6370  H  HB2    . LYS C 2 83  ? 45.690  17.473  39.531  1.00 49.69  ? 82  LYS D HB2    1 
ATOM   6371  H  HB3    . LYS C 2 83  ? 45.271  18.944  39.098  1.00 49.69  ? 82  LYS D HB3    1 
ATOM   6372  H  HG2    . LYS C 2 83  ? 43.891  18.036  37.426  1.00 60.14  ? 82  LYS D HG2    1 
ATOM   6373  H  HG3    . LYS C 2 83  ? 44.279  16.576  37.918  1.00 60.14  ? 82  LYS D HG3    1 
ATOM   6374  H  HD2    . LYS C 2 83  ? 43.259  17.116  40.030  1.00 60.83  ? 82  LYS D HD2    1 
ATOM   6375  H  HD3    . LYS C 2 83  ? 42.710  18.445  39.354  1.00 60.83  ? 82  LYS D HD3    1 
ATOM   6376  H  HE2    . LYS C 2 83  ? 41.004  17.370  38.572  1.00 62.21  ? 82  LYS D HE2    1 
ATOM   6377  H  HE3    . LYS C 2 83  ? 41.962  16.346  37.825  1.00 62.21  ? 82  LYS D HE3    1 
ATOM   6378  H  HZ1    . LYS C 2 83  ? 40.590  15.241  39.286  1.00 72.11  ? 82  LYS D HZ1    1 
ATOM   6379  H  HZ2    . LYS C 2 83  ? 41.961  15.064  39.721  1.00 72.11  ? 82  LYS D HZ2    1 
ATOM   6380  H  HZ3    . LYS C 2 83  ? 41.097  16.000  40.410  1.00 72.11  ? 82  LYS D HZ3    1 
ATOM   6381  N  N      . PHE C 2 84  ? 47.748  20.212  38.093  1.00 40.75  ? 83  PHE D N      1 
ATOM   6382  C  CA     . PHE C 2 84  ? 48.729  21.107  38.709  1.00 38.09  ? 83  PHE D CA     1 
ATOM   6383  C  C      . PHE C 2 84  ? 48.061  22.408  39.140  1.00 36.21  ? 83  PHE D C      1 
ATOM   6384  O  O      . PHE C 2 84  ? 46.932  22.722  38.744  1.00 36.04  ? 83  PHE D O      1 
ATOM   6385  C  CB     . PHE C 2 84  ? 49.930  21.359  37.776  1.00 39.17  ? 83  PHE D CB     1 
ATOM   6386  C  CG     . PHE C 2 84  ? 49.608  22.118  36.524  1.00 38.16  ? 83  PHE D CG     1 
ATOM   6387  C  CD1    . PHE C 2 84  ? 49.034  21.483  35.437  1.00 35.75  ? 83  PHE D CD1    1 
ATOM   6388  C  CD2    . PHE C 2 84  ? 49.925  23.460  36.417  1.00 40.57  ? 83  PHE D CD2    1 
ATOM   6389  C  CE1    . PHE C 2 84  ? 48.750  22.185  34.277  1.00 38.80  ? 83  PHE D CE1    1 
ATOM   6390  C  CE2    . PHE C 2 84  ? 49.638  24.168  35.261  1.00 34.78  ? 83  PHE D CE2    1 
ATOM   6391  C  CZ     . PHE C 2 84  ? 49.069  23.523  34.187  1.00 30.89  ? 83  PHE D CZ     1 
ATOM   6392  H  H      . PHE C 2 84  ? 47.181  20.601  37.577  1.00 48.94  ? 83  PHE D H      1 
ATOM   6393  H  HA     . PHE C 2 84  ? 49.066  20.692  39.518  1.00 45.74  ? 83  PHE D HA     1 
ATOM   6394  H  HB2    . PHE C 2 84  ? 50.595  21.870  38.263  1.00 47.03  ? 83  PHE D HB2    1 
ATOM   6395  H  HB3    . PHE C 2 84  ? 50.298  20.502  37.511  1.00 47.03  ? 83  PHE D HB3    1 
ATOM   6396  H  HD1    . PHE C 2 84  ? 48.837  20.575  35.485  1.00 42.94  ? 83  PHE D HD1    1 
ATOM   6397  H  HD2    . PHE C 2 84  ? 50.336  23.893  37.130  1.00 48.72  ? 83  PHE D HD2    1 
ATOM   6398  H  HE1    . PHE C 2 84  ? 48.344  21.754  33.559  1.00 46.60  ? 83  PHE D HE1    1 
ATOM   6399  H  HE2    . PHE C 2 84  ? 49.829  25.076  35.211  1.00 41.77  ? 83  PHE D HE2    1 
ATOM   6400  H  HZ     . PHE C 2 84  ? 48.899  23.989  33.400  1.00 36.89  ? 83  PHE D HZ     1 
ATOM   6401  N  N      . GLU C 2 85  ? 48.791  23.159  39.967  1.00 37.34  ? 84  GLU D N      1 
ATOM   6402  C  CA     . GLU C 2 85  ? 48.256  24.294  40.694  1.00 35.77  ? 84  GLU D CA     1 
ATOM   6403  C  C      . GLU C 2 85  ? 48.010  25.483  39.777  1.00 35.70  ? 84  GLU D C      1 
ATOM   6404  O  O      . GLU C 2 85  ? 48.623  25.628  38.716  1.00 35.99  ? 84  GLU D O      1 
ATOM   6405  C  CB     . GLU C 2 85  ? 49.230  24.714  41.805  1.00 40.31  ? 84  GLU D CB     1 
ATOM   6406  C  CG     . GLU C 2 85  ? 50.653  25.052  41.311  1.00 42.86  ? 84  GLU D CG     1 
ATOM   6407  C  CD     . GLU C 2 85  ? 51.434  23.836  40.780  1.00 52.08  ? 84  GLU D CD     1 
ATOM   6408  O  OE1    . GLU C 2 85  ? 51.058  22.670  41.106  1.00 55.66  ? 84  GLU D OE1    1 
ATOM   6409  O  OE2    . GLU C 2 85  ? 52.389  24.040  40.006  1.00 52.19  ? 84  GLU D OE2    1 
ATOM   6410  H  H      . GLU C 2 85  ? 49.625  23.023  40.126  1.00 44.84  ? 84  GLU D H      1 
ATOM   6411  H  HA     . GLU C 2 85  ? 47.407  24.037  41.086  1.00 42.75  ? 84  GLU D HA     1 
ATOM   6412  H  HB2    . GLU C 2 85  ? 48.876  25.503  42.244  1.00 48.40  ? 84  GLU D HB2    1 
ATOM   6413  H  HB3    . GLU C 2 85  ? 49.305  23.986  42.441  1.00 48.40  ? 84  GLU D HB3    1 
ATOM   6414  H  HG2    . GLU C 2 85  ? 50.589  25.699  40.591  1.00 51.47  ? 84  GLU D HG2    1 
ATOM   6415  H  HG3    . GLU C 2 85  ? 51.158  25.427  42.050  1.00 51.47  ? 84  GLU D HG3    1 
ATOM   6416  N  N      . ASP C 2 86  ? 47.092  26.348  40.207  1.00 34.38  ? 85  ASP D N      1 
ATOM   6417  C  CA     . ASP C 2 86  ? 46.879  27.642  39.584  1.00 35.54  ? 85  ASP D CA     1 
ATOM   6418  C  C      . ASP C 2 86  ? 48.161  28.452  39.720  1.00 34.44  ? 85  ASP D C      1 
ATOM   6419  O  O      . ASP C 2 86  ? 48.533  28.848  40.824  1.00 35.83  ? 85  ASP D O      1 
ATOM   6420  C  CB     . ASP C 2 86  ? 45.699  28.379  40.217  1.00 36.50  ? 85  ASP D CB     1 
ATOM   6421  C  CG     . ASP C 2 86  ? 44.365  27.700  39.936  1.00 35.00  ? 85  ASP D CG     1 
ATOM   6422  O  OD1    . ASP C 2 86  ? 44.129  27.264  38.796  1.00 33.07  ? 85  ASP D OD1    1 
ATOM   6423  O  OD2    . ASP C 2 86  ? 43.539  27.650  40.887  1.00 33.05  ? 85  ASP D OD2    1 
ATOM   6424  H  H      . ASP C 2 86  ? 46.569  26.201  40.874  1.00 41.09  ? 85  ASP D H      1 
ATOM   6425  H  HA     . ASP C 2 86  ? 46.658  27.531  38.646  1.00 42.69  ? 85  ASP D HA     1 
ATOM   6426  H  HB2    . ASP C 2 86  ? 45.824  28.409  41.179  1.00 43.84  ? 85  ASP D HB2    1 
ATOM   6427  H  HB3    . ASP C 2 86  ? 45.660  29.279  39.860  1.00 43.84  ? 85  ASP D HB3    1 
ATOM   6428  N  N      . GLU C 2 87  ? 48.868  28.673  38.616  1.00 33.86  ? 86  GLU D N      1 
ATOM   6429  C  CA     . GLU C 2 87  ? 50.190  29.275  38.719  1.00 34.76  ? 86  GLU D CA     1 
ATOM   6430  C  C      . GLU C 2 87  ? 50.105  30.715  39.223  1.00 35.12  ? 86  GLU D C      1 
ATOM   6431  O  O      . GLU C 2 87  ? 50.899  31.127  40.075  1.00 36.40  ? 86  GLU D O      1 
ATOM   6432  C  CB     . GLU C 2 87  ? 50.905  29.196  37.368  1.00 34.05  ? 86  GLU D CB     1 
ATOM   6433  C  CG     . GLU C 2 87  ? 52.399  29.545  37.438  1.00 35.10  ? 86  GLU D CG     1 
ATOM   6434  C  CD     . GLU C 2 87  ? 53.111  29.296  36.117  1.00 34.52  ? 86  GLU D CD     1 
ATOM   6435  O  OE1    . GLU C 2 87  ? 52.415  28.928  35.124  1.00 34.95  ? 86  GLU D OE1    1 
ATOM   6436  O  OE2    . GLU C 2 87  ? 54.343  29.494  36.056  1.00 35.35  ? 86  GLU D OE2    1 
ATOM   6437  H  H      . GLU C 2 87  ? 48.611  28.489  37.816  1.00 40.47  ? 86  GLU D H      1 
ATOM   6438  H  HA     . GLU C 2 87  ? 50.717  28.774  39.360  1.00 41.54  ? 86  GLU D HA     1 
ATOM   6439  H  HB2    . GLU C 2 87  ? 50.827  28.292  37.027  1.00 40.69  ? 86  GLU D HB2    1 
ATOM   6440  H  HB3    . GLU C 2 87  ? 50.484  29.819  36.756  1.00 40.69  ? 86  GLU D HB3    1 
ATOM   6441  H  HG2    . GLU C 2 87  ? 52.496  30.484  37.662  1.00 41.95  ? 86  GLU D HG2    1 
ATOM   6442  H  HG3    . GLU C 2 87  ? 52.822  28.996  38.117  1.00 41.95  ? 86  GLU D HG3    1 
ATOM   6443  N  N      . ASN C 2 88  ? 49.186  31.506  38.665  1.00 34.07  ? 87  ASN D N      1 
ATOM   6444  C  CA     . ASN C 2 88  ? 48.852  32.854  39.138  1.00 34.35  ? 87  ASN D CA     1 
ATOM   6445  C  C      . ASN C 2 88  ? 47.658  33.318  38.308  1.00 32.97  ? 87  ASN D C      1 
ATOM   6446  O  O      . ASN C 2 88  ? 47.277  32.669  37.324  1.00 31.87  ? 87  ASN D O      1 
ATOM   6447  C  CB     . ASN C 2 88  ? 50.038  33.840  39.043  1.00 35.01  ? 87  ASN D CB     1 
ATOM   6448  C  CG     . ASN C 2 88  ? 50.515  34.080  37.606  1.00 34.05  ? 87  ASN D CG     1 
ATOM   6449  O  OD1    . ASN C 2 88  ? 49.727  34.463  36.728  1.00 32.87  ? 87  ASN D OD1    1 
ATOM   6450  N  ND2    . ASN C 2 88  ? 51.796  33.836  37.352  1.00 34.62  ? 87  ASN D ND2    1 
ATOM   6451  H  H      . ASN C 2 88  ? 48.721  31.276  37.980  1.00 40.71  ? 87  ASN D H      1 
ATOM   6452  H  HA     . ASN C 2 88  ? 48.601  32.821  40.075  1.00 41.05  ? 87  ASN D HA     1 
ATOM   6453  H  HB2    . ASN C 2 88  ? 49.765  34.695  39.412  1.00 41.85  ? 87  ASN D HB2    1 
ATOM   6454  H  HB3    . ASN C 2 88  ? 50.784  33.483  39.549  1.00 41.85  ? 87  ASN D HB3    1 
ATOM   6455  H  HD21   . ASN C 2 88  ? 52.108  33.956  36.559  1.00 41.37  ? 87  ASN D HD21   1 
ATOM   6456  H  HD22   . ASN C 2 88  ? 52.314  33.557  37.980  1.00 41.37  ? 87  ASN D HD22   1 
ATOM   6457  N  N      . PHE C 2 89  ? 47.070  34.445  38.703  1.00 33.11  ? 88  PHE D N      1 
ATOM   6458  C  CA     . PHE C 2 89  ? 46.015  35.079  37.909  1.00 31.95  ? 88  PHE D CA     1 
ATOM   6459  C  C      . PHE C 2 89  ? 46.417  36.486  37.486  1.00 31.98  ? 88  PHE D C      1 
ATOM   6460  O  O      . PHE C 2 89  ? 45.618  37.428  37.530  1.00 33.03  ? 88  PHE D O      1 
ATOM   6461  C  CB     . PHE C 2 89  ? 44.695  35.121  38.667  1.00 32.00  ? 88  PHE D CB     1 
ATOM   6462  C  CG     . PHE C 2 89  ? 44.271  33.799  39.167  1.00 32.09  ? 88  PHE D CG     1 
ATOM   6463  C  CD1    . PHE C 2 89  ? 43.702  32.877  38.313  1.00 30.97  ? 88  PHE D CD1    1 
ATOM   6464  C  CD2    . PHE C 2 89  ? 44.475  33.446  40.480  1.00 33.36  ? 88  PHE D CD2    1 
ATOM   6465  C  CE1    . PHE C 2 89  ? 43.328  31.647  38.757  1.00 31.55  ? 88  PHE D CE1    1 
ATOM   6466  C  CE2    . PHE C 2 89  ? 44.099  32.205  40.934  1.00 33.50  ? 88  PHE D CE2    1 
ATOM   6467  C  CZ     . PHE C 2 89  ? 43.523  31.292  40.055  1.00 32.53  ? 88  PHE D CZ     1 
ATOM   6468  H  H      . PHE C 2 89  ? 47.264  34.863  39.428  1.00 39.56  ? 88  PHE D H      1 
ATOM   6469  H  HA     . PHE C 2 89  ? 45.886  34.544  37.109  1.00 38.17  ? 88  PHE D HA     1 
ATOM   6470  H  HB2    . PHE C 2 89  ? 44.791  35.712  39.430  1.00 38.24  ? 88  PHE D HB2    1 
ATOM   6471  H  HB3    . PHE C 2 89  ? 44.003  35.453  38.075  1.00 38.24  ? 88  PHE D HB3    1 
ATOM   6472  H  HD1    . PHE C 2 89  ? 43.573  33.100  37.419  1.00 37.00  ? 88  PHE D HD1    1 
ATOM   6473  H  HD2    . PHE C 2 89  ? 44.869  34.052  41.065  1.00 39.86  ? 88  PHE D HD2    1 
ATOM   6474  H  HE1    . PHE C 2 89  ? 42.935  31.043  38.168  1.00 37.90  ? 88  PHE D HE1    1 
ATOM   6475  H  HE2    . PHE C 2 89  ? 44.230  31.975  41.826  1.00 40.03  ? 88  PHE D HE2    1 
ATOM   6476  H  HZ     . PHE C 2 89  ? 43.274  30.448  40.354  1.00 39.06  ? 88  PHE D HZ     1 
ATOM   6477  N  N      . ILE C 2 90  ? 47.663  36.646  37.048  1.00 32.26  ? 89  ILE D N      1 
ATOM   6478  C  CA     . ILE C 2 90  ? 48.110  37.963  36.613  1.00 32.34  ? 89  ILE D CA     1 
ATOM   6479  C  C      . ILE C 2 90  ? 47.301  38.440  35.409  1.00 31.04  ? 89  ILE D C      1 
ATOM   6480  O  O      . ILE C 2 90  ? 46.879  39.604  35.349  1.00 31.03  ? 89  ILE D O      1 
ATOM   6481  C  CB     . ILE C 2 90  ? 49.609  37.938  36.298  1.00 32.87  ? 89  ILE D CB     1 
ATOM   6482  C  CG1    . ILE C 2 90  ? 50.438  37.864  37.600  1.00 34.42  ? 89  ILE D CG1    1 
ATOM   6483  C  CG2    . ILE C 2 90  ? 50.015  39.182  35.565  1.00 32.72  ? 89  ILE D CG2    1 
ATOM   6484  C  CD1    . ILE C 2 90  ? 51.861  37.526  37.280  1.00 34.94  ? 89  ILE D CD1    1 
ATOM   6485  H  H      . ILE C 2 90  ? 48.254  36.024  36.995  1.00 38.54  ? 89  ILE D H      1 
ATOM   6486  H  HA     . ILE C 2 90  ? 47.959  38.589  37.338  1.00 38.64  ? 89  ILE D HA     1 
ATOM   6487  H  HB     . ILE C 2 90  ? 49.774  37.155  35.750  1.00 39.28  ? 89  ILE D HB     1 
ATOM   6488  H  HG12   . ILE C 2 90  ? 50.415  38.722  38.051  1.00 41.13  ? 89  ILE D HG12   1 
ATOM   6489  H  HG13   . ILE C 2 90  ? 50.076  37.175  38.179  1.00 41.13  ? 89  ILE D HG13   1 
ATOM   6490  H  HG21   . ILE C 2 90  ? 50.981  39.262  35.589  1.00 39.09  ? 89  ILE D HG21   1 
ATOM   6491  H  HG22   . ILE C 2 90  ? 49.711  39.120  34.645  1.00 39.09  ? 89  ILE D HG22   1 
ATOM   6492  H  HG23   . ILE C 2 90  ? 49.608  39.950  35.996  1.00 39.09  ? 89  ILE D HG23   1 
ATOM   6493  H  HD11   . ILE C 2 90  ? 52.278  37.141  38.066  1.00 41.75  ? 89  ILE D HD11   1 
ATOM   6494  H  HD12   . ILE C 2 90  ? 51.877  36.888  36.550  1.00 41.75  ? 89  ILE D HD12   1 
ATOM   6495  H  HD13   . ILE C 2 90  ? 52.327  38.336  37.021  1.00 41.75  ? 89  ILE D HD13   1 
ATOM   6496  N  N      . LEU C 2 91  ? 47.107  37.565  34.422  1.00 30.02  ? 90  LEU D N      1 
ATOM   6497  C  CA     . LEU C 2 91  ? 46.459  37.923  33.166  1.00 28.83  ? 90  LEU D CA     1 
ATOM   6498  C  C      . LEU C 2 91  ? 44.959  37.679  33.249  1.00 28.15  ? 90  LEU D C      1 
ATOM   6499  O  O      . LEU C 2 91  ? 44.504  36.757  33.911  1.00 28.79  ? 90  LEU D O      1 
ATOM   6500  C  CB     . LEU C 2 91  ? 47.040  37.112  32.011  1.00 28.15  ? 90  LEU D CB     1 
ATOM   6501  C  CG     . LEU C 2 91  ? 48.519  37.497  31.796  1.00 29.75  ? 90  LEU D CG     1 
ATOM   6502  C  CD1    . LEU C 2 91  ? 49.174  36.572  30.775  1.00 30.14  ? 90  LEU D CD1    1 
ATOM   6503  C  CD2    . LEU C 2 91  ? 48.583  38.933  31.349  1.00 35.52  ? 90  LEU D CD2    1 
ATOM   6504  H  H      . LEU C 2 91  ? 47.347  36.740  34.459  1.00 35.85  ? 90  LEU D H      1 
ATOM   6505  H  HA     . LEU C 2 91  ? 46.609  38.865  32.989  1.00 34.42  ? 90  LEU D HA     1 
ATOM   6506  H  HB2    . LEU C 2 91  ? 46.989  36.166  32.218  1.00 33.60  ? 90  LEU D HB2    1 
ATOM   6507  H  HB3    . LEU C 2 91  ? 46.545  37.301  31.198  1.00 33.60  ? 90  LEU D HB3    1 
ATOM   6508  H  HG     . LEU C 2 91  ? 49.017  37.402  32.623  1.00 35.74  ? 90  LEU D HG     1 
ATOM   6509  H  HD11   . LEU C 2 91  ? 50.079  36.877  30.608  1.00 36.20  ? 90  LEU D HD11   1 
ATOM   6510  H  HD12   . LEU C 2 91  ? 49.189  35.670  31.131  1.00 36.20  ? 90  LEU D HD12   1 
ATOM   6511  H  HD13   . LEU C 2 91  ? 48.660  36.595  29.953  1.00 36.20  ? 90  LEU D HD13   1 
ATOM   6512  H  HD21   . LEU C 2 91  ? 49.434  39.090  30.911  1.00 42.66  ? 90  LEU D HD21   1 
ATOM   6513  H  HD22   . LEU C 2 91  ? 47.856  39.104  30.731  1.00 42.66  ? 90  LEU D HD22   1 
ATOM   6514  H  HD23   . LEU C 2 91  ? 48.500  39.509  32.125  1.00 42.66  ? 90  LEU D HD23   1 
ATOM   6515  N  N      . LYS C 2 92  ? 44.196  38.492  32.523  1.00 28.56  ? 91  LYS D N      1 
ATOM   6516  C  CA     . LYS C 2 92  ? 42.746  38.482  32.664  1.00 26.99  ? 91  LYS D CA     1 
ATOM   6517  C  C      . LYS C 2 92  ? 42.070  38.185  31.326  1.00 28.62  ? 91  LYS D C      1 
ATOM   6518  O  O      . LYS C 2 92  ? 42.682  38.175  30.256  1.00 26.58  ? 91  LYS D O      1 
ATOM   6519  C  CB     . LYS C 2 92  ? 42.261  39.821  33.251  1.00 29.40  ? 91  LYS D CB     1 
ATOM   6520  C  CG     . LYS C 2 92  ? 42.782  40.183  34.727  1.00 30.43  ? 91  LYS D CG     1 
ATOM   6521  C  CD     . LYS C 2 92  ? 42.576  39.070  35.839  1.00 31.10  ? 91  LYS D CD     1 
ATOM   6522  C  CE     . LYS C 2 92  ? 43.274  39.437  37.211  1.00 38.49  ? 91  LYS D CE     1 
ATOM   6523  N  NZ     . LYS C 2 92  ? 42.724  38.696  38.420  1.00 42.19  ? 91  LYS D NZ     1 
ATOM   6524  H  H      . LYS C 2 92  ? 44.496  39.054  31.945  1.00 34.30  ? 91  LYS D H      1 
ATOM   6525  H  HA     . LYS C 2 92  ? 42.485  37.769  33.267  1.00 32.21  ? 91  LYS D HA     1 
ATOM   6526  H  HB2    . LYS C 2 92  ? 42.556  40.533  32.662  1.00 35.32  ? 91  LYS D HB2    1 
ATOM   6527  H  HB3    . LYS C 2 92  ? 41.292  39.801  33.288  1.00 35.32  ? 91  LYS D HB3    1 
ATOM   6528  H  HG2    . LYS C 2 92  ? 43.734  40.361  34.676  1.00 36.55  ? 91  LYS D HG2    1 
ATOM   6529  H  HG3    . LYS C 2 92  ? 42.311  40.976  35.028  1.00 36.55  ? 91  LYS D HG3    1 
ATOM   6530  H  HD2    . LYS C 2 92  ? 41.627  38.961  36.006  1.00 37.36  ? 91  LYS D HD2    1 
ATOM   6531  H  HD3    . LYS C 2 92  ? 42.956  38.234  35.524  1.00 37.36  ? 91  LYS D HD3    1 
ATOM   6532  H  HE2    . LYS C 2 92  ? 44.219  39.226  37.143  1.00 46.22  ? 91  LYS D HE2    1 
ATOM   6533  H  HE3    . LYS C 2 92  ? 43.157  40.386  37.373  1.00 46.22  ? 91  LYS D HE3    1 
ATOM   6534  H  HZ1    . LYS C 2 92  ? 42.806  37.817  38.302  1.00 50.66  ? 91  LYS D HZ1    1 
ATOM   6535  H  HZ2    . LYS C 2 92  ? 43.174  38.931  39.152  1.00 50.66  ? 91  LYS D HZ2    1 
ATOM   6536  H  HZ3    . LYS C 2 92  ? 41.864  38.894  38.533  1.00 50.66  ? 91  LYS D HZ3    1 
ATOM   6537  N  N      . HIS C 2 93  ? 40.777  37.912  31.412  1.00 26.85  ? 92  HIS D N      1 
ATOM   6538  C  CA     . HIS C 2 93  ? 39.977  37.503  30.260  1.00 27.82  ? 92  HIS D CA     1 
ATOM   6539  C  C      . HIS C 2 93  ? 39.439  38.757  29.569  1.00 28.79  ? 92  HIS D C      1 
ATOM   6540  O  O      . HIS C 2 93  ? 38.276  39.125  29.711  1.00 29.94  ? 92  HIS D O      1 
ATOM   6541  C  CB     . HIS C 2 93  ? 38.863  36.587  30.741  1.00 26.60  ? 92  HIS D CB     1 
ATOM   6542  C  CG     . HIS C 2 93  ? 39.366  35.340  31.405  1.00 24.61  ? 92  HIS D CG     1 
ATOM   6543  N  ND1    . HIS C 2 93  ? 39.674  35.274  32.745  1.00 27.34  ? 92  HIS D ND1    1 
ATOM   6544  C  CD2    . HIS C 2 93  ? 39.640  34.117  30.898  1.00 23.79  ? 92  HIS D CD2    1 
ATOM   6545  C  CE1    . HIS C 2 93  ? 40.093  34.060  33.048  1.00 25.43  ? 92  HIS D CE1    1 
ATOM   6546  N  NE2    . HIS C 2 93  ? 40.086  33.336  31.944  1.00 24.54  ? 92  HIS D NE2    1 
ATOM   6547  H  H      . HIS C 2 93  ? 40.326  37.956  32.143  1.00 32.25  ? 92  HIS D H      1 
ATOM   6548  H  HA     . HIS C 2 93  ? 40.525  37.029  29.615  1.00 33.42  ? 92  HIS D HA     1 
ATOM   6549  H  HB2    . HIS C 2 93  ? 38.317  37.067  31.382  1.00 31.96  ? 92  HIS D HB2    1 
ATOM   6550  H  HB3    . HIS C 2 93  ? 38.324  36.322  29.979  1.00 31.96  ? 92  HIS D HB3    1 
ATOM   6551  H  HD1    . HIS C 2 93  ? 39.604  35.926  33.301  1.00 32.84  ? 92  HIS D HD1    1 
ATOM   6552  H  HD2    . HIS C 2 93  ? 39.546  33.852  30.012  1.00 28.37  ? 92  HIS D HD2    1 
ATOM   6553  H  HE1    . HIS C 2 93  ? 40.348  33.765  33.893  1.00 30.35  ? 92  HIS D HE1    1 
ATOM   6554  N  N      . THR C 2 94  ? 40.324  39.453  28.835  1.00 23.85  ? 93  THR D N      1 
ATOM   6555  C  CA     . THR C 2 94  ? 40.038  40.812  28.417  1.00 24.52  ? 93  THR D CA     1 
ATOM   6556  C  C      . THR C 2 94  ? 39.265  40.923  27.116  1.00 26.46  ? 93  THR D C      1 
ATOM   6557  O  O      . THR C 2 94  ? 38.782  42.012  26.799  1.00 29.25  ? 93  THR D O      1 
ATOM   6558  C  CB     . THR C 2 94  ? 41.350  41.603  28.269  1.00 28.26  ? 93  THR D CB     1 
ATOM   6559  O  OG1    . THR C 2 94  ? 42.233  40.889  27.391  1.00 27.98  ? 93  THR D OG1    1 
ATOM   6560  C  CG2    . THR C 2 94  ? 41.998  41.759  29.621  1.00 33.79  ? 93  THR D CG2    1 
ATOM   6561  H  H      . THR C 2 94  ? 41.087  39.153  28.576  1.00 28.45  ? 93  THR D H      1 
ATOM   6562  H  HA     . THR C 2 94  ? 39.494  41.218  29.110  1.00 29.46  ? 93  THR D HA     1 
ATOM   6563  H  HB     . THR C 2 94  ? 41.177  42.484  27.902  1.00 33.95  ? 93  THR D HB     1 
ATOM   6564  H  HG1    . THR C 2 94  ? 41.871  40.787  26.640  1.00 33.60  ? 93  THR D HG1    1 
ATOM   6565  H  HG21   . THR C 2 94  ? 42.810  42.284  29.541  1.00 40.58  ? 93  THR D HG21   1 
ATOM   6566  H  HG22   . THR C 2 94  ? 41.392  42.208  30.230  1.00 40.58  ? 93  THR D HG22   1 
ATOM   6567  H  HG23   . THR C 2 94  ? 42.221  40.888  29.985  1.00 40.58  ? 93  THR D HG23   1 
ATOM   6568  N  N      . GLY C 2 95  ? 39.148  39.857  26.365  1.00 25.06  ? 94  GLY D N      1 
ATOM   6569  C  CA     . GLY C 2 95  ? 38.526  39.934  25.063  1.00 27.40  ? 94  GLY D CA     1 
ATOM   6570  C  C      . GLY C 2 95  ? 38.695  38.693  24.219  1.00 25.37  ? 94  GLY D C      1 
ATOM   6571  O  O      . GLY C 2 95  ? 39.206  37.653  24.657  1.00 24.61  ? 94  GLY D O      1 
ATOM   6572  H  H      . GLY C 2 95  ? 39.423  39.072  26.584  1.00 30.11  ? 94  GLY D H      1 
ATOM   6573  H  HA2    . GLY C 2 95  ? 37.575  40.088  25.179  1.00 32.91  ? 94  GLY D HA2    1 
ATOM   6574  H  HA3    . GLY C 2 95  ? 38.909  40.680  24.576  1.00 32.91  ? 94  GLY D HA3    1 
ATOM   6575  N  N      . PRO C 2 96  ? 38.247  38.774  22.978  1.00 23.43  ? 95  PRO D N      1 
ATOM   6576  C  CA     . PRO C 2 96  ? 38.344  37.604  22.104  1.00 23.78  ? 95  PRO D CA     1 
ATOM   6577  C  C      . PRO C 2 96  ? 39.797  37.204  21.929  1.00 25.04  ? 95  PRO D C      1 
ATOM   6578  O  O      . PRO C 2 96  ? 40.692  38.043  21.886  1.00 28.69  ? 95  PRO D O      1 
ATOM   6579  C  CB     . PRO C 2 96  ? 37.724  38.077  20.778  1.00 25.33  ? 95  PRO D CB     1 
ATOM   6580  C  CG     . PRO C 2 96  ? 36.965  39.340  21.108  1.00 28.00  ? 95  PRO D CG     1 
ATOM   6581  C  CD     . PRO C 2 96  ? 37.584  39.928  22.344  1.00 27.16  ? 95  PRO D CD     1 
ATOM   6582  H  HA     . PRO C 2 96  ? 37.824  36.861  22.447  1.00 28.57  ? 95  PRO D HA     1 
ATOM   6583  H  HB2    . PRO C 2 96  ? 38.427  38.256  20.134  1.00 30.43  ? 95  PRO D HB2    1 
ATOM   6584  H  HB3    . PRO C 2 96  ? 37.126  37.395  20.435  1.00 30.43  ? 95  PRO D HB3    1 
ATOM   6585  H  HG2    . PRO C 2 96  ? 37.038  39.960  20.366  1.00 33.64  ? 95  PRO D HG2    1 
ATOM   6586  H  HG3    . PRO C 2 96  ? 36.034  39.121  21.267  1.00 33.64  ? 95  PRO D HG3    1 
ATOM   6587  H  HD2    . PRO C 2 96  ? 38.230  40.613  22.114  1.00 32.63  ? 95  PRO D HD2    1 
ATOM   6588  H  HD3    . PRO C 2 96  ? 36.903  40.297  22.928  1.00 32.63  ? 95  PRO D HD3    1 
ATOM   6589  N  N      . GLY C 2 97  ? 40.020  35.901  21.794  1.00 20.68  ? 96  GLY D N      1 
ATOM   6590  C  CA     . GLY C 2 97  ? 41.341  35.380  21.551  1.00 21.75  ? 96  GLY D CA     1 
ATOM   6591  C  C      . GLY C 2 97  ? 42.100  34.968  22.794  1.00 22.22  ? 96  GLY D C      1 
ATOM   6592  O  O      . GLY C 2 97  ? 43.144  34.307  22.675  1.00 23.70  ? 96  GLY D O      1 
ATOM   6593  H  H      . GLY C 2 97  ? 39.409  35.298  21.841  1.00 24.85  ? 96  GLY D H      1 
ATOM   6594  H  HA2    . GLY C 2 97  ? 41.267  34.602  20.978  1.00 26.13  ? 96  GLY D HA2    1 
ATOM   6595  H  HA3    . GLY C 2 97  ? 41.864  36.059  21.097  1.00 26.13  ? 96  GLY D HA3    1 
ATOM   6596  N  N      . ILE C 2 98  ? 41.604  35.310  23.987  1.00 22.54  ? 97  ILE D N      1 
ATOM   6597  C  CA     . ILE C 2 98  ? 42.294  34.896  25.198  1.00 21.91  ? 97  ILE D CA     1 
ATOM   6598  C  C      . ILE C 2 98  ? 42.273  33.380  25.301  1.00 21.43  ? 97  ILE D C      1 
ATOM   6599  O  O      . ILE C 2 98  ? 41.238  32.732  25.104  1.00 20.84  ? 97  ILE D O      1 
ATOM   6600  C  CB     . ILE C 2 98  ? 41.666  35.541  26.437  1.00 22.09  ? 97  ILE D CB     1 
ATOM   6601  C  CG1    . ILE C 2 98  ? 41.982  37.045  26.456  1.00 26.78  ? 97  ILE D CG1    1 
ATOM   6602  C  CG2    . ILE C 2 98  ? 42.186  34.815  27.718  1.00 27.36  ? 97  ILE D CG2    1 
ATOM   6603  C  CD1    . ILE C 2 98  ? 43.447  37.434  26.760  1.00 30.99  ? 97  ILE D CD1    1 
ATOM   6604  H  H      . ILE C 2 98  ? 40.888  35.770  24.113  1.00 27.08  ? 97  ILE D H      1 
ATOM   6605  H  HA     . ILE C 2 98  ? 43.216  35.193  25.140  1.00 26.32  ? 97  ILE D HA     1 
ATOM   6606  H  HB     . ILE C 2 98  ? 40.701  35.447  26.409  1.00 26.34  ? 97  ILE D HB     1 
ATOM   6607  H  HG12   . ILE C 2 98  ? 41.765  37.410  25.584  1.00 32.17  ? 97  ILE D HG12   1 
ATOM   6608  H  HG13   . ILE C 2 98  ? 41.430  37.461  27.137  1.00 32.17  ? 97  ILE D HG13   1 
ATOM   6609  H  HG21   . ILE C 2 98  ? 42.053  35.393  28.485  1.00 32.87  ? 97  ILE D HG21   1 
ATOM   6610  H  HG22   . ILE C 2 98  ? 41.691  33.989  27.836  1.00 32.87  ? 97  ILE D HG22   1 
ATOM   6611  H  HG23   . ILE C 2 98  ? 43.131  34.621  27.609  1.00 32.87  ? 97  ILE D HG23   1 
ATOM   6612  H  HD11   . ILE C 2 98  ? 43.519  38.401  26.781  1.00 37.22  ? 97  ILE D HD11   1 
ATOM   6613  H  HD12   . ILE C 2 98  ? 43.699  37.065  27.621  1.00 37.22  ? 97  ILE D HD12   1 
ATOM   6614  H  HD13   . ILE C 2 98  ? 44.020  37.074  26.065  1.00 37.22  ? 97  ILE D HD13   1 
ATOM   6615  N  N      . LEU C 2 99  ? 43.426  32.810  25.635  1.00 22.04  ? 98  LEU D N      1 
ATOM   6616  C  CA     . LEU C 2 99  ? 43.575  31.384  25.885  1.00 22.13  ? 98  LEU D CA     1 
ATOM   6617  C  C      . LEU C 2 99  ? 43.797  31.130  27.374  1.00 23.02  ? 98  LEU D C      1 
ATOM   6618  O  O      . LEU C 2 99  ? 44.694  31.717  27.999  1.00 23.84  ? 98  LEU D O      1 
ATOM   6619  C  CB     . LEU C 2 99  ? 44.728  30.830  25.053  1.00 23.28  ? 98  LEU D CB     1 
ATOM   6620  C  CG     . LEU C 2 99  ? 45.159  29.377  25.238  1.00 23.96  ? 98  LEU D CG     1 
ATOM   6621  C  CD1    . LEU C 2 99  ? 44.141  28.456  24.660  1.00 24.37  ? 98  LEU D CD1    1 
ATOM   6622  C  CD2    . LEU C 2 99  ? 46.500  29.166  24.554  1.00 23.52  ? 98  LEU D CD2    1 
ATOM   6623  H  H      . LEU C 2 99  ? 44.162  33.245  25.725  1.00 26.28  ? 98  LEU D H      1 
ATOM   6624  H  HA     . LEU C 2 99  ? 42.761  30.915  25.641  1.00 26.39  ? 98  LEU D HA     1 
ATOM   6625  H  HB2    . LEU C 2 99  ? 44.481  30.924  24.120  1.00 27.97  ? 98  LEU D HB2    1 
ATOM   6626  H  HB3    . LEU C 2 99  ? 45.509  31.372  25.246  1.00 27.97  ? 98  LEU D HB3    1 
ATOM   6627  H  HG     . LEU C 2 99  ? 45.244  29.176  26.183  1.00 28.79  ? 98  LEU D HG     1 
ATOM   6628  H  HD11   . LEU C 2 99  ? 44.425  27.540  24.806  1.00 29.28  ? 98  LEU D HD11   1 
ATOM   6629  H  HD12   . LEU C 2 99  ? 43.290  28.612  25.097  1.00 29.28  ? 98  LEU D HD12   1 
ATOM   6630  H  HD13   . LEU C 2 99  ? 44.062  28.630  23.709  1.00 29.28  ? 98  LEU D HD13   1 
ATOM   6631  H  HD21   . LEU C 2 99  ? 46.774  28.243  24.672  1.00 28.26  ? 98  LEU D HD21   1 
ATOM   6632  H  HD22   . LEU C 2 99  ? 46.407  29.365  23.609  1.00 28.26  ? 98  LEU D HD22   1 
ATOM   6633  H  HD23   . LEU C 2 99  ? 47.156  29.759  24.953  1.00 28.26  ? 98  LEU D HD23   1 
ATOM   6634  N  N      . SER C 2 100 ? 42.975  30.250  27.938  1.00 22.91  ? 99  SER D N      1 
ATOM   6635  C  CA     . SER C 2 100 ? 42.971  30.095  29.385  1.00 23.77  ? 99  SER D CA     1 
ATOM   6636  C  C      . SER C 2 100 ? 42.682  28.639  29.726  1.00 23.81  ? 99  SER D C      1 
ATOM   6637  O  O      . SER C 2 100 ? 42.195  27.866  28.900  1.00 23.81  ? 99  SER D O      1 
ATOM   6638  C  CB     . SER C 2 100 ? 41.951  31.063  29.984  1.00 23.74  ? 99  SER D CB     1 
ATOM   6639  O  OG     . SER C 2 100 ? 41.844  30.863  31.378  1.00 24.59  ? 99  SER D OG     1 
ATOM   6640  H  H      . SER C 2 100 ? 42.425  29.743  27.513  1.00 27.32  ? 99  SER D H      1 
ATOM   6641  H  HA     . SER C 2 100 ? 43.838  30.286  29.774  1.00 28.35  ? 99  SER D HA     1 
ATOM   6642  H  HB2    . SER C 2 100 ? 42.241  31.974  29.815  1.00 28.32  ? 99  SER D HB2    1 
ATOM   6643  H  HB3    . SER C 2 100 ? 41.087  30.908  29.573  1.00 28.32  ? 99  SER D HB3    1 
ATOM   6644  H  HG     . SER C 2 100 ? 41.195  31.302  31.682  1.00 29.34  ? 99  SER D HG     1 
ATOM   6645  N  N      . MET C 2 101 ? 43.019  28.262  30.960  1.00 24.76  ? 100 MET D N      1 
ATOM   6646  C  CA     . MET C 2 101 ? 42.867  26.884  31.412  1.00 25.02  ? 100 MET D CA     1 
ATOM   6647  C  C      . MET C 2 101 ? 41.464  26.631  31.950  1.00 24.73  ? 100 MET D C      1 
ATOM   6648  O  O      . MET C 2 101 ? 40.954  27.394  32.776  1.00 25.08  ? 100 MET D O      1 
ATOM   6649  C  CB     . MET C 2 101 ? 43.897  26.527  32.507  1.00 26.30  ? 100 MET D CB     1 
ATOM   6650  C  CG     . MET C 2 101 ? 45.334  26.646  31.997  1.00 26.70  ? 100 MET D CG     1 
ATOM   6651  S  SD     . MET C 2 101 ? 45.634  25.329  30.722  1.00 30.03  ? 100 MET D SD     1 
ATOM   6652  C  CE     . MET C 2 101 ? 45.464  23.844  31.754  1.00 31.16  ? 100 MET D CE     1 
ATOM   6653  H  H      . MET C 2 101 ? 43.340  28.792  31.556  1.00 29.55  ? 100 MET D H      1 
ATOM   6654  H  HA     . MET C 2 101 ? 43.023  26.315  30.642  1.00 29.85  ? 100 MET D HA     1 
ATOM   6655  H  HB2    . MET C 2 101 ? 43.789  27.133  33.257  1.00 31.40  ? 100 MET D HB2    1 
ATOM   6656  H  HB3    . MET C 2 101 ? 43.752  25.612  32.796  1.00 31.40  ? 100 MET D HB3    1 
ATOM   6657  H  HG2    . MET C 2 101 ? 45.469  27.516  31.590  1.00 31.87  ? 100 MET D HG2    1 
ATOM   6658  H  HG3    . MET C 2 101 ? 45.956  26.523  32.730  1.00 31.87  ? 100 MET D HG3    1 
ATOM   6659  H  HE1    . MET C 2 101 ? 45.640  23.060  31.210  1.00 37.42  ? 100 MET D HE1    1 
ATOM   6660  H  HE2    . MET C 2 101 ? 46.103  23.891  32.482  1.00 37.42  ? 100 MET D HE2    1 
ATOM   6661  H  HE3    . MET C 2 101 ? 44.562  23.806  32.107  1.00 37.42  ? 100 MET D HE3    1 
ATOM   6662  N  N      . ALA C 2 102 ? 40.855  25.546  31.488  1.00 24.18  ? 101 ALA D N      1 
ATOM   6663  C  CA     . ALA C 2 102 ? 39.681  25.037  32.179  1.00 27.08  ? 101 ALA D CA     1 
ATOM   6664  C  C      . ALA C 2 102 ? 40.087  24.349  33.483  1.00 25.88  ? 101 ALA D C      1 
ATOM   6665  O  O      . ALA C 2 102 ? 41.234  23.952  33.685  1.00 28.11  ? 101 ALA D O      1 
ATOM   6666  C  CB     . ALA C 2 102 ? 38.934  24.068  31.269  1.00 26.42  ? 101 ALA D CB     1 
ATOM   6667  H  H      . ALA C 2 102 ? 41.097  25.099  30.794  1.00 28.95  ? 101 ALA D H      1 
ATOM   6668  H  HA     . ALA C 2 102 ? 39.081  25.765  32.406  1.00 32.53  ? 101 ALA D HA     1 
ATOM   6669  H  HB1    . ALA C 2 102 ? 38.177  23.702  31.753  1.00 31.74  ? 101 ALA D HB1    1 
ATOM   6670  H  HB2    . ALA C 2 102 ? 38.625  24.547  30.484  1.00 31.74  ? 101 ALA D HB2    1 
ATOM   6671  H  HB3    . ALA C 2 102 ? 39.535  23.354  31.007  1.00 31.74  ? 101 ALA D HB3    1 
ATOM   6672  N  N      . ASN C 2 103 ? 39.120  24.204  34.385  1.00 25.64  ? 102 ASN D N      1 
ATOM   6673  C  CA     . ASN C 2 103 ? 39.402  23.556  35.660  1.00 28.30  ? 102 ASN D CA     1 
ATOM   6674  C  C      . ASN C 2 103 ? 38.093  23.111  36.284  1.00 29.27  ? 102 ASN D C      1 
ATOM   6675  O  O      . ASN C 2 103 ? 37.010  23.350  35.753  1.00 30.06  ? 102 ASN D O      1 
ATOM   6676  C  CB     . ASN C 2 103 ? 40.208  24.458  36.612  1.00 30.31  ? 102 ASN D CB     1 
ATOM   6677  C  CG     . ASN C 2 103 ? 39.436  25.690  37.092  1.00 33.17  ? 102 ASN D CG     1 
ATOM   6678  O  OD1    . ASN C 2 103 ? 38.296  25.598  37.552  1.00 31.08  ? 102 ASN D OD1    1 
ATOM   6679  N  ND2    . ASN C 2 103 ? 40.094  26.860  37.011  1.00 29.63  ? 102 ASN D ND2    1 
ATOM   6680  H  H      . ASN C 2 103 ? 38.308  24.469  34.283  1.00 30.80  ? 102 ASN D H      1 
ATOM   6681  H  HA     . ASN C 2 103 ? 39.937  22.765  35.492  1.00 33.99  ? 102 ASN D HA     1 
ATOM   6682  H  HB2    . ASN C 2 103 ? 40.458  23.943  37.394  1.00 36.41  ? 102 ASN D HB2    1 
ATOM   6683  H  HB3    . ASN C 2 103 ? 41.002  24.768  36.150  1.00 36.41  ? 102 ASN D HB3    1 
ATOM   6684  H  HD21   . ASN C 2 103 ? 39.711  27.587  37.266  1.00 35.60  ? 102 ASN D HD21   1 
ATOM   6685  H  HD22   . ASN C 2 103 ? 40.897  26.881  36.704  1.00 35.60  ? 102 ASN D HD22   1 
ATOM   6686  N  N      . ALA C 2 104 ? 38.218  22.389  37.385  1.00 33.46  ? 103 ALA D N      1 
ATOM   6687  C  CA     . ALA C 2 104 ? 37.065  21.948  38.159  1.00 38.63  ? 103 ALA D CA     1 
ATOM   6688  C  C      . ALA C 2 104 ? 37.248  22.358  39.598  1.00 39.09  ? 103 ALA D C      1 
ATOM   6689  O  O      . ALA C 2 104 ? 36.981  21.587  40.527  1.00 42.40  ? 103 ALA D O      1 
ATOM   6690  C  CB     . ALA C 2 104 ? 36.851  20.440  38.024  1.00 39.63  ? 103 ALA D CB     1 
ATOM   6691  H  H      . ALA C 2 104 ? 38.973  22.136  37.711  1.00 40.19  ? 103 ALA D H      1 
ATOM   6692  H  HA     . ALA C 2 104 ? 36.263  22.376  37.822  1.00 46.39  ? 103 ALA D HA     1 
ATOM   6693  H  HB1    . ALA C 2 104 ? 36.077  20.182  38.549  1.00 47.59  ? 103 ALA D HB1    1 
ATOM   6694  H  HB2    . ALA C 2 104 ? 36.704  20.224  37.090  1.00 47.59  ? 103 ALA D HB2    1 
ATOM   6695  H  HB3    . ALA C 2 104 ? 37.640  19.978  38.350  1.00 47.59  ? 103 ALA D HB3    1 
ATOM   6696  N  N      . GLY C 2 105 ? 37.730  23.590  39.802  1.00 37.27  ? 104 GLY D N      1 
ATOM   6697  C  CA     . GLY C 2 105 ? 38.084  24.090  41.113  1.00 37.56  ? 104 GLY D CA     1 
ATOM   6698  C  C      . GLY C 2 105 ? 39.541  24.521  41.197  1.00 39.71  ? 104 GLY D C      1 
ATOM   6699  O  O      . GLY C 2 105 ? 40.324  24.340  40.257  1.00 36.60  ? 104 GLY D O      1 
ATOM   6700  H  H      . GLY C 2 105 ? 37.862  24.162  39.173  1.00 44.76  ? 104 GLY D H      1 
ATOM   6701  H  HA2    . GLY C 2 105 ? 37.526  24.855  41.325  1.00 45.11  ? 104 GLY D HA2    1 
ATOM   6702  H  HA3    . GLY C 2 105 ? 37.932  23.396  41.773  1.00 45.11  ? 104 GLY D HA3    1 
ATOM   6703  N  N      . PRO C 2 106 ? 39.933  25.109  42.325  1.00 41.54  ? 105 PRO D N      1 
ATOM   6704  C  CA     . PRO C 2 106 ? 41.325  25.553  42.475  1.00 36.29  ? 105 PRO D CA     1 
ATOM   6705  C  C      . PRO C 2 106 ? 42.315  24.413  42.305  1.00 38.82  ? 105 PRO D C      1 
ATOM   6706  O  O      . PRO C 2 106 ? 42.083  23.289  42.750  1.00 36.70  ? 105 PRO D O      1 
ATOM   6707  C  CB     . PRO C 2 106 ? 41.365  26.110  43.905  1.00 40.70  ? 105 PRO D CB     1 
ATOM   6708  C  CG     . PRO C 2 106 ? 39.989  26.614  44.133  1.00 40.87  ? 105 PRO D CG     1 
ATOM   6709  C  CD     . PRO C 2 106 ? 39.054  25.713  43.342  1.00 37.44  ? 105 PRO D CD     1 
ATOM   6710  H  HA     . PRO C 2 106 ? 41.523  26.250  41.831  1.00 43.59  ? 105 PRO D HA     1 
ATOM   6711  H  HB2    . PRO C 2 106 ? 41.589  25.404  44.532  1.00 48.87  ? 105 PRO D HB2    1 
ATOM   6712  H  HB3    . PRO C 2 106 ? 42.016  26.827  43.966  1.00 48.87  ? 105 PRO D HB3    1 
ATOM   6713  H  HG2    . PRO C 2 106 ? 39.782  26.571  45.080  1.00 49.08  ? 105 PRO D HG2    1 
ATOM   6714  H  HG3    . PRO C 2 106 ? 39.924  27.530  43.821  1.00 49.08  ? 105 PRO D HG3    1 
ATOM   6715  H  HD2    . PRO C 2 106 ? 38.669  25.030  43.913  1.00 44.96  ? 105 PRO D HD2    1 
ATOM   6716  H  HD3    . PRO C 2 106 ? 38.349  26.231  42.923  1.00 44.96  ? 105 PRO D HD3    1 
ATOM   6717  N  N      . ASN C 2 107 ? 43.440  24.734  41.670  1.00 34.53  ? 106 ASN D N      1 
ATOM   6718  C  CA     . ASN C 2 107 ? 44.549  23.806  41.485  1.00 36.03  ? 106 ASN D CA     1 
ATOM   6719  C  C      . ASN C 2 107 ? 44.102  22.461  40.928  1.00 36.85  ? 106 ASN D C      1 
ATOM   6720  O  O      . ASN C 2 107 ? 44.509  21.400  41.406  1.00 42.45  ? 106 ASN D O      1 
ATOM   6721  C  CB     . ASN C 2 107 ? 45.304  23.642  42.813  1.00 38.00  ? 106 ASN D CB     1 
ATOM   6722  C  CG     . ASN C 2 107 ? 45.600  24.962  43.434  1.00 39.51  ? 106 ASN D CG     1 
ATOM   6723  O  OD1    . ASN C 2 107 ? 46.266  25.811  42.814  1.00 42.08  ? 106 ASN D OD1    1 
ATOM   6724  N  ND2    . ASN C 2 107 ? 45.103  25.177  44.651  1.00 44.97  ? 106 ASN D ND2    1 
ATOM   6725  H  H      . ASN C 2 107 ? 43.588  25.509  41.326  1.00 41.46  ? 106 ASN D H      1 
ATOM   6726  H  HA     . ASN C 2 107 ? 45.149  24.177  40.820  1.00 43.27  ? 106 ASN D HA     1 
ATOM   6727  H  HB2    . ASN C 2 107 ? 44.760  23.128  43.431  1.00 45.63  ? 106 ASN D HB2    1 
ATOM   6728  H  HB3    . ASN C 2 107 ? 46.144  23.184  42.651  1.00 45.63  ? 106 ASN D HB3    1 
ATOM   6729  H  HD21   . ASN C 2 107 ? 44.636  24.567  45.039  1.00 54.00  ? 106 ASN D HD21   1 
ATOM   6730  H  HD22   . ASN C 2 107 ? 45.248  25.925  45.049  1.00 54.00  ? 106 ASN D HD22   1 
ATOM   6731  N  N      . THR C 2 108 ? 43.292  22.512  39.858  1.00 35.91  ? 107 THR D N      1 
ATOM   6732  C  CA     . THR C 2 108 ? 42.928  21.328  39.100  1.00 35.19  ? 107 THR D CA     1 
ATOM   6733  C  C      . THR C 2 108 ? 43.218  21.510  37.603  1.00 34.36  ? 107 THR D C      1 
ATOM   6734  O  O      . THR C 2 108 ? 42.525  20.962  36.767  1.00 34.51  ? 107 THR D O      1 
ATOM   6735  C  CB     . THR C 2 108 ? 41.454  20.955  39.331  1.00 36.24  ? 107 THR D CB     1 
ATOM   6736  O  OG1    . THR C 2 108 ? 40.594  21.993  38.860  1.00 33.87  ? 107 THR D OG1    1 
ATOM   6737  C  CG2    . THR C 2 108 ? 41.167  20.738  40.820  1.00 37.76  ? 107 THR D CG2    1 
ATOM   6738  H  H      . THR C 2 108 ? 42.941  23.237  39.557  1.00 43.13  ? 107 THR D H      1 
ATOM   6739  H  HA     . THR C 2 108 ? 43.470  20.586  39.411  1.00 42.26  ? 107 THR D HA     1 
ATOM   6740  H  HB     . THR C 2 108 ? 41.274  20.133  38.848  1.00 43.52  ? 107 THR D HB     1 
ATOM   6741  H  HG1    . THR C 2 108 ? 40.729  22.698  39.297  1.00 40.68  ? 107 THR D HG1    1 
ATOM   6742  H  HG21   . THR C 2 108 ? 40.270  20.389  40.937  1.00 45.35  ? 107 THR D HG21   1 
ATOM   6743  H  HG22   . THR C 2 108 ? 41.802  20.105  41.191  1.00 45.35  ? 107 THR D HG22   1 
ATOM   6744  H  HG23   . THR C 2 108 ? 41.244  21.578  41.298  1.00 45.35  ? 107 THR D HG23   1 
ATOM   6745  N  N      . ASN C 2 109 ? 44.263  22.239  37.244  1.00 32.99  ? 108 ASN D N      1 
ATOM   6746  C  CA     . ASN C 2 109 ? 44.599  22.342  35.833  1.00 32.90  ? 108 ASN D CA     1 
ATOM   6747  C  C      . ASN C 2 109 ? 45.130  21.014  35.295  1.00 33.67  ? 108 ASN D C      1 
ATOM   6748  O  O      . ASN C 2 109 ? 45.965  20.355  35.931  1.00 37.15  ? 108 ASN D O      1 
ATOM   6749  C  CB     . ASN C 2 109 ? 45.656  23.421  35.612  1.00 36.07  ? 108 ASN D CB     1 
ATOM   6750  C  CG     . ASN C 2 109 ? 45.209  24.762  36.075  1.00 31.83  ? 108 ASN D CG     1 
ATOM   6751  O  OD1    . ASN C 2 109 ? 44.365  25.402  35.429  1.00 33.29  ? 108 ASN D OD1    1 
ATOM   6752  N  ND2    . ASN C 2 109 ? 45.726  25.193  37.216  1.00 31.04  ? 108 ASN D ND2    1 
ATOM   6753  H  H      . ASN C 2 109 ? 44.778  22.671  37.781  1.00 39.63  ? 108 ASN D H      1 
ATOM   6754  H  HA     . ASN C 2 109 ? 43.796  22.579  35.344  1.00 39.51  ? 108 ASN D HA     1 
ATOM   6755  H  HB2    . ASN C 2 109 ? 46.458  23.185  36.105  1.00 43.32  ? 108 ASN D HB2    1 
ATOM   6756  H  HB3    . ASN C 2 109 ? 45.855  23.481  34.665  1.00 43.32  ? 108 ASN D HB3    1 
ATOM   6757  H  HD21   . ASN C 2 109 ? 45.500  25.962  37.528  1.00 37.08  ? 108 ASN D HD21   1 
ATOM   6758  H  HD22   . ASN C 2 109 ? 46.287  24.703  37.646  1.00 37.08  ? 108 ASN D HD22   1 
ATOM   6759  N  N      . GLY C 2 110 ? 44.703  20.664  34.092  1.00 34.07  ? 109 GLY D N      1 
ATOM   6760  C  CA     . GLY C 2 110 ? 45.176  19.476  33.406  1.00 32.00  ? 109 GLY D CA     1 
ATOM   6761  C  C      . GLY C 2 110 ? 45.650  19.773  31.997  1.00 31.99  ? 109 GLY D C      1 
ATOM   6762  O  O      . GLY C 2 110 ? 46.761  20.279  31.793  1.00 32.41  ? 109 GLY D O      1 
ATOM   6763  H  H      . GLY C 2 110 ? 44.124  21.111  33.640  1.00 40.92  ? 109 GLY D H      1 
ATOM   6764  H  HA2    . GLY C 2 110 ? 45.916  19.092  33.902  1.00 38.43  ? 109 GLY D HA2    1 
ATOM   6765  H  HA3    . GLY C 2 110 ? 44.457  18.827  33.356  1.00 38.43  ? 109 GLY D HA3    1 
ATOM   6766  N  N      . SER C 2 111 ? 44.819  19.447  31.010  1.00 32.30  ? 110 SER D N      1 
ATOM   6767  C  CA     . SER C 2 111 ? 45.092  19.812  29.627  1.00 31.14  ? 110 SER D CA     1 
ATOM   6768  C  C      . SER C 2 111 ? 43.973  20.616  28.995  1.00 30.26  ? 110 SER D C      1 
ATOM   6769  O  O      . SER C 2 111 ? 44.204  21.260  27.970  1.00 27.67  ? 110 SER D O      1 
ATOM   6770  C  CB     . SER C 2 111 ? 45.346  18.555  28.778  1.00 32.96  ? 110 SER D CB     1 
ATOM   6771  O  OG     . SER C 2 111 ? 44.294  17.622  28.936  1.00 33.79  ? 110 SER D OG     1 
ATOM   6772  H  H      . SER C 2 111 ? 44.086  19.011  31.119  1.00 38.80  ? 110 SER D H      1 
ATOM   6773  H  HA     . SER C 2 111 ? 45.901  20.346  29.592  1.00 37.40  ? 110 SER D HA     1 
ATOM   6774  H  HB2    . SER C 2 111 ? 45.404  18.811  27.844  1.00 39.58  ? 110 SER D HB2    1 
ATOM   6775  H  HB3    . SER C 2 111 ? 46.178  18.145  29.061  1.00 39.58  ? 110 SER D HB3    1 
ATOM   6776  H  HG     . SER C 2 111 ? 43.557  17.987  28.763  1.00 40.58  ? 110 SER D HG     1 
ATOM   6777  N  N      . GLN C 2 112 ? 42.785  20.612  29.579  1.00 28.50  ? 111 GLN D N      1 
ATOM   6778  C  CA     . GLN C 2 112 ? 41.662  21.305  28.986  1.00 30.60  ? 111 GLN D CA     1 
ATOM   6779  C  C      . GLN C 2 112 ? 41.866  22.807  29.080  1.00 27.00  ? 111 GLN D C      1 
ATOM   6780  O  O      . GLN C 2 112 ? 42.347  23.332  30.091  1.00 24.69  ? 111 GLN D O      1 
ATOM   6781  C  CB     . GLN C 2 112 ? 40.362  20.894  29.669  1.00 27.06  ? 111 GLN D CB     1 
ATOM   6782  C  CG     . GLN C 2 112 ? 39.883  19.513  29.266  1.00 29.84  ? 111 GLN D CG     1 
ATOM   6783  C  CD     . GLN C 2 112 ? 38.443  19.288  29.617  1.00 28.72  ? 111 GLN D CD     1 
ATOM   6784  O  OE1    . GLN C 2 112 ? 37.595  20.102  29.301  1.00 25.90  ? 111 GLN D OE1    1 
ATOM   6785  N  NE2    . GLN C 2 112 ? 38.158  18.179  30.321  1.00 33.38  ? 111 GLN D NE2    1 
ATOM   6786  H  H      . GLN C 2 112 ? 42.606  20.215  30.320  1.00 34.24  ? 111 GLN D H      1 
ATOM   6787  H  HA     . GLN C 2 112 ? 41.588  21.067  28.048  1.00 36.76  ? 111 GLN D HA     1 
ATOM   6788  H  HB2    . GLN C 2 112 ? 40.499  20.893  30.629  1.00 32.51  ? 111 GLN D HB2    1 
ATOM   6789  H  HB3    . GLN C 2 112 ? 39.669  21.530  29.434  1.00 32.51  ? 111 GLN D HB3    1 
ATOM   6790  H  HG2    . GLN C 2 112 ? 39.980  19.411  28.306  1.00 35.84  ? 111 GLN D HG2    1 
ATOM   6791  H  HG3    . GLN C 2 112 ? 40.415  18.845  29.726  1.00 35.84  ? 111 GLN D HG3    1 
ATOM   6792  H  HE21   . GLN C 2 112 ? 38.788  17.640  30.547  1.00 40.09  ? 111 GLN D HE21   1 
ATOM   6793  H  HE22   . GLN C 2 112 ? 37.345  18.009  30.545  1.00 40.09  ? 111 GLN D HE22   1 
ATOM   6794  N  N      . PHE C 2 113 ? 41.466  23.493  28.000  1.00 26.18  ? 112 PHE D N      1 
ATOM   6795  C  CA     . PHE C 2 113 ? 41.692  24.911  27.801  1.00 22.31  ? 112 PHE D CA     1 
ATOM   6796  C  C      . PHE C 2 113 ? 40.465  25.468  27.086  1.00 23.61  ? 112 PHE D C      1 
ATOM   6797  O  O      . PHE C 2 113 ? 39.626  24.723  26.547  1.00 23.37  ? 112 PHE D O      1 
ATOM   6798  C  CB     . PHE C 2 113 ? 42.932  25.131  26.948  1.00 24.10  ? 112 PHE D CB     1 
ATOM   6799  C  CG     . PHE C 2 113 ? 42.769  24.530  25.582  1.00 23.53  ? 112 PHE D CG     1 
ATOM   6800  C  CD1    . PHE C 2 113 ? 42.225  25.263  24.548  1.00 24.16  ? 112 PHE D CD1    1 
ATOM   6801  C  CD2    . PHE C 2 113 ? 43.062  23.196  25.367  1.00 25.15  ? 112 PHE D CD2    1 
ATOM   6802  C  CE1    . PHE C 2 113 ? 42.005  24.710  23.286  1.00 24.77  ? 112 PHE D CE1    1 
ATOM   6803  C  CE2    . PHE C 2 113 ? 42.862  22.627  24.092  1.00 26.65  ? 112 PHE D CE2    1 
ATOM   6804  C  CZ     . PHE C 2 113 ? 42.358  23.410  23.045  1.00 24.53  ? 112 PHE D CZ     1 
ATOM   6805  H  H      . PHE C 2 113 ? 41.044  23.132  27.344  1.00 31.45  ? 112 PHE D H      1 
ATOM   6806  H  HA     . PHE C 2 113 ? 41.807  25.367  28.650  1.00 26.60  ? 112 PHE D HA     1 
ATOM   6807  H  HB2    . PHE C 2 113 ? 43.087  26.083  26.847  1.00 28.95  ? 112 PHE D HB2    1 
ATOM   6808  H  HB3    . PHE C 2 113 ? 43.695  24.714  27.377  1.00 28.95  ? 112 PHE D HB3    1 
ATOM   6809  H  HD1    . PHE C 2 113 ? 41.999  26.153  24.696  1.00 29.02  ? 112 PHE D HD1    1 
ATOM   6810  H  HD2    . PHE C 2 113 ? 43.391  22.674  26.062  1.00 30.21  ? 112 PHE D HD2    1 
ATOM   6811  H  HE1    . PHE C 2 113 ? 41.619  25.222  22.612  1.00 29.76  ? 112 PHE D HE1    1 
ATOM   6812  H  HE2    . PHE C 2 113 ? 43.064  21.731  23.947  1.00 32.02  ? 112 PHE D HE2    1 
ATOM   6813  H  HZ     . PHE C 2 113 ? 42.265  23.049  22.193  1.00 29.47  ? 112 PHE D HZ     1 
ATOM   6814  N  N      . PHE C 2 114 ? 40.343  26.784  27.083  1.00 21.30  ? 113 PHE D N      1 
ATOM   6815  C  CA     . PHE C 2 114 ? 39.322  27.406  26.263  1.00 21.20  ? 113 PHE D CA     1 
ATOM   6816  C  C      . PHE C 2 114 ? 39.876  28.640  25.590  1.00 22.71  ? 113 PHE D C      1 
ATOM   6817  O  O      . PHE C 2 114 ? 40.833  29.264  26.064  1.00 21.04  ? 113 PHE D O      1 
ATOM   6818  C  CB     . PHE C 2 114 ? 38.060  27.757  27.067  1.00 22.76  ? 113 PHE D CB     1 
ATOM   6819  C  CG     . PHE C 2 114 ? 38.279  28.696  28.222  1.00 23.22  ? 113 PHE D CG     1 
ATOM   6820  C  CD1    . PHE C 2 114 ? 38.883  28.251  29.399  1.00 25.15  ? 113 PHE D CD1    1 
ATOM   6821  C  CD2    . PHE C 2 114 ? 37.781  29.986  28.187  1.00 20.96  ? 113 PHE D CD2    1 
ATOM   6822  C  CE1    . PHE C 2 114 ? 39.042  29.111  30.495  1.00 24.48  ? 113 PHE D CE1    1 
ATOM   6823  C  CE2    . PHE C 2 114 ? 37.927  30.846  29.279  1.00 21.75  ? 113 PHE D CE2    1 
ATOM   6824  C  CZ     . PHE C 2 114 ? 38.568  30.406  30.425  1.00 22.65  ? 113 PHE D CZ     1 
ATOM   6825  H  H      . PHE C 2 114 ? 40.830  27.327  27.539  1.00 25.59  ? 113 PHE D H      1 
ATOM   6826  H  HA     . PHE C 2 114 ? 39.068  26.781  25.566  1.00 25.48  ? 113 PHE D HA     1 
ATOM   6827  H  HB2    . PHE C 2 114 ? 37.422  28.177  26.469  1.00 27.34  ? 113 PHE D HB2    1 
ATOM   6828  H  HB3    . PHE C 2 114 ? 37.687  26.937  27.426  1.00 27.34  ? 113 PHE D HB3    1 
ATOM   6829  H  HD1    . PHE C 2 114 ? 39.184  27.373  29.457  1.00 30.22  ? 113 PHE D HD1    1 
ATOM   6830  H  HD2    . PHE C 2 114 ? 37.341  30.287  27.424  1.00 24.99  ? 113 PHE D HD2    1 
ATOM   6831  H  HE1    . PHE C 2 114 ? 39.465  28.810  31.266  1.00 29.41  ? 113 PHE D HE1    1 
ATOM   6832  H  HE2    . PHE C 2 114 ? 37.594  31.713  29.237  1.00 26.10  ? 113 PHE D HE2    1 
ATOM   6833  H  HZ     . PHE C 2 114 ? 38.679  30.981  31.147  1.00 27.01  ? 113 PHE D HZ     1 
ATOM   6834  N  N      . ILE C 2 115 ? 39.242  28.981  24.473  1.00 19.46  ? 114 ILE D N      1 
ATOM   6835  C  CA     . ILE C 2 115 ? 39.570  30.184  23.710  1.00 19.30  ? 114 ILE D CA     1 
ATOM   6836  C  C      . ILE C 2 115 ? 38.362  31.101  23.782  1.00 19.62  ? 114 ILE D C      1 
ATOM   6837  O  O      . ILE C 2 115 ? 37.269  30.738  23.332  1.00 19.96  ? 114 ILE D O      1 
ATOM   6838  C  CB     . ILE C 2 115 ? 39.923  29.860  22.257  1.00 18.92  ? 114 ILE D CB     1 
ATOM   6839  C  CG1    . ILE C 2 115 ? 40.995  28.793  22.116  1.00 21.83  ? 114 ILE D CG1    1 
ATOM   6840  C  CG2    . ILE C 2 115 ? 40.346  31.158  21.573  1.00 19.71  ? 114 ILE D CG2    1 
ATOM   6841  C  CD1    . ILE C 2 115 ? 40.989  28.157  20.689  1.00 23.25  ? 114 ILE D CD1    1 
ATOM   6842  H  H      . ILE C 2 115 ? 38.603  28.521  24.128  1.00 23.19  ? 114 ILE D H      1 
ATOM   6843  H  HA     . ILE C 2 115 ? 40.333  30.627  24.112  1.00 22.99  ? 114 ILE D HA     1 
ATOM   6844  H  HB     . ILE C 2 115 ? 39.136  29.485  21.831  1.00 22.73  ? 114 ILE D HB     1 
ATOM   6845  H  HG12   . ILE C 2 115 ? 41.866  29.192  22.269  1.00 26.23  ? 114 ILE D HG12   1 
ATOM   6846  H  HG13   . ILE C 2 115 ? 40.833  28.090  22.765  1.00 26.23  ? 114 ILE D HG13   1 
ATOM   6847  H  HG21   . ILE C 2 115 ? 40.727  30.949  20.706  1.00 23.69  ? 114 ILE D HG21   1 
ATOM   6848  H  HG22   . ILE C 2 115 ? 39.567  31.726  21.464  1.00 23.69  ? 114 ILE D HG22   1 
ATOM   6849  H  HG23   . ILE C 2 115 ? 41.006  31.605  22.126  1.00 23.69  ? 114 ILE D HG23   1 
ATOM   6850  H  HD11   . ILE C 2 115 ? 41.653  27.451  20.655  1.00 27.93  ? 114 ILE D HD11   1 
ATOM   6851  H  HD12   . ILE C 2 115 ? 40.108  27.791  20.510  1.00 27.93  ? 114 ILE D HD12   1 
ATOM   6852  H  HD13   . ILE C 2 115 ? 41.201  28.843  20.037  1.00 27.93  ? 114 ILE D HD13   1 
ATOM   6853  N  N      . CYS C 2 116 ? 38.552  32.274  24.363  1.00 19.44  ? 115 CYS D N      1 
ATOM   6854  C  CA     . CYS C 2 116 ? 37.492  33.264  24.463  1.00 19.28  ? 115 CYS D CA     1 
ATOM   6855  C  C      . CYS C 2 116 ? 37.156  33.812  23.084  1.00 20.37  ? 115 CYS D C      1 
ATOM   6856  O  O      . CYS C 2 116 ? 38.037  34.028  22.255  1.00 21.33  ? 115 CYS D O      1 
ATOM   6857  C  CB     . CYS C 2 116 ? 37.931  34.394  25.376  1.00 21.29  ? 115 CYS D CB     1 
ATOM   6858  S  SG     . CYS C 2 116 ? 38.149  33.897  27.096  1.00 24.04  ? 115 CYS D SG     1 
ATOM   6859  H  H      . CYS C 2 116 ? 39.296  32.526  24.712  1.00 23.15  ? 115 CYS D H      1 
ATOM   6860  H  HA     . CYS C 2 116 ? 36.693  32.859  24.836  1.00 22.97  ? 115 CYS D HA     1 
ATOM   6861  H  HB2    . CYS C 2 116 ? 38.780  34.739  25.058  1.00 25.58  ? 115 CYS D HB2    1 
ATOM   6862  H  HB3    . CYS C 2 116 ? 37.259  35.093  25.353  1.00 25.58  ? 115 CYS D HB3    1 
ATOM   6863  H  HG     . CYS C 2 116 ? 37.088  33.555  27.541  1.00 28.88  ? 115 CYS D HG     1 
ATOM   6864  N  N      . THR C 2 117 ? 35.870  33.992  22.817  1.00 20.85  ? 116 THR D N      1 
ATOM   6865  C  CA     . THR C 2 117 ? 35.424  34.740  21.643  1.00 21.97  ? 116 THR D CA     1 
ATOM   6866  C  C      . THR C 2 117 ? 34.800  36.061  22.055  1.00 23.89  ? 116 THR D C      1 
ATOM   6867  O  O      . THR C 2 117 ? 34.204  36.750  21.205  1.00 24.60  ? 116 THR D O      1 
ATOM   6868  C  CB     . THR C 2 117 ? 34.438  33.916  20.833  1.00 20.95  ? 116 THR D CB     1 
ATOM   6869  O  OG1    . THR C 2 117 ? 33.327  33.613  21.671  1.00 21.91  ? 116 THR D OG1    1 
ATOM   6870  C  CG2    . THR C 2 117 ? 35.096  32.636  20.371  1.00 22.95  ? 116 THR D CG2    1 
ATOM   6871  H  H      . THR C 2 117 ? 35.229  33.688  23.303  1.00 25.06  ? 116 THR D H      1 
ATOM   6872  H  HA     . THR C 2 117 ? 36.180  34.920  21.064  1.00 26.40  ? 116 THR D HA     1 
ATOM   6873  H  HB     . THR C 2 117 ? 34.140  34.399  20.047  1.00 25.17  ? 116 THR D HB     1 
ATOM   6874  H  HG1    . THR C 2 117 ? 32.754  33.175  21.241  1.00 26.33  ? 116 THR D HG1    1 
ATOM   6875  H  HG21   . THR C 2 117 ? 34.482  32.130  19.816  1.00 27.57  ? 116 THR D HG21   1 
ATOM   6876  H  HG22   . THR C 2 117 ? 35.892  32.840  19.856  1.00 27.57  ? 116 THR D HG22   1 
ATOM   6877  H  HG23   . THR C 2 117 ? 35.346  32.096  21.137  1.00 27.57  ? 116 THR D HG23   1 
ATOM   6878  N  N      . ALA C 2 118 ? 34.861  36.387  23.350  1.00 22.67  ? 117 ALA D N      1 
ATOM   6879  C  CA     . ALA C 2 118 ? 34.378  37.638  23.914  1.00 22.09  ? 117 ALA D CA     1 
ATOM   6880  C  C      . ALA C 2 118 ? 35.104  37.840  25.238  1.00 21.51  ? 117 ALA D C      1 
ATOM   6881  O  O      . ALA C 2 118 ? 35.683  36.898  25.791  1.00 22.92  ? 117 ALA D O      1 
ATOM   6882  C  CB     . ALA C 2 118 ? 32.869  37.632  24.151  1.00 24.19  ? 117 ALA D CB     1 
ATOM   6883  H  H      . ALA C 2 118 ? 35.197  35.870  23.949  1.00 27.24  ? 117 ALA D H      1 
ATOM   6884  H  HA     . ALA C 2 118 ? 34.580  38.359  23.298  1.00 26.54  ? 117 ALA D HA     1 
ATOM   6885  H  HB1    . ALA C 2 118 ? 32.604  38.487  24.525  1.00 29.06  ? 117 ALA D HB1    1 
ATOM   6886  H  HB2    . ALA C 2 118 ? 32.417  37.487  23.305  1.00 29.06  ? 117 ALA D HB2    1 
ATOM   6887  H  HB3    . ALA C 2 118 ? 32.649  36.918  24.770  1.00 29.06  ? 117 ALA D HB3    1 
ATOM   6888  N  N      . LYS C 2 119 ? 35.001  39.054  25.775  1.00 23.97  ? 118 LYS D N      1 
ATOM   6889  C  CA     . LYS C 2 119 ? 35.399  39.314  27.154  1.00 25.06  ? 118 LYS D CA     1 
ATOM   6890  C  C      . LYS C 2 119 ? 34.576  38.458  28.102  1.00 28.90  ? 118 LYS D C      1 
ATOM   6891  O  O      . LYS C 2 119 ? 33.343  38.455  28.033  1.00 29.48  ? 118 LYS D O      1 
ATOM   6892  C  CB     . LYS C 2 119 ? 35.204  40.804  27.488  1.00 24.61  ? 118 LYS D CB     1 
ATOM   6893  C  CG     . LYS C 2 119 ? 35.571  41.242  28.927  1.00 31.71  ? 118 LYS D CG     1 
ATOM   6894  C  CD     . LYS C 2 119 ? 35.606  42.797  28.994  1.00 35.59  ? 118 LYS D CD     1 
ATOM   6895  C  CE     . LYS C 2 119 ? 36.541  43.389  30.034  1.00 42.72  ? 118 LYS D CE     1 
ATOM   6896  N  NZ     . LYS C 2 119 ? 35.964  43.398  31.398  1.00 48.35  ? 118 LYS D NZ     1 
ATOM   6897  H  H      . LYS C 2 119 ? 34.703  39.746  25.361  1.00 28.80  ? 118 LYS D H      1 
ATOM   6898  H  HA     . LYS C 2 119 ? 36.337  39.096  27.268  1.00 30.11  ? 118 LYS D HA     1 
ATOM   6899  H  HB2    . LYS C 2 119 ? 35.756  41.323  26.883  1.00 29.56  ? 118 LYS D HB2    1 
ATOM   6900  H  HB3    . LYS C 2 119 ? 34.268  41.022  27.354  1.00 29.56  ? 118 LYS D HB3    1 
ATOM   6901  H  HG2    . LYS C 2 119 ? 34.905  40.915  29.552  1.00 38.09  ? 118 LYS D HG2    1 
ATOM   6902  H  HG3    . LYS C 2 119 ? 36.446  40.897  29.164  1.00 38.09  ? 118 LYS D HG3    1 
ATOM   6903  H  HD2    . LYS C 2 119 ? 35.889  43.134  28.129  1.00 42.75  ? 118 LYS D HD2    1 
ATOM   6904  H  HD3    . LYS C 2 119 ? 34.712  43.115  29.198  1.00 42.75  ? 118 LYS D HD3    1 
ATOM   6905  H  HE2    . LYS C 2 119 ? 37.356  42.864  30.058  1.00 51.30  ? 118 LYS D HE2    1 
ATOM   6906  H  HE3    . LYS C 2 119 ? 36.743  44.306  29.790  1.00 51.30  ? 118 LYS D HE3    1 
ATOM   6907  H  HZ1    . LYS C 2 119 ? 35.447  42.683  31.515  1.00 58.05  ? 118 LYS D HZ1    1 
ATOM   6908  H  HZ2    . LYS C 2 119 ? 36.616  43.385  32.004  1.00 58.05  ? 118 LYS D HZ2    1 
ATOM   6909  H  HZ3    . LYS C 2 119 ? 35.474  44.131  31.517  1.00 58.05  ? 118 LYS D HZ3    1 
ATOM   6910  N  N      . THR C 2 120 ? 35.258  37.749  29.023  1.00 29.34  ? 119 THR D N      1 
ATOM   6911  C  CA     . THR C 2 120 ? 34.599  36.943  30.040  1.00 24.31  ? 119 THR D CA     1 
ATOM   6912  C  C      . THR C 2 120 ? 35.184  37.222  31.431  1.00 28.74  ? 119 THR D C      1 
ATOM   6913  O  O      . THR C 2 120 ? 35.735  36.346  32.090  1.00 26.69  ? 119 THR D O      1 
ATOM   6914  C  CB     . THR C 2 120 ? 34.695  35.462  29.744  1.00 26.80  ? 119 THR D CB     1 
ATOM   6915  O  OG1    . THR C 2 120 ? 36.076  35.055  29.646  1.00 25.35  ? 119 THR D OG1    1 
ATOM   6916  C  CG2    . THR C 2 120 ? 34.006  35.197  28.415  1.00 26.35  ? 119 THR D CG2    1 
ATOM   6917  H  H      . THR C 2 120 ? 36.116  37.726  29.070  1.00 35.24  ? 119 THR D H      1 
ATOM   6918  H  HA     . THR C 2 120 ? 33.668  37.215  30.040  1.00 29.21  ? 119 THR D HA     1 
ATOM   6919  H  HB     . THR C 2 120 ? 34.276  34.949  30.453  1.00 32.19  ? 119 THR D HB     1 
ATOM   6920  H  HG1    . THR C 2 120 ? 36.457  35.150  30.389  1.00 30.46  ? 119 THR D HG1    1 
ATOM   6921  H  HG21   . THR C 2 120 ? 33.967  34.242  28.246  1.00 31.66  ? 119 THR D HG21   1 
ATOM   6922  H  HG22   . THR C 2 120 ? 33.103  35.550  28.434  1.00 31.66  ? 119 THR D HG22   1 
ATOM   6923  H  HG23   . THR C 2 120 ? 34.497  35.624  27.696  1.00 31.66  ? 119 THR D HG23   1 
ATOM   6924  N  N      . GLU C 2 121 ? 34.983  38.441  31.900  1.00 28.51  ? 120 GLU D N      1 
ATOM   6925  C  CA     . GLU C 2 121 ? 35.698  38.922  33.075  1.00 30.39  ? 120 GLU D CA     1 
ATOM   6926  C  C      . GLU C 2 121 ? 35.303  38.204  34.362  1.00 30.35  ? 120 GLU D C      1 
ATOM   6927  O  O      . GLU C 2 121 ? 36.064  38.267  35.334  1.00 33.48  ? 120 GLU D O      1 
ATOM   6928  C  CB     . GLU C 2 121 ? 35.469  40.432  33.202  1.00 33.75  ? 120 GLU D CB     1 
ATOM   6929  C  CG     . GLU C 2 121 ? 34.063  40.810  33.669  1.00 33.82  ? 120 GLU D CG     1 
ATOM   6930  C  CD     . GLU C 2 121 ? 33.007  40.654  32.575  1.00 35.72  ? 120 GLU D CD     1 
ATOM   6931  O  OE1    . GLU C 2 121 ? 33.353  40.372  31.381  1.00 36.05  ? 120 GLU D OE1    1 
ATOM   6932  O  OE2    . GLU C 2 121 ? 31.822  40.829  32.916  1.00 38.33  ? 120 GLU D OE2    1 
ATOM   6933  H  H      . GLU C 2 121 ? 34.439  39.012  31.559  1.00 34.24  ? 120 GLU D H      1 
ATOM   6934  H  HA     . GLU C 2 121 ? 36.647  38.759  32.959  1.00 36.50  ? 120 GLU D HA     1 
ATOM   6935  H  HB2    . GLU C 2 121 ? 36.101  40.789  33.846  1.00 40.54  ? 120 GLU D HB2    1 
ATOM   6936  H  HB3    . GLU C 2 121 ? 35.613  40.843  32.335  1.00 40.54  ? 120 GLU D HB3    1 
ATOM   6937  H  HG2    . GLU C 2 121 ? 33.812  40.237  34.410  1.00 40.62  ? 120 GLU D HG2    1 
ATOM   6938  H  HG3    . GLU C 2 121 ? 34.064  41.738  33.953  1.00 40.62  ? 120 GLU D HG3    1 
ATOM   6939  N  N      . TRP C 2 122 ? 34.142  37.547  34.417  1.00 29.18  ? 121 TRP D N      1 
ATOM   6940  C  CA     . TRP C 2 122 ? 33.721  36.821  35.610  1.00 34.21  ? 121 TRP D CA     1 
ATOM   6941  C  C      . TRP C 2 122 ? 34.563  35.569  35.847  1.00 31.78  ? 121 TRP D C      1 
ATOM   6942  O  O      . TRP C 2 122 ? 34.462  34.961  36.919  1.00 33.07  ? 121 TRP D O      1 
ATOM   6943  C  CB     . TRP C 2 122 ? 32.204  36.460  35.534  1.00 34.23  ? 121 TRP D CB     1 
ATOM   6944  C  CG     . TRP C 2 122 ? 31.842  35.614  34.355  1.00 30.70  ? 121 TRP D CG     1 
ATOM   6945  C  CD1    . TRP C 2 122 ? 31.745  34.248  34.338  1.00 27.64  ? 121 TRP D CD1    1 
ATOM   6946  C  CD2    . TRP C 2 122 ? 31.535  36.056  33.025  1.00 29.91  ? 121 TRP D CD2    1 
ATOM   6947  N  NE1    . TRP C 2 122 ? 31.457  33.818  33.068  1.00 32.14  ? 121 TRP D NE1    1 
ATOM   6948  C  CE2    . TRP C 2 122 ? 31.320  34.904  32.250  1.00 31.01  ? 121 TRP D CE2    1 
ATOM   6949  C  CE3    . TRP C 2 122 ? 31.470  37.309  32.399  1.00 30.00  ? 121 TRP D CE3    1 
ATOM   6950  C  CZ2    . TRP C 2 122 ? 31.002  34.968  30.905  1.00 28.98  ? 121 TRP D CZ2    1 
ATOM   6951  C  CZ3    . TRP C 2 122 ? 31.154  37.367  31.061  1.00 31.17  ? 121 TRP D CZ3    1 
ATOM   6952  C  CH2    . TRP C 2 122 ? 30.946  36.198  30.323  1.00 29.88  ? 121 TRP D CH2    1 
ATOM   6953  H  H      . TRP C 2 122 ? 33.577  37.507  33.769  1.00 35.05  ? 121 TRP D H      1 
ATOM   6954  H  HA     . TRP C 2 122 ? 33.826  37.399  36.382  1.00 41.09  ? 121 TRP D HA     1 
ATOM   6955  H  HB2    . TRP C 2 122 ? 31.959  35.971  36.335  1.00 41.11  ? 121 TRP D HB2    1 
ATOM   6956  H  HB3    . TRP C 2 122 ? 31.691  37.281  35.477  1.00 41.11  ? 121 TRP D HB3    1 
ATOM   6957  H  HD1    . TRP C 2 122 ? 31.857  33.694  35.077  1.00 33.20  ? 121 TRP D HD1    1 
ATOM   6958  H  HE1    . TRP C 2 122 ? 31.376  32.997  32.826  1.00 38.61  ? 121 TRP D HE1    1 
ATOM   6959  H  HE3    . TRP C 2 122 ? 31.637  38.088  32.879  1.00 36.03  ? 121 TRP D HE3    1 
ATOM   6960  H  HZ2    . TRP C 2 122 ? 30.832  34.196  30.415  1.00 34.81  ? 121 TRP D HZ2    1 
ATOM   6961  H  HZ3    . TRP C 2 122 ? 31.077  38.194  30.643  1.00 37.43  ? 121 TRP D HZ3    1 
ATOM   6962  H  HH2    . TRP C 2 122 ? 30.766  36.262  29.413  1.00 35.89  ? 121 TRP D HH2    1 
ATOM   6963  N  N      . LEU C 2 123 ? 35.390  35.169  34.883  1.00 29.78  ? 122 LEU D N      1 
ATOM   6964  C  CA     . LEU C 2 123 ? 36.341  34.074  35.048  1.00 28.31  ? 122 LEU D CA     1 
ATOM   6965  C  C      . LEU C 2 123 ? 37.675  34.576  35.617  1.00 28.30  ? 122 LEU D C      1 
ATOM   6966  O  O      . LEU C 2 123 ? 38.536  33.773  35.977  1.00 27.89  ? 122 LEU D O      1 
ATOM   6967  C  CB     . LEU C 2 123 ? 36.541  33.373  33.684  1.00 25.45  ? 122 LEU D CB     1 
ATOM   6968  C  CG     . LEU C 2 123 ? 35.256  32.809  33.071  1.00 25.55  ? 122 LEU D CG     1 
ATOM   6969  C  CD1    . LEU C 2 123 ? 35.531  32.225  31.708  1.00 24.30  ? 122 LEU D CD1    1 
ATOM   6970  C  CD2    . LEU C 2 123 ? 34.593  31.761  33.973  1.00 29.51  ? 122 LEU D CD2    1 
ATOM   6971  H  H      . LEU C 2 123 ? 35.420  35.527  34.101  1.00 35.76  ? 122 LEU D H      1 
ATOM   6972  H  HA     . LEU C 2 123 ? 36.001  33.402  35.660  1.00 34.01  ? 122 LEU D HA     1 
ATOM   6973  H  HB2    . LEU C 2 123 ? 36.908  34.015  33.057  1.00 30.57  ? 122 LEU D HB2    1 
ATOM   6974  H  HB3    . LEU C 2 123 ? 37.159  32.635  33.803  1.00 30.57  ? 122 LEU D HB3    1 
ATOM   6975  H  HG     . LEU C 2 123 ? 34.628  33.542  32.978  1.00 30.70  ? 122 LEU D HG     1 
ATOM   6976  H  HD11   . LEU C 2 123 ? 34.705  31.872  31.342  1.00 29.19  ? 122 LEU D HD11   1 
ATOM   6977  H  HD12   . LEU C 2 123 ? 35.878  32.922  31.129  1.00 29.19  ? 122 LEU D HD12   1 
ATOM   6978  H  HD13   . LEU C 2 123 ? 36.184  31.513  31.795  1.00 29.19  ? 122 LEU D HD13   1 
ATOM   6979  H  HD21   . LEU C 2 123 ? 33.844  31.366  33.501  1.00 35.45  ? 122 LEU D HD21   1 
ATOM   6980  H  HD22   . LEU C 2 123 ? 35.244  31.077  34.193  1.00 35.45  ? 122 LEU D HD22   1 
ATOM   6981  H  HD23   . LEU C 2 123 ? 34.282  32.194  34.784  1.00 35.45  ? 122 LEU D HD23   1 
ATOM   6982  N  N      . ASP C 2 124 ? 37.837  35.878  35.743  1.00 27.12  ? 123 ASP D N      1 
ATOM   6983  C  CA     . ASP C 2 124 ? 39.107  36.431  36.201  1.00 30.47  ? 123 ASP D CA     1 
ATOM   6984  C  C      . ASP C 2 124 ? 39.356  35.978  37.634  1.00 32.66  ? 123 ASP D C      1 
ATOM   6985  O  O      . ASP C 2 124 ? 38.423  35.912  38.450  1.00 31.49  ? 123 ASP D O      1 
ATOM   6986  C  CB     . ASP C 2 124 ? 39.080  37.954  36.138  1.00 32.48  ? 123 ASP D CB     1 
ATOM   6987  C  CG     . ASP C 2 124 ? 39.066  38.522  34.714  1.00 30.86  ? 123 ASP D CG     1 
ATOM   6988  O  OD1    . ASP C 2 124 ? 39.250  37.802  33.685  1.00 28.86  ? 123 ASP D OD1    1 
ATOM   6989  O  OD2    . ASP C 2 124 ? 38.909  39.757  34.632  1.00 30.01  ? 123 ASP D OD2    1 
ATOM   6990  H  H      . ASP C 2 124 ? 37.233  36.466  35.572  1.00 32.48  ? 123 ASP D H      1 
ATOM   6991  H  HA     . ASP C 2 124 ? 39.829  36.125  35.630  1.00 36.60  ? 123 ASP D HA     1 
ATOM   6992  H  HB2    . ASP C 2 124 ? 38.281  38.270  36.588  1.00 39.01  ? 123 ASP D HB2    1 
ATOM   6993  H  HB3    . ASP C 2 124 ? 39.870  38.298  36.584  1.00 39.01  ? 123 ASP D HB3    1 
ATOM   6994  N  N      . GLY C 2 125 ? 40.612  35.657  37.956  1.00 30.52  ? 124 GLY D N      1 
ATOM   6995  C  CA     . GLY C 2 125 ? 40.904  35.174  39.299  1.00 31.82  ? 124 GLY D CA     1 
ATOM   6996  C  C      . GLY C 2 125 ? 40.505  33.729  39.561  1.00 30.89  ? 124 GLY D C      1 
ATOM   6997  O  O      . GLY C 2 125 ? 40.741  33.227  40.670  1.00 31.95  ? 124 GLY D O      1 
ATOM   6998  H  H      . GLY C 2 125 ? 41.288  35.710  37.427  1.00 36.66  ? 124 GLY D H      1 
ATOM   6999  H  HA2    . GLY C 2 125 ? 41.858  35.250  39.456  1.00 38.22  ? 124 GLY D HA2    1 
ATOM   7000  H  HA3    . GLY C 2 125 ? 40.432  35.731  39.939  1.00 38.22  ? 124 GLY D HA3    1 
ATOM   7001  N  N      . LYS C 2 126 ? 39.905  33.052  38.588  1.00 29.70  ? 125 LYS D N      1 
ATOM   7002  C  CA     . LYS C 2 126 ? 39.485  31.659  38.725  1.00 32.68  ? 125 LYS D CA     1 
ATOM   7003  C  C      . LYS C 2 126 ? 40.111  30.725  37.708  1.00 30.31  ? 125 LYS D C      1 
ATOM   7004  O  O      . LYS C 2 126 ? 40.387  29.561  38.024  1.00 34.75  ? 125 LYS D O      1 
ATOM   7005  C  CB     . LYS C 2 126 ? 37.961  31.565  38.616  1.00 34.95  ? 125 LYS D CB     1 
ATOM   7006  C  CG     . LYS C 2 126 ? 37.271  32.147  39.825  1.00 36.50  ? 125 LYS D CG     1 
ATOM   7007  C  CD     . LYS C 2 126 ? 36.000  32.912  39.470  1.00 42.20  ? 125 LYS D CD     1 
ATOM   7008  C  CE     . LYS C 2 126 ? 35.279  33.339  40.750  1.00 50.49  ? 125 LYS D CE     1 
ATOM   7009  N  NZ     . LYS C 2 126 ? 33.842  33.557  40.459  1.00 61.07  ? 125 LYS D NZ     1 
ATOM   7010  H  H      . LYS C 2 126 ? 39.724  33.387  37.817  1.00 35.56  ? 125 LYS D H      1 
ATOM   7011  H  HA     . LYS C 2 126 ? 39.752  31.347  39.604  1.00 39.25  ? 125 LYS D HA     1 
ATOM   7012  H  HB2    . LYS C 2 126 ? 37.667  32.056  37.832  1.00 41.98  ? 125 LYS D HB2    1 
ATOM   7013  H  HB3    . LYS C 2 126 ? 37.704  30.633  38.538  1.00 41.98  ? 125 LYS D HB3    1 
ATOM   7014  H  HG2    . LYS C 2 126 ? 37.028  31.426  40.427  1.00 43.83  ? 125 LYS D HG2    1 
ATOM   7015  H  HG3    . LYS C 2 126 ? 37.876  32.761  40.269  1.00 43.83  ? 125 LYS D HG3    1 
ATOM   7016  H  HD2    . LYS C 2 126 ? 36.227  33.705  38.959  1.00 50.67  ? 125 LYS D HD2    1 
ATOM   7017  H  HD3    . LYS C 2 126 ? 35.408  32.343  38.953  1.00 50.67  ? 125 LYS D HD3    1 
ATOM   7018  H  HE2    . LYS C 2 126 ? 35.361  32.643  41.421  1.00 60.62  ? 125 LYS D HE2    1 
ATOM   7019  H  HE3    . LYS C 2 126 ? 35.661  34.167  41.081  1.00 60.62  ? 125 LYS D HE3    1 
ATOM   7020  H  HZ1    . LYS C 2 126 ? 33.441  33.923  41.165  1.00 73.31  ? 125 LYS D HZ1    1 
ATOM   7021  H  HZ2    . LYS C 2 126 ? 33.751  34.102  39.761  1.00 73.31  ? 125 LYS D HZ2    1 
ATOM   7022  H  HZ3    . LYS C 2 126 ? 33.447  32.782  40.272  1.00 73.31  ? 125 LYS D HZ3    1 
ATOM   7023  N  N      . HIS C 2 127 ? 40.295  31.188  36.487  1.00 27.83  ? 126 HIS D N      1 
ATOM   7024  C  CA     . HIS C 2 127 ? 40.935  30.439  35.420  1.00 27.16  ? 126 HIS D CA     1 
ATOM   7025  C  C      . HIS C 2 127 ? 42.249  31.127  35.076  1.00 27.49  ? 126 HIS D C      1 
ATOM   7026  O  O      . HIS C 2 127 ? 42.324  32.362  35.005  1.00 27.57  ? 126 HIS D O      1 
ATOM   7027  C  CB     . HIS C 2 127 ? 39.996  30.358  34.230  1.00 28.72  ? 126 HIS D CB     1 
ATOM   7028  C  CG     . HIS C 2 127 ? 38.771  29.546  34.518  1.00 27.34  ? 126 HIS D CG     1 
ATOM   7029  N  ND1    . HIS C 2 127 ? 38.715  28.195  34.266  1.00 25.80  ? 126 HIS D ND1    1 
ATOM   7030  C  CD2    . HIS C 2 127 ? 37.584  29.873  35.093  1.00 29.57  ? 126 HIS D CD2    1 
ATOM   7031  C  CE1    . HIS C 2 127 ? 37.523  27.731  34.621  1.00 27.19  ? 126 HIS D CE1    1 
ATOM   7032  N  NE2    . HIS C 2 127 ? 36.826  28.722  35.143  1.00 28.47  ? 126 HIS D NE2    1 
ATOM   7033  H  H      . HIS C 2 127 ? 40.046  31.972  36.238  1.00 33.23  ? 126 HIS D H      1 
ATOM   7034  H  HA     . HIS C 2 127 ? 41.148  29.529  35.680  1.00 32.43  ? 126 HIS D HA     1 
ATOM   7035  H  HB2    . HIS C 2 127 ? 39.714  31.253  33.988  1.00 34.50  ? 126 HIS D HB2    1 
ATOM   7036  H  HB3    . HIS C 2 127 ? 40.463  29.945  33.487  1.00 34.50  ? 126 HIS D HB3    1 
ATOM   7037  H  HD1    . HIS C 2 127 ? 39.352  27.725  33.930  1.00 31.00  ? 126 HIS D HD1    1 
ATOM   7038  H  HD2    . HIS C 2 127 ? 37.331  30.715  35.396  1.00 35.51  ? 126 HIS D HD2    1 
ATOM   7039  H  HE1    . HIS C 2 127 ? 37.229  26.854  34.519  1.00 32.66  ? 126 HIS D HE1    1 
ATOM   7040  N  N      . VAL C 2 128 ? 43.304  30.327  34.913  1.00 28.65  ? 127 VAL D N      1 
ATOM   7041  C  CA     . VAL C 2 128 ? 44.637  30.874  34.633  1.00 29.09  ? 127 VAL D CA     1 
ATOM   7042  C  C      . VAL C 2 128 ? 44.736  31.202  33.150  1.00 27.19  ? 127 VAL D C      1 
ATOM   7043  O  O      . VAL C 2 128 ? 44.734  30.304  32.304  1.00 26.55  ? 127 VAL D O      1 
ATOM   7044  C  CB     . VAL C 2 128 ? 45.752  29.908  35.061  1.00 29.11  ? 127 VAL D CB     1 
ATOM   7045  C  CG1    . VAL C 2 128 ? 47.133  30.441  34.629  1.00 29.53  ? 127 VAL D CG1    1 
ATOM   7046  C  CG2    . VAL C 2 128 ? 45.695  29.642  36.600  1.00 30.31  ? 127 VAL D CG2    1 
ATOM   7047  H  H      . VAL C 2 128 ? 43.276  29.469  34.958  1.00 34.41  ? 127 VAL D H      1 
ATOM   7048  H  HA     . VAL C 2 128 ? 44.738  31.700  35.131  1.00 34.94  ? 127 VAL D HA     1 
ATOM   7049  H  HB     . VAL C 2 128 ? 45.618  29.058  34.614  1.00 34.76  ? 127 VAL D HB     1 
ATOM   7050  H  HG11   . VAL C 2 128 ? 47.824  29.937  35.088  1.00 35.26  ? 127 VAL D HG11   1 
ATOM   7051  H  HG12   . VAL C 2 128 ? 47.228  30.333  33.670  1.00 35.26  ? 127 VAL D HG12   1 
ATOM   7052  H  HG13   . VAL C 2 128 ? 47.197  31.379  34.865  1.00 35.26  ? 127 VAL D HG13   1 
ATOM   7053  H  HG21   . VAL C 2 128 ? 46.418  29.043  36.844  1.00 36.21  ? 127 VAL D HG21   1 
ATOM   7054  H  HG22   . VAL C 2 128 ? 45.791  30.485  37.070  1.00 36.21  ? 127 VAL D HG22   1 
ATOM   7055  H  HG23   . VAL C 2 128 ? 44.841  29.237  36.819  1.00 36.21  ? 127 VAL D HG23   1 
ATOM   7056  N  N      . VAL C 2 129 ? 44.853  32.493  32.829  1.00 27.09  ? 128 VAL D N      1 
ATOM   7057  C  CA     . VAL C 2 129 ? 45.078  32.936  31.456  1.00 26.28  ? 128 VAL D CA     1 
ATOM   7058  C  C      . VAL C 2 129 ? 46.545  32.743  31.118  1.00 26.78  ? 128 VAL D C      1 
ATOM   7059  O  O      . VAL C 2 129 ? 47.419  33.180  31.882  1.00 27.79  ? 128 VAL D O      1 
ATOM   7060  C  CB     . VAL C 2 129 ? 44.675  34.412  31.296  1.00 26.13  ? 128 VAL D CB     1 
ATOM   7061  C  CG1    . VAL C 2 129 ? 45.146  34.988  29.944  1.00 25.54  ? 128 VAL D CG1    1 
ATOM   7062  C  CG2    . VAL C 2 129 ? 43.154  34.586  31.413  1.00 25.56  ? 128 VAL D CG2    1 
ATOM   7063  H  H      . VAL C 2 129 ? 44.805  33.138  33.397  1.00 32.34  ? 128 VAL D H      1 
ATOM   7064  H  HA     . VAL C 2 129 ? 44.542  32.398  30.851  1.00 31.37  ? 128 VAL D HA     1 
ATOM   7065  H  HB     . VAL C 2 129 ? 45.109  34.904  32.010  1.00 31.19  ? 128 VAL D HB     1 
ATOM   7066  H  HG11   . VAL C 2 129 ? 44.664  35.810  29.766  1.00 30.58  ? 128 VAL D HG11   1 
ATOM   7067  H  HG12   . VAL C 2 129 ? 46.099  35.166  29.992  1.00 30.58  ? 128 VAL D HG12   1 
ATOM   7068  H  HG13   . VAL C 2 129 ? 44.966  34.340  29.245  1.00 30.58  ? 128 VAL D HG13   1 
ATOM   7069  H  HG21   . VAL C 2 129 ? 42.937  35.528  31.329  1.00 30.50  ? 128 VAL D HG21   1 
ATOM   7070  H  HG22   . VAL C 2 129 ? 42.723  34.082  30.705  1.00 30.50  ? 128 VAL D HG22   1 
ATOM   7071  H  HG23   . VAL C 2 129 ? 42.864  34.256  32.278  1.00 30.50  ? 128 VAL D HG23   1 
ATOM   7072  N  N      . PHE C 2 130 ? 46.832  32.134  29.949  1.00 26.14  ? 129 PHE D N      1 
ATOM   7073  C  CA     . PHE C 2 130 ? 48.222  31.852  29.619  1.00 26.69  ? 129 PHE D CA     1 
ATOM   7074  C  C      . PHE C 2 130 ? 48.596  32.061  28.160  1.00 26.04  ? 129 PHE D C      1 
ATOM   7075  O  O      . PHE C 2 130 ? 49.757  31.821  27.809  1.00 28.63  ? 129 PHE D O      1 
ATOM   7076  C  CB     . PHE C 2 130 ? 48.599  30.427  30.036  1.00 28.02  ? 129 PHE D CB     1 
ATOM   7077  C  CG     . PHE C 2 130 ? 47.875  29.365  29.252  1.00 26.25  ? 129 PHE D CG     1 
ATOM   7078  C  CD1    . PHE C 2 130 ? 46.603  28.899  29.642  1.00 25.77  ? 129 PHE D CD1    1 
ATOM   7079  C  CD2    . PHE C 2 130 ? 48.444  28.844  28.105  1.00 27.32  ? 129 PHE D CD2    1 
ATOM   7080  C  CE1    . PHE C 2 130 ? 45.926  27.933  28.883  1.00 24.96  ? 129 PHE D CE1    1 
ATOM   7081  C  CE2    . PHE C 2 130 ? 47.795  27.873  27.376  1.00 27.59  ? 129 PHE D CE2    1 
ATOM   7082  C  CZ     . PHE C 2 130 ? 46.530  27.414  27.755  1.00 24.66  ? 129 PHE D CZ     1 
ATOM   7083  H  H      . PHE C 2 130 ? 46.255  31.888  29.361  1.00 31.19  ? 129 PHE D H      1 
ATOM   7084  H  HA     . PHE C 2 130 ? 48.767  32.468  30.133  1.00 31.86  ? 129 PHE D HA     1 
ATOM   7085  H  HB2    . PHE C 2 130 ? 49.551  30.301  29.898  1.00 33.66  ? 129 PHE D HB2    1 
ATOM   7086  H  HB3    . PHE C 2 130 ? 48.381  30.306  30.973  1.00 33.66  ? 129 PHE D HB3    1 
ATOM   7087  H  HD1    . PHE C 2 130 ? 46.207  29.236  30.413  1.00 30.75  ? 129 PHE D HD1    1 
ATOM   7088  H  HD2    . PHE C 2 130 ? 49.274  29.153  27.823  1.00 32.82  ? 129 PHE D HD2    1 
ATOM   7089  H  HE1    . PHE C 2 130 ? 45.079  27.645  29.136  1.00 29.78  ? 129 PHE D HE1    1 
ATOM   7090  H  HE2    . PHE C 2 130 ? 48.204  27.517  26.620  1.00 33.15  ? 129 PHE D HE2    1 
ATOM   7091  H  HZ     . PHE C 2 130 ? 46.097  26.763  27.250  1.00 29.42  ? 129 PHE D HZ     1 
ATOM   7092  N  N      . GLY C 2 131 ? 47.698  32.548  27.324  1.00 25.07  ? 130 GLY D N      1 
ATOM   7093  C  CA     . GLY C 2 131 ? 48.107  32.924  25.991  1.00 25.27  ? 130 GLY D CA     1 
ATOM   7094  C  C      . GLY C 2 131 ? 47.014  33.666  25.273  1.00 23.97  ? 130 GLY D C      1 
ATOM   7095  O  O      . GLY C 2 131 ? 46.032  34.097  25.869  1.00 23.53  ? 130 GLY D O      1 
ATOM   7096  H  H      . GLY C 2 131 ? 46.865  32.667  27.501  1.00 30.06  ? 130 GLY D H      1 
ATOM   7097  H  HA2    . GLY C 2 131 ? 48.889  33.495  26.040  1.00 30.35  ? 130 GLY D HA2    1 
ATOM   7098  H  HA3    . GLY C 2 131 ? 48.327  32.128  25.482  1.00 30.35  ? 130 GLY D HA3    1 
ATOM   7099  N  N      . LYS C 2 132 ? 47.203  33.794  23.963  1.00 24.33  ? 131 LYS D N      1 
ATOM   7100  C  CA     . LYS C 2 132 ? 46.240  34.490  23.137  1.00 23.74  ? 131 LYS D CA     1 
ATOM   7101  C  C      . LYS C 2 132 ? 46.453  34.049  21.703  1.00 24.43  ? 131 LYS D C      1 
ATOM   7102  O  O      . LYS C 2 132 ? 47.580  33.734  21.288  1.00 27.84  ? 131 LYS D O      1 
ATOM   7103  C  CB     . LYS C 2 132 ? 46.397  36.010  23.249  1.00 25.64  ? 131 LYS D CB     1 
ATOM   7104  C  CG     . LYS C 2 132 ? 47.710  36.563  22.728  1.00 32.32  ? 131 LYS D CG     1 
ATOM   7105  C  CD     . LYS C 2 132 ? 47.605  38.084  22.475  1.00 34.91  ? 131 LYS D CD     1 
ATOM   7106  C  CE     . LYS C 2 132 ? 48.906  38.690  22.003  1.00 39.86  ? 131 LYS D CE     1 
ATOM   7107  N  NZ     . LYS C 2 132 ? 49.166  40.000  22.656  1.00 49.77  ? 131 LYS D NZ     1 
ATOM   7108  H  H      . LYS C 2 132 ? 47.882  33.484  23.535  1.00 29.23  ? 131 LYS D H      1 
ATOM   7109  H  HA     . LYS C 2 132 ? 45.340  34.258  23.413  1.00 28.53  ? 131 LYS D HA     1 
ATOM   7110  H  HB2    . LYS C 2 132 ? 45.684  36.429  22.743  1.00 30.80  ? 131 LYS D HB2    1 
ATOM   7111  H  HB3    . LYS C 2 132 ? 46.330  36.257  24.185  1.00 30.80  ? 131 LYS D HB3    1 
ATOM   7112  H  HG2    . LYS C 2 132 ? 48.409  36.407  23.382  1.00 38.82  ? 131 LYS D HG2    1 
ATOM   7113  H  HG3    . LYS C 2 132 ? 47.935  36.127  21.891  1.00 38.82  ? 131 LYS D HG3    1 
ATOM   7114  H  HD2    . LYS C 2 132 ? 46.934  38.246  21.793  1.00 41.92  ? 131 LYS D HD2    1 
ATOM   7115  H  HD3    . LYS C 2 132 ? 47.351  38.525  23.301  1.00 41.92  ? 131 LYS D HD3    1 
ATOM   7116  H  HE2    . LYS C 2 132 ? 49.637  38.090  22.221  1.00 47.86  ? 131 LYS D HE2    1 
ATOM   7117  H  HE3    . LYS C 2 132 ? 48.867  38.830  21.044  1.00 47.86  ? 131 LYS D HE3    1 
ATOM   7118  H  HZ1    . LYS C 2 132 ? 49.937  40.337  22.366  1.00 59.76  ? 131 LYS D HZ1    1 
ATOM   7119  H  HZ2    . LYS C 2 132 ? 48.510  40.570  22.464  1.00 59.76  ? 131 LYS D HZ2    1 
ATOM   7120  H  HZ3    . LYS C 2 132 ? 49.210  39.896  23.539  1.00 59.76  ? 131 LYS D HZ3    1 
ATOM   7121  N  N      . VAL C 2 133 ? 45.353  34.039  20.953  1.00 23.56  ? 132 VAL D N      1 
ATOM   7122  C  CA     . VAL C 2 133 ? 45.419  33.807  19.521  1.00 23.25  ? 132 VAL D CA     1 
ATOM   7123  C  C      . VAL C 2 133 ? 46.318  34.848  18.892  1.00 24.66  ? 132 VAL D C      1 
ATOM   7124  O  O      . VAL C 2 133 ? 46.176  36.049  19.147  1.00 23.96  ? 132 VAL D O      1 
ATOM   7125  C  CB     . VAL C 2 133 ? 44.007  33.829  18.919  1.00 24.89  ? 132 VAL D CB     1 
ATOM   7126  C  CG1    . VAL C 2 133 ? 44.079  33.654  17.400  1.00 21.84  ? 132 VAL D CG1    1 
ATOM   7127  C  CG2    . VAL C 2 133 ? 43.175  32.739  19.527  1.00 20.42  ? 132 VAL D CG2    1 
ATOM   7128  H  H      . VAL C 2 133 ? 44.556  34.164  21.253  1.00 28.30  ? 132 VAL D H      1 
ATOM   7129  H  HA     . VAL C 2 133 ? 45.804  32.933  19.350  1.00 27.93  ? 132 VAL D HA     1 
ATOM   7130  H  HB     . VAL C 2 133 ? 43.589  34.683  19.110  1.00 29.91  ? 132 VAL D HB     1 
ATOM   7131  H  HG11   . VAL C 2 133 ? 43.187  33.485  17.059  1.00 26.25  ? 132 VAL D HG11   1 
ATOM   7132  H  HG12   . VAL C 2 133 ? 44.436  34.466  17.005  1.00 26.25  ? 132 VAL D HG12   1 
ATOM   7133  H  HG13   . VAL C 2 133 ? 44.659  32.904  17.195  1.00 26.25  ? 132 VAL D HG13   1 
ATOM   7134  H  HG21   . VAL C 2 133 ? 42.323  32.697  19.066  1.00 24.54  ? 132 VAL D HG21   1 
ATOM   7135  H  HG22   . VAL C 2 133 ? 43.644  31.895  19.435  1.00 24.54  ? 132 VAL D HG22   1 
ATOM   7136  H  HG23   . VAL C 2 133 ? 43.033  32.937  20.466  1.00 24.54  ? 132 VAL D HG23   1 
ATOM   7137  N  N      . LYS C 2 134 ? 47.274  34.376  18.070  1.00 27.28  ? 133 LYS D N      1 
ATOM   7138  C  CA     . LYS C 2 134 ? 48.126  35.237  17.255  1.00 27.81  ? 133 LYS D CA     1 
ATOM   7139  C  C      . LYS C 2 134 ? 47.527  35.355  15.859  1.00 28.59  ? 133 LYS D C      1 
ATOM   7140  O  O      . LYS C 2 134 ? 47.032  36.418  15.474  1.00 34.23  ? 133 LYS D O      1 
ATOM   7141  C  CB     . LYS C 2 134 ? 49.530  34.670  17.223  1.00 28.63  ? 133 LYS D CB     1 
ATOM   7142  C  CG     . LYS C 2 134 ? 50.537  35.578  16.568  1.00 40.03  ? 133 LYS D CG     1 
ATOM   7143  C  CD     . LYS C 2 134 ? 51.839  34.886  16.203  1.00 42.45  ? 133 LYS D CD     1 
ATOM   7144  C  CE     . LYS C 2 134 ? 52.778  34.734  17.371  1.00 40.79  ? 133 LYS D CE     1 
ATOM   7145  N  NZ     . LYS C 2 134 ? 54.192  34.769  16.875  1.00 49.01  ? 133 LYS D NZ     1 
ATOM   7146  H  H      . LYS C 2 134 ? 47.446  33.540  17.970  1.00 32.77  ? 133 LYS D H      1 
ATOM   7147  H  HA     . LYS C 2 134 ? 48.186  36.130  17.628  1.00 33.41  ? 133 LYS D HA     1 
ATOM   7148  H  HB2    . LYS C 2 134 ? 49.823  34.512  18.134  1.00 34.39  ? 133 LYS D HB2    1 
ATOM   7149  H  HB3    . LYS C 2 134 ? 49.519  33.836  16.728  1.00 34.39  ? 133 LYS D HB3    1 
ATOM   7150  H  HG2    . LYS C 2 134 ? 50.153  35.934  15.751  1.00 48.07  ? 133 LYS D HG2    1 
ATOM   7151  H  HG3    . LYS C 2 134 ? 50.749  36.302  17.178  1.00 48.07  ? 133 LYS D HG3    1 
ATOM   7152  H  HD2    . LYS C 2 134 ? 51.639  33.999  15.864  1.00 50.98  ? 133 LYS D HD2    1 
ATOM   7153  H  HD3    . LYS C 2 134 ? 52.292  35.407  15.522  1.00 50.98  ? 133 LYS D HD3    1 
ATOM   7154  H  HE2    . LYS C 2 134 ? 52.647  35.463  17.998  1.00 48.98  ? 133 LYS D HE2    1 
ATOM   7155  H  HE3    . LYS C 2 134 ? 52.621  33.885  17.813  1.00 48.98  ? 133 LYS D HE3    1 
ATOM   7156  H  HZ1    . LYS C 2 134 ? 54.757  34.712  17.560  1.00 58.85  ? 133 LYS D HZ1    1 
ATOM   7157  H  HZ2    . LYS C 2 134 ? 54.338  34.086  16.323  1.00 58.85  ? 133 LYS D HZ2    1 
ATOM   7158  H  HZ3    . LYS C 2 134 ? 54.343  35.530  16.439  1.00 58.85  ? 133 LYS D HZ3    1 
ATOM   7159  N  N      . GLU C 2 135 ? 47.540  34.277  15.094  1.00 25.93  ? 134 GLU D N      1 
ATOM   7160  C  CA     . GLU C 2 135 ? 46.885  34.268  13.796  1.00 29.56  ? 134 GLU D CA     1 
ATOM   7161  C  C      . GLU C 2 135 ? 45.715  33.298  13.826  1.00 24.58  ? 134 GLU D C      1 
ATOM   7162  O  O      . GLU C 2 135 ? 45.699  32.347  14.614  1.00 27.04  ? 134 GLU D O      1 
ATOM   7163  C  CB     . GLU C 2 135 ? 47.848  33.875  12.676  1.00 34.46  ? 134 GLU D CB     1 
ATOM   7164  C  CG     . GLU C 2 135 ? 49.271  34.377  12.875  1.00 39.71  ? 134 GLU D CG     1 
ATOM   7165  C  CD     . GLU C 2 135 ? 50.322  33.446  12.263  1.00 46.98  ? 134 GLU D CD     1 
ATOM   7166  O  OE1    . GLU C 2 135 ? 51.076  32.768  13.037  1.00 43.59  ? 134 GLU D OE1    1 
ATOM   7167  O  OE2    . GLU C 2 135 ? 50.392  33.410  11.004  1.00 41.70  ? 134 GLU D OE2    1 
ATOM   7168  H  H      . GLU C 2 135 ? 47.922  33.536  15.304  1.00 31.15  ? 134 GLU D H      1 
ATOM   7169  H  HA     . GLU C 2 135 ? 46.554  35.159  13.599  1.00 35.50  ? 134 GLU D HA     1 
ATOM   7170  H  HB2    . GLU C 2 135 ? 47.882  32.907  12.621  1.00 41.39  ? 134 GLU D HB2    1 
ATOM   7171  H  HB3    . GLU C 2 135 ? 47.520  34.243  11.841  1.00 41.39  ? 134 GLU D HB3    1 
ATOM   7172  H  HG2    . GLU C 2 135 ? 49.361  35.247  12.456  1.00 47.68  ? 134 GLU D HG2    1 
ATOM   7173  H  HG3    . GLU C 2 135 ? 49.451  34.447  13.826  1.00 47.68  ? 134 GLU D HG3    1 
ATOM   7174  N  N      . GLY C 2 136 ? 44.742  33.552  12.961  1.00 25.36  ? 135 GLY D N      1 
ATOM   7175  C  CA     . GLY C 2 136 ? 43.624  32.639  12.796  1.00 23.69  ? 135 GLY D CA     1 
ATOM   7176  C  C      . GLY C 2 136 ? 42.426  32.869  13.683  1.00 22.39  ? 135 GLY D C      1 
ATOM   7177  O  O      . GLY C 2 136 ? 41.605  31.952  13.849  1.00 22.95  ? 135 GLY D O      1 
ATOM   7178  H  H      . GLY C 2 136 ? 44.707  34.248  12.457  1.00 30.46  ? 135 GLY D H      1 
ATOM   7179  H  HA2    . GLY C 2 136 ? 43.318  32.697  11.878  1.00 28.46  ? 135 GLY D HA2    1 
ATOM   7180  H  HA3    . GLY C 2 136 ? 43.940  31.738  12.967  1.00 28.46  ? 135 GLY D HA3    1 
ATOM   7181  N  N      . MET C 2 137 ? 42.270  34.063  14.254  1.00 23.29  ? 136 MET D N      1 
ATOM   7182  C  CA     . MET C 2 137 ? 41.041  34.337  14.995  1.00 21.79  ? 136 MET D CA     1 
ATOM   7183  C  C      . MET C 2 137 ? 39.820  34.052  14.144  1.00 22.19  ? 136 MET D C      1 
ATOM   7184  O  O      . MET C 2 137 ? 38.773  33.622  14.654  1.00 18.48  ? 136 MET D O      1 
ATOM   7185  C  CB     . MET C 2 137 ? 40.993  35.800  15.463  1.00 23.44  ? 136 MET D CB     1 
ATOM   7186  C  CG     . MET C 2 137 ? 40.027  36.076  16.628  1.00 26.42  ? 136 MET D CG     1 
ATOM   7187  S  SD     . MET C 2 137 ? 40.121  34.932  18.054  1.00 24.59  ? 136 MET D SD     1 
ATOM   7188  C  CE     . MET C 2 137 ? 38.399  34.895  18.599  1.00 22.76  ? 136 MET D CE     1 
ATOM   7189  H  H      . MET C 2 137 ? 42.839  34.708  14.229  1.00 27.98  ? 136 MET D H      1 
ATOM   7190  H  HA     . MET C 2 137 ? 41.039  33.775  15.785  1.00 26.19  ? 136 MET D HA     1 
ATOM   7191  H  HB2    . MET C 2 137 ? 41.882  36.059  15.754  1.00 28.16  ? 136 MET D HB2    1 
ATOM   7192  H  HB3    . MET C 2 137 ? 40.714  36.353  14.716  1.00 28.16  ? 136 MET D HB3    1 
ATOM   7193  H  HG2    . MET C 2 137 ? 40.210  36.967  16.966  1.00 31.74  ? 136 MET D HG2    1 
ATOM   7194  H  HG3    . MET C 2 137 ? 39.121  36.030  16.286  1.00 31.74  ? 136 MET D HG3    1 
ATOM   7195  H  HE1    . MET C 2 137 ? 38.317  34.284  19.347  1.00 27.35  ? 136 MET D HE1    1 
ATOM   7196  H  HE2    . MET C 2 137 ? 38.135  35.788  18.871  1.00 27.35  ? 136 MET D HE2    1 
ATOM   7197  H  HE3    . MET C 2 137 ? 37.842  34.595  17.864  1.00 27.35  ? 136 MET D HE3    1 
ATOM   7198  N  N      . ASN C 2 138 ? 39.921  34.271  12.817  1.00 21.44  ? 137 ASN D N      1 
ATOM   7199  C  CA     . ASN C 2 138 ? 38.750  34.025  11.987  1.00 23.71  ? 137 ASN D CA     1 
ATOM   7200  C  C      . ASN C 2 138 ? 38.371  32.553  11.979  1.00 19.83  ? 137 ASN D C      1 
ATOM   7201  O  O      . ASN C 2 138 ? 37.206  32.202  11.730  1.00 21.02  ? 137 ASN D O      1 
ATOM   7202  C  CB     . ASN C 2 138 ? 39.013  34.489  10.541  1.00 28.66  ? 137 ASN D CB     1 
ATOM   7203  C  CG     . ASN C 2 138 ? 40.077  33.657  9.859   1.00 26.52  ? 137 ASN D CG     1 
ATOM   7204  O  OD1    . ASN C 2 138 ? 41.216  33.624  10.314  1.00 26.09  ? 137 ASN D OD1    1 
ATOM   7205  N  ND2    . ASN C 2 138 ? 39.707  32.943  8.779   1.00 30.38  ? 137 ASN D ND2    1 
ATOM   7206  H  H      . ASN C 2 138 ? 40.623  34.548  12.404  1.00 25.76  ? 137 ASN D H      1 
ATOM   7207  H  HA     . ASN C 2 138 ? 38.009  34.536  12.348  1.00 28.48  ? 137 ASN D HA     1 
ATOM   7208  H  HB2    . ASN C 2 138 ? 38.193  34.412  10.028  1.00 34.43  ? 137 ASN D HB2    1 
ATOM   7209  H  HB3    . ASN C 2 138 ? 39.312  35.412  10.553  1.00 34.43  ? 137 ASN D HB3    1 
ATOM   7210  H  HD21   . ASN C 2 138 ? 40.284  32.459  8.365   1.00 36.49  ? 137 ASN D HD21   1 
ATOM   7211  H  HD22   . ASN C 2 138 ? 38.893  32.973  8.502   1.00 36.49  ? 137 ASN D HD22   1 
ATOM   7212  N  N      . ILE C 2 139 ? 39.334  31.677  12.224  1.00 20.67  ? 138 ILE D N      1 
ATOM   7213  C  CA     . ILE C 2 139 ? 39.013  30.257  12.306  1.00 20.41  ? 138 ILE D CA     1 
ATOM   7214  C  C      . ILE C 2 139 ? 38.274  29.955  13.598  1.00 20.43  ? 138 ILE D C      1 
ATOM   7215  O  O      . ILE C 2 139 ? 37.349  29.132  13.619  1.00 21.73  ? 138 ILE D O      1 
ATOM   7216  C  CB     . ILE C 2 139 ? 40.296  29.421  12.195  1.00 21.86  ? 138 ILE D CB     1 
ATOM   7217  C  CG1    . ILE C 2 139 ? 40.976  29.667  10.832  1.00 26.24  ? 138 ILE D CG1    1 
ATOM   7218  C  CG2    . ILE C 2 139 ? 39.989  27.947  12.326  1.00 21.19  ? 138 ILE D CG2    1 
ATOM   7219  C  CD1    . ILE C 2 139 ? 40.054  29.347  9.675   1.00 28.64  ? 138 ILE D CD1    1 
ATOM   7220  H  H      . ILE C 2 139 ? 40.163  31.872  12.344  1.00 24.84  ? 138 ILE D H      1 
ATOM   7221  H  HA     . ILE C 2 139 ? 38.432  30.028  11.563  1.00 24.52  ? 138 ILE D HA     1 
ATOM   7222  H  HB     . ILE C 2 139 ? 40.889  29.692  12.913  1.00 26.27  ? 138 ILE D HB     1 
ATOM   7223  H  HG12   . ILE C 2 139 ? 41.232  30.600  10.768  1.00 31.52  ? 138 ILE D HG12   1 
ATOM   7224  H  HG13   . ILE C 2 139 ? 41.761  29.102  10.761  1.00 31.52  ? 138 ILE D HG13   1 
ATOM   7225  H  HG21   . ILE C 2 139 ? 40.723  27.437  11.951  1.00 25.46  ? 138 ILE D HG21   1 
ATOM   7226  H  HG22   . ILE C 2 139 ? 39.880  27.730  13.265  1.00 25.46  ? 138 ILE D HG22   1 
ATOM   7227  H  HG23   . ILE C 2 139 ? 39.169  27.752  11.845  1.00 25.46  ? 138 ILE D HG23   1 
ATOM   7228  H  HD11   . ILE C 2 139 ? 40.572  29.327  8.855   1.00 34.41  ? 138 ILE D HD11   1 
ATOM   7229  H  HD12   . ILE C 2 139 ? 39.644  28.481  9.828   1.00 34.41  ? 138 ILE D HD12   1 
ATOM   7230  H  HD13   . ILE C 2 139 ? 39.370  30.031  9.618   1.00 34.41  ? 138 ILE D HD13   1 
ATOM   7231  N  N      . VAL C 2 140 ? 38.684  30.591  14.702  1.00 19.27  ? 139 VAL D N      1 
ATOM   7232  C  CA     . VAL C 2 140 ? 37.947  30.435  15.953  1.00 18.51  ? 139 VAL D CA     1 
ATOM   7233  C  C      . VAL C 2 140 ? 36.530  30.961  15.802  1.00 21.61  ? 139 VAL D C      1 
ATOM   7234  O  O      . VAL C 2 140 ? 35.561  30.353  16.292  1.00 20.74  ? 139 VAL D O      1 
ATOM   7235  C  CB     . VAL C 2 140 ? 38.688  31.134  17.107  1.00 20.85  ? 139 VAL D CB     1 
ATOM   7236  C  CG1    . VAL C 2 140 ? 37.905  30.945  18.392  1.00 21.17  ? 139 VAL D CG1    1 
ATOM   7237  C  CG2    . VAL C 2 140 ? 40.086  30.582  17.259  1.00 20.29  ? 139 VAL D CG2    1 
ATOM   7238  H  H      . VAL C 2 140 ? 39.371  31.106  14.749  1.00 23.16  ? 139 VAL D H      1 
ATOM   7239  H  HA     . VAL C 2 140 ? 37.897  29.490  16.161  1.00 22.24  ? 139 VAL D HA     1 
ATOM   7240  H  HB     . VAL C 2 140 ? 38.764  32.082  16.913  1.00 25.05  ? 139 VAL D HB     1 
ATOM   7241  H  HG11   . VAL C 2 140 ? 38.472  31.179  19.144  1.00 25.44  ? 139 VAL D HG11   1 
ATOM   7242  H  HG12   . VAL C 2 140 ? 37.125  31.520  18.374  1.00 25.44  ? 139 VAL D HG12   1 
ATOM   7243  H  HG13   . VAL C 2 140 ? 37.631  30.017  18.461  1.00 25.44  ? 139 VAL D HG13   1 
ATOM   7244  H  HG21   . VAL C 2 140 ? 40.499  30.980  18.040  1.00 24.38  ? 139 VAL D HG21   1 
ATOM   7245  H  HG22   . VAL C 2 140 ? 40.035  29.619  17.366  1.00 24.38  ? 139 VAL D HG22   1 
ATOM   7246  H  HG23   . VAL C 2 140 ? 40.600  30.800  16.465  1.00 24.38  ? 139 VAL D HG23   1 
ATOM   7247  N  N      . GLU C 2 141 ? 36.371  32.093  15.128  1.00 21.43  ? 140 GLU D N      1 
ATOM   7248  C  CA     . GLU C 2 141 ? 35.032  32.586  14.821  1.00 22.07  ? 140 GLU D CA     1 
ATOM   7249  C  C      . GLU C 2 141 ? 34.255  31.555  14.002  1.00 20.38  ? 140 GLU D C      1 
ATOM   7250  O  O      . GLU C 2 141 ? 33.109  31.230  14.329  1.00 21.51  ? 140 GLU D O      1 
ATOM   7251  C  CB     . GLU C 2 141 ? 35.130  33.938  14.089  1.00 25.48  ? 140 GLU D CB     1 
ATOM   7252  C  CG     . GLU C 2 141 ? 35.578  35.112  14.979  1.00 28.39  ? 140 GLU D CG     1 
ATOM   7253  C  CD     . GLU C 2 141 ? 36.205  36.261  14.180  1.00 33.33  ? 140 GLU D CD     1 
ATOM   7254  O  OE1    . GLU C 2 141 ? 36.153  36.235  12.934  1.00 33.13  ? 140 GLU D OE1    1 
ATOM   7255  O  OE2    . GLU C 2 141 ? 36.749  37.202  14.796  1.00 32.09  ? 140 GLU D OE2    1 
ATOM   7256  H  H      . GLU C 2 141 ? 37.012  32.590  14.841  1.00 25.75  ? 140 GLU D H      1 
ATOM   7257  H  HA     . GLU C 2 141 ? 34.542  32.738  15.644  1.00 26.52  ? 140 GLU D HA     1 
ATOM   7258  H  HB2    . GLU C 2 141 ? 35.774  33.853  13.368  1.00 30.61  ? 140 GLU D HB2    1 
ATOM   7259  H  HB3    . GLU C 2 141 ? 34.257  34.159  13.729  1.00 30.61  ? 140 GLU D HB3    1 
ATOM   7260  H  HG2    . GLU C 2 141 ? 34.806  35.461  15.452  1.00 34.10  ? 140 GLU D HG2    1 
ATOM   7261  H  HG3    . GLU C 2 141 ? 36.238  34.793  15.614  1.00 34.10  ? 140 GLU D HG3    1 
ATOM   7262  N  N      . ALA C 2 142 ? 34.866  31.011  12.950  1.00 19.76  ? 141 ALA D N      1 
ATOM   7263  C  CA     . ALA C 2 142 ? 34.187  30.019  12.127  1.00 17.95  ? 141 ALA D CA     1 
ATOM   7264  C  C      . ALA C 2 142 ? 33.794  28.814  12.965  1.00 22.54  ? 141 ALA D C      1 
ATOM   7265  O  O      . ALA C 2 142 ? 32.733  28.224  12.750  1.00 20.38  ? 141 ALA D O      1 
ATOM   7266  C  CB     . ALA C 2 142 ? 35.045  29.602  10.934  1.00 23.51  ? 141 ALA D CB     1 
ATOM   7267  H  H      . ALA C 2 142 ? 35.665  31.198  12.695  1.00 23.75  ? 141 ALA D H      1 
ATOM   7268  H  HA     . ALA C 2 142 ? 33.384  30.417  11.755  1.00 21.57  ? 141 ALA D HA     1 
ATOM   7269  H  HB1    . ALA C 2 142 ? 34.566  28.935  10.417  1.00 28.25  ? 141 ALA D HB1    1 
ATOM   7270  H  HB2    . ALA C 2 142 ? 35.223  30.381  10.384  1.00 28.25  ? 141 ALA D HB2    1 
ATOM   7271  H  HB3    . ALA C 2 142 ? 35.880  29.230  11.260  1.00 28.25  ? 141 ALA D HB3    1 
ATOM   7272  N  N      . MET C 2 143 ? 34.575  28.471  13.990  1.00 20.14  ? 142 MET D N      1 
ATOM   7273  C  CA     . MET C 2 143 ? 34.169  27.329  14.804  1.00 19.27  ? 142 MET D CA     1 
ATOM   7274  C  C      . MET C 2 143 ? 32.841  27.579  15.519  1.00 20.87  ? 142 MET D C      1 
ATOM   7275  O  O      . MET C 2 143 ? 32.087  26.638  15.756  1.00 21.09  ? 142 MET D O      1 
ATOM   7276  C  CB     . MET C 2 143 ? 35.245  26.958  15.837  1.00 20.97  ? 142 MET D CB     1 
ATOM   7277  C  CG     . MET C 2 143 ? 36.441  26.285  15.284  1.00 20.45  ? 142 MET D CG     1 
ATOM   7278  S  SD     . MET C 2 143 ? 37.983  26.591  16.179  1.00 28.14  ? 142 MET D SD     1 
ATOM   7279  C  CE     . MET C 2 143 ? 37.579  25.593  17.545  1.00 22.53  ? 142 MET D CE     1 
ATOM   7280  H  H      . MET C 2 143 ? 35.305  28.862  14.222  1.00 24.20  ? 142 MET D H      1 
ATOM   7281  H  HA     . MET C 2 143 ? 34.074  26.574  14.202  1.00 23.16  ? 142 MET D HA     1 
ATOM   7282  H  HB2    . MET C 2 143 ? 35.545  27.771  16.272  1.00 25.20  ? 142 MET D HB2    1 
ATOM   7283  H  HB3    . MET C 2 143 ? 34.850  26.359  16.490  1.00 25.20  ? 142 MET D HB3    1 
ATOM   7284  H  HG2    . MET C 2 143 ? 36.286  25.328  15.294  1.00 24.57  ? 142 MET D HG2    1 
ATOM   7285  H  HG3    . MET C 2 143 ? 36.570  26.591  14.372  1.00 24.57  ? 142 MET D HG3    1 
ATOM   7286  H  HE1    . MET C 2 143 ? 38.301  25.635  18.191  1.00 27.06  ? 142 MET D HE1    1 
ATOM   7287  H  HE2    . MET C 2 143 ? 36.759  25.922  17.944  1.00 27.06  ? 142 MET D HE2    1 
ATOM   7288  H  HE3    . MET C 2 143 ? 37.457  24.679  17.243  1.00 27.06  ? 142 MET D HE3    1 
ATOM   7289  N  N      . GLU C 2 144 ? 32.512  28.830  15.822  1.00 18.07  ? 143 GLU D N      1 
ATOM   7290  C  CA     . GLU C 2 144 ? 31.256  29.113  16.483  1.00 19.48  ? 143 GLU D CA     1 
ATOM   7291  C  C      . GLU C 2 144 ? 30.076  28.747  15.593  1.00 22.51  ? 143 GLU D C      1 
ATOM   7292  O  O      . GLU C 2 144 ? 28.968  28.625  16.102  1.00 21.92  ? 143 GLU D O      1 
ATOM   7293  C  CB     . GLU C 2 144 ? 31.141  30.576  16.860  1.00 20.64  ? 143 GLU D CB     1 
ATOM   7294  C  CG     . GLU C 2 144 ? 32.034  31.029  17.991  1.00 19.81  ? 143 GLU D CG     1 
ATOM   7295  C  CD     . GLU C 2 144 ? 31.676  32.374  18.518  1.00 23.12  ? 143 GLU D CD     1 
ATOM   7296  O  OE1    . GLU C 2 144 ? 31.405  33.288  17.718  1.00 26.00  ? 143 GLU D OE1    1 
ATOM   7297  O  OE2    . GLU C 2 144 ? 31.672  32.547  19.752  1.00 24.60  ? 143 GLU D OE2    1 
ATOM   7298  H  H      . GLU C 2 144 ? 32.996  29.522  15.656  1.00 21.71  ? 143 GLU D H      1 
ATOM   7299  H  HA     . GLU C 2 144 ? 31.228  28.599  17.305  1.00 23.41  ? 143 GLU D HA     1 
ATOM   7300  H  HB2    . GLU C 2 144 ? 31.366  31.110  16.083  1.00 24.80  ? 143 GLU D HB2    1 
ATOM   7301  H  HB3    . GLU C 2 144 ? 30.225  30.750  17.128  1.00 24.80  ? 143 GLU D HB3    1 
ATOM   7302  H  HG2    . GLU C 2 144 ? 31.964  30.394  18.721  1.00 23.81  ? 143 GLU D HG2    1 
ATOM   7303  H  HG3    . GLU C 2 144 ? 32.950  31.068  17.672  1.00 23.81  ? 143 GLU D HG3    1 
ATOM   7304  N  N      . ARG C 2 145 ? 30.299  28.579  14.287  1.00 22.48  ? 144 ARG D N      1 
ATOM   7305  C  CA     . ARG C 2 145 ? 29.202  28.147  13.423  1.00 21.92  ? 144 ARG D CA     1 
ATOM   7306  C  C      . ARG C 2 145 ? 28.593  26.838  13.890  1.00 23.72  ? 144 ARG D C      1 
ATOM   7307  O  O      . ARG C 2 145 ? 27.451  26.515  13.524  1.00 25.06  ? 144 ARG D O      1 
ATOM   7308  C  CB     . ARG C 2 145 ? 29.684  27.945  11.986  1.00 25.16  ? 144 ARG D CB     1 
ATOM   7309  C  CG     . ARG C 2 145 ? 30.207  29.175  11.303  1.00 24.47  ? 144 ARG D CG     1 
ATOM   7310  C  CD     . ARG C 2 145 ? 30.700  28.779  9.921   1.00 27.83  ? 144 ARG D CD     1 
ATOM   7311  N  NE     . ARG C 2 145 ? 31.410  29.850  9.237   1.00 32.01  ? 144 ARG D NE     1 
ATOM   7312  C  CZ     . ARG C 2 145 ? 32.358  29.650  8.331   1.00 28.44  ? 144 ARG D CZ     1 
ATOM   7313  N  NH1    . ARG C 2 145 ? 32.726  28.430  7.968   1.00 29.97  ? 144 ARG D NH1    1 
ATOM   7314  N  NH2    . ARG C 2 145 ? 32.974  30.697  7.801   1.00 32.74  ? 144 ARG D NH2    1 
ATOM   7315  H  H      . ARG C 2 145 ? 31.052  28.705  13.891  1.00 27.02  ? 144 ARG D H      1 
ATOM   7316  H  HA     . ARG C 2 145 ? 28.533  28.849  13.444  1.00 26.34  ? 144 ARG D HA     1 
ATOM   7317  H  HB2    . ARG C 2 145 ? 30.401  27.292  11.993  1.00 30.23  ? 144 ARG D HB2    1 
ATOM   7318  H  HB3    . ARG C 2 145 ? 28.941  27.615  11.458  1.00 30.23  ? 144 ARG D HB3    1 
ATOM   7319  H  HG2    . ARG C 2 145 ? 29.500  29.832  11.212  1.00 29.40  ? 144 ARG D HG2    1 
ATOM   7320  H  HG3    . ARG C 2 145 ? 30.945  29.549  11.809  1.00 29.40  ? 144 ARG D HG3    1 
ATOM   7321  H  HD2    . ARG C 2 145 ? 31.307  28.027  10.007  1.00 33.42  ? 144 ARG D HD2    1 
ATOM   7322  H  HD3    . ARG C 2 145 ? 29.938  28.531  9.375   1.00 33.42  ? 144 ARG D HD3    1 
ATOM   7323  H  HE     . ARG C 2 145 ? 31.202  30.662  9.432   1.00 38.45  ? 144 ARG D HE     1 
ATOM   7324  H  HH11   . ARG C 2 145 ? 32.347  27.743  8.322   1.00 36.00  ? 144 ARG D HH11   1 
ATOM   7325  H  HH12   . ARG C 2 145 ? 33.343  28.324  7.379   1.00 36.00  ? 144 ARG D HH12   1 
ATOM   7326  H  HH21   . ARG C 2 145 ? 32.757  31.493  8.046   1.00 39.32  ? 144 ARG D HH21   1 
ATOM   7327  H  HH22   . ARG C 2 145 ? 33.590  30.581  7.213   1.00 39.32  ? 144 ARG D HH22   1 
ATOM   7328  N  N      . PHE C 2 146 ? 29.372  26.015  14.611  1.00 20.65  ? 145 PHE D N      1 
ATOM   7329  C  CA     . PHE C 2 146 ? 28.977  24.659  14.965  1.00 22.69  ? 145 PHE D CA     1 
ATOM   7330  C  C      . PHE C 2 146 ? 28.732  24.479  16.463  1.00 20.94  ? 145 PHE D C      1 
ATOM   7331  O  O      . PHE C 2 146 ? 28.706  23.342  16.943  1.00 23.28  ? 145 PHE D O      1 
ATOM   7332  C  CB     . PHE C 2 146 ? 30.038  23.689  14.463  1.00 25.67  ? 145 PHE D CB     1 
ATOM   7333  C  CG     . PHE C 2 146 ? 30.368  23.900  13.014  1.00 25.90  ? 145 PHE D CG     1 
ATOM   7334  C  CD1    . PHE C 2 146 ? 29.399  23.695  12.039  1.00 30.02  ? 145 PHE D CD1    1 
ATOM   7335  C  CD2    . PHE C 2 146 ? 31.610  24.402  12.645  1.00 26.80  ? 145 PHE D CD2    1 
ATOM   7336  C  CE1    . PHE C 2 146 ? 29.692  23.949  10.692  1.00 29.71  ? 145 PHE D CE1    1 
ATOM   7337  C  CE2    . PHE C 2 146 ? 31.914  24.648  11.313  1.00 29.08  ? 145 PHE D CE2    1 
ATOM   7338  C  CZ     . PHE C 2 146 ? 30.957  24.412  10.342  1.00 28.01  ? 145 PHE D CZ     1 
ATOM   7339  H  H      . PHE C 2 146 ? 30.149  26.233  14.909  1.00 24.81  ? 145 PHE D H      1 
ATOM   7340  H  HA     . PHE C 2 146 ? 28.136  24.451  14.529  1.00 27.26  ? 145 PHE D HA     1 
ATOM   7341  H  HB2    . PHE C 2 146 ? 30.851  23.814  14.978  1.00 30.84  ? 145 PHE D HB2    1 
ATOM   7342  H  HB3    . PHE C 2 146 ? 29.714  22.781  14.569  1.00 30.84  ? 145 PHE D HB3    1 
ATOM   7343  H  HD1    . PHE C 2 146 ? 28.554  23.390  12.280  1.00 36.05  ? 145 PHE D HD1    1 
ATOM   7344  H  HD2    . PHE C 2 146 ? 32.247  24.576  13.300  1.00 32.19  ? 145 PHE D HD2    1 
ATOM   7345  H  HE1    . PHE C 2 146 ? 29.047  23.808  10.037  1.00 35.68  ? 145 PHE D HE1    1 
ATOM   7346  H  HE2    . PHE C 2 146 ? 32.754  24.969  11.075  1.00 34.93  ? 145 PHE D HE2    1 
ATOM   7347  H  HZ     . PHE C 2 146 ? 31.161  24.565  9.448   1.00 33.64  ? 145 PHE D HZ     1 
ATOM   7348  N  N      . GLY C 2 147 ? 28.542  25.568  17.202  1.00 23.30  ? 146 GLY D N      1 
ATOM   7349  C  CA     . GLY C 2 147 ? 28.209  25.494  18.611  1.00 23.00  ? 146 GLY D CA     1 
ATOM   7350  C  C      . GLY C 2 147 ? 26.724  25.651  18.885  1.00 25.20  ? 146 GLY D C      1 
ATOM   7351  O  O      . GLY C 2 147 ? 25.882  25.635  17.983  1.00 24.97  ? 146 GLY D O      1 
ATOM   7352  H  H      . GLY C 2 147 ? 28.602  26.371  16.901  1.00 28.00  ? 146 GLY D H      1 
ATOM   7353  H  HA2    . GLY C 2 147 ? 28.492  24.634  18.959  1.00 27.64  ? 146 GLY D HA2    1 
ATOM   7354  H  HA3    . GLY C 2 147 ? 28.680  26.197  19.085  1.00 27.64  ? 146 GLY D HA3    1 
ATOM   7355  N  N      . SER C 2 148 ? 26.399  25.776  20.174  1.00 21.45  ? 147 SER D N      1 
ATOM   7356  C  CA     . SER C 2 148 ? 25.016  25.901  20.601  1.00 23.57  ? 147 SER D CA     1 
ATOM   7357  C  C      . SER C 2 148 ? 25.001  26.548  21.981  1.00 24.79  ? 147 SER D C      1 
ATOM   7358  O  O      . SER C 2 148 ? 26.038  26.696  22.630  1.00 22.31  ? 147 SER D O      1 
ATOM   7359  C  CB     . SER C 2 148 ? 24.313  24.538  20.615  1.00 26.09  ? 147 SER D CB     1 
ATOM   7360  O  OG     . SER C 2 148 ? 24.827  23.684  21.634  1.00 25.51  ? 147 SER D OG     1 
ATOM   7361  H  H      . SER C 2 148 ? 26.968  25.791  20.819  1.00 25.77  ? 147 SER D H      1 
ATOM   7362  H  HA     . SER C 2 148 ? 24.536  26.481  19.989  1.00 28.31  ? 147 SER D HA     1 
ATOM   7363  H  HB2    . SER C 2 148 ? 23.367  24.677  20.773  1.00 31.34  ? 147 SER D HB2    1 
ATOM   7364  H  HB3    . SER C 2 148 ? 24.446  24.110  19.754  1.00 31.34  ? 147 SER D HB3    1 
ATOM   7365  H  HG     . SER C 2 148 ? 25.624  23.481  21.463  1.00 30.65  ? 147 SER D HG     1 
ATOM   7366  N  N      . ARG C 2 149 ? 23.819  26.938  22.417  1.00 24.57  ? 148 ARG D N      1 
ATOM   7367  C  CA     . ARG C 2 149 ? 23.676  27.589  23.711  1.00 26.89  ? 148 ARG D CA     1 
ATOM   7368  C  C      . ARG C 2 149 ? 24.294  26.780  24.851  1.00 26.47  ? 148 ARG D C      1 
ATOM   7369  O  O      . ARG C 2 149 ? 24.907  27.363  25.753  1.00 25.18  ? 148 ARG D O      1 
ATOM   7370  C  CB     . ARG C 2 149 ? 22.196  27.850  23.975  1.00 28.17  ? 148 ARG D CB     1 
ATOM   7371  C  CG     . ARG C 2 149 ? 21.905  28.424  25.312  1.00 29.39  ? 148 ARG D CG     1 
ATOM   7372  C  CD     . ARG C 2 149 ? 20.489  28.955  25.317  1.00 29.54  ? 148 ARG D CD     1 
ATOM   7373  N  NE     . ARG C 2 149 ? 20.056  29.260  26.666  1.00 38.43  ? 148 ARG D NE     1 
ATOM   7374  C  CZ     . ARG C 2 149 ? 19.721  28.343  27.556  1.00 35.21  ? 148 ARG D CZ     1 
ATOM   7375  N  NH1    . ARG C 2 149 ? 19.668  27.061  27.239  1.00 36.87  ? 148 ARG D NH1    1 
ATOM   7376  N  NH2    . ARG C 2 149 ? 19.444  28.721  28.797  1.00 41.00  ? 148 ARG D NH2    1 
ATOM   7377  H  H      . ARG C 2 149 ? 23.081  26.840  21.986  1.00 29.52  ? 148 ARG D H      1 
ATOM   7378  H  HA     . ARG C 2 149 ? 24.149  28.435  23.687  1.00 32.30  ? 148 ARG D HA     1 
ATOM   7379  H  HB2    . ARG C 2 149 ? 21.869  28.476  23.309  1.00 33.84  ? 148 ARG D HB2    1 
ATOM   7380  H  HB3    . ARG C 2 149 ? 21.716  27.010  23.905  1.00 33.84  ? 148 ARG D HB3    1 
ATOM   7381  H  HG2    . ARG C 2 149 ? 21.987  27.738  25.992  1.00 35.30  ? 148 ARG D HG2    1 
ATOM   7382  H  HG3    . ARG C 2 149 ? 22.517  29.153  25.500  1.00 35.30  ? 148 ARG D HG3    1 
ATOM   7383  H  HD2    . ARG C 2 149 ? 20.447  29.768  24.790  1.00 35.48  ? 148 ARG D HD2    1 
ATOM   7384  H  HD3    . ARG C 2 149 ? 19.892  28.287  24.946  1.00 35.48  ? 148 ARG D HD3    1 
ATOM   7385  H  HE     . ARG C 2 149 ? 20.015  30.086  26.900  1.00 46.15  ? 148 ARG D HE     1 
ATOM   7386  H  HH11   . ARG C 2 149 ? 19.853  26.809  26.438  1.00 44.28  ? 148 ARG D HH11   1 
ATOM   7387  H  HH12   . ARG C 2 149 ? 19.447  26.480  27.833  1.00 44.28  ? 148 ARG D HH12   1 
ATOM   7388  H  HH21   . ARG C 2 149 ? 19.483  29.553  29.012  1.00 49.23  ? 148 ARG D HH21   1 
ATOM   7389  H  HH22   . ARG C 2 149 ? 19.225  28.135  29.387  1.00 49.23  ? 148 ARG D HH22   1 
ATOM   7390  N  N      . ASN C 2 150 ? 24.134  25.451  24.871  1.00 24.15  ? 149 ASN D N      1 
ATOM   7391  C  CA     . ASN C 2 150 ? 24.720  24.677  25.961  1.00 25.13  ? 149 ASN D CA     1 
ATOM   7392  C  C      . ASN C 2 150 ? 26.071  24.057  25.603  1.00 25.70  ? 149 ASN D C      1 
ATOM   7393  O  O      . ASN C 2 150 ? 26.635  23.309  26.408  1.00 27.67  ? 149 ASN D O      1 
ATOM   7394  C  CB     . ASN C 2 150 ? 23.749  23.595  26.491  1.00 26.02  ? 149 ASN D CB     1 
ATOM   7395  C  CG     . ASN C 2 150 ? 23.749  22.329  25.666  1.00 32.00  ? 149 ASN D CG     1 
ATOM   7396  O  OD1    . ASN C 2 150 ? 24.252  22.298  24.548  1.00 24.94  ? 149 ASN D OD1    1 
ATOM   7397  N  ND2    . ASN C 2 150 ? 23.179  21.246  26.240  1.00 26.73  ? 149 ASN D ND2    1 
ATOM   7398  H  H      . ASN C 2 150 ? 23.703  24.995  24.282  1.00 29.01  ? 149 ASN D H      1 
ATOM   7399  H  HA     . ASN C 2 150 ? 24.867  25.293  26.696  1.00 30.18  ? 149 ASN D HA     1 
ATOM   7400  H  HB2    . ASN C 2 150 ? 24.006  23.359  27.396  1.00 31.26  ? 149 ASN D HB2    1 
ATOM   7401  H  HB3    . ASN C 2 150 ? 22.848  23.953  26.485  1.00 31.26  ? 149 ASN D HB3    1 
ATOM   7402  H  HD21   . ASN C 2 150 ? 23.152  20.499  25.815  1.00 32.10  ? 149 ASN D HD21   1 
ATOM   7403  H  HD22   . ASN C 2 150 ? 22.845  21.304  27.030  1.00 32.10  ? 149 ASN D HD22   1 
ATOM   7404  N  N      . GLY C 2 151 ? 26.606  24.379  24.428  1.00 23.55  ? 150 GLY D N      1 
ATOM   7405  C  CA     . GLY C 2 151 ? 27.940  23.999  24.024  1.00 24.34  ? 150 GLY D CA     1 
ATOM   7406  C  C      . GLY C 2 151 ? 28.035  22.732  23.192  1.00 21.89  ? 150 GLY D C      1 
ATOM   7407  O  O      . GLY C 2 151 ? 29.084  22.464  22.614  1.00 22.33  ? 150 GLY D O      1 
ATOM   7408  H  H      . GLY C 2 151 ? 26.192  24.836  23.828  1.00 28.29  ? 150 GLY D H      1 
ATOM   7409  H  HA2    . GLY C 2 151 ? 28.321  24.722  23.502  1.00 29.24  ? 150 GLY D HA2    1 
ATOM   7410  H  HA3    . GLY C 2 151 ? 28.477  23.867  24.821  1.00 29.24  ? 150 GLY D HA3    1 
ATOM   7411  N  N      . LYS C 2 152 ? 26.993  21.914  23.147  1.00 23.16  ? 151 LYS D N      1 
ATOM   7412  C  CA     . LYS C 2 152 ? 27.047  20.764  22.249  1.00 26.52  ? 151 LYS D CA     1 
ATOM   7413  C  C      . LYS C 2 152 ? 27.328  21.193  20.815  1.00 22.41  ? 151 LYS D C      1 
ATOM   7414  O  O      . LYS C 2 152 ? 26.685  22.107  20.271  1.00 22.52  ? 151 LYS D O      1 
ATOM   7415  C  CB     . LYS C 2 152 ? 25.735  19.987  22.268  1.00 27.08  ? 151 LYS D CB     1 
ATOM   7416  C  CG     . LYS C 2 152 ? 25.872  18.585  21.705  1.00 34.74  ? 151 LYS D CG     1 
ATOM   7417  C  CD     . LYS C 2 152 ? 26.840  17.697  22.513  1.00 40.72  ? 151 LYS D CD     1 
ATOM   7418  C  CE     . LYS C 2 152 ? 26.643  17.760  24.057  1.00 42.69  ? 151 LYS D CE     1 
ATOM   7419  N  NZ     . LYS C 2 152 ? 27.942  17.588  24.778  1.00 44.76  ? 151 LYS D NZ     1 
ATOM   7420  H  H      . LYS C 2 152 ? 26.271  21.997  23.607  1.00 27.83  ? 151 LYS D H      1 
ATOM   7421  H  HA     . LYS C 2 152 ? 27.762  20.187  22.558  1.00 31.86  ? 151 LYS D HA     1 
ATOM   7422  H  HB2    . LYS C 2 152 ? 25.425  19.913  23.184  1.00 32.53  ? 151 LYS D HB2    1 
ATOM   7423  H  HB3    . LYS C 2 152 ? 25.079  20.461  21.733  1.00 32.53  ? 151 LYS D HB3    1 
ATOM   7424  H  HG2    . LYS C 2 152 ? 25.002  18.157  21.710  1.00 41.72  ? 151 LYS D HG2    1 
ATOM   7425  H  HG3    . LYS C 2 152 ? 26.209  18.642  20.797  1.00 41.72  ? 151 LYS D HG3    1 
ATOM   7426  H  HD2    . LYS C 2 152 ? 26.714  16.775  22.241  1.00 48.90  ? 151 LYS D HD2    1 
ATOM   7427  H  HD3    . LYS C 2 152 ? 27.749  17.978  22.324  1.00 48.90  ? 151 LYS D HD3    1 
ATOM   7428  H  HE2    . LYS C 2 152 ? 26.270  18.622  24.299  1.00 51.26  ? 151 LYS D HE2    1 
ATOM   7429  H  HE3    . LYS C 2 152 ? 26.043  17.049  24.334  1.00 51.26  ? 151 LYS D HE3    1 
ATOM   7430  H  HZ1    . LYS C 2 152 ? 27.810  17.632  25.657  1.00 53.75  ? 151 LYS D HZ1    1 
ATOM   7431  H  HZ2    . LYS C 2 152 ? 28.298  16.798  24.578  1.00 53.75  ? 151 LYS D HZ2    1 
ATOM   7432  H  HZ3    . LYS C 2 152 ? 28.510  18.230  24.538  1.00 53.75  ? 151 LYS D HZ3    1 
ATOM   7433  N  N      . THR C 2 153 ? 28.230  20.472  20.172  1.00 22.98  ? 152 THR D N      1 
ATOM   7434  C  CA     . THR C 2 153 ? 28.614  20.840  18.814  1.00 21.93  ? 152 THR D CA     1 
ATOM   7435  C  C      . THR C 2 153 ? 27.821  20.051  17.777  1.00 27.90  ? 152 THR D C      1 
ATOM   7436  O  O      . THR C 2 153 ? 27.487  18.876  17.968  1.00 27.79  ? 152 THR D O      1 
ATOM   7437  C  CB     . THR C 2 153 ? 30.108  20.648  18.543  1.00 21.85  ? 152 THR D CB     1 
ATOM   7438  O  OG1    . THR C 2 153 ? 30.501  19.274  18.655  1.00 25.72  ? 152 THR D OG1    1 
ATOM   7439  C  CG2    . THR C 2 153 ? 30.964  21.498  19.543  1.00 23.64  ? 152 THR D CG2    1 
ATOM   7440  H  H      . THR C 2 153 ? 28.628  19.780  20.492  1.00 27.61  ? 152 THR D H      1 
ATOM   7441  H  HA     . THR C 2 153 ? 28.413  21.784  18.713  1.00 26.35  ? 152 THR D HA     1 
ATOM   7442  H  HB     . THR C 2 153 ? 30.281  20.942  17.635  1.00 26.26  ? 152 THR D HB     1 
ATOM   7443  H  HG1    . THR C 2 153 ? 30.146  18.823  18.042  1.00 30.89  ? 152 THR D HG1    1 
ATOM   7444  H  HG21   . THR C 2 153 ? 31.908  21.395  19.343  1.00 28.40  ? 152 THR D HG21   1 
ATOM   7445  H  HG22   . THR C 2 153 ? 30.728  22.436  19.469  1.00 28.40  ? 152 THR D HG22   1 
ATOM   7446  H  HG23   . THR C 2 153 ? 30.802  21.204  20.453  1.00 28.40  ? 152 THR D HG23   1 
ATOM   7447  N  N      . SER C 2 154 ? 27.557  20.702  16.649  1.00 25.47  ? 153 SER D N      1 
ATOM   7448  C  CA     . SER C 2 154 ? 26.735  20.084  15.596  1.00 26.27  ? 153 SER D CA     1 
ATOM   7449  C  C      . SER C 2 154 ? 27.566  19.310  14.584  1.00 29.27  ? 153 SER D C      1 
ATOM   7450  O  O      . SER C 2 154 ? 27.021  18.522  13.794  1.00 29.15  ? 153 SER D O      1 
ATOM   7451  C  CB     . SER C 2 154 ? 25.897  21.158  14.911  1.00 22.03  ? 153 SER D CB     1 
ATOM   7452  O  OG     . SER C 2 154 ? 26.687  22.166  14.350  1.00 28.09  ? 153 SER D OG     1 
ATOM   7453  H  H      . SER C 2 154 ? 27.837  21.494  16.465  1.00 30.60  ? 153 SER D H      1 
ATOM   7454  H  HA     . SER C 2 154 ? 26.115  19.449  15.988  1.00 31.56  ? 153 SER D HA     1 
ATOM   7455  H  HB2    . SER C 2 154 ? 25.376  20.743  14.206  1.00 26.47  ? 153 SER D HB2    1 
ATOM   7456  H  HB3    . SER C 2 154 ? 25.306  21.557  15.569  1.00 26.47  ? 153 SER D HB3    1 
ATOM   7457  H  HG     . SER C 2 154 ? 26.199  22.758  14.009  1.00 33.74  ? 153 SER D HG     1 
ATOM   7458  N  N      . LYS C 2 155 ? 28.867  19.498  14.587  1.00 25.34  ? 154 LYS D N      1 
ATOM   7459  C  CA     . LYS C 2 155 ? 29.797  18.767  13.753  1.00 25.56  ? 154 LYS D CA     1 
ATOM   7460  C  C      . LYS C 2 155 ? 31.000  18.481  14.634  1.00 29.02  ? 154 LYS D C      1 
ATOM   7461  O  O      . LYS C 2 155 ? 31.181  19.124  15.668  1.00 27.73  ? 154 LYS D O      1 
ATOM   7462  C  CB     . LYS C 2 155 ? 30.191  19.555  12.511  1.00 27.10  ? 154 LYS D CB     1 
ATOM   7463  C  CG     . LYS C 2 155 ? 29.083  19.671  11.445  1.00 26.20  ? 154 LYS D CG     1 
ATOM   7464  C  CD     . LYS C 2 155 ? 29.592  20.358  10.184  1.00 30.50  ? 154 LYS D CD     1 
ATOM   7465  C  CE     . LYS C 2 155 ? 28.433  20.737  9.268   1.00 37.47  ? 154 LYS D CE     1 
ATOM   7466  N  NZ     . LYS C 2 155 ? 28.150  19.670  8.283   1.00 47.96  ? 154 LYS D NZ     1 
ATOM   7467  H  H      . LYS C 2 155 ? 29.259  20.074  15.091  1.00 30.44  ? 154 LYS D H      1 
ATOM   7468  H  HA     . LYS C 2 155 ? 29.417  17.934  13.431  1.00 30.71  ? 154 LYS D HA     1 
ATOM   7469  H  HB2    . LYS C 2 155 ? 30.433  20.455  12.781  1.00 32.56  ? 154 LYS D HB2    1 
ATOM   7470  H  HB3    . LYS C 2 155 ? 30.951  19.117  12.096  1.00 32.56  ? 154 LYS D HB3    1 
ATOM   7471  H  HG2    . LYS C 2 155 ? 28.774  18.783  11.205  1.00 31.48  ? 154 LYS D HG2    1 
ATOM   7472  H  HG3    . LYS C 2 155 ? 28.347  20.193  11.801  1.00 31.48  ? 154 LYS D HG3    1 
ATOM   7473  H  HD2    . LYS C 2 155 ? 30.070  21.166  10.427  1.00 36.64  ? 154 LYS D HD2    1 
ATOM   7474  H  HD3    . LYS C 2 155 ? 30.181  19.756  9.703   1.00 36.64  ? 154 LYS D HD3    1 
ATOM   7475  H  HE2    . LYS C 2 155 ? 27.635  20.880  9.801   1.00 45.00  ? 154 LYS D HE2    1 
ATOM   7476  H  HE3    . LYS C 2 155 ? 28.657  21.547  8.784   1.00 45.00  ? 154 LYS D HE3    1 
ATOM   7477  H  HZ1    . LYS C 2 155 ? 27.475  19.914  7.757   1.00 57.59  ? 154 LYS D HZ1    1 
ATOM   7478  H  HZ2    . LYS C 2 155 ? 28.869  19.521  7.781   1.00 57.59  ? 154 LYS D HZ2    1 
ATOM   7479  H  HZ3    . LYS C 2 155 ? 27.930  18.918  8.705   1.00 57.59  ? 154 LYS D HZ3    1 
ATOM   7480  N  N      . LYS C 2 156 ? 31.812  17.515  14.252  1.00 29.50  ? 155 LYS D N      1 
ATOM   7481  C  CA     . LYS C 2 156 ? 32.954  17.143  15.068  1.00 28.84  ? 155 LYS D CA     1 
ATOM   7482  C  C      . LYS C 2 156 ? 34.129  18.040  14.684  1.00 29.83  ? 155 LYS D C      1 
ATOM   7483  O  O      . LYS C 2 156 ? 34.610  18.023  13.540  1.00 29.92  ? 155 LYS D O      1 
ATOM   7484  C  CB     . LYS C 2 156 ? 33.287  15.655  14.934  1.00 30.35  ? 155 LYS D CB     1 
ATOM   7485  C  CG     . LYS C 2 156 ? 34.029  15.101  16.155  1.00 39.70  ? 155 LYS D CG     1 
ATOM   7486  C  CD     . LYS C 2 156 ? 34.426  13.622  16.021  1.00 45.24  ? 155 LYS D CD     1 
ATOM   7487  C  CE     . LYS C 2 156 ? 35.580  13.451  15.045  1.00 45.41  ? 155 LYS D CE     1 
ATOM   7488  N  NZ     . LYS C 2 156 ? 36.462  12.251  15.290  1.00 47.88  ? 155 LYS D NZ     1 
ATOM   7489  H  H      . LYS C 2 156 ? 31.725  17.061  13.526  1.00 35.44  ? 155 LYS D H      1 
ATOM   7490  H  HA     . LYS C 2 156 ? 32.753  17.288  16.006  1.00 34.65  ? 155 LYS D HA     1 
ATOM   7491  H  HB2    . LYS C 2 156 ? 32.462  15.155  14.832  1.00 36.45  ? 155 LYS D HB2    1 
ATOM   7492  H  HB3    . LYS C 2 156 ? 33.851  15.527  14.156  1.00 36.45  ? 155 LYS D HB3    1 
ATOM   7493  H  HG2    . LYS C 2 156 ? 34.842  15.613  16.286  1.00 47.68  ? 155 LYS D HG2    1 
ATOM   7494  H  HG3    . LYS C 2 156 ? 33.456  15.183  16.933  1.00 47.68  ? 155 LYS D HG3    1 
ATOM   7495  H  HD2    . LYS C 2 156 ? 34.703  13.282  16.886  1.00 54.32  ? 155 LYS D HD2    1 
ATOM   7496  H  HD3    . LYS C 2 156 ? 33.668  13.113  15.691  1.00 54.32  ? 155 LYS D HD3    1 
ATOM   7497  H  HE2    . LYS C 2 156 ? 35.215  13.364  14.151  1.00 54.53  ? 155 LYS D HE2    1 
ATOM   7498  H  HE3    . LYS C 2 156 ? 36.144  14.239  15.098  1.00 54.53  ? 155 LYS D HE3    1 
ATOM   7499  H  HZ1    . LYS C 2 156 ? 37.111  12.221  14.681  1.00 57.49  ? 155 LYS D HZ1    1 
ATOM   7500  H  HZ2    . LYS C 2 156 ? 36.827  12.301  16.100  1.00 57.49  ? 155 LYS D HZ2    1 
ATOM   7501  H  HZ3    . LYS C 2 156 ? 35.982  11.504  15.235  1.00 57.49  ? 155 LYS D HZ3    1 
ATOM   7502  N  N      . ILE C 2 157 ? 34.596  18.815  15.657  1.00 28.57  ? 156 ILE D N      1 
ATOM   7503  C  CA     . ILE C 2 157 ? 35.649  19.809  15.464  1.00 23.84  ? 156 ILE D CA     1 
ATOM   7504  C  C      . ILE C 2 157 ? 36.906  19.223  16.081  1.00 26.96  ? 156 ILE D C      1 
ATOM   7505  O  O      . ILE C 2 157 ? 36.925  18.945  17.282  1.00 28.16  ? 156 ILE D O      1 
ATOM   7506  C  CB     . ILE C 2 157 ? 35.268  21.133  16.139  1.00 26.17  ? 156 ILE D CB     1 
ATOM   7507  C  CG1    . ILE C 2 157 ? 33.822  21.511  15.843  1.00 28.17  ? 156 ILE D CG1    1 
ATOM   7508  C  CG2    . ILE C 2 157 ? 36.212  22.218  15.728  1.00 26.58  ? 156 ILE D CG2    1 
ATOM   7509  C  CD1    . ILE C 2 157 ? 33.496  21.501  14.335  1.00 29.44  ? 156 ILE D CD1    1 
ATOM   7510  H  H      . ILE C 2 157 ? 34.310  18.782  16.467  1.00 34.32  ? 156 ILE D H      1 
ATOM   7511  H  HA     . ILE C 2 157 ? 35.801  19.979  14.521  1.00 28.65  ? 156 ILE D HA     1 
ATOM   7512  H  HB     . ILE C 2 157 ? 35.341  21.012  17.098  1.00 31.43  ? 156 ILE D HB     1 
ATOM   7513  H  HG12   . ILE C 2 157 ? 33.234  20.876  16.281  1.00 33.84  ? 156 ILE D HG12   1 
ATOM   7514  H  HG13   . ILE C 2 157 ? 33.655  22.405  16.180  1.00 33.84  ? 156 ILE D HG13   1 
ATOM   7515  H  HG21   . ILE C 2 157 ? 35.878  23.067  16.057  1.00 31.93  ? 156 ILE D HG21   1 
ATOM   7516  H  HG22   . ILE C 2 157 ? 37.086  22.036  16.108  1.00 31.93  ? 156 ILE D HG22   1 
ATOM   7517  H  HG23   . ILE C 2 157 ? 36.269  22.237  14.760  1.00 31.93  ? 156 ILE D HG23   1 
ATOM   7518  H  HD11   . ILE C 2 157 ? 32.604  21.858  14.203  1.00 35.36  ? 156 ILE D HD11   1 
ATOM   7519  H  HD12   . ILE C 2 157 ? 34.145  22.051  13.868  1.00 35.36  ? 156 ILE D HD12   1 
ATOM   7520  H  HD13   . ILE C 2 157 ? 33.539  20.589  14.009  1.00 35.36  ? 156 ILE D HD13   1 
ATOM   7521  N  N      . THR C 2 158 ? 37.960  19.046  15.293  1.00 28.38  ? 157 THR D N      1 
ATOM   7522  C  CA     . THR C 2 158 ? 39.145  18.370  15.787  1.00 26.41  ? 157 THR D CA     1 
ATOM   7523  C  C      . THR C 2 158 ? 40.409  19.177  15.531  1.00 25.69  ? 157 THR D C      1 
ATOM   7524  O  O      . THR C 2 158 ? 40.464  20.059  14.670  1.00 25.83  ? 157 THR D O      1 
ATOM   7525  C  CB     . THR C 2 158 ? 39.313  16.971  15.145  1.00 30.80  ? 157 THR D CB     1 
ATOM   7526  O  OG1    . THR C 2 158 ? 39.295  17.101  13.721  1.00 30.38  ? 157 THR D OG1    1 
ATOM   7527  C  CG2    . THR C 2 158 ? 38.200  16.028  15.585  1.00 30.53  ? 157 THR D CG2    1 
ATOM   7528  H  H      . THR C 2 158 ? 38.009  19.308  14.475  1.00 34.09  ? 157 THR D H      1 
ATOM   7529  H  HA     . THR C 2 158 ? 39.046  18.283  16.748  1.00 31.73  ? 157 THR D HA     1 
ATOM   7530  H  HB     . THR C 2 158 ? 40.156  16.585  15.429  1.00 36.99  ? 157 THR D HB     1 
ATOM   7531  H  HG1    . THR C 2 158 ? 38.556  17.411  13.470  1.00 36.49  ? 157 THR D HG1    1 
ATOM   7532  H  HG21   . THR C 2 158 ? 38.328  15.154  15.184  1.00 36.67  ? 157 THR D HG21   1 
ATOM   7533  H  HG22   . THR C 2 158 ? 38.207  15.935  16.551  1.00 36.67  ? 157 THR D HG22   1 
ATOM   7534  H  HG23   . THR C 2 158 ? 37.339  16.379  15.309  1.00 36.67  ? 157 THR D HG23   1 
ATOM   7535  N  N      . ILE C 2 159 ? 41.420  18.854  16.329  1.00 26.42  ? 158 ILE D N      1 
ATOM   7536  C  CA     . ILE C 2 159 ? 42.799  19.299  16.112  1.00 28.22  ? 158 ILE D CA     1 
ATOM   7537  C  C      . ILE C 2 159 ? 43.427  18.201  15.253  1.00 32.88  ? 158 ILE D C      1 
ATOM   7538  O  O      . ILE C 2 159 ? 43.893  17.172  15.746  1.00 31.12  ? 158 ILE D O      1 
ATOM   7539  C  CB     . ILE C 2 159 ? 43.535  19.505  17.436  1.00 31.57  ? 158 ILE D CB     1 
ATOM   7540  C  CG1    . ILE C 2 159 ? 42.833  20.601  18.252  1.00 30.86  ? 158 ILE D CG1    1 
ATOM   7541  C  CG2    . ILE C 2 159 ? 44.987  19.827  17.221  1.00 28.11  ? 158 ILE D CG2    1 
ATOM   7542  C  CD1    . ILE C 2 159 ? 43.319  20.695  19.718  1.00 27.48  ? 158 ILE D CD1    1 
ATOM   7543  H  H      . ILE C 2 159 ? 41.334  18.360  17.029  1.00 31.73  ? 158 ILE D H      1 
ATOM   7544  H  HA     . ILE C 2 159 ? 42.818  20.138  15.626  1.00 33.89  ? 158 ILE D HA     1 
ATOM   7545  H  HB     . ILE C 2 159 ? 43.503  18.674  17.935  1.00 37.91  ? 158 ILE D HB     1 
ATOM   7546  H  HG12   . ILE C 2 159 ? 42.998  21.458  17.829  1.00 37.07  ? 158 ILE D HG12   1 
ATOM   7547  H  HG13   . ILE C 2 159 ? 41.880  20.417  18.267  1.00 37.07  ? 158 ILE D HG13   1 
ATOM   7548  H  HG21   . ILE C 2 159 ? 45.398  20.020  18.078  1.00 33.77  ? 158 ILE D HG21   1 
ATOM   7549  H  HG22   . ILE C 2 159 ? 45.423  19.064  16.810  1.00 33.77  ? 158 ILE D HG22   1 
ATOM   7550  H  HG23   . ILE C 2 159 ? 45.056  20.601  16.639  1.00 33.77  ? 158 ILE D HG23   1 
ATOM   7551  H  HD11   . ILE C 2 159 ? 42.741  21.305  20.204  1.00 33.01  ? 158 ILE D HD11   1 
ATOM   7552  H  HD12   . ILE C 2 159 ? 43.283  19.814  20.120  1.00 33.01  ? 158 ILE D HD12   1 
ATOM   7553  H  HD13   . ILE C 2 159 ? 44.231  21.026  19.728  1.00 33.01  ? 158 ILE D HD13   1 
ATOM   7554  N  N      . ALA C 2 160 ? 43.417  18.407  13.930  1.00 30.84  ? 159 ALA D N      1 
ATOM   7555  C  CA     . ALA C 2 160 ? 43.967  17.392  13.029  1.00 34.00  ? 159 ALA D CA     1 
ATOM   7556  C  C      . ALA C 2 160 ? 45.486  17.324  13.125  1.00 35.50  ? 159 ALA D C      1 
ATOM   7557  O  O      . ALA C 2 160 ? 46.076  16.233  13.019  1.00 32.94  ? 159 ALA D O      1 
ATOM   7558  C  CB     . ALA C 2 160 ? 43.517  17.681  11.591  1.00 36.02  ? 159 ALA D CB     1 
ATOM   7559  H  H      . ALA C 2 160 ? 43.106  19.107  13.540  1.00 37.04  ? 159 ALA D H      1 
ATOM   7560  H  HA     . ALA C 2 160 ? 43.621  16.521  13.277  1.00 40.83  ? 159 ALA D HA     1 
ATOM   7561  H  HB1    . ALA C 2 160 ? 43.887  17.004  11.003  1.00 43.26  ? 159 ALA D HB1    1 
ATOM   7562  H  HB2    . ALA C 2 160 ? 42.548  17.659  11.553  1.00 43.26  ? 159 ALA D HB2    1 
ATOM   7563  H  HB3    . ALA C 2 160 ? 43.839  18.558  11.330  1.00 43.26  ? 159 ALA D HB3    1 
ATOM   7564  N  N      . ASP C 2 161 ? 46.133  18.467  13.346  1.00 31.99  ? 160 ASP D N      1 
ATOM   7565  C  CA     . ASP C 2 161 ? 47.570  18.557  13.535  1.00 30.73  ? 160 ASP D CA     1 
ATOM   7566  C  C      . ASP C 2 161 ? 47.823  19.701  14.513  1.00 32.62  ? 160 ASP D C      1 
ATOM   7567  O  O      . ASP C 2 161 ? 46.965  20.562  14.742  1.00 28.26  ? 160 ASP D O      1 
ATOM   7568  C  CB     . ASP C 2 161 ? 48.311  18.805  12.210  1.00 34.33  ? 160 ASP D CB     1 
ATOM   7569  C  CG     . ASP C 2 161 ? 49.781  18.364  12.249  1.00 38.67  ? 160 ASP D CG     1 
ATOM   7570  O  OD1    . ASP C 2 161 ? 50.268  17.891  13.313  1.00 36.38  ? 160 ASP D OD1    1 
ATOM   7571  O  OD2    . ASP C 2 161 ? 50.473  18.501  11.200  1.00 43.82  ? 160 ASP D OD2    1 
ATOM   7572  H  H      . ASP C 2 161 ? 45.743  19.232  13.393  1.00 38.42  ? 160 ASP D H      1 
ATOM   7573  H  HA     . ASP C 2 161 ? 47.912  17.729  13.907  1.00 36.92  ? 160 ASP D HA     1 
ATOM   7574  H  HB2    . ASP C 2 161 ? 47.869  18.307  11.505  1.00 41.23  ? 160 ASP D HB2    1 
ATOM   7575  H  HB3    . ASP C 2 161 ? 48.289  19.754  12.011  1.00 41.23  ? 160 ASP D HB3    1 
ATOM   7576  N  N      . CYS C 2 162 ? 49.003  19.695  15.098  1.00 29.86  ? 161 CYS D N      1 
ATOM   7577  C  CA     . CYS C 2 162 ? 49.415  20.785  15.965  1.00 28.33  ? 161 CYS D CA     1 
ATOM   7578  C  C      . CYS C 2 162 ? 50.902  20.593  16.214  1.00 34.82  ? 161 CYS D C      1 
ATOM   7579  O  O      . CYS C 2 162 ? 51.429  19.484  16.118  1.00 33.25  ? 161 CYS D O      1 
ATOM   7580  C  CB     . CYS C 2 162 ? 48.635  20.818  17.280  1.00 32.59  ? 161 CYS D CB     1 
ATOM   7581  S  SG     . CYS C 2 162 ? 48.519  19.238  18.168  1.00 32.52  ? 161 CYS D SG     1 
ATOM   7582  H  H      . CYS C 2 162 ? 49.587  19.070  15.011  1.00 35.86  ? 161 CYS D H      1 
ATOM   7583  H  HA     . CYS C 2 162 ? 49.263  21.638  15.530  1.00 34.03  ? 161 CYS D HA     1 
ATOM   7584  H  HB2    . CYS C 2 162 ? 49.067  21.451  17.874  1.00 39.14  ? 161 CYS D HB2    1 
ATOM   7585  H  HB3    . CYS C 2 162 ? 47.729  21.107  17.088  1.00 39.14  ? 161 CYS D HB3    1 
ATOM   7586  H  HG     . CYS C 2 162 ? 49.626  18.817  18.362  1.00 39.06  ? 161 CYS D HG     1 
ATOM   7587  N  N      . GLY C 2 163 ? 51.566  21.699  16.526  1.00 32.95  ? 162 GLY D N      1 
ATOM   7588  C  CA     . GLY C 2 163 ? 52.983  21.674  16.825  1.00 35.53  ? 162 GLY D CA     1 
ATOM   7589  C  C      . GLY C 2 163 ? 53.443  23.049  17.260  1.00 33.48  ? 162 GLY D C      1 
ATOM   7590  O  O      . GLY C 2 163 ? 52.632  23.946  17.517  1.00 31.19  ? 162 GLY D O      1 
ATOM   7591  H  H      . GLY C 2 163 ? 51.213  22.482  16.572  1.00 39.58  ? 162 GLY D H      1 
ATOM   7592  H  HA2    . GLY C 2 163 ? 53.160  21.042  17.540  1.00 42.67  ? 162 GLY D HA2    1 
ATOM   7593  H  HA3    . GLY C 2 163 ? 53.483  21.408  16.038  1.00 42.67  ? 162 GLY D HA3    1 
ATOM   7594  N  N      . GLN C 2 164 ? 54.758  23.213  17.312  1.00 33.85  ? 163 GLN D N      1 
ATOM   7595  C  CA     . GLN C 2 164 ? 55.374  24.477  17.676  1.00 32.65  ? 163 GLN D CA     1 
ATOM   7596  C  C      . GLN C 2 164 ? 55.872  25.190  16.431  1.00 38.00  ? 163 GLN D C      1 
ATOM   7597  O  O      . GLN C 2 164 ? 56.512  24.569  15.569  1.00 35.87  ? 163 GLN D O      1 
ATOM   7598  C  CB     . GLN C 2 164 ? 56.544  24.264  18.642  1.00 34.51  ? 163 GLN D CB     1 
ATOM   7599  C  CG     . GLN C 2 164 ? 57.206  25.572  19.067  1.00 32.78  ? 163 GLN D CG     1 
ATOM   7600  C  CD     . GLN C 2 164 ? 58.056  25.436  20.310  1.00 36.03  ? 163 GLN D CD     1 
ATOM   7601  O  OE1    . GLN C 2 164 ? 58.261  24.337  20.820  1.00 38.90  ? 163 GLN D OE1    1 
ATOM   7602  N  NE2    . GLN C 2 164 ? 58.553  26.560  20.812  1.00 36.79  ? 163 GLN D NE2    1 
ATOM   7603  H  H      . GLN C 2 164 ? 55.325  22.591  17.137  1.00 40.65  ? 163 GLN D H      1 
ATOM   7604  H  HA     . GLN C 2 164 ? 54.709  25.034  18.109  1.00 39.21  ? 163 GLN D HA     1 
ATOM   7605  H  HB2    . GLN C 2 164 ? 56.217  23.820  19.440  1.00 41.44  ? 163 GLN D HB2    1 
ATOM   7606  H  HB3    . GLN C 2 164 ? 57.216  23.715  18.209  1.00 41.44  ? 163 GLN D HB3    1 
ATOM   7607  H  HG2    . GLN C 2 164 ? 57.777  25.883  18.348  1.00 39.38  ? 163 GLN D HG2    1 
ATOM   7608  H  HG3    . GLN C 2 164 ? 56.515  26.229  19.250  1.00 39.38  ? 163 GLN D HG3    1 
ATOM   7609  H  HE21   . GLN C 2 164 ? 58.384  27.312  20.431  1.00 44.19  ? 163 GLN D HE21   1 
ATOM   7610  H  HE22   . GLN C 2 164 ? 59.043  26.535  21.518  1.00 44.19  ? 163 GLN D HE22   1 
ATOM   7611  N  N      . LEU C 2 165 ? 55.597  26.488  16.346  1.00 35.00  ? 164 LEU D N      1 
ATOM   7612  C  CA     . LEU C 2 165 ? 56.243  27.328  15.340  1.00 36.68  ? 164 LEU D CA     1 
ATOM   7613  C  C      . LEU C 2 165 ? 57.492  28.054  15.866  1.00 39.13  ? 164 LEU D C      1 
ATOM   7614  O  O      . LEU C 2 165 ? 57.501  28.599  16.973  1.00 43.60  ? 164 LEU D O      1 
ATOM   7615  C  CB     . LEU C 2 165 ? 55.245  28.358  14.767  1.00 33.47  ? 164 LEU D CB     1 
ATOM   7616  C  CG     . LEU C 2 165 ? 53.892  27.823  14.356  1.00 36.28  ? 164 LEU D CG     1 
ATOM   7617  C  CD1    . LEU C 2 165 ? 52.965  28.970  13.959  1.00 37.44  ? 164 LEU D CD1    1 
ATOM   7618  C  CD2    . LEU C 2 165 ? 54.064  26.850  13.218  1.00 39.56  ? 164 LEU D CD2    1 
ATOM   7619  H  H      . LEU C 2 165 ? 55.043  26.905  16.855  1.00 42.04  ? 164 LEU D H      1 
ATOM   7620  H  HA     . LEU C 2 165 ? 56.540  26.743  14.626  1.00 44.05  ? 164 LEU D HA     1 
ATOM   7621  H  HB2    . LEU C 2 165 ? 55.090  29.037  15.442  1.00 40.20  ? 164 LEU D HB2    1 
ATOM   7622  H  HB3    . LEU C 2 165 ? 55.644  28.759  13.979  1.00 40.20  ? 164 LEU D HB3    1 
ATOM   7623  H  HG     . LEU C 2 165 ? 53.479  27.358  15.100  1.00 43.56  ? 164 LEU D HG     1 
ATOM   7624  H  HD11   . LEU C 2 165 ? 52.110  28.604  13.682  1.00 44.96  ? 164 LEU D HD11   1 
ATOM   7625  H  HD12   . LEU C 2 165 ? 52.842  29.555  14.722  1.00 44.96  ? 164 LEU D HD12   1 
ATOM   7626  H  HD13   . LEU C 2 165 ? 53.367  29.462  13.226  1.00 44.96  ? 164 LEU D HD13   1 
ATOM   7627  H  HD21   . LEU C 2 165 ? 53.191  26.538  12.934  1.00 47.50  ? 164 LEU D HD21   1 
ATOM   7628  H  HD22   . LEU C 2 165 ? 54.510  27.299  12.482  1.00 47.50  ? 164 LEU D HD22   1 
ATOM   7629  H  HD23   . LEU C 2 165 ? 54.601  26.101  13.521  1.00 47.50  ? 164 LEU D HD23   1 
ATOM   7630  N  N      . GLY D 1 1   ? -4.414  14.265  24.921  1.00 44.05  ? 0   GLY C N      1 
ATOM   7631  C  CA     . GLY D 1 1   ? -2.926  14.148  24.991  1.00 41.47  ? 0   GLY C CA     1 
ATOM   7632  C  C      . GLY D 1 1   ? -2.510  14.071  26.438  1.00 43.82  ? 0   GLY C C      1 
ATOM   7633  O  O      . GLY D 1 1   ? -3.269  14.490  27.316  1.00 42.66  ? 0   GLY C O      1 
ATOM   7634  H  H1     . GLY D 1 1   ? -4.766  13.467  24.745  1.00 52.89  ? 0   GLY C H1     1 
ATOM   7635  H  H2     . GLY D 1 1   ? -4.726  14.562  25.700  1.00 52.89  ? 0   GLY C H2     1 
ATOM   7636  H  H3     . GLY D 1 1   ? -4.637  14.836  24.275  1.00 52.89  ? 0   GLY C H3     1 
ATOM   7637  H  HA2    . GLY D 1 1   ? -2.631  13.348  24.529  1.00 49.80  ? 0   GLY C HA2    1 
ATOM   7638  H  HA3    . GLY D 1 1   ? -2.510  14.922  24.579  1.00 49.80  ? 0   GLY C HA3    1 
ATOM   7639  N  N      . MET D 1 2   ? -1.322  13.539  26.709  1.00 42.27  ? 1   MET C N      1 
ATOM   7640  C  CA     . MET D 1 2   ? -0.924  13.376  28.100  1.00 41.44  ? 1   MET C CA     1 
ATOM   7641  C  C      . MET D 1 2   ? -0.488  14.710  28.686  1.00 39.95  ? 1   MET C C      1 
ATOM   7642  O  O      . MET D 1 2   ? 0.006   15.597  27.984  1.00 45.85  ? 1   MET C O      1 
ATOM   7643  C  CB     . MET D 1 2   ? 0.196   12.343  28.247  1.00 45.22  ? 1   MET C CB     1 
ATOM   7644  C  CG     . MET D 1 2   ? 1.513   12.685  27.615  1.00 42.22  ? 1   MET C CG     1 
ATOM   7645  S  SD     . MET D 1 2   ? 2.644   11.247  27.626  1.00 35.63  ? 1   MET C SD     1 
ATOM   7646  C  CE     . MET D 1 2   ? 1.936   10.284  26.323  1.00 35.58  ? 1   MET C CE     1 
ATOM   7647  H  H      . MET D 1 2   ? -0.749  13.275  26.124  1.00 50.76  ? 1   MET C H      1 
ATOM   7648  H  HA     . MET D 1 2   ? -1.682  13.039  28.603  1.00 49.77  ? 1   MET C HA     1 
ATOM   7649  H  HB2    . MET D 1 2   ? 0.361   12.211  29.194  1.00 54.30  ? 1   MET C HB2    1 
ATOM   7650  H  HB3    . MET D 1 2   ? -0.106  11.513  27.845  1.00 54.30  ? 1   MET C HB3    1 
ATOM   7651  H  HG2    . MET D 1 2   ? 1.368   12.955  26.695  1.00 50.70  ? 1   MET C HG2    1 
ATOM   7652  H  HG3    . MET D 1 2   ? 1.930   13.408  28.110  1.00 50.70  ? 1   MET C HG3    1 
ATOM   7653  H  HE1    . MET D 1 2   ? 2.443   9.463   26.226  1.00 42.72  ? 1   MET C HE1    1 
ATOM   7654  H  HE2    . MET D 1 2   ? 1.014   10.079  26.547  1.00 42.72  ? 1   MET C HE2    1 
ATOM   7655  H  HE3    . MET D 1 2   ? 1.971   10.794  25.499  1.00 42.72  ? 1   MET C HE3    1 
ATOM   7656  N  N      . THR D 1 3   ? -0.703  14.855  29.981  1.00 40.64  ? 2   THR C N      1 
ATOM   7657  C  CA     . THR D 1 3   ? -0.284  16.066  30.657  1.00 45.24  ? 2   THR C CA     1 
ATOM   7658  C  C      . THR D 1 3   ? 1.234   16.086  30.748  1.00 45.43  ? 2   THR C C      1 
ATOM   7659  O  O      . THR D 1 3   ? 1.872   15.041  30.918  1.00 39.47  ? 2   THR C O      1 
ATOM   7660  C  CB     . THR D 1 3   ? -0.922  16.150  32.036  1.00 47.53  ? 2   THR C CB     1 
ATOM   7661  O  OG1    . THR D 1 3   ? -2.341  16.266  31.879  1.00 50.64  ? 2   THR C OG1    1 
ATOM   7662  C  CG2    . THR D 1 3   ? -0.398  17.355  32.778  1.00 49.20  ? 2   THR C CG2    1 
ATOM   7663  H  H      . THR D 1 3   ? -1.086  14.274  30.486  1.00 48.80  ? 2   THR C H      1 
ATOM   7664  H  HA     . THR D 1 3   ? -0.572  16.851  30.165  1.00 54.32  ? 2   THR C HA     1 
ATOM   7665  H  HB     . THR D 1 3   ? -0.711  15.358  32.554  1.00 57.07  ? 2   THR C HB     1 
ATOM   7666  H  HG1    . THR D 1 3   ? -2.638  15.606  31.453  1.00 60.80  ? 2   THR C HG1    1 
ATOM   7667  H  HG21   . THR D 1 3   ? -0.930  17.512  33.573  1.00 59.07  ? 2   THR C HG21   1 
ATOM   7668  H  HG22   . THR D 1 3   ? 0.525   17.209  33.039  1.00 59.07  ? 2   THR C HG22   1 
ATOM   7669  H  HG23   . THR D 1 3   ? -0.443  18.140  32.209  1.00 59.07  ? 2   THR C HG23   1 
ATOM   7670  N  N      . GLU D 1 4   ? 1.801   17.278  30.582  1.00 40.11  ? 3   GLU C N      1 
ATOM   7671  C  CA     . GLU D 1 4   ? 3.233   17.526  30.667  1.00 42.77  ? 3   GLU C CA     1 
ATOM   7672  C  C      . GLU D 1 4   ? 3.535   18.219  31.983  1.00 40.67  ? 3   GLU C C      1 
ATOM   7673  O  O      . GLU D 1 4   ? 2.733   19.031  32.459  1.00 47.61  ? 3   GLU C O      1 
ATOM   7674  C  CB     . GLU D 1 4   ? 3.722   18.402  29.496  1.00 45.20  ? 3   GLU C CB     1 
ATOM   7675  C  CG     . GLU D 1 4   ? 3.206   17.968  28.114  1.00 43.71  ? 3   GLU C CG     1 
ATOM   7676  C  CD     . GLU D 1 4   ? 4.058   18.462  26.952  1.00 47.53  ? 3   GLU C CD     1 
ATOM   7677  O  OE1    . GLU D 1 4   ? 5.026   19.231  27.182  1.00 49.25  ? 3   GLU C OE1    1 
ATOM   7678  O  OE2    . GLU D 1 4   ? 3.759   18.074  25.798  1.00 41.91  ? 3   GLU C OE2    1 
ATOM   7679  H  H      . GLU D 1 4   ? 1.352   17.992  30.410  1.00 48.17  ? 3   GLU C H      1 
ATOM   7680  H  HA     . GLU D 1 4   ? 3.714   16.684  30.631  1.00 51.35  ? 3   GLU C HA     1 
ATOM   7681  H  HB2    . GLU D 1 4   ? 3.426   19.313  29.647  1.00 54.27  ? 3   GLU C HB2    1 
ATOM   7682  H  HB3    . GLU D 1 4   ? 4.692   18.368  29.470  1.00 54.27  ? 3   GLU C HB3    1 
ATOM   7683  H  HG2    . GLU D 1 4   ? 3.190   16.999  28.077  1.00 52.48  ? 3   GLU C HG2    1 
ATOM   7684  H  HG3    . GLU D 1 4   ? 2.310   18.319  27.992  1.00 52.48  ? 3   GLU C HG3    1 
ATOM   7685  N  N      . TYR D 1 5   ? 4.676   17.883  32.584  1.00 37.19  ? 4   TYR C N      1 
ATOM   7686  C  CA     . TYR D 1 5   ? 5.133   18.501  33.824  1.00 42.17  ? 4   TYR C CA     1 
ATOM   7687  C  C      . TYR D 1 5   ? 6.582   18.949  33.664  1.00 40.97  ? 4   TYR C C      1 
ATOM   7688  O  O      . TYR D 1 5   ? 7.334   18.363  32.894  1.00 38.35  ? 4   TYR C O      1 
ATOM   7689  C  CB     . TYR D 1 5   ? 5.034   17.549  34.990  1.00 44.88  ? 4   TYR C CB     1 
ATOM   7690  C  CG     . TYR D 1 5   ? 3.628   17.016  35.244  1.00 51.25  ? 4   TYR C CG     1 
ATOM   7691  C  CD1    . TYR D 1 5   ? 2.549   17.888  35.390  1.00 51.69  ? 4   TYR C CD1    1 
ATOM   7692  C  CD2    . TYR D 1 5   ? 3.391   15.646  35.347  1.00 50.09  ? 4   TYR C CD2    1 
ATOM   7693  C  CE1    . TYR D 1 5   ? 1.270   17.418  35.624  1.00 54.66  ? 4   TYR C CE1    1 
ATOM   7694  C  CE2    . TYR D 1 5   ? 2.108   15.157  35.572  1.00 50.03  ? 4   TYR C CE2    1 
ATOM   7695  C  CZ     . TYR D 1 5   ? 1.050   16.051  35.709  1.00 55.42  ? 4   TYR C CZ     1 
ATOM   7696  O  OH     . TYR D 1 5   ? -0.234  15.600  35.940  1.00 53.33  ? 4   TYR C OH     1 
ATOM   7697  H  H      . TYR D 1 5   ? 5.215   17.284  32.283  1.00 44.67  ? 4   TYR C H      1 
ATOM   7698  H  HA     . TYR D 1 5   ? 4.586   19.278  34.016  1.00 50.64  ? 4   TYR C HA     1 
ATOM   7699  H  HB2    . TYR D 1 5   ? 5.610   16.788  34.820  1.00 53.89  ? 4   TYR C HB2    1 
ATOM   7700  H  HB3    . TYR D 1 5   ? 5.322   18.010  35.793  1.00 53.89  ? 4   TYR C HB3    1 
ATOM   7701  H  HD1    . TYR D 1 5   ? 2.693   18.805  35.329  1.00 62.06  ? 4   TYR C HD1    1 
ATOM   7702  H  HD2    . TYR D 1 5   ? 4.101   15.051  35.264  1.00 60.14  ? 4   TYR C HD2    1 
ATOM   7703  H  HE1    . TYR D 1 5   ? 0.563   18.013  35.723  1.00 65.62  ? 4   TYR C HE1    1 
ATOM   7704  H  HE2    . TYR D 1 5   ? 1.958   14.241  35.630  1.00 60.07  ? 4   TYR C HE2    1 
ATOM   7705  H  HH     . TYR D 1 5   ? -0.251  14.760  35.929  1.00 64.03  ? 4   TYR C HH     1 
ATOM   7706  N  N      . LYS D 1 6   ? 6.977   19.977  34.427  1.00 48.26  ? 5   LYS C N      1 
ATOM   7707  C  CA     . LYS D 1 6   ? 8.278   20.640  34.265  1.00 38.51  ? 5   LYS C CA     1 
ATOM   7708  C  C      . LYS D 1 6   ? 9.037   20.599  35.573  1.00 40.01  ? 5   LYS C C      1 
ATOM   7709  O  O      . LYS D 1 6   ? 8.763   21.375  36.499  1.00 44.04  ? 5   LYS C O      1 
ATOM   7710  C  CB     . LYS D 1 6   ? 8.102   22.077  33.825  1.00 44.80  ? 5   LYS C CB     1 
ATOM   7711  C  CG     . LYS D 1 6   ? 7.418   22.262  32.545  1.00 42.77  ? 5   LYS C CG     1 
ATOM   7712  C  CD     . LYS D 1 6   ? 7.124   23.733  32.349  1.00 50.83  ? 5   LYS C CD     1 
ATOM   7713  C  CE     . LYS D 1 6   ? 6.103   23.934  31.248  1.00 55.05  ? 5   LYS C CE     1 
ATOM   7714  N  NZ     . LYS D 1 6   ? 6.642   23.388  29.991  1.00 56.93  ? 5   LYS C NZ     1 
ATOM   7715  H  H      . LYS D 1 6   ? 6.499   20.314  35.058  1.00 57.95  ? 5   LYS C H      1 
ATOM   7716  H  HA     . LYS D 1 6   ? 8.780   20.144  33.600  1.00 46.24  ? 5   LYS C HA     1 
ATOM   7717  H  HB2    . LYS D 1 6   ? 7.583   22.542  34.500  1.00 53.80  ? 5   LYS C HB2    1 
ATOM   7718  H  HB3    . LYS D 1 6   ? 8.980   22.482  33.745  1.00 53.80  ? 5   LYS C HB3    1 
ATOM   7719  H  HG2    . LYS D 1 6   ? 7.985   21.954  31.821  1.00 51.35  ? 5   LYS C HG2    1 
ATOM   7720  H  HG3    . LYS D 1 6   ? 6.582   21.770  32.544  1.00 51.35  ? 5   LYS C HG3    1 
ATOM   7721  H  HD2    . LYS D 1 6   ? 6.768   24.105  33.171  1.00 61.03  ? 5   LYS C HD2    1 
ATOM   7722  H  HD3    . LYS D 1 6   ? 7.940   24.196  32.101  1.00 61.03  ? 5   LYS C HD3    1 
ATOM   7723  H  HE2    . LYS D 1 6   ? 5.282   23.467  31.469  1.00 66.09  ? 5   LYS C HE2    1 
ATOM   7724  H  HE3    . LYS D 1 6   ? 5.925   24.881  31.131  1.00 66.09  ? 5   LYS C HE3    1 
ATOM   7725  H  HZ1    . LYS D 1 6   ? 6.743   22.507  30.061  1.00 68.35  ? 5   LYS C HZ1    1 
ATOM   7726  H  HZ2    . LYS D 1 6   ? 6.084   23.562  29.320  1.00 68.35  ? 5   LYS C HZ2    1 
ATOM   7727  H  HZ3    . LYS D 1 6   ? 7.432   23.757  29.813  1.00 68.35  ? 5   LYS C HZ3    1 
ATOM   7728  N  N      . LEU D 1 7   ? 9.989   19.696  35.648  1.00 38.04  ? 6   LEU C N      1 
ATOM   7729  C  CA     . LEU D 1 7   ? 10.783  19.445  36.837  1.00 38.79  ? 6   LEU C CA     1 
ATOM   7730  C  C      . LEU D 1 7   ? 12.150  20.106  36.651  1.00 37.98  ? 6   LEU C C      1 
ATOM   7731  O  O      . LEU D 1 7   ? 12.617  20.254  35.519  1.00 36.67  ? 6   LEU C O      1 
ATOM   7732  C  CB     . LEU D 1 7   ? 10.940  17.940  37.037  1.00 38.69  ? 6   LEU C CB     1 
ATOM   7733  C  CG     . LEU D 1 7   ? 9.693   17.051  36.849  1.00 41.36  ? 6   LEU C CG     1 
ATOM   7734  C  CD1    . LEU D 1 7   ? 9.975   15.690  37.484  1.00 42.47  ? 6   LEU C CD1    1 
ATOM   7735  C  CD2    . LEU D 1 7   ? 8.435   17.633  37.469  1.00 44.92  ? 6   LEU C CD2    1 
ATOM   7736  H  H      . LEU D 1 7   ? 10.208  19.187  34.991  1.00 45.69  ? 6   LEU C H      1 
ATOM   7737  H  HA     . LEU D 1 7   ? 10.366  19.811  37.632  1.00 46.59  ? 6   LEU C HA     1 
ATOM   7738  H  HB2    . LEU D 1 7   ? 11.604  17.626  36.404  1.00 46.46  ? 6   LEU C HB2    1 
ATOM   7739  H  HB3    . LEU D 1 7   ? 11.252  17.795  37.944  1.00 46.46  ? 6   LEU C HB3    1 
ATOM   7740  H  HG     . LEU D 1 7   ? 9.519   16.977  35.898  1.00 49.67  ? 6   LEU C HG     1 
ATOM   7741  H  HD11   . LEU D 1 7   ? 9.191   15.127  37.385  1.00 51.00  ? 6   LEU C HD11   1 
ATOM   7742  H  HD12   . LEU D 1 7   ? 10.733  15.284  37.036  1.00 51.00  ? 6   LEU C HD12   1 
ATOM   7743  H  HD13   . LEU D 1 7   ? 10.175  15.815  38.425  1.00 51.00  ? 6   LEU C HD13   1 
ATOM   7744  H  HD21   . LEU D 1 7   ? 7.731   16.966  37.440  1.00 53.94  ? 6   LEU C HD21   1 
ATOM   7745  H  HD22   . LEU D 1 7   ? 8.620   17.878  38.389  1.00 53.94  ? 6   LEU C HD22   1 
ATOM   7746  H  HD23   . LEU D 1 7   ? 8.168   18.418  36.965  1.00 53.94  ? 6   LEU C HD23   1 
ATOM   7747  N  N      . VAL D 1 8   ? 12.801  20.468  37.762  1.00 39.05  ? 7   VAL C N      1 
ATOM   7748  C  CA     . VAL D 1 8   ? 14.089  21.174  37.733  1.00 37.39  ? 7   VAL C CA     1 
ATOM   7749  C  C      . VAL D 1 8   ? 14.981  20.676  38.874  1.00 38.44  ? 7   VAL C C      1 
ATOM   7750  O  O      . VAL D 1 8   ? 14.622  20.805  40.045  1.00 36.83  ? 7   VAL C O      1 
ATOM   7751  C  CB     . VAL D 1 8   ? 13.888  22.691  37.841  1.00 39.11  ? 7   VAL C CB     1 
ATOM   7752  C  CG1    . VAL D 1 8   ? 15.245  23.425  37.852  1.00 37.92  ? 7   VAL C CG1    1 
ATOM   7753  C  CG2    . VAL D 1 8   ? 12.969  23.192  36.743  1.00 34.85  ? 7   VAL C CG2    1 
ATOM   7754  H  H      . VAL D 1 8   ? 12.512  20.314  38.557  1.00 46.89  ? 7   VAL C H      1 
ATOM   7755  H  HA     . VAL D 1 8   ? 14.548  20.959  36.906  1.00 44.90  ? 7   VAL C HA     1 
ATOM   7756  H  HB     . VAL D 1 8   ? 13.453  22.894  38.684  1.00 46.97  ? 7   VAL C HB     1 
ATOM   7757  H  HG11   . VAL D 1 8   ? 15.093  24.371  37.701  1.00 45.53  ? 7   VAL C HG11   1 
ATOM   7758  H  HG12   . VAL D 1 8   ? 15.669  23.292  38.714  1.00 45.53  ? 7   VAL C HG12   1 
ATOM   7759  H  HG13   . VAL D 1 8   ? 15.806  23.063  37.148  1.00 45.53  ? 7   VAL C HG13   1 
ATOM   7760  H  HG21   . VAL D 1 8   ? 12.971  24.162  36.747  1.00 41.85  ? 7   VAL C HG21   1 
ATOM   7761  H  HG22   . VAL D 1 8   ? 13.290  22.865  35.888  1.00 41.85  ? 7   VAL C HG22   1 
ATOM   7762  H  HG23   . VAL D 1 8   ? 12.072  22.863  36.907  1.00 41.85  ? 7   VAL C HG23   1 
ATOM   7763  N  N      . VAL D 1 9   ? 16.144  20.126  38.534  1.00 31.90  ? 8   VAL C N      1 
ATOM   7764  C  CA     . VAL D 1 9   ? 17.071  19.554  39.515  1.00 33.40  ? 8   VAL C CA     1 
ATOM   7765  C  C      . VAL D 1 9   ? 18.153  20.587  39.838  1.00 36.40  ? 8   VAL C C      1 
ATOM   7766  O  O      . VAL D 1 9   ? 18.748  21.169  38.927  1.00 33.17  ? 8   VAL C O      1 
ATOM   7767  C  CB     . VAL D 1 9   ? 17.708  18.266  38.964  1.00 35.32  ? 8   VAL C CB     1 
ATOM   7768  C  CG1    . VAL D 1 9   ? 18.507  17.555  40.037  1.00 37.04  ? 8   VAL C CG1    1 
ATOM   7769  C  CG2    . VAL D 1 9   ? 16.645  17.359  38.361  1.00 35.35  ? 8   VAL C CG2    1 
ATOM   7770  H  H      . VAL D 1 9   ? 16.426  20.070  37.724  1.00 38.31  ? 8   VAL C H      1 
ATOM   7771  H  HA     . VAL D 1 9   ? 16.589  19.352  40.333  1.00 40.12  ? 8   VAL C HA     1 
ATOM   7772  H  HB     . VAL D 1 9   ? 18.328  18.501  38.256  1.00 42.42  ? 8   VAL C HB     1 
ATOM   7773  H  HG11   . VAL D 1 9   ? 18.884  16.743  39.664  1.00 44.48  ? 8   VAL C HG11   1 
ATOM   7774  H  HG12   . VAL D 1 9   ? 19.218  18.140  40.342  1.00 44.48  ? 8   VAL C HG12   1 
ATOM   7775  H  HG13   . VAL D 1 9   ? 17.918  17.337  40.777  1.00 44.48  ? 8   VAL C HG13   1 
ATOM   7776  H  HG21   . VAL D 1 9   ? 17.047  16.505  38.140  1.00 42.45  ? 8   VAL C HG21   1 
ATOM   7777  H  HG22   . VAL D 1 9   ? 15.934  17.232  39.009  1.00 42.45  ? 8   VAL C HG22   1 
ATOM   7778  H  HG23   . VAL D 1 9   ? 16.291  17.776  37.560  1.00 42.45  ? 8   VAL C HG23   1 
ATOM   7779  N  N      . VAL D 1 10  ? 18.454  20.763  41.119  1.00 36.83  ? 9   VAL C N      1 
ATOM   7780  C  CA     . VAL D 1 10  ? 19.368  21.797  41.594  1.00 38.79  ? 9   VAL C CA     1 
ATOM   7781  C  C      . VAL D 1 10  ? 20.194  21.253  42.752  1.00 39.65  ? 9   VAL C C      1 
ATOM   7782  O  O      . VAL D 1 10  ? 19.835  20.258  43.381  1.00 33.44  ? 9   VAL C O      1 
ATOM   7783  C  CB     . VAL D 1 10  ? 18.603  23.062  42.053  1.00 37.15  ? 9   VAL C CB     1 
ATOM   7784  C  CG1    . VAL D 1 10  ? 17.671  23.552  40.948  1.00 34.03  ? 9   VAL C CG1    1 
ATOM   7785  C  CG2    . VAL D 1 10  ? 17.789  22.744  43.221  1.00 31.08  ? 9   VAL C CG2    1 
ATOM   7786  H  H      . VAL D 1 10  ? 18.131  20.281  41.754  1.00 44.23  ? 9   VAL C H      1 
ATOM   7787  H  HA     . VAL D 1 10  ? 19.978  22.031  40.877  1.00 46.58  ? 9   VAL C HA     1 
ATOM   7788  H  HB     . VAL D 1 10  ? 19.249  23.754  42.267  1.00 44.61  ? 9   VAL C HB     1 
ATOM   7789  H  HG11   . VAL D 1 10  ? 17.284  24.401  41.215  1.00 40.87  ? 9   VAL C HG11   1 
ATOM   7790  H  HG12   . VAL D 1 10  ? 18.181  23.664  40.131  1.00 40.87  ? 9   VAL C HG12   1 
ATOM   7791  H  HG13   . VAL D 1 10  ? 16.969  22.897  40.813  1.00 40.87  ? 9   VAL C HG13   1 
ATOM   7792  H  HG21   . VAL D 1 10  ? 17.103  23.423  43.322  1.00 37.33  ? 9   VAL C HG21   1 
ATOM   7793  H  HG22   . VAL D 1 10  ? 17.378  21.875  43.093  1.00 37.33  ? 9   VAL C HG22   1 
ATOM   7794  H  HG23   . VAL D 1 10  ? 18.357  22.729  44.007  1.00 37.33  ? 9   VAL C HG23   1 
ATOM   7795  N  N      . GLY D 1 11  ? 21.289  21.943  43.051  1.00 43.36  ? 10  GLY C N      1 
ATOM   7796  C  CA     . GLY D 1 11  ? 22.210  21.575  44.119  1.00 40.24  ? 10  GLY C CA     1 
ATOM   7797  C  C      . GLY D 1 11  ? 23.648  21.866  43.699  1.00 43.31  ? 10  GLY C C      1 
ATOM   7798  O  O      . GLY D 1 11  ? 23.957  22.075  42.529  1.00 45.19  ? 10  GLY C O      1 
ATOM   7799  H  H      . GLY D 1 11  ? 21.529  22.655  42.633  1.00 52.07  ? 10  GLY C H      1 
ATOM   7800  H  HA2    . GLY D 1 11  ? 22.007  22.085  44.919  1.00 48.32  ? 10  GLY C HA2    1 
ATOM   7801  H  HA3    . GLY D 1 11  ? 22.126  20.630  44.317  1.00 48.32  ? 10  GLY C HA3    1 
ATOM   7802  N  N      . ALA D 1 12  ? 24.544  21.875  44.679  1.00 47.03  ? 11  ALA C N      1 
ATOM   7803  C  CA     . ALA D 1 12  ? 25.945  22.168  44.412  1.00 45.37  ? 11  ALA C CA     1 
ATOM   7804  C  C      . ALA D 1 12  ? 26.512  21.182  43.397  1.00 44.47  ? 11  ALA C C      1 
ATOM   7805  O  O      . ALA D 1 12  ? 25.970  20.099  43.164  1.00 41.40  ? 11  ALA C O      1 
ATOM   7806  C  CB     . ALA D 1 12  ? 26.764  22.103  45.699  1.00 46.42  ? 11  ALA C CB     1 
ATOM   7807  H  H      . ALA D 1 12  ? 24.367  21.715  45.505  1.00 56.47  ? 11  ALA C H      1 
ATOM   7808  H  HA     . ALA D 1 12  ? 26.019  23.065  44.050  1.00 54.48  ? 11  ALA C HA     1 
ATOM   7809  H  HB1    . ALA D 1 12  ? 27.693  22.293  45.492  1.00 55.73  ? 11  ALA C HB1    1 
ATOM   7810  H  HB2    . ALA D 1 12  ? 26.423  22.762  46.324  1.00 55.73  ? 11  ALA C HB2    1 
ATOM   7811  H  HB3    . ALA D 1 12  ? 26.685  21.214  46.079  1.00 55.73  ? 11  ALA C HB3    1 
ATOM   7812  N  N      . ASP D 1 13  ? 27.631  21.556  42.801  1.00 45.04  ? 12  ASP C N      1 
ATOM   7813  C  CA     . ASP D 1 13  ? 28.227  20.662  41.815  1.00 47.41  ? 12  ASP C CA     1 
ATOM   7814  C  C      . ASP D 1 13  ? 28.746  19.401  42.508  1.00 43.52  ? 12  ASP C C      1 
ATOM   7815  O  O      . ASP D 1 13  ? 29.154  19.420  43.674  1.00 42.04  ? 12  ASP C O      1 
ATOM   7816  C  CB     . ASP D 1 13  ? 29.347  21.358  41.020  1.00 54.70  ? 12  ASP C CB     1 
ATOM   7817  C  CG     . ASP D 1 13  ? 30.152  22.361  41.852  1.00 53.43  ? 12  ASP C CG     1 
ATOM   7818  O  OD1    . ASP D 1 13  ? 30.122  22.287  43.088  1.00 51.92  ? 12  ASP C OD1    1 
ATOM   7819  O  OD2    . ASP D 1 13  ? 30.810  23.241  41.244  1.00 59.54  ? 12  ASP C OD2    1 
ATOM   7820  H  H      . ASP D 1 13  ? 28.052  22.292  42.941  1.00 54.09  ? 12  ASP C H      1 
ATOM   7821  H  HA     . ASP D 1 13  ? 27.556  20.402  41.164  1.00 56.92  ? 12  ASP C HA     1 
ATOM   7822  H  HB2    . ASP D 1 13  ? 29.962  20.685  40.689  1.00 65.67  ? 12  ASP C HB2    1 
ATOM   7823  H  HB3    . ASP D 1 13  ? 28.951  21.839  40.276  1.00 65.67  ? 12  ASP C HB3    1 
ATOM   7824  N  N      . GLY D 1 14  ? 28.675  18.287  41.781  1.00 43.41  ? 13  GLY C N      1 
ATOM   7825  C  CA     . GLY D 1 14  ? 29.229  17.030  42.239  1.00 43.85  ? 13  GLY C CA     1 
ATOM   7826  C  C      . GLY D 1 14  ? 28.289  16.148  43.030  1.00 43.22  ? 13  GLY C C      1 
ATOM   7827  O  O      . GLY D 1 14  ? 28.649  14.988  43.317  1.00 41.99  ? 13  GLY C O      1 
ATOM   7828  H  H      . GLY D 1 14  ? 28.303  18.240  41.007  1.00 52.12  ? 13  GLY C H      1 
ATOM   7829  H  HA2    . GLY D 1 14  ? 29.523  16.524  41.465  1.00 52.66  ? 13  GLY C HA2    1 
ATOM   7830  H  HA3    . GLY D 1 14  ? 29.996  17.219  42.802  1.00 52.66  ? 13  GLY C HA3    1 
ATOM   7831  N  N      . VAL D 1 15  ? 27.099  16.645  43.395  1.00 42.79  ? 14  VAL C N      1 
ATOM   7832  C  CA     . VAL D 1 15  ? 26.204  15.856  44.251  1.00 41.68  ? 14  VAL C CA     1 
ATOM   7833  C  C      . VAL D 1 15  ? 25.649  14.661  43.491  1.00 41.27  ? 14  VAL C C      1 
ATOM   7834  O  O      . VAL D 1 15  ? 25.330  13.623  44.091  1.00 42.20  ? 14  VAL C O      1 
ATOM   7835  C  CB     . VAL D 1 15  ? 25.054  16.731  44.796  1.00 40.06  ? 14  VAL C CB     1 
ATOM   7836  C  CG1    . VAL D 1 15  ? 25.619  17.924  45.539  1.00 43.92  ? 14  VAL C CG1    1 
ATOM   7837  C  CG2    . VAL D 1 15  ? 24.127  17.177  43.650  1.00 38.90  ? 14  VAL C CG2    1 
ATOM   7838  H  H      . VAL D 1 15  ? 26.795  17.416  43.167  1.00 51.39  ? 14  VAL C H      1 
ATOM   7839  H  HA     . VAL D 1 15  ? 26.724  15.532  45.003  1.00 50.05  ? 14  VAL C HA     1 
ATOM   7840  H  HB     . VAL D 1 15  ? 24.522  16.213  45.419  1.00 48.11  ? 14  VAL C HB     1 
ATOM   7841  H  HG11   . VAL D 1 15  ? 24.886  18.455  45.887  1.00 52.73  ? 14  VAL C HG11   1 
ATOM   7842  H  HG12   . VAL D 1 15  ? 26.175  17.608  46.268  1.00 52.73  ? 14  VAL C HG12   1 
ATOM   7843  H  HG13   . VAL D 1 15  ? 26.150  18.455  44.925  1.00 52.73  ? 14  VAL C HG13   1 
ATOM   7844  H  HG21   . VAL D 1 15  ? 23.515  17.851  43.984  1.00 46.71  ? 14  VAL C HG21   1 
ATOM   7845  H  HG22   . VAL D 1 15  ? 24.666  17.546  42.933  1.00 46.71  ? 14  VAL C HG22   1 
ATOM   7846  H  HG23   . VAL D 1 15  ? 23.630  16.409  43.329  1.00 46.71  ? 14  VAL C HG23   1 
ATOM   7847  N  N      . GLY D 1 16  ? 25.495  14.789  42.188  1.00 37.06  ? 15  GLY C N      1 
ATOM   7848  C  CA     . GLY D 1 16  ? 24.933  13.744  41.372  1.00 38.99  ? 15  GLY C CA     1 
ATOM   7849  C  C      . GLY D 1 16  ? 23.596  14.051  40.745  1.00 39.05  ? 15  GLY C C      1 
ATOM   7850  O  O      . GLY D 1 16  ? 22.879  13.103  40.395  1.00 37.05  ? 15  GLY C O      1 
ATOM   7851  H  H      . GLY D 1 16  ? 25.715  15.492  41.745  1.00 44.51  ? 15  GLY C H      1 
ATOM   7852  H  HA2    . GLY D 1 16  ? 25.555  13.548  40.654  1.00 46.82  ? 15  GLY C HA2    1 
ATOM   7853  H  HA3    . GLY D 1 16  ? 24.824  12.952  41.921  1.00 46.82  ? 15  GLY C HA3    1 
ATOM   7854  N  N      . LYS D 1 17  ? 23.233  15.336  40.602  1.00 39.30  ? 16  LYS C N      1 
ATOM   7855  C  CA     . LYS D 1 17  ? 22.027  15.715  39.856  1.00 39.39  ? 16  LYS C CA     1 
ATOM   7856  C  C      . LYS D 1 17  ? 21.979  15.073  38.485  1.00 37.57  ? 16  LYS C C      1 
ATOM   7857  O  O      . LYS D 1 17  ? 20.974  14.482  38.077  1.00 34.49  ? 16  LYS C O      1 
ATOM   7858  C  CB     . LYS D 1 17  ? 21.982  17.231  39.676  1.00 40.08  ? 16  LYS C CB     1 
ATOM   7859  C  CG     . LYS D 1 17  ? 22.107  18.002  40.965  1.00 34.13  ? 16  LYS C CG     1 
ATOM   7860  C  CD     . LYS D 1 17  ? 22.184  19.507  40.646  1.00 37.29  ? 16  LYS C CD     1 
ATOM   7861  C  CE     . LYS D 1 17  ? 23.502  19.883  39.931  1.00 41.17  ? 16  LYS C CE     1 
ATOM   7862  N  NZ     . LYS D 1 17  ? 24.706  19.441  40.690  1.00 36.47  ? 16  LYS C NZ     1 
ATOM   7863  H  H      . LYS D 1 17  ? 23.668  16.003  40.927  1.00 47.20  ? 16  LYS C H      1 
ATOM   7864  H  HA     . LYS D 1 17  ? 21.263  15.416  40.373  1.00 47.31  ? 16  LYS C HA     1 
ATOM   7865  H  HB2    . LYS D 1 17  ? 22.715  17.498  39.099  1.00 48.13  ? 16  LYS C HB2    1 
ATOM   7866  H  HB3    . LYS D 1 17  ? 21.135  17.471  39.269  1.00 48.13  ? 16  LYS C HB3    1 
ATOM   7867  H  HG2    . LYS D 1 17  ? 21.332  17.838  41.525  1.00 40.99  ? 16  LYS C HG2    1 
ATOM   7868  H  HG3    . LYS D 1 17  ? 22.915  17.737  41.432  1.00 40.99  ? 16  LYS C HG3    1 
ATOM   7869  H  HD2    . LYS D 1 17  ? 21.445  19.748  40.065  1.00 44.79  ? 16  LYS C HD2    1 
ATOM   7870  H  HD3    . LYS D 1 17  ? 22.134  20.011  41.473  1.00 44.79  ? 16  LYS C HD3    1 
ATOM   7871  H  HE2    . LYS D 1 17  ? 23.523  19.459  39.059  1.00 49.44  ? 16  LYS C HE2    1 
ATOM   7872  H  HE3    . LYS D 1 17  ? 23.546  20.847  39.832  1.00 49.44  ? 16  LYS C HE3    1 
ATOM   7873  H  HZ1    . LYS D 1 17  ? 25.441  19.778  40.318  1.00 43.80  ? 16  LYS C HZ1    1 
ATOM   7874  H  HZ2    . LYS D 1 17  ? 24.654  19.721  41.533  1.00 43.80  ? 16  LYS C HZ2    1 
ATOM   7875  H  HZ3    . LYS D 1 17  ? 24.760  18.552  40.683  1.00 43.80  ? 16  LYS C HZ3    1 
ATOM   7876  N  N      . SER D 1 18  ? 23.011  15.292  37.688  1.00 33.82  ? 17  SER C N      1 
ATOM   7877  C  CA     . SER D 1 18  ? 22.984  14.663  36.376  1.00 34.44  ? 17  SER C CA     1 
ATOM   7878  C  C      . SER D 1 18  ? 22.997  13.141  36.506  1.00 33.89  ? 17  SER C C      1 
ATOM   7879  O  O      . SER D 1 18  ? 22.317  12.435  35.754  1.00 35.13  ? 17  SER C O      1 
ATOM   7880  C  CB     . SER D 1 18  ? 24.147  15.158  35.513  1.00 32.97  ? 17  SER C CB     1 
ATOM   7881  O  OG     . SER D 1 18  ? 24.210  16.584  35.516  1.00 36.13  ? 17  SER C OG     1 
ATOM   7882  H  H      . SER D 1 18  ? 23.701  15.772  37.870  1.00 40.62  ? 17  SER C H      1 
ATOM   7883  H  HA     . SER D 1 18  ? 22.168  14.920  35.920  1.00 41.36  ? 17  SER C HA     1 
ATOM   7884  H  HB2    . SER D 1 18  ? 24.977  14.805  35.869  1.00 39.60  ? 17  SER C HB2    1 
ATOM   7885  H  HB3    . SER D 1 18  ? 24.019  14.850  34.603  1.00 39.60  ? 17  SER C HB3    1 
ATOM   7886  N  N      . ALA D 1 19  ? 23.765  12.609  37.454  1.00 37.73  ? 18  ALA C N      1 
ATOM   7887  C  CA     . ALA D 1 19  ? 23.833  11.165  37.580  1.00 34.05  ? 18  ALA C CA     1 
ATOM   7888  C  C      . ALA D 1 19  ? 22.463  10.601  37.921  1.00 38.65  ? 18  ALA C C      1 
ATOM   7889  O  O      . ALA D 1 19  ? 22.082  9.539   37.416  1.00 36.19  ? 18  ALA C O      1 
ATOM   7890  C  CB     . ALA D 1 19  ? 24.869  10.781  38.632  1.00 36.85  ? 18  ALA C CB     1 
ATOM   7891  H  H      . ALA D 1 19  ? 24.240  13.052  38.018  1.00 45.31  ? 18  ALA C H      1 
ATOM   7892  H  HA     . ALA D 1 19  ? 24.120  10.775  36.739  1.00 40.89  ? 18  ALA C HA     1 
ATOM   7893  H  HB1    . ALA D 1 19  ? 24.888  9.815   38.720  1.00 44.26  ? 18  ALA C HB1    1 
ATOM   7894  H  HB2    . ALA D 1 19  ? 25.740  11.105  38.352  1.00 44.26  ? 18  ALA C HB2    1 
ATOM   7895  H  HB3    . ALA D 1 19  ? 24.624  11.185  39.479  1.00 44.26  ? 18  ALA C HB3    1 
ATOM   7896  N  N      . LEU D 1 20  ? 21.690  11.335  38.735  1.00 32.24  ? 19  LEU C N      1 
ATOM   7897  C  CA     . LEU D 1 20  ? 20.331  10.931  39.077  1.00 35.91  ? 19  LEU C CA     1 
ATOM   7898  C  C      . LEU D 1 20  ? 19.404  11.081  37.885  1.00 38.04  ? 19  LEU C C      1 
ATOM   7899  O  O      . LEU D 1 20  ? 18.724  10.123  37.485  1.00 36.72  ? 19  LEU C O      1 
ATOM   7900  C  CB     . LEU D 1 20  ? 19.809  11.793  40.239  1.00 35.97  ? 19  LEU C CB     1 
ATOM   7901  C  CG     . LEU D 1 20  ? 20.304  11.541  41.650  1.00 37.71  ? 19  LEU C CG     1 
ATOM   7902  C  CD1    . LEU D 1 20  ? 19.853  12.730  42.483  1.00 40.95  ? 19  LEU C CD1    1 
ATOM   7903  C  CD2    . LEU D 1 20  ? 19.768  10.224  42.198  1.00 40.52  ? 19  LEU C CD2    1 
ATOM   7904  H  H      . LEU D 1 20  ? 21.935  12.074  39.101  1.00 38.72  ? 19  LEU C H      1 
ATOM   7905  H  HA     . LEU D 1 20  ? 20.345  10.001  39.351  1.00 43.12  ? 19  LEU C HA     1 
ATOM   7906  H  HB2    . LEU D 1 20  ? 20.033  12.715  40.036  1.00 43.20  ? 19  LEU C HB2    1 
ATOM   7907  H  HB3    . LEU D 1 20  ? 18.846  11.684  40.268  1.00 43.20  ? 19  LEU C HB3    1 
ATOM   7908  H  HG     . LEU D 1 20  ? 21.270  11.456  41.683  1.00 45.28  ? 19  LEU C HG     1 
ATOM   7909  H  HD11   . LEU D 1 20  ? 20.082  12.570  43.412  1.00 49.17  ? 19  LEU C HD11   1 
ATOM   7910  H  HD12   . LEU D 1 20  ? 20.303  13.527  42.164  1.00 49.17  ? 19  LEU C HD12   1 
ATOM   7911  H  HD13   . LEU D 1 20  ? 18.893  12.833  42.392  1.00 49.17  ? 19  LEU C HD13   1 
ATOM   7912  H  HD21   . LEU D 1 20  ? 20.093  10.103  43.104  1.00 48.66  ? 19  LEU C HD21   1 
ATOM   7913  H  HD22   . LEU D 1 20  ? 18.799  10.252  42.196  1.00 48.66  ? 19  LEU C HD22   1 
ATOM   7914  H  HD23   . LEU D 1 20  ? 20.079  9.498   41.636  1.00 48.66  ? 19  LEU C HD23   1 
ATOM   7915  N  N      . THR D 1 21  ? 19.366  12.291  37.305  1.00 37.89  ? 20  THR C N      1 
ATOM   7916  C  CA     . THR D 1 21  ? 18.553  12.551  36.115  1.00 31.09  ? 20  THR C CA     1 
ATOM   7917  C  C      . THR D 1 21  ? 18.812  11.500  35.056  1.00 34.39  ? 20  THR C C      1 
ATOM   7918  O  O      . THR D 1 21  ? 17.878  10.923  34.485  1.00 33.53  ? 20  THR C O      1 
ATOM   7919  C  CB     . THR D 1 21  ? 18.866  13.951  35.577  1.00 32.43  ? 20  THR C CB     1 
ATOM   7920  O  OG1    . THR D 1 21  ? 18.473  14.957  36.528  1.00 30.52  ? 20  THR C OG1    1 
ATOM   7921  C  CG2    . THR D 1 21  ? 18.161  14.204  34.225  1.00 33.13  ? 20  THR C CG2    1 
ATOM   7922  H  H      . THR D 1 21  ? 19.804  12.977  37.583  1.00 45.51  ? 20  THR C H      1 
ATOM   7923  H  HA     . THR D 1 21  ? 17.613  12.522  36.351  1.00 37.34  ? 20  THR C HA     1 
ATOM   7924  H  HB     . THR D 1 21  ? 19.822  14.018  35.430  1.00 38.95  ? 20  THR C HB     1 
ATOM   7925  H  HG1    . THR D 1 21  ? 18.844  14.812  37.268  1.00 36.66  ? 20  THR C HG1    1 
ATOM   7926  H  HG21   . THR D 1 21  ? 18.174  15.152  34.016  1.00 39.80  ? 20  THR C HG21   1 
ATOM   7927  H  HG22   . THR D 1 21  ? 18.617  13.721  33.518  1.00 39.80  ? 20  THR C HG22   1 
ATOM   7928  H  HG23   . THR D 1 21  ? 17.240  13.904  34.269  1.00 39.80  ? 20  THR C HG23   1 
ATOM   7929  N  N      . ILE D 1 22  ? 20.097  11.224  34.773  1.00 32.62  ? 21  ILE C N      1 
ATOM   7930  C  CA     . ILE D 1 22  ? 20.401  10.273  33.696  1.00 36.88  ? 21  ILE C CA     1 
ATOM   7931  C  C      . ILE D 1 22  ? 19.945  8.862   34.086  1.00 36.07  ? 21  ILE C C      1 
ATOM   7932  O  O      . ILE D 1 22  ? 19.534  8.071   33.228  1.00 41.24  ? 21  ILE C O      1 
ATOM   7933  C  CB     . ILE D 1 22  ? 21.904  10.317  33.354  1.00 38.30  ? 21  ILE C CB     1 
ATOM   7934  C  CG1    . ILE D 1 22  ? 22.255  11.571  32.532  1.00 36.99  ? 21  ILE C CG1    1 
ATOM   7935  C  CG2    . ILE D 1 22  ? 22.307  9.083   32.560  1.00 40.09  ? 21  ILE C CG2    1 
ATOM   7936  C  CD1    . ILE D 1 22  ? 21.306  11.901  31.376  1.00 41.30  ? 21  ILE C CD1    1 
ATOM   7937  H  H      . ILE D 1 22  ? 20.780  11.560  35.174  1.00 39.18  ? 21  ILE C H      1 
ATOM   7938  H  HA     . ILE D 1 22  ? 19.911  10.534  32.900  1.00 44.29  ? 21  ILE C HA     1 
ATOM   7939  H  HB     . ILE D 1 22  ? 22.386  10.342  34.196  1.00 45.99  ? 21  ILE C HB     1 
ATOM   7940  H  HG12   . ILE D 1 22  ? 22.256  12.336  33.129  1.00 44.43  ? 21  ILE C HG12   1 
ATOM   7941  H  HG13   . ILE D 1 22  ? 23.138  11.447  32.151  1.00 44.43  ? 21  ILE C HG13   1 
ATOM   7942  H  HG21   . ILE D 1 22  ? 23.238  9.165   32.299  1.00 48.14  ? 21  ILE C HG21   1 
ATOM   7943  H  HG22   . ILE D 1 22  ? 22.187  8.296   33.115  1.00 48.14  ? 21  ILE C HG22   1 
ATOM   7944  H  HG23   . ILE D 1 22  ? 21.747  9.019   31.770  1.00 48.14  ? 21  ILE C HG23   1 
ATOM   7945  H  HD11   . ILE D 1 22  ? 21.663  12.654  30.879  1.00 49.59  ? 21  ILE C HD11   1 
ATOM   7946  H  HD12   . ILE D 1 22  ? 21.234  11.126  30.797  1.00 49.59  ? 21  ILE C HD12   1 
ATOM   7947  H  HD13   . ILE D 1 22  ? 20.435  12.127  31.738  1.00 49.59  ? 21  ILE C HD13   1 
ATOM   7948  N  N      . GLN D 1 23  ? 20.023  8.519   35.353  1.00 35.95  ? 22  GLN C N      1 
ATOM   7949  C  CA     . GLN D 1 23  ? 19.532  7.205   35.762  1.00 41.13  ? 22  GLN C CA     1 
ATOM   7950  C  C      . GLN D 1 23  ? 18.014  7.134   35.576  1.00 40.87  ? 22  GLN C C      1 
ATOM   7951  O  O      . GLN D 1 23  ? 17.509  6.163   35.000  1.00 45.65  ? 22  GLN C O      1 
ATOM   7952  C  CB     . GLN D 1 23  ? 19.969  6.917   37.187  1.00 43.26  ? 22  GLN C CB     1 
ATOM   7953  C  CG     . GLN D 1 23  ? 19.984  5.429   37.595  1.00 47.64  ? 22  GLN C CG     1 
ATOM   7954  C  CD     . GLN D 1 23  ? 20.841  4.510   36.724  1.00 45.73  ? 22  GLN C CD     1 
ATOM   7955  O  OE1    . GLN D 1 23  ? 20.439  4.117   35.636  1.00 47.82  ? 22  GLN C OE1    1 
ATOM   7956  N  NE2    . GLN D 1 23  ? 21.995  4.099   37.256  1.00 48.11  ? 22  GLN C NE2    1 
ATOM   7957  H  H      . GLN D 1 23  ? 20.345  9.006   35.984  1.00 43.17  ? 22  GLN C H      1 
ATOM   7958  H  HA     . GLN D 1 23  ? 19.919  6.504   35.215  1.00 49.39  ? 22  GLN C HA     1 
ATOM   7959  H  HB2    . GLN D 1 23  ? 20.870  7.257   37.303  1.00 51.95  ? 22  GLN C HB2    1 
ATOM   7960  H  HB3    . GLN D 1 23  ? 19.362  7.375   37.789  1.00 51.95  ? 22  GLN C HB3    1 
ATOM   7961  H  HG2    . GLN D 1 23  ? 20.324  5.365   38.501  1.00 57.21  ? 22  GLN C HG2    1 
ATOM   7962  H  HG3    . GLN D 1 23  ? 19.074  5.094   37.557  1.00 57.21  ? 22  GLN C HG3    1 
ATOM   7963  H  HE21   . GLN D 1 23  ? 22.219  4.353   38.047  1.00 57.77  ? 22  GLN C HE21   1 
ATOM   7964  H  HE22   . GLN D 1 23  ? 22.515  3.581   36.807  1.00 57.77  ? 22  GLN C HE22   1 
ATOM   7965  N  N      . LEU D 1 24  ? 17.287  8.191   35.964  1.00 37.47  ? 23  LEU C N      1 
ATOM   7966  C  CA     . LEU D 1 24  ? 15.853  8.268   35.644  1.00 38.09  ? 23  LEU C CA     1 
ATOM   7967  C  C      . LEU D 1 24  ? 15.593  8.141   34.148  1.00 40.84  ? 23  LEU C C      1 
ATOM   7968  O  O      . LEU D 1 24  ? 14.704  7.390   33.720  1.00 36.05  ? 23  LEU C O      1 
ATOM   7969  C  CB     . LEU D 1 24  ? 15.260  9.583   36.148  1.00 35.99  ? 23  LEU C CB     1 
ATOM   7970  C  CG     . LEU D 1 24  ? 13.750  9.766   35.900  1.00 37.86  ? 23  LEU C CG     1 
ATOM   7971  C  CD1    . LEU D 1 24  ? 12.930  9.096   37.018  1.00 37.18  ? 23  LEU C CD1    1 
ATOM   7972  C  CD2    . LEU D 1 24  ? 13.366  11.246  35.777  1.00 35.63  ? 23  LEU C CD2    1 
ATOM   7973  H  H      . LEU D 1 24  ? 17.592  8.863   36.406  1.00 44.99  ? 23  LEU C H      1 
ATOM   7974  H  HA     . LEU D 1 24  ? 15.417  7.530   36.098  1.00 45.74  ? 23  LEU C HA     1 
ATOM   7975  H  HB2    . LEU D 1 24  ? 15.405  9.636   37.106  1.00 43.22  ? 23  LEU C HB2    1 
ATOM   7976  H  HB3    . LEU D 1 24  ? 15.718  10.314  35.703  1.00 43.22  ? 23  LEU C HB3    1 
ATOM   7977  H  HG     . LEU D 1 24  ? 13.534  9.338   35.056  1.00 45.46  ? 23  LEU C HG     1 
ATOM   7978  H  HD11   . LEU D 1 24  ? 11.986  9.221   36.836  1.00 44.65  ? 23  LEU C HD11   1 
ATOM   7979  H  HD12   . LEU D 1 24  ? 13.140  8.149   37.040  1.00 44.65  ? 23  LEU C HD12   1 
ATOM   7980  H  HD13   . LEU D 1 24  ? 13.161  9.505   37.867  1.00 44.65  ? 23  LEU C HD13   1 
ATOM   7981  H  HD21   . LEU D 1 24  ? 12.404  11.314  35.666  1.00 42.79  ? 23  LEU C HD21   1 
ATOM   7982  H  HD22   . LEU D 1 24  ? 13.640  11.711  36.582  1.00 42.79  ? 23  LEU C HD22   1 
ATOM   7983  H  HD23   . LEU D 1 24  ? 13.816  11.626  35.006  1.00 42.79  ? 23  LEU C HD23   1 
ATOM   7984  N  N      . ILE D 1 25  ? 16.327  8.906   33.333  1.00 34.43  ? 24  ILE C N      1 
ATOM   7985  C  CA     . ILE D 1 25  ? 16.028  8.941   31.908  1.00 38.55  ? 24  ILE C CA     1 
ATOM   7986  C  C      . ILE D 1 25  ? 16.548  7.695   31.205  1.00 36.70  ? 24  ILE C C      1 
ATOM   7987  O  O      . ILE D 1 25  ? 15.816  7.055   30.443  1.00 39.80  ? 24  ILE C O      1 
ATOM   7988  C  CB     . ILE D 1 25  ? 16.598  10.217  31.261  1.00 35.21  ? 24  ILE C CB     1 
ATOM   7989  C  CG1    . ILE D 1 25  ? 16.053  11.463  31.953  1.00 35.63  ? 24  ILE C CG1    1 
ATOM   7990  C  CG2    . ILE D 1 25  ? 16.267  10.244  29.771  1.00 32.75  ? 24  ILE C CG2    1 
ATOM   7991  C  CD1    . ILE D 1 25  ? 14.544  11.609  31.847  1.00 30.61  ? 24  ILE C CD1    1 
ATOM   7992  H  H      . ILE D 1 25  ? 16.987  9.401   33.578  1.00 41.35  ? 24  ILE C H      1 
ATOM   7993  H  HA     . ILE D 1 25  ? 15.063  8.958   31.813  1.00 46.29  ? 24  ILE C HA     1 
ATOM   7994  H  HB     . ILE D 1 25  ? 17.562  10.209  31.368  1.00 42.28  ? 24  ILE C HB     1 
ATOM   7995  H  HG12   . ILE D 1 25  ? 16.282  11.423  32.894  1.00 42.79  ? 24  ILE C HG12   1 
ATOM   7996  H  HG13   . ILE D 1 25  ? 16.456  12.247  31.547  1.00 42.79  ? 24  ILE C HG13   1 
ATOM   7997  H  HG21   . ILE D 1 25  ? 16.414  11.141  29.431  1.00 39.34  ? 24  ILE C HG21   1 
ATOM   7998  H  HG22   . ILE D 1 25  ? 16.844  9.616   29.308  1.00 39.34  ? 24  ILE C HG22   1 
ATOM   7999  H  HG23   . ILE D 1 25  ? 15.339  9.992   29.649  1.00 39.34  ? 24  ILE C HG23   1 
ATOM   8000  H  HD11   . ILE D 1 25  ? 14.284  12.469  32.210  1.00 36.76  ? 24  ILE C HD11   1 
ATOM   8001  H  HD12   . ILE D 1 25  ? 14.286  11.551  30.913  1.00 36.76  ? 24  ILE C HD12   1 
ATOM   8002  H  HD13   . ILE D 1 25  ? 14.122  10.895  32.351  1.00 36.76  ? 24  ILE C HD13   1 
ATOM   8003  N  N      . GLN D 1 26  ? 17.822  7.348   31.409  1.00 38.12  ? 25  GLN C N      1 
ATOM   8004  C  CA     . GLN D 1 26  ? 18.468  6.389   30.517  1.00 41.41  ? 25  GLN C CA     1 
ATOM   8005  C  C      . GLN D 1 26  ? 18.843  5.070   31.178  1.00 49.81  ? 25  GLN C C      1 
ATOM   8006  O  O      . GLN D 1 26  ? 19.286  4.151   30.472  1.00 48.32  ? 25  GLN C O      1 
ATOM   8007  C  CB     . GLN D 1 26  ? 19.724  7.000   29.886  1.00 46.45  ? 25  GLN C CB     1 
ATOM   8008  C  CG     . GLN D 1 26  ? 19.432  8.036   28.839  1.00 38.34  ? 25  GLN C CG     1 
ATOM   8009  C  CD     . GLN D 1 26  ? 20.681  8.643   28.265  1.00 48.57  ? 25  GLN C CD     1 
ATOM   8010  O  OE1    . GLN D 1 26  ? 21.695  7.963   28.110  1.00 50.31  ? 25  GLN C OE1    1 
ATOM   8011  N  NE2    . GLN D 1 26  ? 20.620  9.941   27.930  1.00 48.24  ? 25  GLN C NE2    1 
ATOM   8012  H  H      . GLN D 1 26  ? 18.318  7.649   32.043  1.00 45.78  ? 25  GLN C H      1 
ATOM   8013  H  HA     . GLN D 1 26  ? 17.833  6.189   29.812  1.00 49.73  ? 25  GLN C HA     1 
ATOM   8014  H  HB2    . GLN D 1 26  ? 20.248  7.424   30.584  1.00 55.77  ? 25  GLN C HB2    1 
ATOM   8015  H  HB3    . GLN D 1 26  ? 20.239  6.293   29.468  1.00 55.77  ? 25  GLN C HB3    1 
ATOM   8016  H  HG2    . GLN D 1 26  ? 18.938  7.622   28.114  1.00 46.05  ? 25  GLN C HG2    1 
ATOM   8017  H  HG3    . GLN D 1 26  ? 18.906  8.748   29.235  1.00 46.05  ? 25  GLN C HG3    1 
ATOM   8018  H  HE21   . GLN D 1 26  ? 19.890  10.381  28.047  1.00 57.92  ? 25  GLN C HE21   1 
ATOM   8019  H  HE22   . GLN D 1 26  ? 21.310  10.332  27.598  1.00 57.92  ? 25  GLN C HE22   1 
ATOM   8020  N  N      . ASN D 1 27  ? 18.655  4.928   32.486  1.00 46.62  ? 26  ASN C N      1 
ATOM   8021  C  CA     . ASN D 1 27  ? 19.002  3.676   33.151  1.00 53.48  ? 26  ASN C CA     1 
ATOM   8022  C  C      . ASN D 1 27  ? 20.462  3.360   32.854  1.00 54.44  ? 26  ASN C C      1 
ATOM   8023  O  O      . ASN D 1 27  ? 20.835  2.241   32.481  1.00 50.16  ? 26  ASN C O      1 
ATOM   8024  C  CB     . ASN D 1 27  ? 18.082  2.541   32.710  1.00 57.27  ? 26  ASN C CB     1 
ATOM   8025  C  CG     . ASN D 1 27  ? 16.609  2.887   32.881  1.00 59.63  ? 26  ASN C CG     1 
ATOM   8026  O  OD1    . ASN D 1 27  ? 16.115  3.042   34.008  1.00 58.89  ? 26  ASN C OD1    1 
ATOM   8027  N  ND2    . ASN D 1 27  ? 15.902  3.020   31.759  1.00 58.92  ? 26  ASN C ND2    1 
ATOM   8028  H  H      . ASN D 1 27  ? 18.331  5.534   33.003  1.00 55.97  ? 26  ASN C H      1 
ATOM   8029  H  HA     . ASN D 1 27  ? 18.888  3.764   34.110  1.00 64.21  ? 26  ASN C HA     1 
ATOM   8030  H  HB2    . ASN D 1 27  ? 18.240  2.351   31.772  1.00 68.75  ? 26  ASN C HB2    1 
ATOM   8031  H  HB3    . ASN D 1 27  ? 18.271  1.754   33.244  1.00 68.75  ? 26  ASN C HB3    1 
ATOM   8032  H  HD21   . ASN D 1 27  ? 15.065  3.215   31.798  1.00 70.74  ? 26  ASN C HD21   1 
ATOM   8033  H  HD22   . ASN D 1 27  ? 16.282  2.911   30.995  1.00 70.74  ? 26  ASN C HD22   1 
ATOM   8034  N  N      . HIS D 1 28  ? 21.273  4.406   32.941  1.00 50.02  ? 27  HIS C N      1 
ATOM   8035  C  CA     . HIS D 1 28  ? 22.715  4.371   32.778  1.00 50.04  ? 27  HIS C CA     1 
ATOM   8036  C  C      . HIS D 1 28  ? 23.321  5.105   33.960  1.00 41.87  ? 27  HIS C C      1 
ATOM   8037  O  O      . HIS D 1 28  ? 22.748  6.091   34.435  1.00 43.25  ? 27  HIS C O      1 
ATOM   8038  C  CB     . HIS D 1 28  ? 23.134  5.054   31.480  1.00 47.99  ? 27  HIS C CB     1 
ATOM   8039  C  CG     . HIS D 1 28  ? 24.607  5.023   31.243  1.00 52.48  ? 27  HIS C CG     1 
ATOM   8040  N  ND1    . HIS D 1 28  ? 25.336  6.150   30.935  1.00 56.14  ? 27  HIS C ND1    1 
ATOM   8041  C  CD2    . HIS D 1 28  ? 25.492  3.997   31.276  1.00 56.67  ? 27  HIS C CD2    1 
ATOM   8042  C  CE1    . HIS D 1 28  ? 26.611  5.822   30.792  1.00 56.49  ? 27  HIS C CE1    1 
ATOM   8043  N  NE2    . HIS D 1 28  ? 26.732  4.522   30.994  1.00 59.22  ? 27  HIS C NE2    1 
ATOM   8044  H  H      . HIS D 1 28  ? 20.990  5.201   33.105  1.00 60.06  ? 27  HIS C H      1 
ATOM   8045  H  HA     . HIS D 1 28  ? 23.041  3.458   32.755  1.00 60.08  ? 27  HIS C HA     1 
ATOM   8046  H  HB2    . HIS D 1 28  ? 22.704  4.604   30.737  1.00 57.62  ? 27  HIS C HB2    1 
ATOM   8047  H  HB3    . HIS D 1 28  ? 22.857  5.983   31.511  1.00 57.62  ? 27  HIS C HB3    1 
ATOM   8048  H  HD2    . HIS D 1 28  ? 25.298  3.106   31.456  1.00 68.04  ? 27  HIS C HD2    1 
ATOM   8049  H  HE1    . HIS D 1 28  ? 27.303  6.408   30.584  1.00 67.82  ? 27  HIS C HE1    1 
ATOM   8050  H  HE2    . HIS D 1 28  ? 27.466  4.076   30.955  1.00 71.10  ? 27  HIS C HE2    1 
ATOM   8051  N  N      . PHE D 1 29  ? 24.472  4.637   34.439  1.00 47.17  ? 28  PHE C N      1 
ATOM   8052  C  CA     . PHE D 1 29  ? 25.193  5.341   35.486  1.00 46.35  ? 28  PHE C CA     1 
ATOM   8053  C  C      . PHE D 1 29  ? 26.430  6.020   34.926  1.00 48.33  ? 28  PHE C C      1 
ATOM   8054  O  O      . PHE D 1 29  ? 27.222  5.373   34.223  1.00 43.41  ? 28  PHE C O      1 
ATOM   8055  C  CB     . PHE D 1 29  ? 25.644  4.417   36.601  1.00 42.90  ? 28  PHE C CB     1 
ATOM   8056  C  CG     . PHE D 1 29  ? 26.439  5.111   37.656  1.00 44.21  ? 28  PHE C CG     1 
ATOM   8057  C  CD1    . PHE D 1 29  ? 25.886  6.166   38.358  1.00 42.73  ? 28  PHE C CD1    1 
ATOM   8058  C  CD2    . PHE D 1 29  ? 27.725  4.698   37.968  1.00 45.23  ? 28  PHE C CD2    1 
ATOM   8059  C  CE1    . PHE D 1 29  ? 26.585  6.791   39.373  1.00 44.40  ? 28  PHE C CE1    1 
ATOM   8060  C  CE2    . PHE D 1 29  ? 28.446  5.329   38.985  1.00 46.75  ? 28  PHE C CE2    1 
ATOM   8061  C  CZ     . PHE D 1 29  ? 27.872  6.378   39.685  1.00 45.22  ? 28  PHE C CZ     1 
ATOM   8062  H  H      . PHE D 1 29  ? 24.850  3.913   34.171  1.00 56.64  ? 28  PHE C H      1 
ATOM   8063  H  HA     . PHE D 1 29  ? 24.585  6.008   35.841  1.00 55.66  ? 28  PHE C HA     1 
ATOM   8064  H  HB2    . PHE D 1 29  ? 24.862  4.029   37.023  1.00 51.51  ? 28  PHE C HB2    1 
ATOM   8065  H  HB3    . PHE D 1 29  ? 26.198  3.716   36.223  1.00 51.51  ? 28  PHE C HB3    1 
ATOM   8066  H  HD1    . PHE D 1 29  ? 25.031  6.461   38.143  1.00 51.30  ? 28  PHE C HD1    1 
ATOM   8067  H  HD2    . PHE D 1 29  ? 28.111  3.995   37.497  1.00 54.31  ? 28  PHE C HD2    1 
ATOM   8068  H  HE1    . PHE D 1 29  ? 26.192  7.487   39.848  1.00 53.32  ? 28  PHE C HE1    1 
ATOM   8069  H  HE2    . PHE D 1 29  ? 29.308  5.046   39.191  1.00 56.13  ? 28  PHE C HE2    1 
ATOM   8070  H  HZ     . PHE D 1 29  ? 28.348  6.805   40.361  1.00 54.30  ? 28  PHE C HZ     1 
ATOM   8071  N  N      . VAL D 1 30  ? 26.611  7.290   35.290  1.00 48.49  ? 29  VAL C N      1 
ATOM   8072  C  CA     . VAL D 1 30  ? 27.768  8.094   34.902  1.00 45.36  ? 29  VAL C CA     1 
ATOM   8073  C  C      . VAL D 1 30  ? 28.764  8.063   36.058  1.00 43.01  ? 29  VAL C C      1 
ATOM   8074  O  O      . VAL D 1 30  ? 28.548  8.687   37.107  1.00 42.38  ? 29  VAL C O      1 
ATOM   8075  C  CB     . VAL D 1 30  ? 27.372  9.541   34.555  1.00 46.78  ? 29  VAL C CB     1 
ATOM   8076  C  CG1    . VAL D 1 30  ? 26.503  9.579   33.287  1.00 47.20  ? 29  VAL C CG1    1 
ATOM   8077  C  CG2    . VAL D 1 30  ? 26.703  10.252  35.779  1.00 45.54  ? 29  VAL C CG2    1 
ATOM   8078  H  H      . VAL D 1 30  ? 26.055  7.724   35.783  1.00 58.22  ? 29  VAL C H      1 
ATOM   8079  H  HA     . VAL D 1 30  ? 28.182  7.694   34.121  1.00 54.46  ? 29  VAL C HA     1 
ATOM   8080  H  HB     . VAL D 1 30  ? 28.172  10.051  34.355  1.00 56.17  ? 29  VAL C HB     1 
ATOM   8081  H  HG11   . VAL D 1 30  ? 26.266  10.499  33.094  1.00 56.67  ? 29  VAL C HG11   1 
ATOM   8082  H  HG12   . VAL D 1 30  ? 27.007  9.205   32.548  1.00 56.67  ? 29  VAL C HG12   1 
ATOM   8083  H  HG13   . VAL D 1 30  ? 25.700  9.056   33.439  1.00 56.67  ? 29  VAL C HG13   1 
ATOM   8084  H  HG21   . VAL D 1 30  ? 26.138  10.972  35.457  1.00 54.68  ? 29  VAL C HG21   1 
ATOM   8085  H  HG22   . VAL D 1 30  ? 26.168  9.605   36.267  1.00 54.68  ? 29  VAL C HG22   1 
ATOM   8086  H  HG23   . VAL D 1 30  ? 27.397  10.609  36.355  1.00 54.68  ? 29  VAL C HG23   1 
ATOM   8087  N  N      . ASP D 1 31  ? 29.863  7.334   35.882  1.00 44.81  ? 30  ASP C N      1 
ATOM   8088  C  CA     . ASP D 1 31  ? 30.914  7.319   36.891  1.00 43.32  ? 30  ASP C CA     1 
ATOM   8089  C  C      . ASP D 1 31  ? 31.910  8.461   36.719  1.00 45.31  ? 30  ASP C C      1 
ATOM   8090  O  O      . ASP D 1 31  ? 32.601  8.815   37.677  1.00 41.95  ? 30  ASP C O      1 
ATOM   8091  C  CB     . ASP D 1 31  ? 31.636  5.960   36.885  1.00 49.25  ? 30  ASP C CB     1 
ATOM   8092  C  CG     . ASP D 1 31  ? 32.007  5.481   35.487  1.00 51.63  ? 30  ASP C CG     1 
ATOM   8093  O  OD1    . ASP D 1 31  ? 33.223  5.344   35.203  1.00 57.57  ? 30  ASP C OD1    1 
ATOM   8094  O  OD2    . ASP D 1 31  ? 31.100  5.223   34.673  1.00 55.73  ? 30  ASP C OD2    1 
ATOM   8095  H  H      . ASP D 1 31  ? 30.021  6.844   35.193  1.00 53.80  ? 30  ASP C H      1 
ATOM   8096  H  HA     . ASP D 1 31  ? 30.518  7.420   37.771  1.00 52.02  ? 30  ASP C HA     1 
ATOM   8097  H  HB2    . ASP D 1 31  ? 32.454  6.037   37.401  1.00 59.14  ? 30  ASP C HB2    1 
ATOM   8098  H  HB3    . ASP D 1 31  ? 31.055  5.294   37.284  1.00 59.14  ? 30  ASP C HB3    1 
ATOM   8099  N  N      . GLU D 1 32  ? 31.962  9.079   35.551  1.00 44.20  ? 31  GLU C N      1 
ATOM   8100  C  CA     . GLU D 1 32  ? 32.877  10.187  35.286  1.00 44.71  ? 31  GLU C CA     1 
ATOM   8101  C  C      . GLU D 1 32  ? 32.189  11.514  35.575  1.00 43.43  ? 31  GLU C C      1 
ATOM   8102  O  O      . GLU D 1 32  ? 30.972  11.644  35.421  1.00 45.80  ? 31  GLU C O      1 
ATOM   8103  C  CB     . GLU D 1 32  ? 33.336  10.112  33.830  1.00 44.28  ? 31  GLU C CB     1 
ATOM   8104  C  CG     . GLU D 1 32  ? 34.456  9.111   33.610  1.00 46.94  ? 31  GLU C CG     1 
ATOM   8105  C  CD     . GLU D 1 32  ? 34.484  8.554   32.204  1.00 52.88  ? 31  GLU C CD     1 
ATOM   8106  O  OE1    . GLU D 1 32  ? 33.515  7.882   31.805  1.00 62.68  ? 31  GLU C OE1    1 
ATOM   8107  O  OE2    . GLU D 1 32  ? 35.486  8.739   31.498  1.00 51.68  ? 31  GLU C OE2    1 
ATOM   8108  H  H      . GLU D 1 32  ? 31.467  8.875   34.877  1.00 53.07  ? 31  GLU C H      1 
ATOM   8109  H  HA     . GLU D 1 32  ? 33.660  10.139  35.857  1.00 53.69  ? 31  GLU C HA     1 
ATOM   8110  H  HB2    . GLU D 1 32  ? 32.585  9.847   33.276  1.00 53.17  ? 31  GLU C HB2    1 
ATOM   8111  H  HB3    . GLU D 1 32  ? 33.657  10.986  33.556  1.00 53.17  ? 31  GLU C HB3    1 
ATOM   8112  H  HG2    . GLU D 1 32  ? 35.306  9.549   33.775  1.00 56.36  ? 31  GLU C HG2    1 
ATOM   8113  H  HG3    . GLU D 1 32  ? 34.341  8.369   34.223  1.00 56.36  ? 31  GLU C HG3    1 
ATOM   8114  N  N      . TYR D 1 33  ? 32.974  12.508  35.977  1.00 40.99  ? 32  TYR C N      1 
ATOM   8115  C  CA     . TYR D 1 33  ? 32.448  13.820  36.363  1.00 42.10  ? 32  TYR C CA     1 
ATOM   8116  C  C      . TYR D 1 33  ? 32.451  14.761  35.159  1.00 46.13  ? 32  TYR C C      1 
ATOM   8117  O  O      . TYR D 1 33  ? 33.521  15.176  34.690  1.00 39.18  ? 32  TYR C O      1 
ATOM   8118  C  CB     . TYR D 1 33  ? 33.272  14.416  37.497  1.00 45.18  ? 32  TYR C CB     1 
ATOM   8119  C  CG     . TYR D 1 33  ? 32.782  15.770  37.983  1.00 47.42  ? 32  TYR C CG     1 
ATOM   8120  C  CD1    . TYR D 1 33  ? 31.437  16.109  37.905  1.00 47.16  ? 32  TYR C CD1    1 
ATOM   8121  C  CD2    . TYR D 1 33  ? 33.661  16.714  38.488  1.00 50.56  ? 32  TYR C CD2    1 
ATOM   8122  C  CE1    . TYR D 1 33  ? 30.984  17.343  38.345  1.00 45.94  ? 32  TYR C CE1    1 
ATOM   8123  C  CE2    . TYR D 1 33  ? 33.212  17.952  38.931  1.00 50.98  ? 32  TYR C CE2    1 
ATOM   8124  C  CZ     . TYR D 1 33  ? 31.866  18.255  38.851  1.00 49.48  ? 32  TYR C CZ     1 
ATOM   8125  O  OH     . TYR D 1 33  ? 31.380  19.477  39.285  1.00 50.87  ? 32  TYR C OH     1 
ATOM   8126  H  H      . TYR D 1 33  ? 33.830  12.450  36.037  1.00 49.22  ? 32  TYR C H      1 
ATOM   8127  H  HA     . TYR D 1 33  ? 31.531  13.704  36.656  1.00 50.55  ? 32  TYR C HA     1 
ATOM   8128  H  HB2    . TYR D 1 33  ? 33.246  13.806  38.251  1.00 54.24  ? 32  TYR C HB2    1 
ATOM   8129  H  HB3    . TYR D 1 33  ? 34.185  14.526  37.191  1.00 54.24  ? 32  TYR C HB3    1 
ATOM   8130  H  HD1    . TYR D 1 33  ? 30.831  15.498  37.553  1.00 56.63  ? 32  TYR C HD1    1 
ATOM   8131  H  HD2    . TYR D 1 33  ? 34.569  16.516  38.530  1.00 60.71  ? 32  TYR C HD2    1 
ATOM   8132  H  HE1    . TYR D 1 33  ? 30.079  17.550  38.296  1.00 55.16  ? 32  TYR C HE1    1 
ATOM   8133  H  HE2    . TYR D 1 33  ? 33.812  18.571  39.280  1.00 61.21  ? 32  TYR C HE2    1 
ATOM   8134  H  HH     . TYR D 1 33  ? 32.007  19.942  39.595  1.00 61.08  ? 32  TYR C HH     1 
ATOM   8135  N  N      . ASP D 1 34  ? 31.245  15.134  34.696  1.00 44.15  ? 33  ASP C N      1 
ATOM   8136  C  CA     . ASP D 1 34  ? 31.032  16.036  33.554  1.00 44.42  ? 33  ASP C CA     1 
ATOM   8137  C  C      . ASP D 1 34  ? 30.100  17.160  34.005  1.00 42.55  ? 33  ASP C C      1 
ATOM   8138  O  O      . ASP D 1 34  ? 28.880  17.077  33.808  1.00 40.45  ? 33  ASP C O      1 
ATOM   8139  C  CB     . ASP D 1 34  ? 30.441  15.259  32.367  1.00 43.68  ? 33  ASP C CB     1 
ATOM   8140  C  CG     . ASP D 1 34  ? 30.310  16.095  31.103  1.00 46.29  ? 33  ASP C CG     1 
ATOM   8141  O  OD1    . ASP D 1 34  ? 31.049  17.102  30.937  1.00 40.95  ? 33  ASP C OD1    1 
ATOM   8142  O  OD2    . ASP D 1 34  ? 29.470  15.729  30.259  1.00 42.64  ? 33  ASP C OD2    1 
ATOM   8143  H  H      . ASP D 1 34  ? 30.505  14.864  35.043  1.00 53.02  ? 33  ASP C H      1 
ATOM   8144  H  HA     . ASP D 1 34  ? 31.873  16.433  33.280  1.00 53.33  ? 33  ASP C HA     1 
ATOM   8145  H  HB2    . ASP D 1 34  ? 31.017  14.506  32.167  1.00 52.46  ? 33  ASP C HB2    1 
ATOM   8146  H  HB3    . ASP D 1 34  ? 29.555  14.945  32.608  1.00 52.46  ? 33  ASP C HB3    1 
ATOM   8147  N  N      . PRO D 1 35  ? 30.644  18.228  34.606  1.00 42.28  ? 34  PRO C N      1 
ATOM   8148  C  CA     . PRO D 1 35  ? 29.781  19.263  35.203  1.00 38.04  ? 34  PRO C CA     1 
ATOM   8149  C  C      . PRO D 1 35  ? 28.897  19.927  34.160  1.00 39.87  ? 34  PRO C C      1 
ATOM   8150  O  O      . PRO D 1 35  ? 29.300  20.110  33.011  1.00 36.95  ? 34  PRO C O      1 
ATOM   8151  C  CB     . PRO D 1 35  ? 30.769  20.270  35.801  1.00 43.62  ? 34  PRO C CB     1 
ATOM   8152  C  CG     . PRO D 1 35  ? 32.091  19.941  35.227  1.00 42.09  ? 34  PRO C CG     1 
ATOM   8153  C  CD     . PRO D 1 35  ? 32.078  18.506  34.811  1.00 42.70  ? 34  PRO C CD     1 
ATOM   8154  H  HA     . PRO D 1 35  ? 29.235  18.877  35.906  1.00 45.68  ? 34  PRO C HA     1 
ATOM   8155  H  HB2    . PRO D 1 35  ? 30.504  21.171  35.556  1.00 52.38  ? 34  PRO C HB2    1 
ATOM   8156  H  HB3    . PRO D 1 35  ? 30.782  20.179  36.767  1.00 52.38  ? 34  PRO C HB3    1 
ATOM   8157  H  HG2    . PRO D 1 35  ? 32.253  20.510  34.458  1.00 50.54  ? 34  PRO C HG2    1 
ATOM   8158  H  HG3    . PRO D 1 35  ? 32.774  20.088  35.899  1.00 50.54  ? 34  PRO C HG3    1 
ATOM   8159  H  HD2    . PRO D 1 35  ? 32.575  18.380  33.988  1.00 51.28  ? 34  PRO C HD2    1 
ATOM   8160  H  HD3    . PRO D 1 35  ? 32.443  17.941  35.509  1.00 51.28  ? 34  PRO C HD3    1 
ATOM   8161  N  N      . THR D 1 36  ? 27.704  20.341  34.589  1.00 35.70  ? 35  THR C N      1 
ATOM   8162  C  CA     . THR D 1 36  ? 26.622  20.676  33.663  1.00 36.66  ? 35  THR C CA     1 
ATOM   8163  C  C      . THR D 1 36  ? 26.626  22.146  33.276  1.00 33.99  ? 35  THR C C      1 
ATOM   8164  O  O      . THR D 1 36  ? 26.969  23.011  34.083  1.00 32.80  ? 35  THR C O      1 
ATOM   8165  C  CB     . THR D 1 36  ? 25.269  20.320  34.293  1.00 33.51  ? 35  THR C CB     1 
ATOM   8166  O  OG1    . THR D 1 36  ? 25.258  18.912  34.515  1.00 29.51  ? 35  THR C OG1    1 
ATOM   8167  C  CG2    . THR D 1 36  ? 24.101  20.720  33.340  1.00 32.07  ? 35  THR C CG2    1 
ATOM   8168  H  H      . THR D 1 36  ? 27.496  20.437  35.418  1.00 42.87  ? 35  THR C H      1 
ATOM   8169  H  HA     . THR D 1 36  ? 26.751  20.168  32.847  1.00 44.03  ? 35  THR C HA     1 
ATOM   8170  H  HB     . THR D 1 36  ? 25.135  20.795  35.128  1.00 40.24  ? 35  THR C HB     1 
ATOM   8171  H  HG21   . THR D 1 36  ? 23.279  20.291  33.625  1.00 38.51  ? 35  THR C HG21   1 
ATOM   8172  H  HG22   . THR D 1 36  ? 23.976  21.682  33.354  1.00 38.51  ? 35  THR C HG22   1 
ATOM   8173  H  HG23   . THR D 1 36  ? 24.303  20.442  32.433  1.00 38.51  ? 35  THR C HG23   1 
ATOM   8174  N  N      . ILE D 1 37  ? 26.256  22.419  32.027  1.00 33.60  ? 36  ILE C N      1 
ATOM   8175  C  CA     . ILE D 1 37  ? 25.958  23.780  31.589  1.00 32.63  ? 36  ILE C CA     1 
ATOM   8176  C  C      . ILE D 1 37  ? 24.453  23.955  31.713  1.00 31.55  ? 36  ILE C C      1 
ATOM   8177  O  O      . ILE D 1 37  ? 23.940  24.743  32.511  1.00 28.68  ? 36  ILE C O      1 
ATOM   8178  C  CB     . ILE D 1 37  ? 26.404  24.052  30.131  1.00 28.97  ? 36  ILE C CB     1 
ATOM   8179  C  CG1    . ILE D 1 37  ? 27.880  23.700  29.901  1.00 32.60  ? 36  ILE C CG1    1 
ATOM   8180  C  CG2    . ILE D 1 37  ? 26.089  25.526  29.790  1.00 24.82  ? 36  ILE C CG2    1 
ATOM   8181  C  CD1    . ILE D 1 37  ? 28.866  24.686  30.549  1.00 31.05  ? 36  ILE C CD1    1 
ATOM   8182  H  H      . ILE D 1 37  ? 26.169  21.827  31.408  1.00 40.36  ? 36  ILE C H      1 
ATOM   8183  H  HA     . ILE D 1 37  ? 26.434  24.410  32.152  1.00 39.19  ? 36  ILE C HA     1 
ATOM   8184  H  HB     . ILE D 1 37  ? 25.908  23.471  29.532  1.00 34.80  ? 36  ILE C HB     1 
ATOM   8185  H  HG12   . ILE D 1 37  ? 28.053  22.822  30.274  1.00 39.16  ? 36  ILE C HG12   1 
ATOM   8186  H  HG13   . ILE D 1 37  ? 28.053  23.694  28.946  1.00 39.16  ? 36  ILE C HG13   1 
ATOM   8187  H  HG21   . ILE D 1 37  ? 26.517  25.755  28.950  1.00 29.82  ? 36  ILE C HG21   1 
ATOM   8188  H  HG22   . ILE D 1 37  ? 25.128  25.634  29.712  1.00 29.82  ? 36  ILE C HG22   1 
ATOM   8189  H  HG23   . ILE D 1 37  ? 26.428  26.094  30.500  1.00 29.82  ? 36  ILE C HG23   1 
ATOM   8190  H  HD11   . ILE D 1 37  ? 29.768  24.343  30.449  1.00 37.29  ? 36  ILE C HD11   1 
ATOM   8191  H  HD12   . ILE D 1 37  ? 28.789  25.546  30.107  1.00 37.29  ? 36  ILE C HD12   1 
ATOM   8192  H  HD13   . ILE D 1 37  ? 28.649  24.777  31.490  1.00 37.29  ? 36  ILE C HD13   1 
ATOM   8193  N  N      . GLU D 1 38  ? 23.735  23.206  30.887  1.00 30.21  ? 37  GLU C N      1 
ATOM   8194  C  CA     . GLU D 1 38  ? 22.291  23.106  31.008  1.00 29.94  ? 37  GLU C CA     1 
ATOM   8195  C  C      . GLU D 1 38  ? 21.805  21.998  30.102  1.00 28.76  ? 37  GLU C C      1 
ATOM   8196  O  O      . GLU D 1 38  ? 22.194  21.958  28.943  1.00 28.37  ? 37  GLU C O      1 
ATOM   8197  C  CB     . GLU D 1 38  ? 21.619  24.395  30.614  1.00 26.98  ? 37  GLU C CB     1 
ATOM   8198  C  CG     . GLU D 1 38  ? 20.204  24.472  31.033  1.00 36.83  ? 37  GLU C CG     1 
ATOM   8199  C  CD     . GLU D 1 38  ? 19.515  25.573  30.305  1.00 40.60  ? 37  GLU C CD     1 
ATOM   8200  O  OE1    . GLU D 1 38  ? 19.762  26.753  30.635  1.00 46.08  ? 37  GLU C OE1    1 
ATOM   8201  O  OE2    . GLU D 1 38  ? 18.773  25.255  29.365  1.00 41.25  ? 37  GLU C OE2    1 
ATOM   8202  H  H      . GLU D 1 38  ? 24.066  22.741  30.243  1.00 36.28  ? 37  GLU C H      1 
ATOM   8203  H  HA     . GLU D 1 38  ? 22.057  22.921  31.931  1.00 35.96  ? 37  GLU C HA     1 
ATOM   8204  H  HB2    . GLU D 1 38  ? 22.092  25.134  31.027  1.00 32.40  ? 37  GLU C HB2    1 
ATOM   8205  H  HB3    . GLU D 1 38  ? 21.648  24.482  29.648  1.00 32.40  ? 37  GLU C HB3    1 
ATOM   8206  H  HG2    . GLU D 1 38  ? 19.757  23.636  30.828  1.00 44.22  ? 37  GLU C HG2    1 
ATOM   8207  H  HG3    . GLU D 1 38  ? 20.155  24.651  31.985  1.00 44.22  ? 37  GLU C HG3    1 
ATOM   8208  N  N      . ASP D 1 39  ? 20.929  21.120  30.603  1.00 26.60  ? 38  ASP C N      1 
ATOM   8209  C  CA     . ASP D 1 39  ? 20.395  20.060  29.774  1.00 25.32  ? 38  ASP C CA     1 
ATOM   8210  C  C      . ASP D 1 39  ? 18.919  19.884  30.080  1.00 24.89  ? 38  ASP C C      1 
ATOM   8211  O  O      . ASP D 1 39  ? 18.462  20.101  31.201  1.00 26.55  ? 38  ASP C O      1 
ATOM   8212  C  CB     . ASP D 1 39  ? 21.145  18.738  30.015  1.00 26.64  ? 38  ASP C CB     1 
ATOM   8213  C  CG     . ASP D 1 39  ? 22.569  18.786  29.476  1.00 32.51  ? 38  ASP C CG     1 
ATOM   8214  O  OD1    . ASP D 1 39  ? 22.716  18.662  28.256  1.00 33.79  ? 38  ASP C OD1    1 
ATOM   8215  O  OD2    . ASP D 1 39  ? 23.502  18.972  30.277  1.00 32.14  ? 38  ASP C OD2    1 
ATOM   8216  H  H      . ASP D 1 39  ? 20.638  21.126  31.412  1.00 31.95  ? 38  ASP C H      1 
ATOM   8217  H  HA     . ASP D 1 39  ? 20.483  20.296  28.837  1.00 30.41  ? 38  ASP C HA     1 
ATOM   8218  H  HB2    . ASP D 1 39  ? 21.187  18.563  30.968  1.00 32.00  ? 38  ASP C HB2    1 
ATOM   8219  H  HB3    . ASP D 1 39  ? 20.675  18.018  29.566  1.00 32.00  ? 38  ASP C HB3    1 
ATOM   8220  N  N      . SER D 1 40  ? 18.182  19.499  29.047  1.00 25.20  ? 39  SER C N      1 
ATOM   8221  C  CA     . SER D 1 40  ? 16.756  19.220  29.142  1.00 27.58  ? 39  SER C CA     1 
ATOM   8222  C  C      . SER D 1 40  ? 16.502  17.791  28.695  1.00 26.45  ? 39  SER C C      1 
ATOM   8223  O  O      . SER D 1 40  ? 17.123  17.315  27.740  1.00 22.57  ? 39  SER C O      1 
ATOM   8224  C  CB     . SER D 1 40  ? 15.964  20.175  28.241  1.00 31.63  ? 39  SER C CB     1 
ATOM   8225  O  OG     . SER D 1 40  ? 16.040  21.504  28.732  1.00 34.86  ? 39  SER C OG     1 
ATOM   8226  H  H      . SER D 1 40  ? 18.496  19.388  28.254  1.00 30.27  ? 39  SER C H      1 
ATOM   8227  H  HA     . SER D 1 40  ? 16.454  19.324  30.058  1.00 33.14  ? 39  SER C HA     1 
ATOM   8228  H  HB2    . SER D 1 40  ? 16.336  20.147  27.345  1.00 37.99  ? 39  SER C HB2    1 
ATOM   8229  H  HB3    . SER D 1 40  ? 15.035  19.896  28.223  1.00 37.99  ? 39  SER C HB3    1 
ATOM   8230  H  HG     . SER D 1 40  ? 15.604  22.020  28.232  1.00 41.87  ? 39  SER C HG     1 
ATOM   8231  N  N      . TYR D 1 41  ? 15.568  17.115  29.368  1.00 24.49  ? 40  TYR C N      1 
ATOM   8232  C  CA     . TYR D 1 41  ? 15.190  15.755  29.009  1.00 25.75  ? 40  TYR C CA     1 
ATOM   8233  C  C      . TYR D 1 41  ? 13.669  15.620  29.010  1.00 24.80  ? 40  TYR C C      1 
ATOM   8234  O  O      . TYR D 1 41  ? 12.961  16.393  29.660  1.00 25.27  ? 40  TYR C O      1 
ATOM   8235  C  CB     . TYR D 1 41  ? 15.788  14.744  29.993  1.00 25.81  ? 40  TYR C CB     1 
ATOM   8236  C  CG     . TYR D 1 41  ? 17.292  14.853  30.136  1.00 27.15  ? 40  TYR C CG     1 
ATOM   8237  C  CD1    . TYR D 1 41  ? 18.124  14.126  29.310  1.00 32.32  ? 40  TYR C CD1    1 
ATOM   8238  C  CD2    . TYR D 1 41  ? 17.868  15.674  31.120  1.00 25.72  ? 40  TYR C CD2    1 
ATOM   8239  C  CE1    . TYR D 1 41  ? 19.503  14.211  29.418  1.00 34.25  ? 40  TYR C CE1    1 
ATOM   8240  C  CE2    . TYR D 1 41  ? 19.239  15.766  31.234  1.00 29.89  ? 40  TYR C CE2    1 
ATOM   8241  C  CZ     . TYR D 1 41  ? 20.053  15.033  30.377  1.00 34.19  ? 40  TYR C CZ     1 
ATOM   8242  O  OH     . TYR D 1 41  ? 21.427  15.101  30.460  1.00 33.90  ? 40  TYR C OH     1 
ATOM   8243  H  H      . TYR D 1 41  ? 15.137  17.430  30.043  1.00 29.42  ? 40  TYR C H      1 
ATOM   8244  H  HA     . TYR D 1 41  ? 15.510  15.559  28.115  1.00 30.93  ? 40  TYR C HA     1 
ATOM   8245  H  HB2    . TYR D 1 41  ? 15.395  14.890  30.867  1.00 31.01  ? 40  TYR C HB2    1 
ATOM   8246  H  HB3    . TYR D 1 41  ? 15.583  13.848  29.682  1.00 31.01  ? 40  TYR C HB3    1 
ATOM   8247  H  HD1    . TYR D 1 41  ? 17.752  13.567  28.667  1.00 38.82  ? 40  TYR C HD1    1 
ATOM   8248  H  HD2    . TYR D 1 41  ? 17.322  16.157  31.697  1.00 30.89  ? 40  TYR C HD2    1 
ATOM   8249  H  HE1    . TYR D 1 41  ? 20.050  13.718  28.849  1.00 41.14  ? 40  TYR C HE1    1 
ATOM   8250  H  HE2    . TYR D 1 41  ? 19.618  16.316  31.881  1.00 35.91  ? 40  TYR C HE2    1 
ATOM   8251  H  HH     . TYR D 1 41  ? 21.654  15.757  30.934  1.00 40.72  ? 40  TYR C HH     1 
ATOM   8252  N  N      . ARG D 1 42  ? 13.188  14.622  28.255  1.00 22.25  ? 41  ARG C N      1 
ATOM   8253  C  CA     . ARG D 1 42  ? 11.767  14.297  28.119  1.00 23.79  ? 41  ARG C CA     1 
ATOM   8254  C  C      . ARG D 1 42  ? 11.612  12.803  28.397  1.00 23.07  ? 41  ARG C C      1 
ATOM   8255  O  O      . ARG D 1 42  ? 12.375  11.991  27.859  1.00 23.45  ? 41  ARG C O      1 
ATOM   8256  C  CB     . ARG D 1 42  ? 11.226  14.605  26.706  1.00 25.71  ? 41  ARG C CB     1 
ATOM   8257  C  CG     . ARG D 1 42  ? 11.057  16.082  26.332  1.00 32.94  ? 41  ARG C CG     1 
ATOM   8258  C  CD     . ARG D 1 42  ? 9.865   16.721  27.088  1.00 35.10  ? 41  ARG C CD     1 
ATOM   8259  N  NE     . ARG D 1 42  ? 9.095   17.644  26.254  1.00 37.44  ? 41  ARG C NE     1 
ATOM   8260  C  CZ     . ARG D 1 42  ? 8.346   17.255  25.232  1.00 30.40  ? 41  ARG C CZ     1 
ATOM   8261  N  NH1    . ARG D 1 42  ? 8.322   15.995  24.841  1.00 34.96  ? 41  ARG C NH1    1 
ATOM   8262  N  NH2    . ARG D 1 42  ? 7.618   18.145  24.587  1.00 38.02  ? 41  ARG C NH2    1 
ATOM   8263  H  H      . ARG D 1 42  ? 13.690  14.098  27.793  1.00 26.73  ? 41  ARG C H      1 
ATOM   8264  H  HA     . ARG D 1 42  ? 11.253  14.820  28.753  1.00 28.58  ? 41  ARG C HA     1 
ATOM   8265  H  HB2    . ARG D 1 42  ? 11.839  14.219  26.061  1.00 30.89  ? 41  ARG C HB2    1 
ATOM   8266  H  HB3    . ARG D 1 42  ? 10.353  14.191  26.623  1.00 30.89  ? 41  ARG C HB3    1 
ATOM   8267  H  HG2    . ARG D 1 42  ? 11.863  16.568  26.567  1.00 39.57  ? 41  ARG C HG2    1 
ATOM   8268  H  HG3    . ARG D 1 42  ? 10.890  16.157  25.380  1.00 39.57  ? 41  ARG C HG3    1 
ATOM   8269  H  HD2    . ARG D 1 42  ? 9.267   16.018  27.387  1.00 42.16  ? 41  ARG C HD2    1 
ATOM   8270  H  HD3    . ARG D 1 42  ? 10.203  17.216  27.850  1.00 42.16  ? 41  ARG C HD3    1 
ATOM   8271  H  HE     . ARG D 1 42  ? 9.129   18.484  26.438  1.00 44.97  ? 41  ARG C HE     1 
ATOM   8272  H  HH11   . ARG D 1 42  ? 8.797   15.408  25.252  1.00 41.99  ? 41  ARG C HH11   1 
ATOM   8273  H  HH12   . ARG D 1 42  ? 7.830   15.761  24.175  1.00 41.99  ? 41  ARG C HH12   1 
ATOM   8274  H  HH21   . ARG D 1 42  ? 7.632   18.969  24.830  1.00 45.66  ? 41  ARG C HH21   1 
ATOM   8275  H  HH22   . ARG D 1 42  ? 7.130   17.900  23.922  1.00 45.66  ? 41  ARG C HH22   1 
ATOM   8276  N  N      . LYS D 1 43  ? 10.629  12.432  29.206  1.00 22.35  ? 42  LYS C N      1 
ATOM   8277  C  CA     . LYS D 1 43  ? 10.319  11.032  29.429  1.00 24.80  ? 42  LYS C CA     1 
ATOM   8278  C  C      . LYS D 1 43  ? 8.831   10.865  29.734  1.00 24.17  ? 42  LYS C C      1 
ATOM   8279  O  O      . LYS D 1 43  ? 8.257   11.636  30.502  1.00 24.31  ? 42  LYS C O      1 
ATOM   8280  C  CB     . LYS D 1 43  ? 11.128  10.468  30.600  1.00 27.08  ? 42  LYS C CB     1 
ATOM   8281  C  CG     . LYS D 1 43  ? 10.946  8.982   30.846  1.00 29.55  ? 42  LYS C CG     1 
ATOM   8282  C  CD     . LYS D 1 43  ? 11.599  8.591   32.163  1.00 30.82  ? 42  LYS C CD     1 
ATOM   8283  C  CE     . LYS D 1 43  ? 11.481  7.112   32.463  1.00 41.49  ? 42  LYS C CE     1 
ATOM   8284  N  NZ     . LYS D 1 43  ? 12.693  6.391   32.014  1.00 46.41  ? 42  LYS C NZ     1 
ATOM   8285  H  H      . LYS D 1 43  ? 10.124  12.978  29.639  1.00 26.86  ? 42  LYS C H      1 
ATOM   8286  H  HA     . LYS D 1 43  ? 10.523  10.538  28.620  1.00 29.79  ? 42  LYS C HA     1 
ATOM   8287  H  HB2    . LYS D 1 43  ? 12.070  10.621  30.425  1.00 32.53  ? 42  LYS C HB2    1 
ATOM   8288  H  HB3    . LYS D 1 43  ? 10.862  10.932  31.409  1.00 32.53  ? 42  LYS C HB3    1 
ATOM   8289  H  HG2    . LYS D 1 43  ? 10.000  8.772   30.893  1.00 35.50  ? 42  LYS C HG2    1 
ATOM   8290  H  HG3    . LYS D 1 43  ? 11.363  8.478   30.130  1.00 35.50  ? 42  LYS C HG3    1 
ATOM   8291  H  HD2    . LYS D 1 43  ? 12.542  8.814   32.127  1.00 37.02  ? 42  LYS C HD2    1 
ATOM   8292  H  HD3    . LYS D 1 43  ? 11.170  9.077   32.885  1.00 37.02  ? 42  LYS C HD3    1 
ATOM   8293  H  HE2    . LYS D 1 43  ? 11.381  6.982   33.419  1.00 49.82  ? 42  LYS C HE2    1 
ATOM   8294  H  HE3    . LYS D 1 43  ? 10.713  6.746   31.996  1.00 49.82  ? 42  LYS C HE3    1 
ATOM   8295  H  HZ1    . LYS D 1 43  ? 13.408  6.699   32.446  1.00 55.73  ? 42  LYS C HZ1    1 
ATOM   8296  H  HZ2    . LYS D 1 43  ? 12.608  5.521   32.180  1.00 55.73  ? 42  LYS C HZ2    1 
ATOM   8297  H  HZ3    . LYS D 1 43  ? 12.810  6.509   31.140  1.00 55.73  ? 42  LYS C HZ3    1 
ATOM   8298  N  N      . GLN D 1 44  ? 8.215   9.850   29.140  1.00 26.21  ? 43  GLN C N      1 
ATOM   8299  C  CA     . GLN D 1 44  ? 6.835   9.518   29.483  1.00 25.42  ? 43  GLN C CA     1 
ATOM   8300  C  C      . GLN D 1 44  ? 6.858   8.413   30.519  1.00 27.72  ? 43  GLN C C      1 
ATOM   8301  O  O      . GLN D 1 44  ? 7.696   7.509   30.455  1.00 26.29  ? 43  GLN C O      1 
ATOM   8302  C  CB     . GLN D 1 44  ? 6.026   9.112   28.251  1.00 25.77  ? 43  GLN C CB     1 
ATOM   8303  C  CG     . GLN D 1 44  ? 6.438   7.869   27.512  1.00 24.17  ? 43  GLN C CG     1 
ATOM   8304  C  CD     . GLN D 1 44  ? 5.320   7.390   26.573  1.00 30.38  ? 43  GLN C CD     1 
ATOM   8305  O  OE1    . GLN D 1 44  ? 4.157   7.263   26.995  1.00 27.07  ? 43  GLN C OE1    1 
ATOM   8306  N  NE2    . GLN D 1 44  ? 5.657   7.151   25.307  1.00 23.92  ? 43  GLN C NE2    1 
ATOM   8307  H  H      . GLN D 1 44  ? 8.570   9.344   28.542  1.00 31.49  ? 43  GLN C H      1 
ATOM   8308  H  HA     . GLN D 1 44  ? 6.381   10.289  29.857  1.00 30.54  ? 43  GLN C HA     1 
ATOM   8309  H  HB2    . GLN D 1 44  ? 5.107   8.976   28.533  1.00 30.96  ? 43  GLN C HB2    1 
ATOM   8310  H  HB3    . GLN D 1 44  ? 6.072   9.842   27.614  1.00 30.96  ? 43  GLN C HB3    1 
ATOM   8311  H  HG2    . GLN D 1 44  ? 7.228   8.056   26.980  1.00 29.03  ? 43  GLN C HG2    1 
ATOM   8312  H  HG3    . GLN D 1 44  ? 6.628   7.162   28.149  1.00 29.03  ? 43  GLN C HG3    1 
ATOM   8313  H  HE21   . GLN D 1 44  ? 6.470   7.266   25.050  1.00 28.74  ? 43  GLN C HE21   1 
ATOM   8314  H  HE22   . GLN D 1 44  ? 5.063   6.882   24.748  1.00 28.74  ? 43  GLN C HE22   1 
ATOM   8315  N  N      . VAL D 1 45  ? 5.956   8.521   31.496  1.00 26.74  ? 44  VAL C N      1 
ATOM   8316  C  CA     . VAL D 1 45  ? 5.840   7.625   32.633  1.00 29.61  ? 44  VAL C CA     1 
ATOM   8317  C  C      . VAL D 1 45  ? 4.362   7.524   32.996  1.00 33.80  ? 44  VAL C C      1 
ATOM   8318  O  O      . VAL D 1 45  ? 3.528   8.297   32.525  1.00 31.14  ? 44  VAL C O      1 
ATOM   8319  C  CB     . VAL D 1 45  ? 6.643   8.146   33.840  1.00 30.90  ? 44  VAL C CB     1 
ATOM   8320  C  CG1    . VAL D 1 45  ? 8.117   8.229   33.467  1.00 34.07  ? 44  VAL C CG1    1 
ATOM   8321  C  CG2    . VAL D 1 45  ? 6.108   9.513   34.264  1.00 29.41  ? 44  VAL C CG2    1 
ATOM   8322  H  H      . VAL D 1 45  ? 5.366   9.147   31.518  1.00 32.13  ? 44  VAL C H      1 
ATOM   8323  H  HA     . VAL D 1 45  ? 6.163   6.742   32.394  1.00 35.57  ? 44  VAL C HA     1 
ATOM   8324  H  HB     . VAL D 1 45  ? 6.551   7.541   34.593  1.00 37.12  ? 44  VAL C HB     1 
ATOM   8325  H  HG11   . VAL D 1 45  ? 8.636   8.404   34.268  1.00 40.91  ? 44  VAL C HG11   1 
ATOM   8326  H  HG12   . VAL D 1 45  ? 8.391   7.387   33.073  1.00 40.91  ? 44  VAL C HG12   1 
ATOM   8327  H  HG13   . VAL D 1 45  ? 8.241   8.949   32.829  1.00 40.91  ? 44  VAL C HG13   1 
ATOM   8328  H  HG21   . VAL D 1 45  ? 6.706   9.894   34.926  1.00 35.33  ? 44  VAL C HG21   1 
ATOM   8329  H  HG22   . VAL D 1 45  ? 6.064   10.090  33.486  1.00 35.33  ? 44  VAL C HG22   1 
ATOM   8330  H  HG23   . VAL D 1 45  ? 5.223   9.401   34.644  1.00 35.33  ? 44  VAL C HG23   1 
ATOM   8331  N  N      . VAL D 1 46  ? 4.035   6.561   33.842  1.00 32.83  ? 45  VAL C N      1 
ATOM   8332  C  CA     . VAL D 1 46  ? 2.710   6.468   34.431  1.00 34.01  ? 45  VAL C CA     1 
ATOM   8333  C  C      . VAL D 1 46  ? 2.891   6.630   35.931  1.00 33.81  ? 45  VAL C C      1 
ATOM   8334  O  O      . VAL D 1 46  ? 3.676   5.900   36.542  1.00 36.30  ? 45  VAL C O      1 
ATOM   8335  C  CB     . VAL D 1 46  ? 2.026   5.140   34.085  1.00 36.45  ? 45  VAL C CB     1 
ATOM   8336  C  CG1    . VAL D 1 46  ? 0.594   5.124   34.633  1.00 34.93  ? 45  VAL C CG1    1 
ATOM   8337  C  CG2    . VAL D 1 46  ? 2.012   4.958   32.608  1.00 34.44  ? 45  VAL C CG2    1 
ATOM   8338  H  H      . VAL D 1 46  ? 4.573   5.938   34.093  1.00 39.43  ? 45  VAL C H      1 
ATOM   8339  H  HA     . VAL D 1 46  ? 2.142   7.183   34.105  1.00 40.84  ? 45  VAL C HA     1 
ATOM   8340  H  HB     . VAL D 1 46  ? 2.515   4.406   34.489  1.00 43.77  ? 45  VAL C HB     1 
ATOM   8341  H  HG11   . VAL D 1 46  ? 0.188   4.266   34.431  1.00 41.95  ? 45  VAL C HG11   1 
ATOM   8342  H  HG12   . VAL D 1 46  ? 0.623   5.257   35.594  1.00 41.95  ? 45  VAL C HG12   1 
ATOM   8343  H  HG13   . VAL D 1 46  ? 0.088   5.837   34.215  1.00 41.95  ? 45  VAL C HG13   1 
ATOM   8344  H  HG21   . VAL D 1 46  ? 1.463   4.189   32.390  1.00 41.37  ? 45  VAL C HG21   1 
ATOM   8345  H  HG22   . VAL D 1 46  ? 1.644   5.755   32.196  1.00 41.37  ? 45  VAL C HG22   1 
ATOM   8346  H  HG23   . VAL D 1 46  ? 2.920   4.815   32.299  1.00 41.37  ? 45  VAL C HG23   1 
ATOM   8347  N  N      . ILE D 1 47  ? 2.213   7.612   36.504  1.00 31.06  ? 46  ILE C N      1 
ATOM   8348  C  CA     . ILE D 1 47  ? 2.275   7.901   37.930  1.00 30.63  ? 46  ILE C CA     1 
ATOM   8349  C  C      . ILE D 1 47  ? 0.850   7.850   38.444  1.00 38.34  ? 46  ILE C C      1 
ATOM   8350  O  O      . ILE D 1 47  ? -0.018  8.593   37.960  1.00 38.87  ? 46  ILE C O      1 
ATOM   8351  C  CB     . ILE D 1 47  ? 2.917   9.265   38.220  1.00 37.21  ? 46  ILE C CB     1 
ATOM   8352  C  CG1    . ILE D 1 47  ? 4.376   9.263   37.763  1.00 34.42  ? 46  ILE C CG1    1 
ATOM   8353  C  CG2    . ILE D 1 47  ? 2.826   9.574   39.705  1.00 37.43  ? 46  ILE C CG2    1 
ATOM   8354  C  CD1    . ILE D 1 47  ? 4.966   10.677  37.582  1.00 37.42  ? 46  ILE C CD1    1 
ATOM   8355  H  H      . ILE D 1 47  ? 1.692   8.144   36.073  1.00 37.30  ? 46  ILE C H      1 
ATOM   8356  H  HA     . ILE D 1 47  ? 2.806   7.226   38.382  1.00 36.78  ? 46  ILE C HA     1 
ATOM   8357  H  HB     . ILE D 1 47  ? 2.439   9.950   37.728  1.00 44.69  ? 46  ILE C HB     1 
ATOM   8358  H  HG12   . ILE D 1 47  ? 4.912   8.800   38.426  1.00 41.34  ? 46  ILE C HG12   1 
ATOM   8359  H  HG13   . ILE D 1 47  ? 4.436   8.805   36.910  1.00 41.34  ? 46  ILE C HG13   1 
ATOM   8360  H  HG21   . ILE D 1 47  ? 3.431   10.303  39.913  1.00 44.95  ? 46  ILE C HG21   1 
ATOM   8361  H  HG22   . ILE D 1 47  ? 1.915   9.828   39.919  1.00 44.95  ? 46  ILE C HG22   1 
ATOM   8362  H  HG23   . ILE D 1 47  ? 3.076   8.783   40.208  1.00 44.95  ? 46  ILE C HG23   1 
ATOM   8363  H  HD11   . ILE D 1 47  ? 5.860   10.602  37.212  1.00 44.94  ? 46  ILE C HD11   1 
ATOM   8364  H  HD12   . ILE D 1 47  ? 4.399   11.180  36.976  1.00 44.94  ? 46  ILE C HD12   1 
ATOM   8365  H  HD13   . ILE D 1 47  ? 5.001   11.118  38.445  1.00 44.94  ? 46  ILE C HD13   1 
ATOM   8366  N  N      . ASP D 1 48  ? 0.607   6.948   39.385  1.00 38.49  ? 47  ASP C N      1 
ATOM   8367  C  CA     . ASP D 1 48  ? -0.711  6.797   40.006  1.00 39.08  ? 47  ASP C CA     1 
ATOM   8368  C  C      . ASP D 1 48  ? -1.778  6.613   38.934  1.00 39.70  ? 47  ASP C C      1 
ATOM   8369  O  O      . ASP D 1 48  ? -2.882  7.152   39.013  1.00 43.86  ? 47  ASP C O      1 
ATOM   8370  C  CB     . ASP D 1 48  ? -1.002  7.990   40.918  1.00 35.50  ? 47  ASP C CB     1 
ATOM   8371  C  CG     . ASP D 1 48  ? -0.042  8.062   42.064  1.00 39.51  ? 47  ASP C CG     1 
ATOM   8372  O  OD1    . ASP D 1 48  ? 0.483   6.994   42.441  1.00 36.48  ? 47  ASP C OD1    1 
ATOM   8373  O  OD2    . ASP D 1 48  ? 0.172   9.165   42.617  1.00 43.71  ? 47  ASP C OD2    1 
ATOM   8374  H  H      . ASP D 1 48  ? 1.196   6.400   39.689  1.00 46.22  ? 47  ASP C H      1 
ATOM   8375  H  HA     . ASP D 1 48  ? -0.730  6.002   40.561  1.00 46.92  ? 47  ASP C HA     1 
ATOM   8376  H  HB2    . ASP D 1 48  ? -0.926  8.810   40.406  1.00 42.63  ? 47  ASP C HB2    1 
ATOM   8377  H  HB3    . ASP D 1 48  ? -1.899  7.906   41.279  1.00 42.63  ? 47  ASP C HB3    1 
ATOM   8378  N  N      . GLY D 1 49  ? -1.429  5.828   37.921  1.00 37.61  ? 48  GLY C N      1 
ATOM   8379  C  CA     . GLY D 1 49  ? -2.328  5.436   36.864  1.00 38.95  ? 48  GLY C CA     1 
ATOM   8380  C  C      . GLY D 1 49  ? -2.497  6.406   35.716  1.00 40.26  ? 48  GLY C C      1 
ATOM   8381  O  O      . GLY D 1 49  ? -3.254  6.104   34.790  1.00 41.88  ? 48  GLY C O      1 
ATOM   8382  H  H      . GLY D 1 49  ? -0.640  5.499   37.825  1.00 45.17  ? 48  GLY C H      1 
ATOM   8383  H  HA2    . GLY D 1 49  ? -2.009  4.600   36.489  1.00 46.78  ? 48  GLY C HA2    1 
ATOM   8384  H  HA3    . GLY D 1 49  ? -3.206  5.293   37.251  1.00 46.78  ? 48  GLY C HA3    1 
ATOM   8385  N  N      . GLU D 1 50  ? -1.835  7.558   35.730  1.00 38.10  ? 49  GLU C N      1 
ATOM   8386  C  CA     . GLU D 1 50  ? -2.044  8.583   34.725  1.00 39.29  ? 49  GLU C CA     1 
ATOM   8387  C  C      . GLU D 1 50  ? -0.746  8.721   33.923  1.00 39.36  ? 49  GLU C C      1 
ATOM   8388  O  O      . GLU D 1 50  ? 0.329   8.933   34.499  1.00 37.12  ? 49  GLU C O      1 
ATOM   8389  C  CB     . GLU D 1 50  ? -2.456  9.914   35.359  1.00 45.29  ? 49  GLU C CB     1 
ATOM   8390  C  CG     . GLU D 1 50  ? -2.526  11.075  34.348  1.00 50.55  ? 49  GLU C CG     1 
ATOM   8391  C  CD     . GLU D 1 50  ? -3.801  11.909  34.474  1.00 56.00  ? 49  GLU C CD     1 
ATOM   8392  O  OE1    . GLU D 1 50  ? -4.897  11.380  34.182  1.00 61.68  ? 49  GLU C OE1    1 
ATOM   8393  O  OE2    . GLU D 1 50  ? -3.709  13.102  34.838  1.00 61.55  ? 49  GLU C OE2    1 
ATOM   8394  H  H      . GLU D 1 50  ? -1.250  7.768   36.324  1.00 45.75  ? 49  GLU C H      1 
ATOM   8395  H  HA     . GLU D 1 50  ? -2.758  8.321   34.122  1.00 47.19  ? 49  GLU C HA     1 
ATOM   8396  H  HB2    . GLU D 1 50  ? -3.334  9.812   35.757  1.00 54.39  ? 49  GLU C HB2    1 
ATOM   8397  H  HB3    . GLU D 1 50  ? -1.808  10.150  36.040  1.00 54.39  ? 49  GLU C HB3    1 
ATOM   8398  H  HG2    . GLU D 1 50  ? -1.769  11.664  34.494  1.00 60.69  ? 49  GLU C HG2    1 
ATOM   8399  H  HG3    . GLU D 1 50  ? -2.496  10.711  33.450  1.00 60.69  ? 49  GLU C HG3    1 
ATOM   8400  N  N      . THR D 1 51  ? -0.841  8.559   32.610  1.00 39.50  ? 50  THR C N      1 
ATOM   8401  C  CA     . THR D 1 51  ? 0.329   8.756   31.761  1.00 35.08  ? 50  THR C CA     1 
ATOM   8402  C  C      . THR D 1 51  ? 0.650   10.239  31.731  1.00 38.93  ? 50  THR C C      1 
ATOM   8403  O  O      . THR D 1 51  ? -0.250  11.065  31.583  1.00 39.28  ? 50  THR C O      1 
ATOM   8404  C  CB     . THR D 1 51  ? 0.072   8.235   30.353  1.00 34.03  ? 50  THR C CB     1 
ATOM   8405  O  OG1    . THR D 1 51  ? -0.199  6.825   30.429  1.00 36.66  ? 50  THR C OG1    1 
ATOM   8406  C  CG2    . THR D 1 51  ? 1.276   8.486   29.465  1.00 36.16  ? 50  THR C CG2    1 
ATOM   8407  H  H      . THR D 1 51  ? -1.559  8.339   32.191  1.00 47.43  ? 50  THR C H      1 
ATOM   8408  H  HA     . THR D 1 51  ? 1.087   8.263   32.112  1.00 42.13  ? 50  THR C HA     1 
ATOM   8409  H  HB     . THR D 1 51  ? -0.685  8.693   29.955  1.00 40.86  ? 50  THR C HB     1 
ATOM   8410  H  HG1    . THR D 1 51  ? -0.310  6.512   29.658  1.00 44.03  ? 50  THR C HG1    1 
ATOM   8411  H  HG21   . THR D 1 51  ? 1.201   7.967   28.649  1.00 43.43  ? 50  THR C HG21   1 
ATOM   8412  H  HG22   . THR D 1 51  ? 1.329   9.427   29.236  1.00 43.43  ? 50  THR C HG22   1 
ATOM   8413  H  HG23   . THR D 1 51  ? 2.089   8.228   29.928  1.00 43.43  ? 50  THR C HG23   1 
ATOM   8414  N  N      . CYS D 1 52  ? 1.925   10.591  31.922  1.00 32.55  ? 51  CYS C N      1 
ATOM   8415  C  CA     . CYS D 1 52  ? 2.317   11.979  31.760  1.00 35.94  ? 51  CYS C CA     1 
ATOM   8416  C  C      . CYS D 1 52  ? 3.697   12.073  31.137  1.00 31.61  ? 51  CYS C C      1 
ATOM   8417  O  O      . CYS D 1 52  ? 4.460   11.100  31.115  1.00 26.76  ? 51  CYS C O      1 
ATOM   8418  C  CB     . CYS D 1 52  ? 2.342   12.725  33.074  1.00 38.39  ? 51  CYS C CB     1 
ATOM   8419  S  SG     . CYS D 1 52  ? 3.275   11.887  34.270  1.00 45.53  ? 51  CYS C SG     1 
ATOM   8420  H  H      . CYS D 1 52  ? 2.560   10.053  32.141  1.00 39.09  ? 51  CYS C H      1 
ATOM   8421  H  HA     . CYS D 1 52  ? 1.673   12.392  31.164  1.00 43.16  ? 51  CYS C HA     1 
ATOM   8422  H  HB2    . CYS D 1 52  ? 2.738   13.600  32.936  1.00 46.10  ? 51  CYS C HB2    1 
ATOM   8423  H  HB3    . CYS D 1 52  ? 1.436   12.819  33.405  1.00 46.10  ? 51  CYS C HB3    1 
ATOM   8424  H  HG     . CYS D 1 52  ? 3.176   12.464  35.317  1.00 54.67  ? 51  CYS C HG     1 
ATOM   8425  N  N      . LEU D 1 53  ? 3.998   13.281  30.674  1.00 31.38  ? 52  LEU C N      1 
ATOM   8426  C  CA     . LEU D 1 53  ? 5.262   13.639  30.019  1.00 26.88  ? 52  LEU C CA     1 
ATOM   8427  C  C      . LEU D 1 53  ? 6.053   14.486  31.006  1.00 34.32  ? 52  LEU C C      1 
ATOM   8428  O  O      . LEU D 1 53  ? 5.582   15.537  31.451  1.00 35.91  ? 52  LEU C O      1 
ATOM   8429  C  CB     . LEU D 1 53  ? 4.996   14.390  28.730  1.00 32.42  ? 52  LEU C CB     1 
ATOM   8430  C  CG     . LEU D 1 53  ? 6.165   14.551  27.762  1.00 31.65  ? 52  LEU C CG     1 
ATOM   8431  C  CD1    . LEU D 1 53  ? 6.867   13.235  27.485  1.00 28.04  ? 52  LEU C CD1    1 
ATOM   8432  C  CD2    . LEU D 1 53  ? 5.630   15.163  26.463  1.00 34.65  ? 52  LEU C CD2    1 
ATOM   8433  H  H      . LEU D 1 53  ? 3.459   13.949  30.729  1.00 37.69  ? 52  LEU C H      1 
ATOM   8434  H  HA     . LEU D 1 53  ? 5.781   12.850  29.797  1.00 32.30  ? 52  LEU C HA     1 
ATOM   8435  H  HB2    . LEU D 1 53  ? 4.296   13.920  28.250  1.00 38.94  ? 52  LEU C HB2    1 
ATOM   8436  H  HB3    . LEU D 1 53  ? 4.697   15.283  28.962  1.00 38.94  ? 52  LEU C HB3    1 
ATOM   8437  H  HG     . LEU D 1 53  ? 6.833   15.134  28.156  1.00 38.01  ? 52  LEU C HG     1 
ATOM   8438  H  HD11   . LEU D 1 53  ? 7.467   13.349  26.732  1.00 33.68  ? 52  LEU C HD11   1 
ATOM   8439  H  HD12   . LEU D 1 53  ? 7.370   12.974  28.272  1.00 33.68  ? 52  LEU C HD12   1 
ATOM   8440  H  HD13   . LEU D 1 53  ? 6.202   12.560  27.278  1.00 33.68  ? 52  LEU C HD13   1 
ATOM   8441  H  HD21   . LEU D 1 53  ? 6.282   15.026  25.758  1.00 41.62  ? 52  LEU C HD21   1 
ATOM   8442  H  HD22   . LEU D 1 53  ? 4.795   14.728  26.230  1.00 41.62  ? 52  LEU C HD22   1 
ATOM   8443  H  HD23   . LEU D 1 53  ? 5.483   16.112  26.599  1.00 41.62  ? 52  LEU C HD23   1 
ATOM   8444  N  N      . LEU D 1 54  ? 7.224   14.002  31.396  1.00 31.79  ? 53  LEU C N      1 
ATOM   8445  C  CA     . LEU D 1 54  ? 8.105   14.789  32.255  1.00 27.56  ? 53  LEU C CA     1 
ATOM   8446  C  C      . LEU D 1 54  ? 9.086   15.548  31.379  1.00 29.99  ? 53  LEU C C      1 
ATOM   8447  O  O      . LEU D 1 54  ? 9.710   14.963  30.495  1.00 28.71  ? 53  LEU C O      1 
ATOM   8448  C  CB     . LEU D 1 54  ? 8.856   13.898  33.225  1.00 28.89  ? 53  LEU C CB     1 
ATOM   8449  C  CG     . LEU D 1 54  ? 7.973   12.975  34.070  1.00 33.90  ? 53  LEU C CG     1 
ATOM   8450  C  CD1    . LEU D 1 54  ? 8.761   12.194  35.093  1.00 33.49  ? 53  LEU C CD1    1 
ATOM   8451  C  CD2    . LEU D 1 54  ? 6.897   13.782  34.781  1.00 36.10  ? 53  LEU C CD2    1 
ATOM   8452  H  H      . LEU D 1 54  ? 7.530   13.229  31.180  1.00 38.18  ? 53  LEU C H      1 
ATOM   8453  H  HA     . LEU D 1 54  ? 7.582   15.418  32.776  1.00 33.11  ? 53  LEU C HA     1 
ATOM   8454  H  HB2    . LEU D 1 54  ? 9.463   13.337  32.719  1.00 34.70  ? 53  LEU C HB2    1 
ATOM   8455  H  HB3    . LEU D 1 54  ? 9.356   14.462  33.836  1.00 34.70  ? 53  LEU C HB3    1 
ATOM   8456  H  HG     . LEU D 1 54  ? 7.564   12.336  33.465  1.00 40.72  ? 53  LEU C HG     1 
ATOM   8457  H  HD11   . LEU D 1 54  ? 8.158   11.611  35.579  1.00 40.22  ? 53  LEU C HD11   1 
ATOM   8458  H  HD12   . LEU D 1 54  ? 9.435   11.666  34.636  1.00 40.22  ? 53  LEU C HD12   1 
ATOM   8459  H  HD13   . LEU D 1 54  ? 9.187   12.814  35.705  1.00 40.22  ? 53  LEU C HD13   1 
ATOM   8460  H  HD21   . LEU D 1 54  ? 6.443   13.209  35.419  1.00 43.35  ? 53  LEU C HD21   1 
ATOM   8461  H  HD22   . LEU D 1 54  ? 7.314   14.526  35.242  1.00 43.35  ? 53  LEU C HD22   1 
ATOM   8462  H  HD23   . LEU D 1 54  ? 6.264   14.112  34.124  1.00 43.35  ? 53  LEU C HD23   1 
ATOM   8463  N  N      . ASP D 1 55  ? 9.174   16.858  31.602  1.00 30.07  ? 54  ASP C N      1 
ATOM   8464  C  CA     . ASP D 1 55  ? 10.150  17.744  30.970  1.00 28.23  ? 54  ASP C CA     1 
ATOM   8465  C  C      . ASP D 1 55  ? 11.056  18.184  32.104  1.00 33.02  ? 54  ASP C C      1 
ATOM   8466  O  O      . ASP D 1 55  ? 10.599  18.825  33.061  1.00 31.50  ? 54  ASP C O      1 
ATOM   8467  C  CB     . ASP D 1 55  ? 9.473   18.916  30.282  1.00 33.61  ? 54  ASP C CB     1 
ATOM   8468  C  CG     . ASP D 1 55  ? 10.461  19.792  29.577  1.00 36.29  ? 54  ASP C CG     1 
ATOM   8469  O  OD1    . ASP D 1 55  ? 11.286  20.411  30.278  1.00 38.28  ? 54  ASP C OD1    1 
ATOM   8470  O  OD2    . ASP D 1 55  ? 10.454  19.820  28.335  1.00 39.54  ? 54  ASP C OD2    1 
ATOM   8471  H  H      . ASP D 1 55  ? 8.653   17.277  32.143  1.00 36.12  ? 54  ASP C H      1 
ATOM   8472  H  HA     . ASP D 1 55  ? 10.664  17.291  30.283  1.00 33.91  ? 54  ASP C HA     1 
ATOM   8473  H  HB2    . ASP D 1 55  ? 8.841   18.581  29.626  1.00 40.36  ? 54  ASP C HB2    1 
ATOM   8474  H  HB3    . ASP D 1 55  ? 9.010   19.452  30.945  1.00 40.36  ? 54  ASP C HB3    1 
ATOM   8475  N  N      . ILE D 1 56  ? 12.295  17.725  32.078  1.00 27.74  ? 55  ILE C N      1 
ATOM   8476  C  CA     . ILE D 1 56  ? 13.197  17.854  33.208  1.00 30.56  ? 55  ILE C CA     1 
ATOM   8477  C  C      . ILE D 1 56  ? 14.350  18.745  32.789  1.00 30.18  ? 55  ILE C C      1 
ATOM   8478  O  O      . ILE D 1 56  ? 14.989  18.485  31.772  1.00 25.53  ? 55  ILE C O      1 
ATOM   8479  C  CB     . ILE D 1 56  ? 13.707  16.487  33.674  1.00 29.18  ? 55  ILE C CB     1 
ATOM   8480  C  CG1    . ILE D 1 56  ? 12.495  15.611  34.066  1.00 31.67  ? 55  ILE C CG1    1 
ATOM   8481  C  CG2    . ILE D 1 56  ? 14.656  16.626  34.852  1.00 30.25  ? 55  ILE C CG2    1 
ATOM   8482  C  CD1    . ILE D 1 56  ? 12.855  14.220  34.347  1.00 34.40  ? 55  ILE C CD1    1 
ATOM   8483  H  H      . ILE D 1 56  ? 12.644  17.325  31.401  1.00 33.32  ? 55  ILE C H      1 
ATOM   8484  H  HA     . ILE D 1 56  ? 12.735  18.278  33.948  1.00 36.71  ? 55  ILE C HA     1 
ATOM   8485  H  HB     . ILE D 1 56  ? 14.197  16.071  32.948  1.00 35.05  ? 55  ILE C HB     1 
ATOM   8486  H  HG12   . ILE D 1 56  ? 12.086  15.980  34.864  1.00 38.04  ? 55  ILE C HG12   1 
ATOM   8487  H  HG13   . ILE D 1 56  ? 11.857  15.612  33.335  1.00 38.04  ? 55  ILE C HG13   1 
ATOM   8488  H  HG21   . ILE D 1 56  ? 14.913  15.742  35.157  1.00 36.33  ? 55  ILE C HG21   1 
ATOM   8489  H  HG22   . ILE D 1 56  ? 15.441  17.120  34.568  1.00 36.33  ? 55  ILE C HG22   1 
ATOM   8490  H  HG23   . ILE D 1 56  ? 14.205  17.104  35.566  1.00 36.33  ? 55  ILE C HG23   1 
ATOM   8491  H  HD11   . ILE D 1 56  ? 12.052  13.675  34.325  1.00 41.32  ? 55  ILE C HD11   1 
ATOM   8492  H  HD12   . ILE D 1 56  ? 13.480  13.913  33.672  1.00 41.32  ? 55  ILE C HD12   1 
ATOM   8493  H  HD13   . ILE D 1 56  ? 13.264  14.170  35.225  1.00 41.32  ? 55  ILE C HD13   1 
ATOM   8494  N  N      . LEU D 1 57  ? 14.619  19.768  33.583  1.00 28.59  ? 56  LEU C N      1 
ATOM   8495  C  CA     . LEU D 1 57  ? 15.714  20.695  33.341  1.00 29.06  ? 56  LEU C CA     1 
ATOM   8496  C  C      . LEU D 1 57  ? 16.782  20.439  34.385  1.00 30.66  ? 56  LEU C C      1 
ATOM   8497  O  O      . LEU D 1 57  ? 16.515  20.552  35.585  1.00 32.38  ? 56  LEU C O      1 
ATOM   8498  C  CB     . LEU D 1 57  ? 15.209  22.135  33.381  1.00 34.93  ? 56  LEU C CB     1 
ATOM   8499  C  CG     . LEU D 1 57  ? 16.286  23.212  33.214  1.00 35.19  ? 56  LEU C CG     1 
ATOM   8500  C  CD1    . LEU D 1 57  ? 16.866  23.098  31.797  1.00 36.81  ? 56  LEU C CD1    1 
ATOM   8501  C  CD2    . LEU D 1 57  ? 15.738  24.604  33.489  1.00 39.38  ? 56  LEU C CD2    1 
ATOM   8502  H  H      . LEU D 1 57  ? 14.168  19.952  34.291  1.00 34.34  ? 56  LEU C H      1 
ATOM   8503  H  HA     . LEU D 1 57  ? 16.108  20.548  32.467  1.00 34.91  ? 56  LEU C HA     1 
ATOM   8504  H  HB2    . LEU D 1 57  ? 14.567  22.253  32.664  1.00 41.95  ? 56  LEU C HB2    1 
ATOM   8505  H  HB3    . LEU D 1 57  ? 14.781  22.284  34.239  1.00 41.95  ? 56  LEU C HB3    1 
ATOM   8506  H  HG     . LEU D 1 57  ? 16.996  23.077  33.861  1.00 42.26  ? 56  LEU C HG     1 
ATOM   8507  H  HD11   . LEU D 1 57  ? 17.465  23.845  31.640  1.00 44.20  ? 56  LEU C HD11   1 
ATOM   8508  H  HD12   . LEU D 1 57  ? 17.352  22.262  31.720  1.00 44.20  ? 56  LEU C HD12   1 
ATOM   8509  H  HD13   . LEU D 1 57  ? 16.138  23.117  31.155  1.00 44.20  ? 56  LEU C HD13   1 
ATOM   8510  H  HD21   . LEU D 1 57  ? 16.433  25.257  33.315  1.00 47.28  ? 56  LEU C HD21   1 
ATOM   8511  H  HD22   . LEU D 1 57  ? 14.979  24.765  32.907  1.00 47.28  ? 56  LEU C HD22   1 
ATOM   8512  H  HD23   . LEU D 1 57  ? 15.461  24.656  34.417  1.00 47.28  ? 56  LEU C HD23   1 
ATOM   8513  N  N      . ASP D 1 58  ? 17.967  20.050  33.924  1.00 25.18  ? 57  ASP C N      1 
ATOM   8514  C  CA     . ASP D 1 58  ? 19.112  19.697  34.749  1.00 29.32  ? 57  ASP C CA     1 
ATOM   8515  C  C      . ASP D 1 58  ? 20.063  20.885  34.715  1.00 32.01  ? 57  ASP C C      1 
ATOM   8516  O  O      . ASP D 1 58  ? 20.577  21.234  33.650  1.00 31.17  ? 57  ASP C O      1 
ATOM   8517  C  CB     . ASP D 1 58  ? 19.800  18.450  34.192  1.00 31.29  ? 57  ASP C CB     1 
ATOM   8518  C  CG     . ASP D 1 58  ? 21.016  18.031  35.019  1.00 33.62  ? 57  ASP C CG     1 
ATOM   8519  O  OD1    . ASP D 1 58  ? 21.073  18.401  36.193  1.00 31.54  ? 57  ASP C OD1    1 
ATOM   8520  O  OD2    . ASP D 1 58  ? 21.870  17.295  34.473  1.00 31.51  ? 57  ASP C OD2    1 
ATOM   8521  H  H      . ASP D 1 58  ? 18.141  19.980  33.085  1.00 30.25  ? 57  ASP C H      1 
ATOM   8522  H  HA     . ASP D 1 58  ? 18.842  19.514  35.663  1.00 35.22  ? 57  ASP C HA     1 
ATOM   8523  H  HB2    . ASP D 1 58  ? 19.169  17.713  34.191  1.00 37.58  ? 57  ASP C HB2    1 
ATOM   8524  H  HB3    . ASP D 1 58  ? 20.100  18.631  33.287  1.00 37.58  ? 57  ASP C HB3    1 
ATOM   8525  N  N      . THR D 1 59  ? 20.322  21.473  35.876  1.00 33.45  ? 58  THR C N      1 
ATOM   8526  C  CA     . THR D 1 59  ? 21.040  22.732  35.957  1.00 35.19  ? 58  THR C CA     1 
ATOM   8527  C  C      . THR D 1 59  ? 22.412  22.541  36.585  1.00 35.85  ? 58  THR C C      1 
ATOM   8528  O  O      . THR D 1 59  ? 22.745  21.476  37.150  1.00 35.88  ? 58  THR C O      1 
ATOM   8529  C  CB     . THR D 1 59  ? 20.238  23.743  36.762  1.00 37.28  ? 58  THR C CB     1 
ATOM   8530  O  OG1    . THR D 1 59  ? 20.355  23.413  38.152  1.00 37.76  ? 58  THR C OG1    1 
ATOM   8531  C  CG2    . THR D 1 59  ? 18.770  23.683  36.341  1.00 39.42  ? 58  THR C CG2    1 
ATOM   8532  H  H      . THR D 1 59  ? 20.087  21.156  36.639  1.00 40.17  ? 58  THR C H      1 
ATOM   8533  H  HA     . THR D 1 59  ? 21.174  23.073  35.059  1.00 42.26  ? 58  THR C HA     1 
ATOM   8534  H  HB     . THR D 1 59  ? 20.564  24.644  36.611  1.00 44.77  ? 58  THR C HB     1 
ATOM   8535  H  HG1    . THR D 1 59  ? 20.091  22.626  38.284  1.00 45.35  ? 58  THR C HG1    1 
ATOM   8536  H  HG21   . THR D 1 59  ? 18.298  24.464  36.670  1.00 47.34  ? 58  THR C HG21   1 
ATOM   8537  H  HG22   . THR D 1 59  ? 18.703  23.660  35.374  1.00 47.34  ? 58  THR C HG22   1 
ATOM   8538  H  HG23   . THR D 1 59  ? 18.352  22.887  36.705  1.00 47.34  ? 58  THR C HG23   1 
ATOM   8539  N  N      . ALA D 1 60  ? 23.205  23.604  36.456  1.00 39.89  ? 59  ALA C N      1 
ATOM   8540  C  CA     . ALA D 1 60  ? 24.511  23.710  37.087  1.00 36.68  ? 59  ALA C CA     1 
ATOM   8541  C  C      . ALA D 1 60  ? 24.397  24.430  38.428  1.00 37.98  ? 59  ALA C C      1 
ATOM   8542  O  O      . ALA D 1 60  ? 23.606  25.370  38.578  1.00 39.08  ? 59  ALA C O      1 
ATOM   8543  C  CB     . ALA D 1 60  ? 25.482  24.455  36.167  1.00 38.98  ? 59  ALA C CB     1 
ATOM   8544  H  H      . ALA D 1 60  ? 22.997  24.298  35.993  1.00 47.91  ? 59  ALA C H      1 
ATOM   8545  H  HA     . ALA D 1 60  ? 24.866  22.824  37.259  1.00 44.05  ? 59  ALA C HA     1 
ATOM   8546  H  HB1    . ALA D 1 60  ? 26.390  24.295  36.469  1.00 46.81  ? 59  ALA C HB1    1 
ATOM   8547  H  HB2    . ALA D 1 60  ? 25.373  24.127  35.261  1.00 46.81  ? 59  ALA C HB2    1 
ATOM   8548  H  HB3    . ALA D 1 60  ? 25.284  25.404  36.201  1.00 46.81  ? 59  ALA C HB3    1 
ATOM   8549  N  N      . GLY D 1 61  ? 25.212  24.009  39.386  1.00 46.84  ? 60  GLY C N      1 
ATOM   8550  C  CA     . GLY D 1 61  ? 25.232  24.647  40.684  1.00 48.67  ? 60  GLY C CA     1 
ATOM   8551  C  C      . GLY D 1 61  ? 26.374  25.624  40.878  1.00 53.77  ? 60  GLY C C      1 
ATOM   8552  O  O      . GLY D 1 61  ? 26.791  25.886  42.010  1.00 51.85  ? 60  GLY C O      1 
ATOM   8553  H  H      . GLY D 1 61  ? 25.763  23.354  39.304  1.00 56.24  ? 60  GLY C H      1 
ATOM   8554  H  HA2    . GLY D 1 61  ? 24.400  25.131  40.808  1.00 58.44  ? 60  GLY C HA2    1 
ATOM   8555  H  HA3    . GLY D 1 61  ? 25.305  23.963  41.368  1.00 58.44  ? 60  GLY C HA3    1 
ATOM   8556  N  N      . GLN D 1 62  ? 26.901  26.169  39.789  1.00 52.81  ? 61  GLN C N      1 
ATOM   8557  C  CA     . GLN D 1 62  ? 27.968  27.158  39.913  1.00 54.93  ? 61  GLN C CA     1 
ATOM   8558  C  C      . GLN D 1 62  ? 27.415  28.444  40.516  1.00 56.33  ? 61  GLN C C      1 
ATOM   8559  O  O      . GLN D 1 62  ? 26.488  29.051  39.962  1.00 52.27  ? 61  GLN C O      1 
ATOM   8560  C  CB     . GLN D 1 62  ? 28.622  27.463  38.565  1.00 48.75  ? 61  GLN C CB     1 
ATOM   8561  C  CG     . GLN D 1 62  ? 28.763  26.291  37.622  1.00 44.26  ? 61  GLN C CG     1 
ATOM   8562  C  CD     . GLN D 1 62  ? 30.073  25.541  37.815  1.00 49.71  ? 61  GLN C CD     1 
ATOM   8563  O  OE1    . GLN D 1 62  ? 31.108  26.135  38.118  1.00 49.45  ? 61  GLN C OE1    1 
ATOM   8564  N  NE2    . GLN D 1 62  ? 30.036  24.227  37.613  1.00 50.16  ? 61  GLN C NE2    1 
ATOM   8565  H  H      . GLN D 1 62  ? 26.664  25.989  38.983  1.00 63.41  ? 61  GLN C H      1 
ATOM   8566  H  HA     . GLN D 1 62  ? 28.650  26.789  40.496  1.00 65.95  ? 61  GLN C HA     1 
ATOM   8567  H  HB2    . GLN D 1 62  ? 28.086  28.133  38.113  1.00 58.54  ? 61  GLN C HB2    1 
ATOM   8568  H  HB3    . GLN D 1 62  ? 29.513  27.808  38.731  1.00 58.54  ? 61  GLN C HB3    1 
ATOM   8569  H  HG2    . GLN D 1 62  ? 28.035  25.669  37.777  1.00 53.15  ? 61  GLN C HG2    1 
ATOM   8570  H  HG3    . GLN D 1 62  ? 28.734  26.614  36.708  1.00 53.15  ? 61  GLN C HG3    1 
ATOM   8571  H  HE21   . GLN D 1 62  ? 29.299  23.847  37.386  1.00 60.22  ? 61  GLN C HE21   1 
ATOM   8572  H  HE22   . GLN D 1 62  ? 30.750  23.757  37.709  1.00 60.22  ? 61  GLN C HE22   1 
ATOM   8573  N  N      . GLU D 1 63  ? 28.006  28.873  41.637  1.00 59.15  ? 62  GLU C N      1 
ATOM   8574  C  CA     . GLU D 1 63  ? 27.548  30.082  42.308  1.00 59.58  ? 62  GLU C CA     1 
ATOM   8575  C  C      . GLU D 1 63  ? 27.662  31.307  41.414  1.00 57.16  ? 62  GLU C C      1 
ATOM   8576  O  O      . GLU D 1 63  ? 26.932  32.290  41.614  1.00 54.87  ? 62  GLU C O      1 
ATOM   8577  C  CB     . GLU D 1 63  ? 28.362  30.293  43.596  1.00 61.67  ? 62  GLU C CB     1 
ATOM   8578  C  CG     . GLU D 1 63  ? 28.887  28.992  44.206  1.00 67.38  ? 62  GLU C CG     1 
ATOM   8579  C  CD     . GLU D 1 63  ? 29.062  29.041  45.711  1.00 75.51  ? 62  GLU C CD     1 
ATOM   8580  O  OE1    . GLU D 1 63  ? 28.809  30.106  46.321  1.00 79.05  ? 62  GLU C OE1    1 
ATOM   8581  O  OE2    . GLU D 1 63  ? 29.438  27.992  46.284  1.00 73.90  ? 62  GLU C OE2    1 
ATOM   8582  H  H      . GLU D 1 63  ? 28.668  28.483  42.022  1.00 71.02  ? 62  GLU C H      1 
ATOM   8583  H  HA     . GLU D 1 63  ? 26.615  29.979  42.552  1.00 71.52  ? 62  GLU C HA     1 
ATOM   8584  H  HB2    . GLU D 1 63  ? 29.126  30.856  43.394  1.00 74.04  ? 62  GLU C HB2    1 
ATOM   8585  H  HB3    . GLU D 1 63  ? 27.797  30.724  44.256  1.00 74.04  ? 62  GLU C HB3    1 
ATOM   8586  H  HG2    . GLU D 1 63  ? 28.260  28.279  44.005  1.00 80.89  ? 62  GLU C HG2    1 
ATOM   8587  H  HG3    . GLU D 1 63  ? 29.752  28.792  43.815  1.00 80.89  ? 62  GLU C HG3    1 
ATOM   8588  N  N      . GLU D 1 64  ? 28.558  31.269  40.432  1.00 54.17  ? 63  GLU C N      1 
ATOM   8589  C  CA     . GLU D 1 64  ? 28.823  32.467  39.651  1.00 52.03  ? 63  GLU C CA     1 
ATOM   8590  C  C      . GLU D 1 64  ? 27.551  32.975  38.982  1.00 50.71  ? 63  GLU C C      1 
ATOM   8591  O  O      . GLU D 1 64  ? 27.336  34.187  38.889  1.00 52.43  ? 63  GLU C O      1 
ATOM   8592  C  CB     . GLU D 1 64  ? 29.911  32.175  38.621  1.00 51.86  ? 63  GLU C CB     1 
ATOM   8593  C  CG     . GLU D 1 64  ? 31.270  32.780  38.956  1.00 56.15  ? 63  GLU C CG     1 
ATOM   8594  C  CD     . GLU D 1 64  ? 31.172  34.229  39.403  1.00 60.47  ? 63  GLU C CD     1 
ATOM   8595  O  OE1    . GLU D 1 64  ? 30.747  35.070  38.579  1.00 59.08  ? 63  GLU C OE1    1 
ATOM   8596  O  OE2    . GLU D 1 64  ? 31.505  34.519  40.577  1.00 65.47  ? 63  GLU C OE2    1 
ATOM   8597  H  H      . GLU D 1 64  ? 29.015  30.577  40.204  1.00 65.04  ? 63  GLU C H      1 
ATOM   8598  H  HA     . GLU D 1 64  ? 29.147  33.170  40.236  1.00 62.48  ? 63  GLU C HA     1 
ATOM   8599  H  HB2    . GLU D 1 64  ? 30.025  31.214  38.555  1.00 62.27  ? 63  GLU C HB2    1 
ATOM   8600  H  HB3    . GLU D 1 64  ? 29.631  32.536  37.765  1.00 62.27  ? 63  GLU C HB3    1 
ATOM   8601  H  HG2    . GLU D 1 64  ? 31.675  32.271  39.675  1.00 67.41  ? 63  GLU C HG2    1 
ATOM   8602  H  HG3    . GLU D 1 64  ? 31.834  32.747  38.167  1.00 67.41  ? 63  GLU C HG3    1 
ATOM   8603  N  N      . TYR D 1 65  ? 26.680  32.067  38.534  1.00 46.30  ? 64  TYR C N      1 
ATOM   8604  C  CA     . TYR D 1 65  ? 25.558  32.431  37.684  1.00 47.90  ? 64  TYR C CA     1 
ATOM   8605  C  C      . TYR D 1 65  ? 24.233  32.350  38.417  1.00 53.50  ? 64  TYR C C      1 
ATOM   8606  O  O      . TYR D 1 65  ? 23.194  32.119  37.798  1.00 52.20  ? 64  TYR C O      1 
ATOM   8607  C  CB     . TYR D 1 65  ? 25.554  31.543  36.441  1.00 42.24  ? 64  TYR C CB     1 
ATOM   8608  C  CG     . TYR D 1 65  ? 26.957  31.422  35.838  1.00 36.89  ? 64  TYR C CG     1 
ATOM   8609  C  CD1    . TYR D 1 65  ? 27.605  32.522  35.292  1.00 38.57  ? 64  TYR C CD1    1 
ATOM   8610  C  CD2    . TYR D 1 65  ? 27.621  30.211  35.854  1.00 34.24  ? 64  TYR C CD2    1 
ATOM   8611  C  CE1    . TYR D 1 65  ? 28.891  32.408  34.754  1.00 30.67  ? 64  TYR C CE1    1 
ATOM   8612  C  CE2    . TYR D 1 65  ? 28.871  30.075  35.313  1.00 34.61  ? 64  TYR C CE2    1 
ATOM   8613  C  CZ     . TYR D 1 65  ? 29.508  31.186  34.766  1.00 30.85  ? 64  TYR C CZ     1 
ATOM   8614  O  OH     . TYR D 1 65  ? 30.767  31.011  34.263  1.00 29.69  ? 64  TYR C OH     1 
ATOM   8615  H  H      . TYR D 1 65  ? 26.725  31.227  38.715  1.00 55.59  ? 64  TYR C H      1 
ATOM   8616  H  HA     . TYR D 1 65  ? 25.660  33.353  37.400  1.00 57.51  ? 64  TYR C HA     1 
ATOM   8617  H  HB2    . TYR D 1 65  ? 25.246  30.655  36.682  1.00 50.73  ? 64  TYR C HB2    1 
ATOM   8618  H  HB3    . TYR D 1 65  ? 24.965  31.928  35.773  1.00 50.73  ? 64  TYR C HB3    1 
ATOM   8619  H  HD1    . TYR D 1 65  ? 27.178  33.348  35.285  1.00 46.32  ? 64  TYR C HD1    1 
ATOM   8620  H  HD2    . TYR D 1 65  ? 27.210  29.472  36.241  1.00 41.12  ? 64  TYR C HD2    1 
ATOM   8621  H  HE1    . TYR D 1 65  ? 29.320  33.151  34.393  1.00 36.84  ? 64  TYR C HE1    1 
ATOM   8622  H  HE2    . TYR D 1 65  ? 29.292  29.246  35.311  1.00 41.57  ? 64  TYR C HE2    1 
ATOM   8623  H  HH     . TYR D 1 65  ? 30.989  30.203  34.321  1.00 35.66  ? 64  TYR C HH     1 
ATOM   8624  N  N      . SER D 1 66  ? 24.261  32.562  39.737  1.00 57.48  ? 65  SER C N      1 
ATOM   8625  C  CA     . SER D 1 66  ? 23.029  32.549  40.519  1.00 62.07  ? 65  SER C CA     1 
ATOM   8626  C  C      . SER D 1 66  ? 21.990  33.480  39.914  1.00 62.99  ? 65  SER C C      1 
ATOM   8627  O  O      . SER D 1 66  ? 20.812  33.126  39.811  1.00 63.78  ? 65  SER C O      1 
ATOM   8628  C  CB     . SER D 1 66  ? 23.320  32.946  41.970  1.00 63.47  ? 65  SER C CB     1 
ATOM   8629  O  OG     . SER D 1 66  ? 24.571  32.438  42.417  1.00 62.43  ? 65  SER C OG     1 
ATOM   8630  H  H      . SER D 1 66  ? 24.973  32.714  40.195  1.00 69.01  ? 65  SER C H      1 
ATOM   8631  H  HA     . SER D 1 66  ? 22.670  31.648  40.522  1.00 74.52  ? 65  SER C HA     1 
ATOM   8632  H  HB2    . SER D 1 66  ? 23.337  33.914  42.030  1.00 76.20  ? 65  SER C HB2    1 
ATOM   8633  H  HB3    . SER D 1 66  ? 22.618  32.591  42.537  1.00 76.20  ? 65  SER C HB3    1 
ATOM   8634  H  HG     . SER D 1 66  ? 24.726  32.703  43.199  1.00 74.96  ? 65  SER C HG     1 
ATOM   8635  N  N      . ALA D 1 67  ? 22.414  34.668  39.484  1.00 62.33  ? 66  ALA C N      1 
ATOM   8636  C  CA     . ALA D 1 67  ? 21.471  35.645  38.955  1.00 64.65  ? 66  ALA C CA     1 
ATOM   8637  C  C      . ALA D 1 67  ? 20.573  35.030  37.894  1.00 65.33  ? 66  ALA C C      1 
ATOM   8638  O  O      . ALA D 1 67  ? 19.361  35.274  37.885  1.00 69.28  ? 66  ALA C O      1 
ATOM   8639  C  CB     . ALA D 1 67  ? 22.222  36.850  38.386  1.00 69.06  ? 66  ALA C CB     1 
ATOM   8640  H  H      . ALA D 1 67  ? 23.234  34.929  39.488  1.00 74.83  ? 66  ALA C H      1 
ATOM   8641  H  HA     . ALA D 1 67  ? 20.909  35.958  39.681  1.00 77.61  ? 66  ALA C HA     1 
ATOM   8642  H  HB1    . ALA D 1 67  ? 21.579  37.487  38.036  1.00 82.90  ? 66  ALA C HB1    1 
ATOM   8643  H  HB2    . ALA D 1 67  ? 22.744  37.260  39.093  1.00 82.90  ? 66  ALA C HB2    1 
ATOM   8644  H  HB3    . ALA D 1 67  ? 22.809  36.548  37.675  1.00 82.90  ? 66  ALA C HB3    1 
ATOM   8645  N  N      . MET D 1 68  ? 21.140  34.201  37.008  1.00 62.26  ? 67  MET C N      1 
ATOM   8646  C  CA     . MET D 1 68  ? 20.377  33.660  35.892  1.00 64.85  ? 67  MET C CA     1 
ATOM   8647  C  C      . MET D 1 68  ? 19.686  32.332  36.191  1.00 66.29  ? 67  MET C C      1 
ATOM   8648  O  O      . MET D 1 68  ? 18.850  31.905  35.387  1.00 65.98  ? 67  MET C O      1 
ATOM   8649  C  CB     . MET D 1 68  ? 21.259  33.441  34.665  1.00 60.05  ? 67  MET C CB     1 
ATOM   8650  C  CG     . MET D 1 68  ? 22.427  34.387  34.500  1.00 58.64  ? 67  MET C CG     1 
ATOM   8651  S  SD     . MET D 1 68  ? 22.837  34.323  32.755  1.00 58.86  ? 67  MET C SD     1 
ATOM   8652  C  CE     . MET D 1 68  ? 22.077  35.867  32.229  1.00 52.84  ? 67  MET C CE     1 
ATOM   8653  H  H      . MET D 1 68  ? 21.960  33.943  37.038  1.00 74.75  ? 67  MET C H      1 
ATOM   8654  H  HA     . MET D 1 68  ? 19.711  34.332  35.679  1.00 77.85  ? 67  MET C HA     1 
ATOM   8655  H  HB2    . MET D 1 68  ? 21.624  32.543  34.713  1.00 72.10  ? 67  MET C HB2    1 
ATOM   8656  H  HB3    . MET D 1 68  ? 20.705  33.532  33.875  1.00 72.10  ? 67  MET C HB3    1 
ATOM   8657  H  HG2    . MET D 1 68  ? 22.177  35.290  34.748  1.00 70.41  ? 67  MET C HG2    1 
ATOM   8658  H  HG3    . MET D 1 68  ? 23.186  34.095  35.029  1.00 70.41  ? 67  MET C HG3    1 
ATOM   8659  H  HE1    . MET D 1 68  ? 22.233  35.989  31.280  1.00 63.44  ? 67  MET C HE1    1 
ATOM   8660  H  HE2    . MET D 1 68  ? 21.124  35.826  32.405  1.00 63.44  ? 67  MET C HE2    1 
ATOM   8661  H  HE3    . MET D 1 68  ? 22.474  36.600  32.726  1.00 63.44  ? 67  MET C HE3    1 
ATOM   8662  N  N      . ARG D 1 69  ? 20.051  31.644  37.281  1.00 69.49  ? 68  ARG C N      1 
ATOM   8663  C  CA     . ARG D 1 69  ? 19.226  30.569  37.818  1.00 63.68  ? 68  ARG C CA     1 
ATOM   8664  C  C      . ARG D 1 69  ? 17.777  31.027  37.834  1.00 62.40  ? 68  ARG C C      1 
ATOM   8665  O  O      . ARG D 1 69  ? 16.851  30.229  37.655  1.00 64.80  ? 68  ARG C O      1 
ATOM   8666  C  CB     . ARG D 1 69  ? 19.621  30.193  39.248  1.00 64.98  ? 68  ARG C CB     1 
ATOM   8667  C  CG     . ARG D 1 69  ? 20.482  28.952  39.405  1.00 65.11  ? 68  ARG C CG     1 
ATOM   8668  C  CD     . ARG D 1 69  ? 21.101  28.918  40.813  1.00 66.63  ? 68  ARG C CD     1 
ATOM   8669  N  NE     . ARG D 1 69  ? 22.505  28.518  40.791  1.00 72.08  ? 68  ARG C NE     1 
ATOM   8670  C  CZ     . ARG D 1 69  ? 23.364  28.706  41.787  1.00 73.60  ? 68  ARG C CZ     1 
ATOM   8671  N  NH1    . ARG D 1 69  ? 22.984  29.242  42.939  1.00 70.30  ? 68  ARG C NH1    1 
ATOM   8672  N  NH2    . ARG D 1 69  ? 24.638  28.351  41.618  1.00 69.70  ? 68  ARG C NH2    1 
ATOM   8673  H  H      . ARG D 1 69  ? 20.775  31.785  37.725  1.00 83.42  ? 68  ARG C H      1 
ATOM   8674  H  HA     . ARG D 1 69  ? 19.346  29.783  37.262  1.00 76.45  ? 68  ARG C HA     1 
ATOM   8675  H  HB2    . ARG D 1 69  ? 20.117  30.935  39.628  1.00 78.01  ? 68  ARG C HB2    1 
ATOM   8676  H  HB3    . ARG D 1 69  ? 18.808  30.043  39.756  1.00 78.01  ? 68  ARG C HB3    1 
ATOM   8677  H  HG2    . ARG D 1 69  ? 19.937  28.159  39.286  1.00 78.16  ? 68  ARG C HG2    1 
ATOM   8678  H  HG3    . ARG D 1 69  ? 21.197  28.965  38.750  1.00 78.16  ? 68  ARG C HG3    1 
ATOM   8679  H  HD2    . ARG D 1 69  ? 21.046  29.803  41.207  1.00 79.99  ? 68  ARG C HD2    1 
ATOM   8680  H  HD3    . ARG D 1 69  ? 20.615  28.281  41.359  1.00 79.99  ? 68  ARG C HD3    1 
ATOM   8681  H  HE     . ARG D 1 69  ? 22.798  28.132  40.081  1.00 86.53  ? 68  ARG C HE     1 
ATOM   8682  H  HH11   . ARG D 1 69  ? 22.165  29.477  43.055  1.00 84.39  ? 68  ARG C HH11   1 
ATOM   8683  H  HH12   . ARG D 1 69  ? 23.557  29.354  43.571  1.00 84.39  ? 68  ARG C HH12   1 
ATOM   8684  H  HH21   . ARG D 1 69  ? 24.893  28.006  40.873  1.00 83.68  ? 68  ARG C HH21   1 
ATOM   8685  H  HH22   . ARG D 1 69  ? 25.205  28.467  42.254  1.00 83.68  ? 68  ARG C HH22   1 
ATOM   8686  N  N      . ASP D 1 70  ? 17.586  32.323  38.084  1.00 63.66  ? 69  ASP C N      1 
ATOM   8687  C  CA     . ASP D 1 70  ? 16.251  32.858  38.319  1.00 64.69  ? 69  ASP C CA     1 
ATOM   8688  C  C      . ASP D 1 70  ? 15.294  32.437  37.214  1.00 64.76  ? 69  ASP C C      1 
ATOM   8689  O  O      . ASP D 1 70  ? 14.176  31.982  37.490  1.00 60.01  ? 69  ASP C O      1 
ATOM   8690  C  CB     . ASP D 1 70  ? 16.336  34.383  38.437  1.00 63.90  ? 69  ASP C CB     1 
ATOM   8691  C  CG     . ASP D 1 70  ? 16.735  34.834  39.834  1.00 64.01  ? 69  ASP C CG     1 
ATOM   8692  O  OD1    . ASP D 1 70  ? 17.331  34.016  40.577  1.00 61.38  ? 69  ASP C OD1    1 
ATOM   8693  O  OD2    . ASP D 1 70  ? 16.450  36.003  40.188  1.00 68.86  ? 69  ASP C OD2    1 
ATOM   8694  H  H      . ASP D 1 70  ? 18.213  32.911  38.122  1.00 76.42  ? 69  ASP C H      1 
ATOM   8695  H  HA     . ASP D 1 70  ? 15.896  32.514  39.154  1.00 77.66  ? 69  ASP C HA     1 
ATOM   8696  H  HB2    . ASP D 1 70  ? 17.000  34.713  37.812  1.00 76.72  ? 69  ASP C HB2    1 
ATOM   8697  H  HB3    . ASP D 1 70  ? 15.469  34.766  38.232  1.00 76.72  ? 69  ASP C HB3    1 
ATOM   8698  N  N      . GLN D 1 71  ? 15.729  32.539  35.959  1.00 62.02  ? 70  GLN C N      1 
ATOM   8699  C  CA     . GLN D 1 71  ? 14.866  32.181  34.836  1.00 68.75  ? 70  GLN C CA     1 
ATOM   8700  C  C      . GLN D 1 71  ? 14.428  30.720  34.924  1.00 63.15  ? 70  GLN C C      1 
ATOM   8701  O  O      . GLN D 1 71  ? 13.236  30.411  34.803  1.00 63.80  ? 70  GLN C O      1 
ATOM   8702  C  CB     . GLN D 1 71  ? 15.600  32.459  33.523  1.00 69.24  ? 70  GLN C CB     1 
ATOM   8703  C  CG     . GLN D 1 71  ? 14.719  32.551  32.269  1.00 72.54  ? 70  GLN C CG     1 
ATOM   8704  C  CD     . GLN D 1 71  ? 13.320  33.048  32.552  1.00 69.59  ? 70  GLN C CD     1 
ATOM   8705  O  OE1    . GLN D 1 71  ? 13.083  34.256  32.641  1.00 71.61  ? 70  GLN C OE1    1 
ATOM   8706  N  NE2    . GLN D 1 71  ? 12.375  32.119  32.676  1.00 69.44  ? 70  GLN C NE2    1 
ATOM   8707  H  H      . GLN D 1 71  ? 16.513  32.810  35.733  1.00 74.46  ? 70  GLN C H      1 
ATOM   8708  H  HA     . GLN D 1 71  ? 14.066  32.729  34.858  1.00 82.54  ? 70  GLN C HA     1 
ATOM   8709  H  HB2    . GLN D 1 71  ? 16.066  33.306  33.609  1.00 83.12  ? 70  GLN C HB2    1 
ATOM   8710  H  HB3    . GLN D 1 71  ? 16.237  31.743  33.374  1.00 83.12  ? 70  GLN C HB3    1 
ATOM   8711  H  HG2    . GLN D 1 71  ? 15.131  33.165  31.641  1.00 87.08  ? 70  GLN C HG2    1 
ATOM   8712  H  HG3    . GLN D 1 71  ? 14.646  31.670  31.871  1.00 87.08  ? 70  GLN C HG3    1 
ATOM   8713  H  HE21   . GLN D 1 71  ? 12.578  31.287  32.595  1.00 83.36  ? 70  GLN C HE21   1 
ATOM   8714  H  HE22   . GLN D 1 71  ? 11.563  32.350  32.838  1.00 83.36  ? 70  GLN C HE22   1 
ATOM   8715  N  N      . TYR D 1 72  ? 15.382  29.802  35.123  1.00 66.12  ? 71  TYR C N      1 
ATOM   8716  C  CA     . TYR D 1 72  ? 15.035  28.421  35.438  1.00 58.07  ? 71  TYR C CA     1 
ATOM   8717  C  C      . TYR D 1 72  ? 13.906  28.382  36.456  1.00 57.37  ? 71  TYR C C      1 
ATOM   8718  O  O      . TYR D 1 72  ? 12.886  27.707  36.280  1.00 53.01  ? 71  TYR C O      1 
ATOM   8719  C  CB     . TYR D 1 72  ? 16.230  27.679  36.034  1.00 59.59  ? 71  TYR C CB     1 
ATOM   8720  C  CG     . TYR D 1 72  ? 17.480  27.587  35.195  1.00 53.78  ? 71  TYR C CG     1 
ATOM   8721  C  CD1    . TYR D 1 72  ? 17.449  27.759  33.822  1.00 58.44  ? 71  TYR C CD1    1 
ATOM   8722  C  CD2    . TYR D 1 72  ? 18.695  27.280  35.790  1.00 56.63  ? 71  TYR C CD2    1 
ATOM   8723  C  CE1    . TYR D 1 72  ? 18.618  27.644  33.057  1.00 58.36  ? 71  TYR C CE1    1 
ATOM   8724  C  CE2    . TYR D 1 72  ? 19.859  27.164  35.045  1.00 54.56  ? 71  TYR C CE2    1 
ATOM   8725  C  CZ     . TYR D 1 72  ? 19.819  27.344  33.687  1.00 52.18  ? 71  TYR C CZ     1 
ATOM   8726  O  OH     . TYR D 1 72  ? 20.985  27.231  32.959  1.00 46.05  ? 71  TYR C OH     1 
ATOM   8727  H  H      . TYR D 1 72  ? 16.227  29.956  35.082  1.00 79.38  ? 71  TYR C H      1 
ATOM   8728  H  HA     . TYR D 1 72  ? 14.776  27.982  34.613  1.00 69.71  ? 71  TYR C HA     1 
ATOM   8729  H  HB2    . TYR D 1 72  ? 16.477  28.128  36.858  1.00 71.54  ? 71  TYR C HB2    1 
ATOM   8730  H  HB3    . TYR D 1 72  ? 15.951  26.769  36.223  1.00 71.54  ? 71  TYR C HB3    1 
ATOM   8731  H  HD1    . TYR D 1 72  ? 16.642  27.954  33.402  1.00 70.16  ? 71  TYR C HD1    1 
ATOM   8732  H  HD2    . TYR D 1 72  ? 18.731  27.149  36.710  1.00 67.99  ? 71  TYR C HD2    1 
ATOM   8733  H  HE1    . TYR D 1 72  ? 18.590  27.767  32.136  1.00 70.06  ? 71  TYR C HE1    1 
ATOM   8734  H  HE2    . TYR D 1 72  ? 20.664  26.964  35.465  1.00 65.50  ? 71  TYR C HE2    1 
ATOM   8735  H  HH     . TYR D 1 72  ? 20.833  27.386  32.147  1.00 55.29  ? 71  TYR C HH     1 
ATOM   8736  N  N      . MET D 1 73  ? 14.105  29.101  37.555  1.00 59.99  ? 72  MET C N      1 
ATOM   8737  C  CA     . MET D 1 73  ? 13.175  29.040  38.675  1.00 58.68  ? 72  MET C CA     1 
ATOM   8738  C  C      . MET D 1 73  ? 11.801  29.554  38.281  1.00 56.25  ? 72  MET C C      1 
ATOM   8739  O  O      . MET D 1 73  ? 10.792  29.103  38.843  1.00 53.06  ? 72  MET C O      1 
ATOM   8740  C  CB     . MET D 1 73  ? 13.791  29.806  39.845  1.00 56.47  ? 72  MET C CB     1 
ATOM   8741  C  CG     . MET D 1 73  ? 14.988  29.027  40.404  1.00 57.55  ? 72  MET C CG     1 
ATOM   8742  S  SD     . MET D 1 73  ? 15.766  29.747  41.829  1.00 57.98  ? 72  MET C SD     1 
ATOM   8743  C  CE     . MET D 1 73  ? 16.976  28.531  42.356  1.00 55.41  ? 72  MET C CE     1 
ATOM   8744  H  H      . MET D 1 73  ? 14.771  29.632  37.678  1.00 72.02  ? 72  MET C H      1 
ATOM   8745  H  HA     . MET D 1 73  ? 13.046  28.125  38.970  1.00 70.45  ? 72  MET C HA     1 
ATOM   8746  H  HB2    . MET D 1 73  ? 14.097  30.675  39.542  1.00 67.80  ? 72  MET C HB2    1 
ATOM   8747  H  HB3    . MET D 1 73  ? 13.132  29.914  40.549  1.00 67.80  ? 72  MET C HB3    1 
ATOM   8748  H  HG2    . MET D 1 73  ? 14.686  28.140  40.657  1.00 69.10  ? 72  MET C HG2    1 
ATOM   8749  H  HG3    . MET D 1 73  ? 15.662  28.961  39.709  1.00 69.10  ? 72  MET C HG3    1 
ATOM   8750  H  HE1    . MET D 1 73  ? 17.416  28.850  43.159  1.00 66.53  ? 72  MET C HE1    1 
ATOM   8751  H  HE2    . MET D 1 73  ? 16.522  27.693  42.538  1.00 66.53  ? 72  MET C HE2    1 
ATOM   8752  H  HE3    . MET D 1 73  ? 17.627  28.407  41.648  1.00 66.53  ? 72  MET C HE3    1 
ATOM   8753  N  N      . ARG D 1 74  ? 11.732  30.435  37.283  1.00 58.06  ? 73  ARG C N      1 
ATOM   8754  C  CA     . ARG D 1 74  ? 10.447  30.983  36.864  1.00 56.47  ? 73  ARG C CA     1 
ATOM   8755  C  C      . ARG D 1 74  ? 9.597   29.914  36.204  1.00 50.90  ? 73  ARG C C      1 
ATOM   8756  O  O      . ARG D 1 74  ? 8.458   29.679  36.615  1.00 53.35  ? 73  ARG C O      1 
ATOM   8757  C  CB     . ARG D 1 74  ? 10.659  32.174  35.923  1.00 54.71  ? 73  ARG C CB     1 
ATOM   8758  C  CG     . ARG D 1 74  ? 10.769  33.545  36.654  1.00 59.34  ? 73  ARG C CG     1 
ATOM   8759  C  CD     . ARG D 1 74  ? 11.766  34.531  35.990  1.00 64.73  ? 73  ARG C CD     1 
ATOM   8760  N  NE     . ARG D 1 74  ? 12.368  35.466  36.945  1.00 61.55  ? 73  ARG C NE     1 
ATOM   8761  C  CZ     . ARG D 1 74  ? 13.639  35.860  36.922  1.00 62.50  ? 73  ARG C CZ     1 
ATOM   8762  N  NH1    . ARG D 1 74  ? 14.485  35.411  36.014  1.00 60.52  ? 73  ARG C NH1    1 
ATOM   8763  N  NH2    . ARG D 1 74  ? 14.072  36.728  37.836  1.00 66.41  ? 73  ARG C NH2    1 
ATOM   8764  H  H      . ARG D 1 74  ? 12.407  30.727  36.837  1.00 69.71  ? 73  ARG C H      1 
ATOM   8765  H  HA     . ARG D 1 74  ? 9.972   31.308  37.645  1.00 67.80  ? 73  ARG C HA     1 
ATOM   8766  H  HB2    . ARG D 1 74  ? 11.481  32.037  35.428  1.00 65.68  ? 73  ARG C HB2    1 
ATOM   8767  H  HB3    . ARG D 1 74  ? 9.908   32.225  35.311  1.00 65.68  ? 73  ARG C HB3    1 
ATOM   8768  H  HG2    . ARG D 1 74  ? 9.895   33.967  36.659  1.00 71.24  ? 73  ARG C HG2    1 
ATOM   8769  H  HG3    . ARG D 1 74  ? 11.068  33.391  37.563  1.00 71.24  ? 73  ARG C HG3    1 
ATOM   8770  H  HD2    . ARG D 1 74  ? 12.481  34.024  35.575  1.00 77.71  ? 73  ARG C HD2    1 
ATOM   8771  H  HD3    . ARG D 1 74  ? 11.295  35.051  35.319  1.00 77.71  ? 73  ARG C HD3    1 
ATOM   8772  H  HE     . ARG D 1 74  ? 11.864  35.784  37.565  1.00 73.90  ? 73  ARG C HE     1 
ATOM   8773  H  HH11   . ARG D 1 74  ? 14.220  34.850  35.418  1.00 72.65  ? 73  ARG C HH11   1 
ATOM   8774  H  HH12   . ARG D 1 74  ? 15.303  35.678  36.018  1.00 72.65  ? 73  ARG C HH12   1 
ATOM   8775  H  HH21   . ARG D 1 74  ? 13.531  37.029  38.433  1.00 79.72  ? 73  ARG C HH21   1 
ATOM   8776  H  HH22   . ARG D 1 74  ? 14.891  36.987  37.828  1.00 79.72  ? 73  ARG C HH22   1 
ATOM   8777  N  N      . THR D 1 75  ? 10.152  29.225  35.203  1.00 51.48  ? 74  THR C N      1 
ATOM   8778  C  CA     . THR D 1 75  ? 9.385   28.299  34.383  1.00 52.62  ? 74  THR C CA     1 
ATOM   8779  C  C      . THR D 1 75  ? 9.082   26.977  35.089  1.00 46.91  ? 74  THR C C      1 
ATOM   8780  O  O      . THR D 1 75  ? 8.086   26.325  34.770  1.00 53.42  ? 74  THR C O      1 
ATOM   8781  C  CB     . THR D 1 75  ? 10.161  28.039  33.087  1.00 59.92  ? 74  THR C CB     1 
ATOM   8782  O  OG1    . THR D 1 75  ? 11.562  28.000  33.396  1.00 61.27  ? 74  THR C OG1    1 
ATOM   8783  C  CG2    . THR D 1 75  ? 9.907   29.140  32.051  1.00 60.06  ? 74  THR C CG2    1 
ATOM   8784  H  H      . THR D 1 75  ? 10.981  29.280  34.979  1.00 61.81  ? 74  THR C H      1 
ATOM   8785  H  HA     . THR D 1 75  ? 8.528   28.700  34.170  1.00 63.18  ? 74  THR C HA     1 
ATOM   8786  H  HB     . THR D 1 75  ? 9.871   27.199  32.699  1.00 71.94  ? 74  THR C HB     1 
ATOM   8787  H  HG1    . THR D 1 75  ? 12.007  27.870  32.695  1.00 73.56  ? 74  THR C HG1    1 
ATOM   8788  H  HG21   . THR D 1 75  ? 10.406  28.954  31.240  1.00 72.10  ? 74  THR C HG21   1 
ATOM   8789  H  HG22   . THR D 1 75  ? 8.962   29.182  31.837  1.00 72.10  ? 74  THR C HG22   1 
ATOM   8790  H  HG23   . THR D 1 75  ? 10.189  29.998  32.404  1.00 72.10  ? 74  THR C HG23   1 
ATOM   8791  N  N      . GLY D 1 76  ? 9.889   26.568  36.062  1.00 45.69  ? 75  GLY C N      1 
ATOM   8792  C  CA     . GLY D 1 76  ? 9.745   25.222  36.621  1.00 47.35  ? 75  GLY C CA     1 
ATOM   8793  C  C      . GLY D 1 76  ? 8.575   25.077  37.589  1.00 47.51  ? 75  GLY C C      1 
ATOM   8794  O  O      . GLY D 1 76  ? 8.340   25.925  38.454  1.00 51.88  ? 75  GLY C O      1 
ATOM   8795  H  H      . GLY D 1 76  ? 10.517  27.039  36.413  1.00 54.86  ? 75  GLY C H      1 
ATOM   8796  H  HA2    . GLY D 1 76  ? 9.614   24.592  35.895  1.00 56.85  ? 75  GLY C HA2    1 
ATOM   8797  H  HA3    . GLY D 1 76  ? 10.558  24.990  37.097  1.00 56.85  ? 75  GLY C HA3    1 
ATOM   8798  N  N      . GLU D 1 77  ? 7.853   23.942  37.453  1.00 46.00  ? 76  GLU C N      1 
ATOM   8799  C  CA     . GLU D 1 77  ? 6.699   23.625  38.308  1.00 37.81  ? 76  GLU C CA     1 
ATOM   8800  C  C      . GLU D 1 77  ? 7.118   23.015  39.641  1.00 43.69  ? 76  GLU C C      1 
ATOM   8801  O  O      . GLU D 1 77  ? 6.344   23.073  40.603  1.00 46.39  ? 76  GLU C O      1 
ATOM   8802  C  CB     . GLU D 1 77  ? 5.740   22.682  37.556  1.00 45.31  ? 76  GLU C CB     1 
ATOM   8803  C  CG     . GLU D 1 77  ? 4.981   23.324  36.338  1.00 44.59  ? 76  GLU C CG     1 
ATOM   8804  C  CD     . GLU D 1 77  ? 4.509   22.275  35.315  1.00 54.05  ? 76  GLU C CD     1 
ATOM   8805  O  OE1    . GLU D 1 77  ? 4.953   21.114  35.461  1.00 49.85  ? 76  GLU C OE1    1 
ATOM   8806  O  OE2    . GLU D 1 77  ? 3.800   22.605  34.313  1.00 50.03  ? 76  GLU C OE2    1 
ATOM   8807  H  H      . GLU D 1 77  ? 8.018   23.336  36.865  1.00 55.23  ? 76  GLU C H      1 
ATOM   8808  H  HA     . GLU D 1 77  ? 6.208   24.437  38.506  1.00 45.40  ? 76  GLU C HA     1 
ATOM   8809  H  HB2    . GLU D 1 77  ? 6.254   21.933  37.215  1.00 54.41  ? 76  GLU C HB2    1 
ATOM   8810  H  HB3    . GLU D 1 77  ? 5.069   22.367  38.182  1.00 54.41  ? 76  GLU C HB3    1 
ATOM   8811  H  HG2    . GLU D 1 77  ? 4.200   23.798  36.665  1.00 53.54  ? 76  GLU C HG2    1 
ATOM   8812  H  HG3    . GLU D 1 77  ? 5.576   23.940  35.883  1.00 53.54  ? 76  GLU C HG3    1 
ATOM   8813  N  N      . GLY D 1 78  ? 8.327   22.471  39.738  1.00 41.46  ? 77  GLY C N      1 
ATOM   8814  C  CA     . GLY D 1 78  ? 8.793   21.878  40.981  1.00 42.06  ? 77  GLY C CA     1 
ATOM   8815  C  C      . GLY D 1 78  ? 10.262  21.525  40.901  1.00 43.01  ? 77  GLY C C      1 
ATOM   8816  O  O      . GLY D 1 78  ? 10.847  21.445  39.813  1.00 44.53  ? 77  GLY C O      1 
ATOM   8817  H  H      . GLY D 1 78  ? 8.897   22.433  39.095  1.00 49.79  ? 77  GLY C H      1 
ATOM   8818  H  HA2    . GLY D 1 78  ? 8.663   22.505  41.710  1.00 50.50  ? 77  GLY C HA2    1 
ATOM   8819  H  HA3    . GLY D 1 78  ? 8.289   21.070  41.166  1.00 50.50  ? 77  GLY C HA3    1 
ATOM   8820  N  N      . PHE D 1 79  ? 10.845  21.260  42.076  1.00 46.12  ? 78  PHE C N      1 
ATOM   8821  C  CA     . PHE D 1 79  ? 12.290  21.277  42.221  1.00 39.65  ? 78  PHE C CA     1 
ATOM   8822  C  C      . PHE D 1 79  ? 12.816  20.137  43.074  1.00 44.43  ? 78  PHE C C      1 
ATOM   8823  O  O      . PHE D 1 79  ? 12.394  19.943  44.215  1.00 47.32  ? 78  PHE C O      1 
ATOM   8824  C  CB     . PHE D 1 79  ? 12.682  22.647  42.795  1.00 45.44  ? 78  PHE C CB     1 
ATOM   8825  C  CG     . PHE D 1 79  ? 12.236  23.767  41.911  1.00 46.53  ? 78  PHE C CG     1 
ATOM   8826  C  CD1    . PHE D 1 79  ? 10.929  24.230  41.947  1.00 42.55  ? 78  PHE C CD1    1 
ATOM   8827  C  CD2    . PHE D 1 79  ? 13.099  24.286  40.955  1.00 45.08  ? 78  PHE C CD2    1 
ATOM   8828  C  CE1    . PHE D 1 79  ? 10.511  25.220  41.074  1.00 43.36  ? 78  PHE C CE1    1 
ATOM   8829  C  CE2    . PHE D 1 79  ? 12.687  25.275  40.106  1.00 45.29  ? 78  PHE C CE2    1 
ATOM   8830  C  CZ     . PHE D 1 79  ? 11.400  25.743  40.158  1.00 43.82  ? 78  PHE C CZ     1 
ATOM   8831  H  H      . PHE D 1 79  ? 10.418  21.069  42.798  1.00 55.37  ? 78  PHE C H      1 
ATOM   8832  H  HA     . PHE D 1 79  ? 12.704  21.116  41.358  1.00 47.61  ? 78  PHE C HA     1 
ATOM   8833  H  HB2    . PHE D 1 79  ? 12.265  22.761  43.664  1.00 54.56  ? 78  PHE C HB2    1 
ATOM   8834  H  HB3    . PHE D 1 79  ? 13.647  22.693  42.882  1.00 54.56  ? 78  PHE C HB3    1 
ATOM   8835  H  HD1    . PHE D 1 79  ? 10.330  23.874  42.562  1.00 51.10  ? 78  PHE C HD1    1 
ATOM   8836  H  HD2    . PHE D 1 79  ? 13.966  23.957  40.891  1.00 54.13  ? 78  PHE C HD2    1 
ATOM   8837  H  HE1    . PHE D 1 79  ? 9.635   25.530  41.104  1.00 52.07  ? 78  PHE C HE1    1 
ATOM   8838  H  HE2    . PHE D 1 79  ? 13.284  25.633  39.490  1.00 54.39  ? 78  PHE C HE2    1 
ATOM   8839  H  HZ     . PHE D 1 79  ? 11.126  26.413  39.576  1.00 52.62  ? 78  PHE C HZ     1 
ATOM   8840  N  N      . LEU D 1 80  ? 13.747  19.377  42.489  1.00 41.79  ? 79  LEU C N      1 
ATOM   8841  C  CA     . LEU D 1 80  ? 14.497  18.333  43.190  1.00 45.05  ? 79  LEU C CA     1 
ATOM   8842  C  C      . LEU D 1 80  ? 15.797  18.936  43.733  1.00 42.39  ? 79  LEU C C      1 
ATOM   8843  O  O      . LEU D 1 80  ? 16.674  19.333  42.968  1.00 41.06  ? 79  LEU C O      1 
ATOM   8844  C  CB     . LEU D 1 80  ? 14.754  17.177  42.220  1.00 42.97  ? 79  LEU C CB     1 
ATOM   8845  C  CG     . LEU D 1 80  ? 14.906  15.767  42.765  1.00 48.41  ? 79  LEU C CG     1 
ATOM   8846  C  CD1    . LEU D 1 80  ? 13.523  15.126  42.910  1.00 45.45  ? 79  LEU C CD1    1 
ATOM   8847  C  CD2    . LEU D 1 80  ? 15.796  14.895  41.869  1.00 43.38  ? 79  LEU C CD2    1 
ATOM   8848  H  H      . LEU D 1 80  ? 13.967  19.450  41.661  1.00 50.19  ? 79  LEU C H      1 
ATOM   8849  H  HA     . LEU D 1 80  ? 13.998  18.001  43.953  1.00 54.09  ? 79  LEU C HA     1 
ATOM   8850  H  HB2    . LEU D 1 80  ? 14.011  17.150  41.598  1.00 51.59  ? 79  LEU C HB2    1 
ATOM   8851  H  HB3    . LEU D 1 80  ? 15.577  17.376  41.745  1.00 51.59  ? 79  LEU C HB3    1 
ATOM   8852  H  HG     . LEU D 1 80  ? 15.338  15.818  43.632  1.00 58.13  ? 79  LEU C HG     1 
ATOM   8853  H  HD11   . LEU D 1 80  ? 13.628  14.223  43.248  1.00 54.57  ? 79  LEU C HD11   1 
ATOM   8854  H  HD12   . LEU D 1 80  ? 12.995  15.652  43.530  1.00 54.57  ? 79  LEU C HD12   1 
ATOM   8855  H  HD13   . LEU D 1 80  ? 13.092  15.106  42.041  1.00 54.57  ? 79  LEU C HD13   1 
ATOM   8856  H  HD21   . LEU D 1 80  ? 15.866  14.010  42.259  1.00 52.09  ? 79  LEU C HD21   1 
ATOM   8857  H  HD22   . LEU D 1 80  ? 15.397  14.837  40.987  1.00 52.09  ? 79  LEU C HD22   1 
ATOM   8858  H  HD23   . LEU D 1 80  ? 16.676  15.300  41.808  1.00 52.09  ? 79  LEU C HD23   1 
ATOM   8859  N  N      . CYS D 1 81  ? 15.927  18.997  45.047  1.00 38.71  ? 80  CYS C N      1 
ATOM   8860  C  CA     . CYS D 1 81  ? 17.062  19.680  45.696  1.00 40.98  ? 80  CYS C CA     1 
ATOM   8861  C  C      . CYS D 1 81  ? 18.047  18.630  46.192  1.00 44.47  ? 80  CYS C C      1 
ATOM   8862  O  O      . CYS D 1 81  ? 17.811  17.977  47.219  1.00 43.31  ? 80  CYS C O      1 
ATOM   8863  C  CB     . CYS D 1 81  ? 16.568  20.554  46.833  1.00 46.23  ? 80  CYS C CB     1 
ATOM   8864  S  SG     . CYS D 1 81  ? 15.471  21.788  46.224  1.00 51.17  ? 80  CYS C SG     1 
ATOM   8865  H  H      . CYS D 1 81  ? 15.369  18.649  45.601  1.00 46.48  ? 80  CYS C H      1 
ATOM   8866  H  HA     . CYS D 1 81  ? 17.518  20.234  45.043  1.00 49.20  ? 80  CYS C HA     1 
ATOM   8867  H  HB2    . CYS D 1 81  ? 16.093  20.009  47.479  1.00 55.51  ? 80  CYS C HB2    1 
ATOM   8868  H  HB3    . CYS D 1 81  ? 17.322  20.992  47.258  1.00 55.51  ? 80  CYS C HB3    1 
ATOM   8869  H  HG     . CYS D 1 81  ? 15.124  22.487  47.135  1.00 61.44  ? 80  CYS C HG     1 
ATOM   8870  N  N      . VAL D 1 82  ? 19.159  18.465  45.454  1.00 40.44  ? 81  VAL C N      1 
ATOM   8871  C  CA     . VAL D 1 82  ? 20.115  17.401  45.750  1.00 43.72  ? 81  VAL C CA     1 
ATOM   8872  C  C      . VAL D 1 82  ? 21.300  17.940  46.557  1.00 38.95  ? 81  VAL C C      1 
ATOM   8873  O  O      . VAL D 1 82  ? 21.884  18.982  46.220  1.00 43.60  ? 81  VAL C O      1 
ATOM   8874  C  CB     . VAL D 1 82  ? 20.587  16.727  44.451  1.00 40.43  ? 81  VAL C CB     1 
ATOM   8875  C  CG1    . VAL D 1 82  ? 21.406  15.490  44.763  1.00 41.97  ? 81  VAL C CG1    1 
ATOM   8876  C  CG2    . VAL D 1 82  ? 19.379  16.360  43.551  1.00 39.88  ? 81  VAL C CG2    1 
ATOM   8877  H  H      . VAL D 1 82  ? 19.373  18.958  44.782  1.00 48.56  ? 81  VAL C H      1 
ATOM   8878  H  HA     . VAL D 1 82  ? 19.676  16.745  46.315  1.00 52.50  ? 81  VAL C HA     1 
ATOM   8879  H  HB     . VAL D 1 82  ? 21.147  17.352  43.964  1.00 48.55  ? 81  VAL C HB     1 
ATOM   8880  H  HG11   . VAL D 1 82  ? 21.603  15.025  43.935  1.00 50.39  ? 81  VAL C HG11   1 
ATOM   8881  H  HG12   . VAL D 1 82  ? 22.231  15.758  45.197  1.00 50.39  ? 81  VAL C HG12   1 
ATOM   8882  H  HG13   . VAL D 1 82  ? 20.894  14.913  45.352  1.00 50.39  ? 81  VAL C HG13   1 
ATOM   8883  H  HG21   . VAL D 1 82  ? 19.693  15.830  42.802  1.00 47.88  ? 81  VAL C HG21   1 
ATOM   8884  H  HG22   . VAL D 1 82  ? 18.740  15.851  44.072  1.00 47.88  ? 81  VAL C HG22   1 
ATOM   8885  H  HG23   . VAL D 1 82  ? 18.967  17.177  43.228  1.00 47.88  ? 81  VAL C HG23   1 
ATOM   8886  N  N      . PHE D 1 83  ? 21.651  17.227  47.628  1.00 41.94  ? 82  PHE C N      1 
ATOM   8887  C  CA     . PHE D 1 83  ? 22.961  17.290  48.269  1.00 46.20  ? 82  PHE C CA     1 
ATOM   8888  C  C      . PHE D 1 83  ? 23.528  15.872  48.316  1.00 45.35  ? 82  PHE C C      1 
ATOM   8889  O  O      . PHE D 1 83  ? 22.843  14.899  47.978  1.00 42.91  ? 82  PHE C O      1 
ATOM   8890  C  CB     . PHE D 1 83  ? 22.882  17.888  49.668  1.00 37.15  ? 82  PHE C CB     1 
ATOM   8891  C  CG     . PHE D 1 83  ? 22.347  16.927  50.725  1.00 44.44  ? 82  PHE C CG     1 
ATOM   8892  C  CD1    . PHE D 1 83  ? 20.982  16.669  50.837  1.00 44.90  ? 82  PHE C CD1    1 
ATOM   8893  C  CD2    . PHE D 1 83  ? 23.215  16.292  51.605  1.00 40.02  ? 82  PHE C CD2    1 
ATOM   8894  C  CE1    . PHE D 1 83  ? 20.490  15.784  51.801  1.00 44.29  ? 82  PHE C CE1    1 
ATOM   8895  C  CE2    . PHE D 1 83  ? 22.734  15.407  52.576  1.00 46.20  ? 82  PHE C CE2    1 
ATOM   8896  C  CZ     . PHE D 1 83  ? 21.366  15.145  52.663  1.00 44.52  ? 82  PHE C CZ     1 
ATOM   8897  H  H      . PHE D 1 83  ? 21.120  16.673  48.017  1.00 50.36  ? 82  PHE C H      1 
ATOM   8898  H  HA     . PHE D 1 83  ? 23.556  17.861  47.758  1.00 55.47  ? 82  PHE C HA     1 
ATOM   8899  H  HB2    . PHE D 1 83  ? 23.772  18.161  49.941  1.00 44.41  ? 82  PHE C HB2    1 
ATOM   8900  H  HB3    . PHE D 1 83  ? 22.292  18.658  49.645  1.00 44.41  ? 82  PHE C HB3    1 
ATOM   8901  H  HD1    . PHE D 1 83  ? 20.388  17.093  50.260  1.00 53.91  ? 82  PHE C HD1    1 
ATOM   8902  H  HD2    . PHE D 1 83  ? 24.128  16.457  51.548  1.00 48.05  ? 82  PHE C HD2    1 
ATOM   8903  H  HE1    . PHE D 1 83  ? 19.576  15.624  51.864  1.00 53.18  ? 82  PHE C HE1    1 
ATOM   8904  H  HE2    . PHE D 1 83  ? 23.325  14.994  53.163  1.00 55.47  ? 82  PHE C HE2    1 
ATOM   8905  H  HZ     . PHE D 1 83  ? 21.045  14.544  53.296  1.00 53.46  ? 82  PHE C HZ     1 
ATOM   8906  N  N      . ALA D 1 84  ? 24.783  15.746  48.748  1.00 43.86  ? 83  ALA C N      1 
ATOM   8907  C  CA     . ALA D 1 84  ? 25.458  14.450  48.779  1.00 42.05  ? 83  ALA C CA     1 
ATOM   8908  C  C      . ALA D 1 84  ? 25.865  14.145  50.215  1.00 45.14  ? 83  ALA C C      1 
ATOM   8909  O  O      . ALA D 1 84  ? 26.462  15.001  50.895  1.00 45.53  ? 83  ALA C O      1 
ATOM   8910  C  CB     . ALA D 1 84  ? 26.670  14.417  47.838  1.00 44.44  ? 83  ALA C CB     1 
ATOM   8911  H  H      . ALA D 1 84  ? 25.265  16.400  49.028  1.00 52.66  ? 83  ALA C H      1 
ATOM   8912  H  HA     . ALA D 1 84  ? 24.849  13.755  48.482  1.00 50.49  ? 83  ALA C HA     1 
ATOM   8913  H  HB1    . ALA D 1 84  ? 27.120  13.563  47.933  1.00 53.36  ? 83  ALA C HB1    1 
ATOM   8914  H  HB2    . ALA D 1 84  ? 26.363  14.530  46.924  1.00 53.36  ? 83  ALA C HB2    1 
ATOM   8915  H  HB3    . ALA D 1 84  ? 27.274  15.138  48.075  1.00 53.36  ? 83  ALA C HB3    1 
ATOM   8916  N  N      . ILE D 1 85  ? 25.518  12.927  50.671  1.00 45.93  ? 84  ILE C N      1 
ATOM   8917  C  CA     . ILE D 1 85  ? 25.599  12.576  52.087  1.00 43.08  ? 84  ILE C CA     1 
ATOM   8918  C  C      . ILE D 1 85  ? 27.028  12.477  52.574  1.00 48.98  ? 84  ILE C C      1 
ATOM   8919  O  O      . ILE D 1 85  ? 27.261  12.349  53.784  1.00 52.16  ? 84  ILE C O      1 
ATOM   8920  C  CB     . ILE D 1 85  ? 24.813  11.271  52.377  1.00 49.15  ? 84  ILE C CB     1 
ATOM   8921  C  CG1    . ILE D 1 85  ? 25.328  10.056  51.586  1.00 50.24  ? 84  ILE C CG1    1 
ATOM   8922  C  CG2    . ILE D 1 85  ? 23.307  11.484  52.117  1.00 45.43  ? 84  ILE C CG2    1 
ATOM   8923  C  CD1    . ILE D 1 85  ? 26.375  9.195   52.321  1.00 51.36  ? 84  ILE C CD1    1 
ATOM   8924  H  H      . ILE D 1 85  ? 25.232  12.288  50.172  1.00 55.15  ? 84  ILE C H      1 
ATOM   8925  H  HA     . ILE D 1 85  ? 25.171  13.278  52.603  1.00 51.73  ? 84  ILE C HA     1 
ATOM   8926  H  HB     . ILE D 1 85  ? 24.960  11.068  53.314  1.00 59.02  ? 84  ILE C HB     1 
ATOM   8927  H  HG12   . ILE D 1 85  ? 24.574  9.482   51.379  1.00 60.33  ? 84  ILE C HG12   1 
ATOM   8928  H  HG13   . ILE D 1 85  ? 25.737  10.375  50.766  1.00 60.33  ? 84  ILE C HG13   1 
ATOM   8929  H  HG21   . ILE D 1 85  ? 22.828  10.672  52.346  1.00 54.54  ? 84  ILE C HG21   1 
ATOM   8930  H  HG22   . ILE D 1 85  ? 22.992  12.219  52.667  1.00 54.54  ? 84  ILE C HG22   1 
ATOM   8931  H  HG23   . ILE D 1 85  ? 23.174  11.693  51.179  1.00 54.54  ? 84  ILE C HG23   1 
ATOM   8932  H  HD11   . ILE D 1 85  ? 26.572  8.411   51.785  1.00 61.66  ? 84  ILE C HD11   1 
ATOM   8933  H  HD12   . ILE D 1 85  ? 27.182  9.719   52.448  1.00 61.66  ? 84  ILE C HD12   1 
ATOM   8934  H  HD13   . ILE D 1 85  ? 26.016  8.926   53.181  1.00 61.66  ? 84  ILE C HD13   1 
ATOM   8935  N  N      . ASN D 1 86  ? 28.001  12.581  51.673  1.00 48.91  ? 85  ASN C N      1 
ATOM   8936  C  CA     . ASN D 1 86  ? 29.388  12.773  52.071  1.00 53.60  ? 85  ASN C CA     1 
ATOM   8937  C  C      . ASN D 1 86  ? 29.883  14.186  51.777  1.00 48.53  ? 85  ASN C C      1 
ATOM   8938  O  O      . ASN D 1 86  ? 31.097  14.421  51.779  1.00 51.04  ? 85  ASN C O      1 
ATOM   8939  C  CB     . ASN D 1 86  ? 30.300  11.755  51.388  1.00 54.43  ? 85  ASN C CB     1 
ATOM   8940  C  CG     . ASN D 1 86  ? 30.584  12.105  49.935  1.00 51.91  ? 85  ASN C CG     1 
ATOM   8941  O  OD1    . ASN D 1 86  ? 29.744  12.694  49.241  1.00 48.27  ? 85  ASN C OD1    1 
ATOM   8942  N  ND2    . ASN D 1 86  ? 31.780  11.751  49.469  1.00 49.94  ? 85  ASN C ND2    1 
ATOM   8943  H  H      . ASN D 1 86  ? 27.880  12.543  50.822  1.00 58.72  ? 85  ASN C H      1 
ATOM   8944  H  HA     . ASN D 1 86  ? 29.442  12.626  53.028  1.00 64.36  ? 85  ASN C HA     1 
ATOM   8945  H  HB2    . ASN D 1 86  ? 31.147  11.722  51.860  1.00 65.35  ? 85  ASN C HB2    1 
ATOM   8946  H  HB3    . ASN D 1 86  ? 29.874  10.884  51.409  1.00 65.35  ? 85  ASN C HB3    1 
ATOM   8947  H  HD21   . ASN D 1 86  ? 31.992  11.925  48.654  1.00 59.96  ? 85  ASN C HD21   1 
ATOM   8948  H  HD22   . ASN D 1 86  ? 32.340  11.348  49.982  1.00 59.96  ? 85  ASN C HD22   1 
ATOM   8949  N  N      . ASN D 1 87  ? 28.973  15.136  51.548  1.00 45.79  ? 86  ASN C N      1 
ATOM   8950  C  CA     . ASN D 1 87  ? 29.350  16.530  51.264  1.00 52.46  ? 86  ASN C CA     1 
ATOM   8951  C  C      . ASN D 1 87  ? 28.562  17.488  52.157  1.00 48.16  ? 86  ASN C C      1 
ATOM   8952  O  O      . ASN D 1 87  ? 27.513  18.000  51.766  1.00 51.09  ? 86  ASN C O      1 
ATOM   8953  C  CB     . ASN D 1 87  ? 29.126  16.819  49.772  1.00 50.47  ? 86  ASN C CB     1 
ATOM   8954  C  CG     . ASN D 1 87  ? 29.750  18.121  49.303  1.00 47.76  ? 86  ASN C CG     1 
ATOM   8955  O  OD1    . ASN D 1 87  ? 30.129  18.983  50.105  1.00 45.62  ? 86  ASN C OD1    1 
ATOM   8956  N  ND2    . ASN D 1 87  ? 29.864  18.266  47.983  1.00 50.10  ? 86  ASN C ND2    1 
ATOM   8957  H  H      . ASN D 1 87  ? 28.124  14.998  51.550  1.00 54.98  ? 86  ASN C H      1 
ATOM   8958  H  HA     . ASN D 1 87  ? 30.283  16.657  51.499  1.00 62.98  ? 86  ASN C HA     1 
ATOM   8959  H  HB2    . ASN D 1 87  ? 29.517  16.099  49.252  1.00 60.60  ? 86  ASN C HB2    1 
ATOM   8960  H  HB3    . ASN D 1 87  ? 28.172  16.870  49.603  1.00 60.60  ? 86  ASN C HB3    1 
ATOM   8961  H  HD21   . ASN D 1 87  ? 30.210  18.982  47.657  1.00 60.15  ? 86  ASN C HD21   1 
ATOM   8962  H  HD22   . ASN D 1 87  ? 29.591  17.642  47.457  1.00 60.15  ? 86  ASN C HD22   1 
ATOM   8963  N  N      . THR D 1 88  ? 29.091  17.767  53.348  1.00 46.58  ? 87  THR C N      1 
ATOM   8964  C  CA     . THR D 1 88  ? 28.392  18.667  54.264  1.00 52.76  ? 87  THR C CA     1 
ATOM   8965  C  C      . THR D 1 88  ? 28.117  20.027  53.624  1.00 51.38  ? 87  THR C C      1 
ATOM   8966  O  O      . THR D 1 88  ? 27.047  20.615  53.833  1.00 51.58  ? 87  THR C O      1 
ATOM   8967  C  CB     . THR D 1 88  ? 29.204  18.849  55.553  1.00 51.68  ? 87  THR C CB     1 
ATOM   8968  O  OG1    . THR D 1 88  ? 29.416  17.563  56.158  1.00 55.11  ? 87  THR C OG1    1 
ATOM   8969  C  CG2    . THR D 1 88  ? 28.462  19.770  56.537  1.00 52.91  ? 87  THR C CG2    1 
ATOM   8970  H  H      . THR D 1 88  ? 29.835  17.455  53.645  1.00 55.93  ? 87  THR C H      1 
ATOM   8971  H  HA     . THR D 1 88  ? 27.540  18.264  54.491  1.00 63.35  ? 87  THR C HA     1 
ATOM   8972  H  HB     . THR D 1 88  ? 30.059  19.258  55.350  1.00 62.05  ? 87  THR C HB     1 
ATOM   8973  H  HG1    . THR D 1 88  ? 29.857  17.648  56.867  1.00 66.17  ? 87  THR C HG1    1 
ATOM   8974  H  HG21   . THR D 1 88  ? 28.893  19.744  57.405  1.00 63.53  ? 87  THR C HG21   1 
ATOM   8975  H  HG22   . THR D 1 88  ? 28.472  20.683  56.208  1.00 63.53  ? 87  THR C HG22   1 
ATOM   8976  H  HG23   . THR D 1 88  ? 27.542  19.480  56.633  1.00 63.53  ? 87  THR C HG23   1 
ATOM   8977  N  N      . LYS D 1 89  ? 29.073  20.543  52.845  1.00 51.37  ? 88  LYS C N      1 
ATOM   8978  C  CA     . LYS D 1 89  ? 28.889  21.833  52.186  1.00 53.84  ? 88  LYS C CA     1 
ATOM   8979  C  C      . LYS D 1 89  ? 27.665  21.815  51.259  1.00 50.39  ? 88  LYS C C      1 
ATOM   8980  O  O      . LYS D 1 89  ? 26.849  22.743  51.272  1.00 48.78  ? 88  LYS C O      1 
ATOM   8981  C  CB     . LYS D 1 89  ? 30.162  22.192  51.407  1.00 55.50  ? 88  LYS C CB     1 
ATOM   8982  C  CG     . LYS D 1 89  ? 30.141  23.562  50.752  1.00 57.20  ? 88  LYS C CG     1 
ATOM   8983  C  CD     . LYS D 1 89  ? 31.529  24.240  50.778  1.00 64.66  ? 88  LYS C CD     1 
ATOM   8984  C  CE     . LYS D 1 89  ? 32.639  23.406  50.127  1.00 64.39  ? 88  LYS C CE     1 
ATOM   8985  N  NZ     . LYS D 1 89  ? 33.924  24.175  49.992  1.00 70.83  ? 88  LYS C NZ     1 
ATOM   8986  H  H      . LYS D 1 89  ? 29.830  20.168  52.685  1.00 61.67  ? 88  LYS C H      1 
ATOM   8987  H  HA     . LYS D 1 89  ? 28.737  22.516  52.857  1.00 64.64  ? 88  LYS C HA     1 
ATOM   8988  H  HB2    . LYS D 1 89  ? 30.914  22.173  52.020  1.00 66.63  ? 88  LYS C HB2    1 
ATOM   8989  H  HB3    . LYS D 1 89  ? 30.289  21.535  50.705  1.00 66.63  ? 88  LYS C HB3    1 
ATOM   8990  H  HG2    . LYS D 1 89  ? 29.867  23.469  49.826  1.00 68.67  ? 88  LYS C HG2    1 
ATOM   8991  H  HG3    . LYS D 1 89  ? 29.516  24.133  51.226  1.00 68.67  ? 88  LYS C HG3    1 
ATOM   8992  H  HD2    . LYS D 1 89  ? 31.475  25.083  50.301  1.00 77.62  ? 88  LYS C HD2    1 
ATOM   8993  H  HD3    . LYS D 1 89  ? 31.782  24.397  51.702  1.00 77.62  ? 88  LYS C HD3    1 
ATOM   8994  H  HE2    . LYS D 1 89  ? 32.811  22.623  50.672  1.00 77.30  ? 88  LYS C HE2    1 
ATOM   8995  H  HE3    . LYS D 1 89  ? 32.354  23.136  49.239  1.00 77.30  ? 88  LYS C HE3    1 
ATOM   8996  H  HZ1    . LYS D 1 89  ? 34.545  23.665  49.608  1.00 85.03  ? 88  LYS C HZ1    1 
ATOM   8997  H  HZ2    . LYS D 1 89  ? 33.795  24.899  49.492  1.00 85.03  ? 88  LYS C HZ2    1 
ATOM   8998  H  HZ3    . LYS D 1 89  ? 34.214  24.426  50.795  1.00 85.03  ? 88  LYS C HZ3    1 
ATOM   8999  N  N      . SER D 1 90  ? 27.516  20.766  50.447  1.00 49.13  ? 89  SER C N      1 
ATOM   9000  C  CA     . SER D 1 90  ? 26.332  20.701  49.596  1.00 47.68  ? 89  SER C CA     1 
ATOM   9001  C  C      . SER D 1 90  ? 25.049  20.650  50.424  1.00 45.39  ? 89  SER C C      1 
ATOM   9002  O  O      . SER D 1 90  ? 23.995  21.067  49.939  1.00 44.27  ? 89  SER C O      1 
ATOM   9003  C  CB     . SER D 1 90  ? 26.402  19.489  48.645  1.00 47.40  ? 89  SER C CB     1 
ATOM   9004  O  OG     . SER D 1 90  ? 26.321  18.254  49.366  1.00 50.44  ? 89  SER C OG     1 
ATOM   9005  H  H      . SER D 1 90  ? 28.064  20.108  50.374  1.00 58.98  ? 89  SER C H      1 
ATOM   9006  H  HA     . SER D 1 90  ? 26.308  21.494  49.039  1.00 57.25  ? 89  SER C HA     1 
ATOM   9007  H  HB2    . SER D 1 90  ? 25.660  19.537  48.021  1.00 56.91  ? 89  SER C HB2    1 
ATOM   9008  H  HB3    . SER D 1 90  ? 27.243  19.516  48.163  1.00 56.91  ? 89  SER C HB3    1 
ATOM   9009  H  HG     . SER D 1 90  ? 26.808  18.288  50.049  1.00 60.56  ? 89  SER C HG     1 
ATOM   9010  N  N      . PHE D 1 91  ? 25.119  20.176  51.666  1.00 49.96  ? 90  PHE C N      1 
ATOM   9011  C  CA     . PHE D 1 91  ? 23.945  20.167  52.540  1.00 50.63  ? 90  PHE C CA     1 
ATOM   9012  C  C      . PHE D 1 91  ? 23.679  21.567  53.088  1.00 47.81  ? 90  PHE C C      1 
ATOM   9013  O  O      . PHE D 1 91  ? 22.525  22.012  53.133  1.00 51.27  ? 90  PHE C O      1 
ATOM   9014  C  CB     . PHE D 1 91  ? 24.170  19.126  53.663  1.00 48.28  ? 90  PHE C CB     1 
ATOM   9015  C  CG     . PHE D 1 91  ? 22.991  18.919  54.596  1.00 51.29  ? 90  PHE C CG     1 
ATOM   9016  C  CD1    . PHE D 1 91  ? 21.775  18.450  54.134  1.00 50.07  ? 90  PHE C CD1    1 
ATOM   9017  C  CD2    . PHE D 1 91  ? 23.133  19.148  55.961  1.00 47.43  ? 90  PHE C CD2    1 
ATOM   9018  C  CE1    . PHE D 1 91  ? 20.704  18.252  55.012  1.00 50.04  ? 90  PHE C CE1    1 
ATOM   9019  C  CE2    . PHE D 1 91  ? 22.077  18.932  56.841  1.00 52.91  ? 90  PHE C CE2    1 
ATOM   9020  C  CZ     . PHE D 1 91  ? 20.867  18.490  56.369  1.00 49.56  ? 90  PHE C CZ     1 
ATOM   9021  H  H      . PHE D 1 91  ? 25.830  19.855  52.027  1.00 59.98  ? 90  PHE C H      1 
ATOM   9022  H  HA     . PHE D 1 91  ? 23.149  19.898  52.056  1.00 60.79  ? 90  PHE C HA     1 
ATOM   9023  H  HB2    . PHE D 1 91  ? 24.369  18.270  53.252  1.00 57.97  ? 90  PHE C HB2    1 
ATOM   9024  H  HB3    . PHE D 1 91  ? 24.921  19.416  54.204  1.00 57.97  ? 90  PHE C HB3    1 
ATOM   9025  H  HD1    . PHE D 1 91  ? 21.667  18.264  53.229  1.00 60.12  ? 90  PHE C HD1    1 
ATOM   9026  H  HD2    . PHE D 1 91  ? 23.948  19.451  56.291  1.00 56.95  ? 90  PHE C HD2    1 
ATOM   9027  H  HE1    . PHE D 1 91  ? 19.883  17.961  54.686  1.00 60.08  ? 90  PHE C HE1    1 
ATOM   9028  H  HE2    . PHE D 1 91  ? 22.191  19.086  57.751  1.00 63.52  ? 90  PHE C HE2    1 
ATOM   9029  H  HZ     . PHE D 1 91  ? 20.159  18.351  56.956  1.00 59.51  ? 90  PHE C HZ     1 
ATOM   9030  N  N      . GLU D 1 92  ? 24.736  22.265  53.495  1.00 53.38  ? 91  GLU C N      1 
ATOM   9031  C  CA     . GLU D 1 92  ? 24.609  23.655  53.929  1.00 48.85  ? 91  GLU C CA     1 
ATOM   9032  C  C      . GLU D 1 92  ? 24.047  24.532  52.814  1.00 57.99  ? 91  GLU C C      1 
ATOM   9033  O  O      . GLU D 1 92  ? 23.183  25.390  53.059  1.00 57.19  ? 91  GLU C O      1 
ATOM   9034  C  CB     . GLU D 1 92  ? 25.976  24.166  54.361  1.00 58.72  ? 91  GLU C CB     1 
ATOM   9035  C  CG     . GLU D 1 92  ? 26.671  23.329  55.457  1.00 60.98  ? 91  GLU C CG     1 
ATOM   9036  C  CD     . GLU D 1 92  ? 28.104  23.793  55.706  1.00 62.46  ? 91  GLU C CD     1 
ATOM   9037  O  OE1    . GLU D 1 92  ? 28.793  24.169  54.726  1.00 72.95  ? 91  GLU C OE1    1 
ATOM   9038  O  OE2    . GLU D 1 92  ? 28.539  23.786  56.871  1.00 75.13  ? 91  GLU C OE2    1 
ATOM   9039  H  H      . GLU D 1 92  ? 25.539  21.959  53.530  1.00 64.10  ? 91  GLU C H      1 
ATOM   9040  H  HA     . GLU D 1 92  ? 24.001  23.704  54.683  1.00 58.65  ? 91  GLU C HA     1 
ATOM   9041  H  HB2    . GLU D 1 92  ? 26.560  24.171  53.586  1.00 70.50  ? 91  GLU C HB2    1 
ATOM   9042  H  HB3    . GLU D 1 92  ? 25.872  25.067  54.704  1.00 70.50  ? 91  GLU C HB3    1 
ATOM   9043  H  HG2    . GLU D 1 92  ? 26.175  23.416  56.286  1.00 73.21  ? 91  GLU C HG2    1 
ATOM   9044  H  HG3    . GLU D 1 92  ? 26.696  22.400  55.181  1.00 73.21  ? 91  GLU C HG3    1 
ATOM   9045  N  N      . ASP D 1 93  ? 24.533  24.324  51.586  1.00 51.15  ? 92  ASP C N      1 
ATOM   9046  C  CA     . ASP D 1 93  ? 24.026  25.049  50.436  1.00 55.47  ? 92  ASP C CA     1 
ATOM   9047  C  C      . ASP D 1 93  ? 22.537  24.802  50.184  1.00 54.82  ? 92  ASP C C      1 
ATOM   9048  O  O      . ASP D 1 93  ? 21.883  25.619  49.520  1.00 57.78  ? 92  ASP C O      1 
ATOM   9049  C  CB     . ASP D 1 93  ? 24.790  24.640  49.160  1.00 56.13  ? 92  ASP C CB     1 
ATOM   9050  C  CG     . ASP D 1 93  ? 26.247  25.088  49.162  1.00 56.90  ? 92  ASP C CG     1 
ATOM   9051  O  OD1    . ASP D 1 93  ? 26.627  25.907  50.016  1.00 59.71  ? 92  ASP C OD1    1 
ATOM   9052  O  OD2    . ASP D 1 93  ? 26.997  24.613  48.281  1.00 53.91  ? 92  ASP C OD2    1 
ATOM   9053  H  H      . ASP D 1 93  ? 25.160  23.765  51.398  1.00 61.42  ? 92  ASP C H      1 
ATOM   9054  H  HA     . ASP D 1 93  ? 24.163  25.991  50.619  1.00 66.60  ? 92  ASP C HA     1 
ATOM   9055  H  HB2    . ASP D 1 93  ? 24.776  23.674  49.080  1.00 67.38  ? 92  ASP C HB2    1 
ATOM   9056  H  HB3    . ASP D 1 93  ? 24.357  25.043  48.391  1.00 67.38  ? 92  ASP C HB3    1 
ATOM   9057  N  N      . ILE D 1 94  ? 21.990  23.673  50.630  1.00 52.35  ? 93  ILE C N      1 
ATOM   9058  C  CA     . ILE D 1 94  ? 20.589  23.400  50.334  1.00 52.46  ? 93  ILE C CA     1 
ATOM   9059  C  C      . ILE D 1 94  ? 19.721  24.558  50.825  1.00 55.48  ? 93  ILE C C      1 
ATOM   9060  O  O      . ILE D 1 94  ? 18.844  25.053  50.105  1.00 52.85  ? 93  ILE C O      1 
ATOM   9061  C  CB     . ILE D 1 94  ? 20.151  22.052  50.946  1.00 53.79  ? 93  ILE C CB     1 
ATOM   9062  C  CG1    . ILE D 1 94  ? 20.711  20.842  50.155  1.00 44.73  ? 93  ILE C CG1    1 
ATOM   9063  C  CG2    . ILE D 1 94  ? 18.633  21.975  51.006  1.00 53.57  ? 93  ILE C CG2    1 
ATOM   9064  C  CD1    . ILE D 1 94  ? 20.091  20.541  48.802  1.00 43.36  ? 93  ILE C CD1    1 
ATOM   9065  H  H      . ILE D 1 94  ? 22.396  23.069  51.090  1.00 62.86  ? 93  ILE C H      1 
ATOM   9066  H  HA     . ILE D 1 94  ? 20.481  23.328  49.373  1.00 62.98  ? 93  ILE C HA     1 
ATOM   9067  H  HB     . ILE D 1 94  ? 20.519  22.012  51.843  1.00 64.58  ? 93  ILE C HB     1 
ATOM   9068  H  HG12   . ILE D 1 94  ? 21.656  20.998  50.002  1.00 53.72  ? 93  ILE C HG12   1 
ATOM   9069  H  HG13   . ILE D 1 94  ? 20.591  20.049  50.701  1.00 53.72  ? 93  ILE C HG13   1 
ATOM   9070  H  HG21   . ILE D 1 94  ? 18.374  21.108  51.356  1.00 64.32  ? 93  ILE C HG21   1 
ATOM   9071  H  HG22   . ILE D 1 94  ? 18.303  22.678  51.587  1.00 64.32  ? 93  ILE C HG22   1 
ATOM   9072  H  HG23   . ILE D 1 94  ? 18.275  22.091  50.112  1.00 64.32  ? 93  ILE C HG23   1 
ATOM   9073  H  HD11   . ILE D 1 94  ? 20.520  19.757  48.425  1.00 52.07  ? 93  ILE C HD11   1 
ATOM   9074  H  HD12   . ILE D 1 94  ? 19.142  20.374  48.919  1.00 52.07  ? 93  ILE C HD12   1 
ATOM   9075  H  HD13   . ILE D 1 94  ? 20.223  21.303  48.217  1.00 52.07  ? 93  ILE C HD13   1 
ATOM   9076  N  N      . HIS D 1 95  ? 19.938  24.998  52.072  1.00 56.69  ? 94  HIS C N      1 
ATOM   9077  C  CA     . HIS D 1 95  ? 19.242  26.189  52.544  1.00 59.42  ? 94  HIS C CA     1 
ATOM   9078  C  C      . HIS D 1 95  ? 19.198  27.259  51.446  1.00 63.95  ? 94  HIS C C      1 
ATOM   9079  O  O      . HIS D 1 95  ? 18.136  27.817  51.135  1.00 61.30  ? 94  HIS C O      1 
ATOM   9080  C  CB     . HIS D 1 95  ? 19.937  26.747  53.782  1.00 63.04  ? 94  HIS C CB     1 
ATOM   9081  C  CG     . HIS D 1 95  ? 19.504  28.133  54.140  1.00 69.57  ? 94  HIS C CG     1 
ATOM   9082  N  ND1    . HIS D 1 95  ? 20.196  29.255  53.734  1.00 69.94  ? 94  HIS C ND1    1 
ATOM   9083  C  CD2    . HIS D 1 95  ? 18.460  28.581  54.878  1.00 67.16  ? 94  HIS C CD2    1 
ATOM   9084  C  CE1    . HIS D 1 95  ? 19.595  30.333  54.207  1.00 67.93  ? 94  HIS C CE1    1 
ATOM   9085  N  NE2    . HIS D 1 95  ? 18.539  29.953  54.899  1.00 61.07  ? 94  HIS C NE2    1 
ATOM   9086  H  H      . HIS D 1 95  ? 20.468  24.633  52.642  1.00 68.07  ? 94  HIS C H      1 
ATOM   9087  H  HA     . HIS D 1 95  ? 18.336  25.946  52.792  1.00 71.34  ? 94  HIS C HA     1 
ATOM   9088  H  HB2    . HIS D 1 95  ? 19.740  26.170  54.537  1.00 75.69  ? 94  HIS C HB2    1 
ATOM   9089  H  HB3    . HIS D 1 95  ? 20.893  26.767  53.620  1.00 75.69  ? 94  HIS C HB3    1 
ATOM   9090  H  HD2    . HIS D 1 95  ? 17.812  28.059  55.293  1.00 80.63  ? 94  HIS C HD2    1 
ATOM   9091  H  HE1    . HIS D 1 95  ? 19.871  31.212  54.074  1.00 81.55  ? 94  HIS C HE1    1 
ATOM   9092  H  HE2    . HIS D 1 95  ? 17.989  30.479  55.300  1.00 73.32  ? 94  HIS C HE2    1 
ATOM   9093  N  N      . HIS D 1 96  ? 20.348  27.516  50.816  1.00 59.97  ? 95  HIS C N      1 
ATOM   9094  C  CA     . HIS D 1 96  ? 20.452  28.635  49.886  1.00 60.88  ? 95  HIS C CA     1 
ATOM   9095  C  C      . HIS D 1 96  ? 19.590  28.426  48.647  1.00 57.65  ? 95  HIS C C      1 
ATOM   9096  O  O      . HIS D 1 96  ? 18.816  29.311  48.267  1.00 60.12  ? 95  HIS C O      1 
ATOM   9097  C  CB     . HIS D 1 96  ? 21.921  28.863  49.517  1.00 60.20  ? 95  HIS C CB     1 
ATOM   9098  C  CG     . HIS D 1 96  ? 22.729  29.436  50.640  1.00 65.38  ? 95  HIS C CG     1 
ATOM   9099  N  ND1    . HIS D 1 96  ? 22.336  30.560  51.338  1.00 66.43  ? 95  HIS C ND1    1 
ATOM   9100  C  CD2    . HIS D 1 96  ? 23.892  29.031  51.205  1.00 67.14  ? 95  HIS C CD2    1 
ATOM   9101  C  CE1    . HIS D 1 96  ? 23.221  30.822  52.283  1.00 65.91  ? 95  HIS C CE1    1 
ATOM   9102  N  NE2    . HIS D 1 96  ? 24.178  29.912  52.219  1.00 65.38  ? 95  HIS C NE2    1 
ATOM   9103  H  H      . HIS D 1 96  ? 21.072  27.062  50.909  1.00 72.00  ? 95  HIS C H      1 
ATOM   9104  H  HA     . HIS D 1 96  ? 20.124  29.436  50.323  1.00 73.09  ? 95  HIS C HA     1 
ATOM   9105  H  HB2    . HIS D 1 96  ? 22.317  28.014  49.266  1.00 72.28  ? 95  HIS C HB2    1 
ATOM   9106  H  HB3    . HIS D 1 96  ? 21.965  29.482  48.771  1.00 72.28  ? 95  HIS C HB3    1 
ATOM   9107  H  HD2    . HIS D 1 96  ? 24.401  28.294  50.953  1.00 80.60  ? 95  HIS C HD2    1 
ATOM   9108  H  HE1    . HIS D 1 96  ? 23.178  31.526  52.889  1.00 79.13  ? 95  HIS C HE1    1 
ATOM   9109  H  HE2    . HIS D 1 96  ? 24.869  29.878  52.731  1.00 78.49  ? 95  HIS C HE2    1 
ATOM   9110  N  N      . TYR D 1 97  ? 19.720  27.281  47.977  1.00 57.27  ? 96  TYR C N      1 
ATOM   9111  C  CA     . TYR D 1 97  ? 18.842  27.042  46.832  1.00 58.07  ? 96  TYR C CA     1 
ATOM   9112  C  C      . TYR D 1 97  ? 17.376  27.201  47.232  1.00 56.26  ? 96  TYR C C      1 
ATOM   9113  O  O      . TYR D 1 97  ? 16.541  27.619  46.411  1.00 53.52  ? 96  TYR C O      1 
ATOM   9114  C  CB     . TYR D 1 97  ? 19.048  25.649  46.236  1.00 55.21  ? 96  TYR C CB     1 
ATOM   9115  C  CG     . TYR D 1 97  ? 20.360  25.422  45.506  1.00 54.45  ? 96  TYR C CG     1 
ATOM   9116  C  CD1    . TYR D 1 97  ? 21.477  24.973  46.197  1.00 54.15  ? 96  TYR C CD1    1 
ATOM   9117  C  CD2    . TYR D 1 97  ? 20.472  25.614  44.134  1.00 51.56  ? 96  TYR C CD2    1 
ATOM   9118  C  CE1    . TYR D 1 97  ? 22.684  24.745  45.553  1.00 54.09  ? 96  TYR C CE1    1 
ATOM   9119  C  CE2    . TYR D 1 97  ? 21.691  25.384  43.473  1.00 54.96  ? 96  TYR C CE2    1 
ATOM   9120  C  CZ     . TYR D 1 97  ? 22.794  24.947  44.214  1.00 54.60  ? 96  TYR C CZ     1 
ATOM   9121  O  OH     . TYR D 1 97  ? 24.023  24.711  43.612  1.00 56.72  ? 96  TYR C OH     1 
ATOM   9122  H  H      . TYR D 1 97  ? 20.281  26.654  48.157  1.00 68.75  ? 96  TYR C H      1 
ATOM   9123  H  HA     . TYR D 1 97  ? 19.073  27.686  46.143  1.00 69.72  ? 96  TYR C HA     1 
ATOM   9124  H  HB2    . TYR D 1 97  ? 19.007  25.003  46.958  1.00 66.28  ? 96  TYR C HB2    1 
ATOM   9125  H  HB3    . TYR D 1 97  ? 18.334  25.483  45.601  1.00 66.28  ? 96  TYR C HB3    1 
ATOM   9126  H  HD1    . TYR D 1 97  ? 21.414  24.821  47.113  1.00 65.02  ? 96  TYR C HD1    1 
ATOM   9127  H  HD2    . TYR D 1 97  ? 19.731  25.897  43.647  1.00 61.91  ? 96  TYR C HD2    1 
ATOM   9128  H  HE1    . TYR D 1 97  ? 23.421  24.454  46.039  1.00 64.94  ? 96  TYR C HE1    1 
ATOM   9129  H  HE2    . TYR D 1 97  ? 21.764  25.522  42.556  1.00 65.99  ? 96  TYR C HE2    1 
ATOM   9130  H  HH     . TYR D 1 97  ? 24.601  24.539  44.197  1.00 68.10  ? 96  TYR C HH     1 
ATOM   9131  N  N      . ARG D 1 98  ? 17.047  26.874  48.488  1.00 60.39  ? 97  ARG C N      1 
ATOM   9132  C  CA     . ARG D 1 98  ? 15.663  26.965  48.934  1.00 57.52  ? 97  ARG C CA     1 
ATOM   9133  C  C      . ARG D 1 98  ? 15.223  28.414  49.021  1.00 57.45  ? 97  ARG C C      1 
ATOM   9134  O  O      . ARG D 1 98  ? 14.217  28.805  48.415  1.00 60.15  ? 97  ARG C O      1 
ATOM   9135  C  CB     . ARG D 1 98  ? 15.468  26.270  50.282  1.00 59.04  ? 97  ARG C CB     1 
ATOM   9136  C  CG     . ARG D 1 98  ? 14.000  25.849  50.489  1.00 53.12  ? 97  ARG C CG     1 
ATOM   9137  C  CD     . ARG D 1 98  ? 13.654  25.492  51.920  1.00 59.37  ? 97  ARG C CD     1 
ATOM   9138  N  NE     . ARG D 1 98  ? 12.213  25.358  52.110  1.00 53.77  ? 97  ARG C NE     1 
ATOM   9139  C  CZ     . ARG D 1 98  ? 11.494  26.084  52.959  1.00 61.57  ? 97  ARG C CZ     1 
ATOM   9140  N  NH1    . ARG D 1 98  ? 12.036  27.073  53.651  1.00 58.36  ? 97  ARG C NH1    1 
ATOM   9141  N  NH2    . ARG D 1 98  ? 10.203  25.805  53.115  1.00 53.99  ? 97  ARG C NH2    1 
ATOM   9142  H  H      . ARG D 1 98  ? 17.601  26.601  49.088  1.00 72.50  ? 97  ARG C H      1 
ATOM   9143  H  HA     . ARG D 1 98  ? 15.107  26.503  48.287  1.00 69.06  ? 97  ARG C HA     1 
ATOM   9144  H  HB2    . ARG D 1 98  ? 16.022  25.475  50.317  1.00 70.88  ? 97  ARG C HB2    1 
ATOM   9145  H  HB3    . ARG D 1 98  ? 15.716  26.879  50.996  1.00 70.88  ? 97  ARG C HB3    1 
ATOM   9146  H  HG2    . ARG D 1 98  ? 13.425  26.584  50.223  1.00 63.78  ? 97  ARG C HG2    1 
ATOM   9147  H  HG3    . ARG D 1 98  ? 13.819  25.071  49.940  1.00 63.78  ? 97  ARG C HG3    1 
ATOM   9148  H  HD2    . ARG D 1 98  ? 14.071  24.646  52.148  1.00 71.28  ? 97  ARG C HD2    1 
ATOM   9149  H  HD3    . ARG D 1 98  ? 13.975  26.190  52.511  1.00 71.28  ? 97  ARG C HD3    1 
ATOM   9150  H  HE     . ARG D 1 98  ? 11.801  24.768  51.640  1.00 64.55  ? 97  ARG C HE     1 
ATOM   9151  H  HH11   . ARG D 1 98  ? 12.870  27.258  53.556  1.00 70.07  ? 97  ARG C HH11   1 
ATOM   9152  H  HH12   . ARG D 1 98  ? 11.553  27.531  54.196  1.00 70.07  ? 97  ARG C HH12   1 
ATOM   9153  H  HH21   . ARG D 1 98  ? 9.844   25.163  52.670  1.00 64.82  ? 97  ARG C HH21   1 
ATOM   9154  H  HH22   . ARG D 1 98  ? 9.726   26.268  53.662  1.00 64.82  ? 97  ARG C HH22   1 
ATOM   9155  N  N      . GLU D 1 99  ? 15.971  29.226  49.773  1.00 59.68  ? 98  GLU C N      1 
ATOM   9156  C  CA     . GLU D 1 99  ? 15.657  30.643  49.864  1.00 55.33  ? 98  GLU C CA     1 
ATOM   9157  C  C      . GLU D 1 99  ? 15.466  31.241  48.474  1.00 60.91  ? 98  GLU C C      1 
ATOM   9158  O  O      . GLU D 1 99  ? 14.432  31.870  48.201  1.00 63.15  ? 98  GLU C O      1 
ATOM   9159  C  CB     . GLU D 1 99  ? 16.753  31.361  50.644  1.00 62.19  ? 98  GLU C CB     1 
ATOM   9160  C  CG     . GLU D 1 99  ? 16.724  31.045  52.147  1.00 62.58  ? 98  GLU C CG     1 
ATOM   9161  C  CD     . GLU D 1 99  ? 15.506  31.629  52.847  1.00 62.35  ? 98  GLU C CD     1 
ATOM   9162  O  OE1    . GLU D 1 99  ? 15.429  32.863  53.009  1.00 58.99  ? 98  GLU C OE1    1 
ATOM   9163  O  OE2    . GLU D 1 99  ? 14.604  30.851  53.212  1.00 64.92  ? 98  GLU C OE2    1 
ATOM   9164  H  H      . GLU D 1 99  ? 16.656  28.980  50.231  1.00 71.65  ? 98  GLU C H      1 
ATOM   9165  H  HA     . GLU D 1 99  ? 14.828  30.767  50.352  1.00 66.43  ? 98  GLU C HA     1 
ATOM   9166  H  HB2    . GLU D 1 99  ? 17.616  31.087  50.297  1.00 74.67  ? 98  GLU C HB2    1 
ATOM   9167  H  HB3    . GLU D 1 99  ? 16.640  32.318  50.536  1.00 74.67  ? 98  GLU C HB3    1 
ATOM   9168  H  HG2    . GLU D 1 99  ? 16.707  30.083  52.269  1.00 75.13  ? 98  GLU C HG2    1 
ATOM   9169  H  HG3    . GLU D 1 99  ? 17.517  31.418  52.564  1.00 75.13  ? 98  GLU C HG3    1 
ATOM   9170  N  N      . GLN D 1 100 ? 16.417  30.995  47.554  1.00 51.70  ? 99  GLN C N      1 
ATOM   9171  C  CA     . GLN D 1 100 ? 16.319  31.610  46.243  1.00 52.17  ? 99  GLN C CA     1 
ATOM   9172  C  C      . GLN D 1 100 ? 15.023  31.214  45.545  1.00 58.01  ? 99  GLN C C      1 
ATOM   9173  O  O      . GLN D 1 100 ? 14.331  32.066  44.973  1.00 59.22  ? 99  GLN C O      1 
ATOM   9174  C  CB     . GLN D 1 100 ? 17.524  31.236  45.366  1.00 58.08  ? 99  GLN C CB     1 
ATOM   9175  C  CG     . GLN D 1 100 ? 17.575  32.049  44.041  1.00 59.80  ? 99  GLN C CG     1 
ATOM   9176  C  CD     . GLN D 1 100 ? 18.836  31.827  43.202  1.00 64.18  ? 99  GLN C CD     1 
ATOM   9177  O  OE1    . GLN D 1 100 ? 19.647  30.944  43.482  1.00 64.59  ? 99  GLN C OE1    1 
ATOM   9178  N  NE2    . GLN D 1 100 ? 18.987  32.625  42.148  1.00 64.29  ? 99  GLN C NE2    1 
ATOM   9179  H  H      . GLN D 1 100 ? 17.103  30.490  47.671  1.00 62.08  ? 99  GLN C H      1 
ATOM   9180  H  HA     . GLN D 1 100 ? 16.328  32.573  46.366  1.00 62.63  ? 99  GLN C HA     1 
ATOM   9181  H  HB2    . GLN D 1 100 ? 18.340  31.413  45.859  1.00 69.73  ? 99  GLN C HB2    1 
ATOM   9182  H  HB3    . GLN D 1 100 ? 17.470  30.295  45.140  1.00 69.73  ? 99  GLN C HB3    1 
ATOM   9183  H  HG2    . GLN D 1 100 ? 16.814  31.798  43.495  1.00 71.79  ? 99  GLN C HG2    1 
ATOM   9184  H  HG3    . GLN D 1 100 ? 17.531  32.994  44.257  1.00 71.79  ? 99  GLN C HG3    1 
ATOM   9185  H  HE21   . GLN D 1 100 ? 18.393  33.223  41.973  1.00 77.18  ? 99  GLN C HE21   1 
ATOM   9186  H  HE22   . GLN D 1 100 ? 19.677  32.544  41.642  1.00 77.18  ? 99  GLN C HE22   1 
ATOM   9187  N  N      . ILE D 1 101 ? 14.683  29.917  45.556  1.00 52.33  ? 100 ILE C N      1 
ATOM   9188  C  CA     . ILE D 1 101 ? 13.494  29.489  44.828  1.00 46.50  ? 100 ILE C CA     1 
ATOM   9189  C  C      . ILE D 1 101 ? 12.247  30.114  45.435  1.00 57.29  ? 100 ILE C C      1 
ATOM   9190  O  O      . ILE D 1 101 ? 11.354  30.581  44.712  1.00 58.80  ? 100 ILE C O      1 
ATOM   9191  C  CB     . ILE D 1 101 ? 13.380  27.954  44.790  1.00 54.96  ? 100 ILE C CB     1 
ATOM   9192  C  CG1    . ILE D 1 101 ? 14.539  27.368  43.986  1.00 54.30  ? 100 ILE C CG1    1 
ATOM   9193  C  CG2    . ILE D 1 101 ? 12.053  27.533  44.124  1.00 53.16  ? 100 ILE C CG2    1 
ATOM   9194  C  CD1    . ILE D 1 101 ? 14.732  25.871  44.103  1.00 55.34  ? 100 ILE C CD1    1 
ATOM   9195  H  H      . ILE D 1 101 ? 15.112  29.293  45.964  1.00 62.84  ? 100 ILE C H      1 
ATOM   9196  H  HA     . ILE D 1 101 ? 13.584  29.799  43.914  1.00 55.84  ? 100 ILE C HA     1 
ATOM   9197  H  HB     . ILE D 1 101 ? 13.409  27.623  45.701  1.00 65.99  ? 100 ILE C HB     1 
ATOM   9198  H  HG12   . ILE D 1 101 ? 14.388  27.566  43.048  1.00 65.19  ? 100 ILE C HG12   1 
ATOM   9199  H  HG13   . ILE D 1 101 ? 15.360  27.788  44.286  1.00 65.19  ? 100 ILE C HG13   1 
ATOM   9200  H  HG21   . ILE D 1 101 ? 12.016  26.565  44.076  1.00 63.83  ? 100 ILE C HG21   1 
ATOM   9201  H  HG22   . ILE D 1 101 ? 11.313  27.866  44.657  1.00 63.83  ? 100 ILE C HG22   1 
ATOM   9202  H  HG23   . ILE D 1 101 ? 12.013  27.911  43.232  1.00 63.83  ? 100 ILE C HG23   1 
ATOM   9203  H  HD11   . ILE D 1 101 ? 15.434  25.595  43.493  1.00 66.44  ? 100 ILE C HD11   1 
ATOM   9204  H  HD12   . ILE D 1 101 ? 14.982  25.655  45.015  1.00 66.44  ? 100 ILE C HD12   1 
ATOM   9205  H  HD13   . ILE D 1 101 ? 13.901  25.427  43.874  1.00 66.44  ? 100 ILE C HD13   1 
ATOM   9206  N  N      . LYS D 1 102 ? 12.144  30.108  46.766  1.00 50.04  ? 101 LYS C N      1 
ATOM   9207  C  CA     . LYS D 1 102 ? 11.014  30.766  47.399  1.00 59.01  ? 101 LYS C CA     1 
ATOM   9208  C  C      . LYS D 1 102 ? 10.924  32.218  46.940  1.00 59.92  ? 101 LYS C C      1 
ATOM   9209  O  O      . LYS D 1 102 ? 9.857   32.687  46.528  1.00 62.70  ? 101 LYS C O      1 
ATOM   9210  C  CB     . LYS D 1 102 ? 11.134  30.655  48.928  1.00 61.25  ? 101 LYS C CB     1 
ATOM   9211  C  CG     . LYS D 1 102 ? 10.862  29.214  49.434  1.00 59.66  ? 101 LYS C CG     1 
ATOM   9212  C  CD     . LYS D 1 102 ? 10.704  29.097  50.957  1.00 65.00  ? 101 LYS C CD     1 
ATOM   9213  C  CE     . LYS D 1 102 ? 11.950  29.522  51.730  1.00 63.23  ? 101 LYS C CE     1 
ATOM   9214  N  NZ     . LYS D 1 102 ? 11.601  29.956  53.109  1.00 61.42  ? 101 LYS C NZ     1 
ATOM   9215  H  H      . LYS D 1 102 ? 12.703  29.739  47.306  1.00 60.09  ? 101 LYS C H      1 
ATOM   9216  H  HA     . LYS D 1 102 ? 10.190  30.323  47.146  1.00 70.85  ? 101 LYS C HA     1 
ATOM   9217  H  HB2    . LYS D 1 102 ? 12.032  30.906  49.195  1.00 73.54  ? 101 LYS C HB2    1 
ATOM   9218  H  HB3    . LYS D 1 102 ? 10.487  31.248  49.341  1.00 73.54  ? 101 LYS C HB3    1 
ATOM   9219  H  HG2    . LYS D 1 102 ? 10.042  28.893  49.028  1.00 71.63  ? 101 LYS C HG2    1 
ATOM   9220  H  HG3    . LYS D 1 102 ? 11.606  28.649  49.172  1.00 71.63  ? 101 LYS C HG3    1 
ATOM   9221  H  HD2    . LYS D 1 102 ? 9.970   29.664  51.241  1.00 78.03  ? 101 LYS C HD2    1 
ATOM   9222  H  HD3    . LYS D 1 102 ? 10.515  28.172  51.182  1.00 78.03  ? 101 LYS C HD3    1 
ATOM   9223  H  HE2    . LYS D 1 102 ? 12.564  28.774  51.790  1.00 75.91  ? 101 LYS C HE2    1 
ATOM   9224  H  HE3    . LYS D 1 102 ? 12.375  30.264  51.273  1.00 75.91  ? 101 LYS C HE3    1 
ATOM   9225  H  HZ1    . LYS D 1 102 ? 12.343  30.103  53.579  1.00 73.74  ? 101 LYS C HZ1    1 
ATOM   9226  H  HZ2    . LYS D 1 102 ? 11.124  30.707  53.081  1.00 73.74  ? 101 LYS C HZ2    1 
ATOM   9227  H  HZ3    . LYS D 1 102 ? 11.123  29.325  53.515  1.00 73.74  ? 101 LYS C HZ3    1 
ATOM   9228  N  N      . ARG D 1 103 ? 12.049  32.929  46.960  1.00 53.85  ? 102 ARG C N      1 
ATOM   9229  C  CA     . ARG D 1 103 ? 12.092  34.302  46.476  1.00 54.47  ? 102 ARG C CA     1 
ATOM   9230  C  C      . ARG D 1 103 ? 11.601  34.394  45.036  1.00 56.44  ? 102 ARG C C      1 
ATOM   9231  O  O      . ARG D 1 103 ? 10.504  34.906  44.784  1.00 57.93  ? 102 ARG C O      1 
ATOM   9232  C  CB     . ARG D 1 103 ? 13.521  34.858  46.604  1.00 59.34  ? 102 ARG C CB     1 
ATOM   9233  C  CG     . ARG D 1 103 ? 13.665  36.365  46.310  1.00 57.77  ? 102 ARG C CG     1 
ATOM   9234  C  CD     . ARG D 1 103 ? 14.998  36.725  45.638  1.00 53.88  ? 102 ARG C CD     1 
ATOM   9235  N  NE     . ARG D 1 103 ? 14.870  36.918  44.193  1.00 63.87  ? 102 ARG C NE     1 
ATOM   9236  C  CZ     . ARG D 1 103 ? 14.083  37.815  43.610  1.00 60.87  ? 102 ARG C CZ     1 
ATOM   9237  N  NH1    . ARG D 1 103 ? 13.323  38.635  44.319  1.00 58.79  ? 102 ARG C NH1    1 
ATOM   9238  N  NH2    . ARG D 1 103 ? 14.046  37.880  42.281  1.00 60.10  ? 102 ARG C NH2    1 
ATOM   9239  H  H      . ARG D 1 103 ? 12.804  32.637  47.251  1.00 64.65  ? 102 ARG C H      1 
ATOM   9240  H  HA     . ARG D 1 103 ? 11.503  34.851  47.017  1.00 65.40  ? 102 ARG C HA     1 
ATOM   9241  H  HB2    . ARG D 1 103 ? 13.828  34.709  47.512  1.00 71.25  ? 102 ARG C HB2    1 
ATOM   9242  H  HB3    . ARG D 1 103 ? 14.092  34.384  45.979  1.00 71.25  ? 102 ARG C HB3    1 
ATOM   9243  H  HG2    . ARG D 1 103 ? 12.949  36.640  45.717  1.00 69.36  ? 102 ARG C HG2    1 
ATOM   9244  H  HG3    . ARG D 1 103 ? 13.611  36.855  47.146  1.00 69.36  ? 102 ARG C HG3    1 
ATOM   9245  H  HD2    . ARG D 1 103 ? 15.332  37.551  46.022  1.00 64.69  ? 102 ARG C HD2    1 
ATOM   9246  H  HD3    . ARG D 1 103 ? 15.633  36.008  45.790  1.00 64.69  ? 102 ARG C HD3    1 
ATOM   9247  H  HE     . ARG D 1 103 ? 15.340  36.410  43.682  1.00 76.68  ? 102 ARG C HE     1 
ATOM   9248  H  HH11   . ARG D 1 103 ? 13.332  38.595  45.178  1.00 70.58  ? 102 ARG C HH11   1 
ATOM   9249  H  HH12   . ARG D 1 103 ? 12.821  39.209  43.921  1.00 70.58  ? 102 ARG C HH12   1 
ATOM   9250  H  HH21   . ARG D 1 103 ? 14.527  37.345  41.811  1.00 72.15  ? 102 ARG C HH21   1 
ATOM   9251  H  HH22   . ARG D 1 103 ? 13.540  38.457  41.893  1.00 72.15  ? 102 ARG C HH22   1 
ATOM   9252  N  N      . VAL D 1 104 ? 12.397  33.883  44.090  1.00 59.61  ? 103 VAL C N      1 
ATOM   9253  C  CA     . VAL D 1 104 ? 12.108  34.081  42.670  1.00 50.38  ? 103 VAL C CA     1 
ATOM   9254  C  C      . VAL D 1 104 ? 10.635  33.838  42.380  1.00 57.13  ? 103 VAL C C      1 
ATOM   9255  O  O      . VAL D 1 104 ? 9.973   34.637  41.702  1.00 56.26  ? 103 VAL C O      1 
ATOM   9256  C  CB     . VAL D 1 104 ? 13.006  33.173  41.809  1.00 56.60  ? 103 VAL C CB     1 
ATOM   9257  C  CG1    . VAL D 1 104 ? 12.561  33.206  40.334  1.00 58.38  ? 103 VAL C CG1    1 
ATOM   9258  C  CG2    . VAL D 1 104 ? 14.475  33.579  41.954  1.00 59.14  ? 103 VAL C CG2    1 
ATOM   9259  H  H      . VAL D 1 104 ? 13.106  33.422  44.244  1.00 71.57  ? 103 VAL C H      1 
ATOM   9260  H  HA     . VAL D 1 104 ? 12.304  35.004  42.446  1.00 60.49  ? 103 VAL C HA     1 
ATOM   9261  H  HB     . VAL D 1 104 ? 12.919  32.258  42.121  1.00 67.96  ? 103 VAL C HB     1 
ATOM   9262  H  HG11   . VAL D 1 104 ? 13.172  32.667  39.807  1.00 70.09  ? 103 VAL C HG11   1 
ATOM   9263  H  HG12   . VAL D 1 104 ? 11.662  32.846  40.267  1.00 70.09  ? 103 VAL C HG12   1 
ATOM   9264  H  HG13   . VAL D 1 104 ? 12.574  34.123  40.021  1.00 70.09  ? 103 VAL C HG13   1 
ATOM   9265  H  HG21   . VAL D 1 104 ? 15.019  32.995  41.402  1.00 71.00  ? 103 VAL C HG21   1 
ATOM   9266  H  HG22   . VAL D 1 104 ? 14.578  34.499  41.664  1.00 71.00  ? 103 VAL C HG22   1 
ATOM   9267  H  HG23   . VAL D 1 104 ? 14.736  33.493  42.884  1.00 71.00  ? 103 VAL C HG23   1 
ATOM   9268  N  N      . LYS D 1 105 ? 10.104  32.724  42.892  1.00 56.67  ? 104 LYS C N      1 
ATOM   9269  C  CA     . LYS D 1 105 ? 8.732   32.308  42.663  1.00 53.54  ? 104 LYS C CA     1 
ATOM   9270  C  C      . LYS D 1 105 ? 7.733   33.009  43.576  1.00 62.61  ? 104 LYS C C      1 
ATOM   9271  O  O      . LYS D 1 105 ? 6.525   32.788  43.425  1.00 62.42  ? 104 LYS C O      1 
ATOM   9272  C  CB     . LYS D 1 105 ? 8.631   30.797  42.859  1.00 57.26  ? 104 LYS C CB     1 
ATOM   9273  C  CG     . LYS D 1 105 ? 9.586   30.018  41.981  1.00 57.07  ? 104 LYS C CG     1 
ATOM   9274  C  CD     . LYS D 1 105 ? 9.126   28.587  41.741  1.00 56.21  ? 104 LYS C CD     1 
ATOM   9275  C  CE     . LYS D 1 105 ? 7.829   28.472  40.930  1.00 51.82  ? 104 LYS C CE     1 
ATOM   9276  N  NZ     . LYS D 1 105 ? 7.954   28.838  39.492  1.00 52.21  ? 104 LYS C NZ     1 
ATOM   9277  H  H      . LYS D 1 105 ? 10.539  32.177  43.393  1.00 68.04  ? 104 LYS C H      1 
ATOM   9278  H  HA     . LYS D 1 105 ? 8.485   32.521  41.749  1.00 64.29  ? 104 LYS C HA     1 
ATOM   9279  H  HB2    . LYS D 1 105 ? 8.836   30.586  43.784  1.00 68.74  ? 104 LYS C HB2    1 
ATOM   9280  H  HB3    . LYS D 1 105 ? 7.729   30.511  42.646  1.00 68.74  ? 104 LYS C HB3    1 
ATOM   9281  H  HG2    . LYS D 1 105 ? 9.656   30.460  41.120  1.00 68.52  ? 104 LYS C HG2    1 
ATOM   9282  H  HG3    . LYS D 1 105 ? 10.456  29.986  42.409  1.00 68.52  ? 104 LYS C HG3    1 
ATOM   9283  H  HD2    . LYS D 1 105 ? 9.820   28.115  41.254  1.00 67.48  ? 104 LYS C HD2    1 
ATOM   9284  H  HD3    . LYS D 1 105 ? 8.975   28.161  42.599  1.00 67.48  ? 104 LYS C HD3    1 
ATOM   9285  H  HE2    . LYS D 1 105 ? 7.521   27.553  40.970  1.00 62.21  ? 104 LYS C HE2    1 
ATOM   9286  H  HE3    . LYS D 1 105 ? 7.167   29.062  41.323  1.00 62.21  ? 104 LYS C HE3    1 
ATOM   9287  H  HZ1    . LYS D 1 105 ? 7.165   28.760  39.089  1.00 62.68  ? 104 LYS C HZ1    1 
ATOM   9288  H  HZ2    . LYS D 1 105 ? 8.236   29.678  39.415  1.00 62.68  ? 104 LYS C HZ2    1 
ATOM   9289  H  HZ3    . LYS D 1 105 ? 8.538   28.299  39.091  1.00 62.68  ? 104 LYS C HZ3    1 
ATOM   9290  N  N      . ASP D 1 106 ? 8.203   33.844  44.503  1.00 57.03  ? 105 ASP C N      1 
ATOM   9291  C  CA     . ASP D 1 106 ? 7.332   34.582  45.414  1.00 66.21  ? 105 ASP C CA     1 
ATOM   9292  C  C      . ASP D 1 106 ? 6.265   33.670  46.012  1.00 70.24  ? 105 ASP C C      1 
ATOM   9293  O  O      . ASP D 1 106 ? 5.099   33.682  45.598  1.00 73.41  ? 105 ASP C O      1 
ATOM   9294  C  CB     . ASP D 1 106 ? 6.700   35.778  44.694  1.00 64.58  ? 105 ASP C CB     1 
ATOM   9295  C  CG     . ASP D 1 106 ? 6.110   36.800  45.657  1.00 67.76  ? 105 ASP C CG     1 
ATOM   9296  O  OD1    . ASP D 1 106 ? 6.818   37.249  46.595  1.00 68.00  ? 105 ASP C OD1    1 
ATOM   9297  O  OD2    . ASP D 1 106 ? 4.926   37.159  45.470  1.00 64.69  ? 105 ASP C OD2    1 
ATOM   9298  H  H      . ASP D 1 106 ? 9.039   34.004  44.626  1.00 68.47  ? 105 ASP C H      1 
ATOM   9299  H  HA     . ASP D 1 106 ? 7.860   34.926  46.151  1.00 79.49  ? 105 ASP C HA     1 
ATOM   9300  H  HB2    . ASP D 1 106 ? 7.379   36.222  44.163  1.00 77.53  ? 105 ASP C HB2    1 
ATOM   9301  H  HB3    . ASP D 1 106 ? 5.986   35.460  44.120  1.00 77.53  ? 105 ASP C HB3    1 
ATOM   9302  N  N      . SER D 1 107 ? 6.677   32.854  46.976  1.00 70.28  ? 106 SER C N      1 
ATOM   9303  C  CA     . SER D 1 107 ? 5.777   32.045  47.785  1.00 71.70  ? 106 SER C CA     1 
ATOM   9304  C  C      . SER D 1 107 ? 6.617   31.517  48.937  1.00 72.86  ? 106 SER C C      1 
ATOM   9305  O  O      . SER D 1 107 ? 7.833   31.725  48.989  1.00 69.44  ? 106 SER C O      1 
ATOM   9306  C  CB     . SER D 1 107 ? 5.134   30.891  47.000  1.00 70.49  ? 106 SER C CB     1 
ATOM   9307  O  OG     . SER D 1 107 ? 3.872   30.519  47.558  1.00 67.67  ? 106 SER C OG     1 
ATOM   9308  H  H      . SER D 1 107 ? 7.503   32.749  47.187  1.00 84.37  ? 106 SER C H      1 
ATOM   9309  H  HA     . SER D 1 107 ? 5.049   32.592  48.118  1.00 86.08  ? 106 SER C HA     1 
ATOM   9310  H  HB2    . SER D 1 107 ? 5.000   31.174  46.082  1.00 84.62  ? 106 SER C HB2    1 
ATOM   9311  H  HB3    . SER D 1 107 ? 5.728   30.125  47.028  1.00 84.62  ? 106 SER C HB3    1 
ATOM   9312  H  HG     . SER D 1 107 ? 3.537   29.889  47.115  1.00 81.24  ? 106 SER C HG     1 
ATOM   9313  N  N      . GLU D 1 108 ? 5.947   30.855  49.870  1.00 74.37  ? 107 GLU C N      1 
ATOM   9314  C  CA     . GLU D 1 108 ? 6.610   30.039  50.874  1.00 75.51  ? 107 GLU C CA     1 
ATOM   9315  C  C      . GLU D 1 108 ? 6.389   28.554  50.608  1.00 73.09  ? 107 GLU C C      1 
ATOM   9316  O  O      . GLU D 1 108 ? 6.802   27.719  51.415  1.00 73.58  ? 107 GLU C O      1 
ATOM   9317  C  CB     . GLU D 1 108 ? 6.103   30.417  52.265  1.00 75.76  ? 107 GLU C CB     1 
ATOM   9318  C  CG     . GLU D 1 108 ? 6.775   31.644  52.874  1.00 78.40  ? 107 GLU C CG     1 
ATOM   9319  C  CD     . GLU D 1 108 ? 8.108   31.320  53.527  1.00 78.80  ? 107 GLU C CD     1 
ATOM   9320  O  OE1    . GLU D 1 108 ? 9.002   32.193  53.538  1.00 80.59  ? 107 GLU C OE1    1 
ATOM   9321  O  OE2    . GLU D 1 108 ? 8.263   30.187  54.024  1.00 80.50  ? 107 GLU C OE2    1 
ATOM   9322  H  H      . GLU D 1 108 ? 5.090   30.863  49.943  1.00 89.27  ? 107 GLU C H      1 
ATOM   9323  H  HA     . GLU D 1 108 ? 7.564   30.210  50.859  1.00 90.64  ? 107 GLU C HA     1 
ATOM   9324  H  HB2    . GLU D 1 108 ? 5.153   30.602  52.208  1.00 90.94  ? 107 GLU C HB2    1 
ATOM   9325  H  HB3    . GLU D 1 108 ? 6.260   29.670  52.864  1.00 90.94  ? 107 GLU C HB3    1 
ATOM   9326  H  HG2    . GLU D 1 108 ? 6.935   32.297  52.175  1.00 94.11  ? 107 GLU C HG2    1 
ATOM   9327  H  HG3    . GLU D 1 108 ? 6.192   32.020  53.552  1.00 94.11  ? 107 GLU C HG3    1 
ATOM   9328  N  N      . ASP D 1 109 ? 5.762   28.205  49.475  1.00 70.25  ? 108 ASP C N      1 
ATOM   9329  C  CA     . ASP D 1 109 ? 5.172   26.877  49.283  1.00 70.29  ? 108 ASP C CA     1 
ATOM   9330  C  C      . ASP D 1 109 ? 5.316   26.480  47.808  1.00 67.51  ? 108 ASP C C      1 
ATOM   9331  O  O      . ASP D 1 109 ? 4.387   26.598  47.002  1.00 71.81  ? 108 ASP C O      1 
ATOM   9332  C  CB     . ASP D 1 109 ? 3.706   26.884  49.726  1.00 77.69  ? 108 ASP C CB     1 
ATOM   9333  C  CG     . ASP D 1 109 ? 3.150   25.500  49.964  1.00 78.84  ? 108 ASP C CG     1 
ATOM   9334  O  OD1    . ASP D 1 109 ? 3.741   24.762  50.781  1.00 80.32  ? 108 ASP C OD1    1 
ATOM   9335  O  OD2    . ASP D 1 109 ? 2.111   25.159  49.354  1.00 80.81  ? 108 ASP C OD2    1 
ATOM   9336  H  H      . ASP D 1 109 ? 5.665   28.727  48.798  1.00 84.33  ? 108 ASP C H      1 
ATOM   9337  H  HA     . ASP D 1 109 ? 5.670   26.221  49.796  1.00 84.38  ? 108 ASP C HA     1 
ATOM   9338  H  HB2    . ASP D 1 109 ? 3.630   27.383  50.554  1.00 93.26  ? 108 ASP C HB2    1 
ATOM   9339  H  HB3    . ASP D 1 109 ? 3.171   27.305  49.035  1.00 93.26  ? 108 ASP C HB3    1 
ATOM   9340  N  N      . VAL D 1 110 ? 6.485   25.989  47.456  1.00 62.15  ? 109 VAL C N      1 
ATOM   9341  C  CA     . VAL D 1 110 ? 6.809   25.597  46.075  1.00 58.33  ? 109 VAL C CA     1 
ATOM   9342  C  C      . VAL D 1 110 ? 7.017   24.093  46.047  1.00 52.52  ? 109 VAL C C      1 
ATOM   9343  O  O      . VAL D 1 110 ? 7.789   23.577  46.868  1.00 52.35  ? 109 VAL C O      1 
ATOM   9344  C  CB     . VAL D 1 110 ? 8.072   26.323  45.555  1.00 55.69  ? 109 VAL C CB     1 
ATOM   9345  C  CG1    . VAL D 1 110 ? 9.289   26.058  46.438  1.00 51.29  ? 109 VAL C CG1    1 
ATOM   9346  C  CG2    . VAL D 1 110 ? 8.364   25.863  44.143  1.00 51.90  ? 109 VAL C CG2    1 
ATOM   9347  H  H      . VAL D 1 110 ? 7.135   25.866  48.006  1.00 74.61  ? 109 VAL C H      1 
ATOM   9348  H  HA     . VAL D 1 110 ? 6.063   25.817  45.495  1.00 70.03  ? 109 VAL C HA     1 
ATOM   9349  H  HB     . VAL D 1 110 ? 7.903   27.278  45.572  1.00 66.86  ? 109 VAL C HB     1 
ATOM   9350  H  HG11   . VAL D 1 110 ? 10.015  26.636  46.157  1.00 61.59  ? 109 VAL C HG11   1 
ATOM   9351  H  HG12   . VAL D 1 110 ? 9.056   26.244  47.361  1.00 61.59  ? 109 VAL C HG12   1 
ATOM   9352  H  HG13   . VAL D 1 110 ? 9.551   25.129  46.344  1.00 61.59  ? 109 VAL C HG13   1 
ATOM   9353  H  HG21   . VAL D 1 110 ? 9.120   26.363  43.798  1.00 62.32  ? 109 VAL C HG21   1 
ATOM   9354  H  HG22   . VAL D 1 110 ? 8.573   24.916  44.156  1.00 62.32  ? 109 VAL C HG22   1 
ATOM   9355  H  HG23   . VAL D 1 110 ? 7.583   26.021  43.591  1.00 62.32  ? 109 VAL C HG23   1 
ATOM   9356  N  N      . PRO D 1 111 ? 6.377   23.356  45.124  1.00 50.57  ? 110 PRO C N      1 
ATOM   9357  C  CA     . PRO D 1 111 ? 6.618   21.908  45.060  1.00 49.06  ? 110 PRO C CA     1 
ATOM   9358  C  C      . PRO D 1 111 ? 8.106   21.581  45.066  1.00 47.42  ? 110 PRO C C      1 
ATOM   9359  O  O      . PRO D 1 111 ? 8.838   21.992  44.158  1.00 49.77  ? 110 PRO C O      1 
ATOM   9360  C  CB     . PRO D 1 111 ? 5.947   21.494  43.744  1.00 49.62  ? 110 PRO C CB     1 
ATOM   9361  C  CG     . PRO D 1 111 ? 4.948   22.574  43.456  1.00 50.96  ? 110 PRO C CG     1 
ATOM   9362  C  CD     . PRO D 1 111 ? 5.501   23.827  44.027  1.00 52.97  ? 110 PRO C CD     1 
ATOM   9363  H  HA     . PRO D 1 111 ? 6.178   21.451  45.794  1.00 58.91  ? 110 PRO C HA     1 
ATOM   9364  H  HB2    . PRO D 1 111 ? 6.611   21.438  43.039  1.00 59.58  ? 110 PRO C HB2    1 
ATOM   9365  H  HB3    . PRO D 1 111 ? 5.507   20.636  43.854  1.00 59.58  ? 110 PRO C HB3    1 
ATOM   9366  H  HG2    . PRO D 1 111 ? 4.831   22.660  42.497  1.00 61.19  ? 110 PRO C HG2    1 
ATOM   9367  H  HG3    . PRO D 1 111 ? 4.102   22.353  43.876  1.00 61.19  ? 110 PRO C HG3    1 
ATOM   9368  H  HD2    . PRO D 1 111 ? 6.014   24.311  43.362  1.00 63.60  ? 110 PRO C HD2    1 
ATOM   9369  H  HD3    . PRO D 1 111 ? 4.791   24.390  44.373  1.00 63.60  ? 110 PRO C HD3    1 
ATOM   9370  N  N      . MET D 1 112 ? 8.558   20.806  46.052  1.00 42.85  ? 111 MET C N      1 
ATOM   9371  C  CA     . MET D 1 112 ? 9.973   20.704  46.358  1.00 48.10  ? 111 MET C CA     1 
ATOM   9372  C  C      . MET D 1 112 ? 10.271  19.370  47.014  1.00 49.06  ? 111 MET C C      1 
ATOM   9373  O  O      . MET D 1 112 ? 9.422   18.813  47.712  1.00 52.22  ? 111 MET C O      1 
ATOM   9374  C  CB     . MET D 1 112 ? 10.350  21.866  47.292  1.00 52.20  ? 111 MET C CB     1 
ATOM   9375  C  CG     . MET D 1 112 ? 11.799  22.038  47.629  1.00 54.18  ? 111 MET C CG     1 
ATOM   9376  S  SD     . MET D 1 112 ? 12.220  23.807  47.625  1.00 53.92  ? 111 MET C SD     1 
ATOM   9377  C  CE     . MET D 1 112 ? 13.069  23.946  45.993  1.00 40.98  ? 111 MET C CE     1 
ATOM   9378  H  H      . MET D 1 112 ? 8.055   20.328  46.559  1.00 51.45  ? 111 MET C H      1 
ATOM   9379  H  HA     . MET D 1 112 ? 10.503  20.740  45.547  1.00 57.76  ? 111 MET C HA     1 
ATOM   9380  H  HB2    . MET D 1 112 ? 10.060  22.691  46.873  1.00 62.68  ? 111 MET C HB2    1 
ATOM   9381  H  HB3    . MET D 1 112 ? 9.881   21.738  48.131  1.00 62.68  ? 111 MET C HB3    1 
ATOM   9382  H  HG2    . MET D 1 112 ? 11.977  21.676  48.512  1.00 65.05  ? 111 MET C HG2    1 
ATOM   9383  H  HG3    . MET D 1 112 ? 12.346  21.585  46.969  1.00 65.05  ? 111 MET C HG3    1 
ATOM   9384  H  HE1    . MET D 1 112 ? 13.314  24.872  45.842  1.00 49.22  ? 111 MET C HE1    1 
ATOM   9385  H  HE2    . MET D 1 112 ? 13.864  23.391  46.002  1.00 49.22  ? 111 MET C HE2    1 
ATOM   9386  H  HE3    . MET D 1 112 ? 12.465  23.646  45.296  1.00 49.22  ? 111 MET C HE3    1 
ATOM   9387  N  N      . VAL D 1 113 ? 11.498  18.869  46.814  1.00 53.68  ? 112 VAL C N      1 
ATOM   9388  C  CA     . VAL D 1 113 ? 11.895  17.576  47.382  1.00 55.86  ? 112 VAL C CA     1 
ATOM   9389  C  C      . VAL D 1 113 ? 13.390  17.502  47.706  1.00 52.74  ? 112 VAL C C      1 
ATOM   9390  O  O      . VAL D 1 113 ? 14.236  17.639  46.813  1.00 53.40  ? 112 VAL C O      1 
ATOM   9391  C  CB     . VAL D 1 113 ? 11.493  16.441  46.412  1.00 54.65  ? 112 VAL C CB     1 
ATOM   9392  C  CG1    . VAL D 1 113 ? 12.188  15.130  46.780  1.00 51.77  ? 112 VAL C CG1    1 
ATOM   9393  C  CG2    . VAL D 1 113 ? 9.970   16.277  46.361  1.00 47.60  ? 112 VAL C CG2    1 
ATOM   9394  H  H      . VAL D 1 113 ? 12.113  19.258  46.355  1.00 64.45  ? 112 VAL C H      1 
ATOM   9395  H  HA     . VAL D 1 113 ? 11.441  17.481  48.234  1.00 67.07  ? 112 VAL C HA     1 
ATOM   9396  H  HB     . VAL D 1 113 ? 11.789  16.681  45.520  1.00 65.62  ? 112 VAL C HB     1 
ATOM   9397  H  HG11   . VAL D 1 113 ? 11.721  14.395  46.353  1.00 62.16  ? 112 VAL C HG11   1 
ATOM   9398  H  HG12   . VAL D 1 113 ? 13.107  15.163  46.471  1.00 62.16  ? 112 VAL C HG12   1 
ATOM   9399  H  HG13   . VAL D 1 113 ? 12.167  15.021  47.743  1.00 62.16  ? 112 VAL C HG13   1 
ATOM   9400  H  HG21   . VAL D 1 113 ? 9.753   15.526  45.786  1.00 57.16  ? 112 VAL C HG21   1 
ATOM   9401  H  HG22   . VAL D 1 113 ? 9.639   16.113  47.258  1.00 57.16  ? 112 VAL C HG22   1 
ATOM   9402  H  HG23   . VAL D 1 113 ? 9.576   17.090  46.006  1.00 57.16  ? 112 VAL C HG23   1 
ATOM   9403  N  N      . LEU D 1 114 ? 13.727  17.246  48.972  1.00 45.15  ? 113 LEU C N      1 
ATOM   9404  C  CA     . LEU D 1 114 ? 15.129  17.114  49.373  1.00 48.64  ? 113 LEU C CA     1 
ATOM   9405  C  C      . LEU D 1 114 ? 15.645  15.695  49.126  1.00 48.16  ? 113 LEU C C      1 
ATOM   9406  O  O      . LEU D 1 114 ? 14.994  14.704  49.505  1.00 47.88  ? 113 LEU C O      1 
ATOM   9407  C  CB     . LEU D 1 114 ? 15.301  17.469  50.855  1.00 49.69  ? 113 LEU C CB     1 
ATOM   9408  C  CG     . LEU D 1 114 ? 16.706  17.512  51.481  1.00 47.59  ? 113 LEU C CG     1 
ATOM   9409  C  CD1    . LEU D 1 114 ? 17.525  18.673  51.018  1.00 48.84  ? 113 LEU C CD1    1 
ATOM   9410  C  CD2    . LEU D 1 114 ? 16.644  17.522  53.045  1.00 48.57  ? 113 LEU C CD2    1 
ATOM   9411  H  H      . LEU D 1 114 ? 13.165  17.144  49.615  1.00 54.21  ? 113 LEU C H      1 
ATOM   9412  H  HA     . LEU D 1 114 ? 15.656  17.726  48.836  1.00 58.40  ? 113 LEU C HA     1 
ATOM   9413  H  HB2    . LEU D 1 114 ? 14.922  18.353  50.983  1.00 59.66  ? 113 LEU C HB2    1 
ATOM   9414  H  HB3    . LEU D 1 114 ? 14.798  16.816  51.365  1.00 59.66  ? 113 LEU C HB3    1 
ATOM   9415  H  HG     . LEU D 1 114 ? 17.148  16.702  51.183  1.00 57.14  ? 113 LEU C HG     1 
ATOM   9416  H  HD11   . LEU D 1 114 ? 18.277  18.789  51.620  1.00 58.64  ? 113 LEU C HD11   1 
ATOM   9417  H  HD12   . LEU D 1 114 ? 17.845  18.495  50.120  1.00 58.64  ? 113 LEU C HD12   1 
ATOM   9418  H  HD13   . LEU D 1 114 ? 16.973  19.470  51.021  1.00 58.64  ? 113 LEU C HD13   1 
ATOM   9419  H  HD21   . LEU D 1 114 ? 17.548  17.516  53.397  1.00 58.32  ? 113 LEU C HD21   1 
ATOM   9420  H  HD22   . LEU D 1 114 ? 16.181  18.322  53.338  1.00 58.32  ? 113 LEU C HD22   1 
ATOM   9421  H  HD23   . LEU D 1 114 ? 16.167  16.734  53.348  1.00 58.32  ? 113 LEU C HD23   1 
ATOM   9422  N  N      . VAL D 1 115 ? 16.843  15.601  48.551  1.00 44.81  ? 114 VAL C N      1 
ATOM   9423  C  CA     . VAL D 1 115 ? 17.449  14.335  48.139  1.00 41.35  ? 114 VAL C CA     1 
ATOM   9424  C  C      . VAL D 1 115 ? 18.845  14.211  48.737  1.00 44.13  ? 114 VAL C C      1 
ATOM   9425  O  O      . VAL D 1 115 ? 19.753  14.964  48.360  1.00 40.29  ? 114 VAL C O      1 
ATOM   9426  C  CB     . VAL D 1 115 ? 17.515  14.208  46.607  1.00 41.89  ? 114 VAL C CB     1 
ATOM   9427  C  CG1    . VAL D 1 115 ? 17.940  12.770  46.217  1.00 37.89  ? 114 VAL C CG1    1 
ATOM   9428  C  CG2    . VAL D 1 115 ? 16.179  14.624  46.005  1.00 39.85  ? 114 VAL C CG2    1 
ATOM   9429  H  H      . VAL D 1 115 ? 17.342  16.281  48.384  1.00 53.81  ? 114 VAL C H      1 
ATOM   9430  H  HA     . VAL D 1 115 ? 16.915  13.615  48.510  1.00 49.66  ? 114 VAL C HA     1 
ATOM   9431  H  HB     . VAL D 1 115 ? 18.187  14.802  46.237  1.00 50.31  ? 114 VAL C HB     1 
ATOM   9432  H  HG11   . VAL D 1 115 ? 17.890  12.676  45.253  1.00 45.51  ? 114 VAL C HG11   1 
ATOM   9433  H  HG12   . VAL D 1 115 ? 18.849  12.616  46.517  1.00 45.51  ? 114 VAL C HG12   1 
ATOM   9434  H  HG13   . VAL D 1 115 ? 17.340  12.137  46.642  1.00 45.51  ? 114 VAL C HG13   1 
ATOM   9435  H  HG21   . VAL D 1 115 ? 16.144  14.331  45.081  1.00 47.85  ? 114 VAL C HG21   1 
ATOM   9436  H  HG22   . VAL D 1 115 ? 15.463  14.210  46.511  1.00 47.85  ? 114 VAL C HG22   1 
ATOM   9437  H  HG23   . VAL D 1 115 ? 16.100  15.590  46.049  1.00 47.85  ? 114 VAL C HG23   1 
ATOM   9438  N  N      . GLY D 1 116 ? 19.024  13.251  49.638  1.00 38.54  ? 115 GLY C N      1 
ATOM   9439  C  CA     . GLY D 1 116 ? 20.357  12.866  50.064  1.00 45.55  ? 115 GLY C CA     1 
ATOM   9440  C  C      . GLY D 1 116 ? 21.000  11.823  49.160  1.00 46.40  ? 115 GLY C C      1 
ATOM   9441  O  O      . GLY D 1 116 ? 20.705  10.621  49.278  1.00 46.59  ? 115 GLY C O      1 
ATOM   9442  H  H      . GLY D 1 116 ? 18.389  12.811  50.015  1.00 46.28  ? 115 GLY C H      1 
ATOM   9443  H  HA2    . GLY D 1 116 ? 20.927  13.651  50.072  1.00 54.70  ? 115 GLY C HA2    1 
ATOM   9444  H  HA3    . GLY D 1 116 ? 20.311  12.501  50.961  1.00 54.70  ? 115 GLY C HA3    1 
ATOM   9445  N  N      . ASN D 1 117 ? 21.922  12.264  48.302  1.00 36.56  ? 116 ASN C N      1 
ATOM   9446  C  CA     . ASN D 1 117 ? 22.495  11.444  47.246  1.00 44.81  ? 116 ASN C CA     1 
ATOM   9447  C  C      . ASN D 1 117 ? 23.761  10.702  47.669  1.00 42.37  ? 116 ASN C C      1 
ATOM   9448  O  O      . ASN D 1 117 ? 24.524  11.169  48.498  1.00 41.60  ? 116 ASN C O      1 
ATOM   9449  C  CB     . ASN D 1 117 ? 22.877  12.311  46.031  1.00 48.14  ? 116 ASN C CB     1 
ATOM   9450  C  CG     . ASN D 1 117 ? 23.325  11.485  44.857  1.00 49.19  ? 116 ASN C CG     1 
ATOM   9451  O  OD1    . ASN D 1 117 ? 23.549  10.291  44.999  1.00 52.67  ? 116 ASN C OD1    1 
ATOM   9452  N  ND2    . ASN D 1 117 ? 23.527  12.113  43.718  1.00 49.85  ? 116 ASN C ND2    1 
ATOM   9453  H  H      . ASN D 1 117 ? 22.241  13.063  48.316  1.00 43.91  ? 116 ASN C H      1 
ATOM   9454  H  HA     . ASN D 1 117 ? 21.816  10.790  47.016  1.00 53.81  ? 116 ASN C HA     1 
ATOM   9455  H  HB2    . ASN D 1 117 ? 22.106  12.832  45.757  1.00 57.81  ? 116 ASN C HB2    1 
ATOM   9456  H  HB3    . ASN D 1 117 ? 23.605  12.902  46.280  1.00 57.81  ? 116 ASN C HB3    1 
ATOM   9457  H  HD21   . ASN D 1 117 ? 23.784  11.674  43.024  1.00 59.86  ? 116 ASN C HD21   1 
ATOM   9458  H  HD22   . ASN D 1 117 ? 23.403  12.963  43.667  1.00 59.86  ? 116 ASN C HD22   1 
ATOM   9459  N  N      . LYS D 1 118 ? 24.041  9.612   46.934  1.00 47.98  ? 117 LYS C N      1 
ATOM   9460  C  CA     . LYS D 1 118 ? 25.237  8.781   47.077  1.00 45.52  ? 117 LYS C CA     1 
ATOM   9461  C  C      . LYS D 1 118 ? 25.191  7.941   48.343  1.00 42.67  ? 117 LYS C C      1 
ATOM   9462  O  O      . LYS D 1 118 ? 26.225  7.644   48.954  1.00 46.62  ? 117 LYS C O      1 
ATOM   9463  C  CB     . LYS D 1 118 ? 26.531  9.600   47.052  1.00 44.45  ? 117 LYS C CB     1 
ATOM   9464  C  CG     . LYS D 1 118 ? 26.573  10.655  45.965  1.00 42.88  ? 117 LYS C CG     1 
ATOM   9465  C  CD     . LYS D 1 118 ? 28.008  11.058  45.731  1.00 44.98  ? 117 LYS C CD     1 
ATOM   9466  C  CE     . LYS D 1 118 ? 28.121  12.318  44.876  1.00 45.53  ? 117 LYS C CE     1 
ATOM   9467  N  NZ     . LYS D 1 118 ? 29.572  12.680  44.709  1.00 47.36  ? 117 LYS C NZ     1 
ATOM   9468  H  H      . LYS D 1 118 ? 23.521  9.322   46.312  1.00 57.61  ? 117 LYS C H      1 
ATOM   9469  H  HA     . LYS D 1 118 ? 25.260  8.183   46.314  1.00 54.65  ? 117 LYS C HA     1 
ATOM   9470  H  HB2    . LYS D 1 118 ? 26.629  10.052  47.905  1.00 53.37  ? 117 LYS C HB2    1 
ATOM   9471  H  HB3    . LYS D 1 118 ? 27.277  8.998   46.907  1.00 53.37  ? 117 LYS C HB3    1 
ATOM   9472  H  HG2    . LYS D 1 118 ? 26.207  10.296  45.141  1.00 51.49  ? 117 LYS C HG2    1 
ATOM   9473  H  HG3    . LYS D 1 118 ? 26.066  11.435  46.240  1.00 51.49  ? 117 LYS C HG3    1 
ATOM   9474  H  HD2    . LYS D 1 118 ? 28.433  11.234  46.585  1.00 54.01  ? 117 LYS C HD2    1 
ATOM   9475  H  HD3    . LYS D 1 118 ? 28.471  10.340  45.272  1.00 54.01  ? 117 LYS C HD3    1 
ATOM   9476  H  HE2    . LYS D 1 118 ? 27.734  12.158  44.001  1.00 54.67  ? 117 LYS C HE2    1 
ATOM   9477  H  HE3    . LYS D 1 118 ? 27.662  13.054  45.312  1.00 54.67  ? 117 LYS C HE3    1 
ATOM   9478  H  HZ1    . LYS D 1 118 ? 29.646  13.433  44.240  1.00 56.87  ? 117 LYS C HZ1    1 
ATOM   9479  H  HZ2    . LYS D 1 118 ? 29.950  12.798  45.506  1.00 56.87  ? 117 LYS C HZ2    1 
ATOM   9480  H  HZ3    . LYS D 1 118 ? 30.000  12.029  44.279  1.00 56.87  ? 117 LYS C HZ3    1 
ATOM   9481  N  N      . CYS D 1 119 ? 24.003  7.563   48.761  1.00 43.59  ? 118 CYS C N      1 
ATOM   9482  C  CA     . CYS D 1 119 ? 23.906  6.835   50.027  1.00 44.53  ? 118 CYS C CA     1 
ATOM   9483  C  C      . CYS D 1 119 ? 24.596  5.474   49.962  1.00 50.60  ? 118 CYS C C      1 
ATOM   9484  O  O      . CYS D 1 119 ? 24.587  4.735   50.959  1.00 50.77  ? 118 CYS C O      1 
ATOM   9485  C  CB     . CYS D 1 119 ? 22.430  6.711   50.389  1.00 49.90  ? 118 CYS C CB     1 
ATOM   9486  S  SG     . CYS D 1 119 ? 21.493  5.627   49.252  1.00 60.90  ? 118 CYS C SG     1 
ATOM   9487  H  H      . CYS D 1 119 ? 23.259  7.705   48.352  1.00 52.34  ? 118 CYS C H      1 
ATOM   9488  H  HA     . CYS D 1 119 ? 24.341  7.321   50.744  1.00 53.47  ? 118 CYS C HA     1 
ATOM   9489  H  HB2    . CYS D 1 119 ? 22.357  6.340   51.282  1.00 59.91  ? 118 CYS C HB2    1 
ATOM   9490  H  HB3    . CYS D 1 119 ? 22.026  7.592   50.361  1.00 59.91  ? 118 CYS C HB3    1 
ATOM   9491  H  HG     . CYS D 1 119 ? 20.324  5.707   49.511  1.00 73.11  ? 118 CYS C HG     1 
ATOM   9492  N  N      . ASP D 1 120 ? 25.238  5.141   48.833  1.00 49.56  ? 119 ASP C N      1 
ATOM   9493  C  CA     . ASP D 1 120 ? 26.026  3.919   48.752  1.00 51.55  ? 119 ASP C CA     1 
ATOM   9494  C  C      . ASP D 1 120 ? 27.395  4.038   49.419  1.00 55.33  ? 119 ASP C C      1 
ATOM   9495  O  O      . ASP D 1 120 ? 28.024  3.007   49.696  1.00 52.70  ? 119 ASP C O      1 
ATOM   9496  C  CB     . ASP D 1 120 ? 26.267  3.488   47.295  1.00 52.03  ? 119 ASP C CB     1 
ATOM   9497  C  CG     . ASP D 1 120 ? 26.979  4.560   46.475  1.00 51.17  ? 119 ASP C CG     1 
ATOM   9498  O  OD1    . ASP D 1 120 ? 26.323  5.535   46.058  1.00 48.59  ? 119 ASP C OD1    1 
ATOM   9499  O  OD2    . ASP D 1 120 ? 28.218  4.467   46.320  1.00 51.24  ? 119 ASP C OD2    1 
ATOM   9500  H  H      . ASP D 1 120 ? 25.228  5.607   48.110  1.00 59.51  ? 119 ASP C H      1 
ATOM   9501  H  HA     . ASP D 1 120 ? 25.505  3.232   49.196  1.00 61.90  ? 119 ASP C HA     1 
ATOM   9502  H  HB2    . ASP D 1 120 ? 26.818  2.689   47.288  1.00 62.47  ? 119 ASP C HB2    1 
ATOM   9503  H  HB3    . ASP D 1 120 ? 25.412  3.305   46.874  1.00 62.47  ? 119 ASP C HB3    1 
ATOM   9504  N  N      . LEU D 1 121 ? 27.874  5.253   49.668  1.00 53.35  ? 120 LEU C N      1 
ATOM   9505  C  CA     . LEU D 1 121 ? 29.240  5.430   50.128  1.00 57.63  ? 120 LEU C CA     1 
ATOM   9506  C  C      . LEU D 1 121 ? 29.365  5.017   51.593  1.00 63.98  ? 120 LEU C C      1 
ATOM   9507  O  O      . LEU D 1 121 ? 28.467  5.293   52.395  1.00 64.28  ? 120 LEU C O      1 
ATOM   9508  C  CB     . LEU D 1 121 ? 29.666  6.887   49.948  1.00 59.56  ? 120 LEU C CB     1 
ATOM   9509  C  CG     . LEU D 1 121 ? 29.791  7.337   48.495  1.00 56.36  ? 120 LEU C CG     1 
ATOM   9510  C  CD1    . LEU D 1 121 ? 30.147  8.820   48.401  1.00 53.79  ? 120 LEU C CD1    1 
ATOM   9511  C  CD2    . LEU D 1 121 ? 30.824  6.491   47.755  1.00 56.10  ? 120 LEU C CD2    1 
ATOM   9512  H  H      . LEU D 1 121 ? 27.430  5.984   49.579  1.00 64.05  ? 120 LEU C H      1 
ATOM   9513  H  HA     . LEU D 1 121 ? 29.838  4.868   49.609  1.00 69.19  ? 120 LEU C HA     1 
ATOM   9514  H  HB2    . LEU D 1 121 ? 29.006  7.456   50.375  1.00 71.51  ? 120 LEU C HB2    1 
ATOM   9515  H  HB3    . LEU D 1 121 ? 30.532  7.009   50.368  1.00 71.51  ? 120 LEU C HB3    1 
ATOM   9516  H  HG     . LEU D 1 121 ? 28.932  7.214   48.064  1.00 67.66  ? 120 LEU C HG     1 
ATOM   9517  H  HD11   . LEU D 1 121 ? 30.196  9.074   47.466  1.00 64.58  ? 120 LEU C HD11   1 
ATOM   9518  H  HD12   . LEU D 1 121 ? 29.460  9.338   48.849  1.00 64.58  ? 120 LEU C HD12   1 
ATOM   9519  H  HD13   . LEU D 1 121 ? 31.004  8.967   48.830  1.00 64.58  ? 120 LEU C HD13   1 
ATOM   9520  H  HD21   . LEU D 1 121 ? 31.055  6.932   46.922  1.00 67.35  ? 120 LEU C HD21   1 
ATOM   9521  H  HD22   . LEU D 1 121 ? 31.613  6.398   48.310  1.00 67.35  ? 120 LEU C HD22   1 
ATOM   9522  H  HD23   . LEU D 1 121 ? 30.443  5.617   47.571  1.00 67.35  ? 120 LEU C HD23   1 
ATOM   9523  N  N      . PRO D 1 122 ? 30.459  4.341   51.968  1.00 69.35  ? 121 PRO C N      1 
ATOM   9524  C  CA     . PRO D 1 122 ? 30.644  4.007   53.395  1.00 72.04  ? 121 PRO C CA     1 
ATOM   9525  C  C      . PRO D 1 122 ? 30.946  5.229   54.231  1.00 72.85  ? 121 PRO C C      1 
ATOM   9526  O  O      . PRO D 1 122 ? 30.530  5.313   55.393  1.00 77.03  ? 121 PRO C O      1 
ATOM   9527  C  CB     . PRO D 1 122 ? 31.823  3.022   53.387  1.00 74.46  ? 121 PRO C CB     1 
ATOM   9528  C  CG     . PRO D 1 122 ? 32.585  3.349   52.113  1.00 71.79  ? 121 PRO C CG     1 
ATOM   9529  C  CD     . PRO D 1 122 ? 31.572  3.860   51.122  1.00 67.60  ? 121 PRO C CD     1 
ATOM   9530  H  HA     . PRO D 1 122 ? 29.857  3.553   53.736  1.00 86.48  ? 121 PRO C HA     1 
ATOM   9531  H  HB2    . PRO D 1 122 ? 32.377  3.162   54.171  1.00 89.39  ? 121 PRO C HB2    1 
ATOM   9532  H  HB3    . PRO D 1 122 ? 31.493  2.110   53.372  1.00 89.39  ? 121 PRO C HB3    1 
ATOM   9533  H  HG2    . PRO D 1 122 ? 33.251  4.029   52.299  1.00 86.19  ? 121 PRO C HG2    1 
ATOM   9534  H  HG3    . PRO D 1 122 ? 33.014  2.547   51.777  1.00 86.19  ? 121 PRO C HG3    1 
ATOM   9535  H  HD2    . PRO D 1 122 ? 31.942  4.586   50.596  1.00 81.15  ? 121 PRO C HD2    1 
ATOM   9536  H  HD3    . PRO D 1 122 ? 31.274  3.146   50.537  1.00 81.15  ? 121 PRO C HD3    1 
ATOM   9537  N  N      . SER D 1 123 ? 31.702  6.170   53.685  1.00 73.36  ? 122 SER C N      1 
ATOM   9538  C  CA     . SER D 1 123 ? 31.820  7.459   54.338  1.00 75.16  ? 122 SER C CA     1 
ATOM   9539  C  C      . SER D 1 123 ? 30.442  8.102   54.379  1.00 75.19  ? 122 SER C C      1 
ATOM   9540  O  O      . SER D 1 123 ? 29.601  7.887   53.499  1.00 73.79  ? 122 SER C O      1 
ATOM   9541  C  CB     . SER D 1 123 ? 32.815  8.354   53.602  1.00 76.23  ? 122 SER C CB     1 
ATOM   9542  O  OG     . SER D 1 123 ? 32.342  8.707   52.316  1.00 81.35  ? 122 SER C OG     1 
ATOM   9543  H  H      . SER D 1 123 ? 32.147  6.088   52.953  1.00 88.06  ? 122 SER C H      1 
ATOM   9544  H  HA     . SER D 1 123 ? 32.157  7.357   55.242  1.00 90.23  ? 122 SER C HA     1 
ATOM   9545  H  HB2    . SER D 1 123 ? 32.949  9.163   54.119  1.00 91.51  ? 122 SER C HB2    1 
ATOM   9546  H  HB3    . SER D 1 123 ? 33.654  7.877   53.508  1.00 91.51  ? 122 SER C HB3    1 
ATOM   9547  H  HG     . SER D 1 123 ? 32.903  9.198   51.928  1.00 97.65  ? 122 SER C HG     1 
ATOM   9548  N  N      . ARG D 1 124 ? 30.191  8.857   55.434  1.00 68.55  ? 123 ARG C N      1 
ATOM   9549  C  CA     . ARG D 1 124 ? 29.000  9.685   55.492  1.00 61.79  ? 123 ARG C CA     1 
ATOM   9550  C  C      . ARG D 1 124 ? 29.327  10.828  56.433  1.00 58.39  ? 123 ARG C C      1 
ATOM   9551  O  O      . ARG D 1 124 ? 30.028  10.628  57.432  1.00 53.05  ? 123 ARG C O      1 
ATOM   9552  C  CB     . ARG D 1 124 ? 27.785  8.890   55.958  1.00 60.07  ? 123 ARG C CB     1 
ATOM   9553  C  CG     . ARG D 1 124 ? 26.541  9.729   56.165  1.00 60.21  ? 123 ARG C CG     1 
ATOM   9554  C  CD     . ARG D 1 124 ? 25.421  8.900   56.791  1.00 55.30  ? 123 ARG C CD     1 
ATOM   9555  N  NE     . ARG D 1 124 ? 24.645  8.095   55.859  1.00 56.40  ? 123 ARG C NE     1 
ATOM   9556  C  CZ     . ARG D 1 124 ? 23.531  8.494   55.251  1.00 55.50  ? 123 ARG C CZ     1 
ATOM   9557  N  NH1    . ARG D 1 124 ? 23.106  9.748   55.329  1.00 52.67  ? 123 ARG C NH1    1 
ATOM   9558  N  NH2    . ARG D 1 124 ? 22.808  7.606   54.586  1.00 51.05  ? 123 ARG C NH2    1 
ATOM   9559  H  H      . ARG D 1 124 ? 30.695  8.908   56.128  1.00 82.29  ? 123 ARG C H      1 
ATOM   9560  H  HA     . ARG D 1 124 ? 28.766  10.046  54.622  1.00 74.18  ? 123 ARG C HA     1 
ATOM   9561  H  HB2    . ARG D 1 124 ? 27.579  8.217   55.291  1.00 72.11  ? 123 ARG C HB2    1 
ATOM   9562  H  HB3    . ARG D 1 124 ? 27.997  8.465   56.804  1.00 72.11  ? 123 ARG C HB3    1 
ATOM   9563  H  HG2    . ARG D 1 124 ? 26.745  10.469  56.758  1.00 72.29  ? 123 ARG C HG2    1 
ATOM   9564  H  HG3    . ARG D 1 124 ? 26.232  10.066  55.309  1.00 72.29  ? 123 ARG C HG3    1 
ATOM   9565  H  HD2    . ARG D 1 124 ? 25.813  8.294   57.439  1.00 66.40  ? 123 ARG C HD2    1 
ATOM   9566  H  HD3    . ARG D 1 124 ? 24.803  9.504   57.233  1.00 66.40  ? 123 ARG C HD3    1 
ATOM   9567  H  HE     . ARG D 1 124 ? 24.929  7.301   55.687  1.00 67.72  ? 123 ARG C HE     1 
ATOM   9568  H  HH11   . ARG D 1 124 ? 23.555  10.326  55.781  1.00 63.24  ? 123 ARG C HH11   1 
ATOM   9569  H  HH12   . ARG D 1 124 ? 22.383  9.982   54.928  1.00 63.24  ? 123 ARG C HH12   1 
ATOM   9570  H  HH21   . ARG D 1 124 ? 23.061  6.785   54.551  1.00 61.30  ? 123 ARG C HH21   1 
ATOM   9571  H  HH22   . ARG D 1 124 ? 22.085  7.850   54.188  1.00 61.30  ? 123 ARG C HH22   1 
ATOM   9572  N  N      . THR D 1 125 ? 28.876  12.029  56.086  1.00 51.61  ? 124 THR C N      1 
ATOM   9573  C  CA     . THR D 1 125 ? 29.077  13.190  56.943  1.00 55.20  ? 124 THR C CA     1 
ATOM   9574  C  C      . THR D 1 125 ? 27.770  13.856  57.357  1.00 56.06  ? 124 THR C C      1 
ATOM   9575  O  O      . THR D 1 125 ? 27.727  14.498  58.410  1.00 54.90  ? 124 THR C O      1 
ATOM   9576  C  CB     . THR D 1 125 ? 29.989  14.221  56.255  1.00 56.56  ? 124 THR C CB     1 
ATOM   9577  O  OG1    . THR D 1 125 ? 29.387  14.720  55.051  1.00 51.79  ? 124 THR C OG1    1 
ATOM   9578  C  CG2    . THR D 1 125 ? 31.341  13.592  55.898  1.00 55.71  ? 124 THR C CG2    1 
ATOM   9579  H  H      . THR D 1 125 ? 28.449  12.196  55.358  1.00 61.96  ? 124 THR C H      1 
ATOM   9580  H  HA     . THR D 1 125 ? 29.537  12.916  57.752  1.00 66.27  ? 124 THR C HA     1 
ATOM   9581  H  HB     . THR D 1 125 ? 30.127  14.960  56.869  1.00 67.91  ? 124 THR C HB     1 
ATOM   9582  H  HG1    . THR D 1 125 ? 28.687  15.147  55.235  1.00 62.18  ? 124 THR C HG1    1 
ATOM   9583  H  HG21   . THR D 1 125 ? 31.925  14.259  55.507  1.00 66.89  ? 124 THR C HG21   1 
ATOM   9584  H  HG22   . THR D 1 125 ? 31.761  13.235  56.696  1.00 66.89  ? 124 THR C HG22   1 
ATOM   9585  H  HG23   . THR D 1 125 ? 31.214  12.871  55.261  1.00 66.89  ? 124 THR C HG23   1 
ATOM   9586  N  N      . VAL D 1 126 ? 26.706  13.679  56.588  1.00 53.23  ? 125 VAL C N      1 
ATOM   9587  C  CA     . VAL D 1 126 ? 25.395  14.254  56.844  1.00 53.90  ? 125 VAL C CA     1 
ATOM   9588  C  C      . VAL D 1 126 ? 24.527  13.092  57.307  1.00 50.87  ? 125 VAL C C      1 
ATOM   9589  O  O      . VAL D 1 126 ? 24.121  12.264  56.485  1.00 52.44  ? 125 VAL C O      1 
ATOM   9590  C  CB     . VAL D 1 126 ? 24.816  14.913  55.579  1.00 51.15  ? 125 VAL C CB     1 
ATOM   9591  C  CG1    . VAL D 1 126 ? 23.487  15.599  55.873  1.00 53.73  ? 125 VAL C CG1    1 
ATOM   9592  C  CG2    . VAL D 1 126 ? 25.803  15.899  54.983  1.00 49.75  ? 125 VAL C CG2    1 
ATOM   9593  H  H      . VAL D 1 126 ? 26.720  13.203  55.872  1.00 63.91  ? 125 VAL C H      1 
ATOM   9594  H  HA     . VAL D 1 126 ? 25.445  14.923  57.546  1.00 64.71  ? 125 VAL C HA     1 
ATOM   9595  H  HB     . VAL D 1 126 ? 24.652  14.217  54.924  1.00 61.41  ? 125 VAL C HB     1 
ATOM   9596  H  HG11   . VAL D 1 126 ? 23.258  16.178  55.129  1.00 64.51  ? 125 VAL C HG11   1 
ATOM   9597  H  HG12   . VAL D 1 126 ? 22.801  14.922  55.988  1.00 64.51  ? 125 VAL C HG12   1 
ATOM   9598  H  HG13   . VAL D 1 126 ? 23.574  16.122  56.685  1.00 64.51  ? 125 VAL C HG13   1 
ATOM   9599  H  HG21   . VAL D 1 126 ? 25.381  16.360  54.241  1.00 59.73  ? 125 VAL C HG21   1 
ATOM   9600  H  HG22   . VAL D 1 126 ? 26.062  16.538  55.666  1.00 59.73  ? 125 VAL C HG22   1 
ATOM   9601  H  HG23   . VAL D 1 126 ? 26.584  15.415  54.671  1.00 59.73  ? 125 VAL C HG23   1 
ATOM   9602  N  N      . ASP D 1 127 ? 24.252  13.000  58.606  1.00 51.76  ? 126 ASP C N      1 
ATOM   9603  C  CA     . ASP D 1 127 ? 23.410  11.908  59.086  1.00 53.54  ? 126 ASP C CA     1 
ATOM   9604  C  C      . ASP D 1 127 ? 22.027  11.992  58.445  1.00 51.57  ? 126 ASP C C      1 
ATOM   9605  O  O      . ASP D 1 127 ? 21.490  13.077  58.217  1.00 51.29  ? 126 ASP C O      1 
ATOM   9606  C  CB     . ASP D 1 127 ? 23.225  11.914  60.621  1.00 53.02  ? 126 ASP C CB     1 
ATOM   9607  C  CG     . ASP D 1 127 ? 24.525  11.834  61.387  1.00 54.41  ? 126 ASP C CG     1 
ATOM   9608  O  OD1    . ASP D 1 127 ? 25.465  11.151  60.940  1.00 54.95  ? 126 ASP C OD1    1 
ATOM   9609  O  OD2    . ASP D 1 127 ? 24.593  12.420  62.493  1.00 57.89  ? 126 ASP C OD2    1 
ATOM   9610  H  H      . ASP D 1 127 ? 24.532  13.542  59.212  1.00 62.15  ? 126 ASP C H      1 
ATOM   9611  H  HA     . ASP D 1 127 ? 23.853  11.079  58.848  1.00 64.28  ? 126 ASP C HA     1 
ATOM   9612  H  HB2    . ASP D 1 127 ? 22.780  12.736  60.879  1.00 63.46  ? 126 ASP C HB2    1 
ATOM   9613  H  HB3    . ASP D 1 127 ? 22.684  11.150  60.874  1.00 63.46  ? 126 ASP C HB3    1 
ATOM   9614  N  N      . THR D 1 128 ? 21.440  10.823  58.178  1.00 52.08  ? 127 THR C N      1 
ATOM   9615  C  CA     . THR D 1 128 ? 20.037  10.743  57.787  1.00 50.78  ? 127 THR C CA     1 
ATOM   9616  C  C      . THR D 1 128 ? 19.162  11.644  58.652  1.00 52.86  ? 127 THR C C      1 
ATOM   9617  O  O      . THR D 1 128 ? 18.294  12.369  58.147  1.00 52.25  ? 127 THR C O      1 
ATOM   9618  C  CB     . THR D 1 128 ? 19.553  9.289   57.892  1.00 51.82  ? 127 THR C CB     1 
ATOM   9619  O  OG1    . THR D 1 128 ? 20.435  8.439   57.142  1.00 54.30  ? 127 THR C OG1    1 
ATOM   9620  C  CG2    . THR D 1 128 ? 18.127  9.147   57.332  1.00 49.92  ? 127 THR C CG2    1 
ATOM   9621  H  H      . THR D 1 128 ? 21.836  10.060  58.218  1.00 62.53  ? 127 THR C H      1 
ATOM   9622  H  HA     . THR D 1 128 ? 19.957  11.032  56.864  1.00 60.97  ? 127 THR C HA     1 
ATOM   9623  H  HB     . THR D 1 128 ? 19.545  9.020   58.824  1.00 62.22  ? 127 THR C HB     1 
ATOM   9624  H  HG1    . THR D 1 128 ? 20.443  8.674   56.336  1.00 65.19  ? 127 THR C HG1    1 
ATOM   9625  H  HG21   . THR D 1 128 ? 17.870  8.212   57.313  1.00 59.93  ? 127 THR C HG21   1 
ATOM   9626  H  HG22   . THR D 1 128 ? 17.501  9.633   57.891  1.00 59.93  ? 127 THR C HG22   1 
ATOM   9627  H  HG23   . THR D 1 128 ? 18.087  9.503   56.431  1.00 59.93  ? 127 THR C HG23   1 
ATOM   9628  N  N      . LYS D 1 129 ? 19.371  11.583  59.970  1.00 51.78  ? 128 LYS C N      1 
ATOM   9629  C  CA     . LYS D 1 129 ? 18.544  12.354  60.887  1.00 53.05  ? 128 LYS C CA     1 
ATOM   9630  C  C      . LYS D 1 129 ? 18.675  13.847  60.623  1.00 57.51  ? 128 LYS C C      1 
ATOM   9631  O  O      . LYS D 1 129 ? 17.694  14.590  60.757  1.00 58.09  ? 128 LYS C O      1 
ATOM   9632  C  CB     . LYS D 1 129 ? 18.929  12.024  62.336  1.00 55.38  ? 128 LYS C CB     1 
ATOM   9633  C  CG     . LYS D 1 129 ? 18.252  12.863  63.393  1.00 56.95  ? 128 LYS C CG     1 
ATOM   9634  C  CD     . LYS D 1 129 ? 17.049  12.158  64.009  1.00 58.07  ? 128 LYS C CD     1 
ATOM   9635  C  CE     . LYS D 1 129 ? 16.372  13.030  65.062  1.00 59.74  ? 128 LYS C CE     1 
ATOM   9636  N  NZ     . LYS D 1 129 ? 17.364  13.727  65.925  1.00 63.64  ? 128 LYS C NZ     1 
ATOM   9637  H  H      . LYS D 1 129 ? 19.979  11.108  60.350  1.00 61.96  ? 128 LYS C H      1 
ATOM   9638  H  HA     . LYS D 1 129 ? 17.615  12.108  60.757  1.00 63.49  ? 128 LYS C HA     1 
ATOM   9639  H  HB2    . LYS D 1 129 ? 18.699  11.098  62.510  1.00 66.28  ? 128 LYS C HB2    1 
ATOM   9640  H  HB3    . LYS D 1 129 ? 19.886  12.152  62.434  1.00 66.28  ? 128 LYS C HB3    1 
ATOM   9641  H  HG2    . LYS D 1 129 ? 18.885  13.054  64.103  1.00 68.18  ? 128 LYS C HG2    1 
ATOM   9642  H  HG3    . LYS D 1 129 ? 17.943  13.691  62.993  1.00 68.18  ? 128 LYS C HG3    1 
ATOM   9643  H  HD2    . LYS D 1 129 ? 16.402  11.960  63.315  1.00 69.51  ? 128 LYS C HD2    1 
ATOM   9644  H  HD3    . LYS D 1 129 ? 17.341  11.337  64.435  1.00 69.51  ? 128 LYS C HD3    1 
ATOM   9645  H  HE2    . LYS D 1 129 ? 15.829  13.702  64.620  1.00 71.51  ? 128 LYS C HE2    1 
ATOM   9646  H  HE3    . LYS D 1 129 ? 15.815  12.474  65.628  1.00 71.51  ? 128 LYS C HE3    1 
ATOM   9647  H  HZ1    . LYS D 1 129 ? 16.948  14.133  66.599  1.00 76.40  ? 128 LYS C HZ1    1 
ATOM   9648  H  HZ2    . LYS D 1 129 ? 17.945  13.140  66.255  1.00 76.40  ? 128 LYS C HZ2    1 
ATOM   9649  H  HZ3    . LYS D 1 129 ? 17.806  14.335  65.450  1.00 76.40  ? 128 LYS C HZ3    1 
ATOM   9650  N  N      . GLN D 1 130 ? 19.880  14.315  60.275  1.00 53.57  ? 129 GLN C N      1 
ATOM   9651  C  CA     . GLN D 1 130 ? 20.036  15.732  59.978  1.00 55.12  ? 129 GLN C CA     1 
ATOM   9652  C  C      . GLN D 1 130 ? 19.110  16.122  58.839  1.00 50.85  ? 129 GLN C C      1 
ATOM   9653  O  O      . GLN D 1 130 ? 18.346  17.081  58.944  1.00 49.69  ? 129 GLN C O      1 
ATOM   9654  C  CB     . GLN D 1 130 ? 21.481  16.076  59.603  1.00 53.02  ? 129 GLN C CB     1 
ATOM   9655  C  CG     . GLN D 1 130 ? 22.530  15.931  60.708  1.00 59.86  ? 129 GLN C CG     1 
ATOM   9656  C  CD     . GLN D 1 130 ? 23.945  16.091  60.165  1.00 59.82  ? 129 GLN C CD     1 
ATOM   9657  O  OE1    . GLN D 1 130 ? 24.767  15.179  60.272  1.00 59.20  ? 129 GLN C OE1    1 
ATOM   9658  N  NE2    . GLN D 1 130 ? 24.231  17.254  59.562  1.00 60.88  ? 129 GLN C NE2    1 
ATOM   9659  H  H      . GLN D 1 130 ? 20.597  13.845  60.207  1.00 64.31  ? 129 GLN C H      1 
ATOM   9660  H  HA     . GLN D 1 130 ? 19.818  16.234  60.778  1.00 66.18  ? 129 GLN C HA     1 
ATOM   9661  H  HB2    . GLN D 1 130 ? 21.751  15.491  58.877  1.00 63.65  ? 129 GLN C HB2    1 
ATOM   9662  H  HB3    . GLN D 1 130 ? 21.504  17.000  59.309  1.00 63.65  ? 129 GLN C HB3    1 
ATOM   9663  H  HG2    . GLN D 1 130 ? 22.383  16.615  61.380  1.00 71.87  ? 129 GLN C HG2    1 
ATOM   9664  H  HG3    . GLN D 1 130 ? 22.455  15.051  61.108  1.00 71.87  ? 129 GLN C HG3    1 
ATOM   9665  H  HE21   . GLN D 1 130 ? 23.629  17.864  59.498  1.00 73.09  ? 129 GLN C HE21   1 
ATOM   9666  H  HE22   . GLN D 1 130 ? 25.017  17.389  59.240  1.00 73.09  ? 129 GLN C HE22   1 
ATOM   9667  N  N      . ALA D 1 131 ? 19.190  15.393  57.724  1.00 53.32  ? 130 ALA C N      1 
ATOM   9668  C  CA     . ALA D 1 131 ? 18.346  15.696  56.577  1.00 51.38  ? 130 ALA C CA     1 
ATOM   9669  C  C      . ALA D 1 131 ? 16.870  15.458  56.884  1.00 53.21  ? 130 ALA C C      1 
ATOM   9670  O  O      . ALA D 1 131 ? 16.004  16.195  56.393  1.00 51.23  ? 130 ALA C O      1 
ATOM   9671  C  CB     . ALA D 1 131 ? 18.783  14.854  55.378  1.00 50.49  ? 130 ALA C CB     1 
ATOM   9672  H  H      . ALA D 1 131 ? 19.720  14.725  57.611  1.00 64.02  ? 130 ALA C H      1 
ATOM   9673  H  HA     . ALA D 1 131 ? 18.454  16.634  56.352  1.00 61.70  ? 130 ALA C HA     1 
ATOM   9674  H  HB1    . ALA D 1 131 ? 18.213  15.062  54.621  1.00 60.62  ? 130 ALA C HB1    1 
ATOM   9675  H  HB2    . ALA D 1 131 ? 19.706  15.063  55.165  1.00 60.62  ? 130 ALA C HB2    1 
ATOM   9676  H  HB3    . ALA D 1 131 ? 18.701  13.915  55.605  1.00 60.62  ? 130 ALA C HB3    1 
ATOM   9677  N  N      . GLN D 1 132 ? 16.549  14.426  57.671  1.00 56.82  ? 131 GLN C N      1 
ATOM   9678  C  CA     . GLN D 1 132 ? 15.161  14.259  58.088  1.00 54.62  ? 131 GLN C CA     1 
ATOM   9679  C  C      . GLN D 1 132 ? 14.692  15.507  58.832  1.00 50.34  ? 131 GLN C C      1 
ATOM   9680  O  O      . GLN D 1 132 ? 13.704  16.141  58.456  1.00 54.98  ? 131 GLN C O      1 
ATOM   9681  C  CB     . GLN D 1 132 ? 14.996  13.000  58.951  1.00 53.98  ? 131 GLN C CB     1 
ATOM   9682  C  CG     . GLN D 1 132 ? 15.136  11.671  58.209  1.00 52.46  ? 131 GLN C CG     1 
ATOM   9683  C  CD     . GLN D 1 132 ? 15.070  10.448  59.139  1.00 54.84  ? 131 GLN C CD     1 
ATOM   9684  O  OE1    . GLN D 1 132 ? 15.640  10.458  60.226  1.00 58.69  ? 131 GLN C OE1    1 
ATOM   9685  N  NE2    . GLN D 1 132 ? 14.377  9.393   58.702  1.00 56.34  ? 131 GLN C NE2    1 
ATOM   9686  H  H      . GLN D 1 132 ? 17.097  13.833  57.966  1.00 68.21  ? 131 GLN C H      1 
ATOM   9687  H  HA     . GLN D 1 132 ? 14.605  14.132  57.303  1.00 65.57  ? 131 GLN C HA     1 
ATOM   9688  H  HB2    . GLN D 1 132 ? 15.673  13.016  59.645  1.00 64.81  ? 131 GLN C HB2    1 
ATOM   9689  H  HB3    . GLN D 1 132 ? 14.112  13.017  59.349  1.00 64.81  ? 131 GLN C HB3    1 
ATOM   9690  H  HG2    . GLN D 1 132 ? 14.416  11.594  57.563  1.00 62.99  ? 131 GLN C HG2    1 
ATOM   9691  H  HG3    . GLN D 1 132 ? 15.993  11.654  57.754  1.00 62.99  ? 131 GLN C HG3    1 
ATOM   9692  H  HE21   . GLN D 1 132 ? 13.994  9.419   57.933  1.00 67.64  ? 131 GLN C HE21   1 
ATOM   9693  H  HE22   . GLN D 1 132 ? 14.314  8.688   59.191  1.00 67.64  ? 131 GLN C HE22   1 
ATOM   9694  N  N      . ASP D 1 133 ? 15.416  15.892  59.876  1.00 57.00  ? 132 ASP C N      1 
ATOM   9695  C  CA     . ASP D 1 133 ? 15.010  17.041  60.683  1.00 52.87  ? 132 ASP C CA     1 
ATOM   9696  C  C      . ASP D 1 133 ? 14.905  18.323  59.872  1.00 58.86  ? 132 ASP C C      1 
ATOM   9697  O  O      . ASP D 1 133 ? 14.064  19.172  60.182  1.00 59.67  ? 132 ASP C O      1 
ATOM   9698  C  CB     . ASP D 1 133 ? 15.999  17.229  61.819  1.00 58.34  ? 132 ASP C CB     1 
ATOM   9699  C  CG     . ASP D 1 133 ? 15.924  16.108  62.821  1.00 55.88  ? 132 ASP C CG     1 
ATOM   9700  O  OD1    . ASP D 1 133 ? 14.871  15.450  62.879  1.00 56.10  ? 132 ASP C OD1    1 
ATOM   9701  O  OD2    . ASP D 1 133 ? 16.930  15.874  63.514  1.00 62.77  ? 132 ASP C OD2    1 
ATOM   9702  H  H      . ASP D 1 133 ? 16.140  15.511  60.139  1.00 68.43  ? 132 ASP C H      1 
ATOM   9703  H  HA     . ASP D 1 133 ? 14.129  16.862  61.049  1.00 63.48  ? 132 ASP C HA     1 
ATOM   9704  H  HB2    . ASP D 1 133 ? 16.899  17.254  61.458  1.00 70.05  ? 132 ASP C HB2    1 
ATOM   9705  H  HB3    . ASP D 1 133 ? 15.803  18.060  62.279  1.00 70.05  ? 132 ASP C HB3    1 
ATOM   9706  N  N      . LEU D 1 134 ? 15.747  18.492  58.838  1.00 53.15  ? 133 LEU C N      1 
ATOM   9707  C  CA     . LEU D 1 134 ? 15.679  19.695  58.017  1.00 53.29  ? 133 LEU C CA     1 
ATOM   9708  C  C      . LEU D 1 134 ? 14.493  19.617  57.059  1.00 55.33  ? 133 LEU C C      1 
ATOM   9709  O  O      . LEU D 1 134 ? 13.773  20.601  56.871  1.00 59.49  ? 133 LEU C O      1 
ATOM   9710  C  CB     . LEU D 1 134 ? 16.990  19.897  57.229  1.00 54.62  ? 133 LEU C CB     1 
ATOM   9711  C  CG     . LEU D 1 134 ? 17.059  21.110  56.283  1.00 55.06  ? 133 LEU C CG     1 
ATOM   9712  C  CD1    . LEU D 1 134 ? 17.096  22.419  57.044  1.00 56.04  ? 133 LEU C CD1    1 
ATOM   9713  C  CD2    . LEU D 1 134 ? 18.242  21.071  55.275  1.00 53.11  ? 133 LEU C CD2    1 
ATOM   9714  H  H      . LEU D 1 134 ? 16.354  17.931  58.601  1.00 63.82  ? 133 LEU C H      1 
ATOM   9715  H  HA     . LEU D 1 134 ? 15.571  20.466  58.596  1.00 63.98  ? 133 LEU C HA     1 
ATOM   9716  H  HB2    . LEU D 1 134 ? 17.710  19.998  57.870  1.00 65.58  ? 133 LEU C HB2    1 
ATOM   9717  H  HB3    . LEU D 1 134 ? 17.136  19.107  56.686  1.00 65.58  ? 133 LEU C HB3    1 
ATOM   9718  H  HG     . LEU D 1 134 ? 16.244  21.062  55.759  1.00 66.11  ? 133 LEU C HG     1 
ATOM   9719  H  HD11   . LEU D 1 134 ? 17.683  23.037  56.581  1.00 67.29  ? 133 LEU C HD11   1 
ATOM   9720  H  HD12   . LEU D 1 134 ? 16.199  22.785  57.087  1.00 67.29  ? 133 LEU C HD12   1 
ATOM   9721  H  HD13   . LEU D 1 134 ? 17.430  22.254  57.940  1.00 67.29  ? 133 LEU C HD13   1 
ATOM   9722  H  HD21   . LEU D 1 134 ? 18.181  21.839  54.686  1.00 63.76  ? 133 LEU C HD21   1 
ATOM   9723  H  HD22   . LEU D 1 134 ? 19.078  21.098  55.768  1.00 63.76  ? 133 LEU C HD22   1 
ATOM   9724  H  HD23   . LEU D 1 134 ? 18.190  20.252  54.758  1.00 63.76  ? 133 LEU C HD23   1 
ATOM   9725  N  N      . ALA D 1 135 ? 14.263  18.455  56.457  1.00 46.43  ? 134 ALA C N      1 
ATOM   9726  C  CA     . ALA D 1 135 ? 13.107  18.305  55.595  1.00 50.72  ? 134 ALA C CA     1 
ATOM   9727  C  C      . ALA D 1 135 ? 11.824  18.547  56.379  1.00 56.50  ? 134 ALA C C      1 
ATOM   9728  O  O      . ALA D 1 135 ? 10.928  19.260  55.917  1.00 55.82  ? 134 ALA C O      1 
ATOM   9729  C  CB     . ALA D 1 135 ? 13.109  16.915  54.951  1.00 50.23  ? 134 ALA C CB     1 
ATOM   9730  H  H      . ALA D 1 135 ? 14.755  17.753  56.532  1.00 55.54  ? 134 ALA C H      1 
ATOM   9731  H  HA     . ALA D 1 135 ? 13.151  18.959  54.880  1.00 60.90  ? 134 ALA C HA     1 
ATOM   9732  H  HB1    . ALA D 1 135 ? 12.331  16.832  54.378  1.00 60.31  ? 134 ALA C HB1    1 
ATOM   9733  H  HB2    . ALA D 1 135 ? 13.918  16.812  54.426  1.00 60.31  ? 134 ALA C HB2    1 
ATOM   9734  H  HB3    . ALA D 1 135 ? 13.079  16.243  55.650  1.00 60.31  ? 134 ALA C HB3    1 
ATOM   9735  N  N      . ARG D 1 136 ? 11.718  17.969  57.575  1.00 48.46  ? 135 ARG C N      1 
ATOM   9736  C  CA     . ARG D 1 136 ? 10.540  18.207  58.399  1.00 58.07  ? 135 ARG C CA     1 
ATOM   9737  C  C      . ARG D 1 136 ? 10.234  19.699  58.480  1.00 61.15  ? 135 ARG C C      1 
ATOM   9738  O  O      . ARG D 1 136 ? 9.130   20.141  58.142  1.00 64.57  ? 135 ARG C O      1 
ATOM   9739  C  CB     . ARG D 1 136 ? 10.738  17.635  59.810  1.00 58.31  ? 135 ARG C CB     1 
ATOM   9740  C  CG     . ARG D 1 136 ? 9.433   17.458  60.619  1.00 64.24  ? 135 ARG C CG     1 
ATOM   9741  C  CD     . ARG D 1 136 ? 9.682   16.714  61.930  1.00 68.88  ? 135 ARG C CD     1 
ATOM   9742  N  NE     . ARG D 1 136 ? 10.055  15.331  61.653  1.00 71.96  ? 135 ARG C NE     1 
ATOM   9743  C  CZ     . ARG D 1 136 ? 11.253  14.808  61.884  1.00 71.02  ? 135 ARG C CZ     1 
ATOM   9744  N  NH1    . ARG D 1 136 ? 12.197  15.488  62.524  1.00 64.97  ? 135 ARG C NH1    1 
ATOM   9745  N  NH2    . ARG D 1 136 ? 11.513  13.574  61.455  1.00 67.33  ? 135 ARG C NH2    1 
ATOM   9746  H  H      . ARG D 1 136 ? 12.304  17.445  57.924  1.00 57.98  ? 135 ARG C H      1 
ATOM   9747  H  HA     . ARG D 1 136 ? 9.788   17.747  57.995  1.00 69.72  ? 135 ARG C HA     1 
ATOM   9748  H  HB2    . ARG D 1 136 ? 11.157  16.764  59.735  1.00 70.01  ? 135 ARG C HB2    1 
ATOM   9749  H  HB3    . ARG D 1 136 ? 11.313  18.237  60.310  1.00 70.01  ? 135 ARG C HB3    1 
ATOM   9750  H  HG2    . ARG D 1 136 ? 9.064   18.330  60.829  1.00 77.12  ? 135 ARG C HG2    1 
ATOM   9751  H  HG3    . ARG D 1 136 ? 8.797   16.946  60.095  1.00 77.12  ? 135 ARG C HG3    1 
ATOM   9752  H  HD2    . ARG D 1 136 ? 10.405  17.140  62.416  1.00 82.69  ? 135 ARG C HD2    1 
ATOM   9753  H  HD3    . ARG D 1 136 ? 8.874   16.717  62.466  1.00 82.69  ? 135 ARG C HD3    1 
ATOM   9754  H  HE     . ARG D 1 136 ? 9.454   14.817  61.314  1.00 86.39  ? 135 ARG C HE     1 
ATOM   9755  H  HH11   . ARG D 1 136 ? 12.039  16.288  62.800  1.00 78.00  ? 135 ARG C HH11   1 
ATOM   9756  H  HH12   . ARG D 1 136 ? 12.966  15.129  62.663  1.00 78.00  ? 135 ARG C HH12   1 
ATOM   9757  H  HH21   . ARG D 1 136 ? 10.909  13.129  61.034  1.00 80.83  ? 135 ARG C HH21   1 
ATOM   9758  H  HH22   . ARG D 1 136 ? 12.285  13.223  61.598  1.00 80.83  ? 135 ARG C HH22   1 
ATOM   9759  N  N      . SER D 1 137 ? 11.222  20.492  58.914  1.00 56.16  ? 136 SER C N      1 
ATOM   9760  C  CA     . SER D 1 137 ? 10.998  21.918  59.128  1.00 53.43  ? 136 SER C CA     1 
ATOM   9761  C  C      . SER D 1 137 ? 10.398  22.592  57.902  1.00 59.84  ? 136 SER C C      1 
ATOM   9762  O  O      . SER D 1 137 ? 9.459   23.391  58.023  1.00 60.26  ? 136 SER C O      1 
ATOM   9763  C  CB     . SER D 1 137 ? 12.315  22.599  59.519  1.00 60.25  ? 136 SER C CB     1 
ATOM   9764  O  OG     . SER D 1 137 ? 13.283  22.470  58.494  1.00 56.99  ? 136 SER C OG     1 
ATOM   9765  H  H      . SER D 1 137 ? 12.022  20.229  59.088  1.00 67.43  ? 136 SER C H      1 
ATOM   9766  H  HA     . SER D 1 137 ? 10.367  22.022  59.858  1.00 64.15  ? 136 SER C HA     1 
ATOM   9767  H  HB2    . SER D 1 137 ? 12.147  23.541  59.677  1.00 72.34  ? 136 SER C HB2    1 
ATOM   9768  H  HB3    . SER D 1 137 ? 12.656  22.183  60.327  1.00 72.34  ? 136 SER C HB3    1 
ATOM   9769  H  HG     . SER D 1 137 ? 13.438  21.658  58.345  1.00 68.42  ? 136 SER C HG     1 
ATOM   9770  N  N      . TYR D 1 138 ? 10.917  22.281  56.711  1.00 54.51  ? 137 TYR C N      1 
ATOM   9771  C  CA     . TYR D 1 138 ? 10.431  22.933  55.512  1.00 53.22  ? 137 TYR C CA     1 
ATOM   9772  C  C      . TYR D 1 138 ? 9.083   22.410  55.007  1.00 57.64  ? 137 TYR C C      1 
ATOM   9773  O  O      . TYR D 1 138 ? 8.477   23.051  54.143  1.00 58.87  ? 137 TYR C O      1 
ATOM   9774  C  CB     . TYR D 1 138 ? 11.417  22.781  54.344  1.00 59.91  ? 137 TYR C CB     1 
ATOM   9775  C  CG     . TYR D 1 138 ? 12.852  23.192  54.578  1.00 60.47  ? 137 TYR C CG     1 
ATOM   9776  C  CD1    . TYR D 1 138 ? 13.183  24.231  55.439  1.00 55.41  ? 137 TYR C CD1    1 
ATOM   9777  C  CD2    . TYR D 1 138 ? 13.875  22.592  53.846  1.00 58.95  ? 137 TYR C CD2    1 
ATOM   9778  C  CE1    . TYR D 1 138 ? 14.504  24.617  55.604  1.00 59.84  ? 137 TYR C CE1    1 
ATOM   9779  C  CE2    . TYR D 1 138 ? 15.192  22.978  54.003  1.00 60.44  ? 137 TYR C CE2    1 
ATOM   9780  C  CZ     . TYR D 1 138 ? 15.500  23.993  54.863  1.00 61.44  ? 137 TYR C CZ     1 
ATOM   9781  O  OH     . TYR D 1 138 ? 16.825  24.348  54.989  1.00 69.31  ? 137 TYR C OH     1 
ATOM   9782  H  H      . TYR D 1 138 ? 11.542  21.704  56.581  1.00 65.45  ? 137 TYR C H      1 
ATOM   9783  H  HA     . TYR D 1 138 ? 10.344  23.869  55.751  1.00 63.89  ? 137 TYR C HA     1 
ATOM   9784  H  HB2    . TYR D 1 138 ? 11.432  21.846  54.088  1.00 71.93  ? 137 TYR C HB2    1 
ATOM   9785  H  HB3    . TYR D 1 138 ? 11.089  23.321  53.607  1.00 71.93  ? 137 TYR C HB3    1 
ATOM   9786  H  HD1    . TYR D 1 138 ? 12.512  24.671  55.909  1.00 66.53  ? 137 TYR C HD1    1 
ATOM   9787  H  HD2    . TYR D 1 138 ? 13.666  21.918  53.240  1.00 70.77  ? 137 TYR C HD2    1 
ATOM   9788  H  HE1    . TYR D 1 138 ? 14.722  25.290  56.208  1.00 71.84  ? 137 TYR C HE1    1 
ATOM   9789  H  HE2    . TYR D 1 138 ? 15.865  22.550  53.525  1.00 72.56  ? 137 TYR C HE2    1 
ATOM   9790  H  HH     . TYR D 1 138 ? 17.307  23.819  54.548  1.00 83.20  ? 137 TYR C HH     1 
ATOM   9791  N  N      . GLY D 1 139 ? 8.621   21.252  55.472  1.00 55.28  ? 138 GLY C N      1 
ATOM   9792  C  CA     . GLY D 1 139 ? 7.378   20.700  54.964  1.00 57.42  ? 138 GLY C CA     1 
ATOM   9793  C  C      . GLY D 1 139 ? 7.445   19.941  53.645  1.00 59.15  ? 138 GLY C C      1 
ATOM   9794  O  O      . GLY D 1 139 ? 6.465   19.951  52.877  1.00 55.09  ? 138 GLY C O      1 
ATOM   9795  H  H      . GLY D 1 139 ? 9.007   20.774  56.074  1.00 66.37  ? 138 GLY C H      1 
ATOM   9796  H  HA2    . GLY D 1 139 ? 7.025   20.088  55.629  1.00 68.94  ? 138 GLY C HA2    1 
ATOM   9797  H  HA3    . GLY D 1 139 ? 6.751   21.430  54.843  1.00 68.94  ? 138 GLY C HA3    1 
ATOM   9798  N  N      . ILE D 1 140 ? 8.543   19.242  53.370  1.00 54.58  ? 139 ILE C N      1 
ATOM   9799  C  CA     . ILE D 1 140 ? 8.683   18.519  52.104  1.00 50.48  ? 139 ILE C CA     1 
ATOM   9800  C  C      . ILE D 1 140 ? 9.276   17.137  52.352  1.00 48.77  ? 139 ILE C C      1 
ATOM   9801  O  O      . ILE D 1 140 ? 9.934   16.887  53.370  1.00 52.41  ? 139 ILE C O      1 
ATOM   9802  C  CB     . ILE D 1 140 ? 9.561   19.301  51.091  1.00 50.18  ? 139 ILE C CB     1 
ATOM   9803  C  CG1    . ILE D 1 140 ? 11.011  19.380  51.605  1.00 52.86  ? 139 ILE C CG1    1 
ATOM   9804  C  CG2    . ILE D 1 140 ? 8.960   20.692  50.803  1.00 47.62  ? 139 ILE C CG2    1 
ATOM   9805  C  CD1    . ILE D 1 140 ? 12.027  20.024  50.603  1.00 44.14  ? 139 ILE C CD1    1 
ATOM   9806  H  H      . ILE D 1 140 ? 9.219   19.169  53.897  1.00 65.53  ? 139 ILE C H      1 
ATOM   9807  H  HA     . ILE D 1 140 ? 7.802   18.392  51.719  1.00 60.62  ? 139 ILE C HA     1 
ATOM   9808  H  HB     . ILE D 1 140 ? 9.576   18.823  50.247  1.00 60.25  ? 139 ILE C HB     1 
ATOM   9809  H  HG12   . ILE D 1 140 ? 11.022  19.914  52.415  1.00 63.46  ? 139 ILE C HG12   1 
ATOM   9810  H  HG13   . ILE D 1 140 ? 11.320  18.481  51.796  1.00 63.46  ? 139 ILE C HG13   1 
ATOM   9811  H  HG21   . ILE D 1 140 ? 9.629   21.241  50.364  1.00 57.18  ? 139 ILE C HG21   1 
ATOM   9812  H  HG22   . ILE D 1 140 ? 8.186   20.589  50.227  1.00 57.18  ? 139 ILE C HG22   1 
ATOM   9813  H  HG23   . ILE D 1 140 ? 8.695   21.101  51.642  1.00 57.18  ? 139 ILE C HG23   1 
ATOM   9814  H  HD11   . ILE D 1 140 ? 12.929  19.792  50.875  1.00 53.00  ? 139 ILE C HD11   1 
ATOM   9815  H  HD12   . ILE D 1 140 ? 11.852  19.682  49.712  1.00 53.00  ? 139 ILE C HD12   1 
ATOM   9816  H  HD13   . ILE D 1 140 ? 11.916  20.987  50.616  1.00 53.00  ? 139 ILE C HD13   1 
ATOM   9817  N  N      . PRO D 1 141 ? 9.069   16.220  51.414  1.00 40.58  ? 140 PRO C N      1 
ATOM   9818  C  CA     . PRO D 1 141 ? 9.625   14.865  51.555  1.00 46.68  ? 140 PRO C CA     1 
ATOM   9819  C  C      . PRO D 1 141 ? 11.147  14.839  51.519  1.00 47.49  ? 140 PRO C C      1 
ATOM   9820  O  O      . PRO D 1 141 ? 11.790  15.705  50.920  1.00 49.45  ? 140 PRO C O      1 
ATOM   9821  C  CB     . PRO D 1 141 ? 9.039   14.119  50.342  1.00 51.10  ? 140 PRO C CB     1 
ATOM   9822  C  CG     . PRO D 1 141 ? 7.793   14.886  49.990  1.00 47.74  ? 140 PRO C CG     1 
ATOM   9823  C  CD     . PRO D 1 141 ? 8.150   16.325  50.264  1.00 47.39  ? 140 PRO C CD     1 
ATOM   9824  H  HA     . PRO D 1 141 ? 9.320   14.468  52.386  1.00 56.05  ? 140 PRO C HA     1 
ATOM   9825  H  HB2    . PRO D 1 141 ? 9.674   14.129  49.608  1.00 61.35  ? 140 PRO C HB2    1 
ATOM   9826  H  HB3    . PRO D 1 141 ? 8.829   13.204  50.585  1.00 61.35  ? 140 PRO C HB3    1 
ATOM   9827  H  HG2    . PRO D 1 141 ? 7.573   14.753  49.055  1.00 57.32  ? 140 PRO C HG2    1 
ATOM   9828  H  HG3    . PRO D 1 141 ? 7.055   14.597  50.549  1.00 57.32  ? 140 PRO C HG3    1 
ATOM   9829  H  HD2    . PRO D 1 141 ? 8.595   16.723  49.500  1.00 56.90  ? 140 PRO C HD2    1 
ATOM   9830  H  HD3    . PRO D 1 141 ? 7.361   16.840  50.495  1.00 56.90  ? 140 PRO C HD3    1 
ATOM   9831  N  N      . PHE D 1 142 ? 11.723  13.808  52.169  1.00 50.57  ? 141 PHE C N      1 
ATOM   9832  C  CA     . PHE D 1 142 ? 13.166  13.530  52.117  1.00 48.74  ? 141 PHE C CA     1 
ATOM   9833  C  C      . PHE D 1 142 ? 13.417  12.089  51.666  1.00 49.25  ? 141 PHE C C      1 
ATOM   9834  O  O      . PHE D 1 142 ? 12.858  11.145  52.249  1.00 44.85  ? 141 PHE C O      1 
ATOM   9835  C  CB     . PHE D 1 142 ? 13.843  13.782  53.479  1.00 48.54  ? 141 PHE C CB     1 
ATOM   9836  C  CG     . PHE D 1 142 ? 15.255  13.223  53.573  1.00 51.16  ? 141 PHE C CG     1 
ATOM   9837  C  CD1    . PHE D 1 142 ? 16.266  13.704  52.745  1.00 50.00  ? 141 PHE C CD1    1 
ATOM   9838  C  CD2    . PHE D 1 142 ? 15.565  12.225  54.500  1.00 52.05  ? 141 PHE C CD2    1 
ATOM   9839  C  CE1    . PHE D 1 142 ? 17.563  13.186  52.825  1.00 50.53  ? 141 PHE C CE1    1 
ATOM   9840  C  CE2    . PHE D 1 142 ? 16.845  11.699  54.591  1.00 53.28  ? 141 PHE C CE2    1 
ATOM   9841  C  CZ     . PHE D 1 142 ? 17.848  12.177  53.761  1.00 52.92  ? 141 PHE C CZ     1 
ATOM   9842  H  H      . PHE D 1 142 ? 11.286  13.247  52.654  1.00 60.72  ? 141 PHE C H      1 
ATOM   9843  H  HA     . PHE D 1 142 ? 13.565  14.120  51.459  1.00 58.53  ? 141 PHE C HA     1 
ATOM   9844  H  HB2    . PHE D 1 142 ? 13.892  14.738  53.631  1.00 58.29  ? 141 PHE C HB2    1 
ATOM   9845  H  HB3    . PHE D 1 142 ? 13.311  13.362  54.174  1.00 58.29  ? 141 PHE C HB3    1 
ATOM   9846  H  HD1    . PHE D 1 142 ? 16.077  14.378  52.133  1.00 60.03  ? 141 PHE C HD1    1 
ATOM   9847  H  HD2    . PHE D 1 142 ? 14.901  11.906  55.067  1.00 62.49  ? 141 PHE C HD2    1 
ATOM   9848  H  HE1    . PHE D 1 142 ? 18.232  13.506  52.263  1.00 60.67  ? 141 PHE C HE1    1 
ATOM   9849  H  HE2    . PHE D 1 142 ? 17.030  11.028  55.206  1.00 63.97  ? 141 PHE C HE2    1 
ATOM   9850  H  HZ     . PHE D 1 142 ? 18.708  11.831  53.824  1.00 63.54  ? 141 PHE C HZ     1 
ATOM   9851  N  N      . ILE D 1 143 ? 14.265  11.935  50.636  1.00 47.23  ? 142 ILE C N      1 
ATOM   9852  C  CA     . ILE D 1 143 ? 14.608  10.645  50.035  1.00 46.31  ? 142 ILE C CA     1 
ATOM   9853  C  C      . ILE D 1 143 ? 16.129  10.543  49.890  1.00 47.99  ? 142 ILE C C      1 
ATOM   9854  O  O      . ILE D 1 143 ? 16.754  11.411  49.275  1.00 42.92  ? 142 ILE C O      1 
ATOM   9855  C  CB     . ILE D 1 143 ? 13.944  10.453  48.659  1.00 51.00  ? 142 ILE C CB     1 
ATOM   9856  C  CG1    . ILE D 1 143 ? 12.425  10.678  48.726  1.00 52.23  ? 142 ILE C CG1    1 
ATOM   9857  C  CG2    . ILE D 1 143 ? 14.273  9.061   48.116  1.00 50.38  ? 142 ILE C CG2    1 
ATOM   9858  C  CD1    . ILE D 1 143 ? 12.008  12.158  48.777  1.00 52.41  ? 142 ILE C CD1    1 
ATOM   9859  H  H      . ILE D 1 143 ? 14.668  12.593  50.256  1.00 56.70  ? 142 ILE C H      1 
ATOM   9860  H  HA     . ILE D 1 143 ? 14.313  9.944   50.637  1.00 55.61  ? 142 ILE C HA     1 
ATOM   9861  H  HB     . ILE D 1 143 ? 14.302  11.121  48.053  1.00 61.23  ? 142 ILE C HB     1 
ATOM   9862  H  HG12   . ILE D 1 143 ? 12.018  10.286  47.938  1.00 62.71  ? 142 ILE C HG12   1 
ATOM   9863  H  HG13   . ILE D 1 143 ? 12.083  10.248  49.525  1.00 62.71  ? 142 ILE C HG13   1 
ATOM   9864  H  HG21   . ILE D 1 143 ? 13.721  8.887   47.337  1.00 60.49  ? 142 ILE C HG21   1 
ATOM   9865  H  HG22   . ILE D 1 143 ? 15.211  9.032   47.870  1.00 60.49  ? 142 ILE C HG22   1 
ATOM   9866  H  HG23   . ILE D 1 143 ? 14.091  8.402   48.804  1.00 60.49  ? 142 ILE C HG23   1 
ATOM   9867  H  HD11   . ILE D 1 143 ? 11.353  12.326  48.082  1.00 62.93  ? 142 ILE C HD11   1 
ATOM   9868  H  HD12   . ILE D 1 143 ? 11.623  12.347  49.647  1.00 62.93  ? 142 ILE C HD12   1 
ATOM   9869  H  HD13   . ILE D 1 143 ? 12.791  12.712  48.635  1.00 62.93  ? 142 ILE C HD13   1 
ATOM   9870  N  N      . GLU D 1 144 ? 16.724  9.487   50.457  1.00 52.57  ? 143 GLU C N      1 
ATOM   9871  C  CA     . GLU D 1 144 ? 18.124  9.163   50.183  1.00 49.91  ? 143 GLU C CA     1 
ATOM   9872  C  C      . GLU D 1 144 ? 18.202  8.345   48.898  1.00 49.07  ? 143 GLU C C      1 
ATOM   9873  O  O      . GLU D 1 144 ? 17.397  7.432   48.684  1.00 48.33  ? 143 GLU C O      1 
ATOM   9874  C  CB     . GLU D 1 144 ? 18.751  8.373   51.338  1.00 52.58  ? 143 GLU C CB     1 
ATOM   9875  C  CG     . GLU D 1 144 ? 19.537  9.233   52.321  1.00 54.88  ? 143 GLU C CG     1 
ATOM   9876  C  CD     . GLU D 1 144 ? 19.746  8.562   53.673  1.00 57.69  ? 143 GLU C CD     1 
ATOM   9877  O  OE1    . GLU D 1 144 ? 19.178  7.463   53.917  1.00 62.64  ? 143 GLU C OE1    1 
ATOM   9878  O  OE2    . GLU D 1 144 ? 20.472  9.148   54.509  1.00 59.48  ? 143 GLU C OE2    1 
ATOM   9879  H  H      . GLU D 1 144 ? 16.337  8.946   51.001  1.00 63.12  ? 143 GLU C H      1 
ATOM   9880  H  HA     . GLU D 1 144 ? 18.635  9.981   50.084  1.00 59.92  ? 143 GLU C HA     1 
ATOM   9881  H  HB2    . GLU D 1 144 ? 18.043  7.931   51.833  1.00 63.13  ? 143 GLU C HB2    1 
ATOM   9882  H  HB3    . GLU D 1 144 ? 19.360  7.714   50.970  1.00 63.13  ? 143 GLU C HB3    1 
ATOM   9883  H  HG2    . GLU D 1 144 ? 20.411  9.421   51.945  1.00 65.89  ? 143 GLU C HG2    1 
ATOM   9884  H  HG3    . GLU D 1 144 ? 19.054  10.061  52.471  1.00 65.89  ? 143 GLU C HG3    1 
ATOM   9885  N  N      . THR D 1 145 ? 19.171  8.684   48.031  1.00 41.67  ? 144 THR C N      1 
ATOM   9886  C  CA     . THR D 1 145 ? 19.321  7.993   46.763  1.00 46.71  ? 144 THR C CA     1 
ATOM   9887  C  C      . THR D 1 145 ? 20.739  7.477   46.547  1.00 44.42  ? 144 THR C C      1 
ATOM   9888  O  O      . THR D 1 145 ? 21.678  7.850   47.231  1.00 44.78  ? 144 THR C O      1 
ATOM   9889  C  CB     . THR D 1 145 ? 18.961  8.917   45.591  1.00 45.97  ? 144 THR C CB     1 
ATOM   9890  O  OG1    . THR D 1 145 ? 19.868  10.013  45.588  1.00 40.77  ? 144 THR C OG1    1 
ATOM   9891  C  CG2    . THR D 1 145 ? 17.536  9.436   45.726  1.00 47.89  ? 144 THR C CG2    1 
ATOM   9892  H  H      . THR D 1 145 ? 19.745  9.310   48.165  1.00 50.03  ? 144 THR C H      1 
ATOM   9893  H  HA     . THR D 1 145 ? 18.734  7.221   46.792  1.00 56.09  ? 144 THR C HA     1 
ATOM   9894  H  HB     . THR D 1 145 ? 19.018  8.430   44.754  1.00 55.19  ? 144 THR C HB     1 
ATOM   9895  H  HG1    . THR D 1 145 ? 20.650  9.739   45.454  1.00 48.95  ? 144 THR C HG1    1 
ATOM   9896  H  HG21   . THR D 1 145 ? 17.340  10.056  45.006  1.00 57.51  ? 144 THR C HG21   1 
ATOM   9897  H  HG22   . THR D 1 145 ? 16.909  8.698   45.686  1.00 57.51  ? 144 THR C HG22   1 
ATOM   9898  H  HG23   . THR D 1 145 ? 17.429  9.895   46.574  1.00 57.51  ? 144 THR C HG23   1 
ATOM   9899  N  N      . SER D 1 146 ? 20.891  6.611   45.553  1.00 47.17  ? 145 SER C N      1 
ATOM   9900  C  CA     . SER D 1 146 ? 22.206  6.304   45.004  1.00 46.61  ? 145 SER C CA     1 
ATOM   9901  C  C      . SER D 1 146 ? 22.018  6.160   43.511  1.00 46.20  ? 145 SER C C      1 
ATOM   9902  O  O      . SER D 1 146 ? 21.408  5.181   43.063  1.00 46.62  ? 145 SER C O      1 
ATOM   9903  C  CB     . SER D 1 146 ? 22.823  5.029   45.556  1.00 48.37  ? 145 SER C CB     1 
ATOM   9904  O  OG     . SER D 1 146 ? 23.928  4.661   44.726  1.00 47.29  ? 145 SER C OG     1 
ATOM   9905  H  H      . SER D 1 146 ? 20.244  6.186   45.177  1.00 56.64  ? 145 SER C H      1 
ATOM   9906  H  HA     . SER D 1 146 ? 22.806  7.032   45.226  1.00 55.96  ? 145 SER C HA     1 
ATOM   9907  H  HB2    . SER D 1 146 ? 23.135  5.184   46.461  1.00 58.08  ? 145 SER C HB2    1 
ATOM   9908  H  HB3    . SER D 1 146 ? 22.162  4.319   45.549  1.00 58.08  ? 145 SER C HB3    1 
ATOM   9909  H  HG     . SER D 1 146 ? 24.491  5.284   44.705  1.00 56.78  ? 145 SER C HG     1 
ATOM   9910  N  N      . ALA D 1 147 ? 22.511  7.131   42.744  1.00 41.67  ? 146 ALA C N      1 
ATOM   9911  C  CA     . ALA D 1 147 ? 22.564  6.924   41.310  1.00 38.35  ? 146 ALA C CA     1 
ATOM   9912  C  C      . ALA D 1 147 ? 23.451  5.732   40.948  1.00 45.01  ? 146 ALA C C      1 
ATOM   9913  O  O      . ALA D 1 147 ? 23.200  5.054   39.937  1.00 45.59  ? 146 ALA C O      1 
ATOM   9914  C  CB     . ALA D 1 147 ? 23.058  8.192   40.628  1.00 38.73  ? 146 ALA C CB     1 
ATOM   9915  H  H      . ALA D 1 147 ? 22.807  7.889   43.023  1.00 50.03  ? 146 ALA C H      1 
ATOM   9916  H  HA     . ALA D 1 147 ? 21.672  6.734   40.980  1.00 46.06  ? 146 ALA C HA     1 
ATOM   9917  H  HB1    . ALA D 1 147 ? 23.060  8.054   39.668  1.00 46.51  ? 146 ALA C HB1    1 
ATOM   9918  H  HB2    . ALA D 1 147 ? 22.465  8.925   40.856  1.00 46.51  ? 146 ALA C HB2    1 
ATOM   9919  H  HB3    . ALA D 1 147 ? 23.957  8.386   40.936  1.00 46.51  ? 146 ALA C HB3    1 
ATOM   9920  N  N      . LYS D 1 148 ? 24.487  5.455   41.752  1.00 43.84  ? 147 LYS C N      1 
ATOM   9921  C  CA     . LYS D 1 148 ? 25.394  4.350   41.441  1.00 42.03  ? 147 LYS C CA     1 
ATOM   9922  C  C      . LYS D 1 148 ? 24.649  3.023   41.441  1.00 46.44  ? 147 LYS C C      1 
ATOM   9923  O  O      . LYS D 1 148 ? 24.693  2.274   40.457  1.00 44.45  ? 147 LYS C O      1 
ATOM   9924  C  CB     . LYS D 1 148 ? 26.562  4.326   42.430  1.00 46.28  ? 147 LYS C CB     1 
ATOM   9925  C  CG     . LYS D 1 148 ? 27.716  3.374   42.060  1.00 43.14  ? 147 LYS C CG     1 
ATOM   9926  C  CD     . LYS D 1 148 ? 28.782  3.388   43.143  1.00 51.27  ? 147 LYS C CD     1 
ATOM   9927  C  CE     . LYS D 1 148 ? 29.751  2.184   43.081  1.00 51.00  ? 147 LYS C CE     1 
ATOM   9928  N  NZ     . LYS D 1 148 ? 31.204  2.579   43.220  1.00 50.53  ? 147 LYS C NZ     1 
ATOM   9929  H  H      . LYS D 1 148 ? 24.681  5.886   42.470  1.00 52.65  ? 147 LYS C H      1 
ATOM   9930  H  HA     . LYS D 1 148 ? 25.765  4.488   40.555  1.00 50.47  ? 147 LYS C HA     1 
ATOM   9931  H  HB2    . LYS D 1 148 ? 26.931  5.221   42.489  1.00 55.57  ? 147 LYS C HB2    1 
ATOM   9932  H  HB3    . LYS D 1 148 ? 26.224  4.049   43.296  1.00 55.57  ? 147 LYS C HB3    1 
ATOM   9933  H  HG2    . LYS D 1 148 ? 27.377  2.470   41.972  1.00 51.80  ? 147 LYS C HG2    1 
ATOM   9934  H  HG3    . LYS D 1 148 ? 28.119  3.660   41.226  1.00 51.80  ? 147 LYS C HG3    1 
ATOM   9935  H  HD2    . LYS D 1 148 ? 29.310  4.197   43.051  1.00 61.56  ? 147 LYS C HD2    1 
ATOM   9936  H  HD3    . LYS D 1 148 ? 28.348  3.373   44.010  1.00 61.56  ? 147 LYS C HD3    1 
ATOM   9937  H  HE2    . LYS D 1 148 ? 29.538  1.572   43.802  1.00 61.23  ? 147 LYS C HE2    1 
ATOM   9938  H  HE3    . LYS D 1 148 ? 29.644  1.739   42.225  1.00 61.23  ? 147 LYS C HE3    1 
ATOM   9939  H  HZ1    . LYS D 1 148 ? 31.721  1.856   43.174  1.00 60.67  ? 147 LYS C HZ1    1 
ATOM   9940  H  HZ2    . LYS D 1 148 ? 31.431  3.138   42.566  1.00 60.67  ? 147 LYS C HZ2    1 
ATOM   9941  H  HZ3    . LYS D 1 148 ? 31.337  2.980   44.003  1.00 60.67  ? 147 LYS C HZ3    1 
ATOM   9942  N  N      . THR D 1 149 ? 23.920  2.733   42.521  1.00 42.36  ? 148 THR C N      1 
ATOM   9943  C  CA     . THR D 1 149 ? 23.125  1.511   42.613  1.00 48.09  ? 148 THR C CA     1 
ATOM   9944  C  C      . THR D 1 149 ? 21.699  1.660   42.077  1.00 49.21  ? 148 THR C C      1 
ATOM   9945  O  O      . THR D 1 149 ? 20.966  0.654   42.041  1.00 48.69  ? 148 THR C O      1 
ATOM   9946  C  CB     . THR D 1 149 ? 23.032  1.047   44.073  1.00 48.84  ? 148 THR C CB     1 
ATOM   9947  O  OG1    . THR D 1 149 ? 22.227  1.989   44.803  1.00 49.99  ? 148 THR C OG1    1 
ATOM   9948  C  CG2    . THR D 1 149 ? 24.442  0.940   44.706  1.00 44.45  ? 148 THR C CG2    1 
ATOM   9949  H  H      . THR D 1 149 ? 23.870  3.234   43.219  1.00 50.86  ? 148 THR C H      1 
ATOM   9950  H  HA     . THR D 1 149 ? 23.576  0.830   42.090  1.00 57.75  ? 148 THR C HA     1 
ATOM   9951  H  HB     . THR D 1 149 ? 22.627  0.167   44.121  1.00 58.64  ? 148 THR C HB     1 
ATOM   9952  H  HG1    . THR D 1 149 ? 22.195  1.772   45.614  1.00 60.02  ? 148 THR C HG1    1 
ATOM   9953  H  HG21   . THR D 1 149 ? 24.378  0.554   45.594  1.00 53.37  ? 148 THR C HG21   1 
ATOM   9954  H  HG22   . THR D 1 149 ? 25.010  0.376   44.158  1.00 53.37  ? 148 THR C HG22   1 
ATOM   9955  H  HG23   . THR D 1 149 ? 24.843  1.821   44.774  1.00 53.37  ? 148 THR C HG23   1 
ATOM   9956  N  N      . ARG D 1 150 ? 21.279  2.883   41.715  1.00 47.17  ? 149 ARG C N      1 
ATOM   9957  C  CA     . ARG D 1 150 ? 19.916  3.214   41.277  1.00 47.92  ? 149 ARG C CA     1 
ATOM   9958  C  C      . ARG D 1 150 ? 18.896  3.207   42.431  1.00 52.54  ? 149 ARG C C      1 
ATOM   9959  O  O      . ARG D 1 150 ? 17.695  3.108   42.188  1.00 47.30  ? 149 ARG C O      1 
ATOM   9960  C  CB     . ARG D 1 150 ? 19.474  2.263   40.146  1.00 47.04  ? 149 ARG C CB     1 
ATOM   9961  C  CG     . ARG D 1 150 ? 18.062  2.473   39.532  1.00 55.27  ? 149 ARG C CG     1 
ATOM   9962  C  CD     . ARG D 1 150 ? 17.644  3.938   39.435  1.00 53.22  ? 149 ARG C CD     1 
ATOM   9963  N  NE     . ARG D 1 150 ? 16.512  4.222   38.544  1.00 51.18  ? 149 ARG C NE     1 
ATOM   9964  C  CZ     . ARG D 1 150 ? 16.461  3.968   37.239  1.00 51.43  ? 149 ARG C CZ     1 
ATOM   9965  N  NH1    . ARG D 1 150 ? 17.437  3.326   36.615  1.00 50.77  ? 149 ARG C NH1    1 
ATOM   9966  N  NH2    . ARG D 1 150 ? 15.410  4.390   36.537  1.00 48.99  ? 149 ARG C NH2    1 
ATOM   9967  H  H      . ARG D 1 150 ? 21.795  3.571   41.716  1.00 56.63  ? 149 ARG C H      1 
ATOM   9968  H  HA     . ARG D 1 150 ? 19.914  4.119   40.928  1.00 57.54  ? 149 ARG C HA     1 
ATOM   9969  H  HB2    . ARG D 1 150 ? 20.110  2.353   39.419  1.00 56.48  ? 149 ARG C HB2    1 
ATOM   9970  H  HB3    . ARG D 1 150 ? 19.494  1.358   40.495  1.00 56.48  ? 149 ARG C HB3    1 
ATOM   9971  H  HG2    . ARG D 1 150 ? 18.053  2.103   38.635  1.00 66.35  ? 149 ARG C HG2    1 
ATOM   9972  H  HG3    . ARG D 1 150 ? 17.410  2.016   40.086  1.00 66.35  ? 149 ARG C HG3    1 
ATOM   9973  H  HD2    . ARG D 1 150 ? 17.395  4.243   40.321  1.00 63.90  ? 149 ARG C HD2    1 
ATOM   9974  H  HD3    . ARG D 1 150 ? 18.400  4.450   39.109  1.00 63.90  ? 149 ARG C HD3    1 
ATOM   9975  H  HE     . ARG D 1 150 ? 15.818  4.586   38.899  1.00 61.45  ? 149 ARG C HE     1 
ATOM   9976  H  HH11   . ARG D 1 150 ? 18.128  3.062   37.054  1.00 60.95  ? 149 ARG C HH11   1 
ATOM   9977  H  HH12   . ARG D 1 150 ? 17.381  3.173   35.771  1.00 60.95  ? 149 ARG C HH12   1 
ATOM   9978  H  HH21   . ARG D 1 150 ? 14.777  4.820   36.928  1.00 58.82  ? 149 ARG C HH21   1 
ATOM   9979  H  HH22   . ARG D 1 150 ? 15.365  4.231   35.693  1.00 58.82  ? 149 ARG C HH22   1 
ATOM   9980  N  N      . GLN D 1 151 ? 19.324  3.351   43.685  1.00 50.68  ? 150 GLN C N      1 
ATOM   9981  C  CA     . GLN D 1 151 ? 18.381  3.408   44.804  1.00 52.56  ? 150 GLN C CA     1 
ATOM   9982  C  C      . GLN D 1 151 ? 17.702  4.774   44.921  1.00 47.86  ? 150 GLN C C      1 
ATOM   9983  O  O      . GLN D 1 151 ? 18.373  5.805   44.940  1.00 48.59  ? 150 GLN C O      1 
ATOM   9984  C  CB     . GLN D 1 151 ? 19.094  3.095   46.123  1.00 51.55  ? 150 GLN C CB     1 
ATOM   9985  C  CG     . GLN D 1 151 ? 18.215  3.285   47.376  1.00 51.83  ? 150 GLN C CG     1 
ATOM   9986  C  CD     . GLN D 1 151 ? 18.899  2.832   48.660  1.00 60.20  ? 150 GLN C CD     1 
ATOM   9987  O  OE1    . GLN D 1 151 ? 19.366  1.696   48.759  1.00 64.82  ? 150 GLN C OE1    1 
ATOM   9988  N  NE2    . GLN D 1 151 ? 18.936  3.715   49.665  1.00 60.25  ? 150 GLN C NE2    1 
ATOM   9989  H  H      . GLN D 1 151 ? 20.151  3.417   43.914  1.00 60.85  ? 150 GLN C H      1 
ATOM   9990  H  HA     . GLN D 1 151 ? 17.692  2.747   44.634  1.00 63.11  ? 150 GLN C HA     1 
ATOM   9991  H  HB2    . GLN D 1 151 ? 19.386  2.170   46.106  1.00 61.90  ? 150 GLN C HB2    1 
ATOM   9992  H  HB3    . GLN D 1 151 ? 19.861  3.683   46.209  1.00 61.90  ? 150 GLN C HB3    1 
ATOM   9993  H  HG2    . GLN D 1 151 ? 17.999  4.226   47.470  1.00 62.24  ? 150 GLN C HG2    1 
ATOM   9994  H  HG3    . GLN D 1 151 ? 17.402  2.766   47.272  1.00 62.24  ? 150 GLN C HG3    1 
ATOM   9995  H  HE21   . GLN D 1 151 ? 18.584  4.493   49.566  1.00 72.33  ? 150 GLN C HE21   1 
ATOM   9996  H  HE22   . GLN D 1 151 ? 19.311  3.504   50.409  1.00 72.33  ? 150 GLN C HE22   1 
ATOM   9997  N  N      . GLY D 1 152 ? 16.365  4.774   45.035  1.00 50.69  ? 151 GLY C N      1 
ATOM   9998  C  CA     . GLY D 1 152 ? 15.595  5.981   45.308  1.00 49.99  ? 151 GLY C CA     1 
ATOM   9999  C  C      . GLY D 1 152 ? 15.306  6.873   44.101  1.00 43.89  ? 151 GLY C C      1 
ATOM   10000 O  O      . GLY D 1 152 ? 14.542  7.844   44.220  1.00 39.82  ? 151 GLY C O      1 
ATOM   10001 H  H      . GLY D 1 152 ? 15.878  4.070   44.956  1.00 60.86  ? 151 GLY C H      1 
ATOM   10002 H  HA2    . GLY D 1 152 ? 14.742  5.720   45.689  1.00 60.03  ? 151 GLY C HA2    1 
ATOM   10003 H  HA3    . GLY D 1 152 ? 16.081  6.515   45.956  1.00 60.03  ? 151 GLY C HA3    1 
ATOM   10004 N  N      . VAL D 1 153 ? 15.889  6.598   42.947  1.00 45.42  ? 152 VAL C N      1 
ATOM   10005 C  CA     . VAL D 1 153 ? 15.787  7.562   41.848  1.00 43.23  ? 152 VAL C CA     1 
ATOM   10006 C  C      . VAL D 1 153 ? 14.322  7.853   41.515  1.00 43.08  ? 152 VAL C C      1 
ATOM   10007 O  O      . VAL D 1 153 ? 13.850  8.992   41.641  1.00 46.20  ? 152 VAL C O      1 
ATOM   10008 C  CB     . VAL D 1 153 ? 16.554  7.050   40.616  1.00 46.81  ? 152 VAL C CB     1 
ATOM   10009 C  CG1    . VAL D 1 153 ? 16.284  7.936   39.420  1.00 42.68  ? 152 VAL C CG1    1 
ATOM   10010 C  CG2    . VAL D 1 153 ? 18.059  6.995   40.942  1.00 49.68  ? 152 VAL C CG2    1 
ATOM   10011 H  H      . VAL D 1 153 ? 16.338  5.886   42.773  1.00 54.54  ? 152 VAL C H      1 
ATOM   10012 H  HA     . VAL D 1 153 ? 16.191  8.397   42.133  1.00 51.91  ? 152 VAL C HA     1 
ATOM   10013 H  HB     . VAL D 1 153 ? 16.255  6.156   40.387  1.00 56.20  ? 152 VAL C HB     1 
ATOM   10014 H  HG11   . VAL D 1 153 ? 16.965  7.775   38.748  1.00 51.25  ? 152 VAL C HG11   1 
ATOM   10015 H  HG12   . VAL D 1 153 ? 15.408  7.725   39.062  1.00 51.25  ? 152 VAL C HG12   1 
ATOM   10016 H  HG13   . VAL D 1 153 ? 16.311  8.864   39.703  1.00 51.25  ? 152 VAL C HG13   1 
ATOM   10017 H  HG21   . VAL D 1 153 ? 18.542  6.693   40.157  1.00 59.64  ? 152 VAL C HG21   1 
ATOM   10018 H  HG22   . VAL D 1 153 ? 18.360  7.882   41.194  1.00 59.64  ? 152 VAL C HG22   1 
ATOM   10019 H  HG23   . VAL D 1 153 ? 18.201  6.377   41.676  1.00 59.64  ? 152 VAL C HG23   1 
ATOM   10020 N  N      . ASP D 1 154 ? 13.571  6.817   41.127  1.00 44.19  ? 153 ASP C N      1 
ATOM   10021 C  CA     . ASP D 1 154 ? 12.201  7.039   40.655  1.00 44.43  ? 153 ASP C CA     1 
ATOM   10022 C  C      . ASP D 1 154 ? 11.347  7.703   41.728  1.00 44.48  ? 153 ASP C C      1 
ATOM   10023 O  O      . ASP D 1 154 ? 10.554  8.612   41.441  1.00 39.37  ? 153 ASP C O      1 
ATOM   10024 C  CB     . ASP D 1 154 ? 11.555  5.720   40.231  1.00 40.88  ? 153 ASP C CB     1 
ATOM   10025 C  CG     . ASP D 1 154 ? 12.154  5.151   38.965  1.00 44.87  ? 153 ASP C CG     1 
ATOM   10026 O  OD1    . ASP D 1 154 ? 12.434  5.933   38.035  1.00 44.85  ? 153 ASP C OD1    1 
ATOM   10027 O  OD2    . ASP D 1 154 ? 12.329  3.912   38.894  1.00 46.01  ? 153 ASP C OD2    1 
ATOM   10028 H  H      . ASP D 1 154 ? 13.824  5.995   41.127  1.00 53.06  ? 153 ASP C H      1 
ATOM   10029 H  HA     . ASP D 1 154 ? 12.242  7.622   39.880  1.00 53.35  ? 153 ASP C HA     1 
ATOM   10030 H  HB2    . ASP D 1 154 ? 11.676  5.068   40.939  1.00 49.09  ? 153 ASP C HB2    1 
ATOM   10031 H  HB3    . ASP D 1 154 ? 10.610  5.868   40.074  1.00 49.09  ? 153 ASP C HB3    1 
ATOM   10032 N  N      . ASP D 1 155 ? 11.491  7.252   42.974  1.00 44.90  ? 154 ASP C N      1 
ATOM   10033 C  CA     . ASP D 1 155 ? 10.700  7.804   44.068  1.00 47.25  ? 154 ASP C CA     1 
ATOM   10034 C  C      . ASP D 1 155 ? 10.874  9.308   44.165  1.00 45.51  ? 154 ASP C C      1 
ATOM   10035 O  O      . ASP D 1 155 ? 9.892   10.063  44.217  1.00 43.36  ? 154 ASP C O      1 
ATOM   10036 C  CB     . ASP D 1 155 ? 11.103  7.119   45.377  1.00 46.97  ? 154 ASP C CB     1 
ATOM   10037 C  CG     . ASP D 1 155 ? 10.116  7.386   46.512  1.00 52.81  ? 154 ASP C CG     1 
ATOM   10038 O  OD1    . ASP D 1 155 ? 8.983   7.836   46.214  1.00 54.94  ? 154 ASP C OD1    1 
ATOM   10039 O  OD2    . ASP D 1 155 ? 10.476  7.143   47.695  1.00 51.90  ? 154 ASP C OD2    1 
ATOM   10040 H  H      . ASP D 1 155 ? 12.037  6.630   43.210  1.00 53.91  ? 154 ASP C H      1 
ATOM   10041 H  HA     . ASP D 1 155 ? 9.760   7.628   43.905  1.00 56.74  ? 154 ASP C HA     1 
ATOM   10042 H  HB2    . ASP D 1 155 ? 11.142  6.161   45.233  1.00 56.40  ? 154 ASP C HB2    1 
ATOM   10043 H  HB3    . ASP D 1 155 ? 11.972  7.450   45.652  1.00 56.40  ? 154 ASP C HB3    1 
ATOM   10044 N  N      . ALA D 1 156 ? 12.134  9.769   44.168  1.00 45.03  ? 155 ALA C N      1 
ATOM   10045 C  CA     . ALA D 1 156 ? 12.413  11.196  44.203  1.00 41.44  ? 155 ALA C CA     1 
ATOM   10046 C  C      . ALA D 1 156 ? 11.559  11.979  43.202  1.00 42.03  ? 155 ALA C C      1 
ATOM   10047 O  O      . ALA D 1 156 ? 10.862  12.935  43.565  1.00 39.70  ? 155 ALA C O      1 
ATOM   10048 C  CB     . ALA D 1 156 ? 13.909  11.408  43.920  1.00 42.99  ? 155 ALA C CB     1 
ATOM   10049 H  H      . ALA D 1 156 ? 12.836  9.272   44.150  1.00 54.07  ? 155 ALA C H      1 
ATOM   10050 H  HA     . ALA D 1 156 ? 12.198  11.535  45.086  1.00 49.76  ? 155 ALA C HA     1 
ATOM   10051 H  HB1    . ALA D 1 156 ? 14.126  12.344  44.057  1.00 51.62  ? 155 ALA C HB1    1 
ATOM   10052 H  HB2    . ALA D 1 156 ? 14.427  10.856  44.526  1.00 51.62  ? 155 ALA C HB2    1 
ATOM   10053 H  HB3    . ALA D 1 156 ? 14.095  11.157  43.001  1.00 51.62  ? 155 ALA C HB3    1 
ATOM   10054 N  N      . PHE D 1 157 ? 11.616  11.601  41.923  1.00 44.71  ? 156 PHE C N      1 
ATOM   10055 C  CA     . PHE D 1 157 ? 10.963  12.405  40.890  1.00 41.71  ? 156 PHE C CA     1 
ATOM   10056 C  C      . PHE D 1 157 ? 9.448   12.239  40.880  1.00 42.41  ? 156 PHE C C      1 
ATOM   10057 O  O      . PHE D 1 157 ? 8.717   13.197  40.583  1.00 34.87  ? 156 PHE C O      1 
ATOM   10058 C  CB     . PHE D 1 157 ? 11.486  12.028  39.501  1.00 38.29  ? 156 PHE C CB     1 
ATOM   10059 C  CG     . PHE D 1 157 ? 12.818  12.637  39.155  1.00 38.56  ? 156 PHE C CG     1 
ATOM   10060 C  CD1    . PHE D 1 157 ? 12.891  13.889  38.562  1.00 39.94  ? 156 PHE C CD1    1 
ATOM   10061 C  CD2    . PHE D 1 157 ? 13.988  11.928  39.373  1.00 38.22  ? 156 PHE C CD2    1 
ATOM   10062 C  CE1    . PHE D 1 157 ? 14.121  14.437  38.219  1.00 34.86  ? 156 PHE C CE1    1 
ATOM   10063 C  CE2    . PHE D 1 157 ? 15.208  12.466  39.029  1.00 40.02  ? 156 PHE C CE2    1 
ATOM   10064 C  CZ     . PHE D 1 157 ? 15.269  13.718  38.461  1.00 30.93  ? 156 PHE C CZ     1 
ATOM   10065 H  H      . PHE D 1 157 ? 12.018  10.898  41.634  1.00 53.69  ? 156 PHE C H      1 
ATOM   10066 H  HA     . PHE D 1 157 ? 11.179  13.331  41.082  1.00 50.09  ? 156 PHE C HA     1 
ATOM   10067 H  HB2    . PHE D 1 157 ? 11.584  11.064  39.457  1.00 45.98  ? 156 PHE C HB2    1 
ATOM   10068 H  HB3    . PHE D 1 157 ? 10.845  12.327  38.837  1.00 45.98  ? 156 PHE C HB3    1 
ATOM   10069 H  HD1    . PHE D 1 157 ? 12.111  14.365  38.393  1.00 47.96  ? 156 PHE C HD1    1 
ATOM   10070 H  HD2    . PHE D 1 157 ? 13.949  11.081  39.756  1.00 45.89  ? 156 PHE C HD2    1 
ATOM   10071 H  HE1    . PHE D 1 157 ? 14.168  15.280  37.830  1.00 41.87  ? 156 PHE C HE1    1 
ATOM   10072 H  HE2    . PHE D 1 157 ? 15.989  11.984  39.181  1.00 48.05  ? 156 PHE C HE2    1 
ATOM   10073 H  HZ     . PHE D 1 157 ? 16.096  14.082  38.239  1.00 37.15  ? 156 PHE C HZ     1 
ATOM   10074 N  N      . TYR D 1 158 ? 8.975   11.010  41.109  1.00 40.55  ? 157 TYR C N      1 
ATOM   10075 C  CA     . TYR D 1 158 ? 7.540   10.782  41.176  1.00 43.07  ? 157 TYR C CA     1 
ATOM   10076 C  C      . TYR D 1 158 ? 6.967   11.466  42.397  1.00 43.25  ? 157 TYR C C      1 
ATOM   10077 O  O      . TYR D 1 158 ? 5.987   12.226  42.310  1.00 40.93  ? 157 TYR C O      1 
ATOM   10078 C  CB     . TYR D 1 158 ? 7.249   9.288   41.238  1.00 42.78  ? 157 TYR C CB     1 
ATOM   10079 C  CG     . TYR D 1 158 ? 7.556   8.550   39.972  1.00 39.78  ? 157 TYR C CG     1 
ATOM   10080 C  CD1    . TYR D 1 158 ? 8.126   9.194   38.868  1.00 39.83  ? 157 TYR C CD1    1 
ATOM   10081 C  CD2    . TYR D 1 158 ? 7.254   7.198   39.868  1.00 41.76  ? 157 TYR C CD2    1 
ATOM   10082 C  CE1    . TYR D 1 158 ? 8.397   8.495   37.696  1.00 39.80  ? 157 TYR C CE1    1 
ATOM   10083 C  CE2    . TYR D 1 158 ? 7.514   6.495   38.705  1.00 41.92  ? 157 TYR C CE2    1 
ATOM   10084 C  CZ     . TYR D 1 158 ? 8.089   7.136   37.632  1.00 42.52  ? 157 TYR C CZ     1 
ATOM   10085 O  OH     . TYR D 1 158 ? 8.326   6.379   36.506  1.00 43.72  ? 157 TYR C OH     1 
ATOM   10086 H  H      . TYR D 1 158 ? 9.459   10.308  41.225  1.00 48.70  ? 157 TYR C H      1 
ATOM   10087 H  HA     . TYR D 1 158 ? 7.121   11.140  40.378  1.00 51.72  ? 157 TYR C HA     1 
ATOM   10088 H  HB2    . TYR D 1 158 ? 7.785   8.896   41.944  1.00 51.37  ? 157 TYR C HB2    1 
ATOM   10089 H  HB3    . TYR D 1 158 ? 6.306   9.163   41.429  1.00 51.37  ? 157 TYR C HB3    1 
ATOM   10090 H  HD1    . TYR D 1 158 ? 8.325   10.101  38.917  1.00 47.83  ? 157 TYR C HD1    1 
ATOM   10091 H  HD2    . TYR D 1 158 ? 6.871   6.758   40.593  1.00 50.15  ? 157 TYR C HD2    1 
ATOM   10092 H  HE1    . TYR D 1 158 ? 8.779   8.927   36.967  1.00 47.79  ? 157 TYR C HE1    1 
ATOM   10093 H  HE2    . TYR D 1 158 ? 7.300   5.592   38.648  1.00 50.34  ? 157 TYR C HE2    1 
ATOM   10094 H  HH     . TYR D 1 158 ? 8.055   5.593   36.626  1.00 52.50  ? 157 TYR C HH     1 
ATOM   10095 N  N      . THR D 1 159 ? 7.601   11.228  43.547  1.00 42.47  ? 158 THR C N      1 
ATOM   10096 C  CA     . THR D 1 159 ? 7.232   11.970  44.732  1.00 47.99  ? 158 THR C CA     1 
ATOM   10097 C  C      . THR D 1 159 ? 7.158   13.437  44.368  1.00 43.09  ? 158 THR C C      1 
ATOM   10098 O  O      . THR D 1 159 ? 6.255   14.149  44.806  1.00 44.82  ? 158 THR C O      1 
ATOM   10099 C  CB     . THR D 1 159 ? 8.220   11.681  45.857  1.00 46.97  ? 158 THR C CB     1 
ATOM   10100 O  OG1    . THR D 1 159 ? 8.107   10.292  46.244  1.00 45.89  ? 158 THR C OG1    1 
ATOM   10101 C  CG2    . THR D 1 159 ? 7.956   12.576  47.070  1.00 45.33  ? 158 THR C CG2    1 
ATOM   10102 H  H      . THR D 1 159 ? 8.232   10.654  43.657  1.00 50.99  ? 158 THR C H      1 
ATOM   10103 H  HA     . THR D 1 159 ? 6.367   11.696  45.076  1.00 57.62  ? 158 THR C HA     1 
ATOM   10104 H  HB     . THR D 1 159 ? 9.122   11.863  45.549  1.00 56.39  ? 158 THR C HB     1 
ATOM   10105 H  HG1    . THR D 1 159 ? 8.307   9.796   45.596  1.00 55.10  ? 158 THR C HG1    1 
ATOM   10106 H  HG21   . THR D 1 159 ? 8.472   12.266  47.830  1.00 54.43  ? 158 THR C HG21   1 
ATOM   10107 H  HG22   . THR D 1 159 ? 8.210   13.491  46.869  1.00 54.43  ? 158 THR C HG22   1 
ATOM   10108 H  HG23   . THR D 1 159 ? 7.014   12.555  47.299  1.00 54.43  ? 158 THR C HG23   1 
ATOM   10109 N  N      . LEU D 1 160 ? 8.054   13.895  43.479  1.00 45.97  ? 159 LEU C N      1 
ATOM   10110 C  CA     . LEU D 1 160 ? 8.024   15.305  43.124  1.00 44.41  ? 159 LEU C CA     1 
ATOM   10111 C  C      . LEU D 1 160 ? 6.818   15.616  42.247  1.00 37.67  ? 159 LEU C C      1 
ATOM   10112 O  O      . LEU D 1 160 ? 6.143   16.623  42.465  1.00 43.87  ? 159 LEU C O      1 
ATOM   10113 C  CB     . LEU D 1 160 ? 9.333   15.721  42.456  1.00 45.50  ? 159 LEU C CB     1 
ATOM   10114 C  CG     . LEU D 1 160 ? 9.469   17.212  42.156  1.00 43.40  ? 159 LEU C CG     1 
ATOM   10115 C  CD1    . LEU D 1 160 ? 9.155   18.091  43.352  1.00 45.77  ? 159 LEU C CD1    1 
ATOM   10116 C  CD2    . LEU D 1 160 ? 10.901  17.529  41.696  1.00 42.63  ? 159 LEU C CD2    1 
ATOM   10117 H  H      . LEU D 1 160 ? 8.659   13.425  43.089  1.00 55.20  ? 159 LEU C H      1 
ATOM   10118 H  HA     . LEU D 1 160 ? 7.945   15.833  43.934  1.00 53.33  ? 159 LEU C HA     1 
ATOM   10119 H  HB2    . LEU D 1 160 ? 10.066  15.475  43.042  1.00 54.63  ? 159 LEU C HB2    1 
ATOM   10120 H  HB3    . LEU D 1 160 ? 9.409   15.247  41.613  1.00 54.63  ? 159 LEU C HB3    1 
ATOM   10121 H  HG     . LEU D 1 160 ? 8.825   17.415  41.459  1.00 52.12  ? 159 LEU C HG     1 
ATOM   10122 H  HD11   . LEU D 1 160 ? 9.230   19.021  43.088  1.00 54.95  ? 159 LEU C HD11   1 
ATOM   10123 H  HD12   . LEU D 1 160 ? 8.252   17.904  43.653  1.00 54.95  ? 159 LEU C HD12   1 
ATOM   10124 H  HD13   . LEU D 1 160 ? 9.788   17.896  44.061  1.00 54.95  ? 159 LEU C HD13   1 
ATOM   10125 H  HD21   . LEU D 1 160 ? 10.965  18.476  41.494  1.00 51.19  ? 159 LEU C HD21   1 
ATOM   10126 H  HD22   . LEU D 1 160 ? 11.519  17.300  42.407  1.00 51.19  ? 159 LEU C HD22   1 
ATOM   10127 H  HD23   . LEU D 1 160 ? 11.100  17.007  40.903  1.00 51.19  ? 159 LEU C HD23   1 
ATOM   10128 N  N      . VAL D 1 161 ? 6.547   14.788  41.226  1.00 45.84  ? 160 VAL C N      1 
ATOM   10129 C  CA     . VAL D 1 161 ? 5.307   14.939  40.463  1.00 40.65  ? 160 VAL C CA     1 
ATOM   10130 C  C      . VAL D 1 161 ? 4.104   14.824  41.395  1.00 45.04  ? 160 VAL C C      1 
ATOM   10131 O  O      . VAL D 1 161 ? 3.112   15.545  41.258  1.00 45.80  ? 160 VAL C O      1 
ATOM   10132 C  CB     . VAL D 1 161 ? 5.220   13.875  39.353  1.00 40.84  ? 160 VAL C CB     1 
ATOM   10133 C  CG1    . VAL D 1 161 ? 3.804   13.787  38.785  1.00 41.10  ? 160 VAL C CG1    1 
ATOM   10134 C  CG2    . VAL D 1 161 ? 6.195   14.208  38.219  1.00 41.03  ? 160 VAL C CG2    1 
ATOM   10135 H  H      . VAL D 1 161 ? 7.056   14.146  40.963  1.00 55.04  ? 160 VAL C H      1 
ATOM   10136 H  HA     . VAL D 1 161 ? 5.313   15.817  40.051  1.00 48.82  ? 160 VAL C HA     1 
ATOM   10137 H  HB     . VAL D 1 161 ? 5.454   13.017  39.741  1.00 49.04  ? 160 VAL C HB     1 
ATOM   10138 H  HG11   . VAL D 1 161 ? 3.791   13.131  38.070  1.00 49.35  ? 160 VAL C HG11   1 
ATOM   10139 H  HG12   . VAL D 1 161 ? 3.197   13.518  39.492  1.00 49.35  ? 160 VAL C HG12   1 
ATOM   10140 H  HG13   . VAL D 1 161 ? 3.548   14.656  38.440  1.00 49.35  ? 160 VAL C HG13   1 
ATOM   10141 H  HG21   . VAL D 1 161 ? 6.134   13.520  37.538  1.00 49.27  ? 160 VAL C HG21   1 
ATOM   10142 H  HG22   . VAL D 1 161 ? 5.957   15.070  37.841  1.00 49.27  ? 160 VAL C HG22   1 
ATOM   10143 H  HG23   . VAL D 1 161 ? 7.096   14.241  38.576  1.00 49.27  ? 160 VAL C HG23   1 
ATOM   10144 N  N      . ARG D 1 162 ? 4.149   13.880  42.321  1.00 43.38  ? 161 ARG C N      1 
ATOM   10145 C  CA     . ARG D 1 162 ? 3.048   13.800  43.285  1.00 50.21  ? 161 ARG C CA     1 
ATOM   10146 C  C      . ARG D 1 162 ? 2.951   15.064  44.130  1.00 51.45  ? 161 ARG C C      1 
ATOM   10147 O  O      . ARG D 1 162 ? 1.843   15.441  44.527  1.00 52.80  ? 161 ARG C O      1 
ATOM   10148 C  CB     . ARG D 1 162 ? 3.213   12.562  44.166  1.00 48.54  ? 161 ARG C CB     1 
ATOM   10149 C  CG     . ARG D 1 162 ? 2.728   11.315  43.467  1.00 43.95  ? 161 ARG C CG     1 
ATOM   10150 C  CD     . ARG D 1 162 ? 2.966   10.097  44.278  1.00 42.28  ? 161 ARG C CD     1 
ATOM   10151 N  NE     . ARG D 1 162 ? 3.038   8.884   43.474  1.00 39.79  ? 161 ARG C NE     1 
ATOM   10152 C  CZ     . ARG D 1 162 ? 4.074   8.050   43.477  1.00 47.86  ? 161 ARG C CZ     1 
ATOM   10153 N  NH1    . ARG D 1 162 ? 5.170   8.302   44.183  1.00 46.87  ? 161 ARG C NH1    1 
ATOM   10154 N  NH2    . ARG D 1 162 ? 4.006   6.930   42.760  1.00 46.37  ? 161 ARG C NH2    1 
ATOM   10155 H  H      . ARG D 1 162 ? 4.774   13.297  42.415  1.00 52.09  ? 161 ARG C H      1 
ATOM   10156 H  HA     . ARG D 1 162 ? 2.211   13.706  42.802  1.00 60.28  ? 161 ARG C HA     1 
ATOM   10157 H  HB2    . ARG D 1 162 ? 4.151   12.446  44.383  1.00 58.28  ? 161 ARG C HB2    1 
ATOM   10158 H  HB3    . ARG D 1 162 ? 2.696   12.677  44.979  1.00 58.28  ? 161 ARG C HB3    1 
ATOM   10159 H  HG2    . ARG D 1 162 ? 1.775   11.390  43.304  1.00 52.78  ? 161 ARG C HG2    1 
ATOM   10160 H  HG3    . ARG D 1 162 ? 3.201   11.216  42.626  1.00 52.78  ? 161 ARG C HG3    1 
ATOM   10161 H  HD2    . ARG D 1 162 ? 3.807   10.192  44.752  1.00 50.77  ? 161 ARG C HD2    1 
ATOM   10162 H  HD3    . ARG D 1 162 ? 2.238   9.993   44.912  1.00 50.77  ? 161 ARG C HD3    1 
ATOM   10163 H  HE     . ARG D 1 162 ? 2.370   8.697   42.965  1.00 47.78  ? 161 ARG C HE     1 
ATOM   10164 H  HH11   . ARG D 1 162 ? 5.224   9.020   44.653  1.00 56.28  ? 161 ARG C HH11   1 
ATOM   10165 H  HH12   . ARG D 1 162 ? 5.827   7.747   44.169  1.00 56.28  ? 161 ARG C HH12   1 
ATOM   10166 H  HH21   . ARG D 1 162 ? 3.299   6.754   42.303  1.00 55.67  ? 161 ARG C HH21   1 
ATOM   10167 H  HH22   . ARG D 1 162 ? 4.669   6.383   42.754  1.00 55.67  ? 161 ARG C HH22   1 
ATOM   10168 N  N      . GLU D 1 163 ? 4.079   15.737  44.407  1.00 46.93  ? 162 GLU C N      1 
ATOM   10169 C  CA     . GLU D 1 163 ? 3.989   16.993  45.155  1.00 49.43  ? 162 GLU C CA     1 
ATOM   10170 C  C      . GLU D 1 163 ? 3.461   18.122  44.267  1.00 51.57  ? 162 GLU C C      1 
ATOM   10171 O  O      . GLU D 1 163 ? 2.819   19.051  44.757  1.00 52.95  ? 162 GLU C O      1 
ATOM   10172 C  CB     . GLU D 1 163 ? 5.347   17.420  45.732  1.00 46.92  ? 162 GLU C CB     1 
ATOM   10173 C  CG     . GLU D 1 163 ? 5.846   16.613  46.926  1.00 48.70  ? 162 GLU C CG     1 
ATOM   10174 C  CD     . GLU D 1 163 ? 5.121   16.968  48.237  1.00 43.26  ? 162 GLU C CD     1 
ATOM   10175 O  OE1    . GLU D 1 163 ? 4.051   16.397  48.465  1.00 52.13  ? 162 GLU C OE1    1 
ATOM   10176 O  OE2    . GLU D 1 163 ? 5.604   17.796  49.036  1.00 44.67  ? 162 GLU C OE2    1 
ATOM   10177 H  H      . GLU D 1 163 ? 4.873   15.496  44.182  1.00 56.35  ? 162 GLU C H      1 
ATOM   10178 H  HA     . GLU D 1 163 ? 3.387   16.841  45.900  1.00 59.36  ? 162 GLU C HA     1 
ATOM   10179 H  HB2    . GLU D 1 163 ? 6.013   17.339  45.031  1.00 56.34  ? 162 GLU C HB2    1 
ATOM   10180 H  HB3    . GLU D 1 163 ? 5.278   18.344  46.018  1.00 56.34  ? 162 GLU C HB3    1 
ATOM   10181 H  HG2    . GLU D 1 163 ? 5.704   15.670  46.751  1.00 58.47  ? 162 GLU C HG2    1 
ATOM   10182 H  HG3    . GLU D 1 163 ? 6.792   16.788  47.050  1.00 58.47  ? 162 GLU C HG3    1 
ATOM   10183 N  N      . ILE D 1 164 ? 3.765   18.088  42.970  1.00 53.95  ? 163 ILE C N      1 
ATOM   10184 C  CA     . ILE D 1 164 ? 3.208   19.087  42.061  1.00 49.22  ? 163 ILE C CA     1 
ATOM   10185 C  C      . ILE D 1 164 ? 1.697   18.936  42.010  1.00 54.45  ? 163 ILE C C      1 
ATOM   10186 O  O      . ILE D 1 164 ? 0.950   19.856  42.365  1.00 55.61  ? 163 ILE C O      1 
ATOM   10187 C  CB     . ILE D 1 164 ? 3.856   18.970  40.669  1.00 46.42  ? 163 ILE C CB     1 
ATOM   10188 C  CG1    . ILE D 1 164 ? 5.373   19.141  40.824  1.00 48.82  ? 163 ILE C CG1    1 
ATOM   10189 C  CG2    . ILE D 1 164 ? 3.281   20.022  39.706  1.00 44.77  ? 163 ILE C CG2    1 
ATOM   10190 C  CD1    . ILE D 1 164 ? 6.163   18.866  39.550  1.00 46.49  ? 163 ILE C CD1    1 
ATOM   10191 H  H      . ILE D 1 164 ? 4.280   17.508  42.599  1.00 64.78  ? 163 ILE C H      1 
ATOM   10192 H  HA     . ILE D 1 164 ? 3.408   19.976  42.395  1.00 59.10  ? 163 ILE C HA     1 
ATOM   10193 H  HB     . ILE D 1 164 ? 3.662   18.097  40.293  1.00 55.74  ? 163 ILE C HB     1 
ATOM   10194 H  HG12   . ILE D 1 164 ? 5.556   20.055  41.093  1.00 58.61  ? 163 ILE C HG12   1 
ATOM   10195 H  HG13   . ILE D 1 164 ? 5.687   18.525  41.505  1.00 58.61  ? 163 ILE C HG13   1 
ATOM   10196 H  HG21   . ILE D 1 164 ? 3.707   19.924  38.840  1.00 53.75  ? 163 ILE C HG21   1 
ATOM   10197 H  HG22   . ILE D 1 164 ? 2.324   19.884  39.622  1.00 53.75  ? 163 ILE C HG22   1 
ATOM   10198 H  HG23   . ILE D 1 164 ? 3.457   20.907  40.063  1.00 53.75  ? 163 ILE C HG23   1 
ATOM   10199 H  HD11   . ILE D 1 164 ? 7.109   18.981  39.734  1.00 55.82  ? 163 ILE C HD11   1 
ATOM   10200 H  HD12   . ILE D 1 164 ? 5.990   17.956  39.261  1.00 55.82  ? 163 ILE C HD12   1 
ATOM   10201 H  HD13   . ILE D 1 164 ? 5.881   19.490  38.863  1.00 55.82  ? 163 ILE C HD13   1 
ATOM   10202 N  N      . ARG D 1 165 ? 1.234   17.736  41.632  1.00 58.72  ? 164 ARG C N      1 
ATOM   10203 C  CA     . ARG D 1 165 ? -0.197  17.458  41.529  1.00 60.43  ? 164 ARG C CA     1 
ATOM   10204 C  C      . ARG D 1 165 ? -0.942  17.890  42.783  1.00 60.72  ? 164 ARG C C      1 
ATOM   10205 O  O      . ARG D 1 165 ? -2.018  18.495  42.700  1.00 61.60  ? 164 ARG C O      1 
ATOM   10206 C  CB     . ARG D 1 165 ? -0.421  15.964  41.278  1.00 55.80  ? 164 ARG C CB     1 
ATOM   10207 C  CG     . ARG D 1 165 ? -0.710  15.590  39.835  1.00 54.05  ? 164 ARG C CG     1 
ATOM   10208 C  CD     . ARG D 1 165 ? -0.566  14.087  39.621  1.00 50.94  ? 164 ARG C CD     1 
ATOM   10209 N  NE     . ARG D 1 165 ? -0.558  13.716  38.206  1.00 52.13  ? 164 ARG C NE     1 
ATOM   10210 C  CZ     . ARG D 1 165 ? -0.370  12.480  37.771  1.00 45.49  ? 164 ARG C CZ     1 
ATOM   10211 N  NH1    . ARG D 1 165 ? -0.239  11.464  38.615  1.00 45.99  ? 164 ARG C NH1    1 
ATOM   10212 N  NH2    . ARG D 1 165 ? -0.316  12.253  36.466  1.00 46.69  ? 164 ARG C NH2    1 
ATOM   10213 H  H      . ARG D 1 165 ? 1.733   17.065  41.429  1.00 70.49  ? 164 ARG C H      1 
ATOM   10214 H  HA     . ARG D 1 165 ? -0.555  17.957  40.778  1.00 72.55  ? 164 ARG C HA     1 
ATOM   10215 H  HB2    . ARG D 1 165 ? 0.378   15.485  41.547  1.00 66.99  ? 164 ARG C HB2    1 
ATOM   10216 H  HB3    . ARG D 1 165 ? -1.177  15.673  41.811  1.00 66.99  ? 164 ARG C HB3    1 
ATOM   10217 H  HG2    . ARG D 1 165 ? -1.618  15.846  39.611  1.00 64.89  ? 164 ARG C HG2    1 
ATOM   10218 H  HG3    . ARG D 1 165 ? -0.083  16.045  39.252  1.00 64.89  ? 164 ARG C HG3    1 
ATOM   10219 H  HD2    . ARG D 1 165 ? 0.269   13.790  40.014  1.00 61.16  ? 164 ARG C HD2    1 
ATOM   10220 H  HD3    . ARG D 1 165 ? -1.312  13.634  40.045  1.00 61.16  ? 164 ARG C HD3    1 
ATOM   10221 H  HE     . ARG D 1 165 ? -0.682  14.336  37.623  1.00 62.59  ? 164 ARG C HE     1 
ATOM   10222 H  HH11   . ARG D 1 165 ? -0.275  11.602  39.463  1.00 55.23  ? 164 ARG C HH11   1 
ATOM   10223 H  HH12   . ARG D 1 165 ? -0.117  10.667  38.314  1.00 55.23  ? 164 ARG C HH12   1 
ATOM   10224 H  HH21   . ARG D 1 165 ? -0.403  12.905  35.912  1.00 56.06  ? 164 ARG C HH21   1 
ATOM   10225 H  HH22   . ARG D 1 165 ? -0.195  11.454  36.173  1.00 56.06  ? 164 ARG C HH22   1 
ATOM   10226 N  N      . LYS D 1 166 ? -0.388  17.576  43.956  1.00 67.66  ? 165 LYS C N      1 
ATOM   10227 C  CA     . LYS D 1 166 ? -1.019  17.958  45.218  1.00 68.68  ? 165 LYS C CA     1 
ATOM   10228 C  C      . LYS D 1 166 ? -1.249  19.464  45.262  1.00 69.30  ? 165 LYS C C      1 
ATOM   10229 O  O      . LYS D 1 166 ? -2.386  19.937  45.340  1.00 70.95  ? 165 LYS C O      1 
ATOM   10230 C  CB     . LYS D 1 166 ? -0.136  17.518  46.392  1.00 65.66  ? 165 LYS C CB     1 
ATOM   10231 C  CG     . LYS D 1 166 ? -0.580  16.273  47.150  1.00 71.73  ? 165 LYS C CG     1 
ATOM   10232 C  CD     . LYS D 1 166 ? -1.954  16.436  47.793  1.00 82.11  ? 165 LYS C CD     1 
ATOM   10233 C  CE     . LYS D 1 166 ? -2.100  15.582  49.062  1.00 89.99  ? 165 LYS C CE     1 
ATOM   10234 N  NZ     . LYS D 1 166 ? -3.394  14.826  49.135  1.00 87.88  ? 165 LYS C NZ     1 
ATOM   10235 H  H      . LYS D 1 166 ? 0.350   17.143  44.048  1.00 81.22  ? 165 LYS C H      1 
ATOM   10236 H  HA     . LYS D 1 166 ? -1.875  17.509  45.297  1.00 82.45  ? 165 LYS C HA     1 
ATOM   10237 H  HB2    . LYS D 1 166 ? 0.754   17.340  46.049  1.00 78.82  ? 165 LYS C HB2    1 
ATOM   10238 H  HB3    . LYS D 1 166 ? -0.104  18.245  47.034  1.00 78.82  ? 165 LYS C HB3    1 
ATOM   10239 H  HG2    . LYS D 1 166 ? -0.623  15.525  46.534  1.00 86.11  ? 165 LYS C HG2    1 
ATOM   10240 H  HG3    . LYS D 1 166 ? 0.061   16.085  47.854  1.00 86.11  ? 165 LYS C HG3    1 
ATOM   10241 H  HD2    . LYS D 1 166 ? -2.084  17.366  48.037  1.00 98.57  ? 165 LYS C HD2    1 
ATOM   10242 H  HD3    . LYS D 1 166 ? -2.637  16.160  47.162  1.00 98.57  ? 165 LYS C HD3    1 
ATOM   10243 H  HE2    . LYS D 1 166 ? -1.378  14.935  49.088  1.00 108.02 ? 165 LYS C HE2    1 
ATOM   10244 H  HE3    . LYS D 1 166 ? -2.054  16.163  49.837  1.00 108.02 ? 165 LYS C HE3    1 
ATOM   10245 H  HZ1    . LYS D 1 166 ? -3.425  14.348  49.885  1.00 105.49 ? 165 LYS C HZ1    1 
ATOM   10246 H  HZ2    . LYS D 1 166 ? -4.080  15.394  49.126  1.00 105.49 ? 165 LYS C HZ2    1 
ATOM   10247 H  HZ3    . LYS D 1 166 ? -3.465  14.276  48.439  1.00 105.49 ? 165 LYS C HZ3    1 
ATOM   10248 N  N      . HIS D 1 167 ? -0.156  20.231  45.197  1.00 67.51  ? 166 HIS C N      1 
ATOM   10249 C  CA     . HIS D 1 167 ? -0.160  21.692  45.105  1.00 67.07  ? 166 HIS C CA     1 
ATOM   10250 C  C      . HIS D 1 167 ? -0.917  22.209  43.887  1.00 67.30  ? 166 HIS C C      1 
ATOM   10251 O  O      . HIS D 1 167 ? -1.202  23.409  43.818  1.00 70.69  ? 166 HIS C O      1 
ATOM   10252 C  CB     . HIS D 1 167 ? 1.322   22.108  45.122  1.00 62.82  ? 166 HIS C CB     1 
ATOM   10253 C  CG     . HIS D 1 167 ? 1.589   23.534  44.768  1.00 65.38  ? 166 HIS C CG     1 
ATOM   10254 N  ND1    . HIS D 1 167 ? 1.903   24.481  45.717  1.00 64.70  ? 166 HIS C ND1    1 
ATOM   10255 C  CD2    . HIS D 1 167 ? 1.672   24.159  43.570  1.00 64.87  ? 166 HIS C CD2    1 
ATOM   10256 C  CE1    . HIS D 1 167 ? 2.129   25.640  45.122  1.00 65.60  ? 166 HIS C CE1    1 
ATOM   10257 N  NE2    . HIS D 1 167 ? 1.990   25.472  43.819  1.00 66.66  ? 166 HIS C NE2    1 
ATOM   10258 H  H      . HIS D 1 167 ? 0.642   19.912  45.206  1.00 81.05  ? 166 HIS C H      1 
ATOM   10259 H  HA     . HIS D 1 167 ? -0.613  22.114  45.852  1.00 80.52  ? 166 HIS C HA     1 
ATOM   10260 H  HB2    . HIS D 1 167 ? 1.670   21.961  46.016  1.00 75.42  ? 166 HIS C HB2    1 
ATOM   10261 H  HB3    . HIS D 1 167 ? 1.802   21.556  44.485  1.00 75.42  ? 166 HIS C HB3    1 
ATOM   10262 H  HD2    . HIS D 1 167 ? 1.538   23.772  42.735  1.00 77.88  ? 166 HIS C HD2    1 
ATOM   10263 H  HE1    . HIS D 1 167 ? 2.348   26.437  45.548  1.00 78.76  ? 166 HIS C HE1    1 
ATOM   10264 H  HE2    . HIS D 1 167 ? 2.084   26.085  43.224  1.00 80.02  ? 166 HIS C HE2    1 
ATOM   10265 N  N      . LYS D 1 168 ? -1.296  21.338  42.968  1.00 65.16  ? 167 LYS C N      1 
ATOM   10266 C  CA     . LYS D 1 168 ? -1.846  21.727  41.671  1.00 68.14  ? 167 LYS C CA     1 
ATOM   10267 C  C      . LYS D 1 168 ? -3.352  21.549  41.715  1.00 69.38  ? 167 LYS C C      1 
ATOM   10268 O  O      . LYS D 1 168 ? -3.942  21.588  42.800  1.00 70.34  ? 167 LYS C O      1 
ATOM   10269 C  CB     . LYS D 1 168 ? -1.179  20.883  40.578  1.00 63.84  ? 167 LYS C CB     1 
ATOM   10270 C  CG     . LYS D 1 168 ? -1.842  20.830  39.224  1.00 68.71  ? 167 LYS C CG     1 
ATOM   10271 C  CD     . LYS D 1 168 ? -1.024  19.882  38.338  1.00 68.63  ? 167 LYS C CD     1 
ATOM   10272 C  CE     . LYS D 1 168 ? -1.408  19.927  36.864  1.00 70.07  ? 167 LYS C CE     1 
ATOM   10273 N  NZ     . LYS D 1 168 ? -1.842  21.271  36.409  1.00 72.66  ? 167 LYS C NZ     1 
ATOM   10274 H  H      . LYS D 1 168 ? -1.246  20.485  43.069  1.00 78.23  ? 167 LYS C H      1 
ATOM   10275 H  HA     . LYS D 1 168 ? -1.669  22.655  41.450  1.00 81.81  ? 167 LYS C HA     1 
ATOM   10276 H  HB2    . LYS D 1 168 ? -0.286  21.234  40.436  1.00 76.65  ? 167 LYS C HB2    1 
ATOM   10277 H  HB3    . LYS D 1 168 ? -1.129  19.969  40.899  1.00 76.65  ? 167 LYS C HB3    1 
ATOM   10278 H  HG2    . LYS D 1 168 ? -2.747  20.489  39.307  1.00 82.48  ? 167 LYS C HG2    1 
ATOM   10279 H  HG3    . LYS D 1 168 ? -1.856  21.713  38.822  1.00 82.48  ? 167 LYS C HG3    1 
ATOM   10280 H  HD2    . LYS D 1 168 ? -0.087  20.124  38.405  1.00 82.39  ? 167 LYS C HD2    1 
ATOM   10281 H  HD3    . LYS D 1 168 ? -1.155  18.973  38.649  1.00 82.39  ? 167 LYS C HD3    1 
ATOM   10282 H  HE2    . LYS D 1 168 ? -0.640  19.667  36.332  1.00 84.11  ? 167 LYS C HE2    1 
ATOM   10283 H  HE3    . LYS D 1 168 ? -2.141  19.311  36.712  1.00 84.11  ? 167 LYS C HE3    1 
ATOM   10284 H  HZ1    . LYS D 1 168 ? -1.985  21.264  35.531  1.00 87.23  ? 167 LYS C HZ1    1 
ATOM   10285 H  HZ2    . LYS D 1 168 ? -2.596  21.504  36.822  1.00 87.23  ? 167 LYS C HZ2    1 
ATOM   10286 H  HZ3    . LYS D 1 168 ? -1.214  21.874  36.595  1.00 87.23  ? 167 LYS C HZ3    1 
HETATM 10287 P  PG     . GNP E 3 .   ? 9.289   24.405  7.260   1.00 34.78  ? 201 GNP A PG     1 
HETATM 10288 O  O1G    . GNP E 3 .   ? 10.322  24.257  8.280   1.00 20.01  ? 201 GNP A O1G    1 
HETATM 10289 O  O2G    . GNP E 3 .   ? 8.082   25.283  7.736   1.00 30.66  ? 201 GNP A O2G    1 
HETATM 10290 O  O3G    . GNP E 3 .   ? 8.703   22.985  6.902   1.00 31.13  ? 201 GNP A O3G    1 
HETATM 10291 N  N3B    . GNP E 3 .   ? 10.063  24.932  5.828   1.00 20.24  ? 201 GNP A N3B    1 
HETATM 10292 P  PB     . GNP E 3 .   ? 11.069  26.217  5.749   1.00 18.89  ? 201 GNP A PB     1 
HETATM 10293 O  O1B    . GNP E 3 .   ? 12.150  26.178  6.808   1.00 17.35  ? 201 GNP A O1B    1 
HETATM 10294 O  O2B    . GNP E 3 .   ? 10.377  27.517  5.621   1.00 18.15  ? 201 GNP A O2B    1 
HETATM 10295 O  O3A    . GNP E 3 .   ? 11.797  26.063  4.276   1.00 19.23  ? 201 GNP A O3A    1 
HETATM 10296 P  PA     . GNP E 3 .   ? 13.246  25.503  3.984   1.00 20.12  ? 201 GNP A PA     1 
HETATM 10297 O  O1A    . GNP E 3 .   ? 13.245  24.066  4.474   1.00 17.62  ? 201 GNP A O1A    1 
HETATM 10298 O  O2A    . GNP E 3 .   ? 14.372  26.403  4.467   1.00 18.30  ? 201 GNP A O2A    1 
HETATM 10299 O  "O5'"  . GNP E 3 .   ? 13.292  25.451  2.407   1.00 20.13  ? 201 GNP A "O5'"  1 
HETATM 10300 C  "C5'"  . GNP E 3 .   ? 12.264  24.760  1.664   1.00 19.76  ? 201 GNP A "C5'"  1 
HETATM 10301 C  "C4'"  . GNP E 3 .   ? 12.791  24.464  0.268   1.00 22.31  ? 201 GNP A "C4'"  1 
HETATM 10302 O  "O4'"  . GNP E 3 .   ? 13.016  25.748  -0.365  1.00 22.08  ? 201 GNP A "O4'"  1 
HETATM 10303 C  "C3'"  . GNP E 3 .   ? 14.158  23.782  0.333   1.00 23.78  ? 201 GNP A "C3'"  1 
HETATM 10304 O  "O3'"  . GNP E 3 .   ? 14.269  23.012  -0.869  1.00 29.26  ? 201 GNP A "O3'"  1 
HETATM 10305 C  "C2'"  . GNP E 3 .   ? 15.120  24.958  0.216   1.00 22.50  ? 201 GNP A "C2'"  1 
HETATM 10306 O  "O2'"  . GNP E 3 .   ? 16.258  24.545  -0.540  1.00 27.51  ? 201 GNP A "O2'"  1 
HETATM 10307 C  "C1'"  . GNP E 3 .   ? 14.363  25.852  -0.748  1.00 23.79  ? 201 GNP A "C1'"  1 
HETATM 10308 N  N9     . GNP E 3 .   ? 14.744  27.258  -0.564  1.00 22.21  ? 201 GNP A N9     1 
HETATM 10309 C  C8     . GNP E 3 .   ? 14.765  27.971  0.622   1.00 20.85  ? 201 GNP A C8     1 
HETATM 10310 N  N7     . GNP E 3 .   ? 15.155  29.216  0.476   1.00 18.54  ? 201 GNP A N7     1 
HETATM 10311 C  C5     . GNP E 3 .   ? 15.386  29.340  -0.900  1.00 22.06  ? 201 GNP A C5     1 
HETATM 10312 C  C6     . GNP E 3 .   ? 15.809  30.472  -1.689  1.00 20.34  ? 201 GNP A C6     1 
HETATM 10313 O  O6     . GNP E 3 .   ? 16.107  31.635  -1.284  1.00 20.36  ? 201 GNP A O6     1 
HETATM 10314 N  N1     . GNP E 3 .   ? 15.915  30.151  -3.036  1.00 23.17  ? 201 GNP A N1     1 
HETATM 10315 C  C2     . GNP E 3 .   ? 15.659  28.924  -3.578  1.00 25.11  ? 201 GNP A C2     1 
HETATM 10316 N  N2     . GNP E 3 .   ? 15.776  28.817  -4.916  1.00 25.74  ? 201 GNP A N2     1 
HETATM 10317 N  N3     . GNP E 3 .   ? 15.275  27.870  -2.859  1.00 23.84  ? 201 GNP A N3     1 
HETATM 10318 C  C4     . GNP E 3 .   ? 15.136  28.147  -1.545  1.00 22.76  ? 201 GNP A C4     1 
HETATM 10319 H  HNB3   . GNP E 3 .   ? 9.912   24.493  5.104   1.00 24.32  ? 201 GNP A HNB3   1 
HETATM 10320 H  "H5'2" . GNP E 3 .   ? 11.473  25.319  1.604   1.00 23.74  ? 201 GNP A "H5'2" 1 
HETATM 10321 H  "H5'1" . GNP E 3 .   ? 12.039  23.930  2.112   1.00 23.74  ? 201 GNP A "H5'1" 1 
HETATM 10322 H  "H4'"  . GNP E 3 .   ? 12.180  23.942  -0.274  1.00 26.80  ? 201 GNP A "H4'"  1 
HETATM 10323 H  "H3'"  . GNP E 3 .   ? 14.289  23.292  1.160   1.00 28.57  ? 201 GNP A "H3'"  1 
HETATM 10324 H  "HO3'" . GNP E 3 .   ? 15.046  23.104  -1.203  1.00 35.15  ? 201 GNP A "HO3'" 1 
HETATM 10325 H  "H2'"  . GNP E 3 .   ? 15.302  25.352  1.084   1.00 27.03  ? 201 GNP A "H2'"  1 
HETATM 10326 H  "HO2'" . GNP E 3 .   ? 16.931  24.467  -0.033  1.00 33.05  ? 201 GNP A "HO2'" 1 
HETATM 10327 H  "H1'"  . GNP E 3 .   ? 14.481  25.564  -1.666  1.00 28.58  ? 201 GNP A "H1'"  1 
HETATM 10328 H  H8     . GNP E 3 .   ? 14.525  27.604  1.442   1.00 25.05  ? 201 GNP A H8     1 
HETATM 10329 H  HN1    . GNP E 3 .   ? 16.163  30.776  -3.573  1.00 27.84  ? 201 GNP A HN1    1 
HETATM 10330 H  HN21   . GNP E 3 .   ? 15.986  29.509  -5.381  1.00 30.92  ? 201 GNP A HN21   1 
HETATM 10331 H  HN22   . GNP E 3 .   ? 15.614  28.070  -5.310  1.00 30.92  ? 201 GNP A HN22   1 
HETATM 10332 MG MG     . MG  F 4 .   ? 12.212  24.986  8.375   1.00 18.06  ? 202 MG  A MG     1 
HETATM 10333 C  C1     . ZNI G 5 .   ? 5.037   12.394  13.080  1.00 14.71  ? 201 ZNI B C1     1 
HETATM 10334 C  C10    . ZNI G 5 .   ? 10.670  14.976  5.706   1.00 20.10  ? 201 ZNI B C10    1 
HETATM 10335 C  C11    . ZNI G 5 .   ? 11.116  15.338  4.354   1.00 19.96  ? 201 ZNI B C11    1 
HETATM 10336 C  C12    . ZNI G 5 .   ? 10.361  13.189  4.126   1.00 23.00  ? 201 ZNI B C12    1 
HETATM 10337 C  C13    . ZNI G 5 .   ? 5.782   15.446  9.293   1.00 16.70  ? 201 ZNI B C13    1 
HETATM 10338 C  C14    . ZNI G 5 .   ? 6.192   16.676  10.065  1.00 19.23  ? 201 ZNI B C14    1 
HETATM 10339 C  C15    . ZNI G 5 .   ? 6.453   18.384  11.627  1.00 19.79  ? 201 ZNI B C15    1 
HETATM 10340 C  C16    . ZNI G 5 .   ? 7.442   18.736  10.771  1.00 22.69  ? 201 ZNI B C16    1 
HETATM 10341 C  C17    . ZNI G 5 .   ? 6.161   18.922  12.877  1.00 18.61  ? 201 ZNI B C17    1 
HETATM 10342 C  C18    . ZNI G 5 .   ? 5.584   18.143  13.881  1.00 17.81  ? 201 ZNI B C18    1 
HETATM 10343 C  C19    . ZNI G 5 .   ? 5.361   18.554  15.199  1.00 16.78  ? 201 ZNI B C19    1 
HETATM 10344 C  C2     . ZNI G 5 .   ? 5.763   13.676  12.614  1.00 15.42  ? 201 ZNI B C2     1 
HETATM 10345 C  C20    . ZNI G 5 .   ? 5.697   19.899  15.550  1.00 18.67  ? 201 ZNI B C20    1 
HETATM 10346 C  C21    . ZNI G 5 .   ? 6.307   20.697  14.536  1.00 20.62  ? 201 ZNI B C21    1 
HETATM 10347 C  C22    . ZNI G 5 .   ? 6.527   20.233  13.255  1.00 21.24  ? 201 ZNI B C22    1 
HETATM 10348 C  C23    . ZNI G 5 .   ? 5.539   21.326  17.644  1.00 28.01  ? 201 ZNI B C23    1 
HETATM 10349 C  C24    . ZNI G 5 .   ? 4.491   22.368  17.157  1.00 26.97  ? 201 ZNI B C24    1 
HETATM 10350 C  C25    . ZNI G 5 .   ? 4.786   18.896  17.407  1.00 19.24  ? 201 ZNI B C25    1 
HETATM 10351 C  C26    . ZNI G 5 .   ? 4.270   18.763  18.753  1.00 21.20  ? 201 ZNI B C26    1 
HETATM 10352 C  C27    . ZNI G 5 .   ? 5.073   18.859  19.925  1.00 21.12  ? 201 ZNI B C27    1 
HETATM 10353 C  C28    . ZNI G 5 .   ? 6.642   19.064  19.886  1.00 20.51  ? 201 ZNI B C28    1 
HETATM 10354 C  C29    . ZNI G 5 .   ? 8.375   20.728  19.825  1.00 23.50  ? 201 ZNI B C29    1 
HETATM 10355 C  C3     . ZNI G 5 .   ? 5.743   11.272  10.976  1.00 14.84  ? 201 ZNI B C3     1 
HETATM 10356 C  C30    . ZNI G 5 .   ? 7.386   17.994  20.700  1.00 23.71  ? 201 ZNI B C30    1 
HETATM 10357 C  C31    . ZNI G 5 .   ? 3.184   18.545  21.320  1.00 25.10  ? 201 ZNI B C31    1 
HETATM 10358 C  C32    . ZNI G 5 .   ? 2.271   18.451  20.266  1.00 27.00  ? 201 ZNI B C32    1 
HETATM 10359 C  C33    . ZNI G 5 .   ? 0.066   18.712  21.468  1.00 30.04  ? 201 ZNI B C33    1 
HETATM 10360 C  C34    . ZNI G 5 .   ? -1.158  17.781  21.697  1.00 28.58  ? 201 ZNI B C34    1 
HETATM 10361 C  C35    . ZNI G 5 .   ? -2.997  16.597  20.926  1.00 36.63  ? 201 ZNI B C35    1 
HETATM 10362 C  C36    . ZNI G 5 .   ? -4.370  16.434  20.360  1.00 38.35  ? 201 ZNI B C36    1 
HETATM 10363 C  C37    . ZNI G 5 .   ? -4.131  17.231  21.651  1.00 34.49  ? 201 ZNI B C37    1 
HETATM 10364 C  C38    . ZNI G 5 .   ? -1.253  17.235  19.346  1.00 29.12  ? 201 ZNI B C38    1 
HETATM 10365 C  C39    . ZNI G 5 .   ? 0.050   18.112  19.123  1.00 31.68  ? 201 ZNI B C39    1 
HETATM 10366 C  C4     . ZNI G 5 .   ? 4.554   11.596  11.863  1.00 15.19  ? 201 ZNI B C4     1 
HETATM 10367 C  C40    . ZNI G 5 .   ? 2.914   18.586  19.004  1.00 23.18  ? 201 ZNI B C40    1 
HETATM 10368 C  C41    . ZNI G 5 .   ? 4.756   17.957  16.382  1.00 18.57  ? 201 ZNI B C41    1 
HETATM 10369 C  C42    . ZNI G 5 .   ? 4.169   16.552  16.505  1.00 17.14  ? 201 ZNI B C42    1 
HETATM 10370 C  C43    . ZNI G 5 .   ? 5.037   15.356  16.929  1.00 15.11  ? 201 ZNI B C43    1 
HETATM 10371 C  C44    . ZNI G 5 .   ? 4.157   14.055  16.909  1.00 17.33  ? 201 ZNI B C44    1 
HETATM 10372 C  C45    . ZNI G 5 .   ? 5.563   15.686  18.351  1.00 16.52  ? 201 ZNI B C45    1 
HETATM 10373 C  C46    . ZNI G 5 .   ? 6.148   15.145  15.999  1.00 17.24  ? 201 ZNI B C46    1 
HETATM 10374 C  C47    . ZNI G 5 .   ? 6.442   14.312  13.794  1.00 15.11  ? 201 ZNI B C47    1 
HETATM 10375 C  C5     . ZNI G 5 .   ? 6.379   13.075  9.272   1.00 16.58  ? 201 ZNI B C5     1 
HETATM 10376 C  C6     . ZNI G 5 .   ? 6.939   14.487  9.068   1.00 14.86  ? 201 ZNI B C6     1 
HETATM 10377 C  C7     . ZNI G 5 .   ? 8.878   14.383  7.516   1.00 15.44  ? 201 ZNI B C7     1 
HETATM 10378 C  C8     . ZNI G 5 .   ? 9.330   14.459  6.145   1.00 17.59  ? 201 ZNI B C8     1 
HETATM 10379 C  C9     . ZNI G 5 .   ? 10.346  13.502  5.583   1.00 19.72  ? 201 ZNI B C9     1 
HETATM 10380 N  N1     . ZNI G 5 .   ? 6.826   13.361  11.647  1.00 16.84  ? 201 ZNI B N1     1 
HETATM 10381 N  N2     . ZNI G 5 .   ? 6.330   12.567  10.609  1.00 17.88  ? 201 ZNI B N2     1 
HETATM 10382 N  N3     . ZNI G 5 .   ? 7.583   14.569  7.771   1.00 15.80  ? 201 ZNI B N3     1 
HETATM 10383 N  N4     . ZNI G 5 .   ? 5.835   17.139  11.199  1.00 19.56  ? 201 ZNI B N4     1 
HETATM 10384 N  N5     . ZNI G 5 .   ? 5.375   20.072  16.887  1.00 22.00  ? 201 ZNI B N5     1 
HETATM 10385 N  N6     . ZNI G 5 .   ? 4.514   18.733  21.130  1.00 22.17  ? 201 ZNI B N6     1 
HETATM 10386 N  N7     . ZNI G 5 .   ? 0.858   18.215  20.333  1.00 27.03  ? 201 ZNI B N7     1 
HETATM 10387 N  N8     . ZNI G 5 .   ? -2.000  17.558  20.534  1.00 31.95  ? 201 ZNI B N8     1 
HETATM 10388 O  O1     . ZNI G 5 .   ? 5.959   12.477  8.300   1.00 16.90  ? 201 ZNI B O1     1 
HETATM 10389 O  O2     . ZNI G 5 .   ? 9.706   14.119  8.394   1.00 15.28  ? 201 ZNI B O2     1 
HETATM 10390 O  O3     . ZNI G 5 .   ? 10.323  14.466  3.555   1.00 19.80  ? 201 ZNI B O3     1 
HETATM 10391 O  O4     . ZNI G 5 .   ? 7.004   20.380  20.267  1.00 26.51  ? 201 ZNI B O4     1 
HETATM 10392 O  O5     . ZNI G 5 .   ? 5.621   14.860  14.678  1.00 14.40  ? 201 ZNI B O5     1 
HETATM 10393 O  O6     . ZNI G 5 .   ? 7.654   14.284  13.943  1.00 16.72  ? 201 ZNI B O6     1 
HETATM 10394 S  S1     . ZNI G 5 .   ? 7.548   17.683  9.415   1.00 20.16  ? 201 ZNI B S1     1 
HETATM 10395 H  H1     . ZNI G 5 .   ? 5.603   11.835  13.635  1.00 17.69  ? 201 ZNI B H1     1 
HETATM 10396 H  H2     . ZNI G 5 .   ? 4.288   12.590  13.663  1.00 17.69  ? 201 ZNI B H2     1 
HETATM 10397 H  H3     . ZNI G 5 .   ? 11.293  15.252  6.396   1.00 24.16  ? 201 ZNI B H3     1 
HETATM 10398 H  H4     . ZNI G 5 .   ? 10.977  16.263  4.097   1.00 23.99  ? 201 ZNI B H4     1 
HETATM 10399 H  H5     . ZNI G 5 .   ? 12.060  15.208  4.172   1.00 23.99  ? 201 ZNI B H5     1 
HETATM 10400 H  H6     . ZNI G 5 .   ? 9.598   12.662  3.842   1.00 27.64  ? 201 ZNI B H6     1 
HETATM 10401 H  H7     . ZNI G 5 .   ? 11.157  12.711  3.848   1.00 27.64  ? 201 ZNI B H7     1 
HETATM 10402 H  H8     . ZNI G 5 .   ? 5.049   14.954  9.695   1.00 20.07  ? 201 ZNI B H8     1 
HETATM 10403 H  H9     . ZNI G 5 .   ? 5.371   15.638  8.435   1.00 20.07  ? 201 ZNI B H9     1 
HETATM 10404 H  H10    . ZNI G 5 .   ? 8.088   19.403  10.717  1.00 27.26  ? 201 ZNI B H10    1 
HETATM 10405 H  H11    . ZNI G 5 .   ? 5.329   17.279  13.652  1.00 21.40  ? 201 ZNI B H11    1 
HETATM 10406 H  H12    . ZNI G 5 .   ? 5.110   14.270  12.213  1.00 18.53  ? 201 ZNI B H12    1 
HETATM 10407 H  H13    . ZNI G 5 .   ? 6.574   21.567  14.727  1.00 24.77  ? 201 ZNI B H13    1 
HETATM 10408 H  H14    . ZNI G 5 .   ? 6.923   20.784  12.618  1.00 25.53  ? 201 ZNI B H14    1 
HETATM 10409 H  H15    . ZNI G 5 .   ? 6.430   21.702  17.577  1.00 33.64  ? 201 ZNI B H15    1 
HETATM 10410 H  H16    . ZNI G 5 .   ? 5.461   21.208  18.604  1.00 33.64  ? 201 ZNI B H16    1 
HETATM 10411 H  H17    . ZNI G 5 .   ? 3.754   22.527  17.767  1.00 32.40  ? 201 ZNI B H17    1 
HETATM 10412 H  H18    . ZNI G 5 .   ? 4.841   23.258  16.993  1.00 32.40  ? 201 ZNI B H18    1 
HETATM 10413 H  H19    . ZNI G 5 .   ? 4.047   22.147  16.323  1.00 32.40  ? 201 ZNI B H19    1 
HETATM 10414 H  H20    . ZNI G 5 .   ? 6.975   18.998  18.977  1.00 24.64  ? 201 ZNI B H20    1 
HETATM 10415 H  H21    . ZNI G 5 .   ? 8.583   20.595  18.887  1.00 28.23  ? 201 ZNI B H21    1 
HETATM 10416 H  H22    . ZNI G 5 .   ? 8.658   21.647  19.949  1.00 28.23  ? 201 ZNI B H22    1 
HETATM 10417 H  H23    . ZNI G 5 .   ? 9.107   20.250  20.246  1.00 28.23  ? 201 ZNI B H23    1 
HETATM 10418 H  H24    . ZNI G 5 .   ? 6.356   10.675  11.433  1.00 17.85  ? 201 ZNI B H24    1 
HETATM 10419 H  H25    . ZNI G 5 .   ? 5.467   10.733  10.219  1.00 17.85  ? 201 ZNI B H25    1 
HETATM 10420 H  H26    . ZNI G 5 .   ? 7.941   18.353  21.410  1.00 28.48  ? 201 ZNI B H26    1 
HETATM 10421 H  H27    . ZNI G 5 .   ? 6.803   17.359  21.145  1.00 28.48  ? 201 ZNI B H27    1 
HETATM 10422 H  H28    . ZNI G 5 .   ? 7.988   17.444  20.175  1.00 28.48  ? 201 ZNI B H28    1 
HETATM 10423 H  H29    . ZNI G 5 .   ? 2.906   18.480  22.205  1.00 30.15  ? 201 ZNI B H29    1 
HETATM 10424 H  H30    . ZNI G 5 .   ? -0.239  19.617  21.297  1.00 36.08  ? 201 ZNI B H30    1 
HETATM 10425 H  H31    . ZNI G 5 .   ? 0.608   18.742  22.271  1.00 36.08  ? 201 ZNI B H31    1 
HETATM 10426 H  H32    . ZNI G 5 .   ? -0.900  16.905  22.024  1.00 34.33  ? 201 ZNI B H32    1 
HETATM 10427 H  H33    . ZNI G 5 .   ? -1.741  18.105  22.401  1.00 34.33  ? 201 ZNI B H33    1 
HETATM 10428 H  H34    . ZNI G 5 .   ? -2.630  15.791  21.321  1.00 44.00  ? 201 ZNI B H34    1 
HETATM 10429 H  H35    . ZNI G 5 .   ? -4.749  15.541  20.364  1.00 46.06  ? 201 ZNI B H35    1 
HETATM 10430 H  H36    . ZNI G 5 .   ? -4.554  16.866  19.511  1.00 46.06  ? 201 ZNI B H36    1 
HETATM 10431 H  H37    . ZNI G 5 .   ? -4.108  18.200  21.668  1.00 41.42  ? 201 ZNI B H37    1 
HETATM 10432 H  H38    . ZNI G 5 .   ? -4.305  16.860  22.531  1.00 41.42  ? 201 ZNI B H38    1 
HETATM 10433 H  H39    . ZNI G 5 .   ? -1.096  16.282  19.430  1.00 34.98  ? 201 ZNI B H39    1 
HETATM 10434 H  H40    . ZNI G 5 .   ? -1.915  17.298  18.640  1.00 34.98  ? 201 ZNI B H40    1 
HETATM 10435 H  H41    . ZNI G 5 .   ? 0.584   17.712  18.419  1.00 38.05  ? 201 ZNI B H41    1 
HETATM 10436 H  H42    . ZNI G 5 .   ? -0.213  19.003  18.841  1.00 38.05  ? 201 ZNI B H42    1 
HETATM 10437 H  H43    . ZNI G 5 .   ? 3.862   12.068  11.373  1.00 18.26  ? 201 ZNI B H43    1 
HETATM 10438 H  H44    . ZNI G 5 .   ? 4.075   10.794  12.124  1.00 18.26  ? 201 ZNI B H44    1 
HETATM 10439 H  H45    . ZNI G 5 .   ? 2.329   18.546  18.282  1.00 27.85  ? 201 ZNI B H45    1 
HETATM 10440 H  H46    . ZNI G 5 .   ? 3.387   16.569  17.079  1.00 20.60  ? 201 ZNI B H46    1 
HETATM 10441 H  H47    . ZNI G 5 .   ? 3.712   16.311  15.684  1.00 20.60  ? 201 ZNI B H47    1 
HETATM 10442 H  H48    . ZNI G 5 .   ? 3.681   13.856  16.088  1.00 20.83  ? 201 ZNI B H48    1 
HETATM 10443 H  H49    . ZNI G 5 .   ? 4.612   13.212  17.067  1.00 20.83  ? 201 ZNI B H49    1 
HETATM 10444 H  H50    . ZNI G 5 .   ? 3.437   13.999  17.557  1.00 20.83  ? 201 ZNI B H50    1 
HETATM 10445 H  H51    . ZNI G 5 .   ? 5.996   14.953  18.816  1.00 19.86  ? 201 ZNI B H51    1 
HETATM 10446 H  H52    . ZNI G 5 .   ? 6.226   16.392  18.396  1.00 19.86  ? 201 ZNI B H52    1 
HETATM 10447 H  H53    . ZNI G 5 .   ? 4.892   15.979  18.986  1.00 19.86  ? 201 ZNI B H53    1 
HETATM 10448 H  H54    . ZNI G 5 .   ? 6.720   14.430  16.317  1.00 20.73  ? 201 ZNI B H54    1 
HETATM 10449 H  H55    . ZNI G 5 .   ? 6.730   15.921  15.991  1.00 20.73  ? 201 ZNI B H55    1 
HETATM 10450 H  H56    . ZNI G 5 .   ? 7.544   14.692  9.798   1.00 17.87  ? 201 ZNI B H56    1 
HETATM 10451 H  H57    . ZNI G 5 .   ? 8.657   14.726  5.500   1.00 21.14  ? 201 ZNI B H57    1 
HETATM 10452 H  H58    . ZNI G 5 .   ? 10.870  12.885  6.117   1.00 23.70  ? 201 ZNI B H58    1 
HETATM 10453 H  H59    . ZNI G 5 .   ? 7.159   14.123  11.331  1.00 20.24  ? 201 ZNI B H59    1 
HETATM 10454 H  H60    . ZNI G 5 .   ? 7.058   14.756  7.116   1.00 18.99  ? 201 ZNI B H60    1 
HETATM 10455 C  C1     . ZNI H 5 .   ? 34.309  28.554  30.592  1.00 24.21  ? 201 ZNI D C1     1 
HETATM 10456 C  C10    . ZNI H 5 .   ? 36.783  19.905  32.916  1.00 34.27  ? 201 ZNI D C10    1 
HETATM 10457 C  C11    . ZNI H 5 .   ? 37.839  19.043  33.538  1.00 35.36  ? 201 ZNI D C11    1 
HETATM 10458 C  C12    . ZNI H 5 .   ? 35.805  18.149  34.196  1.00 35.22  ? 201 ZNI D C12    1 
HETATM 10459 C  C13    . ZNI H 5 .   ? 33.944  25.335  34.201  1.00 30.05  ? 201 ZNI D C13    1 
HETATM 10460 C  C14    . ZNI H 5 .   ? 32.427  25.259  34.143  1.00 31.31  ? 201 ZNI D C14    1 
HETATM 10461 C  C15    . ZNI H 5 .   ? 30.138  25.664  33.922  1.00 35.48  ? 201 ZNI D C15    1 
HETATM 10462 C  C16    . ZNI H 5 .   ? 30.126  24.335  34.187  1.00 38.53  ? 201 ZNI D C16    1 
HETATM 10463 C  C17    . ZNI H 5 .   ? 28.964  26.525  33.594  1.00 32.18  ? 201 ZNI D C17    1 
HETATM 10464 C  C18    . ZNI H 5 .   ? 29.107  27.707  32.847  1.00 30.44  ? 201 ZNI D C18    1 
HETATM 10465 C  C19    . ZNI H 5 .   ? 28.033  28.585  32.401  1.00 32.14  ? 201 ZNI D C19    1 
HETATM 10466 C  C2     . ZNI H 5 .   ? 33.399  27.437  31.182  1.00 21.38  ? 201 ZNI D C2     1 
HETATM 10467 C  C20    . ZNI H 5 .   ? 26.691  28.193  32.710  1.00 31.19  ? 201 ZNI D C20    1 
HETATM 10468 C  C21    . ZNI H 5 .   ? 26.531  26.948  33.422  1.00 32.90  ? 201 ZNI D C21    1 
HETATM 10469 C  C22    . ZNI H 5 .   ? 27.600  26.147  33.828  1.00 33.35  ? 201 ZNI D C22    1 
HETATM 10470 C  C23    . ZNI H 5 .   ? 24.314  29.198  32.322  1.00 33.83  ? 201 ZNI D C23    1 
HETATM 10471 C  C24    . ZNI H 5 .   ? 23.784  29.971  33.601  1.00 38.39  ? 201 ZNI D C24    1 
HETATM 10472 C  C25    . ZNI H 5 .   ? 26.602  30.239  31.579  1.00 31.93  ? 201 ZNI D C25    1 
HETATM 10473 C  C26    . ZNI H 5 .   ? 26.030  31.476  30.941  1.00 32.94  ? 201 ZNI D C26    1 
HETATM 10474 C  C27    . ZNI H 5 .   ? 25.204  31.459  29.786  1.00 30.63  ? 201 ZNI D C27    1 
HETATM 10475 C  C28    . ZNI H 5 .   ? 24.824  30.077  29.068  1.00 29.16  ? 201 ZNI D C28    1 
HETATM 10476 C  C29    . ZNI H 5 .   ? 23.224  28.231  29.164  1.00 37.01  ? 201 ZNI D C29    1 
HETATM 10477 C  C3     . ZNI H 5 .   ? 36.290  26.953  30.840  1.00 27.21  ? 201 ZNI D C3     1 
HETATM 10478 C  C30    . ZNI H 5 .   ? 25.173  30.072  27.557  1.00 28.52  ? 201 ZNI D C30    1 
HETATM 10479 C  C31    . ZNI H 5 .   ? 25.018  33.842  29.781  1.00 31.93  ? 201 ZNI D C31    1 
HETATM 10480 C  C32    . ZNI H 5 .   ? 25.812  34.023  30.915  1.00 34.64  ? 201 ZNI D C32    1 
HETATM 10481 C  C33    . ZNI H 5 .   ? 27.109  35.290  32.679  1.00 40.04  ? 201 ZNI D C33    1 
HETATM 10482 C  C34    . ZNI H 5 .   ? 27.920  36.618  32.707  1.00 38.26  ? 201 ZNI D C34    1 
HETATM 10483 C  C35    . ZNI H 5 .   ? 27.969  38.968  32.700  1.00 42.46  ? 201 ZNI D C35    1 
HETATM 10484 C  C36    . ZNI H 5 .   ? 28.244  39.801  33.918  1.00 48.18  ? 201 ZNI D C36    1 
HETATM 10485 C  C37    . ZNI H 5 .   ? 27.227  40.257  32.864  1.00 45.18  ? 201 ZNI D C37    1 
HETATM 10486 C  C38    . ZNI H 5 .   ? 26.211  37.750  31.498  1.00 45.20  ? 201 ZNI D C38    1 
HETATM 10487 C  C39    . ZNI H 5 .   ? 25.328  36.444  31.443  1.00 40.48  ? 201 ZNI D C39    1 
HETATM 10488 C  C4     . ZNI H 5 .   ? 35.760  28.378  31.005  1.00 21.97  ? 201 ZNI D C4     1 
HETATM 10489 C  C40    . ZNI H 5 .   ? 26.279  32.763  31.450  1.00 29.54  ? 201 ZNI D C40    1 
HETATM 10490 C  C41    . ZNI H 5 .   ? 27.948  29.874  31.692  1.00 28.24  ? 201 ZNI D C41    1 
HETATM 10491 C  C42    . ZNI H 5 .   ? 29.171  30.700  31.188  1.00 25.43  ? 201 ZNI D C42    1 
HETATM 10492 C  C43    . ZNI H 5 .   ? 29.777  30.383  29.779  1.00 24.30  ? 201 ZNI D C43    1 
HETATM 10493 C  C44    . ZNI H 5 .   ? 30.960  31.401  29.454  1.00 25.94  ? 201 ZNI D C44    1 
HETATM 10494 C  C45    . ZNI H 5 .   ? 28.655  30.483  28.752  1.00 25.08  ? 201 ZNI D C45    1 
HETATM 10495 C  C46    . ZNI H 5 .   ? 30.222  28.917  29.766  1.00 25.36  ? 201 ZNI D C46    1 
HETATM 10496 C  C47    . ZNI H 5 .   ? 32.115  27.526  30.356  1.00 20.53  ? 201 ZNI D C47    1 
HETATM 10497 C  C5     . ZNI H 5 .   ? 35.636  25.256  32.538  1.00 27.08  ? 201 ZNI D C5     1 
HETATM 10498 C  C6     . ZNI H 5 .   ? 34.567  24.393  33.201  1.00 31.56  ? 201 ZNI D C6     1 
HETATM 10499 C  C7     . ZNI H 5 .   ? 35.118  21.997  33.059  1.00 30.12  ? 201 ZNI D C7     1 
HETATM 10500 C  C8     . ZNI H 5 .   ? 35.692  20.756  33.621  1.00 31.65  ? 201 ZNI D C8     1 
HETATM 10501 C  C9     . ZNI H 5 .   ? 35.443  19.306  33.270  1.00 37.41  ? 201 ZNI D C9     1 
HETATM 10502 N  N1     . ZNI H 5 .   ? 33.967  26.097  30.971  1.00 24.99  ? 201 ZNI D N1     1 
HETATM 10503 N  N2     . ZNI H 5 .   ? 35.282  26.064  31.438  1.00 23.40  ? 201 ZNI D N2     1 
HETATM 10504 N  N3     . ZNI H 5 .   ? 35.102  23.178  33.749  1.00 30.83  ? 201 ZNI D N3     1 
HETATM 10505 N  N4     . ZNI H 5 .   ? 31.521  26.160  33.912  1.00 29.79  ? 201 ZNI D N4     1 
HETATM 10506 N  N5     . ZNI H 5 .   ? 25.812  29.191  32.202  1.00 32.52  ? 201 ZNI D N5     1 
HETATM 10507 N  N6     . ZNI H 5 .   ? 24.732  32.618  29.282  1.00 29.37  ? 201 ZNI D N6     1 
HETATM 10508 N  N7     . ZNI H 5 .   ? 26.179  35.279  31.545  1.00 34.07  ? 201 ZNI D N7     1 
HETATM 10509 N  N8     . ZNI H 5 .   ? 27.071  37.835  32.655  1.00 41.97  ? 201 ZNI D N8     1 
HETATM 10510 O  O1     . ZNI H 5 .   ? 36.767  25.195  32.969  1.00 26.69  ? 201 ZNI D O1     1 
HETATM 10511 O  O2     . ZNI H 5 .   ? 34.674  21.978  31.917  1.00 28.83  ? 201 ZNI D O2     1 
HETATM 10512 O  O3     . ZNI H 5 .   ? 37.092  18.513  34.656  1.00 34.05  ? 201 ZNI D O3     1 
HETATM 10513 O  O4     . ZNI H 5 .   ? 23.497  29.686  29.268  1.00 31.12  ? 201 ZNI D O4     1 
HETATM 10514 O  O5     . ZNI H 5 .   ? 31.428  28.659  30.526  1.00 21.93  ? 201 ZNI D O5     1 
HETATM 10515 O  O6     . ZNI H 5 .   ? 31.779  26.688  29.536  1.00 24.68  ? 201 ZNI D O6     1 
HETATM 10516 S  S1     . ZNI H 5 .   ? 31.676  23.612  34.413  1.00 37.38  ? 201 ZNI D S1     1 
HETATM 10517 H  H1     . ZNI H 5 .   ? 34.007  29.437  30.856  1.00 29.08  ? 201 ZNI D H1     1 
HETATM 10518 H  H2     . ZNI H 5 .   ? 34.254  28.586  29.624  1.00 29.08  ? 201 ZNI D H2     1 
HETATM 10519 H  H3     . ZNI H 5 .   ? 36.921  20.035  31.965  1.00 41.16  ? 201 ZNI D H3     1 
HETATM 10520 H  H4     . ZNI H 5 .   ? 38.193  18.332  32.982  1.00 42.46  ? 201 ZNI D H4     1 
HETATM 10521 H  H5     . ZNI H 5 .   ? 38.642  19.499  33.835  1.00 42.46  ? 201 ZNI D H5     1 
HETATM 10522 H  H6     . ZNI H 5 .   ? 35.835  17.293  33.740  1.00 42.30  ? 201 ZNI D H6     1 
HETATM 10523 H  H7     . ZNI H 5 .   ? 35.191  18.053  34.941  1.00 42.30  ? 201 ZNI D H7     1 
HETATM 10524 H  H8     . ZNI H 5 .   ? 34.305  26.225  34.066  1.00 36.10  ? 201 ZNI D H8     1 
HETATM 10525 H  H9     . ZNI H 5 .   ? 34.320  25.160  35.078  1.00 36.10  ? 201 ZNI D H9     1 
HETATM 10526 H  H10    . ZNI H 5 .   ? 29.477  23.676  34.284  1.00 46.26  ? 201 ZNI D H10    1 
HETATM 10527 H  H11    . ZNI H 5 .   ? 29.974  27.949  32.615  1.00 36.56  ? 201 ZNI D H11    1 
HETATM 10528 H  H12    . ZNI H 5 .   ? 33.271  27.552  32.136  1.00 25.65  ? 201 ZNI D H12    1 
HETATM 10529 H  H13    . ZNI H 5 .   ? 25.677  26.646  33.631  1.00 39.51  ? 201 ZNI D H13    1 
HETATM 10530 H  H14    . ZNI H 5 .   ? 27.437  25.341  34.264  1.00 40.05  ? 201 ZNI D H14    1 
HETATM 10531 H  H15    . ZNI H 5 .   ? 23.941  28.303  32.327  1.00 40.63  ? 201 ZNI D H15    1 
HETATM 10532 H  H16    . ZNI H 5 .   ? 23.883  29.572  31.537  1.00 40.63  ? 201 ZNI D H16    1 
HETATM 10533 H  H17    . ZNI H 5 .   ? 23.461  30.870  33.434  1.00 46.10  ? 201 ZNI D H17    1 
HETATM 10534 H  H18    . ZNI H 5 .   ? 23.040  29.548  34.058  1.00 46.10  ? 201 ZNI D H18    1 
HETATM 10535 H  H19    . ZNI H 5 .   ? 24.437  30.096  34.306  1.00 46.10  ? 201 ZNI D H19    1 
HETATM 10536 H  H20    . ZNI H 5 .   ? 25.325  29.364  29.495  1.00 35.03  ? 201 ZNI D H20    1 
HETATM 10537 H  H21    . ZNI H 5 .   ? 22.314  27.940  29.329  1.00 44.45  ? 201 ZNI D H21    1 
HETATM 10538 H  H22    . ZNI H 5 .   ? 23.400  27.810  28.308  1.00 44.45  ? 201 ZNI D H22    1 
HETATM 10539 H  H23    . ZNI H 5 .   ? 23.716  27.646  29.762  1.00 44.45  ? 201 ZNI D H23    1 
HETATM 10540 H  H24    . ZNI H 5 .   ? 37.172  26.873  31.236  1.00 32.69  ? 201 ZNI D H24    1 
HETATM 10541 H  H25    . ZNI H 5 .   ? 36.474  26.768  29.905  1.00 32.69  ? 201 ZNI D H25    1 
HETATM 10542 H  H26    . ZNI H 5 .   ? 24.409  29.931  26.975  1.00 34.26  ? 201 ZNI D H26    1 
HETATM 10543 H  H27    . ZNI H 5 .   ? 25.805  29.383  27.299  1.00 34.26  ? 201 ZNI D H27    1 
HETATM 10544 H  H28    . ZNI H 5 .   ? 25.570  30.898  27.240  1.00 34.26  ? 201 ZNI D H28    1 
HETATM 10545 H  H29    . ZNI H 5 .   ? 24.654  34.565  29.324  1.00 38.35  ? 201 ZNI D H29    1 
HETATM 10546 H  H30    . ZNI H 5 .   ? 26.623  35.192  33.512  1.00 48.08  ? 201 ZNI D H30    1 
HETATM 10547 H  H31    . ZNI H 5 .   ? 27.722  34.540  32.617  1.00 48.08  ? 201 ZNI D H31    1 
HETATM 10548 H  H32    . ZNI H 5 .   ? 28.484  36.696  33.492  1.00 45.95  ? 201 ZNI D H32    1 
HETATM 10549 H  H33    . ZNI H 5 .   ? 28.559  36.683  31.980  1.00 45.95  ? 201 ZNI D H33    1 
HETATM 10550 H  H34    . ZNI H 5 .   ? 28.669  38.960  32.028  1.00 50.99  ? 201 ZNI D H34    1 
HETATM 10551 H  H35    . ZNI H 5 .   ? 29.125  40.199  33.993  1.00 57.85  ? 201 ZNI D H35    1 
HETATM 10552 H  H36    . ZNI H 5 .   ? 27.972  39.436  34.775  1.00 57.85  ? 201 ZNI D H36    1 
HETATM 10553 H  H37    . ZNI H 5 .   ? 27.436  40.929  32.196  1.00 54.25  ? 201 ZNI D H37    1 
HETATM 10554 H  H38    . ZNI H 5 .   ? 26.270  40.158  32.987  1.00 54.25  ? 201 ZNI D H38    1 
HETATM 10555 H  H39    . ZNI H 5 .   ? 25.713  38.582  31.521  1.00 54.28  ? 201 ZNI D H39    1 
HETATM 10556 H  H40    . ZNI H 5 .   ? 26.819  37.867  30.751  1.00 54.28  ? 201 ZNI D H40    1 
HETATM 10557 H  H41    . ZNI H 5 .   ? 24.691  36.448  32.174  1.00 48.61  ? 201 ZNI D H41    1 
HETATM 10558 H  H42    . ZNI H 5 .   ? 24.836  36.416  30.607  1.00 48.61  ? 201 ZNI D H42    1 
HETATM 10559 H  H43    . ZNI H 5 .   ? 36.327  29.002  30.526  1.00 26.19  ? 201 ZNI D H43    1 
HETATM 10560 H  H44    . ZNI H 5 .   ? 35.892  28.678  31.918  1.00 26.19  ? 201 ZNI D H44    1 
HETATM 10561 H  H45    . ZNI H 5 .   ? 26.801  32.849  32.215  1.00 35.48  ? 201 ZNI D H45    1 
HETATM 10562 H  H46    . ZNI H 5 .   ? 29.886  30.684  31.843  1.00 30.55  ? 201 ZNI D H46    1 
HETATM 10563 H  H47    . ZNI H 5 .   ? 28.982  31.650  31.236  1.00 30.55  ? 201 ZNI D H47    1 
HETATM 10564 H  H48    . ZNI H 5 .   ? 31.769  31.321  29.982  1.00 31.17  ? 201 ZNI D H48    1 
HETATM 10565 H  H49    . ZNI H 5 .   ? 31.325  31.382  28.555  1.00 31.17  ? 201 ZNI D H49    1 
HETATM 10566 H  H50    . ZNI H 5 .   ? 30.768  32.347  29.553  1.00 31.17  ? 201 ZNI D H50    1 
HETATM 10567 H  H51    . ZNI H 5 .   ? 28.015  29.754  28.761  1.00 30.13  ? 201 ZNI D H51    1 
HETATM 10568 H  H52    . ZNI H 5 .   ? 28.089  31.267  28.827  1.00 30.13  ? 201 ZNI D H52    1 
HETATM 10569 H  H53    . ZNI H 5 .   ? 28.939  30.509  27.824  1.00 30.13  ? 201 ZNI D H53    1 
HETATM 10570 H  H54    . ZNI H 5 .   ? 29.493  28.366  30.091  1.00 30.46  ? 201 ZNI D H54    1 
HETATM 10571 H  H55    . ZNI H 5 .   ? 30.335  28.632  28.846  1.00 30.46  ? 201 ZNI D H55    1 
HETATM 10572 H  H56    . ZNI H 5 .   ? 33.885  24.182  32.544  1.00 37.91  ? 201 ZNI D H56    1 
HETATM 10573 H  H57    . ZNI H 5 .   ? 35.804  20.797  34.584  1.00 38.01  ? 201 ZNI D H57    1 
HETATM 10574 H  H58    . ZNI H 5 .   ? 34.838  19.042  32.559  1.00 44.92  ? 201 ZNI D H58    1 
HETATM 10575 H  H59    . ZNI H 5 .   ? 33.460  25.497  31.390  1.00 30.03  ? 201 ZNI D H59    1 
HETATM 10576 H  H60    . ZNI H 5 .   ? 35.421  23.218  34.547  1.00 37.02  ? 201 ZNI D H60    1 
HETATM 10577 P  PG     . GNP I 3 .   ? 27.112  19.556  38.292  1.00 50.77  ? 201 GNP C PG     1 
HETATM 10578 O  O1G    . GNP I 3 .   ? 26.313  19.384  37.074  1.00 33.34  ? 201 GNP C O1G    1 
HETATM 10579 O  O2G    . GNP I 3 .   ? 26.332  20.464  39.274  1.00 43.81  ? 201 GNP C O2G    1 
HETATM 10580 O  O3G    . GNP I 3 .   ? 28.415  20.324  37.900  1.00 49.50  ? 201 GNP C O3G    1 
HETATM 10581 N  N3B    . GNP I 3 .   ? 27.538  18.039  39.046  1.00 41.57  ? 201 GNP C N3B    1 
HETATM 10582 P  PB     . GNP I 3 .   ? 26.431  16.853  39.356  1.00 31.82  ? 201 GNP C PB     1 
HETATM 10583 O  O1B    . GNP I 3 .   ? 25.524  16.739  38.145  1.00 34.50  ? 201 GNP C O1B    1 
HETATM 10584 O  O2B    . GNP I 3 .   ? 25.671  17.231  40.614  1.00 28.70  ? 201 GNP C O2B    1 
HETATM 10585 O  O3A    . GNP I 3 .   ? 27.084  15.397  39.758  1.00 34.28  ? 201 GNP C O3A    1 
HETATM 10586 P  PA     . GNP I 3 .   ? 27.417  14.264  38.654  1.00 34.04  ? 201 GNP C PA     1 
HETATM 10587 O  O1A    . GNP I 3 .   ? 26.110  13.557  38.295  1.00 36.38  ? 201 GNP C O1A    1 
HETATM 10588 O  O2A    . GNP I 3 .   ? 28.166  14.821  37.437  1.00 36.40  ? 201 GNP C O2A    1 
HETATM 10589 O  "O5'"  . GNP I 3 .   ? 28.289  13.221  39.496  1.00 37.86  ? 201 GNP C "O5'"  1 
HETATM 10590 C  "C5'"  . GNP I 3 .   ? 29.374  13.655  40.344  1.00 42.59  ? 201 GNP C "C5'"  1 
HETATM 10591 C  "C4'"  . GNP I 3 .   ? 30.317  12.490  40.572  1.00 39.73  ? 201 GNP C "C4'"  1 
HETATM 10592 O  "O4'"  . GNP I 3 .   ? 29.660  11.636  41.526  1.00 43.33  ? 201 GNP C "O4'"  1 
HETATM 10593 C  "C3'"  . GNP I 3 .   ? 30.444  11.643  39.302  1.00 43.41  ? 201 GNP C "C3'"  1 
HETATM 10594 O  "O3'"  . GNP I 3 .   ? 31.724  11.021  39.389  1.00 39.37  ? 201 GNP C "O3'"  1 
HETATM 10595 C  "C2'"  . GNP I 3 .   ? 29.371  10.577  39.499  1.00 40.00  ? 201 GNP C "C2'"  1 
HETATM 10596 O  "O2'"  . GNP I 3 .   ? 29.836  9.366   38.901  1.00 42.44  ? 201 GNP C "O2'"  1 
HETATM 10597 C  "C1'"  . GNP I 3 .   ? 29.495  10.348  40.995  1.00 41.47  ? 201 GNP C "C1'"  1 
HETATM 10598 N  N9     . GNP I 3 .   ? 28.240  9.830   41.567  1.00 43.10  ? 201 GNP C N9     1 
HETATM 10599 C  C8     . GNP I 3 .   ? 26.963  10.234  41.257  1.00 43.19  ? 201 GNP C C8     1 
HETATM 10600 N  N7     . GNP I 3 .   ? 26.040  9.591   41.942  1.00 42.63  ? 201 GNP C N7     1 
HETATM 10601 C  C5     . GNP I 3 .   ? 26.749  8.736   42.761  1.00 41.58  ? 201 GNP C C5     1 
HETATM 10602 C  C6     . GNP I 3 .   ? 26.302  7.792   43.759  1.00 42.93  ? 201 GNP C C6     1 
HETATM 10603 O  O6     . GNP I 3 .   ? 25.144  7.535   44.080  1.00 46.08  ? 201 GNP C O6     1 
HETATM 10604 N  N1     . GNP I 3 .   ? 27.354  7.130   44.351  1.00 41.29  ? 201 GNP C N1     1 
HETATM 10605 C  C2     . GNP I 3 .   ? 28.678  7.333   44.066  1.00 47.25  ? 201 GNP C C2     1 
HETATM 10606 N  N2     . GNP I 3 .   ? 29.564  6.604   44.761  1.00 41.88  ? 201 GNP C N2     1 
HETATM 10607 N  N3     . GNP I 3 .   ? 29.110  8.207   43.153  1.00 42.48  ? 201 GNP C N3     1 
HETATM 10608 C  C4     . GNP I 3 .   ? 28.104  8.872   42.549  1.00 42.22  ? 201 GNP C C4     1 
HETATM 10609 H  HNB3   . GNP I 3 .   ? 28.358  17.905  39.265  1.00 49.91  ? 201 GNP C HNB3   1 
HETATM 10610 H  "H5'2" . GNP I 3 .   ? 29.020  13.959  41.195  1.00 51.15  ? 201 GNP C "H5'2" 1 
HETATM 10611 H  "H5'1" . GNP I 3 .   ? 29.852  14.382  39.914  1.00 51.15  ? 201 GNP C "H5'1" 1 
HETATM 10612 H  "H4'"  . GNP I 3 .   ? 31.191  12.752  40.902  1.00 47.71  ? 201 GNP C "H4'"  1 
HETATM 10613 H  "H3'"  . GNP I 3 .   ? 30.280  12.150  38.490  1.00 52.13  ? 201 GNP C "H3'"  1 
HETATM 10614 H  "HO3'" . GNP I 3 .   ? 31.753  10.360  38.857  1.00 47.27  ? 201 GNP C "HO3'" 1 
HETATM 10615 H  "H2'"  . GNP I 3 .   ? 28.493  10.876  39.214  1.00 48.03  ? 201 GNP C "H2'"  1 
HETATM 10616 H  "HO2'" . GNP I 3 .   ? 29.441  8.705   39.258  1.00 50.97  ? 201 GNP C "HO2'" 1 
HETATM 10617 H  "H1'"  . GNP I 3 .   ? 30.243  9.768   41.205  1.00 49.80  ? 201 GNP C "H1'"  1 
HETATM 10618 H  H8     . GNP I 3 .   ? 26.771  10.892  40.629  1.00 51.86  ? 201 GNP C H8     1 
HETATM 10619 H  HN1    . GNP I 3 .   ? 27.164  6.542   44.948  1.00 49.58  ? 201 GNP C HN1    1 
HETATM 10620 H  HN21   . GNP I 3 .   ? 29.291  6.069   45.376  1.00 50.29  ? 201 GNP C HN21   1 
HETATM 10621 H  HN22   . GNP I 3 .   ? 30.407  6.678   44.602  1.00 50.29  ? 201 GNP C HN22   1 
HETATM 10622 MG MG     . MG  J 4 .   ? 25.643  17.728  36.387  1.00 35.06  ? 202 MG  C MG     1 
HETATM 10623 O  O      . HOH K 6 .   ? 1.983   29.236  2.622   1.00 72.78  ? 301 HOH A O      1 
HETATM 10624 O  O      . HOH K 6 .   ? 27.640  38.243  7.307   1.00 45.88  ? 302 HOH A O      1 
HETATM 10625 O  O      . HOH K 6 .   ? 2.034   26.185  6.052   1.00 40.80  ? 303 HOH A O      1 
HETATM 10626 O  O      . HOH K 6 .   ? 2.036   27.915  8.551   1.00 38.53  ? 304 HOH A O      1 
HETATM 10627 O  O      . HOH K 6 .   ? -1.342  44.106  11.359  1.00 46.53  ? 305 HOH A O      1 
HETATM 10628 O  O      . HOH K 6 .   ? 6.286   24.032  8.126   1.00 41.77  ? 306 HOH A O      1 
HETATM 10629 O  O      . HOH K 6 .   ? 8.381   40.642  23.594  1.00 40.46  ? 307 HOH A O      1 
HETATM 10630 O  O      . HOH K 6 .   ? 16.614  23.959  -3.119  1.00 36.18  ? 308 HOH A O      1 
HETATM 10631 O  O      . HOH K 6 .   ? 0.465   28.594  6.415   1.00 43.51  ? 309 HOH A O      1 
HETATM 10632 O  O      . HOH K 6 .   ? 20.682  22.998  11.704  1.00 38.77  ? 310 HOH A O      1 
HETATM 10633 O  O      . HOH K 6 .   ? 10.475  32.348  21.615  1.00 31.33  ? 311 HOH A O      1 
HETATM 10634 O  O      . HOH K 6 .   ? 2.292   28.315  0.722   1.00 47.97  ? 312 HOH A O      1 
HETATM 10635 O  O      . HOH K 6 .   ? 18.755  39.995  -7.062  1.00 43.33  ? 313 HOH A O      1 
HETATM 10636 O  O      . HOH K 6 .   ? 7.311   25.900  20.528  1.00 39.90  ? 314 HOH A O      1 
HETATM 10637 O  O      . HOH K 6 .   ? -4.636  19.778  16.156  1.00 45.34  ? 315 HOH A O      1 
HETATM 10638 O  O      . HOH K 6 .   ? 22.494  14.408  1.060   1.00 35.14  ? 316 HOH A O      1 
HETATM 10639 O  O      . HOH K 6 .   ? 17.154  17.452  10.979  1.00 35.39  ? 317 HOH A O      1 
HETATM 10640 O  O      . HOH K 6 .   ? 11.676  26.437  9.868   1.00 20.35  ? 318 HOH A O      1 
HETATM 10641 O  O      . HOH K 6 .   ? 20.809  49.634  16.034  1.00 43.20  ? 319 HOH A O      1 
HETATM 10642 O  O      . HOH K 6 .   ? 11.720  16.933  8.747   1.00 24.77  ? 320 HOH A O      1 
HETATM 10643 O  O      . HOH K 6 .   ? 23.996  46.653  8.452   1.00 44.59  ? 321 HOH A O      1 
HETATM 10644 O  O      . HOH K 6 .   ? 7.735   25.117  18.148  1.00 38.91  ? 322 HOH A O      1 
HETATM 10645 O  O      . HOH K 6 .   ? 2.576   25.973  12.985  1.00 35.28  ? 323 HOH A O      1 
HETATM 10646 O  O      . HOH K 6 .   ? 16.758  24.624  11.689  1.00 26.20  ? 324 HOH A O      1 
HETATM 10647 O  O      . HOH K 6 .   ? 20.017  36.362  -5.710  1.00 32.30  ? 325 HOH A O      1 
HETATM 10648 O  O      . HOH K 6 .   ? 3.129   25.327  15.760  1.00 39.16  ? 326 HOH A O      1 
HETATM 10649 O  O      . HOH K 6 .   ? 18.278  30.182  -8.491  1.00 33.65  ? 327 HOH A O      1 
HETATM 10650 O  O      . HOH K 6 .   ? 18.639  21.927  16.789  1.00 40.93  ? 328 HOH A O      1 
HETATM 10651 O  O      . HOH K 6 .   ? -0.547  33.181  -7.635  1.00 50.43  ? 329 HOH A O      1 
HETATM 10652 O  O      . HOH K 6 .   ? 18.596  46.834  22.789  1.00 47.13  ? 330 HOH A O      1 
HETATM 10653 O  O      . HOH K 6 .   ? 17.615  42.621  -0.743  1.00 32.63  ? 331 HOH A O      1 
HETATM 10654 O  O      . HOH K 6 .   ? 33.118  39.260  20.720  1.00 32.81  ? 332 HOH A O      1 
HETATM 10655 O  O      . HOH K 6 .   ? 3.155   16.254  12.055  1.00 19.88  ? 333 HOH A O      1 
HETATM 10656 O  O      . HOH K 6 .   ? 25.512  35.680  7.255   1.00 32.14  ? 334 HOH A O      1 
HETATM 10657 O  O      . HOH K 6 .   ? 17.497  47.296  5.103   1.00 48.37  ? 335 HOH A O      1 
HETATM 10658 O  O      . HOH K 6 .   ? 27.352  31.097  15.763  1.00 24.06  ? 336 HOH A O      1 
HETATM 10659 O  O      . HOH K 6 .   ? 4.464   32.865  5.134   1.00 26.59  ? 337 HOH A O      1 
HETATM 10660 O  O      . HOH K 6 .   ? 15.243  22.338  4.696   1.00 24.99  ? 338 HOH A O      1 
HETATM 10661 O  O      . HOH K 6 .   ? -1.949  43.024  27.907  1.00 47.24  ? 339 HOH A O      1 
HETATM 10662 O  O      . HOH K 6 .   ? 9.699   42.591  21.988  1.00 37.21  ? 340 HOH A O      1 
HETATM 10663 O  O      . HOH K 6 .   ? 17.081  42.347  23.981  1.00 38.78  ? 341 HOH A O      1 
HETATM 10664 O  O      . HOH K 6 .   ? 26.861  33.829  7.684   1.00 31.60  ? 342 HOH A O      1 
HETATM 10665 O  O      . HOH K 6 .   ? 28.365  45.430  10.892  1.00 40.68  ? 343 HOH A O      1 
HETATM 10666 O  O      . HOH K 6 .   ? 18.094  48.119  8.678   1.00 38.04  ? 344 HOH A O      1 
HETATM 10667 O  O      . HOH K 6 .   ? 25.863  37.792  10.221  1.00 32.65  ? 345 HOH A O      1 
HETATM 10668 O  O      . HOH K 6 .   ? 12.849  23.413  7.130   1.00 20.16  ? 346 HOH A O      1 
HETATM 10669 O  O      . HOH K 6 .   ? 23.707  38.674  3.134   1.00 25.70  ? 347 HOH A O      1 
HETATM 10670 O  O      . HOH K 6 .   ? 28.483  45.501  26.441  1.00 61.33  ? 348 HOH A O      1 
HETATM 10671 O  O      . HOH K 6 .   ? 13.769  20.459  13.972  1.00 24.67  ? 349 HOH A O      1 
HETATM 10672 O  O      . HOH K 6 .   ? 15.525  29.572  21.713  1.00 40.55  ? 350 HOH A O      1 
HETATM 10673 O  O      . HOH K 6 .   ? 5.295   25.140  19.613  1.00 41.62  ? 351 HOH A O      1 
HETATM 10674 O  O      . HOH K 6 .   ? 20.809  27.558  4.088   1.00 18.99  ? 352 HOH A O      1 
HETATM 10675 O  O      . HOH K 6 .   ? 18.849  17.150  7.700   1.00 41.57  ? 353 HOH A O      1 
HETATM 10676 O  O      . HOH K 6 .   ? 14.850  33.483  20.051  1.00 25.96  ? 354 HOH A O      1 
HETATM 10677 O  O      . HOH K 6 .   ? 28.668  41.058  12.184  1.00 41.69  ? 355 HOH A O      1 
HETATM 10678 O  O      . HOH K 6 .   ? -5.476  44.042  14.690  1.00 53.46  ? 356 HOH A O      1 
HETATM 10679 O  O      . HOH K 6 .   ? 14.996  22.269  10.097  1.00 30.46  ? 357 HOH A O      1 
HETATM 10680 O  O      . HOH K 6 .   ? 8.184   28.556  -2.791  1.00 33.57  ? 358 HOH A O      1 
HETATM 10681 O  O      . HOH K 6 .   ? -4.256  34.693  12.835  1.00 41.73  ? 359 HOH A O      1 
HETATM 10682 O  O      . HOH K 6 .   ? 28.027  31.615  13.118  1.00 23.75  ? 360 HOH A O      1 
HETATM 10683 O  O      . HOH K 6 .   ? 13.038  16.106  1.437   1.00 26.02  ? 361 HOH A O      1 
HETATM 10684 O  O      . HOH K 6 .   ? 14.470  25.081  20.354  1.00 39.45  ? 362 HOH A O      1 
HETATM 10685 O  O      . HOH K 6 .   ? 19.825  18.312  4.669   1.00 37.42  ? 363 HOH A O      1 
HETATM 10686 O  O      . HOH K 6 .   ? 14.796  15.160  9.726   1.00 24.39  ? 364 HOH A O      1 
HETATM 10687 O  O      . HOH K 6 .   ? 21.328  20.796  1.562   1.00 49.62  ? 365 HOH A O      1 
HETATM 10688 O  O      . HOH K 6 .   ? 29.869  26.079  6.950   1.00 32.37  ? 366 HOH A O      1 
HETATM 10689 O  O      . HOH K 6 .   ? -3.779  32.669  3.698   1.00 41.18  ? 367 HOH A O      1 
HETATM 10690 O  O      . HOH K 6 .   ? 7.666   21.988  9.513   1.00 32.06  ? 368 HOH A O      1 
HETATM 10691 O  O      . HOH K 6 .   ? 29.196  47.636  12.269  1.00 44.65  ? 369 HOH A O      1 
HETATM 10692 O  O      . HOH K 6 .   ? 21.779  45.831  7.854   1.00 35.00  ? 370 HOH A O      1 
HETATM 10693 O  O      . HOH K 6 .   ? 4.453   45.545  14.329  1.00 41.79  ? 371 HOH A O      1 
HETATM 10694 O  O      . HOH K 6 .   ? 14.791  20.052  -2.008  1.00 47.77  ? 372 HOH A O      1 
HETATM 10695 O  O      . HOH K 6 .   ? 6.160   46.821  14.213  1.00 42.39  ? 373 HOH A O      1 
HETATM 10696 O  O      . HOH K 6 .   ? -2.894  46.057  23.896  1.00 41.06  ? 374 HOH A O      1 
HETATM 10697 O  O      . HOH K 6 .   ? 23.379  45.542  21.202  1.00 41.30  ? 375 HOH A O      1 
HETATM 10698 O  O      . HOH K 6 .   ? 8.211   25.251  15.919  1.00 23.75  ? 376 HOH A O      1 
HETATM 10699 O  O      . HOH K 6 .   ? 8.916   46.470  13.276  1.00 35.29  ? 377 HOH A O      1 
HETATM 10700 O  O      . HOH K 6 .   ? 22.330  41.167  3.589   1.00 24.54  ? 378 HOH A O      1 
HETATM 10701 O  O      . HOH K 6 .   ? 1.032   22.479  7.255   1.00 40.83  ? 379 HOH A O      1 
HETATM 10702 O  O      . HOH K 6 .   ? 22.410  25.526  18.153  1.00 27.41  ? 380 HOH A O      1 
HETATM 10703 O  O      . HOH K 6 .   ? 6.194   29.492  11.459  1.00 22.90  ? 381 HOH A O      1 
HETATM 10704 O  O      . HOH K 6 .   ? 11.261  48.648  4.163   1.00 42.08  ? 382 HOH A O      1 
HETATM 10705 O  O      . HOH K 6 .   ? 24.021  27.941  17.018  1.00 26.94  ? 383 HOH A O      1 
HETATM 10706 O  O      . HOH K 6 .   ? -1.056  38.837  3.948   1.00 36.03  ? 384 HOH A O      1 
HETATM 10707 O  O      . HOH K 6 .   ? 26.144  47.153  10.877  1.00 38.73  ? 385 HOH A O      1 
HETATM 10708 O  O      . HOH K 6 .   ? 30.183  35.206  14.284  1.00 33.19  ? 386 HOH A O      1 
HETATM 10709 O  O      . HOH K 6 .   ? 26.100  30.328  0.117   1.00 33.41  ? 387 HOH A O      1 
HETATM 10710 O  O      . HOH K 6 .   ? 28.367  32.281  9.747   1.00 35.09  ? 388 HOH A O      1 
HETATM 10711 O  O      . HOH K 6 .   ? 20.298  33.285  27.689  1.00 36.75  ? 389 HOH A O      1 
HETATM 10712 O  O      . HOH K 6 .   ? 24.530  37.912  27.098  1.00 41.51  ? 390 HOH A O      1 
HETATM 10713 O  O      . HOH K 6 .   ? 10.249  27.092  -5.339  1.00 37.80  ? 391 HOH A O      1 
HETATM 10714 O  O      . HOH K 6 .   ? 1.927   31.196  -6.296  1.00 43.34  ? 392 HOH A O      1 
HETATM 10715 O  O      . HOH K 6 .   ? 12.536  37.368  -8.844  1.00 42.98  ? 393 HOH A O      1 
HETATM 10716 O  O      . HOH K 6 .   ? 9.196   24.959  -1.097  1.00 43.34  ? 394 HOH A O      1 
HETATM 10717 O  O      . HOH K 6 .   ? 20.467  40.536  27.075  1.00 40.51  ? 395 HOH A O      1 
HETATM 10718 O  O      . HOH K 6 .   ? 18.041  23.166  17.902  1.00 32.86  ? 396 HOH A O      1 
HETATM 10719 O  O      . HOH K 6 .   ? 7.901   42.503  -8.580  1.00 45.06  ? 397 HOH A O      1 
HETATM 10720 O  O      . HOH K 6 .   ? 16.965  39.058  25.541  1.00 37.59  ? 398 HOH A O      1 
HETATM 10721 O  O      . HOH K 6 .   ? 14.842  44.548  -0.305  1.00 35.98  ? 399 HOH A O      1 
HETATM 10722 O  O      . HOH K 6 .   ? 23.115  41.118  0.185   1.00 29.62  ? 400 HOH A O      1 
HETATM 10723 O  O      . HOH K 6 .   ? -1.265  28.988  9.372   1.00 51.76  ? 401 HOH A O      1 
HETATM 10724 O  O      . HOH K 6 .   ? -1.877  30.748  10.294  1.00 52.67  ? 402 HOH A O      1 
HETATM 10725 O  O      . HOH K 6 .   ? 5.290   18.258  6.176   1.00 39.18  ? 403 HOH A O      1 
HETATM 10726 O  O      . HOH K 6 .   ? 26.154  26.878  -0.276  1.00 42.36  ? 404 HOH A O      1 
HETATM 10727 O  O      . HOH K 6 .   ? 12.416  26.341  -3.886  1.00 30.86  ? 405 HOH A O      1 
HETATM 10728 O  O      . HOH K 6 .   ? 10.557  29.722  22.813  1.00 37.11  ? 406 HOH A O      1 
HETATM 10729 O  O      . HOH K 6 .   ? 10.547  27.075  22.510  1.00 39.19  ? 407 HOH A O      1 
HETATM 10730 O  O      . HOH K 6 .   ? 15.965  41.250  -5.954  1.00 47.53  ? 408 HOH A O      1 
HETATM 10731 O  O      . HOH K 6 .   ? 19.756  28.895  21.324  1.00 31.54  ? 409 HOH A O      1 
HETATM 10732 O  O      . HOH K 6 .   ? 31.160  39.628  16.802  1.00 42.38  ? 410 HOH A O      1 
HETATM 10733 O  O      . HOH K 6 .   ? 23.607  30.583  -5.474  1.00 39.30  ? 411 HOH A O      1 
HETATM 10734 O  O      . HOH K 6 .   ? 17.549  23.372  19.427  1.00 34.14  ? 412 HOH A O      1 
HETATM 10735 O  O      . HOH K 6 .   ? 14.810  22.937  19.885  1.00 37.73  ? 413 HOH A O      1 
HETATM 10736 O  O      . HOH K 6 .   ? 11.332  37.923  -10.382 1.00 49.07  ? 414 HOH A O      1 
HETATM 10737 O  O      . HOH K 6 .   ? 6.827   28.167  -0.429  1.00 43.83  ? 415 HOH A O      1 
HETATM 10738 O  O      . HOH K 6 .   ? -2.442  20.567  17.581  1.00 42.59  ? 416 HOH A O      1 
HETATM 10739 O  O      . HOH K 6 .   ? 13.940  19.012  11.371  1.00 40.02  ? 417 HOH A O      1 
HETATM 10740 O  O      . HOH K 6 .   ? 29.601  35.152  7.954   1.00 40.30  ? 418 HOH A O      1 
HETATM 10741 O  O      . HOH K 6 .   ? 22.751  36.179  27.011  1.00 38.81  ? 419 HOH A O      1 
HETATM 10742 O  O      . HOH K 6 .   ? 1.161   27.446  22.802  1.00 43.02  ? 420 HOH A O      1 
HETATM 10743 O  O      . HOH K 6 .   ? -0.495  20.805  8.443   1.00 46.21  ? 421 HOH A O      1 
HETATM 10744 O  O      . HOH K 6 .   ? 27.001  21.474  5.561   1.00 44.45  ? 422 HOH A O      1 
HETATM 10745 O  O      . HOH K 6 .   ? 18.994  25.371  -9.955  1.00 44.52  ? 423 HOH A O      1 
HETATM 10746 O  O      . HOH K 6 .   ? 1.552   25.770  -1.244  1.00 53.06  ? 424 HOH A O      1 
HETATM 10747 O  O      . HOH K 6 .   ? 3.704   38.200  -11.683 1.00 51.07  ? 425 HOH A O      1 
HETATM 10748 O  O      . HOH K 6 .   ? -2.243  29.895  7.620   1.00 50.47  ? 426 HOH A O      1 
HETATM 10749 O  O      . HOH K 6 .   ? 12.203  46.492  -0.813  1.00 54.65  ? 427 HOH A O      1 
HETATM 10750 O  O      . HOH K 6 .   ? 17.836  37.789  -8.899  1.00 43.48  ? 428 HOH A O      1 
HETATM 10751 O  O      . HOH K 6 .   ? 13.194  54.532  18.513  1.00 58.81  ? 429 HOH A O      1 
HETATM 10752 O  O      . HOH K 6 .   ? 14.920  31.853  23.647  1.00 44.24  ? 430 HOH A O      1 
HETATM 10753 O  O      . HOH K 6 .   ? -7.177  34.934  21.199  1.00 47.52  ? 431 HOH A O      1 
HETATM 10754 O  O      . HOH K 6 .   ? 4.009   19.991  5.223   1.00 49.16  ? 432 HOH A O      1 
HETATM 10755 O  O      . HOH K 6 .   ? 18.103  52.329  18.118  1.00 53.32  ? 433 HOH A O      1 
HETATM 10756 O  O      . HOH K 6 .   ? 21.608  51.320  9.326   1.00 43.70  ? 434 HOH A O      1 
HETATM 10757 O  O      . HOH K 6 .   ? 5.045   27.205  -5.695  1.00 44.67  ? 435 HOH A O      1 
HETATM 10758 O  O      . HOH K 6 .   ? 32.716  37.691  16.154  1.00 43.38  ? 436 HOH A O      1 
HETATM 10759 O  O      . HOH K 6 .   ? 28.930  23.782  7.430   1.00 41.15  ? 437 HOH A O      1 
HETATM 10760 O  O      . HOH K 6 .   ? 20.348  42.502  -6.568  1.00 53.61  ? 438 HOH A O      1 
HETATM 10761 O  O      . HOH K 6 .   ? 20.510  31.325  -7.958  1.00 35.75  ? 439 HOH A O      1 
HETATM 10762 O  O      . HOH K 6 .   ? 12.817  33.421  21.706  1.00 33.28  ? 440 HOH A O      1 
HETATM 10763 O  O      . HOH K 6 .   ? 17.024  22.932  9.321   1.00 30.64  ? 441 HOH A O      1 
HETATM 10764 O  O      . HOH K 6 .   ? 20.465  22.837  16.042  1.00 46.76  ? 442 HOH A O      1 
HETATM 10765 O  O      . HOH K 6 .   ? 23.709  44.564  6.588   1.00 44.69  ? 443 HOH A O      1 
HETATM 10766 O  O      . HOH K 6 .   ? 16.919  22.629  6.653   1.00 34.51  ? 444 HOH A O      1 
HETATM 10767 O  O      . HOH K 6 .   ? 13.571  33.015  24.335  1.00 47.65  ? 445 HOH A O      1 
HETATM 10768 O  O      . HOH K 6 .   ? -3.177  30.521  -3.693  1.00 48.90  ? 446 HOH A O      1 
HETATM 10769 O  O      . HOH K 6 .   ? 11.310  28.393  -10.411 1.00 46.21  ? 447 HOH A O      1 
HETATM 10770 O  O      . HOH K 6 .   ? 26.151  47.439  27.035  1.00 64.68  ? 448 HOH A O      1 
HETATM 10771 O  O      . HOH K 6 .   ? 33.085  41.305  22.191  1.00 37.26  ? 449 HOH A O      1 
HETATM 10772 O  O      . HOH K 6 .   ? 13.504  45.644  -2.501  1.00 54.79  ? 450 HOH A O      1 
HETATM 10773 O  O      . HOH K 6 .   ? 20.322  36.702  -8.038  1.00 36.46  ? 451 HOH A O      1 
HETATM 10774 O  O      . HOH K 6 .   ? 13.202  29.715  22.882  1.00 47.57  ? 452 HOH A O      1 
HETATM 10775 O  O      . HOH K 6 .   ? 27.415  24.318  0.143   1.00 39.65  ? 453 HOH A O      1 
HETATM 10776 O  O      . HOH K 6 .   ? 1.561   25.266  -5.509  1.00 51.09  ? 454 HOH A O      1 
HETATM 10777 O  O      . HOH K 6 .   ? -0.321  27.875  29.699  1.00 47.41  ? 455 HOH A O      1 
HETATM 10778 O  O      . HOH K 6 .   ? 24.463  43.096  -1.368  1.00 34.46  ? 456 HOH A O      1 
HETATM 10779 O  O      . HOH K 6 .   ? -1.306  36.139  29.715  1.00 59.32  ? 457 HOH A O      1 
HETATM 10780 O  O      . HOH K 6 .   ? -3.125  35.380  29.497  1.00 61.34  ? 458 HOH A O      1 
HETATM 10781 O  O      . HOH K 6 .   ? 20.230  46.862  -2.548  1.00 62.13  ? 459 HOH A O      1 
HETATM 10782 O  O      . HOH K 6 .   ? 25.995  43.236  1.959   1.00 42.38  ? 460 HOH A O      1 
HETATM 10783 O  O      . HOH K 6 .   ? 26.476  20.290  -4.347  1.00 49.50  ? 461 HOH A O      1 
HETATM 10784 O  O      . HOH K 6 .   ? -12.495 37.428  1.716   1.00 40.60  ? 462 HOH A O      1 
HETATM 10785 O  O      . HOH L 6 .   ? 14.364  7.098   -6.733  1.00 33.29  ? 301 HOH B O      1 
HETATM 10786 O  O      . HOH L 6 .   ? 18.273  0.460   30.508  1.00 40.70  ? 302 HOH B O      1 
HETATM 10787 O  O      . HOH L 6 .   ? 9.590   -0.455  28.584  1.00 37.74  ? 303 HOH B O      1 
HETATM 10788 O  O      . HOH L 6 .   ? -8.188  7.887   8.528   1.00 38.31  ? 304 HOH B O      1 
HETATM 10789 O  O      . HOH L 6 .   ? -12.437 6.647   8.963   1.00 39.38  ? 305 HOH B O      1 
HETATM 10790 O  O      . HOH L 6 .   ? 8.252   11.933  1.702   1.00 30.31  ? 306 HOH B O      1 
HETATM 10791 O  O      . HOH L 6 .   ? 24.130  -3.161  9.659   1.00 37.79  ? 307 HOH B O      1 
HETATM 10792 O  O      . HOH L 6 .   ? 12.671  3.801   -6.250  1.00 30.87  ? 308 HOH B O      1 
HETATM 10793 O  O      . HOH L 6 .   ? 10.169  -8.288  -4.870  1.00 41.67  ? 309 HOH B O      1 
HETATM 10794 O  O      . HOH L 6 .   ? 16.872  8.465   -3.921  1.00 36.33  ? 310 HOH B O      1 
HETATM 10795 O  O      . HOH L 6 .   ? 7.741   8.002   3.645   1.00 16.81  ? 311 HOH B O      1 
HETATM 10796 O  O      . HOH L 6 .   ? 12.047  -7.315  24.191  1.00 31.97  ? 312 HOH B O      1 
HETATM 10797 O  O      . HOH L 6 .   ? 1.341   8.720   4.158   1.00 21.55  ? 313 HOH B O      1 
HETATM 10798 O  O      . HOH L 6 .   ? 1.053   14.800  6.071   1.00 38.16  ? 314 HOH B O      1 
HETATM 10799 O  O      . HOH L 6 .   ? 16.227  14.577  14.342  1.00 26.67  ? 315 HOH B O      1 
HETATM 10800 O  O      . HOH L 6 .   ? 1.931   16.733  -2.097  1.00 34.56  ? 316 HOH B O      1 
HETATM 10801 O  O      . HOH L 6 .   ? 2.049   15.371  9.562   1.00 22.79  ? 317 HOH B O      1 
HETATM 10802 O  O      . HOH L 6 .   ? -4.639  -7.098  0.027   1.00 33.52  ? 318 HOH B O      1 
HETATM 10803 O  O      . HOH L 6 .   ? 14.622  -3.813  -1.180  1.00 30.41  ? 319 HOH B O      1 
HETATM 10804 O  O      . HOH L 6 .   ? -3.943  0.757   19.354  1.00 32.01  ? 320 HOH B O      1 
HETATM 10805 O  O      . HOH L 6 .   ? -4.217  4.840   7.381   1.00 18.51  ? 321 HOH B O      1 
HETATM 10806 O  O      . HOH L 6 .   ? 3.808   -7.768  0.810   1.00 29.40  ? 322 HOH B O      1 
HETATM 10807 O  O      . HOH L 6 .   ? 24.496  -0.727  13.774  1.00 35.01  ? 323 HOH B O      1 
HETATM 10808 O  O      . HOH L 6 .   ? 1.895   11.039  1.516   1.00 17.08  ? 324 HOH B O      1 
HETATM 10809 O  O      . HOH L 6 .   ? 17.700  11.320  26.948  1.00 46.50  ? 325 HOH B O      1 
HETATM 10810 O  O      . HOH L 6 .   ? 24.055  2.091   16.351  1.00 27.21  ? 326 HOH B O      1 
HETATM 10811 O  O      . HOH L 6 .   ? 6.697   -12.948 6.700   1.00 38.98  ? 327 HOH B O      1 
HETATM 10812 O  O      . HOH L 6 .   ? 17.306  10.222  -1.918  1.00 29.96  ? 328 HOH B O      1 
HETATM 10813 O  O      . HOH L 6 .   ? -0.318  3.646   -3.036  1.00 31.11  ? 329 HOH B O      1 
HETATM 10814 O  O      . HOH L 6 .   ? 19.793  6.731   8.060   1.00 24.86  ? 330 HOH B O      1 
HETATM 10815 O  O      . HOH L 6 .   ? -10.088 1.902   10.966  1.00 39.51  ? 331 HOH B O      1 
HETATM 10816 O  O      . HOH L 6 .   ? -6.431  2.451   -2.778  1.00 30.21  ? 332 HOH B O      1 
HETATM 10817 O  O      . HOH L 6 .   ? 13.029  12.556  -0.018  1.00 29.35  ? 333 HOH B O      1 
HETATM 10818 O  O      . HOH L 6 .   ? 2.992   -3.782  -4.718  1.00 27.34  ? 334 HOH B O      1 
HETATM 10819 O  O      . HOH L 6 .   ? -9.687  9.891   13.964  1.00 37.38  ? 335 HOH B O      1 
HETATM 10820 O  O      . HOH L 6 .   ? 18.666  12.167  24.637  1.00 32.43  ? 336 HOH B O      1 
HETATM 10821 O  O      . HOH L 6 .   ? 12.028  -1.628  -7.008  1.00 37.75  ? 337 HOH B O      1 
HETATM 10822 O  O      . HOH L 6 .   ? 19.001  12.588  15.416  1.00 23.90  ? 338 HOH B O      1 
HETATM 10823 O  O      . HOH L 6 .   ? -4.952  -0.870  -2.139  1.00 32.91  ? 339 HOH B O      1 
HETATM 10824 O  O      . HOH L 6 .   ? 4.005   1.450   24.760  1.00 29.82  ? 340 HOH B O      1 
HETATM 10825 O  O      . HOH L 6 .   ? 14.470  11.097  -1.248  1.00 30.29  ? 341 HOH B O      1 
HETATM 10826 O  O      . HOH L 6 .   ? 7.131   -8.986  -4.287  1.00 45.23  ? 342 HOH B O      1 
HETATM 10827 O  O      . HOH L 6 .   ? 20.916  -1.209  3.311   1.00 28.50  ? 343 HOH B O      1 
HETATM 10828 O  O      . HOH L 6 .   ? 19.991  -4.622  0.083   1.00 40.31  ? 344 HOH B O      1 
HETATM 10829 O  O      . HOH L 6 .   ? 1.519   12.180  23.794  1.00 31.89  ? 345 HOH B O      1 
HETATM 10830 O  O      . HOH L 6 .   ? 13.789  15.837  14.471  1.00 21.93  ? 346 HOH B O      1 
HETATM 10831 O  O      . HOH L 6 .   ? 16.268  -2.796  -8.085  1.00 38.83  ? 347 HOH B O      1 
HETATM 10832 O  O      . HOH L 6 .   ? -6.841  7.463   16.149  1.00 26.38  ? 348 HOH B O      1 
HETATM 10833 O  O      . HOH L 6 .   ? 5.774   1.350   2.919   1.00 20.39  ? 349 HOH B O      1 
HETATM 10834 O  O      . HOH L 6 .   ? 19.910  8.055   15.788  1.00 19.62  ? 350 HOH B O      1 
HETATM 10835 O  O      . HOH L 6 .   ? 20.306  -5.750  17.956  1.00 28.18  ? 351 HOH B O      1 
HETATM 10836 O  O      . HOH L 6 .   ? -1.391  12.530  3.091   1.00 25.49  ? 352 HOH B O      1 
HETATM 10837 O  O      . HOH L 6 .   ? 8.467   9.954   -6.971  1.00 30.61  ? 353 HOH B O      1 
HETATM 10838 O  O      . HOH L 6 .   ? 5.709   5.728   -7.637  1.00 32.25  ? 354 HOH B O      1 
HETATM 10839 O  O      . HOH L 6 .   ? 15.915  3.717   9.623   1.00 22.38  ? 355 HOH B O      1 
HETATM 10840 O  O      . HOH L 6 .   ? 21.684  2.600   2.409   1.00 26.92  ? 356 HOH B O      1 
HETATM 10841 O  O      . HOH L 6 .   ? 15.491  18.384  12.322  1.00 39.56  ? 357 HOH B O      1 
HETATM 10842 O  O      . HOH L 6 .   ? 7.969   -6.152  -5.053  1.00 37.88  ? 358 HOH B O      1 
HETATM 10843 O  O      . HOH L 6 .   ? 16.518  7.754   8.826   1.00 19.51  ? 359 HOH B O      1 
HETATM 10844 O  O      . HOH L 6 .   ? -3.883  11.652  -0.542  1.00 28.02  ? 360 HOH B O      1 
HETATM 10845 O  O      . HOH L 6 .   ? 1.390   -6.694  0.151   1.00 28.65  ? 361 HOH B O      1 
HETATM 10846 O  O      . HOH L 6 .   ? 4.498   3.621   24.653  1.00 31.71  ? 362 HOH B O      1 
HETATM 10847 O  O      . HOH L 6 .   ? 19.150  -1.409  -6.733  1.00 41.30  ? 363 HOH B O      1 
HETATM 10848 O  O      . HOH L 6 .   ? -1.837  0.186   21.057  1.00 33.57  ? 364 HOH B O      1 
HETATM 10849 O  O      . HOH L 6 .   ? 0.465   4.656   0.705   1.00 20.80  ? 365 HOH B O      1 
HETATM 10850 O  O      . HOH L 6 .   ? 18.668  -7.783  18.369  1.00 33.85  ? 366 HOH B O      1 
HETATM 10851 O  O      . HOH L 6 .   ? 18.592  -9.024  0.090   1.00 40.63  ? 367 HOH B O      1 
HETATM 10852 O  O      . HOH L 6 .   ? 14.884  -11.351 5.067   1.00 33.71  ? 368 HOH B O      1 
HETATM 10853 O  O      . HOH L 6 .   ? -5.040  0.846   13.238  1.00 30.75  ? 369 HOH B O      1 
HETATM 10854 O  O      . HOH L 6 .   ? 9.911   8.177   27.308  1.00 25.50  ? 370 HOH B O      1 
HETATM 10855 O  O      . HOH L 6 .   ? 5.587   22.442  21.607  1.00 44.69  ? 371 HOH B O      1 
HETATM 10856 O  O      . HOH L 6 .   ? 17.377  18.348  20.922  1.00 29.73  ? 372 HOH B O      1 
HETATM 10857 O  O      . HOH L 6 .   ? 20.332  0.505   1.090   1.00 27.83  ? 373 HOH B O      1 
HETATM 10858 O  O      . HOH L 6 .   ? 17.446  -3.736  3.996   1.00 24.31  ? 374 HOH B O      1 
HETATM 10859 O  O      . HOH L 6 .   ? 12.491  13.754  8.865   1.00 18.43  ? 375 HOH B O      1 
HETATM 10860 O  O      . HOH L 6 .   ? 1.609   -2.909  18.987  1.00 31.45  ? 376 HOH B O      1 
HETATM 10861 O  O      . HOH L 6 .   ? 10.576  14.577  0.708   1.00 33.44  ? 377 HOH B O      1 
HETATM 10862 O  O      . HOH L 6 .   ? 19.332  14.789  21.809  1.00 29.71  ? 378 HOH B O      1 
HETATM 10863 O  O      . HOH L 6 .   ? 15.243  13.458  26.479  1.00 27.20  ? 379 HOH B O      1 
HETATM 10864 O  O      . HOH L 6 .   ? 17.087  -10.217 3.678   1.00 38.80  ? 380 HOH B O      1 
HETATM 10865 O  O      . HOH L 6 .   ? 6.576   17.922  -0.346  1.00 34.75  ? 381 HOH B O      1 
HETATM 10866 O  O      . HOH L 6 .   ? -4.600  7.462   8.904   1.00 24.94  ? 382 HOH B O      1 
HETATM 10867 O  O      . HOH L 6 .   ? 11.321  8.580   2.477   1.00 18.36  ? 383 HOH B O      1 
HETATM 10868 O  O      . HOH L 6 .   ? 7.791   -8.640  23.084  1.00 35.07  ? 384 HOH B O      1 
HETATM 10869 O  O      . HOH L 6 .   ? 3.112   4.608   -7.973  1.00 35.20  ? 385 HOH B O      1 
HETATM 10870 O  O      . HOH L 6 .   ? 14.849  17.072  -0.238  1.00 28.71  ? 386 HOH B O      1 
HETATM 10871 O  O      . HOH L 6 .   ? -1.742  7.112   24.102  1.00 30.55  ? 387 HOH B O      1 
HETATM 10872 O  O      . HOH L 6 .   ? 2.541   13.996  -4.935  1.00 32.91  ? 388 HOH B O      1 
HETATM 10873 O  O      . HOH L 6 .   ? 3.613   15.847  6.582   1.00 29.26  ? 389 HOH B O      1 
HETATM 10874 O  O      . HOH L 6 .   ? 19.168  11.639  -2.759  1.00 41.32  ? 390 HOH B O      1 
HETATM 10875 O  O      . HOH L 6 .   ? 24.204  4.712   2.015   1.00 38.58  ? 391 HOH B O      1 
HETATM 10876 O  O      . HOH L 6 .   ? 7.539   -5.693  24.508  1.00 28.66  ? 392 HOH B O      1 
HETATM 10877 O  O      . HOH L 6 .   ? 24.979  10.047  24.747  1.00 40.69  ? 393 HOH B O      1 
HETATM 10878 O  O      . HOH L 6 .   ? 26.790  8.662   20.148  1.00 36.74  ? 394 HOH B O      1 
HETATM 10879 O  O      . HOH L 6 .   ? -6.867  0.519   -1.035  1.00 31.53  ? 395 HOH B O      1 
HETATM 10880 O  O      . HOH L 6 .   ? -4.700  2.325   6.241   1.00 19.30  ? 396 HOH B O      1 
HETATM 10881 O  O      . HOH L 6 .   ? 11.913  -0.419  27.767  1.00 26.62  ? 397 HOH B O      1 
HETATM 10882 O  O      . HOH L 6 .   ? 5.536   -6.172  22.097  1.00 31.82  ? 398 HOH B O      1 
HETATM 10883 O  O      . HOH L 6 .   ? 14.554  17.507  25.141  1.00 24.23  ? 399 HOH B O      1 
HETATM 10884 O  O      . HOH L 6 .   ? -1.170  6.151   17.464  1.00 27.17  ? 400 HOH B O      1 
HETATM 10885 O  O      . HOH L 6 .   ? 21.999  -0.180  -0.949  1.00 34.90  ? 401 HOH B O      1 
HETATM 10886 O  O      . HOH L 6 .   ? 25.021  -4.324  16.577  1.00 34.35  ? 402 HOH B O      1 
HETATM 10887 O  O      . HOH L 6 .   ? 21.911  2.072   5.058   1.00 31.83  ? 403 HOH B O      1 
HETATM 10888 O  O      . HOH L 6 .   ? 10.632  -4.127  -8.563  1.00 46.29  ? 404 HOH B O      1 
HETATM 10889 O  O      . HOH L 6 .   ? 12.761  -13.353 15.827  1.00 36.58  ? 405 HOH B O      1 
HETATM 10890 O  O      . HOH L 6 .   ? 18.201  -6.499  4.880   1.00 32.07  ? 406 HOH B O      1 
HETATM 10891 O  O      . HOH L 6 .   ? -8.009  1.587   12.850  1.00 30.30  ? 407 HOH B O      1 
HETATM 10892 O  O      . HOH L 6 .   ? 22.778  10.722  17.047  1.00 31.16  ? 408 HOH B O      1 
HETATM 10893 O  O      . HOH L 6 .   ? 7.845   -11.970 15.776  1.00 41.16  ? 409 HOH B O      1 
HETATM 10894 O  O      . HOH L 6 .   ? -9.081  -7.617  2.768   1.00 48.09  ? 410 HOH B O      1 
HETATM 10895 O  O      . HOH L 6 .   ? 20.418  10.661  10.739  1.00 35.55  ? 411 HOH B O      1 
HETATM 10896 O  O      . HOH L 6 .   ? 15.047  19.264  21.871  1.00 29.89  ? 412 HOH B O      1 
HETATM 10897 O  O      . HOH L 6 .   ? -7.823  4.549   19.826  1.00 41.19  ? 413 HOH B O      1 
HETATM 10898 O  O      . HOH L 6 .   ? -4.026  13.495  3.127   1.00 27.43  ? 414 HOH B O      1 
HETATM 10899 O  O      . HOH L 6 .   ? 6.421   -12.458 1.174   1.00 40.15  ? 415 HOH B O      1 
HETATM 10900 O  O      . HOH L 6 .   ? 20.303  2.321   -4.460  1.00 40.60  ? 416 HOH B O      1 
HETATM 10901 O  O      . HOH L 6 .   ? 14.376  18.763  13.721  1.00 29.46  ? 417 HOH B O      1 
HETATM 10902 O  O      . HOH L 6 .   ? 24.390  12.410  8.300   1.00 40.95  ? 418 HOH B O      1 
HETATM 10903 O  O      . HOH L 6 .   ? 19.009  6.839   -4.630  1.00 42.51  ? 419 HOH B O      1 
HETATM 10904 O  O      . HOH L 6 .   ? 24.754  -6.734  11.459  1.00 44.02  ? 420 HOH B O      1 
HETATM 10905 O  O      . HOH L 6 .   ? -2.566  3.026   -4.308  1.00 34.57  ? 421 HOH B O      1 
HETATM 10906 O  O      . HOH L 6 .   ? 18.184  -13.039 11.934  1.00 44.64  ? 422 HOH B O      1 
HETATM 10907 O  O      . HOH L 6 .   ? 13.544  5.670   -7.003  1.00 33.54  ? 423 HOH B O      1 
HETATM 10908 O  O      . HOH L 6 .   ? 4.286   9.064   -7.586  1.00 36.44  ? 424 HOH B O      1 
HETATM 10909 O  O      . HOH L 6 .   ? -0.413  15.020  3.945   1.00 40.68  ? 425 HOH B O      1 
HETATM 10910 O  O      . HOH L 6 .   ? 2.496   11.956  -6.506  1.00 32.78  ? 426 HOH B O      1 
HETATM 10911 O  O      . HOH L 6 .   ? 9.083   12.152  16.044  1.00 30.78  ? 427 HOH B O      1 
HETATM 10912 O  O      . HOH L 6 .   ? 13.950  13.739  -1.608  1.00 49.66  ? 428 HOH B O      1 
HETATM 10913 O  O      . HOH L 6 .   ? 19.105  8.870   8.746   1.00 37.66  ? 429 HOH B O      1 
HETATM 10914 O  O      . HOH L 6 .   ? -5.634  -5.500  9.691   1.00 46.15  ? 430 HOH B O      1 
HETATM 10915 O  O      . HOH L 6 .   ? 0.749   -5.244  -3.513  1.00 36.04  ? 431 HOH B O      1 
HETATM 10916 O  O      . HOH L 6 .   ? 16.864  -14.477 12.466  1.00 45.66  ? 432 HOH B O      1 
HETATM 10917 O  O      . HOH L 6 .   ? 13.680  21.400  21.769  1.00 33.55  ? 433 HOH B O      1 
HETATM 10918 O  O      . HOH L 6 .   ? 26.318  2.911   15.229  1.00 34.08  ? 434 HOH B O      1 
HETATM 10919 O  O      . HOH L 6 .   ? 25.562  -3.093  15.027  1.00 37.27  ? 435 HOH B O      1 
HETATM 10920 O  O      . HOH L 6 .   ? 24.946  10.329  18.188  1.00 47.08  ? 436 HOH B O      1 
HETATM 10921 O  O      . HOH L 6 .   ? 1.819   -2.615  21.118  1.00 39.04  ? 437 HOH B O      1 
HETATM 10922 O  O      . HOH L 6 .   ? 21.916  10.672  -2.262  1.00 48.02  ? 438 HOH B O      1 
HETATM 10923 O  O      . HOH L 6 .   ? 25.089  6.286   8.053   1.00 40.53  ? 439 HOH B O      1 
HETATM 10924 O  O      . HOH L 6 .   ? -10.558 9.790   11.082  1.00 50.36  ? 440 HOH B O      1 
HETATM 10925 O  O      . HOH L 6 .   ? 19.455  -3.468  2.343   1.00 29.18  ? 441 HOH B O      1 
HETATM 10926 O  O      . HOH L 6 .   ? 19.565  13.412  11.138  1.00 34.86  ? 442 HOH B O      1 
HETATM 10927 O  O      . HOH L 6 .   ? 8.165   -3.047  -7.682  1.00 44.18  ? 443 HOH B O      1 
HETATM 10928 O  O      . HOH L 6 .   ? 9.204   9.964   3.079   1.00 33.61  ? 444 HOH B O      1 
HETATM 10929 O  O      . HOH L 6 .   ? 21.807  15.786  21.279  1.00 36.03  ? 445 HOH B O      1 
HETATM 10930 O  O      . HOH L 6 .   ? 18.665  15.016  24.565  1.00 33.54  ? 446 HOH B O      1 
HETATM 10931 O  O      . HOH L 6 .   ? 28.461  3.717   16.511  1.00 44.90  ? 447 HOH B O      1 
HETATM 10932 O  O      . HOH L 6 .   ? 17.182  14.806  11.607  1.00 30.62  ? 448 HOH B O      1 
HETATM 10933 O  O      . HOH L 6 .   ? 4.240   -10.674 0.945   1.00 38.90  ? 449 HOH B O      1 
HETATM 10934 O  O      . HOH L 6 .   ? 13.364  1.471   28.703  1.00 34.14  ? 450 HOH B O      1 
HETATM 10935 O  O      . HOH L 6 .   ? 24.505  2.299   5.561   1.00 39.34  ? 451 HOH B O      1 
HETATM 10936 O  O      . HOH L 6 .   ? -9.605  9.922   7.318   1.00 33.62  ? 452 HOH B O      1 
HETATM 10937 O  O      . HOH L 6 .   ? 0.941   16.627  9.117   1.00 47.40  ? 453 HOH B O      1 
HETATM 10938 O  O      . HOH L 6 .   ? 24.544  -2.473  7.084   1.00 36.05  ? 454 HOH B O      1 
HETATM 10939 O  O      . HOH L 6 .   ? 20.384  -7.696  4.179   1.00 37.43  ? 455 HOH B O      1 
HETATM 10940 O  O      . HOH L 6 .   ? -4.222  -1.562  14.960  1.00 41.92  ? 456 HOH B O      1 
HETATM 10941 O  O      . HOH L 6 .   ? 23.598  2.609   25.550  1.00 40.37  ? 457 HOH B O      1 
HETATM 10942 O  O      . HOH L 6 .   ? -8.857  6.280   17.299  1.00 42.47  ? 458 HOH B O      1 
HETATM 10943 O  O      . HOH L 6 .   ? 3.009   -10.140 -2.532  1.00 51.49  ? 459 HOH B O      1 
HETATM 10944 O  O      . HOH L 6 .   ? -3.969  5.056   -5.779  1.00 46.54  ? 460 HOH B O      1 
HETATM 10945 O  O      . HOH L 6 .   ? 22.361  -7.688  14.246  1.00 42.00  ? 461 HOH B O      1 
HETATM 10946 O  O      . HOH L 6 .   ? 0.522   18.039  -3.187  1.00 41.57  ? 462 HOH B O      1 
HETATM 10947 O  O      . HOH L 6 .   ? 21.470  -8.077  -0.603  1.00 53.73  ? 463 HOH B O      1 
HETATM 10948 O  O      . HOH L 6 .   ? 25.963  -5.305  13.160  1.00 47.80  ? 464 HOH B O      1 
HETATM 10949 O  O      . HOH L 6 .   ? 21.042  9.483   13.341  1.00 50.79  ? 465 HOH B O      1 
HETATM 10950 O  O      . HOH L 6 .   ? 20.900  -6.193  2.595   1.00 36.76  ? 466 HOH B O      1 
HETATM 10951 O  O      . HOH L 6 .   ? 20.607  13.827  13.821  1.00 41.09  ? 467 HOH B O      1 
HETATM 10952 O  O      . HOH L 6 .   ? -5.059  15.977  3.505   1.00 43.66  ? 468 HOH B O      1 
HETATM 10953 O  O      . HOH L 6 .   ? 19.001  -9.897  19.868  1.00 46.99  ? 469 HOH B O      1 
HETATM 10954 O  O      . HOH L 6 .   ? -14.365 -6.351  3.194   1.00 56.50  ? 470 HOH B O      1 
HETATM 10955 O  O      . HOH L 6 .   ? 3.912   3.797   -10.915 1.00 46.81  ? 471 HOH B O      1 
HETATM 10956 O  O      . HOH L 6 .   ? -9.349  1.269   18.178  1.00 54.31  ? 472 HOH B O      1 
HETATM 10957 O  O      . HOH L 6 .   ? 22.643  -6.215  16.450  1.00 35.35  ? 473 HOH B O      1 
HETATM 10958 O  O      . HOH L 6 .   ? -2.766  16.714  4.201   1.00 44.39  ? 474 HOH B O      1 
HETATM 10959 O  O      . HOH L 6 .   ? -1.649  3.845   25.478  1.00 42.51  ? 475 HOH B O      1 
HETATM 10960 O  O      . HOH L 6 .   ? 23.099  15.296  23.160  1.00 42.98  ? 476 HOH B O      1 
HETATM 10961 O  O      . HOH L 6 .   ? 2.852   -4.158  22.397  1.00 44.00  ? 477 HOH B O      1 
HETATM 10962 O  O      . HOH L 6 .   ? 9.397   17.358  -0.605  1.00 38.88  ? 478 HOH B O      1 
HETATM 10963 O  O      . HOH L 6 .   ? -5.904  -1.525  13.314  1.00 44.38  ? 479 HOH B O      1 
HETATM 10964 O  O      . HOH L 6 .   ? -10.564 -1.813  9.532   1.00 51.04  ? 480 HOH B O      1 
HETATM 10965 O  O      . HOH L 6 .   ? -12.759 3.224   5.097   1.00 38.03  ? 481 HOH B O      1 
HETATM 10966 O  O      . HOH L 6 .   ? 31.439  -4.081  21.968  1.00 62.55  ? 482 HOH B O      1 
HETATM 10967 O  O      . HOH L 6 .   ? -6.180  -4.174  11.360  1.00 51.47  ? 483 HOH B O      1 
HETATM 10968 O  O      . HOH L 6 .   ? 7.838   15.655  -3.159  1.00 37.87  ? 484 HOH B O      1 
HETATM 10969 O  O      . HOH L 6 .   ? -12.473 -3.021  10.295  1.00 64.59  ? 485 HOH B O      1 
HETATM 10970 O  O      . HOH L 6 .   ? 24.149  3.551   -6.864  1.00 55.66  ? 486 HOH B O      1 
HETATM 10971 O  O      . HOH L 6 .   ? -2.375  -9.260  20.292  1.00 59.02  ? 487 HOH B O      1 
HETATM 10972 O  O      . HOH L 6 .   ? 21.644  -11.885 20.789  1.00 41.06  ? 488 HOH B O      1 
HETATM 10973 O  O      . HOH L 6 .   ? 11.974  17.007  -8.564  1.00 50.85  ? 489 HOH B O      1 
HETATM 10974 O  O      . HOH L 6 .   ? 24.789  -17.826 8.782   1.00 61.13  ? 490 HOH B O      1 
HETATM 10975 O  O      . HOH L 6 .   ? -19.915 3.398   15.652  1.00 58.42  ? 491 HOH B O      1 
HETATM 10976 O  O      . HOH M 6 .   ? 51.098  28.629  15.767  1.00 65.68  ? 301 HOH D O      1 
HETATM 10977 O  O      . HOH M 6 .   ? 60.667  35.493  27.540  1.00 44.55  ? 302 HOH D O      1 
HETATM 10978 O  O      . HOH M 6 .   ? 40.378  22.782  44.319  1.00 50.48  ? 303 HOH D O      1 
HETATM 10979 O  O      . HOH M 6 .   ? 32.268  26.103  7.833   1.00 33.87  ? 304 HOH D O      1 
HETATM 10980 O  O      . HOH M 6 .   ? 36.089  12.209  35.767  1.00 42.66  ? 305 HOH D O      1 
HETATM 10981 O  O      . HOH M 6 .   ? 53.668  39.478  24.111  1.00 45.03  ? 306 HOH D O      1 
HETATM 10982 O  O      . HOH M 6 .   ? 59.360  20.374  29.400  1.00 46.22  ? 307 HOH D O      1 
HETATM 10983 O  O      . HOH M 6 .   ? 44.626  27.535  43.473  1.00 41.00  ? 308 HOH D O      1 
HETATM 10984 O  O      . HOH M 6 .   ? 36.743  37.938  17.153  1.00 34.48  ? 309 HOH D O      1 
HETATM 10985 O  O      . HOH M 6 .   ? 45.049  30.666  9.788   1.00 32.24  ? 310 HOH D O      1 
HETATM 10986 O  O      . HOH M 6 .   ? 58.516  30.848  17.280  1.00 40.56  ? 311 HOH D O      1 
HETATM 10987 O  O      . HOH M 6 .   ? 57.909  28.979  19.400  1.00 35.65  ? 312 HOH D O      1 
HETATM 10988 O  O      . HOH M 6 .   ? 40.900  28.612  40.366  1.00 37.68  ? 313 HOH D O      1 
HETATM 10989 O  O      . HOH M 6 .   ? 37.799  35.919  40.952  1.00 37.68  ? 314 HOH D O      1 
HETATM 10990 O  O      . HOH M 6 .   ? 43.615  39.950  40.498  1.00 40.00  ? 315 HOH D O      1 
HETATM 10991 O  O      . HOH M 6 .   ? 37.055  16.879  12.435  1.00 30.28  ? 316 HOH D O      1 
HETATM 10992 O  O      . HOH M 6 .   ? 34.287  19.839  29.832  1.00 28.52  ? 317 HOH D O      1 
HETATM 10993 O  O      . HOH M 6 .   ? 41.011  31.243  42.342  1.00 38.30  ? 318 HOH D O      1 
HETATM 10994 O  O      . HOH M 6 .   ? 30.079  18.599  21.533  1.00 27.74  ? 319 HOH D O      1 
HETATM 10995 O  O      . HOH M 6 .   ? 43.515  32.973  9.239   1.00 29.60  ? 320 HOH D O      1 
HETATM 10996 O  O      . HOH M 6 .   ? 44.079  37.434  19.930  1.00 29.66  ? 321 HOH D O      1 
HETATM 10997 O  O      . HOH M 6 .   ? 25.098  24.072  16.002  1.00 30.68  ? 322 HOH D O      1 
HETATM 10998 O  O      . HOH M 6 .   ? 57.559  27.884  29.731  1.00 36.92  ? 323 HOH D O      1 
HETATM 10999 O  O      . HOH M 6 .   ? 31.583  40.886  29.459  1.00 37.60  ? 324 HOH D O      1 
HETATM 11000 O  O      . HOH M 6 .   ? 25.491  31.230  23.171  1.00 29.46  ? 325 HOH D O      1 
HETATM 11001 O  O      . HOH M 6 .   ? 41.972  41.036  24.737  1.00 37.81  ? 326 HOH D O      1 
HETATM 11002 O  O      . HOH M 6 .   ? 45.004  39.093  29.283  1.00 34.73  ? 327 HOH D O      1 
HETATM 11003 O  O      . HOH M 6 .   ? 21.749  26.945  20.708  1.00 27.57  ? 328 HOH D O      1 
HETATM 11004 O  O      . HOH M 6 .   ? 47.791  12.868  20.318  1.00 38.18  ? 329 HOH D O      1 
HETATM 11005 O  O      . HOH M 6 .   ? 53.871  16.030  24.898  1.00 37.28  ? 330 HOH D O      1 
HETATM 11006 O  O      . HOH M 6 .   ? 34.321  28.509  36.130  1.00 35.64  ? 331 HOH D O      1 
HETATM 11007 O  O      . HOH M 6 .   ? 29.475  19.833  24.955  1.00 32.62  ? 332 HOH D O      1 
HETATM 11008 O  O      . HOH M 6 .   ? 52.150  15.977  14.033  1.00 48.52  ? 333 HOH D O      1 
HETATM 11009 O  O      . HOH M 6 .   ? 42.797  27.546  35.949  1.00 30.81  ? 334 HOH D O      1 
HETATM 11010 O  O      . HOH M 6 .   ? 33.260  18.826  18.315  1.00 24.82  ? 335 HOH D O      1 
HETATM 11011 O  O      . HOH M 6 .   ? 37.093  27.702  38.780  1.00 40.27  ? 336 HOH D O      1 
HETATM 11012 O  O      . HOH M 6 .   ? 38.636  40.844  32.146  1.00 31.80  ? 337 HOH D O      1 
HETATM 11013 O  O      . HOH M 6 .   ? 42.415  25.101  38.677  1.00 32.82  ? 338 HOH D O      1 
HETATM 11014 O  O      . HOH M 6 .   ? 28.905  33.402  16.619  1.00 22.65  ? 339 HOH D O      1 
HETATM 11015 O  O      . HOH M 6 .   ? 45.421  34.374  34.889  1.00 29.09  ? 340 HOH D O      1 
HETATM 11016 O  O      . HOH M 6 .   ? 23.211  33.163  27.074  1.00 30.67  ? 341 HOH D O      1 
HETATM 11017 O  O      . HOH M 6 .   ? 24.631  21.597  18.527  1.00 27.71  ? 342 HOH D O      1 
HETATM 11018 O  O      . HOH M 6 .   ? 34.156  41.201  24.283  1.00 33.81  ? 343 HOH D O      1 
HETATM 11019 O  O      . HOH M 6 .   ? 38.887  15.032  22.499  1.00 37.14  ? 344 HOH D O      1 
HETATM 11020 O  O      . HOH M 6 .   ? 42.690  21.909  32.427  1.00 32.33  ? 345 HOH D O      1 
HETATM 11021 O  O      . HOH M 6 .   ? 38.214  17.703  24.332  1.00 27.54  ? 346 HOH D O      1 
HETATM 11022 O  O      . HOH M 6 .   ? 38.223  38.015  12.497  1.00 48.87  ? 347 HOH D O      1 
HETATM 11023 O  O      . HOH M 6 .   ? 52.653  12.396  20.963  1.00 41.08  ? 348 HOH D O      1 
HETATM 11024 O  O      . HOH M 6 .   ? 52.883  29.815  41.514  1.00 46.59  ? 349 HOH D O      1 
HETATM 11025 O  O      . HOH M 6 .   ? 20.264  25.022  25.442  1.00 34.93  ? 350 HOH D O      1 
HETATM 11026 O  O      . HOH M 6 .   ? 31.899  13.251  12.160  1.00 43.44  ? 351 HOH D O      1 
HETATM 11027 O  O      . HOH M 6 .   ? 55.999  20.838  16.558  1.00 38.09  ? 352 HOH D O      1 
HETATM 11028 O  O      . HOH M 6 .   ? 41.055  19.664  21.925  1.00 30.77  ? 353 HOH D O      1 
HETATM 11029 O  O      . HOH M 6 .   ? 43.128  22.101  9.013   1.00 32.88  ? 354 HOH D O      1 
HETATM 11030 O  O      . HOH M 6 .   ? 32.177  35.092  15.740  1.00 38.99  ? 355 HOH D O      1 
HETATM 11031 O  O      . HOH M 6 .   ? 56.184  14.696  18.827  1.00 45.06  ? 356 HOH D O      1 
HETATM 11032 O  O      . HOH M 6 .   ? 29.338  37.351  25.834  1.00 33.66  ? 357 HOH D O      1 
HETATM 11033 O  O      . HOH M 6 .   ? 55.608  18.382  17.200  1.00 41.79  ? 358 HOH D O      1 
HETATM 11034 O  O      . HOH M 6 .   ? 44.497  35.426  10.891  1.00 30.08  ? 359 HOH D O      1 
HETATM 11035 O  O      . HOH M 6 .   ? 48.268  27.176  36.210  1.00 31.54  ? 360 HOH D O      1 
HETATM 11036 O  O      . HOH M 6 .   ? 42.238  18.668  31.830  1.00 32.97  ? 361 HOH D O      1 
HETATM 11037 O  O      . HOH M 6 .   ? 30.983  32.236  12.749  1.00 30.17  ? 362 HOH D O      1 
HETATM 11038 O  O      . HOH M 6 .   ? 28.912  21.566  26.835  1.00 28.50  ? 363 HOH D O      1 
HETATM 11039 O  O      . HOH M 6 .   ? 41.981  36.058  11.619  1.00 31.10  ? 364 HOH D O      1 
HETATM 11040 O  O      . HOH M 6 .   ? 50.056  16.769  20.194  1.00 33.47  ? 365 HOH D O      1 
HETATM 11041 O  O      . HOH M 6 .   ? 40.650  15.244  11.998  1.00 39.55  ? 366 HOH D O      1 
HETATM 11042 O  O      . HOH M 6 .   ? 44.772  13.736  13.593  1.00 41.60  ? 367 HOH D O      1 
HETATM 11043 O  O      . HOH M 6 .   ? 60.414  26.433  23.001  1.00 41.01  ? 368 HOH D O      1 
HETATM 11044 O  O      . HOH M 6 .   ? 48.519  24.628  30.273  1.00 31.71  ? 369 HOH D O      1 
HETATM 11045 O  O      . HOH M 6 .   ? 56.512  23.170  13.052  1.00 43.97  ? 370 HOH D O      1 
HETATM 11046 O  O      . HOH M 6 .   ? 48.103  34.712  34.363  1.00 30.10  ? 371 HOH D O      1 
HETATM 11047 O  O      . HOH M 6 .   ? 57.922  23.668  33.168  1.00 41.70  ? 372 HOH D O      1 
HETATM 11048 O  O      . HOH M 6 .   ? 57.581  27.013  27.170  1.00 38.69  ? 373 HOH D O      1 
HETATM 11049 O  O      . HOH M 6 .   ? 42.315  35.193  35.590  1.00 28.39  ? 374 HOH D O      1 
HETATM 11050 O  O      . HOH M 6 .   ? 49.970  32.302  42.552  1.00 38.23  ? 375 HOH D O      1 
HETATM 11051 O  O      . HOH M 6 .   ? 45.284  40.900  31.284  1.00 39.78  ? 376 HOH D O      1 
HETATM 11052 O  O      . HOH M 6 .   ? 38.048  36.996  27.524  1.00 28.84  ? 377 HOH D O      1 
HETATM 11053 O  O      . HOH M 6 .   ? 43.993  36.453  14.262  1.00 29.93  ? 378 HOH D O      1 
HETATM 11054 O  O      . HOH M 6 .   ? 47.355  20.560  41.524  1.00 46.66  ? 379 HOH D O      1 
HETATM 11055 O  O      . HOH M 6 .   ? 34.903  36.728  18.312  1.00 30.32  ? 380 HOH D O      1 
HETATM 11056 O  O      . HOH M 6 .   ? 50.132  30.215  11.790  1.00 39.69  ? 381 HOH D O      1 
HETATM 11057 O  O      . HOH M 6 .   ? 22.321  22.106  22.173  1.00 33.41  ? 382 HOH D O      1 
HETATM 11058 O  O      . HOH M 6 .   ? 34.830  33.497  10.396  1.00 40.29  ? 383 HOH D O      1 
HETATM 11059 O  O      . HOH M 6 .   ? 61.081  33.511  29.359  1.00 48.71  ? 384 HOH D O      1 
HETATM 11060 O  O      . HOH M 6 .   ? 28.495  19.448  30.059  1.00 42.08  ? 385 HOH D O      1 
HETATM 11061 O  O      . HOH M 6 .   ? 35.965  22.741  6.802   1.00 35.47  ? 386 HOH D O      1 
HETATM 11062 O  O      . HOH M 6 .   ? 44.484  29.028  7.937   1.00 35.08  ? 387 HOH D O      1 
HETATM 11063 O  O      . HOH M 6 .   ? 52.901  27.031  40.454  1.00 42.62  ? 388 HOH D O      1 
HETATM 11064 O  O      . HOH M 6 .   ? 52.998  38.860  28.744  1.00 44.50  ? 389 HOH D O      1 
HETATM 11065 O  O      . HOH M 6 .   ? 57.171  39.357  32.820  1.00 41.91  ? 390 HOH D O      1 
HETATM 11066 O  O      . HOH M 6 .   ? 29.849  16.415  17.631  1.00 37.81  ? 391 HOH D O      1 
HETATM 11067 O  O      . HOH M 6 .   ? 41.629  28.815  6.288   1.00 32.76  ? 392 HOH D O      1 
HETATM 11068 O  O      . HOH M 6 .   ? 47.567  28.885  43.789  1.00 49.37  ? 393 HOH D O      1 
HETATM 11069 O  O      . HOH M 6 .   ? 47.873  11.667  22.647  1.00 39.93  ? 394 HOH D O      1 
HETATM 11070 O  O      . HOH M 6 .   ? 51.367  16.801  17.777  1.00 35.72  ? 395 HOH D O      1 
HETATM 11071 O  O      . HOH M 6 .   ? 36.614  24.498  4.864   1.00 39.12  ? 396 HOH D O      1 
HETATM 11072 O  O      . HOH M 6 .   ? 41.994  17.138  8.395   1.00 47.50  ? 397 HOH D O      1 
HETATM 11073 O  O      . HOH M 6 .   ? 30.522  18.171  26.613  1.00 38.92  ? 398 HOH D O      1 
HETATM 11074 O  O      . HOH M 6 .   ? 61.812  19.057  29.553  1.00 52.64  ? 399 HOH D O      1 
HETATM 11075 O  O      . HOH M 6 .   ? 37.553  18.420  40.960  1.00 58.27  ? 400 HOH D O      1 
HETATM 11076 O  O      . HOH M 6 .   ? 36.801  15.302  23.927  1.00 39.60  ? 401 HOH D O      1 
HETATM 11077 O  O      . HOH M 6 .   ? 51.790  29.020  10.135  1.00 36.55  ? 402 HOH D O      1 
HETATM 11078 O  O      . HOH M 6 .   ? 36.720  14.255  12.668  1.00 37.26  ? 403 HOH D O      1 
HETATM 11079 O  O      . HOH M 6 .   ? 56.557  37.275  21.714  1.00 44.48  ? 404 HOH D O      1 
HETATM 11080 O  O      . HOH M 6 .   ? 41.048  15.320  9.758   1.00 43.87  ? 405 HOH D O      1 
HETATM 11081 O  O      . HOH M 6 .   ? 38.686  27.862  40.677  1.00 41.84  ? 406 HOH D O      1 
HETATM 11082 O  O      . HOH M 6 .   ? 42.165  38.055  18.754  1.00 41.55  ? 407 HOH D O      1 
HETATM 11083 O  O      . HOH M 6 .   ? 52.880  32.742  42.415  1.00 40.59  ? 408 HOH D O      1 
HETATM 11084 O  O      . HOH M 6 .   ? 43.095  23.179  46.667  1.00 55.26  ? 409 HOH D O      1 
HETATM 11085 O  O      . HOH M 6 .   ? 33.953  15.106  22.296  1.00 40.45  ? 410 HOH D O      1 
HETATM 11086 O  O      . HOH M 6 .   ? 61.490  20.914  28.404  1.00 52.27  ? 411 HOH D O      1 
HETATM 11087 O  O      . HOH M 6 .   ? 43.947  7.998   24.231  1.00 51.97  ? 412 HOH D O      1 
HETATM 11088 O  O      . HOH M 6 .   ? 39.760  39.027  14.549  1.00 42.21  ? 413 HOH D O      1 
HETATM 11089 O  O      . HOH M 6 .   ? 48.801  11.003  14.849  1.00 52.53  ? 414 HOH D O      1 
HETATM 11090 O  O      . HOH M 6 .   ? 23.883  19.033  17.581  1.00 34.74  ? 415 HOH D O      1 
HETATM 11091 O  O      . HOH M 6 .   ? 57.553  33.722  15.643  1.00 46.46  ? 416 HOH D O      1 
HETATM 11092 O  O      . HOH M 6 .   ? 36.838  13.982  19.547  1.00 47.89  ? 417 HOH D O      1 
HETATM 11093 O  O      . HOH M 6 .   ? 35.882  33.716  8.488   1.00 58.51  ? 418 HOH D O      1 
HETATM 11094 O  O      . HOH M 6 .   ? 22.968  23.148  17.494  1.00 32.66  ? 419 HOH D O      1 
HETATM 11095 O  O      . HOH M 6 .   ? 46.849  28.270  46.226  1.00 55.47  ? 420 HOH D O      1 
HETATM 11096 O  O      . HOH M 6 .   ? 53.103  15.294  16.079  1.00 41.98  ? 421 HOH D O      1 
HETATM 11097 O  O      . HOH M 6 .   ? 28.783  21.956  5.185   1.00 45.96  ? 422 HOH D O      1 
HETATM 11098 O  O      . HOH M 6 .   ? 43.109  25.063  5.621   1.00 49.18  ? 423 HOH D O      1 
HETATM 11099 O  O      . HOH M 6 .   ? 60.575  31.661  29.583  1.00 42.64  ? 424 HOH D O      1 
HETATM 11100 O  O      . HOH M 6 .   ? 36.536  30.717  6.113   1.00 42.96  ? 425 HOH D O      1 
HETATM 11101 O  O      . HOH M 6 .   ? 41.921  14.110  13.761  1.00 49.10  ? 426 HOH D O      1 
HETATM 11102 O  O      . HOH M 6 .   ? 45.649  11.765  15.410  1.00 44.66  ? 427 HOH D O      1 
HETATM 11103 O  O      . HOH M 6 .   ? 61.570  24.423  23.930  1.00 45.92  ? 428 HOH D O      1 
HETATM 11104 O  O      . HOH M 6 .   ? 57.561  22.582  37.279  1.00 55.38  ? 429 HOH D O      1 
HETATM 11105 O  O      . HOH M 6 .   ? 32.488  37.253  14.359  1.00 54.62  ? 430 HOH D O      1 
HETATM 11106 O  O      . HOH M 6 .   ? 45.233  8.776   30.713  1.00 49.00  ? 431 HOH D O      1 
HETATM 11107 O  O      . HOH M 6 .   ? 43.363  19.241  8.233   1.00 42.49  ? 432 HOH D O      1 
HETATM 11108 O  O      . HOH M 6 .   ? 31.812  25.973  4.666   1.00 29.25  ? 433 HOH D O      1 
HETATM 11109 O  O      . HOH M 6 .   ? 38.786  38.312  10.314  1.00 42.52  ? 434 HOH D O      1 
HETATM 11110 O  O      . HOH M 6 .   ? 59.578  27.730  25.363  1.00 39.60  ? 435 HOH D O      1 
HETATM 11111 O  O      . HOH M 6 .   ? 54.285  30.724  42.671  1.00 46.83  ? 436 HOH D O      1 
HETATM 11112 O  O      . HOH M 6 .   ? 37.425  34.406  43.127  1.00 44.61  ? 437 HOH D O      1 
HETATM 11113 O  O      . HOH M 6 .   ? 47.520  27.260  7.027   1.00 41.96  ? 438 HOH D O      1 
HETATM 11114 O  O      . HOH M 6 .   ? 60.366  22.637  15.914  1.00 56.03  ? 439 HOH D O      1 
HETATM 11115 O  O      . HOH M 6 .   ? 60.704  31.873  33.479  1.00 51.87  ? 440 HOH D O      1 
HETATM 11116 O  O      . HOH M 6 .   ? 38.594  39.926  17.671  1.00 35.98  ? 441 HOH D O      1 
HETATM 11117 O  O      . HOH M 6 .   ? 19.990  24.852  22.017  1.00 44.41  ? 442 HOH D O      1 
HETATM 11118 O  O      . HOH M 6 .   ? 23.313  16.583  12.361  1.00 42.17  ? 443 HOH D O      1 
HETATM 11119 O  O      . HOH M 6 .   ? 48.250  29.501  45.228  1.00 54.58  ? 444 HOH D O      1 
HETATM 11120 O  O      . HOH M 6 .   ? 63.403  37.775  26.411  1.00 50.48  ? 445 HOH D O      1 
HETATM 11121 O  O      . HOH M 6 .   ? 43.969  10.635  16.489  1.00 47.74  ? 446 HOH D O      1 
HETATM 11122 O  O      . HOH M 6 .   ? 64.907  32.978  29.324  1.00 52.06  ? 447 HOH D O      1 
HETATM 11123 O  O      . HOH M 6 .   ? 36.685  37.985  42.597  1.00 46.47  ? 448 HOH D O      1 
HETATM 11124 O  O      . HOH M 6 .   ? 63.988  37.932  28.417  1.00 60.61  ? 449 HOH D O      1 
HETATM 11125 O  O      . HOH M 6 .   ? 36.499  39.783  8.862   1.00 43.81  ? 450 HOH D O      1 
HETATM 11126 O  O      . HOH M 6 .   ? 56.296  10.538  17.710  1.00 54.93  ? 451 HOH D O      1 
HETATM 11127 O  O      . HOH M 6 .   ? 62.091  23.864  16.383  1.00 44.07  ? 452 HOH D O      1 
HETATM 11128 O  O      . HOH M 6 .   ? 21.842  18.568  20.710  1.00 41.00  ? 453 HOH D O      1 
HETATM 11129 O  O      . HOH M 6 .   ? 66.483  32.723  30.246  1.00 62.95  ? 454 HOH D O      1 
HETATM 11130 O  O      . HOH M 6 .   ? 39.205  41.104  9.773   1.00 48.10  ? 455 HOH D O      1 
HETATM 11131 O  O      . HOH M 6 .   ? 62.466  19.080  16.545  1.00 41.18  ? 456 HOH D O      1 
HETATM 11132 O  O      . HOH N 6 .   ? 9.071   14.815  23.800  1.00 30.63  ? 301 HOH C O      1 
HETATM 11133 O  O      . HOH N 6 .   ? 26.794  22.189  39.268  1.00 46.28  ? 302 HOH C O      1 
HETATM 11134 O  O      . HOH N 6 .   ? 22.081  9.370   44.496  1.00 39.99  ? 303 HOH C O      1 
HETATM 11135 O  O      . HOH N 6 .   ? 2.072   16.534  40.094  1.00 48.08  ? 304 HOH C O      1 
HETATM 11136 O  O      . HOH N 6 .   ? 10.134  20.032  54.335  1.00 55.68  ? 305 HOH C O      1 
HETATM 11137 O  O      . HOH N 6 .   ? 7.269   27.003  33.017  1.00 46.59  ? 306 HOH C O      1 
HETATM 11138 O  O      . HOH N 6 .   ? 6.140   19.965  50.847  1.00 52.83  ? 307 HOH C O      1 
HETATM 11139 O  O      . HOH N 6 .   ? 26.787  26.643  52.060  1.00 59.52  ? 308 HOH C O      1 
HETATM 11140 O  O      . HOH N 6 .   ? 24.462  28.169  39.440  1.00 55.11  ? 309 HOH C O      1 
HETATM 11141 O  O      . HOH N 6 .   ? 22.189  25.788  34.285  1.00 36.19  ? 310 HOH C O      1 
HETATM 11142 O  O      . HOH N 6 .   ? 5.470   18.367  23.759  1.00 33.05  ? 311 HOH C O      1 
HETATM 11143 O  O      . HOH N 6 .   ? 22.564  16.291  32.090  1.00 33.74  ? 312 HOH C O      1 
HETATM 11144 O  O      . HOH N 6 .   ? 29.717  19.667  46.120  1.00 51.59  ? 313 HOH C O      1 
HETATM 11145 O  O      . HOH N 6 .   ? 32.966  6.817   51.089  1.00 64.01  ? 314 HOH C O      1 
HETATM 11146 O  O      . HOH N 6 .   ? 13.480  21.404  30.364  1.00 36.97  ? 315 HOH C O      1 
HETATM 11147 O  O      . HOH N 6 .   ? 13.081  10.033  54.382  1.00 57.52  ? 316 HOH C O      1 
HETATM 11148 O  O      . HOH N 6 .   ? 6.190   29.616  37.459  1.00 53.63  ? 317 HOH C O      1 
HETATM 11149 O  O      . HOH N 6 .   ? 6.250   20.589  28.788  1.00 46.43  ? 318 HOH C O      1 
HETATM 11150 O  O      . HOH N 6 .   ? 23.291  26.569  55.198  1.00 63.41  ? 319 HOH C O      1 
HETATM 11151 O  O      . HOH N 6 .   ? 27.374  16.504  35.842  1.00 38.88  ? 320 HOH C O      1 
HETATM 11152 O  O      . HOH N 6 .   ? 13.735  7.802   29.384  1.00 37.56  ? 321 HOH C O      1 
HETATM 11153 O  O      . HOH N 6 .   ? 32.123  28.969  34.323  1.00 32.14  ? 322 HOH C O      1 
HETATM 11154 O  O      . HOH N 6 .   ? 21.059  17.912  26.584  1.00 35.11  ? 323 HOH C O      1 
HETATM 11155 O  O      . HOH N 6 .   ? 25.440  35.707  38.380  1.00 60.05  ? 324 HOH C O      1 
HETATM 11156 O  O      . HOH N 6 .   ? 28.524  24.388  43.023  1.00 50.92  ? 325 HOH C O      1 
HETATM 11157 O  O      . HOH N 6 .   ? 23.837  19.049  36.866  1.00 29.67  ? 326 HOH C O      1 
HETATM 11158 O  O      . HOH N 6 .   ? 8.670   36.762  42.112  1.00 55.10  ? 327 HOH C O      1 
HETATM 11159 O  O      . HOH N 6 .   ? 3.839   28.045  45.004  1.00 54.25  ? 328 HOH C O      1 
HETATM 11160 O  O      . HOH N 6 .   ? 30.518  13.582  46.874  1.00 47.98  ? 329 HOH C O      1 
HETATM 11161 O  O      . HOH N 6 .   ? 2.827   19.578  47.234  1.00 48.15  ? 330 HOH C O      1 
HETATM 11162 O  O      . HOH N 6 .   ? 29.038  13.540  35.327  1.00 36.11  ? 331 HOH C O      1 
HETATM 11163 O  O      . HOH N 6 .   ? 11.524  21.555  32.622  1.00 41.98  ? 332 HOH C O      1 
HETATM 11164 O  O      . HOH N 6 .   ? 6.958   23.194  57.245  1.00 55.33  ? 333 HOH C O      1 
HETATM 11165 O  O      . HOH N 6 .   ? 25.536  20.514  29.636  1.00 33.55  ? 334 HOH C O      1 
HETATM 11166 O  O      . HOH N 6 .   ? 31.964  18.302  28.745  1.00 37.30  ? 335 HOH C O      1 
HETATM 11167 O  O      . HOH N 6 .   ? 23.555  20.868  47.079  1.00 41.67  ? 336 HOH C O      1 
HETATM 11168 O  O      . HOH N 6 .   ? 23.748  8.225   35.697  1.00 40.78  ? 337 HOH C O      1 
HETATM 11169 O  O      . HOH N 6 .   ? 10.893  6.568   35.755  1.00 41.98  ? 338 HOH C O      1 
HETATM 11170 O  O      . HOH N 6 .   ? 18.063  6.123   55.974  1.00 56.86  ? 339 HOH C O      1 
HETATM 11171 O  O      . HOH N 6 .   ? 1.996   6.276   25.697  1.00 28.35  ? 340 HOH C O      1 
HETATM 11172 O  O      . HOH N 6 .   ? 16.804  15.658  25.613  1.00 29.07  ? 341 HOH C O      1 
HETATM 11173 O  O      . HOH N 6 .   ? 13.587  4.872   43.030  1.00 46.43  ? 342 HOH C O      1 
HETATM 11174 O  O      . HOH N 6 .   ? 20.944  -1.237  40.083  1.00 44.61  ? 343 HOH C O      1 
HETATM 11175 O  O      . HOH N 6 .   ? 36.137  15.128  35.481  1.00 41.94  ? 344 HOH C O      1 
HETATM 11176 O  O      . HOH N 6 .   ? 12.546  9.331   27.223  1.00 34.95  ? 345 HOH C O      1 
HETATM 11177 O  O      . HOH N 6 .   ? 31.844  19.808  32.032  1.00 39.81  ? 346 HOH C O      1 
HETATM 11178 O  O      . HOH N 6 .   ? 25.748  17.110  32.492  1.00 38.97  ? 347 HOH C O      1 
HETATM 11179 O  O      . HOH N 6 .   ? -4.379  13.378  22.308  1.00 51.35  ? 348 HOH C O      1 
HETATM 11180 O  O      . HOH N 6 .   ? 10.500  11.921  53.775  1.00 51.41  ? 349 HOH C O      1 
HETATM 11181 O  O      . HOH N 6 .   ? 16.936  20.257  60.622  1.00 65.44  ? 350 HOH C O      1 
HETATM 11182 O  O      . HOH N 6 .   ? 1.800   16.119  25.568  1.00 39.52  ? 351 HOH C O      1 
HETATM 11183 O  O      . HOH N 6 .   ? 6.127   25.317  52.653  1.00 64.17  ? 352 HOH C O      1 
HETATM 11184 O  O      . HOH N 6 .   ? 27.840  10.401  62.224  1.00 56.73  ? 353 HOH C O      1 
HETATM 11185 O  O      . HOH N 6 .   ? 26.582  17.225  58.034  1.00 56.77  ? 354 HOH C O      1 
HETATM 11186 O  O      . HOH N 6 .   ? 19.428  19.752  26.545  1.00 31.16  ? 355 HOH C O      1 
HETATM 11187 O  O      . HOH N 6 .   ? 13.297  2.943   33.933  1.00 57.40  ? 356 HOH C O      1 
HETATM 11188 O  O      . HOH N 6 .   ? 21.855  23.551  40.564  1.00 40.96  ? 357 HOH C O      1 
HETATM 11189 O  O      . HOH N 6 .   ? 12.775  19.224  26.779  1.00 33.29  ? 358 HOH C O      1 
HETATM 11190 O  O      . HOH N 6 .   ? 0.613   3.858   37.541  1.00 40.75  ? 359 HOH C O      1 
HETATM 11191 O  O      . HOH N 6 .   ? -1.147  10.244  44.956  1.00 49.58  ? 360 HOH C O      1 
HETATM 11192 O  O      . HOH N 6 .   ? 13.104  33.267  50.363  1.00 55.96  ? 361 HOH C O      1 
HETATM 11193 O  O      . HOH N 6 .   ? 19.079  19.641  60.097  1.00 61.18  ? 362 HOH C O      1 
HETATM 11194 O  O      . HOH N 6 .   ? 31.672  16.530  53.947  1.00 51.38  ? 363 HOH C O      1 
HETATM 11195 O  O      . HOH N 6 .   ? 7.712   35.715  48.924  1.00 61.34  ? 364 HOH C O      1 
HETATM 11196 O  O      . HOH N 6 .   ? 14.565  7.766   51.458  1.00 54.78  ? 365 HOH C O      1 
HETATM 11197 O  O      . HOH N 6 .   ? 3.530   34.361  43.174  1.00 57.66  ? 366 HOH C O      1 
HETATM 11198 O  O      . HOH N 6 .   ? 7.592   34.114  39.981  1.00 52.66  ? 367 HOH C O      1 
HETATM 11199 O  O      . HOH N 6 .   ? 7.300   6.212   44.220  1.00 50.47  ? 368 HOH C O      1 
HETATM 11200 O  O      . HOH N 6 .   ? 32.309  13.710  44.106  1.00 51.45  ? 369 HOH C O      1 
HETATM 11201 O  O      . HOH N 6 .   ? 30.591  7.773   32.435  1.00 50.07  ? 370 HOH C O      1 
HETATM 11202 O  O      . HOH N 6 .   ? 5.558   9.480   47.587  1.00 55.02  ? 371 HOH C O      1 
HETATM 11203 O  O      . HOH N 6 .   ? 4.284   21.773  51.894  1.00 52.57  ? 372 HOH C O      1 
HETATM 11204 O  O      . HOH N 6 .   ? -2.734  12.785  30.789  1.00 50.25  ? 373 HOH C O      1 
HETATM 11205 O  O      . HOH N 6 .   ? 14.827  3.282   41.276  1.00 45.74  ? 374 HOH C O      1 
HETATM 11206 O  O      . HOH N 6 .   ? 4.240   5.411   29.373  1.00 39.14  ? 375 HOH C O      1 
HETATM 11207 O  O      . HOH N 6 .   ? 5.512   23.419  53.635  1.00 62.80  ? 376 HOH C O      1 
HETATM 11208 O  O      . HOH N 6 .   ? 31.294  10.274  44.011  1.00 47.59  ? 377 HOH C O      1 
HETATM 11209 O  O      . HOH N 6 .   ? 6.081   4.305   34.137  1.00 41.01  ? 378 HOH C O      1 
HETATM 11210 O  O      . HOH N 6 .   ? 20.026  30.043  57.578  1.00 66.70  ? 379 HOH C O      1 
HETATM 11211 O  O      . HOH N 6 .   ? 4.259   33.376  50.381  1.00 59.33  ? 380 HOH C O      1 
HETATM 11212 O  O      . HOH N 6 .   ? 20.209  32.542  50.286  1.00 60.98  ? 381 HOH C O      1 
HETATM 11213 O  O      . HOH N 6 .   ? 6.406   4.006   35.862  1.00 55.97  ? 382 HOH C O      1 
HETATM 11214 O  O      . HOH N 6 .   ? 11.984  19.852  62.409  1.00 66.89  ? 383 HOH C O      1 
HETATM 11215 O  O      . HOH N 6 .   ? 6.966   31.815  39.310  1.00 57.97  ? 384 HOH C O      1 
HETATM 11216 O  O      . HOH N 6 .   ? 4.889   26.674  43.630  1.00 53.00  ? 385 HOH C O      1 
HETATM 11217 O  O      . HOH N 6 .   ? 32.021  19.410  52.937  1.00 56.51  ? 386 HOH C O      1 
HETATM 11218 O  O      . HOH N 6 .   ? 22.008  -2.276  41.400  1.00 43.35  ? 387 HOH C O      1 
HETATM 11219 O  O      . HOH N 6 .   ? 20.972  35.553  42.212  1.00 67.71  ? 388 HOH C O      1 
HETATM 11220 O  O      . HOH N 6 .   ? 0.352   19.646  28.932  1.00 49.39  ? 389 HOH C O      1 
HETATM 11221 O  O      . HOH N 6 .   ? 31.468  -0.178  44.883  1.00 52.24  ? 390 HOH C O      1 
HETATM 11222 O  O      . HOH N 6 .   ? 1.459   4.274   29.331  1.00 39.62  ? 391 HOH C O      1 
HETATM 11223 O  O      . HOH N 6 .   ? 24.921  4.998   54.553  1.00 58.70  ? 392 HOH C O      1 
HETATM 11224 O  O      . HOH N 6 .   ? 19.835  22.793  26.702  1.00 39.22  ? 393 HOH C O      1 
HETATM 11225 O  O      . HOH N 6 .   ? 5.728   4.306   27.466  1.00 43.84  ? 394 HOH C O      1 
HETATM 11226 O  O      . HOH N 6 .   ? 6.422   22.096  49.609  1.00 54.58  ? 395 HOH C O      1 
HETATM 11227 O  O      . HOH N 6 .   ? 16.382  18.775  24.652  1.00 38.44  ? 396 HOH C O      1 
HETATM 11228 O  O      . HOH N 6 .   ? 15.462  8.039   53.404  1.00 61.89  ? 397 HOH C O      1 
HETATM 11229 O  O      . HOH N 6 .   ? 13.043  29.517  30.285  1.00 59.57  ? 398 HOH C O      1 
HETATM 11230 O  O      . HOH N 6 .   ? 33.202  22.404  38.234  1.00 57.43  ? 399 HOH C O      1 
HETATM 11231 O  O      . HOH N 6 .   ? 20.581  15.924  26.728  1.00 46.95  ? 400 HOH C O      1 
HETATM 11232 O  O      . HOH N 6 .   ? 10.527  34.063  50.403  1.00 62.07  ? 401 HOH C O      1 
HETATM 11233 O  O      . HOH N 6 .   ? 27.026  13.643  33.396  1.00 42.59  ? 402 HOH C O      1 
HETATM 11234 O  O      . HOH N 6 .   ? 26.917  19.695  28.471  1.00 44.03  ? 403 HOH C O      1 
HETATM 11235 O  O      . HOH N 6 .   ? 5.200   22.844  56.783  1.00 57.68  ? 404 HOH C O      1 
HETATM 11236 O  O      . HOH N 6 .   ? 4.964   34.405  40.116  1.00 54.59  ? 405 HOH C O      1 
HETATM 11237 O  O      . HOH N 6 .   ? 2.916   38.507  42.113  1.00 61.34  ? 406 HOH C O      1 
HETATM 11238 O  O      . HOH N 6 .   ? 0.869   4.059   26.963  1.00 36.26  ? 407 HOH C O      1 
HETATM 11239 O  O      . HOH N 6 .   ? -0.629  8.224   25.973  1.00 34.72  ? 408 HOH C O      1 
HETATM 11240 O  O      . HOH N 6 .   ? 4.448   25.289  59.418  1.00 70.50  ? 409 HOH C O      1 
HETATM 11241 O  O      . HOH N 6 .   ? 1.230   19.313  60.856  1.00 72.29  ? 410 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     . GLY A 1   ? 0.7361 0.6447 0.6123 -0.1199 0.1116  -0.1089 0   GLY A N     
2     C  CA    . GLY A 1   ? 0.6981 0.6152 0.5863 -0.1084 0.1069  -0.1003 0   GLY A CA    
3     C  C     . GLY A 1   ? 0.6272 0.5406 0.5334 -0.0967 0.1128  -0.0990 0   GLY A C     
4     O  O     . GLY A 1   ? 0.6728 0.5760 0.5825 -0.0969 0.1223  -0.1053 0   GLY A O     
10    N  N     . MET A 2   ? 0.6008 0.5222 0.5185 -0.0868 0.1070  -0.0908 1   MET A N     
11    C  CA    . MET A 2   ? 0.5639 0.4824 0.4979 -0.0760 0.1115  -0.0885 1   MET A CA    
12    C  C     . MET A 2   ? 0.4972 0.4137 0.4355 -0.0711 0.1181  -0.0899 1   MET A C     
13    O  O     . MET A 2   ? 0.5567 0.4776 0.4876 -0.0736 0.1165  -0.0896 1   MET A O     
14    C  CB    . MET A 2   ? 0.5335 0.4610 0.4778 -0.0679 0.1026  -0.0793 1   MET A CB    
15    C  CG    . MET A 2   ? 0.4499 0.3883 0.3911 -0.0668 0.0930  -0.0734 1   MET A CG    
16    S  SD    . MET A 2   ? 0.4839 0.4311 0.4391 -0.0564 0.0854  -0.0643 1   MET A SD    
17    C  CE    . MET A 2   ? 0.4720 0.4277 0.4222 -0.0625 0.0752  -0.0619 1   MET A CE    
27    N  N     . THR A 3   ? 0.5351 0.4452 0.4864 -0.0641 0.1253  -0.0910 2   THR A N     
28    C  CA    . THR A 3   ? 0.4720 0.3806 0.4307 -0.0588 0.1321  -0.0923 2   THR A CA    
29    C  C     . THR A 3   ? 0.4945 0.4130 0.4609 -0.0504 0.1247  -0.0835 2   THR A C     
30    O  O     . THR A 3   ? 0.4385 0.3615 0.4110 -0.0453 0.1175  -0.0767 2   THR A O     
31    C  CB    . THR A 3   ? 0.4977 0.3963 0.4699 -0.0537 0.1413  -0.0957 2   THR A CB    
32    O  OG1   . THR A 3   ? 0.5739 0.4624 0.5381 -0.0621 0.1484  -0.1046 2   THR A OG1   
33    C  CG2   . THR A 3   ? 0.5215 0.4193 0.5035 -0.0481 0.1484  -0.0972 2   THR A CG2   
41    N  N     . GLU A 4   ? 0.4809 0.4028 0.4462 -0.0498 0.1265  -0.0838 3   GLU A N     
42    C  CA    . GLU A 4   ? 0.4766 0.4071 0.4489 -0.0425 0.1202  -0.0761 3   GLU A CA    
43    C  C     . GLU A 4   ? 0.4221 0.3500 0.4103 -0.0343 0.1269  -0.0760 3   GLU A C     
44    O  O     . GLU A 4   ? 0.4252 0.3469 0.4158 -0.0359 0.1371  -0.0828 3   GLU A O     
45    C  CB    . GLU A 4   ? 0.4888 0.4253 0.4491 -0.0478 0.1164  -0.0756 3   GLU A CB    
46    C  CG    . GLU A 4   ? 0.5593 0.5041 0.5267 -0.0408 0.1104  -0.0683 3   GLU A CG    
47    C  CD    . GLU A 4   ? 0.5718 0.5192 0.5315 -0.0453 0.1122  -0.0698 3   GLU A CD    
48    O  OE1   . GLU A 4   ? 0.5123 0.4655 0.4778 -0.0403 0.1086  -0.0647 3   GLU A OE1   
49    O  OE2   . GLU A 4   ? 0.6077 0.5515 0.5545 -0.0546 0.1170  -0.0760 3   GLU A OE2   
56    N  N     . TYR A 5   ? 0.3796 0.3123 0.3792 -0.0255 0.1214  -0.0684 4   TYR A N     
57    C  CA    . TYR A 5   ? 0.3940 0.3251 0.4103 -0.0173 0.1259  -0.0666 4   TYR A CA    
58    C  C     . TYR A 5   ? 0.3926 0.3327 0.4127 -0.0126 0.1201  -0.0606 4   TYR A C     
59    O  O     . TYR A 5   ? 0.3491 0.2954 0.3667 -0.0106 0.1107  -0.0543 4   TYR A O     
60    C  CB    . TYR A 5   ? 0.3940 0.3213 0.4208 -0.0115 0.1241  -0.0624 4   TYR A CB    
61    C  CG    . TYR A 5   ? 0.4030 0.3201 0.4284 -0.0154 0.1303  -0.0681 4   TYR A CG    
62    C  CD1   . TYR A 5   ? 0.4612 0.3697 0.4964 -0.0139 0.1404  -0.0735 4   TYR A CD1   
63    C  CD2   . TYR A 5   ? 0.4388 0.3549 0.4544 -0.0206 0.1263  -0.0683 4   TYR A CD2   
64    C  CE1   . TYR A 5   ? 0.4537 0.3518 0.4882 -0.0175 0.1462  -0.0790 4   TYR A CE1   
65    C  CE2   . TYR A 5   ? 0.4743 0.3805 0.4888 -0.0247 0.1320  -0.0737 4   TYR A CE2   
66    C  CZ    . TYR A 5   ? 0.4674 0.3641 0.4909 -0.0232 0.1421  -0.0791 4   TYR A CZ    
67    O  OH    . TYR A 5   ? 0.4924 0.3780 0.5154 -0.0272 0.1484  -0.0851 4   TYR A OH    
77    N  N     . LYS A 6   ? 0.3508 0.2918 0.3775 -0.0110 0.1261  -0.0627 5   LYS A N     
78    C  CA    . LYS A 6   ? 0.3499 0.2993 0.3794 -0.0080 0.1213  -0.0578 5   LYS A CA    
79    C  C     . LYS A 6   ? 0.3103 0.2616 0.3578 0.0016  0.1197  -0.0520 5   LYS A C     
80    O  O     . LYS A 6   ? 0.3054 0.2543 0.3663 0.0051  0.1270  -0.0541 5   LYS A O     
81    C  CB    . LYS A 6   ? 0.3565 0.3069 0.3815 -0.0131 0.1283  -0.0633 5   LYS A CB    
82    C  CG    . LYS A 6   ? 0.4176 0.3668 0.4227 -0.0236 0.1284  -0.0680 5   LYS A CG    
83    C  CD    . LYS A 6   ? 0.5008 0.4503 0.5010 -0.0294 0.1367  -0.0738 5   LYS A CD    
84    C  CE    . LYS A 6   ? 0.5726 0.5166 0.5554 -0.0404 0.1420  -0.0817 5   LYS A CE    
85    N  NZ    . LYS A 6   ? 0.6691 0.6165 0.6349 -0.0466 0.1315  -0.0779 5   LYS A NZ    
99    N  N     . LEU A 7   ? 0.2691 0.2243 0.3171 0.0056  0.1103  -0.0447 6   LEU A N     
100   C  CA    . LEU A 7   ? 0.2714 0.2287 0.3337 0.0138  0.1067  -0.0380 6   LEU A CA    
101   C  C     . LEU A 7   ? 0.2564 0.2222 0.3208 0.0162  0.1011  -0.0335 6   LEU A C     
102   O  O     . LEU A 7   ? 0.2734 0.2435 0.3265 0.0127  0.0960  -0.0329 6   LEU A O     
103   C  CB    . LEU A 7   ? 0.2641 0.2204 0.3241 0.0157  0.1001  -0.0333 6   LEU A CB    
104   C  CG    . LEU A 7   ? 0.3074 0.2563 0.3616 0.0116  0.1036  -0.0374 6   LEU A CG    
105   C  CD1   . LEU A 7   ? 0.3356 0.2842 0.3898 0.0140  0.0975  -0.0320 6   LEU A CD1   
106   C  CD2   . LEU A 7   ? 0.3078 0.2484 0.3705 0.0118  0.1133  -0.0425 6   LEU A CD2   
118   N  N     . VAL A 8   ? 0.2319 0.1997 0.3113 0.0222  0.1017  -0.0300 7   VAL A N     
119   C  CA    . VAL A 8   ? 0.2151 0.1906 0.2984 0.0245  0.0968  -0.0257 7   VAL A CA    
120   C  C     . VAL A 8   ? 0.2162 0.1938 0.3106 0.0314  0.0905  -0.0181 7   VAL A C     
121   O  O     . VAL A 8   ? 0.2446 0.2183 0.3516 0.0354  0.0937  -0.0169 7   VAL A O     
122   C  CB    . VAL A 8   ? 0.2518 0.2294 0.3436 0.0239  0.1044  -0.0294 7   VAL A CB    
123   C  CG1   . VAL A 8   ? 0.2320 0.2179 0.3281 0.0260  0.0988  -0.0244 7   VAL A CG1   
124   C  CG2   . VAL A 8   ? 0.2527 0.2280 0.3311 0.0158  0.1109  -0.0371 7   VAL A CG2   
134   N  N     . VAL A 9   ? 0.1993 0.1821 0.2885 0.0323  0.0816  -0.0130 8   VAL A N     
135   C  CA    . VAL A 9   ? 0.1970 0.1818 0.2930 0.0375  0.0747  -0.0058 8   VAL A CA    
136   C  C     . VAL A 9   ? 0.2089 0.2002 0.3147 0.0401  0.0723  -0.0025 8   VAL A C     
137   O  O     . VAL A 9   ? 0.1974 0.1934 0.2970 0.0377  0.0695  -0.0030 8   VAL A O     
138   C  CB    . VAL A 9   ? 0.2138 0.2000 0.2975 0.0364  0.0670  -0.0032 8   VAL A CB    
139   C  CG1   . VAL A 9   ? 0.1934 0.1807 0.2822 0.0406  0.0609  0.0035  8   VAL A CG1   
140   C  CG2   . VAL A 9   ? 0.1861 0.1671 0.2605 0.0329  0.0697  -0.0071 8   VAL A CG2   
150   N  N     . VAL A 10  ? 0.2320 0.2235 0.3537 0.0449  0.0728  0.0012  9   VAL A N     
151   C  CA    . VAL A 10  ? 0.1809 0.1791 0.3144 0.0473  0.0709  0.0044  9   VAL A CA    
152   C  C     . VAL A 10  ? 0.2616 0.2616 0.4039 0.0519  0.0632  0.0125  9   VAL A C     
153   O  O     . VAL A 10  ? 0.2209 0.2161 0.3638 0.0538  0.0615  0.0155  9   VAL A O     
154   C  CB    . VAL A 10  ? 0.2292 0.2275 0.3775 0.0481  0.0804  0.0002  9   VAL A CB    
155   C  CG1   . VAL A 10  ? 0.2578 0.2530 0.3954 0.0426  0.0886  -0.0082 9   VAL A CG1   
156   C  CG2   . VAL A 10  ? 0.2472 0.2403 0.4110 0.0529  0.0837  0.0020  9   VAL A CG2   
166   N  N     . GLY A 11  ? 0.2263 0.2333 0.3756 0.0533  0.0586  0.0163  10  GLY A N     
167   C  CA    . GLY A 11  ? 0.2271 0.2370 0.3852 0.0569  0.0507  0.0243  10  GLY A CA    
168   C  C     . GLY A 11  ? 0.2466 0.2634 0.4003 0.0556  0.0431  0.0272  10  GLY A C     
169   O  O     . GLY A 11  ? 0.2538 0.2725 0.3970 0.0521  0.0435  0.0234  10  GLY A O     
173   N  N     . ALA A 12  ? 0.2201 0.2405 0.3822 0.0582  0.0357  0.0344  11  ALA A N     
174   C  CA    . ALA A 12  ? 0.2466 0.2733 0.4061 0.0568  0.0283  0.0373  11  ALA A CA    
175   C  C     . ALA A 12  ? 0.2417 0.2668 0.3809 0.0535  0.0238  0.0356  11  ALA A C     
176   O  O     . ALA A 12  ? 0.2590 0.2789 0.3871 0.0528  0.0241  0.0343  11  ALA A O     
177   C  CB    . ALA A 12  ? 0.3556 0.3856 0.5255 0.0595  0.0201  0.0458  11  ALA A CB    
183   N  N     . ASP A 13  ? 0.3079 0.3376 0.4435 0.0514  0.0192  0.0358  12  ASP A N     
184   C  CA    . ASP A 13  ? 0.3365 0.3649 0.4550 0.0487  0.0145  0.0342  12  ASP A CA    
185   C  C     . ASP A 13  ? 0.2753 0.3014 0.3867 0.0494  0.0084  0.0381  12  ASP A C     
186   O  O     . ASP A 13  ? 0.2776 0.3056 0.3969 0.0510  0.0039  0.0440  12  ASP A O     
187   C  CB    . ASP A 13  ? 0.4457 0.4790 0.5639 0.0466  0.0099  0.0347  12  ASP A CB    
188   C  CG    . ASP A 13  ? 0.4992 0.5381 0.6308 0.0481  0.0048  0.0406  12  ASP A CG    
189   O  OD1   . ASP A 13  ? 0.5019 0.5454 0.6476 0.0487  0.0082  0.0408  12  ASP A OD1   
190   O  OD2   . ASP A 13  ? 0.5358 0.5751 0.6642 0.0483  -0.0027 0.0451  12  ASP A OD2   
195   N  N     . GLY A 14  ? 0.2450 0.2673 0.3420 0.0478  0.0084  0.0349  13  GLY A N     
196   C  CA    . GLY A 14  ? 0.2853 0.3059 0.3730 0.0473  0.0032  0.0376  13  GLY A CA    
197   C  C     . GLY A 14  ? 0.2260 0.2427 0.3143 0.0485  0.0051  0.0402  13  GLY A C     
198   O  O     . GLY A 14  ? 0.2916 0.3068 0.3713 0.0475  0.0010  0.0427  13  GLY A O     
202   N  N     . VAL A 15  ? 0.2442 0.2585 0.3420 0.0503  0.0113  0.0395  14  VAL A N     
203   C  CA    . VAL A 15  ? 0.2211 0.2307 0.3209 0.0515  0.0129  0.0425  14  VAL A CA    
204   C  C     . VAL A 15  ? 0.2119 0.2170 0.2990 0.0495  0.0163  0.0383  14  VAL A C     
205   O  O     . VAL A 15  ? 0.2398 0.2408 0.3253 0.0495  0.0167  0.0411  14  VAL A O     
206   C  CB    . VAL A 15  ? 0.2662 0.2741 0.3822 0.0544  0.0187  0.0429  14  VAL A CB    
207   C  CG1   . VAL A 15  ? 0.2667 0.2798 0.3985 0.0568  0.0152  0.0478  14  VAL A CG1   
208   C  CG2   . VAL A 15  ? 0.2182 0.2248 0.3334 0.0533  0.0270  0.0351  14  VAL A CG2   
218   N  N     . GLY A 16  ? 0.2063 0.2122 0.2857 0.0476  0.0189  0.0321  15  GLY A N     
219   C  CA    . GLY A 16  ? 0.2242 0.2270 0.2933 0.0457  0.0220  0.0279  15  GLY A CA    
220   C  C     . GLY A 16  ? 0.2201 0.2200 0.2908 0.0448  0.0293  0.0226  15  GLY A C     
221   O  O     . GLY A 16  ? 0.1988 0.1955 0.2640 0.0433  0.0322  0.0204  15  GLY A O     
225   N  N     . LYS A 17  ? 0.1984 0.1996 0.2761 0.0452  0.0324  0.0206  16  LYS A N     
226   C  CA    . LYS A 17  ? 0.1697 0.1681 0.2465 0.0433  0.0393  0.0149  16  LYS A CA    
227   C  C     . LYS A 17  ? 0.1983 0.1970 0.2627 0.0401  0.0386  0.0108  16  LYS A C     
228   O  O     . LYS A 17  ? 0.2147 0.2100 0.2748 0.0381  0.0424  0.0076  16  LYS A O     
229   C  CB    . LYS A 17  ? 0.1977 0.1988 0.2817 0.0432  0.0423  0.0130  16  LYS A CB    
230   C  CG    . LYS A 17  ? 0.2209 0.2228 0.3201 0.0465  0.0437  0.0165  16  LYS A CG    
231   C  CD    . LYS A 17  ? 0.2290 0.2343 0.3363 0.0460  0.0476  0.0141  16  LYS A CD    
232   C  CE    . LYS A 17  ? 0.2320 0.2427 0.3349 0.0445  0.0424  0.0150  16  LYS A CE    
233   N  NZ    . LYS A 17  ? 0.2636 0.2784 0.3721 0.0471  0.0348  0.0212  16  LYS A NZ    
247   N  N     . SER A 18  ? 0.1823 0.1849 0.2416 0.0396  0.0336  0.0108  17  SER A N     
248   C  CA    . SER A 18  ? 0.1972 0.2004 0.2470 0.0370  0.0323  0.0072  17  SER A CA    
249   C  C     . SER A 18  ? 0.2023 0.2046 0.2466 0.0370  0.0310  0.0074  17  SER A C     
250   O  O     . SER A 18  ? 0.1972 0.1987 0.2367 0.0348  0.0329  0.0042  17  SER A O     
251   C  CB    . SER A 18  ? 0.1871 0.1938 0.2343 0.0368  0.0271  0.0074  17  SER A CB    
252   O  OG    . SER A 18  ? 0.2121 0.2198 0.2639 0.0360  0.0289  0.0071  17  SER A OG    
257   N  N     . ALA A 19  ? 0.2201 0.2230 0.2648 0.0388  0.0278  0.0113  18  ALA A N     
258   C  CA    . ALA A 19  ? 0.1789 0.1813 0.2178 0.0380  0.0273  0.0113  18  ALA A CA    
259   C  C     . ALA A 19  ? 0.1938 0.1921 0.2338 0.0369  0.0326  0.0106  18  ALA A C     
260   O  O     . ALA A 19  ? 0.2130 0.2111 0.2479 0.0349  0.0340  0.0081  18  ALA A O     
261   C  CB    . ALA A 19  ? 0.2333 0.2366 0.2712 0.0392  0.0231  0.0159  18  ALA A CB    
267   N  N     . LEU A 20  ? 0.1948 0.1896 0.2422 0.0380  0.0357  0.0124  19  LEU A N     
268   C  CA    . LEU A 20  ? 0.1934 0.1831 0.2424 0.0368  0.0411  0.0112  19  LEU A CA    
269   C  C     . LEU A 20  ? 0.2043 0.1937 0.2490 0.0336  0.0446  0.0052  19  LEU A C     
270   O  O     . LEU A 20  ? 0.2198 0.2075 0.2603 0.0312  0.0466  0.0032  19  LEU A O     
271   C  CB    . LEU A 20  ? 0.2135 0.1993 0.2731 0.0390  0.0442  0.0136  19  LEU A CB    
272   C  CG    . LEU A 20  ? 0.2392 0.2237 0.3041 0.0416  0.0409  0.0205  19  LEU A CG    
273   C  CD1   . LEU A 20  ? 0.2318 0.2131 0.3103 0.0445  0.0435  0.0230  19  LEU A CD1   
274   C  CD2   . LEU A 20  ? 0.2338 0.2146 0.2936 0.0399  0.0411  0.0227  19  LEU A CD2   
286   N  N     . THR A 21  ? 0.1896 0.1808 0.2350 0.0331  0.0450  0.0026  20  THR A N     
287   C  CA    . THR A 21  ? 0.2093 0.2003 0.2497 0.0294  0.0475  -0.0024 20  THR A CA    
288   C  C     . THR A 21  ? 0.2188 0.2132 0.2520 0.0276  0.0438  -0.0039 20  THR A C     
289   O  O     . THR A 21  ? 0.2279 0.2212 0.2574 0.0244  0.0458  -0.0069 20  THR A O     
290   C  CB    . THR A 21  ? 0.1894 0.1821 0.2311 0.0289  0.0476  -0.0037 20  THR A CB    
291   O  OG1   . THR A 21  ? 0.2189 0.2088 0.2690 0.0305  0.0524  -0.0033 20  THR A OG1   
292   C  CG2   . THR A 21  ? 0.2173 0.2098 0.2523 0.0244  0.0491  -0.0081 20  THR A CG2   
300   N  N     . ILE A 22  ? 0.1854 0.1839 0.2172 0.0295  0.0384  -0.0021 21  ILE A N     
301   C  CA    . ILE A 22  ? 0.2332 0.2354 0.2604 0.0284  0.0352  -0.0038 21  ILE A CA    
302   C  C     . ILE A 22  ? 0.2138 0.2157 0.2397 0.0277  0.0369  -0.0038 21  ILE A C     
303   O  O     . ILE A 22  ? 0.2287 0.2327 0.2522 0.0255  0.0369  -0.0064 21  ILE A O     
304   C  CB    . ILE A 22  ? 0.2289 0.2348 0.2558 0.0307  0.0298  -0.0025 21  ILE A CB    
305   C  CG1   . ILE A 22  ? 0.2559 0.2623 0.2835 0.0305  0.0277  -0.0026 21  ILE A CG1   
306   C  CG2   . ILE A 22  ? 0.2421 0.2516 0.2662 0.0304  0.0271  -0.0046 21  ILE A CG2   
307   C  CD1   . ILE A 22  ? 0.3282 0.3343 0.3532 0.0271  0.0286  -0.0053 21  ILE A CD1   
319   N  N     . GLN A 23  ? 0.2038 0.2030 0.2315 0.0291  0.0384  -0.0006 22  GLN A N     
320   C  CA    . GLN A 23  ? 0.2385 0.2365 0.2643 0.0275  0.0407  -0.0003 22  GLN A CA    
321   C  C     . GLN A 23  ? 0.2609 0.2557 0.2867 0.0242  0.0451  -0.0033 22  GLN A C     
322   O  O     . GLN A 23  ? 0.2442 0.2407 0.2676 0.0215  0.0460  -0.0054 22  GLN A O     
323   C  CB    . GLN A 23  ? 0.2737 0.2683 0.3012 0.0290  0.0412  0.0046  22  GLN A CB    
324   C  CG    . GLN A 23  ? 0.2936 0.2910 0.3176 0.0299  0.0377  0.0074  22  GLN A CG    
325   C  CD    . GLN A 23  ? 0.2954 0.2965 0.3142 0.0276  0.0381  0.0050  22  GLN A CD    
326   O  OE1   . GLN A 23  ? 0.2676 0.2699 0.2863 0.0253  0.0407  0.0015  22  GLN A OE1   
327   N  NE2   . GLN A 23  ? 0.2600 0.2635 0.2747 0.0279  0.0358  0.0068  22  GLN A NE2   
336   N  N     . LEU A 24  ? 0.2227 0.2127 0.2517 0.0241  0.0483  -0.0037 23  LEU A N     
337   C  CA    . LEU A 24  ? 0.2558 0.2419 0.2839 0.0204  0.0528  -0.0074 23  LEU A CA    
338   C  C     . LEU A 24  ? 0.2739 0.2644 0.2973 0.0171  0.0509  -0.0112 23  LEU A C     
339   O  O     . LEU A 24  ? 0.2538 0.2443 0.2751 0.0135  0.0523  -0.0135 23  LEU A O     
340   C  CB    . LEU A 24  ? 0.2636 0.2446 0.2957 0.0208  0.0569  -0.0084 23  LEU A CB    
341   C  CG    . LEU A 24  ? 0.2663 0.2419 0.2969 0.0164  0.0625  -0.0130 23  LEU A CG    
342   C  CD1   . LEU A 24  ? 0.3216 0.2913 0.3546 0.0158  0.0660  -0.0119 23  LEU A CD1   
343   C  CD2   . LEU A 24  ? 0.2899 0.2623 0.3235 0.0165  0.0665  -0.0154 23  LEU A CD2   
355   N  N     . ILE A 25  ? 0.2429 0.2371 0.2655 0.0180  0.0473  -0.0115 24  ILE A N     
356   C  CA    . ILE A 25  ? 0.2528 0.2499 0.2715 0.0145  0.0451  -0.0145 24  ILE A CA    
357   C  C     . ILE A 25  ? 0.2779 0.2810 0.2964 0.0147  0.0410  -0.0146 24  ILE A C     
358   O  O     . ILE A 25  ? 0.2852 0.2906 0.3022 0.0111  0.0403  -0.0168 24  ILE A O     
359   C  CB    . ILE A 25  ? 0.2663 0.2644 0.2841 0.0149  0.0428  -0.0144 24  ILE A CB    
360   C  CG1   . ILE A 25  ? 0.2810 0.2738 0.2999 0.0144  0.0480  -0.0152 24  ILE A CG1   
361   C  CG2   . ILE A 25  ? 0.3000 0.3008 0.3133 0.0109  0.0394  -0.0164 24  ILE A CG2   
362   C  CD1   . ILE A 25  ? 0.2506 0.2389 0.2661 0.0092  0.0532  -0.0193 24  ILE A CD1   
374   N  N     . GLN A 26  ? 0.2467 0.2529 0.2671 0.0185  0.0383  -0.0124 25  GLN A N     
375   C  CA    . GLN A 26  ? 0.2490 0.2614 0.2704 0.0192  0.0346  -0.0132 25  GLN A CA    
376   C  C     . GLN A 26  ? 0.2830 0.2971 0.3051 0.0204  0.0362  -0.0124 25  GLN A C     
377   O  O     . GLN A 26  ? 0.3032 0.3228 0.3270 0.0209  0.0343  -0.0139 25  GLN A O     
378   C  CB    . GLN A 26  ? 0.2595 0.2744 0.2818 0.0221  0.0297  -0.0125 25  GLN A CB    
379   C  CG    . GLN A 26  ? 0.2900 0.3036 0.3107 0.0201  0.0277  -0.0129 25  GLN A CG    
380   C  CD    . GLN A 26  ? 0.3796 0.3946 0.4011 0.0225  0.0227  -0.0117 25  GLN A CD    
381   O  OE1   . GLN A 26  ? 0.4123 0.4296 0.4359 0.0257  0.0204  -0.0113 25  GLN A OE1   
382   N  NE2   . GLN A 26  ? 0.4593 0.4727 0.4785 0.0203  0.0213  -0.0113 25  GLN A NE2   
391   N  N     . ASN A 27  ? 0.2459 0.2556 0.2672 0.0209  0.0395  -0.0100 26  ASN A N     
392   C  CA    . ASN A 27  ? 0.3050 0.3152 0.3252 0.0208  0.0413  -0.0085 26  ASN A CA    
393   C  C     . ASN A 27  ? 0.3141 0.3288 0.3334 0.0233  0.0384  -0.0081 26  ASN A C     
394   O  O     . ASN A 27  ? 0.3181 0.3365 0.3364 0.0224  0.0394  -0.0092 26  ASN A O     
395   C  CB    . ASN A 27  ? 0.2853 0.2977 0.3059 0.0170  0.0440  -0.0109 26  ASN A CB    
396   C  CG    . ASN A 27  ? 0.3478 0.3560 0.3668 0.0150  0.0481  -0.0084 26  ASN A CG    
397   O  OD1   . ASN A 27  ? 0.3572 0.3595 0.3765 0.0131  0.0510  -0.0080 26  ASN A OD1   
398   N  ND2   . ASN A 27  ? 0.3073 0.3183 0.3242 0.0151  0.0485  -0.0071 26  ASN A ND2   
405   N  N     . HIS A 28  ? 0.2801 0.2941 0.2994 0.0262  0.0351  -0.0068 27  HIS A N     
406   C  CA    . HIS A 28  ? 0.3706 0.3869 0.3878 0.0281  0.0328  -0.0061 27  HIS A CA    
407   C  C     . HIS A 28  ? 0.3224 0.3356 0.3395 0.0303  0.0303  -0.0026 27  HIS A C     
408   O  O     . HIS A 28  ? 0.2714 0.2817 0.2912 0.0308  0.0304  -0.0015 27  HIS A O     
409   C  CB    . HIS A 28  ? 0.3913 0.4129 0.4102 0.0291  0.0302  -0.0099 27  HIS A CB    
410   C  CG    . HIS A 28  ? 0.3590 0.3802 0.3804 0.0306  0.0265  -0.0104 27  HIS A CG    
411   N  ND1   . HIS A 28  ? 0.4535 0.4739 0.4744 0.0329  0.0230  -0.0093 27  HIS A ND1   
412   C  CD2   . HIS A 28  ? 0.3968 0.4180 0.4205 0.0294  0.0256  -0.0115 27  HIS A CD2   
413   C  CE1   . HIS A 28  ? 0.4238 0.4437 0.4468 0.0331  0.0203  -0.0097 27  HIS A CE1   
414   N  NE2   . HIS A 28  ? 0.4809 0.5012 0.5051 0.0309  0.0218  -0.0109 27  HIS A NE2   
422   N  N     . PHE A 29  ? 0.3303 0.3446 0.3443 0.0313  0.0281  -0.0013 28  PHE A N     
423   C  CA    . PHE A 29  ? 0.3079 0.3196 0.3218 0.0329  0.0254  0.0029  28  PHE A CA    
424   C  C     . PHE A 29  ? 0.4140 0.4277 0.4281 0.0346  0.0211  0.0014  28  PHE A C     
425   O  O     . PHE A 29  ? 0.3954 0.4117 0.4064 0.0346  0.0197  -0.0013 28  PHE A O     
426   C  CB    . PHE A 29  ? 0.3157 0.3262 0.3248 0.0317  0.0254  0.0066  28  PHE A CB    
427   C  CG    . PHE A 29  ? 0.3272 0.3363 0.3360 0.0329  0.0213  0.0112  28  PHE A CG    
428   C  CD1   . PHE A 29  ? 0.3317 0.3380 0.3469 0.0345  0.0207  0.0149  28  PHE A CD1   
429   C  CD2   . PHE A 29  ? 0.3666 0.3775 0.3693 0.0322  0.0183  0.0114  28  PHE A CD2   
430   C  CE1   . PHE A 29  ? 0.3116 0.3177 0.3283 0.0356  0.0164  0.0194  28  PHE A CE1   
431   C  CE2   . PHE A 29  ? 0.3677 0.3778 0.3701 0.0327  0.0137  0.0158  28  PHE A CE2   
432   C  CZ    . PHE A 29  ? 0.3210 0.3290 0.3309 0.0345  0.0125  0.0202  28  PHE A CZ    
442   N  N     . VAL A 30  ? 0.4214 0.4338 0.4395 0.0359  0.0193  0.0030  29  VAL A N     
443   C  CA    . VAL A 30  ? 0.4554 0.4689 0.4741 0.0371  0.0150  0.0023  29  VAL A CA    
444   C  C     . VAL A 30  ? 0.4487 0.4620 0.4649 0.0375  0.0119  0.0056  29  VAL A C     
445   O  O     . VAL A 30  ? 0.4160 0.4279 0.4351 0.0379  0.0112  0.0100  29  VAL A O     
446   C  CB    . VAL A 30  ? 0.4317 0.4442 0.4551 0.0375  0.0148  0.0028  29  VAL A CB    
447   C  CG1   . VAL A 30  ? 0.4356 0.4482 0.4596 0.0361  0.0172  -0.0003 29  VAL A CG1   
448   C  CG2   . VAL A 30  ? 0.4551 0.4654 0.4825 0.0380  0.0164  0.0069  29  VAL A CG2   
458   N  N     . ASP A 31  ? 0.3868 0.4016 0.3979 0.0370  0.0101  0.0034  30  ASP A N     
459   C  CA    . ASP A 31  ? 0.4531 0.4676 0.4598 0.0363  0.0066  0.0060  30  ASP A CA    
460   C  C     . ASP A 31  ? 0.4451 0.4596 0.4545 0.0372  0.0020  0.0069  30  ASP A C     
461   O  O     . ASP A 31  ? 0.4758 0.4902 0.4842 0.0366  -0.0014 0.0108  30  ASP A O     
462   C  CB    . ASP A 31  ? 0.5532 0.5692 0.5526 0.0348  0.0074  0.0021  30  ASP A CB    
463   C  CG    . ASP A 31  ? 0.5837 0.5990 0.5756 0.0326  0.0049  0.0051  30  ASP A CG    
464   O  OD1   . ASP A 31  ? 0.7637 0.7800 0.7482 0.0306  0.0061  0.0017  30  ASP A OD1   
465   O  OD2   . ASP A 31  ? 0.7260 0.7402 0.7199 0.0326  0.0017  0.0109  30  ASP A OD2   
470   N  N     . GLU A 32  ? 0.4089 0.4236 0.4221 0.0383  0.0014  0.0040  31  GLU A N     
471   C  CA    . GLU A 32  ? 0.3777 0.3922 0.3934 0.0386  -0.0028 0.0046  31  GLU A CA    
472   C  C     . GLU A 32  ? 0.3795 0.3940 0.4019 0.0391  -0.0024 0.0086  31  GLU A C     
473   O  O     . GLU A 32  ? 0.3618 0.3759 0.3873 0.0393  0.0016  0.0096  31  GLU A O     
474   C  CB    . GLU A 32  ? 0.4134 0.4276 0.4299 0.0392  -0.0037 -0.0001 31  GLU A CB    
475   C  CG    . GLU A 32  ? 0.4092 0.4237 0.4210 0.0392  -0.0036 -0.0049 31  GLU A CG    
476   C  CD    . GLU A 32  ? 0.4152 0.4293 0.4302 0.0404  -0.0042 -0.0093 31  GLU A CD    
477   O  OE1   . GLU A 32  ? 0.4097 0.4238 0.4291 0.0407  -0.0042 -0.0083 31  GLU A OE1   
478   O  OE2   . GLU A 32  ? 0.4622 0.4762 0.4757 0.0409  -0.0048 -0.0137 31  GLU A OE2   
485   N  N     . TYR A 33  ? 0.2990 0.3141 0.3242 0.0389  -0.0062 0.0106  32  TYR A N     
486   C  CA    . TYR A 33  ? 0.2965 0.3125 0.3294 0.0391  -0.0055 0.0140  32  TYR A CA    
487   C  C     . TYR A 33  ? 0.2797 0.2954 0.3148 0.0385  -0.0055 0.0120  32  TYR A C     
488   O  O     . TYR A 33  ? 0.2485 0.2639 0.2827 0.0377  -0.0096 0.0113  32  TYR A O     
489   C  CB    . TYR A 33  ? 0.3093 0.3271 0.3452 0.0388  -0.0098 0.0183  32  TYR A CB    
490   C  CG    . TYR A 33  ? 0.3220 0.3418 0.3682 0.0394  -0.0086 0.0218  32  TYR A CG    
491   C  CD1   . TYR A 33  ? 0.3192 0.3385 0.3707 0.0405  -0.0030 0.0221  32  TYR A CD1   
492   C  CD2   . TYR A 33  ? 0.2941 0.3164 0.3451 0.0386  -0.0128 0.0243  32  TYR A CD2   
493   C  CE1   . TYR A 33  ? 0.3183 0.3396 0.3802 0.0411  -0.0009 0.0245  32  TYR A CE1   
494   C  CE2   . TYR A 33  ? 0.3332 0.3583 0.3951 0.0392  -0.0110 0.0271  32  TYR A CE2   
495   C  CZ    . TYR A 33  ? 0.3436 0.3682 0.4111 0.0405  -0.0048 0.0270  32  TYR A CZ    
496   O  OH    . TYR A 33  ? 0.3888 0.4164 0.4683 0.0411  -0.0022 0.0291  32  TYR A OH    
506   N  N     . ASP A 34  ? 0.3203 0.3354 0.3575 0.0383  -0.0010 0.0110  33  ASP A N     
507   C  CA    . ASP A 34  ? 0.2901 0.3047 0.3281 0.0367  -0.0004 0.0096  33  ASP A CA    
508   C  C     . ASP A 34  ? 0.3293 0.3449 0.3735 0.0361  0.0037  0.0115  33  ASP A C     
509   O  O     . ASP A 34  ? 0.2662 0.2809 0.3110 0.0357  0.0088  0.0103  33  ASP A O     
510   C  CB    . ASP A 34  ? 0.3052 0.3183 0.3389 0.0361  0.0013  0.0062  33  ASP A CB    
511   C  CG    . ASP A 34  ? 0.3555 0.3676 0.3882 0.0338  0.0003  0.0053  33  ASP A CG    
512   O  OD1   . ASP A 34  ? 0.3514 0.3636 0.3859 0.0325  -0.0017 0.0069  33  ASP A OD1   
513   O  OD2   . ASP A 34  ? 0.4225 0.4339 0.4525 0.0328  0.0012  0.0033  33  ASP A OD2   
518   N  N     . PRO A 35  ? 0.2725 0.2903 0.3224 0.0360  0.0020  0.0142  34  PRO A N     
519   C  CA    . PRO A 35  ? 0.2864 0.3059 0.3445 0.0359  0.0068  0.0157  34  PRO A CA    
520   C  C     . PRO A 35  ? 0.2727 0.2909 0.3287 0.0332  0.0113  0.0129  34  PRO A C     
521   O  O     . PRO A 35  ? 0.2726 0.2900 0.3237 0.0308  0.0089  0.0119  34  PRO A O     
522   C  CB    . PRO A 35  ? 0.3095 0.3325 0.3741 0.0357  0.0031  0.0188  34  PRO A CB    
523   C  CG    . PRO A 35  ? 0.2551 0.2770 0.3132 0.0345  -0.0029 0.0181  34  PRO A CG    
524   C  CD    . PRO A 35  ? 0.2950 0.3140 0.3450 0.0357  -0.0040 0.0158  34  PRO A CD    
532   N  N     . THR A 36  ? 0.2750 0.2926 0.3344 0.0332  0.0178  0.0118  35  THR A N     
533   C  CA    . THR A 36  ? 0.2196 0.2353 0.2747 0.0300  0.0227  0.0084  35  THR A CA    
534   C  C     . THR A 36  ? 0.2253 0.2427 0.2830 0.0268  0.0256  0.0081  35  THR A C     
535   O  O     . THR A 36  ? 0.2034 0.2239 0.2706 0.0278  0.0275  0.0098  35  THR A O     
536   C  CB    . THR A 36  ? 0.1954 0.2090 0.2531 0.0311  0.0290  0.0068  35  THR A CB    
537   O  OG1   . THR A 36  ? 0.2152 0.2273 0.2695 0.0333  0.0263  0.0074  35  THR A OG1   
538   C  CG2   . THR A 36  ? 0.2550 0.2659 0.3069 0.0271  0.0345  0.0027  35  THR A CG2   
545   N  N     . ILE A 37  ? 0.2101 0.2258 0.2595 0.0225  0.0260  0.0061  36  ILE A N     
546   C  CA    . ILE A 37  ? 0.2282 0.2449 0.2777 0.0180  0.0304  0.0051  36  ILE A CA    
547   C  C     . ILE A 37  ? 0.2427 0.2575 0.2920 0.0165  0.0390  0.0013  36  ILE A C     
548   O  O     . ILE A 37  ? 0.2430 0.2595 0.3015 0.0175  0.0454  0.0003  36  ILE A O     
549   C  CB    . ILE A 37  ? 0.2278 0.2429 0.2675 0.0131  0.0264  0.0055  36  ILE A CB    
550   C  CG1   . ILE A 37  ? 0.2992 0.3145 0.3385 0.0145  0.0178  0.0085  36  ILE A CG1   
551   C  CG2   . ILE A 37  ? 0.2615 0.2777 0.3001 0.0076  0.0320  0.0044  36  ILE A CG2   
552   C  CD1   . ILE A 37  ? 0.2574 0.2762 0.3049 0.0154  0.0170  0.0109  36  ILE A CD1   
564   N  N     . GLU A 38  ? 0.2504 0.2618 0.2900 0.0142  0.0390  -0.0010 37  GLU A N     
565   C  CA    . GLU A 38  ? 0.2714 0.2800 0.3092 0.0124  0.0464  -0.0051 37  GLU A CA    
566   C  C     . GLU A 38  ? 0.2537 0.2594 0.2811 0.0105  0.0429  -0.0062 37  GLU A C     
567   O  O     . GLU A 38  ? 0.2564 0.2622 0.2765 0.0075  0.0374  -0.0049 37  GLU A O     
568   C  CB    . GLU A 38  ? 0.2546 0.2630 0.2900 0.0067  0.0537  -0.0082 37  GLU A CB    
569   C  CG    . GLU A 38  ? 0.2937 0.2989 0.3292 0.0054  0.0626  -0.0132 37  GLU A CG    
570   C  CD    . GLU A 38  ? 0.4184 0.4227 0.4482 -0.0016 0.0702  -0.0174 37  GLU A CD    
571   O  OE1   . GLU A 38  ? 0.4943 0.5010 0.5331 -0.0013 0.0766  -0.0188 37  GLU A OE1   
572   O  OE2   . GLU A 38  ? 0.4575 0.4591 0.4739 -0.0077 0.0697  -0.0194 37  GLU A OE2   
579   N  N     . ASP A 39  ? 0.2424 0.2459 0.2704 0.0122  0.0454  -0.0081 38  ASP A N     
580   C  CA    . ASP A 39  ? 0.2292 0.2310 0.2491 0.0103  0.0424  -0.0092 38  ASP A CA    
581   C  C     . ASP A 39  ? 0.2648 0.2630 0.2830 0.0081  0.0496  -0.0134 38  ASP A C     
582   O  O     . ASP A 39  ? 0.2471 0.2439 0.2731 0.0110  0.0551  -0.0143 38  ASP A O     
583   C  CB    . ASP A 39  ? 0.2585 0.2616 0.2810 0.0151  0.0366  -0.0068 38  ASP A CB    
584   C  CG    . ASP A 39  ? 0.2817 0.2873 0.3043 0.0167  0.0292  -0.0036 38  ASP A CG    
585   O  OD1   . ASP A 39  ? 0.2826 0.2881 0.2992 0.0135  0.0249  -0.0033 38  ASP A OD1   
586   O  OD2   . ASP A 39  ? 0.2833 0.2905 0.3122 0.0205  0.0278  -0.0014 38  ASP A OD2   
591   N  N     . SER A 40  ? 0.2659 0.2625 0.2746 0.0030  0.0488  -0.0155 39  SER A N     
592   C  CA    . SER A 40  ? 0.2445 0.2373 0.2498 -0.0002 0.0546  -0.0198 39  SER A CA    
593   C  C     . SER A 40  ? 0.2796 0.2726 0.2811 -0.0005 0.0500  -0.0196 39  SER A C     
594   O  O     . SER A 40  ? 0.2665 0.2623 0.2647 -0.0009 0.0426  -0.0172 39  SER A O     
595   C  CB    . SER A 40  ? 0.3122 0.3028 0.3080 -0.0081 0.0592  -0.0236 39  SER A CB    
596   O  OG    . SER A 40  ? 0.4249 0.4151 0.4253 -0.0083 0.0661  -0.0253 39  SER A OG    
602   N  N     . TYR A 41  ? 0.2735 0.2634 0.2766 -0.0003 0.0545  -0.0222 40  TYR A N     
603   C  CA    . TYR A 41  ? 0.2630 0.2535 0.2640 -0.0007 0.0512  -0.0222 40  TYR A CA    
604   C  C     . TYR A 41  ? 0.2680 0.2538 0.2646 -0.0056 0.0571  -0.0269 40  TYR A C     
605   O  O     . TYR A 41  ? 0.2651 0.2465 0.2630 -0.0068 0.0646  -0.0300 40  TYR A O     
606   C  CB    . TYR A 41  ? 0.2775 0.2693 0.2864 0.0057  0.0496  -0.0195 40  TYR A CB    
607   C  CG    . TYR A 41  ? 0.2567 0.2525 0.2696 0.0104  0.0441  -0.0155 40  TYR A CG    
608   C  CD1   . TYR A 41  ? 0.2770 0.2767 0.2882 0.0112  0.0371  -0.0137 40  TYR A CD1   
609   C  CD2   . TYR A 41  ? 0.2335 0.2290 0.2526 0.0140  0.0460  -0.0137 40  TYR A CD2   
610   C  CE1   . TYR A 41  ? 0.2994 0.3018 0.3139 0.0151  0.0324  -0.0108 40  TYR A CE1   
611   C  CE2   . TYR A 41  ? 0.2562 0.2552 0.2784 0.0176  0.0407  -0.0102 40  TYR A CE2   
612   C  CZ    . TYR A 41  ? 0.3248 0.3268 0.3439 0.0180  0.0341  -0.0090 40  TYR A CZ    
613   O  OH    . TYR A 41  ? 0.2970 0.3016 0.3186 0.0212  0.0290  -0.0064 40  TYR A OH    
623   N  N     . ARG A 42  ? 0.2793 0.2662 0.2719 -0.0085 0.0537  -0.0274 41  ARG A N     
624   C  CA    . ARG A 42  ? 0.2825 0.2652 0.2706 -0.0137 0.0582  -0.0317 41  ARG A CA    
625   C  C     . ARG A 42  ? 0.2282 0.2123 0.2203 -0.0117 0.0562  -0.0307 41  ARG A C     
626   O  O     . ARG A 42  ? 0.2455 0.2352 0.2393 -0.0095 0.0496  -0.0277 41  ARG A O     
627   C  CB    . ARG A 42  ? 0.3049 0.2881 0.2819 -0.0219 0.0556  -0.0338 41  ARG A CB    
628   C  CG    . ARG A 42  ? 0.3290 0.3095 0.2989 -0.0267 0.0595  -0.0362 41  ARG A CG    
629   C  CD    . ARG A 42  ? 0.3644 0.3380 0.3329 -0.0296 0.0696  -0.0421 41  ARG A CD    
630   N  NE    . ARG A 42  ? 0.3966 0.3676 0.3581 -0.0349 0.0750  -0.0455 41  ARG A NE    
631   C  CZ    . ARG A 42  ? 0.4230 0.3917 0.3713 -0.0443 0.0762  -0.0493 41  ARG A CZ    
632   N  NH1   . ARG A 42  ? 0.3992 0.3693 0.3402 -0.0493 0.0701  -0.0487 41  ARG A NH1   
633   N  NH2   . ARG A 42  ? 0.4790 0.4444 0.4215 -0.0492 0.0837  -0.0539 41  ARG A NH2   
647   N  N     . LYS A 43  ? 0.2540 0.2327 0.2479 -0.0123 0.0623  -0.0333 42  LYS A N     
648   C  CA    . LYS A 43  ? 0.2578 0.2374 0.2545 -0.0118 0.0611  -0.0325 42  LYS A CA    
649   C  C     . LYS A 43  ? 0.2597 0.2323 0.2540 -0.0166 0.0676  -0.0370 42  LYS A C     
650   O  O     . LYS A 43  ? 0.3186 0.2844 0.3152 -0.0158 0.0744  -0.0392 42  LYS A O     
651   C  CB    . LYS A 43  ? 0.2835 0.2640 0.2885 -0.0046 0.0608  -0.0285 42  LYS A CB    
652   C  CG    . LYS A 43  ? 0.3004 0.2819 0.3076 -0.0047 0.0603  -0.0276 42  LYS A CG    
653   C  CD    . LYS A 43  ? 0.3102 0.2904 0.3238 0.0009  0.0614  -0.0238 42  LYS A CD    
654   C  CE    . LYS A 43  ? 0.3508 0.3356 0.3652 0.0007  0.0587  -0.0222 42  LYS A CE    
655   N  NZ    . LYS A 43  ? 0.4149 0.3982 0.4334 0.0048  0.0597  -0.0183 42  LYS A NZ    
669   N  N     . GLN A 44  ? 0.3074 0.2814 0.2982 -0.0213 0.0655  -0.0384 43  GLN A N     
670   C  CA    . GLN A 44  ? 0.3230 0.2900 0.3119 -0.0261 0.0713  -0.0425 43  GLN A CA    
671   C  C     . GLN A 44  ? 0.3092 0.2749 0.3054 -0.0223 0.0726  -0.0400 43  GLN A C     
672   O  O     . GLN A 44  ? 0.3409 0.3133 0.3405 -0.0195 0.0678  -0.0362 43  GLN A O     
673   C  CB    . GLN A 44  ? 0.3556 0.3246 0.3363 -0.0345 0.0684  -0.0455 43  GLN A CB    
674   C  CG    . GLN A 44  ? 0.3691 0.3466 0.3524 -0.0346 0.0613  -0.0425 43  GLN A CG    
675   C  CD    . GLN A 44  ? 0.3886 0.3671 0.3656 -0.0435 0.0593  -0.0456 43  GLN A CD    
676   O  OE1   . GLN A 44  ? 0.3514 0.3232 0.3256 -0.0483 0.0645  -0.0495 43  GLN A OE1   
677   N  NE2   . GLN A 44  ? 0.3558 0.3423 0.3309 -0.0459 0.0514  -0.0437 43  GLN A NE2   
686   N  N     . VAL A 45  ? 0.3044 0.2610 0.3032 -0.0224 0.0795  -0.0421 44  VAL A N     
687   C  CA    . VAL A 45  ? 0.3872 0.3410 0.3925 -0.0193 0.0810  -0.0390 44  VAL A CA    
688   C  C     . VAL A 45  ? 0.4278 0.3717 0.4320 -0.0243 0.0874  -0.0433 44  VAL A C     
689   O  O     . VAL A 45  ? 0.4265 0.3645 0.4269 -0.0281 0.0920  -0.0487 44  VAL A O     
690   C  CB    . VAL A 45  ? 0.3896 0.3413 0.4028 -0.0116 0.0822  -0.0346 44  VAL A CB    
691   C  CG1   . VAL A 45  ? 0.3621 0.3227 0.3763 -0.0068 0.0761  -0.0305 44  VAL A CG1   
692   C  CG2   . VAL A 45  ? 0.3358 0.2794 0.3516 -0.0109 0.0886  -0.0378 44  VAL A CG2   
702   N  N     . VAL A 46  ? 0.3918 0.3334 0.3996 -0.0243 0.0880  -0.0410 45  VAL A N     
703   C  CA    . VAL A 46  ? 0.4760 0.4066 0.4845 -0.0281 0.0942  -0.0442 45  VAL A CA    
704   C  C     . VAL A 46  ? 0.4808 0.4035 0.4982 -0.0219 0.0979  -0.0408 45  VAL A C     
705   O  O     . VAL A 46  ? 0.4944 0.4197 0.5163 -0.0175 0.0950  -0.0344 45  VAL A O     
706   C  CB    . VAL A 46  ? 0.5181 0.4504 0.5249 -0.0332 0.0926  -0.0437 45  VAL A CB    
707   C  CG1   . VAL A 46  ? 0.5727 0.4924 0.5800 -0.0376 0.0991  -0.0475 45  VAL A CG1   
708   C  CG2   . VAL A 46  ? 0.5239 0.4653 0.5241 -0.0388 0.0878  -0.0462 45  VAL A CG2   
718   N  N     . ILE A 47  ? 0.4915 0.4046 0.5117 -0.0217 0.1044  -0.0450 46  ILE A N     
719   C  CA    . ILE A 47  ? 0.4919 0.3963 0.5227 -0.0161 0.1083  -0.0421 46  ILE A CA    
720   C  C     . ILE A 47  ? 0.5829 0.4744 0.6149 -0.0205 0.1151  -0.0469 46  ILE A C     
721   O  O     . ILE A 47  ? 0.5903 0.4770 0.6181 -0.0252 0.1203  -0.0548 46  ILE A O     
722   C  CB    . ILE A 47  ? 0.4527 0.3573 0.4892 -0.0107 0.1105  -0.0427 46  ILE A CB    
723   C  CG1   . ILE A 47  ? 0.4227 0.3395 0.4577 -0.0067 0.1035  -0.0379 46  ILE A CG1   
724   C  CG2   . ILE A 47  ? 0.4497 0.3456 0.4994 -0.0047 0.1141  -0.0394 46  ILE A CG2   
725   C  CD1   . ILE A 47  ? 0.3828 0.3015 0.4221 -0.0027 0.1053  -0.0391 46  ILE A CD1   
737   N  N     . ASP A 48  ? 0.5471 0.4325 0.5844 -0.0196 0.1152  -0.0423 47  ASP A N     
738   C  CA    . ASP A 48  ? 0.5474 0.4193 0.5868 -0.0237 0.1214  -0.0465 47  ASP A CA    
739   C  C     . ASP A 48  ? 0.5845 0.4569 0.6128 -0.0333 0.1226  -0.0537 47  ASP A C     
740   O  O     . ASP A 48  ? 0.5982 0.4615 0.6242 -0.0379 0.1289  -0.0616 47  ASP A O     
741   C  CB    . ASP A 48  ? 0.5414 0.4030 0.5902 -0.0199 0.1286  -0.0504 47  ASP A CB    
742   C  CG    . ASP A 48  ? 0.5134 0.3736 0.5753 -0.0108 0.1269  -0.0422 47  ASP A CG    
743   O  OD1   . ASP A 48  ? 0.5135 0.3766 0.5762 -0.0091 0.1212  -0.0339 47  ASP A OD1   
744   O  OD2   . ASP A 48  ? 0.5738 0.4306 0.6451 -0.0059 0.1309  -0.0440 47  ASP A OD2   
749   N  N     . GLY A 49  ? 0.5796 0.4627 0.6012 -0.0364 0.1164  -0.0511 48  GLY A N     
750   C  CA    . GLY A 49  ? 0.6093 0.4949 0.6213 -0.0455 0.1158  -0.0567 48  GLY A CA    
751   C  C     . GLY A 49  ? 0.6318 0.5200 0.6357 -0.0494 0.1168  -0.0638 48  GLY A C     
752   O  O     . GLY A 49  ? 0.6672 0.5573 0.6623 -0.0576 0.1157  -0.0684 48  GLY A O     
756   N  N     . GLU A 50  ? 0.6243 0.5128 0.6305 -0.0442 0.1186  -0.0645 49  GLU A N     
757   C  CA    . GLU A 50  ? 0.6187 0.5094 0.6164 -0.0481 0.1199  -0.0708 49  GLU A CA    
758   C  C     . GLU A 50  ? 0.6075 0.5119 0.6031 -0.0446 0.1126  -0.0662 49  GLU A C     
759   O  O     . GLU A 50  ? 0.5550 0.4629 0.5583 -0.0364 0.1108  -0.0606 49  GLU A O     
760   C  CB    . GLU A 50  ? 0.6252 0.5063 0.6274 -0.0457 0.1285  -0.0760 49  GLU A CB    
761   C  CG    . GLU A 50  ? 0.7345 0.6007 0.7431 -0.0465 0.1364  -0.0798 49  GLU A CG    
762   C  CD    . GLU A 50  ? 0.8523 0.7103 0.8510 -0.0562 0.1426  -0.0903 49  GLU A CD    
763   O  OE1   . GLU A 50  ? 0.8817 0.7332 0.8809 -0.0564 0.1504  -0.0972 49  GLU A OE1   
764   O  OE2   . GLU A 50  ? 0.8627 0.7212 0.8529 -0.0641 0.1399  -0.0920 49  GLU A OE2   
771   N  N     . THR A 51  ? 0.5469 0.4587 0.5323 -0.0510 0.1079  -0.0682 50  THR A N     
772   C  CA    . THR A 51  ? 0.5195 0.4430 0.5027 -0.0482 0.1010  -0.0644 50  THR A CA    
773   C  C     . THR A 51  ? 0.5019 0.4234 0.4822 -0.0474 0.1047  -0.0677 50  THR A C     
774   O  O     . THR A 51  ? 0.4840 0.3987 0.4575 -0.0537 0.1105  -0.0748 50  THR A O     
775   C  CB    . THR A 51  ? 0.5307 0.4627 0.5056 -0.0551 0.0940  -0.0646 50  THR A CB    
776   O  OG1   . THR A 51  ? 0.5581 0.4920 0.5364 -0.0566 0.0917  -0.0624 50  THR A OG1   
777   C  CG2   . THR A 51  ? 0.5014 0.4450 0.4763 -0.0513 0.0864  -0.0598 50  THR A CG2   
785   N  N     . CYS A 52  ? 0.4226 0.3500 0.4082 -0.0402 0.1019  -0.0629 51  CYS A N     
786   C  CA    . CYS A 52  ? 0.4724 0.3999 0.4560 -0.0393 0.1047  -0.0652 51  CYS A CA    
787   C  C     . CYS A 52  ? 0.3708 0.3091 0.3545 -0.0353 0.0969  -0.0594 51  CYS A C     
788   O  O     . CYS A 52  ? 0.3790 0.3240 0.3658 -0.0320 0.0901  -0.0539 51  CYS A O     
789   C  CB    . CYS A 52  ? 0.4850 0.4049 0.4793 -0.0333 0.1126  -0.0662 51  CYS A CB    
790   S  SG    . CYS A 52  ? 0.4984 0.4209 0.5065 -0.0230 0.1087  -0.0573 51  CYS A SG    
796   N  N     . LEU A 53  ? 0.3633 0.3027 0.3434 -0.0359 0.0984  -0.0610 52  LEU A N     
797   C  CA    . LEU A 53  ? 0.3444 0.2928 0.3235 -0.0331 0.0915  -0.0563 52  LEU A CA    
798   C  C     . LEU A 53  ? 0.3173 0.2654 0.3063 -0.0256 0.0947  -0.0541 52  LEU A C     
799   O  O     . LEU A 53  ? 0.3802 0.3229 0.3708 -0.0263 0.1026  -0.0585 52  LEU A O     
800   C  CB    . LEU A 53  ? 0.3924 0.3429 0.3583 -0.0412 0.0896  -0.0592 52  LEU A CB    
801   C  CG    . LEU A 53  ? 0.3825 0.3416 0.3460 -0.0399 0.0814  -0.0541 52  LEU A CG    
802   C  CD1   . LEU A 53  ? 0.3805 0.3468 0.3493 -0.0354 0.0726  -0.0482 52  LEU A CD1   
803   C  CD2   . LEU A 53  ? 0.4459 0.4057 0.3948 -0.0496 0.0792  -0.0568 52  LEU A CD2   
815   N  N     . LEU A 54  ? 0.3104 0.2640 0.3068 -0.0185 0.0890  -0.0476 53  LEU A N     
816   C  CA    . LEU A 54  ? 0.3141 0.2691 0.3198 -0.0115 0.0899  -0.0443 53  LEU A CA    
817   C  C     . LEU A 54  ? 0.3077 0.2693 0.3089 -0.0121 0.0855  -0.0426 53  LEU A C     
818   O  O     . LEU A 54  ? 0.2810 0.2484 0.2771 -0.0133 0.0778  -0.0398 53  LEU A O     
819   C  CB    . LEU A 54  ? 0.3147 0.2719 0.3294 -0.0045 0.0860  -0.0381 53  LEU A CB    
820   C  CG    . LEU A 54  ? 0.3235 0.2749 0.3422 -0.0039 0.0885  -0.0379 53  LEU A CG    
821   C  CD1   . LEU A 54  ? 0.3396 0.2933 0.3664 0.0029  0.0846  -0.0311 53  LEU A CD1   
822   C  CD2   . LEU A 54  ? 0.3630 0.3053 0.3862 -0.0047 0.0972  -0.0424 53  LEU A CD2   
834   N  N     . ASP A 55  ? 0.2880 0.2485 0.2918 -0.0116 0.0905  -0.0445 54  ASP A N     
835   C  CA    . ASP A 55  ? 0.2860 0.2520 0.2870 -0.0118 0.0870  -0.0424 54  ASP A CA    
836   C  C     . ASP A 55  ? 0.2785 0.2467 0.2927 -0.0039 0.0873  -0.0384 54  ASP A C     
837   O  O     . ASP A 55  ? 0.3336 0.2979 0.3565 -0.0016 0.0946  -0.0406 54  ASP A O     
838   C  CB    . ASP A 55  ? 0.3348 0.2985 0.3272 -0.0190 0.0929  -0.0480 54  ASP A CB    
839   C  CG    . ASP A 55  ? 0.4033 0.3724 0.3924 -0.0199 0.0894  -0.0454 54  ASP A CG    
840   O  OD1   . ASP A 55  ? 0.4210 0.3921 0.4201 -0.0148 0.0914  -0.0435 54  ASP A OD1   
841   O  OD2   . ASP A 55  ? 0.4368 0.4082 0.4142 -0.0258 0.0841  -0.0447 54  ASP A OD2   
846   N  N     . ILE A 56  ? 0.2823 0.2561 0.2987 0.0004  0.0792  -0.0325 55  ILE A N     
847   C  CA    . ILE A 56  ? 0.2470 0.2231 0.2751 0.0077  0.0778  -0.0279 55  ILE A CA    
848   C  C     . ILE A 56  ? 0.2318 0.2131 0.2597 0.0080  0.0747  -0.0258 55  ILE A C     
849   O  O     . ILE A 56  ? 0.2487 0.2337 0.2689 0.0058  0.0683  -0.0241 55  ILE A O     
850   C  CB    . ILE A 56  ? 0.2537 0.2318 0.2843 0.0120  0.0715  -0.0231 55  ILE A CB    
851   C  CG1   . ILE A 56  ? 0.3282 0.3020 0.3564 0.0102  0.0732  -0.0248 55  ILE A CG1   
852   C  CG2   . ILE A 56  ? 0.2549 0.2340 0.2973 0.0186  0.0708  -0.0185 55  ILE A CG2   
853   C  CD1   . ILE A 56  ? 0.3352 0.3023 0.3710 0.0116  0.0806  -0.0267 55  ILE A CD1   
865   N  N     . LEU A 57  ? 0.2361 0.2179 0.2733 0.0106  0.0790  -0.0257 56  LEU A N     
866   C  CA    . LEU A 57  ? 0.1958 0.1827 0.2353 0.0115  0.0763  -0.0231 56  LEU A CA    
867   C  C     . LEU A 57  ? 0.2254 0.2152 0.2760 0.0185  0.0719  -0.0174 56  LEU A C     
868   O  O     . LEU A 57  ? 0.2080 0.1960 0.2699 0.0225  0.0756  -0.0167 56  LEU A O     
869   C  CB    . LEU A 57  ? 0.2542 0.2405 0.2968 0.0087  0.0847  -0.0272 56  LEU A CB    
870   C  CG    . LEU A 57  ? 0.2513 0.2433 0.2950 0.0082  0.0820  -0.0246 56  LEU A CG    
871   C  CD1   . LEU A 57  ? 0.3062 0.2997 0.3357 0.0028  0.0762  -0.0239 56  LEU A CD1   
872   C  CD2   . LEU A 57  ? 0.3066 0.2988 0.3571 0.0065  0.0916  -0.0287 56  LEU A CD2   
884   N  N     . ASP A 58  ? 0.1989 0.1930 0.2464 0.0196  0.0638  -0.0135 57  ASP A N     
885   C  CA    . ASP A 58  ? 0.1982 0.1955 0.2530 0.0250  0.0582  -0.0082 57  ASP A CA    
886   C  C     . ASP A 58  ? 0.2049 0.2065 0.2643 0.0251  0.0573  -0.0066 57  ASP A C     
887   O  O     . ASP A 58  ? 0.2297 0.2330 0.2816 0.0216  0.0546  -0.0071 57  ASP A O     
888   C  CB    . ASP A 58  ? 0.2230 0.2216 0.2703 0.0255  0.0505  -0.0060 57  ASP A CB    
889   C  CG    . ASP A 58  ? 0.2150 0.2164 0.2675 0.0301  0.0448  -0.0012 57  ASP A CG    
890   O  OD1   . ASP A 58  ? 0.2239 0.2251 0.2858 0.0334  0.0464  0.0013  57  ASP A OD1   
891   O  OD2   . ASP A 58  ? 0.2185 0.2219 0.2653 0.0303  0.0386  0.0001  57  ASP A OD2   
896   N  N     . THR A 59  ? 0.2073 0.2106 0.2796 0.0290  0.0591  -0.0044 58  THR A N     
897   C  CA    . THR A 59  ? 0.2172 0.2249 0.2962 0.0285  0.0604  -0.0037 58  THR A CA    
898   C  C     . THR A 59  ? 0.2564 0.2688 0.3410 0.0319  0.0527  0.0019  58  THR A C     
899   O  O     . THR A 59  ? 0.2190 0.2310 0.3040 0.0351  0.0473  0.0054  58  THR A O     
900   C  CB    . THR A 59  ? 0.2443 0.2515 0.3361 0.0297  0.0695  -0.0062 58  THR A CB    
901   O  OG1   . THR A 59  ? 0.2257 0.2326 0.3300 0.0354  0.0681  -0.0024 58  THR A OG1   
902   C  CG2   . THR A 59  ? 0.2193 0.2209 0.3054 0.0260  0.0777  -0.0126 58  THR A CG2   
910   N  N     . ALA A 60  ? 0.2186 0.2353 0.3074 0.0305  0.0527  0.0026  59  ALA A N     
911   C  CA    . ALA A 60  ? 0.2675 0.2889 0.3627 0.0330  0.0458  0.0076  59  ALA A CA    
912   C  C     . ALA A 60  ? 0.3050 0.3293 0.4174 0.0372  0.0481  0.0103  59  ALA A C     
913   O  O     . ALA A 60  ? 0.2996 0.3246 0.4213 0.0370  0.0561  0.0075  59  ALA A O     
914   C  CB    . ALA A 60  ? 0.2569 0.2818 0.3497 0.0292  0.0446  0.0076  59  ALA A CB    
920   N  N     . GLY A 61  ? 0.3658 0.3919 0.4827 0.0406  0.0410  0.0155  60  GLY A N     
921   C  CA    . GLY A 61  ? 0.4032 0.4329 0.5373 0.0445  0.0408  0.0195  60  GLY A CA    
922   C  C     . GLY A 61  ? 0.4200 0.4570 0.5639 0.0440  0.0384  0.0220  60  GLY A C     
923   O  O     . GLY A 61  ? 0.4648 0.5060 0.6259 0.0470  0.0394  0.0249  60  GLY A O     
927   N  N     . GLN A 62  ? 0.3391 0.3776 0.4736 0.0402  0.0355  0.0210  61  GLN A N     
928   C  CA    . GLN A 62  ? 0.3833 0.4283 0.5251 0.0389  0.0320  0.0237  61  GLN A CA    
929   C  C     . GLN A 62  ? 0.3985 0.4493 0.5592 0.0400  0.0386  0.0235  61  GLN A C     
930   O  O     . GLN A 62  ? 0.3862 0.4365 0.5480 0.0378  0.0477  0.0186  61  GLN A O     
931   C  CB    . GLN A 62  ? 0.3267 0.3709 0.4557 0.0338  0.0310  0.0213  61  GLN A CB    
932   C  CG    . GLN A 62  ? 0.3644 0.4034 0.4766 0.0328  0.0249  0.0208  61  GLN A CG    
933   C  CD    . GLN A 62  ? 0.4053 0.4457 0.5165 0.0340  0.0155  0.0249  61  GLN A CD    
934   O  OE1   . GLN A 62  ? 0.4792 0.5248 0.5996 0.0339  0.0123  0.0281  61  GLN A OE1   
935   N  NE2   . GLN A 62  ? 0.4275 0.4635 0.5279 0.0351  0.0111  0.0247  61  GLN A NE2   
944   N  N     . GLU A 63  ? 0.4060 0.4626 0.5817 0.0429  0.0340  0.0288  62  GLU A N     
945   C  CA    . GLU A 63  ? 0.3823 0.4453 0.5795 0.0447  0.0402  0.0289  62  GLU A CA    
946   C  C     . GLU A 63  ? 0.3750 0.4431 0.5743 0.0400  0.0454  0.0257  62  GLU A C     
947   O  O     . GLU A 63  ? 0.3317 0.4034 0.5444 0.0402  0.0547  0.0226  62  GLU A O     
948   C  CB    . GLU A 63  ? 0.4292 0.4980 0.6423 0.0485  0.0323  0.0362  62  GLU A CB    
949   C  CG    . GLU A 63  ? 0.5206 0.5844 0.7336 0.0529  0.0281  0.0400  62  GLU A CG    
950   C  CD    . GLU A 63  ? 0.5830 0.6527 0.8149 0.0567  0.0214  0.0477  62  GLU A CD    
951   O  OE1   . GLU A 63  ? 0.6282 0.6975 0.8535 0.0566  0.0111  0.0532  62  GLU A OE1   
952   O  OE2   . GLU A 63  ? 0.6673 0.7422 0.9212 0.0595  0.0265  0.0481  62  GLU A OE2   
959   N  N     . GLU A 64  ? 0.3521 0.4202 0.5383 0.0356  0.0399  0.0263  63  GLU A N     
960   C  CA    . GLU A 64  ? 0.3624 0.4348 0.5490 0.0303  0.0442  0.0240  63  GLU A CA    
961   C  C     . GLU A 64  ? 0.3542 0.4233 0.5347 0.0270  0.0556  0.0173  63  GLU A C     
962   O  O     . GLU A 64  ? 0.3580 0.4319 0.5439 0.0231  0.0624  0.0148  63  GLU A O     
963   C  CB    . GLU A 64  ? 0.3827 0.4533 0.5542 0.0263  0.0353  0.0260  63  GLU A CB    
964   C  CG    . GLU A 64  ? 0.4000 0.4730 0.5673 0.0197  0.0379  0.0245  63  GLU A CG    
965   C  CD    . GLU A 64  ? 0.4451 0.5279 0.6296 0.0184  0.0375  0.0274  63  GLU A CD    
966   O  OE1   . GLU A 64  ? 0.4919 0.5778 0.6809 0.0196  0.0282  0.0322  63  GLU A OE1   
967   O  OE2   . GLU A 64  ? 0.4564 0.5441 0.6493 0.0156  0.0467  0.0245  63  GLU A OE2   
974   N  N     . TYR A 65  ? 0.2997 0.3611 0.4690 0.0280  0.0581  0.0142  64  TYR A N     
975   C  CA    . TYR A 65  ? 0.3757 0.4329 0.5356 0.0238  0.0678  0.0077  64  TYR A CA    
976   C  C     . TYR A 65  ? 0.3506 0.4059 0.5211 0.0275  0.0769  0.0039  64  TYR A C     
977   O  O     . TYR A 65  ? 0.3001 0.3496 0.4605 0.0248  0.0837  -0.0016 64  TYR A O     
978   C  CB    . TYR A 65  ? 0.3170 0.3667 0.4541 0.0207  0.0631  0.0068  64  TYR A CB    
979   C  CG    . TYR A 65  ? 0.2860 0.3366 0.4144 0.0179  0.0535  0.0107  64  TYR A CG    
980   C  CD1   . TYR A 65  ? 0.3315 0.3862 0.4603 0.0127  0.0549  0.0109  64  TYR A CD1   
981   C  CD2   . TYR A 65  ? 0.2666 0.3138 0.3874 0.0205  0.0436  0.0140  64  TYR A CD2   
982   C  CE1   . TYR A 65  ? 0.3002 0.3549 0.4220 0.0101  0.0462  0.0145  64  TYR A CE1   
983   C  CE2   . TYR A 65  ? 0.2759 0.3233 0.3901 0.0183  0.0353  0.0170  64  TYR A CE2   
984   C  CZ    . TYR A 65  ? 0.2144 0.2652 0.3291 0.0131  0.0365  0.0173  64  TYR A CZ    
985   O  OH    . TYR A 65  ? 0.2023 0.2523 0.3110 0.0107  0.0284  0.0202  64  TYR A OH    
995   N  N     . SER A 66  ? 0.3695 0.4296 0.5613 0.0331  0.0772  0.0066  65  SER A N     
996   C  CA    . SER A 66  ? 0.3667 0.4237 0.5698 0.0374  0.0847  0.0037  65  SER A CA    
997   C  C     . SER A 66  ? 0.3764 0.4333 0.5823 0.0338  0.0987  -0.0043 65  SER A C     
998   O  O     . SER A 66  ? 0.4339 0.4847 0.6397 0.0350  0.1060  -0.0092 65  SER A O     
999   C  CB    . SER A 66  ? 0.4059 0.4683 0.6330 0.0442  0.0814  0.0092  65  SER A CB    
1000  O  OG    . SER A 66  ? 0.3676 0.4401 0.6096 0.0435  0.0812  0.0113  65  SER A OG    
1006  N  N     . ALA A 67  ? 0.4059 0.4691 0.6133 0.0289  0.1029  -0.0062 66  ALA A N     
1007  C  CA    . ALA A 67  ? 0.4027 0.4662 0.6123 0.0247  0.1170  -0.0143 66  ALA A CA    
1008  C  C     . ALA A 67  ? 0.4286 0.4844 0.6125 0.0174  0.1205  -0.0197 66  ALA A C     
1009  O  O     . ALA A 67  ? 0.4865 0.5408 0.6686 0.0132  0.1326  -0.0272 66  ALA A O     
1010  C  CB    . ALA A 67  ? 0.3068 0.3804 0.5282 0.0215  0.1213  -0.0145 66  ALA A CB    
1016  N  N     . MET A 68  ? 0.3914 0.4424 0.5559 0.0157  0.1104  -0.0161 67  MET A N     
1017  C  CA    . MET A 68  ? 0.3963 0.4402 0.5374 0.0092  0.1119  -0.0200 67  MET A CA    
1018  C  C     . MET A 68  ? 0.4169 0.4525 0.5512 0.0122  0.1108  -0.0216 67  MET A C     
1019  O  O     . MET A 68  ? 0.4284 0.4582 0.5430 0.0076  0.1086  -0.0231 67  MET A O     
1020  C  CB    . MET A 68  ? 0.4310 0.4748 0.5557 0.0050  0.1016  -0.0153 67  MET A CB    
1021  C  CG    . MET A 68  ? 0.4605 0.5121 0.5951 0.0053  0.0968  -0.0103 67  MET A CG    
1022  S  SD    . MET A 68  ? 0.5017 0.5516 0.6160 -0.0015 0.0873  -0.0065 67  MET A SD    
1023  C  CE    . MET A 68  ? 0.4817 0.5272 0.5776 -0.0115 0.0967  -0.0128 67  MET A CE    
1033  N  N     . ARG A 69  ? 0.4084 0.4433 0.5587 0.0195  0.1116  -0.0206 68  ARG A N     
1034  C  CA    . ARG A 69  ? 0.3910 0.4178 0.5358 0.0219  0.1117  -0.0223 68  ARG A CA    
1035  C  C     . ARG A 69  ? 0.4067 0.4285 0.5496 0.0184  0.1244  -0.0311 68  ARG A C     
1036  O  O     . ARG A 69  ? 0.3859 0.4001 0.5189 0.0177  0.1253  -0.0338 68  ARG A O     
1037  C  CB    . ARG A 69  ? 0.4165 0.4436 0.5787 0.0305  0.1074  -0.0173 68  ARG A CB    
1038  C  CG    . ARG A 69  ? 0.4193 0.4496 0.5809 0.0338  0.0943  -0.0089 68  ARG A CG    
1039  C  CD    . ARG A 69  ? 0.3976 0.4300 0.5799 0.0415  0.0915  -0.0038 68  ARG A CD    
1040  N  NE    . ARG A 69  ? 0.4159 0.4526 0.5989 0.0438  0.0795  0.0040  68  ARG A NE    
1041  C  CZ    . ARG A 69  ? 0.4103 0.4519 0.6112 0.0489  0.0751  0.0099  68  ARG A CZ    
1042  N  NH1   . ARG A 69  ? 0.4042 0.4472 0.6259 0.0530  0.0814  0.0093  68  ARG A NH1   
1043  N  NH2   . ARG A 69  ? 0.4601 0.5050 0.6583 0.0497  0.0640  0.0164  68  ARG A NH2   
1057  N  N     . ASP A 70  ? 0.4129 0.4390 0.5652 0.0160  0.1346  -0.0358 69  ASP A N     
1058  C  CA    . ASP A 70  ? 0.4491 0.4700 0.6016 0.0131  0.1465  -0.0444 69  ASP A CA    
1059  C  C     . ASP A 70  ? 0.4630 0.4766 0.5917 0.0056  0.1495  -0.0498 69  ASP A C     
1060  O  O     . ASP A 70  ? 0.4942 0.4996 0.6187 0.0050  0.1526  -0.0543 69  ASP A O     
1061  C  CB    . ASP A 70  ? 0.4692 0.4954 0.6288 0.0094  0.1535  -0.0479 69  ASP A CB    
1062  C  CG    . ASP A 70  ? 0.5020 0.5361 0.6863 0.0164  0.1504  -0.0426 69  ASP A CG    
1063  O  OD1   . ASP A 70  ? 0.4528 0.4891 0.6473 0.0234  0.1417  -0.0353 69  ASP A OD1   
1064  O  OD2   . ASP A 70  ? 0.5250 0.5632 0.7182 0.0145  0.1563  -0.0455 69  ASP A OD2   
1069  N  N     . GLN A 71  ? 0.4623 0.4774 0.5722 -0.0011 0.1444  -0.0480 70  GLN A N     
1070  C  CA    . GLN A 71  ? 0.5062 0.5147 0.5929 -0.0096 0.1466  -0.0530 70  GLN A CA    
1071  C  C     . GLN A 71  ? 0.4534 0.4546 0.5339 -0.0068 0.1415  -0.0523 70  GLN A C     
1072  O  O     . GLN A 71  ? 0.4851 0.4795 0.5569 -0.0109 0.1480  -0.0589 70  GLN A O     
1073  C  CB    . GLN A 71  ? 0.5732 0.5840 0.6414 -0.0168 0.1392  -0.0492 70  GLN A CB    
1074  C  CG    . GLN A 71  ? 0.6346 0.6398 0.6790 -0.0273 0.1424  -0.0544 70  GLN A CG    
1075  C  CD    . GLN A 71  ? 0.6685 0.6690 0.7128 -0.0310 0.1567  -0.0645 70  GLN A CD    
1076  O  OE1   . GLN A 71  ? 0.6684 0.6620 0.7082 -0.0307 0.1581  -0.0681 70  GLN A OE1   
1077  N  NE2   . GLN A 71  ? 0.6617 0.6651 0.7102 -0.0349 0.1656  -0.0689 70  GLN A NE2   
1086  N  N     . TYR A 72  ? 0.4659 0.4682 0.5503 -0.0004 0.1302  -0.0447 71  TYR A N     
1087  C  CA    . TYR A 72  ? 0.4125 0.4083 0.4899 0.0013  0.1258  -0.0442 71  TYR A CA    
1088  C  C     . TYR A 72  ? 0.4403 0.4316 0.5330 0.0071  0.1322  -0.0470 71  TYR A C     
1089  O  O     . TYR A 72  ? 0.3740 0.3583 0.4600 0.0060  0.1335  -0.0499 71  TYR A O     
1090  C  CB    . TYR A 72  ? 0.3964 0.3947 0.4704 0.0050  0.1123  -0.0360 71  TYR A CB    
1091  C  CG    . TYR A 72  ? 0.3737 0.3762 0.4649 0.0134  0.1069  -0.0297 71  TYR A CG    
1092  C  CD1   . TYR A 72  ? 0.3934 0.3932 0.4984 0.0198  0.1090  -0.0290 71  TYR A CD1   
1093  C  CD2   . TYR A 72  ? 0.3613 0.3700 0.4538 0.0145  0.0992  -0.0239 71  TYR A CD2   
1094  C  CE1   . TYR A 72  ? 0.3428 0.3464 0.4621 0.0267  0.1031  -0.0225 71  TYR A CE1   
1095  C  CE2   . TYR A 72  ? 0.4025 0.4150 0.5090 0.0213  0.0936  -0.0180 71  TYR A CE2   
1096  C  CZ    . TYR A 72  ? 0.3939 0.4041 0.5136 0.0273  0.0954  -0.0171 71  TYR A CZ    
1097  O  OH    . TYR A 72  ? 0.3987 0.4126 0.5314 0.0334  0.0890  -0.0106 71  TYR A OH    
1107  N  N     . MET A 73  ? 0.4357 0.4308 0.5495 0.0130  0.1362  -0.0460 72  MET A N     
1108  C  CA    . MET A 73  ? 0.3853 0.3749 0.5130 0.0175  0.1415  -0.0485 72  MET A CA    
1109  C  C     . MET A 73  ? 0.4212 0.4044 0.5407 0.0106  0.1505  -0.0573 72  MET A C     
1110  O  O     . MET A 73  ? 0.3709 0.3463 0.4916 0.0111  0.1529  -0.0601 72  MET A O     
1111  C  CB    . MET A 73  ? 0.3487 0.3434 0.4991 0.0244  0.1397  -0.0436 72  MET A CB    
1112  C  CG    . MET A 73  ? 0.3368 0.3385 0.4951 0.0305  0.1300  -0.0346 72  MET A CG    
1113  S  SD    . MET A 73  ? 0.3603 0.3686 0.5450 0.0375  0.1268  -0.0285 72  MET A SD    
1114  C  CE    . MET A 73  ? 0.3900 0.4028 0.5777 0.0435  0.1138  -0.0180 72  MET A CE    
1124  N  N     . ARG A 74  ? 0.4287 0.4150 0.5389 0.0035  0.1554  -0.0616 73  ARG A N     
1125  C  CA    . ARG A 74  ? 0.4581 0.4383 0.5588 -0.0040 0.1638  -0.0701 73  ARG A CA    
1126  C  C     . ARG A 74  ? 0.4277 0.3999 0.5103 -0.0089 0.1631  -0.0734 73  ARG A C     
1127  O  O     . ARG A 74  ? 0.4416 0.4060 0.5235 -0.0109 0.1679  -0.0787 73  ARG A O     
1128  C  CB    . ARG A 74  ? 0.5149 0.5002 0.6067 -0.0115 0.1681  -0.0732 73  ARG A CB    
1129  C  CG    . ARG A 74  ? 0.6236 0.6053 0.7160 -0.0166 0.1778  -0.0812 73  ARG A CG    
1130  C  CD    . ARG A 74  ? 0.6472 0.6365 0.7470 -0.0184 0.1823  -0.0820 73  ARG A CD    
1131  N  NE    . ARG A 74  ? 0.6634 0.6610 0.7576 -0.0199 0.1772  -0.0765 73  ARG A NE    
1132  C  CZ    . ARG A 74  ? 0.6484 0.6548 0.7580 -0.0152 0.1753  -0.0717 73  ARG A CZ    
1133  N  NH1   . ARG A 74  ? 0.6184 0.6273 0.7506 -0.0087 0.1778  -0.0713 73  ARG A NH1   
1134  N  NH2   . ARG A 74  ? 0.6450 0.6580 0.7478 -0.0176 0.1707  -0.0668 73  ARG A NH2   
1148  N  N     . THR A 75  ? 0.4292 0.4034 0.4976 -0.0111 0.1571  -0.0703 74  THR A N     
1149  C  CA    . THR A 75  ? 0.4465 0.4145 0.4965 -0.0168 0.1559  -0.0733 74  THR A CA    
1150  C  C     . THR A 75  ? 0.4416 0.4050 0.4973 -0.0106 0.1516  -0.0705 74  THR A C     
1151  O  O     . THR A 75  ? 0.4319 0.3886 0.4768 -0.0148 0.1525  -0.0742 74  THR A O     
1152  C  CB    . THR A 75  ? 0.4964 0.4686 0.5280 -0.0227 0.1486  -0.0698 74  THR A CB    
1153  O  OG1   . THR A 75  ? 0.5328 0.5115 0.5724 -0.0160 0.1381  -0.0606 74  THR A OG1   
1154  C  CG2   . THR A 75  ? 0.5661 0.5407 0.5867 -0.0318 0.1549  -0.0742 74  THR A CG2   
1162  N  N     . GLY A 76  ? 0.3885 0.3554 0.4600 -0.0014 0.1464  -0.0636 75  GLY A N     
1163  C  CA    . GLY A 76  ? 0.3149 0.2774 0.3905 0.0038  0.1410  -0.0597 75  GLY A CA    
1164  C  C     . GLY A 76  ? 0.3724 0.3264 0.4561 0.0048  0.1475  -0.0641 75  GLY A C     
1165  O  O     . GLY A 76  ? 0.3819 0.3349 0.4769 0.0056  0.1528  -0.0665 75  GLY A O     
1169  N  N     . GLU A 77  ? 0.2909 0.2385 0.3684 0.0042  0.1458  -0.0646 76  GLU A N     
1170  C  CA    . GLU A 77  ? 0.3332 0.2718 0.4167 0.0043  0.1503  -0.0678 76  GLU A CA    
1171  C  C     . GLU A 77  ? 0.3413 0.2782 0.4426 0.0133  0.1467  -0.0612 76  GLU A C     
1172  O  O     . GLU A 77  ? 0.3436 0.2752 0.4570 0.0152  0.1508  -0.0624 76  GLU A O     
1173  C  CB    . GLU A 77  ? 0.3534 0.2853 0.4207 -0.0022 0.1511  -0.0724 76  GLU A CB    
1174  C  CG    . GLU A 77  ? 0.4351 0.3657 0.4845 -0.0127 0.1556  -0.0800 76  GLU A CG    
1175  C  CD    . GLU A 77  ? 0.4470 0.3713 0.4814 -0.0192 0.1552  -0.0839 76  GLU A CD    
1176  O  OE1   . GLU A 77  ? 0.4193 0.3458 0.4470 -0.0185 0.1481  -0.0798 76  GLU A OE1   
1177  O  OE2   . GLU A 77  ? 0.5688 0.4863 0.5984 -0.0253 0.1610  -0.0905 76  GLU A OE2   
1184  N  N     . GLY A 78  ? 0.2809 0.2223 0.3840 0.0184  0.1391  -0.0539 77  GLY A N     
1185  C  CA    . GLY A 78  ? 0.3154 0.2552 0.4334 0.0262  0.1346  -0.0466 77  GLY A CA    
1186  C  C     . GLY A 78  ? 0.2927 0.2416 0.4123 0.0303  0.1251  -0.0382 77  GLY A C     
1187  O  O     . GLY A 78  ? 0.2576 0.2122 0.3632 0.0265  0.1199  -0.0375 77  GLY A O     
1191  N  N     . PHE A 79  ? 0.2555 0.2056 0.3912 0.0375  0.1214  -0.0313 78  PHE A N     
1192  C  CA    . PHE A 79  ? 0.2626 0.2218 0.4006 0.0408  0.1122  -0.0235 78  PHE A CA    
1193  C  C     . PHE A 79  ? 0.2725 0.2305 0.4135 0.0450  0.1036  -0.0149 78  PHE A C     
1194  O  O     . PHE A 79  ? 0.2542 0.2065 0.4082 0.0489  0.1053  -0.0124 78  PHE A O     
1195  C  CB    . PHE A 79  ? 0.2823 0.2469 0.4377 0.0446  0.1153  -0.0229 78  PHE A CB    
1196  C  CG    . PHE A 79  ? 0.2462 0.2130 0.3964 0.0391  0.1228  -0.0307 78  PHE A CG    
1197  C  CD1   . PHE A 79  ? 0.3146 0.2752 0.4653 0.0355  0.1310  -0.0378 78  PHE A CD1   
1198  C  CD2   . PHE A 79  ? 0.2956 0.2701 0.4376 0.0364  0.1205  -0.0307 78  PHE A CD2   
1199  C  CE1   . PHE A 79  ? 0.2782 0.2404 0.4218 0.0295  0.1377  -0.0449 78  PHE A CE1   
1200  C  CE2   . PHE A 79  ? 0.2920 0.2681 0.4284 0.0310  0.1280  -0.0377 78  PHE A CE2   
1201  C  CZ    . PHE A 79  ? 0.2743 0.2443 0.4102 0.0271  0.1361  -0.0447 78  PHE A CZ    
1211  N  N     . LEU A 80  ? 0.2316 0.1947 0.3607 0.0439  0.0947  -0.0104 79  LEU A N     
1212  C  CA    . LEU A 80  ? 0.2370 0.2008 0.3672 0.0472  0.0860  -0.0019 79  LEU A CA    
1213  C  C     . LEU A 80  ? 0.2529 0.2242 0.3939 0.0514  0.0805  0.0042  79  LEU A C     
1214  O  O     . LEU A 80  ? 0.2594 0.2377 0.3945 0.0499  0.0771  0.0041  79  LEU A O     
1215  C  CB    . LEU A 80  ? 0.2381 0.2038 0.3502 0.0435  0.0801  -0.0012 79  LEU A CB    
1216  C  CG    . LEU A 80  ? 0.3030 0.2649 0.4112 0.0439  0.0758  0.0035  79  LEU A CG    
1217  C  CD1   . LEU A 80  ? 0.3165 0.2686 0.4282 0.0430  0.0825  0.0005  79  LEU A CD1   
1218  C  CD2   . LEU A 80  ? 0.2715 0.2372 0.3636 0.0404  0.0707  0.0031  79  LEU A CD2   
1230  N  N     . CYS A 81  ? 0.2347 0.2043 0.3923 0.0564  0.0796  0.0096  80  CYS A N     
1231  C  CA    . CYS A 81  ? 0.2318 0.2086 0.4027 0.0604  0.0746  0.0155  80  CYS A CA    
1232  C  C     . CYS A 81  ? 0.2412 0.2198 0.4075 0.0615  0.0638  0.0244  80  CYS A C     
1233  O  O     . CYS A 81  ? 0.2489 0.2225 0.4212 0.0639  0.0614  0.0298  80  CYS A O     
1234  C  CB    . CYS A 81  ? 0.3004 0.2750 0.4943 0.0651  0.0799  0.0161  80  CYS A CB    
1235  S  SG    . CYS A 81  ? 0.3163 0.2910 0.5135 0.0620  0.0918  0.0052  80  CYS A SG    
1241  N  N     . VAL A 82  ? 0.2239 0.2091 0.3790 0.0596  0.0574  0.0259  81  VAL A N     
1242  C  CA    . VAL A 82  ? 0.2397 0.2260 0.3845 0.0589  0.0482  0.0321  81  VAL A CA    
1243  C  C     . VAL A 82  ? 0.2730 0.2658 0.4268 0.0615  0.0403  0.0395  81  VAL A C     
1244  O  O     . VAL A 82  ? 0.2104 0.2097 0.3680 0.0615  0.0396  0.0383  81  VAL A O     
1245  C  CB    . VAL A 82  ? 0.2156 0.2040 0.3412 0.0547  0.0465  0.0280  81  VAL A CB    
1246  C  CG1   . VAL A 82  ? 0.2275 0.2157 0.3422 0.0537  0.0390  0.0332  81  VAL A CG1   
1247  C  CG2   . VAL A 82  ? 0.2378 0.2218 0.3553 0.0515  0.0538  0.0203  81  VAL A CG2   
1257  N  N     . PHE A 83  ? 0.2701 0.2610 0.4258 0.0628  0.0339  0.0473  82  PHE A N     
1258  C  CA    . PHE A 83  ? 0.2792 0.2761 0.4364 0.0634  0.0243  0.0546  82  PHE A CA    
1259  C  C     . PHE A 83  ? 0.2580 0.2531 0.3980 0.0604  0.0179  0.0582  82  PHE A C     
1260  O  O     . PHE A 83  ? 0.2548 0.2441 0.3852 0.0585  0.0209  0.0562  82  PHE A O     
1261  C  CB    . PHE A 83  ? 0.2393 0.2369 0.4176 0.0677  0.0213  0.0621  82  PHE A CB    
1262  C  CG    . PHE A 83  ? 0.2962 0.2860 0.4776 0.0689  0.0202  0.0677  82  PHE A CG    
1263  C  CD1   . PHE A 83  ? 0.2429 0.2249 0.4310 0.0704  0.0287  0.0637  82  PHE A CD1   
1264  C  CD2   . PHE A 83  ? 0.2728 0.2623 0.4493 0.0679  0.0104  0.0771  82  PHE A CD2   
1265  C  CE1   . PHE A 83  ? 0.3045 0.2783 0.4954 0.0712  0.0274  0.0693  82  PHE A CE1   
1266  C  CE2   . PHE A 83  ? 0.3082 0.2900 0.4865 0.0683  0.0089  0.0830  82  PHE A CE2   
1267  C  CZ    . PHE A 83  ? 0.3068 0.2805 0.4928 0.0702  0.0173  0.0794  82  PHE A CZ    
1277  N  N     . ALA A 84  ? 0.2662 0.2665 0.4024 0.0594  0.0093  0.0633  83  ALA A N     
1278  C  CA    . ALA A 84  ? 0.2826 0.2817 0.4030 0.0561  0.0030  0.0672  83  ALA A CA    
1279  C  C     . ALA A 84  ? 0.3350 0.3325 0.4627 0.0571  -0.0040 0.0776  83  ALA A C     
1280  O  O     . ALA A 84  ? 0.3043 0.3058 0.4471 0.0597  -0.0082 0.0828  83  ALA A O     
1281  C  CB    . ALA A 84  ? 0.2920 0.2969 0.4008 0.0534  -0.0017 0.0650  83  ALA A CB    
1287  N  N     . ILE A 85  ? 0.2755 0.2674 0.3933 0.0548  -0.0053 0.0811  84  ILE A N     
1288  C  CA    . ILE A 85  ? 0.3670 0.3560 0.4912 0.0552  -0.0119 0.0917  84  ILE A CA    
1289  C  C     . ILE A 85  ? 0.4035 0.3980 0.5233 0.0529  -0.0225 0.0986  84  ILE A C     
1290  O  O     . ILE A 85  ? 0.4310 0.4243 0.5576 0.0532  -0.0296 0.1085  84  ILE A O     
1291  C  CB    . ILE A 85  ? 0.3837 0.3649 0.4964 0.0522  -0.0107 0.0941  84  ILE A CB    
1292  C  CG1   . ILE A 85  ? 0.3897 0.3725 0.4795 0.0469  -0.0107 0.0896  84  ILE A CG1   
1293  C  CG2   . ILE A 85  ? 0.3906 0.3651 0.5116 0.0546  -0.0016 0.0895  84  ILE A CG2   
1294  C  CD1   . ILE A 85  ? 0.4521 0.4364 0.5294 0.0426  -0.0195 0.0967  84  ILE A CD1   
1306  N  N     . ASN A 86  ? 0.3483 0.3485 0.4573 0.0505  -0.0240 0.0937  85  ASN A N     
1307  C  CA    . ASN A 86  ? 0.4373 0.4427 0.5405 0.0477  -0.0336 0.0987  85  ASN A CA    
1308  C  C     . ASN A 86  ? 0.4300 0.4428 0.5461 0.0500  -0.0354 0.0973  85  ASN A C     
1309  O  O     . ASN A 86  ? 0.4017 0.4193 0.5114 0.0472  -0.0423 0.0989  85  ASN A O     
1310  C  CB    . ASN A 86  ? 0.4238 0.4294 0.5036 0.0424  -0.0342 0.0940  85  ASN A CB    
1311  C  CG    . ASN A 86  ? 0.4371 0.4452 0.5124 0.0429  -0.0281 0.0834  85  ASN A CG    
1312  O  OD1   . ASN A 86  ? 0.4118 0.4195 0.4973 0.0464  -0.0212 0.0784  85  ASN A OD1   
1313  N  ND2   . ASN A 86  ? 0.4485 0.4591 0.5088 0.0392  -0.0308 0.0799  85  ASN A ND2   
1320  N  N     . ASN A 87  ? 0.4083 0.4219 0.5414 0.0546  -0.0289 0.0938  86  ASN A N     
1321  C  CA    . ASN A 87  ? 0.3744 0.3953 0.5209 0.0566  -0.0294 0.0922  86  ASN A CA    
1322  C  C     . ASN A 87  ? 0.3836 0.4050 0.5554 0.0619  -0.0268 0.0957  86  ASN A C     
1323  O  O     . ASN A 87  ? 0.3457 0.3644 0.5256 0.0648  -0.0173 0.0899  86  ASN A O     
1324  C  CB    . ASN A 87  ? 0.4085 0.4309 0.5480 0.0560  -0.0222 0.0817  86  ASN A CB    
1325  C  CG    . ASN A 87  ? 0.4639 0.4939 0.6149 0.0568  -0.0235 0.0806  86  ASN A CG    
1326  O  OD1   . ASN A 87  ? 0.4089 0.4413 0.5786 0.0603  -0.0193 0.0805  86  ASN A OD1   
1327  N  ND2   . ASN A 87  ? 0.5147 0.5484 0.6547 0.0533  -0.0289 0.0795  86  ASN A ND2   
1334  N  N     . THR A 88  ? 0.3966 0.4216 0.5812 0.0630  -0.0354 0.1052  87  THR A N     
1335  C  CA    . THR A 88  ? 0.4156 0.4409 0.6213 0.0663  -0.0326 0.1064  87  THR A CA    
1336  C  C     . THR A 88  ? 0.3476 0.3777 0.5664 0.0687  -0.0241 0.0984  87  THR A C     
1337  O  O     . THR A 88  ? 0.3853 0.4127 0.6169 0.0715  -0.0162 0.0948  87  THR A O     
1338  C  CB    . THR A 88  ? 0.4130 0.4424 0.6244 0.0643  -0.0433 0.1149  87  THR A CB    
1339  O  OG1   . THR A 88  ? 0.4637 0.4874 0.6629 0.0616  -0.0500 0.1222  87  THR A OG1   
1340  C  CG2   . THR A 88  ? 0.4489 0.4800 0.6829 0.0674  -0.0404 0.1154  87  THR A CG2   
1348  N  N     . LYS A 89  ? 0.3679 0.4049 0.5836 0.0672  -0.0255 0.0956  88  LYS A N     
1349  C  CA    . LYS A 89  ? 0.4045 0.4464 0.6323 0.0686  -0.0178 0.0888  88  LYS A CA    
1350  C  C     . LYS A 89  ? 0.3826 0.4193 0.6074 0.0703  -0.0060 0.0804  88  LYS A C     
1351  O  O     . LYS A 89  ? 0.3158 0.3531 0.5525 0.0718  0.0026  0.0749  88  LYS A O     
1352  C  CB    . LYS A 89  ? 0.3959 0.4459 0.6202 0.0661  -0.0224 0.0881  88  LYS A CB    
1353  C  CG    . LYS A 89  ? 0.4693 0.5250 0.7050 0.0668  -0.0144 0.0814  88  LYS A CG    
1354  C  CD    . LYS A 89  ? 0.5322 0.5916 0.7560 0.0636  -0.0151 0.0773  88  LYS A CD    
1355  C  CE    . LYS A 89  ? 0.5639 0.6220 0.7858 0.0631  -0.0035 0.0677  88  LYS A CE    
1356  N  NZ    . LYS A 89  ? 0.5208 0.5701 0.7230 0.0617  0.0009  0.0624  88  LYS A NZ    
1370  N  N     . SER A 90  ? 0.3764 0.4073 0.5811 0.0681  -0.0051 0.0776  89  SER A N     
1371  C  CA    . SER A 90  ? 0.3235 0.3486 0.5213 0.0679  0.0056  0.0688  89  SER A CA    
1372  C  C     . SER A 90  ? 0.3376 0.3567 0.5494 0.0717  0.0116  0.0694  89  SER A C     
1373  O  O     . SER A 90  ? 0.3296 0.3460 0.5459 0.0726  0.0217  0.0621  89  SER A O     
1374  C  CB    . SER A 90  ? 0.3367 0.3569 0.5097 0.0640  0.0045  0.0659  89  SER A CB    
1375  O  OG    . SER A 90  ? 0.3359 0.3499 0.5047 0.0642  0.0018  0.0709  89  SER A OG    
1381  N  N     . PHE A 91  ? 0.2979 0.3141 0.5152 0.0732  0.0054  0.0777  90  PHE A N     
1382  C  CA    . PHE A 91  ? 0.2975 0.3074 0.5256 0.0750  0.0100  0.0776  90  PHE A CA    
1383  C  C     . PHE A 91  ? 0.3427 0.3573 0.5899 0.0766  0.0140  0.0751  90  PHE A C     
1384  O  O     . PHE A 91  ? 0.3016 0.3121 0.5569 0.0778  0.0232  0.0693  90  PHE A O     
1385  C  CB    . PHE A 91  ? 0.3524 0.3584 0.5788 0.0747  0.0011  0.0874  90  PHE A CB    
1386  C  CG    . PHE A 91  ? 0.3156 0.3146 0.5534 0.0766  0.0045  0.0885  90  PHE A CG    
1387  C  CD1   . PHE A 91  ? 0.3324 0.3223 0.5657 0.0770  0.0123  0.0841  90  PHE A CD1   
1388  C  CD2   . PHE A 91  ? 0.3577 0.3593 0.6112 0.0778  -0.0002 0.0941  90  PHE A CD2   
1389  C  CE1   . PHE A 91  ? 0.3377 0.3207 0.5815 0.0785  0.0155  0.0848  90  PHE A CE1   
1390  C  CE2   . PHE A 91  ? 0.3558 0.3507 0.6205 0.0797  0.0028  0.0952  90  PHE A CE2   
1391  C  CZ    . PHE A 91  ? 0.3987 0.3841 0.6584 0.0800  0.0106  0.0905  90  PHE A CZ    
1401  N  N     . GLU A 92  ? 0.3339 0.3571 0.5886 0.0762  0.0072  0.0792  91  GLU A N     
1402  C  CA    . GLU A 92  ? 0.3500 0.3787 0.6236 0.0775  0.0112  0.0769  91  GLU A CA    
1403  C  C     . GLU A 92  ? 0.3676 0.3978 0.6409 0.0770  0.0223  0.0667  91  GLU A C     
1404  O  O     . GLU A 92  ? 0.3925 0.4222 0.6783 0.0781  0.0307  0.0617  91  GLU A O     
1405  C  CB    . GLU A 92  ? 0.3714 0.4093 0.6509 0.0764  0.0013  0.0834  91  GLU A CB    
1406  C  CG    . GLU A 92  ? 0.4122 0.4489 0.6965 0.0767  -0.0089 0.0935  91  GLU A CG    
1407  C  CD    . GLU A 92  ? 0.4860 0.5309 0.7688 0.0741  -0.0204 0.1001  91  GLU A CD    
1408  O  OE1   . GLU A 92  ? 0.4630 0.5134 0.7390 0.0722  -0.0210 0.0972  91  GLU A OE1   
1409  O  OE2   . GLU A 92  ? 0.4793 0.5247 0.7676 0.0737  -0.0290 0.1083  91  GLU A OE2   
1416  N  N     . ASP A 93  ? 0.3843 0.4157 0.6425 0.0750  0.0228  0.0635  92  ASP A N     
1417  C  CA    . ASP A 93  ? 0.3792 0.4121 0.6352 0.0738  0.0328  0.0543  92  ASP A CA    
1418  C  C     . ASP A 93  ? 0.3599 0.3843 0.6145 0.0740  0.0437  0.0470  92  ASP A C     
1419  O  O     . ASP A 93  ? 0.3574 0.3827 0.6135 0.0726  0.0531  0.0392  92  ASP A O     
1420  C  CB    . ASP A 93  ? 0.3694 0.4042 0.6091 0.0717  0.0306  0.0528  92  ASP A CB    
1421  C  CG    . ASP A 93  ? 0.4112 0.4552 0.6528 0.0704  0.0226  0.0570  92  ASP A CG    
1422  O  OD1   . ASP A 93  ? 0.3946 0.4443 0.6510 0.0709  0.0204  0.0599  92  ASP A OD1   
1423  O  OD2   . ASP A 93  ? 0.4056 0.4499 0.6291 0.0670  0.0183  0.0561  92  ASP A OD2   
1428  N  N     . ILE A 94  ? 0.3437 0.3599 0.5947 0.0751  0.0426  0.0495  93  ILE A N     
1429  C  CA    . ILE A 94  ? 0.3292 0.3368 0.5779 0.0749  0.0523  0.0427  93  ILE A CA    
1430  C  C     . ILE A 94  ? 0.3593 0.3674 0.6234 0.0753  0.0605  0.0376  93  ILE A C     
1431  O  O     . ILE A 94  ? 0.3369 0.3416 0.5974 0.0733  0.0707  0.0288  93  ILE A O     
1432  C  CB    . ILE A 94  ? 0.3648 0.3639 0.6109 0.0762  0.0486  0.0479  93  ILE A CB    
1433  C  CG1   . ILE A 94  ? 0.3048 0.3021 0.5334 0.0751  0.0430  0.0511  93  ILE A CG1   
1434  C  CG2   . ILE A 94  ? 0.3571 0.3471 0.6046 0.0759  0.0585  0.0412  93  ILE A CG2   
1435  C  CD1   . ILE A 94  ? 0.3044 0.2995 0.5184 0.0727  0.0501  0.0428  93  ILE A CD1   
1447  N  N     . HIS A 95  ? 0.3867 0.3987 0.6679 0.0776  0.0563  0.0430  94  HIS A N     
1448  C  CA    . HIS A 95  ? 0.4134 0.4260 0.7112 0.0784  0.0642  0.0383  94  HIS A CA    
1449  C  C     . HIS A 95  ? 0.3504 0.3679 0.6459 0.0757  0.0727  0.0299  94  HIS A C     
1450  O  O     . HIS A 95  ? 0.3841 0.3976 0.6809 0.0742  0.0833  0.0216  94  HIS A O     
1451  C  CB    . HIS A 95  ? 0.3883 0.4066 0.7052 0.0812  0.0572  0.0461  94  HIS A CB    
1452  C  CG    . HIS A 95  ? 0.4340 0.4544 0.7701 0.0824  0.0649  0.0416  94  HIS A CG    
1453  N  ND1   . HIS A 95  ? 0.4625 0.4926 0.8093 0.0820  0.0657  0.0409  94  HIS A ND1   
1454  C  CD2   . HIS A 95  ? 0.4118 0.4258 0.7585 0.0837  0.0726  0.0375  94  HIS A CD2   
1455  C  CE1   . HIS A 95  ? 0.4056 0.4353 0.7688 0.0832  0.0737  0.0364  94  HIS A CE1   
1456  N  NE2   . HIS A 95  ? 0.4134 0.4334 0.7770 0.0843  0.0780  0.0342  94  HIS A NE2   
1464  N  N     . HIS A 96  ? 0.4104 0.4360 0.7013 0.0744  0.0681  0.0318  95  HIS A N     
1465  C  CA    . HIS A 96  ? 0.3682 0.3992 0.6574 0.0714  0.0755  0.0247  95  HIS A CA    
1466  C  C     . HIS A 96  ? 0.3618 0.3866 0.6339 0.0680  0.0840  0.0162  95  HIS A C     
1467  O  O     . HIS A 96  ? 0.3302 0.3550 0.6023 0.0651  0.0938  0.0083  95  HIS A O     
1468  C  CB    . HIS A 96  ? 0.4009 0.4414 0.6882 0.0706  0.0677  0.0294  95  HIS A CB    
1469  C  CG    . HIS A 96  ? 0.4792 0.5265 0.7828 0.0730  0.0593  0.0374  95  HIS A CG    
1470  N  ND1   . HIS A 96  ? 0.4570 0.5027 0.7618 0.0752  0.0488  0.0461  95  HIS A ND1   
1471  C  CD2   . HIS A 96  ? 0.5086 0.5643 0.8282 0.0731  0.0600  0.0379  95  HIS A CD2   
1472  C  CE1   . HIS A 96  ? 0.5009 0.5537 0.8211 0.0764  0.0430  0.0518  95  HIS A CE1   
1473  N  NE2   . HIS A 96  ? 0.5614 0.6204 0.8914 0.0754  0.0496  0.0470  95  HIS A NE2   
1481  N  N     . TYR A 97  ? 0.3511 0.3704 0.6080 0.0677  0.0803  0.0177  96  TYR A N     
1482  C  CA    . TYR A 97  ? 0.3273 0.3408 0.5680 0.0642  0.0878  0.0099  96  TYR A CA    
1483  C  C     . TYR A 97  ? 0.3474 0.3526 0.5912 0.0633  0.0969  0.0036  96  TYR A C     
1484  O  O     . TYR A 97  ? 0.3571 0.3603 0.5941 0.0592  0.1061  -0.0050 96  TYR A O     
1485  C  CB    . TYR A 97  ? 0.3023 0.3118 0.5279 0.0645  0.0818  0.0131  96  TYR A CB    
1486  C  CG    . TYR A 97  ? 0.2998 0.3159 0.5156 0.0630  0.0765  0.0151  96  TYR A CG    
1487  C  CD1   . TYR A 97  ? 0.3381 0.3546 0.5383 0.0574  0.0807  0.0085  96  TYR A CD1   
1488  C  CD2   . TYR A 97  ? 0.3054 0.3261 0.5217 0.0647  0.0651  0.0234  96  TYR A CD2   
1489  C  CE1   . TYR A 97  ? 0.3276 0.3486 0.5142 0.0541  0.0736  0.0104  96  TYR A CE1   
1490  C  CE2   . TYR A 97  ? 0.3422 0.3674 0.5447 0.0612  0.0587  0.0245  96  TYR A CE2   
1491  C  CZ    . TYR A 97  ? 0.3193 0.3445 0.5081 0.0563  0.0630  0.0181  96  TYR A CZ    
1492  O  OH    . TYR A 97  ? 0.4153 0.4442 0.5917 0.0532  0.0565  0.0194  96  TYR A OH    
1502  N  N     . ARG A 98  ? 0.2877 0.2878 0.5408 0.0666  0.0943  0.0077  97  ARG A N     
1503  C  CA    . ARG A 98  ? 0.3281 0.3198 0.5850 0.0659  0.1027  0.0018  97  ARG A CA    
1504  C  C     . ARG A 98  ? 0.3267 0.3216 0.5947 0.0644  0.1113  -0.0044 97  ARG A C     
1505  O  O     . ARG A 98  ? 0.3779 0.3680 0.6398 0.0606  0.1210  -0.0133 97  ARG A O     
1506  C  CB    . ARG A 98  ? 0.4185 0.4051 0.6868 0.0700  0.0979  0.0084  97  ARG A CB    
1507  C  CG    . ARG A 98  ? 0.4287 0.4055 0.7000 0.0692  0.1062  0.0026  97  ARG A CG    
1508  C  CD    . ARG A 98  ? 0.4193 0.3906 0.7010 0.0730  0.1009  0.0097  97  ARG A CD    
1509  N  NE    . ARG A 98  ? 0.4699 0.4349 0.7638 0.0734  0.1089  0.0049  97  ARG A NE    
1510  C  CZ    . ARG A 98  ? 0.5080 0.4638 0.7938 0.0704  0.1167  -0.0025 97  ARG A CZ    
1511  N  NH1   . ARG A 98  ? 0.4996 0.4515 0.7654 0.0668  0.1176  -0.0056 97  ARG A NH1   
1512  N  NH2   . ARG A 98  ? 0.5587 0.5092 0.8570 0.0708  0.1239  -0.0070 97  ARG A NH2   
1526  N  N     . GLU A 99  ? 0.3720 0.3750 0.6565 0.0672  0.1078  0.0002  98  GLU A N     
1527  C  CA    . GLU A 99  ? 0.3895 0.3965 0.6865 0.0662  0.1158  -0.0053 98  GLU A CA    
1528  C  C     . GLU A 99  ? 0.3823 0.3915 0.6654 0.0605  0.1234  -0.0135 98  GLU A C     
1529  O  O     . GLU A 99  ? 0.3280 0.3347 0.6119 0.0573  0.1336  -0.0218 98  GLU A O     
1530  C  CB    . GLU A 99  ? 0.3481 0.3650 0.6629 0.0696  0.1092  0.0019  98  GLU A CB    
1531  C  CG    . GLU A 99  ? 0.4195 0.4345 0.7521 0.0745  0.1038  0.0088  98  GLU A CG    
1532  C  CD    . GLU A 99  ? 0.4630 0.4701 0.8053 0.0751  0.1129  0.0030  98  GLU A CD    
1533  O  OE1   . GLU A 99  ? 0.4849 0.4936 0.8350 0.0735  0.1224  -0.0043 98  GLU A OE1   
1534  O  OE2   . GLU A 99  ? 0.4707 0.4695 0.8119 0.0768  0.1108  0.0054  98  GLU A OE2   
1541  N  N     . GLN A 100 ? 0.3189 0.3328 0.5892 0.0588  0.1183  -0.0111 99  GLN A N     
1542  C  CA    . GLN A 100 ? 0.3790 0.3952 0.6353 0.0530  0.1247  -0.0180 99  GLN A CA    
1543  C  C     . GLN A 100 ? 0.3747 0.3812 0.6147 0.0485  0.1322  -0.0260 99  GLN A C     
1544  O  O     . GLN A 100 ? 0.3765 0.3819 0.6114 0.0434  0.1414  -0.0341 99  GLN A O     
1545  C  CB    . GLN A 100 ? 0.3330 0.3555 0.5797 0.0526  0.1170  -0.0131 99  GLN A CB    
1546  C  CG    . GLN A 100 ? 0.3750 0.4016 0.6096 0.0466  0.1222  -0.0184 99  GLN A CG    
1547  C  CD    . GLN A 100 ? 0.4291 0.4635 0.6603 0.0470  0.1141  -0.0124 99  GLN A CD    
1548  O  OE1   . GLN A 100 ? 0.3931 0.4271 0.6236 0.0509  0.1048  -0.0057 99  GLN A OE1   
1549  N  NE2   . GLN A 100 ? 0.4343 0.4756 0.6629 0.0426  0.1175  -0.0147 99  GLN A NE2   
1558  N  N     . ILE A 101 ? 0.3352 0.3345 0.5667 0.0498  0.1283  -0.0239 100 ILE A N     
1559  C  CA    . ILE A 101 ? 0.3214 0.3117 0.5379 0.0451  0.1349  -0.0314 100 ILE A CA    
1560  C  C     . ILE A 101 ? 0.3991 0.3840 0.6241 0.0437  0.1443  -0.0381 100 ILE A C     
1561  O  O     . ILE A 101 ? 0.3568 0.3376 0.5704 0.0375  0.1526  -0.0467 100 ILE A O     
1562  C  CB    . ILE A 101 ? 0.3207 0.3043 0.5294 0.0472  0.1292  -0.0275 100 ILE A CB    
1563  C  CG1   . ILE A 101 ? 0.3240 0.3122 0.5213 0.0474  0.1216  -0.0229 100 ILE A CG1   
1564  C  CG2   . ILE A 101 ? 0.3591 0.3333 0.5552 0.0423  0.1363  -0.0354 100 ILE A CG2   
1565  C  CD1   . ILE A 101 ? 0.2878 0.2730 0.4860 0.0521  0.1129  -0.0152 100 ILE A CD1   
1577  N  N     . LYS A 102 ? 0.4039 0.3882 0.6488 0.0489  0.1431  -0.0344 101 LYS A N     
1578  C  CA    . LYS A 102 ? 0.3878 0.3671 0.6432 0.0481  0.1522  -0.0407 101 LYS A CA    
1579  C  C     . LYS A 102 ? 0.3957 0.3807 0.6536 0.0443  0.1601  -0.0471 101 LYS A C     
1580  O  O     . LYS A 102 ? 0.4088 0.3890 0.6616 0.0393  0.1700  -0.0561 101 LYS A O     
1581  C  CB    . LYS A 102 ? 0.3913 0.3703 0.6696 0.0549  0.1485  -0.0345 101 LYS A CB    
1582  C  CG    . LYS A 102 ? 0.4353 0.4062 0.7133 0.0578  0.1436  -0.0298 101 LYS A CG    
1583  C  CD    . LYS A 102 ? 0.4525 0.4225 0.7543 0.0637  0.1413  -0.0245 101 LYS A CD    
1584  C  CE    . LYS A 102 ? 0.4560 0.4366 0.7727 0.0680  0.1337  -0.0164 101 LYS A CE    
1585  N  NZ    . LYS A 102 ? 0.5060 0.4858 0.8449 0.0736  0.1295  -0.0097 101 LYS A NZ    
1599  N  N     . ARG A 103 ? 0.3650 0.3601 0.6314 0.0464  0.1560  -0.0424 102 ARG A N     
1600  C  CA    . ARG A 103 ? 0.4110 0.4126 0.6807 0.0428  0.1631  -0.0477 102 ARG A CA    
1601  C  C     . ARG A 103 ? 0.4096 0.4091 0.6558 0.0345  0.1690  -0.0552 102 ARG A C     
1602  O  O     . ARG A 103 ? 0.4219 0.4185 0.6648 0.0294  0.1790  -0.0638 102 ARG A O     
1603  C  CB    . ARG A 103 ? 0.4255 0.4386 0.7065 0.0464  0.1558  -0.0401 102 ARG A CB    
1604  C  CG    . ARG A 103 ? 0.4743 0.4958 0.7623 0.0437  0.1615  -0.0435 102 ARG A CG    
1605  C  CD    . ARG A 103 ? 0.5214 0.5529 0.8300 0.0492  0.1541  -0.0352 102 ARG A CD    
1606  N  NE    . ARG A 103 ? 0.5308 0.5655 0.8344 0.0520  0.1420  -0.0261 102 ARG A NE    
1607  C  CZ    . ARG A 103 ? 0.5531 0.5917 0.8416 0.0487  0.1388  -0.0250 102 ARG A CZ    
1608  N  NH1   . ARG A 103 ? 0.5436 0.5838 0.8195 0.0422  0.1463  -0.0317 102 ARG A NH1   
1609  N  NH2   . ARG A 103 ? 0.5386 0.5797 0.8243 0.0517  0.1278  -0.0168 102 ARG A NH2   
1623  N  N     . VAL A 104 ? 0.4360 0.4361 0.6651 0.0328  0.1629  -0.0522 103 VAL A N     
1624  C  CA    . VAL A 104 ? 0.4277 0.4266 0.6342 0.0246  0.1672  -0.0583 103 VAL A CA    
1625  C  C     . VAL A 104 ? 0.4329 0.4210 0.6275 0.0198  0.1741  -0.0661 103 VAL A C     
1626  O  O     . VAL A 104 ? 0.4708 0.4570 0.6526 0.0121  0.1816  -0.0737 103 VAL A O     
1627  C  CB    . VAL A 104 ? 0.4239 0.4259 0.6164 0.0243  0.1589  -0.0529 103 VAL A CB    
1628  C  CG1   . VAL A 104 ? 0.4551 0.4545 0.6236 0.0153  0.1630  -0.0589 103 VAL A CG1   
1629  C  CG2   . VAL A 104 ? 0.4622 0.4753 0.6653 0.0276  0.1529  -0.0461 103 VAL A CG2   
1639  N  N     . LYS A 105 ? 0.4098 0.3905 0.6080 0.0236  0.1716  -0.0643 104 LYS A N     
1640  C  CA    . LYS A 105 ? 0.4194 0.3897 0.6084 0.0192  0.1778  -0.0714 104 LYS A CA    
1641  C  C     . LYS A 105 ? 0.4764 0.4433 0.6799 0.0191  0.1870  -0.0774 104 LYS A C     
1642  O  O     . LYS A 105 ? 0.4755 0.4341 0.6716 0.0144  0.1937  -0.0846 104 LYS A O     
1643  C  CB    . LYS A 105 ? 0.4801 0.4442 0.6681 0.0232  0.1715  -0.0668 104 LYS A CB    
1644  C  CG    . LYS A 105 ? 0.4714 0.4366 0.6414 0.0216  0.1645  -0.0634 104 LYS A CG    
1645  C  CD    . LYS A 105 ? 0.5191 0.4754 0.6714 0.0155  0.1678  -0.0693 104 LYS A CD    
1646  C  CE    . LYS A 105 ? 0.3912 0.3493 0.5251 0.0127  0.1620  -0.0672 104 LYS A CE    
1647  N  NZ    . LYS A 105 ? 0.3850 0.3381 0.4983 0.0034  0.1666  -0.0748 104 LYS A NZ    
1661  N  N     . ASP A 106 ? 0.4649 0.4384 0.6890 0.0239  0.1875  -0.0747 105 ASP A N     
1662  C  CA    . ASP A 106 ? 0.4452 0.4160 0.6882 0.0258  0.1951  -0.0789 105 ASP A CA    
1663  C  C     . ASP A 106 ? 0.4528 0.4128 0.6990 0.0273  0.1967  -0.0805 105 ASP A C     
1664  O  O     . ASP A 106 ? 0.4575 0.4108 0.7035 0.0234  0.2060  -0.0888 105 ASP A O     
1665  C  CB    . ASP A 106 ? 0.4742 0.4455 0.7118 0.0185  0.2062  -0.0888 105 ASP A CB    
1666  C  CG    . ASP A 106 ? 0.5357 0.5083 0.7970 0.0216  0.2133  -0.0918 105 ASP A CG    
1667  O  OD1   . ASP A 106 ? 0.5078 0.4875 0.7887 0.0286  0.2082  -0.0848 105 ASP A OD1   
1668  O  OD2   . ASP A 106 ? 0.5475 0.5141 0.8080 0.0171  0.2236  -0.1009 105 ASP A OD2   
1673  N  N     . SER A 107 ? 0.4498 0.4082 0.6995 0.0330  0.1876  -0.0722 106 SER A N     
1674  C  CA    . SER A 107 ? 0.4216 0.3701 0.6750 0.0349  0.1880  -0.0723 106 SER A CA    
1675  C  C     . SER A 107 ? 0.4919 0.4418 0.7592 0.0431  0.1778  -0.0613 106 SER A C     
1676  O  O     . SER A 107 ? 0.4217 0.3778 0.6855 0.0457  0.1687  -0.0537 106 SER A O     
1677  C  CB    . SER A 107 ? 0.4497 0.3905 0.6796 0.0289  0.1885  -0.0762 106 SER A CB    
1678  O  OG    . SER A 107 ? 0.4448 0.3757 0.6789 0.0298  0.1907  -0.0777 106 SER A OG    
1684  N  N     . GLU A 108 ? 0.4078 0.3513 0.6899 0.0466  0.1794  -0.0606 107 GLU A N     
1685  C  CA    . GLU A 108 ? 0.4625 0.4053 0.7566 0.0535  0.1701  -0.0504 107 GLU A CA    
1686  C  C     . GLU A 108 ? 0.4916 0.4262 0.7710 0.0523  0.1664  -0.0486 107 GLU A C     
1687  O  O     . GLU A 108 ? 0.5205 0.4541 0.8055 0.0571  0.1579  -0.0398 107 GLU A O     
1688  C  CB    . GLU A 108 ? 0.5161 0.4565 0.8354 0.0580  0.1736  -0.0501 107 GLU A CB    
1689  C  CG    . GLU A 108 ? 0.5643 0.5106 0.9023 0.0653  0.1637  -0.0387 107 GLU A CG    
1690  C  CD    . GLU A 108 ? 0.5502 0.5083 0.8970 0.0666  0.1623  -0.0369 107 GLU A CD    
1691  O  OE1   . GLU A 108 ? 0.6196 0.5803 0.9624 0.0624  0.1708  -0.0452 107 GLU A OE1   
1692  O  OE2   . GLU A 108 ? 0.5580 0.5228 0.9144 0.0712  0.1525  -0.0272 107 GLU A OE2   
1699  N  N     . ASP A 109 ? 0.4251 0.3542 0.6851 0.0455  0.1721  -0.0566 108 ASP A N     
1700  C  CA    . ASP A 109 ? 0.4780 0.3983 0.7247 0.0434  0.1706  -0.0568 108 ASP A CA    
1701  C  C     . ASP A 109 ? 0.4736 0.3962 0.6963 0.0382  0.1683  -0.0586 108 ASP A C     
1702  O  O     . ASP A 109 ? 0.4782 0.3968 0.6854 0.0312  0.1746  -0.0670 108 ASP A O     
1703  C  CB    . ASP A 109 ? 0.5284 0.4388 0.7763 0.0398  0.1801  -0.0653 108 ASP A CB    
1704  C  CG    . ASP A 109 ? 0.6468 0.5477 0.8849 0.0384  0.1783  -0.0647 108 ASP A CG    
1705  O  OD1   . ASP A 109 ? 0.6760 0.5752 0.9228 0.0439  0.1712  -0.0561 108 ASP A OD1   
1706  O  OD2   . ASP A 109 ? 0.7223 0.6177 0.9439 0.0314  0.1837  -0.0725 108 ASP A OD2   
1711  N  N     . VAL A 110 ? 0.4593 0.3882 0.6791 0.0416  0.1591  -0.0506 109 VAL A N     
1712  C  CA    . VAL A 110 ? 0.3862 0.3185 0.5857 0.0377  0.1559  -0.0511 109 VAL A CA    
1713  C  C     . VAL A 110 ? 0.3651 0.2939 0.5580 0.0399  0.1484  -0.0449 109 VAL A C     
1714  O  O     . VAL A 110 ? 0.4014 0.3317 0.6058 0.0460  0.1415  -0.0362 109 VAL A O     
1715  C  CB    . VAL A 110 ? 0.3447 0.2883 0.5459 0.0393  0.1520  -0.0477 109 VAL A CB    
1716  C  CG1   . VAL A 110 ? 0.3575 0.3043 0.5379 0.0351  0.1490  -0.0486 109 VAL A CG1   
1717  C  CG2   . VAL A 110 ? 0.4101 0.3572 0.6197 0.0374  0.1595  -0.0534 109 VAL A CG2   
1727  N  N     . PRO A 111 ? 0.3399 0.2644 0.5142 0.0348  0.1492  -0.0487 110 PRO A N     
1728  C  CA    . PRO A 111 ? 0.3558 0.2771 0.5241 0.0368  0.1426  -0.0430 110 PRO A CA    
1729  C  C     . PRO A 111 ? 0.3898 0.3197 0.5594 0.0415  0.1335  -0.0344 110 PRO A C     
1730  O  O     . PRO A 111 ? 0.3163 0.2535 0.4780 0.0397  0.1323  -0.0355 110 PRO A O     
1731  C  CB    . PRO A 111 ? 0.3634 0.2806 0.5109 0.0294  0.1459  -0.0501 110 PRO A CB    
1732  C  CG    . PRO A 111 ? 0.3816 0.2954 0.5276 0.0238  0.1551  -0.0594 110 PRO A CG    
1733  C  CD    . PRO A 111 ? 0.3848 0.3059 0.5433 0.0265  0.1566  -0.0587 110 PRO A CD    
1741  N  N     . MET A 112 ? 0.3375 0.2663 0.5173 0.0471  0.1269  -0.0257 111 MET A N     
1742  C  CA    . MET A 112 ? 0.3475 0.2839 0.5284 0.0513  0.1179  -0.0172 111 MET A CA    
1743  C  C     . MET A 112 ? 0.3578 0.2891 0.5406 0.0547  0.1114  -0.0090 111 MET A C     
1744  O  O     . MET A 112 ? 0.3595 0.2829 0.5499 0.0556  0.1130  -0.0079 111 MET A O     
1745  C  CB    . MET A 112 ? 0.3008 0.2456 0.4972 0.0555  0.1144  -0.0123 111 MET A CB    
1746  C  CG    . MET A 112 ? 0.3881 0.3379 0.5882 0.0532  0.1207  -0.0187 111 MET A CG    
1747  S  SD    . MET A 112 ? 0.4372 0.3966 0.6577 0.0588  0.1149  -0.0109 111 MET A SD    
1748  C  CE    . MET A 112 ? 0.4373 0.3998 0.6645 0.0557  0.1252  -0.0199 111 MET A CE    
1758  N  N     . VAL A 113 ? 0.3067 0.2427 0.4830 0.0564  0.1041  -0.0031 112 VAL A N     
1759  C  CA    . VAL A 113 ? 0.2938 0.2272 0.4687 0.0582  0.0959  0.0060  112 VAL A CA    
1760  C  C     . VAL A 113 ? 0.3052 0.2481 0.4835 0.0614  0.0864  0.0145  112 VAL A C     
1761  O  O     . VAL A 113 ? 0.2631 0.2146 0.4344 0.0598  0.0843  0.0128  112 VAL A O     
1762  C  CB    . VAL A 113 ? 0.3224 0.2536 0.4763 0.0525  0.0938  0.0043  112 VAL A CB    
1763  C  CG1   . VAL A 113 ? 0.2961 0.2268 0.4458 0.0533  0.0848  0.0139  112 VAL A CG1   
1764  C  CG2   . VAL A 113 ? 0.3389 0.2599 0.4904 0.0490  0.1027  -0.0035 112 VAL A CG2   
1774  N  N     . LEU A 114 ? 0.2867 0.2278 0.4769 0.0656  0.0806  0.0236  113 LEU A N     
1775  C  CA    . LEU A 114 ? 0.2561 0.2054 0.4486 0.0679  0.0706  0.0324  113 LEU A CA    
1776  C  C     . LEU A 114 ? 0.2698 0.2197 0.4431 0.0643  0.0629  0.0370  113 LEU A C     
1777  O  O     . LEU A 114 ? 0.2836 0.2260 0.4525 0.0630  0.0624  0.0395  113 LEU A O     
1778  C  CB    . LEU A 114 ? 0.3012 0.2495 0.5125 0.0722  0.0664  0.0403  113 LEU A CB    
1779  C  CG    . LEU A 114 ? 0.3000 0.2570 0.5146 0.0742  0.0557  0.0495  113 LEU A CG    
1780  C  CD1   . LEU A 114 ? 0.2704 0.2377 0.4885 0.0743  0.0564  0.0458  113 LEU A CD1   
1781  C  CD2   . LEU A 114 ? 0.3401 0.2953 0.5693 0.0764  0.0500  0.0577  113 LEU A CD2   
1793  N  N     . VAL A 115 ? 0.2266 0.1852 0.3889 0.0625  0.0575  0.0375  114 VAL A N     
1794  C  CA    . VAL A 115 ? 0.2562 0.2162 0.4002 0.0589  0.0514  0.0402  114 VAL A CA    
1795  C  C     . VAL A 115 ? 0.2460 0.2124 0.3903 0.0602  0.0416  0.0484  114 VAL A C     
1796  O  O     . VAL A 115 ? 0.2371 0.2111 0.3838 0.0611  0.0393  0.0477  114 VAL A O     
1797  C  CB    . VAL A 115 ? 0.2864 0.2499 0.4145 0.0547  0.0541  0.0322  114 VAL A CB    
1798  C  CG1   . VAL A 115 ? 0.2239 0.1897 0.3354 0.0516  0.0480  0.0348  114 VAL A CG1   
1799  C  CG2   . VAL A 115 ? 0.2905 0.2474 0.4167 0.0524  0.0631  0.0243  114 VAL A CG2   
1809  N  N     . GLY A 116 ? 0.2760 0.2394 0.4167 0.0596  0.0356  0.0562  115 GLY A N     
1810  C  CA    . GLY A 116 ? 0.2834 0.2523 0.4193 0.0591  0.0260  0.0635  115 GLY A CA    
1811  C  C     . GLY A 116 ? 0.2785 0.2497 0.3933 0.0544  0.0236  0.0614  115 GLY A C     
1812  O  O     . GLY A 116 ? 0.2610 0.2274 0.3665 0.0516  0.0238  0.0629  115 GLY A O     
1816  N  N     . ASN A 117 ? 0.2217 0.2002 0.3297 0.0534  0.0218  0.0576  116 ASN A N     
1817  C  CA    . ASN A 117 ? 0.2791 0.2601 0.3691 0.0495  0.0210  0.0536  116 ASN A CA    
1818  C  C     . ASN A 117 ? 0.2693 0.2541 0.3507 0.0477  0.0126  0.0593  116 ASN A C     
1819  O  O     . ASN A 117 ? 0.2869 0.2731 0.3755 0.0491  0.0066  0.0665  116 ASN A O     
1820  C  CB    . ASN A 117 ? 0.2426 0.2281 0.3300 0.0493  0.0244  0.0454  116 ASN A CB    
1821  C  CG    . ASN A 117 ? 0.2205 0.2079 0.2918 0.0458  0.0244  0.0407  116 ASN A CG    
1822  O  OD1   . ASN A 117 ? 0.2492 0.2330 0.3139 0.0436  0.0270  0.0395  116 ASN A OD1   
1823  N  ND2   . ASN A 117 ? 0.2264 0.2194 0.2926 0.0452  0.0213  0.0382  116 ASN A ND2   
1830  N  N     . LYS A 118 ? 0.2678 0.2542 0.3334 0.0442  0.0122  0.0559  117 LYS A N     
1831  C  CA    . LYS A 118 ? 0.3028 0.2919 0.3566 0.0412  0.0058  0.0594  117 LYS A CA    
1832  C  C     . LYS A 118 ? 0.3224 0.3073 0.3734 0.0392  0.0023  0.0678  117 LYS A C     
1833  O  O     . LYS A 118 ? 0.2905 0.2771 0.3367 0.0374  -0.0047 0.0737  117 LYS A O     
1834  C  CB    . LYS A 118 ? 0.2632 0.2580 0.3204 0.0423  -0.0002 0.0612  117 LYS A CB    
1835  C  CG    . LYS A 118 ? 0.2866 0.2852 0.3485 0.0443  0.0028  0.0544  117 LYS A CG    
1836  C  CD    . LYS A 118 ? 0.2987 0.3027 0.3576 0.0435  -0.0033 0.0547  117 LYS A CD    
1837  C  CE    . LYS A 118 ? 0.2989 0.3060 0.3620 0.0449  -0.0006 0.0487  117 LYS A CE    
1838  N  NZ    . LYS A 118 ? 0.3200 0.3318 0.3810 0.0440  -0.0064 0.0490  117 LYS A NZ    
1852  N  N     . CYS A 119 ? 0.3039 0.2825 0.3568 0.0388  0.0068  0.0686  118 CYS A N     
1853  C  CA    . CYS A 119 ? 0.3237 0.2972 0.3746 0.0367  0.0032  0.0775  118 CYS A CA    
1854  C  C     . CYS A 119 ? 0.3543 0.3289 0.3865 0.0309  0.0014  0.0781  118 CYS A C     
1855  O  O     . CYS A 119 ? 0.3996 0.3702 0.4267 0.0278  -0.0020 0.0859  118 CYS A O     
1856  C  CB    . CYS A 119 ? 0.3134 0.2792 0.3726 0.0379  0.0086  0.0781  118 CYS A CB    
1857  S  SG    . CYS A 119 ? 0.4464 0.4102 0.4949 0.0344  0.0170  0.0695  118 CYS A SG    
1863  N  N     . ASP A 120 ? 0.3304 0.3102 0.3525 0.0293  0.0035  0.0704  119 ASP A N     
1864  C  CA    . ASP A 120 ? 0.3770 0.3589 0.3821 0.0239  0.0019  0.0702  119 ASP A CA    
1865  C  C     . ASP A 120 ? 0.4155 0.4005 0.4149 0.0221  -0.0063 0.0754  119 ASP A C     
1866  O  O     . ASP A 120 ? 0.4452 0.4312 0.4295 0.0169  -0.0081 0.0762  119 ASP A O     
1867  C  CB    . ASP A 120 ? 0.3636 0.3502 0.3618 0.0233  0.0070  0.0597  119 ASP A CB    
1868  C  CG    . ASP A 120 ? 0.3774 0.3686 0.3815 0.0269  0.0058  0.0548  119 ASP A CG    
1869  O  OD1   . ASP A 120 ? 0.2988 0.2891 0.3148 0.0308  0.0084  0.0528  119 ASP A OD1   
1870  O  OD2   . ASP A 120 ? 0.3549 0.3503 0.3515 0.0255  0.0026  0.0526  119 ASP A OD2   
1875  N  N     . LEU A 121 ? 0.4292 0.4159 0.4399 0.0258  -0.0110 0.0785  120 LEU A N     
1876  C  CA    . LEU A 121 ? 0.3913 0.3819 0.3970 0.0241  -0.0188 0.0819  120 LEU A CA    
1877  C  C     . LEU A 121 ? 0.4769 0.4646 0.4831 0.0219  -0.0264 0.0938  120 LEU A C     
1878  O  O     . LEU A 121 ? 0.5112 0.4945 0.5302 0.0247  -0.0265 0.0997  120 LEU A O     
1879  C  CB    . LEU A 121 ? 0.4168 0.4118 0.4350 0.0287  -0.0203 0.0791  120 LEU A CB    
1880  C  CG    . LEU A 121 ? 0.4143 0.4129 0.4292 0.0296  -0.0154 0.0685  120 LEU A CG    
1881  C  CD1   . LEU A 121 ? 0.4549 0.4575 0.4813 0.0331  -0.0181 0.0676  120 LEU A CD1   
1882  C  CD2   . LEU A 121 ? 0.4289 0.4295 0.4259 0.0249  -0.0160 0.0641  120 LEU A CD2   
1894  N  N     . PRO A 122 ? 0.5559 0.5454 0.5478 0.0164  -0.0327 0.0973  121 PRO A N     
1895  C  CA    . PRO A 122 ? 0.5965 0.5828 0.5858 0.0129  -0.0407 0.1094  121 PRO A CA    
1896  C  C     . PRO A 122 ? 0.6589 0.6472 0.6639 0.0163  -0.0491 0.1174  121 PRO A C     
1897  O  O     . PRO A 122 ? 0.6917 0.6765 0.7021 0.0156  -0.0553 0.1285  121 PRO A O     
1898  C  CB    . PRO A 122 ? 0.6409 0.6290 0.6073 0.0051  -0.0438 0.1087  121 PRO A CB    
1899  C  CG    . PRO A 122 ? 0.6449 0.6387 0.6094 0.0065  -0.0418 0.0986  121 PRO A CG    
1900  C  CD    . PRO A 122 ? 0.5705 0.5648 0.5490 0.0133  -0.0336 0.0907  121 PRO A CD    
1908  N  N     . SER A 123 ? 0.7253 0.7192 0.7382 0.0197  -0.0498 0.1126  122 SER A N     
1909  C  CA    . SER A 123 ? 0.7914 0.7892 0.8179 0.0218  -0.0585 0.1195  122 SER A CA    
1910  C  C     . SER A 123 ? 0.7827 0.7802 0.8343 0.0295  -0.0552 0.1203  122 SER A C     
1911  O  O     . SER A 123 ? 0.7495 0.7519 0.8133 0.0335  -0.0538 0.1159  122 SER A O     
1912  C  CB    . SER A 123 ? 0.8601 0.8642 0.8802 0.0201  -0.0613 0.1139  122 SER A CB    
1913  O  OG    . SER A 123 ? 0.9074 0.9117 0.9060 0.0124  -0.0663 0.1152  122 SER A OG    
1919  N  N     . ARG A 124 ? 0.6197 0.6111 0.6789 0.0312  -0.0537 0.1259  123 ARG A N     
1920  C  CA    . ARG A 124 ? 0.5338 0.5234 0.6162 0.0382  -0.0491 0.1259  123 ARG A CA    
1921  C  C     . ARG A 124 ? 0.5366 0.5300 0.6390 0.0415  -0.0573 0.1346  123 ARG A C     
1922  O  O     . ARG A 124 ? 0.5389 0.5324 0.6391 0.0385  -0.0674 0.1452  123 ARG A O     
1923  C  CB    . ARG A 124 ? 0.5041 0.4848 0.5879 0.0385  -0.0449 0.1289  123 ARG A CB    
1924  C  CG    . ARG A 124 ? 0.5582 0.5358 0.6669 0.0453  -0.0416 0.1307  123 ARG A CG    
1925  C  CD    . ARG A 124 ? 0.5571 0.5250 0.6662 0.0448  -0.0386 0.1345  123 ARG A CD    
1926  N  NE    . ARG A 124 ? 0.5830 0.5475 0.6791 0.0428  -0.0289 0.1248  123 ARG A NE    
1927  C  CZ    . ARG A 124 ? 0.5309 0.4917 0.6364 0.0464  -0.0194 0.1176  123 ARG A CZ    
1928  N  NH1   . ARG A 124 ? 0.5007 0.4610 0.6283 0.0525  -0.0170 0.1173  123 ARG A NH1   
1929  N  NH2   . ARG A 124 ? 0.5395 0.4972 0.6322 0.0435  -0.0121 0.1105  123 ARG A NH2   
1943  N  N     . THR A 125 ? 0.5018 0.4985 0.6243 0.0476  -0.0527 0.1304  124 THR A N     
1944  C  CA    . THR A 125 ? 0.4563 0.4572 0.6019 0.0517  -0.0587 0.1378  124 THR A CA    
1945  C  C     . THR A 125 ? 0.4676 0.4650 0.6339 0.0572  -0.0510 0.1347  124 THR A C     
1946  O  O     . THR A 125 ? 0.4692 0.4697 0.6519 0.0589  -0.0539 0.1372  124 THR A O     
1947  C  CB    . THR A 125 ? 0.4845 0.4951 0.6345 0.0521  -0.0607 0.1335  124 THR A CB    
1948  O  OG1   . THR A 125 ? 0.4302 0.4419 0.5832 0.0551  -0.0500 0.1221  124 THR A OG1   
1949  C  CG2   . THR A 125 ? 0.4902 0.5039 0.6176 0.0453  -0.0682 0.1343  124 THR A CG2   
1957  N  N     . VAL A 126 ? 0.4737 0.4646 0.6400 0.0597  -0.0414 0.1295  125 VAL A N     
1958  C  CA    . VAL A 126 ? 0.4277 0.4142 0.6117 0.0641  -0.0335 0.1258  125 VAL A CA    
1959  C  C     . VAL A 126 ? 0.5117 0.4874 0.6902 0.0630  -0.0319 0.1297  125 VAL A C     
1960  O  O     . VAL A 126 ? 0.5091 0.4803 0.6714 0.0604  -0.0274 0.1261  125 VAL A O     
1961  C  CB    . VAL A 126 ? 0.4306 0.4184 0.6204 0.0675  -0.0223 0.1147  125 VAL A CB    
1962  C  CG1   . VAL A 126 ? 0.3981 0.3808 0.6043 0.0710  -0.0138 0.1103  125 VAL A CG1   
1963  C  CG2   . VAL A 126 ? 0.4258 0.4240 0.6206 0.0680  -0.0239 0.1112  125 VAL A CG2   
1973  N  N     . ASP A 127 ? 0.4879 0.4600 0.6785 0.0639  -0.0346 0.1348  126 ASP A N     
1974  C  CA    . ASP A 127 ? 0.5008 0.4624 0.6875 0.0625  -0.0340 0.1394  126 ASP A CA    
1975  C  C     . ASP A 127 ? 0.4810 0.4354 0.6725 0.0654  -0.0218 0.1310  126 ASP A C     
1976  O  O     . ASP A 127 ? 0.4703 0.4271 0.6760 0.0694  -0.0145 0.1230  126 ASP A O     
1977  C  CB    . ASP A 127 ? 0.5455 0.5051 0.7464 0.0633  -0.0398 0.1466  126 ASP A CB    
1978  C  CG    . ASP A 127 ? 0.6374 0.6027 0.8329 0.0596  -0.0524 0.1559  126 ASP A CG    
1979  O  OD1   . ASP A 127 ? 0.6406 0.6040 0.8464 0.0597  -0.0581 0.1630  126 ASP A OD1   
1980  O  OD2   . ASP A 127 ? 0.6304 0.6017 0.8117 0.0563  -0.0566 0.1560  126 ASP A OD2   
1985  N  N     . THR A 128 ? 0.4870 0.4324 0.6661 0.0627  -0.0196 0.1330  127 THR A N     
1986  C  CA    . THR A 128 ? 0.5069 0.4437 0.6904 0.0645  -0.0087 0.1260  127 THR A CA    
1987  C  C     . THR A 128 ? 0.4959 0.4296 0.7003 0.0683  -0.0057 0.1242  127 THR A C     
1988  O  O     . THR A 128 ? 0.5082 0.4399 0.7218 0.0711  0.0043  0.1147  127 THR A O     
1989  C  CB    . THR A 128 ? 0.5383 0.4661 0.7048 0.0594  -0.0085 0.1297  127 THR A CB    
1990  O  OG1   . THR A 128 ? 0.5060 0.4402 0.6481 0.0536  -0.0097 0.1260  127 THR A OG1   
1991  C  CG2   . THR A 128 ? 0.5572 0.4761 0.7264 0.0601  0.0027  0.1214  127 THR A CG2   
1999  N  N     . LYS A 129 ? 0.5168 0.4498 0.7287 0.0681  -0.0139 0.1330  128 LYS A N     
2000  C  CA    . LYS A 129 ? 0.4724 0.4024 0.7054 0.0719  -0.0110 0.1318  128 LYS A CA    
2001  C  C     . LYS A 129 ? 0.4591 0.3987 0.7083 0.0758  -0.0078 0.1253  128 LYS A C     
2002  O  O     . LYS A 129 ? 0.4856 0.4233 0.7500 0.0791  0.0004  0.1185  128 LYS A O     
2003  C  CB    . LYS A 129 ? 0.5191 0.4460 0.7558 0.0705  -0.0213 0.1437  128 LYS A CB    
2004  C  CG    . LYS A 129 ? 0.5624 0.4921 0.8230 0.0746  -0.0232 0.1454  128 LYS A CG    
2005  C  CD    . LYS A 129 ? 0.5973 0.5166 0.8709 0.0770  -0.0173 0.1437  128 LYS A CD    
2006  C  CE    . LYS A 129 ? 0.6066 0.5259 0.8975 0.0788  -0.0250 0.1525  128 LYS A CE    
2007  N  NZ    . LYS A 129 ? 0.5951 0.5263 0.9023 0.0818  -0.0277 0.1520  128 LYS A NZ    
2021  N  N     . GLN A 130 ? 0.4423 0.3922 0.6881 0.0751  -0.0139 0.1274  129 GLN A N     
2022  C  CA    . GLN A 130 ? 0.4493 0.4087 0.7075 0.0778  -0.0102 0.1208  129 GLN A CA    
2023  C  C     . GLN A 130 ? 0.4724 0.4298 0.7306 0.0793  0.0028  0.1085  129 GLN A C     
2024  O  O     . GLN A 130 ? 0.4282 0.3873 0.7020 0.0820  0.0099  0.1019  129 GLN A O     
2025  C  CB    . GLN A 130 ? 0.5343 0.5034 0.7822 0.0756  -0.0176 0.1235  129 GLN A CB    
2026  C  CG    . GLN A 130 ? 0.5273 0.5067 0.7897 0.0770  -0.0217 0.1247  129 GLN A CG    
2027  C  CD    . GLN A 130 ? 0.5790 0.5658 0.8283 0.0735  -0.0315 0.1298  129 GLN A CD    
2028  O  OE1   . GLN A 130 ? 0.5599 0.5436 0.7933 0.0698  -0.0388 0.1366  129 GLN A OE1   
2029  N  NE2   . GLN A 130 ? 0.5807 0.5770 0.8356 0.0741  -0.0314 0.1261  129 GLN A NE2   
2038  N  N     . ALA A 131 ? 0.4689 0.4229 0.7091 0.0770  0.0060  0.1052  130 ALA A N     
2039  C  CA    . ALA A 131 ? 0.3957 0.3485 0.6334 0.0776  0.0175  0.0935  130 ALA A CA    
2040  C  C     . ALA A 131 ? 0.4476 0.3903 0.6920 0.0784  0.0262  0.0886  130 ALA A C     
2041  O  O     . ALA A 131 ? 0.4428 0.3855 0.6936 0.0794  0.0359  0.0787  130 ALA A O     
2042  C  CB    . ALA A 131 ? 0.4168 0.3691 0.6342 0.0750  0.0179  0.0920  130 ALA A CB    
2048  N  N     . GLN A 132 ? 0.4376 0.3714 0.6795 0.0773  0.0228  0.0952  131 GLN A N     
2049  C  CA    . GLN A 132 ? 0.4656 0.3889 0.7136 0.0778  0.0305  0.0908  131 GLN A CA    
2050  C  C     . GLN A 132 ? 0.4528 0.3778 0.7225 0.0812  0.0336  0.0882  131 GLN A C     
2051  O  O     . GLN A 132 ? 0.4679 0.3885 0.7441 0.0819  0.0437  0.0792  131 GLN A O     
2052  C  CB    . GLN A 132 ? 0.5171 0.4306 0.7589 0.0757  0.0251  0.0997  131 GLN A CB    
2053  C  CG    . GLN A 132 ? 0.5549 0.4631 0.7763 0.0717  0.0258  0.1005  131 GLN A CG    
2054  C  CD    . GLN A 132 ? 0.6085 0.5091 0.8228 0.0686  0.0184  0.1116  131 GLN A CD    
2055  O  OE1   . GLN A 132 ? 0.6252 0.5255 0.8489 0.0696  0.0112  0.1194  131 GLN A OE1   
2056  N  NE2   . GLN A 132 ? 0.6182 0.5126 0.8156 0.0645  0.0201  0.1125  131 GLN A NE2   
2065  N  N     . ASP A 133 ? 0.4753 0.4064 0.7563 0.0830  0.0250  0.0962  132 ASP A N     
2066  C  CA    . ASP A 133 ? 0.4895 0.4227 0.7931 0.0864  0.0273  0.0949  132 ASP A CA    
2067  C  C     . ASP A 133 ? 0.4752 0.4149 0.7846 0.0874  0.0368  0.0838  132 ASP A C     
2068  O  O     . ASP A 133 ? 0.4846 0.4216 0.8071 0.0890  0.0454  0.0769  132 ASP A O     
2069  C  CB    . ASP A 133 ? 0.4828 0.4228 0.7962 0.0876  0.0155  0.1057  132 ASP A CB    
2070  C  CG    . ASP A 133 ? 0.5114 0.4442 0.8222 0.0865  0.0062  0.1172  132 ASP A CG    
2071  O  OD1   . ASP A 133 ? 0.5406 0.4623 0.8470 0.0856  0.0096  0.1168  132 ASP A OD1   
2072  O  OD2   . ASP A 133 ? 0.4825 0.4206 0.7943 0.0858  -0.0048 0.1268  132 ASP A OD2   
2077  N  N     . LEU A 134 ? 0.4566 0.4048 0.7558 0.0861  0.0353  0.0819  133 LEU A N     
2078  C  CA    . LEU A 134 ? 0.4741 0.4288 0.7767 0.0862  0.0437  0.0720  133 LEU A CA    
2079  C  C     . LEU A 134 ? 0.4668 0.4144 0.7612 0.0844  0.0555  0.0610  133 LEU A C     
2080  O  O     . LEU A 134 ? 0.4396 0.3871 0.7432 0.0848  0.0648  0.0527  133 LEU A O     
2081  C  CB    . LEU A 134 ? 0.4391 0.4035 0.7311 0.0848  0.0385  0.0734  133 LEU A CB    
2082  C  CG    . LEU A 134 ? 0.4420 0.4134 0.7348 0.0842  0.0461  0.0640  133 LEU A CG    
2083  C  CD1   . LEU A 134 ? 0.4409 0.4197 0.7545 0.0865  0.0460  0.0647  133 LEU A CD1   
2084  C  CD2   . LEU A 134 ? 0.3821 0.3598 0.6595 0.0823  0.0420  0.0644  133 LEU A CD2   
2096  N  N     . ALA A 135 ? 0.4590 0.4009 0.7354 0.0819  0.0555  0.0607  134 ALA A N     
2097  C  CA    . ALA A 135 ? 0.4355 0.3698 0.7035 0.0796  0.0661  0.0507  134 ALA A CA    
2098  C  C     . ALA A 135 ? 0.4424 0.3682 0.7231 0.0806  0.0720  0.0479  134 ALA A C     
2099  O  O     . ALA A 135 ? 0.4529 0.3758 0.7350 0.0792  0.0824  0.0377  134 ALA A O     
2100  C  CB    . ALA A 135 ? 0.4102 0.3388 0.6593 0.0770  0.0641  0.0526  134 ALA A CB    
2106  N  N     . ARG A 136 ? 0.4361 0.3574 0.7254 0.0825  0.0655  0.0568  135 ARG A N     
2107  C  CA    . ARG A 136 ? 0.4737 0.3869 0.7772 0.0839  0.0702  0.0550  135 ARG A CA    
2108  C  C     . ARG A 136 ? 0.4754 0.3940 0.7968 0.0861  0.0764  0.0491  135 ARG A C     
2109  O  O     . ARG A 136 ? 0.4946 0.4075 0.8222 0.0857  0.0861  0.0407  135 ARG A O     
2110  C  CB    . ARG A 136 ? 0.5164 0.4254 0.8268 0.0858  0.0603  0.0672  135 ARG A CB    
2111  C  CG    . ARG A 136 ? 0.5855 0.4827 0.9050 0.0864  0.0642  0.0665  135 ARG A CG    
2112  C  CD    . ARG A 136 ? 0.6162 0.5087 0.9396 0.0875  0.0532  0.0796  135 ARG A CD    
2113  N  NE    . ARG A 136 ? 0.6652 0.5533 0.9683 0.0839  0.0476  0.0855  135 ARG A NE    
2114  C  CZ    . ARG A 136 ? 0.6173 0.5110 0.9114 0.0829  0.0372  0.0949  135 ARG A CZ    
2115  N  NH1   . ARG A 136 ? 0.6050 0.5088 0.9083 0.0851  0.0301  0.1002  135 ARG A NH1   
2116  N  NH2   . ARG A 136 ? 0.6580 0.5469 0.9331 0.0791  0.0338  0.0990  135 ARG A NH2   
2130  N  N     . SER A 137 ? 0.4707 0.4001 0.8011 0.0882  0.0709  0.0534  136 SER A N     
2131  C  CA    . SER A 137 ? 0.4371 0.3720 0.7858 0.0902  0.0766  0.0485  136 SER A CA    
2132  C  C     . SER A 137 ? 0.4745 0.4108 0.8154 0.0872  0.0881  0.0358  136 SER A C     
2133  O  O     . SER A 137 ? 0.4521 0.3871 0.8045 0.0875  0.0972  0.0283  136 SER A O     
2134  C  CB    . SER A 137 ? 0.4816 0.4281 0.8401 0.0923  0.0680  0.0558  136 SER A CB    
2135  O  OG    . SER A 137 ? 0.4732 0.4280 0.8199 0.0902  0.0686  0.0522  136 SER A OG    
2141  N  N     . TYR A 138 ? 0.4530 0.3918 0.7741 0.0842  0.0876  0.0335  137 TYR A N     
2142  C  CA    . TYR A 138 ? 0.4271 0.3665 0.7371 0.0805  0.0975  0.0221  137 TYR A CA    
2143  C  C     . TYR A 138 ? 0.4396 0.3677 0.7421 0.0775  0.1063  0.0142  137 TYR A C     
2144  O  O     . TYR A 138 ? 0.4450 0.3725 0.7409 0.0740  0.1157  0.0040  137 TYR A O     
2145  C  CB    . TYR A 138 ? 0.4169 0.3615 0.7079 0.0782  0.0934  0.0228  137 TYR A CB    
2146  C  CG    . TYR A 138 ? 0.4368 0.3932 0.7315 0.0797  0.0863  0.0282  137 TYR A CG    
2147  C  CD1   . TYR A 138 ? 0.4348 0.3978 0.7486 0.0823  0.0855  0.0302  137 TYR A CD1   
2148  C  CD2   . TYR A 138 ? 0.4120 0.3730 0.6914 0.0783  0.0806  0.0309  137 TYR A CD2   
2149  C  CE1   . TYR A 138 ? 0.4152 0.3889 0.7319 0.0832  0.0788  0.0349  137 TYR A CE1   
2150  C  CE2   . TYR A 138 ? 0.4133 0.3845 0.6952 0.0793  0.0740  0.0355  137 TYR A CE2   
2151  C  CZ    . TYR A 138 ? 0.4254 0.4030 0.7256 0.0815  0.0730  0.0375  137 TYR A CZ    
2152  O  OH    . TYR A 138 ? 0.3977 0.3854 0.6999 0.0820  0.0663  0.0420  137 TYR A OH    
2162  N  N     . GLY A 139 ? 0.4291 0.3483 0.7309 0.0782  0.1032  0.0188  138 GLY A N     
2163  C  CA    . GLY A 139 ? 0.3904 0.2987 0.6830 0.0748  0.1108  0.0116  138 GLY A CA    
2164  C  C     . GLY A 139 ? 0.4004 0.3072 0.6699 0.0703  0.1121  0.0077  138 GLY A C     
2165  O  O     . GLY A 139 ? 0.4226 0.3232 0.6829 0.0661  0.1204  -0.0014 138 GLY A O     
2169  N  N     . ILE A 140 ? 0.3759 0.2881 0.6360 0.0709  0.1039  0.0143  139 ILE A N     
2170  C  CA    . ILE A 140 ? 0.3983 0.3098 0.6377 0.0670  0.1050  0.0106  139 ILE A CA    
2171  C  C     . ILE A 140 ? 0.3716 0.2797 0.6034 0.0678  0.0966  0.0198  139 ILE A C     
2172  O  O     . ILE A 140 ? 0.3228 0.2320 0.5635 0.0711  0.0883  0.0299  139 ILE A O     
2173  C  CB    . ILE A 140 ? 0.3695 0.2919 0.6022 0.0661  0.1047  0.0077  139 ILE A CB    
2174  C  CG1   . ILE A 140 ? 0.3663 0.2974 0.6050 0.0700  0.0943  0.0179  139 ILE A CG1   
2175  C  CG2   . ILE A 140 ? 0.3676 0.2930 0.6067 0.0645  0.1134  -0.0012 139 ILE A CG2   
2176  C  CD1   . ILE A 140 ? 0.3406 0.2822 0.5735 0.0692  0.0933  0.0158  139 ILE A CD1   
2188  N  N     . PRO A 141 ? 0.3602 0.2643 0.5749 0.0643  0.0983  0.0168  140 PRO A N     
2189  C  CA    . PRO A 141 ? 0.3708 0.2716 0.5770 0.0644  0.0910  0.0254  140 PRO A CA    
2190  C  C     . PRO A 141 ? 0.3975 0.3081 0.6008 0.0666  0.0823  0.0328  140 PRO A C     
2191  O  O     . PRO A 141 ? 0.3515 0.2716 0.5553 0.0673  0.0825  0.0297  140 PRO A O     
2192  C  CB    . PRO A 141 ? 0.3796 0.2743 0.5691 0.0596  0.0968  0.0182  140 PRO A CB    
2193  C  CG    . PRO A 141 ? 0.3629 0.2547 0.5539 0.0567  0.1068  0.0067  140 PRO A CG    
2194  C  CD    . PRO A 141 ? 0.3982 0.2995 0.6005 0.0593  0.1072  0.0054  140 PRO A CD    
2202  N  N     . PHE A 142 ? 0.3824 0.2907 0.5812 0.0669  0.0743  0.0427  141 PHE A N     
2203  C  CA    . PHE A 142 ? 0.3417 0.2601 0.5327 0.0667  0.0646  0.0496  141 PHE A CA    
2204  C  C     . PHE A 142 ? 0.3650 0.2830 0.5347 0.0611  0.0603  0.0518  141 PHE A C     
2205  O  O     . PHE A 142 ? 0.3550 0.2641 0.5224 0.0593  0.0602  0.0553  141 PHE A O     
2206  C  CB    . PHE A 142 ? 0.3917 0.3115 0.5985 0.0713  0.0565  0.0607  141 PHE A CB    
2207  C  CG    . PHE A 142 ? 0.3553 0.2829 0.5516 0.0700  0.0457  0.0690  141 PHE A CG    
2208  C  CD1   . PHE A 142 ? 0.3269 0.2655 0.5152 0.0690  0.0438  0.0657  141 PHE A CD1   
2209  C  CD2   . PHE A 142 ? 0.4308 0.3547 0.6240 0.0689  0.0375  0.0799  141 PHE A CD2   
2210  C  CE1   . PHE A 142 ? 0.3689 0.3144 0.5468 0.0672  0.0341  0.0724  141 PHE A CE1   
2211  C  CE2   . PHE A 142 ? 0.4121 0.3432 0.5938 0.0667  0.0280  0.0867  141 PHE A CE2   
2212  C  CZ    . PHE A 142 ? 0.3803 0.3222 0.5545 0.0659  0.0264  0.0826  141 PHE A CZ    
2222  N  N     . ILE A 143 ? 0.3278 0.2550 0.4826 0.0584  0.0571  0.0498  142 ILE A N     
2223  C  CA    . ILE A 143 ? 0.3303 0.2590 0.4654 0.0532  0.0540  0.0504  142 ILE A CA    
2224  C  C     . ILE A 143 ? 0.3521 0.2905 0.4791 0.0529  0.0459  0.0548  142 ILE A C     
2225  O  O     . ILE A 143 ? 0.2890 0.2350 0.4167 0.0542  0.0457  0.0511  142 ILE A O     
2226  C  CB    . ILE A 143 ? 0.3399 0.2688 0.4630 0.0490  0.0608  0.0399  142 ILE A CB    
2227  C  CG1   . ILE A 143 ? 0.4064 0.3266 0.5399 0.0498  0.0696  0.0339  142 ILE A CG1   
2228  C  CG2   . ILE A 143 ? 0.3796 0.3091 0.4855 0.0438  0.0584  0.0408  142 ILE A CG2   
2229  C  CD1   . ILE A 143 ? 0.4598 0.3778 0.5822 0.0448  0.0761  0.0246  142 ILE A CD1   
2241  N  N     . GLU A 144 ? 0.3385 0.2765 0.4565 0.0505  0.0395  0.0622  143 GLU A N     
2242  C  CA    . GLU A 144 ? 0.3650 0.3114 0.4719 0.0489  0.0324  0.0653  143 GLU A CA    
2243  C  C     . GLU A 144 ? 0.3071 0.2571 0.3966 0.0444  0.0348  0.0584  143 GLU A C     
2244  O  O     . GLU A 144 ? 0.2909 0.2362 0.3740 0.0412  0.0389  0.0558  143 GLU A O     
2245  C  CB    . GLU A 144 ? 0.3770 0.3212 0.4818 0.0477  0.0245  0.0765  143 GLU A CB    
2246  C  CG    . GLU A 144 ? 0.4297 0.3737 0.5525 0.0526  0.0194  0.0842  143 GLU A CG    
2247  C  CD    . GLU A 144 ? 0.5176 0.4632 0.6358 0.0509  0.0089  0.0956  143 GLU A CD    
2248  O  OE1   . GLU A 144 ? 0.5377 0.4850 0.6703 0.0546  0.0033  0.1024  143 GLU A OE1   
2249  O  OE2   . GLU A 144 ? 0.5284 0.4738 0.6292 0.0457  0.0063  0.0978  143 GLU A OE2   
2256  N  N     . THR A 145 ? 0.2689 0.2273 0.3523 0.0443  0.0324  0.0553  144 THR A N     
2257  C  CA    . THR A 145 ? 0.2547 0.2174 0.3248 0.0410  0.0346  0.0483  144 THR A CA    
2258  C  C     . THR A 145 ? 0.2716 0.2413 0.3317 0.0396  0.0284  0.0501  144 THR A C     
2259  O  O     . THR A 145 ? 0.2734 0.2456 0.3370 0.0413  0.0226  0.0556  144 THR A O     
2260  C  CB    . THR A 145 ? 0.2569 0.2220 0.3302 0.0420  0.0397  0.0397  144 THR A CB    
2261  O  OG1   . THR A 145 ? 0.2523 0.2228 0.3321 0.0450  0.0367  0.0404  144 THR A OG1   
2262  C  CG2   . THR A 145 ? 0.2647 0.2226 0.3469 0.0427  0.0467  0.0364  144 THR A CG2   
2270  N  N     . SER A 146 ? 0.2692 0.2423 0.3173 0.0365  0.0298  0.0449  145 SER A N     
2271  C  CA    . SER A 146 ? 0.2759 0.2557 0.3147 0.0353  0.0258  0.0435  145 SER A CA    
2272  C  C     . SER A 146 ? 0.2966 0.2800 0.3312 0.0344  0.0296  0.0349  145 SER A C     
2273  O  O     . SER A 146 ? 0.2656 0.2477 0.2958 0.0318  0.0336  0.0317  145 SER A O     
2274  C  CB    . SER A 146 ? 0.2816 0.2615 0.3091 0.0316  0.0227  0.0479  145 SER A CB    
2275  O  OG    . SER A 146 ? 0.2851 0.2712 0.3033 0.0301  0.0209  0.0438  145 SER A OG    
2281  N  N     . ALA A 147 ? 0.2640 0.2518 0.3004 0.0362  0.0281  0.0317  146 ALA A N     
2282  C  CA    . ALA A 147 ? 0.2763 0.2678 0.3085 0.0352  0.0301  0.0246  146 ALA A CA    
2283  C  C     . ALA A 147 ? 0.3059 0.3011 0.3280 0.0329  0.0284  0.0229  146 ALA A C     
2284  O  O     . ALA A 147 ? 0.2894 0.2872 0.3084 0.0316  0.0306  0.0175  146 ALA A O     
2285  C  CB    . ALA A 147 ? 0.2612 0.2558 0.2976 0.0374  0.0283  0.0225  146 ALA A CB    
2291  N  N     . LYS A 148 ? 0.2587 0.2545 0.2759 0.0321  0.0246  0.0274  147 LYS A N     
2292  C  CA    . LYS A 148 ? 0.3045 0.3037 0.3116 0.0294  0.0239  0.0252  147 LYS A CA    
2293  C  C     . LYS A 148 ? 0.2734 0.2712 0.2759 0.0261  0.0282  0.0248  147 LYS A C     
2294  O  O     . LYS A 148 ? 0.3113 0.3127 0.3102 0.0245  0.0309  0.0194  147 LYS A O     
2295  C  CB    . LYS A 148 ? 0.3274 0.3274 0.3292 0.0286  0.0186  0.0299  147 LYS A CB    
2296  C  CG    . LYS A 148 ? 0.3605 0.3642 0.3514 0.0258  0.0181  0.0264  147 LYS A CG    
2297  C  CD    . LYS A 148 ? 0.3693 0.3735 0.3546 0.0247  0.0122  0.0307  147 LYS A CD    
2298  C  CE    . LYS A 148 ? 0.3957 0.4029 0.3693 0.0213  0.0127  0.0265  147 LYS A CE    
2299  N  NZ    . LYS A 148 ? 0.5217 0.5283 0.4870 0.0185  0.0071  0.0313  147 LYS A NZ    
2313  N  N     . THR A 149 ? 0.2704 0.2630 0.2736 0.0249  0.0287  0.0306  148 THR A N     
2314  C  CA    . THR A 149 ? 0.2792 0.2699 0.2783 0.0212  0.0328  0.0307  148 THR A CA    
2315  C  C     . THR A 149 ? 0.2639 0.2518 0.2695 0.0214  0.0377  0.0273  148 THR A C     
2316  O  O     . THR A 149 ? 0.2565 0.2435 0.2594 0.0180  0.0415  0.0262  148 THR A O     
2317  C  CB    . THR A 149 ? 0.3100 0.2953 0.3063 0.0191  0.0308  0.0391  148 THR A CB    
2318  O  OG1   . THR A 149 ? 0.2966 0.2760 0.3036 0.0221  0.0305  0.0429  148 THR A OG1   
2319  C  CG2   . THR A 149 ? 0.3183 0.3060 0.3069 0.0180  0.0252  0.0430  148 THR A CG2   
2327  N  N     . ARG A 150 ? 0.2380 0.2245 0.2518 0.0247  0.0379  0.0257  149 ARG A N     
2328  C  CA    . ARG A 150 ? 0.2775 0.2602 0.2972 0.0245  0.0424  0.0227  149 ARG A CA    
2329  C  C     . ARG A 150 ? 0.2769 0.2512 0.3014 0.0242  0.0443  0.0276  149 ARG A C     
2330  O  O     . ARG A 150 ? 0.2700 0.2401 0.2991 0.0237  0.0486  0.0245  149 ARG A O     
2331  C  CB    . ARG A 150 ? 0.2970 0.2825 0.3130 0.0211  0.0460  0.0171  149 ARG A CB    
2332  C  CG    . ARG A 150 ? 0.2960 0.2896 0.3082 0.0212  0.0443  0.0126  149 ARG A CG    
2333  C  CD    . ARG A 150 ? 0.3139 0.3109 0.3256 0.0185  0.0474  0.0073  149 ARG A CD    
2334  N  NE    . ARG A 150 ? 0.3611 0.3582 0.3771 0.0195  0.0475  0.0035  149 ARG A NE    
2335  C  CZ    . ARG A 150 ? 0.3713 0.3633 0.3904 0.0184  0.0505  0.0026  149 ARG A CZ    
2336  N  NH1   . ARG A 150 ? 0.4020 0.3890 0.4211 0.0157  0.0539  0.0040  149 ARG A NH1   
2337  N  NH2   . ARG A 150 ? 0.3381 0.3296 0.3600 0.0196  0.0501  0.0001  149 ARG A NH2   
2351  N  N     . GLN A 151 ? 0.2810 0.2523 0.3046 0.0242  0.0412  0.0349  150 GLN A N     
2352  C  CA    . GLN A 151 ? 0.2766 0.2393 0.3068 0.0247  0.0421  0.0404  150 GLN A CA    
2353  C  C     . GLN A 151 ? 0.2864 0.2458 0.3285 0.0286  0.0444  0.0381  150 GLN A C     
2354  O  O     . GLN A 151 ? 0.2678 0.2309 0.3146 0.0319  0.0419  0.0378  150 GLN A O     
2355  C  CB    . GLN A 151 ? 0.3098 0.2708 0.3391 0.0250  0.0364  0.0496  150 GLN A CB    
2356  C  CG    . GLN A 151 ? 0.3536 0.3055 0.3926 0.0264  0.0363  0.0562  150 GLN A CG    
2357  C  CD    . GLN A 151 ? 0.4001 0.3498 0.4372 0.0257  0.0297  0.0665  150 GLN A CD    
2358  O  OE1   . GLN A 151 ? 0.3861 0.3406 0.4118 0.0228  0.0259  0.0686  150 GLN A OE1   
2359  N  NE2   . GLN A 151 ? 0.5031 0.4452 0.5515 0.0281  0.0283  0.0731  150 GLN A NE2   
2368  N  N     . GLY A 152 ? 0.2660 0.2184 0.3129 0.0277  0.0495  0.0363  151 GLY A N     
2369  C  CA    . GLY A 152 ? 0.2782 0.2258 0.3367 0.0308  0.0529  0.0342  151 GLY A CA    
2370  C  C     . GLY A 152 ? 0.3023 0.2542 0.3613 0.0313  0.0559  0.0261  151 GLY A C     
2371  O  O     . GLY A 152 ? 0.3048 0.2529 0.3728 0.0334  0.0597  0.0235  151 GLY A O     
2375  N  N     . VAL A 153 ? 0.2599 0.2192 0.3100 0.0294  0.0545  0.0221  152 VAL A N     
2376  C  CA    . VAL A 153 ? 0.2289 0.1923 0.2791 0.0298  0.0559  0.0158  152 VAL A CA    
2377  C  C     . VAL A 153 ? 0.2726 0.2308 0.3241 0.0272  0.0622  0.0099  152 VAL A C     
2378  O  O     . VAL A 153 ? 0.2684 0.2239 0.3259 0.0284  0.0657  0.0069  152 VAL A O     
2379  C  CB    . VAL A 153 ? 0.2689 0.2407 0.3103 0.0283  0.0526  0.0132  152 VAL A CB    
2380  C  CG1   . VAL A 153 ? 0.2808 0.2557 0.3216 0.0278  0.0539  0.0071  152 VAL A CG1   
2381  C  CG2   . VAL A 153 ? 0.2659 0.2423 0.3060 0.0308  0.0467  0.0179  152 VAL A CG2   
2391  N  N     . ASP A 154 ? 0.3124 0.2690 0.3583 0.0231  0.0642  0.0080  153 ASP A N     
2392  C  CA    . ASP A 154 ? 0.2875 0.2386 0.3338 0.0198  0.0699  0.0024  153 ASP A CA    
2393  C  C     . ASP A 154 ? 0.3231 0.2646 0.3791 0.0218  0.0742  0.0034  153 ASP A C     
2394  O  O     . ASP A 154 ? 0.3651 0.3031 0.4243 0.0213  0.0790  -0.0019 153 ASP A O     
2395  C  CB    . ASP A 154 ? 0.3486 0.2993 0.3885 0.0148  0.0709  0.0011  153 ASP A CB    
2396  C  CG    . ASP A 154 ? 0.3808 0.3405 0.4135 0.0122  0.0685  -0.0028 153 ASP A CG    
2397  O  OD1   . ASP A 154 ? 0.3619 0.3268 0.3938 0.0135  0.0665  -0.0052 153 ASP A OD1   
2398  O  OD2   . ASP A 154 ? 0.4143 0.3763 0.4430 0.0087  0.0684  -0.0032 153 ASP A OD2   
2403  N  N     . ASP A 155 ? 0.2831 0.2201 0.3439 0.0239  0.0725  0.0103  154 ASP A N     
2404  C  CA    . ASP A 155 ? 0.3694 0.2966 0.4414 0.0263  0.0762  0.0120  154 ASP A CA    
2405  C  C     . ASP A 155 ? 0.3357 0.2639 0.4171 0.0305  0.0781  0.0098  154 ASP A C     
2406  O  O     . ASP A 155 ? 0.3436 0.2650 0.4328 0.0310  0.0842  0.0057  154 ASP A O     
2407  C  CB    . ASP A 155 ? 0.3664 0.2901 0.4420 0.0282  0.0720  0.0214  154 ASP A CB    
2408  C  CG    . ASP A 155 ? 0.4335 0.3459 0.5216 0.0304  0.0752  0.0242  154 ASP A CG    
2409  O  OD1   . ASP A 155 ? 0.4717 0.3770 0.5643 0.0293  0.0819  0.0181  154 ASP A OD1   
2410  O  OD2   . ASP A 155 ? 0.4383 0.3487 0.5320 0.0332  0.0706  0.0329  154 ASP A OD2   
2415  N  N     . ALA A 156 ? 0.2713 0.2080 0.3522 0.0332  0.0732  0.0120  155 ALA A N     
2416  C  CA    . ALA A 156 ? 0.3138 0.2522 0.4047 0.0370  0.0749  0.0106  155 ALA A CA    
2417  C  C     . ALA A 156 ? 0.3124 0.2508 0.4002 0.0340  0.0811  0.0014  155 ALA A C     
2418  O  O     . ALA A 156 ? 0.2794 0.2133 0.3763 0.0353  0.0872  -0.0023 155 ALA A O     
2419  C  CB    . ALA A 156 ? 0.2673 0.2150 0.3573 0.0396  0.0680  0.0149  155 ALA A CB    
2425  N  N     . PHE A 157 ? 0.2625 0.2061 0.3378 0.0299  0.0797  -0.0024 156 PHE A N     
2426  C  CA    . PHE A 157 ? 0.2843 0.2280 0.3545 0.0261  0.0846  -0.0104 156 PHE A CA    
2427  C  C     . PHE A 157 ? 0.3262 0.2607 0.3961 0.0224  0.0915  -0.0157 156 PHE A C     
2428  O  O     . PHE A 157 ? 0.2987 0.2297 0.3707 0.0208  0.0980  -0.0219 156 PHE A O     
2429  C  CB    . PHE A 157 ? 0.2780 0.2293 0.3359 0.0227  0.0800  -0.0120 156 PHE A CB    
2430  C  CG    . PHE A 157 ? 0.2519 0.2112 0.3099 0.0256  0.0748  -0.0092 156 PHE A CG    
2431  C  CD1   . PHE A 157 ? 0.2489 0.2106 0.3082 0.0254  0.0768  -0.0124 156 PHE A CD1   
2432  C  CD2   . PHE A 157 ? 0.2590 0.2232 0.3155 0.0279  0.0681  -0.0036 156 PHE A CD2   
2433  C  CE1   . PHE A 157 ? 0.2209 0.1897 0.2803 0.0277  0.0716  -0.0096 156 PHE A CE1   
2434  C  CE2   . PHE A 157 ? 0.2249 0.1957 0.2814 0.0303  0.0632  -0.0013 156 PHE A CE2   
2435  C  CZ    . PHE A 157 ? 0.2586 0.2316 0.3169 0.0302  0.0648  -0.0042 156 PHE A CZ    
2445  N  N     . TYR A 158 ? 0.2870 0.2174 0.3540 0.0204  0.0907  -0.0137 157 TYR A N     
2446  C  CA    . TYR A 158 ? 0.3747 0.2955 0.4414 0.0164  0.0972  -0.0188 157 TYR A CA    
2447  C  C     . TYR A 158 ? 0.3518 0.2635 0.4324 0.0201  0.1030  -0.0190 157 TYR A C     
2448  O  O     . TYR A 158 ? 0.3633 0.2679 0.4452 0.0174  0.1104  -0.0261 157 TYR A O     
2449  C  CB    . TYR A 158 ? 0.3269 0.2453 0.3885 0.0133  0.0951  -0.0160 157 TYR A CB    
2450  C  CG    . TYR A 158 ? 0.3563 0.2828 0.4060 0.0089  0.0910  -0.0173 157 TYR A CG    
2451  C  CD1   . TYR A 158 ? 0.3072 0.2429 0.3514 0.0087  0.0876  -0.0190 157 TYR A CD1   
2452  C  CD2   . TYR A 158 ? 0.3806 0.3057 0.4256 0.0049  0.0902  -0.0162 157 TYR A CD2   
2453  C  CE1   . TYR A 158 ? 0.3793 0.3224 0.4149 0.0052  0.0835  -0.0198 157 TYR A CE1   
2454  C  CE2   . TYR A 158 ? 0.4134 0.3467 0.4498 0.0012  0.0866  -0.0174 157 TYR A CE2   
2455  C  CZ    . TYR A 158 ? 0.4037 0.3459 0.4360 0.0016  0.0832  -0.0192 157 TYR A CZ    
2456  O  OH    . TYR A 158 ? 0.4514 0.4020 0.4775 -0.0014 0.0792  -0.0201 157 TYR A OH    
2466  N  N     . THR A 159 ? 0.3097 0.2215 0.4011 0.0262  0.0997  -0.0116 158 THR A N     
2467  C  CA    . THR A 159 ? 0.3368 0.2404 0.4440 0.0304  0.1045  -0.0110 158 THR A CA    
2468  C  C     . THR A 159 ? 0.3668 0.2721 0.4796 0.0314  0.1105  -0.0178 158 THR A C     
2469  O  O     . THR A 159 ? 0.3843 0.2815 0.5042 0.0310  0.1188  -0.0239 158 THR A O     
2470  C  CB    . THR A 159 ? 0.3799 0.2847 0.4977 0.0364  0.0981  -0.0006 158 THR A CB    
2471  O  OG1   . THR A 159 ? 0.3864 0.2878 0.4989 0.0346  0.0938  0.0055  158 THR A OG1   
2472  C  CG2   . THR A 159 ? 0.3541 0.2517 0.4916 0.0419  0.1023  0.0006  158 THR A CG2   
2480  N  N     . LEU A 160 ? 0.3390 0.2547 0.4474 0.0320  0.1070  -0.0176 159 LEU A N     
2481  C  CA    . LEU A 160 ? 0.2882 0.2064 0.4001 0.0319  0.1128  -0.0240 159 LEU A CA    
2482  C  C     . LEU A 160 ? 0.3611 0.2740 0.4636 0.0252  0.1207  -0.0341 159 LEU A C     
2483  O  O     . LEU A 160 ? 0.3726 0.2808 0.4823 0.0250  0.1294  -0.0407 159 LEU A O     
2484  C  CB    . LEU A 160 ? 0.2698 0.1997 0.3757 0.0323  0.1068  -0.0216 159 LEU A CB    
2485  C  CG    . LEU A 160 ? 0.2567 0.1905 0.3651 0.0316  0.1121  -0.0273 159 LEU A CG    
2486  C  CD1   . LEU A 160 ? 0.2803 0.2102 0.4084 0.0367  0.1185  -0.0279 159 LEU A CD1   
2487  C  CD2   . LEU A 160 ? 0.2526 0.1973 0.3565 0.0324  0.1052  -0.0235 159 LEU A CD2   
2499  N  N     . VAL A 161 ? 0.3218 0.2354 0.4089 0.0193  0.1180  -0.0358 160 VAL A N     
2500  C  CA    . VAL A 161 ? 0.3813 0.2896 0.4585 0.0120  0.1245  -0.0451 160 VAL A CA    
2501  C  C     . VAL A 161 ? 0.4416 0.3372 0.5278 0.0122  0.1325  -0.0490 160 VAL A C     
2502  O  O     . VAL A 161 ? 0.4116 0.3017 0.4990 0.0094  0.1415  -0.0575 160 VAL A O     
2503  C  CB    . VAL A 161 ? 0.3370 0.2486 0.3984 0.0060  0.1192  -0.0451 160 VAL A CB    
2504  C  CG1   . VAL A 161 ? 0.4338 0.3384 0.4857 -0.0021 0.1254  -0.0540 160 VAL A CG1   
2505  C  CG2   . VAL A 161 ? 0.3695 0.2925 0.4224 0.0053  0.1126  -0.0430 160 VAL A CG2   
2515  N  N     . ARG A 162 ? 0.3944 0.2849 0.4872 0.0152  0.1297  -0.0430 161 ARG A N     
2516  C  CA    . ARG A 162 ? 0.4492 0.3265 0.5521 0.0158  0.1368  -0.0460 161 ARG A CA    
2517  C  C     . ARG A 162 ? 0.4613 0.3360 0.5802 0.0205  0.1437  -0.0491 161 ARG A C     
2518  O  O     . ARG A 162 ? 0.5068 0.3757 0.6277 0.0170  0.1501  -0.0554 161 ARG A O     
2519  C  CB    . ARG A 162 ? 0.4340 0.3068 0.5430 0.0189  0.1315  -0.0370 161 ARG A CB    
2520  C  CG    . ARG A 162 ? 0.4481 0.3217 0.5422 0.0128  0.1271  -0.0358 161 ARG A CG    
2521  C  CD    . ARG A 162 ? 0.4577 0.3247 0.5568 0.0143  0.1237  -0.0280 161 ARG A CD    
2522  N  NE    . ARG A 162 ? 0.4623 0.3334 0.5477 0.0088  0.1189  -0.0261 161 ARG A NE    
2523  C  CZ    . ARG A 162 ? 0.4259 0.3059 0.5066 0.0101  0.1110  -0.0187 161 ARG A CZ    
2524  N  NH1   . ARG A 162 ? 0.4898 0.3753 0.5771 0.0164  0.1063  -0.0119 161 ARG A NH1   
2525  N  NH2   . ARG A 162 ? 0.4811 0.3651 0.5504 0.0048  0.1080  -0.0184 161 ARG A NH2   
2539  N  N     . GLU A 163 ? 0.4417 0.3250 0.5699 0.0265  0.1395  -0.0432 162 GLU A N     
2540  C  CA    . GLU A 163 ? 0.4597 0.3459 0.6016 0.0291  0.1426  -0.0442 162 GLU A CA    
2541  C  C     . GLU A 163 ? 0.4772 0.3661 0.6104 0.0229  0.1493  -0.0540 162 GLU A C     
2542  O  O     . GLU A 163 ? 0.4803 0.3665 0.6212 0.0218  0.1555  -0.0588 162 GLU A O     
2543  C  CB    . GLU A 163 ? 0.4695 0.3648 0.6226 0.0360  0.1361  -0.0358 162 GLU A CB    
2544  C  CG    . GLU A 163 ? 0.4084 0.3012 0.5713 0.0420  0.1290  -0.0251 162 GLU A CG    
2545  C  CD    . GLU A 163 ? 0.4498 0.3353 0.6283 0.0445  0.1308  -0.0230 162 GLU A CD    
2546  O  OE1   . GLU A 163 ? 0.4677 0.3568 0.6602 0.0473  0.1323  -0.0230 162 GLU A OE1   
2547  O  OE2   . GLU A 163 ? 0.5072 0.3833 0.6840 0.0434  0.1307  -0.0213 162 GLU A OE2   
2554  N  N     . ILE A 164 ? 0.4232 0.3173 0.5403 0.0186  0.1480  -0.0570 163 ILE A N     
2555  C  CA    . ILE A 164 ? 0.4645 0.3605 0.5711 0.0115  0.1538  -0.0657 163 ILE A CA    
2556  C  C     . ILE A 164 ? 0.5321 0.4182 0.6324 0.0047  0.1604  -0.0735 163 ILE A C     
2557  O  O     . ILE A 164 ? 0.5810 0.4647 0.6845 0.0018  0.1672  -0.0795 163 ILE A O     
2558  C  CB    . ILE A 164 ? 0.4267 0.3301 0.5168 0.0079  0.1501  -0.0665 163 ILE A CB    
2559  C  CG1   . ILE A 164 ? 0.3724 0.2857 0.4696 0.0143  0.1443  -0.0594 163 ILE A CG1   
2560  C  CG2   . ILE A 164 ? 0.4561 0.3603 0.5332 -0.0006 0.1554  -0.0750 163 ILE A CG2   
2561  C  CD1   . ILE A 164 ? 0.3375 0.2597 0.4191 0.0109  0.1379  -0.0578 163 ILE A CD1   
2573  N  N     . ARG A 165 ? 0.5039 0.3840 0.5956 0.0020  0.1587  -0.0737 164 ARG A N     
2574  C  CA    . ARG A 165 ? 0.5858 0.4561 0.6717 -0.0046 0.1645  -0.0807 164 ARG A CA    
2575  C  C     . ARG A 165 ? 0.6276 0.4918 0.7300 -0.0018 0.1701  -0.0819 164 ARG A C     
2576  O  O     . ARG A 165 ? 0.6997 0.5600 0.7996 -0.0072 0.1773  -0.0897 164 ARG A O     
2577  C  CB    . ARG A 165 ? 0.5482 0.4123 0.6282 -0.0059 0.1611  -0.0785 164 ARG A CB    
2578  C  CG    . ARG A 165 ? 0.5780 0.4470 0.6406 -0.0106 0.1566  -0.0793 164 ARG A CG    
2579  C  CD    . ARG A 165 ? 0.5898 0.4569 0.6486 -0.0120 0.1501  -0.0739 164 ARG A CD    
2580  N  NE    . ARG A 165 ? 0.6118 0.4875 0.6540 -0.0182 0.1431  -0.0731 164 ARG A NE    
2581  C  CZ    . ARG A 165 ? 0.6097 0.4872 0.6471 -0.0204 0.1369  -0.0686 164 ARG A CZ    
2582  N  NH1   . ARG A 165 ? 0.6313 0.5020 0.6770 -0.0176 0.1368  -0.0643 164 ARG A NH1   
2583  N  NH2   . ARG A 165 ? 0.6193 0.5056 0.6439 -0.0256 0.1308  -0.0683 164 ARG A NH2   
2597  N  N     . LYS A 166 ? 0.6069 0.4705 0.7263 0.0066  0.1667  -0.0739 165 LYS A N     
2598  C  CA    . LYS A 166 ? 0.6377 0.4959 0.7749 0.0103  0.1709  -0.0738 165 LYS A CA    
2599  C  C     . LYS A 166 ? 0.6652 0.5280 0.8089 0.0098  0.1768  -0.0789 165 LYS A C     
2600  O  O     . LYS A 166 ? 0.7347 0.5917 0.8836 0.0073  0.1843  -0.0853 165 LYS A O     
2601  C  CB    . LYS A 166 ? 0.5797 0.4387 0.7330 0.0194  0.1642  -0.0628 165 LYS A CB    
2602  C  CG    . LYS A 166 ? 0.6452 0.4945 0.8001 0.0201  0.1618  -0.0586 165 LYS A CG    
2603  C  CD    . LYS A 166 ? 0.6190 0.4704 0.7849 0.0279  0.1532  -0.0464 165 LYS A CD    
2604  C  CE    . LYS A 166 ? 0.6468 0.5031 0.8327 0.0347  0.1522  -0.0420 165 LYS A CE    
2605  N  NZ    . LYS A 166 ? 0.7147 0.5735 0.9102 0.0415  0.1428  -0.0296 165 LYS A NZ    
2619  N  N     . HIS A 167 ? 0.6479 0.5209 0.7924 0.0124  0.1737  -0.0761 166 HIS A N     
2620  C  CA    . HIS A 167 ? 0.6840 0.5617 0.8356 0.0120  0.1792  -0.0804 166 HIS A CA    
2621  C  C     . HIS A 167 ? 0.7186 0.5940 0.8548 0.0023  0.1868  -0.0911 166 HIS A C     
2622  O  O     . HIS A 167 ? 0.7526 0.6276 0.8952 0.0005  0.1941  -0.0969 166 HIS A O     
2623  C  CB    . HIS A 167 ? 0.6195 0.5085 0.7735 0.0163  0.1734  -0.0746 166 HIS A CB    
2624  C  CG    . HIS A 167 ? 0.6214 0.5163 0.7781 0.0143  0.1787  -0.0795 166 HIS A CG    
2625  N  ND1   . HIS A 167 ? 0.6331 0.5298 0.7725 0.0062  0.1826  -0.0867 166 HIS A ND1   
2626  C  CD2   . HIS A 167 ? 0.5790 0.4786 0.7534 0.0190  0.1804  -0.0778 166 HIS A CD2   
2627  C  CE1   . HIS A 167 ? 0.6409 0.5427 0.7869 0.0060  0.1869  -0.0894 166 HIS A CE1   
2628  N  NE2   . HIS A 167 ? 0.5837 0.4875 0.7513 0.0138  0.1859  -0.0843 166 HIS A NE2   
2636  N  N     . LYS A 168 ? 0.7345 0.6084 0.8504 -0.0043 0.1850  -0.0939 167 LYS A N     
2637  C  CA    . LYS A 168 ? 0.7977 0.6682 0.8973 -0.0146 0.1912  -0.1035 167 LYS A CA    
2638  C  C     . LYS A 168 ? 0.8923 0.7517 0.9929 -0.0182 0.1970  -0.1089 167 LYS A C     
2639  O  O     . LYS A 168 ? 0.9332 0.7891 1.0216 -0.0271 0.2029  -0.1174 167 LYS A O     
2640  C  CB    . LYS A 168 ? 0.7556 0.6294 0.8335 -0.0206 0.1860  -0.1038 167 LYS A CB    
2641  C  CG    . LYS A 168 ? 0.7465 0.6310 0.8218 -0.0177 0.1804  -0.0989 167 LYS A CG    
2642  C  CD    . LYS A 168 ? 0.7048 0.5929 0.7576 -0.0256 0.1771  -0.1013 167 LYS A CD    
2643  C  CE    . LYS A 168 ? 0.6708 0.5581 0.7168 -0.0246 0.1703  -0.0971 167 LYS A CE    
2644  N  NZ    . LYS A 168 ? 0.6107 0.4994 0.6347 -0.0339 0.1678  -0.1008 167 LYS A NZ    
2658  N  N     . GLU A 169 ? 0.9877 0.8416 1.1021 -0.0120 0.1953  -0.1041 168 GLU A N     
2659  C  CA    . GLU A 169 ? 0.9691 0.8120 1.0851 -0.0149 0.2000  -0.1082 168 GLU A CA    
2660  C  C     . GLU A 169 ? 1.0289 0.8678 1.1227 -0.0248 0.2000  -0.1137 168 GLU A C     
2661  O  O     . GLU A 169 ? 1.0482 0.8831 1.1328 -0.0330 0.2066  -0.1224 168 GLU A O     
2662  C  CB    . GLU A 169 ? 0.9585 0.7974 1.0855 -0.0159 0.2096  -0.1152 168 GLU A CB    
2663  C  CG    . GLU A 169 ? 0.9676 0.8088 1.1192 -0.0061 0.2096  -0.1099 168 GLU A CG    
2664  C  CD    . GLU A 169 ? 1.0190 0.8684 1.1755 -0.0058 0.2132  -0.1125 168 GLU A CD    
2665  O  OE1   . GLU A 169 ? 1.0133 0.8619 1.1595 -0.0136 0.2205  -0.1215 168 GLU A OE1   
2666  O  OE2   . GLU A 169 ? 1.0330 0.8895 1.2028 0.0018  0.2086  -0.1054 168 GLU A OE2   
2673  N  N     . LYS A 170 ? 0.9700 0.8105 1.0558 -0.0241 0.1924  -0.1083 169 LYS A N     
2674  C  CA    . LYS A 170 ? 0.9806 0.8179 1.0469 -0.0330 0.1910  -0.1122 169 LYS A CA    
2675  C  C     . LYS A 170 ? 0.9541 0.7881 1.0209 -0.0299 0.1846  -0.1057 169 LYS A C     
2676  O  O     . LYS A 170 ? 0.8757 0.7160 0.9430 -0.0250 0.1778  -0.0989 169 LYS A O     
2677  C  CB    . LYS A 170 ? 0.9638 0.8095 1.0121 -0.0391 0.1885  -0.1147 169 LYS A CB    
2678  C  CG    . LYS A 170 ? 0.9331 0.7850 0.9843 -0.0388 0.1923  -0.1171 169 LYS A CG    
2679  C  CD    . LYS A 170 ? 0.9326 0.7908 0.9636 -0.0473 0.1907  -0.1208 169 LYS A CD    
2680  C  CE    . LYS A 170 ? 0.9542 0.8143 0.9853 -0.0509 0.1977  -0.1265 169 LYS A CE    
2681  N  NZ    . LYS A 170 ? 1.0006 0.8626 1.0096 -0.0625 0.1982  -0.1322 169 LYS A NZ    
2695  N  N     . VAL B 3   ? 0.8483 0.7197 0.9000 -0.0668 -0.1379 0.0172  2   VAL B N     
2696  C  CA    . VAL B 3   ? 0.8296 0.7089 0.8843 -0.0666 -0.1344 0.0254  2   VAL B CA    
2697  C  C     . VAL B 3   ? 0.7268 0.6139 0.7798 -0.0578 -0.1287 0.0238  2   VAL B C     
2698  O  O     . VAL B 3   ? 0.6697 0.5518 0.7197 -0.0516 -0.1280 0.0169  2   VAL B O     
2699  C  CB    . VAL B 3   ? 0.8235 0.6895 0.8793 -0.0692 -0.1375 0.0303  2   VAL B CB    
2700  C  CG1   . VAL B 3   ? 0.7916 0.6667 0.8492 -0.0731 -0.1345 0.0395  2   VAL B CG1   
2701  C  CG2   . VAL B 3   ? 0.8686 0.7223 0.9254 -0.0765 -0.1438 0.0293  2   VAL B CG2   
2710  N  N     . ASN B 4   ? 0.6496 0.5488 0.7046 -0.0579 -0.1242 0.0299  3   ASN B N     
2711  C  CA    . ASN B 4   ? 0.5108 0.4183 0.5644 -0.0505 -0.1185 0.0290  3   ASN B CA    
2712  C  C     . ASN B 4   ? 0.5266 0.4228 0.5780 -0.0446 -0.1189 0.0267  3   ASN B C     
2713  O  O     . ASN B 4   ? 0.5792 0.4656 0.6314 -0.0470 -0.1220 0.0307  3   ASN B O     
2714  C  CB    . ASN B 4   ? 0.4667 0.3863 0.5229 -0.0527 -0.1137 0.0360  3   ASN B CB    
2715  C  CG    . ASN B 4   ? 0.4014 0.3360 0.4621 -0.0556 -0.1114 0.0373  3   ASN B CG    
2716  O  OD1   . ASN B 4   ? 0.4370 0.3741 0.4978 -0.0549 -0.1134 0.0332  3   ASN B OD1   
2717  N  ND2   . ASN B 4   ? 0.4061 0.3507 0.4709 -0.0590 -0.1072 0.0431  3   ASN B ND2   
2724  N  N     . PRO B 5   ? 0.4664 0.3636 0.5158 -0.0371 -0.1163 0.0209  4   PRO B N     
2725  C  CA    . PRO B 5   ? 0.4931 0.3808 0.5425 -0.0312 -0.1166 0.0186  4   PRO B CA    
2726  C  C     . PRO B 5   ? 0.4817 0.3738 0.5314 -0.0298 -0.1139 0.0249  4   PRO B C     
2727  O  O     . PRO B 5   ? 0.4252 0.3288 0.4743 -0.0321 -0.1101 0.0294  4   PRO B O     
2728  C  CB    . PRO B 5   ? 0.4752 0.3653 0.5222 -0.0247 -0.1136 0.0103  4   PRO B CB    
2729  C  CG    . PRO B 5   ? 0.4974 0.4019 0.5427 -0.0261 -0.1103 0.0112  4   PRO B CG    
2730  C  CD    . PRO B 5   ? 0.4738 0.3803 0.5211 -0.0342 -0.1135 0.0159  4   PRO B CD    
2738  N  N     . THR B 6   ? 0.4446 0.3272 0.4956 -0.0261 -0.1160 0.0249  5   THR B N     
2739  C  CA    . THR B 6   ? 0.4169 0.3020 0.4673 -0.0250 -0.1146 0.0307  5   THR B CA    
2740  C  C     . THR B 6   ? 0.4256 0.3085 0.4779 -0.0165 -0.1134 0.0259  5   THR B C     
2741  O  O     . THR B 6   ? 0.4761 0.3489 0.5320 -0.0129 -0.1165 0.0207  5   THR B O     
2742  C  CB    . THR B 6   ? 0.4283 0.3036 0.4793 -0.0307 -0.1201 0.0382  5   THR B CB    
2743  O  OG1   . THR B 6   ? 0.4469 0.3255 0.4966 -0.0391 -0.1204 0.0424  5   THR B OG1   
2744  C  CG2   . THR B 6   ? 0.4834 0.3613 0.5322 -0.0304 -0.1191 0.0443  5   THR B CG2   
2752  N  N     . VAL B 7   ? 0.3747 0.2675 0.4251 -0.0135 -0.1086 0.0271  6   VAL B N     
2753  C  CA    . VAL B 7   ? 0.3852 0.2779 0.4377 -0.0060 -0.1071 0.0232  6   VAL B CA    
2754  C  C     . VAL B 7   ? 0.3440 0.2382 0.3956 -0.0066 -0.1075 0.0299  6   VAL B C     
2755  O  O     . VAL B 7   ? 0.3528 0.2514 0.4003 -0.0124 -0.1066 0.0363  6   VAL B O     
2756  C  CB    . VAL B 7   ? 0.3620 0.2652 0.4124 -0.0017 -0.1008 0.0173  6   VAL B CB    
2757  C  CG1   . VAL B 7   ? 0.3566 0.2574 0.4067 -0.0011 -0.1009 0.0102  6   VAL B CG1   
2758  C  CG2   . VAL B 7   ? 0.3797 0.2949 0.4263 -0.0050 -0.0962 0.0214  6   VAL B CG2   
2768  N  N     . PHE B 8   ? 0.3723 0.2631 0.4278 -0.0010 -0.1088 0.0281  7   PHE B N     
2769  C  CA    . PHE B 8   ? 0.3675 0.2592 0.4224 -0.0013 -0.1103 0.0342  7   PHE B CA    
2770  C  C     . PHE B 8   ? 0.3603 0.2597 0.4165 0.0050  -0.1058 0.0300  7   PHE B C     
2771  O  O     . PHE B 8   ? 0.3314 0.2311 0.3916 0.0109  -0.1036 0.0225  7   PHE B O     
2772  C  CB    . PHE B 8   ? 0.3556 0.2342 0.4164 -0.0013 -0.1187 0.0382  7   PHE B CB    
2773  C  CG    . PHE B 8   ? 0.3585 0.2317 0.4288 0.0068  -0.1203 0.0318  7   PHE B CG    
2774  C  CD1   . PHE B 8   ? 0.4036 0.2806 0.4780 0.0118  -0.1199 0.0315  7   PHE B CD1   
2775  C  CD2   . PHE B 8   ? 0.4363 0.3007 0.5119 0.0091  -0.1219 0.0255  7   PHE B CD2   
2776  C  CE1   . PHE B 8   ? 0.4063 0.2794 0.4909 0.0194  -0.1206 0.0253  7   PHE B CE1   
2777  C  CE2   . PHE B 8   ? 0.4497 0.3095 0.5348 0.0166  -0.1222 0.0186  7   PHE B CE2   
2778  C  CZ    . PHE B 8   ? 0.4136 0.2783 0.5038 0.0219  -0.1213 0.0185  7   PHE B CZ    
2788  N  N     . PHE B 9   ? 0.3244 0.2300 0.3765 0.0032  -0.1042 0.0349  8   PHE B N     
2789  C  CA    . PHE B 9   ? 0.2958 0.2072 0.3494 0.0081  -0.1015 0.0328  8   PHE B CA    
2790  C  C     . PHE B 9   ? 0.3418 0.2482 0.3969 0.0066  -0.1079 0.0395  8   PHE B C     
2791  O  O     . PHE B 9   ? 0.3164 0.2214 0.3652 -0.0004 -0.1103 0.0468  8   PHE B O     
2792  C  CB    . PHE B 9   ? 0.3180 0.2413 0.3646 0.0067  -0.0941 0.0328  8   PHE B CB    
2793  C  CG    . PHE B 9   ? 0.2825 0.2125 0.3277 0.0084  -0.0878 0.0272  8   PHE B CG    
2794  C  CD1   . PHE B 9   ? 0.2944 0.2210 0.3430 0.0112  -0.0884 0.0216  8   PHE B CD1   
2795  C  CD2   . PHE B 9   ? 0.2851 0.2250 0.3255 0.0072  -0.0813 0.0275  8   PHE B CD2   
2796  C  CE1   . PHE B 9   ? 0.2901 0.2233 0.3364 0.0121  -0.0834 0.0174  8   PHE B CE1   
2797  C  CE2   . PHE B 9   ? 0.2373 0.1835 0.2771 0.0087  -0.0763 0.0234  8   PHE B CE2   
2798  C  CZ    . PHE B 9   ? 0.2533 0.1964 0.2958 0.0111  -0.0777 0.0186  8   PHE B CZ    
2808  N  N     . ASP B 10  ? 0.3167 0.2207 0.3802 0.0126  -0.1107 0.0373  9   ASP B N     
2809  C  CA    . ASP B 10  ? 0.3288 0.2309 0.3942 0.0117  -0.1165 0.0436  9   ASP B CA    
2810  C  C     . ASP B 10  ? 0.3554 0.2686 0.4170 0.0130  -0.1109 0.0422  9   ASP B C     
2811  O  O     . ASP B 10  ? 0.3180 0.2364 0.3848 0.0193  -0.1065 0.0352  9   ASP B O     
2812  C  CB    . ASP B 10  ? 0.3479 0.2416 0.4271 0.0176  -0.1232 0.0425  9   ASP B CB    
2813  C  CG    . ASP B 10  ? 0.3965 0.2775 0.4789 0.0150  -0.1301 0.0460  9   ASP B CG    
2814  O  OD1   . ASP B 10  ? 0.4297 0.3074 0.5043 0.0074  -0.1337 0.0542  9   ASP B OD1   
2815  O  OD2   . ASP B 10  ? 0.4498 0.3236 0.5419 0.0201  -0.1315 0.0405  9   ASP B OD2   
2820  N  N     . ILE B 11  ? 0.3199 0.2369 0.3716 0.0063  -0.1105 0.0484  10  ILE B N     
2821  C  CA    . ILE B 11  ? 0.2653 0.1921 0.3117 0.0061  -0.1048 0.0471  10  ILE B CA    
2822  C  C     . ILE B 11  ? 0.2952 0.2219 0.3451 0.0068  -0.1105 0.0508  10  ILE B C     
2823  O  O     . ILE B 11  ? 0.3229 0.2431 0.3726 0.0029  -0.1187 0.0582  10  ILE B O     
2824  C  CB    . ILE B 11  ? 0.3114 0.2425 0.3449 -0.0020 -0.1002 0.0507  10  ILE B CB    
2825  C  CG1   . ILE B 11  ? 0.2989 0.2310 0.3303 -0.0032 -0.0952 0.0480  10  ILE B CG1   
2826  C  CG2   . ILE B 11  ? 0.2747 0.2151 0.3033 -0.0019 -0.0940 0.0485  10  ILE B CG2   
2827  C  CD1   . ILE B 11  ? 0.2804 0.2185 0.3154 0.0028  -0.0886 0.0401  10  ILE B CD1   
2839  N  N     . ALA B 12  ? 0.2836 0.2178 0.3362 0.0111  -0.1064 0.0464  11  ALA B N     
2840  C  CA    . ALA B 12  ? 0.3170 0.2533 0.3733 0.0116  -0.1111 0.0494  11  ALA B CA    
2841  C  C     . ALA B 12  ? 0.3224 0.2679 0.3700 0.0090  -0.1047 0.0480  11  ALA B C     
2842  O  O     . ALA B 12  ? 0.2876 0.2387 0.3312 0.0102  -0.0958 0.0425  11  ALA B O     
2843  C  CB    . ALA B 12  ? 0.3191 0.2547 0.3917 0.0205  -0.1136 0.0446  11  ALA B CB    
2849  N  N     . VAL B 13  ? 0.3030 0.2498 0.3478 0.0051  -0.1095 0.0533  12  VAL B N     
2850  C  CA    . VAL B 13  ? 0.2872 0.2416 0.3234 0.0017  -0.1044 0.0523  12  VAL B CA    
2851  C  C     . VAL B 13  ? 0.3316 0.2896 0.3772 0.0055  -0.1087 0.0521  12  VAL B C     
2852  O  O     . VAL B 13  ? 0.2984 0.2528 0.3482 0.0037  -0.1186 0.0586  12  VAL B O     
2853  C  CB    . VAL B 13  ? 0.3450 0.2980 0.3658 -0.0088 -0.1056 0.0589  12  VAL B CB    
2854  C  CG1   . VAL B 13  ? 0.3336 0.2939 0.3453 -0.0123 -0.0994 0.0567  12  VAL B CG1   
2855  C  CG2   . VAL B 13  ? 0.3043 0.2539 0.3178 -0.0125 -0.1015 0.0594  12  VAL B CG2   
2865  N  N     . ASP B 14  ? 0.3335 0.2989 0.3830 0.0102  -0.1018 0.0452  13  ASP B N     
2866  C  CA    . ASP B 14  ? 0.3470 0.3171 0.4080 0.0147  -0.1048 0.0437  13  ASP B CA    
2867  C  C     . ASP B 14  ? 0.3840 0.3487 0.4603 0.0196  -0.1137 0.0461  13  ASP B C     
2868  O  O     . ASP B 14  ? 0.3721 0.3375 0.4564 0.0196  -0.1218 0.0505  13  ASP B O     
2869  C  CB    . ASP B 14  ? 0.4054 0.3794 0.4589 0.0082  -0.1076 0.0482  13  ASP B CB    
2870  C  CG    . ASP B 14  ? 0.4101 0.3901 0.4526 0.0053  -0.0977 0.0437  13  ASP B CG    
2871  O  OD1   . ASP B 14  ? 0.3894 0.3722 0.4341 0.0103  -0.0892 0.0368  13  ASP B OD1   
2872  O  OD2   . ASP B 14  ? 0.3954 0.3768 0.4269 -0.0021 -0.0985 0.0471  13  ASP B OD2   
2877  N  N     . GLY B 15  ? 0.3248 0.2838 0.4054 0.0234  -0.1126 0.0433  14  GLY B N     
2878  C  CA    . GLY B 15  ? 0.3389 0.2919 0.4351 0.0290  -0.1193 0.0436  14  GLY B CA    
2879  C  C     . GLY B 15  ? 0.4092 0.3528 0.5049 0.0247  -0.1297 0.0526  14  GLY B C     
2880  O  O     . GLY B 15  ? 0.3586 0.2950 0.4670 0.0293  -0.1352 0.0529  14  GLY B O     
2884  N  N     . GLU B 16  ? 0.3578 0.3005 0.4391 0.0160  -0.1324 0.0598  15  GLU B N     
2885  C  CA    . GLU B 16  ? 0.3666 0.3007 0.4446 0.0101  -0.1425 0.0697  15  GLU B CA    
2886  C  C     . GLU B 16  ? 0.3500 0.2772 0.4193 0.0068  -0.1400 0.0702  15  GLU B C     
2887  O  O     . GLU B 16  ? 0.3547 0.2859 0.4118 0.0034  -0.1312 0.0669  15  GLU B O     
2888  C  CB    . GLU B 16  ? 0.4202 0.3577 0.4846 0.0010  -0.1456 0.0766  15  GLU B CB    
2889  C  CG    . GLU B 16  ? 0.4929 0.4241 0.5546 -0.0057 -0.1554 0.0861  15  GLU B CG    
2890  C  CD    . GLU B 16  ? 0.5070 0.4434 0.5566 -0.0138 -0.1580 0.0913  15  GLU B CD    
2891  O  OE1   . GLU B 16  ? 0.5213 0.4573 0.5521 -0.0223 -0.1559 0.0945  15  GLU B OE1   
2892  O  OE2   . GLU B 16  ? 0.5541 0.4953 0.6127 -0.0118 -0.1612 0.0913  15  GLU B OE2   
2899  N  N     . PRO B 17  ? 0.3419 0.2593 0.4182 0.0076  -0.1468 0.0737  16  PRO B N     
2900  C  CA    . PRO B 17  ? 0.3492 0.2601 0.4174 0.0038  -0.1448 0.0745  16  PRO B CA    
2901  C  C     . PRO B 17  ? 0.3860 0.2982 0.4349 -0.0071 -0.1430 0.0804  16  PRO B C     
2902  O  O     . PRO B 17  ? 0.3286 0.2398 0.3706 -0.0138 -0.1494 0.0885  16  PRO B O     
2903  C  CB    . PRO B 17  ? 0.3744 0.2754 0.4524 0.0044  -0.1519 0.0774  16  PRO B CB    
2904  C  CG    . PRO B 17  ? 0.4036 0.3076 0.4989 0.0122  -0.1529 0.0726  16  PRO B CG    
2905  C  CD    . PRO B 17  ? 0.3808 0.2948 0.4730 0.0117  -0.1516 0.0732  16  PRO B CD    
2913  N  N     . LEU B 18  ? 0.3440 0.2589 0.3845 -0.0091 -0.1340 0.0760  17  LEU B N     
2914  C  CA    . LEU B 18  ? 0.3556 0.2711 0.3797 -0.0191 -0.1308 0.0803  17  LEU B CA    
2915  C  C     . LEU B 18  ? 0.3204 0.2274 0.3428 -0.0230 -0.1335 0.0839  17  LEU B C     
2916  O  O     . LEU B 18  ? 0.3344 0.2366 0.3474 -0.0319 -0.1383 0.0922  17  LEU B O     
2917  C  CB    . LEU B 18  ? 0.3210 0.2464 0.3383 -0.0188 -0.1186 0.0730  17  LEU B CB    
2918  C  CG    . LEU B 18  ? 0.3641 0.2917 0.3659 -0.0286 -0.1133 0.0759  17  LEU B CG    
2919  C  CD1   . LEU B 18  ? 0.3752 0.3020 0.3653 -0.0376 -0.1179 0.0835  17  LEU B CD1   
2920  C  CD2   . LEU B 18  ? 0.3597 0.2969 0.3584 -0.0267 -0.1012 0.0682  17  LEU B CD2   
2932  N  N     . GLY B 19  ? 0.3490 0.2536 0.3796 -0.0173 -0.1308 0.0781  18  GLY B N     
2933  C  CA    . GLY B 19  ? 0.3021 0.1983 0.3323 -0.0209 -0.1338 0.0811  18  GLY B CA    
2934  C  C     . GLY B 19  ? 0.3536 0.2516 0.3885 -0.0161 -0.1271 0.0728  18  GLY B C     
2935  O  O     . GLY B 19  ? 0.3501 0.2556 0.3878 -0.0103 -0.1203 0.0651  18  GLY B O     
2939  N  N     . ARG B 20  ? 0.3350 0.2255 0.3700 -0.0194 -0.1298 0.0750  19  ARG B N     
2940  C  CA    . ARG B 20  ? 0.3921 0.2826 0.4317 -0.0159 -0.1254 0.0679  19  ARG B CA    
2941  C  C     . ARG B 20  ? 0.3757 0.2721 0.4060 -0.0226 -0.1187 0.0684  19  ARG B C     
2942  O  O     . ARG B 20  ? 0.3912 0.2849 0.4140 -0.0312 -0.1207 0.0754  19  ARG B O     
2943  C  CB    . ARG B 20  ? 0.3974 0.2749 0.4451 -0.0148 -0.1330 0.0692  19  ARG B CB    
2944  C  CG    . ARG B 20  ? 0.4079 0.2844 0.4587 -0.0128 -0.1294 0.0624  19  ARG B CG    
2945  C  CD    . ARG B 20  ? 0.4010 0.2641 0.4618 -0.0097 -0.1366 0.0616  19  ARG B CD    
2946  N  NE    . ARG B 20  ? 0.4248 0.2866 0.4965 -0.0005 -0.1378 0.0563  19  ARG B NE    
2947  C  CZ    . ARG B 20  ? 0.4437 0.2956 0.5266 0.0047  -0.1417 0.0521  19  ARG B CZ    
2948  N  NH1   . ARG B 20  ? 0.4407 0.2827 0.5247 0.0017  -0.1448 0.0523  19  ARG B NH1   
2949  N  NH2   . ARG B 20  ? 0.4342 0.2863 0.5279 0.0129  -0.1421 0.0473  19  ARG B NH2   
2963  N  N     . VAL B 21  ? 0.3336 0.2377 0.3652 -0.0188 -0.1112 0.0610  20  VAL B N     
2964  C  CA    . VAL B 21  ? 0.3234 0.2330 0.3503 -0.0239 -0.1055 0.0607  20  VAL B CA    
2965  C  C     . VAL B 21  ? 0.2978 0.2043 0.3313 -0.0205 -0.1060 0.0555  20  VAL B C     
2966  O  O     . VAL B 21  ? 0.3323 0.2378 0.3719 -0.0130 -0.1060 0.0491  20  VAL B O     
2967  C  CB    . VAL B 21  ? 0.3644 0.2866 0.3868 -0.0235 -0.0963 0.0577  20  VAL B CB    
2968  C  CG1   . VAL B 21  ? 0.3612 0.2875 0.3885 -0.0150 -0.0935 0.0509  20  VAL B CG1   
2969  C  CG2   . VAL B 21  ? 0.3541 0.2825 0.3753 -0.0274 -0.0905 0.0567  20  VAL B CG2   
2979  N  N     . SER B 22  ? 0.3240 0.2285 0.3560 -0.0265 -0.1066 0.0580  21  SER B N     
2980  C  CA    . SER B 22  ? 0.3670 0.2691 0.4039 -0.0247 -0.1071 0.0532  21  SER B CA    
2981  C  C     . SER B 22  ? 0.3381 0.2504 0.3728 -0.0285 -0.1008 0.0524  21  SER B C     
2982  O  O     . SER B 22  ? 0.3317 0.2502 0.3616 -0.0343 -0.0970 0.0568  21  SER B O     
2983  C  CB    . SER B 22  ? 0.3654 0.2543 0.4047 -0.0284 -0.1150 0.0569  21  SER B CB    
2984  O  OG    . SER B 22  ? 0.4063 0.2962 0.4403 -0.0376 -0.1149 0.0636  21  SER B OG    
2990  N  N     . PHE B 23  ? 0.3228 0.2369 0.3615 -0.0255 -0.0997 0.0467  22  PHE B N     
2991  C  CA    . PHE B 23  ? 0.3239 0.2485 0.3630 -0.0276 -0.0944 0.0453  22  PHE B CA    
2992  C  C     . PHE B 23  ? 0.2977 0.2181 0.3399 -0.0304 -0.0981 0.0439  22  PHE B C     
2993  O  O     . PHE B 23  ? 0.3392 0.2510 0.3836 -0.0270 -0.1024 0.0396  22  PHE B O     
2994  C  CB    . PHE B 23  ? 0.2704 0.2036 0.3106 -0.0210 -0.0892 0.0395  22  PHE B CB    
2995  C  CG    . PHE B 23  ? 0.2315 0.1681 0.2692 -0.0173 -0.0858 0.0394  22  PHE B CG    
2996  C  CD1   . PHE B 23  ? 0.2952 0.2408 0.3301 -0.0197 -0.0798 0.0419  22  PHE B CD1   
2997  C  CD2   . PHE B 23  ? 0.2981 0.2294 0.3369 -0.0114 -0.0882 0.0363  22  PHE B CD2   
2998  C  CE1   . PHE B 23  ? 0.2920 0.2403 0.3241 -0.0167 -0.0768 0.0415  22  PHE B CE1   
2999  C  CE2   . PHE B 23  ? 0.3115 0.2465 0.3485 -0.0084 -0.0854 0.0363  22  PHE B CE2   
3000  C  CZ    . PHE B 23  ? 0.2967 0.2399 0.3297 -0.0113 -0.0799 0.0389  22  PHE B CZ    
3010  N  N     . GLU B 24  ? 0.2842 0.2108 0.3271 -0.0366 -0.0962 0.0469  23  GLU B N     
3011  C  CA    . GLU B 24  ? 0.3498 0.2764 0.3963 -0.0389 -0.0985 0.0447  23  GLU B CA    
3012  C  C     . GLU B 24  ? 0.3318 0.2698 0.3806 -0.0346 -0.0939 0.0402  23  GLU B C     
3013  O  O     . GLU B 24  ? 0.3061 0.2547 0.3554 -0.0337 -0.0879 0.0414  23  GLU B O     
3014  C  CB    . GLU B 24  ? 0.3698 0.2984 0.4176 -0.0480 -0.0990 0.0504  23  GLU B CB    
3015  C  CG    . GLU B 24  ? 0.4100 0.3417 0.4623 -0.0508 -0.1007 0.0484  23  GLU B CG    
3016  C  CD    . GLU B 24  ? 0.4591 0.3913 0.5135 -0.0602 -0.1021 0.0538  23  GLU B CD    
3017  O  OE1   . GLU B 24  ? 0.4969 0.4258 0.5482 -0.0650 -0.1018 0.0593  23  GLU B OE1   
3018  O  OE2   . GLU B 24  ? 0.4249 0.3613 0.4840 -0.0632 -0.1036 0.0527  23  GLU B OE2   
3025  N  N     . LEU B 25  ? 0.3089 0.2439 0.3586 -0.0321 -0.0969 0.0349  24  LEU B N     
3026  C  CA    . LEU B 25  ? 0.2917 0.2361 0.3427 -0.0288 -0.0942 0.0310  24  LEU B CA    
3027  C  C     . LEU B 25  ? 0.3365 0.2850 0.3912 -0.0345 -0.0967 0.0322  24  LEU B C     
3028  O  O     . LEU B 25  ? 0.3334 0.2732 0.3877 -0.0381 -0.1022 0.0310  24  LEU B O     
3029  C  CB    . LEU B 25  ? 0.3312 0.2695 0.3792 -0.0228 -0.0956 0.0241  24  LEU B CB    
3030  C  CG    . LEU B 25  ? 0.3075 0.2405 0.3534 -0.0169 -0.0943 0.0220  24  LEU B CG    
3031  C  CD1   . LEU B 25  ? 0.3691 0.2995 0.4130 -0.0114 -0.0941 0.0145  24  LEU B CD1   
3032  C  CD2   . LEU B 25  ? 0.2869 0.2289 0.3325 -0.0152 -0.0885 0.0256  24  LEU B CD2   
3044  N  N     . PHE B 26  ? 0.2982 0.2599 0.3575 -0.0355 -0.0929 0.0345  25  PHE B N     
3045  C  CA    . PHE B 26  ? 0.3056 0.2735 0.3707 -0.0415 -0.0951 0.0369  25  PHE B CA    
3046  C  C     . PHE B 26  ? 0.3206 0.2893 0.3852 -0.0407 -0.0992 0.0327  25  PHE B C     
3047  O  O     . PHE B 26  ? 0.2955 0.2753 0.3646 -0.0403 -0.0981 0.0335  25  PHE B O     
3048  C  CB    . PHE B 26  ? 0.3107 0.2927 0.3828 -0.0427 -0.0891 0.0411  25  PHE B CB    
3049  C  CG    . PHE B 26  ? 0.3315 0.3131 0.4025 -0.0450 -0.0845 0.0450  25  PHE B CG    
3050  C  CD1   . PHE B 26  ? 0.3701 0.3419 0.4376 -0.0503 -0.0877 0.0476  25  PHE B CD1   
3051  C  CD2   . PHE B 26  ? 0.3101 0.3008 0.3832 -0.0424 -0.0771 0.0461  25  PHE B CD2   
3052  C  CE1   . PHE B 26  ? 0.3558 0.3275 0.4209 -0.0533 -0.0838 0.0516  25  PHE B CE1   
3053  C  CE2   . PHE B 26  ? 0.3280 0.3184 0.3986 -0.0456 -0.0727 0.0493  25  PHE B CE2   
3054  C  CZ    . PHE B 26  ? 0.3160 0.2972 0.3821 -0.0511 -0.0762 0.0521  25  PHE B CZ    
3064  N  N     . ALA B 27  ? 0.3542 0.3105 0.4130 -0.0405 -0.1039 0.0280  26  ALA B N     
3065  C  CA    . ALA B 27  ? 0.3343 0.2900 0.3901 -0.0403 -0.1076 0.0232  26  ALA B CA    
3066  C  C     . ALA B 27  ? 0.3571 0.3194 0.4181 -0.0472 -0.1117 0.0259  26  ALA B C     
3067  O  O     . ALA B 27  ? 0.3656 0.3318 0.4250 -0.0479 -0.1146 0.0236  26  ALA B O     
3068  C  CB    . ALA B 27  ? 0.3503 0.2907 0.3994 -0.0395 -0.1113 0.0169  26  ALA B CB    
3074  N  N     . ASP B 28  ? 0.3342 0.2978 0.4010 -0.0530 -0.1122 0.0310  27  ASP B N     
3075  C  CA    . ASP B 28  ? 0.3969 0.3681 0.4707 -0.0600 -0.1158 0.0342  27  ASP B CA    
3076  C  C     . ASP B 28  ? 0.3802 0.3683 0.4620 -0.0584 -0.1129 0.0374  27  ASP B C     
3077  O  O     . ASP B 28  ? 0.3832 0.3786 0.4702 -0.0624 -0.1170 0.0386  27  ASP B O     
3078  C  CB    . ASP B 28  ? 0.4249 0.3943 0.5034 -0.0664 -0.1157 0.0392  27  ASP B CB    
3079  C  CG    . ASP B 28  ? 0.4504 0.4256 0.5318 -0.0644 -0.1085 0.0434  27  ASP B CG    
3080  O  OD1   . ASP B 28  ? 0.4246 0.3980 0.5013 -0.0576 -0.1047 0.0414  27  ASP B OD1   
3081  O  OD2   . ASP B 28  ? 0.5155 0.4971 0.6036 -0.0700 -0.1064 0.0485  27  ASP B OD2   
3086  N  N     . LYS B 29  ? 0.3288 0.3232 0.4126 -0.0528 -0.1061 0.0389  28  LYS B N     
3087  C  CA    . LYS B 29  ? 0.3342 0.3437 0.4269 -0.0505 -0.1027 0.0418  28  LYS B CA    
3088  C  C     . LYS B 29  ? 0.2890 0.2999 0.3768 -0.0432 -0.1011 0.0388  28  LYS B C     
3089  O  O     . LYS B 29  ? 0.2768 0.2977 0.3704 -0.0423 -0.1021 0.0406  28  LYS B O     
3090  C  CB    . LYS B 29  ? 0.3785 0.3957 0.4791 -0.0506 -0.0953 0.0461  28  LYS B CB    
3091  C  CG    . LYS B 29  ? 0.4131 0.4355 0.5229 -0.0584 -0.0953 0.0505  28  LYS B CG    
3092  C  CD    . LYS B 29  ? 0.5277 0.5555 0.6445 -0.0638 -0.1021 0.0518  28  LYS B CD    
3093  C  CE    . LYS B 29  ? 0.5796 0.6254 0.7131 -0.0645 -0.0994 0.0561  28  LYS B CE    
3094  N  NZ    . LYS B 29  ? 0.6358 0.6870 0.7779 -0.0721 -0.1058 0.0586  28  LYS B NZ    
3108  N  N     . VAL B 30  ? 0.3093 0.3107 0.3873 -0.0383 -0.0988 0.0348  29  VAL B N     
3109  C  CA    . VAL B 30  ? 0.3008 0.3028 0.3733 -0.0321 -0.0973 0.0316  29  VAL B CA    
3110  C  C     . VAL B 30  ? 0.2708 0.2597 0.3315 -0.0307 -0.1001 0.0252  29  VAL B C     
3111  O  O     . VAL B 30  ? 0.2929 0.2759 0.3486 -0.0259 -0.0966 0.0224  29  VAL B O     
3112  C  CB    . VAL B 30  ? 0.2685 0.2746 0.3425 -0.0264 -0.0897 0.0327  29  VAL B CB    
3113  C  CG1   . VAL B 30  ? 0.2792 0.2989 0.3643 -0.0257 -0.0864 0.0372  29  VAL B CG1   
3114  C  CG2   . VAL B 30  ? 0.2801 0.2805 0.3532 -0.0274 -0.0866 0.0336  29  VAL B CG2   
3124  N  N     . PRO B 31  ? 0.2918 0.2761 0.3482 -0.0346 -0.1063 0.0222  30  PRO B N     
3125  C  CA    . PRO B 31  ? 0.2887 0.2595 0.3350 -0.0337 -0.1082 0.0152  30  PRO B CA    
3126  C  C     . PRO B 31  ? 0.2621 0.2313 0.3009 -0.0274 -0.1047 0.0105  30  PRO B C     
3127  O  O     . PRO B 31  ? 0.2952 0.2545 0.3290 -0.0242 -0.1031 0.0054  30  PRO B O     
3128  C  CB    . PRO B 31  ? 0.2993 0.2679 0.3428 -0.0402 -0.1152 0.0132  30  PRO B CB    
3129  C  CG    . PRO B 31  ? 0.3785 0.3617 0.4296 -0.0427 -0.1169 0.0192  30  PRO B CG    
3130  C  CD    . PRO B 31  ? 0.3343 0.3248 0.3958 -0.0410 -0.1118 0.0251  30  PRO B CD    
3138  N  N     . LYS B 32  ? 0.2813 0.2600 0.3199 -0.0258 -0.1038 0.0121  31  LYS B N     
3139  C  CA    . LYS B 32  ? 0.2808 0.2579 0.3114 -0.0208 -0.1006 0.0076  31  LYS B CA    
3140  C  C     . LYS B 32  ? 0.2707 0.2474 0.3036 -0.0147 -0.0941 0.0080  31  LYS B C     
3141  O  O     . LYS B 32  ? 0.2492 0.2189 0.2764 -0.0109 -0.0916 0.0027  31  LYS B O     
3142  C  CB    . LYS B 32  ? 0.2900 0.2772 0.3201 -0.0211 -0.1017 0.0105  31  LYS B CB    
3143  C  CG    . LYS B 32  ? 0.3457 0.3309 0.3658 -0.0175 -0.0990 0.0059  31  LYS B CG    
3144  C  CD    . LYS B 32  ? 0.3759 0.3691 0.3930 -0.0197 -0.1023 0.0089  31  LYS B CD    
3145  C  CE    . LYS B 32  ? 0.3862 0.3763 0.3916 -0.0171 -0.0993 0.0039  31  LYS B CE    
3146  N  NZ    . LYS B 32  ? 0.4203 0.4172 0.4213 -0.0198 -0.1030 0.0074  31  LYS B NZ    
3160  N  N     . THR B 33  ? 0.2663 0.2507 0.3077 -0.0140 -0.0912 0.0140  32  THR B N     
3161  C  CA    . THR B 33  ? 0.2375 0.2222 0.2808 -0.0093 -0.0853 0.0149  32  THR B CA    
3162  C  C     . THR B 33  ? 0.2529 0.2273 0.2948 -0.0094 -0.0857 0.0130  32  THR B C     
3163  O  O     . THR B 33  ? 0.2485 0.2183 0.2875 -0.0051 -0.0829 0.0101  32  THR B O     
3164  C  CB    . THR B 33  ? 0.2297 0.2250 0.2824 -0.0098 -0.0821 0.0213  32  THR B CB    
3165  O  OG1   . THR B 33  ? 0.2362 0.2407 0.2922 -0.0100 -0.0832 0.0238  32  THR B OG1   
3166  C  CG2   . THR B 33  ? 0.1964 0.1928 0.2497 -0.0053 -0.0755 0.0219  32  THR B CG2   
3174  N  N     . ALA B 34  ? 0.2725 0.2431 0.3170 -0.0145 -0.0897 0.0147  33  ALA B N     
3175  C  CA    . ALA B 34  ? 0.2501 0.2096 0.2935 -0.0151 -0.0913 0.0134  33  ALA B CA    
3176  C  C     . ALA B 34  ? 0.2887 0.2380 0.3262 -0.0119 -0.0926 0.0061  33  ALA B C     
3177  O  O     . ALA B 34  ? 0.3017 0.2443 0.3390 -0.0085 -0.0915 0.0045  33  ALA B O     
3178  C  CB    . ALA B 34  ? 0.2979 0.2548 0.3449 -0.0220 -0.0959 0.0166  33  ALA B CB    
3184  N  N     . GLU B 35  ? 0.2899 0.2379 0.3226 -0.0131 -0.0950 0.0014  34  GLU B N     
3185  C  CA    . GLU B 35  ? 0.3007 0.2386 0.3280 -0.0108 -0.0955 -0.0067 34  GLU B CA    
3186  C  C     . GLU B 35  ? 0.3003 0.2402 0.3253 -0.0042 -0.0901 -0.0099 34  GLU B C     
3187  O  O     . GLU B 35  ? 0.3173 0.2493 0.3420 -0.0007 -0.0890 -0.0149 34  GLU B O     
3188  C  CB    . GLU B 35  ? 0.3216 0.2582 0.3427 -0.0149 -0.0989 -0.0112 34  GLU B CB    
3189  C  CG    . GLU B 35  ? 0.3772 0.3056 0.3909 -0.0127 -0.0977 -0.0208 34  GLU B CG    
3190  C  CD    . GLU B 35  ? 0.4027 0.3176 0.4190 -0.0115 -0.0988 -0.0254 34  GLU B CD    
3191  O  OE1   . GLU B 35  ? 0.3853 0.2962 0.4072 -0.0141 -0.1021 -0.0209 34  GLU B OE1   
3192  O  OE2   . GLU B 35  ? 0.4276 0.3360 0.4410 -0.0079 -0.0961 -0.0333 34  GLU B OE2   
3199  N  N     . ASN B 36  ? 0.2914 0.2419 0.3159 -0.0026 -0.0868 -0.0069 35  ASN B N     
3200  C  CA    . ASN B 36  ? 0.2483 0.2016 0.2716 0.0032  -0.0815 -0.0087 35  ASN B CA    
3201  C  C     . ASN B 36  ? 0.3049 0.2543 0.3330 0.0063  -0.0799 -0.0072 35  ASN B C     
3202  O  O     . ASN B 36  ? 0.2726 0.2174 0.3005 0.0105  -0.0779 -0.0118 35  ASN B O     
3203  C  CB    . ASN B 36  ? 0.2436 0.2084 0.2674 0.0037  -0.0787 -0.0039 35  ASN B CB    
3204  C  CG    . ASN B 36  ? 0.2600 0.2280 0.2822 0.0089  -0.0733 -0.0055 35  ASN B CG    
3205  O  OD1   . ASN B 36  ? 0.2451 0.2102 0.2619 0.0110  -0.0716 -0.0113 35  ASN B OD1   
3206  N  ND2   . ASN B 36  ? 0.2772 0.2512 0.3040 0.0107  -0.0700 -0.0005 35  ASN B ND2   
3213  N  N     . PHE B 37  ? 0.2722 0.2241 0.3051 0.0040  -0.0806 -0.0007 36  PHE B N     
3214  C  CA    . PHE B 37  ? 0.2742 0.2233 0.3104 0.0061  -0.0794 0.0018  36  PHE B CA    
3215  C  C     . PHE B 37  ? 0.2621 0.1990 0.2996 0.0065  -0.0833 -0.0013 36  PHE B C     
3216  O  O     . PHE B 37  ? 0.2799 0.2132 0.3195 0.0105  -0.0825 -0.0027 36  PHE B O     
3217  C  CB    . PHE B 37  ? 0.2434 0.1976 0.2827 0.0024  -0.0790 0.0091  36  PHE B CB    
3218  C  CG    . PHE B 37  ? 0.2333 0.1865 0.2739 0.0036  -0.0773 0.0123  36  PHE B CG    
3219  C  CD1   . PHE B 37  ? 0.2214 0.1817 0.2615 0.0065  -0.0721 0.0132  36  PHE B CD1   
3220  C  CD2   . PHE B 37  ? 0.2491 0.1939 0.2910 0.0014  -0.0813 0.0145  36  PHE B CD2   
3221  C  CE1   . PHE B 37  ? 0.2664 0.2258 0.3066 0.0067  -0.0709 0.0161  36  PHE B CE1   
3222  C  CE2   . PHE B 37  ? 0.3007 0.2445 0.3427 0.0017  -0.0805 0.0181  36  PHE B CE2   
3223  C  CZ    . PHE B 37  ? 0.2383 0.1898 0.2791 0.0042  -0.0752 0.0187  36  PHE B CZ    
3233  N  N     . ARG B 38  ? 0.2877 0.2184 0.3250 0.0025  -0.0878 -0.0025 37  ARG B N     
3234  C  CA    . ARG B 38  ? 0.3575 0.2755 0.3969 0.0029  -0.0917 -0.0060 37  ARG B CA    
3235  C  C     . ARG B 38  ? 0.3492 0.2631 0.3880 0.0085  -0.0893 -0.0141 37  ARG B C     
3236  O  O     . ARG B 38  ? 0.3519 0.2597 0.3955 0.0123  -0.0897 -0.0155 37  ARG B O     
3237  C  CB    . ARG B 38  ? 0.3634 0.2757 0.4015 -0.0028 -0.0963 -0.0072 37  ARG B CB    
3238  C  CG    . ARG B 38  ? 0.3581 0.2557 0.3996 -0.0034 -0.1009 -0.0097 37  ARG B CG    
3239  C  CD    . ARG B 38  ? 0.4341 0.3243 0.4729 -0.0082 -0.1048 -0.0144 37  ARG B CD    
3240  N  NE    . ARG B 38  ? 0.4356 0.3269 0.4686 -0.0066 -0.1022 -0.0228 37  ARG B NE    
3241  C  CZ    . ARG B 38  ? 0.4377 0.3233 0.4706 -0.0016 -0.0996 -0.0308 37  ARG B CZ    
3242  N  NH1   . ARG B 38  ? 0.4064 0.2835 0.4464 0.0026  -0.1001 -0.0318 37  ARG B NH1   
3243  N  NH2   . ARG B 38  ? 0.4877 0.3762 0.5136 -0.0011 -0.0964 -0.0377 37  ARG B NH2   
3257  N  N     . ALA B 39  ? 0.3354 0.2526 0.3686 0.0086  -0.0870 -0.0197 38  ALA B N     
3258  C  CA    . ALA B 39  ? 0.3216 0.2355 0.3535 0.0131  -0.0838 -0.0283 38  ALA B CA    
3259  C  C     . ALA B 39  ? 0.3417 0.2608 0.3769 0.0188  -0.0794 -0.0276 38  ALA B C     
3260  O  O     . ALA B 39  ? 0.3381 0.2525 0.3774 0.0233  -0.0778 -0.0329 38  ALA B O     
3261  C  CB    . ALA B 39  ? 0.3178 0.2356 0.3409 0.0109  -0.0820 -0.0332 38  ALA B CB    
3267  N  N     . LEU B 40  ? 0.3191 0.2481 0.3532 0.0186  -0.0772 -0.0214 39  LEU B N     
3268  C  CA    . LEU B 40  ? 0.2384 0.1721 0.2752 0.0234  -0.0732 -0.0209 39  LEU B CA    
3269  C  C     . LEU B 40  ? 0.2624 0.1904 0.3066 0.0252  -0.0760 -0.0179 39  LEU B C     
3270  O  O     . LEU B 40  ? 0.3023 0.2301 0.3509 0.0297  -0.0742 -0.0202 39  LEU B O     
3271  C  CB    . LEU B 40  ? 0.2870 0.2315 0.3210 0.0224  -0.0702 -0.0154 39  LEU B CB    
3272  C  CG    . LEU B 40  ? 0.3030 0.2535 0.3304 0.0214  -0.0677 -0.0177 39  LEU B CG    
3273  C  CD1   . LEU B 40  ? 0.2647 0.2245 0.2917 0.0199  -0.0659 -0.0112 39  LEU B CD1   
3274  C  CD2   . LEU B 40  ? 0.2808 0.2320 0.3058 0.0254  -0.0632 -0.0244 39  LEU B CD2   
3286  N  N     . SER B 41  ? 0.2846 0.2076 0.3305 0.0213  -0.0809 -0.0129 40  SER B N     
3287  C  CA    . SER B 41  ? 0.3230 0.2395 0.3751 0.0221  -0.0847 -0.0091 40  SER B CA    
3288  C  C     . SER B 41  ? 0.3510 0.2569 0.4095 0.0256  -0.0872 -0.0151 40  SER B C     
3289  O  O     . SER B 41  ? 0.3612 0.2642 0.4267 0.0292  -0.0886 -0.0142 40  SER B O     
3290  C  CB    . SER B 41  ? 0.3249 0.2392 0.3760 0.0159  -0.0889 -0.0016 40  SER B CB    
3291  O  OG    . SER B 41  ? 0.3123 0.2370 0.3594 0.0132  -0.0857 0.0036  40  SER B OG    
3297  N  N     . THR B 42  ? 0.3749 0.2754 0.4316 0.0247  -0.0874 -0.0217 41  THR B N     
3298  C  CA    . THR B 42  ? 0.3949 0.2849 0.4583 0.0283  -0.0887 -0.0288 41  THR B CA    
3299  C  C     . THR B 42  ? 0.4014 0.2950 0.4671 0.0341  -0.0829 -0.0368 41  THR B C     
3300  O  O     . THR B 42  ? 0.4533 0.3397 0.5277 0.0384  -0.0831 -0.0423 41  THR B O     
3301  C  CB    . THR B 42  ? 0.4266 0.3082 0.4867 0.0247  -0.0907 -0.0341 41  THR B CB    
3302  O  OG1   . THR B 42  ? 0.4192 0.3076 0.4700 0.0232  -0.0861 -0.0393 41  THR B OG1   
3303  C  CG2   . THR B 42  ? 0.3890 0.2666 0.4476 0.0183  -0.0964 -0.0267 41  THR B CG2   
3311  N  N     . GLY B 43  ? 0.3516 0.2557 0.4101 0.0342  -0.0775 -0.0379 42  GLY B N     
3312  C  CA    . GLY B 43  ? 0.3776 0.2854 0.4365 0.0385  -0.0715 -0.0458 42  GLY B CA    
3313  C  C     . GLY B 43  ? 0.3890 0.2910 0.4441 0.0378  -0.0692 -0.0560 42  GLY B C     
3314  O  O     . GLY B 43  ? 0.4539 0.3576 0.5102 0.0412  -0.0637 -0.0638 42  GLY B O     
3318  N  N     . GLU B 44  ? 0.4104 0.3062 0.4605 0.0329  -0.0729 -0.0562 43  GLU B N     
3319  C  CA    . GLU B 44  ? 0.4732 0.3610 0.5203 0.0317  -0.0714 -0.0666 43  GLU B CA    
3320  C  C     . GLU B 44  ? 0.5212 0.4157 0.5570 0.0302  -0.0654 -0.0729 43  GLU B C     
3321  O  O     . GLU B 44  ? 0.4926 0.3815 0.5254 0.0299  -0.0622 -0.0832 43  GLU B O     
3322  C  CB    . GLU B 44  ? 0.5157 0.3954 0.5595 0.0259  -0.0774 -0.0647 43  GLU B CB    
3323  C  CG    . GLU B 44  ? 0.4762 0.3633 0.5092 0.0196  -0.0792 -0.0592 43  GLU B CG    
3324  C  CD    . GLU B 44  ? 0.5280 0.4081 0.5609 0.0140  -0.0858 -0.0552 43  GLU B CD    
3325  O  OE1   . GLU B 44  ? 0.4727 0.3497 0.5131 0.0143  -0.0898 -0.0482 43  GLU B OE1   
3326  O  OE2   . GLU B 44  ? 0.5472 0.4249 0.5722 0.0088  -0.0872 -0.0590 43  GLU B OE2   
3333  N  N     . LYS B 45  ? 0.4192 0.3250 0.4483 0.0290  -0.0637 -0.0674 44  LYS B N     
3334  C  CA    . LYS B 45  ? 0.4312 0.3431 0.4493 0.0273  -0.0585 -0.0722 44  LYS B CA    
3335  C  C     . LYS B 45  ? 0.4720 0.3887 0.4938 0.0325  -0.0517 -0.0767 44  LYS B C     
3336  O  O     . LYS B 45  ? 0.5253 0.4478 0.5380 0.0311  -0.0468 -0.0802 44  LYS B O     
3337  C  CB    . LYS B 45  ? 0.4100 0.3314 0.4199 0.0233  -0.0602 -0.0639 44  LYS B CB    
3338  C  CG    . LYS B 45  ? 0.4065 0.3255 0.4146 0.0181  -0.0669 -0.0581 44  LYS B CG    
3339  C  CD    . LYS B 45  ? 0.4516 0.3639 0.4513 0.0127  -0.0689 -0.0648 44  LYS B CD    
3340  C  CE    . LYS B 45  ? 0.4877 0.4010 0.4847 0.0067  -0.0754 -0.0580 44  LYS B CE    
3341  N  NZ    . LYS B 45  ? 0.5588 0.4644 0.5480 0.0008  -0.0784 -0.0644 44  LYS B NZ    
3355  N  N     . GLY B 46  ? 0.4396 0.3545 0.4749 0.0381  -0.0516 -0.0762 45  GLY B N     
3356  C  CA    . GLY B 46  ? 0.4710 0.3914 0.5122 0.0432  -0.0457 -0.0796 45  GLY B CA    
3357  C  C     . GLY B 46  ? 0.4477 0.3779 0.4908 0.0449  -0.0454 -0.0709 45  GLY B C     
3358  O  O     . GLY B 46  ? 0.3994 0.3354 0.4468 0.0485  -0.0405 -0.0733 45  GLY B O     
3362  N  N     . PHE B 47  ? 0.3992 0.3316 0.4393 0.0420  -0.0502 -0.0615 46  PHE B N     
3363  C  CA    . PHE B 47  ? 0.3804 0.3212 0.4216 0.0429  -0.0498 -0.0534 46  PHE B CA    
3364  C  C     . PHE B 47  ? 0.3718 0.3109 0.4138 0.0401  -0.0559 -0.0446 46  PHE B C     
3365  O  O     . PHE B 47  ? 0.3408 0.2740 0.3805 0.0368  -0.0599 -0.0443 46  PHE B O     
3366  C  CB    . PHE B 47  ? 0.3815 0.3311 0.4126 0.0410  -0.0452 -0.0528 46  PHE B CB    
3367  C  CG    . PHE B 47  ? 0.4071 0.3564 0.4271 0.0357  -0.0469 -0.0524 46  PHE B CG    
3368  C  CD1   . PHE B 47  ? 0.3698 0.3218 0.3874 0.0325  -0.0508 -0.0442 46  PHE B CD1   
3369  C  CD2   . PHE B 47  ? 0.4340 0.3806 0.4461 0.0336  -0.0445 -0.0603 46  PHE B CD2   
3370  C  CE1   . PHE B 47  ? 0.3834 0.3360 0.3925 0.0276  -0.0531 -0.0432 46  PHE B CE1   
3371  C  CE2   . PHE B 47  ? 0.4274 0.3741 0.4288 0.0280  -0.0470 -0.0593 46  PHE B CE2   
3372  C  CZ    . PHE B 47  ? 0.4261 0.3760 0.4267 0.0252  -0.0517 -0.0504 46  PHE B CZ    
3382  N  N     . GLY B 48  ? 0.3432 0.2875 0.3884 0.0410  -0.0563 -0.0376 47  GLY B N     
3383  C  CA    . GLY B 48  ? 0.3118 0.2550 0.3567 0.0376  -0.0610 -0.0296 47  GLY B CA    
3384  C  C     . GLY B 48  ? 0.2804 0.2267 0.3303 0.0390  -0.0617 -0.0235 47  GLY B C     
3385  O  O     . GLY B 48  ? 0.2679 0.2191 0.3201 0.0421  -0.0583 -0.0248 47  GLY B O     
3389  N  N     . TYR B 49  ? 0.3037 0.2469 0.3546 0.0358  -0.0664 -0.0170 48  TYR B N     
3390  C  CA    . TYR B 49  ? 0.2717 0.2184 0.3238 0.0349  -0.0670 -0.0102 48  TYR B CA    
3391  C  C     . TYR B 49  ? 0.3090 0.2529 0.3689 0.0382  -0.0694 -0.0099 48  TYR B C     
3392  O  O     . TYR B 49  ? 0.2508 0.1993 0.3108 0.0381  -0.0686 -0.0060 48  TYR B O     
3393  C  CB    . TYR B 49  ? 0.2559 0.2001 0.3057 0.0296  -0.0709 -0.0036 48  TYR B CB    
3394  C  CG    . TYR B 49  ? 0.2226 0.1722 0.2667 0.0262  -0.0685 -0.0020 48  TYR B CG    
3395  C  CD1   . TYR B 49  ? 0.2571 0.2155 0.2978 0.0270  -0.0632 -0.0020 48  TYR B CD1   
3396  C  CD2   . TYR B 49  ? 0.2103 0.1562 0.2533 0.0220  -0.0720 -0.0003 48  TYR B CD2   
3397  C  CE1   . TYR B 49  ? 0.2296 0.1931 0.2671 0.0242  -0.0616 0.0000  48  TYR B CE1   
3398  C  CE2   . TYR B 49  ? 0.2550 0.2067 0.2946 0.0190  -0.0703 0.0014  48  TYR B CE2   
3399  C  CZ    . TYR B 49  ? 0.2211 0.1818 0.2585 0.0203  -0.0652 0.0017  48  TYR B CZ    
3400  O  OH    . TYR B 49  ? 0.2357 0.2021 0.2717 0.0175  -0.0642 0.0040  48  TYR B OH    
3410  N  N     . LYS B 50  ? 0.2816 0.2177 0.3486 0.0409  -0.0726 -0.0137 49  LYS B N     
3411  C  CA    . LYS B 50  ? 0.2837 0.2170 0.3603 0.0439  -0.0762 -0.0121 49  LYS B CA    
3412  C  C     . LYS B 50  ? 0.2707 0.2126 0.3495 0.0472  -0.0718 -0.0136 49  LYS B C     
3413  O  O     . LYS B 50  ? 0.3140 0.2602 0.3922 0.0499  -0.0662 -0.0202 49  LYS B O     
3414  C  CB    . LYS B 50  ? 0.3173 0.2416 0.4031 0.0475  -0.0787 -0.0179 49  LYS B CB    
3415  C  CG    . LYS B 50  ? 0.3842 0.3057 0.4829 0.0517  -0.0827 -0.0168 49  LYS B CG    
3416  C  CD    . LYS B 50  ? 0.4079 0.3188 0.5173 0.0550  -0.0858 -0.0218 49  LYS B CD    
3417  C  CE    . LYS B 50  ? 0.4652 0.3709 0.5873 0.0573  -0.0933 -0.0164 49  LYS B CE    
3418  N  NZ    . LYS B 50  ? 0.5195 0.4153 0.6554 0.0620  -0.0956 -0.0222 49  LYS B NZ    
3432  N  N     . GLY B 51  ? 0.2799 0.2241 0.3606 0.0462  -0.0746 -0.0074 50  GLY B N     
3433  C  CA    . GLY B 51  ? 0.2775 0.2296 0.3606 0.0486  -0.0712 -0.0084 50  GLY B CA    
3434  C  C     . GLY B 51  ? 0.3048 0.2651 0.3782 0.0458  -0.0660 -0.0064 50  GLY B C     
3435  O  O     . GLY B 51  ? 0.3001 0.2666 0.3750 0.0468  -0.0637 -0.0063 50  GLY B O     
3439  N  N     . SER B 52  ? 0.2465 0.2073 0.3111 0.0424  -0.0638 -0.0053 51  SER B N     
3440  C  CA    . SER B 52  ? 0.2853 0.2531 0.3422 0.0400  -0.0587 -0.0034 51  SER B CA    
3441  C  C     . SER B 52  ? 0.2579 0.2261 0.3112 0.0354  -0.0610 0.0037  51  SER B C     
3442  O  O     . SER B 52  ? 0.2732 0.2360 0.3285 0.0334  -0.0670 0.0078  51  SER B O     
3443  C  CB    . SER B 52  ? 0.2316 0.2003 0.2824 0.0384  -0.0558 -0.0049 51  SER B CB    
3444  O  OG    . SER B 52  ? 0.2611 0.2244 0.3106 0.0352  -0.0600 -0.0019 51  SER B OG    
3450  N  N     . CYS B 53  ? 0.2492 0.2234 0.2970 0.0336  -0.0562 0.0049  52  CYS B N     
3451  C  CA    . CYS B 53  ? 0.2547 0.2301 0.2982 0.0290  -0.0568 0.0102  52  CYS B CA    
3452  C  C     . CYS B 53  ? 0.2486 0.2259 0.2857 0.0249  -0.0534 0.0126  52  CYS B C     
3453  O  O     . CYS B 53  ? 0.2258 0.2052 0.2621 0.0260  -0.0499 0.0104  52  CYS B O     
3454  C  CB    . CYS B 53  ? 0.3164 0.2971 0.3594 0.0297  -0.0537 0.0095  52  CYS B CB    
3455  S  SG    . CYS B 53  ? 0.5530 0.5405 0.5925 0.0311  -0.0451 0.0058  52  CYS B SG    
3461  N  N     . PHE B 54  ? 0.2566 0.2331 0.2893 0.0198  -0.0545 0.0175  53  PHE B N     
3462  C  CA    . PHE B 54  ? 0.2276 0.2074 0.2548 0.0156  -0.0495 0.0193  53  PHE B CA    
3463  C  C     . PHE B 54  ? 0.2508 0.2360 0.2754 0.0158  -0.0436 0.0177  53  PHE B C     
3464  O  O     . PHE B 54  ? 0.2628 0.2481 0.2841 0.0130  -0.0443 0.0195  53  PHE B O     
3465  C  CB    . PHE B 54  ? 0.2072 0.1837 0.2302 0.0091  -0.0526 0.0247  53  PHE B CB    
3466  C  CG    . PHE B 54  ? 0.2441 0.2159 0.2692 0.0079  -0.0568 0.0264  53  PHE B CG    
3467  C  CD1   . PHE B 54  ? 0.2383 0.2034 0.2676 0.0099  -0.0638 0.0268  53  PHE B CD1   
3468  C  CD2   . PHE B 54  ? 0.2458 0.2197 0.2697 0.0048  -0.0537 0.0274  53  PHE B CD2   
3469  C  CE1   . PHE B 54  ? 0.2429 0.2028 0.2740 0.0084  -0.0677 0.0282  53  PHE B CE1   
3470  C  CE2   . PHE B 54  ? 0.2487 0.2184 0.2747 0.0032  -0.0578 0.0290  53  PHE B CE2   
3471  C  CZ    . PHE B 54  ? 0.2260 0.1881 0.2548 0.0048  -0.0649 0.0294  53  PHE B CZ    
3481  N  N     . HIS B 55  ? 0.1856 0.1749 0.2115 0.0187  -0.0383 0.0145  54  HIS B N     
3482  C  CA    . HIS B 55  ? 0.1896 0.1832 0.2140 0.0196  -0.0329 0.0125  54  HIS B CA    
3483  C  C     . HIS B 55  ? 0.2154 0.2113 0.2355 0.0153  -0.0275 0.0140  54  HIS B C     
3484  O  O     . HIS B 55  ? 0.2192 0.2174 0.2371 0.0147  -0.0233 0.0126  54  HIS B O     
3485  C  CB    . HIS B 55  ? 0.2273 0.2237 0.2547 0.0244  -0.0297 0.0089  54  HIS B CB    
3486  C  CG    . HIS B 55  ? 0.2159 0.2138 0.2444 0.0247  -0.0276 0.0092  54  HIS B CG    
3487  N  ND1   . HIS B 55  ? 0.2111 0.2065 0.2415 0.0253  -0.0316 0.0094  54  HIS B ND1   
3488  C  CD2   . HIS B 55  ? 0.2105 0.2120 0.2393 0.0245  -0.0224 0.0095  54  HIS B CD2   
3489  C  CE1   . HIS B 55  ? 0.1937 0.1919 0.2252 0.0252  -0.0293 0.0100  54  HIS B CE1   
3490  N  NE2   . HIS B 55  ? 0.1993 0.2013 0.2306 0.0250  -0.0238 0.0103  54  HIS B NE2   
3498  N  N     . ARG B 56  ? 0.2218 0.2175 0.2415 0.0123  -0.0268 0.0162  55  ARG B N     
3499  C  CA    . ARG B 56  ? 0.1801 0.1787 0.1974 0.0086  -0.0204 0.0167  55  ARG B CA    
3500  C  C     . ARG B 56  ? 0.2255 0.2222 0.2393 0.0025  -0.0218 0.0201  55  ARG B C     
3501  O  O     . ARG B 56  ? 0.2267 0.2223 0.2433 0.0021  -0.0249 0.0220  55  ARG B O     
3502  C  CB    . ARG B 56  ? 0.2089 0.2114 0.2318 0.0115  -0.0157 0.0154  55  ARG B CB    
3503  C  CG    . ARG B 56  ? 0.2081 0.2137 0.2313 0.0079  -0.0088 0.0158  55  ARG B CG    
3504  C  CD    . ARG B 56  ? 0.1928 0.2024 0.2239 0.0116  -0.0057 0.0152  55  ARG B CD    
3505  N  NE    . ARG B 56  ? 0.2101 0.2206 0.2424 0.0158  -0.0031 0.0129  55  ARG B NE    
3506  C  CZ    . ARG B 56  ? 0.2412 0.2539 0.2789 0.0199  -0.0029 0.0128  55  ARG B CZ    
3507  N  NH1   . ARG B 56  ? 0.2111 0.2256 0.2539 0.0205  -0.0054 0.0148  55  ARG B NH1   
3508  N  NH2   . ARG B 56  ? 0.2404 0.2532 0.2781 0.0230  -0.0006 0.0111  55  ARG B NH2   
3522  N  N     . ILE B 57  ? 0.2088 0.2050 0.2158 -0.0029 -0.0197 0.0211  56  ILE B N     
3523  C  CA    . ILE B 57  ? 0.1839 0.1780 0.1854 -0.0099 -0.0210 0.0247  56  ILE B CA    
3524  C  C     . ILE B 57  ? 0.2294 0.2264 0.2259 -0.0149 -0.0125 0.0231  56  ILE B C     
3525  O  O     . ILE B 57  ? 0.2202 0.2170 0.2111 -0.0166 -0.0103 0.0215  56  ILE B O     
3526  C  CB    . ILE B 57  ? 0.2087 0.1975 0.2046 -0.0130 -0.0291 0.0283  56  ILE B CB    
3527  C  CG1   . ILE B 57  ? 0.2370 0.2223 0.2393 -0.0080 -0.0369 0.0292  56  ILE B CG1   
3528  C  CG2   . ILE B 57  ? 0.2388 0.2254 0.2268 -0.0218 -0.0295 0.0324  56  ILE B CG2   
3529  C  CD1   . ILE B 57  ? 0.2616 0.2417 0.2616 -0.0097 -0.0452 0.0327  56  ILE B CD1   
3541  N  N     . ILE B 58  ? 0.1975 0.1973 0.1962 -0.0176 -0.0075 0.0234  57  ILE B N     
3542  C  CA    . ILE B 58  ? 0.2032 0.2060 0.1991 -0.0220 0.0021  0.0209  57  ILE B CA    
3543  C  C     . ILE B 58  ? 0.2380 0.2402 0.2277 -0.0304 0.0031  0.0237  57  ILE B C     
3544  O  O     . ILE B 58  ? 0.2241 0.2283 0.2194 -0.0312 0.0032  0.0254  57  ILE B O     
3545  C  CB    . ILE B 58  ? 0.1822 0.1904 0.1892 -0.0169 0.0091  0.0177  57  ILE B CB    
3546  C  CG1   . ILE B 58  ? 0.1940 0.2021 0.2052 -0.0095 0.0080  0.0154  57  ILE B CG1   
3547  C  CG2   . ILE B 58  ? 0.2347 0.2456 0.2398 -0.0215 0.0197  0.0145  57  ILE B CG2   
3548  C  CD1   . ILE B 58  ? 0.2485 0.2609 0.2702 -0.0045 0.0133  0.0134  57  ILE B CD1   
3560  N  N     . PRO B 59  ? 0.2277 0.2271 0.2051 -0.0377 0.0032  0.0246  58  PRO B N     
3561  C  CA    . PRO B 59  ? 0.2482 0.2464 0.2177 -0.0467 0.0035  0.0279  58  PRO B CA    
3562  C  C     . PRO B 59  ? 0.2617 0.2654 0.2362 -0.0493 0.0139  0.0253  58  PRO B C     
3563  O  O     . PRO B 59  ? 0.2584 0.2658 0.2362 -0.0478 0.0231  0.0201  58  PRO B O     
3564  C  CB    . PRO B 59  ? 0.2729 0.2676 0.2275 -0.0540 0.0030  0.0284  58  PRO B CB    
3565  C  CG    . PRO B 59  ? 0.2416 0.2340 0.1981 -0.0478 -0.0039 0.0284  58  PRO B CG    
3566  C  CD    . PRO B 59  ? 0.2544 0.2508 0.2239 -0.0383 0.0003  0.0239  58  PRO B CD    
3574  N  N     . GLY B 60  ? 0.2529 0.2571 0.2284 -0.0534 0.0123  0.0288  59  GLY B N     
3575  C  CA    . GLY B 60  ? 0.2601 0.2705 0.2427 -0.0557 0.0212  0.0269  59  GLY B CA    
3576  C  C     . GLY B 60  ? 0.2520 0.2670 0.2512 -0.0480 0.0204  0.0267  59  GLY B C     
3577  O  O     . GLY B 60  ? 0.2557 0.2764 0.2630 -0.0500 0.0261  0.0263  59  GLY B O     
3581  N  N     . PHE B 61  ? 0.2328 0.2455 0.2370 -0.0400 0.0130  0.0273  60  PHE B N     
3582  C  CA    . PHE B 61  ? 0.1961 0.2131 0.2147 -0.0331 0.0119  0.0270  60  PHE B CA    
3583  C  C     . PHE B 61  ? 0.1980 0.2106 0.2181 -0.0293 0.0009  0.0302  60  PHE B C     
3584  O  O     . PHE B 61  ? 0.1957 0.2092 0.2208 -0.0306 -0.0024 0.0328  60  PHE B O     
3585  C  CB    . PHE B 61  ? 0.2291 0.2495 0.2549 -0.0263 0.0174  0.0226  60  PHE B CB    
3586  C  CG    . PHE B 61  ? 0.2023 0.2274 0.2307 -0.0291 0.0290  0.0188  60  PHE B CG    
3587  C  CD1   . PHE B 61  ? 0.2742 0.3064 0.3152 -0.0290 0.0351  0.0181  60  PHE B CD1   
3588  C  CD2   . PHE B 61  ? 0.2641 0.2865 0.2827 -0.0318 0.0342  0.0155  60  PHE B CD2   
3589  C  CE1   . PHE B 61  ? 0.2800 0.3165 0.3247 -0.0314 0.0471  0.0137  60  PHE B CE1   
3590  C  CE2   . PHE B 61  ? 0.3004 0.3263 0.3210 -0.0345 0.0456  0.0109  60  PHE B CE2   
3591  C  CZ    . PHE B 61  ? 0.3173 0.3501 0.3515 -0.0340 0.0524  0.0098  60  PHE B CZ    
3601  N  N     . MET B 62  ? 0.1949 0.2029 0.2113 -0.0248 -0.0045 0.0296  61  MET B N     
3602  C  CA    . MET B 62  ? 0.1866 0.1905 0.2055 -0.0207 -0.0138 0.0314  61  MET B CA    
3603  C  C     . MET B 62  ? 0.2000 0.1988 0.2144 -0.0168 -0.0191 0.0306  61  MET B C     
3604  O  O     . MET B 62  ? 0.2159 0.2150 0.2259 -0.0164 -0.0160 0.0285  61  MET B O     
3605  C  CB    . MET B 62  ? 0.2154 0.2239 0.2459 -0.0152 -0.0138 0.0302  61  MET B CB    
3606  C  CG    . MET B 62  ? 0.2646 0.2788 0.3016 -0.0106 -0.0071 0.0270  61  MET B CG    
3607  S  SD    . MET B 62  ? 0.2230 0.2363 0.2558 -0.0070 -0.0032 0.0234  61  MET B SD    
3608  C  CE    . MET B 62  ? 0.2579 0.2659 0.2907 -0.0019 -0.0145 0.0244  61  MET B CE    
3618  N  N     . CYS B 63  ? 0.2195 0.2135 0.2354 -0.0145 -0.0274 0.0321  62  CYS B N     
3619  C  CA    . CYS B 63  ? 0.1838 0.1735 0.1988 -0.0096 -0.0328 0.0309  62  CYS B CA    
3620  C  C     . CYS B 63  ? 0.2081 0.1989 0.2305 -0.0031 -0.0346 0.0283  62  CYS B C     
3621  O  O     . CYS B 63  ? 0.2193 0.2090 0.2451 -0.0037 -0.0377 0.0295  62  CYS B O     
3622  C  CB    . CYS B 63  ? 0.1920 0.1743 0.2033 -0.0124 -0.0411 0.0346  62  CYS B CB    
3623  S  SG    . CYS B 63  ? 0.2557 0.2357 0.2559 -0.0217 -0.0409 0.0390  62  CYS B SG    
3629  N  N     . GLN B 64  ? 0.1784 0.1707 0.2021 0.0023  -0.0331 0.0249  63  GLN B N     
3630  C  CA    . GLN B 64  ? 0.1997 0.1934 0.2287 0.0078  -0.0339 0.0222  63  GLN B CA    
3631  C  C     . GLN B 64  ? 0.2160 0.2061 0.2447 0.0123  -0.0379 0.0197  63  GLN B C     
3632  O  O     . GLN B 64  ? 0.2109 0.2003 0.2369 0.0128  -0.0374 0.0190  63  GLN B O     
3633  C  CB    . GLN B 64  ? 0.1999 0.2000 0.2318 0.0100  -0.0271 0.0205  63  GLN B CB    
3634  C  CG    . GLN B 64  ? 0.1945 0.1961 0.2301 0.0151  -0.0279 0.0182  63  GLN B CG    
3635  C  CD    . GLN B 64  ? 0.1898 0.1972 0.2293 0.0167  -0.0221 0.0179  63  GLN B CD    
3636  O  OE1   . GLN B 64  ? 0.1930 0.2035 0.2343 0.0143  -0.0172 0.0190  63  GLN B OE1   
3637  N  NE2   . GLN B 64  ? 0.1885 0.1970 0.2294 0.0209  -0.0226 0.0163  63  GLN B NE2   
3646  N  N     . GLY B 65  ? 0.2323 0.2200 0.2638 0.0150  -0.0417 0.0180  64  GLY B N     
3647  C  CA    . GLY B 65  ? 0.1691 0.1534 0.2016 0.0192  -0.0449 0.0147  64  GLY B CA    
3648  C  C     . GLY B 65  ? 0.2050 0.1893 0.2393 0.0222  -0.0456 0.0115  64  GLY B C     
3649  O  O     . GLY B 65  ? 0.2024 0.1907 0.2373 0.0216  -0.0435 0.0120  64  GLY B O     
3653  N  N     . GLY B 66  ? 0.2064 0.1865 0.2420 0.0252  -0.0488 0.0081  65  GLY B N     
3654  C  CA    . GLY B 66  ? 0.1748 0.1534 0.2107 0.0270  -0.0501 0.0044  65  GLY B CA    
3655  C  C     . GLY B 66  ? 0.2309 0.2126 0.2656 0.0306  -0.0466 0.0000  65  GLY B C     
3656  O  O     . GLY B 66  ? 0.2597 0.2401 0.2930 0.0313  -0.0475 -0.0034 65  GLY B O     
3660  N  N     . ASP B 67  ? 0.2261 0.2117 0.2606 0.0324  -0.0426 -0.0004 66  ASP B N     
3661  C  CA    . ASP B 67  ? 0.2312 0.2195 0.2644 0.0355  -0.0391 -0.0045 66  ASP B CA    
3662  C  C     . ASP B 67  ? 0.2470 0.2320 0.2833 0.0384  -0.0405 -0.0091 66  ASP B C     
3663  O  O     . ASP B 67  ? 0.2501 0.2363 0.2892 0.0398  -0.0396 -0.0092 66  ASP B O     
3664  C  CB    . ASP B 67  ? 0.2367 0.2304 0.2688 0.0358  -0.0341 -0.0030 66  ASP B CB    
3665  C  CG    . ASP B 67  ? 0.2689 0.2653 0.2993 0.0384  -0.0304 -0.0069 66  ASP B CG    
3666  O  OD1   . ASP B 67  ? 0.2875 0.2819 0.3170 0.0397  -0.0313 -0.0111 66  ASP B OD1   
3667  O  OD2   . ASP B 67  ? 0.2525 0.2526 0.2821 0.0386  -0.0263 -0.0059 66  ASP B OD2   
3672  N  N     . PHE B 68  ? 0.2349 0.2161 0.2713 0.0392  -0.0424 -0.0131 67  PHE B N     
3673  C  CA    . PHE B 68  ? 0.2600 0.2378 0.3010 0.0424  -0.0431 -0.0184 67  PHE B CA    
3674  C  C     . PHE B 68  ? 0.2884 0.2694 0.3271 0.0445  -0.0382 -0.0242 67  PHE B C     
3675  O  O     . PHE B 68  ? 0.3111 0.2904 0.3545 0.0472  -0.0374 -0.0296 67  PHE B O     
3676  C  CB    . PHE B 68  ? 0.2881 0.2582 0.3313 0.0419  -0.0479 -0.0202 67  PHE B CB    
3677  C  CG    . PHE B 68  ? 0.2810 0.2498 0.3183 0.0396  -0.0481 -0.0222 67  PHE B CG    
3678  C  CD1   . PHE B 68  ? 0.3036 0.2727 0.3374 0.0407  -0.0450 -0.0287 67  PHE B CD1   
3679  C  CD2   . PHE B 68  ? 0.2889 0.2564 0.3237 0.0359  -0.0514 -0.0178 67  PHE B CD2   
3680  C  CE1   . PHE B 68  ? 0.3264 0.2942 0.3533 0.0377  -0.0459 -0.0303 67  PHE B CE1   
3681  C  CE2   . PHE B 68  ? 0.2751 0.2422 0.3048 0.0334  -0.0523 -0.0192 67  PHE B CE2   
3682  C  CZ    . PHE B 68  ? 0.2787 0.2456 0.3040 0.0342  -0.0499 -0.0254 67  PHE B CZ    
3692  N  N     . THR B 69  ? 0.2826 0.2685 0.3150 0.0431  -0.0346 -0.0230 68  THR B N     
3693  C  CA    . THR B 69  ? 0.3205 0.3093 0.3495 0.0442  -0.0299 -0.0280 68  THR B CA    
3694  C  C     . THR B 69  ? 0.3270 0.3215 0.3574 0.0455  -0.0255 -0.0271 68  THR B C     
3695  O  O     . THR B 69  ? 0.3441 0.3407 0.3755 0.0471  -0.0217 -0.0319 68  THR B O     
3696  C  CB    . THR B 69  ? 0.3222 0.3121 0.3425 0.0414  -0.0292 -0.0276 68  THR B CB    
3697  O  OG1   . THR B 69  ? 0.3157 0.3095 0.3343 0.0399  -0.0288 -0.0211 68  THR B OG1   
3698  C  CG2   . THR B 69  ? 0.2877 0.2721 0.3061 0.0394  -0.0338 -0.0289 68  THR B CG2   
3706  N  N     . ARG B 70  ? 0.2852 0.2822 0.3156 0.0443  -0.0254 -0.0214 69  ARG B N     
3707  C  CA    . ARG B 70  ? 0.2880 0.2896 0.3193 0.0449  -0.0215 -0.0204 69  ARG B CA    
3708  C  C     . ARG B 70  ? 0.3203 0.3218 0.3569 0.0450  -0.0234 -0.0176 69  ARG B C     
3709  O  O     . ARG B 70  ? 0.3137 0.3187 0.3520 0.0454  -0.0208 -0.0176 69  ARG B O     
3710  C  CB    . ARG B 70  ? 0.2823 0.2868 0.3084 0.0431  -0.0188 -0.0165 69  ARG B CB    
3711  C  CG    . ARG B 70  ? 0.3453 0.3502 0.3652 0.0423  -0.0174 -0.0182 69  ARG B CG    
3712  C  CD    . ARG B 70  ? 0.3755 0.3829 0.3921 0.0407  -0.0157 -0.0135 69  ARG B CD    
3713  N  NE    . ARG B 70  ? 0.4312 0.4388 0.4410 0.0393  -0.0157 -0.0140 69  ARG B NE    
3714  C  CZ    . ARG B 70  ? 0.4012 0.4105 0.4084 0.0378  -0.0156 -0.0094 69  ARG B CZ    
3715  N  NH1   . ARG B 70  ? 0.3328 0.3434 0.3442 0.0381  -0.0147 -0.0047 69  ARG B NH1   
3716  N  NH2   . ARG B 70  ? 0.4310 0.4401 0.4313 0.0358  -0.0168 -0.0094 69  ARG B NH2   
3730  N  N     . HIS B 71  ? 0.3052 0.3028 0.3434 0.0440  -0.0281 -0.0149 70  HIS B N     
3731  C  CA    . HIS B 71  ? 0.2894 0.2864 0.3309 0.0429  -0.0308 -0.0114 70  HIS B CA    
3732  C  C     . HIS B 71  ? 0.3341 0.3349 0.3726 0.0410  -0.0272 -0.0085 70  HIS B C     
3733  O  O     . HIS B 71  ? 0.3661 0.3681 0.4065 0.0402  -0.0277 -0.0073 70  HIS B O     
3734  C  CB    . HIS B 71  ? 0.3281 0.3244 0.3770 0.0455  -0.0331 -0.0140 70  HIS B CB    
3735  C  CG    . HIS B 71  ? 0.3350 0.3269 0.3881 0.0478  -0.0358 -0.0180 70  HIS B CG    
3736  N  ND1   . HIS B 71  ? 0.3232 0.3091 0.3787 0.0471  -0.0415 -0.0159 70  HIS B ND1   
3737  C  CD2   . HIS B 71  ? 0.2918 0.2841 0.3474 0.0506  -0.0333 -0.0242 70  HIS B CD2   
3738  C  CE1   . HIS B 71  ? 0.3519 0.3340 0.4116 0.0497  -0.0425 -0.0208 70  HIS B CE1   
3739  N  NE2   . HIS B 71  ? 0.3138 0.2998 0.3731 0.0517  -0.0373 -0.0263 70  HIS B NE2   
3747  N  N     . ASN B 72  ? 0.2619 0.2645 0.2961 0.0399  -0.0238 -0.0072 71  ASN B N     
3748  C  CA    . ASN B 72  ? 0.3399 0.3452 0.3721 0.0381  -0.0199 -0.0049 71  ASN B CA    
3749  C  C     . ASN B 72  ? 0.2703 0.2757 0.3003 0.0360  -0.0185 -0.0015 71  ASN B C     
3750  O  O     . ASN B 72  ? 0.3265 0.3339 0.3555 0.0349  -0.0143 -0.0003 71  ASN B O     
3751  C  CB    . ASN B 72  ? 0.3276 0.3363 0.3591 0.0396  -0.0152 -0.0074 71  ASN B CB    
3752  C  CG    . ASN B 72  ? 0.3855 0.3950 0.4141 0.0404  -0.0130 -0.0079 71  ASN B CG    
3753  O  OD1   . ASN B 72  ? 0.2723 0.2805 0.2996 0.0398  -0.0148 -0.0060 71  ASN B OD1   
3754  N  ND2   . ASN B 72  ? 0.3557 0.3676 0.3830 0.0413  -0.0094 -0.0100 71  ASN B ND2   
3761  N  N     . GLY B 73  ? 0.2407 0.2440 0.2710 0.0353  -0.0218 -0.0001 72  GLY B N     
3762  C  CA    . GLY B 73  ? 0.2259 0.2304 0.2563 0.0333  -0.0205 0.0031  72  GLY B CA    
3763  C  C     . GLY B 73  ? 0.2482 0.2549 0.2786 0.0345  -0.0190 0.0035  72  GLY B C     
3764  O  O     . GLY B 73  ? 0.2421 0.2502 0.2746 0.0333  -0.0188 0.0064  72  GLY B O     
3768  N  N     . THR B 74  ? 0.2505 0.2578 0.2789 0.0366  -0.0181 0.0010  73  THR B N     
3769  C  CA    . THR B 74  ? 0.2616 0.2707 0.2889 0.0370  -0.0176 0.0021  73  THR B CA    
3770  C  C     . THR B 74  ? 0.2783 0.2856 0.3029 0.0369  -0.0217 0.0003  73  THR B C     
3771  O  O     . THR B 74  ? 0.2894 0.2981 0.3123 0.0363  -0.0227 0.0020  73  THR B O     
3772  C  CB    . THR B 74  ? 0.2971 0.3079 0.3222 0.0382  -0.0135 0.0011  73  THR B CB    
3773  O  OG1   . THR B 74  ? 0.3060 0.3159 0.3284 0.0393  -0.0137 -0.0033 73  THR B OG1   
3774  C  CG2   . THR B 74  ? 0.3022 0.3139 0.3294 0.0380  -0.0090 0.0021  73  THR B CG2   
3782  N  N     . GLY B 75  ? 0.2396 0.2438 0.2640 0.0373  -0.0243 -0.0030 74  GLY B N     
3783  C  CA    . GLY B 75  ? 0.2721 0.2739 0.2934 0.0371  -0.0273 -0.0062 74  GLY B CA    
3784  C  C     . GLY B 75  ? 0.2835 0.2820 0.3061 0.0354  -0.0322 -0.0055 74  GLY B C     
3785  O  O     . GLY B 75  ? 0.2843 0.2838 0.3098 0.0337  -0.0336 -0.0012 74  GLY B O     
3789  N  N     . GLY B 76  ? 0.2683 0.2628 0.2892 0.0357  -0.0345 -0.0100 75  GLY B N     
3790  C  CA    . GLY B 76  ? 0.2677 0.2580 0.2889 0.0337  -0.0394 -0.0102 75  GLY B CA    
3791  C  C     . GLY B 76  ? 0.2488 0.2392 0.2644 0.0317  -0.0411 -0.0116 75  GLY B C     
3792  O  O     . GLY B 76  ? 0.2605 0.2548 0.2722 0.0312  -0.0391 -0.0103 75  GLY B O     
3796  N  N     . LYS B 77  ? 0.2602 0.2455 0.2747 0.0300  -0.0450 -0.0143 76  LYS B N     
3797  C  CA    . LYS B 77  ? 0.2778 0.2627 0.2859 0.0269  -0.0475 -0.0155 76  LYS B CA    
3798  C  C     . LYS B 77  ? 0.2247 0.2044 0.2342 0.0243  -0.0527 -0.0160 76  LYS B C     
3799  O  O     . LYS B 77  ? 0.2538 0.2286 0.2680 0.0255  -0.0538 -0.0174 76  LYS B O     
3800  C  CB    . LYS B 77  ? 0.2914 0.2747 0.2925 0.0274  -0.0447 -0.0223 76  LYS B CB    
3801  C  CG    . LYS B 77  ? 0.3075 0.2840 0.3109 0.0292  -0.0446 -0.0293 76  LYS B CG    
3802  C  CD    . LYS B 77  ? 0.3681 0.3444 0.3659 0.0301  -0.0398 -0.0366 76  LYS B CD    
3803  C  CE    . LYS B 77  ? 0.3938 0.3639 0.3958 0.0325  -0.0388 -0.0443 76  LYS B CE    
3804  N  NZ    . LYS B 77  ? 0.4429 0.4137 0.4390 0.0326  -0.0332 -0.0522 76  LYS B NZ    
3818  N  N     . SER B 78  ? 0.2438 0.2248 0.2498 0.0204  -0.0563 -0.0141 77  SER B N     
3819  C  CA    . SER B 78  ? 0.2547 0.2309 0.2616 0.0170  -0.0615 -0.0144 77  SER B CA    
3820  C  C     . SER B 78  ? 0.2768 0.2462 0.2768 0.0157  -0.0624 -0.0225 77  SER B C     
3821  O  O     . SER B 78  ? 0.3127 0.2820 0.3068 0.0170  -0.0587 -0.0274 77  SER B O     
3822  C  CB    . SER B 78  ? 0.2411 0.2224 0.2487 0.0130  -0.0656 -0.0086 77  SER B CB    
3823  O  OG    . SER B 78  ? 0.2696 0.2514 0.2688 0.0096  -0.0680 -0.0107 77  SER B OG    
3829  N  N     . ILE B 79  ? 0.2824 0.2457 0.2830 0.0127  -0.0670 -0.0240 78  ILE B N     
3830  C  CA    . ILE B 79  ? 0.2925 0.2484 0.2863 0.0107  -0.0679 -0.0322 78  ILE B CA    
3831  C  C     . ILE B 79  ? 0.3154 0.2742 0.2990 0.0056  -0.0701 -0.0326 78  ILE B C     
3832  O  O     . ILE B 79  ? 0.3391 0.2920 0.3147 0.0026  -0.0707 -0.0398 78  ILE B O     
3833  C  CB    . ILE B 79  ? 0.2767 0.2238 0.2748 0.0089  -0.0721 -0.0339 78  ILE B CB    
3834  C  CG1   . ILE B 79  ? 0.2848 0.2347 0.2838 0.0036  -0.0779 -0.0276 78  ILE B CG1   
3835  C  CG2   . ILE B 79  ? 0.3389 0.2824 0.3468 0.0134  -0.0710 -0.0326 78  ILE B CG2   
3836  C  CD1   . ILE B 79  ? 0.2983 0.2392 0.3000 0.0003  -0.0826 -0.0292 78  ILE B CD1   
3848  N  N     . TYR B 80  ? 0.3282 0.2955 0.3123 0.0042  -0.0716 -0.0250 79  TYR B N     
3849  C  CA    . TYR B 80  ? 0.3062 0.2775 0.2823 -0.0010 -0.0754 -0.0229 79  TYR B CA    
3850  C  C     . TYR B 80  ? 0.3256 0.3023 0.2950 0.0000  -0.0719 -0.0220 79  TYR B C     
3851  O  O     . TYR B 80  ? 0.3765 0.3569 0.3388 -0.0044 -0.0754 -0.0191 79  TYR B O     
3852  C  CB    . TYR B 80  ? 0.2911 0.2687 0.2749 -0.0034 -0.0805 -0.0141 79  TYR B CB    
3853  C  CG    . TYR B 80  ? 0.3383 0.3116 0.3292 -0.0051 -0.0840 -0.0136 79  TYR B CG    
3854  C  CD1   . TYR B 80  ? 0.3507 0.3162 0.3364 -0.0095 -0.0878 -0.0189 79  TYR B CD1   
3855  C  CD2   . TYR B 80  ? 0.3151 0.2915 0.3173 -0.0027 -0.0830 -0.0080 79  TYR B CD2   
3856  C  CE1   . TYR B 80  ? 0.3443 0.3051 0.3363 -0.0113 -0.0910 -0.0183 79  TYR B CE1   
3857  C  CE2   . TYR B 80  ? 0.2806 0.2528 0.2885 -0.0050 -0.0861 -0.0071 79  TYR B CE2   
3858  C  CZ    . TYR B 80  ? 0.3161 0.2803 0.3191 -0.0092 -0.0903 -0.0120 79  TYR B CZ    
3859  O  OH    . TYR B 80  ? 0.3315 0.2906 0.3399 -0.0119 -0.0936 -0.0110 79  TYR B OH    
3869  N  N     . GLY B 81  ? 0.3739 0.3509 0.3451 0.0050  -0.0657 -0.0241 80  GLY B N     
3870  C  CA    . GLY B 81  ? 0.3530 0.3360 0.3209 0.0065  -0.0621 -0.0212 80  GLY B CA    
3871  C  C     . GLY B 81  ? 0.3588 0.3457 0.3375 0.0118  -0.0585 -0.0166 80  GLY B C     
3872  O  O     . GLY B 81  ? 0.3383 0.3238 0.3260 0.0138  -0.0590 -0.0153 80  GLY B O     
3876  N  N     . GLU B 82  ? 0.3367 0.3282 0.3135 0.0136  -0.0548 -0.0142 81  GLU B N     
3877  C  CA    . GLU B 82  ? 0.3066 0.3012 0.2925 0.0182  -0.0508 -0.0108 81  GLU B CA    
3878  C  C     . GLU B 82  ? 0.3105 0.3081 0.3064 0.0183  -0.0538 -0.0041 81  GLU B C     
3879  O  O     . GLU B 82  ? 0.3322 0.3292 0.3355 0.0209  -0.0519 -0.0036 81  GLU B O     
3880  C  CB    . GLU B 82  ? 0.3305 0.3296 0.3136 0.0194  -0.0471 -0.0080 81  GLU B CB    
3881  C  CG    . GLU B 82  ? 0.5110 0.5083 0.4857 0.0196  -0.0424 -0.0142 81  GLU B CG    
3882  C  CD    . GLU B 82  ? 0.5159 0.5125 0.4968 0.0242  -0.0370 -0.0177 81  GLU B CD    
3883  O  OE1   . GLU B 82  ? 0.5340 0.5341 0.5198 0.0267  -0.0342 -0.0137 81  GLU B OE1   
3884  O  OE2   . GLU B 82  ? 0.4760 0.4683 0.4574 0.0253  -0.0359 -0.0245 81  GLU B OE2   
3891  N  N     . LYS B 83  ? 0.2783 0.2795 0.2746 0.0151  -0.0585 0.0009  82  LYS B N     
3892  C  CA    . LYS B 83  ? 0.2456 0.2511 0.2527 0.0149  -0.0608 0.0073  82  LYS B CA    
3893  C  C     . LYS B 83  ? 0.2955 0.3018 0.3017 0.0100  -0.0678 0.0092  82  LYS B C     
3894  O  O     . LYS B 83  ? 0.3253 0.3298 0.3218 0.0067  -0.0709 0.0070  82  LYS B O     
3895  C  CB    . LYS B 83  ? 0.3151 0.3270 0.3282 0.0171  -0.0582 0.0134  82  LYS B CB    
3896  C  CG    . LYS B 83  ? 0.3150 0.3267 0.3300 0.0216  -0.0512 0.0121  82  LYS B CG    
3897  C  CD    . LYS B 83  ? 0.3812 0.3892 0.3996 0.0234  -0.0487 0.0087  82  LYS B CD    
3898  C  CE    . LYS B 83  ? 0.3805 0.3869 0.3964 0.0267  -0.0430 0.0053  82  LYS B CE    
3899  N  NZ    . LYS B 83  ? 0.3712 0.3721 0.3839 0.0273  -0.0430 -0.0009 82  LYS B NZ    
3913  N  N     . PHE B 84  ? 0.2494 0.2583 0.2654 0.0090  -0.0701 0.0131  83  PHE B N     
3914  C  CA    . PHE B 84  ? 0.2660 0.2772 0.2838 0.0042  -0.0769 0.0160  83  PHE B CA    
3915  C  C     . PHE B 84  ? 0.2501 0.2691 0.2820 0.0044  -0.0775 0.0231  83  PHE B C     
3916  O  O     . PHE B 84  ? 0.2342 0.2556 0.2740 0.0079  -0.0722 0.0250  83  PHE B O     
3917  C  CB    . PHE B 84  ? 0.2733 0.2774 0.2872 0.0009  -0.0801 0.0110  83  PHE B CB    
3918  C  CG    . PHE B 84  ? 0.2739 0.2751 0.2952 0.0022  -0.0781 0.0106  83  PHE B CG    
3919  C  CD1   . PHE B 84  ? 0.2448 0.2414 0.2650 0.0062  -0.0730 0.0069  83  PHE B CD1   
3920  C  CD2   . PHE B 84  ? 0.2487 0.2518 0.2777 -0.0012 -0.0817 0.0141  83  PHE B CD2   
3921  C  CE1   . PHE B 84  ? 0.2725 0.2659 0.2983 0.0068  -0.0719 0.0072  83  PHE B CE1   
3922  C  CE2   . PHE B 84  ? 0.2715 0.2713 0.3057 -0.0010 -0.0800 0.0140  83  PHE B CE2   
3923  C  CZ    . PHE B 84  ? 0.2345 0.2294 0.2668 0.0030  -0.0754 0.0109  83  PHE B CZ    
3933  N  N     . GLU B 85  ? 0.2313 0.2545 0.2663 0.0002  -0.0839 0.0269  84  GLU B N     
3934  C  CA    . GLU B 85  ? 0.2430 0.2754 0.2925 0.0001  -0.0853 0.0341  84  GLU B CA    
3935  C  C     . GLU B 85  ? 0.2259 0.2591 0.2853 -0.0002 -0.0829 0.0344  84  GLU B C     
3936  O  O     . GLU B 85  ? 0.2592 0.2854 0.3135 -0.0017 -0.0828 0.0300  84  GLU B O     
3937  C  CB    . GLU B 85  ? 0.2752 0.3122 0.3250 -0.0048 -0.0939 0.0382  84  GLU B CB    
3938  C  CG    . GLU B 85  ? 0.3190 0.3524 0.3649 -0.0107 -0.0997 0.0355  84  GLU B CG    
3939  C  CD    . GLU B 85  ? 0.3552 0.3778 0.3840 -0.0124 -0.0999 0.0273  84  GLU B CD    
3940  O  OE1   . GLU B 85  ? 0.3108 0.3305 0.3290 -0.0107 -0.0977 0.0245  84  GLU B OE1   
3941  O  OE2   . GLU B 85  ? 0.3936 0.4108 0.4203 -0.0156 -0.1020 0.0235  84  GLU B OE2   
3948  N  N     . ASP B 86  ? 0.2157 0.2571 0.2894 0.0011  -0.0807 0.0397  85  ASP B N     
3949  C  CA    . ASP B 86  ? 0.1795 0.2233 0.2631 -0.0004 -0.0784 0.0408  85  ASP B CA    
3950  C  C     . ASP B 86  ? 0.2323 0.2775 0.3184 -0.0064 -0.0856 0.0420  85  ASP B C     
3951  O  O     . ASP B 86  ? 0.2170 0.2693 0.3097 -0.0086 -0.0911 0.0464  85  ASP B O     
3952  C  CB    . ASP B 86  ? 0.1808 0.2339 0.2800 0.0023  -0.0735 0.0454  85  ASP B CB    
3953  C  CG    . ASP B 86  ? 0.1956 0.2470 0.2930 0.0076  -0.0660 0.0439  85  ASP B CG    
3954  O  OD1   . ASP B 86  ? 0.1910 0.2352 0.2795 0.0087  -0.0620 0.0395  85  ASP B OD1   
3955  O  OD2   . ASP B 86  ? 0.2103 0.2676 0.3166 0.0105  -0.0641 0.0475  85  ASP B OD2   
3960  N  N     . GLU B 87  ? 0.1912 0.2298 0.2729 -0.0092 -0.0859 0.0387  86  GLU B N     
3961  C  CA    . GLU B 87  ? 0.2257 0.2634 0.3076 -0.0153 -0.0928 0.0390  86  GLU B CA    
3962  C  C     . GLU B 87  ? 0.2118 0.2599 0.3100 -0.0182 -0.0934 0.0446  86  GLU B C     
3963  O  O     . GLU B 87  ? 0.2104 0.2645 0.3141 -0.0220 -0.1000 0.0478  86  GLU B O     
3964  C  CB    . GLU B 87  ? 0.2498 0.2761 0.3227 -0.0171 -0.0927 0.0338  86  GLU B CB    
3965  C  CG    . GLU B 87  ? 0.3064 0.3295 0.3784 -0.0238 -0.0996 0.0333  86  GLU B CG    
3966  C  CD    . GLU B 87  ? 0.2851 0.2946 0.3467 -0.0248 -0.1002 0.0274  86  GLU B CD    
3967  O  OE1   . GLU B 87  ? 0.2323 0.2364 0.2904 -0.0206 -0.0950 0.0249  86  GLU B OE1   
3968  O  OE2   . GLU B 87  ? 0.2980 0.3022 0.3551 -0.0298 -0.1062 0.0250  86  GLU B OE2   
3975  N  N     . ASN B 88  ? 0.1872 0.2379 0.2934 -0.0171 -0.0868 0.0457  87  ASN B N     
3976  C  CA    . ASN B 88  ? 0.1833 0.2451 0.3065 -0.0191 -0.0851 0.0505  87  ASN B CA    
3977  C  C     . ASN B 88  ? 0.1977 0.2597 0.3242 -0.0169 -0.0756 0.0499  87  ASN B C     
3978  O  O     . ASN B 88  ? 0.1954 0.2485 0.3107 -0.0149 -0.0721 0.0462  87  ASN B O     
3979  C  CB    . ASN B 88  ? 0.1943 0.2575 0.3217 -0.0263 -0.0910 0.0520  87  ASN B CB    
3980  C  CG    . ASN B 88  ? 0.2619 0.3149 0.3806 -0.0296 -0.0900 0.0488  87  ASN B CG    
3981  O  OD1   . ASN B 88  ? 0.2054 0.2580 0.3262 -0.0291 -0.0834 0.0489  87  ASN B OD1   
3982  N  ND2   . ASN B 88  ? 0.2425 0.2871 0.3516 -0.0334 -0.0968 0.0462  87  ASN B ND2   
3989  N  N     . PHE B 89  ? 0.1742 0.2467 0.3165 -0.0176 -0.0715 0.0534  88  PHE B N     
3990  C  CA    . PHE B 89  ? 0.1697 0.2439 0.3160 -0.0165 -0.0619 0.0528  88  PHE B CA    
3991  C  C     . PHE B 89  ? 0.1767 0.2553 0.3312 -0.0228 -0.0604 0.0546  88  PHE B C     
3992  O  O     . PHE B 89  ? 0.2041 0.2906 0.3700 -0.0232 -0.0531 0.0557  88  PHE B O     
3993  C  CB    . PHE B 89  ? 0.1956 0.2783 0.3538 -0.0113 -0.0561 0.0543  88  PHE B CB    
3994  C  CG    . PHE B 89  ? 0.1791 0.2571 0.3289 -0.0055 -0.0567 0.0528  88  PHE B CG    
3995  C  CD1   . PHE B 89  ? 0.1736 0.2423 0.3096 -0.0031 -0.0527 0.0488  88  PHE B CD1   
3996  C  CD2   . PHE B 89  ? 0.2009 0.2835 0.3561 -0.0031 -0.0618 0.0558  88  PHE B CD2   
3997  C  CE1   . PHE B 89  ? 0.2056 0.2705 0.3344 0.0017  -0.0527 0.0474  88  PHE B CE1   
3998  C  CE2   . PHE B 89  ? 0.2127 0.2908 0.3593 0.0014  -0.0622 0.0547  88  PHE B CE2   
3999  C  CZ    . PHE B 89  ? 0.2069 0.2762 0.3404 0.0039  -0.0573 0.0503  88  PHE B CZ    
4009  N  N     . ILE B 90  ? 0.1917 0.2656 0.3410 -0.0281 -0.0674 0.0547  89  ILE B N     
4010  C  CA    . ILE B 90  ? 0.1892 0.2672 0.3462 -0.0351 -0.0670 0.0569  89  ILE B CA    
4011  C  C     . ILE B 90  ? 0.2031 0.2775 0.3554 -0.0368 -0.0588 0.0558  89  ILE B C     
4012  O  O     . ILE B 90  ? 0.2138 0.2964 0.3767 -0.0400 -0.0525 0.0575  89  ILE B O     
4013  C  CB    . ILE B 90  ? 0.1909 0.2616 0.3404 -0.0405 -0.0763 0.0566  89  ILE B CB    
4014  C  CG1   . ILE B 90  ? 0.1931 0.2694 0.3482 -0.0407 -0.0846 0.0583  89  ILE B CG1   
4015  C  CG2   . ILE B 90  ? 0.2310 0.3035 0.3858 -0.0484 -0.0755 0.0588  89  ILE B CG2   
4016  C  CD1   . ILE B 90  ? 0.2763 0.3435 0.4209 -0.0454 -0.0938 0.0565  89  ILE B CD1   
4028  N  N     . LEU B 91  ? 0.2148 0.2770 0.3513 -0.0351 -0.0588 0.0529  90  LEU B N     
4029  C  CA    . LEU B 91  ? 0.1851 0.2419 0.3143 -0.0377 -0.0531 0.0523  90  LEU B CA    
4030  C  C     . LEU B 91  ? 0.2369 0.2974 0.3672 -0.0332 -0.0439 0.0508  90  LEU B C     
4031  O  O     . LEU B 91  ? 0.2034 0.2646 0.3335 -0.0267 -0.0433 0.0492  90  LEU B O     
4032  C  CB    . LEU B 91  ? 0.2382 0.2801 0.3513 -0.0378 -0.0584 0.0502  90  LEU B CB    
4033  C  CG    . LEU B 91  ? 0.2605 0.2965 0.3715 -0.0428 -0.0671 0.0509  90  LEU B CG    
4034  C  CD1   . LEU B 91  ? 0.2978 0.3184 0.3949 -0.0426 -0.0720 0.0485  90  LEU B CD1   
4035  C  CD2   . LEU B 91  ? 0.3131 0.3543 0.4319 -0.0508 -0.0657 0.0546  90  LEU B CD2   
4047  N  N     . LYS B 92  ? 0.2134 0.2755 0.3436 -0.0373 -0.0365 0.0513  91  LYS B N     
4048  C  CA    . LYS B 92  ? 0.2202 0.2865 0.3522 -0.0346 -0.0266 0.0496  91  LYS B CA    
4049  C  C     . LYS B 92  ? 0.2076 0.2637 0.3233 -0.0355 -0.0241 0.0479  91  LYS B C     
4050  O  O     . LYS B 92  ? 0.2433 0.2902 0.3483 -0.0394 -0.0291 0.0490  91  LYS B O     
4051  C  CB    . LYS B 92  ? 0.2209 0.2987 0.3665 -0.0390 -0.0185 0.0508  91  LYS B CB    
4052  C  CG    . LYS B 92  ? 0.2748 0.3636 0.4383 -0.0399 -0.0217 0.0534  91  LYS B CG    
4053  C  CD    . LYS B 92  ? 0.3098 0.4032 0.4822 -0.0323 -0.0247 0.0534  91  LYS B CD    
4054  C  CE    . LYS B 92  ? 0.3360 0.4433 0.5300 -0.0332 -0.0255 0.0564  91  LYS B CE    
4055  N  NZ    . LYS B 92  ? 0.3487 0.4578 0.5475 -0.0278 -0.0336 0.0580  91  LYS B NZ    
4069  N  N     . HIS B 93  ? 0.1992 0.2570 0.3138 -0.0319 -0.0167 0.0454  92  HIS B N     
4070  C  CA    . HIS B 93  ? 0.2037 0.2532 0.3037 -0.0328 -0.0141 0.0439  92  HIS B CA    
4071  C  C     . HIS B 93  ? 0.2037 0.2563 0.3027 -0.0406 -0.0067 0.0448  92  HIS B C     
4072  O  O     . HIS B 93  ? 0.2460 0.3043 0.3487 -0.0408 0.0028  0.0426  92  HIS B O     
4073  C  CB    . HIS B 93  ? 0.1945 0.2440 0.2931 -0.0262 -0.0098 0.0406  92  HIS B CB    
4074  C  CG    . HIS B 93  ? 0.2017 0.2489 0.3008 -0.0191 -0.0162 0.0398  92  HIS B CG    
4075  N  ND1   . HIS B 93  ? 0.1837 0.2380 0.2952 -0.0155 -0.0177 0.0406  92  HIS B ND1   
4076  C  CD2   . HIS B 93  ? 0.2100 0.2488 0.2987 -0.0155 -0.0211 0.0383  92  HIS B CD2   
4077  C  CE1   . HIS B 93  ? 0.1949 0.2450 0.3020 -0.0105 -0.0233 0.0396  92  HIS B CE1   
4078  N  NE2   . HIS B 93  ? 0.1857 0.2265 0.2794 -0.0102 -0.0250 0.0379  92  HIS B NE2   
4086  N  N     . THR B 94  ? 0.2366 0.2851 0.3306 -0.0477 -0.0110 0.0479  93  THR B N     
4087  C  CA    . THR B 94  ? 0.2498 0.3027 0.3448 -0.0563 -0.0045 0.0496  93  THR B CA    
4088  C  C     . THR B 94  ? 0.2565 0.3026 0.3355 -0.0616 -0.0008 0.0496  93  THR B C     
4089  O  O     . THR B 94  ? 0.2576 0.3081 0.3358 -0.0689 0.0069  0.0500  93  THR B O     
4090  C  CB    . THR B 94  ? 0.2245 0.2762 0.3217 -0.0625 -0.0109 0.0535  93  THR B CB    
4091  O  OG1   . THR B 94  ? 0.2799 0.3191 0.3661 -0.0617 -0.0212 0.0551  93  THR B OG1   
4092  C  CG2   . THR B 94  ? 0.2727 0.3343 0.3876 -0.0598 -0.0126 0.0538  93  THR B CG2   
4100  N  N     . GLY B 95  ? 0.2588 0.2948 0.3254 -0.0584 -0.0061 0.0493  94  GLY B N     
4101  C  CA    . GLY B 95  ? 0.2608 0.2896 0.3117 -0.0640 -0.0051 0.0505  94  GLY B CA    
4102  C  C     . GLY B 95  ? 0.2728 0.2907 0.3134 -0.0597 -0.0135 0.0510  94  GLY B C     
4103  O  O     . GLY B 95  ? 0.2501 0.2655 0.2949 -0.0524 -0.0196 0.0497  94  GLY B O     
4107  N  N     . PRO B 96  ? 0.2309 0.2421 0.2576 -0.0649 -0.0140 0.0529  95  PRO B N     
4108  C  CA    . PRO B 96  ? 0.2489 0.2499 0.2670 -0.0615 -0.0225 0.0540  95  PRO B CA    
4109  C  C     . PRO B 96  ? 0.2604 0.2545 0.2817 -0.0594 -0.0329 0.0564  95  PRO B C     
4110  O  O     . PRO B 96  ? 0.2633 0.2568 0.2873 -0.0647 -0.0352 0.0596  95  PRO B O     
4111  C  CB    . PRO B 96  ? 0.2777 0.2733 0.2810 -0.0701 -0.0221 0.0575  95  PRO B CB    
4112  C  CG    . PRO B 96  ? 0.2800 0.2832 0.2827 -0.0772 -0.0120 0.0567  95  PRO B CG    
4113  C  CD    . PRO B 96  ? 0.3093 0.3219 0.3278 -0.0751 -0.0078 0.0549  95  PRO B CD    
4121  N  N     . GLY B 97  ? 0.2478 0.2366 0.2693 -0.0517 -0.0387 0.0545  96  GLY B N     
4122  C  CA    . GLY B 97  ? 0.2839 0.2648 0.3076 -0.0491 -0.0482 0.0555  96  GLY B CA    
4123  C  C     . GLY B 97  ? 0.2320 0.2168 0.2658 -0.0428 -0.0492 0.0519  96  GLY B C     
4124  O  O     . GLY B 97  ? 0.2355 0.2136 0.2705 -0.0389 -0.0563 0.0509  96  GLY B O     
4128  N  N     . ILE B 98  ? 0.2230 0.2184 0.2641 -0.0416 -0.0423 0.0498  97  ILE B N     
4129  C  CA    . ILE B 98  ? 0.2110 0.2113 0.2616 -0.0363 -0.0434 0.0472  97  ILE B CA    
4130  C  C     . ILE B 98  ? 0.2203 0.2168 0.2688 -0.0282 -0.0462 0.0434  97  ILE B C     
4131  O  O     . ILE B 98  ? 0.2111 0.2081 0.2556 -0.0251 -0.0425 0.0417  97  ILE B O     
4132  C  CB    . ILE B 98  ? 0.2121 0.2248 0.2720 -0.0365 -0.0353 0.0463  97  ILE B CB    
4133  C  CG1   . ILE B 98  ? 0.2520 0.2696 0.3170 -0.0442 -0.0330 0.0495  97  ILE B CG1   
4134  C  CG2   . ILE B 98  ? 0.2096 0.2271 0.2780 -0.0297 -0.0366 0.0438  97  ILE B CG2   
4135  C  CD1   . ILE B 98  ? 0.2659 0.2829 0.3371 -0.0457 -0.0399 0.0510  97  ILE B CD1   
4147  N  N     . LEU B 99  ? 0.2006 0.1934 0.2514 -0.0252 -0.0524 0.0420  98  LEU B N     
4148  C  CA    . LEU B 99  ? 0.1935 0.1829 0.2426 -0.0181 -0.0549 0.0380  98  LEU B CA    
4149  C  C     . LEU B 99  ? 0.2035 0.2006 0.2594 -0.0146 -0.0536 0.0359  98  LEU B C     
4150  O  O     . LEU B 99  ? 0.2170 0.2161 0.2777 -0.0170 -0.0566 0.0369  98  LEU B O     
4151  C  CB    . LEU B 99  ? 0.2158 0.1946 0.2620 -0.0177 -0.0627 0.0372  98  LEU B CB    
4152  C  CG    . LEU B 99  ? 0.2287 0.2038 0.2737 -0.0110 -0.0651 0.0324  98  LEU B CG    
4153  C  CD1   . LEU B 99  ? 0.2125 0.1872 0.2538 -0.0072 -0.0622 0.0311  98  LEU B CD1   
4154  C  CD2   . LEU B 99  ? 0.2474 0.2120 0.2914 -0.0115 -0.0723 0.0311  98  LEU B CD2   
4166  N  N     . SER B 100 ? 0.1798 0.1807 0.2358 -0.0094 -0.0496 0.0335  99  SER B N     
4167  C  CA    . SER B 100 ? 0.1870 0.1958 0.2495 -0.0064 -0.0477 0.0327  99  SER B CA    
4168  C  C     . SER B 100 ? 0.1921 0.1996 0.2511 -0.0002 -0.0474 0.0293  99  SER B C     
4169  O  O     . SER B 100 ? 0.1793 0.1821 0.2324 0.0021  -0.0465 0.0273  99  SER B O     
4170  C  CB    . SER B 100 ? 0.1928 0.2107 0.2623 -0.0079 -0.0405 0.0347  99  SER B CB    
4171  O  OG    . SER B 100 ? 0.1798 0.2058 0.2579 -0.0049 -0.0390 0.0349  99  SER B OG    
4177  N  N     . MET B 101 ? 0.1682 0.1802 0.2310 0.0021  -0.0484 0.0288  100 MET B N     
4178  C  CA    . MET B 101 ? 0.1658 0.1763 0.2244 0.0070  -0.0488 0.0257  100 MET B CA    
4179  C  C     . MET B 101 ? 0.1718 0.1875 0.2328 0.0102  -0.0423 0.0260  100 MET B C     
4180  O  O     . MET B 101 ? 0.1602 0.1831 0.2291 0.0097  -0.0390 0.0285  100 MET B O     
4181  C  CB    . MET B 101 ? 0.1833 0.1961 0.2434 0.0071  -0.0533 0.0256  100 MET B CB    
4182  C  CG    . MET B 101 ? 0.1867 0.1921 0.2410 0.0057  -0.0596 0.0228  100 MET B CG    
4183  S  SD    . MET B 101 ? 0.2276 0.2225 0.2743 0.0073  -0.0607 0.0184  100 MET B SD    
4184  C  CE    . MET B 101 ? 0.2660 0.2602 0.3067 0.0117  -0.0603 0.0137  100 MET B CE    
4194  N  N     . ALA B 102 ? 0.1569 0.1693 0.2121 0.0134  -0.0403 0.0233  101 ALA B N     
4195  C  CA    . ALA B 102 ? 0.1518 0.1682 0.2087 0.0166  -0.0349 0.0230  101 ALA B CA    
4196  C  C     . ALA B 102 ? 0.1790 0.1982 0.2372 0.0192  -0.0367 0.0232  101 ALA B C     
4197  O  O     . ALA B 102 ? 0.1942 0.2111 0.2490 0.0188  -0.0419 0.0221  101 ALA B O     
4198  C  CB    . ALA B 102 ? 0.1545 0.1667 0.2050 0.0187  -0.0325 0.0202  101 ALA B CB    
4204  N  N     . ASN B 103 ? 0.1821 0.2060 0.2448 0.0215  -0.0324 0.0245  102 ASN B N     
4205  C  CA    . ASN B 103 ? 0.1857 0.2122 0.2495 0.0235  -0.0345 0.0257  102 ASN B CA    
4206  C  C     . ASN B 103 ? 0.2148 0.2439 0.2819 0.0266  -0.0290 0.0266  102 ASN B C     
4207  O  O     . ASN B 103 ? 0.2129 0.2422 0.2823 0.0270  -0.0232 0.0259  102 ASN B O     
4208  C  CB    . ASN B 103 ? 0.1876 0.2190 0.2589 0.0213  -0.0389 0.0295  102 ASN B CB    
4209  C  CG    . ASN B 103 ? 0.1804 0.2186 0.2644 0.0209  -0.0348 0.0327  102 ASN B CG    
4210  O  OD1   . ASN B 103 ? 0.1765 0.2173 0.2658 0.0235  -0.0297 0.0335  102 ASN B OD1   
4211  N  ND2   . ASN B 103 ? 0.1917 0.2327 0.2814 0.0174  -0.0372 0.0345  102 ASN B ND2   
4218  N  N     . ALA B 104 ? 0.2013 0.2318 0.2682 0.0283  -0.0310 0.0282  103 ALA B N     
4219  C  CA    . ALA B 104 ? 0.2269 0.2592 0.2975 0.0311  -0.0267 0.0297  103 ALA B CA    
4220  C  C     . ALA B 104 ? 0.2556 0.2935 0.3366 0.0316  -0.0292 0.0350  103 ALA B C     
4221  O  O     . ALA B 104 ? 0.3055 0.3440 0.3871 0.0334  -0.0297 0.0374  103 ALA B O     
4222  C  CB    . ALA B 104 ? 0.2414 0.2696 0.3018 0.0326  -0.0267 0.0273  103 ALA B CB    
4228  N  N     . GLY B 105 ? 0.2349 0.2772 0.3247 0.0297  -0.0309 0.0371  104 GLY B N     
4229  C  CA    . GLY B 105 ? 0.2053 0.2539 0.3068 0.0297  -0.0345 0.0424  104 GLY B CA    
4230  C  C     . GLY B 105 ? 0.2149 0.2648 0.3142 0.0262  -0.0427 0.0439  104 GLY B C     
4231  O  O     . GLY B 105 ? 0.1990 0.2443 0.2880 0.0238  -0.0451 0.0404  104 GLY B O     
4235  N  N     . PRO B 106 ? 0.2159 0.2721 0.3257 0.0258  -0.0473 0.0492  105 PRO B N     
4236  C  CA    . PRO B 106 ? 0.2268 0.2850 0.3356 0.0217  -0.0554 0.0509  105 PRO B CA    
4237  C  C     . PRO B 106 ? 0.2087 0.2605 0.3002 0.0196  -0.0605 0.0480  105 PRO B C     
4238  O  O     . PRO B 106 ? 0.2041 0.2531 0.2877 0.0211  -0.0606 0.0480  105 PRO B O     
4239  C  CB    . PRO B 106 ? 0.2200 0.2862 0.3429 0.0222  -0.0599 0.0579  105 PRO B CB    
4240  C  CG    . PRO B 106 ? 0.2978 0.3674 0.4347 0.0265  -0.0520 0.0591  105 PRO B CG    
4241  C  CD    . PRO B 106 ? 0.2810 0.3429 0.4056 0.0289  -0.0455 0.0541  105 PRO B CD    
4249  N  N     . ASN B 107 ? 0.1683 0.2176 0.2542 0.0157  -0.0644 0.0454  106 ASN B N     
4250  C  CA    . ASN B 107 ? 0.1876 0.2311 0.2586 0.0129  -0.0696 0.0421  106 ASN B CA    
4251  C  C     . ASN B 107 ? 0.2053 0.2417 0.2634 0.0153  -0.0654 0.0369  106 ASN B C     
4252  O  O     . ASN B 107 ? 0.2234 0.2570 0.2707 0.0143  -0.0679 0.0357  106 ASN B O     
4253  C  CB    . ASN B 107 ? 0.1814 0.2288 0.2520 0.0105  -0.0771 0.0469  106 ASN B CB    
4254  C  CG    . ASN B 107 ? 0.1849 0.2399 0.2693 0.0079  -0.0820 0.0521  106 ASN B CG    
4255  O  OD1   . ASN B 107 ? 0.2144 0.2691 0.3008 0.0050  -0.0831 0.0502  106 ASN B OD1   
4256  N  ND2   . ASN B 107 ? 0.2233 0.2856 0.3185 0.0089  -0.0850 0.0589  106 ASN B ND2   
4263  N  N     . THR B 108 ? 0.1741 0.2075 0.2328 0.0177  -0.0590 0.0336  107 THR B N     
4264  C  CA    . THR B 108 ? 0.2051 0.2326 0.2537 0.0200  -0.0549 0.0286  107 THR B CA    
4265  C  C     . THR B 108 ? 0.2003 0.2224 0.2458 0.0198  -0.0531 0.0239  107 THR B C     
4266  O  O     . THR B 108 ? 0.2265 0.2458 0.2698 0.0223  -0.0482 0.0211  107 THR B O     
4267  C  CB    . THR B 108 ? 0.2048 0.2342 0.2570 0.0239  -0.0488 0.0301  107 THR B CB    
4268  O  OG1   . THR B 108 ? 0.2304 0.2625 0.2926 0.0250  -0.0443 0.0314  107 THR B OG1   
4269  C  CG2   . THR B 108 ? 0.2020 0.2357 0.2575 0.0242  -0.0512 0.0354  107 THR B CG2   
4277  N  N     . ASN B 109 ? 0.2053 0.2255 0.2506 0.0164  -0.0577 0.0231  108 ASN B N     
4278  C  CA    . ASN B 109 ? 0.2056 0.2196 0.2480 0.0159  -0.0572 0.0192  108 ASN B CA    
4279  C  C     . ASN B 109 ? 0.2343 0.2417 0.2664 0.0171  -0.0573 0.0133  108 ASN B C     
4280  O  O     . ASN B 109 ? 0.2416 0.2477 0.2671 0.0156  -0.0604 0.0114  108 ASN B O     
4281  C  CB    . ASN B 109 ? 0.2053 0.2184 0.2505 0.0116  -0.0623 0.0202  108 ASN B CB    
4282  C  CG    . ASN B 109 ? 0.2138 0.2343 0.2705 0.0101  -0.0617 0.0257  108 ASN B CG    
4283  O  OD1   . ASN B 109 ? 0.1967 0.2185 0.2586 0.0105  -0.0573 0.0269  108 ASN B OD1   
4284  N  ND2   . ASN B 109 ? 0.1891 0.2152 0.2502 0.0081  -0.0659 0.0292  108 ASN B ND2   
4291  N  N     . GLY B 110 ? 0.2341 0.2372 0.2651 0.0193  -0.0541 0.0103  109 GLY B N     
4292  C  CA    . GLY B 110 ? 0.2040 0.2013 0.2280 0.0209  -0.0535 0.0043  109 GLY B CA    
4293  C  C     . GLY B 110 ? 0.2039 0.1946 0.2291 0.0206  -0.0552 0.0019  109 GLY B C     
4294  O  O     . GLY B 110 ? 0.2285 0.2155 0.2536 0.0177  -0.0597 0.0012  109 GLY B O     
4298  N  N     . SER B 111 ? 0.2181 0.2074 0.2449 0.0233  -0.0521 0.0010  110 SER B N     
4299  C  CA    . SER B 111 ? 0.2114 0.1947 0.2405 0.0230  -0.0541 0.0003  110 SER B CA    
4300  C  C     . SER B 111 ? 0.2334 0.2190 0.2665 0.0226  -0.0520 0.0047  110 SER B C     
4301  O  O     . SER B 111 ? 0.2036 0.1849 0.2385 0.0207  -0.0546 0.0061  110 SER B O     
4302  C  CB    . SER B 111 ? 0.2358 0.2140 0.2635 0.0262  -0.0534 -0.0054 110 SER B CB    
4303  O  OG    . SER B 111 ? 0.2389 0.2209 0.2657 0.0293  -0.0487 -0.0066 110 SER B OG    
4309  N  N     . GLN B 112 ? 0.2152 0.2068 0.2491 0.0237  -0.0474 0.0067  111 GLN B N     
4310  C  CA    . GLN B 112 ? 0.1974 0.1906 0.2337 0.0227  -0.0447 0.0100  111 GLN B CA    
4311  C  C     . GLN B 112 ? 0.1801 0.1747 0.2197 0.0185  -0.0463 0.0141  111 GLN B C     
4312  O  O     . GLN B 112 ? 0.1758 0.1738 0.2179 0.0171  -0.0474 0.0156  111 GLN B O     
4313  C  CB    . GLN B 112 ? 0.1564 0.1552 0.1933 0.0244  -0.0391 0.0109  111 GLN B CB    
4314  C  CG    . GLN B 112 ? 0.1903 0.1879 0.2243 0.0278  -0.0370 0.0074  111 GLN B CG    
4315  C  CD    . GLN B 112 ? 0.1876 0.1895 0.2219 0.0289  -0.0314 0.0083  111 GLN B CD    
4316  O  OE1   . GLN B 112 ? 0.1899 0.1936 0.2259 0.0271  -0.0287 0.0107  111 GLN B OE1   
4317  N  NE2   . GLN B 112 ? 0.2130 0.2162 0.2453 0.0315  -0.0293 0.0060  111 GLN B NE2   
4326  N  N     . PHE B 113 ? 0.1990 0.1915 0.2387 0.0161  -0.0461 0.0163  112 PHE B N     
4327  C  CA    . PHE B 113 ? 0.1827 0.1758 0.2249 0.0113  -0.0473 0.0200  112 PHE B CA    
4328  C  C     . PHE B 113 ? 0.2127 0.2071 0.2537 0.0090  -0.0433 0.0223  112 PHE B C     
4329  O  O     . PHE B 113 ? 0.1882 0.1812 0.2260 0.0109  -0.0416 0.0210  112 PHE B O     
4330  C  CB    . PHE B 113 ? 0.1995 0.1850 0.2406 0.0092  -0.0536 0.0199  112 PHE B CB    
4331  C  CG    . PHE B 113 ? 0.2077 0.1865 0.2460 0.0102  -0.0556 0.0191  112 PHE B CG    
4332  C  CD1   . PHE B 113 ? 0.2079 0.1848 0.2447 0.0066  -0.0559 0.0228  112 PHE B CD1   
4333  C  CD2   . PHE B 113 ? 0.2158 0.1909 0.2533 0.0146  -0.0571 0.0148  112 PHE B CD2   
4334  C  CE1   . PHE B 113 ? 0.2246 0.1961 0.2595 0.0075  -0.0585 0.0230  112 PHE B CE1   
4335  C  CE2   . PHE B 113 ? 0.2401 0.2102 0.2773 0.0161  -0.0591 0.0144  112 PHE B CE2   
4336  C  CZ    . PHE B 113 ? 0.2327 0.2010 0.2687 0.0126  -0.0603 0.0188  112 PHE B CZ    
4346  N  N     . PHE B 114 ? 0.1941 0.1914 0.2375 0.0043  -0.0417 0.0256  113 PHE B N     
4347  C  CA    . PHE B 114 ? 0.1705 0.1677 0.2106 0.0006  -0.0384 0.0277  113 PHE B CA    
4348  C  C     . PHE B 114 ? 0.1952 0.1898 0.2347 -0.0057 -0.0411 0.0313  113 PHE B C     
4349  O  O     . PHE B 114 ? 0.1793 0.1747 0.2230 -0.0076 -0.0437 0.0325  113 PHE B O     
4350  C  CB    . PHE B 114 ? 0.1741 0.1787 0.2169 0.0007  -0.0303 0.0274  113 PHE B CB    
4351  C  CG    . PHE B 114 ? 0.1654 0.1769 0.2165 -0.0005 -0.0276 0.0287  113 PHE B CG    
4352  C  CD1   . PHE B 114 ? 0.1699 0.1846 0.2267 0.0033  -0.0293 0.0280  113 PHE B CD1   
4353  C  CD2   . PHE B 114 ? 0.1664 0.1817 0.2201 -0.0057 -0.0234 0.0308  113 PHE B CD2   
4354  C  CE1   . PHE B 114 ? 0.1596 0.1815 0.2257 0.0024  -0.0275 0.0298  113 PHE B CE1   
4355  C  CE2   . PHE B 114 ? 0.1771 0.1998 0.2406 -0.0065 -0.0207 0.0319  113 PHE B CE2   
4356  C  CZ    . PHE B 114 ? 0.1704 0.1966 0.2410 -0.0023 -0.0231 0.0317  113 PHE B CZ    
4366  N  N     . ILE B 115 ? 0.1827 0.1742 0.2163 -0.0096 -0.0406 0.0334  114 ILE B N     
4367  C  CA    . ILE B 115 ? 0.1910 0.1797 0.2222 -0.0167 -0.0426 0.0375  114 ILE B CA    
4368  C  C     . ILE B 115 ? 0.1920 0.1863 0.2209 -0.0214 -0.0348 0.0385  114 ILE B C     
4369  O  O     . ILE B 115 ? 0.2014 0.1957 0.2249 -0.0212 -0.0315 0.0374  114 ILE B O     
4370  C  CB    . ILE B 115 ? 0.2039 0.1831 0.2292 -0.0183 -0.0496 0.0398  114 ILE B CB    
4371  C  CG1   . ILE B 115 ? 0.2711 0.2445 0.2993 -0.0127 -0.0560 0.0374  114 ILE B CG1   
4372  C  CG2   . ILE B 115 ? 0.2115 0.1873 0.2342 -0.0261 -0.0521 0.0447  114 ILE B CG2   
4373  C  CD1   . ILE B 115 ? 0.2417 0.2068 0.2664 -0.0122 -0.0619 0.0388  114 ILE B CD1   
4385  N  N     . CYS B 116 ? 0.1929 0.1926 0.2266 -0.0254 -0.0312 0.0398  115 CYS B N     
4386  C  CA    . CYS B 116 ? 0.2066 0.2120 0.2389 -0.0303 -0.0226 0.0400  115 CYS B CA    
4387  C  C     . CYS B 116 ? 0.2235 0.2236 0.2445 -0.0380 -0.0234 0.0432  115 CYS B C     
4388  O  O     . CYS B 116 ? 0.2136 0.2075 0.2312 -0.0419 -0.0301 0.0471  115 CYS B O     
4389  C  CB    . CYS B 116 ? 0.1945 0.2074 0.2363 -0.0331 -0.0186 0.0408  115 CYS B CB    
4390  S  SG    . CYS B 116 ? 0.2340 0.2543 0.2896 -0.0252 -0.0179 0.0382  115 CYS B SG    
4396  N  N     . THR B 117 ? 0.2087 0.2112 0.2238 -0.0409 -0.0164 0.0418  116 THR B N     
4397  C  CA    . THR B 117 ? 0.2352 0.2342 0.2386 -0.0498 -0.0157 0.0449  116 THR B CA    
4398  C  C     . THR B 117 ? 0.2618 0.2679 0.2658 -0.0562 -0.0056 0.0439  116 THR B C     
4399  O  O     . THR B 117 ? 0.2653 0.2697 0.2583 -0.0648 -0.0028 0.0457  116 THR B O     
4400  C  CB    . THR B 117 ? 0.2611 0.2561 0.2544 -0.0496 -0.0166 0.0441  116 THR B CB    
4401  O  OG1   . THR B 117 ? 0.2458 0.2463 0.2423 -0.0454 -0.0086 0.0388  116 THR B OG1   
4402  C  CG2   . THR B 117 ? 0.2594 0.2474 0.2534 -0.0436 -0.0270 0.0454  116 THR B CG2   
4410  N  N     . ALA B 118 ? 0.2172 0.2313 0.2344 -0.0527 -0.0003 0.0413  117 ALA B N     
4411  C  CA    . ALA B 118 ? 0.2408 0.2630 0.2630 -0.0577 0.0099  0.0398  117 ALA B CA    
4412  C  C     . ALA B 118 ? 0.2244 0.2540 0.2639 -0.0525 0.0103  0.0391  117 ALA B C     
4413  O  O     . ALA B 118 ? 0.2484 0.2767 0.2936 -0.0451 0.0041  0.0389  117 ALA B O     
4414  C  CB    . ALA B 118 ? 0.2576 0.2831 0.2771 -0.0576 0.0201  0.0348  117 ALA B CB    
4420  N  N     . LYS B 119 ? 0.2407 0.2786 0.2888 -0.0566 0.0181  0.0385  118 LYS B N     
4421  C  CA    . LYS B 119 ? 0.2253 0.2718 0.2916 -0.0519 0.0191  0.0380  118 LYS B CA    
4422  C  C     . LYS B 119 ? 0.2320 0.2823 0.3066 -0.0433 0.0234  0.0338  118 LYS B C     
4423  O  O     . LYS B 119 ? 0.2431 0.2949 0.3155 -0.0438 0.0323  0.0300  118 LYS B O     
4424  C  CB    . LYS B 119 ? 0.2296 0.2849 0.3042 -0.0587 0.0273  0.0382  118 LYS B CB    
4425  C  CG    . LYS B 119 ? 0.2802 0.3464 0.3762 -0.0546 0.0288  0.0380  118 LYS B CG    
4426  C  CD    . LYS B 119 ? 0.3244 0.3999 0.4286 -0.0621 0.0387  0.0374  118 LYS B CD    
4427  C  CE    . LYS B 119 ? 0.4199 0.5071 0.5469 -0.0591 0.0397  0.0381  118 LYS B CE    
4428  N  NZ    . LYS B 119 ? 0.4453 0.5413 0.5794 -0.0674 0.0489  0.0378  118 LYS B NZ    
4442  N  N     . THR B 120 ? 0.2022 0.2535 0.2857 -0.0359 0.0170  0.0344  119 THR B N     
4443  C  CA    . THR B 120 ? 0.1803 0.2343 0.2713 -0.0278 0.0196  0.0315  119 THR B CA    
4444  C  C     . THR B 120 ? 0.2193 0.2823 0.3291 -0.0240 0.0187  0.0328  119 THR B C     
4445  O  O     . THR B 120 ? 0.2021 0.2642 0.3154 -0.0186 0.0113  0.0342  119 THR B O     
4446  C  CB    . THR B 120 ? 0.1947 0.2405 0.2762 -0.0225 0.0122  0.0312  119 THR B CB    
4447  O  OG1   . THR B 120 ? 0.2381 0.2808 0.3194 -0.0214 0.0021  0.0341  119 THR B OG1   
4448  C  CG2   . THR B 120 ? 0.2286 0.2664 0.2935 -0.0260 0.0123  0.0304  119 THR B CG2   
4456  N  N     . GLU B 121 ? 0.2361 0.3079 0.3579 -0.0271 0.0266  0.0323  120 GLU B N     
4457  C  CA    . GLU B 121 ? 0.2403 0.3214 0.3806 -0.0254 0.0246  0.0347  120 GLU B CA    
4458  C  C     . GLU B 121 ? 0.2061 0.2910 0.3587 -0.0168 0.0239  0.0342  120 GLU B C     
4459  O  O     . GLU B 121 ? 0.2027 0.2926 0.3668 -0.0142 0.0177  0.0373  120 GLU B O     
4460  C  CB    . GLU B 121 ? 0.2346 0.3250 0.3859 -0.0311 0.0341  0.0340  120 GLU B CB    
4461  C  CG    . GLU B 121 ? 0.3411 0.4362 0.4997 -0.0294 0.0470  0.0291  120 GLU B CG    
4462  C  CD    . GLU B 121 ? 0.4479 0.5354 0.5878 -0.0339 0.0537  0.0253  120 GLU B CD    
4463  O  OE1   . GLU B 121 ? 0.4739 0.5641 0.6180 -0.0331 0.0648  0.0203  120 GLU B OE1   
4464  O  OE2   . GLU B 121 ? 0.3644 0.4434 0.4859 -0.0386 0.0480  0.0271  120 GLU B OE2   
4471  N  N     . TRP B 122 ? 0.1882 0.2705 0.3381 -0.0127 0.0297  0.0308  121 TRP B N     
4472  C  CA    . TRP B 122 ? 0.2383 0.3234 0.3999 -0.0049 0.0294  0.0308  121 TRP B CA    
4473  C  C     . TRP B 122 ? 0.2326 0.3121 0.3870 -0.0006 0.0183  0.0332  121 TRP B C     
4474  O  O     . TRP B 122 ? 0.2524 0.3342 0.4157 0.0052  0.0160  0.0345  121 TRP B O     
4475  C  CB    . TRP B 122 ? 0.2839 0.3666 0.4436 -0.0025 0.0388  0.0262  121 TRP B CB    
4476  C  CG    . TRP B 122 ? 0.2745 0.3469 0.4139 -0.0031 0.0371  0.0242  121 TRP B CG    
4477  C  CD1   . TRP B 122 ? 0.2236 0.2902 0.3567 0.0022  0.0323  0.0241  121 TRP B CD1   
4478  C  CD2   . TRP B 122 ? 0.2501 0.3170 0.3732 -0.0096 0.0399  0.0222  121 TRP B CD2   
4479  N  NE1   . TRP B 122 ? 0.3061 0.3647 0.4215 -0.0003 0.0320  0.0220  121 TRP B NE1   
4480  C  CE2   . TRP B 122 ? 0.2626 0.3209 0.3713 -0.0075 0.0360  0.0212  121 TRP B CE2   
4481  C  CE3   . TRP B 122 ? 0.2944 0.3630 0.4136 -0.0175 0.0449  0.0216  121 TRP B CE3   
4482  C  CZ2   . TRP B 122 ? 0.2868 0.3384 0.3784 -0.0126 0.0364  0.0198  121 TRP B CZ2   
4483  C  CZ3   . TRP B 122 ? 0.3159 0.3771 0.4163 -0.0232 0.0453  0.0205  121 TRP B CZ3   
4484  C  CH2   . TRP B 122 ? 0.2889 0.3418 0.3761 -0.0205 0.0408  0.0198  121 TRP B CH2   
4495  N  N     . LEU B 123 ? 0.1929 0.2650 0.3320 -0.0035 0.0116  0.0339  122 LEU B N     
4496  C  CA    . LEU B 123 ? 0.1922 0.2590 0.3243 -0.0003 0.0015  0.0355  122 LEU B CA    
4497  C  C     . LEU B 123 ? 0.1794 0.2505 0.3191 -0.0019 -0.0062 0.0392  122 LEU B C     
4498  O  O     . LEU B 123 ? 0.1844 0.2527 0.3207 0.0006  -0.0143 0.0404  122 LEU B O     
4499  C  CB    . LEU B 123 ? 0.1723 0.2289 0.2858 -0.0023 -0.0014 0.0339  122 LEU B CB    
4500  C  CG    . LEU B 123 ? 0.1936 0.2461 0.2992 -0.0008 0.0051  0.0304  122 LEU B CG    
4501  C  CD1   . LEU B 123 ? 0.2037 0.2471 0.2931 -0.0028 0.0006  0.0298  122 LEU B CD1   
4502  C  CD2   . LEU B 123 ? 0.2176 0.2709 0.3278 0.0059  0.0065  0.0294  122 LEU B CD2   
4514  N  N     . ASP B 124 ? 0.2159 0.2942 0.3661 -0.0064 -0.0037 0.0407  123 ASP B N     
4515  C  CA    . ASP B 124 ? 0.1860 0.2689 0.3443 -0.0085 -0.0111 0.0443  123 ASP B CA    
4516  C  C     . ASP B 124 ? 0.2037 0.2923 0.3739 -0.0032 -0.0154 0.0466  123 ASP B C     
4517  O  O     . ASP B 124 ? 0.1722 0.2663 0.3541 0.0010  -0.0100 0.0465  123 ASP B O     
4518  C  CB    . ASP B 124 ? 0.1948 0.2865 0.3654 -0.0141 -0.0061 0.0455  123 ASP B CB    
4519  C  CG    . ASP B 124 ? 0.2283 0.3143 0.3862 -0.0210 -0.0035 0.0445  123 ASP B CG    
4520  O  OD1   . ASP B 124 ? 0.2000 0.2755 0.3411 -0.0214 -0.0071 0.0434  123 ASP B OD1   
4521  O  OD2   . ASP B 124 ? 0.2124 0.3049 0.3781 -0.0264 0.0020  0.0450  123 ASP B OD2   
4526  N  N     . GLY B 125 ? 0.1976 0.2842 0.3643 -0.0037 -0.0256 0.0488  124 GLY B N     
4527  C  CA    . GLY B 125 ? 0.2323 0.3231 0.4068 0.0002  -0.0315 0.0516  124 GLY B CA    
4528  C  C     . GLY B 125 ? 0.2129 0.2975 0.3781 0.0057  -0.0323 0.0502  124 GLY B C     
4529  O  O     . GLY B 125 ? 0.2053 0.2923 0.3744 0.0085  -0.0379 0.0530  124 GLY B O     
4533  N  N     . LYS B 126 ? 0.1927 0.2693 0.3448 0.0068  -0.0276 0.0464  125 LYS B N     
4534  C  CA    . LYS B 126 ? 0.1990 0.2693 0.3411 0.0113  -0.0281 0.0447  125 LYS B CA    
4535  C  C     . LYS B 126 ? 0.1996 0.2599 0.3236 0.0101  -0.0323 0.0418  125 LYS B C     
4536  O  O     . LYS B 126 ? 0.1938 0.2499 0.3100 0.0129  -0.0358 0.0410  125 LYS B O     
4537  C  CB    . LYS B 126 ? 0.2284 0.2988 0.3730 0.0143  -0.0183 0.0423  125 LYS B CB    
4538  C  CG    . LYS B 126 ? 0.3451 0.4242 0.5089 0.0177  -0.0143 0.0448  125 LYS B CG    
4539  C  CD    . LYS B 126 ? 0.3461 0.4318 0.5221 0.0152  -0.0061 0.0439  125 LYS B CD    
4540  C  CE    . LYS B 126 ? 0.4536 0.5484 0.6516 0.0189  -0.0012 0.0458  125 LYS B CE    
4541  N  NZ    . LYS B 126 ? 0.4550 0.5595 0.6705 0.0186  -0.0071 0.0509  125 LYS B NZ    
4555  N  N     . HIS B 127 ? 0.1492 0.2056 0.2669 0.0059  -0.0322 0.0404  126 HIS B N     
4556  C  CA    . HIS B 127 ? 0.1524 0.1991 0.2553 0.0049  -0.0362 0.0378  126 HIS B CA    
4557  C  C     . HIS B 127 ? 0.1778 0.2233 0.2806 -0.0001 -0.0424 0.0391  126 HIS B C     
4558  O  O     . HIS B 127 ? 0.1925 0.2427 0.3029 -0.0042 -0.0404 0.0411  126 HIS B O     
4559  C  CB    . HIS B 127 ? 0.1701 0.2118 0.2653 0.0045  -0.0302 0.0352  126 HIS B CB    
4560  C  CG    . HIS B 127 ? 0.1718 0.2139 0.2665 0.0090  -0.0245 0.0336  126 HIS B CG    
4561  N  ND1   . HIS B 127 ? 0.1635 0.1997 0.2486 0.0123  -0.0258 0.0311  126 HIS B ND1   
4562  C  CD2   . HIS B 127 ? 0.1479 0.1956 0.2514 0.0108  -0.0174 0.0338  126 HIS B CD2   
4563  C  CE1   . HIS B 127 ? 0.1570 0.1952 0.2445 0.0156  -0.0203 0.0303  126 HIS B CE1   
4564  N  NE2   . HIS B 127 ? 0.1590 0.2035 0.2573 0.0148  -0.0150 0.0317  126 HIS B NE2   
4573  N  N     . VAL B 128 ? 0.1746 0.2138 0.2688 -0.0001 -0.0492 0.0375  127 VAL B N     
4574  C  CA    . VAL B 128 ? 0.1892 0.2253 0.2819 -0.0049 -0.0556 0.0381  127 VAL B CA    
4575  C  C     . VAL B 128 ? 0.1711 0.1996 0.2569 -0.0079 -0.0547 0.0369  127 VAL B C     
4576  O  O     . VAL B 128 ? 0.1879 0.2080 0.2641 -0.0059 -0.0555 0.0340  127 VAL B O     
4577  C  CB    . VAL B 128 ? 0.1736 0.2050 0.2592 -0.0043 -0.0628 0.0360  127 VAL B CB    
4578  C  CG1   . VAL B 128 ? 0.2013 0.2284 0.2853 -0.0098 -0.0690 0.0360  127 VAL B CG1   
4579  C  CG2   . VAL B 128 ? 0.1854 0.2244 0.2771 -0.0026 -0.0648 0.0384  127 VAL B CG2   
4589  N  N     . VAL B 129 ? 0.1893 0.2207 0.2806 -0.0130 -0.0537 0.0395  128 VAL B N     
4590  C  CA    . VAL B 129 ? 0.2201 0.2441 0.3052 -0.0173 -0.0544 0.0397  128 VAL B CA    
4591  C  C     . VAL B 129 ? 0.2197 0.2362 0.3008 -0.0200 -0.0627 0.0390  128 VAL B C     
4592  O  O     . VAL B 129 ? 0.2217 0.2425 0.3087 -0.0226 -0.0666 0.0404  128 VAL B O     
4593  C  CB    . VAL B 129 ? 0.2006 0.2310 0.2929 -0.0226 -0.0496 0.0430  128 VAL B CB    
4594  C  CG1   . VAL B 129 ? 0.1945 0.2170 0.2799 -0.0282 -0.0516 0.0443  128 VAL B CG1   
4595  C  CG2   . VAL B 129 ? 0.2220 0.2587 0.3177 -0.0201 -0.0405 0.0425  128 VAL B CG2   
4605  N  N     . PHE B 130 ? 0.2025 0.2080 0.2743 -0.0197 -0.0654 0.0370  129 PHE B N     
4606  C  CA    . PHE B 130 ? 0.2209 0.2177 0.2888 -0.0215 -0.0728 0.0352  129 PHE B CA    
4607  C  C     . PHE B 130 ? 0.2377 0.2237 0.3003 -0.0244 -0.0753 0.0358  129 PHE B C     
4608  O  O     . PHE B 130 ? 0.2543 0.2313 0.3138 -0.0254 -0.0811 0.0337  129 PHE B O     
4609  C  CB    . PHE B 130 ? 0.2444 0.2375 0.3069 -0.0161 -0.0749 0.0304  129 PHE B CB    
4610  C  CG    . PHE B 130 ? 0.2084 0.1961 0.2648 -0.0112 -0.0722 0.0277  129 PHE B CG    
4611  C  CD1   . PHE B 130 ? 0.1889 0.1828 0.2458 -0.0070 -0.0663 0.0276  129 PHE B CD1   
4612  C  CD2   . PHE B 130 ? 0.2028 0.1796 0.2540 -0.0106 -0.0754 0.0253  129 PHE B CD2   
4613  C  CE1   . PHE B 130 ? 0.1898 0.1795 0.2417 -0.0029 -0.0639 0.0253  129 PHE B CE1   
4614  C  CE2   . PHE B 130 ? 0.2267 0.1996 0.2739 -0.0059 -0.0732 0.0230  129 PHE B CE2   
4615  C  CZ    . PHE B 130 ? 0.2153 0.1950 0.2626 -0.0023 -0.0675 0.0230  129 PHE B CZ    
4625  N  N     . GLY B 131 ? 0.2504 0.2366 0.3118 -0.0261 -0.0713 0.0386  130 GLY B N     
4626  C  CA    . GLY B 131 ? 0.2364 0.2119 0.2926 -0.0292 -0.0747 0.0402  130 GLY B CA    
4627  C  C     . GLY B 131 ? 0.2265 0.2042 0.2808 -0.0329 -0.0701 0.0443  130 GLY B C     
4628  O  O     . GLY B 131 ? 0.2326 0.2200 0.2898 -0.0332 -0.0634 0.0451  130 GLY B O     
4632  N  N     . LYS B 132 ? 0.2426 0.2105 0.2917 -0.0361 -0.0738 0.0467  131 LYS B N     
4633  C  CA    . LYS B 132 ? 0.2483 0.2169 0.2930 -0.0408 -0.0703 0.0510  131 LYS B CA    
4634  C  C     . LYS B 132 ? 0.3014 0.2577 0.3396 -0.0411 -0.0758 0.0528  131 LYS B C     
4635  O  O     . LYS B 132 ? 0.3071 0.2538 0.3459 -0.0405 -0.0827 0.0523  131 LYS B O     
4636  C  CB    . LYS B 132 ? 0.3224 0.2953 0.3700 -0.0493 -0.0686 0.0552  131 LYS B CB    
4637  C  CG    . LYS B 132 ? 0.3736 0.3494 0.4161 -0.0550 -0.0629 0.0589  131 LYS B CG    
4638  C  CD    . LYS B 132 ? 0.4405 0.4295 0.4895 -0.0585 -0.0546 0.0591  131 LYS B CD    
4639  C  CE    . LYS B 132 ? 0.4433 0.4346 0.4855 -0.0648 -0.0479 0.0618  131 LYS B CE    
4640  N  NZ    . LYS B 132 ? 0.5487 0.5365 0.5875 -0.0748 -0.0497 0.0671  131 LYS B NZ    
4654  N  N     . VAL B 133 ? 0.2664 0.2231 0.2987 -0.0422 -0.0729 0.0549  132 VAL B N     
4655  C  CA    . VAL B 133 ? 0.3008 0.2467 0.3274 -0.0436 -0.0787 0.0583  132 VAL B CA    
4656  C  C     . VAL B 133 ? 0.3060 0.2448 0.3313 -0.0515 -0.0836 0.0637  132 VAL B C     
4657  O  O     . VAL B 133 ? 0.3306 0.2748 0.3549 -0.0587 -0.0798 0.0669  132 VAL B O     
4658  C  CB    . VAL B 133 ? 0.2863 0.2349 0.3057 -0.0451 -0.0747 0.0602  132 VAL B CB    
4659  C  CG1   . VAL B 133 ? 0.3027 0.2403 0.3162 -0.0484 -0.0820 0.0656  132 VAL B CG1   
4660  C  CG2   . VAL B 133 ? 0.2638 0.2173 0.2844 -0.0371 -0.0711 0.0550  132 VAL B CG2   
4670  N  N     . LYS B 134 ? 0.3360 0.2626 0.3619 -0.0502 -0.0920 0.0647  133 LYS B N     
4671  C  CA    . LYS B 134 ? 0.3606 0.2773 0.3853 -0.0572 -0.0983 0.0703  133 LYS B CA    
4672  C  C     . LYS B 134 ? 0.4262 0.3355 0.4436 -0.0613 -0.1022 0.0769  133 LYS B C     
4673  O  O     . LYS B 134 ? 0.4444 0.3541 0.4556 -0.0703 -0.1012 0.0830  133 LYS B O     
4674  C  CB    . LYS B 134 ? 0.4058 0.3125 0.4365 -0.0528 -0.1051 0.0667  133 LYS B CB    
4675  C  CG    . LYS B 134 ? 0.4966 0.3924 0.5279 -0.0595 -0.1117 0.0713  133 LYS B CG    
4676  C  CD    . LYS B 134 ? 0.5562 0.4455 0.5940 -0.0556 -0.1159 0.0656  133 LYS B CD    
4677  C  CE    . LYS B 134 ? 0.6590 0.5314 0.6982 -0.0571 -0.1247 0.0684  133 LYS B CE    
4678  N  NZ    . LYS B 134 ? 0.6785 0.5464 0.7204 -0.0629 -0.1276 0.0685  133 LYS B NZ    
4692  N  N     . GLU B 135 ? 0.3942 0.2972 0.4122 -0.0552 -0.1067 0.0760  134 GLU B N     
4693  C  CA    . GLU B 135 ? 0.4287 0.3257 0.4404 -0.0585 -0.1112 0.0825  134 GLU B CA    
4694  C  C     . GLU B 135 ? 0.3536 0.2568 0.3636 -0.0528 -0.1079 0.0796  134 GLU B C     
4695  O  O     . GLU B 135 ? 0.3832 0.2916 0.3985 -0.0447 -0.1044 0.0724  134 GLU B O     
4696  C  CB    . GLU B 135 ? 0.4935 0.3754 0.5094 -0.0572 -0.1217 0.0858  134 GLU B CB    
4697  C  CG    . GLU B 135 ? 0.5698 0.4439 0.5879 -0.0627 -0.1257 0.0884  134 GLU B CG    
4698  C  CD    . GLU B 135 ? 0.6344 0.5021 0.6446 -0.0734 -0.1300 0.0986  134 GLU B CD    
4699  O  OE1   . GLU B 135 ? 0.6694 0.5447 0.6728 -0.0817 -0.1242 0.1014  134 GLU B OE1   
4700  O  OE2   . GLU B 135 ? 0.7472 0.6027 0.7582 -0.0736 -0.1390 0.1040  134 GLU B OE2   
4707  N  N     . GLY B 136 ? 0.3335 0.2361 0.3349 -0.0580 -0.1089 0.0854  135 GLY B N     
4708  C  CA    . GLY B 136 ? 0.3556 0.2628 0.3548 -0.0538 -0.1071 0.0835  135 GLY B CA    
4709  C  C     . GLY B 136 ? 0.3250 0.2449 0.3198 -0.0544 -0.0964 0.0793  135 GLY B C     
4710  O  O     . GLY B 136 ? 0.3124 0.2374 0.3082 -0.0487 -0.0934 0.0751  135 GLY B O     
4714  N  N     . MET B 137 ? 0.3162 0.2418 0.3069 -0.0614 -0.0901 0.0803  136 MET B N     
4715  C  CA    . MET B 137 ? 0.3262 0.2633 0.3137 -0.0616 -0.0797 0.0762  136 MET B CA    
4716  C  C     . MET B 137 ? 0.2990 0.2365 0.2766 -0.0646 -0.0792 0.0785  136 MET B C     
4717  O  O     . MET B 137 ? 0.2869 0.2318 0.2638 -0.0612 -0.0725 0.0736  136 MET B O     
4718  C  CB    . MET B 137 ? 0.3446 0.2882 0.3310 -0.0687 -0.0725 0.0768  136 MET B CB    
4719  C  CG    . MET B 137 ? 0.3626 0.3176 0.3463 -0.0695 -0.0612 0.0727  136 MET B CG    
4720  S  SD    . MET B 137 ? 0.2988 0.2621 0.2960 -0.0578 -0.0564 0.0641  136 MET B SD    
4721  C  CE    . MET B 137 ? 0.2893 0.2613 0.2815 -0.0575 -0.0461 0.0602  136 MET B CE    
4731  N  N     . ASN B 138 ? 0.3249 0.2541 0.2949 -0.0709 -0.0869 0.0859  137 ASN B N     
4732  C  CA    . ASN B 138 ? 0.3360 0.2659 0.2956 -0.0745 -0.0871 0.0883  137 ASN B CA    
4733  C  C     . ASN B 138 ? 0.3143 0.2448 0.2799 -0.0649 -0.0897 0.0843  137 ASN B C     
4734  O  O     . ASN B 138 ? 0.3133 0.2476 0.2724 -0.0662 -0.0872 0.0835  137 ASN B O     
4735  C  CB    . ASN B 138 ? 0.3602 0.2811 0.3096 -0.0841 -0.0956 0.0981  137 ASN B CB    
4736  C  CG    . ASN B 138 ? 0.4183 0.3278 0.3754 -0.0813 -0.1074 0.1029  137 ASN B CG    
4737  O  OD1   . ASN B 138 ? 0.3837 0.2914 0.3536 -0.0716 -0.1098 0.0985  137 ASN B OD1   
4738  N  ND2   . ASN B 138 ? 0.4246 0.3258 0.3735 -0.0903 -0.1149 0.1123  137 ASN B ND2   
4745  N  N     . ILE B 139 ? 0.3071 0.2344 0.2851 -0.0557 -0.0940 0.0812  138 ILE B N     
4746  C  CA    . ILE B 139 ? 0.2853 0.2146 0.2703 -0.0464 -0.0950 0.0763  138 ILE B CA    
4747  C  C     . ILE B 139 ? 0.2814 0.2213 0.2668 -0.0428 -0.0842 0.0690  138 ILE B C     
4748  O  O     . ILE B 139 ? 0.2892 0.2332 0.2734 -0.0399 -0.0820 0.0663  138 ILE B O     
4749  C  CB    . ILE B 139 ? 0.3470 0.2702 0.3448 -0.0382 -0.1009 0.0740  138 ILE B CB    
4750  C  CG1   . ILE B 139 ? 0.3456 0.2571 0.3445 -0.0417 -0.1114 0.0813  138 ILE B CG1   
4751  C  CG2   . ILE B 139 ? 0.3602 0.2857 0.3656 -0.0291 -0.1014 0.0689  138 ILE B CG2   
4752  C  CD1   . ILE B 139 ? 0.3950 0.3027 0.3898 -0.0445 -0.1184 0.0876  138 ILE B CD1   
4764  N  N     . VAL B 140 ? 0.2650 0.2092 0.2535 -0.0425 -0.0779 0.0657  139 VAL B N     
4765  C  CA    . VAL B 140 ? 0.2421 0.1960 0.2319 -0.0394 -0.0680 0.0595  139 VAL B CA    
4766  C  C     . VAL B 140 ? 0.2479 0.2064 0.2273 -0.0460 -0.0617 0.0602  139 VAL B C     
4767  O  O     . VAL B 140 ? 0.2557 0.2195 0.2347 -0.0427 -0.0563 0.0559  139 VAL B O     
4768  C  CB    . VAL B 140 ? 0.2554 0.2130 0.2511 -0.0392 -0.0637 0.0574  139 VAL B CB    
4769  C  CG1   . VAL B 140 ? 0.2509 0.2182 0.2496 -0.0355 -0.0541 0.0516  139 VAL B CG1   
4770  C  CG2   . VAL B 140 ? 0.2674 0.2191 0.2717 -0.0336 -0.0705 0.0564  139 VAL B CG2   
4780  N  N     . GLU B 141 ? 0.2750 0.2314 0.2454 -0.0557 -0.0618 0.0654  140 GLU B N     
4781  C  CA    . GLU B 141 ? 0.2649 0.2246 0.2233 -0.0634 -0.0560 0.0661  140 GLU B CA    
4782  C  C     . GLU B 141 ? 0.2755 0.2330 0.2289 -0.0622 -0.0606 0.0668  140 GLU B C     
4783  O  O     . GLU B 141 ? 0.2849 0.2475 0.2346 -0.0620 -0.0543 0.0627  140 GLU B O     
4784  C  CB    . GLU B 141 ? 0.2846 0.2409 0.2329 -0.0749 -0.0572 0.0725  140 GLU B CB    
4785  C  CG    . GLU B 141 ? 0.2949 0.2544 0.2488 -0.0770 -0.0523 0.0719  140 GLU B CG    
4786  C  CD    . GLU B 141 ? 0.3850 0.3407 0.3304 -0.0883 -0.0539 0.0785  140 GLU B CD    
4787  O  OE1   . GLU B 141 ? 0.4413 0.3908 0.3749 -0.0955 -0.0595 0.0846  140 GLU B OE1   
4788  O  OE2   . GLU B 141 ? 0.4229 0.3816 0.3736 -0.0905 -0.0502 0.0783  140 GLU B OE2   
4795  N  N     . ALA B 142 ? 0.2851 0.2351 0.2403 -0.0609 -0.0718 0.0718  141 ALA B N     
4796  C  CA    . ALA B 142 ? 0.3078 0.2562 0.2613 -0.0590 -0.0774 0.0729  141 ALA B CA    
4797  C  C     . ALA B 142 ? 0.2845 0.2388 0.2461 -0.0497 -0.0729 0.0655  141 ALA B C     
4798  O  O     . ALA B 142 ? 0.3043 0.2607 0.2615 -0.0502 -0.0728 0.0646  141 ALA B O     
4799  C  CB    . ALA B 142 ? 0.3336 0.2732 0.2922 -0.0573 -0.0903 0.0791  141 ALA B CB    
4805  N  N     . MET B 143 ? 0.2810 0.2380 0.2533 -0.0418 -0.0691 0.0602  142 MET B N     
4806  C  CA    . MET B 143 ? 0.2584 0.2205 0.2378 -0.0334 -0.0651 0.0537  142 MET B CA    
4807  C  C     . MET B 143 ? 0.2789 0.2478 0.2522 -0.0358 -0.0548 0.0495  142 MET B C     
4808  O  O     . MET B 143 ? 0.2508 0.2230 0.2258 -0.0317 -0.0524 0.0457  142 MET B O     
4809  C  CB    . MET B 143 ? 0.2678 0.2305 0.2583 -0.0257 -0.0640 0.0497  142 MET B CB    
4810  C  CG    . MET B 143 ? 0.2679 0.2243 0.2668 -0.0205 -0.0731 0.0509  142 MET B CG    
4811  S  SD    . MET B 143 ? 0.3768 0.3309 0.3844 -0.0161 -0.0734 0.0482  142 MET B SD    
4812  C  CE    . MET B 143 ? 0.2856 0.2481 0.2970 -0.0095 -0.0651 0.0408  142 MET B CE    
4822  N  N     . GLU B 144 ? 0.3235 0.2946 0.2902 -0.0427 -0.0484 0.0500  143 GLU B N     
4823  C  CA    . GLU B 144 ? 0.3062 0.2831 0.2678 -0.0453 -0.0379 0.0456  143 GLU B CA    
4824  C  C     . GLU B 144 ? 0.3513 0.3276 0.3030 -0.0496 -0.0386 0.0460  143 GLU B C     
4825  O  O     . GLU B 144 ? 0.3827 0.3631 0.3324 -0.0492 -0.0310 0.0410  143 GLU B O     
4826  C  CB    . GLU B 144 ? 0.3430 0.3219 0.2991 -0.0531 -0.0310 0.0464  143 GLU B CB    
4827  C  CG    . GLU B 144 ? 0.2733 0.2553 0.2401 -0.0491 -0.0278 0.0447  143 GLU B CG    
4828  C  CD    . GLU B 144 ? 0.3432 0.3298 0.3077 -0.0556 -0.0185 0.0438  143 GLU B CD    
4829  O  OE1   . GLU B 144 ? 0.3624 0.3468 0.3162 -0.0649 -0.0184 0.0472  143 GLU B OE1   
4830  O  OE2   . GLU B 144 ? 0.3153 0.3080 0.2892 -0.0516 -0.0113 0.0397  143 GLU B OE2   
4837  N  N     . ARG B 145 ? 0.3335 0.3045 0.2787 -0.0544 -0.0478 0.0520  144 ARG B N     
4838  C  CA    . ARG B 145 ? 0.4162 0.3868 0.3518 -0.0592 -0.0501 0.0531  144 ARG B CA    
4839  C  C     . ARG B 145 ? 0.3678 0.3417 0.3108 -0.0513 -0.0493 0.0482  144 ARG B C     
4840  O  O     . ARG B 145 ? 0.4057 0.3810 0.3414 -0.0548 -0.0479 0.0469  144 ARG B O     
4841  C  CB    . ARG B 145 ? 0.4372 0.4014 0.3677 -0.0642 -0.0624 0.0615  144 ARG B CB    
4842  C  CG    . ARG B 145 ? 0.5226 0.4824 0.4459 -0.0722 -0.0644 0.0673  144 ARG B CG    
4843  C  CD    . ARG B 145 ? 0.5580 0.5104 0.4776 -0.0766 -0.0779 0.0766  144 ARG B CD    
4844  N  NE    . ARG B 145 ? 0.5605 0.5096 0.4949 -0.0671 -0.0873 0.0782  144 ARG B NE    
4845  C  CZ    . ARG B 145 ? 0.6196 0.5618 0.5550 -0.0690 -0.0996 0.0862  144 ARG B CZ    
4846  N  NH1   . ARG B 145 ? 0.5791 0.5167 0.5011 -0.0801 -0.1044 0.0940  144 ARG B NH1   
4847  N  NH2   . ARG B 145 ? 0.5205 0.4601 0.4710 -0.0597 -0.1070 0.0864  144 ARG B NH2   
4861  N  N     . PHE B 146 ? 0.3453 0.3204 0.3019 -0.0412 -0.0501 0.0454  145 PHE B N     
4862  C  CA    . PHE B 146 ? 0.3235 0.3016 0.2875 -0.0339 -0.0498 0.0412  145 PHE B CA    
4863  C  C     . PHE B 146 ? 0.2910 0.2741 0.2601 -0.0287 -0.0398 0.0345  145 PHE B C     
4864  O  O     . PHE B 146 ? 0.2794 0.2650 0.2554 -0.0222 -0.0389 0.0309  145 PHE B O     
4865  C  CB    . PHE B 146 ? 0.3103 0.2856 0.2855 -0.0270 -0.0589 0.0432  145 PHE B CB    
4866  C  CG    . PHE B 146 ? 0.3638 0.3337 0.3361 -0.0315 -0.0694 0.0504  145 PHE B CG    
4867  C  CD1   . PHE B 146 ? 0.4122 0.3821 0.3779 -0.0365 -0.0741 0.0535  145 PHE B CD1   
4868  C  CD2   . PHE B 146 ? 0.3355 0.2999 0.3108 -0.0317 -0.0751 0.0546  145 PHE B CD2   
4869  C  CE1   . PHE B 146 ? 0.4321 0.3967 0.3951 -0.0412 -0.0850 0.0613  145 PHE B CE1   
4870  C  CE2   . PHE B 146 ? 0.4074 0.3659 0.3802 -0.0361 -0.0855 0.0621  145 PHE B CE2   
4871  C  CZ    . PHE B 146 ? 0.3855 0.3442 0.3523 -0.0408 -0.0907 0.0657  145 PHE B CZ    
4881  N  N     . GLY B 147 ? 0.3191 0.3038 0.2858 -0.0315 -0.0321 0.0330  146 GLY B N     
4882  C  CA    . GLY B 147 ? 0.2968 0.2860 0.2690 -0.0270 -0.0229 0.0274  146 GLY B CA    
4883  C  C     . GLY B 147 ? 0.3089 0.3002 0.2736 -0.0316 -0.0147 0.0239  146 GLY B C     
4884  O  O     . GLY B 147 ? 0.3152 0.3048 0.2697 -0.0381 -0.0164 0.0251  146 GLY B O     
4888  N  N     . SER B 148 ? 0.2466 0.2414 0.2166 -0.0284 -0.0057 0.0194  147 SER B N     
4889  C  CA    . SER B 148 ? 0.2930 0.2894 0.2588 -0.0311 0.0033  0.0148  147 SER B CA    
4890  C  C     . SER B 148 ? 0.2635 0.2634 0.2375 -0.0282 0.0123  0.0116  147 SER B C     
4891  O  O     . SER B 148 ? 0.2633 0.2648 0.2464 -0.0235 0.0107  0.0130  147 SER B O     
4892  C  CB    . SER B 148 ? 0.2860 0.2826 0.2532 -0.0271 0.0024  0.0122  147 SER B CB    
4893  O  OG    . SER B 148 ? 0.2801 0.2790 0.2587 -0.0183 0.0035  0.0102  147 SER B OG    
4899  N  N     . ARG B 149 ? 0.2689 0.2697 0.2406 -0.0304 0.0215  0.0069  148 ARG B N     
4900  C  CA    . ARG B 149 ? 0.2891 0.2932 0.2699 -0.0278 0.0307  0.0037  148 ARG B CA    
4901  C  C     . ARG B 149 ? 0.2759 0.2822 0.2701 -0.0182 0.0293  0.0037  148 ARG B C     
4902  O  O     . ARG B 149 ? 0.2864 0.2959 0.2902 -0.0153 0.0315  0.0043  148 ARG B O     
4903  C  CB    . ARG B 149 ? 0.3481 0.3517 0.3247 -0.0314 0.0407  -0.0020 148 ARG B CB    
4904  C  CG    . ARG B 149 ? 0.3459 0.3527 0.3344 -0.0277 0.0504  -0.0056 148 ARG B CG    
4905  C  CD    . ARG B 149 ? 0.4170 0.4222 0.4003 -0.0327 0.0613  -0.0120 148 ARG B CD    
4906  N  NE    . ARG B 149 ? 0.3828 0.3908 0.3798 -0.0286 0.0708  -0.0155 148 ARG B NE    
4907  C  CZ    . ARG B 149 ? 0.3969 0.4046 0.4039 -0.0219 0.0736  -0.0178 148 ARG B CZ    
4908  N  NH1   . ARG B 149 ? 0.4445 0.4492 0.4483 -0.0190 0.0688  -0.0174 148 ARG B NH1   
4909  N  NH2   . ARG B 149 ? 0.4595 0.4698 0.4804 -0.0182 0.0816  -0.0203 148 ARG B NH2   
4923  N  N     . ASN B 150 ? 0.2652 0.2703 0.2602 -0.0136 0.0258  0.0030  149 ASN B N     
4924  C  CA    . ASN B 150 ? 0.2553 0.2622 0.2612 -0.0054 0.0244  0.0032  149 ASN B CA    
4925  C  C     . ASN B 150 ? 0.2318 0.2383 0.2395 -0.0019 0.0149  0.0067  149 ASN B C     
4926  O  O     . ASN B 150 ? 0.2245 0.2323 0.2392 0.0041  0.0132  0.0068  149 ASN B O     
4927  C  CB    . ASN B 150 ? 0.2752 0.2813 0.2821 -0.0023 0.0276  0.0000  149 ASN B CB    
4928  C  CG    . ASN B 150 ? 0.2945 0.2989 0.2963 -0.0017 0.0210  0.0006  149 ASN B CG    
4929  O  OD1   . ASN B 150 ? 0.2796 0.2828 0.2758 -0.0047 0.0145  0.0031  149 ASN B OD1   
4930  N  ND2   . ASN B 150 ? 0.2801 0.2845 0.2847 0.0020  0.0225  -0.0014 149 ASN B ND2   
4937  N  N     . GLY B 151 ? 0.2329 0.2373 0.2344 -0.0059 0.0089  0.0095  150 GLY B N     
4938  C  CA    . GLY B 151 ? 0.1940 0.1972 0.1980 -0.0033 0.0004  0.0126  150 GLY B CA    
4939  C  C     . GLY B 151 ? 0.2100 0.2109 0.2118 -0.0014 -0.0062 0.0130  150 GLY B C     
4940  O  O     . GLY B 151 ? 0.2301 0.2289 0.2332 -0.0002 -0.0134 0.0154  150 GLY B O     
4944  N  N     . LYS B 152 ? 0.2207 0.2221 0.2202 -0.0011 -0.0038 0.0105  151 LYS B N     
4945  C  CA    . LYS B 152 ? 0.2526 0.2529 0.2514 0.0003  -0.0099 0.0108  151 LYS B CA    
4946  C  C     . LYS B 152 ? 0.2439 0.2413 0.2370 -0.0048 -0.0168 0.0147  151 LYS B C     
4947  O  O     . LYS B 152 ? 0.2581 0.2543 0.2432 -0.0117 -0.0150 0.0161  151 LYS B O     
4948  C  CB    . LYS B 152 ? 0.2930 0.2946 0.2896 -0.0001 -0.0058 0.0077  151 LYS B CB    
4949  C  CG    . LYS B 152 ? 0.3802 0.3838 0.3820 0.0043  0.0011  0.0044  151 LYS B CG    
4950  C  CD    . LYS B 152 ? 0.4457 0.4508 0.4551 0.0114  -0.0011 0.0040  151 LYS B CD    
4951  C  CE    . LYS B 152 ? 0.4995 0.5060 0.5115 0.0144  0.0043  0.0011  151 LYS B CE    
4952  N  NZ    . LYS B 152 ? 0.4962 0.5035 0.5129 0.0171  0.0096  0.0009  151 LYS B NZ    
4966  N  N     . THR B 153 ? 0.2274 0.2234 0.2247 -0.0017 -0.0245 0.0165  152 THR B N     
4967  C  CA    . THR B 153 ? 0.2108 0.2034 0.2045 -0.0058 -0.0324 0.0210  152 THR B CA    
4968  C  C     . THR B 153 ? 0.2749 0.2680 0.2664 -0.0077 -0.0363 0.0216  152 THR B C     
4969  O  O     . THR B 153 ? 0.2875 0.2835 0.2834 -0.0037 -0.0345 0.0183  152 THR B O     
4970  C  CB    . THR B 153 ? 0.2770 0.2668 0.2778 -0.0016 -0.0392 0.0229  152 THR B CB    
4971  O  OG1   . THR B 153 ? 0.2741 0.2653 0.2835 0.0053  -0.0411 0.0201  152 THR B OG1   
4972  C  CG2   . THR B 153 ? 0.2582 0.2480 0.2613 -0.0003 -0.0356 0.0224  152 THR B CG2   
4980  N  N     . SER B 154 ? 0.2631 0.2534 0.2478 -0.0141 -0.0419 0.0261  153 SER B N     
4981  C  CA    . SER B 154 ? 0.3245 0.3154 0.3059 -0.0176 -0.0469 0.0279  153 SER B CA    
4982  C  C     . SER B 154 ? 0.4059 0.3953 0.3959 -0.0141 -0.0574 0.0315  153 SER B C     
4983  O  O     . SER B 154 ? 0.3819 0.3731 0.3737 -0.0149 -0.0623 0.0327  153 SER B O     
4984  C  CB    . SER B 154 ? 0.2982 0.2870 0.2653 -0.0280 -0.0471 0.0311  153 SER B CB    
4985  O  OG    . SER B 154 ? 0.3109 0.2955 0.2742 -0.0319 -0.0514 0.0361  153 SER B OG    
4991  N  N     . LYS B 155 ? 0.3285 0.3149 0.3254 -0.0099 -0.0607 0.0329  154 LYS B N     
4992  C  CA    . LYS B 155 ? 0.3480 0.3324 0.3559 -0.0050 -0.0695 0.0351  154 LYS B CA    
4993  C  C     . LYS B 155 ? 0.3537 0.3376 0.3706 0.0026  -0.0667 0.0311  154 LYS B C     
4994  O  O     . LYS B 155 ? 0.3249 0.3090 0.3384 0.0027  -0.0603 0.0288  154 LYS B O     
4995  C  CB    . LYS B 155 ? 0.3729 0.3514 0.3776 -0.0102 -0.0788 0.0426  154 LYS B CB    
4996  C  CG    . LYS B 155 ? 0.3793 0.3579 0.3732 -0.0190 -0.0829 0.0474  154 LYS B CG    
4997  C  CD    . LYS B 155 ? 0.4172 0.3898 0.4096 -0.0236 -0.0940 0.0558  154 LYS B CD    
4998  C  CE    . LYS B 155 ? 0.4876 0.4604 0.4672 -0.0334 -0.0980 0.0608  154 LYS B CE    
4999  N  NZ    . LYS B 155 ? 0.5300 0.5083 0.5154 -0.0312 -0.1001 0.0589  154 LYS B NZ    
5013  N  N     . LYS B 156 ? 0.3666 0.3498 0.3953 0.0087  -0.0717 0.0301  155 LYS B N     
5014  C  CA    . LYS B 156 ? 0.3215 0.3036 0.3581 0.0154  -0.0696 0.0259  155 LYS B CA    
5015  C  C     . LYS B 156 ? 0.3288 0.3040 0.3653 0.0141  -0.0743 0.0294  155 LYS B C     
5016  O  O     . LYS B 156 ? 0.3047 0.2751 0.3463 0.0141  -0.0826 0.0333  155 LYS B O     
5017  C  CB    . LYS B 156 ? 0.4097 0.3939 0.4592 0.0221  -0.0720 0.0225  155 LYS B CB    
5018  C  CG    . LYS B 156 ? 0.4874 0.4775 0.5392 0.0265  -0.0639 0.0158  155 LYS B CG    
5019  C  CD    . LYS B 156 ? 0.5132 0.5047 0.5781 0.0335  -0.0649 0.0113  155 LYS B CD    
5020  C  CE    . LYS B 156 ? 0.6076 0.5940 0.6762 0.0372  -0.0652 0.0087  155 LYS B CE    
5021  N  NZ    . LYS B 156 ? 0.5655 0.5519 0.6256 0.0362  -0.0589 0.0066  155 LYS B NZ    
5035  N  N     . ILE B 157 ? 0.2716 0.2460 0.3032 0.0129  -0.0694 0.0282  156 ILE B N     
5036  C  CA    . ILE B 157 ? 0.2739 0.2422 0.3045 0.0107  -0.0732 0.0315  156 ILE B CA    
5037  C  C     . ILE B 157 ? 0.2969 0.2631 0.3355 0.0168  -0.0730 0.0270  156 ILE B C     
5038  O  O     . ILE B 157 ? 0.2491 0.2185 0.2865 0.0187  -0.0668 0.0229  156 ILE B O     
5039  C  CB    . ILE B 157 ? 0.2795 0.2488 0.3002 0.0046  -0.0683 0.0333  156 ILE B CB    
5040  C  CG1   . ILE B 157 ? 0.2862 0.2583 0.2974 -0.0018 -0.0661 0.0359  156 ILE B CG1   
5041  C  CG2   . ILE B 157 ? 0.2855 0.2483 0.3059 0.0016  -0.0731 0.0373  156 ILE B CG2   
5042  C  CD1   . ILE B 157 ? 0.3422 0.3105 0.3512 -0.0059 -0.0745 0.0417  156 ILE B CD1   
5054  N  N     . THR B 158 ? 0.2800 0.2403 0.3265 0.0194  -0.0799 0.0279  157 THR B N     
5055  C  CA    . THR B 158 ? 0.2357 0.1936 0.2900 0.0254  -0.0794 0.0224  157 THR B CA    
5056  C  C     . THR B 158 ? 0.2682 0.2180 0.3236 0.0240  -0.0839 0.0243  157 THR B C     
5057  O  O     . THR B 158 ? 0.2777 0.2220 0.3312 0.0196  -0.0899 0.0306  157 THR B O     
5058  C  CB    . THR B 158 ? 0.2771 0.2353 0.3428 0.0314  -0.0820 0.0192  157 THR B CB    
5059  O  OG1   . THR B 158 ? 0.3272 0.2806 0.3972 0.0297  -0.0906 0.0252  157 THR B OG1   
5060  C  CG2   . THR B 158 ? 0.3072 0.2740 0.3725 0.0332  -0.0765 0.0160  157 THR B CG2   
5068  N  N     . ILE B 159 ? 0.2299 0.1786 0.2876 0.0272  -0.0811 0.0188  158 ILE B N     
5069  C  CA    . ILE B 159 ? 0.2546 0.1949 0.3157 0.0271  -0.0856 0.0188  158 ILE B CA    
5070  C  C     . ILE B 159 ? 0.3251 0.2607 0.3978 0.0330  -0.0896 0.0155  158 ILE B C     
5071  O  O     . ILE B 159 ? 0.3052 0.2423 0.3828 0.0380  -0.0860 0.0082  158 ILE B O     
5072  C  CB    . ILE B 159 ? 0.2421 0.1834 0.2998 0.0273  -0.0812 0.0143  158 ILE B CB    
5073  C  CG1   . ILE B 159 ? 0.2479 0.1949 0.2966 0.0220  -0.0770 0.0178  158 ILE B CG1   
5074  C  CG2   . ILE B 159 ? 0.2293 0.1615 0.2902 0.0267  -0.0858 0.0137  158 ILE B CG2   
5075  C  CD1   . ILE B 159 ? 0.2499 0.2010 0.2964 0.0230  -0.0720 0.0132  158 ILE B CD1   
5087  N  N     . ALA B 160 ? 0.2974 0.2277 0.3751 0.0320  -0.0970 0.0211  159 ALA B N     
5088  C  CA    . ALA B 160 ? 0.3133 0.2399 0.4047 0.0379  -0.1011 0.0186  159 ALA B CA    
5089  C  C     . ALA B 160 ? 0.3485 0.2665 0.4467 0.0410  -0.1024 0.0136  159 ALA B C     
5090  O  O     . ALA B 160 ? 0.3949 0.3116 0.5043 0.0472  -0.1018 0.0074  159 ALA B O     
5091  C  CB    . ALA B 160 ? 0.3582 0.2811 0.4535 0.0356  -0.1099 0.0272  159 ALA B CB    
5097  N  N     . ASP B 161 ? 0.3491 0.2611 0.4409 0.0365  -0.1041 0.0160  160 ASP B N     
5098  C  CA    . ASP B 161 ? 0.3729 0.2763 0.4689 0.0381  -0.1051 0.0110  160 ASP B CA    
5099  C  C     . ASP B 161 ? 0.3374 0.2401 0.4221 0.0320  -0.1035 0.0128  160 ASP B C     
5100  O  O     . ASP B 161 ? 0.3314 0.2381 0.4077 0.0265  -0.1035 0.0193  160 ASP B O     
5101  C  CB    . ASP B 161 ? 0.3765 0.2682 0.4834 0.0394  -0.1137 0.0143  160 ASP B CB    
5102  C  CG    . ASP B 161 ? 0.4449 0.3275 0.5595 0.0432  -0.1137 0.0065  160 ASP B CG    
5103  O  OD1   . ASP B 161 ? 0.3848 0.2706 0.4958 0.0447  -0.1070 -0.0019 160 ASP B OD1   
5104  O  OD2   . ASP B 161 ? 0.4630 0.3348 0.5871 0.0442  -0.1206 0.0089  160 ASP B OD2   
5109  N  N     . CYS B 162 ? 0.3521 0.2503 0.4373 0.0328  -0.1021 0.0067  161 CYS B N     
5110  C  CA    . CYS B 162 ? 0.3769 0.2751 0.4531 0.0271  -0.1011 0.0081  161 CYS B CA    
5111  C  C     . CYS B 162 ? 0.3753 0.2651 0.4545 0.0283  -0.1019 0.0013  161 CYS B C     
5112  O  O     . CYS B 162 ? 0.4010 0.2880 0.4871 0.0338  -0.1004 -0.0062 161 CYS B O     
5113  C  CB    . CYS B 162 ? 0.3567 0.2669 0.4241 0.0258  -0.0940 0.0070  161 CYS B CB    
5114  S  SG    . CYS B 162 ? 0.3394 0.2569 0.4079 0.0323  -0.0866 -0.0028 161 CYS B SG    
5120  N  N     . GLY B 163 ? 0.3085 0.1944 0.3827 0.0226  -0.1041 0.0039  162 GLY B N     
5121  C  CA    . GLY B 163 ? 0.3936 0.2714 0.4689 0.0221  -0.1052 -0.0021 162 GLY B CA    
5122  C  C     . GLY B 163 ? 0.3861 0.2610 0.4559 0.0146  -0.1084 0.0030  162 GLY B C     
5123  O  O     . GLY B 163 ? 0.3865 0.2679 0.4510 0.0099  -0.1079 0.0101  162 GLY B O     
5127  N  N     . GLN B 164 ? 0.3772 0.2426 0.4485 0.0131  -0.1109 -0.0014 163 GLN B N     
5128  C  CA    . GLN B 164 ? 0.3814 0.2427 0.4488 0.0058  -0.1144 0.0024  163 GLN B CA    
5129  C  C     . GLN B 164 ? 0.4984 0.3461 0.5716 0.0036  -0.1217 0.0073  163 GLN B C     
5130  O  O     . GLN B 164 ? 0.4641 0.3021 0.5456 0.0084  -0.1243 0.0040  163 GLN B O     
5131  C  CB    . GLN B 164 ? 0.4411 0.3005 0.5052 0.0045  -0.1129 -0.0058 163 GLN B CB    
5132  C  CG    . GLN B 164 ? 0.4587 0.3168 0.5186 -0.0036 -0.1160 -0.0021 163 GLN B CG    
5133  C  CD    . GLN B 164 ? 0.4073 0.2664 0.4624 -0.0055 -0.1144 -0.0097 163 GLN B CD    
5134  O  OE1   . GLN B 164 ? 0.4463 0.3063 0.5001 -0.0010 -0.1108 -0.0179 163 GLN B OE1   
5135  N  NE2   . GLN B 164 ? 0.4487 0.3082 0.5007 -0.0127 -0.1171 -0.0068 163 GLN B NE2   
5144  N  N     . LEU B 165 ? 0.4535 0.3007 0.5229 -0.0038 -0.1247 0.0153  164 LEU B N     
5145  C  CA    . LEU B 165 ? 0.5311 0.3657 0.6041 -0.0077 -0.1319 0.0217  164 LEU B CA    
5146  C  C     . LEU B 165 ? 0.5058 0.3313 0.5787 -0.0122 -0.1346 0.0182  164 LEU B C     
5147  O  O     . LEU B 165 ? 0.5464 0.3791 0.6136 -0.0160 -0.1316 0.0158  164 LEU B O     
5148  C  CB    . LEU B 165 ? 0.4556 0.2959 0.5233 -0.0141 -0.1329 0.0326  164 LEU B CB    
5149  C  CG    . LEU B 165 ? 0.5094 0.3566 0.5765 -0.0112 -0.1315 0.0369  164 LEU B CG    
5150  C  CD1   . LEU B 165 ? 0.4950 0.3484 0.5545 -0.0190 -0.1310 0.0462  164 LEU B CD1   
5151  C  CD2   . LEU B 165 ? 0.4755 0.3120 0.5508 -0.0068 -0.1375 0.0389  164 LEU B CD2   
5163  N  N     . VAL C 3   ? 0.3646 0.6219 0.5916 -0.1568 -0.1313 0.0013  2   VAL D N     
5164  C  CA    . VAL C 3   ? 0.3972 0.6476 0.6195 -0.1511 -0.1150 -0.0049 2   VAL D CA    
5165  C  C     . VAL C 3   ? 0.3214 0.5578 0.5292 -0.1417 -0.1112 -0.0046 2   VAL D C     
5166  O  O     . VAL C 3   ? 0.3183 0.5583 0.5347 -0.1354 -0.1203 0.0009  2   VAL D O     
5167  C  CB    . VAL C 3   ? 0.4296 0.6956 0.6824 -0.1424 -0.1078 -0.0069 2   VAL D CB    
5168  C  CG1   . VAL C 3   ? 0.3886 0.6598 0.6589 -0.1278 -0.1091 -0.0042 2   VAL D CG1   
5169  C  CG2   . VAL C 3   ? 0.4086 0.6659 0.6516 -0.1414 -0.0902 -0.0142 2   VAL D CG2   
5178  N  N     . ASN C 4   ? 0.2989 0.5197 0.4863 -0.1403 -0.0979 -0.0102 3   ASN D N     
5179  C  CA    . ASN C 4   ? 0.3221 0.5291 0.4946 -0.1322 -0.0938 -0.0102 3   ASN D CA    
5180  C  C     . ASN C 4   ? 0.3230 0.5367 0.5159 -0.1176 -0.0881 -0.0104 3   ASN D C     
5181  O  O     . ASN C 4   ? 0.3394 0.5561 0.5408 -0.1137 -0.0768 -0.0148 3   ASN D O     
5182  C  CB    . ASN C 4   ? 0.2947 0.4831 0.4399 -0.1361 -0.0819 -0.0160 3   ASN D CB    
5183  C  CG    . ASN C 4   ? 0.3474 0.5264 0.4690 -0.1498 -0.0876 -0.0162 3   ASN D CG    
5184  O  OD1   . ASN C 4   ? 0.3185 0.5038 0.4414 -0.1561 -0.1015 -0.0111 3   ASN D OD1   
5185  N  ND2   . ASN C 4   ? 0.3408 0.5045 0.4409 -0.1548 -0.0772 -0.0221 3   ASN D ND2   
5192  N  N     . PRO C 5   ? 0.2799 0.4961 0.4810 -0.1098 -0.0956 -0.0057 4   PRO D N     
5193  C  CA    . PRO C 5   ? 0.2946 0.5155 0.5135 -0.0960 -0.0896 -0.0067 4   PRO D CA    
5194  C  C     . PRO C 5   ? 0.2900 0.4952 0.4901 -0.0900 -0.0772 -0.0108 4   PRO D C     
5195  O  O     . PRO C 5   ? 0.2443 0.4346 0.4189 -0.0951 -0.0748 -0.0119 4   PRO D O     
5196  C  CB    . PRO C 5   ? 0.3115 0.5382 0.5431 -0.0913 -0.1034 0.0002  4   PRO D CB    
5197  C  CG    . PRO C 5   ? 0.3016 0.5173 0.5083 -0.1011 -0.1126 0.0041  4   PRO D CG    
5198  C  CD    . PRO C 5   ? 0.2695 0.4825 0.4617 -0.1137 -0.1096 0.0007  4   PRO D CD    
5206  N  N     . THR C 6   ? 0.2613 0.4702 0.4752 -0.0791 -0.0692 -0.0133 5   THR D N     
5207  C  CA    . THR C 6   ? 0.2429 0.4389 0.4427 -0.0723 -0.0581 -0.0166 5   THR D CA    
5208  C  C     . THR C 6   ? 0.3050 0.5032 0.5167 -0.0609 -0.0607 -0.0147 5   THR D C     
5209  O  O     . THR C 6   ? 0.2660 0.4780 0.5029 -0.0556 -0.0638 -0.0139 5   THR D O     
5210  C  CB    . THR C 6   ? 0.2807 0.4774 0.4822 -0.0712 -0.0443 -0.0222 5   THR D CB    
5211  O  OG1   . THR C 6   ? 0.3028 0.4959 0.4926 -0.0821 -0.0419 -0.0240 5   THR D OG1   
5212  C  CG2   . THR C 6   ? 0.2931 0.4769 0.4806 -0.0643 -0.0341 -0.0248 5   THR D CG2   
5220  N  N     . VAL C 7   ? 0.2748 0.4592 0.4690 -0.0573 -0.0590 -0.0142 6   VAL D N     
5221  C  CA    . VAL C 7   ? 0.2513 0.4350 0.4533 -0.0471 -0.0613 -0.0124 6   VAL D CA    
5222  C  C     . VAL C 7   ? 0.2849 0.4567 0.4725 -0.0416 -0.0494 -0.0164 6   VAL D C     
5223  O  O     . VAL C 7   ? 0.2524 0.4152 0.4226 -0.0460 -0.0415 -0.0192 6   VAL D O     
5224  C  CB    . VAL C 7   ? 0.2584 0.4380 0.4547 -0.0490 -0.0745 -0.0060 6   VAL D CB    
5225  C  CG1   . VAL C 7   ? 0.3189 0.5106 0.5290 -0.0555 -0.0872 -0.0014 6   VAL D CG1   
5226  C  CG2   . VAL C 7   ? 0.2747 0.4386 0.4415 -0.0552 -0.0731 -0.0057 6   VAL D CG2   
5236  N  N     . PHE C 8   ? 0.2650 0.4371 0.4616 -0.0318 -0.0482 -0.0166 7   PHE D N     
5237  C  CA    . PHE C 8   ? 0.2607 0.4230 0.4459 -0.0261 -0.0378 -0.0201 7   PHE D CA    
5238  C  C     . PHE C 8   ? 0.2443 0.4001 0.4272 -0.0195 -0.0424 -0.0175 7   PHE D C     
5239  O  O     . PHE C 8   ? 0.2406 0.4026 0.4387 -0.0160 -0.0514 -0.0143 7   PHE D O     
5240  C  CB    . PHE C 8   ? 0.2963 0.4665 0.4953 -0.0209 -0.0279 -0.0250 7   PHE D CB    
5241  C  CG    . PHE C 8   ? 0.3009 0.4811 0.5232 -0.0125 -0.0309 -0.0254 7   PHE D CG    
5242  C  CD1   . PHE C 8   ? 0.3033 0.4774 0.5243 -0.0043 -0.0290 -0.0263 7   PHE D CD1   
5243  C  CD2   . PHE C 8   ? 0.2936 0.4891 0.5398 -0.0129 -0.0355 -0.0252 7   PHE D CD2   
5244  C  CE1   . PHE C 8   ? 0.3123 0.4947 0.5554 0.0034  -0.0314 -0.0273 7   PHE D CE1   
5245  C  CE2   . PHE C 8   ? 0.3079 0.5123 0.5772 -0.0048 -0.0377 -0.0260 7   PHE D CE2   
5246  C  CZ    . PHE C 8   ? 0.2746 0.4718 0.5420 0.0035  -0.0354 -0.0273 7   PHE D CZ    
5256  N  N     . PHE C 9   ? 0.2212 0.3642 0.3852 -0.0181 -0.0365 -0.0186 8   PHE D N     
5257  C  CA    . PHE C 9   ? 0.2538 0.3897 0.4145 -0.0111 -0.0373 -0.0176 8   PHE D CA    
5258  C  C     . PHE C 9   ? 0.2841 0.4179 0.4443 -0.0050 -0.0261 -0.0224 8   PHE D C     
5259  O  O     . PHE C 9   ? 0.2318 0.3608 0.3802 -0.0079 -0.0176 -0.0249 8   PHE D O     
5260  C  CB    . PHE C 9   ? 0.2456 0.3683 0.3843 -0.0146 -0.0391 -0.0150 8   PHE D CB    
5261  C  CG    . PHE C 9   ? 0.2213 0.3432 0.3547 -0.0216 -0.0500 -0.0100 8   PHE D CG    
5262  C  CD1   . PHE C 9   ? 0.2108 0.3431 0.3600 -0.0233 -0.0599 -0.0066 8   PHE D CD1   
5263  C  CD2   . PHE C 9   ? 0.2884 0.3990 0.4008 -0.0265 -0.0502 -0.0085 8   PHE D CD2   
5264  C  CE1   . PHE C 9   ? 0.2505 0.3816 0.3929 -0.0306 -0.0704 -0.0015 8   PHE D CE1   
5265  C  CE2   . PHE C 9   ? 0.2712 0.3803 0.3759 -0.0340 -0.0598 -0.0040 8   PHE D CE2   
5266  C  CZ    . PHE C 9   ? 0.2334 0.3527 0.3526 -0.0362 -0.0703 -0.0002 8   PHE D CZ    
5276  N  N     . ASP C 10  ? 0.2690 0.4051 0.4406 0.0029  -0.0260 -0.0235 9   ASP D N     
5277  C  CA    . ASP C 10  ? 0.3004 0.4316 0.4665 0.0082  -0.0167 -0.0274 9   ASP D CA    
5278  C  C     . ASP C 10  ? 0.2372 0.3565 0.3894 0.0105  -0.0190 -0.0249 9   ASP D C     
5279  O  O     . ASP C 10  ? 0.3011 0.4197 0.4593 0.0137  -0.0267 -0.0222 9   ASP D O     
5280  C  CB    . ASP C 10  ? 0.2537 0.3941 0.4395 0.0150  -0.0139 -0.0312 9   ASP D CB    
5281  C  CG    . ASP C 10  ? 0.2823 0.4340 0.4797 0.0126  -0.0082 -0.0347 9   ASP D CG    
5282  O  OD1   . ASP C 10  ? 0.3197 0.4691 0.5057 0.0072  -0.0022 -0.0355 9   ASP D OD1   
5283  O  OD2   . ASP C 10  ? 0.3430 0.5057 0.5617 0.0162  -0.0095 -0.0366 9   ASP D OD2   
5288  N  N     . ILE C 11  ? 0.2521 0.3621 0.3868 0.0088  -0.0127 -0.0256 10  ILE D N     
5289  C  CA    . ILE C 11  ? 0.2242 0.3233 0.3449 0.0096  -0.0146 -0.0232 10  ILE D CA    
5290  C  C     . ILE C 11  ? 0.2735 0.3693 0.3942 0.0164  -0.0100 -0.0255 10  ILE D C     
5291  O  O     . ILE C 11  ? 0.2577 0.3552 0.3787 0.0179  -0.0020 -0.0291 10  ILE D O     
5292  C  CB    . ILE C 11  ? 0.2269 0.3177 0.3295 0.0037  -0.0104 -0.0226 10  ILE D CB    
5293  C  CG1   . ILE C 11  ? 0.2493 0.3427 0.3503 -0.0041 -0.0147 -0.0211 10  ILE D CG1   
5294  C  CG2   . ILE C 11  ? 0.2853 0.3658 0.3752 0.0050  -0.0112 -0.0207 10  ILE D CG2   
5295  C  CD1   . ILE C 11  ? 0.2700 0.3634 0.3717 -0.0061 -0.0252 -0.0168 10  ILE D CD1   
5307  N  N     . ALA C 12  ? 0.2320 0.3227 0.3512 0.0197  -0.0151 -0.0233 11  ALA D N     
5308  C  CA    . ALA C 12  ? 0.3140 0.4000 0.4307 0.0252  -0.0113 -0.0253 11  ALA D CA    
5309  C  C     . ALA C 12  ? 0.3342 0.4097 0.4359 0.0244  -0.0125 -0.0224 11  ALA D C     
5310  O  O     . ALA C 12  ? 0.2783 0.3504 0.3745 0.0208  -0.0183 -0.0185 11  ALA D O     
5311  C  CB    . ALA C 12  ? 0.3109 0.4011 0.4433 0.0313  -0.0154 -0.0265 11  ALA D CB    
5317  N  N     . VAL C 13  ? 0.2883 0.3591 0.3834 0.0273  -0.0070 -0.0242 12  VAL D N     
5318  C  CA    . VAL C 13  ? 0.3377 0.3996 0.4206 0.0273  -0.0072 -0.0219 12  VAL D CA    
5319  C  C     . VAL C 13  ? 0.3969 0.4567 0.4838 0.0328  -0.0088 -0.0229 12  VAL D C     
5320  O  O     . VAL C 13  ? 0.3706 0.4320 0.4598 0.0360  -0.0039 -0.0265 12  VAL D O     
5321  C  CB    . VAL C 13  ? 0.3445 0.4021 0.4160 0.0254  0.0003  -0.0226 12  VAL D CB    
5322  C  CG1   . VAL C 13  ? 0.3524 0.4021 0.4142 0.0260  0.0001  -0.0204 12  VAL D CG1   
5323  C  CG2   . VAL C 13  ? 0.3290 0.3875 0.3968 0.0197  0.0021  -0.0221 12  VAL D CG2   
5333  N  N     . ASP C 14  ? 0.3247 0.3806 0.4116 0.0334  -0.0157 -0.0197 13  ASP D N     
5334  C  CA    . ASP C 14  ? 0.4039 0.4576 0.4965 0.0383  -0.0187 -0.0204 13  ASP D CA    
5335  C  C     . ASP C 14  ? 0.4494 0.5094 0.5560 0.0428  -0.0170 -0.0251 13  ASP D C     
5336  O  O     . ASP C 14  ? 0.4340 0.4924 0.5420 0.0466  -0.0141 -0.0286 13  ASP D O     
5337  C  CB    . ASP C 14  ? 0.4166 0.4637 0.4986 0.0393  -0.0152 -0.0207 13  ASP D CB    
5338  C  CG    . ASP C 14  ? 0.3648 0.4057 0.4366 0.0359  -0.0181 -0.0162 13  ASP D CG    
5339  O  OD1   . ASP C 14  ? 0.3764 0.4168 0.4495 0.0335  -0.0243 -0.0128 13  ASP D OD1   
5340  O  OD2   . ASP C 14  ? 0.3701 0.4067 0.4328 0.0355  -0.0142 -0.0159 13  ASP D OD2   
5345  N  N     . GLY C 15  ? 0.3714 0.4389 0.4887 0.0419  -0.0186 -0.0255 14  GLY D N     
5346  C  CA    . GLY C 15  ? 0.3914 0.4664 0.5246 0.0459  -0.0168 -0.0301 14  GLY D CA    
5347  C  C     . GLY C 15  ? 0.4082 0.4884 0.5405 0.0453  -0.0074 -0.0348 14  GLY D C     
5348  O  O     . GLY C 15  ? 0.4429 0.5308 0.5889 0.0477  -0.0048 -0.0391 14  GLY D O     
5352  N  N     . GLU C 16  ? 0.3733 0.4497 0.4909 0.0421  -0.0024 -0.0342 15  GLU D N     
5353  C  CA    . GLU C 16  ? 0.4258 0.5057 0.5403 0.0407  0.0063  -0.0378 15  GLU D CA    
5354  C  C     . GLU C 16  ? 0.3473 0.4326 0.4635 0.0360  0.0074  -0.0366 15  GLU D C     
5355  O  O     . GLU C 16  ? 0.3677 0.4491 0.4757 0.0322  0.0047  -0.0327 15  GLU D O     
5356  C  CB    . GLU C 16  ? 0.4129 0.4852 0.5111 0.0396  0.0105  -0.0368 15  GLU D CB    
5357  C  CG    . GLU C 16  ? 0.5165 0.5913 0.6103 0.0381  0.0190  -0.0399 15  GLU D CG    
5358  C  CD    . GLU C 16  ? 0.5493 0.6258 0.6465 0.0416  0.0226  -0.0450 15  GLU D CD    
5359  O  OE1   . GLU C 16  ? 0.6530 0.7241 0.7471 0.0444  0.0201  -0.0452 15  GLU D OE1   
5360  O  OE2   . GLU C 16  ? 0.5760 0.6594 0.6790 0.0412  0.0283  -0.0493 15  GLU D OE2   
5367  N  N     . PRO C 17  ? 0.3771 0.4713 0.5034 0.0358  0.0116  -0.0402 16  PRO D N     
5368  C  CA    . PRO C 17  ? 0.3316 0.4310 0.4599 0.0308  0.0123  -0.0391 16  PRO D CA    
5369  C  C     . PRO C 17  ? 0.3873 0.4799 0.4989 0.0262  0.0165  -0.0369 16  PRO D C     
5370  O  O     . PRO C 17  ? 0.3806 0.4687 0.4827 0.0268  0.0220  -0.0379 16  PRO D O     
5371  C  CB    . PRO C 17  ? 0.3961 0.5059 0.5371 0.0316  0.0182  -0.0441 16  PRO D CB    
5372  C  CG    . PRO C 17  ? 0.4078 0.5179 0.5543 0.0372  0.0205  -0.0483 16  PRO D CG    
5373  C  CD    . PRO C 17  ? 0.4055 0.5056 0.5432 0.0400  0.0158  -0.0459 16  PRO D CD    
5381  N  N     . LEU C 18  ? 0.3245 0.4159 0.4325 0.0215  0.0133  -0.0339 17  LEU D N     
5382  C  CA    . LEU C 18  ? 0.2960 0.3809 0.3904 0.0170  0.0172  -0.0322 17  LEU D CA    
5383  C  C     . LEU C 18  ? 0.3327 0.4233 0.4304 0.0122  0.0212  -0.0335 17  LEU D C     
5384  O  O     . LEU C 18  ? 0.3376 0.4260 0.4289 0.0103  0.0279  -0.0343 17  LEU D O     
5385  C  CB    . LEU C 18  ? 0.2839 0.3621 0.3702 0.0144  0.0118  -0.0287 17  LEU D CB    
5386  C  CG    . LEU C 18  ? 0.2697 0.3401 0.3428 0.0101  0.0160  -0.0274 17  LEU D CG    
5387  C  CD1   . LEU C 18  ? 0.3781 0.4424 0.4435 0.0131  0.0212  -0.0274 17  LEU D CD1   
5388  C  CD2   . LEU C 18  ? 0.2856 0.3504 0.3515 0.0070  0.0112  -0.0249 17  LEU D CD2   
5400  N  N     . GLY C 19  ? 0.2668 0.3647 0.3747 0.0099  0.0166  -0.0334 18  GLY D N     
5401  C  CA    . GLY C 19  ? 0.2739 0.3781 0.3863 0.0049  0.0199  -0.0347 18  GLY D CA    
5402  C  C     . GLY C 19  ? 0.2908 0.4008 0.4114 0.0015  0.0123  -0.0331 18  GLY D C     
5403  O  O     . GLY C 19  ? 0.2631 0.3714 0.3846 0.0028  0.0047  -0.0307 18  GLY D O     
5407  N  N     . ARG C 20  ? 0.2762 0.3930 0.4027 -0.0034 0.0142  -0.0342 19  ARG D N     
5408  C  CA    . ARG C 20  ? 0.2198 0.3445 0.3564 -0.0073 0.0071  -0.0329 19  ARG D CA    
5409  C  C     . ARG C 20  ? 0.2785 0.3969 0.4024 -0.0153 0.0061  -0.0313 19  ARG D C     
5410  O  O     . ARG C 20  ? 0.2580 0.3716 0.3731 -0.0188 0.0132  -0.0327 19  ARG D O     
5411  C  CB    . ARG C 20  ? 0.2233 0.3615 0.3773 -0.0079 0.0097  -0.0356 19  ARG D CB    
5412  C  CG    . ARG C 20  ? 0.2452 0.3927 0.4107 -0.0130 0.0023  -0.0340 19  ARG D CG    
5413  C  CD    . ARG C 20  ? 0.2951 0.4582 0.4833 -0.0113 0.0035  -0.0366 19  ARG D CD    
5414  N  NE    . ARG C 20  ? 0.3230 0.4908 0.5253 -0.0030 0.0015  -0.0377 19  ARG D NE    
5415  C  CZ    . ARG C 20  ? 0.2969 0.4782 0.5218 0.0002  0.0017  -0.0401 19  ARG D CZ    
5416  N  NH1   . ARG C 20  ? 0.3218 0.5144 0.5584 -0.0044 0.0036  -0.0415 19  ARG D NH1   
5417  N  NH2   . ARG C 20  ? 0.3260 0.5096 0.5629 0.0080  0.0000  -0.0415 19  ARG D NH2   
5431  N  N     . VAL C 21  ? 0.2607 0.3789 0.3836 -0.0185 -0.0026 -0.0285 20  VAL D N     
5432  C  CA    . VAL C 21  ? 0.2351 0.3484 0.3468 -0.0271 -0.0044 -0.0277 20  VAL D CA    
5433  C  C     . VAL C 21  ? 0.2409 0.3656 0.3655 -0.0318 -0.0117 -0.0265 20  VAL D C     
5434  O  O     . VAL C 21  ? 0.2452 0.3769 0.3818 -0.0287 -0.0197 -0.0242 20  VAL D O     
5435  C  CB    . VAL C 21  ? 0.2334 0.3360 0.3299 -0.0285 -0.0084 -0.0253 20  VAL D CB    
5436  C  CG1   . VAL C 21  ? 0.2516 0.3489 0.3359 -0.0380 -0.0086 -0.0257 20  VAL D CG1   
5437  C  CG2   . VAL C 21  ? 0.2750 0.3679 0.3619 -0.0229 -0.0023 -0.0259 20  VAL D CG2   
5447  N  N     . SER C 22  ? 0.2278 0.3546 0.3511 -0.0391 -0.0092 -0.0280 21  SER D N     
5448  C  CA    . SER C 22  ? 0.2243 0.3626 0.3600 -0.0446 -0.0163 -0.0269 21  SER D CA    
5449  C  C     . SER C 22  ? 0.2499 0.3811 0.3703 -0.0544 -0.0204 -0.0258 21  SER D C     
5450  O  O     . SER C 22  ? 0.2332 0.3524 0.3365 -0.0575 -0.0141 -0.0277 21  SER D O     
5451  C  CB    . SER C 22  ? 0.2908 0.4392 0.4396 -0.0462 -0.0104 -0.0297 21  SER D CB    
5452  O  OG    . SER C 22  ? 0.2732 0.4150 0.4102 -0.0528 -0.0032 -0.0319 21  SER D OG    
5458  N  N     . PHE C 23  ? 0.2028 0.3414 0.3296 -0.0593 -0.0309 -0.0229 22  PHE D N     
5459  C  CA    . PHE C 23  ? 0.2642 0.3970 0.3761 -0.0696 -0.0358 -0.0220 22  PHE D CA    
5460  C  C     . PHE C 23  ? 0.2334 0.3777 0.3561 -0.0775 -0.0417 -0.0213 22  PHE D C     
5461  O  O     . PHE C 23  ? 0.2588 0.4165 0.4015 -0.0749 -0.0488 -0.0187 22  PHE D O     
5462  C  CB    . PHE C 23  ? 0.2140 0.3430 0.3185 -0.0702 -0.0456 -0.0176 22  PHE D CB    
5463  C  CG    . PHE C 23  ? 0.2651 0.3851 0.3621 -0.0623 -0.0421 -0.0173 22  PHE D CG    
5464  C  CD1   . PHE C 23  ? 0.2600 0.3854 0.3714 -0.0526 -0.0447 -0.0152 22  PHE D CD1   
5465  C  CD2   . PHE C 23  ? 0.2197 0.3257 0.2958 -0.0646 -0.0361 -0.0192 22  PHE D CD2   
5466  C  CE1   . PHE C 23  ? 0.2347 0.3514 0.3385 -0.0460 -0.0417 -0.0149 22  PHE D CE1   
5467  C  CE2   . PHE C 23  ? 0.2340 0.3322 0.3037 -0.0579 -0.0332 -0.0187 22  PHE D CE2   
5468  C  CZ    . PHE C 23  ? 0.2565 0.3599 0.3393 -0.0489 -0.0363 -0.0164 22  PHE D CZ    
5478  N  N     . GLU C 24  ? 0.2162 0.3549 0.3260 -0.0874 -0.0392 -0.0238 23  GLU D N     
5479  C  CA    . GLU C 24  ? 0.2290 0.3760 0.3436 -0.0973 -0.0471 -0.0226 23  GLU D CA    
5480  C  C     . GLU C 24  ? 0.2351 0.3786 0.3379 -0.1035 -0.0582 -0.0188 23  GLU D C     
5481  O  O     . GLU C 24  ? 0.2409 0.3706 0.3229 -0.1055 -0.0557 -0.0198 23  GLU D O     
5482  C  CB    . GLU C 24  ? 0.2458 0.3871 0.3505 -0.1059 -0.0395 -0.0272 23  GLU D CB    
5483  C  CG    . GLU C 24  ? 0.2778 0.4262 0.3844 -0.1177 -0.0478 -0.0264 23  GLU D CG    
5484  C  CD    . GLU C 24  ? 0.3359 0.4778 0.4333 -0.1262 -0.0397 -0.0313 23  GLU D CD    
5485  O  OE1   . GLU C 24  ? 0.3361 0.4686 0.4274 -0.1223 -0.0279 -0.0349 23  GLU D OE1   
5486  O  OE2   . GLU C 24  ? 0.3610 0.5074 0.4581 -0.1367 -0.0458 -0.0313 23  GLU D OE2   
5493  N  N     . LEU C 25  ? 0.2624 0.4182 0.3787 -0.1064 -0.0706 -0.0141 24  LEU D N     
5494  C  CA    . LEU C 25  ? 0.2657 0.4194 0.3716 -0.1128 -0.0830 -0.0092 24  LEU D CA    
5495  C  C     . LEU C 25  ? 0.2785 0.4350 0.3781 -0.1268 -0.0889 -0.0094 24  LEU D C     
5496  O  O     . LEU C 25  ? 0.2723 0.4420 0.3898 -0.1294 -0.0927 -0.0088 24  LEU D O     
5497  C  CB    . LEU C 25  ? 0.2517 0.4162 0.3770 -0.1060 -0.0944 -0.0026 24  LEU D CB    
5498  C  CG    . LEU C 25  ? 0.2368 0.3988 0.3693 -0.0925 -0.0896 -0.0024 24  LEU D CG    
5499  C  CD1   . LEU C 25  ? 0.2657 0.4372 0.4169 -0.0871 -0.1024 0.0045  24  LEU D CD1   
5500  C  CD2   . LEU C 25  ? 0.2711 0.4162 0.3789 -0.0919 -0.0833 -0.0041 24  LEU D CD2   
5512  N  N     . PHE C 26  ? 0.2788 0.4230 0.3529 -0.1364 -0.0898 -0.0106 25  PHE D N     
5513  C  CA    . PHE C 26  ? 0.3116 0.4561 0.3762 -0.1508 -0.0934 -0.0124 25  PHE D CA    
5514  C  C     . PHE C 26  ? 0.3400 0.4954 0.4106 -0.1582 -0.1109 -0.0052 25  PHE D C     
5515  O  O     . PHE C 26  ? 0.3301 0.4795 0.3811 -0.1691 -0.1181 -0.0036 25  PHE D O     
5516  C  CB    . PHE C 26  ? 0.3293 0.4560 0.3642 -0.1584 -0.0859 -0.0177 25  PHE D CB    
5517  C  CG    . PHE C 26  ? 0.3239 0.4396 0.3537 -0.1515 -0.0697 -0.0240 25  PHE D CG    
5518  C  CD1   . PHE C 26  ? 0.3444 0.4646 0.3883 -0.1474 -0.0616 -0.0272 25  PHE D CD1   
5519  C  CD2   . PHE C 26  ? 0.2999 0.4011 0.3112 -0.1492 -0.0629 -0.0264 25  PHE D CD2   
5520  C  CE1   . PHE C 26  ? 0.3585 0.4681 0.3972 -0.1412 -0.0476 -0.0320 25  PHE D CE1   
5521  C  CE2   . PHE C 26  ? 0.3176 0.4091 0.3254 -0.1428 -0.0491 -0.0315 25  PHE D CE2   
5522  C  CZ    . PHE C 26  ? 0.3397 0.4351 0.3609 -0.1388 -0.0418 -0.0340 25  PHE D CZ    
5532  N  N     . ALA C 27  ? 0.3378 0.5101 0.4369 -0.1526 -0.1178 -0.0009 26  ALA D N     
5533  C  CA    . ALA C 27  ? 0.3351 0.5190 0.4438 -0.1589 -0.1352 0.0066  26  ALA D CA    
5534  C  C     . ALA C 27  ? 0.3184 0.5022 0.4165 -0.1729 -0.1387 0.0049  26  ALA D C     
5535  O  O     . ALA C 27  ? 0.3329 0.5183 0.4291 -0.1764 -0.1496 0.0103  26  ALA D O     
5536  C  CB    . ALA C 27  ? 0.3527 0.5551 0.4968 -0.1496 -0.1410 0.0109  26  ALA D CB    
5542  N  N     . ASP C 28  ? 0.3333 0.5133 0.4245 -0.1788 -0.1279 -0.0026 27  ASP D N     
5543  C  CA    . ASP C 28  ? 0.3915 0.5680 0.4709 -0.1904 -0.1292 -0.0050 27  ASP D CA    
5544  C  C     . ASP C 28  ? 0.3567 0.5159 0.4025 -0.1992 -0.1294 -0.0064 27  ASP D C     
5545  O  O     . ASP C 28  ? 0.4266 0.5830 0.4617 -0.2086 -0.1328 -0.0068 27  ASP D O     
5546  C  CB    . ASP C 28  ? 0.3701 0.5470 0.4531 -0.1939 -0.1173 -0.0126 27  ASP D CB    
5547  C  CG    . ASP C 28  ? 0.4307 0.5918 0.4980 -0.1895 -0.1017 -0.0193 27  ASP D CG    
5548  O  OD1   . ASP C 28  ? 0.3812 0.5324 0.4353 -0.1845 -0.1003 -0.0184 27  ASP D OD1   
5549  O  OD2   . ASP C 28  ? 0.4926 0.6505 0.5616 -0.1896 -0.0904 -0.0250 27  ASP D OD2   
5554  N  N     . LYS C 29  ? 0.3551 0.5030 0.3843 -0.1969 -0.1255 -0.0072 28  LYS D N     
5555  C  CA    . LYS C 29  ? 0.4226 0.5551 0.4211 -0.2048 -0.1257 -0.0080 28  LYS D CA    
5556  C  C     . LYS C 29  ? 0.3784 0.5097 0.3720 -0.2012 -0.1348 -0.0003 28  LYS D C     
5557  O  O     . LYS C 29  ? 0.3983 0.5224 0.3723 -0.2086 -0.1398 0.0024  28  LYS D O     
5558  C  CB    . LYS C 29  ? 0.4294 0.5459 0.4065 -0.2075 -0.1110 -0.0171 28  LYS D CB    
5559  C  CG    . LYS C 29  ? 0.4637 0.5788 0.4461 -0.2089 -0.0993 -0.0251 28  LYS D CG    
5560  C  CD    . LYS C 29  ? 0.4467 0.5506 0.4096 -0.2198 -0.0941 -0.0311 28  LYS D CD    
5561  C  CE    . LYS C 29  ? 0.4989 0.6085 0.4763 -0.2216 -0.0893 -0.0350 28  LYS D CE    
5562  N  NZ    . LYS C 29  ? 0.5016 0.6010 0.4753 -0.2201 -0.0740 -0.0433 28  LYS D NZ    
5576  N  N     . VAL C 30  ? 0.3607 0.4982 0.3708 -0.1903 -0.1367 0.0034  29  VAL D N     
5577  C  CA    . VAL C 30  ? 0.3763 0.5116 0.3829 -0.1858 -0.1446 0.0108  29  VAL D CA    
5578  C  C     . VAL C 30  ? 0.3487 0.4994 0.3873 -0.1748 -0.1535 0.0178  29  VAL D C     
5579  O  O     . VAL C 30  ? 0.3381 0.4912 0.3886 -0.1649 -0.1518 0.0189  29  VAL D O     
5580  C  CB    . VAL C 30  ? 0.3569 0.4805 0.3478 -0.1830 -0.1360 0.0073  29  VAL D CB    
5581  C  CG1   . VAL C 30  ? 0.3885 0.4957 0.3456 -0.1939 -0.1299 0.0026  29  VAL D CG1   
5582  C  CG2   . VAL C 30  ? 0.3375 0.4603 0.3392 -0.1734 -0.1219 0.0005  29  VAL D CG2   
5592  N  N     . PRO C 31  ? 0.3551 0.5163 0.4088 -0.1760 -0.1626 0.0222  30  PRO D N     
5593  C  CA    . PRO C 31  ? 0.3416 0.5182 0.4287 -0.1650 -0.1691 0.0273  30  PRO D CA    
5594  C  C     . PRO C 31  ? 0.3390 0.5143 0.4315 -0.1563 -0.1761 0.0346  30  PRO D C     
5595  O  O     . PRO C 31  ? 0.3228 0.5062 0.4393 -0.1446 -0.1754 0.0356  30  PRO D O     
5596  C  CB    . PRO C 31  ? 0.3551 0.5406 0.4513 -0.1706 -0.1781 0.0306  30  PRO D CB    
5597  C  CG    . PRO C 31  ? 0.3792 0.5518 0.4431 -0.1835 -0.1806 0.0312  30  PRO D CG    
5598  C  CD    . PRO C 31  ? 0.3762 0.5359 0.4175 -0.1876 -0.1673 0.0226  30  PRO D CD    
5606  N  N     . LYS C 32  ? 0.3566 0.5219 0.4281 -0.1617 -0.1826 0.0399  31  LYS D N     
5607  C  CA    . LYS C 32  ? 0.3702 0.5333 0.4466 -0.1539 -0.1894 0.0474  31  LYS D CA    
5608  C  C     . LYS C 32  ? 0.3571 0.5146 0.4317 -0.1463 -0.1809 0.0438  31  LYS D C     
5609  O  O     . LYS C 32  ? 0.3482 0.5094 0.4411 -0.1350 -0.1834 0.0474  31  LYS D O     
5610  C  CB    . LYS C 32  ? 0.3792 0.5315 0.4307 -0.1627 -0.1968 0.0538  31  LYS D CB    
5611  C  CG    . LYS C 32  ? 0.5072 0.6638 0.5592 -0.1700 -0.2078 0.0600  31  LYS D CG    
5612  C  CD    . LYS C 32  ? 0.5676 0.7169 0.6078 -0.1729 -0.2183 0.0703  31  LYS D CD    
5613  C  CE    . LYS C 32  ? 0.5589 0.6959 0.5829 -0.1704 -0.2143 0.0713  31  LYS D CE    
5614  N  NZ    . LYS C 32  ? 0.6289 0.7589 0.6416 -0.1744 -0.2243 0.0816  31  LYS D NZ    
5628  N  N     . THR C 33  ? 0.3408 0.4884 0.3927 -0.1524 -0.1706 0.0367  32  THR D N     
5629  C  CA    . THR C 33  ? 0.3498 0.4910 0.3967 -0.1467 -0.1626 0.0334  32  THR D CA    
5630  C  C     . THR C 33  ? 0.3034 0.4532 0.3749 -0.1355 -0.1545 0.0288  32  THR D C     
5631  O  O     . THR C 33  ? 0.3029 0.4506 0.3833 -0.1234 -0.1497 0.0288  32  THR D O     
5632  C  CB    . THR C 33  ? 0.3660 0.4935 0.3813 -0.1567 -0.1528 0.0264  32  THR D CB    
5633  O  OG1   . THR C 33  ? 0.3874 0.5062 0.3798 -0.1661 -0.1581 0.0302  32  THR D OG1   
5634  C  CG2   . THR C 33  ? 0.3240 0.4408 0.3315 -0.1478 -0.1412 0.0228  32  THR D CG2   
5642  N  N     . ALA C 34  ? 0.3099 0.4677 0.3917 -0.1380 -0.1506 0.0244  33  ALA D N     
5643  C  CA    . ALA C 34  ? 0.2824 0.4475 0.3873 -0.1264 -0.1410 0.0200  33  ALA D CA    
5644  C  C     . ALA C 34  ? 0.2900 0.4683 0.4254 -0.1163 -0.1500 0.0260  33  ALA D C     
5645  O  O     . ALA C 34  ? 0.2757 0.4550 0.4251 -0.1037 -0.1425 0.0237  33  ALA D O     
5646  C  CB    . ALA C 34  ? 0.2933 0.4646 0.4024 -0.1328 -0.1361 0.0147  33  ALA D CB    
5652  N  N     . GLU C 35  ? 0.3000 0.4869 0.4453 -0.1207 -0.1650 0.0334  34  GLU D N     
5653  C  CA    . GLU C 35  ? 0.3224 0.5191 0.4964 -0.1091 -0.1712 0.0382  34  GLU D CA    
5654  C  C     . GLU C 35  ? 0.3002 0.4896 0.4737 -0.1000 -0.1724 0.0416  34  GLU D C     
5655  O  O     . GLU C 35  ? 0.3262 0.5216 0.5229 -0.0880 -0.1702 0.0412  34  GLU D O     
5656  C  CB    . GLU C 35  ? 0.3215 0.5224 0.4993 -0.1133 -0.1829 0.0445  34  GLU D CB    
5657  C  CG    . GLU C 35  ? 0.3668 0.5750 0.5704 -0.1024 -0.1903 0.0505  34  GLU D CG    
5658  C  CD    . GLU C 35  ? 0.3800 0.6022 0.6156 -0.0918 -0.1839 0.0459  34  GLU D CD    
5659  O  OE1   . GLU C 35  ? 0.3527 0.5805 0.5918 -0.0941 -0.1749 0.0391  34  GLU D OE1   
5660  O  OE2   . GLU C 35  ? 0.4069 0.6337 0.6638 -0.0814 -0.1872 0.0491  34  GLU D OE2   
5667  N  N     . ASN C 36  ? 0.3124 0.4883 0.4594 -0.1058 -0.1753 0.0446  35  ASN D N     
5668  C  CA    . ASN C 36  ? 0.2849 0.4528 0.4293 -0.0983 -0.1764 0.0479  35  ASN D CA    
5669  C  C     . ASN C 36  ? 0.2958 0.4624 0.4470 -0.0885 -0.1637 0.0412  35  ASN D C     
5670  O  O     . ASN C 36  ? 0.3133 0.4825 0.4834 -0.0767 -0.1636 0.0424  35  ASN D O     
5671  C  CB    . ASN C 36  ? 0.3310 0.4844 0.4424 -0.1079 -0.1784 0.0505  35  ASN D CB    
5672  C  CG    . ASN C 36  ? 0.3300 0.4746 0.4373 -0.1014 -0.1800 0.0546  35  ASN D CG    
5673  O  OD1   . ASN C 36  ? 0.3462 0.4933 0.4709 -0.0932 -0.1865 0.0602  35  ASN D OD1   
5674  N  ND2   . ASN C 36  ? 0.3246 0.4585 0.4090 -0.1052 -0.1737 0.0515  35  ASN D ND2   
5681  N  N     . PHE C 37  ? 0.2687 0.4278 0.4017 -0.0915 -0.1498 0.0332  36  PHE D N     
5682  C  CA    . PHE C 37  ? 0.2909 0.4454 0.4260 -0.0810 -0.1346 0.0261  36  PHE D CA    
5683  C  C     . PHE C 37  ? 0.2940 0.4615 0.4589 -0.0716 -0.1310 0.0234  36  PHE D C     
5684  O  O     . PHE C 37  ? 0.2816 0.4486 0.4576 -0.0602 -0.1248 0.0211  36  PHE D O     
5685  C  CB    . PHE C 37  ? 0.2593 0.4042 0.3714 -0.0869 -0.1216 0.0188  36  PHE D CB    
5686  C  CG    . PHE C 37  ? 0.2680 0.4046 0.3754 -0.0778 -0.1074 0.0130  36  PHE D CG    
5687  C  CD1   . PHE C 37  ? 0.2238 0.3654 0.3446 -0.0711 -0.0970 0.0073  36  PHE D CD1   
5688  C  CD2   . PHE C 37  ? 0.2664 0.3904 0.3556 -0.0768 -0.1046 0.0134  36  PHE D CD2   
5689  C  CE1   . PHE C 37  ? 0.2534 0.3872 0.3685 -0.0638 -0.0849 0.0026  36  PHE D CE1   
5690  C  CE2   . PHE C 37  ? 0.2950 0.4117 0.3801 -0.0690 -0.0924 0.0086  36  PHE D CE2   
5691  C  CZ    . PHE C 37  ? 0.2522 0.3737 0.3499 -0.0626 -0.0829 0.0034  36  PHE D CZ    
5701  N  N     . ARG C 38  ? 0.2780 0.4574 0.4558 -0.0765 -0.1342 0.0231  37  ARG D N     
5702  C  CA    . ARG C 38  ? 0.3122 0.5057 0.5200 -0.0684 -0.1312 0.0206  37  ARG D CA    
5703  C  C     . ARG C 38  ? 0.2820 0.4816 0.5133 -0.0584 -0.1395 0.0256  37  ARG D C     
5704  O  O     . ARG C 38  ? 0.2836 0.4844 0.5284 -0.0474 -0.1315 0.0217  37  ARG D O     
5705  C  CB    . ARG C 38  ? 0.2768 0.4830 0.4955 -0.0768 -0.1363 0.0212  37  ARG D CB    
5706  C  CG    . ARG C 38  ? 0.2950 0.5164 0.5435 -0.0698 -0.1308 0.0173  37  ARG D CG    
5707  C  CD    . ARG C 38  ? 0.2472 0.4844 0.5146 -0.0766 -0.1415 0.0210  37  ARG D CD    
5708  N  NE    . ARG C 38  ? 0.3099 0.5502 0.5876 -0.0741 -0.1555 0.0288  37  ARG D NE    
5709  C  CZ    . ARG C 38  ? 0.3010 0.5455 0.5998 -0.0620 -0.1564 0.0302  37  ARG D CZ    
5710  N  NH1   . ARG C 38  ? 0.2891 0.5383 0.6051 -0.0520 -0.1461 0.0246  37  ARG D NH1   
5711  N  NH2   . ARG C 38  ? 0.2760 0.5189 0.5781 -0.0601 -0.1673 0.0373  37  ARG D NH2   
5725  N  N     . ALA C 39  ? 0.2576 0.4598 0.4930 -0.0624 -0.1556 0.0343  38  ALA D N     
5726  C  CA    . ALA C 39  ? 0.3006 0.5061 0.5572 -0.0521 -0.1619 0.0386  38  ALA D CA    
5727  C  C     . ALA C 39  ? 0.2876 0.4830 0.5399 -0.0439 -0.1589 0.0385  38  ALA D C     
5728  O  O     . ALA C 39  ? 0.2826 0.4806 0.5547 -0.0323 -0.1563 0.0373  38  ALA D O     
5729  C  CB    . ALA C 39  ? 0.2942 0.4977 0.5464 -0.0568 -0.1749 0.0470  38  ALA D CB    
5735  N  N     . LEU C 40  ? 0.2555 0.4367 0.4784 -0.0489 -0.1560 0.0384  39  LEU D N     
5736  C  CA    . LEU C 40  ? 0.2928 0.4625 0.5081 -0.0411 -0.1508 0.0374  39  LEU D CA    
5737  C  C     . LEU C 40  ? 0.3086 0.4778 0.5288 -0.0320 -0.1345 0.0282  39  LEU D C     
5738  O  O     . LEU C 40  ? 0.2993 0.4631 0.5231 -0.0230 -0.1308 0.0269  39  LEU D O     
5739  C  CB    . LEU C 40  ? 0.2423 0.3972 0.4243 -0.0491 -0.1503 0.0391  39  LEU D CB    
5740  C  CG    . LEU C 40  ? 0.3492 0.5010 0.5201 -0.0585 -0.1658 0.0486  39  LEU D CG    
5741  C  CD1   . LEU C 40  ? 0.3066 0.4448 0.4429 -0.0677 -0.1609 0.0472  39  LEU D CD1   
5742  C  CD2   . LEU C 40  ? 0.3757 0.5246 0.5585 -0.0507 -0.1737 0.0549  39  LEU D CD2   
5754  N  N     . SER C 41  ? 0.2849 0.4586 0.5035 -0.0348 -0.1247 0.0219  40  SER D N     
5755  C  CA    . SER C 41  ? 0.2786 0.4528 0.5022 -0.0271 -0.1098 0.0137  40  SER D CA    
5756  C  C     . SER C 41  ? 0.2666 0.4543 0.5227 -0.0181 -0.1097 0.0119  40  SER D C     
5757  O  O     . SER C 41  ? 0.2470 0.4339 0.5095 -0.0096 -0.0997 0.0063  40  SER D O     
5758  C  CB    . SER C 41  ? 0.2648 0.4385 0.4754 -0.0336 -0.0994 0.0080  40  SER D CB    
5759  O  OG    . SER C 41  ? 0.2620 0.4234 0.4439 -0.0420 -0.0984 0.0086  40  SER D OG    
5765  N  N     . THR C 42  ? 0.2736 0.4741 0.5508 -0.0202 -0.1202 0.0161  41  THR D N     
5766  C  CA    . THR C 42  ? 0.2803 0.4941 0.5908 -0.0111 -0.1201 0.0142  41  THR D CA    
5767  C  C     . THR C 42  ? 0.3182 0.5287 0.6409 -0.0029 -0.1283 0.0189  41  THR D C     
5768  O  O     . THR C 42  ? 0.2874 0.5019 0.6289 0.0066  -0.1229 0.0153  41  THR D O     
5769  C  CB    . THR C 42  ? 0.2930 0.5231 0.6241 -0.0158 -0.1266 0.0162  41  THR D CB    
5770  O  OG1   . THR C 42  ? 0.2857 0.5127 0.6104 -0.0209 -0.1404 0.0248  41  THR D OG1   
5771  C  CG2   . THR C 42  ? 0.2705 0.5026 0.5882 -0.0245 -0.1180 0.0114  41  THR D CG2   
5779  N  N     . GLY C 43  ? 0.2629 0.4623 0.5686 -0.0065 -0.1380 0.0260  42  GLY D N     
5780  C  CA    . GLY C 43  ? 0.3108 0.5029 0.6211 0.0000  -0.1442 0.0310  42  GLY D CA    
5781  C  C     . GLY C 43  ? 0.3417 0.5408 0.6701 0.0014  -0.1516 0.0354  42  GLY D C     
5782  O  O     . GLY C 43  ? 0.3192 0.5136 0.6573 0.0081  -0.1553 0.0383  42  GLY D O     
5786  N  N     . GLU C 44  ? 0.3224 0.5322 0.6557 -0.0052 -0.1543 0.0360  43  GLU D N     
5787  C  CA    . GLU C 44  ? 0.2996 0.5185 0.6543 -0.0029 -0.1599 0.0390  43  GLU D CA    
5788  C  C     . GLU C 44  ? 0.3210 0.5328 0.6714 -0.0055 -0.1738 0.0490  43  GLU D C     
5789  O  O     . GLU C 44  ? 0.3354 0.5527 0.7058 -0.0016 -0.1789 0.0519  43  GLU D O     
5790  C  CB    . GLU C 44  ? 0.3296 0.5620 0.6900 -0.0099 -0.1589 0.0369  43  GLU D CB    
5791  C  CG    . GLU C 44  ? 0.3512 0.5809 0.6893 -0.0232 -0.1666 0.0414  43  GLU D CG    
5792  C  CD    . GLU C 44  ? 0.3077 0.5503 0.6515 -0.0298 -0.1630 0.0374  43  GLU D CD    
5793  O  OE1   . GLU C 44  ? 0.2354 0.4823 0.5820 -0.0285 -0.1514 0.0298  43  GLU D OE1   
5794  O  OE2   . GLU C 44  ? 0.2959 0.5443 0.6423 -0.0362 -0.1716 0.0419  43  GLU D OE2   
5801  N  N     . LYS C 45  ? 0.3300 0.5298 0.6556 -0.0121 -0.1799 0.0543  44  LYS D N     
5802  C  CA    . LYS C 45  ? 0.3547 0.5461 0.6746 -0.0147 -0.1924 0.0640  44  LYS D CA    
5803  C  C     . LYS C 45  ? 0.4126 0.5920 0.7329 -0.0068 -0.1921 0.0656  44  LYS D C     
5804  O  O     . LYS C 45  ? 0.4404 0.6100 0.7510 -0.0099 -0.2015 0.0737  44  LYS D O     
5805  C  CB    . LYS C 45  ? 0.4197 0.6039 0.7101 -0.0277 -0.1990 0.0692  44  LYS D CB    
5806  C  CG    . LYS C 45  ? 0.3816 0.5745 0.6650 -0.0376 -0.1987 0.0671  44  LYS D CG    
5807  C  CD    . LYS C 45  ? 0.4284 0.6334 0.7314 -0.0386 -0.2050 0.0697  44  LYS D CD    
5808  C  CE    . LYS C 45  ? 0.4481 0.6588 0.7386 -0.0506 -0.2062 0.0686  44  LYS D CE    
5809  N  NZ    . LYS C 45  ? 0.4369 0.6618 0.7495 -0.0507 -0.2102 0.0694  44  LYS D NZ    
5823  N  N     . GLY C 46  ? 0.3687 0.5479 0.6982 0.0025  -0.1814 0.0581  45  GLY D N     
5824  C  CA    . GLY C 46  ? 0.3520 0.5199 0.6824 0.0100  -0.1803 0.0585  45  GLY D CA    
5825  C  C     . GLY C 46  ? 0.3952 0.5510 0.7011 0.0075  -0.1775 0.0582  45  GLY D C     
5826  O  O     . GLY C 46  ? 0.4178 0.5637 0.7232 0.0132  -0.1766 0.0586  45  GLY D O     
5830  N  N     . PHE C 47  ? 0.3865 0.5429 0.6726 -0.0009 -0.1758 0.0571  46  PHE D N     
5831  C  CA    . PHE C 47  ? 0.3921 0.5380 0.6550 -0.0038 -0.1727 0.0564  46  PHE D CA    
5832  C  C     . PHE C 47  ? 0.3479 0.4997 0.6001 -0.0100 -0.1664 0.0511  46  PHE D C     
5833  O  O     . PHE C 47  ? 0.3547 0.5171 0.6138 -0.0141 -0.1667 0.0497  46  PHE D O     
5834  C  CB    . PHE C 47  ? 0.3986 0.5330 0.6409 -0.0115 -0.1827 0.0655  46  PHE D CB    
5835  C  CG    . PHE C 47  ? 0.4218 0.5597 0.6555 -0.0223 -0.1913 0.0713  46  PHE D CG    
5836  C  CD1   . PHE C 47  ? 0.4119 0.5516 0.6266 -0.0323 -0.1895 0.0694  46  PHE D CD1   
5837  C  CD2   . PHE C 47  ? 0.4516 0.5906 0.6965 -0.0227 -0.2012 0.0784  46  PHE D CD2   
5838  C  CE1   . PHE C 47  ? 0.3990 0.5412 0.6046 -0.0427 -0.1971 0.0741  46  PHE D CE1   
5839  C  CE2   . PHE C 47  ? 0.4291 0.5715 0.6659 -0.0330 -0.2094 0.0838  46  PHE D CE2   
5840  C  CZ    . PHE C 47  ? 0.4369 0.5807 0.6535 -0.0430 -0.2071 0.0814  46  PHE D CZ    
5850  N  N     . GLY C 48  ? 0.3560 0.5011 0.5927 -0.0106 -0.1606 0.0478  47  GLY D N     
5851  C  CA    . GLY C 48  ? 0.2776 0.4248 0.5000 -0.0172 -0.1528 0.0424  47  GLY D CA    
5852  C  C     . GLY C 48  ? 0.3398 0.4769 0.5468 -0.0126 -0.1384 0.0354  47  GLY D C     
5853  O  O     . GLY C 48  ? 0.3022 0.4307 0.5063 -0.0076 -0.1388 0.0368  47  GLY D O     
5857  N  N     . TYR C 49  ? 0.3074 0.4460 0.5061 -0.0145 -0.1261 0.0280  48  TYR D N     
5858  C  CA    . TYR C 49  ? 0.3105 0.4388 0.4892 -0.0135 -0.1136 0.0225  48  TYR D CA    
5859  C  C     . TYR C 49  ? 0.2921 0.4198 0.4824 -0.0023 -0.1049 0.0170  48  TYR D C     
5860  O  O     . TYR C 49  ? 0.2800 0.3980 0.4555 -0.0003 -0.0974 0.0143  48  TYR D O     
5861  C  CB    . TYR C 49  ? 0.2406 0.3698 0.4063 -0.0199 -0.1043 0.0172  48  TYR D CB    
5862  C  CG    . TYR C 49  ? 0.2745 0.4007 0.4212 -0.0323 -0.1100 0.0208  48  TYR D CG    
5863  C  CD1   . TYR C 49  ? 0.2798 0.3952 0.4057 -0.0377 -0.1141 0.0249  48  TYR D CD1   
5864  C  CD2   . TYR C 49  ? 0.3134 0.4472 0.4623 -0.0391 -0.1105 0.0195  48  TYR D CD2   
5865  C  CE1   . TYR C 49  ? 0.3307 0.4428 0.4375 -0.0498 -0.1182 0.0273  48  TYR D CE1   
5866  C  CE2   . TYR C 49  ? 0.2972 0.4277 0.4278 -0.0510 -0.1151 0.0219  48  TYR D CE2   
5867  C  CZ    . TYR C 49  ? 0.2554 0.3750 0.3647 -0.0563 -0.1187 0.0255  48  TYR D CZ    
5868  O  OH    . TYR C 49  ? 0.3036 0.4200 0.3940 -0.0687 -0.1225 0.0270  48  TYR D OH    
5878  N  N     . LYS C 50  ? 0.2616 0.3996 0.4780 0.0047  -0.1054 0.0150  49  LYS D N     
5879  C  CA    . LYS C 50  ? 0.2887 0.4259 0.5138 0.0144  -0.0957 0.0086  49  LYS D CA    
5880  C  C     . LYS C 50  ? 0.3041 0.4294 0.5211 0.0185  -0.0976 0.0108  49  LYS D C     
5881  O  O     . LYS C 50  ? 0.3485 0.4713 0.5703 0.0186  -0.1091 0.0175  49  LYS D O     
5882  C  CB    . LYS C 50  ? 0.3033 0.4532 0.5595 0.0213  -0.0970 0.0064  49  LYS D CB    
5883  C  CG    . LYS C 50  ? 0.3127 0.4622 0.5785 0.0308  -0.0865 -0.0012 49  LYS D CG    
5884  C  CD    . LYS C 50  ? 0.3657 0.5296 0.6609 0.0359  -0.0848 -0.0051 49  LYS D CD    
5885  C  CE    . LYS C 50  ? 0.3820 0.5458 0.6881 0.0451  -0.0751 -0.0128 49  LYS D CE    
5886  N  NZ    . LYS C 50  ? 0.4169 0.5949 0.7510 0.0492  -0.0724 -0.0170 49  LYS D NZ    
5900  N  N     . GLY C 51  ? 0.2933 0.4114 0.4980 0.0215  -0.0869 0.0055  50  GLY D N     
5901  C  CA    . GLY C 51  ? 0.3329 0.4402 0.5297 0.0250  -0.0879 0.0070  50  GLY D CA    
5902  C  C     . GLY C 51  ? 0.3037 0.4006 0.4754 0.0179  -0.0899 0.0112  50  GLY D C     
5903  O  O     . GLY C 51  ? 0.3641 0.4518 0.5258 0.0202  -0.0874 0.0110  50  GLY D O     
5907  N  N     . SER C 52  ? 0.3389 0.4369 0.4995 0.0091  -0.0934 0.0144  51  SER D N     
5908  C  CA    . SER C 52  ? 0.3292 0.4173 0.4660 0.0020  -0.0945 0.0178  51  SER D CA    
5909  C  C     . SER C 52  ? 0.3143 0.3970 0.4346 0.0014  -0.0815 0.0120  51  SER D C     
5910  O  O     . SER C 52  ? 0.3187 0.4054 0.4446 0.0051  -0.0725 0.0060  51  SER D O     
5911  C  CB    . SER C 52  ? 0.3250 0.4154 0.4542 -0.0080 -0.1027 0.0229  51  SER D CB    
5912  O  OG    . SER C 52  ? 0.3121 0.4087 0.4401 -0.0121 -0.0970 0.0188  51  SER D OG    
5918  N  N     . CYS C 53  ? 0.3107 0.3842 0.4109 -0.0036 -0.0804 0.0138  52  CYS D N     
5919  C  CA    . CYS C 53  ? 0.3276 0.3953 0.4135 -0.0038 -0.0689 0.0089  52  CYS D CA    
5920  C  C     . CYS C 53  ? 0.3244 0.3885 0.3918 -0.0132 -0.0659 0.0087  52  CYS D C     
5921  O  O     . CYS C 53  ? 0.3137 0.3780 0.3749 -0.0207 -0.0732 0.0127  52  CYS D O     
5922  C  CB    . CYS C 53  ? 0.4259 0.4854 0.5059 0.0002  -0.0671 0.0095  52  CYS D CB    
5923  S  SG    . CYS C 53  ? 0.5777 0.6288 0.6409 -0.0073 -0.0741 0.0161  52  CYS D SG    
5929  N  N     . PHE C 54  ? 0.2811 0.3418 0.3399 -0.0128 -0.0551 0.0037  53  PHE D N     
5930  C  CA    . PHE C 54  ? 0.2828 0.3380 0.3238 -0.0205 -0.0502 0.0023  53  PHE D CA    
5931  C  C     . PHE C 54  ? 0.3190 0.3656 0.3476 -0.0212 -0.0487 0.0038  53  PHE D C     
5932  O  O     . PHE C 54  ? 0.3027 0.3459 0.3311 -0.0157 -0.0421 0.0015  53  PHE D O     
5933  C  CB    . PHE C 54  ? 0.2775 0.3328 0.3171 -0.0196 -0.0393 -0.0034 53  PHE D CB    
5934  C  CG    . PHE C 54  ? 0.2744 0.3369 0.3207 -0.0228 -0.0398 -0.0051 53  PHE D CG    
5935  C  CD1   . PHE C 54  ? 0.2432 0.3144 0.3070 -0.0176 -0.0416 -0.0057 53  PHE D CD1   
5936  C  CD2   . PHE C 54  ? 0.2921 0.3525 0.3272 -0.0315 -0.0381 -0.0065 53  PHE D CD2   
5937  C  CE1   . PHE C 54  ? 0.2497 0.3286 0.3209 -0.0209 -0.0420 -0.0071 53  PHE D CE1   
5938  C  CE2   . PHE C 54  ? 0.2603 0.3275 0.3018 -0.0351 -0.0389 -0.0079 53  PHE D CE2   
5939  C  CZ    . PHE C 54  ? 0.2768 0.3536 0.3368 -0.0297 -0.0410 -0.0080 53  PHE D CZ    
5949  N  N     . HIS C 55  ? 0.3086 0.3520 0.3268 -0.0283 -0.0551 0.0080  54  HIS D N     
5950  C  CA    . HIS C 55  ? 0.2951 0.3314 0.3032 -0.0292 -0.0550 0.0103  54  HIS D CA    
5951  C  C     . HIS C 55  ? 0.3739 0.4038 0.3660 -0.0341 -0.0456 0.0067  54  HIS D C     
5952  O  O     . HIS C 55  ? 0.3542 0.3789 0.3403 -0.0331 -0.0424 0.0071  54  HIS D O     
5953  C  CB    . HIS C 55  ? 0.3213 0.3566 0.3256 -0.0347 -0.0665 0.0172  54  HIS D CB    
5954  C  CG    . HIS C 55  ? 0.3331 0.3694 0.3268 -0.0453 -0.0705 0.0185  54  HIS D CG    
5955  N  ND1   . HIS C 55  ? 0.3262 0.3697 0.3289 -0.0470 -0.0766 0.0196  54  HIS D ND1   
5956  C  CD2   . HIS C 55  ? 0.3366 0.3677 0.3111 -0.0553 -0.0693 0.0189  54  HIS D CD2   
5957  C  CE1   . HIS C 55  ? 0.3430 0.3855 0.3319 -0.0577 -0.0794 0.0207  54  HIS D CE1   
5958  N  NE2   . HIS C 55  ? 0.3252 0.3598 0.2963 -0.0631 -0.0748 0.0201  54  HIS D NE2   
5966  N  N     . ARG C 56  ? 0.2901 0.3205 0.2764 -0.0391 -0.0406 0.0028  55  ARG D N     
5967  C  CA    . ARG C 56  ? 0.2583 0.2824 0.2304 -0.0442 -0.0314 -0.0012 55  ARG D CA    
5968  C  C     . ARG C 56  ? 0.3270 0.3518 0.3025 -0.0422 -0.0228 -0.0068 55  ARG D C     
5969  O  O     . ARG C 56  ? 0.3004 0.3290 0.2779 -0.0458 -0.0246 -0.0079 55  ARG D O     
5970  C  CB    . ARG C 56  ? 0.3195 0.3410 0.2760 -0.0559 -0.0350 0.0001  55  ARG D CB    
5971  C  CG    . ARG C 56  ? 0.3223 0.3374 0.2644 -0.0620 -0.0246 -0.0055 55  ARG D CG    
5972  C  CD    . ARG C 56  ? 0.3486 0.3611 0.2737 -0.0747 -0.0285 -0.0044 55  ARG D CD    
5973  N  NE    . ARG C 56  ? 0.4037 0.4148 0.3233 -0.0770 -0.0355 0.0016  55  ARG D NE    
5974  C  CZ    . ARG C 56  ? 0.4225 0.4334 0.3309 -0.0866 -0.0440 0.0060  55  ARG D CZ    
5975  N  NH1   . ARG C 56  ? 0.4078 0.4208 0.3108 -0.0944 -0.0481 0.0056  55  ARG D NH1   
5976  N  NH2   . ARG C 56  ? 0.4194 0.4277 0.3217 -0.0889 -0.0491 0.0114  55  ARG D NH2   
5990  N  N     . ILE C 57  ? 0.2956 0.3168 0.2719 -0.0371 -0.0138 -0.0099 56  ILE D N     
5991  C  CA    . ILE C 57  ? 0.2938 0.3141 0.2727 -0.0352 -0.0053 -0.0146 56  ILE D CA    
5992  C  C     . ILE C 57  ? 0.2523 0.2651 0.2219 -0.0371 0.0040  -0.0180 56  ILE D C     
5993  O  O     . ILE C 57  ? 0.2800 0.2905 0.2507 -0.0325 0.0066  -0.0172 56  ILE D O     
5994  C  CB    . ILE C 57  ? 0.2426 0.2668 0.2349 -0.0259 -0.0039 -0.0147 56  ILE D CB    
5995  C  CG1   . ILE C 57  ? 0.2815 0.3136 0.2851 -0.0235 -0.0123 -0.0120 56  ILE D CG1   
5996  C  CG2   . ILE C 57  ? 0.2653 0.2881 0.2593 -0.0249 0.0046  -0.0187 56  ILE D CG2   
5997  C  CD1   . ILE C 57  ? 0.3109 0.3466 0.3266 -0.0146 -0.0103 -0.0126 56  ILE D CD1   
6009  N  N     . ILE C 58  ? 0.2553 0.2644 0.2165 -0.0439 0.0089  -0.0219 57  ILE D N     
6010  C  CA    . ILE C 58  ? 0.2581 0.2599 0.2114 -0.0464 0.0184  -0.0261 57  ILE D CA    
6011  C  C     . ILE C 58  ? 0.2811 0.2803 0.2386 -0.0447 0.0260  -0.0303 57  ILE D C     
6012  O  O     . ILE C 58  ? 0.2743 0.2726 0.2278 -0.0506 0.0269  -0.0331 57  ILE D O     
6013  C  CB    . ILE C 58  ? 0.2752 0.2734 0.2132 -0.0571 0.0182  -0.0277 57  ILE D CB    
6014  C  CG1   . ILE C 58  ? 0.2785 0.2784 0.2118 -0.0591 0.0105  -0.0227 57  ILE D CG1   
6015  C  CG2   . ILE C 58  ? 0.3242 0.3148 0.2552 -0.0596 0.0295  -0.0332 57  ILE D CG2   
6016  C  CD1   . ILE C 58  ? 0.3475 0.3445 0.2638 -0.0712 0.0086  -0.0233 57  ILE D CD1   
6028  N  N     . PRO C 59  ? 0.2730 0.2707 0.2385 -0.0369 0.0313  -0.0304 58  PRO D N     
6029  C  CA    . PRO C 59  ? 0.2788 0.2737 0.2490 -0.0349 0.0379  -0.0333 58  PRO D CA    
6030  C  C     . PRO C 59  ? 0.2778 0.2653 0.2396 -0.0419 0.0452  -0.0387 58  PRO D C     
6031  O  O     . PRO C 59  ? 0.3013 0.2839 0.2566 -0.0447 0.0498  -0.0412 58  PRO D O     
6032  C  CB    . PRO C 59  ? 0.2863 0.2798 0.2641 -0.0264 0.0417  -0.0317 58  PRO D CB    
6033  C  CG    . PRO C 59  ? 0.2504 0.2483 0.2299 -0.0230 0.0354  -0.0277 58  PRO D CG    
6034  C  CD    . PRO C 59  ? 0.2823 0.2805 0.2522 -0.0303 0.0311  -0.0276 58  PRO D CD    
6042  N  N     . GLY C 60  ? 0.2879 0.2743 0.2506 -0.0447 0.0470  -0.0411 59  GLY D N     
6043  C  CA    . GLY C 60  ? 0.2859 0.2648 0.2406 -0.0520 0.0535  -0.0468 59  GLY D CA    
6044  C  C     . GLY C 60  ? 0.3117 0.2920 0.2556 -0.0621 0.0489  -0.0485 59  GLY D C     
6045  O  O     . GLY C 60  ? 0.3478 0.3220 0.2842 -0.0693 0.0539  -0.0538 59  GLY D O     
6049  N  N     . PHE C 61  ? 0.3044 0.2921 0.2474 -0.0631 0.0394  -0.0440 60  PHE D N     
6050  C  CA    . PHE C 61  ? 0.3099 0.2992 0.2422 -0.0732 0.0335  -0.0445 60  PHE D CA    
6051  C  C     . PHE C 61  ? 0.2819 0.2808 0.2210 -0.0731 0.0228  -0.0397 60  PHE D C     
6052  O  O     . PHE C 61  ? 0.2908 0.2916 0.2298 -0.0783 0.0211  -0.0413 60  PHE D O     
6053  C  CB    . PHE C 61  ? 0.3234 0.3107 0.2444 -0.0776 0.0322  -0.0438 60  PHE D CB    
6054  C  CG    . PHE C 61  ? 0.3309 0.3093 0.2445 -0.0796 0.0431  -0.0495 60  PHE D CG    
6055  C  CD1   . PHE C 61  ? 0.3303 0.3067 0.2511 -0.0714 0.0489  -0.0491 60  PHE D CD1   
6056  C  CD2   . PHE C 61  ? 0.3657 0.3380 0.2660 -0.0900 0.0479  -0.0556 60  PHE D CD2   
6057  C  CE1   . PHE C 61  ? 0.3781 0.3470 0.2942 -0.0731 0.0594  -0.0546 60  PHE D CE1   
6058  C  CE2   . PHE C 61  ? 0.3941 0.3582 0.2887 -0.0919 0.0589  -0.0617 60  PHE D CE2   
6059  C  CZ    . PHE C 61  ? 0.3743 0.3370 0.2777 -0.0832 0.0648  -0.0612 60  PHE D CZ    
6069  N  N     . MET C 62  ? 0.2732 0.2784 0.2191 -0.0673 0.0156  -0.0341 61  MET D N     
6070  C  CA    . MET C 62  ? 0.3112 0.3257 0.2650 -0.0672 0.0055  -0.0299 61  MET D CA    
6071  C  C     . MET C 62  ? 0.2980 0.3181 0.2623 -0.0587 -0.0005 -0.0247 61  MET D C     
6072  O  O     . MET C 62  ? 0.2872 0.3041 0.2503 -0.0541 0.0018  -0.0236 61  MET D O     
6073  C  CB    . MET C 62  ? 0.2832 0.2992 0.2265 -0.0780 -0.0023 -0.0287 61  MET D CB    
6074  C  CG    . MET C 62  ? 0.3909 0.3998 0.3169 -0.0854 -0.0005 -0.0300 61  MET D CG    
6075  S  SD    . MET C 62  ? 0.3494 0.3575 0.2753 -0.0796 -0.0026 -0.0254 61  MET D SD    
6076  C  CE    . MET C 62  ? 0.3958 0.4142 0.3338 -0.0764 -0.0174 -0.0174 61  MET D CE    
6086  N  N     . CYS C 63  ? 0.2546 0.2833 0.2302 -0.0566 -0.0077 -0.0218 62  CYS D N     
6087  C  CA    . CYS C 63  ? 0.2656 0.3005 0.2526 -0.0494 -0.0148 -0.0171 62  CYS D CA    
6088  C  C     . CYS C 63  ? 0.3039 0.3442 0.2912 -0.0548 -0.0264 -0.0127 62  CYS D C     
6089  O  O     . CYS C 63  ? 0.2687 0.3141 0.2593 -0.0595 -0.0300 -0.0129 62  CYS D O     
6090  C  CB    . CYS C 63  ? 0.2602 0.3018 0.2630 -0.0421 -0.0134 -0.0177 62  CYS D CB    
6091  S  SG    . CYS C 63  ? 0.2831 0.3191 0.2868 -0.0354 -0.0013 -0.0214 62  CYS D SG    
6097  N  N     . GLN C 64  ? 0.2762 0.3155 0.2612 -0.0540 -0.0327 -0.0082 63  GLN D N     
6098  C  CA    . GLN C 64  ? 0.2812 0.3245 0.2654 -0.0597 -0.0448 -0.0029 63  GLN D CA    
6099  C  C     . GLN C 64  ? 0.3049 0.3537 0.3047 -0.0518 -0.0528 0.0021  63  GLN D C     
6100  O  O     . GLN C 64  ? 0.3248 0.3707 0.3276 -0.0446 -0.0500 0.0024  63  GLN D O     
6101  C  CB    . GLN C 64  ? 0.2858 0.3220 0.2509 -0.0685 -0.0461 -0.0015 63  GLN D CB    
6102  C  CG    . GLN C 64  ? 0.3326 0.3720 0.2952 -0.0750 -0.0594 0.0051  63  GLN D CG    
6103  C  CD    . GLN C 64  ? 0.3336 0.3657 0.2752 -0.0848 -0.0600 0.0063  63  GLN D CD    
6104  O  OE1   . GLN C 64  ? 0.3373 0.3626 0.2659 -0.0882 -0.0496 0.0009  63  GLN D OE1   
6105  N  NE2   . GLN C 64  ? 0.3434 0.3770 0.2819 -0.0898 -0.0722 0.0136  63  GLN D NE2   
6114  N  N     . GLY C 65  ? 0.3053 0.3620 0.3156 -0.0532 -0.0628 0.0059  64  GLY D N     
6115  C  CA    . GLY C 65  ? 0.2880 0.3500 0.3147 -0.0464 -0.0716 0.0107  64  GLY D CA    
6116  C  C     . GLY C 65  ? 0.2819 0.3499 0.3137 -0.0519 -0.0851 0.0168  64  GLY D C     
6117  O  O     . GLY C 65  ? 0.2751 0.3410 0.2927 -0.0624 -0.0890 0.0186  64  GLY D O     
6121  N  N     . GLY C 66  ? 0.2877 0.3629 0.3401 -0.0450 -0.0923 0.0201  65  GLY D N     
6122  C  CA    . GLY C 66  ? 0.2824 0.3654 0.3458 -0.0483 -0.1053 0.0259  65  GLY D CA    
6123  C  C     . GLY C 66  ? 0.3207 0.4017 0.3870 -0.0480 -0.1176 0.0342  65  GLY D C     
6124  O  O     . GLY C 66  ? 0.3806 0.4681 0.4572 -0.0508 -0.1298 0.0400  65  GLY D O     
6128  N  N     . ASP C 67  ? 0.3551 0.4275 0.4132 -0.0452 -0.1157 0.0354  66  ASP D N     
6129  C  CA    . ASP C 67  ? 0.3586 0.4281 0.4183 -0.0459 -0.1279 0.0439  66  ASP D CA    
6130  C  C     . ASP C 67  ? 0.3962 0.4695 0.4807 -0.0341 -0.1312 0.0450  66  ASP D C     
6131  O  O     . ASP C 67  ? 0.3963 0.4644 0.4825 -0.0269 -0.1258 0.0427  66  ASP D O     
6132  C  CB    . ASP C 67  ? 0.4049 0.4632 0.4432 -0.0501 -0.1248 0.0451  66  ASP D CB    
6133  C  CG    . ASP C 67  ? 0.4557 0.5100 0.4959 -0.0504 -0.1369 0.0542  66  ASP D CG    
6134  O  OD1   . ASP C 67  ? 0.4114 0.4713 0.4695 -0.0477 -0.1484 0.0598  66  ASP D OD1   
6135  O  OD2   . ASP C 67  ? 0.4550 0.5006 0.4800 -0.0531 -0.1349 0.0557  66  ASP D OD2   
6140  N  N     . PHE C 68  ? 0.3876 0.4700 0.4920 -0.0323 -0.1407 0.0485  67  PHE D N     
6141  C  CA    . PHE C 68  ? 0.4075 0.4942 0.5380 -0.0211 -0.1439 0.0490  67  PHE D CA    
6142  C  C     . PHE C 68  ? 0.4177 0.5017 0.5562 -0.0207 -0.1585 0.0586  67  PHE D C     
6143  O  O     . PHE C 68  ? 0.4145 0.5022 0.5769 -0.0117 -0.1625 0.0594  67  PHE D O     
6144  C  CB    . PHE C 68  ? 0.3515 0.4514 0.5037 -0.0179 -0.1437 0.0458  67  PHE D CB    
6145  C  CG    . PHE C 68  ? 0.3655 0.4723 0.5202 -0.0264 -0.1555 0.0520  67  PHE D CG    
6146  C  CD1   . PHE C 68  ? 0.3883 0.4972 0.5566 -0.0258 -0.1697 0.0606  67  PHE D CD1   
6147  C  CD2   . PHE C 68  ? 0.3859 0.4960 0.5282 -0.0351 -0.1518 0.0491  67  PHE D CD2   
6148  C  CE1   . PHE C 68  ? 0.3975 0.5103 0.5641 -0.0335 -0.1773 0.0654  67  PHE D CE1   
6149  C  CE2   . PHE C 68  ? 0.3819 0.4986 0.5258 -0.0436 -0.1631 0.0547  67  PHE D CE2   
6150  C  CZ    . PHE C 68  ? 0.3808 0.4990 0.5366 -0.0428 -0.1761 0.0631  67  PHE D CZ    
6160  N  N     . THR C 69  ? 0.4240 0.5015 0.5436 -0.0306 -0.1665 0.0659  68  THR D N     
6161  C  CA    . THR C 69  ? 0.4602 0.5314 0.5825 -0.0306 -0.1765 0.0744  68  THR D CA    
6162  C  C     . THR C 69  ? 0.4792 0.5390 0.5897 -0.0293 -0.1746 0.0759  68  THR D C     
6163  O  O     . THR C 69  ? 0.5070 0.5612 0.6275 -0.0236 -0.1777 0.0791  68  THR D O     
6164  C  CB    . THR C 69  ? 0.4395 0.5090 0.5474 -0.0423 -0.1848 0.0816  68  THR D CB    
6165  O  OG1   . THR C 69  ? 0.4576 0.5220 0.5368 -0.0537 -0.1825 0.0816  68  THR D OG1   
6166  C  CG2   . THR C 69  ? 0.4489 0.5295 0.5698 -0.0436 -0.1879 0.0811  68  THR D CG2   
6174  N  N     . ARG C 70  ? 0.4650 0.5204 0.5543 -0.0341 -0.1668 0.0721  69  ARG D N     
6175  C  CA    . ARG C 70  ? 0.4803 0.5250 0.5559 -0.0340 -0.1629 0.0727  69  ARG D CA    
6176  C  C     . ARG C 70  ? 0.5251 0.5679 0.5994 -0.0269 -0.1474 0.0629  69  ARG D C     
6177  O  O     . ARG C 70  ? 0.5266 0.5621 0.5980 -0.0232 -0.1445 0.0627  69  ARG D O     
6178  C  CB    . ARG C 70  ? 0.4546 0.4929 0.5017 -0.0474 -0.1641 0.0766  69  ARG D CB    
6179  C  CG    . ARG C 70  ? 0.5158 0.5536 0.5595 -0.0558 -0.1774 0.0862  69  ARG D CG    
6180  C  CD    . ARG C 70  ? 0.5653 0.5951 0.5794 -0.0688 -0.1771 0.0896  69  ARG D CD    
6181  N  NE    . ARG C 70  ? 0.6190 0.6458 0.6259 -0.0774 -0.1854 0.0975  69  ARG D NE    
6182  C  CZ    . ARG C 70  ? 0.6388 0.6607 0.6202 -0.0905 -0.1852 0.0999  69  ARG D CZ    
6183  N  NH1   . ARG C 70  ? 0.5903 0.6098 0.5511 -0.0964 -0.1766 0.0946  69  ARG D NH1   
6184  N  NH2   . ARG C 70  ? 0.6551 0.6746 0.6317 -0.0981 -0.1934 0.1075  69  ARG D NH2   
6198  N  N     . HIS C 71  ? 0.4499 0.4991 0.5264 -0.0251 -0.1379 0.0551  70  HIS D N     
6199  C  CA    . HIS C 71  ? 0.4870 0.5348 0.5623 -0.0187 -0.1238 0.0463  70  HIS D CA    
6200  C  C     . HIS C 71  ? 0.4854 0.5239 0.5395 -0.0227 -0.1171 0.0455  70  HIS D C     
6201  O  O     . HIS C 71  ? 0.4832 0.5180 0.5385 -0.0165 -0.1099 0.0416  70  HIS D O     
6202  C  CB    . HIS C 71  ? 0.4968 0.5462 0.5936 -0.0069 -0.1231 0.0439  70  HIS D CB    
6203  C  CG    . HIS C 71  ? 0.4719 0.5309 0.5920 -0.0022 -0.1288 0.0442  70  HIS D CG    
6204  N  ND1   . HIS C 71  ? 0.4897 0.5574 0.6187 0.0006  -0.1215 0.0375  70  HIS D ND1   
6205  C  CD2   . HIS C 71  ? 0.4983 0.5600 0.6357 -0.0001 -0.1412 0.0505  70  HIS D CD2   
6206  C  CE1   . HIS C 71  ? 0.4421 0.5180 0.5934 0.0044  -0.1285 0.0393  70  HIS D CE1   
6207  N  NE2   . HIS C 71  ? 0.5323 0.6049 0.6896 0.0043  -0.1408 0.0472  70  HIS D NE2   
6215  N  N     . ASN C 72  ? 0.4738 0.5089 0.5085 -0.0336 -0.1194 0.0489  71  ASN D N     
6216  C  CA    . ASN C 72  ? 0.4929 0.5204 0.5078 -0.0381 -0.1114 0.0470  71  ASN D CA    
6217  C  C     . ASN C 72  ? 0.5140 0.5409 0.5093 -0.0485 -0.1061 0.0444  71  ASN D C     
6218  O  O     . ASN C 72  ? 0.5165 0.5372 0.4949 -0.0535 -0.1000 0.0433  71  ASN D O     
6219  C  CB    . ASN C 72  ? 0.5243 0.5446 0.5325 -0.0413 -0.1191 0.0545  71  ASN D CB    
6220  C  CG    . ASN C 72  ? 0.5490 0.5699 0.5541 -0.0495 -0.1330 0.0633  71  ASN D CG    
6221  O  OD1   . ASN C 72  ? 0.5288 0.5516 0.5212 -0.0590 -0.1340 0.0638  71  ASN D OD1   
6222  N  ND2   . ASN C 72  ? 0.5453 0.5643 0.5620 -0.0463 -0.1441 0.0705  71  ASN D ND2   
6229  N  N     . GLY C 73  ? 0.4660 0.4989 0.4631 -0.0522 -0.1080 0.0432  72  GLY D N     
6230  C  CA    . GLY C 73  ? 0.4160 0.4475 0.3948 -0.0619 -0.1020 0.0396  72  GLY D CA    
6231  C  C     . GLY C 73  ? 0.4766 0.5062 0.4397 -0.0746 -0.1112 0.0458  72  GLY D C     
6232  O  O     . GLY C 73  ? 0.4708 0.4986 0.4170 -0.0838 -0.1062 0.0423  72  GLY D O     
6236  N  N     . THR C 74  ? 0.4411 0.4704 0.4086 -0.0759 -0.1246 0.0548  73  THR D N     
6237  C  CA    . THR C 74  ? 0.5000 0.5278 0.4526 -0.0886 -0.1351 0.0619  73  THR D CA    
6238  C  C     . THR C 74  ? 0.4736 0.5091 0.4406 -0.0893 -0.1490 0.0680  73  THR D C     
6239  O  O     . THR C 74  ? 0.4961 0.5313 0.4514 -0.1003 -0.1589 0.0742  73  THR D O     
6240  C  CB    . THR C 74  ? 0.5265 0.5469 0.4694 -0.0923 -0.1413 0.0695  73  THR D CB    
6241  O  OG1   . THR C 74  ? 0.5350 0.5570 0.4987 -0.0837 -0.1519 0.0761  73  THR D OG1   
6242  C  CG2   . THR C 74  ? 0.5418 0.5556 0.4744 -0.0903 -0.1282 0.0641  73  THR D CG2   
6250  N  N     . GLY C 75  ? 0.4909 0.5332 0.4831 -0.0780 -0.1505 0.0667  74  GLY D N     
6251  C  CA    . GLY C 75  ? 0.4884 0.5383 0.4980 -0.0774 -0.1644 0.0733  74  GLY D CA    
6252  C  C     . GLY C 75  ? 0.4726 0.5320 0.4903 -0.0783 -0.1625 0.0686  74  GLY D C     
6253  O  O     . GLY C 75  ? 0.4370 0.4956 0.4396 -0.0845 -0.1534 0.0622  74  GLY D O     
6257  N  N     . GLY C 76  ? 0.4298 0.4980 0.4725 -0.0721 -0.1709 0.0717  75  GLY D N     
6258  C  CA    . GLY C 76  ? 0.4525 0.5309 0.5046 -0.0740 -0.1716 0.0688  75  GLY D CA    
6259  C  C     . GLY C 76  ? 0.4699 0.5503 0.5217 -0.0812 -0.1830 0.0764  75  GLY D C     
6260  O  O     . GLY C 76  ? 0.4489 0.5210 0.4823 -0.0893 -0.1874 0.0822  75  GLY D O     
6264  N  N     . LYS C 77  ? 0.4336 0.5244 0.5058 -0.0778 -0.1860 0.0758  76  LYS D N     
6265  C  CA    . LYS C 77  ? 0.4214 0.5148 0.4941 -0.0842 -0.1948 0.0817  76  LYS D CA    
6266  C  C     . LYS C 77  ? 0.4304 0.5362 0.5174 -0.0839 -0.1932 0.0768  76  LYS D C     
6267  O  O     . LYS C 77  ? 0.3968 0.5098 0.5008 -0.0758 -0.1869 0.0705  76  LYS D O     
6268  C  CB    . LYS C 77  ? 0.4550 0.5470 0.5447 -0.0778 -0.2039 0.0898  76  LYS D CB    
6269  C  CG    . LYS C 77  ? 0.4813 0.5815 0.6032 -0.0637 -0.2025 0.0870  76  LYS D CG    
6270  C  CD    . LYS C 77  ? 0.5282 0.6266 0.6669 -0.0587 -0.2116 0.0947  76  LYS D CD    
6271  C  CE    . LYS C 77  ? 0.5043 0.6068 0.6710 -0.0442 -0.2079 0.0910  76  LYS D CE    
6272  N  NZ    . LYS C 77  ? 0.5610 0.6617 0.7449 -0.0397 -0.2166 0.0980  76  LYS D NZ    
6286  N  N     . SER C 78  ? 0.4173 0.5256 0.4978 -0.0931 -0.1990 0.0799  77  SER D N     
6287  C  CA    . SER C 78  ? 0.4601 0.5802 0.5539 -0.0941 -0.1985 0.0761  77  SER D CA    
6288  C  C     . SER C 78  ? 0.4090 0.5378 0.5312 -0.0865 -0.2063 0.0809  77  SER D C     
6289  O  O     . SER C 78  ? 0.4565 0.5810 0.5864 -0.0816 -0.2126 0.0875  77  SER D O     
6290  C  CB    . SER C 78  ? 0.4358 0.5539 0.5066 -0.1086 -0.1998 0.0759  77  SER D CB    
6291  O  OG    . SER C 78  ? 0.5111 0.6270 0.5780 -0.1143 -0.2106 0.0847  77  SER D OG    
6297  N  N     . ILE C 79  ? 0.4354 0.5761 0.5734 -0.0860 -0.2057 0.0775  78  ILE D N     
6298  C  CA    . ILE C 79  ? 0.4083 0.5584 0.5728 -0.0804 -0.2130 0.0816  78  ILE D CA    
6299  C  C     . ILE C 79  ? 0.4394 0.5870 0.5942 -0.0899 -0.2245 0.0903  78  ILE D C     
6300  O  O     . ILE C 79  ? 0.4525 0.6069 0.6276 -0.0866 -0.2323 0.0952  78  ILE D O     
6301  C  CB    . ILE C 79  ? 0.3941 0.5587 0.5795 -0.0769 -0.2077 0.0748  78  ILE D CB    
6302  C  CG1   . ILE C 79  ? 0.3783 0.5451 0.5465 -0.0895 -0.2062 0.0716  78  ILE D CG1   
6303  C  CG2   . ILE C 79  ? 0.3845 0.5519 0.5814 -0.0672 -0.1963 0.0667  78  ILE D CG2   
6304  C  CD1   . ILE C 79  ? 0.3686 0.5504 0.5581 -0.0881 -0.2032 0.0666  78  ILE D CD1   
6316  N  N     . TYR C 80  ? 0.4470 0.5851 0.5712 -0.1021 -0.2254 0.0920  79  TYR D N     
6317  C  CA    . TYR C 80  ? 0.4699 0.6050 0.5807 -0.1132 -0.2354 0.0997  79  TYR D CA    
6318  C  C     . TYR C 80  ? 0.4913 0.6139 0.5879 -0.1160 -0.2416 0.1082  79  TYR D C     
6319  O  O     . TYR C 80  ? 0.5972 0.7161 0.6815 -0.1256 -0.2502 0.1156  79  TYR D O     
6320  C  CB    . TYR C 80  ? 0.4539 0.5870 0.5390 -0.1264 -0.2312 0.0950  79  TYR D CB    
6321  C  CG    . TYR C 80  ? 0.4377 0.5816 0.5342 -0.1253 -0.2243 0.0863  79  TYR D CG    
6322  C  CD1   . TYR C 80  ? 0.4298 0.5869 0.5516 -0.1218 -0.2291 0.0871  79  TYR D CD1   
6323  C  CD2   . TYR C 80  ? 0.3937 0.5348 0.4764 -0.1278 -0.2129 0.0771  79  TYR D CD2   
6324  C  CE1   . TYR C 80  ? 0.4136 0.5809 0.5462 -0.1213 -0.2224 0.0791  79  TYR D CE1   
6325  C  CE2   . TYR C 80  ? 0.3963 0.5467 0.4896 -0.1273 -0.2064 0.0694  79  TYR D CE2   
6326  C  CZ    . TYR C 80  ? 0.4332 0.5968 0.5514 -0.1242 -0.2110 0.0704  79  TYR D CZ    
6327  O  OH    . TYR C 80  ? 0.3911 0.5639 0.5195 -0.1244 -0.2039 0.0628  79  TYR D OH    
6337  N  N     . GLY C 81  ? 0.5363 0.6523 0.6336 -0.1084 -0.2373 0.1075  80  GLY D N     
6338  C  CA    . GLY C 81  ? 0.5579 0.6611 0.6387 -0.1119 -0.2409 0.1142  80  GLY D CA    
6339  C  C     . GLY C 81  ? 0.5848 0.6802 0.6480 -0.1116 -0.2306 0.1083  80  GLY D C     
6340  O  O     . GLY C 81  ? 0.5442 0.6441 0.6127 -0.1061 -0.2212 0.0995  80  GLY D O     
6344  N  N     . GLU C 82  ? 0.6040 0.6876 0.6458 -0.1180 -0.2320 0.1131  81  GLU D N     
6345  C  CA    . GLU C 82  ? 0.6144 0.6906 0.6403 -0.1174 -0.2222 0.1078  81  GLU D CA    
6346  C  C     . GLU C 82  ? 0.5679 0.6443 0.5732 -0.1255 -0.2129 0.0992  81  GLU D C     
6347  O  O     . GLU C 82  ? 0.5478 0.6228 0.5487 -0.1220 -0.2031 0.0918  81  GLU D O     
6348  C  CB    . GLU C 82  ? 0.7228 0.7867 0.7308 -0.1231 -0.2255 0.1149  81  GLU D CB    
6349  C  CG    . GLU C 82  ? 0.8046 0.8651 0.8304 -0.1120 -0.2285 0.1190  81  GLU D CG    
6350  C  CD    . GLU C 82  ? 0.9304 0.9786 0.9365 -0.1171 -0.2278 0.1231  81  GLU D CD    
6351  O  OE1   . GLU C 82  ? 0.9441 0.9872 0.9235 -0.1270 -0.2218 0.1201  81  GLU D OE1   
6352  O  OE2   . GLU C 82  ? 0.9979 1.0415 1.0155 -0.1114 -0.2329 0.1289  81  GLU D OE2   
6359  N  N     . LYS C 83  ? 0.5224 0.6002 0.5149 -0.1367 -0.2155 0.0999  82  LYS D N     
6360  C  CA    . LYS C 83  ? 0.5181 0.5937 0.4877 -0.1464 -0.2066 0.0919  82  LYS D CA    
6361  C  C     . LYS C 83  ? 0.5096 0.5917 0.4796 -0.1539 -0.2109 0.0919  82  LYS D C     
6362  O  O     . LYS C 83  ? 0.5295 0.6142 0.5069 -0.1561 -0.2217 0.1001  82  LYS D O     
6363  C  CB    . LYS C 83  ? 0.5235 0.5866 0.4622 -0.1569 -0.2031 0.0932  82  LYS D CB    
6364  C  CG    . LYS C 83  ? 0.6371 0.6938 0.5723 -0.1507 -0.1964 0.0910  82  LYS D CG    
6365  C  CD    . LYS C 83  ? 0.6585 0.7036 0.5630 -0.1619 -0.1918 0.0915  82  LYS D CD    
6366  C  CE    . LYS C 83  ? 0.6754 0.7144 0.5787 -0.1556 -0.1872 0.0914  82  LYS D CE    
6367  N  NZ    . LYS C 83  ? 0.7860 0.8168 0.6793 -0.1607 -0.1933 0.1007  82  LYS D NZ    
6381  N  N     . PHE C 84  ? 0.5007 0.5852 0.4626 -0.1582 -0.2023 0.0827  83  PHE D N     
6382  C  CA    . PHE C 84  ? 0.4667 0.5558 0.4247 -0.1671 -0.2053 0.0819  83  PHE D CA    
6383  C  C     . PHE C 84  ? 0.4543 0.5366 0.3848 -0.1782 -0.1946 0.0732  83  PHE D C     
6384  O  O     . PHE C 84  ? 0.4582 0.5342 0.3769 -0.1773 -0.1841 0.0665  83  PHE D O     
6385  C  CB    . PHE C 84  ? 0.4659 0.5688 0.4535 -0.1590 -0.2076 0.0798  83  PHE D CB    
6386  C  CG    . PHE C 84  ? 0.4489 0.5560 0.4448 -0.1528 -0.1966 0.0697  83  PHE D CG    
6387  C  CD1   . PHE C 84  ? 0.4134 0.5214 0.4237 -0.1410 -0.1928 0.0682  83  PHE D CD1   
6388  C  CD2   . PHE C 84  ? 0.4804 0.5905 0.4707 -0.1591 -0.1903 0.0618  83  PHE D CD2   
6389  C  CE1   . PHE C 84  ? 0.4481 0.5601 0.4661 -0.1360 -0.1829 0.0594  83  PHE D CE1   
6390  C  CE2   . PHE C 84  ? 0.4033 0.5167 0.4014 -0.1542 -0.1801 0.0530  83  PHE D CE2   
6391  C  CZ    . PHE C 84  ? 0.3488 0.4637 0.3611 -0.1428 -0.1767 0.0520  83  PHE D CZ    
6401  N  N     . GLU C 85  ? 0.4715 0.5550 0.3923 -0.1887 -0.1974 0.0732  84  GLU D N     
6402  C  CA    . GLU C 85  ? 0.4638 0.5391 0.3561 -0.2012 -0.1887 0.0663  84  GLU D CA    
6403  C  C     . GLU C 85  ? 0.4620 0.5387 0.3556 -0.1991 -0.1763 0.0542  84  GLU D C     
6404  O  O     . GLU C 85  ? 0.4546 0.5409 0.3718 -0.1905 -0.1764 0.0518  84  GLU D O     
6405  C  CB    . GLU C 85  ? 0.5236 0.6004 0.4074 -0.2127 -0.1962 0.0702  84  GLU D CB    
6406  C  CG    . GLU C 85  ? 0.5435 0.6333 0.4516 -0.2089 -0.2025 0.0706  84  GLU D CG    
6407  C  CD    . GLU C 85  ? 0.6469 0.7463 0.5855 -0.1973 -0.2138 0.0793  84  GLU D CD    
6408  O  OE1   . GLU C 85  ? 0.6937 0.7888 0.6322 -0.1946 -0.2197 0.0874  84  GLU D OE1   
6409  O  OE2   . GLU C 85  ? 0.6362 0.7472 0.5994 -0.1908 -0.2159 0.0777  84  GLU D OE2   
6416  N  N     . ASP C 86  ? 0.4573 0.5238 0.3253 -0.2074 -0.1650 0.0465  85  ASP D N     
6417  C  CA    . ASP C 86  ? 0.4734 0.5387 0.3384 -0.2084 -0.1528 0.0347  85  ASP D CA    
6418  C  C     . ASP C 86  ? 0.4545 0.5270 0.3271 -0.2131 -0.1567 0.0336  85  ASP D C     
6419  O  O     . ASP C 86  ? 0.4784 0.5476 0.3351 -0.2241 -0.1596 0.0351  85  ASP D O     
6420  C  CB    . ASP C 86  ? 0.4997 0.5518 0.3355 -0.2172 -0.1400 0.0270  85  ASP D CB    
6421  C  CG    . ASP C 86  ? 0.4849 0.5304 0.3146 -0.2121 -0.1343 0.0265  85  ASP D CG    
6422  O  OD1   . ASP C 86  ? 0.4532 0.5031 0.3004 -0.2009 -0.1335 0.0260  85  ASP D OD1   
6423  O  OD2   . ASP C 86  ? 0.4710 0.5070 0.2777 -0.2201 -0.1300 0.0263  85  ASP D OD2   
6428  N  N     . GLU C 87  ? 0.4356 0.5184 0.3327 -0.2051 -0.1571 0.0314  86  GLU D N     
6429  C  CA    . GLU C 87  ? 0.4404 0.5318 0.3483 -0.2088 -0.1625 0.0317  86  GLU D CA    
6430  C  C     . GLU C 87  ? 0.4544 0.5384 0.3417 -0.2201 -0.1533 0.0229  86  GLU D C     
6431  O  O     . GLU C 87  ? 0.4724 0.5576 0.3531 -0.2290 -0.1587 0.0249  86  GLU D O     
6432  C  CB    . GLU C 87  ? 0.4166 0.5210 0.3562 -0.1978 -0.1634 0.0307  86  GLU D CB    
6433  C  CG    . GLU C 87  ? 0.4205 0.5364 0.3767 -0.2000 -0.1711 0.0330  86  GLU D CG    
6434  C  CD    . GLU C 87  ? 0.3973 0.5272 0.3869 -0.1886 -0.1721 0.0328  86  GLU D CD    
6435  O  OE1   . GLU C 87  ? 0.3998 0.5299 0.3983 -0.1795 -0.1662 0.0305  86  GLU D OE1   
6436  O  OE2   . GLU C 87  ? 0.3984 0.5393 0.4053 -0.1890 -0.1780 0.0347  86  GLU D OE2   
6443  N  N     . ASN C 88  ? 0.4466 0.5229 0.3250 -0.2195 -0.1393 0.0129  87  ASN D N     
6444  C  CA    . ASN C 88  ? 0.4605 0.5268 0.3177 -0.2293 -0.1281 0.0033  87  ASN D CA    
6445  C  C     . ASN C 88  ? 0.4472 0.5054 0.3001 -0.2246 -0.1134 -0.0060 87  ASN D C     
6446  O  O     . ASN C 88  ? 0.4270 0.4892 0.2947 -0.2143 -0.1130 -0.0048 87  ASN D O     
6447  C  CB    . ASN C 88  ? 0.4641 0.5365 0.3298 -0.2338 -0.1295 0.0004  87  ASN D CB    
6448  C  CG    . ASN C 88  ? 0.4399 0.5219 0.3321 -0.2247 -0.1270 -0.0026 87  ASN D CG    
6449  O  OD1   . ASN C 88  ? 0.4262 0.5036 0.3193 -0.2199 -0.1157 -0.0097 87  ASN D OD1   
6450  N  ND2   . ASN C 88  ? 0.4352 0.5308 0.3494 -0.2223 -0.1370 0.0027  87  ASN D ND2   
6457  N  N     . PHE C 89  ? 0.4594 0.5060 0.2926 -0.2319 -0.1012 -0.0153 88  PHE D N     
6458  C  CA    . PHE C 89  ? 0.4485 0.4867 0.2788 -0.2276 -0.0862 -0.0251 88  PHE D CA    
6459  C  C     . PHE C 89  ? 0.4490 0.4846 0.2817 -0.2306 -0.0773 -0.0340 88  PHE D C     
6460  O  O     . PHE C 89  ? 0.4707 0.4942 0.2902 -0.2332 -0.0637 -0.0433 88  PHE D O     
6461  C  CB    . PHE C 89  ? 0.4616 0.4866 0.2678 -0.2319 -0.0768 -0.0291 88  PHE D CB    
6462  C  CG    . PHE C 89  ? 0.4636 0.4900 0.2656 -0.2304 -0.0848 -0.0204 88  PHE D CG    
6463  C  CD1   . PHE C 89  ? 0.4444 0.4740 0.2584 -0.2200 -0.0861 -0.0175 88  PHE D CD1   
6464  C  CD2   . PHE C 89  ? 0.4855 0.5101 0.2720 -0.2395 -0.0916 -0.0146 88  PHE D CD2   
6465  C  CE1   . PHE C 89  ? 0.4525 0.4829 0.2634 -0.2185 -0.0936 -0.0091 88  PHE D CE1   
6466  C  CE2   . PHE C 89  ? 0.4881 0.5135 0.2713 -0.2383 -0.0991 -0.0059 88  PHE D CE2   
6467  C  CZ    . PHE C 89  ? 0.4706 0.4987 0.2665 -0.2274 -0.1002 -0.0031 88  PHE D CZ    
6477  N  N     . ILE C 90  ? 0.4428 0.4894 0.2935 -0.2297 -0.0847 -0.0311 89  ILE D N     
6478  C  CA    . ILE C 90  ? 0.4434 0.4878 0.2975 -0.2327 -0.0768 -0.0388 89  ILE D CA    
6479  C  C     . ILE C 90  ? 0.4265 0.4655 0.2874 -0.2255 -0.0637 -0.0464 89  ILE D C     
6480  O  O     . ILE C 90  ? 0.4332 0.4610 0.2849 -0.2286 -0.0514 -0.0554 89  ILE D O     
6481  C  CB    . ILE C 90  ? 0.4383 0.4974 0.3132 -0.2326 -0.0874 -0.0337 89  ILE D CB    
6482  C  CG1   . ILE C 90  ? 0.4604 0.5219 0.3254 -0.2421 -0.0980 -0.0283 89  ILE D CG1   
6483  C  CG2   . ILE C 90  ? 0.4343 0.4922 0.3167 -0.2337 -0.0787 -0.0411 89  ILE D CG2   
6484  C  CD1   . ILE C 90  ? 0.4536 0.5314 0.3424 -0.2400 -0.1102 -0.0215 89  ILE D CD1   
6496  N  N     . LEU C 91  ? 0.4053 0.4520 0.2832 -0.2156 -0.0663 -0.0427 90  LEU D N     
6497  C  CA    . LEU C 91  ? 0.3879 0.4300 0.2774 -0.2023 -0.0528 -0.0466 90  LEU D CA    
6498  C  C     . LEU C 91  ? 0.3876 0.4178 0.2642 -0.1973 -0.0434 -0.0494 90  LEU D C     
6499  O  O     . LEU C 91  ? 0.3988 0.4290 0.2662 -0.1988 -0.0493 -0.0452 90  LEU D O     
6500  C  CB    . LEU C 91  ? 0.3656 0.4214 0.2824 -0.1890 -0.0575 -0.0399 90  LEU D CB    
6501  C  CG    . LEU C 91  ? 0.3767 0.4448 0.3091 -0.1933 -0.0645 -0.0382 90  LEU D CG    
6502  C  CD1   . LEU C 91  ? 0.3674 0.4504 0.3274 -0.1810 -0.0700 -0.0315 90  LEU D CD1   
6503  C  CD2   . LEU C 91  ? 0.4528 0.5136 0.3834 -0.1963 -0.0527 -0.0462 90  LEU D CD2   
6515  N  N     . LYS C 92  ? 0.3956 0.4162 0.2731 -0.1911 -0.0290 -0.0560 91  LYS D N     
6516  C  CA    . LYS C 92  ? 0.3839 0.3924 0.2490 -0.1877 -0.0187 -0.0601 91  LYS D CA    
6517  C  C     . LYS C 92  ? 0.3991 0.4079 0.2806 -0.1715 -0.0115 -0.0586 91  LYS D C     
6518  O  O     . LYS C 92  ? 0.3643 0.3808 0.2648 -0.1635 -0.0123 -0.0559 91  LYS D O     
6519  C  CB    . LYS C 92  ? 0.4251 0.4192 0.2728 -0.1971 -0.0073 -0.0705 91  LYS D CB    
6520  C  CG    . LYS C 92  ? 0.4463 0.4376 0.2724 -0.2155 -0.0132 -0.0736 91  LYS D CG    
6521  C  CD    . LYS C 92  ? 0.4585 0.4528 0.2704 -0.2210 -0.0229 -0.0676 91  LYS D CD    
6522  C  CE    . LYS C 92  ? 0.5573 0.5510 0.3540 -0.2329 -0.0280 -0.0660 91  LYS D CE    
6523  N  NZ    . LYS C 92  ? 0.6112 0.6021 0.3896 -0.2383 -0.0312 -0.0620 91  LYS D NZ    
6537  N  N     . HIS C 93  ? 0.3819 0.3827 0.2555 -0.1671 -0.0044 -0.0603 92  HIS D N     
6538  C  CA    . HIS C 93  ? 0.3899 0.3905 0.2765 -0.1525 0.0015  -0.0584 92  HIS D CA    
6539  C  C     . HIS C 93  ? 0.4047 0.3954 0.2937 -0.1489 0.0153  -0.0654 92  HIS D C     
6540  O  O     . HIS C 93  ? 0.4254 0.4056 0.3065 -0.1476 0.0251  -0.0702 92  HIS D O     
6541  C  CB    . HIS C 93  ? 0.3787 0.3760 0.2561 -0.1504 0.0017  -0.0565 92  HIS D CB    
6542  C  CG    . HIS C 93  ? 0.3512 0.3574 0.2265 -0.1539 -0.0123 -0.0489 92  HIS D CG    
6543  N  ND1   . HIS C 93  ? 0.3920 0.3970 0.2498 -0.1675 -0.0189 -0.0487 92  HIS D ND1   
6544  C  CD2   . HIS C 93  ? 0.3330 0.3488 0.2220 -0.1457 -0.0213 -0.0408 92  HIS D CD2   
6545  C  CE1   . HIS C 93  ? 0.3640 0.3775 0.2248 -0.1675 -0.0319 -0.0403 92  HIS D CE1   
6546  N  NE2   . HIS C 93  ? 0.3440 0.3640 0.2244 -0.1540 -0.0334 -0.0355 92  HIS D NE2   
6554  N  N     . THR C 94  ? 0.3372 0.3312 0.2378 -0.1480 0.0159  -0.0658 93  THR D N     
6555  C  CA    . THR C 94  ? 0.3493 0.3328 0.2497 -0.1482 0.0274  -0.0725 93  THR D CA    
6556  C  C     . THR C 94  ? 0.3707 0.3512 0.2834 -0.1351 0.0355  -0.0716 93  THR D C     
6557  O  O     . THR C 94  ? 0.4098 0.3797 0.3219 -0.1344 0.0456  -0.0767 93  THR D O     
6558  C  CB    . THR C 94  ? 0.3935 0.3811 0.2993 -0.1547 0.0246  -0.0735 93  THR D CB    
6559  O  OG1   . THR C 94  ? 0.3792 0.3810 0.3027 -0.1479 0.0170  -0.0665 93  THR D OG1   
6560  C  CG2   . THR C 94  ? 0.4682 0.4561 0.3594 -0.1693 0.0181  -0.0758 93  THR D CG2   
6568  N  N     . GLY C 95  ? 0.3464 0.3355 0.2702 -0.1251 0.0311  -0.0652 94  GLY D N     
6569  C  CA    . GLY C 95  ? 0.3727 0.3601 0.3081 -0.1134 0.0375  -0.0638 94  GLY D CA    
6570  C  C     . GLY C 95  ? 0.3391 0.3378 0.2871 -0.1038 0.0311  -0.0568 94  GLY D C     
6571  O  O     . GLY C 95  ? 0.3261 0.3338 0.2751 -0.1050 0.0214  -0.0527 94  GLY D O     
6575  N  N     . PRO C 96  ? 0.3115 0.3094 0.2695 -0.0941 0.0362  -0.0553 95  PRO D N     
6576  C  CA    . PRO C 96  ? 0.3088 0.3165 0.2783 -0.0848 0.0312  -0.0496 95  PRO D CA    
6577  C  C     . PRO C 96  ? 0.3172 0.3377 0.2966 -0.0867 0.0231  -0.0467 95  PRO D C     
6578  O  O     . PRO C 96  ? 0.3621 0.3840 0.3439 -0.0922 0.0238  -0.0485 95  PRO D O     
6579  C  CB    . PRO C 96  ? 0.3274 0.3308 0.3043 -0.0763 0.0390  -0.0493 95  PRO D CB    
6580  C  CG    . PRO C 96  ? 0.3685 0.3584 0.3371 -0.0798 0.0482  -0.0545 95  PRO D CG    
6581  C  CD    . PRO C 96  ? 0.3620 0.3493 0.3207 -0.0914 0.0468  -0.0587 95  PRO D CD    
6589  N  N     . GLY C 97  ? 0.2564 0.2863 0.2430 -0.0819 0.0154  -0.0420 96  GLY D N     
6590  C  CA    . GLY C 97  ? 0.2614 0.3043 0.2606 -0.0820 0.0077  -0.0390 96  GLY D CA    
6591  C  C     . GLY C 97  ? 0.2669 0.3152 0.2624 -0.0904 -0.0023 -0.0374 96  GLY D C     
6592  O  O     . GLY C 97  ? 0.2773 0.3377 0.2854 -0.0897 -0.0103 -0.0340 96  GLY D O     
6596  N  N     . ILE C 98  ? 0.2791 0.3192 0.2581 -0.0986 -0.0023 -0.0397 97  ILE D N     
6597  C  CA    . ILE C 98  ? 0.2713 0.3162 0.2449 -0.1077 -0.0127 -0.0375 97  ILE D CA    
6598  C  C     . ILE C 98  ? 0.2608 0.3130 0.2406 -0.1024 -0.0221 -0.0313 97  ILE D C     
6599  O  O     . ILE C 98  ? 0.2557 0.3034 0.2327 -0.0961 -0.0198 -0.0301 97  ILE D O     
6600  C  CB    . ILE C 98  ? 0.2843 0.3181 0.2368 -0.1179 -0.0099 -0.0418 97  ILE D CB    
6601  C  CG1   . ILE C 98  ? 0.3474 0.3749 0.2953 -0.1248 -0.0024 -0.0480 97  ILE D CG1   
6602  C  CG2   . ILE C 98  ? 0.3521 0.3907 0.2968 -0.1269 -0.0221 -0.0380 97  ILE D CG2   
6603  C  CD1   . ILE C 98  ? 0.3961 0.4322 0.3491 -0.1331 -0.0095 -0.0475 97  ILE D CD1   
6615  N  N     . LEU C 99  ? 0.2617 0.3250 0.2508 -0.1053 -0.0332 -0.0270 98  LEU D N     
6616  C  CA    . LEU C 99  ? 0.2583 0.3284 0.2541 -0.1017 -0.0438 -0.0205 98  LEU D CA    
6617  C  C     . LEU C 99  ? 0.2742 0.3437 0.2567 -0.1130 -0.0538 -0.0176 98  LEU D C     
6618  O  O     . LEU C 99  ? 0.2841 0.3572 0.2644 -0.1225 -0.0585 -0.0181 98  LEU D O     
6619  C  CB    . LEU C 99  ? 0.2603 0.3443 0.2799 -0.0954 -0.0492 -0.0173 98  LEU D CB    
6620  C  CG    . LEU C 99  ? 0.2620 0.3547 0.2938 -0.0912 -0.0613 -0.0105 98  LEU D CG    
6621  C  CD1   . LEU C 99  ? 0.2683 0.3565 0.3012 -0.0813 -0.0584 -0.0092 98  LEU D CD1   
6622  C  CD2   . LEU C 99  ? 0.2437 0.3507 0.2994 -0.0874 -0.0655 -0.0090 98  LEU D CD2   
6634  N  N     . SER C 100 ? 0.2775 0.3423 0.2507 -0.1125 -0.0573 -0.0143 99  SER D N     
6635  C  CA    . SER C 100 ? 0.2950 0.3569 0.2510 -0.1244 -0.0652 -0.0119 99  SER D CA    
6636  C  C     . SER C 100 ? 0.2944 0.3583 0.2520 -0.1211 -0.0749 -0.0044 99  SER D C     
6637  O  O     . SER C 100 ? 0.2906 0.3551 0.2588 -0.1100 -0.0729 -0.0026 99  SER D O     
6638  C  CB    . SER C 100 ? 0.3067 0.3554 0.2399 -0.1315 -0.0547 -0.0187 99  SER D CB    
6639  O  OG    . SER C 100 ? 0.3250 0.3702 0.2393 -0.1435 -0.0613 -0.0168 99  SER D OG    
6645  N  N     . MET C 101 ? 0.3098 0.3745 0.2565 -0.1315 -0.0860 0.0004  100 MET D N     
6646  C  CA    . MET C 101 ? 0.3122 0.3785 0.2599 -0.1301 -0.0970 0.0087  100 MET D CA    
6647  C  C     . MET C 101 ? 0.3192 0.3740 0.2466 -0.1325 -0.0916 0.0078  100 MET D C     
6648  O  O     . MET C 101 ? 0.3334 0.3803 0.2392 -0.1427 -0.0862 0.0032  100 MET D O     
6649  C  CB    . MET C 101 ? 0.3270 0.3998 0.2727 -0.1407 -0.1130 0.0157  100 MET D CB    
6650  C  CG    . MET C 101 ? 0.3199 0.4058 0.2889 -0.1381 -0.1197 0.0175  100 MET D CG    
6651  S  SD    . MET C 101 ? 0.3485 0.4435 0.3492 -0.1204 -0.1233 0.0224  100 MET D SD    
6652  C  CE    . MET C 101 ? 0.3647 0.4585 0.3607 -0.1236 -0.1394 0.0336  100 MET D CE    
6662  N  N     . ALA C 102 ? 0.3099 0.3641 0.2448 -0.1233 -0.0928 0.0118  101 ALA D N     
6663  C  CA    . ALA C 102 ? 0.3556 0.4009 0.2724 -0.1269 -0.0914 0.0133  101 ALA D CA    
6664  C  C     . ALA C 102 ? 0.3439 0.3901 0.2494 -0.1380 -0.1058 0.0213  101 ALA D C     
6665  O  O     . ALA C 102 ? 0.3657 0.4202 0.2823 -0.1398 -0.1186 0.0274  101 ALA D O     
6666  C  CB    . ALA C 102 ? 0.3436 0.3880 0.2723 -0.1142 -0.0890 0.0154  101 ALA D CB    
6672  N  N     . ASN C 103 ? 0.3512 0.3887 0.2344 -0.1460 -0.1036 0.0215  102 ASN D N     
6673  C  CA    . ASN C 103 ? 0.3896 0.4268 0.2587 -0.1578 -0.1170 0.0295  102 ASN D CA    
6674  C  C     . ASN C 103 ? 0.4116 0.4395 0.2609 -0.1623 -0.1125 0.0300  102 ASN D C     
6675  O  O     . ASN C 103 ? 0.4241 0.4464 0.2716 -0.1563 -0.0992 0.0239  102 ASN D O     
6676  C  CB    . ASN C 103 ? 0.4193 0.4578 0.2746 -0.1722 -0.1212 0.0278  102 ASN D CB    
6677  C  CG    . ASN C 103 ? 0.4662 0.4955 0.2985 -0.1810 -0.1068 0.0173  102 ASN D CG    
6678  O  OD1   . ASN C 103 ? 0.4484 0.4692 0.2634 -0.1847 -0.0995 0.0149  102 ASN D OD1   
6679  N  ND2   . ASN C 103 ? 0.4207 0.4517 0.2535 -0.1849 -0.1026 0.0107  102 ASN D ND2   
6686  N  N     . ALA C 104 ? 0.4695 0.4959 0.3059 -0.1721 -0.1239 0.0382  103 ALA D N     
6687  C  CA    . ALA C 104 ? 0.5445 0.5620 0.3611 -0.1777 -0.1195 0.0395  103 ALA D CA    
6688  C  C     . ALA C 104 ? 0.5589 0.5715 0.3548 -0.1915 -0.1191 0.0405  103 ALA D C     
6689  O  O     . ALA C 104 ? 0.6056 0.6140 0.3912 -0.1974 -0.1237 0.0478  103 ALA D O     
6690  C  CB    . ALA C 104 ? 0.5538 0.5714 0.3805 -0.1711 -0.1288 0.0498  103 ALA D CB    
6696  N  N     . GLY C 105 ? 0.5378 0.5508 0.3277 -0.1973 -0.1136 0.0332  104 GLY D N     
6697  C  CA    . GLY C 105 ? 0.5487 0.5580 0.3206 -0.2105 -0.1138 0.0338  104 GLY D CA    
6698  C  C     . GLY C 105 ? 0.5702 0.5865 0.3521 -0.2121 -0.1224 0.0361  104 GLY D C     
6699  O  O     . GLY C 105 ? 0.5204 0.5452 0.3249 -0.2027 -0.1288 0.0380  104 GLY D O     
6703  N  N     . PRO C 106 ? 0.5998 0.6130 0.3655 -0.2243 -0.1223 0.0358  105 PRO D N     
6704  C  CA    . PRO C 106 ? 0.5283 0.5482 0.3025 -0.2268 -0.1306 0.0381  105 PRO D CA    
6705  C  C     . PRO C 106 ? 0.5506 0.5788 0.3455 -0.2204 -0.1469 0.0501  105 PRO D C     
6706  O  O     . PRO C 106 ? 0.5248 0.5509 0.3187 -0.2204 -0.1541 0.0591  105 PRO D O     
6707  C  CB    . PRO C 106 ? 0.5943 0.6080 0.3441 -0.2423 -0.1285 0.0375  105 PRO D CB    
6708  C  CG    . PRO C 106 ? 0.6059 0.6101 0.3368 -0.2465 -0.1129 0.0284  105 PRO D CG    
6709  C  CD    . PRO C 106 ? 0.5598 0.5635 0.2992 -0.2362 -0.1112 0.0300  105 PRO D CD    
6717  N  N     . ASN C 107 ? 0.4866 0.5240 0.3011 -0.2151 -0.1523 0.0500  106 ASN D N     
6718  C  CA    . ASN C 107 ? 0.4952 0.5415 0.3324 -0.2088 -0.1670 0.0602  106 ASN D CA    
6719  C  C     . ASN C 107 ? 0.5008 0.5475 0.3519 -0.1982 -0.1718 0.0668  106 ASN D C     
6720  O  O     . ASN C 107 ? 0.5693 0.6168 0.4267 -0.1977 -0.1831 0.0772  106 ASN D O     
6721  C  CB    . ASN C 107 ? 0.5238 0.5693 0.3506 -0.2200 -0.1769 0.0682  106 ASN D CB    
6722  C  CG    . ASN C 107 ? 0.5492 0.5926 0.3594 -0.2314 -0.1712 0.0613  106 ASN D CG    
6723  O  OD1   . ASN C 107 ? 0.5760 0.6256 0.3972 -0.2288 -0.1689 0.0554  106 ASN D OD1   
6724  N  ND2   . ASN C 107 ? 0.6301 0.6648 0.4138 -0.2445 -0.1682 0.0615  106 ASN D ND2   
6731  N  N     . THR C 108 ? 0.4870 0.5333 0.3442 -0.1894 -0.1634 0.0605  107 THR D N     
6732  C  CA    . THR C 108 ? 0.4718 0.5196 0.3455 -0.1778 -0.1672 0.0654  107 THR D CA    
6733  C  C     . THR C 108 ? 0.4503 0.5066 0.3486 -0.1653 -0.1646 0.0604  107 THR D C     
6734  O  O     . THR C 108 ? 0.4497 0.5054 0.3562 -0.1564 -0.1618 0.0596  107 THR D O     
6735  C  CB    . THR C 108 ? 0.4945 0.5323 0.3501 -0.1798 -0.1599 0.0642  107 THR D CB    
6736  O  OG1   . THR C 108 ? 0.4693 0.5037 0.3138 -0.1809 -0.1458 0.0526  107 THR D OG1   
6737  C  CG2   . THR C 108 ? 0.5244 0.5542 0.3562 -0.1929 -0.1620 0.0693  107 THR D CG2   
6745  N  N     . ASN C 109 ? 0.4260 0.4907 0.3369 -0.1647 -0.1658 0.0574  108 ASN D N     
6746  C  CA    . ASN C 109 ? 0.4135 0.4872 0.3492 -0.1534 -0.1637 0.0534  108 ASN D CA    
6747  C  C     . ASN C 109 ? 0.4124 0.4924 0.3746 -0.1416 -0.1733 0.0615  108 ASN D C     
6748  O  O     . ASN C 109 ? 0.4533 0.5357 0.4227 -0.1424 -0.1839 0.0696  108 ASN D O     
6749  C  CB    . ASN C 109 ? 0.4483 0.5300 0.3924 -0.1563 -0.1627 0.0486  108 ASN D CB    
6750  C  CG    . ASN C 109 ? 0.4048 0.4797 0.3251 -0.1672 -0.1524 0.0398  108 ASN D CG    
6751  O  OD1   . ASN C 109 ? 0.4265 0.4975 0.3407 -0.1661 -0.1411 0.0313  108 ASN D OD1   
6752  N  ND2   . ASN C 109 ? 0.4002 0.4727 0.3064 -0.1779 -0.1558 0.0416  108 ASN D ND2   
6759  N  N     . GLY C 110 ? 0.4115 0.4942 0.3890 -0.1307 -0.1694 0.0588  109 GLY D N     
6760  C  CA    . GLY C 110 ? 0.3743 0.4627 0.3787 -0.1182 -0.1762 0.0644  109 GLY D CA    
6761  C  C     . GLY C 110 ? 0.3623 0.4613 0.3921 -0.1082 -0.1721 0.0589  109 GLY D C     
6762  O  O     . GLY C 110 ? 0.3596 0.4681 0.4037 -0.1081 -0.1739 0.0576  109 GLY D O     
6766  N  N     . SER C 111 ? 0.3661 0.4604 0.4008 -0.0971 -0.1616 0.0546  110 SER D N     
6767  C  CA    . SER C 111 ? 0.3432 0.4430 0.3969 -0.0858 -0.1511 0.0474  110 SER D CA    
6768  C  C     . SER C 111 ? 0.3395 0.4310 0.3792 -0.0833 -0.1340 0.0384  110 SER D C     
6769  O  O     . SER C 111 ? 0.3020 0.3973 0.3521 -0.0772 -0.1243 0.0318  110 SER D O     
6770  C  CB    . SER C 111 ? 0.3562 0.4604 0.4356 -0.0728 -0.1553 0.0507  110 SER D CB    
6771  O  OG    . SER C 111 ? 0.3729 0.4675 0.4434 -0.0703 -0.1563 0.0541  110 SER D OG    
6777  N  N     . GLN C 112 ? 0.3285 0.4090 0.3455 -0.0882 -0.1302 0.0382  111 GLN D N     
6778  C  CA    . GLN C 112 ? 0.3615 0.4341 0.3672 -0.0852 -0.1147 0.0303  111 GLN D CA    
6779  C  C     . GLN C 112 ? 0.3192 0.3915 0.3152 -0.0918 -0.1062 0.0232  111 GLN D C     
6780  O  O     . GLN C 112 ? 0.2935 0.3665 0.2781 -0.1033 -0.1114 0.0243  111 GLN D O     
6781  C  CB    . GLN C 112 ? 0.3271 0.3889 0.3122 -0.0893 -0.1131 0.0320  111 GLN D CB    
6782  C  CG    . GLN C 112 ? 0.3597 0.4197 0.3544 -0.0807 -0.1174 0.0371  111 GLN D CG    
6783  C  CD    . GLN C 112 ? 0.3551 0.4047 0.3313 -0.0829 -0.1117 0.0366  111 GLN D CD    
6784  O  OE1   . GLN C 112 ? 0.3243 0.3690 0.2908 -0.0826 -0.0989 0.0296  111 GLN D OE1   
6785  N  NE2   . GLN C 112 ? 0.4169 0.4630 0.3883 -0.0858 -0.1214 0.0444  111 GLN D NE2   
6794  N  N     . PHE C 113 ? 0.3079 0.3788 0.3081 -0.0848 -0.0931 0.0160  112 PHE D N     
6795  C  CA    . PHE C 113 ? 0.2605 0.3310 0.2560 -0.0887 -0.0840 0.0090  112 PHE D CA    
6796  C  C     . PHE C 113 ? 0.2824 0.3443 0.2705 -0.0835 -0.0695 0.0027  112 PHE D C     
6797  O  O     . PHE C 113 ? 0.2795 0.3382 0.2702 -0.0757 -0.0670 0.0037  112 PHE D O     
6798  C  CB    . PHE C 113 ? 0.2722 0.3538 0.2896 -0.0837 -0.0852 0.0081  112 PHE D CB    
6799  C  CG    . PHE C 113 ? 0.2582 0.3428 0.2931 -0.0703 -0.0805 0.0071  112 PHE D CG    
6800  C  CD1   . PHE C 113 ? 0.2674 0.3484 0.3020 -0.0649 -0.0674 0.0008  112 PHE D CD1   
6801  C  CD2   . PHE C 113 ? 0.2720 0.3615 0.3221 -0.0636 -0.0891 0.0125  112 PHE D CD2   
6802  C  CE1   . PHE C 113 ? 0.2700 0.3530 0.3181 -0.0536 -0.0629 -0.0003 112 PHE D CE1   
6803  C  CE2   . PHE C 113 ? 0.2856 0.3768 0.3503 -0.0517 -0.0840 0.0107  112 PHE D CE2   
6804  C  CZ    . PHE C 113 ? 0.2601 0.3485 0.3233 -0.0471 -0.0709 0.0041  112 PHE D CZ    
6814  N  N     . PHE C 114 ? 0.2574 0.3153 0.2366 -0.0881 -0.0603 -0.0036 113 PHE D N     
6815  C  CA    . PHE C 114 ? 0.2595 0.3104 0.2357 -0.0823 -0.0470 -0.0092 113 PHE D CA    
6816  C  C     . PHE C 114 ? 0.2762 0.3287 0.2578 -0.0822 -0.0395 -0.0146 113 PHE D C     
6817  O  O     . PHE C 114 ? 0.2540 0.3103 0.2352 -0.0897 -0.0428 -0.0154 113 PHE D O     
6818  C  CB    . PHE C 114 ? 0.2899 0.3296 0.2452 -0.0881 -0.0407 -0.0120 113 PHE D CB    
6819  C  CG    . PHE C 114 ? 0.3027 0.3383 0.2414 -0.1010 -0.0401 -0.0151 113 PHE D CG    
6820  C  CD1   . PHE C 114 ? 0.3289 0.3672 0.2595 -0.1108 -0.0514 -0.0107 113 PHE D CD1   
6821  C  CD2   . PHE C 114 ? 0.2795 0.3076 0.2094 -0.1040 -0.0284 -0.0225 113 PHE D CD2   
6822  C  CE1   . PHE C 114 ? 0.3278 0.3617 0.2408 -0.1238 -0.0507 -0.0141 113 PHE D CE1   
6823  C  CE2   . PHE C 114 ? 0.2966 0.3197 0.2100 -0.1164 -0.0271 -0.0264 113 PHE D CE2   
6824  C  CZ    . PHE C 114 ? 0.3100 0.3363 0.2144 -0.1266 -0.0382 -0.0224 113 PHE D CZ    
6834  N  N     . ILE C 115 ? 0.2346 0.2839 0.2210 -0.0741 -0.0297 -0.0179 114 ILE D N     
6835  C  CA    . ILE C 115 ? 0.2313 0.2803 0.2218 -0.0734 -0.0212 -0.0227 114 ILE D CA    
6836  C  C     . ILE C 115 ? 0.2437 0.2809 0.2209 -0.0747 -0.0103 -0.0275 114 ILE D C     
6837  O  O     . ILE C 115 ? 0.2499 0.2824 0.2260 -0.0683 -0.0058 -0.0274 114 ILE D O     
6838  C  CB    . ILE C 115 ? 0.2183 0.2739 0.2265 -0.0630 -0.0191 -0.0221 114 ILE D CB    
6839  C  CG1   . ILE C 115 ? 0.2461 0.3134 0.2700 -0.0600 -0.0292 -0.0176 114 ILE D CG1   
6840  C  CG2   . ILE C 115 ? 0.2276 0.2828 0.2386 -0.0641 -0.0111 -0.0264 114 ILE D CG2   
6841  C  CD1   . ILE C 115 ? 0.2574 0.3294 0.2966 -0.0487 -0.0263 -0.0174 114 ILE D CD1   
6853  N  N     . CYS C 116 ? 0.2461 0.2784 0.2140 -0.0831 -0.0062 -0.0318 115 CYS D N     
6854  C  CA    . CYS C 116 ? 0.2516 0.2724 0.2086 -0.0846 0.0048  -0.0372 115 CYS D CA    
6855  C  C     . CYS C 116 ? 0.2627 0.2817 0.2296 -0.0759 0.0131  -0.0387 115 CYS D C     
6856  O  O     . CYS C 116 ? 0.2691 0.2942 0.2472 -0.0732 0.0125  -0.0379 115 CYS D O     
6857  C  CB    . CYS C 116 ? 0.2823 0.2984 0.2282 -0.0959 0.0069  -0.0419 115 CYS D CB    
6858  S  SG    . CYS C 116 ? 0.3226 0.3386 0.2522 -0.1082 -0.0020 -0.0406 115 CYS D SG    
6864  N  N     . THR C 117 ? 0.2728 0.2837 0.2358 -0.0715 0.0207  -0.0404 116 THR D N     
6865  C  CA    . THR C 117 ? 0.2861 0.2930 0.2557 -0.0649 0.0291  -0.0419 116 THR D CA    
6866  C  C     . THR C 117 ? 0.3170 0.3126 0.2781 -0.0695 0.0383  -0.0475 116 THR D C     
6867  O  O     . THR C 117 ? 0.3263 0.3164 0.2918 -0.0644 0.0457  -0.0486 116 THR D O     
6868  C  CB    . THR C 117 ? 0.2713 0.2784 0.2461 -0.0552 0.0301  -0.0390 116 THR D CB    
6869  O  OG1   . THR C 117 ? 0.2887 0.2900 0.2539 -0.0569 0.0317  -0.0399 116 THR D OG1   
6870  C  CG2   . THR C 117 ? 0.2901 0.3076 0.2743 -0.0505 0.0215  -0.0342 116 THR D CG2   
6878  N  N     . ALA C 118 ? 0.3071 0.2985 0.2558 -0.0791 0.0381  -0.0509 117 ALA D N     
6879  C  CA    . ALA C 118 ? 0.3064 0.2867 0.2463 -0.0849 0.0469  -0.0574 117 ALA D CA    
6880  C  C     . ALA C 118 ? 0.3033 0.2834 0.2309 -0.0971 0.0429  -0.0602 117 ALA D C     
6881  O  O     . ALA C 118 ? 0.3194 0.3072 0.2445 -0.1004 0.0334  -0.0565 117 ALA D O     
6882  C  CB    . ALA C 118 ? 0.3372 0.3094 0.2723 -0.0819 0.0542  -0.0597 117 ALA D CB    
6888  N  N     . LYS C 119 ? 0.3402 0.3108 0.2598 -0.1041 0.0502  -0.0669 118 LYS D N     
6889  C  CA    . LYS C 119 ? 0.3600 0.3279 0.2642 -0.1169 0.0482  -0.0709 118 LYS D CA    
6890  C  C     . LYS C 119 ? 0.4128 0.3797 0.3054 -0.1196 0.0467  -0.0706 118 LYS D C     
6891  O  O     . LYS C 119 ? 0.4226 0.3834 0.3141 -0.1150 0.0544  -0.0727 118 LYS D O     
6892  C  CB    . LYS C 119 ? 0.3605 0.3162 0.2582 -0.1230 0.0584  -0.0793 118 LYS D CB    
6893  C  CG    . LYS C 119 ? 0.4580 0.4090 0.3379 -0.1375 0.0578  -0.0851 118 LYS D CG    
6894  C  CD    . LYS C 119 ? 0.5121 0.4512 0.3892 -0.1426 0.0677  -0.0934 118 LYS D CD    
6895  C  CE    . LYS C 119 ? 0.6074 0.5445 0.4713 -0.1571 0.0647  -0.0981 118 LYS D CE    
6896  N  NZ    . LYS C 119 ? 0.6876 0.6178 0.5317 -0.1672 0.0679  -0.1042 118 LYS D NZ    
6910  N  N     . THR C 120 ? 0.4194 0.3922 0.3031 -0.1277 0.0368  -0.0678 119 THR D N     
6911  C  CA    . THR C 120 ? 0.3606 0.3324 0.2308 -0.1325 0.0345  -0.0670 119 THR D CA    
6912  C  C     . THR C 120 ? 0.4234 0.3931 0.2753 -0.1478 0.0306  -0.0700 119 THR D C     
6913  O  O     . THR C 120 ? 0.3972 0.3736 0.2432 -0.1533 0.0194  -0.0647 119 THR D O     
6914  C  CB    . THR C 120 ? 0.3864 0.3679 0.2639 -0.1262 0.0242  -0.0581 119 THR D CB    
6915  O  OG1   . THR C 120 ? 0.3624 0.3539 0.2469 -0.1280 0.0125  -0.0529 119 THR D OG1   
6916  C  CG2   . THR C 120 ? 0.3751 0.3577 0.2684 -0.1122 0.0287  -0.0559 119 THR D CG2   
6924  N  N     . GLU C 121 ? 0.4270 0.3868 0.2693 -0.1548 0.0401  -0.0788 120 GLU D N     
6925  C  CA    . GLU C 121 ? 0.4572 0.4146 0.2828 -0.1700 0.0369  -0.0827 120 GLU D CA    
6926  C  C     . GLU C 121 ? 0.4635 0.4200 0.2694 -0.1798 0.0331  -0.0821 120 GLU D C     
6927  O  O     . GLU C 121 ? 0.5075 0.4651 0.2994 -0.1927 0.0261  -0.0824 120 GLU D O     
6928  C  CB    . GLU C 121 ? 0.5055 0.4509 0.3261 -0.1746 0.0494  -0.0932 120 GLU D CB    
6929  C  CG    . GLU C 121 ? 0.5133 0.4473 0.3243 -0.1751 0.0627  -0.1009 120 GLU D CG    
6930  C  CD    . GLU C 121 ? 0.5323 0.4653 0.3597 -0.1601 0.0700  -0.0992 120 GLU D CD    
6931  O  OE1   . GLU C 121 ? 0.5283 0.4681 0.3735 -0.1492 0.0657  -0.0928 120 GLU D OE1   
6932  O  OE2   . GLU C 121 ? 0.5695 0.4950 0.3917 -0.1595 0.0802  -0.1046 120 GLU D OE2   
6939  N  N     . TRP C 122 ? 0.4502 0.4047 0.2539 -0.1750 0.0374  -0.0813 121 TRP D N     
6940  C  CA    . TRP C 122 ? 0.5205 0.4743 0.3052 -0.1845 0.0342  -0.0802 121 TRP D CA    
6941  C  C     . TRP C 122 ? 0.4860 0.4506 0.2711 -0.1864 0.0172  -0.0693 121 TRP D C     
6942  O  O     . TRP C 122 ? 0.5081 0.4725 0.2759 -0.1965 0.0117  -0.0670 121 TRP D O     
6943  C  CB    . TRP C 122 ? 0.5225 0.4716 0.3066 -0.1783 0.0441  -0.0821 121 TRP D CB    
6944  C  CG    . TRP C 122 ? 0.4689 0.4245 0.2729 -0.1631 0.0413  -0.0748 121 TRP D CG    
6945  C  CD1   . TRP C 122 ? 0.4271 0.3898 0.2332 -0.1597 0.0318  -0.0659 121 TRP D CD1   
6946  C  CD2   . TRP C 122 ? 0.4524 0.4077 0.2763 -0.1496 0.0477  -0.0755 121 TRP D CD2   
6947  N  NE1   . TRP C 122 ? 0.4761 0.4430 0.3022 -0.1452 0.0318  -0.0617 121 TRP D NE1   
6948  C  CE2   . TRP C 122 ? 0.4597 0.4224 0.2962 -0.1390 0.0413  -0.0672 121 TRP D CE2   
6949  C  CE3   . TRP C 122 ? 0.4529 0.4020 0.2849 -0.1459 0.0575  -0.0820 121 TRP D CE3   
6950  C  CZ2   . TRP C 122 ? 0.4272 0.3915 0.2826 -0.1256 0.0447  -0.0656 121 TRP D CZ2   
6951  C  CZ3   . TRP C 122 ? 0.4608 0.4115 0.3119 -0.1323 0.0604  -0.0795 121 TRP D CZ3   
6952  C  CH2   . TRP C 122 ? 0.4381 0.3968 0.3003 -0.1226 0.0539  -0.0714 121 TRP D CH2   
6963  N  N     . LEU C 123 ? 0.4510 0.4247 0.2556 -0.1773 0.0088  -0.0625 122 LEU D N     
6964  C  CA    . LEU C 123 ? 0.4275 0.4118 0.2363 -0.1786 -0.0077 -0.0524 122 LEU D CA    
6965  C  C     . LEU C 123 ? 0.4277 0.4157 0.2317 -0.1896 -0.0162 -0.0524 122 LEU D C     
6966  O  O     . LEU C 123 ? 0.4192 0.4158 0.2247 -0.1933 -0.0306 -0.0443 122 LEU D O     
6967  C  CB    . LEU C 123 ? 0.3802 0.3729 0.2139 -0.1629 -0.0115 -0.0460 122 LEU D CB    
6968  C  CG    . LEU C 123 ? 0.3807 0.3704 0.2198 -0.1520 -0.0044 -0.0454 122 LEU D CG    
6969  C  CD1   . LEU C 123 ? 0.3545 0.3519 0.2168 -0.1377 -0.0078 -0.0401 122 LEU D CD1   
6970  C  CD2   . LEU C 123 ? 0.4356 0.4243 0.2613 -0.1569 -0.0090 -0.0411 122 LEU D CD2   
6982  N  N     . ASP C 124 ? 0.4168 0.3984 0.2151 -0.1955 -0.0078 -0.0611 123 ASP D N     
6983  C  CA    . ASP C 124 ? 0.4593 0.4444 0.2542 -0.2059 -0.0153 -0.0615 123 ASP D CA    
6984  C  C     . ASP C 124 ? 0.4933 0.4788 0.2689 -0.2187 -0.0239 -0.0575 123 ASP D C     
6985  O  O     . ASP C 124 ? 0.4864 0.4643 0.2458 -0.2228 -0.0172 -0.0596 123 ASP D O     
6986  C  CB    . ASP C 124 ? 0.4892 0.4649 0.2799 -0.2102 -0.0031 -0.0722 123 ASP D CB    
6987  C  CG    . ASP C 124 ? 0.4613 0.4373 0.2738 -0.1967 0.0046  -0.0738 123 ASP D CG    
6988  O  OD1   . ASP C 124 ? 0.4266 0.4113 0.2585 -0.1842 0.0002  -0.0669 123 ASP D OD1   
6989  O  OD2   . ASP C 124 ? 0.4547 0.4215 0.2641 -0.1993 0.0153  -0.0824 123 ASP D OD2   
6994  N  N     . GLY C 125 ? 0.4615 0.4563 0.2420 -0.2225 -0.0376 -0.0499 124 GLY D N     
6995  C  CA    . GLY C 125 ? 0.4826 0.4782 0.2484 -0.2318 -0.0457 -0.0434 124 GLY D CA    
6996  C  C     . GLY C 125 ? 0.4699 0.4691 0.2348 -0.2291 -0.0545 -0.0340 124 GLY D C     
6997  O  O     . GLY C 125 ? 0.4871 0.4866 0.2402 -0.2368 -0.0619 -0.0275 124 GLY D O     
7001  N  N     . LYS C 126 ? 0.4502 0.4517 0.2267 -0.2189 -0.0539 -0.0331 125 LYS D N     
7002  C  CA    . LYS C 126 ? 0.4867 0.4912 0.2638 -0.2154 -0.0620 -0.0242 125 LYS D CA    
7003  C  C     . LYS C 126 ? 0.4451 0.4609 0.2458 -0.2053 -0.0737 -0.0167 125 LYS D C     
7004  O  O     . LYS C 126 ? 0.4982 0.5191 0.3030 -0.2038 -0.0858 -0.0064 125 LYS D O     
7005  C  CB    . LYS C 126 ? 0.5216 0.5173 0.2891 -0.2127 -0.0498 -0.0297 125 LYS D CB    
7006  C  CG    . LYS C 126 ? 0.5520 0.5378 0.2969 -0.2229 -0.0398 -0.0347 125 LYS D CG    
7007  C  CD    . LYS C 126 ? 0.6289 0.6053 0.3692 -0.2199 -0.0218 -0.0461 125 LYS D CD    
7008  C  CE    . LYS C 126 ? 0.7436 0.7114 0.4634 -0.2302 -0.0122 -0.0503 125 LYS D CE    
7009  N  NZ    . LYS C 126 ? 0.8805 0.8411 0.5986 -0.2255 0.0030  -0.0580 125 LYS D NZ    
7023  N  N     . HIS C 127 ? 0.4062 0.4250 0.2263 -0.1943 -0.0676 -0.0204 126 HIS D N     
7024  C  CA    . HIS C 127 ? 0.3852 0.4146 0.2322 -0.1813 -0.0746 -0.0137 126 HIS D CA    
7025  C  C     . HIS C 127 ? 0.3824 0.4196 0.2424 -0.1827 -0.0786 -0.0146 126 HIS D C     
7026  O  O     . HIS C 127 ? 0.3866 0.4193 0.2416 -0.1869 -0.0694 -0.0228 126 HIS D O     
7027  C  CB    . HIS C 127 ? 0.4019 0.4282 0.2611 -0.1665 -0.0629 -0.0167 126 HIS D CB    
7028  C  CG    . HIS C 127 ? 0.3897 0.4101 0.2391 -0.1645 -0.0604 -0.0147 126 HIS D CG    
7029  N  ND1   . HIS C 127 ? 0.3652 0.3904 0.2248 -0.1573 -0.0693 -0.0061 126 HIS D ND1   
7030  C  CD2   . HIS C 127 ? 0.4276 0.4377 0.2581 -0.1694 -0.0503 -0.0201 126 HIS D CD2   
7031  C  CE1   . HIS C 127 ? 0.3891 0.4073 0.2366 -0.1578 -0.0647 -0.0061 126 HIS D CE1   
7032  N  NE2   . HIS C 127 ? 0.4141 0.4236 0.2439 -0.1652 -0.0532 -0.0145 126 HIS D NE2   
7040  N  N     . VAL C 128 ? 0.3874 0.4366 0.2646 -0.1800 -0.0925 -0.0062 127 VAL D N     
7041  C  CA    . VAL C 128 ? 0.3849 0.4437 0.2765 -0.1819 -0.0977 -0.0061 127 VAL D CA    
7042  C  C     . VAL C 128 ? 0.3524 0.4147 0.2659 -0.1681 -0.0884 -0.0097 127 VAL D C     
7043  O  O     . VAL C 128 ? 0.3361 0.4043 0.2682 -0.1559 -0.0906 -0.0052 127 VAL D O     
7044  C  CB    . VAL C 128 ? 0.3773 0.4482 0.2804 -0.1845 -0.1164 0.0043  127 VAL D CB    
7045  C  CG1   . VAL C 128 ? 0.3724 0.4549 0.2946 -0.1849 -0.1210 0.0043  127 VAL D CG1   
7046  C  CG2   . VAL C 128 ? 0.4020 0.4666 0.2832 -0.1949 -0.1225 0.0092  127 VAL D CG2   
7056  N  N     . VAL C 129 ? 0.3531 0.4117 0.2646 -0.1707 -0.0783 -0.0176 128 VAL D N     
7057  C  CA    . VAL C 129 ? 0.3351 0.3973 0.2661 -0.1597 -0.0700 -0.0208 128 VAL D CA    
7058  C  C     . VAL C 129 ? 0.3294 0.4065 0.2816 -0.1590 -0.0799 -0.0163 128 VAL D C     
7059  O  O     . VAL C 129 ? 0.3424 0.4234 0.2903 -0.1704 -0.0873 -0.0158 128 VAL D O     
7060  C  CB    . VAL C 129 ? 0.3401 0.3920 0.2608 -0.1635 -0.0560 -0.0303 128 VAL D CB    
7061  C  CG1   . VAL C 129 ? 0.3246 0.3810 0.2649 -0.1547 -0.0491 -0.0327 128 VAL D CG1   
7062  C  CG2   . VAL C 129 ? 0.3427 0.3808 0.2476 -0.1614 -0.0446 -0.0351 128 VAL D CG2   
7072  N  N     . PHE C 130 ? 0.3107 0.3962 0.2861 -0.1460 -0.0797 -0.0136 129 PHE D N     
7073  C  CA    . PHE C 130 ? 0.3051 0.4059 0.3030 -0.1448 -0.0889 -0.0094 129 PHE D CA    
7074  C  C     . PHE C 130 ? 0.2875 0.3948 0.3069 -0.1339 -0.0810 -0.0119 129 PHE D C     
7075  O  O     . PHE C 130 ? 0.3089 0.4297 0.3490 -0.1322 -0.0874 -0.0090 129 PHE D O     
7076  C  CB    . PHE C 130 ? 0.3159 0.4250 0.3237 -0.1423 -0.1036 -0.0002 129 PHE D CB    
7077  C  CG    . PHE C 130 ? 0.2907 0.3987 0.3079 -0.1288 -0.1011 0.0022  129 PHE D CG    
7078  C  CD1   . PHE C 130 ? 0.2942 0.3908 0.2941 -0.1279 -0.0984 0.0026  129 PHE D CD1   
7079  C  CD2   . PHE C 130 ? 0.2923 0.4105 0.3353 -0.1173 -0.1007 0.0034  129 PHE D CD2   
7080  C  CE1   . PHE C 130 ? 0.2813 0.3768 0.2900 -0.1157 -0.0960 0.0046  129 PHE D CE1   
7081  C  CE2   . PHE C 130 ? 0.2936 0.4103 0.3445 -0.1054 -0.0983 0.0050  129 PHE D CE2   
7082  C  CZ    . PHE C 130 ? 0.2660 0.3712 0.2998 -0.1046 -0.0962 0.0057  129 PHE D CZ    
7092  N  N     . GLY C 131 ? 0.2796 0.3781 0.2949 -0.1272 -0.0675 -0.0171 130 GLY D N     
7093  C  CA    . GLY C 131 ? 0.2745 0.3784 0.3071 -0.1193 -0.0598 -0.0197 130 GLY D CA    
7094  C  C     . GLY C 131 ? 0.2653 0.3570 0.2883 -0.1148 -0.0454 -0.0253 130 GLY D C     
7095  O  O     . GLY C 131 ? 0.2704 0.3495 0.2741 -0.1189 -0.0406 -0.0283 130 GLY D O     
7099  N  N     . LYS C 132 ? 0.2637 0.3596 0.3013 -0.1063 -0.0385 -0.0267 131 LYS D N     
7100  C  CA    . LYS C 132 ? 0.2619 0.3472 0.2930 -0.1014 -0.0256 -0.0310 131 LYS D CA    
7101  C  C     . LYS C 132 ? 0.2623 0.3549 0.3110 -0.0905 -0.0217 -0.0301 131 LYS D C     
7102  O  O     . LYS C 132 ? 0.2952 0.4009 0.3616 -0.0891 -0.0259 -0.0284 131 LYS D O     
7103  C  CB    . LYS C 132 ? 0.2911 0.3695 0.3136 -0.1096 -0.0184 -0.0362 131 LYS D CB    
7104  C  CG    . LYS C 132 ? 0.3674 0.4563 0.4044 -0.1124 -0.0188 -0.0367 131 LYS D CG    
7105  C  CD    . LYS C 132 ? 0.4059 0.4852 0.4351 -0.1178 -0.0088 -0.0420 131 LYS D CD    
7106  C  CE    . LYS C 132 ? 0.4608 0.5501 0.5035 -0.1218 -0.0089 -0.0425 131 LYS D CE    
7107  N  NZ    . LYS C 132 ? 0.5926 0.6744 0.6242 -0.1336 -0.0063 -0.0467 131 LYS D NZ    
7121  N  N     . VAL C 133 ? 0.2556 0.3398 0.2996 -0.0830 -0.0135 -0.0315 132 VAL D N     
7122  C  CA    . VAL C 133 ? 0.2458 0.3347 0.3029 -0.0738 -0.0080 -0.0316 132 VAL D CA    
7123  C  C     . VAL C 133 ? 0.2600 0.3531 0.3241 -0.0773 -0.0028 -0.0340 132 VAL D C     
7124  O  O     . VAL C 133 ? 0.2572 0.3421 0.3111 -0.0839 0.0023  -0.0370 132 VAL D O     
7125  C  CB    . VAL C 133 ? 0.2735 0.3510 0.3214 -0.0671 -0.0001 -0.0326 132 VAL D CB    
7126  C  CG1   . VAL C 133 ? 0.2296 0.3115 0.2889 -0.0587 0.0057  -0.0327 132 VAL D CG1   
7127  C  CG2   . VAL C 133 ? 0.2198 0.2942 0.2620 -0.0640 -0.0053 -0.0300 132 VAL D CG2   
7137  N  N     . LYS C 134 ? 0.2827 0.3889 0.3651 -0.0731 -0.0041 -0.0330 133 LYS D N     
7138  C  CA    . LYS C 134 ? 0.2847 0.3964 0.3757 -0.0754 0.0018  -0.0350 133 LYS D CA    
7139  C  C     . LYS C 134 ? 0.2956 0.4035 0.3871 -0.0679 0.0114  -0.0361 133 LYS D C     
7140  O  O     . LYS C 134 ? 0.3735 0.4715 0.4555 -0.0700 0.0193  -0.0379 133 LYS D O     
7141  C  CB    . LYS C 134 ? 0.2826 0.4115 0.3936 -0.0760 -0.0048 -0.0336 133 LYS D CB    
7142  C  CG    . LYS C 134 ? 0.4214 0.5576 0.5418 -0.0803 0.0004  -0.0357 133 LYS D CG    
7143  C  CD    . LYS C 134 ? 0.4381 0.5928 0.5822 -0.0782 -0.0039 -0.0347 133 LYS D CD    
7144  C  CE    . LYS C 134 ? 0.4115 0.5753 0.5629 -0.0853 -0.0151 -0.0325 133 LYS D CE    
7145  N  NZ    . LYS C 134 ? 0.5023 0.6835 0.6764 -0.0867 -0.0155 -0.0330 133 LYS D NZ    
7159  N  N     . GLU C 135 ? 0.2561 0.3709 0.3583 -0.0594 0.0108  -0.0350 134 GLU D N     
7160  C  CA    . GLU C 135 ? 0.3038 0.4146 0.4046 -0.0526 0.0191  -0.0357 134 GLU D CA    
7161  C  C     . GLU C 135 ? 0.2450 0.3494 0.3396 -0.0454 0.0172  -0.0343 134 GLU D C     
7162  O  O     . GLU C 135 ? 0.2744 0.3814 0.3714 -0.0440 0.0092  -0.0324 134 GLU D O     
7163  C  CB    . GLU C 135 ? 0.3559 0.4799 0.4737 -0.0489 0.0218  -0.0367 134 GLU D CB    
7164  C  CG    . GLU C 135 ? 0.4143 0.5500 0.5444 -0.0556 0.0203  -0.0376 134 GLU D CG    
7165  C  CD    . GLU C 135 ? 0.4937 0.6459 0.6453 -0.0511 0.0188  -0.0382 134 GLU D CD    
7166  O  OE1   . GLU C 135 ? 0.4432 0.6054 0.6075 -0.0518 0.0099  -0.0368 134 GLU D OE1   
7167  O  OE2   . GLU C 135 ? 0.4243 0.5795 0.5804 -0.0472 0.0267  -0.0401 134 GLU D OE2   
7174  N  N     . GLY C 136 ? 0.2603 0.3561 0.3470 -0.0411 0.0242  -0.0346 135 GLY D N     
7175  C  CA    . GLY C 136 ? 0.2426 0.3330 0.3246 -0.0341 0.0232  -0.0333 135 GLY D CA    
7176  C  C     . GLY C 136 ? 0.2351 0.3131 0.3023 -0.0356 0.0224  -0.0326 135 GLY D C     
7177  O  O     . GLY C 136 ? 0.2441 0.3192 0.3085 -0.0308 0.0194  -0.0311 135 GLY D O     
7181  N  N     . MET C 137 ? 0.2523 0.3226 0.3101 -0.0422 0.0253  -0.0338 136 MET D N     
7182  C  CA    . MET C 137 ? 0.2419 0.3000 0.2861 -0.0433 0.0264  -0.0340 136 MET D CA    
7183  C  C     . MET C 137 ? 0.2501 0.3019 0.2910 -0.0359 0.0307  -0.0329 136 MET D C     
7184  O  O     . MET C 137 ? 0.2075 0.2531 0.2414 -0.0339 0.0295  -0.0322 136 MET D O     
7185  C  CB    . MET C 137 ? 0.2686 0.3180 0.3041 -0.0507 0.0313  -0.0364 136 MET D CB    
7186  C  CG    . MET C 137 ? 0.3142 0.3529 0.3367 -0.0543 0.0315  -0.0378 136 MET D CG    
7187  S  SD    . MET C 137 ? 0.2908 0.3337 0.3096 -0.0573 0.0215  -0.0365 136 MET D SD    
7188  C  CE    . MET C 137 ? 0.2764 0.3065 0.2819 -0.0555 0.0254  -0.0373 136 MET D CE    
7198  N  N     . ASN C 138 ? 0.2385 0.2920 0.2840 -0.0321 0.0357  -0.0326 137 ASN D N     
7199  C  CA    . ASN C 138 ? 0.2705 0.3180 0.3123 -0.0257 0.0390  -0.0312 137 ASN D CA    
7200  C  C     . ASN C 138 ? 0.2190 0.2706 0.2640 -0.0198 0.0338  -0.0299 137 ASN D C     
7201  O  O     . ASN C 138 ? 0.2376 0.2833 0.2778 -0.0154 0.0348  -0.0286 137 ASN D O     
7202  C  CB    . ASN C 138 ? 0.3315 0.3807 0.3767 -0.0238 0.0446  -0.0307 137 ASN D CB    
7203  C  CG    . ASN C 138 ? 0.2965 0.3583 0.3527 -0.0216 0.0428  -0.0313 137 ASN D CG    
7204  O  OD1   . ASN C 138 ? 0.2859 0.3559 0.3495 -0.0252 0.0402  -0.0326 137 ASN D OD1   
7205  N  ND2   . ASN C 138 ? 0.3443 0.4079 0.4022 -0.0157 0.0442  -0.0307 137 ASN D ND2   
7212  N  N     . ILE C 139 ? 0.2232 0.2849 0.2773 -0.0195 0.0283  -0.0300 138 ILE D N     
7213  C  CA    . ILE C 139 ? 0.2177 0.2823 0.2754 -0.0141 0.0228  -0.0287 138 ILE D CA    
7214  C  C     . ILE C 139 ? 0.2226 0.2814 0.2722 -0.0163 0.0182  -0.0274 138 ILE D C     
7215  O  O     . ILE C 139 ? 0.2412 0.2966 0.2880 -0.0121 0.0164  -0.0259 138 ILE D O     
7216  C  CB    . ILE C 139 ? 0.2273 0.3042 0.2992 -0.0129 0.0180  -0.0291 138 ILE D CB    
7217  C  CG1   . ILE C 139 ? 0.2781 0.3612 0.3577 -0.0109 0.0238  -0.0310 138 ILE D CG1   
7218  C  CG2   . ILE C 139 ? 0.2166 0.2954 0.2930 -0.0074 0.0120  -0.0276 138 ILE D CG2   
7219  C  CD1   . ILE C 139 ? 0.3113 0.3900 0.3869 -0.0051 0.0283  -0.0310 138 ILE D CD1   
7231  N  N     . VAL C 140 ? 0.2098 0.2674 0.2550 -0.0234 0.0164  -0.0280 139 VAL D N     
7232  C  CA    . VAL C 140 ? 0.2056 0.2569 0.2407 -0.0269 0.0132  -0.0272 139 VAL D CA    
7233  C  C     . VAL C 140 ? 0.2517 0.2922 0.2770 -0.0252 0.0197  -0.0279 139 VAL D C     
7234  O  O     . VAL C 140 ? 0.2441 0.2803 0.2638 -0.0238 0.0180  -0.0267 139 VAL D O     
7235  C  CB    . VAL C 140 ? 0.2365 0.2883 0.2674 -0.0360 0.0107  -0.0283 139 VAL D CB    
7236  C  CG1   . VAL C 140 ? 0.2469 0.2919 0.2655 -0.0403 0.0080  -0.0279 139 VAL D CG1   
7237  C  CG2   . VAL C 140 ? 0.2217 0.2851 0.2642 -0.0374 0.0034  -0.0270 139 VAL D CG2   
7247  N  N     . GLU C 141 ? 0.2514 0.2875 0.2754 -0.0255 0.0269  -0.0295 140 GLU D N     
7248  C  CA    . GLU C 141 ? 0.2647 0.2913 0.2825 -0.0229 0.0328  -0.0296 140 GLU D CA    
7249  C  C     . GLU C 141 ? 0.2420 0.2697 0.2628 -0.0152 0.0316  -0.0272 140 GLU D C     
7250  O  O     . GLU C 141 ? 0.2595 0.2821 0.2756 -0.0133 0.0319  -0.0265 140 GLU D O     
7251  C  CB    . GLU C 141 ? 0.3094 0.3315 0.3272 -0.0241 0.0399  -0.0308 140 GLU D CB    
7252  C  CG    . GLU C 141 ? 0.3495 0.3669 0.3622 -0.0320 0.0423  -0.0337 140 GLU D CG    
7253  C  CD    . GLU C 141 ? 0.4115 0.4277 0.4272 -0.0340 0.0473  -0.0343 140 GLU D CD    
7254  O  OE1   . GLU C 141 ? 0.4069 0.4248 0.4272 -0.0293 0.0495  -0.0323 140 GLU D OE1   
7255  O  OE2   . GLU C 141 ? 0.3977 0.4110 0.4105 -0.0408 0.0490  -0.0368 140 GLU D OE2   
7262  N  N     . ALA C 142 ? 0.2291 0.2638 0.2579 -0.0111 0.0305  -0.0264 141 ALA D N     
7263  C  CA    . ALA C 142 ? 0.2050 0.2407 0.2362 -0.0044 0.0293  -0.0247 141 ALA D CA    
7264  C  C     . ALA C 142 ? 0.2632 0.2996 0.2936 -0.0033 0.0231  -0.0235 141 ALA D C     
7265  O  O     . ALA C 142 ? 0.2377 0.2707 0.2658 0.0005  0.0228  -0.0221 141 ALA D O     
7266  C  CB    . ALA C 142 ? 0.2702 0.3135 0.3096 -0.0011 0.0294  -0.0251 141 ALA D CB    
7272  N  N     . MET C 143 ? 0.2312 0.2714 0.2627 -0.0073 0.0177  -0.0235 142 MET D N     
7273  C  CA    . MET C 143 ? 0.2207 0.2608 0.2507 -0.0068 0.0114  -0.0215 142 MET D CA    
7274  C  C     . MET C 143 ? 0.2473 0.2789 0.2667 -0.0087 0.0139  -0.0212 142 MET D C     
7275  O  O     . MET C 143 ? 0.2511 0.2811 0.2689 -0.0065 0.0108  -0.0193 142 MET D O     
7276  C  CB    . MET C 143 ? 0.2396 0.2851 0.2722 -0.0115 0.0043  -0.0207 142 MET D CB    
7277  C  CG    . MET C 143 ? 0.2254 0.2803 0.2712 -0.0086 0.0001  -0.0204 142 MET D CG    
7278  S  SD    . MET C 143 ? 0.3183 0.3810 0.3697 -0.0153 -0.0055 -0.0202 142 MET D SD    
7279  C  CE    . MET C 143 ? 0.2500 0.3102 0.2956 -0.0181 -0.0146 -0.0164 142 MET D CE    
7289  N  N     . GLU C 144 ? 0.2158 0.2417 0.2289 -0.0126 0.0198  -0.0233 143 GLU D N     
7290  C  CA    . GLU C 144 ? 0.2391 0.2574 0.2438 -0.0142 0.0233  -0.0238 143 GLU D CA    
7291  C  C     . GLU C 144 ? 0.2776 0.2933 0.2844 -0.0076 0.0258  -0.0223 143 GLU D C     
7292  O  O     . GLU C 144 ? 0.2731 0.2843 0.2753 -0.0079 0.0274  -0.0221 143 GLU D O     
7293  C  CB    . GLU C 144 ? 0.2576 0.2697 0.2569 -0.0189 0.0301  -0.0269 143 GLU D CB    
7294  C  CG    . GLU C 144 ? 0.2487 0.2613 0.2428 -0.0271 0.0281  -0.0290 143 GLU D CG    
7295  C  CD    . GLU C 144 ? 0.2954 0.3001 0.2827 -0.0322 0.0353  -0.0328 143 GLU D CD    
7296  O  OE1   . GLU C 144 ? 0.3322 0.3329 0.3227 -0.0295 0.0415  -0.0339 143 GLU D OE1   
7297  O  OE2   . GLU C 144 ? 0.3182 0.3200 0.2966 -0.0392 0.0349  -0.0350 143 GLU D OE2   
7304  N  N     . ARG C 145 ? 0.2740 0.2929 0.2875 -0.0023 0.0262  -0.0214 144 ARG D N     
7305  C  CA    . ARG C 145 ? 0.2670 0.2840 0.2820 0.0034  0.0274  -0.0196 144 ARG D CA    
7306  C  C     . ARG C 145 ? 0.2898 0.3074 0.3040 0.0049  0.0223  -0.0178 144 ARG D C     
7307  O  O     . ARG C 145 ? 0.3078 0.3228 0.3217 0.0081  0.0234  -0.0165 144 ARG D O     
7308  C  CB    . ARG C 145 ? 0.3046 0.3258 0.3256 0.0079  0.0274  -0.0191 144 ARG D CB    
7309  C  CG    . ARG C 145 ? 0.2959 0.3163 0.3176 0.0067  0.0325  -0.0200 144 ARG D CG    
7310  C  CD    . ARG C 145 ? 0.3352 0.3604 0.3616 0.0104  0.0323  -0.0196 144 ARG D CD    
7311  N  NE    . ARG C 145 ? 0.3878 0.4135 0.4150 0.0085  0.0367  -0.0202 144 ARG D NE    
7312  C  CZ    . ARG C 145 ? 0.3392 0.3710 0.3705 0.0093  0.0370  -0.0211 144 ARG D CZ    
7313  N  NH1   . ARG C 145 ? 0.3550 0.3928 0.3910 0.0124  0.0335  -0.0218 144 ARG D NH1   
7314  N  NH2   . ARG C 145 ? 0.3935 0.4254 0.4249 0.0066  0.0413  -0.0214 144 ARG D NH2   
7328  N  N     . PHE C 146 ? 0.2494 0.2709 0.2643 0.0027  0.0162  -0.0173 145 PHE D N     
7329  C  CA    . PHE C 146 ? 0.2750 0.2972 0.2901 0.0042  0.0103  -0.0150 145 PHE D CA    
7330  C  C     . PHE C 146 ? 0.2562 0.2758 0.2637 -0.0018 0.0078  -0.0141 145 PHE D C     
7331  O  O     . PHE C 146 ? 0.2854 0.3060 0.2930 -0.0020 0.0015  -0.0116 145 PHE D O     
7332  C  CB    . PHE C 146 ? 0.3078 0.3362 0.3314 0.0072  0.0045  -0.0144 145 PHE D CB    
7333  C  CG    . PHE C 146 ? 0.3077 0.3389 0.3374 0.0120  0.0078  -0.0159 145 PHE D CG    
7334  C  CD1   . PHE C 146 ? 0.3608 0.3895 0.3901 0.0163  0.0103  -0.0155 145 PHE D CD1   
7335  C  CD2   . PHE C 146 ? 0.3157 0.3520 0.3505 0.0112  0.0088  -0.0177 145 PHE D CD2   
7336  C  CE1   . PHE C 146 ? 0.3550 0.3860 0.3878 0.0196  0.0135  -0.0168 145 PHE D CE1   
7337  C  CE2   . PHE C 146 ? 0.3423 0.3812 0.3814 0.0146  0.0126  -0.0192 145 PHE D CE2   
7338  C  CZ    . PHE C 146 ? 0.3303 0.3662 0.3676 0.0186  0.0149  -0.0187 145 PHE D CZ    
7348  N  N     . GLY C 147 ? 0.2896 0.3056 0.2902 -0.0070 0.0126  -0.0163 146 GLY D N     
7349  C  CA    . GLY C 147 ? 0.2899 0.3029 0.2812 -0.0137 0.0115  -0.0161 146 GLY D CA    
7350  C  C     . GLY C 147 ? 0.3211 0.3287 0.3074 -0.0139 0.0170  -0.0168 146 GLY D C     
7351  O  O     . GLY C 147 ? 0.3170 0.3236 0.3081 -0.0082 0.0202  -0.0164 146 GLY D O     
7355  N  N     . SER C 148 ? 0.2780 0.2825 0.2545 -0.0209 0.0179  -0.0177 147 SER D N     
7356  C  CA    . SER C 148 ? 0.3078 0.3079 0.2798 -0.0220 0.0237  -0.0188 147 SER D CA    
7357  C  C     . SER C 148 ? 0.3284 0.3248 0.2887 -0.0312 0.0272  -0.0220 147 SER D C     
7358  O  O     . SER C 148 ? 0.2985 0.2959 0.2533 -0.0368 0.0234  -0.0223 147 SER D O     
7359  C  CB    . SER C 148 ? 0.3390 0.3404 0.3118 -0.0200 0.0189  -0.0148 147 SER D CB    
7360  O  OG    . SER C 148 ? 0.3337 0.3360 0.2996 -0.0257 0.0116  -0.0121 147 SER D OG    
7366  N  N     . ARG C 149 ? 0.3282 0.3205 0.2847 -0.0329 0.0347  -0.0246 148 ARG D N     
7367  C  CA    . ARG C 149 ? 0.3629 0.3511 0.3076 -0.0420 0.0397  -0.0288 148 ARG D CA    
7368  C  C     . ARG C 149 ? 0.3610 0.3505 0.2942 -0.0501 0.0321  -0.0262 148 ARG D C     
7369  O  O     . ARG C 149 ? 0.3487 0.3362 0.2719 -0.0583 0.0326  -0.0290 148 ARG D O     
7370  C  CB    . ARG C 149 ? 0.3805 0.3653 0.3247 -0.0419 0.0486  -0.0315 148 ARG D CB    
7371  C  CG    . ARG C 149 ? 0.4015 0.3819 0.3331 -0.0514 0.0551  -0.0366 148 ARG D CG    
7372  C  CD    . ARG C 149 ? 0.4030 0.3804 0.3389 -0.0494 0.0659  -0.0405 148 ARG D CD    
7373  N  NE    . ARG C 149 ? 0.5211 0.4948 0.4442 -0.0590 0.0725  -0.0456 148 ARG D NE    
7374  C  CZ    . ARG C 149 ? 0.4834 0.4583 0.3961 -0.0654 0.0700  -0.0436 148 ARG D CZ    
7375  N  NH1   . ARG C 149 ? 0.5022 0.4814 0.4174 -0.0625 0.0613  -0.0367 148 ARG D NH1   
7376  N  NH2   . ARG C 149 ? 0.5625 0.5338 0.4616 -0.0753 0.0765  -0.0488 148 ARG D NH2   
7390  N  N     . ASN C 150 ? 0.3305 0.3227 0.2643 -0.0488 0.0246  -0.0208 149 ASN D N     
7391  C  CA    . ASN C 150 ? 0.3462 0.3392 0.2693 -0.0568 0.0164  -0.0173 149 ASN D CA    
7392  C  C     . ASN C 150 ? 0.3498 0.3476 0.2791 -0.0546 0.0054  -0.0128 149 ASN D C     
7393  O  O     . ASN C 150 ? 0.3764 0.3754 0.2994 -0.0603 -0.0033 -0.0087 149 ASN D O     
7394  C  CB    . ASN C 150 ? 0.3595 0.3516 0.2775 -0.0591 0.0146  -0.0138 149 ASN D CB    
7395  C  CG    . ASN C 150 ? 0.4308 0.4261 0.3591 -0.0517 0.0066  -0.0079 149 ASN D CG    
7396  O  OD1   . ASN C 150 ? 0.3364 0.3345 0.2767 -0.0436 0.0044  -0.0073 149 ASN D OD1   
7397  N  ND2   . ASN C 150 ? 0.3661 0.3604 0.2890 -0.0549 0.0025  -0.0036 149 ASN D ND2   
7404  N  N     . GLY C 151 ? 0.3174 0.3181 0.2592 -0.0468 0.0057  -0.0136 150 GLY D N     
7405  C  CA    . GLY C 151 ? 0.3231 0.3291 0.2726 -0.0445 -0.0028 -0.0108 150 GLY D CA    
7406  C  C     . GLY C 151 ? 0.2871 0.2967 0.2478 -0.0368 -0.0097 -0.0062 150 GLY D C     
7407  O  O     . GLY C 151 ? 0.2879 0.3022 0.2582 -0.0331 -0.0150 -0.0048 150 GLY D O     
7411  N  N     . LYS C 152 ? 0.3043 0.3116 0.2642 -0.0347 -0.0097 -0.0040 151 LYS D N     
7412  C  CA    . LYS C 152 ? 0.3424 0.3522 0.3133 -0.0271 -0.0154 -0.0005 151 LYS D CA    
7413  C  C     . LYS C 152 ? 0.2854 0.2981 0.2679 -0.0188 -0.0118 -0.0032 151 LYS D C     
7414  O  O     . LYS C 152 ? 0.2874 0.2982 0.2700 -0.0166 -0.0034 -0.0066 151 LYS D O     
7415  C  CB    . LYS C 152 ? 0.3512 0.3579 0.3199 -0.0259 -0.0144 0.0014  151 LYS D CB    
7416  C  CG    . LYS C 152 ? 0.4449 0.4528 0.4222 -0.0206 -0.0224 0.0057  151 LYS D CG    
7417  C  CD    . LYS C 152 ? 0.5206 0.5296 0.4971 -0.0245 -0.0333 0.0106  151 LYS D CD    
7418  C  CE    . LYS C 152 ? 0.5516 0.5576 0.5129 -0.0352 -0.0351 0.0129  151 LYS D CE    
7419  N  NZ    . LYS C 152 ? 0.5773 0.5857 0.5378 -0.0399 -0.0442 0.0162  151 LYS D NZ    
7433  N  N     . THR C 153 ? 0.2879 0.3048 0.2806 -0.0141 -0.0181 -0.0014 152 THR D N     
7434  C  CA    . THR C 153 ? 0.2702 0.2902 0.2729 -0.0071 -0.0146 -0.0040 152 THR D CA    
7435  C  C     . THR C 153 ? 0.3442 0.3632 0.3525 -0.0002 -0.0142 -0.0034 152 THR D C     
7436  O  O     . THR C 153 ? 0.3429 0.3607 0.3522 0.0006  -0.0197 -0.0003 152 THR D O     
7437  C  CB    . THR C 153 ? 0.2641 0.2901 0.2761 -0.0057 -0.0199 -0.0038 152 THR D CB    
7438  O  OG1   . THR C 153 ? 0.3103 0.3380 0.3288 -0.0036 -0.0287 -0.0001 152 THR D OG1   
7439  C  CG2   . THR C 153 ? 0.2880 0.3155 0.2946 -0.0132 -0.0209 -0.0044 152 THR D CG2   
7447  N  N     . SER C 154 ? 0.3121 0.3316 0.3240 0.0043  -0.0080 -0.0061 153 SER D N     
7448  C  CA    . SER C 154 ? 0.3213 0.3398 0.3373 0.0101  -0.0071 -0.0058 153 SER D CA    
7449  C  C     . SER C 154 ? 0.3548 0.3771 0.3804 0.0155  -0.0108 -0.0064 153 SER D C     
7450  O  O     . SER C 154 ? 0.3525 0.3738 0.3812 0.0198  -0.0118 -0.0061 153 SER D O     
7451  C  CB    . SER C 154 ? 0.2687 0.2853 0.2830 0.0117  0.0008  -0.0078 153 SER D CB    
7452  O  OG    . SER C 154 ? 0.3440 0.3627 0.3606 0.0122  0.0046  -0.0102 153 SER D OG    
7458  N  N     . LYS C 155 ? 0.3017 0.3285 0.3325 0.0152  -0.0126 -0.0074 154 LYS D N     
7459  C  CA    . LYS C 155 ? 0.2996 0.3308 0.3409 0.0199  -0.0156 -0.0086 154 LYS D CA    
7460  C  C     . LYS C 155 ? 0.3405 0.3755 0.3866 0.0172  -0.0219 -0.0071 154 LYS D C     
7461  O  O     . LYS C 155 ? 0.3263 0.3610 0.3663 0.0114  -0.0225 -0.0060 154 LYS D O     
7462  C  CB    . LYS C 155 ? 0.3170 0.3512 0.3616 0.0227  -0.0094 -0.0121 154 LYS D CB    
7463  C  CG    . LYS C 155 ? 0.3078 0.3387 0.3490 0.0259  -0.0047 -0.0129 154 LYS D CG    
7464  C  CD    . LYS C 155 ? 0.3604 0.3944 0.4042 0.0281  0.0006  -0.0159 154 LYS D CD    
7465  C  CE    . LYS C 155 ? 0.4516 0.4820 0.4902 0.0298  0.0049  -0.0156 154 LYS D CE    
7466  N  NZ    . LYS C 155 ? 0.5835 0.6139 0.6248 0.0338  0.0031  -0.0165 154 LYS D NZ    
7480  N  N     . LYS C 156 ? 0.3417 0.3803 0.3990 0.0211  -0.0267 -0.0072 155 LYS D N     
7481  C  CA    . LYS C 156 ? 0.3296 0.3724 0.3940 0.0190  -0.0339 -0.0050 155 LYS D CA    
7482  C  C     . LYS C 156 ? 0.3375 0.3875 0.4084 0.0186  -0.0306 -0.0081 155 LYS D C     
7483  O  O     . LYS C 156 ? 0.3345 0.3885 0.4139 0.0233  -0.0268 -0.0117 155 LYS D O     
7484  C  CB    . LYS C 156 ? 0.3448 0.3880 0.4204 0.0235  -0.0411 -0.0033 155 LYS D CB    
7485  C  CG    . LYS C 156 ? 0.4614 0.5061 0.5411 0.0200  -0.0509 0.0016  155 LYS D CG    
7486  C  CD    . LYS C 156 ? 0.5271 0.5717 0.6202 0.0249  -0.0586 0.0036  155 LYS D CD    
7487  C  CE    . LYS C 156 ? 0.5210 0.5730 0.6316 0.0308  -0.0571 -0.0007 155 LYS D CE    
7488  N  NZ    . LYS C 156 ? 0.5458 0.6001 0.6735 0.0343  -0.0661 0.0018  155 LYS D NZ    
7502  N  N     . ILE C 157 ? 0.3226 0.3741 0.3890 0.0125  -0.0320 -0.0068 156 ILE D N     
7503  C  CA    . ILE C 157 ? 0.2592 0.3169 0.3300 0.0105  -0.0289 -0.0094 156 ILE D CA    
7504  C  C     . ILE C 157 ? 0.2924 0.3569 0.3750 0.0095  -0.0376 -0.0070 156 ILE D C     
7505  O  O     . ILE C 157 ? 0.3096 0.3725 0.3877 0.0046  -0.0447 -0.0028 156 ILE D O     
7506  C  CB    . ILE C 157 ? 0.2942 0.3483 0.3516 0.0037  -0.0245 -0.0099 156 ILE D CB    
7507  C  CG1   . ILE C 157 ? 0.3259 0.3723 0.3722 0.0045  -0.0179 -0.0107 156 ILE D CG1   
7508  C  CG2   . ILE C 157 ? 0.2963 0.3557 0.3578 0.0020  -0.0200 -0.0129 156 ILE D CG2   
7509  C  CD1   . ILE C 157 ? 0.3404 0.3871 0.3911 0.0110  -0.0121 -0.0134 156 ILE D CD1   
7521  N  N     . THR C 158 ? 0.3027 0.3751 0.4006 0.0136  -0.0370 -0.0095 157 THR D N     
7522  C  CA    . THR C 158 ? 0.2704 0.3500 0.3831 0.0139  -0.0456 -0.0071 157 THR D CA    
7523  C  C     . THR C 158 ? 0.2548 0.3440 0.3774 0.0122  -0.0433 -0.0097 157 THR D C     
7524  O  O     . THR C 158 ? 0.2566 0.3474 0.3774 0.0126  -0.0344 -0.0140 157 THR D O     
7525  C  CB    . THR C 158 ? 0.3206 0.4014 0.4480 0.0217  -0.0490 -0.0073 157 THR D CB    
7526  O  OG1   . THR C 158 ? 0.3132 0.3960 0.4452 0.0270  -0.0401 -0.0132 157 THR D OG1   
7527  C  CG2   . THR C 158 ? 0.3230 0.3947 0.4424 0.0224  -0.0535 -0.0037 157 THR D CG2   
7535  N  N     . ILE C 159 ? 0.2583 0.3539 0.3915 0.0099  -0.0521 -0.0064 158 ILE D N     
7536  C  CA    . ILE C 159 ? 0.2723 0.3793 0.4206 0.0092  -0.0521 -0.0082 158 ILE D CA    
7537  C  C     . ILE C 159 ? 0.3222 0.4354 0.4918 0.0177  -0.0531 -0.0102 158 ILE D C     
7538  O  O     . ILE C 159 ? 0.2946 0.4105 0.4772 0.0200  -0.0625 -0.0065 158 ILE D O     
7539  C  CB    . ILE C 159 ? 0.3131 0.4241 0.4623 0.0019  -0.0618 -0.0034 158 ILE D CB    
7540  C  CG1   . ILE C 159 ? 0.3142 0.4178 0.4407 -0.0068 -0.0594 -0.0027 158 ILE D CG1   
7541  C  CG2   . ILE C 159 ? 0.2588 0.3827 0.4265 0.0015  -0.0629 -0.0048 158 ILE D CG2   
7542  C  CD1   . ILE C 159 ? 0.2724 0.3774 0.3945 -0.0155 -0.0699 0.0025  158 ILE D CD1   
7554  N  N     . ALA C 160 ? 0.2944 0.4096 0.4677 0.0223  -0.0431 -0.0162 159 ALA D N     
7555  C  CA    . ALA C 160 ? 0.3262 0.4468 0.5188 0.0302  -0.0422 -0.0195 159 ALA D CA    
7556  C  C     . ALA C 160 ? 0.3333 0.4672 0.5486 0.0307  -0.0456 -0.0200 159 ALA D C     
7557  O  O     . ALA C 160 ? 0.2927 0.4312 0.5277 0.0364  -0.0505 -0.0199 159 ALA D O     
7558  C  CB    . ALA C 160 ? 0.3540 0.4728 0.5418 0.0338  -0.0302 -0.0259 159 ALA D CB    
7564  N  N     . ASP C 161 ? 0.2871 0.4273 0.5011 0.0248  -0.0434 -0.0204 160 ASP D N     
7565  C  CA    . ASP C 161 ? 0.2597 0.4134 0.4946 0.0239  -0.0470 -0.0203 160 ASP D CA    
7566  C  C     . ASP C 161 ? 0.2868 0.4416 0.5112 0.0143  -0.0502 -0.0170 160 ASP D C     
7567  O  O     . ASP C 161 ? 0.2419 0.3878 0.4441 0.0093  -0.0462 -0.0168 160 ASP D O     
7568  C  CB    . ASP C 161 ? 0.2975 0.4606 0.5462 0.0275  -0.0363 -0.0276 160 ASP D CB    
7569  C  CG    . ASP C 161 ? 0.3378 0.5158 0.6156 0.0299  -0.0405 -0.0281 160 ASP D CG    
7570  O  OD1   . ASP C 161 ? 0.3042 0.4857 0.5923 0.0287  -0.0526 -0.0223 160 ASP D OD1   
7571  O  OD2   . ASP C 161 ? 0.3956 0.5826 0.6867 0.0327  -0.0316 -0.0344 160 ASP D OD2   
7576  N  N     . CYS C 162 ? 0.2425 0.4083 0.4835 0.0118  -0.0574 -0.0146 161 CYS D N     
7577  C  CA    . CYS C 162 ? 0.2250 0.3934 0.4580 0.0023  -0.0604 -0.0122 161 CYS D CA    
7578  C  C     . CYS C 162 ? 0.2935 0.4773 0.5523 0.0018  -0.0672 -0.0107 161 CYS D C     
7579  O  O     . CYS C 162 ? 0.2644 0.4544 0.5446 0.0083  -0.0729 -0.0094 161 CYS D O     
7580  C  CB    . CYS C 162 ? 0.2890 0.4471 0.5021 -0.0041 -0.0688 -0.0062 161 CYS D CB    
7581  S  SG    . CYS C 162 ? 0.2862 0.4420 0.5074 -0.0007 -0.0836 0.0013  161 CYS D SG    
7587  N  N     . GLY C 163 ? 0.2683 0.4582 0.5256 -0.0060 -0.0664 -0.0111 162 GLY D N     
7588  C  CA    . GLY C 163 ? 0.2879 0.4933 0.5689 -0.0078 -0.0729 -0.0095 162 GLY D CA    
7589  C  C     . GLY C 163 ? 0.2638 0.4724 0.5360 -0.0182 -0.0715 -0.0099 162 GLY D C     
7590  O  O     . GLY C 163 ? 0.2468 0.4443 0.4939 -0.0241 -0.0671 -0.0107 162 GLY D O     
7594  N  N     . GLN C 164 ? 0.2560 0.4799 0.5503 -0.0203 -0.0750 -0.0096 163 GLN D N     
7595  C  CA    . GLN C 164 ? 0.2406 0.4695 0.5303 -0.0303 -0.0741 -0.0102 163 GLN D CA    
7596  C  C     . GLN C 164 ? 0.3032 0.5393 0.6014 -0.0290 -0.0604 -0.0172 163 GLN D C     
7597  O  O     . GLN C 164 ? 0.2647 0.5117 0.5864 -0.0216 -0.0567 -0.0202 163 GLN D O     
7598  C  CB    . GLN C 164 ? 0.2536 0.4956 0.5620 -0.0351 -0.0880 -0.0047 163 GLN D CB    
7599  C  CG    . GLN C 164 ? 0.2317 0.4788 0.5351 -0.0465 -0.0878 -0.0053 163 GLN D CG    
7600  C  CD    . GLN C 164 ? 0.2668 0.5226 0.5795 -0.0537 -0.1037 0.0015  163 GLN D CD    
7601  O  OE1   . GLN C 164 ? 0.2975 0.5569 0.6235 -0.0498 -0.1155 0.0073  163 GLN D OE1   
7602  N  NE2   . GLN C 164 ? 0.2779 0.5366 0.5835 -0.0648 -0.1047 0.0012  163 GLN D NE2   
7611  N  N     . LEU C 165 ? 0.2735 0.5036 0.5530 -0.0364 -0.0529 -0.0198 164 LEU D N     
7612  C  CA    . LEU C 165 ? 0.2895 0.5275 0.5768 -0.0378 -0.0416 -0.0251 164 LEU D CA    
7613  C  C     . LEU C 165 ? 0.3119 0.5630 0.6120 -0.0465 -0.0462 -0.0240 164 LEU D C     
7614  O  O     . LEU C 165 ? 0.3736 0.6210 0.6620 -0.0554 -0.0541 -0.0205 164 LEU D O     
7615  C  CB    . LEU C 165 ? 0.2622 0.4860 0.5236 -0.0404 -0.0297 -0.0286 164 LEU D CB    
7616  C  CG    . LEU C 165 ? 0.3077 0.5174 0.5532 -0.0335 -0.0257 -0.0292 164 LEU D CG    
7617  C  CD1   . LEU C 165 ? 0.3351 0.5312 0.5562 -0.0373 -0.0158 -0.0316 164 LEU D CD1   
7618  C  CD2   . LEU C 165 ? 0.3415 0.5577 0.6038 -0.0235 -0.0205 -0.0325 164 LEU D CD2   
7630  N  N     . GLY D 1   ? 0.5031 0.5797 0.5909 -0.0611 0.0977  0.0051  0   GLY C N     
7631  C  CA    . GLY D 1   ? 0.4809 0.5464 0.5485 -0.0609 0.0898  0.0064  0   GLY C CA    
7632  C  C     . GLY D 1   ? 0.5191 0.5799 0.5660 -0.0717 0.0958  0.0040  0   GLY C C     
7633  O  O     . GLY D 1   ? 0.5021 0.5679 0.5508 -0.0777 0.1084  -0.0007 0   GLY C O     
7639  N  N     . MET D 2   ? 0.5091 0.5606 0.5364 -0.0746 0.0871  0.0071  1   MET C N     
7640  C  CA    . MET D 2   ? 0.5072 0.5542 0.5133 -0.0860 0.0912  0.0060  1   MET C CA    
7641  C  C     . MET D 2   ? 0.4904 0.5359 0.4915 -0.0863 0.1014  -0.0017 1   MET C C     
7642  O  O     . MET D 2   ? 0.5629 0.6074 0.5717 -0.0773 0.1009  -0.0046 1   MET C O     
7643  C  CB    . MET D 2   ? 0.5642 0.6019 0.5522 -0.0894 0.0778  0.0126  1   MET C CB    
7644  C  CG    . MET D 2   ? 0.5295 0.5609 0.5139 -0.0817 0.0695  0.0129  1   MET C CG    
7645  S  SD    . MET D 2   ? 0.4541 0.4761 0.4234 -0.0845 0.0527  0.0216  1   MET C SD    
7646  C  CE    . MET D 2   ? 0.4469 0.4717 0.4331 -0.0776 0.0447  0.0263  1   MET C CE    
7656  N  N     . THR D 3   ? 0.5037 0.5490 0.4914 -0.0972 0.1110  -0.0054 2   THR C N     
7657  C  CA    . THR D 3   ? 0.5651 0.6081 0.5456 -0.0993 0.1210  -0.0133 2   THR C CA    
7658  C  C     . THR D 3   ? 0.5766 0.6102 0.5395 -0.0994 0.1114  -0.0112 2   THR C C     
7659  O  O     . THR D 3   ? 0.5072 0.5358 0.4565 -0.1036 0.1000  -0.0042 2   THR C O     
7660  C  CB    . THR D 3   ? 0.5973 0.6423 0.5663 -0.1121 0.1340  -0.0181 2   THR C CB    
7661  O  OG1   . THR D 3   ? 0.6267 0.6817 0.6158 -0.1108 0.1441  -0.0209 2   THR C OG1   
7662  C  CG2   . THR D 3   ? 0.6231 0.6643 0.5819 -0.1153 0.1440  -0.0267 2   THR C CG2   
7670  N  N     . GLU D 4   ? 0.5092 0.5406 0.4743 -0.0942 0.1157  -0.0171 3   GLU C N     
7671  C  CA    . GLU D 4   ? 0.5502 0.5739 0.5009 -0.0940 0.1083  -0.0165 3   GLU C CA    
7672  C  C     . GLU D 4   ? 0.5308 0.5511 0.4634 -0.1045 0.1179  -0.0230 3   GLU C C     
7673  O  O     . GLU D 4   ? 0.6159 0.6396 0.5536 -0.1070 0.1323  -0.0308 3   GLU C O     
7674  C  CB    . GLU D 4   ? 0.5762 0.5995 0.5416 -0.0813 0.1059  -0.0183 3   GLU C CB    
7675  C  CG    . GLU D 4   ? 0.5490 0.5769 0.5347 -0.0706 0.0993  -0.0136 3   GLU C CG    
7676  C  CD    . GLU D 4   ? 0.5958 0.6212 0.5890 -0.0599 0.0921  -0.0127 3   GLU C CD    
7677  O  OE1   . GLU D 4   ? 0.6219 0.6425 0.6068 -0.0599 0.0930  -0.0160 3   GLU C OE1   
7678  O  OE2   . GLU D 4   ? 0.5191 0.5474 0.5261 -0.0520 0.0857  -0.0087 3   GLU C OE2   
7685  N  N     . TYR D 5   ? 0.4959 0.5095 0.4077 -0.1110 0.1098  -0.0198 4   TYR C N     
7686  C  CA    . TYR D 5   ? 0.5671 0.5765 0.4587 -0.1219 0.1167  -0.0254 4   TYR C CA    
7687  C  C     . TYR D 5   ? 0.5566 0.5600 0.4400 -0.1194 0.1085  -0.0250 4   TYR C C     
7688  O  O     . TYR D 5   ? 0.5227 0.5245 0.4099 -0.1128 0.0952  -0.0181 4   TYR C O     
7689  C  CB    . TYR D 5   ? 0.6091 0.6166 0.4795 -0.1362 0.1149  -0.0212 4   TYR C CB    
7690  C  CG    . TYR D 5   ? 0.6857 0.6994 0.5624 -0.1405 0.1230  -0.0212 4   TYR C CG    
7691  C  CD1   . TYR D 5   ? 0.6853 0.7047 0.5740 -0.1400 0.1397  -0.0303 4   TYR C CD1   
7692  C  CD2   . TYR D 5   ? 0.6726 0.6863 0.5442 -0.1452 0.1141  -0.0120 4   TYR C CD2   
7693  C  CE1   . TYR D 5   ? 0.7180 0.7434 0.6153 -0.1421 0.1453  -0.0304 4   TYR C CE1   
7694  C  CE2   . TYR D 5   ? 0.6678 0.6875 0.5456 -0.1496 0.1215  -0.0119 4   TYR C CE2   
7695  C  CZ    . TYR D 5   ? 0.7296 0.7559 0.6203 -0.1484 0.1376  -0.0212 4   TYR C CZ    
7696  O  OH    . TYR D 5   ? 0.6980 0.7306 0.5977 -0.1506 0.1433  -0.0215 4   TYR C OH    
7706  N  N     . LYS D 6   ? 0.6538 0.6539 0.5259 -0.1252 0.1168  -0.0326 5   LYS C N     
7707  C  CA    . LYS D 6   ? 0.5338 0.5289 0.4004 -0.1226 0.1112  -0.0338 5   LYS C CA    
7708  C  C     . LYS D 6   ? 0.5635 0.5535 0.4033 -0.1367 0.1097  -0.0342 5   LYS C C     
7709  O  O     . LYS D 6   ? 0.6187 0.6071 0.4476 -0.1454 0.1219  -0.0425 5   LYS C O     
7710  C  CB    . LYS D 6   ? 0.6090 0.6043 0.4890 -0.1154 0.1222  -0.0430 5   LYS C CB    
7711  C  CG    . LYS D 6   ? 0.5731 0.5730 0.4789 -0.1020 0.1234  -0.0425 5   LYS C CG    
7712  C  CD    . LYS D 6   ? 0.6715 0.6708 0.5890 -0.0970 0.1359  -0.0520 5   LYS C CD    
7713  C  CE    . LYS D 6   ? 0.7141 0.7192 0.6582 -0.0853 0.1394  -0.0517 5   LYS C CE    
7714  N  NZ    . LYS D 6   ? 0.7346 0.7405 0.6880 -0.0755 0.1255  -0.0436 5   LYS C NZ    
7728  N  N     . LEU D 7   ? 0.5430 0.5302 0.3724 -0.1392 0.0947  -0.0254 6   LEU C N     
7729  C  CA    . LEU D 7   ? 0.5625 0.5451 0.3664 -0.1528 0.0896  -0.0231 6   LEU C CA    
7730  C  C     . LEU D 7   ? 0.5544 0.5336 0.3553 -0.1501 0.0829  -0.0241 6   LEU C C     
7731  O  O     . LEU D 7   ? 0.5317 0.5122 0.3495 -0.1377 0.0773  -0.0225 6   LEU C O     
7732  C  CB    . LEU D 7   ? 0.5639 0.5458 0.3603 -0.1571 0.0760  -0.0115 6   LEU C CB    
7733  C  CG    . LEU D 7   ? 0.5938 0.5794 0.3984 -0.1565 0.0787  -0.0081 6   LEU C CG    
7734  C  CD1   . LEU D 7   ? 0.6139 0.5964 0.4033 -0.1657 0.0664  0.0027  6   LEU C CD1   
7735  C  CD2   . LEU D 7   ? 0.6383 0.6271 0.4414 -0.1628 0.0965  -0.0167 6   LEU C CD2   
7747  N  N     . VAL D 8   ? 0.5766 0.5517 0.3555 -0.1625 0.0831  -0.0263 7   VAL C N     
7748  C  CA    . VAL D 8   ? 0.5580 0.5302 0.3325 -0.1620 0.0777  -0.0280 7   VAL C CA    
7749  C  C     . VAL D 8   ? 0.5809 0.5494 0.3304 -0.1761 0.0677  -0.0225 7   VAL C C     
7750  O  O     . VAL D 8   ? 0.5658 0.5322 0.3013 -0.1873 0.0724  -0.0261 7   VAL C O     
7751  C  CB    . VAL D 8   ? 0.5798 0.5503 0.3560 -0.1618 0.0926  -0.0405 7   VAL C CB    
7752  C  CG1   . VAL D 8   ? 0.5675 0.5348 0.3383 -0.1624 0.0868  -0.0421 7   VAL C CG1   
7753  C  CG2   . VAL D 8   ? 0.5162 0.4902 0.3177 -0.1482 0.1019  -0.0450 7   VAL C CG2   
7763  N  N     . VAL D 9   ? 0.4974 0.4657 0.2488 -0.1728 0.0517  -0.0142 8   VAL C N     
7764  C  CA    . VAL D 9   ? 0.5244 0.4898 0.2550 -0.1850 0.0394  -0.0071 8   VAL C CA    
7765  C  C     . VAL D 9   ? 0.5657 0.5291 0.2881 -0.1889 0.0387  -0.0121 8   VAL C C     
7766  O  O     . VAL D 9   ? 0.5190 0.4839 0.2574 -0.1781 0.0374  -0.0144 8   VAL C O     
7767  C  CB    . VAL D 9   ? 0.5453 0.5118 0.2850 -0.1788 0.0217  0.0055  8   VAL C CB    
7768  C  CG1   . VAL D 9   ? 0.5749 0.5384 0.2940 -0.1919 0.0085  0.0143  8   VAL C CG1   
7769  C  CG2   . VAL D 9   ? 0.5407 0.5092 0.2932 -0.1721 0.0230  0.0093  8   VAL C CG2   
7779  N  N     . VAL D 10  ? 0.5780 0.5384 0.2832 -0.2021 0.0372  -0.0132 9   VAL C N     
7780  C  CA    . VAL D 10  ? 0.6056 0.5639 0.3045 -0.2070 0.0374  -0.0188 9   VAL C CA    
7781  C  C     . VAL D 10  ? 0.6221 0.5786 0.3059 -0.2195 0.0245  -0.0115 9   VAL C C     
7782  O  O     . VAL D 10  ? 0.5459 0.5019 0.2228 -0.2258 0.0189  -0.0046 9   VAL C O     
7783  C  CB    . VAL D 10  ? 0.5855 0.5413 0.2846 -0.2095 0.0549  -0.0325 9   VAL C CB    
7784  C  CG1   . VAL D 10  ? 0.5394 0.4972 0.2565 -0.1968 0.0676  -0.0390 9   VAL C CG1   
7785  C  CG2   . VAL D 10  ? 0.5128 0.4669 0.2012 -0.2202 0.0592  -0.0338 9   VAL C CG2   
7795  N  N     . GLY D 11  ? 0.6709 0.6265 0.3501 -0.2234 0.0200  -0.0130 10  GLY C N     
7796  C  CA    . GLY D 11  ? 0.6359 0.5903 0.3026 -0.2350 0.0078  -0.0060 10  GLY C CA    
7797  C  C     . GLY D 11  ? 0.6726 0.6290 0.3439 -0.2318 -0.0032 -0.0024 10  GLY C C     
7798  O  O     . GLY D 11  ? 0.6913 0.6505 0.3753 -0.2203 -0.0041 -0.0034 10  GLY C O     
7802  N  N     . ALA D 12  ? 0.7234 0.6788 0.3846 -0.2423 -0.0118 0.0018  11  ALA C N     
7803  C  CA    . ALA D 12  ? 0.6999 0.6580 0.3661 -0.2403 -0.0225 0.0053  11  ALA C CA    
7804  C  C     . ALA D 12  ? 0.6820 0.6445 0.3631 -0.2291 -0.0364 0.0153  11  ALA C C     
7805  O  O     . ALA D 12  ? 0.6418 0.6046 0.3267 -0.2256 -0.0408 0.0220  11  ALA C O     
7806  C  CB    . ALA D 12  ? 0.7179 0.6746 0.3711 -0.2539 -0.0310 0.0106  11  ALA C CB    
7812  N  N     . ASP D 13  ? 0.6848 0.6510 0.3756 -0.2236 -0.0436 0.0161  12  ASP C N     
7813  C  CA    . ASP D 13  ? 0.7076 0.6785 0.4152 -0.2125 -0.0568 0.0248  12  ASP C CA    
7814  C  C     . ASP D 13  ? 0.6583 0.6294 0.3659 -0.2169 -0.0724 0.0383  12  ASP C C     
7815  O  O     . ASP D 13  ? 0.6441 0.6132 0.3400 -0.2285 -0.0761 0.0415  12  ASP C O     
7816  C  CB    . ASP D 13  ? 0.7942 0.7699 0.5143 -0.2059 -0.0611 0.0221  12  ASP C CB    
7817  C  CG    . ASP D 13  ? 0.7814 0.7564 0.4924 -0.2155 -0.0599 0.0183  12  ASP C CG    
7818  O  OD1   . ASP D 13  ? 0.7681 0.7398 0.4646 -0.2274 -0.0603 0.0207  12  ASP C OD1   
7819  O  OD2   . ASP D 13  ? 0.8553 0.8330 0.5739 -0.2114 -0.0583 0.0126  12  ASP C OD2   
7824  N  N     . GLY D 14  ? 0.6517 0.6247 0.3728 -0.2077 -0.0811 0.0461  13  GLY C N     
7825  C  CA    . GLY D 14  ? 0.6558 0.6286 0.3817 -0.2092 -0.0963 0.0591  13  GLY C CA    
7826  C  C     . GLY D 14  ? 0.6532 0.6209 0.3680 -0.2166 -0.0955 0.0640  13  GLY C C     
7827  O  O     . GLY D 14  ? 0.6361 0.6028 0.3566 -0.2169 -0.1081 0.0751  13  GLY C O     
7831  N  N     . VAL D 15  ? 0.6537 0.6181 0.3542 -0.2226 -0.0810 0.0558  14  VAL C N     
7832  C  CA    . VAL D 15  ? 0.6447 0.6049 0.3341 -0.2312 -0.0798 0.0598  14  VAL C CA    
7833  C  C     . VAL D 15  ? 0.6357 0.5955 0.3368 -0.2221 -0.0848 0.0665  14  VAL C C     
7834  O  O     . VAL D 15  ? 0.6498 0.6065 0.3473 -0.2274 -0.0908 0.0744  14  VAL C O     
7835  C  CB    . VAL D 15  ? 0.6302 0.5878 0.3042 -0.2391 -0.0619 0.0482  14  VAL C CB    
7836  C  CG1   . VAL D 15  ? 0.6828 0.6398 0.3460 -0.2480 -0.0569 0.0412  14  VAL C CG1   
7837  C  CG2   . VAL D 15  ? 0.6123 0.5713 0.2944 -0.2281 -0.0492 0.0396  14  VAL C CG2   
7847  N  N     . GLY D 16  ? 0.5770 0.5397 0.2917 -0.2091 -0.0821 0.0634  15  GLY C N     
7848  C  CA    . GLY D 16  ? 0.5976 0.5599 0.3238 -0.2000 -0.0858 0.0688  15  GLY C CA    
7849  C  C     . GLY D 16  ? 0.5992 0.5611 0.3233 -0.1959 -0.0713 0.0613  15  GLY C C     
7850  O  O     . GLY D 16  ? 0.5728 0.5330 0.3017 -0.1923 -0.0728 0.0662  15  GLY C O     
7854  N  N     . LYS D 17  ? 0.6040 0.5671 0.3222 -0.1965 -0.0568 0.0496  16  LYS C N     
7855  C  CA    . LYS D 17  ? 0.6018 0.5658 0.3291 -0.1884 -0.0412 0.0412  16  LYS C CA    
7856  C  C     . LYS D 17  ? 0.5690 0.5355 0.3229 -0.1716 -0.0450 0.0440  16  LYS C C     
7857  O  O     . LYS D 17  ? 0.5280 0.4940 0.2886 -0.1672 -0.0407 0.0448  16  LYS C O     
7858  C  CB    . LYS D 17  ? 0.6100 0.5753 0.3376 -0.1869 -0.0272 0.0284  16  LYS C CB    
7859  C  CG    . LYS D 17  ? 0.5437 0.5062 0.2470 -0.2027 -0.0223 0.0236  16  LYS C CG    
7860  C  CD    . LYS D 17  ? 0.5828 0.5458 0.2883 -0.1999 -0.0094 0.0110  16  LYS C CD    
7861  C  CE    . LYS D 17  ? 0.6260 0.5922 0.3462 -0.1915 -0.0183 0.0120  16  LYS C CE    
7862  N  NZ    . LYS D 17  ? 0.5702 0.5365 0.2791 -0.2008 -0.0345 0.0206  16  LYS C NZ    
7876  N  N     . SER D 18  ? 0.5150 0.4848 0.2852 -0.1618 -0.0514 0.0441  17  SER C N     
7877  C  CA    . SER D 18  ? 0.5141 0.4861 0.3084 -0.1465 -0.0546 0.0463  17  SER C CA    
7878  C  C     . SER D 18  ? 0.5073 0.4768 0.3037 -0.1470 -0.0677 0.0578  17  SER C C     
7879  O  O     . SER D 18  ? 0.5191 0.4880 0.3278 -0.1389 -0.0667 0.0592  17  SER C O     
7880  C  CB    . SER D 18  ? 0.4885 0.4648 0.2994 -0.1367 -0.0588 0.0443  17  SER C CB    
7881  O  OG    . SER D 18  ? 0.5294 0.5070 0.3365 -0.1379 -0.0477 0.0344  17  SER C OG    
7886  N  N     . ALA D 19  ? 0.5605 0.5279 0.3451 -0.1567 -0.0806 0.0663  18  ALA C N     
7887  C  CA    . ALA D 19  ? 0.5140 0.4780 0.3017 -0.1570 -0.0938 0.0778  18  ALA C CA    
7888  C  C     . ALA D 19  ? 0.5768 0.5369 0.3547 -0.1624 -0.0874 0.0790  18  ALA C C     
7889  O  O     . ALA D 19  ? 0.5428 0.5007 0.3316 -0.1565 -0.0922 0.0845  18  ALA C O     
7890  C  CB    . ALA D 19  ? 0.5541 0.5164 0.3297 -0.1678 -0.1089 0.0873  18  ALA C CB    
7896  N  N     . LEU D 20  ? 0.5024 0.4617 0.2607 -0.1733 -0.0755 0.0732  19  LEU C N     
7897  C  CA    . LEU D 20  ? 0.5528 0.5096 0.3020 -0.1789 -0.0671 0.0730  19  LEU C CA    
7898  C  C     . LEU D 20  ? 0.5725 0.5322 0.3408 -0.1659 -0.0561 0.0660  19  LEU C C     
7899  O  O     . LEU D 20  ? 0.5536 0.5117 0.3297 -0.1622 -0.0581 0.0704  19  LEU C O     
7900  C  CB    . LEU D 20  ? 0.5621 0.5181 0.2866 -0.1938 -0.0558 0.0669  19  LEU C CB    
7901  C  CG    . LEU D 20  ? 0.5891 0.5425 0.3010 -0.2068 -0.0627 0.0707  19  LEU C CG    
7902  C  CD1   . LEU D 20  ? 0.6349 0.5890 0.3320 -0.2163 -0.0482 0.0596  19  LEU C CD1   
7903  C  CD2   . LEU D 20  ? 0.6267 0.5765 0.3365 -0.2121 -0.0694 0.0794  19  LEU C CD2   
7915  N  N     . THR D 21  ? 0.5667 0.5304 0.3426 -0.1593 -0.0448 0.0554  20  THR C N     
7916  C  CA    . THR D 21  ? 0.4733 0.4401 0.2679 -0.1467 -0.0350 0.0490  20  THR C CA    
7917  C  C     . THR D 21  ? 0.5087 0.4754 0.3228 -0.1349 -0.0452 0.0551  20  THR C C     
7918  O  O     . THR D 21  ? 0.4947 0.4614 0.3177 -0.1300 -0.0421 0.0556  20  THR C O     
7919  C  CB    . THR D 21  ? 0.4867 0.4570 0.2884 -0.1404 -0.0257 0.0389  20  THR C CB    
7920  O  OG1   . THR D 21  ? 0.4685 0.4382 0.2529 -0.1511 -0.0142 0.0317  20  THR C OG1   
7921  C  CG2   . THR D 21  ? 0.4876 0.4612 0.3102 -0.1264 -0.0177 0.0335  20  THR C CG2   
7929  N  N     . ILE D 22  ? 0.4837 0.4505 0.3053 -0.1303 -0.0574 0.0596  21  ILE C N     
7930  C  CA    . ILE D 22  ? 0.5311 0.4977 0.3725 -0.1184 -0.0661 0.0640  21  ILE C CA    
7931  C  C     . ILE D 22  ? 0.5237 0.4851 0.3617 -0.1229 -0.0745 0.0734  21  ILE C C     
7932  O  O     . ILE D 22  ? 0.5849 0.5453 0.4369 -0.1146 -0.0765 0.0751  21  ILE C O     
7933  C  CB    . ILE D 22  ? 0.5451 0.5136 0.3965 -0.1129 -0.0765 0.0662  21  ILE C CB    
7934  C  CG1   . ILE D 22  ? 0.5237 0.4973 0.3846 -0.1048 -0.0678 0.0566  21  ILE C CG1   
7935  C  CG2   . ILE D 22  ? 0.5626 0.5294 0.4313 -0.1036 -0.0877 0.0725  21  ILE C CG2   
7936  C  CD1   . ILE D 22  ? 0.5733 0.5490 0.4468 -0.0948 -0.0567 0.0497  21  ILE C CD1   
7948  N  N     . GLN D 23  ? 0.5296 0.4874 0.3488 -0.1362 -0.0799 0.0799  22  GLN C N     
7949  C  CA    . GLN D 23  ? 0.5986 0.5508 0.4134 -0.1415 -0.0876 0.0892  22  GLN C CA    
7950  C  C     . GLN D 23  ? 0.5955 0.5481 0.4093 -0.1422 -0.0755 0.0852  22  GLN C C     
7951  O  O     . GLN D 23  ? 0.6534 0.6035 0.4777 -0.1372 -0.0789 0.0890  22  GLN C O     
7952  C  CB    . GLN D 23  ? 0.6341 0.5824 0.4274 -0.1566 -0.0962 0.0974  22  GLN C CB    
7953  C  CG    . GLN D 23  ? 0.6925 0.6339 0.4838 -0.1611 -0.1101 0.1103  22  GLN C CG    
7954  C  CD    . GLN D 23  ? 0.6615 0.6009 0.4750 -0.1490 -0.1234 0.1161  22  GLN C CD    
7955  O  OE1   . GLN D 23  ? 0.6820 0.6217 0.5132 -0.1377 -0.1208 0.1132  22  GLN C OE1   
7956  N  NE2   . GLN D 23  ? 0.6902 0.6287 0.5091 -0.1503 -0.1350 0.1213  22  GLN C NE2   
7965  N  N     . LEU D 24  ? 0.5547 0.5106 0.3582 -0.1476 -0.0611 0.0769  23  LEU C N     
7966  C  CA    . LEU D 24  ? 0.5608 0.5188 0.3677 -0.1465 -0.0485 0.0718  23  LEU C CA    
7967  C  C     . LEU D 24  ? 0.5868 0.5476 0.4174 -0.1310 -0.0469 0.0684  23  LEU C C     
7968  O  O     . LEU D 24  ? 0.5240 0.4840 0.3618 -0.1286 -0.0461 0.0704  23  LEU C O     
7969  C  CB    . LEU D 24  ? 0.5363 0.4982 0.3329 -0.1522 -0.0326 0.0619  23  LEU C CB    
7970  C  CG    . LEU D 24  ? 0.5573 0.5226 0.3586 -0.1515 -0.0186 0.0562  23  LEU C CG    
7971  C  CD1   . LEU D 24  ? 0.5555 0.5181 0.3392 -0.1659 -0.0168 0.0610  23  LEU C CD1   
7972  C  CD2   . LEU D 24  ? 0.5268 0.4969 0.3301 -0.1493 -0.0030 0.0443  23  LEU C CD2   
7984  N  N     . ILE D 25  ? 0.5005 0.4646 0.3429 -0.1209 -0.0460 0.0629  24  ILE C N     
7985  C  CA    . ILE D 25  ? 0.5449 0.5120 0.4078 -0.1072 -0.0430 0.0588  24  ILE C CA    
7986  C  C     . ILE D 25  ? 0.5185 0.4821 0.3937 -0.1001 -0.0559 0.0655  24  ILE C C     
7987  O  O     . ILE D 25  ? 0.5544 0.5175 0.4401 -0.0946 -0.0554 0.0659  24  ILE C O     
7988  C  CB    . ILE D 25  ? 0.4985 0.4701 0.3690 -0.0996 -0.0369 0.0506  24  ILE C CB    
7989  C  CG1   . ILE D 25  ? 0.5069 0.4809 0.3661 -0.1064 -0.0236 0.0433  24  ILE C CG1   
7990  C  CG2   . ILE D 25  ? 0.4599 0.4344 0.3501 -0.0863 -0.0342 0.0468  24  ILE C CG2   
7991  C  CD1   . ILE D 25  ? 0.4416 0.4180 0.3032 -0.1071 -0.0118 0.0393  24  ILE C CD1   
8003  N  N     . GLN D 26  ? 0.5372 0.4985 0.4127 -0.0998 -0.0675 0.0706  25  GLN C N     
8004  C  CA    . GLN D 26  ? 0.5743 0.5332 0.4660 -0.0902 -0.0781 0.0745  25  GLN C CA    
8005  C  C     . GLN D 26  ? 0.6842 0.6363 0.5720 -0.0957 -0.0918 0.0853  25  GLN C C     
8006  O  O     . GLN D 26  ? 0.6616 0.6106 0.5636 -0.0880 -0.1005 0.0887  25  GLN C O     
8007  C  CB    . GLN D 26  ? 0.6334 0.5959 0.5356 -0.0819 -0.0807 0.0710  25  GLN C CB    
8008  C  CG    . GLN D 26  ? 0.5258 0.4938 0.4373 -0.0733 -0.0696 0.0614  25  GLN C CG    
8009  C  CD    . GLN D 26  ? 0.6511 0.6227 0.5718 -0.0663 -0.0719 0.0582  25  GLN C CD    
8010  O  OE1   . GLN D 26  ? 0.6709 0.6412 0.5996 -0.0629 -0.0825 0.0626  25  GLN C OE1   
8011  N  NE2   . GLN D 26  ? 0.6452 0.6215 0.5661 -0.0639 -0.0617 0.0505  25  GLN C NE2   
8020  N  N     . ASN D 27  ? 0.6510 0.6001 0.5202 -0.1089 -0.0939 0.0908  26  ASN C N     
8021  C  CA    . ASN D 27  ? 0.7417 0.6837 0.6067 -0.1148 -0.1077 0.1022  26  ASN C CA    
8022  C  C     . ASN D 27  ? 0.7500 0.6913 0.6272 -0.1081 -0.1203 0.1060  26  ASN C C     
8023  O  O     . ASN D 27  ? 0.6934 0.6298 0.5827 -0.1030 -0.1310 0.1121  26  ASN C O     
8024  C  CB    . ASN D 27  ? 0.7891 0.7261 0.6606 -0.1127 -0.1092 0.1057  26  ASN C CB    
8025  C  CG    . ASN D 27  ? 0.8211 0.7605 0.6840 -0.1183 -0.0960 0.1012  26  ASN C CG    
8026  O  OD1   . ASN D 27  ? 0.8182 0.7568 0.6625 -0.1310 -0.0926 0.1036  26  ASN C OD1   
8027  N  ND2   . ASN D 27  ? 0.8065 0.7491 0.6831 -0.1089 -0.0884 0.0945  26  ASN C ND2   
8034  N  N     . HIS D 28  ? 0.6926 0.6394 0.5685 -0.1073 -0.1181 0.1014  27  HIS C N     
8035  C  CA    . HIS D 28  ? 0.6888 0.6371 0.5754 -0.1022 -0.1285 0.1040  27  HIS C CA    
8036  C  C     . HIS D 28  ? 0.5905 0.5407 0.4598 -0.1135 -0.1307 0.1060  27  HIS C C     
8037  O  O     . HIS D 28  ? 0.6121 0.5648 0.4663 -0.1204 -0.1196 0.1001  27  HIS C O     
8038  C  CB    . HIS D 28  ? 0.6548 0.6093 0.5593 -0.0889 -0.1221 0.0947  27  HIS C CB    
8039  C  CG    . HIS D 28  ? 0.7064 0.6636 0.6239 -0.0833 -0.1317 0.0966  27  HIS C CG    
8040  N  ND1   . HIS D 28  ? 0.7493 0.7134 0.6704 -0.0799 -0.1270 0.0899  27  HIS C ND1   
8041  C  CD2   . HIS D 28  ? 0.7568 0.7108 0.6857 -0.0805 -0.1458 0.1045  27  HIS C CD2   
8042  C  CE1   . HIS D 28  ? 0.7487 0.7147 0.6830 -0.0755 -0.1375 0.0935  27  HIS C CE1   
8043  N  NE2   . HIS D 28  ? 0.7833 0.7434 0.7233 -0.0754 -0.1491 0.1023  27  HIS C NE2   
8051  N  N     . PHE D 29  ? 0.6572 0.6062 0.5290 -0.1156 -0.1450 0.1141  28  PHE C N     
8052  C  CA    . PHE D 29  ? 0.6503 0.6018 0.5090 -0.1253 -0.1470 0.1149  28  PHE C CA    
8053  C  C     . PHE D 29  ? 0.6687 0.6269 0.5408 -0.1177 -0.1500 0.1114  28  PHE C C     
8054  O  O     . PHE D 29  ? 0.5988 0.5577 0.4930 -0.1072 -0.1572 0.1134  28  PHE C O     
8055  C  CB    . PHE D 29  ? 0.6090 0.5556 0.4654 -0.1334 -0.1565 0.1236  28  PHE C CB    
8056  C  CG    . PHE D 29  ? 0.6286 0.5777 0.4735 -0.1430 -0.1585 0.1242  28  PHE C CG    
8057  C  CD1   . PHE D 29  ? 0.6167 0.5675 0.4391 -0.1537 -0.1488 0.1190  28  PHE C CD1   
8058  C  CD2   . PHE D 29  ? 0.6373 0.5870 0.4941 -0.1418 -0.1696 0.1297  28  PHE C CD2   
8059  C  CE1   . PHE D 29  ? 0.6413 0.5936 0.4522 -0.1635 -0.1505 0.1192  28  PHE C CE1   
8060  C  CE2   . PHE D 29  ? 0.6597 0.6115 0.5051 -0.1516 -0.1719 0.1308  28  PHE C CE2   
8061  C  CZ    . PHE D 29  ? 0.6477 0.6007 0.4699 -0.1626 -0.1624 0.1255  28  PHE C CZ    
8071  N  N     . VAL D 30  ? 0.6732 0.6360 0.5332 -0.1231 -0.1431 0.1053  29  VAL C N     
8072  C  CA    . VAL D 30  ? 0.6277 0.5973 0.4984 -0.1179 -0.1442 0.1010  29  VAL C CA    
8073  C  C     . VAL D 30  ? 0.6001 0.5697 0.4643 -0.1272 -0.1534 0.1070  29  VAL C C     
8074  O  O     . VAL D 30  ? 0.5994 0.5680 0.4428 -0.1396 -0.1493 0.1059  29  VAL C O     
8075  C  CB    . VAL D 30  ? 0.6460 0.6199 0.5115 -0.1169 -0.1280 0.0886  29  VAL C CB    
8076  C  CG1   . VAL D 30  ? 0.6467 0.6211 0.5255 -0.1050 -0.1167 0.0813  29  VAL C CG1   
8077  C  CG2   . VAL D 30  ? 0.6403 0.6118 0.4782 -0.1320 -0.1209 0.0867  29  VAL C CG2   
8087  N  N     . ASP D 31  ? 0.6159 0.5866 0.4999 -0.1208 -0.1639 0.1123  30  ASP C N     
8088  C  CA    . ASP D 31  ? 0.5976 0.5689 0.4795 -0.1281 -0.1718 0.1175  30  ASP C CA    
8089  C  C     . ASP D 31  ? 0.6190 0.5982 0.5044 -0.1269 -0.1709 0.1125  30  ASP C C     
8090  O  O     . ASP D 31  ? 0.5789 0.5591 0.4560 -0.1358 -0.1747 0.1151  30  ASP C O     
8091  C  CB    . ASP D 31  ? 0.6673 0.6355 0.5686 -0.1228 -0.1835 0.1260  30  ASP C CB    
8092  C  CG    . ASP D 31  ? 0.6877 0.6586 0.6156 -0.1067 -0.1847 0.1235  30  ASP C CG    
8093  O  OD1   . ASP D 31  ? 0.7552 0.7305 0.7017 -0.1004 -0.1910 0.1246  30  ASP C OD1   
8094  O  OD2   . ASP D 31  ? 0.7393 0.7081 0.6700 -0.1006 -0.1794 0.1202  30  ASP C OD2   
8099  N  N     . GLU D 32  ? 0.5993 0.5843 0.4958 -0.1172 -0.1658 0.1052  31  GLU C N     
8100  C  CA    . GLU D 32  ? 0.6016 0.5946 0.5027 -0.1159 -0.1645 0.0998  31  GLU C CA    
8101  C  C     . GLU D 32  ? 0.5927 0.5862 0.4712 -0.1245 -0.1535 0.0917  31  GLU C C     
8102  O  O     . GLU D 32  ? 0.6275 0.6169 0.4960 -0.1250 -0.1430 0.0872  31  GLU C O     
8103  C  CB    . GLU D 32  ? 0.5857 0.5847 0.5122 -0.1010 -0.1648 0.0960  31  GLU C CB    
8104  C  CG    . GLU D 32  ? 0.6107 0.6113 0.5615 -0.0931 -0.1748 0.1018  31  GLU C CG    
8105  C  CD    . GLU D 32  ? 0.6773 0.6800 0.6519 -0.0784 -0.1739 0.0989  31  GLU C CD    
8106  O  OE1   . GLU D 32  ? 0.8036 0.8004 0.7774 -0.0749 -0.1714 0.0993  31  GLU C OE1   
8107  O  OE2   . GLU D 32  ? 0.6531 0.6631 0.6475 -0.0704 -0.1754 0.0962  31  GLU C OE2   
8114  N  N     . TYR D 33  ? 0.5619 0.5599 0.4356 -0.1299 -0.1529 0.0884  32  TYR C N     
8115  C  CA    . TYR D 33  ? 0.5831 0.5806 0.4359 -0.1385 -0.1413 0.0797  32  TYR C CA    
8116  C  C     . TYR D 33  ? 0.6279 0.6296 0.4951 -0.1273 -0.1284 0.0687  32  TYR C C     
8117  O  O     . TYR D 33  ? 0.5330 0.5412 0.4146 -0.1226 -0.1316 0.0672  32  TYR C O     
8118  C  CB    . TYR D 33  ? 0.6257 0.6240 0.4668 -0.1499 -0.1446 0.0809  32  TYR C CB    
8119  C  CG    . TYR D 33  ? 0.6619 0.6587 0.4810 -0.1597 -0.1324 0.0714  32  TYR C CG    
8120  C  CD1   . TYR D 33  ? 0.6648 0.6569 0.4702 -0.1616 -0.1195 0.0648  32  TYR C CD1   
8121  C  CD2   . TYR D 33  ? 0.7023 0.7020 0.5167 -0.1661 -0.1325 0.0684  32  TYR C CD2   
8122  C  CE1   . TYR D 33  ? 0.6557 0.6456 0.4440 -0.1694 -0.1064 0.0550  32  TYR C CE1   
8123  C  CE2   . TYR D 33  ? 0.7148 0.7120 0.5100 -0.1748 -0.1205 0.0589  32  TYR C CE2   
8124  C  CZ    . TYR D 33  ? 0.7021 0.6943 0.4838 -0.1766 -0.1078 0.0521  32  TYR C CZ    
8125  O  OH    . TYR D 33  ? 0.7265 0.7154 0.4910 -0.1845 -0.0944 0.0417  32  TYR C OH    
8135  N  N     . ASP D 34  ? 0.6055 0.6037 0.4685 -0.1238 -0.1139 0.0614  33  ASP C N     
8136  C  CA    . ASP D 34  ? 0.6041 0.6049 0.4786 -0.1138 -0.1010 0.0514  33  ASP C CA    
8137  C  C     . ASP D 34  ? 0.5879 0.5849 0.4440 -0.1209 -0.0865 0.0429  33  ASP C C     
8138  O  O     . ASP D 34  ? 0.5637 0.5569 0.4161 -0.1190 -0.0772 0.0399  33  ASP C O     
8139  C  CB    . ASP D 34  ? 0.5892 0.5896 0.4810 -0.1005 -0.0984 0.0514  33  ASP C CB    
8140  C  CG    . ASP D 34  ? 0.6169 0.6203 0.5217 -0.0899 -0.0868 0.0424  33  ASP C CG    
8141  O  OD1   . ASP D 34  ? 0.5471 0.5545 0.4545 -0.0901 -0.0839 0.0377  33  ASP C OD1   
8142  O  OD2   . ASP D 34  ? 0.5687 0.5705 0.4811 -0.0818 -0.0811 0.0405  33  ASP C OD2   
8147  N  N     . PRO D 35  ? 0.5876 0.5856 0.4330 -0.1291 -0.0842 0.0386  34  PRO C N     
8148  C  CA    . PRO D 35  ? 0.5419 0.5352 0.3684 -0.1374 -0.0708 0.0304  34  PRO C CA    
8149  C  C     . PRO D 35  ? 0.5620 0.5546 0.3983 -0.1273 -0.0558 0.0218  34  PRO C C     
8150  O  O     . PRO D 35  ? 0.5174 0.5139 0.3725 -0.1159 -0.0548 0.0198  34  PRO C O     
8151  C  CB    . PRO D 35  ? 0.6147 0.6098 0.4328 -0.1459 -0.0724 0.0272  34  PRO C CB    
8152  C  CG    . PRO D 35  ? 0.5867 0.5887 0.4236 -0.1393 -0.0841 0.0322  34  PRO C CG    
8153  C  CD    . PRO D 35  ? 0.5896 0.5930 0.4399 -0.1318 -0.0941 0.0411  34  PRO C CD    
8161  N  N     . THR D 36  ? 0.5151 0.5029 0.3383 -0.1321 -0.0441 0.0165  35  THR C N     
8162  C  CA    . THR D 36  ? 0.5244 0.5112 0.3574 -0.1226 -0.0315 0.0104  35  THR C CA    
8163  C  C     . THR D 36  ? 0.4900 0.4763 0.3253 -0.1205 -0.0196 0.0006  35  THR C C     
8164  O  O     . THR D 36  ? 0.4800 0.4642 0.3018 -0.1301 -0.0166 -0.0038 35  THR C O     
8165  C  CB    . THR D 36  ? 0.4901 0.4725 0.3105 -0.1283 -0.0246 0.0099  35  THR C CB    
8166  O  OG1   . THR D 36  ? 0.4396 0.4220 0.2598 -0.1292 -0.0359 0.0196  35  THR C OG1   
8167  C  CG2   . THR D 36  ? 0.4681 0.4502 0.3001 -0.1185 -0.0115 0.0037  35  THR C CG2   
8174  N  N     . ILE D 37  ? 0.4789 0.4667 0.3312 -0.1082 -0.0133 -0.0026 36  ILE C N     
8175  C  CA    . ILE D 37  ? 0.4661 0.4522 0.3215 -0.1054 -0.0007 -0.0116 36  ILE C CA    
8176  C  C     . ILE D 37  ? 0.4550 0.4373 0.3065 -0.1055 0.0112  -0.0159 36  ILE C C     
8177  O  O     . ILE D 37  ? 0.4241 0.4024 0.2631 -0.1135 0.0207  -0.0223 36  ILE C O     
8178  C  CB    . ILE D 37  ? 0.4118 0.4016 0.2875 -0.0926 -0.0005 -0.0123 36  ILE C CB    
8179  C  CG1   . ILE D 37  ? 0.4537 0.4486 0.3365 -0.0912 -0.0125 -0.0075 36  ILE C CG1   
8180  C  CG2   . ILE D 37  ? 0.3597 0.3465 0.2370 -0.0910 0.0123  -0.0210 36  ILE C CG2   
8181  C  CD1   . ILE D 37  ? 0.4367 0.4316 0.3114 -0.0996 -0.0130 -0.0109 36  ILE C CD1   
8193  N  N     . GLU D 38  ? 0.4334 0.4175 0.2969 -0.0965 0.0110  -0.0128 37  GLU C N     
8194  C  CA    . GLU D 38  ? 0.4312 0.4132 0.2931 -0.0965 0.0202  -0.0152 37  GLU C CA    
8195  C  C     . GLU D 38  ? 0.4110 0.3957 0.2859 -0.0873 0.0154  -0.0095 37  GLU C C     
8196  O  O     . GLU D 38  ? 0.4002 0.3876 0.2901 -0.0772 0.0125  -0.0084 37  GLU C O     
8197  C  CB    . GLU D 38  ? 0.3926 0.3726 0.2598 -0.0930 0.0341  -0.0238 37  GLU C CB    
8198  C  CG    . GLU D 38  ? 0.5192 0.4972 0.3828 -0.0955 0.0447  -0.0274 37  GLU C CG    
8199  C  CD    . GLU D 38  ? 0.5633 0.5403 0.4391 -0.0883 0.0565  -0.0342 37  GLU C CD    
8200  O  OE1   . GLU D 38  ? 0.6352 0.6087 0.5068 -0.0918 0.0637  -0.0411 37  GLU C OE1   
8201  O  OE2   . GLU D 38  ? 0.5659 0.5454 0.4559 -0.0791 0.0577  -0.0324 37  GLU C OE2   
8208  N  N     . ASP D 39  ? 0.3859 0.3697 0.2550 -0.0911 0.0150  -0.0062 38  ASP C N     
8209  C  CA    . ASP D 39  ? 0.3651 0.3508 0.2461 -0.0831 0.0107  -0.0011 38  ASP C CA    
8210  C  C     . ASP D 39  ? 0.3609 0.3456 0.2391 -0.0855 0.0192  -0.0027 38  ASP C C     
8211  O  O     . ASP D 39  ? 0.3875 0.3700 0.2512 -0.0957 0.0247  -0.0050 38  ASP C O     
8212  C  CB    . ASP D 39  ? 0.3824 0.3684 0.2614 -0.0849 -0.0038 0.0077  38  ASP C CB    
8213  C  CG    . ASP D 39  ? 0.4532 0.4416 0.3404 -0.0801 -0.0125 0.0096  38  ASP C CG    
8214  O  OD1   . ASP D 39  ? 0.4633 0.4542 0.3661 -0.0694 -0.0135 0.0095  38  ASP C OD1   
8215  O  OD2   . ASP D 39  ? 0.4517 0.4399 0.3295 -0.0874 -0.0178 0.0109  38  ASP C OD2   
8220  N  N     . SER D 40  ? 0.3593 0.3461 0.2519 -0.0763 0.0205  -0.0018 39  SER C N     
8221  C  CA    . SER D 40  ? 0.3889 0.3762 0.2830 -0.0770 0.0276  -0.0025 39  SER C CA    
8222  C  C     . SER D 40  ? 0.3724 0.3605 0.2722 -0.0737 0.0186  0.0048  39  SER C C     
8223  O  O     . SER D 40  ? 0.3194 0.3085 0.2296 -0.0656 0.0107  0.0080  39  SER C O     
8224  C  CB    . SER D 40  ? 0.4349 0.4241 0.3429 -0.0688 0.0380  -0.0084 39  SER C CB    
8225  O  OG    . SER D 40  ? 0.4780 0.4655 0.3811 -0.0724 0.0477  -0.0157 39  SER C OG    
8231  N  N     . TYR D 41  ? 0.3500 0.3374 0.2431 -0.0800 0.0203  0.0071  40  TYR C N     
8232  C  CA    . TYR D 41  ? 0.3643 0.3517 0.2623 -0.0778 0.0125  0.0138  40  TYR C CA    
8233  C  C     . TYR D 41  ? 0.3503 0.3398 0.2521 -0.0787 0.0211  0.0123  40  TYR C C     
8234  O  O     . TYR D 41  ? 0.3578 0.3481 0.2542 -0.0840 0.0323  0.0069  40  TYR C O     
8235  C  CB    . TYR D 41  ? 0.3708 0.3547 0.2552 -0.0867 0.0022  0.0210  40  TYR C CB    
8236  C  CG    . TYR D 41  ? 0.3892 0.3719 0.2703 -0.0870 -0.0068 0.0230  40  TYR C CG    
8237  C  CD1   . TYR D 41  ? 0.4510 0.4338 0.3432 -0.0791 -0.0176 0.0275  40  TYR C CD1   
8238  C  CD2   . TYR D 41  ? 0.3762 0.3578 0.2431 -0.0956 -0.0043 0.0202  40  TYR C CD2   
8239  C  CE1   . TYR D 41  ? 0.4758 0.4585 0.3673 -0.0790 -0.0257 0.0294  40  TYR C CE1   
8240  C  CE2   . TYR D 41  ? 0.4298 0.4111 0.2950 -0.0960 -0.0131 0.0224  40  TYR C CE2   
8241  C  CZ    . TYR D 41  ? 0.4795 0.4618 0.3578 -0.0874 -0.0238 0.0271  40  TYR C CZ    
8242  O  OH    . TYR D 41  ? 0.4753 0.4585 0.3544 -0.0874 -0.0325 0.0294  40  TYR C OH    
8252  N  N     . ARG D 42  ? 0.3145 0.3047 0.2262 -0.0734 0.0158  0.0167  41  ARG C N     
8253  C  CA    . ARG D 42  ? 0.3311 0.3241 0.2488 -0.0736 0.0219  0.0165  41  ARG C CA    
8254  C  C     . ARG D 42  ? 0.3243 0.3146 0.2378 -0.0778 0.0126  0.0243  41  ARG C C     
8255  O  O     . ARG D 42  ? 0.3287 0.3164 0.2459 -0.0734 0.0015  0.0291  41  ARG C O     
8256  C  CB    . ARG D 42  ? 0.3479 0.3447 0.2844 -0.0621 0.0245  0.0141  41  ARG C CB    
8257  C  CG    . ARG D 42  ? 0.4362 0.4357 0.3798 -0.0575 0.0346  0.0069  41  ARG C CG    
8258  C  CD    . ARG D 42  ? 0.4631 0.4652 0.4055 -0.0631 0.0476  0.0021  41  ARG C CD    
8259  N  NE    . ARG D 42  ? 0.4860 0.4922 0.4445 -0.0553 0.0557  -0.0024 41  ARG C NE    
8260  C  CZ    . ARG D 42  ? 0.3907 0.4005 0.3638 -0.0484 0.0538  -0.0002 41  ARG C CZ    
8261  N  NH1   . ARG D 42  ? 0.4484 0.4579 0.4222 -0.0477 0.0444  0.0058  41  ARG C NH1   
8262  N  NH2   . ARG D 42  ? 0.4813 0.4949 0.4686 -0.0423 0.0611  -0.0038 41  ARG C NH2   
8276  N  N     . LYS D 43  ? 0.3174 0.3081 0.2239 -0.0863 0.0174  0.0253  42  LYS C N     
8277  C  CA    . LYS D 43  ? 0.3503 0.3383 0.2537 -0.0905 0.0095  0.0328  42  LYS C CA    
8278  C  C     . LYS D 43  ? 0.3406 0.3322 0.2455 -0.0954 0.0183  0.0318  42  LYS C C     
8279  O  O     . LYS D 43  ? 0.3436 0.3378 0.2422 -0.1018 0.0296  0.0268  42  LYS C O     
8280  C  CB    . LYS D 43  ? 0.3871 0.3695 0.2723 -0.1008 0.0018  0.0385  42  LYS C CB    
8281  C  CG    . LYS D 43  ? 0.4210 0.3991 0.3028 -0.1053 -0.0080 0.0473  42  LYS C CG    
8282  C  CD    . LYS D 43  ? 0.4453 0.4183 0.3075 -0.1173 -0.0142 0.0529  42  LYS C CD    
8283  C  CE    . LYS D 43  ? 0.5836 0.5510 0.4418 -0.1222 -0.0248 0.0626  42  LYS C CE    
8284  N  NZ    . LYS D 43  ? 0.6456 0.6082 0.5096 -0.1162 -0.0394 0.0685  42  LYS C NZ    
8298  N  N     . GLN D 44  ? 0.3636 0.3552 0.2772 -0.0927 0.0135  0.0361  43  GLN C N     
8299  C  CA    . GLN D 44  ? 0.3518 0.3471 0.2670 -0.0984 0.0205  0.0363  43  GLN C CA    
8300  C  C     . GLN D 44  ? 0.3878 0.3778 0.2876 -0.1099 0.0145  0.0436  43  GLN C C     
8301  O  O     . GLN D 44  ? 0.3731 0.3568 0.2691 -0.1096 0.0019  0.0501  43  GLN C O     
8302  C  CB    . GLN D 44  ? 0.3488 0.3478 0.2825 -0.0899 0.0194  0.0367  43  GLN C CB    
8303  C  CG    . GLN D 44  ? 0.3286 0.3227 0.2669 -0.0856 0.0062  0.0430  43  GLN C CG    
8304  C  CD    . GLN D 44  ? 0.4009 0.3991 0.3544 -0.0811 0.0068  0.0433  43  GLN C CD    
8305  O  OE1   . GLN D 44  ? 0.3571 0.3596 0.3120 -0.0870 0.0135  0.0433  43  GLN C OE1   
8306  N  NE2   . GLN D 44  ? 0.3156 0.3129 0.2804 -0.0712 0.0002  0.0434  43  GLN C NE2   
8315  N  N     . VAL D 45  ? 0.3775 0.3701 0.2685 -0.1204 0.0238  0.0423  44  VAL C N     
8316  C  CA    . VAL D 45  ? 0.4210 0.4092 0.2949 -0.1335 0.0204  0.0488  44  VAL C CA    
8317  C  C     . VAL D 45  ? 0.4713 0.4654 0.3476 -0.1401 0.0314  0.0469  44  VAL C C     
8318  O  O     . VAL D 45  ? 0.4305 0.4321 0.3205 -0.1350 0.0423  0.0400  44  VAL C O     
8319  C  CB    . VAL D 45  ? 0.4455 0.4302 0.2984 -0.1432 0.0215  0.0481  44  VAL C CB    
8320  C  CG1   . VAL D 45  ? 0.4873 0.4672 0.3398 -0.1367 0.0103  0.0502  44  VAL C CG1   
8321  C  CG2   . VAL D 45  ? 0.4252 0.4158 0.2765 -0.1456 0.0379  0.0380  44  VAL C CG2   
8331  N  N     . VAL D 46  ? 0.4645 0.4551 0.3279 -0.1517 0.0284  0.0535  45  VAL C N     
8332  C  CA    . VAL D 46  ? 0.4779 0.4741 0.3401 -0.1607 0.0396  0.0519  45  VAL C CA    
8333  C  C     . VAL D 46  ? 0.4846 0.4779 0.3220 -0.1759 0.0442  0.0523  45  VAL C C     
8334  O  O     . VAL D 46  ? 0.5244 0.5096 0.3454 -0.1830 0.0332  0.0603  45  VAL C O     
8335  C  CB    . VAL D 46  ? 0.5071 0.5020 0.3758 -0.1621 0.0327  0.0593  45  VAL C CB    
8336  C  CG1   . VAL D 46  ? 0.4850 0.4873 0.3548 -0.1711 0.0455  0.0570  45  VAL C CG1   
8337  C  CG2   . VAL D 46  ? 0.4740 0.4704 0.3644 -0.1477 0.0267  0.0590  45  VAL C CG2   
8347  N  N     . ILE D 47  ? 0.4485 0.4482 0.2833 -0.1808 0.0603  0.0437  46  ILE C N     
8348  C  CA    . ILE D 47  ? 0.4512 0.4490 0.2634 -0.1945 0.0664  0.0415  46  ILE C CA    
8349  C  C     . ILE D 47  ? 0.5450 0.5497 0.3621 -0.1989 0.0782  0.0367  46  ILE C C     
8350  O  O     . ILE D 47  ? 0.5431 0.5563 0.3775 -0.1932 0.0907  0.0290  46  ILE C O     
8351  C  CB    . ILE D 47  ? 0.5363 0.5344 0.3432 -0.1924 0.0734  0.0323  46  ILE C CB    
8352  C  CG1   . ILE D 47  ? 0.5044 0.4959 0.3074 -0.1872 0.0603  0.0371  46  ILE C CG1   
8353  C  CG2   . ILE D 47  ? 0.5457 0.5421 0.3342 -0.2029 0.0783  0.0273  46  ILE C CG2   
8354  C  CD1   . ILE D 47  ? 0.5410 0.5340 0.3469 -0.1809 0.0670  0.0276  46  ILE C CD1   
8366  N  N     . ASP D 48  ? 0.5527 0.5539 0.3559 -0.2088 0.0736  0.0417  47  ASP C N     
8367  C  CA    . ASP D 48  ? 0.5574 0.5645 0.3627 -0.2146 0.0841  0.0378  47  ASP C CA    
8368  C  C     . ASP D 48  ? 0.5544 0.5698 0.3842 -0.2076 0.0894  0.0377  47  ASP C C     
8369  O  O     . ASP D 48  ? 0.6001 0.6244 0.4419 -0.2066 0.1028  0.0302  47  ASP C O     
8370  C  CB    . ASP D 48  ? 0.5131 0.5236 0.3122 -0.2179 0.0981  0.0260  47  ASP C CB    
8371  C  CG    . ASP D 48  ? 0.5748 0.5774 0.3489 -0.2270 0.0922  0.0265  47  ASP C CG    
8372  O  OD1   . ASP D 48  ? 0.5431 0.5390 0.3039 -0.2333 0.0788  0.0364  47  ASP C OD1   
8373  O  OD2   . ASP D 48  ? 0.6299 0.6328 0.3980 -0.2282 0.1004  0.0171  47  ASP C OD2   
8378  N  N     . GLY D 49  ? 0.5262 0.5386 0.3643 -0.2027 0.0779  0.0462  48  GLY C N     
8379  C  CA    . GLY D 49  ? 0.5337 0.5527 0.3937 -0.1974 0.0794  0.0480  48  GLY C CA    
8380  C  C     . GLY D 49  ? 0.5402 0.5667 0.4226 -0.1850 0.0857  0.0414  48  GLY C C     
8381  O  O     . GLY D 49  ? 0.5520 0.5841 0.4552 -0.1777 0.0847  0.0419  48  GLY C O     
8385  N  N     . GLU D 50  ? 0.5136 0.5398 0.3942 -0.1798 0.0902  0.0344  49  GLU C N     
8386  C  CA    . GLU D 50  ? 0.5190 0.5518 0.4222 -0.1659 0.0957  0.0269  49  GLU C CA    
8387  C  C     . GLU D 50  ? 0.5219 0.5476 0.4258 -0.1550 0.0830  0.0290  49  GLU C C     
8388  O  O     . GLU D 50  ? 0.5019 0.5205 0.3881 -0.1585 0.0790  0.0296  49  GLU C O     
8389  C  CB    . GLU D 50  ? 0.5930 0.6317 0.4962 -0.1685 0.1135  0.0159  49  GLU C CB    
8390  C  CG    . GLU D 50  ? 0.6503 0.6942 0.5760 -0.1539 0.1183  0.0086  49  GLU C CG    
8391  C  CD    . GLU D 50  ? 0.7099 0.7650 0.6527 -0.1536 0.1359  -0.0001 49  GLU C CD    
8392  O  OE1   . GLU D 50  ? 0.7744 0.8372 0.7321 -0.1539 0.1383  0.0019  49  GLU C OE1   
8393  O  OE2   . GLU D 50  ? 0.7799 0.8354 0.7232 -0.1513 0.1457  -0.0090 49  GLU C OE2   
8400  N  N     . THR D 51  ? 0.5164 0.5442 0.4401 -0.1424 0.0764  0.0303  50  THR C N     
8401  C  CA    . THR D 51  ? 0.4614 0.4837 0.3877 -0.1317 0.0659  0.0313  50  THR C CA    
8402  C  C     . THR D 51  ? 0.5082 0.5331 0.4377 -0.1264 0.0751  0.0226  50  THR C C     
8403  O  O     . THR D 51  ? 0.5054 0.5383 0.4486 -0.1236 0.0872  0.0160  50  THR C O     
8404  C  CB    . THR D 51  ? 0.4410 0.4651 0.3867 -0.1206 0.0576  0.0343  50  THR C CB    
8405  O  OG1   . THR D 51  ? 0.4769 0.4973 0.4189 -0.1261 0.0489  0.0423  50  THR C OG1   
8406  C  CG2   . THR D 51  ? 0.4689 0.4879 0.4172 -0.1098 0.0481  0.0346  50  THR C CG2   
8414  N  N     . CYS D 52  ? 0.4338 0.4519 0.3511 -0.1254 0.0697  0.0224  51  CYS C N     
8415  C  CA    . CYS D 52  ? 0.4749 0.4945 0.3962 -0.1196 0.0771  0.0145  51  CYS C CA    
8416  C  C     . CYS D 52  ? 0.4228 0.4363 0.3421 -0.1119 0.0658  0.0166  51  CYS C C     
8417  O  O     . CYS D 52  ? 0.3660 0.3736 0.2772 -0.1132 0.0530  0.0238  51  CYS C O     
8418  C  CB    . CYS D 52  ? 0.5116 0.5306 0.4165 -0.1303 0.0884  0.0086  51  CYS C CB    
8419  S  SG    . CYS D 52  ? 0.6145 0.6247 0.4905 -0.1437 0.0794  0.0154  51  CYS C SG    
8425  N  N     . LEU D 53  ? 0.4166 0.4318 0.3439 -0.1043 0.0712  0.0101  52  LEU C N     
8426  C  CA    . LEU D 53  ? 0.3610 0.3719 0.2886 -0.0964 0.0630  0.0105  52  LEU C CA    
8427  C  C     . LEU D 53  ? 0.4618 0.4690 0.3731 -0.1030 0.0676  0.0060  52  LEU C C     
8428  O  O     . LEU D 53  ? 0.4810 0.4908 0.3928 -0.1052 0.0805  -0.0016 52  LEU C O     
8429  C  CB    . LEU D 53  ? 0.4228 0.4380 0.3711 -0.0837 0.0654  0.0069  52  LEU C CB    
8430  C  CG    . LEU D 53  ? 0.4129 0.4246 0.3649 -0.0743 0.0560  0.0083  52  LEU C CG    
8431  C  CD1   . LEU D 53  ? 0.3704 0.3776 0.3175 -0.0741 0.0417  0.0161  52  LEU C CD1   
8432  C  CD2   . LEU D 53  ? 0.4425 0.4591 0.4151 -0.0630 0.0586  0.0059  52  LEU C CD2   
8444  N  N     . LEU D 54  ? 0.4366 0.4377 0.3335 -0.1068 0.0571  0.0108  53  LEU C N     
8445  C  CA    . LEU D 54  ? 0.3895 0.3870 0.2708 -0.1129 0.0595  0.0071  53  LEU C CA    
8446  C  C     . LEU D 54  ? 0.4177 0.4143 0.3075 -0.1027 0.0559  0.0047  53  LEU C C     
8447  O  O     . LEU D 54  ? 0.3993 0.3948 0.2966 -0.0950 0.0449  0.0096  53  LEU C O     
8448  C  CB    . LEU D 54  ? 0.4149 0.4069 0.2759 -0.1235 0.0497  0.0140  53  LEU C CB    
8449  C  CG    . LEU D 54  ? 0.4817 0.4737 0.3327 -0.1345 0.0512  0.0183  53  LEU C CG    
8450  C  CD1   . LEU D 54  ? 0.4857 0.4715 0.3153 -0.1458 0.0412  0.0256  53  LEU C CD1   
8451  C  CD2   . LEU D 54  ? 0.5092 0.5054 0.3571 -0.1413 0.0683  0.0100  53  LEU C CD2   
8463  N  N     . ASP D 55  ? 0.4188 0.4158 0.3079 -0.1026 0.0659  -0.0034 54  ASP C N     
8464  C  CA    . ASP D 55  ? 0.3942 0.3898 0.2885 -0.0951 0.0640  -0.0064 54  ASP C CA    
8465  C  C     . ASP D 55  ? 0.4630 0.4542 0.3374 -0.1051 0.0641  -0.0085 54  ASP C C     
8466  O  O     . ASP D 55  ? 0.4473 0.4380 0.3115 -0.1137 0.0750  -0.0145 54  ASP C O     
8467  C  CB    . ASP D 55  ? 0.4558 0.4547 0.3664 -0.0871 0.0752  -0.0137 54  ASP C CB    
8468  C  CG    . ASP D 55  ? 0.4885 0.4856 0.4045 -0.0796 0.0729  -0.0161 54  ASP C CG    
8469  O  OD1   . ASP D 55  ? 0.5192 0.5127 0.4225 -0.0853 0.0741  -0.0193 54  ASP C OD1   
8470  O  OD2   . ASP D 55  ? 0.5238 0.5230 0.4555 -0.0689 0.0693  -0.0144 54  ASP C OD2   
8475  N  N     . ILE D 56  ? 0.3993 0.3875 0.2672 -0.1053 0.0516  -0.0031 55  ILE C N     
8476  C  CA    . ILE D 56  ? 0.4431 0.4274 0.2908 -0.1162 0.0483  -0.0026 55  ILE C CA    
8477  C  C     . ILE D 56  ? 0.4376 0.4208 0.2883 -0.1111 0.0459  -0.0057 55  ILE C C     
8478  O  O     . ILE D 56  ? 0.3743 0.3585 0.2374 -0.1014 0.0376  -0.0023 55  ILE C O     
8479  C  CB    . ILE D 56  ? 0.4299 0.4116 0.2673 -0.1220 0.0345  0.0074  55  ILE C CB    
8480  C  CG1   . ILE D 56  ? 0.4620 0.4447 0.2967 -0.1274 0.0375  0.0105  55  ILE C CG1   
8481  C  CG2   . ILE D 56  ? 0.4516 0.4296 0.2680 -0.1338 0.0299  0.0087  55  ILE C CG2   
8482  C  CD1   . ILE D 56  ? 0.4998 0.4795 0.3279 -0.1315 0.0239  0.0209  55  ILE C CD1   
8494  N  N     . LEU D 57  ? 0.4221 0.4031 0.2610 -0.1184 0.0533  -0.0123 56  LEU C N     
8495  C  CA    . LEU D 57  ? 0.4283 0.4079 0.2680 -0.1156 0.0518  -0.0157 56  LEU C CA    
8496  C  C     . LEU D 57  ? 0.4561 0.4328 0.2762 -0.1268 0.0431  -0.0122 56  LEU C C     
8497  O  O     . LEU D 57  ? 0.4848 0.4591 0.2865 -0.1394 0.0478  -0.0145 56  LEU C O     
8498  C  CB    . LEU D 57  ? 0.5019 0.4807 0.3446 -0.1150 0.0669  -0.0264 56  LEU C CB    
8499  C  CG    . LEU D 57  ? 0.5060 0.4826 0.3485 -0.1134 0.0667  -0.0307 56  LEU C CG    
8500  C  CD1   . LEU D 57  ? 0.5195 0.4986 0.3805 -0.1000 0.0590  -0.0269 56  LEU C CD1   
8501  C  CD2   . LEU D 57  ? 0.5597 0.5339 0.4025 -0.1150 0.0822  -0.0416 56  LEU C CD2   
8513  N  N     . ASP D 58  ? 0.3850 0.3622 0.2096 -0.1224 0.0302  -0.0065 57  ASP C N     
8514  C  CA    . ASP D 58  ? 0.4429 0.4183 0.2529 -0.1313 0.0190  -0.0014 57  ASP C CA    
8515  C  C     . ASP D 58  ? 0.4774 0.4524 0.2865 -0.1313 0.0209  -0.0072 57  ASP C C     
8516  O  O     . ASP D 58  ? 0.4606 0.4378 0.2858 -0.1205 0.0192  -0.0080 57  ASP C O     
8517  C  CB    . ASP D 58  ? 0.4643 0.4411 0.2833 -0.1254 0.0035  0.0087  57  ASP C CB    
8518  C  CG    . ASP D 58  ? 0.4984 0.4740 0.3050 -0.1340 -0.0096 0.0151  57  ASP C CG    
8519  O  OD1   . ASP D 58  ? 0.4794 0.4525 0.2663 -0.1469 -0.0074 0.0135  57  ASP C OD1   
8520  O  OD2   . ASP D 58  ? 0.4676 0.4448 0.2849 -0.1278 -0.0220 0.0219  57  ASP C OD2   
8525  N  N     . THR D 59  ? 0.5031 0.4750 0.2928 -0.1440 0.0241  -0.0109 58  THR C N     
8526  C  CA    . THR D 59  ? 0.5264 0.4971 0.3137 -0.1456 0.0284  -0.0180 58  THR C CA    
8527  C  C     . THR D 59  ? 0.5385 0.5091 0.3146 -0.1534 0.0154  -0.0129 58  THR C C     
8528  O  O     . THR D 59  ? 0.5416 0.5124 0.3091 -0.1594 0.0036  -0.0040 58  THR C O     
8529  C  CB    . THR D 59  ? 0.5584 0.5253 0.3329 -0.1541 0.0440  -0.0282 58  THR C CB    
8530  O  OG1   . THR D 59  ? 0.5736 0.5377 0.3234 -0.1701 0.0413  -0.0265 58  THR C OG1   
8531  C  CG2   . THR D 59  ? 0.5817 0.5495 0.3665 -0.1482 0.0556  -0.0316 58  THR C CG2   
8539  N  N     . ALA D 60  ? 0.5894 0.5597 0.3668 -0.1532 0.0174  -0.0183 59  ALA C N     
8540  C  CA    . ALA D 60  ? 0.5520 0.5226 0.3190 -0.1615 0.0069  -0.0154 59  ALA C CA    
8541  C  C     . ALA D 60  ? 0.5784 0.5441 0.3205 -0.1775 0.0135  -0.0216 59  ALA C C     
8542  O  O     . ALA D 60  ? 0.5948 0.5568 0.3331 -0.1791 0.0287  -0.0317 59  ALA C O     
8543  C  CB    . ALA D 60  ? 0.5751 0.5484 0.3577 -0.1528 0.0051  -0.0177 59  ALA C CB    
8549  N  N     . GLY D 61  ? 0.6961 0.6616 0.4218 -0.1893 0.0020  -0.0158 60  GLY C N     
8550  C  CA    . GLY D 61  ? 0.7284 0.6895 0.4314 -0.2049 0.0068  -0.0210 60  GLY C CA    
8551  C  C     . GLY D 61  ? 0.7935 0.7544 0.4953 -0.2086 0.0043  -0.0246 60  GLY C C     
8552  O  O     . GLY D 61  ? 0.7737 0.7326 0.4638 -0.2200 0.0025  -0.0242 60  GLY C O     
8556  N  N     . GLN D 62  ? 0.7755 0.7389 0.4922 -0.1985 0.0044  -0.0276 61  GLN C N     
8557  C  CA    . GLN D 62  ? 0.8032 0.7663 0.5175 -0.2027 0.0027  -0.0319 61  GLN C CA    
8558  C  C     . GLN D 62  ? 0.8256 0.7823 0.5325 -0.2085 0.0190  -0.0435 61  GLN C C     
8559  O  O     . GLN D 62  ? 0.7731 0.7266 0.4865 -0.2020 0.0331  -0.0518 61  GLN C O     
8560  C  CB    . GLN D 62  ? 0.7148 0.6827 0.4550 -0.1879 0.0005  -0.0313 61  GLN C CB    
8561  C  CG    . GLN D 62  ? 0.6493 0.6233 0.4092 -0.1753 -0.0095 -0.0215 61  GLN C CG    
8562  C  CD    . GLN D 62  ? 0.7155 0.6953 0.4778 -0.1779 -0.0277 -0.0116 61  GLN C CD    
8563  O  OE1   . GLN D 62  ? 0.7129 0.6943 0.4718 -0.1838 -0.0326 -0.0126 61  GLN C OE1   
8564  N  NE2   . GLN D 62  ? 0.7177 0.7007 0.4873 -0.1732 -0.0379 -0.0018 61  GLN C NE2   
8573  N  N     . GLU D 63  ? 0.8659 0.8206 0.5610 -0.2203 0.0170  -0.0437 62  GLU C N     
8574  C  CA    . GLU D 63  ? 0.8756 0.8240 0.5640 -0.2268 0.0315  -0.0545 62  GLU C CA    
8575  C  C     . GLU D 63  ? 0.8420 0.7880 0.5419 -0.2190 0.0409  -0.0638 62  GLU C C     
8576  O  O     . GLU D 63  ? 0.8147 0.7548 0.5152 -0.2197 0.0557  -0.0736 62  GLU C O     
8577  C  CB    . GLU D 63  ? 0.9075 0.8548 0.5810 -0.2410 0.0256  -0.0520 62  GLU C CB    
8578  C  CG    . GLU D 63  ? 0.9808 0.9323 0.6471 -0.2468 0.0095  -0.0389 62  GLU C CG    
8579  C  CD    . GLU D 63  ? 1.0908 1.0393 0.7390 -0.2625 0.0081  -0.0373 62  GLU C CD    
8580  O  OE1   . GLU D 63  ? 1.1399 1.0832 0.7803 -0.2695 0.0198  -0.0468 62  GLU C OE1   
8581  O  OE2   . GLU D 63  ? 1.0715 1.0225 0.7138 -0.2678 -0.0046 -0.0264 62  GLU C OE2   
8588  N  N     . GLU D 64  ? 0.7992 0.7495 0.5095 -0.2118 0.0325  -0.0609 63  GLU C N     
8589  C  CA    . GLU D 64  ? 0.7697 0.7173 0.4901 -0.2060 0.0402  -0.0692 63  GLU C CA    
8590  C  C     . GLU D 64  ? 0.7511 0.6942 0.4813 -0.1968 0.0561  -0.0772 63  GLU C C     
8591  O  O     . GLU D 64  ? 0.7733 0.7107 0.5082 -0.1957 0.0677  -0.0860 63  GLU C O     
8592  C  CB    . GLU D 64  ? 0.7611 0.7152 0.4942 -0.1988 0.0280  -0.0638 63  GLU C CB    
8593  C  CG    . GLU D 64  ? 0.8158 0.7716 0.5458 -0.2061 0.0204  -0.0636 63  GLU C CG    
8594  C  CD    . GLU D 64  ? 0.8746 0.8228 0.6001 -0.2111 0.0334  -0.0737 63  GLU C CD    
8595  O  OE1   . GLU D 64  ? 0.8551 0.7989 0.5908 -0.2035 0.0444  -0.0815 63  GLU C OE1   
8596  O  OE2   . GLU D 64  ? 0.9430 0.8892 0.6552 -0.2226 0.0325  -0.0736 63  GLU C OE2   
8603  N  N     . TYR D 65  ? 0.6931 0.6385 0.4276 -0.1901 0.0568  -0.0737 64  TYR C N     
8604  C  CA    . TYR D 65  ? 0.7087 0.6521 0.4592 -0.1783 0.0696  -0.0786 64  TYR C CA    
8605  C  C     . TYR D 65  ? 0.7826 0.7227 0.5275 -0.1819 0.0804  -0.0825 64  TYR C C     
8606  O  O     . TYR D 65  ? 0.7622 0.7031 0.5181 -0.1731 0.0876  -0.0833 64  TYR C O     
8607  C  CB    . TYR D 65  ? 0.6274 0.5780 0.3997 -0.1634 0.0616  -0.0692 64  TYR C CB    
8608  C  CG    . TYR D 65  ? 0.5548 0.5107 0.3363 -0.1596 0.0485  -0.0630 64  TYR C CG    
8609  C  CD1   . TYR D 65  ? 0.5739 0.5281 0.3636 -0.1567 0.0517  -0.0678 64  TYR C CD1   
8610  C  CD2   . TYR D 65  ? 0.5187 0.4813 0.3010 -0.1595 0.0334  -0.0524 64  TYR C CD2   
8611  C  CE1   . TYR D 65  ? 0.4689 0.4289 0.2677 -0.1537 0.0404  -0.0623 64  TYR C CE1   
8612  C  CE2   . TYR D 65  ? 0.5181 0.4863 0.3107 -0.1559 0.0222  -0.0471 64  TYR C CE2   
8613  C  CZ    . TYR D 65  ? 0.4680 0.4353 0.2687 -0.1532 0.0260  -0.0523 64  TYR C CZ    
8614  O  OH    . TYR D 65  ? 0.4477 0.4215 0.2588 -0.1502 0.0150  -0.0470 64  TYR C OH    
8624  N  N     . SER D 66  ? 0.8386 0.7758 0.5696 -0.1945 0.0815  -0.0843 65  SER C N     
8625  C  CA    . SER D 66  ? 0.8987 0.8332 0.6265 -0.1985 0.0917  -0.0883 65  SER C CA    
8626  C  C     . SER D 66  ? 0.9059 0.8367 0.6505 -0.1891 0.1069  -0.0971 65  SER C C     
8627  O  O     . SER D 66  ? 0.9133 0.8450 0.6649 -0.1846 0.1136  -0.0980 65  SER C O     
8628  C  CB    . SER D 66  ? 0.9233 0.8540 0.6343 -0.2137 0.0924  -0.0910 65  SER C CB    
8629  O  OG    . SER D 66  ? 0.9133 0.8470 0.6120 -0.2217 0.0778  -0.0833 65  SER C OG    
8635  N  N     . ALA D 67  ? 0.8964 0.8231 0.6489 -0.1857 0.1119  -0.1031 66  ALA C N     
8636  C  CA    . ALA D 67  ? 0.9214 0.8438 0.6911 -0.1769 0.1255  -0.1107 66  ALA C CA    
8637  C  C     . ALA D 67  ? 0.9233 0.8499 0.7090 -0.1639 0.1275  -0.1075 66  ALA C C     
8638  O  O     . ALA D 67  ? 0.9702 0.8956 0.7665 -0.1596 0.1374  -0.1115 66  ALA C O     
8639  C  CB    . ALA D 67  ? 0.9762 0.8942 0.7535 -0.1735 0.1278  -0.1151 66  ALA C CB    
8645  N  N     . MET D 68  ? 0.8820 0.8141 0.6697 -0.1579 0.1178  -0.1001 67  MET C N     
8646  C  CA    . MET D 68  ? 0.9081 0.8443 0.7115 -0.1454 0.1196  -0.0967 67  MET C CA    
8647  C  C     . MET D 68  ? 0.9265 0.8679 0.7244 -0.1471 0.1161  -0.0907 67  MET C C     
8648  O  O     . MET D 68  ? 0.9168 0.8616 0.7284 -0.1375 0.1192  -0.0885 67  MET C O     
8649  C  CB    . MET D 68  ? 0.8422 0.7824 0.6571 -0.1358 0.1098  -0.0902 67  MET C CB    
8650  C  CG    . MET D 68  ? 0.8257 0.7625 0.6400 -0.1374 0.1073  -0.0929 67  MET C CG    
8651  S  SD    . MET D 68  ? 0.8183 0.7601 0.6580 -0.1209 0.1004  -0.0857 67  MET C SD    
8652  C  CE    . MET D 68  ? 0.7402 0.6740 0.5934 -0.1146 0.1162  -0.0953 67  MET C CE    
8662  N  N     . ARG D 69  ? 0.9731 0.9151 0.7520 -0.1590 0.1090  -0.0872 68  ARG C N     
8663  C  CA    . ARG D 69  ? 0.9004 0.8456 0.6735 -0.1627 0.1079  -0.0829 68  ARG C CA    
8664  C  C     . ARG D 69  ? 0.8803 0.8241 0.6663 -0.1582 0.1216  -0.0894 68  ARG C C     
8665  O  O     . ARG D 69  ? 0.9077 0.8554 0.6988 -0.1548 0.1231  -0.0861 68  ARG C O     
8666  C  CB    . ARG D 69  ? 0.9245 0.8681 0.6764 -0.1779 0.1022  -0.0811 68  ARG C CB    
8667  C  CG    . ARG D 69  ? 0.9289 0.8765 0.6683 -0.1827 0.0861  -0.0700 68  ARG C CG    
8668  C  CD    . ARG D 69  ? 0.9554 0.9006 0.6756 -0.1980 0.0803  -0.0688 68  ARG C CD    
8669  N  NE    . ARG D 69  ? 1.0262 0.9736 0.7390 -0.2013 0.0649  -0.0612 68  ARG C NE    
8670  C  CZ    . ARG D 69  ? 1.0503 0.9963 0.7498 -0.2129 0.0585  -0.0598 68  ARG C CZ    
8671  N  NH1   . ARG D 69  ? 1.0134 0.9551 0.7025 -0.2235 0.0661  -0.0655 68  ARG C NH1   
8672  N  NH2   . ARG D 69  ? 1.0007 0.9498 0.6979 -0.2139 0.0440  -0.0524 68  ARG C NH2   
8686  N  N     . ASP D 70  ? 0.8963 0.8346 0.6879 -0.1585 0.1313  -0.0983 69  ASP C N     
8687  C  CA    . ASP D 70  ? 0.9062 0.8427 0.7090 -0.1560 0.1440  -0.1051 69  ASP C CA    
8688  C  C     . ASP D 70  ? 0.8989 0.8403 0.7214 -0.1430 0.1468  -0.1021 69  ASP C C     
8689  O  O     . ASP D 70  ? 0.8366 0.7806 0.6629 -0.1430 0.1517  -0.1025 69  ASP C O     
8690  C  CB    . ASP D 70  ? 0.8963 0.8258 0.7058 -0.1558 0.1528  -0.1141 69  ASP C CB    
8691  C  CG    . ASP D 70  ? 0.9055 0.8300 0.6966 -0.1705 0.1545  -0.1191 69  ASP C CG    
8692  O  OD1   . ASP D 70  ? 0.8779 0.8043 0.6500 -0.1807 0.1459  -0.1143 69  ASP C OD1   
8693  O  OD2   . ASP D 70  ? 0.9673 0.8859 0.7631 -0.1720 0.1643  -0.1275 69  ASP C OD2   
8698  N  N     . GLN D 71  ? 0.8595 0.8027 0.6943 -0.1324 0.1434  -0.0989 70  GLN C N     
8699  C  CA    . GLN D 71  ? 0.9366 0.8846 0.7911 -0.1200 0.1456  -0.0957 70  GLN C CA    
8700  C  C     . GLN D 71  ? 0.8655 0.8199 0.7141 -0.1219 0.1405  -0.0885 70  GLN C C     
8701  O  O     . GLN D 71  ? 0.8690 0.8268 0.7285 -0.1180 0.1459  -0.0885 70  GLN C O     
8702  C  CB    . GLN D 71  ? 0.9389 0.8875 0.8043 -0.1100 0.1415  -0.0928 70  GLN C CB    
8703  C  CG    . GLN D 71  ? 0.9715 0.9234 0.8612 -0.0962 0.1454  -0.0911 70  GLN C CG    
8704  C  CD    . GLN D 71  ? 0.9299 0.8812 0.8329 -0.0937 0.1554  -0.0959 70  GLN C CD    
8705  O  OE1   . GLN D 71  ? 0.9545 0.9003 0.8662 -0.0920 0.1623  -0.1020 70  GLN C OE1   
8706  N  NE2   . GLN D 71  ? 0.9254 0.8823 0.8306 -0.0937 0.1561  -0.0929 70  GLN C NE2   
8715  N  N     . TYR D 72  ? 0.9080 0.8643 0.7400 -0.1280 0.1295  -0.0818 71  TYR C N     
8716  C  CA    . TYR D 72  ? 0.8071 0.7679 0.6313 -0.1320 0.1231  -0.0743 71  TYR C CA    
8717  C  C     . TYR D 72  ? 0.7997 0.7599 0.6201 -0.1387 0.1314  -0.0787 71  TYR C C     
8718  O  O     . TYR D 72  ? 0.7405 0.7050 0.5685 -0.1359 0.1341  -0.0762 71  TYR C O     
8719  C  CB    . TYR D 72  ? 0.8328 0.7931 0.6382 -0.1407 0.1090  -0.0674 71  TYR C CB    
8720  C  CG    . TYR D 72  ? 0.7563 0.7179 0.5692 -0.1336 0.0958  -0.0612 71  TYR C CG    
8721  C  CD1   . TYR D 72  ? 0.8070 0.7712 0.6423 -0.1193 0.0942  -0.0592 71  TYR C CD1   
8722  C  CD2   . TYR D 72  ? 0.7977 0.7585 0.5953 -0.1418 0.0845  -0.0570 71  TYR C CD2   
8723  C  CE1   . TYR D 72  ? 0.8032 0.7691 0.6450 -0.1133 0.0827  -0.0538 71  TYR C CE1   
8724  C  CE2   . TYR D 72  ? 0.7681 0.7309 0.5738 -0.1355 0.0728  -0.0515 71  TYR C CE2   
8725  C  CZ    . TYR D 72  ? 0.7298 0.6952 0.5574 -0.1214 0.0724  -0.0503 71  TYR C CZ    
8726  O  OH    . TYR D 72  ? 0.6488 0.6167 0.4841 -0.1157 0.0616  -0.0454 71  TYR C OH    
8736  N  N     . MET D 73  ? 0.8384 0.7934 0.6475 -0.1481 0.1351  -0.0851 72  MET C N     
8737  C  CA    . MET D 73  ? 0.8243 0.7782 0.6270 -0.1564 0.1419  -0.0893 72  MET C CA    
8738  C  C     . MET D 73  ? 0.7860 0.7415 0.6096 -0.1480 0.1539  -0.0949 72  MET C C     
8739  O  O     . MET D 73  ? 0.7451 0.7029 0.5681 -0.1516 0.1586  -0.0959 72  MET C O     
8740  C  CB    . MET D 73  ? 0.8037 0.7513 0.5906 -0.1681 0.1433  -0.0953 72  MET C CB    
8741  C  CG    . MET D 73  ? 0.8246 0.7721 0.5901 -0.1781 0.1298  -0.0879 72  MET C CG    
8742  S  SD    . MET D 73  ? 0.8389 0.7800 0.5841 -0.1936 0.1296  -0.0932 72  MET C SD    
8743  C  CE    . MET D 73  ? 0.8127 0.7559 0.5369 -0.2036 0.1116  -0.0814 72  MET C CE    
8753  N  N     . ARG D 74  ? 0.8029 0.7576 0.6455 -0.1367 0.1582  -0.0979 73  ARG C N     
8754  C  CA    . ARG D 74  ? 0.7750 0.7312 0.6393 -0.1282 0.1685  -0.1024 73  ARG C CA    
8755  C  C     . ARG D 74  ? 0.6983 0.6624 0.5732 -0.1220 0.1667  -0.0959 73  ARG C C     
8756  O  O     . ARG D 74  ? 0.7267 0.6937 0.6067 -0.1234 0.1730  -0.0979 73  ARG C O     
8757  C  CB    . ARG D 74  ? 0.7479 0.7008 0.6300 -0.1178 0.1717  -0.1057 73  ARG C CB    
8758  C  CG    . ARG D 74  ? 0.8097 0.7547 0.6901 -0.1226 0.1796  -0.1151 73  ARG C CG    
8759  C  CD    . ARG D 74  ? 0.8782 0.8181 0.7633 -0.1178 0.1776  -0.1163 73  ARG C CD    
8760  N  NE    . ARG D 74  ? 0.8446 0.7769 0.7173 -0.1274 0.1811  -0.1233 73  ARG C NE    
8761  C  CZ    . ARG D 74  ? 0.8611 0.7896 0.7239 -0.1308 0.1757  -0.1230 73  ARG C CZ    
8762  N  NH1   . ARG D 74  ? 0.8349 0.7663 0.6981 -0.1254 0.1667  -0.1165 73  ARG C NH1   
8763  N  NH2   . ARG D 74  ? 0.9163 0.8381 0.7687 -0.1401 0.1797  -0.1297 73  ARG C NH2   
8777  N  N     . THR D 75  ? 0.7035 0.6713 0.5813 -0.1159 0.1583  -0.0881 74  THR C N     
8778  C  CA    . THR D 75  ? 0.7111 0.6864 0.6018 -0.1090 0.1567  -0.0819 74  THR C CA    
8779  C  C     . THR D 75  ? 0.6425 0.6212 0.5188 -0.1179 0.1526  -0.0765 74  THR C C     
8780  O  O     . THR D 75  ? 0.7194 0.7039 0.6064 -0.1147 0.1546  -0.0736 74  THR C O     
8781  C  CB    . THR D 75  ? 0.8006 0.7779 0.6982 -0.1004 0.1493  -0.0757 74  THR C CB    
8782  O  OG1   . THR D 75  ? 0.8248 0.7979 0.7052 -0.1058 0.1400  -0.0735 74  THR C OG1   
8783  C  CG2   . THR D 75  ? 0.7951 0.7715 0.7154 -0.0881 0.1541  -0.0791 74  THR C CG2   
8791  N  N     . GLY D 76  ? 0.6360 0.6112 0.4888 -0.1294 0.1466  -0.0748 75  GLY C N     
8792  C  CA    . GLY D 76  ? 0.6607 0.6386 0.4996 -0.1376 0.1402  -0.0676 75  GLY C CA    
8793  C  C     . GLY D 76  ? 0.6631 0.6421 0.4999 -0.1441 0.1479  -0.0716 75  GLY C C     
8794  O  O     . GLY D 76  ? 0.7211 0.6962 0.5539 -0.1493 0.1556  -0.0800 75  GLY C O     
8798  N  N     . GLU D 77  ? 0.6414 0.6257 0.4806 -0.1446 0.1457  -0.0652 76  GLU C N     
8799  C  CA    . GLU D 77  ? 0.5375 0.5239 0.3750 -0.1508 0.1525  -0.0678 76  GLU C CA    
8800  C  C     . GLU D 77  ? 0.6220 0.6046 0.4335 -0.1656 0.1472  -0.0656 76  GLU C C     
8801  O  O     . GLU D 77  ? 0.6580 0.6404 0.4642 -0.1729 0.1543  -0.0705 76  GLU C O     
8802  C  CB    . GLU D 77  ? 0.6252 0.6192 0.4773 -0.1452 0.1522  -0.0618 76  GLU C CB    
8803  C  CG    . GLU D 77  ? 0.6048 0.6037 0.4857 -0.1311 0.1592  -0.0647 76  GLU C CG    
8804  C  CD    . GLU D 77  ? 0.7179 0.7239 0.6117 -0.1253 0.1545  -0.0562 76  GLU C CD    
8805  O  OE1   . GLU D 77  ? 0.6696 0.6752 0.5494 -0.1316 0.1451  -0.0477 76  GLU C OE1   
8806  O  OE2   . GLU D 77  ? 0.6573 0.6685 0.5751 -0.1146 0.1588  -0.0572 76  GLU C OE2   
8813  N  N     . GLY D 78  ? 0.6001 0.5796 0.3957 -0.1703 0.1348  -0.0585 77  GLY C N     
8814  C  CA    . GLY D 78  ? 0.6169 0.5926 0.3885 -0.1843 0.1280  -0.0552 77  GLY C CA    
8815  C  C     . GLY D 78  ? 0.6343 0.6068 0.3930 -0.1870 0.1138  -0.0477 77  GLY C C     
8816  O  O     . GLY D 78  ? 0.6501 0.6240 0.4177 -0.1781 0.1083  -0.0433 77  GLY C O     
8820  N  N     . PHE D 79  ? 0.6820 0.6505 0.4198 -0.1998 0.1074  -0.0458 78  PHE C N     
8821  C  CA    . PHE D 79  ? 0.6052 0.5702 0.3309 -0.2035 0.0955  -0.0411 78  PHE C CA    
8822  C  C     . PHE D 79  ? 0.6726 0.6356 0.3801 -0.2147 0.0819  -0.0311 78  PHE C C     
8823  O  O     . PHE D 79  ? 0.7139 0.6752 0.4088 -0.2259 0.0841  -0.0327 78  PHE C O     
8824  C  CB    . PHE D 79  ? 0.6814 0.6423 0.4028 -0.2074 0.1029  -0.0517 78  PHE C CB    
8825  C  CG    . PHE D 79  ? 0.6883 0.6502 0.4292 -0.1956 0.1148  -0.0606 78  PHE C CG    
8826  C  CD1   . PHE D 79  ? 0.6335 0.5970 0.3864 -0.1924 0.1286  -0.0685 78  PHE C CD1   
8827  C  CD2   . PHE D 79  ? 0.6674 0.6290 0.4164 -0.1871 0.1114  -0.0601 78  PHE C CD2   
8828  C  CE1   . PHE D 79  ? 0.6366 0.6010 0.4099 -0.1808 0.1381  -0.0753 78  PHE C CE1   
8829  C  CE2   . PHE D 79  ? 0.6636 0.6259 0.4315 -0.1761 0.1215  -0.0673 78  PHE C CE2   
8830  C  CZ    . PHE D 79  ? 0.6403 0.6038 0.4208 -0.1728 0.1344  -0.0746 78  PHE C CZ    
8840  N  N     . LEU D 80  ? 0.6392 0.6024 0.3463 -0.2115 0.0676  -0.0204 79  LEU C N     
8841  C  CA    . LEU D 80  ? 0.6860 0.6469 0.3786 -0.2206 0.0519  -0.0095 79  LEU C CA    
8842  C  C     . LEU D 80  ? 0.6569 0.6148 0.3389 -0.2266 0.0450  -0.0100 79  LEU C C     
8843  O  O     . LEU D 80  ? 0.6377 0.5962 0.3262 -0.2194 0.0406  -0.0092 79  LEU C O     
8844  C  CB    . LEU D 80  ? 0.6564 0.6189 0.3573 -0.2128 0.0399  0.0024  79  LEU C CB    
8845  C  CG    . LEU D 80  ? 0.7288 0.6894 0.4212 -0.2197 0.0259  0.0146  79  LEU C CG    
8846  C  CD1   . LEU D 80  ? 0.6899 0.6521 0.3848 -0.2212 0.0331  0.0145  79  LEU C CD1   
8847  C  CD2   . LEU D 80  ? 0.6626 0.6229 0.3626 -0.2120 0.0101  0.0263  79  LEU C CD2   
8859  N  N     . CYS D 81  ? 0.6166 0.5715 0.2827 -0.2401 0.0440  -0.0112 80  CYS C N     
8860  C  CA    . CYS D 81  ? 0.6496 0.6018 0.3054 -0.2475 0.0392  -0.0127 80  CYS C CA    
8861  C  C     . CYS D 81  ? 0.6973 0.6485 0.3441 -0.2543 0.0206  0.0006  80  CYS C C     
8862  O  O     . CYS D 81  ? 0.6872 0.6365 0.3218 -0.2656 0.0168  0.0047  80  CYS C O     
8863  C  CB    . CYS D 81  ? 0.7208 0.6702 0.3656 -0.2584 0.0511  -0.0233 80  CYS C CB    
8864  S  SG    . CYS D 81  ? 0.7782 0.7285 0.4376 -0.2490 0.0718  -0.0382 80  CYS C SG    
8870  N  N     . VAL D 82  ? 0.6434 0.5958 0.2974 -0.2472 0.0088  0.0073  81  VAL C N     
8871  C  CA    . VAL D 82  ? 0.6861 0.6380 0.3370 -0.2508 -0.0098 0.0209  81  VAL C CA    
8872  C  C     . VAL D 82  ? 0.6292 0.5798 0.2708 -0.2598 -0.0164 0.0216  81  VAL C C     
8873  O  O     . VAL D 82  ? 0.6869 0.6382 0.3315 -0.2565 -0.0126 0.0152  81  VAL C O     
8874  C  CB    . VAL D 82  ? 0.6383 0.5928 0.3052 -0.2372 -0.0199 0.0288  81  VAL C CB    
8875  C  CG1   . VAL D 82  ? 0.6579 0.6114 0.3251 -0.2398 -0.0388 0.0430  81  VAL C CG1   
8876  C  CG2   . VAL D 82  ? 0.6274 0.5835 0.3042 -0.2280 -0.0114 0.0270  81  VAL C CG2   
8886  N  N     . PHE D 83  ? 0.6716 0.6200 0.3019 -0.2714 -0.0265 0.0298  82  PHE C N     
8887  C  CA    . PHE D 83  ? 0.7277 0.6754 0.3523 -0.2786 -0.0385 0.0359  82  PHE C CA    
8888  C  C     . PHE D 83  ? 0.7154 0.6629 0.3447 -0.2780 -0.0564 0.0512  82  PHE C C     
8889  O  O     . PHE D 83  ? 0.6829 0.6301 0.3175 -0.2739 -0.0586 0.0561  82  PHE C O     
8890  C  CB    . PHE D 83  ? 0.6205 0.5650 0.2261 -0.2949 -0.0328 0.0308  82  PHE C CB    
8891  C  CG    . PHE D 83  ? 0.7180 0.6597 0.3109 -0.3070 -0.0368 0.0370  82  PHE C CG    
8892  C  CD1   . PHE D 83  ? 0.7250 0.6660 0.3149 -0.3083 -0.0262 0.0320  82  PHE C CD1   
8893  C  CD2   . PHE D 83  ? 0.6653 0.6052 0.2500 -0.3172 -0.0512 0.0478  82  PHE C CD2   
8894  C  CE1   . PHE D 83  ? 0.7221 0.6607 0.3001 -0.3197 -0.0300 0.0375  82  PHE C CE1   
8895  C  CE2   . PHE D 83  ? 0.7485 0.6855 0.3212 -0.3288 -0.0552 0.0537  82  PHE C CE2   
8896  C  CZ    . PHE D 83  ? 0.7287 0.6651 0.2978 -0.3301 -0.0446 0.0484  82  PHE C CZ    
8906  N  N     . ALA D 84  ? 0.6967 0.6443 0.3252 -0.2821 -0.0694 0.0588  83  ALA C N     
8907  C  CA    . ALA D 84  ? 0.6715 0.6187 0.3076 -0.2806 -0.0870 0.0734  83  ALA C CA    
8908  C  C     . ALA D 84  ? 0.7169 0.6609 0.3374 -0.2969 -0.0943 0.0797  83  ALA C C     
8909  O  O     . ALA D 84  ? 0.7253 0.6691 0.3355 -0.3054 -0.0928 0.0761  83  ALA C O     
8910  C  CB    . ALA D 84  ? 0.6944 0.6453 0.3487 -0.2683 -0.0977 0.0783  83  ALA C CB    
8916  N  N     . ILE D 85  ? 0.7286 0.6696 0.3469 -0.3015 -0.1022 0.0889  84  ILE C N     
8917  C  CA    . ILE D 85  ? 0.6995 0.6369 0.3004 -0.3185 -0.1072 0.0941  84  ILE C CA    
8918  C  C     . ILE D 85  ? 0.7739 0.7113 0.3758 -0.3227 -0.1217 0.1033  84  ILE C C     
8919  O  O     . ILE D 85  ? 0.8203 0.7547 0.4067 -0.3378 -0.1263 0.1076  84  ILE C O     
8920  C  CB    . ILE D 85  ? 0.7781 0.7122 0.3773 -0.3218 -0.1119 0.1016  84  ILE C CB    
8921  C  CG1   . ILE D 85  ? 0.7852 0.7193 0.4045 -0.3100 -0.1265 0.1136  84  ILE C CG1   
8922  C  CG2   . ILE D 85  ? 0.7322 0.6666 0.3271 -0.3205 -0.0959 0.0914  84  ILE C CG2   
8923  C  CD1   . ILE D 85  ? 0.8000 0.7314 0.4200 -0.3167 -0.1443 0.1273  84  ILE C CD1   
8935  N  N     . ASN D 86  ? 0.7659 0.7068 0.3856 -0.3102 -0.1287 0.1061  85  ASN C N     
8936  C  CA    . ASN D 86  ? 0.8243 0.7666 0.4458 -0.3134 -0.1401 0.1124  85  ASN C CA    
8937  C  C     . ASN D 86  ? 0.7592 0.7050 0.3797 -0.3111 -0.1321 0.1024  85  ASN C C     
8938  O  O     . ASN D 86  ? 0.7880 0.7365 0.4149 -0.3098 -0.1411 0.1066  85  ASN C O     
8939  C  CB    . ASN D 86  ? 0.8267 0.7706 0.4706 -0.3016 -0.1560 0.1241  85  ASN C CB    
8940  C  CG    . ASN D 86  ? 0.7862 0.7353 0.4508 -0.2837 -0.1537 0.1194  85  ASN C CG    
8941  O  OD1   . ASN D 86  ? 0.7398 0.6900 0.4041 -0.2778 -0.1406 0.1092  85  ASN C OD1   
8942  N  ND2   . ASN D 86  ? 0.7541 0.7063 0.4370 -0.2751 -0.1662 0.1266  85  ASN C ND2   
8949  N  N     . ASN D 87  ? 0.7268 0.6727 0.3401 -0.3109 -0.1153 0.0891  86  ASN C N     
8950  C  CA    . ASN D 87  ? 0.8109 0.7593 0.4230 -0.3090 -0.1063 0.0785  86  ASN C CA    
8951  C  C     . ASN D 87  ? 0.7645 0.7095 0.3560 -0.3221 -0.0912 0.0672  86  ASN C C     
8952  O  O     . ASN D 87  ? 0.8021 0.7466 0.3926 -0.3186 -0.0765 0.0564  86  ASN C O     
8953  C  CB    . ASN D 87  ? 0.7785 0.7307 0.4086 -0.2917 -0.1006 0.0726  86  ASN C CB    
8954  C  CG    . ASN D 87  ? 0.7420 0.6972 0.3754 -0.2876 -0.0948 0.0638  86  ASN C CG    
8955  O  OD1   . ASN D 87  ? 0.7196 0.6736 0.3401 -0.2981 -0.0914 0.0594  86  ASN C OD1   
8956  N  ND2   . ASN D 87  ? 0.7645 0.7237 0.4154 -0.2725 -0.0939 0.0610  86  ASN C ND2   
8963  N  N     . THR D 88  ? 0.7505 0.6932 0.3262 -0.3369 -0.0946 0.0693  87  THR C N     
8964  C  CA    . THR D 88  ? 0.8366 0.7757 0.3925 -0.3502 -0.0805 0.0583  87  THR C CA    
8965  C  C     . THR D 88  ? 0.8176 0.7577 0.3770 -0.3437 -0.0650 0.0436  87  THR C C     
8966  O  O     . THR D 88  ? 0.8235 0.7611 0.3752 -0.3471 -0.0494 0.0322  87  THR C O     
8967  C  CB    . THR D 88  ? 0.8291 0.7660 0.3685 -0.3667 -0.0876 0.0631  87  THR C CB    
8968  O  OG1   . THR D 88  ? 0.8740 0.8094 0.4105 -0.3730 -0.1020 0.0769  87  THR C OG1   
8969  C  CG2   . THR D 88  ? 0.8530 0.7858 0.3716 -0.3811 -0.0726 0.0512  87  THR C CG2   
8977  N  N     . LYS D 89  ? 0.8120 0.7558 0.3839 -0.3342 -0.0691 0.0436  88  LYS C N     
8978  C  CA    . LYS D 89  ? 0.8416 0.7861 0.4179 -0.3277 -0.0554 0.0302  88  LYS C CA    
8979  C  C     . LYS D 89  ? 0.7947 0.7394 0.3805 -0.3165 -0.0435 0.0227  88  LYS C C     
8980  O  O     . LYS D 89  ? 0.7764 0.7187 0.3583 -0.3174 -0.0273 0.0099  88  LYS C O     
8981  C  CB    . LYS D 89  ? 0.8565 0.8056 0.4465 -0.3184 -0.0641 0.0331  88  LYS C CB    
8982  C  CG    . LYS D 89  ? 0.8764 0.8259 0.4710 -0.3125 -0.0514 0.0200  88  LYS C CG    
8983  C  CD    . LYS D 89  ? 0.9693 0.9215 0.5660 -0.3138 -0.0588 0.0215  88  LYS C CD    
8984  C  CE    . LYS D 89  ? 0.9583 0.9166 0.5716 -0.3045 -0.0764 0.0337  88  LYS C CE    
8985  N  NZ    . LYS D 89  ? 1.0371 0.9990 0.6552 -0.3041 -0.0820 0.0333  88  LYS C NZ    
8999  N  N     . SER D 90  ? 0.7734 0.7207 0.3725 -0.3058 -0.0511 0.0304  89  SER C N     
9000  C  CA    . SER D 90  ? 0.7522 0.6997 0.3595 -0.2959 -0.0402 0.0240  89  SER C CA    
9001  C  C     . SER D 90  ? 0.7290 0.6727 0.3231 -0.3054 -0.0287 0.0181  89  SER C C     
9002  O  O     . SER D 90  ? 0.7134 0.6568 0.3117 -0.2997 -0.0148 0.0085  89  SER C O     
9003  C  CB    . SER D 90  ? 0.7425 0.6931 0.3653 -0.2837 -0.0513 0.0342  89  SER C CB    
9004  O  OG    . SER D 90  ? 0.7835 0.7323 0.4007 -0.2908 -0.0618 0.0453  89  SER C OG    
9010  N  N     . PHE D 91  ? 0.7928 0.7338 0.3715 -0.3200 -0.0341 0.0235  90  PHE C N     
9011  C  CA    . PHE D 91  ? 0.8070 0.7447 0.3722 -0.3305 -0.0232 0.0174  90  PHE C CA    
9012  C  C     . PHE D 91  ? 0.7754 0.7102 0.3309 -0.3377 -0.0080 0.0033  90  PHE C C     
9013  O  O     . PHE D 91  ? 0.8201 0.7534 0.3745 -0.3376 0.0072  -0.0075 90  PHE C O     
9014  C  CB    . PHE D 91  ? 0.7824 0.7179 0.3342 -0.3440 -0.0353 0.0287  90  PHE C CB    
9015  C  CG    . PHE D 91  ? 0.8264 0.7588 0.3637 -0.3556 -0.0261 0.0240  90  PHE C CG    
9016  C  CD1   . PHE D 91  ? 0.8087 0.7419 0.3520 -0.3492 -0.0186 0.0209  90  PHE C CD1   
9017  C  CD2   . PHE D 91  ? 0.7853 0.7142 0.3027 -0.3734 -0.0259 0.0232  90  PHE C CD2   
9018  C  CE1   . PHE D 91  ? 0.8135 0.7443 0.3437 -0.3600 -0.0103 0.0165  90  PHE C CE1   
9019  C  CE2   . PHE D 91  ? 0.8602 0.7863 0.3637 -0.3846 -0.0178 0.0189  90  PHE C CE2   
9020  C  CZ    . PHE D 91  ? 0.8152 0.7425 0.3255 -0.3778 -0.0099 0.0154  90  PHE C CZ    
9030  N  N     . GLU D 92  ? 0.8482 0.7823 0.3979 -0.3436 -0.0119 0.0033  91  GLU C N     
9031  C  CA    . GLU D 92  ? 0.7942 0.7254 0.3365 -0.3495 0.0020  -0.0100 91  GLU C CA    
9032  C  C     . GLU D 92  ? 0.9046 0.8366 0.4621 -0.3355 0.0155  -0.0214 91  GLU C C     
9033  O  O     . GLU D 92  ? 0.8963 0.8252 0.4513 -0.3378 0.0316  -0.0341 91  GLU C O     
9034  C  CB    . GLU D 92  ? 0.9213 0.8524 0.4573 -0.3561 -0.0066 -0.0063 91  GLU C CB    
9035  C  CG    . GLU D 92  ? 0.9550 0.8853 0.4768 -0.3700 -0.0214 0.0061  91  GLU C CG    
9036  C  CD    . GLU D 92  ? 0.9743 0.9056 0.4934 -0.3741 -0.0313 0.0108  91  GLU C CD    
9037  O  OE1   . GLU D 92  ? 1.1011 1.0359 0.6349 -0.3620 -0.0342 0.0108  91  GLU C OE1   
9038  O  OE2   . GLU D 92  ? 1.1411 1.0699 0.6434 -0.3895 -0.0361 0.0145  91  GLU C OE2   
9045  N  N     . ASP D 93  ? 0.8111 0.7471 0.3853 -0.3209 0.0091  -0.0170 92  ASP C N     
9046  C  CA    . ASP D 93  ? 0.8604 0.7972 0.4499 -0.3070 0.0205  -0.0264 92  ASP C CA    
9047  C  C     . ASP D 93  ? 0.8508 0.7872 0.4451 -0.3023 0.0323  -0.0322 92  ASP C C     
9048  O  O     . ASP D 93  ? 0.8849 0.8207 0.4898 -0.2936 0.0456  -0.0426 92  ASP C O     
9049  C  CB    . ASP D 93  ? 0.8617 0.8033 0.4675 -0.2928 0.0097  -0.0191 92  ASP C CB    
9050  C  CG    . ASP D 93  ? 0.8710 0.8142 0.4768 -0.2942 -0.0002 -0.0154 92  ASP C CG    
9051  O  OD1   . ASP D 93  ? 0.9114 0.8516 0.5057 -0.3049 0.0034  -0.0201 92  ASP C OD1   
9052  O  OD2   . ASP D 93  ? 0.8276 0.7751 0.4457 -0.2844 -0.0114 -0.0079 92  ASP C OD2   
9057  N  N     . ILE D 94  ? 0.8212 0.7581 0.4098 -0.3069 0.0274  -0.0253 93  ILE C N     
9058  C  CA    . ILE D 94  ? 0.8206 0.7577 0.4149 -0.3017 0.0383  -0.0303 93  ILE C CA    
9059  C  C     . ILE D 94  ? 0.8610 0.7947 0.4522 -0.3060 0.0567  -0.0452 93  ILE C C     
9060  O  O     . ILE D 94  ? 0.8232 0.7574 0.4275 -0.2958 0.0690  -0.0536 93  ILE C O     
9061  C  CB    . ILE D 94  ? 0.8401 0.7776 0.4259 -0.3088 0.0304  -0.0209 93  ILE C CB    
9062  C  CG1   . ILE D 94  ? 0.7212 0.6620 0.3165 -0.3002 0.0143  -0.0070 93  ILE C CG1   
9063  C  CG2   . ILE D 94  ? 0.8368 0.7741 0.4244 -0.3077 0.0441  -0.0283 93  ILE C CG2   
9064  C  CD1   . ILE D 94  ? 0.6968 0.6409 0.3098 -0.2841 0.0177  -0.0073 93  ILE C CD1   
9076  N  N     . HIS D 95  ? 0.8833 0.8132 0.4577 -0.3212 0.0587  -0.0486 94  HIS C N     
9077  C  CA    . HIS D 95  ? 0.9198 0.8459 0.4919 -0.3254 0.0760  -0.0630 94  HIS C CA    
9078  C  C     . HIS D 95  ? 0.9712 0.8973 0.5613 -0.3113 0.0853  -0.0716 94  HIS C C     
9079  O  O     . HIS D 95  ? 0.9345 0.8597 0.5348 -0.3051 0.0996  -0.0815 94  HIS C O     
9080  C  CB    . HIS D 95  ? 0.9733 0.8953 0.5267 -0.3418 0.0749  -0.0649 94  HIS C CB    
9081  C  CG    . HIS D 95  ? 1.0577 0.9751 0.6104 -0.3450 0.0915  -0.0797 94  HIS C CG    
9082  N  ND1   . HIS D 95  ? 1.0609 0.9766 0.6198 -0.3408 0.0946  -0.0852 94  HIS C ND1   
9083  C  CD2   . HIS D 95  ? 1.0302 0.9443 0.5773 -0.3522 0.1058  -0.0902 94  HIS C CD2   
9084  C  CE1   . HIS D 95  ? 1.0376 0.9486 0.5949 -0.3452 0.1100  -0.0982 94  HIS C CE1   
9085  N  NE2   . HIS D 95  ? 0.9533 0.8634 0.5038 -0.3519 0.1172  -0.1016 94  HIS C NE2   
9093  N  N     . HIS D 96  ? 0.9187 0.8461 0.5140 -0.3058 0.0766  -0.0673 95  HIS C N     
9094  C  CA    . HIS D 96  ? 0.9254 0.8520 0.5356 -0.2946 0.0849  -0.0755 95  HIS C CA    
9095  C  C     . HIS D 96  ? 0.8771 0.8066 0.5067 -0.2784 0.0904  -0.0770 95  HIS C C     
9096  O  O     . HIS D 96  ? 0.9051 0.8327 0.5463 -0.2718 0.1044  -0.0873 95  HIS C O     
9097  C  CB    . HIS D 96  ? 0.9164 0.8443 0.5268 -0.2931 0.0733  -0.0698 95  HIS C CB    
9098  C  CG    . HIS D 96  ? 0.9885 0.9130 0.5825 -0.3078 0.0712  -0.0710 95  HIS C CG    
9099  N  ND1   . HIS D 96  ? 1.0056 0.9247 0.5937 -0.3153 0.0848  -0.0828 95  HIS C ND1   
9100  C  CD2   . HIS D 96  ? 1.0142 0.9400 0.5967 -0.3166 0.0570  -0.0616 95  HIS C CD2   
9101  C  CE1   . HIS D 96  ? 1.0050 0.9220 0.5773 -0.3285 0.0794  -0.0809 95  HIS C CE1   
9102  N  NE2   . HIS D 96  ? 0.9980 0.9192 0.5670 -0.3295 0.0624  -0.0679 95  HIS C NE2   
9110  N  N     . TYR D 97  ? 0.8690 0.8032 0.5036 -0.2716 0.0795  -0.0665 96  TYR C N     
9111  C  CA    . TYR D 97  ? 0.8723 0.8095 0.5246 -0.2571 0.0851  -0.0676 96  TYR C CA    
9112  C  C     . TYR D 97  ? 0.8491 0.7850 0.5037 -0.2583 0.0995  -0.0758 96  TYR C C     
9113  O  O     . TYR D 97  ? 0.8084 0.7454 0.4798 -0.2468 0.1097  -0.0816 96  TYR C O     
9114  C  CB    . TYR D 97  ? 0.8337 0.7755 0.4885 -0.2519 0.0717  -0.0549 96  TYR C CB    
9115  C  CG    . TYR D 97  ? 0.8220 0.7663 0.4805 -0.2465 0.0579  -0.0468 96  TYR C CG    
9116  C  CD1   . TYR D 97  ? 0.8223 0.7666 0.4686 -0.2559 0.0438  -0.0383 96  TYR C CD1   
9117  C  CD2   . TYR D 97  ? 0.7792 0.7260 0.4539 -0.2321 0.0586  -0.0472 96  TYR C CD2   
9118  C  CE1   . TYR D 97  ? 0.8189 0.7660 0.4703 -0.2506 0.0307  -0.0308 96  TYR C CE1   
9119  C  CE2   . TYR D 97  ? 0.8203 0.7696 0.4984 -0.2274 0.0457  -0.0401 96  TYR C CE2   
9120  C  CZ    . TYR D 97  ? 0.8193 0.7690 0.4861 -0.2368 0.0317  -0.0320 96  TYR C CZ    
9121  O  OH    . TYR D 97  ? 0.8435 0.7964 0.5154 -0.2321 0.0182  -0.0249 96  TYR C OH    
9131  N  N     . ARG D 98  ? 0.9073 0.8414 0.5458 -0.2722 0.1002  -0.0760 97  ARG C N     
9132  C  CA    . ARG D 98  ? 0.8707 0.8041 0.5107 -0.2742 0.1135  -0.0836 97  ARG C CA    
9133  C  C     . ARG D 98  ? 0.8687 0.7980 0.5160 -0.2727 0.1292  -0.0974 97  ARG C C     
9134  O  O     . ARG D 98  ? 0.8970 0.8274 0.5610 -0.2626 0.1404  -0.1038 97  ARG C O     
9135  C  CB    . ARG D 98  ? 0.8971 0.8292 0.5170 -0.2903 0.1104  -0.0807 97  ARG C CB    
9136  C  CG    . ARG D 98  ? 0.8204 0.7542 0.4437 -0.2901 0.1203  -0.0844 97  ARG C CG    
9137  C  CD    . ARG D 98  ? 0.9070 0.8384 0.5103 -0.3071 0.1216  -0.0853 97  ARG C CD    
9138  N  NE    . ARG D 98  ? 0.8339 0.7668 0.4421 -0.3065 0.1339  -0.0915 97  ARG C NE    
9139  C  CZ    . ARG D 98  ? 0.9354 0.8654 0.5386 -0.3145 0.1475  -0.1026 97  ARG C CZ    
9140  N  NH1   . ARG D 98  ? 0.8997 0.8245 0.4935 -0.3232 0.1516  -0.1097 97  ARG C NH1   
9141  N  NH2   . ARG D 98  ? 0.8370 0.7693 0.4450 -0.3139 0.1573  -0.1068 97  ARG C NH2   
9155  N  N     . GLU D 99  ? 0.9023 0.8271 0.5382 -0.2826 0.1298  -0.1016 98  GLU C N     
9156  C  CA    . GLU D 99  ? 0.8465 0.7666 0.4893 -0.2815 0.1440  -0.1144 98  GLU C CA    
9157  C  C     . GLU D 99  ? 0.9089 0.8302 0.5754 -0.2640 0.1488  -0.1172 98  GLU C C     
9158  O  O     . GLU D 99  ? 0.9327 0.8530 0.6137 -0.2573 0.1619  -0.1256 98  GLU C O     
9159  C  CB    . GLU D 99  ? 0.9399 0.8554 0.5678 -0.2932 0.1411  -0.1163 98  GLU C CB    
9160  C  CG    . GLU D 99  ? 0.9532 0.8663 0.5582 -0.3118 0.1404  -0.1164 98  GLU C CG    
9161  C  CD    . GLU D 99  ? 0.9515 0.8612 0.5562 -0.3169 0.1570  -0.1283 98  GLU C CD    
9162  O  OE1   . GLU D 99  ? 0.9093 0.8142 0.5179 -0.3177 0.1681  -0.1388 98  GLU C OE1   
9163  O  OE2   . GLU D 99  ? 0.9844 0.8964 0.5859 -0.3199 0.1591  -0.1272 98  GLU C OE2   
9170  N  N     . GLN D 100 ? 0.7896 0.7135 0.4613 -0.2562 0.1379  -0.1098 99  GLN C N     
9171  C  CA    . GLN D 100 ? 0.7881 0.7127 0.4812 -0.2404 0.1422  -0.1124 99  GLN C CA    
9172  C  C     . GLN D 100 ? 0.8554 0.7837 0.5652 -0.2294 0.1490  -0.1130 99  GLN C C     
9173  O  O     . GLN D 100 ? 0.8652 0.7922 0.5928 -0.2201 0.1599  -0.1203 99  GLN C O     
9174  C  CB    . GLN D 100 ? 0.8614 0.7890 0.5563 -0.2344 0.1287  -0.1036 99  GLN C CB    
9175  C  CG    . GLN D 100 ? 0.8764 0.8037 0.5920 -0.2194 0.1334  -0.1070 99  GLN C CG    
9176  C  CD    . GLN D 100 ? 0.9306 0.8604 0.6474 -0.2143 0.1211  -0.0998 99  GLN C CD    
9177  O  OE1   . GLN D 100 ? 0.9390 0.8716 0.6434 -0.2201 0.1081  -0.0910 99  GLN C OE1   
9178  N  NE2   . GLN D 100 ? 0.9270 0.8559 0.6598 -0.2031 0.1251  -0.1033 99  GLN C NE2   
9187  N  N     . ILE D 101 ? 0.7833 0.7164 0.4888 -0.2301 0.1422  -0.1049 100 ILE C N     
9188  C  CA    . ILE D 101 ? 0.7025 0.6399 0.4245 -0.2195 0.1480  -0.1047 100 ILE C CA    
9189  C  C     . ILE D 101 ? 0.8380 0.7735 0.5652 -0.2219 0.1631  -0.1149 100 ILE C C     
9190  O  O     . ILE D 101 ? 0.8498 0.7868 0.5974 -0.2108 0.1722  -0.1194 100 ILE C O     
9191  C  CB    . ILE D 101 ? 0.8101 0.7527 0.5254 -0.2210 0.1377  -0.0937 100 ILE C CB    
9192  C  CG1   . ILE D 101 ? 0.8012 0.7460 0.5159 -0.2161 0.1235  -0.0837 100 ILE C CG1   
9193  C  CG2   . ILE D 101 ? 0.7801 0.7275 0.5124 -0.2112 0.1448  -0.0939 100 ILE C CG2   
9194  C  CD1   . ILE D 101 ? 0.8164 0.7647 0.5214 -0.2198 0.1107  -0.0718 100 ILE C CD1   
9206  N  N     . LYS D 102 ? 0.7532 0.6857 0.4626 -0.2366 0.1656  -0.1183 101 LYS C N     
9207  C  CA    . LYS D 102 ? 0.8661 0.7964 0.5797 -0.2397 0.1805  -0.1289 101 LYS C CA    
9208  C  C     . LYS D 102 ? 0.8736 0.7997 0.6035 -0.2321 0.1908  -0.1382 101 LYS C C     
9209  O  O     . LYS D 102 ? 0.9023 0.8293 0.6509 -0.2236 0.2015  -0.1440 101 LYS C O     
9210  C  CB    . LYS D 102 ? 0.9036 0.8303 0.5934 -0.2581 0.1813  -0.1316 101 LYS C CB    
9211  C  CG    . LYS D 102 ? 0.8866 0.8174 0.5629 -0.2654 0.1735  -0.1230 101 LYS C CG    
9212  C  CD    . LYS D 102 ? 0.9625 0.8901 0.6168 -0.2835 0.1763  -0.1265 101 LYS C CD    
9213  C  CE    . LYS D 102 ? 0.9482 0.8706 0.5837 -0.2957 0.1699  -0.1261 101 LYS C CE    
9214  N  NZ    . LYS D 102 ? 0.9321 0.8501 0.5516 -0.3116 0.1787  -0.1343 101 LYS C NZ    
9228  N  N     . ARG D 103 ? 0.8001 0.7217 0.5242 -0.2347 0.1870  -0.1392 102 ARG C N     
9229  C  CA    . ARG D 103 ? 0.8045 0.7215 0.5435 -0.2276 0.1954  -0.1471 102 ARG C CA    
9230  C  C     . ARG D 103 ? 0.8198 0.7404 0.5843 -0.2098 0.1968  -0.1450 102 ARG C C     
9231  O  O     . ARG D 103 ? 0.8327 0.7534 0.6148 -0.2029 0.2077  -0.1508 102 ARG C O     
9232  C  CB    . ARG D 103 ? 0.8714 0.7841 0.5993 -0.2329 0.1886  -0.1461 102 ARG C CB    
9233  C  CG    . ARG D 103 ? 0.8494 0.7561 0.5894 -0.2285 0.1975  -0.1547 102 ARG C CG    
9234  C  CD    . ARG D 103 ? 0.8007 0.7061 0.5405 -0.2249 0.1886  -0.1506 102 ARG C CD    
9235  N  NE    . ARG D 103 ? 0.9191 0.8267 0.6812 -0.2082 0.1881  -0.1482 102 ARG C NE    
9236  C  CZ    . ARG D 103 ? 0.8749 0.7801 0.6579 -0.1984 0.1985  -0.1542 102 ARG C CZ    
9237  N  NH1   . ARG D 103 ? 0.8492 0.7497 0.6349 -0.2029 0.2109  -0.1636 102 ARG C NH1   
9238  N  NH2   . ARG D 103 ? 0.8580 0.7656 0.6598 -0.1840 0.1962  -0.1504 102 ARG C NH2   
9252  N  N     . VAL D 104 ? 0.8580 0.7818 0.6251 -0.2025 0.1857  -0.1364 103 VAL C N     
9253  C  CA    . VAL D 104 ? 0.7323 0.6589 0.5229 -0.1861 0.1863  -0.1343 103 VAL C CA    
9254  C  C     . VAL D 104 ? 0.8109 0.7416 0.6181 -0.1788 0.1945  -0.1359 103 VAL C C     
9255  O  O     . VAL D 104 ? 0.7929 0.7230 0.6215 -0.1686 0.2023  -0.1402 103 VAL C O     
9256  C  CB    . VAL D 104 ? 0.8105 0.7416 0.5986 -0.1809 0.1727  -0.1237 103 VAL C CB    
9257  C  CG1   . VAL D 104 ? 0.8237 0.7586 0.6359 -0.1644 0.1735  -0.1210 103 VAL C CG1   
9258  C  CG2   . VAL D 104 ? 0.8480 0.7754 0.6236 -0.1864 0.1651  -0.1226 103 VAL C CG2   
9268  N  N     . LYS D 105 ? 0.8066 0.7419 0.6047 -0.1843 0.1923  -0.1321 104 LYS C N     
9269  C  CA    . LYS D 105 ? 0.7606 0.7011 0.5728 -0.1786 0.1989  -0.1325 104 LYS C CA    
9270  C  C     . LYS D 105 ? 0.8755 0.8132 0.6901 -0.1843 0.2124  -0.1428 104 LYS C C     
9271  O  O     . LYS D 105 ? 0.8671 0.8093 0.6953 -0.1796 0.2191  -0.1442 104 LYS C O     
9272  C  CB    . LYS D 105 ? 0.8096 0.7559 0.6101 -0.1831 0.1906  -0.1238 104 LYS C CB    
9273  C  CG    . LYS D 105 ? 0.8070 0.7563 0.6052 -0.1779 0.1773  -0.1134 104 LYS C CG    
9274  C  CD    . LYS D 105 ? 0.7943 0.7503 0.5911 -0.1771 0.1711  -0.1045 104 LYS C CD    
9275  C  CE    . LYS D 105 ? 0.7289 0.6908 0.5491 -0.1658 0.1782  -0.1049 104 LYS C CE    
9276  N  NZ    . LYS D 105 ? 0.7262 0.6902 0.5672 -0.1512 0.1770  -0.1027 104 LYS C NZ    
9290  N  N     . ASP D 106 ? 0.8113 0.7420 0.6135 -0.1944 0.2167  -0.1500 105 ASP C N     
9291  C  CA    . ASP D 106 ? 0.9284 0.8556 0.7318 -0.2007 0.2302  -0.1606 105 ASP C CA    
9292  C  C     . ASP D 106 ? 0.9789 0.9113 0.7785 -0.2057 0.2339  -0.1603 105 ASP C C     
9293  O  O     . ASP D 106 ? 1.0113 0.9480 0.8301 -0.1976 0.2413  -0.1622 105 ASP C O     
9294  C  CB    . ASP D 106 ? 0.8996 0.8247 0.7293 -0.1889 0.2401  -0.1670 105 ASP C CB    
9295  C  CG    . ASP D 106 ? 0.9417 0.8611 0.7716 -0.1963 0.2539  -0.1789 105 ASP C CG    
9296  O  OD1   . ASP D 106 ? 0.9530 0.8662 0.7644 -0.2085 0.2550  -0.1835 105 ASP C OD1   
9297  O  OD2   . ASP D 106 ? 0.8958 0.8172 0.7451 -0.1899 0.2639  -0.1836 105 ASP C OD2   
9302  N  N     . SER D 107 ? 0.9876 0.9199 0.7626 -0.2192 0.2282  -0.1572 106 SER C N     
9303  C  CA    . SER D 107 ? 1.0073 0.9432 0.7738 -0.2274 0.2319  -0.1576 106 SER C CA    
9304  C  C     . SER D 107 ? 1.0330 0.9657 0.7696 -0.2442 0.2246  -0.1550 106 SER C C     
9305  O  O     . SER D 107 ? 0.9948 0.9236 0.7200 -0.2479 0.2163  -0.1522 106 SER C O     
9306  C  CB    . SER D 107 ? 0.9856 0.9300 0.7626 -0.2187 0.2269  -0.1489 106 SER C CB    
9307  O  OG    . SER D 107 ? 0.9478 0.8960 0.7273 -0.2224 0.2358  -0.1524 106 SER C OG    
9313  N  N     . GLU D 108 ? 1.0556 0.9900 0.7800 -0.2546 0.2277  -0.1558 107 GLU C N     
9314  C  CA    . GLU D 108 ? 1.0797 1.0127 0.7765 -0.2700 0.2186  -0.1505 107 GLU C CA    
9315  C  C     . GLU D 108 ? 1.0482 0.9875 0.7414 -0.2689 0.2088  -0.1392 107 GLU C C     
9316  O  O     . GLU D 108 ? 1.0618 1.0005 0.7335 -0.2813 0.2006  -0.1334 107 GLU C O     
9317  C  CB    . GLU D 108 ? 1.0890 1.0181 0.7713 -0.2852 0.2291  -0.1599 107 GLU C CB    
9318  C  CG    . GLU D 108 ? 1.1277 1.0490 0.8021 -0.2928 0.2342  -0.1685 107 GLU C CG    
9319  C  CD    . GLU D 108 ? 1.1422 1.0601 0.7917 -0.3054 0.2216  -0.1623 107 GLU C CD    
9320  O  OE1   . GLU D 108 ? 1.1674 1.0803 0.8143 -0.3068 0.2206  -0.1651 107 GLU C OE1   
9321  O  OE2   . GLU D 108 ? 1.1685 1.0888 0.8015 -0.3140 0.2123  -0.1541 107 GLU C OE2   
9328  N  N     . ASP D 109 ? 1.0031 0.9484 0.7175 -0.2544 0.2091  -0.1355 108 ASP C N     
9329  C  CA    . ASP D 109 ? 1.0014 0.9533 0.7159 -0.2533 0.2040  -0.1269 108 ASP C CA    
9330  C  C     . ASP D 109 ? 0.9584 0.9152 0.6914 -0.2375 0.1970  -0.1189 108 ASP C C     
9331  O  O     . ASP D 109 ? 1.0039 0.9655 0.7590 -0.2259 0.2037  -0.1205 108 ASP C O     
9332  C  CB    . ASP D 109 ? 1.0915 1.0467 0.8135 -0.2550 0.2174  -0.1338 108 ASP C CB    
9333  C  CG    . ASP D 109 ? 1.1068 1.0673 0.8214 -0.2596 0.2126  -0.1258 108 ASP C CG    
9334  O  OD1   . ASP D 109 ? 1.1341 1.0922 0.8253 -0.2724 0.2037  -0.1201 108 ASP C OD1   
9335  O  OD2   . ASP D 109 ? 1.1236 1.0907 0.8562 -0.2510 0.2176  -0.1249 108 ASP C OD2   
9340  N  N     . VAL D 110 ? 0.8938 0.8495 0.6179 -0.2373 0.1831  -0.1100 109 VAL C N     
9341  C  CA    . VAL D 110 ? 0.8392 0.7988 0.5783 -0.2235 0.1754  -0.1021 109 VAL C CA    
9342  C  C     . VAL D 110 ? 0.7680 0.7308 0.4967 -0.2270 0.1629  -0.0897 109 VAL C C     
9343  O  O     . VAL D 110 ? 0.7740 0.7336 0.4814 -0.2387 0.1537  -0.0848 109 VAL C O     
9344  C  CB    . VAL D 110 ? 0.8070 0.7626 0.5464 -0.2192 0.1696  -0.1018 109 VAL C CB    
9345  C  CG1   . VAL D 110 ? 0.7611 0.7121 0.4757 -0.2323 0.1590  -0.0977 109 VAL C CG1   
9346  C  CG2   . VAL D 110 ? 0.7527 0.7126 0.5068 -0.2058 0.1622  -0.0939 109 VAL C CG2   
9356  N  N     . PRO D 111 ? 0.7363 0.7053 0.4799 -0.2175 0.1616  -0.0838 110 PRO C N     
9357  C  CA    . PRO D 111 ? 0.7195 0.6907 0.4539 -0.2208 0.1491  -0.0715 110 PRO C CA    
9358  C  C     . PRO D 111 ? 0.7048 0.6721 0.4249 -0.2244 0.1342  -0.0637 110 PRO C C     
9359  O  O     . PRO D 111 ? 0.7317 0.6988 0.4605 -0.2154 0.1305  -0.0625 110 PRO C O     
9360  C  CB    . PRO D 111 ? 0.7169 0.6947 0.4738 -0.2071 0.1501  -0.0674 110 PRO C CB    
9361  C  CG    . PRO D 111 ? 0.7265 0.7067 0.5031 -0.1995 0.1652  -0.0781 110 PRO C CG    
9362  C  CD    . PRO D 111 ? 0.7561 0.7300 0.5266 -0.2031 0.1704  -0.0874 110 PRO C CD    
9370  N  N     . MET D 112 ? 0.6547 0.6193 0.3539 -0.2373 0.1251  -0.0577 111 MET C N     
9371  C  CA    . MET D 112 ? 0.7276 0.6880 0.4121 -0.2431 0.1121  -0.0520 111 MET C CA    
9372  C  C     . MET D 112 ? 0.7454 0.7049 0.4138 -0.2532 0.0989  -0.0406 111 MET C C     
9373  O  O     . MET D 112 ? 0.7874 0.7476 0.4493 -0.2606 0.1023  -0.0405 111 MET C O     
9374  C  CB    . MET D 112 ? 0.7847 0.7402 0.4586 -0.2518 0.1186  -0.0618 111 MET C CB    
9375  C  CG    . MET D 112 ? 0.8155 0.7670 0.4763 -0.2579 0.1072  -0.0578 111 MET C CG    
9376  S  SD    . MET D 112 ? 0.8118 0.7595 0.4773 -0.2558 0.1177  -0.0708 111 MET C SD    
9377  C  CE    . MET D 112 ? 0.6415 0.5916 0.3242 -0.2393 0.1106  -0.0658 111 MET C CE    
9387  N  N     . VAL D 113 ? 0.8064 0.7641 0.4689 -0.2536 0.0835  -0.0309 112 VAL C N     
9388  C  CA    . VAL D 113 ? 0.8390 0.7952 0.4884 -0.2623 0.0689  -0.0187 112 VAL C CA    
9389  C  C     . VAL D 113 ? 0.8040 0.7569 0.4429 -0.2675 0.0543  -0.0118 112 VAL C C     
9390  O  O     . VAL D 113 ? 0.8091 0.7627 0.4569 -0.2585 0.0476  -0.0083 112 VAL C O     
9391  C  CB    . VAL D 113 ? 0.8186 0.7780 0.4800 -0.2532 0.0628  -0.0093 112 VAL C CB    
9392  C  CG1   . VAL D 113 ? 0.7862 0.7431 0.4376 -0.2596 0.0448  0.0048  112 VAL C CG1   
9393  C  CG2   . VAL D 113 ? 0.7254 0.6885 0.3947 -0.2515 0.0755  -0.0141 112 VAL C CG2   
9403  N  N     . LEU D 114 ? 0.7150 0.6646 0.3357 -0.2822 0.0488  -0.0093 113 LEU C N     
9404  C  CA    . LEU D 114 ? 0.7632 0.7102 0.3748 -0.2882 0.0342  -0.0018 113 LEU C CA    
9405  C  C     . LEU D 114 ? 0.7566 0.7035 0.3696 -0.2869 0.0165  0.0136  113 LEU C C     
9406  O  O     . LEU D 114 ? 0.7546 0.7011 0.3634 -0.2917 0.0137  0.0191  113 LEU C O     
9407  C  CB    . LEU D 114 ? 0.7844 0.7277 0.3761 -0.3052 0.0356  -0.0052 113 LEU C CB    
9408  C  CG    . LEU D 114 ? 0.7622 0.7028 0.3431 -0.3139 0.0224  0.0013  113 LEU C CG    
9409  C  CD1   . LEU D 114 ? 0.7762 0.7169 0.3628 -0.3084 0.0250  -0.0046 113 LEU C CD1   
9410  C  CD2   . LEU D 114 ? 0.7830 0.7200 0.3425 -0.3328 0.0229  0.0002  113 LEU C CD2   
9422  N  N     . VAL D 115 ? 0.7122 0.6592 0.3313 -0.2810 0.0043  0.0206  114 VAL C N     
9423  C  CA    . VAL D 115 ? 0.6665 0.6132 0.2916 -0.2771 -0.0128 0.0349  114 VAL C CA    
9424  C  C     . VAL D 115 ? 0.7045 0.6492 0.3231 -0.2838 -0.0274 0.0427  114 VAL C C     
9425  O  O     . VAL D 115 ? 0.6541 0.5998 0.2770 -0.2794 -0.0291 0.0405  114 VAL C O     
9426  C  CB    . VAL D 115 ? 0.6661 0.6156 0.3101 -0.2603 -0.0140 0.0368  114 VAL C CB    
9427  C  CG1   . VAL D 115 ? 0.6133 0.5618 0.2646 -0.2563 -0.0309 0.0513  114 VAL C CG1   
9428  C  CG2   . VAL D 115 ? 0.6368 0.5889 0.2883 -0.2537 0.0026  0.0274  114 VAL C CG2   
9438  N  N     . GLY D 116 ? 0.6378 0.5796 0.2470 -0.2942 -0.0382 0.0521  115 GLY C N     
9439  C  CA    . GLY D 116 ? 0.7277 0.6680 0.3351 -0.2986 -0.0545 0.0624  115 GLY C CA    
9440  C  C     . GLY D 116 ? 0.7326 0.6734 0.3569 -0.2872 -0.0694 0.0743  115 GLY C C     
9441  O  O     . GLY D 116 ? 0.7352 0.6738 0.3613 -0.2883 -0.0775 0.0833  115 GLY C O     
9445  N  N     . ASN D 117 ? 0.6031 0.5463 0.2398 -0.2767 -0.0736 0.0745  116 ASN C N     
9446  C  CA    . ASN D 117 ? 0.7009 0.6451 0.3566 -0.2635 -0.0854 0.0833  116 ASN C CA    
9447  C  C     . ASN D 117 ? 0.6690 0.6117 0.3290 -0.2660 -0.1035 0.0956  116 ASN C C     
9448  O  O     . ASN D 117 ? 0.6624 0.6048 0.3133 -0.2750 -0.1068 0.0962  116 ASN C O     
9449  C  CB    . ASN D 117 ? 0.7375 0.6857 0.4060 -0.2502 -0.0808 0.0768  116 ASN C CB    
9450  C  CG    . ASN D 117 ? 0.7437 0.6931 0.4323 -0.2359 -0.0914 0.0844  116 ASN C CG    
9451  O  OD1   . ASN D 117 ? 0.7866 0.7336 0.4811 -0.2358 -0.1034 0.0950  116 ASN C OD1   
9452  N  ND2   . ASN D 117 ? 0.7471 0.7000 0.4471 -0.2241 -0.0874 0.0791  116 ASN C ND2   
9459  N  N     . LYS D 118 ? 0.7348 0.6768 0.4116 -0.2559 -0.1146 0.1047  117 LYS C N     
9460  C  CA    . LYS D 118 ? 0.7004 0.6412 0.3878 -0.2544 -0.1319 0.1165  117 LYS C CA    
9461  C  C     . LYS D 118 ? 0.6700 0.6061 0.3454 -0.2684 -0.1398 0.1249  117 LYS C C     
9462  O  O     . LYS D 118 ? 0.7201 0.6551 0.3963 -0.2733 -0.1517 0.1329  117 LYS C O     
9463  C  CB    . LYS D 118 ? 0.6844 0.6287 0.3757 -0.2527 -0.1362 0.1155  117 LYS C CB    
9464  C  CG    . LYS D 118 ? 0.6603 0.6094 0.3594 -0.2417 -0.1270 0.1056  117 LYS C CG    
9465  C  CD    . LYS D 118 ? 0.6821 0.6349 0.3919 -0.2370 -0.1356 0.1078  117 LYS C CD    
9466  C  CE    . LYS D 118 ? 0.6863 0.6438 0.3998 -0.2295 -0.1258 0.0968  117 LYS C CE    
9467  N  NZ    . LYS D 118 ? 0.7045 0.6663 0.4288 -0.2257 -0.1349 0.0993  117 LYS C NZ    
9481  N  N     . CYS D 119 ? 0.6861 0.6197 0.3505 -0.2752 -0.1332 0.1233  118 CYS C N     
9482  C  CA    . CYS D 119 ? 0.7039 0.6331 0.3548 -0.2900 -0.1400 0.1307  118 CYS C CA    
9483  C  C     . CYS D 119 ? 0.7773 0.7030 0.4421 -0.2865 -0.1574 0.1444  118 CYS C C     
9484  O  O     . CYS D 119 ? 0.7840 0.7057 0.4395 -0.2982 -0.1650 0.1521  118 CYS C O     
9485  C  CB    . CYS D 119 ? 0.7767 0.7047 0.4144 -0.2970 -0.1286 0.1253  118 CYS C CB    
9486  S  SG    . CYS D 119 ? 0.9110 0.8380 0.5649 -0.2841 -0.1285 0.1281  118 CYS C SG    
9492  N  N     . ASP D 120 ? 0.7561 0.6833 0.4436 -0.2709 -0.1639 0.1475  119 ASP C N     
9493  C  CA    . ASP D 120 ? 0.7772 0.7011 0.4805 -0.2666 -0.1801 0.1596  119 ASP C CA    
9494  C  C     . ASP D 120 ? 0.8246 0.7488 0.5288 -0.2716 -0.1914 0.1660  119 ASP C C     
9495  O  O     . ASP D 120 ? 0.7893 0.7100 0.5028 -0.2721 -0.2052 0.1768  119 ASP C O     
9496  C  CB    . ASP D 120 ? 0.7742 0.6995 0.5031 -0.2478 -0.1828 0.1599  119 ASP C CB    
9497  C  CG    . ASP D 120 ? 0.7583 0.6896 0.4963 -0.2376 -0.1787 0.1530  119 ASP C CG    
9498  O  OD1   . ASP D 120 ? 0.7268 0.6614 0.4579 -0.2358 -0.1655 0.1427  119 ASP C OD1   
9499  O  OD2   . ASP D 120 ? 0.7540 0.6870 0.5058 -0.2325 -0.1887 0.1576  119 ASP C OD2   
9504  N  N     . LEU D 121 ? 0.8011 0.7293 0.4966 -0.2752 -0.1860 0.1598  120 LEU C N     
9505  C  CA    . LEU D 121 ? 0.8538 0.7832 0.5528 -0.2779 -0.1967 0.1656  120 LEU C CA    
9506  C  C     . LEU D 121 ? 0.9414 0.8665 0.6232 -0.2957 -0.2040 0.1733  120 LEU C C     
9507  O  O     . LEU D 121 ? 0.9531 0.8762 0.6133 -0.3086 -0.1959 0.1693  120 LEU C O     
9508  C  CB    . LEU D 121 ? 0.8780 0.8129 0.5722 -0.2769 -0.1882 0.1560  120 LEU C CB    
9509  C  CG    . LEU D 121 ? 0.8295 0.7694 0.5423 -0.2594 -0.1830 0.1493  120 LEU C CG    
9510  C  CD1   . LEU D 121 ? 0.7976 0.7425 0.5036 -0.2600 -0.1742 0.1395  120 LEU C CD1   
9511  C  CD2   . LEU D 121 ? 0.8171 0.7581 0.5562 -0.2465 -0.1964 0.1574  120 LEU C CD2   
9523  N  N     . PRO D 122 ? 1.0069 0.9303 0.6979 -0.2969 -0.2195 0.1845  121 PRO C N     
9524  C  CA    . PRO D 122 ? 1.0481 0.9674 0.7216 -0.3149 -0.2272 0.1924  121 PRO C CA    
9525  C  C     . PRO D 122 ? 1.0643 0.9859 0.7179 -0.3272 -0.2217 0.1870  121 PRO C C     
9526  O  O     . PRO D 122 ? 1.1258 1.0443 0.7569 -0.3441 -0.2201 0.1877  121 PRO C O     
9527  C  CB    . PRO D 122 ? 1.0729 0.9906 0.7658 -0.3103 -0.2452 0.2053  121 PRO C CB    
9528  C  CG    . PRO D 122 ? 1.0291 0.9523 0.7465 -0.2918 -0.2452 0.2017  121 PRO C CG    
9529  C  CD    . PRO D 122 ? 0.9748 0.9004 0.6931 -0.2823 -0.2303 0.1901  121 PRO C CD    
9537  N  N     . SER D 123 ? 1.0663 0.9933 0.7277 -0.3195 -0.2190 0.1817  122 SER C N     
9538  C  CA    . SER D 123 ? 1.0948 1.0239 0.7370 -0.3301 -0.2108 0.1740  122 SER C CA    
9539  C  C     . SER D 123 ? 1.1010 1.0295 0.7265 -0.3345 -0.1932 0.1618  122 SER C C     
9540  O  O     . SER D 123 ? 1.0802 1.0093 0.7141 -0.3242 -0.1859 0.1570  122 SER C O     
9541  C  CB    . SER D 123 ? 1.1020 1.0372 0.7572 -0.3196 -0.2104 0.1697  122 SER C CB    
9542  O  OG    . SER D 123 ? 1.1614 1.1001 0.8295 -0.3043 -0.2007 0.1608  122 SER C OG    
9548  N  N     . ARG D 124 ? 1.0251 0.9523 0.6270 -0.3504 -0.1864 0.1569  123 ARG C N     
9549  C  CA    . ARG D 124 ? 0.9444 0.8718 0.5314 -0.3545 -0.1684 0.1434  123 ARG C CA    
9550  C  C     . ARG D 124 ? 0.9079 0.8354 0.4754 -0.3682 -0.1627 0.1373  123 ARG C C     
9551  O  O     . ARG D 124 ? 0.8443 0.7696 0.4019 -0.3806 -0.1728 0.1453  123 ARG C O     
9552  C  CB    . ARG D 124 ? 0.9274 0.8507 0.5041 -0.3619 -0.1650 0.1444  123 ARG C CB    
9553  C  CG    . ARG D 124 ? 0.9344 0.8580 0.4953 -0.3676 -0.1462 0.1303  123 ARG C CG    
9554  C  CD    . ARG D 124 ? 0.8773 0.7972 0.4267 -0.3769 -0.1442 0.1321  123 ARG C CD    
9555  N  NE    . ARG D 124 ? 0.8864 0.8066 0.4500 -0.3647 -0.1431 0.1332  123 ARG C NE    
9556  C  CZ    . ARG D 124 ? 0.8739 0.7962 0.4385 -0.3585 -0.1283 0.1225  123 ARG C CZ    
9557  N  NH1   . ARG D 124 ? 0.8405 0.7649 0.3959 -0.3608 -0.1129 0.1090  123 ARG C NH1   
9558  N  NH2   . ARG D 124 ? 0.8143 0.7361 0.3894 -0.3501 -0.1289 0.1253  123 ARG C NH2   
9572  N  N     . THR D 125 ? 0.8227 0.7525 0.3856 -0.3657 -0.1471 0.1235  124 THR C N     
9573  C  CA    . THR D 125 ? 0.8745 0.8039 0.4189 -0.3785 -0.1397 0.1159  124 THR C CA    
9574  C  C     . THR D 125 ? 0.8916 0.8191 0.4193 -0.3865 -0.1215 0.1025  124 THR C C     
9575  O  O     . THR D 125 ? 0.8842 0.8093 0.3923 -0.4018 -0.1163 0.0979  124 THR C O     
9576  C  CB    . THR D 125 ? 0.8870 0.8207 0.4414 -0.3694 -0.1381 0.1108  124 THR C CB    
9577  O  OG1   . THR D 125 ? 0.8215 0.7581 0.3882 -0.3547 -0.1264 0.1008  124 THR C OG1   
9578  C  CG2   . THR D 125 ? 0.8696 0.8059 0.4414 -0.3618 -0.1561 0.1236  124 THR C CG2   
9586  N  N     . VAL D 126 ? 0.8530 0.7813 0.3883 -0.3769 -0.1121 0.0965  125 VAL C N     
9587  C  CA    . VAL D 126 ? 0.8658 0.7929 0.3893 -0.3820 -0.0943 0.0835  125 VAL C CA    
9588  C  C     . VAL D 126 ? 0.8302 0.7547 0.3479 -0.3881 -0.0973 0.0894  125 VAL C C     
9589  O  O     . VAL D 126 ? 0.8450 0.7705 0.3769 -0.3767 -0.1003 0.0936  125 VAL C O     
9590  C  CB    . VAL D 126 ? 0.8250 0.7555 0.3629 -0.3659 -0.0816 0.0726  125 VAL C CB    
9591  C  CG1   . VAL D 126 ? 0.8616 0.7910 0.3889 -0.3708 -0.0625 0.0584  125 VAL C CG1   
9592  C  CG2   . VAL D 126 ? 0.8035 0.7368 0.3500 -0.3583 -0.0815 0.0689  125 VAL C CG2   
9602  N  N     . ASP D 127 ? 0.8497 0.7706 0.3465 -0.4061 -0.0967 0.0898  126 ASP C N     
9603  C  CA    . ASP D 127 ? 0.8752 0.7936 0.3654 -0.4128 -0.0994 0.0952  126 ASP C CA    
9604  C  C     . ASP D 127 ? 0.8482 0.7683 0.3431 -0.4048 -0.0844 0.0849  126 ASP C C     
9605  O  O     . ASP D 127 ? 0.8445 0.7662 0.3381 -0.4021 -0.0685 0.0711  126 ASP C O     
9606  C  CB    . ASP D 127 ? 0.8785 0.7930 0.3433 -0.4347 -0.0990 0.0955  126 ASP C CB    
9607  C  CG    . ASP D 127 ? 0.8991 0.8116 0.3567 -0.4449 -0.1136 0.1058  126 ASP C CG    
9608  O  OD1   . ASP D 127 ? 0.9009 0.8140 0.3730 -0.4372 -0.1291 0.1181  126 ASP C OD1   
9609  O  OD2   . ASP D 127 ? 0.9507 0.8609 0.3878 -0.4614 -0.1098 0.1020  126 ASP C OD2   
9614  N  N     . THR D 128 ? 0.8527 0.7722 0.3538 -0.4011 -0.0896 0.0920  127 THR C N     
9615  C  CA    . THR D 128 ? 0.8353 0.7561 0.3380 -0.3965 -0.0762 0.0837  127 THR C CA    
9616  C  C     . THR D 128 ? 0.8680 0.7882 0.3524 -0.4086 -0.0595 0.0702  127 THR C C     
9617  O  O     . THR D 128 ? 0.8579 0.7805 0.3469 -0.4017 -0.0435 0.0577  127 THR C O     
9618  C  CB    . THR D 128 ? 0.8487 0.7675 0.3527 -0.3981 -0.0855 0.0944  127 THR C CB    
9619  O  OG1   . THR D 128 ? 0.8742 0.7928 0.3960 -0.3871 -0.1015 0.1070  127 THR C OG1   
9620  C  CG2   . THR D 128 ? 0.8224 0.7433 0.3309 -0.3912 -0.0723 0.0868  127 THR C CG2   
9628  N  N     . LYS D 129 ? 0.8621 0.7789 0.3263 -0.4270 -0.0630 0.0728  128 LYS C N     
9629  C  CA    . LYS D 129 ? 0.8847 0.8003 0.3306 -0.4400 -0.0476 0.0603  128 LYS C CA    
9630  C  C     . LYS D 129 ? 0.9401 0.8571 0.3880 -0.4359 -0.0341 0.0464  128 LYS C C     
9631  O  O     . LYS D 129 ? 0.9486 0.8661 0.3924 -0.4373 -0.0168 0.0327  128 LYS C O     
9632  C  CB    . LYS D 129 ? 0.9231 0.8345 0.3465 -0.4610 -0.0557 0.0667  128 LYS C CB    
9633  C  CG    . LYS D 129 ? 0.9506 0.8601 0.3533 -0.4764 -0.0408 0.0540  128 LYS C CG    
9634  C  CD    . LYS D 129 ? 0.9689 0.8773 0.3601 -0.4856 -0.0355 0.0530  128 LYS C CD    
9635  C  CE    . LYS D 129 ? 0.9974 0.9040 0.3684 -0.5010 -0.0198 0.0395  128 LYS C CE    
9636  N  NZ    . LYS D 129 ? 1.0528 0.9563 0.4089 -0.5143 -0.0236 0.0395  128 LYS C NZ    
9650  N  N     . GLN D 130 ? 0.8877 0.8052 0.3424 -0.4311 -0.0416 0.0498  129 GLN C N     
9651  C  CA    . GLN D 130 ? 0.9061 0.8247 0.3635 -0.4268 -0.0292 0.0370  129 GLN C CA    
9652  C  C     . GLN D 130 ? 0.8454 0.7672 0.3193 -0.4106 -0.0157 0.0270  129 GLN C C     
9653  O  O     . GLN D 130 ? 0.8317 0.7533 0.3029 -0.4114 0.0012  0.0128  129 GLN C O     
9654  C  CB    . GLN D 130 ? 0.8767 0.7961 0.3416 -0.4219 -0.0403 0.0431  129 GLN C CB    
9655  C  CG    . GLN D 130 ? 0.9695 0.8861 0.4190 -0.4375 -0.0529 0.0521  129 GLN C CG    
9656  C  CD    . GLN D 130 ? 0.9645 0.8830 0.4255 -0.4297 -0.0652 0.0598  129 GLN C CD    
9657  O  OE1   . GLN D 130 ? 0.9556 0.8738 0.4200 -0.4305 -0.0824 0.0742  129 GLN C OE1   
9658  N  NE2   . GLN D 130 ? 0.9748 0.8952 0.4431 -0.4216 -0.0565 0.0501  129 GLN C NE2   
9667  N  N     . ALA D 131 ? 0.8698 0.7943 0.3618 -0.3955 -0.0232 0.0343  130 ALA C N     
9668  C  CA    . ALA D 131 ? 0.8388 0.7665 0.3471 -0.3798 -0.0115 0.0262  130 ALA C CA    
9669  C  C     . ALA D 131 ? 0.8634 0.7913 0.3669 -0.3833 0.0009  0.0194  130 ALA C C     
9670  O  O     . ALA D 131 ? 0.8352 0.7650 0.3463 -0.3758 0.0166  0.0074  130 ALA C O     
9671  C  CB    . ALA D 131 ? 0.8202 0.7505 0.3476 -0.3645 -0.0234 0.0367  130 ALA C CB    
9677  N  N     . GLN D 132 ? 0.9136 0.8396 0.4055 -0.3942 -0.0059 0.0272  131 GLN C N     
9678  C  CA    . GLN D 132 ? 0.8878 0.8141 0.3733 -0.3992 0.0065  0.0202  131 GLN C CA    
9679  C  C     . GLN D 132 ? 0.8378 0.7628 0.3121 -0.4081 0.0233  0.0050  131 GLN C C     
9680  O  O     . GLN D 132 ? 0.8934 0.8205 0.3753 -0.4016 0.0395  -0.0069 131 GLN C O     
9681  C  CB    . GLN D 132 ? 0.8849 0.8090 0.3573 -0.4117 -0.0041 0.0312  131 GLN C CB    
9682  C  CG    . GLN D 132 ? 0.8612 0.7861 0.3462 -0.4025 -0.0183 0.0450  131 GLN C CG    
9683  C  CD    . GLN D 132 ? 0.8968 0.8185 0.3684 -0.4159 -0.0298 0.0564  131 GLN C CD    
9684  O  OE1   . GLN D 132 ? 0.9523 0.8706 0.4070 -0.4311 -0.0361 0.0599  131 GLN C OE1   
9685  N  NE2   . GLN D 132 ? 0.9131 0.8355 0.3920 -0.4106 -0.0328 0.0624  131 GLN C NE2   
9694  N  N     . ASP D 133 ? 0.9289 0.8505 0.3862 -0.4229 0.0196  0.0053  132 ASP C N     
9695  C  CA    . ASP D 133 ? 0.8814 0.8008 0.3265 -0.4331 0.0351  -0.0089 132 ASP C CA    
9696  C  C     . ASP D 133 ? 0.9520 0.8728 0.4115 -0.4205 0.0484  -0.0215 132 ASP C C     
9697  O  O     . ASP D 133 ? 0.9633 0.8833 0.4206 -0.4232 0.0654  -0.0353 132 ASP C O     
9698  C  CB    . ASP D 133 ? 0.9586 0.8740 0.3842 -0.4502 0.0267  -0.0048 132 ASP C CB    
9699  C  CG    . ASP D 133 ? 0.9339 0.8470 0.3423 -0.4654 0.0164  0.0055  132 ASP C CG    
9700  O  OD1   . ASP D 133 ? 0.9365 0.8507 0.3443 -0.4659 0.0210  0.0050  132 ASP C OD1   
9701  O  OD2   . ASP D 133 ? 1.0260 0.9364 0.4226 -0.4765 0.0034  0.0146  132 ASP C OD2   
9706  N  N     . LEU D 134 ? 0.8740 0.7967 0.3490 -0.4070 0.0412  -0.0172 133 LEU C N     
9707  C  CA    . LEU D 134 ? 0.8706 0.7944 0.3599 -0.3948 0.0531  -0.0286 133 LEU C CA    
9708  C  C     . LEU D 134 ? 0.8894 0.8168 0.3961 -0.3805 0.0640  -0.0342 133 LEU C C     
9709  O  O     . LEU D 134 ? 0.9397 0.8672 0.4533 -0.3760 0.0803  -0.0475 133 LEU C O     
9710  C  CB    . LEU D 134 ? 0.8837 0.8086 0.3831 -0.3857 0.0417  -0.0220 133 LEU C CB    
9711  C  CG    . LEU D 134 ? 0.8838 0.8097 0.3986 -0.3725 0.0522  -0.0324 133 LEU C CG    
9712  C  CD1   . LEU D 134 ? 0.9007 0.8228 0.4058 -0.3818 0.0642  -0.0448 133 LEU C CD1   
9713  C  CD2   . LEU D 134 ? 0.8541 0.7822 0.3817 -0.3608 0.0400  -0.0244 133 LEU C CD2   
9725  N  N     . ALA D 135 ? 0.7731 0.7033 0.2876 -0.3733 0.0553  -0.0242 134 ALA C N     
9726  C  CA    . ALA D 135 ? 0.8209 0.7549 0.3513 -0.3607 0.0653  -0.0286 134 ALA C CA    
9727  C  C     . ALA D 135 ? 0.8968 0.8304 0.4197 -0.3689 0.0807  -0.0388 134 ALA C C     
9728  O  O     . ALA D 135 ? 0.8834 0.8190 0.4187 -0.3607 0.0959  -0.0498 134 ALA C O     
9729  C  CB    . ALA D 135 ? 0.8115 0.7479 0.3492 -0.3539 0.0523  -0.0150 134 ALA C CB    
9735  N  N     . ARG D 136 ? 0.8023 0.7335 0.3055 -0.3854 0.0769  -0.0353 135 ARG C N     
9736  C  CA    . ARG D 136 ? 0.9270 0.8578 0.4216 -0.3946 0.0917  -0.0453 135 ARG C CA    
9737  C  C     . ARG D 136 ? 0.9650 0.8946 0.4639 -0.3932 0.1088  -0.0613 135 ARG C C     
9738  O  O     . ARG D 136 ? 1.0035 0.9355 0.5144 -0.3861 0.1239  -0.0712 135 ARG C O     
9739  C  CB    . ARG D 136 ? 0.9397 0.8668 0.4092 -0.4151 0.0851  -0.0404 135 ARG C CB    
9740  C  CG    . ARG D 136 ? 1.0177 0.9453 0.4778 -0.4249 0.0977  -0.0474 135 ARG C CG    
9741  C  CD    . ARG D 136 ? 1.0860 1.0100 0.5210 -0.4450 0.0887  -0.0402 135 ARG C CD    
9742  N  NE    . ARG D 136 ? 1.1245 1.0494 0.5602 -0.4433 0.0711  -0.0239 135 ARG C NE    
9743  C  CZ    . ARG D 136 ? 1.1160 1.0382 0.5443 -0.4486 0.0531  -0.0114 135 ARG C CZ    
9744  N  NH1   . ARG D 136 ? 1.0444 0.9631 0.4611 -0.4581 0.0499  -0.0128 135 ARG C NH1   
9745  N  NH2   . ARG D 136 ? 1.0672 0.9901 0.5009 -0.4441 0.0381  0.0028  135 ARG C NH2   
9759  N  N     . SER D 137 ? 0.9061 0.8317 0.3962 -0.3998 0.1064  -0.0638 136 SER C N     
9760  C  CA    . SER D 137 ? 0.8716 0.7948 0.3637 -0.4005 0.1221  -0.0788 136 SER C CA    
9761  C  C     . SER D 137 ? 0.9433 0.8695 0.4608 -0.3816 0.1331  -0.0865 136 SER C C     
9762  O  O     . SER D 137 ? 0.9466 0.8726 0.4705 -0.3803 0.1499  -0.0993 136 SER C O     
9763  C  CB    . SER D 137 ? 0.9627 0.8818 0.4449 -0.4076 0.1154  -0.0780 136 SER C CB    
9764  O  OG    . SER D 137 ? 0.9166 0.8375 0.4111 -0.3953 0.1035  -0.0697 136 SER C OG    
9770  N  N     . TYR D 138 ? 0.8697 0.7989 0.4025 -0.3670 0.1240  -0.0788 137 TYR C N     
9771  C  CA    . TYR D 138 ? 0.8444 0.7764 0.4011 -0.3493 0.1334  -0.0853 137 TYR C CA    
9772  C  C     . TYR D 138 ? 0.8942 0.8312 0.4645 -0.3409 0.1414  -0.0866 137 TYR C C     
9773  O  O     . TYR D 138 ? 0.9023 0.8416 0.4928 -0.3275 0.1517  -0.0935 137 TYR C O     
9774  C  CB    . TYR D 138 ? 0.9246 0.8584 0.4935 -0.3364 0.1214  -0.0769 137 TYR C CB    
9775  C  CG    . TYR D 138 ? 0.9358 0.8662 0.4954 -0.3416 0.1113  -0.0734 137 TYR C CG    
9776  C  CD1   . TYR D 138 ? 0.8771 0.8028 0.4256 -0.3522 0.1180  -0.0821 137 TYR C CD1   
9777  C  CD2   . TYR D 138 ? 0.9145 0.8467 0.4786 -0.3348 0.0957  -0.0616 137 TYR C CD2   
9778  C  CE1   . TYR D 138 ? 0.9364 0.8596 0.4776 -0.3566 0.1088  -0.0785 137 TYR C CE1   
9779  C  CE2   . TYR D 138 ? 0.9363 0.8662 0.4939 -0.3387 0.0866  -0.0582 137 TYR C CE2   
9780  C  CZ    . TYR D 138 ? 0.9542 0.8799 0.5006 -0.3494 0.0931  -0.0665 137 TYR C CZ    
9781  O  OH    . TYR D 138 ? 1.0562 0.9803 0.5969 -0.3531 0.0836  -0.0623 137 TYR C OH    
9791  N  N     . GLY D 139 ? 0.8669 0.8057 0.4278 -0.3479 0.1363  -0.0794 138 GLY C N     
9792  C  CA    . GLY D 139 ? 0.8879 0.8319 0.4620 -0.3400 0.1432  -0.0797 138 GLY C CA    
9793  C  C     . GLY D 139 ? 0.9027 0.8511 0.4938 -0.3249 0.1346  -0.0699 138 GLY C C     
9794  O  O     . GLY D 139 ? 0.8434 0.7967 0.4530 -0.3136 0.1433  -0.0730 138 GLY C O     
9798  N  N     . ILE D 140 ? 0.8468 0.7941 0.4328 -0.3245 0.1176  -0.0578 139 ILE C N     
9799  C  CA    . ILE D 140 ? 0.7885 0.7395 0.3902 -0.3105 0.1091  -0.0485 139 ILE C CA    
9800  C  C     . ILE D 140 ? 0.7708 0.7208 0.3613 -0.3167 0.0914  -0.0336 139 ILE C C     
9801  O  O     . ILE D 140 ? 0.8245 0.7706 0.3962 -0.3304 0.0831  -0.0296 139 ILE C O     
9802  C  CB    . ILE D 140 ? 0.7804 0.7312 0.3950 -0.2984 0.1068  -0.0497 139 ILE C CB    
9803  C  CG1   . ILE D 140 ? 0.8206 0.7671 0.4206 -0.3066 0.0939  -0.0444 139 ILE C CG1   
9804  C  CG2   . ILE D 140 ? 0.7435 0.6947 0.3712 -0.2916 0.1240  -0.0642 139 ILE C CG2   
9805  C  CD1   . ILE D 140 ? 0.7064 0.6529 0.3178 -0.2953 0.0894  -0.0439 139 ILE C CD1   
9817  N  N     . PRO D 141 ? 0.6620 0.6152 0.2646 -0.3069 0.0849  -0.0249 140 PRO C N     
9818  C  CA    . PRO D 141 ? 0.7424 0.6940 0.3373 -0.3113 0.0675  -0.0101 140 PRO C CA    
9819  C  C     . PRO D 141 ? 0.7554 0.7038 0.3453 -0.3123 0.0523  -0.0026 140 PRO C C     
9820  O  O     . PRO D 141 ? 0.7775 0.7261 0.3752 -0.3047 0.0537  -0.0067 140 PRO C O     
9821  C  CB    . PRO D 141 ? 0.7909 0.7467 0.4040 -0.2980 0.0662  -0.0045 140 PRO C CB    
9822  C  CG    . PRO D 141 ? 0.7425 0.7028 0.3686 -0.2915 0.0850  -0.0165 140 PRO C CG    
9823  C  CD    . PRO D 141 ? 0.7393 0.6977 0.3637 -0.2922 0.0942  -0.0282 140 PRO C CD    
9831  N  N     . PHE D 142 ? 0.7995 0.7449 0.3772 -0.3218 0.0372  0.0091  141 PHE C N     
9832  C  CA    . PHE D 142 ? 0.7779 0.7208 0.3534 -0.3224 0.0204  0.0190  141 PHE C CA    
9833  C  C     . PHE D 142 ? 0.7825 0.7248 0.3639 -0.3185 0.0047  0.0337  141 PHE C C     
9834  O  O     . PHE D 142 ? 0.7297 0.6708 0.3036 -0.3262 0.0013  0.0392  141 PHE C O     
9835  C  CB    . PHE D 142 ? 0.7834 0.7223 0.3387 -0.3391 0.0158  0.0193  141 PHE C CB    
9836  C  CG    . PHE D 142 ? 0.8181 0.7546 0.3713 -0.3413 -0.0034 0.0320  141 PHE C CG    
9837  C  CD1   . PHE D 142 ? 0.7992 0.7368 0.3638 -0.3311 -0.0086 0.0333  141 PHE C CD1   
9838  C  CD2   . PHE D 142 ? 0.8346 0.7679 0.3752 -0.3536 -0.0161 0.0428  141 PHE C CD2   
9839  C  CE1   . PHE D 142 ? 0.8064 0.7424 0.3712 -0.3325 -0.0261 0.0451  141 PHE C CE1   
9840  C  CE2   . PHE D 142 ? 0.8506 0.7820 0.3918 -0.3551 -0.0338 0.0548  141 PHE C CE2   
9841  C  CZ    . PHE D 142 ? 0.8415 0.7743 0.3951 -0.3443 -0.0387 0.0560  141 PHE C CZ    
9851  N  N     . ILE D 143 ? 0.7521 0.6951 0.3471 -0.3066 -0.0048 0.0399  142 ILE C N     
9852  C  CA    . ILE D 143 ? 0.7378 0.6798 0.3421 -0.3005 -0.0198 0.0534  142 ILE C CA    
9853  C  C     . ILE D 143 ? 0.7585 0.6987 0.3660 -0.2985 -0.0354 0.0617  142 ILE C C     
9854  O  O     . ILE D 143 ? 0.6914 0.6334 0.3060 -0.2909 -0.0332 0.0572  142 ILE C O     
9855  C  CB    . ILE D 143 ? 0.7899 0.7352 0.4127 -0.2852 -0.0147 0.0525  142 ILE C CB    
9856  C  CG1   . ILE D 143 ? 0.8045 0.7527 0.4274 -0.2860 0.0021  0.0435  142 ILE C CG1   
9857  C  CG2   . ILE D 143 ? 0.7797 0.7229 0.4116 -0.2800 -0.0304 0.0664  142 ILE C CG2   
9858  C  CD1   . ILE D 143 ? 0.8059 0.7568 0.4288 -0.2849 0.0196  0.0284  142 ILE C CD1   
9870  N  N     . GLU D 144 ? 0.8192 0.7559 0.4224 -0.3051 -0.0511 0.0739  143 GLU C N     
9871  C  CA    . GLU D 144 ? 0.7832 0.7187 0.3943 -0.3010 -0.0672 0.0836  143 GLU C CA    
9872  C  C     . GLU D 144 ? 0.7658 0.7017 0.3969 -0.2859 -0.0745 0.0905  143 GLU C C     
9873  O  O     . GLU D 144 ? 0.7556 0.6905 0.3904 -0.2842 -0.0751 0.0944  143 GLU C O     
9874  C  CB    . GLU D 144 ? 0.8221 0.7534 0.4222 -0.3142 -0.0811 0.0941  143 GLU C CB    
9875  C  CG    . GLU D 144 ? 0.8561 0.7867 0.4423 -0.3256 -0.0813 0.0912  143 GLU C CG    
9876  C  CD    . GLU D 144 ? 0.8984 0.8250 0.4686 -0.3422 -0.0905 0.0991  143 GLU C CD    
9877  O  OE1   . GLU D 144 ? 0.9624 0.8866 0.5311 -0.3457 -0.0955 0.1060  143 GLU C OE1   
9878  O  OE2   . GLU D 144 ? 0.9253 0.8509 0.4840 -0.3524 -0.0927 0.0986  143 GLU C OE2   
9885  N  N     . THR D 145 ? 0.6671 0.6046 0.3114 -0.2749 -0.0799 0.0917  144 THR C N     
9886  C  CA    . THR D 145 ? 0.7244 0.6622 0.3882 -0.2602 -0.0866 0.0974  144 THR C CA    
9887  C  C     . THR D 145 ? 0.6919 0.6285 0.3673 -0.2553 -0.1036 0.1073  144 THR C C     
9888  O  O     . THR D 145 ? 0.6985 0.6349 0.3681 -0.2617 -0.1092 0.1089  144 THR C O     
9889  C  CB    . THR D 145 ? 0.7105 0.6525 0.3835 -0.2482 -0.0746 0.0879  144 THR C CB    
9890  O  OG1   . THR D 145 ? 0.6443 0.5885 0.3161 -0.2474 -0.0732 0.0827  144 THR C OG1   
9891  C  CG2   . THR D 145 ? 0.7368 0.6806 0.4023 -0.2514 -0.0569 0.0778  144 THR C CG2   
9899  N  N     . SER D 146 ? 0.7211 0.6568 0.4145 -0.2433 -0.1116 0.1136  145 SER C N     
9900  C  CA    . SER D 146 ? 0.7084 0.6442 0.4182 -0.2342 -0.1249 0.1202  145 SER C CA    
9901  C  C     . SER D 146 ? 0.6966 0.6342 0.4248 -0.2180 -0.1234 0.1186  145 SER C C     
9902  O  O     . SER D 146 ? 0.7002 0.6349 0.4363 -0.2136 -0.1259 0.1229  145 SER C O     
9903  C  CB    . SER D 146 ? 0.7306 0.6618 0.4456 -0.2377 -0.1408 0.1326  145 SER C CB    
9904  O  OG    . SER D 146 ? 0.7095 0.6414 0.4458 -0.2253 -0.1517 0.1375  145 SER C OG    
9910  N  N     . ALA D 147 ? 0.6355 0.5775 0.3701 -0.2097 -0.1192 0.1122  146 ALA C N     
9911  C  CA    . ALA D 147 ? 0.5866 0.5302 0.3404 -0.1942 -0.1205 0.1119  146 ALA C CA    
9912  C  C     . ALA D 147 ? 0.6653 0.6064 0.4383 -0.1865 -0.1363 0.1217  146 ALA C C     
9913  O  O     . ALA D 147 ? 0.6679 0.6078 0.4563 -0.1756 -0.1386 0.1234  146 ALA C O     
9914  C  CB    . ALA D 147 ? 0.5887 0.5377 0.3454 -0.1876 -0.1144 0.1035  146 ALA C CB    
9920  N  N     . LYS D 148 ? 0.6510 0.5909 0.4240 -0.1920 -0.1468 0.1279  147 LYS C N     
9921  C  CA    . LYS D 148 ? 0.6221 0.5598 0.4152 -0.1845 -0.1611 0.1366  147 LYS C CA    
9922  C  C     . LYS D 148 ? 0.6788 0.6103 0.4756 -0.1847 -0.1651 0.1427  147 LYS C C     
9923  O  O     . LYS D 148 ? 0.6477 0.5776 0.4635 -0.1729 -0.1691 0.1446  147 LYS C O     
9924  C  CB    . LYS D 148 ? 0.6767 0.6142 0.4673 -0.1921 -0.1709 0.1424  147 LYS C CB    
9925  C  CG    . LYS D 148 ? 0.6296 0.5660 0.4434 -0.1832 -0.1850 0.1502  147 LYS C CG    
9926  C  CD    . LYS D 148 ? 0.7341 0.6704 0.5435 -0.1924 -0.1943 0.1565  147 LYS C CD    
9927  C  CE    . LYS D 148 ? 0.7248 0.6581 0.5548 -0.1869 -0.2089 0.1660  147 LYS C CE    
9928  N  NZ    . LYS D 148 ? 0.7141 0.6520 0.5539 -0.1849 -0.2164 0.1682  147 LYS C NZ    
9942  N  N     . THR D 149 ? 0.6341 0.5622 0.4131 -0.1983 -0.1633 0.1453  148 THR C N     
9943  C  CA    . THR D 149 ? 0.7082 0.6305 0.4886 -0.2001 -0.1666 0.1509  148 THR C CA    
9944  C  C     . THR D 149 ? 0.7240 0.6468 0.4989 -0.1986 -0.1543 0.1450  148 THR C C     
9945  O  O     . THR D 149 ? 0.7181 0.6366 0.4953 -0.1994 -0.1563 0.1491  148 THR C O     
9946  C  CB    . THR D 149 ? 0.7243 0.6429 0.4883 -0.2162 -0.1715 0.1571  148 THR C CB    
9947  O  OG1   . THR D 149 ? 0.7457 0.6668 0.4870 -0.2277 -0.1592 0.1502  148 THR C OG1   
9948  C  CG2   . THR D 149 ? 0.6676 0.5857 0.4357 -0.2193 -0.1838 0.1637  148 THR C CG2   
9956  N  N     . ARG D 150 ? 0.6988 0.6268 0.4665 -0.1971 -0.1416 0.1356  149 ARG C N     
9957  C  CA    . ARG D 150 ? 0.7100 0.6394 0.4715 -0.1966 -0.1281 0.1292  149 ARG C CA    
9958  C  C     . ARG D 150 ? 0.7756 0.7040 0.5168 -0.2114 -0.1207 0.1279  149 ARG C C     
9959  O  O     . ARG D 150 ? 0.7100 0.6388 0.4483 -0.2118 -0.1114 0.1247  149 ARG C O     
9960  C  CB    . ARG D 150 ? 0.6939 0.6205 0.4728 -0.1852 -0.1312 0.1322  149 ARG C CB    
9961  C  CG    . ARG D 150 ? 0.7986 0.7265 0.5748 -0.1833 -0.1182 0.1269  149 ARG C CG    
9962  C  CD    . ARG D 150 ? 0.7742 0.7080 0.5401 -0.1846 -0.1031 0.1168  149 ARG C CD    
9963  N  NE    . ARG D 150 ? 0.7464 0.6823 0.5159 -0.1793 -0.0911 0.1117  149 ARG C NE    
9964  C  CZ    . ARG D 150 ? 0.7425 0.6791 0.5327 -0.1653 -0.0918 0.1101  149 ARG C CZ    
9965  N  NH1   . ARG D 150 ? 0.7298 0.6638 0.5353 -0.1560 -0.1047 0.1152  149 ARG C NH1   
9966  N  NH2   . ARG D 150 ? 0.7071 0.6483 0.5059 -0.1595 -0.0784 0.1016  149 ARG C NH2   
9980  N  N     . GLN D 151 ? 0.7569 0.6846 0.4841 -0.2238 -0.1240 0.1297  150 GLN C N     
9981  C  CA    . GLN D 151 ? 0.7875 0.7146 0.4950 -0.2382 -0.1164 0.1274  150 GLN C CA    
9982  C  C     . GLN D 151 ? 0.7304 0.6625 0.4258 -0.2415 -0.0990 0.1150  150 GLN C C     
9983  O  O     . GLN D 151 ? 0.7395 0.6743 0.4324 -0.2408 -0.0961 0.1097  150 GLN C O     
9984  C  CB    . GLN D 151 ? 0.7795 0.7037 0.4757 -0.2511 -0.1262 0.1337  150 GLN C CB    
9985  C  CG    . GLN D 151 ? 0.7905 0.7145 0.4645 -0.2672 -0.1182 0.1303  150 GLN C CG    
9986  C  CD    . GLN D 151 ? 0.9015 0.8218 0.5642 -0.2805 -0.1294 0.1380  150 GLN C CD    
9987  O  OE1   . GLN D 151 ? 0.9589 0.8747 0.6294 -0.2803 -0.1433 0.1487  150 GLN C OE1   
9988  N  NE2   . GLN D 151 ? 0.9076 0.8294 0.5521 -0.2927 -0.1230 0.1324  150 GLN C NE2   
9997  N  N     . GLY D 152 ? 0.7679 0.7012 0.4567 -0.2452 -0.0872 0.1101  151 GLY C N     
9998  C  CA    . GLY D 152 ? 0.7613 0.6988 0.4394 -0.2494 -0.0696 0.0979  151 GLY C CA    
9999  C  C     . GLY D 152 ? 0.6788 0.6208 0.3680 -0.2372 -0.0585 0.0897  151 GLY C C     
10000 O  O     . GLY D 152 ? 0.6278 0.5734 0.3117 -0.2391 -0.0426 0.0790  151 GLY C O     
10004 N  N     . VAL D 153 ? 0.6930 0.6346 0.3982 -0.2246 -0.0659 0.0940  152 VAL C N     
10005 C  CA    . VAL D 153 ? 0.6609 0.6065 0.3751 -0.2139 -0.0561 0.0864  152 VAL C CA    
10006 C  C     . VAL D 153 ? 0.6574 0.6063 0.3732 -0.2130 -0.0398 0.0792  152 VAL C C     
10007 O  O     . VAL D 153 ? 0.6970 0.6497 0.4086 -0.2144 -0.0250 0.0685  152 VAL C O     
10008 C  CB    . VAL D 153 ? 0.7008 0.6452 0.4326 -0.2005 -0.0674 0.0929  152 VAL C CB    
10009 C  CG1   . VAL D 153 ? 0.6437 0.5923 0.3857 -0.1896 -0.0569 0.0853  152 VAL C CG1   
10010 C  CG2   . VAL D 153 ? 0.7371 0.6801 0.4702 -0.2006 -0.0815 0.0979  152 VAL C CG2   
10020 N  N     . ASP D 154 ? 0.6696 0.6169 0.3926 -0.2107 -0.0421 0.0849  153 ASP C N     
10021 C  CA    . ASP D 154 ? 0.6694 0.6208 0.3980 -0.2084 -0.0273 0.0788  153 ASP C CA    
10022 C  C     . ASP D 154 ? 0.6732 0.6278 0.3892 -0.2187 -0.0134 0.0697  153 ASP C C     
10023 O  O     . ASP D 154 ? 0.6052 0.5649 0.3258 -0.2160 0.0023  0.0598  153 ASP C O     
10024 C  CB    . ASP D 154 ? 0.6224 0.5712 0.3597 -0.2063 -0.0334 0.0870  153 ASP C CB    
10025 C  CG    . ASP D 154 ? 0.6686 0.6144 0.4219 -0.1943 -0.0441 0.0938  153 ASP C CG    
10026 O  OD1   . ASP D 154 ? 0.6617 0.6119 0.4304 -0.1819 -0.0397 0.0861  153 ASP C OD1   
10027 O  OD2   . ASP D 154 ? 0.6833 0.6237 0.4413 -0.1934 -0.0568 0.1030  153 ASP C OD2   
10032 N  N     . ASP D 155 ? 0.6844 0.6360 0.3855 -0.2306 -0.0190 0.0729  154 ASP C N     
10033 C  CA    . ASP D 155 ? 0.7179 0.6717 0.4059 -0.2413 -0.0067 0.0646  154 ASP C CA    
10034 C  C     . ASP D 155 ? 0.6955 0.6525 0.3810 -0.2404 0.0054  0.0526  154 ASP C C     
10035 O  O     . ASP D 155 ? 0.6662 0.6274 0.3540 -0.2403 0.0215  0.0423  154 ASP C O     
10036 C  CB    . ASP D 155 ? 0.7215 0.6707 0.3927 -0.2546 -0.0170 0.0709  154 ASP C CB    
10037 C  CG    . ASP D 155 ? 0.7994 0.7503 0.4569 -0.2666 -0.0053 0.0639  154 ASP C CG    
10038 O  OD1   . ASP D 155 ? 0.8227 0.7783 0.4864 -0.2635 0.0098  0.0557  154 ASP C OD1   
10039 O  OD2   . ASP D 155 ? 0.7944 0.7419 0.4357 -0.2791 -0.0113 0.0666  154 ASP C OD2   
10044 N  N     . ALA D 156 ? 0.6912 0.6461 0.3737 -0.2393 -0.0023 0.0536  155 ALA C N     
10045 C  CA    . ALA D 156 ? 0.6455 0.6025 0.3263 -0.2382 0.0080  0.0426  155 ALA C CA    
10046 C  C     . ALA D 156 ? 0.6464 0.6084 0.3422 -0.2277 0.0233  0.0335  155 ALA C C     
10047 O  O     . ALA D 156 ? 0.6164 0.5809 0.3111 -0.2297 0.0382  0.0222  155 ALA C O     
10048 C  CB    . ALA D 156 ? 0.6657 0.6206 0.3471 -0.2347 -0.0042 0.0470  155 ALA C CB    
10054 N  N     . PHE D 157 ? 0.6749 0.6381 0.3859 -0.2162 0.0196  0.0384  156 PHE C N     
10055 C  CA    . PHE D 157 ? 0.6299 0.5981 0.3567 -0.2060 0.0329  0.0304  156 PHE C CA    
10056 C  C     . PHE D 157 ? 0.6348 0.6073 0.3691 -0.2062 0.0451  0.0263  156 PHE C C     
10057 O  O     . PHE D 157 ? 0.5346 0.5117 0.2788 -0.2016 0.0599  0.0161  156 PHE C O     
10058 C  CB    . PHE D 157 ? 0.5813 0.5497 0.3238 -0.1935 0.0246  0.0367  156 PHE C CB    
10059 C  CG    . PHE D 157 ? 0.5841 0.5513 0.3296 -0.1873 0.0172  0.0356  156 PHE C CG    
10060 C  CD1   . PHE D 157 ? 0.5969 0.5673 0.3535 -0.1788 0.0269  0.0254  156 PHE C CD1   
10061 C  CD2   . PHE D 157 ? 0.5833 0.5463 0.3225 -0.1894 0.0003  0.0453  156 PHE C CD2   
10062 C  CE1   . PHE D 157 ? 0.5317 0.5013 0.2915 -0.1734 0.0202  0.0246  156 PHE C CE1   
10063 C  CE2   . PHE D 157 ? 0.6046 0.5675 0.3484 -0.1836 -0.0064 0.0443  156 PHE C CE2   
10064 C  CZ    . PHE D 157 ? 0.4851 0.4514 0.2386 -0.1759 0.0038  0.0339  156 PHE C CZ    
10074 N  N     . TYR D 158 ? 0.6125 0.5837 0.3446 -0.2104 0.0384  0.0346  157 TYR C N     
10075 C  CA    . TYR D 158 ? 0.6408 0.6164 0.3795 -0.2116 0.0493  0.0312  157 TYR C CA    
10076 C  C     . TYR D 158 ? 0.6463 0.6231 0.3738 -0.2209 0.0607  0.0217  157 TYR C C     
10077 O  O     . TYR D 158 ? 0.6120 0.5940 0.3490 -0.2181 0.0759  0.0119  157 TYR C O     
10078 C  CB    . TYR D 158 ? 0.6384 0.6114 0.3756 -0.2152 0.0386  0.0425  157 TYR C CB    
10079 C  CG    . TYR D 158 ? 0.5963 0.5679 0.3474 -0.2058 0.0288  0.0513  157 TYR C CG    
10080 C  CD1   . TYR D 158 ? 0.5922 0.5652 0.3559 -0.1946 0.0290  0.0491  157 TYR C CD1   
10081 C  CD2   . TYR D 158 ? 0.6217 0.5903 0.3748 -0.2074 0.0192  0.0612  157 TYR C CD2   
10082 C  CE1   . TYR D 158 ? 0.5857 0.5578 0.3686 -0.1817 0.0181  0.0541  157 TYR C CE1   
10083 C  CE2   . TYR D 158 ? 0.6200 0.5863 0.3865 -0.1989 0.0100  0.0689  157 TYR C CE2   
10084 C  CZ    . TYR D 158 ? 0.6210 0.5896 0.4050 -0.1840 0.0087  0.0638  157 TYR C CZ    
10085 O  OH    . TYR D 158 ? 0.6307 0.5977 0.4328 -0.1721 -0.0018 0.0683  157 TYR C OH    
10095 N  N     . THR D 159 ? 0.6446 0.6164 0.3526 -0.2320 0.0531  0.0244  158 THR C N     
10096 C  CA    . THR D 159 ? 0.7186 0.6905 0.4142 -0.2417 0.0633  0.0149  158 THR C CA    
10097 C  C     . THR D 159 ? 0.6526 0.6273 0.3573 -0.2349 0.0765  0.0025  158 THR C C     
10098 O  O     . THR D 159 ? 0.6730 0.6504 0.3797 -0.2369 0.0908  -0.0077 158 THR C O     
10099 C  CB    . THR D 159 ? 0.7147 0.6806 0.3893 -0.2537 0.0517  0.0197  158 THR C CB    
10100 O  OG1   . THR D 159 ? 0.7042 0.6675 0.3720 -0.2601 0.0404  0.0308  158 THR C OG1   
10101 C  CG2   . THR D 159 ? 0.6987 0.6639 0.3597 -0.2643 0.0623  0.0091  158 THR C CG2   
10109 N  N     . LEU D 160 ? 0.6868 0.6609 0.3991 -0.2260 0.0722  0.0034  159 LEU C N     
10110 C  CA    . LEU D 160 ? 0.6633 0.6393 0.3847 -0.2195 0.0842  -0.0082 159 LEU C CA    
10111 C  C     . LEU D 160 ? 0.5686 0.5510 0.3115 -0.2095 0.0969  -0.0136 159 LEU C C     
10112 O  O     . LEU D 160 ? 0.6443 0.6288 0.3936 -0.2082 0.1107  -0.0247 159 LEU C O     
10113 C  CB    . LEU D 160 ? 0.6774 0.6510 0.4002 -0.2134 0.0761  -0.0059 159 LEU C CB    
10114 C  CG    . LEU D 160 ? 0.6481 0.6224 0.3787 -0.2075 0.0872  -0.0174 159 LEU C CG    
10115 C  CD1   . LEU D 160 ? 0.6822 0.6543 0.4025 -0.2166 0.0972  -0.0279 159 LEU C CD1   
10116 C  CD2   . LEU D 160 ? 0.6400 0.6115 0.3681 -0.2040 0.0774  -0.0142 159 LEU C CD2   
10128 N  N     . VAL D 161 ? 0.6669 0.6522 0.4226 -0.2022 0.0920  -0.0058 160 VAL C N     
10129 C  CA    . VAL D 161 ? 0.5920 0.5841 0.3686 -0.1942 0.1031  -0.0098 160 VAL C CA    
10130 C  C     . VAL D 161 ? 0.6476 0.6424 0.4213 -0.2017 0.1126  -0.0145 160 VAL C C     
10131 O  O     . VAL D 161 ? 0.6507 0.6508 0.4388 -0.1973 0.1261  -0.0232 160 VAL C O     
10132 C  CB    . VAL D 161 ? 0.5898 0.5840 0.3780 -0.1880 0.0945  0.0006  160 VAL C CB    
10133 C  CG1   . VAL D 161 ? 0.5838 0.5857 0.3919 -0.1829 0.1046  -0.0021 160 VAL C CG1   
10134 C  CG2   . VAL D 161 ? 0.5899 0.5830 0.3861 -0.1786 0.0888  0.0030  160 VAL C CG2   
10144 N  N     . ARG D 162 ? 0.6334 0.6250 0.3898 -0.2127 0.1054  -0.0084 161 ARG C N     
10145 C  CA    . ARG D 162 ? 0.7206 0.7146 0.4724 -0.2209 0.1149  -0.0132 161 ARG C CA    
10146 C  C     . ARG D 162 ? 0.7387 0.7316 0.4847 -0.2250 0.1267  -0.0259 161 ARG C C     
10147 O  O     . ARG D 162 ? 0.7525 0.7493 0.5044 -0.2266 0.1395  -0.0336 161 ARG C O     
10148 C  CB    . ARG D 162 ? 0.7072 0.6970 0.4400 -0.2329 0.1041  -0.0040 161 ARG C CB    
10149 C  CG    . ARG D 162 ? 0.6453 0.6373 0.3874 -0.2298 0.0974  0.0062  161 ARG C CG    
10150 C  CD    . ARG D 162 ? 0.6316 0.6186 0.3562 -0.2407 0.0855  0.0159  161 ARG C CD    
10151 N  NE    . ARG D 162 ? 0.5979 0.5837 0.3301 -0.2366 0.0738  0.0277  161 ARG C NE    
10152 C  CZ    . ARG D 162 ? 0.7054 0.6844 0.4286 -0.2386 0.0571  0.0384  161 ARG C CZ    
10153 N  NH1   . ARG D 162 ? 0.6999 0.6736 0.4074 -0.2442 0.0496  0.0393  161 ARG C NH1   
10154 N  NH2   . ARG D 162 ? 0.6842 0.6617 0.4158 -0.2348 0.0472  0.0485  161 ARG C NH2   
10168 N  N     . GLU D 163 ? 0.6869 0.6743 0.4221 -0.2269 0.1226  -0.0282 162 GLU C N     
10169 C  CA    . GLU D 163 ? 0.7206 0.7062 0.4515 -0.2306 0.1340  -0.0406 162 GLU C CA    
10170 C  C     . GLU D 163 ? 0.7385 0.7281 0.4928 -0.2178 0.1461  -0.0497 162 GLU C C     
10171 O  O     . GLU D 163 ? 0.7546 0.7447 0.5128 -0.2190 0.1589  -0.0605 162 GLU C O     
10172 C  CB    . GLU D 163 ? 0.6970 0.6756 0.4102 -0.2371 0.1261  -0.0406 162 GLU C CB    
10173 C  CG    . GLU D 163 ? 0.7292 0.7032 0.4179 -0.2521 0.1161  -0.0343 162 GLU C CG    
10174 C  CD    . GLU D 163 ? 0.6648 0.6377 0.3411 -0.2644 0.1266  -0.0428 162 GLU C CD    
10175 O  OE1   . GLU D 163 ? 0.7753 0.7517 0.4539 -0.2669 0.1319  -0.0425 162 GLU C OE1   
10176 O  OE2   . GLU D 163 ? 0.6881 0.6567 0.3525 -0.2719 0.1297  -0.0497 162 GLU C OE2   
10183 N  N     . ILE D 164 ? 0.7626 0.7547 0.5327 -0.2057 0.1419  -0.0455 163 ILE C N     
10184 C  CA    . ILE D 164 ? 0.6933 0.6896 0.4874 -0.1932 0.1524  -0.0529 163 ILE C CA    
10185 C  C     . ILE D 164 ? 0.7520 0.7553 0.5615 -0.1910 0.1629  -0.0560 163 ILE C C     
10186 O  O     . ILE D 164 ? 0.7635 0.7681 0.5813 -0.1901 0.1754  -0.0662 163 ILE C O     
10187 C  CB    . ILE D 164 ? 0.6532 0.6508 0.4599 -0.1817 0.1449  -0.0468 163 ILE C CB    
10188 C  CG1   . ILE D 164 ? 0.6911 0.6819 0.4818 -0.1848 0.1347  -0.0440 163 ILE C CG1   
10189 C  CG2   . ILE D 164 ? 0.6223 0.6241 0.4546 -0.1687 0.1551  -0.0541 163 ILE C CG2   
10190 C  CD1   . ILE D 164 ? 0.6585 0.6500 0.4578 -0.1754 0.1256  -0.0368 163 ILE C CD1   
10202 N  N     . ARG D 165 ? 0.8035 0.8110 0.6165 -0.1910 0.1574  -0.0471 164 ARG C N     
10203 C  CA    . ARG D 165 ? 0.8175 0.8327 0.6460 -0.1892 0.1660  -0.0486 164 ARG C CA    
10204 C  C     . ARG D 165 ? 0.8238 0.8388 0.6445 -0.1982 0.1771  -0.0574 164 ARG C C     
10205 O  O     . ARG D 165 ? 0.8273 0.8477 0.6654 -0.1937 0.1892  -0.0648 164 ARG C O     
10206 C  CB    . ARG D 165 ? 0.7587 0.7763 0.5849 -0.1923 0.1567  -0.0370 164 ARG C CB    
10207 C  CG    . ARG D 165 ? 0.7272 0.7507 0.5758 -0.1810 0.1536  -0.0314 164 ARG C CG    
10208 C  CD    . ARG D 165 ? 0.6903 0.7129 0.5322 -0.1852 0.1413  -0.0188 164 ARG C CD    
10209 N  NE    . ARG D 165 ? 0.6981 0.7244 0.5584 -0.1754 0.1361  -0.0129 164 ARG C NE    
10210 C  CZ    . ARG D 165 ? 0.6152 0.6400 0.4732 -0.1772 0.1246  -0.0020 164 ARG C CZ    
10211 N  NH1   . ARG D 165 ? 0.6293 0.6494 0.4689 -0.1876 0.1170  0.0047  164 ARG C NH1   
10212 N  NH2   . ARG D 165 ? 0.6238 0.6516 0.4986 -0.1687 0.1203  0.0023  164 ARG C NH2   
10226 N  N     . LYS D 166 ? 0.9224 0.9311 0.7171 -0.2113 0.1728  -0.0566 165 LYS C N     
10227 C  CA    . LYS D 166 ? 0.9391 0.9468 0.7235 -0.2216 0.1831  -0.0651 165 LYS C CA    
10228 C  C     . LYS D 166 ? 0.9435 0.9504 0.7391 -0.2166 0.1957  -0.0779 165 LYS C C     
10229 O  O     . LYS D 166 ? 0.9577 0.9696 0.7684 -0.2140 0.2082  -0.0852 165 LYS C O     
10230 C  CB    . LYS D 166 ? 0.9135 0.9135 0.6677 -0.2362 0.1748  -0.0619 165 LYS C CB    
10231 C  CG    . LYS D 166 ? 0.9950 0.9957 0.7348 -0.2476 0.1705  -0.0550 165 LYS C CG    
10232 C  CD    . LYS D 166 ? 1.1232 1.1288 0.8679 -0.2521 0.1848  -0.0628 165 LYS C CD    
10233 C  CE    . LYS D 166 ? 1.2319 1.2348 0.9526 -0.2684 0.1820  -0.0595 165 LYS C CE    
10234 N  NZ    . LYS D 166 ? 1.2002 1.2101 0.9289 -0.2702 0.1878  -0.0577 165 LYS C NZ    
10248 N  N     . HIS D 167 ? 0.9250 0.9256 0.7144 -0.2151 0.1922  -0.0805 166 HIS C N     
10249 C  CA    . HIS D 167 ? 0.9166 0.9149 0.7169 -0.2095 0.2021  -0.0916 166 HIS C CA    
10250 C  C     . HIS D 167 ? 0.9070 0.9117 0.7384 -0.1940 0.2083  -0.0937 166 HIS C C     
10251 O  O     . HIS D 167 ? 0.9462 0.9496 0.7903 -0.1889 0.2179  -0.1031 166 HIS C O     
10252 C  CB    . HIS D 167 ? 0.8700 0.8606 0.6564 -0.2111 0.1933  -0.0904 166 HIS C CB    
10253 C  CG    . HIS D 167 ? 0.8996 0.8869 0.6978 -0.2037 0.2001  -0.0993 166 HIS C CG    
10254 N  ND1   . HIS D 167 ? 0.8969 0.8777 0.6836 -0.2117 0.2061  -0.1085 166 HIS C ND1   
10255 C  CD2   . HIS D 167 ? 0.8854 0.8744 0.7049 -0.1897 0.2008  -0.0998 166 HIS C CD2   
10256 C  CE1   . HIS D 167 ? 0.9044 0.8827 0.7055 -0.2026 0.2106  -0.1144 166 HIS C CE1   
10257 N  NE2   . HIS D 167 ? 0.9094 0.8927 0.7306 -0.1891 0.2074  -0.1092 166 HIS C NE2   
10265 N  N     . LYS D 168 ? 0.8735 0.8848 0.7175 -0.1872 0.2032  -0.0852 167 LYS C N     
10266 C  CA    . LYS D 168 ? 0.8994 0.9171 0.7726 -0.1724 0.2062  -0.0852 167 LYS C CA    
10267 C  C     . LYS D 168 ? 0.9066 0.9327 0.7968 -0.1709 0.2157  -0.0876 167 LYS C C     
10268 O  O     . LYS D 168 ? 0.9219 0.9477 0.8032 -0.1802 0.2234  -0.0932 167 LYS C O     
10269 C  CB    . LYS D 168 ? 0.8435 0.8628 0.7194 -0.1664 0.1935  -0.0740 167 LYS C CB    
10270 C  CG    . LYS D 168 ? 0.8931 0.9204 0.7971 -0.1533 0.1941  -0.0709 167 LYS C CG    
10271 C  CD    . LYS D 168 ? 0.8932 0.9205 0.7940 -0.1506 0.1809  -0.0598 167 LYS C CD    
10272 C  CE    . LYS D 168 ? 0.9002 0.9342 0.8278 -0.1375 0.1799  -0.0566 167 LYS C CE    
10273 N  NZ    . LYS D 168 ? 0.9255 0.9611 0.8742 -0.1274 0.1888  -0.0649 167 LYS C NZ    
10287 P  PG    . GNP E .   ? 0.4062 0.4259 0.4893 0.0417  0.0204  0.0201  201 GNP A PG    
10288 O  O1G   . GNP E .   ? 0.2232 0.2400 0.2972 0.0391  0.0238  0.0152  201 GNP A O1G   
10289 O  O2G   . GNP E .   ? 0.3486 0.3701 0.4463 0.0433  0.0256  0.0212  201 GNP A O2G   
10290 O  O3G   . GNP E .   ? 0.3591 0.3824 0.4411 0.0406  0.0139  0.0218  201 GNP A O3G   
10291 N  N3B   . GNP E .   ? 0.2245 0.2419 0.3026 0.0435  0.0165  0.0228  201 GNP A N3B   
10292 P  PB    . GNP E .   ? 0.2099 0.2227 0.2851 0.0441  0.0208  0.0216  201 GNP A PB    
10293 O  O1B   . GNP E .   ? 0.1937 0.2041 0.2613 0.0417  0.0250  0.0161  201 GNP A O1B   
10294 O  O2B   . GNP E .   ? 0.1973 0.2086 0.2837 0.0464  0.0240  0.0245  201 GNP A O2B   
10295 O  O3A   . GNP E .   ? 0.2172 0.2295 0.2842 0.0442  0.0152  0.0241  201 GNP A O3A   
10296 P  PA    . GNP E .   ? 0.2329 0.2441 0.2874 0.0425  0.0139  0.0207  201 GNP A PA    
10297 O  O1A   . GNP E .   ? 0.2017 0.2150 0.2527 0.0413  0.0112  0.0179  201 GNP A O1A   
10298 O  O2A   . GNP E .   ? 0.2120 0.2200 0.2632 0.0417  0.0191  0.0177  201 GNP A O2A   
10299 O  "O5'" . GNP E .   ? 0.2343 0.2460 0.2844 0.0427  0.0088  0.0244  201 GNP A "O5'" 
10300 C  "C5'" . GNP E .   ? 0.2280 0.2425 0.2802 0.0429  0.0030  0.0280  201 GNP A "C5'" 
10301 C  "C4'" . GNP E .   ? 0.2636 0.2779 0.3061 0.0414  -0.0013 0.0292  201 GNP A "C4'" 
10302 O  "O4'" . GNP E .   ? 0.2615 0.2735 0.3040 0.0415  0.0000  0.0329  201 GNP A "O4'" 
10303 C  "C3'" . GNP E .   ? 0.2857 0.2993 0.3185 0.0402  0.0002  0.0233  201 GNP A "C3'" 
10304 O  "O3'" . GNP E .   ? 0.3575 0.3719 0.3824 0.0386  -0.0044 0.0233  201 GNP A "O3'" 
10305 C  "C2'" . GNP E .   ? 0.2711 0.2823 0.3014 0.0399  0.0046  0.0231  201 GNP A "C2'" 
10306 O  "O2'" . GNP E .   ? 0.3377 0.3492 0.3584 0.0382  0.0044  0.0200  201 GNP A "O2'" 
10307 C  "C1'" . GNP E .   ? 0.2870 0.2974 0.3196 0.0399  0.0022  0.0297  201 GNP A "C1'" 
10308 N  N9    . GNP E .   ? 0.2672 0.2742 0.3026 0.0403  0.0066  0.0314  201 GNP A N9    
10309 C  C8    . GNP E .   ? 0.2481 0.2532 0.2908 0.0416  0.0119  0.0296  201 GNP A C8    
10310 N  N7    . GNP E .   ? 0.2199 0.2212 0.2635 0.0413  0.0151  0.0315  201 GNP A N7    
10311 C  C5    . GNP E .   ? 0.2669 0.2680 0.3034 0.0397  0.0114  0.0355  201 GNP A C5    
10312 C  C6    . GNP E .   ? 0.2473 0.2447 0.2809 0.0382  0.0122  0.0396  201 GNP A C6    
10313 O  O6    . GNP E .   ? 0.2476 0.2406 0.2854 0.0384  0.0165  0.0403  201 GNP A O6    
10314 N  N1    . GNP E .   ? 0.2859 0.2844 0.3100 0.0356  0.0076  0.0428  201 GNP A N1    
10315 C  C2    . GNP E .   ? 0.3111 0.3135 0.3295 0.0347  0.0031  0.0416  201 GNP A C2    
10316 N  N2    . GNP E .   ? 0.3223 0.3250 0.3306 0.0315  -0.0007 0.0448  201 GNP A N2    
10317 N  N3    . GNP E .   ? 0.2928 0.2982 0.3147 0.0364  0.0023  0.0376  201 GNP A N3    
10318 C  C4    . GNP E .   ? 0.2764 0.2811 0.3073 0.0388  0.0064  0.0352  201 GNP A C4    
10332 MG MG    . MG  F .   ? 0.2039 0.2156 0.2667 0.0381  0.0264  0.0115  202 MG  A MG    
10333 C  C1    . ZNI G .   ? 0.1565 0.1832 0.2193 0.0059  -0.0035 0.0239  201 ZNI B C1    
10334 C  C10   . ZNI G .   ? 0.2343 0.2508 0.2788 0.0322  -0.0167 0.0148  201 ZNI B C10   
10335 C  C11   . ZNI G .   ? 0.2336 0.2500 0.2747 0.0340  -0.0182 0.0142  201 ZNI B C11   
10336 C  C12   . ZNI G .   ? 0.2733 0.2873 0.3133 0.0311  -0.0263 0.0138  201 ZNI B C12   
10337 C  C13   . ZNI G .   ? 0.1760 0.2070 0.2514 0.0234  -0.0045 0.0230  201 ZNI B C13   
10338 C  C14   . ZNI G .   ? 0.2081 0.2387 0.2838 0.0242  0.0032  0.0208  201 ZNI B C14   
10339 C  C15   . ZNI G .   ? 0.2149 0.2450 0.2921 0.0233  0.0163  0.0168  201 ZNI B C15   
10340 C  C16   . ZNI G .   ? 0.2542 0.2813 0.3267 0.0265  0.0134  0.0166  201 ZNI B C16   
10341 C  C17   . ZNI G .   ? 0.1995 0.2300 0.2777 0.0204  0.0242  0.0144  201 ZNI B C17   
10342 C  C18   . ZNI G .   ? 0.1894 0.2213 0.2659 0.0153  0.0258  0.0142  201 ZNI B C18   
10343 C  C19   . ZNI G .   ? 0.1769 0.2089 0.2516 0.0110  0.0339  0.0113  201 ZNI B C19   
10344 C  C2    . ZNI G .   ? 0.1653 0.1919 0.2285 0.0108  -0.0002 0.0215  201 ZNI B C2    
10345 C  C20   . ZNI G .   ? 0.2010 0.2315 0.2769 0.0123  0.0414  0.0077  201 ZNI B C20   
10346 C  C21   . ZNI G .   ? 0.2254 0.2541 0.3038 0.0178  0.0394  0.0080  201 ZNI B C21   
10347 C  C22   . ZNI G .   ? 0.2330 0.2619 0.3123 0.0216  0.0312  0.0115  201 ZNI B C22   
10348 C  C23   . ZNI G .   ? 0.3208 0.3496 0.3936 0.0057  0.0588  -0.0006 201 ZNI B C23   
10349 C  C24   . ZNI G .   ? 0.3002 0.3331 0.3914 0.0107  0.0649  -0.0012 201 ZNI B C24   
10350 C  C25   . ZNI G .   ? 0.2093 0.2422 0.2795 0.0018  0.0471  0.0064  201 ZNI B C25   
10351 C  C26   . ZNI G .   ? 0.2352 0.2691 0.3012 -0.0053 0.0542  0.0040  201 ZNI B C26   
10352 C  C27   . ZNI G .   ? 0.2407 0.2699 0.2917 -0.0114 0.0574  0.0011  201 ZNI B C27   
10353 C  C28   . ZNI G .   ? 0.2392 0.2621 0.2778 -0.0107 0.0527  0.0004  201 ZNI B C28   
10354 C  C29   . ZNI G .   ? 0.2816 0.2981 0.3131 -0.0076 0.0556  -0.0047 201 ZNI B C29   
10355 C  C3    . ZNI G .   ? 0.1607 0.1825 0.2209 0.0110  -0.0163 0.0244  201 ZNI B C3    
10356 C  C30   . ZNI G .   ? 0.2863 0.3053 0.3092 -0.0172 0.0469  0.0024  201 ZNI B C30   
10357 C  C31   . ZNI G .   ? 0.2867 0.3233 0.3436 -0.0204 0.0694  -0.0010 201 ZNI B C31   
10358 C  C32   . ZNI G .   ? 0.3033 0.3456 0.3772 -0.0145 0.0670  0.0018  201 ZNI B C32   
10359 C  C33   . ZNI G .   ? 0.3323 0.3859 0.4231 -0.0211 0.0839  -0.0023 201 ZNI B C33   
10360 C  C34   . ZNI G .   ? 0.3090 0.3697 0.4072 -0.0256 0.0847  0.0003  201 ZNI B C34   
10361 C  C35   . ZNI G .   ? 0.3996 0.4726 0.5198 -0.0255 0.0801  0.0066  201 ZNI B C35   
10362 C  C36   . ZNI G .   ? 0.4107 0.4940 0.5525 -0.0234 0.0805  0.0090  201 ZNI B C36   
10363 C  C37   . ZNI G .   ? 0.3652 0.4462 0.4991 -0.0280 0.0933  0.0022  201 ZNI B C37   
10364 C  C38   . ZNI G .   ? 0.3099 0.3730 0.4237 -0.0138 0.0674  0.0086  201 ZNI B C38   
10365 C  C39   . ZNI G .   ? 0.3477 0.4034 0.4526 -0.0095 0.0666  0.0062  201 ZNI B C39   
10366 C  C4    . ZNI G .   ? 0.1609 0.1882 0.2279 0.0075  -0.0107 0.0258  201 ZNI B C4    
10367 C  C40   . ZNI G .   ? 0.2546 0.2948 0.3315 -0.0071 0.0590  0.0043  201 ZNI B C40   
10368 C  C41   . ZNI G .   ? 0.2001 0.2336 0.2720 0.0045  0.0376  0.0106  201 ZNI B C41   
10369 C  C42   . ZNI G .   ? 0.1819 0.2169 0.2524 0.0006  0.0324  0.0139  201 ZNI B C42   
10370 C  C43   . ZNI G .   ? 0.1628 0.1923 0.2191 -0.0035 0.0256  0.0155  201 ZNI B C43   
10371 C  C44   . ZNI G .   ? 0.1895 0.2209 0.2481 -0.0069 0.0210  0.0191  201 ZNI B C44   
10372 C  C45   . ZNI G .   ? 0.1853 0.2119 0.2304 -0.0094 0.0314  0.0127  201 ZNI B C45   
10373 C  C46   . ZNI G .   ? 0.1926 0.2180 0.2446 0.0011  0.0181  0.0162  201 ZNI B C46   
10374 C  C47   . ZNI G .   ? 0.1643 0.1888 0.2210 0.0086  0.0057  0.0191  201 ZNI B C47   
10375 C  C5    . ZNI G .   ? 0.1806 0.2051 0.2442 0.0195  -0.0145 0.0226  201 ZNI B C5    
10376 C  C6    . ZNI G .   ? 0.1583 0.1837 0.2227 0.0230  -0.0097 0.0213  201 ZNI B C6    
10377 C  C7    . ZNI G .   ? 0.1713 0.1908 0.2244 0.0275  -0.0150 0.0181  201 ZNI B C7    
10378 C  C8    . ZNI G .   ? 0.1998 0.2185 0.2501 0.0299  -0.0182 0.0175  201 ZNI B C8    
10379 C  C9    . ZNI G .   ? 0.2306 0.2451 0.2737 0.0303  -0.0223 0.0145  201 ZNI B C9    
10380 N  N1    . ZNI G .   ? 0.1865 0.2090 0.2443 0.0143  -0.0062 0.0209  201 ZNI B N1    
10381 N  N2    . ZNI G .   ? 0.1986 0.2216 0.2593 0.0153  -0.0124 0.0225  201 ZNI B N2    
10382 N  N3    . ZNI G .   ? 0.1718 0.1955 0.2329 0.0262  -0.0136 0.0208  201 ZNI B N3    
10383 N  N4    . ZNI G .   ? 0.2110 0.2428 0.2892 0.0220  0.0099  0.0195  201 ZNI B N4    
10384 N  N5    . ZNI G .   ? 0.2441 0.2748 0.3169 0.0068  0.0492  0.0044  201 ZNI B N5    
10385 N  N6    . ZNI G .   ? 0.2552 0.2856 0.3015 -0.0187 0.0643  -0.0011 201 ZNI B N6    
10386 N  N7    . ZNI G .   ? 0.2966 0.3465 0.3841 -0.0158 0.0713  0.0025  201 ZNI B N7    
10387 N  N8    . ZNI G .   ? 0.3435 0.4106 0.4600 -0.0196 0.0794  0.0044  201 ZNI B N8    
10388 O  O1    . ZNI G .   ? 0.1840 0.2090 0.2492 0.0199  -0.0198 0.0238  201 ZNI B O1    
10389 O  O2    . ZNI G .   ? 0.1719 0.1884 0.2202 0.0263  -0.0139 0.0163  201 ZNI B O2    
10390 O  O3    . ZNI G .   ? 0.2314 0.2482 0.2726 0.0328  -0.0235 0.0154  201 ZNI B O3    
10391 O  O4    . ZNI G .   ? 0.3161 0.3370 0.3540 -0.0104 0.0605  -0.0045 201 ZNI B O4    
10392 O  O5    . ZNI G .   ? 0.1527 0.1808 0.2136 0.0056  0.0131  0.0184  201 ZNI B O5    
10393 O  O6    . ZNI G .   ? 0.1890 0.2090 0.2373 0.0090  0.0039  0.0178  201 ZNI B O6    
10394 S  S1    . ZNI G .   ? 0.2230 0.2499 0.2930 0.0281  0.0040  0.0190  201 ZNI B S1    
10455 C  C1    . ZNI H .   ? 0.3426 0.3503 0.2269 -0.1152 -0.0226 -0.0213 201 ZNI D C1    
10456 C  C10   . ZNI H .   ? 0.4536 0.4851 0.3636 -0.1161 -0.1118 0.0393  201 ZNI D C10   
10457 C  C11   . ZNI H .   ? 0.4635 0.5001 0.3798 -0.1200 -0.1294 0.0494  201 ZNI D C11   
10458 C  C12   . ZNI H .   ? 0.4743 0.4974 0.3665 -0.1242 -0.1238 0.0519  201 ZNI D C12   
10459 C  C13   . ZNI H .   ? 0.4315 0.4374 0.2730 -0.1421 -0.0534 -0.0006 201 ZNI D C13   
10460 C  C14   . ZNI H .   ? 0.4519 0.4511 0.2865 -0.1396 -0.0420 -0.0043 201 ZNI D C14   
10461 C  C15   . ZNI H .   ? 0.5105 0.5000 0.3376 -0.1356 -0.0205 -0.0131 201 ZNI D C15   
10462 C  C16   . ZNI H .   ? 0.5485 0.5401 0.3752 -0.1359 -0.0312 -0.0043 201 ZNI D C16   
10463 C  C17   . ZNI H .   ? 0.4706 0.4547 0.2972 -0.1323 -0.0043 -0.0218 201 ZNI D C17   
10464 C  C18   . ZNI H .   ? 0.4459 0.4289 0.2817 -0.1269 0.0044  -0.0287 201 ZNI D C18   
10465 C  C19   . ZNI H .   ? 0.4681 0.4461 0.3071 -0.1222 0.0192  -0.0365 201 ZNI D C19   
10466 C  C2    . ZNI H .   ? 0.3105 0.3157 0.1861 -0.1165 -0.0257 -0.0168 201 ZNI D C2    
10467 C  C20   . ZNI H .   ? 0.4588 0.4336 0.2925 -0.1226 0.0261  -0.0376 201 ZNI D C20   
10468 C  C21   . ZNI H .   ? 0.4831 0.4595 0.3074 -0.1279 0.0177  -0.0307 201 ZNI D C21   
10469 C  C22   . ZNI H .   ? 0.4886 0.4690 0.3094 -0.1324 0.0030  -0.0229 201 ZNI D C22   
10470 C  C23   . ZNI H .   ? 0.4929 0.4601 0.3323 -0.1159 0.0511  -0.0490 201 ZNI D C23   
10471 C  C24   . ZNI H .   ? 0.5590 0.5196 0.3799 -0.1283 0.0617  -0.0575 201 ZNI D C24   
10472 C  C25   . ZNI H .   ? 0.4650 0.4350 0.3133 -0.1141 0.0419  -0.0489 201 ZNI D C25   
10473 C  C26   . ZNI H .   ? 0.4765 0.4416 0.3336 -0.1085 0.0547  -0.0563 201 ZNI D C26   
10474 C  C27   . ZNI H .   ? 0.4414 0.4072 0.3150 -0.0963 0.0595  -0.0555 201 ZNI D C27   
10475 C  C28   . ZNI H .   ? 0.4175 0.3896 0.3009 -0.0878 0.0520  -0.0473 201 ZNI D C28   
10476 C  C29   . ZNI H .   ? 0.5156 0.4910 0.3998 -0.0843 0.0496  -0.0404 201 ZNI D C29   
10477 C  C3    . ZNI H .   ? 0.3708 0.3934 0.2697 -0.1161 -0.0483 -0.0078 201 ZNI D C3    
10478 C  C30   . ZNI H .   ? 0.4021 0.3779 0.3037 -0.0758 0.0491  -0.0440 201 ZNI D C30   
10479 C  C31   . ZNI H .   ? 0.4613 0.4159 0.3361 -0.0983 0.0772  -0.0690 201 ZNI D C31   
10480 C  C32   . ZNI H .   ? 0.5017 0.4546 0.3597 -0.1107 0.0742  -0.0715 201 ZNI D C32   
10481 C  C33   . ZNI H .   ? 0.5818 0.5271 0.4125 -0.1325 0.0754  -0.0811 201 ZNI D C33   
10482 C  C34   . ZNI H .   ? 0.5615 0.5014 0.3908 -0.1369 0.0790  -0.0875 201 ZNI D C34   
10483 C  C35   . ZNI H .   ? 0.6193 0.5446 0.4496 -0.1405 0.0957  -0.1021 201 ZNI D C35   
10484 C  C36   . ZNI H .   ? 0.7006 0.6180 0.5121 -0.1548 0.1010  -0.1113 201 ZNI D C36   
10485 C  C37   . ZNI H .   ? 0.6573 0.5711 0.4882 -0.1414 0.1108  -0.1127 201 ZNI D C37   
10486 C  C38   . ZNI H .   ? 0.6450 0.5763 0.4963 -0.1216 0.0984  -0.0945 201 ZNI D C38   
10487 C  C39   . ZNI H .   ? 0.5825 0.5199 0.4358 -0.1170 0.0954  -0.0885 201 ZNI D C39   
10488 C  C4    . ZNI H .   ? 0.3108 0.3259 0.1980 -0.1209 -0.0350 -0.0170 201 ZNI D C4    
10489 C  C40   . ZNI H .   ? 0.4380 0.3969 0.2875 -0.1153 0.0624  -0.0644 201 ZNI D C40   
10490 C  C41   . ZNI H .   ? 0.4169 0.3917 0.2644 -0.1172 0.0297  -0.0438 201 ZNI D C41   
10491 C  C42   . ZNI H .   ? 0.3782 0.3550 0.2331 -0.1161 0.0272  -0.0453 201 ZNI D C42   
10492 C  C43   . ZNI H .   ? 0.3548 0.3381 0.2302 -0.1038 0.0219  -0.0406 201 ZNI D C43   
10493 C  C44   . ZNI H .   ? 0.3737 0.3582 0.2539 -0.1052 0.0214  -0.0434 201 ZNI D C44   
10494 C  C45   . ZNI H .   ? 0.3616 0.3429 0.2486 -0.0929 0.0305  -0.0420 201 ZNI D C45   
10495 C  C46   . ZNI H .   ? 0.3647 0.3549 0.2439 -0.1018 0.0088  -0.0316 201 ZNI D C46   
10496 C  C47   . ZNI H .   ? 0.2994 0.3003 0.1804 -0.1072 -0.0145 -0.0202 201 ZNI D C47   
10497 C  C5    . ZNI H .   ? 0.3773 0.3963 0.2552 -0.1268 -0.0617 0.0025  201 ZNI D C5    
10498 C  C6    . ZNI H .   ? 0.4403 0.4538 0.3051 -0.1301 -0.0624 0.0061  201 ZNI D C6    
10499 C  C7    . ZNI H .   ? 0.4140 0.4343 0.2962 -0.1228 -0.0841 0.0224  201 ZNI D C7    
10500 C  C8    . ZNI H .   ? 0.4315 0.4546 0.3164 -0.1254 -0.1002 0.0330  201 ZNI D C8    
10501 C  C9    . ZNI H .   ? 0.5006 0.5239 0.3969 -0.1178 -0.1080 0.0407  201 ZNI D C9    
10502 N  N1    . ZNI H .   ? 0.3504 0.3625 0.2368 -0.1120 -0.0387 -0.0079 201 ZNI D N1    
10503 N  N2    . ZNI H .   ? 0.3278 0.3456 0.2156 -0.1179 -0.0496 -0.0044 201 ZNI D N2    
10504 N  N3    . ZNI H .   ? 0.4295 0.4465 0.2952 -0.1330 -0.0776 0.0160  201 ZNI D N3    
10505 N  N4    . ZNI H .   ? 0.4358 0.4295 0.2668 -0.1381 -0.0274 -0.0127 201 ZNI D N4    
10506 N  N5    . ZNI H .   ? 0.4750 0.4455 0.3151 -0.1174 0.0400  -0.0453 201 ZNI D N5    
10507 N  N6    . ZNI H .   ? 0.4246 0.3855 0.3059 -0.0920 0.0702  -0.0616 201 ZNI D N6    
10508 N  N7    . ZNI H .   ? 0.5000 0.4457 0.3489 -0.1190 0.0811  -0.0799 201 ZNI D N7    
10509 N  N8    . ZNI H .   ? 0.6107 0.5409 0.4429 -0.1355 0.0942  -0.0971 201 ZNI D N8    
10510 O  O1    . ZNI H .   ? 0.3699 0.3944 0.2498 -0.1322 -0.0721 0.0063  201 ZNI D O1    
10511 O  O2    . ZNI H .   ? 0.3930 0.4136 0.2887 -0.1112 -0.0768 0.0192  201 ZNI D O2    
10512 O  O3    . ZNI H .   ? 0.4565 0.4859 0.3515 -0.1301 -0.1333 0.0544  201 ZNI D O3    
10513 O  O4    . ZNI H .   ? 0.4431 0.4138 0.3257 -0.0868 0.0580  -0.0480 201 ZNI D O4    
10514 O  O5    . ZNI H .   ? 0.3220 0.3161 0.1951 -0.1101 -0.0021 -0.0281 201 ZNI D O5    
10515 O  O6    . ZNI H .   ? 0.3471 0.3507 0.2401 -0.0975 -0.0164 -0.0164 201 ZNI D O6    
10516 S  S1    . ZNI H .   ? 0.5297 0.5281 0.3622 -0.1382 -0.0495 0.0049  201 ZNI D S1    
10577 P  PG    . GNP I .   ? 0.7303 0.7078 0.4908 -0.1723 -0.0525 0.0251  201 GNP C PG    
10578 O  O1G   . GNP I .   ? 0.5028 0.4814 0.2826 -0.1578 -0.0447 0.0224  201 GNP C O1G   
10579 O  O2G   . GNP I .   ? 0.6515 0.6241 0.3889 -0.1849 -0.0391 0.0165  201 GNP C O2G   
10580 O  O3G   . GNP I .   ? 0.7095 0.6913 0.4798 -0.1691 -0.0568 0.0229  201 GNP C O3G   
10581 N  N3B   . GNP I .   ? 0.6163 0.5933 0.3698 -0.1793 -0.0709 0.0396  201 GNP C N3B   
10582 P  PB    . GNP I .   ? 0.4963 0.4693 0.2433 -0.1817 -0.0717 0.0460  201 GNP C PB    
10583 O  O1B   . GNP I .   ? 0.5237 0.4976 0.2896 -0.1674 -0.0620 0.0416  201 GNP C O1B   
10584 O  O2B   . GNP I .   ? 0.4668 0.4352 0.1883 -0.1970 -0.0630 0.0423  201 GNP C O2B   
10585 O  O3A   . GNP I .   ? 0.5269 0.4994 0.2763 -0.1840 -0.0910 0.0607  201 GNP C O3A   
10586 P  PA    . GNP I .   ? 0.5146 0.4895 0.2892 -0.1696 -0.1017 0.0682  201 GNP C PA    
10587 O  O1A   . GNP I .   ? 0.5446 0.5161 0.3216 -0.1654 -0.0950 0.0685  201 GNP C O1A   
10588 O  O2A   . GNP I .   ? 0.5348 0.5154 0.3329 -0.1555 -0.1001 0.0629  201 GNP C O2A   
10589 O  "O5'" . GNP I .   ? 0.5630 0.5364 0.3392 -0.1748 -0.1177 0.0804  201 GNP C "O5'" 
10590 C  "C5'" . GNP I .   ? 0.6239 0.5987 0.3958 -0.1823 -0.1233 0.0822  201 GNP C "C5'" 
10591 C  "C4'" . GNP I .   ? 0.5830 0.5577 0.3689 -0.1800 -0.1391 0.0940  201 GNP C "C4'" 
10592 O  "O4'" . GNP I .   ? 0.6347 0.6030 0.4086 -0.1891 -0.1410 0.1003  201 GNP C "O4'" 
10593 C  "C3'" . GNP I .   ? 0.6208 0.5976 0.4309 -0.1647 -0.1449 0.0971  201 GNP C "C3'" 
10594 O  "O3'" . GNP I .   ? 0.5634 0.5424 0.3900 -0.1612 -0.1581 0.1048  201 GNP C "O3'" 
10595 C  "C2'" . GNP I .   ? 0.5813 0.5516 0.3868 -0.1663 -0.1447 0.1020  201 GNP C "C2'" 
10596 O  "O2'" . GNP I .   ? 0.6052 0.5749 0.4325 -0.1562 -0.1554 0.1094  201 GNP C "O2'" 
10597 C  "C1'" . GNP I .   ? 0.6069 0.5730 0.3959 -0.1809 -0.1484 0.1076  201 GNP C "C1'" 
10598 N  N9    . GNP I .   ? 0.6344 0.5947 0.4086 -0.1886 -0.1432 0.1088  201 GNP C N9    
10599 C  C8    . GNP I .   ? 0.6391 0.5985 0.4036 -0.1889 -0.1303 0.1015  201 GNP C C8    
10600 N  N7    . GNP I .   ? 0.6373 0.5918 0.3905 -0.1970 -0.1282 0.1046  201 GNP C N7    
10601 C  C5    . GNP I .   ? 0.6245 0.5762 0.3790 -0.2027 -0.1408 0.1145  201 GNP C C5    
10602 C  C6    . GNP I .   ? 0.6467 0.5929 0.3916 -0.2131 -0.1453 0.1217  201 GNP C C6    
10603 O  O6    . GNP I .   ? 0.6913 0.6346 0.4250 -0.2189 -0.1384 0.1202  201 GNP C O6    
10604 N  N1    . GNP I .   ? 0.6246 0.5691 0.3751 -0.2161 -0.1591 0.1312  201 GNP C N1    
10605 C  C2    . GNP I .   ? 0.6943 0.6424 0.4586 -0.2100 -0.1674 0.1335  201 GNP C C2    
10606 N  N2    . GNP I .   ? 0.6256 0.5716 0.3942 -0.2144 -0.1804 0.1433  201 GNP C N2    
10607 N  N3    . GNP I .   ? 0.6289 0.5827 0.4024 -0.2005 -0.1631 0.1265  201 GNP C N3    
10608 C  C4    . GNP I .   ? 0.6271 0.5822 0.3947 -0.1975 -0.1500 0.1173  201 GNP C C4    
10622 MG MG    . MG  J .   ? 0.5198 0.4986 0.3138 -0.1482 -0.0516 0.0316  202 MG  C MG    
10623 O  O     . HOH K .   ? 0.8466 0.8846 1.0341 0.0624  0.0039  0.0611  301 HOH A O     
10624 O  O     . HOH K .   ? 0.5824 0.5555 0.6051 0.0043  0.0661  -0.0088 302 HOH A O     
10625 O  O     . HOH K .   ? 0.4448 0.4898 0.6155 0.0532  0.0183  0.0411  303 HOH A O     
10626 O  O     . HOH K .   ? 0.4137 0.4536 0.5967 0.0541  0.0412  0.0295  304 HOH A O     
10627 O  O     . HOH K .   ? 0.4894 0.4633 0.8153 0.0778  0.1092  0.0076  305 HOH A O     
10628 O  O     . HOH K .   ? 0.4830 0.5124 0.5917 0.0420  0.0232  0.0233  306 HOH A O     
10629 O  O     . HOH K .   ? 0.4993 0.4375 0.6003 -0.0026 0.1714  -0.0823 307 HOH A O     
10630 O  O     . HOH K .   ? 0.4527 0.4651 0.4567 0.0341  -0.0011 0.0214  308 HOH A O     
10631 O  O     . HOH K .   ? 0.4650 0.5122 0.6758 0.0612  0.0283  0.0440  309 HOH A O     
10632 O  O     . HOH K .   ? 0.4813 0.4901 0.5015 0.0236  0.0189  -0.0056 310 HOH A O     
10633 O  O     . HOH K .   ? 0.3869 0.3668 0.4365 -0.0037 0.1212  -0.0486 311 HOH A O     
10634 O  O     . HOH K .   ? 0.5379 0.5770 0.7078 0.0588  -0.0112 0.0685  312 HOH A O     
10635 O  O     . HOH K .   ? 0.5607 0.5120 0.5738 0.0172  0.0154  0.0851  313 HOH A O     
10636 O  O     . HOH K .   ? 0.4820 0.4944 0.5398 -0.0020 0.0919  -0.0231 314 HOH A O     
10637 O  O     . HOH K .   ? 0.4790 0.5685 0.6753 0.0101  0.0696  0.0144  315 HOH A O     
10638 O  O     . HOH K .   ? 0.4329 0.4470 0.4551 0.0439  -0.0056 -0.0217 316 HOH A O     
10639 O  O     . HOH K .   ? 0.4365 0.4457 0.4623 0.0272  -0.0008 0.0030  317 HOH A O     
10640 O  O     . HOH K .   ? 0.2313 0.2402 0.3017 0.0369  0.0375  0.0080  318 HOH A O     
10641 O  O     . HOH K .   ? 0.5701 0.4260 0.6455 -0.0050 0.1440  -0.0599 319 HOH A O     
10642 O  O     . HOH K .   ? 0.2938 0.3095 0.3380 0.0301  -0.0027 0.0122  320 HOH A O     
10643 O  O     . HOH K .   ? 0.5788 0.4777 0.6376 0.0046  0.0959  -0.0066 321 HOH A O     
10644 O  O     . HOH K .   ? 0.4657 0.4808 0.5321 0.0090  0.0745  -0.0126 322 HOH A O     
10645 O  O     . HOH K .   ? 0.3825 0.4220 0.5360 0.0374  0.0622  0.0093  323 HOH A O     
10646 O  O     . HOH K .   ? 0.3194 0.3247 0.3515 0.0261  0.0305  -0.0022 324 HOH A O     
10647 O  O     . HOH K .   ? 0.4174 0.3911 0.4186 0.0193  0.0217  0.0590  325 HOH A O     
10648 O  O     . HOH K .   ? 0.4403 0.4764 0.5714 0.0249  0.0755  -0.0019 326 HOH A O     
10649 O  O     . HOH K .   ? 0.4371 0.4354 0.4062 0.0165  0.0012  0.0505  327 HOH A O     
10650 O  O     . HOH K .   ? 0.5162 0.5197 0.5193 0.0055  0.0221  -0.0058 328 HOH A O     
10651 O  O     . HOH K .   ? 0.5648 0.5978 0.7534 0.0536  -0.0708 0.1339  329 HOH A O     
10652 O  O     . HOH K .   ? 0.6276 0.5025 0.6607 -0.0302 0.1667  -0.0983 330 HOH A O     
10653 O  O     . HOH K .   ? 0.4108 0.3420 0.4871 0.0350  0.0424  0.0607  331 HOH A O     
10654 O  O     . HOH K .   ? 0.4374 0.4073 0.4021 -0.0645 0.0637  -0.0559 332 HOH A O     
10655 O  O     . HOH K .   ? 0.2057 0.2480 0.3015 0.0163  0.0128  0.0229  333 HOH A O     
10656 O  O     . HOH K .   ? 0.4049 0.3862 0.4299 0.0143  0.0581  -0.0062 334 HOH A O     
10657 O  O     . HOH K .   ? 0.6094 0.4986 0.7297 0.0372  0.0824  0.0283  335 HOH A O     
10658 O  O     . HOH K .   ? 0.3055 0.3032 0.3053 -0.0078 0.0432  -0.0257 336 HOH A O     
10659 O  O     . HOH K .   ? 0.2709 0.2835 0.4558 0.0656  0.0344  0.0445  337 HOH A O     
10660 O  O     . HOH K .   ? 0.2998 0.3129 0.3370 0.0392  0.0082  0.0109  338 HOH A O     
10661 O  O     . HOH K .   ? 0.5414 0.4973 0.7563 -0.0014 0.2341  -0.1160 339 HOH A O     
10662 O  O     . HOH K .   ? 0.4593 0.3838 0.5707 0.0049  0.1670  -0.0775 340 HOH A O     
10663 O  O     . HOH K .   ? 0.5177 0.4249 0.5311 -0.0315 0.1575  -0.0932 341 HOH A O     
10664 O  O     . HOH K .   ? 0.3952 0.3891 0.4163 0.0130  0.0525  -0.0104 342 HOH A O     
10665 O  O     . HOH K .   ? 0.5331 0.4521 0.5602 -0.0180 0.0950  -0.0258 343 HOH A O     
10666 O  O     . HOH K .   ? 0.4827 0.3611 0.6014 0.0303  0.1045  0.0003  344 HOH A O     
10667 O  O     . HOH K .   ? 0.4164 0.3837 0.4403 0.0047  0.0692  -0.0169 345 HOH A O     
10668 O  O     . HOH K .   ? 0.2328 0.2464 0.2869 0.0384  0.0167  0.0129  346 HOH A O     
10669 O  O     . HOH K .   ? 0.3271 0.2902 0.3590 0.0190  0.0582  0.0158  347 HOH A O     
10670 O  O     . HOH K .   ? 0.8398 0.7309 0.7595 -0.0981 0.1262  -0.1085 348 HOH A O     
10671 O  O     . HOH K .   ? 0.2990 0.3090 0.3292 0.0183  0.0217  0.0025  349 HOH A O     
10672 O  O     . HOH K .   ? 0.5212 0.5030 0.5166 -0.0165 0.0844  -0.0371 350 HOH A O     
10673 O  O     . HOH K .   ? 0.4923 0.5151 0.5740 0.0037  0.0903  -0.0174 351 HOH A O     
10674 O  O     . HOH K .   ? 0.2302 0.2363 0.2552 0.0343  0.0275  0.0045  352 HOH A O     
10675 O  O     . HOH K .   ? 0.5136 0.5248 0.5411 0.0354  -0.0044 -0.0012 353 HOH A O     
10676 O  O     . HOH K .   ? 0.3301 0.2991 0.3574 -0.0034 0.1028  -0.0438 354 HOH A O     
10677 O  O     . HOH K .   ? 0.5386 0.4910 0.5543 -0.0150 0.0806  -0.0292 355 HOH A O     
10678 O  O     . HOH K .   ? 0.5549 0.5462 0.9301 0.0758  0.1393  -0.0147 356 HOH A O     
10679 O  O     . HOH K .   ? 0.3695 0.3800 0.4079 0.0309  0.0194  0.0041  357 HOH A O     
10680 O  O     . HOH K .   ? 0.3922 0.4078 0.4754 0.0465  -0.0174 0.0651  358 HOH A O     
10681 O  O     . HOH K .   ? 0.4144 0.4552 0.7159 0.0650  0.0982  0.0075  359 HOH A O     
10682 O  O     . HOH K .   ? 0.2967 0.2981 0.3075 0.0003  0.0443  -0.0223 360 HOH A O     
10683 O  O     . HOH K .   ? 0.3158 0.3304 0.3426 0.0364  -0.0189 0.0103  361 HOH A O     
10684 O  O     . HOH K .   ? 0.5006 0.4975 0.5010 -0.0094 0.0593  -0.0189 362 HOH A O     
10685 O  O     . HOH K .   ? 0.4612 0.4753 0.4854 0.0391  -0.0005 -0.0041 363 HOH A O     
10686 O  O     . HOH K .   ? 0.2956 0.3044 0.3267 0.0286  -0.0095 0.0072  364 HOH A O     
10687 O  O     . HOH K .   ? 0.6177 0.6349 0.6326 0.0385  0.0083  -0.0052 365 HOH A O     
10688 O  O     . HOH K .   ? 0.3890 0.4205 0.4204 0.0230  0.0276  -0.0181 366 HOH A O     
10689 O  O     . HOH K .   ? 0.4072 0.4610 0.6962 0.0742  0.0146  0.0691  367 HOH A O     
10690 O  O     . HOH K .   ? 0.3688 0.3951 0.4542 0.0349  0.0214  0.0172  368 HOH A O     
10691 O  O     . HOH K .   ? 0.5905 0.4910 0.6152 -0.0295 0.1048  -0.0356 369 HOH A O     
10692 O  O     . HOH K .   ? 0.4515 0.3543 0.5240 0.0160  0.0919  0.0004  370 HOH A O     
10693 O  O     . HOH K .   ? 0.4691 0.4038 0.7151 0.0577  0.1351  -0.0236 371 HOH A O     
10694 O  O     . HOH K .   ? 0.5964 0.6118 0.6070 0.0358  -0.0117 0.0152  372 HOH A O     
10695 O  O     . HOH K .   ? 0.4861 0.4053 0.7194 0.0548  0.1372  -0.0259 373 HOH A O     
10696 O  O     . HOH K .   ? 0.4394 0.3894 0.7312 0.0307  0.2181  -0.0935 374 HOH A O     
10697 O  O     . HOH K .   ? 0.5603 0.4490 0.5601 -0.0404 0.1373  -0.0843 375 HOH A O     
10698 O  O     . HOH K .   ? 0.2706 0.2861 0.3458 0.0191  0.0634  -0.0058 376 HOH A O     
10699 O  O     . HOH K .   ? 0.4095 0.3202 0.6112 0.0511  0.1296  -0.0220 377 HOH A O     
10700 O  O     . HOH K .   ? 0.3138 0.2575 0.3612 0.0211  0.0640  0.0204  378 HOH A O     
10701 O  O     . HOH K .   ? 0.4456 0.5011 0.6048 0.0428  0.0130  0.0370  379 HOH A O     
10702 O  O     . HOH K .   ? 0.3505 0.3502 0.3407 -0.0054 0.0305  -0.0161 380 HOH A O     
10703 O  O     . HOH K .   ? 0.2397 0.2549 0.3756 0.0448  0.0627  0.0079  381 HOH A O     
10704 O  O     . HOH K .   ? 0.5019 0.3879 0.7091 0.0656  0.0746  0.0501  382 HOH A O     
10705 O  O     . HOH K .   ? 0.3434 0.3415 0.3388 -0.0039 0.0373  -0.0205 383 HOH A O     
10706 O  O     . HOH K .   ? 0.3561 0.3650 0.6481 0.0818  0.0344  0.0649  384 HOH A O     
10707 O  O     . HOH K .   ? 0.5106 0.4074 0.5534 -0.0109 0.1037  -0.0244 385 HOH A O     
10708 O  O     . HOH K .   ? 0.4217 0.4129 0.4266 -0.0156 0.0552  -0.0304 386 HOH A O     
10709 O  O     . HOH K .   ? 0.4175 0.4284 0.4237 0.0229  0.0394  0.0024  387 HOH A O     
10710 O  O     . HOH K .   ? 0.4370 0.4407 0.4557 0.0081  0.0469  -0.0172 388 HOH A O     
10711 O  O     . HOH K .   ? 0.5080 0.4634 0.4250 -0.0687 0.0996  -0.0679 389 HOH A O     
10712 O  O     . HOH K .   ? 0.5755 0.5119 0.4898 -0.0785 0.1031  -0.0819 390 HOH A O     
10713 O  O     . HOH K .   ? 0.4612 0.4748 0.5002 0.0363  -0.0249 0.0620  391 HOH A O     
10714 O  O     . HOH K .   ? 0.4868 0.5173 0.6427 0.0528  -0.0574 0.1164  392 HOH A O     
10715 O  O     . HOH K .   ? 0.5409 0.5097 0.5825 0.0291  -0.0222 0.1103  393 HOH A O     
10716 O  O     . HOH K .   ? 0.5204 0.5411 0.5853 0.0432  -0.0136 0.0457  394 HOH A O     
10717 O  O     . HOH K .   ? 0.5606 0.4743 0.5041 -0.0664 0.1436  -0.1008 395 HOH A O     
10718 O  O     . HOH K .   ? 0.4162 0.4171 0.4153 0.0003  0.0316  -0.0095 396 HOH A O     
10719 O  O     . HOH K .   ? 0.5420 0.4875 0.6827 0.0502  -0.0390 0.1523  397 HOH A O     
10720 O  O     . HOH K .   ? 0.5064 0.4331 0.4889 -0.0426 0.1481  -0.0904 398 HOH A O     
10721 O  O     . HOH K .   ? 0.4438 0.3606 0.5626 0.0465  0.0421  0.0707  399 HOH A O     
10722 O  O     . HOH K .   ? 0.3818 0.3295 0.4141 0.0171  0.0550  0.0357  400 HOH A O     
10723 O  O     . HOH K .   ? 0.5572 0.6124 0.7971 0.0604  0.0529  0.0309  401 HOH A O     
10724 O  O     . HOH K .   ? 0.5636 0.6149 0.8228 0.0634  0.0666  0.0251  402 HOH A O     
10725 O  O     . HOH K .   ? 0.4539 0.4904 0.5444 0.0339  -0.0066 0.0290  403 HOH A O     
10726 O  O     . HOH K .   ? 0.5276 0.5486 0.5334 0.0277  0.0324  -0.0055 404 HOH A O     
10727 O  O     . HOH K .   ? 0.3773 0.3889 0.4063 0.0369  -0.0126 0.0463  405 HOH A O     
10728 O  O     . HOH K .   ? 0.4654 0.4538 0.4908 -0.0147 0.1114  -0.0442 406 HOH A O     
10729 O  O     . HOH K .   ? 0.4918 0.4888 0.5085 -0.0162 0.0944  -0.0331 407 HOH A O     
10730 O  O     . HOH K .   ? 0.6035 0.5457 0.6567 0.0298  0.0103  0.0948  408 HOH A O     
10731 O  O     . HOH K .   ? 0.4130 0.3967 0.3888 -0.0213 0.0620  -0.0317 409 HOH A O     
10732 O  O     . HOH K .   ? 0.5512 0.5165 0.5423 -0.0383 0.0725  -0.0453 410 HOH A O     
10733 O  O     . HOH K .   ? 0.5040 0.5089 0.4805 0.0170  0.0292  0.0224  411 HOH A O     
10734 O  O     . HOH K .   ? 0.4359 0.4346 0.4266 -0.0073 0.0366  -0.0118 412 HOH A O     
10735 O  O     . HOH K .   ? 0.4786 0.4791 0.4761 -0.0083 0.0449  -0.0113 413 HOH A O     
10736 O  O     . HOH K .   ? 0.6180 0.5850 0.6614 0.0264  -0.0364 0.1277  414 HOH A O     
10737 O  O     . HOH K .   ? 0.5122 0.5332 0.6201 0.0513  -0.0091 0.0589  415 HOH A O     
10738 O  O     . HOH K .   ? 0.4609 0.5337 0.6235 0.0061  0.0780  0.0055  416 HOH A O     
10739 O  O     . HOH K .   ? 0.4913 0.5032 0.5261 0.0259  0.0096  0.0062  417 HOH A O     
10740 O  O     . HOH K .   ? 0.5049 0.5019 0.5244 0.0035  0.0563  -0.0150 418 HOH A O     
10741 O  O     . HOH K .   ? 0.5370 0.4810 0.4565 -0.0711 0.1023  -0.0760 419 HOH A O     
10742 O  O     . HOH K .   ? 0.4926 0.5269 0.6149 -0.0047 0.1404  -0.0400 420 HOH A O     
10743 O  O     . HOH K .   ? 0.5078 0.5727 0.6751 0.0366  0.0145  0.0359  421 HOH A O     
10744 O  O     . HOH K .   ? 0.5430 0.5711 0.5746 0.0351  0.0139  -0.0165 422 HOH A O     
10745 O  O     . HOH K .   ? 0.5798 0.5898 0.5218 0.0117  -0.0014 0.0277  423 HOH A O     
10746 O  O     . HOH K .   ? 0.6049 0.6534 0.7576 0.0512  -0.0320 0.0748  424 HOH A O     
10747 O  O     . HOH K .   ? 0.6074 0.5956 0.7375 0.0400  -0.0810 0.1654  425 HOH A O     
10748 O  O     . HOH K .   ? 0.5325 0.5907 0.7944 0.0668  0.0417  0.0428  426 HOH A O     
10749 O  O     . HOH K .   ? 0.6696 0.5733 0.8337 0.0581  0.0365  0.0873  427 HOH A O     
10750 O  O     . HOH K .   ? 0.5645 0.5286 0.5589 0.0140  0.0027  0.0889  428 HOH A O     
10751 O  O     . HOH K .   ? 0.7418 0.5774 0.9153 0.0150  0.1822  -0.0764 429 HOH A O     
10752 O  O     . HOH K .   ? 0.5735 0.5443 0.5632 -0.0267 0.1072  -0.0529 430 HOH A O     
10753 O  O     . HOH K .   ? 0.4885 0.5325 0.7845 0.0355  0.1714  -0.0486 431 HOH A O     
10754 O  O     . HOH K .   ? 0.5719 0.6143 0.6815 0.0383  -0.0059 0.0353  432 HOH A O     
10755 O  O     . HOH K .   ? 0.6949 0.5306 0.8003 -0.0034 0.1681  -0.0767 433 HOH A O     
10756 O  O     . HOH K .   ? 0.5707 0.4193 0.6704 0.0104  0.1159  -0.0098 434 HOH A O     
10757 O  O     . HOH K .   ? 0.5261 0.5549 0.6162 0.0413  -0.0463 0.0852  435 HOH A O     
10758 O  O     . HOH K .   ? 0.5555 0.5413 0.5515 -0.0359 0.0595  -0.0398 436 HOH A O     
10759 O  O     . HOH K .   ? 0.4995 0.5308 0.5331 0.0276  0.0191  -0.0174 437 HOH A O     
10760 O  O     . HOH K .   ? 0.6952 0.6308 0.7109 0.0120  0.0258  0.0862  438 HOH A O     
10761 O  O     . HOH K .   ? 0.4650 0.4617 0.4316 0.0141  0.0135  0.0443  439 HOH A O     
10762 O  O     . HOH K .   ? 0.4212 0.3910 0.4525 -0.0084 0.1178  -0.0518 440 HOH A O     
10763 O  O     . HOH K .   ? 0.3740 0.3833 0.4068 0.0319  0.0192  0.0017  441 HOH A O     
10764 O  O     . HOH K .   ? 0.5894 0.5938 0.5936 0.0077  0.0213  -0.0079 442 HOH A O     
10765 O  O     . HOH K .   ? 0.5754 0.4934 0.6291 0.0107  0.0834  0.0045  443 HOH A O     
10766 O  O     . HOH K .   ? 0.4221 0.4335 0.4556 0.0366  0.0137  0.0050  444 HOH A O     
10767 O  O     . HOH K .   ? 0.6152 0.5816 0.6136 -0.0277 0.1237  -0.0617 445 HOH A O     
10768 O  O     . HOH K .   ? 0.5218 0.5801 0.7559 0.0608  -0.0511 0.1106  446 HOH A O     
10769 O  O     . HOH K .   ? 0.5862 0.5929 0.5767 0.0184  -0.0407 0.0806  447 HOH A O     
10770 O  O     . HOH K .   ? 0.8877 0.7532 0.8168 -0.0949 0.1531  -0.1248 448 HOH A O     
10771 O  O     . HOH K .   ? 0.5041 0.4567 0.4551 -0.0784 0.0745  -0.0673 449 HOH A O     
10772 O  O     . HOH K .   ? 0.6800 0.5898 0.8120 0.0491  0.0271  0.0944  450 HOH A O     
10773 O  O     . HOH K .   ? 0.4773 0.4496 0.4586 0.0108  0.0164  0.0692  451 HOH A O     
10774 O  O     . HOH K .   ? 0.6076 0.5902 0.6097 -0.0198 0.0996  -0.0429 452 HOH A O     
10775 O  O     . HOH K .   ? 0.4882 0.5177 0.5007 0.0310  0.0293  -0.0155 453 HOH A O     
10776 O  O     . HOH K .   ? 0.5904 0.6384 0.7123 0.0410  -0.0611 0.0921  454 HOH A O     
10777 O  O     . HOH K .   ? 0.5697 0.5962 0.6354 -0.0506 0.1867  -0.0743 455 HOH A O     
10778 O  O     . HOH K .   ? 0.4494 0.3866 0.4734 0.0082  0.0571  0.0447  456 HOH A O     
10779 O  O     . HOH K .   ? 0.7104 0.6996 0.8438 -0.0273 0.2187  -0.1065 457 HOH A O     
10780 O  O     . HOH K .   ? 0.7238 0.7266 0.8802 -0.0232 0.2212  -0.1035 458 HOH A O     
10781 O  O     . HOH K .   ? 0.7989 0.6982 0.8638 0.0201  0.0472  0.0760  459 HOH A O     
10782 O  O     . HOH K .   ? 0.5475 0.4857 0.5770 0.0051  0.0689  0.0234  460 HOH A O     
10783 O  O     . HOH K .   ? 0.6195 0.6497 0.6117 0.0315  0.0251  -0.0267 461 HOH A O     
10784 O  O     . HOH K .   ? 0.3390 0.4196 0.7838 0.0889  -0.0016 0.1002  462 HOH A O     
10785 O  O     . HOH L .   ? 0.4358 0.4216 0.4074 0.0203  -0.0402 -0.0313 301 HOH B O     
10786 O  O     . HOH L .   ? 0.5690 0.4979 0.4794 -0.0911 -0.1221 0.1085  302 HOH B O     
10787 O  O     . HOH L .   ? 0.5257 0.4657 0.4424 -0.1014 -0.0720 0.0928  303 HOH B O     
10788 O  O     . HOH L .   ? 0.3920 0.4894 0.5741 -0.0169 -0.0347 0.0545  304 HOH B O     
10789 O  O     . HOH L .   ? 0.3771 0.5085 0.6106 -0.0322 -0.0357 0.0638  305 HOH B O     
10790 O  O     . HOH L .   ? 0.3650 0.3815 0.4052 0.0273  -0.0385 0.0174  306 HOH B O     
10791 O  O     . HOH L .   ? 0.4624 0.3943 0.5793 0.0555  -0.0910 -0.0038 307 HOH B O     
10792 O  O     . HOH L .   ? 0.4079 0.3795 0.3856 0.0158  -0.0527 -0.0355 308 HOH B O     
10793 O  O     . HOH L .   ? 0.5641 0.4508 0.5683 -0.0006 -0.0869 -0.0629 309 HOH B O     
10794 O  O     . HOH L .   ? 0.4649 0.4566 0.4589 0.0326  -0.0292 -0.0295 310 HOH B O     
10795 O  O     . HOH L .   ? 0.1974 0.2026 0.2386 0.0203  -0.0469 0.0146  311 HOH B O     
10796 O  O     . HOH L .   ? 0.4481 0.3352 0.4313 -0.0658 -0.1304 0.1061  312 HOH B O     
10797 O  O     . HOH L .   ? 0.2340 0.2688 0.3160 0.0094  -0.0504 0.0337  313 HOH B O     
10798 O  O     . HOH L .   ? 0.4278 0.4804 0.5418 0.0236  -0.0211 0.0375  314 HOH B O     
10799 O  O     . HOH L .   ? 0.3310 0.3345 0.3479 0.0149  -0.0103 0.0091  315 HOH B O     
10800 O  O     . HOH L .   ? 0.3918 0.4414 0.4797 0.0272  -0.0554 0.0530  316 HOH B O     
10801 O  O     . HOH L .   ? 0.2372 0.2848 0.3440 0.0200  -0.0018 0.0296  317 HOH B O     
10802 O  O     . HOH L .   ? 0.4146 0.3846 0.4745 -0.0589 -0.1259 0.0225  318 HOH B O     
10803 O  O     . HOH L .   ? 0.4009 0.3219 0.4325 0.0278  -0.0678 -0.0460 319 HOH B O     
10804 O  O     . HOH L .   ? 0.3764 0.4021 0.4379 -0.0748 -0.0200 0.0597  320 HOH B O     
10805 O  O     . HOH L .   ? 0.1771 0.2300 0.2961 -0.0180 -0.0538 0.0462  321 HOH B O     
10806 O  O     . HOH L .   ? 0.3898 0.3056 0.4218 -0.0221 -0.1072 -0.0063 322 HOH B O     
10807 O  O     . HOH L .   ? 0.4287 0.3762 0.5254 0.0406  -0.0987 0.0209  323 HOH B O     
10808 O  O     . HOH L .   ? 0.1769 0.2161 0.2557 0.0165  -0.0531 0.0360  324 HOH B O     
10809 O  O     . HOH L .   ? 0.6206 0.6017 0.5444 -0.0599 -0.0343 0.0376  325 HOH B O     
10810 O  O     . HOH L .   ? 0.3350 0.2968 0.4019 0.0251  -0.0939 0.0317  326 HOH B O     
10811 O  O     . HOH L .   ? 0.5233 0.3779 0.5798 -0.0215 -0.1241 0.0124  327 HOH B O     
10812 O  O     . HOH L .   ? 0.3783 0.3767 0.3833 0.0367  -0.0254 -0.0210 328 HOH B O     
10813 O  O     . HOH L .   ? 0.3729 0.3907 0.4185 -0.0127 -0.0955 0.0257  329 HOH B O     
10814 O  O     . HOH L .   ? 0.3047 0.2896 0.3501 0.0391  -0.0440 -0.0044 330 HOH B O     
10815 O  O     . HOH L .   ? 0.4167 0.5019 0.5827 -0.0536 -0.0445 0.0601  331 HOH B O     
10816 O  O     . HOH L .   ? 0.3332 0.3852 0.4292 -0.0335 -0.1166 0.0476  332 HOH B O     
10817 O  O     . HOH L .   ? 0.3634 0.3712 0.3804 0.0332  -0.0302 0.0024  333 HOH B O     
10818 O  O     . HOH L .   ? 0.3623 0.3123 0.3640 -0.0239 -0.1046 -0.0154 334 HOH B O     
10819 O  O     . HOH L .   ? 0.3656 0.4828 0.5718 -0.0259 0.0140  0.0458  335 HOH B O     
10820 O  O     . HOH L .   ? 0.4326 0.4191 0.3805 -0.0409 -0.0325 0.0302  336 HOH B O     
10821 O  O     . HOH L .   ? 0.5065 0.4439 0.4837 0.0078  -0.0640 -0.0571 337 HOH B O     
10822 O  O     . HOH L .   ? 0.2985 0.2970 0.3127 0.0131  -0.0259 0.0116  338 HOH B O     
10823 O  O     . HOH L .   ? 0.3864 0.4066 0.4573 -0.0401 -0.1173 0.0332  339 HOH B O     
10824 O  O     . HOH L .   ? 0.3952 0.3729 0.3648 -0.0840 -0.0316 0.0670  340 HOH B O     
10825 O  O     . HOH L .   ? 0.3802 0.3824 0.3884 0.0332  -0.0312 -0.0074 341 HOH B O     
10826 O  O     . HOH L .   ? 0.6087 0.4973 0.6125 -0.0148 -0.1005 -0.0488 342 HOH B O     
10827 O  O     . HOH L .   ? 0.3554 0.2978 0.4297 0.0520  -0.0593 -0.0356 343 HOH B O     
10828 O  O     . HOH L .   ? 0.5148 0.4302 0.5867 0.0504  -0.0599 -0.0591 344 HOH B O     
10829 O  O     . HOH L .   ? 0.3847 0.4196 0.4074 -0.0543 0.0488  0.0190  345 HOH B O     
10830 O  O     . HOH L .   ? 0.2680 0.2755 0.2897 0.0133  0.0007  0.0093  346 HOH B O     
10831 O  O     . HOH L .   ? 0.5223 0.4469 0.5061 0.0198  -0.0447 -0.0871 347 HOH B O     
10832 O  O     . HOH L .   ? 0.2590 0.3423 0.4012 -0.0401 0.0101  0.0438  348 HOH B O     
10833 O  O     . HOH L .   ? 0.2527 0.2310 0.2909 0.0042  -0.0725 0.0103  349 HOH B O     
10834 O  O     . HOH L .   ? 0.2456 0.2306 0.2694 0.0139  -0.0513 0.0203  350 HOH B O     
10835 O  O     . HOH L .   ? 0.3663 0.2668 0.4377 0.0093  -0.1336 0.0609  351 HOH B O     
10836 O  O     . HOH L .   ? 0.2615 0.3234 0.3837 0.0164  -0.0464 0.0468  352 HOH B O     
10837 O  O     . HOH L .   ? 0.3912 0.3981 0.3736 0.0105  -0.0616 0.0062  353 HOH B O     
10838 O  O     . HOH L .   ? 0.4159 0.4134 0.3963 -0.0039 -0.0814 0.0008  354 HOH B O     
10839 O  O     . HOH L .   ? 0.2801 0.2495 0.3206 0.0265  -0.0575 0.0086  355 HOH B O     
10840 O  O     . HOH L .   ? 0.3317 0.2995 0.3915 0.0522  -0.0432 -0.0367 356 HOH B O     
10841 O  O     . HOH L .   ? 0.4890 0.4985 0.5155 0.0230  0.0065  0.0044  357 HOH B O     
10842 O  O     . HOH L .   ? 0.5109 0.4225 0.5057 -0.0083 -0.0907 -0.0468 358 HOH B O     
10843 O  O     . HOH L .   ? 0.2395 0.2275 0.2743 0.0306  -0.0403 0.0042  359 HOH B O     
10844 O  O     . HOH L .   ? 0.2862 0.3608 0.4178 0.0086  -0.0742 0.0592  360 HOH B O     
10845 O  O     . HOH L .   ? 0.3727 0.3094 0.4066 -0.0307 -0.1101 0.0016  361 HOH B O     
10846 O  O     . HOH L .   ? 0.4153 0.4027 0.3866 -0.0767 -0.0195 0.0575  362 HOH B O     
10847 O  O     . HOH L .   ? 0.5420 0.4788 0.5482 0.0344  -0.0329 -0.0870 363 HOH B O     
10848 O  O     . HOH L .   ? 0.4126 0.4191 0.4439 -0.0802 -0.0245 0.0634  364 HOH B O     
10849 O  O     . HOH L .   ? 0.2354 0.2561 0.2987 -0.0035 -0.0774 0.0289  365 HOH B O     
10850 O  O     . HOH L .   ? 0.4456 0.3275 0.5129 0.0005  -0.1423 0.0696  366 HOH B O     
10851 O  O     . HOH L .   ? 0.5282 0.4035 0.6122 0.0458  -0.0759 -0.0643 367 HOH B O     
10852 O  O     . HOH L .   ? 0.4473 0.3009 0.5326 0.0256  -0.1082 -0.0194 368 HOH B O     
10853 O  O     . HOH L .   ? 0.3436 0.3802 0.4447 -0.0500 -0.0436 0.0538  369 HOH B O     
10854 O  O     . HOH L .   ? 0.3525 0.3359 0.2807 -0.0771 -0.0119 0.0449  370 HOH B O     
10855 O  O     . HOH L .   ? 0.5417 0.5652 0.5910 -0.0137 0.0842  -0.0151 371 HOH B O     
10856 O  O     . HOH L .   ? 0.3844 0.3840 0.3612 -0.0165 0.0108  0.0027  372 HOH B O     
10857 O  O     . HOH L .   ? 0.3496 0.3029 0.4050 0.0494  -0.0480 -0.0432 373 HOH B O     
10858 O  O     . HOH L .   ? 0.3123 0.2338 0.3777 0.0396  -0.0745 -0.0254 374 HOH B O     
10859 O  O     . HOH L .   ? 0.2180 0.2277 0.2546 0.0276  -0.0151 0.0111  375 HOH B O     
10860 O  O     . HOH L .   ? 0.4026 0.3686 0.4236 -0.0658 -0.0613 0.0671  376 HOH B O     
10861 O  O     . HOH L .   ? 0.4077 0.4242 0.4387 0.0328  -0.0291 0.0150  377 HOH B O     
10862 O  O     . HOH L .   ? 0.3876 0.3830 0.3582 -0.0212 -0.0179 0.0159  378 HOH B O     
10863 O  O     . HOH L .   ? 0.3725 0.3607 0.3002 -0.0581 -0.0060 0.0238  379 HOH B O     
10864 O  O     . HOH L .   ? 0.5061 0.3700 0.5981 0.0383  -0.0966 -0.0347 380 HOH B O     
10865 O  O     . HOH L .   ? 0.4093 0.4410 0.4699 0.0341  -0.0327 0.0362  381 HOH B O     
10866 O  O     . HOH L .   ? 0.2481 0.3155 0.3841 -0.0122 -0.0351 0.0464  382 HOH B O     
10867 O  O     . HOH L .   ? 0.2237 0.2221 0.2517 0.0282  -0.0418 0.0034  383 HOH B O     
10868 O  O     . HOH L .   ? 0.4862 0.3744 0.4718 -0.0787 -0.1188 0.1037  384 HOH B O     
10869 O  O     . HOH L .   ? 0.4492 0.4512 0.4369 -0.0138 -0.0958 0.0080  385 HOH B O     
10870 O  O     . HOH L .   ? 0.3539 0.3678 0.3693 0.0369  -0.0153 0.0067  386 HOH B O     
10871 O  O     . HOH L .   ? 0.3645 0.4032 0.3929 -0.0770 0.0323  0.0390  387 HOH B O     
10872 O  O     . HOH L .   ? 0.3864 0.4274 0.4365 0.0154  -0.0723 0.0468  388 HOH B O     
10873 O  O     . HOH L .   ? 0.3251 0.3664 0.4202 0.0275  -0.0139 0.0311  389 HOH B O     
10874 O  O     . HOH L .   ? 0.5219 0.5254 0.5226 0.0379  -0.0163 -0.0254 390 HOH B O     
10875 O  O     . HOH L .   ? 0.4721 0.4561 0.5376 0.0570  -0.0314 -0.0421 391 HOH B O     
10876 O  O     . HOH L .   ? 0.4028 0.3162 0.3699 -0.0848 -0.0982 0.0989  392 HOH B O     
10877 O  O     . HOH L .   ? 0.5281 0.5159 0.5020 -0.0323 -0.0779 0.0449  393 HOH B O     
10878 O  O     . HOH L .   ? 0.4569 0.4512 0.4878 0.0031  -0.0797 0.0332  394 HOH B O     
10879 O  O     . HOH L .   ? 0.3507 0.3955 0.4517 -0.0399 -0.1140 0.0454  395 HOH B O     
10880 O  O     . HOH L .   ? 0.1930 0.2358 0.3044 -0.0268 -0.0693 0.0463  396 HOH B O     
10881 O  O     . HOH L .   ? 0.3829 0.3180 0.3105 -0.0869 -0.0852 0.0920  397 HOH B O     
10882 O  O     . HOH L .   ? 0.4335 0.3529 0.4227 -0.0771 -0.0926 0.0890  398 HOH B O     
10883 O  O     . HOH L .   ? 0.3268 0.3224 0.2715 -0.0458 0.0233  0.0041  399 HOH B O     
10884 O  O     . HOH L .   ? 0.3088 0.3449 0.3787 -0.0393 -0.0052 0.0416  400 HOH B O     
10885 O  O     . HOH L .   ? 0.4385 0.3893 0.4983 0.0542  -0.0392 -0.0615 401 HOH B O     
10886 O  O     . HOH L .   ? 0.4240 0.3443 0.5369 0.0342  -0.1319 0.0455  402 HOH B O     
10887 O  O     . HOH L .   ? 0.3915 0.3561 0.4616 0.0516  -0.0529 -0.0247 403 HOH B O     
10888 O  O     . HOH L .   ? 0.6250 0.5444 0.5894 -0.0047 -0.0731 -0.0684 404 HOH B O     
10889 O  O     . HOH L .   ? 0.4963 0.3293 0.5641 -0.0179 -0.1504 0.0673  405 HOH B O     
10890 O  O     . HOH L .   ? 0.4119 0.3107 0.4961 0.0422  -0.0863 -0.0248 406 HOH B O     
10891 O  O     . HOH L .   ? 0.3169 0.3819 0.4525 -0.0547 -0.0374 0.0570  407 HOH B O     
10892 O  O     . HOH L .   ? 0.3894 0.3851 0.4095 0.0113  -0.0470 0.0173  408 HOH B O     
10893 O  O     . HOH L .   ? 0.5540 0.4141 0.5956 -0.0420 -0.1317 0.0691  409 HOH B O     
10894 O  O     . HOH L .   ? 0.5743 0.5765 0.6766 -0.0803 -0.1263 0.0453  410 HOH B O     
10895 O  O     . HOH L .   ? 0.4392 0.4373 0.4742 0.0322  -0.0325 0.0020  411 HOH B O     
10896 O  O     . HOH L .   ? 0.3868 0.3868 0.3622 -0.0222 0.0268  -0.0014 412 HOH B O     
10897 O  O     . HOH L .   ? 0.4576 0.5347 0.5729 -0.0730 0.0185  0.0498  413 HOH B O     
10898 O  O     . HOH L .   ? 0.2674 0.3487 0.4261 0.0165  -0.0467 0.0559  414 HOH B O     
10899 O  O     . HOH L .   ? 0.5420 0.4010 0.5825 -0.0182 -0.1166 -0.0221 415 HOH B O     
10900 O  O     . HOH L .   ? 0.5208 0.4842 0.5375 0.0418  -0.0280 -0.0660 416 HOH B O     
10901 O  O     . HOH L .   ? 0.3612 0.3707 0.3872 0.0181  0.0122  0.0046  417 HOH B O     
10902 O  O     . HOH L .   ? 0.4995 0.5102 0.5464 0.0420  -0.0231 -0.0113 418 HOH B O     
10903 O  O     . HOH L .   ? 0.5444 0.5300 0.5410 0.0359  -0.0239 -0.0457 419 HOH B O     
10904 O  O     . HOH L .   ? 0.5416 0.4455 0.6855 0.0564  -0.1162 0.0100  420 HOH B O     
10905 O  O     . HOH L .   ? 0.4115 0.4385 0.4636 -0.0234 -0.1094 0.0320  421 HOH B O     
10906 O  O     . HOH L .   ? 0.5807 0.4148 0.7004 0.0271  -0.1426 0.0286  422 HOH B O     
10907 O  O     . HOH L .   ? 0.4415 0.4213 0.4116 0.0170  -0.0458 -0.0342 423 HOH B O     
10908 O  O     . HOH L .   ? 0.4570 0.4743 0.4535 -0.0005 -0.0830 0.0214  424 HOH B O     
10909 O  O     . HOH L .   ? 0.4524 0.5136 0.5797 0.0246  -0.0327 0.0454  425 HOH B O     
10910 O  O     . HOH L .   ? 0.3936 0.4289 0.4229 0.0063  -0.0826 0.0411  426 HOH B O     
10911 O  O     . HOH L .   ? 0.3775 0.3872 0.4048 -0.0015 -0.0043 0.0202  427 HOH B O     
10912 O  O     . HOH L .   ? 0.6232 0.6326 0.6311 0.0333  -0.0269 0.0009  428 HOH B O     
10913 O  O     . HOH L .   ? 0.4668 0.4593 0.5046 0.0356  -0.0365 -0.0008 429 HOH B O     
10914 O  O     . HOH L .   ? 0.5560 0.5513 0.6461 -0.0657 -0.0881 0.0546  430 HOH B O     
10915 O  O     . HOH L .   ? 0.4678 0.4178 0.4840 -0.0342 -0.1140 -0.0062 431 HOH B O     
10916 O  O     . HOH L .   ? 0.5999 0.4200 0.7149 0.0175  -0.1498 0.0360  432 HOH B O     
10917 O  O     . HOH L .   ? 0.4295 0.4306 0.4145 -0.0199 0.0449  -0.0093 433 HOH B O     
10918 O  O     . HOH L .   ? 0.4120 0.3848 0.4980 0.0355  -0.0903 0.0226  434 HOH B O     
10919 O  O     . HOH L .   ? 0.4555 0.3879 0.5727 0.0419  -0.1187 0.0317  435 HOH B O     
10920 O  O     . HOH L .   ? 0.5887 0.5862 0.6139 0.0090  -0.0580 0.0212  436 HOH B O     
10921 O  O     . HOH L .   ? 0.5040 0.4696 0.5096 -0.0767 -0.0561 0.0727  437 HOH B O     
10922 O  O     . HOH L .   ? 0.6026 0.6066 0.6153 0.0434  -0.0107 -0.0370 438 HOH B O     
10923 O  O     . HOH L .   ? 0.4912 0.4828 0.5658 0.0510  -0.0460 -0.0146 439 HOH B O     
10924 O  O     . HOH L .   ? 0.5206 0.6459 0.7470 -0.0186 -0.0069 0.0536  440 HOH B O     
10925 O  O     . HOH L .   ? 0.3708 0.2952 0.4426 0.0481  -0.0656 -0.0407 441 HOH B O     
10926 O  O     . HOH L .   ? 0.4309 0.4349 0.4585 0.0289  -0.0203 0.0024  442 HOH B O     
10927 O  O     . HOH L .   ? 0.5915 0.5260 0.5609 -0.0103 -0.0836 -0.0478 443 HOH B O     
10928 O  O     . HOH L .   ? 0.4106 0.4187 0.4477 0.0260  -0.0399 0.0124  444 HOH B O     
10929 O  O     . HOH L .   ? 0.4644 0.4637 0.4410 -0.0166 -0.0217 0.0127  445 HOH B O     
10930 O  O     . HOH L .   ? 0.4459 0.4376 0.3909 -0.0405 -0.0140 0.0181  446 HOH B O     
10931 O  O     . HOH L .   ? 0.5429 0.5254 0.6377 0.0341  -0.0970 0.0271  447 HOH B O     
10932 O  O     . HOH L .   ? 0.3777 0.3834 0.4023 0.0252  -0.0118 0.0052  448 HOH B O     
10933 O  O     . HOH L .   ? 0.5192 0.4051 0.5536 -0.0262 -0.1154 -0.0126 449 HOH B O     
10934 O  O     . HOH L .   ? 0.4800 0.4224 0.3949 -0.0887 -0.0806 0.0876  450 HOH B O     
10935 O  O     . HOH L .   ? 0.4787 0.4495 0.5668 0.0584  -0.0518 -0.0280 451 HOH B O     
10936 O  O     . HOH L .   ? 0.3147 0.4316 0.5310 -0.0085 -0.0349 0.0598  452 HOH B O     
10937 O  O     . HOH L .   ? 0.5404 0.5955 0.6652 0.0236  0.0016  0.0321  453 HOH B O     
10938 O  O     . HOH L .   ? 0.4379 0.3770 0.5548 0.0619  -0.0761 -0.0220 454 HOH B O     
10939 O  O     . HOH L .   ? 0.4755 0.3651 0.5817 0.0530  -0.0855 -0.0369 455 HOH B O     
10940 O  O     . HOH L .   ? 0.4997 0.5141 0.5789 -0.0629 -0.0503 0.0591  456 HOH B O     
10941 O  O     . HOH L .   ? 0.5301 0.4829 0.5210 -0.0342 -0.1230 0.0792  457 HOH B O     
10942 O  O     . HOH L .   ? 0.4547 0.5499 0.6091 -0.0546 0.0161  0.0473  458 HOH B O     
10943 O  O     . HOH L .   ? 0.6820 0.5766 0.6978 -0.0342 -0.1177 -0.0255 459 HOH B O     
10944 O  O     . HOH L .   ? 0.5533 0.5992 0.6158 -0.0241 -0.1175 0.0445  460 HOH B O     
10945 O  O     . HOH L .   ? 0.5295 0.4183 0.6480 0.0368  -0.1325 0.0359  461 HOH B O     
10946 O  O     . HOH L .   ? 0.4727 0.5304 0.5765 0.0280  -0.0628 0.0646  462 HOH B O     
10947 O  O     . HOH L .   ? 0.6848 0.5717 0.7849 0.0585  -0.0630 -0.0772 463 HOH B O     
10948 O  O     . HOH L .   ? 0.5852 0.5036 0.7272 0.0532  -0.1194 0.0202  464 HOH B O     
10949 O  O     . HOH L .   ? 0.6344 0.6276 0.6678 0.0253  -0.0425 0.0095  465 HOH B O     
10950 O  O     . HOH L .   ? 0.4653 0.3688 0.5628 0.0553  -0.0729 -0.0478 466 HOH B O     
10951 O  O     . HOH L .   ? 0.5122 0.5157 0.5332 0.0208  -0.0219 0.0055  467 HOH B O     
10952 O  O     . HOH L .   ? 0.4585 0.5516 0.6489 0.0245  -0.0378 0.0609  468 HOH B O     
10953 O  O     . HOH L .   ? 0.6162 0.4812 0.6878 -0.0073 -0.1588 0.0837  469 HOH B O     
10954 O  O     . HOH L .   ? 0.6392 0.7034 0.8041 -0.0978 -0.1277 0.0654  470 HOH B O     
10955 O  O     . HOH L .   ? 0.6118 0.6033 0.5634 -0.0247 -0.1003 -0.0043 471 HOH B O     
10956 O  O     . HOH L .   ? 0.6214 0.6950 0.7471 -0.0827 -0.0058 0.0607  472 HOH B O     
10957 O  O     . HOH L .   ? 0.4467 0.3472 0.5493 0.0270  -0.1359 0.0499  473 HOH B O     
10958 O  O     . HOH L .   ? 0.4808 0.5589 0.6471 0.0282  -0.0282 0.0531  474 HOH B O     
10959 O  O     . HOH L .   ? 0.5305 0.5527 0.5322 -0.0977 0.0155  0.0541  475 HOH B O     
10960 O  O     . HOH L .   ? 0.5570 0.5547 0.5214 -0.0278 -0.0323 0.0182  476 HOH B O     
10961 O  O     . HOH L .   ? 0.5777 0.5255 0.5685 -0.0852 -0.0680 0.0826  477 HOH B O     
10962 O  O     . HOH L .   ? 0.4722 0.4951 0.5102 0.0342  -0.0283 0.0257  478 HOH B O     
10963 O  O     . HOH L .   ? 0.5198 0.5475 0.6189 -0.0622 -0.0539 0.0586  479 HOH B O     
10964 O  O     . HOH L .   ? 0.5739 0.6392 0.7261 -0.0686 -0.0699 0.0632  480 HOH B O     
10965 O  O     . HOH L .   ? 0.3725 0.4893 0.5832 -0.0444 -0.0782 0.0692  481 HOH B O     
10966 O  O     . HOH L .   ? 0.7651 0.7065 0.9050 0.0207  -0.1657 0.0760  482 HOH B O     
10967 O  O     . HOH L .   ? 0.6163 0.6266 0.7127 -0.0672 -0.0750 0.0587  483 HOH B O     
10968 O  O     . HOH L .   ? 0.4620 0.4865 0.4903 0.0272  -0.0442 0.0290  484 HOH B O     
10969 O  O     . HOH L .   ? 0.7373 0.8123 0.9045 -0.0832 -0.0699 0.0687  485 HOH B O     
10970 O  O     . HOH L .   ? 0.7072 0.6839 0.7236 0.0458  -0.0030 -0.0892 486 HOH B O     
10971 O  O     . HOH L .   ? 0.7615 0.6981 0.7828 -0.1094 -0.0846 0.0933  487 HOH B O     
10972 O  O     . HOH L .   ? 0.5343 0.3925 0.6334 -0.0029 -0.1740 0.0886  488 HOH B O     
10973 O  O     . HOH L .   ? 0.6502 0.6650 0.6169 0.0165  -0.0402 0.0199  489 HOH B O     
10974 O  O     . HOH L .   ? 0.7628 0.5835 0.9763 0.0646  -0.1352 -0.0116 490 HOH B O     
10975 O  O     . HOH L .   ? 0.5682 0.7681 0.8834 -0.0891 0.0148  0.0685  491 HOH B O     
10976 O  O     . HOH M .   ? 0.7116 0.8845 0.8992 -0.0401 -0.0269 -0.0255 301 HOH D O     
10977 O  O     . HOH M .   ? 0.4275 0.6598 0.6052 -0.1762 -0.1260 -0.0049 302 HOH D O     
10978 O  O     . HOH M .   ? 0.7170 0.7276 0.4733 -0.2353 -0.1465 0.0610  303 HOH D O     
10979 O  O     . HOH M .   ? 0.4016 0.4430 0.4422 0.0190  0.0260  -0.0219 304 HOH D O     
10980 O  O     . HOH M .   ? 0.5650 0.5762 0.4797 -0.1205 -0.1726 0.0959  305 HOH D O     
10981 O  O     . HOH M .   ? 0.5026 0.6334 0.5749 -0.1561 -0.0390 -0.0388 306 HOH D O     
10982 O  O     . HOH M .   ? 0.4186 0.6468 0.6906 -0.0780 -0.2070 0.0631  307 HOH D O     
10983 O  O     . HOH M .   ? 0.5818 0.6145 0.3615 -0.2427 -0.1442 0.0380  308 HOH D O     
10984 O  O     . HOH M .   ? 0.4354 0.4403 0.4343 -0.0534 0.0483  -0.0425 309 HOH D O     
10985 O  O     . HOH M .   ? 0.3317 0.4468 0.4463 -0.0194 0.0289  -0.0365 310 HOH D O     
10986 O  O     . HOH M .   ? 0.3358 0.5883 0.6169 -0.0735 -0.0494 -0.0232 311 HOH D O     
10987 O  O     . HOH M .   ? 0.2772 0.5237 0.5536 -0.0714 -0.0762 -0.0117 312 HOH D O     
10988 O  O     . HOH M .   ? 0.5438 0.5623 0.3256 -0.2193 -0.1004 0.0077  313 HOH D O     
10989 O  O     . HOH M .   ? 0.5800 0.5484 0.3031 -0.2416 -0.0134 -0.0589 314 HOH D O     
10990 O  O     . HOH M .   ? 0.5951 0.5792 0.3456 -0.2594 -0.0316 -0.0649 315 HOH D O     
10991 O  O     . HOH M .   ? 0.3228 0.3919 0.4357 0.0315  -0.0304 -0.0162 316 HOH D O     
10992 O  O     . HOH M .   ? 0.3755 0.4003 0.3077 -0.0859 -0.0817 0.0260  317 HOH D O     
10993 O  O     . HOH M .   ? 0.5703 0.5739 0.3108 -0.2451 -0.0823 -0.0080 318 HOH D O     
10994 O  O     . HOH M .   ? 0.3450 0.3666 0.3426 -0.0191 -0.0392 0.0075  319 HOH D O     
10995 O  O     . HOH M .   ? 0.3148 0.4080 0.4019 -0.0251 0.0406  -0.0352 320 HOH D O     
10996 O  O     . HOH M .   ? 0.3492 0.4058 0.3720 -0.0884 0.0135  -0.0421 321 HOH D O     
10997 O  O     . HOH M .   ? 0.3841 0.3943 0.3873 0.0038  0.0156  -0.0122 322 HOH D O     
10998 O  O     . HOH M .   ? 0.3402 0.5518 0.5110 -0.1341 -0.1701 0.0305  323 HOH D O     
10999 O  O     . HOH M .   ? 0.5415 0.4743 0.4129 -0.1266 0.0813  -0.0932 324 HOH D O     
11000 O  O     . HOH M .   ? 0.3970 0.3774 0.3448 -0.0451 0.0525  -0.0403 325 HOH D O     
11001 O  O     . HOH M .   ? 0.4935 0.4986 0.4447 -0.1272 0.0266  -0.0626 326 HOH D O     
11002 O  O     . HOH M .   ? 0.4538 0.4860 0.3798 -0.1662 -0.0181 -0.0545 327 HOH D O     
11003 O  O     . HOH M .   ? 0.3607 0.3527 0.3341 -0.0196 0.0423  -0.0234 328 HOH D O     
11004 O  O     . HOH M .   ? 0.3509 0.4889 0.6109 0.0181  -0.1336 0.0293  329 HOH D O     
11005 O  O     . HOH M .   ? 0.3172 0.5032 0.5961 -0.0236 -0.1724 0.0502  330 HOH D O     
11006 O  O     . HOH M .   ? 0.5200 0.5140 0.3200 -0.1712 -0.0369 -0.0203 331 HOH D O     
11007 O  O     . HOH M .   ? 0.4225 0.4360 0.3807 -0.0450 -0.0382 0.0088  332 HOH D O     
11008 O  O     . HOH M .   ? 0.4341 0.6336 0.7760 0.0372  -0.0711 -0.0169 333 HOH D O     
11009 O  O     . HOH M .   ? 0.4154 0.4672 0.2881 -0.1794 -0.1151 0.0128  334 HOH D O     
11010 O  O     . HOH M .   ? 0.2871 0.3278 0.3281 -0.0006 -0.0388 0.0004  335 HOH D O     
11011 O  O     . HOH M .   ? 0.5837 0.5878 0.3586 -0.2023 -0.0747 -0.0033 336 HOH D O     
11012 O  O     . HOH M .   ? 0.4668 0.4309 0.3107 -0.1769 0.0299  -0.0845 337 HOH D O     
11013 O  O     . HOH M .   ? 0.4530 0.4961 0.2980 -0.1912 -0.1365 0.0356  338 HOH D O     
11014 O  O     . HOH M .   ? 0.2914 0.2833 0.2858 -0.0187 0.0499  -0.0321 339 HOH D O     
11015 O  O     . HOH M .   ? 0.3945 0.4430 0.2678 -0.2014 -0.0788 -0.0268 340 HOH D O     
11016 O  O     . HOH M .   ? 0.4308 0.3910 0.3434 -0.0706 0.0804  -0.0609 341 HOH D O     
11017 O  O     . HOH M .   ? 0.3510 0.3597 0.3424 -0.0054 0.0028  -0.0064 342 HOH D O     
11018 O  O     . HOH M .   ? 0.4662 0.4205 0.3977 -0.0960 0.0684  -0.0727 343 HOH D O     
11019 O  O     . HOH M .   ? 0.4195 0.4837 0.5080 -0.0125 -0.1017 0.0285  344 HOH D O     
11020 O  O     . HOH M .   ? 0.3968 0.4685 0.3633 -0.1203 -0.1378 0.0404  345 HOH D O     
11021 O  O     . HOH M .   ? 0.3143 0.3731 0.3589 -0.0346 -0.0928 0.0254  346 HOH D O     
11022 O  O     . HOH M .   ? 0.6034 0.6249 0.6287 -0.0396 0.0540  -0.0344 347 HOH D O     
11023 O  O     . HOH M .   ? 0.3545 0.5266 0.6798 0.0201  -0.1473 0.0348  348 HOH D O     
11024 O  O     . HOH M .   ? 0.5924 0.6910 0.4868 -0.2345 -0.1873 0.0449  349 HOH D O     
11025 O  O     . HOH M .   ? 0.4693 0.4567 0.4012 -0.0488 0.0423  -0.0237 350 HOH D O     
11026 O  O     . HOH M .   ? 0.5095 0.5451 0.5960 0.0386  -0.0378 -0.0094 351 HOH D O     
11027 O  O     . HOH M .   ? 0.2848 0.5276 0.6348 -0.0024 -0.0825 -0.0091 352 HOH D O     
11028 O  O     . HOH M .   ? 0.3337 0.4171 0.4185 -0.0246 -0.0804 0.0123  353 HOH D O     
11029 O  O     . HOH M .   ? 0.3263 0.4446 0.4784 0.0221  0.0040  -0.0364 354 HOH D O     
11030 O  O     . HOH M .   ? 0.4942 0.4927 0.4946 -0.0264 0.0494  -0.0341 355 HOH D O     
11031 O  O     . HOH M .   ? 0.3706 0.5901 0.7513 0.0224  -0.1257 0.0166  356 HOH D O     
11032 O  O     . HOH M .   ? 0.4687 0.4245 0.3858 -0.0828 0.0709  -0.0678 357 HOH D O     
11033 O  O     . HOH M .   ? 0.3295 0.5645 0.6939 0.0096  -0.0988 -0.0008 358 HOH D O     
11034 O  O     . HOH M .   ? 0.3251 0.4126 0.4051 -0.0424 0.0411  -0.0361 359 HOH D O     
11035 O  O     . HOH M .   ? 0.3887 0.4821 0.3274 -0.1791 -0.1562 0.0331  360 HOH D O     
11036 O  O     . HOH M .   ? 0.3954 0.4668 0.3903 -0.1017 -0.1548 0.0565  361 HOH D O     
11037 O  O     . HOH M .   ? 0.3738 0.3845 0.3883 -0.0057 0.0421  -0.0246 362 HOH D O     
11038 O  O     . HOH M .   ? 0.3821 0.3891 0.3118 -0.0624 -0.0282 0.0029  363 HOH D O     
11039 O  O     . HOH M .   ? 0.3548 0.4167 0.4104 -0.0404 0.0436  -0.0346 364 HOH D O     
11040 O  O     . HOH M .   ? 0.2818 0.4486 0.5412 0.0007  -0.1193 0.0189  365 HOH D O     
11041 O  O     . HOH M .   ? 0.4140 0.5068 0.5820 0.0408  -0.0396 -0.0200 366 HOH D O     
11042 O  O     . HOH M .   ? 0.4075 0.5296 0.6437 0.0446  -0.0639 -0.0135 367 HOH D O     
11043 O  O     . HOH M .   ? 0.3187 0.5966 0.6430 -0.0801 -0.1347 0.0137  368 HOH D O     
11044 O  O     . HOH M .   ? 0.3427 0.4672 0.3947 -0.1159 -0.1447 0.0315  369 HOH D O     
11045 O  O     . HOH M .   ? 0.3564 0.6098 0.7042 -0.0024 -0.0382 -0.0312 370 HOH D O     
11046 O  O     . HOH M .   ? 0.3878 0.4606 0.2951 -0.2045 -0.0952 -0.0211 371 HOH D O     
11047 O  O     . HOH M .   ? 0.4079 0.6056 0.5708 -0.1287 -0.2136 0.0642  372 HOH D O     
11048 O  O     . HOH M .   ? 0.3415 0.5693 0.5591 -0.1115 -0.1577 0.0260  373 HOH D O     
11049 O  O     . HOH M .   ? 0.4104 0.4272 0.2412 -0.2040 -0.0500 -0.0421 374 HOH D O     
11050 O  O     . HOH M .   ? 0.5233 0.5855 0.3437 -0.2552 -0.1499 0.0196  375 HOH D O     
11051 O  O     . HOH M .   ? 0.5342 0.5508 0.4265 -0.1932 -0.0155 -0.0660 376 HOH D O     
11052 O  O     . HOH M .   ? 0.3948 0.3923 0.3086 -0.1214 0.0172  -0.0559 377 HOH D O     
11053 O  O     . HOH M .   ? 0.3350 0.4072 0.3950 -0.0567 0.0317  -0.0373 378 HOH D O     
11054 O  O     . HOH M .   ? 0.6027 0.6682 0.5020 -0.1920 -0.2090 0.0924  379 HOH D O     
11055 O  O     . HOH M .   ? 0.3880 0.3873 0.3767 -0.0501 0.0465  -0.0424 380 HOH D O     
11056 O  O     . HOH M .   ? 0.3895 0.5535 0.5651 -0.0319 0.0098  -0.0371 381 HOH D O     
11057 O  O     . HOH M .   ? 0.4363 0.4353 0.3978 -0.0262 0.0129  -0.0081 382 HOH D O     
11058 O  O     . HOH M .   ? 0.4916 0.5191 0.5202 -0.0104 0.0454  -0.0260 383 HOH D O     
11059 O  O     . HOH M .   ? 0.4792 0.7137 0.6580 -0.1718 -0.1517 0.0087  384 HOH D O     
11060 O  O     . HOH M .   ? 0.5678 0.5682 0.4630 -0.0864 -0.0472 0.0174  385 HOH D O     
11061 O  O     . HOH M .   ? 0.4011 0.4690 0.4778 0.0271  0.0181  -0.0310 386 HOH D O     
11062 O  O     . HOH M .   ? 0.3648 0.4828 0.4855 -0.0070 0.0335  -0.0389 387 HOH D O     
11063 O  O     . HOH M .   ? 0.5243 0.6342 0.4607 -0.2105 -0.2022 0.0608  388 HOH D O     
11064 O  O     . HOH M .   ? 0.5200 0.6351 0.5359 -0.1869 -0.0683 -0.0354 389 HOH D O     
11065 O  O     . HOH M .   ? 0.4801 0.6207 0.4918 -0.2272 -0.1145 -0.0228 390 HOH D O     
11066 O  O     . HOH M .   ? 0.4596 0.4848 0.4922 0.0073  -0.0387 0.0044  391 HOH D O     
11067 O  O     . HOH M .   ? 0.3517 0.4481 0.4449 0.0008  0.0408  -0.0370 392 HOH D O     
11068 O  O     . HOH M .   ? 0.6766 0.7251 0.4742 -0.2508 -0.1589 0.0397  393 HOH D O     
11069 O  O     . HOH M .   ? 0.3816 0.5081 0.6274 0.0085  -0.1557 0.0466  394 HOH D O     
11070 O  O     . HOH M .   ? 0.2908 0.4762 0.5902 0.0147  -0.1012 0.0051  395 HOH D O     
11071 O  O     . HOH M .   ? 0.4479 0.5193 0.5193 0.0235  0.0314  -0.0341 396 HOH D O     
11072 O  O     . HOH M .   ? 0.5064 0.6159 0.6824 0.0439  -0.0095 -0.0383 397 HOH D O     
11073 O  O     . HOH M .   ? 0.5038 0.5182 0.4567 -0.0546 -0.0591 0.0206  398 HOH D O     
11074 O  O     . HOH M .   ? 0.4765 0.7247 0.7990 -0.0687 -0.2210 0.0716  399 HOH D O     
11075 O  O     . HOH M .   ? 0.7989 0.8084 0.6068 -0.1899 -0.1517 0.0748  400 HOH D O     
11076 O  O     . HOH M .   ? 0.4687 0.5174 0.5184 -0.0247 -0.0987 0.0318  401 HOH D O     
11077 O  O     . HOH M .   ? 0.3290 0.5177 0.5421 -0.0232 0.0156  -0.0423 402 HOH D O     
11078 O  O     . HOH M .   ? 0.4088 0.4720 0.5349 0.0388  -0.0425 -0.0127 403 HOH D O     
11079 O  O     . HOH M .   ? 0.4505 0.6362 0.6035 -0.1357 -0.0477 -0.0297 404 HOH D O     
11080 O  O     . HOH M .   ? 0.4638 0.5623 0.6407 0.0474  -0.0249 -0.0310 405 HOH D O     
11081 O  O     . HOH M .   ? 0.6072 0.6135 0.3690 -0.2190 -0.0883 0.0056  406 HOH D O     
11082 O  O     . HOH M .   ? 0.5081 0.5475 0.5230 -0.0786 0.0277  -0.0437 407 HOH D O     
11083 O  O     . HOH M .   ? 0.5338 0.6191 0.3892 -0.2571 -0.1695 0.0266  408 HOH D O     
11084 O  O     . HOH M .   ? 0.7795 0.7954 0.5248 -0.2590 -0.1702 0.0755  409 HOH D O     
11085 O  O     . HOH M .   ? 0.4881 0.5234 0.5255 -0.0147 -0.0789 0.0239  410 HOH D O     
11086 O  O     . HOH M .   ? 0.4714 0.7269 0.7876 -0.0733 -0.2036 0.0578  411 HOH D O     
11087 O  O     . HOH M .   ? 0.5673 0.6424 0.7648 0.0071  -0.1690 0.0647  412 HOH D O     
11088 O  O     . HOH M .   ? 0.5198 0.5425 0.5414 -0.0553 0.0506  -0.0398 413 HOH D O     
11089 O  O     . HOH M .   ? 0.5098 0.6570 0.8290 0.0552  -0.0917 -0.0039 414 HOH D O     
11090 O  O     . HOH M .   ? 0.4368 0.4460 0.4370 0.0022  -0.0075 -0.0007 415 HOH D O     
11091 O  O     . HOH M .   ? 0.4303 0.6612 0.6736 -0.0827 -0.0194 -0.0332 416 HOH D O     
11092 O  O     . HOH M .   ? 0.5566 0.6109 0.6520 0.0078  -0.0825 0.0176  417 HOH D O     
11093 O  O     . HOH M .   ? 0.7178 0.7527 0.7525 -0.0091 0.0492  -0.0253 418 HOH D O     
11094 O  O     . HOH M .   ? 0.4135 0.4189 0.4083 -0.0008 0.0164  -0.0100 419 HOH D O     
11095 O  O     . HOH M .   ? 0.7729 0.8072 0.5276 -0.2721 -0.1628 0.0486  420 HOH D O     
11096 O  O     . HOH M .   ? 0.3469 0.5491 0.6988 0.0320  -0.0945 -0.0027 421 HOH D O     
11097 O  O     . HOH M .   ? 0.5586 0.5929 0.5947 0.0340  0.0172  -0.0201 422 HOH D O     
11098 O  O     . HOH M .   ? 0.5400 0.6581 0.6707 0.0154  0.0336  -0.0444 423 HOH D O     
11099 O  O     . HOH M .   ? 0.4000 0.6344 0.5856 -0.1596 -0.1613 0.0170  424 HOH D O     
11100 O  O     . HOH M .   ? 0.5104 0.5643 0.5575 0.0026  0.0455  -0.0267 425 HOH D O     
11101 O  O     . HOH M .   ? 0.5258 0.6244 0.7152 0.0398  -0.0585 -0.0112 426 HOH D O     
11102 O  O     . HOH M .   ? 0.4368 0.5599 0.7000 0.0469  -0.0898 -0.0003 427 HOH D O     
11103 O  O     . HOH M .   ? 0.3715 0.6557 0.7177 -0.0698 -0.1525 0.0238  428 HOH D O     
11104 O  O     . HOH M .   ? 0.6105 0.7813 0.7125 -0.1548 -0.2416 0.0877  429 HOH D O     
11105 O  O     . HOH M .   ? 0.6934 0.6836 0.6982 -0.0268 0.0591  -0.0345 430 HOH D O     
11106 O  O     . HOH M .   ? 0.5542 0.6207 0.6867 -0.0442 -0.2098 0.1014  431 HOH D O     
11107 O  O     . HOH M .   ? 0.4383 0.5604 0.6158 0.0359  -0.0013 -0.0403 432 HOH D O     
11108 O  O     . HOH M .   ? 0.3441 0.3863 0.3809 0.0238  0.0325  -0.0225 433 HOH D O     
11109 O  O     . HOH M .   ? 0.5188 0.5456 0.5513 -0.0360 0.0590  -0.0313 434 HOH D O     
11110 O  O     . HOH M .   ? 0.3263 0.5834 0.5949 -0.1049 -0.1471 0.0187  435 HOH D O     
11111 O  O     . HOH M .   ? 0.5967 0.6991 0.4834 -0.2493 -0.1955 0.0468  436 HOH D O     
11112 O  O     . HOH M .   ? 0.6771 0.6454 0.3726 -0.2568 -0.0239 -0.0463 437 HOH D O     
11113 O  O     . HOH M .   ? 0.4241 0.5767 0.5937 -0.0013 0.0331  -0.0462 438 HOH D O     
11114 O  O     . HOH M .   ? 0.4736 0.7687 0.8865 -0.0128 -0.0765 -0.0147 439 HOH D O     
11115 O  O     . HOH M .   ? 0.5444 0.7561 0.6702 -0.1856 -0.1854 0.0277  440 HOH D O     
11116 O  O     . HOH M .   ? 0.4554 0.4585 0.4531 -0.0683 0.0510  -0.0475 441 HOH D O     
11117 O  O     . HOH M .   ? 0.5763 0.5694 0.5415 -0.0248 0.0389  -0.0190 442 HOH D O     
11118 O  O     . HOH M .   ? 0.5212 0.5337 0.5474 0.0260  -0.0122 -0.0027 443 HOH D O     
11119 O  O     . HOH M .   ? 0.7502 0.7958 0.5278 -0.2671 -0.1633 0.0416  444 HOH D O     
11120 O  O     . HOH M .   ? 0.4823 0.7391 0.6968 -0.1877 -0.1158 -0.0127 445 HOH D O     
11121 O  O     . HOH M .   ? 0.4897 0.5933 0.7309 0.0446  -0.1004 0.0090  446 HOH D O     
11122 O  O     . HOH M .   ? 0.4830 0.7624 0.7326 -0.1678 -0.1697 0.0157  447 HOH D O     
11123 O  O     . HOH M .   ? 0.7076 0.6561 0.4020 -0.2575 0.0134  -0.0767 448 HOH D O     
11124 O  O     . HOH M .   ? 0.6190 0.8693 0.8148 -0.1992 -0.1324 -0.0085 449 HOH D O     
11125 O  O     . HOH M .   ? 0.5456 0.5498 0.5690 -0.0303 0.0682  -0.0258 450 HOH D O     
11126 O  O     . HOH M .   ? 0.4909 0.6907 0.9055 0.0488  -0.1259 0.0159  451 HOH D O     
11127 O  O     . HOH M .   ? 0.3111 0.6253 0.7379 -0.0244 -0.0793 -0.0134 452 HOH D O     
11128 O  O     . HOH M .   ? 0.5264 0.5283 0.5031 -0.0148 -0.0053 0.0031  453 HOH D O     
11129 O  O     . HOH M .   ? 0.6109 0.9038 0.8769 -0.1716 -0.1842 0.0216  454 HOH D O     
11130 O  O     . HOH M .   ? 0.5958 0.6078 0.6239 -0.0459 0.0694  -0.0311 455 HOH D O     
11131 O  O     . HOH M .   ? 0.2666 0.5696 0.7285 0.0081  -0.0960 -0.0044 456 HOH D O     
11132 O  O     . HOH N .   ? 0.3933 0.4003 0.3702 -0.0417 0.0302  0.0119  301 HOH C O     
11133 O  O     . HOH N .   ? 0.6840 0.6561 0.4184 -0.1871 -0.0285 0.0042  302 HOH C O     
11134 O  O     . HOH N .   ? 0.6256 0.5705 0.3232 -0.2318 -0.0981 0.0959  303 HOH C O     
11135 O  O     . HOH N .   ? 0.6661 0.6745 0.4861 -0.1826 0.1402  -0.0317 304 HOH C O     
11136 O  O     . HOH N .   ? 0.8699 0.8102 0.4356 -0.3379 0.1097  -0.0587 305 HOH C O     
11137 O  O     . HOH N .   ? 0.6191 0.6087 0.5425 -0.0959 0.1596  -0.0741 306 HOH C O     
11138 O  O     . HOH N .   ? 0.8015 0.7613 0.4447 -0.2886 0.1443  -0.0702 307 HOH C O     
11139 O  O     . HOH N .   ? 0.9204 0.8544 0.4868 -0.3298 0.0083  -0.0248 308 HOH C O     
11140 O  O     . HOH N .   ? 0.8068 0.7602 0.5271 -0.1927 0.0448  -0.0521 309 HOH C O     
11141 O  O     . HOH N .   ? 0.5310 0.5007 0.3434 -0.1301 0.0425  -0.0348 310 HOH C O     
11142 O  O     . HOH N .   ? 0.4064 0.4296 0.4198 -0.0364 0.0697  -0.0047 311 HOH C O     
11143 O  O     . HOH N .   ? 0.4811 0.4634 0.3373 -0.1029 -0.0331 0.0270  312 HOH C O     
11144 O  O     . HOH N .   ? 0.7762 0.7401 0.4439 -0.2543 -0.0797 0.0456  313 HOH C O     
11145 O  O     . HOH N .   ? 0.9288 0.8669 0.6363 -0.2835 -0.2184 0.1743  314 HOH C O     
11146 O  O     . HOH N .   ? 0.5081 0.4961 0.4006 -0.0858 0.0669  -0.0213 315 HOH C O     
11147 O  O     . HOH N .   ? 0.9023 0.8372 0.4458 -0.3534 -0.0119 0.0497  316 HOH C O     
11148 O  O     . HOH N .   ? 0.7243 0.6961 0.6174 -0.1256 0.1880  -0.1046 317 HOH C O     
11149 O  O     . HOH N .   ? 0.5971 0.6096 0.5575 -0.0705 0.1024  -0.0253 318 HOH C O     
11150 O  O     . HOH N .   ? 0.9878 0.9090 0.5125 -0.3651 0.0416  -0.0443 319 HOH C O     
11151 O  O     . HOH N .   ? 0.5597 0.5435 0.3741 -0.1403 -0.0750 0.0443  320 HOH C O     
11152 O  O     . HOH N .   ? 0.5197 0.4901 0.4173 -0.0884 -0.0361 0.0557  321 HOH C O     
11153 O  O     . HOH N .   ? 0.4718 0.4588 0.2905 -0.1492 -0.0114 -0.0297 322 HOH C O     
11154 O  O     . HOH N .   ? 0.4734 0.4654 0.3951 -0.0555 -0.0081 0.0095  323 HOH C O     
11155 O  O     . HOH N .   ? 0.8671 0.7944 0.6201 -0.1849 0.0953  -0.1007 324 HOH C O     
11156 O  O     . HOH N .   ? 0.7621 0.7262 0.4465 -0.2297 -0.0272 -0.0037 325 HOH C O     
11157 O  O     . HOH N .   ? 0.4584 0.4328 0.2362 -0.1548 -0.0259 0.0172  326 HOH C O     
11158 O  O     . HOH N .   ? 0.7733 0.6952 0.6249 -0.1659 0.2247  -0.1571 327 HOH C O     
11159 O  O     . HOH N .   ? 0.7652 0.7298 0.5660 -0.1993 0.2130  -0.1261 328 HOH C O     
11160 O  O     . HOH N .   ? 0.7222 0.6819 0.4190 -0.2503 -0.1377 0.1006  329 HOH C O     
11161 O  O     . HOH N .   ? 0.7078 0.6900 0.4316 -0.2433 0.1664  -0.0711 330 HOH C O     
11162 O  O     . HOH N .   ? 0.5135 0.5000 0.3586 -0.1293 -0.1114 0.0684  331 HOH C O     
11163 O  O     . HOH N .   ? 0.5785 0.5662 0.4503 -0.1060 0.0880  -0.0296 332 HOH C O     
11164 O  O     . HOH N .   ? 0.8722 0.8062 0.4238 -0.3648 0.1720  -0.1092 333 HOH C O     
11165 O  O     . HOH N .   ? 0.4649 0.4577 0.3523 -0.0834 -0.0195 0.0055  334 HOH C O     
11166 O  O     . HOH N .   ? 0.4881 0.5044 0.4247 -0.0725 -0.0737 0.0273  335 HOH C O     
11167 O  O     . HOH N .   ? 0.6667 0.6165 0.3003 -0.2670 -0.0118 0.0069  336 HOH C O     
11168 O  O     . HOH N .   ? 0.5865 0.5460 0.4171 -0.1336 -0.1134 0.0928  337 HOH C O     
11169 O  O     . HOH N .   ? 0.6085 0.5695 0.4171 -0.1584 -0.0223 0.0719  338 HOH C O     
11170 O  O     . HOH N .   ? 0.9011 0.8193 0.4399 -0.3734 -0.0993 0.1134  339 HOH C O     
11171 O  O     . HOH N .   ? 0.3620 0.3731 0.3420 -0.0837 0.0143  0.0453  340 HOH C O     
11172 O  O     . HOH N .   ? 0.3928 0.3842 0.3275 -0.0493 -0.0001 0.0145  341 HOH C O     
11173 O  O     . HOH N .   ? 0.7061 0.6455 0.4124 -0.2294 -0.0602 0.0991  342 HOH C O     
11174 O  O     . HOH N .   ? 0.6558 0.5675 0.4717 -0.1768 -0.1672 0.1550  343 HOH C O     
11175 O  O     . HOH N .   ? 0.5597 0.5792 0.4547 -0.1290 -0.1559 0.0775  344 HOH C O     
11176 O  O     . HOH N .   ? 0.4744 0.4554 0.3983 -0.0706 -0.0189 0.0419  345 HOH C O     
11177 O  O     . HOH N .   ? 0.5397 0.5483 0.4246 -0.1061 -0.0730 0.0259  346 HOH C O     
11178 O  O     . HOH N .   ? 0.5452 0.5327 0.4028 -0.1065 -0.0504 0.0296  347 HOH C O     
11179 O  O     . HOH N .   ? 0.5892 0.6665 0.6953 -0.0466 0.0749  0.0149  348 HOH C O     
11180 O  O     . HOH N .   ? 0.8183 0.7614 0.3735 -0.3430 0.0320  0.0190  349 HOH C O     
11181 O  O     . HOH N .   ? 1.0416 0.9571 0.4878 -0.4322 0.0464  -0.0276 350 HOH C O     
11182 O  O     . HOH N .   ? 0.4814 0.5190 0.5011 -0.0559 0.0818  -0.0007 351 HOH C O     
11183 O  O     . HOH N .   ? 0.9502 0.8942 0.5938 -0.2995 0.1902  -0.1202 352 HOH C O     
11184 O  O     . HOH N .   ? 0.9264 0.8362 0.3931 -0.4528 -0.1618 0.1431  353 HOH C O     
11185 O  O     . HOH N .   ? 0.9107 0.8371 0.4093 -0.3998 -0.0790 0.0646  354 HOH C O     
11186 O  O     . HOH N .   ? 0.4240 0.4151 0.3448 -0.0557 0.0133  -0.0012 355 HOH C O     
11187 O  O     . HOH N .   ? 0.7995 0.7417 0.6399 -0.1376 -0.0719 0.0978  356 HOH C O     
11188 O  O     . HOH N .   ? 0.6305 0.5894 0.3365 -0.1995 0.0296  -0.0241 357 HOH C O     
11189 O  O     . HOH N .   ? 0.4441 0.4405 0.3802 -0.0571 0.0474  -0.0066 358 HOH C O     
11190 O  O     . HOH N .   ? 0.5786 0.5703 0.3993 -0.2039 0.0433  0.0678  359 HOH C O     
11191 O  O     . HOH N .   ? 0.7094 0.7157 0.4587 -0.2454 0.1239  -0.0007 360 HOH C O     
11192 O  O     . HOH N .   ? 0.8492 0.7603 0.5168 -0.2777 0.1871  -0.1464 361 HOH C O     
11193 O  O     . HOH N .   ? 0.9852 0.9020 0.4374 -0.4273 0.0185  -0.0073 362 HOH C O     
11194 O  O     . HOH N .   ? 0.8068 0.7522 0.3931 -0.3402 -0.1307 0.0957  363 HOH C O     
11195 O  O     . HOH N .   ? 0.8876 0.8002 0.6428 -0.2407 0.2453  -0.1800 364 HOH C O     
11196 O  O     . HOH N .   ? 0.8524 0.7869 0.4423 -0.3189 -0.0467 0.0785  365 HOH C O     
11197 O  O     . HOH N .   ? 0.7893 0.7342 0.6672 -0.1655 0.2481  -0.1604 366 HOH C O     
11198 O  O     . HOH N .   ? 0.7283 0.6703 0.6024 -0.1447 0.2101  -0.1364 367 HOH C O     
11199 O  O     . HOH N .   ? 0.7541 0.7138 0.4497 -0.2474 0.0108  0.0647  368 HOH C O     
11200 O  O     . HOH N .   ? 0.7447 0.7174 0.4928 -0.2165 -0.1487 0.1003  369 HOH C O     
11201 O  O     . HOH N .   ? 0.6616 0.6448 0.5962 -0.0867 -0.1574 0.0981  370 HOH C O     
11202 O  O     . HOH N .   ? 0.8211 0.7890 0.4805 -0.2752 0.0577  0.0260  371 HOH C O     
11203 O  O     . HOH N .   ? 0.7956 0.7554 0.4465 -0.2937 0.1775  -0.0961 372 HOH C O     
11204 O  O     . HOH N .   ? 0.6219 0.6764 0.6108 -0.1132 0.1134  0.0025  373 HOH C O     
11205 O  O     . HOH N .   ? 0.6894 0.6222 0.4262 -0.2097 -0.0848 0.1145  374 HOH C O     
11206 O  O     . HOH N .   ? 0.5244 0.5158 0.4469 -0.1113 0.0059  0.0558  375 HOH C O     
11207 O  O     . HOH N .   ? 0.9388 0.8863 0.5611 -0.3142 0.1822  -0.1094 376 HOH C O     
11208 O  O     . HOH N .   ? 0.6931 0.6558 0.4591 -0.2094 -0.1659 0.1216  377 HOH C O     
11209 O  O     . HOH N .   ? 0.5803 0.5512 0.4266 -0.1555 -0.0052 0.0736  378 HOH C O     
11210 O  O     . HOH N .   ? 1.0425 0.9461 0.5456 -0.3906 0.1061  -0.0967 379 HOH C O     
11211 O  O     . HOH N .   ? 0.8581 0.7858 0.6105 -0.2515 0.2609  -0.1821 380 HOH C O     
11212 O  O     . HOH N .   ? 0.9286 0.8416 0.5466 -0.2972 0.1201  -0.1086 381 HOH C O     
11213 O  O     . HOH N .   ? 0.7814 0.7465 0.5989 -0.1738 -0.0073 0.0799  382 HOH C O     
11214 O  O     . HOH N .   ? 1.0662 0.9819 0.4934 -0.4515 0.0950  -0.0574 383 HOH C O     
11215 O  O     . HOH N .   ? 0.7909 0.7465 0.6651 -0.1405 0.1996  -0.1222 384 HOH C O     
11216 O  O     . HOH N .   ? 0.7479 0.7173 0.5484 -0.1905 0.1932  -0.1089 385 HOH C O     
11217 O  O     . HOH N .   ? 0.8696 0.8199 0.4577 -0.3319 -0.1076 0.0703  386 HOH C O     
11218 O  O     . HOH N .   ? 0.6418 0.5479 0.4575 -0.1865 -0.1838 0.1666  387 HOH C O     
11219 O  O     . HOH N .   ? 0.9742 0.8914 0.7070 -0.2081 0.1306  -0.1164 388 HOH C O     
11220 O  O     . HOH N .   ? 0.6062 0.6488 0.6217 -0.0729 0.1333  -0.0285 389 HOH C O     
11221 O  O     . HOH N .   ? 0.7395 0.6624 0.5831 -0.1988 -0.2412 0.1917  390 HOH C O     
11222 O  O     . HOH N .   ? 0.5227 0.5235 0.4592 -0.1203 0.0147  0.0586  391 HOH C O     
11223 O  O     . HOH N .   ? 0.9039 0.8194 0.5071 -0.3442 -0.1715 0.1588  392 HOH C O     
11224 O  O     . HOH N .   ? 0.5277 0.5164 0.4460 -0.0576 0.0314  -0.0151 393 HOH C O     
11225 O  O     . HOH N .   ? 0.5822 0.5643 0.5194 -0.0941 -0.0154 0.0604  394 HOH C O     
11226 O  O     . HOH N .   ? 0.8148 0.7737 0.4851 -0.2701 0.1574  -0.0844 395 HOH C O     
11227 O  O     . HOH N .   ? 0.5067 0.5016 0.4523 -0.0413 0.0215  0.0003  396 HOH C O     
11228 O  O     . HOH N .   ? 0.9527 0.8828 0.5160 -0.3419 -0.0540 0.0808  397 HOH C O     
11229 O  O     . HOH N .   ? 0.7911 0.7621 0.7100 -0.0771 0.1282  -0.0689 398 HOH C O     
11230 O  O     . HOH N .   ? 0.8011 0.7983 0.5826 -0.1793 -0.0831 0.0231  399 HOH C O     
11231 O  O     . HOH N .   ? 0.6239 0.6139 0.5461 -0.0560 -0.0188 0.0185  400 HOH C O     
11232 O  O     . HOH N .   ? 0.9178 0.8287 0.6116 -0.2695 0.2147  -0.1630 401 HOH C O     
11233 O  O     . HOH N .   ? 0.5903 0.5752 0.4526 -0.1107 -0.0889 0.0566  402 HOH C O     
11234 O  O     . HOH N .   ? 0.5886 0.5874 0.4968 -0.0725 -0.0322 0.0110  403 HOH C O     
11235 O  O     . HOH N .   ? 0.8935 0.8342 0.4637 -0.3556 0.1856  -0.1138 404 HOH C O     
11236 O  O     . HOH N .   ? 0.7405 0.6885 0.6451 -0.1380 0.2284  -0.1441 405 HOH C O     
11237 O  O     . HOH N .   ? 0.8226 0.7518 0.7564 -0.1454 0.2714  -0.1799 406 HOH C O     
11238 O  O     . HOH N .   ? 0.4679 0.4739 0.4358 -0.1024 0.0089  0.0563  407 HOH C O     
11239 O  O     . HOH N .   ? 0.4271 0.4609 0.4312 -0.0851 0.0427  0.0343  408 HOH C O     
11240 O  O     . HOH N .   ? 1.0682 0.9974 0.6132 -0.3853 0.2194  -0.1466 409 HOH C O     
11241 O  O     . HOH N .   ? 1.0960 1.0441 0.6068 -0.4113 0.2026  -0.1115 410 HOH C O     
# 
