data_9BGH
# 
_entry.id   9BGH 
# 
_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   9BGH         pdb_00009bgh 10.2210/pdb9bgh/pdb 
WWPDB D_1000283325 ?            ?                   
# 
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 2024-11-13 
3 'Structure model' 1 2 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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 2 'Structure model' 'Source and taxonomy' 
3 2 'Structure model' 'Structure summary'   
4 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' entity_src_gen  
3 2 'Structure model' struct          
4 3 'Structure model' citation        
5 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.title'                                
2  2 'Structure model' '_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id' 
3  2 'Structure model' '_entity_src_gen.pdbx_gene_src_scientific_name'  
4  2 'Structure model' '_struct.title'                                  
5  3 'Structure model' '_citation.country'                              
6  3 'Structure model' '_citation.journal_abbrev'                       
7  3 'Structure model' '_citation.journal_id_ASTM'                      
8  3 'Structure model' '_citation.journal_id_CSD'                       
9  3 'Structure model' '_citation.journal_id_ISSN'                      
10 3 'Structure model' '_citation.journal_volume'                       
11 3 'Structure model' '_citation.page_first'                           
12 3 'Structure model' '_citation.page_last'                            
13 3 'Structure model' '_citation.pdbx_database_id_DOI'                 
14 3 'Structure model' '_citation.pdbx_database_id_PubMed'              
15 3 'Structure model' '_citation.title'                                
16 3 '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                        9BGH 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pourfary@mskcc.org 
_pdbx_contact_author.name_first         Yasin 
_pdbx_contact_author.name_last          Pourfarjam 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0009-8881-6824 
# 
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 'Peptidyl-prolyl cis-trans isomerase A' 18093.555 2   5.2.1.8 ?    ? ? 
2 polymer     man 'GTPase KRas' 19386.848 2   3.6.5.2 G12D ? ? 
3 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   ?       ?    ? ? 
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE" 443.201   2   ?       ?    ? ? 
5 non-polymer syn 'MAGNESIUM ION' 24.305    2   ?       ?    ? ? 
6 non-polymer syn 'ALUMINUM FLUORIDE' 83.977    1   ?       ?    ? ? 
7 water       nat water 18.015    485 ?       ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'PPIase A,Cyclophilin A,Cyclosporin A-binding protein,Rotamase A' 
2 'K-Ras 2,Ki-Ras,K-ras'                                            
# 
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 
;GMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;GMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
B,D ? 
2 'polypeptide(L)' no no 
;GMTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
;GMTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
A,C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;(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 
4 "GUANOSINE-5'-DIPHOSPHATE" GDP 
5 'MAGNESIUM ION' MG  
6 'ALUMINUM FLUORIDE' AF3 
7 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   VAL n 
1 4   ASN n 
1 5   PRO n 
1 6   THR n 
1 7   VAL n 
1 8   PHE n 
1 9   PHE n 
1 10  ASP n 
1 11  ILE n 
1 12  ALA n 
1 13  VAL n 
1 14  ASP n 
1 15  GLY n 
1 16  GLU n 
1 17  PRO n 
1 18  LEU n 
1 19  GLY n 
1 20  ARG n 
1 21  VAL n 
1 22  SER n 
1 23  PHE n 
1 24  GLU n 
1 25  LEU n 
1 26  PHE n 
1 27  ALA n 
1 28  ASP n 
1 29  LYS n 
1 30  VAL n 
1 31  PRO n 
1 32  LYS n 
1 33  THR n 
1 34  ALA n 
1 35  GLU n 
1 36  ASN n 
1 37  PHE n 
1 38  ARG n 
1 39  ALA n 
1 40  LEU n 
1 41  SER n 
1 42  THR n 
1 43  GLY n 
1 44  GLU n 
1 45  LYS n 
1 46  GLY n 
1 47  PHE n 
1 48  GLY n 
1 49  TYR n 
1 50  LYS n 
1 51  GLY n 
1 52  SER n 
1 53  CYS n 
1 54  PHE n 
1 55  HIS n 
1 56  ARG n 
1 57  ILE n 
1 58  ILE n 
1 59  PRO n 
1 60  GLY n 
1 61  PHE n 
1 62  MET n 
1 63  CYS n 
1 64  GLN n 
1 65  GLY n 
1 66  GLY n 
1 67  ASP n 
1 68  PHE n 
1 69  THR n 
1 70  ARG n 
1 71  HIS n 
1 72  ASN n 
1 73  GLY n 
1 74  THR n 
1 75  GLY n 
1 76  GLY n 
1 77  LYS n 
1 78  SER n 
1 79  ILE n 
1 80  TYR n 
1 81  GLY n 
1 82  GLU n 
1 83  LYS n 
1 84  PHE n 
1 85  GLU n 
1 86  ASP n 
1 87  GLU n 
1 88  ASN n 
1 89  PHE n 
1 90  ILE n 
1 91  LEU n 
1 92  LYS n 
1 93  HIS n 
1 94  THR n 
1 95  GLY n 
1 96  PRO n 
1 97  GLY n 
1 98  ILE n 
1 99  LEU n 
1 100 SER n 
1 101 MET n 
1 102 ALA n 
1 103 ASN n 
1 104 ALA n 
1 105 GLY n 
1 106 PRO n 
1 107 ASN n 
1 108 THR n 
1 109 ASN n 
1 110 GLY n 
1 111 SER n 
1 112 GLN n 
1 113 PHE n 
1 114 PHE n 
1 115 ILE n 
1 116 CYS n 
1 117 THR n 
1 118 ALA n 
1 119 LYS n 
1 120 THR n 
1 121 GLU n 
1 122 TRP n 
1 123 LEU n 
1 124 ASP n 
1 125 GLY n 
1 126 LYS n 
1 127 HIS n 
1 128 VAL n 
1 129 VAL n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 VAL n 
1 134 LYS n 
1 135 GLU n 
1 136 GLY n 
1 137 MET n 
1 138 ASN n 
1 139 ILE n 
1 140 VAL n 
1 141 GLU n 
1 142 ALA n 
1 143 MET n 
1 144 GLU n 
1 145 ARG n 
1 146 PHE n 
1 147 GLY n 
1 148 SER n 
1 149 ARG n 
1 150 ASN n 
1 151 GLY n 
1 152 LYS n 
1 153 THR n 
1 154 SER n 
1 155 LYS n 
1 156 LYS n 
1 157 ILE n 
1 158 THR n 
1 159 ILE n 
1 160 ALA n 
1 161 ASP n 
1 162 CYS n 
1 163 GLY n 
1 164 GLN n 
1 165 LEU n 
1 166 GLU n 
2 1   GLY n 
2 2   MET n 
2 3   THR n 
2 4   GLU n 
2 5   TYR n 
2 6   LYS n 
2 7   LEU n 
2 8   VAL n 
2 9   VAL n 
2 10  VAL n 
2 11  GLY n 
2 12  ALA n 
2 13  ASP n 
2 14  GLY n 
2 15  VAL n 
2 16  GLY n 
2 17  LYS n 
2 18  SER n 
2 19  ALA n 
2 20  LEU n 
2 21  THR n 
2 22  ILE n 
2 23  GLN n 
2 24  LEU n 
2 25  ILE n 
2 26  GLN n 
2 27  ASN n 
2 28  HIS n 
2 29  PHE n 
2 30  VAL n 
2 31  ASP n 
2 32  GLU n 
2 33  TYR n 
2 34  ASP n 
2 35  PRO n 
2 36  THR n 
2 37  ILE n 
2 38  GLU n 
2 39  ASP n 
2 40  SER n 
2 41  TYR n 
2 42  ARG n 
2 43  LYS n 
2 44  GLN n 
2 45  VAL n 
2 46  VAL n 
2 47  ILE n 
2 48  ASP n 
2 49  GLY n 
2 50  GLU n 
2 51  THR n 
2 52  CYS n 
2 53  LEU n 
2 54  LEU n 
2 55  ASP n 
2 56  ILE n 
2 57  LEU n 
2 58  ASP n 
2 59  THR n 
2 60  ALA n 
2 61  GLY n 
2 62  GLN n 
2 63  GLU n 
2 64  GLU n 
2 65  TYR n 
2 66  SER n 
2 67  ALA n 
2 68  MET n 
2 69  ARG n 
2 70  ASP n 
2 71  GLN n 
2 72  TYR n 
2 73  MET n 
2 74  ARG n 
2 75  THR n 
2 76  GLY n 
2 77  GLU n 
2 78  GLY n 
2 79  PHE n 
2 80  LEU n 
2 81  CYS n 
2 82  VAL n 
2 83  PHE n 
2 84  ALA n 
2 85  ILE n 
2 86  ASN n 
2 87  ASN n 
2 88  THR n 
2 89  LYS n 
2 90  SER n 
2 91  PHE n 
2 92  GLU n 
2 93  ASP n 
2 94  ILE n 
2 95  HIS n 
2 96  HIS n 
2 97  TYR n 
2 98  ARG n 
2 99  GLU n 
2 100 GLN n 
2 101 ILE n 
2 102 LYS n 
2 103 ARG n 
2 104 VAL n 
2 105 LYS n 
2 106 ASP n 
2 107 SER n 
2 108 GLU n 
2 109 ASP n 
2 110 VAL n 
2 111 PRO n 
2 112 MET n 
2 113 VAL n 
2 114 LEU n 
2 115 VAL n 
2 116 GLY n 
2 117 ASN n 
2 118 LYS n 
2 119 CYS n 
2 120 ASP n 
2 121 LEU n 
2 122 PRO n 
2 123 SER n 
2 124 ARG n 
2 125 THR n 
2 126 VAL n 
2 127 ASP n 
2 128 THR n 
2 129 LYS n 
2 130 GLN n 
2 131 ALA n 
2 132 GLN n 
2 133 ASP n 
2 134 LEU n 
2 135 ALA n 
2 136 ARG n 
2 137 SER n 
2 138 TYR n 
2 139 GLY n 
2 140 ILE n 
2 141 PRO n 
2 142 PHE n 
2 143 ILE n 
2 144 GLU n 
2 145 THR n 
2 146 SER n 
2 147 ALA n 
2 148 LYS n 
2 149 THR n 
2 150 ARG n 
2 151 GLN n 
2 152 GLY n 
2 153 VAL n 
2 154 ASP n 
2 155 ASP n 
2 156 ALA n 
2 157 PHE n 
2 158 TYR n 
2 159 THR n 
2 160 LEU n 
2 161 VAL n 
2 162 ARG n 
2 163 GLU n 
2 164 ILE n 
2 165 ARG n 
2 166 LYS n 
2 167 HIS n 
2 168 LYS n 
2 169 GLU n 
2 170 LYS 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' 1 166 ? ? 'PPIA, CYPA' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 170 ? ? KRAS         ? ? ? ? ? ? '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 
AF3 non-polymer         . 'ALUMINUM FLUORIDE' ?        'Al F3'             83.977  
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 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE" ?        'C10 H15 N5 O11 P2' 443.201 
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  
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   ?   ?   ?   B . n 
A 1 2   MET 2   1   ?   ?   ?   B . n 
A 1 3   VAL 3   2   2   VAL VAL B . n 
A 1 4   ASN 4   3   3   ASN ASN B . n 
A 1 5   PRO 5   4   4   PRO PRO B . n 
A 1 6   THR 6   5   5   THR THR B . n 
A 1 7   VAL 7   6   6   VAL VAL B . n 
A 1 8   PHE 8   7   7   PHE PHE B . n 
A 1 9   PHE 9   8   8   PHE PHE B . n 
A 1 10  ASP 10  9   9   ASP ASP B . n 
A 1 11  ILE 11  10  10  ILE ILE B . n 
A 1 12  ALA 12  11  11  ALA ALA B . n 
A 1 13  VAL 13  12  12  VAL VAL B . n 
A 1 14  ASP 14  13  13  ASP ASP B . n 
A 1 15  GLY 15  14  14  GLY GLY B . n 
A 1 16  GLU 16  15  15  GLU GLU B . n 
A 1 17  PRO 17  16  16  PRO PRO B . n 
A 1 18  LEU 18  17  17  LEU LEU B . n 
A 1 19  GLY 19  18  18  GLY GLY B . n 
A 1 20  ARG 20  19  19  ARG ARG B . n 
A 1 21  VAL 21  20  20  VAL VAL B . n 
A 1 22  SER 22  21  21  SER SER B . n 
A 1 23  PHE 23  22  22  PHE PHE B . n 
A 1 24  GLU 24  23  23  GLU GLU B . n 
A 1 25  LEU 25  24  24  LEU LEU B . n 
A 1 26  PHE 26  25  25  PHE PHE B . n 
A 1 27  ALA 27  26  26  ALA ALA B . n 
A 1 28  ASP 28  27  27  ASP ASP B . n 
A 1 29  LYS 29  28  28  LYS LYS B . n 
A 1 30  VAL 30  29  29  VAL VAL B . n 
A 1 31  PRO 31  30  30  PRO PRO B . n 
A 1 32  LYS 32  31  31  LYS LYS B . n 
A 1 33  THR 33  32  32  THR THR B . n 
A 1 34  ALA 34  33  33  ALA ALA B . n 
A 1 35  GLU 35  34  34  GLU GLU B . n 
A 1 36  ASN 36  35  35  ASN ASN B . n 
A 1 37  PHE 37  36  36  PHE PHE B . n 
A 1 38  ARG 38  37  37  ARG ARG B . n 
A 1 39  ALA 39  38  38  ALA ALA B . n 
A 1 40  LEU 40  39  39  LEU LEU B . n 
A 1 41  SER 41  40  40  SER SER B . n 
A 1 42  THR 42  41  41  THR THR B . n 
A 1 43  GLY 43  42  42  GLY GLY B . n 
A 1 44  GLU 44  43  43  GLU GLU B . n 
A 1 45  LYS 45  44  44  LYS LYS B . n 
A 1 46  GLY 46  45  45  GLY GLY B . n 
A 1 47  PHE 47  46  46  PHE PHE B . n 
A 1 48  GLY 48  47  47  GLY GLY B . n 
A 1 49  TYR 49  48  48  TYR TYR B . n 
A 1 50  LYS 50  49  49  LYS LYS B . n 
A 1 51  GLY 51  50  50  GLY GLY B . n 
A 1 52  SER 52  51  51  SER SER B . n 
A 1 53  CYS 53  52  52  CYS CYS B . n 
A 1 54  PHE 54  53  53  PHE PHE B . n 
A 1 55  HIS 55  54  54  HIS HIS B . n 
A 1 56  ARG 56  55  55  ARG ARG B . n 
A 1 57  ILE 57  56  56  ILE ILE B . n 
A 1 58  ILE 58  57  57  ILE ILE B . n 
A 1 59  PRO 59  58  58  PRO PRO B . n 
A 1 60  GLY 60  59  59  GLY GLY B . n 
A 1 61  PHE 61  60  60  PHE PHE B . n 
A 1 62  MET 62  61  61  MET MET B . n 
A 1 63  CYS 63  62  62  CYS CYS B . n 
A 1 64  GLN 64  63  63  GLN GLN B . n 
A 1 65  GLY 65  64  64  GLY GLY B . n 
A 1 66  GLY 66  65  65  GLY GLY B . n 
A 1 67  ASP 67  66  66  ASP ASP B . n 
A 1 68  PHE 68  67  67  PHE PHE B . n 
A 1 69  THR 69  68  68  THR THR B . n 
A 1 70  ARG 70  69  69  ARG ARG B . n 
A 1 71  HIS 71  70  70  HIS HIS B . n 
A 1 72  ASN 72  71  71  ASN ASN B . n 
A 1 73  GLY 73  72  72  GLY GLY B . n 
A 1 74  THR 74  73  73  THR THR B . n 
A 1 75  GLY 75  74  74  GLY GLY B . n 
A 1 76  GLY 76  75  75  GLY GLY B . n 
A 1 77  LYS 77  76  76  LYS LYS B . n 
A 1 78  SER 78  77  77  SER SER B . n 
A 1 79  ILE 79  78  78  ILE ILE B . n 
A 1 80  TYR 80  79  79  TYR TYR B . n 
A 1 81  GLY 81  80  80  GLY GLY B . n 
A 1 82  GLU 82  81  81  GLU GLU B . n 
A 1 83  LYS 83  82  82  LYS LYS B . n 
A 1 84  PHE 84  83  83  PHE PHE B . n 
A 1 85  GLU 85  84  84  GLU GLU B . n 
A 1 86  ASP 86  85  85  ASP ASP B . n 
A 1 87  GLU 87  86  86  GLU GLU B . n 
A 1 88  ASN 88  87  87  ASN ASN B . n 
A 1 89  PHE 89  88  88  PHE PHE B . n 
A 1 90  ILE 90  89  89  ILE ILE B . n 
A 1 91  LEU 91  90  90  LEU LEU B . n 
A 1 92  LYS 92  91  91  LYS LYS B . n 
A 1 93  HIS 93  92  92  HIS HIS B . n 
A 1 94  THR 94  93  93  THR THR B . n 
A 1 95  GLY 95  94  94  GLY GLY B . n 
A 1 96  PRO 96  95  95  PRO PRO B . n 
A 1 97  GLY 97  96  96  GLY GLY B . n 
A 1 98  ILE 98  97  97  ILE ILE B . n 
A 1 99  LEU 99  98  98  LEU LEU B . n 
A 1 100 SER 100 99  99  SER SER B . n 
A 1 101 MET 101 100 100 MET MET B . n 
A 1 102 ALA 102 101 101 ALA ALA B . n 
A 1 103 ASN 103 102 102 ASN ASN B . n 
A 1 104 ALA 104 103 103 ALA ALA B . n 
A 1 105 GLY 105 104 104 GLY GLY B . n 
A 1 106 PRO 106 105 105 PRO PRO B . n 
A 1 107 ASN 107 106 106 ASN ASN B . n 
A 1 108 THR 108 107 107 THR THR B . n 
A 1 109 ASN 109 108 108 ASN ASN B . n 
A 1 110 GLY 110 109 109 GLY GLY B . n 
A 1 111 SER 111 110 110 SER SER B . n 
A 1 112 GLN 112 111 111 GLN GLN B . n 
A 1 113 PHE 113 112 112 PHE PHE B . n 
A 1 114 PHE 114 113 113 PHE PHE B . n 
A 1 115 ILE 115 114 114 ILE ILE B . n 
A 1 116 CYS 116 115 115 CYS CYS B . n 
A 1 117 THR 117 116 116 THR THR B . n 
A 1 118 ALA 118 117 117 ALA ALA B . n 
A 1 119 LYS 119 118 118 LYS LYS B . n 
A 1 120 THR 120 119 119 THR THR B . n 
A 1 121 GLU 121 120 120 GLU GLU B . n 
A 1 122 TRP 122 121 121 TRP TRP B . n 
A 1 123 LEU 123 122 122 LEU LEU B . n 
A 1 124 ASP 124 123 123 ASP ASP B . n 
A 1 125 GLY 125 124 124 GLY GLY B . n 
A 1 126 LYS 126 125 125 LYS LYS B . n 
A 1 127 HIS 127 126 126 HIS HIS B . n 
A 1 128 VAL 128 127 127 VAL VAL B . n 
A 1 129 VAL 129 128 128 VAL VAL B . n 
A 1 130 PHE 130 129 129 PHE PHE B . n 
A 1 131 GLY 131 130 130 GLY GLY B . n 
A 1 132 LYS 132 131 131 LYS LYS B . n 
A 1 133 VAL 133 132 132 VAL VAL B . n 
A 1 134 LYS 134 133 133 LYS LYS B . n 
A 1 135 GLU 135 134 134 GLU GLU B . n 
A 1 136 GLY 136 135 135 GLY GLY B . n 
A 1 137 MET 137 136 136 MET MET B . n 
A 1 138 ASN 138 137 137 ASN ASN B . n 
A 1 139 ILE 139 138 138 ILE ILE B . n 
A 1 140 VAL 140 139 139 VAL VAL B . n 
A 1 141 GLU 141 140 140 GLU GLU B . n 
A 1 142 ALA 142 141 141 ALA ALA B . n 
A 1 143 MET 143 142 142 MET MET B . n 
A 1 144 GLU 144 143 143 GLU GLU B . n 
A 1 145 ARG 145 144 144 ARG ARG B . n 
A 1 146 PHE 146 145 145 PHE PHE B . n 
A 1 147 GLY 147 146 146 GLY GLY B . n 
A 1 148 SER 148 147 147 SER SER B . n 
A 1 149 ARG 149 148 148 ARG ARG B . n 
A 1 150 ASN 150 149 149 ASN ASN B . n 
A 1 151 GLY 151 150 150 GLY GLY B . n 
A 1 152 LYS 152 151 151 LYS LYS B . n 
A 1 153 THR 153 152 152 THR THR B . n 
A 1 154 SER 154 153 153 SER SER B . n 
A 1 155 LYS 155 154 154 LYS LYS B . n 
A 1 156 LYS 156 155 155 LYS LYS B . n 
A 1 157 ILE 157 156 156 ILE ILE B . n 
A 1 158 THR 158 157 157 THR THR B . n 
A 1 159 ILE 159 158 158 ILE ILE B . n 
A 1 160 ALA 160 159 159 ALA ALA B . n 
A 1 161 ASP 161 160 160 ASP ASP B . n 
A 1 162 CYS 162 161 161 CYS CYS B . n 
A 1 163 GLY 163 162 162 GLY GLY B . n 
A 1 164 GLN 164 163 163 GLN GLN B . n 
A 1 165 LEU 165 164 164 LEU LEU B . n 
A 1 166 GLU 166 165 ?   ?   ?   B . n 
B 1 1   GLY 1   0   ?   ?   ?   D . n 
B 1 2   MET 2   1   ?   ?   ?   D . n 
B 1 3   VAL 3   2   2   VAL VAL D . n 
B 1 4   ASN 4   3   3   ASN ASN D . n 
B 1 5   PRO 5   4   4   PRO PRO D . n 
B 1 6   THR 6   5   5   THR THR D . n 
B 1 7   VAL 7   6   6   VAL VAL D . n 
B 1 8   PHE 8   7   7   PHE PHE D . n 
B 1 9   PHE 9   8   8   PHE PHE D . n 
B 1 10  ASP 10  9   9   ASP ASP D . n 
B 1 11  ILE 11  10  10  ILE ILE D . n 
B 1 12  ALA 12  11  11  ALA ALA D . n 
B 1 13  VAL 13  12  12  VAL VAL D . n 
B 1 14  ASP 14  13  13  ASP ASP D . n 
B 1 15  GLY 15  14  14  GLY GLY D . n 
B 1 16  GLU 16  15  15  GLU GLU D . n 
B 1 17  PRO 17  16  16  PRO PRO D . n 
B 1 18  LEU 18  17  17  LEU LEU D . n 
B 1 19  GLY 19  18  18  GLY GLY D . n 
B 1 20  ARG 20  19  19  ARG ARG D . n 
B 1 21  VAL 21  20  20  VAL VAL D . n 
B 1 22  SER 22  21  21  SER SER D . n 
B 1 23  PHE 23  22  22  PHE PHE D . n 
B 1 24  GLU 24  23  23  GLU GLU D . n 
B 1 25  LEU 25  24  24  LEU LEU D . n 
B 1 26  PHE 26  25  25  PHE PHE D . n 
B 1 27  ALA 27  26  26  ALA ALA D . n 
B 1 28  ASP 28  27  27  ASP ASP D . n 
B 1 29  LYS 29  28  28  LYS LYS D . n 
B 1 30  VAL 30  29  29  VAL VAL D . n 
B 1 31  PRO 31  30  30  PRO PRO D . n 
B 1 32  LYS 32  31  31  LYS LYS D . n 
B 1 33  THR 33  32  32  THR THR D . n 
B 1 34  ALA 34  33  33  ALA ALA D . n 
B 1 35  GLU 35  34  34  GLU GLU D . n 
B 1 36  ASN 36  35  35  ASN ASN D . n 
B 1 37  PHE 37  36  36  PHE PHE D . n 
B 1 38  ARG 38  37  37  ARG ARG D . n 
B 1 39  ALA 39  38  38  ALA ALA D . n 
B 1 40  LEU 40  39  39  LEU LEU D . n 
B 1 41  SER 41  40  40  SER SER D . n 
B 1 42  THR 42  41  41  THR THR D . n 
B 1 43  GLY 43  42  42  GLY GLY D . n 
B 1 44  GLU 44  43  43  GLU GLU D . n 
B 1 45  LYS 45  44  44  LYS LYS D . n 
B 1 46  GLY 46  45  45  GLY GLY D . n 
B 1 47  PHE 47  46  46  PHE PHE D . n 
B 1 48  GLY 48  47  47  GLY GLY D . n 
B 1 49  TYR 49  48  48  TYR TYR D . n 
B 1 50  LYS 50  49  49  LYS LYS D . n 
B 1 51  GLY 51  50  50  GLY GLY D . n 
B 1 52  SER 52  51  51  SER SER D . n 
B 1 53  CYS 53  52  52  CYS CYS D . n 
B 1 54  PHE 54  53  53  PHE PHE D . n 
B 1 55  HIS 55  54  54  HIS HIS D . n 
B 1 56  ARG 56  55  55  ARG ARG D . n 
B 1 57  ILE 57  56  56  ILE ILE D . n 
B 1 58  ILE 58  57  57  ILE ILE D . n 
B 1 59  PRO 59  58  58  PRO PRO D . n 
B 1 60  GLY 60  59  59  GLY GLY D . n 
B 1 61  PHE 61  60  60  PHE PHE D . n 
B 1 62  MET 62  61  61  MET MET D . n 
B 1 63  CYS 63  62  62  CYS CYS D . n 
B 1 64  GLN 64  63  63  GLN GLN D . n 
B 1 65  GLY 65  64  64  GLY GLY D . n 
B 1 66  GLY 66  65  65  GLY GLY D . n 
B 1 67  ASP 67  66  66  ASP ASP D . n 
B 1 68  PHE 68  67  67  PHE PHE D . n 
B 1 69  THR 69  68  68  THR THR D . n 
B 1 70  ARG 70  69  69  ARG ARG D . n 
B 1 71  HIS 71  70  70  HIS HIS D . n 
B 1 72  ASN 72  71  71  ASN ASN D . n 
B 1 73  GLY 73  72  72  GLY GLY D . n 
B 1 74  THR 74  73  73  THR THR D . n 
B 1 75  GLY 75  74  74  GLY GLY D . n 
B 1 76  GLY 76  75  75  GLY GLY D . n 
B 1 77  LYS 77  76  76  LYS LYS D . n 
B 1 78  SER 78  77  77  SER SER D . n 
B 1 79  ILE 79  78  78  ILE ILE D . n 
B 1 80  TYR 80  79  79  TYR TYR D . n 
B 1 81  GLY 81  80  80  GLY GLY D . n 
B 1 82  GLU 82  81  81  GLU GLU D . n 
B 1 83  LYS 83  82  82  LYS LYS D . n 
B 1 84  PHE 84  83  83  PHE PHE D . n 
B 1 85  GLU 85  84  84  GLU GLU D . n 
B 1 86  ASP 86  85  85  ASP ASP D . n 
B 1 87  GLU 87  86  86  GLU GLU D . n 
B 1 88  ASN 88  87  87  ASN ASN D . n 
B 1 89  PHE 89  88  88  PHE PHE D . n 
B 1 90  ILE 90  89  89  ILE ILE D . n 
B 1 91  LEU 91  90  90  LEU LEU D . n 
B 1 92  LYS 92  91  91  LYS LYS D . n 
B 1 93  HIS 93  92  92  HIS HIS D . n 
B 1 94  THR 94  93  93  THR THR D . n 
B 1 95  GLY 95  94  94  GLY GLY D . n 
B 1 96  PRO 96  95  95  PRO PRO D . n 
B 1 97  GLY 97  96  96  GLY GLY D . n 
B 1 98  ILE 98  97  97  ILE ILE D . n 
B 1 99  LEU 99  98  98  LEU LEU D . n 
B 1 100 SER 100 99  99  SER SER D . n 
B 1 101 MET 101 100 100 MET MET D . n 
B 1 102 ALA 102 101 101 ALA ALA D . n 
B 1 103 ASN 103 102 102 ASN ASN D . n 
B 1 104 ALA 104 103 103 ALA ALA D . n 
B 1 105 GLY 105 104 104 GLY GLY D . n 
B 1 106 PRO 106 105 105 PRO PRO D . n 
B 1 107 ASN 107 106 106 ASN ASN D . n 
B 1 108 THR 108 107 107 THR THR D . n 
B 1 109 ASN 109 108 108 ASN ASN D . n 
B 1 110 GLY 110 109 109 GLY GLY D . n 
B 1 111 SER 111 110 110 SER SER D . n 
B 1 112 GLN 112 111 111 GLN GLN D . n 
B 1 113 PHE 113 112 112 PHE PHE D . n 
B 1 114 PHE 114 113 113 PHE PHE D . n 
B 1 115 ILE 115 114 114 ILE ILE D . n 
B 1 116 CYS 116 115 115 CYS CYS D . n 
B 1 117 THR 117 116 116 THR THR D . n 
B 1 118 ALA 118 117 117 ALA ALA D . n 
B 1 119 LYS 119 118 118 LYS LYS D . n 
B 1 120 THR 120 119 119 THR THR D . n 
B 1 121 GLU 121 120 120 GLU GLU D . n 
B 1 122 TRP 122 121 121 TRP TRP D . n 
B 1 123 LEU 123 122 122 LEU LEU D . n 
B 1 124 ASP 124 123 123 ASP ASP D . n 
B 1 125 GLY 125 124 124 GLY GLY D . n 
B 1 126 LYS 126 125 125 LYS LYS D . n 
B 1 127 HIS 127 126 126 HIS HIS D . n 
B 1 128 VAL 128 127 127 VAL VAL D . n 
B 1 129 VAL 129 128 128 VAL VAL D . n 
B 1 130 PHE 130 129 129 PHE PHE D . n 
B 1 131 GLY 131 130 130 GLY GLY D . n 
B 1 132 LYS 132 131 131 LYS LYS D . n 
B 1 133 VAL 133 132 132 VAL VAL D . n 
B 1 134 LYS 134 133 133 LYS LYS D . n 
B 1 135 GLU 135 134 134 GLU GLU D . n 
B 1 136 GLY 136 135 135 GLY GLY D . n 
B 1 137 MET 137 136 136 MET MET D . n 
B 1 138 ASN 138 137 137 ASN ASN D . n 
B 1 139 ILE 139 138 138 ILE ILE D . n 
B 1 140 VAL 140 139 139 VAL VAL D . n 
B 1 141 GLU 141 140 140 GLU GLU D . n 
B 1 142 ALA 142 141 141 ALA ALA D . n 
B 1 143 MET 143 142 142 MET MET D . n 
B 1 144 GLU 144 143 143 GLU GLU D . n 
B 1 145 ARG 145 144 144 ARG ARG D . n 
B 1 146 PHE 146 145 145 PHE PHE D . n 
B 1 147 GLY 147 146 146 GLY GLY D . n 
B 1 148 SER 148 147 147 SER SER D . n 
B 1 149 ARG 149 148 148 ARG ARG D . n 
B 1 150 ASN 150 149 149 ASN ASN D . n 
B 1 151 GLY 151 150 150 GLY GLY D . n 
B 1 152 LYS 152 151 151 LYS LYS D . n 
B 1 153 THR 153 152 152 THR THR D . n 
B 1 154 SER 154 153 153 SER SER D . n 
B 1 155 LYS 155 154 154 LYS LYS D . n 
B 1 156 LYS 156 155 155 LYS LYS D . n 
B 1 157 ILE 157 156 156 ILE ILE D . n 
B 1 158 THR 158 157 157 THR THR D . n 
B 1 159 ILE 159 158 158 ILE ILE D . n 
B 1 160 ALA 160 159 159 ALA ALA D . n 
B 1 161 ASP 161 160 160 ASP ASP D . n 
B 1 162 CYS 162 161 161 CYS CYS D . n 
B 1 163 GLY 163 162 162 GLY GLY D . n 
B 1 164 GLN 164 163 163 GLN GLN D . n 
B 1 165 LEU 165 164 164 LEU LEU D . n 
B 1 166 GLU 166 165 ?   ?   ?   D . n 
C 2 1   GLY 1   0   0   GLY GLY A . n 
C 2 2   MET 2   1   1   MET MET A . n 
C 2 3   THR 3   2   2   THR THR A . n 
C 2 4   GLU 4   3   3   GLU GLU A . n 
C 2 5   TYR 5   4   4   TYR TYR A . n 
C 2 6   LYS 6   5   5   LYS LYS A . n 
C 2 7   LEU 7   6   6   LEU LEU A . n 
C 2 8   VAL 8   7   7   VAL VAL A . n 
C 2 9   VAL 9   8   8   VAL VAL A . n 
C 2 10  VAL 10  9   9   VAL VAL A . n 
C 2 11  GLY 11  10  10  GLY GLY A . n 
C 2 12  ALA 12  11  11  ALA ALA A . n 
C 2 13  ASP 13  12  12  ASP ASP A . n 
C 2 14  GLY 14  13  13  GLY GLY A . n 
C 2 15  VAL 15  14  14  VAL VAL A . n 
C 2 16  GLY 16  15  15  GLY GLY A . n 
C 2 17  LYS 17  16  16  LYS LYS A . n 
C 2 18  SER 18  17  17  SER SER A . n 
C 2 19  ALA 19  18  18  ALA ALA A . n 
C 2 20  LEU 20  19  19  LEU LEU A . n 
C 2 21  THR 21  20  20  THR THR A . n 
C 2 22  ILE 22  21  21  ILE ILE A . n 
C 2 23  GLN 23  22  22  GLN GLN A . n 
C 2 24  LEU 24  23  23  LEU LEU A . n 
C 2 25  ILE 25  24  24  ILE ILE A . n 
C 2 26  GLN 26  25  25  GLN GLN A . n 
C 2 27  ASN 27  26  26  ASN ASN A . n 
C 2 28  HIS 28  27  27  HIS HIS A . n 
C 2 29  PHE 29  28  28  PHE PHE A . n 
C 2 30  VAL 30  29  29  VAL VAL A . n 
C 2 31  ASP 31  30  30  ASP ASP A . n 
C 2 32  GLU 32  31  31  GLU GLU A . n 
C 2 33  TYR 33  32  32  TYR TYR A . n 
C 2 34  ASP 34  33  33  ASP ASP A . n 
C 2 35  PRO 35  34  34  PRO PRO A . n 
C 2 36  THR 36  35  35  THR THR A . n 
C 2 37  ILE 37  36  36  ILE ILE A . n 
C 2 38  GLU 38  37  37  GLU GLU A . n 
C 2 39  ASP 39  38  38  ASP ASP A . n 
C 2 40  SER 40  39  39  SER SER A . n 
C 2 41  TYR 41  40  40  TYR TYR A . n 
C 2 42  ARG 42  41  41  ARG ARG A . n 
C 2 43  LYS 43  42  42  LYS LYS A . n 
C 2 44  GLN 44  43  43  GLN GLN A . n 
C 2 45  VAL 45  44  44  VAL VAL A . n 
C 2 46  VAL 46  45  45  VAL VAL A . n 
C 2 47  ILE 47  46  46  ILE ILE A . n 
C 2 48  ASP 48  47  47  ASP ASP A . n 
C 2 49  GLY 49  48  48  GLY GLY A . n 
C 2 50  GLU 50  49  49  GLU GLU A . n 
C 2 51  THR 51  50  50  THR THR A . n 
C 2 52  CYS 52  51  51  CYS CYS A . n 
C 2 53  LEU 53  52  52  LEU LEU A . n 
C 2 54  LEU 54  53  53  LEU LEU A . n 
C 2 55  ASP 55  54  54  ASP ASP A . n 
C 2 56  ILE 56  55  55  ILE ILE A . n 
C 2 57  LEU 57  56  56  LEU LEU A . n 
C 2 58  ASP 58  57  57  ASP ASP A . n 
C 2 59  THR 59  58  58  THR THR A . n 
C 2 60  ALA 60  59  59  ALA ALA A . n 
C 2 61  GLY 61  60  60  GLY GLY A . n 
C 2 62  GLN 62  61  61  GLN GLN A . n 
C 2 63  GLU 63  62  62  GLU GLU A . n 
C 2 64  GLU 64  63  63  GLU GLU A . n 
C 2 65  TYR 65  64  64  TYR TYR A . n 
C 2 66  SER 66  65  65  SER SER A . n 
C 2 67  ALA 67  66  66  ALA ALA A . n 
C 2 68  MET 68  67  67  MET MET A . n 
C 2 69  ARG 69  68  68  ARG ARG A . n 
C 2 70  ASP 70  69  69  ASP ASP A . n 
C 2 71  GLN 71  70  70  GLN GLN A . n 
C 2 72  TYR 72  71  71  TYR TYR A . n 
C 2 73  MET 73  72  72  MET MET A . n 
C 2 74  ARG 74  73  73  ARG ARG A . n 
C 2 75  THR 75  74  74  THR THR A . n 
C 2 76  GLY 76  75  75  GLY GLY A . n 
C 2 77  GLU 77  76  76  GLU GLU A . n 
C 2 78  GLY 78  77  77  GLY GLY A . n 
C 2 79  PHE 79  78  78  PHE PHE A . n 
C 2 80  LEU 80  79  79  LEU LEU A . n 
C 2 81  CYS 81  80  80  CYS CYS A . n 
C 2 82  VAL 82  81  81  VAL VAL A . n 
C 2 83  PHE 83  82  82  PHE PHE A . n 
C 2 84  ALA 84  83  83  ALA ALA A . n 
C 2 85  ILE 85  84  84  ILE ILE A . n 
C 2 86  ASN 86  85  85  ASN ASN A . n 
C 2 87  ASN 87  86  86  ASN ASN A . n 
C 2 88  THR 88  87  87  THR THR A . n 
C 2 89  LYS 89  88  88  LYS LYS A . n 
C 2 90  SER 90  89  89  SER SER A . n 
C 2 91  PHE 91  90  90  PHE PHE A . n 
C 2 92  GLU 92  91  91  GLU GLU A . n 
C 2 93  ASP 93  92  92  ASP ASP A . n 
C 2 94  ILE 94  93  93  ILE ILE A . n 
C 2 95  HIS 95  94  94  HIS HIS A . n 
C 2 96  HIS 96  95  95  HIS HIS A . n 
C 2 97  TYR 97  96  96  TYR TYR A . n 
C 2 98  ARG 98  97  97  ARG ARG A . n 
C 2 99  GLU 99  98  98  GLU GLU A . n 
C 2 100 GLN 100 99  99  GLN GLN A . n 
C 2 101 ILE 101 100 100 ILE ILE A . n 
C 2 102 LYS 102 101 101 LYS LYS A . n 
C 2 103 ARG 103 102 102 ARG ARG A . n 
C 2 104 VAL 104 103 103 VAL VAL A . n 
C 2 105 LYS 105 104 104 LYS LYS A . n 
C 2 106 ASP 106 105 105 ASP ASP A . n 
C 2 107 SER 107 106 106 SER SER A . n 
C 2 108 GLU 108 107 107 GLU GLU A . n 
C 2 109 ASP 109 108 108 ASP ASP A . n 
C 2 110 VAL 110 109 109 VAL VAL A . n 
C 2 111 PRO 111 110 110 PRO PRO A . n 
C 2 112 MET 112 111 111 MET MET A . n 
C 2 113 VAL 113 112 112 VAL VAL A . n 
C 2 114 LEU 114 113 113 LEU LEU A . n 
C 2 115 VAL 115 114 114 VAL VAL A . n 
C 2 116 GLY 116 115 115 GLY GLY A . n 
C 2 117 ASN 117 116 116 ASN ASN A . n 
C 2 118 LYS 118 117 117 LYS LYS A . n 
C 2 119 CYS 119 118 118 CYS CYS A . n 
C 2 120 ASP 120 119 119 ASP ASP A . n 
C 2 121 LEU 121 120 120 LEU LEU A . n 
C 2 122 PRO 122 121 121 PRO PRO A . n 
C 2 123 SER 123 122 122 SER SER A . n 
C 2 124 ARG 124 123 123 ARG ARG A . n 
C 2 125 THR 125 124 124 THR THR A . n 
C 2 126 VAL 126 125 125 VAL VAL A . n 
C 2 127 ASP 127 126 126 ASP ASP A . n 
C 2 128 THR 128 127 127 THR THR A . n 
C 2 129 LYS 129 128 128 LYS LYS A . n 
C 2 130 GLN 130 129 129 GLN GLN A . n 
C 2 131 ALA 131 130 130 ALA ALA A . n 
C 2 132 GLN 132 131 131 GLN GLN A . n 
C 2 133 ASP 133 132 132 ASP ASP A . n 
C 2 134 LEU 134 133 133 LEU LEU A . n 
C 2 135 ALA 135 134 134 ALA ALA A . n 
C 2 136 ARG 136 135 135 ARG ARG A . n 
C 2 137 SER 137 136 136 SER SER A . n 
C 2 138 TYR 138 137 137 TYR TYR A . n 
C 2 139 GLY 139 138 138 GLY GLY A . n 
C 2 140 ILE 140 139 139 ILE ILE A . n 
C 2 141 PRO 141 140 140 PRO PRO A . n 
C 2 142 PHE 142 141 141 PHE PHE A . n 
C 2 143 ILE 143 142 142 ILE ILE A . n 
C 2 144 GLU 144 143 143 GLU GLU A . n 
C 2 145 THR 145 144 144 THR THR A . n 
C 2 146 SER 146 145 145 SER SER A . n 
C 2 147 ALA 147 146 146 ALA ALA A . n 
C 2 148 LYS 148 147 147 LYS LYS A . n 
C 2 149 THR 149 148 148 THR THR A . n 
C 2 150 ARG 150 149 149 ARG ARG A . n 
C 2 151 GLN 151 150 150 GLN GLN A . n 
C 2 152 GLY 152 151 151 GLY GLY A . n 
C 2 153 VAL 153 152 152 VAL VAL A . n 
C 2 154 ASP 154 153 153 ASP ASP A . n 
C 2 155 ASP 155 154 154 ASP ASP A . n 
C 2 156 ALA 156 155 155 ALA ALA A . n 
C 2 157 PHE 157 156 156 PHE PHE A . n 
C 2 158 TYR 158 157 157 TYR TYR A . n 
C 2 159 THR 159 158 158 THR THR A . n 
C 2 160 LEU 160 159 159 LEU LEU A . n 
C 2 161 VAL 161 160 160 VAL VAL A . n 
C 2 162 ARG 162 161 161 ARG ARG A . n 
C 2 163 GLU 163 162 162 GLU GLU A . n 
C 2 164 ILE 164 163 163 ILE ILE A . n 
C 2 165 ARG 165 164 164 ARG ARG A . n 
C 2 166 LYS 166 165 165 LYS LYS A . n 
C 2 167 HIS 167 166 166 HIS HIS A . n 
C 2 168 LYS 168 167 167 LYS LYS A . n 
C 2 169 GLU 169 168 168 GLU GLU A . n 
C 2 170 LYS 170 169 ?   ?   ?   A . n 
D 2 1   GLY 1   0   0   GLY GLY C . n 
D 2 2   MET 2   1   1   MET MET C . n 
D 2 3   THR 3   2   2   THR THR C . n 
D 2 4   GLU 4   3   3   GLU GLU C . n 
D 2 5   TYR 5   4   4   TYR TYR C . n 
D 2 6   LYS 6   5   5   LYS LYS C . n 
D 2 7   LEU 7   6   6   LEU LEU C . n 
D 2 8   VAL 8   7   7   VAL VAL C . n 
D 2 9   VAL 9   8   8   VAL VAL C . n 
D 2 10  VAL 10  9   9   VAL VAL C . n 
D 2 11  GLY 11  10  10  GLY GLY C . n 
D 2 12  ALA 12  11  11  ALA ALA C . n 
D 2 13  ASP 13  12  12  ASP ASP C . n 
D 2 14  GLY 14  13  13  GLY GLY C . n 
D 2 15  VAL 15  14  14  VAL VAL C . n 
D 2 16  GLY 16  15  15  GLY GLY C . n 
D 2 17  LYS 17  16  16  LYS LYS C . n 
D 2 18  SER 18  17  17  SER SER C . n 
D 2 19  ALA 19  18  18  ALA ALA C . n 
D 2 20  LEU 20  19  19  LEU LEU C . n 
D 2 21  THR 21  20  20  THR THR C . n 
D 2 22  ILE 22  21  21  ILE ILE C . n 
D 2 23  GLN 23  22  22  GLN GLN C . n 
D 2 24  LEU 24  23  23  LEU LEU C . n 
D 2 25  ILE 25  24  24  ILE ILE C . n 
D 2 26  GLN 26  25  25  GLN GLN C . n 
D 2 27  ASN 27  26  26  ASN ASN C . n 
D 2 28  HIS 28  27  27  HIS HIS C . n 
D 2 29  PHE 29  28  28  PHE PHE C . n 
D 2 30  VAL 30  29  29  VAL VAL C . n 
D 2 31  ASP 31  30  30  ASP ASP C . n 
D 2 32  GLU 32  31  31  GLU GLU C . n 
D 2 33  TYR 33  32  32  TYR TYR C . n 
D 2 34  ASP 34  33  33  ASP ASP C . n 
D 2 35  PRO 35  34  34  PRO PRO C . n 
D 2 36  THR 36  35  35  THR THR C . n 
D 2 37  ILE 37  36  36  ILE ILE C . n 
D 2 38  GLU 38  37  37  GLU GLU C . n 
D 2 39  ASP 39  38  38  ASP ASP C . n 
D 2 40  SER 40  39  39  SER SER C . n 
D 2 41  TYR 41  40  40  TYR TYR C . n 
D 2 42  ARG 42  41  41  ARG ARG C . n 
D 2 43  LYS 43  42  42  LYS LYS C . n 
D 2 44  GLN 44  43  43  GLN GLN C . n 
D 2 45  VAL 45  44  44  VAL VAL C . n 
D 2 46  VAL 46  45  45  VAL VAL C . n 
D 2 47  ILE 47  46  46  ILE ILE C . n 
D 2 48  ASP 48  47  47  ASP ASP C . n 
D 2 49  GLY 49  48  48  GLY GLY C . n 
D 2 50  GLU 50  49  49  GLU GLU C . n 
D 2 51  THR 51  50  50  THR THR C . n 
D 2 52  CYS 52  51  51  CYS CYS C . n 
D 2 53  LEU 53  52  52  LEU LEU C . n 
D 2 54  LEU 54  53  53  LEU LEU C . n 
D 2 55  ASP 55  54  54  ASP ASP C . n 
D 2 56  ILE 56  55  55  ILE ILE C . n 
D 2 57  LEU 57  56  56  LEU LEU C . n 
D 2 58  ASP 58  57  57  ASP ASP C . n 
D 2 59  THR 59  58  58  THR THR C . n 
D 2 60  ALA 60  59  59  ALA ALA C . n 
D 2 61  GLY 61  60  60  GLY GLY C . n 
D 2 62  GLN 62  61  61  GLN GLN C . n 
D 2 63  GLU 63  62  62  GLU GLU C . n 
D 2 64  GLU 64  63  63  GLU GLU C . n 
D 2 65  TYR 65  64  64  TYR TYR C . n 
D 2 66  SER 66  65  65  SER SER C . n 
D 2 67  ALA 67  66  66  ALA ALA C . n 
D 2 68  MET 68  67  67  MET MET C . n 
D 2 69  ARG 69  68  68  ARG ARG C . n 
D 2 70  ASP 70  69  69  ASP ASP C . n 
D 2 71  GLN 71  70  70  GLN GLN C . n 
D 2 72  TYR 72  71  71  TYR TYR C . n 
D 2 73  MET 73  72  72  MET MET C . n 
D 2 74  ARG 74  73  73  ARG ARG C . n 
D 2 75  THR 75  74  74  THR THR C . n 
D 2 76  GLY 76  75  75  GLY GLY C . n 
D 2 77  GLU 77  76  76  GLU GLU C . n 
D 2 78  GLY 78  77  77  GLY GLY C . n 
D 2 79  PHE 79  78  78  PHE PHE C . n 
D 2 80  LEU 80  79  79  LEU LEU C . n 
D 2 81  CYS 81  80  80  CYS CYS C . n 
D 2 82  VAL 82  81  81  VAL VAL C . n 
D 2 83  PHE 83  82  82  PHE PHE C . n 
D 2 84  ALA 84  83  83  ALA ALA C . n 
D 2 85  ILE 85  84  84  ILE ILE C . n 
D 2 86  ASN 86  85  85  ASN ASN C . n 
D 2 87  ASN 87  86  86  ASN ASN C . n 
D 2 88  THR 88  87  87  THR THR C . n 
D 2 89  LYS 89  88  88  LYS LYS C . n 
D 2 90  SER 90  89  89  SER SER C . n 
D 2 91  PHE 91  90  90  PHE PHE C . n 
D 2 92  GLU 92  91  91  GLU GLU C . n 
D 2 93  ASP 93  92  92  ASP ASP C . n 
D 2 94  ILE 94  93  93  ILE ILE C . n 
D 2 95  HIS 95  94  94  HIS HIS C . n 
D 2 96  HIS 96  95  95  HIS HIS C . n 
D 2 97  TYR 97  96  96  TYR TYR C . n 
D 2 98  ARG 98  97  97  ARG ARG C . n 
D 2 99  GLU 99  98  98  GLU GLU C . n 
D 2 100 GLN 100 99  99  GLN GLN C . n 
D 2 101 ILE 101 100 100 ILE ILE C . n 
D 2 102 LYS 102 101 101 LYS LYS C . n 
D 2 103 ARG 103 102 102 ARG ARG C . n 
D 2 104 VAL 104 103 103 VAL VAL C . n 
D 2 105 LYS 105 104 104 LYS LYS C . n 
D 2 106 ASP 106 105 105 ASP ASP C . n 
D 2 107 SER 107 106 106 SER SER C . n 
D 2 108 GLU 108 107 107 GLU GLU C . n 
D 2 109 ASP 109 108 108 ASP ASP C . n 
D 2 110 VAL 110 109 109 VAL VAL C . n 
D 2 111 PRO 111 110 110 PRO PRO C . n 
D 2 112 MET 112 111 111 MET MET C . n 
D 2 113 VAL 113 112 112 VAL VAL C . n 
D 2 114 LEU 114 113 113 LEU LEU C . n 
D 2 115 VAL 115 114 114 VAL VAL C . n 
D 2 116 GLY 116 115 115 GLY GLY C . n 
D 2 117 ASN 117 116 116 ASN ASN C . n 
D 2 118 LYS 118 117 117 LYS LYS C . n 
D 2 119 CYS 119 118 118 CYS CYS C . n 
D 2 120 ASP 120 119 119 ASP ASP C . n 
D 2 121 LEU 121 120 120 LEU LEU C . n 
D 2 122 PRO 122 121 121 PRO PRO C . n 
D 2 123 SER 123 122 122 SER SER C . n 
D 2 124 ARG 124 123 123 ARG ARG C . n 
D 2 125 THR 125 124 124 THR THR C . n 
D 2 126 VAL 126 125 125 VAL VAL C . n 
D 2 127 ASP 127 126 126 ASP ASP C . n 
D 2 128 THR 128 127 127 THR THR C . n 
D 2 129 LYS 129 128 128 LYS LYS C . n 
D 2 130 GLN 130 129 129 GLN GLN C . n 
D 2 131 ALA 131 130 130 ALA ALA C . n 
D 2 132 GLN 132 131 131 GLN GLN C . n 
D 2 133 ASP 133 132 132 ASP ASP C . n 
D 2 134 LEU 134 133 133 LEU LEU C . n 
D 2 135 ALA 135 134 134 ALA ALA C . n 
D 2 136 ARG 136 135 135 ARG ARG C . n 
D 2 137 SER 137 136 136 SER SER C . n 
D 2 138 TYR 138 137 137 TYR TYR C . n 
D 2 139 GLY 139 138 138 GLY GLY C . n 
D 2 140 ILE 140 139 139 ILE ILE C . n 
D 2 141 PRO 141 140 140 PRO PRO C . n 
D 2 142 PHE 142 141 141 PHE PHE C . n 
D 2 143 ILE 143 142 142 ILE ILE C . n 
D 2 144 GLU 144 143 143 GLU GLU C . n 
D 2 145 THR 145 144 144 THR THR C . n 
D 2 146 SER 146 145 145 SER SER C . n 
D 2 147 ALA 147 146 146 ALA ALA C . n 
D 2 148 LYS 148 147 147 LYS LYS C . n 
D 2 149 THR 149 148 148 THR THR C . n 
D 2 150 ARG 150 149 149 ARG ARG C . n 
D 2 151 GLN 151 150 150 GLN GLN C . n 
D 2 152 GLY 152 151 151 GLY GLY C . n 
D 2 153 VAL 153 152 152 VAL VAL C . n 
D 2 154 ASP 154 153 153 ASP ASP C . n 
D 2 155 ASP 155 154 154 ASP ASP C . n 
D 2 156 ALA 156 155 155 ALA ALA C . n 
D 2 157 PHE 157 156 156 PHE PHE C . n 
D 2 158 TYR 158 157 157 TYR TYR C . n 
D 2 159 THR 159 158 158 THR THR C . n 
D 2 160 LEU 160 159 159 LEU LEU C . n 
D 2 161 VAL 161 160 160 VAL VAL C . n 
D 2 162 ARG 162 161 161 ARG ARG C . n 
D 2 163 GLU 163 162 162 GLU GLU C . n 
D 2 164 ILE 164 163 163 ILE ILE C . n 
D 2 165 ARG 165 164 164 ARG ARG C . n 
D 2 166 LYS 166 165 165 LYS LYS C . n 
D 2 167 HIS 167 166 166 HIS HIS C . n 
D 2 168 LYS 168 167 167 LYS LYS C . n 
D 2 169 GLU 169 168 ?   ?   ?   C . n 
D 2 170 LYS 170 169 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZNI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZNI 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 ZNI 1   201 201 ZNI ZNI B . 
F 3 ZNI 1   201 201 ZNI ZNI D . 
G 4 GDP 1   201 201 GDP GDP A . 
H 5 MG  1   202 202 MG  MG  A . 
I 4 GDP 1   201 201 GDP GDP C . 
J 5 MG  1   202 202 MG  MG  C . 
K 6 AF3 1   203 203 AF3 AF3 C . 
L 7 HOH 1   301 291 HOH HOH B . 
L 7 HOH 2   302 631 HOH HOH B . 
L 7 HOH 3   303 311 HOH HOH B . 
L 7 HOH 4   304 365 HOH HOH B . 
L 7 HOH 5   305 304 HOH HOH B . 
L 7 HOH 6   306 213 HOH HOH B . 
L 7 HOH 7   307 158 HOH HOH B . 
L 7 HOH 8   308 484 HOH HOH B . 
L 7 HOH 9   309 641 HOH HOH B . 
L 7 HOH 10  310 198 HOH HOH B . 
L 7 HOH 11  311 502 HOH HOH B . 
L 7 HOH 12  312 445 HOH HOH B . 
L 7 HOH 13  313 455 HOH HOH B . 
L 7 HOH 14  314 276 HOH HOH B . 
L 7 HOH 15  315 566 HOH HOH B . 
L 7 HOH 16  316 246 HOH HOH B . 
L 7 HOH 17  317 529 HOH HOH B . 
L 7 HOH 18  318 575 HOH HOH B . 
L 7 HOH 19  319 85  HOH HOH B . 
L 7 HOH 20  320 513 HOH HOH B . 
L 7 HOH 21  321 29  HOH HOH B . 
L 7 HOH 22  322 545 HOH HOH B . 
L 7 HOH 23  323 40  HOH HOH B . 
L 7 HOH 24  324 361 HOH HOH B . 
L 7 HOH 25  325 460 HOH HOH B . 
L 7 HOH 26  326 146 HOH HOH B . 
L 7 HOH 27  327 181 HOH HOH B . 
L 7 HOH 28  328 166 HOH HOH B . 
L 7 HOH 29  329 425 HOH HOH B . 
L 7 HOH 30  330 551 HOH HOH B . 
L 7 HOH 31  331 183 HOH HOH B . 
L 7 HOH 32  332 144 HOH HOH B . 
L 7 HOH 33  333 252 HOH HOH B . 
L 7 HOH 34  334 4   HOH HOH B . 
L 7 HOH 35  335 240 HOH HOH B . 
L 7 HOH 36  336 24  HOH HOH B . 
L 7 HOH 37  337 427 HOH HOH B . 
L 7 HOH 38  338 606 HOH HOH B . 
L 7 HOH 39  339 623 HOH HOH B . 
L 7 HOH 40  340 116 HOH HOH B . 
L 7 HOH 41  341 79  HOH HOH B . 
L 7 HOH 42  342 327 HOH HOH B . 
L 7 HOH 43  343 101 HOH HOH B . 
L 7 HOH 44  344 62  HOH HOH B . 
L 7 HOH 45  345 230 HOH HOH B . 
L 7 HOH 46  346 343 HOH HOH B . 
L 7 HOH 47  347 94  HOH HOH B . 
L 7 HOH 48  348 197 HOH HOH B . 
L 7 HOH 49  349 11  HOH HOH B . 
L 7 HOH 50  350 163 HOH HOH B . 
L 7 HOH 51  351 7   HOH HOH B . 
L 7 HOH 52  352 253 HOH HOH B . 
L 7 HOH 53  353 334 HOH HOH B . 
L 7 HOH 54  354 377 HOH HOH B . 
L 7 HOH 55  355 282 HOH HOH B . 
L 7 HOH 56  356 612 HOH HOH B . 
L 7 HOH 57  357 269 HOH HOH B . 
L 7 HOH 58  358 78  HOH HOH B . 
L 7 HOH 59  359 34  HOH HOH B . 
L 7 HOH 60  360 236 HOH HOH B . 
L 7 HOH 61  361 131 HOH HOH B . 
L 7 HOH 62  362 53  HOH HOH B . 
L 7 HOH 63  363 140 HOH HOH B . 
L 7 HOH 64  364 33  HOH HOH B . 
L 7 HOH 65  365 98  HOH HOH B . 
L 7 HOH 66  366 106 HOH HOH B . 
L 7 HOH 67  367 25  HOH HOH B . 
L 7 HOH 68  368 5   HOH HOH B . 
L 7 HOH 69  369 16  HOH HOH B . 
L 7 HOH 70  370 202 HOH HOH B . 
L 7 HOH 71  371 572 HOH HOH B . 
L 7 HOH 72  372 84  HOH HOH B . 
L 7 HOH 73  373 627 HOH HOH B . 
L 7 HOH 74  374 136 HOH HOH B . 
L 7 HOH 75  375 561 HOH HOH B . 
L 7 HOH 76  376 142 HOH HOH B . 
L 7 HOH 77  377 492 HOH HOH B . 
L 7 HOH 78  378 30  HOH HOH B . 
L 7 HOH 79  379 244 HOH HOH B . 
L 7 HOH 80  380 336 HOH HOH B . 
L 7 HOH 81  381 310 HOH HOH B . 
L 7 HOH 82  382 122 HOH HOH B . 
L 7 HOH 83  383 32  HOH HOH B . 
L 7 HOH 84  384 207 HOH HOH B . 
L 7 HOH 85  385 587 HOH HOH B . 
L 7 HOH 86  386 437 HOH HOH B . 
L 7 HOH 87  387 35  HOH HOH B . 
L 7 HOH 88  388 398 HOH HOH B . 
L 7 HOH 89  389 283 HOH HOH B . 
L 7 HOH 90  390 154 HOH HOH B . 
L 7 HOH 91  391 360 HOH HOH B . 
L 7 HOH 92  392 406 HOH HOH B . 
L 7 HOH 93  393 104 HOH HOH B . 
L 7 HOH 94  394 23  HOH HOH B . 
L 7 HOH 95  395 110 HOH HOH B . 
L 7 HOH 96  396 103 HOH HOH B . 
L 7 HOH 97  397 69  HOH HOH B . 
L 7 HOH 98  398 504 HOH HOH B . 
L 7 HOH 99  399 457 HOH HOH B . 
L 7 HOH 100 400 302 HOH HOH B . 
L 7 HOH 101 401 156 HOH HOH B . 
L 7 HOH 102 402 546 HOH HOH B . 
L 7 HOH 103 403 42  HOH HOH B . 
L 7 HOH 104 404 611 HOH HOH B . 
L 7 HOH 105 405 582 HOH HOH B . 
L 7 HOH 106 406 170 HOH HOH B . 
L 7 HOH 107 407 89  HOH HOH B . 
L 7 HOH 108 408 288 HOH HOH B . 
L 7 HOH 109 409 178 HOH HOH B . 
L 7 HOH 110 410 97  HOH HOH B . 
L 7 HOH 111 411 31  HOH HOH B . 
L 7 HOH 112 412 212 HOH HOH B . 
L 7 HOH 113 413 224 HOH HOH B . 
L 7 HOH 114 414 588 HOH HOH B . 
L 7 HOH 115 415 200 HOH HOH B . 
L 7 HOH 116 416 339 HOH HOH B . 
L 7 HOH 117 417 638 HOH HOH B . 
L 7 HOH 118 418 383 HOH HOH B . 
L 7 HOH 119 419 314 HOH HOH B . 
L 7 HOH 120 420 605 HOH HOH B . 
L 7 HOH 121 421 118 HOH HOH B . 
L 7 HOH 122 422 574 HOH HOH B . 
L 7 HOH 123 423 241 HOH HOH B . 
L 7 HOH 124 424 402 HOH HOH B . 
L 7 HOH 125 425 417 HOH HOH B . 
L 7 HOH 126 426 275 HOH HOH B . 
L 7 HOH 127 427 569 HOH HOH B . 
L 7 HOH 128 428 607 HOH HOH B . 
L 7 HOH 129 429 326 HOH HOH B . 
L 7 HOH 130 430 348 HOH HOH B . 
L 7 HOH 131 431 352 HOH HOH B . 
L 7 HOH 132 432 552 HOH HOH B . 
L 7 HOH 133 433 168 HOH HOH B . 
L 7 HOH 134 434 199 HOH HOH B . 
L 7 HOH 135 435 562 HOH HOH B . 
L 7 HOH 136 436 474 HOH HOH B . 
L 7 HOH 137 437 556 HOH HOH B . 
L 7 HOH 138 438 463 HOH HOH B . 
L 7 HOH 139 439 488 HOH HOH B . 
L 7 HOH 140 440 555 HOH HOH B . 
L 7 HOH 141 441 172 HOH HOH B . 
L 7 HOH 142 442 338 HOH HOH B . 
L 7 HOH 143 443 579 HOH HOH B . 
L 7 HOH 144 444 637 HOH HOH B . 
L 7 HOH 145 445 603 HOH HOH B . 
L 7 HOH 146 446 186 HOH HOH B . 
L 7 HOH 147 447 486 HOH HOH B . 
L 7 HOH 148 448 433 HOH HOH B . 
L 7 HOH 149 449 535 HOH HOH B . 
L 7 HOH 150 450 285 HOH HOH B . 
L 7 HOH 151 451 563 HOH HOH B . 
L 7 HOH 152 452 578 HOH HOH B . 
L 7 HOH 153 453 405 HOH HOH B . 
L 7 HOH 154 454 300 HOH HOH B . 
L 7 HOH 155 455 568 HOH HOH B . 
L 7 HOH 156 456 129 HOH HOH B . 
L 7 HOH 157 457 621 HOH HOH B . 
L 7 HOH 158 458 472 HOH HOH B . 
L 7 HOH 159 459 243 HOH HOH B . 
L 7 HOH 160 460 192 HOH HOH B . 
M 7 HOH 1   301 134 HOH HOH D . 
M 7 HOH 2   302 396 HOH HOH D . 
M 7 HOH 3   303 367 HOH HOH D . 
M 7 HOH 4   304 549 HOH HOH D . 
M 7 HOH 5   305 171 HOH HOH D . 
M 7 HOH 6   306 221 HOH HOH D . 
M 7 HOH 7   307 550 HOH HOH D . 
M 7 HOH 8   308 391 HOH HOH D . 
M 7 HOH 9   309 83  HOH HOH D . 
M 7 HOH 10  310 52  HOH HOH D . 
M 7 HOH 11  311 46  HOH HOH D . 
M 7 HOH 12  312 251 HOH HOH D . 
M 7 HOH 13  313 416 HOH HOH D . 
M 7 HOH 14  314 505 HOH HOH D . 
M 7 HOH 15  315 105 HOH HOH D . 
M 7 HOH 16  316 58  HOH HOH D . 
M 7 HOH 17  317 187 HOH HOH D . 
M 7 HOH 18  318 226 HOH HOH D . 
M 7 HOH 19  319 544 HOH HOH D . 
M 7 HOH 20  320 303 HOH HOH D . 
M 7 HOH 21  321 229 HOH HOH D . 
M 7 HOH 22  322 150 HOH HOH D . 
M 7 HOH 23  323 18  HOH HOH D . 
M 7 HOH 24  324 74  HOH HOH D . 
M 7 HOH 25  325 523 HOH HOH D . 
M 7 HOH 26  326 193 HOH HOH D . 
M 7 HOH 27  327 13  HOH HOH D . 
M 7 HOH 28  328 152 HOH HOH D . 
M 7 HOH 29  329 2   HOH HOH D . 
M 7 HOH 30  330 51  HOH HOH D . 
M 7 HOH 31  331 126 HOH HOH D . 
M 7 HOH 32  332 57  HOH HOH D . 
M 7 HOH 33  333 109 HOH HOH D . 
M 7 HOH 34  334 350 HOH HOH D . 
M 7 HOH 35  335 64  HOH HOH D . 
M 7 HOH 36  336 249 HOH HOH D . 
M 7 HOH 37  337 508 HOH HOH D . 
M 7 HOH 38  338 72  HOH HOH D . 
M 7 HOH 39  339 36  HOH HOH D . 
M 7 HOH 40  340 228 HOH HOH D . 
M 7 HOH 41  341 164 HOH HOH D . 
M 7 HOH 42  342 102 HOH HOH D . 
M 7 HOH 43  343 266 HOH HOH D . 
M 7 HOH 44  344 38  HOH HOH D . 
M 7 HOH 45  345 70  HOH HOH D . 
M 7 HOH 46  346 206 HOH HOH D . 
M 7 HOH 47  347 6   HOH HOH D . 
M 7 HOH 48  348 8   HOH HOH D . 
M 7 HOH 49  349 167 HOH HOH D . 
M 7 HOH 50  350 68  HOH HOH D . 
M 7 HOH 51  351 565 HOH HOH D . 
M 7 HOH 52  352 9   HOH HOH D . 
M 7 HOH 53  353 67  HOH HOH D . 
M 7 HOH 54  354 20  HOH HOH D . 
M 7 HOH 55  355 214 HOH HOH D . 
M 7 HOH 56  356 41  HOH HOH D . 
M 7 HOH 57  357 133 HOH HOH D . 
M 7 HOH 58  358 37  HOH HOH D . 
M 7 HOH 59  359 143 HOH HOH D . 
M 7 HOH 60  360 617 HOH HOH D . 
M 7 HOH 61  361 112 HOH HOH D . 
M 7 HOH 62  362 60  HOH HOH D . 
M 7 HOH 63  363 344 HOH HOH D . 
M 7 HOH 64  364 55  HOH HOH D . 
M 7 HOH 65  365 92  HOH HOH D . 
M 7 HOH 66  366 397 HOH HOH D . 
M 7 HOH 67  367 151 HOH HOH D . 
M 7 HOH 68  368 520 HOH HOH D . 
M 7 HOH 69  369 589 HOH HOH D . 
M 7 HOH 70  370 203 HOH HOH D . 
M 7 HOH 71  371 21  HOH HOH D . 
M 7 HOH 72  372 341 HOH HOH D . 
M 7 HOH 73  373 647 HOH HOH D . 
M 7 HOH 74  374 162 HOH HOH D . 
M 7 HOH 75  375 107 HOH HOH D . 
M 7 HOH 76  376 625 HOH HOH D . 
M 7 HOH 77  377 19  HOH HOH D . 
M 7 HOH 78  378 216 HOH HOH D . 
M 7 HOH 79  379 194 HOH HOH D . 
M 7 HOH 80  380 147 HOH HOH D . 
M 7 HOH 81  381 329 HOH HOH D . 
M 7 HOH 82  382 99  HOH HOH D . 
M 7 HOH 83  383 222 HOH HOH D . 
M 7 HOH 84  384 452 HOH HOH D . 
M 7 HOH 85  385 91  HOH HOH D . 
M 7 HOH 86  386 295 HOH HOH D . 
M 7 HOH 87  387 309 HOH HOH D . 
M 7 HOH 88  388 274 HOH HOH D . 
M 7 HOH 89  389 45  HOH HOH D . 
M 7 HOH 90  390 77  HOH HOH D . 
M 7 HOH 91  391 495 HOH HOH D . 
M 7 HOH 92  392 528 HOH HOH D . 
M 7 HOH 93  393 465 HOH HOH D . 
M 7 HOH 94  394 177 HOH HOH D . 
M 7 HOH 95  395 394 HOH HOH D . 
M 7 HOH 96  396 268 HOH HOH D . 
M 7 HOH 97  397 649 HOH HOH D . 
M 7 HOH 98  398 628 HOH HOH D . 
M 7 HOH 99  399 342 HOH HOH D . 
M 7 HOH 100 400 355 HOH HOH D . 
M 7 HOH 101 401 532 HOH HOH D . 
M 7 HOH 102 402 262 HOH HOH D . 
M 7 HOH 103 403 530 HOH HOH D . 
M 7 HOH 104 404 419 HOH HOH D . 
M 7 HOH 105 405 645 HOH HOH D . 
M 7 HOH 106 406 354 HOH HOH D . 
M 7 HOH 107 407 639 HOH HOH D . 
M 7 HOH 108 408 507 HOH HOH D . 
M 7 HOH 109 409 245 HOH HOH D . 
M 7 HOH 110 410 424 HOH HOH D . 
M 7 HOH 111 411 318 HOH HOH D . 
M 7 HOH 112 412 317 HOH HOH D . 
M 7 HOH 113 413 239 HOH HOH D . 
M 7 HOH 114 414 386 HOH HOH D . 
M 7 HOH 115 415 510 HOH HOH D . 
M 7 HOH 116 416 135 HOH HOH D . 
M 7 HOH 117 417 399 HOH HOH D . 
M 7 HOH 118 418 501 HOH HOH D . 
N 7 HOH 1   301 153 HOH HOH A . 
N 7 HOH 2   302 61  HOH HOH A . 
N 7 HOH 3   303 471 HOH HOH A . 
N 7 HOH 4   304 175 HOH HOH A . 
N 7 HOH 5   305 75  HOH HOH A . 
N 7 HOH 6   306 176 HOH HOH A . 
N 7 HOH 7   307 525 HOH HOH A . 
N 7 HOH 8   308 421 HOH HOH A . 
N 7 HOH 9   309 591 HOH HOH A . 
N 7 HOH 10  310 585 HOH HOH A . 
N 7 HOH 11  311 195 HOH HOH A . 
N 7 HOH 12  312 384 HOH HOH A . 
N 7 HOH 13  313 435 HOH HOH A . 
N 7 HOH 14  314 225 HOH HOH A . 
N 7 HOH 15  315 71  HOH HOH A . 
N 7 HOH 16  316 521 HOH HOH A . 
N 7 HOH 17  317 392 HOH HOH A . 
N 7 HOH 18  318 108 HOH HOH A . 
N 7 HOH 19  319 50  HOH HOH A . 
N 7 HOH 20  320 368 HOH HOH A . 
N 7 HOH 21  321 353 HOH HOH A . 
N 7 HOH 22  322 73  HOH HOH A . 
N 7 HOH 23  323 335 HOH HOH A . 
N 7 HOH 24  324 185 HOH HOH A . 
N 7 HOH 25  325 174 HOH HOH A . 
N 7 HOH 26  326 539 HOH HOH A . 
N 7 HOH 27  327 22  HOH HOH A . 
N 7 HOH 28  328 3   HOH HOH A . 
N 7 HOH 29  329 604 HOH HOH A . 
N 7 HOH 30  330 480 HOH HOH A . 
N 7 HOH 31  331 87  HOH HOH A . 
N 7 HOH 32  332 59  HOH HOH A . 
N 7 HOH 33  333 436 HOH HOH A . 
N 7 HOH 34  334 145 HOH HOH A . 
N 7 HOH 35  335 382 HOH HOH A . 
N 7 HOH 36  336 440 HOH HOH A . 
N 7 HOH 37  337 320 HOH HOH A . 
N 7 HOH 38  338 82  HOH HOH A . 
N 7 HOH 39  339 12  HOH HOH A . 
N 7 HOH 40  340 287 HOH HOH A . 
N 7 HOH 41  341 189 HOH HOH A . 
N 7 HOH 42  342 184 HOH HOH A . 
N 7 HOH 43  343 90  HOH HOH A . 
N 7 HOH 44  344 28  HOH HOH A . 
N 7 HOH 45  345 1   HOH HOH A . 
N 7 HOH 46  346 49  HOH HOH A . 
N 7 HOH 47  347 567 HOH HOH A . 
N 7 HOH 48  348 157 HOH HOH A . 
N 7 HOH 49  349 15  HOH HOH A . 
N 7 HOH 50  350 477 HOH HOH A . 
N 7 HOH 51  351 509 HOH HOH A . 
N 7 HOH 52  352 459 HOH HOH A . 
N 7 HOH 53  353 543 HOH HOH A . 
N 7 HOH 54  354 130 HOH HOH A . 
N 7 HOH 55  355 39  HOH HOH A . 
N 7 HOH 56  356 577 HOH HOH A . 
N 7 HOH 57  357 115 HOH HOH A . 
N 7 HOH 58  358 165 HOH HOH A . 
N 7 HOH 59  359 422 HOH HOH A . 
N 7 HOH 60  360 81  HOH HOH A . 
N 7 HOH 61  361 43  HOH HOH A . 
N 7 HOH 62  362 414 HOH HOH A . 
N 7 HOH 63  363 613 HOH HOH A . 
N 7 HOH 64  364 385 HOH HOH A . 
N 7 HOH 65  365 346 HOH HOH A . 
N 7 HOH 66  366 231 HOH HOH A . 
N 7 HOH 67  367 499 HOH HOH A . 
N 7 HOH 68  368 468 HOH HOH A . 
N 7 HOH 69  369 467 HOH HOH A . 
N 7 HOH 70  370 56  HOH HOH A . 
N 7 HOH 71  371 273 HOH HOH A . 
N 7 HOH 72  372 442 HOH HOH A . 
N 7 HOH 73  373 260 HOH HOH A . 
N 7 HOH 74  374 139 HOH HOH A . 
N 7 HOH 75  375 14  HOH HOH A . 
N 7 HOH 76  376 292 HOH HOH A . 
N 7 HOH 77  377 356 HOH HOH A . 
N 7 HOH 78  378 63  HOH HOH A . 
N 7 HOH 79  379 323 HOH HOH A . 
N 7 HOH 80  380 219 HOH HOH A . 
N 7 HOH 81  381 584 HOH HOH A . 
N 7 HOH 82  382 438 HOH HOH A . 
N 7 HOH 83  383 517 HOH HOH A . 
N 7 HOH 84  384 205 HOH HOH A . 
N 7 HOH 85  385 449 HOH HOH A . 
N 7 HOH 86  386 411 HOH HOH A . 
N 7 HOH 87  387 258 HOH HOH A . 
N 7 HOH 88  388 443 HOH HOH A . 
N 7 HOH 89  389 478 HOH HOH A . 
N 7 HOH 90  390 496 HOH HOH A . 
N 7 HOH 91  391 464 HOH HOH A . 
N 7 HOH 92  392 120 HOH HOH A . 
N 7 HOH 93  393 296 HOH HOH A . 
N 7 HOH 94  394 132 HOH HOH A . 
N 7 HOH 95  395 182 HOH HOH A . 
N 7 HOH 96  396 149 HOH HOH A . 
N 7 HOH 97  397 65  HOH HOH A . 
N 7 HOH 98  398 223 HOH HOH A . 
N 7 HOH 99  399 503 HOH HOH A . 
N 7 HOH 100 400 592 HOH HOH A . 
N 7 HOH 101 401 489 HOH HOH A . 
N 7 HOH 102 402 473 HOH HOH A . 
N 7 HOH 103 403 220 HOH HOH A . 
N 7 HOH 104 404 497 HOH HOH A . 
N 7 HOH 105 405 487 HOH HOH A . 
N 7 HOH 106 406 407 HOH HOH A . 
N 7 HOH 107 407 401 HOH HOH A . 
N 7 HOH 108 408 211 HOH HOH A . 
N 7 HOH 109 409 596 HOH HOH A . 
N 7 HOH 110 410 622 HOH HOH A . 
N 7 HOH 111 411 257 HOH HOH A . 
N 7 HOH 112 412 571 HOH HOH A . 
N 7 HOH 113 413 359 HOH HOH A . 
N 7 HOH 114 414 325 HOH HOH A . 
N 7 HOH 115 415 299 HOH HOH A . 
N 7 HOH 116 416 330 HOH HOH A . 
N 7 HOH 117 417 255 HOH HOH A . 
N 7 HOH 118 418 479 HOH HOH A . 
N 7 HOH 119 419 524 HOH HOH A . 
N 7 HOH 120 420 580 HOH HOH A . 
N 7 HOH 121 421 441 HOH HOH A . 
N 7 HOH 122 422 640 HOH HOH A . 
N 7 HOH 123 423 636 HOH HOH A . 
O 7 HOH 1   301 409 HOH HOH C . 
O 7 HOH 2   302 369 HOH HOH C . 
O 7 HOH 3   303 609 HOH HOH C . 
O 7 HOH 4   304 80  HOH HOH C . 
O 7 HOH 5   305 278 HOH HOH C . 
O 7 HOH 6   306 600 HOH HOH C . 
O 7 HOH 7   307 651 HOH HOH C . 
O 7 HOH 8   308 374 HOH HOH C . 
O 7 HOH 9   309 375 HOH HOH C . 
O 7 HOH 10  310 537 HOH HOH C . 
O 7 HOH 11  311 250 HOH HOH C . 
O 7 HOH 12  312 634 HOH HOH C . 
O 7 HOH 13  313 559 HOH HOH C . 
O 7 HOH 14  314 281 HOH HOH C . 
O 7 HOH 15  315 279 HOH HOH C . 
O 7 HOH 16  316 44  HOH HOH C . 
O 7 HOH 17  317 233 HOH HOH C . 
O 7 HOH 18  318 26  HOH HOH C . 
O 7 HOH 19  319 54  HOH HOH C . 
O 7 HOH 20  320 541 HOH HOH C . 
O 7 HOH 21  321 648 HOH HOH C . 
O 7 HOH 22  322 511 HOH HOH C . 
O 7 HOH 23  323 148 HOH HOH C . 
O 7 HOH 24  324 593 HOH HOH C . 
O 7 HOH 25  325 47  HOH HOH C . 
O 7 HOH 26  326 629 HOH HOH C . 
O 7 HOH 27  327 540 HOH HOH C . 
O 7 HOH 28  328 27  HOH HOH C . 
O 7 HOH 29  329 270 HOH HOH C . 
O 7 HOH 30  330 128 HOH HOH C . 
O 7 HOH 31  331 650 HOH HOH C . 
O 7 HOH 32  332 345 HOH HOH C . 
O 7 HOH 33  333 630 HOH HOH C . 
O 7 HOH 34  334 564 HOH HOH C . 
O 7 HOH 35  335 624 HOH HOH C . 
O 7 HOH 36  336 358 HOH HOH C . 
O 7 HOH 37  337 614 HOH HOH C . 
O 7 HOH 38  338 117 HOH HOH C . 
O 7 HOH 39  339 114 HOH HOH C . 
O 7 HOH 40  340 554 HOH HOH C . 
O 7 HOH 41  341 76  HOH HOH C . 
O 7 HOH 42  342 204 HOH HOH C . 
O 7 HOH 43  343 586 HOH HOH C . 
O 7 HOH 44  344 88  HOH HOH C . 
O 7 HOH 45  345 423 HOH HOH C . 
O 7 HOH 46  346 626 HOH HOH C . 
O 7 HOH 47  347 237 HOH HOH C . 
O 7 HOH 48  348 366 HOH HOH C . 
O 7 HOH 49  349 547 HOH HOH C . 
O 7 HOH 50  350 232 HOH HOH C . 
O 7 HOH 51  351 635 HOH HOH C . 
O 7 HOH 52  352 215 HOH HOH C . 
O 7 HOH 53  353 17  HOH HOH C . 
O 7 HOH 54  354 86  HOH HOH C . 
O 7 HOH 55  355 576 HOH HOH C . 
O 7 HOH 56  356 601 HOH HOH C . 
O 7 HOH 57  357 610 HOH HOH C . 
O 7 HOH 58  358 633 HOH HOH C . 
O 7 HOH 59  359 602 HOH HOH C . 
O 7 HOH 60  360 599 HOH HOH C . 
O 7 HOH 61  361 548 HOH HOH C . 
O 7 HOH 62  362 430 HOH HOH C . 
O 7 HOH 63  363 307 HOH HOH C . 
O 7 HOH 64  364 619 HOH HOH C . 
O 7 HOH 65  365 264 HOH HOH C . 
O 7 HOH 66  366 48  HOH HOH C . 
O 7 HOH 67  367 191 HOH HOH C . 
O 7 HOH 68  368 389 HOH HOH C . 
O 7 HOH 69  369 598 HOH HOH C . 
O 7 HOH 70  370 466 HOH HOH C . 
O 7 HOH 71  371 180 HOH HOH C . 
O 7 HOH 72  372 518 HOH HOH C . 
O 7 HOH 73  373 615 HOH HOH C . 
O 7 HOH 74  374 238 HOH HOH C . 
O 7 HOH 75  375 475 HOH HOH C . 
O 7 HOH 76  376 583 HOH HOH C . 
O 7 HOH 77  377 553 HOH HOH C . 
O 7 HOH 78  378 646 HOH HOH C . 
O 7 HOH 79  379 573 HOH HOH C . 
O 7 HOH 80  380 597 HOH HOH C . 
O 7 HOH 81  381 208 HOH HOH C . 
O 7 HOH 82  382 301 HOH HOH C . 
O 7 HOH 83  383 362 HOH HOH C . 
O 7 HOH 84  384 531 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 C ARG 68  ? CG  ? D ARG 69  CG  
2  1 Y 1 C ARG 68  ? CD  ? D ARG 69  CD  
3  1 Y 1 C ARG 68  ? NE  ? D ARG 69  NE  
4  1 Y 1 C ARG 68  ? CZ  ? D ARG 69  CZ  
5  1 Y 1 C ARG 68  ? NH1 ? D ARG 69  NH1 
6  1 Y 1 C ARG 68  ? NH2 ? D ARG 69  NH2 
7  1 Y 1 C LYS 165 ? CG  ? D LYS 166 CG  
8  1 Y 1 C LYS 165 ? CD  ? D LYS 166 CD  
9  1 Y 1 C LYS 165 ? CE  ? D LYS 166 CE  
10 1 Y 1 C LYS 165 ? NZ  ? D LYS 166 NZ  
11 1 Y 1 C HIS 166 ? CG  ? D HIS 167 CG  
12 1 Y 1 C HIS 166 ? ND1 ? D HIS 167 ND1 
13 1 Y 1 C HIS 166 ? CD2 ? D HIS 167 CD2 
14 1 Y 1 C HIS 166 ? CE1 ? D HIS 167 CE1 
15 1 Y 1 C HIS 166 ? NE2 ? D HIS 167 NE2 
16 1 Y 1 C LYS 167 ? CG  ? D LYS 168 CG  
17 1 Y 1 C LYS 167 ? CD  ? D LYS 168 CD  
18 1 Y 1 C LYS 167 ? CE  ? D LYS 168 CE  
19 1 Y 1 C LYS 167 ? NZ  ? D LYS 168 NZ  
# 
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'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    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                     9BGH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.483 
_cell.length_a_esd                 ? 
_cell.length_b                     81.787 
_cell.length_b_esd                 ? 
_cell.length_c                     127.832 
_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                         9BGH 
_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                   9BGH 
_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             2.28 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.13 
_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, 22% PEG 8K.' 
_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         2023-10-09 
_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   0.9793 
_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        0.9793 
_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                                       9BGH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.175 
_reflns.d_resolution_low                               34.45 
_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                                     77267 
_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                           74.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.4 
_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                                ? 
_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                                   0.998 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
1.452 1.461 ? ? ? ? ? ? 2232 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1 1 0.0518 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1.533 1.545 ? ? ? ? ? ? 2318 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 0.1736 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1.582 1.595 ? ? ? ? ? ? 2279 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 3 1 0.1888 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1.637 1.652 ? ? ? ? ? ? 2190 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 4 1 0.3034 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_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                                 9BGH 
_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                             33.48 
_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                     77261 
_refine.ls_number_reflns_R_free                  3928 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.96 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2193 
_refine.ls_R_factor_R_free                       0.2509 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2176 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       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                 27.26 
_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                            0.28 
_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.pdbx_number_atoms_protein        5166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         186 
_refine_hist.number_atoms_solvent             485 
_refine_hist.number_atoms_total               5837 
_refine_hist.d_res_high                       1.65 
_refine_hist.d_res_low                        33.48 
# 
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' ? 0.018  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.531  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.749 ? 782 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.084  ? 789 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 946 ? 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  . . 138 2752 98.00  . . . . 0.3955 . . . . . . . . . . . 0.4651 
'X-RAY DIFFRACTION' 1.67 1.69  . . 160 2714 98.00  . . . . 0.3731 . . . . . . . . . . . 0.4482 
'X-RAY DIFFRACTION' 1.69 1.71  . . 135 2801 100.00 . . . . 0.3418 . . . . . . . . . . . 0.3601 
'X-RAY DIFFRACTION' 1.71 1.74  . . 147 2734 99.00  . . . . 0.3411 . . . . . . . . . . . 0.3952 
'X-RAY DIFFRACTION' 1.74 1.76  . . 147 2781 100.00 . . . . 0.3074 . . . . . . . . . . . 0.3315 
'X-RAY DIFFRACTION' 1.76 1.79  . . 127 2807 100.00 . . . . 0.2930 . . . . . . . . . . . 0.3426 
'X-RAY DIFFRACTION' 1.79 1.82  . . 177 2785 100.00 . . . . 0.2769 . . . . . . . . . . . 0.3105 
'X-RAY DIFFRACTION' 1.82 1.85  . . 184 2719 100.00 . . . . 0.2659 . . . . . . . . . . . 0.3151 
'X-RAY DIFFRACTION' 1.85 1.88  . . 160 2803 100.00 . . . . 0.2492 . . . . . . . . . . . 0.3219 
'X-RAY DIFFRACTION' 1.88 1.90  . . 105 2071 100.00 . . . . 0.2450 . . . . . . . . . . . 0.2615 
'X-RAY DIFFRACTION' 1.93 1.95  . . 93  1758 99.00  . . . . 0.2523 . . . . . . . . . . . 0.2913 
'X-RAY DIFFRACTION' 1.95 1.99  . . 142 2797 100.00 . . . . 0.2507 . . . . . . . . . . . 0.3355 
'X-RAY DIFFRACTION' 1.99 2.03  . . 156 2782 100.00 . . . . 0.2524 . . . . . . . . . . . 0.2949 
'X-RAY DIFFRACTION' 2.03 2.05  . . 60  1254 99.00  . . . . 0.2638 . . . . . . . . . . . 0.2838 
'X-RAY DIFFRACTION' 2.09 2.13  . . 128 2397 99.00  . . . . 0.2290 . . . . . . . . . . . 0.2953 
'X-RAY DIFFRACTION' 2.13 2.19  . . 140 2791 100.00 . . . . 0.2224 . . . . . . . . . . . 0.2686 
'X-RAY DIFFRACTION' 2.19 2.23  . . 112 1967 100.00 . . . . 0.2217 . . . . . . . . . . . 0.2569 
'X-RAY DIFFRACTION' 2.26 2.33  . . 141 2706 99.00  . . . . 0.2126 . . . . . . . . . . . 0.2558 
'X-RAY DIFFRACTION' 2.33 2.41  . . 167 2805 100.00 . . . . 0.2234 . . . . . . . . . . . 0.2271 
'X-RAY DIFFRACTION' 2.41 2.51  . . 144 2824 100.00 . . . . 0.2229 . . . . . . . . . . . 0.2543 
'X-RAY DIFFRACTION' 2.51 2.62  . . 148 2824 100.00 . . . . 0.2222 . . . . . . . . . . . 0.2718 
'X-RAY DIFFRACTION' 2.62 2.76  . . 139 2847 100.00 . . . . 0.2204 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 2.76 2.93  . . 146 2821 100.00 . . . . 0.2053 . . . . . . . . . . . 0.2211 
'X-RAY DIFFRACTION' 2.93 3.16  . . 151 2840 100.00 . . . . 0.2151 . . . . . . . . . . . 0.2467 
'X-RAY DIFFRACTION' 3.16 3.47  . . 112 2390 83.00  . . . . 0.2031 . . . . . . . . . . . 0.2179 
'X-RAY DIFFRACTION' 3.48 3.98  . . 136 2631 92.00  . . . . 0.1870 . . . . . . . . . . . 0.2127 
'X-RAY DIFFRACTION' 3.98 5.01  . . 158 2915 100.00 . . . . 0.1740 . . . . . . . . . . . 0.1893 
'X-RAY DIFFRACTION' 5.01 33.48 . . 175 3017 100.00 . . . . 0.2042 . . . . . . . . . . . 0.2468 
# 
_struct.entry_id                     9BGH 
_struct.title                        'Crystal structure of KRAS G12D in a transition state mimetic 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        9BGH 
_struct_keywords.text            'GTPase 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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L N N 7 ? 
M N N 7 ? 
N N N 7 ? 
O N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP PPIA_CHLAE P62938 ? 1 
;MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
;
1 
2 UNP RASK_MELGA P79800 ? 2 
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
;
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 9BGH B 2 ? 166 ? P62938 1 ? 165 ? 1 165 
2 1 9BGH D 2 ? 166 ? P62938 1 ? 165 ? 1 165 
3 2 9BGH A 2 ? 170 ? P79800 1 ? 169 ? 1 169 
4 2 9BGH C 2 ? 170 ? P79800 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 9BGH GLY B 1  ? UNP P62938 ?   ?  'expression tag'      0  1 
2 9BGH GLY D 1  ? UNP P62938 ?   ?  'expression tag'      0  2 
3 9BGH GLY A 1  ? UNP P79800 ?   ?  'expression tag'      0  3 
3 9BGH ASP A 13 ? UNP P79800 GLY 12 'engineered mutation' 12 4 
4 9BGH GLY C 1  ? UNP P79800 ?   ?  'expression tag'      0  5 
4 9BGH ASP C 13 ? UNP P79800 GLY 12 'engineered mutation' 12 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_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,O 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 VAL A 30  ? GLY A 43  ? VAL B 29  GLY B 42  1 ? 14 
HELX_P HELX_P2  AA2 THR A 120 ? ASP A 124 ? THR B 119 ASP B 123 5 ? 5  
HELX_P HELX_P3  AA3 GLY A 136 ? GLU A 144 ? GLY B 135 GLU B 143 1 ? 9  
HELX_P HELX_P4  AA4 ARG A 145 ? GLY A 147 ? ARG B 144 GLY B 146 5 ? 3  
HELX_P HELX_P5  AA5 VAL B 30  ? GLY B 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P6  AA6 THR B 120 ? ASP B 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P7  AA7 GLY B 136 ? GLU B 144 ? GLY D 135 GLU D 143 1 ? 9  
HELX_P HELX_P8  AA8 ARG B 145 ? GLY B 147 ? ARG D 144 GLY D 146 5 ? 3  
HELX_P HELX_P9  AA9 GLY C 16  ? ASN C 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P10 AB1 GLN C 62  ? MET C 68  ? GLN A 61  MET A 67  5 ? 7  
HELX_P HELX_P11 AB2 ARG C 69  ? GLY C 76  ? ARG A 68  GLY A 75  1 ? 8  
HELX_P HELX_P12 AB3 ASN C 87  ? ASP C 106 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P13 AB4 ASP C 127 ? GLY C 139 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P14 AB5 GLY C 152 ? GLU C 169 ? GLY A 151 GLU A 168 1 ? 18 
HELX_P HELX_P15 AB6 GLY D 16  ? ASN D 27  ? GLY C 15  ASN C 26  1 ? 12 
HELX_P HELX_P16 AB7 GLN D 62  ? ALA D 67  ? GLN C 61  ALA C 66  5 ? 6  
HELX_P HELX_P17 AB8 MET D 68  ? GLY D 76  ? MET C 67  GLY C 75  1 ? 9  
HELX_P HELX_P18 AB9 ASN D 87  ? ASP D 106 ? ASN C 86  ASP C 105 1 ? 20 
HELX_P HELX_P19 AC1 ASP D 127 ? GLY D 139 ? ASP C 126 GLY C 138 1 ? 13 
HELX_P HELX_P20 AC2 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 ? ? C SER 18 OG  ? ? ? 1_555 H MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc2  metalc ? ? C THR 36 OG1 ? ? ? 1_555 H MG  . MG ? ? A THR 35  A MG  202 1_555 ? ? ? ? ? ? ? 2.115 ? ? 
metalc3  metalc ? ? G GDP .  O1B ? ? ? 1_555 H MG  . MG ? ? A GDP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc4  metalc ? ? H MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  202 A HOH 313 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc5  metalc ? ? H MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  202 A HOH 326 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc6  metalc ? ? H MG  .  MG  ? ? ? 1_555 N HOH . O  ? ? A MG  202 A HOH 333 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc7  metalc ? ? D SER 18 OG  ? ? ? 1_555 J MG  . MG ? ? C SER 17  C MG  202 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc8  metalc ? ? D THR 36 OG1 ? ? ? 1_555 J MG  . MG ? ? C THR 35  C MG  202 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
metalc9  metalc ? ? I GDP .  O1B ? ? ? 1_555 J MG  . MG ? ? C GDP 201 C MG  202 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc10 metalc ? ? J MG  .  MG  ? ? ? 1_555 O HOH . O  ? ? C MG  202 C HOH 310 1_555 ? ? ? ? ? ? ? 2.222 ? ? 
metalc11 metalc ? ? J MG  .  MG  ? ? ? 1_555 O HOH . O  ? ? C MG  202 C HOH 320 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc12 metalc ? ? J MG  .  MG  ? ? ? 1_555 O HOH . O  ? ? C MG  202 C HOH 327 1_555 ? ? ? ? ? ? ? 2.076 ? ? 
# 
_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  ? C SER 18 ? A SER 17  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 OG1 ? C THR 36 ? A THR 35  ? 1_555 80.2  ? 
2  OG  ? C SER 18 ? A SER 17  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O1B ? G GDP .  ? A GDP 201 ? 1_555 94.7  ? 
3  OG1 ? C THR 36 ? A THR 35  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O1B ? G GDP .  ? A GDP 201 ? 1_555 174.1 ? 
4  OG  ? C SER 18 ? A SER 17  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 313 ? 1_555 86.7  ? 
5  OG1 ? C THR 36 ? A THR 35  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 313 ? 1_555 88.9  ? 
6  O1B ? G GDP .  ? A GDP 201 ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 313 ? 1_555 93.6  ? 
7  OG  ? C SER 18 ? A SER 17  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 326 ? 1_555 173.4 ? 
8  OG1 ? C THR 36 ? A THR 35  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 326 ? 1_555 93.2  ? 
9  O1B ? G GDP .  ? A GDP 201 ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 326 ? 1_555 92.0  ? 
10 O   ? N HOH .  ? A HOH 313 ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 326 ? 1_555 92.4  ? 
11 OG  ? C SER 18 ? A SER 17  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 333 ? 1_555 94.1  ? 
12 OG1 ? C THR 36 ? A THR 35  ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 333 ? 1_555 87.1  ? 
13 O1B ? G GDP .  ? A GDP 201 ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 333 ? 1_555 90.5  ? 
14 O   ? N HOH .  ? A HOH 313 ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 333 ? 1_555 175.7 ? 
15 O   ? N HOH .  ? A HOH 326 ? 1_555 MG ? H MG . ? A MG 202 ? 1_555 O   ? N HOH .  ? A HOH 333 ? 1_555 86.4  ? 
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 81.9  ? 
17 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O1B ? I GDP .  ? C GDP 201 ? 1_555 90.1  ? 
18 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O1B ? I GDP .  ? C GDP 201 ? 1_555 167.5 ? 
19 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 310 ? 1_555 102.4 ? 
20 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 310 ? 1_555 98.8  ? 
21 O1B ? I GDP .  ? C GDP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 310 ? 1_555 92.2  ? 
22 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 320 ? 1_555 80.8  ? 
23 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 320 ? 1_555 74.5  ? 
24 O1B ? I GDP .  ? C GDP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 320 ? 1_555 94.9  ? 
25 O   ? O HOH .  ? C HOH 310 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 320 ? 1_555 172.2 ? 
26 OG  ? D SER 18 ? C SER 17  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 327 ? 1_555 159.7 ? 
27 OG1 ? D THR 36 ? C THR 35  ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 327 ? 1_555 90.5  ? 
28 O1B ? I GDP .  ? C GDP 201 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 327 ? 1_555 94.0  ? 
29 O   ? O HOH .  ? C HOH 310 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 327 ? 1_555 97.3  ? 
30 O   ? O HOH .  ? C HOH 320 ? 1_555 MG ? J MG . ? C MG 202 ? 1_555 O   ? O HOH .  ? C HOH 327 ? 1_555 79.0  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 6 ? 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? 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 ARG A 56  ? ILE A 58  ? ARG B 55  ILE B 57  
AA1 2 MET A 62  ? GLY A 65  ? MET B 61  GLY B 64  
AA1 3 PHE A 113 ? CYS A 116 ? PHE B 112 CYS B 115 
AA1 4 ILE A 98  ? MET A 101 ? ILE B 97  MET B 100 
AA1 5 VAL A 129 ? VAL A 133 ? VAL B 128 VAL B 132 
AA1 6 GLU A 16  ? LEU A 25  ? GLU B 15  LEU B 24  
AA1 7 THR A 6   ? VAL A 13  ? THR B 5   VAL B 12  
AA1 8 ILE A 157 ? GLN A 164 ? ILE B 156 GLN B 163 
AA2 1 PHE B 54  ? ILE B 58  ? PHE D 53  ILE D 57  
AA2 2 MET B 62  ? GLY B 65  ? MET D 61  GLY D 64  
AA2 3 PHE B 113 ? CYS B 116 ? PHE D 112 CYS D 115 
AA2 4 ILE B 98  ? MET B 101 ? ILE D 97  MET D 100 
AA2 5 VAL B 129 ? VAL B 133 ? VAL D 128 VAL D 132 
AA2 6 GLU B 16  ? LEU B 25  ? GLU D 15  LEU D 24  
AA2 7 THR B 6   ? VAL B 13  ? THR D 5   VAL D 12  
AA2 8 ILE B 157 ? LEU B 165 ? ILE D 156 LEU D 164 
AA3 1 GLU C 38  ? ILE C 47  ? GLU A 37  ILE A 46  
AA3 2 GLU C 50  ? THR C 59  ? GLU A 49  THR A 58  
AA3 3 GLU C 4   ? VAL C 10  ? GLU A 3   VAL A 9   
AA3 4 GLY C 78  ? ALA C 84  ? GLY A 77  ALA A 83  
AA3 5 MET C 112 ? ASN C 117 ? MET A 111 ASN A 116 
AA3 6 PHE C 142 ? GLU C 144 ? PHE A 141 GLU A 143 
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 ARG A 56  ? N ARG B 55  O GLN A 64  ? O GLN B 63  
AA1 2 3 N CYS A 63  ? N CYS B 62  O ILE A 115 ? O ILE B 114 
AA1 3 4 O PHE A 114 ? O PHE B 113 N SER A 100 ? N SER B 99  
AA1 4 5 N LEU A 99  ? N LEU B 98  O GLY A 131 ? O GLY B 130 
AA1 5 6 O LYS A 132 ? O LYS B 131 N GLU A 24  ? N GLU B 23  
AA1 6 7 O PHE A 23  ? O PHE B 22  N VAL A 7   ? N VAL B 6   
AA1 7 8 N ASP A 10  ? N ASP B 9   O ASP A 161 ? O ASP B 160 
AA2 1 2 N ARG B 56  ? N ARG D 55  O GLN B 64  ? O GLN D 63  
AA2 2 3 N CYS B 63  ? N CYS D 62  O ILE B 115 ? O ILE D 114 
AA2 3 4 O CYS B 116 ? O CYS D 115 N ILE B 98  ? N ILE D 97  
AA2 4 5 N LEU B 99  ? N LEU D 98  O GLY B 131 ? O GLY D 130 
AA2 5 6 O LYS B 132 ? O LYS D 131 N GLU B 24  ? N GLU D 23  
AA2 6 7 O PHE B 23  ? O PHE D 22  N VAL B 7   ? N VAL D 6   
AA2 7 8 N THR B 6   ? N THR D 5   O LEU B 165 ? O LEU D 164 
AA3 1 2 N ASP C 39  ? N ASP A 38  O ASP C 58  ? O ASP A 57  
AA3 2 3 O ASP C 55  ? O ASP A 54  N LEU C 7   ? N LEU A 6   
AA3 3 4 N VAL C 10  ? N VAL A 9   O VAL C 82  ? O VAL A 81  
AA3 4 5 N PHE C 83  ? N PHE A 82  O ASN C 117 ? O ASN A 116 
AA3 5 6 N LEU C 114 ? N LEU A 113 O ILE C 143 ? O ILE A 142 
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 8   ? N VAL C 7   O GLY D 78  ? O GLY C 77  
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                   9BGH 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 OD1 C ASP 12  ? ? F2  C AF3 203 ? ? 1.91 
2  1 O   C HOH 349 ? ? O   C HOH 380 ? ? 1.92 
3  1 NE  C ARG 41  ? ? O   C HOH 301 ? ? 1.95 
4  1 O   D HOH 404 ? ? O   D HOH 405 ? ? 1.96 
5  1 AL  C AF3 203 ? ? O   C HOH 307 ? ? 1.97 
6  1 F3  C AF3 203 ? ? O   C HOH 320 ? ? 1.97 
7  1 O   B HOH 445 ? ? O   A HOH 353 ? ? 2.01 
8  1 O   D HOH 304 ? ? O   D HOH 407 ? ? 2.03 
9  1 O3B C GDP 201 ? ? AL  C AF3 203 ? ? 2.03 
10 1 O   D HOH 395 ? ? O   D HOH 405 ? ? 2.05 
11 1 NH1 B ARG 144 ? ? O   B HOH 301 ? ? 2.07 
12 1 O   A HOH 312 ? ? O   A HOH 385 ? ? 2.08 
13 1 O   A HOH 394 ? ? O   A HOH 420 ? ? 2.09 
14 1 OE2 A GLU 37  ? ? O   A HOH 301 ? ? 2.10 
15 1 O   B HOH 420 ? ? O   B HOH 445 ? ? 2.10 
16 1 NZ  C LYS 5   ? ? O   C HOH 302 ? ? 2.13 
17 1 O   D HOH 368 ? ? O   D HOH 408 ? ? 2.13 
18 1 OE2 C GLU 76  ? ? O   C HOH 303 ? ? 2.13 
19 1 O   B HOH 364 ? ? O   B HOH 431 ? ? 2.14 
20 1 O   C HOH 304 ? ? O   C HOH 333 ? ? 2.14 
21 1 OE2 C GLU 49  ? ? NH2 C ARG 164 ? ? 2.15 
22 1 O   D HOH 367 ? ? O   D HOH 399 ? ? 2.16 
23 1 O   B HOH 327 ? ? O   B HOH 409 ? ? 2.17 
24 1 O   A HOH 395 ? ? O   A HOH 408 ? ? 2.17 
25 1 O1B C GDP 201 ? ? F3  C AF3 203 ? ? 2.17 
26 1 O   B PRO 58  ? ? O   C HOH 301 ? ? 2.18 
27 1 O   B HOH 400 ? ? O   B HOH 431 ? ? 2.18 
28 1 O   C HOH 324 ? ? O   C HOH 379 ? ? 2.18 
29 1 OH  A TYR 96  ? ? O   A HOH 302 ? ? 2.18 
30 1 OE2 B GLU 15  ? ? O   B HOH 302 ? ? 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 B HOH 381 ? ? 1_555 O D HOH 397 ? ? 4_455 1.94 
2 1 O D HOH 393 ? ? 1_555 O C HOH 375 ? ? 3_655 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             D 
_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             D 
_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             D 
_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                86.49 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -13.71 
_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 PHE B 60  ? ? -130.26 -63.65 
2  1 LYS B 133 ? ? -101.60 -63.49 
3  1 PHE D 60  ? ? -132.34 -64.56 
4  1 GLU D 81  ? ? -56.98  -72.82 
5  1 LYS D 133 ? ? -98.25  -61.62 
6  1 ILE A 36  ? ? -91.12  -64.42 
7  1 GLU A 37  ? ? -170.11 131.14 
8  1 LYS A 117 ? ? 71.92   32.27  
9  1 SER A 122 ? ? -96.94  57.64  
10 1 ASN C 26  ? ? 59.97   10.30  
11 1 GLU C 37  ? ? -172.51 130.17 
12 1 ARG C 102 ? ? -60.67  -70.24 
13 1 CYS C 118 ? ? -64.37  5.71   
# 
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 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            0.083 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 8.7048  3.4840  10.4528 0.1485 ? 0.0113  ? -0.0367 ? 0.1607 ? 0.0246 ? 0.1459 ? 1.9492 ? -0.2486 ? 
0.6639  ? 1.4621 ? -0.3014 ? 3.0981 ? 0.1065 ? -0.0546 ? -0.1398 ? -0.1153 ? 0.0282  ? 0.0466  ? 0.3355  ? 0.1082  ? -0.1293 ? 
2 'X-RAY DIFFRACTION' ? refined 42.0882 25.7686 25.1303 0.2114 ? -0.0878 ? -0.0546 ? 0.2484 ? 0.0114 ? 0.1763 ? 3.2519 ? -0.3241 ? 
0.8147  ? 1.4140 ? 0.2193  ? 2.3943 ? 0.2882 ? -0.2789 ? -0.2457 ? 0.0791  ? -0.0313 ? -0.1703 ? 0.2412  ? 0.0827  ? -0.2271 ? 
3 'X-RAY DIFFRACTION' ? refined 11.4421 35.8161 9.5752  0.1821 ? 0.0609  ? 0.0770  ? 0.2140 ? 0.0343 ? 0.2341 ? 2.8932 ? 0.0542  ? 
-0.3043 ? 2.6649 ? -0.5234 ? 2.4061 ? 0.1784 ? 0.1523  ? 0.3277  ? 0.1156  ? 0.0112  ? 0.3553  ? -0.3528 ? -0.3186 ? -0.1007 ? 
4 'X-RAY DIFFRACTION' ? refined 16.7285 17.4366 42.5681 0.5630 ? -0.2482 ? 0.0737  ? 0.6222 ? 0.0493 ? 0.4016 ? 0.9619 ? 0.7146  ? 
-0.2899 ? 2.1121 ? -0.2088 ? 3.1279 ? 0.3888 ? -0.6178 ? 0.0045  ? 0.8479  ? -0.3011 ? 0.0324  ? -0.1966 ? 0.2902  ? -0.0659 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '(chain B and resseq 2:201)' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '(chain D and resseq 2:201)' 
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? '(chain A and resseq 0:202)' 
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? '(chain C and resseq 0:203)' 
# 
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   ? A GLY 1   
2 1 Y 1 B MET 1   ? A MET 2   
3 1 Y 1 B GLU 165 ? A GLU 166 
4 1 Y 1 D GLY 0   ? B GLY 1   
5 1 Y 1 D MET 1   ? B MET 2   
6 1 Y 1 D GLU 165 ? B GLU 166 
7 1 Y 1 A LYS 169 ? C LYS 170 
8 1 Y 1 C GLU 168 ? D GLU 169 
9 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 
AF3 AL     AL N N 1   
AF3 F1     F  N N 2   
AF3 F2     F  N N 3   
AF3 F3     F  N N 4   
ALA N      N  N N 5   
ALA CA     C  N S 6   
ALA C      C  N N 7   
ALA O      O  N N 8   
ALA CB     C  N N 9   
ALA OXT    O  N N 10  
ALA H      H  N N 11  
ALA H2     H  N N 12  
ALA HA     H  N N 13  
ALA HB1    H  N N 14  
ALA HB2    H  N N 15  
ALA HB3    H  N N 16  
ALA HXT    H  N N 17  
ARG N      N  N N 18  
ARG CA     C  N S 19  
ARG C      C  N N 20  
ARG O      O  N N 21  
ARG CB     C  N N 22  
ARG CG     C  N N 23  
ARG CD     C  N N 24  
ARG NE     N  N N 25  
ARG CZ     C  N N 26  
ARG NH1    N  N N 27  
ARG NH2    N  N N 28  
ARG OXT    O  N N 29  
ARG H      H  N N 30  
ARG H2     H  N N 31  
ARG HA     H  N N 32  
ARG HB2    H  N N 33  
ARG HB3    H  N N 34  
ARG HG2    H  N N 35  
ARG HG3    H  N N 36  
ARG HD2    H  N N 37  
ARG HD3    H  N N 38  
ARG HE     H  N N 39  
ARG HH11   H  N N 40  
ARG HH12   H  N N 41  
ARG HH21   H  N N 42  
ARG HH22   H  N N 43  
ARG HXT    H  N N 44  
ASN N      N  N N 45  
ASN CA     C  N S 46  
ASN C      C  N N 47  
ASN O      O  N N 48  
ASN CB     C  N N 49  
ASN CG     C  N N 50  
ASN OD1    O  N N 51  
ASN ND2    N  N N 52  
ASN OXT    O  N N 53  
ASN H      H  N N 54  
ASN H2     H  N N 55  
ASN HA     H  N N 56  
ASN HB2    H  N N 57  
ASN HB3    H  N N 58  
ASN HD21   H  N N 59  
ASN HD22   H  N N 60  
ASN HXT    H  N N 61  
ASP N      N  N N 62  
ASP CA     C  N S 63  
ASP C      C  N N 64  
ASP O      O  N N 65  
ASP CB     C  N N 66  
ASP CG     C  N N 67  
ASP OD1    O  N N 68  
ASP OD2    O  N N 69  
ASP OXT    O  N N 70  
ASP H      H  N N 71  
ASP H2     H  N N 72  
ASP HA     H  N N 73  
ASP HB2    H  N N 74  
ASP HB3    H  N N 75  
ASP HD2    H  N N 76  
ASP HXT    H  N N 77  
CYS N      N  N N 78  
CYS CA     C  N R 79  
CYS C      C  N N 80  
CYS O      O  N N 81  
CYS CB     C  N N 82  
CYS SG     S  N N 83  
CYS OXT    O  N N 84  
CYS H      H  N N 85  
CYS H2     H  N N 86  
CYS HA     H  N N 87  
CYS HB2    H  N N 88  
CYS HB3    H  N N 89  
CYS HG     H  N N 90  
CYS HXT    H  N N 91  
GDP PB     P  N N 92  
GDP O1B    O  N N 93  
GDP O2B    O  N N 94  
GDP O3B    O  N N 95  
GDP O3A    O  N N 96  
GDP PA     P  N N 97  
GDP O1A    O  N N 98  
GDP O2A    O  N N 99  
GDP "O5'"  O  N N 100 
GDP "C5'"  C  N N 101 
GDP "C4'"  C  N R 102 
GDP "O4'"  O  N N 103 
GDP "C3'"  C  N S 104 
GDP "O3'"  O  N N 105 
GDP "C2'"  C  N R 106 
GDP "O2'"  O  N N 107 
GDP "C1'"  C  N R 108 
GDP N9     N  Y N 109 
GDP C8     C  Y N 110 
GDP N7     N  Y N 111 
GDP C5     C  Y N 112 
GDP C6     C  N N 113 
GDP O6     O  N N 114 
GDP N1     N  N N 115 
GDP C2     C  N N 116 
GDP N2     N  N N 117 
GDP N3     N  N N 118 
GDP C4     C  Y N 119 
GDP HOB2   H  N N 120 
GDP HOB3   H  N N 121 
GDP HOA2   H  N N 122 
GDP "H5'"  H  N N 123 
GDP "H5''" H  N N 124 
GDP "H4'"  H  N N 125 
GDP "H3'"  H  N N 126 
GDP "HO3'" H  N N 127 
GDP "H2'"  H  N N 128 
GDP "HO2'" H  N N 129 
GDP "H1'"  H  N N 130 
GDP H8     H  N N 131 
GDP HN1    H  N N 132 
GDP HN21   H  N N 133 
GDP HN22   H  N N 134 
GLN N      N  N N 135 
GLN CA     C  N S 136 
GLN C      C  N N 137 
GLN O      O  N N 138 
GLN CB     C  N N 139 
GLN CG     C  N N 140 
GLN CD     C  N N 141 
GLN OE1    O  N N 142 
GLN NE2    N  N N 143 
GLN OXT    O  N N 144 
GLN H      H  N N 145 
GLN H2     H  N N 146 
GLN HA     H  N N 147 
GLN HB2    H  N N 148 
GLN HB3    H  N N 149 
GLN HG2    H  N N 150 
GLN HG3    H  N N 151 
GLN HE21   H  N N 152 
GLN HE22   H  N N 153 
GLN HXT    H  N N 154 
GLU N      N  N N 155 
GLU CA     C  N S 156 
GLU C      C  N N 157 
GLU O      O  N N 158 
GLU CB     C  N N 159 
GLU CG     C  N N 160 
GLU CD     C  N N 161 
GLU OE1    O  N N 162 
GLU OE2    O  N N 163 
GLU OXT    O  N N 164 
GLU H      H  N N 165 
GLU H2     H  N N 166 
GLU HA     H  N N 167 
GLU HB2    H  N N 168 
GLU HB3    H  N N 169 
GLU HG2    H  N N 170 
GLU HG3    H  N N 171 
GLU HE2    H  N N 172 
GLU HXT    H  N N 173 
GLY N      N  N N 174 
GLY CA     C  N N 175 
GLY C      C  N N 176 
GLY O      O  N N 177 
GLY OXT    O  N N 178 
GLY H      H  N N 179 
GLY H2     H  N N 180 
GLY HA2    H  N N 181 
GLY HA3    H  N N 182 
GLY HXT    H  N N 183 
HIS N      N  N N 184 
HIS CA     C  N S 185 
HIS C      C  N N 186 
HIS O      O  N N 187 
HIS CB     C  N N 188 
HIS CG     C  Y N 189 
HIS ND1    N  Y N 190 
HIS CD2    C  Y N 191 
HIS CE1    C  Y N 192 
HIS NE2    N  Y N 193 
HIS OXT    O  N N 194 
HIS H      H  N N 195 
HIS H2     H  N N 196 
HIS HA     H  N N 197 
HIS HB2    H  N N 198 
HIS HB3    H  N N 199 
HIS HD1    H  N N 200 
HIS HD2    H  N N 201 
HIS HE1    H  N N 202 
HIS HE2    H  N N 203 
HIS HXT    H  N N 204 
HOH O      O  N N 205 
HOH H1     H  N N 206 
HOH H2     H  N N 207 
ILE N      N  N N 208 
ILE CA     C  N S 209 
ILE C      C  N N 210 
ILE O      O  N N 211 
ILE CB     C  N S 212 
ILE CG1    C  N N 213 
ILE CG2    C  N N 214 
ILE CD1    C  N N 215 
ILE OXT    O  N N 216 
ILE H      H  N N 217 
ILE H2     H  N N 218 
ILE HA     H  N N 219 
ILE HB     H  N N 220 
ILE HG12   H  N N 221 
ILE HG13   H  N N 222 
ILE HG21   H  N N 223 
ILE HG22   H  N N 224 
ILE HG23   H  N N 225 
ILE HD11   H  N N 226 
ILE HD12   H  N N 227 
ILE HD13   H  N N 228 
ILE HXT    H  N N 229 
LEU N      N  N N 230 
LEU CA     C  N S 231 
LEU C      C  N N 232 
LEU O      O  N N 233 
LEU CB     C  N N 234 
LEU CG     C  N N 235 
LEU CD1    C  N N 236 
LEU CD2    C  N N 237 
LEU OXT    O  N N 238 
LEU H      H  N N 239 
LEU H2     H  N N 240 
LEU HA     H  N N 241 
LEU HB2    H  N N 242 
LEU HB3    H  N N 243 
LEU HG     H  N N 244 
LEU HD11   H  N N 245 
LEU HD12   H  N N 246 
LEU HD13   H  N N 247 
LEU HD21   H  N N 248 
LEU HD22   H  N N 249 
LEU HD23   H  N N 250 
LEU HXT    H  N N 251 
LYS N      N  N N 252 
LYS CA     C  N S 253 
LYS C      C  N N 254 
LYS O      O  N N 255 
LYS CB     C  N N 256 
LYS CG     C  N N 257 
LYS CD     C  N N 258 
LYS CE     C  N N 259 
LYS NZ     N  N N 260 
LYS OXT    O  N N 261 
LYS H      H  N N 262 
LYS H2     H  N N 263 
LYS HA     H  N N 264 
LYS HB2    H  N N 265 
LYS HB3    H  N N 266 
LYS HG2    H  N N 267 
LYS HG3    H  N N 268 
LYS HD2    H  N N 269 
LYS HD3    H  N N 270 
LYS HE2    H  N N 271 
LYS HE3    H  N N 272 
LYS HZ1    H  N N 273 
LYS HZ2    H  N N 274 
LYS HZ3    H  N N 275 
LYS HXT    H  N N 276 
MET N      N  N N 277 
MET CA     C  N S 278 
MET C      C  N N 279 
MET O      O  N N 280 
MET CB     C  N N 281 
MET CG     C  N N 282 
MET SD     S  N N 283 
MET CE     C  N N 284 
MET OXT    O  N N 285 
MET H      H  N N 286 
MET H2     H  N N 287 
MET HA     H  N N 288 
MET HB2    H  N N 289 
MET HB3    H  N N 290 
MET HG2    H  N N 291 
MET HG3    H  N N 292 
MET HE1    H  N N 293 
MET HE2    H  N N 294 
MET HE3    H  N N 295 
MET HXT    H  N N 296 
MG  MG     MG N N 297 
PHE N      N  N N 298 
PHE CA     C  N S 299 
PHE C      C  N N 300 
PHE O      O  N N 301 
PHE CB     C  N N 302 
PHE CG     C  Y N 303 
PHE CD1    C  Y N 304 
PHE CD2    C  Y N 305 
PHE CE1    C  Y N 306 
PHE CE2    C  Y N 307 
PHE CZ     C  Y N 308 
PHE OXT    O  N N 309 
PHE H      H  N N 310 
PHE H2     H  N N 311 
PHE HA     H  N N 312 
PHE HB2    H  N N 313 
PHE HB3    H  N N 314 
PHE HD1    H  N N 315 
PHE HD2    H  N N 316 
PHE HE1    H  N N 317 
PHE HE2    H  N N 318 
PHE HZ     H  N N 319 
PHE HXT    H  N N 320 
PRO N      N  N N 321 
PRO CA     C  N S 322 
PRO C      C  N N 323 
PRO O      O  N N 324 
PRO CB     C  N N 325 
PRO CG     C  N N 326 
PRO CD     C  N N 327 
PRO OXT    O  N N 328 
PRO H      H  N N 329 
PRO HA     H  N N 330 
PRO HB2    H  N N 331 
PRO HB3    H  N N 332 
PRO HG2    H  N N 333 
PRO HG3    H  N N 334 
PRO HD2    H  N N 335 
PRO HD3    H  N N 336 
PRO HXT    H  N N 337 
SER N      N  N N 338 
SER CA     C  N S 339 
SER C      C  N N 340 
SER O      O  N N 341 
SER CB     C  N N 342 
SER OG     O  N N 343 
SER OXT    O  N N 344 
SER H      H  N N 345 
SER H2     H  N N 346 
SER HA     H  N N 347 
SER HB2    H  N N 348 
SER HB3    H  N N 349 
SER HG     H  N N 350 
SER HXT    H  N N 351 
THR N      N  N N 352 
THR CA     C  N S 353 
THR C      C  N N 354 
THR O      O  N N 355 
THR CB     C  N R 356 
THR OG1    O  N N 357 
THR CG2    C  N N 358 
THR OXT    O  N N 359 
THR H      H  N N 360 
THR H2     H  N N 361 
THR HA     H  N N 362 
THR HB     H  N N 363 
THR HG1    H  N N 364 
THR HG21   H  N N 365 
THR HG22   H  N N 366 
THR HG23   H  N N 367 
THR HXT    H  N N 368 
TRP N      N  N N 369 
TRP CA     C  N S 370 
TRP C      C  N N 371 
TRP O      O  N N 372 
TRP CB     C  N N 373 
TRP CG     C  Y N 374 
TRP CD1    C  Y N 375 
TRP CD2    C  Y N 376 
TRP NE1    N  Y N 377 
TRP CE2    C  Y N 378 
TRP CE3    C  Y N 379 
TRP CZ2    C  Y N 380 
TRP CZ3    C  Y N 381 
TRP CH2    C  Y N 382 
TRP OXT    O  N N 383 
TRP H      H  N N 384 
TRP H2     H  N N 385 
TRP HA     H  N N 386 
TRP HB2    H  N N 387 
TRP HB3    H  N N 388 
TRP HD1    H  N N 389 
TRP HE1    H  N N 390 
TRP HE3    H  N N 391 
TRP HZ2    H  N N 392 
TRP HZ3    H  N N 393 
TRP HH2    H  N N 394 
TRP HXT    H  N N 395 
TYR N      N  N N 396 
TYR CA     C  N S 397 
TYR C      C  N N 398 
TYR O      O  N N 399 
TYR CB     C  N N 400 
TYR CG     C  Y N 401 
TYR CD1    C  Y N 402 
TYR CD2    C  Y N 403 
TYR CE1    C  Y N 404 
TYR CE2    C  Y N 405 
TYR CZ     C  Y N 406 
TYR OH     O  N N 407 
TYR OXT    O  N N 408 
TYR H      H  N N 409 
TYR H2     H  N N 410 
TYR HA     H  N N 411 
TYR HB2    H  N N 412 
TYR HB3    H  N N 413 
TYR HD1    H  N N 414 
TYR HD2    H  N N 415 
TYR HE1    H  N N 416 
TYR HE2    H  N N 417 
TYR HH     H  N N 418 
TYR HXT    H  N N 419 
VAL N      N  N N 420 
VAL CA     C  N S 421 
VAL C      C  N N 422 
VAL O      O  N N 423 
VAL CB     C  N N 424 
VAL CG1    C  N N 425 
VAL CG2    C  N N 426 
VAL OXT    O  N N 427 
VAL H      H  N N 428 
VAL H2     H  N N 429 
VAL HA     H  N N 430 
VAL HB     H  N N 431 
VAL HG11   H  N N 432 
VAL HG12   H  N N 433 
VAL HG13   H  N N 434 
VAL HG21   H  N N 435 
VAL HG22   H  N N 436 
VAL HG23   H  N N 437 
VAL HXT    H  N N 438 
ZNI C1     C  N N 439 
ZNI C10    C  N R 440 
ZNI C11    C  N N 441 
ZNI C12    C  N N 442 
ZNI C13    C  N N 443 
ZNI C14    C  Y N 444 
ZNI C15    C  Y N 445 
ZNI C16    C  Y N 446 
ZNI C17    C  Y N 447 
ZNI C18    C  Y N 448 
ZNI C19    C  Y N 449 
ZNI C2     C  N S 450 
ZNI C20    C  Y N 451 
ZNI C21    C  Y N 452 
ZNI C22    C  Y N 453 
ZNI C23    C  N N 454 
ZNI C24    C  N N 455 
ZNI C25    C  Y N 456 
ZNI C26    C  Y N 457 
ZNI C27    C  Y N 458 
ZNI C28    C  N S 459 
ZNI C29    C  N N 460 
ZNI C3     C  N N 461 
ZNI C30    C  N N 462 
ZNI C31    C  Y N 463 
ZNI C32    C  Y N 464 
ZNI C33    C  N N 465 
ZNI C34    C  N N 466 
ZNI C35    C  N N 467 
ZNI C36    C  N N 468 
ZNI C37    C  N N 469 
ZNI C38    C  N N 470 
ZNI C39    C  N N 471 
ZNI C4     C  N N 472 
ZNI C40    C  Y N 473 
ZNI C41    C  Y N 474 
ZNI C42    C  N N 475 
ZNI C43    C  N N 476 
ZNI C44    C  N N 477 
ZNI C45    C  N N 478 
ZNI C46    C  N N 479 
ZNI C47    C  N N 480 
ZNI C5     C  N N 481 
ZNI C6     C  N S 482 
ZNI C7     C  N N 483 
ZNI C8     C  N N 484 
ZNI C9     C  N S 485 
ZNI N1     N  N N 486 
ZNI N2     N  N S 487 
ZNI N3     N  N N 488 
ZNI N4     N  Y N 489 
ZNI N5     N  Y N 490 
ZNI N6     N  Y N 491 
ZNI N7     N  N N 492 
ZNI N8     N  N N 493 
ZNI O1     O  N N 494 
ZNI O2     O  N N 495 
ZNI O3     O  N N 496 
ZNI O4     O  N N 497 
ZNI O5     O  N N 498 
ZNI O6     O  N N 499 
ZNI S1     S  Y N 500 
ZNI H1     H  N N 501 
ZNI H2     H  N N 502 
ZNI H3     H  N N 503 
ZNI H4     H  N N 504 
ZNI H5     H  N N 505 
ZNI H6     H  N N 506 
ZNI H7     H  N N 507 
ZNI H8     H  N N 508 
ZNI H9     H  N N 509 
ZNI H10    H  N N 510 
ZNI H11    H  N N 511 
ZNI H12    H  N N 512 
ZNI H13    H  N N 513 
ZNI H14    H  N N 514 
ZNI H15    H  N N 515 
ZNI H16    H  N N 516 
ZNI H17    H  N N 517 
ZNI H18    H  N N 518 
ZNI H19    H  N N 519 
ZNI H20    H  N N 520 
ZNI H21    H  N N 521 
ZNI H22    H  N N 522 
ZNI H23    H  N N 523 
ZNI H24    H  N N 524 
ZNI H25    H  N N 525 
ZNI H26    H  N N 526 
ZNI H27    H  N N 527 
ZNI H28    H  N N 528 
ZNI H29    H  N N 529 
ZNI H30    H  N N 530 
ZNI H31    H  N N 531 
ZNI H32    H  N N 532 
ZNI H33    H  N N 533 
ZNI H34    H  N N 534 
ZNI H35    H  N N 535 
ZNI H36    H  N N 536 
ZNI H37    H  N N 537 
ZNI H38    H  N N 538 
ZNI H39    H  N N 539 
ZNI H40    H  N N 540 
ZNI H41    H  N N 541 
ZNI H42    H  N N 542 
ZNI H43    H  N N 543 
ZNI H44    H  N N 544 
ZNI H45    H  N N 545 
ZNI H46    H  N N 546 
ZNI H47    H  N N 547 
ZNI H48    H  N N 548 
ZNI H49    H  N N 549 
ZNI H50    H  N N 550 
ZNI H51    H  N N 551 
ZNI H52    H  N N 552 
ZNI H53    H  N N 553 
ZNI H54    H  N N 554 
ZNI H55    H  N N 555 
ZNI H56    H  N N 556 
ZNI H57    H  N N 557 
ZNI H58    H  N N 558 
ZNI H59    H  N N 559 
ZNI H60    H  N N 560 
# 
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 
AF3 AL    F1     sing N N 1   
AF3 AL    F2     sing N N 2   
AF3 AL    F3     sing N N 3   
ALA N     CA     sing N N 4   
ALA N     H      sing N N 5   
ALA N     H2     sing N N 6   
ALA CA    C      sing N N 7   
ALA CA    CB     sing N N 8   
ALA CA    HA     sing N N 9   
ALA C     O      doub N N 10  
ALA C     OXT    sing N N 11  
ALA CB    HB1    sing N N 12  
ALA CB    HB2    sing N N 13  
ALA CB    HB3    sing N N 14  
ALA OXT   HXT    sing N N 15  
ARG N     CA     sing N N 16  
ARG N     H      sing N N 17  
ARG N     H2     sing N N 18  
ARG CA    C      sing N N 19  
ARG CA    CB     sing N N 20  
ARG CA    HA     sing N N 21  
ARG C     O      doub N N 22  
ARG C     OXT    sing N N 23  
ARG CB    CG     sing N N 24  
ARG CB    HB2    sing N N 25  
ARG CB    HB3    sing N N 26  
ARG CG    CD     sing N N 27  
ARG CG    HG2    sing N N 28  
ARG CG    HG3    sing N N 29  
ARG CD    NE     sing N N 30  
ARG CD    HD2    sing N N 31  
ARG CD    HD3    sing N N 32  
ARG NE    CZ     sing N N 33  
ARG NE    HE     sing N N 34  
ARG CZ    NH1    sing N N 35  
ARG CZ    NH2    doub N N 36  
ARG NH1   HH11   sing N N 37  
ARG NH1   HH12   sing N N 38  
ARG NH2   HH21   sing N N 39  
ARG NH2   HH22   sing N N 40  
ARG OXT   HXT    sing N N 41  
ASN N     CA     sing N N 42  
ASN N     H      sing N N 43  
ASN N     H2     sing N N 44  
ASN CA    C      sing N N 45  
ASN CA    CB     sing N N 46  
ASN CA    HA     sing N N 47  
ASN C     O      doub N N 48  
ASN C     OXT    sing N N 49  
ASN CB    CG     sing N N 50  
ASN CB    HB2    sing N N 51  
ASN CB    HB3    sing N N 52  
ASN CG    OD1    doub N N 53  
ASN CG    ND2    sing N N 54  
ASN ND2   HD21   sing N N 55  
ASN ND2   HD22   sing N N 56  
ASN OXT   HXT    sing N N 57  
ASP N     CA     sing N N 58  
ASP N     H      sing N N 59  
ASP N     H2     sing N N 60  
ASP CA    C      sing N N 61  
ASP CA    CB     sing N N 62  
ASP CA    HA     sing N N 63  
ASP C     O      doub N N 64  
ASP C     OXT    sing N N 65  
ASP CB    CG     sing N N 66  
ASP CB    HB2    sing N N 67  
ASP CB    HB3    sing N N 68  
ASP CG    OD1    doub N N 69  
ASP CG    OD2    sing N N 70  
ASP OD2   HD2    sing N N 71  
ASP OXT   HXT    sing N N 72  
CYS N     CA     sing N N 73  
CYS N     H      sing N N 74  
CYS N     H2     sing N N 75  
CYS CA    C      sing N N 76  
CYS CA    CB     sing N N 77  
CYS CA    HA     sing N N 78  
CYS C     O      doub N N 79  
CYS C     OXT    sing N N 80  
CYS CB    SG     sing N N 81  
CYS CB    HB2    sing N N 82  
CYS CB    HB3    sing N N 83  
CYS SG    HG     sing N N 84  
CYS OXT   HXT    sing N N 85  
GDP PB    O1B    doub N N 86  
GDP PB    O2B    sing N N 87  
GDP PB    O3B    sing N N 88  
GDP PB    O3A    sing N N 89  
GDP O2B   HOB2   sing N N 90  
GDP O3B   HOB3   sing N N 91  
GDP O3A   PA     sing N N 92  
GDP PA    O1A    doub N N 93  
GDP PA    O2A    sing N N 94  
GDP PA    "O5'"  sing N N 95  
GDP O2A   HOA2   sing N N 96  
GDP "O5'" "C5'"  sing N N 97  
GDP "C5'" "C4'"  sing N N 98  
GDP "C5'" "H5'"  sing N N 99  
GDP "C5'" "H5''" sing N N 100 
GDP "C4'" "O4'"  sing N N 101 
GDP "C4'" "C3'"  sing N N 102 
GDP "C4'" "H4'"  sing N N 103 
GDP "O4'" "C1'"  sing N N 104 
GDP "C3'" "O3'"  sing N N 105 
GDP "C3'" "C2'"  sing N N 106 
GDP "C3'" "H3'"  sing N N 107 
GDP "O3'" "HO3'" sing N N 108 
GDP "C2'" "O2'"  sing N N 109 
GDP "C2'" "C1'"  sing N N 110 
GDP "C2'" "H2'"  sing N N 111 
GDP "O2'" "HO2'" sing N N 112 
GDP "C1'" N9     sing N N 113 
GDP "C1'" "H1'"  sing N N 114 
GDP N9    C8     sing Y N 115 
GDP N9    C4     sing Y N 116 
GDP C8    N7     doub Y N 117 
GDP C8    H8     sing N N 118 
GDP N7    C5     sing Y N 119 
GDP C5    C6     sing N N 120 
GDP C5    C4     doub Y N 121 
GDP C6    O6     doub N N 122 
GDP C6    N1     sing N N 123 
GDP N1    C2     sing N N 124 
GDP N1    HN1    sing N N 125 
GDP C2    N2     sing N N 126 
GDP C2    N3     doub N N 127 
GDP N2    HN21   sing N N 128 
GDP N2    HN22   sing N N 129 
GDP N3    C4     sing N N 130 
GLN N     CA     sing N N 131 
GLN N     H      sing N N 132 
GLN N     H2     sing N N 133 
GLN CA    C      sing N N 134 
GLN CA    CB     sing N N 135 
GLN CA    HA     sing N N 136 
GLN C     O      doub N N 137 
GLN C     OXT    sing N N 138 
GLN CB    CG     sing N N 139 
GLN CB    HB2    sing N N 140 
GLN CB    HB3    sing N N 141 
GLN CG    CD     sing N N 142 
GLN CG    HG2    sing N N 143 
GLN CG    HG3    sing N N 144 
GLN CD    OE1    doub N N 145 
GLN CD    NE2    sing N N 146 
GLN NE2   HE21   sing N N 147 
GLN NE2   HE22   sing N N 148 
GLN OXT   HXT    sing N N 149 
GLU N     CA     sing N N 150 
GLU N     H      sing N N 151 
GLU N     H2     sing N N 152 
GLU CA    C      sing N N 153 
GLU CA    CB     sing N N 154 
GLU CA    HA     sing N N 155 
GLU C     O      doub N N 156 
GLU C     OXT    sing N N 157 
GLU CB    CG     sing N N 158 
GLU CB    HB2    sing N N 159 
GLU CB    HB3    sing N N 160 
GLU CG    CD     sing N N 161 
GLU CG    HG2    sing N N 162 
GLU CG    HG3    sing N N 163 
GLU CD    OE1    doub N N 164 
GLU CD    OE2    sing N N 165 
GLU OE2   HE2    sing N N 166 
GLU OXT   HXT    sing N N 167 
GLY N     CA     sing N N 168 
GLY N     H      sing N N 169 
GLY N     H2     sing N N 170 
GLY CA    C      sing N N 171 
GLY CA    HA2    sing N N 172 
GLY CA    HA3    sing N N 173 
GLY C     O      doub N N 174 
GLY C     OXT    sing N N 175 
GLY OXT   HXT    sing N N 176 
HIS N     CA     sing N N 177 
HIS N     H      sing N N 178 
HIS N     H2     sing N N 179 
HIS CA    C      sing N N 180 
HIS CA    CB     sing N N 181 
HIS CA    HA     sing N N 182 
HIS C     O      doub N N 183 
HIS C     OXT    sing N N 184 
HIS CB    CG     sing N N 185 
HIS CB    HB2    sing N N 186 
HIS CB    HB3    sing N N 187 
HIS CG    ND1    sing Y N 188 
HIS CG    CD2    doub Y N 189 
HIS ND1   CE1    doub Y N 190 
HIS ND1   HD1    sing N N 191 
HIS CD2   NE2    sing Y N 192 
HIS CD2   HD2    sing N N 193 
HIS CE1   NE2    sing Y N 194 
HIS CE1   HE1    sing N N 195 
HIS NE2   HE2    sing N N 196 
HIS OXT   HXT    sing N N 197 
HOH O     H1     sing N N 198 
HOH O     H2     sing N N 199 
ILE N     CA     sing N N 200 
ILE N     H      sing N N 201 
ILE N     H2     sing N N 202 
ILE CA    C      sing N N 203 
ILE CA    CB     sing N N 204 
ILE CA    HA     sing N N 205 
ILE C     O      doub N N 206 
ILE C     OXT    sing N N 207 
ILE CB    CG1    sing N N 208 
ILE CB    CG2    sing N N 209 
ILE CB    HB     sing N N 210 
ILE CG1   CD1    sing N N 211 
ILE CG1   HG12   sing N N 212 
ILE CG1   HG13   sing N N 213 
ILE CG2   HG21   sing N N 214 
ILE CG2   HG22   sing N N 215 
ILE CG2   HG23   sing N N 216 
ILE CD1   HD11   sing N N 217 
ILE CD1   HD12   sing N N 218 
ILE CD1   HD13   sing N N 219 
ILE OXT   HXT    sing N N 220 
LEU N     CA     sing N N 221 
LEU N     H      sing N N 222 
LEU N     H2     sing N N 223 
LEU CA    C      sing N N 224 
LEU CA    CB     sing N N 225 
LEU CA    HA     sing N N 226 
LEU C     O      doub N N 227 
LEU C     OXT    sing N N 228 
LEU CB    CG     sing N N 229 
LEU CB    HB2    sing N N 230 
LEU CB    HB3    sing N N 231 
LEU CG    CD1    sing N N 232 
LEU CG    CD2    sing N N 233 
LEU CG    HG     sing N N 234 
LEU CD1   HD11   sing N N 235 
LEU CD1   HD12   sing N N 236 
LEU CD1   HD13   sing N N 237 
LEU CD2   HD21   sing N N 238 
LEU CD2   HD22   sing N N 239 
LEU CD2   HD23   sing N N 240 
LEU OXT   HXT    sing N N 241 
LYS N     CA     sing N N 242 
LYS N     H      sing N N 243 
LYS N     H2     sing N N 244 
LYS CA    C      sing N N 245 
LYS CA    CB     sing N N 246 
LYS CA    HA     sing N N 247 
LYS C     O      doub N N 248 
LYS C     OXT    sing N N 249 
LYS CB    CG     sing N N 250 
LYS CB    HB2    sing N N 251 
LYS CB    HB3    sing N N 252 
LYS CG    CD     sing N N 253 
LYS CG    HG2    sing N N 254 
LYS CG    HG3    sing N N 255 
LYS CD    CE     sing N N 256 
LYS CD    HD2    sing N N 257 
LYS CD    HD3    sing N N 258 
LYS CE    NZ     sing N N 259 
LYS CE    HE2    sing N N 260 
LYS CE    HE3    sing N N 261 
LYS NZ    HZ1    sing N N 262 
LYS NZ    HZ2    sing N N 263 
LYS NZ    HZ3    sing N N 264 
LYS OXT   HXT    sing N N 265 
MET N     CA     sing N N 266 
MET N     H      sing N N 267 
MET N     H2     sing N N 268 
MET CA    C      sing N N 269 
MET CA    CB     sing N N 270 
MET CA    HA     sing N N 271 
MET C     O      doub N N 272 
MET C     OXT    sing N N 273 
MET CB    CG     sing N N 274 
MET CB    HB2    sing N N 275 
MET CB    HB3    sing N N 276 
MET CG    SD     sing N N 277 
MET CG    HG2    sing N N 278 
MET CG    HG3    sing N N 279 
MET SD    CE     sing N N 280 
MET CE    HE1    sing N N 281 
MET CE    HE2    sing N N 282 
MET CE    HE3    sing N N 283 
MET OXT   HXT    sing N N 284 
PHE N     CA     sing N N 285 
PHE N     H      sing N N 286 
PHE N     H2     sing N N 287 
PHE CA    C      sing N N 288 
PHE CA    CB     sing N N 289 
PHE CA    HA     sing N N 290 
PHE C     O      doub N N 291 
PHE C     OXT    sing N N 292 
PHE CB    CG     sing N N 293 
PHE CB    HB2    sing N N 294 
PHE CB    HB3    sing N N 295 
PHE CG    CD1    doub Y N 296 
PHE CG    CD2    sing Y N 297 
PHE CD1   CE1    sing Y N 298 
PHE CD1   HD1    sing N N 299 
PHE CD2   CE2    doub Y N 300 
PHE CD2   HD2    sing N N 301 
PHE CE1   CZ     doub Y N 302 
PHE CE1   HE1    sing N N 303 
PHE CE2   CZ     sing Y N 304 
PHE CE2   HE2    sing N N 305 
PHE CZ    HZ     sing N N 306 
PHE OXT   HXT    sing N N 307 
PRO N     CA     sing N N 308 
PRO N     CD     sing N N 309 
PRO N     H      sing N N 310 
PRO CA    C      sing N N 311 
PRO CA    CB     sing N N 312 
PRO CA    HA     sing N N 313 
PRO C     O      doub N N 314 
PRO C     OXT    sing N N 315 
PRO CB    CG     sing N N 316 
PRO CB    HB2    sing N N 317 
PRO CB    HB3    sing N N 318 
PRO CG    CD     sing N N 319 
PRO CG    HG2    sing N N 320 
PRO CG    HG3    sing N N 321 
PRO CD    HD2    sing N N 322 
PRO CD    HD3    sing N N 323 
PRO OXT   HXT    sing N N 324 
SER N     CA     sing N N 325 
SER N     H      sing N N 326 
SER N     H2     sing N N 327 
SER CA    C      sing N N 328 
SER CA    CB     sing N N 329 
SER CA    HA     sing N N 330 
SER C     O      doub N N 331 
SER C     OXT    sing N N 332 
SER CB    OG     sing N N 333 
SER CB    HB2    sing N N 334 
SER CB    HB3    sing N N 335 
SER OG    HG     sing N N 336 
SER OXT   HXT    sing N N 337 
THR N     CA     sing N N 338 
THR N     H      sing N N 339 
THR N     H2     sing N N 340 
THR CA    C      sing N N 341 
THR CA    CB     sing N N 342 
THR CA    HA     sing N N 343 
THR C     O      doub N N 344 
THR C     OXT    sing N N 345 
THR CB    OG1    sing N N 346 
THR CB    CG2    sing N N 347 
THR CB    HB     sing N N 348 
THR OG1   HG1    sing N N 349 
THR CG2   HG21   sing N N 350 
THR CG2   HG22   sing N N 351 
THR CG2   HG23   sing N N 352 
THR OXT   HXT    sing N N 353 
TRP N     CA     sing N N 354 
TRP N     H      sing N N 355 
TRP N     H2     sing N N 356 
TRP CA    C      sing N N 357 
TRP CA    CB     sing N N 358 
TRP CA    HA     sing N N 359 
TRP C     O      doub N N 360 
TRP C     OXT    sing N N 361 
TRP CB    CG     sing N N 362 
TRP CB    HB2    sing N N 363 
TRP CB    HB3    sing N N 364 
TRP CG    CD1    doub Y N 365 
TRP CG    CD2    sing Y N 366 
TRP CD1   NE1    sing Y N 367 
TRP CD1   HD1    sing N N 368 
TRP CD2   CE2    doub Y N 369 
TRP CD2   CE3    sing Y N 370 
TRP NE1   CE2    sing Y N 371 
TRP NE1   HE1    sing N N 372 
TRP CE2   CZ2    sing Y N 373 
TRP CE3   CZ3    doub Y N 374 
TRP CE3   HE3    sing N N 375 
TRP CZ2   CH2    doub Y N 376 
TRP CZ2   HZ2    sing N N 377 
TRP CZ3   CH2    sing Y N 378 
TRP CZ3   HZ3    sing N N 379 
TRP CH2   HH2    sing N N 380 
TRP OXT   HXT    sing N N 381 
TYR N     CA     sing N N 382 
TYR N     H      sing N N 383 
TYR N     H2     sing N N 384 
TYR CA    C      sing N N 385 
TYR CA    CB     sing N N 386 
TYR CA    HA     sing N N 387 
TYR C     O      doub N N 388 
TYR C     OXT    sing N N 389 
TYR CB    CG     sing N N 390 
TYR CB    HB2    sing N N 391 
TYR CB    HB3    sing N N 392 
TYR CG    CD1    doub Y N 393 
TYR CG    CD2    sing Y N 394 
TYR CD1   CE1    sing Y N 395 
TYR CD1   HD1    sing N N 396 
TYR CD2   CE2    doub Y N 397 
TYR CD2   HD2    sing N N 398 
TYR CE1   CZ     doub Y N 399 
TYR CE1   HE1    sing N N 400 
TYR CE2   CZ     sing Y N 401 
TYR CE2   HE2    sing N N 402 
TYR CZ    OH     sing N N 403 
TYR OH    HH     sing N N 404 
TYR OXT   HXT    sing N N 405 
VAL N     CA     sing N N 406 
VAL N     H      sing N N 407 
VAL N     H2     sing N N 408 
VAL CA    C      sing N N 409 
VAL CA    CB     sing N N 410 
VAL CA    HA     sing N N 411 
VAL C     O      doub N N 412 
VAL C     OXT    sing N N 413 
VAL CB    CG1    sing N N 414 
VAL CB    CG2    sing N N 415 
VAL CB    HB     sing N N 416 
VAL CG1   HG11   sing N N 417 
VAL CG1   HG12   sing N N 418 
VAL CG1   HG13   sing N N 419 
VAL CG2   HG21   sing N N 420 
VAL CG2   HG22   sing N N 421 
VAL CG2   HG23   sing N N 422 
VAL OXT   HXT    sing N N 423 
ZNI C30   C28    sing N N 424 
ZNI C44   C43    sing N N 425 
ZNI C29   O4     sing N N 426 
ZNI C28   O4     sing N N 427 
ZNI C28   C27    sing N N 428 
ZNI N6    C27    doub Y N 429 
ZNI N6    C31    sing Y N 430 
ZNI C45   C43    sing N N 431 
ZNI O6    C47    doub N N 432 
ZNI C46   C43    sing N N 433 
ZNI C46   O5     sing N N 434 
ZNI C43   C42    sing N N 435 
ZNI C27   C26    sing Y N 436 
ZNI C31   C32    doub Y N 437 
ZNI C47   O5     sing N N 438 
ZNI C47   C2     sing N N 439 
ZNI C1    C4     sing N N 440 
ZNI C1    C2     sing N N 441 
ZNI C3    C4     sing N N 442 
ZNI C3    N2     sing N N 443 
ZNI C32   N7     sing N N 444 
ZNI C32   C40    sing Y N 445 
ZNI N1    C2     sing N N 446 
ZNI N1    N2     sing N N 447 
ZNI C26   C40    doub Y N 448 
ZNI C26   C25    sing N N 449 
ZNI C39   C38    sing N N 450 
ZNI C39   N7     sing N N 451 
ZNI C42   C41    sing N N 452 
ZNI C38   N8     sing N N 453 
ZNI N7    C33    sing N N 454 
ZNI N2    C5     sing N N 455 
ZNI C25   C41    doub Y N 456 
ZNI C25   N5     sing Y N 457 
ZNI C41   C19    sing Y N 458 
ZNI O2    C7     doub N N 459 
ZNI N5    C23    sing N N 460 
ZNI N5    C20    sing Y N 461 
ZNI C19   C20    doub Y N 462 
ZNI C19   C18    sing Y N 463 
ZNI C23   C24    sing N N 464 
ZNI N8    C35    sing N N 465 
ZNI N8    C34    sing N N 466 
ZNI C5    O1     doub N N 467 
ZNI C5    C6     sing N N 468 
ZNI C35   C37    sing N N 469 
ZNI C35   C36    sing N N 470 
ZNI C33   C34    sing N N 471 
ZNI C20   C21    sing Y N 472 
ZNI C18   C17    doub Y N 473 
ZNI C9    C10    sing N N 474 
ZNI C9    C12    sing N N 475 
ZNI C9    C8     sing N N 476 
ZNI C7    N3     sing N N 477 
ZNI C7    C8     sing N N 478 
ZNI C37   C36    sing N N 479 
ZNI C6    N3     sing N N 480 
ZNI C6    C13    sing N N 481 
ZNI C21   C22    doub Y N 482 
ZNI C10   C8     sing N N 483 
ZNI C10   C11    sing N N 484 
ZNI C17   C22    sing Y N 485 
ZNI C17   C15    sing N N 486 
ZNI C12   O3     sing N N 487 
ZNI N4    C15    sing Y N 488 
ZNI N4    C14    doub Y N 489 
ZNI C15   C16    doub Y N 490 
ZNI C14   C13    sing N N 491 
ZNI C14   S1     sing Y N 492 
ZNI C16   S1     sing Y N 493 
ZNI C11   O3     sing N N 494 
ZNI C1    H1     sing N N 495 
ZNI C1    H2     sing N N 496 
ZNI C10   H3     sing N N 497 
ZNI C11   H4     sing N N 498 
ZNI C11   H5     sing N N 499 
ZNI C12   H6     sing N N 500 
ZNI C12   H7     sing N N 501 
ZNI C13   H8     sing N N 502 
ZNI C13   H9     sing N N 503 
ZNI C16   H10    sing N N 504 
ZNI C18   H11    sing N N 505 
ZNI C2    H12    sing N N 506 
ZNI C21   H13    sing N N 507 
ZNI C22   H14    sing N N 508 
ZNI C23   H15    sing N N 509 
ZNI C23   H16    sing N N 510 
ZNI C24   H17    sing N N 511 
ZNI C24   H18    sing N N 512 
ZNI C24   H19    sing N N 513 
ZNI C28   H20    sing N N 514 
ZNI C29   H21    sing N N 515 
ZNI C29   H22    sing N N 516 
ZNI C29   H23    sing N N 517 
ZNI C3    H24    sing N N 518 
ZNI C3    H25    sing N N 519 
ZNI C30   H26    sing N N 520 
ZNI C30   H27    sing N N 521 
ZNI C30   H28    sing N N 522 
ZNI C31   H29    sing N N 523 
ZNI C33   H30    sing N N 524 
ZNI C33   H31    sing N N 525 
ZNI C34   H32    sing N N 526 
ZNI C34   H33    sing N N 527 
ZNI C35   H34    sing N N 528 
ZNI C36   H35    sing N N 529 
ZNI C36   H36    sing N N 530 
ZNI C37   H37    sing N N 531 
ZNI C37   H38    sing N N 532 
ZNI C38   H39    sing N N 533 
ZNI C38   H40    sing N N 534 
ZNI C39   H41    sing N N 535 
ZNI C39   H42    sing N N 536 
ZNI C4    H43    sing N N 537 
ZNI C4    H44    sing N N 538 
ZNI C40   H45    sing N N 539 
ZNI C42   H46    sing N N 540 
ZNI C42   H47    sing N N 541 
ZNI C44   H48    sing N N 542 
ZNI C44   H49    sing N N 543 
ZNI C44   H50    sing N N 544 
ZNI C45   H51    sing N N 545 
ZNI C45   H52    sing N N 546 
ZNI C45   H53    sing N N 547 
ZNI C46   H54    sing N N 548 
ZNI C46   H55    sing N N 549 
ZNI C6    H56    sing N N 550 
ZNI C8    H57    sing N N 551 
ZNI C9    H58    sing N N 552 
ZNI N1    H59    sing N N 553 
ZNI N3    H60    sing N N 554 
# 
_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 
# 
_atom_sites.entry_id                    9BGH 
_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]   0.015271 
_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]   0.012227 
_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]   0.007823 
_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 
AL 
C  
F  
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     . VAL A 1 3   ? -1.279  -14.621 3.775   1.00 63.39 ? 2   VAL B N     1 
ATOM   2    C  CA    . VAL A 1 3   ? -1.245  -14.193 5.173   1.00 61.38 ? 2   VAL B CA    1 
ATOM   3    C  C     . VAL A 1 3   ? -0.206  -13.062 5.374   1.00 53.72 ? 2   VAL B C     1 
ATOM   4    O  O     . VAL A 1 3   ? 0.850   -13.061 4.738   1.00 53.98 ? 2   VAL B O     1 
ATOM   5    C  CB    . VAL A 1 3   ? -0.999  -15.411 6.082   1.00 60.20 ? 2   VAL B CB    1 
ATOM   6    C  CG1   . VAL A 1 3   ? -0.727  -14.998 7.525   1.00 56.69 ? 2   VAL B CG1   1 
ATOM   7    C  CG2   . VAL A 1 3   ? -2.197  -16.306 6.020   1.00 61.39 ? 2   VAL B CG2   1 
ATOM   8    N  N     . ASN A 1 4   ? -0.551  -12.086 6.225   1.00 52.32 ? 3   ASN B N     1 
ATOM   9    C  CA    . ASN A 1 4   ? 0.223   -10.856 6.394   1.00 44.18 ? 3   ASN B CA    1 
ATOM   10   C  C     . ASN A 1 4   ? 1.685   -11.170 6.705   1.00 44.62 ? 3   ASN B C     1 
ATOM   11   O  O     . ASN A 1 4   ? 1.958   -11.998 7.584   1.00 47.80 ? 3   ASN B O     1 
ATOM   12   C  CB    . ASN A 1 4   ? -0.378  -10.021 7.522   1.00 38.28 ? 3   ASN B CB    1 
ATOM   13   C  CG    . ASN A 1 4   ? -1.623  -9.247  7.066   1.00 36.49 ? 3   ASN B CG    1 
ATOM   14   O  OD1   . ASN A 1 4   ? -1.874  -9.131  5.861   1.00 37.34 ? 3   ASN B OD1   1 
ATOM   15   N  ND2   . ASN A 1 4   ? -2.388  -8.714  8.021   1.00 35.38 ? 3   ASN B ND2   1 
ATOM   16   N  N     . PRO A 1 5   ? 2.637   -10.570 5.997   1.00 42.26 ? 4   PRO B N     1 
ATOM   17   C  CA    . PRO A 1 5   ? 4.048   -10.857 6.269   1.00 39.62 ? 4   PRO B CA    1 
ATOM   18   C  C     . PRO A 1 5   ? 4.480   -10.235 7.583   1.00 38.35 ? 4   PRO B C     1 
ATOM   19   O  O     . PRO A 1 5   ? 3.861   -9.286  8.085   1.00 34.29 ? 4   PRO B O     1 
ATOM   20   C  CB    . PRO A 1 5   ? 4.783   -10.211 5.091   1.00 41.41 ? 4   PRO B CB    1 
ATOM   21   C  CG    . PRO A 1 5   ? 3.879   -9.094  4.662   1.00 39.84 ? 4   PRO B CG    1 
ATOM   22   C  CD    . PRO A 1 5   ? 2.470   -9.652  4.854   1.00 39.98 ? 4   PRO B CD    1 
ATOM   23   N  N     . THR A 1 6   ? 5.587   -10.767 8.112   1.00 33.99 ? 5   THR B N     1 
ATOM   24   C  CA    . THR A 1 6   ? 6.174   -10.294 9.371   1.00 36.69 ? 5   THR B CA    1 
ATOM   25   C  C     . THR A 1 6   ? 7.641   -9.936  9.108   1.00 35.40 ? 5   THR B C     1 
ATOM   26   O  O     . THR A 1 6   ? 8.365   -10.735 8.501   1.00 36.30 ? 5   THR B O     1 
ATOM   27   C  CB    . THR A 1 6   ? 6.070   -11.404 10.419  1.00 37.52 ? 5   THR B CB    1 
ATOM   28   O  OG1   . THR A 1 6   ? 4.692   -11.544 10.825  1.00 38.40 ? 5   THR B OG1   1 
ATOM   29   C  CG2   . THR A 1 6   ? 6.892   -11.024 11.614  1.00 39.75 ? 5   THR B CG2   1 
ATOM   30   N  N     . VAL A 1 7   ? 8.088   -8.749  9.540   1.00 32.62 ? 6   VAL B N     1 
ATOM   31   C  CA    . VAL A 1 7   ? 9.473   -8.332  9.355   1.00 30.70 ? 6   VAL B CA    1 
ATOM   32   C  C     . VAL A 1 7   ? 10.058  -7.959  10.714  1.00 31.28 ? 6   VAL B C     1 
ATOM   33   O  O     . VAL A 1 7   ? 9.344   -7.679  11.673  1.00 28.69 ? 6   VAL B O     1 
ATOM   34   C  CB    . VAL A 1 7   ? 9.632   -7.148  8.380   1.00 30.15 ? 6   VAL B CB    1 
ATOM   35   C  CG1   . VAL A 1 7   ? 9.027   -7.473  7.000   1.00 29.73 ? 6   VAL B CG1   1 
ATOM   36   C  CG2   . VAL A 1 7   ? 9.004   -5.950  8.923   1.00 28.42 ? 6   VAL B CG2   1 
ATOM   37   N  N     . PHE A 1 8   ? 11.381  -7.945  10.784  1.00 31.76 ? 7   PHE B N     1 
ATOM   38   C  CA    . PHE A 1 8   ? 12.069  -7.632  12.034  1.00 30.31 ? 7   PHE B CA    1 
ATOM   39   C  C     . PHE A 1 8   ? 13.171  -6.621  11.783  1.00 28.28 ? 7   PHE B C     1 
ATOM   40   O  O     . PHE A 1 8   ? 13.777  -6.601  10.713  1.00 27.27 ? 7   PHE B O     1 
ATOM   41   C  CB    . PHE A 1 8   ? 12.709  -8.885  12.681  1.00 28.96 ? 7   PHE B CB    1 
ATOM   42   C  CG    . PHE A 1 8   ? 13.955  -9.370  11.968  1.00 33.44 ? 7   PHE B CG    1 
ATOM   43   C  CD1   . PHE A 1 8   ? 13.868  -10.293 10.919  1.00 35.00 ? 7   PHE B CD1   1 
ATOM   44   C  CD2   . PHE A 1 8   ? 15.224  -8.898  12.332  1.00 33.64 ? 7   PHE B CD2   1 
ATOM   45   C  CE1   . PHE A 1 8   ? 15.014  -10.746 10.258  1.00 36.92 ? 7   PHE B CE1   1 
ATOM   46   C  CE2   . PHE A 1 8   ? 16.351  -9.329  11.659  1.00 34.39 ? 7   PHE B CE2   1 
ATOM   47   C  CZ    . PHE A 1 8   ? 16.253  -10.247 10.627  1.00 35.40 ? 7   PHE B CZ    1 
ATOM   48   N  N     . PHE A 1 9   ? 13.456  -5.824  12.811  1.00 26.65 ? 8   PHE B N     1 
ATOM   49   C  CA    . PHE A 1 9   ? 14.644  -4.974  12.904  1.00 25.96 ? 8   PHE B CA    1 
ATOM   50   C  C     . PHE A 1 9   ? 15.450  -5.420  14.116  1.00 28.83 ? 8   PHE B C     1 
ATOM   51   O  O     . PHE A 1 9   ? 14.883  -5.568  15.195  1.00 26.62 ? 8   PHE B O     1 
ATOM   52   C  CB    . PHE A 1 9   ? 14.309  -3.489  13.160  1.00 25.69 ? 8   PHE B CB    1 
ATOM   53   C  CG    . PHE A 1 9   ? 13.581  -2.764  12.050  1.00 23.67 ? 8   PHE B CG    1 
ATOM   54   C  CD1   . PHE A 1 9   ? 13.506  -3.268  10.738  1.00 25.56 ? 8   PHE B CD1   1 
ATOM   55   C  CD2   . PHE A 1 9   ? 13.043  -1.523  12.311  1.00 19.81 ? 8   PHE B CD2   1 
ATOM   56   C  CE1   . PHE A 1 9   ? 12.841  -2.521  9.691   1.00 23.54 ? 8   PHE B CE1   1 
ATOM   57   C  CE2   . PHE A 1 9   ? 12.378  -0.786  11.300  1.00 21.39 ? 8   PHE B CE2   1 
ATOM   58   C  CZ    . PHE A 1 9   ? 12.306  -1.271  9.979   1.00 22.30 ? 8   PHE B CZ    1 
ATOM   59   N  N     . ASP A 1 10  ? 16.747  -5.568  13.957  1.00 25.11 ? 9   ASP B N     1 
ATOM   60   C  CA    . ASP A 1 10  ? 17.638  -5.665  15.098  1.00 26.88 ? 9   ASP B CA    1 
ATOM   61   C  C     . ASP A 1 10  ? 18.210  -4.273  15.351  1.00 28.30 ? 9   ASP B C     1 
ATOM   62   O  O     . ASP A 1 10  ? 18.904  -3.709  14.490  1.00 27.47 ? 9   ASP B O     1 
ATOM   63   C  CB    . ASP A 1 10  ? 18.729  -6.711  14.858  1.00 29.06 ? 9   ASP B CB    1 
ATOM   64   C  CG    . ASP A 1 10  ? 18.210  -8.137  14.952  1.00 33.91 ? 9   ASP B CG    1 
ATOM   65   O  OD1   . ASP A 1 10  ? 17.386  -8.428  15.832  1.00 37.01 ? 9   ASP B OD1   1 
ATOM   66   O  OD2   . ASP A 1 10  ? 18.669  -8.995  14.197  1.00 38.31 ? 9   ASP B OD2   1 
ATOM   67   N  N     . ILE A 1 11  ? 17.889  -3.709  16.529  1.00 25.36 ? 10  ILE B N     1 
ATOM   68   C  CA    . ILE A 1 11  ? 18.244  -2.339  16.869  1.00 25.94 ? 10  ILE B CA    1 
ATOM   69   C  C     . ILE A 1 11  ? 19.566  -2.345  17.600  1.00 26.30 ? 10  ILE B C     1 
ATOM   70   O  O     . ILE A 1 11  ? 19.800  -3.183  18.485  1.00 26.04 ? 10  ILE B O     1 
ATOM   71   C  CB    . ILE A 1 11  ? 17.171  -1.673  17.745  1.00 25.86 ? 10  ILE B CB    1 
ATOM   72   C  CG1   . ILE A 1 11  ? 15.772  -1.756  17.064  1.00 24.55 ? 10  ILE B CG1   1 
ATOM   73   C  CG2   . ILE A 1 11  ? 17.528  -0.194  17.990  1.00 22.22 ? 10  ILE B CG2   1 
ATOM   74   C  CD1   . ILE A 1 11  ? 15.651  -0.987  15.726  1.00 23.60 ? 10  ILE B CD1   1 
ATOM   75   N  N     . ALA A 1 12  ? 20.414  -1.383  17.265  1.00 23.41 ? 11  ALA B N     1 
ATOM   76   C  CA    . ALA A 1 12  ? 21.646  -1.144  17.998  1.00 26.23 ? 11  ALA B CA    1 
ATOM   77   C  C     . ALA A 1 12  ? 21.762  0.334   18.361  1.00 27.45 ? 11  ALA B C     1 
ATOM   78   O  O     . ALA A 1 12  ? 21.178  1.215   17.713  1.00 24.80 ? 11  ALA B O     1 
ATOM   79   C  CB    . ALA A 1 12  ? 22.913  -1.592  17.209  1.00 26.74 ? 11  ALA B CB    1 
ATOM   80   N  N     . VAL A 1 13  ? 22.534  0.587   19.417  1.00 24.21 ? 12  VAL B N     1 
ATOM   81   C  CA    . VAL A 1 13  ? 22.705  1.914   19.981  1.00 26.17 ? 12  VAL B CA    1 
ATOM   82   C  C     . VAL A 1 13  ? 24.199  2.120   20.033  1.00 28.37 ? 12  VAL B C     1 
ATOM   83   O  O     . VAL A 1 13  ? 24.885  1.401   20.775  1.00 27.83 ? 12  VAL B O     1 
ATOM   84   C  CB    . VAL A 1 13  ? 22.087  2.053   21.380  1.00 28.82 ? 12  VAL B CB    1 
ATOM   85   C  CG1   . VAL A 1 13  ? 22.278  3.455   21.922  1.00 30.61 ? 12  VAL B CG1   1 
ATOM   86   C  CG2   . VAL A 1 13  ? 20.599  1.706   21.350  1.00 25.89 ? 12  VAL B CG2   1 
ATOM   87   N  N     . ASP A 1 14  ? 24.707  3.081   19.238  1.00 26.90 ? 13  ASP B N     1 
ATOM   88   C  CA    . ASP A 1 14  ? 26.150  3.250   19.042  1.00 27.40 ? 13  ASP B CA    1 
ATOM   89   C  C     . ASP A 1 14  ? 26.797  1.902   18.846  1.00 29.95 ? 13  ASP B C     1 
ATOM   90   O  O     . ASP A 1 14  ? 27.865  1.626   19.412  1.00 30.72 ? 13  ASP B O     1 
ATOM   91   C  CB    . ASP A 1 14  ? 26.782  3.987   20.210  1.00 32.74 ? 13  ASP B CB    1 
ATOM   92   C  CG    . ASP A 1 14  ? 26.406  5.454   20.219  1.00 33.57 ? 13  ASP B CG    1 
ATOM   93   O  OD1   . ASP A 1 14  ? 26.014  5.987   19.139  1.00 32.23 ? 13  ASP B OD1   1 
ATOM   94   O  OD2   . ASP A 1 14  ? 26.500  6.056   21.300  1.00 33.10 ? 13  ASP B OD2   1 
ATOM   95   N  N     . GLY A 1 15  ? 26.162  1.059   18.044  1.00 29.12 ? 14  GLY B N     1 
ATOM   96   C  CA    . GLY A 1 15  ? 26.765  -0.194  17.651  1.00 30.91 ? 14  GLY B CA    1 
ATOM   97   C  C     . GLY A 1 15  ? 26.537  -1.328  18.608  1.00 32.31 ? 14  GLY B C     1 
ATOM   98   O  O     . GLY A 1 15  ? 26.938  -2.455  18.310  1.00 31.62 ? 14  GLY B O     1 
ATOM   99   N  N     . GLU A 1 16  ? 25.917  -1.069  19.752  1.00 29.96 ? 15  GLU B N     1 
ATOM   100  C  CA    . GLU A 1 16  ? 25.757  -2.106  20.760  1.00 28.07 ? 15  GLU B CA    1 
ATOM   101  C  C     . GLU A 1 16  ? 24.352  -2.649  20.673  1.00 28.65 ? 15  GLU B C     1 
ATOM   102  O  O     . GLU A 1 16  ? 23.414  -1.852  20.601  1.00 28.38 ? 15  GLU B O     1 
ATOM   103  C  CB    . GLU A 1 16  ? 26.033  -1.536  22.146  1.00 33.25 ? 15  GLU B CB    1 
ATOM   104  C  CG    . GLU A 1 16  ? 25.809  -2.432  23.308  1.00 34.63 ? 15  GLU B CG    1 
ATOM   105  C  CD    . GLU A 1 16  ? 25.760  -1.607  24.617  1.00 37.89 ? 15  GLU B CD    1 
ATOM   106  O  OE1   . GLU A 1 16  ? 24.718  -1.610  25.330  1.00 43.46 ? 15  GLU B OE1   1 
ATOM   107  O  OE2   . GLU A 1 16  ? 26.773  -0.922  24.870  1.00 38.44 ? 15  GLU B OE2   1 
ATOM   108  N  N     . PRO A 1 17  ? 24.176  -3.964  20.597  1.00 27.86 ? 16  PRO B N     1 
ATOM   109  C  CA    . PRO A 1 17  ? 22.826  -4.516  20.461  1.00 28.92 ? 16  PRO B CA    1 
ATOM   110  C  C     . PRO A 1 17  ? 21.905  -4.045  21.573  1.00 29.59 ? 16  PRO B C     1 
ATOM   111  O  O     . PRO A 1 17  ? 22.268  -4.064  22.744  1.00 27.34 ? 16  PRO B O     1 
ATOM   112  C  CB    . PRO A 1 17  ? 23.047  -6.022  20.528  1.00 27.79 ? 16  PRO B CB    1 
ATOM   113  C  CG    . PRO A 1 17  ? 24.445  -6.177  19.949  1.00 30.64 ? 16  PRO B CG    1 
ATOM   114  C  CD    . PRO A 1 17  ? 25.215  -5.002  20.511  1.00 29.74 ? 16  PRO B CD    1 
ATOM   115  N  N     . LEU A 1 18  ? 20.700  -3.641  21.169  1.00 29.70 ? 17  LEU B N     1 
ATOM   116  C  CA    . LEU A 1 18  ? 19.569  -3.295  22.035  1.00 27.83 ? 17  LEU B CA    1 
ATOM   117  C  C     . LEU A 1 18  ? 18.514  -4.397  22.056  1.00 27.97 ? 17  LEU B C     1 
ATOM   118  O  O     . LEU A 1 18  ? 18.135  -4.871  23.141  1.00 27.13 ? 17  LEU B O     1 
ATOM   119  C  CB    . LEU A 1 18  ? 18.934  -1.981  21.579  1.00 25.93 ? 17  LEU B CB    1 
ATOM   120  C  CG    . LEU A 1 18  ? 17.816  -1.489  22.529  1.00 26.80 ? 17  LEU B CG    1 
ATOM   121  C  CD1   . LEU A 1 18  ? 18.315  -1.314  23.964  1.00 28.80 ? 17  LEU B CD1   1 
ATOM   122  C  CD2   . LEU A 1 18  ? 17.156  -0.163  21.932  1.00 20.20 ? 17  LEU B CD2   1 
ATOM   123  N  N     . GLY A 1 19  ? 18.062  -4.842  20.890  1.00 27.12 ? 18  GLY B N     1 
ATOM   124  C  CA    . GLY A 1 19  ? 17.099  -5.925  20.812  1.00 28.24 ? 18  GLY B CA    1 
ATOM   125  C  C     . GLY A 1 19  ? 16.375  -5.938  19.484  1.00 29.06 ? 18  GLY B C     1 
ATOM   126  O  O     . GLY A 1 19  ? 16.551  -5.056  18.650  1.00 27.24 ? 18  GLY B O     1 
ATOM   127  N  N     . ARG A 1 20  ? 15.497  -6.941  19.337  1.00 27.33 ? 19  ARG B N     1 
ATOM   128  C  CA    . ARG A 1 20  ? 14.743  -7.160  18.102  1.00 30.29 ? 19  ARG B CA    1 
ATOM   129  C  C     . ARG A 1 20  ? 13.322  -6.651  18.264  1.00 30.41 ? 19  ARG B C     1 
ATOM   130  O  O     . ARG A 1 20  ? 12.646  -6.986  19.258  1.00 29.25 ? 19  ARG B O     1 
ATOM   131  C  CB    . ARG A 1 20  ? 14.683  -8.640  17.746  1.00 29.33 ? 19  ARG B CB    1 
ATOM   132  C  CG    . ARG A 1 20  ? 13.826  -8.907  16.514  1.00 33.70 ? 19  ARG B CG    1 
ATOM   133  C  CD    . ARG A 1 20  ? 14.088  -10.313 15.986  1.00 33.14 ? 19  ARG B CD    1 
ATOM   134  N  NE    . ARG A 1 20  ? 15.436  -10.413 15.455  1.00 35.28 ? 19  ARG B NE    1 
ATOM   135  C  CZ    . ARG A 1 20  ? 15.868  -11.447 14.760  1.00 37.72 ? 19  ARG B CZ    1 
ATOM   136  N  NH1   . ARG A 1 20  ? 15.081  -12.487 14.526  1.00 37.48 ? 19  ARG B NH1   1 
ATOM   137  N  NH2   . ARG A 1 20  ? 17.104  -11.427 14.266  1.00 35.06 ? 19  ARG B NH2   1 
ATOM   138  N  N     . VAL A 1 21  ? 12.847  -5.895  17.277  1.00 26.22 ? 20  VAL B N     1 
ATOM   139  C  CA    . VAL A 1 21  ? 11.436  -5.571  17.210  1.00 25.34 ? 20  VAL B CA    1 
ATOM   140  C  C     . VAL A 1 21  ? 10.883  -6.180  15.937  1.00 26.76 ? 20  VAL B C     1 
ATOM   141  O  O     . VAL A 1 21  ? 11.529  -6.142  14.887  1.00 28.41 ? 20  VAL B O     1 
ATOM   142  C  CB    . VAL A 1 21  ? 11.171  -4.056  17.262  1.00 28.35 ? 20  VAL B CB    1 
ATOM   143  C  CG1   . VAL A 1 21  ? 12.050  -3.346  16.343  1.00 27.82 ? 20  VAL B CG1   1 
ATOM   144  C  CG2   . VAL A 1 21  ? 9.747   -3.789  16.872  1.00 25.59 ? 20  VAL B CG2   1 
ATOM   145  N  N     . SER A 1 22  ? 9.707   -6.764  16.014  1.00 27.93 ? 21  SER B N     1 
ATOM   146  C  CA    . SER A 1 22  ? 9.117   -7.278  14.786  1.00 26.59 ? 21  SER B CA    1 
ATOM   147  C  C     . SER A 1 22  ? 7.763   -6.641  14.536  1.00 28.39 ? 21  SER B C     1 
ATOM   148  O  O     . SER A 1 22  ? 7.121   -6.091  15.445  1.00 28.31 ? 21  SER B O     1 
ATOM   149  C  CB    . SER A 1 22  ? 9.013   -8.816  14.843  1.00 31.07 ? 21  SER B CB    1 
ATOM   150  O  OG    . SER A 1 22  ? 8.123   -9.207  15.865  1.00 34.17 ? 21  SER B OG    1 
ATOM   151  N  N     . PHE A 1 23  ? 7.353   -6.681  13.272  1.00 27.98 ? 22  PHE B N     1 
ATOM   152  C  CA    . PHE A 1 23  ? 6.143   -5.992  12.823  1.00 27.99 ? 22  PHE B CA    1 
ATOM   153  C  C     . PHE A 1 23  ? 5.313   -6.900  11.955  1.00 29.65 ? 22  PHE B C     1 
ATOM   154  O  O     . PHE A 1 23  ? 5.838   -7.634  11.113  1.00 30.74 ? 22  PHE B O     1 
ATOM   155  C  CB    . PHE A 1 23  ? 6.399   -4.739  11.984  1.00 24.72 ? 22  PHE B CB    1 
ATOM   156  C  CG    . PHE A 1 23  ? 7.413   -3.821  12.565  1.00 23.77 ? 22  PHE B CG    1 
ATOM   157  C  CD1   . PHE A 1 23  ? 8.752   -3.983  12.261  1.00 24.92 ? 22  PHE B CD1   1 
ATOM   158  C  CD2   . PHE A 1 23  ? 7.035   -2.785  13.396  1.00 23.03 ? 22  PHE B CD2   1 
ATOM   159  C  CE1   . PHE A 1 23  ? 9.732   -3.145  12.769  1.00 25.82 ? 22  PHE B CE1   1 
ATOM   160  C  CE2   . PHE A 1 23  ? 8.033   -1.881  13.911  1.00 22.20 ? 22  PHE B CE2   1 
ATOM   161  C  CZ    . PHE A 1 23  ? 9.378   -2.076  13.614  1.00 24.30 ? 22  PHE B CZ    1 
ATOM   162  N  N     . GLU A 1 24  ? 4.017   -6.825  12.169  1.00 28.53 ? 23  GLU B N     1 
ATOM   163  C  CA    . GLU A 1 24  ? 3.061   -7.390  11.230  1.00 31.63 ? 23  GLU B CA    1 
ATOM   164  C  C     . GLU A 1 24  ? 2.701   -6.272  10.252  1.00 28.34 ? 23  GLU B C     1 
ATOM   165  O  O     . GLU A 1 24  ? 2.481   -5.127  10.665  1.00 25.20 ? 23  GLU B O     1 
ATOM   166  C  CB    . GLU A 1 24  ? 1.828   -7.941  11.947  1.00 31.26 ? 23  GLU B CB    1 
ATOM   167  C  CG    . GLU A 1 24  ? 0.762   -8.327  10.938  1.00 34.28 ? 23  GLU B CG    1 
ATOM   168  C  CD    . GLU A 1 24  ? -0.485  -8.971  11.508  1.00 41.20 ? 23  GLU B CD    1 
ATOM   169  O  OE1   . GLU A 1 24  ? -0.509  -9.351  12.692  1.00 42.14 ? 23  GLU B OE1   1 
ATOM   170  O  OE2   . GLU A 1 24  ? -1.464  -9.110  10.742  1.00 42.08 ? 23  GLU B OE2   1 
ATOM   171  N  N     . LEU A 1 25  ? 2.730   -6.580  8.964   1.00 28.87 ? 24  LEU B N     1 
ATOM   172  C  CA    . LEU A 1 25  ? 2.399   -5.622  7.912   1.00 27.17 ? 24  LEU B CA    1 
ATOM   173  C  C     . LEU A 1 25  ? 1.029   -5.958  7.330   1.00 28.82 ? 24  LEU B C     1 
ATOM   174  O  O     . LEU A 1 25  ? 0.798   -7.086  6.909   1.00 29.28 ? 24  LEU B O     1 
ATOM   175  C  CB    . LEU A 1 25  ? 3.434   -5.671  6.799   1.00 26.82 ? 24  LEU B CB    1 
ATOM   176  C  CG    . LEU A 1 25  ? 4.905   -5.510  7.184   1.00 27.49 ? 24  LEU B CG    1 
ATOM   177  C  CD1   . LEU A 1 25  ? 5.762   -5.518  5.906   1.00 29.18 ? 24  LEU B CD1   1 
ATOM   178  C  CD2   . LEU A 1 25  ? 5.171   -4.263  8.072   1.00 23.47 ? 24  LEU B CD2   1 
ATOM   179  N  N     . PHE A 1 26  ? 0.132   -4.981  7.278   1.00 27.27 ? 25  PHE B N     1 
ATOM   180  C  CA    . PHE A 1 26  ? -1.273  -5.284  6.979   1.00 28.56 ? 25  PHE B CA    1 
ATOM   181  C  C     . PHE A 1 26  ? -1.504  -5.320  5.465   1.00 29.45 ? 25  PHE B C     1 
ATOM   182  O  O     . PHE A 1 26  ? -2.152  -4.448  4.875   1.00 27.09 ? 25  PHE B O     1 
ATOM   183  C  CB    . PHE A 1 26  ? -2.156  -4.245  7.645   1.00 27.57 ? 25  PHE B CB    1 
ATOM   184  C  CG    . PHE A 1 26  ? -1.977  -4.179  9.162   1.00 30.77 ? 25  PHE B CG    1 
ATOM   185  C  CD1   . PHE A 1 26  ? -1.885  -5.347  9.915   1.00 32.82 ? 25  PHE B CD1   1 
ATOM   186  C  CD2   . PHE A 1 26  ? -1.923  -2.963  9.801   1.00 25.05 ? 25  PHE B CD2   1 
ATOM   187  C  CE1   . PHE A 1 26  ? -1.758  -5.294  11.295  1.00 31.91 ? 25  PHE B CE1   1 
ATOM   188  C  CE2   . PHE A 1 26  ? -1.816  -2.905  11.193  1.00 29.46 ? 25  PHE B CE2   1 
ATOM   189  C  CZ    . PHE A 1 26  ? -1.722  -4.060  11.919  1.00 28.49 ? 25  PHE B CZ    1 
ATOM   190  N  N     . ALA A 1 27  ? -0.923  -6.344  4.828   1.00 28.58 ? 26  ALA B N     1 
ATOM   191  C  CA    . ALA A 1 27  ? -1.073  -6.475  3.381   1.00 29.78 ? 26  ALA B CA    1 
ATOM   192  C  C     . ALA A 1 27  ? -2.532  -6.696  2.982   1.00 31.59 ? 26  ALA B C     1 
ATOM   193  O  O     . ALA A 1 27  ? -2.915  -6.394  1.842   1.00 30.79 ? 26  ALA B O     1 
ATOM   194  C  CB    . ALA A 1 27  ? -0.241  -7.655  2.862   1.00 32.48 ? 26  ALA B CB    1 
ATOM   195  N  N     . ASP A 1 28  ? -3.339  -7.264  3.885   1.00 28.59 ? 27  ASP B N     1 
ATOM   196  C  CA    . ASP A 1 28  ? -4.756  -7.465  3.614   1.00 32.54 ? 27  ASP B CA    1 
ATOM   197  C  C     . ASP A 1 28  ? -5.492  -6.151  3.387   1.00 34.31 ? 27  ASP B C     1 
ATOM   198  O  O     . ASP A 1 28  ? -6.470  -6.138  2.639   1.00 33.97 ? 27  ASP B O     1 
ATOM   199  C  CB    . ASP A 1 28  ? -5.435  -8.266  4.748   1.00 36.64 ? 27  ASP B CB    1 
ATOM   200  C  CG    . ASP A 1 28  ? -5.188  -7.674  6.138   1.00 38.08 ? 27  ASP B CG    1 
ATOM   201  O  OD1   . ASP A 1 28  ? -4.313  -6.824  6.283   1.00 36.71 ? 27  ASP B OD1   1 
ATOM   202  O  OD2   . ASP A 1 28  ? -5.860  -8.092  7.108   1.00 48.99 ? 27  ASP B OD2   1 
ATOM   203  N  N     . LYS A 1 29  ? -5.023  -5.041  3.983   1.00 31.86 ? 28  LYS B N     1 
ATOM   204  C  CA    . LYS A 1 29  ? -5.699  -3.730  3.915   1.00 30.06 ? 28  LYS B CA    1 
ATOM   205  C  C     . LYS A 1 29  ? -4.917  -2.698  3.110   1.00 27.71 ? 28  LYS B C     1 
ATOM   206  O  O     . LYS A 1 29  ? -5.528  -1.928  2.373   1.00 28.08 ? 28  LYS B O     1 
ATOM   207  C  CB    . LYS A 1 29  ? -5.941  -3.157  5.326   1.00 33.54 ? 28  LYS B CB    1 
ATOM   208  C  CG    . LYS A 1 29  ? -7.217  -3.691  5.995   1.00 37.29 ? 28  LYS B CG    1 
ATOM   209  C  CD    . LYS A 1 29  ? -8.403  -3.725  5.063   1.00 44.02 ? 28  LYS B CD    1 
ATOM   210  C  CE    . LYS A 1 29  ? -9.668  -2.970  5.566   1.00 47.72 ? 28  LYS B CE    1 
ATOM   211  N  NZ    . LYS A 1 29  ? -10.709 -2.668  4.495   1.00 48.19 ? 28  LYS B NZ    1 
ATOM   212  N  N     . VAL A 1 30  ? -3.586  -2.702  3.177   1.00 27.98 ? 29  VAL B N     1 
ATOM   213  C  CA    . VAL A 1 30  ? -2.743  -1.798  2.374   1.00 26.98 ? 29  VAL B CA    1 
ATOM   214  C  C     . VAL A 1 30  ? -1.647  -2.591  1.684   1.00 25.77 ? 29  VAL B C     1 
ATOM   215  O  O     . VAL A 1 30  ? -0.484  -2.482  2.077   1.00 25.28 ? 29  VAL B O     1 
ATOM   216  C  CB    . VAL A 1 30  ? -2.077  -0.694  3.211   1.00 27.04 ? 29  VAL B CB    1 
ATOM   217  C  CG1   . VAL A 1 30  ? -2.910  0.533   3.230   1.00 24.51 ? 29  VAL B CG1   1 
ATOM   218  C  CG2   . VAL A 1 30  ? -1.758  -1.177  4.620   1.00 25.84 ? 29  VAL B CG2   1 
ATOM   219  N  N     . PRO A 1 31  ? -1.953  -3.372  0.655   1.00 26.35 ? 30  PRO B N     1 
ATOM   220  C  CA    . PRO A 1 31  ? -0.941  -4.277  0.103   1.00 27.87 ? 30  PRO B CA    1 
ATOM   221  C  C     . PRO A 1 31  ? 0.233   -3.553  -0.532  1.00 27.33 ? 30  PRO B C     1 
ATOM   222  O  O     . PRO A 1 31  ? 1.363   -4.054  -0.457  1.00 28.25 ? 30  PRO B O     1 
ATOM   223  C  CB    . PRO A 1 31  ? -1.745  -5.099  -0.930  1.00 26.72 ? 30  PRO B CB    1 
ATOM   224  C  CG    . PRO A 1 31  ? -2.953  -4.188  -1.307  1.00 30.20 ? 30  PRO B CG    1 
ATOM   225  C  CD    . PRO A 1 31  ? -3.286  -3.585  0.068   1.00 26.78 ? 30  PRO B CD    1 
ATOM   226  N  N     . LYS A 1 32  ? -0.001  -2.419  -1.211  1.00 24.57 ? 31  LYS B N     1 
ATOM   227  C  CA    . LYS A 1 32  ? 1.108   -1.709  -1.844  1.00 26.59 ? 31  LYS B CA    1 
ATOM   228  C  C     . LYS A 1 32  ? 2.091   -1.169  -0.815  1.00 24.48 ? 31  LYS B C     1 
ATOM   229  O  O     . LYS A 1 32  ? 3.307   -1.284  -0.988  1.00 23.16 ? 31  LYS B O     1 
ATOM   230  C  CB    . LYS A 1 32  ? 0.572   -0.568  -2.726  1.00 26.74 ? 31  LYS B CB    1 
ATOM   231  C  CG    . LYS A 1 32  ? 1.643   0.010   -3.629  1.00 26.42 ? 31  LYS B CG    1 
ATOM   232  C  CD    . LYS A 1 32  ? 0.999   0.877   -4.789  1.00 30.76 ? 31  LYS B CD    1 
ATOM   233  C  CE    . LYS A 1 32  ? 2.081   1.499   -5.637  1.00 29.10 ? 31  LYS B CE    1 
ATOM   234  N  NZ    . LYS A 1 32  ? 1.511   2.229   -6.832  1.00 29.69 ? 31  LYS B NZ    1 
ATOM   235  N  N     . THR A 1 33  ? 1.569   -0.540  0.235   1.00 24.18 ? 32  THR B N     1 
ATOM   236  C  CA    . THR A 1 33  ? 2.387   0.085   1.262   1.00 21.40 ? 32  THR B CA    1 
ATOM   237  C  C     . THR A 1 33  ? 3.081   -0.992  2.101   1.00 21.23 ? 32  THR B C     1 
ATOM   238  O  O     . THR A 1 33  ? 4.253   -0.843  2.468   1.00 21.91 ? 32  THR B O     1 
ATOM   239  C  CB    . THR A 1 33  ? 1.495   1.015   2.090   1.00 21.99 ? 32  THR B CB    1 
ATOM   240  O  OG1   . THR A 1 33  ? 0.706   1.880   1.208   1.00 22.09 ? 32  THR B OG1   1 
ATOM   241  C  CG2   . THR A 1 33  ? 2.357   1.854   3.098   1.00 18.93 ? 32  THR B CG2   1 
ATOM   242  N  N     . ALA A 1 34  ? 2.381   -2.100  2.359   1.00 23.72 ? 33  ALA B N     1 
ATOM   243  C  CA    . ALA A 1 34  ? 3.002   -3.217  3.093   1.00 24.08 ? 33  ALA B CA    1 
ATOM   244  C  C     . ALA A 1 34  ? 4.137   -3.846  2.287   1.00 25.37 ? 33  ALA B C     1 
ATOM   245  O  O     . ALA A 1 34  ? 5.188   -4.188  2.842   1.00 24.89 ? 33  ALA B O     1 
ATOM   246  C  CB    . ALA A 1 34  ? 1.935   -4.258  3.445   1.00 25.02 ? 33  ALA B CB    1 
ATOM   247  N  N     . GLU A 1 35  ? 3.957   -4.015  0.978   1.00 23.14 ? 34  GLU B N     1 
ATOM   248  C  CA    . GLU A 1 35  ? 5.012   -4.664  0.195   1.00 26.09 ? 34  GLU B CA    1 
ATOM   249  C  C     . GLU A 1 35  ? 6.256   -3.785  0.104   1.00 25.45 ? 34  GLU B C     1 
ATOM   250  O  O     . GLU A 1 35  ? 7.375   -4.298  0.107   1.00 28.15 ? 34  GLU B O     1 
ATOM   251  C  CB    . GLU A 1 35  ? 4.487   -5.006  -1.200  1.00 28.53 ? 34  GLU B CB    1 
ATOM   252  C  CG    . GLU A 1 35  ? 5.520   -5.426  -2.271  1.00 29.82 ? 34  GLU B CG    1 
ATOM   253  C  CD    . GLU A 1 35  ? 6.310   -6.713  -1.935  1.00 35.27 ? 34  GLU B CD    1 
ATOM   254  O  OE1   . GLU A 1 35  ? 5.897   -7.457  -1.015  1.00 35.04 ? 34  GLU B OE1   1 
ATOM   255  O  OE2   . GLU A 1 35  ? 7.344   -6.983  -2.613  1.00 36.10 ? 34  GLU B OE2   1 
ATOM   256  N  N     . ASN A 1 36  ? 6.076   -2.473  -0.047  1.00 23.74 ? 35  ASN B N     1 
ATOM   257  C  CA    . ASN A 1 36  ? 7.218   -1.557  -0.002  1.00 23.35 ? 35  ASN B CA    1 
ATOM   258  C  C     . ASN A 1 36  ? 8.038   -1.791  1.260   1.00 23.92 ? 35  ASN B C     1 
ATOM   259  O  O     . ASN A 1 36  ? 9.259   -1.971  1.203   1.00 24.14 ? 35  ASN B O     1 
ATOM   260  C  CB    . ASN A 1 36  ? 6.718   -0.112  -0.060  1.00 23.29 ? 35  ASN B CB    1 
ATOM   261  C  CG    . ASN A 1 36  ? 7.848   0.931   -0.063  1.00 22.00 ? 35  ASN B CG    1 
ATOM   262  O  OD1   . ASN A 1 36  ? 8.734   0.916   -0.927  1.00 22.49 ? 35  ASN B OD1   1 
ATOM   263  N  ND2   . ASN A 1 36  ? 7.775   1.883   0.891   1.00 21.36 ? 35  ASN B ND2   1 
ATOM   264  N  N     . PHE A 1 37  ? 7.378   -1.773  2.411   1.00 23.06 ? 36  PHE B N     1 
ATOM   265  C  CA    . PHE A 1 37  ? 8.123   -1.880  3.660   1.00 24.28 ? 36  PHE B CA    1 
ATOM   266  C  C     . PHE A 1 37  ? 8.789   -3.253  3.771   1.00 26.01 ? 36  PHE B C     1 
ATOM   267  O  O     . PHE A 1 37  ? 9.924   -3.368  4.248   1.00 23.51 ? 36  PHE B O     1 
ATOM   268  C  CB    . PHE A 1 37  ? 7.191   -1.645  4.849   1.00 22.25 ? 36  PHE B CB    1 
ATOM   269  C  CG    . PHE A 1 37  ? 7.900   -1.476  6.157   1.00 21.47 ? 36  PHE B CG    1 
ATOM   270  C  CD1   . PHE A 1 37  ? 8.303   -0.187  6.565   1.00 19.17 ? 36  PHE B CD1   1 
ATOM   271  C  CD2   . PHE A 1 37  ? 8.117   -2.570  7.014   1.00 21.29 ? 36  PHE B CD2   1 
ATOM   272  C  CE1   . PHE A 1 37  ? 8.955   -0.001  7.796   1.00 20.50 ? 36  PHE B CE1   1 
ATOM   273  C  CE2   . PHE A 1 37  ? 8.775   -2.372  8.276   1.00 22.27 ? 36  PHE B CE2   1 
ATOM   274  C  CZ    . PHE A 1 37  ? 9.181   -1.083  8.629   1.00 21.49 ? 36  PHE B CZ    1 
ATOM   275  N  N     . ARG A 1 38  ? 8.090   -4.294  3.338   1.00 25.06 ? 37  ARG B N     1 
ATOM   276  C  CA    . ARG A 1 38  ? 8.651   -5.642  3.359   1.00 28.06 ? 37  ARG B CA    1 
ATOM   277  C  C     . ARG A 1 38  ? 9.919   -5.716  2.532   1.00 29.99 ? 37  ARG B C     1 
ATOM   278  O  O     . ARG A 1 38  ? 10.962  -6.189  3.007   1.00 28.11 ? 37  ARG B O     1 
ATOM   279  C  CB    . ARG A 1 38  ? 7.611   -6.640  2.810   1.00 26.51 ? 37  ARG B CB    1 
ATOM   280  C  CG    . ARG A 1 38  ? 8.074   -8.097  2.978   1.00 29.54 ? 37  ARG B CG    1 
ATOM   281  C  CD    . ARG A 1 38  ? 7.334   -9.134  2.111   1.00 37.27 ? 37  ARG B CD    1 
ATOM   282  N  NE    . ARG A 1 38  ? 7.625   -8.940  0.699   1.00 36.29 ? 37  ARG B NE    1 
ATOM   283  C  CZ    . ARG A 1 38  ? 8.796   -9.179  0.128   1.00 39.72 ? 37  ARG B CZ    1 
ATOM   284  N  NH1   . ARG A 1 38  ? 9.777   -9.809  0.774   1.00 38.49 ? 37  ARG B NH1   1 
ATOM   285  N  NH2   . ARG A 1 38  ? 8.997   -8.763  -1.117  1.00 40.34 ? 37  ARG B NH2   1 
ATOM   286  N  N     . ALA A 1 39  ? 9.840   -5.260  1.269   1.00 26.81 ? 38  ALA B N     1 
ATOM   287  C  CA    . ALA A 1 39  ? 10.994  -5.370  0.384   1.00 28.24 ? 38  ALA B CA    1 
ATOM   288  C  C     . ALA A 1 39  ? 12.166  -4.528  0.885   1.00 29.76 ? 38  ALA B C     1 
ATOM   289  O  O     . ALA A 1 39  ? 13.320  -4.939  0.752   1.00 29.64 ? 38  ALA B O     1 
ATOM   290  C  CB    . ALA A 1 39  ? 10.606  -4.981  -1.043  1.00 29.23 ? 38  ALA B CB    1 
ATOM   291  N  N     . LEU A 1 40  ? 11.897  -3.336  1.455   1.00 25.88 ? 39  LEU B N     1 
ATOM   292  C  CA    . LEU A 1 40  ? 13.001  -2.541  1.984   1.00 22.45 ? 39  LEU B CA    1 
ATOM   293  C  C     . LEU A 1 40  ? 13.647  -3.200  3.210   1.00 23.59 ? 39  LEU B C     1 
ATOM   294  O  O     . LEU A 1 40  ? 14.862  -3.034  3.467   1.00 24.39 ? 39  LEU B O     1 
ATOM   295  C  CB    . LEU A 1 40  ? 12.489  -1.157  2.343   1.00 20.13 ? 39  LEU B CB    1 
ATOM   296  C  CG    . LEU A 1 40  ? 11.989  -0.358  1.125   1.00 23.54 ? 39  LEU B CG    1 
ATOM   297  C  CD1   . LEU A 1 40  ? 11.266  0.938   1.568   1.00 21.29 ? 39  LEU B CD1   1 
ATOM   298  C  CD2   . LEU A 1 40  ? 13.169  -0.035  0.236   1.00 24.02 ? 39  LEU B CD2   1 
ATOM   299  N  N     . SER A 1 41  ? 12.850  -3.923  3.995   1.00 24.32 ? 40  SER B N     1 
ATOM   300  C  CA    . SER A 1 41  ? 13.421  -4.648  5.129   1.00 27.05 ? 40  SER B CA    1 
ATOM   301  C  C     . SER A 1 41  ? 14.301  -5.822  4.668   1.00 30.02 ? 40  SER B C     1 
ATOM   302  O  O     . SER A 1 41  ? 15.292  -6.135  5.320   1.00 31.11 ? 40  SER B O     1 
ATOM   303  C  CB    . SER A 1 41  ? 12.304  -5.141  6.054   1.00 27.22 ? 40  SER B CB    1 
ATOM   304  O  OG    . SER A 1 41  ? 11.527  -4.027  6.512   1.00 25.50 ? 40  SER B OG    1 
ATOM   305  N  N     . THR A 1 42  ? 13.995  -6.463  3.544   1.00 31.74 ? 41  THR B N     1 
ATOM   306  C  CA    . THR A 1 42  ? 14.863  -7.564  3.130   1.00 33.51 ? 41  THR B CA    1 
ATOM   307  C  C     . THR A 1 42  ? 16.065  -7.117  2.317   1.00 34.23 ? 41  THR B C     1 
ATOM   308  O  O     . THR A 1 42  ? 17.008  -7.901  2.155   1.00 33.59 ? 41  THR B O     1 
ATOM   309  C  CB    . THR A 1 42  ? 14.117  -8.601  2.276   1.00 36.51 ? 41  THR B CB    1 
ATOM   310  O  OG1   . THR A 1 42  ? 13.727  -7.990  1.027   1.00 35.38 ? 41  THR B OG1   1 
ATOM   311  C  CG2   . THR A 1 42  ? 12.908  -9.157  3.038   1.00 31.47 ? 41  THR B CG2   1 
ATOM   312  N  N     . GLY A 1 43  ? 16.030  -5.918  1.755   1.00 30.11 ? 42  GLY B N     1 
ATOM   313  C  CA    . GLY A 1 43  ? 17.098  -5.465  0.890   1.00 32.95 ? 42  GLY B CA    1 
ATOM   314  C  C     . GLY A 1 43  ? 17.060  -6.032  -0.502  1.00 34.91 ? 42  GLY B C     1 
ATOM   315  O  O     . GLY A 1 43  ? 18.010  -5.821  -1.268  1.00 38.55 ? 42  GLY B O     1 
ATOM   316  N  N     . GLU A 1 44  ? 15.982  -6.719  -0.862  1.00 38.43 ? 43  GLU B N     1 
ATOM   317  C  CA    . GLU A 1 44  ? 15.989  -7.552  -2.069  1.00 40.13 ? 43  GLU B CA    1 
ATOM   318  C  C     . GLU A 1 44  ? 16.059  -6.733  -3.355  1.00 42.85 ? 43  GLU B C     1 
ATOM   319  O  O     . GLU A 1 44  ? 16.451  -7.272  -4.407  1.00 41.18 ? 43  GLU B O     1 
ATOM   320  C  CB    . GLU A 1 44  ? 14.766  -8.471  -2.063  1.00 45.61 ? 43  GLU B CB    1 
ATOM   321  C  CG    . GLU A 1 44  ? 13.387  -7.825  -2.289  1.00 41.96 ? 43  GLU B CG    1 
ATOM   322  C  CD    . GLU A 1 44  ? 12.270  -8.807  -1.911  1.00 48.52 ? 43  GLU B CD    1 
ATOM   323  O  OE1   . GLU A 1 44  ? 12.226  -9.219  -0.713  1.00 41.18 ? 43  GLU B OE1   1 
ATOM   324  O  OE2   . GLU A 1 44  ? 11.460  -9.192  -2.803  1.00 47.79 ? 43  GLU B OE2   1 
ATOM   325  N  N     . LYS A 1 45  ? 15.703  -5.448  -3.312  1.00 37.31 ? 44  LYS B N     1 
ATOM   326  C  CA    . LYS A 1 45  ? 15.813  -4.653  -4.524  1.00 37.80 ? 44  LYS B CA    1 
ATOM   327  C  C     . LYS A 1 45  ? 17.204  -4.074  -4.710  1.00 39.22 ? 44  LYS B C     1 
ATOM   328  O  O     . LYS A 1 45  ? 17.416  -3.329  -5.673  1.00 42.11 ? 44  LYS B O     1 
ATOM   329  C  CB    . LYS A 1 45  ? 14.772  -3.529  -4.510  1.00 33.39 ? 44  LYS B CB    1 
ATOM   330  C  CG    . LYS A 1 45  ? 13.352  -4.014  -4.275  1.00 33.24 ? 44  LYS B CG    1 
ATOM   331  C  CD    . LYS A 1 45  ? 12.867  -4.855  -5.447  1.00 39.58 ? 44  LYS B CD    1 
ATOM   332  C  CE    . LYS A 1 45  ? 11.360  -5.034  -5.383  1.00 39.19 ? 44  LYS B CE    1 
ATOM   333  N  NZ    . LYS A 1 45  ? 10.878  -6.072  -6.373  1.00 38.57 ? 44  LYS B NZ    1 
ATOM   334  N  N     . GLY A 1 46  ? 18.151  -4.389  -3.811  1.00 37.83 ? 45  GLY B N     1 
ATOM   335  C  CA    . GLY A 1 46  ? 19.492  -3.816  -3.818  1.00 38.40 ? 45  GLY B CA    1 
ATOM   336  C  C     . GLY A 1 46  ? 19.700  -2.607  -2.907  1.00 38.10 ? 45  GLY B C     1 
ATOM   337  O  O     . GLY A 1 46  ? 20.793  -2.001  -2.950  1.00 35.85 ? 45  GLY B O     1 
ATOM   338  N  N     . PHE A 1 47  ? 18.697  -2.248  -2.093  1.00 30.78 ? 46  PHE B N     1 
ATOM   339  C  CA    . PHE A 1 47  ? 18.704  -1.091  -1.193  1.00 30.90 ? 46  PHE B CA    1 
ATOM   340  C  C     . PHE A 1 47  ? 17.637  -1.301  -0.133  1.00 31.36 ? 46  PHE B C     1 
ATOM   341  O  O     . PHE A 1 47  ? 16.704  -2.082  -0.319  1.00 28.96 ? 46  PHE B O     1 
ATOM   342  C  CB    . PHE A 1 47  ? 18.462  0.234   -1.932  1.00 31.49 ? 46  PHE B CB    1 
ATOM   343  C  CG    . PHE A 1 47  ? 17.194  0.271   -2.774  1.00 33.04 ? 46  PHE B CG    1 
ATOM   344  C  CD1   . PHE A 1 47  ? 15.957  0.638   -2.224  1.00 29.48 ? 46  PHE B CD1   1 
ATOM   345  C  CD2   . PHE A 1 47  ? 17.260  -0.034  -4.128  1.00 33.70 ? 46  PHE B CD2   1 
ATOM   346  C  CE1   . PHE A 1 47  ? 14.787  0.668   -3.032  1.00 30.11 ? 46  PHE B CE1   1 
ATOM   347  C  CE2   . PHE A 1 47  ? 16.110  0.003   -4.946  1.00 32.59 ? 46  PHE B CE2   1 
ATOM   348  C  CZ    . PHE A 1 47  ? 14.875  0.368   -4.393  1.00 33.34 ? 46  PHE B CZ    1 
ATOM   349  N  N     . GLY A 1 48  ? 17.751  -0.588  0.983   1.00 28.38 ? 47  GLY B N     1 
ATOM   350  C  CA    . GLY A 1 48  ? 16.784  -0.826  2.034   1.00 26.43 ? 47  GLY B CA    1 
ATOM   351  C  C     . GLY A 1 48  ? 17.262  -0.273  3.354   1.00 25.11 ? 47  GLY B C     1 
ATOM   352  O  O     . GLY A 1 48  ? 18.251  0.449   3.414   1.00 23.42 ? 47  GLY B O     1 
ATOM   353  N  N     . TYR A 1 49  ? 16.552  -0.694  4.411   1.00 25.41 ? 48  TYR B N     1 
ATOM   354  C  CA    . TYR A 1 49  ? 16.684  -0.168  5.767   1.00 23.73 ? 48  TYR B CA    1 
ATOM   355  C  C     . TYR A 1 49  ? 17.966  -0.576  6.477   1.00 26.50 ? 48  TYR B C     1 
ATOM   356  O  O     . TYR A 1 49  ? 18.366  0.095   7.430   1.00 23.76 ? 48  TYR B O     1 
ATOM   357  C  CB    . TYR A 1 49  ? 15.498  -0.642  6.594   1.00 22.57 ? 48  TYR B CB    1 
ATOM   358  C  CG    . TYR A 1 49  ? 14.201  -0.038  6.154   1.00 21.80 ? 48  TYR B CG    1 
ATOM   359  C  CD1   . TYR A 1 49  ? 14.104  1.334   5.890   1.00 22.27 ? 48  TYR B CD1   1 
ATOM   360  C  CD2   . TYR A 1 49  ? 13.038  -0.825  6.075   1.00 21.35 ? 48  TYR B CD2   1 
ATOM   361  C  CE1   . TYR A 1 49  ? 12.876  1.885   5.464   1.00 18.38 ? 48  TYR B CE1   1 
ATOM   362  C  CE2   . TYR A 1 49  ? 11.841  -0.303  5.685   1.00 20.87 ? 48  TYR B CE2   1 
ATOM   363  C  CZ    . TYR A 1 49  ? 11.744  1.075   5.420   1.00 22.27 ? 48  TYR B CZ    1 
ATOM   364  O  OH    . TYR A 1 49  ? 10.534  1.624   5.019   1.00 19.73 ? 48  TYR B OH    1 
ATOM   365  N  N     . LYS A 1 50  ? 18.579  -1.698  6.099   1.00 26.24 ? 49  LYS B N     1 
ATOM   366  C  CA    . LYS A 1 50  ? 19.708  -2.194  6.887   1.00 26.29 ? 49  LYS B CA    1 
ATOM   367  C  C     . LYS A 1 50  ? 20.795  -1.127  6.975   1.00 27.40 ? 49  LYS B C     1 
ATOM   368  O  O     . LYS A 1 50  ? 21.258  -0.612  5.945   1.00 27.79 ? 49  LYS B O     1 
ATOM   369  C  CB    . LYS A 1 50  ? 20.267  -3.470  6.249   1.00 27.74 ? 49  LYS B CB    1 
ATOM   370  C  CG    . LYS A 1 50  ? 21.543  -4.029  7.008   1.00 31.01 ? 49  LYS B CG    1 
ATOM   371  C  CD    . LYS A 1 50  ? 21.840  -5.493  6.619   1.00 32.17 ? 49  LYS B CD    1 
ATOM   372  C  CE    . LYS A 1 50  ? 22.986  -6.106  7.437   1.00 35.47 ? 49  LYS B CE    1 
ATOM   373  N  NZ    . LYS A 1 50  ? 23.156  -7.527  6.967   1.00 41.21 ? 49  LYS B NZ    1 
ATOM   374  N  N     . GLY A 1 51  ? 21.197  -0.788  8.217   1.00 27.87 ? 50  GLY B N     1 
ATOM   375  C  CA    . GLY A 1 51  ? 22.283  0.152   8.415   1.00 26.85 ? 50  GLY B CA    1 
ATOM   376  C  C     . GLY A 1 51  ? 21.836  1.583   8.563   1.00 27.42 ? 50  GLY B C     1 
ATOM   377  O  O     . GLY A 1 51  ? 22.672  2.441   8.894   1.00 26.74 ? 50  GLY B O     1 
ATOM   378  N  N     . SER A 1 52  ? 20.560  1.862   8.281   1.00 23.46 ? 51  SER B N     1 
ATOM   379  C  CA    . SER A 1 52  ? 19.996  3.194   8.436   1.00 23.67 ? 51  SER B CA    1 
ATOM   380  C  C     . SER A 1 52  ? 19.669  3.493   9.920   1.00 26.11 ? 51  SER B C     1 
ATOM   381  O  O     . SER A 1 52  ? 19.712  2.620   10.812  1.00 24.55 ? 51  SER B O     1 
ATOM   382  C  CB    . SER A 1 52  ? 18.761  3.349   7.518   1.00 22.02 ? 51  SER B CB    1 
ATOM   383  O  OG    . SER A 1 52  ? 17.673  2.514   7.925   1.00 24.35 ? 51  SER B OG    1 
ATOM   384  N  N     . CYS A 1 53  ? 19.427  4.763   10.199  1.00 22.25 ? 52  CYS B N     1 
ATOM   385  C  CA    . CYS A 1 53  ? 19.201  5.179   11.581  1.00 20.76 ? 52  CYS B CA    1 
ATOM   386  C  C     . CYS A 1 53  ? 17.783  5.670   11.817  1.00 21.27 ? 52  CYS B C     1 
ATOM   387  O  O     . CYS A 1 53  ? 17.015  6.002   10.907  1.00 21.25 ? 52  CYS B O     1 
ATOM   388  C  CB    . CYS A 1 53  ? 20.119  6.307   12.007  1.00 21.78 ? 52  CYS B CB    1 
ATOM   389  S  SG    . CYS A 1 53  ? 19.806  7.881   11.232  1.00 41.18 ? 52  CYS B SG    1 
ATOM   390  N  N     . PHE A 1 54  ? 17.431  5.666   13.105  1.00 19.98 ? 53  PHE B N     1 
ATOM   391  C  CA    . PHE A 1 54  ? 16.242  6.360   13.600  1.00 19.87 ? 53  PHE B CA    1 
ATOM   392  C  C     . PHE A 1 54  ? 16.672  7.786   13.867  1.00 19.69 ? 53  PHE B C     1 
ATOM   393  O  O     . PHE A 1 54  ? 17.342  8.083   14.872  1.00 21.06 ? 53  PHE B O     1 
ATOM   394  C  CB    . PHE A 1 54  ? 15.655  5.669   14.851  1.00 19.28 ? 53  PHE B CB    1 
ATOM   395  C  CG    . PHE A 1 54  ? 14.753  4.483   14.519  1.00 20.93 ? 53  PHE B CG    1 
ATOM   396  C  CD1   . PHE A 1 54  ? 15.311  3.215   14.244  1.00 20.10 ? 53  PHE B CD1   1 
ATOM   397  C  CD2   . PHE A 1 54  ? 13.317  4.654   14.447  1.00 19.91 ? 53  PHE B CD2   1 
ATOM   398  C  CE1   . PHE A 1 54  ? 14.516  2.169   13.911  1.00 20.26 ? 53  PHE B CE1   1 
ATOM   399  C  CE2   . PHE A 1 54  ? 12.521  3.581   14.118  1.00 18.47 ? 53  PHE B CE2   1 
ATOM   400  C  CZ    . PHE A 1 54  ? 13.114  2.318   13.865  1.00 18.69 ? 53  PHE B CZ    1 
ATOM   401  N  N     . HIS A 1 55  ? 16.357  8.676   12.941  1.00 17.52 ? 54  HIS B N     1 
ATOM   402  C  CA    . HIS A 1 55  ? 16.910  10.018  13.049  1.00 15.71 ? 54  HIS B CA    1 
ATOM   403  C  C     . HIS A 1 55  ? 16.111  10.925  13.941  1.00 16.82 ? 54  HIS B C     1 
ATOM   404  O  O     . HIS A 1 55  ? 16.629  11.999  14.294  1.00 18.65 ? 54  HIS B O     1 
ATOM   405  C  CB    . HIS A 1 55  ? 16.987  10.695  11.677  1.00 17.75 ? 54  HIS B CB    1 
ATOM   406  C  CG    . HIS A 1 55  ? 15.682  10.796  10.963  1.00 18.31 ? 54  HIS B CG    1 
ATOM   407  N  ND1   . HIS A 1 55  ? 15.108  9.736   10.284  1.00 18.27 ? 54  HIS B ND1   1 
ATOM   408  C  CD2   . HIS A 1 55  ? 14.896  11.875  10.716  1.00 17.08 ? 54  HIS B CD2   1 
ATOM   409  C  CE1   . HIS A 1 55  ? 13.996  10.152  9.694   1.00 17.79 ? 54  HIS B CE1   1 
ATOM   410  N  NE2   . HIS A 1 55  ? 13.848  11.444  9.953   1.00 17.69 ? 54  HIS B NE2   1 
ATOM   411  N  N     . ARG A 1 56  ? 14.834  10.588  14.221  1.00 17.08 ? 55  ARG B N     1 
ATOM   412  C  CA    . ARG A 1 56  ? 13.971  11.465  15.005  1.00 17.72 ? 55  ARG B CA    1 
ATOM   413  C  C     . ARG A 1 56  ? 13.197  10.653  16.037  1.00 20.70 ? 55  ARG B C     1 
ATOM   414  O  O     . ARG A 1 56  ? 12.429  9.755   15.679  1.00 20.89 ? 55  ARG B O     1 
ATOM   415  C  CB    . ARG A 1 56  ? 12.993  12.210  14.083  1.00 17.74 ? 55  ARG B CB    1 
ATOM   416  C  CG    . ARG A 1 56  ? 11.919  13.019  14.839  1.00 19.84 ? 55  ARG B CG    1 
ATOM   417  C  CD    . ARG A 1 56  ? 10.985  13.605  13.767  1.00 18.64 ? 55  ARG B CD    1 
ATOM   418  N  NE    . ARG A 1 56  ? 11.684  14.655  13.052  1.00 19.25 ? 55  ARG B NE    1 
ATOM   419  C  CZ    . ARG A 1 56  ? 11.319  15.073  11.856  1.00 21.12 ? 55  ARG B CZ    1 
ATOM   420  N  NH1   . ARG A 1 56  ? 10.290  14.531  11.232  1.00 21.21 ? 55  ARG B NH1   1 
ATOM   421  N  NH2   . ARG A 1 56  ? 11.987  16.070  11.287  1.00 20.45 ? 55  ARG B NH2   1 
ATOM   422  N  N     . ILE A 1 57  ? 13.418  10.944  17.316  1.00 18.68 ? 56  ILE B N     1 
ATOM   423  C  CA    . ILE A 1 57  ? 12.771  10.200  18.383  1.00 16.69 ? 56  ILE B CA    1 
ATOM   424  C  C     . ILE A 1 57  ? 12.236  11.230  19.354  1.00 18.73 ? 56  ILE B C     1 
ATOM   425  O  O     . ILE A 1 57  ? 13.015  12.027  19.877  1.00 18.52 ? 56  ILE B O     1 
ATOM   426  C  CB    . ILE A 1 57  ? 13.718  9.225   19.092  1.00 17.73 ? 56  ILE B CB    1 
ATOM   427  C  CG1   . ILE A 1 57  ? 14.145  8.102   18.138  1.00 21.11 ? 56  ILE B CG1   1 
ATOM   428  C  CG2   . ILE A 1 57  ? 13.019  8.696   20.364  1.00 19.66 ? 56  ILE B CG2   1 
ATOM   429  C  CD1   . ILE A 1 57  ? 15.312  7.269   18.633  1.00 20.04 ? 56  ILE B CD1   1 
ATOM   430  N  N     . ILE A 1 58  ? 10.921  11.279  19.549  1.00 17.05 ? 57  ILE B N     1 
ATOM   431  C  CA    . ILE A 1 58  ? 10.328  12.307  20.393  1.00 17.70 ? 57  ILE B CA    1 
ATOM   432  C  C     . ILE A 1 58  ? 9.542   11.616  21.488  1.00 19.18 ? 57  ILE B C     1 
ATOM   433  O  O     . ILE A 1 58  ? 8.483   11.059  21.241  1.00 17.97 ? 57  ILE B O     1 
ATOM   434  C  CB    . ILE A 1 58  ? 9.447   13.285  19.589  1.00 16.52 ? 57  ILE B CB    1 
ATOM   435  C  CG1   . ILE A 1 58  ? 10.333  13.995  18.554  1.00 19.48 ? 57  ILE B CG1   1 
ATOM   436  C  CG2   . ILE A 1 58  ? 8.790   14.272  20.548  1.00 20.12 ? 57  ILE B CG2   1 
ATOM   437  C  CD1   . ILE A 1 58  ? 9.589   14.822  17.538  1.00 20.71 ? 57  ILE B CD1   1 
ATOM   438  N  N     . PRO A 1 59  ? 10.089  11.535  22.690  1.00 19.86 ? 58  PRO B N     1 
ATOM   439  C  CA    . PRO A 1 59  ? 9.412   10.793  23.768  1.00 17.92 ? 58  PRO B CA    1 
ATOM   440  C  C     . PRO A 1 59  ? 7.998   11.307  23.981  1.00 21.82 ? 58  PRO B C     1 
ATOM   441  O  O     . PRO A 1 59  ? 7.742   12.521  24.005  1.00 19.28 ? 58  PRO B O     1 
ATOM   442  C  CB    . PRO A 1 59  ? 10.302  11.050  24.984  1.00 20.86 ? 58  PRO B CB    1 
ATOM   443  C  CG    . PRO A 1 59  ? 11.690  11.220  24.346  1.00 19.94 ? 58  PRO B CG    1 
ATOM   444  C  CD    . PRO A 1 59  ? 11.412  12.045  23.131  1.00 20.77 ? 58  PRO B CD    1 
ATOM   445  N  N     . GLY A 1 60  ? 7.083   10.341  24.138  1.00 20.94 ? 59  GLY B N     1 
ATOM   446  C  CA    . GLY A 1 60  ? 5.679   10.625  24.284  1.00 20.53 ? 59  GLY B CA    1 
ATOM   447  C  C     . GLY A 1 60  ? 4.915   10.515  22.980  1.00 19.17 ? 59  GLY B C     1 
ATOM   448  O  O     . GLY A 1 60  ? 3.663   10.508  23.014  1.00 20.70 ? 59  GLY B O     1 
ATOM   449  N  N     . PHE A 1 61  ? 5.621   10.441  21.855  1.00 17.90 ? 60  PHE B N     1 
ATOM   450  C  CA    . PHE A 1 61  ? 4.943   10.441  20.560  1.00 18.20 ? 60  PHE B CA    1 
ATOM   451  C  C     . PHE A 1 61  ? 5.386   9.321   19.615  1.00 17.05 ? 60  PHE B C     1 
ATOM   452  O  O     . PHE A 1 61  ? 4.589   8.428   19.276  1.00 17.28 ? 60  PHE B O     1 
ATOM   453  C  CB    . PHE A 1 61  ? 5.121   11.826  19.903  1.00 22.45 ? 60  PHE B CB    1 
ATOM   454  C  CG    . PHE A 1 61  ? 4.467   12.938  20.696  1.00 21.09 ? 60  PHE B CG    1 
ATOM   455  C  CD1   . PHE A 1 61  ? 3.107   13.217  20.541  1.00 24.15 ? 60  PHE B CD1   1 
ATOM   456  C  CD2   . PHE A 1 61  ? 5.213   13.705  21.607  1.00 21.23 ? 60  PHE B CD2   1 
ATOM   457  C  CE1   . PHE A 1 61  ? 2.475   14.287  21.283  1.00 24.98 ? 60  PHE B CE1   1 
ATOM   458  C  CE2   . PHE A 1 61  ? 4.584   14.754  22.336  1.00 24.75 ? 60  PHE B CE2   1 
ATOM   459  C  CZ    . PHE A 1 61  ? 3.216   15.023  22.168  1.00 27.15 ? 60  PHE B CZ    1 
ATOM   460  N  N     . MET A 1 62  ? 6.644   9.305   19.191  1.00 16.52 ? 61  MET B N     1 
ATOM   461  C  CA    . MET A 1 62  ? 7.019   8.375   18.143  1.00 15.55 ? 61  MET B CA    1 
ATOM   462  C  C     . MET A 1 62  ? 8.511   8.325   17.902  1.00 17.15 ? 61  MET B C     1 
ATOM   463  O  O     . MET A 1 62  ? 9.282   9.178   18.358  1.00 18.95 ? 61  MET B O     1 
ATOM   464  C  CB    . MET A 1 62  ? 6.223   8.640   16.792  1.00 18.04 ? 61  MET B CB    1 
ATOM   465  C  CG    . MET A 1 62  ? 5.821   10.133  16.448  1.00 22.21 ? 61  MET B CG    1 
ATOM   466  S  SD    . MET A 1 62  ? 7.215   11.272  16.477  1.00 20.36 ? 61  MET B SD    1 
ATOM   467  C  CE    . MET A 1 62  ? 8.150   10.304  15.233  1.00 22.12 ? 61  MET B CE    1 
ATOM   468  N  N     . CYS A 1 63  ? 8.902   7.280   17.177  1.00 18.89 ? 62  CYS B N     1 
ATOM   469  C  CA    . CYS A 1 63  ? 10.266  7.048   16.719  1.00 15.88 ? 62  CYS B CA    1 
ATOM   470  C  C     . CYS A 1 63  ? 10.226  6.978   15.197  1.00 18.24 ? 62  CYS B C     1 
ATOM   471  O  O     . CYS A 1 63  ? 9.511   6.132   14.642  1.00 19.65 ? 62  CYS B O     1 
ATOM   472  C  CB    . CYS A 1 63  ? 10.807  5.697   17.216  1.00 16.86 ? 62  CYS B CB    1 
ATOM   473  S  SG    . CYS A 1 63  ? 11.004  5.584   19.030  1.00 21.71 ? 62  CYS B SG    1 
ATOM   474  N  N     . GLN A 1 64  ? 11.032  7.778   14.525  1.00 16.65 ? 63  GLN B N     1 
ATOM   475  C  CA    . GLN A 1 64  ? 10.965  7.839   13.065  1.00 17.22 ? 63  GLN B CA    1 
ATOM   476  C  C     . GLN A 1 64  ? 12.302  7.444   12.434  1.00 18.49 ? 63  GLN B C     1 
ATOM   477  O  O     . GLN A 1 64  ? 13.371  7.856   12.923  1.00 18.32 ? 63  GLN B O     1 
ATOM   478  C  CB    . GLN A 1 64  ? 10.540  9.255   12.657  1.00 17.62 ? 63  GLN B CB    1 
ATOM   479  C  CG    . GLN A 1 64  ? 10.560  9.516   11.141  1.00 17.80 ? 63  GLN B CG    1 
ATOM   480  C  CD    . GLN A 1 64  ? 9.965   10.856  10.759  1.00 19.05 ? 63  GLN B CD    1 
ATOM   481  O  OE1   . GLN A 1 64  ? 9.264   11.459  11.579  1.00 18.90 ? 63  GLN B OE1   1 
ATOM   482  N  NE2   . GLN A 1 64  ? 10.196  11.323  9.504   1.00 15.74 ? 63  GLN B NE2   1 
ATOM   483  N  N     . GLY A 1 65  ? 12.246  6.690   11.314  1.00 16.95 ? 64  GLY B N     1 
ATOM   484  C  CA    . GLY A 1 65  ? 13.507  6.404   10.637  1.00 14.98 ? 64  GLY B CA    1 
ATOM   485  C  C     . GLY A 1 65  ? 13.230  6.155   9.165   1.00 15.81 ? 64  GLY B C     1 
ATOM   486  O  O     . GLY A 1 65  ? 12.244  6.683   8.606   1.00 17.13 ? 64  GLY B O     1 
ATOM   487  N  N     . GLY A 1 66  ? 14.131  5.408   8.518   1.00 18.04 ? 65  GLY B N     1 
ATOM   488  C  CA    . GLY A 1 66  ? 13.865  4.993   7.145   1.00 17.63 ? 65  GLY B CA    1 
ATOM   489  C  C     . GLY A 1 66  ? 14.551  5.768   6.043   1.00 20.09 ? 65  GLY B C     1 
ATOM   490  O  O     . GLY A 1 66  ? 14.362  5.406   4.853   1.00 19.65 ? 65  GLY B O     1 
ATOM   491  N  N     . ASP A 1 67  ? 15.376  6.793   6.369   1.00 19.83 ? 66  ASP B N     1 
ATOM   492  C  CA    . ASP A 1 67  ? 16.119  7.506   5.335   1.00 20.40 ? 66  ASP B CA    1 
ATOM   493  C  C     . ASP A 1 67  ? 17.445  6.794   5.108   1.00 22.37 ? 66  ASP B C     1 
ATOM   494  O  O     . ASP A 1 67  ? 18.457  7.105   5.741   1.00 22.91 ? 66  ASP B O     1 
ATOM   495  C  CB    . ASP A 1 67  ? 16.370  8.962   5.723   1.00 20.43 ? 66  ASP B CB    1 
ATOM   496  C  CG    . ASP A 1 67  ? 17.247  9.715   4.689   1.00 21.08 ? 66  ASP B CG    1 
ATOM   497  O  OD1   . ASP A 1 67  ? 17.631  9.142   3.635   1.00 22.95 ? 66  ASP B OD1   1 
ATOM   498  O  OD2   . ASP A 1 67  ? 17.515  10.911  4.898   1.00 19.49 ? 66  ASP B OD2   1 
ATOM   499  N  N     . PHE A 1 68  ? 17.462  5.903   4.118   1.00 17.97 ? 67  PHE B N     1 
ATOM   500  C  CA    . PHE A 1 68  ? 18.658  5.137   3.830   1.00 21.95 ? 67  PHE B CA    1 
ATOM   501  C  C     . PHE A 1 68  ? 19.409  5.683   2.639   1.00 25.46 ? 67  PHE B C     1 
ATOM   502  O  O     . PHE A 1 68  ? 20.423  5.095   2.241   1.00 25.83 ? 67  PHE B O     1 
ATOM   503  C  CB    . PHE A 1 68  ? 18.339  3.639   3.605   1.00 23.92 ? 67  PHE B CB    1 
ATOM   504  C  CG    . PHE A 1 68  ? 17.362  3.402   2.495   1.00 22.34 ? 67  PHE B CG    1 
ATOM   505  C  CD1   . PHE A 1 68  ? 17.776  3.340   1.172   1.00 25.61 ? 67  PHE B CD1   1 
ATOM   506  C  CD2   . PHE A 1 68  ? 16.018  3.229   2.774   1.00 21.32 ? 67  PHE B CD2   1 
ATOM   507  C  CE1   . PHE A 1 68  ? 16.831  3.135   0.154   1.00 26.09 ? 67  PHE B CE1   1 
ATOM   508  C  CE2   . PHE A 1 68  ? 15.108  3.027   1.724   1.00 22.72 ? 67  PHE B CE2   1 
ATOM   509  C  CZ    . PHE A 1 68  ? 15.528  2.990   0.465   1.00 24.46 ? 67  PHE B CZ    1 
ATOM   510  N  N     . THR A 1 69  ? 18.929  6.765   2.033   1.00 23.84 ? 68  THR B N     1 
ATOM   511  C  CA    . THR A 1 69  ? 19.670  7.301   0.892   1.00 24.88 ? 68  THR B CA    1 
ATOM   512  C  C     . THR A 1 69  ? 20.538  8.484   1.265   1.00 25.09 ? 68  THR B C     1 
ATOM   513  O  O     . THR A 1 69  ? 21.614  8.662   0.667   1.00 29.41 ? 68  THR B O     1 
ATOM   514  C  CB    . THR A 1 69  ? 18.722  7.712   -0.245  1.00 27.19 ? 68  THR B CB    1 
ATOM   515  O  OG1   . THR A 1 69  ? 17.932  8.843   0.155   1.00 24.23 ? 68  THR B OG1   1 
ATOM   516  C  CG2   . THR A 1 69  ? 17.781  6.576   -0.591  1.00 26.06 ? 68  THR B CG2   1 
ATOM   517  N  N     . ARG A 1 70  ? 20.103  9.287   2.234   1.00 25.68 ? 69  ARG B N     1 
ATOM   518  C  CA    . ARG A 1 70  ? 20.826  10.473  2.669   1.00 26.99 ? 69  ARG B CA    1 
ATOM   519  C  C     . ARG A 1 70  ? 21.238  10.424  4.119   1.00 26.16 ? 69  ARG B C     1 
ATOM   520  O  O     . ARG A 1 70  ? 22.144  11.182  4.513   1.00 28.23 ? 69  ARG B O     1 
ATOM   521  C  CB    . ARG A 1 70  ? 19.953  11.725  2.477   1.00 26.22 ? 69  ARG B CB    1 
ATOM   522  C  CG    . ARG A 1 70  ? 19.696  12.023  0.979   1.00 29.33 ? 69  ARG B CG    1 
ATOM   523  C  CD    . ARG A 1 70  ? 18.872  13.245  0.856   1.00 29.26 ? 69  ARG B CD    1 
ATOM   524  N  NE    . ARG A 1 70  ? 18.487  13.471  -0.539  1.00 35.67 ? 69  ARG B NE    1 
ATOM   525  C  CZ    . ARG A 1 70  ? 17.487  14.270  -0.886  1.00 34.63 ? 69  ARG B CZ    1 
ATOM   526  N  NH1   . ARG A 1 70  ? 16.903  15.072  0.000   1.00 29.86 ? 69  ARG B NH1   1 
ATOM   527  N  NH2   . ARG A 1 70  ? 17.030  14.225  -2.135  1.00 35.58 ? 69  ARG B NH2   1 
ATOM   528  N  N     . HIS A 1 71  ? 20.564  9.603   4.926   1.00 26.10 ? 70  HIS B N     1 
ATOM   529  C  CA    . HIS A 1 71  ? 20.868  9.444   6.363   1.00 25.00 ? 70  HIS B CA    1 
ATOM   530  C  C     . HIS A 1 71  ? 20.850  10.780  7.073   1.00 31.48 ? 70  HIS B C     1 
ATOM   531  O  O     . HIS A 1 71  ? 21.637  11.007  8.011   1.00 32.42 ? 70  HIS B O     1 
ATOM   532  C  CB    . HIS A 1 71  ? 22.226  8.773   6.579   1.00 28.00 ? 70  HIS B CB    1 
ATOM   533  C  CG    . HIS A 1 71  ? 22.402  7.509   5.786   1.00 30.26 ? 70  HIS B CG    1 
ATOM   534  N  ND1   . HIS A 1 71  ? 21.995  6.276   6.255   1.00 26.08 ? 70  HIS B ND1   1 
ATOM   535  C  CD2   . HIS A 1 71  ? 22.914  7.292   4.554   1.00 27.43 ? 70  HIS B CD2   1 
ATOM   536  C  CE1   . HIS A 1 71  ? 22.247  5.354   5.343   1.00 28.07 ? 70  HIS B CE1   1 
ATOM   537  N  NE2   . HIS A 1 71  ? 22.823  5.943   4.306   1.00 30.13 ? 70  HIS B NE2   1 
ATOM   538  N  N     . ASN A 1 72  ? 19.965  11.691  6.635   1.00 27.18 ? 71  ASN B N     1 
ATOM   539  C  CA    . ASN A 1 72  ? 19.859  12.948  7.369   1.00 26.75 ? 71  ASN B CA    1 
ATOM   540  C  C     . ASN A 1 72  ? 18.415  13.335  7.668   1.00 23.87 ? 71  ASN B C     1 
ATOM   541  O  O     . ASN A 1 72  ? 18.167  14.468  8.106   1.00 25.84 ? 71  ASN B O     1 
ATOM   542  C  CB    . ASN A 1 72  ? 20.638  14.074  6.631   1.00 26.22 ? 71  ASN B CB    1 
ATOM   543  C  CG    . ASN A 1 72  ? 20.055  14.456  5.241   1.00 29.29 ? 71  ASN B CG    1 
ATOM   544  O  OD1   . ASN A 1 72  ? 18.929  14.116  4.887   1.00 26.67 ? 71  ASN B OD1   1 
ATOM   545  N  ND2   . ASN A 1 72  ? 20.857  15.196  4.468   1.00 26.83 ? 71  ASN B ND2   1 
ATOM   546  N  N     . GLY A 1 73  ? 17.441  12.440  7.436   1.00 21.86 ? 72  GLY B N     1 
ATOM   547  C  CA    . GLY A 1 73  ? 16.047  12.794  7.632   1.00 18.30 ? 72  GLY B CA    1 
ATOM   548  C  C     . GLY A 1 73  ? 15.344  13.371  6.386   1.00 20.67 ? 72  GLY B C     1 
ATOM   549  O  O     . GLY A 1 73  ? 14.121  13.588  6.421   1.00 20.91 ? 72  GLY B O     1 
ATOM   550  N  N     . THR A 1 74  ? 16.065  13.682  5.284   1.00 19.12 ? 73  THR B N     1 
ATOM   551  C  CA    . THR A 1 74  ? 15.370  14.258  4.131   1.00 24.11 ? 73  THR B CA    1 
ATOM   552  C  C     . THR A 1 74  ? 15.137  13.250  3.009   1.00 25.19 ? 73  THR B C     1 
ATOM   553  O  O     . THR A 1 74  ? 14.403  13.558  2.037   1.00 23.94 ? 73  THR B O     1 
ATOM   554  C  CB    . THR A 1 74  ? 16.134  15.432  3.533   1.00 23.75 ? 73  THR B CB    1 
ATOM   555  O  OG1   . THR A 1 74  ? 17.351  14.961  2.925   1.00 23.95 ? 73  THR B OG1   1 
ATOM   556  C  CG2   . THR A 1 74  ? 16.439  16.548  4.603   1.00 23.13 ? 73  THR B CG2   1 
ATOM   557  N  N     . GLY A 1 75  ? 15.751  12.077  3.097   1.00 20.35 ? 74  GLY B N     1 
ATOM   558  C  CA    . GLY A 1 75  ? 15.762  11.212  1.926   1.00 21.49 ? 74  GLY B CA    1 
ATOM   559  C  C     . GLY A 1 75  ? 14.897  9.985   2.068   1.00 24.67 ? 74  GLY B C     1 
ATOM   560  O  O     . GLY A 1 75  ? 13.881  9.992   2.780   1.00 20.82 ? 74  GLY B O     1 
ATOM   561  N  N     . GLY A 1 76  ? 15.334  8.900   1.443   1.00 23.10 ? 75  GLY B N     1 
ATOM   562  C  CA    . GLY A 1 76  ? 14.535  7.700   1.346   1.00 23.35 ? 75  GLY B CA    1 
ATOM   563  C  C     . GLY A 1 76  ? 13.901  7.562   -0.039  1.00 23.47 ? 75  GLY B C     1 
ATOM   564  O  O     . GLY A 1 76  ? 13.718  8.537   -0.786  1.00 24.60 ? 75  GLY B O     1 
ATOM   565  N  N     . LYS A 1 77  ? 13.603  6.310   -0.413  1.00 22.85 ? 76  LYS B N     1 
ATOM   566  C  CA    . LYS A 1 77  ? 12.854  6.088   -1.655  1.00 22.03 ? 76  LYS B CA    1 
ATOM   567  C  C     . LYS A 1 77  ? 12.093  4.787   -1.538  1.00 21.52 ? 76  LYS B C     1 
ATOM   568  O  O     . LYS A 1 77  ? 12.462  3.907   -0.759  1.00 21.54 ? 76  LYS B O     1 
ATOM   569  C  CB    . LYS A 1 77  ? 13.778  6.044   -2.890  1.00 22.62 ? 76  LYS B CB    1 
ATOM   570  C  CG    . LYS A 1 77  ? 14.825  4.887   -2.835  1.00 25.74 ? 76  LYS B CG    1 
ATOM   571  C  CD    . LYS A 1 77  ? 15.760  4.916   -4.022  1.00 28.62 ? 76  LYS B CD    1 
ATOM   572  C  CE    . LYS A 1 77  ? 16.832  3.829   -3.881  1.00 28.87 ? 76  LYS B CE    1 
ATOM   573  N  NZ    . LYS A 1 77  ? 17.823  3.882   -5.025  1.00 35.08 ? 76  LYS B NZ    1 
ATOM   574  N  N     . SER A 1 78  ? 11.023  4.675   -2.317  1.00 22.76 ? 77  SER B N     1 
ATOM   575  C  CA    . SER A 1 78  ? 10.188  3.484   -2.282  1.00 23.58 ? 77  SER B CA    1 
ATOM   576  C  C     . SER A 1 78  ? 10.697  2.500   -3.323  1.00 25.78 ? 77  SER B C     1 
ATOM   577  O  O     . SER A 1 78  ? 11.565  2.821   -4.154  1.00 26.29 ? 77  SER B O     1 
ATOM   578  C  CB    . SER A 1 78  ? 8.706   3.826   -2.539  1.00 21.88 ? 77  SER B CB    1 
ATOM   579  O  OG    . SER A 1 78  ? 8.436   3.932   -3.940  1.00 21.67 ? 77  SER B OG    1 
ATOM   580  N  N     . ILE A 1 79  ? 10.119  1.293   -3.327  1.00 23.74 ? 78  ILE B N     1 
ATOM   581  C  CA    . ILE A 1 79  ? 10.450  0.369   -4.413  1.00 23.82 ? 78  ILE B CA    1 
ATOM   582  C  C     . ILE A 1 79  ? 9.733   0.679   -5.730  1.00 25.57 ? 78  ILE B C     1 
ATOM   583  O  O     . ILE A 1 79  ? 9.940   -0.028  -6.738  1.00 25.27 ? 78  ILE B O     1 
ATOM   584  C  CB    . ILE A 1 79  ? 10.101  -1.072  -4.016  1.00 26.68 ? 78  ILE B CB    1 
ATOM   585  C  CG1   . ILE A 1 79  ? 8.571   -1.196  -3.893  1.00 25.88 ? 78  ILE B CG1   1 
ATOM   586  C  CG2   . ILE A 1 79  ? 10.845  -1.464  -2.778  1.00 24.01 ? 78  ILE B CG2   1 
ATOM   587  C  CD1   . ILE A 1 79  ? 8.090   -2.666  -3.653  1.00 28.25 ? 78  ILE B CD1   1 
ATOM   588  N  N     . TYR A 1 80  ? 8.887   1.713   -5.746  1.00 28.04 ? 79  TYR B N     1 
ATOM   589  C  CA    . TYR A 1 80  ? 8.053   2.089   -6.891  1.00 25.91 ? 79  TYR B CA    1 
ATOM   590  C  C     . TYR A 1 80  ? 8.541   3.342   -7.595  1.00 25.33 ? 79  TYR B C     1 
ATOM   591  O  O     . TYR A 1 80  ? 7.858   3.840   -8.505  1.00 27.24 ? 79  TYR B O     1 
ATOM   592  C  CB    . TYR A 1 80  ? 6.618   2.358   -6.422  1.00 26.85 ? 79  TYR B CB    1 
ATOM   593  C  CG    . TYR A 1 80  ? 6.023   1.231   -5.602  1.00 26.49 ? 79  TYR B CG    1 
ATOM   594  C  CD1   . TYR A 1 80  ? 5.784   -0.017  -6.187  1.00 27.42 ? 79  TYR B CD1   1 
ATOM   595  C  CD2   . TYR A 1 80  ? 5.686   1.416   -4.255  1.00 24.18 ? 79  TYR B CD2   1 
ATOM   596  C  CE1   . TYR A 1 80  ? 5.253   -1.070  -5.443  1.00 29.43 ? 79  TYR B CE1   1 
ATOM   597  C  CE2   . TYR A 1 80  ? 5.176   0.373   -3.493  1.00 24.45 ? 79  TYR B CE2   1 
ATOM   598  C  CZ    . TYR A 1 80  ? 4.966   -0.877  -4.108  1.00 25.46 ? 79  TYR B CZ    1 
ATOM   599  O  OH    . TYR A 1 80  ? 4.425   -1.952  -3.409  1.00 25.98 ? 79  TYR B OH    1 
ATOM   600  N  N     . GLY A 1 81  ? 9.669   3.891   -7.174  1.00 29.23 ? 80  GLY B N     1 
ATOM   601  C  CA    . GLY A 1 81  ? 10.014  5.261   -7.503  1.00 27.22 ? 80  GLY B CA    1 
ATOM   602  C  C     . GLY A 1 81  ? 10.357  6.018   -6.239  1.00 26.88 ? 80  GLY B C     1 
ATOM   603  O  O     . GLY A 1 81  ? 10.252  5.508   -5.124  1.00 25.04 ? 80  GLY B O     1 
ATOM   604  N  N     . GLU A 1 82  ? 10.827  7.252   -6.430  1.00 25.04 ? 81  GLU B N     1 
ATOM   605  C  CA    . GLU A 1 82  ? 11.239  7.977   -5.239  1.00 22.88 ? 81  GLU B CA    1 
ATOM   606  C  C     . GLU A 1 82  ? 10.078  8.146   -4.283  1.00 25.06 ? 81  GLU B C     1 
ATOM   607  O  O     . GLU A 1 82  ? 10.228  7.919   -3.083  1.00 24.80 ? 81  GLU B O     1 
ATOM   608  C  CB    . GLU A 1 82  ? 11.846  9.327   -5.547  1.00 24.74 ? 81  GLU B CB    1 
ATOM   609  C  CG    . GLU A 1 82  ? 12.570  9.743   -4.281  1.00 35.85 ? 81  GLU B CG    1 
ATOM   610  C  CD    . GLU A 1 82  ? 13.370  11.042  -4.346  1.00 43.98 ? 81  GLU B CD    1 
ATOM   611  O  OE1   . GLU A 1 82  ? 12.770  12.134  -4.514  1.00 51.49 ? 81  GLU B OE1   1 
ATOM   612  O  OE2   . GLU A 1 82  ? 14.612  10.945  -4.226  1.00 45.96 ? 81  GLU B OE2   1 
ATOM   613  N  N     . LYS A 1 83  ? 8.886   8.455   -4.801  1.00 22.79 ? 82  LYS B N     1 
ATOM   614  C  CA    . LYS A 1 83  ? 7.727   8.534   -3.922  1.00 21.28 ? 82  LYS B CA    1 
ATOM   615  C  C     . LYS A 1 83  ? 6.519   7.844   -4.568  1.00 23.14 ? 82  LYS B C     1 
ATOM   616  O  O     . LYS A 1 83  ? 6.515   7.572   -5.777  1.00 26.18 ? 82  LYS B O     1 
ATOM   617  C  CB    . LYS A 1 83  ? 7.373   9.987   -3.629  1.00 24.82 ? 82  LYS B CB    1 
ATOM   618  C  CG    . LYS A 1 83  ? 8.623   10.819  -3.163  1.00 29.47 ? 82  LYS B CG    1 
ATOM   619  C  CD    . LYS A 1 83  ? 8.269   11.838  -2.157  1.00 29.76 ? 82  LYS B CD    1 
ATOM   620  C  CE    . LYS A 1 83  ? 9.036   13.152  -2.310  1.00 35.73 ? 82  LYS B CE    1 
ATOM   621  N  NZ    . LYS A 1 83  ? 8.226   14.140  -3.161  1.00 42.06 ? 82  LYS B NZ    1 
ATOM   622  N  N     . PHE A 1 84  ? 5.498   7.535   -3.745  1.00 21.38 ? 83  PHE B N     1 
ATOM   623  C  CA    . PHE A 1 84  ? 4.259   6.944   -4.287  1.00 22.59 ? 83  PHE B CA    1 
ATOM   624  C  C     . PHE A 1 84  ? 3.035   7.443   -3.506  1.00 20.91 ? 83  PHE B C     1 
ATOM   625  O  O     . PHE A 1 84  ? 3.139   8.030   -2.417  1.00 21.63 ? 83  PHE B O     1 
ATOM   626  C  CB    . PHE A 1 84  ? 4.308   5.391   -4.309  1.00 21.25 ? 83  PHE B CB    1 
ATOM   627  C  CG    . PHE A 1 84  ? 4.337   4.715   -2.938  1.00 21.49 ? 83  PHE B CG    1 
ATOM   628  C  CD1   . PHE A 1 84  ? 5.487   4.735   -2.166  1.00 20.78 ? 83  PHE B CD1   1 
ATOM   629  C  CD2   . PHE A 1 84  ? 3.224   4.012   -2.458  1.00 22.62 ? 83  PHE B CD2   1 
ATOM   630  C  CE1   . PHE A 1 84  ? 5.529   4.099   -0.921  1.00 22.91 ? 83  PHE B CE1   1 
ATOM   631  C  CE2   . PHE A 1 84  ? 3.263   3.333   -1.212  1.00 21.28 ? 83  PHE B CE2   1 
ATOM   632  C  CZ    . PHE A 1 84  ? 4.392   3.391   -0.459  1.00 22.12 ? 83  PHE B CZ    1 
ATOM   633  N  N     . GLU A 1 85  ? 1.874   7.234   -4.101  1.00 21.71 ? 84  GLU B N     1 
ATOM   634  C  CA    . GLU A 1 85  ? 0.654   7.884   -3.647  1.00 20.60 ? 84  GLU B CA    1 
ATOM   635  C  C     . GLU A 1 85  ? 0.154   7.260   -2.340  1.00 19.89 ? 84  GLU B C     1 
ATOM   636  O  O     . GLU A 1 85  ? 0.549   6.155   -1.946  1.00 22.04 ? 84  GLU B O     1 
ATOM   637  C  CB    . GLU A 1 85  ? -0.438  7.790   -4.721  1.00 21.61 ? 84  GLU B CB    1 
ATOM   638  C  CG    . GLU A 1 85  ? -0.908  6.344   -4.985  1.00 27.19 ? 84  GLU B CG    1 
ATOM   639  C  CD    . GLU A 1 85  ? 0.146   5.481   -5.756  1.00 32.53 ? 84  GLU B CD    1 
ATOM   640  O  OE1   . GLU A 1 85  ? 1.051   6.063   -6.432  1.00 27.82 ? 84  GLU B OE1   1 
ATOM   641  O  OE2   . GLU A 1 85  ? 0.064   4.218   -5.676  1.00 33.49 ? 84  GLU B OE2   1 
ATOM   642  N  N     . ASP A 1 86  ? -0.695  8.013   -1.631  1.00 20.29 ? 85  ASP B N     1 
ATOM   643  C  CA    . ASP A 1 86  ? -1.345  7.462   -0.434  1.00 17.79 ? 85  ASP B CA    1 
ATOM   644  C  C     . ASP A 1 86  ? -2.349  6.367   -0.823  1.00 21.73 ? 85  ASP B C     1 
ATOM   645  O  O     . ASP A 1 86  ? -3.309  6.613   -1.562  1.00 22.96 ? 85  ASP B O     1 
ATOM   646  C  CB    . ASP A 1 86  ? -2.075  8.554   0.353   1.00 20.59 ? 85  ASP B CB    1 
ATOM   647  C  CG    . ASP A 1 86  ? -1.142  9.620   0.862   1.00 18.22 ? 85  ASP B CG    1 
ATOM   648  O  OD1   . ASP A 1 86  ? -0.103  9.273   1.477   1.00 19.93 ? 85  ASP B OD1   1 
ATOM   649  O  OD2   . ASP A 1 86  ? -1.489  10.799  0.647   1.00 21.42 ? 85  ASP B OD2   1 
ATOM   650  N  N     . GLU A 1 87  ? -2.146  5.159   -0.266  1.00 21.42 ? 86  GLU B N     1 
ATOM   651  C  CA    . GLU A 1 87  ? -2.927  4.015   -0.717  1.00 20.82 ? 86  GLU B CA    1 
ATOM   652  C  C     . GLU A 1 87  ? -4.347  4.092   -0.187  1.00 23.03 ? 86  GLU B C     1 
ATOM   653  O  O     . GLU A 1 87  ? -5.314  4.024   -0.957  1.00 23.74 ? 86  GLU B O     1 
ATOM   654  C  CB    . GLU A 1 87  ? -2.236  2.711   -0.288  1.00 25.12 ? 86  GLU B CB    1 
ATOM   655  C  CG    . GLU A 1 87  ? -2.907  1.451   -0.810  1.00 26.62 ? 86  GLU B CG    1 
ATOM   656  C  CD    . GLU A 1 87  ? -2.066  0.198   -0.573  1.00 27.08 ? 86  GLU B CD    1 
ATOM   657  O  OE1   . GLU A 1 87  ? -1.068  0.308   0.152   1.00 23.70 ? 86  GLU B OE1   1 
ATOM   658  O  OE2   . GLU A 1 87  ? -2.363  -0.848  -1.212  1.00 27.10 ? 86  GLU B OE2   1 
ATOM   659  N  N     . ASN A 1 88  ? -4.480  4.247   1.130   1.00 22.79 ? 87  ASN B N     1 
ATOM   660  C  CA    . ASN A 1 88  ? -5.763  4.490   1.782   1.00 21.18 ? 87  ASN B CA    1 
ATOM   661  C  C     . ASN A 1 88  ? -5.456  4.891   3.220   1.00 20.67 ? 87  ASN B C     1 
ATOM   662  O  O     . ASN A 1 88  ? -4.321  4.750   3.708   1.00 22.82 ? 87  ASN B O     1 
ATOM   663  C  CB    . ASN A 1 88  ? -6.720  3.284   1.715   1.00 23.25 ? 87  ASN B CB    1 
ATOM   664  C  CG    . ASN A 1 88  ? -6.203  2.091   2.454   1.00 26.16 ? 87  ASN B CG    1 
ATOM   665  O  OD1   . ASN A 1 88  ? -6.043  2.140   3.649   1.00 23.87 ? 87  ASN B OD1   1 
ATOM   666  N  ND2   . ASN A 1 88  ? -6.043  0.966   1.737   1.00 25.61 ? 87  ASN B ND2   1 
ATOM   667  N  N     . PHE A 1 89  ? -6.475  5.404   3.883   1.00 21.85 ? 88  PHE B N     1 
ATOM   668  C  CA    . PHE A 1 89  ? -6.388  5.835   5.280   1.00 23.87 ? 88  PHE B CA    1 
ATOM   669  C  C     . PHE A 1 89  ? -7.401  5.058   6.119   1.00 23.70 ? 88  PHE B C     1 
ATOM   670  O  O     . PHE A 1 89  ? -7.994  5.578   7.045   1.00 25.64 ? 88  PHE B O     1 
ATOM   671  C  CB    . PHE A 1 89  ? -6.615  7.349   5.386   1.00 22.13 ? 88  PHE B CB    1 
ATOM   672  C  CG    . PHE A 1 89  ? -5.596  8.158   4.648   1.00 22.25 ? 88  PHE B CG    1 
ATOM   673  C  CD1   . PHE A 1 89  ? -4.285  8.315   5.136   1.00 21.48 ? 88  PHE B CD1   1 
ATOM   674  C  CD2   . PHE A 1 89  ? -5.952  8.788   3.456   1.00 26.26 ? 88  PHE B CD2   1 
ATOM   675  C  CE1   . PHE A 1 89  ? -3.369  9.090   4.445   1.00 22.03 ? 88  PHE B CE1   1 
ATOM   676  C  CE2   . PHE A 1 89  ? -5.033  9.555   2.775   1.00 25.40 ? 88  PHE B CE2   1 
ATOM   677  C  CZ    . PHE A 1 89  ? -3.750  9.707   3.254   1.00 24.00 ? 88  PHE B CZ    1 
ATOM   678  N  N     . ILE A 1 90  ? -7.621  3.800   5.761   1.00 23.02 ? 89  ILE B N     1 
ATOM   679  C  CA    . ILE A 1 90  ? -8.596  2.977   6.476   1.00 25.43 ? 89  ILE B CA    1 
ATOM   680  C  C     . ILE A 1 90  ? -8.213  2.854   7.946   1.00 25.65 ? 89  ILE B C     1 
ATOM   681  O  O     . ILE A 1 90  ? -9.054  3.038   8.843   1.00 25.95 ? 89  ILE B O     1 
ATOM   682  C  CB    . ILE A 1 90  ? -8.708  1.594   5.818   1.00 24.49 ? 89  ILE B CB    1 
ATOM   683  C  CG1   . ILE A 1 90  ? -9.423  1.718   4.442   1.00 24.88 ? 89  ILE B CG1   1 
ATOM   684  C  CG2   . ILE A 1 90  ? -9.531  0.601   6.722   1.00 27.58 ? 89  ILE B CG2   1 
ATOM   685  C  CD1   . ILE A 1 90  ? -9.297  0.541   3.595   1.00 29.74 ? 89  ILE B CD1   1 
ATOM   686  N  N     . LEU A 1 91  ? -6.969  2.482   8.192   1.00 26.13 ? 90  LEU B N     1 
ATOM   687  C  CA    . LEU A 1 91  ? -6.485  2.213   9.541   1.00 24.35 ? 90  LEU B CA    1 
ATOM   688  C  C     . LEU A 1 91  ? -6.071  3.519   10.228  1.00 25.24 ? 90  LEU B C     1 
ATOM   689  O  O     . LEU A 1 91  ? -5.617  4.485   9.575   1.00 23.49 ? 90  LEU B O     1 
ATOM   690  C  CB    . LEU A 1 91  ? -5.289  1.239   9.518   1.00 23.44 ? 90  LEU B CB    1 
ATOM   691  C  CG    . LEU A 1 91  ? -5.717  -0.094  8.882   1.00 27.61 ? 90  LEU B CG    1 
ATOM   692  C  CD1   . LEU A 1 91  ? -4.556  -1.102  8.814   1.00 26.73 ? 90  LEU B CD1   1 
ATOM   693  C  CD2   . LEU A 1 91  ? -6.831  -0.693  9.681   1.00 28.93 ? 90  LEU B CD2   1 
ATOM   694  N  N     . LYS A 1 92  ? -6.256  3.550   11.560  1.00 26.07 ? 91  LYS B N     1 
ATOM   695  C  CA    . LYS A 1 92  ? -5.990  4.739   12.367  1.00 24.75 ? 91  LYS B CA    1 
ATOM   696  C  C     . LYS A 1 92  ? -4.787  4.576   13.304  1.00 24.25 ? 91  LYS B C     1 
ATOM   697  O  O     . LYS A 1 92  ? -4.334  3.471   13.600  1.00 23.83 ? 91  LYS B O     1 
ATOM   698  C  CB    . LYS A 1 92  ? -7.200  5.095   13.245  1.00 23.67 ? 91  LYS B CB    1 
ATOM   699  C  CG    . LYS A 1 92  ? -8.540  5.140   12.557  1.00 29.26 ? 91  LYS B CG    1 
ATOM   700  C  CD    . LYS A 1 92  ? -8.564  6.076   11.367  1.00 32.88 ? 91  LYS B CD    1 
ATOM   701  C  CE    . LYS A 1 92  ? -10.052 6.120   10.850  1.00 34.06 ? 91  LYS B CE    1 
ATOM   702  N  NZ    . LYS A 1 92  ? -10.138 6.827   9.512   1.00 37.89 ? 91  LYS B NZ    1 
ATOM   703  N  N     . HIS A 1 93  ? -4.307  5.716   13.806  1.00 22.73 ? 92  HIS B N     1 
ATOM   704  C  CA    . HIS A 1 93  ? -3.193  5.733   14.762  1.00 21.46 ? 92  HIS B CA    1 
ATOM   705  C  C     . HIS A 1 93  ? -3.815  5.581   16.150  1.00 25.87 ? 92  HIS B C     1 
ATOM   706  O  O     . HIS A 1 93  ? -4.066  6.551   16.855  1.00 26.68 ? 92  HIS B O     1 
ATOM   707  C  CB    . HIS A 1 93  ? -2.369  7.011   14.646  1.00 21.66 ? 92  HIS B CB    1 
ATOM   708  C  CG    . HIS A 1 93  ? -1.825  7.262   13.262  1.00 21.77 ? 92  HIS B CG    1 
ATOM   709  N  ND1   . HIS A 1 93  ? -2.599  7.812   12.264  1.00 21.79 ? 92  HIS B ND1   1 
ATOM   710  C  CD2   . HIS A 1 93  ? -0.594  7.055   12.720  1.00 22.02 ? 92  HIS B CD2   1 
ATOM   711  C  CE1   . HIS A 1 93  ? -1.863  7.942   11.161  1.00 20.66 ? 92  HIS B CE1   1 
ATOM   712  N  NE2   . HIS A 1 93  ? -0.645  7.490   11.411  1.00 19.77 ? 92  HIS B NE2   1 
ATOM   713  N  N     . THR A 1 94  ? -4.096  4.325   16.537  1.00 25.39 ? 93  THR B N     1 
ATOM   714  C  CA    . THR A 1 94  ? -4.904  4.060   17.735  1.00 24.29 ? 93  THR B CA    1 
ATOM   715  C  C     . THR A 1 94  ? -4.146  4.009   19.058  1.00 24.26 ? 93  THR B C     1 
ATOM   716  O  O     . THR A 1 94  ? -4.792  4.022   20.130  1.00 28.19 ? 93  THR B O     1 
ATOM   717  C  CB    . THR A 1 94  ? -5.648  2.727   17.581  1.00 24.12 ? 93  THR B CB    1 
ATOM   718  O  OG1   . THR A 1 94  ? -4.687  1.748   17.175  1.00 26.75 ? 93  THR B OG1   1 
ATOM   719  C  CG2   . THR A 1 94  ? -6.738  2.883   16.521  1.00 30.98 ? 93  THR B CG2   1 
ATOM   720  N  N     . GLY A 1 95  ? -2.842  3.874   19.020  1.00 23.59 ? 94  GLY B N     1 
ATOM   721  C  CA    . GLY A 1 95  ? -2.082  3.649   20.241  1.00 23.18 ? 94  GLY B CA    1 
ATOM   722  C  C     . GLY A 1 95  ? -0.653  3.246   19.923  1.00 23.62 ? 94  GLY B C     1 
ATOM   723  O  O     . GLY A 1 95  ? -0.185  3.224   18.777  1.00 24.15 ? 94  GLY B O     1 
ATOM   724  N  N     . PRO A 1 96  ? 0.106   2.979   20.983  1.00 19.62 ? 95  PRO B N     1 
ATOM   725  C  CA    . PRO A 1 96  ? 1.500   2.565   20.813  1.00 22.60 ? 95  PRO B CA    1 
ATOM   726  C  C     . PRO A 1 96  ? 1.632   1.320   19.938  1.00 23.81 ? 95  PRO B C     1 
ATOM   727  O  O     . PRO A 1 96  ? 0.788   0.431   19.970  1.00 24.44 ? 95  PRO B O     1 
ATOM   728  C  CB    . PRO A 1 96  ? 1.959   2.262   22.251  1.00 22.96 ? 95  PRO B CB    1 
ATOM   729  C  CG    . PRO A 1 96  ? 0.995   2.894   23.131  1.00 23.28 ? 95  PRO B CG    1 
ATOM   730  C  CD    . PRO A 1 96  ? -0.349  2.963   22.386  1.00 22.19 ? 95  PRO B CD    1 
ATOM   731  N  N     . GLY A 1 97  ? 2.706   1.278   19.150  1.00 21.48 ? 96  GLY B N     1 
ATOM   732  C  CA    . GLY A 1 97  ? 3.030   0.168   18.283  1.00 21.68 ? 96  GLY B CA    1 
ATOM   733  C  C     . GLY A 1 97  ? 2.563   0.331   16.847  1.00 21.30 ? 96  GLY B C     1 
ATOM   734  O  O     . GLY A 1 97  ? 3.032   -0.416  15.975  1.00 20.96 ? 96  GLY B O     1 
ATOM   735  N  N     . ILE A 1 98  ? 1.727   1.330   16.569  1.00 19.71 ? 97  ILE B N     1 
ATOM   736  C  CA    . ILE A 1 98  ? 1.239   1.560   15.182  1.00 18.97 ? 97  ILE B CA    1 
ATOM   737  C  C     . ILE A 1 98  ? 2.424   1.941   14.302  1.00 21.84 ? 97  ILE B C     1 
ATOM   738  O  O     . ILE A 1 98  ? 3.263   2.772   14.673  1.00 19.20 ? 97  ILE B O     1 
ATOM   739  C  CB    . ILE A 1 98  ? 0.122   2.626   15.191  1.00 20.70 ? 97  ILE B CB    1 
ATOM   740  C  CG1   . ILE A 1 98  ? -1.180  2.032   15.785  1.00 25.25 ? 97  ILE B CG1   1 
ATOM   741  C  CG2   . ILE A 1 98  ? -0.042  3.343   13.796  1.00 18.33 ? 97  ILE B CG2   1 
ATOM   742  C  CD1   . ILE A 1 98  ? -1.726  0.834   14.972  1.00 26.94 ? 97  ILE B CD1   1 
ATOM   743  N  N     . LEU A 1 99  ? 2.513   1.306   13.134  1.00 18.84 ? 98  LEU B N     1 
ATOM   744  C  CA    . LEU A 1 99  ? 3.561   1.571   12.160  1.00 19.68 ? 98  LEU B CA    1 
ATOM   745  C  C     . LEU A 1 99  ? 2.943   2.288   10.959  1.00 20.83 ? 98  LEU B C     1 
ATOM   746  O  O     . LEU A 1 99  ? 2.021   1.754   10.298  1.00 18.64 ? 98  LEU B O     1 
ATOM   747  C  CB    . LEU A 1 99  ? 4.205   0.263   11.715  1.00 19.27 ? 98  LEU B CB    1 
ATOM   748  C  CG    . LEU A 1 99  ? 5.230   0.381   10.607  1.00 20.63 ? 98  LEU B CG    1 
ATOM   749  C  CD1   . LEU A 1 99  ? 6.511   1.103   11.098  1.00 18.31 ? 98  LEU B CD1   1 
ATOM   750  C  CD2   . LEU A 1 99  ? 5.495   -1.058  10.237  1.00 19.64 ? 98  LEU B CD2   1 
ATOM   751  N  N     . SER A 1 100 ? 3.485   3.460   10.635  1.00 17.00 ? 99  SER B N     1 
ATOM   752  C  CA    . SER A 1 100 ? 2.799   4.351   9.695   1.00 17.67 ? 99  SER B CA    1 
ATOM   753  C  C     . SER A 1 100 ? 3.800   5.113   8.819   1.00 18.12 ? 99  SER B C     1 
ATOM   754  O  O     . SER A 1 100 ? 5.006   5.263   9.147   1.00 18.43 ? 99  SER B O     1 
ATOM   755  C  CB    . SER A 1 100 ? 1.889   5.314   10.462  1.00 19.78 ? 99  SER B CB    1 
ATOM   756  O  OG    . SER A 1 100 ? 1.222   6.290   9.608   1.00 17.52 ? 99  SER B OG    1 
ATOM   757  N  N     . MET A 1 101 ? 3.345   5.585   7.666   1.00 15.64 ? 100 MET B N     1 
ATOM   758  C  CA    . MET A 1 101 ? 4.304   6.166   6.738   1.00 17.20 ? 100 MET B CA    1 
ATOM   759  C  C     . MET A 1 101 ? 4.559   7.650   7.038   1.00 16.08 ? 100 MET B C     1 
ATOM   760  O  O     . MET A 1 101 ? 3.605   8.419   7.193   1.00 16.22 ? 100 MET B O     1 
ATOM   761  C  CB    . MET A 1 101 ? 3.710   6.053   5.326   1.00 16.87 ? 100 MET B CB    1 
ATOM   762  C  CG    . MET A 1 101 ? 4.018   4.817   4.576   1.00 16.06 ? 100 MET B CG    1 
ATOM   763  S  SD    . MET A 1 101 ? 5.538   3.953   4.773   1.00 20.65 ? 100 MET B SD    1 
ATOM   764  C  CE    . MET A 1 101 ? 6.346   4.521   3.265   1.00 21.15 ? 100 MET B CE    1 
ATOM   765  N  N     . ALA A 1 102 ? 5.821   8.082   7.032   1.00 13.29 ? 101 ALA B N     1 
ATOM   766  C  CA    . ALA A 1 102 ? 6.075   9.510   7.053   1.00 14.83 ? 101 ALA B CA    1 
ATOM   767  C  C     . ALA A 1 102 ? 5.842   10.101  5.654   1.00 16.93 ? 101 ALA B C     1 
ATOM   768  O  O     . ALA A 1 102 ? 5.853   9.395   4.644   1.00 16.16 ? 101 ALA B O     1 
ATOM   769  C  CB    . ALA A 1 102 ? 7.523   9.805   7.555   1.00 15.43 ? 101 ALA B CB    1 
ATOM   770  N  N     . ASN A 1 103 ? 5.640   11.411  5.591   1.00 16.63 ? 102 ASN B N     1 
ATOM   771  C  CA    . ASN A 1 103 ? 5.490   12.042  4.293   1.00 15.95 ? 102 ASN B CA    1 
ATOM   772  C  C     . ASN A 1 103 ? 5.712   13.557  4.401   1.00 20.67 ? 102 ASN B C     1 
ATOM   773  O  O     . ASN A 1 103 ? 5.829   14.127  5.476   1.00 19.23 ? 102 ASN B O     1 
ATOM   774  C  CB    . ASN A 1 103 ? 4.080   11.726  3.702   1.00 16.93 ? 102 ASN B CB    1 
ATOM   775  C  CG    . ASN A 1 103 ? 2.971   12.303  4.499   1.00 19.29 ? 102 ASN B CG    1 
ATOM   776  O  OD1   . ASN A 1 103 ? 2.901   13.528  4.774   1.00 19.83 ? 102 ASN B OD1   1 
ATOM   777  N  ND2   . ASN A 1 103 ? 1.995   11.448  4.798   1.00 17.25 ? 102 ASN B ND2   1 
ATOM   778  N  N     . ALA A 1 104 ? 5.669   14.224  3.269   1.00 20.96 ? 103 ALA B N     1 
ATOM   779  C  CA    . ALA A 1 104 ? 5.805   15.665  3.220   1.00 22.89 ? 103 ALA B CA    1 
ATOM   780  C  C     . ALA A 1 104 ? 4.569   16.259  2.571   1.00 24.11 ? 103 ALA B C     1 
ATOM   781  O  O     . ALA A 1 104 ? 4.647   17.176  1.744   1.00 25.68 ? 103 ALA B O     1 
ATOM   782  C  CB    . ALA A 1 104 ? 7.065   16.068  2.455   1.00 23.68 ? 103 ALA B CB    1 
ATOM   783  N  N     . GLY A 1 105 ? 3.411   15.689  2.884   1.00 23.65 ? 104 GLY B N     1 
ATOM   784  C  CA    . GLY A 1 105 ? 2.168   16.128  2.282   1.00 22.63 ? 104 GLY B CA    1 
ATOM   785  C  C     . GLY A 1 105 ? 1.536   14.987  1.523   1.00 20.84 ? 104 GLY B C     1 
ATOM   786  O  O     . GLY A 1 105 ? 2.066   13.861  1.500   1.00 20.18 ? 104 GLY B O     1 
ATOM   787  N  N     . PRO A 1 106 ? 0.375   15.247  0.931   1.00 23.17 ? 105 PRO B N     1 
ATOM   788  C  CA    . PRO A 1 106 ? -0.328  14.213  0.143   1.00 23.03 ? 105 PRO B CA    1 
ATOM   789  C  C     . PRO A 1 106 ? 0.560   13.531  -0.881  1.00 20.44 ? 105 PRO B C     1 
ATOM   790  O  O     . PRO A 1 106 ? 1.288   14.187  -1.646  1.00 20.06 ? 105 PRO B O     1 
ATOM   791  C  CB    . PRO A 1 106 ? -1.450  14.997  -0.567  1.00 23.62 ? 105 PRO B CB    1 
ATOM   792  C  CG    . PRO A 1 106 ? -1.706  16.204  0.337   1.00 26.37 ? 105 PRO B CG    1 
ATOM   793  C  CD    . PRO A 1 106 ? -0.358  16.529  0.991   1.00 23.59 ? 105 PRO B CD    1 
ATOM   794  N  N     . ASN A 1 107 ? 0.412   12.200  -0.950  1.00 18.04 ? 106 ASN B N     1 
ATOM   795  C  CA    . ASN A 1 107 ? 1.008   11.389  -2.009  1.00 19.92 ? 106 ASN B CA    1 
ATOM   796  C  C     . ASN A 1 107 ? 2.517   11.563  -2.104  1.00 22.12 ? 106 ASN B C     1 
ATOM   797  O  O     . ASN A 1 107 ? 3.050   11.741  -3.200  1.00 21.24 ? 106 ASN B O     1 
ATOM   798  C  CB    . ASN A 1 107 ? 0.341   11.719  -3.356  1.00 18.89 ? 106 ASN B CB    1 
ATOM   799  C  CG    . ASN A 1 107 ? -1.137  11.510  -3.308  1.00 22.54 ? 106 ASN B CG    1 
ATOM   800  O  OD1   . ASN A 1 107 ? -1.572  10.420  -2.848  1.00 20.76 ? 106 ASN B OD1   1 
ATOM   801  N  ND2   . ASN A 1 107 ? -1.934  12.504  -3.805  1.00 22.09 ? 106 ASN B ND2   1 
ATOM   802  N  N     . THR A 1 108 ? 3.212   11.484  -0.954  1.00 18.20 ? 107 THR B N     1 
ATOM   803  C  CA    . THR A 1 108 ? 4.677   11.604  -0.950  1.00 19.24 ? 107 THR B CA    1 
ATOM   804  C  C     . THR A 1 108 ? 5.305   10.544  -0.075  1.00 19.16 ? 107 THR B C     1 
ATOM   805  O  O     . THR A 1 108 ? 6.298   10.788  0.637   1.00 20.52 ? 107 THR B O     1 
ATOM   806  C  CB    . THR A 1 108 ? 5.124   13.010  -0.547  1.00 21.58 ? 107 THR B CB    1 
ATOM   807  O  OG1   . THR A 1 108 ? 4.653   13.298  0.774   1.00 18.92 ? 107 THR B OG1   1 
ATOM   808  C  CG2   . THR A 1 108 ? 4.588   14.082  -1.523  1.00 18.74 ? 107 THR B CG2   1 
ATOM   809  N  N     . ASN A 1 109 ? 4.770   9.337   -0.133  1.00 17.52 ? 108 ASN B N     1 
ATOM   810  C  CA    . ASN A 1 109 ? 5.368   8.232   0.594   1.00 20.86 ? 108 ASN B CA    1 
ATOM   811  C  C     . ASN A 1 109 ? 6.650   7.792   -0.075  1.00 19.53 ? 108 ASN B C     1 
ATOM   812  O  O     . ASN A 1 109 ? 6.683   7.599   -1.274  1.00 20.41 ? 108 ASN B O     1 
ATOM   813  C  CB    . ASN A 1 109 ? 4.401   7.052   0.670   1.00 19.40 ? 108 ASN B CB    1 
ATOM   814  C  CG    . ASN A 1 109 ? 3.139   7.426   1.340   1.00 20.49 ? 108 ASN B CG    1 
ATOM   815  O  OD1   . ASN A 1 109 ? 3.111   7.548   2.597   1.00 17.98 ? 108 ASN B OD1   1 
ATOM   816  N  ND2   . ASN A 1 109 ? 2.068   7.621   0.555   1.00 17.29 ? 108 ASN B ND2   1 
ATOM   817  N  N     . GLY A 1 110 ? 7.690   7.512   0.748   1.00 19.13 ? 109 GLY B N     1 
ATOM   818  C  CA    . GLY A 1 110 ? 8.947   7.045   0.215   1.00 18.81 ? 109 GLY B CA    1 
ATOM   819  C  C     . GLY A 1 110 ? 9.341   5.807   0.966   1.00 19.33 ? 109 GLY B C     1 
ATOM   820  O  O     . GLY A 1 110 ? 8.777   4.731   0.763   1.00 20.96 ? 109 GLY B O     1 
ATOM   821  N  N     . SER A 1 111 ? 10.320  5.945   1.842   1.00 18.70 ? 110 SER B N     1 
ATOM   822  C  CA    . SER A 1 111 ? 10.649  4.863   2.741   1.00 15.73 ? 110 SER B CA    1 
ATOM   823  C  C     . SER A 1 111 ? 10.564  5.254   4.210   1.00 18.35 ? 110 SER B C     1 
ATOM   824  O  O     . SER A 1 111 ? 10.530  4.356   5.069   1.00 18.31 ? 110 SER B O     1 
ATOM   825  C  CB    . SER A 1 111 ? 12.060  4.343   2.450   1.00 20.40 ? 110 SER B CB    1 
ATOM   826  O  OG    . SER A 1 111 ? 12.994  5.435   2.535   1.00 18.54 ? 110 SER B OG    1 
ATOM   827  N  N     . GLN A 1 112 ? 10.584  6.545   4.535   1.00 17.32 ? 111 GLN B N     1 
ATOM   828  C  CA    . GLN A 1 112 ? 10.510  6.904   5.966   1.00 17.95 ? 111 GLN B CA    1 
ATOM   829  C  C     . GLN A 1 112 ? 9.179   6.495   6.562   1.00 18.18 ? 111 GLN B C     1 
ATOM   830  O  O     . GLN A 1 112 ? 8.118   6.552   5.918   1.00 16.16 ? 111 GLN B O     1 
ATOM   831  C  CB    . GLN A 1 112 ? 10.673  8.401   6.168   1.00 17.28 ? 111 GLN B CB    1 
ATOM   832  C  CG    . GLN A 1 112 ? 12.120  8.828   5.866   1.00 18.82 ? 111 GLN B CG    1 
ATOM   833  C  CD    . GLN A 1 112 ? 12.370  10.242  6.267   1.00 19.12 ? 111 GLN B CD    1 
ATOM   834  O  OE1   . GLN A 1 112 ? 11.996  10.662  7.395   1.00 18.15 ? 111 GLN B OE1   1 
ATOM   835  N  NE2   . GLN A 1 112 ? 13.057  10.998  5.384   1.00 17.66 ? 111 GLN B NE2   1 
ATOM   836  N  N     . PHE A 1 113 ? 9.244   6.107   7.833   1.00 17.94 ? 112 PHE B N     1 
ATOM   837  C  CA    . PHE A 1 113 ? 8.146   5.532   8.571   1.00 16.52 ? 112 PHE B CA    1 
ATOM   838  C  C     . PHE A 1 113 ? 8.286   5.943   10.034  1.00 19.65 ? 112 PHE B C     1 
ATOM   839  O  O     . PHE A 1 113 ? 9.352   6.357   10.485  1.00 17.25 ? 112 PHE B O     1 
ATOM   840  C  CB    . PHE A 1 113 ? 8.200   4.017   8.419   1.00 17.18 ? 112 PHE B CB    1 
ATOM   841  C  CG    . PHE A 1 113 ? 9.441   3.436   9.098   1.00 15.55 ? 112 PHE B CG    1 
ATOM   842  C  CD1   . PHE A 1 113 ? 9.465   3.165   10.478  1.00 16.88 ? 112 PHE B CD1   1 
ATOM   843  C  CD2   . PHE A 1 113 ? 10.608  3.292   8.383   1.00 17.03 ? 112 PHE B CD2   1 
ATOM   844  C  CE1   . PHE A 1 113 ? 10.548  2.736   11.098  1.00 16.55 ? 112 PHE B CE1   1 
ATOM   845  C  CE2   . PHE A 1 113 ? 11.745  2.845   9.027   1.00 19.00 ? 112 PHE B CE2   1 
ATOM   846  C  CZ    . PHE A 1 113 ? 11.712  2.578   10.395  1.00 18.07 ? 112 PHE B CZ    1 
ATOM   847  N  N     . PHE A 1 114 ? 7.207   5.814   10.798  1.00 17.83 ? 113 PHE B N     1 
ATOM   848  C  CA    . PHE A 1 114 ? 7.353   6.066   12.227  1.00 15.96 ? 113 PHE B CA    1 
ATOM   849  C  C     . PHE A 1 114 ? 6.587   5.015   13.008  1.00 18.29 ? 113 PHE B C     1 
ATOM   850  O  O     . PHE A 1 114 ? 5.641   4.405   12.517  1.00 16.71 ? 113 PHE B O     1 
ATOM   851  C  CB    . PHE A 1 114 ? 6.929   7.512   12.580  1.00 14.89 ? 113 PHE B CB    1 
ATOM   852  C  CG    . PHE A 1 114 ? 5.443   7.806   12.340  1.00 15.32 ? 113 PHE B CG    1 
ATOM   853  C  CD1   . PHE A 1 114 ? 4.987   8.052   11.016  1.00 15.83 ? 113 PHE B CD1   1 
ATOM   854  C  CD2   . PHE A 1 114 ? 4.530   7.840   13.382  1.00 15.86 ? 113 PHE B CD2   1 
ATOM   855  C  CE1   . PHE A 1 114 ? 3.631   8.312   10.736  1.00 17.04 ? 113 PHE B CE1   1 
ATOM   856  C  CE2   . PHE A 1 114 ? 3.152   8.121   13.142  1.00 17.19 ? 113 PHE B CE2   1 
ATOM   857  C  CZ    . PHE A 1 114 ? 2.668   8.377   11.828  1.00 16.45 ? 113 PHE B CZ    1 
ATOM   858  N  N     . ILE A 1 115 ? 7.004   4.822   14.272  1.00 16.21 ? 114 ILE B N     1 
ATOM   859  C  CA    . ILE A 1 115 ? 6.362   3.885   15.175  1.00 18.02 ? 114 ILE B CA    1 
ATOM   860  C  C     . ILE A 1 115 ? 5.810   4.712   16.306  1.00 16.47 ? 114 ILE B C     1 
ATOM   861  O  O     . ILE A 1 115 ? 6.562   5.470   16.932  1.00 17.53 ? 114 ILE B O     1 
ATOM   862  C  CB    . ILE A 1 115 ? 7.334   2.825   15.713  1.00 20.24 ? 114 ILE B CB    1 
ATOM   863  C  CG1   . ILE A 1 115 ? 8.130   2.178   14.565  1.00 22.84 ? 114 ILE B CG1   1 
ATOM   864  C  CG2   . ILE A 1 115 ? 6.561   1.865   16.653  1.00 19.13 ? 114 ILE B CG2   1 
ATOM   865  C  CD1   . ILE A 1 115 ? 9.369   1.384   15.049  1.00 18.50 ? 114 ILE B CD1   1 
ATOM   866  N  N     . CYS A 1 116 ? 4.487   4.694   16.482  1.00 18.36 ? 115 CYS B N     1 
ATOM   867  C  CA    . CYS A 1 116 ? 3.889   5.452   17.588  1.00 19.24 ? 115 CYS B CA    1 
ATOM   868  C  C     . CYS A 1 116 ? 4.260   4.873   18.950  1.00 19.17 ? 115 CYS B C     1 
ATOM   869  O  O     . CYS A 1 116 ? 4.306   3.651   19.141  1.00 18.94 ? 115 CYS B O     1 
ATOM   870  C  CB    . CYS A 1 116 ? 2.364   5.424   17.517  1.00 18.40 ? 115 CYS B CB    1 
ATOM   871  S  SG    . CYS A 1 116 ? 1.844   6.182   15.912  1.00 21.67 ? 115 CYS B SG    1 
ATOM   872  N  N     . THR A 1 117 ? 4.463   5.769   19.931  1.00 19.10 ? 116 THR B N     1 
ATOM   873  C  CA    . THR A 1 117 ? 4.596   5.351   21.323  1.00 19.51 ? 116 THR B CA    1 
ATOM   874  C  C     . THR A 1 117 ? 3.415   5.863   22.150  1.00 20.44 ? 116 THR B C     1 
ATOM   875  O  O     . THR A 1 117 ? 3.404   5.720   23.382  1.00 22.76 ? 116 THR B O     1 
ATOM   876  C  CB    . THR A 1 117 ? 5.929   5.824   21.907  1.00 20.70 ? 116 THR B CB    1 
ATOM   877  O  OG1   . THR A 1 117 ? 6.017   7.258   21.805  1.00 21.37 ? 116 THR B OG1   1 
ATOM   878  C  CG2   . THR A 1 117 ? 7.061   5.193   21.126  1.00 17.83 ? 116 THR B CG2   1 
ATOM   879  N  N     . ALA A 1 118 ? 2.393   6.393   21.476  1.00 19.68 ? 117 ALA B N     1 
ATOM   880  C  CA    . ALA A 1 118 ? 1.159   6.922   22.048  1.00 21.42 ? 117 ALA B CA    1 
ATOM   881  C  C     . ALA A 1 118 ? 0.137   6.991   20.934  1.00 21.60 ? 117 ALA B C     1 
ATOM   882  O  O     . ALA A 1 118 ? 0.487   6.921   19.756  1.00 23.68 ? 117 ALA B O     1 
ATOM   883  C  CB    . ALA A 1 118 ? 1.330   8.329   22.627  1.00 24.66 ? 117 ALA B CB    1 
ATOM   884  N  N     . LYS A 1 119 ? -1.133  7.154   21.315  1.00 24.08 ? 118 LYS B N     1 
ATOM   885  C  CA    . LYS A 1 119 ? -2.149  7.434   20.301  1.00 22.80 ? 118 LYS B CA    1 
ATOM   886  C  C     . LYS A 1 119 ? -1.884  8.810   19.712  1.00 24.92 ? 118 LYS B C     1 
ATOM   887  O  O     . LYS A 1 119 ? -1.708  9.787   20.439  1.00 25.40 ? 118 LYS B O     1 
ATOM   888  C  CB    . LYS A 1 119 ? -3.540  7.374   20.944  1.00 24.69 ? 118 LYS B CB    1 
ATOM   889  C  CG    . LYS A 1 119 ? -4.732  7.732   20.070  1.00 28.23 ? 118 LYS B CG    1 
ATOM   890  C  CD    . LYS A 1 119 ? -6.011  7.456   20.889  1.00 31.75 ? 118 LYS B CD    1 
ATOM   891  C  CE    . LYS A 1 119 ? -7.291  7.841   20.124  1.00 36.79 ? 118 LYS B CE    1 
ATOM   892  N  NZ    . LYS A 1 119 ? -8.525  7.692   20.973  1.00 40.99 ? 118 LYS B NZ    1 
ATOM   893  N  N     . THR A 1 120 ? -1.876  8.900   18.382  1.00 22.06 ? 119 THR B N     1 
ATOM   894  C  CA    . THR A 1 120 ? -1.645  10.149  17.685  1.00 22.61 ? 119 THR B CA    1 
ATOM   895  C  C     . THR A 1 120 ? -2.791  10.333  16.666  1.00 23.71 ? 119 THR B C     1 
ATOM   896  O  O     . THR A 1 120 ? -2.605  10.259  15.439  1.00 25.26 ? 119 THR B O     1 
ATOM   897  C  CB    . THR A 1 120 ? -0.267  10.149  17.010  1.00 22.29 ? 119 THR B CB    1 
ATOM   898  O  OG1   . THR A 1 120 ? -0.227  9.108   16.036  1.00 21.25 ? 119 THR B OG1   1 
ATOM   899  C  CG2   . THR A 1 120 ? 0.940   9.941   18.051  1.00 23.72 ? 119 THR B CG2   1 
ATOM   900  N  N     . GLU A 1 121 ? -3.969  10.636  17.209  1.00 24.14 ? 120 GLU B N     1 
ATOM   901  C  CA    . GLU A 1 121 ? -5.210  10.624  16.431  1.00 26.62 ? 120 GLU B CA    1 
ATOM   902  C  C     . GLU A 1 121 ? -5.230  11.716  15.376  1.00 27.59 ? 120 GLU B C     1 
ATOM   903  O  O     . GLU A 1 121 ? -5.889  11.549  14.339  1.00 23.43 ? 120 GLU B O     1 
ATOM   904  C  CB    . GLU A 1 121 ? -6.380  10.712  17.419  1.00 28.26 ? 120 GLU B CB    1 
ATOM   905  C  CG    . GLU A 1 121 ? -6.458  12.080  18.102  1.00 32.48 ? 120 GLU B CG    1 
ATOM   906  C  CD    . GLU A 1 121 ? -5.547  12.209  19.372  1.00 38.61 ? 120 GLU B CD    1 
ATOM   907  O  OE1   . GLU A 1 121 ? -4.768  11.258  19.704  1.00 35.57 ? 120 GLU B OE1   1 
ATOM   908  O  OE2   . GLU A 1 121 ? -5.644  13.282  20.066  1.00 46.30 ? 120 GLU B OE2   1 
ATOM   909  N  N     . TRP A 1 122 ? -4.509  12.826  15.608  1.00 23.70 ? 121 TRP B N     1 
ATOM   910  C  CA    . TRP A 1 122 ? -4.574  13.925  14.661  1.00 26.19 ? 121 TRP B CA    1 
ATOM   911  C  C     . TRP A 1 122 ? -3.833  13.614  13.368  1.00 28.40 ? 121 TRP B C     1 
ATOM   912  O  O     . TRP A 1 122 ? -3.975  14.358  12.395  1.00 27.55 ? 121 TRP B O     1 
ATOM   913  C  CB    . TRP A 1 122 ? -4.027  15.202  15.280  1.00 28.82 ? 121 TRP B CB    1 
ATOM   914  C  CG    . TRP A 1 122 ? -2.566  15.103  15.608  1.00 29.86 ? 121 TRP B CG    1 
ATOM   915  C  CD1   . TRP A 1 122 ? -1.523  15.569  14.861  1.00 26.73 ? 121 TRP B CD1   1 
ATOM   916  C  CD2   . TRP A 1 122 ? -1.992  14.506  16.776  1.00 27.78 ? 121 TRP B CD2   1 
ATOM   917  N  NE1   . TRP A 1 122 ? -0.340  15.289  15.491  1.00 28.71 ? 121 TRP B NE1   1 
ATOM   918  C  CE2   . TRP A 1 122 ? -0.585  14.635  16.662  1.00 28.06 ? 121 TRP B CE2   1 
ATOM   919  C  CE3   . TRP A 1 122 ? -2.523  13.894  17.911  1.00 29.04 ? 121 TRP B CE3   1 
ATOM   920  C  CZ2   . TRP A 1 122 ? 0.292   14.179  17.644  1.00 28.71 ? 121 TRP B CZ2   1 
ATOM   921  C  CZ3   . TRP A 1 122 ? -1.652  13.427  18.892  1.00 30.00 ? 121 TRP B CZ3   1 
ATOM   922  C  CH2   . TRP A 1 122 ? -0.258  13.564  18.742  1.00 29.91 ? 121 TRP B CH2   1 
ATOM   923  N  N     . LEU A 1 123 ? -3.052  12.542  13.334  1.00 22.44 ? 122 LEU B N     1 
ATOM   924  C  CA    . LEU A 1 123 ? -2.415  12.064  12.095  1.00 24.09 ? 122 LEU B CA    1 
ATOM   925  C  C     . LEU A 1 123 ? -3.330  11.201  11.244  1.00 21.82 ? 122 LEU B C     1 
ATOM   926  O  O     . LEU A 1 123 ? -2.999  10.943  10.079  1.00 21.25 ? 122 LEU B O     1 
ATOM   927  C  CB    . LEU A 1 123 ? -1.133  11.313  12.474  1.00 22.19 ? 122 LEU B CB    1 
ATOM   928  C  CG    . LEU A 1 123 ? -0.156  12.247  13.206  1.00 22.55 ? 122 LEU B CG    1 
ATOM   929  C  CD1   . LEU A 1 123 ? 1.098   11.420  13.554  1.00 19.55 ? 122 LEU B CD1   1 
ATOM   930  C  CD2   . LEU A 1 123 ? 0.314   13.489  12.396  1.00 24.01 ? 122 LEU B CD2   1 
ATOM   931  N  N     . ASP A 1 124 ? -4.493  10.801  11.757  1.00 23.90 ? 123 ASP B N     1 
ATOM   932  C  CA    . ASP A 1 124 ? -5.407  10.000  10.950  1.00 22.88 ? 123 ASP B CA    1 
ATOM   933  C  C     . ASP A 1 124 ? -5.819  10.747  9.683   1.00 25.27 ? 123 ASP B C     1 
ATOM   934  O  O     . ASP A 1 124 ? -6.129  11.949  9.718   1.00 25.85 ? 123 ASP B O     1 
ATOM   935  C  CB    . ASP A 1 124 ? -6.682  9.648   11.746  1.00 23.54 ? 123 ASP B CB    1 
ATOM   936  C  CG    . ASP A 1 124 ? -6.387  8.747   12.943  1.00 26.29 ? 123 ASP B CG    1 
ATOM   937  O  OD1   . ASP A 1 124 ? -5.268  8.223   13.005  1.00 25.16 ? 123 ASP B OD1   1 
ATOM   938  O  OD2   . ASP A 1 124 ? -7.267  8.533   13.776  1.00 26.37 ? 123 ASP B OD2   1 
ATOM   939  N  N     . GLY A 1 125 ? -5.884  10.016  8.559   1.00 22.63 ? 124 GLY B N     1 
ATOM   940  C  CA    . GLY A 1 125 ? -6.191  10.627  7.279   1.00 24.36 ? 124 GLY B CA    1 
ATOM   941  C  C     . GLY A 1 125 ? -5.053  11.385  6.658   1.00 24.57 ? 124 GLY B C     1 
ATOM   942  O  O     . GLY A 1 125 ? -5.194  11.862  5.516   1.00 25.97 ? 124 GLY B O     1 
ATOM   943  N  N     . LYS A 1 126 ? -3.938  11.489  7.330   1.00 23.65 ? 125 LYS B N     1 
ATOM   944  C  CA    . LYS A 1 126 ? -2.805  12.197  6.752   1.00 20.15 ? 125 LYS B CA    1 
ATOM   945  C  C     . LYS A 1 126 ? -1.599  11.308  6.547   1.00 21.88 ? 125 LYS B C     1 
ATOM   946  O  O     . LYS A 1 126 ? -0.816  11.564  5.644   1.00 21.36 ? 125 LYS B O     1 
ATOM   947  C  CB    . LYS A 1 126 ? -2.452  13.395  7.646   1.00 24.00 ? 125 LYS B CB    1 
ATOM   948  C  CG    . LYS A 1 126 ? -3.456  14.593  7.447   1.00 30.87 ? 125 LYS B CG    1 
ATOM   949  C  CD    . LYS A 1 126 ? -3.872  15.207  8.777   1.00 36.32 ? 125 LYS B CD    1 
ATOM   950  C  CE    . LYS A 1 126 ? -2.649  15.621  9.605   1.00 38.35 ? 125 LYS B CE    1 
ATOM   951  N  NZ    . LYS A 1 126 ? -1.940  16.852  9.062   1.00 43.48 ? 125 LYS B NZ    1 
ATOM   952  N  N     . HIS A 1 127 ? -1.464  10.245  7.336   1.00 15.99 ? 126 HIS B N     1 
ATOM   953  C  CA    . HIS A 1 127 ? -0.376  9.296   7.197   1.00 16.40 ? 126 HIS B CA    1 
ATOM   954  C  C     . HIS A 1 127 ? -1.003  7.949   7.048   1.00 17.31 ? 126 HIS B C     1 
ATOM   955  O  O     . HIS A 1 127 ? -1.974  7.663   7.770   1.00 18.84 ? 126 HIS B O     1 
ATOM   956  C  CB    . HIS A 1 127 ? 0.511   9.329   8.444   1.00 16.44 ? 126 HIS B CB    1 
ATOM   957  C  CG    . HIS A 1 127 ? 1.203   10.663  8.605   1.00 18.65 ? 126 HIS B CG    1 
ATOM   958  N  ND1   . HIS A 1 127 ? 2.478   10.892  8.118   1.00 15.67 ? 126 HIS B ND1   1 
ATOM   959  C  CD2   . HIS A 1 127 ? 0.744   11.868  9.038   1.00 18.54 ? 126 HIS B CD2   1 
ATOM   960  C  CE1   . HIS A 1 127 ? 2.790   12.165  8.269   1.00 16.10 ? 126 HIS B CE1   1 
ATOM   961  N  NE2   . HIS A 1 127 ? 1.768   12.787  8.844   1.00 17.82 ? 126 HIS B NE2   1 
ATOM   962  N  N     . VAL A 1 128 ? -0.439  7.128   6.147   1.00 18.54 ? 127 VAL B N     1 
ATOM   963  C  CA    . VAL A 1 128 ? -0.987  5.790   5.867   1.00 18.54 ? 127 VAL B CA    1 
ATOM   964  C  C     . VAL A 1 128 ? -0.449  4.825   6.926   1.00 16.05 ? 127 VAL B C     1 
ATOM   965  O  O     . VAL A 1 128 ? 0.752   4.555   6.976   1.00 17.68 ? 127 VAL B O     1 
ATOM   966  C  CB    . VAL A 1 128 ? -0.604  5.297   4.456   1.00 18.35 ? 127 VAL B CB    1 
ATOM   967  C  CG1   . VAL A 1 128 ? -1.112  3.877   4.216   1.00 21.49 ? 127 VAL B CG1   1 
ATOM   968  C  CG2   . VAL A 1 128 ? -1.130  6.199   3.395   1.00 17.96 ? 127 VAL B CG2   1 
ATOM   969  N  N     . VAL A 1 129 ? -1.362  4.289   7.743   1.00 16.81 ? 128 VAL B N     1 
ATOM   970  C  CA    . VAL A 1 129 ? -1.045  3.225   8.707   1.00 19.30 ? 128 VAL B CA    1 
ATOM   971  C  C     . VAL A 1 129 ? -1.042  1.904   7.958   1.00 20.37 ? 128 VAL B C     1 
ATOM   972  O  O     . VAL A 1 129 ? -2.008  1.595   7.259   1.00 21.44 ? 128 VAL B O     1 
ATOM   973  C  CB    . VAL A 1 129 ? -2.081  3.206   9.850   1.00 19.08 ? 128 VAL B CB    1 
ATOM   974  C  CG1   . VAL A 1 129 ? -1.862  2.016   10.814  1.00 19.30 ? 128 VAL B CG1   1 
ATOM   975  C  CG2   . VAL A 1 129 ? -2.082  4.531   10.603  1.00 20.58 ? 128 VAL B CG2   1 
ATOM   976  N  N     . PHE A 1 130 ? 0.028   1.092   8.157   1.00 21.51 ? 129 PHE B N     1 
ATOM   977  C  CA    . PHE A 1 130 ? 0.174   -0.153  7.406   1.00 21.46 ? 129 PHE B CA    1 
ATOM   978  C  C     . PHE A 1 130 ? 0.725   -1.305  8.260   1.00 21.82 ? 129 PHE B C     1 
ATOM   979  O  O     . PHE A 1 130 ? 0.965   -2.398  7.719   1.00 22.27 ? 129 PHE B O     1 
ATOM   980  C  CB    . PHE A 1 130 ? 1.074   0.069   6.155   1.00 21.37 ? 129 PHE B CB    1 
ATOM   981  C  CG    . PHE A 1 130 ? 2.520   0.418   6.490   1.00 19.58 ? 129 PHE B CG    1 
ATOM   982  C  CD1   . PHE A 1 130 ? 2.899   1.754   6.768   1.00 18.05 ? 129 PHE B CD1   1 
ATOM   983  C  CD2   . PHE A 1 130 ? 3.480   -0.579  6.579   1.00 19.36 ? 129 PHE B CD2   1 
ATOM   984  C  CE1   . PHE A 1 130 ? 4.240   2.069   7.113   1.00 16.87 ? 129 PHE B CE1   1 
ATOM   985  C  CE2   . PHE A 1 130 ? 4.826   -0.281  6.934   1.00 21.73 ? 129 PHE B CE2   1 
ATOM   986  C  CZ    . PHE A 1 130 ? 5.213   1.051   7.200   1.00 17.95 ? 129 PHE B CZ    1 
ATOM   987  N  N     . GLY A 1 131 ? 0.908   -1.132  9.563   1.00 22.17 ? 130 GLY B N     1 
ATOM   988  C  CA    . GLY A 1 131 ? 1.473   -2.255  10.298  1.00 24.04 ? 130 GLY B CA    1 
ATOM   989  C  C     . GLY A 1 131 ? 1.379   -1.994  11.777  1.00 22.44 ? 130 GLY B C     1 
ATOM   990  O  O     . GLY A 1 131 ? 0.954   -0.920  12.216  1.00 23.74 ? 130 GLY B O     1 
ATOM   991  N  N     . LYS A 1 132 ? 1.857   -2.954  12.557  1.00 23.26 ? 131 LYS B N     1 
ATOM   992  C  CA    . LYS A 1 132 ? 2.009   -2.638  13.979  1.00 22.51 ? 131 LYS B CA    1 
ATOM   993  C  C     . LYS A 1 132 ? 3.078   -3.527  14.567  1.00 25.50 ? 131 LYS B C     1 
ATOM   994  O  O     . LYS A 1 132 ? 3.352   -4.626  14.074  1.00 26.71 ? 131 LYS B O     1 
ATOM   995  C  CB    . LYS A 1 132 ? 0.744   -2.833  14.831  1.00 29.44 ? 131 LYS B CB    1 
ATOM   996  C  CG    . LYS A 1 132 ? 0.044   -4.121  14.627  1.00 33.53 ? 131 LYS B CG    1 
ATOM   997  C  CD    . LYS A 1 132 ? -0.672  -4.514  15.906  1.00 39.06 ? 131 LYS B CD    1 
ATOM   998  C  CE    . LYS A 1 132 ? -1.895  -5.433  15.670  1.00 51.32 ? 131 LYS B CE    1 
ATOM   999  N  NZ    . LYS A 1 132 ? -1.595  -6.850  15.287  1.00 48.82 ? 131 LYS B NZ    1 
ATOM   1000 N  N     . VAL A 1 133 ? 3.648   -3.054  15.669  1.00 24.37 ? 132 VAL B N     1 
ATOM   1001 C  CA    . VAL A 1 133 ? 4.629   -3.882  16.371  1.00 26.32 ? 132 VAL B CA    1 
ATOM   1002 C  C     . VAL A 1 133 ? 3.970   -5.161  16.851  1.00 28.96 ? 132 VAL B C     1 
ATOM   1003 O  O     . VAL A 1 133 ? 2.863   -5.145  17.413  1.00 27.51 ? 132 VAL B O     1 
ATOM   1004 C  CB    . VAL A 1 133 ? 5.266   -3.095  17.528  1.00 23.69 ? 132 VAL B CB    1 
ATOM   1005 C  CG1   . VAL A 1 133 ? 6.013   -4.010  18.517  1.00 26.10 ? 132 VAL B CG1   1 
ATOM   1006 C  CG2   . VAL A 1 133 ? 6.198   -1.948  16.925  1.00 20.31 ? 132 VAL B CG2   1 
ATOM   1007 N  N     . LYS A 1 134 ? 4.675   -6.281  16.642  1.00 29.14 ? 133 LYS B N     1 
ATOM   1008 C  CA    . LYS A 1 134 ? 4.270   -7.615  17.068  1.00 27.78 ? 133 LYS B CA    1 
ATOM   1009 C  C     . LYS A 1 134 ? 5.031   -8.000  18.323  1.00 32.41 ? 133 LYS B C     1 
ATOM   1010 O  O     . LYS A 1 134 ? 4.441   -8.120  19.386  1.00 35.58 ? 133 LYS B O     1 
ATOM   1011 C  CB    . LYS A 1 134 ? 4.507   -8.627  15.924  1.00 35.04 ? 133 LYS B CB    1 
ATOM   1012 C  CG    . LYS A 1 134 ? 3.799   -9.975  16.080  1.00 41.03 ? 133 LYS B CG    1 
ATOM   1013 C  CD    . LYS A 1 134 ? 4.265   -10.990 15.037  1.00 44.63 ? 133 LYS B CD    1 
ATOM   1014 C  CE    . LYS A 1 134 ? 4.009   -12.411 15.517  1.00 48.40 ? 133 LYS B CE    1 
ATOM   1015 N  NZ    . LYS A 1 134 ? 3.819   -12.430 17.014  1.00 54.85 ? 133 LYS B NZ    1 
ATOM   1016 N  N     . GLU A 1 135 ? 6.340   -8.110  18.220  1.00 30.55 ? 134 GLU B N     1 
ATOM   1017 C  CA    . GLU A 1 135 ? 7.171   -8.348  19.386  1.00 35.41 ? 134 GLU B CA    1 
ATOM   1018 C  C     . GLU A 1 135 ? 8.146   -7.199  19.563  1.00 27.95 ? 134 GLU B C     1 
ATOM   1019 O  O     . GLU A 1 135 ? 8.516   -6.501  18.616  1.00 28.11 ? 134 GLU B O     1 
ATOM   1020 C  CB    . GLU A 1 135 ? 7.924   -9.667  19.269  1.00 37.10 ? 134 GLU B CB    1 
ATOM   1021 C  CG    . GLU A 1 135 ? 6.990   -10.829 19.099  1.00 44.98 ? 134 GLU B CG    1 
ATOM   1022 C  CD    . GLU A 1 135 ? 6.907   -11.611 20.356  1.00 52.40 ? 134 GLU B CD    1 
ATOM   1023 O  OE1   . GLU A 1 135 ? 6.104   -11.168 21.224  1.00 58.44 ? 134 GLU B OE1   1 
ATOM   1024 O  OE2   . GLU A 1 135 ? 7.669   -12.605 20.520  1.00 58.00 ? 134 GLU B OE2   1 
ATOM   1025 N  N     . GLY A 1 136 ? 8.554   -6.998  20.807  1.00 29.84 ? 135 GLY B N     1 
ATOM   1026 C  CA    . GLY A 1 136 ? 9.605   -6.041  21.045  1.00 26.64 ? 135 GLY B CA    1 
ATOM   1027 C  C     . GLY A 1 136 ? 9.134   -4.606  21.162  1.00 27.45 ? 135 GLY B C     1 
ATOM   1028 O  O     . GLY A 1 136 ? 9.948   -3.693  20.969  1.00 26.00 ? 135 GLY B O     1 
ATOM   1029 N  N     . MET A 1 137 ? 7.868   -4.363  21.544  1.00 24.25 ? 136 MET B N     1 
ATOM   1030 C  CA    . MET A 1 137 ? 7.531   -2.973  21.860  1.00 25.52 ? 136 MET B CA    1 
ATOM   1031 C  C     . MET A 1 137 ? 8.422   -2.380  22.955  1.00 25.77 ? 136 MET B C     1 
ATOM   1032 O  O     . MET A 1 137 ? 8.705   -1.170  22.898  1.00 25.46 ? 136 MET B O     1 
ATOM   1033 C  CB    . MET A 1 137 ? 6.054   -2.852  22.191  1.00 27.69 ? 136 MET B CB    1 
ATOM   1034 C  CG    . MET A 1 137 ? 5.662   -1.372  22.378  1.00 24.61 ? 136 MET B CG    1 
ATOM   1035 S  SD    . MET A 1 137 ? 5.453   -0.509  20.862  1.00 23.03 ? 136 MET B SD    1 
ATOM   1036 C  CE    . MET A 1 137 ? 5.878   1.150   21.363  1.00 24.18 ? 136 MET B CE    1 
ATOM   1037 N  N     . ASN A 1 138 ? 8.949   -3.205  23.879  1.00 25.49 ? 137 ASN B N     1 
ATOM   1038 C  CA    . ASN A 1 138 ? 9.790   -2.603  24.924  1.00 23.95 ? 137 ASN B CA    1 
ATOM   1039 C  C     . ASN A 1 138 ? 11.112  -2.075  24.323  1.00 23.73 ? 137 ASN B C     1 
ATOM   1040 O  O     . ASN A 1 138 ? 11.728  -1.176  24.893  1.00 24.40 ? 137 ASN B O     1 
ATOM   1041 C  CB    . ASN A 1 138 ? 10.053  -3.553  26.118  1.00 26.60 ? 137 ASN B CB    1 
ATOM   1042 C  CG    . ASN A 1 138 ? 10.455  -4.941  25.725  1.00 27.87 ? 137 ASN B CG    1 
ATOM   1043 O  OD1   . ASN A 1 138 ? 10.782  -5.270  24.550  1.00 30.83 ? 137 ASN B OD1   1 
ATOM   1044 N  ND2   . ASN A 1 138 ? 10.339  -5.817  26.686  1.00 31.23 ? 137 ASN B ND2   1 
ATOM   1045 N  N     . ILE A 1 139 ? 11.512  -2.579  23.162  1.00 23.79 ? 138 ILE B N     1 
ATOM   1046 C  CA    . ILE A 1 139 ? 12.675  -2.032  22.448  1.00 23.53 ? 138 ILE B CA    1 
ATOM   1047 C  C     . ILE A 1 139 ? 12.379  -0.620  21.965  1.00 23.94 ? 138 ILE B C     1 
ATOM   1048 O  O     . ILE A 1 139 ? 13.229  0.285   22.018  1.00 21.91 ? 138 ILE B O     1 
ATOM   1049 C  CB    . ILE A 1 139 ? 13.047  -2.942  21.256  1.00 26.28 ? 138 ILE B CB    1 
ATOM   1050 C  CG1   . ILE A 1 139 ? 13.108  -4.422  21.650  1.00 27.46 ? 138 ILE B CG1   1 
ATOM   1051 C  CG2   . ILE A 1 139 ? 14.293  -2.461  20.599  1.00 26.56 ? 138 ILE B CG2   1 
ATOM   1052 C  CD1   . ILE A 1 139 ? 14.032  -4.680  22.743  1.00 29.36 ? 138 ILE B CD1   1 
ATOM   1053 N  N     . VAL A 1 140 ? 11.180  -0.423  21.422  1.00 19.32 ? 139 VAL B N     1 
ATOM   1054 C  CA    . VAL A 1 140 ? 10.792  0.903   20.962  1.00 18.37 ? 139 VAL B CA    1 
ATOM   1055 C  C     . VAL A 1 140 ? 10.698  1.853   22.148  1.00 20.83 ? 139 VAL B C     1 
ATOM   1056 O  O     . VAL A 1 140 ? 11.092  3.023   22.058  1.00 19.59 ? 139 VAL B O     1 
ATOM   1057 C  CB    . VAL A 1 140 ? 9.431   0.778   20.236  1.00 20.56 ? 139 VAL B CB    1 
ATOM   1058 C  CG1   . VAL A 1 140 ? 9.014   2.145   19.688  1.00 19.51 ? 139 VAL B CG1   1 
ATOM   1059 C  CG2   . VAL A 1 140 ? 9.609   -0.263  19.063  1.00 19.71 ? 139 VAL B CG2   1 
ATOM   1060 N  N     . GLU A 1 141 ? 10.106  1.388   23.246  1.00 20.86 ? 140 GLU B N     1 
ATOM   1061 C  CA    . GLU A 1 141 ? 10.087  2.206   24.465  1.00 20.45 ? 140 GLU B CA    1 
ATOM   1062 C  C     . GLU A 1 141 ? 11.513  2.550   24.895  1.00 21.36 ? 140 GLU B C     1 
ATOM   1063 O  O     . GLU A 1 141 ? 11.801  3.709   25.218  1.00 23.41 ? 140 GLU B O     1 
ATOM   1064 C  CB    . GLU A 1 141 ? 9.334   1.530   25.619  1.00 22.38 ? 140 GLU B CB    1 
ATOM   1065 C  CG    . GLU A 1 141 ? 7.902   1.253   25.290  1.00 25.88 ? 140 GLU B CG    1 
ATOM   1066 C  CD    . GLU A 1 141 ? 7.202   0.246   26.204  1.00 28.74 ? 140 GLU B CD    1 
ATOM   1067 O  OE1   . GLU A 1 141 ? 7.773   -0.331  27.160  1.00 29.39 ? 140 GLU B OE1   1 
ATOM   1068 O  OE2   . GLU A 1 141 ? 6.028   -0.044  25.942  1.00 33.75 ? 140 GLU B OE2   1 
ATOM   1069 N  N     . ALA A 1 142 ? 12.424  1.569   24.868  1.00 19.09 ? 141 ALA B N     1 
ATOM   1070 C  CA    . ALA A 1 142 ? 13.798  1.851   25.270  1.00 23.59 ? 141 ALA B CA    1 
ATOM   1071 C  C     . ALA A 1 142 ? 14.478  2.851   24.338  1.00 24.08 ? 141 ALA B C     1 
ATOM   1072 O  O     . ALA A 1 142 ? 15.348  3.608   24.791  1.00 23.52 ? 141 ALA B O     1 
ATOM   1073 C  CB    . ALA A 1 142 ? 14.609  0.557   25.356  1.00 23.81 ? 141 ALA B CB    1 
ATOM   1074 N  N     . MET A 1 143 ? 14.068  2.899   23.063  1.00 21.27 ? 142 MET B N     1 
ATOM   1075 C  CA    . MET A 1 143 ? 14.647  3.879   22.145  1.00 19.70 ? 142 MET B CA    1 
ATOM   1076 C  C     . MET A 1 143 ? 14.293  5.321   22.529  1.00 23.89 ? 142 MET B C     1 
ATOM   1077 O  O     . MET A 1 143 ? 15.034  6.238   22.205  1.00 21.47 ? 142 MET B O     1 
ATOM   1078 C  CB    . MET A 1 143 ? 14.250  3.575   20.684  1.00 22.59 ? 142 MET B CB    1 
ATOM   1079 C  CG    . MET A 1 143 ? 14.773  2.172   20.193  1.00 22.41 ? 142 MET B CG    1 
ATOM   1080 S  SD    . MET A 1 143 ? 13.958  1.566   18.700  1.00 27.96 ? 142 MET B SD    1 
ATOM   1081 C  CE    . MET A 1 143 ? 13.977  3.064   17.782  1.00 23.72 ? 142 MET B CE    1 
ATOM   1082 N  N     . GLU A 1 144 ? 13.156  5.543   23.177  1.00 24.91 ? 143 GLU B N     1 
ATOM   1083 C  CA    . GLU A 1 144 ? 12.801  6.902   23.619  1.00 24.07 ? 143 GLU B CA    1 
ATOM   1084 C  C     . GLU A 1 144 ? 13.820  7.534   24.551  1.00 26.59 ? 143 GLU B C     1 
ATOM   1085 O  O     . GLU A 1 144 ? 13.874  8.766   24.627  1.00 29.76 ? 143 GLU B O     1 
ATOM   1086 C  CB    . GLU A 1 144 ? 11.421  6.888   24.306  1.00 23.20 ? 143 GLU B CB    1 
ATOM   1087 C  CG    . GLU A 1 144 ? 10.296  6.682   23.308  1.00 24.97 ? 143 GLU B CG    1 
ATOM   1088 C  CD    . GLU A 1 144 ? 8.972   7.007   23.945  1.00 26.04 ? 143 GLU B CD    1 
ATOM   1089 O  OE1   . GLU A 1 144 ? 8.726   6.475   25.019  1.00 26.18 ? 143 GLU B OE1   1 
ATOM   1090 O  OE2   . GLU A 1 144 ? 8.198   7.789   23.405  1.00 25.07 ? 143 GLU B OE2   1 
ATOM   1091 N  N     . ARG A 1 145 ? 14.610  6.738   25.292  1.00 26.14 ? 144 ARG B N     1 
ATOM   1092 C  CA    . ARG A 1 145 ? 15.584  7.289   26.226  1.00 29.16 ? 144 ARG B CA    1 
ATOM   1093 C  C     . ARG A 1 145 ? 16.631  8.113   25.489  1.00 29.38 ? 144 ARG B C     1 
ATOM   1094 O  O     . ARG A 1 145 ? 17.378  8.866   26.125  1.00 30.28 ? 144 ARG B O     1 
ATOM   1095 C  CB    . ARG A 1 145 ? 16.284  6.162   27.021  1.00 34.33 ? 144 ARG B CB    1 
ATOM   1096 C  CG    . ARG A 1 145 ? 15.340  5.002   27.492  1.00 39.71 ? 144 ARG B CG    1 
ATOM   1097 C  CD    . ARG A 1 145 ? 16.121  3.740   28.059  1.00 43.23 ? 144 ARG B CD    1 
ATOM   1098 N  NE    . ARG A 1 145 ? 17.049  2.972   27.193  1.00 34.31 ? 144 ARG B NE    1 
ATOM   1099 C  CZ    . ARG A 1 145 ? 17.535  1.804   27.624  1.00 42.87 ? 144 ARG B CZ    1 
ATOM   1100 N  NH1   . ARG A 1 145 ? 17.097  1.267   28.766  1.00 41.36 ? 144 ARG B NH1   1 
ATOM   1101 N  NH2   . ARG A 1 145 ? 18.531  1.195   26.950  1.00 36.85 ? 144 ARG B NH2   1 
ATOM   1102 N  N     . PHE A 1 146 ? 16.742  7.943   24.167  1.00 25.31 ? 145 PHE B N     1 
ATOM   1103 C  CA    . PHE A 1 146 ? 17.767  8.609   23.390  1.00 27.09 ? 145 PHE B CA    1 
ATOM   1104 C  C     . PHE A 1 146 ? 17.202  9.729   22.513  1.00 25.63 ? 145 PHE B C     1 
ATOM   1105 O  O     . PHE A 1 146 ? 17.946  10.263  21.683  1.00 26.48 ? 145 PHE B O     1 
ATOM   1106 C  CB    . PHE A 1 146 ? 18.495  7.572   22.534  1.00 23.67 ? 145 PHE B CB    1 
ATOM   1107 C  CG    . PHE A 1 146 ? 18.990  6.418   23.331  1.00 29.63 ? 145 PHE B CG    1 
ATOM   1108 C  CD1   . PHE A 1 146 ? 19.993  6.607   24.313  1.00 31.78 ? 145 PHE B CD1   1 
ATOM   1109 C  CD2   . PHE A 1 146 ? 18.422  5.157   23.176  1.00 25.58 ? 145 PHE B CD2   1 
ATOM   1110 C  CE1   . PHE A 1 146 ? 20.483  5.520   25.091  1.00 31.96 ? 145 PHE B CE1   1 
ATOM   1111 C  CE2   . PHE A 1 146 ? 18.890  4.094   23.968  1.00 29.64 ? 145 PHE B CE2   1 
ATOM   1112 C  CZ    . PHE A 1 146 ? 19.925  4.268   24.896  1.00 28.20 ? 145 PHE B CZ    1 
ATOM   1113 N  N     . GLY A 1 147 ? 15.930  10.085  22.701  1.00 25.34 ? 146 GLY B N     1 
ATOM   1114 C  CA    . GLY A 1 147 ? 15.271  11.144  21.949  1.00 22.27 ? 146 GLY B CA    1 
ATOM   1115 C  C     . GLY A 1 147 ? 15.249  12.447  22.751  1.00 24.58 ? 146 GLY B C     1 
ATOM   1116 O  O     . GLY A 1 147 ? 15.907  12.582  23.776  1.00 25.57 ? 146 GLY B O     1 
ATOM   1117 N  N     . SER A 1 148 ? 14.479  13.428  22.246  1.00 19.83 ? 147 SER B N     1 
ATOM   1118 C  CA    . SER A 1 148 ? 14.447  14.770  22.815  1.00 23.80 ? 147 SER B CA    1 
ATOM   1119 C  C     . SER A 1 148 ? 13.179  15.452  22.329  1.00 19.94 ? 147 SER B C     1 
ATOM   1120 O  O     . SER A 1 148 ? 12.479  14.938  21.451  1.00 22.31 ? 147 SER B O     1 
ATOM   1121 C  CB    . SER A 1 148 ? 15.707  15.582  22.417  1.00 23.25 ? 147 SER B CB    1 
ATOM   1122 O  OG    . SER A 1 148 ? 15.746  15.820  20.984  1.00 22.30 ? 147 SER B OG    1 
ATOM   1123 N  N     . ARG A 1 149 ? 12.955  16.657  22.835  1.00 21.01 ? 148 ARG B N     1 
ATOM   1124 C  CA    . ARG A 1 149 ? 11.780  17.445  22.445  1.00 22.97 ? 148 ARG B CA    1 
ATOM   1125 C  C     . ARG A 1 149 ? 11.693  17.700  20.933  1.00 22.48 ? 148 ARG B C     1 
ATOM   1126 O  O     . ARG A 1 149 ? 10.597  17.566  20.343  1.00 21.84 ? 148 ARG B O     1 
ATOM   1127 C  CB    . ARG A 1 149 ? 11.780  18.767  23.221  1.00 28.73 ? 148 ARG B CB    1 
ATOM   1128 C  CG    . ARG A 1 149 ? 10.556  19.637  22.911  1.00 27.66 ? 148 ARG B CG    1 
ATOM   1129 C  CD    . ARG A 1 149 ? 10.489  20.831  23.921  1.00 31.27 ? 148 ARG B CD    1 
ATOM   1130 N  NE    . ARG A 1 149 ? 9.421   21.784  23.591  1.00 33.36 ? 148 ARG B NE    1 
ATOM   1131 C  CZ    . ARG A 1 149 ? 9.536   22.691  22.626  1.00 36.53 ? 148 ARG B CZ    1 
ATOM   1132 N  NH1   . ARG A 1 149 ? 10.669  22.845  21.962  1.00 36.89 ? 148 ARG B NH1   1 
ATOM   1133 N  NH2   . ARG A 1 149 ? 8.510   23.491  22.351  1.00 34.02 ? 148 ARG B NH2   1 
ATOM   1134 N  N     . ASN A 1 150 ? 12.798  18.073  20.269  1.00 23.04 ? 149 ASN B N     1 
ATOM   1135 C  CA    . ASN A 1 150 ? 12.698  18.291  18.818  1.00 20.67 ? 149 ASN B CA    1 
ATOM   1136 C  C     . ASN A 1 150 ? 13.090  17.069  17.994  1.00 19.96 ? 149 ASN B C     1 
ATOM   1137 O  O     . ASN A 1 150 ? 13.119  17.137  16.761  1.00 21.77 ? 149 ASN B O     1 
ATOM   1138 C  CB    . ASN A 1 150 ? 13.506  19.523  18.402  1.00 25.23 ? 149 ASN B CB    1 
ATOM   1139 C  CG    . ASN A 1 150 ? 15.003  19.248  18.338  1.00 24.99 ? 149 ASN B CG    1 
ATOM   1140 O  OD1   . ASN A 1 150 ? 15.458  18.209  18.815  1.00 24.36 ? 149 ASN B OD1   1 
ATOM   1141 N  ND2   . ASN A 1 150 ? 15.768  20.172  17.742  1.00 24.14 ? 149 ASN B ND2   1 
ATOM   1142 N  N     . GLY A 1 151 ? 13.341  15.940  18.635  1.00 18.54 ? 150 GLY B N     1 
ATOM   1143 C  CA    . GLY A 1 151 ? 13.573  14.690  17.960  1.00 17.99 ? 150 GLY B CA    1 
ATOM   1144 C  C     . GLY A 1 151 ? 15.028  14.340  17.787  1.00 18.14 ? 150 GLY B C     1 
ATOM   1145 O  O     . GLY A 1 151 ? 15.335  13.196  17.430  1.00 17.38 ? 150 GLY B O     1 
ATOM   1146 N  N     . LYS A 1 152 ? 15.933  15.302  17.966  1.00 19.53 ? 151 LYS B N     1 
ATOM   1147 C  CA    . LYS A 1 152 ? 17.356  14.990  17.875  1.00 19.81 ? 151 LYS B CA    1 
ATOM   1148 C  C     . LYS A 1 152 ? 17.751  13.871  18.839  1.00 22.99 ? 151 LYS B C     1 
ATOM   1149 O  O     . LYS A 1 152 ? 17.358  13.892  20.014  1.00 23.27 ? 151 LYS B O     1 
ATOM   1150 C  CB    . LYS A 1 152 ? 18.141  16.249  18.156  1.00 19.69 ? 151 LYS B CB    1 
ATOM   1151 C  CG    . LYS A 1 152 ? 17.926  17.285  17.128  1.00 29.24 ? 151 LYS B CG    1 
ATOM   1152 C  CD    . LYS A 1 152 ? 18.835  16.969  15.924  1.00 37.87 ? 151 LYS B CD    1 
ATOM   1153 C  CE    . LYS A 1 152 ? 18.424  17.717  14.648  1.00 39.12 ? 151 LYS B CE    1 
ATOM   1154 N  NZ    . LYS A 1 152 ? 19.668  18.332  14.026  1.00 42.63 ? 151 LYS B NZ    1 
ATOM   1155 N  N     . THR A 1 153 ? 18.536  12.904  18.349  1.00 20.24 ? 152 THR B N     1 
ATOM   1156 C  CA    . THR A 1 153 ? 18.919  11.771  19.189  1.00 20.81 ? 152 THR B CA    1 
ATOM   1157 C  C     . THR A 1 153 ? 20.280  12.018  19.839  1.00 24.96 ? 152 THR B C     1 
ATOM   1158 O  O     . THR A 1 153 ? 21.151  12.708  19.283  1.00 27.06 ? 152 THR B O     1 
ATOM   1159 C  CB    . THR A 1 153 ? 18.909  10.447  18.370  1.00 22.32 ? 152 THR B CB    1 
ATOM   1160 O  OG1   . THR A 1 153 ? 19.880  10.449  17.303  1.00 23.51 ? 152 THR B OG1   1 
ATOM   1161 C  CG2   . THR A 1 153 ? 17.535  10.224  17.712  1.00 20.54 ? 152 THR B CG2   1 
ATOM   1162 N  N     . SER A 1 154 ? 20.453  11.465  21.041  1.00 22.67 ? 153 SER B N     1 
ATOM   1163 C  CA    . SER A 1 154 ? 21.731  11.617  21.749  1.00 27.24 ? 153 SER B CA    1 
ATOM   1164 C  C     . SER A 1 154 ? 22.695  10.468  21.517  1.00 27.20 ? 153 SER B C     1 
ATOM   1165 O  O     . SER A 1 154 ? 23.885  10.587  21.887  1.00 27.31 ? 153 SER B O     1 
ATOM   1166 C  CB    . SER A 1 154 ? 21.515  11.757  23.260  1.00 28.45 ? 153 SER B CB    1 
ATOM   1167 O  OG    . SER A 1 154 ? 20.746  10.664  23.735  1.00 26.29 ? 153 SER B OG    1 
ATOM   1168 N  N     . LYS A 1 155 ? 22.230  9.385   20.913  1.00 26.42 ? 154 LYS B N     1 
ATOM   1169 C  CA    . LYS A 1 155 ? 23.069  8.292   20.445  1.00 30.54 ? 154 LYS B CA    1 
ATOM   1170 C  C     . LYS A 1 155 ? 22.614  7.900   19.041  1.00 26.86 ? 154 LYS B C     1 
ATOM   1171 O  O     . LYS A 1 155 ? 21.498  8.221   18.619  1.00 26.16 ? 154 LYS B O     1 
ATOM   1172 C  CB    . LYS A 1 155 ? 22.995  7.076   21.416  1.00 29.30 ? 154 LYS B CB    1 
ATOM   1173 C  CG    . LYS A 1 155 ? 23.633  7.383   22.822  1.00 32.99 ? 154 LYS B CG    1 
ATOM   1174 C  CD    . LYS A 1 155 ? 23.646  6.191   23.778  1.00 34.55 ? 154 LYS B CD    1 
ATOM   1175 C  CE    . LYS A 1 155 ? 24.102  6.579   25.172  1.00 38.31 ? 154 LYS B CE    1 
ATOM   1176 N  NZ    . LYS A 1 155 ? 25.455  7.249   25.128  1.00 41.84 ? 154 LYS B NZ    1 
ATOM   1177 N  N     . LYS A 1 156 ? 23.489  7.193   18.324  1.00 27.02 ? 155 LYS B N     1 
ATOM   1178 C  CA    . LYS A 1 156 ? 23.191  6.694   16.989  1.00 27.42 ? 155 LYS B CA    1 
ATOM   1179 C  C     . LYS A 1 156 ? 22.370  5.426   17.096  1.00 28.03 ? 155 LYS B C     1 
ATOM   1180 O  O     . LYS A 1 156 ? 22.887  4.380   17.505  1.00 26.12 ? 155 LYS B O     1 
ATOM   1181 C  CB    . LYS A 1 156 ? 24.481  6.402   16.246  1.00 31.45 ? 155 LYS B CB    1 
ATOM   1182 C  CG    . LYS A 1 156 ? 24.969  7.569   15.416  1.00 41.85 ? 155 LYS B CG    1 
ATOM   1183 C  CD    . LYS A 1 156 ? 25.824  7.118   14.213  1.00 47.73 ? 155 LYS B CD    1 
ATOM   1184 C  CE    . LYS A 1 156 ? 25.445  5.696   13.703  1.00 43.15 ? 155 LYS B CE    1 
ATOM   1185 N  NZ    . LYS A 1 156 ? 25.965  5.409   12.303  1.00 47.46 ? 155 LYS B NZ    1 
ATOM   1186 N  N     . ILE A 1 157 ? 21.101  5.492   16.713  1.00 22.19 ? 156 ILE B N     1 
ATOM   1187 C  CA    . ILE A 1 157 ? 20.202  4.358   16.844  1.00 23.72 ? 156 ILE B CA    1 
ATOM   1188 C  C     . ILE A 1 157 ? 20.069  3.750   15.469  1.00 23.18 ? 156 ILE B C     1 
ATOM   1189 O  O     . ILE A 1 157 ? 19.431  4.359   14.595  1.00 24.23 ? 156 ILE B O     1 
ATOM   1190 C  CB    . ILE A 1 157 ? 18.825  4.778   17.369  1.00 22.49 ? 156 ILE B CB    1 
ATOM   1191 C  CG1   . ILE A 1 157 ? 18.912  5.682   18.648  1.00 22.78 ? 156 ILE B CG1   1 
ATOM   1192 C  CG2   . ILE A 1 157 ? 17.926  3.497   17.514  1.00 24.08 ? 156 ILE B CG2   1 
ATOM   1193 C  CD1   . ILE A 1 157 ? 19.841  5.126   19.763  1.00 25.59 ? 156 ILE B CD1   1 
ATOM   1194 N  N     . THR A 1 158 ? 20.575  2.538   15.264  1.00 21.57 ? 157 THR B N     1 
ATOM   1195 C  CA    . THR A 1 158 ? 20.601  1.930   13.932  1.00 22.24 ? 157 THR B CA    1 
ATOM   1196 C  C     . THR A 1 158 ? 19.762  0.674   13.812  1.00 27.25 ? 157 THR B C     1 
ATOM   1197 O  O     . THR A 1 158 ? 19.543  -0.065  14.776  1.00 26.28 ? 157 THR B O     1 
ATOM   1198 C  CB    . THR A 1 158 ? 22.032  1.568   13.500  1.00 25.62 ? 157 THR B CB    1 
ATOM   1199 O  OG1   . THR A 1 158 ? 22.607  0.678   14.460  1.00 28.61 ? 157 THR B OG1   1 
ATOM   1200 C  CG2   . THR A 1 158 ? 22.854  2.835   13.365  1.00 28.59 ? 157 THR B CG2   1 
ATOM   1201 N  N     . ILE A 1 159 ? 19.321  0.423   12.575  1.00 23.99 ? 158 ILE B N     1 
ATOM   1202 C  CA    . ILE A 1 159 ? 18.847  -0.895  12.194  1.00 23.60 ? 158 ILE B CA    1 
ATOM   1203 C  C     . ILE A 1 159 ? 20.095  -1.686  11.797  1.00 26.83 ? 158 ILE B C     1 
ATOM   1204 O  O     . ILE A 1 159 ? 20.579  -1.634  10.665  1.00 27.36 ? 158 ILE B O     1 
ATOM   1205 C  CB    . ILE A 1 159 ? 17.800  -0.798  11.093  1.00 23.45 ? 158 ILE B CB    1 
ATOM   1206 C  CG1   . ILE A 1 159 ? 16.658  0.123   11.585  1.00 19.01 ? 158 ILE B CG1   1 
ATOM   1207 C  CG2   . ILE A 1 159 ? 17.197  -2.141  10.767  1.00 24.25 ? 158 ILE B CG2   1 
ATOM   1208 C  CD1   . ILE A 1 159 ? 15.769  0.510   10.355  1.00 19.50 ? 158 ILE B CD1   1 
ATOM   1209 N  N     . ALA A 1 160 ? 20.636  -2.437  12.742  1.00 26.67 ? 159 ALA B N     1 
ATOM   1210 C  CA    . ALA A 1 160 ? 21.861  -3.145  12.479  1.00 26.54 ? 159 ALA B CA    1 
ATOM   1211 C  C     . ALA A 1 160 ? 21.618  -4.325  11.548  1.00 32.08 ? 159 ALA B C     1 
ATOM   1212 O  O     . ALA A 1 160 ? 22.531  -4.752  10.829  1.00 31.40 ? 159 ALA B O     1 
ATOM   1213 C  CB    . ALA A 1 160 ? 22.485  -3.583  13.829  1.00 28.85 ? 159 ALA B CB    1 
ATOM   1214 N  N     . ASP A 1 161 ? 20.403  -4.870  11.558  1.00 30.34 ? 160 ASP B N     1 
ATOM   1215 C  CA    . ASP A 1 161 ? 20.040  -5.941  10.644  1.00 32.70 ? 160 ASP B CA    1 
ATOM   1216 C  C     . ASP A 1 161 ? 18.522  -5.947  10.544  1.00 30.16 ? 160 ASP B C     1 
ATOM   1217 O  O     . ASP A 1 161 ? 17.828  -5.424  11.410  1.00 27.70 ? 160 ASP B O     1 
ATOM   1218 C  CB    . ASP A 1 161 ? 20.578  -7.305  11.107  1.00 32.89 ? 160 ASP B CB    1 
ATOM   1219 C  CG    . ASP A 1 161 ? 20.565  -8.350  9.989   1.00 35.40 ? 160 ASP B CG    1 
ATOM   1220 O  OD1   . ASP A 1 161 ? 20.424  -7.973  8.784   1.00 32.97 ? 160 ASP B OD1   1 
ATOM   1221 O  OD2   . ASP A 1 161 ? 20.703  -9.547  10.330  1.00 37.80 ? 160 ASP B OD2   1 
ATOM   1222 N  N     . CYS A 1 162 ? 18.018  -6.482  9.443   1.00 31.02 ? 161 CYS B N     1 
ATOM   1223 C  CA    . CYS A 1 162 ? 16.577  -6.529  9.238   1.00 29.98 ? 161 CYS B CA    1 
ATOM   1224 C  C     . CYS A 1 162 ? 16.287  -7.564  8.168   1.00 30.34 ? 161 CYS B C     1 
ATOM   1225 O  O     . CYS A 1 162 ? 17.169  -7.955  7.395   1.00 34.57 ? 161 CYS B O     1 
ATOM   1226 C  CB    . CYS A 1 162 ? 15.978  -5.154  8.863   1.00 27.90 ? 161 CYS B CB    1 
ATOM   1227 S  SG    . CYS A 1 162 ? 16.829  -4.226  7.528   1.00 27.34 ? 161 CYS B SG    1 
ATOM   1228 N  N     . GLY A 1 163 ? 15.050  -8.028  8.146   1.00 31.89 ? 162 GLY B N     1 
ATOM   1229 C  CA    . GLY A 1 163 ? 14.691  -9.070  7.198   1.00 32.33 ? 162 GLY B CA    1 
ATOM   1230 C  C     . GLY A 1 163 ? 13.254  -9.484  7.417   1.00 35.30 ? 162 GLY B C     1 
ATOM   1231 O  O     . GLY A 1 163 ? 12.524  -8.894  8.219   1.00 32.55 ? 162 GLY B O     1 
ATOM   1232 N  N     . GLN A 1 164 ? 12.849  -10.495 6.670   1.00 33.07 ? 163 GLN B N     1 
ATOM   1233 C  CA    . GLN A 1 164 ? 11.520  -11.058 6.810   1.00 35.93 ? 163 GLN B CA    1 
ATOM   1234 C  C     . GLN A 1 164 ? 11.585  -12.339 7.644   1.00 41.14 ? 163 GLN B C     1 
ATOM   1235 O  O     . GLN A 1 164 ? 12.543  -13.118 7.542   1.00 40.31 ? 163 GLN B O     1 
ATOM   1236 C  CB    . GLN A 1 164 ? 10.923  -11.335 5.427   1.00 39.04 ? 163 GLN B CB    1 
ATOM   1237 C  CG    . GLN A 1 164 ? 9.477   -11.787 5.433   1.00 39.63 ? 163 GLN B CG    1 
ATOM   1238 C  CD    . GLN A 1 164 ? 8.878   -11.836 4.039   1.00 39.46 ? 163 GLN B CD    1 
ATOM   1239 O  OE1   . GLN A 1 164 ? 9.552   -11.541 3.054   1.00 41.01 ? 163 GLN B OE1   1 
ATOM   1240 N  NE2   . GLN A 1 164 ? 7.608   -12.226 3.945   1.00 40.05 ? 163 GLN B NE2   1 
ATOM   1241 N  N     . LEU A 1 165 ? 10.575  -12.538 8.484   1.00 37.27 ? 164 LEU B N     1 
ATOM   1242 C  CA    . LEU A 1 165 ? 10.508  -13.718 9.334   1.00 40.91 ? 164 LEU B CA    1 
ATOM   1243 C  C     . LEU A 1 165 ? 9.674   -14.789 8.615   1.00 45.41 ? 164 LEU B C     1 
ATOM   1244 O  O     . LEU A 1 165 ? 8.852   -14.434 7.765   1.00 41.11 ? 164 LEU B O     1 
ATOM   1245 C  CB    . LEU A 1 165 ? 9.912   -13.357 10.694  1.00 38.13 ? 164 LEU B CB    1 
ATOM   1246 C  CG    . LEU A 1 165 ? 10.793  -12.549 11.651  1.00 40.70 ? 164 LEU B CG    1 
ATOM   1247 C  CD1   . LEU A 1 165 ? 10.041  -12.204 12.924  1.00 41.74 ? 164 LEU B CD1   1 
ATOM   1248 C  CD2   . LEU A 1 165 ? 12.092  -13.295 12.040  1.00 37.48 ? 164 LEU B CD2   1 
ATOM   1249 N  N     . VAL B 1 3   ? 61.453  33.590  26.364  1.00 39.69 ? 2   VAL D N     1 
ATOM   1250 C  CA    . VAL B 1 3   ? 60.755  34.041  25.151  1.00 40.71 ? 2   VAL D CA    1 
ATOM   1251 C  C     . VAL B 1 3   ? 59.472  33.249  25.051  1.00 34.39 ? 2   VAL D C     1 
ATOM   1252 O  O     . VAL B 1 3   ? 59.446  32.040  25.258  1.00 35.44 ? 2   VAL D O     1 
ATOM   1253 C  CB    . VAL B 1 3   ? 61.558  33.882  23.841  1.00 47.61 ? 2   VAL D CB    1 
ATOM   1254 C  CG1   . VAL B 1 3   ? 61.400  32.476  23.223  1.00 42.01 ? 2   VAL D CG1   1 
ATOM   1255 C  CG2   . VAL B 1 3   ? 61.147  34.952  22.821  1.00 47.64 ? 2   VAL D CG2   1 
ATOM   1256 N  N     . ASN B 1 4   ? 58.424  33.941  24.701  1.00 32.62 ? 3   ASN D N     1 
ATOM   1257 C  CA    . ASN B 1 4   ? 57.121  33.302  24.557  1.00 33.73 ? 3   ASN D CA    1 
ATOM   1258 C  C     . ASN B 1 4   ? 57.065  32.442  23.297  1.00 37.07 ? 3   ASN D C     1 
ATOM   1259 O  O     . ASN B 1 4   ? 57.194  32.972  22.185  1.00 38.35 ? 3   ASN D O     1 
ATOM   1260 C  CB    . ASN B 1 4   ? 56.059  34.361  24.513  1.00 30.12 ? 3   ASN D CB    1 
ATOM   1261 C  CG    . ASN B 1 4   ? 55.814  34.974  25.867  1.00 35.20 ? 3   ASN D CG    1 
ATOM   1262 O  OD1   . ASN B 1 4   ? 56.346  34.502  26.897  1.00 34.66 ? 3   ASN D OD1   1 
ATOM   1263 N  ND2   . ASN B 1 4   ? 55.045  36.054  25.884  1.00 35.76 ? 3   ASN D ND2   1 
ATOM   1264 N  N     . PRO B 1 5   ? 56.874  31.140  23.413  1.00 35.48 ? 4   PRO D N     1 
ATOM   1265 C  CA    . PRO B 1 5   ? 56.829  30.291  22.213  1.00 37.13 ? 4   PRO D CA    1 
ATOM   1266 C  C     . PRO B 1 5   ? 55.473  30.409  21.525  1.00 34.93 ? 4   PRO D C     1 
ATOM   1267 O  O     . PRO B 1 5   ? 54.513  30.934  22.086  1.00 30.26 ? 4   PRO D O     1 
ATOM   1268 C  CB    . PRO B 1 5   ? 57.059  28.884  22.777  1.00 32.46 ? 4   PRO D CB    1 
ATOM   1269 C  CG    . PRO B 1 5   ? 56.373  28.959  24.132  1.00 33.72 ? 4   PRO D CG    1 
ATOM   1270 C  CD    . PRO B 1 5   ? 56.619  30.372  24.642  1.00 32.52 ? 4   PRO D CD    1 
ATOM   1271 N  N     . THR B 1 6   ? 55.410  29.917  20.279  1.00 33.49 ? 5   THR D N     1 
ATOM   1272 C  CA    . THR B 1 6   ? 54.174  29.899  19.503  1.00 31.30 ? 5   THR D CA    1 
ATOM   1273 C  C     . THR B 1 6   ? 53.851  28.480  19.078  1.00 33.93 ? 5   THR D C     1 
ATOM   1274 O  O     . THR B 1 6   ? 54.721  27.764  18.580  1.00 31.35 ? 5   THR D O     1 
ATOM   1275 C  CB    . THR B 1 6   ? 54.258  30.774  18.253  1.00 36.50 ? 5   THR D CB    1 
ATOM   1276 O  OG1   . THR B 1 6   ? 54.525  32.124  18.637  1.00 38.64 ? 5   THR D OG1   1 
ATOM   1277 C  CG2   . THR B 1 6   ? 52.935  30.718  17.473  1.00 34.83 ? 5   THR D CG2   1 
ATOM   1278 N  N     . VAL B 1 7   ? 52.584  28.091  19.237  1.00 31.64 ? 6   VAL D N     1 
ATOM   1279 C  CA    . VAL B 1 7   ? 52.121  26.778  18.811  1.00 30.04 ? 6   VAL D CA    1 
ATOM   1280 C  C     . VAL B 1 7   ? 50.932  26.968  17.872  1.00 30.47 ? 6   VAL D C     1 
ATOM   1281 O  O     . VAL B 1 7   ? 50.364  28.056  17.776  1.00 28.89 ? 6   VAL D O     1 
ATOM   1282 C  CB    . VAL B 1 7   ? 51.762  25.877  20.007  1.00 33.81 ? 6   VAL D CB    1 
ATOM   1283 C  CG1   . VAL B 1 7   ? 52.965  25.708  20.910  1.00 33.27 ? 6   VAL D CG1   1 
ATOM   1284 C  CG2   . VAL B 1 7   ? 50.617  26.489  20.812  1.00 30.53 ? 6   VAL D CG2   1 
ATOM   1285 N  N     . PHE B 1 8   ? 50.591  25.902  17.137  1.00 28.43 ? 7   PHE D N     1 
ATOM   1286 C  CA    . PHE B 1 8   ? 49.470  25.955  16.185  1.00 27.80 ? 7   PHE D CA    1 
ATOM   1287 C  C     . PHE B 1 8   ? 48.612  24.701  16.297  1.00 28.72 ? 7   PHE D C     1 
ATOM   1288 O  O     . PHE B 1 8   ? 49.095  23.625  16.670  1.00 29.82 ? 7   PHE D O     1 
ATOM   1289 C  CB    . PHE B 1 8   ? 49.959  26.074  14.748  1.00 30.10 ? 7   PHE D CB    1 
ATOM   1290 C  CG    . PHE B 1 8   ? 50.540  24.769  14.206  1.00 31.06 ? 7   PHE D CG    1 
ATOM   1291 C  CD1   . PHE B 1 8   ? 49.724  23.807  13.593  1.00 32.01 ? 7   PHE D CD1   1 
ATOM   1292 C  CD2   . PHE B 1 8   ? 51.896  24.479  14.370  1.00 32.76 ? 7   PHE D CD2   1 
ATOM   1293 C  CE1   . PHE B 1 8   ? 50.280  22.588  13.130  1.00 34.29 ? 7   PHE D CE1   1 
ATOM   1294 C  CE2   . PHE B 1 8   ? 52.445  23.291  13.914  1.00 32.88 ? 7   PHE D CE2   1 
ATOM   1295 C  CZ    . PHE B 1 8   ? 51.637  22.334  13.301  1.00 34.03 ? 7   PHE D CZ    1 
ATOM   1296 N  N     . PHE B 1 9   ? 47.319  24.876  15.992  1.00 25.26 ? 8   PHE D N     1 
ATOM   1297 C  CA    . PHE B 1 9   ? 46.356  23.796  15.808  1.00 25.95 ? 8   PHE D CA    1 
ATOM   1298 C  C     . PHE B 1 9   ? 45.897  23.889  14.366  1.00 28.34 ? 8   PHE D C     1 
ATOM   1299 O  O     . PHE B 1 9   ? 45.506  24.978  13.931  1.00 25.83 ? 8   PHE D O     1 
ATOM   1300 C  CB    . PHE B 1 9   ? 45.088  23.957  16.669  1.00 24.33 ? 8   PHE D CB    1 
ATOM   1301 C  CG    . PHE B 1 9   ? 45.259  23.804  18.184  1.00 26.02 ? 8   PHE D CG    1 
ATOM   1302 C  CD1   . PHE B 1 9   ? 46.431  23.315  18.778  1.00 22.85 ? 8   PHE D CD1   1 
ATOM   1303 C  CD2   . PHE B 1 9   ? 44.148  24.067  18.997  1.00 27.13 ? 8   PHE D CD2   1 
ATOM   1304 C  CE1   . PHE B 1 9   ? 46.523  23.189  20.178  1.00 27.84 ? 8   PHE D CE1   1 
ATOM   1305 C  CE2   . PHE B 1 9   ? 44.212  23.939  20.379  1.00 23.76 ? 8   PHE D CE2   1 
ATOM   1306 C  CZ    . PHE B 1 9   ? 45.405  23.476  20.966  1.00 26.35 ? 8   PHE D CZ    1 
ATOM   1307 N  N     . ASP B 1 10  ? 45.927  22.775  13.632  1.00 27.59 ? 9   ASP D N     1 
ATOM   1308 C  CA    . ASP B 1 10  ? 45.172  22.691  12.378  1.00 28.70 ? 9   ASP D CA    1 
ATOM   1309 C  C     . ASP B 1 10  ? 43.824  22.052  12.676  1.00 27.80 ? 9   ASP D C     1 
ATOM   1310 O  O     . ASP B 1 10  ? 43.768  20.907  13.139  1.00 30.32 ? 9   ASP D O     1 
ATOM   1311 C  CB    . ASP B 1 10  ? 45.927  21.891  11.336  1.00 29.77 ? 9   ASP D CB    1 
ATOM   1312 C  CG    . ASP B 1 10  ? 47.128  22.647  10.785  1.00 35.19 ? 9   ASP D CG    1 
ATOM   1313 O  OD1   . ASP B 1 10  ? 47.051  23.884  10.616  1.00 35.97 ? 9   ASP D OD1   1 
ATOM   1314 O  OD2   . ASP B 1 10  ? 48.147  21.992  10.519  1.00 35.63 ? 9   ASP D OD2   1 
ATOM   1315 N  N     . ILE B 1 11  ? 42.752  22.809  12.450  1.00 25.89 ? 10  ILE D N     1 
ATOM   1316 C  CA    . ILE B 1 11  ? 41.393  22.443  12.845  1.00 24.60 ? 10  ILE D CA    1 
ATOM   1317 C  C     . ILE B 1 11  ? 40.708  21.773  11.671  1.00 29.21 ? 10  ILE D C     1 
ATOM   1318 O  O     . ILE B 1 11  ? 40.808  22.278  10.554  1.00 28.59 ? 10  ILE D O     1 
ATOM   1319 C  CB    . ILE B 1 11  ? 40.613  23.703  13.241  1.00 26.47 ? 10  ILE D CB    1 
ATOM   1320 C  CG1   . ILE B 1 11  ? 41.344  24.469  14.366  1.00 24.14 ? 10  ILE D CG1   1 
ATOM   1321 C  CG2   . ILE B 1 11  ? 39.175  23.331  13.609  1.00 27.93 ? 10  ILE D CG2   1 
ATOM   1322 C  CD1   . ILE B 1 11  ? 41.382  23.672  15.650  1.00 24.70 ? 10  ILE D CD1   1 
ATOM   1323 N  N     . ALA B 1 12  ? 39.961  20.683  11.924  1.00 27.92 ? 11  ALA D N     1 
ATOM   1324 C  CA    . ALA B 1 12  ? 39.151  20.043  10.888  1.00 28.35 ? 11  ALA D CA    1 
ATOM   1325 C  C     . ALA B 1 12  ? 37.694  19.977  11.336  1.00 31.27 ? 11  ALA D C     1 
ATOM   1326 O  O     . ALA B 1 12  ? 37.409  19.932  12.540  1.00 27.28 ? 11  ALA D O     1 
ATOM   1327 C  CB    . ALA B 1 12  ? 39.642  18.625  10.572  1.00 31.51 ? 11  ALA D CB    1 
ATOM   1328 N  N     . VAL B 1 13  ? 36.777  19.931  10.356  1.00 29.63 ? 12  VAL D N     1 
ATOM   1329 C  CA    . VAL B 1 13  ? 35.331  19.849  10.582  1.00 31.04 ? 12  VAL D CA    1 
ATOM   1330 C  C     . VAL B 1 13  ? 34.856  18.603  9.854   1.00 33.40 ? 12  VAL D C     1 
ATOM   1331 O  O     . VAL B 1 13  ? 34.917  18.542  8.610   1.00 30.23 ? 12  VAL D O     1 
ATOM   1332 C  CB    . VAL B 1 13  ? 34.576  21.094  10.074  1.00 27.54 ? 12  VAL D CB    1 
ATOM   1333 C  CG1   . VAL B 1 13  ? 33.054  20.910  10.206  1.00 30.46 ? 12  VAL D CG1   1 
ATOM   1334 C  CG2   . VAL B 1 13  ? 35.055  22.349  10.762  1.00 28.33 ? 12  VAL D CG2   1 
ATOM   1335 N  N     . ASP B 1 14  ? 34.442  17.595  10.634  1.00 29.38 ? 13  ASP D N     1 
ATOM   1336 C  CA    . ASP B 1 14  ? 34.083  16.268  10.129  1.00 33.73 ? 13  ASP D CA    1 
ATOM   1337 C  C     . ASP B 1 14  ? 35.163  15.740  9.193   1.00 39.94 ? 13  ASP D C     1 
ATOM   1338 O  O     . ASP B 1 14  ? 34.877  15.108  8.169   1.00 40.59 ? 13  ASP D O     1 
ATOM   1339 C  CB    . ASP B 1 14  ? 32.712  16.263  9.446   1.00 37.15 ? 13  ASP D CB    1 
ATOM   1340 C  CG    . ASP B 1 14  ? 31.563  16.299  10.451  1.00 34.57 ? 13  ASP D CG    1 
ATOM   1341 O  OD1   . ASP B 1 14  ? 31.801  15.948  11.648  1.00 35.99 ? 13  ASP D OD1   1 
ATOM   1342 O  OD2   . ASP B 1 14  ? 30.440  16.665  10.038  1.00 36.07 ? 13  ASP D OD2   1 
ATOM   1343 N  N     . GLY B 1 15  ? 36.430  15.970  9.579   1.00 36.99 ? 14  GLY D N     1 
ATOM   1344 C  CA    . GLY B 1 15  ? 37.564  15.543  8.773   1.00 37.68 ? 14  GLY D CA    1 
ATOM   1345 C  C     . GLY B 1 15  ? 38.004  16.521  7.699   1.00 36.54 ? 14  GLY D C     1 
ATOM   1346 O  O     . GLY B 1 15  ? 39.012  16.268  7.026   1.00 43.62 ? 14  GLY D O     1 
ATOM   1347 N  N     . GLU B 1 16  ? 37.282  17.559  7.480   1.00 34.36 ? 15  GLU D N     1 
ATOM   1348 C  CA    . GLU B 1 16  ? 37.589  18.507  6.413   1.00 38.87 ? 15  GLU D CA    1 
ATOM   1349 C  C     . GLU B 1 16  ? 38.449  19.614  6.977   1.00 34.90 ? 15  GLU D C     1 
ATOM   1350 O  O     . GLU B 1 16  ? 38.044  20.230  7.938   1.00 32.46 ? 15  GLU D O     1 
ATOM   1351 C  CB    . GLU B 1 16  ? 36.315  19.105  5.856   1.00 39.84 ? 15  GLU D CB    1 
ATOM   1352 C  CG    . GLU B 1 16  ? 36.419  19.691  4.452   1.00 44.54 ? 15  GLU D CG    1 
ATOM   1353 C  CD    . GLU B 1 16  ? 36.018  18.708  3.365   1.00 52.07 ? 15  GLU D CD    1 
ATOM   1354 O  OE1   . GLU B 1 16  ? 36.753  17.698  3.153   1.00 53.81 ? 15  GLU D OE1   1 
ATOM   1355 O  OE2   . GLU B 1 16  ? 34.925  18.906  2.768   1.00 58.42 ? 15  GLU D OE2   1 
ATOM   1356 N  N     . PRO B 1 17  ? 39.620  19.902  6.417   1.00 37.83 ? 16  PRO D N     1 
ATOM   1357 C  CA    . PRO B 1 17  ? 40.445  20.982  6.983   1.00 34.27 ? 16  PRO D CA    1 
ATOM   1358 C  C     . PRO B 1 17  ? 39.652  22.275  6.975   1.00 33.05 ? 16  PRO D C     1 
ATOM   1359 O  O     . PRO B 1 17  ? 38.900  22.554  6.031   1.00 35.02 ? 16  PRO D O     1 
ATOM   1360 C  CB    . PRO B 1 17  ? 41.669  21.040  6.062   1.00 36.00 ? 16  PRO D CB    1 
ATOM   1361 C  CG    . PRO B 1 17  ? 41.679  19.731  5.299   1.00 37.58 ? 16  PRO D CG    1 
ATOM   1362 C  CD    . PRO B 1 17  ? 40.250  19.215  5.279   1.00 37.79 ? 16  PRO D CD    1 
ATOM   1363 N  N     . LEU B 1 18  ? 39.718  22.991  8.102   1.00 33.16 ? 17  LEU D N     1 
ATOM   1364 C  CA    . LEU B 1 18  ? 39.084  24.288  8.273   1.00 29.18 ? 17  LEU D CA    1 
ATOM   1365 C  C     . LEU B 1 18  ? 40.113  25.397  8.162   1.00 30.59 ? 17  LEU D C     1 
ATOM   1366 O  O     . LEU B 1 18  ? 39.973  26.287  7.327   1.00 32.89 ? 17  LEU D O     1 
ATOM   1367 C  CB    . LEU B 1 18  ? 38.363  24.353  9.628   1.00 28.66 ? 17  LEU D CB    1 
ATOM   1368 C  CG    . LEU B 1 18  ? 37.633  25.669  9.944   1.00 23.94 ? 17  LEU D CG    1 
ATOM   1369 C  CD1   . LEU B 1 18  ? 36.532  25.884  8.842   1.00 30.15 ? 17  LEU D CD1   1 
ATOM   1370 C  CD2   . LEU B 1 18  ? 37.022  25.653  11.416  1.00 27.04 ? 17  LEU D CD2   1 
ATOM   1371 N  N     . GLY B 1 19  ? 41.168  25.313  8.959   1.00 27.64 ? 18  GLY D N     1 
ATOM   1372 C  CA    . GLY B 1 19  ? 42.239  26.281  8.910   1.00 29.50 ? 18  GLY D CA    1 
ATOM   1373 C  C     . GLY B 1 19  ? 43.041  26.182  10.191  1.00 30.29 ? 18  GLY D C     1 
ATOM   1374 O  O     . GLY B 1 19  ? 42.741  25.378  11.075  1.00 30.58 ? 18  GLY D O     1 
ATOM   1375 N  N     . ARG B 1 20  ? 44.057  27.029  10.270  1.00 28.01 ? 19  ARG D N     1 
ATOM   1376 C  CA    . ARG B 1 20  ? 45.078  26.992  11.312  1.00 25.32 ? 19  ARG D CA    1 
ATOM   1377 C  C     . ARG B 1 20  ? 44.861  28.124  12.300  1.00 29.94 ? 19  ARG D C     1 
ATOM   1378 O  O     . ARG B 1 20  ? 44.646  29.278  11.904  1.00 28.64 ? 19  ARG D O     1 
ATOM   1379 C  CB    . ARG B 1 20  ? 46.472  27.138  10.693  1.00 25.88 ? 19  ARG D CB    1 
ATOM   1380 C  CG    . ARG B 1 20  ? 47.617  27.281  11.728  1.00 27.43 ? 19  ARG D CG    1 
ATOM   1381 C  CD    . ARG B 1 20  ? 48.995  27.013  11.105  1.00 29.97 ? 19  ARG D CD    1 
ATOM   1382 N  NE    . ARG B 1 20  ? 49.143  25.635  10.647  1.00 34.30 ? 19  ARG D NE    1 
ATOM   1383 C  CZ    . ARG B 1 20  ? 50.283  25.074  10.262  1.00 36.58 ? 19  ARG D CZ    1 
ATOM   1384 N  NH1   . ARG B 1 20  ? 51.435  25.755  10.244  1.00 35.42 ? 19  ARG D NH1   1 
ATOM   1385 N  NH2   . ARG B 1 20  ? 50.276  23.795  9.876   1.00 36.75 ? 19  ARG D NH2   1 
ATOM   1386 N  N     . VAL B 1 21  ? 44.944  27.804  13.594  1.00 26.02 ? 20  VAL D N     1 
ATOM   1387 C  CA    . VAL B 1 21  ? 44.950  28.821  14.643  1.00 24.69 ? 20  VAL D CA    1 
ATOM   1388 C  C     . VAL B 1 21  ? 46.306  28.722  15.325  1.00 25.75 ? 20  VAL D C     1 
ATOM   1389 O  O     . VAL B 1 21  ? 46.720  27.616  15.662  1.00 25.43 ? 20  VAL D O     1 
ATOM   1390 C  CB    . VAL B 1 21  ? 43.810  28.601  15.657  1.00 24.19 ? 20  VAL D CB    1 
ATOM   1391 C  CG1   . VAL B 1 21  ? 43.787  29.741  16.689  1.00 22.58 ? 20  VAL D CG1   1 
ATOM   1392 C  CG2   . VAL B 1 21  ? 42.474  28.469  14.950  1.00 25.84 ? 20  VAL D CG2   1 
ATOM   1393 N  N     . SER B 1 22  ? 47.023  29.842  15.458  1.00 25.40 ? 21  SER D N     1 
ATOM   1394 C  CA    . SER B 1 22  ? 48.302  29.855  16.163  1.00 24.98 ? 21  SER D CA    1 
ATOM   1395 C  C     . SER B 1 22  ? 48.151  30.631  17.463  1.00 27.21 ? 21  SER D C     1 
ATOM   1396 O  O     . SER B 1 22  ? 47.311  31.533  17.562  1.00 25.36 ? 21  SER D O     1 
ATOM   1397 C  CB    . SER B 1 22  ? 49.408  30.468  15.310  1.00 31.25 ? 21  SER D CB    1 
ATOM   1398 O  OG    . SER B 1 22  ? 49.298  31.889  15.232  1.00 29.19 ? 21  SER D OG    1 
ATOM   1399 N  N     . PHE B 1 23  ? 48.947  30.262  18.479  1.00 23.44 ? 22  PHE D N     1 
ATOM   1400 C  CA    . PHE B 1 23  ? 48.822  30.920  19.780  1.00 25.18 ? 22  PHE D CA    1 
ATOM   1401 C  C     . PHE B 1 23  ? 50.179  31.364  20.277  1.00 25.65 ? 22  PHE D C     1 
ATOM   1402 O  O     . PHE B 1 23  ? 51.144  30.600  20.200  1.00 28.84 ? 22  PHE D O     1 
ATOM   1403 C  CB    . PHE B 1 23  ? 48.275  29.994  20.852  1.00 22.31 ? 22  PHE D CB    1 
ATOM   1404 C  CG    . PHE B 1 23  ? 47.012  29.285  20.482  1.00 27.31 ? 22  PHE D CG    1 
ATOM   1405 C  CD1   . PHE B 1 23  ? 47.044  28.046  19.805  1.00 27.16 ? 22  PHE D CD1   1 
ATOM   1406 C  CD2   . PHE B 1 23  ? 45.775  29.841  20.817  1.00 23.65 ? 22  PHE D CD2   1 
ATOM   1407 C  CE1   . PHE B 1 23  ? 45.854  27.396  19.479  1.00 27.15 ? 22  PHE D CE1   1 
ATOM   1408 C  CE2   . PHE B 1 23  ? 44.592  29.186  20.503  1.00 22.87 ? 22  PHE D CE2   1 
ATOM   1409 C  CZ    . PHE B 1 23  ? 44.613  27.968  19.868  1.00 27.27 ? 22  PHE D CZ    1 
ATOM   1410 N  N     . GLU B 1 24  ? 50.225  32.566  20.835  1.00 24.86 ? 23  GLU D N     1 
ATOM   1411 C  CA    . GLU B 1 24  ? 51.366  32.985  21.630  1.00 28.53 ? 23  GLU D CA    1 
ATOM   1412 C  C     . GLU B 1 24  ? 51.153  32.481  23.032  1.00 28.78 ? 23  GLU D C     1 
ATOM   1413 O  O     . GLU B 1 24  ? 50.056  32.654  23.591  1.00 25.28 ? 23  GLU D O     1 
ATOM   1414 C  CB    . GLU B 1 24  ? 51.489  34.502  21.657  1.00 28.37 ? 23  GLU D CB    1 
ATOM   1415 C  CG    . GLU B 1 24  ? 52.720  34.965  22.418  1.00 33.34 ? 23  GLU D CG    1 
ATOM   1416 C  CD    . GLU B 1 24  ? 52.760  36.471  22.589  1.00 31.56 ? 23  GLU D CD    1 
ATOM   1417 O  OE1   . GLU B 1 24  ? 51.971  37.188  21.927  1.00 34.29 ? 23  GLU D OE1   1 
ATOM   1418 O  OE2   . GLU B 1 24  ? 53.635  36.928  23.328  1.00 33.70 ? 23  GLU D OE2   1 
ATOM   1419 N  N     . LEU B 1 25  ? 52.162  31.822  23.596  1.00 30.61 ? 24  LEU D N     1 
ATOM   1420 C  CA    . LEU B 1 25  ? 52.040  31.294  24.958  1.00 28.02 ? 24  LEU D CA    1 
ATOM   1421 C  C     . LEU B 1 25  ? 52.833  32.149  25.932  1.00 30.84 ? 24  LEU D C     1 
ATOM   1422 O  O     . LEU B 1 25  ? 54.042  32.347  25.762  1.00 30.80 ? 24  LEU D O     1 
ATOM   1423 C  CB    . LEU B 1 25  ? 52.476  29.832  25.073  1.00 29.77 ? 24  LEU D CB    1 
ATOM   1424 C  CG    . LEU B 1 25  ? 51.812  28.822  24.128  1.00 27.34 ? 24  LEU D CG    1 
ATOM   1425 C  CD1   . LEU B 1 25  ? 52.265  27.380  24.549  1.00 25.28 ? 24  LEU D CD1   1 
ATOM   1426 C  CD2   . LEU B 1 25  ? 50.307  28.965  24.177  1.00 27.69 ? 24  LEU D CD2   1 
ATOM   1427 N  N     . PHE B 1 26  ? 52.159  32.630  26.974  1.00 29.60 ? 25  PHE D N     1 
ATOM   1428 C  CA    . PHE B 1 26  ? 52.786  33.612  27.870  1.00 31.72 ? 25  PHE D CA    1 
ATOM   1429 C  C     . PHE B 1 26  ? 53.708  32.964  28.919  1.00 31.93 ? 25  PHE D C     1 
ATOM   1430 O  O     . PHE B 1 26  ? 53.488  33.036  30.128  1.00 33.07 ? 25  PHE D O     1 
ATOM   1431 C  CB    . PHE B 1 26  ? 51.690  34.436  28.521  1.00 31.91 ? 25  PHE D CB    1 
ATOM   1432 C  CG    . PHE B 1 26  ? 50.836  35.170  27.538  1.00 30.42 ? 25  PHE D CG    1 
ATOM   1433 C  CD1   . PHE B 1 26  ? 51.388  35.806  26.434  1.00 30.56 ? 25  PHE D CD1   1 
ATOM   1434 C  CD2   . PHE B 1 26  ? 49.476  35.224  27.718  1.00 28.09 ? 25  PHE D CD2   1 
ATOM   1435 C  CE1   . PHE B 1 26  ? 50.575  36.454  25.511  1.00 28.30 ? 25  PHE D CE1   1 
ATOM   1436 C  CE2   . PHE B 1 26  ? 48.659  35.889  26.796  1.00 30.01 ? 25  PHE D CE2   1 
ATOM   1437 C  CZ    . PHE B 1 26  ? 49.228  36.507  25.698  1.00 27.37 ? 25  PHE D CZ    1 
ATOM   1438 N  N     . ALA B 1 27  ? 54.778  32.327  28.433  1.00 32.41 ? 26  ALA D N     1 
ATOM   1439 C  CA    . ALA B 1 27  ? 55.776  31.749  29.326  1.00 33.46 ? 26  ALA D CA    1 
ATOM   1440 C  C     . ALA B 1 27  ? 56.401  32.798  30.222  1.00 32.56 ? 26  ALA D C     1 
ATOM   1441 O  O     . ALA B 1 27  ? 56.991  32.460  31.265  1.00 32.75 ? 26  ALA D O     1 
ATOM   1442 C  CB    . ALA B 1 27  ? 56.897  31.069  28.537  1.00 35.70 ? 26  ALA D CB    1 
ATOM   1443 N  N     . ASP B 1 28  ? 56.358  34.059  29.814  1.00 32.65 ? 27  ASP D N     1 
ATOM   1444 C  CA    . ASP B 1 28  ? 57.014  35.063  30.636  1.00 35.33 ? 27  ASP D CA    1 
ATOM   1445 C  C     . ASP B 1 28  ? 56.190  35.501  31.843  1.00 33.94 ? 27  ASP D C     1 
ATOM   1446 O  O     . ASP B 1 28  ? 56.718  36.235  32.677  1.00 36.71 ? 27  ASP D O     1 
ATOM   1447 C  CB    . ASP B 1 28  ? 57.393  36.264  29.767  1.00 36.51 ? 27  ASP D CB    1 
ATOM   1448 C  CG    . ASP B 1 28  ? 56.199  36.938  29.136  1.00 37.17 ? 27  ASP D CG    1 
ATOM   1449 O  OD1   . ASP B 1 28  ? 55.067  36.404  29.192  1.00 36.63 ? 27  ASP D OD1   1 
ATOM   1450 O  OD2   . ASP B 1 28  ? 56.442  37.988  28.487  1.00 45.43 ? 27  ASP D OD2   1 
ATOM   1451 N  N     . LYS B 1 29  ? 54.942  35.072  31.970  1.00 31.36 ? 28  LYS D N     1 
ATOM   1452 C  CA    . LYS B 1 29  ? 54.117  35.302  33.162  1.00 33.44 ? 28  LYS D CA    1 
ATOM   1453 C  C     . LYS B 1 29  ? 53.631  34.008  33.829  1.00 31.48 ? 28  LYS D C     1 
ATOM   1454 O  O     . LYS B 1 29  ? 53.428  33.990  35.053  1.00 31.60 ? 28  LYS D O     1 
ATOM   1455 C  CB    . LYS B 1 29  ? 52.880  36.155  32.818  1.00 35.37 ? 28  LYS D CB    1 
ATOM   1456 C  CG    . LYS B 1 29  ? 53.274  37.410  32.036  1.00 41.12 ? 28  LYS D CG    1 
ATOM   1457 C  CD    . LYS B 1 29  ? 52.423  38.599  32.350  1.00 37.36 ? 28  LYS D CD    1 
ATOM   1458 C  CE    . LYS B 1 29  ? 53.302  39.795  32.510  1.00 33.94 ? 28  LYS D CE    1 
ATOM   1459 N  NZ    . LYS B 1 29  ? 53.661  40.429  31.210  1.00 36.90 ? 28  LYS D NZ    1 
ATOM   1460 N  N     . VAL B 1 30  ? 53.471  32.932  33.072  1.00 29.62 ? 29  VAL D N     1 
ATOM   1461 C  CA    . VAL B 1 30  ? 52.998  31.632  33.555  1.00 31.51 ? 29  VAL D CA    1 
ATOM   1462 C  C     . VAL B 1 30  ? 53.809  30.542  32.867  1.00 31.29 ? 29  VAL D C     1 
ATOM   1463 O  O     . VAL B 1 30  ? 53.304  29.837  31.990  1.00 32.50 ? 29  VAL D O     1 
ATOM   1464 C  CB    . VAL B 1 30  ? 51.482  31.444  33.318  1.00 29.77 ? 29  VAL D CB    1 
ATOM   1465 C  CG1   . VAL B 1 30  ? 50.660  32.190  34.407  1.00 29.86 ? 29  VAL D CG1   1 
ATOM   1466 C  CG2   . VAL B 1 30  ? 51.036  31.982  31.941  1.00 30.24 ? 29  VAL D CG2   1 
ATOM   1467 N  N     . PRO B 1 31  ? 55.073  30.381  33.237  1.00 31.73 ? 30  PRO D N     1 
ATOM   1468 C  CA    . PRO B 1 31  ? 55.947  29.442  32.513  1.00 31.47 ? 30  PRO D CA    1 
ATOM   1469 C  C     . PRO B 1 31  ? 55.506  28.009  32.609  1.00 30.19 ? 30  PRO D C     1 
ATOM   1470 O  O     . PRO B 1 31  ? 55.622  27.280  31.623  1.00 34.07 ? 30  PRO D O     1 
ATOM   1471 C  CB    . PRO B 1 31  ? 57.318  29.620  33.219  1.00 30.60 ? 30  PRO D CB    1 
ATOM   1472 C  CG    . PRO B 1 31  ? 56.987  30.266  34.568  1.00 30.91 ? 30  PRO D CG    1 
ATOM   1473 C  CD    . PRO B 1 31  ? 55.789  31.117  34.307  1.00 30.02 ? 30  PRO D CD    1 
ATOM   1474 N  N     . LYS B 1 32  ? 55.065  27.567  33.790  1.00 31.17 ? 31  LYS D N     1 
ATOM   1475 C  CA    . LYS B 1 32  ? 54.690  26.163  33.978  1.00 31.97 ? 31  LYS D CA    1 
ATOM   1476 C  C     . LYS B 1 32  ? 53.450  25.803  33.154  1.00 32.47 ? 31  LYS D C     1 
ATOM   1477 O  O     . LYS B 1 32  ? 53.375  24.706  32.563  1.00 31.77 ? 31  LYS D O     1 
ATOM   1478 C  CB    . LYS B 1 32  ? 54.423  25.892  35.454  1.00 31.31 ? 31  LYS D CB    1 
ATOM   1479 C  CG    . LYS B 1 32  ? 55.667  25.643  36.346  1.00 39.76 ? 31  LYS D CG    1 
ATOM   1480 C  CD    . LYS B 1 32  ? 55.193  25.009  37.658  1.00 41.96 ? 31  LYS D CD    1 
ATOM   1481 C  CE    . LYS B 1 32  ? 54.052  23.980  37.350  1.00 42.50 ? 31  LYS D CE    1 
ATOM   1482 N  NZ    . LYS B 1 32  ? 53.692  23.047  38.505  1.00 50.55 ? 31  LYS D NZ    1 
ATOM   1483 N  N     . THR B 1 33  ? 52.474  26.720  33.123  1.00 31.00 ? 32  THR D N     1 
ATOM   1484 C  CA    . THR B 1 33  ? 51.231  26.530  32.363  1.00 29.01 ? 32  THR D CA    1 
ATOM   1485 C  C     . THR B 1 33  ? 51.483  26.639  30.870  1.00 28.84 ? 32  THR D C     1 
ATOM   1486 O  O     . THR B 1 33  ? 50.939  25.857  30.088  1.00 27.77 ? 32  THR D O     1 
ATOM   1487 C  CB    . THR B 1 33  ? 50.193  27.567  32.803  1.00 29.12 ? 32  THR D CB    1 
ATOM   1488 O  OG1   . THR B 1 33  ? 50.077  27.528  34.234  1.00 30.25 ? 32  THR D OG1   1 
ATOM   1489 C  CG2   . THR B 1 33  ? 48.775  27.248  32.189  1.00 23.96 ? 32  THR D CG2   1 
ATOM   1490 N  N     . ALA B 1 34  ? 52.312  27.594  30.458  1.00 29.84 ? 33  ALA D N     1 
ATOM   1491 C  CA    . ALA B 1 34  ? 52.695  27.687  29.056  1.00 30.10 ? 33  ALA D CA    1 
ATOM   1492 C  C     . ALA B 1 34  ? 53.408  26.421  28.599  1.00 30.97 ? 33  ALA D C     1 
ATOM   1493 O  O     . ALA B 1 34  ? 53.112  25.869  27.527  1.00 33.23 ? 33  ALA D O     1 
ATOM   1494 C  CB    . ALA B 1 34  ? 53.578  28.916  28.857  1.00 28.62 ? 33  ALA D CB    1 
ATOM   1495 N  N     . GLU B 1 35  ? 54.353  25.939  29.410  1.00 29.41 ? 34  GLU D N     1 
ATOM   1496 C  CA    . GLU B 1 35  ? 55.127  24.777  28.992  1.00 33.57 ? 34  GLU D CA    1 
ATOM   1497 C  C     . GLU B 1 35  ? 54.241  23.551  28.825  1.00 33.52 ? 34  GLU D C     1 
ATOM   1498 O  O     . GLU B 1 35  ? 54.401  22.776  27.875  1.00 34.34 ? 34  GLU D O     1 
ATOM   1499 C  CB    . GLU B 1 35  ? 56.250  24.528  30.009  1.00 33.19 ? 34  GLU D CB    1 
ATOM   1500 C  CG    . GLU B 1 35  ? 56.990  23.220  29.813  1.00 38.69 ? 34  GLU D CG    1 
ATOM   1501 C  CD    . GLU B 1 35  ? 57.736  23.112  28.463  1.00 39.52 ? 34  GLU D CD    1 
ATOM   1502 O  OE1   . GLU B 1 35  ? 57.817  24.096  27.700  1.00 33.50 ? 34  GLU D OE1   1 
ATOM   1503 O  OE2   . GLU B 1 35  ? 58.253  22.014  28.173  1.00 43.20 ? 34  GLU D OE2   1 
ATOM   1504 N  N     . ASN B 1 36  ? 53.308  23.338  29.743  1.00 34.01 ? 35  ASN D N     1 
ATOM   1505 C  CA    . ASN B 1 36  ? 52.373  22.217  29.593  1.00 31.47 ? 35  ASN D CA    1 
ATOM   1506 C  C     . ASN B 1 36  ? 51.674  22.239  28.231  1.00 32.78 ? 35  ASN D C     1 
ATOM   1507 O  O     . ASN B 1 36  ? 51.655  21.233  27.509  1.00 33.57 ? 35  ASN D O     1 
ATOM   1508 C  CB    . ASN B 1 36  ? 51.343  22.289  30.715  1.00 32.21 ? 35  ASN D CB    1 
ATOM   1509 C  CG    . ASN B 1 36  ? 50.334  21.166  30.659  1.00 33.48 ? 35  ASN D CG    1 
ATOM   1510 O  OD1   . ASN B 1 36  ? 50.701  19.986  30.631  1.00 36.28 ? 35  ASN D OD1   1 
ATOM   1511 N  ND2   . ASN B 1 36  ? 49.040  21.528  30.640  1.00 32.29 ? 35  ASN D ND2   1 
ATOM   1512 N  N     . PHE B 1 37  ? 51.123  23.395  27.854  1.00 32.62 ? 36  PHE D N     1 
ATOM   1513 C  CA    . PHE B 1 37  ? 50.364  23.506  26.605  1.00 27.75 ? 36  PHE D CA    1 
ATOM   1514 C  C     . PHE B 1 37  ? 51.291  23.376  25.400  1.00 31.85 ? 36  PHE D C     1 
ATOM   1515 O  O     . PHE B 1 37  ? 50.954  22.713  24.400  1.00 30.54 ? 36  PHE D O     1 
ATOM   1516 C  CB    . PHE B 1 37  ? 49.632  24.852  26.571  1.00 27.59 ? 36  PHE D CB    1 
ATOM   1517 C  CG    . PHE B 1 37  ? 48.572  24.956  25.490  1.00 24.35 ? 36  PHE D CG    1 
ATOM   1518 C  CD1   . PHE B 1 37  ? 47.260  24.582  25.744  1.00 25.95 ? 36  PHE D CD1   1 
ATOM   1519 C  CD2   . PHE B 1 37  ? 48.903  25.465  24.222  1.00 24.86 ? 36  PHE D CD2   1 
ATOM   1520 C  CE1   . PHE B 1 37  ? 46.299  24.715  24.750  1.00 25.23 ? 36  PHE D CE1   1 
ATOM   1521 C  CE2   . PHE B 1 37  ? 47.947  25.593  23.213  1.00 26.81 ? 36  PHE D CE2   1 
ATOM   1522 C  CZ    . PHE B 1 37  ? 46.656  25.225  23.464  1.00 23.17 ? 36  PHE D CZ    1 
ATOM   1523 N  N     . ARG B 1 38  ? 52.481  23.978  25.502  1.00 28.23 ? 37  ARG D N     1 
ATOM   1524 C  CA    . ARG B 1 38  ? 53.493  23.805  24.464  1.00 33.18 ? 37  ARG D CA    1 
ATOM   1525 C  C     . ARG B 1 38  ? 53.796  22.338  24.230  1.00 32.96 ? 37  ARG D C     1 
ATOM   1526 O  O     . ARG B 1 38  ? 53.729  21.853  23.093  1.00 34.35 ? 37  ARG D O     1 
ATOM   1527 C  CB    . ARG B 1 38  ? 54.777  24.535  24.866  1.00 30.53 ? 37  ARG D CB    1 
ATOM   1528 C  CG    . ARG B 1 38  ? 55.820  24.493  23.769  1.00 33.69 ? 37  ARG D CG    1 
ATOM   1529 C  CD    . ARG B 1 38  ? 57.222  24.697  24.324  1.00 31.92 ? 37  ARG D CD    1 
ATOM   1530 N  NE    . ARG B 1 38  ? 57.710  23.565  25.108  1.00 35.00 ? 37  ARG D NE    1 
ATOM   1531 C  CZ    . ARG B 1 38  ? 58.069  22.388  24.594  1.00 37.20 ? 37  ARG D CZ    1 
ATOM   1532 N  NH1   . ARG B 1 38  ? 58.083  22.166  23.284  1.00 32.29 ? 37  ARG D NH1   1 
ATOM   1533 N  NH2   . ARG B 1 38  ? 58.412  21.399  25.413  1.00 37.86 ? 37  ARG D NH2   1 
ATOM   1534 N  N     . ALA B 1 39  ? 54.088  21.604  25.309  1.00 30.45 ? 38  ALA D N     1 
ATOM   1535 C  CA    . ALA B 1 39  ? 54.502  20.208  25.161  1.00 34.93 ? 38  ALA D CA    1 
ATOM   1536 C  C     . ALA B 1 39  ? 53.349  19.331  24.712  1.00 34.57 ? 38  ALA D C     1 
ATOM   1537 O  O     . ALA B 1 39  ? 53.566  18.378  23.950  1.00 34.23 ? 38  ALA D O     1 
ATOM   1538 C  CB    . ALA B 1 39  ? 55.099  19.649  26.463  1.00 33.72 ? 38  ALA D CB    1 
ATOM   1539 N  N     . LEU B 1 40  ? 52.119  19.628  25.170  1.00 31.97 ? 39  LEU D N     1 
ATOM   1540 C  CA    . LEU B 1 40  ? 50.973  18.861  24.673  1.00 31.49 ? 39  LEU D CA    1 
ATOM   1541 C  C     . LEU B 1 40  ? 50.673  19.179  23.222  1.00 33.52 ? 39  LEU D C     1 
ATOM   1542 O  O     . LEU B 1 40  ? 50.082  18.341  22.507  1.00 34.08 ? 39  LEU D O     1 
ATOM   1543 C  CB    . LEU B 1 40  ? 49.734  19.123  25.531  1.00 30.24 ? 39  LEU D CB    1 
ATOM   1544 C  CG    . LEU B 1 40  ? 49.828  18.711  26.997  1.00 33.69 ? 39  LEU D CG    1 
ATOM   1545 C  CD1   . LEU B 1 40  ? 48.632  19.272  27.768  1.00 32.60 ? 39  LEU D CD1   1 
ATOM   1546 C  CD2   . LEU B 1 40  ? 49.861  17.232  27.127  1.00 33.70 ? 39  LEU D CD2   1 
ATOM   1547 N  N     . SER B 1 41  ? 51.056  20.370  22.760  1.00 31.55 ? 40  SER D N     1 
ATOM   1548 C  CA    . SER B 1 41  ? 50.823  20.669  21.354  1.00 29.79 ? 40  SER D CA    1 
ATOM   1549 C  C     . SER B 1 41  ? 51.857  19.975  20.471  1.00 32.91 ? 40  SER D C     1 
ATOM   1550 O  O     . SER B 1 41  ? 51.552  19.649  19.317  1.00 32.84 ? 40  SER D O     1 
ATOM   1551 C  CB    . SER B 1 41  ? 50.852  22.181  21.111  1.00 30.69 ? 40  SER D CB    1 
ATOM   1552 O  OG    . SER B 1 41  ? 49.854  22.886  21.820  1.00 29.37 ? 40  SER D OG    1 
ATOM   1553 N  N     . THR B 1 42  ? 53.078  19.739  20.975  1.00 34.10 ? 41  THR D N     1 
ATOM   1554 C  CA    . THR B 1 42  ? 54.022  18.965  20.172  1.00 35.63 ? 41  THR D CA    1 
ATOM   1555 C  C     . THR B 1 42  ? 53.867  17.453  20.329  1.00 37.67 ? 41  THR D C     1 
ATOM   1556 O  O     . THR B 1 42  ? 54.302  16.710  19.432  1.00 37.98 ? 41  THR D O     1 
ATOM   1557 C  CB    . THR B 1 42  ? 55.491  19.337  20.462  1.00 35.70 ? 41  THR D CB    1 
ATOM   1558 O  OG1   . THR B 1 42  ? 55.875  18.876  21.766  1.00 34.43 ? 41  THR D OG1   1 
ATOM   1559 C  CG2   . THR B 1 42  ? 55.709  20.850  20.301  1.00 33.43 ? 41  THR D CG2   1 
ATOM   1560 N  N     . GLY B 1 43  ? 53.248  16.978  21.414  1.00 35.73 ? 42  GLY D N     1 
ATOM   1561 C  CA    . GLY B 1 43  ? 53.196  15.539  21.647  1.00 36.03 ? 42  GLY D CA    1 
ATOM   1562 C  C     . GLY B 1 43  ? 54.522  14.951  22.047  1.00 41.91 ? 42  GLY D C     1 
ATOM   1563 O  O     . GLY B 1 43  ? 54.677  13.726  22.087  1.00 42.89 ? 42  GLY D O     1 
ATOM   1564 N  N     . GLU B 1 44  ? 55.491  15.801  22.377  1.00 39.80 ? 43  GLU D N     1 
ATOM   1565 C  CA    . GLU B 1 44  ? 56.837  15.317  22.613  1.00 41.73 ? 43  GLU D CA    1 
ATOM   1566 C  C     . GLU B 1 44  ? 56.953  14.412  23.835  1.00 40.49 ? 43  GLU D C     1 
ATOM   1567 O  O     . GLU B 1 44  ? 57.949  13.699  23.963  1.00 42.39 ? 43  GLU D O     1 
ATOM   1568 C  CB    . GLU B 1 44  ? 57.780  16.505  22.715  1.00 41.95 ? 43  GLU D CB    1 
ATOM   1569 C  CG    . GLU B 1 44  ? 57.614  17.322  23.960  1.00 39.46 ? 43  GLU D CG    1 
ATOM   1570 C  CD    . GLU B 1 44  ? 58.381  18.619  23.828  1.00 40.47 ? 43  GLU D CD    1 
ATOM   1571 O  OE1   . GLU B 1 44  ? 58.160  19.340  22.815  1.00 37.03 ? 43  GLU D OE1   1 
ATOM   1572 O  OE2   . GLU B 1 44  ? 59.261  18.848  24.685  1.00 41.36 ? 43  GLU D OE2   1 
ATOM   1573 N  N     . LYS B 1 45  ? 55.966  14.395  24.721  1.00 40.92 ? 44  LYS D N     1 
ATOM   1574 C  CA    . LYS B 1 45  ? 56.030  13.526  25.884  1.00 43.49 ? 44  LYS D CA    1 
ATOM   1575 C  C     . LYS B 1 45  ? 55.333  12.191  25.665  1.00 44.13 ? 44  LYS D C     1 
ATOM   1576 O  O     . LYS B 1 45  ? 55.211  11.421  26.615  1.00 48.64 ? 44  LYS D O     1 
ATOM   1577 C  CB    . LYS B 1 45  ? 55.425  14.223  27.115  1.00 44.83 ? 44  LYS D CB    1 
ATOM   1578 C  CG    . LYS B 1 45  ? 56.029  15.570  27.447  1.00 43.15 ? 44  LYS D CG    1 
ATOM   1579 C  CD    . LYS B 1 45  ? 57.541  15.520  27.784  1.00 45.04 ? 44  LYS D CD    1 
ATOM   1580 C  CE    . LYS B 1 45  ? 57.967  16.836  28.432  1.00 46.82 ? 44  LYS D CE    1 
ATOM   1581 N  NZ    . LYS B 1 45  ? 59.410  17.146  28.228  1.00 47.34 ? 44  LYS D NZ    1 
ATOM   1582 N  N     . GLY B 1 46  ? 54.858  11.910  24.454  1.00 42.13 ? 45  GLY D N     1 
ATOM   1583 C  CA    . GLY B 1 46  ? 54.145  10.681  24.164  1.00 42.56 ? 45  GLY D CA    1 
ATOM   1584 C  C     . GLY B 1 46  ? 52.627  10.784  24.123  1.00 44.23 ? 45  GLY D C     1 
ATOM   1585 O  O     . GLY B 1 46  ? 51.964  9.761   23.898  1.00 45.17 ? 45  GLY D O     1 
ATOM   1586 N  N     . PHE B 1 47  ? 52.054  11.980  24.297  1.00 41.08 ? 46  PHE D N     1 
ATOM   1587 C  CA    . PHE B 1 47  ? 50.604  12.179  24.328  1.00 42.59 ? 46  PHE D CA    1 
ATOM   1588 C  C     . PHE B 1 47  ? 50.358  13.679  24.211  1.00 39.95 ? 46  PHE D C     1 
ATOM   1589 O  O     . PHE B 1 47  ? 51.275  14.480  24.411  1.00 39.08 ? 46  PHE D O     1 
ATOM   1590 C  CB    . PHE B 1 47  ? 49.978  11.571  25.600  1.00 41.97 ? 46  PHE D CB    1 
ATOM   1591 C  CG    . PHE B 1 47  ? 50.579  12.073  26.894  1.00 42.48 ? 46  PHE D CG    1 
ATOM   1592 C  CD1   . PHE B 1 47  ? 50.629  13.434  27.193  1.00 40.83 ? 46  PHE D CD1   1 
ATOM   1593 C  CD2   . PHE B 1 47  ? 51.232  11.194  27.734  1.00 44.92 ? 46  PHE D CD2   1 
ATOM   1594 C  CE1   . PHE B 1 47  ? 51.233  13.891  28.357  1.00 42.91 ? 46  PHE D CE1   1 
ATOM   1595 C  CE2   . PHE B 1 47  ? 51.832  11.644  28.887  1.00 48.58 ? 46  PHE D CE2   1 
ATOM   1596 C  CZ    . PHE B 1 47  ? 51.853  13.000  29.186  1.00 45.17 ? 46  PHE D CZ    1 
ATOM   1597 N  N     . GLY B 1 48  ? 49.141  14.052  23.834  1.00 38.09 ? 47  GLY D N     1 
ATOM   1598 C  CA    . GLY B 1 48  ? 48.812  15.470  23.748  1.00 31.26 ? 47  GLY D CA    1 
ATOM   1599 C  C     . GLY B 1 48  ? 47.573  15.695  22.882  1.00 34.19 ? 47  GLY D C     1 
ATOM   1600 O  O     . GLY B 1 48  ? 46.726  14.809  22.745  1.00 30.63 ? 47  GLY D O     1 
ATOM   1601 N  N     . TYR B 1 49  ? 47.556  16.854  22.219  1.00 31.81 ? 48  TYR D N     1 
ATOM   1602 C  CA    . TYR B 1 49  ? 46.326  17.365  21.639  1.00 29.01 ? 48  TYR D CA    1 
ATOM   1603 C  C     . TYR B 1 49  ? 46.013  16.792  20.272  1.00 32.79 ? 48  TYR D C     1 
ATOM   1604 O  O     . TYR B 1 49  ? 44.842  16.833  19.842  1.00 31.08 ? 48  TYR D O     1 
ATOM   1605 C  CB    . TYR B 1 49  ? 46.382  18.891  21.525  1.00 27.56 ? 48  TYR D CB    1 
ATOM   1606 C  CG    . TYR B 1 49  ? 46.338  19.607  22.888  1.00 29.72 ? 48  TYR D CG    1 
ATOM   1607 C  CD1   . TYR B 1 49  ? 45.381  19.251  23.862  1.00 24.82 ? 48  TYR D CD1   1 
ATOM   1608 C  CD2   . TYR B 1 49  ? 47.209  20.670  23.151  1.00 27.22 ? 48  TYR D CD2   1 
ATOM   1609 C  CE1   . TYR B 1 49  ? 45.325  19.955  25.104  1.00 27.88 ? 48  TYR D CE1   1 
ATOM   1610 C  CE2   . TYR B 1 49  ? 47.162  21.359  24.332  1.00 27.46 ? 48  TYR D CE2   1 
ATOM   1611 C  CZ    . TYR B 1 49  ? 46.236  20.996  25.302  1.00 27.13 ? 48  TYR D CZ    1 
ATOM   1612 O  OH    . TYR B 1 49  ? 46.239  21.724  26.436  1.00 27.09 ? 48  TYR D OH    1 
ATOM   1613 N  N     . LYS B 1 50  ? 47.013  16.299  19.555  1.00 32.76 ? 49  LYS D N     1 
ATOM   1614 C  CA    . LYS B 1 50  ? 46.726  15.863  18.201  1.00 31.36 ? 49  LYS D CA    1 
ATOM   1615 C  C     . LYS B 1 50  ? 45.624  14.809  18.232  1.00 34.97 ? 49  LYS D C     1 
ATOM   1616 O  O     . LYS B 1 50  ? 45.709  13.836  18.989  1.00 36.44 ? 49  LYS D O     1 
ATOM   1617 C  CB    . LYS B 1 50  ? 47.997  15.323  17.553  1.00 32.42 ? 49  LYS D CB    1 
ATOM   1618 C  CG    . LYS B 1 50  ? 47.769  14.835  16.090  1.00 32.94 ? 49  LYS D CG    1 
ATOM   1619 C  CD    . LYS B 1 50  ? 49.089  14.730  15.371  1.00 38.77 ? 49  LYS D CD    1 
ATOM   1620 C  CE    . LYS B 1 50  ? 48.961  14.039  14.017  1.00 41.58 ? 49  LYS D CE    1 
ATOM   1621 N  NZ    . LYS B 1 50  ? 50.321  13.649  13.501  1.00 45.73 ? 49  LYS D NZ    1 
ATOM   1622 N  N     . GLY B 1 51  ? 44.571  15.007  17.414  1.00 32.41 ? 50  GLY D N     1 
ATOM   1623 C  CA    . GLY B 1 51  ? 43.489  14.055  17.359  1.00 33.06 ? 50  GLY D CA    1 
ATOM   1624 C  C     . GLY B 1 51  ? 42.340  14.315  18.307  1.00 32.70 ? 50  GLY D C     1 
ATOM   1625 O  O     . GLY B 1 51  ? 41.296  13.672  18.163  1.00 34.60 ? 50  GLY D O     1 
ATOM   1626 N  N     . SER B 1 52  ? 42.466  15.258  19.235  1.00 33.67 ? 51  SER D N     1 
ATOM   1627 C  CA    . SER B 1 52  ? 41.390  15.496  20.195  1.00 32.84 ? 51  SER D CA    1 
ATOM   1628 C  C     . SER B 1 52  ? 40.355  16.449  19.593  1.00 31.09 ? 51  SER D C     1 
ATOM   1629 O  O     . SER B 1 52  ? 40.579  17.066  18.541  1.00 29.73 ? 51  SER D O     1 
ATOM   1630 C  CB    . SER B 1 52  ? 41.942  16.047  21.512  1.00 30.12 ? 51  SER D CB    1 
ATOM   1631 O  OG    . SER B 1 52  ? 42.520  17.339  21.332  1.00 28.85 ? 51  SER D OG    1 
ATOM   1632 N  N     . CYS B 1 53  ? 39.204  16.575  20.254  1.00 27.85 ? 52  CYS D N     1 
ATOM   1633 C  CA    . CYS B 1 53  ? 38.156  17.440  19.707  1.00 27.51 ? 52  CYS D CA    1 
ATOM   1634 C  C     . CYS B 1 53  ? 37.855  18.668  20.568  1.00 28.66 ? 52  CYS D C     1 
ATOM   1635 O  O     . CYS B 1 53  ? 38.218  18.753  21.742  1.00 27.74 ? 52  CYS D O     1 
ATOM   1636 C  CB    . CYS B 1 53  ? 36.859  16.666  19.511  1.00 33.18 ? 52  CYS D CB    1 
ATOM   1637 S  SG    . CYS B 1 53  ? 36.050  16.252  21.040  1.00 44.25 ? 52  CYS D SG    1 
ATOM   1638 N  N     . PHE B 1 54  ? 37.198  19.647  19.956  1.00 25.19 ? 53  PHE D N     1 
ATOM   1639 C  CA    . PHE B 1 54  ? 36.582  20.741  20.709  1.00 27.21 ? 53  PHE D CA    1 
ATOM   1640 C  C     . PHE B 1 54  ? 35.189  20.273  21.086  1.00 27.42 ? 53  PHE D C     1 
ATOM   1641 O  O     . PHE B 1 54  ? 34.302  20.176  20.215  1.00 28.68 ? 53  PHE D O     1 
ATOM   1642 C  CB    . PHE B 1 54  ? 36.522  22.050  19.935  1.00 25.31 ? 53  PHE D CB    1 
ATOM   1643 C  CG    . PHE B 1 54  ? 37.826  22.810  19.918  1.00 22.81 ? 53  PHE D CG    1 
ATOM   1644 C  CD1   . PHE B 1 54  ? 38.860  22.435  19.065  1.00 24.86 ? 53  PHE D CD1   1 
ATOM   1645 C  CD2   . PHE B 1 54  ? 38.021  23.889  20.786  1.00 24.83 ? 53  PHE D CD2   1 
ATOM   1646 C  CE1   . PHE B 1 54  ? 40.117  23.142  19.098  1.00 24.75 ? 53  PHE D CE1   1 
ATOM   1647 C  CE2   . PHE B 1 54  ? 39.241  24.588  20.801  1.00 25.26 ? 53  PHE D CE2   1 
ATOM   1648 C  CZ    . PHE B 1 54  ? 40.281  24.202  19.945  1.00 24.49 ? 53  PHE D CZ    1 
ATOM   1649 N  N     . HIS B 1 55  ? 35.010  19.949  22.368  1.00 25.37 ? 54  HIS D N     1 
ATOM   1650 C  CA    . HIS B 1 55  ? 33.779  19.282  22.761  1.00 25.59 ? 54  HIS D CA    1 
ATOM   1651 C  C     . HIS B 1 55  ? 32.668  20.247  23.143  1.00 27.75 ? 54  HIS D C     1 
ATOM   1652 O  O     . HIS B 1 55  ? 31.484  19.847  23.153  1.00 27.64 ? 54  HIS D O     1 
ATOM   1653 C  CB    . HIS B 1 55  ? 34.014  18.296  23.908  1.00 24.17 ? 54  HIS D CB    1 
ATOM   1654 C  CG    . HIS B 1 55  ? 34.641  18.925  25.116  1.00 26.15 ? 54  HIS D CG    1 
ATOM   1655 N  ND1   . HIS B 1 55  ? 36.003  19.140  25.215  1.00 26.36 ? 54  HIS D ND1   1 
ATOM   1656 C  CD2   . HIS B 1 55  ? 34.096  19.362  26.280  1.00 26.69 ? 54  HIS D CD2   1 
ATOM   1657 C  CE1   . HIS B 1 55  ? 36.262  19.722  26.380  1.00 28.14 ? 54  HIS D CE1   1 
ATOM   1658 N  NE2   . HIS B 1 55  ? 35.123  19.842  27.052  1.00 27.63 ? 54  HIS D NE2   1 
ATOM   1659 N  N     . ARG B 1 56  ? 32.996  21.502  23.398  1.00 24.16 ? 55  ARG D N     1 
ATOM   1660 C  CA    . ARG B 1 56  ? 32.009  22.473  23.817  1.00 22.43 ? 55  ARG D CA    1 
ATOM   1661 C  C     . ARG B 1 56  ? 32.285  23.780  23.091  1.00 24.54 ? 55  ARG D C     1 
ATOM   1662 O  O     . ARG B 1 56  ? 33.310  24.418  23.332  1.00 22.61 ? 55  ARG D O     1 
ATOM   1663 C  CB    . ARG B 1 56  ? 32.062  22.653  25.352  1.00 25.93 ? 55  ARG D CB    1 
ATOM   1664 C  CG    . ARG B 1 56  ? 31.293  23.863  25.909  1.00 29.06 ? 55  ARG D CG    1 
ATOM   1665 C  CD    . ARG B 1 56  ? 31.428  23.932  27.445  1.00 29.00 ? 55  ARG D CD    1 
ATOM   1666 N  NE    . ARG B 1 56  ? 30.928  22.727  28.096  1.00 30.74 ? 55  ARG D NE    1 
ATOM   1667 C  CZ    . ARG B 1 56  ? 31.379  22.288  29.266  1.00 30.06 ? 55  ARG D CZ    1 
ATOM   1668 N  NH1   . ARG B 1 56  ? 32.443  22.833  29.849  1.00 29.99 ? 55  ARG D NH1   1 
ATOM   1669 N  NH2   . ARG B 1 56  ? 30.797  21.250  29.840  1.00 30.50 ? 55  ARG D NH2   1 
ATOM   1670 N  N     . ILE B 1 57  ? 31.316  24.227  22.313  1.00 24.37 ? 56  ILE D N     1 
ATOM   1671 C  CA    . ILE B 1 57  ? 31.409  25.519  21.624  1.00 23.77 ? 56  ILE D CA    1 
ATOM   1672 C  C     . ILE B 1 57  ? 30.132  26.285  21.907  1.00 21.46 ? 56  ILE D C     1 
ATOM   1673 O  O     . ILE B 1 57  ? 29.044  25.843  21.523  1.00 24.34 ? 56  ILE D O     1 
ATOM   1674 C  CB    . ILE B 1 57  ? 31.623  25.337  20.125  1.00 23.51 ? 56  ILE D CB    1 
ATOM   1675 C  CG1   . ILE B 1 57  ? 32.933  24.548  19.895  1.00 23.91 ? 56  ILE D CG1   1 
ATOM   1676 C  CG2   . ILE B 1 57  ? 31.588  26.706  19.401  1.00 21.10 ? 56  ILE D CG2   1 
ATOM   1677 C  CD1   . ILE B 1 57  ? 33.182  24.182  18.434  1.00 24.84 ? 56  ILE D CD1   1 
ATOM   1678 N  N     . ILE B 1 58  ? 30.255  27.404  22.602  1.00 21.08 ? 57  ILE D N     1 
ATOM   1679 C  CA    . ILE B 1 58  ? 29.104  28.250  22.932  1.00 20.45 ? 57  ILE D CA    1 
ATOM   1680 C  C     . ILE B 1 58  ? 29.315  29.599  22.264  1.00 20.33 ? 57  ILE D C     1 
ATOM   1681 O  O     . ILE B 1 58  ? 30.095  30.428  22.753  1.00 20.68 ? 57  ILE D O     1 
ATOM   1682 C  CB    . ILE B 1 58  ? 28.943  28.371  24.470  1.00 23.94 ? 57  ILE D CB    1 
ATOM   1683 C  CG1   . ILE B 1 58  ? 28.821  26.963  25.064  1.00 20.46 ? 57  ILE D CG1   1 
ATOM   1684 C  CG2   . ILE B 1 58  ? 27.744  29.238  24.863  1.00 22.62 ? 57  ILE D CG2   1 
ATOM   1685 C  CD1   . ILE B 1 58  ? 28.863  26.935  26.628  1.00 24.79 ? 57  ILE D CD1   1 
ATOM   1686 N  N     . PRO B 1 59  ? 28.562  29.881  21.208  1.00 22.89 ? 58  PRO D N     1 
ATOM   1687 C  CA    . PRO B 1 59  ? 28.729  31.118  20.442  1.00 21.07 ? 58  PRO D CA    1 
ATOM   1688 C  C     . PRO B 1 59  ? 28.520  32.334  21.319  1.00 21.67 ? 58  PRO D C     1 
ATOM   1689 O  O     . PRO B 1 59  ? 27.583  32.400  22.120  1.00 23.14 ? 58  PRO D O     1 
ATOM   1690 C  CB    . PRO B 1 59  ? 27.647  31.005  19.339  1.00 20.79 ? 58  PRO D CB    1 
ATOM   1691 C  CG    . PRO B 1 59  ? 27.368  29.505  19.252  1.00 23.02 ? 58  PRO D CG    1 
ATOM   1692 C  CD    . PRO B 1 59  ? 27.567  28.967  20.651  1.00 20.33 ? 58  PRO D CD    1 
ATOM   1693 N  N     . GLY B 1 60  ? 29.431  33.292  21.179  1.00 24.65 ? 59  GLY D N     1 
ATOM   1694 C  CA    . GLY B 1 60  ? 29.387  34.484  21.997  1.00 24.60 ? 59  GLY D CA    1 
ATOM   1695 C  C     . GLY B 1 60  ? 30.221  34.414  23.237  1.00 25.00 ? 59  GLY D C     1 
ATOM   1696 O  O     . GLY B 1 60  ? 30.363  35.443  23.931  1.00 25.91 ? 59  GLY D O     1 
ATOM   1697 N  N     . PHE B 1 61  ? 30.769  33.238  23.560  1.00 22.93 ? 60  PHE D N     1 
ATOM   1698 C  CA    . PHE B 1 61  ? 31.545  33.091  24.781  1.00 22.66 ? 60  PHE D CA    1 
ATOM   1699 C  C     . PHE B 1 61  ? 32.860  32.384  24.539  1.00 23.63 ? 60  PHE D C     1 
ATOM   1700 O  O     . PHE B 1 61  ? 33.902  33.005  24.764  1.00 22.07 ? 60  PHE D O     1 
ATOM   1701 C  CB    . PHE B 1 61  ? 30.746  32.308  25.830  1.00 23.78 ? 60  PHE D CB    1 
ATOM   1702 C  CG    . PHE B 1 61  ? 29.526  33.026  26.284  1.00 25.77 ? 60  PHE D CG    1 
ATOM   1703 C  CD1   . PHE B 1 61  ? 29.587  33.930  27.334  1.00 27.31 ? 60  PHE D CD1   1 
ATOM   1704 C  CD2   . PHE B 1 61  ? 28.312  32.831  25.614  1.00 24.66 ? 60  PHE D CD2   1 
ATOM   1705 C  CE1   . PHE B 1 61  ? 28.462  34.588  27.777  1.00 28.00 ? 60  PHE D CE1   1 
ATOM   1706 C  CE2   . PHE B 1 61  ? 27.151  33.501  26.042  1.00 26.97 ? 60  PHE D CE2   1 
ATOM   1707 C  CZ    . PHE B 1 61  ? 27.239  34.411  27.128  1.00 30.25 ? 60  PHE D CZ    1 
ATOM   1708 N  N     . MET B 1 62  ? 32.850  31.097  24.127  1.00 22.46 ? 61  MET D N     1 
ATOM   1709 C  CA    . MET B 1 62  ? 34.141  30.405  24.013  1.00 21.02 ? 61  MET D CA    1 
ATOM   1710 C  C     . MET B 1 62  ? 34.034  29.024  23.364  1.00 22.14 ? 61  MET D C     1 
ATOM   1711 O  O     . MET B 1 62  ? 32.938  28.473  23.183  1.00 22.41 ? 61  MET D O     1 
ATOM   1712 C  CB    . MET B 1 62  ? 34.867  30.328  25.381  1.00 21.17 ? 61  MET D CB    1 
ATOM   1713 C  CG    . MET B 1 62  ? 34.007  30.003  26.631  1.00 28.84 ? 61  MET D CG    1 
ATOM   1714 S  SD    . MET B 1 62  ? 32.675  28.800  26.582  1.00 26.87 ? 61  MET D SD    1 
ATOM   1715 C  CE    . MET B 1 62  ? 33.982  27.529  26.377  1.00 26.04 ? 61  MET D CE    1 
ATOM   1716 N  N     . CYS B 1 63  ? 35.203  28.522  22.942  1.00 20.19 ? 62  CYS D N     1 
ATOM   1717 C  CA    . CYS B 1 63  ? 35.412  27.181  22.403  1.00 19.98 ? 62  CYS D CA    1 
ATOM   1718 C  C     . CYS B 1 63  ? 36.289  26.428  23.377  1.00 21.30 ? 62  CYS D C     1 
ATOM   1719 O  O     . CYS B 1 63  ? 37.357  26.921  23.747  1.00 22.80 ? 62  CYS D O     1 
ATOM   1720 C  CB    . CYS B 1 63  ? 36.141  27.213  21.043  1.00 20.47 ? 62  CYS D CB    1 
ATOM   1721 S  SG    . CYS B 1 63  ? 35.205  28.132  19.761  1.00 23.36 ? 62  CYS D SG    1 
ATOM   1722 N  N     . GLN B 1 64  ? 35.889  25.212  23.748  1.00 21.08 ? 63  GLN D N     1 
ATOM   1723 C  CA    . GLN B 1 64  ? 36.673  24.507  24.762  1.00 24.83 ? 63  GLN D CA    1 
ATOM   1724 C  C     . GLN B 1 64  ? 37.044  23.129  24.215  1.00 24.85 ? 63  GLN D C     1 
ATOM   1725 O  O     . GLN B 1 64  ? 36.223  22.510  23.522  1.00 24.47 ? 63  GLN D O     1 
ATOM   1726 C  CB    . GLN B 1 64  ? 35.845  24.406  26.059  1.00 21.12 ? 63  GLN D CB    1 
ATOM   1727 C  CG    . GLN B 1 64  ? 36.486  23.584  27.169  1.00 23.12 ? 63  GLN D CG    1 
ATOM   1728 C  CD    . GLN B 1 64  ? 35.654  23.516  28.467  1.00 28.32 ? 63  GLN D CD    1 
ATOM   1729 O  OE1   . GLN B 1 64  ? 34.711  24.332  28.677  1.00 26.29 ? 63  GLN D OE1   1 
ATOM   1730 N  NE2   . GLN B 1 64  ? 36.013  22.546  29.355  1.00 26.05 ? 63  GLN D NE2   1 
ATOM   1731 N  N     . GLY B 1 65  ? 38.285  22.666  24.492  1.00 24.99 ? 64  GLY D N     1 
ATOM   1732 C  CA    . GLY B 1 65  ? 38.725  21.326  24.121  1.00 25.64 ? 64  GLY D CA    1 
ATOM   1733 C  C     . GLY B 1 65  ? 39.789  20.789  25.072  1.00 27.79 ? 64  GLY D C     1 
ATOM   1734 O  O     . GLY B 1 65  ? 39.843  21.182  26.247  1.00 26.13 ? 64  GLY D O     1 
ATOM   1735 N  N     . GLY B 1 66  ? 40.592  19.840  24.582  1.00 28.66 ? 65  GLY D N     1 
ATOM   1736 C  CA    . GLY B 1 66  ? 41.787  19.396  25.293  1.00 25.64 ? 65  GLY D CA    1 
ATOM   1737 C  C     . GLY B 1 66  ? 41.685  18.043  25.944  1.00 29.11 ? 65  GLY D C     1 
ATOM   1738 O  O     . GLY B 1 66  ? 42.634  17.634  26.623  1.00 34.73 ? 65  GLY D O     1 
ATOM   1739 N  N     . ASP B 1 67  ? 40.553  17.346  25.815  1.00 31.89 ? 66  ASP D N     1 
ATOM   1740 C  CA    . ASP B 1 67  ? 40.418  16.052  26.506  1.00 34.02 ? 66  ASP D CA    1 
ATOM   1741 C  C     . ASP B 1 67  ? 40.845  14.926  25.575  1.00 36.77 ? 66  ASP D C     1 
ATOM   1742 O  O     . ASP B 1 67  ? 40.040  14.335  24.861  1.00 36.22 ? 66  ASP D O     1 
ATOM   1743 C  CB    . ASP B 1 67  ? 39.004  15.851  27.025  1.00 34.25 ? 66  ASP D CB    1 
ATOM   1744 C  CG    . ASP B 1 67  ? 38.821  14.488  27.711  1.00 38.64 ? 66  ASP D CG    1 
ATOM   1745 O  OD1   . ASP B 1 67  ? 39.817  13.724  27.840  1.00 38.24 ? 66  ASP D OD1   1 
ATOM   1746 O  OD2   . ASP B 1 67  ? 37.664  14.171  28.087  1.00 40.20 ? 66  ASP D OD2   1 
ATOM   1747 N  N     . PHE B 1 68  ? 42.126  14.602  25.618  1.00 36.12 ? 67  PHE D N     1 
ATOM   1748 C  CA    . PHE B 1 68  ? 42.703  13.568  24.784  1.00 38.26 ? 67  PHE D CA    1 
ATOM   1749 C  C     . PHE B 1 68  ? 42.809  12.213  25.487  1.00 39.89 ? 67  PHE D C     1 
ATOM   1750 O  O     . PHE B 1 68  ? 43.282  11.253  24.868  1.00 42.32 ? 67  PHE D O     1 
ATOM   1751 C  CB    . PHE B 1 68  ? 44.085  14.029  24.288  1.00 36.07 ? 67  PHE D CB    1 
ATOM   1752 C  CG    . PHE B 1 68  ? 45.060  14.270  25.377  1.00 37.04 ? 67  PHE D CG    1 
ATOM   1753 C  CD1   . PHE B 1 68  ? 45.670  13.211  26.015  1.00 37.35 ? 67  PHE D CD1   1 
ATOM   1754 C  CD2   . PHE B 1 68  ? 45.400  15.581  25.758  1.00 37.63 ? 67  PHE D CD2   1 
ATOM   1755 C  CE1   . PHE B 1 68  ? 46.591  13.433  27.047  1.00 40.00 ? 67  PHE D CE1   1 
ATOM   1756 C  CE2   . PHE B 1 68  ? 46.316  15.820  26.779  1.00 37.41 ? 67  PHE D CE2   1 
ATOM   1757 C  CZ    . PHE B 1 68  ? 46.920  14.726  27.435  1.00 36.95 ? 67  PHE D CZ    1 
ATOM   1758 N  N     . THR B 1 69  ? 42.389  12.099  26.753  1.00 39.57 ? 68  THR D N     1 
ATOM   1759 C  CA    . THR B 1 69  ? 42.437  10.802  27.432  1.00 39.69 ? 68  THR D CA    1 
ATOM   1760 C  C     . THR B 1 69  ? 41.107  10.071  27.384  1.00 45.87 ? 68  THR D C     1 
ATOM   1761 O  O     . THR B 1 69  ? 41.097  8.846   27.237  1.00 44.60 ? 68  THR D O     1 
ATOM   1762 C  CB    . THR B 1 69  ? 42.882  10.903  28.911  1.00 43.66 ? 68  THR D CB    1 
ATOM   1763 O  OG1   . THR B 1 69  ? 41.916  11.643  29.677  1.00 45.05 ? 68  THR D OG1   1 
ATOM   1764 C  CG2   . THR B 1 69  ? 44.291  11.536  29.038  1.00 40.70 ? 68  THR D CG2   1 
ATOM   1765 N  N     . ARG B 1 70  ? 39.990  10.809  27.450  1.00 43.99 ? 69  ARG D N     1 
ATOM   1766 C  CA    . ARG B 1 70  ? 38.658  10.222  27.388  1.00 42.92 ? 69  ARG D CA    1 
ATOM   1767 C  C     . ARG B 1 70  ? 37.897  10.655  26.151  1.00 44.09 ? 69  ARG D C     1 
ATOM   1768 O  O     . ARG B 1 70  ? 36.958  9.958   25.753  1.00 47.95 ? 69  ARG D O     1 
ATOM   1769 C  CB    . ARG B 1 70  ? 37.839  10.607  28.630  1.00 41.89 ? 69  ARG D CB    1 
ATOM   1770 C  CG    . ARG B 1 70  ? 38.549  10.266  29.991  1.00 49.87 ? 69  ARG D CG    1 
ATOM   1771 C  CD    . ARG B 1 70  ? 37.500  10.161  31.120  1.00 53.71 ? 69  ARG D CD    1 
ATOM   1772 N  NE    . ARG B 1 70  ? 38.034  9.863   32.442  1.00 53.26 ? 69  ARG D NE    1 
ATOM   1773 C  CZ    . ARG B 1 70  ? 37.723  10.512  33.561  1.00 52.92 ? 69  ARG D CZ    1 
ATOM   1774 N  NH1   . ARG B 1 70  ? 36.823  11.477  33.573  1.00 50.54 ? 69  ARG D NH1   1 
ATOM   1775 N  NH2   . ARG B 1 70  ? 38.354  10.195  34.698  1.00 55.12 ? 69  ARG D NH2   1 
ATOM   1776 N  N     . HIS B 1 71  ? 38.276  11.783  25.543  1.00 40.23 ? 70  HIS D N     1 
ATOM   1777 C  CA    . HIS B 1 71  ? 37.557  12.341  24.396  1.00 46.12 ? 70  HIS D CA    1 
ATOM   1778 C  C     . HIS B 1 71  ? 36.059  12.500  24.674  1.00 44.19 ? 70  HIS D C     1 
ATOM   1779 O  O     . HIS B 1 71  ? 35.231  12.271  23.795  1.00 43.01 ? 70  HIS D O     1 
ATOM   1780 C  CB    . HIS B 1 71  ? 37.768  11.475  23.155  1.00 44.62 ? 70  HIS D CB    1 
ATOM   1781 C  CG    . HIS B 1 71  ? 39.210  11.227  22.851  1.00 46.78 ? 70  HIS D CG    1 
ATOM   1782 N  ND1   . HIS B 1 71  ? 39.947  12.034  22.009  1.00 46.18 ? 70  HIS D ND1   1 
ATOM   1783 C  CD2   . HIS B 1 71  ? 40.053  10.259  23.278  1.00 46.92 ? 70  HIS D CD2   1 
ATOM   1784 C  CE1   . HIS B 1 71  ? 41.183  11.575  21.930  1.00 42.83 ? 70  HIS D CE1   1 
ATOM   1785 N  NE2   . HIS B 1 71  ? 41.276  10.506  22.700  1.00 49.64 ? 70  HIS D NE2   1 
ATOM   1786 N  N     . ASN B 1 72  ? 35.698  12.866  25.917  1.00 39.26 ? 71  ASN D N     1 
ATOM   1787 C  CA    . ASN B 1 72  ? 34.290  13.128  26.186  1.00 43.68 ? 71  ASN D CA    1 
ATOM   1788 C  C     . ASN B 1 72  ? 34.044  14.347  27.070  1.00 42.52 ? 71  ASN D C     1 
ATOM   1789 O  O     . ASN B 1 72  ? 32.923  14.512  27.561  1.00 41.52 ? 71  ASN D O     1 
ATOM   1790 C  CB    . ASN B 1 72  ? 33.609  11.924  26.838  1.00 44.75 ? 71  ASN D CB    1 
ATOM   1791 C  CG    . ASN B 1 72  ? 34.269  11.520  28.152  1.00 46.94 ? 71  ASN D CG    1 
ATOM   1792 O  OD1   . ASN B 1 72  ? 34.915  12.336  28.825  1.00 45.11 ? 71  ASN D OD1   1 
ATOM   1793 N  ND2   . ASN B 1 72  ? 34.045  10.281  28.564  1.00 47.18 ? 71  ASN D ND2   1 
ATOM   1794 N  N     . GLY B 1 73  ? 35.053  15.176  27.351  1.00 39.75 ? 72  GLY D N     1 
ATOM   1795 C  CA    . GLY B 1 73  ? 34.843  16.383  28.127  1.00 34.08 ? 72  GLY D CA    1 
ATOM   1796 C  C     . GLY B 1 73  ? 35.156  16.271  29.598  1.00 37.23 ? 72  GLY D C     1 
ATOM   1797 O  O     . GLY B 1 73  ? 35.094  17.287  30.295  1.00 34.48 ? 72  GLY D O     1 
ATOM   1798 N  N     . THR B 1 74  ? 35.469  15.070  30.109  1.00 34.53 ? 73  THR D N     1 
ATOM   1799 C  CA    . THR B 1 74  ? 35.801  14.893  31.521  1.00 41.06 ? 73  THR D CA    1 
ATOM   1800 C  C     . THR B 1 74  ? 37.265  14.573  31.766  1.00 38.92 ? 73  THR D C     1 
ATOM   1801 O  O     . THR B 1 74  ? 37.684  14.495  32.922  1.00 38.64 ? 73  THR D O     1 
ATOM   1802 C  CB    . THR B 1 74  ? 34.936  13.763  32.140  1.00 42.16 ? 73  THR D CB    1 
ATOM   1803 O  OG1   . THR B 1 74  ? 35.322  12.489  31.597  1.00 46.14 ? 73  THR D OG1   1 
ATOM   1804 C  CG2   . THR B 1 74  ? 33.458  13.973  31.828  1.00 41.30 ? 73  THR D CG2   1 
ATOM   1805 N  N     . GLY B 1 75  ? 38.056  14.349  30.729  1.00 40.22 ? 74  GLY D N     1 
ATOM   1806 C  CA    . GLY B 1 75  ? 39.396  13.876  30.999  1.00 39.10 ? 74  GLY D CA    1 
ATOM   1807 C  C     . GLY B 1 75  ? 40.492  14.883  30.693  1.00 37.19 ? 74  GLY D C     1 
ATOM   1808 O  O     . GLY B 1 75  ? 40.308  16.107  30.768  1.00 36.95 ? 74  GLY D O     1 
ATOM   1809 N  N     . GLY B 1 76  ? 41.651  14.352  30.346  1.00 36.12 ? 75  GLY D N     1 
ATOM   1810 C  CA    . GLY B 1 76  ? 42.827  15.156  30.124  1.00 37.39 ? 75  GLY D CA    1 
ATOM   1811 C  C     . GLY B 1 76  ? 43.817  15.021  31.261  1.00 38.28 ? 75  GLY D C     1 
ATOM   1812 O  O     . GLY B 1 76  ? 43.496  14.568  32.362  1.00 41.95 ? 75  GLY D O     1 
ATOM   1813 N  N     . LYS B 1 77  ? 45.053  15.421  30.986  1.00 38.25 ? 76  LYS D N     1 
ATOM   1814 C  CA    . LYS B 1 77  ? 46.093  15.337  32.005  1.00 36.72 ? 76  LYS D CA    1 
ATOM   1815 C  C     . LYS B 1 77  ? 47.225  16.255  31.594  1.00 38.45 ? 76  LYS D C     1 
ATOM   1816 O  O     . LYS B 1 77  ? 47.404  16.552  30.409  1.00 37.75 ? 76  LYS D O     1 
ATOM   1817 C  CB    . LYS B 1 77  ? 46.616  13.909  32.174  1.00 40.74 ? 76  LYS D CB    1 
ATOM   1818 C  CG    . LYS B 1 77  ? 47.226  13.274  30.905  1.00 42.80 ? 76  LYS D CG    1 
ATOM   1819 C  CD    . LYS B 1 77  ? 47.972  11.958  31.215  1.00 45.46 ? 76  LYS D CD    1 
ATOM   1820 C  CE    . LYS B 1 77  ? 48.082  11.060  29.976  1.00 43.55 ? 76  LYS D CE    1 
ATOM   1821 N  NZ    . LYS B 1 77  ? 49.004  9.901   30.214  1.00 51.07 ? 76  LYS D NZ    1 
ATOM   1822 N  N     . SER B 1 78  ? 48.015  16.683  32.570  1.00 39.50 ? 77  SER D N     1 
ATOM   1823 C  CA    . SER B 1 78  ? 49.118  17.583  32.260  1.00 40.62 ? 77  SER D CA    1 
ATOM   1824 C  C     . SER B 1 78  ? 50.400  16.780  32.087  1.00 42.37 ? 77  SER D C     1 
ATOM   1825 O  O     . SER B 1 78  ? 50.436  15.573  32.320  1.00 42.07 ? 77  SER D O     1 
ATOM   1826 C  CB    . SER B 1 78  ? 49.274  18.642  33.350  1.00 38.42 ? 77  SER D CB    1 
ATOM   1827 O  OG    . SER B 1 78  ? 49.823  18.089  34.511  1.00 41.06 ? 77  SER D OG    1 
ATOM   1828 N  N     . ILE B 1 79  ? 51.467  17.460  31.655  1.00 40.21 ? 78  ILE D N     1 
ATOM   1829 C  CA    . ILE B 1 79  ? 52.763  16.787  31.632  1.00 41.92 ? 78  ILE D CA    1 
ATOM   1830 C  C     . ILE B 1 79  ? 53.316  16.587  33.041  1.00 43.59 ? 78  ILE D C     1 
ATOM   1831 O  O     . ILE B 1 79  ? 54.319  15.881  33.224  1.00 46.84 ? 78  ILE D O     1 
ATOM   1832 C  CB    . ILE B 1 79  ? 53.744  17.566  30.723  1.00 40.82 ? 78  ILE D CB    1 
ATOM   1833 C  CG1   . ILE B 1 79  ? 54.013  18.953  31.302  1.00 39.85 ? 78  ILE D CG1   1 
ATOM   1834 C  CG2   . ILE B 1 79  ? 53.176  17.680  29.266  1.00 37.71 ? 78  ILE D CG2   1 
ATOM   1835 C  CD1   . ILE B 1 79  ? 55.166  19.708  30.649  1.00 38.99 ? 78  ILE D CD1   1 
ATOM   1836 N  N     . TYR B 1 80  ? 52.676  17.169  34.053  1.00 43.75 ? 79  TYR D N     1 
ATOM   1837 C  CA    . TYR B 1 80  ? 53.134  17.089  35.444  1.00 44.33 ? 79  TYR D CA    1 
ATOM   1838 C  C     . TYR B 1 80  ? 52.373  16.051  36.244  1.00 44.82 ? 79  TYR D C     1 
ATOM   1839 O  O     . TYR B 1 80  ? 52.519  15.985  37.465  1.00 52.50 ? 79  TYR D O     1 
ATOM   1840 C  CB    . TYR B 1 80  ? 52.992  18.453  36.118  1.00 43.40 ? 79  TYR D CB    1 
ATOM   1841 C  CG    . TYR B 1 80  ? 53.537  19.590  35.295  1.00 41.64 ? 79  TYR D CG    1 
ATOM   1842 C  CD1   . TYR B 1 80  ? 54.900  19.680  35.033  1.00 41.95 ? 79  TYR D CD1   1 
ATOM   1843 C  CD2   . TYR B 1 80  ? 52.681  20.547  34.742  1.00 38.81 ? 79  TYR D CD2   1 
ATOM   1844 C  CE1   . TYR B 1 80  ? 55.413  20.713  34.270  1.00 42.19 ? 79  TYR D CE1   1 
ATOM   1845 C  CE2   . TYR B 1 80  ? 53.187  21.595  33.963  1.00 39.07 ? 79  TYR D CE2   1 
ATOM   1846 C  CZ    . TYR B 1 80  ? 54.573  21.674  33.758  1.00 40.60 ? 79  TYR D CZ    1 
ATOM   1847 O  OH    . TYR B 1 80  ? 55.104  22.681  32.978  1.00 39.64 ? 79  TYR D OH    1 
ATOM   1848 N  N     . GLY B 1 81  ? 51.531  15.265  35.602  1.00 47.55 ? 80  GLY D N     1 
ATOM   1849 C  CA    . GLY B 1 81  ? 50.777  14.289  36.352  1.00 51.89 ? 80  GLY D CA    1 
ATOM   1850 C  C     . GLY B 1 81  ? 49.321  14.559  36.104  1.00 49.40 ? 80  GLY D C     1 
ATOM   1851 O  O     . GLY B 1 81  ? 48.978  15.216  35.111  1.00 47.88 ? 80  GLY D O     1 
ATOM   1852 N  N     . GLU B 1 82  ? 48.464  14.104  37.006  1.00 52.48 ? 81  GLU D N     1 
ATOM   1853 C  CA    . GLU B 1 82  ? 47.029  14.241  36.818  1.00 53.35 ? 81  GLU D CA    1 
ATOM   1854 C  C     . GLU B 1 82  ? 46.682  15.716  36.631  1.00 49.51 ? 81  GLU D C     1 
ATOM   1855 O  O     . GLU B 1 82  ? 46.335  16.147  35.521  1.00 49.34 ? 81  GLU D O     1 
ATOM   1856 C  CB    . GLU B 1 82  ? 46.277  13.642  38.008  1.00 59.49 ? 81  GLU D CB    1 
ATOM   1857 C  CG    . GLU B 1 82  ? 44.764  13.730  37.879  1.00 63.42 ? 81  GLU D CG    1 
ATOM   1858 C  CD    . GLU B 1 82  ? 44.096  12.357  37.843  1.00 70.49 ? 81  GLU D CD    1 
ATOM   1859 O  OE1   . GLU B 1 82  ? 44.815  11.339  37.980  1.00 70.02 ? 81  GLU D OE1   1 
ATOM   1860 O  OE2   . GLU B 1 82  ? 42.853  12.297  37.655  1.00 74.22 ? 81  GLU D OE2   1 
ATOM   1861 N  N     . LYS B 1 83  ? 46.749  16.486  37.711  1.00 44.27 ? 82  LYS D N     1 
ATOM   1862 C  CA    . LYS B 1 83  ? 46.454  17.914  37.734  1.00 44.04 ? 82  LYS D CA    1 
ATOM   1863 C  C     . LYS B 1 83  ? 47.662  18.690  38.269  1.00 41.77 ? 82  LYS D C     1 
ATOM   1864 O  O     . LYS B 1 83  ? 48.613  18.110  38.814  1.00 40.26 ? 82  LYS D O     1 
ATOM   1865 C  CB    . LYS B 1 83  ? 45.204  18.205  38.587  1.00 45.63 ? 82  LYS D CB    1 
ATOM   1866 C  CG    . LYS B 1 83  ? 44.187  17.037  38.589  1.00 54.99 ? 82  LYS D CG    1 
ATOM   1867 C  CD    . LYS B 1 83  ? 42.961  17.199  39.531  1.00 55.29 ? 82  LYS D CD    1 
ATOM   1868 C  CE    . LYS B 1 83  ? 41.823  16.207  39.160  1.00 58.75 ? 82  LYS D CE    1 
ATOM   1869 N  NZ    . LYS B 1 83  ? 40.755  16.824  38.280  1.00 58.24 ? 82  LYS D NZ    1 
ATOM   1870 N  N     . PHE B 1 84  ? 47.620  20.021  38.114  1.00 39.02 ? 83  PHE D N     1 
ATOM   1871 C  CA    . PHE B 1 84  ? 48.612  20.903  38.726  1.00 37.50 ? 83  PHE D CA    1 
ATOM   1872 C  C     . PHE B 1 84  ? 47.937  22.188  39.201  1.00 37.85 ? 83  PHE D C     1 
ATOM   1873 O  O     . PHE B 1 84  ? 46.789  22.473  38.852  1.00 36.09 ? 83  PHE D O     1 
ATOM   1874 C  CB    . PHE B 1 84  ? 49.805  21.184  37.783  1.00 36.42 ? 83  PHE D CB    1 
ATOM   1875 C  CG    . PHE B 1 84  ? 49.466  21.965  36.553  1.00 37.00 ? 83  PHE D CG    1 
ATOM   1876 C  CD1   . PHE B 1 84  ? 48.937  21.325  35.442  1.00 36.66 ? 83  PHE D CD1   1 
ATOM   1877 C  CD2   . PHE B 1 84  ? 49.772  23.320  36.468  1.00 38.37 ? 83  PHE D CD2   1 
ATOM   1878 C  CE1   . PHE B 1 84  ? 48.640  22.032  34.278  1.00 30.56 ? 83  PHE D CE1   1 
ATOM   1879 C  CE2   . PHE B 1 84  ? 49.489  24.040  35.306  1.00 34.77 ? 83  PHE D CE2   1 
ATOM   1880 C  CZ    . PHE B 1 84  ? 48.908  23.381  34.206  1.00 30.44 ? 83  PHE D CZ    1 
ATOM   1881 N  N     . GLU B 1 85  ? 48.646  22.932  40.064  1.00 37.13 ? 84  GLU D N     1 
ATOM   1882 C  CA    . GLU B 1 85  ? 48.079  24.091  40.760  1.00 35.53 ? 84  GLU D CA    1 
ATOM   1883 C  C     . GLU B 1 85  ? 47.847  25.270  39.797  1.00 32.73 ? 84  GLU D C     1 
ATOM   1884 O  O     . GLU B 1 85  ? 48.491  25.400  38.755  1.00 33.84 ? 84  GLU D O     1 
ATOM   1885 C  CB    . GLU B 1 85  ? 49.018  24.557  41.883  1.00 39.14 ? 84  GLU D CB    1 
ATOM   1886 C  CG    . GLU B 1 85  ? 50.356  24.991  41.320  1.00 42.09 ? 84  GLU D CG    1 
ATOM   1887 C  CD    . GLU B 1 85  ? 51.254  23.837  40.783  1.00 50.29 ? 84  GLU D CD    1 
ATOM   1888 O  OE1   . GLU B 1 85  ? 52.323  24.144  40.208  1.00 48.30 ? 84  GLU D OE1   1 
ATOM   1889 O  OE2   . GLU B 1 85  ? 50.970  22.632  41.055  1.00 53.95 ? 84  GLU D OE2   1 
ATOM   1890 N  N     . ASP B 1 86  ? 46.924  26.157  40.176  1.00 30.99 ? 85  ASP D N     1 
ATOM   1891 C  CA    . ASP B 1 86  ? 46.777  27.437  39.500  1.00 34.57 ? 85  ASP D CA    1 
ATOM   1892 C  C     . ASP B 1 86  ? 48.071  28.230  39.667  1.00 34.65 ? 85  ASP D C     1 
ATOM   1893 O  O     . ASP B 1 86  ? 48.487  28.525  40.787  1.00 36.43 ? 85  ASP D O     1 
ATOM   1894 C  CB    . ASP B 1 86  ? 45.598  28.231  40.070  1.00 35.15 ? 85  ASP D CB    1 
ATOM   1895 C  CG    . ASP B 1 86  ? 44.231  27.516  39.906  1.00 33.51 ? 85  ASP D CG    1 
ATOM   1896 O  OD1   . ASP B 1 86  ? 43.958  27.033  38.820  1.00 32.59 ? 85  ASP D OD1   1 
ATOM   1897 O  OD2   . ASP B 1 86  ? 43.427  27.457  40.890  1.00 33.67 ? 85  ASP D OD2   1 
ATOM   1898 N  N     . GLU B 1 87  ? 48.734  28.535  38.564  1.00 33.87 ? 86  GLU D N     1 
ATOM   1899 C  CA    . GLU B 1 87  ? 50.061  29.123  38.708  1.00 30.92 ? 86  GLU D CA    1 
ATOM   1900 C  C     . GLU B 1 87  ? 49.959  30.564  39.199  1.00 33.17 ? 86  GLU D C     1 
ATOM   1901 O  O     . GLU B 1 87  ? 50.737  30.983  40.062  1.00 32.46 ? 86  GLU D O     1 
ATOM   1902 C  CB    . GLU B 1 87  ? 50.813  29.017  37.378  1.00 30.47 ? 86  GLU D CB    1 
ATOM   1903 C  CG    . GLU B 1 87  ? 52.260  29.525  37.384  1.00 29.28 ? 86  GLU D CG    1 
ATOM   1904 C  CD    . GLU B 1 87  ? 52.964  29.173  36.081  1.00 32.84 ? 86  GLU D CD    1 
ATOM   1905 O  OE1   . GLU B 1 87  ? 52.274  28.779  35.085  1.00 34.23 ? 86  GLU D OE1   1 
ATOM   1906 O  OE2   . GLU B 1 87  ? 54.208  29.256  36.077  1.00 32.73 ? 86  GLU D OE2   1 
ATOM   1907 N  N     . ASN B 1 88  ? 49.048  31.348  38.624  1.00 31.76 ? 87  ASN D N     1 
ATOM   1908 C  CA    . ASN B 1 88  ? 48.712  32.676  39.141  1.00 30.41 ? 87  ASN D CA    1 
ATOM   1909 C  C     . ASN B 1 88  ? 47.527  33.175  38.328  1.00 29.83 ? 87  ASN D C     1 
ATOM   1910 O  O     . ASN B 1 88  ? 47.126  32.556  37.322  1.00 30.11 ? 87  ASN D O     1 
ATOM   1911 C  CB    . ASN B 1 88  ? 49.909  33.670  39.065  1.00 30.34 ? 87  ASN D CB    1 
ATOM   1912 C  CG    . ASN B 1 88  ? 50.395  33.866  37.630  1.00 30.97 ? 87  ASN D CG    1 
ATOM   1913 O  OD1   . ASN B 1 88  ? 49.621  34.279  36.769  1.00 31.22 ? 87  ASN D OD1   1 
ATOM   1914 N  ND2   . ASN B 1 88  ? 51.686  33.577  37.364  1.00 30.74 ? 87  ASN D ND2   1 
ATOM   1915 N  N     . PHE B 1 89  ? 47.006  34.336  38.716  1.00 28.42 ? 88  PHE D N     1 
ATOM   1916 C  CA    . PHE B 1 89  ? 45.915  34.949  37.946  1.00 27.27 ? 88  PHE D CA    1 
ATOM   1917 C  C     . PHE B 1 89  ? 46.295  36.336  37.453  1.00 31.47 ? 88  PHE D C     1 
ATOM   1918 O  O     . PHE B 1 89  ? 45.466  37.262  37.434  1.00 28.64 ? 88  PHE D O     1 
ATOM   1919 C  CB    . PHE B 1 89  ? 44.627  35.006  38.773  1.00 31.90 ? 88  PHE D CB    1 
ATOM   1920 C  CG    . PHE B 1 89  ? 44.198  33.681  39.236  1.00 28.14 ? 88  PHE D CG    1 
ATOM   1921 C  CD1   . PHE B 1 89  ? 43.601  32.802  38.321  1.00 31.11 ? 88  PHE D CD1   1 
ATOM   1922 C  CD2   . PHE B 1 89  ? 44.404  33.271  40.539  1.00 29.80 ? 88  PHE D CD2   1 
ATOM   1923 C  CE1   . PHE B 1 89  ? 43.207  31.545  38.725  1.00 30.61 ? 88  PHE D CE1   1 
ATOM   1924 C  CE2   . PHE B 1 89  ? 44.019  32.005  40.969  1.00 31.38 ? 88  PHE D CE2   1 
ATOM   1925 C  CZ    . PHE B 1 89  ? 43.401  31.126  40.018  1.00 31.14 ? 88  PHE D CZ    1 
ATOM   1926 N  N     . ILE B 1 90  ? 47.570  36.498  37.055  1.00 27.78 ? 89  ILE D N     1 
ATOM   1927 C  CA    . ILE B 1 90  ? 48.019  37.807  36.618  1.00 31.27 ? 89  ILE D CA    1 
ATOM   1928 C  C     . ILE B 1 90  ? 47.201  38.272  35.424  1.00 27.24 ? 89  ILE D C     1 
ATOM   1929 O  O     . ILE B 1 90  ? 46.729  39.418  35.388  1.00 29.74 ? 89  ILE D O     1 
ATOM   1930 C  CB    . ILE B 1 90  ? 49.520  37.780  36.300  1.00 28.56 ? 89  ILE D CB    1 
ATOM   1931 C  CG1   . ILE B 1 90  ? 50.323  37.673  37.594  1.00 30.37 ? 89  ILE D CG1   1 
ATOM   1932 C  CG2   . ILE B 1 90  ? 49.943  39.049  35.542  1.00 32.17 ? 89  ILE D CG2   1 
ATOM   1933 C  CD1   . ILE B 1 90  ? 51.777  37.258  37.313  1.00 32.00 ? 89  ILE D CD1   1 
ATOM   1934 N  N     . LEU B 1 91  ? 47.001  37.390  34.446  1.00 27.08 ? 90  LEU D N     1 
ATOM   1935 C  CA    . LEU B 1 91  ? 46.359  37.751  33.188  1.00 25.89 ? 90  LEU D CA    1 
ATOM   1936 C  C     . LEU B 1 91  ? 44.849  37.517  33.266  1.00 26.27 ? 90  LEU D C     1 
ATOM   1937 O  O     . LEU B 1 91  ? 44.381  36.595  33.944  1.00 28.36 ? 90  LEU D O     1 
ATOM   1938 C  CB    . LEU B 1 91  ? 46.950  36.925  32.043  1.00 25.64 ? 90  LEU D CB    1 
ATOM   1939 C  CG    . LEU B 1 91  ? 48.425  37.274  31.818  1.00 27.27 ? 90  LEU D CG    1 
ATOM   1940 C  CD1   . LEU B 1 91  ? 49.048  36.281  30.783  1.00 30.47 ? 90  LEU D CD1   1 
ATOM   1941 C  CD2   . LEU B 1 91  ? 48.604  38.739  31.432  1.00 31.19 ? 90  LEU D CD2   1 
ATOM   1942 N  N     . LYS B 1 92  ? 44.095  38.357  32.550  1.00 26.81 ? 91  LYS D N     1 
ATOM   1943 C  CA    . LYS B 1 92  ? 42.636  38.403  32.673  1.00 26.91 ? 91  LYS D CA    1 
ATOM   1944 C  C     . LYS B 1 92  ? 41.974  38.050  31.340  1.00 27.28 ? 91  LYS D C     1 
ATOM   1945 O  O     . LYS B 1 92  ? 42.597  38.062  30.264  1.00 24.95 ? 91  LYS D O     1 
ATOM   1946 C  CB    . LYS B 1 92  ? 42.196  39.804  33.128  1.00 27.39 ? 91  LYS D CB    1 
ATOM   1947 C  CG    . LYS B 1 92  ? 42.651  40.225  34.557  1.00 29.14 ? 91  LYS D CG    1 
ATOM   1948 C  CD    . LYS B 1 92  ? 42.627  39.097  35.635  1.00 31.12 ? 91  LYS D CD    1 
ATOM   1949 C  CE    . LYS B 1 92  ? 43.442  39.572  36.923  1.00 35.50 ? 91  LYS D CE    1 
ATOM   1950 N  NZ    . LYS B 1 92  ? 43.206  38.712  38.162  1.00 38.07 ? 91  LYS D NZ    1 
ATOM   1951 N  N     . HIS B 1 93  ? 40.680  37.711  31.421  1.00 27.26 ? 92  HIS D N     1 
ATOM   1952 C  CA    . HIS B 1 93  ? 39.913  37.344  30.220  1.00 25.93 ? 92  HIS D CA    1 
ATOM   1953 C  C     . HIS B 1 93  ? 39.390  38.618  29.552  1.00 28.28 ? 92  HIS D C     1 
ATOM   1954 O  O     . HIS B 1 93  ? 38.225  38.978  29.672  1.00 30.31 ? 92  HIS D O     1 
ATOM   1955 C  CB    . HIS B 1 93  ? 38.777  36.408  30.614  1.00 25.19 ? 92  HIS D CB    1 
ATOM   1956 C  CG    . HIS B 1 93  ? 39.261  35.190  31.323  1.00 23.46 ? 92  HIS D CG    1 
ATOM   1957 N  ND1   . HIS B 1 93  ? 39.544  35.179  32.679  1.00 25.38 ? 92  HIS D ND1   1 
ATOM   1958 C  CD2   . HIS B 1 93  ? 39.557  33.952  30.864  1.00 22.23 ? 92  HIS D CD2   1 
ATOM   1959 C  CE1   . HIS B 1 93  ? 39.969  33.976  33.024  1.00 24.37 ? 92  HIS D CE1   1 
ATOM   1960 N  NE2   . HIS B 1 93  ? 39.991  33.215  31.944  1.00 24.14 ? 92  HIS D NE2   1 
ATOM   1961 N  N     . THR B 1 94  ? 40.277  39.338  28.856  1.00 27.74 ? 93  THR D N     1 
ATOM   1962 C  CA    . THR B 1 94  ? 39.946  40.697  28.440  1.00 29.81 ? 93  THR D CA    1 
ATOM   1963 C  C     . THR B 1 94  ? 39.176  40.796  27.133  1.00 31.22 ? 93  THR D C     1 
ATOM   1964 O  O     . THR B 1 94  ? 38.666  41.873  26.812  1.00 32.91 ? 93  THR D O     1 
ATOM   1965 C  CB    . THR B 1 94  ? 41.221  41.513  28.302  1.00 29.77 ? 93  THR D CB    1 
ATOM   1966 O  OG1   . THR B 1 94  ? 42.127  40.795  27.442  1.00 28.81 ? 93  THR D OG1   1 
ATOM   1967 C  CG2   . THR B 1 94  ? 41.826  41.730  29.664  1.00 35.22 ? 93  THR D CG2   1 
ATOM   1968 N  N     . GLY B 1 95  ? 39.078  39.726  26.361  1.00 28.00 ? 94  GLY D N     1 
ATOM   1969 C  CA    . GLY B 1 95  ? 38.431  39.814  25.073  1.00 29.33 ? 94  GLY D CA    1 
ATOM   1970 C  C     . GLY B 1 95  ? 38.639  38.575  24.228  1.00 25.21 ? 94  GLY D C     1 
ATOM   1971 O  O     . GLY B 1 95  ? 39.214  37.574  24.670  1.00 25.08 ? 94  GLY D O     1 
ATOM   1972 N  N     . PRO B 1 96  ? 38.208  38.646  22.967  1.00 26.84 ? 95  PRO D N     1 
ATOM   1973 C  CA    . PRO B 1 96  ? 38.323  37.499  22.070  1.00 24.30 ? 95  PRO D CA    1 
ATOM   1974 C  C     . PRO B 1 96  ? 39.780  37.112  21.873  1.00 25.00 ? 95  PRO D C     1 
ATOM   1975 O  O     . PRO B 1 96  ? 40.664  37.965  21.797  1.00 29.93 ? 95  PRO D O     1 
ATOM   1976 C  CB    . PRO B 1 96  ? 37.720  38.011  20.753  1.00 23.60 ? 95  PRO D CB    1 
ATOM   1977 C  CG    . PRO B 1 96  ? 36.968  39.234  21.096  1.00 29.64 ? 95  PRO D CG    1 
ATOM   1978 C  CD    . PRO B 1 96  ? 37.642  39.826  22.303  1.00 30.11 ? 95  PRO D CD    1 
ATOM   1979 N  N     . GLY B 1 97  ? 40.019  35.833  21.767  1.00 21.98 ? 96  GLY D N     1 
ATOM   1980 C  CA    . GLY B 1 97  ? 41.357  35.336  21.539  1.00 22.41 ? 96  GLY D CA    1 
ATOM   1981 C  C     . GLY B 1 97  ? 42.089  34.862  22.772  1.00 25.81 ? 96  GLY D C     1 
ATOM   1982 O  O     . GLY B 1 97  ? 43.071  34.135  22.637  1.00 21.67 ? 96  GLY D O     1 
ATOM   1983 N  N     . ILE B 1 98  ? 41.611  35.210  23.973  1.00 22.63 ? 97  ILE D N     1 
ATOM   1984 C  CA    . ILE B 1 98  ? 42.306  34.784  25.183  1.00 23.06 ? 97  ILE D CA    1 
ATOM   1985 C  C     . ILE B 1 98  ? 42.279  33.272  25.303  1.00 20.62 ? 97  ILE D C     1 
ATOM   1986 O  O     . ILE B 1 98  ? 41.233  32.627  25.128  1.00 21.93 ? 97  ILE D O     1 
ATOM   1987 C  CB    . ILE B 1 98  ? 41.650  35.426  26.409  1.00 22.18 ? 97  ILE D CB    1 
ATOM   1988 C  CG1   . ILE B 1 98  ? 41.965  36.940  26.424  1.00 26.86 ? 97  ILE D CG1   1 
ATOM   1989 C  CG2   . ILE B 1 98  ? 42.040  34.618  27.659  1.00 21.01 ? 97  ILE D CG2   1 
ATOM   1990 C  CD1   . ILE B 1 98  ? 43.439  37.342  26.661  1.00 27.66 ? 97  ILE D CD1   1 
ATOM   1991 N  N     . LEU B 1 99  ? 43.444  32.693  25.617  1.00 22.29 ? 98  LEU D N     1 
ATOM   1992 C  CA    . LEU B 1 99  ? 43.580  31.257  25.831  1.00 20.89 ? 98  LEU D CA    1 
ATOM   1993 C  C     . LEU B 1 99  ? 43.754  31.026  27.327  1.00 20.91 ? 98  LEU D C     1 
ATOM   1994 O  O     . LEU B 1 99  ? 44.665  31.606  27.949  1.00 22.60 ? 98  LEU D O     1 
ATOM   1995 C  CB    . LEU B 1 99  ? 44.764  30.712  25.032  1.00 21.20 ? 98  LEU D CB    1 
ATOM   1996 C  CG    . LEU B 1 99  ? 45.187  29.238  25.199  1.00 22.40 ? 98  LEU D CG    1 
ATOM   1997 C  CD1   . LEU B 1 99  ? 44.158  28.262  24.633  1.00 22.66 ? 98  LEU D CD1   1 
ATOM   1998 C  CD2   . LEU B 1 99  ? 46.472  29.066  24.436  1.00 22.90 ? 98  LEU D CD2   1 
ATOM   1999 N  N     . SER B 1 100 ? 42.885  30.199  27.904  1.00 20.98 ? 99  SER D N     1 
ATOM   2000 C  CA    . SER B 1 100 ? 42.869  30.053  29.362  1.00 22.09 ? 99  SER D CA    1 
ATOM   2001 C  C     . SER B 1 100 ? 42.616  28.595  29.750  1.00 23.46 ? 99  SER D C     1 
ATOM   2002 O  O     . SER B 1 100 ? 42.140  27.783  28.937  1.00 23.43 ? 99  SER D O     1 
ATOM   2003 C  CB    . SER B 1 100 ? 41.807  30.961  29.983  1.00 22.53 ? 99  SER D CB    1 
ATOM   2004 O  OG    . SER B 1 100 ? 41.782  30.754  31.413  1.00 23.32 ? 99  SER D OG    1 
ATOM   2005 N  N     . MET B 1 101 ? 42.900  28.238  31.009  1.00 22.20 ? 100 MET D N     1 
ATOM   2006 C  CA    . MET B 1 101 ? 42.792  26.822  31.366  1.00 21.80 ? 100 MET D CA    1 
ATOM   2007 C  C     . MET B 1 101 ? 41.400  26.508  31.898  1.00 25.70 ? 100 MET D C     1 
ATOM   2008 O  O     . MET B 1 101 ? 40.895  27.216  32.770  1.00 25.36 ? 100 MET D O     1 
ATOM   2009 C  CB    . MET B 1 101 ? 43.800  26.444  32.462  1.00 25.04 ? 100 MET D CB    1 
ATOM   2010 C  CG    . MET B 1 101 ? 45.262  26.348  31.964  1.00 23.72 ? 100 MET D CG    1 
ATOM   2011 S  SD    . MET B 1 101 ? 45.517  25.121  30.713  1.00 28.30 ? 100 MET D SD    1 
ATOM   2012 C  CE    . MET B 1 101 ? 45.793  23.613  31.720  1.00 29.83 ? 100 MET D CE    1 
ATOM   2013 N  N     . ALA B 1 102 ? 40.816  25.390  31.445  1.00 25.56 ? 101 ALA D N     1 
ATOM   2014 C  CA    . ALA B 1 102 ? 39.605  24.905  32.080  1.00 24.22 ? 101 ALA D CA    1 
ATOM   2015 C  C     . ALA B 1 102 ? 39.963  24.228  33.397  1.00 28.14 ? 101 ALA D C     1 
ATOM   2016 O  O     . ALA B 1 102 ? 41.101  23.802  33.602  1.00 25.59 ? 101 ALA D O     1 
ATOM   2017 C  CB    . ALA B 1 102 ? 38.848  23.928  31.155  1.00 24.54 ? 101 ALA D CB    1 
ATOM   2018 N  N     . ASN B 1 103 ? 38.984  24.138  34.295  1.00 26.68 ? 102 ASN D N     1 
ATOM   2019 C  CA    . ASN B 1 103 ? 39.244  23.454  35.564  1.00 29.63 ? 102 ASN D CA    1 
ATOM   2020 C  C     . ASN B 1 103 ? 37.946  23.015  36.206  1.00 34.19 ? 102 ASN D C     1 
ATOM   2021 O  O     . ASN B 1 103 ? 36.847  23.341  35.757  1.00 32.12 ? 102 ASN D O     1 
ATOM   2022 C  CB    . ASN B 1 103 ? 40.074  24.299  36.574  1.00 32.10 ? 102 ASN D CB    1 
ATOM   2023 C  CG    . ASN B 1 103 ? 39.334  25.531  37.086  1.00 32.76 ? 102 ASN D CG    1 
ATOM   2024 O  OD1   . ASN B 1 103 ? 38.174  25.452  37.509  1.00 32.15 ? 102 ASN D OD1   1 
ATOM   2025 N  ND2   . ASN B 1 103 ? 39.996  26.701  37.012  1.00 29.02 ? 102 ASN D ND2   1 
ATOM   2026 N  N     . ALA B 1 104 ? 38.107  22.226  37.246  1.00 34.35 ? 103 ALA D N     1 
ATOM   2027 C  CA    . ALA B 1 104 ? 36.976  21.768  38.042  1.00 36.31 ? 103 ALA D CA    1 
ATOM   2028 C  C     . ALA B 1 104 ? 37.133  22.207  39.497  1.00 39.33 ? 103 ALA D C     1 
ATOM   2029 O  O     . ALA B 1 104 ? 36.896  21.416  40.423  1.00 40.20 ? 103 ALA D O     1 
ATOM   2030 C  CB    . ALA B 1 104 ? 36.843  20.246  37.908  1.00 36.35 ? 103 ALA D CB    1 
ATOM   2031 N  N     . GLY B 1 105 ? 37.511  23.476  39.715  1.00 35.83 ? 104 GLY D N     1 
ATOM   2032 C  CA    . GLY B 1 105 ? 37.828  23.971  41.047  1.00 36.21 ? 104 GLY D CA    1 
ATOM   2033 C  C     . GLY B 1 105 ? 39.289  24.408  41.139  1.00 40.07 ? 104 GLY D C     1 
ATOM   2034 O  O     . GLY B 1 105 ? 40.075  24.244  40.195  1.00 34.64 ? 104 GLY D O     1 
ATOM   2035 N  N     . PRO B 1 106 ? 39.697  24.954  42.288  1.00 38.97 ? 105 PRO D N     1 
ATOM   2036 C  CA    . PRO B 1 106 ? 41.088  25.408  42.415  1.00 35.10 ? 105 PRO D CA    1 
ATOM   2037 C  C     . PRO B 1 106 ? 42.082  24.265  42.266  1.00 36.67 ? 105 PRO D C     1 
ATOM   2038 O  O     . PRO B 1 106 ? 41.876  23.160  42.765  1.00 39.62 ? 105 PRO D O     1 
ATOM   2039 C  CB    . PRO B 1 106 ? 41.149  26.018  43.827  1.00 41.49 ? 105 PRO D CB    1 
ATOM   2040 C  CG    . PRO B 1 106 ? 39.748  26.341  44.189  1.00 40.37 ? 105 PRO D CG    1 
ATOM   2041 C  CD    . PRO B 1 106 ? 38.868  25.348  43.428  1.00 38.99 ? 105 PRO D CD    1 
ATOM   2042 N  N     . ASN B 1 107 ? 43.214  24.590  41.659  1.00 35.26 ? 106 ASN D N     1 
ATOM   2043 C  CA    . ASN B 1 107 ? 44.351  23.693  41.491  1.00 35.21 ? 106 ASN D CA    1 
ATOM   2044 C  C     . ASN B 1 107 ? 43.951  22.347  40.888  1.00 37.16 ? 106 ASN D C     1 
ATOM   2045 O  O     . ASN B 1 107 ? 44.377  21.285  41.362  1.00 40.49 ? 106 ASN D O     1 
ATOM   2046 C  CB    . ASN B 1 107 ? 45.092  23.537  42.836  1.00 39.21 ? 106 ASN D CB    1 
ATOM   2047 C  CG    . ASN B 1 107 ? 45.392  24.867  43.439  1.00 36.10 ? 106 ASN D CG    1 
ATOM   2048 O  OD1   . ASN B 1 107 ? 45.983  25.749  42.774  1.00 39.88 ? 106 ASN D OD1   1 
ATOM   2049 N  ND2   . ASN B 1 107 ? 44.943  25.069  44.669  1.00 43.91 ? 106 ASN D ND2   1 
ATOM   2050 N  N     . THR B 1 108 ? 43.158  22.394  39.801  1.00 35.95 ? 107 THR D N     1 
ATOM   2051 C  CA    . THR B 1 108 ? 42.787  21.200  39.032  1.00 36.80 ? 107 THR D CA    1 
ATOM   2052 C  C     . THR B 1 108 ? 43.075  21.396  37.551  1.00 35.44 ? 107 THR D C     1 
ATOM   2053 O  O     . THR B 1 108 ? 42.299  20.976  36.691  1.00 36.82 ? 107 THR D O     1 
ATOM   2054 C  CB    . THR B 1 108 ? 41.318  20.813  39.223  1.00 35.38 ? 107 THR D CB    1 
ATOM   2055 O  OG1   . THR B 1 108 ? 40.483  21.905  38.810  1.00 36.22 ? 107 THR D OG1   1 
ATOM   2056 C  CG2   . THR B 1 108 ? 41.012  20.416  40.665  1.00 38.02 ? 107 THR D CG2   1 
ATOM   2057 N  N     . ASN B 1 109 ? 44.186  22.049  37.198  1.00 32.85 ? 108 ASN D N     1 
ATOM   2058 C  CA    . ASN B 1 109 ? 44.492  22.169  35.781  1.00 31.68 ? 108 ASN D CA    1 
ATOM   2059 C  C     . ASN B 1 109 ? 44.988  20.841  35.235  1.00 33.64 ? 108 ASN D C     1 
ATOM   2060 O  O     . ASN B 1 109 ? 45.829  20.192  35.851  1.00 38.55 ? 108 ASN D O     1 
ATOM   2061 C  CB    . ASN B 1 109 ? 45.539  23.250  35.522  1.00 31.62 ? 108 ASN D CB    1 
ATOM   2062 C  CG    . ASN B 1 109 ? 45.119  24.582  36.049  1.00 31.84 ? 108 ASN D CG    1 
ATOM   2063 O  OD1   . ASN B 1 109 ? 44.284  25.269  35.435  1.00 31.62 ? 108 ASN D OD1   1 
ATOM   2064 N  ND2   . ASN B 1 109 ? 45.613  24.931  37.240  1.00 32.22 ? 108 ASN D ND2   1 
ATOM   2065 N  N     . GLY B 1 110 ? 44.487  20.458  34.057  1.00 31.90 ? 109 GLY D N     1 
ATOM   2066 C  CA    . GLY B 1 110 ? 45.017  19.279  33.402  1.00 33.68 ? 109 GLY D CA    1 
ATOM   2067 C  C     . GLY B 1 110 ? 45.472  19.628  32.009  1.00 29.74 ? 109 GLY D C     1 
ATOM   2068 O  O     . GLY B 1 110 ? 46.513  20.281  31.827  1.00 32.34 ? 109 GLY D O     1 
ATOM   2069 N  N     . SER B 1 111 ? 44.674  19.246  31.009  1.00 30.61 ? 110 SER D N     1 
ATOM   2070 C  CA    . SER B 1 111 ? 44.963  19.623  29.632  1.00 30.63 ? 110 SER D CA    1 
ATOM   2071 C  C     . SER B 1 111 ? 43.859  20.431  28.994  1.00 29.70 ? 110 SER D C     1 
ATOM   2072 O  O     . SER B 1 111 ? 44.115  21.119  28.002  1.00 28.05 ? 110 SER D O     1 
ATOM   2073 C  CB    . SER B 1 111 ? 45.219  18.376  28.772  1.00 30.08 ? 110 SER D CB    1 
ATOM   2074 O  OG    . SER B 1 111 ? 44.126  17.497  28.900  1.00 32.22 ? 110 SER D OG    1 
ATOM   2075 N  N     . GLN B 1 112 ? 42.652  20.396  29.537  1.00 27.44 ? 111 GLN D N     1 
ATOM   2076 C  CA    . GLN B 1 112 ? 41.568  21.109  28.889  1.00 29.91 ? 111 GLN D CA    1 
ATOM   2077 C  C     . GLN B 1 112 ? 41.788  22.610  28.973  1.00 26.52 ? 111 GLN D C     1 
ATOM   2078 O  O     . GLN B 1 112 ? 42.295  23.128  29.966  1.00 24.01 ? 111 GLN D O     1 
ATOM   2079 C  CB    . GLN B 1 112 ? 40.238  20.748  29.514  1.00 28.13 ? 111 GLN D CB    1 
ATOM   2080 C  CG    . GLN B 1 112 ? 39.789  19.341  29.200  1.00 29.97 ? 111 GLN D CG    1 
ATOM   2081 C  CD    . GLN B 1 112 ? 38.352  19.108  29.564  1.00 31.19 ? 111 GLN D CD    1 
ATOM   2082 O  OE1   . GLN B 1 112 ? 37.474  19.939  29.310  1.00 28.34 ? 111 GLN D OE1   1 
ATOM   2083 N  NE2   . GLN B 1 112 ? 38.083  17.944  30.127  1.00 33.35 ? 111 GLN D NE2   1 
ATOM   2084 N  N     . PHE B 1 113 ? 41.378  23.309  27.915  1.00 23.67 ? 112 PHE D N     1 
ATOM   2085 C  CA    . PHE B 1 113 ? 41.601  24.747  27.761  1.00 22.42 ? 112 PHE D CA    1 
ATOM   2086 C  C     . PHE B 1 113 ? 40.368  25.336  27.067  1.00 27.42 ? 112 PHE D C     1 
ATOM   2087 O  O     . PHE B 1 113 ? 39.506  24.606  26.528  1.00 24.34 ? 112 PHE D O     1 
ATOM   2088 C  CB    . PHE B 1 113 ? 42.853  25.035  26.893  1.00 23.31 ? 112 PHE D CB    1 
ATOM   2089 C  CG    . PHE B 1 113 ? 42.718  24.433  25.508  1.00 22.47 ? 112 PHE D CG    1 
ATOM   2090 C  CD1   . PHE B 1 113 ? 43.098  23.124  25.283  1.00 22.78 ? 112 PHE D CD1   1 
ATOM   2091 C  CD2   . PHE B 1 113 ? 42.099  25.148  24.465  1.00 24.67 ? 112 PHE D CD2   1 
ATOM   2092 C  CE1   . PHE B 1 113 ? 42.871  22.549  24.017  1.00 24.98 ? 112 PHE D CE1   1 
ATOM   2093 C  CE2   . PHE B 1 113 ? 41.879  24.615  23.223  1.00 24.23 ? 112 PHE D CE2   1 
ATOM   2094 C  CZ    . PHE B 1 113 ? 42.277  23.301  22.971  1.00 21.48 ? 112 PHE D CZ    1 
ATOM   2095 N  N     . PHE B 1 114 ? 40.296  26.660  27.037  1.00 21.69 ? 113 PHE D N     1 
ATOM   2096 C  CA    . PHE B 1 114 ? 39.275  27.295  26.228  1.00 21.84 ? 113 PHE D CA    1 
ATOM   2097 C  C     . PHE B 1 114 ? 39.835  28.540  25.575  1.00 21.36 ? 113 PHE D C     1 
ATOM   2098 O  O     . PHE B 1 114 ? 40.817  29.140  26.047  1.00 22.37 ? 113 PHE D O     1 
ATOM   2099 C  CB    . PHE B 1 114 ? 38.004  27.636  27.031  1.00 21.24 ? 113 PHE D CB    1 
ATOM   2100 C  CG    . PHE B 1 114 ? 38.218  28.602  28.194  1.00 22.37 ? 113 PHE D CG    1 
ATOM   2101 C  CD1   . PHE B 1 114 ? 38.835  28.163  29.394  1.00 22.59 ? 113 PHE D CD1   1 
ATOM   2102 C  CD2   . PHE B 1 114 ? 37.714  29.899  28.129  1.00 20.46 ? 113 PHE D CD2   1 
ATOM   2103 C  CE1   . PHE B 1 114 ? 38.968  29.058  30.503  1.00 24.52 ? 113 PHE D CE1   1 
ATOM   2104 C  CE2   . PHE B 1 114 ? 37.810  30.776  29.199  1.00 21.89 ? 113 PHE D CE2   1 
ATOM   2105 C  CZ    . PHE B 1 114 ? 38.451  30.376  30.375  1.00 22.13 ? 113 PHE D CZ    1 
ATOM   2106 N  N     . ILE B 1 115 ? 39.202  28.914  24.462  1.00 19.28 ? 114 ILE D N     1 
ATOM   2107 C  CA    . ILE B 1 115 ? 39.545  30.131  23.710  1.00 18.70 ? 114 ILE D CA    1 
ATOM   2108 C  C     . ILE B 1 115 ? 38.354  31.060  23.778  1.00 19.32 ? 114 ILE D C     1 
ATOM   2109 O  O     . ILE B 1 115 ? 37.252  30.684  23.335  1.00 19.89 ? 114 ILE D O     1 
ATOM   2110 C  CB    . ILE B 1 115 ? 39.839  29.785  22.248  1.00 21.41 ? 114 ILE D CB    1 
ATOM   2111 C  CG1   . ILE B 1 115 ? 40.913  28.690  22.184  1.00 24.74 ? 114 ILE D CG1   1 
ATOM   2112 C  CG2   . ILE B 1 115 ? 40.197  31.045  21.480  1.00 19.58 ? 114 ILE D CG2   1 
ATOM   2113 C  CD1   . ILE B 1 115 ? 40.992  28.055  20.753  1.00 21.99 ? 114 ILE D CD1   1 
ATOM   2114 N  N     . CYS B 1 116 ? 38.535  32.242  24.360  1.00 21.04 ? 115 CYS D N     1 
ATOM   2115 C  CA    . CYS B 1 116 ? 37.421  33.181  24.438  1.00 21.95 ? 115 CYS D CA    1 
ATOM   2116 C  C     . CYS B 1 116 ? 37.074  33.721  23.054  1.00 22.06 ? 115 CYS D C     1 
ATOM   2117 O  O     . CYS B 1 116 ? 37.949  33.971  22.213  1.00 24.16 ? 115 CYS D O     1 
ATOM   2118 C  CB    . CYS B 1 116 ? 37.748  34.346  25.382  1.00 22.12 ? 115 CYS D CB    1 
ATOM   2119 S  SG    . CYS B 1 116 ? 38.099  33.829  27.043  1.00 25.34 ? 115 CYS D SG    1 
ATOM   2120 N  N     . THR B 1 117 ? 35.779  33.908  22.801  1.00 22.39 ? 116 THR D N     1 
ATOM   2121 C  CA    . THR B 1 117 ? 35.381  34.678  21.625  1.00 23.82 ? 116 THR D CA    1 
ATOM   2122 C  C     . THR B 1 117 ? 34.758  35.998  22.031  1.00 25.93 ? 116 THR D C     1 
ATOM   2123 O  O     . THR B 1 117 ? 34.224  36.707  21.186  1.00 25.11 ? 116 THR D O     1 
ATOM   2124 C  CB    . THR B 1 117 ? 34.430  33.877  20.747  1.00 25.53 ? 116 THR D CB    1 
ATOM   2125 O  OG1   . THR B 1 117 ? 33.271  33.525  21.521  1.00 23.56 ? 116 THR D OG1   1 
ATOM   2126 C  CG2   . THR B 1 117 ? 35.149  32.642  20.177  1.00 23.30 ? 116 THR D CG2   1 
ATOM   2127 N  N     . ALA B 1 118 ? 34.838  36.334  23.324  1.00 23.12 ? 117 ALA D N     1 
ATOM   2128 C  CA    . ALA B 1 118 ? 34.303  37.546  23.913  1.00 25.49 ? 117 ALA D CA    1 
ATOM   2129 C  C     . ALA B 1 118 ? 35.019  37.722  25.241  1.00 24.50 ? 117 ALA D C     1 
ATOM   2130 O  O     . ALA B 1 118 ? 35.650  36.787  25.745  1.00 21.91 ? 117 ALA D O     1 
ATOM   2131 C  CB    . ALA B 1 118 ? 32.782  37.471  24.127  1.00 25.67 ? 117 ALA D CB    1 
ATOM   2132 N  N     . LYS B 1 119 ? 34.935  38.928  25.782  1.00 26.61 ? 118 LYS D N     1 
ATOM   2133 C  CA    . LYS B 1 119 ? 35.325  39.143  27.165  1.00 24.99 ? 118 LYS D CA    1 
ATOM   2134 C  C     . LYS B 1 119 ? 34.500  38.257  28.093  1.00 30.29 ? 118 LYS D C     1 
ATOM   2135 O  O     . LYS B 1 119 ? 33.266  38.243  28.022  1.00 29.73 ? 118 LYS D O     1 
ATOM   2136 C  CB    . LYS B 1 119 ? 35.134  40.603  27.543  1.00 27.87 ? 118 LYS D CB    1 
ATOM   2137 C  CG    . LYS B 1 119 ? 35.487  40.844  29.023  1.00 31.65 ? 118 LYS D CG    1 
ATOM   2138 C  CD    . LYS B 1 119 ? 35.206  42.249  29.505  1.00 38.95 ? 118 LYS D CD    1 
ATOM   2139 C  CE    . LYS B 1 119 ? 36.171  43.224  28.936  1.00 43.99 ? 118 LYS D CE    1 
ATOM   2140 N  NZ    . LYS B 1 119 ? 36.434  44.219  30.026  1.00 50.96 ? 118 LYS D NZ    1 
ATOM   2141 N  N     . THR B 1 120 ? 35.166  37.533  29.002  1.00 26.16 ? 119 THR D N     1 
ATOM   2142 C  CA    . THR B 1 120 ? 34.477  36.717  30.012  1.00 26.48 ? 119 THR D CA    1 
ATOM   2143 C  C     . THR B 1 120 ? 35.053  37.023  31.395  1.00 31.20 ? 119 THR D C     1 
ATOM   2144 O  O     . THR B 1 120 ? 35.645  36.167  32.053  1.00 26.67 ? 119 THR D O     1 
ATOM   2145 C  CB    . THR B 1 120 ? 34.588  35.222  29.717  1.00 25.78 ? 119 THR D CB    1 
ATOM   2146 O  OG1   . THR B 1 120 ? 35.989  34.864  29.702  1.00 26.11 ? 119 THR D OG1   1 
ATOM   2147 C  CG2   . THR B 1 120 ? 33.994  34.874  28.312  1.00 24.61 ? 119 THR D CG2   1 
ATOM   2148 N  N     . GLU B 1 121 ? 34.847  38.262  31.850  1.00 29.65 ? 120 GLU D N     1 
ATOM   2149 C  CA    . GLU B 1 121 ? 35.576  38.733  33.021  1.00 29.86 ? 120 GLU D CA    1 
ATOM   2150 C  C     . GLU B 1 121 ? 35.148  38.011  34.302  1.00 30.04 ? 120 GLU D C     1 
ATOM   2151 O  O     . GLU B 1 121 ? 35.860  38.094  35.297  1.00 33.84 ? 120 GLU D O     1 
ATOM   2152 C  CB    . GLU B 1 121 ? 35.394  40.244  33.204  1.00 33.38 ? 120 GLU D CB    1 
ATOM   2153 C  CG    . GLU B 1 121 ? 34.025  40.664  33.709  1.00 32.06 ? 120 GLU D CG    1 
ATOM   2154 C  CD    . GLU B 1 121 ? 32.958  40.514  32.609  1.00 36.36 ? 120 GLU D CD    1 
ATOM   2155 O  OE1   . GLU B 1 121 ? 33.293  40.226  31.410  1.00 36.65 ? 120 GLU D OE1   1 
ATOM   2156 O  OE2   . GLU B 1 121 ? 31.782  40.736  32.944  1.00 40.53 ? 120 GLU D OE2   1 
ATOM   2157 N  N     . TRP B 1 122 ? 33.968  37.364  34.329  1.00 33.88 ? 121 TRP D N     1 
ATOM   2158 C  CA    . TRP B 1 122 ? 33.555  36.629  35.529  1.00 33.63 ? 121 TRP D CA    1 
ATOM   2159 C  C     . TRP B 1 122 ? 34.383  35.371  35.749  1.00 32.49 ? 121 TRP D C     1 
ATOM   2160 O  O     . TRP B 1 122 ? 34.291  34.778  36.838  1.00 33.61 ? 121 TRP D O     1 
ATOM   2161 C  CB    . TRP B 1 122 ? 32.038  36.268  35.495  1.00 34.53 ? 121 TRP D CB    1 
ATOM   2162 C  CG    . TRP B 1 122 ? 31.675  35.425  34.340  1.00 33.24 ? 121 TRP D CG    1 
ATOM   2163 C  CD1   . TRP B 1 122 ? 31.610  34.062  34.296  1.00 31.76 ? 121 TRP D CD1   1 
ATOM   2164 C  CD2   . TRP B 1 122 ? 31.427  35.889  33.013  1.00 29.50 ? 121 TRP D CD2   1 
ATOM   2165 N  NE1   . TRP B 1 122 ? 31.286  33.658  33.012  1.00 30.28 ? 121 TRP D NE1   1 
ATOM   2166 C  CE2   . TRP B 1 122 ? 31.186  34.756  32.207  1.00 32.47 ? 121 TRP D CE2   1 
ATOM   2167 C  CE3   . TRP B 1 122 ? 31.390  37.162  32.412  1.00 31.33 ? 121 TRP D CE3   1 
ATOM   2168 C  CZ2   . TRP B 1 122 ? 30.884  34.860  30.838  1.00 29.98 ? 121 TRP D CZ2   1 
ATOM   2169 C  CZ3   . TRP B 1 122 ? 31.099  37.264  31.062  1.00 32.39 ? 121 TRP D CZ3   1 
ATOM   2170 C  CH2   . TRP B 1 122 ? 30.887  36.113  30.276  1.00 29.23 ? 121 TRP D CH2   1 
ATOM   2171 N  N     . LEU B 1 123 ? 35.238  35.002  34.785  1.00 28.01 ? 122 LEU D N     1 
ATOM   2172 C  CA    . LEU B 1 123 ? 36.199  33.925  34.943  1.00 29.09 ? 122 LEU D CA    1 
ATOM   2173 C  C     . LEU B 1 123 ? 37.516  34.425  35.549  1.00 28.93 ? 122 LEU D C     1 
ATOM   2174 O  O     . LEU B 1 123 ? 38.362  33.609  35.894  1.00 27.80 ? 122 LEU D O     1 
ATOM   2175 C  CB    . LEU B 1 123 ? 36.491  33.254  33.575  1.00 25.74 ? 122 LEU D CB    1 
ATOM   2176 C  CG    . LEU B 1 123 ? 35.183  32.747  32.933  1.00 23.68 ? 122 LEU D CG    1 
ATOM   2177 C  CD1   . LEU B 1 123 ? 35.461  32.074  31.612  1.00 24.46 ? 122 LEU D CD1   1 
ATOM   2178 C  CD2   . LEU B 1 123 ? 34.426  31.810  33.902  1.00 30.81 ? 122 LEU D CD2   1 
ATOM   2179 N  N     . ASP B 1 124 ? 37.697  35.740  35.684  1.00 28.00 ? 123 ASP D N     1 
ATOM   2180 C  CA    . ASP B 1 124 ? 38.970  36.270  36.157  1.00 28.37 ? 123 ASP D CA    1 
ATOM   2181 C  C     . ASP B 1 124 ? 39.213  35.843  37.603  1.00 29.32 ? 123 ASP D C     1 
ATOM   2182 O  O     . ASP B 1 124 ? 38.297  35.867  38.451  1.00 30.81 ? 123 ASP D O     1 
ATOM   2183 C  CB    . ASP B 1 124 ? 38.989  37.797  36.093  1.00 30.95 ? 123 ASP D CB    1 
ATOM   2184 C  CG    . ASP B 1 124 ? 38.961  38.345  34.676  1.00 30.13 ? 123 ASP D CG    1 
ATOM   2185 O  OD1   . ASP B 1 124 ? 39.104  37.578  33.698  1.00 29.38 ? 123 ASP D OD1   1 
ATOM   2186 O  OD2   . ASP B 1 124 ? 38.855  39.590  34.579  1.00 31.37 ? 123 ASP D OD2   1 
ATOM   2187 N  N     . GLY B 1 125 ? 40.460  35.458  37.884  1.00 29.48 ? 124 GLY D N     1 
ATOM   2188 C  CA    . GLY B 1 125 ? 40.814  35.007  39.215  1.00 30.77 ? 124 GLY D CA    1 
ATOM   2189 C  C     . GLY B 1 125 ? 40.389  33.591  39.521  1.00 30.37 ? 124 GLY D C     1 
ATOM   2190 O  O     . GLY B 1 125 ? 40.650  33.100  40.632  1.00 30.97 ? 124 GLY D O     1 
ATOM   2191 N  N     . LYS B 1 126 ? 39.750  32.914  38.570  1.00 30.34 ? 125 LYS D N     1 
ATOM   2192 C  CA    . LYS B 1 126 ? 39.345  31.525  38.731  1.00 31.57 ? 125 LYS D CA    1 
ATOM   2193 C  C     . LYS B 1 126 ? 39.951  30.588  37.686  1.00 31.03 ? 125 LYS D C     1 
ATOM   2194 O  O     . LYS B 1 126 ? 40.234  29.424  38.004  1.00 31.13 ? 125 LYS D O     1 
ATOM   2195 C  CB    . LYS B 1 126 ? 37.814  31.448  38.695  1.00 33.65 ? 125 LYS D CB    1 
ATOM   2196 C  CG    . LYS B 1 126 ? 37.140  32.151  39.869  1.00 37.03 ? 125 LYS D CG    1 
ATOM   2197 C  CD    . LYS B 1 126 ? 35.664  32.481  39.537  1.00 47.01 ? 125 LYS D CD    1 
ATOM   2198 C  CE    . LYS B 1 126 ? 35.043  33.562  40.455  1.00 50.11 ? 125 LYS D CE    1 
ATOM   2199 N  NZ    . LYS B 1 126 ? 34.209  34.543  39.644  1.00 50.67 ? 125 LYS D NZ    1 
ATOM   2200 N  N     . HIS B 1 127 ? 40.165  31.060  36.468  1.00 27.11 ? 126 HIS D N     1 
ATOM   2201 C  CA    . HIS B 1 127 ? 40.845  30.325  35.406  1.00 28.00 ? 126 HIS D CA    1 
ATOM   2202 C  C     . HIS B 1 127 ? 42.165  31.013  35.073  1.00 27.74 ? 126 HIS D C     1 
ATOM   2203 O  O     . HIS B 1 127 ? 42.212  32.244  34.985  1.00 27.10 ? 126 HIS D O     1 
ATOM   2204 C  CB    . HIS B 1 127 ? 39.925  30.241  34.193  1.00 27.05 ? 126 HIS D CB    1 
ATOM   2205 C  CG    . HIS B 1 127 ? 38.713  29.394  34.469  1.00 25.98 ? 126 HIS D CG    1 
ATOM   2206 N  ND1   . HIS B 1 127 ? 38.686  28.049  34.180  1.00 26.02 ? 126 HIS D ND1   1 
ATOM   2207 C  CD2   . HIS B 1 127 ? 37.545  29.667  35.119  1.00 28.89 ? 126 HIS D CD2   1 
ATOM   2208 C  CE1   . HIS B 1 127 ? 37.522  27.534  34.572  1.00 28.21 ? 126 HIS D CE1   1 
ATOM   2209 N  NE2   . HIS B 1 127 ? 36.810  28.493  35.142  1.00 29.06 ? 126 HIS D NE2   1 
ATOM   2210 N  N     . VAL B 1 128 ? 43.225  30.218  34.893  1.00 25.76 ? 127 VAL D N     1 
ATOM   2211 C  CA    . VAL B 1 128 ? 44.551  30.763  34.590  1.00 26.55 ? 127 VAL D CA    1 
ATOM   2212 C  C     . VAL B 1 128 ? 44.650  31.102  33.105  1.00 26.94 ? 127 VAL D C     1 
ATOM   2213 O  O     . VAL B 1 128 ? 44.673  30.220  32.243  1.00 25.41 ? 127 VAL D O     1 
ATOM   2214 C  CB    . VAL B 1 128 ? 45.667  29.798  35.018  1.00 26.27 ? 127 VAL D CB    1 
ATOM   2215 C  CG1   . VAL B 1 128 ? 46.995  30.385  34.657  1.00 25.69 ? 127 VAL D CG1   1 
ATOM   2216 C  CG2   . VAL B 1 128 ? 45.575  29.420  36.525  1.00 26.92 ? 127 VAL D CG2   1 
ATOM   2217 N  N     . VAL B 1 129 ? 44.792  32.398  32.795  1.00 25.17 ? 128 VAL D N     1 
ATOM   2218 C  CA    . VAL B 1 129 ? 45.047  32.809  31.432  1.00 20.93 ? 128 VAL D CA    1 
ATOM   2219 C  C     . VAL B 1 129 ? 46.511  32.583  31.124  1.00 24.86 ? 128 VAL D C     1 
ATOM   2220 O  O     . VAL B 1 129 ? 47.382  32.986  31.911  1.00 24.70 ? 128 VAL D O     1 
ATOM   2221 C  CB    . VAL B 1 129 ? 44.680  34.288  31.233  1.00 24.92 ? 128 VAL D CB    1 
ATOM   2222 C  CG1   . VAL B 1 129 ? 45.111  34.771  29.839  1.00 24.51 ? 128 VAL D CG1   1 
ATOM   2223 C  CG2   . VAL B 1 129 ? 43.144  34.471  31.410  1.00 21.72 ? 128 VAL D CG2   1 
ATOM   2224 N  N     . PHE B 1 130 ? 46.793  32.007  29.943  1.00 23.98 ? 129 PHE D N     1 
ATOM   2225 C  CA    . PHE B 1 130 ? 48.184  31.733  29.636  1.00 25.48 ? 129 PHE D CA    1 
ATOM   2226 C  C     . PHE B 1 130 ? 48.570  31.962  28.185  1.00 25.31 ? 129 PHE D C     1 
ATOM   2227 O  O     . PHE B 1 130 ? 49.740  31.725  27.850  1.00 27.49 ? 129 PHE D O     1 
ATOM   2228 C  CB    . PHE B 1 130 ? 48.561  30.302  30.059  1.00 25.56 ? 129 PHE D CB    1 
ATOM   2229 C  CG    . PHE B 1 130 ? 47.824  29.232  29.271  1.00 24.54 ? 129 PHE D CG    1 
ATOM   2230 C  CD1   . PHE B 1 130 ? 46.511  28.807  29.638  1.00 24.32 ? 129 PHE D CD1   1 
ATOM   2231 C  CD2   . PHE B 1 130 ? 48.409  28.689  28.124  1.00 25.64 ? 129 PHE D CD2   1 
ATOM   2232 C  CE1   . PHE B 1 130 ? 45.844  27.828  28.877  1.00 24.29 ? 129 PHE D CE1   1 
ATOM   2233 C  CE2   . PHE B 1 130 ? 47.738  27.719  27.384  1.00 25.72 ? 129 PHE D CE2   1 
ATOM   2234 C  CZ    . PHE B 1 130 ? 46.448  27.281  27.782  1.00 22.36 ? 129 PHE D CZ    1 
ATOM   2235 N  N     . GLY B 1 131 ? 47.671  32.443  27.334  1.00 21.87 ? 130 GLY D N     1 
ATOM   2236 C  CA    . GLY B 1 131 ? 48.075  32.746  25.977  1.00 23.42 ? 130 GLY D CA    1 
ATOM   2237 C  C     . GLY B 1 131 ? 46.998  33.510  25.256  1.00 25.30 ? 130 GLY D C     1 
ATOM   2238 O  O     . GLY B 1 131 ? 45.972  33.884  25.832  1.00 23.02 ? 130 GLY D O     1 
ATOM   2239 N  N     . LYS B 1 132 ? 47.219  33.684  23.961  1.00 25.50 ? 131 LYS D N     1 
ATOM   2240 C  CA    . LYS B 1 132 ? 46.254  34.371  23.128  1.00 23.39 ? 131 LYS D CA    1 
ATOM   2241 C  C     . LYS B 1 132 ? 46.450  33.903  21.689  1.00 26.17 ? 131 LYS D C     1 
ATOM   2242 O  O     . LYS B 1 132 ? 47.553  33.508  21.276  1.00 28.40 ? 131 LYS D O     1 
ATOM   2243 C  CB    . LYS B 1 132 ? 46.383  35.900  23.224  1.00 24.43 ? 131 LYS D CB    1 
ATOM   2244 C  CG    . LYS B 1 132 ? 47.541  36.430  22.410  1.00 31.74 ? 131 LYS D CG    1 
ATOM   2245 C  CD    . LYS B 1 132 ? 47.840  37.916  22.688  1.00 33.45 ? 131 LYS D CD    1 
ATOM   2246 C  CE    . LYS B 1 132 ? 47.426  38.825  21.530  1.00 44.09 ? 131 LYS D CE    1 
ATOM   2247 N  NZ    . LYS B 1 132 ? 47.102  40.220  22.015  1.00 52.19 ? 131 LYS D NZ    1 
ATOM   2248 N  N     . VAL B 1 133 ? 45.347  33.931  20.944  1.00 24.17 ? 132 VAL D N     1 
ATOM   2249 C  CA    . VAL B 1 133 ? 45.382  33.658  19.523  1.00 24.02 ? 132 VAL D CA    1 
ATOM   2250 C  C     . VAL B 1 133 ? 46.294  34.672  18.840  1.00 27.44 ? 132 VAL D C     1 
ATOM   2251 O  O     . VAL B 1 133 ? 46.198  35.895  19.053  1.00 27.11 ? 132 VAL D O     1 
ATOM   2252 C  CB    . VAL B 1 133 ? 43.943  33.658  18.965  1.00 23.35 ? 132 VAL D CB    1 
ATOM   2253 C  CG1   . VAL B 1 133 ? 43.980  33.562  17.361  1.00 25.27 ? 132 VAL D CG1   1 
ATOM   2254 C  CG2   . VAL B 1 133 ? 43.153  32.498  19.565  1.00 20.22 ? 132 VAL D CG2   1 
ATOM   2255 N  N     . LYS B 1 134 ? 47.230  34.164  18.031  1.00 25.97 ? 133 LYS D N     1 
ATOM   2256 C  CA    . LYS B 1 134 ? 48.114  35.042  17.281  1.00 31.23 ? 133 LYS D CA    1 
ATOM   2257 C  C     . LYS B 1 134 ? 47.593  35.196  15.862  1.00 32.60 ? 133 LYS D C     1 
ATOM   2258 O  O     . LYS B 1 134 ? 47.224  36.298  15.454  1.00 36.20 ? 133 LYS D O     1 
ATOM   2259 C  CB    . LYS B 1 134 ? 49.547  34.521  17.303  1.00 30.70 ? 133 LYS D CB    1 
ATOM   2260 C  CG    . LYS B 1 134 ? 50.469  35.386  16.481  1.00 36.79 ? 133 LYS D CG    1 
ATOM   2261 C  CD    . LYS B 1 134 ? 51.855  35.567  17.083  1.00 40.04 ? 133 LYS D CD    1 
ATOM   2262 C  CE    . LYS B 1 134 ? 52.688  34.313  16.918  1.00 42.06 ? 133 LYS D CE    1 
ATOM   2263 N  NZ    . LYS B 1 134 ? 54.080  34.602  16.419  1.00 47.24 ? 133 LYS D NZ    1 
ATOM   2264 N  N     . GLU B 1 135 ? 47.516  34.103  15.116  1.00 31.65 ? 134 GLU D N     1 
ATOM   2265 C  CA    . GLU B 1 135 ? 46.858  34.112  13.812  1.00 33.11 ? 134 GLU D CA    1 
ATOM   2266 C  C     . GLU B 1 135 ? 45.703  33.123  13.824  1.00 27.05 ? 134 GLU D C     1 
ATOM   2267 O  O     . GLU B 1 135 ? 45.665  32.193  14.631  1.00 27.69 ? 134 GLU D O     1 
ATOM   2268 C  CB    . GLU B 1 135 ? 47.815  33.758  12.662  1.00 38.54 ? 134 GLU D CB    1 
ATOM   2269 C  CG    . GLU B 1 135 ? 49.143  34.500  12.692  1.00 41.16 ? 134 GLU D CG    1 
ATOM   2270 C  CD    . GLU B 1 135 ? 49.687  34.814  11.305  1.00 52.94 ? 134 GLU D CD    1 
ATOM   2271 O  OE1   . GLU B 1 135 ? 50.919  34.718  11.139  1.00 54.78 ? 134 GLU D OE1   1 
ATOM   2272 O  OE2   . GLU B 1 135 ? 48.913  35.191  10.387  1.00 55.87 ? 134 GLU D OE2   1 
ATOM   2273 N  N     . GLY B 1 136 ? 44.739  33.366  12.946  1.00 30.32 ? 135 GLY D N     1 
ATOM   2274 C  CA    . GLY B 1 136 ? 43.621  32.457  12.767  1.00 25.53 ? 135 GLY D CA    1 
ATOM   2275 C  C     . GLY B 1 136 ? 42.409  32.708  13.643  1.00 25.78 ? 135 GLY D C     1 
ATOM   2276 O  O     . GLY B 1 136 ? 41.613  31.788  13.853  1.00 25.22 ? 135 GLY D O     1 
ATOM   2277 N  N     . MET B 1 137 ? 42.251  33.909  14.193  1.00 23.49 ? 136 MET D N     1 
ATOM   2278 C  CA    . MET B 1 137 ? 41.022  34.190  14.951  1.00 22.30 ? 136 MET D CA    1 
ATOM   2279 C  C     . MET B 1 137 ? 39.798  33.925  14.088  1.00 25.18 ? 136 MET D C     1 
ATOM   2280 O  O     . MET B 1 137 ? 38.740  33.539  14.599  1.00 20.48 ? 136 MET D O     1 
ATOM   2281 C  CB    . MET B 1 137 ? 40.944  35.673  15.424  1.00 24.30 ? 136 MET D CB    1 
ATOM   2282 C  CG    . MET B 1 137 ? 40.031  36.007  16.642  1.00 25.31 ? 136 MET D CG    1 
ATOM   2283 S  SD    . MET B 1 137 ? 40.096  34.875  18.053  1.00 25.57 ? 136 MET D SD    1 
ATOM   2284 C  CE    . MET B 1 137 ? 38.347  34.722  18.452  1.00 24.66 ? 136 MET D CE    1 
ATOM   2285 N  N     . ASN B 1 138 ? 39.897  34.189  12.776  1.00 24.31 ? 137 ASN D N     1 
ATOM   2286 C  CA    . ASN B 1 138 ? 38.753  33.954  11.920  1.00 25.19 ? 137 ASN D CA    1 
ATOM   2287 C  C     . ASN B 1 138 ? 38.352  32.488  11.940  1.00 23.53 ? 137 ASN D C     1 
ATOM   2288 O  O     . ASN B 1 138 ? 37.174  32.142  11.746  1.00 23.22 ? 137 ASN D O     1 
ATOM   2289 C  CB    . ASN B 1 138 ? 39.093  34.425  10.494  1.00 26.76 ? 137 ASN D CB    1 
ATOM   2290 C  CG    . ASN B 1 138 ? 40.129  33.518  9.826   1.00 27.55 ? 137 ASN D CG    1 
ATOM   2291 O  OD1   . ASN B 1 138 ? 41.258  33.369  10.312  1.00 27.66 ? 137 ASN D OD1   1 
ATOM   2292 N  ND2   . ASN B 1 138 ? 39.708  32.818  8.791   1.00 30.15 ? 137 ASN D ND2   1 
ATOM   2293 N  N     . ILE B 1 139 ? 39.308  31.602  12.212  1.00 24.06 ? 138 ILE D N     1 
ATOM   2294 C  CA    . ILE B 1 139 ? 38.975  30.181  12.282  1.00 20.97 ? 138 ILE D CA    1 
ATOM   2295 C  C     . ILE B 1 139 ? 38.233  29.870  13.580  1.00 22.38 ? 138 ILE D C     1 
ATOM   2296 O  O     . ILE B 1 139 ? 37.301  29.063  13.587  1.00 23.09 ? 138 ILE D O     1 
ATOM   2297 C  CB    . ILE B 1 139 ? 40.255  29.329  12.139  1.00 24.17 ? 138 ILE D CB    1 
ATOM   2298 C  CG1   . ILE B 1 139 ? 40.935  29.557  10.763  1.00 26.26 ? 138 ILE D CG1   1 
ATOM   2299 C  CG2   . ILE B 1 139 ? 39.959  27.827  12.399  1.00 24.26 ? 138 ILE D CG2   1 
ATOM   2300 C  CD1   . ILE B 1 139 ? 40.034  29.251  9.610   1.00 29.24 ? 138 ILE D CD1   1 
ATOM   2301 N  N     . VAL B 1 140 ? 38.661  30.467  14.702  1.00 18.84 ? 139 VAL D N     1 
ATOM   2302 C  CA    . VAL B 1 140 ? 37.910  30.297  15.959  1.00 18.06 ? 139 VAL D CA    1 
ATOM   2303 C  C     . VAL B 1 140 ? 36.505  30.825  15.768  1.00 21.64 ? 139 VAL D C     1 
ATOM   2304 O  O     . VAL B 1 140 ? 35.533  30.242  16.257  1.00 21.26 ? 139 VAL D O     1 
ATOM   2305 C  CB    . VAL B 1 140 ? 38.642  31.022  17.115  1.00 21.80 ? 139 VAL D CB    1 
ATOM   2306 C  CG1   . VAL B 1 140 ? 37.870  30.852  18.408  1.00 19.59 ? 139 VAL D CG1   1 
ATOM   2307 C  CG2   . VAL B 1 140 ? 40.022  30.437  17.343  1.00 19.66 ? 139 VAL D CG2   1 
ATOM   2308 N  N     . GLU B 1 141 ? 36.368  31.944  15.045  1.00 22.04 ? 140 GLU D N     1 
ATOM   2309 C  CA    . GLU B 1 141 ? 35.028  32.467  14.787  1.00 24.92 ? 140 GLU D CA    1 
ATOM   2310 C  C     . GLU B 1 141 ? 34.223  31.464  13.971  1.00 22.75 ? 140 GLU D C     1 
ATOM   2311 O  O     . GLU B 1 141 ? 33.057  31.201  14.258  1.00 23.93 ? 140 GLU D O     1 
ATOM   2312 C  CB    . GLU B 1 141 ? 35.112  33.822  14.075  1.00 25.82 ? 140 GLU D CB    1 
ATOM   2313 C  CG    . GLU B 1 141 ? 35.629  34.995  14.930  1.00 27.15 ? 140 GLU D CG    1 
ATOM   2314 C  CD    . GLU B 1 141 ? 36.242  36.124  14.052  1.00 33.37 ? 140 GLU D CD    1 
ATOM   2315 O  OE1   . GLU B 1 141 ? 36.071  36.132  12.796  1.00 31.12 ? 140 GLU D OE1   1 
ATOM   2316 O  OE2   . GLU B 1 141 ? 36.902  37.041  14.608  1.00 31.60 ? 140 GLU D OE2   1 
ATOM   2317 N  N     . ALA B 1 142 ? 34.841  30.869  12.960  1.00 20.35 ? 141 ALA D N     1 
ATOM   2318 C  CA    . ALA B 1 142 ? 34.105  29.925  12.134  1.00 22.27 ? 141 ALA D CA    1 
ATOM   2319 C  C     . ALA B 1 142 ? 33.726  28.698  12.951  1.00 22.50 ? 141 ALA D C     1 
ATOM   2320 O  O     . ALA B 1 142 ? 32.695  28.062  12.691  1.00 22.31 ? 141 ALA D O     1 
ATOM   2321 C  CB    . ALA B 1 142 ? 34.942  29.526  10.910  1.00 24.16 ? 141 ALA D CB    1 
ATOM   2322 N  N     . MET B 1 143 ? 34.519  28.358  13.962  1.00 20.19 ? 142 MET D N     1 
ATOM   2323 C  CA    . MET B 1 143 ? 34.095  27.225  14.797  1.00 21.71 ? 142 MET D CA    1 
ATOM   2324 C  C     . MET B 1 143 ? 32.782  27.487  15.524  1.00 21.38 ? 142 MET D C     1 
ATOM   2325 O  O     . MET B 1 143 ? 31.998  26.555  15.722  1.00 22.56 ? 142 MET D O     1 
ATOM   2326 C  CB    . MET B 1 143 ? 35.160  26.788  15.815  1.00 24.67 ? 142 MET D CB    1 
ATOM   2327 C  CG    . MET B 1 143 ? 36.426  26.146  15.251  1.00 22.93 ? 142 MET D CG    1 
ATOM   2328 S  SD    . MET B 1 143 ? 37.960  26.404  16.165  1.00 27.91 ? 142 MET D SD    1 
ATOM   2329 C  CE    . MET B 1 143 ? 37.491  25.404  17.515  1.00 20.88 ? 142 MET D CE    1 
ATOM   2330 N  N     . GLU B 1 144 ? 32.480  28.743  15.831  1.00 20.62 ? 143 GLU D N     1 
ATOM   2331 C  CA    . GLU B 1 144 ? 31.191  29.045  16.439  1.00 21.80 ? 143 GLU D CA    1 
ATOM   2332 C  C     . GLU B 1 144 ? 30.014  28.691  15.519  1.00 23.38 ? 143 GLU D C     1 
ATOM   2333 O  O     . GLU B 1 144 ? 28.888  28.550  16.019  1.00 25.49 ? 143 GLU D O     1 
ATOM   2334 C  CB    . GLU B 1 144 ? 31.093  30.518  16.817  1.00 21.72 ? 143 GLU D CB    1 
ATOM   2335 C  CG    . GLU B 1 144 ? 32.026  30.942  17.941  1.00 23.47 ? 143 GLU D CG    1 
ATOM   2336 C  CD    . GLU B 1 144 ? 31.662  32.298  18.507  1.00 24.21 ? 143 GLU D CD    1 
ATOM   2337 O  OE1   . GLU B 1 144 ? 31.420  33.232  17.718  1.00 27.01 ? 143 GLU D OE1   1 
ATOM   2338 O  OE2   . GLU B 1 144 ? 31.673  32.468  19.753  1.00 24.44 ? 143 GLU D OE2   1 
ATOM   2339 N  N     . ARG B 1 145 ? 30.232  28.510  14.208  1.00 21.96 ? 144 ARG D N     1 
ATOM   2340 C  CA    . ARG B 1 145 ? 29.123  28.039  13.345  1.00 24.33 ? 144 ARG D CA    1 
ATOM   2341 C  C     . ARG B 1 145 ? 28.526  26.722  13.829  1.00 24.39 ? 144 ARG D C     1 
ATOM   2342 O  O     . ARG B 1 145 ? 27.395  26.354  13.432  1.00 26.56 ? 144 ARG D O     1 
ATOM   2343 C  CB    . ARG B 1 145 ? 29.592  27.810  11.910  1.00 27.68 ? 144 ARG D CB    1 
ATOM   2344 C  CG    . ARG B 1 145 ? 30.229  29.008  11.310  1.00 27.83 ? 144 ARG D CG    1 
ATOM   2345 C  CD    . ARG B 1 145 ? 30.603  28.668  9.896   1.00 28.42 ? 144 ARG D CD    1 
ATOM   2346 N  NE    . ARG B 1 145 ? 31.321  29.743  9.222   1.00 34.37 ? 144 ARG D NE    1 
ATOM   2347 C  CZ    . ARG B 1 145 ? 32.275  29.513  8.329   1.00 31.09 ? 144 ARG D CZ    1 
ATOM   2348 N  NH1   . ARG B 1 145 ? 32.597  28.274  7.961   1.00 32.02 ? 144 ARG D NH1   1 
ATOM   2349 N  NH2   . ARG B 1 145 ? 32.899  30.544  7.772   1.00 37.01 ? 144 ARG D NH2   1 
ATOM   2350 N  N     . PHE B 1 146 ? 29.303  25.956  14.592  1.00 24.92 ? 145 PHE D N     1 
ATOM   2351 C  CA    . PHE B 1 146 ? 28.964  24.577  14.906  1.00 26.28 ? 145 PHE D CA    1 
ATOM   2352 C  C     . PHE B 1 146 ? 28.670  24.383  16.379  1.00 26.43 ? 145 PHE D C     1 
ATOM   2353 O  O     . PHE B 1 146 ? 28.644  23.250  16.850  1.00 24.26 ? 145 PHE D O     1 
ATOM   2354 C  CB    . PHE B 1 146 ? 30.105  23.660  14.441  1.00 25.69 ? 145 PHE D CB    1 
ATOM   2355 C  CG    . PHE B 1 146 ? 30.385  23.839  12.965  1.00 27.15 ? 145 PHE D CG    1 
ATOM   2356 C  CD1   . PHE B 1 146 ? 29.356  23.650  12.036  1.00 31.36 ? 145 PHE D CD1   1 
ATOM   2357 C  CD2   . PHE B 1 146 ? 31.615  24.333  12.539  1.00 30.75 ? 145 PHE D CD2   1 
ATOM   2358 C  CE1   . PHE B 1 146 ? 29.578  23.890  10.651  1.00 32.77 ? 145 PHE D CE1   1 
ATOM   2359 C  CE2   . PHE B 1 146 ? 31.845  24.573  11.174  1.00 31.77 ? 145 PHE D CE2   1 
ATOM   2360 C  CZ    . PHE B 1 146 ? 30.851  24.331  10.242  1.00 32.18 ? 145 PHE D CZ    1 
ATOM   2361 N  N     . GLY B 1 147 ? 28.467  25.465  17.120  1.00 26.08 ? 146 GLY D N     1 
ATOM   2362 C  CA    . GLY B 1 147 ? 28.146  25.364  18.532  1.00 25.48 ? 146 GLY D CA    1 
ATOM   2363 C  C     . GLY B 1 147 ? 26.663  25.534  18.799  1.00 24.93 ? 146 GLY D C     1 
ATOM   2364 O  O     . GLY B 1 147 ? 25.824  25.515  17.898  1.00 27.49 ? 146 GLY D O     1 
ATOM   2365 N  N     . SER B 1 148 ? 26.334  25.680  20.083  1.00 26.14 ? 147 SER D N     1 
ATOM   2366 C  CA    . SER B 1 148 ? 24.948  25.822  20.490  1.00 27.01 ? 147 SER D CA    1 
ATOM   2367 C  C     . SER B 1 148 ? 24.962  26.480  21.870  1.00 24.71 ? 147 SER D C     1 
ATOM   2368 O  O     . SER B 1 148 ? 26.013  26.645  22.492  1.00 23.70 ? 147 SER D O     1 
ATOM   2369 C  CB    . SER B 1 148 ? 24.255  24.449  20.524  1.00 26.84 ? 147 SER D CB    1 
ATOM   2370 O  OG    . SER B 1 148 ? 24.791  23.694  21.631  1.00 27.20 ? 147 SER D OG    1 
ATOM   2371 N  N     . ARG B 1 149 ? 23.774  26.807  22.343  1.00 26.95 ? 148 ARG D N     1 
ATOM   2372 C  CA    . ARG B 1 149 ? 23.620  27.492  23.621  1.00 29.26 ? 148 ARG D CA    1 
ATOM   2373 C  C     . ARG B 1 149 ? 24.230  26.698  24.771  1.00 28.36 ? 148 ARG D C     1 
ATOM   2374 O  O     . ARG B 1 149 ? 24.861  27.287  25.675  1.00 29.47 ? 148 ARG D O     1 
ATOM   2375 C  CB    . ARG B 1 149 ? 22.129  27.735  23.870  1.00 31.05 ? 148 ARG D CB    1 
ATOM   2376 C  CG    . ARG B 1 149 ? 21.818  28.358  25.215  1.00 31.79 ? 148 ARG D CG    1 
ATOM   2377 C  CD    . ARG B 1 149 ? 20.419  28.889  25.163  1.00 34.00 ? 148 ARG D CD    1 
ATOM   2378 N  NE    . ARG B 1 149 ? 19.958  29.247  26.491  1.00 40.83 ? 148 ARG D NE    1 
ATOM   2379 C  CZ    . ARG B 1 149 ? 19.720  28.366  27.445  1.00 40.78 ? 148 ARG D CZ    1 
ATOM   2380 N  NH1   . ARG B 1 149 ? 19.640  27.071  27.175  1.00 39.26 ? 148 ARG D NH1   1 
ATOM   2381 N  NH2   . ARG B 1 149 ? 19.520  28.798  28.691  1.00 40.28 ? 148 ARG D NH2   1 
ATOM   2382 N  N     . ASN B 1 150 ? 24.038  25.375  24.803  1.00 26.72 ? 149 ASN D N     1 
ATOM   2383 C  CA    . ASN B 1 150 ? 24.666  24.626  25.903  1.00 27.08 ? 149 ASN D CA    1 
ATOM   2384 C  C     . ASN B 1 150 ? 26.000  23.991  25.513  1.00 29.14 ? 149 ASN D C     1 
ATOM   2385 O  O     . ASN B 1 150 ? 26.566  23.210  26.289  1.00 26.34 ? 149 ASN D O     1 
ATOM   2386 C  CB    . ASN B 1 150 ? 23.728  23.560  26.484  1.00 29.84 ? 149 ASN D CB    1 
ATOM   2387 C  CG    . ASN B 1 150 ? 23.651  22.323  25.658  1.00 32.34 ? 149 ASN D CG    1 
ATOM   2388 O  OD1   . ASN B 1 150 ? 24.051  22.316  24.499  1.00 27.59 ? 149 ASN D OD1   1 
ATOM   2389 N  ND2   . ASN B 1 150 ? 23.069  21.256  26.246  1.00 31.16 ? 149 ASN D ND2   1 
ATOM   2390 N  N     . GLY B 1 151 ? 26.502  24.287  24.320  1.00 25.62 ? 150 GLY D N     1 
ATOM   2391 C  CA    . GLY B 1 151 ? 27.847  23.900  23.956  1.00 25.82 ? 150 GLY D CA    1 
ATOM   2392 C  C     . GLY B 1 151 ? 27.950  22.629  23.137  1.00 25.05 ? 150 GLY D C     1 
ATOM   2393 O  O     . GLY B 1 151 ? 28.989  22.401  22.519  1.00 26.27 ? 150 GLY D O     1 
ATOM   2394 N  N     . LYS B 1 152 ? 26.910  21.813  23.074  1.00 25.33 ? 151 LYS D N     1 
ATOM   2395 C  CA    . LYS B 1 152 ? 26.971  20.660  22.183  1.00 25.66 ? 151 LYS D CA    1 
ATOM   2396 C  C     . LYS B 1 152 ? 27.251  21.096  20.749  1.00 25.99 ? 151 LYS D C     1 
ATOM   2397 O  O     . LYS B 1 152 ? 26.661  22.072  20.233  1.00 27.08 ? 151 LYS D O     1 
ATOM   2398 C  CB    . LYS B 1 152 ? 25.669  19.862  22.279  1.00 27.23 ? 151 LYS D CB    1 
ATOM   2399 C  CG    . LYS B 1 152 ? 25.457  18.773  21.268  1.00 36.43 ? 151 LYS D CG    1 
ATOM   2400 C  CD    . LYS B 1 152 ? 26.225  17.508  21.628  1.00 41.57 ? 151 LYS D CD    1 
ATOM   2401 C  CE    . LYS B 1 152 ? 25.518  16.290  20.998  1.00 40.76 ? 151 LYS D CE    1 
ATOM   2402 N  NZ    . LYS B 1 152 ? 25.055  16.512  19.580  1.00 47.79 ? 151 LYS D NZ    1 
ATOM   2403 N  N     . THR B 1 153 ? 28.155  20.377  20.097  1.00 26.01 ? 152 THR D N     1 
ATOM   2404 C  CA    . THR B 1 153 ? 28.554  20.745  18.749  1.00 27.27 ? 152 THR D CA    1 
ATOM   2405 C  C     . THR B 1 153 ? 27.752  19.951  17.728  1.00 28.76 ? 152 THR D C     1 
ATOM   2406 O  O     . THR B 1 153 ? 27.345  18.794  17.963  1.00 29.09 ? 152 THR D O     1 
ATOM   2407 C  CB    . THR B 1 153 ? 30.058  20.531  18.516  1.00 27.33 ? 152 THR D CB    1 
ATOM   2408 O  OG1   . THR B 1 153 ? 30.370  19.144  18.681  1.00 28.08 ? 152 THR D OG1   1 
ATOM   2409 C  CG2   . THR B 1 153 ? 30.906  21.395  19.506  1.00 24.68 ? 152 THR D CG2   1 
ATOM   2410 N  N     . SER B 1 154 ? 27.524  20.588  16.573  1.00 27.53 ? 153 SER D N     1 
ATOM   2411 C  CA    . SER B 1 154 ? 26.706  19.948  15.554  1.00 28.31 ? 153 SER D CA    1 
ATOM   2412 C  C     . SER B 1 154 ? 27.527  19.219  14.504  1.00 28.19 ? 153 SER D C     1 
ATOM   2413 O  O     . SER B 1 154 ? 26.941  18.519  13.652  1.00 30.01 ? 153 SER D O     1 
ATOM   2414 C  CB    . SER B 1 154 ? 25.793  20.980  14.897  1.00 25.66 ? 153 SER D CB    1 
ATOM   2415 O  OG    . SER B 1 154 ? 26.494  22.099  14.414  1.00 31.26 ? 153 SER D OG    1 
ATOM   2416 N  N     . LYS B 1 155 ? 28.834  19.423  14.508  1.00 29.77 ? 154 LYS D N     1 
ATOM   2417 C  CA    . LYS B 1 155 ? 29.772  18.666  13.690  1.00 32.21 ? 154 LYS D CA    1 
ATOM   2418 C  C     . LYS B 1 155 ? 30.978  18.366  14.572  1.00 32.23 ? 154 LYS D C     1 
ATOM   2419 O  O     . LYS B 1 155 ? 31.177  19.008  15.600  1.00 29.34 ? 154 LYS D O     1 
ATOM   2420 C  CB    . LYS B 1 155 ? 30.182  19.450  12.422  1.00 28.00 ? 154 LYS D CB    1 
ATOM   2421 C  CG    . LYS B 1 155 ? 29.026  19.588  11.379  1.00 28.52 ? 154 LYS D CG    1 
ATOM   2422 C  CD    . LYS B 1 155 ? 29.471  20.346  10.118  1.00 32.92 ? 154 LYS D CD    1 
ATOM   2423 C  CE    . LYS B 1 155 ? 28.322  20.389  9.077   1.00 32.80 ? 154 LYS D CE    1 
ATOM   2424 N  NZ    . LYS B 1 155 ? 28.480  19.284  8.119   1.00 42.59 ? 154 LYS D NZ    1 
ATOM   2425 N  N     . LYS B 1 156 ? 31.795  17.402  14.157  1.00 33.22 ? 155 LYS D N     1 
ATOM   2426 C  CA    . LYS B 1 156 ? 32.944  16.971  14.929  1.00 30.89 ? 155 LYS D CA    1 
ATOM   2427 C  C     . LYS B 1 156 ? 34.105  17.905  14.600  1.00 32.44 ? 155 LYS D C     1 
ATOM   2428 O  O     . LYS B 1 156 ? 34.633  17.896  13.479  1.00 30.11 ? 155 LYS D O     1 
ATOM   2429 C  CB    . LYS B 1 156 ? 33.263  15.500  14.634  1.00 31.41 ? 155 LYS D CB    1 
ATOM   2430 C  CG    . LYS B 1 156 ? 34.301  14.872  15.558  1.00 38.90 ? 155 LYS D CG    1 
ATOM   2431 C  CD    . LYS B 1 156 ? 34.604  13.433  15.156  1.00 40.94 ? 155 LYS D CD    1 
ATOM   2432 C  CE    . LYS B 1 156 ? 36.022  13.252  14.524  1.00 47.38 ? 155 LYS D CE    1 
ATOM   2433 N  NZ    . LYS B 1 156 ? 36.164  13.718  13.031  1.00 40.36 ? 155 LYS D NZ    1 
ATOM   2434 N  N     . ILE B 1 157 ? 34.505  18.706  15.584  1.00 29.54 ? 156 ILE D N     1 
ATOM   2435 C  CA    . ILE B 1 157 ? 35.557  19.714  15.435  1.00 25.16 ? 156 ILE D CA    1 
ATOM   2436 C  C     . ILE B 1 157 ? 36.823  19.136  16.067  1.00 27.74 ? 156 ILE D C     1 
ATOM   2437 O  O     . ILE B 1 157 ? 36.863  18.936  17.282  1.00 30.91 ? 156 ILE D O     1 
ATOM   2438 C  CB    . ILE B 1 157 ? 35.135  21.022  16.112  1.00 25.67 ? 156 ILE D CB    1 
ATOM   2439 C  CG1   . ILE B 1 157 ? 33.701  21.388  15.719  1.00 28.47 ? 156 ILE D CG1   1 
ATOM   2440 C  CG2   . ILE B 1 157 ? 36.090  22.138  15.822  1.00 24.13 ? 156 ILE D CG2   1 
ATOM   2441 C  CD1   . ILE B 1 157 ? 33.514  21.464  14.240  1.00 29.50 ? 156 ILE D CD1   1 
ATOM   2442 N  N     . THR B 1 158 ? 37.876  18.903  15.272  1.00 30.33 ? 157 THR D N     1 
ATOM   2443 C  CA    . THR B 1 158 ? 39.080  18.204  15.724  1.00 26.52 ? 157 THR D CA    1 
ATOM   2444 C  C     . THR B 1 158 ? 40.344  19.008  15.467  1.00 27.76 ? 157 THR D C     1 
ATOM   2445 O  O     . THR B 1 158 ? 40.414  19.866  14.582  1.00 27.72 ? 157 THR D O     1 
ATOM   2446 C  CB    . THR B 1 158 ? 39.225  16.845  15.035  1.00 27.45 ? 157 THR D CB    1 
ATOM   2447 O  OG1   . THR B 1 158 ? 39.274  17.027  13.601  1.00 28.88 ? 157 THR D OG1   1 
ATOM   2448 C  CG2   . THR B 1 158 ? 38.043  15.946  15.412  1.00 29.99 ? 157 THR D CG2   1 
ATOM   2449 N  N     . ILE B 1 159 ? 41.360  18.695  16.260  1.00 28.32 ? 158 ILE D N     1 
ATOM   2450 C  CA    . ILE B 1 159 ? 42.722  19.176  16.027  1.00 28.88 ? 158 ILE D CA    1 
ATOM   2451 C  C     . ILE B 1 159 ? 43.379  18.083  15.182  1.00 29.94 ? 158 ILE D C     1 
ATOM   2452 O  O     . ILE B 1 159 ? 43.855  17.057  15.697  1.00 30.82 ? 158 ILE D O     1 
ATOM   2453 C  CB    . ILE B 1 159 ? 43.456  19.441  17.345  1.00 29.09 ? 158 ILE D CB    1 
ATOM   2454 C  CG1   . ILE B 1 159 ? 42.674  20.445  18.194  1.00 28.28 ? 158 ILE D CG1   1 
ATOM   2455 C  CG2   . ILE B 1 159 ? 44.909  19.864  17.132  1.00 29.61 ? 158 ILE D CG2   1 
ATOM   2456 C  CD1   . ILE B 1 159 ? 43.141  20.525  19.729  1.00 26.67 ? 158 ILE D CD1   1 
ATOM   2457 N  N     . ALA B 1 160 ? 43.367  18.267  13.854  1.00 29.92 ? 159 ALA D N     1 
ATOM   2458 C  CA    . ALA B 1 160 ? 43.923  17.231  12.990  1.00 31.18 ? 159 ALA D CA    1 
ATOM   2459 C  C     . ALA B 1 160 ? 45.447  17.182  13.094  1.00 33.96 ? 159 ALA D C     1 
ATOM   2460 O  O     . ALA B 1 160 ? 46.060  16.123  12.907  1.00 31.37 ? 159 ALA D O     1 
ATOM   2461 C  CB    . ALA B 1 160 ? 43.471  17.452  11.541  1.00 31.72 ? 159 ALA D CB    1 
ATOM   2462 N  N     . ASP B 1 161 ? 46.073  18.302  13.414  1.00 32.30 ? 160 ASP D N     1 
ATOM   2463 C  CA    . ASP B 1 161 ? 47.518  18.367  13.573  1.00 31.88 ? 160 ASP D CA    1 
ATOM   2464 C  C     . ASP B 1 161 ? 47.792  19.488  14.547  1.00 31.39 ? 160 ASP D C     1 
ATOM   2465 O  O     . ASP B 1 161 ? 46.962  20.378  14.755  1.00 29.72 ? 160 ASP D O     1 
ATOM   2466 C  CB    . ASP B 1 161 ? 48.221  18.621  12.224  1.00 33.25 ? 160 ASP D CB    1 
ATOM   2467 C  CG    . ASP B 1 161 ? 49.685  18.223  12.216  1.00 37.82 ? 160 ASP D CG    1 
ATOM   2468 O  OD1   . ASP B 1 161 ? 50.241  17.784  13.267  1.00 38.49 ? 160 ASP D OD1   1 
ATOM   2469 O  OD2   . ASP B 1 161 ? 50.290  18.346  11.112  1.00 41.79 ? 160 ASP D OD2   1 
ATOM   2470 N  N     . CYS B 1 162 ? 48.959  19.443  15.161  1.00 32.29 ? 161 CYS D N     1 
ATOM   2471 C  CA    . CYS B 1 162 ? 49.345  20.563  16.004  1.00 28.38 ? 161 CYS D CA    1 
ATOM   2472 C  C     . CYS B 1 162 ? 50.825  20.392  16.284  1.00 32.92 ? 161 CYS D C     1 
ATOM   2473 O  O     . CYS B 1 162 ? 51.362  19.277  16.215  1.00 33.45 ? 161 CYS D O     1 
ATOM   2474 C  CB    . CYS B 1 162 ? 48.550  20.630  17.342  1.00 27.85 ? 161 CYS D CB    1 
ATOM   2475 S  SG    . CYS B 1 162 ? 48.519  19.032  18.213  1.00 30.64 ? 161 CYS D SG    1 
ATOM   2476 N  N     . GLY B 1 163 ? 51.459  21.511  16.596  1.00 31.18 ? 162 GLY D N     1 
ATOM   2477 C  CA    . GLY B 1 163 ? 52.865  21.518  16.936  1.00 33.05 ? 162 GLY D CA    1 
ATOM   2478 C  C     . GLY B 1 163 ? 53.328  22.909  17.333  1.00 33.29 ? 162 GLY D C     1 
ATOM   2479 O  O     . GLY B 1 163 ? 52.530  23.788  17.673  1.00 31.55 ? 162 GLY D O     1 
ATOM   2480 N  N     . GLN B 1 164 ? 54.635  23.102  17.278  1.00 34.30 ? 163 GLN D N     1 
ATOM   2481 C  CA    . GLN B 1 164 ? 55.265  24.352  17.674  1.00 31.90 ? 163 GLN D CA    1 
ATOM   2482 C  C     . GLN B 1 164 ? 55.829  25.052  16.445  1.00 34.78 ? 163 GLN D C     1 
ATOM   2483 O  O     . GLN B 1 164 ? 56.418  24.405  15.565  1.00 34.10 ? 163 GLN D O     1 
ATOM   2484 C  CB    . GLN B 1 164 ? 56.381  24.084  18.692  1.00 34.16 ? 163 GLN D CB    1 
ATOM   2485 C  CG    . GLN B 1 164 ? 57.154  25.354  19.127  1.00 29.85 ? 163 GLN D CG    1 
ATOM   2486 C  CD    . GLN B 1 164 ? 57.986  25.160  20.375  1.00 34.80 ? 163 GLN D CD    1 
ATOM   2487 O  OE1   . GLN B 1 164 ? 58.226  24.032  20.822  1.00 36.07 ? 163 GLN D OE1   1 
ATOM   2488 N  NE2   . GLN B 1 164 ? 58.468  26.261  20.931  1.00 31.55 ? 163 GLN D NE2   1 
ATOM   2489 N  N     . LEU B 1 165 ? 55.592  26.363  16.353  1.00 34.97 ? 164 LEU D N     1 
ATOM   2490 C  CA    . LEU B 1 165 ? 56.243  27.190  15.317  1.00 36.58 ? 164 LEU D CA    1 
ATOM   2491 C  C     . LEU B 1 165 ? 57.463  27.937  15.836  1.00 38.67 ? 164 LEU D C     1 
ATOM   2492 O  O     . LEU B 1 165 ? 57.463  28.408  16.982  1.00 40.54 ? 164 LEU D O     1 
ATOM   2493 C  CB    . LEU B 1 165 ? 55.248  28.179  14.674  1.00 32.60 ? 164 LEU D CB    1 
ATOM   2494 C  CG    . LEU B 1 165 ? 53.906  27.608  14.280  1.00 31.65 ? 164 LEU D CG    1 
ATOM   2495 C  CD1   . LEU B 1 165 ? 52.857  28.650  13.849  1.00 37.13 ? 164 LEU D CD1   1 
ATOM   2496 C  CD2   . LEU B 1 165 ? 54.222  26.735  13.091  1.00 36.60 ? 164 LEU D CD2   1 
ATOM   2497 N  N     . GLY C 2 1   ? 28.576  42.792  29.401  1.00 53.57 ? 0   GLY A N     1 
ATOM   2498 C  CA    . GLY C 2 1   ? 28.118  41.759  28.490  1.00 50.42 ? 0   GLY A CA    1 
ATOM   2499 C  C     . GLY C 2 1   ? 27.438  42.297  27.240  1.00 48.73 ? 0   GLY A C     1 
ATOM   2500 O  O     . GLY C 2 1   ? 27.042  43.479  27.156  1.00 47.75 ? 0   GLY A O     1 
ATOM   2501 N  N     . MET C 2 2   ? 27.316  41.434  26.240  1.00 45.65 ? 1   MET A N     1 
ATOM   2502 C  CA    . MET C 2 2   ? 26.657  41.838  25.014  1.00 43.59 ? 1   MET A CA    1 
ATOM   2503 C  C     . MET C 2 2   ? 25.169  41.571  25.135  1.00 42.29 ? 1   MET A C     1 
ATOM   2504 O  O     . MET C 2 2   ? 24.723  40.646  25.819  1.00 42.17 ? 1   MET A O     1 
ATOM   2505 C  CB    . MET C 2 2   ? 27.324  41.156  23.792  1.00 40.01 ? 1   MET A CB    1 
ATOM   2506 C  CG    . MET C 2 2   ? 27.407  39.672  23.793  1.00 35.52 ? 1   MET A CG    1 
ATOM   2507 S  SD    . MET C 2 2   ? 27.949  38.953  22.208  1.00 32.97 ? 1   MET A SD    1 
ATOM   2508 C  CE    . MET C 2 2   ? 29.743  38.830  22.512  1.00 32.75 ? 1   MET A CE    1 
ATOM   2509 N  N     . THR C 2 3   ? 24.396  42.452  24.526  1.00 41.78 ? 2   THR A N     1 
ATOM   2510 C  CA    . THR C 2 3   ? 22.956  42.313  24.598  1.00 40.25 ? 2   THR A CA    1 
ATOM   2511 C  C     . THR C 2 3   ? 22.519  41.124  23.748  1.00 38.85 ? 2   THR A C     1 
ATOM   2512 O  O     . THR C 2 3   ? 23.084  40.863  22.681  1.00 34.98 ? 2   THR A O     1 
ATOM   2513 C  CB    . THR C 2 3   ? 22.296  43.586  24.095  1.00 40.07 ? 2   THR A CB    1 
ATOM   2514 O  OG1   . THR C 2 3   ? 22.630  44.669  24.970  1.00 42.20 ? 2   THR A OG1   1 
ATOM   2515 C  CG2   . THR C 2 3   ? 20.788  43.396  24.078  1.00 39.60 ? 2   THR A CG2   1 
ATOM   2516 N  N     . GLU C 2 4   ? 21.516  40.393  24.223  1.00 36.96 ? 3   GLU A N     1 
ATOM   2517 C  CA    . GLU C 2 4   ? 20.979  39.253  23.498  1.00 32.39 ? 3   GLU A CA    1 
ATOM   2518 C  C     . GLU C 2 4   ? 19.639  39.641  22.880  1.00 33.26 ? 3   GLU A C     1 
ATOM   2519 O  O     . GLU C 2 4   ? 18.825  40.309  23.519  1.00 34.45 ? 3   GLU A O     1 
ATOM   2520 C  CB    . GLU C 2 4   ? 20.771  38.066  24.442  1.00 36.56 ? 3   GLU A CB    1 
ATOM   2521 C  CG    . GLU C 2 4   ? 19.509  37.234  24.119  1.00 41.22 ? 3   GLU A CG    1 
ATOM   2522 C  CD    . GLU C 2 4   ? 19.569  35.844  24.750  1.00 44.95 ? 3   GLU A CD    1 
ATOM   2523 O  OE1   . GLU C 2 4   ? 18.782  34.935  24.358  1.00 40.47 ? 3   GLU A OE1   1 
ATOM   2524 O  OE2   . GLU C 2 4   ? 20.343  35.725  25.740  1.00 45.69 ? 3   GLU A OE2   1 
ATOM   2525 N  N     . TYR C 2 5   ? 19.402  39.211  21.643  1.00 30.24 ? 4   TYR A N     1 
ATOM   2526 C  CA    . TYR C 2 5   ? 18.199  39.542  20.886  1.00 28.02 ? 4   TYR A CA    1 
ATOM   2527 C  C     . TYR C 2 5   ? 17.512  38.226  20.522  1.00 28.71 ? 4   TYR A C     1 
ATOM   2528 O  O     . TYR C 2 5   ? 18.105  37.395  19.830  1.00 27.82 ? 4   TYR A O     1 
ATOM   2529 C  CB    . TYR C 2 5   ? 18.555  40.326  19.609  1.00 29.47 ? 4   TYR A CB    1 
ATOM   2530 C  CG    . TYR C 2 5   ? 19.134  41.690  19.919  1.00 29.24 ? 4   TYR A CG    1 
ATOM   2531 C  CD1   . TYR C 2 5   ? 18.286  42.752  20.215  1.00 32.00 ? 4   TYR A CD1   1 
ATOM   2532 C  CD2   . TYR C 2 5   ? 20.516  41.898  20.021  1.00 33.96 ? 4   TYR A CD2   1 
ATOM   2533 C  CE1   . TYR C 2 5   ? 18.785  43.999  20.558  1.00 31.72 ? 4   TYR A CE1   1 
ATOM   2534 C  CE2   . TYR C 2 5   ? 21.025  43.177  20.368  1.00 33.73 ? 4   TYR A CE2   1 
ATOM   2535 C  CZ    . TYR C 2 5   ? 20.128  44.218  20.637  1.00 35.10 ? 4   TYR A CZ    1 
ATOM   2536 O  OH    . TYR C 2 5   ? 20.565  45.484  20.996  1.00 33.88 ? 4   TYR A OH    1 
ATOM   2537 N  N     . LYS C 2 6   ? 16.262  38.038  20.964  1.00 27.12 ? 5   LYS A N     1 
ATOM   2538 C  CA    . LYS C 2 6   ? 15.547  36.787  20.703  1.00 25.12 ? 5   LYS A CA    1 
ATOM   2539 C  C     . LYS C 2 6   ? 14.699  36.949  19.452  1.00 24.23 ? 5   LYS A C     1 
ATOM   2540 O  O     . LYS C 2 6   ? 13.657  37.606  19.452  1.00 23.91 ? 5   LYS A O     1 
ATOM   2541 C  CB    . LYS C 2 6   ? 14.694  36.406  21.896  1.00 27.81 ? 5   LYS A CB    1 
ATOM   2542 C  CG    . LYS C 2 6   ? 15.513  36.202  23.120  1.00 30.35 ? 5   LYS A CG    1 
ATOM   2543 C  CD    . LYS C 2 6   ? 14.580  35.810  24.248  1.00 35.02 ? 5   LYS A CD    1 
ATOM   2544 C  CE    . LYS C 2 6   ? 15.246  36.028  25.591  1.00 42.67 ? 5   LYS A CE    1 
ATOM   2545 N  NZ    . LYS C 2 6   ? 16.531  35.272  25.595  1.00 50.02 ? 5   LYS A NZ    1 
ATOM   2546 N  N     . LEU C 2 7   ? 15.165  36.388  18.376  1.00 24.62 ? 6   LEU A N     1 
ATOM   2547 C  CA    . LEU C 2 7   ? 14.519  36.496  17.081  1.00 23.09 ? 6   LEU A CA    1 
ATOM   2548 C  C     . LEU C 2 7   ? 13.808  35.182  16.761  1.00 22.04 ? 6   LEU A C     1 
ATOM   2549 O  O     . LEU C 2 7   ? 14.316  34.103  17.067  1.00 23.35 ? 6   LEU A O     1 
ATOM   2550 C  CB    . LEU C 2 7   ? 15.573  36.791  15.998  1.00 20.97 ? 6   LEU A CB    1 
ATOM   2551 C  CG    . LEU C 2 7   ? 16.607  37.888  16.243  1.00 24.92 ? 6   LEU A CG    1 
ATOM   2552 C  CD1   . LEU C 2 7   ? 17.434  38.190  14.920  1.00 21.86 ? 6   LEU A CD1   1 
ATOM   2553 C  CD2   . LEU C 2 7   ? 16.026  39.102  16.847  1.00 26.38 ? 6   LEU A CD2   1 
ATOM   2554 N  N     . VAL C 2 8   ? 12.643  35.274  16.132  1.00 22.12 ? 7   VAL A N     1 
ATOM   2555 C  CA    . VAL C 2 8   ? 11.836  34.101  15.814  1.00 20.48 ? 7   VAL A CA    1 
ATOM   2556 C  C     . VAL C 2 8   ? 11.479  34.182  14.343  1.00 21.46 ? 7   VAL A C     1 
ATOM   2557 O  O     . VAL C 2 8   ? 11.040  35.239  13.874  1.00 21.12 ? 7   VAL A O     1 
ATOM   2558 C  CB    . VAL C 2 8   ? 10.549  34.026  16.662  1.00 23.06 ? 7   VAL A CB    1 
ATOM   2559 C  CG1   . VAL C 2 8   ? 9.760   32.769  16.301  1.00 19.69 ? 7   VAL A CG1   1 
ATOM   2560 C  CG2   . VAL C 2 8   ? 10.908  33.982  18.180  1.00 22.64 ? 7   VAL A CG2   1 
ATOM   2561 N  N     . VAL C 2 9   ? 11.740  33.096  13.605  1.00 16.90 ? 8   VAL A N     1 
ATOM   2562 C  CA    . VAL C 2 9   ? 11.514  33.050  12.154  1.00 19.62 ? 8   VAL A CA    1 
ATOM   2563 C  C     . VAL C 2 9   ? 10.234  32.263  11.929  1.00 20.95 ? 8   VAL A C     1 
ATOM   2564 O  O     . VAL C 2 9   ? 10.119  31.107  12.368  1.00 18.69 ? 8   VAL A O     1 
ATOM   2565 C  CB    . VAL C 2 9   ? 12.701  32.421  11.409  1.00 18.11 ? 8   VAL A CB    1 
ATOM   2566 C  CG1   . VAL C 2 9   ? 12.480  32.544  9.876   1.00 20.29 ? 8   VAL A CG1   1 
ATOM   2567 C  CG2   . VAL C 2 9   ? 13.999  33.121  11.810  1.00 19.76 ? 8   VAL A CG2   1 
ATOM   2568 N  N     . VAL C 2 10  ? 9.232   32.900  11.296  1.00 19.67 ? 9   VAL A N     1 
ATOM   2569 C  CA    . VAL C 2 10  ? 7.914   32.310  11.143  1.00 19.28 ? 9   VAL A CA    1 
ATOM   2570 C  C     . VAL C 2 10  ? 7.457   32.461  9.690   1.00 24.31 ? 9   VAL A C     1 
ATOM   2571 O  O     . VAL C 2 10  ? 7.947   33.315  8.952   1.00 22.84 ? 9   VAL A O     1 
ATOM   2572 C  CB    . VAL C 2 10  ? 6.842   32.977  12.070  1.00 23.74 ? 9   VAL A CB    1 
ATOM   2573 C  CG1   . VAL C 2 10  ? 7.342   33.013  13.465  1.00 24.61 ? 9   VAL A CG1   1 
ATOM   2574 C  CG2   . VAL C 2 10  ? 6.567   34.459  11.620  1.00 22.24 ? 9   VAL A CG2   1 
ATOM   2575 N  N     . GLY C 2 11  ? 6.448   31.673  9.321   1.00 23.10 ? 10  GLY A N     1 
ATOM   2576 C  CA    . GLY C 2 11  ? 5.890   31.661  7.967   1.00 22.52 ? 10  GLY A CA    1 
ATOM   2577 C  C     . GLY C 2 11  ? 5.467   30.257  7.574   1.00 25.52 ? 10  GLY A C     1 
ATOM   2578 O  O     . GLY C 2 11  ? 5.797   29.265  8.248   1.00 24.69 ? 10  GLY A O     1 
ATOM   2579 N  N     . ALA C 2 12  ? 4.742   30.163  6.438   1.00 24.47 ? 11  ALA A N     1 
ATOM   2580 C  CA    . ALA C 2 12  ? 4.302   28.864  5.940   1.00 24.29 ? 11  ALA A CA    1 
ATOM   2581 C  C     . ALA C 2 12  ? 5.506   27.983  5.647   1.00 24.40 ? 11  ALA A C     1 
ATOM   2582 O  O     . ALA C 2 12  ? 6.569   28.464  5.285   1.00 24.16 ? 11  ALA A O     1 
ATOM   2583 C  CB    . ALA C 2 12  ? 3.497   29.014  4.632   1.00 29.51 ? 11  ALA A CB    1 
ATOM   2584 N  N     . ASP C 2 13  ? 5.360   26.676  5.813   1.00 27.09 ? 12  ASP A N     1 
ATOM   2585 C  CA    . ASP C 2 13  ? 6.533   25.844  5.514   1.00 26.08 ? 12  ASP A CA    1 
ATOM   2586 C  C     . ASP C 2 13  ? 6.825   25.857  4.004   1.00 23.80 ? 12  ASP A C     1 
ATOM   2587 O  O     . ASP C 2 13  ? 5.956   26.112  3.163   1.00 26.19 ? 12  ASP A O     1 
ATOM   2588 C  CB    . ASP C 2 13  ? 6.353   24.410  6.046   1.00 28.26 ? 12  ASP A CB    1 
ATOM   2589 C  CG    . ASP C 2 13  ? 6.512   24.325  7.604   1.00 26.10 ? 12  ASP A CG    1 
ATOM   2590 O  OD1   . ASP C 2 13  ? 7.304   25.126  8.137   1.00 24.54 ? 12  ASP A OD1   1 
ATOM   2591 O  OD2   . ASP C 2 13  ? 5.848   23.471  8.261   1.00 30.32 ? 12  ASP A OD2   1 
ATOM   2592 N  N     . GLY C 2 14  ? 8.077   25.640  3.683   1.00 23.00 ? 13  GLY A N     1 
ATOM   2593 C  CA    . GLY C 2 14  ? 8.569   25.672  2.325   1.00 26.05 ? 13  GLY A CA    1 
ATOM   2594 C  C     . GLY C 2 14  ? 9.002   27.027  1.827   1.00 22.88 ? 13  GLY A C     1 
ATOM   2595 O  O     . GLY C 2 14  ? 9.494   27.122  0.692   1.00 26.95 ? 13  GLY A O     1 
ATOM   2596 N  N     . VAL C 2 15  ? 8.876   28.079  2.644   1.00 23.42 ? 14  VAL A N     1 
ATOM   2597 C  CA    . VAL C 2 15  ? 9.238   29.415  2.161   1.00 22.73 ? 14  VAL A CA    1 
ATOM   2598 C  C     . VAL C 2 15  ? 10.722  29.695  2.290   1.00 21.85 ? 14  VAL A C     1 
ATOM   2599 O  O     . VAL C 2 15  ? 11.239  30.582  1.601   1.00 21.62 ? 14  VAL A O     1 
ATOM   2600 C  CB    . VAL C 2 15  ? 8.490   30.522  2.905   1.00 21.41 ? 14  VAL A CB    1 
ATOM   2601 C  CG1   . VAL C 2 15  ? 6.979   30.343  2.738   1.00 25.05 ? 14  VAL A CG1   1 
ATOM   2602 C  CG2   . VAL C 2 15  ? 8.865   30.493  4.400   1.00 22.40 ? 14  VAL A CG2   1 
ATOM   2603 N  N     . GLY C 2 16  ? 11.428  28.945  3.134   1.00 19.92 ? 15  GLY A N     1 
ATOM   2604 C  CA    . GLY C 2 16  ? 12.821  29.186  3.350   1.00 19.26 ? 15  GLY A CA    1 
ATOM   2605 C  C     . GLY C 2 16  ? 13.205  29.707  4.722   1.00 19.74 ? 15  GLY A C     1 
ATOM   2606 O  O     . GLY C 2 16  ? 14.293  30.285  4.849   1.00 18.59 ? 15  GLY A O     1 
ATOM   2607 N  N     . LYS C 2 17  ? 12.349  29.550  5.743   1.00 18.94 ? 16  LYS A N     1 
ATOM   2608 C  CA    . LYS C 2 17  ? 12.740  29.927  7.108   1.00 18.73 ? 16  LYS A CA    1 
ATOM   2609 C  C     . LYS C 2 17  ? 14.054  29.281  7.510   1.00 18.35 ? 16  LYS A C     1 
ATOM   2610 O  O     . LYS C 2 17  ? 14.953  29.945  8.036   1.00 18.51 ? 16  LYS A O     1 
ATOM   2611 C  CB    . LYS C 2 17  ? 11.638  29.484  8.092   1.00 19.10 ? 16  LYS A CB    1 
ATOM   2612 C  CG    . LYS C 2 17  ? 10.307  30.169  7.777   1.00 19.31 ? 16  LYS A CG    1 
ATOM   2613 C  CD    . LYS C 2 17  ? 9.238   29.776  8.777   1.00 19.82 ? 16  LYS A CD    1 
ATOM   2614 C  CE    . LYS C 2 17  ? 9.084   28.293  8.821   1.00 22.40 ? 16  LYS A CE    1 
ATOM   2615 N  NZ    . LYS C 2 17  ? 8.295   27.710  7.693   1.00 25.08 ? 16  LYS A NZ    1 
ATOM   2616 N  N     . SER C 2 18  ? 14.160  27.968  7.316   1.00 17.41 ? 17  SER A N     1 
ATOM   2617 C  CA    . SER C 2 18  ? 15.342  27.245  7.774   1.00 17.28 ? 17  SER A CA    1 
ATOM   2618 C  C     . SER C 2 18  ? 16.548  27.561  6.878   1.00 19.23 ? 17  SER A C     1 
ATOM   2619 O  O     . SER C 2 18  ? 17.669  27.734  7.366   1.00 17.21 ? 17  SER A O     1 
ATOM   2620 C  CB    . SER C 2 18  ? 15.071  25.749  7.778   1.00 18.02 ? 17  SER A CB    1 
ATOM   2621 O  OG    . SER C 2 18  ? 14.046  25.449  8.718   1.00 18.44 ? 17  SER A OG    1 
ATOM   2622 N  N     . ALA C 2 19  ? 16.336  27.642  5.567   1.00 19.78 ? 18  ALA A N     1 
ATOM   2623 C  CA    . ALA C 2 19  ? 17.436  27.988  4.685   1.00 15.96 ? 18  ALA A CA    1 
ATOM   2624 C  C     . ALA C 2 19  ? 18.010  29.379  5.021   1.00 17.74 ? 18  ALA A C     1 
ATOM   2625 O  O     . ALA C 2 19  ? 19.231  29.574  4.970   1.00 18.98 ? 18  ALA A O     1 
ATOM   2626 C  CB    . ALA C 2 19  ? 16.937  27.882  3.238   1.00 18.91 ? 18  ALA A CB    1 
ATOM   2627 N  N     . LEU C 2 20  ? 17.155  30.346  5.353   1.00 18.72 ? 19  LEU A N     1 
ATOM   2628 C  CA    . LEU C 2 20  ? 17.656  31.676  5.731   1.00 19.45 ? 19  LEU A CA    1 
ATOM   2629 C  C     . LEU C 2 20  ? 18.475  31.594  7.019   1.00 18.62 ? 19  LEU A C     1 
ATOM   2630 O  O     . LEU C 2 20  ? 19.569  32.163  7.110   1.00 20.76 ? 19  LEU A O     1 
ATOM   2631 C  CB    . LEU C 2 20  ? 16.495  32.660  5.929   1.00 17.82 ? 19  LEU A CB    1 
ATOM   2632 C  CG    . LEU C 2 20  ? 15.857  33.201  4.644   1.00 20.62 ? 19  LEU A CG    1 
ATOM   2633 C  CD1   . LEU C 2 20  ? 14.558  33.925  5.011   1.00 20.61 ? 19  LEU A CD1   1 
ATOM   2634 C  CD2   . LEU C 2 20  ? 16.827  34.110  3.845   1.00 20.19 ? 19  LEU A CD2   1 
ATOM   2635 N  N     . THR C 2 21  ? 17.939  30.880  7.996   1.00 16.19 ? 20  THR A N     1 
ATOM   2636 C  CA    . THR C 2 21  ? 18.599  30.697  9.288   1.00 16.96 ? 20  THR A CA    1 
ATOM   2637 C  C     . THR C 2 21  ? 19.929  29.996  9.126   1.00 18.19 ? 20  THR A C     1 
ATOM   2638 O  O     . THR C 2 21  ? 20.932  30.445  9.676   1.00 18.68 ? 20  THR A O     1 
ATOM   2639 C  CB    . THR C 2 21  ? 17.699  29.899  10.226  1.00 17.12 ? 20  THR A CB    1 
ATOM   2640 O  OG1   . THR C 2 21  ? 16.504  30.640  10.462  1.00 18.22 ? 20  THR A OG1   1 
ATOM   2641 C  CG2   . THR C 2 21  ? 18.393  29.696  11.525  1.00 16.23 ? 20  THR A CG2   1 
ATOM   2642 N  N     . ILE C 2 22  ? 19.952  28.861  8.397   1.00 15.04 ? 21  ILE A N     1 
ATOM   2643 C  CA    . ILE C 2 22  ? 21.231  28.147  8.191   1.00 14.31 ? 21  ILE A CA    1 
ATOM   2644 C  C     . ILE C 2 22  ? 22.225  28.975  7.403   1.00 17.59 ? 21  ILE A C     1 
ATOM   2645 O  O     . ILE C 2 22  ? 23.440  28.895  7.652   1.00 19.80 ? 21  ILE A O     1 
ATOM   2646 C  CB    . ILE C 2 22  ? 21.002  26.789  7.535   1.00 18.58 ? 21  ILE A CB    1 
ATOM   2647 C  CG1   . ILE C 2 22  ? 20.164  25.859  8.467   1.00 21.40 ? 21  ILE A CG1   1 
ATOM   2648 C  CG2   . ILE C 2 22  ? 22.372  26.115  7.193   1.00 20.22 ? 21  ILE A CG2   1 
ATOM   2649 C  CD1   . ILE C 2 22  ? 20.744  25.643  9.816   1.00 23.43 ? 21  ILE A CD1   1 
ATOM   2650 N  N     . GLN C 2 23  ? 21.773  29.803  6.473   1.00 16.71 ? 22  GLN A N     1 
ATOM   2651 C  CA    . GLN C 2 23  ? 22.743  30.713  5.843   1.00 18.21 ? 22  GLN A CA    1 
ATOM   2652 C  C     . GLN C 2 23  ? 23.357  31.662  6.866   1.00 21.60 ? 22  GLN A C     1 
ATOM   2653 O  O     . GLN C 2 23  ? 24.563  31.981  6.824   1.00 21.41 ? 22  GLN A O     1 
ATOM   2654 C  CB    . GLN C 2 23  ? 22.070  31.555  4.773   1.00 21.66 ? 22  GLN A CB    1 
ATOM   2655 C  CG    . GLN C 2 23  ? 22.116  31.013  3.428   1.00 23.07 ? 22  GLN A CG    1 
ATOM   2656 C  CD    . GLN C 2 23  ? 23.543  30.837  2.820   1.00 24.10 ? 22  GLN A CD    1 
ATOM   2657 O  OE1   . GLN C 2 23  ? 24.590  31.138  3.439   1.00 25.24 ? 22  GLN A OE1   1 
ATOM   2658 N  NE2   . GLN C 2 23  ? 23.566  30.328  1.601   1.00 22.63 ? 22  GLN A NE2   1 
ATOM   2659 N  N     . LEU C 2 24  ? 22.510  32.295  7.660   1.00 17.49 ? 23  LEU A N     1 
ATOM   2660 C  CA    . LEU C 2 24  ? 23.027  33.187  8.673   1.00 19.99 ? 23  LEU A CA    1 
ATOM   2661 C  C     . LEU C 2 24  ? 24.040  32.472  9.551   1.00 19.87 ? 23  LEU A C     1 
ATOM   2662 O  O     . LEU C 2 24  ? 25.103  33.006  9.849   1.00 19.55 ? 23  LEU A O     1 
ATOM   2663 C  CB    . LEU C 2 24  ? 21.878  33.722  9.513   1.00 20.32 ? 23  LEU A CB    1 
ATOM   2664 C  CG    . LEU C 2 24  ? 22.246  34.708  10.625  1.00 20.21 ? 23  LEU A CG    1 
ATOM   2665 C  CD1   . LEU C 2 24  ? 22.641  36.075  10.055  1.00 22.99 ? 23  LEU A CD1   1 
ATOM   2666 C  CD2   . LEU C 2 24  ? 21.076  34.793  11.652  1.00 21.96 ? 23  LEU A CD2   1 
ATOM   2667 N  N     . ILE C 2 25  ? 23.692  31.269  10.034  1.00 20.02 ? 24  ILE A N     1 
ATOM   2668 C  CA    . ILE C 2 25  ? 24.496  30.664  11.098  1.00 19.76 ? 24  ILE A CA    1 
ATOM   2669 C  C     . ILE C 2 25  ? 25.740  30.026  10.501  1.00 23.49 ? 24  ILE A C     1 
ATOM   2670 O  O     . ILE C 2 25  ? 26.867  30.130  11.044  1.00 22.71 ? 24  ILE A O     1 
ATOM   2671 C  CB    . ILE C 2 25  ? 23.645  29.614  11.841  1.00 21.19 ? 24  ILE A CB    1 
ATOM   2672 C  CG1   . ILE C 2 25  ? 22.363  30.233  12.480  1.00 21.71 ? 24  ILE A CG1   1 
ATOM   2673 C  CG2   . ILE C 2 25  ? 24.517  28.881  12.828  1.00 21.97 ? 24  ILE A CG2   1 
ATOM   2674 C  CD1   . ILE C 2 25  ? 22.659  31.390  13.477  1.00 20.56 ? 24  ILE A CD1   1 
ATOM   2675 N  N     . GLN C 2 26  ? 25.545  29.320  9.385   1.00 22.49 ? 25  GLN A N     1 
ATOM   2676 C  CA    . GLN C 2 26  ? 26.605  28.476  8.830   1.00 23.71 ? 25  GLN A CA    1 
ATOM   2677 C  C     . GLN C 2 26  ? 27.128  28.871  7.454   1.00 25.43 ? 25  GLN A C     1 
ATOM   2678 O  O     . GLN C 2 26  ? 28.124  28.280  7.001   1.00 25.04 ? 25  GLN A O     1 
ATOM   2679 C  CB    . GLN C 2 26  ? 26.098  27.044  8.759   1.00 23.88 ? 25  GLN A CB    1 
ATOM   2680 C  CG    . GLN C 2 26  ? 25.669  26.498  10.126  1.00 24.45 ? 25  GLN A CG    1 
ATOM   2681 C  CD    . GLN C 2 26  ? 25.246  25.044  10.040  1.00 33.59 ? 25  GLN A CD    1 
ATOM   2682 O  OE1   . GLN C 2 26  ? 25.368  24.413  8.981   1.00 34.83 ? 25  GLN A OE1   1 
ATOM   2683 N  NE2   . GLN C 2 26  ? 24.773  24.498  11.155  1.00 35.77 ? 25  GLN A NE2   1 
ATOM   2684 N  N     . ASN C 2 27  ? 26.486  29.797  6.759   1.00 23.51 ? 26  ASN A N     1 
ATOM   2685 C  CA    . ASN C 2 27  ? 27.000  30.343  5.492   1.00 23.79 ? 26  ASN A CA    1 
ATOM   2686 C  C     . ASN C 2 27  ? 27.043  29.246  4.404   1.00 26.23 ? 26  ASN A C     1 
ATOM   2687 O  O     . ASN C 2 27  ? 27.954  29.176  3.574   1.00 26.26 ? 26  ASN A O     1 
ATOM   2688 C  CB    . ASN C 2 27  ? 28.377  30.992  5.682   1.00 22.04 ? 26  ASN A CB    1 
ATOM   2689 C  CG    . ASN C 2 27  ? 28.572  32.294  4.812   1.00 27.49 ? 26  ASN A CG    1 
ATOM   2690 O  OD1   . ASN C 2 27  ? 28.275  33.393  5.293   1.00 27.26 ? 26  ASN A OD1   1 
ATOM   2691 N  ND2   . ASN C 2 27  ? 28.977  32.153  3.499   1.00 24.61 ? 26  ASN A ND2   1 
ATOM   2692 N  N     . HIS C 2 28  ? 26.031  28.380  4.375   1.00 23.81 ? 27  HIS A N     1 
ATOM   2693 C  CA    . HIS C 2 28  ? 25.841  27.530  3.208   1.00 28.93 ? 27  HIS A CA    1 
ATOM   2694 C  C     . HIS C 2 28  ? 24.343  27.319  3.046   1.00 24.15 ? 27  HIS A C     1 
ATOM   2695 O  O     . HIS C 2 28  ? 23.542  27.700  3.910   1.00 24.63 ? 27  HIS A O     1 
ATOM   2696 C  CB    . HIS C 2 28  ? 26.597  26.200  3.316   1.00 32.15 ? 27  HIS A CB    1 
ATOM   2697 C  CG    . HIS C 2 28  ? 25.984  25.269  4.313   1.00 31.31 ? 27  HIS A CG    1 
ATOM   2698 N  ND1   . HIS C 2 28  ? 24.996  24.369  3.986   1.00 35.63 ? 27  HIS A ND1   1 
ATOM   2699 C  CD2   . HIS C 2 28  ? 26.152  25.173  5.647   1.00 33.26 ? 27  HIS A CD2   1 
ATOM   2700 C  CE1   . HIS C 2 28  ? 24.612  23.719  5.063   1.00 34.09 ? 27  HIS A CE1   1 
ATOM   2701 N  NE2   . HIS C 2 28  ? 25.292  24.197  6.092   1.00 37.46 ? 27  HIS A NE2   1 
ATOM   2702 N  N     . PHE C 2 29  ? 23.976  26.750  1.907   1.00 28.40 ? 28  PHE A N     1 
ATOM   2703 C  CA    . PHE C 2 29  ? 22.584  26.696  1.473   1.00 26.65 ? 28  PHE A CA    1 
ATOM   2704 C  C     . PHE C 2 29  ? 22.056  25.258  1.488   1.00 33.00 ? 28  PHE A C     1 
ATOM   2705 O  O     . PHE C 2 29  ? 22.528  24.414  0.740   1.00 34.43 ? 28  PHE A O     1 
ATOM   2706 C  CB    . PHE C 2 29  ? 22.433  27.350  0.101   1.00 26.94 ? 28  PHE A CB    1 
ATOM   2707 C  CG    . PHE C 2 29  ? 21.085  27.100  -0.548  1.00 27.29 ? 28  PHE A CG    1 
ATOM   2708 C  CD1   . PHE C 2 29  ? 19.929  27.608  0.024   1.00 28.64 ? 28  PHE A CD1   1 
ATOM   2709 C  CD2   . PHE C 2 29  ? 20.988  26.345  -1.697  1.00 28.53 ? 28  PHE A CD2   1 
ATOM   2710 C  CE1   . PHE C 2 29  ? 18.667  27.360  -0.542  1.00 27.91 ? 28  PHE A CE1   1 
ATOM   2711 C  CE2   . PHE C 2 29  ? 19.733  26.093  -2.286  1.00 30.43 ? 28  PHE A CE2   1 
ATOM   2712 C  CZ    . PHE C 2 29  ? 18.583  26.602  -1.716  1.00 25.98 ? 28  PHE A CZ    1 
ATOM   2713 N  N     . VAL C 2 30  ? 21.053  25.002  2.337   1.00 34.23 ? 29  VAL A N     1 
ATOM   2714 C  CA    . VAL C 2 30  ? 20.423  23.687  2.444   1.00 37.30 ? 29  VAL A CA    1 
ATOM   2715 C  C     . VAL C 2 30  ? 19.527  23.486  1.212   1.00 35.80 ? 29  VAL A C     1 
ATOM   2716 O  O     . VAL C 2 30  ? 18.490  24.127  1.081   1.00 36.31 ? 29  VAL A O     1 
ATOM   2717 C  CB    . VAL C 2 30  ? 19.623  23.571  3.756   1.00 37.91 ? 29  VAL A CB    1 
ATOM   2718 C  CG1   . VAL C 2 30  ? 18.643  22.399  3.721   1.00 39.02 ? 29  VAL A CG1   1 
ATOM   2719 C  CG2   . VAL C 2 30  ? 20.571  23.377  4.924   1.00 38.21 ? 29  VAL A CG2   1 
ATOM   2720 N  N     . ASP C 2 31  ? 19.947  22.636  0.281   1.00 34.60 ? 30  ASP A N     1 
ATOM   2721 C  CA    . ASP C 2 31  ? 19.121  22.463  -0.904  1.00 36.59 ? 30  ASP A CA    1 
ATOM   2722 C  C     . ASP C 2 31  ? 17.955  21.505  -0.643  1.00 37.27 ? 30  ASP A C     1 
ATOM   2723 O  O     . ASP C 2 31  ? 16.892  21.623  -1.261  1.00 40.52 ? 30  ASP A O     1 
ATOM   2724 C  CB    . ASP C 2 31  ? 19.972  21.969  -2.046  1.00 41.58 ? 30  ASP A CB    1 
ATOM   2725 C  CG    . ASP C 2 31  ? 19.393  22.341  -3.387  1.00 45.71 ? 30  ASP A CG    1 
ATOM   2726 O  OD1   . ASP C 2 31  ? 20.163  22.882  -4.202  1.00 55.14 ? 30  ASP A OD1   1 
ATOM   2727 O  OD2   . ASP C 2 31  ? 18.176  22.157  -3.609  1.00 52.95 ? 30  ASP A OD2   1 
ATOM   2728 N  N     . GLU C 2 32  ? 18.110  20.618  0.325   1.00 35.03 ? 31  GLU A N     1 
ATOM   2729 C  CA    . GLU C 2 32  ? 17.154  19.567  0.605   1.00 33.78 ? 31  GLU A CA    1 
ATOM   2730 C  C     . GLU C 2 32  ? 16.056  20.105  1.510   1.00 30.19 ? 31  GLU A C     1 
ATOM   2731 O  O     . GLU C 2 32  ? 16.202  21.153  2.141   1.00 29.97 ? 31  GLU A O     1 
ATOM   2732 C  CB    . GLU C 2 32  ? 17.897  18.375  1.239   1.00 33.42 ? 31  GLU A CB    1 
ATOM   2733 C  CG    . GLU C 2 32  ? 19.153  17.949  0.443   1.00 34.16 ? 31  GLU A CG    1 
ATOM   2734 C  CD    . GLU C 2 32  ? 19.941  16.838  1.121   1.00 34.94 ? 31  GLU A CD    1 
ATOM   2735 O  OE1   . GLU C 2 32  ? 20.023  16.886  2.363   1.00 34.08 ? 31  GLU A OE1   1 
ATOM   2736 O  OE2   . GLU C 2 32  ? 20.469  15.950  0.430   1.00 39.20 ? 31  GLU A OE2   1 
ATOM   2737 N  N     . TYR C 2 33  ? 14.917  19.407  1.532   1.00 27.36 ? 32  TYR A N     1 
ATOM   2738 C  CA    . TYR C 2 33  ? 13.765  19.851  2.329   1.00 24.58 ? 32  TYR A CA    1 
ATOM   2739 C  C     . TYR C 2 33  ? 13.685  19.024  3.607   1.00 24.54 ? 32  TYR A C     1 
ATOM   2740 O  O     . TYR C 2 33  ? 13.440  17.813  3.542   1.00 22.68 ? 32  TYR A O     1 
ATOM   2741 C  CB    . TYR C 2 33  ? 12.470  19.705  1.546   1.00 23.40 ? 32  TYR A CB    1 
ATOM   2742 C  CG    . TYR C 2 33  ? 11.268  20.252  2.300   1.00 23.41 ? 32  TYR A CG    1 
ATOM   2743 C  CD1   . TYR C 2 33  ? 10.052  19.580  2.218   1.00 27.85 ? 32  TYR A CD1   1 
ATOM   2744 C  CD2   . TYR C 2 33  ? 11.351  21.427  3.084   1.00 24.44 ? 32  TYR A CD2   1 
ATOM   2745 C  CE1   . TYR C 2 33  ? 8.918   20.049  2.848   1.00 29.81 ? 32  TYR A CE1   1 
ATOM   2746 C  CE2   . TYR C 2 33  ? 10.202  21.915  3.759   1.00 24.92 ? 32  TYR A CE2   1 
ATOM   2747 C  CZ    . TYR C 2 33  ? 8.995   21.212  3.625   1.00 28.46 ? 32  TYR A CZ    1 
ATOM   2748 O  OH    . TYR C 2 33  ? 7.797   21.600  4.216   1.00 30.34 ? 32  TYR A OH    1 
ATOM   2749 N  N     . ASP C 2 34  ? 13.896  19.682  4.756   1.00 24.10 ? 33  ASP A N     1 
ATOM   2750 C  CA    . ASP C 2 34  ? 13.874  19.032  6.063   1.00 22.94 ? 33  ASP A CA    1 
ATOM   2751 C  C     . ASP C 2 34  ? 12.856  19.803  6.886   1.00 24.99 ? 33  ASP A C     1 
ATOM   2752 O  O     . ASP C 2 34  ? 13.206  20.783  7.556   1.00 23.19 ? 33  ASP A O     1 
ATOM   2753 C  CB    . ASP C 2 34  ? 15.261  19.063  6.699   1.00 25.63 ? 33  ASP A CB    1 
ATOM   2754 C  CG    . ASP C 2 34  ? 15.349  18.232  7.975   1.00 28.30 ? 33  ASP A CG    1 
ATOM   2755 O  OD1   . ASP C 2 34  ? 14.385  17.497  8.333   1.00 29.35 ? 33  ASP A OD1   1 
ATOM   2756 O  OD2   . ASP C 2 34  ? 16.405  18.363  8.641   1.00 29.50 ? 33  ASP A OD2   1 
ATOM   2757 N  N     . PRO C 2 35  ? 11.582  19.473  6.772   1.00 23.68 ? 34  PRO A N     1 
ATOM   2758 C  CA    . PRO C 2 35  ? 10.581  20.348  7.401   1.00 23.67 ? 34  PRO A CA    1 
ATOM   2759 C  C     . PRO C 2 35  ? 10.779  20.319  8.904   1.00 24.26 ? 34  PRO A C     1 
ATOM   2760 O  O     . PRO C 2 35  ? 10.972  19.255  9.502   1.00 23.65 ? 34  PRO A O     1 
ATOM   2761 C  CB    . PRO C 2 35  ? 9.226   19.763  6.939   1.00 24.41 ? 34  PRO A CB    1 
ATOM   2762 C  CG    . PRO C 2 35  ? 9.533   18.396  6.556   1.00 23.43 ? 34  PRO A CG    1 
ATOM   2763 C  CD    . PRO C 2 35  ? 10.934  18.406  5.992   1.00 24.79 ? 34  PRO A CD    1 
ATOM   2764 N  N     . THR C 2 36  ? 10.785  21.526  9.484   1.00 23.76 ? 35  THR A N     1 
ATOM   2765 C  CA    . THR C 2 36  ? 11.263  21.810  10.837  1.00 23.38 ? 35  THR A CA    1 
ATOM   2766 C  C     . THR C 2 36  ? 10.299  21.376  11.937  1.00 19.17 ? 35  THR A C     1 
ATOM   2767 O  O     . THR C 2 36  ? 9.073   21.532  11.810  1.00 20.17 ? 35  THR A O     1 
ATOM   2768 C  CB    . THR C 2 36  ? 11.521  23.318  10.906  1.00 19.37 ? 35  THR A CB    1 
ATOM   2769 O  OG1   . THR C 2 36  ? 12.530  23.605  9.938   1.00 16.53 ? 35  THR A OG1   1 
ATOM   2770 C  CG2   . THR C 2 36  ? 12.053  23.791  12.308  1.00 20.55 ? 35  THR A CG2   1 
ATOM   2771 N  N     . ILE C 2 37  ? 10.864  20.826  13.026  1.00 19.49 ? 36  ILE A N     1 
ATOM   2772 C  CA    . ILE C 2 37  ? 10.048  20.677  14.239  1.00 20.29 ? 36  ILE A CA    1 
ATOM   2773 C  C     . ILE C 2 37  ? 10.246  21.943  15.070  1.00 22.18 ? 36  ILE A C     1 
ATOM   2774 O  O     . ILE C 2 37  ? 9.317   22.756  15.227  1.00 21.97 ? 36  ILE A O     1 
ATOM   2775 C  CB    . ILE C 2 37  ? 10.345  19.368  14.974  1.00 20.26 ? 36  ILE A CB    1 
ATOM   2776 C  CG1   . ILE C 2 37  ? 9.835   18.223  14.066  1.00 26.26 ? 36  ILE A CG1   1 
ATOM   2777 C  CG2   . ILE C 2 37  ? 9.629   19.293  16.379  1.00 21.42 ? 36  ILE A CG2   1 
ATOM   2778 C  CD1   . ILE C 2 37  ? 9.808   16.884  14.618  1.00 24.84 ? 36  ILE A CD1   1 
ATOM   2779 N  N     . GLU C 2 38  ? 11.480  22.162  15.540  1.00 20.37 ? 37  GLU A N     1 
ATOM   2780 C  CA    . GLU C 2 38  ? 11.821  23.395  16.243  1.00 21.21 ? 37  GLU A CA    1 
ATOM   2781 C  C     . GLU C 2 38  ? 13.328  23.373  16.387  1.00 19.68 ? 37  GLU A C     1 
ATOM   2782 O  O     . GLU C 2 38  ? 13.860  22.356  16.796  1.00 22.01 ? 37  GLU A O     1 
ATOM   2783 C  CB    . GLU C 2 38  ? 11.168  23.492  17.634  1.00 21.17 ? 37  GLU A CB    1 
ATOM   2784 C  CG    . GLU C 2 38  ? 11.385  24.896  18.204  1.00 27.24 ? 37  GLU A CG    1 
ATOM   2785 C  CD    . GLU C 2 38  ? 10.320  25.271  19.200  1.00 36.27 ? 37  GLU A CD    1 
ATOM   2786 O  OE1   . GLU C 2 38  ? 10.583  25.037  20.375  1.00 37.84 ? 37  GLU A OE1   1 
ATOM   2787 O  OE2   . GLU C 2 38  ? 9.238   25.792  18.799  1.00 38.21 ? 37  GLU A OE2   1 
ATOM   2788 N  N     . ASP C 2 39  ? 14.017  24.452  16.043  1.00 19.90 ? 38  ASP A N     1 
ATOM   2789 C  CA    . ASP C 2 39  ? 15.464  24.501  16.246  1.00 21.15 ? 38  ASP A CA    1 
ATOM   2790 C  C     . ASP C 2 39  ? 15.882  25.885  16.746  1.00 22.29 ? 38  ASP A C     1 
ATOM   2791 O  O     . ASP C 2 39  ? 15.351  26.917  16.292  1.00 20.44 ? 38  ASP A O     1 
ATOM   2792 C  CB    . ASP C 2 39  ? 16.219  24.220  14.944  1.00 19.56 ? 38  ASP A CB    1 
ATOM   2793 C  CG    . ASP C 2 39  ? 16.034  22.795  14.453  1.00 24.01 ? 38  ASP A CG    1 
ATOM   2794 O  OD1   . ASP C 2 39  ? 16.591  21.879  15.063  1.00 24.34 ? 38  ASP A OD1   1 
ATOM   2795 O  OD2   . ASP C 2 39  ? 15.257  22.617  13.515  1.00 25.67 ? 38  ASP A OD2   1 
ATOM   2796 N  N     . SER C 2 40  ? 16.917  25.907  17.582  1.00 19.49 ? 39  SER A N     1 
ATOM   2797 C  CA    . SER C 2 40  ? 17.463  27.139  18.125  1.00 20.39 ? 39  SER A CA    1 
ATOM   2798 C  C     . SER C 2 40  ? 18.938  27.239  17.787  1.00 22.11 ? 39  SER A C     1 
ATOM   2799 O  O     . SER C 2 40  ? 19.660  26.228  17.793  1.00 21.51 ? 39  SER A O     1 
ATOM   2800 C  CB    . SER C 2 40  ? 17.321  27.264  19.659  1.00 27.32 ? 39  SER A CB    1 
ATOM   2801 O  OG    . SER C 2 40  ? 15.971  27.483  20.005  1.00 33.91 ? 39  SER A OG    1 
ATOM   2802 N  N     . TYR C 2 41  ? 19.367  28.486  17.545  1.00 19.72 ? 40  TYR A N     1 
ATOM   2803 C  CA    . TYR C 2 41  ? 20.737  28.803  17.095  1.00 18.18 ? 40  TYR A CA    1 
ATOM   2804 C  C     . TYR C 2 41  ? 21.189  30.059  17.801  1.00 21.64 ? 40  TYR A C     1 
ATOM   2805 O  O     . TYR C 2 41  ? 20.366  30.845  18.277  1.00 20.90 ? 40  TYR A O     1 
ATOM   2806 C  CB    . TYR C 2 41  ? 20.805  29.019  15.588  1.00 16.67 ? 40  TYR A CB    1 
ATOM   2807 C  CG    . TYR C 2 41  ? 20.349  27.853  14.804  1.00 19.34 ? 40  TYR A CG    1 
ATOM   2808 C  CD1   . TYR C 2 41  ? 21.228  26.838  14.475  1.00 19.89 ? 40  TYR A CD1   1 
ATOM   2809 C  CD2   . TYR C 2 41  ? 19.017  27.771  14.397  1.00 19.21 ? 40  TYR A CD2   1 
ATOM   2810 C  CE1   . TYR C 2 41  ? 20.788  25.735  13.731  1.00 23.65 ? 40  TYR A CE1   1 
ATOM   2811 C  CE2   . TYR C 2 41  ? 18.545  26.710  13.617  1.00 20.74 ? 40  TYR A CE2   1 
ATOM   2812 C  CZ    . TYR C 2 41  ? 19.440  25.681  13.322  1.00 21.96 ? 40  TYR A CZ    1 
ATOM   2813 O  OH    . TYR C 2 41  ? 19.014  24.621  12.563  1.00 22.50 ? 40  TYR A OH    1 
ATOM   2814 N  N     . ARG C 2 42  ? 22.524  30.238  17.867  1.00 22.57 ? 41  ARG A N     1 
ATOM   2815 C  CA    . ARG C 2 42  ? 23.192  31.357  18.550  1.00 21.27 ? 41  ARG A CA    1 
ATOM   2816 C  C     . ARG C 2 42  ? 24.289  31.871  17.619  1.00 20.09 ? 41  ARG A C     1 
ATOM   2817 O  O     . ARG C 2 42  ? 25.030  31.068  17.039  1.00 20.55 ? 41  ARG A O     1 
ATOM   2818 C  CB    . ARG C 2 42  ? 23.847  30.920  19.878  1.00 22.89 ? 41  ARG A CB    1 
ATOM   2819 C  CG    . ARG C 2 42  ? 22.871  30.701  21.074  1.00 24.29 ? 41  ARG A CG    1 
ATOM   2820 C  CD    . ARG C 2 42  ? 22.496  32.065  21.598  1.00 30.21 ? 41  ARG A CD    1 
ATOM   2821 N  NE    . ARG C 2 42  ? 21.521  32.064  22.690  1.00 31.27 ? 41  ARG A NE    1 
ATOM   2822 C  CZ    . ARG C 2 42  ? 21.840  32.140  23.978  1.00 36.20 ? 41  ARG A CZ    1 
ATOM   2823 N  NH1   . ARG C 2 42  ? 23.100  32.089  24.390  1.00 32.28 ? 41  ARG A NH1   1 
ATOM   2824 N  NH2   . ARG C 2 42  ? 20.866  32.303  24.877  1.00 36.00 ? 41  ARG A NH2   1 
ATOM   2825 N  N     . LYS C 2 43  ? 24.382  33.188  17.456  1.00 19.91 ? 42  LYS A N     1 
ATOM   2826 C  CA    . LYS C 2 43  ? 25.477  33.753  16.651  1.00 22.25 ? 42  LYS A CA    1 
ATOM   2827 C  C     . LYS C 2 43  ? 25.795  35.151  17.164  1.00 21.26 ? 42  LYS A C     1 
ATOM   2828 O  O     . LYS C 2 43  ? 24.882  35.938  17.411  1.00 23.69 ? 42  LYS A O     1 
ATOM   2829 C  CB    . LYS C 2 43  ? 25.126  33.828  15.150  1.00 21.23 ? 42  LYS A CB    1 
ATOM   2830 C  CG    . LYS C 2 43  ? 26.310  34.348  14.287  1.00 22.78 ? 42  LYS A CG    1 
ATOM   2831 C  CD    . LYS C 2 43  ? 25.854  34.616  12.831  1.00 24.05 ? 42  LYS A CD    1 
ATOM   2832 C  CE    . LYS C 2 43  ? 27.091  34.839  11.982  1.00 26.08 ? 42  LYS A CE    1 
ATOM   2833 N  NZ    . LYS C 2 43  ? 26.649  35.380  10.665  1.00 30.13 ? 42  LYS A NZ    1 
ATOM   2834 N  N     . GLN C 2 44  ? 27.071  35.472  17.384  1.00 23.98 ? 43  GLN A N     1 
ATOM   2835 C  CA    . GLN C 2 44  ? 27.387  36.857  17.689  1.00 23.30 ? 43  GLN A CA    1 
ATOM   2836 C  C     . GLN C 2 44  ? 27.750  37.589  16.403  1.00 25.92 ? 43  GLN A C     1 
ATOM   2837 O  O     . GLN C 2 44  ? 28.387  37.024  15.498  1.00 24.97 ? 43  GLN A O     1 
ATOM   2838 C  CB    . GLN C 2 44  ? 28.535  36.950  18.666  1.00 24.75 ? 43  GLN A CB    1 
ATOM   2839 C  CG    . GLN C 2 44  ? 29.820  36.433  18.133  1.00 29.11 ? 43  GLN A CG    1 
ATOM   2840 C  CD    . GLN C 2 44  ? 30.980  36.795  19.047  1.00 27.20 ? 43  GLN A CD    1 
ATOM   2841 O  OE1   . GLN C 2 44  ? 31.167  37.950  19.475  1.00 28.95 ? 43  GLN A OE1   1 
ATOM   2842 N  NE2   . GLN C 2 44  ? 31.732  35.773  19.438  1.00 32.07 ? 43  GLN A NE2   1 
ATOM   2843 N  N     . VAL C 2 45  ? 27.341  38.849  16.332  1.00 25.39 ? 44  VAL A N     1 
ATOM   2844 C  CA    . VAL C 2 45  ? 27.485  39.650  15.123  1.00 28.28 ? 44  VAL A CA    1 
ATOM   2845 C  C     . VAL C 2 45  ? 27.755  41.086  15.555  1.00 32.09 ? 44  VAL A C     1 
ATOM   2846 O  O     . VAL C 2 45  ? 27.443  41.486  16.670  1.00 32.46 ? 44  VAL A O     1 
ATOM   2847 C  CB    . VAL C 2 45  ? 26.221  39.603  14.231  1.00 28.23 ? 44  VAL A CB    1 
ATOM   2848 C  CG1   . VAL C 2 45  ? 25.875  38.151  13.758  1.00 27.28 ? 44  VAL A CG1   1 
ATOM   2849 C  CG2   . VAL C 2 45  ? 25.040  40.166  14.989  1.00 28.07 ? 44  VAL A CG2   1 
ATOM   2850 N  N     . VAL C 2 46  ? 28.337  41.873  14.658  1.00 32.49 ? 45  VAL A N     1 
ATOM   2851 C  CA    . VAL C 2 46  ? 28.490  43.310  14.874  1.00 34.54 ? 45  VAL A CA    1 
ATOM   2852 C  C     . VAL C 2 46  ? 27.401  44.027  14.094  1.00 38.91 ? 45  VAL A C     1 
ATOM   2853 O  O     . VAL C 2 46  ? 27.337  43.905  12.867  1.00 37.93 ? 45  VAL A O     1 
ATOM   2854 C  CB    . VAL C 2 46  ? 29.879  43.802  14.429  1.00 38.01 ? 45  VAL A CB    1 
ATOM   2855 C  CG1   . VAL C 2 46  ? 29.986  45.319  14.651  1.00 40.44 ? 45  VAL A CG1   1 
ATOM   2856 C  CG2   . VAL C 2 46  ? 30.970  43.071  15.194  1.00 35.38 ? 45  VAL A CG2   1 
ATOM   2857 N  N     . ILE C 2 47  ? 26.550  44.782  14.782  1.00 38.47 ? 46  ILE A N     1 
ATOM   2858 C  CA    . ILE C 2 47  ? 25.500  45.556  14.130  1.00 39.92 ? 46  ILE A CA    1 
ATOM   2859 C  C     . ILE C 2 47  ? 25.680  47.025  14.527  1.00 45.30 ? 46  ILE A C     1 
ATOM   2860 O  O     . ILE C 2 47  ? 25.506  47.394  15.698  1.00 45.56 ? 46  ILE A O     1 
ATOM   2861 C  CB    . ILE C 2 47  ? 24.096  45.034  14.472  1.00 37.45 ? 46  ILE A CB    1 
ATOM   2862 C  CG1   . ILE C 2 47  ? 23.908  43.592  13.945  1.00 30.26 ? 46  ILE A CG1   1 
ATOM   2863 C  CG2   . ILE C 2 47  ? 23.010  45.952  13.916  1.00 38.02 ? 46  ILE A CG2   1 
ATOM   2864 C  CD1   . ILE C 2 47  ? 22.593  42.925  14.412  1.00 30.34 ? 46  ILE A CD1   1 
ATOM   2865 N  N     . ASP C 2 48  ? 26.041  47.866  13.560  1.00 40.82 ? 47  ASP A N     1 
ATOM   2866 C  CA    . ASP C 2 48  ? 26.318  49.269  13.855  1.00 42.67 ? 47  ASP A CA    1 
ATOM   2867 C  C     . ASP C 2 48  ? 27.483  49.411  14.836  1.00 45.94 ? 47  ASP A C     1 
ATOM   2868 O  O     . ASP C 2 48  ? 27.445  50.216  15.774  1.00 45.78 ? 47  ASP A O     1 
ATOM   2869 C  CB    . ASP C 2 48  ? 25.061  49.975  14.385  1.00 45.05 ? 47  ASP A CB    1 
ATOM   2870 C  CG    . ASP C 2 48  ? 23.929  49.986  13.364  1.00 45.19 ? 47  ASP A CG    1 
ATOM   2871 O  OD1   . ASP C 2 48  ? 24.231  49.929  12.152  1.00 43.93 ? 47  ASP A OD1   1 
ATOM   2872 O  OD2   . ASP C 2 48  ? 22.744  50.029  13.779  1.00 46.25 ? 47  ASP A OD2   1 
ATOM   2873 N  N     . GLY C 2 49  ? 28.553  48.653  14.595  1.00 43.64 ? 48  GLY A N     1 
ATOM   2874 C  CA    . GLY C 2 49  ? 29.684  48.750  15.501  1.00 46.93 ? 48  GLY A CA    1 
ATOM   2875 C  C     . GLY C 2 49  ? 29.428  48.263  16.916  1.00 46.46 ? 48  GLY A C     1 
ATOM   2876 O  O     . GLY C 2 49  ? 30.261  48.506  17.796  1.00 52.74 ? 48  GLY A O     1 
ATOM   2877 N  N     . GLU C 2 50  ? 28.309  47.579  17.161  1.00 47.01 ? 49  GLU A N     1 
ATOM   2878 C  CA    . GLU C 2 50  ? 27.939  47.048  18.474  1.00 46.31 ? 49  GLU A CA    1 
ATOM   2879 C  C     . GLU C 2 50  ? 27.861  45.532  18.363  1.00 43.81 ? 49  GLU A C     1 
ATOM   2880 O  O     . GLU C 2 50  ? 27.038  45.015  17.593  1.00 45.48 ? 49  GLU A O     1 
ATOM   2881 C  CB    . GLU C 2 50  ? 26.593  47.622  18.930  1.00 48.96 ? 49  GLU A CB    1 
ATOM   2882 C  CG    . GLU C 2 50  ? 26.399  47.717  20.440  1.00 56.66 ? 49  GLU A CG    1 
ATOM   2883 C  CD    . GLU C 2 50  ? 25.833  49.082  20.894  1.00 70.90 ? 49  GLU A CD    1 
ATOM   2884 O  OE1   . GLU C 2 50  ? 25.348  49.848  20.022  1.00 69.66 ? 49  GLU A OE1   1 
ATOM   2885 O  OE2   . GLU C 2 50  ? 25.909  49.405  22.111  1.00 71.54 ? 49  GLU A OE2   1 
ATOM   2886 N  N     . THR C 2 51  ? 28.723  44.815  19.103  1.00 39.27 ? 50  THR A N     1 
ATOM   2887 C  CA    . THR C 2 51  ? 28.623  43.359  19.081  1.00 37.88 ? 50  THR A CA    1 
ATOM   2888 C  C     . THR C 2 51  ? 27.389  42.926  19.879  1.00 37.83 ? 50  THR A C     1 
ATOM   2889 O  O     . THR C 2 51  ? 27.192  43.360  21.020  1.00 36.87 ? 50  THR A O     1 
ATOM   2890 C  CB    . THR C 2 51  ? 29.884  42.697  19.653  1.00 39.42 ? 50  THR A CB    1 
ATOM   2891 O  OG1   . THR C 2 51  ? 31.036  43.185  18.973  1.00 42.49 ? 50  THR A OG1   1 
ATOM   2892 C  CG2   . THR C 2 51  ? 29.845  41.157  19.438  1.00 36.75 ? 50  THR A CG2   1 
ATOM   2893 N  N     . CYS C 2 52  ? 26.577  42.040  19.306  1.00 31.84 ? 51  CYS A N     1 
ATOM   2894 C  CA    . CYS C 2 52  ? 25.485  41.463  20.079  1.00 33.71 ? 51  CYS A CA    1 
ATOM   2895 C  C     . CYS C 2 52  ? 25.347  39.980  19.767  1.00 31.88 ? 51  CYS A C     1 
ATOM   2896 O  O     . CYS C 2 52  ? 25.967  39.457  18.840  1.00 28.63 ? 51  CYS A O     1 
ATOM   2897 C  CB    . CYS C 2 52  ? 24.178  42.182  19.811  1.00 38.00 ? 51  CYS A CB    1 
ATOM   2898 S  SG    . CYS C 2 52  ? 23.797  42.097  18.115  1.00 36.26 ? 51  CYS A SG    1 
ATOM   2899 N  N     . LEU C 2 53  ? 24.501  39.320  20.561  1.00 29.49 ? 52  LEU A N     1 
ATOM   2900 C  CA    . LEU C 2 53  ? 24.253  37.889  20.504  1.00 30.24 ? 52  LEU A CA    1 
ATOM   2901 C  C     . LEU C 2 53  ? 22.858  37.678  19.946  1.00 28.27 ? 52  LEU A C     1 
ATOM   2902 O  O     . LEU C 2 53  ? 21.891  38.220  20.484  1.00 29.00 ? 52  LEU A O     1 
ATOM   2903 C  CB    . LEU C 2 53  ? 24.397  37.261  21.894  1.00 27.90 ? 52  LEU A CB    1 
ATOM   2904 C  CG    . LEU C 2 53  ? 24.471  35.719  21.959  1.00 28.61 ? 52  LEU A CG    1 
ATOM   2905 C  CD1   . LEU C 2 53  ? 25.296  35.020  20.899  1.00 27.54 ? 52  LEU A CD1   1 
ATOM   2906 C  CD2   . LEU C 2 53  ? 24.865  35.257  23.392  1.00 33.65 ? 52  LEU A CD2   1 
ATOM   2907 N  N     . LEU C 2 54  ? 22.768  36.988  18.817  1.00 23.51 ? 53  LEU A N     1 
ATOM   2908 C  CA    . LEU C 2 54  ? 21.477  36.644  18.234  1.00 24.98 ? 53  LEU A CA    1 
ATOM   2909 C  C     . LEU C 2 54  ? 21.078  35.250  18.687  1.00 27.18 ? 53  LEU A C     1 
ATOM   2910 O  O     . LEU C 2 54  ? 21.843  34.299  18.531  1.00 23.82 ? 53  LEU A O     1 
ATOM   2911 C  CB    . LEU C 2 54  ? 21.515  36.693  16.713  1.00 22.79 ? 53  LEU A CB    1 
ATOM   2912 C  CG    . LEU C 2 54  ? 22.077  37.960  16.056  1.00 25.26 ? 53  LEU A CG    1 
ATOM   2913 C  CD1   . LEU C 2 54  ? 21.880  37.821  14.528  1.00 26.48 ? 53  LEU A CD1   1 
ATOM   2914 C  CD2   . LEU C 2 54  ? 21.415  39.203  16.550  1.00 27.28 ? 53  LEU A CD2   1 
ATOM   2915 N  N     . ASP C 2 55  ? 19.879  35.140  19.257  1.00 23.31 ? 54  ASP A N     1 
ATOM   2916 C  CA    . ASP C 2 55  ? 19.265  33.874  19.609  1.00 22.14 ? 54  ASP A CA    1 
ATOM   2917 C  C     . ASP C 2 55  ? 18.106  33.699  18.632  1.00 23.03 ? 54  ASP A C     1 
ATOM   2918 O  O     . ASP C 2 55  ? 17.195  34.542  18.586  1.00 25.15 ? 54  ASP A O     1 
ATOM   2919 C  CB    . ASP C 2 55  ? 18.809  33.879  21.074  1.00 24.07 ? 54  ASP A CB    1 
ATOM   2920 C  CG    . ASP C 2 55  ? 18.274  32.540  21.489  1.00 31.56 ? 54  ASP A CG    1 
ATOM   2921 O  OD1   . ASP C 2 55  ? 17.198  32.204  20.967  1.00 32.46 ? 54  ASP A OD1   1 
ATOM   2922 O  OD2   . ASP C 2 55  ? 18.897  31.821  22.317  1.00 35.75 ? 54  ASP A OD2   1 
ATOM   2923 N  N     . ILE C 2 56  ? 18.196  32.682  17.772  1.00 23.72 ? 55  ILE A N     1 
ATOM   2924 C  CA    . ILE C 2 56  ? 17.260  32.505  16.643  1.00 19.65 ? 55  ILE A CA    1 
ATOM   2925 C  C     . ILE C 2 56  ? 16.450  31.246  16.874  1.00 21.85 ? 55  ILE A C     1 
ATOM   2926 O  O     . ILE C 2 56  ? 17.019  30.171  17.069  1.00 21.28 ? 55  ILE A O     1 
ATOM   2927 C  CB    . ILE C 2 56  ? 18.007  32.365  15.312  1.00 20.33 ? 55  ILE A CB    1 
ATOM   2928 C  CG1   . ILE C 2 56  ? 19.124  33.409  15.202  1.00 26.59 ? 55  ILE A CG1   1 
ATOM   2929 C  CG2   . ILE C 2 56  ? 16.976  32.423  14.141  1.00 21.01 ? 55  ILE A CG2   1 
ATOM   2930 C  CD1   . ILE C 2 56  ? 18.596  34.727  14.998  1.00 25.58 ? 55  ILE A CD1   1 
ATOM   2931 N  N     . LEU C 2 57  ? 15.125  31.360  16.820  1.00 20.49 ? 56  LEU A N     1 
ATOM   2932 C  CA    . LEU C 2 57  ? 14.268  30.193  16.922  1.00 17.50 ? 56  LEU A CA    1 
ATOM   2933 C  C     . LEU C 2 57  ? 13.666  30.004  15.535  1.00 20.92 ? 56  LEU A C     1 
ATOM   2934 O  O     . LEU C 2 57  ? 13.019  30.912  15.010  1.00 19.44 ? 56  LEU A O     1 
ATOM   2935 C  CB    . LEU C 2 57  ? 13.185  30.411  17.987  1.00 20.26 ? 56  LEU A CB    1 
ATOM   2936 C  CG    . LEU C 2 57  ? 12.319  29.166  18.198  1.00 20.56 ? 56  LEU A CG    1 
ATOM   2937 C  CD1   . LEU C 2 57  ? 13.046  28.020  18.930  1.00 25.98 ? 56  LEU A CD1   1 
ATOM   2938 C  CD2   . LEU C 2 57  ? 11.053  29.561  18.934  1.00 24.22 ? 56  LEU A CD2   1 
ATOM   2939 N  N     . ASP C 2 58  ? 13.910  28.828  14.954  1.00 17.91 ? 57  ASP A N     1 
ATOM   2940 C  CA    . ASP C 2 58  ? 13.399  28.453  13.654  1.00 19.42 ? 57  ASP A CA    1 
ATOM   2941 C  C     . ASP C 2 58  ? 12.216  27.529  13.885  1.00 19.17 ? 57  ASP A C     1 
ATOM   2942 O  O     . ASP C 2 58  ? 12.352  26.529  14.599  1.00 18.21 ? 57  ASP A O     1 
ATOM   2943 C  CB    . ASP C 2 58  ? 14.548  27.786  12.883  1.00 16.85 ? 57  ASP A CB    1 
ATOM   2944 C  CG    . ASP C 2 58  ? 14.167  27.356  11.483  1.00 17.39 ? 57  ASP A CG    1 
ATOM   2945 O  OD1   . ASP C 2 58  ? 13.236  27.925  10.874  1.00 19.72 ? 57  ASP A OD1   1 
ATOM   2946 O  OD2   . ASP C 2 58  ? 14.869  26.447  10.942  1.00 19.68 ? 57  ASP A OD2   1 
ATOM   2947 N  N     . THR C 2 59  ? 11.027  27.883  13.339  1.00 20.03 ? 58  THR A N     1 
ATOM   2948 C  CA    . THR C 2 59  ? 9.757   27.292  13.793  1.00 18.71 ? 58  THR A CA    1 
ATOM   2949 C  C     . THR C 2 59  ? 9.113   26.459  12.694  1.00 20.61 ? 58  THR A C     1 
ATOM   2950 O  O     . THR C 2 59  ? 9.458   26.563  11.509  1.00 19.44 ? 58  THR A O     1 
ATOM   2951 C  CB    . THR C 2 59  ? 8.747   28.378  14.236  1.00 23.05 ? 58  THR A CB    1 
ATOM   2952 O  OG1   . THR C 2 59  ? 8.440   29.187  13.094  1.00 21.84 ? 58  THR A OG1   1 
ATOM   2953 C  CG2   . THR C 2 59  ? 9.367   29.269  15.315  1.00 19.90 ? 58  THR A CG2   1 
ATOM   2954 N  N     . ALA C 2 60  ? 8.125   25.680  13.115  1.00 19.98 ? 59  ALA A N     1 
ATOM   2955 C  CA    . ALA C 2 60  ? 7.312   24.888  12.212  1.00 22.40 ? 59  ALA A CA    1 
ATOM   2956 C  C     . ALA C 2 60  ? 6.108   25.713  11.760  1.00 26.86 ? 59  ALA A C     1 
ATOM   2957 O  O     . ALA C 2 60  ? 5.424   26.316  12.592  1.00 24.76 ? 59  ALA A O     1 
ATOM   2958 C  CB    . ALA C 2 60  ? 6.833   23.648  12.943  1.00 23.46 ? 59  ALA A CB    1 
ATOM   2959 N  N     . GLY C 2 61  ? 5.843   25.717  10.454  1.00 25.85 ? 60  GLY A N     1 
ATOM   2960 C  CA    . GLY C 2 61  ? 4.603   26.342  10.012  1.00 28.13 ? 60  GLY A CA    1 
ATOM   2961 C  C     . GLY C 2 61  ? 3.417   25.430  9.886   1.00 29.80 ? 60  GLY A C     1 
ATOM   2962 O  O     . GLY C 2 61  ? 2.322   25.931  9.581   1.00 35.56 ? 60  GLY A O     1 
ATOM   2963 N  N     . GLN C 2 62  ? 3.563   24.134  10.174  1.00 26.71 ? 61  GLN A N     1 
ATOM   2964 C  CA    . GLN C 2 62  ? 2.506   23.132  10.005  1.00 32.11 ? 61  GLN A CA    1 
ATOM   2965 C  C     . GLN C 2 62  ? 1.171   23.653  10.514  1.00 35.10 ? 61  GLN A C     1 
ATOM   2966 O  O     . GLN C 2 62  ? 1.056   24.075  11.665  1.00 32.64 ? 61  GLN A O     1 
ATOM   2967 C  CB    . GLN C 2 62  ? 2.850   21.869  10.803  1.00 29.45 ? 61  GLN A CB    1 
ATOM   2968 C  CG    . GLN C 2 62  ? 4.169   21.289  10.448  1.00 34.54 ? 61  GLN A CG    1 
ATOM   2969 C  CD    . GLN C 2 62  ? 4.079   20.190  9.456   1.00 32.22 ? 61  GLN A CD    1 
ATOM   2970 O  OE1   . GLN C 2 62  ? 2.955   19.770  9.109   1.00 35.90 ? 61  GLN A OE1   1 
ATOM   2971 N  NE2   . GLN C 2 62  ? 5.222   19.732  8.946   1.00 36.25 ? 61  GLN A NE2   1 
ATOM   2972 N  N     . GLU C 2 63  ? 0.145   23.572  9.683   1.00 33.58 ? 62  GLU A N     1 
ATOM   2973 C  CA    . GLU C 2 63  ? -1.098  24.201  10.105  1.00 37.79 ? 62  GLU A CA    1 
ATOM   2974 C  C     . GLU C 2 63  ? -1.788  23.413  11.217  1.00 34.47 ? 62  GLU A C     1 
ATOM   2975 O  O     . GLU C 2 63  ? -2.537  24.000  12.007  1.00 33.74 ? 62  GLU A O     1 
ATOM   2976 C  CB    . GLU C 2 63  ? -2.001  24.391  8.898   1.00 39.15 ? 62  GLU A CB    1 
ATOM   2977 C  CG    . GLU C 2 63  ? -1.576  25.669  8.140   1.00 44.22 ? 62  GLU A CG    1 
ATOM   2978 C  CD    . GLU C 2 63  ? -2.654  26.272  7.215   1.00 56.84 ? 62  GLU A CD    1 
ATOM   2979 O  OE1   . GLU C 2 63  ? -3.353  25.527  6.471   1.00 60.30 ? 62  GLU A OE1   1 
ATOM   2980 O  OE2   . GLU C 2 63  ? -2.748  27.533  7.204   1.00 57.40 ? 62  GLU A OE2   1 
ATOM   2981 N  N     . GLU C 2 64  ? -1.521  22.106  11.328  1.00 32.07 ? 63  GLU A N     1 
ATOM   2982 C  CA    . GLU C 2 64  ? -2.153  21.295  12.358  1.00 35.59 ? 63  GLU A CA    1 
ATOM   2983 C  C     . GLU C 2 64  ? -1.815  21.813  13.754  1.00 34.10 ? 63  GLU A C     1 
ATOM   2984 O  O     . GLU C 2 64  ? -2.615  21.603  14.688  1.00 33.46 ? 63  GLU A O     1 
ATOM   2985 C  CB    . GLU C 2 64  ? -1.730  19.808  12.185  1.00 32.19 ? 63  GLU A CB    1 
ATOM   2986 C  CG    . GLU C 2 64  ? -2.241  18.804  13.236  1.00 40.56 ? 63  GLU A CG    1 
ATOM   2987 C  CD    . GLU C 2 64  ? -3.749  18.497  13.160  1.00 42.42 ? 63  GLU A CD    1 
ATOM   2988 O  OE1   . GLU C 2 64  ? -4.419  18.341  14.225  1.00 46.74 ? 63  GLU A OE1   1 
ATOM   2989 O  OE2   . GLU C 2 64  ? -4.300  18.325  12.040  1.00 49.76 ? 63  GLU A OE2   1 
ATOM   2990 N  N     . TYR C 2 65  ? -0.683  22.524  13.893  1.00 33.97 ? 64  TYR A N     1 
ATOM   2991 C  CA    . TYR C 2 65  ? -0.140  22.961  15.182  1.00 36.52 ? 64  TYR A CA    1 
ATOM   2992 C  C     . TYR C 2 65  ? -0.215  24.480  15.364  1.00 35.06 ? 64  TYR A C     1 
ATOM   2993 O  O     . TYR C 2 65  ? 0.555   25.045  16.138  1.00 32.59 ? 64  TYR A O     1 
ATOM   2994 C  CB    . TYR C 2 65  ? 1.310   22.464  15.338  1.00 31.69 ? 64  TYR A CB    1 
ATOM   2995 C  CG    . TYR C 2 65  ? 1.440   20.966  15.004  1.00 29.58 ? 64  TYR A CG    1 
ATOM   2996 C  CD1   . TYR C 2 65  ? 0.689   20.036  15.677  1.00 31.07 ? 64  TYR A CD1   1 
ATOM   2997 C  CD2   . TYR C 2 65  ? 2.304   20.512  13.953  1.00 26.58 ? 64  TYR A CD2   1 
ATOM   2998 C  CE1   . TYR C 2 65  ? 0.734   18.665  15.366  1.00 32.52 ? 64  TYR A CE1   1 
ATOM   2999 C  CE2   . TYR C 2 65  ? 2.341   19.129  13.608  1.00 26.70 ? 64  TYR A CE2   1 
ATOM   3000 C  CZ    . TYR C 2 65  ? 1.604   18.224  14.328  1.00 28.53 ? 64  TYR A CZ    1 
ATOM   3001 O  OH    . TYR C 2 65  ? 1.589   16.850  14.048  1.00 29.71 ? 64  TYR A OH    1 
ATOM   3002 N  N     . SER C 2 66  ? -1.129  25.153  14.642  1.00 33.54 ? 65  SER A N     1 
ATOM   3003 C  CA    . SER C 2 66  ? -1.183  26.617  14.664  1.00 36.02 ? 65  SER A CA    1 
ATOM   3004 C  C     . SER C 2 66  ? -1.518  27.159  16.045  1.00 38.42 ? 65  SER A C     1 
ATOM   3005 O  O     . SER C 2 66  ? -1.052  28.243  16.407  1.00 40.64 ? 65  SER A O     1 
ATOM   3006 C  CB    . SER C 2 66  ? -2.217  27.126  13.636  1.00 38.73 ? 65  SER A CB    1 
ATOM   3007 O  OG    . SER C 2 66  ? -3.473  26.511  13.829  1.00 39.20 ? 65  SER A OG    1 
ATOM   3008 N  N     . ALA C 2 67  ? -2.303  26.427  16.843  1.00 38.32 ? 66  ALA A N     1 
ATOM   3009 C  CA    . ALA C 2 67  ? -2.680  26.913  18.171  1.00 40.98 ? 66  ALA A CA    1 
ATOM   3010 C  C     . ALA C 2 67  ? -1.627  26.650  19.234  1.00 41.12 ? 66  ALA A C     1 
ATOM   3011 O  O     . ALA C 2 67  ? -1.830  27.044  20.386  1.00 44.40 ? 66  ALA A O     1 
ATOM   3012 C  CB    . ALA C 2 67  ? -4.013  26.303  18.617  1.00 36.18 ? 66  ALA A CB    1 
ATOM   3013 N  N     . MET C 2 68  ? -0.524  25.999  18.877  1.00 39.77 ? 67  MET A N     1 
ATOM   3014 C  CA    . MET C 2 68  ? 0.608   25.787  19.755  1.00 37.76 ? 67  MET A CA    1 
ATOM   3015 C  C     . MET C 2 68  ? 1.725   26.766  19.495  1.00 39.77 ? 67  MET A C     1 
ATOM   3016 O  O     . MET C 2 68  ? 2.824   26.588  20.016  1.00 39.57 ? 67  MET A O     1 
ATOM   3017 C  CB    . MET C 2 68  ? 1.117   24.369  19.605  1.00 38.43 ? 67  MET A CB    1 
ATOM   3018 C  CG    . MET C 2 68  ? -0.031  23.408  19.479  1.00 44.36 ? 67  MET A CG    1 
ATOM   3019 S  SD    . MET C 2 68  ? 0.638   21.761  19.600  1.00 45.56 ? 67  MET A SD    1 
ATOM   3020 C  CE    . MET C 2 68  ? 1.218   21.773  21.297  1.00 45.21 ? 67  MET A CE    1 
ATOM   3021 N  N     . ARG C 2 69  ? 1.476   27.773  18.662  1.00 40.17 ? 68  ARG A N     1 
ATOM   3022 C  CA    . ARG C 2 69  ? 2.496   28.758  18.375  1.00 38.90 ? 68  ARG A CA    1 
ATOM   3023 C  C     . ARG C 2 69  ? 2.682   29.729  19.515  1.00 39.94 ? 68  ARG A C     1 
ATOM   3024 O  O     . ARG C 2 69  ? 3.668   30.481  19.512  1.00 38.71 ? 68  ARG A O     1 
ATOM   3025 C  CB    . ARG C 2 69  ? 2.147   29.514  17.102  1.00 37.96 ? 68  ARG A CB    1 
ATOM   3026 C  CG    . ARG C 2 69  ? 2.220   28.675  15.831  1.00 39.50 ? 68  ARG A CG    1 
ATOM   3027 C  CD    . ARG C 2 69  ? 1.558   29.419  14.685  1.00 38.92 ? 68  ARG A CD    1 
ATOM   3028 N  NE    . ARG C 2 69  ? 1.449   28.600  13.482  1.00 36.51 ? 68  ARG A NE    1 
ATOM   3029 C  CZ    . ARG C 2 69  ? 0.582   28.844  12.517  1.00 38.36 ? 68  ARG A CZ    1 
ATOM   3030 N  NH1   . ARG C 2 69  ? -0.215  29.889  12.570  1.00 38.13 ? 68  ARG A NH1   1 
ATOM   3031 N  NH2   . ARG C 2 69  ? 0.494   28.006  11.489  1.00 39.15 ? 68  ARG A NH2   1 
ATOM   3032 N  N     . ASP C 2 70  ? 1.789   29.677  20.497  1.00 40.73 ? 69  ASP A N     1 
ATOM   3033 C  CA    . ASP C 2 70  ? 1.605   30.780  21.417  1.00 45.37 ? 69  ASP A CA    1 
ATOM   3034 C  C     . ASP C 2 70  ? 2.820   30.956  22.325  1.00 47.50 ? 69  ASP A C     1 
ATOM   3035 O  O     . ASP C 2 70  ? 3.289   32.083  22.536  1.00 48.16 ? 69  ASP A O     1 
ATOM   3036 C  CB    . ASP C 2 70  ? 0.305   30.581  22.220  1.00 44.26 ? 69  ASP A CB    1 
ATOM   3037 C  CG    . ASP C 2 70  ? -0.981  30.519  21.309  1.00 46.73 ? 69  ASP A CG    1 
ATOM   3038 O  OD1   . ASP C 2 70  ? -0.918  30.650  20.064  1.00 45.78 ? 69  ASP A OD1   1 
ATOM   3039 O  OD2   . ASP C 2 70  ? -2.095  30.408  21.838  1.00 48.72 ? 69  ASP A OD2   1 
ATOM   3040 N  N     . GLN C 2 71  ? 3.358   29.868  22.867  1.00 44.63 ? 70  GLN A N     1 
ATOM   3041 C  CA    . GLN C 2 71  ? 4.452   30.038  23.824  1.00 48.51 ? 70  GLN A CA    1 
ATOM   3042 C  C     . GLN C 2 71  ? 5.684   30.661  23.180  1.00 45.42 ? 70  GLN A C     1 
ATOM   3043 O  O     . GLN C 2 71  ? 6.343   31.517  23.791  1.00 45.27 ? 70  GLN A O     1 
ATOM   3044 C  CB    . GLN C 2 71  ? 4.861   28.724  24.480  1.00 52.65 ? 70  GLN A CB    1 
ATOM   3045 C  CG    . GLN C 2 71  ? 6.093   28.825  25.456  1.00 54.66 ? 70  GLN A CG    1 
ATOM   3046 C  CD    . GLN C 2 71  ? 6.182   30.086  26.369  1.00 60.63 ? 70  GLN A CD    1 
ATOM   3047 O  OE1   . GLN C 2 71  ? 5.455   31.074  26.222  1.00 57.33 ? 70  GLN A OE1   1 
ATOM   3048 N  NE2   . GLN C 2 71  ? 7.108   30.034  27.326  1.00 67.16 ? 70  GLN A NE2   1 
ATOM   3049 N  N     . TYR C 2 72  ? 6.041   30.239  21.969  1.00 43.46 ? 71  TYR A N     1 
ATOM   3050 C  CA    . TYR C 2 72  ? 7.239   30.847  21.405  1.00 39.57 ? 71  TYR A CA    1 
ATOM   3051 C  C     . TYR C 2 72  ? 6.985   32.300  21.002  1.00 39.19 ? 71  TYR A C     1 
ATOM   3052 O  O     . TYR C 2 72  ? 7.881   33.148  21.129  1.00 35.17 ? 71  TYR A O     1 
ATOM   3053 C  CB    . TYR C 2 72  ? 7.788   29.977  20.285  1.00 35.20 ? 71  TYR A CB    1 
ATOM   3054 C  CG    . TYR C 2 72  ? 7.106   30.005  18.934  1.00 33.43 ? 71  TYR A CG    1 
ATOM   3055 C  CD1   . TYR C 2 72  ? 7.045   31.168  18.178  1.00 34.08 ? 71  TYR A CD1   1 
ATOM   3056 C  CD2   . TYR C 2 72  ? 6.534   28.841  18.404  1.00 33.56 ? 71  TYR A CD2   1 
ATOM   3057 C  CE1   . TYR C 2 72  ? 6.445   31.177  16.914  1.00 32.82 ? 71  TYR A CE1   1 
ATOM   3058 C  CE2   . TYR C 2 72  ? 5.953   28.831  17.158  1.00 35.53 ? 71  TYR A CE2   1 
ATOM   3059 C  CZ    . TYR C 2 72  ? 5.900   29.998  16.416  1.00 33.88 ? 71  TYR A CZ    1 
ATOM   3060 O  OH    . TYR C 2 72  ? 5.275   30.002  15.194  1.00 36.29 ? 71  TYR A OH    1 
ATOM   3061 N  N     . MET C 2 73  ? 5.750   32.636  20.624  1.00 40.11 ? 72  MET A N     1 
ATOM   3062 C  CA    . MET C 2 73  ? 5.478   34.026  20.314  1.00 36.91 ? 72  MET A CA    1 
ATOM   3063 C  C     . MET C 2 73  ? 5.501   34.897  21.556  1.00 40.08 ? 72  MET A C     1 
ATOM   3064 O  O     . MET C 2 73  ? 5.868   36.081  21.480  1.00 35.37 ? 72  MET A O     1 
ATOM   3065 C  CB    . MET C 2 73  ? 4.176   34.163  19.512  1.00 33.82 ? 72  MET A CB    1 
ATOM   3066 C  CG    . MET C 2 73  ? 4.178   33.461  18.121  1.00 30.81 ? 72  MET A CG    1 
ATOM   3067 S  SD    . MET C 2 73  ? 2.458   33.574  17.521  1.00 34.74 ? 72  MET A SD    1 
ATOM   3068 C  CE    . MET C 2 73  ? 2.647   32.864  15.880  1.00 36.37 ? 72  MET A CE    1 
ATOM   3069 N  N     . ARG C 2 74  ? 5.146   34.332  22.714  1.00 39.34 ? 73  ARG A N     1 
ATOM   3070 C  CA    . ARG C 2 74  ? 5.200   35.094  23.948  1.00 42.58 ? 73  ARG A CA    1 
ATOM   3071 C  C     . ARG C 2 74  ? 6.636   35.443  24.313  1.00 38.68 ? 73  ARG A C     1 
ATOM   3072 O  O     . ARG C 2 74  ? 6.915   36.560  24.763  1.00 36.62 ? 73  ARG A O     1 
ATOM   3073 C  CB    . ARG C 2 74  ? 4.524   34.299  25.066  1.00 44.29 ? 73  ARG A CB    1 
ATOM   3074 C  CG    . ARG C 2 74  ? 3.033   34.614  25.200  1.00 49.70 ? 73  ARG A CG    1 
ATOM   3075 C  CD    . ARG C 2 74  ? 2.494   34.004  26.487  1.00 57.52 ? 73  ARG A CD    1 
ATOM   3076 N  NE    . ARG C 2 74  ? 2.576   32.553  26.374  1.00 57.54 ? 73  ARG A NE    1 
ATOM   3077 C  CZ    . ARG C 2 74  ? 1.591   31.778  25.948  1.00 59.26 ? 73  ARG A CZ    1 
ATOM   3078 N  NH1   . ARG C 2 74  ? 0.413   32.286  25.601  1.00 59.47 ? 73  ARG A NH1   1 
ATOM   3079 N  NH2   . ARG C 2 74  ? 1.794   30.463  25.866  1.00 62.28 ? 73  ARG A NH2   1 
ATOM   3080 N  N     . THR C 2 75  ? 7.558   34.509  24.113  1.00 37.24 ? 74  THR A N     1 
ATOM   3081 C  CA    . THR C 2 75  ? 8.939   34.737  24.524  1.00 37.96 ? 74  THR A CA    1 
ATOM   3082 C  C     . THR C 2 75  ? 9.751   35.494  23.474  1.00 36.41 ? 74  THR A C     1 
ATOM   3083 O  O     . THR C 2 75  ? 10.710  36.180  23.832  1.00 34.58 ? 74  THR A O     1 
ATOM   3084 C  CB    . THR C 2 75  ? 9.618   33.402  24.831  1.00 39.59 ? 74  THR A CB    1 
ATOM   3085 O  OG1   . THR C 2 75  ? 9.410   32.503  23.737  1.00 46.17 ? 74  THR A OG1   1 
ATOM   3086 C  CG2   . THR C 2 75  ? 9.033   32.788  26.095  1.00 45.43 ? 74  THR A CG2   1 
ATOM   3087 N  N     . GLY C 2 76  ? 9.422   35.363  22.187  1.00 33.97 ? 75  GLY A N     1 
ATOM   3088 C  CA    . GLY C 2 76  ? 10.202  36.040  21.161  1.00 30.79 ? 75  GLY A CA    1 
ATOM   3089 C  C     . GLY C 2 76  ? 10.147  37.561  21.258  1.00 31.24 ? 75  GLY A C     1 
ATOM   3090 O  O     . GLY C 2 76  ? 9.110   38.164  21.580  1.00 34.25 ? 75  GLY A O     1 
ATOM   3091 N  N     . GLU C 2 77  ? 11.291  38.210  20.922  1.00 26.56 ? 76  GLU A N     1 
ATOM   3092 C  CA    . GLU C 2 77  ? 11.366  39.677  20.969  1.00 28.62 ? 76  GLU A CA    1 
ATOM   3093 C  C     . GLU C 2 77  ? 11.082  40.328  19.625  1.00 27.62 ? 76  GLU A C     1 
ATOM   3094 O  O     . GLU C 2 77  ? 10.485  41.417  19.586  1.00 30.28 ? 76  GLU A O     1 
ATOM   3095 C  CB    . GLU C 2 77  ? 12.734  40.174  21.453  1.00 30.45 ? 76  GLU A CB    1 
ATOM   3096 C  CG    . GLU C 2 77  ? 12.997  40.022  22.929  1.00 32.55 ? 76  GLU A CG    1 
ATOM   3097 C  CD    . GLU C 2 77  ? 14.472  40.154  23.323  1.00 36.69 ? 76  GLU A CD    1 
ATOM   3098 O  OE1   . GLU C 2 77  ? 14.789  40.210  24.546  1.00 45.28 ? 76  GLU A OE1   1 
ATOM   3099 O  OE2   . GLU C 2 77  ? 15.351  40.124  22.468  1.00 34.21 ? 76  GLU A OE2   1 
ATOM   3100 N  N     . GLY C 2 78  ? 11.447  39.678  18.527  1.00 27.67 ? 77  GLY A N     1 
ATOM   3101 C  CA    . GLY C 2 78  ? 11.074  40.178  17.215  1.00 28.64 ? 77  GLY A CA    1 
ATOM   3102 C  C     . GLY C 2 78  ? 10.905  38.998  16.283  1.00 24.28 ? 77  GLY A C     1 
ATOM   3103 O  O     . GLY C 2 78  ? 11.379  37.892  16.562  1.00 23.98 ? 77  GLY A O     1 
ATOM   3104 N  N     . PHE C 2 79  ? 10.213  39.246  15.173  1.00 24.24 ? 78  PHE A N     1 
ATOM   3105 C  CA    . PHE C 2 79  ? 9.747   38.178  14.297  1.00 23.68 ? 78  PHE A CA    1 
ATOM   3106 C  C     . PHE C 2 79  ? 10.092  38.488  12.856  1.00 24.18 ? 78  PHE A C     1 
ATOM   3107 O  O     . PHE C 2 79  ? 9.724   39.548  12.352  1.00 24.10 ? 78  PHE A O     1 
ATOM   3108 C  CB    . PHE C 2 79  ? 8.240   37.971  14.417  1.00 26.25 ? 78  PHE A CB    1 
ATOM   3109 C  CG    . PHE C 2 79  ? 7.831   37.602  15.795  1.00 26.48 ? 78  PHE A CG    1 
ATOM   3110 C  CD1   . PHE C 2 79  ? 7.619   38.580  16.756  1.00 26.46 ? 78  PHE A CD1   1 
ATOM   3111 C  CD2   . PHE C 2 79  ? 7.758   36.264  16.169  1.00 29.43 ? 78  PHE A CD2   1 
ATOM   3112 C  CE1   . PHE C 2 79  ? 7.316   38.225  18.046  1.00 27.26 ? 78  PHE A CE1   1 
ATOM   3113 C  CE2   . PHE C 2 79  ? 7.450   35.918  17.447  1.00 26.47 ? 78  PHE A CE2   1 
ATOM   3114 C  CZ    . PHE C 2 79  ? 7.231   36.872  18.385  1.00 30.26 ? 78  PHE A CZ    1 
ATOM   3115 N  N     . LEU C 2 80  ? 10.778  37.545  12.197  1.00 22.27 ? 79  LEU A N     1 
ATOM   3116 C  CA    . LEU C 2 80  ? 10.951  37.571  10.743  1.00 21.19 ? 79  LEU A CA    1 
ATOM   3117 C  C     . LEU C 2 80  ? 9.761   36.844  10.152  1.00 22.36 ? 79  LEU A C     1 
ATOM   3118 O  O     . LEU C 2 80  ? 9.637   35.623  10.316  1.00 23.26 ? 79  LEU A O     1 
ATOM   3119 C  CB    . LEU C 2 80  ? 12.223  36.860  10.289  1.00 21.95 ? 79  LEU A CB    1 
ATOM   3120 C  CG    . LEU C 2 80  ? 13.522  37.570  10.095  1.00 25.20 ? 79  LEU A CG    1 
ATOM   3121 C  CD1   . LEU C 2 80  ? 14.286  36.664  9.181   1.00 22.44 ? 79  LEU A CD1   1 
ATOM   3122 C  CD2   . LEU C 2 80  ? 13.528  38.969  9.586   1.00 25.22 ? 79  LEU A CD2   1 
ATOM   3123 N  N     . CYS C 2 81  ? 8.891   37.578  9.484   1.00 22.51 ? 80  CYS A N     1 
ATOM   3124 C  CA    . CYS C 2 81  ? 7.711   37.013  8.849   1.00 23.33 ? 80  CYS A CA    1 
ATOM   3125 C  C     . CYS C 2 81  ? 8.045   36.736  7.379   1.00 23.61 ? 80  CYS A C     1 
ATOM   3126 O  O     . CYS C 2 81  ? 8.085   37.668  6.575   1.00 24.55 ? 80  CYS A O     1 
ATOM   3127 C  CB    . CYS C 2 81  ? 6.547   37.977  8.953   1.00 26.83 ? 80  CYS A CB    1 
ATOM   3128 S  SG    . CYS C 2 81  ? 6.055   38.227  10.652  1.00 29.77 ? 80  CYS A SG    1 
ATOM   3129 N  N     . VAL C 2 82  ? 8.195   35.457  7.019   1.00 21.70 ? 81  VAL A N     1 
ATOM   3130 C  CA    . VAL C 2 82  ? 8.781   35.078  5.724   1.00 23.23 ? 81  VAL A CA    1 
ATOM   3131 C  C     . VAL C 2 82  ? 7.698   34.532  4.794   1.00 24.42 ? 81  VAL A C     1 
ATOM   3132 O  O     . VAL C 2 82  ? 6.885   33.689  5.194   1.00 24.15 ? 81  VAL A O     1 
ATOM   3133 C  CB    . VAL C 2 82  ? 9.881   34.024  5.908   1.00 21.26 ? 81  VAL A CB    1 
ATOM   3134 C  CG1   . VAL C 2 82  ? 10.628  33.729  4.530   1.00 20.52 ? 81  VAL A CG1   1 
ATOM   3135 C  CG2   . VAL C 2 82  ? 10.843  34.434  6.987   1.00 23.17 ? 81  VAL A CG2   1 
ATOM   3136 N  N     . PHE C 2 83  ? 7.706   34.974  3.543   1.00 25.75 ? 82  PHE A N     1 
ATOM   3137 C  CA    . PHE C 2 83  ? 6.937   34.287  2.503   1.00 24.76 ? 82  PHE A CA    1 
ATOM   3138 C  C     . PHE C 2 83  ? 7.887   34.041  1.340   1.00 27.28 ? 82  PHE A C     1 
ATOM   3139 O  O     . PHE C 2 83  ? 9.009   34.550  1.335   1.00 25.66 ? 82  PHE A O     1 
ATOM   3140 C  CB    . PHE C 2 83  ? 5.701   35.097  2.053   1.00 24.16 ? 82  PHE A CB    1 
ATOM   3141 C  CG    . PHE C 2 83  ? 6.029   36.374  1.360   1.00 29.28 ? 82  PHE A CG    1 
ATOM   3142 C  CD1   . PHE C 2 83  ? 6.329   37.521  2.098   1.00 28.57 ? 82  PHE A CD1   1 
ATOM   3143 C  CD2   . PHE C 2 83  ? 6.068   36.440  -0.044  1.00 27.01 ? 82  PHE A CD2   1 
ATOM   3144 C  CE1   . PHE C 2 83  ? 6.642   38.719  1.469   1.00 27.28 ? 82  PHE A CE1   1 
ATOM   3145 C  CE2   . PHE C 2 83  ? 6.410   37.631  -0.695  1.00 30.57 ? 82  PHE A CE2   1 
ATOM   3146 C  CZ    . PHE C 2 83  ? 6.697   38.780  0.059   1.00 31.15 ? 82  PHE A CZ    1 
ATOM   3147 N  N     . ALA C 2 84  ? 7.445   33.255  0.359   1.00 27.57 ? 83  ALA A N     1 
ATOM   3148 C  CA    . ALA C 2 84  ? 8.241   33.000  -0.834  1.00 29.09 ? 83  ALA A CA    1 
ATOM   3149 C  C     . ALA C 2 84  ? 7.616   33.774  -1.994  1.00 31.43 ? 83  ALA A C     1 
ATOM   3150 O  O     . ALA C 2 84  ? 6.380   33.789  -2.164  1.00 30.66 ? 83  ALA A O     1 
ATOM   3151 C  CB    . ALA C 2 84  ? 8.326   31.504  -1.162  1.00 29.16 ? 83  ALA A CB    1 
ATOM   3152 N  N     . ILE C 2 85  ? 8.465   34.444  -2.774  1.00 26.75 ? 84  ILE A N     1 
ATOM   3153 C  CA    . ILE C 2 85  ? 7.941   35.323  -3.812  1.00 33.59 ? 84  ILE A CA    1 
ATOM   3154 C  C     . ILE C 2 85  ? 7.352   34.569  -4.980  1.00 33.53 ? 84  ILE A C     1 
ATOM   3155 O  O     . ILE C 2 85  ? 6.707   35.183  -5.820  1.00 38.12 ? 84  ILE A O     1 
ATOM   3156 C  CB    . ILE C 2 85  ? 9.006   36.314  -4.322  1.00 35.19 ? 84  ILE A CB    1 
ATOM   3157 C  CG1   . ILE C 2 85  ? 10.072  35.552  -5.141  1.00 32.43 ? 84  ILE A CG1   1 
ATOM   3158 C  CG2   . ILE C 2 85  ? 9.468   37.317  -3.222  1.00 32.11 ? 84  ILE A CG2   1 
ATOM   3159 C  CD1   . ILE C 2 85  ? 10.904  36.476  -5.944  1.00 39.56 ? 84  ILE A CD1   1 
ATOM   3160 N  N     . ASN C 2 86  ? 7.504   33.252  -5.032  1.00 33.84 ? 85  ASN A N     1 
ATOM   3161 C  CA    . ASN C 2 86  ? 6.821   32.431  -6.025  1.00 37.59 ? 85  ASN A CA    1 
ATOM   3162 C  C     . ASN C 2 86  ? 5.637   31.650  -5.438  1.00 37.78 ? 85  ASN A C     1 
ATOM   3163 O  O     . ASN C 2 86  ? 5.177   30.678  -6.039  1.00 37.71 ? 85  ASN A O     1 
ATOM   3164 C  CB    . ASN C 2 86  ? 7.821   31.481  -6.680  1.00 38.78 ? 85  ASN A CB    1 
ATOM   3165 C  CG    . ASN C 2 86  ? 8.352   30.471  -5.710  1.00 37.93 ? 85  ASN A CG    1 
ATOM   3166 O  OD1   . ASN C 2 86  ? 8.380   30.740  -4.510  1.00 33.43 ? 85  ASN A OD1   1 
ATOM   3167 N  ND2   . ASN C 2 86  ? 8.770   29.308  -6.206  1.00 38.72 ? 85  ASN A ND2   1 
ATOM   3168 N  N     . ASN C 2 87  ? 5.113   32.066  -4.285  1.00 37.76 ? 86  ASN A N     1 
ATOM   3169 C  CA    . ASN C 2 87  ? 4.016   31.322  -3.649  1.00 37.39 ? 86  ASN A CA    1 
ATOM   3170 C  C     . ASN C 2 87  ? 3.027   32.306  -3.016  1.00 37.09 ? 86  ASN A C     1 
ATOM   3171 O  O     . ASN C 2 87  ? 3.193   32.756  -1.877  1.00 34.97 ? 86  ASN A O     1 
ATOM   3172 C  CB    . ASN C 2 87  ? 4.573   30.319  -2.653  1.00 36.23 ? 86  ASN A CB    1 
ATOM   3173 C  CG    . ASN C 2 87  ? 3.506   29.359  -2.151  1.00 44.14 ? 86  ASN A CG    1 
ATOM   3174 O  OD1   . ASN C 2 87  ? 2.703   29.711  -1.278  1.00 40.79 ? 86  ASN A OD1   1 
ATOM   3175 N  ND2   . ASN C 2 87  ? 3.461   28.152  -2.736  1.00 46.19 ? 86  ASN A ND2   1 
ATOM   3176 N  N     . THR C 2 88  ? 1.992   32.656  -3.786  1.00 40.20 ? 87  THR A N     1 
ATOM   3177 C  CA    . THR C 2 88  ? 1.028   33.659  -3.328  1.00 39.03 ? 87  THR A CA    1 
ATOM   3178 C  C     . THR C 2 88  ? 0.340   33.236  -2.027  1.00 37.18 ? 87  THR A C     1 
ATOM   3179 O  O     . THR C 2 88  ? 0.049   34.090  -1.189  1.00 39.04 ? 87  THR A O     1 
ATOM   3180 C  CB    . THR C 2 88  ? -0.020  33.953  -4.413  1.00 42.34 ? 87  THR A CB    1 
ATOM   3181 O  OG1   . THR C 2 88  ? -0.539  32.728  -4.948  1.00 47.59 ? 87  THR A OG1   1 
ATOM   3182 C  CG2   . THR C 2 88  ? 0.594   34.701  -5.551  1.00 41.54 ? 87  THR A CG2   1 
ATOM   3183 N  N     . LYS C 2 89  ? 0.144   31.933  -1.805  1.00 38.56 ? 88  LYS A N     1 
ATOM   3184 C  CA    . LYS C 2 89  ? -0.514  31.470  -0.576  1.00 39.08 ? 88  LYS A CA    1 
ATOM   3185 C  C     . LYS C 2 89  ? 0.352   31.763  0.660   1.00 38.95 ? 88  LYS A C     1 
ATOM   3186 O  O     . LYS C 2 89  ? -0.171  32.104  1.732   1.00 36.71 ? 88  LYS A O     1 
ATOM   3187 C  CB    . LYS C 2 89  ? -0.795  29.967  -0.695  1.00 41.02 ? 88  LYS A CB    1 
ATOM   3188 C  CG    . LYS C 2 89  ? -1.273  29.195  0.564   1.00 46.05 ? 88  LYS A CG    1 
ATOM   3189 C  CD    . LYS C 2 89  ? -2.290  29.961  1.448   1.00 50.26 ? 88  LYS A CD    1 
ATOM   3190 C  CE    . LYS C 2 89  ? -2.863  29.069  2.576   1.00 50.38 ? 88  LYS A CE    1 
ATOM   3191 N  NZ    . LYS C 2 89  ? -2.067  27.798  2.744   1.00 51.88 ? 88  LYS A NZ    1 
ATOM   3192 N  N     . SER C 2 90  ? 1.686   31.622  0.534   1.00 37.34 ? 89  SER A N     1 
ATOM   3193 C  CA    . SER C 2 90  ? 2.570   31.973  1.647   1.00 33.63 ? 89  SER A CA    1 
ATOM   3194 C  C     . SER C 2 90  ? 2.523   33.469  1.954   1.00 35.22 ? 89  SER A C     1 
ATOM   3195 O  O     . SER C 2 90  ? 2.642   33.868  3.122   1.00 32.07 ? 89  SER A O     1 
ATOM   3196 C  CB    . SER C 2 90  ? 4.000   31.524  1.335   1.00 34.46 ? 89  SER A CB    1 
ATOM   3197 O  OG    . SER C 2 90  ? 4.537   32.282  0.267   1.00 32.37 ? 89  SER A OG    1 
ATOM   3198 N  N     . PHE C 2 91  ? 2.306   34.307  0.932   1.00 32.32 ? 90  PHE A N     1 
ATOM   3199 C  CA    . PHE C 2 91  ? 2.114   35.733  1.158   1.00 31.61 ? 90  PHE A CA    1 
ATOM   3200 C  C     . PHE C 2 91  ? 0.801   35.990  1.869   1.00 34.75 ? 90  PHE A C     1 
ATOM   3201 O  O     . PHE C 2 91  ? 0.731   36.833  2.763   1.00 34.38 ? 90  PHE A O     1 
ATOM   3202 C  CB    . PHE C 2 91  ? 2.171   36.478  -0.178  1.00 35.86 ? 90  PHE A CB    1 
ATOM   3203 C  CG    . PHE C 2 91  ? 1.995   37.966  -0.072  1.00 35.77 ? 90  PHE A CG    1 
ATOM   3204 C  CD1   . PHE C 2 91  ? 2.983   38.752  0.508   1.00 35.61 ? 90  PHE A CD1   1 
ATOM   3205 C  CD2   . PHE C 2 91  ? 0.860   38.580  -0.565  1.00 37.54 ? 90  PHE A CD2   1 
ATOM   3206 C  CE1   . PHE C 2 91  ? 2.858   40.113  0.607   1.00 37.46 ? 90  PHE A CE1   1 
ATOM   3207 C  CE2   . PHE C 2 91  ? 0.720   39.964  -0.466  1.00 41.86 ? 90  PHE A CE2   1 
ATOM   3208 C  CZ    . PHE C 2 91  ? 1.745   40.730  0.112   1.00 40.75 ? 90  PHE A CZ    1 
ATOM   3209 N  N     . GLU C 2 92  ? -0.237  35.250  1.505   1.00 33.92 ? 91  GLU A N     1 
ATOM   3210 C  CA    . GLU C 2 92  ? -1.534  35.454  2.136   1.00 39.30 ? 91  GLU A CA    1 
ATOM   3211 C  C     . GLU C 2 92  ? -1.501  34.991  3.587   1.00 38.54 ? 91  GLU A C     1 
ATOM   3212 O  O     . GLU C 2 92  ? -2.163  35.584  4.449   1.00 39.17 ? 91  GLU A O     1 
ATOM   3213 C  CB    . GLU C 2 92  ? -2.591  34.701  1.348   1.00 39.43 ? 91  GLU A CB    1 
ATOM   3214 C  CG    . GLU C 2 92  ? -2.875  35.315  -0.027  1.00 42.74 ? 91  GLU A CG    1 
ATOM   3215 C  CD    . GLU C 2 92  ? -3.678  34.389  -0.905  1.00 50.01 ? 91  GLU A CD    1 
ATOM   3216 O  OE1   . GLU C 2 92  ? -3.813  33.186  -0.545  1.00 50.52 ? 91  GLU A OE1   1 
ATOM   3217 O  OE2   . GLU C 2 92  ? -4.207  34.869  -1.934  1.00 47.88 ? 91  GLU A OE2   1 
ATOM   3218 N  N     . ASP C 2 93  ? -0.709  33.950  3.860   1.00 37.82 ? 92  ASP A N     1 
ATOM   3219 C  CA    . ASP C 2 93  ? -0.518  33.426  5.210   1.00 38.54 ? 92  ASP A CA    1 
ATOM   3220 C  C     . ASP C 2 93  ? 0.079   34.449  6.162   1.00 38.85 ? 92  ASP A C     1 
ATOM   3221 O  O     . ASP C 2 93  ? -0.091  34.325  7.382   1.00 37.53 ? 92  ASP A O     1 
ATOM   3222 C  CB    . ASP C 2 93  ? 0.398   32.197  5.185   1.00 36.94 ? 92  ASP A CB    1 
ATOM   3223 C  CG    . ASP C 2 93  ? -0.293  30.964  4.653   1.00 40.16 ? 92  ASP A CG    1 
ATOM   3224 O  OD1   . ASP C 2 93  ? -1.525  31.056  4.477   1.00 38.94 ? 92  ASP A OD1   1 
ATOM   3225 O  OD2   . ASP C 2 93  ? 0.387   29.912  4.420   1.00 38.44 ? 92  ASP A OD2   1 
ATOM   3226 N  N     . ILE C 2 94  ? 0.771   35.449  5.624   1.00 36.14 ? 93  ILE A N     1 
ATOM   3227 C  CA    . ILE C 2 94  ? 1.457   36.437  6.445   1.00 36.86 ? 93  ILE A CA    1 
ATOM   3228 C  C     . ILE C 2 94  ? 0.488   37.136  7.388   1.00 40.01 ? 93  ILE A C     1 
ATOM   3229 O  O     . ILE C 2 94  ? 0.772   37.309  8.579   1.00 36.74 ? 93  ILE A O     1 
ATOM   3230 C  CB    . ILE C 2 94  ? 2.170   37.444  5.528   1.00 38.10 ? 93  ILE A CB    1 
ATOM   3231 C  CG1   . ILE C 2 94  ? 3.361   36.768  4.863   1.00 33.17 ? 93  ILE A CG1   1 
ATOM   3232 C  CG2   . ILE C 2 94  ? 2.568   38.681  6.304   1.00 37.41 ? 93  ILE A CG2   1 
ATOM   3233 C  CD1   . ILE C 2 94  ? 4.491   36.429  5.843   1.00 30.17 ? 93  ILE A CD1   1 
ATOM   3234 N  N     . HIS C 2 95  ? -0.647  37.597  6.848   1.00 39.40 ? 94  HIS A N     1 
ATOM   3235 C  CA    . HIS C 2 95  ? -1.669  38.246  7.668   1.00 43.17 ? 94  HIS A CA    1 
ATOM   3236 C  C     . HIS C 2 95  ? -2.006  37.383  8.872   1.00 41.26 ? 94  HIS A C     1 
ATOM   3237 O  O     . HIS C 2 95  ? -2.037  37.857  10.013  1.00 41.09 ? 94  HIS A O     1 
ATOM   3238 C  CB    . HIS C 2 95  ? -2.921  38.481  6.829   1.00 40.80 ? 94  HIS A CB    1 
ATOM   3239 C  CG    . HIS C 2 95  ? -4.068  39.076  7.587   1.00 50.89 ? 94  HIS A CG    1 
ATOM   3240 N  ND1   . HIS C 2 95  ? -5.329  38.513  7.577   1.00 51.14 ? 94  HIS A ND1   1 
ATOM   3241 C  CD2   . HIS C 2 95  ? -4.174  40.226  8.300   1.00 49.49 ? 94  HIS A CD2   1 
ATOM   3242 C  CE1   . HIS C 2 95  ? -6.144  39.250  8.310   1.00 50.36 ? 94  HIS A CE1   1 
ATOM   3243 N  NE2   . HIS C 2 95  ? -5.470  40.297  8.757   1.00 50.84 ? 94  HIS A NE2   1 
ATOM   3244 N  N     . HIS C 2 96  ? -2.254  36.098  8.634   1.00 42.36 ? 95  HIS A N     1 
ATOM   3245 C  CA    . HIS C 2 96  ? -2.638  35.238  9.747   1.00 41.46 ? 95  HIS A CA    1 
ATOM   3246 C  C     . HIS C 2 96  ? -1.528  35.188  10.793  1.00 39.77 ? 95  HIS A C     1 
ATOM   3247 O  O     . HIS C 2 96  ? -1.807  35.169  11.992  1.00 35.72 ? 95  HIS A O     1 
ATOM   3248 C  CB    . HIS C 2 96  ? -2.993  33.837  9.236   1.00 43.57 ? 95  HIS A CB    1 
ATOM   3249 C  CG    . HIS C 2 96  ? -4.146  33.825  8.268   1.00 48.13 ? 95  HIS A CG    1 
ATOM   3250 N  ND1   . HIS C 2 96  ? -4.090  34.425  7.024   1.00 49.25 ? 95  HIS A ND1   1 
ATOM   3251 C  CD2   . HIS C 2 96  ? -5.406  33.335  8.388   1.00 54.73 ? 95  HIS A CD2   1 
ATOM   3252 C  CE1   . HIS C 2 96  ? -5.263  34.297  6.417   1.00 49.40 ? 95  HIS A CE1   1 
ATOM   3253 N  NE2   . HIS C 2 96  ? -6.074  33.629  7.218   1.00 57.18 ? 95  HIS A NE2   1 
ATOM   3254 N  N     . TYR C 2 97  ? -0.257  35.225  10.362  1.00 37.67 ? 96  TYR A N     1 
ATOM   3255 C  CA    . TYR C 2 97  ? 0.830   35.161  11.336  1.00 36.63 ? 96  TYR A CA    1 
ATOM   3256 C  C     . TYR C 2 97  ? 0.937   36.452  12.130  1.00 36.92 ? 96  TYR A C     1 
ATOM   3257 O  O     . TYR C 2 97  ? 1.158   36.423  13.346  1.00 35.19 ? 96  TYR A O     1 
ATOM   3258 C  CB    . TYR C 2 97  ? 2.180   34.871  10.658  1.00 30.90 ? 96  TYR A CB    1 
ATOM   3259 C  CG    . TYR C 2 97  ? 2.477   33.391  10.543  1.00 30.75 ? 96  TYR A CG    1 
ATOM   3260 C  CD1   . TYR C 2 97  ? 2.985   32.699  11.622  1.00 32.08 ? 96  TYR A CD1   1 
ATOM   3261 C  CD2   . TYR C 2 97  ? 2.231   32.692  9.368   1.00 31.83 ? 96  TYR A CD2   1 
ATOM   3262 C  CE1   . TYR C 2 97  ? 3.255   31.333  11.523  1.00 30.93 ? 96  TYR A CE1   1 
ATOM   3263 C  CE2   . TYR C 2 97  ? 2.499   31.339  9.276   1.00 31.73 ? 96  TYR A CE2   1 
ATOM   3264 C  CZ    . TYR C 2 97  ? 2.995   30.689  10.355  1.00 31.36 ? 96  TYR A CZ    1 
ATOM   3265 O  OH    . TYR C 2 97  ? 3.250   29.357  10.282  1.00 35.10 ? 96  TYR A OH    1 
ATOM   3266 N  N     . ARG C 2 98  ? 0.868   37.588  11.453  1.00 36.52 ? 97  ARG A N     1 
ATOM   3267 C  CA    . ARG C 2 98  ? 0.990   38.861  12.151  1.00 38.35 ? 97  ARG A CA    1 
ATOM   3268 C  C     . ARG C 2 98  ? -0.138  39.036  13.143  1.00 37.73 ? 97  ARG A C     1 
ATOM   3269 O  O     . ARG C 2 98  ? 0.082   39.449  14.284  1.00 39.96 ? 97  ARG A O     1 
ATOM   3270 C  CB    . ARG C 2 98  ? 0.960   40.011  11.161  1.00 42.35 ? 97  ARG A CB    1 
ATOM   3271 C  CG    . ARG C 2 98  ? 1.225   41.356  11.801  1.00 42.96 ? 97  ARG A CG    1 
ATOM   3272 C  CD    . ARG C 2 98  ? 1.243   42.447  10.725  1.00 43.61 ? 97  ARG A CD    1 
ATOM   3273 N  NE    . ARG C 2 98  ? 0.857   43.746  11.257  1.00 44.35 ? 97  ARG A NE    1 
ATOM   3274 C  CZ    . ARG C 2 98  ? 1.688   44.521  11.948  1.00 47.57 ? 97  ARG A CZ    1 
ATOM   3275 N  NH1   . ARG C 2 98  ? 2.941   44.148  12.195  1.00 48.42 ? 97  ARG A NH1   1 
ATOM   3276 N  NH2   . ARG C 2 98  ? 1.261   45.699  12.393  1.00 51.74 ? 97  ARG A NH2   1 
ATOM   3277 N  N     . GLU C 2 99  ? -1.365  38.759  12.693  1.00 39.73 ? 98  GLU A N     1 
ATOM   3278 C  CA    . GLU C 2 99  ? -2.531  38.823  13.569  1.00 40.28 ? 98  GLU A CA    1 
ATOM   3279 C  C     . GLU C 2 99  ? -2.294  37.983  14.807  1.00 40.67 ? 98  GLU A C     1 
ATOM   3280 O  O     . GLU C 2 99  ? -2.550  38.433  15.929  1.00 39.26 ? 98  GLU A O     1 
ATOM   3281 C  CB    . GLU C 2 99  ? -3.767  38.350  12.809  1.00 41.04 ? 98  GLU A CB    1 
ATOM   3282 C  CG    . GLU C 2 99  ? -4.475  39.446  11.987  1.00 48.48 ? 98  GLU A CG    1 
ATOM   3283 C  CD    . GLU C 2 99  ? -4.381  40.854  12.602  1.00 50.68 ? 98  GLU A CD    1 
ATOM   3284 O  OE1   . GLU C 2 99  ? -3.746  41.747  11.972  1.00 49.95 ? 98  GLU A OE1   1 
ATOM   3285 O  OE2   . GLU C 2 99  ? -5.009  41.076  13.676  1.00 45.84 ? 98  GLU A OE2   1 
ATOM   3286 N  N     . GLN C 2 100 ? -1.723  36.785  14.620  1.00 38.60 ? 99  GLN A N     1 
ATOM   3287 C  CA    . GLN C 2 100 ? -1.571  35.868  15.733  1.00 40.20 ? 99  GLN A CA    1 
ATOM   3288 C  C     . GLN C 2 100 ? -0.505  36.364  16.699  1.00 37.38 ? 99  GLN A C     1 
ATOM   3289 O  O     . GLN C 2 100 ? -0.678  36.267  17.917  1.00 37.11 ? 99  GLN A O     1 
ATOM   3290 C  CB    . GLN C 2 100 ? -1.245  34.468  15.214  1.00 36.40 ? 99  GLN A CB    1 
ATOM   3291 C  CG    . GLN C 2 100 ? -1.281  33.428  16.323  1.00 41.84 ? 99  GLN A CG    1 
ATOM   3292 C  CD    . GLN C 2 100 ? -1.154  32.003  15.815  1.00 42.71 ? 99  GLN A CD    1 
ATOM   3293 O  OE1   . GLN C 2 100 ? -0.807  31.776  14.654  1.00 45.24 ? 99  GLN A OE1   1 
ATOM   3294 N  NE2   . GLN C 2 100 ? -1.465  31.028  16.680  1.00 42.38 ? 99  GLN A NE2   1 
ATOM   3295 N  N     . ILE C 2 101 ? 0.595   36.921  16.173  1.00 35.02 ? 100 ILE A N     1 
ATOM   3296 C  CA    . ILE C 2 101 ? 1.627   37.495  17.030  1.00 33.99 ? 100 ILE A CA    1 
ATOM   3297 C  C     . ILE C 2 101 ? 1.078   38.675  17.828  1.00 39.36 ? 100 ILE A C     1 
ATOM   3298 O  O     . ILE C 2 101 ? 1.344   38.820  19.030  1.00 37.19 ? 100 ILE A O     1 
ATOM   3299 C  CB    . ILE C 2 101 ? 2.847   37.921  16.194  1.00 36.02 ? 100 ILE A CB    1 
ATOM   3300 C  CG1   . ILE C 2 101 ? 3.572   36.703  15.609  1.00 33.28 ? 100 ILE A CG1   1 
ATOM   3301 C  CG2   . ILE C 2 101 ? 3.792   38.694  17.084  1.00 36.35 ? 100 ILE A CG2   1 
ATOM   3302 C  CD1   . ILE C 2 101 ? 4.326   37.033  14.367  1.00 31.82 ? 100 ILE A CD1   1 
ATOM   3303 N  N     . LYS C 2 102 ? 0.359   39.574  17.165  1.00 39.62 ? 101 LYS A N     1 
ATOM   3304 C  CA    . LYS C 2 102 ? -0.305  40.647  17.913  1.00 39.52 ? 101 LYS A CA    1 
ATOM   3305 C  C     . LYS C 2 102 ? -1.271  40.077  18.955  1.00 40.60 ? 101 LYS A C     1 
ATOM   3306 O  O     . LYS C 2 102 ? -1.314  40.538  20.111  1.00 42.69 ? 101 LYS A O     1 
ATOM   3307 C  CB    . LYS C 2 102 ? -1.053  41.571  16.951  1.00 41.45 ? 101 LYS A CB    1 
ATOM   3308 C  CG    . LYS C 2 102 ? -0.170  42.476  16.090  1.00 41.86 ? 101 LYS A CG    1 
ATOM   3309 C  CD    . LYS C 2 102 ? -1.030  43.562  15.368  1.00 43.88 ? 101 LYS A CD    1 
ATOM   3310 C  CE    . LYS C 2 102 ? -2.012  42.896  14.425  1.00 43.99 ? 101 LYS A CE    1 
ATOM   3311 N  NZ    . LYS C 2 102 ? -2.978  43.804  13.735  1.00 47.94 ? 101 LYS A NZ    1 
ATOM   3312 N  N     . ARG C 2 103 ? -2.094  39.096  18.552  1.00 38.05 ? 102 ARG A N     1 
ATOM   3313 C  CA    . ARG C 2 103 ? -3.133  38.597  19.466  1.00 43.38 ? 102 ARG A CA    1 
ATOM   3314 C  C     . ARG C 2 103 ? -2.485  37.906  20.664  1.00 43.05 ? 102 ARG A C     1 
ATOM   3315 O  O     . ARG C 2 103 ? -2.915  38.094  21.803  1.00 44.18 ? 102 ARG A O     1 
ATOM   3316 C  CB    . ARG C 2 103 ? -4.084  37.666  18.686  1.00 41.27 ? 102 ARG A CB    1 
ATOM   3317 C  CG    . ARG C 2 103 ? -5.326  37.110  19.332  1.00 46.20 ? 102 ARG A CG    1 
ATOM   3318 C  CD    . ARG C 2 103 ? -6.227  36.446  18.245  1.00 51.06 ? 102 ARG A CD    1 
ATOM   3319 N  NE    . ARG C 2 103 ? -5.624  35.270  17.606  1.00 53.77 ? 102 ARG A NE    1 
ATOM   3320 C  CZ    . ARG C 2 103 ? -5.346  35.130  16.306  1.00 49.96 ? 102 ARG A CZ    1 
ATOM   3321 N  NH1   . ARG C 2 103 ? -5.540  36.112  15.436  1.00 50.03 ? 102 ARG A NH1   1 
ATOM   3322 N  NH2   . ARG C 2 103 ? -4.863  33.969  15.865  1.00 51.53 ? 102 ARG A NH2   1 
ATOM   3323 N  N     . VAL C 2 104 ? -1.384  37.171  20.427  1.00 41.96 ? 103 VAL A N     1 
ATOM   3324 C  CA    . VAL C 2 104 ? -0.685  36.487  21.516  1.00 42.66 ? 103 VAL A CA    1 
ATOM   3325 C  C     . VAL C 2 104 ? 0.087   37.479  22.391  1.00 40.07 ? 103 VAL A C     1 
ATOM   3326 O  O     . VAL C 2 104 ? 0.050   37.395  23.620  1.00 45.08 ? 103 VAL A O     1 
ATOM   3327 C  CB    . VAL C 2 104 ? 0.221   35.373  20.963  1.00 44.91 ? 103 VAL A CB    1 
ATOM   3328 C  CG1   . VAL C 2 104 ? 1.066   34.760  22.070  1.00 42.63 ? 103 VAL A CG1   1 
ATOM   3329 C  CG2   . VAL C 2 104 ? -0.634  34.283  20.273  1.00 44.14 ? 103 VAL A CG2   1 
ATOM   3330 N  N     . LYS C 2 105 ? 0.752   38.446  21.801  1.00 37.09 ? 104 LYS A N     1 
ATOM   3331 C  CA    . LYS C 2 105 ? 1.483   39.432  22.580  1.00 39.05 ? 104 LYS A CA    1 
ATOM   3332 C  C     . LYS C 2 105 ? 0.577   40.541  23.110  1.00 42.54 ? 104 LYS A C     1 
ATOM   3333 O  O     . LYS C 2 105 ? 1.004   41.352  23.948  1.00 43.52 ? 104 LYS A O     1 
ATOM   3334 C  CB    . LYS C 2 105 ? 2.573   40.027  21.706  1.00 44.03 ? 104 LYS A CB    1 
ATOM   3335 C  CG    . LYS C 2 105 ? 3.744   39.082  21.494  1.00 38.82 ? 104 LYS A CG    1 
ATOM   3336 C  CD    . LYS C 2 105 ? 4.990   39.910  21.371  1.00 42.48 ? 104 LYS A CD    1 
ATOM   3337 C  CE    . LYS C 2 105 ? 6.205   39.086  21.513  1.00 36.56 ? 104 LYS A CE    1 
ATOM   3338 N  NZ    . LYS C 2 105 ? 6.670   38.821  22.891  1.00 35.04 ? 104 LYS A NZ    1 
ATOM   3339 N  N     . ASP C 2 106 ? -0.670  40.589  22.652  1.00 47.57 ? 105 ASP A N     1 
ATOM   3340 C  CA    . ASP C 2 106 ? -1.620  41.662  22.980  1.00 44.14 ? 105 ASP A CA    1 
ATOM   3341 C  C     . ASP C 2 106 ? -1.014  43.066  22.842  1.00 44.85 ? 105 ASP A C     1 
ATOM   3342 O  O     . ASP C 2 106 ? -1.063  43.907  23.745  1.00 47.18 ? 105 ASP A O     1 
ATOM   3343 C  CB    . ASP C 2 106 ? -2.230  41.444  24.356  1.00 46.53 ? 105 ASP A CB    1 
ATOM   3344 C  CG    . ASP C 2 106 ? -3.486  42.214  24.499  1.00 50.16 ? 105 ASP A CG    1 
ATOM   3345 O  OD1   . ASP C 2 106 ? -4.283  42.144  23.531  1.00 50.00 ? 105 ASP A OD1   1 
ATOM   3346 O  OD2   . ASP C 2 106 ? -3.682  42.865  25.558  1.00 52.47 ? 105 ASP A OD2   1 
ATOM   3347 N  N     . SER C 2 107 ? -0.481  43.329  21.650  1.00 45.36 ? 106 SER A N     1 
ATOM   3348 C  CA    . SER C 2 107 ? 0.149   44.600  21.341  1.00 43.61 ? 106 SER A CA    1 
ATOM   3349 C  C     . SER C 2 107 ? 0.102   44.813  19.832  1.00 46.57 ? 106 SER A C     1 
ATOM   3350 O  O     . SER C 2 107 ? 0.331   43.878  19.046  1.00 41.94 ? 106 SER A O     1 
ATOM   3351 C  CB    . SER C 2 107 ? 1.611   44.640  21.831  1.00 46.36 ? 106 SER A CB    1 
ATOM   3352 O  OG    . SER C 2 107 ? 2.271   45.873  21.529  1.00 43.08 ? 106 SER A OG    1 
ATOM   3353 N  N     . GLU C 2 108 ? -0.166  46.054  19.446  1.00 44.51 ? 107 GLU A N     1 
ATOM   3354 C  CA    . GLU C 2 108 ? -0.108  46.468  18.058  1.00 45.10 ? 107 GLU A CA    1 
ATOM   3355 C  C     . GLU C 2 108 ? 1.308   46.825  17.643  1.00 46.70 ? 107 GLU A C     1 
ATOM   3356 O  O     . GLU C 2 108 ? 1.549   47.098  16.461  1.00 46.97 ? 107 GLU A O     1 
ATOM   3357 C  CB    . GLU C 2 108 ? -1.048  47.670  17.848  1.00 47.26 ? 107 GLU A CB    1 
ATOM   3358 C  CG    . GLU C 2 108 ? -2.537  47.312  17.920  1.00 49.19 ? 107 GLU A CG    1 
ATOM   3359 C  CD    . GLU C 2 108 ? -2.975  46.426  16.780  1.00 51.37 ? 107 GLU A CD    1 
ATOM   3360 O  OE1   . GLU C 2 108 ? -2.815  46.862  15.631  1.00 50.48 ? 107 GLU A OE1   1 
ATOM   3361 O  OE2   . GLU C 2 108 ? -3.454  45.295  17.019  1.00 51.43 ? 107 GLU A OE2   1 
ATOM   3362 N  N     . ASP C 2 109 ? 2.256   46.823  18.586  1.00 42.97 ? 108 ASP A N     1 
ATOM   3363 C  CA    . ASP C 2 109 ? 3.599   47.344  18.335  1.00 43.33 ? 108 ASP A CA    1 
ATOM   3364 C  C     . ASP C 2 109 ? 4.639   46.265  18.710  1.00 43.05 ? 108 ASP A C     1 
ATOM   3365 O  O     . ASP C 2 109 ? 5.259   46.256  19.774  1.00 43.37 ? 108 ASP A O     1 
ATOM   3366 C  CB    . ASP C 2 109 ? 3.781   48.644  19.078  1.00 48.19 ? 108 ASP A CB    1 
ATOM   3367 C  CG    . ASP C 2 109 ? 5.157   49.216  18.904  1.00 53.92 ? 108 ASP A CG    1 
ATOM   3368 O  OD1   . ASP C 2 109 ? 5.729   49.062  17.794  1.00 53.83 ? 108 ASP A OD1   1 
ATOM   3369 O  OD2   . ASP C 2 109 ? 5.628   49.894  19.853  1.00 59.52 ? 108 ASP A OD2   1 
ATOM   3370 N  N     . VAL C 2 110 ? 4.815   45.312  17.801  1.00 41.15 ? 109 VAL A N     1 
ATOM   3371 C  CA    . VAL C 2 110 ? 5.729   44.196  17.983  1.00 37.19 ? 109 VAL A CA    1 
ATOM   3372 C  C     . VAL C 2 110 ? 6.804   44.293  16.911  1.00 33.46 ? 109 VAL A C     1 
ATOM   3373 O  O     . VAL C 2 110 ? 6.474   44.316  15.732  1.00 35.92 ? 109 VAL A O     1 
ATOM   3374 C  CB    . VAL C 2 110 ? 5.017   42.839  17.867  1.00 35.32 ? 109 VAL A CB    1 
ATOM   3375 C  CG1   . VAL C 2 110 ? 6.005   41.717  18.123  1.00 33.12 ? 109 VAL A CG1   1 
ATOM   3376 C  CG2   . VAL C 2 110 ? 3.850   42.781  18.821  1.00 34.70 ? 109 VAL A CG2   1 
ATOM   3377 N  N     . PRO C 2 111 ? 8.085   44.252  17.267  1.00 35.32 ? 110 PRO A N     1 
ATOM   3378 C  CA    . PRO C 2 111 ? 9.147   44.273  16.248  1.00 33.09 ? 110 PRO A CA    1 
ATOM   3379 C  C     . PRO C 2 111 ? 8.989   43.136  15.243  1.00 34.99 ? 110 PRO A C     1 
ATOM   3380 O  O     . PRO C 2 111 ? 8.927   41.970  15.616  1.00 29.35 ? 110 PRO A O     1 
ATOM   3381 C  CB    . PRO C 2 111 ? 10.428  44.129  17.081  1.00 31.76 ? 110 PRO A CB    1 
ATOM   3382 C  CG    . PRO C 2 111 ? 10.008  44.676  18.463  1.00 34.36 ? 110 PRO A CG    1 
ATOM   3383 C  CD    . PRO C 2 111 ? 8.632   44.147  18.632  1.00 35.61 ? 110 PRO A CD    1 
ATOM   3384 N  N     . MET C 2 112 ? 8.848   43.496  13.964  1.00 32.69 ? 111 MET A N     1 
ATOM   3385 C  CA    . MET C 2 112 ? 8.736   42.529  12.883  1.00 30.21 ? 111 MET A CA    1 
ATOM   3386 C  C     . MET C 2 112 ? 9.378   43.089  11.632  1.00 32.99 ? 111 MET A C     1 
ATOM   3387 O  O     . MET C 2 112 ? 9.507   44.307  11.476  1.00 33.09 ? 111 MET A O     1 
ATOM   3388 C  CB    . MET C 2 112 ? 7.296   42.121  12.505  1.00 29.67 ? 111 MET A CB    1 
ATOM   3389 C  CG    . MET C 2 112 ? 6.397   41.679  13.578  1.00 34.98 ? 111 MET A CG    1 
ATOM   3390 S  SD    . MET C 2 112 ? 4.749   41.267  12.900  1.00 37.69 ? 111 MET A SD    1 
ATOM   3391 C  CE    . MET C 2 112 ? 3.798   41.260  14.416  1.00 38.89 ? 111 MET A CE    1 
ATOM   3392 N  N     . VAL C 2 113 ? 9.799   42.160  10.756  1.00 29.19 ? 112 VAL A N     1 
ATOM   3393 C  CA    . VAL C 2 113 ? 10.291  42.461  9.412   1.00 28.43 ? 112 VAL A CA    1 
ATOM   3394 C  C     . VAL C 2 113 ? 9.601   41.512  8.439   1.00 28.72 ? 112 VAL A C     1 
ATOM   3395 O  O     . VAL C 2 113 ? 9.496   40.308  8.706   1.00 28.23 ? 112 VAL A O     1 
ATOM   3396 C  CB    . VAL C 2 113 ? 11.827  42.325  9.335   1.00 25.75 ? 112 VAL A CB    1 
ATOM   3397 C  CG1   . VAL C 2 113 ? 12.321  42.392  7.893   1.00 28.49 ? 112 VAL A CG1   1 
ATOM   3398 C  CG2   . VAL C 2 113 ? 12.470  43.445  10.144  1.00 29.75 ? 112 VAL A CG2   1 
ATOM   3399 N  N     . LEU C 2 114 ? 9.093   42.054  7.337   1.00 27.24 ? 113 LEU A N     1 
ATOM   3400 C  CA    . LEU C 2 114 ? 8.479   41.254  6.283   1.00 26.82 ? 113 LEU A CA    1 
ATOM   3401 C  C     . LEU C 2 114 ? 9.582   40.805  5.344   1.00 26.66 ? 113 LEU A C     1 
ATOM   3402 O  O     . LEU C 2 114 ? 10.330  41.637  4.830   1.00 25.12 ? 113 LEU A O     1 
ATOM   3403 C  CB    . LEU C 2 114 ? 7.413   42.063  5.520   1.00 31.58 ? 113 LEU A CB    1 
ATOM   3404 C  CG    . LEU C 2 114 ? 6.677   41.276  4.406   1.00 32.85 ? 113 LEU A CG    1 
ATOM   3405 C  CD1   . LEU C 2 114 ? 5.838   40.136  4.981   1.00 29.68 ? 113 LEU A CD1   1 
ATOM   3406 C  CD2   . LEU C 2 114 ? 5.800   42.180  3.465   1.00 32.28 ? 113 LEU A CD2   1 
ATOM   3407 N  N     . VAL C 2 115 ? 9.696   39.505  5.120   1.00 23.71 ? 114 VAL A N     1 
ATOM   3408 C  CA    . VAL C 2 115 ? 10.766  38.973  4.271   1.00 25.84 ? 114 VAL A CA    1 
ATOM   3409 C  C     . VAL C 2 115 ? 10.161  38.243  3.078   1.00 25.25 ? 114 VAL A C     1 
ATOM   3410 O  O     . VAL C 2 115 ? 9.458   37.252  3.260   1.00 22.18 ? 114 VAL A O     1 
ATOM   3411 C  CB    . VAL C 2 115 ? 11.680  38.034  5.051   1.00 23.48 ? 114 VAL A CB    1 
ATOM   3412 C  CG1   . VAL C 2 115 ? 12.763  37.379  4.102   1.00 20.04 ? 114 VAL A CG1   1 
ATOM   3413 C  CG2   . VAL C 2 115 ? 12.381  38.804  6.188   1.00 26.76 ? 114 VAL A CG2   1 
ATOM   3414 N  N     . GLY C 2 116 ? 10.472  38.707  1.861   1.00 25.91 ? 115 GLY A N     1 
ATOM   3415 C  CA    . GLY C 2 116 ? 10.134  37.956  0.657   1.00 25.21 ? 115 GLY A CA    1 
ATOM   3416 C  C     . GLY C 2 116 ? 11.320  37.151  0.143   1.00 23.80 ? 115 GLY A C     1 
ATOM   3417 O  O     . GLY C 2 116 ? 12.272  37.716  -0.419  1.00 25.49 ? 115 GLY A O     1 
ATOM   3418 N  N     . ASN C 2 117 ? 11.308  35.843  0.366   1.00 20.78 ? 116 ASN A N     1 
ATOM   3419 C  CA    . ASN C 2 117 ? 12.452  35.003  0.058   1.00 24.56 ? 116 ASN A CA    1 
ATOM   3420 C  C     . ASN C 2 117 ? 12.337  34.349  -1.329  1.00 24.80 ? 116 ASN A C     1 
ATOM   3421 O  O     . ASN C 2 117 ? 11.300  34.410  -1.997  1.00 24.53 ? 116 ASN A O     1 
ATOM   3422 C  CB    . ASN C 2 117 ? 12.592  33.958  1.181   1.00 22.32 ? 116 ASN A CB    1 
ATOM   3423 C  CG    . ASN C 2 117 ? 13.916  33.179  1.083   1.00 21.97 ? 116 ASN A CG    1 
ATOM   3424 O  OD1   . ASN C 2 117 ? 14.989  33.770  0.923   1.00 21.52 ? 116 ASN A OD1   1 
ATOM   3425 N  ND2   . ASN C 2 117 ? 13.823  31.851  1.133   1.00 21.54 ? 116 ASN A ND2   1 
ATOM   3426 N  N     . LYS C 2 118 ? 13.449  33.714  -1.754  1.00 24.29 ? 117 LYS A N     1 
ATOM   3427 C  CA    . LYS C 2 118 ? 13.579  33.040  -3.057  1.00 25.68 ? 117 LYS A CA    1 
ATOM   3428 C  C     . LYS C 2 118 ? 13.662  34.029  -4.215  1.00 28.21 ? 117 LYS A C     1 
ATOM   3429 O  O     . LYS C 2 118 ? 13.257  33.729  -5.339  1.00 28.64 ? 117 LYS A O     1 
ATOM   3430 C  CB    . LYS C 2 118 ? 12.454  32.027  -3.285  1.00 25.14 ? 117 LYS A CB    1 
ATOM   3431 C  CG    . LYS C 2 118 ? 12.230  31.077  -2.109  1.00 25.96 ? 117 LYS A CG    1 
ATOM   3432 C  CD    . LYS C 2 118 ? 11.564  29.736  -2.541  1.00 26.66 ? 117 LYS A CD    1 
ATOM   3433 C  CE    . LYS C 2 118 ? 11.298  28.822  -1.309  1.00 26.21 ? 117 LYS A CE    1 
ATOM   3434 N  NZ    . LYS C 2 118 ? 10.688  27.542  -1.818  1.00 26.15 ? 117 LYS A NZ    1 
ATOM   3435 N  N     . CYS C 2 119 ? 14.249  35.193  -3.976  1.00 28.12 ? 118 CYS A N     1 
ATOM   3436 C  CA    . CYS C 2 119 ? 14.237  36.206  -4.997  1.00 25.13 ? 118 CYS A CA    1 
ATOM   3437 C  C     . CYS C 2 119 ? 15.222  35.900  -6.119  1.00 27.78 ? 118 CYS A C     1 
ATOM   3438 O  O     . CYS C 2 119 ? 15.244  36.618  -7.128  1.00 31.81 ? 118 CYS A O     1 
ATOM   3439 C  CB    . CYS C 2 119 ? 14.496  37.586  -4.378  1.00 28.48 ? 118 CYS A CB    1 
ATOM   3440 S  SG    . CYS C 2 119 ? 16.173  37.787  -3.829  1.00 36.56 ? 118 CYS A SG    1 
ATOM   3441 N  N     . ASP C 2 120 ? 15.922  34.783  -6.030  1.00 29.18 ? 119 ASP A N     1 
ATOM   3442 C  CA    . ASP C 2 120 ? 16.666  34.266  -7.176  1.00 30.28 ? 119 ASP A CA    1 
ATOM   3443 C  C     . ASP C 2 120 ? 15.768  33.576  -8.194  1.00 32.55 ? 119 ASP A C     1 
ATOM   3444 O  O     . ASP C 2 120 ? 16.224  33.230  -9.284  1.00 36.74 ? 119 ASP A O     1 
ATOM   3445 C  CB    . ASP C 2 120 ? 17.712  33.262  -6.670  1.00 29.97 ? 119 ASP A CB    1 
ATOM   3446 C  CG    . ASP C 2 120 ? 17.082  32.113  -5.871  1.00 28.44 ? 119 ASP A CG    1 
ATOM   3447 O  OD1   . ASP C 2 120 ? 16.642  32.322  -4.695  1.00 25.77 ? 119 ASP A OD1   1 
ATOM   3448 O  OD2   . ASP C 2 120 ? 17.019  30.981  -6.416  1.00 29.42 ? 119 ASP A OD2   1 
ATOM   3449 N  N     . LEU C 2 121 ? 14.529  33.328  -7.854  1.00 35.37 ? 120 LEU A N     1 
ATOM   3450 C  CA    . LEU C 2 121 ? 13.815  32.485  -8.808  1.00 34.50 ? 120 LEU A CA    1 
ATOM   3451 C  C     . LEU C 2 121 ? 13.109  33.334  -9.845  1.00 40.72 ? 120 LEU A C     1 
ATOM   3452 O  O     . LEU C 2 121 ? 12.720  34.465  -9.557  1.00 45.68 ? 120 LEU A O     1 
ATOM   3453 C  CB    . LEU C 2 121 ? 12.782  31.630  -8.079  1.00 36.32 ? 120 LEU A CB    1 
ATOM   3454 C  CG    . LEU C 2 121 ? 13.355  30.503  -7.243  1.00 30.98 ? 120 LEU A CG    1 
ATOM   3455 C  CD1   . LEU C 2 121 ? 12.206  29.744  -6.625  1.00 37.66 ? 120 LEU A CD1   1 
ATOM   3456 C  CD2   . LEU C 2 121 ? 14.217  29.560  -8.099  1.00 34.05 ? 120 LEU A CD2   1 
ATOM   3457 N  N     . PRO C 2 122 ? 12.945  32.812  -11.066 1.00 45.58 ? 121 PRO A N     1 
ATOM   3458 C  CA    . PRO C 2 122 ? 12.283  33.590  -12.124 1.00 47.09 ? 121 PRO A CA    1 
ATOM   3459 C  C     . PRO C 2 122 ? 10.766  33.568  -12.065 1.00 56.52 ? 121 PRO A C     1 
ATOM   3460 O  O     . PRO C 2 122 ? 10.116  34.391  -12.733 1.00 55.41 ? 121 PRO A O     1 
ATOM   3461 C  CB    . PRO C 2 122 ? 12.770  32.914  -13.415 1.00 50.34 ? 121 PRO A CB    1 
ATOM   3462 C  CG    . PRO C 2 122 ? 13.088  31.501  -13.008 1.00 46.85 ? 121 PRO A CG    1 
ATOM   3463 C  CD    . PRO C 2 122 ? 13.517  31.543  -11.542 1.00 42.45 ? 121 PRO A CD    1 
ATOM   3464 N  N     . SER C 2 123 ? 10.172  32.661  -11.308 1.00 65.30 ? 122 SER A N     1 
ATOM   3465 C  CA    . SER C 2 123 ? 8.738   32.393  -11.429 1.00 69.46 ? 122 SER A CA    1 
ATOM   3466 C  C     . SER C 2 123 ? 7.940   33.163  -10.374 1.00 69.56 ? 122 SER A C     1 
ATOM   3467 O  O     . SER C 2 123 ? 7.186   32.594  -9.577  1.00 65.39 ? 122 SER A O     1 
ATOM   3468 C  CB    . SER C 2 123 ? 8.499   30.891  -11.326 1.00 74.53 ? 122 SER A CB    1 
ATOM   3469 O  OG    . SER C 2 123 ? 9.261   30.370  -10.244 1.00 69.00 ? 122 SER A OG    1 
ATOM   3470 N  N     . ARG C 2 124 ? 8.095   34.483  -10.391 1.00 58.36 ? 123 ARG A N     1 
ATOM   3471 C  CA    . ARG C 2 124 ? 7.601   35.309  -9.299  1.00 49.19 ? 123 ARG A CA    1 
ATOM   3472 C  C     . ARG C 2 124 ? 6.104   35.519  -9.443  1.00 48.90 ? 123 ARG A C     1 
ATOM   3473 O  O     . ARG C 2 124 ? 5.621   35.764  -10.546 1.00 42.65 ? 123 ARG A O     1 
ATOM   3474 C  CB    . ARG C 2 124 ? 8.310   36.648  -9.321  1.00 49.79 ? 123 ARG A CB    1 
ATOM   3475 C  CG    . ARG C 2 124 ? 7.759   37.640  -8.370  1.00 51.34 ? 123 ARG A CG    1 
ATOM   3476 C  CD    . ARG C 2 124 ? 8.316   39.010  -8.718  1.00 49.39 ? 123 ARG A CD    1 
ATOM   3477 N  NE    . ARG C 2 124 ? 9.674   39.135  -8.201  1.00 53.74 ? 123 ARG A NE    1 
ATOM   3478 C  CZ    . ARG C 2 124 ? 9.990   39.578  -6.991  1.00 47.95 ? 123 ARG A CZ    1 
ATOM   3479 N  NH1   . ARG C 2 124 ? 9.062   39.864  -6.095  1.00 43.76 ? 123 ARG A NH1   1 
ATOM   3480 N  NH2   . ARG C 2 124 ? 11.279  39.700  -6.663  1.00 50.78 ? 123 ARG A NH2   1 
ATOM   3481 N  N     . THR C 2 125 ? 5.365   35.428  -8.327  1.00 42.55 ? 124 THR A N     1 
ATOM   3482 C  CA    . THR C 2 125 ? 3.930   35.678  -8.337  1.00 46.14 ? 124 THR A CA    1 
ATOM   3483 C  C     . THR C 2 125 ? 3.506   36.783  -7.390  1.00 44.63 ? 124 THR A C     1 
ATOM   3484 O  O     . THR C 2 125 ? 2.334   37.176  -7.413  1.00 47.06 ? 124 THR A O     1 
ATOM   3485 C  CB    . THR C 2 125 ? 3.142   34.405  -7.977  1.00 46.31 ? 124 THR A CB    1 
ATOM   3486 O  OG1   . THR C 2 125 ? 3.563   33.949  -6.688  1.00 40.69 ? 124 THR A OG1   1 
ATOM   3487 C  CG2   . THR C 2 125 ? 3.315   33.306  -9.050  1.00 48.69 ? 124 THR A CG2   1 
ATOM   3488 N  N     . VAL C 2 126 ? 4.411   37.298  -6.565  1.00 45.31 ? 125 VAL A N     1 
ATOM   3489 C  CA    . VAL C 2 126 ? 4.100   38.393  -5.666  1.00 43.25 ? 125 VAL A CA    1 
ATOM   3490 C  C     . VAL C 2 126 ? 4.977   39.568  -6.056  1.00 48.53 ? 125 VAL A C     1 
ATOM   3491 O  O     . VAL C 2 126 ? 6.215   39.489  -5.962  1.00 48.80 ? 125 VAL A O     1 
ATOM   3492 C  CB    . VAL C 2 126 ? 4.305   37.993  -4.207  1.00 43.48 ? 125 VAL A CB    1 
ATOM   3493 C  CG1   . VAL C 2 126 ? 3.981   39.153  -3.269  1.00 41.26 ? 125 VAL A CG1   1 
ATOM   3494 C  CG2   . VAL C 2 126 ? 3.502   36.741  -3.925  1.00 41.38 ? 125 VAL A CG2   1 
ATOM   3495 N  N     . ASP C 2 127 ? 4.330   40.638  -6.527  1.00 48.95 ? 126 ASP A N     1 
ATOM   3496 C  CA    . ASP C 2 127 ? 5.009   41.872  -6.893  1.00 52.62 ? 126 ASP A CA    1 
ATOM   3497 C  C     . ASP C 2 127 ? 5.759   42.430  -5.703  1.00 47.36 ? 126 ASP A C     1 
ATOM   3498 O  O     . ASP C 2 127 ? 5.259   42.421  -4.578  1.00 46.66 ? 126 ASP A O     1 
ATOM   3499 C  CB    . ASP C 2 127 ? 3.995   42.945  -7.347  1.00 52.19 ? 126 ASP A CB    1 
ATOM   3500 C  CG    . ASP C 2 127 ? 3.268   42.571  -8.602  1.00 57.39 ? 126 ASP A CG    1 
ATOM   3501 O  OD1   . ASP C 2 127 ? 3.505   41.448  -9.105  1.00 60.65 ? 126 ASP A OD1   1 
ATOM   3502 O  OD2   . ASP C 2 127 ? 2.442   43.389  -9.076  1.00 64.51 ? 126 ASP A OD2   1 
ATOM   3503 N  N     . THR C 2 128 ? 6.932   43.000  -5.981  1.00 48.46 ? 127 THR A N     1 
ATOM   3504 C  CA    . THR C 2 128 ? 7.637   43.781  -4.969  1.00 47.39 ? 127 THR A CA    1 
ATOM   3505 C  C     . THR C 2 128 ? 6.796   44.939  -4.429  1.00 47.77 ? 127 THR A C     1 
ATOM   3506 O  O     . THR C 2 128 ? 6.813   45.206  -3.223  1.00 46.84 ? 127 THR A O     1 
ATOM   3507 C  CB    . THR C 2 128 ? 8.957   44.302  -5.534  1.00 49.79 ? 127 THR A CB    1 
ATOM   3508 O  OG1   . THR C 2 128 ? 9.814   43.197  -5.845  1.00 47.60 ? 127 THR A OG1   1 
ATOM   3509 C  CG2   . THR C 2 128 ? 9.664   45.196  -4.505  1.00 49.33 ? 127 THR A CG2   1 
ATOM   3510 N  N     . LYS C 2 129 ? 6.076   45.674  -5.288  1.00 47.43 ? 128 LYS A N     1 
ATOM   3511 C  CA    . LYS C 2 129 ? 5.328   46.781  -4.702  1.00 47.20 ? 128 LYS A CA    1 
ATOM   3512 C  C     . LYS C 2 129 ? 4.159   46.257  -3.892  1.00 48.32 ? 128 LYS A C     1 
ATOM   3513 O  O     . LYS C 2 129 ? 3.812   46.835  -2.858  1.00 49.72 ? 128 LYS A O     1 
ATOM   3514 C  CB    . LYS C 2 129 ? 4.856   47.796  -5.757  1.00 52.57 ? 128 LYS A CB    1 
ATOM   3515 C  CG    . LYS C 2 129 ? 4.277   49.113  -5.124  1.00 52.06 ? 128 LYS A CG    1 
ATOM   3516 C  CD    . LYS C 2 129 ? 3.628   50.075  -6.158  1.00 57.90 ? 128 LYS A CD    1 
ATOM   3517 C  CE    . LYS C 2 129 ? 2.317   50.678  -5.681  1.00 62.37 ? 128 LYS A CE    1 
ATOM   3518 N  NZ    . LYS C 2 129 ? 1.156   49.729  -5.799  1.00 59.40 ? 128 LYS A NZ    1 
ATOM   3519 N  N     . GLN C 2 130 ? 3.597   45.126  -4.303  1.00 48.15 ? 129 GLN A N     1 
ATOM   3520 C  CA    . GLN C 2 130 ? 2.542   44.492  -3.523  1.00 47.07 ? 129 GLN A CA    1 
ATOM   3521 C  C     . GLN C 2 130 ? 3.020   44.131  -2.111  1.00 47.61 ? 129 GLN A C     1 
ATOM   3522 O  O     . GLN C 2 130 ? 2.285   44.336  -1.131  1.00 45.11 ? 129 GLN A O     1 
ATOM   3523 C  CB    . GLN C 2 130 ? 2.048   43.267  -4.279  1.00 54.01 ? 129 GLN A CB    1 
ATOM   3524 C  CG    . GLN C 2 130 ? 0.906   42.545  -3.644  1.00 55.32 ? 129 GLN A CG    1 
ATOM   3525 C  CD    . GLN C 2 130 ? 0.541   41.316  -4.436  1.00 59.19 ? 129 GLN A CD    1 
ATOM   3526 O  OE1   . GLN C 2 130 ? -0.305  40.524  -4.011  1.00 59.63 ? 129 GLN A OE1   1 
ATOM   3527 N  NE2   . GLN C 2 130 ? 1.182   41.144  -5.609  1.00 56.07 ? 129 GLN A NE2   1 
ATOM   3528 N  N     . ALA C 2 131 ? 4.258   43.615  -1.977  1.00 46.57 ? 130 ALA A N     1 
ATOM   3529 C  CA    . ALA C 2 131 ? 4.776   43.340  -0.636  1.00 42.04 ? 130 ALA A CA    1 
ATOM   3530 C  C     . ALA C 2 131 ? 5.167   44.618  0.088   1.00 43.16 ? 130 ALA A C     1 
ATOM   3531 O  O     . ALA C 2 131 ? 5.014   44.697  1.317   1.00 42.51 ? 130 ALA A O     1 
ATOM   3532 C  CB    . ALA C 2 131 ? 5.973   42.384  -0.687  1.00 40.42 ? 130 ALA A CB    1 
ATOM   3533 N  N     . GLN C 2 132 ? 5.666   45.613  -0.653  1.00 42.60 ? 131 GLN A N     1 
ATOM   3534 C  CA    . GLN C 2 132 ? 6.027   46.900  -0.059  1.00 45.74 ? 131 GLN A CA    1 
ATOM   3535 C  C     . GLN C 2 132 ? 4.809   47.637  0.480   1.00 47.07 ? 131 GLN A C     1 
ATOM   3536 O  O     . GLN C 2 132 ? 4.854   48.220  1.575   1.00 47.35 ? 131 GLN A O     1 
ATOM   3537 C  CB    . GLN C 2 132 ? 6.711   47.796  -1.078  1.00 48.06 ? 131 GLN A CB    1 
ATOM   3538 C  CG    . GLN C 2 132 ? 8.221   47.786  -1.064  1.00 48.47 ? 131 GLN A CG    1 
ATOM   3539 C  CD    . GLN C 2 132 ? 8.771   48.294  -2.402  1.00 48.41 ? 131 GLN A CD    1 
ATOM   3540 O  OE1   . GLN C 2 132 ? 8.006   48.689  -3.294  1.00 50.80 ? 131 GLN A OE1   1 
ATOM   3541 N  NE2   . GLN C 2 132 ? 10.091  48.350  -2.516  1.00 51.11 ? 131 GLN A NE2   1 
ATOM   3542 N  N     . ASP C 2 133 ? 3.741   47.710  -0.321  1.00 48.37 ? 132 ASP A N     1 
ATOM   3543 C  CA    . ASP C 2 133 ? 2.523   48.350  0.163   1.00 48.51 ? 132 ASP A CA    1 
ATOM   3544 C  C     . ASP C 2 133 ? 2.067   47.679  1.452   1.00 46.20 ? 132 ASP A C     1 
ATOM   3545 O  O     . ASP C 2 133 ? 1.711   48.358  2.428   1.00 47.07 ? 132 ASP A O     1 
ATOM   3546 C  CB    . ASP C 2 133 ? 1.417   48.301  -0.899  1.00 49.46 ? 132 ASP A CB    1 
ATOM   3547 C  CG    . ASP C 2 133 ? 1.778   49.070  -2.176  1.00 54.81 ? 132 ASP A CG    1 
ATOM   3548 O  OD1   . ASP C 2 133 ? 2.711   49.909  -2.157  1.00 56.40 ? 132 ASP A OD1   1 
ATOM   3549 O  OD2   . ASP C 2 133 ? 1.154   48.802  -3.224  1.00 56.05 ? 132 ASP A OD2   1 
ATOM   3550 N  N     . LEU C 2 134 ? 2.125   46.346  1.494   1.00 45.98 ? 133 LEU A N     1 
ATOM   3551 C  CA    . LEU C 2 134 ? 1.684   45.625  2.684   1.00 43.16 ? 133 LEU A CA    1 
ATOM   3552 C  C     . LEU C 2 134 ? 2.543   45.960  3.893   1.00 46.17 ? 133 LEU A C     1 
ATOM   3553 O  O     . LEU C 2 134 ? 2.027   46.188  4.995   1.00 44.63 ? 133 LEU A O     1 
ATOM   3554 C  CB    . LEU C 2 134 ? 1.712   44.117  2.454   1.00 42.99 ? 133 LEU A CB    1 
ATOM   3555 C  CG    . LEU C 2 134 ? 1.152   43.424  3.706   1.00 42.50 ? 133 LEU A CG    1 
ATOM   3556 C  CD1   . LEU C 2 134 ? -0.354  43.687  3.786   1.00 42.58 ? 133 LEU A CD1   1 
ATOM   3557 C  CD2   . LEU C 2 134 ? 1.484   41.943  3.802   1.00 40.36 ? 133 LEU A CD2   1 
ATOM   3558 N  N     . ALA C 2 135 ? 3.869   45.901  3.724   1.00 46.29 ? 134 ALA A N     1 
ATOM   3559 C  CA    . ALA C 2 135 ? 4.777   46.289  4.795   1.00 43.80 ? 134 ALA A CA    1 
ATOM   3560 C  C     . ALA C 2 135 ? 4.511   47.710  5.254   1.00 43.94 ? 134 ALA A C     1 
ATOM   3561 O  O     . ALA C 2 135 ? 4.552   48.001  6.455   1.00 44.04 ? 134 ALA A O     1 
ATOM   3562 C  CB    . ALA C 2 135 ? 6.223   46.157  4.329   1.00 40.22 ? 134 ALA A CB    1 
ATOM   3563 N  N     . ARG C 2 136 ? 4.283   48.616  4.310   1.00 45.15 ? 135 ARG A N     1 
ATOM   3564 C  CA    . ARG C 2 136 ? 3.989   49.991  4.684   1.00 46.87 ? 135 ARG A CA    1 
ATOM   3565 C  C     . ARG C 2 136 ? 2.751   50.060  5.568   1.00 46.72 ? 135 ARG A C     1 
ATOM   3566 O  O     . ARG C 2 136 ? 2.734   50.791  6.566   1.00 51.54 ? 135 ARG A O     1 
ATOM   3567 C  CB    . ARG C 2 136 ? 3.833   50.848  3.424   1.00 50.70 ? 135 ARG A CB    1 
ATOM   3568 C  CG    . ARG C 2 136 ? 3.663   52.347  3.684   1.00 58.11 ? 135 ARG A CG    1 
ATOM   3569 C  CD    . ARG C 2 136 ? 3.588   53.171  2.373   1.00 64.10 ? 135 ARG A CD    1 
ATOM   3570 N  NE    . ARG C 2 136 ? 4.715   52.880  1.482   1.00 66.62 ? 135 ARG A NE    1 
ATOM   3571 C  CZ    . ARG C 2 136 ? 4.651   52.074  0.424   1.00 65.09 ? 135 ARG A CZ    1 
ATOM   3572 N  NH1   . ARG C 2 136 ? 3.500   51.539  0.025   1.00 61.05 ? 135 ARG A NH1   1 
ATOM   3573 N  NH2   . ARG C 2 136 ? 5.765   51.795  -0.253  1.00 62.04 ? 135 ARG A NH2   1 
ATOM   3574 N  N     . SER C 2 137 ? 1.713   49.281  5.243   1.00 45.52 ? 136 SER A N     1 
ATOM   3575 C  CA    . SER C 2 137 ? 0.461   49.378  5.994   1.00 48.34 ? 136 SER A CA    1 
ATOM   3576 C  C     . SER C 2 137 ? 0.600   48.773  7.378   1.00 46.83 ? 136 SER A C     1 
ATOM   3577 O  O     . SER C 2 137 ? -0.159  49.126  8.284   1.00 51.74 ? 136 SER A O     1 
ATOM   3578 C  CB    . SER C 2 137 ? -0.689  48.685  5.246   1.00 47.59 ? 136 SER A CB    1 
ATOM   3579 O  OG    . SER C 2 137 ? -0.605  47.263  5.351   1.00 48.27 ? 136 SER A OG    1 
ATOM   3580 N  N     . TYR C 2 138 ? 1.544   47.853  7.546   1.00 46.56 ? 137 TYR A N     1 
ATOM   3581 C  CA    . TYR C 2 138 ? 1.879   47.304  8.848   1.00 43.73 ? 137 TYR A CA    1 
ATOM   3582 C  C     . TYR C 2 138 ? 2.799   48.217  9.645   1.00 45.90 ? 137 TYR A C     1 
ATOM   3583 O  O     . TYR C 2 138 ? 2.922   48.049  10.866  1.00 46.38 ? 137 TYR A O     1 
ATOM   3584 C  CB    . TYR C 2 138 ? 2.593   45.968  8.680   1.00 43.83 ? 137 TYR A CB    1 
ATOM   3585 C  CG    . TYR C 2 138 ? 1.756   44.830  8.141   1.00 43.67 ? 137 TYR A CG    1 
ATOM   3586 C  CD1   . TYR C 2 138 ? 0.364   44.924  8.007   1.00 44.12 ? 137 TYR A CD1   1 
ATOM   3587 C  CD2   . TYR C 2 138 ? 2.357   43.628  7.827   1.00 43.02 ? 137 TYR A CD2   1 
ATOM   3588 C  CE1   . TYR C 2 138 ? -0.375  43.845  7.523   1.00 42.73 ? 137 TYR A CE1   1 
ATOM   3589 C  CE2   . TYR C 2 138 ? 1.640   42.562  7.353   1.00 41.86 ? 137 TYR A CE2   1 
ATOM   3590 C  CZ    . TYR C 2 138 ? 0.290   42.664  7.182   1.00 43.00 ? 137 TYR A CZ    1 
ATOM   3591 O  OH    . TYR C 2 138 ? -0.371  41.554  6.709   1.00 42.78 ? 137 TYR A OH    1 
ATOM   3592 N  N     . GLY C 2 139 ? 3.497   49.132  8.977   1.00 43.89 ? 138 GLY A N     1 
ATOM   3593 C  CA    . GLY C 2 139 ? 4.520   49.919  9.649   1.00 43.94 ? 138 GLY A CA    1 
ATOM   3594 C  C     . GLY C 2 139 ? 5.804   49.167  9.950   1.00 40.60 ? 138 GLY A C     1 
ATOM   3595 O  O     . GLY C 2 139 ? 6.452   49.446  10.964  1.00 41.10 ? 138 GLY A O     1 
ATOM   3596 N  N     . ILE C 2 140 ? 6.193   48.233  9.089   1.00 38.63 ? 139 ILE A N     1 
ATOM   3597 C  CA    . ILE C 2 140 ? 7.407   47.436  9.271   1.00 40.41 ? 139 ILE A CA    1 
ATOM   3598 C  C     . ILE C 2 140 ? 8.242   47.487  7.998   1.00 36.77 ? 139 ILE A C     1 
ATOM   3599 O  O     . ILE C 2 140 ? 7.719   47.763  6.905   1.00 36.60 ? 139 ILE A O     1 
ATOM   3600 C  CB    . ILE C 2 140 ? 7.080   45.971  9.663   1.00 38.54 ? 139 ILE A CB    1 
ATOM   3601 C  CG1   . ILE C 2 140 ? 6.485   45.168  8.495   1.00 35.38 ? 139 ILE A CG1   1 
ATOM   3602 C  CG2   . ILE C 2 140 ? 6.280   45.895  11.016  1.00 39.14 ? 139 ILE A CG2   1 
ATOM   3603 C  CD1   . ILE C 2 140 ? 6.056   43.769  8.904   1.00 33.84 ? 139 ILE A CD1   1 
ATOM   3604 N  N     . PRO C 2 141 ? 9.550   47.230  8.112   1.00 35.78 ? 140 PRO A N     1 
ATOM   3605 C  CA    . PRO C 2 141 ? 10.408  47.142  6.917   1.00 34.96 ? 140 PRO A CA    1 
ATOM   3606 C  C     . PRO C 2 141 ? 10.134  45.886  6.097   1.00 35.21 ? 140 PRO A C     1 
ATOM   3607 O  O     . PRO C 2 141 ? 9.657   44.865  6.600   1.00 33.14 ? 140 PRO A O     1 
ATOM   3608 C  CB    . PRO C 2 141 ? 11.832  47.101  7.497   1.00 31.54 ? 140 PRO A CB    1 
ATOM   3609 C  CG    . PRO C 2 141 ? 11.718  47.439  8.953   1.00 34.54 ? 140 PRO A CG    1 
ATOM   3610 C  CD    . PRO C 2 141 ? 10.327  47.066  9.353   1.00 36.69 ? 140 PRO A CD    1 
ATOM   3611 N  N     . PHE C 2 142 ? 10.516  45.952  4.824   1.00 35.41 ? 141 PHE A N     1 
ATOM   3612 C  CA    . PHE C 2 142 ? 10.391  44.830  3.901   1.00 31.31 ? 141 PHE A CA    1 
ATOM   3613 C  C     . PHE C 2 142 ? 11.735  44.630  3.226   1.00 31.30 ? 141 PHE A C     1 
ATOM   3614 O  O     . PHE C 2 142 ? 12.359  45.587  2.747   1.00 33.88 ? 141 PHE A O     1 
ATOM   3615 C  CB    . PHE C 2 142 ? 9.281   45.064  2.840   1.00 34.11 ? 141 PHE A CB    1 
ATOM   3616 C  CG    . PHE C 2 142 ? 9.299   44.059  1.697   1.00 34.75 ? 141 PHE A CG    1 
ATOM   3617 C  CD1   . PHE C 2 142 ? 9.179   42.697  1.954   1.00 31.78 ? 141 PHE A CD1   1 
ATOM   3618 C  CD2   . PHE C 2 142 ? 9.427   44.485  0.364   1.00 37.71 ? 141 PHE A CD2   1 
ATOM   3619 C  CE1   . PHE C 2 142 ? 9.207   41.766  0.910   1.00 32.02 ? 141 PHE A CE1   1 
ATOM   3620 C  CE2   . PHE C 2 142 ? 9.452   43.577  -0.684  1.00 36.52 ? 141 PHE A CE2   1 
ATOM   3621 C  CZ    . PHE C 2 142 ? 9.350   42.197  -0.412  1.00 33.24 ? 141 PHE A CZ    1 
ATOM   3622 N  N     . ILE C 2 143 ? 12.146  43.385  3.148   1.00 30.21 ? 142 ILE A N     1 
ATOM   3623 C  CA    . ILE C 2 143 ? 13.423  42.976  2.572   1.00 30.85 ? 142 ILE A CA    1 
ATOM   3624 C  C     . ILE C 2 143 ? 13.218  41.739  1.725   1.00 30.31 ? 142 ILE A C     1 
ATOM   3625 O  O     . ILE C 2 143 ? 12.680  40.740  2.207   1.00 27.89 ? 142 ILE A O     1 
ATOM   3626 C  CB    . ILE C 2 143 ? 14.485  42.730  3.676   1.00 30.88 ? 142 ILE A CB    1 
ATOM   3627 C  CG1   . ILE C 2 143 ? 14.400  43.839  4.750   1.00 35.46 ? 142 ILE A CG1   1 
ATOM   3628 C  CG2   . ILE C 2 143 ? 15.840  42.323  3.117   1.00 29.78 ? 142 ILE A CG2   1 
ATOM   3629 C  CD1   . ILE C 2 143 ? 15.593  44.002  5.698   1.00 37.05 ? 142 ILE A CD1   1 
ATOM   3630 N  N     . GLU C 2 144 ? 13.684  41.794  0.472   1.00 30.60 ? 143 GLU A N     1 
ATOM   3631 C  CA    . GLU C 2 144 ? 13.703  40.608  -0.369  1.00 29.36 ? 143 GLU A CA    1 
ATOM   3632 C  C     . GLU C 2 144 ? 15.010  39.887  -0.169  1.00 27.11 ? 143 GLU A C     1 
ATOM   3633 O  O     . GLU C 2 144 ? 16.063  40.509  -0.061  1.00 27.37 ? 143 GLU A O     1 
ATOM   3634 C  CB    . GLU C 2 144 ? 13.533  40.953  -1.851  1.00 31.26 ? 143 GLU A CB    1 
ATOM   3635 C  CG    . GLU C 2 144 ? 12.089  41.205  -2.147  1.00 33.90 ? 143 GLU A CG    1 
ATOM   3636 C  CD    . GLU C 2 144 ? 11.838  41.467  -3.635  1.00 43.52 ? 143 GLU A CD    1 
ATOM   3637 O  OE1   . GLU C 2 144 ? 12.827  41.703  -4.379  1.00 48.11 ? 143 GLU A OE1   1 
ATOM   3638 O  OE2   . GLU C 2 144 ? 10.657  41.453  -4.058  1.00 49.30 ? 143 GLU A OE2   1 
ATOM   3639 N  N     . THR C 2 145 ? 14.929  38.579  -0.082  1.00 24.80 ? 144 THR A N     1 
ATOM   3640 C  CA    . THR C 2 145 ? 16.099  37.764  0.197   1.00 23.43 ? 144 THR A CA    1 
ATOM   3641 C  C     . THR C 2 145 ? 16.209  36.597  -0.754  1.00 24.46 ? 144 THR A C     1 
ATOM   3642 O  O     . THR C 2 145 ? 15.253  36.191  -1.392  1.00 23.51 ? 144 THR A O     1 
ATOM   3643 C  CB    . THR C 2 145 ? 16.065  37.202  1.626   1.00 24.92 ? 144 THR A CB    1 
ATOM   3644 O  OG1   . THR C 2 145 ? 14.913  36.321  1.766   1.00 20.91 ? 144 THR A OG1   1 
ATOM   3645 C  CG2   . THR C 2 145 ? 15.984  38.368  2.645   1.00 22.67 ? 144 THR A CG2   1 
ATOM   3646 N  N     . SER C 2 146 ? 17.397  35.990  -0.758  1.00 23.70 ? 145 SER A N     1 
ATOM   3647 C  CA    . SER C 2 146 ? 17.561  34.662  -1.335  1.00 23.87 ? 145 SER A CA    1 
ATOM   3648 C  C     . SER C 2 146 ? 18.489  33.892  -0.411  1.00 26.13 ? 145 SER A C     1 
ATOM   3649 O  O     . SER C 2 146 ? 19.655  34.278  -0.228  1.00 24.69 ? 145 SER A O     1 
ATOM   3650 C  CB    . SER C 2 146 ? 18.119  34.735  -2.763  1.00 22.59 ? 145 SER A CB    1 
ATOM   3651 O  OG    . SER C 2 146 ? 18.576  33.469  -3.203  1.00 25.80 ? 145 SER A OG    1 
ATOM   3652 N  N     . ALA C 2 147 ? 17.955  32.838  0.208   1.00 23.68 ? 146 ALA A N     1 
ATOM   3653 C  CA    . ALA C 2 147 ? 18.835  31.977  0.986   1.00 24.11 ? 146 ALA A CA    1 
ATOM   3654 C  C     . ALA C 2 147 ? 19.869  31.261  0.099   1.00 23.84 ? 146 ALA A C     1 
ATOM   3655 O  O     . ALA C 2 147 ? 20.925  30.821  0.599   1.00 21.80 ? 146 ALA A O     1 
ATOM   3656 C  CB    . ALA C 2 147 ? 17.970  30.986  1.771   1.00 22.96 ? 146 ALA A CB    1 
ATOM   3657 N  N     . LYS C 2 148 ? 19.567  31.112  -1.184  1.00 22.23 ? 147 LYS A N     1 
ATOM   3658 C  CA    . LYS C 2 148 ? 20.485  30.448  -2.114  1.00 24.90 ? 147 LYS A CA    1 
ATOM   3659 C  C     . LYS C 2 148 ? 21.675  31.334  -2.472  1.00 26.85 ? 147 LYS A C     1 
ATOM   3660 O  O     . LYS C 2 148 ? 22.829  30.859  -2.480  1.00 25.61 ? 147 LYS A O     1 
ATOM   3661 C  CB    . LYS C 2 148 ? 19.748  30.056  -3.392  1.00 25.12 ? 147 LYS A CB    1 
ATOM   3662 C  CG    . LYS C 2 148 ? 20.610  29.302  -4.399  1.00 29.84 ? 147 LYS A CG    1 
ATOM   3663 C  CD    . LYS C 2 148 ? 19.717  28.594  -5.370  1.00 29.96 ? 147 LYS A CD    1 
ATOM   3664 C  CE    . LYS C 2 148 ? 20.564  27.880  -6.377  1.00 33.72 ? 147 LYS A CE    1 
ATOM   3665 N  NZ    . LYS C 2 148 ? 19.591  27.324  -7.321  1.00 42.48 ? 147 LYS A NZ    1 
ATOM   3666 N  N     . THR C 2 149 ? 21.416  32.600  -2.852  1.00 25.42 ? 148 THR A N     1 
ATOM   3667 C  CA    . THR C 2 149 ? 22.521  33.486  -3.204  1.00 24.67 ? 148 THR A CA    1 
ATOM   3668 C  C     . THR C 2 149 ? 23.056  34.292  -2.029  1.00 23.54 ? 148 THR A C     1 
ATOM   3669 O  O     . THR C 2 149 ? 24.100  34.943  -2.184  1.00 24.42 ? 148 THR A O     1 
ATOM   3670 C  CB    . THR C 2 149 ? 22.123  34.492  -4.293  1.00 25.67 ? 148 THR A CB    1 
ATOM   3671 O  OG1   . THR C 2 149 ? 21.205  35.424  -3.681  1.00 23.88 ? 148 THR A OG1   1 
ATOM   3672 C  CG2   . THR C 2 149 ? 21.531  33.801  -5.511  1.00 24.88 ? 148 THR A CG2   1 
ATOM   3673 N  N     . ARG C 2 150 ? 22.377  34.269  -0.868  1.00 20.43 ? 149 ARG A N     1 
ATOM   3674 C  CA    . ARG C 2 150 ? 22.640  35.055  0.345   1.00 23.61 ? 149 ARG A CA    1 
ATOM   3675 C  C     . ARG C 2 150 ? 22.158  36.508  0.224   1.00 22.80 ? 149 ARG A C     1 
ATOM   3676 O  O     . ARG C 2 150 ? 22.355  37.255  1.175   1.00 24.32 ? 149 ARG A O     1 
ATOM   3677 C  CB    . ARG C 2 150 ? 24.121  35.070  0.803   1.00 23.19 ? 149 ARG A CB    1 
ATOM   3678 C  CG    . ARG C 2 150 ? 24.807  33.700  0.750   1.00 23.87 ? 149 ARG A CG    1 
ATOM   3679 C  CD    . ARG C 2 150 ? 26.192  33.718  1.472   1.00 26.00 ? 149 ARG A CD    1 
ATOM   3680 N  NE    . ARG C 2 150 ? 25.901  33.420  2.847   1.00 31.42 ? 149 ARG A NE    1 
ATOM   3681 C  CZ    . ARG C 2 150 ? 25.839  34.328  3.802   1.00 30.31 ? 149 ARG A CZ    1 
ATOM   3682 N  NH1   . ARG C 2 150 ? 26.340  35.537  3.639   1.00 32.20 ? 149 ARG A NH1   1 
ATOM   3683 N  NH2   . ARG C 2 150 ? 25.241  34.021  4.925   1.00 27.52 ? 149 ARG A NH2   1 
ATOM   3684 N  N     . GLN C 2 151 ? 21.573  36.931  -0.896  1.00 21.71 ? 150 GLN A N     1 
ATOM   3685 C  CA    . GLN C 2 151 ? 21.079  38.289  -1.007  1.00 20.81 ? 150 GLN A CA    1 
ATOM   3686 C  C     . GLN C 2 151 ? 20.162  38.584  0.170   1.00 23.84 ? 150 GLN A C     1 
ATOM   3687 O  O     . GLN C 2 151 ? 19.242  37.812  0.452   1.00 23.69 ? 150 GLN A O     1 
ATOM   3688 C  CB    . GLN C 2 151 ? 20.325  38.457  -2.310  1.00 24.29 ? 150 GLN A CB    1 
ATOM   3689 C  CG    . GLN C 2 151 ? 19.694  39.832  -2.443  1.00 29.60 ? 150 GLN A CG    1 
ATOM   3690 C  CD    . GLN C 2 151 ? 19.035  40.028  -3.781  1.00 32.20 ? 150 GLN A CD    1 
ATOM   3691 O  OE1   . GLN C 2 151 ? 19.391  39.379  -4.788  1.00 31.79 ? 150 GLN A OE1   1 
ATOM   3692 N  NE2   . GLN C 2 151 ? 18.042  40.926  -3.812  1.00 41.07 ? 150 GLN A NE2   1 
ATOM   3693 N  N     . GLY C 2 152 ? 20.475  39.663  0.882   1.00 25.45 ? 151 GLY A N     1 
ATOM   3694 C  CA    . GLY C 2 152 ? 19.653  40.233  1.933   1.00 23.92 ? 151 GLY A CA    1 
ATOM   3695 C  C     . GLY C 2 152 ? 19.613  39.472  3.242   1.00 26.01 ? 151 GLY A C     1 
ATOM   3696 O  O     . GLY C 2 152 ? 18.848  39.889  4.140   1.00 23.99 ? 151 GLY A O     1 
ATOM   3697 N  N     . VAL C 2 153 ? 20.370  38.363  3.375   1.00 22.74 ? 152 VAL A N     1 
ATOM   3698 C  CA    . VAL C 2 153 ? 20.220  37.501  4.551   1.00 20.30 ? 152 VAL A CA    1 
ATOM   3699 C  C     . VAL C 2 153 ? 20.646  38.261  5.809   1.00 24.32 ? 152 VAL A C     1 
ATOM   3700 O  O     . VAL C 2 153 ? 19.886  38.349  6.792   1.00 22.77 ? 152 VAL A O     1 
ATOM   3701 C  CB    . VAL C 2 153 ? 21.016  36.180  4.390   1.00 20.37 ? 152 VAL A CB    1 
ATOM   3702 C  CG1   . VAL C 2 153 ? 21.079  35.379  5.738   1.00 21.50 ? 152 VAL A CG1   1 
ATOM   3703 C  CG2   . VAL C 2 153 ? 20.427  35.269  3.264   1.00 22.32 ? 152 VAL A CG2   1 
ATOM   3704 N  N     . ASP C 2 154 ? 21.850  38.868  5.784   1.00 24.59 ? 153 ASP A N     1 
ATOM   3705 C  CA    . ASP C 2 154 ? 22.270  39.676  6.929   1.00 23.59 ? 153 ASP A CA    1 
ATOM   3706 C  C     . ASP C 2 154 ? 21.336  40.868  7.123   1.00 27.28 ? 153 ASP A C     1 
ATOM   3707 O  O     . ASP C 2 154 ? 20.904  41.159  8.256   1.00 28.30 ? 153 ASP A O     1 
ATOM   3708 C  CB    . ASP C 2 154 ? 23.734  40.156  6.762   1.00 27.73 ? 153 ASP A CB    1 
ATOM   3709 C  CG    . ASP C 2 154 ? 24.752  39.069  7.070   1.00 27.45 ? 153 ASP A CG    1 
ATOM   3710 O  OD1   . ASP C 2 154 ? 24.404  38.067  7.653   1.00 25.77 ? 153 ASP A OD1   1 
ATOM   3711 O  OD2   . ASP C 2 154 ? 25.951  39.211  6.746   1.00 27.53 ? 153 ASP A OD2   1 
ATOM   3712 N  N     . ASP C 2 155 ? 20.972  41.543  6.027   1.00 24.28 ? 154 ASP A N     1 
ATOM   3713 C  CA    . ASP C 2 155 ? 20.125  42.722  6.113   1.00 27.50 ? 154 ASP A CA    1 
ATOM   3714 C  C     . ASP C 2 155 ? 18.830  42.386  6.833   1.00 25.96 ? 154 ASP A C     1 
ATOM   3715 O  O     . ASP C 2 155 ? 18.362  43.160  7.678   1.00 28.95 ? 154 ASP A O     1 
ATOM   3716 C  CB    . ASP C 2 155 ? 19.883  43.285  4.704   1.00 30.72 ? 154 ASP A CB    1 
ATOM   3717 C  CG    . ASP C 2 155 ? 19.180  44.653  4.702   1.00 37.02 ? 154 ASP A CG    1 
ATOM   3718 O  OD1   . ASP C 2 155 ? 19.171  45.355  5.752   1.00 38.90 ? 154 ASP A OD1   1 
ATOM   3719 O  OD2   . ASP C 2 155 ? 18.663  45.038  3.613   1.00 38.18 ? 154 ASP A OD2   1 
ATOM   3720 N  N     . ALA C 2 156 ? 18.260  41.213  6.558   1.00 23.77 ? 155 ALA A N     1 
ATOM   3721 C  CA    . ALA C 2 156 ? 16.979  40.878  7.172   1.00 26.01 ? 155 ALA A CA    1 
ATOM   3722 C  C     . ALA C 2 156 ? 17.127  40.708  8.681   1.00 24.69 ? 155 ALA A C     1 
ATOM   3723 O  O     . ALA C 2 156 ? 16.346  41.275  9.446   1.00 25.04 ? 155 ALA A O     1 
ATOM   3724 C  CB    . ALA C 2 156 ? 16.395  39.602  6.537   1.00 23.74 ? 155 ALA A CB    1 
ATOM   3725 N  N     . PHE C 2 157 ? 18.115  39.919  9.127   1.00 24.35 ? 156 PHE A N     1 
ATOM   3726 C  CA    . PHE C 2 157 ? 18.285  39.690  10.564  1.00 24.15 ? 156 PHE A CA    1 
ATOM   3727 C  C     . PHE C 2 157 ? 18.816  40.934  11.266  1.00 26.00 ? 156 PHE A C     1 
ATOM   3728 O  O     . PHE C 2 157 ? 18.370  41.254  12.372  1.00 25.01 ? 156 PHE A O     1 
ATOM   3729 C  CB    . PHE C 2 157 ? 19.212  38.489  10.801  1.00 22.01 ? 156 PHE A CB    1 
ATOM   3730 C  CG    . PHE C 2 157 ? 18.587  37.158  10.474  1.00 20.83 ? 156 PHE A CG    1 
ATOM   3731 C  CD1   . PHE C 2 157 ? 17.790  36.497  11.431  1.00 19.12 ? 156 PHE A CD1   1 
ATOM   3732 C  CD2   . PHE C 2 157 ? 18.794  36.550  9.220   1.00 20.87 ? 156 PHE A CD2   1 
ATOM   3733 C  CE1   . PHE C 2 157 ? 17.216  35.221  11.137  1.00 18.79 ? 156 PHE A CE1   1 
ATOM   3734 C  CE2   . PHE C 2 157 ? 18.218  35.266  8.932   1.00 20.13 ? 156 PHE A CE2   1 
ATOM   3735 C  CZ    . PHE C 2 157 ? 17.427  34.617  9.932   1.00 17.55 ? 156 PHE A CZ    1 
ATOM   3736 N  N     . TYR C 2 158 ? 19.700  41.708  10.620  1.00 24.83 ? 157 TYR A N     1 
ATOM   3737 C  CA    . TYR C 2 158 ? 20.192  42.924  11.282  1.00 27.65 ? 157 TYR A CA    1 
ATOM   3738 C  C     . TYR C 2 158 ? 19.087  43.984  11.399  1.00 27.81 ? 157 TYR A C     1 
ATOM   3739 O  O     . TYR C 2 158 ? 19.023  44.722  12.387  1.00 27.74 ? 157 TYR A O     1 
ATOM   3740 C  CB    . TYR C 2 158 ? 21.402  43.498  10.510  1.00 27.64 ? 157 TYR A CB    1 
ATOM   3741 C  CG    . TYR C 2 158 ? 22.678  42.666  10.573  1.00 27.93 ? 157 TYR A CG    1 
ATOM   3742 C  CD1   . TYR C 2 158 ? 22.686  41.388  11.088  1.00 27.55 ? 157 TYR A CD1   1 
ATOM   3743 C  CD2   . TYR C 2 158 ? 23.888  43.173  10.058  1.00 28.57 ? 157 TYR A CD2   1 
ATOM   3744 C  CE1   . TYR C 2 158 ? 23.829  40.618  11.122  1.00 30.06 ? 157 TYR A CE1   1 
ATOM   3745 C  CE2   . TYR C 2 158 ? 25.042  42.409  10.076  1.00 31.91 ? 157 TYR A CE2   1 
ATOM   3746 C  CZ    . TYR C 2 158 ? 25.013  41.125  10.628  1.00 31.21 ? 157 TYR A CZ    1 
ATOM   3747 O  OH    . TYR C 2 158 ? 26.161  40.351  10.653  1.00 34.77 ? 157 TYR A OH    1 
ATOM   3748 N  N     . THR C 2 159 ? 18.203  44.064  10.402  1.00 25.44 ? 158 THR A N     1 
ATOM   3749 C  CA    . THR C 2 159 ? 17.139  45.055  10.420  1.00 28.54 ? 158 THR A CA    1 
ATOM   3750 C  C     . THR C 2 159 ? 16.128  44.715  11.508  1.00 29.06 ? 158 THR A C     1 
ATOM   3751 O  O     . THR C 2 159 ? 15.547  45.604  12.143  1.00 32.33 ? 158 THR A O     1 
ATOM   3752 C  CB    . THR C 2 159 ? 16.460  45.104  9.043   1.00 31.35 ? 158 THR A CB    1 
ATOM   3753 O  OG1   . THR C 2 159 ? 17.391  45.632  8.072   1.00 29.68 ? 158 THR A OG1   1 
ATOM   3754 C  CG2   . THR C 2 159 ? 15.178  45.974  9.066   1.00 31.59 ? 158 THR A CG2   1 
ATOM   3755 N  N     . LEU C 2 160 ? 15.905  43.437  11.735  1.00 24.86 ? 159 LEU A N     1 
ATOM   3756 C  CA    . LEU C 2 160 ? 15.011  43.061  12.829  1.00 26.89 ? 159 LEU A CA    1 
ATOM   3757 C  C     . LEU C 2 160 ? 15.629  43.419  14.192  1.00 30.30 ? 159 LEU A C     1 
ATOM   3758 O  O     . LEU C 2 160 ? 14.937  43.958  15.086  1.00 30.82 ? 159 LEU A O     1 
ATOM   3759 C  CB    . LEU C 2 160 ? 14.688  41.567  12.719  1.00 22.94 ? 159 LEU A CB    1 
ATOM   3760 C  CG    . LEU C 2 160 ? 13.783  40.987  13.863  1.00 22.33 ? 159 LEU A CG    1 
ATOM   3761 C  CD1   . LEU C 2 160 ? 12.418  41.756  13.920  1.00 24.59 ? 159 LEU A CD1   1 
ATOM   3762 C  CD2   . LEU C 2 160 ? 13.615  39.465  13.735  1.00 24.63 ? 159 LEU A CD2   1 
ATOM   3763 N  N     . VAL C 2 161 ? 16.941  43.171  14.362  1.00 29.35 ? 160 VAL A N     1 
ATOM   3764 C  CA    . VAL C 2 161 ? 17.606  43.663  15.571  1.00 31.39 ? 160 VAL A CA    1 
ATOM   3765 C  C     . VAL C 2 161 ? 17.418  45.162  15.697  1.00 34.50 ? 160 VAL A C     1 
ATOM   3766 O  O     . VAL C 2 161 ? 17.061  45.660  16.771  1.00 33.60 ? 160 VAL A O     1 
ATOM   3767 C  CB    . VAL C 2 161 ? 19.093  43.276  15.596  1.00 29.87 ? 160 VAL A CB    1 
ATOM   3768 C  CG1   . VAL C 2 161 ? 19.859  44.037  16.737  1.00 31.72 ? 160 VAL A CG1   1 
ATOM   3769 C  CG2   . VAL C 2 161 ? 19.194  41.790  15.714  1.00 27.23 ? 160 VAL A CG2   1 
ATOM   3770 N  N     . ARG C 2 162 ? 17.582  45.904  14.594  1.00 32.16 ? 161 ARG A N     1 
ATOM   3771 C  CA    . ARG C 2 162 ? 17.375  47.363  14.689  1.00 36.82 ? 161 ARG A CA    1 
ATOM   3772 C  C     . ARG C 2 162 ? 15.935  47.712  15.071  1.00 37.80 ? 161 ARG A C     1 
ATOM   3773 O  O     . ARG C 2 162 ? 15.695  48.703  15.785  1.00 40.61 ? 161 ARG A O     1 
ATOM   3774 C  CB    . ARG C 2 162 ? 17.783  48.045  13.361  1.00 32.23 ? 161 ARG A CB    1 
ATOM   3775 C  CG    . ARG C 2 162 ? 19.299  48.057  13.132  1.00 35.31 ? 161 ARG A CG    1 
ATOM   3776 C  CD    . ARG C 2 162 ? 19.704  48.874  11.881  1.00 38.56 ? 161 ARG A CD    1 
ATOM   3777 N  NE    . ARG C 2 162 ? 21.120  48.693  11.551  1.00 38.92 ? 161 ARG A NE    1 
ATOM   3778 C  CZ    . ARG C 2 162 ? 21.547  47.895  10.581  1.00 38.75 ? 161 ARG A CZ    1 
ATOM   3779 N  NH1   . ARG C 2 162 ? 20.702  47.233  9.802   1.00 38.48 ? 161 ARG A NH1   1 
ATOM   3780 N  NH2   . ARG C 2 162 ? 22.851  47.768  10.369  1.00 41.15 ? 161 ARG A NH2   1 
ATOM   3781 N  N     . GLU C 2 163 ? 14.954  46.902  14.645  1.00 33.86 ? 162 GLU A N     1 
ATOM   3782 C  CA    . GLU C 2 163 ? 13.580  47.171  15.058  1.00 39.65 ? 162 GLU A CA    1 
ATOM   3783 C  C     . GLU C 2 163 ? 13.393  46.889  16.547  1.00 39.78 ? 162 GLU A C     1 
ATOM   3784 O  O     . GLU C 2 163 ? 12.686  47.634  17.252  1.00 41.61 ? 162 GLU A O     1 
ATOM   3785 C  CB    . GLU C 2 163 ? 12.606  46.341  14.215  1.00 38.37 ? 162 GLU A CB    1 
ATOM   3786 C  CG    . GLU C 2 163 ? 12.549  46.724  12.724  1.00 34.32 ? 162 GLU A CG    1 
ATOM   3787 C  CD    . GLU C 2 163 ? 11.955  48.106  12.451  1.00 40.83 ? 162 GLU A CD    1 
ATOM   3788 O  OE1   . GLU C 2 163 ? 10.734  48.346  12.645  1.00 40.08 ? 162 GLU A OE1   1 
ATOM   3789 O  OE2   . GLU C 2 163 ? 12.750  48.967  12.055  1.00 41.08 ? 162 GLU A OE2   1 
ATOM   3790 N  N     . ILE C 2 164 ? 14.050  45.848  17.064  1.00 38.31 ? 163 ILE A N     1 
ATOM   3791 C  CA    . ILE C 2 164 ? 13.910  45.563  18.491  1.00 36.87 ? 163 ILE A CA    1 
ATOM   3792 C  C     . ILE C 2 164 ? 14.487  46.707  19.328  1.00 43.50 ? 163 ILE A C     1 
ATOM   3793 O  O     . ILE C 2 164 ? 13.867  47.146  20.303  1.00 46.65 ? 163 ILE A O     1 
ATOM   3794 C  CB    . ILE C 2 164 ? 14.551  44.216  18.841  1.00 35.82 ? 163 ILE A CB    1 
ATOM   3795 C  CG1   . ILE C 2 164 ? 13.781  43.101  18.123  1.00 32.34 ? 163 ILE A CG1   1 
ATOM   3796 C  CG2   . ILE C 2 164 ? 14.494  44.006  20.369  1.00 34.62 ? 163 ILE A CG2   1 
ATOM   3797 C  CD1   . ILE C 2 164 ? 14.440  41.707  18.211  1.00 27.64 ? 163 ILE A CD1   1 
ATOM   3798 N  N     . ARG C 2 165 ? 15.667  47.221  18.948  1.00 39.57 ? 164 ARG A N     1 
ATOM   3799 C  CA    . ARG C 2 165 ? 16.248  48.355  19.669  1.00 45.07 ? 164 ARG A CA    1 
ATOM   3800 C  C     . ARG C 2 165 ? 15.304  49.550  19.661  1.00 49.54 ? 164 ARG A C     1 
ATOM   3801 O  O     . ARG C 2 165 ? 15.057  50.162  20.703  1.00 52.97 ? 164 ARG A O     1 
ATOM   3802 C  CB    . ARG C 2 165 ? 17.586  48.766  19.055  1.00 44.58 ? 164 ARG A CB    1 
ATOM   3803 C  CG    . ARG C 2 165 ? 18.580  47.677  18.937  1.00 40.89 ? 164 ARG A CG    1 
ATOM   3804 C  CD    . ARG C 2 165 ? 19.797  48.115  18.068  1.00 45.61 ? 164 ARG A CD    1 
ATOM   3805 N  NE    . ARG C 2 165 ? 20.988  47.318  18.382  1.00 49.18 ? 164 ARG A NE    1 
ATOM   3806 C  CZ    . ARG C 2 165 ? 22.132  47.324  17.704  1.00 47.50 ? 164 ARG A CZ    1 
ATOM   3807 N  NH1   . ARG C 2 165 ? 22.365  48.196  16.734  1.00 49.68 ? 164 ARG A NH1   1 
ATOM   3808 N  NH2   . ARG C 2 165 ? 23.083  46.454  18.038  1.00 46.98 ? 164 ARG A NH2   1 
ATOM   3809 N  N     . LYS C 2 166 ? 14.769  49.903  18.484  1.00 46.39 ? 165 LYS A N     1 
ATOM   3810 C  CA    . LYS C 2 166 ? 13.822  51.017  18.397  1.00 48.50 ? 165 LYS A CA    1 
ATOM   3811 C  C     . LYS C 2 166 ? 12.640  50.817  19.339  1.00 51.28 ? 165 LYS A C     1 
ATOM   3812 O  O     . LYS C 2 166 ? 12.232  51.748  20.038  1.00 55.58 ? 165 LYS A O     1 
ATOM   3813 C  CB    . LYS C 2 166 ? 13.327  51.180  16.958  1.00 48.70 ? 165 LYS A CB    1 
ATOM   3814 C  CG    . LYS C 2 166 ? 14.336  51.858  16.022  1.00 53.58 ? 165 LYS A CG    1 
ATOM   3815 C  CD    . LYS C 2 166 ? 13.738  52.244  14.660  1.00 56.61 ? 165 LYS A CD    1 
ATOM   3816 C  CE    . LYS C 2 166 ? 12.397  51.561  14.362  1.00 54.54 ? 165 LYS A CE    1 
ATOM   3817 N  NZ    . LYS C 2 166 ? 11.892  51.879  12.968  1.00 57.27 ? 165 LYS A NZ    1 
ATOM   3818 N  N     . HIS C 2 167 ? 12.072  49.607  19.368  1.00 48.36 ? 166 HIS A N     1 
ATOM   3819 C  CA    . HIS C 2 167 ? 10.923  49.345  20.231  1.00 52.17 ? 166 HIS A CA    1 
ATOM   3820 C  C     . HIS C 2 167 ? 11.314  49.455  21.699  1.00 56.44 ? 166 HIS A C     1 
ATOM   3821 O  O     . HIS C 2 167 ? 10.580  50.044  22.501  1.00 60.10 ? 166 HIS A O     1 
ATOM   3822 C  CB    . HIS C 2 167 ? 10.341  47.963  19.915  1.00 46.98 ? 166 HIS A CB    1 
ATOM   3823 C  CG    . HIS C 2 167 ? 9.202   47.556  20.794  1.00 49.94 ? 166 HIS A CG    1 
ATOM   3824 N  ND1   . HIS C 2 167 ? 9.384   47.032  22.055  1.00 53.89 ? 166 HIS A ND1   1 
ATOM   3825 C  CD2   . HIS C 2 167 ? 7.867   47.592  20.591  1.00 49.38 ? 166 HIS A CD2   1 
ATOM   3826 C  CE1   . HIS C 2 167 ? 8.207   46.773  22.596  1.00 54.19 ? 166 HIS A CE1   1 
ATOM   3827 N  NE2   . HIS C 2 167 ? 7.269   47.100  21.727  1.00 51.74 ? 166 HIS A NE2   1 
ATOM   3828 N  N     . LYS C 2 168 ? 12.489  48.930  22.053  1.00 56.84 ? 167 LYS A N     1 
ATOM   3829 C  CA    . LYS C 2 168 ? 13.017  49.022  23.406  1.00 59.25 ? 167 LYS A CA    1 
ATOM   3830 C  C     . LYS C 2 168 ? 13.319  50.465  23.805  1.00 63.84 ? 167 LYS A C     1 
ATOM   3831 O  O     . LYS C 2 168 ? 13.262  50.792  24.999  1.00 65.15 ? 167 LYS A O     1 
ATOM   3832 C  CB    . LYS C 2 168 ? 14.306  48.203  23.500  1.00 58.42 ? 167 LYS A CB    1 
ATOM   3833 C  CG    . LYS C 2 168 ? 14.118  46.708  23.614  1.00 58.69 ? 167 LYS A CG    1 
ATOM   3834 C  CD    . LYS C 2 168 ? 13.112  46.303  24.692  1.00 67.97 ? 167 LYS A CD    1 
ATOM   3835 C  CE    . LYS C 2 168 ? 13.568  45.020  25.396  1.00 73.75 ? 167 LYS A CE    1 
ATOM   3836 N  NZ    . LYS C 2 168 ? 12.912  43.780  24.828  1.00 65.91 ? 167 LYS A NZ    1 
ATOM   3837 N  N     . GLU C 2 169 ? 13.608  51.335  22.829  1.00 63.92 ? 168 GLU A N     1 
ATOM   3838 C  CA    . GLU C 2 169 ? 14.304  52.622  23.054  1.00 66.52 ? 168 GLU A CA    1 
ATOM   3839 C  C     . GLU C 2 169 ? 15.726  52.412  23.593  1.00 70.45 ? 168 GLU A C     1 
ATOM   3840 O  O     . GLU C 2 169 ? 16.677  52.169  22.833  1.00 66.83 ? 168 GLU A O     1 
ATOM   3841 C  CB    . GLU C 2 169 ? 13.527  53.543  24.001  1.00 68.51 ? 168 GLU A CB    1 
ATOM   3842 C  CG    . GLU C 2 169 ? 12.560  54.525  23.335  1.00 70.32 ? 168 GLU A CG    1 
ATOM   3843 C  CD    . GLU C 2 169 ? 11.245  53.900  22.905  1.00 72.39 ? 168 GLU A CD    1 
ATOM   3844 O  OE1   . GLU C 2 169 ? 11.190  52.673  22.688  1.00 69.14 ? 168 GLU A OE1   1 
ATOM   3845 O  OE2   . GLU C 2 169 ? 10.257  54.656  22.790  1.00 77.95 ? 168 GLU A OE2   1 
ATOM   3846 N  N     . GLY D 2 1   ? -4.619  14.048  25.074  1.00 41.67 ? 0   GLY C N     1 
ATOM   3847 C  CA    . GLY D 2 1   ? -3.164  14.124  25.086  1.00 42.26 ? 0   GLY C CA    1 
ATOM   3848 C  C     . GLY D 2 1   ? -2.652  13.873  26.493  1.00 41.75 ? 0   GLY C C     1 
ATOM   3849 O  O     . GLY D 2 1   ? -3.373  14.121  27.440  1.00 42.37 ? 0   GLY C O     1 
ATOM   3850 N  N     . MET D 2 2   ? -1.441  13.350  26.665  1.00 40.26 ? 1   MET C N     1 
ATOM   3851 C  CA    . MET D 2 2   ? -0.971  13.183  28.040  1.00 42.16 ? 1   MET C CA    1 
ATOM   3852 C  C     . MET D 2 2   ? -0.575  14.535  28.617  1.00 41.35 ? 1   MET C C     1 
ATOM   3853 O  O     . MET D 2 2   ? -0.262  15.476  27.888  1.00 40.75 ? 1   MET C O     1 
ATOM   3854 C  CB    . MET D 2 2   ? 0.192   12.176  28.137  1.00 44.70 ? 1   MET C CB    1 
ATOM   3855 C  CG    . MET D 2 2   ? 1.438   12.500  27.416  1.00 40.94 ? 1   MET C CG    1 
ATOM   3856 S  SD    . MET D 2 2   ? 2.710   11.171  27.654  1.00 37.63 ? 1   MET C SD    1 
ATOM   3857 C  CE    . MET D 2 2   ? 2.154   9.993   26.433  1.00 36.58 ? 1   MET C CE    1 
ATOM   3858 N  N     . THR D 2 3   ? -0.683  14.661  29.932  1.00 41.64 ? 2   THR C N     1 
ATOM   3859 C  CA    . THR D 2 3   ? -0.293  15.916  30.552  1.00 42.47 ? 2   THR C CA    1 
ATOM   3860 C  C     . THR D 2 3   ? 1.204   15.941  30.742  1.00 43.15 ? 2   THR C C     1 
ATOM   3861 O  O     . THR D 2 3   ? 1.828   14.895  30.972  1.00 38.48 ? 2   THR C O     1 
ATOM   3862 C  CB    . THR D 2 3   ? -1.000  16.122  31.889  1.00 42.36 ? 2   THR C CB    1 
ATOM   3863 O  OG1   . THR D 2 3   ? -2.386  15.898  31.684  1.00 44.07 ? 2   THR C OG1   1 
ATOM   3864 C  CG2   . THR D 2 3   ? -0.796  17.557  32.357  1.00 44.72 ? 2   THR C CG2   1 
ATOM   3865 N  N     . GLU D 2 4   ? 1.773   17.134  30.575  1.00 39.50 ? 3   GLU C N     1 
ATOM   3866 C  CA    . GLU D 2 4   ? 3.207   17.359  30.657  1.00 40.55 ? 3   GLU C CA    1 
ATOM   3867 C  C     . GLU D 2 4   ? 3.509   18.100  31.950  1.00 41.25 ? 3   GLU C C     1 
ATOM   3868 O  O     . GLU D 2 4   ? 2.698   18.901  32.423  1.00 45.09 ? 3   GLU C O     1 
ATOM   3869 C  CB    . GLU D 2 4   ? 3.734   18.182  29.464  1.00 44.03 ? 3   GLU C CB    1 
ATOM   3870 C  CG    . GLU D 2 4   ? 3.243   17.689  28.108  1.00 44.08 ? 3   GLU C CG    1 
ATOM   3871 C  CD    . GLU D 2 4   ? 4.055   18.179  26.911  1.00 46.79 ? 3   GLU C CD    1 
ATOM   3872 O  OE1   . GLU D 2 4   ? 4.935   19.084  27.044  1.00 48.78 ? 3   GLU C OE1   1 
ATOM   3873 O  OE2   . GLU D 2 4   ? 3.741   17.686  25.799  1.00 44.80 ? 3   GLU C OE2   1 
ATOM   3874 N  N     . TYR D 2 5   ? 4.656   17.799  32.536  1.00 39.65 ? 4   TYR C N     1 
ATOM   3875 C  CA    . TYR D 2 5   ? 5.081   18.374  33.803  1.00 41.62 ? 4   TYR C CA    1 
ATOM   3876 C  C     . TYR D 2 5   ? 6.512   18.845  33.665  1.00 39.84 ? 4   TYR C C     1 
ATOM   3877 O  O     . TYR D 2 5   ? 7.387   18.076  33.261  1.00 38.88 ? 4   TYR C O     1 
ATOM   3878 C  CB    . TYR D 2 5   ? 4.961   17.385  34.951  1.00 39.32 ? 4   TYR C CB    1 
ATOM   3879 C  CG    . TYR D 2 5   ? 3.544   16.912  35.200  1.00 43.87 ? 4   TYR C CG    1 
ATOM   3880 C  CD1   . TYR D 2 5   ? 3.214   15.559  35.119  1.00 44.01 ? 4   TYR C CD1   1 
ATOM   3881 C  CD2   . TYR D 2 5   ? 2.570   17.809  35.648  1.00 45.00 ? 4   TYR C CD2   1 
ATOM   3882 C  CE1   . TYR D 2 5   ? 1.927   15.117  35.363  1.00 47.82 ? 4   TYR C CE1   1 
ATOM   3883 C  CE2   . TYR D 2 5   ? 1.276   17.380  35.912  1.00 45.51 ? 4   TYR C CE2   1 
ATOM   3884 C  CZ    . TYR D 2 5   ? 0.958   16.031  35.776  1.00 48.37 ? 4   TYR C CZ    1 
ATOM   3885 O  OH    . TYR D 2 5   ? -0.319  15.592  36.043  1.00 51.62 ? 4   TYR C OH    1 
ATOM   3886 N  N     . LYS D 2 6   ? 6.739   20.121  33.959  1.00 45.53 ? 5   LYS C N     1 
ATOM   3887 C  CA    . LYS D 2 6   ? 8.067   20.722  33.855  1.00 37.96 ? 5   LYS C CA    1 
ATOM   3888 C  C     . LYS D 2 6   ? 8.703   20.785  35.237  1.00 42.07 ? 5   LYS C C     1 
ATOM   3889 O  O     . LYS D 2 6   ? 8.318   21.621  36.068  1.00 45.90 ? 5   LYS C O     1 
ATOM   3890 C  CB    . LYS D 2 6   ? 7.961   22.082  33.173  1.00 44.23 ? 5   LYS C CB    1 
ATOM   3891 C  CG    . LYS D 2 6   ? 7.032   21.988  31.951  1.00 48.36 ? 5   LYS C CG    1 
ATOM   3892 C  CD    . LYS D 2 6   ? 7.037   23.205  31.048  1.00 48.69 ? 5   LYS C CD    1 
ATOM   3893 C  CE    . LYS D 2 6   ? 5.994   24.171  31.527  1.00 56.26 ? 5   LYS C CE    1 
ATOM   3894 N  NZ    . LYS D 2 6   ? 6.531   25.011  32.658  1.00 60.34 ? 5   LYS C NZ    1 
ATOM   3895 N  N     . LEU D 2 7   ? 9.665   19.882  35.478  1.00 39.10 ? 6   LEU C N     1 
ATOM   3896 C  CA    . LEU D 2 7   ? 10.460  19.742  36.699  1.00 38.83 ? 6   LEU C CA    1 
ATOM   3897 C  C     . LEU D 2 7   ? 11.866  20.324  36.520  1.00 39.38 ? 6   LEU C C     1 
ATOM   3898 O  O     . LEU D 2 7   ? 12.429  20.248  35.427  1.00 38.68 ? 6   LEU C O     1 
ATOM   3899 C  CB    . LEU D 2 7   ? 10.626  18.270  37.062  1.00 37.33 ? 6   LEU C CB    1 
ATOM   3900 C  CG    . LEU D 2 7   ? 9.497   17.237  36.886  1.00 41.63 ? 6   LEU C CG    1 
ATOM   3901 C  CD1   . LEU D 2 7   ? 9.882   15.972  37.613  1.00 40.02 ? 6   LEU C CD1   1 
ATOM   3902 C  CD2   . LEU D 2 7   ? 8.163   17.733  37.373  1.00 45.11 ? 6   LEU C CD2   1 
ATOM   3903 N  N     . VAL D 2 8   ? 12.466  20.825  37.618  1.00 38.19 ? 7   VAL C N     1 
ATOM   3904 C  CA    . VAL D 2 8   ? 13.811  21.435  37.619  1.00 38.76 ? 7   VAL C CA    1 
ATOM   3905 C  C     . VAL D 2 8   ? 14.654  20.868  38.764  1.00 41.26 ? 7   VAL C C     1 
ATOM   3906 O  O     . VAL D 2 8   ? 14.230  20.911  39.925  1.00 43.60 ? 7   VAL C O     1 
ATOM   3907 C  CB    . VAL D 2 8   ? 13.735  22.962  37.754  1.00 41.97 ? 7   VAL C CB    1 
ATOM   3908 C  CG1   . VAL D 2 8   ? 15.165  23.597  37.732  1.00 37.99 ? 7   VAL C CG1   1 
ATOM   3909 C  CG2   . VAL D 2 8   ? 12.842  23.569  36.699  1.00 41.63 ? 7   VAL C CG2   1 
ATOM   3910 N  N     . VAL D 2 9   ? 15.858  20.364  38.449  1.00 37.29 ? 8   VAL C N     1 
ATOM   3911 C  CA    . VAL D 2 9   ? 16.776  19.768  39.425  1.00 38.37 ? 8   VAL C CA    1 
ATOM   3912 C  C     . VAL D 2 9   ? 17.861  20.786  39.758  1.00 39.44 ? 8   VAL C C     1 
ATOM   3913 O  O     . VAL D 2 9   ? 18.487  21.326  38.847  1.00 39.67 ? 8   VAL C O     1 
ATOM   3914 C  CB    . VAL D 2 9   ? 17.410  18.483  38.868  1.00 38.02 ? 8   VAL C CB    1 
ATOM   3915 C  CG1   . VAL D 2 9   ? 18.299  17.816  39.874  1.00 39.51 ? 8   VAL C CG1   1 
ATOM   3916 C  CG2   . VAL D 2 9   ? 16.349  17.503  38.306  1.00 36.41 ? 8   VAL C CG2   1 
ATOM   3917 N  N     . VAL D 2 10  ? 18.137  20.988  41.061  1.00 41.19 ? 9   VAL C N     1 
ATOM   3918 C  CA    . VAL D 2 10  ? 19.117  21.967  41.566  1.00 46.67 ? 9   VAL C CA    1 
ATOM   3919 C  C     . VAL D 2 10  ? 19.964  21.369  42.689  1.00 46.12 ? 9   VAL C C     1 
ATOM   3920 O  O     . VAL D 2 10  ? 19.578  20.398  43.346  1.00 44.60 ? 9   VAL C O     1 
ATOM   3921 C  CB    . VAL D 2 10  ? 18.442  23.232  42.125  1.00 50.10 ? 9   VAL C CB    1 
ATOM   3922 C  CG1   . VAL D 2 10  ? 17.589  23.906  41.054  1.00 42.48 ? 9   VAL C CG1   1 
ATOM   3923 C  CG2   . VAL D 2 10  ? 17.612  22.824  43.273  1.00 44.88 ? 9   VAL C CG2   1 
ATOM   3924 N  N     . GLY D 2 11  ? 21.122  21.977  42.918  1.00 49.41 ? 10  GLY C N     1 
ATOM   3925 C  CA    . GLY D 2 11  ? 22.060  21.569  43.953  1.00 50.55 ? 10  GLY C CA    1 
ATOM   3926 C  C     . GLY D 2 11  ? 23.474  21.984  43.604  1.00 50.84 ? 10  GLY C C     1 
ATOM   3927 O  O     . GLY D 2 11  ? 23.797  22.323  42.469  1.00 51.18 ? 10  GLY C O     1 
ATOM   3928 N  N     . ALA D 2 12  ? 24.342  21.959  44.603  1.00 50.06 ? 11  ALA C N     1 
ATOM   3929 C  CA    . ALA D 2 12  ? 25.745  22.236  44.338  1.00 51.03 ? 11  ALA C CA    1 
ATOM   3930 C  C     . ALA D 2 12  ? 26.338  21.169  43.430  1.00 49.89 ? 11  ALA C C     1 
ATOM   3931 O  O     . ALA D 2 12  ? 25.796  20.067  43.265  1.00 51.08 ? 11  ALA C O     1 
ATOM   3932 C  CB    . ALA D 2 12  ? 26.549  22.290  45.635  1.00 53.82 ? 11  ALA C CB    1 
ATOM   3933 N  N     . ASP D 2 13  ? 27.465  21.495  42.838  1.00 50.32 ? 12  ASP C N     1 
ATOM   3934 C  CA    . ASP D 2 13  ? 28.006  20.576  41.855  1.00 51.74 ? 12  ASP C CA    1 
ATOM   3935 C  C     . ASP D 2 13  ? 28.699  19.380  42.517  1.00 51.39 ? 12  ASP C C     1 
ATOM   3936 O  O     . ASP D 2 13  ? 29.212  19.461  43.639  1.00 53.03 ? 12  ASP C O     1 
ATOM   3937 C  CB    . ASP D 2 13  ? 28.917  21.309  40.831  1.00 55.99 ? 12  ASP C CB    1 
ATOM   3938 C  CG    . ASP D 2 13  ? 28.097  22.140  39.770  1.00 49.06 ? 12  ASP C CG    1 
ATOM   3939 O  OD1   . ASP D 2 13  ? 27.078  21.632  39.291  1.00 45.22 ? 12  ASP C OD1   1 
ATOM   3940 O  OD2   . ASP D 2 13  ? 28.443  23.292  39.406  1.00 52.01 ? 12  ASP C OD2   1 
ATOM   3941 N  N     . GLY D 2 14  ? 28.691  18.247  41.798  1.00 49.60 ? 13  GLY C N     1 
ATOM   3942 C  CA    . GLY D 2 14  ? 29.303  17.018  42.263  1.00 50.95 ? 13  GLY C CA    1 
ATOM   3943 C  C     . GLY D 2 14  ? 28.390  16.103  43.049  1.00 50.91 ? 13  GLY C C     1 
ATOM   3944 O  O     . GLY D 2 14  ? 28.787  14.970  43.356  1.00 51.93 ? 13  GLY C O     1 
ATOM   3945 N  N     . VAL D 2 15  ? 27.167  16.542  43.349  1.00 49.89 ? 14  VAL C N     1 
ATOM   3946 C  CA    . VAL D 2 15  ? 26.300  15.770  44.244  1.00 50.24 ? 14  VAL C CA    1 
ATOM   3947 C  C     . VAL D 2 15  ? 25.643  14.621  43.501  1.00 50.84 ? 14  VAL C C     1 
ATOM   3948 O  O     . VAL D 2 15  ? 25.281  13.603  44.111  1.00 49.19 ? 14  VAL C O     1 
ATOM   3949 C  CB    . VAL D 2 15  ? 25.251  16.694  44.890  1.00 51.31 ? 14  VAL C CB    1 
ATOM   3950 C  CG1   . VAL D 2 15  ? 25.967  17.853  45.591  1.00 52.01 ? 14  VAL C CG1   1 
ATOM   3951 C  CG2   . VAL D 2 15  ? 24.215  17.174  43.839  1.00 47.67 ? 14  VAL C CG2   1 
ATOM   3952 N  N     . GLY D 2 16  ? 25.477  14.758  42.183  1.00 46.53 ? 15  GLY C N     1 
ATOM   3953 C  CA    . GLY D 2 16  ? 24.914  13.662  41.426  1.00 45.11 ? 15  GLY C CA    1 
ATOM   3954 C  C     . GLY D 2 16  ? 23.585  13.957  40.766  1.00 45.24 ? 15  GLY C C     1 
ATOM   3955 O  O     . GLY D 2 16  ? 22.918  13.022  40.327  1.00 42.05 ? 15  GLY C O     1 
ATOM   3956 N  N     . LYS D 2 17  ? 23.205  15.240  40.679  1.00 50.12 ? 16  LYS C N     1 
ATOM   3957 C  CA    . LYS D 2 17  ? 21.990  15.638  39.961  1.00 47.00 ? 16  LYS C CA    1 
ATOM   3958 C  C     . LYS D 2 17  ? 21.926  15.056  38.564  1.00 41.15 ? 16  LYS C C     1 
ATOM   3959 O  O     . LYS D 2 17  ? 20.897  14.519  38.144  1.00 40.65 ? 16  LYS C O     1 
ATOM   3960 C  CB    . LYS D 2 17  ? 21.926  17.150  39.854  1.00 46.06 ? 16  LYS C CB    1 
ATOM   3961 C  CG    . LYS D 2 17  ? 21.820  17.716  41.194  1.00 48.34 ? 16  LYS C CG    1 
ATOM   3962 C  CD    . LYS D 2 17  ? 21.330  19.109  41.184  1.00 49.30 ? 16  LYS C CD    1 
ATOM   3963 C  CE    . LYS D 2 17  ? 21.608  19.848  39.966  1.00 50.37 ? 16  LYS C CE    1 
ATOM   3964 N  NZ    . LYS D 2 17  ? 22.076  21.228  40.374  1.00 54.01 ? 16  LYS C NZ    1 
ATOM   3965 N  N     . SER D 2 18  ? 22.976  15.232  37.794  1.00 38.83 ? 17  SER C N     1 
ATOM   3966 C  CA    . SER D 2 18  ? 22.933  14.653  36.456  1.00 38.90 ? 17  SER C CA    1 
ATOM   3967 C  C     . SER D 2 18  ? 22.955  13.127  36.521  1.00 39.32 ? 17  SER C C     1 
ATOM   3968 O  O     . SER D 2 18  ? 22.267  12.449  35.746  1.00 38.24 ? 17  SER C O     1 
ATOM   3969 C  CB    . SER D 2 18  ? 24.081  15.203  35.599  1.00 37.34 ? 17  SER C CB    1 
ATOM   3970 O  OG    . SER D 2 18  ? 24.068  16.612  35.678  1.00 37.38 ? 17  SER C OG    1 
ATOM   3971 N  N     . ALA D 2 19  ? 23.687  12.555  37.474  1.00 39.76 ? 18  ALA C N     1 
ATOM   3972 C  CA    . ALA D 2 19  ? 23.691  11.108  37.559  1.00 39.92 ? 18  ALA C CA    1 
ATOM   3973 C  C     . ALA D 2 19  ? 22.330  10.583  37.993  1.00 40.67 ? 18  ALA C C     1 
ATOM   3974 O  O     . ALA D 2 19  ? 21.965  9.479   37.584  1.00 40.35 ? 18  ALA C O     1 
ATOM   3975 C  CB    . ALA D 2 19  ? 24.812  10.632  38.489  1.00 42.86 ? 18  ALA C CB    1 
ATOM   3976 N  N     . LEU D 2 20  ? 21.567  11.382  38.774  1.00 39.55 ? 19  LEU C N     1 
ATOM   3977 C  CA    . LEU D 2 20  ? 20.203  11.040  39.158  1.00 39.45 ? 19  LEU C CA    1 
ATOM   3978 C  C     . LEU D 2 20  ? 19.250  11.241  37.992  1.00 39.59 ? 19  LEU C C     1 
ATOM   3979 O  O     . LEU D 2 20  ? 18.440  10.359  37.671  1.00 39.86 ? 19  LEU C O     1 
ATOM   3980 C  CB    . LEU D 2 20  ? 19.756  11.924  40.329  1.00 42.43 ? 19  LEU C CB    1 
ATOM   3981 C  CG    . LEU D 2 20  ? 20.147  11.509  41.743  1.00 42.27 ? 19  LEU C CG    1 
ATOM   3982 C  CD1   . LEU D 2 20  ? 19.575  12.548  42.725  1.00 47.14 ? 19  LEU C CD1   1 
ATOM   3983 C  CD2   . LEU D 2 20  ? 19.612  10.100  42.058  1.00 42.78 ? 19  LEU C CD2   1 
ATOM   3984 N  N     . THR D 2 21  ? 19.329  12.418  37.365  1.00 38.87 ? 20  THR C N     1 
ATOM   3985 C  CA    . THR D 2 21  ? 18.520  12.694  36.181  1.00 34.74 ? 20  THR C CA    1 
ATOM   3986 C  C     . THR D 2 21  ? 18.777  11.643  35.107  1.00 35.16 ? 20  THR C C     1 
ATOM   3987 O  O     . THR D 2 21  ? 17.834  11.093  34.541  1.00 33.99 ? 20  THR C O     1 
ATOM   3988 C  CB    . THR D 2 21  ? 18.826  14.108  35.678  1.00 35.71 ? 20  THR C CB    1 
ATOM   3989 O  OG1   . THR D 2 21  ? 18.320  15.095  36.603  1.00 34.89 ? 20  THR C OG1   1 
ATOM   3990 C  CG2   . THR D 2 21  ? 18.160  14.331  34.284  1.00 33.68 ? 20  THR C CG2   1 
ATOM   3991 N  N     . ILE D 2 22  ? 20.063  11.344  34.810  1.00 36.33 ? 21  ILE C N     1 
ATOM   3992 C  CA    . ILE D 2 22  ? 20.400  10.344  33.776  1.00 38.33 ? 21  ILE C CA    1 
ATOM   3993 C  C     . ILE D 2 22  ? 19.976  8.930   34.176  1.00 39.22 ? 21  ILE C C     1 
ATOM   3994 O  O     . ILE D 2 22  ? 19.692  8.087   33.312  1.00 41.63 ? 21  ILE C O     1 
ATOM   3995 C  CB    . ILE D 2 22  ? 21.906  10.426  33.414  1.00 37.60 ? 21  ILE C CB    1 
ATOM   3996 C  CG1   . ILE D 2 22  ? 22.229  11.858  32.952  1.00 37.42 ? 21  ILE C CG1   1 
ATOM   3997 C  CG2   . ILE D 2 22  ? 22.347  9.341   32.394  1.00 39.40 ? 21  ILE C CG2   1 
ATOM   3998 C  CD1   . ILE D 2 22  ? 23.620  11.998  32.343  1.00 41.94 ? 21  ILE C CD1   1 
ATOM   3999 N  N     . GLN D 2 23  ? 19.962  8.648   35.461  1.00 37.31 ? 22  GLN C N     1 
ATOM   4000 C  CA    . GLN D 2 23  ? 19.432  7.373   35.926  1.00 44.70 ? 22  GLN C CA    1 
ATOM   4001 C  C     . GLN D 2 23  ? 17.919  7.321   35.717  1.00 38.41 ? 22  GLN C C     1 
ATOM   4002 O  O     . GLN D 2 23  ? 17.394  6.328   35.205  1.00 48.04 ? 22  GLN C O     1 
ATOM   4003 C  CB    . GLN D 2 23  ? 19.795  7.176   37.397  1.00 46.39 ? 22  GLN C CB    1 
ATOM   4004 C  CG    . GLN D 2 23  ? 19.728  5.739   37.865  1.00 50.51 ? 22  GLN C CG    1 
ATOM   4005 C  CD    . GLN D 2 23  ? 20.722  4.838   37.148  1.00 54.39 ? 22  GLN C CD    1 
ATOM   4006 O  OE1   . GLN D 2 23  ? 20.394  4.187   36.157  1.00 53.81 ? 22  GLN C OE1   1 
ATOM   4007 N  NE2   . GLN D 2 23  ? 21.922  4.743   37.692  1.00 56.40 ? 22  GLN C NE2   1 
ATOM   4008 N  N     . LEU D 2 24  ? 17.211  8.406   36.045  1.00 40.12 ? 23  LEU C N     1 
ATOM   4009 C  CA    . LEU D 2 24  ? 15.772  8.477   35.753  1.00 34.66 ? 23  LEU C CA    1 
ATOM   4010 C  C     . LEU D 2 24  ? 15.512  8.322   34.269  1.00 38.20 ? 23  LEU C C     1 
ATOM   4011 O  O     . LEU D 2 24  ? 14.630  7.558   33.860  1.00 37.58 ? 23  LEU C O     1 
ATOM   4012 C  CB    . LEU D 2 24  ? 15.192  9.798   36.211  1.00 34.51 ? 23  LEU C CB    1 
ATOM   4013 C  CG    . LEU D 2 24  ? 13.692  9.844   35.889  1.00 38.56 ? 23  LEU C CG    1 
ATOM   4014 C  CD1   . LEU D 2 24  ? 12.922  9.028   36.914  1.00 35.30 ? 23  LEU C CD1   1 
ATOM   4015 C  CD2   . LEU D 2 24  ? 13.251  11.313  35.813  1.00 35.72 ? 23  LEU C CD2   1 
ATOM   4016 N  N     . ILE D 2 25  ? 16.288  9.052   33.446  1.00 37.31 ? 24  ILE C N     1 
ATOM   4017 C  CA    . ILE D 2 25  ? 16.049  9.085   32.005  1.00 39.16 ? 24  ILE C CA    1 
ATOM   4018 C  C     . ILE D 2 25  ? 16.608  7.849   31.307  1.00 36.92 ? 24  ILE C C     1 
ATOM   4019 O  O     . ILE D 2 25  ? 15.921  7.220   30.496  1.00 39.86 ? 24  ILE C O     1 
ATOM   4020 C  CB    . ILE D 2 25  ? 16.644  10.362  31.390  1.00 36.47 ? 24  ILE C CB    1 
ATOM   4021 C  CG1   . ILE D 2 25  ? 16.020  11.608  32.021  1.00 34.20 ? 24  ILE C CG1   1 
ATOM   4022 C  CG2   . ILE D 2 25  ? 16.430  10.343  29.859  1.00 36.90 ? 24  ILE C CG2   1 
ATOM   4023 C  CD1   . ILE D 2 25  ? 14.494  11.648  31.892  1.00 30.08 ? 24  ILE C CD1   1 
ATOM   4024 N  N     . GLN D 2 26  ? 17.863  7.512   31.541  1.00 40.95 ? 25  GLN C N     1 
ATOM   4025 C  CA    . GLN D 2 26  ? 18.493  6.513   30.685  1.00 47.13 ? 25  GLN C CA    1 
ATOM   4026 C  C     . GLN D 2 26  ? 18.879  5.246   31.413  1.00 54.39 ? 25  GLN C C     1 
ATOM   4027 O  O     . GLN D 2 26  ? 19.444  4.347   30.780  1.00 54.37 ? 25  GLN C O     1 
ATOM   4028 C  CB    . GLN D 2 26  ? 19.733  7.075   29.969  1.00 50.78 ? 25  GLN C CB    1 
ATOM   4029 C  CG    . GLN D 2 26  ? 19.405  8.169   28.978  1.00 43.28 ? 25  GLN C CG    1 
ATOM   4030 C  CD    . GLN D 2 26  ? 20.617  8.762   28.339  1.00 51.34 ? 25  GLN C CD    1 
ATOM   4031 O  OE1   . GLN D 2 26  ? 21.737  8.246   28.492  1.00 51.51 ? 25  GLN C OE1   1 
ATOM   4032 N  NE2   . GLN D 2 26  ? 20.416  9.860   27.593  1.00 49.88 ? 25  GLN C NE2   1 
ATOM   4033 N  N     . ASN D 2 27  ? 18.595  5.148   32.709  1.00 61.03 ? 26  ASN C N     1 
ATOM   4034 C  CA    . ASN D 2 27  ? 18.854  3.951   33.492  1.00 65.32 ? 26  ASN C CA    1 
ATOM   4035 C  C     . ASN D 2 27  ? 20.333  3.604   33.488  1.00 69.97 ? 26  ASN C C     1 
ATOM   4036 O  O     . ASN D 2 27  ? 20.720  2.516   33.938  1.00 75.26 ? 26  ASN C O     1 
ATOM   4037 C  CB    . ASN D 2 27  ? 18.007  2.773   32.986  1.00 65.49 ? 26  ASN C CB    1 
ATOM   4038 C  CG    . ASN D 2 27  ? 17.311  2.015   34.117  1.00 68.67 ? 26  ASN C CG    1 
ATOM   4039 O  OD1   . ASN D 2 27  ? 17.942  1.638   35.112  1.00 69.06 ? 26  ASN C OD1   1 
ATOM   4040 N  ND2   . ASN D 2 27  ? 15.996  1.809   33.977  1.00 67.51 ? 26  ASN C ND2   1 
ATOM   4041 N  N     . HIS D 2 28  ? 21.166  4.509   32.986  1.00 57.97 ? 27  HIS C N     1 
ATOM   4042 C  CA    . HIS D 2 28  ? 22.613  4.367   32.926  1.00 59.44 ? 27  HIS C CA    1 
ATOM   4043 C  C     . HIS D 2 28  ? 23.278  5.198   34.025  1.00 51.86 ? 27  HIS C C     1 
ATOM   4044 O  O     . HIS D 2 28  ? 22.763  6.242   34.434  1.00 49.43 ? 27  HIS C O     1 
ATOM   4045 C  CB    . HIS D 2 28  ? 23.105  4.790   31.538  1.00 56.04 ? 27  HIS C CB    1 
ATOM   4046 C  CG    . HIS D 2 28  ? 24.573  5.019   31.457  1.00 58.80 ? 27  HIS C CG    1 
ATOM   4047 N  ND1   . HIS D 2 28  ? 25.122  6.281   31.411  1.00 56.05 ? 27  HIS C ND1   1 
ATOM   4048 C  CD2   . HIS D 2 28  ? 25.614  4.149   31.430  1.00 60.85 ? 27  HIS C CD2   1 
ATOM   4049 C  CE1   . HIS D 2 28  ? 26.441  6.180   31.342  1.00 62.50 ? 27  HIS C CE1   1 
ATOM   4050 N  NE2   . HIS D 2 28  ? 26.766  4.898   31.362  1.00 63.20 ? 27  HIS C NE2   1 
ATOM   4051 N  N     . PHE D 2 29  ? 24.410  4.714   34.528  1.00 51.23 ? 28  PHE C N     1 
ATOM   4052 C  CA    . PHE D 2 29  ? 25.153  5.442   35.546  1.00 50.72 ? 28  PHE C CA    1 
ATOM   4053 C  C     . PHE D 2 29  ? 26.438  6.018   34.974  1.00 51.90 ? 28  PHE C C     1 
ATOM   4054 O  O     . PHE D 2 29  ? 27.259  5.280   34.414  1.00 45.83 ? 28  PHE C O     1 
ATOM   4055 C  CB    . PHE D 2 29  ? 25.487  4.566   36.746  1.00 48.84 ? 28  PHE C CB    1 
ATOM   4056 C  CG    . PHE D 2 29  ? 26.350  5.253   37.757  1.00 49.78 ? 28  PHE C CG    1 
ATOM   4057 C  CD1   . PHE D 2 29  ? 25.831  6.295   38.521  1.00 51.48 ? 28  PHE C CD1   1 
ATOM   4058 C  CD2   . PHE D 2 29  ? 27.657  4.832   37.986  1.00 50.86 ? 28  PHE C CD2   1 
ATOM   4059 C  CE1   . PHE D 2 29  ? 26.598  6.925   39.492  1.00 49.06 ? 28  PHE C CE1   1 
ATOM   4060 C  CE2   . PHE D 2 29  ? 28.444  5.452   38.964  1.00 51.05 ? 28  PHE C CE2   1 
ATOM   4061 C  CZ    . PHE D 2 29  ? 27.911  6.501   39.720  1.00 51.75 ? 28  PHE C CZ    1 
ATOM   4062 N  N     . VAL D 2 30  ? 26.595  7.333   35.133  1.00 51.30 ? 29  VAL C N     1 
ATOM   4063 C  CA    . VAL D 2 30  ? 27.801  8.062   34.751  1.00 51.03 ? 29  VAL C CA    1 
ATOM   4064 C  C     . VAL D 2 30  ? 28.764  8.057   35.945  1.00 49.57 ? 29  VAL C C     1 
ATOM   4065 O  O     . VAL D 2 30  ? 28.526  8.693   36.977  1.00 47.06 ? 29  VAL C O     1 
ATOM   4066 C  CB    . VAL D 2 30  ? 27.468  9.490   34.272  1.00 52.47 ? 29  VAL C CB    1 
ATOM   4067 C  CG1   . VAL D 2 30  ? 26.750  10.355  35.363  1.00 50.30 ? 29  VAL C CG1   1 
ATOM   4068 C  CG2   . VAL D 2 30  ? 28.704  10.201  33.751  1.00 51.20 ? 29  VAL C CG2   1 
ATOM   4069 N  N     . ASP D 2 31  ? 29.840  7.289   35.826  1.00 51.02 ? 30  ASP C N     1 
ATOM   4070 C  CA    . ASP D 2 31  ? 30.884  7.348   36.842  1.00 50.77 ? 30  ASP C CA    1 
ATOM   4071 C  C     . ASP D 2 31  ? 31.882  8.488   36.623  1.00 52.58 ? 30  ASP C C     1 
ATOM   4072 O  O     . ASP D 2 31  ? 32.609  8.843   37.554  1.00 52.16 ? 30  ASP C O     1 
ATOM   4073 C  CB    . ASP D 2 31  ? 31.611  5.990   36.983  1.00 55.70 ? 30  ASP C CB    1 
ATOM   4074 C  CG    . ASP D 2 31  ? 31.873  5.259   35.648  1.00 54.76 ? 30  ASP C CG    1 
ATOM   4075 O  OD1   . ASP D 2 31  ? 31.383  5.636   34.562  1.00 55.50 ? 30  ASP C OD1   1 
ATOM   4076 O  OD2   . ASP D 2 31  ? 32.667  4.295   35.701  1.00 64.21 ? 30  ASP C OD2   1 
ATOM   4077 N  N     . GLU D 2 32  ? 31.900  9.107   35.448  1.00 50.09 ? 31  GLU C N     1 
ATOM   4078 C  CA    . GLU D 2 32  ? 32.806  10.217  35.174  1.00 49.91 ? 31  GLU C CA    1 
ATOM   4079 C  C     . GLU D 2 32  ? 32.120  11.548  35.496  1.00 49.32 ? 31  GLU C C     1 
ATOM   4080 O  O     . GLU D 2 32  ? 30.904  11.691  35.334  1.00 46.64 ? 31  GLU C O     1 
ATOM   4081 C  CB    . GLU D 2 32  ? 33.254  10.150  33.710  1.00 48.47 ? 31  GLU C CB    1 
ATOM   4082 C  CG    . GLU D 2 32  ? 34.149  8.938   33.379  1.00 50.36 ? 31  GLU C CG    1 
ATOM   4083 C  CD    . GLU D 2 32  ? 34.401  8.781   31.884  1.00 54.96 ? 31  GLU C CD    1 
ATOM   4084 O  OE1   . GLU D 2 32  ? 33.672  9.422   31.088  1.00 54.21 ? 31  GLU C OE1   1 
ATOM   4085 O  OE2   . GLU D 2 32  ? 35.311  8.013   31.502  1.00 57.81 ? 31  GLU C OE2   1 
ATOM   4086 N  N     . TYR D 2 33  ? 32.904  12.515  35.982  1.00 49.20 ? 32  TYR C N     1 
ATOM   4087 C  CA    . TYR D 2 33  ? 32.383  13.823  36.380  1.00 48.41 ? 32  TYR C CA    1 
ATOM   4088 C  C     . TYR D 2 33  ? 32.382  14.787  35.188  1.00 46.92 ? 32  TYR C C     1 
ATOM   4089 O  O     . TYR D 2 33  ? 33.461  15.202  34.701  1.00 48.05 ? 32  TYR C O     1 
ATOM   4090 C  CB    . TYR D 2 33  ? 33.194  14.382  37.550  1.00 50.90 ? 32  TYR C CB    1 
ATOM   4091 C  CG    . TYR D 2 33  ? 32.754  15.754  38.014  1.00 50.51 ? 32  TYR C CG    1 
ATOM   4092 C  CD1   . TYR D 2 33  ? 31.399  16.089  38.060  1.00 50.64 ? 32  TYR C CD1   1 
ATOM   4093 C  CD2   . TYR D 2 33  ? 33.692  16.721  38.389  1.00 52.38 ? 32  TYR C CD2   1 
ATOM   4094 C  CE1   . TYR D 2 33  ? 30.986  17.337  38.485  1.00 48.32 ? 32  TYR C CE1   1 
ATOM   4095 C  CE2   . TYR D 2 33  ? 33.296  17.969  38.820  1.00 52.23 ? 32  TYR C CE2   1 
ATOM   4096 C  CZ    . TYR D 2 33  ? 31.937  18.270  38.863  1.00 51.61 ? 32  TYR C CZ    1 
ATOM   4097 O  OH    . TYR D 2 33  ? 31.519  19.511  39.289  1.00 54.64 ? 32  TYR C OH    1 
ATOM   4098 N  N     . ASP D 2 34  ? 31.164  15.172  34.756  1.00 47.92 ? 33  ASP C N     1 
ATOM   4099 C  CA    . ASP D 2 34  ? 30.924  16.055  33.606  1.00 44.69 ? 33  ASP C CA    1 
ATOM   4100 C  C     . ASP D 2 34  ? 30.028  17.208  34.060  1.00 43.64 ? 33  ASP C C     1 
ATOM   4101 O  O     . ASP D 2 34  ? 28.802  17.152  33.881  1.00 42.82 ? 33  ASP C O     1 
ATOM   4102 C  CB    . ASP D 2 34  ? 30.278  15.271  32.459  1.00 47.32 ? 33  ASP C CB    1 
ATOM   4103 C  CG    . ASP D 2 34  ? 30.184  16.061  31.156  1.00 47.78 ? 33  ASP C CG    1 
ATOM   4104 O  OD1   . ASP D 2 34  ? 31.006  16.996  30.923  1.00 43.31 ? 33  ASP C OD1   1 
ATOM   4105 O  OD2   . ASP D 2 34  ? 29.265  15.740  30.370  1.00 48.92 ? 33  ASP C OD2   1 
ATOM   4106 N  N     . PRO D 2 35  ? 30.610  18.293  34.607  1.00 44.04 ? 34  PRO C N     1 
ATOM   4107 C  CA    . PRO D 2 35  ? 29.786  19.366  35.208  1.00 43.14 ? 34  PRO C CA    1 
ATOM   4108 C  C     . PRO D 2 35  ? 28.863  20.019  34.175  1.00 41.05 ? 34  PRO C C     1 
ATOM   4109 O  O     . PRO D 2 35  ? 29.255  20.229  33.028  1.00 41.53 ? 34  PRO C O     1 
ATOM   4110 C  CB    . PRO D 2 35  ? 30.821  20.370  35.753  1.00 45.25 ? 34  PRO C CB    1 
ATOM   4111 C  CG    . PRO D 2 35  ? 32.172  19.856  35.396  1.00 46.69 ? 34  PRO C CG    1 
ATOM   4112 C  CD    . PRO D 2 35  ? 32.060  18.522  34.721  1.00 45.68 ? 34  PRO C CD    1 
ATOM   4113 N  N     . THR D 2 36  ? 27.633  20.348  34.597  1.00 40.15 ? 35  THR C N     1 
ATOM   4114 C  CA    . THR D 2 36  ? 26.528  20.686  33.689  1.00 38.19 ? 35  THR C CA    1 
ATOM   4115 C  C     . THR D 2 36  ? 26.491  22.155  33.267  1.00 38.19 ? 35  THR C C     1 
ATOM   4116 O  O     . THR D 2 36  ? 26.677  23.048  34.089  1.00 39.51 ? 35  THR C O     1 
ATOM   4117 C  CB    . THR D 2 36  ? 25.198  20.334  34.359  1.00 37.52 ? 35  THR C CB    1 
ATOM   4118 O  OG1   . THR D 2 36  ? 25.201  18.942  34.623  1.00 37.50 ? 35  THR C OG1   1 
ATOM   4119 C  CG2   . THR D 2 36  ? 24.031  20.645  33.405  1.00 35.72 ? 35  THR C CG2   1 
ATOM   4120 N  N     . ILE D 2 37  ? 26.204  22.404  31.976  1.00 36.83 ? 36  ILE C N     1 
ATOM   4121 C  CA    . ILE D 2 37  ? 25.873  23.758  31.514  1.00 36.68 ? 36  ILE C CA    1 
ATOM   4122 C  C     . ILE D 2 37  ? 24.365  23.923  31.647  1.00 35.64 ? 36  ILE C C     1 
ATOM   4123 O  O     . ILE D 2 37  ? 23.865  24.711  32.444  1.00 36.39 ? 36  ILE C O     1 
ATOM   4124 C  CB    . ILE D 2 37  ? 26.318  24.023  30.041  1.00 35.98 ? 36  ILE C CB    1 
ATOM   4125 C  CG1   . ILE D 2 37  ? 27.810  23.712  29.813  1.00 37.11 ? 36  ILE C CG1   1 
ATOM   4126 C  CG2   . ILE D 2 37  ? 26.005  25.498  29.657  1.00 36.16 ? 36  ILE C CG2   1 
ATOM   4127 C  CD1   . ILE D 2 37  ? 28.773  24.576  30.554  1.00 39.14 ? 36  ILE C CD1   1 
ATOM   4128 N  N     . GLU D 2 38  ? 23.627  23.145  30.878  1.00 34.10 ? 37  GLU C N     1 
ATOM   4129 C  CA    . GLU D 2 38  ? 22.173  23.106  30.994  1.00 33.25 ? 37  GLU C CA    1 
ATOM   4130 C  C     . GLU D 2 38  ? 21.662  21.993  30.112  1.00 31.96 ? 37  GLU C C     1 
ATOM   4131 O  O     . GLU D 2 38  ? 22.067  21.951  28.951  1.00 31.14 ? 37  GLU C O     1 
ATOM   4132 C  CB    . GLU D 2 38  ? 21.588  24.437  30.571  1.00 33.26 ? 37  GLU C CB    1 
ATOM   4133 C  CG    . GLU D 2 38  ? 20.224  24.727  31.109  1.00 38.09 ? 37  GLU C CG    1 
ATOM   4134 C  CD    . GLU D 2 38  ? 19.488  25.575  30.128  1.00 44.55 ? 37  GLU C CD    1 
ATOM   4135 O  OE1   . GLU D 2 38  ? 19.362  26.790  30.408  1.00 47.98 ? 37  GLU C OE1   1 
ATOM   4136 O  OE2   . GLU D 2 38  ? 18.984  25.041  29.126  1.00 47.11 ? 37  GLU C OE2   1 
ATOM   4137 N  N     . ASP D 2 39  ? 20.801  21.099  30.626  1.00 31.43 ? 38  ASP C N     1 
ATOM   4138 C  CA    . ASP D 2 39  ? 20.291  20.022  29.800  1.00 30.24 ? 38  ASP C CA    1 
ATOM   4139 C  C     . ASP D 2 39  ? 18.813  19.835  30.074  1.00 29.82 ? 38  ASP C C     1 
ATOM   4140 O  O     . ASP D 2 39  ? 18.340  20.038  31.196  1.00 30.60 ? 38  ASP C O     1 
ATOM   4141 C  CB    . ASP D 2 39  ? 21.022  18.709  30.068  1.00 30.50 ? 38  ASP C CB    1 
ATOM   4142 C  CG    . ASP D 2 39  ? 22.443  18.736  29.561  1.00 38.04 ? 38  ASP C CG    1 
ATOM   4143 O  OD1   . ASP D 2 39  ? 22.609  18.673  28.336  1.00 36.38 ? 38  ASP C OD1   1 
ATOM   4144 O  OD2   . ASP D 2 39  ? 23.372  18.830  30.397  1.00 33.86 ? 38  ASP C OD2   1 
ATOM   4145 N  N     . SER D 2 40  ? 18.087  19.447  29.023  1.00 28.74 ? 39  SER C N     1 
ATOM   4146 C  CA    . SER D 2 40  ? 16.673  19.164  29.144  1.00 28.46 ? 39  SER C CA    1 
ATOM   4147 C  C     . SER D 2 40  ? 16.425  17.753  28.663  1.00 27.81 ? 39  SER C C     1 
ATOM   4148 O  O     . SER D 2 40  ? 17.073  17.274  27.739  1.00 27.26 ? 39  SER C O     1 
ATOM   4149 C  CB    . SER D 2 40  ? 15.822  20.091  28.307  1.00 32.38 ? 39  SER C CB    1 
ATOM   4150 O  OG    . SER D 2 40  ? 15.982  21.400  28.765  1.00 36.39 ? 39  SER C OG    1 
ATOM   4151 N  N     . TYR D 2 41  ? 15.486  17.107  29.303  1.00 28.04 ? 40  TYR C N     1 
ATOM   4152 C  CA    . TYR D 2 41  ? 15.177  15.723  29.010  1.00 27.70 ? 40  TYR C CA    1 
ATOM   4153 C  C     . TYR D 2 41  ? 13.664  15.557  28.997  1.00 27.68 ? 40  TYR C C     1 
ATOM   4154 O  O     . TYR D 2 41  ? 12.946  16.301  29.681  1.00 28.98 ? 40  TYR C O     1 
ATOM   4155 C  CB    . TYR D 2 41  ? 15.779  14.756  30.055  1.00 28.47 ? 40  TYR C CB    1 
ATOM   4156 C  CG    . TYR D 2 41  ? 17.276  14.869  30.204  1.00 30.18 ? 40  TYR C CG    1 
ATOM   4157 C  CD1   . TYR D 2 41  ? 18.111  14.114  29.401  1.00 30.38 ? 40  TYR C CD1   1 
ATOM   4158 C  CD2   . TYR D 2 41  ? 17.844  15.708  31.170  1.00 29.74 ? 40  TYR C CD2   1 
ATOM   4159 C  CE1   . TYR D 2 41  ? 19.523  14.234  29.506  1.00 33.60 ? 40  TYR C CE1   1 
ATOM   4160 C  CE2   . TYR D 2 41  ? 19.196  15.810  31.301  1.00 30.33 ? 40  TYR C CE2   1 
ATOM   4161 C  CZ    . TYR D 2 41  ? 20.035  15.090  30.453  1.00 33.01 ? 40  TYR C CZ    1 
ATOM   4162 O  OH    . TYR D 2 41  ? 21.390  15.199  30.584  1.00 32.38 ? 40  TYR C OH    1 
ATOM   4163 N  N     . ARG D 2 42  ? 13.182  14.530  28.265  1.00 27.23 ? 41  ARG C N     1 
ATOM   4164 C  CA    . ARG D 2 42  ? 11.759  14.203  28.273  1.00 28.53 ? 41  ARG C CA    1 
ATOM   4165 C  C     . ARG D 2 42  ? 11.597  12.706  28.448  1.00 27.70 ? 41  ARG C C     1 
ATOM   4166 O  O     . ARG D 2 42  ? 12.351  11.924  27.862  1.00 27.33 ? 41  ARG C O     1 
ATOM   4167 C  CB    . ARG D 2 42  ? 10.985  14.574  26.982  1.00 30.27 ? 41  ARG C CB    1 
ATOM   4168 C  CG    . ARG D 2 42  ? 10.973  16.021  26.635  1.00 33.39 ? 41  ARG C CG    1 
ATOM   4169 C  CD    . ARG D 2 42  ? 10.548  16.178  25.219  1.00 32.24 ? 41  ARG C CD    1 
ATOM   4170 N  NE    . ARG D 2 42  ? 9.234   15.589  24.949  1.00 35.85 ? 41  ARG C NE    1 
ATOM   4171 C  CZ    . ARG D 2 42  ? 8.101   16.289  24.858  1.00 33.81 ? 41  ARG C CZ    1 
ATOM   4172 N  NH1   . ARG D 2 42  ? 8.086   17.598  25.031  1.00 29.33 ? 41  ARG C NH1   1 
ATOM   4173 N  NH2   . ARG D 2 42  ? 6.967   15.644  24.552  1.00 37.53 ? 41  ARG C NH2   1 
ATOM   4174 N  N     . LYS D 2 43  ? 10.637  12.311  29.263  1.00 28.49 ? 42  LYS C N     1 
ATOM   4175 C  CA    . LYS D 2 43  ? 10.363  10.913  29.539  1.00 28.98 ? 42  LYS C CA    1 
ATOM   4176 C  C     . LYS D 2 43  ? 8.868   10.776  29.762  1.00 29.67 ? 42  LYS C C     1 
ATOM   4177 O  O     . LYS D 2 43  ? 8.292   11.592  30.488  1.00 30.27 ? 42  LYS C O     1 
ATOM   4178 C  CB    . LYS D 2 43  ? 11.092  10.426  30.801  1.00 29.78 ? 42  LYS C CB    1 
ATOM   4179 C  CG    . LYS D 2 43  ? 10.971  8.952   31.046  1.00 31.24 ? 42  LYS C CG    1 
ATOM   4180 C  CD    . LYS D 2 43  ? 11.661  8.571   32.378  1.00 33.75 ? 42  LYS C CD    1 
ATOM   4181 C  CE    . LYS D 2 43  ? 11.528  7.092   32.736  1.00 40.63 ? 42  LYS C CE    1 
ATOM   4182 N  NZ    . LYS D 2 43  ? 12.160  6.273   31.670  1.00 40.96 ? 42  LYS C NZ    1 
ATOM   4183 N  N     . GLN D 2 44  ? 8.249   9.753   29.169  1.00 29.80 ? 43  GLN C N     1 
ATOM   4184 C  CA    . GLN D 2 44  ? 6.872   9.438   29.514  1.00 30.80 ? 43  GLN C CA    1 
ATOM   4185 C  C     . GLN D 2 44  ? 6.871   8.327   30.545  1.00 31.81 ? 43  GLN C C     1 
ATOM   4186 O  O     . GLN D 2 44  ? 7.714   7.428   30.503  1.00 31.70 ? 43  GLN C O     1 
ATOM   4187 C  CB    . GLN D 2 44  ? 6.061   9.058   28.276  1.00 30.95 ? 43  GLN C CB    1 
ATOM   4188 C  CG    . GLN D 2 44  ? 6.401   7.765   27.614  1.00 30.51 ? 43  GLN C CG    1 
ATOM   4189 C  CD    . GLN D 2 44  ? 5.277   7.290   26.655  1.00 30.93 ? 43  GLN C CD    1 
ATOM   4190 O  OE1   . GLN D 2 44  ? 4.144   7.105   27.058  1.00 32.03 ? 43  GLN C OE1   1 
ATOM   4191 N  NE2   . GLN D 2 44  ? 5.610   7.203   25.368  1.00 32.24 ? 43  GLN C NE2   1 
ATOM   4192 N  N     . VAL D 2 45  ? 5.944   8.416   31.502  1.00 32.99 ? 44  VAL C N     1 
ATOM   4193 C  CA    . VAL D 2 45  ? 5.864   7.515   32.643  1.00 34.20 ? 44  VAL C CA    1 
ATOM   4194 C  C     . VAL D 2 45  ? 4.398   7.440   33.032  1.00 35.52 ? 44  VAL C C     1 
ATOM   4195 O  O     . VAL D 2 45  ? 3.585   8.259   32.606  1.00 35.54 ? 44  VAL C O     1 
ATOM   4196 C  CB    . VAL D 2 45  ? 6.661   8.047   33.852  1.00 35.22 ? 44  VAL C CB    1 
ATOM   4197 C  CG1   . VAL D 2 45  ? 8.120   8.206   33.457  1.00 33.44 ? 44  VAL C CG1   1 
ATOM   4198 C  CG2   . VAL D 2 45  ? 6.097   9.420   34.292  1.00 34.82 ? 44  VAL C CG2   1 
ATOM   4199 N  N     . VAL D 2 46  ? 4.066   6.471   33.881  1.00 36.82 ? 45  VAL C N     1 
ATOM   4200 C  CA    . VAL D 2 46  ? 2.738   6.388   34.473  1.00 38.40 ? 45  VAL C CA    1 
ATOM   4201 C  C     . VAL D 2 46  ? 2.901   6.591   35.976  1.00 41.72 ? 45  VAL C C     1 
ATOM   4202 O  O     . VAL D 2 46  ? 3.704   5.905   36.610  1.00 45.45 ? 45  VAL C O     1 
ATOM   4203 C  CB    . VAL D 2 46  ? 2.054   5.046   34.158  1.00 40.11 ? 45  VAL C CB    1 
ATOM   4204 C  CG1   . VAL D 2 46  ? 0.642   5.030   34.732  1.00 41.17 ? 45  VAL C CG1   1 
ATOM   4205 C  CG2   . VAL D 2 46  ? 1.992   4.825   32.642  1.00 41.86 ? 45  VAL C CG2   1 
ATOM   4206 N  N     . ILE D 2 47  ? 2.177   7.552   36.530  1.00 40.32 ? 46  ILE C N     1 
ATOM   4207 C  CA    . ILE D 2 47  ? 2.244   7.880   37.943  1.00 41.55 ? 46  ILE C CA    1 
ATOM   4208 C  C     . ILE D 2 47  ? 0.833   7.791   38.485  1.00 43.47 ? 46  ILE C C     1 
ATOM   4209 O  O     . ILE D 2 47  ? -0.065  8.509   38.022  1.00 43.76 ? 46  ILE C O     1 
ATOM   4210 C  CB    . ILE D 2 47  ? 2.866   9.270   38.189  1.00 40.91 ? 46  ILE C CB    1 
ATOM   4211 C  CG1   . ILE D 2 47  ? 4.343   9.274   37.801  1.00 40.50 ? 46  ILE C CG1   1 
ATOM   4212 C  CG2   . ILE D 2 47  ? 2.695   9.668   39.657  1.00 42.99 ? 46  ILE C CG2   1 
ATOM   4213 C  CD1   . ILE D 2 47  ? 4.934   10.685  37.585  1.00 40.12 ? 46  ILE C CD1   1 
ATOM   4214 N  N     . ASP D 2 48  ? 0.629   6.874   39.429  1.00 44.96 ? 47  ASP C N     1 
ATOM   4215 C  CA    . ASP D 2 48  ? -0.693  6.647   40.019  1.00 47.09 ? 47  ASP C CA    1 
ATOM   4216 C  C     . ASP D 2 48  ? -1.734  6.422   38.931  1.00 47.20 ? 47  ASP C C     1 
ATOM   4217 O  O     . ASP D 2 48  ? -2.844  6.952   38.978  1.00 48.47 ? 47  ASP C O     1 
ATOM   4218 C  CB    . ASP D 2 48  ? -1.089  7.804   40.941  1.00 48.24 ? 47  ASP C CB    1 
ATOM   4219 C  CG    . ASP D 2 48  ? -0.106  7.998   42.075  1.00 48.44 ? 47  ASP C CG    1 
ATOM   4220 O  OD1   . ASP D 2 48  ? 0.586   7.023   42.452  1.00 48.45 ? 47  ASP C OD1   1 
ATOM   4221 O  OD2   . ASP D 2 48  ? -0.006  9.138   42.563  1.00 48.69 ? 47  ASP C OD2   1 
ATOM   4222 N  N     . GLY D 2 49  ? -1.349  5.652   37.918  1.00 45.99 ? 48  GLY C N     1 
ATOM   4223 C  CA    . GLY D 2 49  ? -2.275  5.233   36.897  1.00 46.30 ? 48  GLY C CA    1 
ATOM   4224 C  C     . GLY D 2 49  ? -2.460  6.187   35.738  1.00 48.97 ? 48  GLY C C     1 
ATOM   4225 O  O     . GLY D 2 49  ? -3.202  5.855   34.809  1.00 50.23 ? 48  GLY C O     1 
ATOM   4226 N  N     . GLU D 2 50  ? -1.823  7.353   35.750  1.00 43.94 ? 49  GLU C N     1 
ATOM   4227 C  CA    . GLU D 2 50  ? -2.059  8.357   34.724  1.00 45.35 ? 49  GLU C CA    1 
ATOM   4228 C  C     . GLU D 2 50  ? -0.758  8.528   33.937  1.00 44.16 ? 49  GLU C C     1 
ATOM   4229 O  O     . GLU D 2 50  ? 0.304   8.805   34.523  1.00 42.09 ? 49  GLU C O     1 
ATOM   4230 C  CB    . GLU D 2 50  ? -2.554  9.668   35.369  1.00 48.91 ? 49  GLU C CB    1 
ATOM   4231 C  CG    . GLU D 2 50  ? -2.676  10.894  34.421  1.00 50.54 ? 49  GLU C CG    1 
ATOM   4232 C  CD    . GLU D 2 50  ? -1.495  11.858  34.627  1.00 56.02 ? 49  GLU C CD    1 
ATOM   4233 O  OE1   . GLU D 2 50  ? -1.551  13.106  34.367  1.00 55.53 ? 49  GLU C OE1   1 
ATOM   4234 O  OE2   . GLU D 2 50  ? -0.448  11.332  35.066  1.00 56.36 ? 49  GLU C OE2   1 
ATOM   4235 N  N     . THR D 2 51  ? -0.818  8.325   32.612  1.00 41.12 ? 50  THR C N     1 
ATOM   4236 C  CA    . THR D 2 51  ? 0.368   8.531   31.793  1.00 40.95 ? 50  THR C CA    1 
ATOM   4237 C  C     . THR D 2 51  ? 0.670   10.018  31.749  1.00 44.07 ? 50  THR C C     1 
ATOM   4238 O  O     . THR D 2 51  ? -0.239  10.840  31.649  1.00 45.58 ? 50  THR C O     1 
ATOM   4239 C  CB    . THR D 2 51  ? 0.150   7.980   30.380  1.00 37.35 ? 50  THR C CB    1 
ATOM   4240 O  OG1   . THR D 2 51  ? -0.114  6.565   30.508  1.00 41.72 ? 50  THR C OG1   1 
ATOM   4241 C  CG2   . THR D 2 51  ? 1.386   8.178   29.500  1.00 40.09 ? 50  THR C CG2   1 
ATOM   4242 N  N     . CYS D 2 52  ? 1.942   10.373  31.914  1.00 36.02 ? 51  CYS C N     1 
ATOM   4243 C  CA    . CYS D 2 52  ? 2.343   11.758  31.719  1.00 37.82 ? 51  CYS C CA    1 
ATOM   4244 C  C     . CYS D 2 52  ? 3.746   11.880  31.146  1.00 36.16 ? 51  CYS C C     1 
ATOM   4245 O  O     . CYS D 2 52  ? 4.534   10.919  31.076  1.00 33.29 ? 51  CYS C O     1 
ATOM   4246 C  CB    . CYS D 2 52  ? 2.240   12.554  33.008  1.00 42.97 ? 51  CYS C CB    1 
ATOM   4247 S  SG    . CYS D 2 52  ? 3.192   11.849  34.320  1.00 49.85 ? 51  CYS C SG    1 
ATOM   4248 N  N     . LEU D 2 53  ? 4.039   13.100  30.730  1.00 33.09 ? 52  LEU C N     1 
ATOM   4249 C  CA    . LEU D 2 53  ? 5.316   13.441  30.096  1.00 31.66 ? 52  LEU C CA    1 
ATOM   4250 C  C     . LEU D 2 53  ? 6.087   14.290  31.098  1.00 35.70 ? 52  LEU C C     1 
ATOM   4251 O  O     . LEU D 2 53  ? 5.599   15.333  31.527  1.00 36.04 ? 52  LEU C O     1 
ATOM   4252 C  CB    . LEU D 2 53  ? 5.075   14.180  28.777  1.00 32.48 ? 52  LEU C CB    1 
ATOM   4253 C  CG    . LEU D 2 53  ? 6.145   14.391  27.698  1.00 34.06 ? 52  LEU C CG    1 
ATOM   4254 C  CD1   . LEU D 2 53  ? 7.080   15.522  28.038  1.00 37.66 ? 52  LEU C CD1   1 
ATOM   4255 C  CD2   . LEU D 2 53  ? 6.934   13.113  27.534  1.00 30.43 ? 52  LEU C CD2   1 
ATOM   4256 N  N     . LEU D 2 54  ? 7.267   13.827  31.512  1.00 34.16 ? 53  LEU C N     1 
ATOM   4257 C  CA    . LEU D 2 54  ? 8.151   14.654  32.339  1.00 31.80 ? 53  LEU C CA    1 
ATOM   4258 C  C     . LEU D 2 54  ? 9.112   15.424  31.455  1.00 32.17 ? 53  LEU C C     1 
ATOM   4259 O  O     . LEU D 2 54  ? 9.794   14.849  30.596  1.00 31.13 ? 53  LEU C O     1 
ATOM   4260 C  CB    . LEU D 2 54  ? 8.927   13.800  33.343  1.00 32.03 ? 53  LEU C CB    1 
ATOM   4261 C  CG    . LEU D 2 54  ? 8.029   12.899  34.180  1.00 34.91 ? 53  LEU C CG    1 
ATOM   4262 C  CD1   . LEU D 2 54  ? 8.812   12.066  35.182  1.00 33.79 ? 53  LEU C CD1   1 
ATOM   4263 C  CD2   . LEU D 2 54  ? 6.968   13.706  34.872  1.00 35.58 ? 53  LEU C CD2   1 
ATOM   4264 N  N     . ASP D 2 55  ? 9.147   16.730  31.652  1.00 30.86 ? 54  ASP C N     1 
ATOM   4265 C  CA    . ASP D 2 55  ? 10.114  17.611  31.018  1.00 31.31 ? 54  ASP C CA    1 
ATOM   4266 C  C     . ASP D 2 55  ? 10.998  18.108  32.141  1.00 32.95 ? 54  ASP C C     1 
ATOM   4267 O  O     . ASP D 2 55  ? 10.529  18.836  33.026  1.00 34.56 ? 54  ASP C O     1 
ATOM   4268 C  CB    . ASP D 2 55  ? 9.424   18.763  30.310  1.00 35.95 ? 54  ASP C CB    1 
ATOM   4269 C  CG    . ASP D 2 55  ? 10.402  19.636  29.573  1.00 37.99 ? 54  ASP C CG    1 
ATOM   4270 O  OD1   . ASP D 2 55  ? 11.197  20.374  30.214  1.00 43.45 ? 54  ASP C OD1   1 
ATOM   4271 O  OD2   . ASP D 2 55  ? 10.398  19.590  28.330  1.00 42.51 ? 54  ASP C OD2   1 
ATOM   4272 N  N     . ILE D 2 56  ? 12.261  17.712  32.109  1.00 32.87 ? 55  ILE C N     1 
ATOM   4273 C  CA    . ILE D 2 56  ? 13.178  17.881  33.232  1.00 32.02 ? 55  ILE C CA    1 
ATOM   4274 C  C     . ILE D 2 56  ? 14.310  18.770  32.809  1.00 31.05 ? 55  ILE C C     1 
ATOM   4275 O  O     . ILE D 2 56  ? 14.962  18.491  31.808  1.00 30.14 ? 55  ILE C O     1 
ATOM   4276 C  CB    . ILE D 2 56  ? 13.691  16.525  33.713  1.00 31.42 ? 55  ILE C CB    1 
ATOM   4277 C  CG1   . ILE D 2 56  ? 12.456  15.750  34.166  1.00 31.86 ? 55  ILE C CG1   1 
ATOM   4278 C  CG2   . ILE D 2 56  ? 14.680  16.644  34.905  1.00 32.68 ? 55  ILE C CG2   1 
ATOM   4279 C  CD1   . ILE D 2 56  ? 12.725  14.386  34.503  1.00 33.90 ? 55  ILE C CD1   1 
ATOM   4280 N  N     . LEU D 2 57  ? 14.533  19.835  33.569  1.00 32.04 ? 56  LEU C N     1 
ATOM   4281 C  CA    . LEU D 2 57  ? 15.643  20.739  33.331  1.00 32.18 ? 56  LEU C CA    1 
ATOM   4282 C  C     . LEU D 2 57  ? 16.705  20.484  34.393  1.00 33.18 ? 56  LEU C C     1 
ATOM   4283 O  O     . LEU D 2 57  ? 16.429  20.596  35.596  1.00 34.37 ? 56  LEU C O     1 
ATOM   4284 C  CB    . LEU D 2 57  ? 15.168  22.190  33.337  1.00 32.79 ? 56  LEU C CB    1 
ATOM   4285 C  CG    . LEU D 2 57  ? 16.285  23.149  32.953  1.00 34.48 ? 56  LEU C CG    1 
ATOM   4286 C  CD1   . LEU D 2 57  ? 16.431  23.315  31.363  1.00 31.74 ? 56  LEU C CD1   1 
ATOM   4287 C  CD2   . LEU D 2 57  ? 16.125  24.475  33.660  1.00 39.16 ? 56  LEU C CD2   1 
ATOM   4288 N  N     . ASP D 2 58  ? 17.899  20.105  33.944  1.00 32.89 ? 57  ASP C N     1 
ATOM   4289 C  CA    . ASP D 2 58  ? 19.038  19.801  34.787  1.00 33.96 ? 57  ASP C CA    1 
ATOM   4290 C  C     . ASP D 2 58  ? 19.928  21.030  34.732  1.00 34.66 ? 57  ASP C C     1 
ATOM   4291 O  O     . ASP D 2 58  ? 20.250  21.495  33.642  1.00 33.92 ? 57  ASP C O     1 
ATOM   4292 C  CB    . ASP D 2 58  ? 19.773  18.570  34.257  1.00 33.45 ? 57  ASP C CB    1 
ATOM   4293 C  CG    . ASP D 2 58  ? 20.999  18.175  35.114  1.00 34.83 ? 57  ASP C CG    1 
ATOM   4294 O  OD1   . ASP D 2 58  ? 21.050  18.560  36.296  1.00 36.14 ? 57  ASP C OD1   1 
ATOM   4295 O  OD2   . ASP D 2 58  ? 21.853  17.456  34.570  1.00 34.70 ? 57  ASP C OD2   1 
ATOM   4296 N  N     . THR D 2 59  ? 20.256  21.589  35.897  1.00 36.20 ? 58  THR C N     1 
ATOM   4297 C  CA    . THR D 2 59  ? 20.894  22.892  35.982  1.00 37.16 ? 58  THR C CA    1 
ATOM   4298 C  C     . THR D 2 59  ? 22.295  22.780  36.580  1.00 38.53 ? 58  THR C C     1 
ATOM   4299 O  O     . THR D 2 59  ? 22.679  21.738  37.152  1.00 40.56 ? 58  THR C O     1 
ATOM   4300 C  CB    . THR D 2 59  ? 20.053  23.863  36.794  1.00 41.31 ? 58  THR C CB    1 
ATOM   4301 O  OG1   . THR D 2 59  ? 20.036  23.426  38.161  1.00 39.45 ? 58  THR C OG1   1 
ATOM   4302 C  CG2   . THR D 2 59  ? 18.620  23.931  36.242  1.00 38.64 ? 58  THR C CG2   1 
ATOM   4303 N  N     . ALA D 2 60  ? 23.062  23.855  36.367  1.00 39.30 ? 59  ALA C N     1 
ATOM   4304 C  CA    . ALA D 2 60  ? 24.391  24.029  36.952  1.00 41.00 ? 59  ALA C CA    1 
ATOM   4305 C  C     . ALA D 2 60  ? 24.302  24.720  38.307  1.00 44.41 ? 59  ALA C C     1 
ATOM   4306 O  O     . ALA D 2 60  ? 23.561  25.695  38.471  1.00 43.11 ? 59  ALA C O     1 
ATOM   4307 C  CB    . ALA D 2 60  ? 25.291  24.858  36.034  1.00 41.15 ? 59  ALA C CB    1 
ATOM   4308 N  N     . GLY D 2 61  ? 25.119  24.248  39.254  1.00 48.78 ? 60  GLY C N     1 
ATOM   4309 C  CA    . GLY D 2 61  ? 25.249  24.878  40.553  1.00 49.20 ? 60  GLY C CA    1 
ATOM   4310 C  C     . GLY D 2 61  ? 26.437  25.809  40.773  1.00 53.17 ? 60  GLY C C     1 
ATOM   4311 O  O     . GLY D 2 61  ? 26.835  26.025  41.919  1.00 51.17 ? 60  GLY C O     1 
ATOM   4312 N  N     . GLN D 2 62  ? 26.996  26.375  39.703  1.00 56.75 ? 61  GLN C N     1 
ATOM   4313 C  CA    . GLN D 2 62  ? 28.045  27.396  39.817  1.00 59.57 ? 61  GLN C CA    1 
ATOM   4314 C  C     . GLN D 2 62  ? 27.500  28.681  40.441  1.00 60.02 ? 61  GLN C C     1 
ATOM   4315 O  O     . GLN D 2 62  ? 26.475  29.212  40.007  1.00 59.11 ? 61  GLN C O     1 
ATOM   4316 C  CB    . GLN D 2 62  ? 28.629  27.745  38.438  1.00 60.35 ? 61  GLN C CB    1 
ATOM   4317 C  CG    . GLN D 2 62  ? 28.869  26.575  37.474  1.00 55.49 ? 61  GLN C CG    1 
ATOM   4318 C  CD    . GLN D 2 62  ? 30.139  25.787  37.776  1.00 58.24 ? 61  GLN C CD    1 
ATOM   4319 O  OE1   . GLN D 2 62  ? 31.204  26.373  38.006  1.00 60.96 ? 61  GLN C OE1   1 
ATOM   4320 N  NE2   . GLN D 2 62  ? 30.034  24.466  37.783  1.00 61.60 ? 61  GLN C NE2   1 
ATOM   4321 N  N     . GLU D 2 63  ? 28.225  29.234  41.415  1.00 60.06 ? 62  GLU C N     1 
ATOM   4322 C  CA    . GLU D 2 63  ? 27.697  30.403  42.114  1.00 65.66 ? 62  GLU C CA    1 
ATOM   4323 C  C     . GLU D 2 63  ? 27.745  31.687  41.283  1.00 63.50 ? 62  GLU C C     1 
ATOM   4324 O  O     . GLU D 2 63  ? 26.935  32.597  41.527  1.00 58.22 ? 62  GLU C O     1 
ATOM   4325 C  CB    . GLU D 2 63  ? 28.435  30.563  43.448  1.00 68.82 ? 62  GLU C CB    1 
ATOM   4326 C  CG    . GLU D 2 63  ? 28.523  29.215  44.165  1.00 72.85 ? 62  GLU C CG    1 
ATOM   4327 C  CD    . GLU D 2 63  ? 28.555  29.301  45.691  1.00 80.65 ? 62  GLU C CD    1 
ATOM   4328 O  OE1   . GLU D 2 63  ? 28.124  30.328  46.270  1.00 82.94 ? 62  GLU C OE1   1 
ATOM   4329 O  OE2   . GLU D 2 63  ? 28.983  28.305  46.313  1.00 83.05 ? 62  GLU C OE2   1 
ATOM   4330 N  N     . GLU D 2 64  ? 28.637  31.766  40.281  1.00 64.32 ? 63  GLU C N     1 
ATOM   4331 C  CA    . GLU D 2 64  ? 28.709  32.964  39.448  1.00 60.43 ? 63  GLU C CA    1 
ATOM   4332 C  C     . GLU D 2 64  ? 27.409  33.212  38.689  1.00 57.89 ? 63  GLU C C     1 
ATOM   4333 O  O     . GLU D 2 64  ? 27.107  34.357  38.348  1.00 57.65 ? 63  GLU C O     1 
ATOM   4334 C  CB    . GLU D 2 64  ? 29.872  32.854  38.450  1.00 59.31 ? 63  GLU C CB    1 
ATOM   4335 C  CG    . GLU D 2 64  ? 31.247  32.858  39.123  1.00 67.02 ? 63  GLU C CG    1 
ATOM   4336 C  CD    . GLU D 2 64  ? 31.810  31.442  39.221  1.00 69.37 ? 63  GLU C CD    1 
ATOM   4337 O  OE1   . GLU D 2 64  ? 32.642  31.068  38.356  1.00 68.21 ? 63  GLU C OE1   1 
ATOM   4338 O  OE2   . GLU D 2 64  ? 31.330  30.665  40.082  1.00 72.32 ? 63  GLU C OE2   1 
ATOM   4339 N  N     . TYR D 2 65  ? 26.628  32.173  38.422  1.00 50.85 ? 64  TYR C N     1 
ATOM   4340 C  CA    . TYR D 2 65  ? 25.469  32.294  37.553  1.00 56.92 ? 64  TYR C CA    1 
ATOM   4341 C  C     . TYR D 2 65  ? 24.173  32.241  38.329  1.00 61.34 ? 64  TYR C C     1 
ATOM   4342 O  O     . TYR D 2 65  ? 23.105  32.166  37.713  1.00 61.00 ? 64  TYR C O     1 
ATOM   4343 C  CB    . TYR D 2 65  ? 25.510  31.199  36.478  1.00 46.64 ? 64  TYR C CB    1 
ATOM   4344 C  CG    . TYR D 2 65  ? 26.913  31.133  35.828  1.00 47.03 ? 64  TYR C CG    1 
ATOM   4345 C  CD1   . TYR D 2 65  ? 27.499  32.257  35.285  1.00 48.07 ? 64  TYR C CD1   1 
ATOM   4346 C  CD2   . TYR D 2 65  ? 27.633  29.952  35.809  1.00 46.63 ? 64  TYR C CD2   1 
ATOM   4347 C  CE1   . TYR D 2 65  ? 28.797  32.208  34.706  1.00 48.69 ? 64  TYR C CE1   1 
ATOM   4348 C  CE2   . TYR D 2 65  ? 28.886  29.887  35.246  1.00 47.25 ? 64  TYR C CE2   1 
ATOM   4349 C  CZ    . TYR D 2 65  ? 29.466  31.013  34.693  1.00 48.27 ? 64  TYR C CZ    1 
ATOM   4350 O  OH    . TYR D 2 65  ? 30.717  30.883  34.162  1.00 49.06 ? 64  TYR C OH    1 
ATOM   4351 N  N     . SER D 2 66  ? 24.248  32.305  39.667  1.00 57.58 ? 65  SER C N     1 
ATOM   4352 C  CA    . SER D 2 66  ? 23.046  32.225  40.498  1.00 64.12 ? 65  SER C CA    1 
ATOM   4353 C  C     . SER D 2 66  ? 22.026  33.296  40.123  1.00 66.82 ? 65  SER C C     1 
ATOM   4354 O  O     . SER D 2 66  ? 20.820  33.082  40.285  1.00 67.92 ? 65  SER C O     1 
ATOM   4355 C  CB    . SER D 2 66  ? 23.406  32.325  41.987  1.00 60.94 ? 65  SER C CB    1 
ATOM   4356 O  OG    . SER D 2 66  ? 24.403  33.300  42.258  1.00 61.57 ? 65  SER C OG    1 
ATOM   4357 N  N     . ALA D 2 67  ? 22.483  34.432  39.594  1.00 64.88 ? 66  ALA C N     1 
ATOM   4358 C  CA    . ALA D 2 67  ? 21.559  35.447  39.099  1.00 65.02 ? 66  ALA C CA    1 
ATOM   4359 C  C     . ALA D 2 67  ? 20.616  34.866  38.050  1.00 66.36 ? 66  ALA C C     1 
ATOM   4360 O  O     . ALA D 2 67  ? 19.393  34.886  38.227  1.00 67.90 ? 66  ALA C O     1 
ATOM   4361 C  CB    . ALA D 2 67  ? 22.340  36.642  38.548  1.00 68.05 ? 66  ALA C CB    1 
ATOM   4362 N  N     . MET D 2 68  ? 21.168  34.296  36.964  1.00 63.11 ? 67  MET C N     1 
ATOM   4363 C  CA    . MET D 2 68  ? 20.330  33.809  35.864  1.00 63.48 ? 67  MET C CA    1 
ATOM   4364 C  C     . MET D 2 68  ? 19.501  32.587  36.231  1.00 67.20 ? 67  MET C C     1 
ATOM   4365 O  O     . MET D 2 68  ? 18.600  32.228  35.468  1.00 66.27 ? 67  MET C O     1 
ATOM   4366 C  CB    . MET D 2 68  ? 21.160  33.414  34.656  1.00 61.86 ? 67  MET C CB    1 
ATOM   4367 C  CG    . MET D 2 68  ? 22.404  34.232  34.455  1.00 62.87 ? 67  MET C CG    1 
ATOM   4368 S  SD    . MET D 2 68  ? 22.875  34.073  32.748  1.00 68.24 ? 67  MET C SD    1 
ATOM   4369 C  CE    . MET D 2 68  ? 21.729  35.216  31.936  1.00 60.97 ? 67  MET C CE    1 
ATOM   4370 N  N     . ARG D 2 69  ? 19.842  31.898  37.332  1.00 68.98 ? 68  ARG C N     1 
ATOM   4371 C  CA    . ARG D 2 69  ? 19.055  30.766  37.808  1.00 66.26 ? 68  ARG C CA    1 
ATOM   4372 C  C     . ARG D 2 69  ? 17.604  31.153  38.015  1.00 67.55 ? 68  ARG C C     1 
ATOM   4373 O  O     . ARG D 2 69  ? 16.721  30.282  37.967  1.00 66.59 ? 68  ARG C O     1 
ATOM   4374 C  CB    . ARG D 2 69  ? 19.638  30.220  39.116  1.00 65.93 ? 68  ARG C CB    1 
ATOM   4375 N  N     . ASP D 2 70  ? 17.351  32.446  38.229  1.00 68.87 ? 69  ASP C N     1 
ATOM   4376 C  CA    . ASP D 2 70  ? 15.995  32.954  38.383  1.00 70.40 ? 69  ASP C CA    1 
ATOM   4377 C  C     . ASP D 2 70  ? 15.106  32.585  37.197  1.00 71.48 ? 69  ASP C C     1 
ATOM   4378 O  O     . ASP D 2 70  ? 13.928  32.262  37.382  1.00 71.01 ? 69  ASP C O     1 
ATOM   4379 C  CB    . ASP D 2 70  ? 16.028  34.476  38.591  1.00 71.34 ? 69  ASP C CB    1 
ATOM   4380 C  CG    . ASP D 2 70  ? 16.706  34.891  39.904  1.00 71.38 ? 69  ASP C CG    1 
ATOM   4381 O  OD1   . ASP D 2 70  ? 17.358  34.046  40.572  1.00 65.61 ? 69  ASP C OD1   1 
ATOM   4382 O  OD2   . ASP D 2 70  ? 16.542  36.079  40.286  1.00 77.01 ? 69  ASP C OD2   1 
ATOM   4383 N  N     . GLN D 2 71  ? 15.644  32.605  35.980  1.00 67.57 ? 70  GLN C N     1 
ATOM   4384 C  CA    . GLN D 2 71  ? 14.792  32.472  34.799  1.00 71.19 ? 70  GLN C CA    1 
ATOM   4385 C  C     . GLN D 2 71  ? 14.126  31.097  34.724  1.00 69.71 ? 70  GLN C C     1 
ATOM   4386 O  O     . GLN D 2 71  ? 12.902  30.986  34.575  1.00 69.92 ? 70  GLN C O     1 
ATOM   4387 C  CB    . GLN D 2 71  ? 15.610  32.751  33.538  1.00 72.33 ? 70  GLN C CB    1 
ATOM   4388 C  CG    . GLN D 2 71  ? 14.889  32.435  32.230  1.00 75.13 ? 70  GLN C CG    1 
ATOM   4389 C  CD    . GLN D 2 71  ? 13.400  32.740  32.280  1.00 74.05 ? 70  GLN C CD    1 
ATOM   4390 O  OE1   . GLN D 2 71  ? 12.564  31.844  32.102  1.00 72.67 ? 70  GLN C OE1   1 
ATOM   4391 N  NE2   . GLN D 2 71  ? 13.059  33.994  32.549  1.00 75.21 ? 70  GLN C NE2   1 
ATOM   4392 N  N     . TYR D 2 72  ? 14.913  30.031  34.781  1.00 67.96 ? 71  TYR C N     1 
ATOM   4393 C  CA    . TYR D 2 72  ? 14.287  28.722  34.763  1.00 63.05 ? 71  TYR C CA    1 
ATOM   4394 C  C     . TYR D 2 72  ? 13.424  28.521  35.994  1.00 63.16 ? 71  TYR C C     1 
ATOM   4395 O  O     . TYR D 2 72  ? 12.526  27.664  35.996  1.00 59.34 ? 71  TYR C O     1 
ATOM   4396 C  CB    . TYR D 2 72  ? 15.346  27.639  34.670  1.00 57.84 ? 71  TYR C CB    1 
ATOM   4397 C  CG    . TYR D 2 72  ? 16.303  27.554  35.839  1.00 56.06 ? 71  TYR C CG    1 
ATOM   4398 C  CD1   . TYR D 2 72  ? 15.862  27.144  37.095  1.00 59.49 ? 71  TYR C CD1   1 
ATOM   4399 C  CD2   . TYR D 2 72  ? 17.658  27.837  35.676  1.00 55.26 ? 71  TYR C CD2   1 
ATOM   4400 C  CE1   . TYR D 2 72  ? 16.729  27.050  38.184  1.00 58.86 ? 71  TYR C CE1   1 
ATOM   4401 C  CE2   . TYR D 2 72  ? 18.546  27.734  36.752  1.00 55.72 ? 71  TYR C CE2   1 
ATOM   4402 C  CZ    . TYR D 2 72  ? 18.069  27.343  38.013  1.00 60.93 ? 71  TYR C CZ    1 
ATOM   4403 O  OH    . TYR D 2 72  ? 18.892  27.227  39.129  1.00 63.92 ? 71  TYR C OH    1 
ATOM   4404 N  N     . MET D 2 73  ? 13.697  29.281  37.050  1.00 62.87 ? 72  MET C N     1 
ATOM   4405 C  CA    . MET D 2 73  ? 12.911  29.141  38.257  1.00 62.37 ? 72  MET C CA    1 
ATOM   4406 C  C     . MET D 2 73  ? 11.504  29.631  37.991  1.00 61.13 ? 72  MET C C     1 
ATOM   4407 O  O     . MET D 2 73  ? 10.537  29.096  38.550  1.00 61.40 ? 72  MET C O     1 
ATOM   4408 C  CB    . MET D 2 73  ? 13.586  29.912  39.378  1.00 60.21 ? 72  MET C CB    1 
ATOM   4409 C  CG    . MET D 2 73  ? 14.540  29.045  40.189  1.00 58.76 ? 72  MET C CG    1 
ATOM   4410 S  SD    . MET D 2 73  ? 15.349  30.038  41.459  1.00 66.84 ? 72  MET C SD    1 
ATOM   4411 C  CE    . MET D 2 73  ? 16.522  28.897  42.160  1.00 57.44 ? 72  MET C CE    1 
ATOM   4412 N  N     . ARG D 2 74  ? 11.374  30.588  37.074  1.00 61.94 ? 73  ARG C N     1 
ATOM   4413 C  CA    . ARG D 2 74  ? 10.054  31.024  36.639  1.00 65.19 ? 73  ARG C CA    1 
ATOM   4414 C  C     . ARG D 2 74  ? 9.309   29.886  35.978  1.00 58.96 ? 73  ARG C C     1 
ATOM   4415 O  O     . ARG D 2 74  ? 8.170   29.588  36.343  1.00 60.16 ? 73  ARG C O     1 
ATOM   4416 C  CB    . ARG D 2 74  ? 10.149  32.223  35.683  1.00 64.73 ? 73  ARG C CB    1 
ATOM   4417 C  CG    . ARG D 2 74  ? 10.457  33.584  36.359  1.00 66.12 ? 73  ARG C CG    1 
ATOM   4418 C  CD    . ARG D 2 74  ? 11.848  34.119  35.974  1.00 72.51 ? 73  ARG C CD    1 
ATOM   4419 N  NE    . ARG D 2 74  ? 12.376  35.152  36.872  1.00 72.64 ? 73  ARG C NE    1 
ATOM   4420 C  CZ    . ARG D 2 74  ? 13.533  35.778  36.682  1.00 72.98 ? 73  ARG C CZ    1 
ATOM   4421 N  NH1   . ARG D 2 74  ? 14.272  35.547  35.615  1.00 69.15 ? 73  ARG C NH1   1 
ATOM   4422 N  NH2   . ARG D 2 74  ? 13.952  36.672  37.577  1.00 75.38 ? 73  ARG C NH2   1 
ATOM   4423 N  N     . THR D 2 75  ? 9.945   29.229  35.006  1.00 59.78 ? 74  THR C N     1 
ATOM   4424 C  CA    . THR D 2 75  ? 9.279   28.209  34.208  1.00 58.51 ? 74  THR C CA    1 
ATOM   4425 C  C     . THR D 2 75  ? 9.071   26.881  34.945  1.00 52.10 ? 74  THR C C     1 
ATOM   4426 O  O     . THR D 2 75  ? 8.167   26.125  34.583  1.00 56.25 ? 74  THR C O     1 
ATOM   4427 C  CB    . THR D 2 75  ? 10.077  27.965  32.931  1.00 61.80 ? 74  THR C CB    1 
ATOM   4428 O  OG1   . THR D 2 75  ? 11.465  28.027  33.253  1.00 64.15 ? 74  THR C OG1   1 
ATOM   4429 C  CG2   . THR D 2 75  ? 9.766   29.035  31.893  1.00 61.35 ? 74  THR C CG2   1 
ATOM   4430 N  N     . GLY D 2 76  ? 9.867   26.567  35.964  1.00 52.28 ? 75  GLY C N     1 
ATOM   4431 C  CA    . GLY D 2 76  ? 9.751   25.262  36.613  1.00 52.10 ? 75  GLY C CA    1 
ATOM   4432 C  C     . GLY D 2 76  ? 8.600   25.195  37.612  1.00 54.97 ? 75  GLY C C     1 
ATOM   4433 O  O     . GLY D 2 76  ? 8.310   26.155  38.330  1.00 56.28 ? 75  GLY C O     1 
ATOM   4434 N  N     . GLU D 2 77  ? 7.956   24.018  37.669  1.00 52.61 ? 76  GLU C N     1 
ATOM   4435 C  CA    . GLU D 2 77  ? 6.851   23.775  38.601  1.00 48.15 ? 76  GLU C CA    1 
ATOM   4436 C  C     . GLU D 2 77  ? 7.250   23.011  39.849  1.00 50.69 ? 76  GLU C C     1 
ATOM   4437 O  O     . GLU D 2 77  ? 6.478   22.990  40.818  1.00 51.82 ? 76  GLU C O     1 
ATOM   4438 C  CB    . GLU D 2 77  ? 5.744   23.021  37.900  1.00 50.66 ? 76  GLU C CB    1 
ATOM   4439 C  CG    . GLU D 2 77  ? 5.115   23.874  36.865  1.00 51.82 ? 76  GLU C CG    1 
ATOM   4440 C  CD    . GLU D 2 77  ? 4.605   23.037  35.768  1.00 54.49 ? 76  GLU C CD    1 
ATOM   4441 O  OE1   . GLU D 2 77  ? 4.933   21.817  35.759  1.00 55.14 ? 76  GLU C OE1   1 
ATOM   4442 O  OE2   . GLU D 2 77  ? 3.936   23.582  34.854  1.00 56.14 ? 76  GLU C OE2   1 
ATOM   4443 N  N     . GLY D 2 78  ? 8.431   22.423  39.873  1.00 45.52 ? 77  GLY C N     1 
ATOM   4444 C  CA    . GLY D 2 78  ? 8.856   21.682  41.039  1.00 48.02 ? 77  GLY C CA    1 
ATOM   4445 C  C     . GLY D 2 78  ? 10.344  21.454  40.979  1.00 49.90 ? 77  GLY C C     1 
ATOM   4446 O  O     . GLY D 2 78  ? 10.941  21.404  39.889  1.00 44.59 ? 77  GLY C O     1 
ATOM   4447 N  N     . PHE D 2 79  ? 10.934  21.255  42.158  1.00 48.30 ? 78  PHE C N     1 
ATOM   4448 C  CA    . PHE D 2 79  ? 12.370  21.326  42.308  1.00 42.59 ? 78  PHE C CA    1 
ATOM   4449 C  C     . PHE D 2 79  ? 12.869  20.163  43.149  1.00 47.71 ? 78  PHE C C     1 
ATOM   4450 O  O     . PHE D 2 79  ? 12.439  19.984  44.299  1.00 52.89 ? 78  PHE C O     1 
ATOM   4451 C  CB    . PHE D 2 79  ? 12.705  22.685  42.913  1.00 48.95 ? 78  PHE C CB    1 
ATOM   4452 C  CG    . PHE D 2 79  ? 12.236  23.806  42.041  1.00 50.86 ? 78  PHE C CG    1 
ATOM   4453 C  CD1   . PHE D 2 79  ? 10.904  24.217  42.054  1.00 44.34 ? 78  PHE C CD1   1 
ATOM   4454 C  CD2   . PHE D 2 79  ? 13.094  24.362  41.102  1.00 49.27 ? 78  PHE C CD2   1 
ATOM   4455 C  CE1   . PHE D 2 79  ? 10.464  25.213  41.172  1.00 44.77 ? 78  PHE C CE1   1 
ATOM   4456 C  CE2   . PHE D 2 79  ? 12.662  25.355  40.249  1.00 48.67 ? 78  PHE C CE2   1 
ATOM   4457 C  CZ    . PHE D 2 79  ? 11.354  25.771  40.277  1.00 48.13 ? 78  PHE C CZ    1 
ATOM   4458 N  N     . LEU D 2 80  ? 13.741  19.349  42.547  1.00 47.11 ? 79  LEU C N     1 
ATOM   4459 C  CA    . LEU D 2 80  ? 14.463  18.300  43.261  1.00 49.25 ? 79  LEU C CA    1 
ATOM   4460 C  C     . LEU D 2 80  ? 15.760  18.897  43.827  1.00 47.13 ? 79  LEU C C     1 
ATOM   4461 O  O     . LEU D 2 80  ? 16.702  19.179  43.092  1.00 43.69 ? 79  LEU C O     1 
ATOM   4462 C  CB    . LEU D 2 80  ? 14.732  17.132  42.314  1.00 45.53 ? 79  LEU C CB    1 
ATOM   4463 C  CG    . LEU D 2 80  ? 14.912  15.782  42.992  1.00 48.65 ? 79  LEU C CG    1 
ATOM   4464 C  CD1   . LEU D 2 80  ? 13.553  15.237  43.381  1.00 46.30 ? 79  LEU C CD1   1 
ATOM   4465 C  CD2   . LEU D 2 80  ? 15.645  14.766  42.140  1.00 42.61 ? 79  LEU C CD2   1 
ATOM   4466 N  N     . CYS D 2 81  ? 15.822  19.103  45.133  1.00 48.98 ? 80  CYS C N     1 
ATOM   4467 C  CA    . CYS D 2 81  ? 16.981  19.757  45.751  1.00 46.99 ? 80  CYS C CA    1 
ATOM   4468 C  C     . CYS D 2 81  ? 17.960  18.693  46.253  1.00 48.79 ? 80  CYS C C     1 
ATOM   4469 O  O     . CYS D 2 81  ? 17.703  18.034  47.277  1.00 49.07 ? 80  CYS C O     1 
ATOM   4470 C  CB    . CYS D 2 81  ? 16.495  20.677  46.869  1.00 51.98 ? 80  CYS C CB    1 
ATOM   4471 S  SG    . CYS D 2 81  ? 15.391  21.948  46.169  1.00 50.21 ? 80  CYS C SG    1 
ATOM   4472 N  N     . VAL D 2 82  ? 19.083  18.522  45.529  1.00 47.01 ? 81  VAL C N     1 
ATOM   4473 C  CA    . VAL D 2 82  ? 20.006  17.407  45.766  1.00 47.60 ? 81  VAL C CA    1 
ATOM   4474 C  C     . VAL D 2 82  ? 21.232  17.884  46.568  1.00 49.62 ? 81  VAL C C     1 
ATOM   4475 O  O     . VAL D 2 82  ? 21.855  18.912  46.245  1.00 49.73 ? 81  VAL C O     1 
ATOM   4476 C  CB    . VAL D 2 82  ? 20.420  16.738  44.430  1.00 47.53 ? 81  VAL C CB    1 
ATOM   4477 C  CG1   . VAL D 2 82  ? 21.230  15.450  44.651  1.00 46.49 ? 81  VAL C CG1   1 
ATOM   4478 C  CG2   . VAL D 2 82  ? 19.188  16.437  43.507  1.00 43.77 ? 81  VAL C CG2   1 
ATOM   4479 N  N     . PHE D 2 83  ? 21.569  17.149  47.644  1.00 51.44 ? 82  PHE C N     1 
ATOM   4480 C  CA    . PHE D 2 83  ? 22.894  17.217  48.277  1.00 53.45 ? 82  PHE C CA    1 
ATOM   4481 C  C     . PHE D 2 83  ? 23.469  15.800  48.326  1.00 53.97 ? 82  PHE C C     1 
ATOM   4482 O  O     . PHE D 2 83  ? 22.792  14.827  47.979  1.00 52.78 ? 82  PHE C O     1 
ATOM   4483 C  CB    . PHE D 2 83  ? 22.847  17.858  49.674  1.00 55.87 ? 82  PHE C CB    1 
ATOM   4484 C  CG    . PHE D 2 83  ? 22.348  16.919  50.765  1.00 58.25 ? 82  PHE C CG    1 
ATOM   4485 C  CD1   . PHE D 2 83  ? 20.980  16.703  50.930  1.00 56.58 ? 82  PHE C CD1   1 
ATOM   4486 C  CD2   . PHE D 2 83  ? 23.239  16.280  51.635  1.00 59.48 ? 82  PHE C CD2   1 
ATOM   4487 C  CE1   . PHE D 2 83  ? 20.499  15.841  51.928  1.00 57.99 ? 82  PHE C CE1   1 
ATOM   4488 C  CE2   . PHE D 2 83  ? 22.762  15.407  52.627  1.00 60.88 ? 82  PHE C CE2   1 
ATOM   4489 C  CZ    . PHE D 2 83  ? 21.388  15.189  52.771  1.00 60.10 ? 82  PHE C CZ    1 
ATOM   4490 N  N     . ALA D 2 84  ? 24.739  15.677  48.714  1.00 55.70 ? 83  ALA C N     1 
ATOM   4491 C  CA    . ALA D 2 84  ? 25.413  14.381  48.765  1.00 56.51 ? 83  ALA C CA    1 
ATOM   4492 C  C     . ALA D 2 84  ? 25.808  14.074  50.206  1.00 59.44 ? 83  ALA C C     1 
ATOM   4493 O  O     . ALA D 2 84  ? 26.402  14.925  50.886  1.00 61.22 ? 83  ALA C O     1 
ATOM   4494 C  CB    . ALA D 2 84  ? 26.645  14.345  47.855  1.00 56.34 ? 83  ALA C CB    1 
ATOM   4495 N  N     . ILE D 2 85  ? 25.492  12.850  50.650  1.00 60.07 ? 84  ILE C N     1 
ATOM   4496 C  CA    . ILE D 2 85  ? 25.580  12.496  52.064  1.00 62.79 ? 84  ILE C CA    1 
ATOM   4497 C  C     . ILE D 2 85  ? 27.017  12.401  52.557  1.00 66.65 ? 84  ILE C C     1 
ATOM   4498 O  O     . ILE D 2 85  ? 27.236  12.186  53.751  1.00 67.95 ? 84  ILE C O     1 
ATOM   4499 C  CB    . ILE D 2 85  ? 24.817  11.179  52.353  1.00 62.84 ? 84  ILE C CB    1 
ATOM   4500 C  CG1   . ILE D 2 85  ? 25.356  10.000  51.525  1.00 64.47 ? 84  ILE C CG1   1 
ATOM   4501 C  CG2   . ILE D 2 85  ? 23.321  11.350  52.063  1.00 60.81 ? 84  ILE C CG2   1 
ATOM   4502 C  CD1   . ILE D 2 85  ? 26.540  9.228   52.160  1.00 65.11 ? 84  ILE C CD1   1 
ATOM   4503 N  N     . ASN D 2 86  ? 28.000  12.549  51.668  1.00 64.91 ? 85  ASN C N     1 
ATOM   4504 C  CA    . ASN D 2 86  ? 29.395  12.686  52.063  1.00 70.03 ? 85  ASN C CA    1 
ATOM   4505 C  C     . ASN D 2 86  ? 29.927  14.099  51.838  1.00 67.53 ? 85  ASN C C     1 
ATOM   4506 O  O     . ASN D 2 86  ? 31.149  14.295  51.863  1.00 69.35 ? 85  ASN C O     1 
ATOM   4507 C  CB    . ASN D 2 86  ? 30.281  11.670  51.323  1.00 69.08 ? 85  ASN C CB    1 
ATOM   4508 C  CG    . ASN D 2 86  ? 30.550  12.060  49.858  1.00 66.59 ? 85  ASN C CG    1 
ATOM   4509 O  OD1   . ASN D 2 86  ? 29.683  12.615  49.176  1.00 62.74 ? 85  ASN C OD1   1 
ATOM   4510 N  ND2   . ASN D 2 86  ? 31.773  11.787  49.389  1.00 66.50 ? 85  ASN C ND2   1 
ATOM   4511 N  N     . ASN D 2 87  ? 29.050  15.087  51.639  1.00 65.83 ? 86  ASN C N     1 
ATOM   4512 C  CA    . ASN D 2 87  ? 29.462  16.467  51.345  1.00 65.80 ? 86  ASN C CA    1 
ATOM   4513 C  C     . ASN D 2 87  ? 28.616  17.404  52.214  1.00 66.33 ? 86  ASN C C     1 
ATOM   4514 O  O     . ASN D 2 87  ? 27.533  17.834  51.807  1.00 64.28 ? 86  ASN C O     1 
ATOM   4515 C  CB    . ASN D 2 87  ? 29.294  16.740  49.833  1.00 64.89 ? 86  ASN C CB    1 
ATOM   4516 C  CG    . ASN D 2 87  ? 29.911  18.054  49.378  1.00 63.04 ? 86  ASN C CG    1 
ATOM   4517 O  OD1   . ASN D 2 87  ? 30.170  18.958  50.165  1.00 64.83 ? 86  ASN C OD1   1 
ATOM   4518 N  ND2   . ASN D 2 87  ? 30.125  18.162  48.070  1.00 64.01 ? 86  ASN C ND2   1 
ATOM   4519 N  N     . THR D 2 88  ? 29.097  17.707  53.424  1.00 69.29 ? 87  THR C N     1 
ATOM   4520 C  CA    . THR D 2 88  ? 28.375  18.652  54.280  1.00 70.17 ? 87  THR C CA    1 
ATOM   4521 C  C     . THR D 2 88  ? 28.150  20.002  53.591  1.00 70.31 ? 87  THR C C     1 
ATOM   4522 O  O     . THR D 2 88  ? 27.060  20.582  53.700  1.00 67.93 ? 87  THR C O     1 
ATOM   4523 C  CB    . THR D 2 88  ? 29.104  18.839  55.615  1.00 73.83 ? 87  THR C CB    1 
ATOM   4524 O  OG1   . THR D 2 88  ? 29.071  17.599  56.332  1.00 75.10 ? 87  THR C OG1   1 
ATOM   4525 C  CG2   . THR D 2 88  ? 28.424  19.925  56.442  1.00 74.91 ? 87  THR C CG2   1 
ATOM   4526 N  N     . LYS D 2 89  ? 29.159  20.509  52.865  1.00 68.82 ? 88  LYS C N     1 
ATOM   4527 C  CA    . LYS D 2 89  ? 29.017  21.785  52.162  1.00 67.71 ? 88  LYS C CA    1 
ATOM   4528 C  C     . LYS D 2 89  ? 27.769  21.793  51.277  1.00 64.55 ? 88  LYS C C     1 
ATOM   4529 O  O     . LYS D 2 89  ? 26.952  22.720  51.341  1.00 64.14 ? 88  LYS C O     1 
ATOM   4530 C  CB    . LYS D 2 89  ? 30.276  22.077  51.333  1.00 67.91 ? 88  LYS C CB    1 
ATOM   4531 C  CG    . LYS D 2 89  ? 30.208  23.349  50.508  1.00 66.82 ? 88  LYS C CG    1 
ATOM   4532 C  CD    . LYS D 2 89  ? 31.545  23.637  49.782  1.00 69.17 ? 88  LYS C CD    1 
ATOM   4533 C  CE    . LYS D 2 89  ? 32.676  23.938  50.757  1.00 72.16 ? 88  LYS C CE    1 
ATOM   4534 N  NZ    . LYS D 2 89  ? 33.962  24.291  50.076  1.00 73.16 ? 88  LYS C NZ    1 
ATOM   4535 N  N     . SER D 2 90  ? 27.588  20.744  50.465  1.00 63.58 ? 89  SER C N     1 
ATOM   4536 C  CA    . SER D 2 90  ? 26.408  20.686  49.601  1.00 63.98 ? 89  SER C CA    1 
ATOM   4537 C  C     . SER D 2 90  ? 25.125  20.625  50.429  1.00 59.83 ? 89  SER C C     1 
ATOM   4538 O  O     . SER D 2 90  ? 24.063  21.042  49.961  1.00 58.20 ? 89  SER C O     1 
ATOM   4539 C  CB    . SER D 2 90  ? 26.494  19.487  48.641  1.00 57.78 ? 89  SER C CB    1 
ATOM   4540 O  OG    . SER D 2 90  ? 26.330  18.236  49.323  1.00 58.53 ? 89  SER C OG    1 
ATOM   4541 N  N     . PHE D 2 91  ? 25.220  20.166  51.681  1.00 64.85 ? 90  PHE C N     1 
ATOM   4542 C  CA    . PHE D 2 91  ? 24.048  20.160  52.555  1.00 66.64 ? 90  PHE C CA    1 
ATOM   4543 C  C     . PHE D 2 91  ? 23.738  21.574  53.051  1.00 63.80 ? 90  PHE C C     1 
ATOM   4544 O  O     . PHE D 2 91  ? 22.574  21.997  53.064  1.00 64.19 ? 90  PHE C O     1 
ATOM   4545 C  CB    . PHE D 2 91  ? 24.286  19.190  53.726  1.00 64.78 ? 90  PHE C CB    1 
ATOM   4546 C  CG    . PHE D 2 91  ? 23.080  18.955  54.617  1.00 66.51 ? 90  PHE C CG    1 
ATOM   4547 C  CD1   . PHE D 2 91  ? 21.838  18.628  54.094  1.00 64.38 ? 90  PHE C CD1   1 
ATOM   4548 C  CD2   . PHE D 2 91  ? 23.195  19.081  55.992  1.00 68.32 ? 90  PHE C CD2   1 
ATOM   4549 C  CE1   . PHE D 2 91  ? 20.742  18.410  54.939  1.00 64.26 ? 90  PHE C CE1   1 
ATOM   4550 C  CE2   . PHE D 2 91  ? 22.103  18.865  56.832  1.00 69.41 ? 90  PHE C CE2   1 
ATOM   4551 C  CZ    . PHE D 2 91  ? 20.883  18.540  56.305  1.00 67.13 ? 90  PHE C CZ    1 
ATOM   4552 N  N     . GLU D 2 92  ? 24.767  22.322  53.448  1.00 70.62 ? 91  GLU C N     1 
ATOM   4553 C  CA    . GLU D 2 92  ? 24.564  23.712  53.850  1.00 68.34 ? 91  GLU C CA    1 
ATOM   4554 C  C     . GLU D 2 92  ? 24.066  24.559  52.681  1.00 69.47 ? 91  GLU C C     1 
ATOM   4555 O  O     . GLU D 2 92  ? 23.217  25.443  52.862  1.00 69.47 ? 91  GLU C O     1 
ATOM   4556 C  CB    . GLU D 2 92  ? 25.857  24.266  54.410  1.00 72.03 ? 91  GLU C CB    1 
ATOM   4557 C  CG    . GLU D 2 92  ? 26.696  23.210  55.120  1.00 78.40 ? 91  GLU C CG    1 
ATOM   4558 C  CD    . GLU D 2 92  ? 27.968  23.772  55.716  1.00 79.11 ? 91  GLU C CD    1 
ATOM   4559 O  OE1   . GLU D 2 92  ? 28.909  24.049  54.940  1.00 78.64 ? 91  GLU C OE1   1 
ATOM   4560 O  OE2   . GLU D 2 92  ? 28.046  23.901  56.958  1.00 84.53 ? 91  GLU C OE2   1 
ATOM   4561 N  N     . ASP D 2 93  ? 24.574  24.290  51.471  1.00 62.87 ? 92  ASP C N     1 
ATOM   4562 C  CA    . ASP D 2 93  ? 24.088  24.969  50.279  1.00 64.91 ? 92  ASP C CA    1 
ATOM   4563 C  C     . ASP D 2 93  ? 22.592  24.776  50.048  1.00 65.01 ? 92  ASP C C     1 
ATOM   4564 O  O     . ASP D 2 93  ? 21.985  25.582  49.327  1.00 66.77 ? 92  ASP C O     1 
ATOM   4565 C  CB    . ASP D 2 93  ? 24.828  24.474  49.024  1.00 63.87 ? 92  ASP C CB    1 
ATOM   4566 C  CG    . ASP D 2 93  ? 26.301  24.892  48.996  1.00 63.42 ? 92  ASP C CG    1 
ATOM   4567 O  OD1   . ASP D 2 93  ? 26.675  25.832  49.726  1.00 63.11 ? 92  ASP C OD1   1 
ATOM   4568 O  OD2   . ASP D 2 93  ? 27.066  24.251  48.247  1.00 60.04 ? 92  ASP C OD2   1 
ATOM   4569 N  N     . ILE D 2 94  ? 21.990  23.723  50.601  1.00 59.03 ? 93  ILE C N     1 
ATOM   4570 C  CA    . ILE D 2 94  ? 20.583  23.464  50.328  1.00 62.32 ? 93  ILE C CA    1 
ATOM   4571 C  C     . ILE D 2 94  ? 19.728  24.623  50.844  1.00 66.48 ? 93  ILE C C     1 
ATOM   4572 O  O     . ILE D 2 94  ? 18.917  25.195  50.104  1.00 62.08 ? 93  ILE C O     1 
ATOM   4573 C  CB    . ILE D 2 94  ? 20.157  22.108  50.934  1.00 61.38 ? 93  ILE C CB    1 
ATOM   4574 C  CG1   . ILE D 2 94  ? 20.805  20.914  50.176  1.00 56.21 ? 93  ILE C CG1   1 
ATOM   4575 C  CG2   . ILE D 2 94  ? 18.630  22.020  51.065  1.00 59.47 ? 93  ILE C CG2   1 
ATOM   4576 C  CD1   . ILE D 2 94  ? 20.110  20.392  48.905  1.00 53.45 ? 93  ILE C CD1   1 
ATOM   4577 N  N     . HIS D 2 95  ? 19.907  25.001  52.120  1.00 63.02 ? 94  HIS C N     1 
ATOM   4578 C  CA    . HIS D 2 95  ? 19.205  26.174  52.639  1.00 69.18 ? 94  HIS C CA    1 
ATOM   4579 C  C     . HIS D 2 95  ? 19.246  27.345  51.646  1.00 73.06 ? 94  HIS C C     1 
ATOM   4580 O  O     . HIS D 2 95  ? 18.211  27.965  51.360  1.00 70.66 ? 94  HIS C O     1 
ATOM   4581 C  CB    . HIS D 2 95  ? 19.809  26.617  53.959  1.00 74.21 ? 94  HIS C CB    1 
ATOM   4582 C  CG    . HIS D 2 95  ? 19.335  27.965  54.398  1.00 79.50 ? 94  HIS C CG    1 
ATOM   4583 N  ND1   . HIS D 2 95  ? 20.023  29.126  54.112  1.00 79.66 ? 94  HIS C ND1   1 
ATOM   4584 C  CD2   . HIS D 2 95  ? 18.256  28.338  55.129  1.00 81.95 ? 94  HIS C CD2   1 
ATOM   4585 C  CE1   . HIS D 2 95  ? 19.381  30.157  54.632  1.00 76.51 ? 94  HIS C CE1   1 
ATOM   4586 N  NE2   . HIS D 2 95  ? 18.307  29.708  55.254  1.00 80.13 ? 94  HIS C NE2   1 
ATOM   4587 N  N     . HIS D 2 96  ? 20.433  27.647  51.088  1.00 69.15 ? 95  HIS C N     1 
ATOM   4588 C  CA    . HIS D 2 96  ? 20.526  28.760  50.148  1.00 70.18 ? 95  HIS C CA    1 
ATOM   4589 C  C     . HIS D 2 96  ? 19.679  28.508  48.912  1.00 66.09 ? 95  HIS C C     1 
ATOM   4590 O  O     . HIS D 2 96  ? 19.025  29.418  48.395  1.00 68.30 ? 95  HIS C O     1 
ATOM   4591 C  CB    . HIS D 2 96  ? 21.989  29.027  49.763  1.00 70.99 ? 95  HIS C CB    1 
ATOM   4592 C  CG    . HIS D 2 96  ? 22.838  29.435  50.922  1.00 75.89 ? 95  HIS C CG    1 
ATOM   4593 N  ND1   . HIS D 2 96  ? 22.832  30.718  51.428  1.00 74.17 ? 95  HIS C ND1   1 
ATOM   4594 C  CD2   . HIS D 2 96  ? 23.683  28.725  51.706  1.00 77.19 ? 95  HIS C CD2   1 
ATOM   4595 C  CE1   . HIS D 2 96  ? 23.648  30.782  52.465  1.00 78.27 ? 95  HIS C CE1   1 
ATOM   4596 N  NE2   . HIS D 2 96  ? 24.178  29.588  52.654  1.00 77.95 ? 95  HIS C NE2   1 
ATOM   4597 N  N     . TYR D 2 97  ? 19.687  27.283  48.421  1.00 65.28 ? 96  TYR C N     1 
ATOM   4598 C  CA    . TYR D 2 97  ? 18.863  26.947  47.266  1.00 66.57 ? 96  TYR C CA    1 
ATOM   4599 C  C     . TYR D 2 97  ? 17.377  27.109  47.584  1.00 66.00 ? 96  TYR C C     1 
ATOM   4600 O  O     . TYR D 2 97  ? 16.590  27.537  46.724  1.00 62.95 ? 96  TYR C O     1 
ATOM   4601 C  CB    . TYR D 2 97  ? 19.212  25.524  46.813  1.00 65.00 ? 96  TYR C CB    1 
ATOM   4602 C  CG    . TYR D 2 97  ? 20.236  25.487  45.690  1.00 62.31 ? 96  TYR C CG    1 
ATOM   4603 C  CD1   . TYR D 2 97  ? 21.413  24.756  45.827  1.00 63.17 ? 96  TYR C CD1   1 
ATOM   4604 C  CD2   . TYR D 2 97  ? 19.958  26.043  44.450  1.00 63.54 ? 96  TYR C CD2   1 
ATOM   4605 C  CE1   . TYR D 2 97  ? 22.343  24.713  44.824  1.00 58.62 ? 96  TYR C CE1   1 
ATOM   4606 C  CE2   . TYR D 2 97  ? 20.869  25.993  43.427  1.00 59.01 ? 96  TYR C CE2   1 
ATOM   4607 C  CZ    . TYR D 2 97  ? 22.054  25.307  43.611  1.00 62.37 ? 96  TYR C CZ    1 
ATOM   4608 O  OH    . TYR D 2 97  ? 22.969  25.248  42.583  1.00 59.54 ? 96  TYR C OH    1 
ATOM   4609 N  N     . ARG D 2 98  ? 16.978  26.806  48.826  1.00 66.42 ? 97  ARG C N     1 
ATOM   4610 C  CA    . ARG D 2 98  ? 15.563  26.894  49.150  1.00 63.05 ? 97  ARG C CA    1 
ATOM   4611 C  C     . ARG D 2 98  ? 15.136  28.344  49.219  1.00 64.26 ? 97  ARG C C     1 
ATOM   4612 O  O     . ARG D 2 98  ? 14.115  28.730  48.636  1.00 63.88 ? 97  ARG C O     1 
ATOM   4613 C  CB    . ARG D 2 98  ? 15.252  26.194  50.467  1.00 62.81 ? 97  ARG C CB    1 
ATOM   4614 C  CG    . ARG D 2 98  ? 13.748  26.149  50.691  1.00 58.52 ? 97  ARG C CG    1 
ATOM   4615 C  CD    . ARG D 2 98  ? 13.354  25.427  51.969  1.00 64.72 ? 97  ARG C CD    1 
ATOM   4616 N  NE    . ARG D 2 98  ? 11.905  25.346  52.104  1.00 62.27 ? 97  ARG C NE    1 
ATOM   4617 C  CZ    . ARG D 2 98  ? 11.183  26.026  52.977  1.00 69.11 ? 97  ARG C CZ    1 
ATOM   4618 N  NH1   . ARG D 2 98  ? 11.741  26.905  53.797  1.00 69.79 ? 97  ARG C NH1   1 
ATOM   4619 N  NH2   . ARG D 2 98  ? 9.866   25.834  53.012  1.00 67.43 ? 97  ARG C NH2   1 
ATOM   4620 N  N     . GLU D 2 99  ? 15.923  29.160  49.928  1.00 67.35 ? 98  GLU C N     1 
ATOM   4621 C  CA    . GLU D 2 99  ? 15.650  30.582  50.057  1.00 63.12 ? 98  GLU C CA    1 
ATOM   4622 C  C     . GLU D 2 99  ? 15.445  31.230  48.690  1.00 68.98 ? 98  GLU C C     1 
ATOM   4623 O  O     . GLU D 2 99  ? 14.423  31.895  48.462  1.00 67.95 ? 98  GLU C O     1 
ATOM   4624 C  CB    . GLU D 2 99  ? 16.799  31.231  50.822  1.00 72.62 ? 98  GLU C CB    1 
ATOM   4625 C  CG    . GLU D 2 99  ? 16.643  31.243  52.368  1.00 73.55 ? 98  GLU C CG    1 
ATOM   4626 C  CD    . GLU D 2 99  ? 15.247  31.594  52.858  1.00 73.08 ? 98  GLU C CD    1 
ATOM   4627 O  OE1   . GLU D 2 99  ? 14.942  32.802  52.878  1.00 72.12 ? 98  GLU C OE1   1 
ATOM   4628 O  OE2   . GLU D 2 99  ? 14.461  30.692  53.238  1.00 70.96 ? 98  GLU C OE2   1 
ATOM   4629 N  N     . GLN D 2 100 ? 16.378  30.997  47.740  1.00 62.69 ? 99  GLN C N     1 
ATOM   4630 C  CA    . GLN D 2 100 ? 16.265  31.648  46.445  1.00 60.05 ? 99  GLN C CA    1 
ATOM   4631 C  C     . GLN D 2 100 ? 15.030  31.165  45.692  1.00 65.92 ? 99  GLN C C     1 
ATOM   4632 O  O     . GLN D 2 100 ? 14.324  31.974  45.075  1.00 66.31 ? 99  GLN C O     1 
ATOM   4633 C  CB    . GLN D 2 100 ? 17.524  31.413  45.599  1.00 65.88 ? 99  GLN C CB    1 
ATOM   4634 C  CG    . GLN D 2 100 ? 17.355  31.758  44.074  1.00 68.81 ? 99  GLN C CG    1 
ATOM   4635 C  CD    . GLN D 2 100 ? 18.617  32.343  43.403  1.00 70.19 ? 99  GLN C CD    1 
ATOM   4636 O  OE1   . GLN D 2 100 ? 19.333  31.669  42.640  1.00 66.08 ? 99  GLN C OE1   1 
ATOM   4637 N  NE2   . GLN D 2 100 ? 18.911  33.599  43.730  1.00 75.79 ? 99  GLN C NE2   1 
ATOM   4638 N  N     . ILE D 2 101 ? 14.749  29.855  45.713  1.00 57.95 ? 100 ILE C N     1 
ATOM   4639 C  CA    . ILE D 2 101 ? 13.568  29.367  45.009  1.00 59.31 ? 100 ILE C CA    1 
ATOM   4640 C  C     . ILE D 2 101 ? 12.312  30.009  45.588  1.00 66.94 ? 100 ILE C C     1 
ATOM   4641 O  O     . ILE D 2 101 ? 11.428  30.468  44.848  1.00 66.44 ? 100 ILE C O     1 
ATOM   4642 C  CB    . ILE D 2 101 ? 13.485  27.828  45.057  1.00 61.69 ? 100 ILE C CB    1 
ATOM   4643 C  CG1   . ILE D 2 101 ? 14.483  27.223  44.088  1.00 57.27 ? 100 ILE C CG1   1 
ATOM   4644 C  CG2   . ILE D 2 101 ? 12.084  27.341  44.658  1.00 59.28 ? 100 ILE C CG2   1 
ATOM   4645 C  CD1   . ILE D 2 101 ? 14.695  25.773  44.189  1.00 57.57 ? 100 ILE C CD1   1 
ATOM   4646 N  N     . LYS D 2 102 ? 12.217  30.055  46.921  1.00 56.67 ? 101 LYS C N     1 
ATOM   4647 C  CA    . LYS D 2 102 ? 11.070  30.706  47.527  1.00 64.89 ? 101 LYS C CA    1 
ATOM   4648 C  C     . LYS D 2 102 ? 11.007  32.180  47.149  1.00 66.81 ? 101 LYS C C     1 
ATOM   4649 O  O     . LYS D 2 102 ? 9.911   32.732  46.987  1.00 70.43 ? 101 LYS C O     1 
ATOM   4650 C  CB    . LYS D 2 102 ? 11.107  30.522  49.050  1.00 66.94 ? 101 LYS C CB    1 
ATOM   4651 C  CG    . LYS D 2 102 ? 10.784  29.074  49.470  1.00 65.77 ? 101 LYS C CG    1 
ATOM   4652 C  CD    . LYS D 2 102 ? 10.574  28.947  50.961  1.00 70.72 ? 101 LYS C CD    1 
ATOM   4653 C  CE    . LYS D 2 102 ? 11.845  29.254  51.715  1.00 69.79 ? 101 LYS C CE    1 
ATOM   4654 N  NZ    . LYS D 2 102 ? 11.485  29.888  52.984  1.00 72.07 ? 101 LYS C NZ    1 
ATOM   4655 N  N     . ARG D 2 103 ? 12.155  32.828  46.985  1.00 65.01 ? 102 ARG C N     1 
ATOM   4656 C  CA    . ARG D 2 103 ? 12.152  34.195  46.493  1.00 63.63 ? 102 ARG C CA    1 
ATOM   4657 C  C     . ARG D 2 103 ? 11.521  34.246  45.107  1.00 65.81 ? 102 ARG C C     1 
ATOM   4658 O  O     . ARG D 2 103 ? 10.397  34.740  44.950  1.00 66.19 ? 102 ARG C O     1 
ATOM   4659 C  CB    . ARG D 2 103 ? 13.575  34.756  46.458  1.00 69.18 ? 102 ARG C CB    1 
ATOM   4660 C  CG    . ARG D 2 103 ? 13.646  36.264  46.268  1.00 68.68 ? 102 ARG C CG    1 
ATOM   4661 C  CD    . ARG D 2 103 ? 14.985  36.717  45.730  1.00 65.01 ? 102 ARG C CD    1 
ATOM   4662 N  NE    . ARG D 2 103 ? 14.937  36.986  44.293  1.00 73.40 ? 102 ARG C NE    1 
ATOM   4663 C  CZ    . ARG D 2 103 ? 14.041  37.759  43.681  1.00 71.53 ? 102 ARG C CZ    1 
ATOM   4664 N  NH1   . ARG D 2 103 ? 13.114  38.429  44.357  1.00 68.49 ? 102 ARG C NH1   1 
ATOM   4665 N  NH2   . ARG D 2 103 ? 14.069  37.855  42.353  1.00 67.63 ? 102 ARG C NH2   1 
ATOM   4666 N  N     . VAL D 2 104 ? 12.231  33.697  44.107  1.00 68.77 ? 103 VAL C N     1 
ATOM   4667 C  CA    . VAL D 2 104 ? 11.870  33.879  42.699  1.00 57.34 ? 103 VAL C CA    1 
ATOM   4668 C  C     . VAL D 2 104 ? 10.411  33.509  42.433  1.00 64.51 ? 103 VAL C C     1 
ATOM   4669 O  O     . VAL D 2 104 ? 9.704   34.216  41.702  1.00 66.48 ? 103 VAL C O     1 
ATOM   4670 C  CB    . VAL D 2 104 ? 12.831  33.082  41.799  1.00 64.17 ? 103 VAL C CB    1 
ATOM   4671 C  CG1   . VAL D 2 104 ? 12.449  33.268  40.332  1.00 64.18 ? 103 VAL C CG1   1 
ATOM   4672 C  CG2   . VAL D 2 104 ? 14.284  33.520  42.043  1.00 66.26 ? 103 VAL C CG2   1 
ATOM   4673 N  N     . LYS D 2 105 ? 9.939   32.397  43.015  1.00 62.62 ? 104 LYS C N     1 
ATOM   4674 C  CA    . LYS D 2 105 ? 8.542   31.997  42.900  1.00 64.10 ? 104 LYS C CA    1 
ATOM   4675 C  C     . LYS D 2 105 ? 7.591   32.864  43.740  1.00 67.91 ? 104 LYS C C     1 
ATOM   4676 O  O     . LYS D 2 105 ? 6.377   32.828  43.513  1.00 69.71 ? 104 LYS C O     1 
ATOM   4677 C  CB    . LYS D 2 105 ? 8.389   30.539  43.339  1.00 66.71 ? 104 LYS C CB    1 
ATOM   4678 C  CG    . LYS D 2 105 ? 9.348   29.550  42.669  1.00 56.83 ? 104 LYS C CG    1 
ATOM   4679 C  CD    . LYS D 2 105 ? 9.103   29.383  41.217  1.00 61.16 ? 104 LYS C CD    1 
ATOM   4680 C  CE    . LYS D 2 105 ? 7.800   28.666  40.917  1.00 57.45 ? 104 LYS C CE    1 
ATOM   4681 N  NZ    . LYS D 2 105 ? 7.554   28.685  39.433  1.00 57.43 ? 104 LYS C NZ    1 
ATOM   4682 N  N     . ASP D 2 106 ? 8.093   33.619  44.711  1.00 62.94 ? 105 ASP C N     1 
ATOM   4683 C  CA    . ASP D 2 106 ? 7.241   34.424  45.597  1.00 71.12 ? 105 ASP C CA    1 
ATOM   4684 C  C     . ASP D 2 106 ? 6.130   33.570  46.235  1.00 74.39 ? 105 ASP C C     1 
ATOM   4685 O  O     . ASP D 2 106 ? 4.933   33.827  46.076  1.00 72.67 ? 105 ASP C O     1 
ATOM   4686 C  CB    . ASP D 2 106 ? 6.651   35.625  44.834  1.00 71.04 ? 105 ASP C CB    1 
ATOM   4687 C  CG    . ASP D 2 106 ? 5.897   36.612  45.733  1.00 75.94 ? 105 ASP C CG    1 
ATOM   4688 O  OD1   . ASP D 2 106 ? 6.513   37.206  46.659  1.00 79.22 ? 105 ASP C OD1   1 
ATOM   4689 O  OD2   . ASP D 2 106 ? 4.669   36.781  45.526  1.00 73.57 ? 105 ASP C OD2   1 
ATOM   4690 N  N     . SER D 2 107 ? 6.544   32.514  46.937  1.00 73.45 ? 106 SER C N     1 
ATOM   4691 C  CA    . SER D 2 107 ? 5.632   31.757  47.793  1.00 75.60 ? 106 SER C CA    1 
ATOM   4692 C  C     . SER D 2 107 ? 6.451   31.131  48.910  1.00 77.60 ? 106 SER C C     1 
ATOM   4693 O  O     . SER D 2 107 ? 7.676   31.005  48.809  1.00 76.60 ? 106 SER C O     1 
ATOM   4694 C  CB    . SER D 2 107 ? 4.855   30.672  47.022  1.00 71.44 ? 106 SER C CB    1 
ATOM   4695 O  OG    . SER D 2 107 ? 3.711   30.209  47.751  1.00 63.53 ? 106 SER C OG    1 
ATOM   4696 N  N     . GLU D 2 108 ? 5.757   30.743  49.981  1.00 79.56 ? 107 GLU C N     1 
ATOM   4697 C  CA    . GLU D 2 108 ? 6.409   29.966  51.025  1.00 80.57 ? 107 GLU C CA    1 
ATOM   4698 C  C     . GLU D 2 108 ? 6.482   28.479  50.675  1.00 79.26 ? 107 GLU C C     1 
ATOM   4699 O  O     . GLU D 2 108 ? 7.463   27.816  51.027  1.00 80.18 ? 107 GLU C O     1 
ATOM   4700 C  CB    . GLU D 2 108 ? 5.692   30.174  52.352  1.00 82.60 ? 107 GLU C CB    1 
ATOM   4701 C  CG    . GLU D 2 108 ? 6.240   31.347  53.138  1.00 80.04 ? 107 GLU C CG    1 
ATOM   4702 C  CD    . GLU D 2 108 ? 7.695   31.156  53.530  1.00 81.51 ? 107 GLU C CD    1 
ATOM   4703 O  OE1   . GLU D 2 108 ? 7.995   30.197  54.265  1.00 85.86 ? 107 GLU C OE1   1 
ATOM   4704 O  OE2   . GLU D 2 108 ? 8.543   31.962  53.109  1.00 81.39 ? 107 GLU C OE2   1 
ATOM   4705 N  N     . ASP D 2 109 ? 5.494   27.935  49.972  1.00 76.38 ? 108 ASP C N     1 
ATOM   4706 C  CA    . ASP D 2 109 ? 5.491   26.507  49.658  1.00 76.54 ? 108 ASP C CA    1 
ATOM   4707 C  C     . ASP D 2 109 ? 5.494   26.314  48.140  1.00 70.63 ? 108 ASP C C     1 
ATOM   4708 O  O     . ASP D 2 109 ? 4.477   26.480  47.465  1.00 71.03 ? 108 ASP C O     1 
ATOM   4709 C  CB    . ASP D 2 109 ? 4.346   25.756  50.390  1.00 78.91 ? 108 ASP C CB    1 
ATOM   4710 C  CG    . ASP D 2 109 ? 2.938   26.071  49.875  1.00 78.08 ? 108 ASP C CG    1 
ATOM   4711 O  OD1   . ASP D 2 109 ? 2.732   27.070  49.159  1.00 79.54 ? 108 ASP C OD1   1 
ATOM   4712 O  OD2   . ASP D 2 109 ? 2.017   25.288  50.204  1.00 81.85 ? 108 ASP C OD2   1 
ATOM   4713 N  N     . VAL D 2 110 ? 6.669   25.999  47.608  1.00 68.21 ? 109 VAL C N     1 
ATOM   4714 C  CA    . VAL D 2 110 ? 6.860   25.621  46.204  1.00 65.53 ? 109 VAL C CA    1 
ATOM   4715 C  C     . VAL D 2 110 ? 6.923   24.098  46.175  1.00 60.75 ? 109 VAL C C     1 
ATOM   4716 O  O     . VAL D 2 110 ? 7.451   23.500  47.127  1.00 62.02 ? 109 VAL C O     1 
ATOM   4717 C  CB    . VAL D 2 110 ? 8.132   26.271  45.619  1.00 61.75 ? 109 VAL C CB    1 
ATOM   4718 C  CG1   . VAL D 2 110 ? 9.351   25.919  46.448  1.00 60.22 ? 109 VAL C CG1   1 
ATOM   4719 C  CG2   . VAL D 2 110 ? 8.367   25.835  44.176  1.00 57.33 ? 109 VAL C CG2   1 
ATOM   4720 N  N     . PRO D 2 111 ? 6.358   23.426  45.172  1.00 58.61 ? 110 PRO C N     1 
ATOM   4721 C  CA    . PRO D 2 111 ? 6.558   21.976  45.071  1.00 55.71 ? 110 PRO C CA    1 
ATOM   4722 C  C     . PRO D 2 111 ? 8.050   21.640  45.082  1.00 50.29 ? 110 PRO C C     1 
ATOM   4723 O  O     . PRO D 2 111 ? 8.819   22.147  44.257  1.00 53.75 ? 110 PRO C O     1 
ATOM   4724 C  CB    . PRO D 2 111 ? 5.901   21.628  43.730  1.00 59.14 ? 110 PRO C CB    1 
ATOM   4725 C  CG    . PRO D 2 111 ? 4.914   22.739  43.472  1.00 55.93 ? 110 PRO C CG    1 
ATOM   4726 C  CD    . PRO D 2 111 ? 5.464   23.955  44.116  1.00 58.34 ? 110 PRO C CD    1 
ATOM   4727 N  N     . MET D 2 112 ? 8.458   20.752  46.001  1.00 50.87 ? 111 MET C N     1 
ATOM   4728 C  CA    . MET D 2 112 ? 9.872   20.651  46.329  1.00 51.56 ? 111 MET C CA    1 
ATOM   4729 C  C     . MET D 2 112 ? 10.186  19.380  47.104  1.00 52.15 ? 111 MET C C     1 
ATOM   4730 O  O     . MET D 2 112 ? 9.396   18.954  47.952  1.00 55.73 ? 111 MET C O     1 
ATOM   4731 C  CB    . MET D 2 112 ? 10.268  21.896  47.131  1.00 56.12 ? 111 MET C CB    1 
ATOM   4732 C  CG    . MET D 2 112 ? 11.688  21.997  47.581  1.00 61.25 ? 111 MET C CG    1 
ATOM   4733 S  SD    . MET D 2 112 ? 12.090  23.756  47.835  1.00 64.18 ? 111 MET C SD    1 
ATOM   4734 C  CE    . MET D 2 112 ? 12.754  24.066  46.183  1.00 55.50 ? 111 MET C CE    1 
ATOM   4735 N  N     . VAL D 2 113 ? 11.373  18.814  46.863  1.00 52.98 ? 112 VAL C N     1 
ATOM   4736 C  CA    . VAL D 2 113 ? 11.787  17.552  47.490  1.00 57.42 ? 112 VAL C CA    1 
ATOM   4737 C  C     . VAL D 2 113 ? 13.291  17.546  47.784  1.00 55.82 ? 112 VAL C C     1 
ATOM   4738 O  O     . VAL D 2 113 ? 14.105  17.694  46.867  1.00 53.94 ? 112 VAL C O     1 
ATOM   4739 C  CB    . VAL D 2 113 ? 11.424  16.348  46.597  1.00 56.76 ? 112 VAL C CB    1 
ATOM   4740 C  CG1   . VAL D 2 113 ? 11.947  15.065  47.200  1.00 54.27 ? 112 VAL C CG1   1 
ATOM   4741 C  CG2   . VAL D 2 113 ? 9.928   16.269  46.392  1.00 50.99 ? 112 VAL C CG2   1 
ATOM   4742 N  N     . LEU D 2 114 ? 13.662  17.301  49.040  1.00 51.97 ? 113 LEU C N     1 
ATOM   4743 C  CA    . LEU D 2 114 ? 15.072  17.157  49.402  1.00 55.30 ? 113 LEU C CA    1 
ATOM   4744 C  C     . LEU D 2 114 ? 15.594  15.739  49.144  1.00 54.60 ? 113 LEU C C     1 
ATOM   4745 O  O     . LEU D 2 114 ? 14.955  14.743  49.514  1.00 55.33 ? 113 LEU C O     1 
ATOM   4746 C  CB    . LEU D 2 114 ? 15.273  17.497  50.888  1.00 54.61 ? 113 LEU C CB    1 
ATOM   4747 C  CG    . LEU D 2 114 ? 16.696  17.476  51.471  1.00 55.71 ? 113 LEU C CG    1 
ATOM   4748 C  CD1   . LEU D 2 114 ? 17.496  18.663  51.030  1.00 55.46 ? 113 LEU C CD1   1 
ATOM   4749 C  CD2   . LEU D 2 114 ? 16.672  17.414  53.023  1.00 58.52 ? 113 LEU C CD2   1 
ATOM   4750 N  N     . VAL D 2 115 ? 16.800  15.650  48.582  1.00 50.52 ? 114 VAL C N     1 
ATOM   4751 C  CA    . VAL D 2 115 ? 17.405  14.379  48.176  1.00 50.00 ? 114 VAL C CA    1 
ATOM   4752 C  C     . VAL D 2 115 ? 18.815  14.259  48.753  1.00 53.03 ? 114 VAL C C     1 
ATOM   4753 O  O     . VAL D 2 115 ? 19.719  15.008  48.362  1.00 51.34 ? 114 VAL C O     1 
ATOM   4754 C  CB    . VAL D 2 115 ? 17.460  14.245  46.642  1.00 47.60 ? 114 VAL C CB    1 
ATOM   4755 C  CG1   . VAL D 2 115 ? 17.893  12.816  46.240  1.00 47.25 ? 114 VAL C CG1   1 
ATOM   4756 C  CG2   . VAL D 2 115 ? 16.146  14.641  46.067  1.00 46.33 ? 114 VAL C CG2   1 
ATOM   4757 N  N     . GLY D 2 116 ? 19.012  13.307  49.653  1.00 53.19 ? 115 GLY C N     1 
ATOM   4758 C  CA    . GLY D 2 116 ? 20.369  12.980  50.026  1.00 54.63 ? 115 GLY C CA    1 
ATOM   4759 C  C     . GLY D 2 116 ? 20.955  11.881  49.154  1.00 53.72 ? 115 GLY C C     1 
ATOM   4760 O  O     . GLY D 2 116 ? 20.601  10.705  49.326  1.00 54.05 ? 115 GLY C O     1 
ATOM   4761 N  N     . ASN D 2 117 ? 21.885  12.219  48.262  1.00 52.84 ? 116 ASN C N     1 
ATOM   4762 C  CA    . ASN D 2 117 ? 22.378  11.236  47.304  1.00 52.06 ? 116 ASN C CA    1 
ATOM   4763 C  C     . ASN D 2 117 ? 23.751  10.687  47.692  1.00 53.89 ? 116 ASN C C     1 
ATOM   4764 O  O     . ASN D 2 117 ? 24.431  11.189  48.598  1.00 55.87 ? 116 ASN C O     1 
ATOM   4765 C  CB    . ASN D 2 117 ? 22.413  11.831  45.881  1.00 52.30 ? 116 ASN C CB    1 
ATOM   4766 C  CG    . ASN D 2 117 ? 22.811  10.803  44.786  1.00 51.21 ? 116 ASN C CG    1 
ATOM   4767 O  OD1   . ASN D 2 117 ? 22.218  9.711   44.655  1.00 48.26 ? 116 ASN C OD1   1 
ATOM   4768 N  ND2   . ASN D 2 117 ? 23.850  11.168  43.996  1.00 51.60 ? 116 ASN C ND2   1 
ATOM   4769 N  N     . LYS D 2 118 ? 24.132  9.627   46.956  1.00 53.46 ? 117 LYS C N     1 
ATOM   4770 C  CA    . LYS D 2 118 ? 25.337  8.810   47.138  1.00 55.33 ? 117 LYS C CA    1 
ATOM   4771 C  C     . LYS D 2 118 ? 25.248  7.923   48.371  1.00 57.66 ? 117 LYS C C     1 
ATOM   4772 O  O     . LYS D 2 118 ? 26.272  7.522   48.914  1.00 59.94 ? 117 LYS C O     1 
ATOM   4773 C  CB    . LYS D 2 118 ? 26.630  9.650   47.173  1.00 56.48 ? 117 LYS C CB    1 
ATOM   4774 C  CG    . LYS D 2 118 ? 26.768  10.559  45.967  1.00 54.39 ? 117 LYS C CG    1 
ATOM   4775 C  CD    . LYS D 2 118 ? 28.078  11.284  45.954  1.00 55.72 ? 117 LYS C CD    1 
ATOM   4776 C  CE    . LYS D 2 118 ? 28.164  12.267  44.802  1.00 53.78 ? 117 LYS C CE    1 
ATOM   4777 N  NZ    . LYS D 2 118 ? 29.592  12.768  44.709  1.00 55.40 ? 117 LYS C NZ    1 
ATOM   4778 N  N     . CYS D 2 119 ? 24.049  7.572   48.789  1.00 57.28 ? 118 CYS C N     1 
ATOM   4779 C  CA    . CYS D 2 119 ? 23.941  6.791   50.028  1.00 59.69 ? 118 CYS C CA    1 
ATOM   4780 C  C     . CYS D 2 119 ? 24.596  5.379   49.922  1.00 61.06 ? 118 CYS C C     1 
ATOM   4781 O  O     . CYS D 2 119 ? 24.468  4.588   50.880  1.00 63.13 ? 118 CYS C O     1 
ATOM   4782 C  CB    . CYS D 2 119 ? 22.471  6.674   50.418  1.00 59.05 ? 118 CYS C CB    1 
ATOM   4783 S  SG    . CYS D 2 119 ? 21.476  5.549   49.320  1.00 65.64 ? 118 CYS C SG    1 
ATOM   4784 N  N     . ASP D 2 120 ? 25.282  5.024   48.822  1.00 60.22 ? 119 ASP C N     1 
ATOM   4785 C  CA    . ASP D 2 120 ? 26.079  3.792   48.757  1.00 61.96 ? 119 ASP C CA    1 
ATOM   4786 C  C     . ASP D 2 120 ? 27.432  3.914   49.461  1.00 65.91 ? 119 ASP C C     1 
ATOM   4787 O  O     . ASP D 2 120 ? 28.014  2.889   49.846  1.00 67.06 ? 119 ASP C O     1 
ATOM   4788 C  CB    . ASP D 2 120 ? 26.344  3.348   47.298  1.00 60.29 ? 119 ASP C CB    1 
ATOM   4789 C  CG    . ASP D 2 120 ? 26.986  4.447   46.434  1.00 58.86 ? 119 ASP C CG    1 
ATOM   4790 O  OD1   . ASP D 2 120 ? 26.250  5.308   45.937  1.00 58.07 ? 119 ASP C OD1   1 
ATOM   4791 O  OD2   . ASP D 2 120 ? 28.232  4.475   46.281  1.00 60.72 ? 119 ASP C OD2   1 
ATOM   4792 N  N     . LEU D 2 121 ? 27.934  5.130   49.644  1.00 64.81 ? 120 LEU C N     1 
ATOM   4793 C  CA    . LEU D 2 121 ? 29.287  5.312   50.128  1.00 70.88 ? 120 LEU C CA    1 
ATOM   4794 C  C     . LEU D 2 121 ? 29.417  4.835   51.577  1.00 77.74 ? 120 LEU C C     1 
ATOM   4795 O  O     . LEU D 2 121 ? 28.490  5.015   52.376  1.00 76.38 ? 120 LEU C O     1 
ATOM   4796 C  CB    . LEU D 2 121 ? 29.666  6.786   50.000  1.00 72.45 ? 120 LEU C CB    1 
ATOM   4797 C  CG    . LEU D 2 121 ? 29.842  7.253   48.553  1.00 65.87 ? 120 LEU C CG    1 
ATOM   4798 C  CD1   . LEU D 2 121 ? 30.134  8.751   48.499  1.00 63.83 ? 120 LEU C CD1   1 
ATOM   4799 C  CD2   . LEU D 2 121 ? 30.936  6.452   47.864  1.00 65.30 ? 120 LEU C CD2   1 
ATOM   4800 N  N     . PRO D 2 122 ? 30.542  4.195   51.940  1.00 80.86 ? 121 PRO C N     1 
ATOM   4801 C  CA    . PRO D 2 122 ? 30.763  3.844   53.360  1.00 86.04 ? 121 PRO C CA    1 
ATOM   4802 C  C     . PRO D 2 122 ? 30.987  5.059   54.241  1.00 87.05 ? 121 PRO C C     1 
ATOM   4803 O  O     . PRO D 2 122 ? 30.786  4.985   55.462  1.00 88.68 ? 121 PRO C O     1 
ATOM   4804 C  CB    . PRO D 2 122 ? 32.017  2.955   53.322  1.00 87.76 ? 121 PRO C CB    1 
ATOM   4805 C  CG    . PRO D 2 122 ? 32.748  3.378   52.045  1.00 81.17 ? 121 PRO C CG    1 
ATOM   4806 C  CD    . PRO D 2 122 ? 31.653  3.762   51.068  1.00 75.84 ? 121 PRO C CD    1 
ATOM   4807 N  N     . SER D 2 123 ? 31.451  6.158   53.658  1.00 86.81 ? 122 SER C N     1 
ATOM   4808 C  CA    . SER D 2 123 ? 31.563  7.423   54.358  1.00 85.89 ? 122 SER C CA    1 
ATOM   4809 C  C     . SER D 2 123 ? 30.197  8.096   54.411  1.00 85.97 ? 122 SER C C     1 
ATOM   4810 O  O     . SER D 2 123 ? 29.388  7.967   53.489  1.00 82.84 ? 122 SER C O     1 
ATOM   4811 C  CB    . SER D 2 123 ? 32.563  8.331   53.639  1.00 89.77 ? 122 SER C CB    1 
ATOM   4812 O  OG    . SER D 2 123 ? 32.332  8.334   52.224  1.00 84.25 ? 122 SER C OG    1 
ATOM   4813 N  N     . ARG D 2 124 ? 29.935  8.794   55.507  1.00 82.08 ? 123 ARG C N     1 
ATOM   4814 C  CA    . ARG D 2 124 ? 28.774  9.657   55.644  1.00 75.73 ? 123 ARG C CA    1 
ATOM   4815 C  C     . ARG D 2 124 ? 29.211  10.835  56.489  1.00 76.77 ? 123 ARG C C     1 
ATOM   4816 O  O     . ARG D 2 124 ? 29.920  10.646  57.479  1.00 79.62 ? 123 ARG C O     1 
ATOM   4817 C  CB    . ARG D 2 124 ? 27.604  8.938   56.324  1.00 74.70 ? 123 ARG C CB    1 
ATOM   4818 C  CG    . ARG D 2 124 ? 26.656  8.219   55.380  1.00 76.14 ? 123 ARG C CG    1 
ATOM   4819 C  CD    . ARG D 2 124 ? 25.276  7.970   56.029  1.00 71.68 ? 123 ARG C CD    1 
ATOM   4820 N  NE    . ARG D 2 124 ? 24.409  9.140   55.941  1.00 70.04 ? 123 ARG C NE    1 
ATOM   4821 C  CZ    . ARG D 2 124 ? 23.226  9.163   55.333  1.00 69.50 ? 123 ARG C CZ    1 
ATOM   4822 N  NH1   . ARG D 2 124 ? 22.746  8.099   54.706  1.00 66.43 ? 123 ARG C NH1   1 
ATOM   4823 N  NH2   . ARG D 2 124 ? 22.511  10.284  55.351  1.00 70.52 ? 123 ARG C NH2   1 
ATOM   4824 N  N     . THR D 2 125 ? 28.824  12.045  56.099  1.00 74.73 ? 124 THR C N     1 
ATOM   4825 C  CA    . THR D 2 125 ? 29.028  13.193  56.975  1.00 76.57 ? 124 THR C CA    1 
ATOM   4826 C  C     . THR D 2 125 ? 27.724  13.875  57.353  1.00 76.33 ? 124 THR C C     1 
ATOM   4827 O  O     . THR D 2 125 ? 27.664  14.545  58.390  1.00 77.61 ? 124 THR C O     1 
ATOM   4828 C  CB    . THR D 2 125 ? 29.970  14.226  56.333  1.00 76.41 ? 124 THR C CB    1 
ATOM   4829 O  OG1   . THR D 2 125 ? 29.493  14.589  55.032  1.00 73.02 ? 124 THR C OG1   1 
ATOM   4830 C  CG2   . THR D 2 125 ? 31.369  13.655  56.204  1.00 78.34 ? 124 THR C CG2   1 
ATOM   4831 N  N     . VAL D 2 126 ? 26.686  13.704  56.551  1.00 72.60 ? 125 VAL C N     1 
ATOM   4832 C  CA    . VAL D 2 126 ? 25.358  14.220  56.824  1.00 71.63 ? 125 VAL C CA    1 
ATOM   4833 C  C     . VAL D 2 126 ? 24.522  13.030  57.277  1.00 71.83 ? 125 VAL C C     1 
ATOM   4834 O  O     . VAL D 2 126 ? 24.219  12.141  56.472  1.00 72.22 ? 125 VAL C O     1 
ATOM   4835 C  CB    . VAL D 2 126 ? 24.761  14.901  55.577  1.00 68.42 ? 125 VAL C CB    1 
ATOM   4836 C  CG1   . VAL D 2 126 ? 23.447  15.571  55.907  1.00 67.85 ? 125 VAL C CG1   1 
ATOM   4837 C  CG2   . VAL D 2 126 ? 25.740  15.927  55.007  1.00 68.29 ? 125 VAL C CG2   1 
ATOM   4838 N  N     . ASP D 2 127 ? 24.169  12.990  58.562  1.00 74.22 ? 126 ASP C N     1 
ATOM   4839 C  CA    . ASP D 2 127 ? 23.266  11.947  59.054  1.00 74.59 ? 126 ASP C CA    1 
ATOM   4840 C  C     . ASP D 2 127 ? 21.910  12.042  58.365  1.00 71.92 ? 126 ASP C C     1 
ATOM   4841 O  O     . ASP D 2 127 ? 21.418  13.134  58.083  1.00 70.78 ? 126 ASP C O     1 
ATOM   4842 C  CB    . ASP D 2 127 ? 23.061  12.044  60.579  1.00 77.75 ? 126 ASP C CB    1 
ATOM   4843 C  CG    . ASP D 2 127 ? 24.332  11.858  61.366  1.00 80.81 ? 126 ASP C CG    1 
ATOM   4844 O  OD1   . ASP D 2 127 ? 25.266  11.211  60.857  1.00 80.80 ? 126 ASP C OD1   1 
ATOM   4845 O  OD2   . ASP D 2 127 ? 24.414  12.402  62.483  1.00 83.38 ? 126 ASP C OD2   1 
ATOM   4846 N  N     . THR D 2 128 ? 21.305  10.878  58.108  1.00 71.14 ? 127 THR C N     1 
ATOM   4847 C  CA    . THR D 2 128 ? 19.883  10.765  57.784  1.00 69.48 ? 127 THR C CA    1 
ATOM   4848 C  C     . THR D 2 128 ? 19.050  11.671  58.691  1.00 70.70 ? 127 THR C C     1 
ATOM   4849 O  O     . THR D 2 128 ? 18.179  12.411  58.220  1.00 69.14 ? 127 THR C O     1 
ATOM   4850 C  CB    . THR D 2 128 ? 19.413  9.306   57.929  1.00 69.90 ? 127 THR C CB    1 
ATOM   4851 O  OG1   . THR D 2 128 ? 20.281  8.435   57.192  1.00 69.26 ? 127 THR C OG1   1 
ATOM   4852 C  CG2   . THR D 2 128 ? 17.976  9.131   57.423  1.00 68.09 ? 127 THR C CG2   1 
ATOM   4853 N  N     . LYS D 2 129 ? 19.353  11.615  59.999  1.00 73.72 ? 128 LYS C N     1 
ATOM   4854 C  CA    . LYS D 2 129 ? 18.640  12.386  61.013  1.00 75.46 ? 128 LYS C CA    1 
ATOM   4855 C  C     . LYS D 2 129 ? 18.632  13.878  60.688  1.00 74.64 ? 128 LYS C C     1 
ATOM   4856 O  O     . LYS D 2 129 ? 17.585  14.530  60.784  1.00 74.37 ? 128 LYS C O     1 
ATOM   4857 C  CB    . LYS D 2 129 ? 19.296  12.145  62.375  1.00 78.97 ? 128 LYS C CB    1 
ATOM   4858 C  CG    . LYS D 2 129 ? 18.640  12.774  63.594  1.00 81.39 ? 128 LYS C CG    1 
ATOM   4859 C  CD    . LYS D 2 129 ? 17.133  12.552  63.694  1.00 80.91 ? 128 LYS C CD    1 
ATOM   4860 C  CE    . LYS D 2 129 ? 16.579  13.018  65.067  1.00 83.97 ? 128 LYS C CE    1 
ATOM   4861 N  NZ    . LYS D 2 129 ? 17.284  14.202  65.682  1.00 85.78 ? 128 LYS C NZ    1 
ATOM   4862 N  N     . GLN D 2 130 ? 19.800  14.443  60.331  1.00 74.51 ? 129 GLN C N     1 
ATOM   4863 C  CA    . GLN D 2 130 ? 19.866  15.868  60.008  1.00 73.91 ? 129 GLN C CA    1 
ATOM   4864 C  C     . GLN D 2 130 ? 18.960  16.202  58.843  1.00 70.90 ? 129 GLN C C     1 
ATOM   4865 O  O     . GLN D 2 130 ? 18.183  17.156  58.902  1.00 70.82 ? 129 GLN C O     1 
ATOM   4866 C  CB    . GLN D 2 130 ? 21.296  16.327  59.689  1.00 74.20 ? 129 GLN C CB    1 
ATOM   4867 C  CG    . GLN D 2 130 ? 22.394  16.056  60.732  1.00 77.70 ? 129 GLN C CG    1 
ATOM   4868 C  CD    . GLN D 2 130 ? 23.810  16.221  60.144  1.00 77.26 ? 129 GLN C CD    1 
ATOM   4869 O  OE1   . GLN D 2 130 ? 24.602  15.277  60.159  1.00 78.01 ? 129 GLN C OE1   1 
ATOM   4870 N  NE2   . GLN D 2 130 ? 24.093  17.398  59.548  1.00 76.33 ? 129 GLN C NE2   1 
ATOM   4871 N  N     . ALA D 2 131 ? 19.069  15.436  57.759  1.00 71.05 ? 130 ALA C N     1 
ATOM   4872 C  CA    . ALA D 2 131 ? 18.250  15.701  56.580  1.00 66.77 ? 130 ALA C CA    1 
ATOM   4873 C  C     . ALA D 2 131 ? 16.763  15.444  56.834  1.00 66.10 ? 130 ALA C C     1 
ATOM   4874 O  O     . ALA D 2 131 ? 15.920  16.120  56.229  1.00 64.37 ? 130 ALA C O     1 
ATOM   4875 C  CB    . ALA D 2 131 ? 18.750  14.869  55.403  1.00 63.57 ? 130 ALA C CB    1 
ATOM   4876 N  N     . GLN D 2 132 ? 16.411  14.490  57.718  1.00 70.61 ? 131 GLN C N     1 
ATOM   4877 C  CA    . GLN D 2 132 ? 15.004  14.353  58.095  1.00 67.73 ? 131 GLN C CA    1 
ATOM   4878 C  C     . GLN D 2 132 ? 14.532  15.580  58.864  1.00 69.39 ? 131 GLN C C     1 
ATOM   4879 O  O     . GLN D 2 132 ? 13.495  16.163  58.538  1.00 68.69 ? 131 GLN C O     1 
ATOM   4880 C  CB    . GLN D 2 132 ? 14.749  13.061  58.888  1.00 69.33 ? 131 GLN C CB    1 
ATOM   4881 C  CG    . GLN D 2 132 ? 15.263  11.771  58.255  1.00 68.20 ? 131 GLN C CG    1 
ATOM   4882 C  CD    . GLN D 2 132 ? 15.253  10.558  59.209  1.00 70.41 ? 131 GLN C CD    1 
ATOM   4883 O  OE1   . GLN D 2 132 ? 15.518  10.681  60.412  1.00 73.07 ? 131 GLN C OE1   1 
ATOM   4884 N  NE2   . GLN D 2 132 ? 14.910  9.383   58.667  1.00 69.44 ? 131 GLN C NE2   1 
ATOM   4885 N  N     . ASP D 2 133 ? 15.302  16.011  59.860  1.00 71.75 ? 132 ASP C N     1 
ATOM   4886 C  CA    . ASP D 2 133 ? 14.916  17.177  60.648  1.00 73.66 ? 132 ASP C CA    1 
ATOM   4887 C  C     . ASP D 2 133 ? 14.843  18.451  59.821  1.00 73.38 ? 132 ASP C C     1 
ATOM   4888 O  O     . ASP D 2 133 ? 13.996  19.304  60.098  1.00 73.02 ? 132 ASP C O     1 
ATOM   4889 C  CB    . ASP D 2 133 ? 15.885  17.347  61.794  1.00 76.50 ? 132 ASP C CB    1 
ATOM   4890 C  CG    . ASP D 2 133 ? 15.853  16.174  62.715  1.00 78.36 ? 132 ASP C CG    1 
ATOM   4891 O  OD1   . ASP D 2 133 ? 14.747  15.625  62.903  1.00 78.46 ? 132 ASP C OD1   1 
ATOM   4892 O  OD2   . ASP D 2 133 ? 16.919  15.797  63.229  1.00 79.85 ? 132 ASP C OD2   1 
ATOM   4893 N  N     . LEU D 2 134 ? 15.698  18.595  58.798  1.00 70.17 ? 133 LEU C N     1 
ATOM   4894 C  CA    . LEU D 2 134 ? 15.594  19.734  57.892  1.00 68.64 ? 133 LEU C CA    1 
ATOM   4895 C  C     . LEU D 2 134 ? 14.354  19.613  57.021  1.00 67.46 ? 133 LEU C C     1 
ATOM   4896 O  O     . LEU D 2 134 ? 13.557  20.550  56.914  1.00 70.33 ? 133 LEU C O     1 
ATOM   4897 C  CB    . LEU D 2 134 ? 16.842  19.834  56.989  1.00 67.39 ? 133 LEU C CB    1 
ATOM   4898 C  CG    . LEU D 2 134 ? 17.024  21.097  56.121  1.00 65.90 ? 133 LEU C CG    1 
ATOM   4899 C  CD1   . LEU D 2 134 ? 17.126  22.315  56.988  1.00 68.33 ? 133 LEU C CD1   1 
ATOM   4900 C  CD2   . LEU D 2 134 ? 18.223  21.024  55.192  1.00 64.40 ? 133 LEU C CD2   1 
ATOM   4901 N  N     . ALA D 2 135 ? 14.182  18.470  56.375  1.00 64.87 ? 134 ALA C N     1 
ATOM   4902 C  CA    . ALA D 2 135 ? 13.023  18.325  55.519  1.00 64.05 ? 134 ALA C CA    1 
ATOM   4903 C  C     . ALA D 2 135 ? 11.748  18.582  56.305  1.00 67.90 ? 134 ALA C C     1 
ATOM   4904 O  O     . ALA D 2 135 ? 10.865  19.306  55.832  1.00 65.41 ? 134 ALA C O     1 
ATOM   4905 C  CB    . ALA D 2 135 ? 13.012  16.944  54.849  1.00 61.38 ? 134 ALA C CB    1 
ATOM   4906 N  N     . ARG D 2 136 ? 11.670  18.072  57.540  1.00 67.18 ? 135 ARG C N     1 
ATOM   4907 C  CA    . ARG D 2 136 ? 10.432  18.218  58.295  1.00 69.02 ? 135 ARG C CA    1 
ATOM   4908 C  C     . ARG D 2 136 ? 10.137  19.690  58.578  1.00 72.88 ? 135 ARG C C     1 
ATOM   4909 O  O     . ARG D 2 136 ? 8.976   20.119  58.511  1.00 74.68 ? 135 ARG C O     1 
ATOM   4910 C  CB    . ARG D 2 136 ? 10.507  17.409  59.601  1.00 72.66 ? 135 ARG C CB    1 
ATOM   4911 C  CG    . ARG D 2 136 ? 9.300   17.533  60.571  1.00 75.37 ? 135 ARG C CG    1 
ATOM   4912 C  CD    . ARG D 2 136 ? 9.230   16.354  61.557  1.00 78.17 ? 135 ARG C CD    1 
ATOM   4913 N  NE    . ARG D 2 136 ? 10.540  15.996  62.101  1.00 79.79 ? 135 ARG C NE    1 
ATOM   4914 C  CZ    . ARG D 2 136 ? 11.249  14.925  61.755  1.00 79.15 ? 135 ARG C CZ    1 
ATOM   4915 N  NH1   . ARG D 2 136 ? 10.774  14.017  60.914  1.00 76.04 ? 135 ARG C NH1   1 
ATOM   4916 N  NH2   . ARG D 2 136 ? 12.474  14.770  62.257  1.00 78.78 ? 135 ARG C NH2   1 
ATOM   4917 N  N     . SER D 2 137 ? 11.172  20.478  58.899  1.00 71.12 ? 136 SER C N     1 
ATOM   4918 C  CA    . SER D 2 137 ? 10.968  21.908  59.108  1.00 72.39 ? 136 SER C CA    1 
ATOM   4919 C  C     . SER D 2 137 ? 10.289  22.537  57.900  1.00 71.72 ? 136 SER C C     1 
ATOM   4920 O  O     . SER D 2 137 ? 9.254   23.209  58.026  1.00 71.46 ? 136 SER C O     1 
ATOM   4921 C  CB    . SER D 2 137 ? 12.303  22.608  59.389  1.00 73.77 ? 136 SER C CB    1 
ATOM   4922 O  OG    . SER D 2 137 ? 13.176  22.579  58.272  1.00 70.72 ? 136 SER C OG    1 
ATOM   4923 N  N     . TYR D 2 138 ? 10.846  22.293  56.711  1.00 67.64 ? 137 TYR C N     1 
ATOM   4924 C  CA    . TYR D 2 138 ? 10.307  22.871  55.503  1.00 65.74 ? 137 TYR C CA    1 
ATOM   4925 C  C     . TYR D 2 138 ? 8.957   22.275  55.106  1.00 65.81 ? 137 TYR C C     1 
ATOM   4926 O  O     . TYR D 2 138 ? 8.236   22.882  54.313  1.00 65.85 ? 137 TYR C O     1 
ATOM   4927 C  CB    . TYR D 2 138 ? 11.284  22.672  54.350  1.00 66.15 ? 137 TYR C CB    1 
ATOM   4928 C  CG    . TYR D 2 138 ? 12.709  23.142  54.580  1.00 66.32 ? 137 TYR C CG    1 
ATOM   4929 C  CD1   . TYR D 2 138 ? 13.014  24.153  55.493  1.00 66.06 ? 137 TYR C CD1   1 
ATOM   4930 C  CD2   . TYR D 2 138 ? 13.739  22.671  53.755  1.00 64.79 ? 137 TYR C CD2   1 
ATOM   4931 C  CE1   . TYR D 2 138 ? 14.330  24.609  55.647  1.00 66.65 ? 137 TYR C CE1   1 
ATOM   4932 C  CE2   . TYR D 2 138 ? 15.043  23.133  53.887  1.00 64.46 ? 137 TYR C CE2   1 
ATOM   4933 C  CZ    . TYR D 2 138 ? 15.336  24.101  54.823  1.00 67.38 ? 137 TYR C CZ    1 
ATOM   4934 O  OH    . TYR D 2 138 ? 16.649  24.533  54.924  1.00 72.03 ? 137 TYR C OH    1 
ATOM   4935 N  N     . GLY D 2 139 ? 8.588   21.113  55.621  1.00 65.53 ? 138 GLY C N     1 
ATOM   4936 C  CA    . GLY D 2 139 ? 7.365   20.491  55.145  1.00 64.84 ? 138 GLY C CA    1 
ATOM   4937 C  C     . GLY D 2 139 ? 7.429   19.917  53.734  1.00 64.71 ? 138 GLY C C     1 
ATOM   4938 O  O     . GLY D 2 139 ? 6.512   20.113  52.923  1.00 64.72 ? 138 GLY C O     1 
ATOM   4939 N  N     . ILE D 2 140 ? 8.495   19.183  53.431  1.00 61.43 ? 139 ILE C N     1 
ATOM   4940 C  CA    . ILE D 2 140 ? 8.623   18.490  52.149  1.00 59.30 ? 139 ILE C CA    1 
ATOM   4941 C  C     . ILE D 2 140 ? 9.226   17.106  52.380  1.00 57.62 ? 139 ILE C C     1 
ATOM   4942 O  O     . ILE D 2 140 ? 9.782   16.820  53.440  1.00 59.19 ? 139 ILE C O     1 
ATOM   4943 C  CB    . ILE D 2 140 ? 9.475   19.309  51.155  1.00 56.02 ? 139 ILE C CB    1 
ATOM   4944 C  CG1   . ILE D 2 140 ? 10.851  19.621  51.762  1.00 58.36 ? 139 ILE C CG1   1 
ATOM   4945 C  CG2   . ILE D 2 140 ? 8.728   20.572  50.729  1.00 56.16 ? 139 ILE C CG2   1 
ATOM   4946 C  CD1   . ILE D 2 140 ? 12.053  19.726  50.725  1.00 54.80 ? 139 ILE C CD1   1 
ATOM   4947 N  N     . PRO D 2 141 ? 9.051   16.210  51.422  1.00 55.64 ? 140 PRO C N     1 
ATOM   4948 C  CA    . PRO D 2 141 ? 9.584   14.847  51.598  1.00 55.54 ? 140 PRO C CA    1 
ATOM   4949 C  C     . PRO D 2 141 ? 11.107  14.849  51.616  1.00 55.22 ? 140 PRO C C     1 
ATOM   4950 O  O     . PRO D 2 141 ? 11.745  15.750  51.082  1.00 54.32 ? 140 PRO C O     1 
ATOM   4951 C  CB    . PRO D 2 141 ? 9.052   14.090  50.374  1.00 58.36 ? 140 PRO C CB    1 
ATOM   4952 C  CG    . PRO D 2 141 ? 7.871   14.890  49.897  1.00 58.55 ? 140 PRO C CG    1 
ATOM   4953 C  CD    . PRO D 2 141 ? 7.952   16.287  50.452  1.00 56.25 ? 140 PRO C CD    1 
ATOM   4954 N  N     . PHE D 2 142 ? 11.687  13.815  52.239  1.00 56.18 ? 141 PHE C N     1 
ATOM   4955 C  CA    . PHE D 2 142 ? 13.127  13.547  52.175  1.00 56.00 ? 141 PHE C CA    1 
ATOM   4956 C  C     . PHE D 2 142 ? 13.353  12.102  51.709  1.00 56.69 ? 141 PHE C C     1 
ATOM   4957 O  O     . PHE D 2 142 ? 12.712  11.171  52.223  1.00 56.25 ? 141 PHE C O     1 
ATOM   4958 C  CB    . PHE D 2 142 ? 13.825  13.778  53.533  1.00 58.52 ? 141 PHE C CB    1 
ATOM   4959 C  CG    . PHE D 2 142 ? 15.256  13.247  53.586  1.00 58.84 ? 141 PHE C CG    1 
ATOM   4960 C  CD1   . PHE D 2 142 ? 16.202  13.645  52.623  1.00 57.28 ? 141 PHE C CD1   1 
ATOM   4961 C  CD2   . PHE D 2 142 ? 15.644  12.321  54.562  1.00 61.47 ? 141 PHE C CD2   1 
ATOM   4962 C  CE1   . PHE D 2 142 ? 17.509  13.143  52.655  1.00 57.81 ? 141 PHE C CE1   1 
ATOM   4963 C  CE2   . PHE D 2 142 ? 16.941  11.814  54.606  1.00 61.90 ? 141 PHE C CE2   1 
ATOM   4964 C  CZ    . PHE D 2 142 ? 17.873  12.211  53.644  1.00 60.91 ? 141 PHE C CZ    1 
ATOM   4965 N  N     . ILE D 2 143 ? 14.269  11.923  50.747  1.00 53.68 ? 142 ILE C N     1 
ATOM   4966 C  CA    . ILE D 2 143 ? 14.610  10.622  50.162  1.00 53.57 ? 142 ILE C CA    1 
ATOM   4967 C  C     . ILE D 2 143 ? 16.123  10.540  49.994  1.00 54.19 ? 142 ILE C C     1 
ATOM   4968 O  O     . ILE D 2 143 ? 16.738  11.434  49.409  1.00 52.07 ? 142 ILE C O     1 
ATOM   4969 C  CB    . ILE D 2 143 ? 13.955  10.345  48.781  1.00 56.72 ? 142 ILE C CB    1 
ATOM   4970 C  CG1   . ILE D 2 143 ? 12.428  10.587  48.738  1.00 57.53 ? 142 ILE C CG1   1 
ATOM   4971 C  CG2   . ILE D 2 143 ? 14.271  8.917   48.306  1.00 55.49 ? 142 ILE C CG2   1 
ATOM   4972 C  CD1   . ILE D 2 143 ? 11.987  12.039  48.691  1.00 56.43 ? 142 ILE C CD1   1 
ATOM   4973 N  N     . GLU D 2 144 ? 16.724  9.466   50.503  1.00 60.78 ? 143 GLU C N     1 
ATOM   4974 C  CA    . GLU D 2 144 ? 18.108  9.142   50.181  1.00 57.58 ? 143 GLU C CA    1 
ATOM   4975 C  C     . GLU D 2 144 ? 18.157  8.336   48.892  1.00 54.74 ? 143 GLU C C     1 
ATOM   4976 O  O     . GLU D 2 144 ? 17.385  7.384   48.721  1.00 52.74 ? 143 GLU C O     1 
ATOM   4977 C  CB    . GLU D 2 144 ? 18.780  8.365   51.310  1.00 57.14 ? 143 GLU C CB    1 
ATOM   4978 C  CG    . GLU D 2 144 ? 19.592  9.244   52.248  1.00 60.16 ? 143 GLU C CG    1 
ATOM   4979 C  CD    . GLU D 2 144 ? 19.621  8.653   53.643  1.00 65.92 ? 143 GLU C CD    1 
ATOM   4980 O  OE1   . GLU D 2 144 ? 19.235  7.463   53.801  1.00 68.85 ? 143 GLU C OE1   1 
ATOM   4981 O  OE2   . GLU D 2 144 ? 20.002  9.373   54.598  1.00 68.11 ? 143 GLU C OE2   1 
ATOM   4982 N  N     . THR D 2 145 ? 19.067  8.717   47.989  1.00 51.59 ? 144 THR C N     1 
ATOM   4983 C  CA    . THR D 2 145 ? 19.239  7.983   46.759  1.00 50.07 ? 144 THR C CA    1 
ATOM   4984 C  C     . THR D 2 145 ? 20.671  7.490   46.561  1.00 53.40 ? 144 THR C C     1 
ATOM   4985 O  O     . THR D 2 145 ? 21.602  7.837   47.287  1.00 52.56 ? 144 THR C O     1 
ATOM   4986 C  CB    . THR D 2 145 ? 18.840  8.856   45.582  1.00 54.60 ? 144 THR C CB    1 
ATOM   4987 O  OG1   . THR D 2 145 ? 19.799  9.897   45.503  1.00 47.76 ? 144 THR C OG1   1 
ATOM   4988 C  CG2   . THR D 2 145 ? 17.416  9.426   45.786  1.00 48.94 ? 144 THR C CG2   1 
ATOM   4989 N  N     . SER D 2 146 ? 20.836  6.658   45.537  1.00 51.39 ? 145 SER C N     1 
ATOM   4990 C  CA    . SER D 2 146 ? 22.155  6.330   45.013  1.00 50.38 ? 145 SER C CA    1 
ATOM   4991 C  C     . SER D 2 146 ? 21.951  6.202   43.529  1.00 51.89 ? 145 SER C C     1 
ATOM   4992 O  O     . SER D 2 146 ? 21.309  5.245   43.097  1.00 48.54 ? 145 SER C O     1 
ATOM   4993 C  CB    . SER D 2 146 ? 22.727  5.032   45.556  1.00 52.51 ? 145 SER C CB    1 
ATOM   4994 O  OG    . SER D 2 146 ? 23.863  4.675   44.784  1.00 52.70 ? 145 SER C OG    1 
ATOM   4995 N  N     . ALA D 2 147 ? 22.450  7.175   42.770  1.00 47.00 ? 146 ALA C N     1 
ATOM   4996 C  CA    . ALA D 2 147 ? 22.544  6.977   41.339  1.00 45.31 ? 146 ALA C CA    1 
ATOM   4997 C  C     . ALA D 2 147 ? 23.372  5.741   40.983  1.00 51.62 ? 146 ALA C C     1 
ATOM   4998 O  O     . ALA D 2 147 ? 23.040  5.041   40.016  1.00 55.93 ? 146 ALA C O     1 
ATOM   4999 C  CB    . ALA D 2 147 ? 23.137  8.230   40.691  1.00 44.32 ? 146 ALA C CB    1 
ATOM   5000 N  N     . LYS D 2 148 ? 24.445  5.451   41.741  1.00 54.44 ? 147 LYS C N     1 
ATOM   5001 C  CA    . LYS D 2 148 ? 25.342  4.344   41.385  1.00 53.37 ? 147 LYS C CA    1 
ATOM   5002 C  C     . LYS D 2 148 ? 24.619  2.994   41.379  1.00 54.24 ? 147 LYS C C     1 
ATOM   5003 O  O     . LYS D 2 148 ? 24.798  2.194   40.452  1.00 50.54 ? 147 LYS C O     1 
ATOM   5004 C  CB    . LYS D 2 148 ? 26.538  4.297   42.337  1.00 53.22 ? 147 LYS C CB    1 
ATOM   5005 C  CG    . LYS D 2 148 ? 27.477  3.135   42.112  1.00 54.38 ? 147 LYS C CG    1 
ATOM   5006 C  CD    . LYS D 2 148 ? 28.829  3.442   42.716  1.00 59.22 ? 147 LYS C CD    1 
ATOM   5007 C  CE    . LYS D 2 148 ? 29.677  2.184   42.934  1.00 59.45 ? 147 LYS C CE    1 
ATOM   5008 N  NZ    . LYS D 2 148 ? 31.110  2.499   43.152  1.00 61.68 ? 147 LYS C NZ    1 
ATOM   5009 N  N     . THR D 2 149 ? 23.799  2.725   42.397  1.00 50.88 ? 148 THR C N     1 
ATOM   5010 C  CA    . THR D 2 149 ? 22.985  1.510   42.467  1.00 53.37 ? 148 THR C CA    1 
ATOM   5011 C  C     . THR D 2 149 ? 21.533  1.722   42.038  1.00 50.43 ? 148 THR C C     1 
ATOM   5012 O  O     . THR D 2 149 ? 20.740  0.764   42.087  1.00 52.39 ? 148 THR C O     1 
ATOM   5013 C  CB    . THR D 2 149 ? 22.960  0.967   43.896  1.00 53.70 ? 148 THR C CB    1 
ATOM   5014 O  OG1   . THR D 2 149 ? 22.214  1.891   44.705  1.00 53.29 ? 148 THR C OG1   1 
ATOM   5015 C  CG2   . THR D 2 149 ? 24.399  0.732   44.486  1.00 56.22 ? 148 THR C CG2   1 
ATOM   5016 N  N     . ARG D 2 150 ? 21.150  2.967   41.725  1.00 53.49 ? 149 ARG C N     1 
ATOM   5017 C  CA    . ARG D 2 150 ? 19.804  3.406   41.319  1.00 53.45 ? 149 ARG C CA    1 
ATOM   5018 C  C     . ARG D 2 150 ? 18.765  3.381   42.465  1.00 56.71 ? 149 ARG C C     1 
ATOM   5019 O  O     . ARG D 2 150 ? 17.563  3.463   42.203  1.00 51.86 ? 149 ARG C O     1 
ATOM   5020 C  CB    . ARG D 2 150 ? 19.300  2.613   40.100  1.00 53.52 ? 149 ARG C CB    1 
ATOM   5021 C  CG    . ARG D 2 150 ? 18.131  3.273   39.362  1.00 53.33 ? 149 ARG C CG    1 
ATOM   5022 C  CD    . ARG D 2 150 ? 17.909  2.729   37.945  1.00 57.92 ? 149 ARG C CD    1 
ATOM   5023 N  NE    . ARG D 2 150 ? 17.094  3.604   37.097  1.00 52.92 ? 149 ARG C NE    1 
ATOM   5024 C  CZ    . ARG D 2 150 ? 15.849  3.980   37.380  1.00 53.16 ? 149 ARG C CZ    1 
ATOM   5025 N  NH1   . ARG D 2 150 ? 15.224  3.565   38.482  1.00 47.63 ? 149 ARG C NH1   1 
ATOM   5026 N  NH2   . ARG D 2 150 ? 15.203  4.775   36.535  1.00 48.88 ? 149 ARG C NH2   1 
ATOM   5027 N  N     . GLN D 2 151 ? 19.180  3.320   43.740  1.00 55.89 ? 150 GLN C N     1 
ATOM   5028 C  CA    . GLN D 2 151 ? 18.217  3.341   44.850  1.00 55.06 ? 150 GLN C CA    1 
ATOM   5029 C  C     . GLN D 2 151 ? 17.472  4.681   44.955  1.00 53.71 ? 150 GLN C C     1 
ATOM   5030 O  O     . GLN D 2 151 ? 18.100  5.737   44.974  1.00 53.77 ? 150 GLN C O     1 
ATOM   5031 C  CB    . GLN D 2 151 ? 18.952  3.040   46.161  1.00 58.99 ? 150 GLN C CB    1 
ATOM   5032 C  CG    . GLN D 2 151 ? 18.066  2.817   47.389  1.00 61.90 ? 150 GLN C CG    1 
ATOM   5033 C  CD    . GLN D 2 151 ? 18.853  2.867   48.695  1.00 72.51 ? 150 GLN C CD    1 
ATOM   5034 O  OE1   . GLN D 2 151 ? 19.657  1.973   48.969  1.00 76.36 ? 150 GLN C OE1   1 
ATOM   5035 N  NE2   . GLN D 2 151 ? 18.593  3.884   49.530  1.00 73.64 ? 150 GLN C NE2   1 
ATOM   5036 N  N     . GLY D 2 152 ? 16.123  4.639   45.024  1.00 52.71 ? 151 GLY C N     1 
ATOM   5037 C  CA    . GLY D 2 152 ? 15.284  5.819   45.270  1.00 50.70 ? 151 GLY C CA    1 
ATOM   5038 C  C     . GLY D 2 152 ? 15.143  6.818   44.114  1.00 48.11 ? 151 GLY C C     1 
ATOM   5039 O  O     . GLY D 2 152 ? 14.472  7.855   44.273  1.00 44.73 ? 151 GLY C O     1 
ATOM   5040 N  N     . VAL D 2 153 ? 15.773  6.581   42.967  1.00 48.44 ? 152 VAL C N     1 
ATOM   5041 C  CA    . VAL D 2 153 ? 15.676  7.557   41.871  1.00 44.94 ? 152 VAL C CA    1 
ATOM   5042 C  C     . VAL D 2 153 ? 14.207  7.850   41.526  1.00 45.49 ? 152 VAL C C     1 
ATOM   5043 O  O     . VAL D 2 153 ? 13.733  8.994   41.638  1.00 45.50 ? 152 VAL C O     1 
ATOM   5044 C  CB    . VAL D 2 153 ? 16.462  7.062   40.644  1.00 49.12 ? 152 VAL C CB    1 
ATOM   5045 C  CG1   . VAL D 2 153 ? 16.364  8.063   39.501  1.00 39.80 ? 152 VAL C CG1   1 
ATOM   5046 C  CG2   . VAL D 2 153 ? 17.941  6.791   41.025  1.00 50.89 ? 152 VAL C CG2   1 
ATOM   5047 N  N     . ASP D 2 154 ? 13.452  6.812   41.133  1.00 44.52 ? 153 ASP C N     1 
ATOM   5048 C  CA    . ASP D 2 154 ? 12.082  7.035   40.660  1.00 44.03 ? 153 ASP C CA    1 
ATOM   5049 C  C     . ASP D 2 154 ? 11.231  7.710   41.726  1.00 44.93 ? 153 ASP C C     1 
ATOM   5050 O  O     . ASP D 2 154 ? 10.473  8.648   41.437  1.00 44.01 ? 153 ASP C O     1 
ATOM   5051 C  CB    . ASP D 2 154 ? 11.444  5.711   40.234  1.00 41.76 ? 153 ASP C CB    1 
ATOM   5052 C  CG    . ASP D 2 154 ? 12.029  5.174   38.949  1.00 45.11 ? 153 ASP C CG    1 
ATOM   5053 O  OD1   . ASP D 2 154 ? 12.343  5.989   38.043  1.00 40.45 ? 153 ASP C OD1   1 
ATOM   5054 O  OD2   . ASP D 2 154 ? 12.146  3.929   38.819  1.00 47.15 ? 153 ASP C OD2   1 
ATOM   5055 N  N     . ASP D 2 155 ? 11.361  7.248   42.976  1.00 46.17 ? 154 ASP C N     1 
ATOM   5056 C  CA    . ASP D 2 155 ? 10.632  7.819   44.102  1.00 46.72 ? 154 ASP C CA    1 
ATOM   5057 C  C     . ASP D 2 155 ? 10.801  9.329   44.197  1.00 44.11 ? 154 ASP C C     1 
ATOM   5058 O  O     . ASP D 2 155 ? 9.821   10.068  44.322  1.00 45.01 ? 154 ASP C O     1 
ATOM   5059 C  CB    . ASP D 2 155 ? 11.118  7.144   45.389  1.00 46.49 ? 154 ASP C CB    1 
ATOM   5060 C  CG    . ASP D 2 155 ? 10.238  7.463   46.589  1.00 56.17 ? 154 ASP C CG    1 
ATOM   5061 O  OD1   . ASP D 2 155 ? 9.194   8.140   46.406  1.00 58.95 ? 154 ASP C OD1   1 
ATOM   5062 O  OD2   . ASP D 2 155 ? 10.610  7.061   47.717  1.00 54.55 ? 154 ASP C OD2   1 
ATOM   5063 N  N     . ALA D 2 156 ? 12.052  9.806   44.177  1.00 44.88 ? 155 ALA C N     1 
ATOM   5064 C  CA    . ALA D 2 156 ? 12.320  11.245  44.213  1.00 46.63 ? 155 ALA C CA    1 
ATOM   5065 C  C     . ALA D 2 156 ? 11.459  12.067  43.230  1.00 44.53 ? 155 ALA C C     1 
ATOM   5066 O  O     . ALA D 2 156 ? 10.789  13.032  43.623  1.00 42.77 ? 155 ALA C O     1 
ATOM   5067 C  CB    . ALA D 2 156 ? 13.808  11.469  43.941  1.00 43.15 ? 155 ALA C CB    1 
ATOM   5068 N  N     . PHE D 2 157 ? 11.491  11.724  41.936  1.00 43.12 ? 156 PHE C N     1 
ATOM   5069 C  CA    . PHE D 2 157 ? 10.819  12.542  40.914  1.00 40.32 ? 156 PHE C CA    1 
ATOM   5070 C  C     . PHE D 2 157 ? 9.305   12.356  40.898  1.00 42.44 ? 156 PHE C C     1 
ATOM   5071 O  O     . PHE D 2 157 ? 8.560   13.309  40.623  1.00 39.62 ? 156 PHE C O     1 
ATOM   5072 C  CB    . PHE D 2 157 ? 11.339  12.197  39.510  1.00 37.56 ? 156 PHE C CB    1 
ATOM   5073 C  CG    . PHE D 2 157 ? 12.749  12.701  39.199  1.00 37.85 ? 156 PHE C CG    1 
ATOM   5074 C  CD1   . PHE D 2 157 ? 12.955  13.941  38.612  1.00 36.25 ? 156 PHE C CD1   1 
ATOM   5075 C  CD2   . PHE D 2 157 ? 13.840  11.868  39.383  1.00 37.66 ? 156 PHE C CD2   1 
ATOM   5076 C  CE1   . PHE D 2 157 ? 14.243  14.377  38.307  1.00 35.89 ? 156 PHE C CE1   1 
ATOM   5077 C  CE2   . PHE D 2 157 ? 15.134  12.295  39.065  1.00 36.99 ? 156 PHE C CE2   1 
ATOM   5078 C  CZ    . PHE D 2 157 ? 15.314  13.549  38.510  1.00 36.25 ? 156 PHE C CZ    1 
ATOM   5079 N  N     . TYR D 2 158 ? 8.840   11.125  41.124  1.00 40.92 ? 157 TYR C N     1 
ATOM   5080 C  CA    . TYR D 2 158 ? 7.405   10.891  41.172  1.00 43.61 ? 157 TYR C CA    1 
ATOM   5081 C  C     . TYR D 2 158 ? 6.804   11.597  42.371  1.00 44.90 ? 157 TYR C C     1 
ATOM   5082 O  O     . TYR D 2 158 ? 5.787   12.298  42.256  1.00 43.08 ? 157 TYR C O     1 
ATOM   5083 C  CB    . TYR D 2 158 ? 7.104   9.398   41.268  1.00 43.15 ? 157 TYR C CB    1 
ATOM   5084 C  CG    . TYR D 2 158 ? 7.430   8.595   40.042  1.00 42.53 ? 157 TYR C CG    1 
ATOM   5085 C  CD1   . TYR D 2 158 ? 8.065   9.166   38.939  1.00 39.83 ? 157 TYR C CD1   1 
ATOM   5086 C  CD2   . TYR D 2 158 ? 7.057   7.247   39.975  1.00 44.80 ? 157 TYR C CD2   1 
ATOM   5087 C  CE1   . TYR D 2 158 ? 8.366   8.405   37.827  1.00 41.98 ? 157 TYR C CE1   1 
ATOM   5088 C  CE2   . TYR D 2 158 ? 7.348   6.482   38.872  1.00 44.15 ? 157 TYR C CE2   1 
ATOM   5089 C  CZ    . TYR D 2 158 ? 7.992   7.052   37.804  1.00 43.00 ? 157 TYR C CZ    1 
ATOM   5090 O  OH    . TYR D 2 158 ? 8.288   6.275   36.695  1.00 44.04 ? 157 TYR C OH    1 
ATOM   5091 N  N     . THR D 2 159 ? 7.433   11.409  43.542  1.00 45.40 ? 158 THR C N     1 
ATOM   5092 C  CA    . THR D 2 159 ? 7.034   12.173  44.709  1.00 50.11 ? 158 THR C CA    1 
ATOM   5093 C  C     . THR D 2 159 ? 6.960   13.627  44.341  1.00 45.17 ? 158 THR C C     1 
ATOM   5094 O  O     . THR D 2 159 ? 6.002   14.318  44.701  1.00 46.27 ? 158 THR C O     1 
ATOM   5095 C  CB    . THR D 2 159 ? 7.993   11.942  45.884  1.00 50.76 ? 158 THR C CB    1 
ATOM   5096 O  OG1   . THR D 2 159 ? 8.031   10.534  46.245  1.00 47.53 ? 158 THR C OG1   1 
ATOM   5097 C  CG2   . THR D 2 159 ? 7.612   12.823  47.067  1.00 50.87 ? 158 THR C CG2   1 
ATOM   5098 N  N     . LEU D 2 160 ? 7.934   14.093  43.548  1.00 47.66 ? 159 LEU C N     1 
ATOM   5099 C  CA    . LEU D 2 160 ? 7.925   15.482  43.132  1.00 46.74 ? 159 LEU C CA    1 
ATOM   5100 C  C     . LEU D 2 160 ? 6.720   15.787  42.259  1.00 43.87 ? 159 LEU C C     1 
ATOM   5101 O  O     . LEU D 2 160 ? 6.084   16.824  42.439  1.00 44.62 ? 159 LEU C O     1 
ATOM   5102 C  CB    . LEU D 2 160 ? 9.227   15.833  42.411  1.00 45.60 ? 159 LEU C CB    1 
ATOM   5103 C  CG    . LEU D 2 160 ? 9.443   17.324  42.136  1.00 48.12 ? 159 LEU C CG    1 
ATOM   5104 C  CD1   . LEU D 2 160 ? 9.324   18.168  43.390  1.00 49.32 ? 159 LEU C CD1   1 
ATOM   5105 C  CD2   . LEU D 2 160 ? 10.806  17.537  41.490  1.00 45.20 ? 159 LEU C CD2   1 
ATOM   5106 N  N     . VAL D 2 161 ? 6.427   14.922  41.266  1.00 47.10 ? 160 VAL C N     1 
ATOM   5107 C  CA    . VAL D 2 161 ? 5.189   15.036  40.479  1.00 42.93 ? 160 VAL C CA    1 
ATOM   5108 C  C     . VAL D 2 161 ? 3.976   14.908  41.381  1.00 49.30 ? 160 VAL C C     1 
ATOM   5109 O  O     . VAL D 2 161 ? 2.943   15.563  41.167  1.00 48.14 ? 160 VAL C O     1 
ATOM   5110 C  CB    . VAL D 2 161 ? 5.127   13.950  39.385  1.00 44.08 ? 160 VAL C CB    1 
ATOM   5111 C  CG1   . VAL D 2 161 ? 3.739   13.884  38.759  1.00 40.51 ? 160 VAL C CG1   1 
ATOM   5112 C  CG2   . VAL D 2 161 ? 6.172   14.189  38.295  1.00 40.70 ? 160 VAL C CG2   1 
ATOM   5113 N  N     . ARG D 2 162 ? 4.043   13.997  42.349  1.00 44.70 ? 161 ARG C N     1 
ATOM   5114 C  CA    . ARG D 2 162 ? 2.927   13.935  43.278  1.00 51.80 ? 161 ARG C CA    1 
ATOM   5115 C  C     . ARG D 2 162 ? 2.867   15.155  44.188  1.00 51.69 ? 161 ARG C C     1 
ATOM   5116 O  O     . ARG D 2 162 ? 1.783   15.448  44.699  1.00 55.46 ? 161 ARG C O     1 
ATOM   5117 C  CB    . ARG D 2 162 ? 2.966   12.643  44.097  1.00 47.92 ? 161 ARG C CB    1 
ATOM   5118 C  CG    . ARG D 2 162 ? 2.503   11.440  43.322  1.00 48.38 ? 161 ARG C CG    1 
ATOM   5119 C  CD    . ARG D 2 162 ? 2.562   10.234  44.191  1.00 48.15 ? 161 ARG C CD    1 
ATOM   5120 N  NE    . ARG D 2 162 ? 2.730   9.019   43.416  1.00 47.18 ? 161 ARG C NE    1 
ATOM   5121 C  CZ    . ARG D 2 162 ? 3.817   8.267   43.452  1.00 47.38 ? 161 ARG C CZ    1 
ATOM   5122 N  NH1   . ARG D 2 162 ? 4.912   8.667   44.088  1.00 46.52 ? 161 ARG C NH1   1 
ATOM   5123 N  NH2   . ARG D 2 162 ? 3.805   7.079   42.841  1.00 46.14 ? 161 ARG C NH2   1 
ATOM   5124 N  N     . GLU D 2 163 ? 3.982   15.884  44.404  1.00 48.51 ? 162 GLU C N     1 
ATOM   5125 C  CA    . GLU D 2 163 ? 3.839   17.165  45.118  1.00 49.10 ? 162 GLU C CA    1 
ATOM   5126 C  C     . GLU D 2 163 ? 3.313   18.257  44.175  1.00 53.97 ? 162 GLU C C     1 
ATOM   5127 O  O     . GLU D 2 163 ? 2.598   19.154  44.610  1.00 54.21 ? 162 GLU C O     1 
ATOM   5128 C  CB    . GLU D 2 163 ? 5.170   17.647  45.756  1.00 51.06 ? 162 GLU C CB    1 
ATOM   5129 C  CG    . GLU D 2 163 ? 5.782   16.736  46.864  1.00 53.47 ? 162 GLU C CG    1 
ATOM   5130 C  CD    . GLU D 2 163 ? 5.192   16.942  48.294  1.00 52.68 ? 162 GLU C CD    1 
ATOM   5131 O  OE1   . GLU D 2 163 ? 5.478   17.912  49.031  1.00 53.98 ? 162 GLU C OE1   1 
ATOM   5132 O  OE2   . GLU D 2 163 ? 4.420   16.079  48.685  1.00 53.61 ? 162 GLU C OE2   1 
ATOM   5133 N  N     . ILE D 2 164 ? 3.680   18.224  42.885  1.00 54.68 ? 163 ILE C N     1 
ATOM   5134 C  CA    . ILE D 2 164 ? 3.071   19.156  41.934  1.00 53.69 ? 163 ILE C CA    1 
ATOM   5135 C  C     . ILE D 2 164 ? 1.588   18.886  41.785  1.00 57.42 ? 163 ILE C C     1 
ATOM   5136 O  O     . ILE D 2 164 ? 0.775   19.808  41.898  1.00 64.73 ? 163 ILE C O     1 
ATOM   5137 C  CB    . ILE D 2 164 ? 3.815   19.152  40.586  1.00 54.55 ? 163 ILE C CB    1 
ATOM   5138 C  CG1   . ILE D 2 164 ? 5.309   19.182  40.864  1.00 53.00 ? 163 ILE C CG1   1 
ATOM   5139 C  CG2   . ILE D 2 164 ? 3.374   20.302  39.681  1.00 51.94 ? 163 ILE C CG2   1 
ATOM   5140 C  CD1   . ILE D 2 164 ? 6.136   18.438  39.868  1.00 52.77 ? 163 ILE C CD1   1 
ATOM   5141 N  N     . ARG D 2 165 ? 1.203   17.619  41.598  1.00 59.71 ? 164 ARG C N     1 
ATOM   5142 C  CA    . ARG D 2 165 ? -0.219  17.302  41.471  1.00 58.85 ? 164 ARG C CA    1 
ATOM   5143 C  C     . ARG D 2 165 ? -1.017  17.760  42.689  1.00 61.20 ? 164 ARG C C     1 
ATOM   5144 O  O     . ARG D 2 165 ? -2.135  18.276  42.547  1.00 58.66 ? 164 ARG C O     1 
ATOM   5145 C  CB    . ARG D 2 165 ? -0.422  15.804  41.250  1.00 55.21 ? 164 ARG C CB    1 
ATOM   5146 C  CG    . ARG D 2 165 ? 0.020   15.329  39.898  1.00 53.85 ? 164 ARG C CG    1 
ATOM   5147 C  CD    . ARG D 2 165 ? -0.926  14.263  39.376  1.00 52.75 ? 164 ARG C CD    1 
ATOM   5148 N  NE    . ARG D 2 165 ? -0.383  13.598  38.194  1.00 51.79 ? 164 ARG C NE    1 
ATOM   5149 C  CZ    . ARG D 2 165 ? -0.203  12.288  38.120  1.00 51.23 ? 164 ARG C CZ    1 
ATOM   5150 N  NH1   . ARG D 2 165 ? -0.528  11.491  39.121  1.00 49.59 ? 164 ARG C NH1   1 
ATOM   5151 N  NH2   . ARG D 2 165 ? 0.327   11.766  37.021  1.00 50.17 ? 164 ARG C NH2   1 
ATOM   5152 N  N     . LYS D 2 166 ? -0.465  17.581  43.894  1.00 61.35 ? 165 LYS C N     1 
ATOM   5153 C  CA    . LYS D 2 166 ? -1.254  17.872  45.095  1.00 64.07 ? 165 LYS C CA    1 
ATOM   5154 C  C     . LYS D 2 166 ? -1.454  19.370  45.284  1.00 63.91 ? 165 LYS C C     1 
ATOM   5155 O  O     . LYS D 2 166 ? -2.446  19.783  45.882  1.00 73.01 ? 165 LYS C O     1 
ATOM   5156 C  CB    . LYS D 2 166 ? -0.600  17.253  46.334  1.00 61.58 ? 165 LYS C CB    1 
ATOM   5157 N  N     . HIS D 2 167 ? -0.535  20.195  44.774  1.00 68.84 ? 166 HIS C N     1 
ATOM   5158 C  CA    . HIS D 2 167 ? -0.662  21.650  44.845  1.00 71.77 ? 166 HIS C CA    1 
ATOM   5159 C  C     . HIS D 2 167 ? -1.161  22.273  43.542  1.00 73.05 ? 166 HIS C C     1 
ATOM   5160 O  O     . HIS D 2 167 ? -1.290  23.500  43.472  1.00 78.23 ? 166 HIS C O     1 
ATOM   5161 C  CB    . HIS D 2 167 ? 0.683   22.285  45.239  1.00 70.88 ? 166 HIS C CB    1 
ATOM   5162 N  N     . LYS D 2 168 ? -1.453  21.471  42.519  1.00 68.33 ? 167 LYS C N     1 
ATOM   5163 C  CA    . LYS D 2 168 ? -1.749  22.005  41.188  1.00 67.51 ? 167 LYS C CA    1 
ATOM   5164 C  C     . LYS D 2 168 ? -3.201  22.449  41.089  1.00 67.35 ? 167 LYS C C     1 
ATOM   5165 O  O     . LYS D 2 168 ? -3.761  22.974  42.055  1.00 72.52 ? 167 LYS C O     1 
ATOM   5166 C  CB    . LYS D 2 168 ? -1.434  20.971  40.099  1.00 63.12 ? 167 LYS C CB    1 
HETATM 5167 C  C1    . ZNI E 3 .   ? 5.100   12.332  13.060  1.00 16.80 ? 201 ZNI B C1    1 
HETATM 5168 C  C10   . ZNI E 3 .   ? 10.646  14.858  5.754   1.00 18.60 ? 201 ZNI B C10   1 
HETATM 5169 C  C11   . ZNI E 3 .   ? 10.968  15.299  4.341   1.00 23.19 ? 201 ZNI B C11   1 
HETATM 5170 C  C12   . ZNI E 3 .   ? 10.378  13.083  4.189   1.00 20.71 ? 201 ZNI B C12   1 
HETATM 5171 C  C13   . ZNI E 3 .   ? 5.748   15.385  9.363   1.00 18.19 ? 201 ZNI B C13   1 
HETATM 5172 C  C14   . ZNI E 3 .   ? 6.174   16.606  10.116  1.00 19.98 ? 201 ZNI B C14   1 
HETATM 5173 C  C15   . ZNI E 3 .   ? 6.454   18.317  11.693  1.00 18.97 ? 201 ZNI B C15   1 
HETATM 5174 C  C16   . ZNI E 3 .   ? 7.438   18.717  10.840  1.00 22.29 ? 201 ZNI B C16   1 
HETATM 5175 C  C17   . ZNI E 3 .   ? 6.140   18.847  12.988  1.00 19.30 ? 201 ZNI B C17   1 
HETATM 5176 C  C18   . ZNI E 3 .   ? 5.574   18.004  13.917  1.00 20.04 ? 201 ZNI B C18   1 
HETATM 5177 C  C19   . ZNI E 3 .   ? 5.295   18.442  15.250  1.00 19.97 ? 201 ZNI B C19   1 
HETATM 5178 C  C2    . ZNI E 3 .   ? 5.822   13.628  12.591  1.00 16.87 ? 201 ZNI B C2    1 
HETATM 5179 C  C20   . ZNI E 3 .   ? 5.649   19.753  15.625  1.00 19.06 ? 201 ZNI B C20   1 
HETATM 5180 C  C21   . ZNI E 3 .   ? 6.283   20.621  14.677  1.00 20.59 ? 201 ZNI B C21   1 
HETATM 5181 C  C22   . ZNI E 3 .   ? 6.510   20.173  13.380  1.00 19.22 ? 201 ZNI B C22   1 
HETATM 5182 C  C23   . ZNI E 3 .   ? 5.401   21.123  17.716  1.00 24.52 ? 201 ZNI B C23   1 
HETATM 5183 C  C24   . ZNI E 3 .   ? 4.340   22.086  17.176  1.00 26.90 ? 201 ZNI B C24   1 
HETATM 5184 C  C25   . ZNI E 3 .   ? 4.702   18.710  17.433  1.00 19.78 ? 201 ZNI B C25   1 
HETATM 5185 C  C26   . ZNI E 3 .   ? 4.169   18.607  18.768  1.00 22.21 ? 201 ZNI B C26   1 
HETATM 5186 C  C27   . ZNI E 3 .   ? 4.997   18.649  19.943  1.00 25.22 ? 201 ZNI B C27   1 
HETATM 5187 C  C28   . ZNI E 3 .   ? 6.537   18.797  19.886  1.00 23.47 ? 201 ZNI B C28   1 
HETATM 5188 C  C29   . ZNI E 3 .   ? 8.178   20.598  19.869  1.00 24.45 ? 201 ZNI B C29   1 
HETATM 5189 C  C3    . ZNI E 3 .   ? 5.766   11.218  10.891  1.00 16.35 ? 201 ZNI B C3    1 
HETATM 5190 C  C30   . ZNI E 3 .   ? 7.257   17.805  20.824  1.00 23.66 ? 201 ZNI B C30   1 
HETATM 5191 C  C31   . ZNI E 3 .   ? 3.115   18.473  21.328  1.00 25.54 ? 201 ZNI B C31   1 
HETATM 5192 C  C32   . ZNI E 3 .   ? 2.203   18.433  20.271  1.00 25.91 ? 201 ZNI B C32   1 
HETATM 5193 C  C33   . ZNI E 3 .   ? 0.156   17.312  19.394  1.00 30.39 ? 201 ZNI B C33   1 
HETATM 5194 C  C34   . ZNI E 3 .   ? -1.395  17.377  19.412  1.00 31.74 ? 201 ZNI B C34   1 
HETATM 5195 C  C35   . ZNI E 3 .   ? -3.348  17.194  20.675  1.00 40.37 ? 201 ZNI B C35   1 
HETATM 5196 C  C36   . ZNI E 3 .   ? -4.324  16.634  21.683  1.00 36.88 ? 201 ZNI B C36   1 
HETATM 5197 C  C37   . ZNI E 3 .   ? -4.071  15.890  20.377  1.00 36.89 ? 201 ZNI B C37   1 
HETATM 5198 C  C38   . ZNI E 3 .   ? -1.296  17.954  21.728  1.00 33.10 ? 201 ZNI B C38   1 
HETATM 5199 C  C39   . ZNI E 3 .   ? 0.255   18.028  21.723  1.00 32.27 ? 201 ZNI B C39   1 
HETATM 5200 C  C4    . ZNI E 3 .   ? 4.600   11.519  11.842  1.00 15.60 ? 201 ZNI B C4    1 
HETATM 5201 C  C40   . ZNI E 3 .   ? 2.790   18.516  18.987  1.00 24.63 ? 201 ZNI B C40   1 
HETATM 5202 C  C41   . ZNI E 3 .   ? 4.666   17.799  16.428  1.00 20.06 ? 201 ZNI B C41   1 
HETATM 5203 C  C42   . ZNI E 3 .   ? 4.054   16.374  16.521  1.00 19.68 ? 201 ZNI B C42   1 
HETATM 5204 C  C43   . ZNI E 3 .   ? 4.978   15.239  16.934  1.00 18.40 ? 201 ZNI B C43   1 
HETATM 5205 C  C44   . ZNI E 3 .   ? 4.154   13.968  16.960  1.00 19.43 ? 201 ZNI B C44   1 
HETATM 5206 C  C45   . ZNI E 3 .   ? 5.602   15.572  18.324  1.00 16.83 ? 201 ZNI B C45   1 
HETATM 5207 C  C46   . ZNI E 3 .   ? 6.157   15.168  15.933  1.00 16.78 ? 201 ZNI B C46   1 
HETATM 5208 C  C47   . ZNI E 3 .   ? 6.497   14.203  13.780  1.00 16.55 ? 201 ZNI B C47   1 
HETATM 5209 C  C5    . ZNI E 3 .   ? 6.386   13.035  9.292   1.00 17.22 ? 201 ZNI B C5    1 
HETATM 5210 C  C6    . ZNI E 3 .   ? 6.952   14.460  9.141   1.00 16.31 ? 201 ZNI B C6    1 
HETATM 5211 C  C7    . ZNI E 3 .   ? 8.821   14.322  7.578   1.00 18.11 ? 201 ZNI B C7    1 
HETATM 5212 C  C8    . ZNI E 3 .   ? 9.239   14.408  6.182   1.00 17.79 ? 201 ZNI B C8    1 
HETATM 5213 C  C9    . ZNI E 3 .   ? 10.262  13.408  5.666   1.00 21.29 ? 201 ZNI B C9    1 
HETATM 5214 N  N1    . ZNI E 3 .   ? 6.863   13.287  11.611  1.00 16.62 ? 201 ZNI B N1    1 
HETATM 5215 N  N2    . ZNI E 3 .   ? 6.311   12.502  10.592  1.00 16.56 ? 201 ZNI B N2    1 
HETATM 5216 N  N3    . ZNI E 3 .   ? 7.521   14.560  7.843   1.00 19.96 ? 201 ZNI B N3    1 
HETATM 5217 N  N4    . ZNI E 3 .   ? 5.851   17.061  11.279  1.00 18.06 ? 201 ZNI B N4    1 
HETATM 5218 N  N5    . ZNI E 3 .   ? 5.281   19.896  16.947  1.00 21.91 ? 201 ZNI B N5    1 
HETATM 5219 N  N6    . ZNI E 3 .   ? 4.456   18.584  21.162  1.00 24.51 ? 201 ZNI B N6    1 
HETATM 5220 N  N7    . ZNI E 3 .   ? 0.771   18.296  20.371  1.00 29.30 ? 201 ZNI B N7    1 
HETATM 5221 N  N8    . ZNI E 3 .   ? -1.911  17.087  20.740  1.00 35.33 ? 201 ZNI B N8    1 
HETATM 5222 O  O1    . ZNI E 3 .   ? 6.006   12.410  8.304   1.00 17.48 ? 201 ZNI B O1    1 
HETATM 5223 O  O2    . ZNI E 3 .   ? 9.673   14.060  8.451   1.00 15.65 ? 201 ZNI B O2    1 
HETATM 5224 O  O3    . ZNI E 3 .   ? 10.221  14.324  3.618   1.00 20.61 ? 201 ZNI B O3    1 
HETATM 5225 O  O4    . ZNI E 3 .   ? 6.862   20.129  20.250  1.00 26.93 ? 201 ZNI B O4    1 
HETATM 5226 O  O5    . ZNI E 3 .   ? 5.656   14.670  14.651  1.00 15.17 ? 201 ZNI B O5    1 
HETATM 5227 O  O6    . ZNI E 3 .   ? 7.715   14.174  13.998  1.00 18.06 ? 201 ZNI B O6    1 
HETATM 5228 S  S1    . ZNI E 3 .   ? 7.534   17.626  9.468   1.00 21.31 ? 201 ZNI B S1    1 
HETATM 5229 C  C1    . ZNI F 3 .   ? 34.257  28.444  30.461  1.00 25.00 ? 201 ZNI D C1    1 
HETATM 5230 C  C10   . ZNI F 3 .   ? 35.232  19.260  33.330  1.00 35.19 ? 201 ZNI D C10   1 
HETATM 5231 C  C11   . ZNI F 3 .   ? 35.599  18.095  34.190  1.00 36.39 ? 201 ZNI D C11   1 
HETATM 5232 C  C12   . ZNI F 3 .   ? 37.631  19.075  33.468  1.00 35.37 ? 201 ZNI D C12   1 
HETATM 5233 C  C13   . ZNI F 3 .   ? 33.783  25.261  34.170  1.00 31.48 ? 201 ZNI D C13   1 
HETATM 5234 C  C14   . ZNI F 3 .   ? 32.258  25.199  34.100  1.00 31.59 ? 201 ZNI D C14   1 
HETATM 5235 C  C15   . ZNI F 3 .   ? 29.989  25.645  33.843  1.00 35.45 ? 201 ZNI D C15   1 
HETATM 5236 C  C16   . ZNI F 3 .   ? 29.940  24.311  34.099  1.00 38.64 ? 201 ZNI D C16   1 
HETATM 5237 C  C17   . ZNI F 3 .   ? 28.894  26.521  33.489  1.00 30.80 ? 201 ZNI D C17   1 
HETATM 5238 C  C18   . ZNI F 3 .   ? 29.106  27.679  32.743  1.00 30.89 ? 201 ZNI D C18   1 
HETATM 5239 C  C19   . ZNI F 3 .   ? 28.066  28.571  32.281  1.00 29.80 ? 201 ZNI D C19   1 
HETATM 5240 C  C2    . ZNI F 3 .   ? 33.312  27.368  31.078  1.00 25.09 ? 201 ZNI D C2    1 
HETATM 5241 C  C20   . ZNI F 3 .   ? 26.730  28.183  32.555  1.00 31.57 ? 201 ZNI D C20   1 
HETATM 5242 C  C21   . ZNI F 3 .   ? 26.489  26.970  33.282  1.00 33.64 ? 201 ZNI D C21   1 
HETATM 5243 C  C22   . ZNI F 3 .   ? 27.521  26.155  33.714  1.00 33.01 ? 201 ZNI D C22   1 
HETATM 5244 C  C23   . ZNI F 3 .   ? 24.448  29.122  32.179  1.00 33.47 ? 201 ZNI D C23   1 
HETATM 5245 C  C24   . ZNI F 3 .   ? 24.078  29.886  33.476  1.00 36.54 ? 201 ZNI D C24   1 
HETATM 5246 C  C25   . ZNI F 3 .   ? 26.639  30.192  31.419  1.00 30.65 ? 201 ZNI D C25   1 
HETATM 5247 C  C26   . ZNI F 3 .   ? 26.034  31.400  30.836  1.00 31.50 ? 201 ZNI D C26   1 
HETATM 5248 C  C27   . ZNI F 3 .   ? 25.216  31.415  29.673  1.00 31.31 ? 201 ZNI D C27   1 
HETATM 5249 C  C28   . ZNI F 3 .   ? 24.876  30.052  28.896  1.00 27.27 ? 201 ZNI D C28   1 
HETATM 5250 C  C29   . ZNI F 3 .   ? 23.247  28.235  28.833  1.00 35.66 ? 201 ZNI D C29   1 
HETATM 5251 C  C3    . ZNI F 3 .   ? 36.173  26.838  30.820  1.00 23.94 ? 201 ZNI D C3    1 
HETATM 5252 C  C30   . ZNI F 3 .   ? 25.153  30.128  27.355  1.00 28.03 ? 201 ZNI D C30   1 
HETATM 5253 C  C31   . ZNI F 3 .   ? 25.017  33.801  29.772  1.00 35.41 ? 201 ZNI D C31   1 
HETATM 5254 C  C32   . ZNI F 3 .   ? 25.800  33.951  30.915  1.00 36.81 ? 201 ZNI D C32   1 
HETATM 5255 C  C33   . ZNI F 3 .   ? 27.115  35.250  32.695  1.00 42.40 ? 201 ZNI D C33   1 
HETATM 5256 C  C34   . ZNI F 3 .   ? 27.842  36.615  32.725  1.00 42.06 ? 201 ZNI D C34   1 
HETATM 5257 C  C35   . ZNI F 3 .   ? 27.751  38.897  32.966  1.00 45.04 ? 201 ZNI D C35   1 
HETATM 5258 C  C36   . ZNI F 3 .   ? 27.674  39.863  34.128  1.00 44.83 ? 201 ZNI D C36   1 
HETATM 5259 C  C37   . ZNI F 3 .   ? 26.995  40.197  32.800  1.00 43.19 ? 201 ZNI D C37   1 
HETATM 5260 C  C38   . ZNI F 3 .   ? 26.111  37.688  31.531  1.00 47.77 ? 201 ZNI D C38   1 
HETATM 5261 C  C39   . ZNI F 3 .   ? 25.242  36.383  31.467  1.00 43.10 ? 201 ZNI D C39   1 
HETATM 5262 C  C4    . ZNI F 3 .   ? 35.664  28.283  30.986  1.00 24.38 ? 201 ZNI D C4    1 
HETATM 5263 C  C40   . ZNI F 3 .   ? 26.278  32.685  31.423  1.00 32.78 ? 201 ZNI D C40   1 
HETATM 5264 C  C41   . ZNI F 3 .   ? 27.994  29.868  31.581  1.00 30.58 ? 201 ZNI D C41   1 
HETATM 5265 C  C42   . ZNI F 3 .   ? 29.229  30.675  31.080  1.00 29.79 ? 201 ZNI D C42   1 
HETATM 5266 C  C43   . ZNI F 3 .   ? 29.779  30.323  29.669  1.00 26.28 ? 201 ZNI D C43   1 
HETATM 5267 C  C44   . ZNI F 3 .   ? 31.068  31.152  29.324  1.00 26.41 ? 201 ZNI D C44   1 
HETATM 5268 C  C45   . ZNI F 3 .   ? 28.679  30.558  28.614  1.00 23.47 ? 201 ZNI D C45   1 
HETATM 5269 C  C46   . ZNI F 3 .   ? 30.145  28.820  29.602  1.00 25.27 ? 201 ZNI D C46   1 
HETATM 5270 C  C47   . ZNI F 3 .   ? 32.072  27.418  30.226  1.00 27.91 ? 201 ZNI D C47   1 
HETATM 5271 C  C5    . ZNI F 3 .   ? 35.502  25.143  32.497  1.00 27.48 ? 201 ZNI D C5    1 
HETATM 5272 C  C6    . ZNI F 3 .   ? 34.359  24.293  33.146  1.00 30.49 ? 201 ZNI D C6    1 
HETATM 5273 C  C7    . ZNI F 3 .   ? 34.961  21.934  32.991  1.00 32.14 ? 201 ZNI D C7    1 
HETATM 5274 C  C8    . ZNI F 3 .   ? 35.596  20.734  33.537  1.00 31.01 ? 201 ZNI D C8    1 
HETATM 5275 C  C9    . ZNI F 3 .   ? 36.513  19.804  32.773  1.00 34.07 ? 201 ZNI D C9    1 
HETATM 5276 N  N1    . ZNI F 3 .   ? 33.871  26.026  30.964  1.00 25.33 ? 201 ZNI D N1    1 
HETATM 5277 N  N2    . ZNI F 3 .   ? 35.197  26.000  31.448  1.00 25.79 ? 201 ZNI D N2    1 
HETATM 5278 N  N3    . ZNI F 3 .   ? 34.912  23.085  33.708  1.00 31.60 ? 201 ZNI D N3    1 
HETATM 5279 N  N4    . ZNI F 3 .   ? 31.362  26.092  33.855  1.00 27.70 ? 201 ZNI D N4    1 
HETATM 5280 N  N5    . ZNI F 3 .   ? 25.888  29.146  32.047  1.00 32.47 ? 201 ZNI D N5    1 
HETATM 5281 N  N6    . ZNI F 3 .   ? 24.734  32.588  29.218  1.00 30.96 ? 201 ZNI D N6    1 
HETATM 5282 N  N7    . ZNI F 3 .   ? 26.133  35.181  31.552  1.00 37.12 ? 201 ZNI D N7    1 
HETATM 5283 N  N8    . ZNI F 3 .   ? 26.947  37.740  32.716  1.00 42.99 ? 201 ZNI D N8    1 
HETATM 5284 O  O1    . ZNI F 3 .   ? 36.636  25.052  32.957  1.00 28.09 ? 201 ZNI D O1    1 
HETATM 5285 O  O2    . ZNI F 3 .   ? 34.454  21.927  31.868  1.00 30.06 ? 201 ZNI D O2    1 
HETATM 5286 O  O3    . ZNI F 3 .   ? 36.953  18.441  34.560  1.00 36.86 ? 201 ZNI D O3    1 
HETATM 5287 O  O4    . ZNI F 3 .   ? 23.546  29.617  29.086  1.00 29.47 ? 201 ZNI D O4    1 
HETATM 5288 O  O5    . ZNI F 3 .   ? 31.327  28.555  30.416  1.00 22.54 ? 201 ZNI D O5    1 
HETATM 5289 O  O6    . ZNI F 3 .   ? 31.757  26.526  29.425  1.00 26.98 ? 201 ZNI D O6    1 
HETATM 5290 S  S1    . ZNI F 3 .   ? 31.489  23.586  34.380  1.00 38.61 ? 201 ZNI D S1    1 
HETATM 5291 P  PB    . GDP G 4 .   ? 10.939  26.206  5.622   1.00 19.34 ? 201 GDP A PB    1 
HETATM 5292 O  O1B   . GDP G 4 .   ? 11.922  26.122  6.731   1.00 18.77 ? 201 GDP A O1B   1 
HETATM 5293 O  O2B   . GDP G 4 .   ? 10.302  27.577  5.596   1.00 18.77 ? 201 GDP A O2B   1 
HETATM 5294 O  O3B   . GDP G 4 .   ? 9.883   25.121  5.667   1.00 21.67 ? 201 GDP A O3B   1 
HETATM 5295 O  O3A   . GDP G 4 .   ? 11.704  26.130  4.204   1.00 20.33 ? 201 GDP A O3A   1 
HETATM 5296 P  PA    . GDP G 4 .   ? 13.143  25.481  3.941   1.00 21.15 ? 201 GDP A PA    1 
HETATM 5297 O  O1A   . GDP G 4 .   ? 14.311  26.313  4.441   1.00 20.24 ? 201 GDP A O1A   1 
HETATM 5298 O  O2A   . GDP G 4 .   ? 13.175  24.048  4.402   1.00 21.72 ? 201 GDP A O2A   1 
HETATM 5299 O  "O5'" . GDP G 4 .   ? 13.272  25.425  2.337   1.00 20.62 ? 201 GDP A "O5'" 1 
HETATM 5300 C  "C5'" . GDP G 4 .   ? 12.208  24.723  1.678   1.00 22.24 ? 201 GDP A "C5'" 1 
HETATM 5301 C  "C4'" . GDP G 4 .   ? 12.738  24.449  0.280   1.00 27.23 ? 201 GDP A "C4'" 1 
HETATM 5302 O  "O4'" . GDP G 4 .   ? 12.925  25.699  -0.406  1.00 23.97 ? 201 GDP A "O4'" 1 
HETATM 5303 C  "C3'" . GDP G 4 .   ? 14.105  23.749  0.319   1.00 25.75 ? 201 GDP A "C3'" 1 
HETATM 5304 O  "O3'" . GDP G 4 .   ? 14.142  22.991  -0.899  1.00 30.07 ? 201 GDP A "O3'" 1 
HETATM 5305 C  "C2'" . GDP G 4 .   ? 15.093  24.857  0.085   1.00 25.04 ? 201 GDP A "C2'" 1 
HETATM 5306 O  "O2'" . GDP G 4 .   ? 16.274  24.389  -0.573  1.00 30.56 ? 201 GDP A "O2'" 1 
HETATM 5307 C  "C1'" . GDP G 4 .   ? 14.310  25.767  -0.845  1.00 26.11 ? 201 GDP A "C1'" 1 
HETATM 5308 N  N9    . GDP G 4 .   ? 14.741  27.150  -0.624  1.00 24.93 ? 201 GDP A N9    1 
HETATM 5309 C  C8    . GDP G 4 .   ? 14.737  27.797  0.589   1.00 23.00 ? 201 GDP A C8    1 
HETATM 5310 N  N7    . GDP G 4 .   ? 15.168  29.080  0.406   1.00 22.65 ? 201 GDP A N7    1 
HETATM 5311 C  C5    . GDP G 4 .   ? 15.350  29.277  -0.950  1.00 23.78 ? 201 GDP A C5    1 
HETATM 5312 C  C6    . GDP G 4 .   ? 15.808  30.378  -1.844  1.00 23.19 ? 201 GDP A C6    1 
HETATM 5313 O  O6    . GDP G 4 .   ? 16.062  31.517  -1.372  1.00 23.58 ? 201 GDP A O6    1 
HETATM 5314 N  N1    . GDP G 4 .   ? 15.929  30.135  -3.176  1.00 25.71 ? 201 GDP A N1    1 
HETATM 5315 C  C2    . GDP G 4 .   ? 15.676  28.933  -3.744  1.00 25.68 ? 201 GDP A C2    1 
HETATM 5316 N  N2    . GDP G 4 .   ? 15.815  28.782  -5.107  1.00 27.74 ? 201 GDP A N2    1 
HETATM 5317 N  N3    . GDP G 4 .   ? 15.268  27.868  -2.977  1.00 25.36 ? 201 GDP A N3    1 
HETATM 5318 C  C4    . GDP G 4 .   ? 15.106  27.988  -1.612  1.00 24.82 ? 201 GDP A C4    1 
HETATM 5319 MG MG    . MG  H 5 .   ? 12.115  24.898  8.317   1.00 16.72 ? 202 MG  A MG    1 
HETATM 5320 P  PB    . GDP I 4 .   ? 26.418  16.729  39.520  1.00 43.96 ? 201 GDP C PB    1 
HETATM 5321 O  O1B   . GDP I 4 .   ? 25.520  16.633  38.257  1.00 42.60 ? 201 GDP C O1B   1 
HETATM 5322 O  O2B   . GDP I 4 .   ? 27.474  17.740  39.181  1.00 44.73 ? 201 GDP C O2B   1 
HETATM 5323 O  O3B   . GDP I 4 .   ? 25.660  17.099  40.760  1.00 44.78 ? 201 GDP C O3B   1 
HETATM 5324 O  O3A   . GDP I 4 .   ? 27.081  15.330  39.859  1.00 45.99 ? 201 GDP C O3A   1 
HETATM 5325 P  PA    . GDP I 4 .   ? 27.330  14.225  38.702  1.00 44.15 ? 201 GDP C PA    1 
HETATM 5326 O  O1A   . GDP I 4 .   ? 26.053  13.562  38.242  1.00 42.32 ? 201 GDP C O1A   1 
HETATM 5327 O  O2A   . GDP I 4 .   ? 28.072  14.907  37.528  1.00 43.55 ? 201 GDP C O2A   1 
HETATM 5328 O  "O5'" . GDP I 4 .   ? 28.264  13.232  39.604  1.00 46.55 ? 201 GDP C "O5'" 1 
HETATM 5329 C  "C5'" . GDP I 4 .   ? 29.472  13.697  40.228  1.00 48.80 ? 201 GDP C "C5'" 1 
HETATM 5330 C  "C4'" . GDP I 4 .   ? 30.367  12.495  40.548  1.00 50.76 ? 201 GDP C "C4'" 1 
HETATM 5331 O  "O4'" . GDP I 4 .   ? 29.643  11.756  41.531  1.00 51.27 ? 201 GDP C "O4'" 1 
HETATM 5332 C  "C3'" . GDP I 4 .   ? 30.539  11.543  39.348  1.00 49.81 ? 201 GDP C "C3'" 1 
HETATM 5333 O  "O3'" . GDP I 4 .   ? 31.824  10.936  39.361  1.00 52.00 ? 201 GDP C "O3'" 1 
HETATM 5334 C  "C2'" . GDP I 4 .   ? 29.451  10.495  39.575  1.00 48.97 ? 201 GDP C "C2'" 1 
HETATM 5335 O  "O2'" . GDP I 4 .   ? 29.594  9.220   38.913  1.00 48.96 ? 201 GDP C "O2'" 1 
HETATM 5336 C  "C1'" . GDP I 4 .   ? 29.469  10.412  41.103  1.00 50.98 ? 201 GDP C "C1'" 1 
HETATM 5337 N  N9    . GDP I 4 .   ? 28.161  9.934   41.616  1.00 50.12 ? 201 GDP C N9    1 
HETATM 5338 C  C8    . GDP I 4 .   ? 26.941  10.388  41.249  1.00 49.01 ? 201 GDP C C8    1 
HETATM 5339 N  N7    . GDP I 4 .   ? 25.976  9.716   41.921  1.00 48.28 ? 201 GDP C N7    1 
HETATM 5340 C  C5    . GDP I 4 .   ? 26.569  8.822   42.744  1.00 50.22 ? 201 GDP C C5    1 
HETATM 5341 C  C6    . GDP I 4 .   ? 26.149  7.811   43.748  1.00 52.17 ? 201 GDP C C6    1 
HETATM 5342 O  O6    . GDP I 4 .   ? 24.936  7.600   43.998  1.00 55.48 ? 201 GDP C O6    1 
HETATM 5343 N  N1    . GDP I 4 .   ? 27.108  7.094   44.366  1.00 54.10 ? 201 GDP C N1    1 
HETATM 5344 C  C2    . GDP I 4 .   ? 28.423  7.274   44.135  1.00 55.48 ? 201 GDP C C2    1 
HETATM 5345 N  N2    . GDP I 4 .   ? 29.340  6.512   44.804  1.00 58.09 ? 201 GDP C N2    1 
HETATM 5346 N  N3    . GDP I 4 .   ? 28.884  8.197   43.224  1.00 54.14 ? 201 GDP C N3    1 
HETATM 5347 C  C4    . GDP I 4 .   ? 28.016  8.976   42.533  1.00 51.62 ? 201 GDP C C4    1 
HETATM 5348 MG MG    . MG  J 5 .   ? 25.597  17.747  36.444  1.00 39.62 ? 202 MG  C MG    1 
HETATM 5349 AL AL    . AF3 K 6 .   ? 25.068  18.997  40.362  1.00 43.90 ? 203 AF3 C AL    1 
HETATM 5350 F  F1    . AF3 K 6 .   ? 23.953  19.061  41.760  1.00 55.62 ? 203 AF3 C F1    1 
HETATM 5351 F  F2    . AF3 K 6 .   ? 26.432  20.159  40.328  1.00 48.84 ? 203 AF3 C F2    1 
HETATM 5352 F  F3    . AF3 K 6 .   ? 24.433  18.441  38.779  1.00 45.33 ? 203 AF3 C F3    1 
HETATM 5353 O  O     . HOH L 7 .   ? 18.325  0.591   30.294  1.00 39.17 ? 301 HOH B O     1 
HETATM 5354 O  O     . HOH L 7 .   ? 28.908  -1.144  24.434  1.00 40.52 ? 302 HOH B O     1 
HETATM 5355 O  O     . HOH L 7 .   ? 8.889   4.777   26.653  1.00 37.47 ? 303 HOH B O     1 
HETATM 5356 O  O     . HOH L 7 .   ? 9.613   -0.584  28.639  1.00 35.51 ? 304 HOH B O     1 
HETATM 5357 O  O     . HOH L 7 .   ? 21.272  -9.063  6.449   1.00 42.41 ? 305 HOH B O     1 
HETATM 5358 O  O     . HOH L 7 .   ? -4.411  -7.284  0.046   1.00 35.45 ? 306 HOH B O     1 
HETATM 5359 O  O     . HOH L 7 .   ? 18.759  11.984  24.559  1.00 31.96 ? 307 HOH B O     1 
HETATM 5360 O  O     . HOH L 7 .   ? 18.301  -9.016  0.269   1.00 42.50 ? 308 HOH B O     1 
HETATM 5361 O  O     . HOH L 7 .   ? 1.183   -9.573  14.588  1.00 39.47 ? 309 HOH B O     1 
HETATM 5362 O  O     . HOH L 7 .   ? -3.842  0.428   19.188  1.00 35.05 ? 310 HOH B O     1 
HETATM 5363 O  O     . HOH L 7 .   ? 7.749   7.994   3.639   1.00 17.81 ? 311 HOH B O     1 
HETATM 5364 O  O     . HOH L 7 .   ? 26.069  0.333   26.994  1.00 41.88 ? 312 HOH B O     1 
HETATM 5365 O  O     . HOH L 7 .   ? 0.978   14.728  5.982   1.00 33.67 ? 313 HOH B O     1 
HETATM 5366 O  O     . HOH L 7 .   ? 17.556  10.287  -1.940  1.00 34.40 ? 314 HOH B O     1 
HETATM 5367 O  O     . HOH L 7 .   ? 10.044  -8.315  -4.778  1.00 46.01 ? 315 HOH B O     1 
HETATM 5368 O  O     . HOH L 7 .   ? 12.831  3.928   -6.118  1.00 34.03 ? 316 HOH B O     1 
HETATM 5369 O  O     . HOH L 7 .   ? 16.750  -2.736  -8.108  1.00 41.81 ? 317 HOH B O     1 
HETATM 5370 O  O     . HOH L 7 .   ? -4.499  -1.177  -2.654  1.00 34.26 ? 318 HOH B O     1 
HETATM 5371 O  O     . HOH L 7 .   ? 12.035  -7.519  24.162  1.00 30.15 ? 319 HOH B O     1 
HETATM 5372 O  O     . HOH L 7 .   ? 19.919  -10.683 12.544  1.00 40.53 ? 320 HOH B O     1 
HETATM 5373 O  O     . HOH L 7 .   ? 1.401   8.688   4.211   1.00 20.83 ? 321 HOH B O     1 
HETATM 5374 O  O     . HOH L 7 .   ? 16.225  14.577  14.147  1.00 27.08 ? 322 HOH B O     1 
HETATM 5375 O  O     . HOH L 7 .   ? 14.803  -3.624  -1.305  1.00 30.55 ? 323 HOH B O     1 
HETATM 5376 O  O     . HOH L 7 .   ? 14.722  10.915  -1.338  1.00 33.15 ? 324 HOH B O     1 
HETATM 5377 O  O     . HOH L 7 .   ? -4.222  4.750   7.333   1.00 18.74 ? 325 HOH B O     1 
HETATM 5378 O  O     . HOH L 7 .   ? 20.355  -5.735  17.956  1.00 28.64 ? 326 HOH B O     1 
HETATM 5379 O  O     . HOH L 7 .   ? 4.014   1.231   24.748  1.00 32.36 ? 327 HOH B O     1 
HETATM 5380 O  O     . HOH L 7 .   ? 3.967   -7.761  0.809   1.00 32.10 ? 328 HOH B O     1 
HETATM 5381 O  O     . HOH L 7 .   ? -7.466  4.158   20.160  1.00 37.48 ? 329 HOH B O     1 
HETATM 5382 O  O     . HOH L 7 .   ? 1.919   -3.210  19.006  1.00 33.06 ? 330 HOH B O     1 
HETATM 5383 O  O     . HOH L 7 .   ? 2.991   -3.833  -4.683  1.00 32.33 ? 331 HOH B O     1 
HETATM 5384 O  O     . HOH L 7 .   ? 21.004  -1.184  3.329   1.00 29.47 ? 332 HOH B O     1 
HETATM 5385 O  O     . HOH L 7 .   ? 17.289  18.532  20.762  1.00 30.80 ? 333 HOH B O     1 
HETATM 5386 O  O     . HOH L 7 .   ? 1.920   11.050  1.573   1.00 17.41 ? 334 HOH B O     1 
HETATM 5387 O  O     . HOH L 7 .   ? 19.036  12.518  15.392  1.00 23.24 ? 335 HOH B O     1 
HETATM 5388 O  O     . HOH L 7 .   ? 16.043  3.725   9.708   1.00 21.75 ? 336 HOH B O     1 
HETATM 5389 O  O     . HOH L 7 .   ? 7.881   -11.901 15.787  1.00 41.19 ? 337 HOH B O     1 
HETATM 5390 O  O     . HOH L 7 .   ? 13.774  15.839  14.474  1.00 23.12 ? 338 HOH B O     1 
HETATM 5391 O  O     . HOH L 7 .   ? 12.599  -8.425  21.556  1.00 34.49 ? 339 HOH B O     1 
HETATM 5392 O  O     . HOH L 7 .   ? 8.536   9.772   -7.150  1.00 27.22 ? 340 HOH B O     1 
HETATM 5393 O  O     . HOH L 7 .   ? 1.556   12.058  23.748  1.00 31.75 ? 341 HOH B O     1 
HETATM 5394 O  O     . HOH L 7 .   ? -6.947  13.276  11.944  1.00 36.41 ? 342 HOH B O     1 
HETATM 5395 O  O     . HOH L 7 .   ? 1.580   -6.667  0.274   1.00 33.86 ? 343 HOH B O     1 
HETATM 5396 O  O     . HOH L 7 .   ? 12.510  13.592  8.911   1.00 19.60 ? 344 HOH B O     1 
HETATM 5397 O  O     . HOH L 7 .   ? -1.755  6.867   23.975  1.00 31.40 ? 345 HOH B O     1 
HETATM 5398 O  O     . HOH L 7 .   ? -0.504  3.621   -3.052  1.00 31.84 ? 346 HOH B O     1 
HETATM 5399 O  O     . HOH L 7 .   ? 21.670  2.643   2.369   1.00 27.99 ? 347 HOH B O     1 
HETATM 5400 O  O     . HOH L 7 .   ? 5.644   5.781   -7.682  1.00 34.76 ? 348 HOH B O     1 
HETATM 5401 O  O     . HOH L 7 .   ? 17.429  -3.841  4.082   1.00 25.81 ? 349 HOH B O     1 
HETATM 5402 O  O     . HOH L 7 .   ? 24.732  -0.826  13.530  1.00 33.79 ? 350 HOH B O     1 
HETATM 5403 O  O     . HOH L 7 .   ? 16.542  7.762   8.825   1.00 20.07 ? 351 HOH B O     1 
HETATM 5404 O  O     . HOH L 7 .   ? 19.724  6.692   8.171   1.00 22.65 ? 352 HOH B O     1 
HETATM 5405 O  O     . HOH L 7 .   ? 24.220  -2.914  9.621   1.00 41.36 ? 353 HOH B O     1 
HETATM 5406 O  O     . HOH L 7 .   ? 25.544  1.942   23.416  1.00 38.55 ? 354 HOH B O     1 
HETATM 5407 O  O     . HOH L 7 .   ? -12.895 6.818   9.157   1.00 42.97 ? 355 HOH B O     1 
HETATM 5408 O  O     . HOH L 7 .   ? 15.010  8.479   -5.447  1.00 39.18 ? 356 HOH B O     1 
HETATM 5409 O  O     . HOH L 7 .   ? 19.240  14.414  21.995  1.00 27.68 ? 357 HOH B O     1 
HETATM 5410 O  O     . HOH L 7 .   ? 5.870   1.372   2.949   1.00 20.87 ? 358 HOH B O     1 
HETATM 5411 O  O     . HOH L 7 .   ? 0.473   4.605   0.667   1.00 18.98 ? 359 HOH B O     1 
HETATM 5412 O  O     . HOH L 7 .   ? 12.755  -13.353 15.813  1.00 37.54 ? 360 HOH B O     1 
HETATM 5413 O  O     . HOH L 7 .   ? -0.877  14.910  -4.760  1.00 32.70 ? 361 HOH B O     1 
HETATM 5414 O  O     . HOH L 7 .   ? 6.748   -12.955 6.655   1.00 43.03 ? 362 HOH B O     1 
HETATM 5415 O  O     . HOH L 7 .   ? 1.736   16.950  -1.760  1.00 32.09 ? 363 HOH B O     1 
HETATM 5416 O  O     . HOH L 7 .   ? 1.755   15.445  9.731   1.00 24.96 ? 364 HOH B O     1 
HETATM 5417 O  O     . HOH L 7 .   ? 5.745   -6.136  21.993  1.00 33.29 ? 365 HOH B O     1 
HETATM 5418 O  O     . HOH L 7 .   ? -3.944  11.610  -0.434  1.00 27.79 ? 366 HOH B O     1 
HETATM 5419 O  O     . HOH L 7 .   ? -6.817  7.330   16.270  1.00 27.09 ? 367 HOH B O     1 
HETATM 5420 O  O     . HOH L 7 .   ? 19.971  7.926   15.840  1.00 21.98 ? 368 HOH B O     1 
HETATM 5421 O  O     . HOH L 7 .   ? 24.194  2.151   16.250  1.00 25.28 ? 369 HOH B O     1 
HETATM 5422 O  O     . HOH L 7 .   ? 1.909   5.992   25.745  1.00 25.23 ? 370 HOH B O     1 
HETATM 5423 O  O     . HOH L 7 .   ? 12.849  12.393  0.001   1.00 33.14 ? 371 HOH B O     1 
HETATM 5424 O  O     . HOH L 7 .   ? 15.551  -8.917  21.340  1.00 34.11 ? 372 HOH B O     1 
HETATM 5425 O  O     . HOH L 7 .   ? 25.131  1.904   10.172  1.00 37.38 ? 373 HOH B O     1 
HETATM 5426 O  O     . HOH L 7 .   ? 18.805  -7.847  18.206  1.00 32.89 ? 374 HOH B O     1 
HETATM 5427 O  O     . HOH L 7 .   ? 26.588  8.741   20.406  1.00 40.44 ? 375 HOH B O     1 
HETATM 5428 O  O     . HOH L 7 .   ? 20.393  2.784   -4.570  1.00 40.13 ? 376 HOH B O     1 
HETATM 5429 O  O     . HOH L 7 .   ? 12.356  -1.439  -7.175  1.00 38.55 ? 377 HOH B O     1 
HETATM 5430 O  O     . HOH L 7 .   ? 14.194  17.481  25.255  1.00 26.85 ? 378 HOH B O     1 
HETATM 5431 O  O     . HOH L 7 .   ? -1.881  0.196   20.920  1.00 33.57 ? 379 HOH B O     1 
HETATM 5432 O  O     . HOH L 7 .   ? 10.809  -4.148  -8.469  1.00 48.49 ? 380 HOH B O     1 
HETATM 5433 O  O     . HOH L 7 .   ? 2.782   13.988  -4.945  1.00 31.65 ? 381 HOH B O     1 
HETATM 5434 O  O     . HOH L 7 .   ? -1.246  12.523  2.986   1.00 26.71 ? 382 HOH B O     1 
HETATM 5435 O  O     . HOH L 7 .   ? -4.616  7.468   8.887   1.00 23.50 ? 383 HOH B O     1 
HETATM 5436 O  O     . HOH L 7 .   ? 3.166   4.361   -7.808  1.00 33.50 ? 384 HOH B O     1 
HETATM 5437 O  O     . HOH L 7 .   ? 10.219  14.377  0.748   1.00 36.00 ? 385 HOH B O     1 
HETATM 5438 O  O     . HOH L 7 .   ? 8.174   -5.980  -5.413  1.00 45.37 ? 386 HOH B O     1 
HETATM 5439 O  O     . HOH L 7 .   ? -4.605  2.186   6.141   1.00 22.26 ? 387 HOH B O     1 
HETATM 5440 O  O     . HOH L 7 .   ? 11.135  9.799   -1.102  1.00 29.81 ? 388 HOH B O     1 
HETATM 5441 O  O     . HOH L 7 .   ? -6.406  2.228   -2.926  1.00 29.75 ? 389 HOH B O     1 
HETATM 5442 O  O     . HOH L 7 .   ? 14.808  17.034  -0.262  1.00 32.55 ? 390 HOH B O     1 
HETATM 5443 O  O     . HOH L 7 .   ? 22.109  -0.332  -0.999  1.00 34.10 ? 391 HOH B O     1 
HETATM 5444 O  O     . HOH L 7 .   ? 22.744  10.629  16.925  1.00 31.89 ? 392 HOH B O     1 
HETATM 5445 O  O     . HOH L 7 .   ? 15.217  13.417  26.461  1.00 27.11 ? 393 HOH B O     1 
HETATM 5446 O  O     . HOH L 7 .   ? 11.320  8.603   2.437   1.00 18.96 ? 394 HOH B O     1 
HETATM 5447 O  O     . HOH L 7 .   ? 14.907  -11.698 4.998   1.00 35.50 ? 395 HOH B O     1 
HETATM 5448 O  O     . HOH L 7 .   ? 7.570   -5.708  24.478  1.00 32.69 ? 396 HOH B O     1 
HETATM 5449 O  O     . HOH L 7 .   ? 7.876   -8.783  23.023  1.00 37.32 ? 397 HOH B O     1 
HETATM 5450 O  O     . HOH L 7 .   ? -8.338  -1.958  1.534   1.00 37.32 ? 398 HOH B O     1 
HETATM 5451 O  O     . HOH L 7 .   ? 20.464  10.888  10.709  1.00 38.64 ? 399 HOH B O     1 
HETATM 5452 O  O     . HOH L 7 .   ? 3.702   15.884  6.514   1.00 31.35 ? 400 HOH B O     1 
HETATM 5453 O  O     . HOH L 7 .   ? 15.001  19.329  21.777  1.00 29.46 ? 401 HOH B O     1 
HETATM 5454 O  O     . HOH L 7 .   ? -0.989  5.865   17.425  1.00 27.96 ? 402 HOH B O     1 
HETATM 5455 O  O     . HOH L 7 .   ? 11.981  -0.554  27.778  1.00 25.92 ? 403 HOH B O     1 
HETATM 5456 O  O     . HOH L 7 .   ? -5.034  0.598   13.328  1.00 33.53 ? 404 HOH B O     1 
HETATM 5457 O  O     . HOH L 7 .   ? 24.182  5.011   1.813   1.00 41.12 ? 405 HOH B O     1 
HETATM 5458 O  O     . HOH L 7 .   ? -2.388  3.062   -4.380  1.00 34.34 ? 406 HOH B O     1 
HETATM 5459 O  O     . HOH L 7 .   ? 20.469  0.708   0.984   1.00 28.68 ? 407 HOH B O     1 
HETATM 5460 O  O     . HOH L 7 .   ? 22.011  2.213   5.156   1.00 32.73 ? 408 HOH B O     1 
HETATM 5461 O  O     . HOH L 7 .   ? 4.629   3.309   24.748  1.00 33.67 ? 409 HOH B O     1 
HETATM 5462 O  O     . HOH L 7 .   ? -6.898  0.585   -1.151  1.00 28.56 ? 410 HOH B O     1 
HETATM 5463 O  O     . HOH L 7 .   ? -8.075  1.484   12.965  1.00 28.66 ? 411 HOH B O     1 
HETATM 5464 O  O     . HOH L 7 .   ? -4.043  13.439  3.110   1.00 31.67 ? 412 HOH B O     1 
HETATM 5465 O  O     . HOH L 7 .   ? 18.393  -6.388  5.013   1.00 32.58 ? 413 HOH B O     1 
HETATM 5466 O  O     . HOH L 7 .   ? 4.886   11.776  -5.712  1.00 37.06 ? 414 HOH B O     1 
HETATM 5467 O  O     . HOH L 7 .   ? 25.000  -4.369  16.718  1.00 33.28 ? 415 HOH B O     1 
HETATM 5468 O  O     . HOH L 7 .   ? 0.545   -5.401  -3.205  1.00 40.73 ? 416 HOH B O     1 
HETATM 5469 O  O     . HOH L 7 .   ? 18.987  6.838   -4.503  1.00 42.32 ? 417 HOH B O     1 
HETATM 5470 O  O     . HOH L 7 .   ? -0.625  14.827  3.966   1.00 35.31 ? 418 HOH B O     1 
HETATM 5471 O  O     . HOH L 7 .   ? 6.894   17.348  -0.612  1.00 40.84 ? 419 HOH B O     1 
HETATM 5472 O  O     . HOH L 7 .   ? 13.788  18.839  11.399  1.00 35.73 ? 420 HOH B O     1 
HETATM 5473 O  O     . HOH L 7 .   ? 20.642  -4.163  -0.141  1.00 39.68 ? 421 HOH B O     1 
HETATM 5474 O  O     . HOH L 7 .   ? 17.352  -13.871 11.913  1.00 51.13 ? 422 HOH B O     1 
HETATM 5475 O  O     . HOH L 7 .   ? 15.920  2.560   -7.530  1.00 50.20 ? 423 HOH B O     1 
HETATM 5476 O  O     . HOH L 7 .   ? 16.898  8.419   -3.788  1.00 38.04 ? 424 HOH B O     1 
HETATM 5477 O  O     . HOH L 7 .   ? -10.585 9.850   11.100  1.00 43.17 ? 425 HOH B O     1 
HETATM 5478 O  O     . HOH L 7 .   ? 25.766  -2.913  15.043  1.00 37.97 ? 426 HOH B O     1 
HETATM 5479 O  O     . HOH L 7 .   ? -5.406  -5.757  9.700   1.00 46.42 ? 427 HOH B O     1 
HETATM 5480 O  O     . HOH L 7 .   ? 19.457  13.558  11.251  1.00 36.13 ? 428 HOH B O     1 
HETATM 5481 O  O     . HOH L 7 .   ? 14.245  6.529   -6.935  1.00 37.54 ? 429 HOH B O     1 
HETATM 5482 O  O     . HOH L 7 .   ? 26.334  2.922   14.987  1.00 32.70 ? 430 HOH B O     1 
HETATM 5483 O  O     . HOH L 7 .   ? 1.953   16.240  7.758   1.00 35.36 ? 431 HOH B O     1 
HETATM 5484 O  O     . HOH L 7 .   ? 2.000   -2.702  21.352  1.00 39.28 ? 432 HOH B O     1 
HETATM 5485 O  O     . HOH L 7 .   ? -12.141 9.585   8.190   1.00 38.30 ? 433 HOH B O     1 
HETATM 5486 O  O     . HOH L 7 .   ? 19.569  -3.480  2.335   1.00 28.68 ? 434 HOH B O     1 
HETATM 5487 O  O     . HOH L 7 .   ? 25.079  6.226   8.269   1.00 45.70 ? 435 HOH B O     1 
HETATM 5488 O  O     . HOH L 7 .   ? 9.272   9.908   3.096   1.00 30.00 ? 436 HOH B O     1 
HETATM 5489 O  O     . HOH L 7 .   ? 17.069  14.860  11.637  1.00 31.66 ? 437 HOH B O     1 
HETATM 5490 O  O     . HOH L 7 .   ? 3.298   -9.665  -2.528  1.00 43.90 ? 438 HOH B O     1 
HETATM 5491 O  O     . HOH L 7 .   ? 28.334  3.808   16.356  1.00 37.11 ? 439 HOH B O     1 
HETATM 5492 O  O     . HOH L 7 .   ? 13.318  1.484   28.681  1.00 34.56 ? 440 HOH B O     1 
HETATM 5493 O  O     . HOH L 7 .   ? -9.669  9.982   7.436   1.00 36.57 ? 441 HOH B O     1 
HETATM 5494 O  O     . HOH L 7 .   ? 22.331  -7.945  14.050  1.00 42.28 ? 442 HOH B O     1 
HETATM 5495 O  O     . HOH L 7 .   ? 20.318  -7.699  4.177   1.00 39.07 ? 443 HOH B O     1 
HETATM 5496 O  O     . HOH L 7 .   ? 11.677  -15.276 4.404   1.00 51.05 ? 444 HOH B O     1 
HETATM 5497 O  O     . HOH L 7 .   ? 14.457  18.659  13.385  1.00 33.65 ? 445 HOH B O     1 
HETATM 5498 O  O     . HOH L 7 .   ? 4.108   -10.674 1.075   1.00 33.35 ? 446 HOH B O     1 
HETATM 5499 O  O     . HOH L 7 .   ? 17.885  -11.030 18.773  1.00 48.01 ? 447 HOH B O     1 
HETATM 5500 O  O     . HOH L 7 .   ? 2.086   -0.331  24.912  1.00 39.33 ? 448 HOH B O     1 
HETATM 5501 O  O     . HOH L 7 .   ? -7.927  15.061  15.491  1.00 39.36 ? 449 HOH B O     1 
HETATM 5502 O  O     . HOH L 7 .   ? 9.113   17.176  -0.562  1.00 37.60 ? 450 HOH B O     1 
HETATM 5503 O  O     . HOH L 7 .   ? 20.331  3.620   -1.747  1.00 36.73 ? 451 HOH B O     1 
HETATM 5504 O  O     . HOH L 7 .   ? 23.487  2.582   25.284  1.00 42.47 ? 452 HOH B O     1 
HETATM 5505 O  O     . HOH L 7 .   ? 25.086  -0.626  11.003  1.00 39.66 ? 453 HOH B O     1 
HETATM 5506 O  O     . HOH L 7 .   ? -0.457  7.886   25.769  1.00 34.11 ? 454 HOH B O     1 
HETATM 5507 O  O     . HOH L 7 .   ? -9.469  10.568  17.337  1.00 44.64 ? 455 HOH B O     1 
HETATM 5508 O  O     . HOH L 7 .   ? 22.867  -6.153  16.569  1.00 38.65 ? 456 HOH B O     1 
HETATM 5509 O  O     . HOH L 7 .   ? -10.570 -1.405  9.712   1.00 46.05 ? 457 HOH B O     1 
HETATM 5510 O  O     . HOH L 7 .   ? 19.605  -9.924  19.855  1.00 42.73 ? 458 HOH B O     1 
HETATM 5511 O  O     . HOH L 7 .   ? -9.873  2.764   15.204  1.00 41.19 ? 459 HOH B O     1 
HETATM 5512 O  O     . HOH L 7 .   ? 22.586  -9.234  17.918  1.00 44.58 ? 460 HOH B O     1 
HETATM 5513 O  O     . HOH M 7 .   ? 35.978  11.964  35.673  1.00 41.49 ? 301 HOH D O     1 
HETATM 5514 O  O     . HOH M 7 .   ? 38.064  37.711  12.719  1.00 38.10 ? 302 HOH D O     1 
HETATM 5515 O  O     . HOH M 7 .   ? 59.116  20.165  29.392  1.00 44.39 ? 303 HOH D O     1 
HETATM 5516 O  O     . HOH M 7 .   ? 58.049  28.771  19.278  1.00 34.27 ? 304 HOH D O     1 
HETATM 5517 O  O     . HOH M 7 .   ? 60.443  16.615  26.096  1.00 42.29 ? 305 HOH D O     1 
HETATM 5518 O  O     . HOH M 7 .   ? 51.446  25.519  38.363  1.00 39.17 ? 306 HOH D O     1 
HETATM 5519 O  O     . HOH M 7 .   ? 58.344  30.729  16.758  1.00 47.16 ? 307 HOH D O     1 
HETATM 5520 O  O     . HOH M 7 .   ? 40.371  19.841  35.559  1.00 38.48 ? 308 HOH D O     1 
HETATM 5521 O  O     . HOH M 7 .   ? 34.257  19.609  29.731  1.00 28.93 ? 309 HOH D O     1 
HETATM 5522 O  O     . HOH M 7 .   ? 43.523  32.792  9.229   1.00 30.70 ? 310 HOH D O     1 
HETATM 5523 O  O     . HOH M 7 .   ? 37.015  16.796  12.378  1.00 31.97 ? 311 HOH D O     1 
HETATM 5524 O  O     . HOH M 7 .   ? 44.947  30.564  9.686   1.00 32.69 ? 312 HOH D O     1 
HETATM 5525 O  O     . HOH M 7 .   ? 60.515  35.736  27.470  1.00 36.75 ? 313 HOH D O     1 
HETATM 5526 O  O     . HOH M 7 .   ? 38.602  17.361  36.258  1.00 46.42 ? 314 HOH D O     1 
HETATM 5527 O  O     . HOH M 7 .   ? 43.442  40.009  40.408  1.00 33.71 ? 315 HOH D O     1 
HETATM 5528 O  O     . HOH M 7 .   ? 40.816  28.262  40.263  1.00 34.41 ? 316 HOH D O     1 
HETATM 5529 O  O     . HOH M 7 .   ? 50.235  13.232  33.453  1.00 48.39 ? 317 HOH D O     1 
HETATM 5530 O  O     . HOH M 7 .   ? 37.637  35.550  40.967  1.00 38.73 ? 318 HOH D O     1 
HETATM 5531 O  O     . HOH M 7 .   ? 25.439  31.290  23.147  1.00 32.61 ? 319 HOH D O     1 
HETATM 5532 O  O     . HOH M 7 .   ? 37.092  27.542  38.671  1.00 36.54 ? 320 HOH D O     1 
HETATM 5533 O  O     . HOH M 7 .   ? 32.393  25.668  7.659   1.00 37.62 ? 321 HOH D O     1 
HETATM 5534 O  O     . HOH M 7 .   ? 55.743  28.890  38.186  1.00 39.11 ? 322 HOH D O     1 
HETATM 5535 O  O     . HOH M 7 .   ? 45.248  34.250  34.790  1.00 24.20 ? 323 HOH D O     1 
HETATM 5536 O  O     . HOH M 7 .   ? 43.900  28.503  43.267  1.00 36.44 ? 324 HOH D O     1 
HETATM 5537 O  O     . HOH M 7 .   ? 54.066  32.729  14.545  1.00 47.32 ? 325 HOH D O     1 
HETATM 5538 O  O     . HOH M 7 .   ? 25.153  23.855  15.937  1.00 31.88 ? 326 HOH D O     1 
HETATM 5539 O  O     . HOH M 7 .   ? 42.280  24.974  38.708  1.00 32.00 ? 327 HOH D O     1 
HETATM 5540 O  O     . HOH M 7 .   ? 51.280  32.470  13.557  1.00 38.70 ? 328 HOH D O     1 
HETATM 5541 O  O     . HOH M 7 .   ? 42.709  21.809  32.604  1.00 28.77 ? 329 HOH D O     1 
HETATM 5542 O  O     . HOH M 7 .   ? 53.576  15.765  24.802  1.00 40.92 ? 330 HOH D O     1 
HETATM 5543 O  O     . HOH M 7 .   ? 36.842  37.721  17.184  1.00 34.79 ? 331 HOH D O     1 
HETATM 5544 O  O     . HOH M 7 .   ? 47.697  12.737  20.384  1.00 34.90 ? 332 HOH D O     1 
HETATM 5545 O  O     . HOH M 7 .   ? 29.969  18.461  21.443  1.00 28.81 ? 333 HOH D O     1 
HETATM 5546 O  O     . HOH M 7 .   ? 52.637  29.681  41.422  1.00 40.52 ? 334 HOH D O     1 
HETATM 5547 O  O     . HOH M 7 .   ? 36.249  14.797  35.169  1.00 38.99 ? 335 HOH D O     1 
HETATM 5548 O  O     . HOH M 7 .   ? 58.890  33.119  33.046  1.00 38.99 ? 336 HOH D O     1 
HETATM 5549 O  O     . HOH M 7 .   ? 44.971  10.807  22.823  1.00 43.65 ? 337 HOH D O     1 
HETATM 5550 O  O     . HOH M 7 .   ? 40.965  19.484  21.803  1.00 31.68 ? 338 HOH D O     1 
HETATM 5551 O  O     . HOH M 7 .   ? 42.208  18.413  31.695  1.00 29.94 ? 339 HOH D O     1 
HETATM 5552 O  O     . HOH M 7 .   ? 33.995  41.010  24.342  1.00 34.34 ? 340 HOH D O     1 
HETATM 5553 O  O     . HOH M 7 .   ? 29.130  37.350  25.406  1.00 35.69 ? 341 HOH D O     1 
HETATM 5554 O  O     . HOH M 7 .   ? 38.805  14.745  22.483  1.00 33.65 ? 342 HOH D O     1 
HETATM 5555 O  O     . HOH M 7 .   ? 31.510  40.788  29.439  1.00 39.65 ? 343 HOH D O     1 
HETATM 5556 O  O     . HOH M 7 .   ? 40.762  31.041  42.401  1.00 31.66 ? 344 HOH D O     1 
HETATM 5557 O  O     . HOH M 7 .   ? 33.114  18.756  18.219  1.00 28.90 ? 345 HOH D O     1 
HETATM 5558 O  O     . HOH M 7 .   ? 44.022  37.226  20.008  1.00 32.80 ? 346 HOH D O     1 
HETATM 5559 O  O     . HOH M 7 .   ? 38.148  17.643  24.244  1.00 25.75 ? 347 HOH D O     1 
HETATM 5560 O  O     . HOH M 7 .   ? 48.256  26.891  36.181  1.00 26.99 ? 348 HOH D O     1 
HETATM 5561 O  O     . HOH M 7 .   ? 57.662  23.617  33.413  1.00 41.23 ? 349 HOH D O     1 
HETATM 5562 O  O     . HOH M 7 .   ? 38.539  40.707  32.075  1.00 32.40 ? 350 HOH D O     1 
HETATM 5563 O  O     . HOH M 7 .   ? 29.383  19.629  24.934  1.00 33.54 ? 351 HOH D O     1 
HETATM 5564 O  O     . HOH M 7 .   ? 42.687  27.473  35.974  1.00 30.12 ? 352 HOH D O     1 
HETATM 5565 O  O     . HOH M 7 .   ? 45.082  38.988  29.444  1.00 36.02 ? 353 HOH D O     1 
HETATM 5566 O  O     . HOH M 7 .   ? 28.900  33.310  16.556  1.00 22.82 ? 354 HOH D O     1 
HETATM 5567 O  O     . HOH M 7 .   ? 40.764  15.149  12.195  1.00 36.89 ? 355 HOH D O     1 
HETATM 5568 O  O     . HOH M 7 .   ? 44.742  35.408  11.041  1.00 38.25 ? 356 HOH D O     1 
HETATM 5569 O  O     . HOH M 7 .   ? 60.261  26.357  23.070  1.00 38.50 ? 357 HOH D O     1 
HETATM 5570 O  O     . HOH M 7 .   ? 48.582  24.365  30.294  1.00 28.25 ? 358 HOH D O     1 
HETATM 5571 O  O     . HOH M 7 .   ? 57.475  26.847  27.268  1.00 38.00 ? 359 HOH D O     1 
HETATM 5572 O  O     . HOH M 7 .   ? 28.857  21.493  26.660  1.00 32.10 ? 360 HOH D O     1 
HETATM 5573 O  O     . HOH M 7 .   ? 43.138  21.946  9.015   1.00 32.42 ? 361 HOH D O     1 
HETATM 5574 O  O     . HOH M 7 .   ? 21.508  26.918  20.676  1.00 30.15 ? 362 HOH D O     1 
HETATM 5575 O  O     . HOH M 7 .   ? 37.885  36.917  27.454  1.00 29.84 ? 363 HOH D O     1 
HETATM 5576 O  O     . HOH M 7 .   ? 42.313  35.001  35.568  1.00 25.16 ? 364 HOH D O     1 
HETATM 5577 O  O     . HOH M 7 .   ? 57.563  27.789  29.628  1.00 32.56 ? 365 HOH D O     1 
HETATM 5578 O  O     . HOH M 7 .   ? 22.378  21.739  22.275  1.00 32.36 ? 366 HOH D O     1 
HETATM 5579 O  O     . HOH M 7 .   ? 56.024  20.654  16.820  1.00 37.77 ? 367 HOH D O     1 
HETATM 5580 O  O     . HOH M 7 .   ? 41.442  16.696  8.457   1.00 41.97 ? 368 HOH D O     1 
HETATM 5581 O  O     . HOH M 7 .   ? 24.012  18.762  18.154  1.00 37.72 ? 369 HOH D O     1 
HETATM 5582 O  O     . HOH M 7 .   ? 24.545  21.626  18.357  1.00 28.74 ? 370 HOH D O     1 
HETATM 5583 O  O     . HOH M 7 .   ? 48.024  34.434  34.323  1.00 25.54 ? 371 HOH D O     1 
HETATM 5584 O  O     . HOH M 7 .   ? 48.709  12.583  11.355  1.00 50.44 ? 372 HOH D O     1 
HETATM 5585 O  O     . HOH M 7 .   ? 53.630  18.733  14.500  1.00 39.90 ? 373 HOH D O     1 
HETATM 5586 O  O     . HOH M 7 .   ? 34.824  36.876  18.358  1.00 31.62 ? 374 HOH D O     1 
HETATM 5587 O  O     . HOH M 7 .   ? 47.841  11.617  22.956  1.00 39.15 ? 375 HOH D O     1 
HETATM 5588 O  O     . HOH M 7 .   ? 38.389  25.865  4.936   1.00 36.78 ? 376 HOH D O     1 
HETATM 5589 O  O     . HOH M 7 .   ? 50.023  16.616  20.150  1.00 34.12 ? 377 HOH D O     1 
HETATM 5590 O  O     . HOH M 7 .   ? 52.349  16.118  14.419  1.00 49.90 ? 378 HOH D O     1 
HETATM 5591 O  O     . HOH M 7 .   ? 30.863  32.086  12.520  1.00 31.63 ? 379 HOH D O     1 
HETATM 5592 O  O     . HOH M 7 .   ? 41.960  35.966  11.509  1.00 34.44 ? 380 HOH D O     1 
HETATM 5593 O  O     . HOH M 7 .   ? 36.079  22.737  6.856   1.00 34.85 ? 381 HOH D O     1 
HETATM 5594 O  O     . HOH M 7 .   ? 44.008  36.288  14.173  1.00 31.51 ? 382 HOH D O     1 
HETATM 5595 O  O     . HOH M 7 .   ? 44.622  13.616  13.705  1.00 42.63 ? 383 HOH D O     1 
HETATM 5596 O  O     . HOH M 7 .   ? 34.933  33.596  10.384  1.00 33.50 ? 384 HOH D O     1 
HETATM 5597 O  O     . HOH M 7 .   ? 45.413  40.747  31.296  1.00 40.40 ? 385 HOH D O     1 
HETATM 5598 O  O     . HOH M 7 .   ? 44.255  29.022  8.022   1.00 34.55 ? 386 HOH D O     1 
HETATM 5599 O  O     . HOH M 7 .   ? 52.293  12.207  21.046  1.00 42.66 ? 387 HOH D O     1 
HETATM 5600 O  O     . HOH M 7 .   ? 44.996  23.880  8.404   1.00 40.11 ? 388 HOH D O     1 
HETATM 5601 O  O     . HOH M 7 .   ? 33.903  28.915  35.974  1.00 35.48 ? 389 HOH D O     1 
HETATM 5602 O  O     . HOH M 7 .   ? 51.462  16.632  17.768  1.00 36.26 ? 390 HOH D O     1 
HETATM 5603 O  O     . HOH M 7 .   ? 47.717  27.961  44.014  1.00 47.15 ? 391 HOH D O     1 
HETATM 5604 O  O     . HOH M 7 .   ? 30.090  16.187  17.699  1.00 38.32 ? 392 HOH D O     1 
HETATM 5605 O  O     . HOH M 7 .   ? 52.632  38.463  28.998  1.00 41.48 ? 393 HOH D O     1 
HETATM 5606 O  O     . HOH M 7 .   ? 51.701  28.907  10.286  1.00 33.13 ? 394 HOH D O     1 
HETATM 5607 O  O     . HOH M 7 .   ? 35.429  28.758  6.570   1.00 37.70 ? 395 HOH D O     1 
HETATM 5608 O  O     . HOH M 7 .   ? 34.812  40.225  37.485  1.00 41.63 ? 396 HOH D O     1 
HETATM 5609 O  O     . HOH M 7 .   ? 33.981  26.204  5.896   1.00 37.71 ? 397 HOH D O     1 
HETATM 5610 O  O     . HOH M 7 .   ? 47.587  11.591  35.134  1.00 55.21 ? 398 HOH D O     1 
HETATM 5611 O  O     . HOH M 7 .   ? 55.570  18.553  17.031  1.00 40.90 ? 399 HOH D O     1 
HETATM 5612 O  O     . HOH M 7 .   ? 41.798  37.995  18.715  1.00 38.68 ? 400 HOH D O     1 
HETATM 5613 O  O     . HOH M 7 .   ? 42.953  22.997  46.460  1.00 53.04 ? 401 HOH D O     1 
HETATM 5614 O  O     . HOH M 7 .   ? 38.349  27.672  40.767  1.00 39.66 ? 402 HOH D O     1 
HETATM 5615 O  O     . HOH M 7 .   ? 36.619  18.069  41.128  1.00 49.93 ? 403 HOH D O     1 
HETATM 5616 O  O     . HOH M 7 .   ? 36.483  32.128  7.711   1.00 39.04 ? 404 HOH D O     1 
HETATM 5617 O  O     . HOH M 7 .   ? 36.142  30.679  6.436   1.00 37.02 ? 405 HOH D O     1 
HETATM 5618 O  O     . HOH M 7 .   ? 33.734  14.752  21.783  1.00 43.92 ? 406 HOH D O     1 
HETATM 5619 O  O     . HOH M 7 .   ? 59.985  29.366  19.258  1.00 40.75 ? 407 HOH D O     1 
HETATM 5620 O  O     . HOH M 7 .   ? 40.956  15.218  9.909   1.00 41.48 ? 408 HOH D O     1 
HETATM 5621 O  O     . HOH M 7 .   ? 36.945  42.355  36.067  1.00 46.23 ? 409 HOH D O     1 
HETATM 5622 O  O     . HOH M 7 .   ? 60.445  31.780  29.517  1.00 39.98 ? 410 HOH D O     1 
HETATM 5623 O  O     . HOH M 7 .   ? 50.187  30.316  11.712  1.00 38.10 ? 411 HOH D O     1 
HETATM 5624 O  O     . HOH M 7 .   ? 45.753  11.775  15.323  1.00 44.30 ? 412 HOH D O     1 
HETATM 5625 O  O     . HOH M 7 .   ? 62.948  19.101  27.932  1.00 48.11 ? 413 HOH D O     1 
HETATM 5626 O  O     . HOH M 7 .   ? 43.111  10.038  18.990  1.00 44.29 ? 414 HOH D O     1 
HETATM 5627 O  O     . HOH M 7 .   ? 61.614  24.304  23.678  1.00 48.21 ? 415 HOH D O     1 
HETATM 5628 O  O     . HOH M 7 .   ? 59.513  27.523  25.601  1.00 40.57 ? 416 HOH D O     1 
HETATM 5629 O  O     . HOH M 7 .   ? 44.330  10.412  16.496  1.00 46.01 ? 417 HOH D O     1 
HETATM 5630 O  O     . HOH M 7 .   ? 58.570  19.350  32.757  1.00 47.67 ? 418 HOH D O     1 
HETATM 5631 O  O     . HOH N 7 .   ? 7.517   24.701  18.286  1.00 38.46 ? 301 HOH A O     1 
HETATM 5632 O  O     . HOH N 7 .   ? 2.079   28.364  8.734   1.00 36.88 ? 302 HOH A O     1 
HETATM 5633 O  O     . HOH N 7 .   ? 16.580  23.706  -3.336  1.00 40.21 ? 303 HOH A O     1 
HETATM 5634 O  O     . HOH N 7 .   ? 10.417  32.323  21.542  1.00 33.60 ? 304 HOH A O     1 
HETATM 5635 O  O     . HOH N 7 .   ? 20.760  49.886  15.844  1.00 43.28 ? 305 HOH A O     1 
HETATM 5636 O  O     . HOH N 7 .   ? 17.819  48.082  8.494   1.00 39.86 ? 306 HOH A O     1 
HETATM 5637 O  O     . HOH N 7 .   ? -1.651  43.881  10.944  1.00 50.08 ? 307 HOH A O     1 
HETATM 5638 O  O     . HOH N 7 .   ? 25.223  35.729  7.117   1.00 31.84 ? 308 HOH A O     1 
HETATM 5639 O  O     . HOH N 7 .   ? 22.346  14.347  1.011   1.00 38.64 ? 309 HOH A O     1 
HETATM 5640 O  O     . HOH N 7 .   ? 22.678  36.187  26.618  1.00 41.33 ? 310 HOH A O     1 
HETATM 5641 O  O     . HOH N 7 .   ? 29.816  41.678  31.315  1.00 49.92 ? 311 HOH A O     1 
HETATM 5642 O  O     . HOH N 7 .   ? -3.948  18.957  16.656  1.00 46.98 ? 312 HOH A O     1 
HETATM 5643 O  O     . HOH N 7 .   ? 11.522  26.413  9.732   1.00 19.87 ? 313 HOH A O     1 
HETATM 5644 O  O     . HOH N 7 .   ? 16.989  39.115  25.280  1.00 38.62 ? 314 HOH A O     1 
HETATM 5645 O  O     . HOH N 7 .   ? 25.676  37.705  10.178  1.00 30.89 ? 315 HOH A O     1 
HETATM 5646 O  O     . HOH N 7 .   ? 23.980  46.571  8.394   1.00 41.33 ? 316 HOH A O     1 
HETATM 5647 O  O     . HOH N 7 .   ? 11.662  16.909  8.697   1.00 24.92 ? 317 HOH A O     1 
HETATM 5648 O  O     . HOH N 7 .   ? 3.104   25.277  15.829  1.00 35.65 ? 318 HOH A O     1 
HETATM 5649 O  O     . HOH N 7 .   ? 19.921  36.950  -5.530  1.00 30.96 ? 319 HOH A O     1 
HETATM 5650 O  O     . HOH N 7 .   ? 24.822  29.452  -1.591  1.00 35.12 ? 320 HOH A O     1 
HETATM 5651 O  O     . HOH N 7 .   ? 0.519   28.434  6.552   1.00 44.43 ? 321 HOH A O     1 
HETATM 5652 O  O     . HOH N 7 .   ? 16.617  24.548  11.564  1.00 25.69 ? 322 HOH A O     1 
HETATM 5653 O  O     . HOH N 7 .   ? 33.115  39.265  20.594  1.00 36.66 ? 323 HOH A O     1 
HETATM 5654 O  O     . HOH N 7 .   ? 18.376  30.006  -8.413  1.00 36.22 ? 324 HOH A O     1 
HETATM 5655 O  O     . HOH N 7 .   ? 21.515  45.900  7.708   1.00 38.26 ? 325 HOH A O     1 
HETATM 5656 O  O     . HOH N 7 .   ? 10.136  24.195  8.107   1.00 19.55 ? 326 HOH A O     1 
HETATM 5657 O  O     . HOH N 7 .   ? 27.249  30.992  15.644  1.00 27.39 ? 327 HOH A O     1 
HETATM 5658 O  O     . HOH N 7 .   ? 3.122   16.167  12.022  1.00 20.09 ? 328 HOH A O     1 
HETATM 5659 O  O     . HOH N 7 .   ? 16.486  19.606  13.741  1.00 31.58 ? 329 HOH A O     1 
HETATM 5660 O  O     . HOH N 7 .   ? 17.185  42.344  23.841  1.00 35.25 ? 330 HOH A O     1 
HETATM 5661 O  O     . HOH N 7 .   ? 25.448  44.300  22.769  1.00 39.89 ? 331 HOH A O     1 
HETATM 5662 O  O     . HOH N 7 .   ? 27.733  31.545  13.117  1.00 25.77 ? 332 HOH A O     1 
HETATM 5663 O  O     . HOH N 7 .   ? 12.659  23.350  7.080   1.00 18.86 ? 333 HOH A O     1 
HETATM 5664 O  O     . HOH N 7 .   ? 28.750  41.053  12.146  1.00 37.42 ? 334 HOH A O     1 
HETATM 5665 O  O     . HOH N 7 .   ? 19.433  43.785  1.377   1.00 37.79 ? 335 HOH A O     1 
HETATM 5666 O  O     . HOH N 7 .   ? 29.267  47.739  12.169  1.00 46.15 ? 336 HOH A O     1 
HETATM 5667 O  O     . HOH N 7 .   ? 22.203  25.352  17.950  1.00 26.24 ? 337 HOH A O     1 
HETATM 5668 O  O     . HOH N 7 .   ? 17.543  42.707  -0.592  1.00 37.88 ? 338 HOH A O     1 
HETATM 5669 O  O     . HOH N 7 .   ? 20.697  27.501  4.043   1.00 21.06 ? 339 HOH A O     1 
HETATM 5670 O  O     . HOH N 7 .   ? 15.626  29.922  21.134  1.00 36.26 ? 340 HOH A O     1 
HETATM 5671 O  O     . HOH N 7 .   ? 18.660  21.926  16.820  1.00 37.11 ? 341 HOH A O     1 
HETATM 5672 O  O     . HOH N 7 .   ? -3.523  23.480  16.435  1.00 42.04 ? 342 HOH A O     1 
HETATM 5673 O  O     . HOH N 7 .   ? 8.902   46.407  13.189  1.00 40.83 ? 343 HOH A O     1 
HETATM 5674 O  O     . HOH N 7 .   ? 4.376   32.612  5.055   1.00 27.98 ? 344 HOH A O     1 
HETATM 5675 O  O     . HOH N 7 .   ? 15.182  22.226  4.764   1.00 25.03 ? 345 HOH A O     1 
HETATM 5676 O  O     . HOH N 7 .   ? 8.227   28.499  -2.946  1.00 33.30 ? 346 HOH A O     1 
HETATM 5677 O  O     . HOH N 7 .   ? 5.040   25.283  19.074  1.00 40.61 ? 347 HOH A O     1 
HETATM 5678 O  O     . HOH N 7 .   ? -1.155  38.442  3.951   1.00 38.77 ? 348 HOH A O     1 
HETATM 5679 O  O     . HOH N 7 .   ? 2.603   25.895  13.026  1.00 29.54 ? 349 HOH A O     1 
HETATM 5680 O  O     . HOH N 7 .   ? 2.438   27.907  0.782   1.00 38.30 ? 350 HOH A O     1 
HETATM 5681 O  O     . HOH N 7 .   ? 4.756   27.844  21.539  1.00 45.40 ? 351 HOH A O     1 
HETATM 5682 O  O     . HOH N 7 .   ? 7.288   21.411  9.643   1.00 32.04 ? 352 HOH A O     1 
HETATM 5683 O  O     . HOH N 7 .   ? 13.618  20.428  13.826  1.00 23.06 ? 353 HOH A O     1 
HETATM 5684 O  O     . HOH N 7 .   ? 23.243  33.259  26.882  1.00 34.39 ? 354 HOH A O     1 
HETATM 5685 O  O     . HOH N 7 .   ? 8.196   25.197  15.931  1.00 25.83 ? 355 HOH A O     1 
HETATM 5686 O  O     . HOH N 7 .   ? 14.844  15.184  9.811   1.00 24.55 ? 356 HOH A O     1 
HETATM 5687 O  O     . HOH N 7 .   ? 12.961  15.970  1.505   1.00 24.04 ? 357 HOH A O     1 
HETATM 5688 O  O     . HOH N 7 .   ? 20.430  40.904  26.741  1.00 39.08 ? 358 HOH A O     1 
HETATM 5689 O  O     . HOH N 7 .   ? 0.846   22.972  7.041   1.00 40.95 ? 359 HOH A O     1 
HETATM 5690 O  O     . HOH N 7 .   ? 23.928  27.981  16.979  1.00 27.02 ? 360 HOH A O     1 
HETATM 5691 O  O     . HOH N 7 .   ? 23.761  38.589  3.200   1.00 24.77 ? 361 HOH A O     1 
HETATM 5692 O  O     . HOH N 7 .   ? 26.808  33.749  7.656   1.00 33.32 ? 362 HOH A O     1 
HETATM 5693 O  O     . HOH N 7 .   ? -4.479  34.571  12.620  1.00 40.18 ? 363 HOH A O     1 
HETATM 5694 O  O     . HOH N 7 .   ? 10.847  48.599  3.905   1.00 40.79 ? 364 HOH A O     1 
HETATM 5695 O  O     . HOH N 7 .   ? 28.462  32.030  9.689   1.00 33.86 ? 365 HOH A O     1 
HETATM 5696 O  O     . HOH N 7 .   ? 7.513   49.126  1.924   1.00 50.35 ? 366 HOH A O     1 
HETATM 5697 O  O     . HOH N 7 .   ? 30.059  35.153  14.180  1.00 34.14 ? 367 HOH A O     1 
HETATM 5698 O  O     . HOH N 7 .   ? 10.250  26.999  -5.439  1.00 35.47 ? 368 HOH A O     1 
HETATM 5699 O  O     . HOH N 7 .   ? 5.024   27.527  0.874   1.00 36.13 ? 369 HOH A O     1 
HETATM 5700 O  O     . HOH N 7 .   ? 6.228   29.393  11.310  1.00 22.72 ? 370 HOH A O     1 
HETATM 5701 O  O     . HOH N 7 .   ? 14.822  21.903  9.826   1.00 32.39 ? 371 HOH A O     1 
HETATM 5702 O  O     . HOH N 7 .   ? -3.023  46.020  23.660  1.00 41.22 ? 372 HOH A O     1 
HETATM 5703 O  O     . HOH N 7 .   ? 25.862  26.455  -0.256  1.00 38.81 ? 373 HOH A O     1 
HETATM 5704 O  O     . HOH N 7 .   ? 14.749  33.473  19.864  1.00 24.98 ? 374 HOH A O     1 
HETATM 5705 O  O     . HOH N 7 .   ? 22.320  41.169  3.478   1.00 24.92 ? 375 HOH A O     1 
HETATM 5706 O  O     . HOH N 7 .   ? 26.049  30.190  0.075   1.00 33.41 ? 376 HOH A O     1 
HETATM 5707 O  O     . HOH N 7 .   ? 29.940  25.986  7.018   1.00 34.16 ? 377 HOH A O     1 
HETATM 5708 O  O     . HOH N 7 .   ? 12.505  26.455  -3.841  1.00 30.89 ? 378 HOH A O     1 
HETATM 5709 O  O     . HOH N 7 .   ? 1.761   31.079  -6.251  1.00 42.35 ? 379 HOH A O     1 
HETATM 5710 O  O     . HOH N 7 .   ? 11.119  39.273  -10.761 1.00 52.20 ? 380 HOH A O     1 
HETATM 5711 O  O     . HOH N 7 .   ? -3.672  44.327  19.822  1.00 49.10 ? 381 HOH A O     1 
HETATM 5712 O  O     . HOH N 7 .   ? 14.904  44.446  -0.128  1.00 36.45 ? 382 HOH A O     1 
HETATM 5713 O  O     . HOH N 7 .   ? -5.659  39.100  22.406  1.00 51.77 ? 383 HOH A O     1 
HETATM 5714 O  O     . HOH N 7 .   ? 20.556  32.985  27.785  1.00 44.43 ? 384 HOH A O     1 
HETATM 5715 O  O     . HOH N 7 .   ? -2.582  20.328  17.410  1.00 41.53 ? 385 HOH A O     1 
HETATM 5716 O  O     . HOH N 7 .   ? -4.090  30.767  -2.331  1.00 47.41 ? 386 HOH A O     1 
HETATM 5717 O  O     . HOH N 7 .   ? 26.256  47.053  10.654  1.00 39.53 ? 387 HOH A O     1 
HETATM 5718 O  O     . HOH N 7 .   ? 30.808  45.877  21.037  1.00 42.85 ? 388 HOH A O     1 
HETATM 5719 O  O     . HOH N 7 .   ? 14.273  24.974  20.225  1.00 37.00 ? 389 HOH A O     1 
HETATM 5720 O  O     . HOH N 7 .   ? 9.336   50.334  10.601  1.00 50.23 ? 390 HOH A O     1 
HETATM 5721 O  O     . HOH N 7 .   ? 7.881   42.052  -8.709  1.00 49.09 ? 391 HOH A O     1 
HETATM 5722 O  O     . HOH N 7 .   ? 2.436   25.938  6.245   1.00 35.95 ? 392 HOH A O     1 
HETATM 5723 O  O     . HOH N 7 .   ? 24.494  37.838  26.982  1.00 43.34 ? 393 HOH A O     1 
HETATM 5724 O  O     . HOH N 7 .   ? 17.803  23.309  18.910  1.00 33.87 ? 394 HOH A O     1 
HETATM 5725 O  O     . HOH N 7 .   ? 5.407   18.077  6.367   1.00 35.14 ? 395 HOH A O     1 
HETATM 5726 O  O     . HOH N 7 .   ? 26.805  38.550  27.262  1.00 42.85 ? 396 HOH A O     1 
HETATM 5727 O  O     . HOH N 7 .   ? 23.193  40.945  0.097   1.00 26.69 ? 397 HOH A O     1 
HETATM 5728 O  O     . HOH N 7 .   ? 0.067   29.613  -3.964  1.00 42.73 ? 398 HOH A O     1 
HETATM 5729 O  O     . HOH N 7 .   ? 10.550  29.679  22.809  1.00 36.33 ? 399 HOH A O     1 
HETATM 5730 O  O     . HOH N 7 .   ? -8.008  33.417  15.694  1.00 45.97 ? 400 HOH A O     1 
HETATM 5731 O  O     . HOH N 7 .   ? -2.095  46.762  9.260   1.00 51.90 ? 401 HOH A O     1 
HETATM 5732 O  O     . HOH N 7 .   ? 19.693  28.885  21.260  1.00 32.01 ? 402 HOH A O     1 
HETATM 5733 O  O     . HOH N 7 .   ? 6.575   28.046  -0.730  1.00 37.85 ? 403 HOH A O     1 
HETATM 5734 O  O     . HOH N 7 .   ? 16.168  35.777  29.048  1.00 54.79 ? 404 HOH A O     1 
HETATM 5735 O  O     . HOH N 7 .   ? 21.739  49.783  20.912  1.00 55.57 ? 405 HOH A O     1 
HETATM 5736 O  O     . HOH N 7 .   ? -0.290  52.303  4.933   1.00 48.32 ? 406 HOH A O     1 
HETATM 5737 O  O     . HOH N 7 .   ? 28.674  24.094  7.450   1.00 37.61 ? 407 HOH A O     1 
HETATM 5738 O  O     . HOH N 7 .   ? 4.601   19.716  5.194   1.00 42.11 ? 408 HOH A O     1 
HETATM 5739 O  O     . HOH N 7 .   ? -4.793  42.105  19.459  1.00 51.21 ? 409 HOH A O     1 
HETATM 5740 O  O     . HOH N 7 .   ? 32.942  37.439  16.052  1.00 39.09 ? 410 HOH A O     1 
HETATM 5741 O  O     . HOH N 7 .   ? 12.738  33.398  21.506  1.00 29.56 ? 411 HOH A O     1 
HETATM 5742 O  O     . HOH N 7 .   ? 16.924  22.865  9.420   1.00 34.86 ? 412 HOH A O     1 
HETATM 5743 O  O     . HOH N 7 .   ? 10.360  50.492  5.478   1.00 44.35 ? 413 HOH A O     1 
HETATM 5744 O  O     . HOH N 7 .   ? 22.352  23.112  17.587  1.00 38.97 ? 414 HOH A O     1 
HETATM 5745 O  O     . HOH N 7 .   ? -3.123  40.074  3.891   1.00 47.39 ? 415 HOH A O     1 
HETATM 5746 O  O     . HOH N 7 .   ? 20.183  24.570  21.635  1.00 39.74 ? 416 HOH A O     1 
HETATM 5747 O  O     . HOH N 7 .   ? 5.391   25.364  16.733  1.00 41.71 ? 417 HOH A O     1 
HETATM 5748 O  O     . HOH N 7 .   ? -2.189  38.906  27.060  1.00 45.70 ? 418 HOH A O     1 
HETATM 5749 O  O     . HOH N 7 .   ? 9.309   22.352  0.098   1.00 39.43 ? 419 HOH A O     1 
HETATM 5750 O  O     . HOH N 7 .   ? 18.456  23.122  20.890  1.00 41.60 ? 420 HOH A O     1 
HETATM 5751 O  O     . HOH N 7 .   ? 17.059  51.787  12.728  1.00 48.31 ? 421 HOH A O     1 
HETATM 5752 O  O     . HOH N 7 .   ? 27.493  24.051  0.187   1.00 39.05 ? 422 HOH A O     1 
HETATM 5753 O  O     . HOH N 7 .   ? 7.553   54.714  18.043  1.00 53.76 ? 423 HOH A O     1 
HETATM 5754 O  O     . HOH O 7 .   ? 8.926   14.285  23.539  1.00 34.92 ? 301 HOH C O     1 
HETATM 5755 O  O     . HOH O 7 .   ? 6.775   27.072  33.121  1.00 54.88 ? 302 HOH C O     1 
HETATM 5756 O  O     . HOH O 7 .   ? 3.694   21.914  33.552  1.00 42.71 ? 303 HOH C O     1 
HETATM 5757 O  O     . HOH O 7 .   ? 24.633  27.989  39.808  1.00 46.42 ? 304 HOH C O     1 
HETATM 5758 O  O     . HOH O 7 .   ? 13.872  7.805   29.723  1.00 38.08 ? 305 HOH C O     1 
HETATM 5759 O  O     . HOH O 7 .   ? 2.222   31.612  48.730  1.00 54.42 ? 306 HOH C O     1 
HETATM 5760 O  O     . HOH O 7 .   ? 24.361  20.794  39.963  1.00 51.96 ? 307 HOH C O     1 
HETATM 5761 O  O     . HOH O 7 .   ? 18.065  22.991  28.395  1.00 37.80 ? 308 HOH C O     1 
HETATM 5762 O  O     . HOH O 7 .   ? 31.428  20.053  32.082  1.00 36.06 ? 309 HOH C O     1 
HETATM 5763 O  O     . HOH O 7 .   ? 27.401  16.653  35.747  1.00 33.85 ? 310 HOH C O     1 
HETATM 5764 O  O     . HOH O 7 .   ? 22.553  16.409  32.318  1.00 38.94 ? 311 HOH C O     1 
HETATM 5765 O  O     . HOH O 7 .   ? 8.863   36.495  41.731  1.00 59.26 ? 312 HOH C O     1 
HETATM 5766 O  O     . HOH O 7 .   ? 17.742  27.688  44.567  1.00 62.25 ? 313 HOH C O     1 
HETATM 5767 O  O     . HOH O 7 .   ? 30.214  13.548  46.973  1.00 46.95 ? 314 HOH C O     1 
HETATM 5768 O  O     . HOH O 7 .   ? 21.223  1.907   31.607  1.00 48.41 ? 315 HOH C O     1 
HETATM 5769 O  O     . HOH O 7 .   ? 11.135  21.596  32.388  1.00 42.28 ? 316 HOH C O     1 
HETATM 5770 O  O     . HOH O 7 .   ? 13.449  21.500  29.925  1.00 39.68 ? 317 HOH C O     1 
HETATM 5771 O  O     . HOH O 7 .   ? 32.105  28.738  34.310  1.00 32.43 ? 318 HOH C O     1 
HETATM 5772 O  O     . HOH O 7 .   ? 23.719  8.196   35.784  1.00 43.04 ? 319 HOH C O     1 
HETATM 5773 O  O     . HOH O 7 .   ? 24.044  18.942  36.911  1.00 30.57 ? 320 HOH C O     1 
HETATM 5774 O  O     . HOH O 7 .   ? 20.816  17.963  26.642  1.00 39.41 ? 321 HOH C O     1 
HETATM 5775 O  O     . HOH O 7 .   ? 6.439   20.466  28.600  1.00 47.59 ? 322 HOH C O     1 
HETATM 5776 O  O     . HOH O 7 .   ? -1.985  12.683  31.263  1.00 43.24 ? 323 HOH C O     1 
HETATM 5777 O  O     . HOH O 7 .   ? 6.568   23.179  52.366  1.00 62.06 ? 324 HOH C O     1 
HETATM 5778 O  O     . HOH O 7 .   ? 22.030  25.536  34.116  1.00 36.65 ? 325 HOH C O     1 
HETATM 5779 O  O     . HOH O 7 .   ? 28.969  13.457  35.250  1.00 42.26 ? 326 HOH C O     1 
HETATM 5780 O  O     . HOH O 7 .   ? 26.582  19.358  37.307  1.00 33.52 ? 327 HOH C O     1 
HETATM 5781 O  O     . HOH O 7 .   ? 23.639  20.700  46.998  1.00 43.54 ? 328 HOH C O     1 
HETATM 5782 O  O     . HOH O 7 .   ? 23.740  0.037   39.361  1.00 35.76 ? 329 HOH C O     1 
HETATM 5783 O  O     . HOH O 7 .   ? 16.596  15.630  25.728  1.00 32.42 ? 330 HOH C O     1 
HETATM 5784 O  O     . HOH O 7 .   ? 12.945  33.309  50.170  1.00 63.39 ? 331 HOH C O     1 
HETATM 5785 O  O     . HOH O 7 .   ? 5.493   18.127  23.820  1.00 33.23 ? 332 HOH C O     1 
HETATM 5786 O  O     . HOH O 7 .   ? 24.532  28.753  41.808  1.00 55.02 ? 333 HOH C O     1 
HETATM 5787 O  O     . HOH O 7 .   ? 10.796  6.534   35.752  1.00 41.38 ? 334 HOH C O     1 
HETATM 5788 O  O     . HOH O 7 .   ? 28.430  24.177  43.059  1.00 45.73 ? 335 HOH C O     1 
HETATM 5789 O  O     . HOH O 7 .   ? 30.499  2.977   46.411  1.00 51.60 ? 336 HOH C O     1 
HETATM 5790 O  O     . HOH O 7 .   ? 6.629   23.055  57.315  1.00 56.73 ? 337 HOH C O     1 
HETATM 5791 O  O     . HOH O 7 .   ? 22.114  3.214   50.904  1.00 66.53 ? 338 HOH C O     1 
HETATM 5792 O  O     . HOH O 7 .   ? 14.925  3.126   41.529  1.00 45.14 ? 339 HOH C O     1 
HETATM 5793 O  O     . HOH O 7 .   ? 19.032  32.174  48.430  1.00 61.80 ? 340 HOH C O     1 
HETATM 5794 O  O     . HOH O 7 .   ? 19.283  19.577  26.536  1.00 33.27 ? 341 HOH C O     1 
HETATM 5795 O  O     . HOH O 7 .   ? 12.875  9.276   27.270  1.00 35.21 ? 342 HOH C O     1 
HETATM 5796 O  O     . HOH O 7 .   ? 26.509  17.607  58.222  1.00 66.61 ? 343 HOH C O     1 
HETATM 5797 O  O     . HOH O 7 .   ? 1.647   15.892  25.553  1.00 44.13 ? 344 HOH C O     1 
HETATM 5798 O  O     . HOH O 7 .   ? -3.387  7.821   31.674  1.00 46.75 ? 345 HOH C O     1 
HETATM 5799 O  O     . HOH O 7 .   ? 2.916   19.442  47.371  1.00 50.81 ? 346 HOH C O     1 
HETATM 5800 O  O     . HOH O 7 .   ? 9.898   6.090   29.356  1.00 38.38 ? 347 HOH C O     1 
HETATM 5801 O  O     . HOH O 7 .   ? 12.693  19.035  26.787  1.00 31.88 ? 348 HOH C O     1 
HETATM 5802 O  O     . HOH O 7 .   ? 25.520  20.543  29.728  1.00 34.39 ? 349 HOH C O     1 
HETATM 5803 O  O     . HOH O 7 .   ? 14.747  2.171   44.742  1.00 51.31 ? 350 HOH C O     1 
HETATM 5804 O  O     . HOH O 7 .   ? 32.472  0.348   41.788  1.00 38.15 ? 351 HOH C O     1 
HETATM 5805 O  O     . HOH O 7 .   ? 26.279  12.590  64.776  1.00 43.24 ? 352 HOH C O     1 
HETATM 5806 O  O     . HOH O 7 .   ? 10.000  8.128   27.402  1.00 25.52 ? 353 HOH C O     1 
HETATM 5807 O  O     . HOH O 7 .   ? 20.719  27.185  33.028  1.00 41.69 ? 354 HOH C O     1 
HETATM 5808 O  O     . HOH O 7 .   ? 6.171   22.064  49.401  1.00 56.96 ? 355 HOH C O     1 
HETATM 5809 O  O     . HOH O 7 .   ? 1.575   28.621  46.379  1.00 57.21 ? 356 HOH C O     1 
HETATM 5810 O  O     . HOH O 7 .   ? 23.095  26.703  55.578  1.00 59.37 ? 357 HOH C O     1 
HETATM 5811 O  O     . HOH O 7 .   ? 7.525   34.414  39.652  1.00 57.26 ? 358 HOH C O     1 
HETATM 5812 O  O     . HOH O 7 .   ? 26.371  16.423  32.283  1.00 45.65 ? 359 HOH C O     1 
HETATM 5813 O  O     . HOH O 7 .   ? 3.887   28.075  44.977  1.00 55.74 ? 360 HOH C O     1 
HETATM 5814 O  O     . HOH O 7 .   ? 28.107  19.428  30.343  1.00 42.07 ? 361 HOH C O     1 
HETATM 5815 O  O     . HOH O 7 .   ? 21.131  35.231  42.409  1.00 63.37 ? 362 HOH C O     1 
HETATM 5816 O  O     . HOH O 7 .   ? 5.775   4.725   42.571  1.00 48.68 ? 363 HOH C O     1 
HETATM 5817 O  O     . HOH O 7 .   ? 3.357   33.698  43.414  1.00 58.74 ? 364 HOH C O     1 
HETATM 5818 O  O     . HOH O 7 .   ? 6.200   4.242   34.242  1.00 38.76 ? 365 HOH C O     1 
HETATM 5819 O  O     . HOH O 7 .   ? 0.444   19.514  29.016  1.00 46.56 ? 366 HOH C O     1 
HETATM 5820 O  O     . HOH O 7 .   ? 31.309  10.179  44.202  1.00 45.27 ? 367 HOH C O     1 
HETATM 5821 O  O     . HOH O 7 .   ? 5.501   9.594   47.892  1.00 51.67 ? 368 HOH C O     1 
HETATM 5822 O  O     . HOH O 7 .   ? -0.019  28.367  48.195  1.00 51.24 ? 369 HOH C O     1 
HETATM 5823 O  O     . HOH O 7 .   ? 19.874  22.797  26.790  1.00 39.36 ? 370 HOH C O     1 
HETATM 5824 O  O     . HOH O 7 .   ? 1.642   4.200   29.195  1.00 36.81 ? 371 HOH C O     1 
HETATM 5825 O  O     . HOH O 7 .   ? 12.980  3.813   34.249  1.00 51.42 ? 372 HOH C O     1 
HETATM 5826 O  O     . HOH O 7 .   ? 6.972   25.482  56.171  1.00 60.03 ? 373 HOH C O     1 
HETATM 5827 O  O     . HOH O 7 .   ? 2.505   20.451  24.086  1.00 42.47 ? 374 HOH C O     1 
HETATM 5828 O  O     . HOH O 7 .   ? 14.557  -1.214  35.267  1.00 49.77 ? 375 HOH C O     1 
HETATM 5829 O  O     . HOH O 7 .   ? 5.078   34.407  40.502  1.00 55.82 ? 376 HOH C O     1 
HETATM 5830 O  O     . HOH O 7 .   ? 19.826  32.915  50.969  1.00 65.71 ? 377 HOH C O     1 
HETATM 5831 O  O     . HOH O 7 .   ? 5.883   3.770   27.272  1.00 40.48 ? 378 HOH C O     1 
HETATM 5832 O  O     . HOH O 7 .   ? 5.094   24.593  53.118  1.00 63.56 ? 379 HOH C O     1 
HETATM 5833 O  O     . HOH O 7 .   ? 26.786  19.782  28.500  1.00 39.70 ? 380 HOH C O     1 
HETATM 5834 O  O     . HOH O 7 .   ? 0.986   4.043   26.810  1.00 36.12 ? 381 HOH C O     1 
HETATM 5835 O  O     . HOH O 7 .   ? 3.409   26.046  38.941  1.00 45.35 ? 382 HOH C O     1 
HETATM 5836 O  O     . HOH O 7 .   ? 6.722   36.622  53.021  1.00 44.46 ? 383 HOH C O     1 
HETATM 5837 O  O     . HOH O 7 .   ? 6.114   11.663  50.747  1.00 55.76 ? 384 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     . VAL A 3   ? 1.0180 0.5727 0.8177 -0.1240 -0.2292 0.0267  2   VAL B N     
2    C  CA    . VAL A 3   ? 0.9768 0.5579 0.7975 -0.1291 -0.2185 0.0415  2   VAL B CA    
3    C  C     . VAL A 3   ? 0.8711 0.4723 0.6977 -0.1092 -0.2048 0.0366  2   VAL B C     
4    O  O     . VAL A 3   ? 0.8872 0.4688 0.6952 -0.0873 -0.2039 0.0224  2   VAL B O     
5    C  CB    . VAL A 3   ? 0.9759 0.5261 0.7853 -0.1321 -0.2230 0.0491  2   VAL B CB    
6    C  CG1   . VAL A 3   ? 0.9176 0.4923 0.7439 -0.1327 -0.2108 0.0627  2   VAL B CG1   
7    C  CG2   . VAL A 3   ? 0.9945 0.5338 0.8043 -0.1564 -0.2350 0.0572  2   VAL B CG2   
8    N  N     . ASN A 4   ? 0.8309 0.4732 0.6838 -0.1170 -0.1941 0.0482  3   ASN B N     
9    C  CA    . ASN A 4   ? 0.7167 0.3826 0.5791 -0.1024 -0.1817 0.0451  3   ASN B CA    
10   C  C     . ASN A 4   ? 0.7362 0.3776 0.5814 -0.0791 -0.1775 0.0386  3   ASN B C     
11   O  O     . ASN A 4   ? 0.7835 0.4093 0.6233 -0.0789 -0.1782 0.0455  3   ASN B O     
12   C  CB    . ASN A 4   ? 0.6180 0.3274 0.5092 -0.1149 -0.1713 0.0608  3   ASN B CB    
13   C  CG    . ASN A 4   ? 0.5758 0.3223 0.4883 -0.1301 -0.1715 0.0643  3   ASN B CG    
14   O  OD1   . ASN A 4   ? 0.5906 0.3318 0.4964 -0.1289 -0.1782 0.0541  3   ASN B OD1   
15   N  ND2   . ASN A 4   ? 0.5401 0.3266 0.4777 -0.1421 -0.1634 0.0784  3   ASN B ND2   
16   N  N     . PRO A 5   ? 0.7101 0.3492 0.5462 -0.0585 -0.1730 0.0254  4   PRO B N     
17   C  CA    . PRO A 5   ? 0.6867 0.3098 0.5089 -0.0336 -0.1679 0.0192  4   PRO B CA    
18   C  C     . PRO A 5   ? 0.6563 0.3051 0.4958 -0.0308 -0.1565 0.0316  4   PRO B C     
19   O  O     . PRO A 5   ? 0.5834 0.2727 0.4467 -0.0427 -0.1482 0.0406  4   PRO B O     
20   C  CB    . PRO A 5   ? 0.7122 0.3373 0.5239 -0.0141 -0.1644 0.0028  4   PRO B CB    
21   C  CG    . PRO A 5   ? 0.6722 0.3375 0.5041 -0.0279 -0.1596 0.0052  4   PRO B CG    
22   C  CD    . PRO A 5   ? 0.6763 0.3291 0.5135 -0.0560 -0.1725 0.0150  4   PRO B CD    
23   N  N     . THR A 6   ? 0.6084 0.2452 0.4379 -0.0123 -0.1537 0.0299  5   THR B N     
24   C  CA    . THR A 6   ? 0.6301 0.2912 0.4726 -0.0062 -0.1438 0.0404  5   THR B CA    
25   C  C     . THR A 6   ? 0.6124 0.2829 0.4499 0.0224  -0.1361 0.0293  5   THR B C     
26   O  O     . THR A 6   ? 0.6390 0.2827 0.4574 0.0392  -0.1408 0.0181  5   THR B O     
27   C  CB    . THR A 6   ? 0.6479 0.2921 0.4855 -0.0130 -0.1477 0.0507  5   THR B CB    
28   O  OG1   . THR A 6   ? 0.6533 0.3041 0.5018 -0.0406 -0.1512 0.0631  5   THR B OG1   
29   C  CG2   . THR A 6   ? 0.6661 0.3324 0.5120 -0.0021 -0.1384 0.0586  5   THR B CG2   
30   N  N     . VAL A 7   ? 0.5546 0.2728 0.4123 0.0271  -0.1222 0.0307  6   VAL B N     
31   C  CA    . VAL A 7   ? 0.5237 0.2609 0.3819 0.0509  -0.1138 0.0216  6   VAL B CA    
32   C  C     . VAL A 7   ? 0.5179 0.2814 0.3892 0.0544  -0.1069 0.0311  6   VAL B C     
33   O  O     . VAL A 7   ? 0.4771 0.2534 0.3594 0.0384  -0.1053 0.0431  6   VAL B O     
34   C  CB    . VAL A 7   ? 0.5023 0.2727 0.3706 0.0538  -0.1040 0.0122  6   VAL B CB    
35   C  CG1   . VAL A 7   ? 0.5099 0.2566 0.3633 0.0505  -0.1113 0.0026  6   VAL B CG1   
36   C  CG2   . VAL A 7   ? 0.4604 0.2681 0.3514 0.0387  -0.0957 0.0199  6   VAL B CG2   
37   N  N     . PHE A 8   ? 0.5209 0.2952 0.3907 0.0761  -0.1029 0.0254  7   PHE B N     
38   C  CA    . PHE A 8   ? 0.4905 0.2901 0.3711 0.0812  -0.0980 0.0330  7   PHE B CA    
39   C  C     . PHE A 8   ? 0.4463 0.2877 0.3407 0.0941  -0.0873 0.0250  7   PHE B C     
40   O  O     . PHE A 8   ? 0.4344 0.2775 0.3243 0.1073  -0.0850 0.0139  7   PHE B O     
41   C  CB    . PHE A 8   ? 0.4886 0.2582 0.3534 0.0954  -0.1068 0.0374  7   PHE B CB    
42   C  CG    . PHE A 8   ? 0.5487 0.3162 0.4059 0.1200  -0.1055 0.0244  7   PHE B CG    
43   C  CD1   . PHE A 8   ? 0.5865 0.3185 0.4249 0.1261  -0.1115 0.0141  7   PHE B CD1   
44   C  CD2   . PHE A 8   ? 0.5350 0.3392 0.4040 0.1365  -0.0984 0.0218  7   PHE B CD2   
45   C  CE1   . PHE A 8   ? 0.6132 0.3462 0.4433 0.1498  -0.1095 0.0018  7   PHE B CE1   
46   C  CE2   . PHE A 8   ? 0.5450 0.3530 0.4088 0.1582  -0.0962 0.0104  7   PHE B CE2   
47   C  CZ    . PHE A 8   ? 0.5762 0.3489 0.4200 0.1658  -0.1013 0.0005  7   PHE B CZ    
48   N  N     . PHE A 9   ? 0.4091 0.2841 0.3193 0.0901  -0.0812 0.0311  8   PHE B N     
49   C  CA    . PHE A 9   ? 0.3825 0.2973 0.3066 0.1010  -0.0731 0.0261  8   PHE B CA    
50   C  C     . PHE A 9   ? 0.4167 0.3380 0.3405 0.1114  -0.0767 0.0324  8   PHE B C     
51   O  O     . PHE A 9   ? 0.3911 0.3069 0.3134 0.1011  -0.0797 0.0427  8   PHE B O     
52   C  CB    . PHE A 9   ? 0.3611 0.3111 0.3039 0.0858  -0.0641 0.0270  8   PHE B CB    
53   C  CG    . PHE A 9   ? 0.3338 0.2854 0.2800 0.0756  -0.0597 0.0220  8   PHE B CG    
54   C  CD1   . PHE A 9   ? 0.3684 0.2999 0.3027 0.0818  -0.0619 0.0147  8   PHE B CD1   
55   C  CD2   . PHE A 9   ? 0.2729 0.2469 0.2330 0.0617  -0.0535 0.0238  8   PHE B CD2   
56   C  CE1   . PHE A 9   ? 0.3407 0.2764 0.2775 0.0725  -0.0582 0.0108  8   PHE B CE1   
57   C  CE2   . PHE A 9   ? 0.2911 0.2673 0.2544 0.0535  -0.0499 0.0203  8   PHE B CE2   
58   C  CZ    . PHE A 9   ? 0.3123 0.2708 0.2642 0.0587  -0.0523 0.0143  8   PHE B CZ    
59   N  N     . ASP A 10  ? 0.3635 0.3008 0.2896 0.1313  -0.0758 0.0269  9   ASP B N     
60   C  CA    . ASP A 10  ? 0.3777 0.3347 0.3090 0.1405  -0.0779 0.0321  9   ASP B CA    
61   C  C     . ASP A 10  ? 0.3720 0.3785 0.3250 0.1343  -0.0695 0.0294  9   ASP B C     
62   O  O     . ASP A 10  ? 0.3499 0.3807 0.3130 0.1398  -0.0630 0.0212  9   ASP B O     
63   C  CB    . ASP A 10  ? 0.4099 0.3592 0.3350 0.1599  -0.0797 0.0269  9   ASP B CB    
64   C  CG    . ASP A 10  ? 0.4950 0.3943 0.3993 0.1619  -0.0884 0.0309  9   ASP B CG    
65   O  OD1   . ASP A 10  ? 0.5424 0.4231 0.4409 0.1489  -0.0933 0.0421  9   ASP B OD1   
66   O  OD2   . ASP A 10  ? 0.5610 0.4406 0.4540 0.1762  -0.0903 0.0230  9   ASP B OD2   
67   N  N     . ILE A 11  ? 0.3281 0.3485 0.2870 0.1215  -0.0695 0.0363  10  ILE B N     
68   C  CA    . ILE A 11  ? 0.3163 0.3764 0.2930 0.1117  -0.0630 0.0334  10  ILE B CA    
69   C  C     . ILE A 11  ? 0.3082 0.3981 0.2929 0.1235  -0.0657 0.0335  10  ILE B C     
70   O  O     . ILE A 11  ? 0.3115 0.3900 0.2879 0.1289  -0.0714 0.0392  10  ILE B O     
71   C  CB    . ILE A 11  ? 0.3154 0.3748 0.2923 0.0925  -0.0614 0.0387  10  ILE B CB    
72   C  CG1   . ILE A 11  ? 0.3100 0.3420 0.2807 0.0804  -0.0595 0.0398  10  ILE B CG1   
73   C  CG2   . ILE A 11  ? 0.2522 0.3467 0.2453 0.0828  -0.0556 0.0334  10  ILE B CG2   
74   C  CD1   . ILE A 11  ? 0.2936 0.3312 0.2721 0.0764  -0.0530 0.0314  10  ILE B CD1   
75   N  N     . ALA A 12  ? 0.2538 0.3800 0.2558 0.1216  -0.0600 0.0270  11  ALA B N     
76   C  CA    . ALA A 12  ? 0.2755 0.4324 0.2887 0.1240  -0.0604 0.0258  11  ALA B CA    
77   C  C     . ALA A 12  ? 0.2759 0.4634 0.3038 0.1075  -0.0570 0.0230  11  ALA B C     
78   O  O     . ALA A 12  ? 0.2395 0.4302 0.2728 0.0970  -0.0523 0.0204  11  ALA B O     
79   C  CB    . ALA A 12  ? 0.2745 0.4472 0.2942 0.1391  -0.0573 0.0204  11  ALA B CB    
80   N  N     . VAL A 13  ? 0.2262 0.4340 0.2595 0.1051  -0.0602 0.0235  12  VAL B N     
81   C  CA    . VAL A 13  ? 0.2397 0.4712 0.2834 0.0891  -0.0593 0.0203  12  VAL B CA    
82   C  C     . VAL A 13  ? 0.2524 0.5156 0.3101 0.0919  -0.0592 0.0172  12  VAL B C     
83   O  O     . VAL A 13  ? 0.2449 0.5127 0.2999 0.1018  -0.0645 0.0198  12  VAL B O     
84   C  CB    . VAL A 13  ? 0.2794 0.5033 0.3124 0.0822  -0.0646 0.0236  12  VAL B CB    
85   C  CG1   . VAL A 13  ? 0.2923 0.5369 0.3337 0.0664  -0.0644 0.0179  12  VAL B CG1   
86   C  CG2   . VAL A 13  ? 0.2570 0.4513 0.2755 0.0800  -0.0643 0.0286  12  VAL B CG2   
87   N  N     . ASP A 14  ? 0.2214 0.5066 0.2940 0.0828  -0.0535 0.0128  13  ASP B N     
88   C  CA    . ASP A 14  ? 0.2120 0.5298 0.2993 0.0850  -0.0521 0.0110  13  ASP B CA    
89   C  C     . ASP A 14  ? 0.2460 0.5628 0.3291 0.1066  -0.0532 0.0128  13  ASP B C     
90   O  O     . ASP A 14  ? 0.2467 0.5845 0.3359 0.1129  -0.0569 0.0135  13  ASP B O     
91   C  CB    . ASP A 14  ? 0.2707 0.6085 0.3647 0.0739  -0.0580 0.0099  13  ASP B CB    
92   C  CG    . ASP A 14  ? 0.2782 0.6192 0.3781 0.0522  -0.0566 0.0063  13  ASP B CG    
93   O  OD1   . ASP A 14  ? 0.2611 0.5984 0.3652 0.0455  -0.0499 0.0053  13  ASP B OD1   
94   O  OD2   . ASP A 14  ? 0.2712 0.6167 0.3698 0.0426  -0.0628 0.0042  13  ASP B OD2   
95   N  N     . GLY A 15  ? 0.2477 0.5390 0.3197 0.1183  -0.0507 0.0133  14  GLY B N     
96   C  CA    . GLY A 15  ? 0.2740 0.5601 0.3402 0.1396  -0.0512 0.0132  14  GLY B CA    
97   C  C     . GLY A 15  ? 0.3051 0.5659 0.3567 0.1511  -0.0597 0.0180  14  GLY B C     
98   O  O     . GLY A 15  ? 0.3028 0.5520 0.3467 0.1695  -0.0613 0.0179  14  GLY B O     
99   N  N     . GLU A 16  ? 0.2802 0.5315 0.3264 0.1408  -0.0654 0.0222  15  GLU B N     
100  C  CA    . GLU A 16  ? 0.2684 0.4979 0.3004 0.1498  -0.0737 0.0287  15  GLU B CA    
101  C  C     . GLU A 16  ? 0.2955 0.4832 0.3098 0.1478  -0.0752 0.0334  15  GLU B C     
102  O  O     . GLU A 16  ? 0.2936 0.4771 0.3077 0.1333  -0.0724 0.0330  15  GLU B O     
103  C  CB    . GLU A 16  ? 0.3269 0.5745 0.3618 0.1402  -0.0792 0.0313  15  GLU B CB    
104  C  CG    . GLU A 16  ? 0.3561 0.5841 0.3756 0.1464  -0.0877 0.0394  15  GLU B CG    
105  C  CD    . GLU A 16  ? 0.3923 0.6360 0.4113 0.1330  -0.0919 0.0405  15  GLU B CD    
106  O  OE1   . GLU A 16  ? 0.4745 0.6981 0.4788 0.1254  -0.0939 0.0455  15  GLU B OE1   
107  O  OE2   . GLU A 16  ? 0.3834 0.6605 0.4166 0.1297  -0.0927 0.0359  15  GLU B OE2   
108  N  N     . PRO A 17  ? 0.3009 0.4569 0.3006 0.1613  -0.0796 0.0376  16  PRO B N     
109  C  CA    . PRO A 17  ? 0.3338 0.4484 0.3166 0.1571  -0.0817 0.0429  16  PRO B CA    
110  C  C     . PRO A 17  ? 0.3457 0.4562 0.3224 0.1414  -0.0843 0.0502  16  PRO B C     
111  O  O     . PRO A 17  ? 0.3141 0.4354 0.2891 0.1405  -0.0889 0.0549  16  PRO B O     
112  C  CB    . PRO A 17  ? 0.3347 0.4182 0.3029 0.1731  -0.0881 0.0474  16  PRO B CB    
113  C  CG    . PRO A 17  ? 0.3588 0.4676 0.3378 0.1894  -0.0854 0.0394  16  PRO B CG    
114  C  CD    . PRO A 17  ? 0.3253 0.4813 0.3233 0.1810  -0.0828 0.0371  16  PRO B CD    
115  N  N     . LEU A 18  ? 0.3536 0.4491 0.3259 0.1300  -0.0812 0.0511  17  LEU B N     
116  C  CA    . LEU A 18  ? 0.3354 0.4231 0.2988 0.1157  -0.0822 0.0583  17  LEU B CA    
117  C  C     . LEU A 18  ? 0.3573 0.4032 0.3022 0.1147  -0.0863 0.0687  17  LEU B C     
118  O  O     . LEU A 18  ? 0.3541 0.3895 0.2870 0.1106  -0.0907 0.0792  17  LEU B O     
119  C  CB    . LEU A 18  ? 0.3028 0.4067 0.2758 0.1027  -0.0754 0.0525  17  LEU B CB    
120  C  CG    . LEU A 18  ? 0.3168 0.4197 0.2816 0.0888  -0.0746 0.0586  17  LEU B CG    
121  C  CD1   . LEU A 18  ? 0.3378 0.4575 0.2992 0.0872  -0.0779 0.0608  17  LEU B CD1   
122  C  CD2   . LEU A 18  ? 0.2263 0.3386 0.2027 0.0736  -0.0656 0.0499  17  LEU B CD2   
123  N  N     . GLY A 19  ? 0.3561 0.3772 0.2973 0.1174  -0.0855 0.0661  18  GLY B N     
124  C  CA    . GLY A 19  ? 0.3903 0.3685 0.3142 0.1141  -0.0902 0.0751  18  GLY B CA    
125  C  C     . GLY A 19  ? 0.4087 0.3653 0.3303 0.1110  -0.0884 0.0695  18  GLY B C     
126  O  O     . GLY A 19  ? 0.3748 0.3514 0.3088 0.1104  -0.0821 0.0593  18  GLY B O     
127  N  N     . ARG A 20  ? 0.4051 0.3211 0.3122 0.1050  -0.0933 0.0765  19  ARG B N     
128  C  CA    . ARG A 20  ? 0.4533 0.3422 0.3553 0.1001  -0.0940 0.0712  19  ARG B CA    
129  C  C     . ARG A 20  ? 0.4533 0.3428 0.3592 0.0762  -0.0902 0.0770  19  ARG B C     
130  O  O     . ARG A 20  ? 0.4431 0.3254 0.3427 0.0650  -0.0925 0.0901  19  ARG B O     
131  C  CB    . ARG A 20  ? 0.4606 0.3064 0.3474 0.1049  -0.1006 0.0724  19  ARG B CB    
132  C  CG    . ARG A 20  ? 0.5281 0.3444 0.4078 0.0973  -0.1029 0.0664  19  ARG B CG    
133  C  CD    . ARG A 20  ? 0.5399 0.3160 0.4034 0.1071  -0.1097 0.0621  19  ARG B CD    
134  N  NE    . ARG A 20  ? 0.5626 0.3506 0.4272 0.1308  -0.1076 0.0502  19  ARG B NE    
135  C  CZ    . ARG A 20  ? 0.6080 0.3670 0.4583 0.1442  -0.1122 0.0420  19  ARG B CZ    
136  N  NH1   . ARG A 20  ? 0.6256 0.3397 0.4590 0.1358  -0.1204 0.0440  19  ARG B NH1   
137  N  NH2   . ARG A 20  ? 0.5672 0.3445 0.4203 0.1659  -0.1086 0.0312  19  ARG B NH2   
138  N  N     . VAL A 21  ? 0.3938 0.2927 0.3098 0.0685  -0.0842 0.0680  20  VAL B N     
139  C  CA    . VAL A 21  ? 0.3820 0.2787 0.3020 0.0478  -0.0817 0.0726  20  VAL B CA    
140  C  C     . VAL A 21  ? 0.4129 0.2784 0.3254 0.0451  -0.0868 0.0678  20  VAL B C     
141  O  O     . VAL A 21  ? 0.4354 0.2976 0.3464 0.0573  -0.0865 0.0562  20  VAL B O     
142  C  CB    . VAL A 21  ? 0.4013 0.3366 0.3394 0.0398  -0.0713 0.0674  20  VAL B CB    
143  C  CG1   . VAL A 21  ? 0.3867 0.3376 0.3328 0.0499  -0.0670 0.0548  20  VAL B CG1   
144  C  CG2   . VAL A 21  ? 0.3658 0.2979 0.3087 0.0225  -0.0694 0.0700  20  VAL B CG2   
145  N  N     . SER A 22  ? 0.4369 0.2805 0.3439 0.0289  -0.0917 0.0765  21  SER B N     
146  C  CA    . SER A 22  ? 0.4319 0.2468 0.3316 0.0241  -0.0979 0.0710  21  SER B CA    
147  C  C     . SER A 22  ? 0.4455 0.2755 0.3578 0.0035  -0.0946 0.0738  21  SER B C     
148  O  O     . SER A 22  ? 0.4323 0.2875 0.3559 -0.0081 -0.0889 0.0827  21  SER B O     
149  C  CB    . SER A 22  ? 0.5124 0.2774 0.3909 0.0243  -0.1110 0.0774  21  SER B CB    
150  O  OG    . SER A 22  ? 0.5517 0.3153 0.4314 0.0059  -0.1119 0.0927  21  SER B OG    
151  N  N     . PHE A 23  ? 0.4454 0.2624 0.3554 0.0009  -0.0982 0.0653  22  PHE B N     
152  C  CA    . PHE A 23  ? 0.4353 0.2698 0.3585 -0.0156 -0.0958 0.0660  22  PHE B CA    
153  C  C     . PHE A 23  ? 0.4710 0.2721 0.3836 -0.0268 -0.1076 0.0657  22  PHE B C     
154  O  O     . PHE A 23  ? 0.5015 0.2699 0.3966 -0.0168 -0.1152 0.0567  22  PHE B O     
155  C  CB    . PHE A 23  ? 0.3812 0.2428 0.3152 -0.0087 -0.0876 0.0548  22  PHE B CB    
156  C  CG    . PHE A 23  ? 0.3569 0.2470 0.2993 0.0032  -0.0776 0.0518  22  PHE B CG    
157  C  CD1   . PHE A 23  ? 0.3752 0.2612 0.3103 0.0210  -0.0768 0.0440  22  PHE B CD1   
158  C  CD2   . PHE A 23  ? 0.3317 0.2538 0.2894 -0.0032 -0.0694 0.0562  22  PHE B CD2   
159  C  CE1   . PHE A 23  ? 0.3741 0.2885 0.3183 0.0301  -0.0688 0.0413  22  PHE B CE1   
160  C  CE2   . PHE A 23  ? 0.3108 0.2575 0.2753 0.0067  -0.0615 0.0520  22  PHE B CE2   
161  C  CZ    . PHE A 23  ? 0.3403 0.2838 0.2990 0.0219  -0.0617 0.0453  22  PHE B CZ    
162  N  N     . GLU A 24  ? 0.4498 0.2611 0.3731 -0.0473 -0.1091 0.0749  23  GLU B N     
163  C  CA    . GLU A 24  ? 0.4977 0.2877 0.4165 -0.0615 -0.1201 0.0736  23  GLU B CA    
164  C  C     . GLU A 24  ? 0.4428 0.2602 0.3737 -0.0602 -0.1153 0.0644  23  GLU B C     
165  O  O     . GLU A 24  ? 0.3839 0.2405 0.3332 -0.0600 -0.1045 0.0666  23  GLU B O     
166  C  CB    . GLU A 24  ? 0.4905 0.2809 0.4165 -0.0860 -0.1251 0.0898  23  GLU B CB    
167  C  CG    . GLU A 24  ? 0.5330 0.3103 0.4591 -0.1029 -0.1367 0.0881  23  GLU B CG    
168  C  CD    . GLU A 24  ? 0.6141 0.4018 0.5496 -0.1254 -0.1403 0.1008  23  GLU B CD    
169  O  OE1   . GLU A 24  ? 0.6232 0.4173 0.5605 -0.1295 -0.1359 0.1122  23  GLU B OE1   
170  O  OE2   . GLU A 24  ? 0.6220 0.4139 0.5628 -0.1382 -0.1476 0.0991  23  GLU B OE2   
171  N  N     . LEU A 25  ? 0.4612 0.2562 0.3794 -0.0571 -0.1234 0.0534  24  LEU B N     
172  C  CA    . LEU A 25  ? 0.4302 0.2464 0.3557 -0.0555 -0.1207 0.0453  24  LEU B CA    
173  C  C     . LEU A 25  ? 0.4513 0.2633 0.3804 -0.0755 -0.1320 0.0486  24  LEU B C     
174  O  O     . LEU A 25  ? 0.4750 0.2497 0.3877 -0.0832 -0.1456 0.0468  24  LEU B O     
175  C  CB    . LEU A 25  ? 0.4379 0.2365 0.3449 -0.0369 -0.1213 0.0304  24  LEU B CB    
176  C  CG    . LEU A 25  ? 0.4469 0.2485 0.3490 -0.0162 -0.1121 0.0259  24  LEU B CG    
177  C  CD1   . LEU A 25  ? 0.4776 0.2682 0.3628 0.0008  -0.1121 0.0113  24  LEU B CD1   
178  C  CD2   . LEU A 25  ? 0.3750 0.2183 0.2985 -0.0140 -0.0981 0.0313  24  LEU B CD2   
179  N  N     . PHE A 26  ? 0.4123 0.2614 0.3622 -0.0834 -0.1275 0.0527  25  PHE B N     
180  C  CA    . PHE A 26  ? 0.4236 0.2784 0.3831 -0.1045 -0.1378 0.0590  25  PHE B CA    
181  C  C     . PHE A 26  ? 0.4434 0.2846 0.3909 -0.1038 -0.1483 0.0477  25  PHE B C     
182  O  O     . PHE A 26  ? 0.4001 0.2692 0.3601 -0.1052 -0.1474 0.0468  25  PHE B O     
183  C  CB    . PHE A 26  ? 0.3854 0.2892 0.3732 -0.1109 -0.1284 0.0686  25  PHE B CB    
184  C  CG    . PHE A 26  ? 0.4174 0.3370 0.4147 -0.1114 -0.1178 0.0793  25  PHE B CG    
185  C  CD1   . PHE A 26  ? 0.4547 0.3494 0.4427 -0.1211 -0.1229 0.0878  25  PHE B CD1   
186  C  CD2   . PHE A 26  ? 0.3274 0.2840 0.3406 -0.1023 -0.1038 0.0806  25  PHE B CD2   
187  C  CE1   . PHE A 26  ? 0.4357 0.3463 0.4303 -0.1219 -0.1135 0.0985  25  PHE B CE1   
188  C  CE2   . PHE A 26  ? 0.3759 0.3480 0.3956 -0.1029 -0.0948 0.0896  25  PHE B CE2   
189  C  CZ    . PHE A 26  ? 0.3738 0.3245 0.3841 -0.1125 -0.0993 0.0987  25  PHE B CZ    
190  N  N     . ALA A 27  ? 0.4562 0.2526 0.3771 -0.0996 -0.1585 0.0384  26  ALA B N     
191  C  CA    . ALA A 27  ? 0.4825 0.2624 0.3867 -0.0977 -0.1692 0.0261  26  ALA B CA    
192  C  C     . ALA A 27  ? 0.4977 0.2895 0.4129 -0.1179 -0.1794 0.0319  26  ALA B C     
193  O  O     . ALA A 27  ? 0.4875 0.2847 0.3977 -0.1161 -0.1842 0.0248  26  ALA B O     
194  C  CB    . ALA A 27  ? 0.5453 0.2722 0.4167 -0.0885 -0.1786 0.0143  26  ALA B CB    
195  N  N     . ASP A 28  ? 0.4524 0.2522 0.3815 -0.1338 -0.1800 0.0454  27  ASP B N     
196  C  CA    . ASP A 28  ? 0.4914 0.3110 0.4341 -0.1504 -0.1857 0.0525  27  ASP B CA    
197  C  C     . ASP A 28  ? 0.4895 0.3576 0.4566 -0.1502 -0.1792 0.0555  27  ASP B C     
198  O  O     . ASP A 28  ? 0.4790 0.3599 0.4517 -0.1576 -0.1855 0.0554  27  ASP B O     
199  C  CB    . ASP A 28  ? 0.5385 0.3622 0.4917 -0.1669 -0.1858 0.0673  27  ASP B CB    
200  C  CG    . ASP A 28  ? 0.5417 0.3924 0.5127 -0.1653 -0.1721 0.0780  27  ASP B CG    
201  O  OD1   . ASP A 28  ? 0.5218 0.3789 0.4940 -0.1516 -0.1640 0.0733  27  ASP B OD1   
202  O  OD2   . ASP A 28  ? 0.6711 0.5365 0.6538 -0.1781 -0.1697 0.0913  27  ASP B OD2   
203  N  N     . LYS A 29  ? 0.4450 0.3394 0.4260 -0.1407 -0.1673 0.0575  28  LYS B N     
204  C  CA    . LYS A 29  ? 0.3988 0.3399 0.4036 -0.1374 -0.1598 0.0611  28  LYS B CA    
205  C  C     . LYS A 29  ? 0.3709 0.3140 0.3679 -0.1204 -0.1574 0.0508  28  LYS B C     
206  O  O     . LYS A 29  ? 0.3658 0.3310 0.3703 -0.1169 -0.1577 0.0498  28  LYS B O     
207  C  CB    . LYS A 29  ? 0.4232 0.3991 0.4521 -0.1390 -0.1469 0.0728  28  LYS B CB    
208  C  CG    . LYS A 29  ? 0.4582 0.4555 0.5033 -0.1548 -0.1465 0.0853  28  LYS B CG    
209  C  CD    . LYS A 29  ? 0.5365 0.5478 0.5884 -0.1621 -0.1544 0.0849  28  LYS B CD    
210  C  CE    . LYS A 29  ? 0.5562 0.6197 0.6371 -0.1647 -0.1464 0.0942  28  LYS B CE    
211  N  NZ    . LYS A 29  ? 0.5532 0.6352 0.6425 -0.1668 -0.1537 0.0917  28  LYS B NZ    
212  N  N     . VAL A 30  ? 0.3879 0.3079 0.3673 -0.1059 -0.1513 0.0435  29  VAL B N     
213  C  CA    . VAL A 30  ? 0.3786 0.2996 0.3469 -0.0867 -0.1441 0.0344  29  VAL B CA    
214  C  C     . VAL A 30  ? 0.3868 0.2680 0.3245 -0.0770 -0.1479 0.0225  29  VAL B C     
215  O  O     . VAL A 30  ? 0.3852 0.2594 0.3161 -0.0632 -0.1374 0.0193  29  VAL B O     
216  C  CB    . VAL A 30  ? 0.3677 0.3112 0.3485 -0.0737 -0.1266 0.0375  29  VAL B CB    
217  C  CG1   . VAL A 30  ? 0.3164 0.2963 0.3185 -0.0731 -0.1222 0.0431  29  VAL B CG1   
218  C  CG2   . VAL A 30  ? 0.3509 0.2926 0.3384 -0.0768 -0.1202 0.0437  29  VAL B CG2   
219  N  N     . PRO A 31  ? 0.4088 0.2649 0.3274 -0.0825 -0.1628 0.0150  30  PRO B N     
220  C  CA    . PRO A 31  ? 0.4520 0.2672 0.3396 -0.0719 -0.1668 0.0026  30  PRO B CA    
221  C  C     . PRO A 31  ? 0.4480 0.2677 0.3226 -0.0501 -0.1551 -0.0057 30  PRO B C     
222  O  O     . PRO A 31  ? 0.4721 0.2710 0.3304 -0.0365 -0.1505 -0.0127 30  PRO B O     
223  C  CB    . PRO A 31  ? 0.4501 0.2432 0.3220 -0.0830 -0.1845 -0.0035 30  PRO B CB    
224  C  CG    . PRO A 31  ? 0.4735 0.3063 0.3678 -0.0917 -0.1847 0.0042  30  PRO B CG    
225  C  CD    . PRO A 31  ? 0.4094 0.2734 0.3346 -0.0986 -0.1760 0.0177  30  PRO B CD    
226  N  N     . LYS A 32  ? 0.4024 0.2485 0.2828 -0.0462 -0.1507 -0.0047 31  LYS B N     
227  C  CA    . LYS A 32  ? 0.4302 0.2819 0.2982 -0.0281 -0.1393 -0.0106 31  LYS B CA    
228  C  C     . LYS A 32  ? 0.3943 0.2601 0.2757 -0.0190 -0.1231 -0.0062 31  LYS B C     
229  O  O     . LYS A 32  ? 0.3844 0.2430 0.2525 -0.0047 -0.1155 -0.0126 31  LYS B O     
230  C  CB    . LYS A 32  ? 0.4231 0.2985 0.2945 -0.0277 -0.1390 -0.0077 31  LYS B CB    
231  C  CG    . LYS A 32  ? 0.4245 0.3018 0.2774 -0.0117 -0.1297 -0.0134 31  LYS B CG    
232  C  CD    . LYS A 32  ? 0.4768 0.3682 0.3239 -0.0122 -0.1341 -0.0112 31  LYS B CD    
233  C  CE    . LYS A 32  ? 0.4604 0.3560 0.2892 0.0021  -0.1233 -0.0143 31  LYS B CE    
234  N  NZ    . LYS A 32  ? 0.4684 0.3736 0.2861 0.0022  -0.1287 -0.0116 31  LYS B NZ    
235  N  N     . THR A 33  ? 0.3741 0.2628 0.2818 -0.0265 -0.1178 0.0043  32  THR B N     
236  C  CA    . THR A 33  ? 0.3294 0.2334 0.2504 -0.0196 -0.1037 0.0084  32  THR B CA    
237  C  C     . THR A 33  ? 0.3356 0.2200 0.2509 -0.0170 -0.1038 0.0067  32  THR B C     
238  O  O     . THR A 33  ? 0.3441 0.2312 0.2574 -0.0054 -0.0944 0.0044  32  THR B O     
239  C  CB    . THR A 33  ? 0.3187 0.2507 0.2661 -0.0277 -0.0997 0.0186  32  THR B CB    
240  O  OG1   . THR A 33  ? 0.3140 0.2603 0.2649 -0.0293 -0.1028 0.0204  32  THR B OG1   
241  C  CG2   . THR A 33  ? 0.2707 0.2187 0.2300 -0.0203 -0.0855 0.0214  32  THR B CG2   
242  N  N     . ALA A 34  ? 0.3751 0.2391 0.2869 -0.0281 -0.1153 0.0083  33  ALA B N     
243  C  CA    . ALA A 34  ? 0.3911 0.2300 0.2937 -0.0253 -0.1174 0.0075  33  ALA B CA    
244  C  C     . ALA A 34  ? 0.4246 0.2380 0.3013 -0.0084 -0.1185 -0.0050 33  ALA B C     
245  O  O     . ALA A 34  ? 0.4220 0.2291 0.2945 0.0038  -0.1130 -0.0067 33  ALA B O     
246  C  CB    . ALA A 34  ? 0.4095 0.2288 0.3124 -0.0433 -0.1308 0.0131  33  ALA B CB    
247  N  N     . GLU A 35  ? 0.4068 0.2073 0.2652 -0.0060 -0.1256 -0.0142 34  GLU B N     
248  C  CA    . GLU A 35  ? 0.4608 0.2380 0.2924 0.0120  -0.1261 -0.0273 34  GLU B CA    
249  C  C     . GLU A 35  ? 0.4425 0.2466 0.2779 0.0290  -0.1099 -0.0292 34  GLU B C     
250  O  O     . GLU A 35  ? 0.4838 0.2786 0.3073 0.0457  -0.1060 -0.0360 34  GLU B O     
251  C  CB    . GLU A 35  ? 0.5055 0.2641 0.3143 0.0105  -0.1376 -0.0373 34  GLU B CB    
252  C  CG    . GLU A 35  ? 0.5375 0.2794 0.3161 0.0315  -0.1362 -0.0526 34  GLU B CG    
253  C  CD    . GLU A 35  ? 0.6249 0.3301 0.3850 0.0448  -0.1406 -0.0609 34  GLU B CD    
254  O  OE1   . GLU A 35  ? 0.6274 0.3108 0.3931 0.0345  -0.1486 -0.0550 34  GLU B OE1   
255  O  OE2   . GLU A 35  ? 0.6447 0.3431 0.3837 0.0664  -0.1359 -0.0729 34  GLU B OE2   
256  N  N     . ASN A 36  ? 0.4046 0.2416 0.2557 0.0251  -0.1012 -0.0233 35  ASN B N     
257  C  CA    . ASN A 36  ? 0.3884 0.2523 0.2466 0.0368  -0.0861 -0.0226 35  ASN B CA    
258  C  C     . ASN A 36  ? 0.3901 0.2588 0.2600 0.0422  -0.0801 -0.0194 35  ASN B C     
259  O  O     . ASN A 36  ? 0.3933 0.2666 0.2572 0.0574  -0.0733 -0.0245 35  ASN B O     
260  C  CB    . ASN A 36  ? 0.3721 0.2648 0.2480 0.0281  -0.0798 -0.0142 35  ASN B CB    
261  C  CG    . ASN A 36  ? 0.3445 0.2636 0.2277 0.0363  -0.0653 -0.0123 35  ASN B CG    
262  O  OD1   . ASN A 36  ? 0.3545 0.2770 0.2231 0.0476  -0.0601 -0.0181 35  ASN B OD1   
263  N  ND2   . ASN A 36  ? 0.3223 0.2611 0.2280 0.0297  -0.0588 -0.0039 35  ASN B ND2   
264  N  N     . PHE A 37  ? 0.3728 0.2438 0.2596 0.0303  -0.0822 -0.0106 36  PHE B N     
265  C  CA    . PHE A 37  ? 0.3821 0.2607 0.2797 0.0348  -0.0766 -0.0065 36  PHE B CA    
266  C  C     . PHE A 37  ? 0.4194 0.2691 0.2996 0.0467  -0.0826 -0.0123 36  PHE B C     
267  O  O     . PHE A 37  ? 0.3847 0.2425 0.2663 0.0599  -0.0767 -0.0137 36  PHE B O     
268  C  CB    . PHE A 37  ? 0.3476 0.2341 0.2636 0.0198  -0.0779 0.0042  36  PHE B CB    
269  C  CG    . PHE A 37  ? 0.3293 0.2297 0.2570 0.0234  -0.0712 0.0091  36  PHE B CG    
270  C  CD1   . PHE A 37  ? 0.2846 0.2157 0.2282 0.0236  -0.0608 0.0115  36  PHE B CD1   
271  C  CD2   . PHE A 37  ? 0.3351 0.2167 0.2571 0.0255  -0.0764 0.0119  36  PHE B CD2   
272  C  CE1   . PHE A 37  ? 0.2936 0.2384 0.2469 0.0262  -0.0558 0.0151  36  PHE B CE1   
273  C  CE2   . PHE A 37  ? 0.3390 0.2360 0.2710 0.0290  -0.0708 0.0171  36  PHE B CE2   
274  C  CZ    . PHE A 37  ? 0.3131 0.2427 0.2606 0.0292  -0.0607 0.0179  36  PHE B CZ    
275  N  N     . ARG A 38  ? 0.4244 0.2398 0.2880 0.0422  -0.0953 -0.0158 37  ARG B N     
276  C  CA    . ARG A 38  ? 0.4811 0.2610 0.3243 0.0543  -0.1029 -0.0222 37  ARG B CA    
277  C  C     . ARG A 38  ? 0.5091 0.2925 0.3378 0.0775  -0.0967 -0.0341 37  ARG B C     
278  O  O     . ARG A 38  ? 0.4868 0.2684 0.3128 0.0938  -0.0938 -0.0362 37  ARG B O     
279  C  CB    . ARG A 38  ? 0.4807 0.2203 0.3061 0.0433  -0.1191 -0.0255 37  ARG B CB    
280  C  CG    . ARG A 38  ? 0.5418 0.2360 0.3446 0.0541  -0.1292 -0.0310 37  ARG B CG    
281  C  CD    . ARG A 38  ? 0.6637 0.3113 0.4409 0.0476  -0.1462 -0.0395 37  ARG B CD    
282  N  NE    . ARG A 38  ? 0.6574 0.3052 0.4163 0.0598  -0.1454 -0.0542 37  ARG B NE    
283  C  CZ    . ARG A 38  ? 0.7079 0.3518 0.4494 0.0855  -0.1400 -0.0666 37  ARG B CZ    
284  N  NH1   . ARG A 38  ? 0.6978 0.3298 0.4348 0.1034  -0.1379 -0.0678 37  ARG B NH1   
285  N  NH2   . ARG A 38  ? 0.7165 0.3715 0.4446 0.0944  -0.1363 -0.0774 37  ARG B NH2   
286  N  N     . ALA A 39  ? 0.4698 0.2604 0.2886 0.0799  -0.0947 -0.0415 38  ALA B N     
287  C  CA    . ALA A 39  ? 0.4912 0.2877 0.2942 0.1021  -0.0880 -0.0528 38  ALA B CA    
288  C  C     . ALA A 39  ? 0.4900 0.3284 0.3124 0.1114  -0.0727 -0.0485 38  ALA B C     
289  O  O     . ALA A 39  ? 0.4892 0.3328 0.3043 0.1319  -0.0678 -0.0552 38  ALA B O     
290  C  CB    . ALA A 39  ? 0.5082 0.3067 0.2958 0.1010  -0.0885 -0.0598 38  ALA B CB    
291  N  N     . LEU A 40  ? 0.4224 0.2915 0.2694 0.0968  -0.0655 -0.0376 39  LEU B N     
292  C  CA    . LEU A 40  ? 0.3602 0.2670 0.2257 0.1029  -0.0529 -0.0336 39  LEU B CA    
293  C  C     . LEU A 40  ? 0.3733 0.2773 0.2459 0.1109  -0.0545 -0.0312 39  LEU B C     
294  O  O     . LEU A 40  ? 0.3722 0.3018 0.2527 0.1239  -0.0466 -0.0321 39  LEU B O     
295  C  CB    . LEU A 40  ? 0.3152 0.2477 0.2021 0.0852  -0.0471 -0.0238 39  LEU B CB    
296  C  CG    . LEU A 40  ? 0.3581 0.2974 0.2388 0.0790  -0.0447 -0.0243 39  LEU B CG    
297  C  CD1   . LEU A 40  ? 0.3174 0.2736 0.2178 0.0620  -0.0418 -0.0143 39  LEU B CD1   
298  C  CD2   . LEU A 40  ? 0.3590 0.3207 0.2331 0.0922  -0.0343 -0.0289 39  LEU B CD2   
299  N  N     . SER A 41  ? 0.3926 0.2681 0.2631 0.1026  -0.0648 -0.0269 40  SER B N     
300  C  CA    . SER A 41  ? 0.4289 0.2971 0.3020 0.1109  -0.0677 -0.0235 40  SER B CA    
301  C  C     . SER A 41  ? 0.4807 0.3268 0.3332 0.1350  -0.0717 -0.0337 40  SER B C     
302  O  O     . SER A 41  ? 0.4896 0.3458 0.3465 0.1499  -0.0697 -0.0330 40  SER B O     
303  C  CB    . SER A 41  ? 0.4390 0.2820 0.3134 0.0945  -0.0773 -0.0145 40  SER B CB    
304  O  OG    . SER A 41  ? 0.4026 0.2698 0.2964 0.0755  -0.0726 -0.0061 40  SER B OG    
305  N  N     . THR A 42  ? 0.5200 0.3370 0.3490 0.1410  -0.0776 -0.0439 41  THR B N     
306  C  CA    . THR A 42  ? 0.5571 0.3517 0.3646 0.1669  -0.0812 -0.0551 41  THR B CA    
307  C  C     . THR A 42  ? 0.5540 0.3848 0.3619 0.1871  -0.0685 -0.0635 41  THR B C     
308  O  O     . THR A 42  ? 0.5519 0.3766 0.3478 0.2124  -0.0686 -0.0720 41  THR B O     
309  C  CB    . THR A 42  ? 0.6226 0.3647 0.3999 0.1678  -0.0946 -0.0651 41  THR B CB    
310  O  OG1   . THR A 42  ? 0.6072 0.3601 0.3771 0.1625  -0.0910 -0.0717 41  THR B OG1   
311  C  CG2   . THR A 42  ? 0.5712 0.2767 0.3477 0.1460  -0.1081 -0.0558 41  THR B CG2   
312  N  N     . GLY A 43  ? 0.4855 0.3529 0.3056 0.1769  -0.0580 -0.0612 42  GLY B N     
313  C  CA    . GLY A 43  ? 0.5096 0.4132 0.3292 0.1928  -0.0453 -0.0675 42  GLY B CA    
314  C  C     . GLY A 43  ? 0.5512 0.4347 0.3407 0.2067  -0.0470 -0.0814 42  GLY B C     
315  O  O     . GLY A 43  ? 0.5887 0.5020 0.3741 0.2235  -0.0359 -0.0876 42  GLY B O     
316  N  N     . GLU A 44  ? 0.6188 0.4547 0.3868 0.1993  -0.0605 -0.0864 43  GLU B N     
317  C  CA    . GLU A 44  ? 0.6596 0.4691 0.3962 0.2129  -0.0657 -0.1003 43  GLU B CA    
318  C  C     . GLU A 44  ? 0.6870 0.5245 0.4165 0.2126  -0.0559 -0.1039 43  GLU B C     
319  O  O     . GLU A 44  ? 0.6726 0.5075 0.3844 0.2250  -0.0555 -0.1117 43  GLU B O     
320  C  CB    . GLU A 44  ? 0.7535 0.5070 0.4723 0.1997  -0.0843 -0.1025 43  GLU B CB    
321  C  CG    . GLU A 44  ? 0.7104 0.4541 0.4299 0.1743  -0.0906 -0.0987 43  GLU B CG    
322  C  CD    . GLU A 44  ? 0.8142 0.5060 0.5232 0.1594  -0.1095 -0.0979 43  GLU B CD    
323  O  OE1   . GLU A 44  ? 0.7219 0.4003 0.4426 0.1550  -0.1139 -0.0896 43  GLU B OE1   
324  O  OE2   . GLU A 44  ? 0.8181 0.4876 0.5102 0.1502  -0.1195 -0.1029 43  GLU B OE2   
325  N  N     . LYS A 45  ? 0.6009 0.4687 0.3480 0.1949  -0.0482 -0.0942 44  LYS B N     
326  C  CA    . LYS A 45  ? 0.6013 0.4954 0.3396 0.1947  -0.0387 -0.0957 44  LYS B CA    
327  C  C     . LYS A 45  ? 0.5979 0.5435 0.3488 0.2084  -0.0208 -0.0934 44  LYS B C     
328  O  O     . LYS A 45  ? 0.6261 0.5994 0.3744 0.2055  -0.0112 -0.0907 44  LYS B O     
329  C  CB    . LYS A 45  ? 0.5374 0.4406 0.2905 0.1671  -0.0397 -0.0831 44  LYS B CB    
330  C  CG    . LYS A 45  ? 0.5515 0.4130 0.2986 0.1507  -0.0569 -0.0828 44  LYS B CG    
331  C  CD    . LYS A 45  ? 0.6554 0.4820 0.3663 0.1579  -0.0678 -0.0972 44  LYS B CD    
332  C  CE    . LYS A 45  ? 0.6613 0.4575 0.3703 0.1360  -0.0842 -0.0943 44  LYS B CE    
333  N  NZ    . LYS A 45  ? 0.6776 0.4343 0.3536 0.1409  -0.0979 -0.1082 44  LYS B NZ    
334  N  N     . GLY A 46  ? 0.5690 0.5306 0.3379 0.2195  -0.0171 -0.0913 45  GLY B N     
335  C  CA    . GLY A 46  ? 0.5511 0.5670 0.3409 0.2267  -0.0020 -0.0854 45  GLY B CA    
336  C  C     . GLY A 46  ? 0.5246 0.5778 0.3450 0.2120  0.0068  -0.0731 45  GLY B C     
337  O  O     . GLY A 46  ? 0.4738 0.5749 0.3134 0.2135  0.0190  -0.0669 45  GLY B O     
338  N  N     . PHE A 47  ? 0.4348 0.4673 0.2673 0.1897  -0.0019 -0.0646 46  PHE B N     
339  C  CA    . PHE A 47  ? 0.4173 0.4766 0.2803 0.1693  0.0025  -0.0508 46  PHE B CA    
340  C  C     . PHE A 47  ? 0.4319 0.4583 0.3013 0.1548  -0.0099 -0.0463 46  PHE B C     
341  O  O     . PHE A 47  ? 0.4212 0.4067 0.2724 0.1542  -0.0211 -0.0513 46  PHE B O     
342  C  CB    . PHE A 47  ? 0.4157 0.4973 0.2833 0.1522  0.0107  -0.0427 46  PHE B CB    
343  C  CG    . PHE A 47  ? 0.4528 0.5028 0.2998 0.1430  0.0033  -0.0444 46  PHE B CG    
344  C  CD1   . PHE A 47  ? 0.4128 0.4402 0.2671 0.1238  -0.0059 -0.0380 46  PHE B CD1   
345  C  CD2   . PHE A 47  ? 0.4711 0.5179 0.2914 0.1542  0.0058  -0.0523 46  PHE B CD2   
346  C  CE1   . PHE A 47  ? 0.4347 0.4375 0.2718 0.1157  -0.0136 -0.0393 46  PHE B CE1   
347  C  CE2   . PHE A 47  ? 0.4727 0.4925 0.2731 0.1458  -0.0023 -0.0541 46  PHE B CE2   
348  C  CZ    . PHE A 47  ? 0.4858 0.4848 0.2961 0.1261  -0.0124 -0.0471 46  PHE B CZ    
349  N  N     . GLY A 48  ? 0.3795 0.4245 0.2743 0.1421  -0.0081 -0.0367 47  GLY B N     
350  C  CA    . GLY A 48  ? 0.3622 0.3799 0.2622 0.1300  -0.0184 -0.0322 47  GLY B CA    
351  C  C     . GLY A 48  ? 0.3294 0.3707 0.2541 0.1233  -0.0159 -0.0245 47  GLY B C     
352  O  O     . GLY A 48  ? 0.2904 0.3693 0.2302 0.1241  -0.0069 -0.0219 47  GLY B O     
353  N  N     . TYR A 49  ? 0.3399 0.3585 0.2671 0.1165  -0.0247 -0.0208 48  TYR B N     
354  C  CA    . TYR A 49  ? 0.3067 0.3412 0.2536 0.1073  -0.0245 -0.0134 48  TYR B CA    
355  C  C     . TYR A 49  ? 0.3319 0.3876 0.2872 0.1219  -0.0231 -0.0141 48  TYR B C     
356  O  O     . TYR A 49  ? 0.2834 0.3630 0.2564 0.1147  -0.0210 -0.0089 48  TYR B O     
357  C  CB    . TYR A 49  ? 0.3034 0.3074 0.2468 0.0973  -0.0339 -0.0091 48  TYR B CB    
358  C  CG    . TYR A 49  ? 0.2978 0.2903 0.2400 0.0808  -0.0353 -0.0065 48  TYR B CG    
359  C  CD1   . TYR A 49  ? 0.2924 0.3072 0.2465 0.0699  -0.0282 -0.0034 48  TYR B CD1   
360  C  CD2   . TYR A 49  ? 0.3072 0.2665 0.2375 0.0754  -0.0447 -0.0061 48  TYR B CD2   
361  C  CE1   . TYR A 49  ? 0.2471 0.2514 0.2000 0.0572  -0.0303 -0.0008 48  TYR B CE1   
362  C  CE2   . TYR A 49  ? 0.3027 0.2560 0.2341 0.0612  -0.0467 -0.0034 48  TYR B CE2   
363  C  CZ    . TYR A 49  ? 0.3088 0.2854 0.2520 0.0532  -0.0394 -0.0007 48  TYR B CZ    
364  O  OH    . TYR A 49  ? 0.2778 0.2493 0.2224 0.0413  -0.0420 0.0023  48  TYR B OH    
365  N  N     . LYS A 50  ? 0.3363 0.3821 0.2784 0.1430  -0.0255 -0.0207 49  LYS B N     
366  C  CA    . LYS A 50  ? 0.3283 0.3923 0.2784 0.1589  -0.0262 -0.0205 49  LYS B CA    
367  C  C     . LYS A 50  ? 0.3170 0.4340 0.2901 0.1561  -0.0163 -0.0180 49  LYS B C     
368  O  O     . LYS A 50  ? 0.3135 0.4538 0.2884 0.1576  -0.0072 -0.0208 49  LYS B O     
369  C  CB    . LYS A 50  ? 0.3586 0.4055 0.2900 0.1854  -0.0291 -0.0295 49  LYS B CB    
370  C  CG    . LYS A 50  ? 0.3898 0.4587 0.3298 0.2049  -0.0299 -0.0294 49  LYS B CG    
371  C  CD    . LYS A 50  ? 0.4236 0.4589 0.3396 0.2237  -0.0356 -0.0370 49  LYS B CD    
372  C  CE    . LYS A 50  ? 0.4584 0.5088 0.3805 0.2352  -0.0372 -0.0352 49  LYS B CE    
373  N  NZ    . LYS A 50  ? 0.5520 0.5652 0.4485 0.2537  -0.0435 -0.0430 49  LYS B NZ    
374  N  N     . GLY A 51  ? 0.3108 0.4473 0.3008 0.1508  -0.0184 -0.0123 50  GLY B N     
375  C  CA    . GLY A 51  ? 0.2737 0.4602 0.2863 0.1467  -0.0113 -0.0099 50  GLY B CA    
376  C  C     . GLY A 51  ? 0.2731 0.4706 0.2980 0.1211  -0.0075 -0.0050 50  GLY B C     
377  O  O     . GLY A 51  ? 0.2455 0.4809 0.2896 0.1134  -0.0035 -0.0022 50  GLY B O     
378  N  N     . SER A 52  ? 0.2372 0.4029 0.2515 0.1083  -0.0090 -0.0040 51  SER B N     
379  C  CA    . SER A 52  ? 0.2355 0.4050 0.2588 0.0863  -0.0064 0.0003  51  SER B CA    
380  C  C     . SER A 52  ? 0.2649 0.4313 0.2958 0.0766  -0.0124 0.0036  51  SER B C     
381  O  O     . SER A 52  ? 0.2492 0.4071 0.2765 0.0854  -0.0189 0.0041  51  SER B O     
382  C  CB    . SER A 52  ? 0.2292 0.3690 0.2384 0.0791  -0.0062 0.0000  51  SER B CB    
383  O  OG    . SER A 52  ? 0.2747 0.3791 0.2715 0.0803  -0.0143 -0.0002 51  SER B OG    
384  N  N     . CYS A 53  ? 0.2102 0.3845 0.2506 0.0592  -0.0103 0.0060  52  CYS B N     
385  C  CA    . CYS A 53  ? 0.1893 0.3640 0.2356 0.0506  -0.0151 0.0076  52  CYS B CA    
386  C  C     . CYS A 53  ? 0.2068 0.3550 0.2465 0.0393  -0.0166 0.0089  52  CYS B C     
387  O  O     . CYS A 53  ? 0.2133 0.3465 0.2476 0.0347  -0.0140 0.0093  52  CYS B O     
388  C  CB    . CYS A 53  ? 0.1865 0.3919 0.2491 0.0397  -0.0134 0.0078  52  CYS B CB    
389  S  SG    . CYS A 53  ? 0.4310 0.6353 0.4981 0.0208  -0.0077 0.0093  52  CYS B SG    
390  N  N     . PHE A 54  ? 0.1916 0.3361 0.2313 0.0362  -0.0212 0.0099  53  PHE B N     
391  C  CA    . PHE A 54  ? 0.1963 0.3253 0.2333 0.0256  -0.0218 0.0106  53  PHE B CA    
392  C  C     . PHE A 54  ? 0.1861 0.3295 0.2327 0.0141  -0.0199 0.0082  53  PHE B C     
393  O  O     . PHE A 54  ? 0.1964 0.3555 0.2484 0.0117  -0.0228 0.0064  53  PHE B O     
394  C  CB    . PHE A 54  ? 0.1941 0.3140 0.2245 0.0281  -0.0266 0.0130  53  PHE B CB    
395  C  CG    . PHE A 54  ? 0.2265 0.3227 0.2460 0.0333  -0.0290 0.0167  53  PHE B CG    
396  C  CD1   . PHE A 54  ? 0.2203 0.3101 0.2333 0.0455  -0.0324 0.0177  53  PHE B CD1   
397  C  CD2   . PHE A 54  ? 0.2203 0.3002 0.2361 0.0260  -0.0286 0.0190  53  PHE B CD2   
398  C  CE1   . PHE A 54  ? 0.2347 0.2987 0.2364 0.0484  -0.0360 0.0205  53  PHE B CE1   
399  C  CE2   . PHE A 54  ? 0.2118 0.2713 0.2188 0.0279  -0.0319 0.0228  53  PHE B CE2   
400  C  CZ    . PHE A 54  ? 0.2208 0.2697 0.2197 0.0381  -0.0361 0.0235  53  PHE B CZ    
401  N  N     . HIS A 55  ? 0.1601 0.2974 0.2080 0.0067  -0.0160 0.0083  54  HIS B N     
402  C  CA    . HIS A 55  ? 0.1310 0.2787 0.1872 -0.0052 -0.0149 0.0067  54  HIS B CA    
403  C  C     . HIS A 55  ? 0.1505 0.2846 0.2039 -0.0124 -0.0174 0.0038  54  HIS B C     
404  O  O     . HIS A 55  ? 0.1704 0.3097 0.2287 -0.0224 -0.0187 0.0010  54  HIS B O     
405  C  CB    . HIS A 55  ? 0.1573 0.3027 0.2145 -0.0109 -0.0099 0.0096  54  HIS B CB    
406  C  CG    . HIS A 55  ? 0.1757 0.2963 0.2236 -0.0101 -0.0088 0.0114  54  HIS B CG    
407  N  ND1   . HIS A 55  ? 0.1811 0.2921 0.2209 -0.0007 -0.0086 0.0126  54  HIS B ND1   
408  C  CD2   . HIS A 55  ? 0.1665 0.2706 0.2120 -0.0174 -0.0086 0.0123  54  HIS B CD2   
409  C  CE1   . HIS A 55  ? 0.1830 0.2759 0.2172 -0.0032 -0.0086 0.0144  54  HIS B CE1   
410  N  NE2   . HIS A 55  ? 0.1818 0.2706 0.2196 -0.0122 -0.0084 0.0145  54  HIS B NE2   
411  N  N     . ARG A 56  ? 0.1623 0.2789 0.2078 -0.0081 -0.0179 0.0042  55  ARG B N     
412  C  CA    . ARG A 56  ? 0.1753 0.2806 0.2174 -0.0122 -0.0190 0.0008  55  ARG B CA    
413  C  C     . ARG A 56  ? 0.2155 0.3194 0.2516 -0.0059 -0.0205 0.0013  55  ARG B C     
414  O  O     . ARG A 56  ? 0.2213 0.3181 0.2543 -0.0011 -0.0198 0.0059  55  ARG B O     
415  C  CB    . ARG A 56  ? 0.1821 0.2696 0.2222 -0.0144 -0.0165 0.0022  55  ARG B CB    
416  C  CG    . ARG A 56  ? 0.2141 0.2895 0.2502 -0.0142 -0.0172 -0.0017 55  ARG B CG    
417  C  CD    . ARG A 56  ? 0.2045 0.2642 0.2395 -0.0139 -0.0155 0.0012  55  ARG B CD    
418  N  NE    . ARG A 56  ? 0.2142 0.2670 0.2504 -0.0217 -0.0155 0.0016  55  ARG B NE    
419  C  CZ    . ARG A 56  ? 0.2420 0.2836 0.2767 -0.0227 -0.0143 0.0064  55  ARG B CZ    
420  N  NH1   . ARG A 56  ? 0.2453 0.2827 0.2779 -0.0162 -0.0139 0.0101  55  ARG B NH1   
421  N  NH2   . ARG A 56  ? 0.2359 0.2705 0.2706 -0.0315 -0.0143 0.0082  55  ARG B NH2   
422  N  N     . ILE A 57  ? 0.1884 0.2994 0.2221 -0.0068 -0.0230 -0.0028 56  ILE B N     
423  C  CA    . ILE A 57  ? 0.1650 0.2778 0.1915 -0.0017 -0.0238 -0.0010 56  ILE B CA    
424  C  C     . ILE A 57  ? 0.1934 0.3039 0.2145 -0.0036 -0.0236 -0.0077 56  ILE B C     
425  O  O     . ILE A 57  ? 0.1894 0.3044 0.2100 -0.0080 -0.0267 -0.0145 56  ILE B O     
426  C  CB    . ILE A 57  ? 0.1740 0.3007 0.1989 0.0025  -0.0278 0.0014  56  ILE B CB    
427  C  CG1   . ILE A 57  ? 0.2163 0.3418 0.2440 0.0080  -0.0280 0.0071  56  ILE B CG1   
428  C  CG2   . ILE A 57  ? 0.2013 0.3294 0.2161 0.0059  -0.0285 0.0039  56  ILE B CG2   
429  C  CD1   . ILE A 57  ? 0.1977 0.3378 0.2258 0.0144  -0.0324 0.0088  56  ILE B CD1   
430  N  N     . ILE A 58  ? 0.1754 0.2796 0.1927 -0.0005 -0.0202 -0.0066 57  ILE B N     
431  C  CA    . ILE A 58  ? 0.1866 0.2883 0.1976 0.0007  -0.0191 -0.0143 57  ILE B CA    
432  C  C     . ILE A 58  ? 0.2044 0.3165 0.2078 0.0058  -0.0167 -0.0111 57  ILE B C     
433  O  O     . ILE A 58  ? 0.1879 0.3011 0.1936 0.0081  -0.0130 -0.0043 57  ILE B O     
434  C  CB    . ILE A 58  ? 0.1756 0.2626 0.1895 0.0015  -0.0164 -0.0167 57  ILE B CB    
435  C  CG1   . ILE A 58  ? 0.2148 0.2912 0.2341 -0.0053 -0.0188 -0.0181 57  ILE B CG1   
436  C  CG2   . ILE A 58  ? 0.2251 0.3088 0.2307 0.0064  -0.0151 -0.0258 57  ILE B CG2   
437  C  CD1   . ILE A 58  ? 0.2351 0.2950 0.2567 -0.0046 -0.0172 -0.0175 57  ILE B CD1   
438  N  N     . PRO A 59  ? 0.2126 0.3348 0.2070 0.0066  -0.0192 -0.0145 58  PRO B N     
439  C  CA    . PRO A 59  ? 0.1872 0.3213 0.1724 0.0108  -0.0165 -0.0093 58  PRO B CA    
440  C  C     . PRO A 59  ? 0.2366 0.3723 0.2200 0.0152  -0.0098 -0.0110 58  PRO B C     
441  O  O     . PRO A 59  ? 0.2076 0.3362 0.1890 0.0181  -0.0087 -0.0216 58  PRO B O     
442  C  CB    . PRO A 59  ? 0.2252 0.3684 0.1989 0.0111  -0.0212 -0.0160 58  PRO B CB    
443  C  CG    . PRO A 59  ? 0.2116 0.3522 0.1937 0.0059  -0.0276 -0.0188 58  PRO B CG    
444  C  CD    . PRO A 59  ? 0.2238 0.3495 0.2159 0.0027  -0.0253 -0.0220 58  PRO B CD    
445  N  N     . GLY A 60  ? 0.2220 0.3672 0.2063 0.0158  -0.0057 0.0001  59  GLY B N     
446  C  CA    . GLY A 60  ? 0.2131 0.3673 0.1995 0.0198  0.0014  0.0012  59  GLY B CA    
447  C  C     . GLY A 60  ? 0.1932 0.3410 0.1942 0.0179  0.0024  0.0065  59  GLY B C     
448  O  O     . GLY A 60  ? 0.2067 0.3669 0.2130 0.0203  0.0077  0.0105  59  GLY B O     
449  N  N     . PHE A 61  ? 0.1803 0.3122 0.1876 0.0138  -0.0025 0.0067  60  PHE B N     
450  C  CA    . PHE A 61  ? 0.1827 0.3074 0.2014 0.0124  -0.0025 0.0105  60  PHE B CA    
451  C  C     . PHE A 61  ? 0.1700 0.2855 0.1923 0.0065  -0.0070 0.0185  60  PHE B C     
452  O  O     . PHE A 61  ? 0.1707 0.2887 0.1973 0.0030  -0.0072 0.0274  60  PHE B O     
453  C  CB    . PHE A 61  ? 0.2403 0.3516 0.2611 0.0156  -0.0033 0.0008  60  PHE B CB    
454  C  CG    . PHE A 61  ? 0.2232 0.3388 0.2394 0.0239  0.0005  -0.0080 60  PHE B CG    
455  C  CD1   . PHE A 61  ? 0.2567 0.3816 0.2794 0.0305  0.0048  -0.0063 60  PHE B CD1   
456  C  CD2   . PHE A 61  ? 0.2302 0.3413 0.2351 0.0260  -0.0008 -0.0188 60  PHE B CD2   
457  C  CE1   . PHE A 61  ? 0.2676 0.3967 0.2850 0.0418  0.0088  -0.0159 60  PHE B CE1   
458  C  CE2   . PHE A 61  ? 0.2772 0.3886 0.2747 0.0357  0.0024  -0.0290 60  PHE B CE2   
459  C  CZ    . PHE A 61  ? 0.3026 0.4230 0.3061 0.0447  0.0077  -0.0276 60  PHE B CZ    
460  N  N     . MET A 62  ? 0.1672 0.2729 0.1877 0.0053  -0.0108 0.0154  61  MET B N     
461  C  CA    . MET A 62  ? 0.1573 0.2533 0.1802 0.0027  -0.0144 0.0208  61  MET B CA    
462  C  C     . MET A 62  ? 0.1793 0.2718 0.2004 0.0033  -0.0174 0.0173  61  MET B C     
463  O  O     . MET A 62  ? 0.2009 0.2978 0.2213 0.0034  -0.0174 0.0105  61  MET B O     
464  C  CB    . MET A 62  ? 0.1892 0.2771 0.2190 0.0015  -0.0145 0.0220  61  MET B CB    
465  C  CG    . MET A 62  ? 0.2415 0.3273 0.2751 0.0041  -0.0121 0.0156  61  MET B CG    
466  S  SD    . MET A 62  ? 0.2214 0.3002 0.2519 0.0036  -0.0128 0.0068  61  MET B SD    
467  C  CE    . MET A 62  ? 0.2454 0.3185 0.2766 0.0007  -0.0156 0.0115  61  MET B CE    
468  N  N     . CYS A 63  ? 0.2041 0.2893 0.2244 0.0038  -0.0203 0.0218  62  CYS B N     
469  C  CA    . CYS A 63  ? 0.1660 0.2511 0.1863 0.0064  -0.0226 0.0194  62  CYS B CA    
470  C  C     . CYS A 63  ? 0.1986 0.2736 0.2209 0.0065  -0.0225 0.0194  62  CYS B C     
471  O  O     . CYS A 63  ? 0.2210 0.2853 0.2403 0.0065  -0.0245 0.0237  62  CYS B O     
472  C  CB    . CYS A 63  ? 0.1808 0.2648 0.1949 0.0109  -0.0265 0.0244  62  CYS B CB    
473  S  SG    . CYS A 63  ? 0.2400 0.3368 0.2480 0.0119  -0.0277 0.0263  62  CYS B SG    
474  N  N     . GLN A 64  ? 0.1760 0.2545 0.2021 0.0057  -0.0208 0.0153  63  GLN B N     
475  C  CA    . GLN A 64  ? 0.1859 0.2566 0.2118 0.0057  -0.0199 0.0157  63  GLN B CA    
476  C  C     . GLN A 64  ? 0.1997 0.2773 0.2255 0.0099  -0.0194 0.0143  63  GLN B C     
477  O  O     . GLN A 64  ? 0.1909 0.2833 0.2218 0.0093  -0.0186 0.0121  63  GLN B O     
478  C  CB    . GLN A 64  ? 0.1906 0.2588 0.2202 0.0007  -0.0174 0.0139  63  GLN B CB    
479  C  CG    . GLN A 64  ? 0.1956 0.2572 0.2234 0.0000  -0.0163 0.0153  63  GLN B CG    
480  C  CD    . GLN A 64  ? 0.2132 0.2680 0.2427 -0.0041 -0.0151 0.0154  63  GLN B CD    
481  O  OE1   . GLN A 64  ? 0.2111 0.2641 0.2429 -0.0044 -0.0153 0.0137  63  GLN B OE1   
482  N  NE2   . GLN A 64  ? 0.1736 0.2238 0.2005 -0.0059 -0.0138 0.0177  63  GLN B NE2   
483  N  N     . GLY A 65  ? 0.1852 0.2539 0.2051 0.0144  -0.0201 0.0152  64  GLY B N     
484  C  CA    . GLY A 65  ? 0.1569 0.2358 0.1764 0.0204  -0.0180 0.0132  64  GLY B CA    
485  C  C     . GLY A 65  ? 0.1736 0.2423 0.1850 0.0230  -0.0171 0.0129  64  GLY B C     
486  O  O     . GLY A 65  ? 0.1943 0.2528 0.2036 0.0174  -0.0173 0.0144  64  GLY B O     
487  N  N     . GLY A 66  ? 0.2018 0.2753 0.2081 0.0327  -0.0160 0.0105  65  GLY B N     
488  C  CA    . GLY A 66  ? 0.2045 0.2666 0.1987 0.0372  -0.0158 0.0087  65  GLY B CA    
489  C  C     . GLY A 66  ? 0.2306 0.3079 0.2249 0.0364  -0.0089 0.0088  65  GLY B C     
490  O  O     . GLY A 66  ? 0.2321 0.3011 0.2134 0.0412  -0.0086 0.0070  65  GLY B O     
491  N  N     . ASP A 67  ? 0.2156 0.3152 0.2227 0.0298  -0.0037 0.0112  66  ASP B N     
492  C  CA    . ASP A 67  ? 0.2170 0.3336 0.2246 0.0272  0.0035  0.0134  66  ASP B CA    
493  C  C     . ASP A 67  ? 0.2334 0.3738 0.2428 0.0390  0.0078  0.0105  66  ASP B C     
494  O  O     . ASP A 67  ? 0.2270 0.3929 0.2507 0.0371  0.0102  0.0114  66  ASP B O     
495  C  CB    . ASP A 67  ? 0.2097 0.3368 0.2298 0.0124  0.0061  0.0181  66  ASP B CB    
496  C  CG    . ASP A 67  ? 0.2108 0.3577 0.2324 0.0069  0.0140  0.0229  66  ASP B CG    
497  O  OD1   . ASP A 67  ? 0.2347 0.3901 0.2471 0.0158  0.0185  0.0223  66  ASP B OD1   
498  O  OD2   . ASP A 67  ? 0.1859 0.3385 0.2163 -0.0069 0.0155  0.0275  66  ASP B OD2   
499  N  N     . PHE A 68  ? 0.1848 0.3189 0.1792 0.0517  0.0087  0.0066  67  PHE B N     
500  C  CA    . PHE A 68  ? 0.2280 0.3840 0.2220 0.0671  0.0130  0.0025  67  PHE B CA    
501  C  C     . PHE A 68  ? 0.2645 0.4461 0.2568 0.0671  0.0232  0.0048  67  PHE B C     
502  O  O     . PHE A 68  ? 0.2615 0.4667 0.2533 0.0815  0.0286  0.0013  67  PHE B O     
503  C  CB    . PHE A 68  ? 0.2672 0.3984 0.2433 0.0847  0.0071  -0.0052 67  PHE B CB    
504  C  CG    . PHE A 68  ? 0.2628 0.3675 0.2185 0.0849  0.0046  -0.0078 67  PHE B CG    
505  C  CD1   . PHE A 68  ? 0.3057 0.4196 0.2478 0.0931  0.0109  -0.0108 67  PHE B CD1   
506  C  CD2   . PHE A 68  ? 0.2625 0.3353 0.2122 0.0768  -0.0043 -0.0070 67  PHE B CD2   
507  C  CE1   . PHE A 68  ? 0.3270 0.4158 0.2483 0.0927  0.0071  -0.0136 67  PHE B CE1   
508  C  CE2   . PHE A 68  ? 0.2935 0.3444 0.2253 0.0760  -0.0080 -0.0094 67  PHE B CE2   
509  C  CZ    . PHE A 68  ? 0.3180 0.3761 0.2355 0.0838  -0.0029 -0.0129 67  PHE B CZ    
510  N  N     . THR A 69  ? 0.2457 0.4239 0.2363 0.0525  0.0260  0.0112  68  THR B N     
511  C  CA    . THR A 69  ? 0.2512 0.4552 0.2391 0.0510  0.0363  0.0156  68  THR B CA    
512  C  C     . THR A 69  ? 0.2367 0.4712 0.2454 0.0349  0.0421  0.0241  68  THR B C     
513  O  O     . THR A 69  ? 0.2778 0.5480 0.2918 0.0359  0.0517  0.0276  68  THR B O     
514  C  CB    . THR A 69  ? 0.2939 0.4764 0.2630 0.0459  0.0362  0.0188  68  THR B CB    
515  O  OG1   . THR A 69  ? 0.2595 0.4257 0.2352 0.0282  0.0322  0.0259  68  THR B OG1   
516  C  CG2   . THR A 69  ? 0.2969 0.4477 0.2457 0.0587  0.0283  0.0100  68  THR B CG2   
517  N  N     . ARG A 70  ? 0.2446 0.4665 0.2647 0.0199  0.0364  0.0273  69  ARG B N     
518  C  CA    . ARG A 70  ? 0.2480 0.4913 0.2862 0.0020  0.0393  0.0346  69  ARG B CA    
519  C  C     . ARG A 70  ? 0.2288 0.4809 0.2841 -0.0005 0.0336  0.0310  69  ARG B C     
520  O  O     . ARG A 70  ? 0.2407 0.5191 0.3130 -0.0134 0.0355  0.0353  69  ARG B O     
521  C  CB    . ARG A 70  ? 0.2486 0.4656 0.2822 -0.0153 0.0368  0.0415  69  ARG B CB    
522  C  CG    . ARG A 70  ? 0.2949 0.5078 0.3119 -0.0162 0.0428  0.0481  69  ARG B CG    
523  C  CD    . ARG A 70  ? 0.3043 0.4902 0.3171 -0.0312 0.0392  0.0556  69  ARG B CD    
524  N  NE    . ARG A 70  ? 0.3941 0.5727 0.3883 -0.0307 0.0432  0.0623  69  ARG B NE    
525  C  CZ    . ARG A 70  ? 0.3942 0.5434 0.3784 -0.0375 0.0386  0.0681  69  ARG B CZ    
526  N  NH1   . ARG A 70  ? 0.3387 0.4653 0.3307 -0.0464 0.0315  0.0686  69  ARG B NH1   
527  N  NH2   . ARG A 70  ? 0.4150 0.5570 0.3798 -0.0332 0.0404  0.0727  69  ARG B NH2   
528  N  N     . HIS A 71  ? 0.2369 0.4674 0.2876 0.0097  0.0260  0.0242  70  HIS B N     
529  C  CA    . HIS A 71  ? 0.2166 0.4534 0.2798 0.0093  0.0197  0.0209  70  HIS B CA    
530  C  C     . HIS A 71  ? 0.2957 0.5309 0.3694 -0.0108 0.0170  0.0241  70  HIS B C     
531  O  O     . HIS A 71  ? 0.2959 0.5520 0.3839 -0.0161 0.0141  0.0231  70  HIS B O     
532  C  CB    . HIS A 71  ? 0.2377 0.5132 0.3131 0.0200  0.0223  0.0191  70  HIS B CB    
533  C  CG    . HIS A 71  ? 0.2694 0.5471 0.3332 0.0419  0.0256  0.0148  70  HIS B CG    
534  N  ND1   . HIS A 71  ? 0.2268 0.4837 0.2806 0.0586  0.0192  0.0088  70  HIS B ND1   
535  C  CD2   . HIS A 71  ? 0.2294 0.5250 0.2876 0.0500  0.0343  0.0154  70  HIS B CD2   
536  C  CE1   . HIS A 71  ? 0.2554 0.5137 0.2974 0.0765  0.0228  0.0047  70  HIS B CE1   
537  N  NE2   . HIS A 71  ? 0.2722 0.5559 0.3165 0.0727  0.0325  0.0080  70  HIS B NE2   
538  N  N     . ASN A 72  ? 0.2524 0.4620 0.3183 -0.0216 0.0168  0.0277  71  ASN B N     
539  C  CA    . ASN A 72  ? 0.2478 0.4482 0.3204 -0.0388 0.0128  0.0291  71  ASN B CA    
540  C  C     . ASN A 72  ? 0.2277 0.3899 0.2894 -0.0394 0.0078  0.0272  71  ASN B C     
541  O  O     . ASN A 72  ? 0.2569 0.4047 0.3201 -0.0517 0.0046  0.0278  71  ASN B O     
542  C  CB    . ASN A 72  ? 0.2340 0.4492 0.3131 -0.0558 0.0179  0.0374  71  ASN B CB    
543  C  CG    . ASN A 72  ? 0.2829 0.4819 0.3482 -0.0575 0.0230  0.0446  71  ASN B CG    
544  O  OD1   . ASN A 72  ? 0.2631 0.4358 0.3146 -0.0483 0.0211  0.0429  71  ASN B OD1   
545  N  ND2   . ASN A 72  ? 0.2441 0.4614 0.3138 -0.0706 0.0291  0.0538  71  ASN B ND2   
546  N  N     . GLY A 73  ? 0.2114 0.3568 0.2622 -0.0266 0.0065  0.0248  72  GLY B N     
547  C  CA    . GLY A 73  ? 0.1789 0.2946 0.2218 -0.0268 0.0024  0.0239  72  GLY B CA    
548  C  C     . GLY A 73  ? 0.2177 0.3167 0.2508 -0.0293 0.0043  0.0296  72  GLY B C     
549  O  O     . GLY A 73  ? 0.2301 0.3072 0.2573 -0.0273 0.0006  0.0294  72  GLY B O     
550  N  N     . THR A 74  ? 0.1949 0.3057 0.2260 -0.0338 0.0099  0.0357  73  THR B N     
551  C  CA    . THR A 74  ? 0.2676 0.3615 0.2870 -0.0361 0.0108  0.0422  73  THR B CA    
552  C  C     . THR A 74  ? 0.2845 0.3811 0.2913 -0.0248 0.0131  0.0422  73  THR B C     
553  O  O     . THR A 74  ? 0.2776 0.3597 0.2723 -0.0245 0.0123  0.0468  73  THR B O     
554  C  CB    . THR A 74  ? 0.2607 0.3602 0.2816 -0.0505 0.0151  0.0512  73  THR B CB    
555  O  OG1   . THR A 74  ? 0.2514 0.3828 0.2756 -0.0504 0.0227  0.0539  73  THR B OG1   
556  C  CG2   . THR A 74  ? 0.2516 0.3441 0.2831 -0.0642 0.0113  0.0506  73  THR B CG2   
557  N  N     . GLY A 75  ? 0.2173 0.3308 0.2252 -0.0147 0.0151  0.0367  74  GLY B N     
558  C  CA    . GLY A 75  ? 0.2355 0.3521 0.2291 -0.0041 0.0178  0.0357  74  GLY B CA    
559  C  C     . GLY A 75  ? 0.2843 0.3840 0.2693 0.0078  0.0113  0.0283  74  GLY B C     
560  O  O     . GLY A 75  ? 0.2406 0.3223 0.2282 0.0060  0.0047  0.0269  74  GLY B O     
561  N  N     . GLY A 76  ? 0.2656 0.3717 0.2404 0.0200  0.0132  0.0234  75  GLY B N     
562  C  CA    . GLY A 76  ? 0.2795 0.3652 0.2423 0.0301  0.0061  0.0167  75  GLY B CA    
563  C  C     . GLY A 76  ? 0.2918 0.3652 0.2346 0.0330  0.0046  0.0167  75  GLY B C     
564  O  O     . GLY A 76  ? 0.3069 0.3821 0.2456 0.0258  0.0074  0.0235  75  GLY B O     
565  N  N     . LYS A 77  ? 0.2937 0.3528 0.2217 0.0440  -0.0006 0.0088  76  LYS B N     
566  C  CA    . LYS A 77  ? 0.2952 0.3394 0.2023 0.0463  -0.0048 0.0071  76  LYS B CA    
567  C  C     . LYS A 77  ? 0.3007 0.3197 0.1972 0.0523  -0.0156 -0.0012 76  LYS B C     
568  O  O     . LYS A 77  ? 0.3012 0.3158 0.2016 0.0587  -0.0175 -0.0062 76  LYS B O     
569  C  CB    . LYS A 77  ? 0.3027 0.3631 0.1937 0.0549  0.0037  0.0056  76  LYS B CB    
570  C  CG    . LYS A 77  ? 0.3412 0.4101 0.2268 0.0716  0.0072  -0.0041 76  LYS B CG    
571  C  CD    . LYS A 77  ? 0.3752 0.4662 0.2461 0.0811  0.0175  -0.0055 76  LYS B CD    
572  C  CE    . LYS A 77  ? 0.3755 0.4781 0.2435 0.1004  0.0214  -0.0154 76  LYS B CE    
573  N  NZ    . LYS A 77  ? 0.4488 0.5804 0.3037 0.1115  0.0337  -0.0167 76  LYS B NZ    
574  N  N     . SER A 78  ? 0.3267 0.3286 0.2095 0.0494  -0.0236 -0.0019 77  SER B N     
575  C  CA    . SER A 78  ? 0.3492 0.3252 0.2216 0.0514  -0.0356 -0.0090 77  SER B CA    
576  C  C     . SER A 78  ? 0.3891 0.3552 0.2352 0.0651  -0.0368 -0.0197 77  SER B C     
577  O  O     . SER A 78  ? 0.3935 0.3762 0.2293 0.0730  -0.0276 -0.0207 77  SER B O     
578  C  CB    . SER A 78  ? 0.3311 0.2960 0.2041 0.0403  -0.0455 -0.0048 77  SER B CB    
579  O  OG    . SER A 78  ? 0.3368 0.2981 0.1886 0.0426  -0.0483 -0.0066 77  SER B OG    
580  N  N     . ILE A 79  ? 0.3768 0.3149 0.2101 0.0677  -0.0486 -0.0278 78  ILE B N     
581  C  CA    . ILE A 79  ? 0.3930 0.3156 0.1966 0.0813  -0.0518 -0.0400 78  ILE B CA    
582  C  C     . ILE A 79  ? 0.4232 0.3413 0.2069 0.0779  -0.0569 -0.0413 78  ILE B C     
583  O  O     . ILE A 79  ? 0.4333 0.3383 0.1885 0.0892  -0.0602 -0.0525 78  ILE B O     
584  C  CB    . ILE A 79  ? 0.4443 0.3320 0.2374 0.0848  -0.0644 -0.0490 78  ILE B CB    
585  C  CG1   . ILE A 79  ? 0.4394 0.3080 0.2358 0.0673  -0.0788 -0.0454 78  ILE B CG1   
586  C  CG2   . ILE A 79  ? 0.4043 0.2948 0.2130 0.0903  -0.0603 -0.0475 78  ILE B CG2   
587  C  CD1   . ILE A 79  ? 0.4873 0.3162 0.2698 0.0668  -0.0937 -0.0536 78  ILE B CD1   
588  N  N     . TYR A 80  ? 0.4470 0.3750 0.2435 0.0640  -0.0584 -0.0306 79  TYR B N     
589  C  CA    . TYR A 80  ? 0.4264 0.3511 0.2068 0.0595  -0.0653 -0.0295 79  TYR B CA    
590  C  C     . TYR A 80  ? 0.4115 0.3610 0.1900 0.0601  -0.0538 -0.0206 79  TYR B C     
591  O  O     . TYR A 80  ? 0.4398 0.3891 0.2061 0.0562  -0.0589 -0.0168 79  TYR B O     
592  C  CB    . TYR A 80  ? 0.4350 0.3534 0.2317 0.0442  -0.0769 -0.0226 79  TYR B CB    
593  C  CG    . TYR A 80  ? 0.4358 0.3324 0.2384 0.0389  -0.0881 -0.0276 79  TYR B CG    
594  C  CD1   . TYR A 80  ? 0.4649 0.3336 0.2432 0.0421  -0.1003 -0.0398 79  TYR B CD1   
595  C  CD2   . TYR A 80  ? 0.3952 0.2977 0.2257 0.0301  -0.0869 -0.0200 79  TYR B CD2   
596  C  CE1   . TYR A 80  ? 0.4968 0.3421 0.2794 0.0353  -0.1113 -0.0429 79  TYR B CE1   
597  C  CE2   . TYR A 80  ? 0.4036 0.2869 0.2386 0.0242  -0.0964 -0.0225 79  TYR B CE2   
598  C  CZ    . TYR A 80  ? 0.4342 0.2879 0.2452 0.0260  -0.1088 -0.0334 79  TYR B CZ    
599  O  OH    . TYR A 80  ? 0.4479 0.2781 0.2612 0.0178  -0.1197 -0.0347 79  TYR B OH    
600  N  N     . GLY A 81  ? 0.4495 0.4206 0.2405 0.0635  -0.0393 -0.0158 80  GLY B N     
601  C  CA    . GLY A 81  ? 0.4146 0.4079 0.2119 0.0580  -0.0291 -0.0033 80  GLY B CA    
602  C  C     . GLY A 81  ? 0.3958 0.4017 0.2238 0.0501  -0.0225 0.0051  80  GLY B C     
603  O  O     . GLY A 81  ? 0.3695 0.3687 0.2133 0.0490  -0.0257 0.0017  80  GLY B O     
604  N  N     . GLU A 82  ? 0.3644 0.3879 0.1990 0.0441  -0.0131 0.0163  81  GLU B N     
605  C  CA    . GLU A 82  ? 0.3246 0.3585 0.1862 0.0363  -0.0075 0.0226  81  GLU B CA    
606  C  C     . GLU A 82  ? 0.3519 0.3707 0.2296 0.0290  -0.0171 0.0241  81  GLU B C     
607  O  O     . GLU A 82  ? 0.3424 0.3622 0.2377 0.0275  -0.0168 0.0218  81  GLU B O     
608  C  CB    . GLU A 82  ? 0.3413 0.3914 0.2074 0.0282  0.0021  0.0350  81  GLU B CB    
609  C  CG    . GLU A 82  ? 0.4696 0.5316 0.3610 0.0224  0.0077  0.0370  81  GLU B CG    
610  C  CD    . GLU A 82  ? 0.5643 0.6425 0.4642 0.0115  0.0169  0.0488  81  GLU B CD    
611  O  OE1   . GLU A 82  ? 0.6633 0.7299 0.5633 0.0023  0.0143  0.0584  81  GLU B OE1   
612  O  OE2   . GLU A 82  ? 0.5792 0.6815 0.4857 0.0123  0.0263  0.0486  81  GLU B OE2   
613  N  N     . LYS A 83  ? 0.3292 0.3361 0.2007 0.0255  -0.0259 0.0276  82  LYS B N     
614  C  CA    . LYS A 83  ? 0.3078 0.3053 0.1955 0.0200  -0.0346 0.0286  82  LYS B CA    
615  C  C     . LYS A 83  ? 0.3396 0.3242 0.2154 0.0206  -0.0476 0.0249  82  LYS B C     
616  O  O     . LYS A 83  ? 0.3868 0.3680 0.2401 0.0246  -0.0504 0.0227  82  LYS B O     
617  C  CB    . LYS A 83  ? 0.3475 0.3477 0.2479 0.0134  -0.0326 0.0392  82  LYS B CB    
618  C  CG    . LYS A 83  ? 0.3995 0.4112 0.3092 0.0098  -0.0208 0.0437  82  LYS B CG    
619  C  CD    . LYS A 83  ? 0.3980 0.4066 0.3260 0.0038  -0.0209 0.0485  82  LYS B CD    
620  C  CE    . LYS A 83  ? 0.4723 0.4837 0.4017 -0.0029 -0.0137 0.0576  82  LYS B CE    
621  N  NZ    . LYS A 83  ? 0.5598 0.5587 0.4796 -0.0042 -0.0183 0.0672  82  LYS B NZ    
622  N  N     . PHE A 84  ? 0.3139 0.2935 0.2047 0.0159  -0.0557 0.0242  83  PHE B N     
623  C  CA    . PHE A 84  ? 0.3346 0.3055 0.2184 0.0135  -0.0694 0.0220  83  PHE B CA    
624  C  C     . PHE A 84  ? 0.3037 0.2807 0.2100 0.0072  -0.0750 0.0281  83  PHE B C     
625  O  O     . PHE A 84  ? 0.3042 0.2883 0.2295 0.0057  -0.0685 0.0317  83  PHE B O     
626  C  CB    . PHE A 84  ? 0.3262 0.2826 0.1985 0.0148  -0.0763 0.0112  83  PHE B CB    
627  C  CG    . PHE A 84  ? 0.3247 0.2780 0.2140 0.0116  -0.0758 0.0092  83  PHE B CG    
628  C  CD1   . PHE A 84  ? 0.3119 0.2701 0.2077 0.0162  -0.0650 0.0082  83  PHE B CD1   
629  C  CD2   . PHE A 84  ? 0.3384 0.2850 0.2362 0.0033  -0.0868 0.0091  83  PHE B CD2   
630  C  CE1   . PHE A 84  ? 0.3357 0.2906 0.2443 0.0140  -0.0652 0.0073  83  PHE B CE1   
631  C  CE2   . PHE A 84  ? 0.3184 0.2612 0.2290 -0.0003 -0.0862 0.0088  83  PHE B CE2   
632  C  CZ    . PHE A 84  ? 0.3265 0.2726 0.2414 0.0056  -0.0757 0.0080  83  PHE B CZ    
633  N  N     . GLU A 85  ? 0.3153 0.2912 0.2184 0.0041  -0.0871 0.0289  84  GLU B N     
634  C  CA    . GLU A 85  ? 0.2906 0.2781 0.2139 0.0006  -0.0924 0.0359  84  GLU B CA    
635  C  C     . GLU A 85  ? 0.2729 0.2656 0.2172 -0.0054 -0.0934 0.0347  84  GLU B C     
636  O  O     . GLU A 85  ? 0.3046 0.2877 0.2450 -0.0084 -0.0939 0.0287  84  GLU B O     
637  C  CB    . GLU A 85  ? 0.3056 0.2951 0.2204 -0.0010 -0.1063 0.0375  84  GLU B CB    
638  C  CG    . GLU A 85  ? 0.3819 0.3627 0.2884 -0.0079 -0.1184 0.0294  84  GLU B CG    
639  C  CD    . GLU A 85  ? 0.4658 0.4271 0.3430 -0.0037 -0.1173 0.0195  84  GLU B CD    
640  O  OE1   . GLU A 85  ? 0.4118 0.3722 0.2731 0.0042  -0.1088 0.0202  84  GLU B OE1   
641  O  OE2   . GLU A 85  ? 0.4852 0.4321 0.3551 -0.0082 -0.1248 0.0112  84  GLU B OE2   
642  N  N     . ASP A 86  ? 0.2657 0.2736 0.2314 -0.0061 -0.0931 0.0409  85  ASP B N     
643  C  CA    . ASP A 86  ? 0.2241 0.2420 0.2097 -0.0123 -0.0940 0.0414  85  ASP B CA    
644  C  C     . ASP A 86  ? 0.2735 0.2927 0.2592 -0.0218 -0.1078 0.0404  85  ASP B C     
645  O  O     . ASP A 86  ? 0.2852 0.3144 0.2729 -0.0230 -0.1174 0.0435  85  ASP B O     
646  C  CB    . ASP A 86  ? 0.2460 0.2828 0.2533 -0.0087 -0.0900 0.0476  85  ASP B CB    
647  C  CG    . ASP A 86  ? 0.2175 0.2497 0.2249 -0.0015 -0.0781 0.0478  85  ASP B CG    
648  O  OD1   . ASP A 86  ? 0.2429 0.2675 0.2468 -0.0025 -0.0707 0.0439  85  ASP B OD1   
649  O  OD2   . ASP A 86  ? 0.2557 0.2915 0.2668 0.0051  -0.0775 0.0522  85  ASP B OD2   
650  N  N     . GLU A 87  ? 0.2735 0.2825 0.2576 -0.0292 -0.1095 0.0367  86  GLU B N     
651  C  CA    . GLU A 87  ? 0.2696 0.2723 0.2493 -0.0404 -0.1238 0.0348  86  GLU B CA    
652  C  C     . GLU A 87  ? 0.2802 0.3094 0.2855 -0.0498 -0.1298 0.0425  86  GLU B C     
653  O  O     . GLU A 87  ? 0.2852 0.3241 0.2926 -0.0552 -0.1420 0.0441  86  GLU B O     
654  C  CB    . GLU A 87  ? 0.3359 0.3145 0.3040 -0.0450 -0.1246 0.0291  86  GLU B CB    
655  C  CG    . GLU A 87  ? 0.3633 0.3261 0.3218 -0.0575 -0.1408 0.0257  86  GLU B CG    
656  C  CD    . GLU A 87  ? 0.3861 0.3163 0.3266 -0.0583 -0.1422 0.0188  86  GLU B CD    
657  O  OE1   . GLU A 87  ? 0.3444 0.2711 0.2850 -0.0498 -0.1303 0.0183  86  GLU B OE1   
658  O  OE2   . GLU A 87  ? 0.3994 0.3065 0.3236 -0.0660 -0.1562 0.0129  86  GLU B OE2   
659  N  N     . ASN A 88  ? 0.2657 0.3097 0.2905 -0.0513 -0.1210 0.0475  87  ASN B N     
660  C  CA    . ASN A 88  ? 0.2256 0.3021 0.2772 -0.0574 -0.1227 0.0556  87  ASN B CA    
661  C  C     . ASN A 88  ? 0.2108 0.2987 0.2759 -0.0531 -0.1086 0.0585  87  ASN B C     
662  O  O     . ASN A 88  ? 0.2480 0.3172 0.3019 -0.0490 -0.1003 0.0546  87  ASN B O     
663  C  CB    . ASN A 88  ? 0.2495 0.3279 0.3060 -0.0743 -0.1329 0.0575  87  ASN B CB    
664  C  CG    . ASN A 88  ? 0.2951 0.3535 0.3453 -0.0851 -0.1339 0.0574  87  ASN B CG    
665  O  OD1   . ASN A 88  ? 0.2589 0.3274 0.3206 -0.0858 -0.1251 0.0622  87  ASN B OD1   
666  N  ND2   . ASN A 88  ? 0.3047 0.3332 0.3352 -0.0933 -0.1447 0.0519  87  ASN B ND2   
667  N  N     . PHE A 89  ? 0.2069 0.3277 0.2957 -0.0532 -0.1060 0.0651  88  PHE B N     
668  C  CA    . PHE A 89  ? 0.2229 0.3594 0.3246 -0.0486 -0.0931 0.0677  88  PHE B CA    
669  C  C     . PHE A 89  ? 0.2071 0.3674 0.3261 -0.0619 -0.0936 0.0751  88  PHE B C     
670  O  O     . PHE A 89  ? 0.2175 0.4047 0.3522 -0.0572 -0.0844 0.0785  88  PHE B O     
671  C  CB    . PHE A 89  ? 0.1924 0.3454 0.3032 -0.0321 -0.0860 0.0674  88  PHE B CB    
672  C  CG    . PHE A 89  ? 0.2086 0.3359 0.3011 -0.0208 -0.0837 0.0617  88  PHE B CG    
673  C  CD1   . PHE A 89  ? 0.2100 0.3164 0.2897 -0.0168 -0.0746 0.0568  88  PHE B CD1   
674  C  CD2   . PHE A 89  ? 0.2610 0.3873 0.3494 -0.0149 -0.0910 0.0624  88  PHE B CD2   
675  C  CE1   . PHE A 89  ? 0.2285 0.3152 0.2934 -0.0087 -0.0722 0.0531  88  PHE B CE1   
676  C  CE2   . PHE A 89  ? 0.2634 0.3672 0.3345 -0.0061 -0.0883 0.0593  88  PHE B CE2   
677  C  CZ    . PHE A 89  ? 0.2556 0.3405 0.3157 -0.0038 -0.0787 0.0549  88  PHE B CZ    
678  N  N     . ILE A 90  ? 0.2057 0.3514 0.3176 -0.0773 -0.1026 0.0762  89  ILE B N     
679  C  CA    . ILE A 90  ? 0.2267 0.3888 0.3506 -0.0913 -0.1019 0.0838  89  ILE B CA    
680  C  C     . ILE A 90  ? 0.2254 0.3953 0.3540 -0.0921 -0.0909 0.0886  89  ILE B C     
681  O  O     . ILE A 90  ? 0.2140 0.4140 0.3578 -0.0928 -0.0828 0.0948  89  ILE B O     
682  C  CB    . ILE A 90  ? 0.2279 0.3637 0.3389 -0.1079 -0.1147 0.0838  89  ILE B CB    
683  C  CG1   . ILE A 90  ? 0.2330 0.3702 0.3422 -0.1082 -0.1253 0.0799  89  ILE B CG1   
684  C  CG2   . ILE A 90  ? 0.2603 0.4071 0.3805 -0.1245 -0.1139 0.0937  89  ILE B CG2   
685  C  CD1   . ILE A 90  ? 0.3114 0.4163 0.4022 -0.1203 -0.1385 0.0761  89  ILE B CD1   
686  N  N     . LEU A 91  ? 0.2449 0.3884 0.3595 -0.0921 -0.0912 0.0859  90  LEU B N     
687  C  CA    . LEU A 91  ? 0.2220 0.3671 0.3363 -0.0932 -0.0817 0.0901  90  LEU B CA    
688  C  C     . LEU A 91  ? 0.2269 0.3872 0.3448 -0.0748 -0.0679 0.0857  90  LEU B C     
689  O  O     . LEU A 91  ? 0.2092 0.3616 0.3218 -0.0610 -0.0664 0.0777  90  LEU B O     
690  C  CB    . LEU A 91  ? 0.2327 0.3348 0.3232 -0.0955 -0.0849 0.0864  90  LEU B CB    
691  C  CG    . LEU A 91  ? 0.2947 0.3756 0.3787 -0.1137 -0.0999 0.0897  90  LEU B CG    
692  C  CD1   . LEU A 91  ? 0.3073 0.3423 0.3659 -0.1132 -0.1041 0.0850  90  LEU B CD1   
693  C  CD2   . LEU A 91  ? 0.2998 0.4022 0.3971 -0.1288 -0.0989 0.1019  90  LEU B CD2   
694  N  N     . LYS A 92  ? 0.2279 0.4091 0.3535 -0.0754 -0.0582 0.0913  91  LYS B N     
695  C  CA    . LYS A 92  ? 0.2051 0.4017 0.3335 -0.0590 -0.0457 0.0867  91  LYS B CA    
696  C  C     . LYS A 92  ? 0.2104 0.3882 0.3229 -0.0550 -0.0389 0.0837  91  LYS B C     
697  O  O     . LYS A 92  ? 0.2143 0.3743 0.3168 -0.0650 -0.0422 0.0882  91  LYS B O     
698  C  CB    . LYS A 92  ? 0.1699 0.4111 0.3182 -0.0587 -0.0382 0.0936  91  LYS B CB    
699  C  CG    . LYS A 92  ? 0.2312 0.4895 0.3911 -0.0614 -0.0426 0.0959  91  LYS B CG    
700  C  CD    . LYS A 92  ? 0.2784 0.5309 0.4399 -0.0497 -0.0480 0.0886  91  LYS B CD    
701  C  CE    . LYS A 92  ? 0.2806 0.5574 0.4561 -0.0520 -0.0516 0.0920  91  LYS B CE    
702  N  NZ    . LYS A 92  ? 0.3322 0.6005 0.5071 -0.0433 -0.0598 0.0866  91  LYS B NZ    
703  N  N     . HIS A 93  ? 0.1905 0.3726 0.3006 -0.0399 -0.0302 0.0762  92  HIS B N     
704  C  CA    . HIS A 93  ? 0.1831 0.3528 0.2797 -0.0352 -0.0241 0.0725  92  HIS B CA    
705  C  C     . HIS A 93  ? 0.2272 0.4258 0.3299 -0.0376 -0.0160 0.0795  92  HIS B C     
706  O  O     . HIS A 93  ? 0.2296 0.4480 0.3360 -0.0265 -0.0077 0.0752  92  HIS B O     
707  C  CB    . HIS A 93  ? 0.1912 0.3505 0.2814 -0.0205 -0.0201 0.0611  92  HIS B CB    
708  C  CG    . HIS A 93  ? 0.2023 0.3380 0.2868 -0.0184 -0.0266 0.0559  92  HIS B CG    
709  N  ND1   . HIS A 93  ? 0.1980 0.3392 0.2907 -0.0157 -0.0305 0.0558  92  HIS B ND1   
710  C  CD2   . HIS A 93  ? 0.2186 0.3283 0.2898 -0.0177 -0.0293 0.0512  92  HIS B CD2   
711  C  CE1   . HIS A 93  ? 0.1948 0.3127 0.2775 -0.0142 -0.0352 0.0516  92  HIS B CE1   
712  N  NE2   . HIS A 93  ? 0.1936 0.2935 0.2639 -0.0153 -0.0340 0.0486  92  HIS B NE2   
713  N  N     . THR A 94  ? 0.2210 0.4208 0.3231 -0.0524 -0.0188 0.0908  93  THR B N     
714  C  CA    . THR A 94  ? 0.1937 0.4261 0.3032 -0.0581 -0.0113 0.1010  93  THR B CA    
715  C  C     . THR A 94  ? 0.1984 0.4297 0.2935 -0.0537 -0.0039 0.1011  93  THR B C     
716  O  O     . THR A 94  ? 0.2365 0.4989 0.3357 -0.0550 0.0047  0.1082  93  THR B O     
717  C  CB    . THR A 94  ? 0.1884 0.4236 0.3042 -0.0792 -0.0181 0.1156  93  THR B CB    
718  O  OG1   . THR A 94  ? 0.2416 0.4345 0.3403 -0.0857 -0.0272 0.1157  93  THR B OG1   
719  C  CG2   . THR A 94  ? 0.2654 0.5141 0.3978 -0.0834 -0.0242 0.1161  93  THR B CG2   
720  N  N     . GLY A 95  ? 0.2060 0.4059 0.2846 -0.0492 -0.0071 0.0948  94  GLY B N     
721  C  CA    . GLY A 95  ? 0.2063 0.4042 0.2703 -0.0466 -0.0027 0.0964  94  GLY B CA    
722  C  C     . GLY A 95  ? 0.2287 0.3911 0.2776 -0.0437 -0.0094 0.0911  94  GLY B C     
723  O  O     . GLY A 95  ? 0.2429 0.3831 0.2916 -0.0423 -0.0160 0.0851  94  GLY B O     
724  N  N     . PRO A 96  ? 0.1833 0.3432 0.2187 -0.0410 -0.0073 0.0929  95  PRO B N     
725  C  CA    . PRO A 96  ? 0.2349 0.3666 0.2572 -0.0366 -0.0134 0.0887  95  PRO B CA    
726  C  C     . PRO A 96  ? 0.2607 0.3642 0.2797 -0.0447 -0.0232 0.0949  95  PRO B C     
727  O  O     . PRO A 96  ? 0.2683 0.3710 0.2894 -0.0573 -0.0261 0.1069  95  PRO B O     
728  C  CB    . PRO A 96  ? 0.2412 0.3807 0.2504 -0.0349 -0.0103 0.0942  95  PRO B CB    
729  C  CG    . PRO A 96  ? 0.2329 0.4048 0.2467 -0.0348 -0.0008 0.0963  95  PRO B CG    
730  C  CD    . PRO A 96  ? 0.2087 0.3945 0.2401 -0.0421 0.0007  0.1003  95  PRO B CD    
731  N  N     . GLY A 97  ? 0.2408 0.3214 0.2541 -0.0374 -0.0285 0.0863  96  GLY B N     
732  C  CA    . GLY A 97  ? 0.2558 0.3060 0.2620 -0.0407 -0.0379 0.0886  96  GLY B CA    
733  C  C     . GLY A 97  ? 0.2514 0.2933 0.2647 -0.0431 -0.0419 0.0830  96  GLY B C     
734  O  O     . GLY A 97  ? 0.2589 0.2739 0.2638 -0.0422 -0.0496 0.0805  96  GLY B O     
735  N  N     . ILE A 98  ? 0.2195 0.2832 0.2462 -0.0440 -0.0371 0.0800  97  ILE B N     
736  C  CA    . ILE A 98  ? 0.2100 0.2680 0.2429 -0.0457 -0.0416 0.0753  97  ILE B CA    
737  C  C     . ILE A 98  ? 0.2544 0.2957 0.2796 -0.0349 -0.0428 0.0643  97  ILE B C     
738  O  O     . ILE A 98  ? 0.2189 0.2672 0.2434 -0.0258 -0.0372 0.0581  97  ILE B O     
739  C  CB    . ILE A 98  ? 0.2167 0.3039 0.2657 -0.0462 -0.0361 0.0751  97  ILE B CB    
740  C  CG1   . ILE A 98  ? 0.2647 0.3714 0.3234 -0.0593 -0.0360 0.0876  97  ILE B CG1   
741  C  CG2   . ILE A 98  ? 0.1866 0.2697 0.2401 -0.0420 -0.0392 0.0676  97  ILE B CG2   
742  C  CD1   . ILE A 98  ? 0.2923 0.3812 0.3500 -0.0736 -0.0472 0.0941  97  ILE B CD1   
743  N  N     . LEU A 99  ? 0.2258 0.2455 0.2445 -0.0364 -0.0505 0.0618  98  LEU B N     
744  C  CA    . LEU A 99  ? 0.2434 0.2500 0.2543 -0.0265 -0.0512 0.0523  98  LEU B CA    
745  C  C     . LEU A 99  ? 0.2549 0.2657 0.2709 -0.0273 -0.0525 0.0484  98  LEU B C     
746  O  O     . LEU A 99  ? 0.2290 0.2337 0.2454 -0.0354 -0.0597 0.0511  98  LEU B O     
747  C  CB    . LEU A 99  ? 0.2531 0.2307 0.2485 -0.0246 -0.0589 0.0512  98  LEU B CB    
748  C  CG    . LEU A 99  ? 0.2771 0.2434 0.2632 -0.0137 -0.0593 0.0415  98  LEU B CG    
749  C  CD1   . LEU A 99  ? 0.2425 0.2225 0.2308 -0.0031 -0.0515 0.0372  98  LEU B CD1   
750  C  CD2   . LEU A 99  ? 0.2802 0.2156 0.2503 -0.0123 -0.0683 0.0408  98  LEU B CD2   
751  N  N     . SER A 100 ? 0.2026 0.2220 0.2212 -0.0195 -0.0467 0.0425  99  SER B N     
752  C  CA    . SER A 100 ? 0.2070 0.2332 0.2312 -0.0196 -0.0472 0.0410  99  SER B CA    
753  C  C     . SER A 100 ? 0.2166 0.2375 0.2344 -0.0118 -0.0442 0.0346  99  SER B C     
754  O  O     . SER A 100 ? 0.2221 0.2420 0.2360 -0.0066 -0.0397 0.0312  99  SER B O     
755  C  CB    . SER A 100 ? 0.2215 0.2701 0.2601 -0.0203 -0.0422 0.0440  99  SER B CB    
756  O  OG    . SER A 100 ? 0.1888 0.2439 0.2332 -0.0179 -0.0429 0.0430  99  SER B OG    
757  N  N     . MET A 101 ? 0.1862 0.2054 0.2026 -0.0116 -0.0470 0.0338  100 MET B N     
758  C  CA    . MET A 101 ? 0.2106 0.2243 0.2185 -0.0058 -0.0442 0.0296  100 MET B CA    
759  C  C     . MET A 101 ? 0.1907 0.2143 0.2059 -0.0032 -0.0374 0.0296  100 MET B C     
760  O  O     . MET A 101 ? 0.1873 0.2181 0.2110 -0.0037 -0.0376 0.0321  100 MET B O     
761  C  CB    . MET A 101 ? 0.2116 0.2179 0.2116 -0.0068 -0.0507 0.0294  100 MET B CB    
762  C  CG    . MET A 101 ? 0.2120 0.2017 0.1967 -0.0063 -0.0567 0.0256  100 MET B CG    
763  S  SD    . MET A 101 ? 0.2774 0.2567 0.2505 0.0012  -0.0534 0.0202  100 MET B SD    
764  C  CE    . MET A 101 ? 0.2883 0.2675 0.2477 0.0085  -0.0499 0.0160  100 MET B CE    
765  N  N     . ALA A 102 ? 0.1566 0.1800 0.1683 -0.0003 -0.0322 0.0268  101 ALA B N     
766  C  CA    . ALA A 102 ? 0.1737 0.2005 0.1894 0.0000  -0.0277 0.0270  101 ALA B CA    
767  C  C     . ALA A 102 ? 0.2046 0.2251 0.2135 0.0005  -0.0293 0.0295  101 ALA B C     
768  O  O     . ALA A 102 ? 0.1999 0.2154 0.1990 0.0013  -0.0326 0.0294  101 ALA B O     
769  C  CB    . ALA A 102 ? 0.1796 0.2110 0.1956 0.0000  -0.0223 0.0241  101 ALA B CB    
770  N  N     . ASN A 103 ? 0.2004 0.2192 0.2124 0.0005  -0.0276 0.0316  102 ASN B N     
771  C  CA    . ASN A 103 ? 0.1968 0.2085 0.2006 0.0010  -0.0293 0.0358  102 ASN B CA    
772  C  C     . ASN A 103 ? 0.2583 0.2633 0.2638 0.0002  -0.0264 0.0383  102 ASN B C     
773  O  O     . ASN A 103 ? 0.2376 0.2426 0.2504 -0.0001 -0.0242 0.0354  102 ASN B O     
774  C  CB    . ASN A 103 ? 0.2093 0.2209 0.2132 0.0031  -0.0367 0.0384  102 ASN B CB    
775  C  CG    . ASN A 103 ? 0.2330 0.2502 0.2496 0.0058  -0.0383 0.0394  102 ASN B CG    
776  O  OD1   . ASN A 103 ? 0.2404 0.2531 0.2599 0.0090  -0.0361 0.0404  102 ASN B OD1   
777  N  ND2   . ASN A 103 ? 0.2016 0.2285 0.2253 0.0049  -0.0427 0.0395  102 ASN B ND2   
778  N  N     . ALA A 104 ? 0.2677 0.2644 0.2644 0.0001  -0.0276 0.0439  103 ALA B N     
779  C  CA    . ALA A 104 ? 0.2966 0.2809 0.2921 -0.0013 -0.0266 0.0480  103 ALA B CA    
780  C  C     . ALA A 104 ? 0.3157 0.2918 0.3086 0.0049  -0.0327 0.0532  103 ALA B C     
781  O  O     . ALA A 104 ? 0.3430 0.3060 0.3269 0.0044  -0.0338 0.0602  103 ALA B O     
782  C  CB    . ALA A 104 ? 0.3105 0.2922 0.2969 -0.0084 -0.0219 0.0526  103 ALA B CB    
783  N  N     . GLY A 105 ? 0.3041 0.2894 0.3049 0.0105  -0.0372 0.0509  104 GLY B N     
784  C  CA    . GLY A 105 ? 0.2916 0.2754 0.2929 0.0175  -0.0440 0.0557  104 GLY B CA    
785  C  C     . GLY A 105 ? 0.2659 0.2611 0.2649 0.0170  -0.0499 0.0564  104 GLY B C     
786  O  O     . GLY A 105 ? 0.2569 0.2573 0.2527 0.0119  -0.0485 0.0525  104 GLY B O     
787  N  N     . PRO A 106 ? 0.2936 0.2924 0.2943 0.0227  -0.0575 0.0609  105 PRO B N     
788  C  CA    . PRO A 106 ? 0.2892 0.2985 0.2873 0.0208  -0.0656 0.0614  105 PRO B CA    
789  C  C     . PRO A 106 ? 0.2652 0.2671 0.2443 0.0155  -0.0654 0.0607  105 PRO B C     
790  O  O     . PRO A 106 ? 0.2689 0.2597 0.2337 0.0157  -0.0624 0.0651  105 PRO B O     
791  C  CB    . PRO A 106 ? 0.2955 0.3071 0.2947 0.0287  -0.0739 0.0683  105 PRO B CB    
792  C  CG    . PRO A 106 ? 0.3280 0.3356 0.3381 0.0371  -0.0700 0.0690  105 PRO B CG    
793  C  CD    . PRO A 106 ? 0.2996 0.2923 0.3046 0.0320  -0.0601 0.0653  105 PRO B CD    
794  N  N     . ASN A 107 ? 0.2332 0.2411 0.2112 0.0111  -0.0693 0.0556  106 ASN B N     
795  C  CA    . ASN A 107 ? 0.2659 0.2670 0.2238 0.0087  -0.0713 0.0529  106 ASN B CA    
796  C  C     . ASN A 107 ? 0.2998 0.2939 0.2469 0.0084  -0.0609 0.0516  106 ASN B C     
797  O  O     . ASN A 107 ? 0.2962 0.2857 0.2252 0.0095  -0.0598 0.0541  106 ASN B O     
798  C  CB    . ASN A 107 ? 0.2578 0.2574 0.2024 0.0114  -0.0803 0.0581  106 ASN B CB    
799  C  CG    . ASN A 107 ? 0.2958 0.3074 0.2532 0.0114  -0.0916 0.0596  106 ASN B CG    
800  O  OD1   . ASN A 107 ? 0.2685 0.2864 0.2340 0.0056  -0.0961 0.0545  106 ASN B OD1   
801  N  ND2   . ASN A 107 ? 0.2881 0.3036 0.2475 0.0174  -0.0972 0.0673  106 ASN B ND2   
802  N  N     . THR A 108 ? 0.2457 0.2420 0.2040 0.0067  -0.0532 0.0481  107 THR B N     
803  C  CA    . THR A 108 ? 0.2614 0.2566 0.2131 0.0057  -0.0437 0.0469  107 THR B CA    
804  C  C     . THR A 108 ? 0.2573 0.2563 0.2144 0.0051  -0.0406 0.0395  107 THR B C     
805  O  O     . THR A 108 ? 0.2710 0.2744 0.2342 0.0040  -0.0330 0.0383  107 THR B O     
806  C  CB    . THR A 108 ? 0.2897 0.2824 0.2478 0.0039  -0.0376 0.0524  107 THR B CB    
807  O  OG1   . THR A 108 ? 0.2497 0.2442 0.2250 0.0040  -0.0375 0.0501  107 THR B OG1   
808  C  CG2   . THR A 108 ? 0.2594 0.2438 0.2087 0.0053  -0.0412 0.0614  107 THR B CG2   
809  N  N     . ASN A 109 ? 0.2383 0.2348 0.1923 0.0055  -0.0472 0.0348  108 ASN B N     
810  C  CA    . ASN A 109 ? 0.2805 0.2762 0.2360 0.0060  -0.0456 0.0286  108 ASN B CA    
811  C  C     . ASN A 109 ? 0.2687 0.2637 0.2095 0.0111  -0.0404 0.0246  108 ASN B C     
812  O  O     . ASN A 109 ? 0.2869 0.2777 0.2107 0.0140  -0.0425 0.0234  108 ASN B O     
813  C  CB    . ASN A 109 ? 0.2646 0.2533 0.2192 0.0035  -0.0556 0.0257  108 ASN B CB    
814  C  CG    . ASN A 109 ? 0.2704 0.2666 0.2417 -0.0013 -0.0597 0.0303  108 ASN B CG    
815  O  OD1   . ASN A 109 ? 0.2315 0.2347 0.2172 -0.0028 -0.0556 0.0314  108 ASN B OD1   
816  N  ND2   . ASN A 109 ? 0.2297 0.2275 0.1996 -0.0029 -0.0678 0.0332  108 ASN B ND2   
817  N  N     . GLY A 110 ? 0.2598 0.2606 0.2066 0.0131  -0.0340 0.0217  109 GLY B N     
818  C  CA    . GLY A 110 ? 0.2578 0.2632 0.1936 0.0199  -0.0283 0.0176  109 GLY B CA    
819  C  C     . GLY A 110 ? 0.2658 0.2664 0.2023 0.0251  -0.0302 0.0113  109 GLY B C     
820  O  O     . GLY A 110 ? 0.2950 0.2796 0.2216 0.0272  -0.0383 0.0068  109 GLY B O     
821  N  N     . SER A 111 ? 0.2499 0.2632 0.1973 0.0267  -0.0239 0.0113  110 SER B N     
822  C  CA    . SER A 111 ? 0.2133 0.2218 0.1627 0.0318  -0.0264 0.0073  110 SER B CA    
823  C  C     . SER A 111 ? 0.2382 0.2539 0.2051 0.0260  -0.0255 0.0108  110 SER B C     
824  O  O     . SER A 111 ? 0.2396 0.2485 0.2076 0.0283  -0.0293 0.0096  110 SER B O     
825  C  CB    . SER A 111 ? 0.2709 0.2899 0.2144 0.0434  -0.0208 0.0025  110 SER B CB    
826  O  OG    . SER A 111 ? 0.2352 0.2792 0.1901 0.0403  -0.0115 0.0064  110 SER B OG    
827  N  N     . GLN A 112 ? 0.2174 0.2449 0.1957 0.0191  -0.0209 0.0150  111 GLN B N     
828  C  CA    . GLN A 112 ? 0.2189 0.2525 0.2108 0.0148  -0.0205 0.0166  111 GLN B CA    
829  C  C     . GLN A 112 ? 0.2246 0.2476 0.2187 0.0113  -0.0265 0.0183  111 GLN B C     
830  O  O     . GLN A 112 ? 0.2027 0.2177 0.1937 0.0084  -0.0305 0.0200  111 GLN B O     
831  C  CB    . GLN A 112 ? 0.2043 0.2470 0.2052 0.0081  -0.0159 0.0193  111 GLN B CB    
832  C  CG    . GLN A 112 ? 0.2179 0.2764 0.2208 0.0083  -0.0097 0.0191  111 GLN B CG    
833  C  CD    . GLN A 112 ? 0.2169 0.2808 0.2287 -0.0007 -0.0068 0.0217  111 GLN B CD    
834  O  OE1   . GLN A 112 ? 0.2030 0.2646 0.2219 -0.0040 -0.0088 0.0205  111 GLN B OE1   
835  N  NE2   . GLN A 112 ? 0.1966 0.2675 0.2070 -0.0051 -0.0021 0.0254  111 GLN B NE2   
836  N  N     . PHE A 113 ? 0.2185 0.2445 0.2185 0.0110  -0.0271 0.0187  112 PHE B N     
837  C  CA    . PHE A 113 ? 0.2018 0.2219 0.2041 0.0072  -0.0316 0.0217  112 PHE B CA    
838  C  C     . PHE A 113 ? 0.2347 0.2662 0.2457 0.0055  -0.0286 0.0229  112 PHE B C     
839  O  O     . PHE A 113 ? 0.2003 0.2414 0.2139 0.0078  -0.0251 0.0205  112 PHE B O     
840  C  CB    . PHE A 113 ? 0.2187 0.2235 0.2106 0.0103  -0.0375 0.0211  112 PHE B CB    
841  C  CG    . PHE A 113 ? 0.1978 0.2054 0.1876 0.0178  -0.0361 0.0193  112 PHE B CG    
842  C  CD1   . PHE A 113 ? 0.2117 0.2236 0.2059 0.0165  -0.0365 0.0228  112 PHE B CD1   
843  C  CD2   . PHE A 113 ? 0.2175 0.2279 0.2017 0.0267  -0.0336 0.0147  112 PHE B CD2   
844  C  CE1   . PHE A 113 ? 0.2064 0.2230 0.1993 0.0237  -0.0361 0.0219  112 PHE B CE1   
845  C  CE2   . PHE A 113 ? 0.2397 0.2577 0.2246 0.0348  -0.0325 0.0134  112 PHE B CE2   
846  C  CZ    . PHE A 113 ? 0.2256 0.2461 0.2150 0.0332  -0.0343 0.0171  112 PHE B CZ    
847  N  N     . PHE A 114 ? 0.2097 0.2427 0.2252 0.0011  -0.0302 0.0266  113 PHE B N     
848  C  CA    . PHE A 114 ? 0.1808 0.2247 0.2008 0.0007  -0.0274 0.0273  113 PHE B CA    
849  C  C     . PHE A 114 ? 0.2115 0.2532 0.2301 -0.0027 -0.0305 0.0333  113 PHE B C     
850  O  O     . PHE A 114 ? 0.1941 0.2287 0.2123 -0.0073 -0.0345 0.0371  113 PHE B O     
851  C  CB    . PHE A 114 ? 0.1615 0.2151 0.1889 -0.0005 -0.0232 0.0251  113 PHE B CB    
852  C  CG    . PHE A 114 ? 0.1646 0.2202 0.1973 -0.0028 -0.0239 0.0281  113 PHE B CG    
853  C  CD1   . PHE A 114 ? 0.1734 0.2221 0.2059 -0.0031 -0.0264 0.0287  113 PHE B CD1   
854  C  CD2   . PHE A 114 ? 0.1659 0.2331 0.2038 -0.0039 -0.0221 0.0308  113 PHE B CD2   
855  C  CE1   . PHE A 114 ? 0.1848 0.2387 0.2238 -0.0044 -0.0283 0.0318  113 PHE B CE1   
856  C  CE2   . PHE A 114 ? 0.1775 0.2526 0.2232 -0.0050 -0.0224 0.0339  113 PHE B CE2   
857  C  CZ    . PHE A 114 ? 0.1695 0.2386 0.2169 -0.0051 -0.0261 0.0345  113 PHE B CZ    
858  N  N     . ILE A 115 ? 0.1831 0.2321 0.2007 -0.0016 -0.0290 0.0348  114 ILE B N     
859  C  CA    . ILE A 115 ? 0.2071 0.2556 0.2220 -0.0057 -0.0310 0.0425  114 ILE B CA    
860  C  C     . ILE A 115 ? 0.1795 0.2469 0.1996 -0.0071 -0.0256 0.0430  114 ILE B C     
861  O  O     . ILE A 115 ? 0.1902 0.2661 0.2097 -0.0028 -0.0226 0.0376  114 ILE B O     
862  C  CB    . ILE A 115 ? 0.2414 0.2809 0.2468 -0.0015 -0.0346 0.0449  114 ILE B CB    
863  C  CG1   . ILE A 115 ? 0.2822 0.3045 0.2812 0.0044  -0.0389 0.0411  114 ILE B CG1   
864  C  CG2   . ILE A 115 ? 0.2297 0.2664 0.2309 -0.0079 -0.0369 0.0555  114 ILE B CG2   
865  C  CD1   . ILE A 115 ? 0.2314 0.2488 0.2227 0.0135  -0.0418 0.0412  114 ILE B CD1   
866  N  N     . CYS A 116 ? 0.1986 0.2745 0.2244 -0.0126 -0.0242 0.0484  115 CYS B N     
867  C  CA    . CYS A 116 ? 0.2017 0.2982 0.2313 -0.0116 -0.0180 0.0483  115 CYS B CA    
868  C  C     . CYS A 116 ? 0.2015 0.3042 0.2226 -0.0119 -0.0168 0.0531  115 CYS B C     
869  O  O     . CYS A 116 ? 0.2036 0.2973 0.2188 -0.0165 -0.0208 0.0618  115 CYS B O     
870  C  CB    . CYS A 116 ? 0.1832 0.2935 0.2226 -0.0169 -0.0163 0.0545  115 CYS B CB    
871  S  SG    . CYS A 116 ? 0.2234 0.3281 0.2720 -0.0153 -0.0189 0.0495  115 CYS B SG    
872  N  N     . THR A 117 ? 0.1968 0.3136 0.2155 -0.0068 -0.0118 0.0475  116 THR B N     
873  C  CA    . THR A 117 ? 0.2015 0.3291 0.2109 -0.0068 -0.0099 0.0524  116 THR B CA    
874  C  C     . THR A 117 ? 0.2047 0.3555 0.2166 -0.0067 -0.0023 0.0541  116 THR B C     
875  O  O     . THR A 117 ? 0.2327 0.3968 0.2352 -0.0057 0.0010  0.0573  116 THR B O     
876  C  CB    . THR A 117 ? 0.2196 0.3462 0.2207 -0.0007 -0.0115 0.0441  116 THR B CB    
877  O  OG1   . THR A 117 ? 0.2256 0.3561 0.2302 0.0037  -0.0086 0.0319  116 THR B OG1   
878  C  CG2   . THR A 117 ? 0.1891 0.2989 0.1895 0.0004  -0.0180 0.0439  116 THR B CG2   
879  N  N     . ALA A 118 ? 0.1887 0.3464 0.2126 -0.0069 0.0004  0.0529  117 ALA B N     
880  C  CA    . ALA A 118 ? 0.2003 0.3836 0.2302 -0.0045 0.0080  0.0540  117 ALA B CA    
881  C  C     . ALA A 118 ? 0.1962 0.3828 0.2418 -0.0075 0.0068  0.0569  117 ALA B C     
882  O  O     . ALA A 118 ? 0.2279 0.3950 0.2768 -0.0094 0.0006  0.0547  117 ALA B O     
883  C  CB    . ALA A 118 ? 0.2406 0.4305 0.2658 0.0074  0.0128  0.0402  117 ALA B CB    
884  N  N     . LYS A 119 ? 0.2151 0.4296 0.2703 -0.0072 0.0130  0.0616  118 LYS B N     
885  C  CA    . LYS A 119 ? 0.1906 0.4134 0.2624 -0.0077 0.0115  0.0629  118 LYS B CA    
886  C  C     . LYS A 119 ? 0.2208 0.4327 0.2933 0.0052  0.0113  0.0493  118 LYS B C     
887  O  O     . LYS A 119 ? 0.2277 0.4437 0.2937 0.0165  0.0165  0.0398  118 LYS B O     
888  C  CB    . LYS A 119 ? 0.1975 0.4593 0.2813 -0.0088 0.0190  0.0710  118 LYS B CB    
889  C  CG    . LYS A 119 ? 0.2296 0.5097 0.3333 -0.0076 0.0180  0.0728  118 LYS B CG    
890  C  CD    . LYS A 119 ? 0.2550 0.5802 0.3714 -0.0108 0.0263  0.0832  118 LYS B CD    
891  C  CE    . LYS A 119 ? 0.3076 0.6491 0.4410 -0.0078 0.0243  0.0837  118 LYS B CE    
892  N  NZ    . LYS A 119 ? 0.3486 0.7221 0.4866 -0.0083 0.0312  0.0899  118 LYS B NZ    
893  N  N     . THR A 120 ? 0.1879 0.3839 0.2664 0.0035  0.0047  0.0484  119 THR B N     
894  C  CA    . THR A 120 ? 0.1995 0.3819 0.2778 0.0139  0.0035  0.0383  119 THR B CA    
895  C  C     . THR A 120 ? 0.2048 0.3979 0.2982 0.0149  0.0004  0.0423  119 THR B C     
896  O  O     . THR A 120 ? 0.2299 0.4060 0.3240 0.0116  -0.0066 0.0429  119 THR B O     
897  C  CB    . THR A 120 ? 0.2092 0.3606 0.2771 0.0111  -0.0020 0.0336  119 THR B CB    
898  O  OG1   . THR A 120 ? 0.1985 0.3404 0.2684 0.0014  -0.0084 0.0406  119 THR B OG1   
899  C  CG2   . THR A 120 ? 0.2340 0.3785 0.2886 0.0102  -0.0002 0.0298  119 THR B CG2   
900  N  N     . GLU A 121 ? 0.1962 0.4202 0.3009 0.0209  0.0059  0.0445  120 GLU B N     
901  C  CA    . GLU A 121 ? 0.2148 0.4593 0.3372 0.0209  0.0028  0.0506  120 GLU B CA    
902  C  C     . GLU A 121 ? 0.2322 0.4606 0.3555 0.0320  -0.0018 0.0442  120 GLU B C     
903  O  O     . GLU A 121 ? 0.1743 0.4080 0.3079 0.0290  -0.0084 0.0493  120 GLU B O     
904  C  CB    . GLU A 121 ? 0.2173 0.5044 0.3523 0.0262  0.0115  0.0545  120 GLU B CB    
905  C  CG    . GLU A 121 ? 0.2707 0.5624 0.4009 0.0472  0.0189  0.0427  120 GLU B CG    
906  C  CD    . GLU A 121 ? 0.3578 0.6400 0.4691 0.0499  0.0253  0.0355  120 GLU B CD    
907  O  OE1   . GLU A 121 ? 0.3260 0.5974 0.4281 0.0364  0.0239  0.0403  120 GLU B OE1   
908  O  OE2   . GLU A 121 ? 0.4563 0.7420 0.5610 0.0670  0.0313  0.0245  120 GLU B OE2   
909  N  N     . TRP A 122 ? 0.1940 0.4013 0.3052 0.0437  0.0006  0.0335  121 TRP B N     
910  C  CA    . TRP A 122 ? 0.2314 0.4214 0.3421 0.0542  -0.0038 0.0290  121 TRP B CA    
911  C  C     . TRP A 122 ? 0.2706 0.4335 0.3749 0.0446  -0.0120 0.0317  121 TRP B C     
912  O  O     . TRP A 122 ? 0.2643 0.4143 0.3682 0.0508  -0.0167 0.0312  121 TRP B O     
913  C  CB    . TRP A 122 ? 0.2751 0.4464 0.3734 0.0676  0.0000  0.0172  121 TRP B CB    
914  C  CG    . TRP A 122 ? 0.3024 0.4476 0.3848 0.0593  -0.0002 0.0122  121 TRP B CG    
915  C  CD1   . TRP A 122 ? 0.2765 0.3899 0.3491 0.0556  -0.0050 0.0093  121 TRP B CD1   
916  C  CD2   . TRP A 122 ? 0.2759 0.4281 0.3514 0.0538  0.0044  0.0104  121 TRP B CD2   
917  N  NE1   . TRP A 122 ? 0.3085 0.4117 0.3708 0.0480  -0.0037 0.0054  121 TRP B NE1   
918  C  CE2   . TRP A 122 ? 0.2928 0.4177 0.3557 0.0473  0.0014  0.0058  121 TRP B CE2   
919  C  CE3   . TRP A 122 ? 0.2816 0.4621 0.3598 0.0536  0.0108  0.0130  121 TRP B CE3   
920  C  CZ2   . TRP A 122 ? 0.3039 0.4291 0.3577 0.0419  0.0035  0.0031  121 TRP B CZ2   
921  C  CZ3   . TRP A 122 ? 0.2984 0.4764 0.3649 0.0479  0.0132  0.0110  121 TRP B CZ3   
922  C  CH2   . TRP A 122 ? 0.3105 0.4609 0.3652 0.0426  0.0090  0.0058  121 TRP B CH2   
923  N  N     . LEU A 123 ? 0.2001 0.3542 0.2982 0.0309  -0.0136 0.0347  122 LEU B N     
924  C  CA    . LEU A 123 ? 0.2302 0.3631 0.3219 0.0225  -0.0207 0.0371  122 LEU B CA    
925  C  C     . LEU A 123 ? 0.1943 0.3394 0.2953 0.0149  -0.0275 0.0450  122 LEU B C     
926  O  O     . LEU A 123 ? 0.1947 0.3233 0.2893 0.0106  -0.0341 0.0461  122 LEU B O     
927  C  CB    . LEU A 123 ? 0.2150 0.3330 0.2953 0.0141  -0.0196 0.0355  122 LEU B CB    
928  C  CG    . LEU A 123 ? 0.2266 0.3324 0.2978 0.0200  -0.0148 0.0272  122 LEU B CG    
929  C  CD1   . LEU A 123 ? 0.1947 0.2912 0.2569 0.0123  -0.0146 0.0265  122 LEU B CD1   
930  C  CD2   . LEU A 123 ? 0.2540 0.3388 0.3195 0.0255  -0.0166 0.0229  122 LEU B CD2   
931  N  N     . ASP A 124 ? 0.2058 0.3809 0.3216 0.0132  -0.0264 0.0504  123 ASP B N     
932  C  CA    . ASP A 124 ? 0.1850 0.3734 0.3111 0.0037  -0.0345 0.0580  123 ASP B CA    
933  C  C     . ASP A 124 ? 0.2163 0.4000 0.3440 0.0110  -0.0415 0.0576  123 ASP B C     
934  O  O     . ASP A 124 ? 0.2210 0.4089 0.3522 0.0257  -0.0389 0.0546  123 ASP B O     
935  C  CB    . ASP A 124 ? 0.1736 0.4020 0.3189 0.0008  -0.0314 0.0650  123 ASP B CB    
936  C  CG    . ASP A 124 ? 0.2074 0.4416 0.3498 -0.0089 -0.0255 0.0685  123 ASP B CG    
937  O  OD1   . ASP A 124 ? 0.2077 0.4140 0.3344 -0.0143 -0.0263 0.0661  123 ASP B OD1   
938  O  OD2   . ASP A 124 ? 0.1929 0.4604 0.3486 -0.0111 -0.0203 0.0745  123 ASP B OD2   
939  N  N     . GLY A 125 ? 0.1870 0.3616 0.3112 0.0013  -0.0513 0.0608  124 GLY B N     
940  C  CA    . GLY A 125 ? 0.2116 0.3802 0.3338 0.0071  -0.0591 0.0611  124 GLY B CA    
941  C  C     . GLY A 125 ? 0.2312 0.3677 0.3347 0.0138  -0.0578 0.0562  124 GLY B C     
942  O  O     . GLY A 125 ? 0.2536 0.3817 0.3515 0.0179  -0.0643 0.0576  124 GLY B O     
943  N  N     . LYS A 126 ? 0.2282 0.3483 0.3219 0.0140  -0.0503 0.0514  125 LYS B N     
944  C  CA    . LYS A 126 ? 0.1983 0.2912 0.2761 0.0177  -0.0489 0.0478  125 LYS B CA    
945  C  C     . LYS A 126 ? 0.2304 0.3062 0.2947 0.0088  -0.0483 0.0455  125 LYS B C     
946  O  O     . LYS A 126 ? 0.2339 0.2922 0.2853 0.0091  -0.0493 0.0446  125 LYS B O     
947  C  CB    . LYS A 126 ? 0.2488 0.3366 0.3266 0.0275  -0.0413 0.0432  125 LYS B CB    
948  C  CG    . LYS A 126 ? 0.3311 0.4254 0.4163 0.0413  -0.0432 0.0446  125 LYS B CG    
949  C  CD    . LYS A 126 ? 0.3932 0.5003 0.4867 0.0512  -0.0362 0.0399  125 LYS B CD    
950  C  CE    . LYS A 126 ? 0.4294 0.5165 0.5112 0.0502  -0.0298 0.0326  125 LYS B CE    
951  N  NZ    . LYS A 126 ? 0.5089 0.5651 0.5781 0.0549  -0.0312 0.0303  125 LYS B NZ    
952  N  N     . HIS A 127 ? 0.1531 0.2345 0.2198 0.0017  -0.0467 0.0452  126 HIS B N     
953  C  CA    . HIS A 127 ? 0.1677 0.2334 0.2221 -0.0044 -0.0469 0.0428  126 HIS B CA    
954  C  C     . HIS A 127 ? 0.1776 0.2465 0.2336 -0.0137 -0.0538 0.0461  126 HIS B C     
955  O  O     . HIS A 127 ? 0.1863 0.2739 0.2556 -0.0177 -0.0541 0.0504  126 HIS B O     
956  C  CB    . HIS A 127 ? 0.1687 0.2337 0.2222 -0.0034 -0.0392 0.0396  126 HIS B CB    
957  C  CG    . HIS A 127 ? 0.1997 0.2584 0.2506 0.0034  -0.0337 0.0357  126 HIS B CG    
958  N  ND1   . HIS A 127 ? 0.1701 0.2146 0.2106 0.0031  -0.0320 0.0330  126 HIS B ND1   
959  C  CD2   . HIS A 127 ? 0.1949 0.2582 0.2515 0.0105  -0.0308 0.0343  126 HIS B CD2   
960  C  CE1   . HIS A 127 ? 0.1774 0.2168 0.2176 0.0070  -0.0287 0.0309  126 HIS B CE1   
961  N  NE2   . HIS A 127 ? 0.1935 0.2413 0.2422 0.0123  -0.0282 0.0310  126 HIS B NE2   
962  N  N     . VAL A 128 ? 0.2039 0.2547 0.2458 -0.0172 -0.0592 0.0439  127 VAL B N     
963  C  CA    . VAL A 128 ? 0.2063 0.2524 0.2459 -0.0271 -0.0682 0.0458  127 VAL B CA    
964  C  C     . VAL A 128 ? 0.1777 0.2172 0.2151 -0.0314 -0.0656 0.0463  127 VAL B C     
965  O  O     . VAL A 128 ? 0.2075 0.2315 0.2329 -0.0269 -0.0625 0.0419  127 VAL B O     
966  C  CB    . VAL A 128 ? 0.2165 0.2427 0.2382 -0.0272 -0.0758 0.0415  127 VAL B CB    
967  C  CG1   . VAL A 128 ? 0.2618 0.2768 0.2781 -0.0380 -0.0866 0.0418  127 VAL B CG1   
968  C  CG2   . VAL A 128 ? 0.2096 0.2418 0.2309 -0.0231 -0.0793 0.0424  127 VAL B CG2   
969  N  N     . VAL A 129 ? 0.1788 0.2318 0.2279 -0.0402 -0.0671 0.0528  128 VAL B N     
970  C  CA    . VAL A 129 ? 0.2142 0.2593 0.2599 -0.0466 -0.0667 0.0560  128 VAL B CA    
971  C  C     . VAL A 129 ? 0.2406 0.2603 0.2732 -0.0549 -0.0780 0.0554  128 VAL B C     
972  O  O     . VAL A 129 ? 0.2521 0.2743 0.2884 -0.0638 -0.0871 0.0575  128 VAL B O     
973  C  CB    . VAL A 129 ? 0.1969 0.2687 0.2596 -0.0539 -0.0633 0.0648  128 VAL B CB    
974  C  CG1   . VAL A 129 ? 0.2046 0.2668 0.2619 -0.0627 -0.0640 0.0709  128 VAL B CG1   
975  C  CG2   . VAL A 129 ? 0.2051 0.2992 0.2775 -0.0432 -0.0523 0.0631  128 VAL B CG2   
976  N  N     . PHE A 130 ? 0.2683 0.2635 0.2855 -0.0518 -0.0784 0.0523  129 PHE B N     
977  C  CA    . PHE A 130 ? 0.2835 0.2479 0.2840 -0.0564 -0.0896 0.0493  129 PHE B CA    
978  C  C     . PHE A 130 ? 0.2984 0.2415 0.2892 -0.0586 -0.0914 0.0525  129 PHE B C     
979  O  O     . PHE A 130 ? 0.3203 0.2316 0.2942 -0.0603 -0.1011 0.0491  129 PHE B O     
980  C  CB    . PHE A 130 ? 0.2931 0.2417 0.2772 -0.0443 -0.0904 0.0385  129 PHE B CB    
981  C  CG    . PHE A 130 ? 0.2730 0.2199 0.2510 -0.0303 -0.0807 0.0337  129 PHE B CG    
982  C  CD1   . PHE A 130 ? 0.2427 0.2120 0.2311 -0.0236 -0.0702 0.0335  129 PHE B CD1   
983  C  CD2   . PHE A 130 ? 0.2832 0.2065 0.2458 -0.0239 -0.0830 0.0298  129 PHE B CD2   
984  C  CE1   . PHE A 130 ? 0.2285 0.1991 0.2133 -0.0132 -0.0623 0.0297  129 PHE B CE1   
985  C  CE2   . PHE A 130 ? 0.3128 0.2401 0.2726 -0.0110 -0.0745 0.0261  129 PHE B CE2   
986  C  CZ    . PHE A 130 ? 0.2525 0.2052 0.2243 -0.0068 -0.0642 0.0262  129 PHE B CZ    
987  N  N     . GLY A 131 ? 0.2954 0.2526 0.2943 -0.0582 -0.0835 0.0589  130 GLY B N     
988  C  CA    . GLY A 131 ? 0.3306 0.2650 0.3178 -0.0591 -0.0866 0.0629  130 GLY B CA    
989  C  C     . GLY A 131 ? 0.2997 0.2558 0.2969 -0.0614 -0.0783 0.0720  130 GLY B C     
990  O  O     . GLY A 131 ? 0.3007 0.2883 0.3129 -0.0605 -0.0698 0.0732  130 GLY B O     
991  N  N     . LYS A 132 ? 0.3198 0.2574 0.3064 -0.0622 -0.0808 0.0777  131 LYS B N     
992  C  CA    . LYS A 132 ? 0.3016 0.2600 0.2937 -0.0612 -0.0723 0.0851  131 LYS B CA    
993  C  C     . LYS A 132 ? 0.3530 0.2870 0.3289 -0.0537 -0.0752 0.0871  131 LYS B C     
994  O  O     . LYS A 132 ? 0.3850 0.2836 0.3461 -0.0539 -0.0851 0.0867  131 LYS B O     
995  C  CB    . LYS A 132 ? 0.3790 0.3573 0.3823 -0.0778 -0.0708 0.0990  131 LYS B CB    
996  C  CG    . LYS A 132 ? 0.4407 0.3951 0.4382 -0.0947 -0.0820 0.1085  131 LYS B CG    
997  C  CD    . LYS A 132 ? 0.5033 0.4745 0.5062 -0.1087 -0.0785 0.1252  131 LYS B CD    
998  C  CE    . LYS A 132 ? 0.6592 0.6238 0.6668 -0.1326 -0.0879 0.1372  131 LYS B CE    
999  N  NZ    . LYS A 132 ? 0.6503 0.5664 0.6384 -0.1375 -0.1014 0.1373  131 LYS B NZ    
1000 N  N     . VAL A 133 ? 0.3321 0.2844 0.3096 -0.0468 -0.0675 0.0892  132 VAL B N     
1001 C  CA    . VAL A 133 ? 0.3680 0.3011 0.3309 -0.0391 -0.0708 0.0930  132 VAL B CA    
1002 C  C     . VAL A 133 ? 0.4122 0.3224 0.3660 -0.0528 -0.0786 0.1074  132 VAL B C     
1003 O  O     . VAL A 133 ? 0.3854 0.3124 0.3476 -0.0685 -0.0761 0.1185  132 VAL B O     
1004 C  CB    . VAL A 133 ? 0.3245 0.2847 0.2908 -0.0309 -0.0620 0.0931  132 VAL B CB    
1005 C  CG1   . VAL A 133 ? 0.3648 0.3103 0.3166 -0.0257 -0.0661 0.1014  132 VAL B CG1   
1006 C  CG2   . VAL A 133 ? 0.2747 0.2495 0.2474 -0.0173 -0.0567 0.0782  132 VAL B CG2   
1007 N  N     . LYS A 134 ? 0.4332 0.3047 0.3692 -0.0465 -0.0881 0.1077  133 LYS B N     
1008 C  CA    . LYS A 134 ? 0.4314 0.2703 0.3539 -0.0581 -0.0978 0.1215  133 LYS B CA    
1009 C  C     . LYS A 134 ? 0.4937 0.3313 0.4063 -0.0498 -0.0962 0.1298  133 LYS B C     
1010 O  O     . LYS A 134 ? 0.5275 0.3812 0.4430 -0.0608 -0.0916 0.1418  133 LYS B O     
1011 C  CB    . LYS A 134 ? 0.5437 0.3367 0.4511 -0.0546 -0.1100 0.1134  133 LYS B CB    
1012 C  CG    . LYS A 134 ? 0.6314 0.3968 0.5305 -0.0694 -0.1181 0.1201  133 LYS B CG    
1013 C  CD    . LYS A 134 ? 0.6982 0.4184 0.5791 -0.0608 -0.1294 0.1084  133 LYS B CD    
1014 C  CE    . LYS A 134 ? 0.7607 0.4496 0.6285 -0.0692 -0.1374 0.1160  133 LYS B CE    
1015 N  NZ    . LYS A 134 ? 0.8338 0.5431 0.7071 -0.0763 -0.1305 0.1324  133 LYS B NZ    
1016 N  N     . GLU A 135 ? 0.4774 0.3029 0.3803 -0.0291 -0.0983 0.1219  134 GLU B N     
1017 C  CA    . GLU A 135 ? 0.5397 0.3705 0.4352 -0.0184 -0.0964 0.1275  134 GLU B CA    
1018 C  C     . GLU A 135 ? 0.4314 0.2952 0.3354 -0.0029 -0.0894 0.1180  134 GLU B C     
1019 O  O     . GLU A 135 ? 0.4268 0.3013 0.3399 0.0048  -0.0859 0.1035  134 GLU B O     
1020 C  CB    . GLU A 135 ? 0.5795 0.3716 0.4585 -0.0065 -0.1044 0.1256  134 GLU B CB    
1021 C  CG    . GLU A 135 ? 0.6922 0.4528 0.5639 -0.0227 -0.1110 0.1320  134 GLU B CG    
1022 C  CD    . GLU A 135 ? 0.7909 0.5456 0.6543 -0.0274 -0.1112 0.1465  134 GLU B CD    
1023 O  OE1   . GLU A 135 ? 0.8557 0.6379 0.7270 -0.0422 -0.1045 0.1576  134 GLU B OE1   
1024 O  OE2   . GLU A 135 ? 0.8762 0.6020 0.7253 -0.0151 -0.1172 0.1469  134 GLU B OE2   
1025 N  N     . GLY A 136 ? 0.4496 0.3327 0.3513 0.0008  -0.0861 0.1252  135 GLY B N     
1026 C  CA    . GLY A 136 ? 0.3965 0.3098 0.3059 0.0153  -0.0805 0.1145  135 GLY B CA    
1027 C  C     . GLY A 136 ? 0.3883 0.3403 0.3143 0.0084  -0.0696 0.1077  135 GLY B C     
1028 O  O     . GLY A 136 ? 0.3600 0.3331 0.2946 0.0180  -0.0655 0.0958  135 GLY B O     
1029 N  N     . MET A 137 ? 0.3424 0.3059 0.2732 -0.0076 -0.0647 0.1153  136 MET B N     
1030 C  CA    . MET A 137 ? 0.3419 0.3420 0.2858 -0.0100 -0.0545 0.1084  136 MET B CA    
1031 C  C     . MET A 137 ? 0.3388 0.3612 0.2790 -0.0006 -0.0517 0.1057  136 MET B C     
1032 O  O     . MET A 137 ? 0.3243 0.3690 0.2741 0.0031  -0.0462 0.0938  136 MET B O     
1033 C  CB    . MET A 137 ? 0.3631 0.3762 0.3127 -0.0260 -0.0493 0.1174  136 MET B CB    
1034 C  CG    . MET A 137 ? 0.3083 0.3558 0.2709 -0.0253 -0.0391 0.1080  136 MET B CG    
1035 S  SD    . MET A 137 ? 0.2833 0.3306 0.2611 -0.0238 -0.0378 0.0939  136 MET B SD    
1036 C  CE    . MET A 137 ? 0.2861 0.3622 0.2703 -0.0153 -0.0294 0.0810  136 MET B CE    
1037 N  N     . ASN A 138 ? 0.3428 0.3570 0.2685 0.0037  -0.0570 0.1158  137 ASN B N     
1038 C  CA    . ASN A 138 ? 0.3167 0.3546 0.2385 0.0122  -0.0556 0.1125  137 ASN B CA    
1039 C  C     . ASN A 138 ? 0.3093 0.3533 0.2389 0.0254  -0.0580 0.0980  137 ASN B C     
1040 O  O     . ASN A 138 ? 0.3087 0.3772 0.2413 0.0295  -0.0559 0.0904  137 ASN B O     
1041 C  CB    . ASN A 138 ? 0.3589 0.3898 0.2621 0.0143  -0.0611 0.1278  137 ASN B CB    
1042 C  CG    . ASN A 138 ? 0.3908 0.3849 0.2833 0.0196  -0.0714 0.1366  137 ASN B CG    
1043 O  OD1   . ASN A 138 ? 0.4335 0.4067 0.3310 0.0252  -0.0754 0.1292  137 ASN B OD1   
1044 N  ND2   . ASN A 138 ? 0.4426 0.4242 0.3198 0.0180  -0.0736 0.1486  137 ASN B ND2   
1045 N  N     . ILE A 139 ? 0.3158 0.3394 0.2486 0.0312  -0.0621 0.0938  138 ILE B N     
1046 C  CA    . ILE A 139 ? 0.3057 0.3398 0.2483 0.0423  -0.0625 0.0806  138 ILE B CA    
1047 C  C     . ILE A 139 ? 0.2993 0.3537 0.2565 0.0356  -0.0545 0.0692  138 ILE B C     
1048 O  O     . ILE A 139 ? 0.2639 0.3394 0.2291 0.0395  -0.0529 0.0600  138 ILE B O     
1049 C  CB    . ILE A 139 ? 0.3503 0.3577 0.2907 0.0509  -0.0676 0.0785  138 ILE B CB    
1050 C  CG1   . ILE A 139 ? 0.3811 0.3580 0.3043 0.0566  -0.0767 0.0905  138 ILE B CG1   
1051 C  CG2   . ILE A 139 ? 0.3451 0.3686 0.2954 0.0631  -0.0670 0.0668  138 ILE B CG2   
1052 C  CD1   . ILE A 139 ? 0.4038 0.3916 0.3201 0.0672  -0.0814 0.0957  138 ILE B CD1   
1053 N  N     . VAL A 140 ? 0.2421 0.2890 0.2031 0.0252  -0.0503 0.0701  139 VAL B N     
1054 C  CA    . VAL A 140 ? 0.2207 0.2833 0.1940 0.0199  -0.0434 0.0606  139 VAL B CA    
1055 C  C     . VAL A 140 ? 0.2442 0.3298 0.2172 0.0174  -0.0392 0.0583  139 VAL B C     
1056 O  O     . VAL A 140 ? 0.2214 0.3210 0.2018 0.0179  -0.0363 0.0480  139 VAL B O     
1057 C  CB    . VAL A 140 ? 0.2512 0.3022 0.2279 0.0103  -0.0411 0.0638  139 VAL B CB    
1058 C  CG1   . VAL A 140 ? 0.2294 0.2940 0.2179 0.0071  -0.0348 0.0546  139 VAL B CG1   
1059 C  CG2   . VAL A 140 ? 0.2506 0.2748 0.2235 0.0134  -0.0472 0.0646  139 VAL B CG2   
1060 N  N     . GLU A 141 ? 0.2470 0.3355 0.2102 0.0140  -0.0389 0.0680  140 GLU B N     
1061 C  CA    . GLU A 141 ? 0.2359 0.3463 0.1946 0.0137  -0.0353 0.0651  140 GLU B CA    
1062 C  C     . GLU A 141 ? 0.2445 0.3657 0.2014 0.0215  -0.0402 0.0579  140 GLU B C     
1063 O  O     . GLU A 141 ? 0.2644 0.4008 0.2244 0.0211  -0.0382 0.0472  140 GLU B O     
1064 C  CB    . GLU A 141 ? 0.2635 0.3776 0.2092 0.0096  -0.0340 0.0784  140 GLU B CB    
1065 C  CG    . GLU A 141 ? 0.3076 0.4182 0.2577 -0.0001 -0.0290 0.0862  140 GLU B CG    
1066 C  CD    . GLU A 141 ? 0.3479 0.4579 0.2860 -0.0069 -0.0287 0.1037  140 GLU B CD    
1067 O  OE1   . GLU A 141 ? 0.3613 0.4709 0.2846 -0.0035 -0.0325 0.1115  140 GLU B OE1   
1068 O  OE2   . GLU A 141 ? 0.4095 0.5196 0.3530 -0.0169 -0.0251 0.1115  140 GLU B OE2   
1069 N  N     . ALA A 142 ? 0.2198 0.3330 0.1724 0.0289  -0.0474 0.0632  141 ALA B N     
1070 C  CA    . ALA A 142 ? 0.2713 0.4000 0.2250 0.0366  -0.0528 0.0572  141 ALA B CA    
1071 C  C     . ALA A 142 ? 0.2693 0.4071 0.2387 0.0362  -0.0512 0.0442  141 ALA B C     
1072 O  O     . ALA A 142 ? 0.2545 0.4115 0.2275 0.0367  -0.0538 0.0366  141 ALA B O     
1073 C  CB    . ALA A 142 ? 0.2798 0.3986 0.2265 0.0472  -0.0610 0.0659  141 ALA B CB    
1074 N  N     . MET A 143 ? 0.2350 0.3599 0.2132 0.0338  -0.0474 0.0420  142 MET B N     
1075 C  CA    . MET A 143 ? 0.2078 0.3410 0.1996 0.0320  -0.0451 0.0316  142 MET B CA    
1076 C  C     . MET A 143 ? 0.2567 0.3997 0.2514 0.0236  -0.0412 0.0231  142 MET B C     
1077 O  O     . MET A 143 ? 0.2197 0.3729 0.2233 0.0208  -0.0415 0.0150  142 MET B O     
1078 C  CB    . MET A 143 ? 0.2483 0.3646 0.2454 0.0320  -0.0422 0.0318  142 MET B CB    
1079 C  CG    . MET A 143 ? 0.2520 0.3552 0.2444 0.0426  -0.0470 0.0373  142 MET B CG    
1080 S  SD    . MET A 143 ? 0.3316 0.4081 0.3226 0.0418  -0.0454 0.0383  142 MET B SD    
1081 C  CE    . MET A 143 ? 0.2691 0.3588 0.2732 0.0349  -0.0387 0.0289  142 MET B CE    
1082 N  N     . GLU A 144 ? 0.2732 0.4128 0.2605 0.0197  -0.0376 0.0249  143 GLU B N     
1083 C  CA    . GLU A 144 ? 0.2604 0.4066 0.2474 0.0149  -0.0344 0.0154  143 GLU B CA    
1084 C  C     . GLU A 144 ? 0.2884 0.4500 0.2719 0.0147  -0.0395 0.0079  143 GLU B C     
1085 O  O     . GLU A 144 ? 0.3276 0.4906 0.3127 0.0100  -0.0390 -0.0025 143 GLU B O     
1086 C  CB    . GLU A 144 ? 0.2526 0.3977 0.2311 0.0137  -0.0291 0.0192  143 GLU B CB    
1087 C  CG    . GLU A 144 ? 0.2766 0.4100 0.2622 0.0111  -0.0243 0.0237  143 GLU B CG    
1088 C  CD    . GLU A 144 ? 0.2895 0.4292 0.2708 0.0099  -0.0181 0.0251  143 GLU B CD    
1089 O  OE1   . GLU A 144 ? 0.2918 0.4404 0.2626 0.0106  -0.0175 0.0314  143 GLU B OE1   
1090 O  OE2   . GLU A 144 ? 0.2757 0.4133 0.2637 0.0091  -0.0139 0.0205  143 GLU B OE2   
1091 N  N     . ARG A 145 ? 0.2812 0.4531 0.2588 0.0197  -0.0456 0.0127  144 ARG B N     
1092 C  CA    . ARG A 145 ? 0.3150 0.5043 0.2888 0.0191  -0.0522 0.0057  144 ARG B CA    
1093 C  C     . ARG A 145 ? 0.3100 0.5072 0.2992 0.0140  -0.0551 -0.0028 144 ARG B C     
1094 O  O     . ARG A 145 ? 0.3171 0.5277 0.3058 0.0096  -0.0609 -0.0109 144 ARG B O     
1095 C  CB    . ARG A 145 ? 0.3796 0.5793 0.3454 0.0270  -0.0593 0.0145  144 ARG B CB    
1096 C  CG    . ARG A 145 ? 0.4563 0.6444 0.4081 0.0313  -0.0568 0.0281  144 ARG B CG    
1097 C  CD    . ARG A 145 ? 0.5023 0.6941 0.4461 0.0407  -0.0650 0.0391  144 ARG B CD    
1098 N  NE    . ARG A 145 ? 0.3871 0.5741 0.3424 0.0483  -0.0689 0.0418  144 ARG B NE    
1099 C  CZ    . ARG A 145 ? 0.5006 0.6793 0.4488 0.0568  -0.0738 0.0508  144 ARG B CZ    
1100 N  NH1   . ARG A 145 ? 0.4893 0.6623 0.4201 0.0569  -0.0751 0.0594  144 ARG B NH1   
1101 N  NH2   . ARG A 145 ? 0.4217 0.5990 0.3797 0.0659  -0.0774 0.0507  144 ARG B NH2   
1102 N  N     . PHE A 146 ? 0.2563 0.4468 0.2585 0.0138  -0.0516 -0.0005 145 PHE B N     
1103 C  CA    . PHE A 146 ? 0.2702 0.4714 0.2876 0.0084  -0.0532 -0.0058 145 PHE B CA    
1104 C  C     . PHE A 146 ? 0.2548 0.4414 0.2775 -0.0005 -0.0476 -0.0112 145 PHE B C     
1105 O  O     . PHE A 146 ? 0.2593 0.4524 0.2945 -0.0065 -0.0475 -0.0133 145 PHE B O     
1106 C  CB    . PHE A 146 ? 0.2215 0.4296 0.2483 0.0168  -0.0534 0.0010  145 PHE B CB    
1107 C  CG    . PHE A 146 ? 0.2959 0.5135 0.3163 0.0279  -0.0595 0.0074  145 PHE B CG    
1108 C  CD1   . PHE A 146 ? 0.3157 0.5551 0.3368 0.0279  -0.0669 0.0046  145 PHE B CD1   
1109 C  CD2   . PHE A 146 ? 0.2533 0.4538 0.2650 0.0375  -0.0585 0.0164  145 PHE B CD2   
1110 C  CE1   . PHE A 146 ? 0.3201 0.5607 0.3336 0.0385  -0.0712 0.0112  145 PHE B CE1   
1111 C  CE2   . PHE A 146 ? 0.3058 0.5112 0.3093 0.0483  -0.0652 0.0235  145 PHE B CE2   
1112 C  CZ    . PHE A 146 ? 0.2813 0.5043 0.2859 0.0489  -0.0703 0.0208  145 PHE B CZ    
1113 N  N     . GLY A 147 ? 0.2600 0.4292 0.2735 -0.0011 -0.0431 -0.0126 146 GLY B N     
1114 C  CA    . GLY A 147 ? 0.2255 0.3786 0.2420 -0.0071 -0.0387 -0.0172 146 GLY B CA    
1115 C  C     . GLY A 147 ? 0.2584 0.4075 0.2681 -0.0132 -0.0416 -0.0283 146 GLY B C     
1116 O  O     . GLY A 147 ? 0.2687 0.4298 0.2729 -0.0147 -0.0477 -0.0332 146 GLY B O     
1117 N  N     . SER A 148 ? 0.2048 0.3350 0.2137 -0.0160 -0.0381 -0.0326 147 SER B N     
1118 C  CA    . SER A 148 ? 0.2615 0.3802 0.2626 -0.0212 -0.0415 -0.0444 147 SER B CA    
1119 C  C     . SER A 148 ? 0.2211 0.3178 0.2187 -0.0174 -0.0360 -0.0463 147 SER B C     
1120 O  O     . SER A 148 ? 0.2502 0.3436 0.2539 -0.0133 -0.0305 -0.0381 147 SER B O     
1121 C  CB    . SER A 148 ? 0.2511 0.3713 0.2610 -0.0345 -0.0476 -0.0483 147 SER B CB    
1122 O  OG    . SER A 148 ? 0.2382 0.3497 0.2595 -0.0393 -0.0436 -0.0421 147 SER B OG    
1123 N  N     . ARG A 149 ? 0.2433 0.3240 0.2311 -0.0187 -0.0386 -0.0576 148 ARG B N     
1124 C  CA    . ARG A 149 ? 0.2767 0.3358 0.2604 -0.0126 -0.0344 -0.0608 148 ARG B CA    
1125 C  C     . ARG A 149 ? 0.2710 0.3171 0.2662 -0.0169 -0.0323 -0.0533 148 ARG B C     
1126 O  O     . ARG A 149 ? 0.2639 0.3045 0.2613 -0.0091 -0.0270 -0.0484 148 ARG B O     
1127 C  CB    . ARG A 149 ? 0.3610 0.4005 0.3303 -0.0132 -0.0396 -0.0760 148 ARG B CB    
1128 C  CG    . ARG A 149 ? 0.3572 0.3732 0.3207 -0.0033 -0.0359 -0.0805 148 ARG B CG    
1129 C  CD    . ARG A 149 ? 0.4162 0.4115 0.3605 0.0001  -0.0412 -0.0981 148 ARG B CD    
1130 N  NE    . ARG A 149 ? 0.4534 0.4226 0.3914 0.0114  -0.0389 -0.1036 148 ARG B NE    
1131 C  CZ    . ARG A 149 ? 0.5023 0.4423 0.4432 0.0057  -0.0426 -0.1026 148 ARG B CZ    
1132 N  NH1   . ARG A 149 ? 0.5061 0.4402 0.4552 -0.0124 -0.0481 -0.0973 148 ARG B NH1   
1133 N  NH2   . ARG A 149 ? 0.4803 0.3971 0.4150 0.0188  -0.0408 -0.1068 148 ARG B NH2   
1134 N  N     . ASN A 150 ? 0.2765 0.3199 0.2791 -0.0295 -0.0363 -0.0514 149 ASN B N     
1135 C  CA    . ASN A 150 ? 0.2472 0.2798 0.2583 -0.0333 -0.0335 -0.0431 149 ASN B CA    
1136 C  C     . ASN A 150 ? 0.2277 0.2805 0.2499 -0.0333 -0.0298 -0.0319 149 ASN B C     
1137 O  O     . ASN A 150 ? 0.2507 0.2981 0.2785 -0.0363 -0.0274 -0.0248 149 ASN B O     
1138 C  CB    . ASN A 150 ? 0.3107 0.3255 0.3222 -0.0474 -0.0388 -0.0458 149 ASN B CB    
1139 C  CG    . ASN A 150 ? 0.2971 0.3337 0.3188 -0.0608 -0.0422 -0.0429 149 ASN B CG    
1140 O  OD1   . ASN A 150 ? 0.2787 0.3418 0.3050 -0.0573 -0.0418 -0.0413 149 ASN B OD1   
1141 N  ND2   . ASN A 150 ? 0.2883 0.3148 0.3141 -0.0762 -0.0456 -0.0413 149 ASN B ND2   
1142 N  N     . GLY A 151 ? 0.2024 0.2762 0.2257 -0.0286 -0.0296 -0.0302 150 GLY B N     
1143 C  CA    . GLY A 151 ? 0.1883 0.2766 0.2188 -0.0252 -0.0267 -0.0211 150 GLY B CA    
1144 C  C     . GLY A 151 ? 0.1807 0.2885 0.2198 -0.0311 -0.0291 -0.0190 150 GLY B C     
1145 O  O     . GLY A 151 ? 0.1654 0.2863 0.2086 -0.0254 -0.0275 -0.0131 150 GLY B O     
1146 N  N     . LYS A 152 ? 0.1965 0.3066 0.2390 -0.0424 -0.0333 -0.0236 151 LYS B N     
1147 C  CA    . LYS A 152 ? 0.1878 0.3236 0.2414 -0.0484 -0.0358 -0.0214 151 LYS B CA    
1148 C  C     . LYS A 152 ? 0.2212 0.3781 0.2741 -0.0396 -0.0388 -0.0215 151 LYS B C     
1149 O  O     . LYS A 152 ? 0.2292 0.3829 0.2721 -0.0363 -0.0422 -0.0268 151 LYS B O     
1150 C  CB    . LYS A 152 ? 0.1857 0.3203 0.2423 -0.0641 -0.0415 -0.0269 151 LYS B CB    
1151 C  CG    . LYS A 152 ? 0.3134 0.4270 0.3706 -0.0737 -0.0392 -0.0243 151 LYS B CG    
1152 C  CD    . LYS A 152 ? 0.4111 0.5457 0.4820 -0.0792 -0.0347 -0.0146 151 LYS B CD    
1153 C  CE    . LYS A 152 ? 0.4346 0.5481 0.5035 -0.0853 -0.0302 -0.0082 151 LYS B CE    
1154 N  NZ    . LYS A 152 ? 0.4695 0.5999 0.5504 -0.1030 -0.0302 -0.0025 151 LYS B NZ    
1155 N  N     . THR A 153 ? 0.1763 0.3545 0.2384 -0.0345 -0.0375 -0.0155 152 THR B N     
1156 C  CA    . THR A 153 ? 0.1783 0.3735 0.2388 -0.0242 -0.0410 -0.0140 152 THR B CA    
1157 C  C     . THR A 153 ? 0.2183 0.4420 0.2881 -0.0303 -0.0481 -0.0170 152 THR B C     
1158 O  O     . THR A 153 ? 0.2359 0.4736 0.3185 -0.0414 -0.0485 -0.0172 152 THR B O     
1159 C  CB    . THR A 153 ? 0.1959 0.3941 0.2582 -0.0115 -0.0369 -0.0066 152 THR B CB    
1160 O  OG1   . THR A 153 ? 0.2007 0.4166 0.2758 -0.0131 -0.0340 -0.0040 152 THR B OG1   
1161 C  CG2   . THR A 153 ? 0.1852 0.3564 0.2389 -0.0079 -0.0315 -0.0039 152 THR B CG2   
1162 N  N     . SER A 154 ? 0.1881 0.4218 0.2514 -0.0238 -0.0541 -0.0185 153 SER B N     
1163 C  CA    . SER A 154 ? 0.2331 0.4970 0.3050 -0.0285 -0.0626 -0.0213 153 SER B CA    
1164 C  C     . SER A 154 ? 0.2235 0.5065 0.3036 -0.0161 -0.0615 -0.0142 153 SER B C     
1165 O  O     . SER A 154 ? 0.2157 0.5181 0.3040 -0.0189 -0.0653 -0.0147 153 SER B O     
1166 C  CB    . SER A 154 ? 0.2543 0.5153 0.3113 -0.0280 -0.0700 -0.0271 153 SER B CB    
1167 O  OG    . SER A 154 ? 0.2342 0.4869 0.2780 -0.0136 -0.0682 -0.0220 153 SER B OG    
1168 N  N     . LYS A 155 ? 0.2166 0.4931 0.2940 -0.0025 -0.0569 -0.0082 154 LYS B N     
1169 C  CA    . LYS A 155 ? 0.2626 0.5517 0.3460 0.0110  -0.0549 -0.0028 154 LYS B CA    
1170 C  C     . LYS A 155 ? 0.2177 0.4989 0.3038 0.0166  -0.0476 0.0004  154 LYS B C     
1171 O  O     . LYS A 155 ? 0.2188 0.4771 0.2980 0.0121  -0.0439 0.0001  154 LYS B O     
1172 C  CB    . LYS A 155 ? 0.2529 0.5365 0.3240 0.0258  -0.0597 0.0011  154 LYS B CB    
1173 C  CG    . LYS A 155 ? 0.2966 0.5924 0.3647 0.0219  -0.0675 -0.0017 154 LYS B CG    
1174 C  CD    . LYS A 155 ? 0.3220 0.6131 0.3776 0.0359  -0.0722 0.0037  154 LYS B CD    
1175 C  CE    . LYS A 155 ? 0.3680 0.6696 0.4181 0.0313  -0.0799 0.0008  154 LYS B CE    
1176 N  NZ    . LYS A 155 ? 0.3982 0.7265 0.4649 0.0238  -0.0830 -0.0033 154 LYS B NZ    
1177 N  N     . LYS A 156 ? 0.2129 0.5077 0.3059 0.0270  -0.0443 0.0031  155 LYS B N     
1178 C  CA    . LYS A 156 ? 0.2200 0.5086 0.3131 0.0351  -0.0376 0.0052  155 LYS B CA    
1179 C  C     . LYS A 156 ? 0.2406 0.5053 0.3191 0.0508  -0.0400 0.0081  155 LYS B C     
1180 O  O     . LYS A 156 ? 0.2181 0.4825 0.2917 0.0647  -0.0432 0.0100  155 LYS B O     
1181 C  CB    . LYS A 156 ? 0.2595 0.5726 0.3629 0.0418  -0.0332 0.0059  155 LYS B CB    
1182 C  CG    . LYS A 156 ? 0.3812 0.7115 0.4973 0.0261  -0.0273 0.0058  155 LYS B CG    
1183 C  CD    . LYS A 156 ? 0.4474 0.7970 0.5691 0.0356  -0.0196 0.0076  155 LYS B CD    
1184 C  CE    . LYS A 156 ? 0.3986 0.7330 0.5079 0.0587  -0.0183 0.0071  155 LYS B CE    
1185 N  NZ    . LYS A 156 ? 0.4485 0.7961 0.5588 0.0674  -0.0094 0.0072  155 LYS B NZ    
1186 N  N     . ILE A 157 ? 0.1809 0.4139 0.2481 0.0464  -0.0368 0.0086  156 ILE B N     
1187 C  CA    . ILE A 157 ? 0.2156 0.4187 0.2668 0.0562  -0.0389 0.0120  156 ILE B CA    
1188 C  C     . ILE A 157 ? 0.2143 0.4046 0.2617 0.0645  -0.0344 0.0117  156 ILE B C     
1189 O  O     . ILE A 157 ? 0.2316 0.4109 0.2782 0.0558  -0.0291 0.0104  156 ILE B O     
1190 C  CB    . ILE A 157 ? 0.2113 0.3901 0.2530 0.0453  -0.0386 0.0129  156 ILE B CB    
1191 C  CG1   . ILE A 157 ? 0.2101 0.4018 0.2538 0.0355  -0.0419 0.0106  156 ILE B CG1   
1192 C  CG2   . ILE A 157 ? 0.2460 0.3964 0.2726 0.0533  -0.0413 0.0185  156 ILE B CG2   
1193 C  CD1   . ILE A 157 ? 0.2392 0.4505 0.2828 0.0435  -0.0493 0.0123  156 ILE B CD1   
1194 N  N     . THR A 158 ? 0.1965 0.3843 0.2388 0.0822  -0.0371 0.0126  157 THR B N     
1195 C  CA    . THR A 158 ? 0.2106 0.3875 0.2470 0.0925  -0.0333 0.0101  157 THR B CA    
1196 C  C     . THR A 158 ? 0.2936 0.4309 0.3110 0.1016  -0.0381 0.0118  157 THR B C     
1197 O  O     . THR A 158 ? 0.2888 0.4116 0.2982 0.1058  -0.0450 0.0163  157 THR B O     
1198 C  CB    . THR A 158 ? 0.2398 0.4481 0.2855 0.1086  -0.0315 0.0075  157 THR B CB    
1199 O  OG1   . THR A 158 ? 0.2787 0.4870 0.3212 0.1207  -0.0382 0.0095  157 THR B OG1   
1200 C  CG2   . THR A 158 ? 0.2573 0.5060 0.3231 0.0965  -0.0260 0.0067  157 THR B CG2   
1201 N  N     . ILE A 159 ? 0.2611 0.3804 0.2701 0.1039  -0.0349 0.0085  158 ILE B N     
1202 C  CA    . ILE A 159 ? 0.2743 0.3576 0.2647 0.1155  -0.0404 0.0079  158 ILE B CA    
1203 C  C     . ILE A 159 ? 0.3118 0.4070 0.3007 0.1388  -0.0407 0.0034  158 ILE B C     
1204 O  O     . ILE A 159 ? 0.3150 0.4209 0.3036 0.1470  -0.0349 -0.0026 158 ILE B O     
1205 C  CB    . ILE A 159 ? 0.2837 0.3429 0.2645 0.1074  -0.0384 0.0053  158 ILE B CB    
1206 C  CG1   . ILE A 159 ? 0.2267 0.2826 0.2130 0.0863  -0.0375 0.0100  158 ILE B CG1   
1207 C  CG2   . ILE A 159 ? 0.3144 0.3321 0.2749 0.1157  -0.0461 0.0044  158 ILE B CG2   
1208 C  CD1   . ILE A 159 ? 0.2392 0.2816 0.2202 0.0783  -0.0346 0.0073  158 ILE B CD1   
1209 N  N     . ALA A 160 ? 0.3104 0.4054 0.2977 0.1510  -0.0475 0.0067  159 ALA B N     
1210 C  CA    . ALA A 160 ? 0.3049 0.4117 0.2918 0.1698  -0.0463 0.0022  159 ALA B CA    
1211 C  C     . ALA A 160 ? 0.3949 0.4637 0.3602 0.1846  -0.0490 -0.0036 159 ALA B C     
1212 O  O     . ALA A 160 ? 0.3837 0.4631 0.3463 0.1998  -0.0450 -0.0104 159 ALA B O     
1213 C  CB    . ALA A 160 ? 0.3311 0.4439 0.3211 0.1725  -0.0518 0.0075  159 ALA B CB    
1214 N  N     . ASP A 161 ? 0.3932 0.4176 0.3419 0.1793  -0.0562 -0.0010 160 ASP B N     
1215 C  CA    . ASP A 161 ? 0.4444 0.4274 0.3706 0.1895  -0.0604 -0.0074 160 ASP B CA    
1216 C  C     . ASP A 161 ? 0.4282 0.3744 0.3435 0.1735  -0.0664 -0.0035 160 ASP B C     
1217 O  O     . ASP A 161 ? 0.3930 0.3429 0.3167 0.1544  -0.0669 0.0051  160 ASP B O     
1218 C  CB    . ASP A 161 ? 0.4593 0.4180 0.3722 0.2033  -0.0670 -0.0076 160 ASP B CB    
1219 C  CG    . ASP A 161 ? 0.5103 0.4343 0.4003 0.2171  -0.0699 -0.0178 160 ASP B CG    
1220 O  OD1   . ASP A 161 ? 0.4796 0.4077 0.3652 0.2192  -0.0650 -0.0260 160 ASP B OD1   
1221 O  OD2   . ASP A 161 ? 0.5561 0.4487 0.4313 0.2258  -0.0776 -0.0175 160 ASP B OD2   
1222 N  N     . CYS A 162 ? 0.4554 0.3703 0.3530 0.1765  -0.0689 -0.0109 161 CYS B N     
1223 C  CA    . CYS A 162 ? 0.4556 0.3388 0.3446 0.1557  -0.0737 -0.0079 161 CYS B CA    
1224 C  C     . CYS A 162 ? 0.4830 0.3232 0.3467 0.1658  -0.0810 -0.0173 161 CYS B C     
1225 O  O     . CYS A 162 ? 0.5388 0.3815 0.3933 0.1868  -0.0785 -0.0278 161 CYS B O     
1226 C  CB    . CYS A 162 ? 0.4149 0.3260 0.3193 0.1356  -0.0649 -0.0068 161 CYS B CB    
1227 S  SG    . CYS A 162 ? 0.3933 0.3415 0.3042 0.1439  -0.0526 -0.0165 161 CYS B SG    
1228 N  N     . GLY A 163 ? 0.5189 0.3214 0.3713 0.1494  -0.0898 -0.0138 162 GLY B N     
1229 C  CA    . GLY A 163 ? 0.5488 0.3047 0.3750 0.1560  -0.0994 -0.0231 162 GLY B CA    
1230 C  C     . GLY A 163 ? 0.6006 0.3207 0.4199 0.1321  -0.1100 -0.0157 162 GLY B C     
1231 O  O     . GLY A 163 ? 0.5547 0.2914 0.3908 0.1114  -0.1079 -0.0039 162 GLY B O     
1232 N  N     . GLN A 164 ? 0.5930 0.2733 0.3903 0.1315  -0.1193 -0.0235 163 GLN B N     
1233 C  CA    . GLN A 164 ? 0.6423 0.2896 0.4332 0.1075  -0.1305 -0.0169 163 GLN B CA    
1234 C  C     . GLN A 164 ? 0.7208 0.3397 0.5025 0.1061  -0.1381 -0.0108 163 GLN B C     
1235 O  O     . GLN A 164 ? 0.7181 0.3261 0.4875 0.1262  -0.1389 -0.0178 163 GLN B O     
1236 C  CB    . GLN A 164 ? 0.6958 0.3191 0.4685 0.1041  -0.1375 -0.0290 163 GLN B CB    
1237 C  CG    . GLN A 164 ? 0.7129 0.3104 0.4826 0.0766  -0.1492 -0.0224 163 GLN B CG    
1238 C  CD    . GLN A 164 ? 0.7206 0.3035 0.4753 0.0722  -0.1558 -0.0342 163 GLN B CD    
1239 O  OE1   . GLN A 164 ? 0.7411 0.3315 0.4854 0.0905  -0.1508 -0.0475 163 GLN B OE1   
1240 N  NE2   . GLN A 164 ? 0.7339 0.2997 0.4879 0.0477  -0.1666 -0.0288 163 GLN B NE2   
1241 N  N     . LEU A 165 ? 0.6727 0.2824 0.4611 0.0827  -0.1431 0.0031  164 LEU B N     
1242 C  CA    . LEU A 165 ? 0.7306 0.3133 0.5107 0.0785  -0.1502 0.0113  164 LEU B CA    
1243 C  C     . LEU A 165 ? 0.8083 0.3483 0.5689 0.0666  -0.1636 0.0070  164 LEU B C     
1244 O  O     . LEU A 165 ? 0.7541 0.2933 0.5144 0.0540  -0.1668 0.0026  164 LEU B O     
1245 C  CB    . LEU A 165 ? 0.6835 0.2842 0.4812 0.0600  -0.1470 0.0299  164 LEU B CB    
1246 C  CG    . LEU A 165 ? 0.6980 0.3367 0.5116 0.0717  -0.1363 0.0359  164 LEU B CG    
1247 C  CD1   . LEU A 165 ? 0.7009 0.3565 0.5283 0.0518  -0.1337 0.0538  164 LEU B CD1   
1248 C  CD2   . LEU A 165 ? 0.6623 0.2943 0.4674 0.0954  -0.1363 0.0328  164 LEU B CD2   
1249 N  N     . VAL B 3   ? 0.2935 0.6545 0.5601 -0.1224 -0.0258 -0.0897 2   VAL D N     
1250 C  CA    . VAL B 3   ? 0.3133 0.6596 0.5739 -0.1272 -0.0086 -0.0823 2   VAL D CA    
1251 C  C     . VAL B 3   ? 0.2482 0.5748 0.4838 -0.1189 -0.0117 -0.0801 2   VAL D C     
1252 O  O     . VAL B 3   ? 0.2625 0.5933 0.4909 -0.1035 -0.0228 -0.0811 2   VAL D O     
1253 C  CB    . VAL B 3   ? 0.3848 0.7592 0.6649 -0.1236 0.0050  -0.0789 2   VAL D CB    
1254 C  CG1   . VAL B 3   ? 0.3096 0.7005 0.5863 -0.1045 0.0028  -0.0813 2   VAL D CG1   
1255 C  CG2   . VAL B 3   ? 0.3918 0.7496 0.6687 -0.1354 0.0234  -0.0686 2   VAL D CG2   
1256 N  N     . ASN B 4   ? 0.2408 0.5386 0.4601 -0.1266 -0.0025 -0.0748 3   ASN D N     
1257 C  CA    . ASN B 4   ? 0.2754 0.5425 0.4639 -0.1164 -0.0044 -0.0688 3   ASN D CA    
1258 C  C     . ASN B 4   ? 0.3190 0.5876 0.5018 -0.1016 0.0023  -0.0633 3   ASN D C     
1259 O  O     . ASN B 4   ? 0.3318 0.6052 0.5202 -0.1049 0.0175  -0.0586 3   ASN D O     
1260 C  CB    . ASN B 4   ? 0.2440 0.4817 0.4185 -0.1273 0.0036  -0.0652 3   ASN D CB    
1261 C  CG    . ASN B 4   ? 0.3127 0.5416 0.4832 -0.1358 -0.0058 -0.0725 3   ASN D CG    
1262 O  OD1   . ASN B 4   ? 0.3007 0.5429 0.4733 -0.1322 -0.0192 -0.0782 3   ASN D OD1   
1263 N  ND2   . ASN B 4   ? 0.3316 0.5342 0.4930 -0.1430 0.0006  -0.0712 3   ASN D ND2   
1264 N  N     . PRO B 5   ? 0.3041 0.5684 0.4756 -0.0853 -0.0088 -0.0636 4   PRO D N     
1265 C  CA    . PRO B 5   ? 0.3263 0.5915 0.4928 -0.0699 -0.0041 -0.0618 4   PRO D CA    
1266 C  C     . PRO B 5   ? 0.3176 0.5511 0.4585 -0.0694 0.0030  -0.0546 4   PRO D C     
1267 O  O     . PRO B 5   ? 0.2711 0.4812 0.3975 -0.0783 0.0019  -0.0508 4   PRO D O     
1268 C  CB    . PRO B 5   ? 0.2675 0.5335 0.4323 -0.0538 -0.0220 -0.0655 4   PRO D CB    
1269 C  CG    . PRO B 5   ? 0.2946 0.5413 0.4454 -0.0616 -0.0340 -0.0624 4   PRO D CG    
1270 C  CD    . PRO B 5   ? 0.2728 0.5290 0.4340 -0.0803 -0.0269 -0.0649 4   PRO D CD    
1271 N  N     . THR B 6   ? 0.3003 0.5362 0.4361 -0.0579 0.0101  -0.0539 5   THR D N     
1272 C  CA    . THR B 6   ? 0.2890 0.4989 0.4011 -0.0551 0.0154  -0.0481 5   THR D CA    
1273 C  C     . THR B 6   ? 0.3291 0.5299 0.4300 -0.0369 0.0055  -0.0521 5   THR D C     
1274 O  O     . THR B 6   ? 0.2858 0.5072 0.3981 -0.0239 0.0040  -0.0595 5   THR D O     
1275 C  CB    . THR B 6   ? 0.3515 0.5709 0.4643 -0.0593 0.0339  -0.0428 5   THR D CB    
1276 O  OG1   . THR B 6   ? 0.3736 0.5962 0.4984 -0.0775 0.0421  -0.0382 5   THR D OG1   
1277 C  CG2   . THR B 6   ? 0.3476 0.5411 0.4347 -0.0549 0.0373  -0.0371 5   THR D CG2   
1278 N  N     . VAL B 7   ? 0.3172 0.4877 0.3973 -0.0360 -0.0012 -0.0482 6   VAL D N     
1279 C  CA    . VAL B 7   ? 0.3054 0.4614 0.3747 -0.0210 -0.0117 -0.0518 6   VAL D CA    
1280 C  C     . VAL B 7   ? 0.3233 0.4615 0.3729 -0.0208 -0.0050 -0.0480 6   VAL D C     
1281 O  O     . VAL B 7   ? 0.3071 0.4403 0.3502 -0.0319 0.0054  -0.0411 6   VAL D O     
1282 C  CB    . VAL B 7   ? 0.3605 0.4980 0.4261 -0.0203 -0.0302 -0.0498 6   VAL D CB    
1283 C  CG1   . VAL B 7   ? 0.3407 0.4982 0.4251 -0.0191 -0.0380 -0.0531 6   VAL D CG1   
1284 C  CG2   . VAL B 7   ? 0.3299 0.4485 0.3815 -0.0347 -0.0303 -0.0409 6   VAL D CG2   
1285 N  N     . PHE B 8   ? 0.3033 0.4323 0.3445 -0.0069 -0.0119 -0.0538 7   PHE D N     
1286 C  CA    . PHE B 8   ? 0.3064 0.4209 0.3289 -0.0050 -0.0078 -0.0521 7   PHE D CA    
1287 C  C     . PHE B 8   ? 0.3297 0.4187 0.3428 0.0018  -0.0244 -0.0552 7   PHE D C     
1288 O  O     . PHE B 8   ? 0.3425 0.4270 0.3637 0.0106  -0.0380 -0.0612 7   PHE D O     
1289 C  CB    . PHE B 8   ? 0.3292 0.4647 0.3498 0.0055  0.0039  -0.0580 7   PHE D CB    
1290 C  CG    . PHE B 8   ? 0.3377 0.4799 0.3625 0.0247  -0.0055 -0.0725 7   PHE D CG    
1291 C  CD1   . PHE B 8   ? 0.3607 0.4837 0.3720 0.0353  -0.0158 -0.0800 7   PHE D CD1   
1292 C  CD2   . PHE B 8   ? 0.3443 0.5117 0.3887 0.0324  -0.0056 -0.0800 7   PHE D CD2   
1293 C  CE1   . PHE B 8   ? 0.3867 0.5129 0.4034 0.0543  -0.0262 -0.0959 7   PHE D CE1   
1294 C  CE2   . PHE B 8   ? 0.3420 0.5153 0.3920 0.0522  -0.0151 -0.0950 7   PHE D CE2   
1295 C  CZ    . PHE B 8   ? 0.3687 0.5196 0.4046 0.0636  -0.0258 -0.1036 7   PHE D CZ    
1296 N  N     . PHE B 9   ? 0.2968 0.3685 0.2943 -0.0030 -0.0239 -0.0504 8   PHE D N     
1297 C  CA    . PHE B 9   ? 0.3161 0.3651 0.3046 0.0016  -0.0378 -0.0534 8   PHE D CA    
1298 C  C     . PHE B 9   ? 0.3492 0.4023 0.3253 0.0099  -0.0315 -0.0594 8   PHE D C     
1299 O  O     . PHE B 9   ? 0.3176 0.3782 0.2857 0.0042  -0.0183 -0.0527 8   PHE D O     
1300 C  CB    . PHE B 9   ? 0.3043 0.3346 0.2855 -0.0122 -0.0426 -0.0425 8   PHE D CB    
1301 C  CG    . PHE B 9   ? 0.3249 0.3503 0.3133 -0.0216 -0.0503 -0.0349 8   PHE D CG    
1302 C  CD1   . PHE B 9   ? 0.2784 0.3107 0.2793 -0.0168 -0.0569 -0.0377 8   PHE D CD1   
1303 C  CD2   . PHE B 9   ? 0.3447 0.3602 0.3261 -0.0344 -0.0520 -0.0250 8   PHE D CD2   
1304 C  CE1   . PHE B 9   ? 0.3413 0.3707 0.3457 -0.0253 -0.0648 -0.0294 8   PHE D CE1   
1305 C  CE2   . PHE B 9   ? 0.3014 0.3157 0.2858 -0.0432 -0.0584 -0.0174 8   PHE D CE2   
1306 C  CZ    . PHE B 9   ? 0.3287 0.3489 0.3236 -0.0386 -0.0654 -0.0191 8   PHE D CZ    
1307 N  N     . ASP B 10  ? 0.3424 0.3898 0.3163 0.0238  -0.0416 -0.0721 9   ASP D N     
1308 C  CA    . ASP B 10  ? 0.3616 0.4085 0.3204 0.0308  -0.0402 -0.0785 9   ASP D CA    
1309 C  C     . ASP B 10  ? 0.3611 0.3808 0.3142 0.0244  -0.0545 -0.0763 9   ASP D C     
1310 O  O     . ASP B 10  ? 0.3971 0.3975 0.3575 0.0264  -0.0710 -0.0810 9   ASP D O     
1311 C  CB    . ASP B 10  ? 0.3711 0.4301 0.3300 0.0503  -0.0430 -0.0965 9   ASP D CB    
1312 C  CG    . ASP B 10  ? 0.4270 0.5207 0.3896 0.0560  -0.0254 -0.0976 9   ASP D CG    
1313 O  OD1   . ASP B 10  ? 0.4341 0.5411 0.3915 0.0464  -0.0095 -0.0852 9   ASP D OD1   
1314 O  OD2   . ASP B 10  ? 0.4246 0.5326 0.3968 0.0702  -0.0279 -0.1108 9   ASP D OD2   
1315 N  N     . ILE B 11  ? 0.3409 0.3596 0.2831 0.0161  -0.0484 -0.0681 10  ILE D N     
1316 C  CA    . ILE B 11  ? 0.3321 0.3314 0.2713 0.0065  -0.0591 -0.0632 10  ILE D CA    
1317 C  C     . ILE B 11  ? 0.3951 0.3898 0.3248 0.0157  -0.0676 -0.0753 10  ILE D C     
1318 O  O     . ILE B 11  ? 0.3857 0.3967 0.3038 0.0247  -0.0585 -0.0804 10  ILE D O     
1319 C  CB    . ILE B 11  ? 0.3556 0.3602 0.2899 -0.0057 -0.0478 -0.0492 10  ILE D CB    
1320 C  CG1   . ILE B 11  ? 0.3211 0.3319 0.2643 -0.0143 -0.0392 -0.0400 10  ILE D CG1   
1321 C  CG2   . ILE B 11  ? 0.3791 0.3701 0.3121 -0.0151 -0.0578 -0.0447 10  ILE D CG2   
1322 C  CD1   . ILE B 11  ? 0.3292 0.3272 0.2820 -0.0217 -0.0513 -0.0363 10  ILE D CD1   
1323 N  N     . ALA B 12  ? 0.3845 0.3575 0.3187 0.0121  -0.0853 -0.0791 11  ALA D N     
1324 C  CA    . ALA B 12  ? 0.3944 0.3615 0.3212 0.0183  -0.0958 -0.0916 11  ALA D CA    
1325 C  C     . ALA B 12  ? 0.4345 0.3906 0.3630 0.0031  -0.1033 -0.0824 11  ALA D C     
1326 O  O     . ALA B 12  ? 0.3838 0.3308 0.3218 -0.0109 -0.1055 -0.0691 11  ALA D O     
1327 C  CB    . ALA B 12  ? 0.4378 0.3881 0.3714 0.0298  -0.1131 -0.1093 11  ALA D CB    
1328 N  N     . VAL B 13  ? 0.4153 0.3753 0.3350 0.0063  -0.1076 -0.0901 12  VAL D N     
1329 C  CA    . VAL B 13  ? 0.4338 0.3890 0.3567 -0.0069 -0.1153 -0.0838 12  VAL D CA    
1330 C  C     . VAL B 13  ? 0.4678 0.4082 0.3932 -0.0029 -0.1351 -0.1008 12  VAL D C     
1331 O  O     . VAL B 13  ? 0.4285 0.3781 0.3420 0.0113  -0.1367 -0.1166 12  VAL D O     
1332 C  CB    . VAL B 13  ? 0.3863 0.3627 0.2976 -0.0069 -0.1027 -0.0768 12  VAL D CB    
1333 C  CG1   . VAL B 13  ? 0.4216 0.3973 0.3385 -0.0186 -0.1122 -0.0731 12  VAL D CG1   
1334 C  CG2   . VAL B 13  ? 0.3930 0.3803 0.3031 -0.0105 -0.0844 -0.0619 12  VAL D CG2   
1335 N  N     . ASP B 14  ? 0.4193 0.3367 0.3603 -0.0154 -0.1506 -0.0976 13  ASP D N     
1336 C  CA    . ASP B 14  ? 0.4777 0.3762 0.4277 -0.0135 -0.1676 -0.1103 13  ASP D CA    
1337 C  C     . ASP B 14  ? 0.5591 0.4548 0.5035 0.0081  -0.1703 -0.1308 13  ASP D C     
1338 O  O     . ASP B 14  ? 0.5681 0.4630 0.5112 0.0172  -0.1768 -0.1457 13  ASP D O     
1339 C  CB    . ASP B 14  ? 0.5177 0.4263 0.4675 -0.0189 -0.1703 -0.1123 13  ASP D CB    
1340 C  CG    . ASP B 14  ? 0.4806 0.3892 0.4437 -0.0408 -0.1714 -0.0939 13  ASP D CG    
1341 O  OD1   . ASP B 14  ? 0.4995 0.3941 0.4737 -0.0521 -0.1730 -0.0800 13  ASP D OD1   
1342 O  OD2   . ASP B 14  ? 0.4943 0.4193 0.4568 -0.0459 -0.1705 -0.0931 13  ASP D OD2   
1343 N  N     . GLY B 15  ? 0.5224 0.4184 0.4648 0.0164  -0.1655 -0.1321 14  GLY D N     
1344 C  CA    . GLY B 15  ? 0.5312 0.4306 0.4697 0.0381  -0.1658 -0.1515 14  GLY D CA    
1345 C  C     . GLY B 15  ? 0.5127 0.4448 0.4308 0.0527  -0.1500 -0.1602 14  GLY D C     
1346 O  O     . GLY B 15  ? 0.6000 0.5426 0.5147 0.0710  -0.1469 -0.1752 14  GLY D O     
1347 N  N     . GLU B 16  ? 0.4828 0.4330 0.3896 0.0459  -0.1386 -0.1491 15  GLU D N     
1348 C  CA    . GLU B 16  ? 0.5363 0.5174 0.4234 0.0583  -0.1225 -0.1520 15  GLU D CA    
1349 C  C     . GLU B 16  ? 0.4806 0.4773 0.3679 0.0553  -0.1016 -0.1347 15  GLU D C     
1350 O  O     . GLU B 16  ? 0.4490 0.4411 0.3431 0.0402  -0.0961 -0.1162 15  GLU D O     
1351 C  CB    . GLU B 16  ? 0.5488 0.5405 0.4243 0.0529  -0.1218 -0.1470 15  GLU D CB    
1352 C  CG    . GLU B 16  ? 0.6060 0.6255 0.4610 0.0676  -0.1110 -0.1524 15  GLU D CG    
1353 C  CD    . GLU B 16  ? 0.7015 0.7199 0.5570 0.0766  -0.1220 -0.1690 15  GLU D CD    
1354 O  OE1   . GLU B 16  ? 0.7237 0.7338 0.5872 0.0868  -0.1291 -0.1847 15  GLU D OE1   
1355 O  OE2   . GLU B 16  ? 0.7817 0.8068 0.6311 0.0737  -0.1251 -0.1671 15  GLU D OE2   
1356 N  N     . PRO B 17  ? 0.5130 0.5301 0.3941 0.0690  -0.0897 -0.1407 16  PRO D N     
1357 C  CA    . PRO B 17  ? 0.4620 0.4938 0.3464 0.0637  -0.0706 -0.1239 16  PRO D CA    
1358 C  C     . PRO B 17  ? 0.4468 0.4873 0.3218 0.0533  -0.0583 -0.1054 16  PRO D C     
1359 O  O     . PRO B 17  ? 0.4739 0.5235 0.3332 0.0578  -0.0582 -0.1073 16  PRO D O     
1360 C  CB    . PRO B 17  ? 0.4772 0.5357 0.3547 0.0810  -0.0601 -0.1354 16  PRO D CB    
1361 C  CG    . PRO B 17  ? 0.5002 0.5525 0.3750 0.0971  -0.0768 -0.1615 16  PRO D CG    
1362 C  CD    . PRO B 17  ? 0.5115 0.5406 0.3840 0.0895  -0.0939 -0.1643 16  PRO D CD    
1363 N  N     . LEU B 18  ? 0.4465 0.4816 0.3319 0.0395  -0.0507 -0.0884 17  LEU D N     
1364 C  CA    . LEU B 18  ? 0.3960 0.4366 0.2761 0.0301  -0.0390 -0.0711 17  LEU D CA    
1365 C  C     . LEU B 18  ? 0.4085 0.4665 0.2872 0.0308  -0.0201 -0.0615 17  LEU D C     
1366 O  O     . LEU B 18  ? 0.4376 0.5092 0.3030 0.0342  -0.0093 -0.0543 17  LEU D O     
1367 C  CB    . LEU B 18  ? 0.3909 0.4146 0.2836 0.0142  -0.0441 -0.0606 17  LEU D CB    
1368 C  CG    . LEU B 18  ? 0.3308 0.3584 0.2206 0.0056  -0.0336 -0.0451 17  LEU D CG    
1369 C  CD1   . LEU B 18  ? 0.4120 0.4462 0.2874 0.0117  -0.0363 -0.0465 17  LEU D CD1   
1370 C  CD2   . LEU B 18  ? 0.3697 0.3852 0.2727 -0.0093 -0.0380 -0.0369 17  LEU D CD2   
1371 N  N     . GLY B 19  ? 0.3663 0.4245 0.2593 0.0275  -0.0168 -0.0609 18  GLY D N     
1372 C  CA    . GLY B 19  ? 0.3829 0.4588 0.2791 0.0263  0.0001  -0.0528 18  GLY D CA    
1373 C  C     . GLY B 19  ? 0.3883 0.4590 0.3036 0.0182  -0.0009 -0.0509 18  GLY D C     
1374 O  O     . GLY B 19  ? 0.3950 0.4486 0.3184 0.0143  -0.0141 -0.0542 18  GLY D O     
1375 N  N     . ARG B 20  ? 0.3517 0.4386 0.2740 0.0149  0.0130  -0.0444 19  ARG D N     
1376 C  CA    . ARG B 20  ? 0.3103 0.4004 0.2514 0.0093  0.0133  -0.0445 19  ARG D CA    
1377 C  C     . ARG B 20  ? 0.3692 0.4519 0.3167 -0.0063 0.0195  -0.0315 19  ARG D C     
1378 O  O     . ARG B 20  ? 0.3532 0.4392 0.2955 -0.0114 0.0312  -0.0214 19  ARG D O     
1379 C  CB    . ARG B 20  ? 0.3056 0.4242 0.2537 0.0163  0.0244  -0.0484 19  ARG D CB    
1380 C  CG    . ARG B 20  ? 0.3149 0.4424 0.2848 0.0097  0.0259  -0.0478 19  ARG D CG    
1381 C  CD    . ARG B 20  ? 0.3332 0.4924 0.3133 0.0201  0.0330  -0.0562 19  ARG D CD    
1382 N  NE    . ARG B 20  ? 0.3884 0.5483 0.3664 0.0379  0.0212  -0.0733 19  ARG D NE    
1383 C  CZ    . ARG B 20  ? 0.4052 0.5906 0.3940 0.0510  0.0226  -0.0854 19  ARG D CZ    
1384 N  NH1   . ARG B 20  ? 0.3750 0.5919 0.3787 0.0473  0.0365  -0.0815 19  ARG D NH1   
1385 N  NH2   . ARG B 20  ? 0.4099 0.5899 0.3964 0.0685  0.0094  -0.1027 19  ARG D NH2   
1386 N  N     . VAL B 21  ? 0.3191 0.3917 0.2778 -0.0135 0.0109  -0.0319 20  VAL D N     
1387 C  CA    . VAL B 21  ? 0.3008 0.3700 0.2673 -0.0271 0.0160  -0.0234 20  VAL D CA    
1388 C  C     . VAL B 21  ? 0.3040 0.3867 0.2876 -0.0291 0.0161  -0.0270 20  VAL D C     
1389 O  O     . VAL B 21  ? 0.2981 0.3808 0.2873 -0.0228 0.0050  -0.0341 20  VAL D O     
1390 C  CB    . VAL B 21  ? 0.3017 0.3525 0.2647 -0.0342 0.0061  -0.0206 20  VAL D CB    
1391 C  CG1   . VAL B 21  ? 0.2798 0.3294 0.2490 -0.0465 0.0119  -0.0147 20  VAL D CG1   
1392 C  CG2   . VAL B 21  ? 0.3307 0.3717 0.2795 -0.0309 0.0034  -0.0191 20  VAL D CG2   
1393 N  N     . SER B 22  ? 0.2924 0.3869 0.2859 -0.0373 0.0277  -0.0223 21  SER D N     
1394 C  CA    . SER B 22  ? 0.2753 0.3859 0.2877 -0.0409 0.0275  -0.0259 21  SER D CA    
1395 C  C     . SER B 22  ? 0.3041 0.4067 0.3230 -0.0546 0.0259  -0.0227 21  SER D C     
1396 O  O     . SER B 22  ? 0.2874 0.3768 0.2992 -0.0617 0.0306  -0.0169 21  SER D O     
1397 C  CB    . SER B 22  ? 0.3430 0.4787 0.3657 -0.0408 0.0415  -0.0247 21  SER D CB    
1398 O  OG    . SER B 22  ? 0.3171 0.4502 0.3419 -0.0534 0.0534  -0.0147 21  SER D OG    
1399 N  N     . PHE B 23  ? 0.2492 0.3604 0.2811 -0.0569 0.0181  -0.0274 22  PHE D N     
1400 C  CA    . PHE B 23  ? 0.2714 0.3778 0.3076 -0.0687 0.0150  -0.0267 22  PHE D CA    
1401 C  C     . PHE B 23  ? 0.2633 0.3908 0.3203 -0.0748 0.0167  -0.0309 22  PHE D C     
1402 O  O     . PHE B 23  ? 0.2943 0.4391 0.3623 -0.0675 0.0122  -0.0356 22  PHE D O     
1403 C  CB    . PHE B 23  ? 0.2407 0.3372 0.2696 -0.0675 0.0002  -0.0275 22  PHE D CB    
1404 C  CG    . PHE B 23  ? 0.3157 0.3940 0.3278 -0.0623 -0.0046 -0.0239 22  PHE D CG    
1405 C  CD1   . PHE B 23  ? 0.3160 0.3908 0.3250 -0.0507 -0.0119 -0.0263 22  PHE D CD1   
1406 C  CD2   . PHE B 23  ? 0.2774 0.3430 0.2783 -0.0686 -0.0027 -0.0197 22  PHE D CD2   
1407 C  CE1   . PHE B 23  ? 0.3261 0.3839 0.3217 -0.0478 -0.0177 -0.0238 22  PHE D CE1   
1408 C  CE2   . PHE B 23  ? 0.2762 0.3286 0.2643 -0.0652 -0.0076 -0.0165 22  PHE D CE2   
1409 C  CZ    . PHE B 23  ? 0.3343 0.3820 0.3200 -0.0561 -0.0155 -0.0181 22  PHE D CZ    
1410 N  N     . GLU B 24  ? 0.2516 0.3777 0.3153 -0.0875 0.0217  -0.0305 23  GLU D N     
1411 C  CA    . GLU B 24  ? 0.2853 0.4298 0.3691 -0.0957 0.0196  -0.0362 23  GLU D CA    
1412 C  C     . GLU B 24  ? 0.2908 0.4330 0.3698 -0.0963 0.0054  -0.0406 23  GLU D C     
1413 O  O     . GLU B 24  ? 0.2574 0.3823 0.3209 -0.0988 0.0027  -0.0390 23  GLU D O     
1414 C  CB    . GLU B 24  ? 0.2809 0.4221 0.3749 -0.1098 0.0294  -0.0353 23  GLU D CB    
1415 C  CG    . GLU B 24  ? 0.3290 0.4911 0.4468 -0.1199 0.0267  -0.0426 23  GLU D CG    
1416 C  CD    . GLU B 24  ? 0.3057 0.4589 0.4345 -0.1353 0.0336  -0.0433 23  GLU D CD    
1417 O  OE1   . GLU B 24  ? 0.3503 0.4824 0.4702 -0.1373 0.0423  -0.0360 23  GLU D OE1   
1418 O  OE2   . GLU B 24  ? 0.3215 0.4891 0.4696 -0.1453 0.0296  -0.0511 23  GLU D OE2   
1419 N  N     . LEU B 25  ? 0.3035 0.4649 0.3946 -0.0931 -0.0038 -0.0453 24  LEU D N     
1420 C  CA    . LEU B 25  ? 0.2726 0.4344 0.3577 -0.0933 -0.0184 -0.0473 24  LEU D CA    
1421 C  C     . LEU B 25  ? 0.2977 0.4763 0.3976 -0.1043 -0.0209 -0.0552 24  LEU D C     
1422 O  O     . LEU B 25  ? 0.2825 0.4834 0.4044 -0.1062 -0.0196 -0.0599 24  LEU D O     
1423 C  CB    . LEU B 25  ? 0.2927 0.4605 0.3780 -0.0805 -0.0311 -0.0460 24  LEU D CB    
1424 C  CG    . LEU B 25  ? 0.2716 0.4226 0.3448 -0.0686 -0.0319 -0.0410 24  LEU D CG    
1425 C  CD1   . LEU B 25  ? 0.2443 0.3969 0.3193 -0.0566 -0.0485 -0.0404 24  LEU D CD1   
1426 C  CD2   . LEU B 25  ? 0.2911 0.4179 0.3431 -0.0728 -0.0298 -0.0348 24  LEU D CD2   
1427 N  N     . PHE B 26  ? 0.2884 0.4592 0.3769 -0.1112 -0.0250 -0.0578 25  PHE D N     
1428 C  CA    . PHE B 26  ? 0.3066 0.4908 0.4079 -0.1225 -0.0273 -0.0682 25  PHE D CA    
1429 C  C     . PHE B 26  ? 0.2990 0.5071 0.4071 -0.1202 -0.0424 -0.0728 25  PHE D C     
1430 O  O     . PHE B 26  ? 0.3176 0.5253 0.4135 -0.1205 -0.0508 -0.0754 25  PHE D O     
1431 C  CB    . PHE B 26  ? 0.3195 0.4875 0.4055 -0.1289 -0.0255 -0.0719 25  PHE D CB    
1432 C  CG    . PHE B 26  ? 0.3096 0.4550 0.3912 -0.1303 -0.0122 -0.0677 25  PHE D CG    
1433 C  CD1   . PHE B 26  ? 0.3064 0.4501 0.4045 -0.1342 -0.0011 -0.0653 25  PHE D CD1   
1434 C  CD2   . PHE B 26  ? 0.2927 0.4208 0.3539 -0.1277 -0.0107 -0.0651 25  PHE D CD2   
1435 C  CE1   . PHE B 26  ? 0.2870 0.4094 0.3789 -0.1345 0.0101  -0.0591 25  PHE D CE1   
1436 C  CE2   . PHE B 26  ? 0.3250 0.4330 0.3823 -0.1273 0.0003  -0.0608 25  PHE D CE2   
1437 C  CZ    . PHE B 26  ? 0.2880 0.3921 0.3600 -0.1305 0.0101  -0.0574 25  PHE D CZ    
1438 N  N     . ALA B 27  ? 0.2933 0.5195 0.4188 -0.1137 -0.0449 -0.0721 26  ALA D N     
1439 C  CA    . ALA B 27  ? 0.2947 0.5460 0.4304 -0.1100 -0.0597 -0.0763 26  ALA D CA    
1440 C  C     . ALA B 27  ? 0.2792 0.5354 0.4224 -0.1174 -0.0608 -0.0842 26  ALA D C     
1441 O  O     . ALA B 27  ? 0.2771 0.5468 0.4203 -0.1138 -0.0738 -0.0867 26  ALA D O     
1442 C  CB    . ALA B 27  ? 0.3092 0.5807 0.4666 -0.1003 -0.0600 -0.0762 26  ALA D CB    
1443 N  N     . ASP B 28  ? 0.2811 0.5273 0.4323 -0.1273 -0.0487 -0.0880 27  ASP D N     
1444 C  CA    . ASP B 28  ? 0.3102 0.5610 0.4713 -0.1346 -0.0517 -0.0967 27  ASP D CA    
1445 C  C     . ASP B 28  ? 0.3042 0.5417 0.4437 -0.1358 -0.0575 -0.1020 27  ASP D C     
1446 O  O     . ASP B 28  ? 0.3352 0.5785 0.4810 -0.1406 -0.0627 -0.1112 27  ASP D O     
1447 C  CB    . ASP B 28  ? 0.3206 0.5655 0.5011 -0.1452 -0.0387 -0.0978 27  ASP D CB    
1448 C  CG    . ASP B 28  ? 0.3428 0.5589 0.5107 -0.1489 -0.0273 -0.0939 27  ASP D CG    
1449 O  OD1   . ASP B 28  ? 0.3477 0.5507 0.4932 -0.1433 -0.0277 -0.0904 27  ASP D OD1   
1450 O  OD2   . ASP B 28  ? 0.4455 0.6529 0.6276 -0.1578 -0.0179 -0.0927 27  ASP D OD2   
1451 N  N     . LYS B 29  ? 0.2845 0.5073 0.3998 -0.1317 -0.0569 -0.0970 28  LYS D N     
1452 C  CA    . LYS B 29  ? 0.3202 0.5371 0.4134 -0.1310 -0.0620 -0.1013 28  LYS D CA    
1453 C  C     . LYS B 29  ? 0.3003 0.5236 0.3721 -0.1228 -0.0719 -0.0923 28  LYS D C     
1454 O  O     . LYS B 29  ? 0.3044 0.5348 0.3613 -0.1214 -0.0795 -0.0951 28  LYS D O     
1455 C  CB    . LYS B 29  ? 0.3557 0.5497 0.4383 -0.1346 -0.0512 -0.1033 28  LYS D CB    
1456 C  CG    . LYS B 29  ? 0.4256 0.6081 0.5288 -0.1427 -0.0417 -0.1085 28  LYS D CG    
1457 C  CD    . LYS B 29  ? 0.3863 0.5503 0.4831 -0.1464 -0.0374 -0.1175 28  LYS D CD    
1458 C  CE    . LYS B 29  ? 0.3366 0.4987 0.4542 -0.1548 -0.0384 -0.1275 28  LYS D CE    
1459 N  NZ    . LYS B 29  ? 0.3717 0.5210 0.5091 -0.1618 -0.0281 -0.1208 28  LYS D NZ    
1460 N  N     . VAL B 30  ? 0.2779 0.4994 0.3482 -0.1178 -0.0726 -0.0811 29  VAL D N     
1461 C  CA    . VAL B 30  ? 0.3075 0.5305 0.3592 -0.1108 -0.0829 -0.0694 29  VAL D CA    
1462 C  C     . VAL B 30  ? 0.2971 0.5291 0.3629 -0.1039 -0.0901 -0.0632 29  VAL D C     
1463 O  O     . VAL B 30  ? 0.3166 0.5389 0.3794 -0.1009 -0.0885 -0.0553 29  VAL D O     
1464 C  CB    . VAL B 30  ? 0.2987 0.5035 0.3291 -0.1119 -0.0766 -0.0614 29  VAL D CB    
1465 C  CG1   . VAL B 30  ? 0.3058 0.5103 0.3184 -0.1152 -0.0741 -0.0668 29  VAL D CG1   
1466 C  CG2   . VAL B 30  ? 0.3069 0.4963 0.3456 -0.1155 -0.0629 -0.0628 29  VAL D CG2   
1467 N  N     . PRO B 31  ? 0.2905 0.5424 0.3728 -0.1003 -0.0990 -0.0675 30  PRO D N     
1468 C  CA    . PRO B 31  ? 0.2767 0.5416 0.3774 -0.0915 -0.1053 -0.0647 30  PRO D CA    
1469 C  C     . PRO B 31  ? 0.2675 0.5256 0.3541 -0.0818 -0.1182 -0.0514 30  PRO D C     
1470 O  O     . PRO B 31  ? 0.3178 0.5651 0.4117 -0.0716 -0.1162 -0.0470 30  PRO D O     
1471 C  CB    . PRO B 31  ? 0.2518 0.5405 0.3702 -0.0894 -0.1141 -0.0718 30  PRO D CB    
1472 C  CG    . PRO B 31  ? 0.2625 0.5485 0.3632 -0.0952 -0.1175 -0.0751 30  PRO D CG    
1473 C  CD    . PRO B 31  ? 0.2628 0.5281 0.3496 -0.1036 -0.1036 -0.0770 30  PRO D CD    
1474 N  N     . LYS B 32  ? 0.2887 0.5421 0.3536 -0.0806 -0.1287 -0.0427 31  LYS D N     
1475 C  CA    . LYS B 32  ? 0.3067 0.5498 0.3582 -0.0722 -0.1426 -0.0261 31  LYS D CA    
1476 C  C     . LYS B 32  ? 0.3281 0.5391 0.3664 -0.0725 -0.1331 -0.0169 31  LYS D C     
1477 O  O     . LYS B 32  ? 0.3249 0.5176 0.3644 -0.0623 -0.1388 -0.0080 31  LYS D O     
1478 C  CB    . LYS B 32  ? 0.3054 0.5494 0.3349 -0.0722 -0.1522 -0.0174 31  LYS D CB    
1479 C  CG    . LYS B 32  ? 0.4025 0.6672 0.4410 -0.0645 -0.1667 -0.0200 31  LYS D CG    
1480 C  CD    . LYS B 32  ? 0.4404 0.7018 0.4522 -0.0626 -0.1770 -0.0056 31  LYS D CD    
1481 C  CE    . LYS B 32  ? 0.4615 0.6972 0.4560 -0.0622 -0.1782 0.0146  31  LYS D CE    
1482 N  NZ    . LYS B 32  ? 0.5728 0.8035 0.5444 -0.0594 -0.1894 0.0343  31  LYS D NZ    
1483 N  N     . THR B 33  ? 0.3157 0.5200 0.3422 -0.0835 -0.1197 -0.0204 32  THR D N     
1484 C  CA    . THR B 33  ? 0.3031 0.4811 0.3180 -0.0849 -0.1102 -0.0132 32  THR D CA    
1485 C  C     . THR B 33  ? 0.2991 0.4667 0.3301 -0.0794 -0.0997 -0.0194 32  THR D C     
1486 O  O     . THR B 33  ? 0.2937 0.4407 0.3209 -0.0734 -0.0996 -0.0125 32  THR D O     
1487 C  CB    . THR B 33  ? 0.3092 0.4878 0.3094 -0.0963 -0.0995 -0.0170 32  THR D CB    
1488 O  OG1   . THR B 33  ? 0.3242 0.5162 0.3090 -0.0991 -0.1072 -0.0133 32  THR D OG1   
1489 C  CG2   . THR B 33  ? 0.2563 0.4111 0.2429 -0.0977 -0.0920 -0.0074 32  THR D CG2   
1490 N  N     . ALA B 34  ? 0.3005 0.4835 0.3499 -0.0818 -0.0912 -0.0323 33  ALA D N     
1491 C  CA    . ALA B 34  ? 0.2998 0.4793 0.3645 -0.0765 -0.0809 -0.0369 33  ALA D CA    
1492 C  C     . ALA B 34  ? 0.3074 0.4875 0.3818 -0.0614 -0.0911 -0.0344 33  ALA D C     
1493 O  O     . ALA B 34  ? 0.3412 0.5064 0.4151 -0.0533 -0.0873 -0.0329 33  ALA D O     
1494 C  CB    . ALA B 34  ? 0.2677 0.4675 0.3522 -0.0840 -0.0713 -0.0489 33  ALA D CB    
1495 N  N     . GLU B 35  ? 0.2788 0.4765 0.3622 -0.0563 -0.1052 -0.0348 34  GLU D N     
1496 C  CA    . GLU B 35  ? 0.3268 0.5261 0.4227 -0.0397 -0.1159 -0.0343 34  GLU D CA    
1497 C  C     . GLU B 35  ? 0.3421 0.5097 0.4220 -0.0320 -0.1250 -0.0227 34  GLU D C     
1498 O  O     . GLU B 35  ? 0.3536 0.5104 0.4406 -0.0191 -0.1267 -0.0253 34  GLU D O     
1499 C  CB    . GLU B 35  ? 0.3093 0.5342 0.4174 -0.0353 -0.1312 -0.0360 34  GLU D CB    
1500 C  CG    . GLU B 35  ? 0.3753 0.5997 0.4950 -0.0159 -0.1464 -0.0341 34  GLU D CG    
1501 C  CD    . GLU B 35  ? 0.3746 0.6102 0.5168 -0.0040 -0.1375 -0.0461 34  GLU D CD    
1502 O  OE1   . GLU B 35  ? 0.2916 0.5393 0.4419 -0.0120 -0.1193 -0.0542 34  GLU D OE1   
1503 O  OE2   . GLU B 35  ? 0.4189 0.6517 0.5708 0.0144  -0.1493 -0.0470 34  GLU D OE2   
1504 N  N     . ASN B 36  ? 0.3600 0.5133 0.4189 -0.0401 -0.1314 -0.0104 35  ASN D N     
1505 C  CA    . ASN B 36  ? 0.3428 0.4650 0.3881 -0.0365 -0.1396 0.0023  35  ASN D CA    
1506 C  C     . ASN B 36  ? 0.3658 0.4694 0.4102 -0.0347 -0.1277 -0.0025 35  ASN D C     
1507 O  O     . ASN B 36  ? 0.3807 0.4659 0.4290 -0.0232 -0.1348 -0.0025 35  ASN D O     
1508 C  CB    . ASN B 36  ? 0.3617 0.4779 0.3844 -0.0497 -0.1426 0.0162  35  ASN D CB    
1509 C  CG    . ASN B 36  ? 0.3920 0.4778 0.4021 -0.0498 -0.1511 0.0317  35  ASN D CG    
1510 O  OD1   . ASN B 36  ? 0.4309 0.5014 0.4463 -0.0393 -0.1668 0.0387  35  ASN D OD1   
1511 N  ND2   . ASN B 36  ? 0.3850 0.4617 0.3801 -0.0619 -0.1416 0.0371  35  ASN D ND2   
1512 N  N     . PHE B 37  ? 0.3637 0.4723 0.4035 -0.0451 -0.1106 -0.0078 36  PHE D N     
1513 C  CA    . PHE B 37  ? 0.3084 0.4015 0.3446 -0.0440 -0.0994 -0.0110 36  PHE D CA    
1514 C  C     . PHE B 37  ? 0.3520 0.4536 0.4047 -0.0310 -0.0948 -0.0228 36  PHE D C     
1515 O  O     . PHE B 37  ? 0.3411 0.4272 0.3921 -0.0220 -0.0953 -0.0253 36  PHE D O     
1516 C  CB    . PHE B 37  ? 0.3075 0.4051 0.3357 -0.0571 -0.0833 -0.0130 36  PHE D CB    
1517 C  CG    . PHE B 37  ? 0.2751 0.3555 0.2948 -0.0574 -0.0739 -0.0127 36  PHE D CG    
1518 C  CD1   . PHE B 37  ? 0.3061 0.3693 0.3106 -0.0632 -0.0769 -0.0035 36  PHE D CD1   
1519 C  CD2   . PHE B 37  ? 0.2774 0.3626 0.3047 -0.0523 -0.0617 -0.0212 36  PHE D CD2   
1520 C  CE1   . PHE B 37  ? 0.3033 0.3540 0.3015 -0.0632 -0.0693 -0.0042 36  PHE D CE1   
1521 C  CE2   . PHE B 37  ? 0.3096 0.3814 0.3277 -0.0517 -0.0540 -0.0208 36  PHE D CE2   
1522 C  CZ    . PHE B 37  ? 0.2739 0.3284 0.2782 -0.0567 -0.0582 -0.0133 36  PHE D CZ    
1523 N  N     . ARG B 38  ? 0.2914 0.4204 0.3609 -0.0298 -0.0907 -0.0308 37  ARG D N     
1524 C  CA    . ARG B 38  ? 0.3428 0.4878 0.4302 -0.0170 -0.0864 -0.0416 37  ARG D CA    
1525 C  C     . ARG B 38  ? 0.3425 0.4756 0.4343 0.0009  -0.1021 -0.0430 37  ARG D C     
1526 O  O     . ARG B 38  ? 0.3619 0.4881 0.4549 0.0123  -0.0993 -0.0501 37  ARG D O     
1527 C  CB    . ARG B 38  ? 0.2909 0.4703 0.3988 -0.0198 -0.0831 -0.0483 37  ARG D CB    
1528 C  CG    . ARG B 38  ? 0.3162 0.5195 0.4443 -0.0084 -0.0754 -0.0591 37  ARG D CG    
1529 C  CD    . ARG B 38  ? 0.2737 0.5125 0.4265 -0.0067 -0.0795 -0.0654 37  ARG D CD    
1530 N  NE    . ARG B 38  ? 0.3114 0.5494 0.4691 0.0064  -0.1004 -0.0644 37  ARG D NE    
1531 C  CZ    . ARG B 38  ? 0.3386 0.5721 0.5029 0.0267  -0.1102 -0.0688 37  ARG D CZ    
1532 N  NH1   . ARG B 38  ? 0.2750 0.5095 0.4422 0.0371  -0.1005 -0.0770 37  ARG D NH1   
1533 N  NH2   . ARG B 38  ? 0.3480 0.5752 0.5152 0.0377  -0.1309 -0.0652 37  ARG D NH2   
1534 N  N     . ALA B 39  ? 0.3116 0.4406 0.4045 0.0042  -0.1198 -0.0363 38  ALA D N     
1535 C  CA    . ALA B 39  ? 0.3704 0.4862 0.4707 0.0227  -0.1372 -0.0376 38  ALA D CA    
1536 C  C     . ALA B 39  ? 0.3836 0.4610 0.4690 0.0245  -0.1435 -0.0321 38  ALA D C     
1537 O  O     . ALA B 39  ? 0.3813 0.4458 0.4736 0.0411  -0.1515 -0.0401 38  ALA D O     
1538 C  CB    . ALA B 39  ? 0.3523 0.4720 0.4569 0.0258  -0.1560 -0.0291 38  ALA D CB    
1539 N  N     . LEU B 40  ? 0.3627 0.4229 0.4290 0.0080  -0.1406 -0.0199 39  LEU D N     
1540 C  CA    . LEU B 40  ? 0.3717 0.3983 0.4264 0.0074  -0.1457 -0.0152 39  LEU D CA    
1541 C  C     . LEU B 40  ? 0.3974 0.4244 0.4517 0.0122  -0.1322 -0.0283 39  LEU D C     
1542 O  O     . LEU B 40  ? 0.4140 0.4164 0.4646 0.0186  -0.1391 -0.0314 39  LEU D O     
1543 C  CB    . LEU B 40  ? 0.3659 0.3805 0.4025 -0.0116 -0.1450 0.0011  39  LEU D CB    
1544 C  CG    . LEU B 40  ? 0.4117 0.4250 0.4433 -0.0175 -0.1589 0.0173  39  LEU D CG    
1545 C  CD1   . LEU B 40  ? 0.4041 0.4172 0.4175 -0.0370 -0.1523 0.0304  39  LEU D CD1   
1546 C  CD2   . LEU B 40  ? 0.4203 0.4050 0.4552 -0.0083 -0.1800 0.0257  39  LEU D CD2   
1547 N  N     . SER B 41  ? 0.3625 0.4162 0.4201 0.0086  -0.1139 -0.0358 40  SER D N     
1548 C  CA    . SER B 41  ? 0.3400 0.3966 0.3953 0.0139  -0.1011 -0.0464 40  SER D CA    
1549 C  C     . SER B 41  ? 0.3711 0.4385 0.4408 0.0348  -0.1045 -0.0615 40  SER D C     
1550 O  O     . SER B 41  ? 0.3738 0.4350 0.4390 0.0440  -0.1016 -0.0712 40  SER D O     
1551 C  CB    . SER B 41  ? 0.3444 0.4235 0.3982 0.0025  -0.0804 -0.0467 40  SER D CB    
1552 O  OG    . SER B 41  ? 0.3350 0.4052 0.3759 -0.0144 -0.0764 -0.0359 40  SER D OG    
1553 N  N     . THR B 42  ? 0.3742 0.4604 0.4612 0.0436  -0.1111 -0.0652 41  THR D N     
1554 C  CA    . THR B 42  ? 0.3849 0.4822 0.4868 0.0660  -0.1158 -0.0810 41  THR D CA    
1555 C  C     . THR B 42  ? 0.4211 0.4857 0.5244 0.0804  -0.1390 -0.0827 41  THR D C     
1556 O  O     . THR B 42  ? 0.4224 0.4872 0.5337 0.1005  -0.1436 -0.0988 41  THR D O     
1557 C  CB    . THR B 42  ? 0.3650 0.5020 0.4892 0.0723  -0.1125 -0.0871 41  THR D CB    
1558 O  OG1   . THR B 42  ? 0.3486 0.4803 0.4795 0.0720  -0.1297 -0.0785 41  THR D OG1   
1559 C  CG2   . THR B 42  ? 0.3254 0.4932 0.4515 0.0562  -0.0904 -0.0851 41  THR D CG2   
1560 N  N     . GLY B 43  ? 0.4085 0.4449 0.5042 0.0709  -0.1537 -0.0667 42  GLY D N     
1561 C  CA    . GLY B 43  ? 0.4221 0.4251 0.5218 0.0835  -0.1773 -0.0654 42  GLY D CA    
1562 C  C     . GLY B 43  ? 0.4854 0.5019 0.6053 0.1021  -0.1903 -0.0711 42  GLY D C     
1563 O  O     . GLY B 43  ? 0.5044 0.4940 0.6314 0.1176  -0.2107 -0.0734 42  GLY D O     
1564 N  N     . GLU B 44  ? 0.4413 0.4986 0.5724 0.1009  -0.1802 -0.0734 43  GLU D N     
1565 C  CA    . GLU B 44  ? 0.4512 0.5297 0.6049 0.1205  -0.1909 -0.0818 43  GLU D CA    
1566 C  C     . GLU B 44  ? 0.4428 0.4975 0.5981 0.1241  -0.2158 -0.0668 43  GLU D C     
1567 O  O     . GLU B 44  ? 0.4581 0.5202 0.6323 0.1449  -0.2302 -0.0738 43  GLU D O     
1568 C  CB    . GLU B 44  ? 0.4327 0.5622 0.5992 0.1147  -0.1741 -0.0866 43  GLU D CB    
1569 C  CG    . GLU B 44  ? 0.4009 0.5383 0.5599 0.0933  -0.1725 -0.0703 43  GLU D CG    
1570 C  CD    . GLU B 44  ? 0.3941 0.5779 0.5658 0.0844  -0.1535 -0.0773 43  GLU D CD    
1571 O  OE1   . GLU B 44  ? 0.3477 0.5425 0.5168 0.0792  -0.1337 -0.0845 43  GLU D OE1   
1572 O  OE2   . GLU B 44  ? 0.3920 0.6017 0.5777 0.0839  -0.1597 -0.0760 43  GLU D OE2   
1573 N  N     . LYS B 45  ? 0.4635 0.4916 0.5999 0.1052  -0.2214 -0.0458 44  LYS D N     
1574 C  CA    . LYS B 45  ? 0.5039 0.5096 0.6391 0.1073  -0.2448 -0.0279 44  LYS D CA    
1575 C  C     . LYS B 45  ? 0.5306 0.4844 0.6619 0.1144  -0.2637 -0.0223 44  LYS D C     
1576 O  O     . LYS B 45  ? 0.5971 0.5257 0.7251 0.1134  -0.2836 -0.0032 44  LYS D O     
1577 C  CB    . LYS B 45  ? 0.5254 0.5360 0.6421 0.0827  -0.2413 -0.0064 44  LYS D CB    
1578 C  CG    . LYS B 45  ? 0.4873 0.5445 0.6076 0.0732  -0.2246 -0.0120 44  LYS D CG    
1579 C  CD    . LYS B 45  ? 0.4922 0.5835 0.6356 0.0895  -0.2330 -0.0206 44  LYS D CD    
1580 C  CE    . LYS B 45  ? 0.5007 0.6332 0.6450 0.0743  -0.2203 -0.0215 44  LYS D CE    
1581 N  NZ    . LYS B 45  ? 0.4836 0.6594 0.6557 0.0872  -0.2187 -0.0375 44  LYS D NZ    
1582 N  N     . GLY B 46  ? 0.5107 0.4478 0.6421 0.1206  -0.2588 -0.0376 45  GLY D N     
1583 C  CA    . GLY B 46  ? 0.5339 0.4202 0.6632 0.1257  -0.2770 -0.0350 45  GLY D CA    
1584 C  C     . GLY B 46  ? 0.5706 0.4299 0.6801 0.1021  -0.2719 -0.0220 45  GLY D C     
1585 O  O     . GLY B 46  ? 0.5971 0.4130 0.7063 0.1033  -0.2877 -0.0190 45  GLY D O     
1586 N  N     . PHE B 47  ? 0.5274 0.4111 0.6225 0.0813  -0.2510 -0.0156 46  PHE D N     
1587 C  CA    . PHE B 47  ? 0.5585 0.4235 0.6361 0.0589  -0.2450 -0.0032 46  PHE D CA    
1588 C  C     . PHE B 47  ? 0.5163 0.4179 0.5838 0.0449  -0.2191 -0.0059 46  PHE D C     
1589 O  O     . PHE B 47  ? 0.4916 0.4283 0.5648 0.0484  -0.2091 -0.0117 46  PHE D O     
1590 C  CB    . PHE B 47  ? 0.5621 0.4013 0.6311 0.0436  -0.2604 0.0257  46  PHE D CB    
1591 C  CG    . PHE B 47  ? 0.5612 0.4266 0.6264 0.0380  -0.2602 0.0409  46  PHE D CG    
1592 C  CD1   . PHE B 47  ? 0.5299 0.4345 0.5869 0.0266  -0.2397 0.0391  46  PHE D CD1   
1593 C  CD2   . PHE B 47  ? 0.5945 0.4463 0.6660 0.0473  -0.2818 0.0540  46  PHE D CD2   
1594 C  CE1   . PHE B 47  ? 0.5488 0.4788 0.6028 0.0226  -0.2410 0.0495  46  PHE D CE1   
1595 C  CE2   . PHE B 47  ? 0.6333 0.5121 0.7006 0.0437  -0.2828 0.0663  46  PHE D CE2   
1596 C  CZ    . PHE B 47  ? 0.5794 0.4986 0.6381 0.0315  -0.2624 0.0625  46  PHE D CZ    
1597 N  N     . GLY B 48  ? 0.4998 0.3932 0.5543 0.0296  -0.2091 -0.0029 47  GLY D N     
1598 C  CA    . GLY B 48  ? 0.4066 0.3299 0.4514 0.0167  -0.1861 -0.0043 47  GLY D CA    
1599 C  C     . GLY B 48  ? 0.4507 0.3629 0.4853 0.0080  -0.1771 -0.0078 47  GLY D C     
1600 O  O     . GLY B 48  ? 0.4166 0.2983 0.4490 0.0042  -0.1892 -0.0026 47  GLY D O     
1601 N  N     . TYR B 49  ? 0.4135 0.3509 0.4442 0.0061  -0.1570 -0.0175 48  TYR D N     
1602 C  CA    . TYR B 49  ? 0.3832 0.3170 0.4021 -0.0049 -0.1465 -0.0170 48  TYR D CA    
1603 C  C     . TYR B 49  ? 0.4355 0.3554 0.4549 0.0064  -0.1494 -0.0323 48  TYR D C     
1604 O  O     . TYR B 49  ? 0.4203 0.3296 0.4310 -0.0023 -0.1476 -0.0307 48  TYR D O     
1605 C  CB    . TYR B 49  ? 0.3566 0.3202 0.3702 -0.0117 -0.1248 -0.0191 48  TYR D CB    
1606 C  CG    . TYR B 49  ? 0.3810 0.3576 0.3905 -0.0261 -0.1209 -0.0055 48  TYR D CG    
1607 C  CD1   . TYR B 49  ? 0.3261 0.2898 0.3270 -0.0399 -0.1284 0.0109  48  TYR D CD1   
1608 C  CD2   . TYR B 49  ? 0.3387 0.3425 0.3529 -0.0266 -0.1091 -0.0097 48  TYR D CD2   
1609 C  CE1   . TYR B 49  ? 0.3614 0.3417 0.3562 -0.0519 -0.1239 0.0213  48  TYR D CE1   
1610 C  CE2   . TYR B 49  ? 0.3390 0.3554 0.3489 -0.0386 -0.1061 -0.0009 48  TYR D CE2   
1611 C  CZ    . TYR B 49  ? 0.3421 0.3475 0.3412 -0.0501 -0.1135 0.0137  48  TYR D CZ    
1612 O  OH    . TYR B 49  ? 0.3378 0.3601 0.3314 -0.0603 -0.1097 0.0197  48  TYR D OH    
1613 N  N     . LYS B 50  ? 0.4308 0.3537 0.4601 0.0261  -0.1537 -0.0486 49  LYS D N     
1614 C  CA    . LYS B 50  ? 0.4165 0.3313 0.4439 0.0378  -0.1550 -0.0661 49  LYS D CA    
1615 C  C     . LYS B 50  ? 0.4754 0.3526 0.5008 0.0315  -0.1726 -0.0617 49  LYS D C     
1616 O  O     . LYS B 50  ? 0.4999 0.3517 0.5330 0.0309  -0.1908 -0.0532 49  LYS D O     
1617 C  CB    . LYS B 50  ? 0.4227 0.3467 0.4624 0.0618  -0.1594 -0.0852 49  LYS D CB    
1618 C  CG    . LYS B 50  ? 0.4321 0.3512 0.4682 0.0768  -0.1611 -0.1070 49  LYS D CG    
1619 C  CD    . LYS B 50  ? 0.4941 0.4388 0.5403 0.1000  -0.1569 -0.1267 49  LYS D CD    
1620 C  CE    . LYS B 50  ? 0.5326 0.4717 0.5754 0.1183  -0.1622 -0.1510 49  LYS D CE    
1621 N  NZ    . LYS B 50  ? 0.5732 0.5351 0.6294 0.1439  -0.1625 -0.1714 49  LYS D NZ    
1622 N  N     . GLY B 51  ? 0.4473 0.3210 0.4630 0.0259  -0.1680 -0.0665 50  GLY D N     
1623 C  CA    . GLY B 51  ? 0.4664 0.3074 0.4825 0.0181  -0.1843 -0.0638 50  GLY D CA    
1624 C  C     . GLY B 51  ? 0.4654 0.3008 0.4765 -0.0062 -0.1834 -0.0411 50  GLY D C     
1625 O  O     . GLY B 51  ? 0.4962 0.3100 0.5083 -0.0157 -0.1943 -0.0382 50  GLY D O     
1626 N  N     . SER B 52  ? 0.4720 0.3289 0.4785 -0.0166 -0.1705 -0.0264 51  SER D N     
1627 C  CA    . SER B 52  ? 0.4634 0.3196 0.4649 -0.0384 -0.1689 -0.0059 51  SER D CA    
1628 C  C     . SER B 52  ? 0.4387 0.3117 0.4308 -0.0461 -0.1541 -0.0085 51  SER D C     
1629 O  O     . SER B 52  ? 0.4183 0.3052 0.4061 -0.0352 -0.1436 -0.0233 51  SER D O     
1630 C  CB    . SER B 52  ? 0.4242 0.2965 0.4238 -0.0452 -0.1632 0.0092  51  SER D CB    
1631 O  OG    . SER B 52  ? 0.3995 0.3018 0.3948 -0.0407 -0.1444 0.0019  51  SER D OG    
1632 N  N     . CYS B 53  ? 0.3982 0.2723 0.3875 -0.0644 -0.1533 0.0068  52  CYS D N     
1633 C  CA    . CYS B 53  ? 0.3909 0.2812 0.3733 -0.0704 -0.1410 0.0044  52  CYS D CA    
1634 C  C     . CYS B 53  ? 0.3991 0.3150 0.3747 -0.0805 -0.1248 0.0153  52  CYS D C     
1635 O  O     . CYS B 53  ? 0.3859 0.3071 0.3611 -0.0870 -0.1244 0.0271  52  CYS D O     
1636 C  CB    . CYS B 53  ? 0.4662 0.3417 0.4529 -0.0823 -0.1524 0.0086  52  CYS D CB    
1637 S  SG    . CYS B 53  ? 0.6056 0.4794 0.5961 -0.1056 -0.1578 0.0347  52  CYS D SG    
1638 N  N     . PHE B 54  ? 0.3517 0.2838 0.3215 -0.0803 -0.1121 0.0102  53  PHE D N     
1639 C  CA    . PHE B 54  ? 0.3719 0.3253 0.3367 -0.0902 -0.0988 0.0190  53  PHE D CA    
1640 C  C     . PHE B 54  ? 0.3736 0.3271 0.3413 -0.1050 -0.1045 0.0294  53  PHE D C     
1641 O  O     . PHE B 54  ? 0.3892 0.3420 0.3584 -0.1051 -0.1065 0.0239  53  PHE D O     
1642 C  CB    . PHE B 54  ? 0.3446 0.3139 0.3033 -0.0826 -0.0833 0.0102  53  PHE D CB    
1643 C  CG    . PHE B 54  ? 0.3109 0.2874 0.2683 -0.0736 -0.0738 0.0046  53  PHE D CG    
1644 C  CD1   . PHE B 54  ? 0.3382 0.3086 0.2976 -0.0606 -0.0763 -0.0057 53  PHE D CD1   
1645 C  CD2   . PHE B 54  ? 0.3322 0.3237 0.2877 -0.0785 -0.0628 0.0088  53  PHE D CD2   
1646 C  CE1   . PHE B 54  ? 0.3326 0.3141 0.2938 -0.0541 -0.0670 -0.0098 53  PHE D CE1   
1647 C  CE2   . PHE B 54  ? 0.3346 0.3332 0.2918 -0.0724 -0.0550 0.0038  53  PHE D CE2   
1648 C  CZ    . PHE B 54  ? 0.3250 0.3195 0.2859 -0.0610 -0.0569 -0.0046 53  PHE D CZ    
1649 N  N     . HIS B 55  ? 0.3460 0.3029 0.3148 -0.1178 -0.1077 0.0447  54  HIS D N     
1650 C  CA    . HIS B 55  ? 0.3471 0.3041 0.3212 -0.1338 -0.1147 0.0571  54  HIS D CA    
1651 C  C     . HIS B 55  ? 0.3655 0.3519 0.3370 -0.1420 -0.1015 0.0610  54  HIS D C     
1652 O  O     . HIS B 55  ? 0.3605 0.3525 0.3372 -0.1494 -0.1025 0.0672  54  HIS D O     
1653 C  CB    . HIS B 55  ? 0.3318 0.2781 0.3085 -0.1451 -0.1259 0.0749  54  HIS D CB    
1654 C  CG    . HIS B 55  ? 0.3539 0.3180 0.3219 -0.1463 -0.1177 0.0828  54  HIS D CG    
1655 N  ND1   . HIS B 55  ? 0.3591 0.3185 0.3240 -0.1339 -0.1175 0.0761  54  HIS D ND1   
1656 C  CD2   . HIS B 55  ? 0.3543 0.3433 0.3163 -0.1583 -0.1100 0.0956  54  HIS D CD2   
1657 C  CE1   . HIS B 55  ? 0.3775 0.3570 0.3347 -0.1385 -0.1107 0.0838  54  HIS D CE1   
1658 N  NE2   . HIS B 55  ? 0.3661 0.3634 0.3203 -0.1527 -0.1062 0.0955  54  HIS D NE2   
1659 N  N     . ARG B 56  ? 0.3165 0.3211 0.2805 -0.1354 -0.0870 0.0557  55  ARG D N     
1660 C  CA    . ARG B 56  ? 0.2860 0.3181 0.2481 -0.1402 -0.0748 0.0573  55  ARG D CA    
1661 C  C     . ARG B 56  ? 0.3123 0.3502 0.2699 -0.1263 -0.0626 0.0433  55  ARG D C     
1662 O  O     . ARG B 56  ? 0.2898 0.3267 0.2426 -0.1194 -0.0567 0.0386  55  ARG D O     
1663 C  CB    . ARG B 56  ? 0.3259 0.3765 0.2830 -0.1498 -0.0704 0.0689  55  ARG D CB    
1664 C  CG    . ARG B 56  ? 0.3562 0.4381 0.3098 -0.1507 -0.0559 0.0661  55  ARG D CG    
1665 C  CD    . ARG B 56  ? 0.3512 0.4532 0.2974 -0.1594 -0.0527 0.0761  55  ARG D CD    
1666 N  NE    . ARG B 56  ? 0.3734 0.4748 0.3199 -0.1696 -0.0615 0.0929  55  ARG D NE    
1667 C  CZ    . ARG B 56  ? 0.3651 0.4724 0.3044 -0.1760 -0.0654 0.1048  55  ARG D CZ    
1668 N  NH1   . ARG B 56  ? 0.3655 0.4770 0.2968 -0.1738 -0.0627 0.1019  55  ARG D NH1   
1669 N  NH2   . ARG B 56  ? 0.3696 0.4784 0.3107 -0.1850 -0.0733 0.1202  55  ARG D NH2   
1670 N  N     . ILE B 57  ? 0.3066 0.3527 0.2665 -0.1234 -0.0590 0.0382  56  ILE D N     
1671 C  CA    . ILE B 57  ? 0.2988 0.3500 0.2544 -0.1108 -0.0479 0.0280  56  ILE D CA    
1672 C  C     . ILE B 57  ? 0.2607 0.3356 0.2191 -0.1132 -0.0406 0.0288  56  ILE D C     
1673 O  O     . ILE B 57  ? 0.2923 0.3752 0.2571 -0.1176 -0.0455 0.0309  56  ILE D O     
1674 C  CB    . ILE B 57  ? 0.3010 0.3373 0.2552 -0.1001 -0.0519 0.0197  56  ILE D CB    
1675 C  CG1   . ILE B 57  ? 0.3131 0.3293 0.2660 -0.0960 -0.0590 0.0170  56  ILE D CG1   
1676 C  CG2   . ILE B 57  ? 0.2702 0.3124 0.2192 -0.0883 -0.0405 0.0131  56  ILE D CG2   
1677 C  CD1   . ILE B 57  ? 0.3297 0.3339 0.2801 -0.0849 -0.0640 0.0072  56  ILE D CD1   
1678 N  N     . ILE B 58  ? 0.2528 0.3401 0.2079 -0.1101 -0.0297 0.0261  57  ILE D N     
1679 C  CA    . ILE B 58  ? 0.2357 0.3471 0.1942 -0.1092 -0.0220 0.0243  57  ILE D CA    
1680 C  C     . ILE B 58  ? 0.2370 0.3427 0.1927 -0.0949 -0.0136 0.0149  57  ILE D C     
1681 O  O     . ILE B 58  ? 0.2439 0.3456 0.1961 -0.0913 -0.0070 0.0104  57  ILE D O     
1682 C  CB    . ILE B 58  ? 0.2730 0.4062 0.2302 -0.1181 -0.0173 0.0284  57  ILE D CB    
1683 C  CG1   . ILE B 58  ? 0.2276 0.3629 0.1867 -0.1334 -0.0265 0.0418  57  ILE D CG1   
1684 C  CG2   . ILE B 58  ? 0.2452 0.4075 0.2068 -0.1154 -0.0089 0.0242  57  ILE D CG2   
1685 C  CD1   . ILE B 58  ? 0.2770 0.4340 0.2309 -0.1429 -0.0227 0.0489  57  ILE D CD1   
1686 N  N     . PRO B 59  ? 0.2683 0.3748 0.2265 -0.0872 -0.0144 0.0125  58  PRO D N     
1687 C  CA    . PRO B 59  ? 0.2492 0.3472 0.2042 -0.0733 -0.0078 0.0068  58  PRO D CA    
1688 C  C     . PRO B 59  ? 0.2526 0.3611 0.2097 -0.0695 0.0014  0.0017  58  PRO D C     
1689 O  O     . PRO B 59  ? 0.2615 0.3936 0.2240 -0.0726 0.0032  0.0008  58  PRO D O     
1690 C  CB    . PRO B 59  ? 0.2426 0.3470 0.2004 -0.0673 -0.0126 0.0070  58  PRO D CB    
1691 C  CG    . PRO B 59  ? 0.2690 0.3753 0.2304 -0.0785 -0.0235 0.0110  58  PRO D CG    
1692 C  CD    . PRO B 59  ? 0.2314 0.3455 0.1956 -0.0919 -0.0231 0.0159  58  PRO D CD    
1693 N  N     . GLY B 60  ? 0.2970 0.3888 0.2507 -0.0629 0.0071  -0.0022 59  GLY D N     
1694 C  CA    . GLY B 60  ? 0.2940 0.3903 0.2503 -0.0588 0.0144  -0.0096 59  GLY D CA    
1695 C  C     . GLY B 60  ? 0.2987 0.3979 0.2532 -0.0670 0.0161  -0.0130 59  GLY D C     
1696 O  O     . GLY B 60  ? 0.3093 0.4098 0.2654 -0.0635 0.0214  -0.0220 59  GLY D O     
1697 N  N     . PHE B 61  ? 0.2734 0.3734 0.2246 -0.0773 0.0107  -0.0069 60  PHE D N     
1698 C  CA    . PHE B 61  ? 0.2690 0.3747 0.2173 -0.0849 0.0108  -0.0087 60  PHE D CA    
1699 C  C     . PHE B 61  ? 0.2875 0.3767 0.2336 -0.0889 0.0059  -0.0046 60  PHE D C     
1700 O  O     . PHE B 61  ? 0.2705 0.3512 0.2170 -0.0879 0.0086  -0.0101 60  PHE D O     
1701 C  CB    . PHE B 61  ? 0.2749 0.4066 0.2218 -0.0941 0.0085  -0.0036 60  PHE D CB    
1702 C  CG    . PHE B 61  ? 0.2910 0.4467 0.2412 -0.0898 0.0146  -0.0096 60  PHE D CG    
1703 C  CD1   . PHE B 61  ? 0.3067 0.4760 0.2549 -0.0870 0.0205  -0.0206 60  PHE D CD1   
1704 C  CD2   . PHE B 61  ? 0.2714 0.4375 0.2280 -0.0873 0.0138  -0.0063 60  PHE D CD2   
1705 C  CE1   . PHE B 61  ? 0.3060 0.5000 0.2579 -0.0809 0.0261  -0.0284 60  PHE D CE1   
1706 C  CE2   . PHE B 61  ? 0.2901 0.4828 0.2520 -0.0818 0.0194  -0.0128 60  PHE D CE2   
1707 C  CZ    . PHE B 61  ? 0.3277 0.5342 0.2873 -0.0776 0.0261  -0.0245 60  PHE D CZ    
1708 N  N     . MET B 62  ? 0.2744 0.3594 0.2197 -0.0935 -0.0020 0.0039  61  MET D N     
1709 C  CA    . MET B 62  ? 0.2611 0.3324 0.2054 -0.0954 -0.0073 0.0062  61  MET D CA    
1710 C  C     . MET B 62  ? 0.2780 0.3403 0.2228 -0.0976 -0.0172 0.0131  61  MET D C     
1711 O  O     . MET B 62  ? 0.2790 0.3472 0.2253 -0.1010 -0.0211 0.0176  61  MET D O     
1712 C  CB    . MET B 62  ? 0.2607 0.3409 0.2028 -0.1020 -0.0087 0.0061  61  MET D CB    
1713 C  CG    . MET B 62  ? 0.3517 0.4542 0.2897 -0.1103 -0.0098 0.0110  61  MET D CG    
1714 S  SD    . MET B 62  ? 0.3233 0.4353 0.2624 -0.1187 -0.0159 0.0239  61  MET D SD    
1715 C  CE    . MET B 62  ? 0.3206 0.4095 0.2595 -0.1210 -0.0280 0.0309  61  MET D CE    
1716 N  N     . CYS B 63  ? 0.2577 0.3062 0.2031 -0.0947 -0.0215 0.0123  62  CYS D N     
1717 C  CA    . CYS B 63  ? 0.2588 0.2951 0.2055 -0.0948 -0.0325 0.0158  62  CYS D CA    
1718 C  C     . CYS B 63  ? 0.2759 0.3102 0.2234 -0.0999 -0.0398 0.0204  62  CYS D C     
1719 O  O     . CYS B 63  ? 0.2939 0.3303 0.2422 -0.0974 -0.0364 0.0165  62  CYS D O     
1720 C  CB    . CYS B 63  ? 0.2689 0.2932 0.2156 -0.0840 -0.0315 0.0092  62  CYS D CB    
1721 S  SG    . CYS B 63  ? 0.3061 0.3323 0.2491 -0.0762 -0.0238 0.0056  62  CYS D SG    
1722 N  N     . GLN B 64  ? 0.2743 0.3039 0.2229 -0.1069 -0.0509 0.0292  63  GLN D N     
1723 C  CA    . GLN B 64  ? 0.3225 0.3501 0.2708 -0.1114 -0.0589 0.0363  63  GLN D CA    
1724 C  C     . GLN B 64  ? 0.3284 0.3342 0.2816 -0.1088 -0.0731 0.0389  63  GLN D C     
1725 O  O     . GLN B 64  ? 0.3259 0.3221 0.2818 -0.1106 -0.0787 0.0397  63  GLN D O     
1726 C  CB    . GLN B 64  ? 0.2714 0.3157 0.2153 -0.1241 -0.0590 0.0479  63  GLN D CB    
1727 C  CG    . GLN B 64  ? 0.2979 0.3414 0.2390 -0.1300 -0.0687 0.0593  63  GLN D CG    
1728 C  CD    . GLN B 64  ? 0.3590 0.4241 0.2930 -0.1430 -0.0674 0.0723  63  GLN D CD    
1729 O  OE1   . GLN B 64  ? 0.3272 0.4131 0.2587 -0.1460 -0.0567 0.0692  63  GLN D OE1   
1730 N  NE2   . GLN B 64  ? 0.3324 0.3945 0.2630 -0.1499 -0.0783 0.0875  63  GLN D NE2   
1731 N  N     . GLY B 65  ? 0.3319 0.3301 0.2876 -0.1037 -0.0798 0.0385  64  GLY D N     
1732 C  CA    . GLY B 65  ? 0.3455 0.3217 0.3071 -0.0994 -0.0951 0.0401  64  GLY D CA    
1733 C  C     . GLY B 65  ? 0.3729 0.3467 0.3361 -0.0982 -0.1041 0.0466  64  GLY D C     
1734 O  O     . GLY B 65  ? 0.3487 0.3380 0.3063 -0.1057 -0.1014 0.0548  64  GLY D O     
1735 N  N     . GLY B 66  ? 0.3877 0.3428 0.3583 -0.0881 -0.1161 0.0425  65  GLY D N     
1736 C  CA    . GLY B 66  ? 0.3486 0.3026 0.3231 -0.0824 -0.1251 0.0458  65  GLY D CA    
1737 C  C     . GLY B 66  ? 0.3989 0.3317 0.3755 -0.0867 -0.1438 0.0611  65  GLY D C     
1738 O  O     . GLY B 66  ? 0.4696 0.4012 0.4488 -0.0816 -0.1531 0.0660  65  GLY D O     
1739 N  N     . ASP B 67  ? 0.4397 0.3561 0.4160 -0.0968 -0.1504 0.0702  66  ASP D N     
1740 C  CA    . ASP B 67  ? 0.4732 0.3668 0.4524 -0.1036 -0.1689 0.0884  66  ASP D CA    
1741 C  C     . ASP B 67  ? 0.5152 0.3755 0.5065 -0.0909 -0.1849 0.0790  66  ASP D C     
1742 O  O     . ASP B 67  ? 0.5130 0.3539 0.5092 -0.0947 -0.1912 0.0763  66  ASP D O     
1743 C  CB    . ASP B 67  ? 0.4771 0.3725 0.4518 -0.1240 -0.1683 0.1060  66  ASP D CB    
1744 C  CG    . ASP B 67  ? 0.5400 0.4096 0.5185 -0.1337 -0.1877 0.1283  66  ASP D CG    
1745 O  OD1   . ASP B 67  ? 0.5402 0.3889 0.5240 -0.1228 -0.2024 0.1299  66  ASP D OD1   
1746 O  OD2   . ASP B 67  ? 0.5599 0.4301 0.5375 -0.1521 -0.1886 0.1446  66  ASP D OD2   
1747 N  N     . PHE B 68  ? 0.5068 0.3617 0.5039 -0.0752 -0.1928 0.0729  67  PHE D N     
1748 C  CA    . PHE B 68  ? 0.5394 0.3654 0.5488 -0.0591 -0.2083 0.0608  67  PHE D CA    
1749 C  C     . PHE B 68  ? 0.5689 0.3620 0.5848 -0.0612 -0.2315 0.0783  67  PHE D C     
1750 O  O     . PHE B 68  ? 0.6053 0.3698 0.6330 -0.0468 -0.2473 0.0680  67  PHE D O     
1751 C  CB    . PHE B 68  ? 0.5041 0.3471 0.5192 -0.0382 -0.2026 0.0413  67  PHE D CB    
1752 C  CG    . PHE B 68  ? 0.5109 0.3707 0.5258 -0.0358 -0.2040 0.0503  67  PHE D CG    
1753 C  CD1   . PHE B 68  ? 0.5193 0.3588 0.5410 -0.0292 -0.2241 0.0608  67  PHE D CD1   
1754 C  CD2   . PHE B 68  ? 0.5085 0.4043 0.5171 -0.0395 -0.1862 0.0476  67  PHE D CD2   
1755 C  CE1   . PHE B 68  ? 0.5469 0.4049 0.5680 -0.0261 -0.2267 0.0693  67  PHE D CE1   
1756 C  CE2   . PHE B 68  ? 0.4996 0.4133 0.5085 -0.0375 -0.1888 0.0541  67  PHE D CE2   
1757 C  CZ    . PHE B 68  ? 0.4977 0.3939 0.5124 -0.0305 -0.2093 0.0653  67  PHE D CZ    
1758 N  N     . THR B 69  ? 0.5663 0.3625 0.5746 -0.0781 -0.2346 0.1046  68  THR D N     
1759 C  CA    . THR B 69  ? 0.5772 0.3399 0.5908 -0.0817 -0.2572 0.1254  68  THR D CA    
1760 C  C     . THR B 69  ? 0.6629 0.4008 0.6791 -0.1015 -0.2650 0.1403  68  THR D C     
1761 O  O     . THR B 69  ? 0.6518 0.3626 0.6804 -0.0987 -0.2805 0.1401  68  THR D O     
1762 C  CB    . THR B 69  ? 0.6256 0.4044 0.6291 -0.0878 -0.2597 0.1492  68  THR D CB    
1763 O  OG1   . THR B 69  ? 0.6386 0.4458 0.6273 -0.1092 -0.2450 0.1646  68  THR D OG1   
1764 C  CG2   . THR B 69  ? 0.5796 0.3830 0.5838 -0.0686 -0.2552 0.1349  68  THR D CG2   
1765 N  N     . ARG B 70  ? 0.6338 0.3957 0.6418 -0.1193 -0.2489 0.1447  69  ARG D N     
1766 C  CA    . ARG B 70  ? 0.6189 0.3797 0.6321 -0.1355 -0.2492 0.1516  69  ARG D CA    
1767 C  C     . ARG B 70  ? 0.6320 0.3951 0.6481 -0.1348 -0.2407 0.1321  69  ARG D C     
1768 O  O     . ARG B 70  ? 0.6808 0.4362 0.7047 -0.1406 -0.2452 0.1319  69  ARG D O     
1769 C  CB    . ARG B 70  ? 0.5979 0.3931 0.6005 -0.1553 -0.2373 0.1735  69  ARG D CB    
1770 C  CG    . ARG B 70  ? 0.6989 0.5002 0.6959 -0.1570 -0.2427 0.1927  69  ARG D CG    
1771 C  CD    . ARG B 70  ? 0.7400 0.5689 0.7317 -0.1772 -0.2353 0.2136  69  ARG D CD    
1772 N  NE    . ARG B 70  ? 0.7333 0.5719 0.7183 -0.1801 -0.2383 0.2318  69  ARG D NE    
1773 C  CZ    . ARG B 70  ? 0.7206 0.5977 0.6925 -0.1899 -0.2249 0.2430  69  ARG D CZ    
1774 N  NH1   . ARG B 70  ? 0.6817 0.5918 0.6470 -0.1982 -0.2077 0.2382  69  ARG D NH1   
1775 N  NH2   . ARG B 70  ? 0.7486 0.6319 0.7137 -0.1896 -0.2290 0.2578  69  ARG D NH2   
1776 N  N     . HIS B 71  ? 0.5797 0.3589 0.5900 -0.1264 -0.2274 0.1143  70  HIS D N     
1777 C  CA    . HIS B 71  ? 0.6507 0.4398 0.6618 -0.1251 -0.2170 0.0950  70  HIS D CA    
1778 C  C     . HIS B 71  ? 0.6202 0.4300 0.6288 -0.1423 -0.2073 0.1070  70  HIS D C     
1779 O  O     . HIS B 71  ? 0.6043 0.4114 0.6182 -0.1415 -0.2067 0.0970  70  HIS D O     
1780 C  CB    . HIS B 71  ? 0.6381 0.3967 0.6604 -0.1104 -0.2309 0.0746  70  HIS D CB    
1781 C  CG    . HIS B 71  ? 0.6686 0.4148 0.6942 -0.0876 -0.2380 0.0600  70  HIS D CG    
1782 N  ND1   . HIS B 71  ? 0.6554 0.4224 0.6769 -0.0690 -0.2250 0.0371  70  HIS D ND1   
1783 C  CD2   . HIS B 71  ? 0.6767 0.3958 0.7103 -0.0790 -0.2559 0.0656  70  HIS D CD2   
1784 C  CE1   . HIS B 71  ? 0.6143 0.3709 0.6420 -0.0502 -0.2338 0.0281  70  HIS D CE1   
1785 N  NE2   . HIS B 71  ? 0.7080 0.4351 0.7432 -0.0548 -0.2530 0.0445  70  HIS D NE2   
1786 N  N     . ASN B 72  ? 0.5524 0.3864 0.5529 -0.1561 -0.1994 0.1276  71  ASN D N     
1787 C  CA    . ASN B 72  ? 0.6004 0.4605 0.5987 -0.1692 -0.1882 0.1356  71  ASN D CA    
1788 C  C     . ASN B 72  ? 0.5768 0.4765 0.5623 -0.1762 -0.1701 0.1422  71  ASN D C     
1789 O  O     . ASN B 72  ? 0.5564 0.4808 0.5402 -0.1868 -0.1618 0.1509  71  ASN D O     
1790 C  CB    . ASN B 72  ? 0.6144 0.4661 0.6199 -0.1811 -0.1995 0.1546  71  ASN D CB    
1791 C  CG    . ASN B 72  ? 0.6433 0.4958 0.6443 -0.1862 -0.2062 0.1743  71  ASN D CG    
1792 O  OD1   . ASN B 72  ? 0.6176 0.4889 0.6073 -0.1847 -0.1980 0.1770  71  ASN D OD1   
1793 N  ND2   . ASN B 72  ? 0.6494 0.4841 0.6592 -0.1931 -0.2205 0.1885  71  ASN D ND2   
1794 N  N     . GLY B 73  ? 0.5416 0.4494 0.5192 -0.1709 -0.1644 0.1379  72  GLY D N     
1795 C  CA    . GLY B 73  ? 0.4612 0.4067 0.4271 -0.1760 -0.1472 0.1403  72  GLY D CA    
1796 C  C     . GLY B 73  ? 0.4991 0.4602 0.4553 -0.1831 -0.1483 0.1589  72  GLY D C     
1797 O  O     . GLY B 73  ? 0.4571 0.4504 0.4025 -0.1851 -0.1346 0.1581  72  GLY D O     
1798 N  N     . THR B 74  ? 0.4701 0.4116 0.4305 -0.1854 -0.1641 0.1735  73  THR D N     
1799 C  CA    . THR B 74  ? 0.5496 0.5082 0.5023 -0.1906 -0.1653 0.1894  73  THR D CA    
1800 C  C     . THR B 74  ? 0.5299 0.4689 0.4802 -0.1796 -0.1768 0.1916  73  THR D C     
1801 O  O     . THR B 74  ? 0.5234 0.4778 0.4668 -0.1812 -0.1771 0.2024  73  THR D O     
1802 C  CB    . THR B 74  ? 0.5615 0.5192 0.5214 -0.2028 -0.1732 0.2071  73  THR D CB    
1803 O  OG1   . THR B 74  ? 0.6218 0.5373 0.5939 -0.1992 -0.1924 0.2106  73  THR D OG1   
1804 C  CG2   . THR B 74  ? 0.5432 0.5195 0.5067 -0.2114 -0.1638 0.2051  73  THR D CG2   
1805 N  N     . GLY B 75  ? 0.5549 0.4618 0.5113 -0.1666 -0.1868 0.1809  74  GLY D N     
1806 C  CA    . GLY B 75  ? 0.5460 0.4365 0.5032 -0.1528 -0.2004 0.1825  74  GLY D CA    
1807 C  C     . GLY B 75  ? 0.5163 0.4249 0.4721 -0.1351 -0.1910 0.1595  74  GLY D C     
1808 O  O     . GLY B 75  ? 0.5053 0.4449 0.4537 -0.1364 -0.1732 0.1486  74  GLY D O     
1809 N  N     . GLY B 76  ? 0.5060 0.3954 0.4711 -0.1181 -0.2033 0.1514  75  GLY D N     
1810 C  CA    . GLY B 76  ? 0.5151 0.4230 0.4826 -0.1019 -0.1963 0.1317  75  GLY D CA    
1811 C  C     . GLY B 76  ? 0.5242 0.4433 0.4869 -0.0976 -0.2054 0.1426  75  GLY D C     
1812 O  O     . GLY B 76  ? 0.5737 0.4943 0.5259 -0.1088 -0.2132 0.1665  75  GLY D O     
1813 N  N     . LYS B 77  ? 0.5175 0.4476 0.4883 -0.0811 -0.2047 0.1253  76  LYS D N     
1814 C  CA    . LYS B 77  ? 0.4941 0.4383 0.4626 -0.0750 -0.2144 0.1327  76  LYS D CA    
1815 C  C     . LYS B 77  ? 0.5047 0.4735 0.4829 -0.0618 -0.2054 0.1089  76  LYS D C     
1816 O  O     . LYS B 77  ? 0.4932 0.4586 0.4827 -0.0533 -0.1970 0.0893  76  LYS D O     
1817 C  CB    . LYS B 77  ? 0.5530 0.4655 0.5296 -0.0654 -0.2386 0.1464  76  LYS D CB    
1818 C  CG    . LYS B 77  ? 0.5810 0.4676 0.5779 -0.0461 -0.2464 0.1276  76  LYS D CG    
1819 C  CD    . LYS B 77  ? 0.6207 0.4791 0.6275 -0.0327 -0.2706 0.1379  76  LYS D CD    
1820 C  CE    . LYS B 77  ? 0.6029 0.4247 0.6272 -0.0175 -0.2823 0.1236  76  LYS D CE    
1821 N  NZ    . LYS B 77  ? 0.7012 0.5012 0.7382 -0.0010 -0.2997 0.1249  76  LYS D NZ    
1822 N  N     . SER B 78  ? 0.5106 0.5056 0.4848 -0.0603 -0.2077 0.1110  77  SER D N     
1823 C  CA    . SER B 78  ? 0.5121 0.5332 0.4981 -0.0503 -0.1997 0.0894  77  SER D CA    
1824 C  C     . SER B 78  ? 0.5304 0.5458 0.5338 -0.0310 -0.2160 0.0853  77  SER D C     
1825 O  O     . SER B 78  ? 0.5348 0.5245 0.5393 -0.0250 -0.2346 0.0999  77  SER D O     
1826 C  CB    . SER B 78  ? 0.4763 0.5326 0.4508 -0.0597 -0.1924 0.0890  77  SER D CB    
1827 O  OG    . SER B 78  ? 0.5093 0.5733 0.4775 -0.0572 -0.2081 0.1035  77  SER D OG    
1828 N  N     . ILE B 79  ? 0.4898 0.5294 0.5086 -0.0210 -0.2093 0.0653  78  ILE D N     
1829 C  CA    . ILE B 79  ? 0.5042 0.5474 0.5412 -0.0019 -0.2247 0.0605  78  ILE D CA    
1830 C  C     . ILE B 79  ? 0.5222 0.5811 0.5527 -0.0021 -0.2399 0.0749  78  ILE D C     
1831 O  O     . ILE B 79  ? 0.5586 0.6187 0.6025 0.0143  -0.2567 0.0755  78  ILE D O     
1832 C  CB    . ILE B 79  ? 0.4746 0.5442 0.5322 0.0077  -0.2120 0.0356  78  ILE D CB    
1833 C  CG1   . ILE B 79  ? 0.4510 0.5570 0.5061 -0.0046 -0.1988 0.0288  78  ILE D CG1   
1834 C  CG2   . ILE B 79  ? 0.4392 0.4932 0.5004 0.0094  -0.1978 0.0230  78  ILE D CG2   
1835 C  CD1   . ILE B 79  ? 0.4220 0.5590 0.5004 0.0026  -0.1889 0.0079  78  ILE D CD1   
1836 N  N     . TYR B 80  ? 0.5266 0.5993 0.5363 -0.0190 -0.2351 0.0864  79  TYR D N     
1837 C  CA    . TYR B 80  ? 0.5316 0.6225 0.5304 -0.0192 -0.2408 0.0965  79  TYR D CA    
1838 C  C     . TYR B 80  ? 0.5523 0.6178 0.5329 -0.0244 -0.2482 0.1221  79  TYR D C     
1839 O  O     . TYR B 80  ? 0.6494 0.7293 0.6161 -0.0269 -0.2512 0.1331  79  TYR D O     
1840 C  CB    . TYR B 80  ? 0.5122 0.6373 0.4996 -0.0323 -0.2261 0.0874  79  TYR D CB    
1841 C  CG    . TYR B 80  ? 0.4764 0.6238 0.4817 -0.0328 -0.2157 0.0636  79  TYR D CG    
1842 C  CD1   . TYR B 80  ? 0.4654 0.6337 0.4947 -0.0202 -0.2226 0.0499  79  TYR D CD1   
1843 C  CD2   . TYR B 80  ? 0.4424 0.5895 0.4426 -0.0454 -0.1968 0.0547  79  TYR D CD2   
1844 C  CE1   . TYR B 80  ? 0.4561 0.6437 0.5034 -0.0213 -0.2070 0.0279  79  TYR D CE1   
1845 C  CE2   . TYR B 80  ? 0.4350 0.5977 0.4520 -0.0454 -0.1819 0.0330  79  TYR D CE2   
1846 C  CZ    . TYR B 80  ? 0.4395 0.6232 0.4801 -0.0344 -0.1869 0.0204  79  TYR D CZ    
1847 O  OH    . TYR B 80  ? 0.4156 0.6161 0.4745 -0.0361 -0.1719 0.0014  79  TYR D OH    
1848 N  N     . GLY B 81  ? 0.5989 0.6282 0.5795 -0.0274 -0.2509 0.1317  80  GLY D N     
1849 C  CA    . GLY B 81  ? 0.6664 0.6724 0.6328 -0.0356 -0.2570 0.1568  80  GLY D CA    
1850 C  C     . GLY B 81  ? 0.6417 0.6385 0.5966 -0.0544 -0.2444 0.1631  80  GLY D C     
1851 O  O     . GLY B 81  ? 0.6204 0.6179 0.5810 -0.0565 -0.2352 0.1482  80  GLY D O     
1852 N  N     . GLU B 82  ? 0.6874 0.6796 0.6269 -0.0682 -0.2431 0.1846  81  GLU D N     
1853 C  CA    . GLU B 82  ? 0.7032 0.6892 0.6346 -0.0864 -0.2317 0.1918  81  GLU D CA    
1854 C  C     . GLU B 82  ? 0.6465 0.6636 0.5712 -0.0927 -0.2129 0.1746  81  GLU D C     
1855 O  O     . GLU B 82  ? 0.6442 0.6540 0.5763 -0.0930 -0.2070 0.1616  81  GLU D O     
1856 C  CB    . GLU B 82  ? 0.7849 0.7731 0.7023 -0.1004 -0.2315 0.2165  81  GLU D CB    
1857 C  CG    . GLU B 82  ? 0.8365 0.8240 0.7490 -0.1198 -0.2197 0.2242  81  GLU D CG    
1858 C  CD    . GLU B 82  ? 0.9347 0.8892 0.8543 -0.1285 -0.2307 0.2444  81  GLU D CD    
1859 O  OE1   . GLU B 82  ? 0.9346 0.8646 0.8612 -0.1190 -0.2474 0.2531  81  GLU D OE1   
1860 O  OE2   . GLU B 82  ? 0.9819 0.9358 0.9021 -0.1444 -0.2231 0.2503  81  GLU D OE2   
1861 N  N     . LYS B 83  ? 0.5735 0.6244 0.4843 -0.0972 -0.2040 0.1737  82  LYS D N     
1862 C  CA    . LYS B 83  ? 0.5627 0.6434 0.4672 -0.1025 -0.1866 0.1562  82  LYS D CA    
1863 C  C     . LYS B 83  ? 0.5245 0.6327 0.4298 -0.0929 -0.1874 0.1406  82  LYS D C     
1864 O  O     . LYS B 83  ? 0.5043 0.6136 0.4117 -0.0831 -0.2008 0.1461  82  LYS D O     
1865 C  CB    . LYS B 83  ? 0.5827 0.6804 0.4707 -0.1181 -0.1736 0.1664  82  LYS D CB    
1866 C  CG    . LYS B 83  ? 0.7090 0.7836 0.5968 -0.1289 -0.1781 0.1897  82  LYS D CG    
1867 C  CD    . LYS B 83  ? 0.7093 0.8071 0.5844 -0.1445 -0.1661 0.2013  82  LYS D CD    
1868 C  CE    . LYS B 83  ? 0.7581 0.8339 0.6402 -0.1573 -0.1687 0.2189  82  LYS D CE    
1869 N  NZ    . LYS B 83  ? 0.7491 0.8275 0.6361 -0.1648 -0.1561 0.2084  82  LYS D NZ    
1870 N  N     . PHE B 84  ? 0.4824 0.6128 0.3876 -0.0956 -0.1734 0.1203  83  PHE D N     
1871 C  CA    . PHE B 84  ? 0.4534 0.6118 0.3598 -0.0899 -0.1726 0.1038  83  PHE D CA    
1872 C  C     . PHE B 84  ? 0.4539 0.6348 0.3495 -0.0988 -0.1556 0.0910  83  PHE D C     
1873 O  O     . PHE B 84  ? 0.4349 0.6110 0.3254 -0.1075 -0.1439 0.0923  83  PHE D O     
1874 C  CB    . PHE B 84  ? 0.4319 0.5907 0.3610 -0.0793 -0.1775 0.0860  83  PHE D CB    
1875 C  CG    . PHE B 84  ? 0.4374 0.5912 0.3774 -0.0830 -0.1652 0.0707  83  PHE D CG    
1876 C  CD1   . PHE B 84  ? 0.4398 0.5671 0.3860 -0.0826 -0.1670 0.0767  83  PHE D CD1   
1877 C  CD2   . PHE B 84  ? 0.4460 0.6198 0.3922 -0.0858 -0.1533 0.0495  83  PHE D CD2   
1878 C  CE1   . PHE B 84  ? 0.3611 0.4830 0.3169 -0.0842 -0.1539 0.0620  83  PHE D CE1   
1879 C  CE2   . PHE B 84  ? 0.3988 0.5668 0.3555 -0.0891 -0.1415 0.0367  83  PHE D CE2   
1880 C  CZ    . PHE B 84  ? 0.3513 0.4935 0.3120 -0.0875 -0.1407 0.0432  83  PHE D CZ    
1881 N  N     . GLU B 85  ? 0.4375 0.6432 0.3301 -0.0958 -0.1556 0.0783  84  GLU D N     
1882 C  CA    . GLU B 85  ? 0.4138 0.6410 0.2953 -0.1021 -0.1423 0.0658  84  GLU D CA    
1883 C  C     . GLU B 85  ? 0.3751 0.5999 0.2686 -0.1048 -0.1289 0.0449  84  GLU D C     
1884 O  O     . GLU B 85  ? 0.3866 0.6009 0.2983 -0.1011 -0.1303 0.0358  84  GLU D O     
1885 C  CB    . GLU B 85  ? 0.4529 0.7041 0.3301 -0.0972 -0.1485 0.0557  84  GLU D CB    
1886 C  CG    . GLU B 85  ? 0.4824 0.7355 0.3814 -0.0901 -0.1547 0.0381  84  GLU D CG    
1887 C  CD    . GLU B 85  ? 0.5860 0.8263 0.4984 -0.0807 -0.1703 0.0488  84  GLU D CD    
1888 O  OE1   . GLU B 85  ? 0.5521 0.7972 0.4860 -0.0749 -0.1744 0.0345  84  GLU D OE1   
1889 O  OE2   . GLU B 85  ? 0.6397 0.8676 0.5425 -0.0785 -0.1793 0.0712  84  GLU D OE2   
1890 N  N     . ASP B 86  ? 0.3526 0.5885 0.2363 -0.1107 -0.1157 0.0369  85  ASP D N     
1891 C  CA    . ASP B 86  ? 0.3949 0.6300 0.2888 -0.1122 -0.1037 0.0156  85  ASP D CA    
1892 C  C     . ASP B 86  ? 0.3883 0.6330 0.2954 -0.1080 -0.1077 -0.0035 85  ASP D C     
1893 O  O     . ASP B 86  ? 0.4072 0.6702 0.3069 -0.1064 -0.1121 -0.0091 85  ASP D O     
1894 C  CB    . ASP B 86  ? 0.4021 0.6502 0.2833 -0.1170 -0.0910 0.0096  85  ASP D CB    
1895 C  CG    . ASP B 86  ? 0.3862 0.6291 0.2577 -0.1228 -0.0856 0.0280  85  ASP D CG    
1896 O  OD1   . ASP B 86  ? 0.3791 0.6014 0.2580 -0.1243 -0.0857 0.0352  85  ASP D OD1   
1897 O  OD2   . ASP B 86  ? 0.3867 0.6482 0.2442 -0.1262 -0.0814 0.0345  85  ASP D OD2   
1898 N  N     . GLU B 87  ? 0.3752 0.6089 0.3028 -0.1065 -0.1068 -0.0129 86  GLU D N     
1899 C  CA    . GLU B 87  ? 0.3289 0.5730 0.2729 -0.1037 -0.1119 -0.0280 86  GLU D CA    
1900 C  C     . GLU B 87  ? 0.3543 0.6072 0.2988 -0.1074 -0.1035 -0.0479 86  GLU D C     
1901 O  O     . GLU B 87  ? 0.3397 0.6078 0.2860 -0.1062 -0.1098 -0.0578 86  GLU D O     
1902 C  CB    . GLU B 87  ? 0.3187 0.5523 0.2866 -0.1017 -0.1120 -0.0314 86  GLU D CB    
1903 C  CG    . GLU B 87  ? 0.2920 0.5385 0.2820 -0.0997 -0.1168 -0.0451 86  GLU D CG    
1904 C  CD    . GLU B 87  ? 0.3310 0.5726 0.3442 -0.0969 -0.1169 -0.0451 86  GLU D CD    
1905 O  OE1   . GLU B 87  ? 0.3542 0.5800 0.3661 -0.0972 -0.1112 -0.0380 86  GLU D OE1   
1906 O  OE2   . GLU B 87  ? 0.3184 0.5742 0.3511 -0.0940 -0.1229 -0.0523 86  GLU D OE2   
1907 N  N     . ASN B 88  ? 0.3399 0.5823 0.2844 -0.1115 -0.0905 -0.0547 87  ASN D N     
1908 C  CA    . ASN B 88  ? 0.3216 0.5695 0.2643 -0.1139 -0.0832 -0.0729 87  ASN D CA    
1909 C  C     . ASN B 88  ? 0.3197 0.5529 0.2610 -0.1165 -0.0704 -0.0745 87  ASN D C     
1910 O  O     . ASN B 88  ? 0.3271 0.5463 0.2706 -0.1172 -0.0674 -0.0628 87  ASN D O     
1911 C  CB    . ASN B 88  ? 0.3133 0.5625 0.2772 -0.1154 -0.0854 -0.0909 87  ASN D CB    
1912 C  CG    . ASN B 88  ? 0.3191 0.5518 0.3060 -0.1177 -0.0802 -0.0915 87  ASN D CG    
1913 O  OD1   . ASN B 88  ? 0.3269 0.5438 0.3155 -0.1200 -0.0698 -0.0919 87  ASN D OD1   
1914 N  ND2   . ASN B 88  ? 0.3080 0.5467 0.3132 -0.1168 -0.0873 -0.0915 87  ASN D ND2   
1915 N  N     . PHE B 89  ? 0.3017 0.5374 0.2409 -0.1174 -0.0636 -0.0904 88  PHE D N     
1916 C  CA    . PHE B 89  ? 0.2915 0.5135 0.2313 -0.1186 -0.0522 -0.0943 88  PHE D CA    
1917 C  C     . PHE B 89  ? 0.3432 0.5515 0.3012 -0.1205 -0.0476 -0.1131 88  PHE D C     
1918 O  O     . PHE B 89  ? 0.3097 0.5123 0.2663 -0.1197 -0.0406 -0.1247 88  PHE D O     
1919 C  CB    . PHE B 89  ? 0.3517 0.5882 0.2723 -0.1168 -0.0474 -0.0943 88  PHE D CB    
1920 C  CG    . PHE B 89  ? 0.3054 0.5537 0.2099 -0.1171 -0.0510 -0.0732 88  PHE D CG    
1921 C  CD1   . PHE B 89  ? 0.3476 0.5833 0.2511 -0.1194 -0.0489 -0.0560 88  PHE D CD1   
1922 C  CD2   . PHE B 89  ? 0.3237 0.5939 0.2148 -0.1158 -0.0572 -0.0694 88  PHE D CD2   
1923 C  CE1   . PHE B 89  ? 0.3430 0.5859 0.2340 -0.1210 -0.0532 -0.0349 88  PHE D CE1   
1924 C  CE2   . PHE B 89  ? 0.3453 0.6241 0.2228 -0.1172 -0.0609 -0.0470 88  PHE D CE2   
1925 C  CZ    . PHE B 89  ? 0.3471 0.6103 0.2256 -0.1204 -0.0589 -0.0292 88  PHE D CZ    
1926 N  N     . ILE B 90  ? 0.2919 0.4949 0.2687 -0.1229 -0.0519 -0.1160 89  ILE D N     
1927 C  CA    . ILE B 90  ? 0.3344 0.5235 0.3304 -0.1265 -0.0482 -0.1311 89  ILE D CA    
1928 C  C     . ILE B 90  ? 0.2890 0.4560 0.2901 -0.1280 -0.0375 -0.1295 89  ILE D C     
1929 O  O     . ILE B 90  ? 0.3232 0.4782 0.3287 -0.1286 -0.0328 -0.1426 89  ILE D O     
1930 C  CB    . ILE B 90  ? 0.2925 0.4831 0.3096 -0.1300 -0.0536 -0.1310 89  ILE D CB    
1931 C  CG1   . ILE B 90  ? 0.3096 0.5213 0.3232 -0.1287 -0.0649 -0.1377 89  ILE D CG1   
1932 C  CG2   . ILE B 90  ? 0.3368 0.5091 0.3764 -0.1361 -0.0479 -0.1408 89  ILE D CG2   
1933 C  CD1   . ILE B 90  ? 0.3212 0.5409 0.3539 -0.1306 -0.0718 -0.1339 89  ILE D CD1   
1934 N  N     . LEU B 91  ? 0.2893 0.4500 0.2897 -0.1279 -0.0344 -0.1139 90  LEU D N     
1935 C  CA    . LEU B 91  ? 0.2792 0.4192 0.2852 -0.1294 -0.0248 -0.1106 90  LEU D CA    
1936 C  C     . LEU B 91  ? 0.2902 0.4305 0.2776 -0.1263 -0.0207 -0.1076 90  LEU D C     
1937 O  O     . LEU B 91  ? 0.3171 0.4730 0.2877 -0.1238 -0.0247 -0.0995 90  LEU D O     
1938 C  CB    . LEU B 91  ? 0.2747 0.4097 0.2899 -0.1303 -0.0237 -0.0965 90  LEU D CB    
1939 C  CG    . LEU B 91  ? 0.2870 0.4248 0.3241 -0.1337 -0.0257 -0.0999 90  LEU D CG    
1940 C  CD1   . LEU B 91  ? 0.3240 0.4643 0.3693 -0.1325 -0.0251 -0.0872 90  LEU D CD1   
1941 C  CD2   . LEU B 91  ? 0.3367 0.4584 0.3898 -0.1391 -0.0192 -0.1097 90  LEU D CD2   
1942 N  N     . LYS B 92  ? 0.3014 0.4245 0.2928 -0.1267 -0.0127 -0.1131 91  LYS D N     
1943 C  CA    . LYS B 92  ? 0.3073 0.4312 0.2841 -0.1213 -0.0080 -0.1131 91  LYS D CA    
1944 C  C     . LYS B 92  ? 0.3176 0.4232 0.2955 -0.1169 -0.0008 -0.0972 91  LYS D C     
1945 O  O     . LYS B 92  ? 0.2895 0.3792 0.2793 -0.1181 0.0019  -0.0897 91  LYS D O     
1946 C  CB    . LYS B 92  ? 0.3141 0.4321 0.2946 -0.1191 -0.0053 -0.1340 91  LYS D CB    
1947 C  CG    . LYS B 92  ? 0.3313 0.4669 0.3089 -0.1177 -0.0117 -0.1490 91  LYS D CG    
1948 C  CD    . LYS B 92  ? 0.3526 0.5177 0.3122 -0.1161 -0.0170 -0.1399 91  LYS D CD    
1949 C  CE    . LYS B 92  ? 0.4030 0.5824 0.3633 -0.1150 -0.0243 -0.1535 91  LYS D CE    
1950 N  NZ    . LYS B 92  ? 0.4322 0.6414 0.3729 -0.1122 -0.0284 -0.1469 91  LYS D NZ    
1951 N  N     . HIS B 93  ? 0.3197 0.4311 0.2848 -0.1118 0.0021  -0.0921 92  HIS D N     
1952 C  CA    . HIS B 93  ? 0.3077 0.4050 0.2727 -0.1072 0.0074  -0.0784 92  HIS D CA    
1953 C  C     . HIS B 93  ? 0.3412 0.4189 0.3145 -0.1018 0.0144  -0.0858 92  HIS D C     
1954 O  O     . HIS B 93  ? 0.3675 0.4481 0.3359 -0.0955 0.0178  -0.0896 92  HIS D O     
1955 C  CB    . HIS B 93  ? 0.2974 0.4118 0.2480 -0.1057 0.0065  -0.0694 92  HIS D CB    
1956 C  CG    . HIS B 93  ? 0.2729 0.4033 0.2151 -0.1113 -0.0015 -0.0600 92  HIS D CG    
1957 N  ND1   . HIS B 93  ? 0.2927 0.4453 0.2263 -0.1147 -0.0064 -0.0669 92  HIS D ND1   
1958 C  CD2   . HIS B 93  ? 0.2592 0.3855 0.2002 -0.1132 -0.0067 -0.0445 92  HIS D CD2   
1959 C  CE1   . HIS B 93  ? 0.2793 0.4403 0.2064 -0.1188 -0.0142 -0.0536 92  HIS D CE1   
1960 N  NE2   . HIS B 93  ? 0.2803 0.4241 0.2129 -0.1177 -0.0148 -0.0404 92  HIS D NE2   
1961 N  N     . THR B 94  ? 0.3362 0.3943 0.3234 -0.1044 0.0165  -0.0873 93  THR D N     
1962 C  CA    . THR B 94  ? 0.3665 0.4032 0.3630 -0.1006 0.0212  -0.0952 93  THR D CA    
1963 C  C     . THR B 94  ? 0.3902 0.4099 0.3862 -0.0935 0.0270  -0.0824 93  THR D C     
1964 O  O     . THR B 94  ? 0.4156 0.4175 0.4173 -0.0880 0.0300  -0.0871 93  THR D O     
1965 C  CB    . THR B 94  ? 0.3651 0.3878 0.3784 -0.1087 0.0207  -0.1009 93  THR D CB    
1966 O  OG1   . THR B 94  ? 0.3513 0.3740 0.3692 -0.1135 0.0219  -0.0863 93  THR D OG1   
1967 C  CG2   . THR B 94  ? 0.4284 0.4667 0.4433 -0.1142 0.0140  -0.1185 93  THR D CG2   
1968 N  N     . GLY B 95  ? 0.3501 0.3741 0.3397 -0.0926 0.0274  -0.0671 94  GLY D N     
1969 C  CA    . GLY B 95  ? 0.3720 0.3820 0.3602 -0.0858 0.0318  -0.0557 94  GLY D CA    
1970 C  C     . GLY B 95  ? 0.3201 0.3352 0.3024 -0.0861 0.0308  -0.0419 94  GLY D C     
1971 O  O     . GLY B 95  ? 0.3151 0.3431 0.2948 -0.0908 0.0261  -0.0405 94  GLY D O     
1972 N  N     . PRO B 96  ? 0.3453 0.3492 0.3253 -0.0801 0.0343  -0.0320 95  PRO D N     
1973 C  CA    . PRO B 96  ? 0.3138 0.3221 0.2874 -0.0785 0.0327  -0.0215 95  PRO D CA    
1974 C  C     . PRO B 96  ? 0.3199 0.3303 0.2995 -0.0842 0.0329  -0.0197 95  PRO D C     
1975 O  O     . PRO B 96  ? 0.3812 0.3850 0.3710 -0.0888 0.0372  -0.0213 95  PRO D O     
1976 C  CB    . PRO B 96  ? 0.3102 0.3058 0.2807 -0.0706 0.0372  -0.0132 95  PRO D CB    
1977 C  CG    . PRO B 96  ? 0.3887 0.3747 0.3630 -0.0665 0.0394  -0.0184 95  PRO D CG    
1978 C  CD    . PRO B 96  ? 0.3916 0.3777 0.3748 -0.0737 0.0389  -0.0304 95  PRO D CD    
1979 N  N     . GLY B 97  ? 0.2800 0.2999 0.2551 -0.0839 0.0278  -0.0165 96  GLY D N     
1980 C  CA    . GLY B 97  ? 0.2815 0.3069 0.2631 -0.0866 0.0271  -0.0157 96  GLY D CA    
1981 C  C     . GLY B 97  ? 0.3190 0.3561 0.3054 -0.0925 0.0205  -0.0218 96  GLY D C     
1982 O  O     . GLY B 97  ? 0.2626 0.3071 0.2538 -0.0925 0.0173  -0.0210 96  GLY D O     
1983 N  N     . ILE B 98  ? 0.2781 0.3194 0.2624 -0.0962 0.0177  -0.0280 97  ILE D N     
1984 C  CA    . ILE B 98  ? 0.2784 0.3331 0.2647 -0.1015 0.0106  -0.0331 97  ILE D CA    
1985 C  C     . ILE B 98  ? 0.2476 0.3087 0.2272 -0.0995 0.0020  -0.0261 97  ILE D C     
1986 O  O     . ILE B 98  ? 0.2681 0.3266 0.2383 -0.0970 -0.0003 -0.0202 97  ILE D O     
1987 C  CB    . ILE B 98  ? 0.2667 0.3276 0.2485 -0.1044 0.0096  -0.0417 97  ILE D CB    
1988 C  CG1   . ILE B 98  ? 0.3255 0.3771 0.3179 -0.1069 0.0155  -0.0516 97  ILE D CG1   
1989 C  CG2   . ILE B 98  ? 0.2476 0.3261 0.2245 -0.1084 0.0005  -0.0429 97  ILE D CG2   
1990 C  CD1   . ILE B 98  ? 0.3295 0.3848 0.3366 -0.1140 0.0142  -0.0577 97  ILE D CD1   
1991 N  N     . LEU B 99  ? 0.2638 0.3331 0.2499 -0.1007 -0.0040 -0.0268 98  LEU D N     
1992 C  CA    . LEU B 99  ? 0.2466 0.3189 0.2283 -0.0982 -0.0143 -0.0203 98  LEU D CA    
1993 C  C     . LEU B 99  ? 0.2437 0.3294 0.2213 -0.1034 -0.0224 -0.0212 98  LEU D C     
1994 O  O     . LEU B 99  ? 0.2591 0.3554 0.2442 -0.1067 -0.0232 -0.0288 98  LEU D O     
1995 C  CB    . LEU B 99  ? 0.2467 0.3198 0.2390 -0.0929 -0.0160 -0.0203 98  LEU D CB    
1996 C  CG    . LEU B 99  ? 0.2618 0.3356 0.2538 -0.0879 -0.0285 -0.0157 98  LEU D CG    
1997 C  CD1   . LEU B 99  ? 0.2730 0.3326 0.2554 -0.0840 -0.0329 -0.0087 98  LEU D CD1   
1998 C  CD2   . LEU B 99  ? 0.2614 0.3416 0.2672 -0.0815 -0.0274 -0.0201 98  LEU D CD2   
1999 N  N     . SER B 100 ? 0.2481 0.3351 0.2138 -0.1049 -0.0286 -0.0130 99  SER D N     
2000 C  CA    . SER B 100 ? 0.2596 0.3624 0.2173 -0.1102 -0.0351 -0.0119 99  SER D CA    
2001 C  C     . SER B 100 ? 0.2800 0.3814 0.2299 -0.1110 -0.0464 0.0025  99  SER D C     
2002 O  O     . SER B 100 ? 0.2844 0.3711 0.2346 -0.1084 -0.0487 0.0101  99  SER D O     
2003 C  CB    . SER B 100 ? 0.2652 0.3766 0.2143 -0.1140 -0.0280 -0.0172 99  SER D CB    
2004 O  OG    . SER B 100 ? 0.2722 0.4033 0.2106 -0.1186 -0.0340 -0.0160 99  SER D OG    
2005 N  N     . MET B 101 ? 0.2616 0.3777 0.2040 -0.1148 -0.0546 0.0069  100 MET D N     
2006 C  CA    . MET B 101 ? 0.2602 0.3716 0.1967 -0.1159 -0.0669 0.0234  100 MET D CA    
2007 C  C     . MET B 101 ? 0.3121 0.4291 0.2353 -0.1237 -0.0654 0.0348  100 MET D C     
2008 O  O     . MET B 101 ? 0.3042 0.4414 0.2179 -0.1283 -0.0597 0.0312  100 MET D O     
2009 C  CB    . MET B 101 ? 0.2975 0.4226 0.2314 -0.1159 -0.0783 0.0267  100 MET D CB    
2010 C  CG    . MET B 101 ? 0.2765 0.3982 0.2265 -0.1077 -0.0835 0.0191  100 MET D CG    
2011 S  SD    . MET B 101 ? 0.3395 0.4356 0.3003 -0.0985 -0.0902 0.0253  100 MET D SD    
2012 C  CE    . MET B 101 ? 0.3624 0.4548 0.3164 -0.0976 -0.1106 0.0443  100 MET D CE    
2013 N  N     . ALA B 102 ? 0.3155 0.4168 0.2388 -0.1254 -0.0715 0.0485  101 ALA D N     
2014 C  CA    . ALA B 102 ? 0.2992 0.4090 0.2120 -0.1352 -0.0721 0.0629  101 ALA D CA    
2015 C  C     . ALA B 102 ? 0.3484 0.4708 0.2501 -0.1406 -0.0825 0.0775  101 ALA D C     
2016 O  O     . ALA B 102 ? 0.3170 0.4337 0.2216 -0.1354 -0.0927 0.0789  101 ALA D O     
2017 C  CB    . ALA B 102 ? 0.3085 0.3964 0.2273 -0.1372 -0.0765 0.0726  101 ALA D CB    
2018 N  N     . ASN B 103 ? 0.3271 0.4680 0.2187 -0.1494 -0.0781 0.0881  102 ASN D N     
2019 C  CA    . ASN B 103 ? 0.3631 0.5145 0.2482 -0.1528 -0.0842 0.1026  102 ASN D CA    
2020 C  C     . ASN B 103 ? 0.4169 0.5831 0.2990 -0.1637 -0.0796 0.1171  102 ASN D C     
2021 O  O     . ASN B 103 ? 0.3875 0.5600 0.2731 -0.1679 -0.0710 0.1140  102 ASN D O     
2022 C  CB    . ASN B 103 ? 0.3890 0.5626 0.2681 -0.1471 -0.0810 0.0903  102 ASN D CB    
2023 C  CG    . ASN B 103 ? 0.3901 0.5903 0.2644 -0.1478 -0.0661 0.0758  102 ASN D CG    
2024 O  OD1   . ASN B 103 ? 0.3781 0.5940 0.2495 -0.1543 -0.0594 0.0826  102 ASN D OD1   
2025 N  ND2   . ASN B 103 ? 0.3402 0.5455 0.2168 -0.1409 -0.0614 0.0543  102 ASN D ND2   
2026 N  N     . ALA B 104 ? 0.4182 0.5912 0.2958 -0.1678 -0.0864 0.1329  103 ALA D N     
2027 C  CA    . ALA B 104 ? 0.4369 0.6295 0.3133 -0.1785 -0.0830 0.1470  103 ALA D CA    
2028 C  C     . ALA B 104 ? 0.4680 0.6936 0.3328 -0.1775 -0.0781 0.1458  103 ALA D C     
2029 O  O     . ALA B 104 ? 0.4770 0.7130 0.3375 -0.1841 -0.0826 0.1638  103 ALA D O     
2030 C  CB    . ALA B 104 ? 0.4434 0.6118 0.3260 -0.1861 -0.0969 0.1700  103 ALA D CB    
2031 N  N     . GLY B 105 ? 0.4198 0.6621 0.2796 -0.1692 -0.0695 0.1244  104 GLY D N     
2032 C  CA    . GLY B 105 ? 0.4186 0.6902 0.2668 -0.1661 -0.0666 0.1194  104 GLY D CA    
2033 C  C     . GLY B 105 ? 0.4712 0.7354 0.3158 -0.1560 -0.0728 0.1069  104 GLY D C     
2034 O  O     . GLY B 105 ? 0.4088 0.6464 0.2609 -0.1516 -0.0797 0.1037  104 GLY D O     
2035 N  N     . PRO B 106 ? 0.4524 0.7418 0.2865 -0.1520 -0.0715 0.0988  105 PRO D N     
2036 C  CA    . PRO B 106 ? 0.4051 0.6903 0.2382 -0.1428 -0.0786 0.0851  105 PRO D CA    
2037 C  C     . PRO B 106 ? 0.4315 0.6952 0.2664 -0.1407 -0.0943 0.1012  105 PRO D C     
2038 O  O     . PRO B 106 ? 0.4714 0.7330 0.3010 -0.1455 -0.1012 0.1240  105 PRO D O     
2039 C  CB    . PRO B 106 ? 0.4793 0.7979 0.2992 -0.1403 -0.0756 0.0767  105 PRO D CB    
2040 C  CG    . PRO B 106 ? 0.4587 0.7999 0.2755 -0.1456 -0.0630 0.0768  105 PRO D CG    
2041 C  CD    . PRO B 106 ? 0.4440 0.7688 0.2686 -0.1546 -0.0629 0.0975  105 PRO D CD    
2042 N  N     . ASN B 107 ? 0.4151 0.6655 0.2590 -0.1328 -0.1005 0.0880  106 ASN D N     
2043 C  CA    . ASN B 107 ? 0.4184 0.6519 0.2674 -0.1270 -0.1163 0.0973  106 ASN D CA    
2044 C  C     . ASN B 107 ? 0.4507 0.6574 0.3040 -0.1310 -0.1240 0.1204  106 ASN D C     
2045 O  O     . ASN B 107 ? 0.4965 0.6951 0.3468 -0.1294 -0.1367 0.1384  106 ASN D O     
2046 C  CB    . ASN B 107 ? 0.4664 0.7198 0.3037 -0.1228 -0.1247 0.1007  106 ASN D CB    
2047 C  CG    . ASN B 107 ? 0.4199 0.6980 0.2536 -0.1197 -0.1180 0.0767  106 ASN D CG    
2048 O  OD1   . ASN B 107 ? 0.4649 0.7388 0.3115 -0.1157 -0.1157 0.0556  106 ASN D OD1   
2049 N  ND2   . ASN B 107 ? 0.5156 0.8196 0.3332 -0.1220 -0.1142 0.0787  106 ASN D ND2   
2050 N  N     . THR B 108 ? 0.4380 0.6288 0.2993 -0.1356 -0.1174 0.1191  107 THR D N     
2051 C  CA    . THR B 108 ? 0.4562 0.6174 0.3248 -0.1392 -0.1257 0.1369  107 THR D CA    
2052 C  C     . THR B 108 ? 0.4417 0.5807 0.3241 -0.1339 -0.1268 0.1246  107 THR D C     
2053 O  O     . THR B 108 ? 0.4638 0.5840 0.3513 -0.1388 -0.1262 0.1303  107 THR D O     
2054 C  CB    . THR B 108 ? 0.4381 0.6031 0.3032 -0.1523 -0.1185 0.1515  107 THR D CB    
2055 O  OG1   . THR B 108 ? 0.4438 0.6228 0.3096 -0.1550 -0.1029 0.1357  107 THR D OG1   
2056 C  CG2   . THR B 108 ? 0.4680 0.6554 0.3210 -0.1581 -0.1187 0.1668  107 THR D CG2   
2057 N  N     . ASN B 109 ? 0.4053 0.5475 0.2954 -0.1242 -0.1284 0.1065  108 ASN D N     
2058 C  CA    . ASN B 109 ? 0.3917 0.5154 0.2965 -0.1191 -0.1294 0.0953  108 ASN D CA    
2059 C  C     . ASN B 109 ? 0.4227 0.5190 0.3366 -0.1129 -0.1465 0.1076  108 ASN D C     
2060 O  O     . ASN B 109 ? 0.4848 0.5804 0.3996 -0.1066 -0.1588 0.1152  108 ASN D O     
2061 C  CB    . ASN B 109 ? 0.3831 0.5206 0.2979 -0.1121 -0.1252 0.0725  108 ASN D CB    
2062 C  CG    . ASN B 109 ? 0.3808 0.5401 0.2888 -0.1167 -0.1103 0.0583  108 ASN D CG    
2063 O  OD1   . ASN B 109 ? 0.3786 0.5356 0.2870 -0.1207 -0.0984 0.0506  108 ASN D OD1   
2064 N  ND2   . ASN B 109 ? 0.3810 0.5612 0.2820 -0.1154 -0.1117 0.0549  108 ASN D ND2   
2065 N  N     . GLY B 110 ? 0.4058 0.4785 0.3278 -0.1130 -0.1474 0.1073  109 GLY D N     
2066 C  CA    . GLY B 110 ? 0.4339 0.4770 0.3687 -0.1033 -0.1618 0.1124  109 GLY D CA    
2067 C  C     . GLY B 110 ? 0.3817 0.4149 0.3333 -0.0921 -0.1548 0.0910  109 GLY D C     
2068 O  O     . GLY B 110 ? 0.4067 0.4547 0.3675 -0.0836 -0.1511 0.0755  109 GLY D O     
2069 N  N     . SER B 111 ? 0.3987 0.4098 0.3544 -0.0931 -0.1522 0.0900  110 SER D N     
2070 C  CA    . SER B 111 ? 0.3970 0.4017 0.3650 -0.0830 -0.1438 0.0704  110 SER D CA    
2071 C  C     . SER B 111 ? 0.3858 0.3936 0.3491 -0.0905 -0.1279 0.0641  110 SER D C     
2072 O  O     . SER B 111 ? 0.3617 0.3726 0.3316 -0.0838 -0.1174 0.0484  110 SER D O     
2073 C  CB    . SER B 111 ? 0.3963 0.3710 0.3755 -0.0720 -0.1575 0.0698  110 SER D CB    
2074 O  OG    . SER B 111 ? 0.4326 0.3852 0.4065 -0.0818 -0.1657 0.0854  110 SER D OG    
2075 N  N     . GLN B 112 ? 0.3601 0.3698 0.3125 -0.1038 -0.1257 0.0766  111 GLN D N     
2076 C  CA    . GLN B 112 ? 0.3911 0.4045 0.3411 -0.1091 -0.1121 0.0703  111 GLN D CA    
2077 C  C     . GLN B 112 ? 0.3412 0.3776 0.2890 -0.1082 -0.0964 0.0568  111 GLN D C     
2078 O  O     . GLN B 112 ? 0.3048 0.3597 0.2479 -0.1105 -0.0953 0.0565  111 GLN D O     
2079 C  CB    . GLN B 112 ? 0.3705 0.3864 0.3118 -0.1237 -0.1128 0.0866  111 GLN D CB    
2080 C  CG    . GLN B 112 ? 0.4012 0.3900 0.3476 -0.1271 -0.1273 0.0993  111 GLN D CG    
2081 C  CD    . GLN B 112 ? 0.4164 0.4106 0.3580 -0.1433 -0.1253 0.1136  111 GLN D CD    
2082 O  OE1   . GLN B 112 ? 0.3756 0.3862 0.3150 -0.1473 -0.1121 0.1071  111 GLN D OE1   
2083 N  NE2   . GLN B 112 ? 0.4485 0.4286 0.3901 -0.1527 -0.1390 0.1340  111 GLN D NE2   
2084 N  N     . PHE B 113 ? 0.3047 0.3388 0.2560 -0.1051 -0.0852 0.0454  112 PHE D N     
2085 C  CA    . PHE B 113 ? 0.2837 0.3326 0.2357 -0.1035 -0.0709 0.0324  112 PHE D CA    
2086 C  C     . PHE B 113 ? 0.3483 0.3959 0.2975 -0.1058 -0.0606 0.0297  112 PHE D C     
2087 O  O     . PHE B 113 ? 0.3133 0.3494 0.2620 -0.1074 -0.0647 0.0354  112 PHE D O     
2088 C  CB    . PHE B 113 ? 0.2920 0.3383 0.2555 -0.0929 -0.0685 0.0204  112 PHE D CB    
2089 C  CG    . PHE B 113 ? 0.2856 0.3147 0.2537 -0.0848 -0.0699 0.0172  112 PHE D CG    
2090 C  CD1   . PHE B 113 ? 0.2930 0.3072 0.2655 -0.0787 -0.0836 0.0206  112 PHE D CD1   
2091 C  CD2   . PHE B 113 ? 0.3145 0.3417 0.2814 -0.0830 -0.0587 0.0111  112 PHE D CD2   
2092 C  CE1   . PHE B 113 ? 0.3249 0.3238 0.3004 -0.0708 -0.0857 0.0150  112 PHE D CE1   
2093 C  CE2   . PHE B 113 ? 0.3126 0.3272 0.2808 -0.0756 -0.0603 0.0075  112 PHE D CE2   
2094 C  CZ    . PHE B 113 ? 0.2809 0.2817 0.2535 -0.0693 -0.0738 0.0080  112 PHE D CZ    
2095 N  N     . PHE B 114 ? 0.2723 0.3307 0.2211 -0.1055 -0.0483 0.0203  113 PHE D N     
2096 C  CA    . PHE B 114 ? 0.2753 0.3312 0.2231 -0.1045 -0.0392 0.0168  113 PHE D CA    
2097 C  C     . PHE B 114 ? 0.2676 0.3234 0.2205 -0.0989 -0.0285 0.0056  113 PHE D C     
2098 O  O     . PHE B 114 ? 0.2768 0.3393 0.2340 -0.0992 -0.0264 -0.0002 113 PHE D O     
2099 C  CB    . PHE B 114 ? 0.2654 0.3356 0.2060 -0.1120 -0.0353 0.0207  113 PHE D CB    
2100 C  CG    . PHE B 114 ? 0.2751 0.3635 0.2116 -0.1150 -0.0299 0.0148  113 PHE D CG    
2101 C  CD1   . PHE B 114 ? 0.2758 0.3753 0.2073 -0.1196 -0.0370 0.0194  113 PHE D CD1   
2102 C  CD2   . PHE B 114 ? 0.2486 0.3434 0.1855 -0.1126 -0.0192 0.0046  113 PHE D CD2   
2103 C  CE1   . PHE B 114 ? 0.2954 0.4147 0.2214 -0.1220 -0.0329 0.0116  113 PHE D CE1   
2104 C  CE2   . PHE B 114 ? 0.2625 0.3734 0.1958 -0.1146 -0.0153 -0.0037 113 PHE D CE2   
2105 C  CZ    . PHE B 114 ? 0.2631 0.3873 0.1905 -0.1193 -0.0219 -0.0014 113 PHE D CZ    
2106 N  N     . ILE B 115 ? 0.2437 0.2920 0.1967 -0.0945 -0.0224 0.0036  114 ILE D N     
2107 C  CA    . ILE B 115 ? 0.2359 0.2818 0.1928 -0.0899 -0.0118 -0.0034 114 ILE D CA    
2108 C  C     . ILE B 115 ? 0.2441 0.2927 0.1974 -0.0904 -0.0049 -0.0047 114 ILE D C     
2109 O  O     . ILE B 115 ? 0.2529 0.3006 0.2024 -0.0892 -0.0063 -0.0008 114 ILE D O     
2110 C  CB    . ILE B 115 ? 0.2731 0.3091 0.2314 -0.0820 -0.0110 -0.0035 114 ILE D CB    
2111 C  CG1   . ILE B 115 ? 0.3142 0.3487 0.2771 -0.0791 -0.0194 -0.0036 114 ILE D CG1   
2112 C  CG2   . ILE B 115 ? 0.2494 0.2836 0.2108 -0.0787 0.0004  -0.0069 114 ILE D CG2   
2113 C  CD1   . ILE B 115 ? 0.2823 0.3089 0.2442 -0.0697 -0.0209 -0.0055 114 ILE D CD1   
2114 N  N     . CYS B 116 ? 0.2636 0.3164 0.2194 -0.0920 0.0015  -0.0114 115 CYS D N     
2115 C  CA    . CYS B 116 ? 0.2751 0.3300 0.2290 -0.0900 0.0075  -0.0146 115 CYS D CA    
2116 C  C     . CYS B 116 ? 0.2803 0.3226 0.2353 -0.0827 0.0129  -0.0128 115 CYS D C     
2117 O  O     . CYS B 116 ? 0.3089 0.3417 0.2674 -0.0803 0.0160  -0.0118 115 CYS D O     
2118 C  CB    . CYS B 116 ? 0.2745 0.3339 0.2318 -0.0922 0.0117  -0.0248 115 CYS D CB    
2119 S  SG    . CYS B 116 ? 0.3105 0.3893 0.2631 -0.0997 0.0054  -0.0275 115 CYS D SG    
2120 N  N     . THR B 117 ? 0.2846 0.3296 0.2366 -0.0788 0.0141  -0.0115 116 THR D N     
2121 C  CA    . THR B 117 ? 0.3062 0.3404 0.2584 -0.0707 0.0191  -0.0099 116 THR D CA    
2122 C  C     . THR B 117 ? 0.3322 0.3653 0.2878 -0.0668 0.0244  -0.0159 116 THR D C     
2123 O  O     . THR B 117 ? 0.3247 0.3490 0.2805 -0.0590 0.0275  -0.0136 116 THR D O     
2124 C  CB    . THR B 117 ? 0.3286 0.3654 0.2760 -0.0667 0.0147  -0.0042 116 THR D CB    
2125 O  OG1   . THR B 117 ? 0.2984 0.3507 0.2460 -0.0696 0.0116  -0.0047 116 THR D OG1   
2126 C  CG2   . THR B 117 ? 0.3024 0.3355 0.2472 -0.0682 0.0087  -0.0007 116 THR D CG2   
2127 N  N     . ALA B 118 ? 0.2928 0.3350 0.2507 -0.0711 0.0247  -0.0242 117 ALA D N     
2128 C  CA    . ALA B 118 ? 0.3214 0.3639 0.2833 -0.0667 0.0285  -0.0341 117 ALA D CA    
2129 C  C     . ALA B 118 ? 0.3057 0.3565 0.2688 -0.0735 0.0276  -0.0441 117 ALA D C     
2130 O  O     . ALA B 118 ? 0.2708 0.3311 0.2304 -0.0810 0.0234  -0.0410 117 ALA D O     
2131 C  CB    . ALA B 118 ? 0.3187 0.3780 0.2788 -0.0610 0.0284  -0.0354 117 ALA D CB    
2132 N  N     . LYS B 119 ? 0.3322 0.3786 0.3004 -0.0700 0.0304  -0.0566 118 LYS D N     
2133 C  CA    . LYS B 119 ? 0.3073 0.3673 0.2748 -0.0747 0.0287  -0.0695 118 LYS D CA    
2134 C  C     . LYS B 119 ? 0.3677 0.4579 0.3254 -0.0766 0.0268  -0.0687 118 LYS D C     
2135 O  O     . LYS B 119 ? 0.3571 0.4593 0.3133 -0.0707 0.0291  -0.0680 118 LYS D O     
2136 C  CB    . LYS B 119 ? 0.3448 0.3946 0.3196 -0.0683 0.0311  -0.0858 118 LYS D CB    
2137 C  CG    . LYS B 119 ? 0.3876 0.4548 0.3600 -0.0721 0.0285  -0.1026 118 LYS D CG    
2138 C  CD    . LYS B 119 ? 0.4807 0.5389 0.4604 -0.0644 0.0295  -0.1228 118 LYS D CD    
2139 C  CE    . LYS B 119 ? 0.5510 0.5759 0.5444 -0.0674 0.0289  -0.1256 118 LYS D CE    
2140 N  NZ    . LYS B 119 ? 0.6376 0.6621 0.6364 -0.0665 0.0257  -0.1500 118 LYS D NZ    
2141 N  N     . THR B 120 ? 0.3125 0.4174 0.2641 -0.0851 0.0226  -0.0679 119 THR D N     
2142 C  CA    . THR B 120 ? 0.3099 0.4450 0.2511 -0.0889 0.0209  -0.0649 119 THR D CA    
2143 C  C     . THR B 120 ? 0.3660 0.5182 0.3014 -0.0924 0.0188  -0.0773 119 THR D C     
2144 O  O     . THR B 120 ? 0.3071 0.4714 0.2349 -0.1000 0.0134  -0.0705 119 THR D O     
2145 C  CB    . THR B 120 ? 0.3019 0.4393 0.2384 -0.0963 0.0156  -0.0464 119 THR D CB    
2146 O  OG1   . THR B 120 ? 0.3095 0.4353 0.2473 -0.1011 0.0104  -0.0440 119 THR D OG1   
2147 C  CG2   . THR B 120 ? 0.2905 0.4127 0.2320 -0.0925 0.0164  -0.0363 119 THR D CG2   
2148 N  N     . GLU B 121 ? 0.3448 0.4981 0.2835 -0.0857 0.0221  -0.0964 120 GLU D N     
2149 C  CA    . GLU B 121 ? 0.3449 0.5097 0.2797 -0.0882 0.0189  -0.1123 120 GLU D CA    
2150 C  C     . GLU B 121 ? 0.3398 0.5434 0.2582 -0.0919 0.0176  -0.1108 120 GLU D C     
2151 O  O     . GLU B 121 ? 0.3857 0.6030 0.2971 -0.0954 0.0131  -0.1200 120 GLU D O     
2152 C  CB    . GLU B 121 ? 0.3901 0.5448 0.3332 -0.0794 0.0216  -0.1356 120 GLU D CB    
2153 C  CG    . GLU B 121 ? 0.3674 0.5447 0.3061 -0.0691 0.0268  -0.1465 120 GLU D CG    
2154 C  CD    . GLU B 121 ? 0.4226 0.5918 0.3671 -0.0627 0.0316  -0.1339 120 GLU D CD    
2155 O  OE1   . GLU B 121 ? 0.4329 0.5757 0.3839 -0.0652 0.0308  -0.1187 120 GLU D OE1   
2156 O  OE2   . GLU B 121 ? 0.4684 0.6601 0.4113 -0.0542 0.0360  -0.1407 120 GLU D OE2   
2157 N  N     . TRP B 122 ? 0.3836 0.6078 0.2958 -0.0915 0.0215  -0.0997 121 TRP D N     
2158 C  CA    . TRP B 122 ? 0.3724 0.6319 0.2736 -0.0956 0.0209  -0.0921 121 TRP D CA    
2159 C  C     . TRP B 122 ? 0.3603 0.6183 0.2559 -0.1061 0.0133  -0.0722 121 TRP D C     
2160 O  O     . TRP B 122 ? 0.3686 0.6502 0.2583 -0.1092 0.0114  -0.0638 121 TRP D O     
2161 C  CB    . TRP B 122 ? 0.3756 0.6578 0.2784 -0.0934 0.0270  -0.0832 121 TRP D CB    
2162 C  CG    . TRP B 122 ? 0.3630 0.6320 0.2679 -0.0990 0.0266  -0.0654 121 TRP D CG    
2163 C  CD1   . TRP B 122 ? 0.3440 0.6157 0.2469 -0.1095 0.0217  -0.0424 121 TRP D CD1   
2164 C  CD2   . TRP B 122 ? 0.3208 0.5626 0.2373 -0.0922 0.0286  -0.0672 121 TRP D CD2   
2165 N  NE1   . TRP B 122 ? 0.3297 0.5820 0.2387 -0.1106 0.0213  -0.0329 121 TRP D NE1   
2166 C  CE2   . TRP B 122 ? 0.3604 0.5936 0.2795 -0.0991 0.0252  -0.0468 121 TRP D CE2   
2167 C  CE3   . TRP B 122 ? 0.3474 0.5685 0.2743 -0.0804 0.0319  -0.0832 121 TRP D CE3   
2168 C  CZ2   . TRP B 122 ? 0.3334 0.5427 0.2630 -0.0938 0.0255  -0.0431 121 TRP D CZ2   
2169 C  CZ3   . TRP B 122 ? 0.3658 0.5621 0.3028 -0.0755 0.0324  -0.0764 121 TRP D CZ3   
2170 C  CH2   . TRP B 122 ? 0.3272 0.5189 0.2646 -0.0821 0.0292  -0.0570 121 TRP D CH2   
2171 N  N     . LEU B 123 ? 0.3117 0.5429 0.2097 -0.1107 0.0083  -0.0658 122 LEU D N     
2172 C  CA    . LEU B 123 ? 0.3280 0.5540 0.2233 -0.1178 -0.0005 -0.0504 122 LEU D CA    
2173 C  C     . LEU B 123 ? 0.3261 0.5492 0.2239 -0.1169 -0.0055 -0.0622 122 LEU D C     
2174 O  O     . LEU B 123 ? 0.3124 0.5356 0.2081 -0.1205 -0.0132 -0.0514 122 LEU D O     
2175 C  CB    . LEU B 123 ? 0.2922 0.4888 0.1970 -0.1191 -0.0034 -0.0373 122 LEU D CB    
2176 C  CG    . LEU B 123 ? 0.2654 0.4630 0.1714 -0.1194 0.0006  -0.0257 122 LEU D CG    
2177 C  CD1   . LEU B 123 ? 0.2816 0.4512 0.1967 -0.1190 -0.0030 -0.0150 122 LEU D CD1   
2178 C  CD2   . LEU B 123 ? 0.3501 0.5767 0.2440 -0.1276 -0.0011 -0.0116 122 LEU D CD2   
2179 N  N     . ASP B 124 ? 0.3135 0.5332 0.2171 -0.1116 -0.0022 -0.0844 123 ASP D N     
2180 C  CA    . ASP B 124 ? 0.3177 0.5328 0.2274 -0.1117 -0.0076 -0.0962 123 ASP D CA    
2181 C  C     . ASP B 124 ? 0.3246 0.5657 0.2238 -0.1115 -0.0120 -0.0933 123 ASP D C     
2182 O  O     . ASP B 124 ? 0.3386 0.6033 0.2288 -0.1086 -0.0079 -0.0941 123 ASP D O     
2183 C  CB    . ASP B 124 ? 0.3507 0.5551 0.2702 -0.1067 -0.0039 -0.1207 123 ASP D CB    
2184 C  CG    . ASP B 124 ? 0.3460 0.5201 0.2786 -0.1068 0.0001  -0.1230 123 ASP D CG    
2185 O  OD1   . ASP B 124 ? 0.3399 0.4996 0.2768 -0.1088 0.0004  -0.1047 123 ASP D OD1   
2186 O  OD2   . ASP B 124 ? 0.3630 0.5239 0.3051 -0.1022 0.0031  -0.1408 123 ASP D OD2   
2187 N  N     . GLY B 125 ? 0.3268 0.5652 0.2281 -0.1141 -0.0203 -0.0900 124 GLY D N     
2188 C  CA    . GLY B 125 ? 0.3391 0.6007 0.2296 -0.1138 -0.0259 -0.0863 124 GLY D CA    
2189 C  C     . GLY B 125 ? 0.3341 0.6069 0.2130 -0.1177 -0.0283 -0.0612 124 GLY D C     
2190 O  O     . GLY B 125 ? 0.3387 0.6306 0.2074 -0.1181 -0.0332 -0.0548 124 GLY D O     
2191 N  N     . LYS B 126 ? 0.3372 0.5975 0.2179 -0.1211 -0.0259 -0.0466 125 LYS D N     
2192 C  CA    . LYS B 126 ? 0.3538 0.6187 0.2269 -0.1264 -0.0295 -0.0216 125 LYS D CA    
2193 C  C     . LYS B 126 ? 0.3534 0.5927 0.2328 -0.1291 -0.0370 -0.0077 125 LYS D C     
2194 O  O     . LYS B 126 ? 0.3564 0.5949 0.2313 -0.1322 -0.0453 0.0107  125 LYS D O     
2195 C  CB    . LYS B 126 ? 0.3768 0.6544 0.2475 -0.1285 -0.0208 -0.0157 125 LYS D CB    
2196 C  CG    . LYS B 126 ? 0.4113 0.7198 0.2759 -0.1249 -0.0144 -0.0270 125 LYS D CG    
2197 C  CD    . LYS B 126 ? 0.5328 0.8520 0.4014 -0.1238 -0.0047 -0.0291 125 LYS D CD    
2198 C  CE    . LYS B 126 ? 0.5637 0.9100 0.4302 -0.1161 0.0022  -0.0488 125 LYS D CE    
2199 N  NZ    . LYS B 126 ? 0.5701 0.9096 0.4456 -0.1091 0.0099  -0.0643 125 LYS D NZ    
2200 N  N     . HIS B 127 ? 0.3072 0.5256 0.1975 -0.1275 -0.0348 -0.0161 126 HIS D N     
2201 C  CA    . HIS B 127 ? 0.3231 0.5186 0.2220 -0.1280 -0.0417 -0.0074 126 HIS D CA    
2202 C  C     . HIS B 127 ? 0.3181 0.5055 0.2302 -0.1245 -0.0439 -0.0221 126 HIS D C     
2203 O  O     . HIS B 127 ? 0.3081 0.4954 0.2263 -0.1232 -0.0372 -0.0397 126 HIS D O     
2204 C  CB    . HIS B 127 ? 0.3148 0.4956 0.2173 -0.1294 -0.0367 -0.0038 126 HIS D CB    
2205 C  CG    . HIS B 127 ? 0.3017 0.4905 0.1951 -0.1343 -0.0361 0.0130  126 HIS D CG    
2206 N  ND1   . HIS B 127 ? 0.3063 0.4832 0.1993 -0.1383 -0.0450 0.0323  126 HIS D ND1   
2207 C  CD2   . HIS B 127 ? 0.3336 0.5433 0.2208 -0.1363 -0.0282 0.0134  126 HIS D CD2   
2208 C  CE1   . HIS B 127 ? 0.3319 0.5202 0.2197 -0.1444 -0.0423 0.0451  126 HIS D CE1   
2209 N  NE2   . HIS B 127 ? 0.3362 0.5467 0.2213 -0.1431 -0.0316 0.0339  126 HIS D NE2   
2210 N  N     . VAL B 128 ? 0.2933 0.4741 0.2116 -0.1232 -0.0537 -0.0148 127 VAL D N     
2211 C  CA    . VAL B 128 ? 0.2990 0.4767 0.2331 -0.1205 -0.0559 -0.0272 127 VAL D CA    
2212 C  C     . VAL B 128 ? 0.3051 0.4646 0.2539 -0.1204 -0.0499 -0.0315 127 VAL D C     
2213 O  O     . VAL B 128 ? 0.2891 0.4345 0.2418 -0.1173 -0.0522 -0.0208 127 VAL D O     
2214 C  CB    . VAL B 128 ? 0.2929 0.4757 0.2296 -0.1176 -0.0690 -0.0189 127 VAL D CB    
2215 C  CG1   . VAL B 128 ? 0.2786 0.4627 0.2347 -0.1155 -0.0703 -0.0320 127 VAL D CG1   
2216 C  CG2   . VAL B 128 ? 0.3003 0.5016 0.2208 -0.1176 -0.0751 -0.0123 127 VAL D CG2   
2217 N  N     . VAL B 129 ? 0.2806 0.4367 0.2392 -0.1215 -0.0414 -0.0469 128 VAL D N     
2218 C  CA    . VAL B 129 ? 0.2279 0.3658 0.2016 -0.1196 -0.0338 -0.0488 128 VAL D CA    
2219 C  C     . VAL B 129 ? 0.2709 0.4127 0.2610 -0.1189 -0.0387 -0.0504 128 VAL D C     
2220 O  O     . VAL B 129 ? 0.2621 0.4177 0.2586 -0.1212 -0.0435 -0.0593 128 VAL D O     
2221 C  CB    . VAL B 129 ? 0.2790 0.4097 0.2582 -0.1217 -0.0238 -0.0622 128 VAL D CB    
2222 C  CG1   . VAL B 129 ? 0.2744 0.3874 0.2695 -0.1205 -0.0158 -0.0614 128 VAL D CG1   
2223 C  CG2   . VAL B 129 ? 0.2439 0.3727 0.2088 -0.1197 -0.0184 -0.0608 128 VAL D CG2   
2224 N  N     . PHE B 130 ? 0.2610 0.3912 0.2591 -0.1140 -0.0365 -0.0431 129 PHE D N     
2225 C  CA    . PHE B 130 ? 0.2714 0.4102 0.2866 -0.1119 -0.0406 -0.0451 129 PHE D CA    
2226 C  C     . PHE B 130 ? 0.2678 0.3975 0.2963 -0.1088 -0.0310 -0.0448 129 PHE D C     
2227 O  O     . PHE B 130 ? 0.2864 0.4274 0.3308 -0.1064 -0.0329 -0.0468 129 PHE D O     
2228 C  CB    . PHE B 130 ? 0.2720 0.4165 0.2828 -0.1059 -0.0542 -0.0359 129 PHE D CB    
2229 C  CG    . PHE B 130 ? 0.2676 0.3942 0.2704 -0.0994 -0.0552 -0.0242 129 PHE D CG    
2230 C  CD1   . PHE B 130 ? 0.2738 0.3915 0.2587 -0.1017 -0.0566 -0.0150 129 PHE D CD1   
2231 C  CD2   . PHE B 130 ? 0.2799 0.4003 0.2940 -0.0912 -0.0544 -0.0235 129 PHE D CD2   
2232 C  CE1   . PHE B 130 ? 0.2808 0.3812 0.2610 -0.0972 -0.0587 -0.0054 129 PHE D CE1   
2233 C  CE2   . PHE B 130 ? 0.2889 0.3920 0.2962 -0.0850 -0.0567 -0.0157 129 PHE D CE2   
2234 C  CZ    . PHE B 130 ? 0.2556 0.3474 0.2465 -0.0887 -0.0596 -0.0065 129 PHE D CZ    
2235 N  N     . GLY B 131 ? 0.2313 0.3448 0.2546 -0.1084 -0.0207 -0.0423 130 GLY D N     
2236 C  CA    . GLY B 131 ? 0.2492 0.3575 0.2832 -0.1060 -0.0111 -0.0409 130 GLY D CA    
2237 C  C     . GLY B 131 ? 0.2814 0.3724 0.3076 -0.1064 -0.0008 -0.0383 130 GLY D C     
2238 O  O     . GLY B 131 ? 0.2585 0.3426 0.2738 -0.1084 -0.0009 -0.0395 130 GLY D O     
2239 N  N     . LYS B 132 ? 0.2838 0.3701 0.3151 -0.1033 0.0077  -0.0343 131 LYS D N     
2240 C  CA    . LYS B 132 ? 0.2649 0.3352 0.2886 -0.1021 0.0167  -0.0299 131 LYS D CA    
2241 C  C     . LYS B 132 ? 0.3005 0.3706 0.3233 -0.0946 0.0221  -0.0234 131 LYS D C     
2242 O  O     . LYS B 132 ? 0.3206 0.4046 0.3539 -0.0926 0.0229  -0.0242 131 LYS D O     
2243 C  CB    . LYS B 132 ? 0.2772 0.3407 0.3105 -0.1104 0.0244  -0.0335 131 LYS D CB    
2244 C  CG    . LYS B 132 ? 0.3619 0.4319 0.4120 -0.1149 0.0323  -0.0310 131 LYS D CG    
2245 C  CD    . LYS B 132 ? 0.3817 0.4434 0.4457 -0.1261 0.0373  -0.0350 131 LYS D CD    
2246 C  CE    . LYS B 132 ? 0.5225 0.5668 0.5858 -0.1266 0.0482  -0.0248 131 LYS D CE    
2247 N  NZ    . LYS B 132 ? 0.6293 0.6539 0.6999 -0.1343 0.0494  -0.0296 131 LYS D NZ    
2248 N  N     . VAL B 133 ? 0.2839 0.3410 0.2935 -0.0896 0.0255  -0.0181 132 VAL D N     
2249 C  CA    . VAL B 133 ? 0.2834 0.3406 0.2888 -0.0821 0.0311  -0.0127 132 VAL D CA    
2250 C  C     . VAL B 133 ? 0.3208 0.3839 0.3379 -0.0869 0.0427  -0.0093 132 VAL D C     
2251 O  O     . VAL B 133 ? 0.3178 0.3719 0.3405 -0.0948 0.0483  -0.0075 132 VAL D O     
2252 C  CB    . VAL B 133 ? 0.2848 0.3282 0.2743 -0.0767 0.0314  -0.0081 132 VAL D CB    
2253 C  CG1   . VAL B 133 ? 0.3107 0.3559 0.2933 -0.0685 0.0382  -0.0025 132 VAL D CG1   
2254 C  CG2   . VAL B 133 ? 0.2488 0.2898 0.2297 -0.0738 0.0199  -0.0101 132 VAL D CG2   
2255 N  N     . LYS B 134 ? 0.2950 0.3743 0.3174 -0.0824 0.0462  -0.0086 133 LYS D N     
2256 C  CA    . LYS B 134 ? 0.3543 0.4440 0.3881 -0.0879 0.0585  -0.0029 133 LYS D CA    
2257 C  C     . LYS B 134 ? 0.3774 0.4641 0.3970 -0.0810 0.0670  0.0065  133 LYS D C     
2258 O  O     . LYS B 134 ? 0.4277 0.5026 0.4453 -0.0862 0.0748  0.0159  133 LYS D O     
2259 C  CB    . LYS B 134 ? 0.3330 0.4495 0.3838 -0.0878 0.0589  -0.0081 133 LYS D CB    
2260 C  CG    . LYS B 134 ? 0.4005 0.5328 0.4646 -0.0950 0.0729  -0.0007 133 LYS D CG    
2261 C  CD    . LYS B 134 ? 0.4251 0.5810 0.5154 -0.1041 0.0732  -0.0060 133 LYS D CD    
2262 C  CE    . LYS B 134 ? 0.4397 0.6223 0.5359 -0.0923 0.0688  -0.0141 133 LYS D CE    
2263 N  NZ    . LYS B 134 ? 0.4862 0.7034 0.6053 -0.0973 0.0790  -0.0130 133 LYS D NZ    
2264 N  N     . GLU B 135 ? 0.3659 0.4617 0.3749 -0.0685 0.0644  0.0038  134 GLU D N     
2265 C  CA    . GLU B 135 ? 0.3909 0.4847 0.3822 -0.0600 0.0698  0.0107  134 GLU D CA    
2266 C  C     . GLU B 135 ? 0.3237 0.4050 0.2990 -0.0503 0.0581  0.0050  134 GLU D C     
2267 O  O     . GLU B 135 ? 0.3316 0.4104 0.3101 -0.0486 0.0469  -0.0036 134 GLU D O     
2268 C  CB    . GLU B 135 ? 0.4508 0.5712 0.4425 -0.0532 0.0783  0.0114  134 GLU D CB    
2269 C  CG    . GLU B 135 ? 0.4704 0.6109 0.4826 -0.0638 0.0894  0.0160  134 GLU D CG    
2270 C  CD    . GLU B 135 ? 0.6134 0.7770 0.6210 -0.0611 0.1039  0.0256  134 GLU D CD    
2271 O  OE1   . GLU B 135 ? 0.6216 0.8145 0.6452 -0.0631 0.1109  0.0237  134 GLU D OE1   
2272 O  OE2   . GLU B 135 ? 0.6596 0.8151 0.6481 -0.0571 0.1087  0.0358  134 GLU D OE2   
2273 N  N     . GLY B 136 ? 0.3732 0.4466 0.3320 -0.0448 0.0603  0.0111  135 GLY D N     
2274 C  CA    . GLY B 136 ? 0.3202 0.3847 0.2651 -0.0362 0.0495  0.0059  135 GLY D CA    
2275 C  C     . GLY B 136 ? 0.3300 0.3763 0.2731 -0.0410 0.0427  0.0069  135 GLY D C     
2276 O  O     . GLY B 136 ? 0.3266 0.3675 0.2640 -0.0374 0.0320  0.0016  135 GLY D O     
2277 N  N     . MET B 137 ? 0.3020 0.3394 0.2510 -0.0492 0.0483  0.0129  136 MET D N     
2278 C  CA    . MET B 137 ? 0.2923 0.3164 0.2388 -0.0514 0.0428  0.0125  136 MET D CA    
2279 C  C     . MET B 137 ? 0.3346 0.3556 0.2665 -0.0426 0.0392  0.0151  136 MET D C     
2280 O  O     . MET B 137 ? 0.2772 0.2943 0.2068 -0.0424 0.0314  0.0119  136 MET D O     
2281 C  CB    . MET B 137 ? 0.3187 0.3319 0.2726 -0.0583 0.0496  0.0173  136 MET D CB    
2282 C  CG    . MET B 137 ? 0.3334 0.3382 0.2903 -0.0618 0.0445  0.0121  136 MET D CG    
2283 S  SD    . MET B 137 ? 0.3324 0.3459 0.2932 -0.0667 0.0343  0.0022  136 MET D SD    
2284 C  CE    . MET B 137 ? 0.3243 0.3356 0.2771 -0.0635 0.0286  0.0014  136 MET D CE    
2285 N  N     . ASN B 138 ? 0.3254 0.3507 0.2474 -0.0357 0.0450  0.0215  137 ASN D N     
2286 C  CA    . ASN B 138 ? 0.3415 0.3663 0.2491 -0.0267 0.0403  0.0232  137 ASN D CA    
2287 C  C     . ASN B 138 ? 0.3202 0.3494 0.2244 -0.0229 0.0283  0.0126  137 ASN D C     
2288 O  O     . ASN B 138 ? 0.3190 0.3464 0.2169 -0.0193 0.0205  0.0109  137 ASN D O     
2289 C  CB    . ASN B 138 ? 0.3630 0.3953 0.2583 -0.0197 0.0486  0.0324  137 ASN D CB    
2290 C  CG    . ASN B 138 ? 0.3685 0.4178 0.2605 -0.0151 0.0502  0.0262  137 ASN D CG    
2291 O  OD1   . ASN B 138 ? 0.3637 0.4191 0.2679 -0.0205 0.0539  0.0228  137 ASN D OD1   
2292 N  ND2   . ASN B 138 ? 0.4037 0.4619 0.2802 -0.0042 0.0454  0.0221  137 ASN D ND2   
2293 N  N     . ILE B 139 ? 0.3232 0.3575 0.2334 -0.0239 0.0255  0.0051  138 ILE D N     
2294 C  CA    . ILE B 139 ? 0.2847 0.3182 0.1938 -0.0207 0.0124  -0.0048 138 ILE D CA    
2295 C  C     . ILE B 139 ? 0.3028 0.3275 0.2199 -0.0296 0.0043  -0.0053 138 ILE D C     
2296 O  O     . ILE B 139 ? 0.3137 0.3350 0.2286 -0.0294 -0.0062 -0.0086 138 ILE D O     
2297 C  CB    . ILE B 139 ? 0.3213 0.3620 0.2352 -0.0167 0.0111  -0.0128 138 ILE D CB    
2298 C  CG1   . ILE B 139 ? 0.3458 0.4018 0.2502 -0.0068 0.0201  -0.0130 138 ILE D CG1   
2299 C  CG2   . ILE B 139 ? 0.3241 0.3575 0.2400 -0.0142 -0.0047 -0.0230 138 ILE D CG2   
2300 C  CD1   . ILE B 139 ? 0.3884 0.4466 0.2760 0.0028  0.0156  -0.0157 138 ILE D CD1   
2301 N  N     . VAL B 140 ? 0.2553 0.2783 0.1822 -0.0381 0.0087  -0.0025 139 VAL D N     
2302 C  CA    . VAL B 140 ? 0.2449 0.2643 0.1769 -0.0464 0.0027  -0.0021 139 VAL D CA    
2303 C  C     . VAL B 140 ? 0.2920 0.3111 0.2192 -0.0454 0.0029  0.0012  139 VAL D C     
2304 O  O     . VAL B 140 ? 0.2863 0.3068 0.2147 -0.0492 -0.0047 0.0008  139 VAL D O     
2305 C  CB    . VAL B 140 ? 0.2889 0.3094 0.2300 -0.0542 0.0081  -0.0013 139 VAL D CB    
2306 C  CG1   . VAL B 140 ? 0.2597 0.2812 0.2034 -0.0619 0.0028  -0.0011 139 VAL D CG1   
2307 C  CG2   . VAL B 140 ? 0.2582 0.2826 0.2063 -0.0547 0.0064  -0.0049 139 VAL D CG2   
2308 N  N     . GLU B 141 ? 0.2988 0.3170 0.2216 -0.0403 0.0114  0.0056  140 GLU D N     
2309 C  CA    . GLU B 141 ? 0.3363 0.3552 0.2552 -0.0367 0.0107  0.0085  140 GLU D CA    
2310 C  C     . GLU B 141 ? 0.3096 0.3332 0.2218 -0.0318 0.0010  0.0058  140 GLU D C     
2311 O  O     . GLU B 141 ? 0.3220 0.3504 0.2367 -0.0337 -0.0052 0.0050  140 GLU D O     
2312 C  CB    . GLU B 141 ? 0.3507 0.3647 0.2657 -0.0310 0.0202  0.0156  140 GLU D CB    
2313 C  CG    . GLU B 141 ? 0.3670 0.3732 0.2913 -0.0366 0.0282  0.0173  140 GLU D CG    
2314 C  CD    . GLU B 141 ? 0.4494 0.4474 0.3711 -0.0334 0.0376  0.0264  140 GLU D CD    
2315 O  OE1   . GLU B 141 ? 0.4240 0.4242 0.3343 -0.0255 0.0387  0.0331  140 GLU D OE1   
2316 O  OE2   . GLU B 141 ? 0.4267 0.4162 0.3577 -0.0394 0.0438  0.0276  140 GLU D OE2   
2317 N  N     . ALA B 142 ? 0.2814 0.3058 0.1861 -0.0257 -0.0007 0.0030  141 ALA D N     
2318 C  CA    . ALA B 142 ? 0.3067 0.3347 0.2048 -0.0205 -0.0113 -0.0024 141 ALA D CA    
2319 C  C     . ALA B 142 ? 0.3076 0.3326 0.2148 -0.0288 -0.0231 -0.0077 141 ALA D C     
2320 O  O     . ALA B 142 ? 0.3041 0.3319 0.2118 -0.0296 -0.0331 -0.0107 141 ALA D O     
2321 C  CB    . ALA B 142 ? 0.3331 0.3645 0.2203 -0.0109 -0.0106 -0.0070 141 ALA D CB    
2322 N  N     . MET B 143 ? 0.2773 0.2973 0.1926 -0.0360 -0.0229 -0.0077 142 MET D N     
2323 C  CA    . MET B 143 ? 0.2952 0.3111 0.2186 -0.0451 -0.0344 -0.0090 142 MET D CA    
2324 C  C     . MET B 143 ? 0.2866 0.3103 0.2154 -0.0532 -0.0356 -0.0038 142 MET D C     
2325 O  O     . MET B 143 ? 0.2996 0.3238 0.2337 -0.0599 -0.0461 -0.0039 142 MET D O     
2326 C  CB    . MET B 143 ? 0.3324 0.3425 0.2625 -0.0508 -0.0353 -0.0082 142 MET D CB    
2327 C  CG    . MET B 143 ? 0.3124 0.3170 0.2417 -0.0431 -0.0378 -0.0151 142 MET D CG    
2328 S  SD    . MET B 143 ? 0.3727 0.3786 0.3092 -0.0452 -0.0319 -0.0137 142 MET D SD    
2329 C  CE    . MET B 143 ? 0.2838 0.2821 0.2273 -0.0566 -0.0444 -0.0086 142 MET D CE    
2330 N  N     . GLU B 144 ? 0.2747 0.3054 0.2032 -0.0522 -0.0253 0.0001  143 GLU D N     
2331 C  CA    . GLU B 144 ? 0.2837 0.3265 0.2179 -0.0572 -0.0256 0.0031  143 GLU D CA    
2332 C  C     . GLU B 144 ? 0.3015 0.3517 0.2352 -0.0536 -0.0333 0.0013  143 GLU D C     
2333 O  O     . GLU B 144 ? 0.3210 0.3847 0.2629 -0.0598 -0.0366 0.0032  143 GLU D O     
2334 C  CB    . GLU B 144 ? 0.2813 0.3283 0.2156 -0.0533 -0.0141 0.0049  143 GLU D CB    
2335 C  CG    . GLU B 144 ? 0.3036 0.3474 0.2409 -0.0588 -0.0078 0.0050  143 GLU D CG    
2336 C  CD    . GLU B 144 ? 0.3105 0.3589 0.2506 -0.0563 0.0009  0.0041  143 GLU D CD    
2337 O  OE1   . GLU B 144 ? 0.3482 0.3921 0.2858 -0.0471 0.0054  0.0049  143 GLU D OE1   
2338 O  OE2   . GLU B 144 ? 0.3095 0.3654 0.2537 -0.0628 0.0031  0.0023  143 GLU D OE2   
2339 N  N     . ARG B 145 ? 0.2881 0.3334 0.2130 -0.0440 -0.0366 -0.0027 144 ARG D N     
2340 C  CA    . ARG B 145 ? 0.3154 0.3691 0.2400 -0.0412 -0.0465 -0.0063 144 ARG D CA    
2341 C  C     . ARG B 145 ? 0.3121 0.3667 0.2479 -0.0536 -0.0593 -0.0083 144 ARG D C     
2342 O  O     . ARG B 145 ? 0.3341 0.3997 0.2754 -0.0557 -0.0680 -0.0106 144 ARG D O     
2343 C  CB    . ARG B 145 ? 0.3638 0.4129 0.2750 -0.0294 -0.0499 -0.0124 144 ARG D CB    
2344 C  CG    . ARG B 145 ? 0.3699 0.4181 0.2694 -0.0186 -0.0377 -0.0078 144 ARG D CG    
2345 C  CD    . ARG B 145 ? 0.3819 0.4312 0.2667 -0.0074 -0.0412 -0.0135 144 ARG D CD    
2346 N  NE    . ARG B 145 ? 0.4613 0.5110 0.3337 0.0018  -0.0290 -0.0065 144 ARG D NE    
2347 C  CZ    . ARG B 145 ? 0.4234 0.4742 0.2836 0.0093  -0.0263 -0.0098 144 ARG D CZ    
2348 N  NH1   . ARG B 145 ? 0.4359 0.4864 0.2944 0.0111  -0.0358 -0.0225 144 ARG D NH1   
2349 N  NH2   . ARG B 145 ? 0.5010 0.5540 0.3513 0.0153  -0.0141 -0.0003 144 ARG D NH2   
2350 N  N     . PHE B 146 ? 0.3215 0.3640 0.2613 -0.0619 -0.0619 -0.0073 145 PHE D N     
2351 C  CA    . PHE B 146 ? 0.3377 0.3736 0.2872 -0.0734 -0.0758 -0.0080 145 PHE D CA    
2352 C  C     . PHE B 146 ? 0.3343 0.3760 0.2941 -0.0886 -0.0743 0.0024  145 PHE D C     
2353 O  O     . PHE B 146 ? 0.3073 0.3397 0.2750 -0.0999 -0.0847 0.0057  145 PHE D O     
2354 C  CB    . PHE B 146 ? 0.3386 0.3536 0.2839 -0.0686 -0.0832 -0.0153 145 PHE D CB    
2355 C  CG    . PHE B 146 ? 0.3613 0.3759 0.2943 -0.0530 -0.0837 -0.0262 145 PHE D CG    
2356 C  CD1   . PHE B 146 ? 0.4122 0.4352 0.3440 -0.0500 -0.0922 -0.0324 145 PHE D CD1   
2357 C  CD2   . PHE B 146 ? 0.4116 0.4227 0.3341 -0.0416 -0.0745 -0.0289 145 PHE D CD2   
2358 C  CE1   . PHE B 146 ? 0.4337 0.4605 0.3508 -0.0346 -0.0922 -0.0418 145 PHE D CE1   
2359 C  CE2   . PHE B 146 ? 0.4275 0.4433 0.3365 -0.0274 -0.0732 -0.0370 145 PHE D CE2   
2360 C  CZ    . PHE B 146 ? 0.4315 0.4547 0.3365 -0.0234 -0.0822 -0.0434 145 PHE D CZ    
2361 N  N     . GLY B 147 ? 0.3250 0.3816 0.2845 -0.0888 -0.0619 0.0075  146 GLY D N     
2362 C  CA    . GLY B 147 ? 0.3111 0.3792 0.2779 -0.1021 -0.0592 0.0166  146 GLY D CA    
2363 C  C     . GLY B 147 ? 0.2921 0.3861 0.2690 -0.1089 -0.0587 0.0199  146 GLY D C     
2364 O  O     . GLY B 147 ? 0.3208 0.4223 0.3015 -0.1051 -0.0637 0.0155  146 GLY D O     
2365 N  N     . SER B 148 ? 0.3000 0.4115 0.2815 -0.1189 -0.0529 0.0276  147 SER D N     
2366 C  CA    . SER B 148 ? 0.2970 0.4395 0.2899 -0.1261 -0.0510 0.0312  147 SER D CA    
2367 C  C     . SER B 148 ? 0.2618 0.4242 0.2530 -0.1296 -0.0393 0.0355  147 SER D C     
2368 O  O     . SER B 148 ? 0.2562 0.4062 0.2381 -0.1288 -0.0354 0.0364  147 SER D O     
2369 C  CB    . SER B 148 ? 0.2898 0.4347 0.2954 -0.1433 -0.0637 0.0387  147 SER D CB    
2370 O  OG    . SER B 148 ? 0.2989 0.4329 0.3016 -0.1530 -0.0636 0.0498  147 SER D OG    
2371 N  N     . ARG B 149 ? 0.2758 0.4717 0.2766 -0.1335 -0.0344 0.0371  148 ARG D N     
2372 C  CA    . ARG B 149 ? 0.2970 0.5184 0.2961 -0.1350 -0.0229 0.0383  148 ARG D CA    
2373 C  C     . ARG B 149 ? 0.2881 0.5077 0.2819 -0.1498 -0.0241 0.0498  148 ARG D C     
2374 O  O     . ARG B 149 ? 0.3041 0.5277 0.2881 -0.1469 -0.0164 0.0479  148 ARG D O     
2375 C  CB    . ARG B 149 ? 0.3011 0.5641 0.3144 -0.1378 -0.0188 0.0385  148 ARG D CB    
2376 C  CG    . ARG B 149 ? 0.2997 0.5963 0.3119 -0.1391 -0.0067 0.0384  148 ARG D CG    
2377 C  CD    . ARG B 149 ? 0.3099 0.6457 0.3364 -0.1341 -0.0018 0.0333  148 ARG D CD    
2378 N  NE    . ARG B 149 ? 0.3882 0.7527 0.4105 -0.1334 0.0077  0.0326  148 ARG D NE    
2379 C  CZ    . ARG B 149 ? 0.3874 0.7579 0.4042 -0.1456 0.0059  0.0443  148 ARG D CZ    
2380 N  NH1   . ARG B 149 ? 0.3735 0.7260 0.3921 -0.1590 -0.0040 0.0577  148 ARG D NH1   
2381 N  NH2   . ARG B 149 ? 0.3747 0.7708 0.3849 -0.1437 0.0135  0.0418  148 ARG D NH2   
2382 N  N     . ASN B 150 ? 0.2715 0.4768 0.2669 -0.1594 -0.0337 0.0607  149 ASN D N     
2383 C  CA    . ASN B 150 ? 0.2824 0.4782 0.2682 -0.1671 -0.0361 0.0722  149 ASN D CA    
2384 C  C     . ASN B 150 ? 0.3232 0.4810 0.3032 -0.1659 -0.0451 0.0733  149 ASN D C     
2385 O  O     . ASN B 150 ? 0.2932 0.4402 0.2673 -0.1720 -0.0503 0.0838  149 ASN D O     
2386 C  CB    . ASN B 150 ? 0.3121 0.5182 0.3034 -0.1793 -0.0408 0.0859  149 ASN D CB    
2387 C  CG    . ASN B 150 ? 0.3503 0.5283 0.3500 -0.1850 -0.0540 0.0909  149 ASN D CG    
2388 O  OD1   . ASN B 150 ? 0.2965 0.4525 0.2992 -0.1783 -0.0595 0.0815  149 ASN D OD1   
2389 N  ND2   . ASN B 150 ? 0.3330 0.5135 0.3375 -0.1974 -0.0597 0.1049  149 ASN D ND2   
2390 N  N     . GLY B 151 ? 0.2841 0.4235 0.2658 -0.1577 -0.0482 0.0626  150 GLY D N     
2391 C  CA    . GLY B 151 ? 0.2990 0.4073 0.2748 -0.1537 -0.0550 0.0603  150 GLY D CA    
2392 C  C     . GLY B 151 ? 0.2968 0.3771 0.2779 -0.1548 -0.0690 0.0616  150 GLY D C     
2393 O  O     . GLY B 151 ? 0.3214 0.3777 0.2992 -0.1481 -0.0751 0.0552  150 GLY D O     
2394 N  N     . LYS B 152 ? 0.2963 0.3796 0.2865 -0.1625 -0.0746 0.0679  151 LYS D N     
2395 C  CA    . LYS B 152 ? 0.3073 0.3633 0.3043 -0.1626 -0.0887 0.0654  151 LYS D CA    
2396 C  C     . LYS B 152 ? 0.3150 0.3617 0.3107 -0.1504 -0.0915 0.0486  151 LYS D C     
2397 O  O     . LYS B 152 ? 0.3223 0.3890 0.3178 -0.1456 -0.0852 0.0415  151 LYS D O     
2398 C  CB    . LYS B 152 ? 0.3203 0.3849 0.3295 -0.1736 -0.0934 0.0730  151 LYS D CB    
2399 C  CG    . LYS B 152 ? 0.4413 0.4822 0.4605 -0.1740 -0.1077 0.0672  151 LYS D CG    
2400 C  CD    . LYS B 152 ? 0.5167 0.5262 0.5365 -0.1780 -0.1196 0.0751  151 LYS D CD    
2401 C  CE    . LYS B 152 ? 0.5071 0.5006 0.5411 -0.1842 -0.1332 0.0735  151 LYS D CE    
2402 N  NZ    . LYS B 152 ? 0.5939 0.5889 0.6331 -0.1761 -0.1366 0.0546  151 LYS D NZ    
2403 N  N     . THR B 153 ? 0.3255 0.3433 0.3193 -0.1444 -0.1019 0.0421  152 THR D N     
2404 C  CA    . THR B 153 ? 0.3459 0.3560 0.3342 -0.1315 -0.1050 0.0260  152 THR D CA    
2405 C  C     . THR B 153 ? 0.3642 0.3676 0.3608 -0.1308 -0.1162 0.0180  152 THR D C     
2406 O  O     . THR B 153 ? 0.3689 0.3602 0.3761 -0.1391 -0.1251 0.0231  152 THR D O     
2407 C  CB    . THR B 153 ? 0.3570 0.3443 0.3372 -0.1217 -0.1085 0.0196  152 THR D CB    
2408 O  OG1   . THR B 153 ? 0.3722 0.3347 0.3598 -0.1252 -0.1217 0.0224  152 THR D OG1   
2409 C  CG2   . THR B 153 ? 0.3231 0.3188 0.2959 -0.1194 -0.0951 0.0257  152 THR D CG2   
2410 N  N     . SER B 154 ? 0.3479 0.3596 0.3384 -0.1207 -0.1164 0.0055  153 SER D N     
2411 C  CA    . SER B 154 ? 0.3560 0.3661 0.3534 -0.1190 -0.1271 -0.0042 153 SER D CA    
2412 C  C     . SER B 154 ? 0.3647 0.3505 0.3560 -0.1073 -0.1380 -0.0194 153 SER D C     
2413 O  O     . SER B 154 ? 0.3869 0.3692 0.3840 -0.1055 -0.1480 -0.0297 153 SER D O     
2414 C  CB    . SER B 154 ? 0.3144 0.3517 0.3088 -0.1143 -0.1229 -0.0085 153 SER D CB    
2415 O  OG    . SER B 154 ? 0.3898 0.4303 0.3675 -0.0979 -0.1116 -0.0129 153 SER D OG    
2416 N  N     . LYS B 155 ? 0.3929 0.3655 0.3728 -0.0984 -0.1356 -0.0226 154 LYS D N     
2417 C  CA    . LYS B 155 ? 0.4327 0.3834 0.4077 -0.0859 -0.1448 -0.0371 154 LYS D CA    
2418 C  C     . LYS B 155 ? 0.4385 0.3724 0.4139 -0.0864 -0.1441 -0.0309 154 LYS D C     
2419 O  O     . LYS B 155 ? 0.3989 0.3423 0.3735 -0.0927 -0.1331 -0.0174 154 LYS D O     
2420 C  CB    . LYS B 155 ? 0.3817 0.3428 0.3394 -0.0668 -0.1385 -0.0508 154 LYS D CB    
2421 C  CG    . LYS B 155 ? 0.3840 0.3601 0.3395 -0.0643 -0.1444 -0.0594 154 LYS D CG    
2422 C  CD    . LYS B 155 ? 0.4424 0.4303 0.3781 -0.0442 -0.1365 -0.0700 154 LYS D CD    
2423 C  CE    . LYS B 155 ? 0.4368 0.4400 0.3693 -0.0408 -0.1451 -0.0788 154 LYS D CE    
2424 N  NZ    . LYS B 155 ? 0.5645 0.5569 0.4966 -0.0337 -0.1563 -0.0959 154 LYS D NZ    
2425 N  N     . LYS B 156 ? 0.4579 0.3695 0.4349 -0.0772 -0.1542 -0.0416 155 LYS D N     
2426 C  CA    . LYS B 156 ? 0.4332 0.3279 0.4127 -0.0759 -0.1570 -0.0369 155 LYS D CA    
2427 C  C     . LYS B 156 ? 0.4528 0.3599 0.4198 -0.0600 -0.1427 -0.0431 155 LYS D C     
2428 O  O     . LYS B 156 ? 0.4254 0.3338 0.3848 -0.0437 -0.1425 -0.0595 155 LYS D O     
2429 C  CB    . LYS B 156 ? 0.4458 0.3124 0.4350 -0.0705 -0.1728 -0.0451 155 LYS D CB    
2430 C  CG    . LYS B 156 ? 0.5455 0.3919 0.5406 -0.0704 -0.1795 -0.0376 155 LYS D CG    
2431 C  CD    . LYS B 156 ? 0.5779 0.3947 0.5830 -0.0623 -0.1968 -0.0473 155 LYS D CD    
2432 C  CE    . LYS B 156 ? 0.6635 0.4721 0.6648 -0.0401 -0.2009 -0.0668 155 LYS D CE    
2433 N  NZ    . LYS B 156 ? 0.5729 0.3984 0.5622 -0.0226 -0.1949 -0.0905 155 LYS D NZ    
2434 N  N     . ILE B 157 ? 0.4127 0.3315 0.3781 -0.0648 -0.1296 -0.0298 156 ILE D N     
2435 C  CA    . ILE B 157 ? 0.3554 0.2884 0.3123 -0.0532 -0.1139 -0.0325 156 ILE D CA    
2436 C  C     . ILE B 157 ? 0.3901 0.3113 0.3527 -0.0491 -0.1186 -0.0319 156 ILE D C     
2437 O  O     . ILE B 157 ? 0.4298 0.3466 0.3980 -0.0601 -0.1212 -0.0186 156 ILE D O     
2438 C  CB    . ILE B 157 ? 0.3565 0.3095 0.3096 -0.0611 -0.0980 -0.0205 156 ILE D CB    
2439 C  CG1   . ILE B 157 ? 0.3888 0.3523 0.3405 -0.0668 -0.0971 -0.0189 156 ILE D CG1   
2440 C  CG2   . ILE B 157 ? 0.3349 0.3011 0.2809 -0.0511 -0.0824 -0.0233 156 ILE D CG2   
2441 C  CD1   . ILE B 157 ? 0.4036 0.3700 0.3472 -0.0543 -0.0984 -0.0320 156 ILE D CD1   
2442 N  N     . THR B 158 ? 0.4239 0.3435 0.3848 -0.0326 -0.1192 -0.0461 157 THR D N     
2443 C  CA    . THR B 158 ? 0.3767 0.2856 0.3456 -0.0254 -0.1264 -0.0486 157 THR D CA    
2444 C  C     . THR B 158 ? 0.3864 0.3156 0.3527 -0.0135 -0.1121 -0.0540 157 THR D C     
2445 O  O     . THR B 158 ? 0.3827 0.3301 0.3404 -0.0071 -0.0989 -0.0597 157 THR D O     
2446 C  CB    . THR B 158 ? 0.3942 0.2800 0.3689 -0.0150 -0.1450 -0.0635 157 THR D CB    
2447 O  OG1   . THR B 158 ? 0.4117 0.3084 0.3775 -0.0004 -0.1409 -0.0819 157 THR D OG1   
2448 C  CG2   . THR B 158 ? 0.4319 0.2945 0.4133 -0.0298 -0.1612 -0.0563 157 THR D CG2   
2449 N  N     . ILE B 159 ? 0.3914 0.3180 0.3664 -0.0112 -0.1156 -0.0509 158 ILE D N     
2450 C  CA    . ILE B 159 ? 0.3913 0.3370 0.3692 0.0009  -0.1057 -0.0580 158 ILE D CA    
2451 C  C     . ILE B 159 ? 0.4060 0.3427 0.3890 0.0193  -0.1173 -0.0760 158 ILE D C     
2452 O  O     . ILE B 159 ? 0.4195 0.3384 0.4131 0.0241  -0.1327 -0.0774 158 ILE D O     
2453 C  CB    . ILE B 159 ? 0.3895 0.3408 0.3750 -0.0057 -0.1044 -0.0466 158 ILE D CB    
2454 C  CG1   . ILE B 159 ? 0.3787 0.3377 0.3582 -0.0230 -0.0946 -0.0318 158 ILE D CG1   
2455 C  CG2   . ILE B 159 ? 0.3864 0.3597 0.3791 0.0059  -0.0956 -0.0545 158 ILE D CG2   
2456 C  CD1   . ILE B 159 ? 0.3556 0.3175 0.3403 -0.0321 -0.0975 -0.0194 158 ILE D CD1   
2457 N  N     . ALA B 160 ? 0.4044 0.3531 0.3792 0.0309  -0.1110 -0.0904 159 ALA D N     
2458 C  CA    . ALA B 160 ? 0.4213 0.3637 0.3997 0.0502  -0.1221 -0.1110 159 ALA D CA    
2459 C  C     . ALA B 160 ? 0.4470 0.4069 0.4363 0.0642  -0.1182 -0.1180 159 ALA D C     
2460 O  O     . ALA B 160 ? 0.4147 0.3639 0.4134 0.0797  -0.1319 -0.1323 159 ALA D O     
2461 C  CB    . ALA B 160 ? 0.4287 0.3836 0.3928 0.0592  -0.1163 -0.1250 159 ALA D CB    
2462 N  N     . ASP B 161 ? 0.4168 0.4034 0.4070 0.0590  -0.1007 -0.1087 160 ASP D N     
2463 C  CA    . ASP B 161 ? 0.3998 0.4084 0.4029 0.0697  -0.0959 -0.1140 160 ASP D CA    
2464 C  C     . ASP B 161 ? 0.3876 0.4108 0.3944 0.0540  -0.0835 -0.0968 160 ASP D C     
2465 O  O     . ASP B 161 ? 0.3699 0.3922 0.3670 0.0387  -0.0745 -0.0846 160 ASP D O     
2466 C  CB    . ASP B 161 ? 0.4081 0.4476 0.4076 0.0863  -0.0834 -0.1303 160 ASP D CB    
2467 C  CG    . ASP B 161 ? 0.4531 0.5141 0.4696 0.1030  -0.0838 -0.1421 160 ASP D CG    
2468 O  OD1   . ASP B 161 ? 0.4596 0.5116 0.4914 0.1026  -0.0944 -0.1376 160 ASP D OD1   
2469 O  OD2   . ASP B 161 ? 0.4946 0.5848 0.5086 0.1176  -0.0734 -0.1562 160 ASP D OD2   
2470 N  N     . CYS B 162 ? 0.3892 0.4265 0.4112 0.0584  -0.0842 -0.0973 161 CYS D N     
2471 C  CA    . CYS B 162 ? 0.3322 0.3872 0.3590 0.0443  -0.0725 -0.0844 161 CYS D CA    
2472 C  C     . CYS B 162 ? 0.3755 0.4539 0.4214 0.0547  -0.0733 -0.0910 161 CYS D C     
2473 O  O     . CYS B 162 ? 0.3812 0.4534 0.4365 0.0709  -0.0873 -0.1016 161 CYS D O     
2474 C  CB    . CYS B 162 ? 0.3338 0.3673 0.3569 0.0270  -0.0803 -0.0682 161 CYS D CB    
2475 S  SG    . CYS B 162 ? 0.3771 0.3799 0.4071 0.0325  -0.1066 -0.0661 161 CYS D SG    
2476 N  N     . GLY B 163 ? 0.3423 0.4471 0.3953 0.0454  -0.0590 -0.0853 162 GLY D N     
2477 C  CA    . GLY B 163 ? 0.3498 0.4826 0.4235 0.0522  -0.0585 -0.0904 162 GLY D CA    
2478 C  C     . GLY B 163 ? 0.3422 0.4998 0.4228 0.0363  -0.0428 -0.0823 162 GLY D C     
2479 O  O     . GLY B 163 ? 0.3273 0.4742 0.3971 0.0197  -0.0360 -0.0714 162 GLY D O     
2480 N  N     . GLN B 164 ? 0.3369 0.5287 0.4377 0.0418  -0.0376 -0.0886 163 GLN D N     
2481 C  CA    . GLN B 164 ? 0.2938 0.5113 0.4068 0.0265  -0.0246 -0.0826 163 GLN D CA    
2482 C  C     . GLN B 164 ? 0.3178 0.5675 0.4363 0.0277  -0.0046 -0.0859 163 GLN D C     
2483 O  O     . GLN B 164 ? 0.3006 0.5702 0.4247 0.0452  -0.0030 -0.0974 163 GLN D O     
2484 C  CB    . GLN B 164 ? 0.3088 0.5452 0.4442 0.0289  -0.0350 -0.0856 163 GLN D CB    
2485 C  CG    . GLN B 164 ? 0.2387 0.5046 0.3911 0.0124  -0.0233 -0.0819 163 GLN D CG    
2486 C  CD    . GLN B 164 ? 0.2909 0.5702 0.4612 0.0115  -0.0367 -0.0833 163 GLN D CD    
2487 O  OE1   . GLN B 164 ? 0.3082 0.5808 0.4816 0.0262  -0.0540 -0.0871 163 GLN D OE1   
2488 N  NE2   . GLN B 164 ? 0.2391 0.5374 0.4222 -0.0054 -0.0298 -0.0806 163 GLN D NE2   
2489 N  N     . LEU B 165 ? 0.3198 0.5735 0.4354 0.0097  0.0105  -0.0756 164 LEU D N     
2490 C  CA    . LEU B 165 ? 0.3265 0.6136 0.4499 0.0066  0.0306  -0.0742 164 LEU D CA    
2491 C  C     . LEU B 165 ? 0.3326 0.6530 0.4839 -0.0047 0.0370  -0.0730 164 LEU D C     
2492 O  O     . LEU B 165 ? 0.3571 0.6677 0.5157 -0.0182 0.0306  -0.0690 164 LEU D O     
2493 C  CB    . LEU B 165 ? 0.2882 0.5588 0.3917 -0.0053 0.0437  -0.0622 164 LEU D CB    
2494 C  CG    . LEU B 165 ? 0.2962 0.5334 0.3729 0.0021  0.0366  -0.0621 164 LEU D CG    
2495 C  CD1   . LEU B 165 ? 0.3776 0.5970 0.4362 -0.0099 0.0470  -0.0493 164 LEU D CD1   
2496 C  CD2   . LEU B 165 ? 0.3545 0.6095 0.4266 0.0222  0.0382  -0.0737 164 LEU D CD2   
2497 N  N     . GLY C 1   ? 0.8479 0.6663 0.5211 -0.1987 -0.0716 -0.1820 0   GLY A N     
2498 C  CA    . GLY C 1   ? 0.7966 0.6319 0.4872 -0.1873 -0.0640 -0.1636 0   GLY A CA    
2499 C  C     . GLY C 1   ? 0.7752 0.5884 0.4881 -0.1800 -0.0426 -0.1628 0   GLY A C     
2500 O  O     . GLY C 1   ? 0.7746 0.5545 0.4851 -0.1795 -0.0291 -0.1757 0   GLY A O     
2501 N  N     . MET C 2   ? 0.7223 0.5539 0.4583 -0.1737 -0.0398 -0.1469 1   MET A N     
2502 C  CA    . MET C 2   ? 0.6919 0.5096 0.4548 -0.1615 -0.0197 -0.1410 1   MET A CA    
2503 C  C     . MET C 2   ? 0.6860 0.4906 0.4302 -0.1413 0.0013  -0.1402 1   MET A C     
2504 O  O     . MET C 2   ? 0.6871 0.5054 0.4099 -0.1344 0.0001  -0.1357 1   MET A O     
2505 C  CB    . MET C 2   ? 0.6190 0.4713 0.4300 -0.1572 -0.0255 -0.1193 1   MET A CB    
2506 C  CG    . MET C 2   ? 0.5475 0.4360 0.3663 -0.1472 -0.0341 -0.1024 1   MET A CG    
2507 S  SD    . MET C 2   ? 0.4865 0.4076 0.3588 -0.1377 -0.0338 -0.0803 1   MET A SD    
2508 C  CE    . MET C 2   ? 0.4663 0.4185 0.3597 -0.1573 -0.0598 -0.0780 1   MET A CE    
2509 N  N     . THR C 3   ? 0.6862 0.4631 0.4383 -0.1324 0.0210  -0.1444 2   THR A N     
2510 C  CA    . THR C 3   ? 0.6744 0.4406 0.4144 -0.1129 0.0418  -0.1437 2   THR A CA    
2511 C  C     . THR C 3   ? 0.6364 0.4356 0.4041 -0.0975 0.0437  -0.1211 2   THR A C     
2512 O  O     . THR C 3   ? 0.5700 0.3875 0.3717 -0.0973 0.0374  -0.1077 2   THR A O     
2513 C  CB    . THR C 3   ? 0.6820 0.4117 0.4288 -0.1060 0.0611  -0.1520 2   THR A CB    
2514 O  OG1   . THR C 3   ? 0.7241 0.4281 0.4511 -0.1163 0.0586  -0.1701 2   THR A OG1   
2515 C  CG2   . THR C 3   ? 0.6789 0.4045 0.4212 -0.0840 0.0826  -0.1485 2   THR A CG2   
2516 N  N     . GLU C 4   ? 0.6151 0.4215 0.3675 -0.0855 0.0528  -0.1174 3   GLU A N     
2517 C  CA    . GLU C 4   ? 0.5401 0.3742 0.3165 -0.0722 0.0550  -0.0981 3   GLU A CA    
2518 C  C     . GLU C 4   ? 0.5502 0.3742 0.3393 -0.0551 0.0762  -0.0956 3   GLU A C     
2519 O  O     . GLU C 4   ? 0.5795 0.3814 0.3482 -0.0500 0.0915  -0.1073 3   GLU A O     
2520 C  CB    . GLU C 4   ? 0.5941 0.4460 0.3491 -0.0716 0.0499  -0.0927 3   GLU A CB    
2521 C  CG    . GLU C 4   ? 0.6449 0.5097 0.4114 -0.0558 0.0635  -0.0803 3   GLU A CG    
2522 C  CD    . GLU C 4   ? 0.6884 0.5748 0.4449 -0.0569 0.0547  -0.0687 3   GLU A CD    
2523 O  OE1   . GLU C 4   ? 0.6212 0.5224 0.3941 -0.0473 0.0610  -0.0559 3   GLU A OE1   
2524 O  OE2   . GLU C 4   ? 0.7069 0.5931 0.4361 -0.0681 0.0420  -0.0732 3   GLU A OE2   
2525 N  N     . TYR C 5   ? 0.4949 0.3364 0.3175 -0.0458 0.0770  -0.0805 4   TYR A N     
2526 C  CA    . TYR C 5   ? 0.4621 0.3001 0.3025 -0.0296 0.0934  -0.0751 4   TYR A CA    
2527 C  C     . TYR C 5   ? 0.4562 0.3235 0.3112 -0.0207 0.0928  -0.0608 4   TYR A C     
2528 O  O     . TYR C 5   ? 0.4322 0.3202 0.3044 -0.0231 0.0806  -0.0505 4   TYR A O     
2529 C  CB    . TYR C 5   ? 0.4740 0.3054 0.3403 -0.0278 0.0934  -0.0696 4   TYR A CB    
2530 C  CG    . TYR C 5   ? 0.4858 0.2840 0.3410 -0.0372 0.0957  -0.0832 4   TYR A CG    
2531 C  CD1   . TYR C 5   ? 0.5339 0.3016 0.3802 -0.0288 0.1127  -0.0929 4   TYR A CD1   
2532 C  CD2   . TYR C 5   ? 0.5468 0.3433 0.4005 -0.0549 0.0813  -0.0875 4   TYR A CD2   
2533 C  CE1   . TYR C 5   ? 0.5462 0.2781 0.3809 -0.0381 0.1155  -0.1073 4   TYR A CE1   
2534 C  CE2   . TYR C 5   ? 0.5583 0.3216 0.4019 -0.0661 0.0830  -0.1017 4   TYR A CE2   
2535 C  CZ    . TYR C 5   ? 0.5908 0.3194 0.4235 -0.0576 0.1005  -0.1121 4   TYR A CZ    
2536 O  OH    . TYR C 5   ? 0.5918 0.2820 0.4136 -0.0685 0.1034  -0.1278 4   TYR A OH    
2537 N  N     . LYS C 6   ? 0.4371 0.3060 0.2873 -0.0107 0.1068  -0.0605 5   LYS A N     
2538 C  CA    . LYS C 6   ? 0.3980 0.2935 0.2631 -0.0047 0.1065  -0.0476 5   LYS A CA    
2539 C  C     . LYS C 6   ? 0.3729 0.2783 0.2696 0.0079  0.1125  -0.0386 5   LYS A C     
2540 O  O     . LYS C 6   ? 0.3689 0.2681 0.2715 0.0188  0.1275  -0.0400 5   LYS A O     
2541 C  CB    . LYS C 6   ? 0.4386 0.3350 0.2831 -0.0028 0.1179  -0.0502 5   LYS A CB    
2542 C  CG    . LYS C 6   ? 0.4850 0.3736 0.2944 -0.0150 0.1103  -0.0576 5   LYS A CG    
2543 C  CD    . LYS C 6   ? 0.5509 0.4415 0.3381 -0.0121 0.1242  -0.0582 5   LYS A CD    
2544 C  CE    . LYS C 6   ? 0.6677 0.5435 0.4102 -0.0229 0.1205  -0.0698 5   LYS A CE    
2545 N  NZ    . LYS C 6   ? 0.7578 0.6445 0.4982 -0.0346 0.0967  -0.0632 5   LYS A NZ    
2546 N  N     . LEU C 7   ? 0.3659 0.2868 0.2825 0.0070  0.1009  -0.0294 6   LEU A N     
2547 C  CA    . LEU C 7   ? 0.3339 0.2662 0.2772 0.0172  0.1027  -0.0204 6   LEU A CA    
2548 C  C     . LEU C 7   ? 0.3070 0.2651 0.2654 0.0198  0.0991  -0.0114 6   LEU A C     
2549 O  O     . LEU C 7   ? 0.3223 0.2891 0.2758 0.0123  0.0900  -0.0097 6   LEU A O     
2550 C  CB    . LEU C 7   ? 0.3043 0.2357 0.2567 0.0137  0.0927  -0.0170 6   LEU A CB    
2551 C  CG    . LEU C 7   ? 0.3660 0.2740 0.3067 0.0058  0.0922  -0.0248 6   LEU A CG    
2552 C  CD1   . LEU C 7   ? 0.3208 0.2328 0.2771 0.0044  0.0858  -0.0172 6   LEU A CD1   
2553 C  CD2   . LEU C 7   ? 0.3965 0.2787 0.3271 0.0103  0.1059  -0.0332 6   LEU A CD2   
2554 N  N     . VAL C 8   ? 0.2972 0.2675 0.2759 0.0302  0.1054  -0.0053 7   VAL A N     
2555 C  CA    . VAL C 8   ? 0.2625 0.2573 0.2584 0.0312  0.1021  0.0022  7   VAL A CA    
2556 C  C     . VAL C 8   ? 0.2627 0.2719 0.2809 0.0380  0.0960  0.0094  7   VAL A C     
2557 O  O     . VAL C 8   ? 0.2571 0.2620 0.2833 0.0477  0.1021  0.0118  7   VAL A O     
2558 C  CB    . VAL C 8   ? 0.2912 0.2934 0.2917 0.0360  0.1162  0.0032  7   VAL A CB    
2559 C  CG1   . VAL C 8   ? 0.2328 0.2608 0.2545 0.0339  0.1114  0.0115  7   VAL A CG1   
2560 C  CG2   . VAL C 8   ? 0.3007 0.2877 0.2719 0.0291  0.1233  -0.0041 7   VAL A CG2   
2561 N  N     . VAL C 9   ? 0.1974 0.2213 0.2234 0.0333  0.0836  0.0128  8   VAL A N     
2562 C  CA    . VAL C 9   ? 0.2220 0.2602 0.2632 0.0382  0.0755  0.0183  8   VAL A CA    
2563 C  C     . VAL C 9   ? 0.2243 0.2857 0.2860 0.0397  0.0738  0.0228  8   VAL A C     
2564 O  O     . VAL C 9   ? 0.1929 0.2605 0.2566 0.0318  0.0706  0.0217  8   VAL A O     
2565 C  CB    . VAL C 9   ? 0.2052 0.2431 0.2396 0.0322  0.0638  0.0166  8   VAL A CB    
2566 C  CG1   . VAL C 9   ? 0.2253 0.2764 0.2690 0.0380  0.0570  0.0216  8   VAL A CG1   
2567 C  CG2   . VAL C 9   ? 0.2380 0.2565 0.2562 0.0283  0.0654  0.0125  8   VAL A CG2   
2568 N  N     . VAL C 10  ? 0.1978 0.2725 0.2771 0.0496  0.0761  0.0290  9   VAL A N     
2569 C  CA    . VAL C 10  ? 0.1761 0.2767 0.2799 0.0508  0.0749  0.0340  9   VAL A CA    
2570 C  C     . VAL C 10  ? 0.2285 0.3484 0.3467 0.0568  0.0635  0.0403  9   VAL A C     
2571 O  O     . VAL C 10  ? 0.2154 0.3271 0.3253 0.0634  0.0615  0.0433  9   VAL A O     
2572 C  CB    . VAL C 10  ? 0.2269 0.3317 0.3435 0.0590  0.0914  0.0368  9   VAL A CB    
2573 C  CG1   . VAL C 10  ? 0.2520 0.3357 0.3472 0.0541  0.1030  0.0299  9   VAL A CG1   
2574 C  CG2   . VAL C 10  ? 0.2078 0.3069 0.3301 0.0743  0.0979  0.0416  9   VAL A CG2   
2575 N  N     . GLY C 11  ? 0.1969 0.3433 0.3373 0.0539  0.0561  0.0434  10  GLY A N     
2576 C  CA    . GLY C 11  ? 0.1775 0.3469 0.3311 0.0577  0.0423  0.0490  10  GLY A CA    
2577 C  C     . GLY C 11  ? 0.2056 0.3936 0.3704 0.0453  0.0290  0.0449  10  GLY A C     
2578 O  O     . GLY C 11  ? 0.2000 0.3784 0.3599 0.0340  0.0302  0.0384  10  GLY A O     
2579 N  N     . ALA C 12  ? 0.1790 0.3927 0.3580 0.0470  0.0149  0.0491  11  ALA A N     
2580 C  CA    . ALA C 12  ? 0.1676 0.3981 0.3571 0.0338  0.0001  0.0433  11  ALA A CA    
2581 C  C     . ALA C 12  ? 0.1858 0.3933 0.3480 0.0245  -0.0059 0.0314  11  ALA A C     
2582 O  O     . ALA C 12  ? 0.1971 0.3866 0.3344 0.0297  -0.0042 0.0294  11  ALA A O     
2583 C  CB    . ALA C 12  ? 0.2194 0.4802 0.4216 0.0370  -0.0170 0.0484  11  ALA A CB    
2584 N  N     . ASP C 13  ? 0.2177 0.4251 0.3865 0.0107  -0.0119 0.0237  12  ASP A N     
2585 C  CA    . ASP C 13  ? 0.2209 0.4048 0.3653 0.0045  -0.0165 0.0122  12  ASP A CA    
2586 C  C     . ASP C 13  ? 0.1953 0.3854 0.3234 0.0068  -0.0303 0.0066  12  ASP A C     
2587 O  O     . ASP C 13  ? 0.2141 0.4290 0.3520 0.0084  -0.0413 0.0100  12  ASP A O     
2588 C  CB    . ASP C 13  ? 0.2473 0.4242 0.4022 -0.0102 -0.0190 0.0056  12  ASP A CB    
2589 C  CG    . ASP C 13  ? 0.2237 0.3862 0.3819 -0.0121 -0.0034 0.0111  12  ASP A CG    
2590 O  OD1   . ASP C 13  ? 0.2143 0.3624 0.3556 -0.0037 0.0067  0.0138  12  ASP A OD1   
2591 O  OD2   . ASP C 13  ? 0.2699 0.4358 0.4465 -0.0228 -0.0018 0.0130  12  ASP A OD2   
2592 N  N     . GLY C 14  ? 0.2008 0.3698 0.3034 0.0078  -0.0291 -0.0011 13  GLY A N     
2593 C  CA    . GLY C 14  ? 0.2460 0.4172 0.3267 0.0110  -0.0381 -0.0070 13  GLY A CA    
2594 C  C     . GLY C 14  ? 0.2099 0.3833 0.2763 0.0236  -0.0331 0.0031  13  GLY A C     
2595 O  O     . GLY C 14  ? 0.2680 0.4431 0.3127 0.0268  -0.0385 0.0001  13  GLY A O     
2596 N  N     . VAL C 15  ? 0.2142 0.3852 0.2903 0.0308  -0.0217 0.0146  14  VAL A N     
2597 C  CA    . VAL C 15  ? 0.2097 0.3795 0.2744 0.0423  -0.0166 0.0254  14  VAL A CA    
2598 C  C     . VAL C 15  ? 0.2131 0.3598 0.2573 0.0435  -0.0068 0.0227  14  VAL A C     
2599 O  O     . VAL C 15  ? 0.2155 0.3600 0.2459 0.0504  -0.0039 0.0299  14  VAL A O     
2600 C  CB    . VAL C 15  ? 0.1855 0.3590 0.2690 0.0505  -0.0077 0.0379  14  VAL A CB    
2601 C  CG1   . VAL C 15  ? 0.2132 0.4156 0.3228 0.0509  -0.0169 0.0430  14  VAL A CG1   
2602 C  CG2   . VAL C 15  ? 0.2030 0.3571 0.2911 0.0471  0.0060  0.0345  14  VAL A CG2   
2603 N  N     . GLY C 16  ? 0.1942 0.3252 0.2376 0.0367  -0.0021 0.0139  15  GLY A N     
2604 C  CA    . GLY C 16  ? 0.1962 0.3097 0.2258 0.0373  0.0062  0.0121  15  GLY A CA    
2605 C  C     . GLY C 16  ? 0.2056 0.3040 0.2405 0.0364  0.0167  0.0149  15  GLY A C     
2606 O  O     . GLY C 16  ? 0.1980 0.2847 0.2238 0.0373  0.0231  0.0162  15  GLY A O     
2607 N  N     . LYS C 17  ? 0.1905 0.2898 0.2394 0.0339  0.0189  0.0158  16  LYS A N     
2608 C  CA    . LYS C 17  ? 0.1931 0.2771 0.2413 0.0320  0.0285  0.0163  16  LYS A CA    
2609 C  C     . LYS C 17  ? 0.1959 0.2672 0.2343 0.0266  0.0282  0.0103  16  LYS A C     
2610 O  O     . LYS C 17  ? 0.2043 0.2639 0.2351 0.0262  0.0337  0.0110  16  LYS A O     
2611 C  CB    . LYS C 17  ? 0.1914 0.2807 0.2538 0.0289  0.0310  0.0171  16  LYS A CB    
2612 C  CG    . LYS C 17  ? 0.1833 0.2891 0.2613 0.0357  0.0323  0.0243  16  LYS A CG    
2613 C  CD    . LYS C 17  ? 0.1815 0.2954 0.2762 0.0327  0.0376  0.0259  16  LYS A CD    
2614 C  CE    . LYS C 17  ? 0.2104 0.3294 0.3114 0.0220  0.0298  0.0212  16  LYS A CE    
2615 N  NZ    . LYS C 17  ? 0.2327 0.3726 0.3477 0.0196  0.0171  0.0204  16  LYS A NZ    
2616 N  N     . SER C 18  ? 0.1827 0.2559 0.2230 0.0220  0.0215  0.0043  17  SER A N     
2617 C  CA    . SER C 18  ? 0.1864 0.2486 0.2217 0.0186  0.0210  0.0000  17  SER A CA    
2618 C  C     . SER C 18  ? 0.2141 0.2761 0.2406 0.0223  0.0215  -0.0019 17  SER A C     
2619 O  O     . SER C 18  ? 0.1914 0.2469 0.2154 0.0214  0.0243  -0.0015 17  SER A O     
2620 C  CB    . SER C 18  ? 0.1940 0.2549 0.2356 0.0139  0.0147  -0.0055 17  SER A CB    
2621 O  OG    . SER C 18  ? 0.1960 0.2575 0.2471 0.0090  0.0160  -0.0018 17  SER A OG    
2622 N  N     . ALA C 19  ? 0.2195 0.2907 0.2414 0.0262  0.0188  -0.0033 18  ALA A N     
2623 C  CA    . ALA C 19  ? 0.1737 0.2465 0.1862 0.0299  0.0219  -0.0037 18  ALA A CA    
2624 C  C     . ALA C 19  ? 0.1982 0.2667 0.2092 0.0307  0.0295  0.0047  18  ALA A C     
2625 O  O     . ALA C 19  ? 0.2149 0.2816 0.2246 0.0300  0.0336  0.0050  18  ALA A O     
2626 C  CB    . ALA C 19  ? 0.2105 0.2945 0.2135 0.0336  0.0175  -0.0058 18  ALA A CB    
2627 N  N     . LEU C 20  ? 0.2105 0.2771 0.2236 0.0320  0.0319  0.0112  19  LEU A N     
2628 C  CA    . LEU C 20  ? 0.2234 0.2804 0.2352 0.0318  0.0394  0.0176  19  LEU A CA    
2629 C  C     . LEU C 20  ? 0.2157 0.2621 0.2295 0.0251  0.0410  0.0139  19  LEU A C     
2630 O  O     . LEU C 20  ? 0.2446 0.2866 0.2577 0.0218  0.0442  0.0152  19  LEU A O     
2631 C  CB    . LEU C 20  ? 0.2028 0.2566 0.2179 0.0362  0.0425  0.0242  19  LEU A CB    
2632 C  CG    . LEU C 20  ? 0.2356 0.2995 0.2484 0.0439  0.0411  0.0326  19  LEU A CG    
2633 C  CD1   . LEU C 20  ? 0.2323 0.2960 0.2547 0.0500  0.0432  0.0387  19  LEU A CD1   
2634 C  CD2   . LEU C 20  ? 0.2346 0.2937 0.2389 0.0452  0.0466  0.0400  19  LEU A CD2   
2635 N  N     . THR C 21  ? 0.1848 0.2288 0.2014 0.0224  0.0382  0.0101  20  THR A N     
2636 C  CA    . THR C 21  ? 0.1979 0.2334 0.2130 0.0163  0.0378  0.0075  20  THR A CA    
2637 C  C     . THR C 21  ? 0.2112 0.2510 0.2290 0.0142  0.0338  0.0054  20  THR A C     
2638 O  O     . THR C 21  ? 0.2184 0.2551 0.2362 0.0096  0.0340  0.0058  20  THR A O     
2639 C  CB    . THR C 21  ? 0.2001 0.2342 0.2162 0.0144  0.0362  0.0061  20  THR A CB    
2640 O  OG1   . THR C 21  ? 0.2144 0.2469 0.2311 0.0173  0.0420  0.0084  20  THR A OG1   
2641 C  CG2   . THR C 21  ? 0.1934 0.2197 0.2036 0.0085  0.0348  0.0049  20  THR A CG2   
2642 N  N     . ILE C 22  ? 0.1676 0.2147 0.1891 0.0175  0.0300  0.0024  21  ILE A N     
2643 C  CA    . ILE C 22  ? 0.1550 0.2067 0.1820 0.0182  0.0280  0.0002  21  ILE A CA    
2644 C  C     . ILE C 22  ? 0.1938 0.2525 0.2220 0.0192  0.0332  0.0027  21  ILE A C     
2645 O  O     . ILE C 22  ? 0.2174 0.2812 0.2539 0.0174  0.0330  0.0034  21  ILE A O     
2646 C  CB    . ILE C 22  ? 0.2076 0.2614 0.2370 0.0224  0.0245  -0.0055 21  ILE A CB    
2647 C  CG1   . ILE C 22  ? 0.2452 0.2909 0.2770 0.0192  0.0196  -0.0061 21  ILE A CG1   
2648 C  CG2   . ILE C 22  ? 0.2241 0.2829 0.2611 0.0263  0.0250  -0.0081 21  ILE A CG2   
2649 C  CD1   . ILE C 22  ? 0.2720 0.3122 0.3061 0.0156  0.0172  -0.0019 21  ILE A CD1   
2650 N  N     . GLN C 23  ? 0.1841 0.2447 0.2061 0.0217  0.0379  0.0057  22  GLN A N     
2651 C  CA    . GLN C 23  ? 0.2010 0.2665 0.2244 0.0208  0.0444  0.0107  22  GLN A CA    
2652 C  C     . GLN C 23  ? 0.2446 0.3028 0.2733 0.0126  0.0453  0.0138  22  GLN A C     
2653 O  O     . GLN C 23  ? 0.2369 0.3017 0.2748 0.0084  0.0477  0.0161  22  GLN A O     
2654 C  CB    . GLN C 23  ? 0.2477 0.3138 0.2616 0.0248  0.0491  0.0165  22  GLN A CB    
2655 C  CG    . GLN C 23  ? 0.2643 0.3417 0.2705 0.0311  0.0505  0.0151  22  GLN A CG    
2656 C  CD    . GLN C 23  ? 0.2724 0.3606 0.2827 0.0318  0.0575  0.0152  22  GLN A CD    
2657 O  OE1   . GLN C 23  ? 0.2818 0.3716 0.3055 0.0265  0.0602  0.0175  22  GLN A OE1   
2658 N  NE2   . GLN C 23  ? 0.2544 0.3518 0.2535 0.0381  0.0604  0.0123  22  GLN A NE2   
2659 N  N     . LEU C 24  ? 0.1988 0.2438 0.2219 0.0100  0.0448  0.0140  23  LEU A N     
2660 C  CA    . LEU C 24  ? 0.2338 0.2683 0.2576 0.0014  0.0452  0.0138  23  LEU A CA    
2661 C  C     . LEU C 24  ? 0.2277 0.2689 0.2584 -0.0043 0.0379  0.0105  23  LEU A C     
2662 O  O     . LEU C 24  ? 0.2203 0.2642 0.2584 -0.0120 0.0369  0.0114  23  LEU A O     
2663 C  CB    . LEU C 24  ? 0.2464 0.2650 0.2608 0.0013  0.0465  0.0118  23  LEU A CB    
2664 C  CG    . LEU C 24  ? 0.2518 0.2545 0.2614 -0.0078 0.0474  0.0084  23  LEU A CG    
2665 C  CD1   . LEU C 24  ? 0.2896 0.2821 0.3020 -0.0110 0.0542  0.0127  23  LEU A CD1   
2666 C  CD2   . LEU C 24  ? 0.2822 0.2721 0.2803 -0.0060 0.0492  0.0039  23  LEU A CD2   
2667 N  N     . ILE C 25  ? 0.2292 0.2730 0.2586 -0.0010 0.0321  0.0077  24  ILE A N     
2668 C  CA    . ILE C 25  ? 0.2232 0.2708 0.2568 -0.0057 0.0239  0.0068  24  ILE A CA    
2669 C  C     . ILE C 25  ? 0.2589 0.3239 0.3096 -0.0030 0.0222  0.0087  24  ILE A C     
2670 O  O     . ILE C 25  ? 0.2423 0.3166 0.3038 -0.0086 0.0169  0.0105  24  ILE A O     
2671 C  CB    . ILE C 25  ? 0.2455 0.2878 0.2719 -0.0030 0.0195  0.0057  24  ILE A CB    
2672 C  CG1   . ILE C 25  ? 0.2618 0.2900 0.2733 -0.0049 0.0237  0.0041  24  ILE A CG1   
2673 C  CG2   . ILE C 25  ? 0.2524 0.2997 0.2827 -0.0061 0.0102  0.0077  24  ILE A CG2   
2674 C  CD1   . ILE C 25  ? 0.2543 0.2720 0.2551 -0.0134 0.0240  0.0015  24  ILE A CD1   
2675 N  N     . GLN C 26  ? 0.2433 0.3140 0.2972 0.0060  0.0263  0.0078  25  GLN A N     
2676 C  CA    . GLN C 26  ? 0.2486 0.3344 0.3181 0.0118  0.0266  0.0079  25  GLN A CA    
2677 C  C     . GLN C 26  ? 0.2649 0.3621 0.3392 0.0156  0.0367  0.0088  25  GLN A C     
2678 O  O     . GLN C 26  ? 0.2502 0.3621 0.3392 0.0209  0.0394  0.0087  25  GLN A O     
2679 C  CB    . GLN C 26  ? 0.2526 0.3337 0.3210 0.0197  0.0235  0.0040  25  GLN A CB    
2680 C  CG    . GLN C 26  ? 0.2645 0.3356 0.3290 0.0163  0.0146  0.0057  25  GLN A CG    
2681 C  CD    . GLN C 26  ? 0.3819 0.4459 0.4484 0.0231  0.0120  0.0033  25  GLN A CD    
2682 O  OE1   . GLN C 26  ? 0.3954 0.4615 0.4666 0.0306  0.0162  -0.0019 25  GLN A OE1   
2683 N  NE2   . GLN C 26  ? 0.4142 0.4685 0.4763 0.0201  0.0057  0.0069  25  GLN A NE2   
2684 N  N     . ASN C 27  ? 0.2464 0.3380 0.3087 0.0145  0.0430  0.0105  26  ASN A N     
2685 C  CA    . ASN C 27  ? 0.2461 0.3483 0.3096 0.0168  0.0534  0.0143  26  ASN A CA    
2686 C  C     . ASN C 27  ? 0.2754 0.3859 0.3354 0.0278  0.0576  0.0088  26  ASN A C     
2687 O  O     . ASN C 27  ? 0.2686 0.3937 0.3354 0.0317  0.0665  0.0100  26  ASN A O     
2688 C  CB    . ASN C 27  ? 0.2132 0.3286 0.2958 0.0096  0.0567  0.0201  26  ASN A CB    
2689 C  CG    . ASN C 27  ? 0.2827 0.3990 0.3628 0.0051  0.0675  0.0284  26  ASN A CG    
2690 O  OD1   . ASN C 27  ? 0.2856 0.3881 0.3622 -0.0036 0.0666  0.0320  26  ASN A OD1   
2691 N  ND2   . ASN C 27  ? 0.2420 0.3721 0.3209 0.0117  0.0787  0.0315  26  ASN A ND2   
2692 N  N     . HIS C 28  ? 0.2517 0.3525 0.3006 0.0325  0.0522  0.0018  27  HIS A N     
2693 C  CA    . HIS C 28  ? 0.3187 0.4226 0.3578 0.0413  0.0559  -0.0057 27  HIS A CA    
2694 C  C     . HIS C 28  ? 0.2673 0.3601 0.2902 0.0412  0.0493  -0.0097 27  HIS A C     
2695 O  O     . HIS C 28  ? 0.2762 0.3604 0.2993 0.0359  0.0435  -0.0065 27  HIS A O     
2696 C  CB    . HIS C 28  ? 0.3544 0.4611 0.4061 0.0481  0.0556  -0.0130 27  HIS A CB    
2697 C  CG    . HIS C 28  ? 0.3473 0.4400 0.4024 0.0471  0.0451  -0.0168 27  HIS A CG    
2698 N  ND1   . HIS C 28  ? 0.4095 0.4902 0.4539 0.0495  0.0409  -0.0256 27  HIS A ND1   
2699 C  CD2   . HIS C 28  ? 0.3695 0.4581 0.4360 0.0425  0.0376  -0.0119 27  HIS A CD2   
2700 C  CE1   . HIS C 28  ? 0.3915 0.4609 0.4428 0.0466  0.0328  -0.0249 27  HIS A CE1   
2701 N  NE2   . HIS C 28  ? 0.4289 0.5030 0.4916 0.0429  0.0308  -0.0162 27  HIS A NE2   
2702 N  N     . PHE C 29  ? 0.3251 0.4200 0.3341 0.0469  0.0508  -0.0171 28  PHE A N     
2703 C  CA    . PHE C 29  ? 0.3094 0.3997 0.3035 0.0462  0.0441  -0.0200 28  PHE A CA    
2704 C  C     . PHE C 29  ? 0.3928 0.4746 0.3864 0.0473  0.0369  -0.0330 28  PHE A C     
2705 O  O     . PHE C 29  ? 0.4129 0.4944 0.4008 0.0527  0.0400  -0.0434 28  PHE A O     
2706 C  CB    . PHE C 29  ? 0.3164 0.4162 0.2911 0.0497  0.0490  -0.0170 28  PHE A CB    
2707 C  CG    . PHE C 29  ? 0.3259 0.4259 0.2850 0.0499  0.0399  -0.0215 28  PHE A CG    
2708 C  CD1   . PHE C 29  ? 0.3421 0.4397 0.3063 0.0461  0.0324  -0.0151 28  PHE A CD1   
2709 C  CD2   . PHE C 29  ? 0.3467 0.4503 0.2872 0.0538  0.0388  -0.0328 28  PHE A CD2   
2710 C  CE1   . PHE C 29  ? 0.3343 0.4367 0.2895 0.0457  0.0225  -0.0182 28  PHE A CE1   
2711 C  CE2   . PHE C 29  ? 0.3744 0.4805 0.3014 0.0522  0.0276  -0.0376 28  PHE A CE2   
2712 C  CZ    . PHE C 29  ? 0.3144 0.4218 0.2509 0.0480  0.0189  -0.0294 28  PHE A CZ    
2713 N  N     . VAL C 30  ? 0.4091 0.4827 0.4089 0.0419  0.0284  -0.0325 29  VAL A N     
2714 C  CA    . VAL C 30  ? 0.4507 0.5140 0.4527 0.0402  0.0211  -0.0429 29  VAL A CA    
2715 C  C     . VAL C 30  ? 0.4356 0.5035 0.4211 0.0401  0.0162  -0.0513 29  VAL A C     
2716 O  O     . VAL C 30  ? 0.4406 0.5160 0.4228 0.0368  0.0110  -0.0458 29  VAL A O     
2717 C  CB    . VAL C 30  ? 0.4566 0.5127 0.4710 0.0333  0.0154  -0.0373 29  VAL A CB    
2718 C  CG1   . VAL C 30  ? 0.4727 0.5201 0.4899 0.0287  0.0076  -0.0458 29  VAL A CG1   
2719 C  CG2   . VAL C 30  ? 0.4584 0.5083 0.4852 0.0334  0.0177  -0.0320 29  VAL A CG2   
2720 N  N     . ASP C 31  ? 0.4252 0.4897 0.3998 0.0444  0.0177  -0.0647 30  ASP A N     
2721 C  CA    . ASP C 31  ? 0.4554 0.5249 0.4100 0.0432  0.0112  -0.0739 30  ASP A CA    
2722 C  C     . ASP C 31  ? 0.4647 0.5252 0.4262 0.0347  -0.0012 -0.0827 30  ASP A C     
2723 O  O     . ASP C 31  ? 0.5058 0.5754 0.4585 0.0300  -0.0109 -0.0852 30  ASP A O     
2724 C  CB    . ASP C 31  ? 0.5251 0.5938 0.4608 0.0505  0.0185  -0.0868 30  ASP A CB    
2725 C  CG    . ASP C 31  ? 0.5829 0.6636 0.4901 0.0509  0.0145  -0.0909 30  ASP A CG    
2726 O  OD1   . ASP C 31  ? 0.7049 0.7951 0.5951 0.0577  0.0248  -0.0883 30  ASP A OD1   
2727 O  OD2   . ASP C 31  ? 0.6754 0.7585 0.5780 0.0440  0.0009  -0.0946 30  ASP A OD2   
2728 N  N     . GLU C 32  ? 0.4358 0.4801 0.4152 0.0320  -0.0015 -0.0850 31  GLU A N     
2729 C  CA    . GLU C 32  ? 0.4209 0.4533 0.4095 0.0229  -0.0113 -0.0931 31  GLU A CA    
2730 C  C     . GLU C 32  ? 0.3672 0.4085 0.3713 0.0149  -0.0165 -0.0797 31  GLU A C     
2731 O  O     . GLU C 32  ? 0.3598 0.4104 0.3686 0.0175  -0.0113 -0.0654 31  GLU A O     
2732 C  CB    . GLU C 32  ? 0.4201 0.4290 0.4209 0.0250  -0.0075 -0.0989 31  GLU A CB    
2733 C  CG    . GLU C 32  ? 0.4356 0.4374 0.4249 0.0364  0.0014  -0.1107 31  GLU A CG    
2734 C  CD    . GLU C 32  ? 0.4475 0.4270 0.4530 0.0414  0.0056  -0.1137 31  GLU A CD    
2735 O  OE1   . GLU C 32  ? 0.4315 0.4084 0.4553 0.0393  0.0050  -0.0994 31  GLU A OE1   
2736 O  OE2   . GLU C 32  ? 0.5086 0.4732 0.5077 0.0479  0.0096  -0.1297 31  GLU A OE2   
2737 N  N     . TYR C 33  ? 0.3292 0.3684 0.3420 0.0047  -0.0264 -0.0850 32  TYR A N     
2738 C  CA    . TYR C 33  ? 0.2842 0.3353 0.3145 -0.0027 -0.0301 -0.0728 32  TYR A CA    
2739 C  C     . TYR C 33  ? 0.2828 0.3174 0.3321 -0.0090 -0.0278 -0.0683 32  TYR A C     
2740 O  O     . TYR C 33  ? 0.2624 0.2812 0.3181 -0.0163 -0.0328 -0.0780 32  TYR A O     
2741 C  CB    . TYR C 33  ? 0.2636 0.3297 0.2957 -0.0112 -0.0428 -0.0786 32  TYR A CB    
2742 C  CG    . TYR C 33  ? 0.2506 0.3343 0.3045 -0.0169 -0.0449 -0.0649 32  TYR A CG    
2743 C  CD1   . TYR C 33  ? 0.2985 0.3903 0.3695 -0.0295 -0.0556 -0.0688 32  TYR A CD1   
2744 C  CD2   . TYR C 33  ? 0.2592 0.3515 0.3178 -0.0100 -0.0355 -0.0489 32  TYR A CD2   
2745 C  CE1   . TYR C 33  ? 0.3088 0.4207 0.4033 -0.0340 -0.0563 -0.0561 32  TYR A CE1   
2746 C  CE2   . TYR C 33  ? 0.2530 0.3616 0.3321 -0.0136 -0.0352 -0.0375 32  TYR A CE2   
2747 C  CZ    . TYR C 33  ? 0.2877 0.4078 0.3857 -0.0250 -0.0451 -0.0406 32  TYR A CZ    
2748 O  OH    . TYR C 33  ? 0.2965 0.4370 0.4193 -0.0287 -0.0444 -0.0295 32  TYR A OH    
2749 N  N     . ASP C 34  ? 0.2743 0.3109 0.3306 -0.0065 -0.0202 -0.0537 33  ASP A N     
2750 C  CA    . ASP C 34  ? 0.2597 0.2824 0.3296 -0.0115 -0.0170 -0.0461 33  ASP A CA    
2751 C  C     . ASP C 34  ? 0.2771 0.3152 0.3573 -0.0159 -0.0142 -0.0334 33  ASP A C     
2752 O  O     . ASP C 34  ? 0.2543 0.2971 0.3297 -0.0105 -0.0071 -0.0241 33  ASP A O     
2753 C  CB    . ASP C 34  ? 0.2996 0.3103 0.3640 -0.0033 -0.0102 -0.0415 33  ASP A CB    
2754 C  CG    . ASP C 34  ? 0.3353 0.3298 0.4102 -0.0076 -0.0086 -0.0331 33  ASP A CG    
2755 O  OD1   . ASP C 34  ? 0.3465 0.3354 0.4332 -0.0175 -0.0113 -0.0313 33  ASP A OD1   
2756 O  OD2   . ASP C 34  ? 0.3533 0.3424 0.4250 -0.0013 -0.0049 -0.0266 33  ASP A OD2   
2757 N  N     . PRO C 35  ? 0.2525 0.3003 0.3471 -0.0253 -0.0195 -0.0337 34  PRO A N     
2758 C  CA    . PRO C 35  ? 0.2419 0.3093 0.3480 -0.0267 -0.0150 -0.0221 34  PRO A CA    
2759 C  C     . PRO C 35  ? 0.2520 0.3094 0.3605 -0.0278 -0.0050 -0.0108 34  PRO A C     
2760 O  O     . PRO C 35  ? 0.2484 0.2888 0.3613 -0.0339 -0.0047 -0.0094 34  PRO A O     
2761 C  CB    . PRO C 35  ? 0.2400 0.3216 0.3661 -0.0381 -0.0238 -0.0252 34  PRO A CB    
2762 C  CG    . PRO C 35  ? 0.2345 0.2955 0.3604 -0.0457 -0.0308 -0.0368 34  PRO A CG    
2763 C  CD    . PRO C 35  ? 0.2648 0.3096 0.3674 -0.0351 -0.0298 -0.0454 34  PRO A CD    
2764 N  N     . THR C 36  ? 0.2445 0.3107 0.3475 -0.0212 0.0034  -0.0028 35  THR A N     
2765 C  CA    . THR C 36  ? 0.2457 0.3022 0.3405 -0.0197 0.0129  0.0058  35  THR A CA    
2766 C  C     . THR C 36  ? 0.1874 0.2466 0.2945 -0.0278 0.0195  0.0151  35  THR A C     
2767 O  O     . THR C 36  ? 0.1881 0.2655 0.3129 -0.0315 0.0212  0.0177  35  THR A O     
2768 C  CB    . THR C 36  ? 0.1963 0.2597 0.2800 -0.0107 0.0191  0.0080  35  THR A CB    
2769 O  OG1   . THR C 36  ? 0.1652 0.2250 0.2378 -0.0047 0.0141  0.0013  35  THR A OG1   
2770 C  CG2   . THR C 36  ? 0.2191 0.2723 0.2895 -0.0096 0.0281  0.0143  35  THR A CG2   
2771 N  N     . ILE C 37  ? 0.1997 0.2428 0.2982 -0.0304 0.0235  0.0216  36  ILE A N     
2772 C  CA    . ILE C 37  ? 0.2070 0.2534 0.3105 -0.0365 0.0335  0.0328  36  ILE A CA    
2773 C  C     . ILE C 37  ? 0.2357 0.2855 0.3215 -0.0294 0.0436  0.0360  36  ILE A C     
2774 O  O     . ILE C 37  ? 0.2256 0.2909 0.3183 -0.0272 0.0523  0.0377  36  ILE A O     
2775 C  CB    . ILE C 37  ? 0.2128 0.2408 0.3162 -0.0441 0.0326  0.0402  36  ILE A CB    
2776 C  CG1   . ILE C 37  ? 0.2827 0.3073 0.4078 -0.0527 0.0238  0.0348  36  ILE A CG1   
2777 C  CG2   . ILE C 37  ? 0.2269 0.2579 0.3289 -0.0500 0.0454  0.0545  36  ILE A CG2   
2778 C  CD1   . ILE C 37  ? 0.2683 0.2743 0.4010 -0.0619 0.0233  0.0424  36  ILE A CD1   
2779 N  N     . GLU C 38  ? 0.2247 0.2603 0.2889 -0.0253 0.0420  0.0356  37  GLU A N     
2780 C  CA    . GLU C 38  ? 0.2419 0.2772 0.2867 -0.0200 0.0494  0.0353  37  GLU A CA    
2781 C  C     . GLU C 38  ? 0.2326 0.2548 0.2606 -0.0175 0.0418  0.0333  37  GLU A C     
2782 O  O     . GLU C 38  ? 0.2659 0.2785 0.2920 -0.0207 0.0366  0.0387  37  GLU A O     
2783 C  CB    . GLU C 38  ? 0.2445 0.2803 0.2796 -0.0234 0.0620  0.0436  37  GLU A CB    
2784 C  CG    . GLU C 38  ? 0.3287 0.3627 0.3435 -0.0175 0.0703  0.0391  37  GLU A CG    
2785 C  CD    . GLU C 38  ? 0.4423 0.4828 0.4530 -0.0180 0.0867  0.0435  37  GLU A CD    
2786 O  OE1   . GLU C 38  ? 0.4724 0.5045 0.4609 -0.0217 0.0914  0.0486  37  GLU A OE1   
2787 O  OE2   . GLU C 38  ? 0.4557 0.5108 0.4852 -0.0140 0.0950  0.0425  37  GLU A OE2   
2788 N  N     . ASP C 39  ? 0.2383 0.2606 0.2572 -0.0121 0.0408  0.0269  38  ASP A N     
2789 C  CA    . ASP C 39  ? 0.2609 0.2752 0.2677 -0.0109 0.0337  0.0257  38  ASP A CA    
2790 C  C     . ASP C 39  ? 0.2817 0.2937 0.2714 -0.0096 0.0379  0.0219  38  ASP A C     
2791 O  O     . ASP C 39  ? 0.2565 0.2719 0.2485 -0.0061 0.0442  0.0173  38  ASP A O     
2792 C  CB    . ASP C 39  ? 0.2363 0.2525 0.2544 -0.0068 0.0256  0.0201  38  ASP A CB    
2793 C  CG    . ASP C 39  ? 0.2892 0.3020 0.3212 -0.0083 0.0203  0.0210  38  ASP A CG    
2794 O  OD1   . ASP C 39  ? 0.2968 0.3005 0.3277 -0.0096 0.0163  0.0266  38  ASP A OD1   
2795 O  OD2   . ASP C 39  ? 0.3044 0.3230 0.3481 -0.0084 0.0200  0.0164  38  ASP A OD2   
2796 N  N     . SER C 40  ? 0.2534 0.2594 0.2278 -0.0122 0.0328  0.0234  39  SER A N     
2797 C  CA    . SER C 40  ? 0.2721 0.2736 0.2292 -0.0136 0.0344  0.0181  39  SER A CA    
2798 C  C     . SER C 40  ? 0.2923 0.2955 0.2521 -0.0142 0.0236  0.0163  39  SER A C     
2799 O  O     . SER C 40  ? 0.2814 0.2876 0.2481 -0.0138 0.0147  0.0216  39  SER A O     
2800 C  CB    . SER C 40  ? 0.3706 0.3654 0.3020 -0.0185 0.0380  0.0204  39  SER A CB    
2801 O  OG    . SER C 40  ? 0.4550 0.4497 0.3836 -0.0174 0.0517  0.0208  39  SER A OG    
2802 N  N     . TYR C 41  ? 0.2642 0.2650 0.2201 -0.0150 0.0253  0.0094  40  TYR A N     
2803 C  CA    . TYR C 41  ? 0.2408 0.2463 0.2038 -0.0167 0.0172  0.0075  40  TYR A CA    
2804 C  C     . TYR C 41  ? 0.2926 0.2901 0.2397 -0.0235 0.0175  0.0012  40  TYR A C     
2805 O  O     . TYR C 41  ? 0.2918 0.2780 0.2245 -0.0242 0.0266  -0.0037 40  TYR A O     
2806 C  CB    . TYR C 41  ? 0.2134 0.2250 0.1948 -0.0112 0.0198  0.0059  40  TYR A CB    
2807 C  CG    . TYR C 41  ? 0.2409 0.2584 0.2356 -0.0055 0.0190  0.0087  40  TYR A CG    
2808 C  CD1   . TYR C 41  ? 0.2421 0.2656 0.2480 -0.0031 0.0118  0.0111  40  TYR A CD1   
2809 C  CD2   . TYR C 41  ? 0.2385 0.2555 0.2359 -0.0025 0.0253  0.0084  40  TYR A CD2   
2810 C  CE1   . TYR C 41  ? 0.2859 0.3104 0.3025 0.0016  0.0114  0.0112  40  TYR A CE1   
2811 C  CE2   . TYR C 41  ? 0.2523 0.2739 0.2618 0.0007  0.0233  0.0090  40  TYR A CE2   
2812 C  CZ    . TYR C 41  ? 0.2648 0.2877 0.2819 0.0023  0.0165  0.0096  40  TYR A CZ    
2813 O  OH    . TYR C 41  ? 0.2681 0.2913 0.2953 0.0048  0.0145  0.0078  40  TYR A OH    
2814 N  N     . ARG C 42  ? 0.3009 0.3045 0.2523 -0.0287 0.0076  0.0008  41  ARG A N     
2815 C  CA    . ARG C 42  ? 0.2911 0.2879 0.2293 -0.0385 0.0042  -0.0062 41  ARG A CA    
2816 C  C     . ARG C 42  ? 0.2661 0.2718 0.2253 -0.0411 0.0007  -0.0065 41  ARG A C     
2817 O  O     . ARG C 42  ? 0.2599 0.2821 0.2389 -0.0375 -0.0052 -0.0003 41  ARG A O     
2818 C  CB    . ARG C 42  ? 0.3161 0.3163 0.2374 -0.0457 -0.0083 -0.0044 41  ARG A CB    
2819 C  CG    . ARG C 42  ? 0.3473 0.3365 0.2390 -0.0463 -0.0035 -0.0049 41  ARG A CG    
2820 C  CD    . ARG C 42  ? 0.4358 0.4068 0.3052 -0.0521 0.0044  -0.0179 41  ARG A CD    
2821 N  NE    . ARG C 42  ? 0.4630 0.4227 0.3023 -0.0519 0.0131  -0.0208 41  ARG A NE    
2822 C  CZ    . ARG C 42  ? 0.5375 0.4927 0.3452 -0.0600 0.0066  -0.0244 41  ARG A CZ    
2823 N  NH1   . ARG C 42  ? 0.4861 0.4500 0.2903 -0.0690 -0.0115 -0.0240 41  ARG A NH1   
2824 N  NH2   . ARG C 42  ? 0.5486 0.4921 0.3272 -0.0589 0.0188  -0.0286 41  ARG A NH2   
2825 N  N     . LYS C 43  ? 0.2687 0.2628 0.2250 -0.0468 0.0058  -0.0133 42  LYS A N     
2826 C  CA    . LYS C 43  ? 0.2886 0.2914 0.2653 -0.0517 0.0035  -0.0122 42  LYS A CA    
2827 C  C     . LYS C 43  ? 0.2851 0.2711 0.2516 -0.0642 0.0039  -0.0212 42  LYS A C     
2828 O  O     . LYS C 43  ? 0.3289 0.2924 0.2789 -0.0631 0.0135  -0.0278 42  LYS A O     
2829 C  CB    . LYS C 43  ? 0.2691 0.2753 0.2624 -0.0424 0.0138  -0.0074 42  LYS A CB    
2830 C  CG    . LYS C 43  ? 0.2778 0.2955 0.2924 -0.0474 0.0135  -0.0041 42  LYS A CG    
2831 C  CD    . LYS C 43  ? 0.2909 0.3087 0.3142 -0.0386 0.0251  0.0009  42  LYS A CD    
2832 C  CE    . LYS C 43  ? 0.3040 0.3383 0.3486 -0.0426 0.0260  0.0063  42  LYS A CE    
2833 N  NZ    . LYS C 43  ? 0.3558 0.3864 0.4024 -0.0361 0.0379  0.0118  42  LYS A NZ    
2834 N  N     . GLN C 44  ? 0.3128 0.3087 0.2896 -0.0763 -0.0066 -0.0222 43  GLN A N     
2835 C  CA    . GLN C 44  ? 0.3125 0.2897 0.2830 -0.0898 -0.0056 -0.0315 43  GLN A CA    
2836 C  C     . GLN C 44  ? 0.3376 0.3151 0.3320 -0.0904 0.0033  -0.0263 43  GLN A C     
2837 O  O     . GLN C 44  ? 0.3096 0.3109 0.3284 -0.0862 0.0028  -0.0165 43  GLN A O     
2838 C  CB    . GLN C 44  ? 0.3281 0.3154 0.2968 -0.1059 -0.0228 -0.0363 43  GLN A CB    
2839 C  CG    . GLN C 44  ? 0.3615 0.3813 0.3633 -0.1089 -0.0324 -0.0267 43  GLN A CG    
2840 C  CD    . GLN C 44  ? 0.3329 0.3635 0.3371 -0.1275 -0.0504 -0.0318 43  GLN A CD    
2841 O  OE1   . GLN C 44  ? 0.3646 0.3764 0.3591 -0.1431 -0.0522 -0.0431 43  GLN A OE1   
2842 N  NE2   . GLN C 44  ? 0.3808 0.4410 0.3968 -0.1259 -0.0654 -0.0239 43  GLN A NE2   
2843 N  N     . VAL C 45  ? 0.3429 0.2925 0.3292 -0.0950 0.0126  -0.0325 44  VAL A N     
2844 C  CA    . VAL C 45  ? 0.3752 0.3193 0.3799 -0.0945 0.0233  -0.0254 44  VAL A CA    
2845 C  C     . VAL C 45  ? 0.4351 0.3499 0.4343 -0.1097 0.0252  -0.0348 44  VAL A C     
2846 O  O     . VAL C 45  ? 0.4546 0.3482 0.4305 -0.1160 0.0221  -0.0485 44  VAL A O     
2847 C  CB    . VAL C 45  ? 0.3787 0.3143 0.3797 -0.0766 0.0372  -0.0188 44  VAL A CB    
2848 C  CG1   . VAL C 45  ? 0.3565 0.3180 0.3621 -0.0627 0.0351  -0.0115 44  VAL A CG1   
2849 C  CG2   . VAL C 45  ? 0.3943 0.3006 0.3717 -0.0722 0.0440  -0.0283 44  VAL A CG2   
2850 N  N     . VAL C 46  ? 0.4343 0.3463 0.4539 -0.1162 0.0312  -0.0276 45  VAL A N     
2851 C  CA    . VAL C 46  ? 0.4722 0.3506 0.4895 -0.1300 0.0358  -0.0348 45  VAL A CA    
2852 C  C     . VAL C 46  ? 0.5382 0.3894 0.5509 -0.1162 0.0530  -0.0287 45  VAL A C     
2853 O  O     . VAL C 46  ? 0.5164 0.3803 0.5442 -0.1068 0.0608  -0.0130 45  VAL A O     
2854 C  CB    . VAL C 46  ? 0.5023 0.3937 0.5482 -0.1485 0.0316  -0.0290 45  VAL A CB    
2855 C  CG1   . VAL C 46  ? 0.5473 0.3982 0.5910 -0.1643 0.0368  -0.0369 45  VAL A CG1   
2856 C  CG2   . VAL C 46  ? 0.4554 0.3787 0.5103 -0.1610 0.0129  -0.0334 45  VAL A CG2   
2857 N  N     . ILE C 47  ? 0.5518 0.3665 0.5435 -0.1141 0.0592  -0.0406 46  ILE A N     
2858 C  CA    . ILE C 47  ? 0.5798 0.3673 0.5696 -0.0998 0.0752  -0.0344 46  ILE A CA    
2859 C  C     . ILE C 47  ? 0.6641 0.4069 0.6501 -0.1127 0.0809  -0.0444 46  ILE A C     
2860 O  O     . ILE C 47  ? 0.6827 0.4010 0.6475 -0.1194 0.0787  -0.0638 46  ILE A O     
2861 C  CB    . ILE C 47  ? 0.5551 0.3407 0.5272 -0.0800 0.0808  -0.0376 46  ILE A CB    
2862 C  CG1   . ILE C 47  ? 0.4481 0.2749 0.4267 -0.0686 0.0754  -0.0270 46  ILE A CG1   
2863 C  CG2   . ILE C 47  ? 0.5716 0.3287 0.5444 -0.0650 0.0965  -0.0316 46  ILE A CG2   
2864 C  CD1   . ILE C 47  ? 0.4530 0.2829 0.4169 -0.0526 0.0790  -0.0305 46  ILE A CD1   
2865 N  N     . ASP C 48  ? 0.6053 0.3355 0.6102 -0.1165 0.0886  -0.0313 47  ASP A N     
2866 C  CA    . ASP C 48  ? 0.6438 0.3287 0.6489 -0.1308 0.0941  -0.0395 47  ASP A CA    
2867 C  C     . ASP C 48  ? 0.6850 0.3718 0.6889 -0.1569 0.0789  -0.0562 47  ASP A C     
2868 O  O     . ASP C 48  ? 0.6971 0.3564 0.6858 -0.1632 0.0750  -0.0735 47  ASP A O     
2869 C  CB    . ASP C 48  ? 0.6937 0.3393 0.6787 -0.1156 0.1049  -0.0500 47  ASP A CB    
2870 C  CG    . ASP C 48  ? 0.6940 0.3376 0.6853 -0.0905 0.1189  -0.0315 47  ASP A CG    
2871 O  OD1   . ASP C 48  ? 0.6661 0.3267 0.6762 -0.0879 0.1214  -0.0099 47  ASP A OD1   
2872 O  OD2   . ASP C 48  ? 0.7165 0.3468 0.6940 -0.0727 0.1265  -0.0378 47  ASP A OD2   
2873 N  N     . GLY C 49  ? 0.6361 0.3636 0.6583 -0.1688 0.0676  -0.0493 48  GLY A N     
2874 C  CA    . GLY C 49  ? 0.6740 0.4101 0.6989 -0.1927 0.0505  -0.0629 48  GLY A CA    
2875 C  C     . GLY C 49  ? 0.6788 0.4133 0.6730 -0.1951 0.0386  -0.0845 48  GLY A C     
2876 O  O     . GLY C 49  ? 0.7576 0.4967 0.7495 -0.2119 0.0224  -0.0967 48  GLY A O     
2877 N  N     . GLU C 50  ? 0.6932 0.4281 0.6649 -0.1747 0.0444  -0.0865 49  GLU A N     
2878 C  CA    . GLU C 50  ? 0.6953 0.4300 0.6344 -0.1740 0.0357  -0.1040 49  GLU A CA    
2879 C  C     . GLU C 50  ? 0.6472 0.4279 0.5893 -0.1609 0.0284  -0.0924 49  GLU A C     
2880 O  O     . GLU C 50  ? 0.6633 0.4538 0.6111 -0.1404 0.0390  -0.0792 49  GLU A O     
2881 C  CB    . GLU C 50  ? 0.7519 0.4457 0.6628 -0.1594 0.0514  -0.1159 49  GLU A CB    
2882 C  CG    . GLU C 50  ? 0.8656 0.5467 0.7405 -0.1635 0.0444  -0.1380 49  GLU A CG    
2883 C  CD    . GLU C 50  ? 1.0642 0.7032 0.9263 -0.1586 0.0549  -0.1508 49  GLU A CD    
2884 O  OE1   . GLU C 50  ? 1.0500 0.6676 0.9289 -0.1483 0.0695  -0.1415 49  GLU A OE1   
2885 O  OE2   . GLU C 50  ? 1.0848 0.7127 0.9207 -0.1649 0.0479  -0.1693 49  GLU A OE2   
2886 N  N     . THR C 51  ? 0.5812 0.3900 0.5208 -0.1729 0.0095  -0.0965 50  THR A N     
2887 C  CA    . THR C 51  ? 0.5502 0.3976 0.4917 -0.1598 0.0029  -0.0857 50  THR A CA    
2888 C  C     . THR C 51  ? 0.5653 0.3997 0.4724 -0.1457 0.0088  -0.0934 50  THR A C     
2889 O  O     . THR C 51  ? 0.5710 0.3829 0.4469 -0.1535 0.0061  -0.1109 50  THR A O     
2890 C  CB    . THR C 51  ? 0.5550 0.4368 0.5060 -0.1745 -0.0191 -0.0853 50  THR A CB    
2891 O  OG1   . THR C 51  ? 0.5778 0.4729 0.5636 -0.1892 -0.0233 -0.0787 50  THR A OG1   
2892 C  CG2   . THR C 51  ? 0.5055 0.4257 0.4650 -0.1590 -0.0242 -0.0710 50  THR A CG2   
2893 N  N     . CYS C 52  ? 0.4825 0.3325 0.3946 -0.1258 0.0168  -0.0810 51  CYS A N     
2894 C  CA    . CYS C 52  ? 0.5171 0.3623 0.4014 -0.1138 0.0216  -0.0857 51  CYS A CA    
2895 C  C     . CYS C 52  ? 0.4790 0.3587 0.3736 -0.1020 0.0169  -0.0713 51  CYS A C     
2896 O  O     . CYS C 52  ? 0.4204 0.3244 0.3428 -0.1001 0.0126  -0.0587 51  CYS A O     
2897 C  CB    . CYS C 52  ? 0.5838 0.3998 0.4602 -0.1000 0.0417  -0.0889 51  CYS A CB    
2898 S  SG    . CYS C 52  ? 0.5468 0.3745 0.4565 -0.0850 0.0519  -0.0695 51  CYS A SG    
2899 N  N     . LEU C 53  ? 0.4566 0.3361 0.3278 -0.0940 0.0193  -0.0736 52  LEU A N     
2900 C  CA    . LEU C 53  ? 0.4557 0.3615 0.3317 -0.0842 0.0151  -0.0615 52  LEU A CA    
2901 C  C     . LEU C 53  ? 0.4312 0.3325 0.3104 -0.0673 0.0314  -0.0563 52  LEU A C     
2902 O  O     . LEU C 53  ? 0.4536 0.3345 0.3136 -0.0629 0.0434  -0.0645 52  LEU A O     
2903 C  CB    . LEU C 53  ? 0.4340 0.3448 0.2815 -0.0901 0.0045  -0.0658 52  LEU A CB    
2904 C  CG    . LEU C 53  ? 0.4316 0.3694 0.2859 -0.0832 -0.0039 -0.0515 52  LEU A CG    
2905 C  CD1   . LEU C 53  ? 0.3978 0.3606 0.2880 -0.0801 -0.0115 -0.0390 52  LEU A CD1   
2906 C  CD2   . LEU C 53  ? 0.5039 0.4462 0.3283 -0.0917 -0.0175 -0.0540 52  LEU A CD2   
2907 N  N     . LEU C 54  ? 0.3564 0.2763 0.2607 -0.0581 0.0322  -0.0437 53  LEU A N     
2908 C  CA    . LEU C 54  ? 0.3725 0.2940 0.2829 -0.0434 0.0441  -0.0378 53  LEU A CA    
2909 C  C     . LEU C 54  ? 0.3962 0.3342 0.3023 -0.0390 0.0400  -0.0318 53  LEU A C     
2910 O  O     . LEU C 54  ? 0.3444 0.3003 0.2605 -0.0410 0.0287  -0.0252 53  LEU A O     
2911 C  CB    . LEU C 54  ? 0.3328 0.2638 0.2692 -0.0364 0.0470  -0.0285 53  LEU A CB    
2912 C  CG    . LEU C 54  ? 0.3657 0.2831 0.3110 -0.0412 0.0506  -0.0295 53  LEU A CG    
2913 C  CD1   . LEU C 54  ? 0.3701 0.2999 0.3362 -0.0316 0.0548  -0.0177 53  LEU A CD1   
2914 C  CD2   . LEU C 54  ? 0.4059 0.2931 0.3374 -0.0409 0.0615  -0.0385 53  LEU A CD2   
2915 N  N     . ASP C 55  ? 0.3537 0.2852 0.2467 -0.0328 0.0502  -0.0334 54  ASP A N     
2916 C  CA    . ASP C 55  ? 0.3350 0.2798 0.2265 -0.0286 0.0497  -0.0260 54  ASP A CA    
2917 C  C     . ASP C 55  ? 0.3374 0.2888 0.2488 -0.0172 0.0595  -0.0202 54  ASP A C     
2918 O  O     . ASP C 55  ? 0.3679 0.3093 0.2785 -0.0111 0.0721  -0.0239 54  ASP A O     
2919 C  CB    . ASP C 55  ? 0.3729 0.3082 0.2337 -0.0319 0.0545  -0.0314 54  ASP A CB    
2920 C  CG    . ASP C 55  ? 0.4636 0.4122 0.3232 -0.0294 0.0539  -0.0212 54  ASP A CG    
2921 O  OD1   . ASP C 55  ? 0.4677 0.4226 0.3429 -0.0214 0.0634  -0.0161 54  ASP A OD1   
2922 O  OD2   . ASP C 55  ? 0.5202 0.4734 0.3648 -0.0357 0.0436  -0.0173 54  ASP A OD2   
2923 N  N     . ILE C 56  ? 0.3341 0.3022 0.2649 -0.0141 0.0530  -0.0118 55  ILE A N     
2924 C  CA    . ILE C 56  ? 0.2728 0.2500 0.2237 -0.0050 0.0581  -0.0068 55  ILE A CA    
2925 C  C     . ILE C 56  ? 0.2953 0.2837 0.2514 -0.0035 0.0581  -0.0010 55  ILE A C     
2926 O  O     . ILE C 56  ? 0.2860 0.2799 0.2425 -0.0073 0.0493  0.0027  55  ILE A O     
2927 C  CB    . ILE C 56  ? 0.2730 0.2591 0.2405 -0.0035 0.0510  -0.0036 55  ILE A CB    
2928 C  CG1   . ILE C 56  ? 0.3564 0.3334 0.3206 -0.0088 0.0491  -0.0074 55  ILE A CG1   
2929 C  CG2   . ILE C 56  ? 0.2736 0.2681 0.2567 0.0055  0.0556  0.0005  55  ILE A CG2   
2930 C  CD1   . ILE C 56  ? 0.3489 0.3117 0.3113 -0.0054 0.0589  -0.0100 55  ILE A CD1   
2931 N  N     . LEU C 57  ? 0.2744 0.2667 0.2376 0.0022  0.0681  0.0007  56  LEU A N     
2932 C  CA    . LEU C 57  ? 0.2290 0.2335 0.2023 0.0021  0.0686  0.0069  56  LEU A CA    
2933 C  C     . LEU C 57  ? 0.2600 0.2778 0.2571 0.0075  0.0660  0.0097  56  LEU A C     
2934 O  O     . LEU C 57  ? 0.2377 0.2579 0.2429 0.0144  0.0721  0.0094  56  LEU A O     
2935 C  CB    . LEU C 57  ? 0.2671 0.2704 0.2325 0.0032  0.0825  0.0074  56  LEU A CB    
2936 C  CG    . LEU C 57  ? 0.2625 0.2789 0.2400 0.0005  0.0839  0.0156  56  LEU A CG    
2937 C  CD1   . LEU C 57  ? 0.3367 0.3487 0.3017 -0.0075 0.0759  0.0205  56  LEU A CD1   
2938 C  CD2   . LEU C 57  ? 0.3070 0.3283 0.2850 0.0040  0.1009  0.0169  56  LEU A CD2   
2939 N  N     . ASP C 58  ? 0.2160 0.2413 0.2231 0.0047  0.0564  0.0122  57  ASP A N     
2940 C  CA    . ASP C 58  ? 0.2248 0.2627 0.2503 0.0078  0.0514  0.0131  57  ASP A CA    
2941 C  C     . ASP C 58  ? 0.2135 0.2619 0.2530 0.0047  0.0530  0.0171  57  ASP A C     
2942 O  O     . ASP C 58  ? 0.2037 0.2477 0.2404 -0.0016 0.0515  0.0198  57  ASP A O     
2943 C  CB    . ASP C 58  ? 0.1931 0.2293 0.2181 0.0064  0.0408  0.0106  57  ASP A CB    
2944 C  CG    . ASP C 58  ? 0.1920 0.2393 0.2296 0.0090  0.0348  0.0090  57  ASP A CG    
2945 O  OD1   . ASP C 58  ? 0.2154 0.2729 0.2611 0.0131  0.0367  0.0105  57  ASP A OD1   
2946 O  OD2   . ASP C 58  ? 0.2213 0.2670 0.2597 0.0077  0.0276  0.0058  57  ASP A OD2   
2947 N  N     . THR C 59  ? 0.2138 0.2770 0.2702 0.0087  0.0563  0.0192  58  THR A N     
2948 C  CA    . THR C 59  ? 0.1871 0.2635 0.2602 0.0052  0.0614  0.0241  58  THR A CA    
2949 C  C     . THR C 59  ? 0.1987 0.2910 0.2933 0.0018  0.0510  0.0242  58  THR A C     
2950 O  O     . THR C 59  ? 0.1829 0.2780 0.2778 0.0048  0.0414  0.0202  58  THR A O     
2951 C  CB    . THR C 59  ? 0.2370 0.3219 0.3170 0.0127  0.0751  0.0270  58  THR A CB    
2952 O  OG1   . THR C 59  ? 0.2146 0.3093 0.3060 0.0213  0.0714  0.0271  58  THR A OG1   
2953 C  CG2   . THR C 59  ? 0.2117 0.2774 0.2667 0.0154  0.0856  0.0237  58  THR A CG2   
2954 N  N     . ALA C 60  ? 0.1813 0.2846 0.2934 -0.0050 0.0536  0.0288  59  ALA A N     
2955 C  CA    . ALA C 60  ? 0.1983 0.3187 0.3341 -0.0109 0.0437  0.0284  59  ALA A CA    
2956 C  C     . ALA C 60  ? 0.2387 0.3851 0.3966 -0.0045 0.0464  0.0325  59  ALA A C     
2957 O  O     . ALA C 60  ? 0.2070 0.3614 0.3725 -0.0002 0.0603  0.0383  59  ALA A O     
2958 C  CB    . ALA C 60  ? 0.2082 0.3277 0.3557 -0.0232 0.0457  0.0329  59  ALA A CB    
2959 N  N     . GLY C 61  ? 0.2180 0.3785 0.3857 -0.0032 0.0331  0.0296  60  GLY A N     
2960 C  CA    . GLY C 61  ? 0.2285 0.4183 0.4222 0.0024  0.0330  0.0357  60  GLY A CA    
2961 C  C     . GLY C 61  ? 0.2305 0.4453 0.4564 -0.0087 0.0271  0.0384  60  GLY A C     
2962 O  O     . GLY C 61  ? 0.2846 0.5289 0.5374 -0.0040 0.0266  0.0449  60  GLY A O     
2963 N  N     . GLN C 62  ? 0.1944 0.3990 0.4215 -0.0233 0.0232  0.0349  61  GLN A N     
2964 C  CA    . GLN C 62  ? 0.2454 0.4704 0.5041 -0.0378 0.0161  0.0364  61  GLN A CA    
2965 C  C     . GLN C 62  ? 0.2611 0.5189 0.5537 -0.0352 0.0268  0.0478  61  GLN A C     
2966 O  O     . GLN C 62  ? 0.2315 0.4861 0.5225 -0.0302 0.0460  0.0547  61  GLN A O     
2967 C  CB    . GLN C 62  ? 0.2204 0.4233 0.4754 -0.0519 0.0195  0.0359  61  GLN A CB    
2968 C  CG    . GLN C 62  ? 0.3054 0.4759 0.5310 -0.0529 0.0114  0.0259  61  GLN A CG    
2969 C  CD    . GLN C 62  ? 0.2744 0.4420 0.5077 -0.0649 -0.0057 0.0156  61  GLN A CD    
2970 O  OE1   . GLN C 62  ? 0.3368 0.4794 0.5478 -0.0641 -0.0125 0.0056  61  GLN A OE1   
2971 N  NE2   . GLN C 62  ? 0.3065 0.4988 0.5720 -0.0767 -0.0125 0.0171  61  GLN A NE2   
2972 N  N     . GLU C 63  ? 0.2202 0.5113 0.5443 -0.0390 0.0146  0.0494  62  GLU A N     
2973 C  CA    . GLU C 63  ? 0.2529 0.5750 0.6078 -0.0328 0.0252  0.0597  62  GLU A CA    
2974 C  C     . GLU C 63  ? 0.2063 0.5286 0.5747 -0.0449 0.0383  0.0639  62  GLU A C     
2975 O  O     . GLU C 63  ? 0.1916 0.5232 0.5671 -0.0370 0.0544  0.0698  62  GLU A O     
2976 C  CB    . GLU C 63  ? 0.2530 0.6054 0.6290 -0.0316 0.0068  0.0586  62  GLU A CB    
2977 C  CG    . GLU C 63  ? 0.3222 0.6754 0.6826 -0.0120 0.0027  0.0602  62  GLU A CG    
2978 C  CD    . GLU C 63  ? 0.4654 0.8484 0.8457 -0.0042 -0.0096 0.0640  62  GLU A CD    
2979 O  OE1   . GLU C 63  ? 0.4959 0.9005 0.8947 -0.0166 -0.0276 0.0603  62  GLU A OE1   
2980 O  OE2   . GLU C 63  ? 0.4743 0.8567 0.8499 0.0147  -0.0017 0.0705  62  GLU A OE2   
2981 N  N     . GLU C 64  ? 0.1797 0.4891 0.5497 -0.0636 0.0324  0.0611  63  GLU A N     
2982 C  CA    . GLU C 64  ? 0.2213 0.5289 0.6020 -0.0760 0.0446  0.0670  63  GLU A CA    
2983 C  C     . GLU C 64  ? 0.2154 0.5065 0.5738 -0.0666 0.0685  0.0739  63  GLU A C     
2984 O  O     . GLU C 64  ? 0.2019 0.5004 0.5690 -0.0705 0.0827  0.0806  63  GLU A O     
2985 C  CB    . GLU C 64  ? 0.1851 0.4720 0.5659 -0.0966 0.0334  0.0625  63  GLU A CB    
2986 C  CG    . GLU C 64  ? 0.2914 0.5701 0.6797 -0.1111 0.0452  0.0701  63  GLU A CG    
2987 C  CD    . GLU C 64  ? 0.2928 0.6033 0.7158 -0.1206 0.0446  0.0730  63  GLU A CD    
2988 O  OE1   . GLU C 64  ? 0.3431 0.6594 0.7734 -0.1236 0.0620  0.0828  63  GLU A OE1   
2989 O  OE2   . GLU C 64  ? 0.3722 0.7027 0.8156 -0.1267 0.0262  0.0654  63  GLU A OE2   
2990 N  N     . TYR C 65  ? 0.2304 0.5009 0.5595 -0.0545 0.0730  0.0716  64  TYR A N     
2991 C  CA    . TYR C 65  ? 0.2796 0.5289 0.5792 -0.0472 0.0927  0.0751  64  TYR A CA    
2992 C  C     . TYR C 65  ? 0.2641 0.5164 0.5517 -0.0273 0.1033  0.0731  64  TYR A C     
2993 O  O     . TYR C 65  ? 0.2507 0.4806 0.5070 -0.0197 0.1147  0.0714  64  TYR A O     
2994 C  CB    . TYR C 65  ? 0.2398 0.4555 0.5089 -0.0510 0.0885  0.0721  64  TYR A CB    
2995 C  CG    . TYR C 65  ? 0.2137 0.4183 0.4917 -0.0691 0.0749  0.0712  64  TYR A CG    
2996 C  CD1   . TYR C 65  ? 0.2244 0.4346 0.5215 -0.0834 0.0821  0.0806  64  TYR A CD1   
2997 C  CD2   . TYR C 65  ? 0.1864 0.3723 0.4513 -0.0709 0.0550  0.0594  64  TYR A CD2   
2998 C  CE1   . TYR C 65  ? 0.2432 0.4406 0.5519 -0.1008 0.0705  0.0800  64  TYR A CE1   
2999 C  CE2   . TYR C 65  ? 0.1887 0.3620 0.4638 -0.0871 0.0434  0.0566  64  TYR A CE2   
3000 C  CZ    . TYR C 65  ? 0.2032 0.3803 0.5005 -0.1022 0.0510  0.0672  64  TYR A CZ    
3001 O  OH    . TYR C 65  ? 0.2194 0.3804 0.5291 -0.1193 0.0407  0.0651  64  TYR A OH    
3002 N  N     . SER C 66  ? 0.2286 0.5060 0.5398 -0.0189 0.0984  0.0728  65  SER A N     
3003 C  CA    . SER C 66  ? 0.2638 0.5395 0.5653 0.0006  0.1064  0.0710  65  SER A CA    
3004 C  C     . SER C 66  ? 0.3019 0.5689 0.5890 0.0069  0.1286  0.0720  65  SER A C     
3005 O  O     . SER C 66  ? 0.3439 0.5928 0.6076 0.0201  0.1375  0.0677  65  SER A O     
3006 C  CB    . SER C 66  ? 0.2777 0.5834 0.6105 0.0077  0.0960  0.0731  65  SER A CB    
3007 O  OG    . SER C 66  ? 0.2643 0.5967 0.6286 -0.0012 0.0973  0.0778  65  SER A OG    
3008 N  N     . ALA C 67  ? 0.2929 0.5711 0.5920 -0.0030 0.1377  0.0772  66  ALA A N     
3009 C  CA    . ALA C 67  ? 0.3333 0.6059 0.6177 0.0028  0.1591  0.0779  66  ALA A CA    
3010 C  C     . ALA C 67  ? 0.3590 0.6012 0.6021 -0.0017 0.1676  0.0760  66  ALA A C     
3011 O  O     . ALA C 67  ? 0.4089 0.6446 0.6333 0.0023  0.1845  0.0753  66  ALA A O     
3012 C  CB    . ALA C 67  ? 0.2533 0.5535 0.5679 -0.0053 0.1671  0.0852  66  ALA A CB    
3013 N  N     . MET C 68  ? 0.3527 0.5773 0.5810 -0.0097 0.1561  0.0752  67  MET A N     
3014 C  CA    . MET C 68  ? 0.3501 0.5458 0.5387 -0.0131 0.1608  0.0741  67  MET A CA    
3015 C  C     . MET C 68  ? 0.3917 0.5659 0.5533 -0.0022 0.1577  0.0652  67  MET A C     
3016 O  O     . MET C 68  ? 0.4077 0.5585 0.5373 -0.0054 0.1576  0.0636  67  MET A O     
3017 C  CB    . MET C 68  ? 0.3601 0.5486 0.5513 -0.0292 0.1507  0.0804  67  MET A CB    
3018 C  CG    . MET C 68  ? 0.4163 0.6269 0.6421 -0.0414 0.1493  0.0878  67  MET A CG    
3019 S  SD    . MET C 68  ? 0.4393 0.6308 0.6611 -0.0603 0.1402  0.0952  67  MET A SD    
3020 C  CE    . MET C 68  ? 0.4579 0.6261 0.6339 -0.0595 0.1565  0.1010  67  MET A CE    
3021 N  N     . ARG C 69  ? 0.3900 0.5716 0.5647 0.0100  0.1542  0.0604  68  ARG A N     
3022 C  CA    . ARG C 69  ? 0.3891 0.5492 0.5399 0.0197  0.1516  0.0524  68  ARG A CA    
3023 C  C     . ARG C 69  ? 0.4192 0.5595 0.5389 0.0272  0.1662  0.0455  68  ARG A C     
3024 O  O     . ARG C 69  ? 0.4197 0.5369 0.5140 0.0321  0.1648  0.0378  68  ARG A O     
3025 C  CB    . ARG C 69  ? 0.3652 0.5380 0.5392 0.0302  0.1427  0.0516  68  ARG A CB    
3026 C  CG    . ARG C 69  ? 0.3710 0.5607 0.5690 0.0231  0.1248  0.0554  68  ARG A CG    
3027 C  CD    . ARG C 69  ? 0.3495 0.5579 0.5713 0.0337  0.1163  0.0570  68  ARG A CD    
3028 N  NE    . ARG C 69  ? 0.3045 0.5335 0.5492 0.0260  0.0976  0.0597  68  ARG A NE    
3029 C  CZ    . ARG C 69  ? 0.3109 0.5649 0.5816 0.0304  0.0871  0.0631  68  ARG A CZ    
3030 N  NH1   . ARG C 69  ? 0.3026 0.5637 0.5824 0.0436  0.0939  0.0658  68  ARG A NH1   
3031 N  NH2   . ARG C 69  ? 0.3092 0.5813 0.5969 0.0209  0.0684  0.0635  68  ARG A NH2   
3032 N  N     . ASP C 70  ? 0.4258 0.5749 0.5468 0.0268  0.1798  0.0477  69  ASP A N     
3033 C  CA    . ASP C 70  ? 0.4955 0.6323 0.5959 0.0366  0.1944  0.0400  69  ASP A CA    
3034 C  C     . ASP C 70  ? 0.5478 0.6550 0.6018 0.0330  0.1965  0.0325  69  ASP A C     
3035 O  O     . ASP C 70  ? 0.5700 0.6567 0.6032 0.0411  0.1999  0.0221  69  ASP A O     
3036 C  CB    . ASP C 70  ? 0.4696 0.6272 0.5848 0.0366  0.2093  0.0448  69  ASP A CB    
3037 C  CG    . ASP C 70  ? 0.4738 0.6638 0.6380 0.0407  0.2065  0.0519  69  ASP A CG    
3038 O  OD1   . ASP C 70  ? 0.4524 0.6494 0.6376 0.0439  0.1925  0.0534  69  ASP A OD1   
3039 O  OD2   . ASP C 70  ? 0.4864 0.6965 0.6683 0.0413  0.2185  0.0562  69  ASP A OD2   
3040 N  N     . GLN C 71  ? 0.5183 0.6219 0.5555 0.0204  0.1935  0.0379  70  GLN A N     
3041 C  CA    . GLN C 71  ? 0.5909 0.6694 0.5828 0.0169  0.1944  0.0316  70  GLN A CA    
3042 C  C     . GLN C 71  ? 0.5638 0.6211 0.5409 0.0195  0.1835  0.0231  70  GLN A C     
3043 O  O     . GLN C 71  ? 0.5796 0.6155 0.5251 0.0219  0.1860  0.0123  70  GLN A O     
3044 C  CB    . GLN C 71  ? 0.6489 0.7266 0.6251 0.0034  0.1913  0.0418  70  GLN A CB    
3045 C  CG    . GLN C 71  ? 0.6986 0.7523 0.6258 -0.0009 0.1886  0.0370  70  GLN A CG    
3046 C  CD    . GLN C 71  ? 0.7894 0.8291 0.6852 0.0062  0.1980  0.0228  70  GLN A CD    
3047 O  OE1   . GLN C 71  ? 0.7422 0.7847 0.6511 0.0164  0.2073  0.0149  70  GLN A OE1   
3048 N  NE2   . GLN C 71  ? 0.8916 0.9152 0.7451 0.0004  0.1945  0.0198  70  GLN A NE2   
3049 N  N     . TYR C 72  ? 0.5300 0.5927 0.5286 0.0180  0.1712  0.0273  71  TYR A N     
3050 C  CA    . TYR C 72  ? 0.4922 0.5354 0.4758 0.0199  0.1624  0.0196  71  TYR A CA    
3051 C  C     . TYR C 72  ? 0.4882 0.5238 0.4772 0.0322  0.1666  0.0108  71  TYR A C     
3052 O  O     . TYR C 72  ? 0.4529 0.4651 0.4184 0.0334  0.1654  0.0010  71  TYR A O     
3053 C  CB    . TYR C 72  ? 0.4288 0.4785 0.4301 0.0142  0.1438  0.0250  71  TYR A CB    
3054 C  CG    . TYR C 72  ? 0.3874 0.4565 0.4263 0.0196  0.1376  0.0285  71  TYR A CG    
3055 C  CD1   . TYR C 72  ? 0.3938 0.4606 0.4406 0.0306  0.1381  0.0240  71  TYR A CD1   
3056 C  CD2   . TYR C 72  ? 0.3737 0.4625 0.4391 0.0128  0.1300  0.0367  71  TYR A CD2   
3057 C  CE1   . TYR C 72  ? 0.3608 0.4471 0.4391 0.0356  0.1303  0.0288  71  TYR A CE1   
3058 C  CE2   . TYR C 72  ? 0.3820 0.4895 0.4783 0.0162  0.1215  0.0389  71  TYR A CE2   
3059 C  CZ    . TYR C 72  ? 0.3592 0.4670 0.4611 0.0281  0.1213  0.0355  71  TYR A CZ    
3060 O  OH    . TYR C 72  ? 0.3732 0.5019 0.5036 0.0319  0.1119  0.0393  71  TYR A OH    
3061 N  N     . MET C 73  ? 0.4839 0.5374 0.5028 0.0407  0.1721  0.0144  72  MET A N     
3062 C  CA    . MET C 73  ? 0.4451 0.4886 0.4688 0.0532  0.1770  0.0082  72  MET A CA    
3063 C  C     . MET C 73  ? 0.5018 0.5245 0.4965 0.0562  0.1899  -0.0027 72  MET A C     
3064 O  O     . MET C 73  ? 0.4531 0.4535 0.4375 0.0627  0.1924  -0.0114 72  MET A O     
3065 C  CB    . MET C 73  ? 0.3839 0.4532 0.4479 0.0623  0.1777  0.0163  72  MET A CB    
3066 C  CG    . MET C 73  ? 0.3298 0.4193 0.4215 0.0599  0.1624  0.0253  72  MET A CG    
3067 S  SD    . MET C 73  ? 0.3534 0.4769 0.4897 0.0687  0.1639  0.0345  72  MET A SD    
3068 C  CE    . MET C 73  ? 0.3591 0.5029 0.5199 0.0650  0.1432  0.0421  72  MET A CE    
3069 N  N     . ARG C 74  ? 0.4955 0.5238 0.4755 0.0508  0.1984  -0.0024 73  ARG A N     
3070 C  CA    . ARG C 74  ? 0.5533 0.5630 0.5018 0.0529  0.2102  -0.0137 73  ARG A CA    
3071 C  C     . ARG C 74  ? 0.5263 0.5069 0.4365 0.0457  0.2028  -0.0245 73  ARG A C     
3072 O  O     . ARG C 74  ? 0.5147 0.4718 0.4049 0.0496  0.2081  -0.0374 73  ARG A O     
3073 C  CB    . ARG C 74  ? 0.5724 0.5979 0.5126 0.0479  0.2203  -0.0090 73  ARG A CB    
3074 C  CG    . ARG C 74  ? 0.6251 0.6707 0.5927 0.0579  0.2351  -0.0059 73  ARG A CG    
3075 C  CD    . ARG C 74  ? 0.7257 0.7826 0.6773 0.0526  0.2478  -0.0033 73  ARG A CD    
3076 N  NE    . ARG C 74  ? 0.7177 0.7913 0.6773 0.0398  0.2398  0.0103  73  ARG A NE    
3077 C  CZ    . ARG C 74  ? 0.7180 0.8192 0.7142 0.0374  0.2413  0.0224  73  ARG A CZ    
3078 N  NH1   . ARG C 74  ? 0.7036 0.8230 0.7329 0.0475  0.2500  0.0235  73  ARG A NH1   
3079 N  NH2   . ARG C 74  ? 0.7517 0.8620 0.7525 0.0244  0.2334  0.0339  73  ARG A NH2   
3080 N  N     . THR C 75  ? 0.5109 0.4923 0.4116 0.0349  0.1903  -0.0195 74  THR A N     
3081 C  CA    . THR C 75  ? 0.5402 0.4975 0.4046 0.0264  0.1818  -0.0289 74  THR A CA    
3082 C  C     . THR C 75  ? 0.5234 0.4651 0.3949 0.0281  0.1736  -0.0344 74  THR A C     
3083 O  O     . THR C 75  ? 0.5173 0.4349 0.3618 0.0229  0.1697  -0.0463 74  THR A O     
3084 C  CB    . THR C 75  ? 0.5632 0.5278 0.4131 0.0143  0.1719  -0.0200 74  THR A CB    
3085 O  OG1   . THR C 75  ? 0.6294 0.6124 0.5124 0.0140  0.1657  -0.0074 74  THR A OG1   
3086 C  CG2   . THR C 75  ? 0.6397 0.6138 0.4726 0.0110  0.1802  -0.0151 74  THR A CG2   
3087 N  N     . GLY C 76  ? 0.4763 0.4317 0.3828 0.0340  0.1699  -0.0258 75  GLY A N     
3088 C  CA    . GLY C 76  ? 0.4383 0.3804 0.3511 0.0357  0.1629  -0.0290 75  GLY A CA    
3089 C  C     . GLY C 76  ? 0.4541 0.3716 0.3614 0.0429  0.1704  -0.0396 75  GLY A C     
3090 O  O     . GLY C 76  ? 0.4888 0.4073 0.4052 0.0526  0.1816  -0.0406 75  GLY A O     
3091 N  N     . GLU C 77  ? 0.4069 0.3012 0.3012 0.0377  0.1645  -0.0473 76  GLU A N     
3092 C  CA    . GLU C 77  ? 0.4441 0.3098 0.3335 0.0424  0.1709  -0.0573 76  GLU A CA    
3093 C  C     . GLU C 77  ? 0.4211 0.2869 0.3415 0.0535  0.1713  -0.0485 76  GLU A C     
3094 O  O     . GLU C 77  ? 0.4567 0.3085 0.3853 0.0634  0.1799  -0.0501 76  GLU A O     
3095 C  CB    . GLU C 77  ? 0.4873 0.3244 0.3454 0.0286  0.1643  -0.0717 76  GLU A CB    
3096 C  CG    . GLU C 77  ? 0.5285 0.3579 0.3503 0.0188  0.1639  -0.0833 76  GLU A CG    
3097 C  CD    . GLU C 77  ? 0.5966 0.4079 0.3896 0.0013  0.1505  -0.0948 76  GLU A CD    
3098 O  OE1   . GLU C 77  ? 0.7187 0.5220 0.4797 -0.0074 0.1475  -0.1053 76  GLU A OE1   
3099 O  OE2   . GLU C 77  ? 0.5582 0.3738 0.3679 -0.0051 0.1358  -0.0889 76  GLU A OE2   
3100 N  N     . GLY C 78  ? 0.4095 0.2937 0.3481 0.0517  0.1592  -0.0371 77  GLY A N     
3101 C  CA    . GLY C 78  ? 0.4104 0.3003 0.3774 0.0627  0.1580  -0.0258 77  GLY A CA    
3102 C  C     . GLY C 78  ? 0.3370 0.2614 0.3243 0.0614  0.1446  -0.0124 77  GLY A C     
3103 O  O     . GLY C 78  ? 0.3316 0.2688 0.3108 0.0505  0.1348  -0.0127 77  GLY A O     
3104 N  N     . PHE C 79  ? 0.3232 0.2614 0.3365 0.0731  0.1439  -0.0007 78  PHE A N     
3105 C  CA    . PHE C 79  ? 0.2981 0.2701 0.3317 0.0735  0.1327  0.0104  78  PHE A CA    
3106 C  C     . PHE C 79  ? 0.2993 0.2758 0.3436 0.0769  0.1222  0.0202  78  PHE A C     
3107 O  O     . PHE C 79  ? 0.2981 0.2654 0.3521 0.0885  0.1280  0.0262  78  PHE A O     
3108 C  CB    . PHE C 79  ? 0.3150 0.3101 0.3722 0.0847  0.1416  0.0164  78  PHE A CB    
3109 C  CG    . PHE C 79  ? 0.3223 0.3161 0.3676 0.0797  0.1507  0.0087  78  PHE A CG    
3110 C  CD1   . PHE C 79  ? 0.3344 0.3054 0.3656 0.0835  0.1631  -0.0001 78  PHE A CD1   
3111 C  CD2   . PHE C 79  ? 0.3534 0.3662 0.3986 0.0703  0.1468  0.0100  78  PHE A CD2   
3112 C  CE1   . PHE C 79  ? 0.3498 0.3202 0.3656 0.0787  0.1712  -0.0072 78  PHE A CE1   
3113 C  CE2   . PHE C 79  ? 0.3213 0.3321 0.3524 0.0652  0.1552  0.0048  78  PHE A CE2   
3114 C  CZ    . PHE C 79  ? 0.3810 0.3722 0.3965 0.0695  0.1671  -0.0037 78  PHE A CZ    
3115 N  N     . LEU C 80  ? 0.2713 0.2615 0.3133 0.0676  0.1076  0.0224  79  LEU A N     
3116 C  CA    . LEU C 80  ? 0.2507 0.2528 0.3015 0.0708  0.0974  0.0323  79  LEU A CA    
3117 C  C     . LEU C 80  ? 0.2481 0.2816 0.3198 0.0767  0.0917  0.0397  79  LEU A C     
3118 O  O     . LEU C 80  ? 0.2535 0.3031 0.3274 0.0688  0.0850  0.0365  79  LEU A O     
3119 C  CB    . LEU C 80  ? 0.2641 0.2673 0.3027 0.0591  0.0861  0.0296  79  LEU A CB    
3120 C  CG    . LEU C 80  ? 0.3161 0.2992 0.3421 0.0534  0.0861  0.0283  79  LEU A CG    
3121 C  CD1   . LEU C 80  ? 0.2765 0.2753 0.3007 0.0477  0.0748  0.0302  79  LEU A CD1   
3122 C  CD2   . LEU C 80  ? 0.3215 0.2871 0.3496 0.0607  0.0929  0.0354  79  LEU A CD2   
3123 N  N     . CYS C 81  ? 0.2417 0.2836 0.3301 0.0900  0.0937  0.0501  80  CYS A N     
3124 C  CA    . CYS C 81  ? 0.2331 0.3085 0.3448 0.0956  0.0863  0.0582  80  CYS A CA    
3125 C  C     . CYS C 81  ? 0.2332 0.3222 0.3418 0.0946  0.0706  0.0653  80  CYS A C     
3126 O  O     . CYS C 81  ? 0.2466 0.3310 0.3551 0.1039  0.0701  0.0756  80  CYS A O     
3127 C  CB    . CYS C 81  ? 0.2682 0.3489 0.4022 0.1123  0.0965  0.0668  80  CYS A CB    
3128 S  SG    . CYS C 81  ? 0.3110 0.3765 0.4436 0.1122  0.1152  0.0561  80  CYS A SG    
3129 N  N     . VAL C 82  ? 0.2043 0.3099 0.3102 0.0840  0.0585  0.0603  81  VAL A N     
3130 C  CA    . VAL C 82  ? 0.2251 0.3385 0.3191 0.0808  0.0452  0.0623  81  VAL A CA    
3131 C  C     . VAL C 82  ? 0.2240 0.3700 0.3339 0.0835  0.0316  0.0681  81  VAL A C     
3132 O  O     . VAL C 82  ? 0.2091 0.3728 0.3358 0.0785  0.0282  0.0642  81  VAL A O     
3133 C  CB    . VAL C 82  ? 0.2086 0.3135 0.2857 0.0675  0.0412  0.0504  81  VAL A CB    
3134 C  CG1   . VAL C 82  ? 0.2027 0.3130 0.2641 0.0657  0.0309  0.0512  81  VAL A CG1   
3135 C  CG2   . VAL C 82  ? 0.2457 0.3239 0.3108 0.0632  0.0521  0.0444  81  VAL A CG2   
3136 N  N     . PHE C 83  ? 0.2400 0.3950 0.3436 0.0899  0.0230  0.0775  82  PHE A N     
3137 C  CA    . PHE C 83  ? 0.2148 0.4008 0.3251 0.0888  0.0058  0.0801  82  PHE A CA    
3138 C  C     . PHE C 83  ? 0.2574 0.4401 0.3391 0.0852  -0.0026 0.0782  82  PHE A C     
3139 O  O     . PHE C 83  ? 0.2507 0.4106 0.3138 0.0854  0.0062  0.0784  82  PHE A O     
3140 C  CB    . PHE C 83  ? 0.1920 0.4009 0.3252 0.1029  0.0017  0.0964  82  PHE A CB    
3141 C  CG    . PHE C 83  ? 0.2641 0.4618 0.3866 0.1158  0.0049  0.1115  82  PHE A CG    
3142 C  CD1   . PHE C 83  ? 0.2637 0.4334 0.3884 0.1242  0.0223  0.1164  82  PHE A CD1   
3143 C  CD2   . PHE C 83  ? 0.2353 0.4480 0.3427 0.1188  -0.0093 0.1209  82  PHE A CD2   
3144 C  CE1   . PHE C 83  ? 0.2549 0.4102 0.3713 0.1354  0.0261  0.1316  82  PHE A CE1   
3145 C  CE2   . PHE C 83  ? 0.2883 0.4888 0.3843 0.1304  -0.0054 0.1377  82  PHE A CE2   
3146 C  CZ    . PHE C 83  ? 0.3035 0.4743 0.4057 0.1386  0.0125  0.1438  82  PHE A CZ    
3147 N  N     . ALA C 84  ? 0.2544 0.4606 0.3326 0.0812  -0.0191 0.0756  83  ALA A N     
3148 C  CA    . ALA C 84  ? 0.2839 0.4895 0.3320 0.0789  -0.0265 0.0731  83  ALA A CA    
3149 C  C     . ALA C 84  ? 0.3083 0.5336 0.3523 0.0897  -0.0366 0.0900  83  ALA A C     
3150 O  O     . ALA C 84  ? 0.2825 0.5342 0.3481 0.0936  -0.0477 0.0970  83  ALA A O     
3151 C  CB    . ALA C 84  ? 0.2851 0.4981 0.3248 0.0661  -0.0378 0.0552  83  ALA A CB    
3152 N  N     . ILE C 85  ? 0.2612 0.4757 0.2793 0.0947  -0.0325 0.0985  84  ILE A N     
3153 C  CA    . ILE C 85  ? 0.3447 0.5746 0.3570 0.1065  -0.0403 0.1186  84  ILE A CA    
3154 C  C     . ILE C 85  ? 0.3385 0.5984 0.3369 0.1032  -0.0617 0.1158  84  ILE A C     
3155 O  O     . ILE C 85  ? 0.3918 0.6688 0.3879 0.1119  -0.0717 0.1321  84  ILE A O     
3156 C  CB    . ILE C 85  ? 0.3800 0.5889 0.3682 0.1122  -0.0285 0.1314  84  ILE A CB    
3157 C  CG1   . ILE C 85  ? 0.3574 0.5643 0.3106 0.1034  -0.0296 0.1198  84  ILE A CG1   
3158 C  CG2   . ILE C 85  ? 0.3460 0.5244 0.3496 0.1160  -0.0089 0.1367  84  ILE A CG2   
3159 C  CD1   . ILE C 85  ? 0.4593 0.6556 0.3881 0.1091  -0.0208 0.1360  84  ILE A CD1   
3160 N  N     . ASN C 86  ? 0.3439 0.6078 0.3341 0.0900  -0.0692 0.0943  85  ASN A N     
3161 C  CA    . ASN C 86  ? 0.3858 0.6773 0.3652 0.0842  -0.0913 0.0874  85  ASN A CA    
3162 C  C     . ASN C 86  ? 0.3696 0.6816 0.3841 0.0762  -0.1031 0.0789  85  ASN A C     
3163 O  O     . ASN C 86  ? 0.3649 0.6946 0.3734 0.0658  -0.1210 0.0661  85  ASN A O     
3164 C  CB    . ASN C 86  ? 0.4170 0.6971 0.3592 0.0748  -0.0918 0.0680  85  ASN A CB    
3165 C  CG    . ASN C 86  ? 0.4097 0.6696 0.3621 0.0638  -0.0829 0.0471  85  ASN A CG    
3166 O  OD1   . ASN C 86  ? 0.3482 0.5953 0.3266 0.0645  -0.0707 0.0499  85  ASN A OD1   
3167 N  ND2   . ASN C 86  ? 0.4281 0.6839 0.3592 0.0541  -0.0887 0.0264  85  ASN A ND2   
3168 N  N     . ASN C 87  ? 0.3579 0.6680 0.4089 0.0801  -0.0931 0.0856  86  ASN A N     
3169 C  CA    . ASN C 87  ? 0.3344 0.6648 0.4215 0.0717  -0.1011 0.0790  86  ASN A CA    
3170 C  C     . ASN C 87  ? 0.3143 0.6562 0.4388 0.0838  -0.0945 0.0967  86  ASN A C     
3171 O  O     . ASN C 87  ? 0.2868 0.6136 0.4281 0.0891  -0.0763 0.0998  86  ASN A O     
3172 C  CB    . ASN C 87  ? 0.3264 0.6337 0.4165 0.0586  -0.0906 0.0599  86  ASN A CB    
3173 C  CG    . ASN C 87  ? 0.4088 0.7363 0.5321 0.0464  -0.0998 0.0521  86  ASN A CG    
3174 O  OD1   . ASN C 87  ? 0.3508 0.6898 0.5094 0.0501  -0.0929 0.0612  86  ASN A OD1   
3175 N  ND2   . ASN C 87  ? 0.4367 0.7691 0.5494 0.0316  -0.1150 0.0353  86  ASN A ND2   
3176 N  N     . THR C 88  ? 0.3442 0.7053 0.4779 0.0871  -0.1076 0.1058  87  THR A N     
3177 C  CA    . THR C 88  ? 0.3168 0.6836 0.4826 0.0993  -0.1001 0.1210  87  THR A CA    
3178 C  C     . THR C 88  ? 0.2786 0.6514 0.4826 0.0946  -0.0906 0.1150  87  THR A C     
3179 O  O     . THR C 88  ? 0.2990 0.6621 0.5221 0.1055  -0.0738 0.1232  87  THR A O     
3180 C  CB    . THR C 88  ? 0.3486 0.7399 0.5201 0.1028  -0.1187 0.1307  87  THR A CB    
3181 O  OG1   . THR C 88  ? 0.4074 0.8208 0.5802 0.0870  -0.1394 0.1171  87  THR A OG1   
3182 C  CG2   . THR C 88  ? 0.3536 0.7354 0.4892 0.1110  -0.1224 0.1418  87  THR A CG2   
3183 N  N     . LYS C 89  ? 0.2891 0.6738 0.5020 0.0780  -0.0991 0.1000  88  LYS A N     
3184 C  CA    . LYS C 89  ? 0.2821 0.6725 0.5302 0.0720  -0.0889 0.0954  88  LYS A CA    
3185 C  C     . LYS C 89  ? 0.2911 0.6537 0.5350 0.0761  -0.0649 0.0938  88  LYS A C     
3186 O  O     . LYS C 89  ? 0.2562 0.6154 0.5233 0.0803  -0.0488 0.0967  88  LYS A O     
3187 C  CB    . LYS C 89  ? 0.2993 0.7042 0.5549 0.0512  -0.1036 0.0799  88  LYS A CB    
3188 C  CG    . LYS C 89  ? 0.3516 0.7593 0.6386 0.0400  -0.0928 0.0736  88  LYS A CG    
3189 C  CD    . LYS C 89  ? 0.3909 0.8074 0.7115 0.0506  -0.0772 0.0846  88  LYS A CD    
3190 C  CE    . LYS C 89  ? 0.3810 0.8034 0.7298 0.0374  -0.0675 0.0784  88  LYS A CE    
3191 N  NZ    . LYS C 89  ? 0.4086 0.8184 0.7443 0.0190  -0.0716 0.0650  88  LYS A NZ    
3192 N  N     . SER C 90  ? 0.2879 0.6304 0.5007 0.0749  -0.0621 0.0882  89  SER A N     
3193 C  CA    . SER C 90  ? 0.2565 0.5631 0.4582 0.0772  -0.0396 0.0843  89  SER A CA    
3194 C  C     . SER C 90  ? 0.2781 0.5745 0.4854 0.0962  -0.0251 0.0990  89  SER A C     
3195 O  O     . SER C 90  ? 0.2423 0.5197 0.4563 0.0996  -0.0061 0.0975  89  SER A O     
3196 C  CB    . SER C 90  ? 0.2904 0.5668 0.4520 0.0693  -0.0393 0.0718  89  SER A CB    
3197 O  OG    . SER C 90  ? 0.2734 0.5458 0.4107 0.0783  -0.0439 0.0798  89  SER A OG    
3198 N  N     . PHE C 91  ? 0.2423 0.5436 0.4422 0.1065  -0.0330 0.1111  90  PHE A N     
3199 C  CA    . PHE C 91  ? 0.2375 0.5218 0.4417 0.1220  -0.0196 0.1235  90  PHE A CA    
3200 C  C     . PHE C 91  ? 0.2619 0.5585 0.4999 0.1261  -0.0132 0.1259  90  PHE A C     
3201 O  O     . PHE C 91  ? 0.2619 0.5382 0.5061 0.1347  0.0052  0.1276  90  PHE A O     
3202 C  CB    . PHE C 91  ? 0.2958 0.5830 0.4836 0.1304  -0.0306 0.1370  90  PHE A CB    
3203 C  CG    . PHE C 91  ? 0.2996 0.5676 0.4919 0.1459  -0.0180 0.1509  90  PHE A CG    
3204 C  CD1   . PHE C 91  ? 0.3144 0.5461 0.4924 0.1507  0.0000  0.1514  90  PHE A CD1   
3205 C  CD2   . PHE C 91  ? 0.3099 0.5952 0.5211 0.1552  -0.0246 0.1631  90  PHE A CD2   
3206 C  CE1   . PHE C 91  ? 0.3439 0.5541 0.5255 0.1633  0.0116  0.1625  90  PHE A CE1   
3207 C  CE2   . PHE C 91  ? 0.3697 0.6352 0.5856 0.1698  -0.0126 0.1756  90  PHE A CE2   
3208 C  CZ    . PHE C 91  ? 0.3740 0.6004 0.5741 0.1733  0.0057  0.1748  90  PHE A CZ    
3209 N  N     . GLU C 92  ? 0.2334 0.5628 0.4925 0.1193  -0.0280 0.1249  91  GLU A N     
3210 C  CA    . GLU C 92  ? 0.2846 0.6303 0.5784 0.1234  -0.0219 0.1279  91  GLU A CA    
3211 C  C     . GLU C 92  ? 0.2754 0.6103 0.5785 0.1169  -0.0039 0.1175  91  GLU A C     
3212 O  O     . GLU C 92  ? 0.2788 0.6104 0.5991 0.1248  0.0116  0.1197  91  GLU A O     
3213 C  CB    . GLU C 92  ? 0.2664 0.6508 0.5810 0.1157  -0.0435 0.1287  91  GLU A CB    
3214 C  CG    . GLU C 92  ? 0.3064 0.7038 0.6136 0.1243  -0.0608 0.1409  91  GLU A CG    
3215 C  CD    . GLU C 92  ? 0.3828 0.8154 0.7019 0.1129  -0.0856 0.1377  91  GLU A CD    
3216 O  OE1   . GLU C 92  ? 0.3826 0.8255 0.7113 0.0964  -0.0902 0.1246  91  GLU A OE1   
3217 O  OE2   . GLU C 92  ? 0.3503 0.7993 0.6697 0.1200  -0.1006 0.1483  91  GLU A OE2   
3218 N  N     . ASP C 93  ? 0.2730 0.6015 0.5625 0.1029  -0.0054 0.1063  92  ASP A N     
3219 C  CA    . ASP C 93  ? 0.2853 0.6013 0.5778 0.0952  0.0111  0.0971  92  ASP A CA    
3220 C  C     . ASP C 93  ? 0.3059 0.5874 0.5828 0.1055  0.0331  0.0965  92  ASP A C     
3221 O  O     . ASP C 93  ? 0.2911 0.5631 0.5716 0.1028  0.0490  0.0908  92  ASP A O     
3222 C  CB    . ASP C 93  ? 0.2711 0.5835 0.5489 0.0795  0.0042  0.0868  92  ASP A CB    
3223 C  CG    . ASP C 93  ? 0.2960 0.6380 0.5920 0.0644  -0.0141 0.0827  92  ASP A CG    
3224 O  OD1   . ASP C 93  ? 0.2638 0.6298 0.5861 0.0657  -0.0192 0.0877  92  ASP A OD1   
3225 O  OD2   . ASP C 93  ? 0.2785 0.6190 0.5631 0.0508  -0.0235 0.0739  92  ASP A OD2   
3226 N  N     . ILE C 94  ? 0.2845 0.5461 0.5424 0.1162  0.0340  0.1020  93  ILE A N     
3227 C  CA    . ILE C 94  ? 0.3116 0.5365 0.5523 0.1238  0.0530  0.0996  93  ILE A CA    
3228 C  C     . ILE C 94  ? 0.3471 0.5687 0.6045 0.1321  0.0686  0.1003  93  ILE A C     
3229 O  O     . ILE C 94  ? 0.3166 0.5157 0.5637 0.1307  0.0852  0.0916  93  ILE A O     
3230 C  CB    . ILE C 94  ? 0.3390 0.5465 0.5621 0.1336  0.0497  0.1083  93  ILE A CB    
3231 C  CG1   . ILE C 94  ? 0.2848 0.4899 0.4857 0.1255  0.0395  0.1051  93  ILE A CG1   
3232 C  CG2   . ILE C 94  ? 0.3461 0.5167 0.5586 0.1424  0.0687  0.1073  93  ILE A CG2   
3233 C  CD1   . ILE C 94  ? 0.2622 0.4404 0.4438 0.1170  0.0514  0.0922  93  ILE A CD1   
3234 N  N     . HIS C 95  ? 0.3239 0.5677 0.6054 0.1415  0.0631  0.1105  94  HIS A N     
3235 C  CA    . HIS C 95  ? 0.3645 0.6100 0.6657 0.1510  0.0778  0.1118  94  HIS A CA    
3236 C  C     . HIS C 95  ? 0.3362 0.5880 0.6436 0.1407  0.0883  0.1017  94  HIS A C     
3237 O  O     . HIS C 95  ? 0.3429 0.5749 0.6435 0.1445  0.1071  0.0955  94  HIS A O     
3238 C  CB    . HIS C 95  ? 0.3131 0.5923 0.6450 0.1595  0.0663  0.1242  94  HIS A CB    
3239 C  CG    . HIS C 95  ? 0.4298 0.7170 0.7870 0.1703  0.0806  0.1265  94  HIS A CG    
3240 N  ND1   . HIS C 95  ? 0.4085 0.7348 0.7998 0.1684  0.0756  0.1299  94  HIS A ND1   
3241 C  CD2   . HIS C 95  ? 0.4211 0.6834 0.7760 0.1837  0.0993  0.1261  94  HIS A CD2   
3242 C  CE1   . HIS C 95  ? 0.3927 0.7191 0.8016 0.1807  0.0919  0.1316  94  HIS A CE1   
3243 N  NE2   . HIS C 95  ? 0.4193 0.7065 0.8058 0.1904  0.1065  0.1289  94  HIS A NE2   
3244 N  N     . HIS C 96  ? 0.3373 0.6158 0.6562 0.1270  0.0764  0.0998  95  HIS A N     
3245 C  CA    . HIS C 96  ? 0.3210 0.6067 0.6474 0.1164  0.0866  0.0928  95  HIS A CA    
3246 C  C     . HIS C 96  ? 0.3221 0.5728 0.6161 0.1112  0.1007  0.0824  95  HIS A C     
3247 O  O     . HIS C 96  ? 0.2742 0.5177 0.5655 0.1101  0.1170  0.0774  95  HIS A O     
3248 C  CB    . HIS C 96  ? 0.3318 0.6483 0.6755 0.1004  0.0702  0.0926  95  HIS A CB    
3249 C  CG    . HIS C 96  ? 0.3667 0.7198 0.7423 0.1034  0.0549  0.1012  95  HIS A CG    
3250 N  ND1   . HIS C 96  ? 0.3794 0.7383 0.7535 0.1121  0.0395  0.1087  95  HIS A ND1   
3251 C  CD2   . HIS C 96  ? 0.4277 0.8142 0.8375 0.0990  0.0528  0.1042  95  HIS A CD2   
3252 C  CE1   . HIS C 96  ? 0.3592 0.7534 0.7642 0.1130  0.0274  0.1154  95  HIS A CE1   
3253 N  NE2   . HIS C 96  ? 0.4440 0.8561 0.8726 0.1049  0.0350  0.1124  95  HIS A NE2   
3254 N  N     . TYR C 97  ? 0.3115 0.5404 0.5795 0.1087  0.0948  0.0793  96  TYR A N     
3255 C  CA    . TYR C 97  ? 0.3190 0.5162 0.5567 0.1030  0.1064  0.0693  96  TYR A CA    
3256 C  C     . TYR C 97  ? 0.3372 0.5051 0.5603 0.1141  0.1233  0.0655  96  TYR A C     
3257 O  O     . TYR C 97  ? 0.3267 0.4774 0.5331 0.1103  0.1370  0.0569  96  TYR A O     
3258 C  CB    . TYR C 97  ? 0.2580 0.4416 0.4743 0.0976  0.0961  0.0668  96  TYR A CB    
3259 C  CG    . TYR C 97  ? 0.2504 0.4491 0.4690 0.0823  0.0863  0.0639  96  TYR A CG    
3260 C  CD1   . TYR C 97  ? 0.2764 0.4619 0.4805 0.0720  0.0952  0.0568  96  TYR A CD1   
3261 C  CD2   . TYR C 97  ? 0.2499 0.4753 0.4842 0.0778  0.0676  0.0683  96  TYR A CD2   
3262 C  CE1   . TYR C 97  ? 0.2584 0.4528 0.4639 0.0571  0.0856  0.0547  96  TYR A CE1   
3263 C  CE2   . TYR C 97  ? 0.2460 0.4793 0.4802 0.0621  0.0577  0.0634  96  TYR A CE2   
3264 C  CZ    . TYR C 97  ? 0.2525 0.4673 0.4719 0.0518  0.0667  0.0566  96  TYR A CZ    
3265 O  OH    . TYR C 97  ? 0.3007 0.5156 0.5171 0.0359  0.0564  0.0515  96  TYR A OH    
3266 N  N     . ARG C 98  ? 0.3339 0.4934 0.5602 0.1271  0.1221  0.0716  97  ARG A N     
3267 C  CA    . ARG C 98  ? 0.3717 0.5002 0.5851 0.1372  0.1379  0.0674  97  ARG A CA    
3268 C  C     . ARG C 98  ? 0.3562 0.4936 0.5838 0.1424  0.1524  0.0651  97  ARG A C     
3269 O  O     . ARG C 98  ? 0.3986 0.5123 0.6074 0.1427  0.1677  0.0549  97  ARG A O     
3270 C  CB    . ARG C 98  ? 0.4231 0.5435 0.6426 0.1505  0.1339  0.0773  97  ARG A CB    
3271 C  CG    . ARG C 98  ? 0.4479 0.5310 0.6534 0.1597  0.1496  0.0722  97  ARG A CG    
3272 C  CD    . ARG C 98  ? 0.4568 0.5310 0.6690 0.1719  0.1448  0.0845  97  ARG A CD    
3273 N  NE    . ARG C 98  ? 0.4737 0.5235 0.6879 0.1845  0.1600  0.0829  97  ARG A NE    
3274 C  CZ    . ARG C 98  ? 0.5363 0.5449 0.7263 0.1831  0.1717  0.0720  97  ARG A CZ    
3275 N  NH1   . ARG C 98  ? 0.5624 0.5514 0.7258 0.1700  0.1698  0.0626  97  ARG A NH1   
3276 N  NH2   . ARG C 98  ? 0.5952 0.5819 0.7886 0.1949  0.1852  0.0699  97  ARG A NH2   
3277 N  N     . GLU C 99  ? 0.3586 0.5314 0.6194 0.1466  0.1473  0.0743  98  GLU A N     
3278 C  CA    . GLU C 99  ? 0.3544 0.5423 0.6339 0.1516  0.1612  0.0735  98  GLU A CA    
3279 C  C     . GLU C 99  ? 0.3665 0.5497 0.6290 0.1390  0.1714  0.0635  98  GLU A C     
3280 O  O     . GLU C 99  ? 0.3561 0.5265 0.6090 0.1433  0.1892  0.0565  98  GLU A O     
3281 C  CB    . GLU C 99  ? 0.3359 0.5679 0.6553 0.1534  0.1505  0.0850  98  GLU A CB    
3282 C  CG    . GLU C 99  ? 0.4202 0.6602 0.7617 0.1710  0.1472  0.0960  98  GLU A CG    
3283 C  CD    . GLU C 99  ? 0.4630 0.6696 0.7929 0.1862  0.1652  0.0924  98  GLU A CD    
3284 O  OE1   . GLU C 99  ? 0.4662 0.6484 0.7835 0.1935  0.1615  0.0959  98  GLU A OE1   
3285 O  OE2   . GLU C 99  ? 0.4003 0.6063 0.7352 0.1909  0.1831  0.0866  98  GLU A OE2   
3286 N  N     . GLN C 100 ? 0.3400 0.5310 0.5955 0.1236  0.1605  0.0625  99  GLN A N     
3287 C  CA    . GLN C 100 ? 0.3653 0.5551 0.6070 0.1110  0.1688  0.0561  99  GLN A CA    
3288 C  C     . GLN C 100 ? 0.3560 0.5070 0.5573 0.1099  0.1796  0.0446  99  GLN A C     
3289 O  O     . GLN C 100 ? 0.3593 0.5041 0.5467 0.1073  0.1939  0.0385  99  GLN A O     
3290 C  CB    . GLN C 100 ? 0.3097 0.5164 0.5568 0.0952  0.1539  0.0590  99  GLN A CB    
3291 C  CG    . GLN C 100 ? 0.3807 0.5900 0.6192 0.0819  0.1624  0.0561  99  GLN A CG    
3292 C  CD    . GLN C 100 ? 0.3818 0.6089 0.6321 0.0660  0.1485  0.0602  99  GLN A CD    
3293 O  OE1   . GLN C 100 ? 0.4088 0.6427 0.6672 0.0643  0.1318  0.0625  99  GLN A OE1   
3294 N  NE2   . GLN C 100 ? 0.3749 0.6094 0.6261 0.0541  0.1555  0.0615  99  GLN A NE2   
3295 N  N     . ILE C 101 ? 0.3412 0.4667 0.5228 0.1114  0.1729  0.0414  100 ILE A N     
3296 C  CA    . ILE C 101 ? 0.3528 0.4413 0.4974 0.1096  0.1815  0.0296  100 ILE A CA    
3297 C  C     . ILE C 101 ? 0.4277 0.5000 0.5677 0.1215  0.1985  0.0236  100 ILE A C     
3298 O  O     . ILE C 101 ? 0.4150 0.4692 0.5288 0.1182  0.2103  0.0129  100 ILE A O     
3299 C  CB    . ILE C 101 ? 0.3907 0.4574 0.5207 0.1089  0.1711  0.0286  100 ILE A CB    
3300 C  CG1   . ILE C 101 ? 0.3526 0.4312 0.4807 0.0965  0.1567  0.0313  100 ILE A CG1   
3301 C  CG2   . ILE C 101 ? 0.4191 0.4475 0.5144 0.1073  0.1803  0.0157  100 ILE A CG2   
3302 C  CD1   . ILE C 101 ? 0.3358 0.4088 0.4645 0.0991  0.1448  0.0356  100 ILE A CD1   
3303 N  N     . LYS C 102 ? 0.4216 0.4988 0.5850 0.1356  0.1996  0.0302  101 LYS A N     
3304 C  CA    . LYS C 102 ? 0.4245 0.4889 0.5882 0.1483  0.2169  0.0249  101 LYS A CA    
3305 C  C     . LYS C 102 ? 0.4286 0.5144 0.5995 0.1470  0.2299  0.0230  101 LYS A C     
3306 O  O     . LYS C 102 ? 0.4678 0.5362 0.6182 0.1494  0.2459  0.0120  101 LYS A O     
3307 C  CB    . LYS C 102 ? 0.4365 0.5085 0.6299 0.1644  0.2151  0.0355  101 LYS A CB    
3308 C  CG    . LYS C 102 ? 0.4543 0.4984 0.6379 0.1686  0.2077  0.0376  101 LYS A CG    
3309 C  CD    . LYS C 102 ? 0.4695 0.5174 0.6804 0.1869  0.2097  0.0484  101 LYS A CD    
3310 C  CE    . LYS C 102 ? 0.4438 0.5368 0.6908 0.1897  0.1971  0.0637  101 LYS A CE    
3311 N  NZ    . LYS C 102 ? 0.4800 0.5843 0.7569 0.2075  0.1974  0.0762  101 LYS A NZ    
3312 N  N     . ARG C 103 ? 0.3735 0.4979 0.5741 0.1430  0.2235  0.0335  102 ARG A N     
3313 C  CA    . ARG C 103 ? 0.4290 0.5771 0.6422 0.1422  0.2370  0.0339  102 ARG A CA    
3314 C  C     . ARG C 103 ? 0.4409 0.5758 0.6189 0.1288  0.2440  0.0248  102 ARG A C     
3315 O  O     . ARG C 103 ? 0.4598 0.5923 0.6265 0.1313  0.2614  0.0185  102 ARG A O     
3316 C  CB    . ARG C 103 ? 0.3741 0.5658 0.6282 0.1382  0.2265  0.0472  102 ARG A CB    
3317 C  CG    . ARG C 103 ? 0.4173 0.6415 0.6964 0.1371  0.2381  0.0514  102 ARG A CG    
3318 C  CD    . ARG C 103 ? 0.4500 0.7158 0.7741 0.1345  0.2234  0.0645  102 ARG A CD    
3319 N  NE    . ARG C 103 ? 0.4828 0.7555 0.8047 0.1175  0.2049  0.0675  102 ARG A NE    
3320 C  CZ    . ARG C 103 ? 0.4283 0.7084 0.7616 0.1161  0.1845  0.0728  102 ARG A CZ    
3321 N  NH1   . ARG C 103 ? 0.4251 0.7053 0.7705 0.1304  0.1783  0.0772  102 ARG A NH1   
3322 N  NH2   . ARG C 103 ? 0.4464 0.7336 0.7780 0.1001  0.1701  0.0739  102 ARG A NH2   
3323 N  N     . VAL C 104 ? 0.4372 0.5619 0.5952 0.1153  0.2309  0.0238  103 VAL A N     
3324 C  CA    . VAL C 104 ? 0.4617 0.5739 0.5851 0.1025  0.2353  0.0170  103 VAL A CA    
3325 C  C     . VAL C 104 ? 0.4546 0.5296 0.5384 0.1060  0.2447  0.0025  103 VAL A C     
3326 O  O     . VAL C 104 ? 0.5283 0.5971 0.5875 0.1029  0.2572  -0.0045 103 VAL A O     
3327 C  CB    . VAL C 104 ? 0.4917 0.6059 0.6090 0.0880  0.2184  0.0213  103 VAL A CB    
3328 C  CG1   . VAL C 104 ? 0.4809 0.5790 0.5598 0.0758  0.2216  0.0155  103 VAL A CG1   
3329 C  CG2   . VAL C 104 ? 0.4570 0.6081 0.6122 0.0820  0.2103  0.0339  103 VAL A CG2   
3330 N  N     . LYS C 105 ? 0.4275 0.4775 0.5042 0.1122  0.2394  -0.0023 104 LYS A N     
3331 C  CA    . LYS C 105 ? 0.4765 0.4896 0.5176 0.1141  0.2473  -0.0173 104 LYS A CA    
3332 C  C     . LYS C 105 ? 0.5210 0.5274 0.5680 0.1290  0.2650  -0.0232 104 LYS A C     
3333 O  O     . LYS C 105 ? 0.5534 0.5300 0.5700 0.1307  0.2743  -0.0377 104 LYS A O     
3334 C  CB    . LYS C 105 ? 0.5504 0.5385 0.5839 0.1132  0.2351  -0.0194 104 LYS A CB    
3335 C  CG    . LYS C 105 ? 0.4910 0.4769 0.5071 0.0981  0.2206  -0.0187 104 LYS A CG    
3336 C  CD    . LYS C 105 ? 0.5574 0.5079 0.5488 0.0952  0.2160  -0.0286 104 LYS A CD    
3337 C  CE    . LYS C 105 ? 0.4922 0.4372 0.4596 0.0802  0.2049  -0.0313 104 LYS A CE    
3338 N  NZ    . LYS C 105 ? 0.4893 0.4226 0.4195 0.0706  0.2093  -0.0419 104 LYS A NZ    
3339 N  N     . ASP C 106 ? 0.5626 0.5965 0.6482 0.1399  0.2697  -0.0130 105 ASP A N     
3340 C  CA    . ASP C 106 ? 0.5159 0.5467 0.6146 0.1567  0.2865  -0.0165 105 ASP A CA    
3341 C  C     . ASP C 106 ? 0.5435 0.5338 0.6266 0.1653  0.2889  -0.0264 105 ASP A C     
3342 O  O     . ASP C 106 ? 0.5877 0.5543 0.6506 0.1715  0.3039  -0.0400 105 ASP A O     
3343 C  CB    . ASP C 106 ? 0.5482 0.5868 0.6330 0.1567  0.3052  -0.0240 105 ASP A CB    
3344 C  CG    . ASP C 106 ? 0.5813 0.6316 0.6931 0.1745  0.3218  -0.0230 105 ASP A CG    
3345 O  OD1   . ASP C 106 ? 0.5561 0.6332 0.7104 0.1819  0.3161  -0.0090 105 ASP A OD1   
3346 O  OD2   . ASP C 106 ? 0.6228 0.6570 0.7138 0.1811  0.3400  -0.0362 105 ASP A OD2   
3347 N  N     . SER C 107 ? 0.5489 0.5317 0.6431 0.1658  0.2741  -0.0189 106 SER A N     
3348 C  CA    . SER C 107 ? 0.5430 0.4878 0.6261 0.1720  0.2746  -0.0252 106 SER A CA    
3349 C  C     . SER C 107 ? 0.5677 0.5216 0.6802 0.1780  0.2610  -0.0091 106 SER A C     
3350 O  O     . SER C 107 ? 0.4979 0.4745 0.6210 0.1699  0.2457  0.0013  106 SER A O     
3351 C  CB    . SER C 107 ? 0.6033 0.5141 0.6439 0.1573  0.2694  -0.0391 106 SER A CB    
3352 O  OG    . SER C 107 ? 0.5779 0.4503 0.6086 0.1610  0.2696  -0.0455 106 SER A OG    
3353 N  N     . GLU C 108 ? 0.5441 0.4792 0.6678 0.1922  0.2666  -0.0075 107 GLU A N     
3354 C  CA    . GLU C 108 ? 0.5434 0.4809 0.6893 0.1987  0.2546  0.0077  107 GLU A CA    
3355 C  C     . GLU C 108 ? 0.5829 0.4869 0.7043 0.1889  0.2457  0.0038  107 GLU A C     
3356 O  O     . GLU C 108 ? 0.5817 0.4863 0.7165 0.1921  0.2350  0.0168  107 GLU A O     
3357 C  CB    . GLU C 108 ? 0.5648 0.4963 0.7345 0.2191  0.2652  0.0128  107 GLU A CB    
3358 C  CG    . GLU C 108 ? 0.5639 0.5365 0.7684 0.2305  0.2712  0.0216  107 GLU A CG    
3359 C  CD    . GLU C 108 ? 0.5677 0.5827 0.8015 0.2283  0.2535  0.0400  107 GLU A CD    
3360 O  OE1   . GLU C 108 ? 0.5530 0.5664 0.7988 0.2335  0.2419  0.0525  107 GLU A OE1   
3361 O  OE2   . GLU C 108 ? 0.5539 0.6028 0.7976 0.2205  0.2507  0.0418  107 GLU A OE2   
3362 N  N     . ASP C 109 ? 0.5569 0.4332 0.6426 0.1767  0.2496  -0.0135 108 ASP A N     
3363 C  CA    . ASP C 109 ? 0.5809 0.4216 0.6439 0.1673  0.2436  -0.0196 108 ASP A CA    
3364 C  C     . ASP C 109 ? 0.5848 0.4287 0.6222 0.1483  0.2343  -0.0269 108 ASP A C     
3365 O  O     . ASP C 109 ? 0.6059 0.4299 0.6121 0.1381  0.2384  -0.0434 108 ASP A O     
3366 C  CB    . ASP C 109 ? 0.6623 0.4610 0.7078 0.1715  0.2566  -0.0347 108 ASP A CB    
3367 C  CG    . ASP C 109 ? 0.7548 0.5161 0.7780 0.1596  0.2506  -0.0423 108 ASP A CG    
3368 O  OD1   . ASP C 109 ? 0.7488 0.5145 0.7819 0.1560  0.2385  -0.0295 108 ASP A OD1   
3369 O  OD2   . ASP C 109 ? 0.8457 0.5732 0.8426 0.1543  0.2581  -0.0611 108 ASP A OD2   
3370 N  N     . VAL C 110 ? 0.5473 0.4181 0.5982 0.1436  0.2206  -0.0140 109 VAL A N     
3371 C  CA    . VAL C 110 ? 0.5008 0.3789 0.5333 0.1276  0.2109  -0.0179 109 VAL A CA    
3372 C  C     . VAL C 110 ? 0.4573 0.3249 0.4892 0.1222  0.1992  -0.0119 109 VAL A C     
3373 O  O     . VAL C 110 ? 0.4750 0.3589 0.5309 0.1300  0.1923  0.0035  109 VAL A O     
3374 C  CB    . VAL C 110 ? 0.4573 0.3778 0.5068 0.1258  0.2054  -0.0088 109 VAL A CB    
3375 C  CG1   . VAL C 110 ? 0.4349 0.3595 0.4640 0.1096  0.1963  -0.0132 109 VAL A CG1   
3376 C  CG2   . VAL C 110 ? 0.4431 0.3770 0.4984 0.1321  0.2184  -0.0121 109 VAL A CG2   
3377 N  N     . PRO C 111 ? 0.4974 0.3420 0.5026 0.1086  0.1957  -0.0229 110 PRO A N     
3378 C  CA    . PRO C 111 ? 0.4715 0.3083 0.4775 0.1029  0.1856  -0.0169 110 PRO A CA    
3379 C  C     . PRO C 111 ? 0.4769 0.3505 0.5019 0.1040  0.1742  -0.0025 110 PRO A C     
3380 O  O     . PRO C 111 ? 0.3992 0.2952 0.4208 0.0974  0.1701  -0.0043 110 PRO A O     
3381 C  CB    . PRO C 111 ? 0.4731 0.2866 0.4469 0.0858  0.1835  -0.0335 110 PRO A CB    
3382 C  CG    . PRO C 111 ? 0.5184 0.3145 0.4728 0.0856  0.1944  -0.0489 110 PRO A CG    
3383 C  CD    . PRO C 111 ? 0.5179 0.3449 0.4903 0.0969  0.2000  -0.0412 110 PRO A CD    
3384 N  N     . MET C 112 ? 0.4389 0.3194 0.4838 0.1127  0.1689  0.0127  111 MET A N     
3385 C  CA    . MET C 112 ? 0.3906 0.3051 0.4519 0.1139  0.1566  0.0260  111 MET A CA    
3386 C  C     . MET C 112 ? 0.4273 0.3329 0.4933 0.1174  0.1507  0.0379  111 MET A C     
3387 O  O     . MET C 112 ? 0.4381 0.3161 0.5031 0.1220  0.1566  0.0405  111 MET A O     
3388 C  CB    . MET C 112 ? 0.3632 0.3135 0.4507 0.1238  0.1534  0.0370  111 MET A CB    
3389 C  CG    . MET C 112 ? 0.4254 0.3881 0.5154 0.1232  0.1605  0.0299  111 MET A CG    
3390 S  SD    . MET C 112 ? 0.4329 0.4393 0.5597 0.1339  0.1551  0.0447  111 MET A SD    
3391 C  CE    . MET C 112 ? 0.4480 0.4554 0.5744 0.1351  0.1708  0.0346  111 MET A CE    
3392 N  N     . VAL C 113 ? 0.3704 0.3012 0.4375 0.1101  0.1355  0.0449  112 VAL A N     
3393 C  CA    . VAL C 113 ? 0.3592 0.2925 0.4285 0.1111  0.1261  0.0588  112 VAL A CA    
3394 C  C     . VAL C 113 ? 0.3446 0.3187 0.4280 0.1152  0.1131  0.0697  112 VAL A C     
3395 O  O     . VAL C 113 ? 0.3313 0.3272 0.4140 0.1069  0.1062  0.0629  112 VAL A O     
3396 C  CB    . VAL C 113 ? 0.3366 0.2558 0.3860 0.0938  0.1201  0.0528  112 VAL A CB    
3397 C  CG1   . VAL C 113 ? 0.3677 0.2968 0.4180 0.0940  0.1111  0.0676  112 VAL A CG1   
3398 C  CG2   . VAL C 113 ? 0.4048 0.2829 0.4427 0.0891  0.1312  0.0434  112 VAL A CG2   
3399 N  N     . LEU C 114 ? 0.3186 0.3020 0.4145 0.1277  0.1094  0.0866  113 LEU A N     
3400 C  CA    . LEU C 114 ? 0.2971 0.3187 0.4033 0.1307  0.0946  0.0968  113 LEU A CA    
3401 C  C     . LEU C 114 ? 0.3006 0.3250 0.3874 0.1197  0.0836  0.0984  113 LEU A C     
3402 O  O     . LEU C 114 ? 0.2911 0.2955 0.3678 0.1201  0.0866  0.1061  113 LEU A O     
3403 C  CB    . LEU C 114 ? 0.3468 0.3798 0.4731 0.1490  0.0936  0.1152  113 LEU A CB    
3404 C  CG    . LEU C 114 ? 0.3455 0.4208 0.4818 0.1511  0.0755  0.1253  113 LEU A CG    
3405 C  CD1   . LEU C 114 ? 0.2906 0.3947 0.4423 0.1455  0.0711  0.1155  113 LEU A CD1   
3406 C  CD2   . LEU C 114 ? 0.3317 0.4160 0.4787 0.1630  0.0701  0.1428  113 LEU A CD2   
3407 N  N     . VAL C 115 ? 0.2569 0.3047 0.3392 0.1098  0.0723  0.0914  114 VAL A N     
3408 C  CA    . VAL C 115 ? 0.2891 0.3402 0.3526 0.1002  0.0638  0.0905  114 VAL A CA    
3409 C  C     . VAL C 115 ? 0.2703 0.3537 0.3354 0.1030  0.0489  0.0970  114 VAL A C     
3410 O  O     . VAL C 115 ? 0.2211 0.3257 0.2961 0.0998  0.0414  0.0903  114 VAL A O     
3411 C  CB    . VAL C 115 ? 0.2647 0.3098 0.3175 0.0854  0.0638  0.0740  114 VAL A CB    
3412 C  CG1   . VAL C 115 ? 0.2243 0.2764 0.2608 0.0774  0.0560  0.0727  114 VAL A CG1   
3413 C  CG2   . VAL C 115 ? 0.3186 0.3324 0.3659 0.0808  0.0761  0.0671  114 VAL A CG2   
3414 N  N     . GLY C 116 ? 0.2815 0.3679 0.3350 0.1074  0.0444  0.1097  115 GLY A N     
3415 C  CA    . GLY C 116 ? 0.2656 0.3807 0.3116 0.1075  0.0292  0.1131  115 GLY A CA    
3416 C  C     . GLY C 116 ? 0.2559 0.3700 0.2784 0.0962  0.0264  0.1034  115 GLY A C     
3417 O  O     . GLY C 116 ? 0.2867 0.3887 0.2931 0.0958  0.0320  0.1102  115 GLY A O     
3418 N  N     . ASN C 117 ? 0.2141 0.3394 0.2361 0.0872  0.0193  0.0878  116 ASN A N     
3419 C  CA    . ASN C 117 ? 0.2692 0.3911 0.2728 0.0779  0.0188  0.0763  116 ASN A CA    
3420 C  C     . ASN C 117 ? 0.2714 0.4137 0.2570 0.0781  0.0067  0.0756  116 ASN A C     
3421 O  O     . ASN C 117 ? 0.2607 0.4226 0.2488 0.0836  -0.0044 0.0829  116 ASN A O     
3422 C  CB    . ASN C 117 ? 0.2394 0.3564 0.2521 0.0685  0.0194  0.0599  116 ASN A CB    
3423 C  CG    . ASN C 117 ? 0.2422 0.3518 0.2407 0.0607  0.0215  0.0487  116 ASN A CG    
3424 O  OD1   . ASN C 117 ? 0.2432 0.3417 0.2326 0.0603  0.0298  0.0525  116 ASN A OD1   
3425 N  ND2   . ASN C 117 ? 0.2345 0.3508 0.2332 0.0547  0.0142  0.0357  116 ASN A ND2   
3426 N  N     . LYS C 118 ? 0.2726 0.4108 0.2396 0.0723  0.0091  0.0662  117 LYS A N     
3427 C  CA    . LYS C 118 ? 0.2931 0.4461 0.2364 0.0719  0.0006  0.0616  117 LYS A CA    
3428 C  C     . LYS C 118 ? 0.3296 0.4887 0.2537 0.0799  0.0017  0.0796  117 LYS A C     
3429 O  O     . LYS C 118 ? 0.3357 0.5123 0.2402 0.0822  -0.0091 0.0807  117 LYS A O     
3430 C  CB    . LYS C 118 ? 0.2786 0.4499 0.2266 0.0688  -0.0158 0.0516  117 LYS A CB    
3431 C  CG    . LYS C 118 ? 0.2842 0.4490 0.2532 0.0606  -0.0164 0.0373  117 LYS A CG    
3432 C  CD    . LYS C 118 ? 0.2891 0.4671 0.2567 0.0532  -0.0315 0.0222  117 LYS A CD    
3433 C  CE    . LYS C 118 ? 0.2785 0.4482 0.2691 0.0447  -0.0308 0.0113  117 LYS A CE    
3434 N  NZ    . LYS C 118 ? 0.2749 0.4543 0.2645 0.0360  -0.0454 -0.0033 117 LYS A NZ    
3435 N  N     . CYS C 119 ? 0.3325 0.4761 0.2597 0.0832  0.0146  0.0937  118 CYS A N     
3436 C  CA    . CYS C 119 ? 0.2988 0.4457 0.2104 0.0911  0.0163  0.1144  118 CYS A CA    
3437 C  C     . CYS C 119 ? 0.3408 0.4934 0.2213 0.0892  0.0207  0.1135  118 CYS A C     
3438 O  O     . CYS C 119 ? 0.3966 0.5545 0.2577 0.0952  0.0218  0.1314  118 CYS A O     
3439 C  CB    . CYS C 119 ? 0.3437 0.4683 0.2703 0.0946  0.0293  0.1302  118 CYS A CB    
3440 S  SG    . CYS C 119 ? 0.4531 0.5561 0.3798 0.0846  0.0469  0.1246  118 CYS A SG    
3441 N  N     . ASP C 120 ? 0.3604 0.5139 0.2345 0.0821  0.0224  0.0934  119 ASP A N     
3442 C  CA    . ASP C 120 ? 0.3816 0.5443 0.2245 0.0819  0.0256  0.0885  119 ASP A CA    
3443 C  C     . ASP C 120 ? 0.4117 0.5942 0.2309 0.0841  0.0087  0.0824  119 ASP A C     
3444 O  O     . ASP C 120 ? 0.4727 0.6638 0.2594 0.0852  0.0104  0.0789  119 ASP A O     
3445 C  CB    . ASP C 120 ? 0.3783 0.5340 0.2263 0.0753  0.0337  0.0680  119 ASP A CB    
3446 C  CG    . ASP C 120 ? 0.3540 0.5086 0.2182 0.0706  0.0223  0.0482  119 ASP A CG    
3447 O  OD1   . ASP C 120 ? 0.3140 0.4598 0.2053 0.0683  0.0206  0.0493  119 ASP A OD1   
3448 O  OD2   . ASP C 120 ? 0.3692 0.5304 0.2182 0.0690  0.0156  0.0312  119 ASP A OD2   
3449 N  N     . LEU C 121 ? 0.4394 0.6303 0.2741 0.0841  -0.0071 0.0797  120 LEU A N     
3450 C  CA    . LEU C 121 ? 0.4295 0.6397 0.2418 0.0829  -0.0245 0.0692  120 LEU A CA    
3451 C  C     . LEU C 121 ? 0.5084 0.7330 0.3057 0.0897  -0.0338 0.0893  120 LEU A C     
3452 O  O     . LEU C 121 ? 0.5662 0.7881 0.3813 0.0963  -0.0314 0.1106  120 LEU A O     
3453 C  CB    . LEU C 121 ? 0.4421 0.6579 0.2801 0.0768  -0.0392 0.0548  120 LEU A CB    
3454 C  CG    . LEU C 121 ? 0.3755 0.5759 0.2257 0.0683  -0.0335 0.0319  120 LEU A CG    
3455 C  CD1   . LEU C 121 ? 0.4494 0.6570 0.3243 0.0616  -0.0482 0.0218  120 LEU A CD1   
3456 C  CD2   . LEU C 121 ? 0.4260 0.6236 0.2442 0.0658  -0.0304 0.0136  120 LEU A CD2   
3457 N  N     . PRO C 122 ? 0.5764 0.8098 0.3456 0.0865  -0.0432 0.0807  121 PRO A N     
3458 C  CA    . PRO C 122 ? 0.5966 0.8393 0.3534 0.0908  -0.0524 0.0983  121 PRO A CA    
3459 C  C     . PRO C 122 ? 0.7033 0.9646 0.4797 0.0914  -0.0741 0.1021  121 PRO A C     
3460 O  O     . PRO C 122 ? 0.6872 0.9564 0.4618 0.0971  -0.0816 0.1206  121 PRO A O     
3461 C  CB    . PRO C 122 ? 0.6513 0.8946 0.3669 0.0861  -0.0536 0.0849  121 PRO A CB    
3462 C  CG    . PRO C 122 ? 0.6091 0.8484 0.3225 0.0784  -0.0544 0.0555  121 PRO A CG    
3463 C  CD    . PRO C 122 ? 0.5458 0.7763 0.2908 0.0795  -0.0431 0.0548  121 PRO A CD    
3464 N  N     . SER C 123 ? 0.8051 1.0741 0.6021 0.0855  -0.0843 0.0859  122 SER A N     
3465 C  CA    . SER C 123 ? 0.8448 1.1346 0.6598 0.0828  -0.1064 0.0854  122 SER A CA    
3466 C  C     . SER C 123 ? 0.8293 1.1248 0.6888 0.0898  -0.1056 0.1017  122 SER A C     
3467 O  O     . SER C 123 ? 0.7630 1.0689 0.6528 0.0851  -0.1136 0.0932  122 SER A O     
3468 C  CB    . SER C 123 ? 0.9082 1.2024 0.7214 0.0699  -0.1183 0.0572  122 SER A CB    
3469 O  OG    . SER C 123 ? 0.8388 1.1197 0.6632 0.0674  -0.1054 0.0446  122 SER A OG    
3470 N  N     . ARG C 124 ? 0.6888 0.9756 0.5530 0.1009  -0.0947 0.1251  123 ARG A N     
3471 C  CA    . ARG C 124 ? 0.5608 0.8439 0.4644 0.1091  -0.0875 0.1390  123 ARG A CA    
3472 C  C     . ARG C 124 ? 0.5409 0.8459 0.4710 0.1124  -0.1038 0.1472  123 ARG A C     
3473 O  O     . ARG C 124 ? 0.4628 0.7797 0.3779 0.1142  -0.1163 0.1553  123 ARG A O     
3474 C  CB    . ARG C 124 ? 0.5771 0.8385 0.4760 0.1186  -0.0697 0.1593  123 ARG A CB    
3475 C  CG    . ARG C 124 ? 0.5874 0.8402 0.5230 0.1281  -0.0616 0.1736  123 ARG A CG    
3476 C  CD    . ARG C 124 ? 0.5726 0.8037 0.5002 0.1363  -0.0477 0.1942  123 ARG A CD    
3477 N  NE    . ARG C 124 ? 0.6394 0.8454 0.5569 0.1325  -0.0290 0.1907  123 ARG A NE    
3478 C  CZ    . ARG C 124 ? 0.5660 0.7507 0.5050 0.1344  -0.0149 0.1911  123 ARG A CZ    
3479 N  NH1   . ARG C 124 ? 0.5019 0.6869 0.4738 0.1404  -0.0155 0.1925  123 ARG A NH1   
3480 N  NH2   . ARG C 124 ? 0.6130 0.7758 0.5406 0.1292  0.0007  0.1886  123 ARG A NH2   
3481 N  N     . THR C 125 ? 0.4451 0.7563 0.4154 0.1132  -0.1032 0.1453  124 THR A N     
3482 C  CA    . THR C 125 ? 0.4728 0.8055 0.4747 0.1171  -0.1158 0.1535  124 THR A CA    
3483 C  C     . THR C 125 ? 0.4453 0.7684 0.4820 0.1296  -0.1015 0.1685  124 THR A C     
3484 O  O     . THR C 125 ? 0.4615 0.8013 0.5254 0.1357  -0.1090 0.1777  124 THR A O     
3485 C  CB    . THR C 125 ? 0.4612 0.8150 0.4835 0.1045  -0.1301 0.1350  124 THR A CB    
3486 O  OG1   . THR C 125 ? 0.3878 0.7306 0.4278 0.1003  -0.1169 0.1241  124 THR A OG1   
3487 C  CG2   . THR C 125 ? 0.4995 0.8623 0.4880 0.0914  -0.1475 0.1183  124 THR A CG2   
3488 N  N     . VAL C 126 ? 0.4630 0.7590 0.4995 0.1336  -0.0810 0.1704  125 VAL A N     
3489 C  CA    . VAL C 126 ? 0.4328 0.7130 0.4976 0.1451  -0.0655 0.1820  125 VAL A CA    
3490 C  C     . VAL C 126 ? 0.5155 0.7684 0.5601 0.1529  -0.0524 0.1971  125 VAL A C     
3491 O  O     . VAL C 126 ? 0.5331 0.7660 0.5553 0.1483  -0.0420 0.1927  125 VAL A O     
3492 C  CB    . VAL C 126 ? 0.4325 0.7015 0.5180 0.1415  -0.0523 0.1692  125 VAL A CB    
3493 C  CG1   . VAL C 126 ? 0.4028 0.6516 0.5134 0.1530  -0.0347 0.1781  125 VAL A CG1   
3494 C  CG2   . VAL C 126 ? 0.3907 0.6870 0.4947 0.1312  -0.0653 0.1545  125 VAL A CG2   
3495 N  N     . ASP C 127 ? 0.5178 0.7706 0.5716 0.1640  -0.0535 0.2151  126 ASP A N     
3496 C  CA    . ASP C 127 ? 0.5777 0.8036 0.6178 0.1714  -0.0411 0.2315  126 ASP A CA    
3497 C  C     . ASP C 127 ? 0.5193 0.7109 0.5691 0.1725  -0.0191 0.2280  126 ASP A C     
3498 O  O     . ASP C 127 ? 0.5028 0.6904 0.5796 0.1748  -0.0122 0.2204  126 ASP A O     
3499 C  CB    . ASP C 127 ? 0.5649 0.7958 0.6222 0.1849  -0.0454 0.2509  126 ASP A CB    
3500 C  CG    . ASP C 127 ? 0.6240 0.8866 0.6700 0.1848  -0.0680 0.2572  126 ASP A CG    
3501 O  OD1   . ASP C 127 ? 0.6667 0.9465 0.6913 0.1734  -0.0803 0.2442  126 ASP A OD1   
3502 O  OD2   . ASP C 127 ? 0.7075 0.9774 0.7661 0.1962  -0.0739 0.2743  126 ASP A OD2   
3503 N  N     . THR C 128 ? 0.5493 0.7151 0.5770 0.1704  -0.0077 0.2340  127 THR A N     
3504 C  CA    . THR C 128 ? 0.5450 0.6739 0.5815 0.1712  0.0126  0.2330  127 THR A CA    
3505 C  C     . THR C 128 ? 0.5456 0.6596 0.6098 0.1832  0.0205  0.2419  127 THR A C     
3506 O  O     . THR C 128 ? 0.5352 0.6284 0.6163 0.1841  0.0335  0.2327  127 THR A O     
3507 C  CB    . THR C 128 ? 0.5917 0.6978 0.6024 0.1658  0.0222  0.2404  127 THR A CB    
3508 O  OG1   . THR C 128 ? 0.5682 0.6857 0.5546 0.1547  0.0185  0.2290  127 THR A OG1   
3509 C  CG2   . THR C 128 ? 0.5957 0.6615 0.6171 0.1646  0.0419  0.2388  127 THR A CG2   
3510 N  N     . LYS C 129 ? 0.5373 0.6597 0.6053 0.1931  0.0134  0.2593  128 LYS A N     
3511 C  CA    . LYS C 129 ? 0.5309 0.6366 0.6257 0.2054  0.0226  0.2665  128 LYS A CA    
3512 C  C     . LYS C 129 ? 0.5285 0.6553 0.6521 0.2094  0.0189  0.2561  128 LYS A C     
3513 O  O     . LYS C 129 ? 0.5455 0.6536 0.6900 0.2153  0.0324  0.2513  128 LYS A O     
3514 C  CB    . LYS C 129 ? 0.5988 0.7054 0.6930 0.2166  0.0171  0.2896  128 LYS A CB    
3515 C  CG    . LYS C 129 ? 0.5923 0.6730 0.7127 0.2302  0.0300  0.2974  128 LYS A CG    
3516 C  CD    . LYS C 129 ? 0.6637 0.7487 0.7876 0.2437  0.0226  0.3219  128 LYS A CD    
3517 C  CE    . LYS C 129 ? 0.7070 0.7972 0.8656 0.2596  0.0237  0.3268  128 LYS A CE    
3518 N  NZ    . LYS C 129 ? 0.6485 0.7848 0.8237 0.2616  0.0067  0.3227  128 LYS A NZ    
3519 N  N     . GLN C 130 ? 0.5137 0.6782 0.6375 0.2046  0.0016  0.2507  129 GLN A N     
3520 C  CA    . GLN C 130 ? 0.4831 0.6701 0.6354 0.2052  -0.0018 0.2397  129 GLN A CA    
3521 C  C     . GLN C 130 ? 0.4945 0.6618 0.6526 0.1988  0.0140  0.2213  129 GLN A C     
3522 O  O     . GLN C 130 ? 0.4552 0.6205 0.6384 0.2038  0.0231  0.2155  129 GLN A O     
3523 C  CB    . GLN C 130 ? 0.5589 0.7866 0.7068 0.1973  -0.0240 0.2353  129 GLN A CB    
3524 C  CG    . GLN C 130 ? 0.5560 0.8112 0.7348 0.1959  -0.0299 0.2256  129 GLN A CG    
3525 C  CD    . GLN C 130 ? 0.5952 0.8866 0.7673 0.1852  -0.0526 0.2194  129 GLN A CD    
3526 O  OE1   . GLN C 130 ? 0.5846 0.9006 0.7804 0.1800  -0.0596 0.2099  129 GLN A OE1   
3527 N  NE2   . GLN C 130 ? 0.5660 0.8597 0.7046 0.1808  -0.0639 0.2239  129 GLN A NE2   
3528 N  N     . ALA C 131 ? 0.4941 0.6468 0.6285 0.1879  0.0180  0.2121  130 ALA A N     
3529 C  CA    . ALA C 131 ? 0.4424 0.5743 0.5805 0.1821  0.0326  0.1955  130 ALA A CA    
3530 C  C     . ALA C 131 ? 0.4696 0.5599 0.6102 0.1878  0.0521  0.1971  130 ALA A C     
3531 O  O     . ALA C 131 ? 0.4626 0.5379 0.6146 0.1876  0.0646  0.1845  130 ALA A O     
3532 C  CB    . ALA C 131 ? 0.4305 0.5604 0.5449 0.1696  0.0302  0.1855  130 ALA A CB    
3533 N  N     . GLN C 132 ? 0.4731 0.5439 0.6018 0.1919  0.0548  0.2115  131 GLN A N     
3534 C  CA    . GLN C 132 ? 0.5257 0.5549 0.6572 0.1962  0.0721  0.2129  131 GLN A CA    
3535 C  C     . GLN C 132 ? 0.5344 0.5620 0.6921 0.2093  0.0781  0.2148  131 GLN A C     
3536 O  O     . GLN C 132 ? 0.5454 0.5440 0.7095 0.2107  0.0937  0.2042  131 GLN A O     
3537 C  CB    . GLN C 132 ? 0.5660 0.5779 0.6820 0.1972  0.0725  0.2300  131 GLN A CB    
3538 C  CG    . GLN C 132 ? 0.5870 0.5740 0.6806 0.1843  0.0796  0.2258  131 GLN A CG    
3539 C  CD    . GLN C 132 ? 0.5924 0.5786 0.6685 0.1836  0.0752  0.2446  131 GLN A CD    
3540 O  OE1   . GLN C 132 ? 0.6162 0.6181 0.6958 0.1935  0.0667  0.2606  131 GLN A OE1   
3541 N  NE2   . GLN C 132 ? 0.6388 0.6060 0.6970 0.1716  0.0818  0.2432  131 GLN A NE2   
3542 N  N     . ASP C 133 ? 0.5365 0.5933 0.7080 0.2193  0.0661  0.2287  132 ASP A N     
3543 C  CA    . ASP C 133 ? 0.5281 0.5877 0.7275 0.2330  0.0714  0.2313  132 ASP A CA    
3544 C  C     . ASP C 133 ? 0.4920 0.5583 0.7051 0.2294  0.0790  0.2120  132 ASP A C     
3545 O  O     . ASP C 133 ? 0.5062 0.5512 0.7312 0.2360  0.0944  0.2050  132 ASP A O     
3546 C  CB    . ASP C 133 ? 0.5226 0.6200 0.7366 0.2427  0.0542  0.2482  132 ASP A CB    
3547 C  CG    . ASP C 133 ? 0.5977 0.6879 0.7970 0.2477  0.0473  0.2692  132 ASP A CG    
3548 O  OD1   . ASP C 133 ? 0.6352 0.6876 0.8200 0.2464  0.0589  0.2726  132 ASP A OD1   
3549 O  OD2   . ASP C 133 ? 0.6020 0.7248 0.8029 0.2515  0.0295  0.2821  132 ASP A OD2   
3550 N  N     . LEU C 134 ? 0.4815 0.5749 0.6906 0.2183  0.0691  0.2024  133 LEU A N     
3551 C  CA    . LEU C 134 ? 0.4389 0.5407 0.6603 0.2136  0.0758  0.1853  133 LEU A CA    
3552 C  C     . LEU C 134 ? 0.4950 0.5566 0.7028 0.2082  0.0946  0.1697  133 LEU A C     
3553 O  O     . LEU C 134 ? 0.4750 0.5274 0.6935 0.2114  0.1076  0.1593  133 LEU A O     
3554 C  CB    . LEU C 134 ? 0.4266 0.5617 0.6450 0.2011  0.0613  0.1782  133 LEU A CB    
3555 C  CG    . LEU C 134 ? 0.4126 0.5565 0.6459 0.1962  0.0694  0.1625  133 LEU A CG    
3556 C  CD1   . LEU C 134 ? 0.3945 0.5635 0.6599 0.2071  0.0686  0.1689  133 LEU A CD1   
3557 C  CD2   . LEU C 134 ? 0.3808 0.5452 0.6077 0.1811  0.0600  0.1514  133 LEU A CD2   
3558 N  N     . ALA C 135 ? 0.5121 0.5514 0.6952 0.1988  0.0955  0.1668  134 ALA A N     
3559 C  CA    . ALA C 135 ? 0.4986 0.4981 0.6673 0.1924  0.1113  0.1521  134 ALA A CA    
3560 C  C     . ALA C 135 ? 0.5094 0.4759 0.6841 0.2022  0.1258  0.1532  134 ALA A C     
3561 O  O     . ALA C 135 ? 0.5193 0.4624 0.6914 0.2005  0.1397  0.1376  134 ALA A O     
3562 C  CB    . ALA C 135 ? 0.4671 0.4492 0.6119 0.1819  0.1089  0.1527  134 ALA A CB    
3563 N  N     . ARG C 136 ? 0.5240 0.4867 0.7046 0.2122  0.1226  0.1710  135 ARG A N     
3564 C  CA    . ARG C 136 ? 0.5539 0.4845 0.7423 0.2228  0.1359  0.1729  135 ARG A CA    
3565 C  C     . ARG C 136 ? 0.5415 0.4827 0.7510 0.2330  0.1439  0.1654  135 ARG A C     
3566 O  O     . ARG C 136 ? 0.6132 0.5234 0.8216 0.2358  0.1596  0.1533  135 ARG A O     
3567 C  CB    . ARG C 136 ? 0.6008 0.5311 0.7942 0.2329  0.1293  0.1960  135 ARG A CB    
3568 C  CG    . ARG C 136 ? 0.7049 0.5973 0.9057 0.2438  0.1426  0.1998  135 ARG A CG    
3569 C  CD    . ARG C 136 ? 0.7801 0.6714 0.9841 0.2531  0.1352  0.2249  135 ARG A CD    
3570 N  NE    . ARG C 136 ? 0.8197 0.7100 1.0015 0.2408  0.1270  0.2328  135 ARG A NE    
3571 C  CZ    . ARG C 136 ? 0.7900 0.7171 0.9659 0.2387  0.1106  0.2446  135 ARG A CZ    
3572 N  NH1   . ARG C 136 ? 0.7200 0.6878 0.9119 0.2477  0.0985  0.2514  135 ARG A NH1   
3573 N  NH2   . ARG C 136 ? 0.7602 0.6838 0.9134 0.2268  0.1059  0.2489  135 ARG A NH2   
3574 N  N     . SER C 137 ? 0.5053 0.4907 0.7337 0.2376  0.1333  0.1714  136 SER A N     
3575 C  CA    . SER C 137 ? 0.5284 0.5277 0.7807 0.2481  0.1412  0.1669  136 SER A CA    
3576 C  C     . SER C 137 ? 0.5143 0.5066 0.7583 0.2387  0.1527  0.1448  136 SER A C     
3577 O  O     . SER C 137 ? 0.5739 0.5624 0.8298 0.2465  0.1657  0.1371  136 SER A O     
3578 C  CB    . SER C 137 ? 0.4935 0.5440 0.7707 0.2537  0.1256  0.1795  136 SER A CB    
3579 O  OG    . SER C 137 ? 0.4937 0.5732 0.7672 0.2398  0.1159  0.1711  136 SER A OG    
3580 N  N     . TYR C 138 ? 0.5180 0.5097 0.7413 0.2225  0.1480  0.1351  137 TYR A N     
3581 C  CA    . TYR C 138 ? 0.4903 0.4711 0.6999 0.2121  0.1582  0.1146  137 TYR A CA    
3582 C  C     . TYR C 138 ? 0.5419 0.4729 0.7290 0.2085  0.1725  0.1015  137 TYR A C     
3583 O  O     . TYR C 138 ? 0.5566 0.4742 0.7315 0.2026  0.1833  0.0838  137 TYR A O     
3584 C  CB    . TYR C 138 ? 0.4901 0.4886 0.6867 0.1965  0.1467  0.1100  137 TYR A CB    
3585 C  CG    . TYR C 138 ? 0.4656 0.5122 0.6813 0.1952  0.1326  0.1169  137 TYR A CG    
3586 C  CD1   . TYR C 138 ? 0.4522 0.5272 0.6968 0.2061  0.1312  0.1250  137 TYR A CD1   
3587 C  CD2   . TYR C 138 ? 0.4551 0.5185 0.6609 0.1822  0.1208  0.1139  137 TYR A CD2   
3588 C  CE1   . TYR C 138 ? 0.4139 0.5328 0.6767 0.2022  0.1171  0.1299  137 TYR A CE1   
3589 C  CE2   . TYR C 138 ? 0.4210 0.5258 0.6435 0.1787  0.1072  0.1180  137 TYR A CE2   
3590 C  CZ    . TYR C 138 ? 0.4169 0.5494 0.6675 0.1877  0.1047  0.1259  137 TYR A CZ    
3591 O  OH    . TYR C 138 ? 0.3950 0.5681 0.6623 0.1816  0.0899  0.1286  137 TYR A OH    
3592 N  N     . GLY C 139 ? 0.5281 0.4320 0.7077 0.2102  0.1719  0.1096  138 GLY A N     
3593 C  CA    . GLY C 139 ? 0.5517 0.4084 0.7095 0.2029  0.1828  0.0963  138 GLY A CA    
3594 C  C     . GLY C 139 ? 0.5206 0.3680 0.6540 0.1844  0.1791  0.0845  138 GLY A C     
3595 O  O     . GLY C 139 ? 0.5435 0.3601 0.6581 0.1755  0.1882  0.0666  138 GLY A O     
3596 N  N     . ILE C 140 ? 0.4871 0.3604 0.6200 0.1787  0.1655  0.0938  139 ILE A N     
3597 C  CA    . ILE C 140 ? 0.5182 0.3862 0.6310 0.1627  0.1612  0.0844  139 ILE A CA    
3598 C  C     . ILE C 140 ? 0.4733 0.3416 0.5821 0.1597  0.1515  0.0997  139 ILE A C     
3599 O  O     . ILE C 140 ? 0.4615 0.3467 0.5827 0.1695  0.1445  0.1183  139 ILE A O     
3600 C  CB    . ILE C 140 ? 0.4825 0.3851 0.5968 0.1572  0.1552  0.0776  139 ILE A CB    
3601 C  CG1   . ILE C 140 ? 0.4227 0.3681 0.5536 0.1621  0.1402  0.0937  139 ILE A CG1   
3602 C  CG2   . ILE C 140 ? 0.4898 0.3922 0.6052 0.1586  0.1662  0.0630  139 ILE A CG2   
3603 C  CD1   . ILE C 140 ? 0.3906 0.3689 0.5263 0.1558  0.1344  0.0865  139 ILE A CD1   
3604 N  N     . PRO C 141 ? 0.4726 0.3232 0.5636 0.1459  0.1508  0.0926  140 PRO A N     
3605 C  CA    . PRO C 141 ? 0.4629 0.3168 0.5486 0.1418  0.1422  0.1073  140 PRO A CA    
3606 C  C     . PRO C 141 ? 0.4503 0.3475 0.5401 0.1441  0.1285  0.1163  140 PRO A C     
3607 O  O     . PRO C 141 ? 0.4146 0.3358 0.5089 0.1433  0.1252  0.1070  140 PRO A O     
3608 C  CB    . PRO C 141 ? 0.4352 0.2600 0.5030 0.1247  0.1461  0.0942  140 PRO A CB    
3609 C  CG    . PRO C 141 ? 0.4834 0.2841 0.5446 0.1204  0.1564  0.0726  140 PRO A CG    
3610 C  CD    . PRO C 141 ? 0.4981 0.3244 0.5717 0.1327  0.1579  0.0708  140 PRO A CD    
3611 N  N     . PHE C 142 ? 0.4509 0.3576 0.5368 0.1449  0.1202  0.1336  141 PHE A N     
3612 C  CA    . PHE C 142 ? 0.3865 0.3330 0.4700 0.1443  0.1052  0.1407  141 PHE A CA    
3613 C  C     . PHE C 142 ? 0.3945 0.3374 0.4575 0.1296  0.1010  0.1421  141 PHE A C     
3614 O  O     . PHE C 142 ? 0.4368 0.3560 0.4945 0.1294  0.1070  0.1541  141 PHE A O     
3615 C  CB    . PHE C 142 ? 0.4091 0.3825 0.5043 0.1577  0.0959  0.1586  141 PHE A CB    
3616 C  CG    . PHE C 142 ? 0.4079 0.4178 0.4947 0.1561  0.0794  0.1669  141 PHE A CG    
3617 C  CD1   . PHE C 142 ? 0.3616 0.3982 0.4477 0.1479  0.0705  0.1529  141 PHE A CD1   
3618 C  CD2   . PHE C 142 ? 0.4465 0.4640 0.5225 0.1588  0.0723  0.1844  141 PHE A CD2   
3619 C  CE1   . PHE C 142 ? 0.3582 0.4256 0.4329 0.1432  0.0548  0.1553  141 PHE A CE1   
3620 C  CE2   . PHE C 142 ? 0.4251 0.4748 0.4879 0.1563  0.0572  0.1891  141 PHE A CE2   
3621 C  CZ    . PHE C 142 ? 0.3755 0.4499 0.4376 0.1491  0.0481  0.1742  141 PHE A CZ    
3622 N  N     . ILE C 143 ? 0.3759 0.3428 0.4293 0.1181  0.0916  0.1311  142 ILE A N     
3623 C  CA    . ILE C 143 ? 0.3890 0.3583 0.4250 0.1046  0.0885  0.1297  142 ILE A CA    
3624 C  C     . ILE C 143 ? 0.3724 0.3781 0.4011 0.1036  0.0749  0.1290  142 ILE A C     
3625 O  O     . ILE C 143 ? 0.3340 0.3574 0.3682 0.1016  0.0685  0.1167  142 ILE A O     
3626 C  CB    . ILE C 143 ? 0.3969 0.3488 0.4277 0.0885  0.0936  0.1109  142 ILE A CB    
3627 C  CG1   . ILE C 143 ? 0.4648 0.3806 0.5019 0.0895  0.1058  0.1060  142 ILE A CG1   
3628 C  CG2   . ILE C 143 ? 0.3852 0.3426 0.4037 0.0756  0.0916  0.1101  142 ILE A CG2   
3629 C  CD1   . ILE C 143 ? 0.4950 0.3879 0.5248 0.0725  0.1105  0.0910  142 ILE A CD1   
3630 N  N     . GLU C 144 ? 0.3776 0.3928 0.3923 0.1040  0.0712  0.1416  143 GLU A N     
3631 C  CA    . GLU C 144 ? 0.3561 0.4016 0.3581 0.1011  0.0594  0.1374  143 GLU A CA    
3632 C  C     . GLU C 144 ? 0.3318 0.3750 0.3233 0.0870  0.0623  0.1234  143 GLU A C     
3633 O  O     . GLU C 144 ? 0.3422 0.3671 0.3306 0.0805  0.0720  0.1262  143 GLU A O     
3634 C  CB    . GLU C 144 ? 0.3803 0.4397 0.3678 0.1092  0.0541  0.1570  143 GLU A CB    
3635 C  CG    . GLU C 144 ? 0.4043 0.4796 0.4041 0.1233  0.0448  0.1687  143 GLU A CG    
3636 C  CD    . GLU C 144 ? 0.5260 0.6191 0.5084 0.1317  0.0362  0.1890  143 GLU A CD    
3637 O  OE1   . GLU C 144 ? 0.5936 0.6802 0.5542 0.1273  0.0417  0.1966  143 GLU A OE1   
3638 O  OE2   . GLU C 144 ? 0.5891 0.7038 0.5803 0.1411  0.0241  0.1965  143 GLU A OE2   
3639 N  N     . THR C 145 ? 0.2973 0.3587 0.2861 0.0822  0.0539  0.1087  144 THR A N     
3640 C  CA    . THR C 145 ? 0.2823 0.3430 0.2650 0.0710  0.0560  0.0948  144 THR A CA    
3641 C  C     . THR C 145 ? 0.2927 0.3756 0.2610 0.0702  0.0476  0.0883  144 THR A C     
3642 O  O     . THR C 145 ? 0.2765 0.3764 0.2406 0.0755  0.0373  0.0898  144 THR A O     
3643 C  CB    . THR C 145 ? 0.2995 0.3526 0.2947 0.0645  0.0561  0.0792  144 THR A CB    
3644 O  OG1   . THR C 145 ? 0.2413 0.3104 0.2428 0.0675  0.0465  0.0729  144 THR A OG1   
3645 C  CG2   . THR C 145 ? 0.2759 0.3041 0.2813 0.0647  0.0652  0.0821  144 THR A CG2   
3646 N  N     . SER C 146 ? 0.2851 0.3678 0.2475 0.0628  0.0518  0.0791  145 SER A N     
3647 C  CA    . SER C 146 ? 0.2858 0.3841 0.2371 0.0613  0.0452  0.0666  145 SER A CA    
3648 C  C     . SER C 146 ? 0.3134 0.4054 0.2742 0.0537  0.0484  0.0527  145 SER A C     
3649 O  O     . SER C 146 ? 0.2962 0.3820 0.2599 0.0495  0.0576  0.0548  145 SER A O     
3650 C  CB    . SER C 146 ? 0.2735 0.3826 0.2022 0.0645  0.0484  0.0733  145 SER A CB    
3651 O  OG    . SER C 146 ? 0.3145 0.4336 0.2323 0.0626  0.0459  0.0579  145 SER A OG    
3652 N  N     . ALA C 147 ? 0.2792 0.3734 0.2471 0.0515  0.0405  0.0401  146 ALA A N     
3653 C  CA    . ALA C 147 ? 0.2838 0.3731 0.2592 0.0458  0.0421  0.0286  146 ALA A CA    
3654 C  C     . ALA C 147 ? 0.2812 0.3785 0.2462 0.0467  0.0455  0.0224  146 ALA A C     
3655 O  O     . ALA C 147 ? 0.2533 0.3482 0.2268 0.0437  0.0498  0.0169  146 ALA A O     
3656 C  CB    . ALA C 147 ? 0.2665 0.3551 0.2509 0.0434  0.0336  0.0189  146 ALA A CB    
3657 N  N     . LYS C 148 ? 0.2633 0.3711 0.2101 0.0515  0.0436  0.0229  147 LYS A N     
3658 C  CA    . LYS C 148 ? 0.2992 0.4146 0.2323 0.0539  0.0490  0.0157  147 LYS A CA    
3659 C  C     . LYS C 148 ? 0.3234 0.4413 0.2555 0.0540  0.0630  0.0268  147 LYS A C     
3660 O  O     . LYS C 148 ? 0.3046 0.4262 0.2421 0.0537  0.0711  0.0212  147 LYS A O     
3661 C  CB    . LYS C 148 ? 0.3067 0.4325 0.2153 0.0581  0.0422  0.0119  147 LYS A CB    
3662 C  CG    . LYS C 148 ? 0.3708 0.5028 0.2601 0.0616  0.0489  0.0014  147 LYS A CG    
3663 C  CD    . LYS C 148 ? 0.3781 0.5167 0.2436 0.0632  0.0377  -0.0091 147 LYS A CD    
3664 C  CE    . LYS C 148 ? 0.4320 0.5745 0.2746 0.0675  0.0463  -0.0215 147 LYS A CE    
3665 N  NZ    . LYS C 148 ? 0.5500 0.6982 0.3660 0.0675  0.0331  -0.0319 147 LYS A NZ    
3666 N  N     . THR C 149 ? 0.3075 0.4246 0.2340 0.0549  0.0665  0.0435  148 THR A N     
3667 C  CA    . THR C 149 ? 0.2971 0.4156 0.2246 0.0531  0.0805  0.0558  148 THR A CA    
3668 C  C     . THR C 149 ? 0.2790 0.3848 0.2306 0.0454  0.0845  0.0613  148 THR A C     
3669 O  O     . THR C 149 ? 0.2874 0.3949 0.2457 0.0410  0.0957  0.0700  148 THR A O     
3670 C  CB    . THR C 149 ? 0.3153 0.4367 0.2233 0.0574  0.0839  0.0736  148 THR A CB    
3671 O  OG1   . THR C 149 ? 0.2936 0.4020 0.2116 0.0574  0.0783  0.0837  148 THR A OG1   
3672 C  CG2   . THR C 149 ? 0.3104 0.4455 0.1894 0.0642  0.0778  0.0687  148 THR A CG2   
3673 N  N     . ARG C 150 ? 0.2393 0.3334 0.2035 0.0428  0.0761  0.0561  149 ARG A N     
3674 C  CA    . ARG C 150 ? 0.2788 0.3578 0.2606 0.0353  0.0777  0.0587  149 ARG A CA    
3675 C  C     . ARG C 150 ? 0.2736 0.3386 0.2540 0.0358  0.0819  0.0738  149 ARG A C     
3676 O  O     . ARG C 150 ? 0.2942 0.3431 0.2866 0.0293  0.0840  0.0746  149 ARG A O     
3677 C  CB    . ARG C 150 ? 0.2673 0.3495 0.2645 0.0271  0.0842  0.0570  149 ARG A CB    
3678 C  CG    . ARG C 150 ? 0.2695 0.3666 0.2707 0.0291  0.0827  0.0450  149 ARG A CG    
3679 C  CD    . ARG C 150 ? 0.2874 0.3900 0.3106 0.0212  0.0861  0.0440  149 ARG A CD    
3680 N  NE    . ARG C 150 ? 0.3566 0.4491 0.3883 0.0169  0.0760  0.0365  149 ARG A NE    
3681 C  CZ    . ARG C 150 ? 0.3452 0.4237 0.3828 0.0084  0.0738  0.0390  149 ARG A CZ    
3682 N  NH1   . ARG C 150 ? 0.3692 0.4424 0.4118 0.0014  0.0808  0.0482  149 ARG A NH1   
3683 N  NH2   . ARG C 150 ? 0.3135 0.3817 0.3504 0.0068  0.0653  0.0320  149 ARG A NH2   
3684 N  N     . GLN C 151 ? 0.2634 0.3327 0.2289 0.0432  0.0830  0.0855  150 GLN A N     
3685 C  CA    . GLN C 151 ? 0.2569 0.3109 0.2229 0.0456  0.0869  0.1016  150 GLN A CA    
3686 C  C     . GLN C 151 ? 0.2966 0.3347 0.2746 0.0464  0.0818  0.0964  150 GLN A C     
3687 O  O     . GLN C 151 ? 0.2920 0.3379 0.2701 0.0509  0.0728  0.0876  150 GLN A O     
3688 C  CB    . GLN C 151 ? 0.3037 0.3683 0.2508 0.0558  0.0844  0.1145  150 GLN A CB    
3689 C  CG    . GLN C 151 ? 0.3757 0.4239 0.3251 0.0611  0.0875  0.1335  150 GLN A CG    
3690 C  CD    . GLN C 151 ? 0.4108 0.4721 0.3404 0.0715  0.0838  0.1494  150 GLN A CD    
3691 O  OE1   . GLN C 151 ? 0.4061 0.4865 0.3155 0.0725  0.0833  0.1487  150 GLN A OE1   
3692 N  NE2   . GLN C 151 ? 0.5250 0.5764 0.4592 0.0805  0.0811  0.1640  150 GLN A NE2   
3693 N  N     . GLY C 152 ? 0.3211 0.3367 0.3094 0.0410  0.0886  0.1006  151 GLY A N     
3694 C  CA    . GLY C 152 ? 0.3054 0.3013 0.3023 0.0428  0.0878  0.0971  151 GLY A CA    
3695 C  C     . GLY C 152 ? 0.3301 0.3250 0.3332 0.0372  0.0828  0.0790  151 GLY A C     
3696 O  O     . GLY C 152 ? 0.3080 0.2878 0.3156 0.0397  0.0835  0.0751  151 GLY A O     
3697 N  N     . VAL C 153 ? 0.2836 0.2939 0.2864 0.0312  0.0785  0.0689  152 VAL A N     
3698 C  CA    . VAL C 153 ? 0.2512 0.2623 0.2578 0.0275  0.0725  0.0544  152 VAL A CA    
3699 C  C     . VAL C 153 ? 0.3076 0.2974 0.3189 0.0185  0.0757  0.0491  152 VAL A C     
3700 O  O     . VAL C 153 ? 0.2919 0.2707 0.3024 0.0197  0.0751  0.0426  152 VAL A O     
3701 C  CB    . VAL C 153 ? 0.2458 0.2755 0.2527 0.0242  0.0676  0.0465  152 VAL A CB    
3702 C  CG1   . VAL C 153 ? 0.2593 0.2868 0.2707 0.0189  0.0617  0.0344  152 VAL A CG1   
3703 C  CG2   . VAL C 153 ? 0.2671 0.3149 0.2660 0.0326  0.0631  0.0468  152 VAL A CG2   
3704 N  N     . ASP C 154 ? 0.3115 0.2954 0.3274 0.0087  0.0797  0.0515  153 ASP A N     
3705 C  CA    . ASP C 154 ? 0.3051 0.2672 0.3238 -0.0018 0.0813  0.0451  153 ASP A CA    
3706 C  C     . ASP C 154 ? 0.3618 0.2973 0.3773 0.0035  0.0882  0.0486  153 ASP A C     
3707 O  O     . ASP C 154 ? 0.3820 0.2999 0.3934 0.0018  0.0886  0.0385  153 ASP A O     
3708 C  CB    . ASP C 154 ? 0.3541 0.3171 0.3824 -0.0150 0.0837  0.0482  153 ASP A CB    
3709 C  CG    . ASP C 154 ? 0.3404 0.3265 0.3761 -0.0214 0.0765  0.0415  153 ASP A CG    
3710 O  OD1   . ASP C 154 ? 0.3177 0.3121 0.3493 -0.0178 0.0693  0.0333  153 ASP A OD1   
3711 O  OD2   . ASP C 154 ? 0.3337 0.3307 0.3818 -0.0301 0.0784  0.0454  153 ASP A OD2   
3712 N  N     . ASP C 155 ? 0.3247 0.2569 0.3409 0.0115  0.0940  0.0632  154 ASP A N     
3713 C  CA    . ASP C 155 ? 0.3742 0.2800 0.3907 0.0188  0.1012  0.0691  154 ASP A CA    
3714 C  C     . ASP C 155 ? 0.3555 0.2608 0.3700 0.0292  0.0997  0.0613  154 ASP A C     
3715 O  O     . ASP C 155 ? 0.4019 0.2819 0.4161 0.0308  0.1058  0.0554  154 ASP A O     
3716 C  CB    . ASP C 155 ? 0.4139 0.3224 0.4308 0.0280  0.1056  0.0894  154 ASP A CB    
3717 C  CG    . ASP C 155 ? 0.5029 0.3805 0.5233 0.0361  0.1142  0.0991  154 ASP A CG    
3718 O  OD1   . ASP C 155 ? 0.5357 0.3842 0.5583 0.0313  0.1190  0.0888  154 ASP A OD1   
3719 O  OD2   . ASP C 155 ? 0.5164 0.3980 0.5363 0.0477  0.1160  0.1175  154 ASP A OD2   
3720 N  N     . ALA C 156 ? 0.3190 0.2515 0.3326 0.0354  0.0924  0.0600  155 ALA A N     
3721 C  CA    . ALA C 156 ? 0.3456 0.2815 0.3612 0.0446  0.0919  0.0549  155 ALA A CA    
3722 C  C     . ALA C 156 ? 0.3347 0.2581 0.3452 0.0365  0.0932  0.0389  155 ALA A C     
3723 O  O     . ALA C 156 ? 0.3447 0.2518 0.3549 0.0420  0.1004  0.0343  155 ALA A O     
3724 C  CB    . ALA C 156 ? 0.3057 0.2733 0.3229 0.0499  0.0828  0.0565  155 ALA A CB    
3725 N  N     . PHE C 157 ? 0.3293 0.2610 0.3350 0.0245  0.0867  0.0305  156 PHE A N     
3726 C  CA    . PHE C 157 ? 0.3328 0.2550 0.3299 0.0165  0.0859  0.0167  156 PHE A CA    
3727 C  C     . PHE C 157 ? 0.3684 0.2599 0.3594 0.0085  0.0919  0.0101  156 PHE A C     
3728 O  O     . PHE C 157 ? 0.3650 0.2395 0.3460 0.0081  0.0965  -0.0004 156 PHE A O     
3729 C  CB    . PHE C 157 ? 0.2999 0.2408 0.2954 0.0073  0.0758  0.0121  156 PHE A CB    
3730 C  CG    . PHE C 157 ? 0.2760 0.2404 0.2750 0.0136  0.0702  0.0140  156 PHE A CG    
3731 C  CD1   . PHE C 157 ? 0.2550 0.2218 0.2497 0.0150  0.0699  0.0084  156 PHE A CD1   
3732 C  CD2   . PHE C 157 ? 0.2681 0.2513 0.2735 0.0172  0.0660  0.0208  156 PHE A CD2   
3733 C  CE1   . PHE C 157 ? 0.2423 0.2290 0.2425 0.0186  0.0644  0.0102  156 PHE A CE1   
3734 C  CE2   . PHE C 157 ? 0.2517 0.2535 0.2598 0.0214  0.0600  0.0201  156 PHE A CE2   
3735 C  CZ    . PHE C 157 ? 0.2191 0.2216 0.2261 0.0213  0.0590  0.0149  156 PHE A CZ    
3736 N  N     . TYR C 158 ? 0.3551 0.2370 0.3514 0.0022  0.0932  0.0161  157 TYR A N     
3737 C  CA    . TYR C 158 ? 0.4031 0.2524 0.3949 -0.0076 0.0984  0.0088  157 TYR A CA    
3738 C  C     . TYR C 158 ? 0.4149 0.2361 0.4055 0.0045  0.1105  0.0094  157 TYR A C     
3739 O  O     . TYR C 158 ? 0.4271 0.2192 0.4078 0.0002  0.1160  -0.0035 157 TYR A O     
3740 C  CB    . TYR C 158 ? 0.4006 0.2473 0.4024 -0.0187 0.0979  0.0170  157 TYR A CB    
3741 C  CG    . TYR C 158 ? 0.3944 0.2657 0.4010 -0.0320 0.0876  0.0146  157 TYR A CG    
3742 C  CD1   . TYR C 158 ? 0.3833 0.2779 0.3856 -0.0312 0.0787  0.0083  157 TYR A CD1   
3743 C  CD2   . TYR C 158 ? 0.3982 0.2704 0.4169 -0.0446 0.0877  0.0207  157 TYR A CD2   
3744 C  CE1   . TYR C 158 ? 0.4050 0.3224 0.4147 -0.0405 0.0697  0.0075  157 TYR A CE1   
3745 C  CE2   . TYR C 158 ? 0.4286 0.3272 0.4565 -0.0547 0.0793  0.0197  157 TYR A CE2   
3746 C  CZ    . TYR C 158 ? 0.4138 0.3348 0.4373 -0.0518 0.0699  0.0128  157 TYR A CZ    
3747 O  OH    . TYR C 158 ? 0.4461 0.3935 0.4815 -0.0596 0.0616  0.0129  157 TYR A OH    
3748 N  N     . THR C 159 ? 0.3788 0.2087 0.3790 0.0203  0.1144  0.0240  158 THR A N     
3749 C  CA    . THR C 159 ? 0.4246 0.2311 0.4287 0.0347  0.1258  0.0276  158 THR A CA    
3750 C  C     . THR C 159 ? 0.4332 0.2398 0.4312 0.0422  0.1303  0.0151  158 THR A C     
3751 O  O     . THR C 159 ? 0.4849 0.2631 0.4803 0.0490  0.1418  0.0082  158 THR A O     
3752 C  CB    . THR C 159 ? 0.4505 0.2735 0.4674 0.0499  0.1259  0.0485  158 THR A CB    
3753 O  OG1   . THR C 159 ? 0.4302 0.2476 0.4499 0.0432  0.1254  0.0612  158 THR A OG1   
3754 C  CG2   . THR C 159 ? 0.4563 0.2621 0.4820 0.0688  0.1365  0.0544  158 THR A CG2   
3755 N  N     . LEU C 160 ? 0.3706 0.2076 0.3665 0.0414  0.1227  0.0122  159 LEU A N     
3756 C  CA    . LEU C 160 ? 0.3978 0.2365 0.3873 0.0466  0.1282  0.0015  159 LEU A CA    
3757 C  C     . LEU C 160 ? 0.4567 0.2696 0.4248 0.0339  0.1312  -0.0173 159 LEU A C     
3758 O  O     . LEU C 160 ? 0.4730 0.2659 0.4322 0.0400  0.1431  -0.0277 159 LEU A O     
3759 C  CB    . LEU C 160 ? 0.3342 0.2100 0.3273 0.0466  0.1190  0.0044  159 LEU A CB    
3760 C  CG    . LEU C 160 ? 0.3262 0.2088 0.3135 0.0499  0.1248  -0.0043 159 LEU A CG    
3761 C  CD1   . LEU C 160 ? 0.3529 0.2289 0.3524 0.0676  0.1394  -0.0012 159 LEU A CD1   
3762 C  CD2   . LEU C 160 ? 0.3428 0.2585 0.3346 0.0467  0.1147  -0.0006 159 LEU A CD2   
3763 N  N     . VAL C 161 ? 0.4475 0.2606 0.4070 0.0165  0.1206  -0.0223 160 VAL A N     
3764 C  CA    . VAL C 161 ? 0.4888 0.2765 0.4275 0.0028  0.1209  -0.0400 160 VAL A CA    
3765 C  C     . VAL C 161 ? 0.5427 0.2890 0.4791 0.0055  0.1334  -0.0461 160 VAL A C     
3766 O  O     . VAL C 161 ? 0.5456 0.2671 0.4639 0.0056  0.1420  -0.0622 160 VAL A O     
3767 C  CB    . VAL C 161 ? 0.4670 0.2645 0.4035 -0.0162 0.1062  -0.0419 160 VAL A CB    
3768 C  CG1   . VAL C 161 ? 0.5068 0.2752 0.4232 -0.0327 0.1045  -0.0603 160 VAL A CG1   
3769 C  CG2   . VAL C 161 ? 0.4220 0.2544 0.3582 -0.0171 0.0957  -0.0383 160 VAL A CG2   
3770 N  N     . ARG C 162 ? 0.5104 0.2472 0.4643 0.0091  0.1359  -0.0330 161 ARG A N     
3771 C  CA    . ARG C 162 ? 0.5842 0.2768 0.5380 0.0127  0.1487  -0.0373 161 ARG A CA    
3772 C  C     . ARG C 162 ? 0.6004 0.2813 0.5544 0.0337  0.1640  -0.0402 161 ARG A C     
3773 O  O     . ARG C 162 ? 0.6477 0.3022 0.5930 0.0341  0.1711  -0.0517 161 ARG A O     
3774 C  CB    . ARG C 162 ? 0.5218 0.2077 0.4951 0.0136  0.1490  -0.0182 161 ARG A CB    
3775 C  CG    . ARG C 162 ? 0.5597 0.2478 0.5343 -0.0090 0.1384  -0.0180 161 ARG A CG    
3776 C  CD    . ARG C 162 ? 0.5987 0.2757 0.5908 -0.0091 0.1421  0.0015  161 ARG A CD    
3777 N  NE    . ARG C 162 ? 0.5969 0.2869 0.5949 -0.0297 0.1328  0.0046  161 ARG A NE    
3778 C  CZ    . ARG C 162 ? 0.5790 0.3063 0.5869 -0.0293 0.1264  0.0197  161 ARG A CZ    
3779 N  NH1   . ARG C 162 ? 0.5660 0.3191 0.5769 -0.0113 0.1266  0.0325  161 ARG A NH1   
3780 N  NH2   . ARG C 162 ? 0.6027 0.3425 0.6184 -0.0475 0.1200  0.0215  161 ARG A NH2   
3781 N  N     . GLU C 163 ? 0.5350 0.2500 0.5015 0.0491  0.1642  -0.0284 162 GLU A N     
3782 C  CA    . GLU C 163 ? 0.6059 0.3232 0.5776 0.0669  0.1757  -0.0293 162 GLU A CA    
3783 C  C     . GLU C 163 ? 0.6163 0.3306 0.5645 0.0609  0.1794  -0.0492 162 GLU A C     
3784 O  O     . GLU C 163 ? 0.6454 0.3462 0.5892 0.0678  0.1888  -0.0569 162 GLU A O     
3785 C  CB    . GLU C 163 ? 0.5693 0.3256 0.5630 0.0825  0.1736  -0.0116 162 GLU A CB    
3786 C  CG    . GLU C 163 ? 0.5088 0.2712 0.5238 0.0916  0.1698  0.0105  162 GLU A CG    
3787 C  CD    . GLU C 163 ? 0.5944 0.3369 0.6200 0.1024  0.1771  0.0175  162 GLU A CD    
3788 O  OE1   . GLU C 163 ? 0.5775 0.3307 0.6146 0.1166  0.1830  0.0201  162 GLU A OE1   
3789 O  OE2   . GLU C 163 ? 0.6071 0.3231 0.6307 0.0956  0.1771  0.0205  162 GLU A OE2   
3790 N  N     . ILE C 164 ? 0.5995 0.3256 0.5307 0.0481  0.1720  -0.0576 163 ILE A N     
3791 C  CA    . ILE C 164 ? 0.5902 0.3152 0.4955 0.0417  0.1742  -0.0743 163 ILE A CA    
3792 C  C     . ILE C 164 ? 0.6934 0.3817 0.5778 0.0311  0.1757  -0.0916 163 ILE A C     
3793 O  O     . ILE C 164 ? 0.7408 0.4198 0.6118 0.0355  0.1840  -0.1025 163 ILE A O     
3794 C  CB    . ILE C 164 ? 0.5735 0.3225 0.4652 0.0291  0.1624  -0.0763 163 ILE A CB    
3795 C  CG1   . ILE C 164 ? 0.5079 0.2982 0.4227 0.0394  0.1591  -0.0587 163 ILE A CG1   
3796 C  CG2   . ILE C 164 ? 0.5709 0.3141 0.4302 0.0220  0.1652  -0.0930 163 ILE A CG2   
3797 C  CD1   . ILE C 164 ? 0.4401 0.2602 0.3500 0.0270  0.1425  -0.0545 163 ILE A CD1   
3798 N  N     . ARG C 165 ? 0.6508 0.3188 0.5340 0.0166  0.1677  -0.0943 164 ARG A N     
3799 C  CA    . ARG C 165 ? 0.7371 0.3713 0.6041 0.0050  0.1671  -0.1104 164 ARG A CA    
3800 C  C     . ARG C 165 ? 0.7975 0.4107 0.6740 0.0208  0.1809  -0.1102 164 ARG A C     
3801 O  O     . ARG C 165 ? 0.8536 0.4479 0.7113 0.0203  0.1865  -0.1265 164 ARG A O     
3802 C  CB    . ARG C 165 ? 0.7332 0.3536 0.6071 -0.0129 0.1562  -0.1087 164 ARG A CB    
3803 C  CG    . ARG C 165 ? 0.6808 0.3220 0.5507 -0.0286 0.1423  -0.1076 164 ARG A CG    
3804 C  CD    . ARG C 165 ? 0.7374 0.3710 0.6248 -0.0444 0.1334  -0.1000 164 ARG A CD    
3805 N  NE    . ARG C 165 ? 0.7752 0.4354 0.6579 -0.0642 0.1144  -0.1025 164 ARG A NE    
3806 C  CZ    . ARG C 165 ? 0.7434 0.4163 0.6449 -0.0784 0.1034  -0.0933 164 ARG A CZ    
3807 N  NH1   . ARG C 165 ? 0.7698 0.4257 0.6919 -0.0790 0.1095  -0.0824 164 ARG A NH1   
3808 N  NH2   . ARG C 165 ? 0.7272 0.4304 0.6273 -0.0923 0.0866  -0.0942 164 ARG A NH2   
3809 N  N     . LYS C 166 ? 0.7471 0.3635 0.6521 0.0352  0.1860  -0.0913 165 LYS A N     
3810 C  CA    . LYS C 166 ? 0.7757 0.3744 0.6927 0.0517  0.1984  -0.0887 165 LYS A CA    
3811 C  C     . LYS C 166 ? 0.8101 0.4192 0.7193 0.0647  0.2091  -0.0967 165 LYS A C     
3812 O  O     . LYS C 166 ? 0.8755 0.4600 0.7764 0.0698  0.2186  -0.1089 165 LYS A O     
3813 C  CB    . LYS C 166 ? 0.7636 0.3745 0.7121 0.0665  0.1998  -0.0638 165 LYS A CB    
3814 C  CG    . LYS C 166 ? 0.8288 0.4204 0.7867 0.0567  0.1938  -0.0545 165 LYS A CG    
3815 C  CD    . LYS C 166 ? 0.8550 0.4554 0.8405 0.0732  0.1961  -0.0291 165 LYS A CD    
3816 C  CE    . LYS C 166 ? 0.8121 0.4477 0.8126 0.0936  0.1995  -0.0171 165 LYS A CE    
3817 N  NZ    . LYS C 166 ? 0.8341 0.4825 0.8596 0.1081  0.1981  0.0087  165 LYS A NZ    
3818 N  N     . HIS C 167 ? 0.7596 0.4052 0.6724 0.0701  0.2080  -0.0897 166 HIS A N     
3819 C  CA    . HIS C 167 ? 0.8045 0.4644 0.7132 0.0815  0.2184  -0.0947 166 HIS A CA    
3820 C  C     . HIS C 167 ? 0.8764 0.5189 0.7491 0.0700  0.2202  -0.1180 166 HIS A C     
3821 O  O     . HIS C 167 ? 0.9293 0.5602 0.7940 0.0788  0.2323  -0.1283 166 HIS A O     
3822 C  CB    . HIS C 167 ? 0.7198 0.4236 0.6416 0.0863  0.2149  -0.0813 166 HIS A CB    
3823 C  CG    . HIS C 167 ? 0.7516 0.4746 0.6714 0.0955  0.2248  -0.0846 166 HIS A CG    
3824 N  ND1   . HIS C 167 ? 0.8111 0.5354 0.7011 0.0861  0.2260  -0.0989 166 HIS A ND1   
3825 C  CD2   . HIS C 167 ? 0.7295 0.4726 0.6740 0.1127  0.2338  -0.0744 166 HIS A CD2   
3826 C  CE1   . HIS C 167 ? 0.8063 0.5498 0.7028 0.0973  0.2369  -0.0974 166 HIS A CE1   
3827 N  NE2   . HIS C 167 ? 0.7598 0.5155 0.6906 0.1132  0.2417  -0.0831 166 HIS A NE2   
3828 N  N     . LYS C 168 ? 0.8897 0.5301 0.7399 0.0504  0.2076  -0.1265 167 LYS A N     
3829 C  CA    . LYS C 168 ? 0.9373 0.5628 0.7509 0.0371  0.2052  -0.1478 167 LYS A CA    
3830 C  C     . LYS C 168 ? 1.0128 0.5968 0.8160 0.0340  0.2091  -0.1639 167 LYS A C     
3831 O  O     . LYS C 168 ? 1.0435 0.6133 0.8185 0.0308  0.2129  -0.1826 167 LYS A O     
3832 C  CB    . LYS C 168 ? 0.9295 0.5637 0.7266 0.0162  0.1876  -0.1506 167 LYS A CB    
3833 C  CG    . LYS C 168 ? 0.9216 0.5925 0.7157 0.0160  0.1831  -0.1415 167 LYS A CG    
3834 C  CD    . LYS C 168 ? 1.0397 0.7244 0.8185 0.0246  0.1935  -0.1458 167 LYS A CD    
3835 C  CE    . LYS C 168 ? 1.1129 0.8206 0.8685 0.0130  0.1832  -0.1459 167 LYS A CE    
3836 N  NZ    . LYS C 168 ? 0.9946 0.7381 0.7716 0.0211  0.1843  -0.1273 167 LYS A NZ    
3837 N  N     . GLU C 169 ? 1.0132 0.5772 0.8382 0.0354  0.2086  -0.1565 168 GLU A N     
3838 C  CA    . GLU C 169 ? 1.0627 0.5855 0.8792 0.0256  0.2070  -0.1707 168 GLU A CA    
3839 C  C     . GLU C 169 ? 1.1224 0.6390 0.9153 -0.0005 0.1897  -0.1843 168 GLU A C     
3840 O  O     . GLU C 169 ? 1.0707 0.5929 0.8755 -0.0134 0.1774  -0.1753 168 GLU A O     
3841 C  CB    . GLU C 169 ? 1.1009 0.5986 0.9034 0.0363  0.2212  -0.1875 168 GLU A CB    
3842 C  CG    . GLU C 169 ? 1.1199 0.6020 0.9498 0.0574  0.2357  -0.1778 168 GLU A CG    
3843 C  CD    . GLU C 169 ? 1.1272 0.6432 0.9801 0.0790  0.2459  -0.1601 168 GLU A CD    
3844 O  OE1   . GLU C 169 ? 1.0727 0.6252 0.9291 0.0770  0.2399  -0.1493 168 GLU A OE1   
3845 O  OE2   . GLU C 169 ? 1.1955 0.7017 1.0644 0.0978  0.2596  -0.1572 168 GLU A OE2   
3846 N  N     . GLY D 1   ? 0.2640 0.6279 0.6914 -0.1080 0.1151  0.0855  0   GLY C N     
3847 C  CA    . GLY D 1   ? 0.2940 0.6184 0.6934 -0.1068 0.1127  0.0851  0   GLY C CA    
3848 C  C     . GLY D 1   ? 0.3007 0.6108 0.6748 -0.1146 0.1263  0.0803  0   GLY C C     
3849 O  O     . GLY D 1   ? 0.2993 0.6294 0.6811 -0.1147 0.1411  0.0764  0   GLY C O     
3850 N  N     . MET D 2   ? 0.3030 0.5800 0.6466 -0.1215 0.1214  0.0811  1   MET C N     
3851 C  CA    . MET D 2   ? 0.3389 0.6041 0.6589 -0.1287 0.1335  0.0779  1   MET C CA    
3852 C  C     . MET D 2   ? 0.3293 0.5903 0.6517 -0.1148 0.1476  0.0717  1   MET C C     
3853 O  O     . MET D 2   ? 0.3206 0.5754 0.6525 -0.1003 0.1445  0.0695  1   MET C O     
3854 C  CB    . MET D 2   ? 0.3926 0.6255 0.6802 -0.1394 0.1240  0.0815  1   MET C CB    
3855 C  CG    . MET D 2   ? 0.3556 0.5649 0.6351 -0.1310 0.1143  0.0826  1   MET C CG    
3856 S  SD    . MET D 2   ? 0.3365 0.5128 0.5806 -0.1421 0.1040  0.0881  1   MET C SD    
3857 C  CE    . MET D 2   ? 0.3238 0.4963 0.5697 -0.1493 0.0900  0.0928  1   MET C CE    
3858 N  N     . THR D 3   ? 0.3369 0.5989 0.6462 -0.1196 0.1632  0.0672  2   THR C N     
3859 C  CA    . THR D 3   ? 0.3536 0.6044 0.6557 -0.1081 0.1771  0.0585  2   THR C CA    
3860 C  C     . THR D 3   ? 0.3854 0.6013 0.6529 -0.1108 0.1688  0.0565  2   THR C C     
3861 O  O     . THR D 3   ? 0.3369 0.5408 0.5844 -0.1235 0.1599  0.0618  2   THR C O     
3862 C  CB    . THR D 3   ? 0.3493 0.6127 0.6473 -0.1121 0.1981  0.0531  2   THR C CB    
3863 O  OG1   . THR D 3   ? 0.3498 0.6487 0.6760 -0.1106 0.2004  0.0555  2   THR C OG1   
3864 C  CG2   . THR D 3   ? 0.3856 0.6363 0.6771 -0.0977 0.2130  0.0425  2   THR C CG2   
3865 N  N     . GLU D 4   ? 0.3466 0.5465 0.6079 -0.0983 0.1708  0.0496  3   GLU C N     
3866 C  CA    . GLU D 4   ? 0.3788 0.5501 0.6116 -0.1002 0.1629  0.0470  3   GLU C CA    
3867 C  C     . GLU D 4   ? 0.4004 0.5587 0.6081 -0.1028 0.1776  0.0382  3   GLU C C     
3868 O  O     . GLU D 4   ? 0.4445 0.6095 0.6593 -0.0959 0.1944  0.0317  3   GLU C O     
3869 C  CB    . GLU D 4   ? 0.4248 0.5841 0.6642 -0.0877 0.1538  0.0454  3   GLU C CB    
3870 C  CG    . GLU D 4   ? 0.4129 0.5847 0.6774 -0.0834 0.1411  0.0528  3   GLU C CG    
3871 C  CD    . GLU D 4   ? 0.4537 0.6083 0.7159 -0.0759 0.1290  0.0529  3   GLU C CD    
3872 O  OE1   . GLU D 4   ? 0.4915 0.6257 0.7363 -0.0725 0.1312  0.0467  3   GLU C OE1   
3873 O  OE2   . GLU D 4   ? 0.4210 0.5827 0.6984 -0.0746 0.1177  0.0592  3   GLU C OE2   
3874 N  N     . TYR D 5   ? 0.3961 0.5364 0.5741 -0.1129 0.1713  0.0383  4   TYR C N     
3875 C  CA    . TYR D 5   ? 0.4358 0.5616 0.5838 -0.1195 0.1822  0.0307  4   TYR C CA    
3876 C  C     . TYR D 5   ? 0.4273 0.5323 0.5543 -0.1213 0.1714  0.0281  4   TYR C C     
3877 O  O     . TYR D 5   ? 0.4167 0.5201 0.5405 -0.1255 0.1552  0.0350  4   TYR C O     
3878 C  CB    . TYR D 5   ? 0.4119 0.5409 0.5411 -0.1348 0.1855  0.0347  4   TYR C CB    
3879 C  CG    . TYR D 5   ? 0.4557 0.6071 0.6040 -0.1365 0.1982  0.0368  4   TYR C CG    
3880 C  CD1   . TYR D 5   ? 0.4521 0.6144 0.6057 -0.1465 0.1908  0.0469  4   TYR C CD1   
3881 C  CD2   . TYR D 5   ? 0.4639 0.6245 0.6216 -0.1296 0.2191  0.0283  4   TYR C CD2   
3882 C  CE1   . TYR D 5   ? 0.4868 0.6720 0.6579 -0.1512 0.2027  0.0489  4   TYR C CE1   
3883 C  CE2   . TYR D 5   ? 0.4547 0.6414 0.6329 -0.1318 0.2320  0.0302  4   TYR C CE2   
3884 C  CZ    . TYR D 5   ? 0.4841 0.6844 0.6692 -0.1440 0.2235  0.0406  4   TYR C CZ    
3885 O  OH    . TYR D 5   ? 0.5111 0.7372 0.7128 -0.1457 0.2306  0.0433  4   TYR C OH    
3886 N  N     . LYS D 6   ? 0.5092 0.5983 0.6223 -0.1179 0.1810  0.0180  5   LYS C N     
3887 C  CA    . LYS D 6   ? 0.4264 0.4969 0.5190 -0.1219 0.1722  0.0143  5   LYS C CA    
3888 C  C     . LYS D 6   ? 0.4942 0.5534 0.5507 -0.1370 0.1757  0.0103  5   LYS C C     
3889 O  O     . LYS D 6   ? 0.5531 0.5996 0.5911 -0.1390 0.1920  0.0008  5   LYS C O     
3890 C  CB    . LYS D 6   ? 0.5091 0.5650 0.6063 -0.1103 0.1788  0.0064  5   LYS C CB    
3891 C  CG    . LYS D 6   ? 0.5450 0.6147 0.6779 -0.0949 0.1769  0.0113  5   LYS C CG    
3892 C  CD    . LYS D 6   ? 0.5529 0.6063 0.6907 -0.0823 0.1788  0.0065  5   LYS C CD    
3893 C  CE    . LYS D 6   ? 0.6504 0.6976 0.7895 -0.0712 0.1985  -0.0012 5   LYS C CE    
3894 N  NZ    . LYS D 6   ? 0.7233 0.7442 0.8250 -0.0798 0.2106  -0.0122 5   LYS C NZ    
3895 N  N     . LEU D 7   ? 0.4590 0.5221 0.5046 -0.1471 0.1602  0.0178  6   LEU C N     
3896 C  CA    . LEU D 7   ? 0.4694 0.5250 0.4810 -0.1626 0.1571  0.0173  6   LEU C CA    
3897 C  C     . LEU D 7   ? 0.4834 0.5313 0.4817 -0.1682 0.1451  0.0147  6   LEU C C     
3898 O  O     . LEU D 7   ? 0.4660 0.5200 0.4837 -0.1615 0.1340  0.0183  6   LEU C O     
3899 C  CB    . LEU D 7   ? 0.4474 0.5140 0.4571 -0.1687 0.1456  0.0294  6   LEU C CB    
3900 C  CG    . LEU D 7   ? 0.4916 0.5702 0.5200 -0.1651 0.1495  0.0367  6   LEU C CG    
3901 C  CD1   . LEU D 7   ? 0.4771 0.5558 0.4875 -0.1753 0.1393  0.0473  6   LEU C CD1   
3902 C  CD2   . LEU D 7   ? 0.5340 0.6146 0.5652 -0.1639 0.1712  0.0296  6   LEU C CD2   
3903 N  N     . VAL D 8   ? 0.4837 0.5198 0.4476 -0.1826 0.1469  0.0092  7   VAL C N     
3904 C  CA    . VAL D 8   ? 0.4977 0.5291 0.4461 -0.1922 0.1359  0.0062  7   VAL C CA    
3905 C  C     . VAL D 8   ? 0.5369 0.5729 0.4579 -0.2084 0.1243  0.0113  7   VAL C C     
3906 O  O     . VAL D 8   ? 0.5794 0.6050 0.4722 -0.2183 0.1334  0.0080  7   VAL C O     
3907 C  CB    . VAL D 8   ? 0.5530 0.5599 0.4818 -0.1958 0.1499  -0.0081 7   VAL C CB    
3908 C  CG1   . VAL D 8   ? 0.5096 0.5126 0.4213 -0.2096 0.1379  -0.0112 7   VAL C CG1   
3909 C  CG2   . VAL D 8   ? 0.5428 0.5428 0.4961 -0.1783 0.1612  -0.0123 7   VAL C CG2   
3910 N  N     . VAL D 9   ? 0.4787 0.5309 0.4072 -0.2109 0.1046  0.0194  8   VAL C N     
3911 C  CA    . VAL D 9   ? 0.4966 0.5578 0.4035 -0.2239 0.0896  0.0266  8   VAL C CA    
3912 C  C     . VAL D 9   ? 0.5179 0.5766 0.4039 -0.2395 0.0839  0.0194  8   VAL C C     
3913 O  O     . VAL D 9   ? 0.5133 0.5779 0.4160 -0.2370 0.0799  0.0166  8   VAL C O     
3914 C  CB    . VAL D 9   ? 0.4767 0.5600 0.4080 -0.2144 0.0710  0.0414  8   VAL C CB    
3915 C  CG1   . VAL D 9   ? 0.4991 0.5923 0.4098 -0.2249 0.0545  0.0507  8   VAL C CG1   
3916 C  CG2   . VAL D 9   ? 0.4490 0.5322 0.4022 -0.1999 0.0763  0.0479  8   VAL C CG2   
3917 N  N     . VAL D 10  ? 0.5556 0.6062 0.4034 -0.2575 0.0825  0.0171  9   VAL C N     
3918 C  CA    . VAL D 10  ? 0.6355 0.6816 0.4560 -0.2773 0.0771  0.0096  9   VAL C CA    
3919 C  C     . VAL D 10  ? 0.6324 0.6916 0.4283 -0.2929 0.0590  0.0184  9   VAL C C     
3920 O  O     . VAL D 10  ? 0.6154 0.6762 0.4030 -0.2908 0.0559  0.0275  9   VAL C O     
3921 C  CB    . VAL D 10  ? 0.7019 0.7132 0.4884 -0.2873 0.0985  -0.0069 9   VAL C CB    
3922 C  CG1   . VAL D 10  ? 0.6027 0.5995 0.4120 -0.2705 0.1159  -0.0150 9   VAL C CG1   
3923 C  CG2   . VAL D 10  ? 0.6493 0.6474 0.4084 -0.2920 0.1085  -0.0070 9   VAL C CG2   
3924 N  N     . GLY D 11  ? 0.6753 0.7439 0.4580 -0.3098 0.0465  0.0160  10  GLY C N     
3925 C  CA    . GLY D 11  ? 0.6924 0.7768 0.4517 -0.3265 0.0265  0.0242  10  GLY C CA    
3926 C  C     . GLY D 11  ? 0.6829 0.7949 0.4538 -0.3372 0.0087  0.0256  10  GLY C C     
3927 O  O     . GLY D 11  ? 0.6732 0.7961 0.4754 -0.3288 0.0099  0.0230  10  GLY C O     
3928 N  N     . ALA D 12  ? 0.6776 0.8024 0.4220 -0.3572 -0.0086 0.0300  11  ALA C N     
3929 C  CA    . ALA D 12  ? 0.6734 0.8330 0.4324 -0.3684 -0.0280 0.0333  11  ALA C CA    
3930 C  C     . ALA D 12  ? 0.6283 0.8279 0.4392 -0.3456 -0.0427 0.0483  11  ALA C C     
3931 O  O     . ALA D 12  ? 0.6378 0.8377 0.4653 -0.3244 -0.0428 0.0586  11  ALA C O     
3932 C  CB    . ALA D 12  ? 0.7175 0.8878 0.4395 -0.3941 -0.0467 0.0374  11  ALA C CB    
3933 N  N     . ASP D 13  ? 0.6147 0.8472 0.4502 -0.3507 -0.0543 0.0493  12  ASP C N     
3934 C  CA    . ASP D 13  ? 0.6040 0.8721 0.4898 -0.3273 -0.0642 0.0613  12  ASP C CA    
3935 C  C     . ASP D 13  ? 0.5863 0.8867 0.4794 -0.3206 -0.0881 0.0798  12  ASP C C     
3936 O  O     . ASP D 13  ? 0.6136 0.9230 0.4783 -0.3396 -0.1030 0.0838  12  ASP C O     
3937 C  CB    . ASP D 13  ? 0.6398 0.9332 0.5542 -0.3324 -0.0650 0.0557  12  ASP C CB    
3938 C  CG    . ASP D 13  ? 0.5617 0.8216 0.4806 -0.3268 -0.0409 0.0415  12  ASP C CG    
3939 O  OD1   . ASP D 13  ? 0.5168 0.7556 0.4458 -0.3058 -0.0288 0.0424  12  ASP C OD1   
3940 O  OD2   . ASP D 13  ? 0.6037 0.8572 0.5152 -0.3435 -0.0343 0.0300  12  ASP C OD2   
3941 N  N     . GLY D 14  ? 0.5467 0.8617 0.4763 -0.2928 -0.0918 0.0916  13  GLY C N     
3942 C  CA    . GLY D 14  ? 0.5514 0.8931 0.4914 -0.2803 -0.1132 0.1103  13  GLY C CA    
3943 C  C     . GLY D 14  ? 0.5699 0.8814 0.4830 -0.2728 -0.1123 0.1185  13  GLY C C     
3944 O  O     . GLY D 14  ? 0.5754 0.9018 0.4959 -0.2588 -0.1290 0.1352  13  GLY C O     
3945 N  N     . VAL D 15  ? 0.5811 0.8503 0.4641 -0.2806 -0.0925 0.1075  14  VAL C N     
3946 C  CA    . VAL D 15  ? 0.6053 0.8463 0.4573 -0.2790 -0.0906 0.1143  14  VAL C CA    
3947 C  C     . VAL D 15  ? 0.6081 0.8391 0.4845 -0.2523 -0.0848 0.1226  14  VAL C C     
3948 O  O     . VAL D 15  ? 0.5972 0.8149 0.4570 -0.2463 -0.0903 0.1345  14  VAL C O     
3949 C  CB    . VAL D 15  ? 0.6453 0.8478 0.4564 -0.2979 -0.0700 0.0988  14  VAL C CB    
3950 C  CG1   . VAL D 15  ? 0.6616 0.8700 0.4446 -0.3259 -0.0758 0.0897  14  VAL C CG1   
3951 C  CG2   . VAL D 15  ? 0.5999 0.7811 0.4301 -0.2869 -0.0447 0.0858  14  VAL C CG2   
3952 N  N     . GLY D 16  ? 0.5403 0.7749 0.4529 -0.2376 -0.0738 0.1167  15  GLY C N     
3953 C  CA    . GLY D 16  ? 0.5183 0.7431 0.4525 -0.2140 -0.0693 0.1242  15  GLY C CA    
3954 C  C     . GLY D 16  ? 0.5285 0.7247 0.4658 -0.2101 -0.0459 0.1130  15  GLY C C     
3955 O  O     . GLY D 16  ? 0.4895 0.6721 0.4362 -0.1951 -0.0414 0.1190  15  GLY C O     
3956 N  N     . LYS D 17  ? 0.5962 0.7827 0.5253 -0.2234 -0.0314 0.0973  16  LYS C N     
3957 C  CA    . LYS D 17  ? 0.5618 0.7255 0.4986 -0.2178 -0.0099 0.0867  16  LYS C CA    
3958 C  C     . LYS D 17  ? 0.4728 0.6430 0.4475 -0.1970 -0.0086 0.0901  16  LYS C C     
3959 O  O     . LYS D 17  ? 0.4700 0.6237 0.4510 -0.1871 0.0014  0.0910  16  LYS C O     
3960 C  CB    . LYS D 17  ? 0.5553 0.7114 0.4834 -0.2313 0.0022  0.0705  16  LYS C CB    
3961 C  CG    . LYS D 17  ? 0.6025 0.7452 0.4890 -0.2518 0.0042  0.0654  16  LYS C CG    
3962 C  CD    . LYS D 17  ? 0.6270 0.7485 0.4977 -0.2629 0.0221  0.0484  16  LYS C CD    
3963 C  CE    . LYS D 17  ? 0.6302 0.7566 0.5270 -0.2571 0.0266  0.0412  16  LYS C CE    
3964 N  NZ    . LYS D 17  ? 0.6887 0.8046 0.5588 -0.2782 0.0305  0.0284  16  LYS C NZ    
3965 N  N     . SER D 18  ? 0.4272 0.6212 0.4268 -0.1919 -0.0170 0.0908  17  SER C N     
3966 C  CA    . SER D 18  ? 0.4161 0.6137 0.4482 -0.1726 -0.0149 0.0936  17  SER C CA    
3967 C  C     . SER D 18  ? 0.4200 0.6169 0.4570 -0.1572 -0.0245 0.1084  17  SER C C     
3968 O  O     . SER D 18  ? 0.4073 0.5898 0.4560 -0.1442 -0.0180 0.1104  17  SER C O     
3969 C  CB    . SER D 18  ? 0.3794 0.6031 0.4364 -0.1712 -0.0198 0.0905  17  SER C CB    
3970 O  OG    . SER D 18  ? 0.3853 0.6043 0.4307 -0.1881 -0.0115 0.0773  17  SER C OG    
3971 N  N     . ALA D 19  ? 0.4257 0.6347 0.4503 -0.1592 -0.0403 0.1193  18  ALA C N     
3972 C  CA    . ALA D 19  ? 0.4297 0.6321 0.4549 -0.1438 -0.0491 0.1339  18  ALA C CA    
3973 C  C     . ALA D 19  ? 0.4580 0.6270 0.4601 -0.1467 -0.0389 0.1350  18  ALA C C     
3974 O  O     . ALA D 19  ? 0.4574 0.6117 0.4639 -0.1334 -0.0391 0.1431  18  ALA C O     
3975 C  CB    . ALA D 19  ? 0.4627 0.6862 0.4797 -0.1439 -0.0700 0.1468  18  ALA C CB    
3976 N  N     . LEU D 20  ? 0.4563 0.6127 0.4338 -0.1645 -0.0285 0.1262  19  LEU C N     
3977 C  CA    . LEU D 20  ? 0.4703 0.5996 0.4290 -0.1692 -0.0155 0.1252  19  LEU C CA    
3978 C  C     . LEU D 20  ? 0.4675 0.5880 0.4487 -0.1618 0.0002  0.1168  19  LEU C C     
3979 O  O     . LEU D 20  ? 0.4753 0.5805 0.4587 -0.1555 0.0049  0.1216  19  LEU C O     
3980 C  CB    . LEU D 20  ? 0.5215 0.6424 0.4482 -0.1895 -0.0074 0.1171  19  LEU C CB    
3981 C  CG    . LEU D 20  ? 0.5325 0.6499 0.4235 -0.2011 -0.0194 0.1265  19  LEU C CG    
3982 C  CD1   . LEU D 20  ? 0.6088 0.7143 0.4680 -0.2218 -0.0065 0.1146  19  LEU C CD1   
3983 C  CD2   . LEU D 20  ? 0.5495 0.6482 0.4276 -0.1949 -0.0224 0.1401  19  LEU C CD2   
3984 N  N     . THR D 21  ? 0.4506 0.5797 0.4466 -0.1639 0.0080  0.1045  20  THR C N     
3985 C  CA    . THR D 21  ? 0.3930 0.5156 0.4112 -0.1561 0.0206  0.0972  20  THR C CA    
3986 C  C     . THR D 21  ? 0.3906 0.5146 0.4310 -0.1397 0.0139  0.1053  20  THR C C     
3987 O  O     . THR D 21  ? 0.3780 0.4886 0.4248 -0.1345 0.0208  0.1063  20  THR C O     
3988 C  CB    . THR D 21  ? 0.3997 0.5299 0.4273 -0.1604 0.0268  0.0845  20  THR C CB    
3989 O  OG1   . THR D 21  ? 0.4003 0.5209 0.4043 -0.1748 0.0371  0.0752  20  THR C OG1   
3990 C  CG2   . THR D 21  ? 0.3674 0.4923 0.4199 -0.1499 0.0363  0.0791  20  THR C CG2   
3991 N  N     . ILE D 22  ? 0.3959 0.5365 0.4479 -0.1316 0.0008  0.1110  21  ILE C N     
3992 C  CA    . ILE D 22  ? 0.4151 0.5550 0.4865 -0.1145 -0.0042 0.1180  21  ILE C CA    
3993 C  C     . ILE D 22  ? 0.4375 0.5580 0.4946 -0.1088 -0.0086 0.1300  21  ILE C C     
3994 O  O     . ILE D 22  ? 0.4697 0.5767 0.5355 -0.0977 -0.0072 0.1335  21  ILE C O     
3995 C  CB    . ILE D 22  ? 0.3911 0.5572 0.4803 -0.1065 -0.0153 0.1206  21  ILE C CB    
3996 C  CG1   . ILE D 22  ? 0.3801 0.5611 0.4805 -0.1153 -0.0091 0.1081  21  ILE C CG1   
3997 C  CG2   . ILE D 22  ? 0.4084 0.5726 0.5159 -0.0868 -0.0192 0.1277  21  ILE C CG2   
3998 C  CD1   . ILE D 22  ? 0.4204 0.6298 0.5433 -0.1087 -0.0169 0.1091  21  ILE C CD1   
3999 N  N     . GLN D 23  ? 0.4233 0.5393 0.4552 -0.1172 -0.0143 0.1365  22  GLN C N     
4000 C  CA    . GLN D 23  ? 0.5312 0.6236 0.5437 -0.1150 -0.0170 0.1477  22  GLN C CA    
4001 C  C     . GLN D 23  ? 0.4597 0.5326 0.4672 -0.1229 -0.0018 0.1424  22  GLN C C     
4002 O  O     . GLN D 23  ? 0.5882 0.6421 0.5952 -0.1172 -0.0004 0.1478  22  GLN C O     
4003 C  CB    . GLN D 23  ? 0.5625 0.6544 0.5458 -0.1240 -0.0269 0.1561  22  GLN C CB    
4004 C  CG    . GLN D 23  ? 0.6293 0.6980 0.5918 -0.1180 -0.0353 0.1714  22  GLN C CG    
4005 C  CD    . GLN D 23  ? 0.6723 0.7431 0.6511 -0.0959 -0.0473 0.1812  22  GLN C CD    
4006 O  OE1   . GLN D 23  ? 0.6666 0.7215 0.6563 -0.0851 -0.0422 0.1814  22  GLN C OE1   
4007 N  NE2   . GLN D 23  ? 0.6916 0.7812 0.6703 -0.0892 -0.0633 0.1898  22  GLN C NE2   
4008 N  N     . LEU D 24  ? 0.4804 0.5584 0.4855 -0.1357 0.0101  0.1314  23  LEU C N     
4009 C  CA    . LEU D 24  ? 0.4140 0.4812 0.4217 -0.1416 0.0251  0.1257  23  LEU C CA    
4010 C  C     . LEU D 24  ? 0.4503 0.5167 0.4844 -0.1308 0.0278  0.1228  23  LEU C C     
4011 O  O     . LEU D 24  ? 0.4469 0.4995 0.4816 -0.1311 0.0319  0.1259  23  LEU C O     
4012 C  CB    . LEU D 24  ? 0.4102 0.4854 0.4157 -0.1526 0.0380  0.1134  23  LEU C CB    
4013 C  CG    . LEU D 24  ? 0.4607 0.5303 0.4741 -0.1563 0.0533  0.1084  23  LEU C CG    
4014 C  CD1   . LEU D 24  ? 0.4320 0.4887 0.4207 -0.1675 0.0576  0.1150  23  LEU C CD1   
4015 C  CD2   . LEU D 24  ? 0.4185 0.4974 0.4411 -0.1593 0.0662  0.0948  23  LEU C CD2   
4016 N  N     . ILE D 25  ? 0.4276 0.5082 0.4818 -0.1230 0.0254  0.1169  24  ILE C N     
4017 C  CA    . ILE D 25  ? 0.4439 0.5233 0.5207 -0.1143 0.0287  0.1129  24  ILE C CA    
4018 C  C     . ILE D 25  ? 0.4181 0.4869 0.4980 -0.1020 0.0200  0.1216  24  ILE C C     
4019 O  O     . ILE D 25  ? 0.4588 0.5130 0.5426 -0.0994 0.0231  0.1227  24  ILE C O     
4020 C  CB    . ILE D 25  ? 0.3991 0.4944 0.4923 -0.1123 0.0308  0.1031  24  ILE C CB    
4021 C  CG1   . ILE D 25  ? 0.3709 0.4703 0.4583 -0.1233 0.0410  0.0936  24  ILE C CG1   
4022 C  CG2   . ILE D 25  ? 0.3990 0.4907 0.5122 -0.1036 0.0334  0.0999  24  ILE C CG2   
4023 C  CD1   . ILE D 25  ? 0.3204 0.4117 0.4107 -0.1268 0.0528  0.0905  24  ILE C CD1   
4024 N  N     . GLN D 26  ? 0.4671 0.5431 0.5459 -0.0937 0.0094  0.1277  25  GLN C N     
4025 C  CA    . GLN D 26  ? 0.5459 0.6130 0.6318 -0.0783 0.0035  0.1339  25  GLN C CA    
4026 C  C     . GLN D 26  ? 0.6492 0.7012 0.7163 -0.0721 -0.0060 0.1471  25  GLN C C     
4027 O  O     . GLN D 26  ? 0.6515 0.6925 0.7218 -0.0573 -0.0105 0.1529  25  GLN C O     
4028 C  CB    . GLN D 26  ? 0.5776 0.6669 0.6850 -0.0683 0.0002  0.1300  25  GLN C CB    
4029 C  CG    . GLN D 26  ? 0.4745 0.5714 0.5984 -0.0722 0.0093  0.1181  25  GLN C CG    
4030 C  CD    . GLN D 26  ? 0.5632 0.6819 0.7055 -0.0656 0.0072  0.1141  25  GLN C CD    
4031 O  OE1   . GLN D 26  ? 0.5595 0.6906 0.7072 -0.0556 -0.0009 0.1205  25  GLN C OE1   
4032 N  NE2   . GLN D 26  ? 0.5394 0.6637 0.6922 -0.0709 0.0147  0.1039  25  GLN C NE2   
4033 N  N     . ASN D 27  ? 0.7418 0.7901 0.7871 -0.0825 -0.0087 0.1522  26  ASN C N     
4034 C  CA    . ASN D 27  ? 0.8101 0.8395 0.8322 -0.0781 -0.0181 0.1661  26  ASN C CA    
4035 C  C     . ASN D 27  ? 0.8615 0.9045 0.8924 -0.0606 -0.0314 0.1739  26  ASN C C     
4036 O  O     . ASN D 27  ? 0.9397 0.9655 0.9542 -0.0511 -0.0407 0.1867  26  ASN C O     
4037 C  CB    . ASN D 27  ? 0.8282 0.8225 0.8377 -0.0767 -0.0140 0.1708  26  ASN C CB    
4038 C  CG    . ASN D 27  ? 0.8876 0.8577 0.8637 -0.0885 -0.0149 0.1799  26  ASN C CG    
4039 O  OD1   . ASN D 27  ? 0.8996 0.8670 0.8573 -0.0862 -0.0252 0.1900  26  ASN C OD1   
4040 N  ND2   . ASN D 27  ? 0.8810 0.8350 0.8492 -0.1023 -0.0043 0.1768  26  ASN C ND2   
4041 N  N     . HIS D 28  ? 0.6907 0.7647 0.7472 -0.0561 -0.0322 0.1667  27  HIS C N     
4042 C  CA    . HIS D 28  ? 0.6962 0.7938 0.7684 -0.0406 -0.0436 0.1726  27  HIS C CA    
4043 C  C     . HIS D 28  ? 0.5912 0.7187 0.6607 -0.0510 -0.0528 0.1733  27  HIS C C     
4044 O  O     . HIS D 28  ? 0.5601 0.6944 0.6237 -0.0692 -0.0466 0.1640  27  HIS C O     
4045 C  CB    . HIS D 28  ? 0.6381 0.7508 0.7404 -0.0307 -0.0372 0.1638  27  HIS C CB    
4046 C  CG    . HIS D 28  ? 0.6535 0.8021 0.7786 -0.0191 -0.0460 0.1664  27  HIS C CG    
4047 N  ND1   . HIS D 28  ? 0.6015 0.7845 0.7437 -0.0291 -0.0453 0.1576  27  HIS C ND1   
4048 C  CD2   . HIS D 28  ? 0.6736 0.8306 0.8079 0.0014  -0.0556 0.1771  27  HIS C CD2   
4049 C  CE1   . HIS D 28  ? 0.6657 0.8804 0.8287 -0.0168 -0.0542 0.1626  27  HIS C CE1   
4050 N  NE2   . HIS D 28  ? 0.6799 0.8813 0.8401 0.0031  -0.0606 0.1746  27  HIS C NE2   
4051 N  N     . PHE D 29  ? 0.5766 0.7210 0.6490 -0.0394 -0.0678 0.1847  28  PHE C N     
4052 C  CA    . PHE D 29  ? 0.5607 0.7361 0.6304 -0.0499 -0.0792 0.1864  28  PHE C CA    
4053 C  C     . PHE D 29  ? 0.5500 0.7683 0.6538 -0.0421 -0.0844 0.1835  28  PHE C C     
4054 O  O     . PHE D 29  ? 0.4630 0.6916 0.5868 -0.0204 -0.0899 0.1908  28  PHE C O     
4055 C  CB    . PHE D 29  ? 0.5476 0.7154 0.5927 -0.0463 -0.0954 0.2029  28  PHE C CB    
4056 C  CG    . PHE D 29  ? 0.5491 0.7510 0.5912 -0.0571 -0.1096 0.2058  28  PHE C CG    
4057 C  CD1   . PHE D 29  ? 0.5769 0.7800 0.5990 -0.0828 -0.1051 0.1966  28  PHE C CD1   
4058 C  CD2   . PHE D 29  ? 0.5476 0.7797 0.6051 -0.0419 -0.1279 0.2182  28  PHE C CD2   
4059 C  CE1   . PHE D 29  ? 0.5399 0.7707 0.5536 -0.0959 -0.1186 0.1989  28  PHE C CE1   
4060 C  CE2   . PHE D 29  ? 0.5403 0.8058 0.5935 -0.0545 -0.1432 0.2217  28  PHE C CE2   
4061 C  CZ    . PHE D 29  ? 0.5580 0.8212 0.5872 -0.0829 -0.1388 0.2117  28  PHE C CZ    
4062 N  N     . VAL D 30  ? 0.5329 0.7747 0.6417 -0.0604 -0.0817 0.1726  29  VAL C N     
4063 C  CA    . VAL D 30  ? 0.5052 0.7908 0.6430 -0.0600 -0.0866 0.1689  29  VAL C CA    
4064 C  C     . VAL D 30  ? 0.4787 0.7942 0.6108 -0.0646 -0.1064 0.1794  29  VAL C C     
4065 O  O     . VAL D 30  ? 0.4555 0.7701 0.5626 -0.0857 -0.1104 0.1772  29  VAL C O     
4066 C  CB    . VAL D 30  ? 0.5202 0.8108 0.6625 -0.0787 -0.0734 0.1518  29  VAL C CB    
4067 C  CG1   . VAL D 30  ? 0.5076 0.7853 0.6182 -0.1035 -0.0711 0.1455  29  VAL C CG1   
4068 C  CG2   . VAL D 30  ? 0.4800 0.8137 0.6518 -0.0798 -0.0768 0.1477  29  VAL C CG2   
4069 N  N     . ASP D 31  ? 0.4811 0.8223 0.6351 -0.0441 -0.1192 0.1914  30  ASP C N     
4070 C  CA    . ASP D 31  ? 0.4651 0.8437 0.6203 -0.0477 -0.1402 0.2020  30  ASP C CA    
4071 C  C     . ASP D 31  ? 0.4622 0.8915 0.6441 -0.0607 -0.1431 0.1940  30  ASP C C     
4072 O  O     . ASP D 31  ? 0.4477 0.9086 0.6256 -0.0730 -0.1598 0.1996  30  ASP C O     
4073 C  CB    . ASP D 31  ? 0.5216 0.9074 0.6874 -0.0189 -0.1551 0.2209  30  ASP C CB    
4074 C  CG    . ASP D 31  ? 0.5004 0.8834 0.6968 0.0094  -0.1450 0.2209  30  ASP C CG    
4075 O  OD1   . ASP D 31  ? 0.5109 0.8806 0.7173 0.0076  -0.1265 0.2074  30  ASP C OD1   
4076 O  OD2   . ASP D 31  ? 0.6109 1.0071 0.8218 0.0347  -0.1567 0.2353  30  ASP C OD2   
4077 N  N     . GLU D 32  ? 0.4207 0.8567 0.6259 -0.0613 -0.1276 0.1811  31  GLU C N     
4078 C  CA    . GLU D 32  ? 0.3958 0.8765 0.6240 -0.0762 -0.1284 0.1727  31  GLU C CA    
4079 C  C     . GLU D 32  ? 0.4031 0.8661 0.6046 -0.1073 -0.1192 0.1578  31  GLU C C     
4080 O  O     . GLU D 32  ? 0.3914 0.8100 0.5706 -0.1116 -0.1049 0.1500  31  GLU C O     
4081 C  CB    . GLU D 32  ? 0.3601 0.8559 0.6255 -0.0601 -0.1159 0.1673  31  GLU C CB    
4082 C  CG    . GLU D 32  ? 0.3658 0.8862 0.6615 -0.0283 -0.1242 0.1812  31  GLU C CG    
4083 C  CD    . GLU D 32  ? 0.4126 0.9371 0.7384 -0.0116 -0.1079 0.1744  31  GLU C CD    
4084 O  OE1   . GLU D 32  ? 0.4145 0.9127 0.7324 -0.0226 -0.0907 0.1606  31  GLU C OE1   
4085 O  OE2   . GLU D 32  ? 0.4292 0.9821 0.7853 0.0131  -0.1120 0.1831  31  GLU C OE2   
4086 N  N     . TYR D 33  ? 0.3894 0.8873 0.5927 -0.1291 -0.1276 0.1541  32  TYR C N     
4087 C  CA    . TYR D 33  ? 0.3950 0.8750 0.5695 -0.1593 -0.1196 0.1400  32  TYR C CA    
4088 C  C     . TYR D 33  ? 0.3706 0.8507 0.5613 -0.1663 -0.1023 0.1251  32  TYR C C     
4089 O  O     . TYR D 33  ? 0.3617 0.8837 0.5803 -0.1706 -0.1056 0.1236  32  TYR C O     
4090 C  CB    . TYR D 33  ? 0.4206 0.9319 0.5816 -0.1825 -0.1377 0.1431  32  TYR C CB    
4091 C  CG    . TYR D 33  ? 0.4337 0.9243 0.5611 -0.2147 -0.1295 0.1280  32  TYR C CG    
4092 C  CD1   . TYR D 33  ? 0.4635 0.9006 0.5600 -0.2193 -0.1119 0.1180  32  TYR C CD1   
4093 C  CD2   . TYR D 33  ? 0.4465 0.9707 0.5729 -0.2404 -0.1386 0.1235  32  TYR C CD2   
4094 C  CE1   . TYR D 33  ? 0.4523 0.8669 0.5169 -0.2461 -0.1028 0.1040  32  TYR C CE1   
4095 C  CE2   . TYR D 33  ? 0.4648 0.9639 0.5558 -0.2699 -0.1302 0.1093  32  TYR C CE2   
4096 C  CZ    . TYR D 33  ? 0.4862 0.9288 0.5461 -0.2712 -0.1117 0.0994  32  TYR C CZ    
4097 O  OH    . TYR D 33  ? 0.5462 0.9602 0.5697 -0.2979 -0.1017 0.0849  32  TYR C OH    
4098 N  N     . ASP D 34  ? 0.4049 0.8387 0.5770 -0.1687 -0.0843 0.1145  33  ASP C N     
4099 C  CA    . ASP D 34  ? 0.3649 0.7874 0.5457 -0.1738 -0.0670 0.1010  33  ASP C CA    
4100 C  C     . ASP D 34  ? 0.3754 0.7621 0.5206 -0.1961 -0.0564 0.0882  33  ASP C C     
4101 O  O     . ASP D 34  ? 0.3833 0.7301 0.5137 -0.1903 -0.0440 0.0840  33  ASP C O     
4102 C  CB    . ASP D 34  ? 0.4005 0.8007 0.5968 -0.1495 -0.0554 0.1019  33  ASP C CB    
4103 C  CG    . ASP D 34  ? 0.4050 0.7976 0.6129 -0.1523 -0.0398 0.0902  33  ASP C CG    
4104 O  OD1   . ASP D 34  ? 0.3376 0.7545 0.5535 -0.1681 -0.0394 0.0839  33  ASP C OD1   
4105 O  OD2   . ASP D 34  ? 0.4302 0.7913 0.6372 -0.1400 -0.0284 0.0877  33  ASP C OD2   
4106 N  N     . PRO D 35  ? 0.3807 0.7806 0.5119 -0.2218 -0.0602 0.0815  34  PRO C N     
4107 C  CA    . PRO D 35  ? 0.3950 0.7572 0.4870 -0.2426 -0.0502 0.0695  34  PRO C CA    
4108 C  C     . PRO D 35  ? 0.3813 0.7071 0.4714 -0.2387 -0.0298 0.0580  34  PRO C C     
4109 O  O     . PRO D 35  ? 0.3761 0.7121 0.4896 -0.2336 -0.0243 0.0552  34  PRO C O     
4110 C  CB    . PRO D 35  ? 0.4170 0.8039 0.4985 -0.2710 -0.0588 0.0646  34  PRO C CB    
4111 C  CG    . PRO D 35  ? 0.4038 0.8468 0.5235 -0.2653 -0.0732 0.0741  34  PRO C CG    
4112 C  CD    . PRO D 35  ? 0.3779 0.8291 0.5288 -0.2327 -0.0740 0.0851  34  PRO C CD    
4113 N  N     . THR D 36  ? 0.3931 0.6774 0.4549 -0.2409 -0.0184 0.0517  35  THR C N     
4114 C  CA    . THR D 36  ? 0.3796 0.6293 0.4421 -0.2308 -0.0007 0.0442  35  THR C CA    
4115 C  C     . THR D 36  ? 0.3914 0.6207 0.4391 -0.2467 0.0111  0.0306  35  THR C C     
4116 O  O     . THR D 36  ? 0.4208 0.6406 0.4399 -0.2679 0.0115  0.0234  35  THR C O     
4117 C  CB    . THR D 36  ? 0.3883 0.6068 0.4304 -0.2246 0.0065  0.0444  35  THR C CB    
4118 O  OG1   . THR D 36  ? 0.3795 0.6117 0.4336 -0.2098 -0.0036 0.0575  35  THR C OG1   
4119 C  CG2   . THR D 36  ? 0.3739 0.5622 0.4210 -0.2129 0.0232  0.0380  35  THR C CG2   
4120 N  N     . ILE D 37  ? 0.3726 0.5905 0.4362 -0.2366 0.0211  0.0269  36  ILE C N     
4121 C  CA    . ILE D 37  ? 0.3870 0.5741 0.4326 -0.2476 0.0343  0.0147  36  ILE C CA    
4122 C  C     . ILE D 37  ? 0.3921 0.5399 0.4223 -0.2374 0.0472  0.0106  36  ILE C C     
4123 O  O     . ILE D 37  ? 0.4203 0.5420 0.4204 -0.2483 0.0547  0.0027  36  ILE C O     
4124 C  CB    . ILE D 37  ? 0.3693 0.5616 0.4362 -0.2430 0.0386  0.0132  36  ILE C CB    
4125 C  CG1   . ILE D 37  ? 0.3606 0.5991 0.4504 -0.2500 0.0272  0.0182  36  ILE C CG1   
4126 C  CG2   . ILE D 37  ? 0.3921 0.5475 0.4343 -0.2561 0.0515  0.0012  36  ILE C CG2   
4127 C  CD1   . ILE D 37  ? 0.3869 0.6401 0.4600 -0.2776 0.0215  0.0133  36  ILE C CD1   
4128 N  N     . GLU D 38  ? 0.3667 0.5112 0.4178 -0.2163 0.0502  0.0159  37  GLU C N     
4129 C  CA    . GLU D 38  ? 0.3678 0.4842 0.4114 -0.2050 0.0608  0.0140  37  GLU C CA    
4130 C  C     . GLU D 38  ? 0.3401 0.4634 0.4108 -0.1845 0.0591  0.0223  37  GLU C C     
4131 O  O     . GLU D 38  ? 0.3219 0.4513 0.4101 -0.1787 0.0582  0.0234  37  GLU C O     
4132 C  CB    . GLU D 38  ? 0.3846 0.4671 0.4120 -0.2085 0.0746  0.0032  37  GLU C CB    
4133 C  CG    . GLU D 38  ? 0.4597 0.5149 0.4725 -0.2021 0.0868  -0.0012 37  GLU C CG    
4134 C  CD    . GLU D 38  ? 0.5502 0.5782 0.5641 -0.1930 0.0980  -0.0066 37  GLU C CD    
4135 O  OE1   . GLU D 38  ? 0.6117 0.6113 0.5999 -0.2018 0.1076  -0.0162 37  GLU C OE1   
4136 O  OE2   . GLU D 38  ? 0.5736 0.6055 0.6109 -0.1773 0.0972  -0.0011 37  GLU C OE2   
4137 N  N     . ASP D 39  ? 0.3337 0.4550 0.4057 -0.1752 0.0591  0.0278  38  ASP C N     
4138 C  CA    . ASP D 39  ? 0.3099 0.4348 0.4041 -0.1582 0.0573  0.0354  38  ASP C CA    
4139 C  C     . ASP D 39  ? 0.3118 0.4192 0.4020 -0.1515 0.0661  0.0351  38  ASP C C     
4140 O  O     . ASP D 39  ? 0.3302 0.4304 0.4021 -0.1583 0.0707  0.0326  38  ASP C O     
4141 C  CB    . ASP D 39  ? 0.3018 0.4500 0.4069 -0.1533 0.0445  0.0462  38  ASP C CB    
4142 C  CG    . ASP D 39  ? 0.3850 0.5569 0.5034 -0.1555 0.0364  0.0477  38  ASP C CG    
4143 O  OD1   . ASP D 39  ? 0.3583 0.5309 0.4932 -0.1474 0.0386  0.0474  38  ASP C OD1   
4144 O  OD2   . ASP D 39  ? 0.3279 0.5188 0.4399 -0.1659 0.0280  0.0493  38  ASP C OD2   
4145 N  N     . SER D 40  ? 0.2943 0.3961 0.4016 -0.1389 0.0687  0.0376  39  SER C N     
4146 C  CA    . SER D 40  ? 0.2934 0.3851 0.4029 -0.1322 0.0760  0.0384  39  SER C CA    
4147 C  C     . SER D 40  ? 0.2776 0.3768 0.4022 -0.1232 0.0693  0.0480  39  SER C C     
4148 O  O     . SER D 40  ? 0.2648 0.3696 0.4013 -0.1177 0.0627  0.0517  39  SER C O     
4149 C  CB    . SER D 40  ? 0.3464 0.4227 0.4612 -0.1263 0.0853  0.0325  39  SER C CB    
4150 O  OG    . SER D 40  ? 0.4076 0.4705 0.5047 -0.1340 0.0929  0.0234  39  SER C OG    
4151 N  N     . TYR D 41  ? 0.2820 0.3795 0.4038 -0.1227 0.0722  0.0516  40  TYR C N     
4152 C  CA    . TYR D 41  ? 0.2740 0.3740 0.4044 -0.1169 0.0663  0.0607  40  TYR C CA    
4153 C  C     . TYR D 41  ? 0.2736 0.3688 0.4094 -0.1152 0.0745  0.0608  40  TYR C C     
4154 O  O     . TYR D 41  ? 0.2928 0.3859 0.4225 -0.1189 0.0846  0.0553  40  TYR C O     
4155 C  CB    . TYR D 41  ? 0.2861 0.3916 0.4039 -0.1209 0.0585  0.0682  40  TYR C CB    
4156 C  CG    . TYR D 41  ? 0.3049 0.4218 0.4201 -0.1225 0.0492  0.0693  40  TYR C CG    
4157 C  CD1   . TYR D 41  ? 0.3010 0.4245 0.4288 -0.1136 0.0406  0.0750  40  TYR C CD1   
4158 C  CD2   . TYR D 41  ? 0.3027 0.4247 0.4026 -0.1334 0.0492  0.0647  40  TYR C CD2   
4159 C  CE1   . TYR D 41  ? 0.3352 0.4757 0.4657 -0.1143 0.0324  0.0763  40  TYR C CE1   
4160 C  CE2   . TYR D 41  ? 0.3049 0.4423 0.4050 -0.1364 0.0396  0.0662  40  TYR C CE2   
4161 C  CZ    . TYR D 41  ? 0.3290 0.4782 0.4470 -0.1263 0.0313  0.0722  40  TYR C CZ    
4162 O  OH    . TYR D 41  ? 0.3125 0.4829 0.4350 -0.1287 0.0222  0.0740  40  TYR C OH    
4163 N  N     . ARG D 42  ? 0.2647 0.3587 0.4113 -0.1103 0.0704  0.0673  41  ARG C N     
4164 C  CA    . ARG D 42  ? 0.2786 0.3731 0.4323 -0.1110 0.0765  0.0688  41  ARG C CA    
4165 C  C     . ARG D 42  ? 0.2707 0.3620 0.4196 -0.1136 0.0707  0.0780  41  ARG C C     
4166 O  O     . ARG D 42  ? 0.2683 0.3537 0.4164 -0.1095 0.0617  0.0829  41  ARG C O     
4167 C  CB    . ARG D 42  ? 0.2945 0.3890 0.4668 -0.1045 0.0779  0.0670  41  ARG C CB    
4168 C  CG    . ARG D 42  ? 0.3332 0.4258 0.5097 -0.1003 0.0836  0.0591  41  ARG C CG    
4169 C  CD    . ARG D 42  ? 0.3145 0.4047 0.5058 -0.0934 0.0803  0.0599  41  ARG C CD    
4170 N  NE    . ARG D 42  ? 0.3530 0.4512 0.5580 -0.0930 0.0808  0.0642  41  ARG C NE    
4171 C  CZ    . ARG D 42  ? 0.3200 0.4261 0.5386 -0.0888 0.0874  0.0621  41  ARG C CZ    
4172 N  NH1   . ARG D 42  ? 0.2650 0.3670 0.4825 -0.0832 0.0950  0.0554  41  ARG C NH1   
4173 N  NH2   . ARG D 42  ? 0.3580 0.4763 0.5915 -0.0901 0.0861  0.0670  41  ARG C NH2   
4174 N  N     . LYS D 43  ? 0.2816 0.3751 0.4257 -0.1206 0.0767  0.0801  42  LYS C N     
4175 C  CA    . LYS D 43  ? 0.2932 0.3798 0.4283 -0.1257 0.0725  0.0890  42  LYS C CA    
4176 C  C     . LYS D 43  ? 0.2969 0.3911 0.4394 -0.1328 0.0818  0.0890  42  LYS C C     
4177 O  O     . LYS D 43  ? 0.3008 0.4048 0.4446 -0.1357 0.0928  0.0835  42  LYS C O     
4178 C  CB    . LYS D 43  ? 0.3130 0.3939 0.4245 -0.1310 0.0693  0.0936  42  LYS C CB    
4179 C  CG    . LYS D 43  ? 0.3406 0.4081 0.4384 -0.1350 0.0637  0.1038  42  LYS C CG    
4180 C  CD    . LYS D 43  ? 0.3830 0.4444 0.4552 -0.1399 0.0597  0.1092  42  LYS C CD    
4181 C  CE    . LYS D 43  ? 0.4827 0.5252 0.5358 -0.1441 0.0543  0.1205  42  LYS C CE    
4182 N  NZ    . LYS D 43  ? 0.4894 0.5193 0.5477 -0.1331 0.0445  0.1255  42  LYS C NZ    
4183 N  N     . GLN D 44  ? 0.2986 0.3886 0.4452 -0.1363 0.0781  0.0950  43  GLN C N     
4184 C  CA    . GLN D 44  ? 0.3056 0.4061 0.4584 -0.1463 0.0862  0.0965  43  GLN C CA    
4185 C  C     . GLN D 44  ? 0.3307 0.4190 0.4591 -0.1577 0.0862  0.1037  43  GLN C C     
4186 O  O     . GLN D 44  ? 0.3417 0.4100 0.4526 -0.1565 0.0765  0.1100  43  GLN C O     
4187 C  CB    . GLN D 44  ? 0.2999 0.4050 0.4711 -0.1470 0.0823  0.0984  43  GLN C CB    
4188 C  CG    . GLN D 44  ? 0.3054 0.3895 0.4643 -0.1502 0.0717  0.1055  43  GLN C CG    
4189 C  CD    . GLN D 44  ? 0.3040 0.3944 0.4769 -0.1576 0.0694  0.1077  43  GLN C CD    
4190 O  OE1   . GLN D 44  ? 0.3115 0.4156 0.4897 -0.1667 0.0754  0.1069  43  GLN C OE1   
4191 N  NE2   . GLN D 44  ? 0.3225 0.4031 0.4995 -0.1516 0.0607  0.1074  43  GLN C NE2   
4192 N  N     . VAL D 45  ? 0.3426 0.4421 0.4687 -0.1680 0.0980  0.1028  44  VAL C N     
4193 C  CA    . VAL D 45  ? 0.3709 0.4585 0.4702 -0.1809 0.1002  0.1092  44  VAL C CA    
4194 C  C     . VAL D 45  ? 0.3784 0.4833 0.4877 -0.1921 0.1134  0.1076  44  VAL C C     
4195 O  O     . VAL D 45  ? 0.3619 0.4896 0.4988 -0.1868 0.1209  0.1008  44  VAL C O     
4196 C  CB    . VAL D 45  ? 0.3926 0.4753 0.4702 -0.1806 0.1028  0.1069  44  VAL C CB    
4197 C  CG1   . VAL D 45  ? 0.3753 0.4473 0.4480 -0.1684 0.0895  0.1076  44  VAL C CG1   
4198 C  CG2   . VAL D 45  ? 0.3768 0.4794 0.4668 -0.1790 0.1178  0.0961  44  VAL C CG2   
4199 N  N     . VAL D 46  ? 0.4069 0.4988 0.4933 -0.2032 0.1153  0.1126  45  VAL C N     
4200 C  CA    . VAL D 46  ? 0.4196 0.5266 0.5130 -0.2105 0.1278  0.1096  45  VAL C CA    
4201 C  C     . VAL D 46  ? 0.4721 0.5740 0.5392 -0.2172 0.1371  0.1090  45  VAL C C     
4202 O  O     . VAL D 46  ? 0.5385 0.6158 0.5725 -0.2232 0.1302  0.1158  45  VAL C O     
4203 C  CB    . VAL D 46  ? 0.4468 0.5429 0.5344 -0.2202 0.1230  0.1155  45  VAL C CB    
4204 C  CG1   . VAL D 46  ? 0.4490 0.5666 0.5486 -0.2283 0.1361  0.1127  45  VAL C CG1   
4205 C  CG2   . VAL D 46  ? 0.4622 0.5588 0.5696 -0.2149 0.1127  0.1155  45  VAL C CG2   
4206 N  N     . ILE D 47  ? 0.4427 0.5665 0.5228 -0.2156 0.1522  0.1011  46  ILE C N     
4207 C  CA    . ILE D 47  ? 0.4685 0.5876 0.5226 -0.2221 0.1630  0.0983  46  ILE C CA    
4208 C  C     . ILE D 47  ? 0.4831 0.6210 0.5477 -0.2280 0.1777  0.0959  46  ILE C C     
4209 O  O     . ILE D 47  ? 0.4660 0.6319 0.5648 -0.2206 0.1868  0.0906  46  ILE C O     
4210 C  CB    . ILE D 47  ? 0.4588 0.5828 0.5129 -0.2142 0.1693  0.0894  46  ILE C CB    
4211 C  CG1   . ILE D 47  ? 0.4640 0.5705 0.5044 -0.2113 0.1542  0.0930  46  ILE C CG1   
4212 C  CG2   . ILE D 47  ? 0.4956 0.6154 0.5226 -0.2220 0.1832  0.0845  46  ILE C CG2   
4213 C  CD1   . ILE D 47  ? 0.4542 0.5668 0.5034 -0.2015 0.1577  0.0833  46  ILE C CD1   
4214 N  N     . ASP D 48  ? 0.5165 0.6396 0.5522 -0.2414 0.1795  0.1008  47  ASP C N     
4215 C  CA    . ASP D 48  ? 0.5354 0.6755 0.5781 -0.2497 0.1935  0.0995  47  ASP C CA    
4216 C  C     . ASP D 48  ? 0.5152 0.6801 0.5980 -0.2469 0.1927  0.1004  47  ASP C C     
4217 O  O     . ASP D 48  ? 0.5117 0.7076 0.6225 -0.2447 0.2059  0.0963  47  ASP C O     
4218 C  CB    . ASP D 48  ? 0.5446 0.7004 0.5878 -0.2469 0.2123  0.0900  47  ASP C CB    
4219 C  CG    . ASP D 48  ? 0.5705 0.7001 0.5698 -0.2525 0.2128  0.0885  47  ASP C CG    
4220 O  OD1   . ASP D 48  ? 0.5908 0.6931 0.5570 -0.2620 0.2010  0.0967  47  ASP C OD1   
4221 O  OD2   . ASP D 48  ? 0.5728 0.7078 0.5696 -0.2473 0.2245  0.0792  47  ASP C OD2   
4222 N  N     . GLY D 49  ? 0.5036 0.6550 0.5889 -0.2467 0.1768  0.1060  48  GLY C N     
4223 C  CA    . GLY D 49  ? 0.4916 0.6604 0.6070 -0.2479 0.1735  0.1074  48  GLY C CA    
4224 C  C     . GLY D 49  ? 0.5039 0.6972 0.6594 -0.2334 0.1717  0.1029  48  GLY C C     
4225 O  O     . GLY D 49  ? 0.5070 0.7145 0.6870 -0.2348 0.1672  0.1037  48  GLY C O     
4226 N  N     . GLU D 50  ? 0.4369 0.6346 0.5980 -0.2207 0.1747  0.0978  49  GLU C N     
4227 C  CA    . GLU D 50  ? 0.4345 0.6558 0.6327 -0.2067 0.1745  0.0936  49  GLU C CA    
4228 C  C     . GLU D 50  ? 0.4296 0.6294 0.6189 -0.1992 0.1607  0.0936  49  GLU C C     
4229 O  O     . GLU D 50  ? 0.4180 0.5991 0.5820 -0.1980 0.1599  0.0926  49  GLU C O     
4230 C  CB    . GLU D 50  ? 0.4661 0.7132 0.6792 -0.1977 0.1917  0.0871  49  GLU C CB    
4231 C  CG    . GLU D 50  ? 0.4679 0.7384 0.7141 -0.1811 0.1918  0.0830  49  GLU C CG    
4232 C  CD    . GLU D 50  ? 0.5500 0.8017 0.7769 -0.1730 0.1927  0.0756  49  GLU C CD    
4233 O  OE1   . GLU D 50  ? 0.5350 0.7976 0.7772 -0.1595 0.2002  0.0671  49  GLU C OE1   
4234 O  OE2   . GLU D 50  ? 0.5752 0.7966 0.7697 -0.1802 0.1862  0.0775  49  GLU C OE2   
4235 N  N     . THR D 51  ? 0.3844 0.5860 0.5921 -0.1956 0.1496  0.0940  50  THR C N     
4236 C  CA    . THR D 51  ? 0.3904 0.5742 0.5912 -0.1881 0.1372  0.0938  50  THR C CA    
4237 C  C     . THR D 51  ? 0.4202 0.6180 0.6363 -0.1755 0.1443  0.0873  50  THR C C     
4238 O  O     . THR D 51  ? 0.4216 0.6459 0.6642 -0.1693 0.1544  0.0821  50  THR C O     
4239 C  CB    . THR D 51  ? 0.3415 0.5238 0.5537 -0.1882 0.1237  0.0950  50  THR C CB    
4240 O  OG1   . THR D 51  ? 0.4087 0.5741 0.6023 -0.2013 0.1186  0.1012  50  THR C OG1   
4241 C  CG2   . THR D 51  ? 0.3848 0.5490 0.5896 -0.1794 0.1107  0.0963  50  THR C CG2   
4242 N  N     . CYS D 52  ? 0.3305 0.5105 0.5275 -0.1720 0.1398  0.0872  51  CYS C N     
4243 C  CA    . CYS D 52  ? 0.3485 0.5331 0.5553 -0.1583 0.1439  0.0796  51  CYS C CA    
4244 C  C     . CYS D 52  ? 0.3398 0.5010 0.5331 -0.1501 0.1297  0.0797  51  CYS C C     
4245 O  O     . CYS D 52  ? 0.3157 0.4586 0.4905 -0.1550 0.1183  0.0860  51  CYS C O     
4246 C  CB    . CYS D 52  ? 0.4172 0.6038 0.6117 -0.1589 0.1607  0.0723  51  CYS C CB    
4247 S  SG    . CYS D 52  ? 0.5275 0.6890 0.6777 -0.1722 0.1590  0.0755  51  CYS C SG    
4248 N  N     . LEU D 53  ? 0.2975 0.4594 0.5004 -0.1372 0.1314  0.0727  52  LEU C N     
4249 C  CA    . LEU D 53  ? 0.2881 0.4325 0.4825 -0.1294 0.1201  0.0715  52  LEU C CA    
4250 C  C     . LEU D 53  ? 0.3494 0.4839 0.5231 -0.1291 0.1266  0.0647  52  LEU C C     
4251 O  O     . LEU D 53  ? 0.3509 0.4903 0.5282 -0.1251 0.1396  0.0571  52  LEU C O     
4252 C  CB    . LEU D 53  ? 0.2890 0.4386 0.5066 -0.1174 0.1162  0.0692  52  LEU C CB    
4253 C  CG    . LEU D 53  ? 0.3148 0.4496 0.5298 -0.1103 0.1039  0.0691  52  LEU C CG    
4254 C  CD1   . LEU D 53  ? 0.3682 0.4920 0.5707 -0.1054 0.1073  0.0618  52  LEU C CD1   
4255 C  CD2   . LEU D 53  ? 0.2776 0.4001 0.4785 -0.1163 0.0925  0.0760  52  LEU C CD2   
4256 N  N     . LEU D 54  ? 0.3421 0.4625 0.4933 -0.1336 0.1178  0.0676  53  LEU C N     
4257 C  CA    . LEU D 54  ? 0.3221 0.4336 0.4527 -0.1351 0.1206  0.0614  53  LEU C CA    
4258 C  C     . LEU D 54  ? 0.3272 0.4326 0.4625 -0.1269 0.1132  0.0577  53  LEU C C     
4259 O  O     . LEU D 54  ? 0.3131 0.4159 0.4538 -0.1235 0.1008  0.0627  53  LEU C O     
4260 C  CB    . LEU D 54  ? 0.3367 0.4399 0.4406 -0.1450 0.1140  0.0673  53  LEU C CB    
4261 C  CG    . LEU D 54  ? 0.3753 0.4808 0.4703 -0.1553 0.1206  0.0725  53  LEU C CG    
4262 C  CD1   . LEU D 54  ? 0.3752 0.4688 0.4400 -0.1645 0.1129  0.0796  53  LEU C CD1   
4263 C  CD2   . LEU D 54  ? 0.3803 0.4944 0.4773 -0.1580 0.1396  0.0645  53  LEU C CD2   
4264 N  N     . ASP D 55  ? 0.3132 0.4143 0.4449 -0.1241 0.1220  0.0484  54  ASP C N     
4265 C  CA    . ASP D 55  ? 0.3224 0.4149 0.4523 -0.1199 0.1170  0.0438  54  ASP C CA    
4266 C  C     . ASP D 55  ? 0.3549 0.4394 0.4576 -0.1296 0.1185  0.0390  54  ASP C C     
4267 O  O     . ASP D 55  ? 0.3819 0.4603 0.4708 -0.1333 0.1314  0.0318  54  ASP C O     
4268 C  CB    . ASP D 55  ? 0.3778 0.4668 0.5214 -0.1100 0.1255  0.0372  54  ASP C CB    
4269 C  CG    . ASP D 55  ? 0.4091 0.4860 0.5484 -0.1074 0.1204  0.0330  54  ASP C CG    
4270 O  OD1   . ASP D 55  ? 0.4887 0.5551 0.6070 -0.1142 0.1229  0.0268  54  ASP C OD1   
4271 O  OD2   . ASP D 55  ? 0.4610 0.5382 0.6159 -0.1001 0.1138  0.0359  54  ASP C OD2   
4272 N  N     . ILE D 56  ? 0.3563 0.4416 0.4510 -0.1337 0.1056  0.0429  55  ILE C N     
4273 C  CA    . ILE D 56  ? 0.3549 0.4378 0.4240 -0.1451 0.1025  0.0413  55  ILE C CA    
4274 C  C     . ILE D 56  ? 0.3446 0.4249 0.4103 -0.1472 0.0974  0.0362  55  ILE C C     
4275 O  O     . ILE D 56  ? 0.3259 0.4125 0.4069 -0.1415 0.0880  0.0400  55  ILE C O     
4276 C  CB    . ILE D 56  ? 0.3470 0.4370 0.4099 -0.1487 0.0904  0.0523  55  ILE C CB    
4277 C  CG1   . ILE D 56  ? 0.3527 0.4422 0.4156 -0.1496 0.0979  0.0564  55  ILE C CG1   
4278 C  CG2   . ILE D 56  ? 0.3718 0.4621 0.4079 -0.1607 0.0842  0.0525  55  ILE C CG2   
4279 C  CD1   . ILE D 56  ? 0.3805 0.4710 0.4366 -0.1519 0.0876  0.0676  55  ILE C CD1   
4280 N  N     . LEU D 57  ? 0.3680 0.4377 0.4116 -0.1564 0.1045  0.0273  56  LEU C N     
4281 C  CA    . LEU D 57  ? 0.3737 0.4399 0.4089 -0.1631 0.1001  0.0218  56  LEU C CA    
4282 C  C     . LEU D 57  ? 0.3907 0.4653 0.4049 -0.1774 0.0900  0.0243  56  LEU C C     
4283 O  O     . LEU D 57  ? 0.4163 0.4835 0.4059 -0.1871 0.0953  0.0216  56  LEU C O     
4284 C  CB    . LEU D 57  ? 0.3932 0.4372 0.4156 -0.1643 0.1147  0.0097  56  LEU C CB    
4285 C  CG    . LEU D 57  ? 0.4202 0.4573 0.4328 -0.1730 0.1107  0.0040  56  LEU C CG    
4286 C  CD1   . LEU D 57  ? 0.3770 0.4150 0.4138 -0.1621 0.1073  0.0058  56  LEU C CD1   
4287 C  CD2   . LEU D 57  ? 0.4984 0.5090 0.4804 -0.1826 0.1236  -0.0083 56  LEU C CD2   
4288 N  N     . ASP D 58  ? 0.3778 0.4694 0.4023 -0.1784 0.0756  0.0299  57  ASP C N     
4289 C  CA    . ASP D 58  ? 0.3909 0.4975 0.4021 -0.1900 0.0625  0.0343  57  ASP C CA    
4290 C  C     . ASP D 58  ? 0.4040 0.5090 0.4040 -0.2033 0.0622  0.0255  57  ASP C C     
4291 O  O     . ASP D 58  ? 0.3890 0.4950 0.4049 -0.1991 0.0631  0.0226  57  ASP C O     
4292 C  CB    . ASP D 58  ? 0.3693 0.4984 0.4032 -0.1802 0.0475  0.0466  57  ASP C CB    
4293 C  CG    . ASP D 58  ? 0.3830 0.5328 0.4075 -0.1894 0.0315  0.0534  57  ASP C CG    
4294 O  OD1   . ASP D 58  ? 0.4107 0.5553 0.4072 -0.2040 0.0312  0.0507  57  ASP C OD1   
4295 O  OD2   . ASP D 58  ? 0.3676 0.5382 0.4127 -0.1810 0.0198  0.0615  57  ASP C OD2   
4296 N  N     . THR D 59  ? 0.4356 0.5348 0.4050 -0.2207 0.0619  0.0206  58  THR C N     
4297 C  CA    . THR D 59  ? 0.4572 0.5468 0.4078 -0.2370 0.0647  0.0101  58  THR C CA    
4298 C  C     . THR D 59  ? 0.4687 0.5836 0.4115 -0.2535 0.0475  0.0143  58  THR C C     
4299 O  O     . THR D 59  ? 0.4858 0.6224 0.4327 -0.2518 0.0340  0.0253  58  THR C O     
4300 C  CB    . THR D 59  ? 0.5324 0.5884 0.4489 -0.2458 0.0812  -0.0017 58  THR C CB    
4301 O  OG1   . THR D 59  ? 0.5170 0.5742 0.4078 -0.2567 0.0776  0.0008  58  THR C OG1   
4302 C  CG2   . THR D 59  ? 0.5008 0.5377 0.4295 -0.2274 0.0978  -0.0047 58  THR C CG2   
4303 N  N     . ALA D 60  ? 0.4825 0.5952 0.4157 -0.2689 0.0475  0.0062  59  ALA C N     
4304 C  CA    . ALA D 60  ? 0.4990 0.6363 0.4225 -0.2893 0.0322  0.0079  59  ALA C CA    
4305 C  C     . ALA D 60  ? 0.5646 0.6808 0.4421 -0.3115 0.0349  0.0001  59  ALA C C     
4306 O  O     . ALA D 60  ? 0.5699 0.6475 0.4207 -0.3168 0.0520  -0.0122 59  ALA C O     
4307 C  CB    . ALA D 60  ? 0.4943 0.6405 0.4288 -0.2985 0.0312  0.0027  59  ALA C CB    
4308 N  N     . GLY D 61  ? 0.6150 0.7561 0.4822 -0.3247 0.0177  0.0073  60  GLY C N     
4309 C  CA    . GLY D 61  ? 0.6414 0.7659 0.4620 -0.3497 0.0170  0.0006  60  GLY C CA    
4310 C  C     . GLY D 61  ? 0.6938 0.8291 0.4973 -0.3780 0.0076  -0.0053 60  GLY C C     
4311 O  O     . GLY D 61  ? 0.6805 0.8148 0.4490 -0.4005 -0.0008 -0.0066 60  GLY C O     
4312 N  N     . GLN D 62  ? 0.7290 0.8734 0.5540 -0.3793 0.0090  -0.0090 61  GLN C N     
4313 C  CA    . GLN D 62  ? 0.7686 0.9191 0.5756 -0.4090 0.0031  -0.0163 61  GLN C CA    
4314 C  C     . GLN D 62  ? 0.8106 0.9064 0.5633 -0.4293 0.0196  -0.0330 61  GLN C C     
4315 O  O     . GLN D 62  ? 0.8163 0.8696 0.5601 -0.4170 0.0404  -0.0419 61  GLN C O     
4316 C  CB    . GLN D 62  ? 0.7620 0.9286 0.6023 -0.4052 0.0049  -0.0173 61  GLN C CB    
4317 C  CG    . GLN D 62  ? 0.6687 0.8759 0.5638 -0.3781 -0.0029 -0.0039 61  GLN C CG    
4318 C  CD    . GLN D 62  ? 0.6751 0.9420 0.5956 -0.3829 -0.0264 0.0088  61  GLN C CD    
4319 O  OE1   . GLN D 62  ? 0.6923 0.9845 0.6395 -0.3614 -0.0359 0.0218  61  GLN C OE1   
4320 N  NE2   . GLN D 62  ? 0.7146 1.0003 0.6254 -0.4055 -0.0351 0.0057  61  GLN C NE2   
4321 N  N     . GLU D 63  ? 0.8233 0.9196 0.5390 -0.4610 0.0102  -0.0375 62  GLU C N     
4322 C  CA    . GLU D 63  ? 0.9325 0.9718 0.5904 -0.4808 0.0267  -0.0539 62  GLU C CA    
4323 C  C     . GLU D 63  ? 0.9208 0.9256 0.5665 -0.4871 0.0416  -0.0666 62  GLU C C     
4324 O  O     . GLU D 63  ? 0.8864 0.8336 0.4921 -0.4917 0.0620  -0.0806 62  GLU C O     
4325 C  CB    . GLU D 63  ? 0.9836 1.0308 0.6006 -0.5137 0.0114  -0.0548 62  GLU C CB    
4326 C  CG    . GLU D 63  ? 1.0167 1.1021 0.6492 -0.5033 -0.0066 -0.0388 62  GLU C CG    
4327 C  CD    . GLU D 63  ? 1.1387 1.2088 0.7170 -0.5279 -0.0131 -0.0412 62  GLU C CD    
4328 O  OE1   . GLU D 63  ? 1.2028 1.2212 0.7276 -0.5470 0.0029  -0.0571 62  GLU C OE1   
4329 O  OE2   . GLU D 63  ? 1.1536 1.2608 0.7411 -0.5269 -0.0339 -0.0267 62  GLU C OE2   
4330 N  N     . GLU D 64  ? 0.9096 0.9457 0.5885 -0.4808 0.0335  -0.0612 63  GLU C N     
4331 C  CA    . GLU D 64  ? 0.8759 0.8784 0.5416 -0.4815 0.0470  -0.0712 63  GLU C CA    
4332 C  C     . GLU D 64  ? 0.8570 0.8154 0.5269 -0.4608 0.0685  -0.0777 63  GLU C C     
4333 O  O     . GLU D 64  ? 0.8795 0.7902 0.5207 -0.4635 0.0840  -0.0888 63  GLU C O     
4334 C  CB    . GLU D 64  ? 0.8338 0.8814 0.5382 -0.4773 0.0349  -0.0631 63  GLU C CB    
4335 C  CG    . GLU D 64  ? 0.9194 1.0084 0.6186 -0.4988 0.0160  -0.0573 63  GLU C CG    
4336 C  CD    . GLU D 64  ? 0.9119 1.0656 0.6582 -0.4878 -0.0044 -0.0412 63  GLU C CD    
4337 O  OE1   . GLU D 64  ? 0.8690 1.0651 0.6575 -0.4776 -0.0124 -0.0333 63  GLU C OE1   
4338 O  OE2   . GLU D 64  ? 0.9490 1.1081 0.6908 -0.4867 -0.0106 -0.0363 63  GLU C OE2   
4339 N  N     . TYR D 65  ? 0.7516 0.7244 0.4559 -0.4399 0.0702  -0.0700 64  TYR C N     
4340 C  CA    . TYR D 65  ? 0.8345 0.7760 0.5523 -0.4129 0.0883  -0.0723 64  TYR C CA    
4341 C  C     . TYR D 65  ? 0.9092 0.8164 0.6051 -0.3991 0.1032  -0.0770 64  TYR C C     
4342 O  O     . TYR D 65  ? 0.9055 0.7946 0.6179 -0.3726 0.1166  -0.0769 64  TYR C O     
4343 C  CB    . TYR D 65  ? 0.6709 0.6547 0.4464 -0.3871 0.0799  -0.0588 64  TYR C CB    
4344 C  CG    . TYR D 65  ? 0.6539 0.6800 0.4532 -0.3974 0.0643  -0.0533 64  TYR C CG    
4345 C  CD1   . TYR D 65  ? 0.6791 0.6865 0.4610 -0.4069 0.0679  -0.0609 64  TYR C CD1   
4346 C  CD2   . TYR D 65  ? 0.6172 0.7002 0.4542 -0.3915 0.0463  -0.0401 64  TYR C CD2   
4347 C  CE1   . TYR D 65  ? 0.6663 0.7138 0.4700 -0.4114 0.0549  -0.0555 64  TYR C CE1   
4348 C  CE2   . TYR D 65  ? 0.6044 0.7263 0.4644 -0.3937 0.0338  -0.0351 64  TYR C CE2   
4349 C  CZ    . TYR D 65  ? 0.6283 0.7334 0.4723 -0.4040 0.0386  -0.0429 64  TYR C CZ    
4350 O  OH    . TYR D 65  ? 0.6161 0.7631 0.4848 -0.4064 0.0275  -0.0374 64  TYR C OH    
4351 N  N     . SER D 66  ? 0.8770 0.7756 0.5352 -0.4176 0.1015  -0.0812 65  SER C N     
4352 C  CA    . SER D 66  ? 0.9776 0.8457 0.6131 -0.4063 0.1171  -0.0861 65  SER C CA    
4353 C  C     . SER D 66  ? 1.0374 0.8487 0.6527 -0.3944 0.1425  -0.0989 65  SER C C     
4354 O  O     . SER D 66  ? 1.0553 0.8508 0.6746 -0.3724 0.1577  -0.1002 65  SER C O     
4355 C  CB    . SER D 66  ? 0.9553 0.8162 0.5438 -0.4333 0.1122  -0.0906 65  SER C CB    
4356 O  OG    . SER D 66  ? 0.9800 0.8271 0.5322 -0.4666 0.1068  -0.0993 65  SER C OG    
4357 N  N     . ALA D 67  ? 1.0296 0.8110 0.6246 -0.4078 0.1475  -0.1078 66  ALA C N     
4358 C  CA    . ALA D 67  ? 1.0553 0.7817 0.6337 -0.3932 0.1703  -0.1182 66  ALA C CA    
4359 C  C     . ALA D 67  ? 1.0512 0.7912 0.6790 -0.3564 0.1752  -0.1096 66  ALA C C     
4360 O  O     . ALA D 67  ? 1.0776 0.7966 0.7056 -0.3344 0.1918  -0.1126 66  ALA C O     
4361 C  CB    . ALA D 67  ? 1.1128 0.8081 0.6647 -0.4143 0.1715  -0.1264 66  ALA C CB    
4362 N  N     . MET D 68  ? 0.9830 0.7611 0.6538 -0.3496 0.1608  -0.0987 67  MET C N     
4363 C  CA    . MET D 68  ? 0.9700 0.7580 0.6840 -0.3175 0.1643  -0.0908 67  MET C CA    
4364 C  C     . MET D 68  ? 0.9975 0.8154 0.7406 -0.2973 0.1631  -0.0822 67  MET C C     
4365 O  O     . MET D 68  ? 0.9739 0.7958 0.7482 -0.2713 0.1682  -0.0771 67  MET C O     
4366 C  CB    . MET D 68  ? 0.9264 0.7478 0.6762 -0.3168 0.1496  -0.0815 67  MET C CB    
4367 C  CG    . MET D 68  ? 0.9488 0.7634 0.6766 -0.3452 0.1436  -0.0865 67  MET C CG    
4368 S  SD    . MET D 68  ? 0.9971 0.8320 0.7638 -0.3355 0.1367  -0.0784 67  MET C SD    
4369 C  CE    . MET D 68  ? 0.9323 0.7033 0.6809 -0.3166 0.1568  -0.0855 67  MET C CE    
4370 N  N     . ARG D 69  ? 1.0154 0.8561 0.7492 -0.3102 0.1545  -0.0794 68  ARG C N     
4371 C  CA    . ARG D 69  ? 0.9668 0.8304 0.7206 -0.2946 0.1544  -0.0717 68  ARG C CA    
4372 C  C     . ARG D 69  ? 0.9962 0.8281 0.7423 -0.2760 0.1770  -0.0786 68  ARG C C     
4373 O  O     . ARG D 69  ? 0.9686 0.8194 0.7423 -0.2571 0.1797  -0.0716 68  ARG C O     
4374 C  CB    . ARG D 69  ? 0.9644 0.8451 0.6955 -0.3149 0.1439  -0.0695 68  ARG C CB    
4375 N  N     . ASP D 70  ? 1.0410 0.8253 0.7504 -0.2812 0.1937  -0.0922 69  ASP C N     
4376 C  CA    . ASP D 70  ? 1.0732 0.8259 0.7759 -0.2613 0.2171  -0.0997 69  ASP C CA    
4377 C  C     . ASP D 70  ? 1.0660 0.8336 0.8166 -0.2309 0.2192  -0.0916 69  ASP C C     
4378 O  O     . ASP D 70  ? 1.0533 0.8251 0.8198 -0.2117 0.2315  -0.0908 69  ASP C O     
4379 C  CB    . ASP D 70  ? 1.1203 0.8148 0.7755 -0.2705 0.2334  -0.1152 69  ASP C CB    
4380 C  CG    . ASP D 70  ? 1.1458 0.8195 0.7467 -0.3015 0.2344  -0.1252 69  ASP C CG    
4381 O  OD1   . ASP D 70  ? 1.0614 0.7692 0.6624 -0.3183 0.2186  -0.1188 69  ASP C OD1   
4382 O  OD2   . ASP D 70  ? 1.2501 0.8703 0.8057 -0.3086 0.2516  -0.1394 69  ASP C OD2   
4383 N  N     . GLN D 71  ? 1.0052 0.7829 0.7792 -0.2274 0.2072  -0.0855 70  GLN C N     
4384 C  CA    . GLN D 71  ? 1.0365 0.8199 0.8484 -0.2002 0.2097  -0.0792 70  GLN C CA    
4385 C  C     . GLN D 71  ? 0.9898 0.8162 0.8427 -0.1854 0.2036  -0.0677 70  GLN C C     
4386 O  O     . GLN D 71  ? 0.9857 0.8132 0.8579 -0.1643 0.2147  -0.0666 70  GLN C O     
4387 C  CB    . GLN D 71  ? 1.0471 0.8310 0.8702 -0.2031 0.1977  -0.0750 70  GLN C CB    
4388 C  CG    . GLN D 71  ? 1.0655 0.8607 0.9283 -0.1779 0.1954  -0.0663 70  GLN C CG    
4389 C  CD    . GLN D 71  ? 1.0544 0.8339 0.9254 -0.1532 0.2120  -0.0686 70  GLN C CD    
4390 O  OE1   . GLN D 71  ? 1.0153 0.8248 0.9208 -0.1370 0.2105  -0.0607 70  GLN C OE1   
4391 N  NE2   . GLN D 71  ? 1.0952 0.8282 0.9343 -0.1505 0.2283  -0.0793 70  GLN C NE2   
4392 N  N     . TYR D 72  ? 0.9506 0.8133 0.8182 -0.1957 0.1859  -0.0587 71  TYR C N     
4393 C  CA    . TYR D 72  ? 0.8659 0.7632 0.7664 -0.1834 0.1808  -0.0481 71  TYR C CA    
4394 C  C     . TYR D 72  ? 0.8734 0.7672 0.7594 -0.1833 0.1944  -0.0520 71  TYR C C     
4395 O  O     . TYR D 72  ? 0.8096 0.7243 0.7208 -0.1707 0.1968  -0.0455 71  TYR C O     
4396 C  CB    . TYR D 72  ? 0.7839 0.7155 0.6983 -0.1938 0.1600  -0.0379 71  TYR C CB    
4397 C  CG    . TYR D 72  ? 0.7700 0.7055 0.6544 -0.2169 0.1530  -0.0399 71  TYR C CG    
4398 C  CD1   . TYR D 72  ? 0.8195 0.7553 0.6854 -0.2226 0.1584  -0.0408 71  TYR C CD1   
4399 C  CD2   . TYR D 72  ? 0.7608 0.7026 0.6362 -0.2339 0.1400  -0.0401 71  TYR C CD2   
4400 C  CE1   . TYR D 72  ? 0.8205 0.7595 0.6564 -0.2446 0.1501  -0.0417 71  TYR C CE1   
4401 C  CE2   . TYR D 72  ? 0.7726 0.7223 0.6222 -0.2558 0.1311  -0.0408 71  TYR C CE2   
4402 C  CZ    . TYR D 72  ? 0.8465 0.7935 0.6750 -0.2609 0.1356  -0.0414 71  TYR C CZ    
4403 O  OH    . TYR D 72  ? 0.8919 0.8454 0.6915 -0.2831 0.1257  -0.0413 71  TYR C OH    
4404 N  N     . MET D 73  ? 0.8927 0.7599 0.7363 -0.1991 0.2036  -0.0628 72  MET C N     
4405 C  CA    . MET D 73  ? 0.8946 0.7556 0.7195 -0.2005 0.2184  -0.0676 72  MET C CA    
4406 C  C     . MET D 73  ? 0.8786 0.7263 0.7176 -0.1774 0.2395  -0.0724 72  MET C C     
4407 O  O     . MET D 73  ? 0.8747 0.7352 0.7231 -0.1698 0.2504  -0.0713 72  MET C O     
4408 C  CB    . MET D 73  ? 0.8946 0.7264 0.6668 -0.2242 0.2233  -0.0788 72  MET C CB    
4409 C  CG    . MET D 73  ? 0.8729 0.7280 0.6317 -0.2458 0.2054  -0.0721 72  MET C CG    
4410 S  SD    . MET D 73  ? 1.0088 0.8286 0.7023 -0.2765 0.2094  -0.0856 72  MET C SD    
4411 C  CE    . MET D 73  ? 0.8787 0.7359 0.5677 -0.2980 0.1825  -0.0735 72  MET C CE    
4412 N  N     . ARG D 74  ? 0.8948 0.7199 0.7386 -0.1652 0.2443  -0.0765 73  ARG C N     
4413 C  CA    . ARG D 74  ? 0.9317 0.7491 0.7962 -0.1394 0.2612  -0.0786 73  ARG C CA    
4414 C  C     . ARG D 74  ? 0.8219 0.6821 0.7363 -0.1238 0.2535  -0.0658 73  ARG C C     
4415 O  O     . ARG D 74  ? 0.8271 0.7008 0.7578 -0.1115 0.2668  -0.0656 73  ARG C O     
4416 C  CB    . ARG D 74  ? 0.9389 0.7226 0.7980 -0.1291 0.2643  -0.0831 73  ARG C CB    
4417 C  CG    . ARG D 74  ? 0.9920 0.7219 0.7985 -0.1392 0.2799  -0.0984 73  ARG C CG    
4418 C  CD    . ARG D 74  ? 1.0881 0.7983 0.8687 -0.1608 0.2660  -0.1004 73  ARG C CD    
4419 N  NE    . ARG D 74  ? 1.1240 0.7881 0.8480 -0.1807 0.2769  -0.1146 73  ARG C NE    
4420 C  CZ    . ARG D 74  ? 1.1452 0.7875 0.8402 -0.2026 0.2680  -0.1184 73  ARG C CZ    
4421 N  NH1   . ARG D 74  ? 1.0829 0.7441 0.8004 -0.2059 0.2501  -0.1097 73  ARG C NH1   
4422 N  NH2   . ARG D 74  ? 1.2078 0.8077 0.8486 -0.2229 0.2782  -0.1318 73  ARG C NH2   
4423 N  N     . THR D 75  ? 0.8171 0.6991 0.7554 -0.1252 0.2328  -0.0553 74  THR C N     
4424 C  CA    . THR D 75  ? 0.7743 0.6916 0.7571 -0.1113 0.2245  -0.0434 74  THR C CA    
4425 C  C     . THR D 75  ? 0.6800 0.6280 0.6717 -0.1191 0.2205  -0.0366 74  THR C C     
4426 O  O     . THR D 75  ? 0.7133 0.6868 0.7372 -0.1079 0.2204  -0.0293 74  THR C O     
4427 C  CB    . THR D 75  ? 0.8077 0.7329 0.8075 -0.1113 0.2051  -0.0356 74  THR C CB    
4428 O  OG1   . THR D 75  ? 0.8483 0.7666 0.8223 -0.1318 0.1948  -0.0376 74  THR C OG1   
4429 C  CG2   . THR D 75  ? 0.8082 0.7099 0.8128 -0.0962 0.2094  -0.0382 74  THR C CG2   
4430 N  N     . GLY D 76  ? 0.6926 0.6385 0.6553 -0.1387 0.2165  -0.0382 75  GLY C N     
4431 C  CA    . GLY D 76  ? 0.6800 0.6516 0.6481 -0.1464 0.2107  -0.0300 75  GLY C CA    
4432 C  C     . GLY D 76  ? 0.7182 0.6906 0.6800 -0.1444 0.2307  -0.0345 75  GLY C C     
4433 O  O     . GLY D 76  ? 0.7516 0.6996 0.6873 -0.1454 0.2487  -0.0462 75  GLY C O     
4434 N  N     . GLU D 77  ? 0.6716 0.6715 0.6558 -0.1425 0.2283  -0.0252 76  GLU C N     
4435 C  CA    . GLU D 77  ? 0.6137 0.6205 0.5950 -0.1427 0.2472  -0.0279 76  GLU C CA    
4436 C  C     . GLU D 77  ? 0.6564 0.6631 0.6064 -0.1627 0.2450  -0.0255 76  GLU C C     
4437 O  O     . GLU D 77  ? 0.6758 0.6812 0.6119 -0.1668 0.2633  -0.0302 76  GLU C O     
4438 C  CB    . GLU D 77  ? 0.6209 0.6580 0.6457 -0.1298 0.2480  -0.0196 76  GLU C CB    
4439 C  CG    . GLU D 77  ? 0.6263 0.6635 0.6794 -0.1091 0.2537  -0.0226 76  GLU C CG    
4440 C  CD    . GLU D 77  ? 0.6366 0.7025 0.7312 -0.1003 0.2416  -0.0113 76  GLU C CD    
4441 O  OE1   . GLU D 77  ? 0.6391 0.7195 0.7365 -0.1113 0.2276  -0.0017 76  GLU C OE1   
4442 O  OE2   . GLU D 77  ? 0.6462 0.7182 0.7688 -0.0827 0.2443  -0.0113 76  GLU C OE2   
4443 N  N     . GLY D 78  ? 0.5949 0.6025 0.5322 -0.1749 0.2239  -0.0184 77  GLY C N     
4444 C  CA    . GLY D 78  ? 0.6372 0.6438 0.5434 -0.1931 0.2192  -0.0143 77  GLY C CA    
4445 C  C     . GLY D 78  ? 0.6665 0.6714 0.5583 -0.2037 0.1958  -0.0088 77  GLY C C     
4446 O  O     . GLY D 78  ? 0.5884 0.6018 0.5041 -0.1959 0.1814  -0.0042 77  GLY C O     
4447 N  N     . PHE D 79  ? 0.6619 0.6581 0.5152 -0.2217 0.1918  -0.0084 78  PHE C N     
4448 C  CA    . PHE D 79  ? 0.5964 0.5908 0.4312 -0.2337 0.1718  -0.0057 78  PHE C CA    
4449 C  C     . PHE D 79  ? 0.6645 0.6676 0.4808 -0.2458 0.1569  0.0064  78  PHE C C     
4450 O  O     . PHE D 79  ? 0.7439 0.7367 0.5289 -0.2574 0.1663  0.0049  78  PHE C O     
4451 C  CB    . PHE D 79  ? 0.6975 0.6659 0.4964 -0.2451 0.1821  -0.0203 78  PHE C CB    
4452 C  CG    . PHE D 79  ? 0.7205 0.6760 0.5360 -0.2313 0.1960  -0.0308 78  PHE C CG    
4453 C  CD1   . PHE D 79  ? 0.6379 0.5851 0.4618 -0.2187 0.2199  -0.0382 78  PHE C CD1   
4454 C  CD2   . PHE D 79  ? 0.6965 0.6515 0.5239 -0.2291 0.1844  -0.0317 78  PHE C CD2   
4455 C  CE1   . PHE D 79  ? 0.6413 0.5770 0.4829 -0.2029 0.2307  -0.0459 78  PHE C CE1   
4456 C  CE2   . PHE D 79  ? 0.6892 0.6297 0.5302 -0.2159 0.1959  -0.0398 78  PHE C CE2   
4457 C  CZ    . PHE D 79  ? 0.6836 0.6137 0.5315 -0.2019 0.2181  -0.0464 78  PHE C CZ    
4458 N  N     . LEU D 80  ? 0.6445 0.6655 0.4801 -0.2419 0.1344  0.0186  79  LEU C N     
4459 C  CA    . LEU D 80  ? 0.6748 0.7033 0.4930 -0.2513 0.1161  0.0314  79  LEU C CA    
4460 C  C     . LEU D 80  ? 0.6574 0.6846 0.4487 -0.2665 0.1023  0.0292  79  LEU C C     
4461 O  O     . LEU D 80  ? 0.6037 0.6434 0.4129 -0.2633 0.0893  0.0301  79  LEU C O     
4462 C  CB    . LEU D 80  ? 0.6102 0.6571 0.4628 -0.2374 0.1002  0.0454  79  LEU C CB    
4463 C  CG    . LEU D 80  ? 0.6538 0.7029 0.4920 -0.2415 0.0874  0.0603  79  LEU C CG    
4464 C  CD1   . LEU D 80  ? 0.6287 0.6688 0.4616 -0.2424 0.1041  0.0611  79  LEU C CD1   
4465 C  CD2   . LEU D 80  ? 0.5632 0.6274 0.4282 -0.2287 0.0677  0.0736  79  LEU C CD2   
4466 N  N     . CYS D 81  ? 0.7004 0.7132 0.4475 -0.2846 0.1052  0.0261  80  CYS C N     
4467 C  CA    . CYS D 81  ? 0.6858 0.6966 0.4031 -0.3026 0.0926  0.0229  80  CYS C CA    
4468 C  C     . CYS D 81  ? 0.7050 0.7339 0.4147 -0.3083 0.0661  0.0396  80  CYS C C     
4469 O  O     . CYS D 81  ? 0.7215 0.7419 0.4011 -0.3172 0.0645  0.0463  80  CYS C O     
4470 C  CB    . CYS D 81  ? 0.7745 0.7562 0.4441 -0.3201 0.1112  0.0089  80  CYS C CB    
4471 S  SG    . CYS D 81  ? 0.7546 0.7152 0.4378 -0.3080 0.1418  -0.0098 80  CYS C SG    
4472 N  N     . VAL D 82  ? 0.6653 0.7190 0.4019 -0.3025 0.0457  0.0468  81  VAL C N     
4473 C  CA    . VAL D 82  ? 0.6640 0.7395 0.4049 -0.3006 0.0200  0.0645  81  VAL C CA    
4474 C  C     . VAL D 82  ? 0.6952 0.7813 0.4089 -0.3208 0.0017  0.0654  81  VAL C C     
4475 O  O     . VAL D 82  ? 0.6934 0.7858 0.4103 -0.3294 0.0009  0.0557  81  VAL C O     
4476 C  CB    . VAL D 82  ? 0.6385 0.7376 0.4300 -0.2784 0.0098  0.0734  81  VAL C CB    
4477 C  CG1   . VAL D 82  ? 0.6171 0.7350 0.4143 -0.2713 -0.0143 0.0926  81  VAL C CG1   
4478 C  CG2   . VAL D 82  ? 0.5854 0.6738 0.4040 -0.2608 0.0280  0.0705  81  VAL C CG2   
4479 N  N     . PHE D 83  ? 0.7278 0.8150 0.4118 -0.3302 -0.0135 0.0774  82  PHE C N     
4480 C  CA    . PHE D 83  ? 0.7514 0.8598 0.4197 -0.3449 -0.0390 0.0847  82  PHE C CA    
4481 C  C     . PHE D 83  ? 0.7457 0.8754 0.4294 -0.3307 -0.0625 0.1066  82  PHE C C     
4482 O  O     . PHE D 83  ? 0.7288 0.8498 0.4269 -0.3131 -0.0573 0.1146  82  PHE C O     
4483 C  CB    . PHE D 83  ? 0.8093 0.8956 0.4178 -0.3734 -0.0368 0.0777  82  PHE C CB    
4484 C  CG    . PHE D 83  ? 0.8575 0.9264 0.4294 -0.3780 -0.0395 0.0887  82  PHE C CG    
4485 C  CD1   . PHE D 83  ? 0.8502 0.8896 0.4099 -0.3737 -0.0146 0.0833  82  PHE C CD1   
4486 C  CD2   . PHE D 83  ? 0.8763 0.9586 0.4250 -0.3874 -0.0668 0.1045  82  PHE C CD2   
4487 C  CE1   . PHE D 83  ? 0.8860 0.9078 0.4096 -0.3800 -0.0155 0.0933  82  PHE C CE1   
4488 C  CE2   . PHE D 83  ? 0.9133 0.9754 0.4245 -0.3922 -0.0691 0.1154  82  PHE C CE2   
4489 C  CZ    . PHE D 83  ? 0.9185 0.9491 0.4160 -0.3893 -0.0427 0.1094  82  PHE C CZ    
4490 N  N     . ALA D 84  ? 0.7587 0.9168 0.4406 -0.3377 -0.0889 0.1168  83  ALA C N     
4491 C  CA    . ALA D 84  ? 0.7567 0.9365 0.4542 -0.3220 -0.1130 0.1385  83  ALA C CA    
4492 C  C     . ALA D 84  ? 0.8111 0.9868 0.4605 -0.3400 -0.1316 0.1493  83  ALA C C     
4493 O  O     . ALA D 84  ? 0.8399 1.0233 0.4629 -0.3640 -0.1399 0.1435  83  ALA C O     
4494 C  CB    . ALA D 84  ? 0.7233 0.9479 0.4694 -0.3090 -0.1303 0.1443  83  ALA C CB    
4495 N  N     . ILE D 85  ? 0.8281 0.9902 0.4641 -0.3295 -0.1388 0.1654  84  ILE C N     
4496 C  CA    . ILE D 85  ? 0.8855 1.0326 0.4675 -0.3470 -0.1524 0.1756  84  ILE C CA    
4497 C  C     . ILE D 85  ? 0.9223 1.1064 0.5035 -0.3527 -0.1864 0.1895  84  ILE C C     
4498 O  O     . ILE D 85  ? 0.9573 1.1325 0.4921 -0.3693 -0.2016 0.1988  84  ILE C O     
4499 C  CB    . ILE D 85  ? 0.9008 1.0196 0.4671 -0.3343 -0.1501 0.1899  84  ILE C CB    
4500 C  CG1   . ILE D 85  ? 0.9006 1.0385 0.5104 -0.3033 -0.1660 0.2076  84  ILE C CG1   
4501 C  CG2   . ILE D 85  ? 0.8882 0.9727 0.4495 -0.3346 -0.1162 0.1756  84  ILE C CG2   
4502 C  CD1   . ILE D 85  ? 0.9040 1.0638 0.5060 -0.2981 -0.2010 0.2304  84  ILE C CD1   
4503 N  N     . ASN D 86  ? 0.8692 1.0961 0.5009 -0.3398 -0.1987 0.1915  85  ASN C N     
4504 C  CA    . ASN D 86  ? 0.9176 1.1883 0.5550 -0.3479 -0.2293 0.2018  85  ASN C CA    
4505 C  C     . ASN D 86  ? 0.8765 1.1687 0.5207 -0.3700 -0.2258 0.1844  85  ASN C C     
4506 O  O     . ASN D 86  ? 0.8778 1.2159 0.5413 -0.3753 -0.2495 0.1911  85  ASN C O     
4507 C  CB    . ASN D 86  ? 0.8750 1.1846 0.5652 -0.3162 -0.2493 0.2204  85  ASN C CB    
4508 C  CG    . ASN D 86  ? 0.8145 1.1507 0.5648 -0.2999 -0.2376 0.2103  85  ASN C CG    
4509 O  OD1   . ASN D 86  ? 0.7717 1.0838 0.5282 -0.3004 -0.2104 0.1931  85  ASN C OD1   
4510 N  ND2   . ASN D 86  ? 0.7816 1.1692 0.5757 -0.2856 -0.2583 0.2212  85  ASN C ND2   
4511 N  N     . ASN D 87  ? 0.8709 1.1312 0.4993 -0.3834 -0.1973 0.1626  86  ASN C N     
4512 C  CA    . ASN D 87  ? 0.8655 1.1373 0.4971 -0.4040 -0.1908 0.1447  86  ASN C CA    
4513 C  C     . ASN D 87  ? 0.9081 1.1329 0.4793 -0.4321 -0.1709 0.1272  86  ASN C C     
4514 O  O     . ASN D 87  ? 0.8947 1.0848 0.4628 -0.4279 -0.1414 0.1122  86  ASN C O     
4515 C  CB    . ASN D 87  ? 0.8328 1.1140 0.5186 -0.3838 -0.1732 0.1352  86  ASN C CB    
4516 C  CG    . ASN D 87  ? 0.8005 1.0986 0.4962 -0.4025 -0.1697 0.1198  86  ASN C CG    
4517 O  OD1   . ASN D 87  ? 0.8391 1.1294 0.4947 -0.4331 -0.1726 0.1109  86  ASN C OD1   
4518 N  ND2   . ASN D 87  ? 0.7891 1.1072 0.5357 -0.3850 -0.1626 0.1163  86  ASN C ND2   
4519 N  N     . THR D 88  ? 0.9625 1.1857 0.4847 -0.4604 -0.1869 0.1294  87  THR C N     
4520 C  CA    . THR D 88  ? 1.0095 1.1863 0.4702 -0.4886 -0.1674 0.1115  87  THR C CA    
4521 C  C     . THR D 88  ? 1.0137 1.1766 0.4810 -0.4980 -0.1439 0.0881  87  THR C C     
4522 O  O     . THR D 88  ? 1.0077 1.1253 0.4479 -0.5020 -0.1143 0.0716  87  THR C O     
4523 C  CB    . THR D 88  ? 1.0698 1.2482 0.4873 -0.5157 -0.1873 0.1167  87  THR C CB    
4524 O  OG1   . THR D 88  ? 1.0893 1.2669 0.4972 -0.5042 -0.2027 0.1368  87  THR C OG1   
4525 C  CG2   . THR D 88  ? 1.1191 1.2465 0.4807 -0.5425 -0.1629 0.0959  87  THR C CG2   
4526 N  N     . LYS D 89  ? 0.9701 1.1711 0.4736 -0.5008 -0.1560 0.0867  88  LYS C N     
4527 C  CA    . LYS D 89  ? 0.9594 1.1453 0.4679 -0.5100 -0.1351 0.0657  88  LYS C CA    
4528 C  C     . LYS D 89  ? 0.9224 1.0773 0.4529 -0.4848 -0.1035 0.0560  88  LYS C C     
4529 O  O     . LYS D 89  ? 0.9410 1.0530 0.4428 -0.4937 -0.0773 0.0375  88  LYS C O     
4530 C  CB    . LYS D 89  ? 0.9294 1.1668 0.4841 -0.5115 -0.1529 0.0690  88  LYS C CB    
4531 C  CG    . LYS D 89  ? 0.9184 1.1405 0.4798 -0.5206 -0.1328 0.0491  88  LYS C CG    
4532 C  CD    . LYS D 89  ? 0.9161 1.1922 0.5197 -0.5267 -0.1512 0.0531  88  LYS C CD    
4533 C  CE    . LYS D 89  ? 0.9533 1.2484 0.5400 -0.5463 -0.1680 0.0609  88  LYS C CE    
4534 N  NZ    . LYS D 89  ? 0.9355 1.2779 0.5662 -0.5458 -0.1776 0.0652  88  LYS C NZ    
4535 N  N     . SER D 90  ? 0.8869 1.0619 0.4668 -0.4529 -0.1059 0.0688  89  SER C N     
4536 C  CA    . SER D 90  ? 0.8930 1.0425 0.4956 -0.4296 -0.0785 0.0610  89  SER C CA    
4537 C  C     . SER D 90  ? 0.8702 0.9738 0.4293 -0.4332 -0.0574 0.0547  89  SER C C     
4538 O  O     . SER D 90  ? 0.8575 0.9329 0.4208 -0.4235 -0.0303 0.0422  89  SER C O     
4539 C  CB    . SER D 90  ? 0.7862 0.9643 0.4448 -0.3972 -0.0867 0.0766  89  SER C CB    
4540 O  OG    . SER D 90  ? 0.7991 0.9778 0.4471 -0.3884 -0.0989 0.0936  89  SER C OG    
4541 N  N     . PHE D 91  ? 0.9506 1.0470 0.4664 -0.4482 -0.0693 0.0628  90  PHE C N     
4542 C  CA    . PHE D 91  ? 1.0032 1.0561 0.4729 -0.4551 -0.0481 0.0559  90  PHE C CA    
4543 C  C     . PHE D 91  ? 0.9942 1.0113 0.4184 -0.4795 -0.0279 0.0338  90  PHE C C     
4544 O  O     . PHE D 91  ? 1.0155 0.9973 0.4260 -0.4753 0.0021  0.0202  90  PHE C O     
4545 C  CB    . PHE D 91  ? 0.9908 1.0452 0.4253 -0.4642 -0.0678 0.0727  90  PHE C CB    
4546 C  CG    . PHE D 91  ? 1.0417 1.0546 0.4308 -0.4701 -0.0465 0.0686  90  PHE C CG    
4547 C  CD1   . PHE D 91  ? 1.0136 1.0094 0.4233 -0.4502 -0.0207 0.0644  90  PHE C CD1   
4548 C  CD2   . PHE D 91  ? 1.0930 1.0853 0.4177 -0.4972 -0.0522 0.0687  90  PHE C CD2   
4549 C  CE1   . PHE D 91  ? 1.0368 0.9987 0.4062 -0.4571 -0.0001 0.0607  90  PHE C CE1   
4550 C  CE2   . PHE D 91  ? 1.1338 1.0883 0.4150 -0.5039 -0.0311 0.0646  90  PHE C CE2   
4551 C  CZ    . PHE D 91  ? 1.1017 1.0424 0.4066 -0.4839 -0.0045 0.0604  90  PHE C CZ    
4552 N  N     . GLU D 92  ? 1.0856 1.1114 0.4861 -0.5050 -0.0436 0.0298  91  GLU C N     
4553 C  CA    . GLU D 92  ? 1.0846 1.0725 0.4396 -0.5291 -0.0248 0.0079  91  GLU C CA    
4554 C  C     . GLU D 92  ? 1.0927 1.0672 0.4794 -0.5144 -0.0009 -0.0072 91  GLU C C     
4555 O  O     . GLU D 92  ? 1.1175 1.0480 0.4739 -0.5191 0.0274  -0.0252 91  GLU C O     
4556 C  CB    . GLU D 92  ? 1.1351 1.1394 0.4622 -0.5606 -0.0497 0.0083  91  GLU C CB    
4557 C  CG    . GLU D 92  ? 1.2041 1.2442 0.5306 -0.5650 -0.0835 0.0306  91  GLU C CG    
4558 C  CD    . GLU D 92  ? 1.2085 1.2677 0.5298 -0.5885 -0.1040 0.0336  91  GLU C CD    
4559 O  OE1   . GLU D 92  ? 1.1771 1.2743 0.5368 -0.5880 -0.1175 0.0364  91  GLU C OE1   
4560 O  OE2   . GLU D 92  ? 1.2978 1.3358 0.5782 -0.6071 -0.1064 0.0344  91  GLU C OE2   
4561 N  N     . ASP D 93  ? 0.9771 0.9879 0.4238 -0.4954 -0.0113 0.0004  92  ASP C N     
4562 C  CA    . ASP D 93  ? 0.9958 0.9953 0.4750 -0.4789 0.0094  -0.0113 92  ASP C CA    
4563 C  C     . ASP D 93  ? 1.0043 0.9751 0.4906 -0.4564 0.0379  -0.0168 92  ASP C C     
4564 O  O     . ASP D 93  ? 1.0304 0.9790 0.5273 -0.4467 0.0597  -0.0300 92  ASP C O     
4565 C  CB    . ASP D 93  ? 0.9461 0.9914 0.4894 -0.4601 -0.0070 0.0002  92  ASP C CB    
4566 C  CG    . ASP D 93  ? 0.9285 1.0065 0.4746 -0.4814 -0.0311 0.0029  92  ASP C CG    
4567 O  OD1   . ASP D 93  ? 0.9465 1.0055 0.4459 -0.5116 -0.0315 -0.0080 92  ASP C OD1   
4568 O  OD2   . ASP D 93  ? 0.8544 0.9777 0.4493 -0.4679 -0.0492 0.0158  92  ASP C OD2   
4569 N  N     . ILE D 94  ? 0.9295 0.9015 0.4117 -0.4475 0.0378  -0.0063 93  ILE C N     
4570 C  CA    . ILE D 94  ? 0.9736 0.9259 0.4685 -0.4267 0.0638  -0.0103 93  ILE C CA    
4571 C  C     . ILE D 94  ? 1.0557 0.9617 0.5085 -0.4368 0.0939  -0.0311 93  ILE C C     
4572 O  O     . ILE D 94  ? 0.9984 0.8888 0.4715 -0.4205 0.1164  -0.0416 93  ILE C O     
4573 C  CB    . ILE D 94  ? 0.9599 0.9205 0.4519 -0.4201 0.0575  0.0051  93  ILE C CB    
4574 C  CG1   . ILE D 94  ? 0.8642 0.8659 0.4056 -0.4018 0.0325  0.0251  93  ILE C CG1   
4575 C  CG2   . ILE D 94  ? 0.9457 0.8805 0.4332 -0.4087 0.0878  -0.0022 93  ILE C CG2   
4576 C  CD1   . ILE D 94  ? 0.8074 0.8196 0.4039 -0.3724 0.0422  0.0285  93  ILE C CD1   
4577 N  N     . HIS D 95  ? 1.0402 0.9223 0.4322 -0.4635 0.0947  -0.0373 94  HIS C N     
4578 C  CA    . HIS D 95  ? 1.1492 0.9834 0.4960 -0.4743 0.1238  -0.0584 94  HIS C CA    
4579 C  C     . HIS D 95  ? 1.1970 1.0171 0.5617 -0.4674 0.1359  -0.0721 94  HIS C C     
4580 O  O     . HIS D 95  ? 1.1757 0.9670 0.5418 -0.4532 0.1648  -0.0850 94  HIS C O     
4581 C  CB    . HIS D 95  ? 1.2432 1.0553 0.5211 -0.5091 0.1167  -0.0641 94  HIS C CB    
4582 C  CG    . HIS D 95  ? 1.3395 1.1009 0.5802 -0.5185 0.1422  -0.0869 94  HIS C CG    
4583 N  ND1   . HIS D 95  ? 1.3518 1.0965 0.5785 -0.5332 0.1406  -0.0984 94  HIS C ND1   
4584 C  CD2   . HIS D 95  ? 1.3908 1.1137 0.6094 -0.5140 0.1690  -0.0996 94  HIS C CD2   
4585 C  CE1   . HIS D 95  ? 1.3386 1.0335 0.5351 -0.5365 0.1658  -0.1163 94  HIS C CE1   
4586 N  NE2   . HIS D 95  ? 1.3903 1.0724 0.5819 -0.5243 0.1834  -0.1176 94  HIS C NE2   
4587 N  N     . HIS D 96  ? 1.1356 0.9766 0.5152 -0.4768 0.1140  -0.0688 95  HIS C N     
4588 C  CA    . HIS D 96  ? 1.1498 0.9746 0.5420 -0.4727 0.1247  -0.0811 95  HIS C CA    
4589 C  C     . HIS D 96  ? 1.0760 0.9100 0.5250 -0.4381 0.1377  -0.0785 95  HIS C C     
4590 O  O     . HIS D 96  ? 1.1142 0.9174 0.5633 -0.4275 0.1602  -0.0915 95  HIS C O     
4591 C  CB    . HIS D 96  ? 1.1483 0.9998 0.5490 -0.4907 0.0981  -0.0765 95  HIS C CB    
4592 C  CG    . HIS D 96  ? 1.2327 1.0746 0.5761 -0.5277 0.0848  -0.0804 95  HIS C CG    
4593 N  ND1   . HIS D 96  ? 1.2459 1.0391 0.5331 -0.5513 0.1000  -0.0994 95  HIS C ND1   
4594 C  CD2   . HIS D 96  ? 1.2433 1.1156 0.5739 -0.5454 0.0576  -0.0675 95  HIS C CD2   
4595 C  CE1   . HIS D 96  ? 1.3100 1.1061 0.5578 -0.5819 0.0825  -0.0973 95  HIS C CE1   
4596 N  NE2   . HIS D 96  ? 1.2830 1.1275 0.5510 -0.5808 0.0558  -0.0788 95  HIS C NE2   
4597 N  N     . TYR D 97  ? 1.0368 0.9111 0.5325 -0.4201 0.1232  -0.0615 96  TYR C N     
4598 C  CA    . TYR D 97  ? 1.0324 0.9168 0.5803 -0.3890 0.1338  -0.0581 96  TYR C CA    
4599 C  C     . TYR D 97  ? 1.0379 0.8938 0.5759 -0.3758 0.1637  -0.0671 96  TYR C C     
4600 O  O     . TYR D 97  ? 0.9935 0.8399 0.5583 -0.3550 0.1807  -0.0728 96  TYR C O     
4601 C  CB    . TYR D 97  ? 0.9826 0.9122 0.5747 -0.3756 0.1118  -0.0382 96  TYR C CB    
4602 C  CG    . TYR D 97  ? 0.9254 0.8851 0.5571 -0.3705 0.0928  -0.0314 96  TYR C CG    
4603 C  CD1   . TYR D 97  ? 0.9208 0.9168 0.5625 -0.3786 0.0650  -0.0178 96  TYR C CD1   
4604 C  CD2   . TYR D 97  ? 0.9322 0.8870 0.5951 -0.3546 0.1029  -0.0369 96  TYR C CD2   
4605 C  CE1   . TYR D 97  ? 0.8408 0.8667 0.5197 -0.3738 0.0499  -0.0121 96  TYR C CE1   
4606 C  CE2   . TYR D 97  ? 0.8546 0.8361 0.5516 -0.3509 0.0876  -0.0311 96  TYR C CE2   
4607 C  CZ    . TYR D 97  ? 0.8817 0.9000 0.5880 -0.3602 0.0619  -0.0190 96  TYR C CZ    
4608 O  OH    . TYR D 97  ? 0.8241 0.8718 0.5664 -0.3558 0.0486  -0.0136 96  TYR C OH    
4609 N  N     . ARG D 98  ? 1.0607 0.9034 0.5595 -0.3879 0.1708  -0.0684 97  ARG C N     
4610 C  CA    . ARG D 98  ? 1.0273 0.8486 0.5199 -0.3753 0.2004  -0.0764 97  ARG C CA    
4611 C  C     . ARG D 98  ? 1.0670 0.8443 0.5304 -0.3769 0.2259  -0.0967 97  ARG C C     
4612 O  O     . ARG D 98  ? 1.0577 0.8247 0.5446 -0.3544 0.2480  -0.1032 97  ARG C O     
4613 C  CB    . ARG D 98  ? 1.0381 0.8551 0.4934 -0.3892 0.2030  -0.0728 97  ARG C CB    
4614 C  CG    . ARG D 98  ? 0.9870 0.7908 0.4456 -0.3743 0.2342  -0.0796 97  ARG C CG    
4615 C  CD    . ARG D 98  ? 1.0795 0.8782 0.5013 -0.3881 0.2391  -0.0761 97  ARG C CD    
4616 N  NE    . ARG D 98  ? 1.0444 0.8379 0.4835 -0.3698 0.2656  -0.0822 97  ARG C NE    
4617 C  CZ    . ARG D 98  ? 1.1508 0.9138 0.5612 -0.3714 0.2879  -0.0972 97  ARG C CZ    
4618 N  NH1   . ARG D 98  ? 1.1874 0.9163 0.5479 -0.3908 0.2880  -0.1090 97  ARG C NH1   
4619 N  NH2   . ARG D 98  ? 1.1201 0.8877 0.5541 -0.3534 0.3104  -0.1001 97  ARG C NH2   
4620 N  N     . GLU D 99  ? 1.1325 0.8827 0.5436 -0.4035 0.2226  -0.1064 98  GLU C N     
4621 C  CA    . GLU D 99  ? 1.1078 0.8086 0.4821 -0.4081 0.2460  -0.1264 98  GLU C CA    
4622 C  C     . GLU D 99  ? 1.1696 0.8670 0.5844 -0.3856 0.2522  -0.1295 98  GLU C C     
4623 O  O     . GLU D 99  ? 1.1651 0.8349 0.5817 -0.3670 0.2792  -0.1404 98  GLU C O     
4624 C  CB    . GLU D 99  ? 1.2541 0.9335 0.5715 -0.4435 0.2332  -0.1332 98  GLU C CB    
4625 C  CG    . GLU D 99  ? 1.2915 0.9462 0.5568 -0.4634 0.2379  -0.1391 98  GLU C CG    
4626 C  CD    . GLU D 99  ? 1.2982 0.9209 0.5578 -0.4456 0.2701  -0.1506 98  GLU C CD    
4627 O  OE1   . GLU D 99  ? 1.3073 0.8862 0.5468 -0.4435 0.2895  -0.1660 98  GLU C OE1   
4628 O  OE2   . GLU D 99  ? 1.2603 0.9009 0.5351 -0.4340 0.2761  -0.1439 98  GLU C OE2   
4629 N  N     . GLN D 100 ? 1.0683 0.7956 0.5180 -0.3853 0.2275  -0.1192 99  GLN C N     
4630 C  CA    . GLN D 100 ? 1.0262 0.7472 0.5084 -0.3670 0.2323  -0.1220 99  GLN C CA    
4631 C  C     . GLN D 100 ? 1.0789 0.8150 0.6109 -0.3329 0.2456  -0.1168 99  GLN C C     
4632 O  O     . GLN D 100 ? 1.0892 0.8004 0.6297 -0.3147 0.2643  -0.1252 99  GLN C O     
4633 C  CB    . GLN D 100 ? 1.0800 0.8334 0.5897 -0.3747 0.2041  -0.1116 99  GLN C CB    
4634 C  CG    . GLN D 100 ? 1.1012 0.8580 0.6554 -0.3520 0.2060  -0.1098 99  GLN C CG    
4635 C  CD    . GLN D 100 ? 1.1181 0.8776 0.6713 -0.3684 0.1897  -0.1101 99  GLN C CD    
4636 O  OE1   . GLN D 100 ? 1.0392 0.8399 0.6318 -0.3655 0.1692  -0.0976 99  GLN C OE1   
4637 N  NE2   . GLN D 100 ? 1.2200 0.9343 0.7255 -0.3873 0.1997  -0.1248 99  GLN C NE2   
4638 N  N     . ILE D 101 ? 0.9538 0.7297 0.5184 -0.3240 0.2357  -0.1027 100 ILE C N     
4639 C  CA    . ILE D 101 ? 0.9499 0.7423 0.5612 -0.2946 0.2473  -0.0976 100 ILE C CA    
4640 C  C     . ILE D 101 ? 1.0634 0.8249 0.6551 -0.2847 0.2796  -0.1109 100 ILE C C     
4641 O  O     . ILE D 101 ? 1.0502 0.8052 0.6689 -0.2606 0.2954  -0.1146 100 ILE C O     
4642 C  CB    . ILE D 101 ? 0.9556 0.7909 0.5975 -0.2907 0.2320  -0.0808 100 ILE C CB    
4643 C  CG1   . ILE D 101 ? 0.8773 0.7447 0.5541 -0.2890 0.2044  -0.0676 100 ILE C CG1   
4644 C  CG2   . ILE D 101 ? 0.9082 0.7568 0.5875 -0.2659 0.2483  -0.0778 100 ILE C CG2   
4645 C  CD1   . ILE D 101 ? 0.8623 0.7652 0.5601 -0.2884 0.1863  -0.0513 100 ILE C CD1   
4646 N  N     . LYS D 102 ? 0.9555 0.6981 0.4994 -0.3025 0.2901  -0.1180 101 LYS C N     
4647 C  CA    . LYS D 102 ? 1.0772 0.7890 0.5993 -0.2936 0.3233  -0.1320 101 LYS C CA    
4648 C  C     . LYS D 102 ? 1.1229 0.7897 0.6258 -0.2869 0.3397  -0.1474 101 LYS C C     
4649 O  O     . LYS D 102 ? 1.1710 0.8213 0.6837 -0.2645 0.3657  -0.1556 101 LYS C O     
4650 C  CB    . LYS D 102 ? 1.1270 0.8224 0.5939 -0.3175 0.3311  -0.1376 101 LYS C CB    
4651 C  CG    . LYS D 102 ? 1.0931 0.8272 0.5787 -0.3188 0.3226  -0.1230 101 LYS C CG    
4652 C  CD    . LYS D 102 ? 1.1769 0.8929 0.6171 -0.3356 0.3294  -0.1284 101 LYS C CD    
4653 C  CE    . LYS D 102 ? 1.1889 0.8853 0.5774 -0.3664 0.3104  -0.1308 101 LYS C CE    
4654 N  NZ    . LYS D 102 ? 1.2463 0.9039 0.5883 -0.3774 0.3258  -0.1444 101 LYS C NZ    
4655 N  N     . ARG D 103 ? 1.1156 0.7625 0.5920 -0.3056 0.3250  -0.1509 102 ARG C N     
4656 C  CA    . ARG D 103 ? 1.1191 0.7208 0.5776 -0.2996 0.3386  -0.1639 102 ARG C CA    
4657 C  C     . ARG D 103 ? 1.1224 0.7397 0.6386 -0.2670 0.3403  -0.1575 102 ARG C C     
4658 O  O     . ARG D 103 ? 1.1295 0.7297 0.6558 -0.2423 0.3647  -0.1642 102 ARG C O     
4659 C  CB    . ARG D 103 ? 1.2062 0.7910 0.6311 -0.3284 0.3191  -0.1665 102 ARG C CB    
4660 C  CG    . ARG D 103 ? 1.2328 0.7575 0.6190 -0.3307 0.3355  -0.1827 102 ARG C CG    
4661 C  CD    . ARG D 103 ? 1.1917 0.7120 0.5665 -0.3531 0.3134  -0.1813 102 ARG C CD    
4662 N  NE    . ARG D 103 ? 1.2817 0.8078 0.6992 -0.3319 0.3091  -0.1756 102 ARG C NE    
4663 C  CZ    . ARG D 103 ? 1.2667 0.7598 0.6914 -0.3053 0.3299  -0.1820 102 ARG C CZ    
4664 N  NH1   . ARG D 103 ? 1.2533 0.7030 0.6461 -0.2950 0.3588  -0.1956 102 ARG C NH1   
4665 N  NH2   . ARG D 103 ? 1.2003 0.7043 0.6650 -0.2878 0.3217  -0.1742 102 ARG C NH2   
4666 N  N     . VAL D 104 ? 1.1354 0.7873 0.6903 -0.2663 0.3142  -0.1441 103 VAL C N     
4667 C  CA    . VAL D 104 ? 0.9722 0.6328 0.5735 -0.2404 0.3122  -0.1384 103 VAL C CA    
4668 C  C     . VAL D 104 ? 1.0436 0.7220 0.6853 -0.2094 0.3290  -0.1353 103 VAL C C     
4669 O  O     . VAL D 104 ? 1.0687 0.7300 0.7271 -0.1856 0.3420  -0.1387 103 VAL C O     
4670 C  CB    . VAL D 104 ? 1.0333 0.7349 0.6701 -0.2460 0.2820  -0.1234 103 VAL C CB    
4671 C  CG1   . VAL D 104 ? 1.0165 0.7248 0.6972 -0.2208 0.2800  -0.1176 103 VAL C CG1   
4672 C  CG2   . VAL D 104 ? 1.0762 0.7649 0.6765 -0.2769 0.2660  -0.1266 103 VAL C CG2   
4673 N  N     . LYS D 105 ? 1.0027 0.7160 0.6606 -0.2097 0.3285  -0.1281 104 LYS C N     
4674 C  CA    . LYS D 105 ? 1.0020 0.7365 0.6969 -0.1846 0.3452  -0.1255 104 LYS C CA    
4675 C  C     . LYS D 105 ? 1.0717 0.7711 0.7373 -0.1760 0.3787  -0.1411 104 LYS C C     
4676 O  O     . LYS D 105 ? 1.0788 0.7924 0.7775 -0.1511 0.3959  -0.1409 104 LYS C O     
4677 C  CB    . LYS D 105 ? 1.0137 0.7924 0.7285 -0.1917 0.3349  -0.1134 104 LYS C CB    
4678 C  CG    . LYS D 105 ? 0.8690 0.6813 0.6088 -0.2003 0.3031  -0.0980 104 LYS C CG    
4679 C  CD    . LYS D 105 ? 0.8998 0.7333 0.6907 -0.1791 0.2934  -0.0892 104 LYS C CD    
4680 C  CE    . LYS D 105 ? 0.8278 0.6926 0.6624 -0.1589 0.3023  -0.0824 104 LYS C CE    
4681 N  NZ    . LYS D 105 ? 0.8073 0.6874 0.6875 -0.1385 0.2928  -0.0749 104 LYS C NZ    
4682 N  N     . ASP D 106 ? 1.0435 0.6993 0.6487 -0.1961 0.3887  -0.1547 105 ASP C N     
4683 C  CA    . ASP D 106 ? 1.1711 0.7892 0.7421 -0.1893 0.4225  -0.1709 105 ASP C CA    
4684 C  C     . ASP D 106 ? 1.1940 0.8457 0.7867 -0.1805 0.4385  -0.1680 105 ASP C C     
4685 O  O     . ASP D 106 ? 1.1597 0.8181 0.7833 -0.1531 0.4569  -0.1699 105 ASP C O     
4686 C  CB    . ASP D 106 ? 1.1784 0.7630 0.7577 -0.1617 0.4399  -0.1790 105 ASP C CB    
4687 C  CG    . ASP D 106 ? 1.2653 0.8071 0.8129 -0.1528 0.4671  -0.1931 105 ASP C CG    
4688 O  OD1   . ASP D 106 ? 1.3392 0.8399 0.8310 -0.1762 0.4678  -0.2023 105 ASP C OD1   
4689 O  OD2   . ASP D 106 ? 1.2193 0.7729 0.8030 -0.1220 0.4840  -0.1925 105 ASP C OD2   
4690 N  N     . SER D 107 ? 1.1769 0.8538 0.7600 -0.2030 0.4247  -0.1603 106 SER C N     
4691 C  CA    . SER D 107 ? 1.1922 0.8936 0.7867 -0.2007 0.4335  -0.1572 106 SER C CA    
4692 C  C     . SER D 107 ? 1.2328 0.9314 0.7843 -0.2329 0.4185  -0.1547 106 SER C C     
4693 O  O     . SER D 107 ? 1.2291 0.9233 0.7579 -0.2541 0.3972  -0.1509 106 SER C O     
4694 C  CB    . SER D 107 ? 1.0997 0.8566 0.7582 -0.1833 0.4298  -0.1428 106 SER C CB    
4695 O  OG    . SER D 107 ? 0.9881 0.7649 0.6610 -0.1758 0.4441  -0.1424 106 SER C OG    
4696 N  N     . GLU D 108 ? 1.2599 0.9624 0.8007 -0.2364 0.4292  -0.1563 107 GLU C N     
4697 C  CA    . GLU D 108 ? 1.2837 0.9886 0.7889 -0.2647 0.4137  -0.1513 107 GLU C CA    
4698 C  C     . GLU D 108 ? 1.2396 0.9928 0.7793 -0.2672 0.3944  -0.1328 107 GLU C C     
4699 O  O     . GLU D 108 ? 1.2568 1.0154 0.7742 -0.2891 0.3714  -0.1243 107 GLU C O     
4700 C  CB    . GLU D 108 ? 1.3265 1.0112 0.8009 -0.2695 0.4331  -0.1607 107 GLU C CB    
4701 C  CG    . GLU D 108 ? 1.3317 0.9620 0.7475 -0.2851 0.4397  -0.1757 107 GLU C CG    
4702 C  CD    . GLU D 108 ? 1.3678 0.9872 0.7419 -0.3172 0.4126  -0.1721 107 GLU C CD    
4703 O  OE1   . GLU D 108 ? 1.4224 1.0581 0.7820 -0.3351 0.3983  -0.1635 107 GLU C OE1   
4704 O  OE2   . GLU D 108 ? 1.3806 0.9755 0.7362 -0.3248 0.4048  -0.1773 107 GLU C OE2   
4705 N  N     . ASP D 109 ? 1.1733 0.9616 0.7671 -0.2453 0.4015  -0.1256 108 ASP C N     
4706 C  CA    . ASP D 109 ? 1.1510 0.9811 0.7763 -0.2481 0.3836  -0.1080 108 ASP C CA    
4707 C  C     . ASP D 109 ? 1.0494 0.9066 0.7276 -0.2308 0.3750  -0.0992 108 ASP C C     
4708 O  O     . ASP D 109 ? 1.0343 0.9089 0.7555 -0.2078 0.3888  -0.1000 108 ASP C O     
4709 C  CB    . ASP D 109 ? 1.1707 1.0203 0.8071 -0.2451 0.3958  -0.1051 108 ASP C CB    
4710 C  CG    . ASP D 109 ? 1.1381 1.0074 0.8213 -0.2180 0.4183  -0.1089 108 ASP C CG    
4711 O  OD1   . ASP D 109 ? 1.1544 1.0136 0.8540 -0.1996 0.4293  -0.1168 108 ASP C OD1   
4712 O  OD2   . ASP D 109 ? 1.1700 1.0662 0.8737 -0.2153 0.4244  -0.1032 108 ASP C OD2   
4713 N  N     . VAL D 110 ? 1.0182 0.8795 0.6940 -0.2418 0.3506  -0.0906 109 VAL C N     
4714 C  CA    . VAL D 110 ? 0.9577 0.8458 0.6863 -0.2259 0.3305  -0.0792 109 VAL C CA    
4715 C  C     . VAL D 110 ? 0.8799 0.8006 0.6278 -0.2322 0.3123  -0.0622 109 VAL C C     
4716 O  O     . VAL D 110 ? 0.9096 0.8253 0.6218 -0.2526 0.3040  -0.0579 109 VAL C O     
4717 C  CB    . VAL D 110 ? 0.9186 0.7904 0.6371 -0.2306 0.3106  -0.0805 109 VAL C CB    
4718 C  CG1   . VAL D 110 ? 0.9160 0.7799 0.5921 -0.2573 0.2915  -0.0769 109 VAL C CG1   
4719 C  CG2   . VAL D 110 ? 0.8367 0.7350 0.6065 -0.2154 0.2905  -0.0688 109 VAL C CG2   
4720 N  N     . PRO D 111 ? 0.8255 0.7768 0.6248 -0.2163 0.3063  -0.0523 110 PRO C N     
4721 C  CA    . PRO D 111 ? 0.7759 0.7516 0.5891 -0.2232 0.2870  -0.0360 110 PRO C CA    
4722 C  C     . PRO D 111 ? 0.7159 0.6857 0.5090 -0.2361 0.2587  -0.0284 110 PRO C C     
4723 O  O     . PRO D 111 ? 0.7566 0.7239 0.5616 -0.2302 0.2455  -0.0291 110 PRO C O     
4724 C  CB    . PRO D 111 ? 0.7911 0.7942 0.6616 -0.2030 0.2830  -0.0291 110 PRO C CB    
4725 C  CG    . PRO D 111 ? 0.7462 0.7455 0.6332 -0.1856 0.3075  -0.0413 110 PRO C CG    
4726 C  CD    . PRO D 111 ? 0.8030 0.7661 0.6476 -0.1915 0.3173  -0.0553 110 PRO C CD    
4727 N  N     . MET D 112 ? 0.7333 0.7025 0.4970 -0.2536 0.2490  -0.0203 111 MET C N     
4728 C  CA    . MET D 112 ? 0.7539 0.7153 0.4898 -0.2678 0.2255  -0.0155 111 MET C CA    
4729 C  C     . MET D 112 ? 0.7666 0.7333 0.4815 -0.2815 0.2114  -0.0016 111 MET C C     
4730 O  O     . MET D 112 ? 0.8199 0.7820 0.5155 -0.2895 0.2259  -0.0014 111 MET C O     
4731 C  CB    . MET D 112 ? 0.8362 0.7685 0.5275 -0.2806 0.2359  -0.0304 111 MET C CB    
4732 C  CG    . MET D 112 ? 0.9144 0.8393 0.5734 -0.2983 0.2136  -0.0276 111 MET C CG    
4733 S  SD    . MET D 112 ? 0.9747 0.8654 0.5985 -0.3072 0.2262  -0.0477 111 MET C SD    
4734 C  CE    . MET D 112 ? 0.8428 0.7502 0.5156 -0.2906 0.2097  -0.0441 111 MET C CE    
4735 N  N     . VAL D 113 ? 0.7739 0.7492 0.4900 -0.2846 0.1835  0.0099  112 VAL C N     
4736 C  CA    . VAL D 113 ? 0.8348 0.8141 0.5329 -0.2943 0.1664  0.0254  112 VAL C CA    
4737 C  C     . VAL D 113 ? 0.8211 0.8013 0.4986 -0.3042 0.1401  0.0316  112 VAL C C     
4738 O  O     . VAL D 113 ? 0.7834 0.7776 0.4886 -0.2950 0.1246  0.0341  112 VAL C O     
4739 C  CB    . VAL D 113 ? 0.8073 0.8046 0.5448 -0.2803 0.1579  0.0388  112 VAL C CB    
4740 C  CG1   . VAL D 113 ? 0.7831 0.7793 0.4995 -0.2887 0.1390  0.0555  112 VAL C CG1   
4741 C  CG2   . VAL D 113 ? 0.7262 0.7274 0.4837 -0.2737 0.1821  0.0341  112 VAL C CG2   
4742 N  N     . LEU D 114 ? 0.7921 0.7600 0.4225 -0.3231 0.1341  0.0353  113 LEU C N     
4743 C  CA    . LEU D 114 ? 0.8385 0.8123 0.4502 -0.3331 0.1066  0.0438  113 LEU C CA    
4744 C  C     . LEU D 114 ? 0.8188 0.8088 0.4471 -0.3247 0.0826  0.0644  113 LEU C C     
4745 O  O     . LEU D 114 ? 0.8331 0.8165 0.4527 -0.3247 0.0856  0.0737  113 LEU C O     
4746 C  CB    . LEU D 114 ? 0.8572 0.8100 0.4076 -0.3580 0.1083  0.0399  113 LEU C CB    
4747 C  CG    . LEU D 114 ? 0.8779 0.8371 0.4017 -0.3728 0.0798  0.0478  113 LEU C CG    
4748 C  CD1   . LEU D 114 ? 0.8707 0.8352 0.4014 -0.3767 0.0755  0.0365  113 LEU C CD1   
4749 C  CD2   . LEU D 114 ? 0.9426 0.8791 0.4017 -0.3975 0.0806  0.0484  113 LEU C CD2   
4750 N  N     . VAL D 115 ? 0.7537 0.7634 0.4023 -0.3186 0.0588  0.0716  114 VAL C N     
4751 C  CA    . VAL D 115 ? 0.7350 0.7604 0.4043 -0.3062 0.0362  0.0904  114 VAL C CA    
4752 C  C     . VAL D 115 ? 0.7750 0.8134 0.4264 -0.3148 0.0086  0.1002  114 VAL C C     
4753 O  O     . VAL D 115 ? 0.7433 0.7989 0.4085 -0.3162 -0.0007 0.0952  114 VAL C O     
4754 C  CB    . VAL D 115 ? 0.6804 0.7234 0.4047 -0.2840 0.0349  0.0908  114 VAL C CB    
4755 C  CG1   . VAL D 115 ? 0.6669 0.7192 0.4091 -0.2696 0.0159  0.1096  114 VAL C CG1   
4756 C  CG2   . VAL D 115 ? 0.6615 0.6954 0.4037 -0.2774 0.0608  0.0793  114 VAL C CG2   
4757 N  N     . GLY D 116 ? 0.7892 0.8207 0.4109 -0.3208 -0.0051 0.1150  115 GLY C N     
4758 C  CA    . GLY D 116 ? 0.8037 0.8537 0.4182 -0.3233 -0.0350 0.1282  115 GLY C CA    
4759 C  C     . GLY D 116 ? 0.7725 0.8417 0.4267 -0.2995 -0.0530 0.1444  115 GLY C C     
4760 O  O     . GLY D 116 ? 0.7837 0.8395 0.4305 -0.2915 -0.0569 0.1580  115 GLY C O     
4761 N  N     . ASN D 117 ? 0.7388 0.8373 0.4318 -0.2887 -0.0641 0.1434  116 ASN C N     
4762 C  CA    . ASN D 117 ? 0.7097 0.8251 0.4431 -0.2638 -0.0768 0.1563  116 ASN C CA    
4763 C  C     . ASN D 117 ? 0.7243 0.8649 0.4583 -0.2596 -0.1071 0.1731  116 ASN C C     
4764 O  O     . ASN D 117 ? 0.7544 0.9057 0.4625 -0.2773 -0.1204 0.1740  116 ASN C O     
4765 C  CB    . ASN D 117 ? 0.6916 0.8229 0.4725 -0.2508 -0.0666 0.1450  116 ASN C CB    
4766 C  CG    . ASN D 117 ? 0.6599 0.8043 0.4815 -0.2244 -0.0757 0.1564  116 ASN C CG    
4767 O  OD1   . ASN D 117 ? 0.6294 0.7549 0.4496 -0.2129 -0.0735 0.1657  116 ASN C OD1   
4768 N  ND2   . ASN D 117 ? 0.6427 0.8188 0.4990 -0.2158 -0.0852 0.1553  116 ASN C ND2   
4769 N  N     . LYS D 118 ? 0.7055 0.8555 0.4703 -0.2350 -0.1177 0.1864  117 LYS C N     
4770 C  CA    . LYS D 118 ? 0.7184 0.8917 0.4924 -0.2219 -0.1455 0.2054  117 LYS C CA    
4771 C  C     . LYS D 118 ? 0.7704 0.9215 0.4990 -0.2275 -0.1589 0.2218  117 LYS C C     
4772 O  O     . LYS D 118 ? 0.7944 0.9651 0.5179 -0.2240 -0.1844 0.2370  117 LYS C O     
4773 C  CB    . LYS D 118 ? 0.7128 0.9295 0.5036 -0.2291 -0.1619 0.2032  117 LYS C CB    
4774 C  CG    . LYS D 118 ? 0.6660 0.9027 0.4980 -0.2256 -0.1486 0.1873  117 LYS C CG    
4775 C  CD    . LYS D 118 ? 0.6618 0.9431 0.5122 -0.2333 -0.1650 0.1864  117 LYS C CD    
4776 C  CE    . LYS D 118 ? 0.6209 0.9168 0.5056 -0.2335 -0.1501 0.1699  117 LYS C CE    
4777 N  NZ    . LYS D 118 ? 0.6168 0.9626 0.5254 -0.2391 -0.1685 0.1721  117 LYS C NZ    
4778 N  N     . CYS D 119 ? 0.7893 0.9010 0.4862 -0.2354 -0.1427 0.2201  118 CYS C N     
4779 C  CA    . CYS D 119 ? 0.8445 0.9316 0.4919 -0.2442 -0.1544 0.2354  118 CYS C CA    
4780 C  C     . CYS D 119 ? 0.8600 0.9456 0.5146 -0.2199 -0.1765 0.2589  118 CYS C C     
4781 O  O     . CYS D 119 ? 0.9091 0.9686 0.5211 -0.2247 -0.1868 0.2739  118 CYS C O     
4782 C  CB    . CYS D 119 ? 0.8608 0.9071 0.4755 -0.2578 -0.1296 0.2282  118 CYS C CB    
4783 S  SG    . CYS D 119 ? 0.9443 0.9657 0.5841 -0.2367 -0.1136 0.2315  118 CYS C SG    
4784 N  N     . ASP D 120 ? 0.8251 0.9344 0.5285 -0.1939 -0.1836 0.2629  119 ASP C N     
4785 C  CA    . ASP D 120 ? 0.8439 0.9552 0.5553 -0.1687 -0.2057 0.2849  119 ASP C CA    
4786 C  C     . ASP D 120 ? 0.8819 1.0301 0.5924 -0.1683 -0.2357 0.2978  119 ASP C C     
4787 O  O     . ASP D 120 ? 0.9009 1.0449 0.6020 -0.1518 -0.2570 0.3191  119 ASP C O     
4788 C  CB    . ASP D 120 ? 0.8014 0.9243 0.5652 -0.1396 -0.2007 0.2839  119 ASP C CB    
4789 C  CG    . ASP D 120 ? 0.7523 0.9212 0.5631 -0.1385 -0.1970 0.2690  119 ASP C CG    
4790 O  OD1   . ASP D 120 ? 0.7409 0.9058 0.5598 -0.1509 -0.1754 0.2502  119 ASP C OD1   
4791 O  OD2   . ASP D 120 ? 0.7528 0.9625 0.5918 -0.1261 -0.2159 0.2766  119 ASP C OD2   
4792 N  N     . LEU D 121 ? 0.8534 1.0367 0.5722 -0.1864 -0.2383 0.2861  120 LEU C N     
4793 C  CA    . LEU D 121 ? 0.9127 1.1402 0.6403 -0.1862 -0.2671 0.2972  120 LEU C CA    
4794 C  C     . LEU D 121 ? 1.0236 1.2337 0.6963 -0.1989 -0.2879 0.3142  120 LEU C C     
4795 O  O     . LEU D 121 ? 1.0359 1.2077 0.6586 -0.2221 -0.2760 0.3087  120 LEU C O     
4796 C  CB    . LEU D 121 ? 0.9158 1.1785 0.6586 -0.2080 -0.2625 0.2786  120 LEU C CB    
4797 C  CG    . LEU D 121 ? 0.8049 1.0929 0.6049 -0.1938 -0.2478 0.2651  120 LEU C CG    
4798 C  CD1   . LEU D 121 ? 0.7681 1.0827 0.5747 -0.2188 -0.2419 0.2465  120 LEU C CD1   
4799 C  CD2   . LEU D 121 ? 0.7700 1.0942 0.6170 -0.1621 -0.2654 0.2802  120 LEU C CD2   
4800 N  N     . PRO D 122 ? 1.0515 1.2889 0.7319 -0.1835 -0.3188 0.3356  121 PRO C N     
4801 C  CA    . PRO D 122 ? 1.1384 1.3588 0.7718 -0.1948 -0.3356 0.3464  121 PRO C CA    
4802 C  C     . PRO D 122 ? 1.1538 1.3905 0.7631 -0.2295 -0.3380 0.3333  121 PRO C C     
4803 O  O     . PRO D 122 ? 1.1997 1.4095 0.7604 -0.2469 -0.3420 0.3353  121 PRO C O     
4804 C  CB    . PRO D 122 ? 1.1394 1.3887 0.8065 -0.1622 -0.3604 0.3639  121 PRO C CB    
4805 C  CG    . PRO D 122 ? 1.0159 1.3184 0.7497 -0.1455 -0.3601 0.3586  121 PRO C CG    
4806 C  CD    . PRO D 122 ? 0.9535 1.2354 0.6924 -0.1516 -0.3336 0.3455  121 PRO C CD    
4807 N  N     . SER D 123 ? 1.1258 1.4047 0.7676 -0.2397 -0.3357 0.3199  122 SER C N     
4808 C  CA    . SER D 123 ? 1.1193 1.4075 0.7366 -0.2747 -0.3334 0.3042  122 SER C CA    
4809 C  C     . SER D 123 ? 1.1479 1.3937 0.7249 -0.2992 -0.3052 0.2871  122 SER C C     
4810 O  O     . SER D 123 ? 1.1076 1.3354 0.7047 -0.2866 -0.2822 0.2788  122 SER C O     
4811 C  CB    . SER D 123 ? 1.1325 1.4784 0.8000 -0.2763 -0.3391 0.2953  122 SER C CB    
4812 O  OG    . SER D 123 ? 1.0432 1.4032 0.7547 -0.2585 -0.3269 0.2911  122 SER C OG    
4813 N  N     . ARG D 124 ? 1.1214 1.3466 0.6507 -0.3297 -0.3003 0.2767  123 ARG C N     
4814 C  CA    . ARG D 124 ? 1.0651 1.2549 0.5573 -0.3547 -0.2718 0.2567  123 ARG C CA    
4815 C  C     . ARG D 124 ? 1.0846 1.2811 0.5514 -0.3858 -0.2736 0.2427  123 ARG C C     
4816 O  O     . ARG D 124 ? 1.1241 1.3269 0.5742 -0.3928 -0.2931 0.2515  123 ARG C O     
4817 C  CB    . ARG D 124 ? 1.0859 1.2207 0.5318 -0.3576 -0.2565 0.2599  123 ARG C CB    
4818 C  CG    . ARG D 124 ? 1.1045 1.2175 0.5710 -0.3361 -0.2369 0.2613  123 ARG C CG    
4819 C  CD    . ARG D 124 ? 1.0823 1.1422 0.4990 -0.3501 -0.2127 0.2563  123 ARG C CD    
4820 N  NE    . ARG D 124 ? 1.0684 1.1152 0.4775 -0.3685 -0.1815 0.2305  123 ARG C NE    
4821 C  CZ    . ARG D 124 ? 1.0642 1.0895 0.4871 -0.3625 -0.1510 0.2181  123 ARG C CZ    
4822 N  NH1   . ARG D 124 ? 1.0217 1.0356 0.4667 -0.3409 -0.1466 0.2278  123 ARG C NH1   
4823 N  NH2   . ARG D 124 ? 1.0836 1.0983 0.4975 -0.3785 -0.1245 0.1956  123 ARG C NH2   
4824 N  N     . THR D 125 ? 1.0608 1.2547 0.5239 -0.4040 -0.2537 0.2213  124 THR C N     
4825 C  CA    . THR D 125 ? 1.0981 1.2842 0.5271 -0.4360 -0.2499 0.2058  124 THR C CA    
4826 C  C     . THR D 125 ? 1.1273 1.2630 0.5099 -0.4554 -0.2172 0.1860  124 THR C C     
4827 O  O     . THR D 125 ? 1.1649 1.2783 0.5056 -0.4808 -0.2120 0.1757  124 THR C O     
4828 C  CB    . THR D 125 ? 1.0703 1.2984 0.5344 -0.4439 -0.2561 0.1959  124 THR C CB    
4829 O  OG1   . THR D 125 ? 1.0156 1.2492 0.5098 -0.4338 -0.2389 0.1851  124 THR C OG1   
4830 C  CG2   . THR D 125 ? 1.0625 1.3432 0.5710 -0.4277 -0.2873 0.2142  124 THR C CG2   
4831 N  N     . VAL D 126 ? 1.0837 1.2010 0.4739 -0.4432 -0.1942 0.1807  125 VAL C N     
4832 C  CA    . VAL D 126 ? 1.0977 1.1694 0.4544 -0.4547 -0.1592 0.1624  125 VAL C CA    
4833 C  C     . VAL D 126 ? 1.1168 1.1590 0.4536 -0.4448 -0.1535 0.1749  125 VAL C C     
4834 O  O     . VAL D 126 ? 1.1078 1.1544 0.4818 -0.4189 -0.1514 0.1845  125 VAL C O     
4835 C  CB    . VAL D 126 ? 1.0415 1.1137 0.4444 -0.4407 -0.1315 0.1438  125 VAL C CB    
4836 C  CG1   . VAL D 126 ? 1.0597 1.0889 0.4293 -0.4527 -0.0957 0.1241  125 VAL C CG1   
4837 C  CG2   . VAL D 126 ? 1.0202 1.1243 0.4501 -0.4474 -0.1404 0.1344  125 VAL C CG2   
4838 N  N     . ASP D 127 ? 1.1727 1.1837 0.4636 -0.4616 -0.1490 0.1721  126 ASP C N     
4839 C  CA    . ASP D 127 ? 1.1948 1.1739 0.4654 -0.4549 -0.1395 0.1804  126 ASP C CA    
4840 C  C     . ASP D 127 ? 1.1643 1.1230 0.4451 -0.4478 -0.1043 0.1680  126 ASP C C     
4841 O  O     . ASP D 127 ? 1.1517 1.1045 0.4332 -0.4563 -0.0805 0.1474  126 ASP C O     
4842 C  CB    . ASP D 127 ? 1.2630 1.2111 0.4801 -0.4772 -0.1375 0.1763  126 ASP C CB    
4843 C  CG    . ASP D 127 ? 1.2996 1.2657 0.5050 -0.4846 -0.1717 0.1901  126 ASP C CG    
4844 O  OD1   . ASP D 127 ? 1.2773 1.2765 0.5161 -0.4663 -0.1987 0.2083  126 ASP C OD1   
4845 O  OD2   . ASP D 127 ? 1.3516 1.3001 0.5164 -0.5082 -0.1711 0.1824  126 ASP C OD2   
4846 N  N     . THR D 128 ? 1.1553 1.1022 0.4454 -0.4314 -0.1008 0.1807  127 THR C N     
4847 C  CA    . THR D 128 ? 1.1405 1.0641 0.4353 -0.4273 -0.0673 0.1703  127 THR C CA    
4848 C  C     . THR D 128 ? 1.1762 1.0733 0.4368 -0.4476 -0.0406 0.1481  127 THR C C     
4849 O  O     . THR D 128 ? 1.1535 1.0454 0.4280 -0.4467 -0.0114 0.1300  127 THR C O     
4850 C  CB    . THR D 128 ? 1.1527 1.0586 0.4444 -0.4153 -0.0709 0.1873  127 THR C CB    
4851 O  OG1   . THR D 128 ? 1.1283 1.0548 0.4485 -0.3949 -0.0977 0.2086  127 THR C OG1   
4852 C  CG2   . THR D 128 ? 1.1299 1.0198 0.4374 -0.4096 -0.0380 0.1773  127 THR C CG2   
4853 N  N     . LYS D 129 ? 1.2345 1.1151 0.4514 -0.4646 -0.0514 0.1500  128 LYS C N     
4854 C  CA    . LYS D 129 ? 1.2787 1.1310 0.4575 -0.4846 -0.0285 0.1306  128 LYS C CA    
4855 C  C     . LYS D 129 ? 1.2653 1.1213 0.4494 -0.4929 -0.0118 0.1083  128 LYS C C     
4856 O  O     . LYS D 129 ? 1.2699 1.1066 0.4492 -0.4956 0.0200  0.0889  128 LYS C O     
4857 C  CB    . LYS D 129 ? 1.3427 1.1820 0.4759 -0.5025 -0.0495 0.1389  128 LYS C CB    
4858 C  CG    . LYS D 129 ? 1.3999 1.2061 0.4866 -0.5247 -0.0292 0.1219  128 LYS C CG    
4859 C  CD    . LYS D 129 ? 1.4022 1.1853 0.4867 -0.5211 0.0049  0.1111  128 LYS C CD    
4860 C  CE    . LYS D 129 ? 1.4689 1.2187 0.5029 -0.5434 0.0216  0.0973  128 LYS C CE    
4861 N  NZ    . LYS D 129 ? 1.5035 1.2468 0.5089 -0.5637 0.0165  0.0852  128 LYS C NZ    
4862 N  N     . GLN D 130 ? 1.2522 1.1324 0.4464 -0.4965 -0.0331 0.1104  129 GLN C N     
4863 C  CA    . GLN D 130 ? 1.2439 1.1241 0.4404 -0.5055 -0.0185 0.0894  129 GLN C CA    
4864 C  C     . GLN D 130 ? 1.1926 1.0751 0.4263 -0.4883 0.0093  0.0782  129 GLN C C     
4865 O  O     . GLN D 130 ? 1.2006 1.0628 0.4275 -0.4921 0.0380  0.0570  129 GLN C O     
4866 C  CB    . GLN D 130 ? 1.2335 1.1445 0.4411 -0.5117 -0.0471 0.0949  129 GLN C CB    
4867 C  CG    . GLN D 130 ? 1.2842 1.2028 0.4652 -0.5273 -0.0790 0.1078  129 GLN C CG    
4868 C  CD    . GLN D 130 ? 1.2540 1.2164 0.4651 -0.5254 -0.1099 0.1178  129 GLN C CD    
4869 O  OE1   . GLN D 130 ? 1.2495 1.2380 0.4766 -0.5149 -0.1391 0.1394  129 GLN C OE1   
4870 N  NE2   . GLN D 130 ? 1.2353 1.2067 0.4584 -0.5331 -0.1020 0.1018  129 GLN C NE2   
4871 N  N     . ALA D 131 ? 1.1727 1.0795 0.4474 -0.4682 0.0009  0.0926  130 ALA C N     
4872 C  CA    . ALA D 131 ? 1.1035 1.0152 0.4184 -0.4513 0.0256  0.0839  130 ALA C CA    
4873 C  C     . ALA D 131 ? 1.1026 0.9915 0.4176 -0.4453 0.0559  0.0750  130 ALA C C     
4874 O  O     . ALA D 131 ? 1.0739 0.9596 0.4123 -0.4366 0.0828  0.0595  130 ALA C O     
4875 C  CB    . ALA D 131 ? 1.0334 0.9763 0.4058 -0.4263 0.0067  0.0995  130 ALA C CB    
4876 N  N     . GLN D 132 ? 1.1725 1.0468 0.4634 -0.4492 0.0520  0.0846  131 GLN C N     
4877 C  CA    . GLN D 132 ? 1.1437 0.9983 0.4314 -0.4470 0.0813  0.0741  131 GLN C CA    
4878 C  C     . GLN D 132 ? 1.1817 1.0141 0.4409 -0.4603 0.1041  0.0510  131 GLN C C     
4879 O  O     . GLN D 132 ? 1.1682 0.9958 0.4460 -0.4518 0.1334  0.0352  131 GLN C O     
4880 C  CB    . GLN D 132 ? 1.1757 1.0176 0.4411 -0.4502 0.0724  0.0893  131 GLN C CB    
4881 C  CG    . GLN D 132 ? 1.1495 1.0059 0.4361 -0.4369 0.0484  0.1134  131 GLN C CG    
4882 C  CD    . GLN D 132 ? 1.1943 1.0322 0.4486 -0.4425 0.0349  0.1293  131 GLN C CD    
4883 O  OE1   . GLN D 132 ? 1.2483 1.0692 0.4588 -0.4595 0.0284  0.1282  131 GLN C OE1   
4884 N  NE2   . GLN D 132 ? 1.1750 1.0135 0.4499 -0.4287 0.0315  0.1436  131 GLN C NE2   
4885 N  N     . ASP D 133 ? 1.2305 1.0496 0.4461 -0.4805 0.0905  0.0489  132 ASP C N     
4886 C  CA    . ASP D 133 ? 1.2740 1.0669 0.4578 -0.4947 0.1114  0.0271  132 ASP C CA    
4887 C  C     . ASP D 133 ? 1.2626 1.0575 0.4681 -0.4882 0.1279  0.0094  132 ASP C C     
4888 O  O     . ASP D 133 ? 1.2679 1.0415 0.4648 -0.4883 0.1564  -0.0098 132 ASP C O     
4889 C  CB    . ASP D 133 ? 1.3305 1.1104 0.4656 -0.5188 0.0898  0.0303  132 ASP C CB    
4890 C  CG    . ASP D 133 ? 1.3655 1.1373 0.4746 -0.5254 0.0765  0.0462  132 ASP C CG    
4891 O  OD1   . ASP D 133 ? 1.3694 1.1307 0.4809 -0.5188 0.0964  0.0447  132 ASP C OD1   
4892 O  OD2   . ASP D 133 ? 1.3896 1.1667 0.4776 -0.5365 0.0462  0.0604  132 ASP C OD2   
4893 N  N     . LEU D 134 ? 1.2043 1.0237 0.4381 -0.4815 0.1112  0.0159  133 LEU C N     
4894 C  CA    . LEU D 134 ? 1.1768 0.9973 0.4339 -0.4737 0.1271  0.0003  133 LEU C CA    
4895 C  C     . LEU D 134 ? 1.1454 0.9718 0.4460 -0.4499 0.1535  -0.0046 133 LEU C C     
4896 O  O     . LEU D 134 ? 1.1856 0.9960 0.4905 -0.4438 0.1808  -0.0230 133 LEU C O     
4897 C  CB    . LEU D 134 ? 1.1448 0.9931 0.4227 -0.4733 0.1018  0.0099  133 LEU C CB    
4898 C  CG    . LEU D 134 ? 1.1210 0.9681 0.4149 -0.4706 0.1132  -0.0056 133 LEU C CG    
4899 C  CD1   . LEU D 134 ? 1.1773 0.9914 0.4276 -0.4900 0.1231  -0.0249 133 LEU C CD1   
4900 C  CD2   . LEU D 134 ? 1.0818 0.9618 0.4034 -0.4685 0.0870  0.0057  133 LEU C CD2   
4901 N  N     . ALA D 135 ? 1.0937 0.9429 0.4281 -0.4358 0.1450  0.0121  134 ALA C N     
4902 C  CA    . ALA D 135 ? 1.0654 0.9236 0.4444 -0.4146 0.1677  0.0083  134 ALA C CA    
4903 C  C     . ALA D 135 ? 1.1257 0.9637 0.4906 -0.4146 0.1963  -0.0055 134 ALA C C     
4904 O  O     . ALA D 135 ? 1.0866 0.9231 0.4756 -0.4014 0.2215  -0.0194 134 ALA C O     
4905 C  CB    . ALA D 135 ? 1.0132 0.8943 0.4249 -0.4026 0.1531  0.0290  134 ALA C CB    
4906 N  N     . ARG D 136 ? 1.1354 0.9572 0.4598 -0.4296 0.1929  -0.0022 135 ARG C N     
4907 C  CA    . ARG D 136 ? 1.1680 0.9736 0.4806 -0.4299 0.2206  -0.0140 135 ARG C CA    
4908 C  C     . ARG D 136 ? 1.2297 1.0132 0.5264 -0.4322 0.2435  -0.0365 135 ARG C C     
4909 O  O     . ARG D 136 ? 1.2476 1.0283 0.5614 -0.4203 0.2721  -0.0485 135 ARG C O     
4910 C  CB    . ARG D 136 ? 1.2343 1.0241 0.5022 -0.4480 0.2112  -0.0058 135 ARG C CB    
4911 C  CG    . ARG D 136 ? 1.2814 1.0527 0.5295 -0.4526 0.2393  -0.0177 135 ARG C CG    
4912 C  CD    . ARG D 136 ? 1.3303 1.0928 0.5472 -0.4660 0.2288  -0.0045 135 ARG C CD    
4913 N  NE    . ARG D 136 ? 1.3656 1.1199 0.5460 -0.4823 0.1967  0.0081  135 ARG C NE    
4914 C  CZ    . ARG D 136 ? 1.3502 1.1183 0.5388 -0.4798 0.1689  0.0291  135 ARG C CZ    
4915 N  NH1   . ARG D 136 ? 1.2915 1.0782 0.5194 -0.4637 0.1691  0.0401  135 ARG C NH1   
4916 N  NH2   . ARG D 136 ? 1.3575 1.1209 0.5150 -0.4934 0.1398  0.0398  135 ARG C NH2   
4917 N  N     . SER D 137 ? 1.2234 0.9911 0.4875 -0.4474 0.2310  -0.0420 136 SER C N     
4918 C  CA    . SER D 137 ? 1.2541 0.9956 0.5009 -0.4499 0.2520  -0.0633 136 SER C CA    
4919 C  C     . SER D 137 ? 1.2261 0.9783 0.5206 -0.4255 0.2720  -0.0719 136 SER C C     
4920 O  O     . SER D 137 ? 1.2257 0.9644 0.5252 -0.4153 0.3012  -0.0864 136 SER C O     
4921 C  CB    . SER D 137 ? 1.2878 1.0155 0.4996 -0.4702 0.2315  -0.0659 136 SER C CB    
4922 O  OG    . SER D 137 ? 1.2312 0.9833 0.4723 -0.4641 0.2118  -0.0573 136 SER C OG    
4923 N  N     . TYR D 138 ? 1.1537 0.9314 0.4850 -0.4152 0.2564  -0.0622 137 TYR C N     
4924 C  CA    . TYR D 138 ? 1.1110 0.8991 0.4877 -0.3928 0.2722  -0.0687 137 TYR C CA    
4925 C  C     . TYR D 138 ? 1.0912 0.8989 0.5104 -0.3723 0.2907  -0.0660 137 TYR C C     
4926 O  O     . TYR D 138 ? 1.0784 0.8914 0.5323 -0.3529 0.3094  -0.0741 137 TYR C O     
4927 C  CB    . TYR D 138 ? 1.0991 0.9104 0.5039 -0.3888 0.2495  -0.0576 137 TYR C CB    
4928 C  CG    . TYR D 138 ? 1.1155 0.9180 0.4865 -0.4093 0.2270  -0.0572 137 TYR C CG    
4929 C  CD1   . TYR D 138 ? 1.1396 0.9084 0.4621 -0.4273 0.2325  -0.0721 137 TYR C CD1   
4930 C  CD2   . TYR D 138 ? 1.0800 0.9094 0.4722 -0.4097 0.2012  -0.0426 137 TYR C CD2   
4931 C  CE1   . TYR D 138 ? 1.1577 0.9220 0.4525 -0.4477 0.2104  -0.0716 137 TYR C CE1   
4932 C  CE2   . TYR D 138 ? 1.0849 0.9129 0.4514 -0.4284 0.1802  -0.0418 137 TYR C CE2   
4933 C  CZ    . TYR D 138 ? 1.1484 0.9449 0.4668 -0.4478 0.1842  -0.0564 137 TYR C CZ    
4934 O  OH    . TYR D 138 ? 1.2138 1.0130 0.5098 -0.4680 0.1612  -0.0551 137 TYR C OH    
4935 N  N     . GLY D 139 ? 1.0844 0.9033 0.5022 -0.3763 0.2856  -0.0545 138 GLY C N     
4936 C  CA    . GLY D 139 ? 1.0536 0.8953 0.5149 -0.3587 0.3003  -0.0505 138 GLY C CA    
4937 C  C     . GLY D 139 ? 1.0236 0.8964 0.5388 -0.3424 0.2887  -0.0384 138 GLY C C     
4938 O  O     . GLY D 139 ? 1.0033 0.8930 0.5627 -0.3233 0.3045  -0.0419 138 GLY C O     
4939 N  N     . ILE D 140 ? 0.9799 0.8614 0.4927 -0.3494 0.2608  -0.0234 139 ILE C N     
4940 C  CA    . ILE D 140 ? 0.9278 0.8366 0.4886 -0.3357 0.2479  -0.0103 139 ILE C CA    
4941 C  C     . ILE D 140 ? 0.9078 0.8232 0.4582 -0.3445 0.2231  0.0094  139 ILE C C     
4942 O  O     . ILE D 140 ? 0.9479 0.8477 0.4535 -0.3615 0.2120  0.0134  139 ILE C O     
4943 C  CB    . ILE D 140 ? 0.8797 0.7921 0.4567 -0.3303 0.2400  -0.0135 139 ILE C CB    
4944 C  CG1   . ILE D 140 ? 0.9289 0.8269 0.4615 -0.3501 0.2206  -0.0121 139 ILE C CG1   
4945 C  CG2   . ILE D 140 ? 0.8783 0.7835 0.4722 -0.3169 0.2656  -0.0312 139 ILE C CG2   
4946 C  CD1   . ILE D 140 ? 0.8704 0.7844 0.4275 -0.3455 0.1963  -0.0049 139 ILE C CD1   
4947 N  N     . PRO D 141 ? 0.8625 0.7987 0.4529 -0.3328 0.2146  0.0219  140 PRO C N     
4948 C  CA    . PRO D 141 ? 0.8640 0.8023 0.4440 -0.3390 0.1918  0.0414  140 PRO C CA    
4949 C  C     . PRO D 141 ? 0.8676 0.8043 0.4264 -0.3479 0.1656  0.0509  140 PRO C C     
4950 O  O     . PRO D 141 ? 0.8510 0.7928 0.4202 -0.3449 0.1621  0.0440  140 PRO C O     
4951 C  CB    . PRO D 141 ? 0.8758 0.8349 0.5069 -0.3228 0.1905  0.0499  140 PRO C CB    
4952 C  CG    . PRO D 141 ? 0.8638 0.8328 0.5280 -0.3102 0.2162  0.0350  140 PRO C CG    
4953 C  CD    . PRO D 141 ? 0.8472 0.8018 0.4881 -0.3143 0.2310  0.0177  140 PRO C CD    
4954 N  N     . PHE D 142 ? 0.8908 0.8214 0.4221 -0.3572 0.1453  0.0670  141 PHE C N     
4955 C  CA    . PHE D 142 ? 0.8897 0.8262 0.4118 -0.3598 0.1146  0.0800  141 PHE C CA    
4956 C  C     . PHE D 142 ? 0.8899 0.8333 0.4306 -0.3487 0.0950  0.1002  141 PHE C C     
4957 O  O     . PHE D 142 ? 0.8955 0.8256 0.4161 -0.3554 0.1001  0.1092  141 PHE C O     
4958 C  CB    . PHE D 142 ? 0.9475 0.8669 0.4091 -0.3824 0.1047  0.0814  141 PHE C CB    
4959 C  CG    . PHE D 142 ? 0.9493 0.8797 0.4065 -0.3818 0.0684  0.0977  141 PHE C CG    
4960 C  CD1   . PHE D 142 ? 0.9085 0.8627 0.4052 -0.3685 0.0519  0.0972  141 PHE C CD1   
4961 C  CD2   . PHE D 142 ? 1.0006 0.9189 0.4161 -0.3933 0.0509  0.1142  141 PHE C CD2   
4962 C  CE1   . PHE D 142 ? 0.9096 0.8795 0.4073 -0.3662 0.0195  0.1124  141 PHE C CE1   
4963 C  CE2   . PHE D 142 ? 1.0019 0.9334 0.4167 -0.3900 0.0171  0.1302  141 PHE C CE2   
4964 C  CZ    . PHE D 142 ? 0.9655 0.9251 0.4239 -0.3757 0.0016  0.1293  141 PHE C CZ    
4965 N  N     . ILE D 143 ? 0.8336 0.7955 0.4104 -0.3325 0.0738  0.1069  142 ILE C N     
4966 C  CA    . ILE D 143 ? 0.8236 0.7907 0.4210 -0.3186 0.0549  0.1249  142 ILE C CA    
4967 C  C     . ILE D 143 ? 0.8243 0.8065 0.4281 -0.3118 0.0252  0.1345  142 ILE C C     
4968 O  O     . ILE D 143 ? 0.7836 0.7836 0.4113 -0.3067 0.0217  0.1255  142 ILE C O     
4969 C  CB    . ILE D 143 ? 0.8425 0.8209 0.4919 -0.2997 0.0639  0.1228  142 ILE C CB    
4970 C  CG1   . ILE D 143 ? 0.8522 0.8256 0.5080 -0.3040 0.0940  0.1118  142 ILE C CG1   
4971 C  CG2   . ILE D 143 ? 0.8242 0.7996 0.4847 -0.2876 0.0459  0.1413  142 ILE C CG2   
4972 C  CD1   . ILE D 143 ? 0.8341 0.8127 0.4972 -0.3061 0.1149  0.0918  142 ILE C CD1   
4973 N  N     . GLU D 144 ? 0.9170 0.8926 0.4998 -0.3115 0.0038  0.1531  143 GLU C N     
4974 C  CA    . GLU D 144 ? 0.8647 0.8595 0.4636 -0.2994 -0.0251 0.1652  143 GLU C CA    
4975 C  C     . GLU D 144 ? 0.8106 0.8139 0.4554 -0.2750 -0.0298 0.1723  143 GLU C C     
4976 O  O     . GLU D 144 ? 0.7920 0.7769 0.4351 -0.2704 -0.0229 0.1792  143 GLU C O     
4977 C  CB    . GLU D 144 ? 0.8770 0.8612 0.4328 -0.3076 -0.0475 0.1831  143 GLU C CB    
4978 C  CG    . GLU D 144 ? 0.9228 0.9155 0.4476 -0.3259 -0.0590 0.1794  143 GLU C CG    
4979 C  CD    . GLU D 144 ? 1.0233 0.9927 0.4887 -0.3429 -0.0693 0.1921  143 GLU C CD    
4980 O  OE1   . GLU D 144 ? 1.0715 1.0205 0.5240 -0.3371 -0.0721 0.2068  143 GLU C OE1   
4981 O  OE2   . GLU D 144 ? 1.0641 1.0321 0.4918 -0.3637 -0.0741 0.1875  143 GLU C OE2   
4982 N  N     . THR D 145 ? 0.7490 0.7789 0.4323 -0.2609 -0.0408 0.1703  144 THR C N     
4983 C  CA    . THR D 145 ? 0.7136 0.7511 0.4379 -0.2378 -0.0457 0.1766  144 THR C CA    
4984 C  C     . THR D 145 ? 0.7438 0.8020 0.4831 -0.2230 -0.0727 0.1904  144 THR C C     
4985 O  O     . THR D 145 ? 0.7332 0.8066 0.4573 -0.2309 -0.0892 0.1945  144 THR C O     
4986 C  CB    . THR D 145 ? 0.7533 0.8039 0.5175 -0.2311 -0.0293 0.1602  144 THR C CB    
4987 O  OG1   . THR D 145 ? 0.6551 0.7298 0.4298 -0.2343 -0.0369 0.1528  144 THR C OG1   
4988 C  CG2   . THR D 145 ? 0.6905 0.7252 0.4438 -0.2436 -0.0023 0.1465  144 THR C CG2   
4989 N  N     . SER D 146 ? 0.7077 0.7671 0.4779 -0.2011 -0.0768 0.1976  145 SER C N     
4990 C  CA    . SER D 146 ? 0.6771 0.7621 0.4751 -0.1823 -0.0973 0.2071  145 SER C CA    
4991 C  C     . SER D 146 ? 0.6807 0.7699 0.5209 -0.1644 -0.0872 0.2010  145 SER C C     
4992 O  O     . SER D 146 ? 0.6467 0.7112 0.4865 -0.1550 -0.0815 0.2064  145 SER C O     
4993 C  CB    . SER D 146 ? 0.7140 0.7875 0.4935 -0.1708 -0.1178 0.2287  145 SER C CB    
4994 O  OG    . SER D 146 ? 0.6958 0.7950 0.5117 -0.1475 -0.1329 0.2363  145 SER C OG    
4995 N  N     . ALA D 147 ? 0.5987 0.7160 0.4710 -0.1622 -0.0844 0.1893  146 ALA C N     
4996 C  CA    . ALA D 147 ? 0.5617 0.6861 0.4737 -0.1434 -0.0791 0.1860  146 ALA C CA    
4997 C  C     . ALA D 147 ? 0.6370 0.7631 0.5614 -0.1201 -0.0950 0.2022  146 ALA C C     
4998 O  O     . ALA D 147 ? 0.6912 0.8023 0.6314 -0.1050 -0.0885 0.2033  146 ALA C O     
4999 C  CB    . ALA D 147 ? 0.5295 0.6847 0.4699 -0.1463 -0.0760 0.1727  146 ALA C CB    
5000 N  N     . LYS D 148 ? 0.6694 0.8129 0.5862 -0.1165 -0.1158 0.2150  147 LYS C N     
5001 C  CA    . LYS D 148 ? 0.6487 0.7977 0.5813 -0.0908 -0.1311 0.2305  147 LYS C CA    
5002 C  C     . LYS D 148 ? 0.6820 0.7861 0.5927 -0.0804 -0.1284 0.2414  147 LYS C C     
5003 O  O     . LYS D 148 ? 0.6321 0.7266 0.5615 -0.0587 -0.1274 0.2457  147 LYS C O     
5004 C  CB    . LYS D 148 ? 0.6396 0.8166 0.5658 -0.0898 -0.1553 0.2436  147 LYS C CB    
5005 C  CG    . LYS D 148 ? 0.6472 0.8306 0.5884 -0.0610 -0.1722 0.2615  147 LYS C CG    
5006 C  CD    . LYS D 148 ? 0.6889 0.9190 0.6422 -0.0592 -0.1952 0.2705  147 LYS C CD    
5007 C  CE    . LYS D 148 ? 0.6902 0.9220 0.6466 -0.0314 -0.2158 0.2927  147 LYS C CE    
5008 N  NZ    . LYS D 148 ? 0.6895 0.9792 0.6750 -0.0241 -0.2370 0.3004  147 LYS C NZ    
5009 N  N     . THR D 149 ? 0.6636 0.7376 0.5322 -0.0969 -0.1263 0.2456  148 THR C N     
5010 C  CA    . THR D 149 ? 0.7192 0.7472 0.5615 -0.0929 -0.1219 0.2550  148 THR C CA    
5011 C  C     . THR D 149 ? 0.6911 0.6962 0.5289 -0.1074 -0.0983 0.2418  148 THR C C     
5012 O  O     . THR D 149 ? 0.7361 0.7033 0.5511 -0.1086 -0.0928 0.2482  148 THR C O     
5013 C  CB    . THR D 149 ? 0.7461 0.7530 0.5411 -0.1033 -0.1344 0.2697  148 THR C CB    
5014 O  OG1   . THR D 149 ? 0.7486 0.7560 0.5203 -0.1316 -0.1236 0.2589  148 THR C OG1   
5015 C  CG2   . THR D 149 ? 0.7693 0.8010 0.5657 -0.0898 -0.1613 0.2855  148 THR C CG2   
5016 N  N     . ARG D 150 ? 0.7165 0.7433 0.5724 -0.1200 -0.0850 0.2243  149 ARG C N     
5017 C  CA    . ARG D 150 ? 0.7195 0.7341 0.5774 -0.1332 -0.0628 0.2105  149 ARG C CA    
5018 C  C     . ARG D 150 ? 0.7813 0.7739 0.5995 -0.1556 -0.0537 0.2107  149 ARG C C     
5019 O  O     . ARG D 150 ? 0.7240 0.7044 0.5422 -0.1652 -0.0358 0.2026  149 ARG C O     
5020 C  CB    . ARG D 150 ? 0.7208 0.7166 0.5962 -0.1201 -0.0552 0.2106  149 ARG C CB    
5021 C  CG    . ARG D 150 ? 0.7124 0.7093 0.6045 -0.1297 -0.0349 0.1951  149 ARG C CG    
5022 C  CD    . ARG D 150 ? 0.7658 0.7532 0.6819 -0.1158 -0.0302 0.1931  149 ARG C CD    
5023 N  NE    . ARG D 150 ? 0.6905 0.6896 0.6305 -0.1218 -0.0149 0.1781  149 ARG C NE    
5024 C  CZ    . ARG D 150 ? 0.6972 0.6922 0.6303 -0.1381 -0.0006 0.1710  149 ARG C CZ    
5025 N  NH1   . ARG D 150 ? 0.6430 0.6218 0.5447 -0.1525 0.0023  0.1766  149 ARG C NH1   
5026 N  NH2   . ARG D 150 ? 0.6304 0.6382 0.5884 -0.1398 0.0112  0.1586  149 ARG C NH2   
5027 N  N     . GLN D 151 ? 0.7833 0.7727 0.5677 -0.1653 -0.0650 0.2194  150 GLN C N     
5028 C  CA    . GLN D 151 ? 0.7932 0.7616 0.5373 -0.1879 -0.0546 0.2188  150 GLN C CA    
5029 C  C     . GLN D 151 ? 0.7694 0.7522 0.5193 -0.2045 -0.0349 0.1996  150 GLN C C     
5030 O  O     . GLN D 151 ? 0.7578 0.7654 0.5198 -0.2063 -0.0377 0.1908  150 GLN C O     
5031 C  CB    . GLN D 151 ? 0.8580 0.8204 0.5629 -0.1944 -0.0730 0.2325  150 GLN C CB    
5032 C  CG    . GLN D 151 ? 0.9209 0.8552 0.5759 -0.2174 -0.0644 0.2354  150 GLN C CG    
5033 C  CD    . GLN D 151 ? 1.0683 1.0023 0.6843 -0.2271 -0.0826 0.2458  150 GLN C CD    
5034 O  OE1   . GLN D 151 ? 1.1243 1.0497 0.7275 -0.2152 -0.1043 0.2640  150 GLN C OE1   
5035 N  NE2   . GLN D 151 ? 1.0876 1.0284 0.6818 -0.2487 -0.0738 0.2347  150 GLN C NE2   
5036 N  N     . GLY D 152 ? 0.7648 0.7319 0.5061 -0.2167 -0.0143 0.1930  151 GLY C N     
5037 C  CA    . GLY D 152 ? 0.7357 0.7125 0.4782 -0.2315 0.0065  0.1759  151 GLY C CA    
5038 C  C     . GLY D 152 ? 0.6808 0.6802 0.4671 -0.2225 0.0166  0.1607  151 GLY C C     
5039 O  O     . GLY D 152 ? 0.6350 0.6412 0.4234 -0.2320 0.0340  0.1464  151 GLY C O     
5040 N  N     . VAL D 153 ? 0.6704 0.6802 0.4898 -0.2043 0.0068  0.1631  152 VAL C N     
5041 C  CA    . VAL D 153 ? 0.6071 0.6362 0.4643 -0.1968 0.0157  0.1492  152 VAL C CA    
5042 C  C     . VAL D 153 ? 0.6119 0.6370 0.4794 -0.2028 0.0377  0.1392  152 VAL C C     
5043 O  O     . VAL D 153 ? 0.6075 0.6416 0.4798 -0.2091 0.0519  0.1259  152 VAL C O     
5044 C  CB    . VAL D 153 ? 0.6470 0.6839 0.5353 -0.1768 0.0036  0.1543  152 VAL C CB    
5045 C  CG1   . VAL D 153 ? 0.5115 0.5656 0.4351 -0.1705 0.0125  0.1407  152 VAL C CG1   
5046 C  CG2   . VAL D 153 ? 0.6681 0.7152 0.5505 -0.1694 -0.0181 0.1647  152 VAL C CG2   
5047 N  N     . ASP D 154 ? 0.6034 0.6147 0.4734 -0.2011 0.0410  0.1459  153 ASP C N     
5048 C  CA    . ASP D 154 ? 0.5908 0.6049 0.4774 -0.2058 0.0600  0.1375  153 ASP C CA    
5049 C  C     . ASP D 154 ? 0.6083 0.6235 0.4755 -0.2221 0.0774  0.1295  153 ASP C C     
5050 O  O     . ASP D 154 ? 0.5858 0.6142 0.4721 -0.2226 0.0935  0.1171  153 ASP C O     
5051 C  CB    . ASP D 154 ? 0.5679 0.5652 0.4535 -0.2060 0.0593  0.1472  153 ASP C CB    
5052 C  CG    . ASP D 154 ? 0.6032 0.5985 0.5122 -0.1891 0.0475  0.1513  153 ASP C CG    
5053 O  OD1   . ASP D 154 ? 0.5285 0.5414 0.4671 -0.1788 0.0477  0.1426  153 ASP C OD1   
5054 O  OD2   . ASP D 154 ? 0.6407 0.6141 0.5367 -0.1865 0.0392  0.1629  153 ASP C OD2   
5055 N  N     . ASP D 155 ? 0.6421 0.6423 0.4697 -0.2347 0.0748  0.1368  154 ASP C N     
5056 C  CA    . ASP D 155 ? 0.6583 0.6561 0.4606 -0.2515 0.0920  0.1296  154 ASP C CA    
5057 C  C     . ASP D 155 ? 0.6183 0.6299 0.4280 -0.2510 0.1010  0.1142  154 ASP C C     
5058 O  O     . ASP D 155 ? 0.6253 0.6432 0.4416 -0.2555 0.1222  0.1025  154 ASP C O     
5059 C  CB    . ASP D 155 ? 0.6783 0.6558 0.4325 -0.2640 0.0823  0.1411  154 ASP C CB    
5060 C  CG    . ASP D 155 ? 0.8142 0.7840 0.5360 -0.2838 0.1018  0.1353  154 ASP C CG    
5061 O  OD1   . ASP D 155 ? 0.8393 0.8212 0.5792 -0.2864 0.1241  0.1227  154 ASP C OD1   
5062 O  OD2   . ASP D 155 ? 0.8143 0.7664 0.4921 -0.2962 0.0950  0.1435  154 ASP C OD2   
5063 N  N     . ALA D 156 ? 0.6273 0.6432 0.4347 -0.2459 0.0854  0.1142  155 ALA C N     
5064 C  CA    . ALA D 156 ? 0.6452 0.6701 0.4565 -0.2468 0.0925  0.0997  155 ALA C CA    
5065 C  C     . ALA D 156 ? 0.6027 0.6387 0.4504 -0.2374 0.1096  0.0870  155 ALA C C     
5066 O  O     . ALA D 156 ? 0.5826 0.6177 0.4247 -0.2426 0.1286  0.0745  155 ALA C O     
5067 C  CB    . ALA D 156 ? 0.5968 0.6302 0.4123 -0.2405 0.0709  0.1032  155 ALA C CB    
5068 N  N     . PHE D 157 ? 0.5697 0.6151 0.4536 -0.2228 0.1029  0.0902  156 PHE C N     
5069 C  CA    . PHE D 157 ? 0.5191 0.5755 0.4374 -0.2127 0.1152  0.0796  156 PHE C CA    
5070 C  C     . PHE D 157 ? 0.5409 0.6012 0.4705 -0.2150 0.1341  0.0769  156 PHE C C     
5071 O  O     . PHE D 157 ? 0.4968 0.5650 0.4435 -0.2105 0.1500  0.0659  156 PHE C O     
5072 C  CB    . PHE D 157 ? 0.4708 0.5350 0.4213 -0.1977 0.1016  0.0842  156 PHE C CB    
5073 C  CG    . PHE D 157 ? 0.4723 0.5409 0.4248 -0.1927 0.0869  0.0834  156 PHE C CG    
5074 C  CD1   . PHE D 157 ? 0.4454 0.5195 0.4124 -0.1881 0.0919  0.0721  156 PHE C CD1   
5075 C  CD2   . PHE D 157 ? 0.4735 0.5415 0.4161 -0.1914 0.0680  0.0947  156 PHE C CD2   
5076 C  CE1   . PHE D 157 ? 0.4382 0.5182 0.4074 -0.1859 0.0790  0.0715  156 PHE C CE1   
5077 C  CE2   . PHE D 157 ? 0.4594 0.5375 0.4084 -0.1869 0.0547  0.0944  156 PHE C CE2   
5078 C  CZ    . PHE D 157 ? 0.4432 0.5281 0.4059 -0.1854 0.0607  0.0825  156 PHE C CZ    
5079 N  N     . TYR D 158 ? 0.5256 0.5813 0.4478 -0.2212 0.1321  0.0874  157 TYR C N     
5080 C  CA    . TYR D 158 ? 0.5536 0.6169 0.4866 -0.2265 0.1500  0.0855  157 TYR C CA    
5081 C  C     . TYR D 158 ? 0.5779 0.6398 0.4882 -0.2377 0.1702  0.0765  157 TYR C C     
5082 O  O     . TYR D 158 ? 0.5439 0.6190 0.4740 -0.2335 0.1887  0.0667  157 TYR C O     
5083 C  CB    . TYR D 158 ? 0.5542 0.6085 0.4769 -0.2346 0.1435  0.0989  157 TYR C CB    
5084 C  CG    . TYR D 158 ? 0.5396 0.5925 0.4840 -0.2243 0.1278  0.1070  157 TYR C CG    
5085 C  CD1   . TYR D 158 ? 0.4939 0.5547 0.4648 -0.2087 0.1189  0.1029  157 TYR C CD1   
5086 C  CD2   . TYR D 158 ? 0.5752 0.6161 0.5109 -0.2315 0.1231  0.1183  157 TYR C CD2   
5087 C  CE1   . TYR D 158 ? 0.5168 0.5740 0.5042 -0.1998 0.1059  0.1097  157 TYR C CE1   
5088 C  CE2   . TYR D 158 ? 0.5640 0.5987 0.5148 -0.2227 0.1099  0.1249  157 TYR C CE2   
5089 C  CZ    . TYR D 158 ? 0.5380 0.5813 0.5147 -0.2067 0.1017  0.1205  157 TYR C CZ    
5090 O  OH    . TYR D 158 ? 0.5499 0.5848 0.5388 -0.1982 0.0898  0.1264  157 TYR C OH    
5091 N  N     . THR D 159 ? 0.6039 0.6490 0.4720 -0.2500 0.1659  0.0798  158 THR C N     
5092 C  CA    . THR D 159 ? 0.6747 0.7137 0.5156 -0.2599 0.1837  0.0697  158 THR C CA    
5093 C  C     . THR D 159 ? 0.6044 0.6503 0.4615 -0.2512 0.1962  0.0548  158 THR C C     
5094 O  O     . THR D 159 ? 0.6156 0.6655 0.4771 -0.2487 0.2169  0.0437  158 THR C O     
5095 C  CB    . THR D 159 ? 0.7062 0.7253 0.4971 -0.2748 0.1733  0.0753  158 THR C CB    
5096 O  OG1   . THR D 159 ? 0.6748 0.6832 0.4480 -0.2814 0.1612  0.0903  158 THR C OG1   
5097 C  CG2   . THR D 159 ? 0.7208 0.7302 0.4819 -0.2833 0.1907  0.0623  158 THR C CG2   
5098 N  N     . LEU D 160 ? 0.6309 0.6777 0.5022 -0.2403 0.1805  0.0539  159 LEU C N     
5099 C  CA    . LEU D 160 ? 0.6143 0.6626 0.4991 -0.2309 0.1902  0.0401  159 LEU C CA    
5100 C  C     . LEU D 160 ? 0.5589 0.6238 0.4843 -0.2178 0.2052  0.0352  159 LEU C C     
5101 O  O     . LEU D 160 ? 0.5675 0.6320 0.4959 -0.2133 0.2248  0.0231  159 LEU C O     
5102 C  CB    . LEU D 160 ? 0.5981 0.6449 0.4898 -0.2240 0.1700  0.0413  159 LEU C CB    
5103 C  CG    . LEU D 160 ? 0.6313 0.6719 0.5253 -0.2185 0.1782  0.0273  159 LEU C CG    
5104 C  CD1   . LEU D 160 ? 0.6655 0.6884 0.5200 -0.2310 0.1942  0.0162  159 LEU C CD1   
5105 C  CD2   . LEU D 160 ? 0.5925 0.6338 0.4911 -0.2155 0.1575  0.0299  159 LEU C CD2   
5106 N  N     . VAL D 161 ? 0.5845 0.6635 0.5415 -0.2106 0.1955  0.0445  160 VAL C N     
5107 C  CA    . VAL D 161 ? 0.5121 0.6111 0.5080 -0.2006 0.2076  0.0421  160 VAL C CA    
5108 C  C     . VAL D 161 ? 0.5919 0.6987 0.5826 -0.2072 0.2277  0.0390  160 VAL C C     
5109 O  O     . VAL D 161 ? 0.5636 0.6860 0.5794 -0.1970 0.2436  0.0317  160 VAL C O     
5110 C  CB    . VAL D 161 ? 0.5143 0.6237 0.5367 -0.1965 0.1917  0.0537  160 VAL C CB    
5111 C  CG1   . VAL D 161 ? 0.4490 0.5822 0.5079 -0.1911 0.2034  0.0529  160 VAL C CG1   
5112 C  CG2   . VAL D 161 ? 0.4688 0.5736 0.5039 -0.1848 0.1732  0.0551  160 VAL C CG2   
5113 N  N     . ARG D 162 ? 0.5468 0.6437 0.5078 -0.2207 0.2242  0.0457  161 ARG C N     
5114 C  CA    . ARG D 162 ? 0.6372 0.7397 0.5913 -0.2252 0.2416  0.0418  161 ARG C CA    
5115 C  C     . ARG D 162 ? 0.6469 0.7389 0.5784 -0.2258 0.2603  0.0278  161 ARG C C     
5116 O  O     . ARG D 162 ? 0.6893 0.7913 0.6267 -0.2236 0.2792  0.0214  161 ARG C O     
5117 C  CB    . ARG D 162 ? 0.6014 0.6926 0.5268 -0.2402 0.2339  0.0522  161 ARG C CB    
5118 C  CG    . ARG D 162 ? 0.5957 0.6975 0.5449 -0.2396 0.2232  0.0636  161 ARG C CG    
5119 C  CD    . ARG D 162 ? 0.6095 0.6943 0.5255 -0.2545 0.2172  0.0730  161 ARG C CD    
5120 N  NE    . ARG D 162 ? 0.5957 0.6764 0.5206 -0.2553 0.2005  0.0853  161 ARG C NE    
5121 C  CZ    . ARG D 162 ? 0.6142 0.6725 0.5137 -0.2598 0.1827  0.0953  161 ARG C CZ    
5122 N  NH1   . ARG D 162 ? 0.6186 0.6617 0.4873 -0.2635 0.1766  0.0955  161 ARG C NH1   
5123 N  NH2   . ARG D 162 ? 0.5995 0.6501 0.5034 -0.2609 0.1704  0.1060  161 ARG C NH2   
5124 N  N     . GLU D 163 ? 0.6220 0.6939 0.5271 -0.2291 0.2559  0.0226  162 GLU C N     
5125 C  CA    . GLU D 163 ? 0.6407 0.6994 0.5255 -0.2283 0.2755  0.0074  162 GLU C CA    
5126 C  C     . GLU D 163 ? 0.6867 0.7561 0.6077 -0.2095 0.2881  -0.0020 162 GLU C C     
5127 O  O     . GLU D 163 ? 0.6912 0.7578 0.6105 -0.2027 0.3097  -0.0138 162 GLU C O     
5128 C  CB    . GLU D 163 ? 0.6897 0.7212 0.5290 -0.2410 0.2672  0.0040  162 GLU C CB    
5129 C  CG    . GLU D 163 ? 0.7396 0.7568 0.5353 -0.2601 0.2546  0.0127  162 GLU C CG    
5130 C  CD    . GLU D 163 ? 0.7467 0.7493 0.5055 -0.2705 0.2716  0.0046  162 GLU C CD    
5131 O  OE1   . GLU D 163 ? 0.7810 0.7631 0.5068 -0.2767 0.2814  -0.0074 162 GLU C OE1   
5132 O  OE2   . GLU D 163 ? 0.7550 0.7655 0.5167 -0.2736 0.2752  0.0103  162 GLU C OE2   
5133 N  N     . ILE D 164 ? 0.6818 0.7614 0.6344 -0.2000 0.2753  0.0030  163 ILE C N     
5134 C  CA    . ILE D 164 ? 0.6533 0.7439 0.6427 -0.1806 0.2857  -0.0040 163 ILE C CA    
5135 C  C     . ILE D 164 ? 0.6793 0.7986 0.7037 -0.1709 0.2978  -0.0027 163 ILE C C     
5136 O  O     . ILE D 164 ? 0.7663 0.8903 0.8028 -0.1582 0.3177  -0.0125 163 ILE C O     
5137 C  CB    . ILE D 164 ? 0.6557 0.7479 0.6690 -0.1698 0.2624  0.0019  163 ILE C CB    
5138 C  CG1   . ILE D 164 ? 0.6550 0.7244 0.6344 -0.1800 0.2446  0.0032  163 ILE C CG1   
5139 C  CG2   . ILE D 164 ? 0.6125 0.7069 0.6541 -0.1492 0.2701  -0.0056 163 ILE C CG2   
5140 C  CD1   . ILE D 164 ? 0.6446 0.7202 0.6402 -0.1775 0.2190  0.0143  163 ILE C CD1   
5141 N  N     . ARG D 165 ? 0.6973 0.8352 0.7362 -0.1768 0.2861  0.0094  164 ARG C N     
5142 C  CA    . ARG D 165 ? 0.6651 0.8339 0.7371 -0.1703 0.2956  0.0117  164 ARG C CA    
5143 C  C     . ARG D 165 ? 0.7002 0.8691 0.7560 -0.1719 0.3189  0.0027  164 ARG C C     
5144 O  O     . ARG D 165 ? 0.6504 0.8427 0.7357 -0.1587 0.3343  -0.0020 164 ARG C O     
5145 C  CB    . ARG D 165 ? 0.6123 0.7937 0.6918 -0.1811 0.2797  0.0259  164 ARG C CB    
5146 C  CG    . ARG D 165 ? 0.5851 0.7721 0.6890 -0.1766 0.2594  0.0344  164 ARG C CG    
5147 C  CD    . ARG D 165 ? 0.5537 0.7657 0.6850 -0.1793 0.2526  0.0447  164 ARG C CD    
5148 N  NE    . ARG D 165 ? 0.5378 0.7475 0.6824 -0.1787 0.2315  0.0535  164 ARG C NE    
5149 C  CZ    . ARG D 165 ? 0.5369 0.7383 0.6713 -0.1899 0.2180  0.0641  164 ARG C CZ    
5150 N  NH1   . ARG D 165 ? 0.5259 0.7208 0.6376 -0.2030 0.2222  0.0677  164 ARG C NH1   
5151 N  NH2   . ARG D 165 ? 0.5219 0.7180 0.6665 -0.1880 0.2005  0.0705  164 ARG C NH2   
5152 N  N     . LYS D 166 ? 0.7262 0.8699 0.7351 -0.1875 0.3213  0.0003  165 LYS C N     
5153 C  CA    . LYS D 166 ? 0.7668 0.9096 0.7578 -0.1910 0.3430  -0.0076 165 LYS C CA    
5154 C  C     . LYS D 166 ? 0.7695 0.9014 0.7576 -0.1771 0.3639  -0.0233 165 LYS C C     
5155 O  O     . LYS D 166 ? 0.8798 1.0216 0.8726 -0.1712 0.3849  -0.0305 165 LYS C O     
5156 C  CB    . LYS D 166 ? 0.7616 0.8779 0.7001 -0.2124 0.3386  -0.0055 165 LYS C CB    
5157 N  N     . HIS D 167 ? 0.8419 0.9521 0.8217 -0.1714 0.3591  -0.0287 166 HIS C N     
5158 C  CA    . HIS D 167 ? 0.8865 0.9794 0.8611 -0.1571 0.3783  -0.0435 166 HIS C CA    
5159 C  C     . HIS D 167 ? 0.8801 0.9919 0.9036 -0.1332 0.3802  -0.0439 166 HIS C C     
5160 O  O     . HIS D 167 ? 0.9518 1.0469 0.9735 -0.1181 0.3956  -0.0554 166 HIS C O     
5161 C  CB    . HIS D 167 ? 0.9053 0.9562 0.8316 -0.1682 0.3737  -0.0506 166 HIS C CB    
5162 N  N     . LYS D 168 ? 0.7961 0.9392 0.8608 -0.1293 0.3645  -0.0317 167 LYS C N     
5163 C  CA    . LYS D 168 ? 0.7661 0.9246 0.8745 -0.1084 0.3614  -0.0304 167 LYS C CA    
5164 C  C     . LYS D 168 ? 0.7414 0.9304 0.8874 -0.0889 0.3780  -0.0333 167 LYS C C     
5165 O  O     . LYS D 168 ? 0.8137 0.9972 0.9445 -0.0858 0.3987  -0.0427 167 LYS C O     
5166 C  CB    . LYS D 168 ? 0.6955 0.8729 0.8299 -0.1132 0.3361  -0.0162 167 LYS C CB    
5167 C  C1    . ZNI E .   ? 0.1805 0.2371 0.2209 0.0060  -0.0150 0.0146  201 ZNI B C1    
5168 C  C10   . ZNI E .   ? 0.2236 0.2467 0.2363 -0.0216 -0.0088 0.0340  201 ZNI B C10   
5169 C  C11   . ZNI E .   ? 0.2857 0.3060 0.2895 -0.0252 -0.0064 0.0418  201 ZNI B C11   
5170 C  C12   . ZNI E .   ? 0.2521 0.2827 0.2521 -0.0119 -0.0089 0.0354  201 ZNI B C12   
5171 C  C13   . ZNI E .   ? 0.2172 0.2270 0.2471 0.0033  -0.0193 0.0202  201 ZNI B C13   
5172 C  C14   . ZNI E .   ? 0.2442 0.2425 0.2723 0.0025  -0.0186 0.0149  201 ZNI B C14   
5173 C  C15   . ZNI E .   ? 0.2392 0.2191 0.2626 0.0040  -0.0194 0.0029  201 ZNI B C15   
5174 C  C16   . ZNI E .   ? 0.2856 0.2553 0.3060 -0.0060 -0.0202 0.0074  201 ZNI B C16   
5175 C  C17   . ZNI E .   ? 0.2450 0.2223 0.2660 0.0099  -0.0193 -0.0065 201 ZNI B C17   
5176 C  C18   . ZNI E .   ? 0.2462 0.2444 0.2709 0.0158  -0.0165 -0.0092 201 ZNI B C18   
5177 C  C19   . ZNI E .   ? 0.2464 0.2460 0.2665 0.0224  -0.0154 -0.0188 201 ZNI B C19   
5178 C  C2    . ZNI E .   ? 0.1871 0.2298 0.2243 0.0052  -0.0151 0.0108  201 ZNI B C2    
5179 C  C20   . ZNI E .   ? 0.2458 0.2216 0.2567 0.0230  -0.0185 -0.0275 201 ZNI B C20   
5180 C  C21   . ZNI E .   ? 0.2747 0.2254 0.2824 0.0150  -0.0225 -0.0246 201 ZNI B C21   
5181 C  C22   . ZNI E .   ? 0.2546 0.2079 0.2676 0.0086  -0.0223 -0.0134 201 ZNI B C22   
5182 C  C23   . ZNI E .   ? 0.3264 0.2864 0.3189 0.0358  -0.0198 -0.0501 201 ZNI B C23   
5183 C  C24   . ZNI E .   ? 0.3637 0.3041 0.3542 0.0494  -0.0206 -0.0510 201 ZNI B C24   
5184 C  C25   . ZNI E .   ? 0.2426 0.2547 0.2541 0.0348  -0.0119 -0.0333 201 ZNI B C25   
5185 C  C26   . ZNI E .   ? 0.2700 0.2975 0.2764 0.0436  -0.0081 -0.0404 201 ZNI B C26   
5186 C  C27   . ZNI E .   ? 0.3112 0.3403 0.3069 0.0402  -0.0092 -0.0490 201 ZNI B C27   
5187 C  C28   . ZNI E .   ? 0.2940 0.3114 0.2863 0.0259  -0.0151 -0.0513 201 ZNI B C28   
5188 C  C29   . ZNI E .   ? 0.3244 0.3002 0.3045 0.0113  -0.0265 -0.0643 201 ZNI B C29   
5189 C  C3    . ZNI E .   ? 0.1800 0.2259 0.2155 0.0011  -0.0194 0.0210  201 ZNI B C3    
5190 C  C30   . ZNI E .   ? 0.2899 0.3291 0.2800 0.0207  -0.0150 -0.0507 201 ZNI B C30   
5191 C  C31   . ZNI E .   ? 0.3056 0.3664 0.2982 0.0619  0.0010  -0.0535 201 ZNI B C31   
5192 C  C32   . ZNI E .   ? 0.3053 0.3684 0.3108 0.0661  0.0022  -0.0453 201 ZNI B C32   
5193 C  C33   . ZNI E .   ? 0.3400 0.4435 0.3711 0.0725  0.0084  -0.0273 201 ZNI B C33   
5194 C  C34   . ZNI E .   ? 0.3445 0.4741 0.3872 0.0856  0.0135  -0.0241 201 ZNI B C34   
5195 C  C35   . ZNI E .   ? 0.4311 0.6182 0.4844 0.1043  0.0265  -0.0232 201 ZNI B C35   
5196 C  C36   . ZNI E .   ? 0.3702 0.6016 0.4296 0.1093  0.0363  -0.0191 201 ZNI B C36   
5197 C  C37   . ZNI E .   ? 0.3702 0.5903 0.4413 0.0930  0.0285  -0.0072 201 ZNI B C37   
5198 C  C38   . ZNI E .   ? 0.3650 0.5071 0.3856 0.0995  0.0221  -0.0416 201 ZNI B C38   
5199 C  C39   . ZNI E .   ? 0.3684 0.4809 0.3767 0.0864  0.0152  -0.0461 201 ZNI B C39   
5200 C  C4    . ZNI E .   ? 0.1656 0.2201 0.2071 0.0042  -0.0183 0.0207  201 ZNI B C4    
5201 C  C40   . ZNI E .   ? 0.2936 0.3376 0.3046 0.0566  -0.0032 -0.0392 201 ZNI B C40   
5202 C  C41   . ZNI E .   ? 0.2399 0.2613 0.2609 0.0292  -0.0116 -0.0221 201 ZNI B C41   
5203 C  C42   . ZNI E .   ? 0.2237 0.2714 0.2527 0.0292  -0.0083 -0.0141 201 ZNI B C42   
5204 C  C43   . ZNI E .   ? 0.2040 0.2629 0.2323 0.0205  -0.0084 -0.0112 201 ZNI B C43   
5205 C  C44   . ZNI E .   ? 0.2086 0.2865 0.2433 0.0207  -0.0063 -0.0026 201 ZNI B C44   
5206 C  C45   . ZNI E .   ? 0.1863 0.2479 0.2054 0.0211  -0.0081 -0.0202 201 ZNI B C45   
5207 C  C46   . ZNI E .   ? 0.1871 0.2346 0.2159 0.0114  -0.0117 -0.0083 201 ZNI B C46   
5208 C  C47   . ZNI E .   ? 0.1837 0.2270 0.2181 0.0046  -0.0138 0.0038  201 ZNI B C47   
5209 C  C5    . ZNI E .   ? 0.1985 0.2270 0.2288 -0.0003 -0.0189 0.0217  201 ZNI B C5    
5210 C  C6    . ZNI E .   ? 0.1914 0.2089 0.2194 -0.0028 -0.0176 0.0207  201 ZNI B C6    
5211 C  C7    . ZNI E .   ? 0.2162 0.2350 0.2370 -0.0114 -0.0145 0.0257  201 ZNI B C7    
5212 C  C8    . ZNI E .   ? 0.2152 0.2319 0.2288 -0.0138 -0.0132 0.0313  201 ZNI B C8    
5213 C  C9    . ZNI E .   ? 0.2559 0.2862 0.2667 -0.0136 -0.0101 0.0312  201 ZNI B C9    
5214 N  N1    . ZNI E .   ? 0.1862 0.2246 0.2207 0.0000  -0.0159 0.0134  201 ZNI B N1    
5215 N  N2    . ZNI E .   ? 0.1857 0.2238 0.2196 0.0007  -0.0178 0.0186  201 ZNI B N2    
5216 N  N3    . ZNI E .   ? 0.2412 0.2538 0.2636 -0.0063 -0.0174 0.0255  201 ZNI B N3    
5217 N  N4    . ZNI E .   ? 0.2197 0.2177 0.2486 0.0069  -0.0181 0.0082  201 ZNI B N4    
5218 N  N5    . ZNI E .   ? 0.2815 0.2641 0.2868 0.0312  -0.0167 -0.0373 201 ZNI B N5    
5219 N  N6    . ZNI E .   ? 0.2997 0.3438 0.2879 0.0493  -0.0052 -0.0554 201 ZNI B N6    
5220 N  N7    . ZNI E .   ? 0.3376 0.4239 0.3516 0.0786  0.0081  -0.0420 201 ZNI B N7    
5221 N  N8    . ZNI E .   ? 0.3814 0.5398 0.4211 0.0920  0.0214  -0.0267 201 ZNI B N8    
5222 O  O1    . ZNI E .   ? 0.2032 0.2305 0.2305 0.0002  -0.0213 0.0253  201 ZNI B O1    
5223 O  O2    . ZNI E .   ? 0.1805 0.2089 0.2053 -0.0138 -0.0129 0.0218  201 ZNI B O2    
5224 O  O3    . ZNI E .   ? 0.2554 0.2757 0.2520 -0.0170 -0.0086 0.0416  201 ZNI B O3    
5225 O  O4    . ZNI E .   ? 0.3503 0.3419 0.3310 0.0265  -0.0199 -0.0634 201 ZNI B O4    
5226 O  O5    . ZNI E .   ? 0.1652 0.2116 0.1995 0.0107  -0.0124 -0.0001 201 ZNI B O5    
5227 O  O6    . ZNI E .   ? 0.2032 0.2472 0.2357 -0.0007 -0.0142 0.0016  201 ZNI B O6    
5228 S  S1    . ZNI E .   ? 0.2684 0.2507 0.2905 -0.0082 -0.0187 0.0170  201 ZNI B S1    
5229 C  C1    . ZNI F .   ? 0.2936 0.4457 0.2106 -0.1355 -0.0208 0.0327  201 ZNI D C1    
5230 C  C10   . ZNI F .   ? 0.4458 0.5288 0.3626 -0.1896 -0.1077 0.1611  201 ZNI D C10   
5231 C  C11   . ZNI F .   ? 0.4637 0.5376 0.3815 -0.1942 -0.1206 0.1797  201 ZNI D C11   
5232 C  C12   . ZNI F .   ? 0.4588 0.5167 0.3684 -0.1730 -0.1225 0.1587  201 ZNI D C12   
5233 C  C13   . ZNI F .   ? 0.3661 0.5657 0.2643 -0.1684 -0.0416 0.0880  201 ZNI D C13   
5234 C  C14   . ZNI F .   ? 0.3594 0.5763 0.2647 -0.1728 -0.0366 0.0907  201 ZNI D C14   
5235 C  C15   . ZNI F .   ? 0.3944 0.6424 0.3102 -0.1737 -0.0261 0.0862  201 ZNI D C15   
5236 C  C16   . ZNI F .   ? 0.4372 0.6765 0.3544 -0.1838 -0.0368 0.1055  201 ZNI D C16   
5237 C  C17   . ZNI F .   ? 0.3276 0.5939 0.2488 -0.1680 -0.0162 0.0743  201 ZNI D C17   
5238 C  C18   . ZNI F .   ? 0.3308 0.5901 0.2528 -0.1574 -0.0085 0.0569  201 ZNI D C18   
5239 C  C19   . ZNI F .   ? 0.3096 0.5843 0.2384 -0.1501 0.0005  0.0452  201 ZNI D C19   
5240 C  C2    . ZNI F .   ? 0.2908 0.4587 0.2040 -0.1476 -0.0250 0.0507  201 ZNI D C2    
5241 C  C20   . ZNI F .   ? 0.3215 0.6211 0.2569 -0.1546 0.0013  0.0519  201 ZNI D C20   
5242 C  C21   . ZNI F .   ? 0.3458 0.6525 0.2799 -0.1668 -0.0063 0.0701  201 ZNI D C21   
5243 C  C22   . ZNI F .   ? 0.3458 0.6351 0.2733 -0.1733 -0.0149 0.0814  201 ZNI D C22   
5244 C  C23   . ZNI F .   ? 0.3256 0.6692 0.2768 -0.1461 0.0130  0.0404  201 ZNI D C23   
5245 C  C24   . ZNI F .   ? 0.3537 0.7332 0.3015 -0.1407 0.0206  0.0306  201 ZNI D C24   
5246 C  C25   . ZNI F .   ? 0.3094 0.6052 0.2498 -0.1346 0.0148  0.0240  201 ZNI D C25   
5247 C  C26   . ZNI F .   ? 0.3152 0.6196 0.2619 -0.1218 0.0238  0.0082  201 ZNI D C26   
5248 C  C27   . ZNI F .   ? 0.3093 0.6132 0.2673 -0.1191 0.0246  0.0091  201 ZNI D C27   
5249 C  C28   . ZNI F .   ? 0.2596 0.5516 0.2248 -0.1313 0.0146  0.0262  201 ZNI D C28   
5250 C  C29   . ZNI F .   ? 0.3563 0.6646 0.3339 -0.1486 0.0035  0.0479  201 ZNI D C29   
5251 C  C3    . ZNI F .   ? 0.2886 0.4175 0.2035 -0.1389 -0.0400 0.0472  201 ZNI D C3    
5252 C  C30   . ZNI F .   ? 0.2787 0.5372 0.2492 -0.1236 0.0092  0.0230  201 ZNI D C30   
5253 C  C31   . ZNI F .   ? 0.3585 0.6681 0.3189 -0.0910 0.0368  -0.0233 201 ZNI D C31   
5254 C  C32   . ZNI F .   ? 0.3782 0.6939 0.3264 -0.0945 0.0389  -0.0279 201 ZNI D C32   
5255 C  C33   . ZNI F .   ? 0.4531 0.7717 0.3861 -0.0864 0.0422  -0.0529 201 ZNI D C33   
5256 C  C34   . ZNI F .   ? 0.4557 0.7551 0.3871 -0.0742 0.0446  -0.0756 201 ZNI D C34   
5257 C  C35   . ZNI F .   ? 0.4942 0.7831 0.4339 -0.0494 0.0496  -0.1138 201 ZNI D C35   
5258 C  C36   . ZNI F .   ? 0.4861 0.7938 0.4235 -0.0398 0.0521  -0.1375 201 ZNI D C36   
5259 C  C37   . ZNI F .   ? 0.4675 0.7555 0.4182 -0.0306 0.0534  -0.1340 201 ZNI D C37   
5260 C  C38   . ZNI F .   ? 0.5201 0.8225 0.4726 -0.0529 0.0503  -0.0861 201 ZNI D C38   
5261 C  C39   . ZNI F .   ? 0.4508 0.7821 0.4046 -0.0654 0.0502  -0.0663 201 ZNI D C39   
5262 C  C4    . ZNI F .   ? 0.2890 0.4348 0.2026 -0.1348 -0.0271 0.0319  201 ZNI D C4    
5263 C  C40   . ZNI F .   ? 0.3300 0.6431 0.2723 -0.1099 0.0314  -0.0105 201 ZNI D C40   
5264 C  C41   . ZNI F .   ? 0.3194 0.5918 0.2507 -0.1379 0.0096  0.0274  201 ZNI D C41   
5265 C  C42   . ZNI F .   ? 0.3198 0.5672 0.2448 -0.1305 0.0120  0.0155  201 ZNI D C42   
5266 C  C43   . ZNI F .   ? 0.2859 0.4948 0.2179 -0.1272 0.0053  0.0181  201 ZNI D C43   
5267 C  C44   . ZNI F .   ? 0.2966 0.4796 0.2272 -0.1178 0.0058  0.0059  201 ZNI D C44   
5268 C  C45   . ZNI F .   ? 0.2466 0.4561 0.1892 -0.1215 0.0076  0.0159  201 ZNI D C45   
5269 C  C46   . ZNI F .   ? 0.2777 0.4739 0.2087 -0.1390 -0.0055 0.0359  201 ZNI D C46   
5270 C  C47   . ZNI F .   ? 0.3230 0.4927 0.2447 -0.1475 -0.0209 0.0505  201 ZNI D C47   
5271 C  C5    . ZNI F .   ? 0.3312 0.4805 0.2324 -0.1577 -0.0519 0.0794  201 ZNI D C5    
5272 C  C6    . ZNI F .   ? 0.3644 0.5285 0.2655 -0.1700 -0.0535 0.0976  201 ZNI D C6    
5273 C  C7    . ZNI F .   ? 0.3971 0.5203 0.3037 -0.1789 -0.0788 0.1271  201 ZNI D C7    
5274 C  C8    . ZNI F .   ? 0.3878 0.4953 0.2950 -0.1820 -0.0933 0.1438  201 ZNI D C8    
5275 C  C9    . ZNI F .   ? 0.4383 0.5069 0.3495 -0.1772 -0.1096 0.1493  201 ZNI D C9    
5276 N  N1    . ZNI F .   ? 0.3000 0.4484 0.2141 -0.1532 -0.0378 0.0657  201 ZNI D N1    
5277 N  N2    . ZNI F .   ? 0.3094 0.4513 0.2190 -0.1498 -0.0432 0.0637  201 ZNI D N2    
5278 N  N3    . ZNI F .   ? 0.3825 0.5352 0.2829 -0.1751 -0.0664 0.1149  201 ZNI D N3    
5279 N  N4    . ZNI F .   ? 0.3035 0.5366 0.2123 -0.1683 -0.0265 0.0786  201 ZNI D N4    
5280 N  N5    . ZNI F .   ? 0.3259 0.6394 0.2685 -0.1453 0.0097  0.0390  201 ZNI D N5    
5281 N  N6    . ZNI F .   ? 0.3017 0.6086 0.2661 -0.1033 0.0304  -0.0061 201 ZNI D N6    
5282 N  N7    . ZNI F .   ? 0.3827 0.7008 0.3270 -0.0826 0.0440  -0.0482 201 ZNI D N7    
5283 N  N8    . ZNI F .   ? 0.4608 0.7719 0.4006 -0.0584 0.0504  -0.0937 201 ZNI D N8    
5284 O  O1    . ZNI F .   ? 0.3413 0.4872 0.2389 -0.1544 -0.0581 0.0786  201 ZNI D O1    
5285 O  O2    . ZNI F .   ? 0.3734 0.4822 0.2868 -0.1786 -0.0777 0.1230  201 ZNI D O2    
5286 O  O3    . ZNI F .   ? 0.4728 0.5451 0.3825 -0.1841 -0.1230 0.1751  201 ZNI D O3    
5287 O  O4    . ZNI F .   ? 0.2756 0.5943 0.2499 -0.1356 0.0137  0.0319  201 ZNI D O4    
5288 O  O5    . ZNI F .   ? 0.2479 0.4388 0.1697 -0.1421 -0.0099 0.0387  201 ZNI D O5    
5289 O  O6    . ZNI F .   ? 0.3142 0.4680 0.2428 -0.1510 -0.0278 0.0588  201 ZNI D O6    
5290 S  S1    . ZNI F .   ? 0.4473 0.6615 0.3583 -0.1857 -0.0479 0.1148  201 ZNI D S1    
5291 P  PB    . GDP G .   ? 0.1829 0.2975 0.2545 0.0145  -0.0014 -0.0007 201 GDP A PB    
5292 O  O1B   . GDP G .   ? 0.1843 0.2796 0.2493 0.0133  0.0071  -0.0007 201 GDP A O1B   
5293 O  O2B   . GDP G .   ? 0.1701 0.2960 0.2471 0.0228  0.0033  0.0097  201 GDP A O2B   
5294 O  O3B   . GDP G .   ? 0.2033 0.3276 0.2925 0.0051  -0.0091 -0.0042 201 GDP A O3B   
5295 O  O3A   . GDP G .   ? 0.2015 0.3164 0.2545 0.0179  -0.0080 -0.0073 201 GDP A O3A   
5296 P  PA    . GDP G .   ? 0.2226 0.3211 0.2597 0.0179  -0.0063 -0.0163 201 GDP A PA    
5297 O  O1A   . GDP G .   ? 0.2170 0.3054 0.2465 0.0228  0.0038  -0.0110 201 GDP A O1A   
5298 O  O2A   . GDP G .   ? 0.2312 0.3185 0.2754 0.0102  -0.0098 -0.0249 201 GDP A O2A   
5299 O  "O5'" . GDP G .   ? 0.2185 0.3262 0.2390 0.0212  -0.0133 -0.0225 201 GDP A "O5'" 
5300 C  "C5'" . GDP G .   ? 0.2337 0.3530 0.2583 0.0156  -0.0257 -0.0291 201 GDP A "C5'" 
5301 C  "C4'" . GDP G .   ? 0.3044 0.4254 0.3050 0.0184  -0.0304 -0.0390 201 GDP A "C4'" 
5302 O  "O4'" . GDP G .   ? 0.2639 0.3958 0.2511 0.0270  -0.0273 -0.0282 201 GDP A "O4'" 
5303 C  "C3'" . GDP G .   ? 0.2955 0.3972 0.2857 0.0201  -0.0228 -0.0489 201 GDP A "C3'" 
5304 O  "O3'" . GDP G .   ? 0.3563 0.4583 0.3279 0.0192  -0.0299 -0.0638 201 GDP A "O3'" 
5305 C  "C2'" . GDP G .   ? 0.2899 0.3932 0.2682 0.0289  -0.0123 -0.0397 201 GDP A "C2'" 
5306 O  "O2'" . GDP G .   ? 0.3674 0.4637 0.3300 0.0331  -0.0065 -0.0491 201 GDP A "O2'" 
5307 C  "C1'" . GDP G .   ? 0.3006 0.4224 0.2690 0.0322  -0.0180 -0.0316 201 GDP A "C1'" 
5308 N  N9    . GDP G .   ? 0.2853 0.4083 0.2535 0.0386  -0.0083 -0.0160 201 GDP A N9    
5309 C  C8    . GDP G .   ? 0.2576 0.3736 0.2427 0.0383  -0.0015 -0.0070 201 GDP A C8    
5310 N  N7    . GDP G .   ? 0.2551 0.3709 0.2347 0.0440  0.0063  0.0053  201 GDP A N7    
5311 C  C5    . GDP G .   ? 0.2730 0.3983 0.2324 0.0483  0.0044  0.0069  201 GDP A C5    
5312 C  C6    . GDP G .   ? 0.2693 0.3987 0.2130 0.0546  0.0105  0.0196  201 GDP A C6    
5313 O  O6    . GDP G .   ? 0.2743 0.3962 0.2254 0.0568  0.0189  0.0323  201 GDP A O6    
5314 N  N1    . GDP G .   ? 0.3058 0.4456 0.2255 0.0573  0.0070  0.0172  201 GDP A N1    
5315 C  C2    . GDP G .   ? 0.3073 0.4524 0.2159 0.0544  -0.0020 0.0012  201 GDP A C2    
5316 N  N2    . GDP G .   ? 0.3399 0.4950 0.2191 0.0574  -0.0048 -0.0019 201 GDP A N2    
5317 N  N3    . GDP G .   ? 0.2999 0.4391 0.2246 0.0479  -0.0083 -0.0120 201 GDP A N3    
5318 C  C4    . GDP G .   ? 0.2876 0.4178 0.2376 0.0448  -0.0051 -0.0084 201 GDP A C4    
5319 MG MG    . MG  H .   ? 0.1617 0.2408 0.2326 0.0040  0.0108  -0.0012 202 MG  A MG    
5320 P  PB    . GDP I .   ? 0.4747 0.7416 0.4541 -0.2350 -0.0574 0.0927  201 GDP C PB    
5321 O  O1B   . GDP I .   ? 0.4564 0.7042 0.4580 -0.2176 -0.0399 0.0873  201 GDP C O1B   
5322 O  O2B   . GDP I .   ? 0.4722 0.7650 0.4624 -0.2490 -0.0617 0.0857  201 GDP C O2B   
5323 O  O3B   . GDP I .   ? 0.5095 0.7479 0.4442 -0.2522 -0.0516 0.0880  201 GDP C O3B   
5324 O  O3A   . GDP I .   ? 0.4888 0.7787 0.4800 -0.2200 -0.0775 0.1117  201 GDP C O3A   
5325 P  PA    . GDP I .   ? 0.4476 0.7505 0.4793 -0.1911 -0.0800 0.1213  201 GDP C PA    
5326 O  O1A   . GDP I .   ? 0.4369 0.7046 0.4666 -0.1770 -0.0658 0.1211  201 GDP C O1A   
5327 O  O2A   . GDP I .   ? 0.4206 0.7484 0.4856 -0.1893 -0.0761 0.1137  201 GDP C O2A   
5328 O  "O5'" . GDP I .   ? 0.4705 0.7985 0.4998 -0.1854 -0.1043 0.1394  201 GDP C "O5'" 
5329 C  "C5'" . GDP I .   ? 0.4861 0.8520 0.5160 -0.1995 -0.1220 0.1427  201 GDP C "C5'" 
5330 C  "C4'" . GDP I .   ? 0.4965 0.8904 0.5416 -0.1814 -0.1441 0.1624  201 GDP C "C4'" 
5331 O  "O4'" . GDP I .   ? 0.5255 0.8876 0.5349 -0.1812 -0.1479 0.1711  201 GDP C "O4'" 
5332 C  "C3'" . GDP I .   ? 0.4695 0.8696 0.5534 -0.1505 -0.1406 0.1686  201 GDP C "C3'" 
5333 O  "O3'" . GDP I .   ? 0.4730 0.9176 0.5853 -0.1360 -0.1599 0.1823  201 GDP C "O3'" 
5334 C  "C2'" . GDP I .   ? 0.4811 0.8367 0.5429 -0.1379 -0.1351 0.1754  201 GDP C "C2'" 
5335 O  "O2'" . GDP I .   ? 0.4752 0.8271 0.5581 -0.1086 -0.1376 0.1869  201 GDP C "O2'" 
5336 C  "C1'" . GDP I .   ? 0.5212 0.8717 0.5440 -0.1536 -0.1498 0.1837  201 GDP C "C1'" 
5337 N  N9    . GDP I .   ? 0.5385 0.8404 0.5255 -0.1564 -0.1395 0.1842  201 GDP C N9    
5338 C  C8    . GDP I .   ? 0.5386 0.8081 0.5153 -0.1634 -0.1172 0.1707  201 GDP C C8    
5339 N  N7    . GDP I .   ? 0.5518 0.7858 0.4968 -0.1652 -0.1130 0.1760  201 GDP C N7    
5340 C  C5    . GDP I .   ? 0.5797 0.8183 0.5101 -0.1597 -0.1330 0.1933  201 GDP C C5    
5341 C  C6    . GDP I .   ? 0.6261 0.8366 0.5197 -0.1596 -0.1408 0.2075  201 GDP C C6    
5342 O  O6    . GDP I .   ? 0.6888 0.8623 0.5569 -0.1668 -0.1257 0.2039  201 GDP C O6    
5343 N  N1    . GDP I .   ? 0.6469 0.8731 0.5357 -0.1510 -0.1647 0.2251  201 GDP C N1    
5344 C  C2    . GDP I .   ? 0.6392 0.9104 0.5584 -0.1428 -0.1816 0.2301  201 GDP C C2    
5345 N  N2    . GDP I .   ? 0.6681 0.9562 0.5830 -0.1325 -0.2067 0.2494  201 GDP C N2    
5346 N  N3    . GDP I .   ? 0.5999 0.9019 0.5554 -0.1441 -0.1745 0.2169  201 GDP C N3    
5347 C  C4    . GDP I .   ? 0.5722 0.8572 0.5321 -0.1527 -0.1510 0.1989  201 GDP C C4    
5348 MG MG    . MG  J .   ? 0.4079 0.6563 0.4411 -0.2136 -0.0241 0.0729  202 MG  C MG    
5349 AL AL    . AF3 K .   ? 0.5135 0.7226 0.4319 -0.2698 -0.0271 0.0639  203 AF3 C AL    
5350 F  F1    . AF3 K .   ? 0.6904 0.8658 0.5569 -0.2867 -0.0183 0.0585  203 AF3 C F1    
5351 F  F2    . AF3 K .   ? 0.5639 0.8001 0.4917 -0.2861 -0.0356 0.0580  203 AF3 C F2    
5352 F  F3    . AF3 K .   ? 0.5225 0.7219 0.4777 -0.2442 -0.0127 0.0627  203 AF3 C F3    
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