data_9BG2
# 
_entry.id   9BG2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BG2         pdb_00009bg2 10.2210/pdb9bg2/pdb 
WWPDB D_1000283246 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BG2 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jyano@revmed.com 
_pdbx_contact_author.name_first         Jason 
_pdbx_contact_author.name_last          Yano 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9774-2611 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tomlinson, A.C.A.' 1 0000-0002-9663-773X 
'Bieder, R.'        2 ?                   
'Chen, A.'          3 0000-0002-3259-5868 
'Knox, J.E.'        4 ?                   
'Yano, J.K.'        5 0000-0002-9774-2611 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Discovery of Daraxonrasib (RMC-6236), a Potent and Orally Bioavailable RAS(ON) Multi-selective, Noncovalent Tri-complex Inhibitor for the Treatment of Patients with Multiple RAS-Addicted Cancers.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02314 
_citation.pdbx_database_id_PubMed   40056080 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cregg, J.'         1  0000-0002-2871-0800 
primary 'Edwards, A.V.'     2  ?                   
primary 'Chang, S.'         3  ?                   
primary 'Lee, B.J.'         4  ?                   
primary 'Knox, J.E.'        5  ?                   
primary 'Tomlinson, A.C.A.' 6  ?                   
primary 'Marquez, A.'       7  ?                   
primary 'Liu, Y.'           8  ?                   
primary 'Freilich, R.'      9  ?                   
primary 'Aay, N.'           10 ?                   
primary 'Wang, Y.'          11 ?                   
primary 'Jiang, L.'         12 ?                   
primary 'Jiang, J.'         13 ?                   
primary 'Wang, Z.'          14 ?                   
primary 'Flagella, M.'      15 ?                   
primary 'Wildes, D.'        16 ?                   
primary 'Smith, J.A.M.'     17 ?                   
primary 'Singh, M.'         18 ?                   
primary 'Wang, Z.'          19 ?                   
primary 'Gill, A.L.'        20 ?                   
primary 'Koltun, E.S.'      21 0009-0005-8720-9097 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas' 19400.916 2   3.6.5.2 ? ? ? 
2 polymer     man 'Peptidyl-prolyl cis-trans isomerase A' 18123.582 2   5.2.1.8 ? ? ? 
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   2   ?       ? ? ? 
4 non-polymer syn 'MAGNESIUM ION' 24.305    2   ?       ? ? ? 
5 non-polymer syn 
;(1S,2R)-N-[(1P,7S,9S,13S,20M)-21-ethyl-20-{2-[(1S)-1-methoxyethyl]pyridin-3-yl}-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]-2-methylcyclopropane-1-carboxamide (non-preferred name)
;
712.901   2   ?       ? ? ? 
6 water       nat water 18.015    632 ?       ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'K-Ras 2,Ki-Ras,c-K-ras,c-Ki-ras'                                 
2 'PPIase A,Cyclophilin A,Cyclosporin A-binding protein,Rotamase A' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;SMTEYKLVVVGAVGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
;SMTEYKLVVVGAVGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
A,B ? 
2 'polypeptide(L)' no no 
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP   
4 'MAGNESIUM ION' MG    
5 
;(1S,2R)-N-[(1P,7S,9S,13S,20M)-21-ethyl-20-{2-[(1S)-1-methoxyethyl]pyridin-3-yl}-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]-2-methylcyclopropane-1-carboxamide (non-preferred name)
;
A1AOJ 
6 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   THR n 
1 4   GLU n 
1 5   TYR n 
1 6   LYS n 
1 7   LEU n 
1 8   VAL n 
1 9   VAL n 
1 10  VAL n 
1 11  GLY n 
1 12  ALA n 
1 13  VAL n 
1 14  GLY n 
1 15  VAL n 
1 16  GLY n 
1 17  LYS n 
1 18  SER n 
1 19  ALA n 
1 20  LEU n 
1 21  THR n 
1 22  ILE n 
1 23  GLN n 
1 24  LEU n 
1 25  ILE n 
1 26  GLN n 
1 27  ASN n 
1 28  HIS n 
1 29  PHE n 
1 30  VAL n 
1 31  ASP n 
1 32  GLU n 
1 33  TYR n 
1 34  ASP n 
1 35  PRO n 
1 36  THR n 
1 37  ILE n 
1 38  GLU n 
1 39  ASP n 
1 40  SER n 
1 41  TYR n 
1 42  ARG n 
1 43  LYS n 
1 44  GLN n 
1 45  VAL n 
1 46  VAL n 
1 47  ILE n 
1 48  ASP n 
1 49  GLY n 
1 50  GLU n 
1 51  THR n 
1 52  CYS n 
1 53  LEU n 
1 54  LEU n 
1 55  ASP n 
1 56  ILE n 
1 57  LEU n 
1 58  ASP n 
1 59  THR n 
1 60  ALA n 
1 61  GLY n 
1 62  GLN n 
1 63  GLU n 
1 64  GLU n 
1 65  TYR n 
1 66  SER n 
1 67  ALA n 
1 68  MET n 
1 69  ARG n 
1 70  ASP n 
1 71  GLN n 
1 72  TYR n 
1 73  MET n 
1 74  ARG n 
1 75  THR n 
1 76  GLY n 
1 77  GLU n 
1 78  GLY n 
1 79  PHE n 
1 80  LEU n 
1 81  CYS n 
1 82  VAL n 
1 83  PHE n 
1 84  ALA n 
1 85  ILE n 
1 86  ASN n 
1 87  ASN n 
1 88  THR n 
1 89  LYS n 
1 90  SER n 
1 91  PHE n 
1 92  GLU n 
1 93  ASP n 
1 94  ILE n 
1 95  HIS n 
1 96  HIS n 
1 97  TYR n 
1 98  ARG n 
1 99  GLU n 
1 100 GLN n 
1 101 ILE n 
1 102 LYS n 
1 103 ARG n 
1 104 VAL n 
1 105 LYS n 
1 106 ASP n 
1 107 SER n 
1 108 GLU n 
1 109 ASP n 
1 110 VAL n 
1 111 PRO n 
1 112 MET n 
1 113 VAL n 
1 114 LEU n 
1 115 VAL n 
1 116 GLY n 
1 117 ASN n 
1 118 LYS n 
1 119 CYS n 
1 120 ASP n 
1 121 LEU n 
1 122 PRO n 
1 123 SER n 
1 124 ARG n 
1 125 THR n 
1 126 VAL n 
1 127 ASP n 
1 128 THR n 
1 129 LYS n 
1 130 GLN n 
1 131 ALA n 
1 132 GLN n 
1 133 ASP n 
1 134 LEU n 
1 135 ALA n 
1 136 ARG n 
1 137 SER n 
1 138 TYR n 
1 139 GLY n 
1 140 ILE n 
1 141 PRO n 
1 142 PHE n 
1 143 ILE n 
1 144 GLU n 
1 145 THR n 
1 146 SER n 
1 147 ALA n 
1 148 LYS n 
1 149 THR n 
1 150 ARG n 
1 151 GLN n 
1 152 GLY n 
1 153 VAL n 
1 154 ASP n 
1 155 ASP n 
1 156 ALA n 
1 157 PHE n 
1 158 TYR n 
1 159 THR n 
1 160 LEU n 
1 161 VAL n 
1 162 ARG n 
1 163 GLU n 
1 164 ILE n 
1 165 ARG n 
1 166 LYS n 
1 167 HIS n 
1 168 LYS n 
1 169 GLU n 
1 170 LYS n 
2 1   SER n 
2 2   MET n 
2 3   VAL n 
2 4   ASN n 
2 5   PRO n 
2 6   THR n 
2 7   VAL n 
2 8   PHE n 
2 9   PHE n 
2 10  ASP n 
2 11  ILE n 
2 12  ALA n 
2 13  VAL n 
2 14  ASP n 
2 15  GLY n 
2 16  GLU n 
2 17  PRO n 
2 18  LEU n 
2 19  GLY n 
2 20  ARG n 
2 21  VAL n 
2 22  SER n 
2 23  PHE n 
2 24  GLU n 
2 25  LEU n 
2 26  PHE n 
2 27  ALA n 
2 28  ASP n 
2 29  LYS n 
2 30  VAL n 
2 31  PRO n 
2 32  LYS n 
2 33  THR n 
2 34  ALA n 
2 35  GLU n 
2 36  ASN n 
2 37  PHE n 
2 38  ARG n 
2 39  ALA n 
2 40  LEU n 
2 41  SER n 
2 42  THR n 
2 43  GLY n 
2 44  GLU n 
2 45  LYS n 
2 46  GLY n 
2 47  PHE n 
2 48  GLY n 
2 49  TYR n 
2 50  LYS n 
2 51  GLY n 
2 52  SER n 
2 53  CYS n 
2 54  PHE n 
2 55  HIS n 
2 56  ARG n 
2 57  ILE n 
2 58  ILE n 
2 59  PRO n 
2 60  GLY n 
2 61  PHE n 
2 62  MET n 
2 63  CYS n 
2 64  GLN n 
2 65  GLY n 
2 66  GLY n 
2 67  ASP n 
2 68  PHE n 
2 69  THR n 
2 70  ARG n 
2 71  HIS n 
2 72  ASN n 
2 73  GLY n 
2 74  THR n 
2 75  GLY n 
2 76  GLY n 
2 77  LYS n 
2 78  SER n 
2 79  ILE n 
2 80  TYR n 
2 81  GLY n 
2 82  GLU n 
2 83  LYS n 
2 84  PHE n 
2 85  GLU n 
2 86  ASP n 
2 87  GLU n 
2 88  ASN n 
2 89  PHE n 
2 90  ILE n 
2 91  LEU n 
2 92  LYS n 
2 93  HIS n 
2 94  THR n 
2 95  GLY n 
2 96  PRO n 
2 97  GLY n 
2 98  ILE n 
2 99  LEU n 
2 100 SER n 
2 101 MET n 
2 102 ALA n 
2 103 ASN n 
2 104 ALA n 
2 105 GLY n 
2 106 PRO n 
2 107 ASN n 
2 108 THR n 
2 109 ASN n 
2 110 GLY n 
2 111 SER n 
2 112 GLN n 
2 113 PHE n 
2 114 PHE n 
2 115 ILE n 
2 116 CYS n 
2 117 THR n 
2 118 ALA n 
2 119 LYS n 
2 120 THR n 
2 121 GLU n 
2 122 TRP n 
2 123 LEU n 
2 124 ASP n 
2 125 GLY n 
2 126 LYS n 
2 127 HIS n 
2 128 VAL n 
2 129 VAL n 
2 130 PHE n 
2 131 GLY n 
2 132 LYS n 
2 133 VAL n 
2 134 LYS n 
2 135 GLU n 
2 136 GLY n 
2 137 MET n 
2 138 ASN n 
2 139 ILE n 
2 140 VAL n 
2 141 GLU n 
2 142 ALA n 
2 143 MET n 
2 144 GLU n 
2 145 ARG n 
2 146 PHE n 
2 147 GLY n 
2 148 SER n 
2 149 ARG n 
2 150 ASN n 
2 151 GLY n 
2 152 LYS n 
2 153 THR n 
2 154 SER n 
2 155 LYS n 
2 156 LYS n 
2 157 ILE n 
2 158 THR n 
2 159 ILE n 
2 160 ALA n 
2 161 ASP n 
2 162 CYS n 
2 163 GLY n 
2 164 GLN n 
2 165 LEU n 
2 166 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 170 human ? 'KRAS, KRAS2, RASK2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 166 human ? 'PPIA, CYPA'         ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AOJ non-polymer         . 
;(1S,2R)-N-[(1P,7S,9S,13S,20M)-21-ethyl-20-{2-[(1S)-1-methoxyethyl]pyridin-3-yl}-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]-2-methylcyclopropane-1-carboxamide (non-preferred name)
;
? 'C39 H48 N6 O5 S'   712.901 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'        75.067  
GNP   non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ? 'C10 H17 N6 O13 P3' 522.196 
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'     149.211 
MG    non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'              24.305  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   0   0   SER SER A . n 
A 1 2   MET 2   1   1   MET MET A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   GLU 4   3   3   GLU GLU A . n 
A 1 5   TYR 5   4   4   TYR TYR A . n 
A 1 6   LYS 6   5   5   LYS LYS A . n 
A 1 7   LEU 7   6   6   LEU LEU A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   VAL 9   8   8   VAL VAL A . n 
A 1 10  VAL 10  9   9   VAL VAL A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ALA 12  11  11  ALA ALA A . n 
A 1 13  VAL 13  12  12  VAL VAL A . n 
A 1 14  GLY 14  13  13  GLY GLY A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLY 16  15  15  GLY GLY A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  ALA 19  18  18  ALA ALA A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  THR 21  20  20  THR THR A . n 
A 1 22  ILE 22  21  21  ILE ILE A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  ILE 25  24  24  ILE ILE A . n 
A 1 26  GLN 26  25  25  GLN GLN A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  HIS 28  27  27  HIS HIS A . n 
A 1 29  PHE 29  28  28  PHE PHE A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  ASP 31  30  30  ASP ASP A . n 
A 1 32  GLU 32  31  31  GLU GLU A . n 
A 1 33  TYR 33  32  32  TYR TYR A . n 
A 1 34  ASP 34  33  33  ASP ASP A . n 
A 1 35  PRO 35  34  34  PRO PRO A . n 
A 1 36  THR 36  35  35  THR THR A . n 
A 1 37  ILE 37  36  36  ILE ILE A . n 
A 1 38  GLU 38  37  37  GLU GLU A . n 
A 1 39  ASP 39  38  38  ASP ASP A . n 
A 1 40  SER 40  39  39  SER SER A . n 
A 1 41  TYR 41  40  40  TYR TYR A . n 
A 1 42  ARG 42  41  41  ARG ARG A . n 
A 1 43  LYS 43  42  42  LYS LYS A . n 
A 1 44  GLN 44  43  43  GLN GLN A . n 
A 1 45  VAL 45  44  44  VAL VAL A . n 
A 1 46  VAL 46  45  45  VAL VAL A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  GLY 49  48  48  GLY GLY A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  THR 51  50  50  THR THR A . n 
A 1 52  CYS 52  51  51  CYS CYS A . n 
A 1 53  LEU 53  52  52  LEU LEU A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  ASP 55  54  54  ASP ASP A . n 
A 1 56  ILE 56  55  55  ILE ILE A . n 
A 1 57  LEU 57  56  56  LEU LEU A . n 
A 1 58  ASP 58  57  57  ASP ASP A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  ALA 60  59  59  ALA ALA A . n 
A 1 61  GLY 61  60  60  GLY GLY A . n 
A 1 62  GLN 62  61  61  GLN GLN A . n 
A 1 63  GLU 63  62  62  GLU GLU A . n 
A 1 64  GLU 64  63  63  GLU GLU A . n 
A 1 65  TYR 65  64  64  TYR TYR A . n 
A 1 66  SER 66  65  65  SER SER A . n 
A 1 67  ALA 67  66  66  ALA ALA A . n 
A 1 68  MET 68  67  67  MET MET A . n 
A 1 69  ARG 69  68  68  ARG ARG A . n 
A 1 70  ASP 70  69  69  ASP ASP A . n 
A 1 71  GLN 71  70  70  GLN GLN A . n 
A 1 72  TYR 72  71  71  TYR TYR A . n 
A 1 73  MET 73  72  72  MET MET A . n 
A 1 74  ARG 74  73  73  ARG ARG A . n 
A 1 75  THR 75  74  74  THR THR A . n 
A 1 76  GLY 76  75  75  GLY GLY A . n 
A 1 77  GLU 77  76  76  GLU GLU A . n 
A 1 78  GLY 78  77  77  GLY GLY A . n 
A 1 79  PHE 79  78  78  PHE PHE A . n 
A 1 80  LEU 80  79  79  LEU LEU A . n 
A 1 81  CYS 81  80  80  CYS CYS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  PHE 83  82  82  PHE PHE A . n 
A 1 84  ALA 84  83  83  ALA ALA A . n 
A 1 85  ILE 85  84  84  ILE ILE A . n 
A 1 86  ASN 86  85  85  ASN ASN A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  THR 88  87  87  THR THR A . n 
A 1 89  LYS 89  88  88  LYS LYS A . n 
A 1 90  SER 90  89  89  SER SER A . n 
A 1 91  PHE 91  90  90  PHE PHE A . n 
A 1 92  GLU 92  91  91  GLU GLU A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  ILE 94  93  93  ILE ILE A . n 
A 1 95  HIS 95  94  94  HIS HIS A . n 
A 1 96  HIS 96  95  95  HIS HIS A . n 
A 1 97  TYR 97  96  96  TYR TYR A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  GLU 99  98  98  GLU GLU A . n 
A 1 100 GLN 100 99  99  GLN GLN A . n 
A 1 101 ILE 101 100 100 ILE ILE A . n 
A 1 102 LYS 102 101 101 LYS LYS A . n 
A 1 103 ARG 103 102 102 ARG ARG A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 LYS 105 104 104 LYS LYS A . n 
A 1 106 ASP 106 105 105 ASP ASP A . n 
A 1 107 SER 107 106 106 SER SER A . n 
A 1 108 GLU 108 107 107 GLU GLU A . n 
A 1 109 ASP 109 108 108 ASP ASP A . n 
A 1 110 VAL 110 109 109 VAL VAL A . n 
A 1 111 PRO 111 110 110 PRO PRO A . n 
A 1 112 MET 112 111 111 MET MET A . n 
A 1 113 VAL 113 112 112 VAL VAL A . n 
A 1 114 LEU 114 113 113 LEU LEU A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 GLY 116 115 115 GLY GLY A . n 
A 1 117 ASN 117 116 116 ASN ASN A . n 
A 1 118 LYS 118 117 117 LYS LYS A . n 
A 1 119 CYS 119 118 118 CYS CYS A . n 
A 1 120 ASP 120 119 119 ASP ASP A . n 
A 1 121 LEU 121 120 120 LEU LEU A . n 
A 1 122 PRO 122 121 121 PRO PRO A . n 
A 1 123 SER 123 122 122 SER SER A . n 
A 1 124 ARG 124 123 123 ARG ARG A . n 
A 1 125 THR 125 124 124 THR THR A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 ASP 127 126 126 ASP ASP A . n 
A 1 128 THR 128 127 127 THR THR A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLN 130 129 129 GLN GLN A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 GLN 132 131 131 GLN GLN A . n 
A 1 133 ASP 133 132 132 ASP ASP A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 ARG 136 135 135 ARG ARG A . n 
A 1 137 SER 137 136 136 SER SER A . n 
A 1 138 TYR 138 137 137 TYR TYR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ILE 140 139 139 ILE ILE A . n 
A 1 141 PRO 141 140 140 PRO PRO A . n 
A 1 142 PHE 142 141 141 PHE PHE A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 GLU 144 143 143 GLU GLU A . n 
A 1 145 THR 145 144 144 THR THR A . n 
A 1 146 SER 146 145 145 SER SER A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 THR 149 148 148 THR THR A . n 
A 1 150 ARG 150 149 149 ARG ARG A . n 
A 1 151 GLN 151 150 150 GLN GLN A . n 
A 1 152 GLY 152 151 151 GLY GLY A . n 
A 1 153 VAL 153 152 152 VAL VAL A . n 
A 1 154 ASP 154 153 153 ASP ASP A . n 
A 1 155 ASP 155 154 154 ASP ASP A . n 
A 1 156 ALA 156 155 155 ALA ALA A . n 
A 1 157 PHE 157 156 156 PHE PHE A . n 
A 1 158 TYR 158 157 157 TYR TYR A . n 
A 1 159 THR 159 158 158 THR THR A . n 
A 1 160 LEU 160 159 159 LEU LEU A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 ARG 162 161 161 ARG ARG A . n 
A 1 163 GLU 163 162 162 GLU GLU A . n 
A 1 164 ILE 164 163 163 ILE ILE A . n 
A 1 165 ARG 165 164 164 ARG ARG A . n 
A 1 166 LYS 166 165 165 LYS LYS A . n 
A 1 167 HIS 167 166 166 HIS HIS A . n 
A 1 168 LYS 168 167 167 LYS LYS A . n 
A 1 169 GLU 169 168 ?   ?   ?   A . n 
A 1 170 LYS 170 169 ?   ?   ?   A . n 
B 1 1   SER 1   0   0   SER SER B . n 
B 1 2   MET 2   1   1   MET MET B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   GLU 4   3   3   GLU GLU B . n 
B 1 5   TYR 5   4   4   TYR TYR B . n 
B 1 6   LYS 6   5   5   LYS LYS B . n 
B 1 7   LEU 7   6   6   LEU LEU B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   VAL 9   8   8   VAL VAL B . n 
B 1 10  VAL 10  9   9   VAL VAL B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ALA 12  11  11  ALA ALA B . n 
B 1 13  VAL 13  12  12  VAL VAL B . n 
B 1 14  GLY 14  13  13  GLY GLY B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLY 16  15  15  GLY GLY B . n 
B 1 17  LYS 17  16  16  LYS LYS B . n 
B 1 18  SER 18  17  17  SER SER B . n 
B 1 19  ALA 19  18  18  ALA ALA B . n 
B 1 20  LEU 20  19  19  LEU LEU B . n 
B 1 21  THR 21  20  20  THR THR B . n 
B 1 22  ILE 22  21  21  ILE ILE B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LEU 24  23  23  LEU LEU B . n 
B 1 25  ILE 25  24  24  ILE ILE B . n 
B 1 26  GLN 26  25  25  GLN GLN B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  HIS 28  27  27  HIS HIS B . n 
B 1 29  PHE 29  28  28  PHE PHE B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  ASP 31  30  30  ASP ASP B . n 
B 1 32  GLU 32  31  31  GLU GLU B . n 
B 1 33  TYR 33  32  32  TYR TYR B . n 
B 1 34  ASP 34  33  33  ASP ASP B . n 
B 1 35  PRO 35  34  34  PRO PRO B . n 
B 1 36  THR 36  35  35  THR THR B . n 
B 1 37  ILE 37  36  36  ILE ILE B . n 
B 1 38  GLU 38  37  37  GLU GLU B . n 
B 1 39  ASP 39  38  38  ASP ASP B . n 
B 1 40  SER 40  39  39  SER SER B . n 
B 1 41  TYR 41  40  40  TYR TYR B . n 
B 1 42  ARG 42  41  41  ARG ARG B . n 
B 1 43  LYS 43  42  42  LYS LYS B . n 
B 1 44  GLN 44  43  43  GLN GLN B . n 
B 1 45  VAL 45  44  44  VAL VAL B . n 
B 1 46  VAL 46  45  45  VAL VAL B . n 
B 1 47  ILE 47  46  46  ILE ILE B . n 
B 1 48  ASP 48  47  47  ASP ASP B . n 
B 1 49  GLY 49  48  48  GLY GLY B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  THR 51  50  50  THR THR B . n 
B 1 52  CYS 52  51  51  CYS CYS B . n 
B 1 53  LEU 53  52  52  LEU LEU B . n 
B 1 54  LEU 54  53  53  LEU LEU B . n 
B 1 55  ASP 55  54  54  ASP ASP B . n 
B 1 56  ILE 56  55  55  ILE ILE B . n 
B 1 57  LEU 57  56  56  LEU LEU B . n 
B 1 58  ASP 58  57  57  ASP ASP B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  ALA 60  59  59  ALA ALA B . n 
B 1 61  GLY 61  60  60  GLY GLY B . n 
B 1 62  GLN 62  61  61  GLN GLN B . n 
B 1 63  GLU 63  62  62  GLU GLU B . n 
B 1 64  GLU 64  63  63  GLU GLU B . n 
B 1 65  TYR 65  64  64  TYR TYR B . n 
B 1 66  SER 66  65  65  SER SER B . n 
B 1 67  ALA 67  66  66  ALA ALA B . n 
B 1 68  MET 68  67  67  MET MET B . n 
B 1 69  ARG 69  68  68  ARG ARG B . n 
B 1 70  ASP 70  69  69  ASP ASP B . n 
B 1 71  GLN 71  70  70  GLN GLN B . n 
B 1 72  TYR 72  71  71  TYR TYR B . n 
B 1 73  MET 73  72  72  MET MET B . n 
B 1 74  ARG 74  73  73  ARG ARG B . n 
B 1 75  THR 75  74  74  THR THR B . n 
B 1 76  GLY 76  75  75  GLY GLY B . n 
B 1 77  GLU 77  76  76  GLU GLU B . n 
B 1 78  GLY 78  77  77  GLY GLY B . n 
B 1 79  PHE 79  78  78  PHE PHE B . n 
B 1 80  LEU 80  79  79  LEU LEU B . n 
B 1 81  CYS 81  80  80  CYS CYS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  PHE 83  82  82  PHE PHE B . n 
B 1 84  ALA 84  83  83  ALA ALA B . n 
B 1 85  ILE 85  84  84  ILE ILE B . n 
B 1 86  ASN 86  85  85  ASN ASN B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  THR 88  87  87  THR THR B . n 
B 1 89  LYS 89  88  88  LYS LYS B . n 
B 1 90  SER 90  89  89  SER SER B . n 
B 1 91  PHE 91  90  90  PHE PHE B . n 
B 1 92  GLU 92  91  91  GLU GLU B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  ILE 94  93  93  ILE ILE B . n 
B 1 95  HIS 95  94  94  HIS HIS B . n 
B 1 96  HIS 96  95  95  HIS HIS B . n 
B 1 97  TYR 97  96  96  TYR TYR B . n 
B 1 98  ARG 98  97  97  ARG ARG B . n 
B 1 99  GLU 99  98  98  GLU GLU B . n 
B 1 100 GLN 100 99  99  GLN GLN B . n 
B 1 101 ILE 101 100 100 ILE ILE B . n 
B 1 102 LYS 102 101 101 LYS LYS B . n 
B 1 103 ARG 103 102 102 ARG ARG B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 LYS 105 104 104 LYS LYS B . n 
B 1 106 ASP 106 105 105 ASP ASP B . n 
B 1 107 SER 107 106 106 SER SER B . n 
B 1 108 GLU 108 107 107 GLU GLU B . n 
B 1 109 ASP 109 108 108 ASP ASP B . n 
B 1 110 VAL 110 109 109 VAL VAL B . n 
B 1 111 PRO 111 110 110 PRO PRO B . n 
B 1 112 MET 112 111 111 MET MET B . n 
B 1 113 VAL 113 112 112 VAL VAL B . n 
B 1 114 LEU 114 113 113 LEU LEU B . n 
B 1 115 VAL 115 114 114 VAL VAL B . n 
B 1 116 GLY 116 115 115 GLY GLY B . n 
B 1 117 ASN 117 116 116 ASN ASN B . n 
B 1 118 LYS 118 117 117 LYS LYS B . n 
B 1 119 CYS 119 118 118 CYS CYS B . n 
B 1 120 ASP 120 119 119 ASP ASP B . n 
B 1 121 LEU 121 120 120 LEU LEU B . n 
B 1 122 PRO 122 121 121 PRO PRO B . n 
B 1 123 SER 123 122 122 SER SER B . n 
B 1 124 ARG 124 123 123 ARG ARG B . n 
B 1 125 THR 125 124 124 THR THR B . n 
B 1 126 VAL 126 125 125 VAL VAL B . n 
B 1 127 ASP 127 126 126 ASP ASP B . n 
B 1 128 THR 128 127 127 THR THR B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLN 130 129 129 GLN GLN B . n 
B 1 131 ALA 131 130 130 ALA ALA B . n 
B 1 132 GLN 132 131 131 GLN GLN B . n 
B 1 133 ASP 133 132 132 ASP ASP B . n 
B 1 134 LEU 134 133 133 LEU LEU B . n 
B 1 135 ALA 135 134 134 ALA ALA B . n 
B 1 136 ARG 136 135 135 ARG ARG B . n 
B 1 137 SER 137 136 136 SER SER B . n 
B 1 138 TYR 138 137 137 TYR TYR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ILE 140 139 139 ILE ILE B . n 
B 1 141 PRO 141 140 140 PRO PRO B . n 
B 1 142 PHE 142 141 141 PHE PHE B . n 
B 1 143 ILE 143 142 142 ILE ILE B . n 
B 1 144 GLU 144 143 143 GLU GLU B . n 
B 1 145 THR 145 144 144 THR THR B . n 
B 1 146 SER 146 145 145 SER SER B . n 
B 1 147 ALA 147 146 146 ALA ALA B . n 
B 1 148 LYS 148 147 147 LYS LYS B . n 
B 1 149 THR 149 148 148 THR THR B . n 
B 1 150 ARG 150 149 149 ARG ARG B . n 
B 1 151 GLN 151 150 150 GLN GLN B . n 
B 1 152 GLY 152 151 151 GLY GLY B . n 
B 1 153 VAL 153 152 152 VAL VAL B . n 
B 1 154 ASP 154 153 153 ASP ASP B . n 
B 1 155 ASP 155 154 154 ASP ASP B . n 
B 1 156 ALA 156 155 155 ALA ALA B . n 
B 1 157 PHE 157 156 156 PHE PHE B . n 
B 1 158 TYR 158 157 157 TYR TYR B . n 
B 1 159 THR 159 158 158 THR THR B . n 
B 1 160 LEU 160 159 159 LEU LEU B . n 
B 1 161 VAL 161 160 160 VAL VAL B . n 
B 1 162 ARG 162 161 161 ARG ARG B . n 
B 1 163 GLU 163 162 162 GLU GLU B . n 
B 1 164 ILE 164 163 163 ILE ILE B . n 
B 1 165 ARG 165 164 164 ARG ARG B . n 
B 1 166 LYS 166 165 165 LYS LYS B . n 
B 1 167 HIS 167 166 166 HIS HIS B . n 
B 1 168 LYS 168 167 167 LYS LYS B . n 
B 1 169 GLU 169 168 ?   ?   ?   B . n 
B 1 170 LYS 170 169 ?   ?   ?   B . n 
C 2 1   SER 1   0   ?   ?   ?   C . n 
C 2 2   MET 2   1   ?   ?   ?   C . n 
C 2 3   VAL 3   2   2   VAL VAL C . n 
C 2 4   ASN 4   3   3   ASN ASN C . n 
C 2 5   PRO 5   4   4   PRO PRO C . n 
C 2 6   THR 6   5   5   THR THR C . n 
C 2 7   VAL 7   6   6   VAL VAL C . n 
C 2 8   PHE 8   7   7   PHE PHE C . n 
C 2 9   PHE 9   8   8   PHE PHE C . n 
C 2 10  ASP 10  9   9   ASP ASP C . n 
C 2 11  ILE 11  10  10  ILE ILE C . n 
C 2 12  ALA 12  11  11  ALA ALA C . n 
C 2 13  VAL 13  12  12  VAL VAL C . n 
C 2 14  ASP 14  13  13  ASP ASP C . n 
C 2 15  GLY 15  14  14  GLY GLY C . n 
C 2 16  GLU 16  15  15  GLU GLU C . n 
C 2 17  PRO 17  16  16  PRO PRO C . n 
C 2 18  LEU 18  17  17  LEU LEU C . n 
C 2 19  GLY 19  18  18  GLY GLY C . n 
C 2 20  ARG 20  19  19  ARG ARG C . n 
C 2 21  VAL 21  20  20  VAL VAL C . n 
C 2 22  SER 22  21  21  SER SER C . n 
C 2 23  PHE 23  22  22  PHE PHE C . n 
C 2 24  GLU 24  23  23  GLU GLU C . n 
C 2 25  LEU 25  24  24  LEU LEU C . n 
C 2 26  PHE 26  25  25  PHE PHE C . n 
C 2 27  ALA 27  26  26  ALA ALA C . n 
C 2 28  ASP 28  27  27  ASP ASP C . n 
C 2 29  LYS 29  28  28  LYS LYS C . n 
C 2 30  VAL 30  29  29  VAL VAL C . n 
C 2 31  PRO 31  30  30  PRO PRO C . n 
C 2 32  LYS 32  31  31  LYS LYS C . n 
C 2 33  THR 33  32  32  THR THR C . n 
C 2 34  ALA 34  33  33  ALA ALA C . n 
C 2 35  GLU 35  34  34  GLU GLU C . n 
C 2 36  ASN 36  35  35  ASN ASN C . n 
C 2 37  PHE 37  36  36  PHE PHE C . n 
C 2 38  ARG 38  37  37  ARG ARG C . n 
C 2 39  ALA 39  38  38  ALA ALA C . n 
C 2 40  LEU 40  39  39  LEU LEU C . n 
C 2 41  SER 41  40  40  SER SER C . n 
C 2 42  THR 42  41  41  THR THR C . n 
C 2 43  GLY 43  42  42  GLY GLY C . n 
C 2 44  GLU 44  43  43  GLU GLU C . n 
C 2 45  LYS 45  44  44  LYS LYS C . n 
C 2 46  GLY 46  45  45  GLY GLY C . n 
C 2 47  PHE 47  46  46  PHE PHE C . n 
C 2 48  GLY 48  47  47  GLY GLY C . n 
C 2 49  TYR 49  48  48  TYR TYR C . n 
C 2 50  LYS 50  49  49  LYS LYS C . n 
C 2 51  GLY 51  50  50  GLY GLY C . n 
C 2 52  SER 52  51  51  SER SER C . n 
C 2 53  CYS 53  52  52  CYS CYS C . n 
C 2 54  PHE 54  53  53  PHE PHE C . n 
C 2 55  HIS 55  54  54  HIS HIS C . n 
C 2 56  ARG 56  55  55  ARG ARG C . n 
C 2 57  ILE 57  56  56  ILE ILE C . n 
C 2 58  ILE 58  57  57  ILE ILE C . n 
C 2 59  PRO 59  58  58  PRO PRO C . n 
C 2 60  GLY 60  59  59  GLY GLY C . n 
C 2 61  PHE 61  60  60  PHE PHE C . n 
C 2 62  MET 62  61  61  MET MET C . n 
C 2 63  CYS 63  62  62  CYS CYS C . n 
C 2 64  GLN 64  63  63  GLN GLN C . n 
C 2 65  GLY 65  64  64  GLY GLY C . n 
C 2 66  GLY 66  65  65  GLY GLY C . n 
C 2 67  ASP 67  66  66  ASP ASP C . n 
C 2 68  PHE 68  67  67  PHE PHE C . n 
C 2 69  THR 69  68  68  THR THR C . n 
C 2 70  ARG 70  69  69  ARG ARG C . n 
C 2 71  HIS 71  70  70  HIS HIS C . n 
C 2 72  ASN 72  71  71  ASN ASN C . n 
C 2 73  GLY 73  72  72  GLY GLY C . n 
C 2 74  THR 74  73  73  THR THR C . n 
C 2 75  GLY 75  74  74  GLY GLY C . n 
C 2 76  GLY 76  75  75  GLY GLY C . n 
C 2 77  LYS 77  76  76  LYS LYS C . n 
C 2 78  SER 78  77  77  SER SER C . n 
C 2 79  ILE 79  78  78  ILE ILE C . n 
C 2 80  TYR 80  79  79  TYR TYR C . n 
C 2 81  GLY 81  80  80  GLY GLY C . n 
C 2 82  GLU 82  81  81  GLU GLU C . n 
C 2 83  LYS 83  82  82  LYS LYS C . n 
C 2 84  PHE 84  83  83  PHE PHE C . n 
C 2 85  GLU 85  84  84  GLU GLU C . n 
C 2 86  ASP 86  85  85  ASP ASP C . n 
C 2 87  GLU 87  86  86  GLU GLU C . n 
C 2 88  ASN 88  87  87  ASN ASN C . n 
C 2 89  PHE 89  88  88  PHE PHE C . n 
C 2 90  ILE 90  89  89  ILE ILE C . n 
C 2 91  LEU 91  90  90  LEU LEU C . n 
C 2 92  LYS 92  91  91  LYS LYS C . n 
C 2 93  HIS 93  92  92  HIS HIS C . n 
C 2 94  THR 94  93  93  THR THR C . n 
C 2 95  GLY 95  94  94  GLY GLY C . n 
C 2 96  PRO 96  95  95  PRO PRO C . n 
C 2 97  GLY 97  96  96  GLY GLY C . n 
C 2 98  ILE 98  97  97  ILE ILE C . n 
C 2 99  LEU 99  98  98  LEU LEU C . n 
C 2 100 SER 100 99  99  SER SER C . n 
C 2 101 MET 101 100 100 MET MET C . n 
C 2 102 ALA 102 101 101 ALA ALA C . n 
C 2 103 ASN 103 102 102 ASN ASN C . n 
C 2 104 ALA 104 103 103 ALA ALA C . n 
C 2 105 GLY 105 104 104 GLY GLY C . n 
C 2 106 PRO 106 105 105 PRO PRO C . n 
C 2 107 ASN 107 106 106 ASN ASN C . n 
C 2 108 THR 108 107 107 THR THR C . n 
C 2 109 ASN 109 108 108 ASN ASN C . n 
C 2 110 GLY 110 109 109 GLY GLY C . n 
C 2 111 SER 111 110 110 SER SER C . n 
C 2 112 GLN 112 111 111 GLN GLN C . n 
C 2 113 PHE 113 112 112 PHE PHE C . n 
C 2 114 PHE 114 113 113 PHE PHE C . n 
C 2 115 ILE 115 114 114 ILE ILE C . n 
C 2 116 CYS 116 115 115 CYS CYS C . n 
C 2 117 THR 117 116 116 THR THR C . n 
C 2 118 ALA 118 117 117 ALA ALA C . n 
C 2 119 LYS 119 118 118 LYS LYS C . n 
C 2 120 THR 120 119 119 THR THR C . n 
C 2 121 GLU 121 120 120 GLU GLU C . n 
C 2 122 TRP 122 121 121 TRP TRP C . n 
C 2 123 LEU 123 122 122 LEU LEU C . n 
C 2 124 ASP 124 123 123 ASP ASP C . n 
C 2 125 GLY 125 124 124 GLY GLY C . n 
C 2 126 LYS 126 125 125 LYS LYS C . n 
C 2 127 HIS 127 126 126 HIS HIS C . n 
C 2 128 VAL 128 127 127 VAL VAL C . n 
C 2 129 VAL 129 128 128 VAL VAL C . n 
C 2 130 PHE 130 129 129 PHE PHE C . n 
C 2 131 GLY 131 130 130 GLY GLY C . n 
C 2 132 LYS 132 131 131 LYS LYS C . n 
C 2 133 VAL 133 132 132 VAL VAL C . n 
C 2 134 LYS 134 133 133 LYS LYS C . n 
C 2 135 GLU 135 134 134 GLU GLU C . n 
C 2 136 GLY 136 135 135 GLY GLY C . n 
C 2 137 MET 137 136 136 MET MET C . n 
C 2 138 ASN 138 137 137 ASN ASN C . n 
C 2 139 ILE 139 138 138 ILE ILE C . n 
C 2 140 VAL 140 139 139 VAL VAL C . n 
C 2 141 GLU 141 140 140 GLU GLU C . n 
C 2 142 ALA 142 141 141 ALA ALA C . n 
C 2 143 MET 143 142 142 MET MET C . n 
C 2 144 GLU 144 143 143 GLU GLU C . n 
C 2 145 ARG 145 144 144 ARG ARG C . n 
C 2 146 PHE 146 145 145 PHE PHE C . n 
C 2 147 GLY 147 146 146 GLY GLY C . n 
C 2 148 SER 148 147 147 SER SER C . n 
C 2 149 ARG 149 148 148 ARG ARG C . n 
C 2 150 ASN 150 149 149 ASN ASN C . n 
C 2 151 GLY 151 150 150 GLY GLY C . n 
C 2 152 LYS 152 151 151 LYS LYS C . n 
C 2 153 THR 153 152 152 THR THR C . n 
C 2 154 SER 154 153 153 SER SER C . n 
C 2 155 LYS 155 154 154 LYS LYS C . n 
C 2 156 LYS 156 155 155 LYS LYS C . n 
C 2 157 ILE 157 156 156 ILE ILE C . n 
C 2 158 THR 158 157 157 THR THR C . n 
C 2 159 ILE 159 158 158 ILE ILE C . n 
C 2 160 ALA 160 159 159 ALA ALA C . n 
C 2 161 ASP 161 160 160 ASP ASP C . n 
C 2 162 CYS 162 161 161 CYS CYS C . n 
C 2 163 GLY 163 162 162 GLY GLY C . n 
C 2 164 GLN 164 163 163 GLN GLN C . n 
C 2 165 LEU 165 164 164 LEU LEU C . n 
C 2 166 GLU 166 165 ?   ?   ?   C . n 
D 2 1   SER 1   0   ?   ?   ?   D . n 
D 2 2   MET 2   1   ?   ?   ?   D . n 
D 2 3   VAL 3   2   ?   ?   ?   D . n 
D 2 4   ASN 4   3   3   ASN ASN D . n 
D 2 5   PRO 5   4   4   PRO PRO D . n 
D 2 6   THR 6   5   5   THR THR D . n 
D 2 7   VAL 7   6   6   VAL VAL D . n 
D 2 8   PHE 8   7   7   PHE PHE D . n 
D 2 9   PHE 9   8   8   PHE PHE D . n 
D 2 10  ASP 10  9   9   ASP ASP D . n 
D 2 11  ILE 11  10  10  ILE ILE D . n 
D 2 12  ALA 12  11  11  ALA ALA D . n 
D 2 13  VAL 13  12  12  VAL VAL D . n 
D 2 14  ASP 14  13  13  ASP ASP D . n 
D 2 15  GLY 15  14  14  GLY GLY D . n 
D 2 16  GLU 16  15  15  GLU GLU D . n 
D 2 17  PRO 17  16  16  PRO PRO D . n 
D 2 18  LEU 18  17  17  LEU LEU D . n 
D 2 19  GLY 19  18  18  GLY GLY D . n 
D 2 20  ARG 20  19  19  ARG ARG D . n 
D 2 21  VAL 21  20  20  VAL VAL D . n 
D 2 22  SER 22  21  21  SER SER D . n 
D 2 23  PHE 23  22  22  PHE PHE D . n 
D 2 24  GLU 24  23  23  GLU GLU D . n 
D 2 25  LEU 25  24  24  LEU LEU D . n 
D 2 26  PHE 26  25  25  PHE PHE D . n 
D 2 27  ALA 27  26  26  ALA ALA D . n 
D 2 28  ASP 28  27  27  ASP ASP D . n 
D 2 29  LYS 29  28  28  LYS LYS D . n 
D 2 30  VAL 30  29  29  VAL VAL D . n 
D 2 31  PRO 31  30  30  PRO PRO D . n 
D 2 32  LYS 32  31  31  LYS LYS D . n 
D 2 33  THR 33  32  32  THR THR D . n 
D 2 34  ALA 34  33  33  ALA ALA D . n 
D 2 35  GLU 35  34  34  GLU GLU D . n 
D 2 36  ASN 36  35  35  ASN ASN D . n 
D 2 37  PHE 37  36  36  PHE PHE D . n 
D 2 38  ARG 38  37  37  ARG ARG D . n 
D 2 39  ALA 39  38  38  ALA ALA D . n 
D 2 40  LEU 40  39  39  LEU LEU D . n 
D 2 41  SER 41  40  40  SER SER D . n 
D 2 42  THR 42  41  41  THR THR D . n 
D 2 43  GLY 43  42  42  GLY GLY D . n 
D 2 44  GLU 44  43  43  GLU GLU D . n 
D 2 45  LYS 45  44  44  LYS LYS D . n 
D 2 46  GLY 46  45  45  GLY GLY D . n 
D 2 47  PHE 47  46  46  PHE PHE D . n 
D 2 48  GLY 48  47  47  GLY GLY D . n 
D 2 49  TYR 49  48  48  TYR TYR D . n 
D 2 50  LYS 50  49  49  LYS LYS D . n 
D 2 51  GLY 51  50  50  GLY GLY D . n 
D 2 52  SER 52  51  51  SER SER D . n 
D 2 53  CYS 53  52  52  CYS CYS D . n 
D 2 54  PHE 54  53  53  PHE PHE D . n 
D 2 55  HIS 55  54  54  HIS HIS D . n 
D 2 56  ARG 56  55  55  ARG ARG D . n 
D 2 57  ILE 57  56  56  ILE ILE D . n 
D 2 58  ILE 58  57  57  ILE ILE D . n 
D 2 59  PRO 59  58  58  PRO PRO D . n 
D 2 60  GLY 60  59  59  GLY GLY D . n 
D 2 61  PHE 61  60  60  PHE PHE D . n 
D 2 62  MET 62  61  61  MET MET D . n 
D 2 63  CYS 63  62  62  CYS CYS D . n 
D 2 64  GLN 64  63  63  GLN GLN D . n 
D 2 65  GLY 65  64  64  GLY GLY D . n 
D 2 66  GLY 66  65  65  GLY GLY D . n 
D 2 67  ASP 67  66  66  ASP ASP D . n 
D 2 68  PHE 68  67  67  PHE PHE D . n 
D 2 69  THR 69  68  68  THR THR D . n 
D 2 70  ARG 70  69  69  ARG ARG D . n 
D 2 71  HIS 71  70  70  HIS HIS D . n 
D 2 72  ASN 72  71  71  ASN ASN D . n 
D 2 73  GLY 73  72  72  GLY GLY D . n 
D 2 74  THR 74  73  73  THR THR D . n 
D 2 75  GLY 75  74  74  GLY GLY D . n 
D 2 76  GLY 76  75  75  GLY GLY D . n 
D 2 77  LYS 77  76  76  LYS LYS D . n 
D 2 78  SER 78  77  77  SER SER D . n 
D 2 79  ILE 79  78  78  ILE ILE D . n 
D 2 80  TYR 80  79  79  TYR TYR D . n 
D 2 81  GLY 81  80  80  GLY GLY D . n 
D 2 82  GLU 82  81  81  GLU GLU D . n 
D 2 83  LYS 83  82  82  LYS LYS D . n 
D 2 84  PHE 84  83  83  PHE PHE D . n 
D 2 85  GLU 85  84  84  GLU GLU D . n 
D 2 86  ASP 86  85  85  ASP ASP D . n 
D 2 87  GLU 87  86  86  GLU GLU D . n 
D 2 88  ASN 88  87  87  ASN ASN D . n 
D 2 89  PHE 89  88  88  PHE PHE D . n 
D 2 90  ILE 90  89  89  ILE ILE D . n 
D 2 91  LEU 91  90  90  LEU LEU D . n 
D 2 92  LYS 92  91  91  LYS LYS D . n 
D 2 93  HIS 93  92  92  HIS HIS D . n 
D 2 94  THR 94  93  93  THR THR D . n 
D 2 95  GLY 95  94  94  GLY GLY D . n 
D 2 96  PRO 96  95  95  PRO PRO D . n 
D 2 97  GLY 97  96  96  GLY GLY D . n 
D 2 98  ILE 98  97  97  ILE ILE D . n 
D 2 99  LEU 99  98  98  LEU LEU D . n 
D 2 100 SER 100 99  99  SER SER D . n 
D 2 101 MET 101 100 100 MET MET D . n 
D 2 102 ALA 102 101 101 ALA ALA D . n 
D 2 103 ASN 103 102 102 ASN ASN D . n 
D 2 104 ALA 104 103 103 ALA ALA D . n 
D 2 105 GLY 105 104 104 GLY GLY D . n 
D 2 106 PRO 106 105 105 PRO PRO D . n 
D 2 107 ASN 107 106 106 ASN ASN D . n 
D 2 108 THR 108 107 107 THR THR D . n 
D 2 109 ASN 109 108 108 ASN ASN D . n 
D 2 110 GLY 110 109 109 GLY GLY D . n 
D 2 111 SER 111 110 110 SER SER D . n 
D 2 112 GLN 112 111 111 GLN GLN D . n 
D 2 113 PHE 113 112 112 PHE PHE D . n 
D 2 114 PHE 114 113 113 PHE PHE D . n 
D 2 115 ILE 115 114 114 ILE ILE D . n 
D 2 116 CYS 116 115 115 CYS CYS D . n 
D 2 117 THR 117 116 116 THR THR D . n 
D 2 118 ALA 118 117 117 ALA ALA D . n 
D 2 119 LYS 119 118 118 LYS LYS D . n 
D 2 120 THR 120 119 119 THR THR D . n 
D 2 121 GLU 121 120 120 GLU GLU D . n 
D 2 122 TRP 122 121 121 TRP TRP D . n 
D 2 123 LEU 123 122 122 LEU LEU D . n 
D 2 124 ASP 124 123 123 ASP ASP D . n 
D 2 125 GLY 125 124 124 GLY GLY D . n 
D 2 126 LYS 126 125 125 LYS LYS D . n 
D 2 127 HIS 127 126 126 HIS HIS D . n 
D 2 128 VAL 128 127 127 VAL VAL D . n 
D 2 129 VAL 129 128 128 VAL VAL D . n 
D 2 130 PHE 130 129 129 PHE PHE D . n 
D 2 131 GLY 131 130 130 GLY GLY D . n 
D 2 132 LYS 132 131 131 LYS LYS D . n 
D 2 133 VAL 133 132 132 VAL VAL D . n 
D 2 134 LYS 134 133 133 LYS LYS D . n 
D 2 135 GLU 135 134 134 GLU GLU D . n 
D 2 136 GLY 136 135 135 GLY GLY D . n 
D 2 137 MET 137 136 136 MET MET D . n 
D 2 138 ASN 138 137 137 ASN ASN D . n 
D 2 139 ILE 139 138 138 ILE ILE D . n 
D 2 140 VAL 140 139 139 VAL VAL D . n 
D 2 141 GLU 141 140 140 GLU GLU D . n 
D 2 142 ALA 142 141 141 ALA ALA D . n 
D 2 143 MET 143 142 142 MET MET D . n 
D 2 144 GLU 144 143 143 GLU GLU D . n 
D 2 145 ARG 145 144 144 ARG ARG D . n 
D 2 146 PHE 146 145 145 PHE PHE D . n 
D 2 147 GLY 147 146 146 GLY GLY D . n 
D 2 148 SER 148 147 147 SER SER D . n 
D 2 149 ARG 149 148 148 ARG ARG D . n 
D 2 150 ASN 150 149 149 ASN ASN D . n 
D 2 151 GLY 151 150 150 GLY GLY D . n 
D 2 152 LYS 152 151 151 LYS LYS D . n 
D 2 153 THR 153 152 152 THR THR D . n 
D 2 154 SER 154 153 153 SER SER D . n 
D 2 155 LYS 155 154 154 LYS LYS D . n 
D 2 156 LYS 156 155 155 LYS LYS D . n 
D 2 157 ILE 157 156 156 ILE ILE D . n 
D 2 158 THR 158 157 157 THR THR D . n 
D 2 159 ILE 159 158 158 ILE ILE D . n 
D 2 160 ALA 160 159 159 ALA ALA D . n 
D 2 161 ASP 161 160 160 ASP ASP D . n 
D 2 162 CYS 162 161 161 CYS CYS D . n 
D 2 163 GLY 163 162 162 GLY GLY D . n 
D 2 164 GLN 164 163 163 GLN GLN D . n 
D 2 165 LEU 165 164 164 LEU LEU D . n 
D 2 166 GLU 166 165 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AOJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AOJ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 GNP   1   201 201  GNP   GNP A . 
F 4 MG    1   202 301  MG    MG  A . 
G 3 GNP   1   201 201  GNP   GNP B . 
H 4 MG    1   202 301  MG    MG  B . 
I 5 A1AOJ 1   201 5766 A1AOJ RMC C . 
J 5 A1AOJ 1   201 5766 A1AOJ RMC D . 
K 6 HOH   1   301 623  HOH   HOH A . 
K 6 HOH   2   302 360  HOH   HOH A . 
K 6 HOH   3   303 138  HOH   HOH A . 
K 6 HOH   4   304 228  HOH   HOH A . 
K 6 HOH   5   305 315  HOH   HOH A . 
K 6 HOH   6   306 636  HOH   HOH A . 
K 6 HOH   7   307 139  HOH   HOH A . 
K 6 HOH   8   308 183  HOH   HOH A . 
K 6 HOH   9   309 553  HOH   HOH A . 
K 6 HOH   10  310 111  HOH   HOH A . 
K 6 HOH   11  311 46   HOH   HOH A . 
K 6 HOH   12  312 54   HOH   HOH A . 
K 6 HOH   13  313 359  HOH   HOH A . 
K 6 HOH   14  314 15   HOH   HOH A . 
K 6 HOH   15  315 473  HOH   HOH A . 
K 6 HOH   16  316 295  HOH   HOH A . 
K 6 HOH   17  317 344  HOH   HOH A . 
K 6 HOH   18  318 286  HOH   HOH A . 
K 6 HOH   19  319 2    HOH   HOH A . 
K 6 HOH   20  320 135  HOH   HOH A . 
K 6 HOH   21  321 426  HOH   HOH A . 
K 6 HOH   22  322 107  HOH   HOH A . 
K 6 HOH   23  323 193  HOH   HOH A . 
K 6 HOH   24  324 140  HOH   HOH A . 
K 6 HOH   25  325 68   HOH   HOH A . 
K 6 HOH   26  326 565  HOH   HOH A . 
K 6 HOH   27  327 431  HOH   HOH A . 
K 6 HOH   28  328 45   HOH   HOH A . 
K 6 HOH   29  329 53   HOH   HOH A . 
K 6 HOH   30  330 555  HOH   HOH A . 
K 6 HOH   31  331 225  HOH   HOH A . 
K 6 HOH   32  332 72   HOH   HOH A . 
K 6 HOH   33  333 5    HOH   HOH A . 
K 6 HOH   34  334 59   HOH   HOH A . 
K 6 HOH   35  335 10   HOH   HOH A . 
K 6 HOH   36  336 552  HOH   HOH A . 
K 6 HOH   37  337 618  HOH   HOH A . 
K 6 HOH   38  338 589  HOH   HOH A . 
K 6 HOH   39  339 370  HOH   HOH A . 
K 6 HOH   40  340 38   HOH   HOH A . 
K 6 HOH   41  341 593  HOH   HOH A . 
K 6 HOH   42  342 137  HOH   HOH A . 
K 6 HOH   43  343 121  HOH   HOH A . 
K 6 HOH   44  344 251  HOH   HOH A . 
K 6 HOH   45  345 52   HOH   HOH A . 
K 6 HOH   46  346 1    HOH   HOH A . 
K 6 HOH   47  347 37   HOH   HOH A . 
K 6 HOH   48  348 654  HOH   HOH A . 
K 6 HOH   49  349 30   HOH   HOH A . 
K 6 HOH   50  350 346  HOH   HOH A . 
K 6 HOH   51  351 93   HOH   HOH A . 
K 6 HOH   52  352 244  HOH   HOH A . 
K 6 HOH   53  353 401  HOH   HOH A . 
K 6 HOH   54  354 585  HOH   HOH A . 
K 6 HOH   55  355 145  HOH   HOH A . 
K 6 HOH   56  356 672  HOH   HOH A . 
K 6 HOH   57  357 425  HOH   HOH A . 
K 6 HOH   58  358 366  HOH   HOH A . 
K 6 HOH   59  359 391  HOH   HOH A . 
K 6 HOH   60  360 615  HOH   HOH A . 
K 6 HOH   61  361 643  HOH   HOH A . 
K 6 HOH   62  362 515  HOH   HOH A . 
K 6 HOH   63  363 124  HOH   HOH A . 
K 6 HOH   64  364 418  HOH   HOH A . 
K 6 HOH   65  365 413  HOH   HOH A . 
K 6 HOH   66  366 85   HOH   HOH A . 
K 6 HOH   67  367 569  HOH   HOH A . 
K 6 HOH   68  368 416  HOH   HOH A . 
K 6 HOH   69  369 499  HOH   HOH A . 
K 6 HOH   70  370 511  HOH   HOH A . 
K 6 HOH   71  371 383  HOH   HOH A . 
K 6 HOH   72  372 322  HOH   HOH A . 
K 6 HOH   73  373 11   HOH   HOH A . 
K 6 HOH   74  374 43   HOH   HOH A . 
K 6 HOH   75  375 205  HOH   HOH A . 
K 6 HOH   76  376 217  HOH   HOH A . 
K 6 HOH   77  377 483  HOH   HOH A . 
K 6 HOH   78  378 577  HOH   HOH A . 
K 6 HOH   79  379 436  HOH   HOH A . 
K 6 HOH   80  380 87   HOH   HOH A . 
K 6 HOH   81  381 650  HOH   HOH A . 
K 6 HOH   82  382 21   HOH   HOH A . 
K 6 HOH   83  383 645  HOH   HOH A . 
K 6 HOH   84  384 305  HOH   HOH A . 
K 6 HOH   85  385 141  HOH   HOH A . 
K 6 HOH   86  386 187  HOH   HOH A . 
K 6 HOH   87  387 71   HOH   HOH A . 
K 6 HOH   88  388 348  HOH   HOH A . 
K 6 HOH   89  389 485  HOH   HOH A . 
K 6 HOH   90  390 219  HOH   HOH A . 
K 6 HOH   91  391 160  HOH   HOH A . 
K 6 HOH   92  392 95   HOH   HOH A . 
K 6 HOH   93  393 89   HOH   HOH A . 
K 6 HOH   94  394 489  HOH   HOH A . 
K 6 HOH   95  395 104  HOH   HOH A . 
K 6 HOH   96  396 23   HOH   HOH A . 
K 6 HOH   97  397 453  HOH   HOH A . 
K 6 HOH   98  398 564  HOH   HOH A . 
K 6 HOH   99  399 403  HOH   HOH A . 
K 6 HOH   100 400 450  HOH   HOH A . 
K 6 HOH   101 401 457  HOH   HOH A . 
K 6 HOH   102 402 201  HOH   HOH A . 
K 6 HOH   103 403 304  HOH   HOH A . 
K 6 HOH   104 404 203  HOH   HOH A . 
K 6 HOH   105 405 112  HOH   HOH A . 
K 6 HOH   106 406 649  HOH   HOH A . 
K 6 HOH   107 407 573  HOH   HOH A . 
K 6 HOH   108 408 109  HOH   HOH A . 
K 6 HOH   109 409 345  HOH   HOH A . 
K 6 HOH   110 410 281  HOH   HOH A . 
K 6 HOH   111 411 361  HOH   HOH A . 
K 6 HOH   112 412 487  HOH   HOH A . 
K 6 HOH   113 413 97   HOH   HOH A . 
K 6 HOH   114 414 601  HOH   HOH A . 
K 6 HOH   115 415 402  HOH   HOH A . 
K 6 HOH   116 416 535  HOH   HOH A . 
K 6 HOH   117 417 625  HOH   HOH A . 
K 6 HOH   118 418 62   HOH   HOH A . 
K 6 HOH   119 419 442  HOH   HOH A . 
K 6 HOH   120 420 380  HOH   HOH A . 
K 6 HOH   121 421 158  HOH   HOH A . 
K 6 HOH   122 422 545  HOH   HOH A . 
K 6 HOH   123 423 501  HOH   HOH A . 
K 6 HOH   124 424 598  HOH   HOH A . 
K 6 HOH   125 425 173  HOH   HOH A . 
K 6 HOH   126 426 556  HOH   HOH A . 
K 6 HOH   127 427 465  HOH   HOH A . 
K 6 HOH   128 428 587  HOH   HOH A . 
K 6 HOH   129 429 634  HOH   HOH A . 
K 6 HOH   130 430 641  HOH   HOH A . 
K 6 HOH   131 431 24   HOH   HOH A . 
K 6 HOH   132 432 653  HOH   HOH A . 
K 6 HOH   133 433 252  HOH   HOH A . 
K 6 HOH   134 434 446  HOH   HOH A . 
K 6 HOH   135 435 648  HOH   HOH A . 
K 6 HOH   136 436 372  HOH   HOH A . 
K 6 HOH   137 437 562  HOH   HOH A . 
K 6 HOH   138 438 142  HOH   HOH A . 
K 6 HOH   139 439 477  HOH   HOH A . 
K 6 HOH   140 440 379  HOH   HOH A . 
K 6 HOH   141 441 547  HOH   HOH A . 
K 6 HOH   142 442 337  HOH   HOH A . 
K 6 HOH   143 443 526  HOH   HOH A . 
K 6 HOH   144 444 523  HOH   HOH A . 
K 6 HOH   145 445 506  HOH   HOH A . 
K 6 HOH   146 446 605  HOH   HOH A . 
K 6 HOH   147 447 644  HOH   HOH A . 
K 6 HOH   148 448 356  HOH   HOH A . 
K 6 HOH   149 449 675  HOH   HOH A . 
K 6 HOH   150 450 122  HOH   HOH A . 
K 6 HOH   151 451 468  HOH   HOH A . 
K 6 HOH   152 452 437  HOH   HOH A . 
K 6 HOH   153 453 428  HOH   HOH A . 
K 6 HOH   154 454 291  HOH   HOH A . 
K 6 HOH   155 455 646  HOH   HOH A . 
K 6 HOH   156 456 144  HOH   HOH A . 
K 6 HOH   157 457 631  HOH   HOH A . 
K 6 HOH   158 458 331  HOH   HOH A . 
K 6 HOH   159 459 254  HOH   HOH A . 
K 6 HOH   160 460 394  HOH   HOH A . 
K 6 HOH   161 461 407  HOH   HOH A . 
K 6 HOH   162 462 302  HOH   HOH A . 
K 6 HOH   163 463 614  HOH   HOH A . 
K 6 HOH   164 464 298  HOH   HOH A . 
L 6 HOH   1   301 262  HOH   HOH B . 
L 6 HOH   2   302 312  HOH   HOH B . 
L 6 HOH   3   303 412  HOH   HOH B . 
L 6 HOH   4   304 324  HOH   HOH B . 
L 6 HOH   5   305 576  HOH   HOH B . 
L 6 HOH   6   306 434  HOH   HOH B . 
L 6 HOH   7   307 186  HOH   HOH B . 
L 6 HOH   8   308 204  HOH   HOH B . 
L 6 HOH   9   309 321  HOH   HOH B . 
L 6 HOH   10  310 215  HOH   HOH B . 
L 6 HOH   11  311 241  HOH   HOH B . 
L 6 HOH   12  312 129  HOH   HOH B . 
L 6 HOH   13  313 94   HOH   HOH B . 
L 6 HOH   14  314 6    HOH   HOH B . 
L 6 HOH   15  315 4    HOH   HOH B . 
L 6 HOH   16  316 630  HOH   HOH B . 
L 6 HOH   17  317 521  HOH   HOH B . 
L 6 HOH   18  318 524  HOH   HOH B . 
L 6 HOH   19  319 290  HOH   HOH B . 
L 6 HOH   20  320 96   HOH   HOH B . 
L 6 HOH   21  321 488  HOH   HOH B . 
L 6 HOH   22  322 3    HOH   HOH B . 
L 6 HOH   23  323 279  HOH   HOH B . 
L 6 HOH   24  324 81   HOH   HOH B . 
L 6 HOH   25  325 395  HOH   HOH B . 
L 6 HOH   26  326 541  HOH   HOH B . 
L 6 HOH   27  327 100  HOH   HOH B . 
L 6 HOH   28  328 249  HOH   HOH B . 
L 6 HOH   29  329 429  HOH   HOH B . 
L 6 HOH   30  330 261  HOH   HOH B . 
L 6 HOH   31  331 570  HOH   HOH B . 
L 6 HOH   32  332 114  HOH   HOH B . 
L 6 HOH   33  333 151  HOH   HOH B . 
L 6 HOH   34  334 103  HOH   HOH B . 
L 6 HOH   35  335 620  HOH   HOH B . 
L 6 HOH   36  336 343  HOH   HOH B . 
L 6 HOH   37  337 607  HOH   HOH B . 
L 6 HOH   38  338 387  HOH   HOH B . 
L 6 HOH   39  339 16   HOH   HOH B . 
L 6 HOH   40  340 189  HOH   HOH B . 
L 6 HOH   41  341 250  HOH   HOH B . 
L 6 HOH   42  342 480  HOH   HOH B . 
L 6 HOH   43  343 616  HOH   HOH B . 
L 6 HOH   44  344 113  HOH   HOH B . 
L 6 HOH   45  345 98   HOH   HOH B . 
L 6 HOH   46  346 174  HOH   HOH B . 
L 6 HOH   47  347 444  HOH   HOH B . 
L 6 HOH   48  348 463  HOH   HOH B . 
L 6 HOH   49  349 50   HOH   HOH B . 
L 6 HOH   50  350 274  HOH   HOH B . 
L 6 HOH   51  351 65   HOH   HOH B . 
L 6 HOH   52  352 673  HOH   HOH B . 
L 6 HOH   53  353 263  HOH   HOH B . 
L 6 HOH   54  354 656  HOH   HOH B . 
L 6 HOH   55  355 18   HOH   HOH B . 
L 6 HOH   56  356 332  HOH   HOH B . 
L 6 HOH   57  357 364  HOH   HOH B . 
L 6 HOH   58  358 404  HOH   HOH B . 
L 6 HOH   59  359 340  HOH   HOH B . 
L 6 HOH   60  360 25   HOH   HOH B . 
L 6 HOH   61  361 167  HOH   HOH B . 
L 6 HOH   62  362 438  HOH   HOH B . 
L 6 HOH   63  363 575  HOH   HOH B . 
L 6 HOH   64  364 537  HOH   HOH B . 
L 6 HOH   65  365 311  HOH   HOH B . 
L 6 HOH   66  366 329  HOH   HOH B . 
L 6 HOH   67  367 368  HOH   HOH B . 
L 6 HOH   68  368 452  HOH   HOH B . 
L 6 HOH   69  369 130  HOH   HOH B . 
L 6 HOH   70  370 76   HOH   HOH B . 
L 6 HOH   71  371 166  HOH   HOH B . 
L 6 HOH   72  372 287  HOH   HOH B . 
L 6 HOH   73  373 509  HOH   HOH B . 
L 6 HOH   74  374 92   HOH   HOH B . 
L 6 HOH   75  375 210  HOH   HOH B . 
L 6 HOH   76  376 415  HOH   HOH B . 
L 6 HOH   77  377 127  HOH   HOH B . 
L 6 HOH   78  378 48   HOH   HOH B . 
L 6 HOH   79  379 338  HOH   HOH B . 
L 6 HOH   80  380 221  HOH   HOH B . 
L 6 HOH   81  381 398  HOH   HOH B . 
L 6 HOH   82  382 550  HOH   HOH B . 
L 6 HOH   83  383 411  HOH   HOH B . 
L 6 HOH   84  384 462  HOH   HOH B . 
L 6 HOH   85  385 153  HOH   HOH B . 
L 6 HOH   86  386 116  HOH   HOH B . 
L 6 HOH   87  387 118  HOH   HOH B . 
L 6 HOH   88  388 608  HOH   HOH B . 
L 6 HOH   89  389 328  HOH   HOH B . 
L 6 HOH   90  390 200  HOH   HOH B . 
L 6 HOH   91  391 191  HOH   HOH B . 
L 6 HOH   92  392 240  HOH   HOH B . 
L 6 HOH   93  393 282  HOH   HOH B . 
L 6 HOH   94  394 82   HOH   HOH B . 
L 6 HOH   95  395 168  HOH   HOH B . 
L 6 HOH   96  396 536  HOH   HOH B . 
L 6 HOH   97  397 333  HOH   HOH B . 
L 6 HOH   98  398 619  HOH   HOH B . 
L 6 HOH   99  399 20   HOH   HOH B . 
L 6 HOH   100 400 382  HOH   HOH B . 
L 6 HOH   101 401 498  HOH   HOH B . 
L 6 HOH   102 402 259  HOH   HOH B . 
L 6 HOH   103 403 559  HOH   HOH B . 
L 6 HOH   104 404 389  HOH   HOH B . 
L 6 HOH   105 405 440  HOH   HOH B . 
L 6 HOH   106 406 561  HOH   HOH B . 
L 6 HOH   107 407 405  HOH   HOH B . 
L 6 HOH   108 408 655  HOH   HOH B . 
L 6 HOH   109 409 494  HOH   HOH B . 
L 6 HOH   110 410 612  HOH   HOH B . 
L 6 HOH   111 411 613  HOH   HOH B . 
L 6 HOH   112 412 610  HOH   HOH B . 
L 6 HOH   113 413 308  HOH   HOH B . 
L 6 HOH   114 414 381  HOH   HOH B . 
L 6 HOH   115 415 476  HOH   HOH B . 
L 6 HOH   116 416 660  HOH   HOH B . 
L 6 HOH   117 417 595  HOH   HOH B . 
L 6 HOH   118 418 532  HOH   HOH B . 
L 6 HOH   119 419 609  HOH   HOH B . 
L 6 HOH   120 420 289  HOH   HOH B . 
L 6 HOH   121 421 658  HOH   HOH B . 
L 6 HOH   122 422 507  HOH   HOH B . 
L 6 HOH   123 423 400  HOH   HOH B . 
L 6 HOH   124 424 549  HOH   HOH B . 
L 6 HOH   125 425 339  HOH   HOH B . 
L 6 HOH   126 426 134  HOH   HOH B . 
L 6 HOH   127 427 229  HOH   HOH B . 
L 6 HOH   128 428 591  HOH   HOH B . 
L 6 HOH   129 429 590  HOH   HOH B . 
L 6 HOH   130 430 443  HOH   HOH B . 
L 6 HOH   131 431 471  HOH   HOH B . 
L 6 HOH   132 432 518  HOH   HOH B . 
L 6 HOH   133 433 349  HOH   HOH B . 
L 6 HOH   134 434 461  HOH   HOH B . 
L 6 HOH   135 435 351  HOH   HOH B . 
L 6 HOH   136 436 544  HOH   HOH B . 
L 6 HOH   137 437 255  HOH   HOH B . 
L 6 HOH   138 438 580  HOH   HOH B . 
L 6 HOH   139 439 520  HOH   HOH B . 
M 6 HOH   1   301 502  HOH   HOH C . 
M 6 HOH   2   302 318  HOH   HOH C . 
M 6 HOH   3   303 459  HOH   HOH C . 
M 6 HOH   4   304 447  HOH   HOH C . 
M 6 HOH   5   305 149  HOH   HOH C . 
M 6 HOH   6   306 198  HOH   HOH C . 
M 6 HOH   7   307 194  HOH   HOH C . 
M 6 HOH   8   308 467  HOH   HOH C . 
M 6 HOH   9   309 280  HOH   HOH C . 
M 6 HOH   10  310 378  HOH   HOH C . 
M 6 HOH   11  311 353  HOH   HOH C . 
M 6 HOH   12  312 258  HOH   HOH C . 
M 6 HOH   13  313 639  HOH   HOH C . 
M 6 HOH   14  314 182  HOH   HOH C . 
M 6 HOH   15  315 272  HOH   HOH C . 
M 6 HOH   16  316 309  HOH   HOH C . 
M 6 HOH   17  317 316  HOH   HOH C . 
M 6 HOH   18  318 430  HOH   HOH C . 
M 6 HOH   19  319 42   HOH   HOH C . 
M 6 HOH   20  320 516  HOH   HOH C . 
M 6 HOH   21  321 41   HOH   HOH C . 
M 6 HOH   22  322 301  HOH   HOH C . 
M 6 HOH   23  323 12   HOH   HOH C . 
M 6 HOH   24  324 460  HOH   HOH C . 
M 6 HOH   25  325 369  HOH   HOH C . 
M 6 HOH   26  326 662  HOH   HOH C . 
M 6 HOH   27  327 218  HOH   HOH C . 
M 6 HOH   28  328 248  HOH   HOH C . 
M 6 HOH   29  329 271  HOH   HOH C . 
M 6 HOH   30  330 157  HOH   HOH C . 
M 6 HOH   31  331 224  HOH   HOH C . 
M 6 HOH   32  332 75   HOH   HOH C . 
M 6 HOH   33  333 472  HOH   HOH C . 
M 6 HOH   34  334 47   HOH   HOH C . 
M 6 HOH   35  335 284  HOH   HOH C . 
M 6 HOH   36  336 231  HOH   HOH C . 
M 6 HOH   37  337 583  HOH   HOH C . 
M 6 HOH   38  338 375  HOH   HOH C . 
M 6 HOH   39  339 242  HOH   HOH C . 
M 6 HOH   40  340 178  HOH   HOH C . 
M 6 HOH   41  341 172  HOH   HOH C . 
M 6 HOH   42  342 352  HOH   HOH C . 
M 6 HOH   43  343 156  HOH   HOH C . 
M 6 HOH   44  344 164  HOH   HOH C . 
M 6 HOH   45  345 177  HOH   HOH C . 
M 6 HOH   46  346 154  HOH   HOH C . 
M 6 HOH   47  347 55   HOH   HOH C . 
M 6 HOH   48  348 245  HOH   HOH C . 
M 6 HOH   49  349 470  HOH   HOH C . 
M 6 HOH   50  350 283  HOH   HOH C . 
M 6 HOH   51  351 273  HOH   HOH C . 
M 6 HOH   52  352 268  HOH   HOH C . 
M 6 HOH   53  353 190  HOH   HOH C . 
M 6 HOH   54  354 34   HOH   HOH C . 
M 6 HOH   55  355 512  HOH   HOH C . 
M 6 HOH   56  356 666  HOH   HOH C . 
M 6 HOH   57  357 266  HOH   HOH C . 
M 6 HOH   58  358 49   HOH   HOH C . 
M 6 HOH   59  359 155  HOH   HOH C . 
M 6 HOH   60  360 216  HOH   HOH C . 
M 6 HOH   61  361 584  HOH   HOH C . 
M 6 HOH   62  362 88   HOH   HOH C . 
M 6 HOH   63  363 355  HOH   HOH C . 
M 6 HOH   64  364 230  HOH   HOH C . 
M 6 HOH   65  365 490  HOH   HOH C . 
M 6 HOH   66  366 51   HOH   HOH C . 
M 6 HOH   67  367 161  HOH   HOH C . 
M 6 HOH   68  368 171  HOH   HOH C . 
M 6 HOH   69  369 209  HOH   HOH C . 
M 6 HOH   70  370 278  HOH   HOH C . 
M 6 HOH   71  371 326  HOH   HOH C . 
M 6 HOH   72  372 330  HOH   HOH C . 
M 6 HOH   73  373 67   HOH   HOH C . 
M 6 HOH   74  374 335  HOH   HOH C . 
M 6 HOH   75  375 410  HOH   HOH C . 
M 6 HOH   76  376 192  HOH   HOH C . 
M 6 HOH   77  377 374  HOH   HOH C . 
M 6 HOH   78  378 417  HOH   HOH C . 
M 6 HOH   79  379 528  HOH   HOH C . 
M 6 HOH   80  380 226  HOH   HOH C . 
M 6 HOH   81  381 551  HOH   HOH C . 
M 6 HOH   82  382 150  HOH   HOH C . 
M 6 HOH   83  383 482  HOH   HOH C . 
M 6 HOH   84  384 22   HOH   HOH C . 
M 6 HOH   85  385 478  HOH   HOH C . 
M 6 HOH   86  386 661  HOH   HOH C . 
M 6 HOH   87  387 222  HOH   HOH C . 
M 6 HOH   88  388 314  HOH   HOH C . 
M 6 HOH   89  389 27   HOH   HOH C . 
M 6 HOH   90  390 628  HOH   HOH C . 
M 6 HOH   91  391 664  HOH   HOH C . 
M 6 HOH   92  392 159  HOH   HOH C . 
M 6 HOH   93  393 119  HOH   HOH C . 
M 6 HOH   94  394 611  HOH   HOH C . 
M 6 HOH   95  395 197  HOH   HOH C . 
M 6 HOH   96  396 439  HOH   HOH C . 
M 6 HOH   97  397 323  HOH   HOH C . 
M 6 HOH   98  398 533  HOH   HOH C . 
M 6 HOH   99  399 358  HOH   HOH C . 
M 6 HOH   100 400 147  HOH   HOH C . 
M 6 HOH   101 401 479  HOH   HOH C . 
M 6 HOH   102 402 320  HOH   HOH C . 
M 6 HOH   103 403 542  HOH   HOH C . 
M 6 HOH   104 404 602  HOH   HOH C . 
M 6 HOH   105 405 484  HOH   HOH C . 
M 6 HOH   106 406 597  HOH   HOH C . 
M 6 HOH   107 407 362  HOH   HOH C . 
M 6 HOH   108 408 531  HOH   HOH C . 
M 6 HOH   109 409 423  HOH   HOH C . 
M 6 HOH   110 410 568  HOH   HOH C . 
M 6 HOH   111 411 376  HOH   HOH C . 
M 6 HOH   112 412 390  HOH   HOH C . 
M 6 HOH   113 413 239  HOH   HOH C . 
M 6 HOH   114 414 265  HOH   HOH C . 
M 6 HOH   115 415 665  HOH   HOH C . 
M 6 HOH   116 416 117  HOH   HOH C . 
M 6 HOH   117 417 451  HOH   HOH C . 
M 6 HOH   118 418 449  HOH   HOH C . 
M 6 HOH   119 419 558  HOH   HOH C . 
M 6 HOH   120 420 578  HOH   HOH C . 
M 6 HOH   121 421 492  HOH   HOH C . 
M 6 HOH   122 422 414  HOH   HOH C . 
M 6 HOH   123 423 632  HOH   HOH C . 
M 6 HOH   124 424 454  HOH   HOH C . 
M 6 HOH   125 425 621  HOH   HOH C . 
M 6 HOH   126 426 297  HOH   HOH C . 
M 6 HOH   127 427 408  HOH   HOH C . 
M 6 HOH   128 428 491  HOH   HOH C . 
M 6 HOH   129 429 300  HOH   HOH C . 
M 6 HOH   130 430 599  HOH   HOH C . 
M 6 HOH   131 431 514  HOH   HOH C . 
M 6 HOH   132 432 517  HOH   HOH C . 
M 6 HOH   133 433 640  HOH   HOH C . 
M 6 HOH   134 434 456  HOH   HOH C . 
M 6 HOH   135 435 386  HOH   HOH C . 
M 6 HOH   136 436 493  HOH   HOH C . 
M 6 HOH   137 437 350  HOH   HOH C . 
M 6 HOH   138 438 635  HOH   HOH C . 
N 6 HOH   1   301 211  HOH   HOH D . 
N 6 HOH   2   302 36   HOH   HOH D . 
N 6 HOH   3   303 276  HOH   HOH D . 
N 6 HOH   4   304 357  HOH   HOH D . 
N 6 HOH   5   305 238  HOH   HOH D . 
N 6 HOH   6   306 235  HOH   HOH D . 
N 6 HOH   7   307 40   HOH   HOH D . 
N 6 HOH   8   308 604  HOH   HOH D . 
N 6 HOH   9   309 126  HOH   HOH D . 
N 6 HOH   10  310 17   HOH   HOH D . 
N 6 HOH   11  311 629  HOH   HOH D . 
N 6 HOH   12  312 14   HOH   HOH D . 
N 6 HOH   13  313 354  HOH   HOH D . 
N 6 HOH   14  314 60   HOH   HOH D . 
N 6 HOH   15  315 132  HOH   HOH D . 
N 6 HOH   16  316 466  HOH   HOH D . 
N 6 HOH   17  317 596  HOH   HOH D . 
N 6 HOH   18  318 264  HOH   HOH D . 
N 6 HOH   19  319 7    HOH   HOH D . 
N 6 HOH   20  320 99   HOH   HOH D . 
N 6 HOH   21  321 626  HOH   HOH D . 
N 6 HOH   22  322 64   HOH   HOH D . 
N 6 HOH   23  323 319  HOH   HOH D . 
N 6 HOH   24  324 435  HOH   HOH D . 
N 6 HOH   25  325 234  HOH   HOH D . 
N 6 HOH   26  326 110  HOH   HOH D . 
N 6 HOH   27  327 633  HOH   HOH D . 
N 6 HOH   28  328 176  HOH   HOH D . 
N 6 HOH   29  329 367  HOH   HOH D . 
N 6 HOH   30  330 179  HOH   HOH D . 
N 6 HOH   31  331 105  HOH   HOH D . 
N 6 HOH   32  332 256  HOH   HOH D . 
N 6 HOH   33  333 77   HOH   HOH D . 
N 6 HOH   34  334 29   HOH   HOH D . 
N 6 HOH   35  335 334  HOH   HOH D . 
N 6 HOH   36  336 214  HOH   HOH D . 
N 6 HOH   37  337 13   HOH   HOH D . 
N 6 HOH   38  338 579  HOH   HOH D . 
N 6 HOH   39  339 91   HOH   HOH D . 
N 6 HOH   40  340 8    HOH   HOH D . 
N 6 HOH   41  341 220  HOH   HOH D . 
N 6 HOH   42  342 33   HOH   HOH D . 
N 6 HOH   43  343 588  HOH   HOH D . 
N 6 HOH   44  344 120  HOH   HOH D . 
N 6 HOH   45  345 202  HOH   HOH D . 
N 6 HOH   46  346 39   HOH   HOH D . 
N 6 HOH   47  347 143  HOH   HOH D . 
N 6 HOH   48  348 58   HOH   HOH D . 
N 6 HOH   49  349 106  HOH   HOH D . 
N 6 HOH   50  350 223  HOH   HOH D . 
N 6 HOH   51  351 35   HOH   HOH D . 
N 6 HOH   52  352 9    HOH   HOH D . 
N 6 HOH   53  353 90   HOH   HOH D . 
N 6 HOH   54  354 80   HOH   HOH D . 
N 6 HOH   55  355 146  HOH   HOH D . 
N 6 HOH   56  356 363  HOH   HOH D . 
N 6 HOH   57  357 26   HOH   HOH D . 
N 6 HOH   58  358 102  HOH   HOH D . 
N 6 HOH   59  359 260  HOH   HOH D . 
N 6 HOH   60  360 207  HOH   HOH D . 
N 6 HOH   61  361 133  HOH   HOH D . 
N 6 HOH   62  362 185  HOH   HOH D . 
N 6 HOH   63  363 70   HOH   HOH D . 
N 6 HOH   64  364 175  HOH   HOH D . 
N 6 HOH   65  365 115  HOH   HOH D . 
N 6 HOH   66  366 162  HOH   HOH D . 
N 6 HOH   67  367 180  HOH   HOH D . 
N 6 HOH   68  368 28   HOH   HOH D . 
N 6 HOH   69  369 212  HOH   HOH D . 
N 6 HOH   70  370 136  HOH   HOH D . 
N 6 HOH   71  371 152  HOH   HOH D . 
N 6 HOH   72  372 669  HOH   HOH D . 
N 6 HOH   73  373 31   HOH   HOH D . 
N 6 HOH   74  374 184  HOH   HOH D . 
N 6 HOH   75  375 567  HOH   HOH D . 
N 6 HOH   76  376 66   HOH   HOH D . 
N 6 HOH   77  377 303  HOH   HOH D . 
N 6 HOH   78  378 299  HOH   HOH D . 
N 6 HOH   79  379 125  HOH   HOH D . 
N 6 HOH   80  380 78   HOH   HOH D . 
N 6 HOH   81  381 84   HOH   HOH D . 
N 6 HOH   82  382 674  HOH   HOH D . 
N 6 HOH   83  383 327  HOH   HOH D . 
N 6 HOH   84  384 538  HOH   HOH D . 
N 6 HOH   85  385 44   HOH   HOH D . 
N 6 HOH   86  386 148  HOH   HOH D . 
N 6 HOH   87  387 57   HOH   HOH D . 
N 6 HOH   88  388 422  HOH   HOH D . 
N 6 HOH   89  389 227  HOH   HOH D . 
N 6 HOH   90  390 396  HOH   HOH D . 
N 6 HOH   91  391 275  HOH   HOH D . 
N 6 HOH   92  392 170  HOH   HOH D . 
N 6 HOH   93  393 169  HOH   HOH D . 
N 6 HOH   94  394 269  HOH   HOH D . 
N 6 HOH   95  395 196  HOH   HOH D . 
N 6 HOH   96  396 530  HOH   HOH D . 
N 6 HOH   97  397 56   HOH   HOH D . 
N 6 HOH   98  398 253  HOH   HOH D . 
N 6 HOH   99  399 19   HOH   HOH D . 
N 6 HOH   100 400 188  HOH   HOH D . 
N 6 HOH   101 401 79   HOH   HOH D . 
N 6 HOH   102 402 294  HOH   HOH D . 
N 6 HOH   103 403 73   HOH   HOH D . 
N 6 HOH   104 404 232  HOH   HOH D . 
N 6 HOH   105 405 123  HOH   HOH D . 
N 6 HOH   106 406 455  HOH   HOH D . 
N 6 HOH   107 407 108  HOH   HOH D . 
N 6 HOH   108 408 432  HOH   HOH D . 
N 6 HOH   109 409 341  HOH   HOH D . 
N 6 HOH   110 410 165  HOH   HOH D . 
N 6 HOH   111 411 445  HOH   HOH D . 
N 6 HOH   112 412 181  HOH   HOH D . 
N 6 HOH   113 413 486  HOH   HOH D . 
N 6 HOH   114 414 574  HOH   HOH D . 
N 6 HOH   115 415 399  HOH   HOH D . 
N 6 HOH   116 416 543  HOH   HOH D . 
N 6 HOH   117 417 342  HOH   HOH D . 
N 6 HOH   118 418 101  HOH   HOH D . 
N 6 HOH   119 419 317  HOH   HOH D . 
N 6 HOH   120 420 163  HOH   HOH D . 
N 6 HOH   121 421 213  HOH   HOH D . 
N 6 HOH   122 422 63   HOH   HOH D . 
N 6 HOH   123 423 86   HOH   HOH D . 
N 6 HOH   124 424 313  HOH   HOH D . 
N 6 HOH   125 425 206  HOH   HOH D . 
N 6 HOH   126 426 571  HOH   HOH D . 
N 6 HOH   127 427 458  HOH   HOH D . 
N 6 HOH   128 428 448  HOH   HOH D . 
N 6 HOH   129 429 236  HOH   HOH D . 
N 6 HOH   130 430 670  HOH   HOH D . 
N 6 HOH   131 431 513  HOH   HOH D . 
N 6 HOH   132 432 424  HOH   HOH D . 
N 6 HOH   133 433 481  HOH   HOH D . 
N 6 HOH   134 434 385  HOH   HOH D . 
N 6 HOH   135 435 74   HOH   HOH D . 
N 6 HOH   136 436 638  HOH   HOH D . 
N 6 HOH   137 437 307  HOH   HOH D . 
N 6 HOH   138 438 233  HOH   HOH D . 
N 6 HOH   139 439 560  HOH   HOH D . 
N 6 HOH   140 440 336  HOH   HOH D . 
N 6 HOH   141 441 671  HOH   HOH D . 
N 6 HOH   142 442 310  HOH   HOH D . 
N 6 HOH   143 443 505  HOH   HOH D . 
N 6 HOH   144 444 409  HOH   HOH D . 
N 6 HOH   145 445 83   HOH   HOH D . 
N 6 HOH   146 446 622  HOH   HOH D . 
N 6 HOH   147 447 69   HOH   HOH D . 
N 6 HOH   148 448 270  HOH   HOH D . 
N 6 HOH   149 449 306  HOH   HOH D . 
N 6 HOH   150 450 61   HOH   HOH D . 
N 6 HOH   151 451 365  HOH   HOH D . 
N 6 HOH   152 452 267  HOH   HOH D . 
N 6 HOH   153 453 572  HOH   HOH D . 
N 6 HOH   154 454 128  HOH   HOH D . 
N 6 HOH   155 455 519  HOH   HOH D . 
N 6 HOH   156 456 406  HOH   HOH D . 
N 6 HOH   157 457 371  HOH   HOH D . 
N 6 HOH   158 458 582  HOH   HOH D . 
N 6 HOH   159 459 208  HOH   HOH D . 
N 6 HOH   160 460 296  HOH   HOH D . 
N 6 HOH   161 461 548  HOH   HOH D . 
N 6 HOH   162 462 288  HOH   HOH D . 
N 6 HOH   163 463 474  HOH   HOH D . 
N 6 HOH   164 464 504  HOH   HOH D . 
N 6 HOH   165 465 600  HOH   HOH D . 
N 6 HOH   166 466 292  HOH   HOH D . 
N 6 HOH   167 467 433  HOH   HOH D . 
N 6 HOH   168 468 522  HOH   HOH D . 
N 6 HOH   169 469 247  HOH   HOH D . 
N 6 HOH   170 470 277  HOH   HOH D . 
N 6 HOH   171 471 594  HOH   HOH D . 
N 6 HOH   172 472 637  HOH   HOH D . 
N 6 HOH   173 473 586  HOH   HOH D . 
N 6 HOH   174 474 421  HOH   HOH D . 
N 6 HOH   175 475 563  HOH   HOH D . 
N 6 HOH   176 476 540  HOH   HOH D . 
N 6 HOH   177 477 373  HOH   HOH D . 
N 6 HOH   178 478 497  HOH   HOH D . 
N 6 HOH   179 479 325  HOH   HOH D . 
N 6 HOH   180 480 503  HOH   HOH D . 
N 6 HOH   181 481 199  HOH   HOH D . 
N 6 HOH   182 482 285  HOH   HOH D . 
N 6 HOH   183 483 420  HOH   HOH D . 
N 6 HOH   184 484 529  HOH   HOH D . 
N 6 HOH   185 485 627  HOH   HOH D . 
N 6 HOH   186 486 427  HOH   HOH D . 
N 6 HOH   187 487 441  HOH   HOH D . 
N 6 HOH   188 488 293  HOH   HOH D . 
N 6 HOH   189 489 525  HOH   HOH D . 
N 6 HOH   190 490 676  HOH   HOH D . 
N 6 HOH   191 491 534  HOH   HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BG2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.360 
_cell.length_a_esd                 ? 
_cell.length_b                     85.570 
_cell.length_b_esd                 ? 
_cell.length_c                     127.330 
_cell.length_c_esd                 ? 
_cell.volume                       723033.881 
_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                         9BG2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_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                   9BG2 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.93 
_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    '28% PEG 3350, 0.1M Bis Tris, pH 5.5, 150 mM NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-19 
_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   .95299 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        .95299 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          26.88 
_reflns.entry_id                                       9BG2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.64 
_reflns.d_resolution_low                               58.85 
_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                                     88855 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.29 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.23 
_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                                .03378 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              .1079 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.64 
_reflns_shell.d_res_low                                     1.699 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           .95 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8775 
_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                               11.8 
_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                               .8608 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .361 
_reflns_shell.pdbx_CC_star                                  .728 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.35 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.892 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.33 
_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                                 9BG2 
_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                            1.64 
_refine.ls_d_res_low                             58.85 
_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                     88804 
_refine.ls_number_reflns_R_free                  4392 
_refine.ls_number_reflns_R_work                  84412 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.30 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2011 
_refine.ls_R_factor_R_free                       0.2283 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1996 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.7943 
_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                            0.2460 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.64 
_refine_hist.d_res_low                        58.85 
_refine_hist.number_atoms_solvent             632 
_refine_hist.number_atoms_total               5971 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5171 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         168 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0106  ? 5514 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1421  ? 7462 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0730  ? 797  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0111  ? 963  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.2550 ? 2082 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.64 1.66  . . 149 2738 98.97  . . . . 0.3322 . . . . . . . . . . . 0.3696 
'X-RAY DIFFRACTION' 1.66 1.68  . . 151 2804 99.60  . . . . 0.3410 . . . . . . . . . . . 0.3731 
'X-RAY DIFFRACTION' 1.68 1.70  . . 126 2806 99.49  . . . . 0.3326 . . . . . . . . . . . 0.3601 
'X-RAY DIFFRACTION' 1.70 1.72  . . 129 2807 99.26  . . . . 0.3376 . . . . . . . . . . . 0.4245 
'X-RAY DIFFRACTION' 1.72 1.74  . . 144 2790 99.59  . . . . 0.3178 . . . . . . . . . . . 0.3708 
'X-RAY DIFFRACTION' 1.74 1.77  . . 144 2745 99.38  . . . . 0.2886 . . . . . . . . . . . 0.3613 
'X-RAY DIFFRACTION' 1.77 1.79  . . 156 2824 99.77  . . . . 0.2673 . . . . . . . . . . . 0.2836 
'X-RAY DIFFRACTION' 1.79 1.82  . . 119 2811 99.69  . . . . 0.2503 . . . . . . . . . . . 0.2978 
'X-RAY DIFFRACTION' 1.82 1.85  . . 141 2801 99.56  . . . . 0.2510 . . . . . . . . . . . 0.2870 
'X-RAY DIFFRACTION' 1.85 1.88  . . 148 2771 99.02  . . . . 0.2648 . . . . . . . . . . . 0.3019 
'X-RAY DIFFRACTION' 1.88 1.91  . . 140 2685 96.35  . . . . 0.3181 . . . . . . . . . . . 0.3473 
'X-RAY DIFFRACTION' 1.91 1.94  . . 122 2718 94.98  . . . . 0.3462 . . . . . . . . . . . 0.3692 
'X-RAY DIFFRACTION' 1.94 1.98  . . 157 2750 99.73  . . . . 0.2440 . . . . . . . . . . . 0.3051 
'X-RAY DIFFRACTION' 1.98 2.02  . . 155 2828 100.00 . . . . 0.2343 . . . . . . . . . . . 0.2427 
'X-RAY DIFFRACTION' 2.02 2.07  . . 144 2808 99.29  . . . . 0.2411 . . . . . . . . . . . 0.3039 
'X-RAY DIFFRACTION' 2.07 2.11  . . 138 2787 98.98  . . . . 0.2392 . . . . . . . . . . . 0.2722 
'X-RAY DIFFRACTION' 2.11 2.17  . . 147 2817 99.97  . . . . 0.2082 . . . . . . . . . . . 0.2777 
'X-RAY DIFFRACTION' 2.17 2.23  . . 156 2818 99.90  . . . . 0.2069 . . . . . . . . . . . 0.2364 
'X-RAY DIFFRACTION' 2.23 2.29  . . 139 2770 97.78  . . . . 0.2494 . . . . . . . . . . . 0.2892 
'X-RAY DIFFRACTION' 2.29 2.37  . . 151 2817 100.00 . . . . 0.2041 . . . . . . . . . . . 0.2637 
'X-RAY DIFFRACTION' 2.37 2.45  . . 139 2849 100.00 . . . . 0.2043 . . . . . . . . . . . 0.2653 
'X-RAY DIFFRACTION' 2.45 2.55  . . 158 2808 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2302 
'X-RAY DIFFRACTION' 2.55 2.66  . . 139 2853 99.90  . . . . 0.2145 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 2.66 2.80  . . 148 2813 99.76  . . . . 0.2068 . . . . . . . . . . . 0.2760 
'X-RAY DIFFRACTION' 2.80 2.98  . . 156 2863 99.97  . . . . 0.1954 . . . . . . . . . . . 0.2570 
'X-RAY DIFFRACTION' 2.98 3.21  . . 158 2843 99.77  . . . . 0.1949 . . . . . . . . . . . 0.2074 
'X-RAY DIFFRACTION' 3.21 3.53  . . 160 2867 99.90  . . . . 0.1793 . . . . . . . . . . . 0.2063 
'X-RAY DIFFRACTION' 3.53 4.04  . . 153 2884 99.74  . . . . 0.1603 . . . . . . . . . . . 0.1933 
'X-RAY DIFFRACTION' 4.04 5.09  . . 160 2934 100.00 . . . . 0.1413 . . . . . . . . . . . 0.1679 
'X-RAY DIFFRACTION' 5.10 58.85 . . 165 3003 98.57  . . . . 0.1709 . . . . . . . . . . . 0.1724 
# 
_struct.entry_id                     9BG2 
_struct.title                        'Tri-complex of Compound-10, KRAS G12V, and CypA' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BG2 
_struct_keywords.text            
'inhibitor, complex, small GTPase, cancer, tri-complex, SIGNALING PROTEIN-INHIBITOR complex, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN/INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP RASK_HUMAN P01116 P01116-2 1 
;MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLC
VFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLV
REIRKHKEK
;
1 
2 UNP PPIA_HUMAN P62937 ?        2 
;MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD
CGQLE
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BG2 A 2 ? 170 ? P01116 1 ? 169 ? 1 169 
2 1 9BG2 B 2 ? 170 ? P01116 1 ? 169 ? 1 169 
3 2 9BG2 C 2 ? 166 ? P62937 1 ? 165 ? 1 165 
4 2 9BG2 D 2 ? 166 ? P62937 1 ? 165 ? 1 165 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BG2 SER A 1  ? UNP P01116 ?   ?  'expression tag'      0  1 
1 9BG2 VAL A 13 ? UNP P01116 GLY 12 'engineered mutation' 12 2 
2 9BG2 SER B 1  ? UNP P01116 ?   ?  'expression tag'      0  3 
2 9BG2 VAL B 13 ? UNP P01116 GLY 12 'engineered mutation' 12 4 
3 9BG2 SER C 1  ? UNP P62937 ?   ?  'expression tag'      0  5 
4 9BG2 SER D 1  ? UNP P62937 ?   ?  'expression tag'      0  6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,J,K,N 
2 1 B,C,G,H,I,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 16  ? ASN A 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2  AA2 GLN A 62  ? MET A 68  ? GLN A 61  MET A 67  5 ? 7  
HELX_P HELX_P3  AA3 ARG A 69  ? GLY A 76  ? ARG A 68  GLY A 75  1 ? 8  
HELX_P HELX_P4  AA4 ASN A 87  ? ASP A 106 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P5  AA5 ASP A 127 ? GLY A 139 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6  AA6 GLY A 152 ? LYS A 168 ? GLY A 151 LYS A 167 1 ? 17 
HELX_P HELX_P7  AA7 GLY B 16  ? ASN B 27  ? GLY B 15  ASN B 26  1 ? 12 
HELX_P HELX_P8  AA8 GLN B 62  ? MET B 68  ? GLN B 61  MET B 67  5 ? 7  
HELX_P HELX_P9  AA9 ARG B 69  ? GLY B 76  ? ARG B 68  GLY B 75  1 ? 8  
HELX_P HELX_P10 AB1 ASN B 87  ? ASP B 106 ? ASN B 86  ASP B 105 1 ? 20 
HELX_P HELX_P11 AB2 ASP B 127 ? GLY B 139 ? ASP B 126 GLY B 138 1 ? 13 
HELX_P HELX_P12 AB3 GLY B 152 ? LYS B 168 ? GLY B 151 LYS B 167 1 ? 17 
HELX_P HELX_P13 AB4 VAL C 30  ? GLY C 43  ? VAL C 29  GLY C 42  1 ? 14 
HELX_P HELX_P14 AB5 THR C 120 ? ASP C 124 ? THR C 119 ASP C 123 5 ? 5  
HELX_P HELX_P15 AB6 GLY C 136 ? GLU C 144 ? GLY C 135 GLU C 143 1 ? 9  
HELX_P HELX_P16 AB7 ARG C 145 ? GLY C 147 ? ARG C 144 GLY C 146 5 ? 3  
HELX_P HELX_P17 AB8 VAL D 30  ? GLY D 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P18 AB9 THR D 120 ? ASP D 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P19 AC1 GLY D 136 ? GLU D 144 ? GLY D 135 GLU D 143 1 ? 9  
HELX_P HELX_P20 AC2 ARG D 145 ? GLY D 147 ? ARG D 144 GLY D 146 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 18 OG  ? ? ? 1_555 F MG  . MG ? ? A SER 17  A MG  202 1_555 ? ? ? ? ? ? ? 2.169 ? ? 
metalc2  metalc ? ? A THR 36 OG1 ? ? ? 1_555 F MG  . MG ? ? A THR 35  A MG  202 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc3  metalc ? ? E GNP .  O1G ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 1.948 ? ? 
metalc4  metalc ? ? E GNP .  O2B ? ? ? 1_555 F MG  . MG ? ? A GNP 201 A MG  202 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc5  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 319 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc6  metalc ? ? F MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? A MG  202 A HOH 346 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc7  metalc ? ? B SER 18 OG  ? ? ? 1_555 H MG  . MG ? ? B SER 17  B MG  202 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc8  metalc ? ? B THR 36 OG1 ? ? ? 1_555 H MG  . MG ? ? B THR 35  B MG  202 1_555 ? ? ? ? ? ? ? 2.171 ? ? 
metalc9  metalc ? ? G GNP .  O1G ? ? ? 1_555 H MG  . MG ? ? B GNP 201 B MG  202 1_555 ? ? ? ? ? ? ? 1.983 ? ? 
metalc10 metalc ? ? G GNP .  O2B ? ? ? 1_555 H MG  . MG ? ? B GNP 201 B MG  202 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc11 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 315 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc12 metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  202 B HOH 322 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 OG1 ? A THR 36 ? A THR 35  ? 1_555 80.8  ? 
2  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 172.2 ? 
3  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 91.4  ? 
4  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O2B ? E GNP .  ? A GNP 201 ? 1_555 91.3  ? 
5  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O2B ? E GNP .  ? A GNP 201 ? 1_555 171.3 ? 
6  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O2B ? E GNP .  ? A GNP 201 ? 1_555 96.6  ? 
7  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 319 ? 1_555 84.2  ? 
8  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 319 ? 1_555 84.7  ? 
9  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 319 ? 1_555 95.1  ? 
10 O2B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 319 ? 1_555 98.1  ? 
11 OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 86.7  ? 
12 OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 91.1  ? 
13 O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 93.6  ? 
14 O2B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 84.9  ? 
15 O   ? K HOH .  ? A HOH 319 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? K HOH .  ? A HOH 346 ? 1_555 170.4 ? 
16 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 OG1 ? B THR 36 ? B THR 35  ? 1_555 81.7  ? 
17 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1G ? G GNP .  ? B GNP 201 ? 1_555 170.4 ? 
18 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O1G ? G GNP .  ? B GNP 201 ? 1_555 88.8  ? 
19 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O2B ? G GNP .  ? B GNP 201 ? 1_555 94.9  ? 
20 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O2B ? G GNP .  ? B GNP 201 ? 1_555 175.1 ? 
21 O1G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O2B ? G GNP .  ? B GNP 201 ? 1_555 94.7  ? 
22 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 315 ? 1_555 87.5  ? 
23 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 315 ? 1_555 85.3  ? 
24 O1G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 315 ? 1_555 93.4  ? 
25 O2B ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 315 ? 1_555 91.0  ? 
26 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 322 ? 1_555 89.7  ? 
27 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 322 ? 1_555 87.5  ? 
28 O1G ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 322 ? 1_555 88.2  ? 
29 O2B ? G GNP .  ? B GNP 201 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 322 ? 1_555 96.1  ? 
30 O   ? L HOH .  ? B HOH 315 ? 1_555 MG ? H MG . ? B MG 202 ? 1_555 O   ? L HOH .  ? B HOH 322 ? 1_555 172.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 8 ? 
AA4 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 38  ? ILE A 47  ? GLU A 37  ILE A 46  
AA1 2 GLU A 50  ? THR A 59  ? GLU A 49  THR A 58  
AA1 3 THR A 3   ? GLY A 11  ? THR A 2   GLY A 10  
AA1 4 GLY A 78  ? ALA A 84  ? GLY A 77  ALA A 83  
AA1 5 MET A 112 ? ASN A 117 ? MET A 111 ASN A 116 
AA1 6 PHE A 142 ? GLU A 144 ? PHE A 141 GLU A 143 
AA2 1 GLU B 38  ? ILE B 47  ? GLU B 37  ILE B 46  
AA2 2 GLU B 50  ? THR B 59  ? GLU B 49  THR B 58  
AA2 3 THR B 3   ? VAL B 10  ? THR B 2   VAL B 9   
AA2 4 GLY B 78  ? ALA B 84  ? GLY B 77  ALA B 83  
AA2 5 MET B 112 ? ASN B 117 ? MET B 111 ASN B 116 
AA2 6 PHE B 142 ? GLU B 144 ? PHE B 141 GLU B 143 
AA3 1 PHE C 54  ? ILE C 58  ? PHE C 53  ILE C 57  
AA3 2 MET C 62  ? GLY C 65  ? MET C 61  GLY C 64  
AA3 3 PHE C 113 ? CYS C 116 ? PHE C 112 CYS C 115 
AA3 4 ILE C 98  ? MET C 101 ? ILE C 97  MET C 100 
AA3 5 VAL C 129 ? GLU C 135 ? VAL C 128 GLU C 134 
AA3 6 GLU C 16  ? LEU C 25  ? GLU C 15  LEU C 24  
AA3 7 THR C 6   ? VAL C 13  ? THR C 5   VAL C 12  
AA3 8 ILE C 157 ? GLN C 164 ? ILE C 156 GLN C 163 
AA4 1 ARG D 56  ? ILE D 58  ? ARG D 55  ILE D 57  
AA4 2 MET D 62  ? GLY D 65  ? MET D 61  GLY D 64  
AA4 3 PHE D 113 ? CYS D 116 ? PHE D 112 CYS D 115 
AA4 4 ILE D 98  ? MET D 101 ? ILE D 97  MET D 100 
AA4 5 VAL D 129 ? GLU D 135 ? VAL D 128 GLU D 134 
AA4 6 GLU D 16  ? LEU D 25  ? GLU D 15  LEU D 24  
AA4 7 THR D 6   ? VAL D 13  ? THR D 5   VAL D 12  
AA4 8 ILE D 157 ? LEU D 165 ? ILE D 156 LEU D 164 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 43  ? N LYS A 42  O LEU A 54  ? O LEU A 53  
AA1 2 3 O LEU A 57  ? O LEU A 56  N VAL A 9   ? N VAL A 8   
AA1 3 4 N VAL A 10  ? N VAL A 9   O LEU A 80  ? O LEU A 79  
AA1 4 5 N CYS A 81  ? N CYS A 80  O VAL A 113 ? O VAL A 112 
AA1 5 6 N LEU A 114 ? N LEU A 113 O ILE A 143 ? O ILE A 142 
AA2 1 2 N LYS B 43  ? N LYS B 42  O LEU B 54  ? O LEU B 53  
AA2 2 3 O LEU B 57  ? O LEU B 56  N VAL B 9   ? N VAL B 8   
AA2 3 4 N VAL B 10  ? N VAL B 9   O LEU B 80  ? O LEU B 79  
AA2 4 5 N CYS B 81  ? N CYS B 80  O VAL B 115 ? O VAL B 114 
AA2 5 6 N LEU B 114 ? N LEU B 113 O ILE B 143 ? O ILE B 142 
AA3 1 2 N ARG C 56  ? N ARG C 55  O GLN C 64  ? O GLN C 63  
AA3 2 3 N CYS C 63  ? N CYS C 62  O ILE C 115 ? O ILE C 114 
AA3 3 4 O CYS C 116 ? O CYS C 115 N ILE C 98  ? N ILE C 97  
AA3 4 5 N LEU C 99  ? N LEU C 98  O PHE C 130 ? O PHE C 129 
AA3 5 6 O LYS C 134 ? O LYS C 133 N SER C 22  ? N SER C 21  
AA3 6 7 O GLU C 16  ? O GLU C 15  N VAL C 13  ? N VAL C 12  
AA3 7 8 N ASP C 10  ? N ASP C 9   O ASP C 161 ? O ASP C 160 
AA4 1 2 N ARG D 56  ? N ARG D 55  O GLN D 64  ? O GLN D 63  
AA4 2 3 N CYS D 63  ? N CYS D 62  O ILE D 115 ? O ILE D 114 
AA4 3 4 O CYS D 116 ? O CYS D 115 N ILE D 98  ? N ILE D 97  
AA4 4 5 N LEU D 99  ? N LEU D 98  O PHE D 130 ? O PHE D 129 
AA4 5 6 O GLU D 135 ? O GLU D 134 N SER D 22  ? N SER D 21  
AA4 6 7 O PHE D 23  ? O PHE D 22  N VAL D 7   ? N VAL D 6   
AA4 7 8 N ASP D 10  ? N ASP D 9   O ASP D 161 ? O ASP D 160 
# 
_pdbx_entry_details.entry_id                   9BG2 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 37  ? ? -170.32 127.66 
2 1 LYS A 117 ? ? 70.21   33.47  
3 1 LYS A 117 ? ? 70.21   33.67  
4 1 SER A 122 ? ? -76.95  48.02  
5 1 ILE B 36  ? ? -92.25  -66.18 
6 1 PHE C 60  ? ? -139.14 -73.48 
7 1 PHE D 60  ? ? -136.44 -71.01 
8 1 PHE D 60  ? ? -136.44 -70.41 
9 1 ASN D 71  ? ? -145.70 17.41  
# 
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 ? C A1AOJ 201 ? PLANAR . 
2 1 N2 ? D A1AOJ 201 ? PLANAR . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         41.5849097239 
_pdbx_refine_tls.origin_y         0.543701253328 
_pdbx_refine_tls.origin_z         19.0996926769 
_pdbx_refine_tls.T[1][1]          0.253349261296 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.00667259924529 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0294499746898 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.270224545356 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0187803545251 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.236827708177 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.317971723505 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.481415549101 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.249114921628 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.702929763386 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.343530959042 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.16871155837 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0739674857061 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0552842561767 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0200028844962 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.135480867154 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0534226292081 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.00407927023827 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0692946186154 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0276824659538 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0199306934195 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     0 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   K 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    S 
_pdbx_refine_tls_group.end_auth_seq_id     676 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 438 ? 6.77 . 
2 1 O ? D HOH 488 ? 5.87 . 
3 1 O ? D HOH 489 ? 5.92 . 
4 1 O ? D HOH 490 ? 6.12 . 
5 1 O ? D HOH 491 ? 6.30 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 168 ? A GLU 169 
2  1 Y 1 A LYS 169 ? A LYS 170 
3  1 Y 1 B GLU 168 ? B GLU 169 
4  1 Y 1 B LYS 169 ? B LYS 170 
5  1 Y 1 C SER 0   ? C SER 1   
6  1 Y 1 C MET 1   ? C MET 2   
7  1 Y 1 C GLU 165 ? C GLU 166 
8  1 Y 1 D SER 0   ? D SER 1   
9  1 Y 1 D MET 1   ? D MET 2   
10 1 Y 1 D VAL 2   ? D VAL 3   
11 1 Y 1 D GLU 165 ? D GLU 166 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AOJ C1     C  N N 1   
A1AOJ C10    C  N N 2   
A1AOJ C11    C  N N 3   
A1AOJ C12    C  N N 4   
A1AOJ C13    C  Y N 5   
A1AOJ C14    C  Y N 6   
A1AOJ C15    C  Y N 7   
A1AOJ C16    C  Y N 8   
A1AOJ C17    C  Y N 9   
A1AOJ C18    C  Y N 10  
A1AOJ C19    C  Y N 11  
A1AOJ C2     C  N S 12  
A1AOJ C20    C  Y N 13  
A1AOJ C21    C  Y N 14  
A1AOJ C22    C  N N 15  
A1AOJ C23    C  N N 16  
A1AOJ C24    C  Y N 17  
A1AOJ C25    C  Y N 18  
A1AOJ C26    C  Y N 19  
A1AOJ C27    C  N S 20  
A1AOJ C28    C  N N 21  
A1AOJ C29    C  N N 22  
A1AOJ C3     C  N N 23  
A1AOJ C30    C  Y N 24  
A1AOJ C31    C  Y N 25  
A1AOJ C32    C  Y N 26  
A1AOJ C33    C  Y N 27  
A1AOJ C34    C  N N 28  
A1AOJ C35    C  N N 29  
A1AOJ C36    C  N N 30  
A1AOJ C37    C  N N 31  
A1AOJ C38    C  N N 32  
A1AOJ C39    C  N N 33  
A1AOJ C4     C  N N 34  
A1AOJ C5     C  N N 35  
A1AOJ C6     C  N S 36  
A1AOJ C7     C  N N 37  
A1AOJ C8     C  N S 38  
A1AOJ C9     C  N S 39  
A1AOJ N1     N  N N 40  
A1AOJ N2     N  N S 41  
A1AOJ N3     N  N N 42  
A1AOJ N4     N  Y N 43  
A1AOJ N5     N  Y N 44  
A1AOJ N6     N  Y N 45  
A1AOJ O1     O  N N 46  
A1AOJ O2     O  N N 47  
A1AOJ O3     O  N N 48  
A1AOJ O4     O  N N 49  
A1AOJ O5     O  N N 50  
A1AOJ S1     S  Y N 51  
A1AOJ H1     H  N N 52  
A1AOJ H2     H  N N 53  
A1AOJ H15    H  N N 54  
A1AOJ H14    H  N N 55  
A1AOJ H13    H  N N 56  
A1AOJ H17    H  N N 57  
A1AOJ H16    H  N N 58  
A1AOJ H19    H  N N 59  
A1AOJ H18    H  N N 60  
A1AOJ H20    H  N N 61  
A1AOJ H21    H  N N 62  
A1AOJ H3     H  N N 63  
A1AOJ H22    H  N N 64  
A1AOJ H23    H  N N 65  
A1AOJ H24    H  N N 66  
A1AOJ H25    H  N N 67  
A1AOJ H27    H  N N 68  
A1AOJ H26    H  N N 69  
A1AOJ H28    H  N N 70  
A1AOJ H29    H  N N 71  
A1AOJ H30    H  N N 72  
A1AOJ H31    H  N N 73  
A1AOJ H32    H  N N 74  
A1AOJ H34    H  N N 75  
A1AOJ H33    H  N N 76  
A1AOJ H35    H  N N 77  
A1AOJ H5     H  N N 78  
A1AOJ H6     H  N N 79  
A1AOJ H36    H  N N 80  
A1AOJ H37    H  N N 81  
A1AOJ H38    H  N N 82  
A1AOJ H40    H  N N 83  
A1AOJ H39    H  N N 84  
A1AOJ H41    H  N N 85  
A1AOJ H43    H  N N 86  
A1AOJ H42    H  N N 87  
A1AOJ H45    H  N N 88  
A1AOJ H44    H  N N 89  
A1AOJ H46    H  N N 90  
A1AOJ H48    H  N N 91  
A1AOJ H47    H  N N 92  
A1AOJ H8     H  N N 93  
A1AOJ H7     H  N N 94  
A1AOJ H9     H  N N 95  
A1AOJ H11    H  N N 96  
A1AOJ H12    H  N N 97  
A1AOJ H4     H  N N 98  
A1AOJ H10    H  N N 99  
ALA   N      N  N N 100 
ALA   CA     C  N S 101 
ALA   C      C  N N 102 
ALA   O      O  N N 103 
ALA   CB     C  N N 104 
ALA   OXT    O  N N 105 
ALA   H      H  N N 106 
ALA   H2     H  N N 107 
ALA   HA     H  N N 108 
ALA   HB1    H  N N 109 
ALA   HB2    H  N N 110 
ALA   HB3    H  N N 111 
ALA   HXT    H  N N 112 
ARG   N      N  N N 113 
ARG   CA     C  N S 114 
ARG   C      C  N N 115 
ARG   O      O  N N 116 
ARG   CB     C  N N 117 
ARG   CG     C  N N 118 
ARG   CD     C  N N 119 
ARG   NE     N  N N 120 
ARG   CZ     C  N N 121 
ARG   NH1    N  N N 122 
ARG   NH2    N  N N 123 
ARG   OXT    O  N N 124 
ARG   H      H  N N 125 
ARG   H2     H  N N 126 
ARG   HA     H  N N 127 
ARG   HB2    H  N N 128 
ARG   HB3    H  N N 129 
ARG   HG2    H  N N 130 
ARG   HG3    H  N N 131 
ARG   HD2    H  N N 132 
ARG   HD3    H  N N 133 
ARG   HE     H  N N 134 
ARG   HH11   H  N N 135 
ARG   HH12   H  N N 136 
ARG   HH21   H  N N 137 
ARG   HH22   H  N N 138 
ARG   HXT    H  N N 139 
ASN   N      N  N N 140 
ASN   CA     C  N S 141 
ASN   C      C  N N 142 
ASN   O      O  N N 143 
ASN   CB     C  N N 144 
ASN   CG     C  N N 145 
ASN   OD1    O  N N 146 
ASN   ND2    N  N N 147 
ASN   OXT    O  N N 148 
ASN   H      H  N N 149 
ASN   H2     H  N N 150 
ASN   HA     H  N N 151 
ASN   HB2    H  N N 152 
ASN   HB3    H  N N 153 
ASN   HD21   H  N N 154 
ASN   HD22   H  N N 155 
ASN   HXT    H  N N 156 
ASP   N      N  N N 157 
ASP   CA     C  N S 158 
ASP   C      C  N N 159 
ASP   O      O  N N 160 
ASP   CB     C  N N 161 
ASP   CG     C  N N 162 
ASP   OD1    O  N N 163 
ASP   OD2    O  N N 164 
ASP   OXT    O  N N 165 
ASP   H      H  N N 166 
ASP   H2     H  N N 167 
ASP   HA     H  N N 168 
ASP   HB2    H  N N 169 
ASP   HB3    H  N N 170 
ASP   HD2    H  N N 171 
ASP   HXT    H  N N 172 
CYS   N      N  N N 173 
CYS   CA     C  N R 174 
CYS   C      C  N N 175 
CYS   O      O  N N 176 
CYS   CB     C  N N 177 
CYS   SG     S  N N 178 
CYS   OXT    O  N N 179 
CYS   H      H  N N 180 
CYS   H2     H  N N 181 
CYS   HA     H  N N 182 
CYS   HB2    H  N N 183 
CYS   HB3    H  N N 184 
CYS   HG     H  N N 185 
CYS   HXT    H  N N 186 
GLN   N      N  N N 187 
GLN   CA     C  N S 188 
GLN   C      C  N N 189 
GLN   O      O  N N 190 
GLN   CB     C  N N 191 
GLN   CG     C  N N 192 
GLN   CD     C  N N 193 
GLN   OE1    O  N N 194 
GLN   NE2    N  N N 195 
GLN   OXT    O  N N 196 
GLN   H      H  N N 197 
GLN   H2     H  N N 198 
GLN   HA     H  N N 199 
GLN   HB2    H  N N 200 
GLN   HB3    H  N N 201 
GLN   HG2    H  N N 202 
GLN   HG3    H  N N 203 
GLN   HE21   H  N N 204 
GLN   HE22   H  N N 205 
GLN   HXT    H  N N 206 
GLU   N      N  N N 207 
GLU   CA     C  N S 208 
GLU   C      C  N N 209 
GLU   O      O  N N 210 
GLU   CB     C  N N 211 
GLU   CG     C  N N 212 
GLU   CD     C  N N 213 
GLU   OE1    O  N N 214 
GLU   OE2    O  N N 215 
GLU   OXT    O  N N 216 
GLU   H      H  N N 217 
GLU   H2     H  N N 218 
GLU   HA     H  N N 219 
GLU   HB2    H  N N 220 
GLU   HB3    H  N N 221 
GLU   HG2    H  N N 222 
GLU   HG3    H  N N 223 
GLU   HE2    H  N N 224 
GLU   HXT    H  N N 225 
GLY   N      N  N N 226 
GLY   CA     C  N N 227 
GLY   C      C  N N 228 
GLY   O      O  N N 229 
GLY   OXT    O  N N 230 
GLY   H      H  N N 231 
GLY   H2     H  N N 232 
GLY   HA2    H  N N 233 
GLY   HA3    H  N N 234 
GLY   HXT    H  N N 235 
GNP   PG     P  N N 236 
GNP   O1G    O  N N 237 
GNP   O2G    O  N N 238 
GNP   O3G    O  N N 239 
GNP   N3B    N  N N 240 
GNP   PB     P  N R 241 
GNP   O1B    O  N N 242 
GNP   O2B    O  N N 243 
GNP   O3A    O  N N 244 
GNP   PA     P  N S 245 
GNP   O1A    O  N N 246 
GNP   O2A    O  N N 247 
GNP   "O5'"  O  N N 248 
GNP   "C5'"  C  N N 249 
GNP   "C4'"  C  N R 250 
GNP   "O4'"  O  N N 251 
GNP   "C3'"  C  N S 252 
GNP   "O3'"  O  N N 253 
GNP   "C2'"  C  N R 254 
GNP   "O2'"  O  N N 255 
GNP   "C1'"  C  N R 256 
GNP   N9     N  Y N 257 
GNP   C8     C  Y N 258 
GNP   N7     N  Y N 259 
GNP   C5     C  Y N 260 
GNP   C6     C  Y N 261 
GNP   O6     O  N N 262 
GNP   N1     N  Y N 263 
GNP   C2     C  Y N 264 
GNP   N2     N  N N 265 
GNP   N3     N  Y N 266 
GNP   C4     C  Y N 267 
GNP   HOG2   H  N N 268 
GNP   HOG3   H  N N 269 
GNP   HNB3   H  N N 270 
GNP   HOB2   H  N N 271 
GNP   HOA2   H  N N 272 
GNP   "H5'2" H  N N 273 
GNP   "H5'1" H  N N 274 
GNP   "H4'"  H  N N 275 
GNP   "H3'"  H  N N 276 
GNP   "HO3'" H  N N 277 
GNP   "H2'"  H  N N 278 
GNP   "HO2'" H  N N 279 
GNP   "H1'"  H  N N 280 
GNP   H8     H  N N 281 
GNP   HN1    H  N N 282 
GNP   HN21   H  N N 283 
GNP   HN22   H  N N 284 
HIS   N      N  N N 285 
HIS   CA     C  N S 286 
HIS   C      C  N N 287 
HIS   O      O  N N 288 
HIS   CB     C  N N 289 
HIS   CG     C  Y N 290 
HIS   ND1    N  Y N 291 
HIS   CD2    C  Y N 292 
HIS   CE1    C  Y N 293 
HIS   NE2    N  Y N 294 
HIS   OXT    O  N N 295 
HIS   H      H  N N 296 
HIS   H2     H  N N 297 
HIS   HA     H  N N 298 
HIS   HB2    H  N N 299 
HIS   HB3    H  N N 300 
HIS   HD1    H  N N 301 
HIS   HD2    H  N N 302 
HIS   HE1    H  N N 303 
HIS   HE2    H  N N 304 
HIS   HXT    H  N N 305 
HOH   O      O  N N 306 
HOH   H1     H  N N 307 
HOH   H2     H  N N 308 
ILE   N      N  N N 309 
ILE   CA     C  N S 310 
ILE   C      C  N N 311 
ILE   O      O  N N 312 
ILE   CB     C  N S 313 
ILE   CG1    C  N N 314 
ILE   CG2    C  N N 315 
ILE   CD1    C  N N 316 
ILE   OXT    O  N N 317 
ILE   H      H  N N 318 
ILE   H2     H  N N 319 
ILE   HA     H  N N 320 
ILE   HB     H  N N 321 
ILE   HG12   H  N N 322 
ILE   HG13   H  N N 323 
ILE   HG21   H  N N 324 
ILE   HG22   H  N N 325 
ILE   HG23   H  N N 326 
ILE   HD11   H  N N 327 
ILE   HD12   H  N N 328 
ILE   HD13   H  N N 329 
ILE   HXT    H  N N 330 
LEU   N      N  N N 331 
LEU   CA     C  N S 332 
LEU   C      C  N N 333 
LEU   O      O  N N 334 
LEU   CB     C  N N 335 
LEU   CG     C  N N 336 
LEU   CD1    C  N N 337 
LEU   CD2    C  N N 338 
LEU   OXT    O  N N 339 
LEU   H      H  N N 340 
LEU   H2     H  N N 341 
LEU   HA     H  N N 342 
LEU   HB2    H  N N 343 
LEU   HB3    H  N N 344 
LEU   HG     H  N N 345 
LEU   HD11   H  N N 346 
LEU   HD12   H  N N 347 
LEU   HD13   H  N N 348 
LEU   HD21   H  N N 349 
LEU   HD22   H  N N 350 
LEU   HD23   H  N N 351 
LEU   HXT    H  N N 352 
LYS   N      N  N N 353 
LYS   CA     C  N S 354 
LYS   C      C  N N 355 
LYS   O      O  N N 356 
LYS   CB     C  N N 357 
LYS   CG     C  N N 358 
LYS   CD     C  N N 359 
LYS   CE     C  N N 360 
LYS   NZ     N  N N 361 
LYS   OXT    O  N N 362 
LYS   H      H  N N 363 
LYS   H2     H  N N 364 
LYS   HA     H  N N 365 
LYS   HB2    H  N N 366 
LYS   HB3    H  N N 367 
LYS   HG2    H  N N 368 
LYS   HG3    H  N N 369 
LYS   HD2    H  N N 370 
LYS   HD3    H  N N 371 
LYS   HE2    H  N N 372 
LYS   HE3    H  N N 373 
LYS   HZ1    H  N N 374 
LYS   HZ2    H  N N 375 
LYS   HZ3    H  N N 376 
LYS   HXT    H  N N 377 
MET   N      N  N N 378 
MET   CA     C  N S 379 
MET   C      C  N N 380 
MET   O      O  N N 381 
MET   CB     C  N N 382 
MET   CG     C  N N 383 
MET   SD     S  N N 384 
MET   CE     C  N N 385 
MET   OXT    O  N N 386 
MET   H      H  N N 387 
MET   H2     H  N N 388 
MET   HA     H  N N 389 
MET   HB2    H  N N 390 
MET   HB3    H  N N 391 
MET   HG2    H  N N 392 
MET   HG3    H  N N 393 
MET   HE1    H  N N 394 
MET   HE2    H  N N 395 
MET   HE3    H  N N 396 
MET   HXT    H  N N 397 
MG    MG     MG N N 398 
PHE   N      N  N N 399 
PHE   CA     C  N S 400 
PHE   C      C  N N 401 
PHE   O      O  N N 402 
PHE   CB     C  N N 403 
PHE   CG     C  Y N 404 
PHE   CD1    C  Y N 405 
PHE   CD2    C  Y N 406 
PHE   CE1    C  Y N 407 
PHE   CE2    C  Y N 408 
PHE   CZ     C  Y N 409 
PHE   OXT    O  N N 410 
PHE   H      H  N N 411 
PHE   H2     H  N N 412 
PHE   HA     H  N N 413 
PHE   HB2    H  N N 414 
PHE   HB3    H  N N 415 
PHE   HD1    H  N N 416 
PHE   HD2    H  N N 417 
PHE   HE1    H  N N 418 
PHE   HE2    H  N N 419 
PHE   HZ     H  N N 420 
PHE   HXT    H  N N 421 
PRO   N      N  N N 422 
PRO   CA     C  N S 423 
PRO   C      C  N N 424 
PRO   O      O  N N 425 
PRO   CB     C  N N 426 
PRO   CG     C  N N 427 
PRO   CD     C  N N 428 
PRO   OXT    O  N N 429 
PRO   H      H  N N 430 
PRO   HA     H  N N 431 
PRO   HB2    H  N N 432 
PRO   HB3    H  N N 433 
PRO   HG2    H  N N 434 
PRO   HG3    H  N N 435 
PRO   HD2    H  N N 436 
PRO   HD3    H  N N 437 
PRO   HXT    H  N N 438 
SER   N      N  N N 439 
SER   CA     C  N S 440 
SER   C      C  N N 441 
SER   O      O  N N 442 
SER   CB     C  N N 443 
SER   OG     O  N N 444 
SER   OXT    O  N N 445 
SER   H      H  N N 446 
SER   H2     H  N N 447 
SER   HA     H  N N 448 
SER   HB2    H  N N 449 
SER   HB3    H  N N 450 
SER   HG     H  N N 451 
SER   HXT    H  N N 452 
THR   N      N  N N 453 
THR   CA     C  N S 454 
THR   C      C  N N 455 
THR   O      O  N N 456 
THR   CB     C  N R 457 
THR   OG1    O  N N 458 
THR   CG2    C  N N 459 
THR   OXT    O  N N 460 
THR   H      H  N N 461 
THR   H2     H  N N 462 
THR   HA     H  N N 463 
THR   HB     H  N N 464 
THR   HG1    H  N N 465 
THR   HG21   H  N N 466 
THR   HG22   H  N N 467 
THR   HG23   H  N N 468 
THR   HXT    H  N N 469 
TRP   N      N  N N 470 
TRP   CA     C  N S 471 
TRP   C      C  N N 472 
TRP   O      O  N N 473 
TRP   CB     C  N N 474 
TRP   CG     C  Y N 475 
TRP   CD1    C  Y N 476 
TRP   CD2    C  Y N 477 
TRP   NE1    N  Y N 478 
TRP   CE2    C  Y N 479 
TRP   CE3    C  Y N 480 
TRP   CZ2    C  Y N 481 
TRP   CZ3    C  Y N 482 
TRP   CH2    C  Y N 483 
TRP   OXT    O  N N 484 
TRP   H      H  N N 485 
TRP   H2     H  N N 486 
TRP   HA     H  N N 487 
TRP   HB2    H  N N 488 
TRP   HB3    H  N N 489 
TRP   HD1    H  N N 490 
TRP   HE1    H  N N 491 
TRP   HE3    H  N N 492 
TRP   HZ2    H  N N 493 
TRP   HZ3    H  N N 494 
TRP   HH2    H  N N 495 
TRP   HXT    H  N N 496 
TYR   N      N  N N 497 
TYR   CA     C  N S 498 
TYR   C      C  N N 499 
TYR   O      O  N N 500 
TYR   CB     C  N N 501 
TYR   CG     C  Y N 502 
TYR   CD1    C  Y N 503 
TYR   CD2    C  Y N 504 
TYR   CE1    C  Y N 505 
TYR   CE2    C  Y N 506 
TYR   CZ     C  Y N 507 
TYR   OH     O  N N 508 
TYR   OXT    O  N N 509 
TYR   H      H  N N 510 
TYR   H2     H  N N 511 
TYR   HA     H  N N 512 
TYR   HB2    H  N N 513 
TYR   HB3    H  N N 514 
TYR   HD1    H  N N 515 
TYR   HD2    H  N N 516 
TYR   HE1    H  N N 517 
TYR   HE2    H  N N 518 
TYR   HH     H  N N 519 
TYR   HXT    H  N N 520 
VAL   N      N  N N 521 
VAL   CA     C  N S 522 
VAL   C      C  N N 523 
VAL   O      O  N N 524 
VAL   CB     C  N N 525 
VAL   CG1    C  N N 526 
VAL   CG2    C  N N 527 
VAL   OXT    O  N N 528 
VAL   H      H  N N 529 
VAL   H2     H  N N 530 
VAL   HA     H  N N 531 
VAL   HB     H  N N 532 
VAL   HG11   H  N N 533 
VAL   HG12   H  N N 534 
VAL   HG13   H  N N 535 
VAL   HG21   H  N N 536 
VAL   HG22   H  N N 537 
VAL   HG23   H  N N 538 
VAL   HXT    H  N N 539 
# 
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 
A1AOJ C1    C2     sing N N 1   
A1AOJ C2    N1     sing N N 2   
A1AOJ N1    N2     sing N N 3   
A1AOJ N2    C3     sing N N 4   
A1AOJ C3    C4     sing N N 5   
A1AOJ N2    C5     sing N N 6   
A1AOJ C5    O1     doub N N 7   
A1AOJ C5    C6     sing N N 8   
A1AOJ C6    N3     sing N N 9   
A1AOJ N3    C7     sing N N 10  
A1AOJ C7    C8     sing N N 11  
A1AOJ C8    C9     sing N N 12  
A1AOJ C9    C10    sing N N 13  
A1AOJ C9    C11    sing N N 14  
A1AOJ C7    O2     doub N N 15  
A1AOJ C6    C12    sing N N 16  
A1AOJ C12   C13    sing N N 17  
A1AOJ C13   N4     doub Y N 18  
A1AOJ N4    C14    sing Y N 19  
A1AOJ C14   C15    doub Y N 20  
A1AOJ C15   S1     sing Y N 21  
A1AOJ C14   C16    sing N N 22  
A1AOJ C16   C17    doub Y N 23  
A1AOJ C17   C18    sing Y N 24  
A1AOJ C18   C19    doub Y N 25  
A1AOJ C19   C20    sing Y N 26  
A1AOJ C20   C21    doub Y N 27  
A1AOJ C19   N5     sing Y N 28  
A1AOJ N5    C22    sing N N 29  
A1AOJ C22   C23    sing N N 30  
A1AOJ N5    C24    sing Y N 31  
A1AOJ C24   C25    sing N N 32  
A1AOJ C25   C26    doub Y N 33  
A1AOJ C26   C27    sing N N 34  
A1AOJ C27   O3     sing N N 35  
A1AOJ O3    C28    sing N N 36  
A1AOJ C27   C29    sing N N 37  
A1AOJ C26   N6     sing Y N 38  
A1AOJ N6    C30    doub Y N 39  
A1AOJ C30   C31    sing Y N 40  
A1AOJ C31   C32    doub Y N 41  
A1AOJ C24   C33    doub Y N 42  
A1AOJ C33   C34    sing N N 43  
A1AOJ C34   C35    sing N N 44  
A1AOJ C35   C36    sing N N 45  
A1AOJ C35   C37    sing N N 46  
A1AOJ C35   C38    sing N N 47  
A1AOJ C38   O4     sing N N 48  
A1AOJ O4    C39    sing N N 49  
A1AOJ C39   O5     doub N N 50  
A1AOJ C1    C4     sing N N 51  
A1AOJ C8    C11    sing N N 52  
A1AOJ C13   S1     sing Y N 53  
A1AOJ C16   C21    sing Y N 54  
A1AOJ C25   C32    sing Y N 55  
A1AOJ C2    C39    sing N N 56  
A1AOJ C18   C33    sing Y N 57  
A1AOJ C1    H1     sing N N 58  
A1AOJ C1    H2     sing N N 59  
A1AOJ C10   H15    sing N N 60  
A1AOJ C10   H14    sing N N 61  
A1AOJ C10   H13    sing N N 62  
A1AOJ C11   H17    sing N N 63  
A1AOJ C11   H16    sing N N 64  
A1AOJ C12   H19    sing N N 65  
A1AOJ C12   H18    sing N N 66  
A1AOJ C15   H20    sing N N 67  
A1AOJ C17   H21    sing N N 68  
A1AOJ C2    H3     sing N N 69  
A1AOJ C20   H22    sing N N 70  
A1AOJ C21   H23    sing N N 71  
A1AOJ C22   H24    sing N N 72  
A1AOJ C22   H25    sing N N 73  
A1AOJ C23   H27    sing N N 74  
A1AOJ C23   H26    sing N N 75  
A1AOJ C23   H28    sing N N 76  
A1AOJ C27   H29    sing N N 77  
A1AOJ C28   H30    sing N N 78  
A1AOJ C28   H31    sing N N 79  
A1AOJ C28   H32    sing N N 80  
A1AOJ C29   H34    sing N N 81  
A1AOJ C29   H33    sing N N 82  
A1AOJ C29   H35    sing N N 83  
A1AOJ C3    H5     sing N N 84  
A1AOJ C3    H6     sing N N 85  
A1AOJ C30   H36    sing N N 86  
A1AOJ C31   H37    sing N N 87  
A1AOJ C32   H38    sing N N 88  
A1AOJ C34   H40    sing N N 89  
A1AOJ C34   H39    sing N N 90  
A1AOJ C36   H41    sing N N 91  
A1AOJ C36   H43    sing N N 92  
A1AOJ C36   H42    sing N N 93  
A1AOJ C37   H45    sing N N 94  
A1AOJ C37   H44    sing N N 95  
A1AOJ C37   H46    sing N N 96  
A1AOJ C38   H48    sing N N 97  
A1AOJ C38   H47    sing N N 98  
A1AOJ C4    H8     sing N N 99  
A1AOJ C4    H7     sing N N 100 
A1AOJ C6    H9     sing N N 101 
A1AOJ C8    H11    sing N N 102 
A1AOJ C9    H12    sing N N 103 
A1AOJ N1    H4     sing N N 104 
A1AOJ N3    H10    sing N N 105 
ALA   N     CA     sing N N 106 
ALA   N     H      sing N N 107 
ALA   N     H2     sing N N 108 
ALA   CA    C      sing N N 109 
ALA   CA    CB     sing N N 110 
ALA   CA    HA     sing N N 111 
ALA   C     O      doub N N 112 
ALA   C     OXT    sing N N 113 
ALA   CB    HB1    sing N N 114 
ALA   CB    HB2    sing N N 115 
ALA   CB    HB3    sing N N 116 
ALA   OXT   HXT    sing N N 117 
ARG   N     CA     sing N N 118 
ARG   N     H      sing N N 119 
ARG   N     H2     sing N N 120 
ARG   CA    C      sing N N 121 
ARG   CA    CB     sing N N 122 
ARG   CA    HA     sing N N 123 
ARG   C     O      doub N N 124 
ARG   C     OXT    sing N N 125 
ARG   CB    CG     sing N N 126 
ARG   CB    HB2    sing N N 127 
ARG   CB    HB3    sing N N 128 
ARG   CG    CD     sing N N 129 
ARG   CG    HG2    sing N N 130 
ARG   CG    HG3    sing N N 131 
ARG   CD    NE     sing N N 132 
ARG   CD    HD2    sing N N 133 
ARG   CD    HD3    sing N N 134 
ARG   NE    CZ     sing N N 135 
ARG   NE    HE     sing N N 136 
ARG   CZ    NH1    sing N N 137 
ARG   CZ    NH2    doub N N 138 
ARG   NH1   HH11   sing N N 139 
ARG   NH1   HH12   sing N N 140 
ARG   NH2   HH21   sing N N 141 
ARG   NH2   HH22   sing N N 142 
ARG   OXT   HXT    sing N N 143 
ASN   N     CA     sing N N 144 
ASN   N     H      sing N N 145 
ASN   N     H2     sing N N 146 
ASN   CA    C      sing N N 147 
ASN   CA    CB     sing N N 148 
ASN   CA    HA     sing N N 149 
ASN   C     O      doub N N 150 
ASN   C     OXT    sing N N 151 
ASN   CB    CG     sing N N 152 
ASN   CB    HB2    sing N N 153 
ASN   CB    HB3    sing N N 154 
ASN   CG    OD1    doub N N 155 
ASN   CG    ND2    sing N N 156 
ASN   ND2   HD21   sing N N 157 
ASN   ND2   HD22   sing N N 158 
ASN   OXT   HXT    sing N N 159 
ASP   N     CA     sing N N 160 
ASP   N     H      sing N N 161 
ASP   N     H2     sing N N 162 
ASP   CA    C      sing N N 163 
ASP   CA    CB     sing N N 164 
ASP   CA    HA     sing N N 165 
ASP   C     O      doub N N 166 
ASP   C     OXT    sing N N 167 
ASP   CB    CG     sing N N 168 
ASP   CB    HB2    sing N N 169 
ASP   CB    HB3    sing N N 170 
ASP   CG    OD1    doub N N 171 
ASP   CG    OD2    sing N N 172 
ASP   OD2   HD2    sing N N 173 
ASP   OXT   HXT    sing N N 174 
CYS   N     CA     sing N N 175 
CYS   N     H      sing N N 176 
CYS   N     H2     sing N N 177 
CYS   CA    C      sing N N 178 
CYS   CA    CB     sing N N 179 
CYS   CA    HA     sing N N 180 
CYS   C     O      doub N N 181 
CYS   C     OXT    sing N N 182 
CYS   CB    SG     sing N N 183 
CYS   CB    HB2    sing N N 184 
CYS   CB    HB3    sing N N 185 
CYS   SG    HG     sing N N 186 
CYS   OXT   HXT    sing N N 187 
GLN   N     CA     sing N N 188 
GLN   N     H      sing N N 189 
GLN   N     H2     sing N N 190 
GLN   CA    C      sing N N 191 
GLN   CA    CB     sing N N 192 
GLN   CA    HA     sing N N 193 
GLN   C     O      doub N N 194 
GLN   C     OXT    sing N N 195 
GLN   CB    CG     sing N N 196 
GLN   CB    HB2    sing N N 197 
GLN   CB    HB3    sing N N 198 
GLN   CG    CD     sing N N 199 
GLN   CG    HG2    sing N N 200 
GLN   CG    HG3    sing N N 201 
GLN   CD    OE1    doub N N 202 
GLN   CD    NE2    sing N N 203 
GLN   NE2   HE21   sing N N 204 
GLN   NE2   HE22   sing N N 205 
GLN   OXT   HXT    sing N N 206 
GLU   N     CA     sing N N 207 
GLU   N     H      sing N N 208 
GLU   N     H2     sing N N 209 
GLU   CA    C      sing N N 210 
GLU   CA    CB     sing N N 211 
GLU   CA    HA     sing N N 212 
GLU   C     O      doub N N 213 
GLU   C     OXT    sing N N 214 
GLU   CB    CG     sing N N 215 
GLU   CB    HB2    sing N N 216 
GLU   CB    HB3    sing N N 217 
GLU   CG    CD     sing N N 218 
GLU   CG    HG2    sing N N 219 
GLU   CG    HG3    sing N N 220 
GLU   CD    OE1    doub N N 221 
GLU   CD    OE2    sing N N 222 
GLU   OE2   HE2    sing N N 223 
GLU   OXT   HXT    sing N N 224 
GLY   N     CA     sing N N 225 
GLY   N     H      sing N N 226 
GLY   N     H2     sing N N 227 
GLY   CA    C      sing N N 228 
GLY   CA    HA2    sing N N 229 
GLY   CA    HA3    sing N N 230 
GLY   C     O      doub N N 231 
GLY   C     OXT    sing N N 232 
GLY   OXT   HXT    sing N N 233 
GNP   PG    O1G    doub N N 234 
GNP   PG    O2G    sing N N 235 
GNP   PG    O3G    sing N N 236 
GNP   PG    N3B    sing N N 237 
GNP   O2G   HOG2   sing N N 238 
GNP   O3G   HOG3   sing N N 239 
GNP   N3B   PB     sing N N 240 
GNP   N3B   HNB3   sing N N 241 
GNP   PB    O1B    doub N N 242 
GNP   PB    O2B    sing N N 243 
GNP   PB    O3A    sing N N 244 
GNP   O2B   HOB2   sing N N 245 
GNP   O3A   PA     sing N N 246 
GNP   PA    O1A    doub N N 247 
GNP   PA    O2A    sing N N 248 
GNP   PA    "O5'"  sing N N 249 
GNP   O2A   HOA2   sing N N 250 
GNP   "O5'" "C5'"  sing N N 251 
GNP   "C5'" "C4'"  sing N N 252 
GNP   "C5'" "H5'2" sing N N 253 
GNP   "C5'" "H5'1" sing N N 254 
GNP   "C4'" "O4'"  sing N N 255 
GNP   "C4'" "C3'"  sing N N 256 
GNP   "C4'" "H4'"  sing N N 257 
GNP   "O4'" "C1'"  sing N N 258 
GNP   "C3'" "O3'"  sing N N 259 
GNP   "C3'" "C2'"  sing N N 260 
GNP   "C3'" "H3'"  sing N N 261 
GNP   "O3'" "HO3'" sing N N 262 
GNP   "C2'" "O2'"  sing N N 263 
GNP   "C2'" "C1'"  sing N N 264 
GNP   "C2'" "H2'"  sing N N 265 
GNP   "O2'" "HO2'" sing N N 266 
GNP   "C1'" N9     sing N N 267 
GNP   "C1'" "H1'"  sing N N 268 
GNP   N9    C8     sing Y N 269 
GNP   N9    C4     sing Y N 270 
GNP   C8    N7     doub Y N 271 
GNP   C8    H8     sing N N 272 
GNP   N7    C5     sing Y N 273 
GNP   C5    C6     sing Y N 274 
GNP   C5    C4     doub Y N 275 
GNP   C6    O6     doub N N 276 
GNP   C6    N1     sing Y N 277 
GNP   N1    C2     sing Y N 278 
GNP   N1    HN1    sing N N 279 
GNP   C2    N2     sing N N 280 
GNP   C2    N3     doub Y N 281 
GNP   N2    HN21   sing N N 282 
GNP   N2    HN22   sing N N 283 
GNP   N3    C4     sing Y N 284 
HIS   N     CA     sing N N 285 
HIS   N     H      sing N N 286 
HIS   N     H2     sing N N 287 
HIS   CA    C      sing N N 288 
HIS   CA    CB     sing N N 289 
HIS   CA    HA     sing N N 290 
HIS   C     O      doub N N 291 
HIS   C     OXT    sing N N 292 
HIS   CB    CG     sing N N 293 
HIS   CB    HB2    sing N N 294 
HIS   CB    HB3    sing N N 295 
HIS   CG    ND1    sing Y N 296 
HIS   CG    CD2    doub Y N 297 
HIS   ND1   CE1    doub Y N 298 
HIS   ND1   HD1    sing N N 299 
HIS   CD2   NE2    sing Y N 300 
HIS   CD2   HD2    sing N N 301 
HIS   CE1   NE2    sing Y N 302 
HIS   CE1   HE1    sing N N 303 
HIS   NE2   HE2    sing N N 304 
HIS   OXT   HXT    sing N N 305 
HOH   O     H1     sing N N 306 
HOH   O     H2     sing N N 307 
ILE   N     CA     sing N N 308 
ILE   N     H      sing N N 309 
ILE   N     H2     sing N N 310 
ILE   CA    C      sing N N 311 
ILE   CA    CB     sing N N 312 
ILE   CA    HA     sing N N 313 
ILE   C     O      doub N N 314 
ILE   C     OXT    sing N N 315 
ILE   CB    CG1    sing N N 316 
ILE   CB    CG2    sing N N 317 
ILE   CB    HB     sing N N 318 
ILE   CG1   CD1    sing N N 319 
ILE   CG1   HG12   sing N N 320 
ILE   CG1   HG13   sing N N 321 
ILE   CG2   HG21   sing N N 322 
ILE   CG2   HG22   sing N N 323 
ILE   CG2   HG23   sing N N 324 
ILE   CD1   HD11   sing N N 325 
ILE   CD1   HD12   sing N N 326 
ILE   CD1   HD13   sing N N 327 
ILE   OXT   HXT    sing N N 328 
LEU   N     CA     sing N N 329 
LEU   N     H      sing N N 330 
LEU   N     H2     sing N N 331 
LEU   CA    C      sing N N 332 
LEU   CA    CB     sing N N 333 
LEU   CA    HA     sing N N 334 
LEU   C     O      doub N N 335 
LEU   C     OXT    sing N N 336 
LEU   CB    CG     sing N N 337 
LEU   CB    HB2    sing N N 338 
LEU   CB    HB3    sing N N 339 
LEU   CG    CD1    sing N N 340 
LEU   CG    CD2    sing N N 341 
LEU   CG    HG     sing N N 342 
LEU   CD1   HD11   sing N N 343 
LEU   CD1   HD12   sing N N 344 
LEU   CD1   HD13   sing N N 345 
LEU   CD2   HD21   sing N N 346 
LEU   CD2   HD22   sing N N 347 
LEU   CD2   HD23   sing N N 348 
LEU   OXT   HXT    sing N N 349 
LYS   N     CA     sing N N 350 
LYS   N     H      sing N N 351 
LYS   N     H2     sing N N 352 
LYS   CA    C      sing N N 353 
LYS   CA    CB     sing N N 354 
LYS   CA    HA     sing N N 355 
LYS   C     O      doub N N 356 
LYS   C     OXT    sing N N 357 
LYS   CB    CG     sing N N 358 
LYS   CB    HB2    sing N N 359 
LYS   CB    HB3    sing N N 360 
LYS   CG    CD     sing N N 361 
LYS   CG    HG2    sing N N 362 
LYS   CG    HG3    sing N N 363 
LYS   CD    CE     sing N N 364 
LYS   CD    HD2    sing N N 365 
LYS   CD    HD3    sing N N 366 
LYS   CE    NZ     sing N N 367 
LYS   CE    HE2    sing N N 368 
LYS   CE    HE3    sing N N 369 
LYS   NZ    HZ1    sing N N 370 
LYS   NZ    HZ2    sing N N 371 
LYS   NZ    HZ3    sing N N 372 
LYS   OXT   HXT    sing N N 373 
MET   N     CA     sing N N 374 
MET   N     H      sing N N 375 
MET   N     H2     sing N N 376 
MET   CA    C      sing N N 377 
MET   CA    CB     sing N N 378 
MET   CA    HA     sing N N 379 
MET   C     O      doub N N 380 
MET   C     OXT    sing N N 381 
MET   CB    CG     sing N N 382 
MET   CB    HB2    sing N N 383 
MET   CB    HB3    sing N N 384 
MET   CG    SD     sing N N 385 
MET   CG    HG2    sing N N 386 
MET   CG    HG3    sing N N 387 
MET   SD    CE     sing N N 388 
MET   CE    HE1    sing N N 389 
MET   CE    HE2    sing N N 390 
MET   CE    HE3    sing N N 391 
MET   OXT   HXT    sing N N 392 
PHE   N     CA     sing N N 393 
PHE   N     H      sing N N 394 
PHE   N     H2     sing N N 395 
PHE   CA    C      sing N N 396 
PHE   CA    CB     sing N N 397 
PHE   CA    HA     sing N N 398 
PHE   C     O      doub N N 399 
PHE   C     OXT    sing N N 400 
PHE   CB    CG     sing N N 401 
PHE   CB    HB2    sing N N 402 
PHE   CB    HB3    sing N N 403 
PHE   CG    CD1    doub Y N 404 
PHE   CG    CD2    sing Y N 405 
PHE   CD1   CE1    sing Y N 406 
PHE   CD1   HD1    sing N N 407 
PHE   CD2   CE2    doub Y N 408 
PHE   CD2   HD2    sing N N 409 
PHE   CE1   CZ     doub Y N 410 
PHE   CE1   HE1    sing N N 411 
PHE   CE2   CZ     sing Y N 412 
PHE   CE2   HE2    sing N N 413 
PHE   CZ    HZ     sing N N 414 
PHE   OXT   HXT    sing N N 415 
PRO   N     CA     sing N N 416 
PRO   N     CD     sing N N 417 
PRO   N     H      sing N N 418 
PRO   CA    C      sing N N 419 
PRO   CA    CB     sing N N 420 
PRO   CA    HA     sing N N 421 
PRO   C     O      doub N N 422 
PRO   C     OXT    sing N N 423 
PRO   CB    CG     sing N N 424 
PRO   CB    HB2    sing N N 425 
PRO   CB    HB3    sing N N 426 
PRO   CG    CD     sing N N 427 
PRO   CG    HG2    sing N N 428 
PRO   CG    HG3    sing N N 429 
PRO   CD    HD2    sing N N 430 
PRO   CD    HD3    sing N N 431 
PRO   OXT   HXT    sing N N 432 
SER   N     CA     sing N N 433 
SER   N     H      sing N N 434 
SER   N     H2     sing N N 435 
SER   CA    C      sing N N 436 
SER   CA    CB     sing N N 437 
SER   CA    HA     sing N N 438 
SER   C     O      doub N N 439 
SER   C     OXT    sing N N 440 
SER   CB    OG     sing N N 441 
SER   CB    HB2    sing N N 442 
SER   CB    HB3    sing N N 443 
SER   OG    HG     sing N N 444 
SER   OXT   HXT    sing N N 445 
THR   N     CA     sing N N 446 
THR   N     H      sing N N 447 
THR   N     H2     sing N N 448 
THR   CA    C      sing N N 449 
THR   CA    CB     sing N N 450 
THR   CA    HA     sing N N 451 
THR   C     O      doub N N 452 
THR   C     OXT    sing N N 453 
THR   CB    OG1    sing N N 454 
THR   CB    CG2    sing N N 455 
THR   CB    HB     sing N N 456 
THR   OG1   HG1    sing N N 457 
THR   CG2   HG21   sing N N 458 
THR   CG2   HG22   sing N N 459 
THR   CG2   HG23   sing N N 460 
THR   OXT   HXT    sing N N 461 
TRP   N     CA     sing N N 462 
TRP   N     H      sing N N 463 
TRP   N     H2     sing N N 464 
TRP   CA    C      sing N N 465 
TRP   CA    CB     sing N N 466 
TRP   CA    HA     sing N N 467 
TRP   C     O      doub N N 468 
TRP   C     OXT    sing N N 469 
TRP   CB    CG     sing N N 470 
TRP   CB    HB2    sing N N 471 
TRP   CB    HB3    sing N N 472 
TRP   CG    CD1    doub Y N 473 
TRP   CG    CD2    sing Y N 474 
TRP   CD1   NE1    sing Y N 475 
TRP   CD1   HD1    sing N N 476 
TRP   CD2   CE2    doub Y N 477 
TRP   CD2   CE3    sing Y N 478 
TRP   NE1   CE2    sing Y N 479 
TRP   NE1   HE1    sing N N 480 
TRP   CE2   CZ2    sing Y N 481 
TRP   CE3   CZ3    doub Y N 482 
TRP   CE3   HE3    sing N N 483 
TRP   CZ2   CH2    doub Y N 484 
TRP   CZ2   HZ2    sing N N 485 
TRP   CZ3   CH2    sing Y N 486 
TRP   CZ3   HZ3    sing N N 487 
TRP   CH2   HH2    sing N N 488 
TRP   OXT   HXT    sing N N 489 
TYR   N     CA     sing N N 490 
TYR   N     H      sing N N 491 
TYR   N     H2     sing N N 492 
TYR   CA    C      sing N N 493 
TYR   CA    CB     sing N N 494 
TYR   CA    HA     sing N N 495 
TYR   C     O      doub N N 496 
TYR   C     OXT    sing N N 497 
TYR   CB    CG     sing N N 498 
TYR   CB    HB2    sing N N 499 
TYR   CB    HB3    sing N N 500 
TYR   CG    CD1    doub Y N 501 
TYR   CG    CD2    sing Y N 502 
TYR   CD1   CE1    sing Y N 503 
TYR   CD1   HD1    sing N N 504 
TYR   CD2   CE2    doub Y N 505 
TYR   CD2   HD2    sing N N 506 
TYR   CE1   CZ     doub Y N 507 
TYR   CE1   HE1    sing N N 508 
TYR   CE2   CZ     sing Y N 509 
TYR   CE2   HE2    sing N N 510 
TYR   CZ    OH     sing N N 511 
TYR   OH    HH     sing N N 512 
TYR   OXT   HXT    sing N N 513 
VAL   N     CA     sing N N 514 
VAL   N     H      sing N N 515 
VAL   N     H2     sing N N 516 
VAL   CA    C      sing N N 517 
VAL   CA    CB     sing N N 518 
VAL   CA    HA     sing N N 519 
VAL   C     O      doub N N 520 
VAL   C     OXT    sing N N 521 
VAL   CB    CG1    sing N N 522 
VAL   CB    CG2    sing N N 523 
VAL   CB    HB     sing N N 524 
VAL   CG1   HG11   sing N N 525 
VAL   CG1   HG12   sing N N 526 
VAL   CG1   HG13   sing N N 527 
VAL   CG2   HG21   sing N N 528 
VAL   CG2   HG22   sing N N 529 
VAL   CG2   HG23   sing N N 530 
VAL   OXT   HXT    sing N N 531 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          In-house 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BG2 
_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]   0.015069 
_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]   0.011686 
_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]   0.007854 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG  ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . SER   A 1 1   ? 5.15500  1.46800   31.10700  1.000 49.65549 ?  0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 1   ? 5.49300  2.35800   29.99700  1.000 47.21328 ?  0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 1   ? 6.35500  1.64000   28.95300  1.000 45.71075 ?  0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 1   ? 7.04800  0.66900   29.25700  1.000 54.01446 ?  0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 1   ? 6.21500  3.61600   30.50600  1.000 47.50340 ?  0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 1   ? 6.42500  4.53800   29.45200  1.000 49.25919 ?  0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 2   ? 6.32600  2.13200   27.72000  1.000 41.79209 ?  1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 2   ? 6.94700  1.39200   26.64300  1.000 38.84333 ?  1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 2   ? 8.45800  1.58800   26.65800  1.000 34.78811 ?  1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 2   ? 8.97900  2.59600   27.14600  1.000 31.69713 ?  1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 2   ? 6.35400  1.81300   25.30200  1.000 39.19586 ?  1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 2   ? 6.67800  3.21300   24.86900  1.000 32.12239 ?  1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 2   ? 5.78100  3.58000   23.35600  1.000 31.88935 ?  1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 2   ? 4.09800  3.56900   23.97200  1.000 32.59161 ?  1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 3   ? 9.16200  0.60300   26.12400  1.000 33.23583 ?  2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 3   ? 10.60900 0.70700   26.01800  1.000 31.83105 ?  2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 3   ? 10.99900 1.84700   25.08400  1.000 28.75571 ?  2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 3   ? 10.39200 2.04800   24.02900  1.000 31.32786 ?  2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 3   ? 11.18400 -0.60800  25.50800  1.000 33.75414 ?  2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 3   ? 10.84100 -1.65400  26.43200  1.000 41.74077 ?  2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 3   ? 12.69500 -0.51000  25.34300  1.000 31.41029 ?  2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 4   ? 12.00300 2.62200   25.48400  1.000 28.01801 ?  3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 4   ? 12.51800 3.67500   24.62800  1.000 28.12573 ?  3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 4   ? 13.86000 3.26000   24.05300  1.000 28.63670 ?  3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 4   ? 14.67300 2.62000   24.73200  1.000 28.37749 ?  3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 4   ? 12.65200 4.99500   25.38100  1.000 30.25191 ?  3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 4   ? 11.32000 5.46400   25.94800  1.000 36.40866 ?  3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 4   ? 11.43400 6.76000   26.72300  1.000 44.11786 ?  3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 4   ? 12.24600 7.62200   26.31000  1.000 47.24425 ?  3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 4   ? 10.71300 6.91100   27.74200  1.000 48.29721 -1 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 5   ? 14.08300 3.61700   22.79700  1.000 24.80883 ?  4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 5   ? 15.31500 3.28100   22.07900  1.000 23.22671 ?  4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 5   ? 15.96700 4.58300   21.64700  1.000 22.76373 ?  4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 5   ? 15.33800 5.37500   20.92900  1.000 25.71643 ?  4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 5   ? 15.03000 2.38600   20.85500  1.000 25.46576 ?  4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 5   ? 14.50900 1.00800   21.21700  1.000 24.11175 ?  4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 5   ? 15.37600 0.01500   21.61900  1.000 28.09737 ?  4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 5   ? 13.14500 0.73100   21.23400  1.000 28.50983 ?  4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 5   ? 14.91700 -1.24600  21.97200  1.000 34.40471 ?  4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 5   ? 12.67300 -0.53600  21.59800  1.000 29.99539 ?  4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 5   ? 13.56100 -1.50500  21.96500  1.000 30.14630 ?  4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 5   ? 13.11400 -2.75600  22.34500  1.000 34.12887 ?  4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 6   ? 17.24000 4.79100   22.04200  1.000 23.45163 ?  5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 6   ? 17.95200 6.02000   21.69600  1.000 24.38903 ?  5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 6   ? 18.73800 5.78800   20.41200  1.000 23.42491 ?  5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 6   ? 19.81400 5.17900   20.42800  1.000 23.81892 ?  5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 6   ? 18.88300 6.46700   22.82200  1.000 29.48626 ?  5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 6   ? 18.11100 6.87000   24.11300  1.000 30.46190 ?  5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 6   ? 19.06100 7.42900   25.19700  1.000 34.35994 ?  5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 6   ? 19.88500 6.31700   25.86400  1.000 45.57125 ?  5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 6   ? 21.03500 6.76700   26.73900  1.000 49.24021 ?  5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 7   ? 18.19800 6.27800   19.30200  1.000 21.76560 ?  6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 7   ? 18.81100 6.13200   17.98800  1.000 22.37042 ?  6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 7   ? 19.53000 7.42100   17.63200  1.000 23.35063 ?  6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 7   ? 19.06000 8.49600   17.99100  1.000 23.75616 ?  6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 7   ? 17.76200 5.84100   16.91000  1.000 22.13539 ?  6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 7   ? 16.69600 4.81900   17.30600  1.000 25.08403 ?  6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 7   ? 15.78500 4.60700   16.07900  1.000 24.17063 ?  6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 7   ? 17.36500 3.52500   17.67600  1.000 23.68188 ?  6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 8   ? 20.67700 7.30800   16.94200  1.000 21.14531 ?  7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 8   ? 21.45900 8.45700   16.48300  1.000 20.96385 ?  7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 8   ? 21.73800 8.26900   15.00200  1.000 21.87353 ?  7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 8   ? 22.18300 7.19700   14.58700  1.000 21.71655 ?  7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 8   ? 22.78100 8.58900   17.26900  1.000 20.48965 ?  7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 8   ? 23.51700 9.82700   16.83700  1.000 20.20649 ?  7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 8   ? 22.44600 8.64100   18.73100  1.000 20.43068 ?  7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 9   ? 21.47700 9.30200   14.20900  1.000 21.42653 ?  8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 9   ? 21.66800 9.24800   12.76400  1.000 21.96229 ?  8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 9   ? 22.94000 10.01300  12.44900  1.000 21.91981 ?  8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 9   ? 23.02000 11.21400  12.73200  1.000 21.59903 ?  8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 9   ? 20.45900 9.85800   12.03100  1.000 21.87892 ?  8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 9   ? 20.64900 9.72000   10.55300  1.000 22.10475 ?  8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 9   ? 19.14400 9.14000   12.51100  1.000 21.96513 ?  8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 10  ? 23.92800 9.33800   11.84000  1.000 21.67869 ?  9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 10  ? 25.22500 9.94800   11.54600  1.000 20.69789 ?  9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 10  ? 25.58800 9.75200   10.07400  1.000 20.98692 ?  9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 10  ? 25.02900 8.90600   9.37300   1.000 22.30572 ?  9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 10  ? 26.36300 9.37500   12.43400  1.000 20.53251 ?  9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 10  ? 26.05500 9.66600   13.93100  1.000 22.60412 ?  9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 10  ? 26.58600 7.87300   12.13700  1.000 20.82602 ?  9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 11  ? 26.55800 10.54900  9.61500   1.000 20.86827 ?  10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 11  ? 26.95900 10.51500  8.21700   1.000 22.49820 ?  10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 11  ? 27.37800 11.88000  7.71300   1.000 21.74317 ?  10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 11  ? 27.19400 12.88300  8.39700   1.000 22.67949 ?  10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 12  ? 27.96600 11.92200  6.52400   1.000 23.25964 ?  11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 12  ? 28.53100 13.13500  5.95900   1.000 24.15031 ?  11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 12  ? 27.45100 14.15900  5.62300   1.000 26.62166 ?  11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 12  ? 26.25700 13.84800  5.51500   1.000 21.85190 ?  11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 12  ? 29.30800 12.79800  4.67700   1.000 23.38926 ?  11  ALA   A CB    1 
ATOM   90   N  N     . VAL   A 1 13  ? 27.89400 15.39900  5.39500   1.000 25.69269 ?  12  VAL   A N     1 
ATOM   91   C  CA    . VAL   A 1 13  ? 26.95400 16.46100  5.05400   1.000 25.86134 ?  12  VAL   A CA    1 
ATOM   92   C  C     . VAL   A 1 13  ? 26.19700 16.08800  3.78100   1.000 27.66441 ?  12  VAL   A C     1 
ATOM   93   O  O     . VAL   A 1 13  ? 26.78300 15.61900  2.79300   1.000 28.42410 ?  12  VAL   A O     1 
ATOM   94   C  CB    . VAL   A 1 13  ? 27.68900 17.80500  4.89600   1.000 28.50869 ?  12  VAL   A CB    1 
ATOM   95   C  CG1   . VAL   A 1 13  ? 26.81700 18.80700  4.20000   1.000 35.99882 ?  12  VAL   A CG1   1 
ATOM   96   C  CG2   . VAL   A 1 13  ? 28.05000 18.35100  6.24700   1.000 32.77089 ?  12  VAL   A CG2   1 
ATOM   97   N  N     . GLY   A 1 14  ? 24.87000 16.28000  3.81000   1.000 26.50302 ?  13  GLY   A N     1 
ATOM   98   C  CA    . GLY   A 1 14  ? 24.03600 16.11600  2.63100   1.000 23.23144 ?  13  GLY   A CA    1 
ATOM   99   C  C     . GLY   A 1 14  ? 23.66500 14.70000  2.24000   1.000 24.23622 ?  13  GLY   A C     1 
ATOM   100  O  O     . GLY   A 1 14  ? 23.06200 14.52100  1.17100   1.000 28.23787 ?  13  GLY   A O     1 
ATOM   101  N  N     . VAL   A 1 15  ? 23.98900 13.68600  3.05000   1.000 24.83013 ?  14  VAL   A N     1 
ATOM   102  C  CA    . VAL   A 1 15  ? 23.66700 12.31700  2.62400   1.000 23.03111 ?  14  VAL   A CA    1 
ATOM   103  C  C     . VAL   A 1 15  ? 22.18900 11.98600  2.79000   1.000 22.67904 ?  14  VAL   A C     1 
ATOM   104  O  O     . VAL   A 1 15  ? 21.70900 11.01000  2.19400   1.000 24.64892 ?  14  VAL   A O     1 
ATOM   105  C  CB    . VAL   A 1 15  ? 24.45500 11.22700  3.37000   1.000 22.49991 ?  14  VAL   A CB    1 
ATOM   106  C  CG1   . VAL   A 1 15  ? 25.96700 11.29700  3.02300   1.000 22.51225 ?  14  VAL   A CG1   1 
ATOM   107  C  CG2   . VAL   A 1 15  ? 24.22300 11.31600  4.88000   1.000 23.80261 ?  14  VAL   A CG2   1 
ATOM   108  N  N     . GLY   A 1 16  ? 21.45500 12.76600  3.56400   1.000 23.24158 ?  15  GLY   A N     1 
ATOM   109  C  CA    . GLY   A 1 16  ? 20.02900 12.54700  3.75600   1.000 22.67470 ?  15  GLY   A CA    1 
ATOM   110  C  C     . GLY   A 1 16  ? 19.62800 12.15600  5.16500   1.000 23.33040 ?  15  GLY   A C     1 
ATOM   111  O  O     . GLY   A 1 16  ? 18.57800 11.49600  5.33600   1.000 22.53259 ?  15  GLY   A O     1 
ATOM   112  N  N     . LYS   A 1 17  ? 20.43900 12.48400  6.16900   1.000 22.20935 ?  16  LYS   A N     1 
ATOM   113  C  CA    . LYS   A 1 17  ? 20.09500 12.13900  7.54100   1.000 22.36803 ?  16  LYS   A CA    1 
ATOM   114  C  C     . LYS   A 1 17  ? 18.76000 12.76300  7.93900   1.000 22.50240 ?  16  LYS   A C     1 
ATOM   115  O  O     . LYS   A 1 17  ? 17.89000 12.10000  8.51400   1.000 22.27831 ?  16  LYS   A O     1 
ATOM   116  C  CB    . LYS   A 1 17  ? 21.20000 12.62800  8.49000   1.000 21.41501 ?  16  LYS   A CB    1 
ATOM   117  C  CG    . LYS   A 1 17  ? 22.51500 11.93500  8.22600   1.000 22.98732 ?  16  LYS   A CG    1 
ATOM   118  C  CD    . LYS   A 1 17  ? 23.62000 12.39400  9.22900   1.000 21.19421 ?  16  LYS   A CD    1 
ATOM   119  C  CE    . LYS   A 1 17  ? 23.94200 13.86300  9.10500   1.000 23.07516 ?  16  LYS   A CE    1 
ATOM   120  N  NZ    . LYS   A 1 17  ? 24.54000 14.24600  7.76500   1.000 23.06180 ?  16  LYS   A NZ    1 
ATOM   121  N  N     . SER   A 1 18  ? 18.61900 14.06300  7.70700   1.000 22.24123 ?  17  SER   A N     1 
ATOM   122  C  CA    . SER   A 1 18  ? 17.38300 14.73800  8.09400   1.000 22.66667 ?  17  SER   A CA    1 
ATOM   123  C  C     . SER   A 1 18  ? 16.22200 14.31500  7.22300   1.000 22.35776 ?  17  SER   A C     1 
ATOM   124  O  O     . SER   A 1 18  ? 15.11000 14.13500  7.73800   1.000 23.45499 ?  17  SER   A O     1 
ATOM   125  C  CB    . SER   A 1 18  ? 17.53800 16.24600  8.03500   1.000 21.80916 ?  17  SER   A CB    1 
ATOM   126  O  OG    . SER   A 1 18  ? 18.58300 16.64300  8.90600   1.000 22.08793 ?  17  SER   A OG    1 
ATOM   127  N  N     . ALA   A 1 19  ? 16.44300 14.19400  5.90400   1.000 23.04079 ?  18  ALA   A N     1 
ATOM   128  C  CA    . ALA   A 1 19  ? 15.34800 13.78200  5.02400   1.000 22.56146 ?  18  ALA   A CA    1 
ATOM   129  C  C     . ALA   A 1 19  ? 14.79800 12.41000  5.42000   1.000 23.33100 ?  18  ALA   A C     1 
ATOM   130  O  O     . ALA   A 1 19  ? 13.57600 12.19900  5.39500   1.000 23.64358 ?  18  ALA   A O     1 
ATOM   131  C  CB    . ALA   A 1 19  ? 15.80100 13.80300  3.56100   1.000 22.82989 ?  18  ALA   A CB    1 
ATOM   132  N  N     . LEU   A 1 20  ? 15.68500 11.48000  5.81900   1.000 22.92513 ?  19  LEU   A N     1 
ATOM   133  C  CA    . LEU   A 1 20  ? 15.25300 10.17600  6.31300   1.000 23.25979 ?  19  LEU   A CA    1 
ATOM   134  C  C     . LEU   A 1 20  ? 14.46000 10.31300  7.60000   1.000 23.12153 ?  19  LEU   A C     1 
ATOM   135  O  O     . LEU   A 1 20  ? 13.39900 9.69200   7.75400   1.000 23.52079 ?  19  LEU   A O     1 
ATOM   136  C  CB    . LEU   A 1 20  ? 16.45200 9.27600   6.55900   1.000 23.20371 ?  19  LEU   A CB    1 
ATOM   137  C  CG    . LEU   A 1 20  ? 17.05000 8.63700   5.31000   1.000 23.56948 ?  19  LEU   A CG    1 
ATOM   138  C  CD1   . LEU   A 1 20  ? 18.37800 8.00500   5.68100   1.000 25.27249 ?  19  LEU   A CD1   1 
ATOM   139  C  CD2   . LEU   A 1 20  ? 16.10800 7.55200   4.81200   1.000 24.21316 ?  19  LEU   A CD2   1 
ATOM   140  N  N     . THR   A 1 21  ? 14.95300 11.14400  8.52600   1.000 22.60793 ?  20  THR   A N     1 
ATOM   141  C  CA    . THR   A 1 21  ? 14.28100 11.24800  9.80700   1.000 23.34275 ?  20  THR   A CA    1 
ATOM   142  C  C     . THR   A 1 21  ? 12.92500 11.93700  9.66400   1.000 24.07758 ?  20  THR   A C     1 
ATOM   143  O  O     . THR   A 1 21  ? 11.93800 11.51300  10.27700  1.000 23.06535 ?  20  THR   A O     1 
ATOM   144  C  CB    . THR   A 1 21  ? 15.18700 11.99000  10.78500  1.000 22.21431 ?  20  THR   A CB    1 
ATOM   145  O  OG1   . THR   A 1 21  ? 16.41900 11.26000  10.91000  1.000 22.06101 ?  20  THR   A OG1   1 
ATOM   146  C  CG2   . THR   A 1 21  ? 14.51800 12.05400  12.14300  1.000 22.68564 ?  20  THR   A CG2   1 
ATOM   147  N  N     . ILE   A 1 22  ? 12.87300 13.02000  8.88800   1.000 22.52496 ?  21  ILE   A N     1 
ATOM   148  C  CA    . ILE   A 1 22  ? 11.60600 13.71100  8.66600   1.000 24.82068 ?  21  ILE   A CA    1 
ATOM   149  C  C     . ILE   A 1 22  ? 10.62200 12.85000  7.87000   1.000 24.57870 ?  21  ILE   A C     1 
ATOM   150  O  O     . ILE   A 1 22  ? 9.40800  12.95800  8.06600   1.000 24.60110 ?  21  ILE   A O     1 
ATOM   151  C  CB    . ILE   A 1 22  ? 11.87300 15.06900  8.00000   1.000 24.94889 ?  21  ILE   A CB    1 
ATOM   152  C  CG1   . ILE   A 1 22  ? 12.73600 15.92700  8.93100   1.000 26.87771 ?  21  ILE   A CG1   1 
ATOM   153  C  CG2   . ILE   A 1 22  ? 10.53100 15.77200  7.60100   1.000 30.23699 ?  21  ILE   A CG2   1 
ATOM   154  C  CD1   . ILE   A 1 22  ? 13.24700 17.21800  8.30200   1.000 31.62615 ?  21  ILE   A CD1   1 
ATOM   155  N  N     . GLN   A 1 23  ? 11.09600 11.95600  6.99100   1.000 23.59176 ?  22  GLN   A N     1 
ATOM   156  C  CA    . GLN   A 1 23  ? 10.14000 11.02600  6.38000   1.000 24.30981 ?  22  GLN   A CA    1 
ATOM   157  C  C     . GLN   A 1 23  ? 9.55000  10.09200  7.41600   1.000 26.93507 ?  22  GLN   A C     1 
ATOM   158  O  O     . GLN   A 1 23  ? 8.35800  9.78800   7.39300   1.000 24.98614 ?  22  GLN   A O     1 
ATOM   159  C  CB    . GLN   A 1 23  ? 10.79700 10.18800  5.30200   1.000 28.46301 ?  22  GLN   A CB    1 
ATOM   160  C  CG    . GLN   A 1 23  ? 10.74900 10.78200  3.94600   1.000 28.67720 ?  22  GLN   A CG    1 
ATOM   161  C  CD    . GLN   A 1 23  ? 9.34800  10.83000  3.29300   1.000 28.07668 ?  22  GLN   A CD    1 
ATOM   162  O  OE1   . GLN   A 1 23  ? 8.30000  10.60600  3.92200   1.000 29.59770 ?  22  GLN   A OE1   1 
ATOM   163  N  NE2   . GLN   A 1 23  ? 9.35300  11.09400  2.00000   1.000 26.84843 ?  22  GLN   A NE2   1 
ATOM   164  N  N     . LEU   A 1 24  ? 10.40600 9.54500   8.26700   1.000 24.28061 ?  23  LEU   A N     1 
ATOM   165  C  CA    . LEU   A 1 24  ? 9.94500  8.70700   9.35900   1.000 24.49670 ?  23  LEU   A CA    1 
ATOM   166  C  C     . LEU   A 1 24  ? 8.88900  9.41500   10.20200  1.000 25.51028 ?  23  LEU   A C     1 
ATOM   167  O  O     . LEU   A 1 24  ? 7.84000  8.83900   10.50900  1.000 26.96468 ?  23  LEU   A O     1 
ATOM   168  C  CB    . LEU   A 1 24  ? 11.13600 8.33400   10.22900  1.000 24.10930 ?  23  LEU   A CB    1 
ATOM   169  C  CG    . LEU   A 1 24  ? 10.66900 7.42800   11.37300  1.000 24.36299 ?  23  LEU   A CG    1 
ATOM   170  C  CD1   . LEU   A 1 24  ? 10.31200 6.06700   10.84700  1.000 25.39569 ?  23  LEU   A CD1   1 
ATOM   171  C  CD2   . LEU   A 1 24  ? 11.71400 7.33300   12.47800  1.000 26.68468 ?  23  LEU   A CD2   1 
ATOM   172  N  N     . ILE   A 1 25  ? 9.18700  10.64600  10.63400  1.000 26.16167 ?  24  ILE   A N     1 
ATOM   173  C  CA    . ILE   A 1 25  ? 8.37800  11.33100  11.65000  1.000 27.77961 ?  24  ILE   A CA    1 
ATOM   174  C  C     . ILE   A 1 25  ? 7.20300  12.05800  11.00900  1.000 28.61731 ?  24  ILE   A C     1 
ATOM   175  O  O     . ILE   A 1 25  ? 6.08600  12.01000  11.52300  1.000 33.75844 ?  24  ILE   A O     1 
ATOM   176  C  CB    . ILE   A 1 25  ? 9.23200  12.32500  12.48600  1.000 28.44450 ?  24  ILE   A CB    1 
ATOM   177  C  CG1   . ILE   A 1 25  ? 10.49900 11.71500  13.13300  1.000 26.12490 ?  24  ILE   A CG1   1 
ATOM   178  C  CG2   . ILE   A 1 25  ? 8.35400  13.06100  13.53800  1.000 29.66780 ?  24  ILE   A CG2   1 
ATOM   179  C  CD1   . ILE   A 1 25  ? 10.25900 10.52800  13.97100  1.000 27.08371 ?  24  ILE   A CD1   1 
ATOM   180  N  N     . GLN   A 1 26  ? 7.40600  12.71400  9.86300   1.000 25.47063 ?  25  GLN   A N     1 
ATOM   181  C  CA    . GLN   A 1 26  ? 6.37600  13.58500  9.30400   1.000 28.35065 ?  25  GLN   A CA    1 
ATOM   182  C  C     . GLN   A 1 26  ? 5.77200  13.09200  7.99100   1.000 32.83414 ?  25  GLN   A C     1 
ATOM   183  O  O     . GLN   A 1 26  ? 4.78800  13.69100  7.51200   1.000 33.91840 ?  25  GLN   A O     1 
ATOM   184  C  CB    . GLN   A 1 26  ? 6.94900  14.99300  9.12500   1.000 31.14470 ?  25  GLN   A CB    1 
ATOM   185  C  CG    . GLN   A 1 26  ? 7.20400  15.65500  10.47600  1.000 40.72481 ?  25  GLN   A CG    1 
ATOM   186  C  CD    . GLN   A 1 26  ? 7.99100  16.94200  10.38600  1.000 41.61967 ?  25  GLN   A CD    1 
ATOM   187  O  OE1   . GLN   A 1 26  ? 8.26200  17.45900  9.29400   1.000 46.63987 ?  25  GLN   A OE1   1 
ATOM   188  N  NE2   . GLN   A 1 26  ? 8.36100  17.47900  11.54700  1.000 51.75693 ?  25  GLN   A NE2   1 
ATOM   189  N  N     . ASN   A 1 27  ? 6.31800  12.01800  7.40700   1.000 27.89213 ?  26  ASN   A N     1 
ATOM   190  C  CA    . ASN   A 1 27  ? 5.81500  11.41800  6.15400   1.000 28.49594 ?  26  ASN   A CA    1 
ATOM   191  C  C     . ASN   A 1 27  ? 5.81900  12.42400  5.00000   1.000 35.26832 ?  26  ASN   A C     1 
ATOM   192  O  O     . ASN   A 1 27  ? 4.90300  12.44300  4.17000   1.000 36.81292 ?  26  ASN   A O     1 
ATOM   193  C  CB    . ASN   A 1 27  ? 4.41600  10.79800  6.32700   1.000 27.97871 ?  26  ASN   A CB    1 
ATOM   194  C  CG    . ASN   A 1 27  ? 4.25100  9.45500   5.55500   1.000 31.53267 ?  26  ASN   A CG    1 
ATOM   195  O  OD1   . ASN   A 1 27  ? 4.39600  8.38000   6.14500   1.000 37.22464 ?  26  ASN   A OD1   1 
ATOM   196  N  ND2   . ASN   A 1 27  ? 3.91200  9.52800   4.22400   1.000 31.65500 ?  26  ASN   A ND2   1 
ATOM   197  N  N     . HIS   A 1 28  ? 6.85500  13.25900  4.93900   1.000 32.24469 ?  27  HIS   A N     1 
ATOM   198  C  CA    . HIS   A 1 28  ? 7.00400  14.18800  3.78500   1.000 37.82430 ?  27  HIS   A CA    1 
ATOM   199  C  C     . HIS   A 1 28  ? 8.47600  14.40800  3.42300   1.000 34.41078 ?  27  HIS   A C     1 
ATOM   200  O  O     . HIS   A 1 28  ? 9.35200  14.22400  4.27900   1.000 29.14012 ?  27  HIS   A O     1 
ATOM   201  C  CB    . HIS   A 1 28  ? 6.26900  15.51200  4.02200   1.000 40.42940 ?  27  HIS   A CB    1 
ATOM   202  C  CG    . HIS   A 1 28  ? 6.92500  16.47500  4.94200   1.000 35.35325 ?  27  HIS   A CG    1 
ATOM   203  N  ND1   . HIS   A 1 28  ? 7.97100  17.28400  4.56500   1.000 43.91672 ?  27  HIS   A ND1   1 
ATOM   204  C  CD2   . HIS   A 1 28  ? 6.64800  16.79000  6.20500   1.000 41.12394 ?  27  HIS   A CD2   1 
ATOM   205  C  CE1   . HIS   A 1 28  ? 8.32700  18.03900  5.58900   1.000 42.86958 ?  27  HIS   A CE1   1 
ATOM   206  N  NE2   . HIS   A 1 28  ? 7.53300  17.75600  6.59500   1.000 45.66571 ?  27  HIS   A NE2   1 
ATOM   207  N  N     . PHE   A 1 29  ? 8.71200  14.82700  2.18700   1.000 35.15302 ?  28  PHE   A N     1 
ATOM   208  C  CA    . PHE   A 1 29  ? 10.08100 15.09300  1.68400   1.000 37.17951 ?  28  PHE   A CA    1 
ATOM   209  C  C     . PHE   A 1 29  ? 10.11800 16.43300  0.95900   1.000 36.86500 ?  28  PHE   A C     1 
ATOM   210  O  O     . PHE   A 1 29  ? 9.16600  16.73200  0.23400   1.000 44.59809 ?  28  PHE   A O     1 
ATOM   211  C  CB    . PHE   A 1 29  ? 10.50900 13.98700  0.71400   1.000 35.04864 ?  28  PHE   A CB    1 
ATOM   212  C  CG    . PHE   A 1 29  ? 11.82100 14.23300  -0.02000  1.000 31.41706 ?  28  PHE   A CG    1 
ATOM   213  C  CD1   . PHE   A 1 29  ? 13.03500 13.89100  0.55900   1.000 28.88470 ?  28  PHE   A CD1   1 
ATOM   214  C  CD2   . PHE   A 1 29  ? 11.83600 14.79900  -1.28700  1.000 35.13858 ?  28  PHE   A CD2   1 
ATOM   215  C  CE1   . PHE   A 1 29  ? 14.22600 14.11300  -0.10800  1.000 28.20043 ?  28  PHE   A CE1   1 
ATOM   216  C  CE2   . PHE   A 1 29  ? 13.03200 15.02700  -1.94400  1.000 36.94844 ?  28  PHE   A CE2   1 
ATOM   217  C  CZ    . PHE   A 1 29  ? 14.22200 14.67700  -1.35700  1.000 31.71977 ?  28  PHE   A CZ    1 
ATOM   218  N  N     . VAL   A 1 30  ? 11.18800 17.20000  1.13500   1.000 42.20967 ?  29  VAL   A N     1 
ATOM   219  C  CA    . VAL   A 1 30  ? 11.40300 18.48100  0.40600   1.000 45.62122 ?  29  VAL   A CA    1 
ATOM   220  C  C     . VAL   A 1 30  ? 12.85700 18.45400  -0.08800  1.000 40.73730 ?  29  VAL   A C     1 
ATOM   221  O  O     . VAL   A 1 30  ? 13.71300 17.95500  0.64800   1.000 39.29094 ?  29  VAL   A O     1 
ATOM   222  C  CB    . VAL   A 1 30  ? 11.16000 19.71700  1.29400   1.000 44.35726 ?  29  VAL   A CB    1 
ATOM   223  C  CG1   . VAL   A 1 30  ? 11.44900 21.01900  0.56000   1.000 47.96303 ?  29  VAL   A CG1   1 
ATOM   224  C  CG2   . VAL   A 1 30  ? 9.75300  19.73900  1.87700   1.000 45.39616 ?  29  VAL   A CG2   1 
ATOM   225  N  N     . ASP   A 1 31  ? 13.10400 18.96400  -1.29400  1.000 43.29555 ?  30  ASP   A N     1 
ATOM   226  C  CA    . ASP   A 1 31  ? 14.47100 18.92500  -1.87500  1.000 41.54541 ?  30  ASP   A CA    1 
ATOM   227  C  C     . ASP   A 1 31  ? 15.30600 20.06800  -1.30500  1.000 39.35274 ?  30  ASP   A C     1 
ATOM   228  O  O     . ASP   A 1 31  ? 16.46000 20.21600  -1.71600  1.000 48.98953 ?  30  ASP   A O     1 
ATOM   229  C  CB    . ASP   A 1 31  ? 14.45900 18.92900  -3.39300  1.000 44.68965 ?  30  ASP   A CB    1 
ATOM   230  C  CG    . ASP   A 1 31  ? 15.68800 18.32400  -4.05300  1.000 52.59654 ?  30  ASP   A CG    1 
ATOM   231  O  OD1   . ASP   A 1 31  ? 16.11300 17.23400  -3.61900  1.000 47.01402 ?  30  ASP   A OD1   1 
ATOM   232  O  OD2   . ASP   A 1 31  ? 16.21500 18.95700  -4.98900  1.000 58.31152 -1 30  ASP   A OD2   1 
ATOM   233  N  N     . GLU   A 1 32  ? 14.75000 20.85500  -0.39400  1.000 44.48249 ?  31  GLU   A N     1 
ATOM   234  C  CA    . GLU   A 1 32  ? 15.53700 22.01900  0.07400   1.000 39.69568 ?  31  GLU   A CA    1 
ATOM   235  C  C     . GLU   A 1 32  ? 16.57000 21.53200  1.08900   1.000 42.16547 ?  31  GLU   A C     1 
ATOM   236  O  O     . GLU   A 1 32  ? 16.29800 20.56500  1.81200   1.000 42.55154 ?  31  GLU   A O     1 
ATOM   237  C  CB    . GLU   A 1 32  ? 14.68200 23.14100  0.65200   1.000 41.41858 ?  31  GLU   A CB    1 
ATOM   238  C  CG    . GLU   A 1 32  ? 14.13900 24.07900  -0.41800  1.000 46.91400 ?  31  GLU   A CG    1 
ATOM   239  C  CD    . GLU   A 1 32  ? 13.19900 25.13400  0.12500   1.000 47.92095 ?  31  GLU   A CD    1 
ATOM   240  O  OE1   . GLU   A 1 32  ? 13.12400 25.33100  1.35300   1.000 52.61044 ?  31  GLU   A OE1   1 
ATOM   241  O  OE2   . GLU   A 1 32  ? 12.53800 25.76600  -0.71200  1.000 54.35553 -1 31  GLU   A OE2   1 
ATOM   242  N  N     . TYR   A 1 33  ? 17.70200 22.20900  1.13000   1.000 34.07196 ?  32  TYR   A N     1 
ATOM   243  C  CA    . TYR   A 1 33  ? 18.77600 21.80000  2.02900   1.000 35.46834 ?  32  TYR   A CA    1 
ATOM   244  C  C     . TYR   A 1 33  ? 18.81600 22.72200  3.24100   1.000 34.21993 ?  32  TYR   A C     1 
ATOM   245  O  O     . TYR   A 1 33  ? 19.25400 23.87000  3.14300   1.000 33.52026 ?  32  TYR   A O     1 
ATOM   246  C  CB    . TYR   A 1 33  ? 20.12700 21.79500  1.32100   1.000 32.46093 ?  32  TYR   A CB    1 
ATOM   247  C  CG    . TYR   A 1 33  ? 21.25500 21.51400  2.29400   1.000 35.80521 ?  32  TYR   A CG    1 
ATOM   248  C  CD1   . TYR   A 1 33  ? 21.09000 20.57000  3.32400   1.000 34.53018 ?  32  TYR   A CD1   1 
ATOM   249  C  CD2   . TYR   A 1 33  ? 22.47200 22.19400  2.20400   1.000 39.44992 ?  32  TYR   A CD2   1 
ATOM   250  C  CE1   . TYR   A 1 33  ? 22.11500 20.30400  4.21200   1.000 33.50022 ?  32  TYR   A CE1   1 
ATOM   251  C  CE2   . TYR   A 1 33  ? 23.51100 21.93500  3.09900   1.000 41.01764 ?  32  TYR   A CE2   1 
ATOM   252  C  CZ    . TYR   A 1 33  ? 23.31600 20.98400  4.10200   1.000 38.33705 ?  32  TYR   A CZ    1 
ATOM   253  O  OH    . TYR   A 1 33  ? 24.31600 20.71900  5.00000   1.000 38.82568 ?  32  TYR   A OH    1 
ATOM   254  N  N     . ASP   A 1 34  ? 18.39000 22.20800  4.39400   1.000 31.02089 ?  33  ASP   A N     1 
ATOM   255  C  CA    . ASP   A 1 34  ? 18.46100 22.95300  5.64400   1.000 32.13642 ?  33  ASP   A CA    1 
ATOM   256  C  C     . ASP   A 1 34  ? 19.49600 22.28400  6.53900   1.000 32.09694 ?  33  ASP   A C     1 
ATOM   257  O  O     . ASP   A 1 34  ? 19.17600 21.29400  7.21600   1.000 26.25902 ?  33  ASP   A O     1 
ATOM   258  C  CB    . ASP   A 1 34  ? 17.08300 22.97500  6.32000   1.000 33.21041 ?  33  ASP   A CB    1 
ATOM   259  C  CG    . ASP   A 1 34  ? 17.05300 23.79200  7.61300   1.000 36.46896 ?  33  ASP   A CG    1 
ATOM   260  O  OD1   . ASP   A 1 34  ? 18.03500 24.50800  7.92600   1.000 37.57555 ?  33  ASP   A OD1   1 
ATOM   261  O  OD2   . ASP   A 1 34  ? 16.01200 23.71500  8.31600   1.000 44.69472 -1 33  ASP   A OD2   1 
ATOM   262  N  N     . PRO   A 1 35  ? 20.73400 22.78300  6.58400   1.000 29.68374 ?  34  PRO   A N     1 
ATOM   263  C  CA    . PRO   A 1 35  ? 21.79900 22.08600  7.32500   1.000 27.69246 ?  34  PRO   A CA    1 
ATOM   264  C  C     . PRO   A 1 35  ? 21.51100 22.00900  8.82000   1.000 25.33913 ?  34  PRO   A C     1 
ATOM   265  O  O     . PRO   A 1 35  ? 21.01400 22.95400  9.44200   1.000 27.81470 ?  34  PRO   A O     1 
ATOM   266  C  CB    . PRO   A 1 35  ? 23.05000 22.92800  7.02900   1.000 28.31568 ?  34  PRO   A CB    1 
ATOM   267  C  CG    . PRO   A 1 35  ? 22.54900 24.26500  6.61000   1.000 29.53117 ?  34  PRO   A CG    1 
ATOM   268  C  CD    . PRO   A 1 35  ? 21.16300 24.09000  6.05100   1.000 31.10302 ?  34  PRO   A CD    1 
ATOM   269  N  N     . THR   A 1 36  ? 21.76600 20.83800  9.38600   1.000 24.65282 ?  35  THR   A N     1 
ATOM   270  C  CA    . THR   A 1 36  ? 21.39600 20.57600  10.76100  1.000 21.19108 ?  35  THR   A CA    1 
ATOM   271  C  C     . THR   A 1 36  ? 22.48300 21.07500  11.71500  1.000 19.97466 ?  35  THR   A C     1 
ATOM   272  O  O     . THR   A 1 36  ? 23.67300 20.89400  11.45400  1.000 20.82704 ?  35  THR   A O     1 
ATOM   273  C  CB    . THR   A 1 36  ? 21.19200 19.07800  10.96900  1.000 20.51229 ?  35  THR   A CB    1 
ATOM   274  O  OG1   . THR   A 1 36  ? 20.17200 18.61700  10.06100  1.000 24.92906 ?  35  THR   A OG1   1 
ATOM   275  C  CG2   . THR   A 1 36  ? 20.82700 18.74400  12.43400  1.000 23.19054 ?  35  THR   A CG2   1 
ATOM   276  N  N     . ILE   A 1 37  ? 22.05500 21.71000  12.81500  1.000 23.08308 ?  36  ILE   A N     1 
ATOM   277  C  CA    . ILE   A 1 37  ? 22.88500 21.86600  14.01400  1.000 21.21396 ?  36  ILE   A CA    1 
ATOM   278  C  C     . ILE   A 1 37  ? 22.72400 20.60400  14.86100  1.000 20.66637 ?  36  ILE   A C     1 
ATOM   279  O  O     . ILE   A 1 37  ? 23.66800 19.83600  15.03300  1.000 24.05077 ?  36  ILE   A O     1 
ATOM   280  C  CB    . ILE   A 1 37  ? 22.48100 23.11300  14.83300  1.000 22.94986 ?  36  ILE   A CB    1 
ATOM   281  C  CG1   . ILE   A 1 37  ? 22.34400 24.34400  13.94300  1.000 28.86432 ?  36  ILE   A CG1   1 
ATOM   282  C  CG2   . ILE   A 1 37  ? 23.42900 23.34400  16.04700  1.000 22.79242 ?  36  ILE   A CG2   1 
ATOM   283  C  CD1   . ILE   A 1 37  ? 23.60200 24.70300  13.26900  1.000 28.69855 ?  36  ILE   A CD1   1 
ATOM   284  N  N     . GLU   A 1 38  ? 21.52300 20.37700  15.39900  1.000 20.37813 ?  37  GLU   A N     1 
ATOM   285  C  CA    . GLU   A 1 38  ? 21.22000 19.14800  16.13400  1.000 22.77641 ?  37  GLU   A CA    1 
ATOM   286  C  C     . GLU   A 1 38  ? 19.72200 19.13800  16.37800  1.000 26.28309 ?  37  GLU   A C     1 
ATOM   287  O  O     . GLU   A 1 38  ? 19.18500 20.13500  16.87200  1.000 25.71724 ?  37  GLU   A O     1 
ATOM   288  C  CB    . GLU   A 1 38  ? 21.97400 19.08700  17.46600  1.000 25.02218 ?  37  GLU   A CB    1 
ATOM   289  C  CG    . GLU   A 1 38  ? 21.79300 17.79400  18.21800  1.000 30.08701 ?  37  GLU   A CG    1 
ATOM   290  C  CD    . GLU   A 1 38  ? 22.35200 17.86600  19.65300  1.000 37.82550 ?  37  GLU   A CD    1 
ATOM   291  O  OE1   . GLU   A 1 38  ? 23.58200 17.79000  19.80700  1.000 40.38037 ?  37  GLU   A OE1   1 
ATOM   292  O  OE2   . GLU   A 1 38  ? 21.55700 18.01300  20.61100  1.000 40.89139 -1 37  GLU   A OE2   1 
ATOM   293  N  N     . ASP   A 1 39  ? 19.02900 18.06900  16.02300  1.000 22.64793 ?  38  ASP   A N     1 
ATOM   294  C  CA    . ASP   A 1 39  ? 17.58900 18.00800  16.24100  1.000 22.42120 ?  38  ASP   A CA    1 
ATOM   295  C  C     . ASP   A 1 39  ? 17.24500 16.67700  16.87700  1.000 25.01215 ?  38  ASP   A C     1 
ATOM   296  O  O     . ASP   A 1 39  ? 17.91400 15.66100  16.64500  1.000 24.35936 ?  38  ASP   A O     1 
ATOM   297  C  CB    . ASP   A 1 39  ? 16.75500 18.20500  14.93900  1.000 23.66593 ?  38  ASP   A CB    1 
ATOM   298  C  CG    . ASP   A 1 39  ? 16.90900 19.60000  14.37400  1.000 31.14125 ?  38  ASP   A CG    1 
ATOM   299  O  OD1   . ASP   A 1 39  ? 16.59900 20.58700  15.08900  1.000 37.15957 ?  38  ASP   A OD1   1 
ATOM   300  O  OD2   . ASP   A 1 39  ? 17.33200 19.70300  13.22300  1.000 30.84894 -1 38  ASP   A OD2   1 
ATOM   301  N  N     . SER   A 1 40  ? 16.22900 16.71300  17.72800  1.000 21.49647 ?  39  SER   A N     1 
ATOM   302  C  CA    . SER   A 1 40  ? 15.74000 15.53000  18.41700  1.000 22.23391 ?  39  SER   A CA    1 
ATOM   303  C  C     . SER   A 1 40  ? 14.27900 15.33200  18.06900  1.000 22.81847 ?  39  SER   A C     1 
ATOM   304  O  O     . SER   A 1 40  ? 13.51500 16.31300  17.95600  1.000 25.13801 ?  39  SER   A O     1 
ATOM   305  C  CB    . SER   A 1 40  ? 15.85900 15.66800  19.93900  1.000 25.02319 ?  39  SER   A CB    1 
ATOM   306  O  OG    . SER   A 1 40  ? 17.21400 15.58300  20.32000  1.000 42.73693 ?  39  SER   A OG    1 
ATOM   307  N  N     . TYR   A 1 41  ? 13.88700 14.06600  17.93000  1.000 21.78698 ?  40  TYR   A N     1 
ATOM   308  C  CA    . TYR   A 1 41  ? 12.51200 13.70900  17.59300  1.000 21.71139 ?  40  TYR   A CA    1 
ATOM   309  C  C     . TYR   A 1 41  ? 12.09600 12.47500  18.38700  1.000 23.73268 ?  40  TYR   A C     1 
ATOM   310  O  O     . TYR   A 1 41  ? 12.92600 11.69000  18.85300  1.000 22.02123 ?  40  TYR   A O     1 
ATOM   311  C  CB    . TYR   A 1 41  ? 12.33300 13.40800  16.10800  1.000 21.86063 ?  40  TYR   A CB    1 
ATOM   312  C  CG    . TYR   A 1 41  ? 12.78500 14.49400  15.18100  1.000 22.70619 ?  40  TYR   A CG    1 
ATOM   313  C  CD1   . TYR   A 1 41  ? 14.11400 14.53600  14.72500  1.000 23.28592 ?  40  TYR   A CD1   1 
ATOM   314  C  CD2   . TYR   A 1 41  ? 11.90600 15.48100  14.77100  1.000 26.67134 ?  40  TYR   A CD2   1 
ATOM   315  C  CE1   . TYR   A 1 41  ? 14.52900 15.51600  13.84800  1.000 24.16434 ?  40  TYR   A CE1   1 
ATOM   316  C  CE2   . TYR   A 1 41  ? 12.32000 16.48100  13.91200  1.000 32.02750 ?  40  TYR   A CE2   1 
ATOM   317  C  CZ    . TYR   A 1 41  ? 13.62800 16.49800  13.46500  1.000 31.79532 ?  40  TYR   A CZ    1 
ATOM   318  O  OH    . TYR   A 1 41  ? 14.01400 17.48200  12.60000  1.000 33.80480 ?  40  TYR   A OH    1 
ATOM   319  N  N     A ARG   A 1 42  ? 10.78900 12.33300  18.55000  0.500 22.50997 ?  41  ARG   A N     1 
ATOM   320  N  N     B ARG   A 1 42  ? 10.79300 12.30300  18.51300  0.500 22.51554 ?  41  ARG   A N     1 
ATOM   321  C  CA    A ARG   A 1 42  ? 10.16500 11.19300  19.19700  0.500 22.98193 ?  41  ARG   A CA    1 
ATOM   322  C  CA    B ARG   A 1 42  ? 10.20700 11.17200  19.20500  0.500 22.97329 ?  41  ARG   A CA    1 
ATOM   323  C  C     A ARG   A 1 42  ? 9.08500  10.62900  18.29500  0.500 23.48239 ?  41  ARG   A C     1 
ATOM   324  C  C     B ARG   A 1 42  ? 9.04500  10.63200  18.38800  0.500 23.49519 ?  41  ARG   A C     1 
ATOM   325  O  O     A ARG   A 1 42  ? 8.35800  11.38200  17.63900  0.500 23.62144 ?  41  ARG   A O     1 
ATOM   326  O  O     B ARG   A 1 42  ? 8.24400  11.40500  17.85000  0.500 23.71580 ?  41  ARG   A O     1 
ATOM   327  C  CB    A ARG   A 1 42  ? 9.52400  11.57600  20.53200  0.500 23.13637 ?  41  ARG   A CB    1 
ATOM   328  C  CB    B ARG   A 1 42  ? 9.73800  11.57700  20.61200  0.500 23.17855 ?  41  ARG   A CB    1 
ATOM   329  C  CG    A ARG   A 1 42  ? 10.50800 11.73500  21.64900  0.500 27.11878 ?  41  ARG   A CG    1 
ATOM   330  C  CG    B ARG   A 1 42  ? 10.91500 11.96100  21.52500  0.500 26.80008 ?  41  ARG   A CG    1 
ATOM   331  C  CD    A ARG   A 1 42  ? 9.85500  12.51100  22.73000  0.500 26.20452 ?  41  ARG   A CD    1 
ATOM   332  C  CD    B ARG   A 1 42  ? 10.73100 11.39700  22.90400  0.500 27.94508 ?  41  ARG   A CD    1 
ATOM   333  N  NE    A ARG   A 1 42  ? 8.90300  11.73100  23.50600  0.500 29.53688 ?  41  ARG   A NE    1 
ATOM   334  N  NE    B ARG   A 1 42  ? 11.96500 11.21600  23.67100  0.500 30.21871 ?  41  ARG   A NE    1 
ATOM   335  C  CZ    A ARG   A 1 42  ? 9.25900  10.97900  24.53400  0.500 31.27153 ?  41  ARG   A CZ    1 
ATOM   336  C  CZ    B ARG   A 1 42  ? 11.97200 10.69900  24.89400  0.500 33.68012 ?  41  ARG   A CZ    1 
ATOM   337  N  NH1   A ARG   A 1 42  ? 10.53100 10.82400  24.86700  0.500 29.62806 ?  41  ARG   A NH1   1 
ATOM   338  N  NH1   B ARG   A 1 42  ? 10.85200 10.30900  25.48100  0.500 33.16283 ?  41  ARG   A NH1   1 
ATOM   339  N  NH2   A ARG   A 1 42  ? 8.32100  10.38300  25.25200  0.500 33.72601 ?  41  ARG   A NH2   1 
ATOM   340  N  NH2   B ARG   A 1 42  ? 13.12800 10.57100  25.54700  0.500 27.84135 ?  41  ARG   A NH2   1 
ATOM   341  N  N     . LYS   A 1 43  ? 8.97500  9.30900   18.27600  1.000 23.86983 ?  42  LYS   A N     1 
ATOM   342  C  CA    . LYS   A 1 43  ? 7.91200  8.66600   17.52300  1.000 24.58143 ?  42  LYS   A CA    1 
ATOM   343  C  C     . LYS   A 1 43  ? 7.62400  7.32400   18.14400  1.000 24.93709 ?  42  LYS   A C     1 
ATOM   344  O  O     . LYS   A 1 43  ? 8.55300  6.56700   18.42500  1.000 24.79614 ?  42  LYS   A O     1 
ATOM   345  C  CB    . LYS   A 1 43  ? 8.25700  8.45900   16.05100  1.000 26.00689 ?  42  LYS   A CB    1 
ATOM   346  C  CG    . LYS   A 1 43  ? 7.09500  7.85600   15.24000  1.000 27.70303 ?  42  LYS   A CG    1 
ATOM   347  C  CD    . LYS   A 1 43  ? 7.45300  7.71900   13.73800  1.000 27.37196 ?  42  LYS   A CD    1 
ATOM   348  C  CE    . LYS   A 1 43  ? 6.36500  6.97900   12.93800  1.000 36.46564 ?  42  LYS   A CE    1 
ATOM   349  N  NZ    . LYS   A 1 43  ? 5.04500  7.62900   13.03400  1.000 41.86427 ?  42  LYS   A NZ    1 
ATOM   350  N  N     . GLN   A 1 44  ? 6.33400  7.03600   18.35100  1.000 25.86721 ?  43  GLN   A N     1 
ATOM   351  C  CA    . GLN   A 1 44  ? 5.85700  5.73800   18.79400  1.000 26.75010 ?  43  GLN   A CA    1 
ATOM   352  C  C     . GLN   A 1 44  ? 5.66000  4.82400   17.58000  1.000 27.55247 ?  43  GLN   A C     1 
ATOM   353  O  O     . GLN   A 1 44  ? 5.08500  5.25400   16.57300  1.000 29.02363 ?  43  GLN   A O     1 
ATOM   354  C  CB    . GLN   A 1 44  ? 4.52800  5.93500   19.54600  1.000 32.25084 ?  43  GLN   A CB    1 
ATOM   355  C  CG    . GLN   A 1 44  ? 3.99100  4.72700   20.21000  1.000 39.33193 ?  43  GLN   A CG    1 
ATOM   356  C  CD    . GLN   A 1 44  ? 2.54500  4.93500   20.67100  1.000 29.99856 ?  43  GLN   A CD    1 
ATOM   357  O  OE1   . GLN   A 1 44  ? 2.10100  6.07000   20.96200  1.000 37.61688 ?  43  GLN   A OE1   1 
ATOM   358  N  NE2   . GLN   A 1 44  ? 1.81200  3.86800   20.69000  1.000 37.51199 ?  43  GLN   A NE2   1 
ATOM   359  N  N     . VAL   A 1 45  ? 6.13700  3.58300   17.66400  1.000 31.31915 ?  44  VAL   A N     1 
ATOM   360  C  CA    . VAL   A 1 45  ? 5.99600  2.60600   16.57400  1.000 29.89470 ?  44  VAL   A CA    1 
ATOM   361  C  C     . VAL   A 1 45  ? 5.70500  1.22100   17.14900  1.000 33.01532 ?  44  VAL   A C     1 
ATOM   362  O  O     . VAL   A 1 45  ? 5.78500  1.00000   18.35600  1.000 35.04826 ?  44  VAL   A O     1 
ATOM   363  C  CB    . VAL   A 1 45  ? 7.26600  2.55700   15.68300  1.000 26.74754 ?  44  VAL   A CB    1 
ATOM   364  C  CG1   . VAL   A 1 45  ? 7.47600  3.88200   14.99900  1.000 26.74933 ?  44  VAL   A CG1   1 
ATOM   365  C  CG2   . VAL   A 1 45  ? 8.50200  2.14300   16.51600  1.000 28.48994 ?  44  VAL   A CG2   1 
ATOM   366  N  N     . VAL   A 1 46  ? 5.37100  0.27000   16.26200  1.000 31.96577 ?  45  VAL   A N     1 
ATOM   367  C  CA    . VAL   A 1 46  ? 5.25000  -1.14800  16.61500  1.000 30.39590 ?  45  VAL   A CA    1 
ATOM   368  C  C     . VAL   A 1 46  ? 6.23000  -1.93800  15.76200  1.000 36.68767 ?  45  VAL   A C     1 
ATOM   369  O  O     . VAL   A 1 46  ? 6.18900  -1.85200  14.52700  1.000 36.51829 ?  45  VAL   A O     1 
ATOM   370  C  CB    . VAL   A 1 46  ? 3.82400  -1.68600  16.40300  1.000 31.61366 ?  45  VAL   A CB    1 
ATOM   371  C  CG1   . VAL   A 1 46  ? 3.72500  -3.13300  16.99800  1.000 35.24819 ?  45  VAL   A CG1   1 
ATOM   372  C  CG2   . VAL   A 1 46  ? 2.82800  -0.76800  17.04600  1.000 33.37165 ?  45  VAL   A CG2   1 
ATOM   373  N  N     . ILE   A 1 47  ? 7.10000  -2.70900  16.41000  1.000 34.07911 ?  46  ILE   A N     1 
ATOM   374  C  CA    . ILE   A 1 47  ? 8.13500  -3.47200  15.72000  1.000 37.98290 ?  46  ILE   A CA    1 
ATOM   375  C  C     . ILE   A 1 47  ? 8.07800  -4.91100  16.21200  1.000 40.68535 ?  46  ILE   A C     1 
ATOM   376  O  O     . ILE   A 1 47  ? 8.28200  -5.17500  17.40400  1.000 36.48839 ?  46  ILE   A O     1 
ATOM   377  C  CB    . ILE   A 1 47  ? 9.54000  -2.86000  15.93300  1.000 32.47734 ?  46  ILE   A CB    1 
ATOM   378  C  CG1   . ILE   A 1 47  ? 9.58700  -1.45400  15.33300  1.000 32.67361 ?  46  ILE   A CG1   1 
ATOM   379  C  CG2   . ILE   A 1 47  ? 10.67600 -3.76200  15.34500  1.000 33.38799 ?  46  ILE   A CG2   1 
ATOM   380  C  CD1   . ILE   A 1 47  ? 10.79600 -0.64200  15.82200  1.000 29.12437 ?  46  ILE   A CD1   1 
ATOM   381  N  N     . ASP   A 1 48  ? 7.80800  -5.84100  15.28800  1.000 44.46166 ?  47  ASP   A N     1 
ATOM   382  C  CA    . ASP   A 1 48  ? 7.68000  -7.26500  15.60500  1.000 46.21834 ?  47  ASP   A CA    1 
ATOM   383  C  C     . ASP   A 1 48  ? 6.72000  -7.47700  16.77400  1.000 42.78576 ?  47  ASP   A C     1 
ATOM   384  O  O     . ASP   A 1 48  ? 7.06700  -8.09400  17.78900  1.000 49.54886 ?  47  ASP   A O     1 
ATOM   385  C  CB    . ASP   A 1 48  ? 9.03400  -7.89800  15.93200  1.000 37.82983 ?  47  ASP   A CB    1 
ATOM   386  C  CG    . ASP   A 1 48  ? 10.07900 -7.68400  14.86600  1.000 41.80345 ?  47  ASP   A CG    1 
ATOM   387  O  OD1   . ASP   A 1 48  ? 9.73200  -7.42300  13.68500  1.000 44.64573 ?  47  ASP   A OD1   1 
ATOM   388  O  OD2   . ASP   A 1 48  ? 11.28300 -7.81800  15.22800  1.000 44.79038 -1 47  ASP   A OD2   1 
ATOM   389  N  N     . GLY   A 1 49  ? 5.52100  -6.91100  16.64900  1.000 48.77311 ?  48  GLY   A N     1 
ATOM   390  C  CA    . GLY   A 1 49  ? 4.49000  -7.03300  17.66600  1.000 51.73865 ?  48  GLY   A CA    1 
ATOM   391  C  C     . GLY   A 1 49  ? 4.62300  -6.12200  18.87500  1.000 50.33224 ?  48  GLY   A C     1 
ATOM   392  O  O     . GLY   A 1 49  ? 3.67300  -6.02800  19.66400  1.000 50.01139 ?  48  GLY   A O     1 
ATOM   393  N  N     . GLU   A 1 50  ? 5.75000  -5.43300  19.05300  1.000 45.52218 ?  49  GLU   A N     1 
ATOM   394  C  CA    . GLU   A 1 50  ? 6.04900  -4.77100  20.31700  1.000 40.23461 ?  49  GLU   A CA    1 
ATOM   395  C  C     . GLU   A 1 50  ? 6.06300  -3.25900  20.15400  1.000 42.69453 ?  49  GLU   A C     1 
ATOM   396  O  O     . GLU   A 1 50  ? 6.85100  -2.72700  19.36800  1.000 44.94279 ?  49  GLU   A O     1 
ATOM   397  C  CB    . GLU   A 1 50  ? 7.38100  -5.25900  20.86600  1.000 43.40796 ?  49  GLU   A CB    1 
ATOM   398  C  CG    . GLU   A 1 50  ? 7.77900  -4.59100  22.14100  1.000 46.78598 ?  49  GLU   A CG    1 
ATOM   399  C  CD    . GLU   A 1 50  ? 8.57200  -5.52600  23.02300  1.000 50.43386 ?  49  GLU   A CD    1 
ATOM   400  O  OE1   . GLU   A 1 50  ? 8.09500  -6.66800  23.23300  1.000 62.07116 ?  49  GLU   A OE1   1 
ATOM   401  O  OE2   . GLU   A 1 50  ? 9.66900  -5.13000  23.48600  1.000 55.57193 -1 49  GLU   A OE2   1 
ATOM   402  N  N     . THR   A 1 51  ? 5.20400  -2.57600  20.91100  1.000 43.49645 ?  50  THR   A N     1 
ATOM   403  C  CA    . THR   A 1 51  ? 5.14600  -1.11800  20.88400  1.000 42.10878 ?  50  THR   A CA    1 
ATOM   404  C  C     . THR   A 1 51  ? 6.39100  -0.53600  21.54300  1.000 37.50610 ?  50  THR   A C     1 
ATOM   405  O  O     . THR   A 1 51  ? 6.91900  -1.09800  22.50300  1.000 37.58073 ?  50  THR   A O     1 
ATOM   406  C  CB    . THR   A 1 51  ? 3.87000  -0.64400  21.58800  1.000 39.32396 ?  50  THR   A CB    1 
ATOM   407  O  OG1   . THR   A 1 51  ? 2.75100  -1.27400  20.96500  1.000 53.31976 ?  50  THR   A OG1   1 
ATOM   408  C  CG2   . THR   A 1 51  ? 3.68200  0.86700   21.48800  1.000 41.00029 ?  50  THR   A CG2   1 
ATOM   409  N  N     . CYS   A 1 52  ? 6.89400  0.56800   20.99400  1.000 33.63826 ?  51  CYS   A N     1 
ATOM   410  C  CA    . CYS   A 1 52  ? 8.08500  1.18700   21.56600  1.000 35.93637 ?  51  CYS   A CA    1 
ATOM   411  C  C     . CYS   A 1 52  ? 8.20400  2.61900   21.07300  1.000 29.05066 ?  51  CYS   A C     1 
ATOM   412  O  O     . CYS   A 1 52  ? 7.51000  3.05200   20.15000  1.000 32.15137 ?  51  CYS   A O     1 
ATOM   413  C  CB    . CYS   A 1 52  ? 9.35600  0.39400   21.25300  1.000 38.11201 ?  51  CYS   A CB    1 
ATOM   414  S  SG    . CYS   A 1 52  ? 9.79500  0.19600   19.51800  1.000 36.82765 ?  51  CYS   A SG    1 
ATOM   415  N  N     . LEU   A 1 53  ? 9.05900  3.36400   21.75100  1.000 27.04294 ?  52  LEU   A N     1 
ATOM   416  C  CA    . LEU   A 1 53  ? 9.25900  4.78200   21.49200  1.000 25.02926 ?  52  LEU   A CA    1 
ATOM   417  C  C     . LEU   A 1 53  ? 10.64700 4.96300   20.89000  1.000 25.08777 ?  52  LEU   A C     1 
ATOM   418  O  O     . LEU   A 1 53  ? 11.63800 4.51100   21.47400  1.000 25.68996 ?  52  LEU   A O     1 
ATOM   419  C  CB    . LEU   A 1 53  ? 9.12600  5.56900   22.80100  1.000 30.34188 ?  52  LEU   A CB    1 
ATOM   420  C  CG    . LEU   A 1 53  ? 9.04700  7.09500   22.83400  1.000 32.29385 ?  52  LEU   A CG    1 
ATOM   421  C  CD1   . LEU   A 1 53  ? 8.04900  7.68800   21.82900  1.000 26.98366 ?  52  LEU   A CD1   1 
ATOM   422  C  CD2   . LEU   A 1 53  ? 8.61800  7.42600   24.28300  1.000 35.36491 ?  52  LEU   A CD2   1 
ATOM   423  N  N     . LEU   A 1 54  ? 10.71900 5.59700   19.72400  1.000 24.23921 ?  53  LEU   A N     1 
ATOM   424  C  CA    . LEU   A 1 54  ? 12.01200 5.95100   19.13900  1.000 23.69668 ?  53  LEU   A CA    1 
ATOM   425  C  C     . LEU   A 1 54  ? 12.36200 7.36500   19.54900  1.000 24.14751 ?  53  LEU   A C     1 
ATOM   426  O  O     . LEU   A 1 54  ? 11.58100 8.28900   19.32500  1.000 24.42670 ?  53  LEU   A O     1 
ATOM   427  C  CB    . LEU   A 1 54  ? 11.99800 5.85500   17.61100  1.000 23.78787 ?  53  LEU   A CB    1 
ATOM   428  C  CG    . LEU   A 1 54  ? 11.50200 4.52200   17.05200  1.000 24.37318 ?  53  LEU   A CG    1 
ATOM   429  C  CD1   . LEU   A 1 54  ? 11.55300 4.54100   15.51800  1.000 29.04958 ?  53  LEU   A CD1   1 
ATOM   430  C  CD2   . LEU   A 1 54  ? 12.20800 3.33800   17.65500  1.000 25.07062 ?  53  LEU   A CD2   1 
ATOM   431  N  N     . ASP   A 1 55  ? 13.51400 7.52500   20.16500  1.000 22.78812 ?  54  ASP   A N     1 
ATOM   432  C  CA    . ASP   A 1 55  ? 14.07400 8.83100   20.50900  1.000 22.41412 ?  54  ASP   A CA    1 
ATOM   433  C  C     . ASP   A 1 55  ? 15.23500 9.01600   19.54200  1.000 23.45325 ?  54  ASP   A C     1 
ATOM   434  O  O     . ASP   A 1 55  ? 16.25200 8.31700   19.65700  1.000 25.28390 ?  54  ASP   A O     1 
ATOM   435  C  CB    . ASP   A 1 55  ? 14.51000 8.80800   21.97100  1.000 29.64724 ?  54  ASP   A CB    1 
ATOM   436  C  CG    . ASP   A 1 55  ? 14.87900 10.17100  22.52600  1.000 41.38232 ?  54  ASP   A CG    1 
ATOM   437  O  OD1   . ASP   A 1 55  ? 14.90800 11.18500  21.77900  1.000 45.09307 ?  54  ASP   A OD1   1 
ATOM   438  O  OD2   . ASP   A 1 55  ? 15.13100 10.21500  23.75200  1.000 46.88213 -1 54  ASP   A OD2   1 
ATOM   439  N  N     . ILE   A 1 56  ? 15.07900 9.90200   18.55600  1.000 21.82055 ?  55  ILE   A N     1 
ATOM   440  C  CA    . ILE   A 1 56  ? 16.02600 9.98000   17.44600  1.000 21.60128 ?  55  ILE   A CA    1 
ATOM   441  C  C     . ILE   A 1 56  ? 16.81400 11.28000  17.53600  1.000 21.77547 ?  55  ILE   A C     1 
ATOM   442  O  O     . ILE   A 1 56  ? 16.23600 12.37300  17.63600  1.000 25.59127 ?  55  ILE   A O     1 
ATOM   443  C  CB    . ILE   A 1 56  ? 15.29400 9.85400   16.10100  1.000 21.89154 ?  55  ILE   A CB    1 
ATOM   444  C  CG1   . ILE   A 1 56  ? 14.53200 8.52500   16.08700  1.000 22.51168 ?  55  ILE   A CG1   1 
ATOM   445  C  CG2   . ILE   A 1 56  ? 16.26800 9.92100   14.90700  1.000 21.74094 ?  55  ILE   A CG2   1 
ATOM   446  C  CD1   . ILE   A 1 56  ? 13.55600 8.51300   15.06300  1.000 27.94504 ?  55  ILE   A CD1   1 
ATOM   447  N  N     . LEU   A 1 57  ? 18.13500 11.16000  17.50500  1.000 21.30444 ?  56  LEU   A N     1 
ATOM   448  C  CA    . LEU   A 1 57  ? 19.02100 12.31500  17.43800  1.000 21.42149 ?  56  LEU   A CA    1 
ATOM   449  C  C     . LEU   A 1 57  ? 19.54100 12.45700  16.01500  1.000 21.55140 ?  56  LEU   A C     1 
ATOM   450  O  O     . LEU   A 1 57  ? 20.24800 11.58000  15.51100  1.000 21.42300 ?  56  LEU   A O     1 
ATOM   451  C  CB    . LEU   A 1 57  ? 20.18500 12.14800  18.41100  1.000 21.75996 ?  56  LEU   A CB    1 
ATOM   452  C  CG    . LEU   A 1 57  ? 21.09200 13.37900  18.46900  1.000 23.94209 ?  56  LEU   A CG    1 
ATOM   453  C  CD1   . LEU   A 1 57  ? 20.36200 14.57400  19.05500  1.000 23.47581 ?  56  LEU   A CD1   1 
ATOM   454  C  CD2   . LEU   A 1 57  ? 22.34700 13.11500  19.31700  1.000 25.54124 ?  56  LEU   A CD2   1 
ATOM   455  N  N     . ASP   A 1 58  ? 19.20700 13.57300  15.37600  1.000 20.61696 ?  57  ASP   A N     1 
ATOM   456  C  CA    . ASP   A 1 58  ? 19.63200 13.88400  14.02200  1.000 22.49378 ?  57  ASP   A CA    1 
ATOM   457  C  C     . ASP   A 1 58  ? 20.83500 14.82300  14.12200  1.000 23.16892 ?  57  ASP   A C     1 
ATOM   458  O  O     . ASP   A 1 58  ? 20.70400 15.95100  14.60600  1.000 23.98559 ?  57  ASP   A O     1 
ATOM   459  C  CB    . ASP   A 1 58  ? 18.45000 14.51900  13.28200  1.000 23.80236 ?  57  ASP   A CB    1 
ATOM   460  C  CG    . ASP   A 1 58  ? 18.76400 14.85600  11.83600  1.000 26.26984 ?  57  ASP   A CG    1 
ATOM   461  O  OD1   . ASP   A 1 58  ? 19.71000 14.25500  11.29800  1.000 28.12624 ?  57  ASP   A OD1   1 
ATOM   462  O  OD2   . ASP   A 1 58  ? 18.06000 15.72100  11.22800  1.000 25.84159 -1 57  ASP   A OD2   1 
ATOM   463  N  N     . THR   A 1 59  ? 22.02000 14.34200  13.74000  1.000 21.23210 ?  58  THR   A N     1 
ATOM   464  C  CA    . THR   A 1 59  ? 23.24900 15.09100  13.98200  1.000 20.74368 ?  58  THR   A CA    1 
ATOM   465  C  C     . THR   A 1 59  ? 23.70800 15.86300  12.74900  1.000 22.22308 ?  58  THR   A C     1 
ATOM   466  O  O     . THR   A 1 59  ? 23.22500 15.65800  11.63900  1.000 24.58843 ?  58  THR   A O     1 
ATOM   467  C  CB    . THR   A 1 59  ? 24.38800 14.15800  14.44100  1.000 21.77197 ?  58  THR   A CB    1 
ATOM   468  O  OG1   . THR   A 1 59  ? 24.72200 13.25700  13.38000  1.000 20.82564 ?  58  THR   A OG1   1 
ATOM   469  C  CG2   . THR   A 1 59  ? 23.94300 13.37700  15.65300  1.000 24.54957 ?  58  THR   A CG2   1 
ATOM   470  N  N     . ALA   A 1 60  ? 24.70400 16.72800  12.96700  1.000 21.79068 ?  59  ALA   A N     1 
ATOM   471  C  CA    . ALA   A 1 60  ? 25.32500 17.49100  11.89100  1.000 22.53053 ?  59  ALA   A CA    1 
ATOM   472  C  C     . ALA   A 1 60  ? 26.43900 16.71100  11.22200  1.000 24.18474 ?  59  ALA   A C     1 
ATOM   473  O  O     . ALA   A 1 60  ? 27.25400 16.06600  11.89200  1.000 22.82327 ?  59  ALA   A O     1 
ATOM   474  C  CB    . ALA   A 1 60  ? 25.90400 18.80200  12.43300  1.000 22.69860 ?  59  ALA   A CB    1 
ATOM   475  N  N     . GLY   A 1 61  ? 26.47400 16.78000  9.90200   1.000 22.97609 ?  60  GLY   A N     1 
ATOM   476  C  CA    . GLY   A 1 61  ? 27.54000 16.16200  9.13600   1.000 25.37248 ?  60  GLY   A CA    1 
ATOM   477  C  C     . GLY   A 1 61  ? 28.84300 16.94300  9.10500   1.000 35.00717 ?  60  GLY   A C     1 
ATOM   478  O  O     . GLY   A 1 61  ? 29.85500 16.39200  8.65300   1.000 32.56870 ?  60  GLY   A O     1 
ATOM   479  N  N     . GLN   A 1 62  ? 28.84000 18.20300  9.57300   1.000 28.87108 ?  61  GLN   A N     1 
ATOM   480  C  CA    . GLN   A 1 62  ? 29.97700 19.11300  9.35100   1.000 34.14578 ?  61  GLN   A CA    1 
ATOM   481  C  C     . GLN   A 1 62  ? 31.26500 18.50600  9.88000   1.000 30.53909 ?  61  GLN   A C     1 
ATOM   482  O  O     . GLN   A 1 62  ? 31.37900 18.22700  11.07600  1.000 30.35791 ?  61  GLN   A O     1 
ATOM   483  C  CB    . GLN   A 1 62  ? 29.75600 20.46900  10.03700  1.000 34.60861 ?  61  GLN   A CB    1 
ATOM   484  C  CG    . GLN   A 1 62  ? 28.46800 21.21000  9.70200   1.000 33.69187 ?  61  GLN   A CG    1 
ATOM   485  C  CD    . GLN   A 1 62  ? 28.40600 21.63900  8.25400   1.000 34.21122 ?  61  GLN   A CD    1 
ATOM   486  O  OE1   . GLN   A 1 62  ? 29.42400 22.01400  7.64000   1.000 38.35462 ?  61  GLN   A OE1   1 
ATOM   487  N  NE2   . GLN   A 1 62  ? 27.23300 21.52900  7.67500   1.000 28.77677 ?  61  GLN   A NE2   1 
ATOM   488  N  N     . GLU   A 1 63  ? 32.24100 18.30100  8.99200   1.000 33.53241 ?  62  GLU   A N     1 
ATOM   489  C  CA    . GLU   A 1 63  ? 33.50400 17.71800  9.44200   1.000 36.60119 ?  62  GLU   A CA    1 
ATOM   490  C  C     . GLU   A 1 63  ? 34.23900 18.64800  10.39300  1.000 33.07772 ?  62  GLU   A C     1 
ATOM   491  O  O     . GLU   A 1 63  ? 35.02100 18.17900  11.22700  1.000 36.81013 ?  62  GLU   A O     1 
ATOM   492  C  CB    . GLU   A 1 63  ? 34.40100 17.35700  8.24800   1.000 41.26799 ?  62  GLU   A CB    1 
ATOM   493  C  CG    . GLU   A 1 63  ? 34.24400 15.89300  7.80200   1.000 45.22539 ?  62  GLU   A CG    1 
ATOM   494  C  CD    . GLU   A 1 63  ? 34.92000 15.57400  6.45800   1.000 53.35081 ?  62  GLU   A CD    1 
ATOM   495  O  OE1   . GLU   A 1 63  ? 34.99000 16.46400  5.56800   1.000 55.67445 ?  62  GLU   A OE1   1 
ATOM   496  O  OE2   . GLU   A 1 63  ? 35.37600 14.41800  6.29400   1.000 55.34690 ?  62  GLU   A OE2   1 
ATOM   497  N  N     . GLU   A 1 64  ? 33.99600 19.96200  10.31200  1.000 28.91780 ?  63  GLU   A N     1 
ATOM   498  C  CA    . GLU   A 1 64  ? 34.76800 20.84900  11.18500  1.000 34.62862 ?  63  GLU   A CA    1 
ATOM   499  C  C     . GLU   A 1 64  ? 34.42100 20.67800  12.65700  1.000 35.21420 ?  63  GLU   A C     1 
ATOM   500  O  O     . GLU   A 1 64  ? 35.20300 21.12300  13.50700  1.000 33.04805 ?  63  GLU   A O     1 
ATOM   501  C  CB    . GLU   A 1 64  ? 34.60800 22.31800  10.76300  1.000 38.79475 ?  63  GLU   A CB    1 
ATOM   502  C  CG    . GLU   A 1 64  ? 33.19000 22.78100  10.63000  1.000 38.51318 ?  63  GLU   A CG    1 
ATOM   503  C  CD    . GLU   A 1 64  ? 33.05500 24.06100  9.80700   1.000 44.05531 ?  63  GLU   A CD    1 
ATOM   504  O  OE1   . GLU   A 1 64  ? 33.23600 25.16100  10.38000  1.000 45.41389 ?  63  GLU   A OE1   1 
ATOM   505  O  OE2   . GLU   A 1 64  ? 32.74300 23.97100  8.59200   1.000 47.89266 -1 63  GLU   A OE2   1 
ATOM   506  N  N     . TYR   A 1 65  ? 33.29200 20.02600  12.99000  1.000 32.59156 ?  64  TYR   A N     1 
ATOM   507  C  CA    . TYR   A 1 65  ? 32.92100 19.74700  14.37500  1.000 29.96690 ?  64  TYR   A CA    1 
ATOM   508  C  C     . TYR   A 1 65  ? 33.05300 18.27000  14.71400  1.000 27.83570 ?  64  TYR   A C     1 
ATOM   509  O  O     . TYR   A 1 65  ? 32.40400 17.78800  15.65200  1.000 29.61095 ?  64  TYR   A O     1 
ATOM   510  C  CB    . TYR   A 1 65  ? 31.49300 20.24700  14.65900  1.000 29.19508 ?  64  TYR   A CB    1 
ATOM   511  C  CG    . TYR   A 1 65  ? 31.36400 21.71200  14.32700  1.000 28.39823 ?  64  TYR   A CG    1 
ATOM   512  C  CD1   . TYR   A 1 65  ? 31.98900 22.67400  15.11600  1.000 25.80027 ?  64  TYR   A CD1   1 
ATOM   513  C  CD2   . TYR   A 1 65  ? 30.65200 22.13200  13.21300  1.000 26.13066 ?  64  TYR   A CD2   1 
ATOM   514  C  CE1   . TYR   A 1 65  ? 31.92300 24.01300  14.80500  1.000 30.87876 ?  64  TYR   A CE1   1 
ATOM   515  C  CE2   . TYR   A 1 65  ? 30.57100 23.48100  12.88900  1.000 26.83474 ?  64  TYR   A CE2   1 
ATOM   516  C  CZ    . TYR   A 1 65  ? 31.20000 24.41100  13.70000  1.000 25.65321 ?  64  TYR   A CZ    1 
ATOM   517  O  OH    . TYR   A 1 65  ? 31.12200 25.73600  13.38900  1.000 22.18798 ?  64  TYR   A OH    1 
ATOM   518  N  N     . SER   A 1 66  ? 33.93300 17.56100  13.99700  1.000 30.28664 ?  65  SER   A N     1 
ATOM   519  C  CA    . SER   A 1 66  ? 34.12000 16.13000  14.21000  1.000 35.90370 ?  65  SER   A CA    1 
ATOM   520  C  C     . SER   A 1 66  ? 34.64000 15.82300  15.60200  1.000 34.20792 ?  65  SER   A C     1 
ATOM   521  O  O     . SER   A 1 66  ? 34.50400 14.68500  16.06100  1.000 41.46517 ?  65  SER   A O     1 
ATOM   522  C  CB    . SER   A 1 66  ? 35.07300 15.55400  13.15800  1.000 35.64506 ?  65  SER   A CB    1 
ATOM   523  O  OG    . SER   A 1 66  ? 36.32800 16.21400  13.19200  1.000 36.97070 ?  65  SER   A OG    1 
ATOM   524  N  N     . ALA   A 1 67  ? 35.19200 16.81400  16.30300  1.000 32.66186 ?  66  ALA   A N     1 
ATOM   525  C  CA    . ALA   A 1 67  ? 35.68900 16.60300  17.65800  1.000 35.39114 ?  66  ALA   A CA    1 
ATOM   526  C  C     . ALA   A 1 67  ? 34.62100 16.75500  18.73900  1.000 36.43543 ?  66  ALA   A C     1 
ATOM   527  O  O     . ALA   A 1 67  ? 34.94400 16.59800  19.91600  1.000 37.94377 ?  66  ALA   A O     1 
ATOM   528  C  CB    . ALA   A 1 67  ? 36.84900 17.56800  17.94800  1.000 38.71255 ?  66  ALA   A CB    1 
ATOM   529  N  N     . MET   A 1 68  ? 33.36100 17.04200  18.37800  1.000 35.93789 ?  67  MET   A N     1 
ATOM   530  C  CA    . MET   A 1 68  ? 32.26800 17.24000  19.32700  1.000 36.40401 ?  67  MET   A CA    1 
ATOM   531  C  C     . MET   A 1 68  ? 31.21900 16.13000  19.27600  1.000 35.22010 ?  67  MET   A C     1 
ATOM   532  O  O     . MET   A 1 68  ? 30.07400 16.35700  19.68400  1.000 36.03723 ?  67  MET   A O     1 
ATOM   533  C  CB    . MET   A 1 68  ? 31.55400 18.57300  19.08100  1.000 40.43534 ?  67  MET   A CB    1 
ATOM   534  C  CG    . MET   A 1 68  ? 32.17300 19.77000  19.76400  1.000 47.50526 ?  67  MET   A CG    1 
ATOM   535  S  SD    . MET   A 1 68  ? 33.11900 20.64700  18.53400  1.000 63.72329 ?  67  MET   A SD    1 
ATOM   536  C  CE    . MET   A 1 68  ? 33.34600 22.21800  19.36700  1.000 46.56645 ?  67  MET   A CE    1 
ATOM   537  N  N     . ARG   A 1 69  ? 31.56100 14.96400  18.73800  1.000 32.95337 ?  68  ARG   A N     1 
ATOM   538  C  CA    . ARG   A 1 69  ? 30.61600 13.85500  18.62600  1.000 30.09135 ?  68  ARG   A CA    1 
ATOM   539  C  C     . ARG   A 1 69  ? 30.63300 12.90900  19.81800  1.000 30.72397 ?  68  ARG   A C     1 
ATOM   540  O  O     . ARG   A 1 69  ? 29.72500 12.07700  19.93400  1.000 28.43480 ?  68  ARG   A O     1 
ATOM   541  C  CB    . ARG   A 1 69  ? 30.91300 13.04500  17.37000  1.000 27.29525 ?  68  ARG   A CB    1 
ATOM   542  C  CG    . ARG   A 1 69  ? 30.83200 13.85800  16.09100  1.000 34.55056 ?  68  ARG   A CG    1 
ATOM   543  C  CD    . ARG   A 1 69  ? 31.18100 13.04200  14.86300  1.000 31.71347 ?  68  ARG   A CD    1 
ATOM   544  N  NE    . ARG   A 1 69  ? 31.20300 13.85400  13.64500  1.000 30.98309 ?  68  ARG   A NE    1 
ATOM   545  C  CZ    . ARG   A 1 69  ? 32.03900 13.66300  12.63600  1.000 32.37693 ?  68  ARG   A CZ    1 
ATOM   546  N  NH1   . ARG   A 1 69  ? 32.98700 12.73300  12.68100  1.000 31.54051 ?  68  ARG   A NH1   1 
ATOM   547  N  NH2   . ARG   A 1 69  ? 31.95800 14.45600  11.56700  1.000 37.15142 ?  68  ARG   A NH2   1 
ATOM   548  N  N     . ASP   A 1 70  ? 31.63100 12.99900  20.70000  1.000 32.07295 ?  69  ASP   A N     1 
ATOM   549  C  CA    . ASP   A 1 70  ? 31.83500 11.92000  21.66200  1.000 32.57520 ?  69  ASP   A CA    1 
ATOM   550  C  C     . ASP   A 1 70  ? 30.65000 11.77400  22.61200  1.000 29.72580 ?  69  ASP   A C     1 
ATOM   551  O  O     . ASP   A 1 70  ? 30.25600 10.65100  22.93300  1.000 30.74694 ?  69  ASP   A O     1 
ATOM   552  C  CB    . ASP   A 1 70  ? 33.13300 12.12300  22.45300  1.000 31.83955 ?  69  ASP   A CB    1 
ATOM   553  C  CG    . ASP   A 1 70  ? 34.38400 11.97500  21.58700  1.000 39.78136 ?  69  ASP   A CG    1 
ATOM   554  O  OD1   . ASP   A 1 70  ? 34.26700 12.05800  20.33600  1.000 35.40716 ?  69  ASP   A OD1   1 
ATOM   555  O  OD2   . ASP   A 1 70  ? 35.48900 11.77300  22.16700  1.000 40.57286 -1 69  ASP   A OD2   1 
ATOM   556  N  N     . GLN   A 1 71  ? 30.08600 12.88500  23.11100  1.000 27.72020 ?  70  GLN   A N     1 
ATOM   557  C  CA    . GLN   A 1 71  ? 29.04100 12.73100  24.11400  1.000 33.59637 ?  70  GLN   A CA    1 
ATOM   558  C  C     . GLN   A 1 71  ? 27.79500 12.10000  23.51300  1.000 31.26410 ?  70  GLN   A C     1 
ATOM   559  O  O     . GLN   A 1 71  ? 27.19900 11.19800  24.11400  1.000 28.49017 ?  70  GLN   A O     1 
ATOM   560  C  CB    . GLN   A 1 71  ? 28.68500 14.05800  24.77000  1.000 34.58539 ?  70  GLN   A CB    1 
ATOM   561  C  CG    . GLN   A 1 71  ? 27.69700 13.83900  25.93300  1.000 33.62900 ?  70  GLN   A CG    1 
ATOM   562  C  CD    . GLN   A 1 71  ? 28.20000 12.82300  26.96700  1.000 44.83134 ?  70  GLN   A CD    1 
ATOM   563  O  OE1   . GLN   A 1 71  ? 29.30100 12.96900  27.52100  1.000 49.30498 ?  70  GLN   A OE1   1 
ATOM   564  N  NE2   . GLN   A 1 71  ? 27.39800 11.79100  27.23200  1.000 42.58350 ?  70  GLN   A NE2   1 
ATOM   565  N  N     . TYR   A 1 72  ? 27.40900 12.50400  22.30600  1.000 29.23916 ?  71  TYR   A N     1 
ATOM   566  C  CA    . TYR   A 1 72  ? 26.18600 11.89200  21.80600  1.000 26.21736 ?  71  TYR   A CA    1 
ATOM   567  C  C     . TYR   A 1 72  ? 26.43500 10.44200  21.41400  1.000 27.08794 ?  71  TYR   A C     1 
ATOM   568  O  O     . TYR   A 1 72  ? 25.51900 9.62000   21.49500  1.000 26.91195 ?  71  TYR   A O     1 
ATOM   569  C  CB    . TYR   A 1 72  ? 25.57000 12.73400  20.67400  1.000 28.01310 ?  71  TYR   A CB    1 
ATOM   570  C  CG    . TYR   A 1 72  ? 26.20400 12.75200  19.30400  1.000 24.78651 ?  71  TYR   A CG    1 
ATOM   571  C  CD1   . TYR   A 1 72  ? 26.38000 11.58200  18.56500  1.000 26.25866 ?  71  TYR   A CD1   1 
ATOM   572  C  CD2   . TYR   A 1 72  ? 26.54800 13.96200  18.68500  1.000 30.53374 ?  71  TYR   A CD2   1 
ATOM   573  C  CE1   . TYR   A 1 72  ? 26.91100 11.60400  17.28000  1.000 32.11309 ?  71  TYR   A CE1   1 
ATOM   574  C  CE2   . TYR   A 1 72  ? 27.08700 13.99200  17.36600  1.000 26.70087 ?  71  TYR   A CE2   1 
ATOM   575  C  CZ    . TYR   A 1 72  ? 27.27200 12.81300  16.67800  1.000 28.06836 ?  71  TYR   A CZ    1 
ATOM   576  O  OH    . TYR   A 1 72  ? 27.80200 12.78700  15.39000  1.000 33.93930 ?  71  TYR   A OH    1 
ATOM   577  N  N     . MET   A 1 73  ? 27.67900 10.09500  21.06300  1.000 26.32772 ?  72  MET   A N     1 
ATOM   578  C  CA    . MET   A 1 73  ? 28.01000 8.69200   20.82200  1.000 26.30766 ?  72  MET   A CA    1 
ATOM   579  C  C     . MET   A 1 73  ? 27.96600 7.85600   22.10500  1.000 28.68390 ?  72  MET   A C     1 
ATOM   580  O  O     . MET   A 1 73  ? 27.43100 6.74700   22.09600  1.000 27.66336 ?  72  MET   A O     1 
ATOM   581  C  CB    . MET   A 1 73  ? 29.36900 8.59500   20.13700  1.000 29.83345 ?  72  MET   A CB    1 
ATOM   582  C  CG    . MET   A 1 73  ? 29.32500 9.15800   18.71000  1.000 28.48264 ?  72  MET   A CG    1 
ATOM   583  S  SD    . MET   A 1 73  ? 30.90700 8.99300   17.86000  1.000 29.62525 ?  72  MET   A SD    1 
ATOM   584  C  CE    . MET   A 1 73  ? 30.42000 9.47700   16.19300  1.000 30.75159 ?  72  MET   A CE    1 
ATOM   585  N  N     . ARG   A 1 74  ? 28.51600 8.36000   23.21400  1.000 26.45484 ?  73  ARG   A N     1 
ATOM   586  C  CA    . ARG   A 1 74  ? 28.35600 7.66600   24.49700  1.000 30.98935 ?  73  ARG   A CA    1 
ATOM   587  C  C     . ARG   A 1 74  ? 26.88000 7.44800   24.82200  1.000 29.51007 ?  73  ARG   A C     1 
ATOM   588  O  O     . ARG   A 1 74  ? 26.48100 6.34800   25.20600  1.000 28.95071 ?  73  ARG   A O     1 
ATOM   589  C  CB    . ARG   A 1 74  ? 29.04000 8.45000   25.62700  1.000 33.88076 ?  73  ARG   A CB    1 
ATOM   590  C  CG    . ARG   A 1 74  ? 30.56400 8.39500   25.61000  1.000 41.11913 ?  73  ARG   A CG    1 
ATOM   591  C  CD    . ARG   A 1 74  ? 31.18200 9.21400   26.78100  1.000 35.91134 ?  73  ARG   A CD    1 
ATOM   592  N  NE    . ARG   A 1 74  ? 32.49600 9.70100   26.39800  1.000 48.82162 ?  73  ARG   A NE    1 
ATOM   593  C  CZ    . ARG   A 1 74  ? 32.77600 10.96100  26.10100  1.000 41.54288 ?  73  ARG   A CZ    1 
ATOM   594  N  NH1   . ARG   A 1 74  ? 31.88200 11.92500  26.26300  1.000 42.92287 ?  73  ARG   A NH1   1 
ATOM   595  N  NH2   . ARG   A 1 74  ? 33.99200 11.26600  25.65200  1.000 51.63717 ?  73  ARG   A NH2   1 
ATOM   596  N  N     . THR   A 1 75  ? 26.04800 8.48000   24.64000  1.000 28.08117 ?  74  THR   A N     1 
ATOM   597  C  CA    . THR   A 1 75  ? 24.65400 8.38900   25.06800  1.000 28.94805 ?  74  THR   A CA    1 
ATOM   598  C  C     . THR   A 1 75  ? 23.82200 7.49500   24.14600  1.000 31.92714 ?  74  THR   A C     1 
ATOM   599  O  O     . THR   A 1 75  ? 22.89200 6.83200   24.60900  1.000 32.59167 ?  74  THR   A O     1 
ATOM   600  C  CB    . THR   A 1 75  ? 24.02900 9.77900   25.13300  1.000 35.73476 ?  74  THR   A CB    1 
ATOM   601  O  OG1   . THR   A 1 75  ? 24.82000 10.63100  25.97300  1.000 37.29982 ?  74  THR   A OG1   1 
ATOM   602  C  CG2   . THR   A 1 75  ? 22.61000 9.70600   25.68000  1.000 35.20953 ?  74  THR   A CG2   1 
ATOM   603  N  N     . GLY   A 1 76  ? 24.12700 7.47300   22.84900  1.000 29.81457 ?  75  GLY   A N     1 
ATOM   604  C  CA    . GLY   A 1 76  ? 23.26700 6.76500   21.90800  1.000 25.86465 ?  75  GLY   A CA    1 
ATOM   605  C  C     . GLY   A 1 76  ? 23.34900 5.25500   22.07500  1.000 29.22774 ?  75  GLY   A C     1 
ATOM   606  O  O     . GLY   A 1 76  ? 24.40300 4.70100   22.38800  1.000 28.59580 ?  75  GLY   A O     1 
ATOM   607  N  N     . GLU   A 1 77  ? 22.21000 4.57400   21.86300  1.000 25.67316 ?  76  GLU   A N     1 
ATOM   608  C  CA    . GLU   A 1 77  ? 22.19300 3.11200   21.93500  1.000 25.75763 ?  76  GLU   A CA    1 
ATOM   609  C  C     . GLU   A 1 77  ? 22.39100 2.43200   20.58600  1.000 30.32682 ?  76  GLU   A C     1 
ATOM   610  O  O     . GLU   A 1 77  ? 22.88900 1.30500   20.53500  1.000 27.44641 ?  76  GLU   A O     1 
ATOM   611  C  CB    . GLU   A 1 77  ? 20.87400 2.61000   22.53400  1.000 28.04389 ?  76  GLU   A CB    1 
ATOM   612  C  CG    . GLU   A 1 77  ? 20.65000 2.98100   23.96700  1.000 33.19975 ?  76  GLU   A CG    1 
ATOM   613  C  CD    . GLU   A 1 77  ? 19.26100 2.55400   24.44300  1.000 40.12553 ?  76  GLU   A CD    1 
ATOM   614  O  OE1   . GLU   A 1 77  ? 18.26000 2.85200   23.74900  1.000 34.23806 ?  76  GLU   A OE1   1 
ATOM   615  O  OE2   . GLU   A 1 77  ? 19.16600 1.89400   25.50100  1.000 53.22621 -1 76  GLU   A OE2   1 
ATOM   616  N  N     . GLY   A 1 78  ? 21.97800 3.05100   19.49200  1.000 25.81630 ?  77  GLY   A N     1 
ATOM   617  C  CA    . GLY   A 1 78  ? 22.18800 2.46400   18.18200  1.000 24.20759 ?  77  GLY   A CA    1 
ATOM   618  C  C     . GLY   A 1 78  ? 22.38900 3.56400   17.16800  1.000 23.64812 ?  77  GLY   A C     1 
ATOM   619  O  O     . GLY   A 1 78  ? 21.92900 4.68700   17.36000  1.000 22.11629 ?  77  GLY   A O     1 
ATOM   620  N  N     . PHE   A 1 79  ? 23.09500 3.24200   16.08700  1.000 22.21050 ?  78  PHE   A N     1 
ATOM   621  C  CA    . PHE   A 1 79  ? 23.49500 4.25500   15.12800  1.000 22.22878 ?  78  PHE   A CA    1 
ATOM   622  C  C     . PHE   A 1 79  ? 23.07400 3.89200   13.72300  1.000 24.29737 ?  78  PHE   A C     1 
ATOM   623  O  O     . PHE   A 1 79  ? 23.34000 2.77400   13.25000  1.000 22.98963 ?  78  PHE   A O     1 
ATOM   624  C  CB    . PHE   A 1 79  ? 25.01200 4.44700   15.20900  1.000 23.28254 ?  78  PHE   A CB    1 
ATOM   625  C  CG    . PHE   A 1 79  ? 25.42000 4.91800   16.54600  1.000 21.39057 ?  78  PHE   A CG    1 
ATOM   626  C  CD1   . PHE   A 1 79  ? 25.50300 4.03200   17.59100  1.000 22.71933 ?  78  PHE   A CD1   1 
ATOM   627  C  CD2   . PHE   A 1 79  ? 25.60300 6.25800   16.78700  1.000 22.55569 ?  78  PHE   A CD2   1 
ATOM   628  C  CE1   . PHE   A 1 79  ? 25.83300 4.47700   18.88500  1.000 23.27659 ?  78  PHE   A CE1   1 
ATOM   629  C  CE2   . PHE   A 1 79  ? 25.92600 6.70600   18.04900  1.000 20.81950 ?  78  PHE   A CE2   1 
ATOM   630  C  CZ    . PHE   A 1 79  ? 26.02300 5.81500   19.10600  1.000 24.13436 ?  78  PHE   A CZ    1 
ATOM   631  N  N     . LEU   A 1 80  ? 22.44000 4.84300   13.04000  1.000 22.23946 ?  79  LEU   A N     1 
ATOM   632  C  CA    . LEU   A 1 80  ? 22.14000 4.69700   11.62200  1.000 22.66556 ?  79  LEU   A CA    1 
ATOM   633  C  C     . LEU   A 1 80  ? 23.28500 5.39300   10.91500  1.000 22.82029 ?  79  LEU   A C     1 
ATOM   634  O  O     . LEU   A 1 80  ? 23.44100 6.61700   11.03500  1.000 24.97199 ?  79  LEU   A O     1 
ATOM   635  C  CB    . LEU   A 1 80  ? 20.79400 5.34400   11.26700  1.000 23.41161 ?  79  LEU   A CB    1 
ATOM   636  C  CG    . LEU   A 1 80  ? 19.82400 4.64600   10.33700  1.000 29.64855 ?  79  LEU   A CG    1 
ATOM   637  C  CD1   . LEU   A 1 80  ? 19.48000 3.28700   10.91800  1.000 25.46075 ?  79  LEU   A CD1   1 
ATOM   638  C  CD2   . LEU   A 1 80  ? 18.56800 5.54500   10.14100  1.000 26.16112 ?  79  LEU   A CD2   1 
ATOM   639  N  N     . CYS   A 1 81  ? 24.10300 4.62300   10.20700  1.000 23.79337 ?  80  CYS   A N     1 
ATOM   640  C  CA    . CYS   A 1 81  ? 25.28800 5.15300   9.53100   1.000 23.74357 ?  80  CYS   A CA    1 
ATOM   641  C  C     . CYS   A 1 81  ? 24.96300 5.34300   8.05600   1.000 22.44765 ?  80  CYS   A C     1 
ATOM   642  O  O     . CYS   A 1 81  ? 24.89600 4.37000   7.29400   1.000 22.89666 ?  80  CYS   A O     1 
ATOM   643  C  CB    . CYS   A 1 81  ? 26.47600 4.21300   9.69800   1.000 23.29585 ?  80  CYS   A CB    1 
ATOM   644  S  SG    . CYS   A 1 81  ? 26.96800 4.09500   11.40700  1.000 28.13223 ?  80  CYS   A SG    1 
ATOM   645  N  N     . VAL   A 1 82  ? 24.77400 6.59300   7.64600   1.000 22.28922 ?  81  VAL   A N     1 
ATOM   646  C  CA    . VAL   A 1 82  ? 24.19400 6.91800   6.35200   1.000 22.63004 ?  81  VAL   A CA    1 
ATOM   647  C  C     . VAL   A 1 82  ? 25.26300 7.41300   5.38800   1.000 22.84454 ?  81  VAL   A C     1 
ATOM   648  O  O     . VAL   A 1 82  ? 26.04400 8.30300   5.72400   1.000 23.06664 ?  81  VAL   A O     1 
ATOM   649  C  CB    . VAL   A 1 82  ? 23.09000 7.98700   6.50000   1.000 22.46676 ?  81  VAL   A CB    1 
ATOM   650  C  CG1   . VAL   A 1 82  ? 22.33200 8.14400   5.21900   1.000 22.87499 ?  81  VAL   A CG1   1 
ATOM   651  C  CG2   . VAL   A 1 82  ? 22.13800 7.61100   7.65400   1.000 22.44031 ?  81  VAL   A CG2   1 
ATOM   652  N  N     . PHE   A 1 83  ? 25.24800 6.88600   4.17600   1.000 23.18139 ?  82  PHE   A N     1 
ATOM   653  C  CA    . PHE   A 1 83  ? 25.98400 7.49400   3.07200   1.000 23.99989 ?  82  PHE   A CA    1 
ATOM   654  C  C     . PHE   A 1 83  ? 25.02500 7.61700   1.89400   1.000 23.78688 ?  82  PHE   A C     1 
ATOM   655  O  O     . PHE   A 1 83  ? 23.92400 7.07400   1.92600   1.000 24.01227 ?  82  PHE   A O     1 
ATOM   656  C  CB    . PHE   A 1 83  ? 27.22400 6.65400   2.72400   1.000 23.57652 ?  82  PHE   A CB    1 
ATOM   657  C  CG    . PHE   A 1 83  ? 26.88600 5.34000   2.05500   1.000 24.16004 ?  82  PHE   A CG    1 
ATOM   658  C  CD1   . PHE   A 1 83  ? 26.55600 4.23100   2.80700   1.000 24.72350 ?  82  PHE   A CD1   1 
ATOM   659  C  CD2   . PHE   A 1 83  ? 26.88500 5.23200   0.67700   1.000 24.81070 ?  82  PHE   A CD2   1 
ATOM   660  C  CE1   . PHE   A 1 83  ? 26.24700 3.01700   2.18000   1.000 25.19049 ?  82  PHE   A CE1   1 
ATOM   661  C  CE2   . PHE   A 1 83  ? 26.56300 4.01700   0.04900   1.000 28.57279 ?  82  PHE   A CE2   1 
ATOM   662  C  CZ    . PHE   A 1 83  ? 26.24900 2.92300   0.82400   1.000 25.33193 ?  82  PHE   A CZ    1 
ATOM   663  N  N     . ALA   A 1 84  ? 25.40600 8.36700   0.86700   1.000 24.73224 ?  83  ALA   A N     1 
ATOM   664  C  CA    . ALA   A 1 84  ? 24.57000 8.54500   -0.31700  1.000 24.99852 ?  83  ALA   A CA    1 
ATOM   665  C  C     . ALA   A 1 84  ? 25.15000 7.72600   -1.47000  1.000 32.84622 ?  83  ALA   A C     1 
ATOM   666  O  O     . ALA   A 1 84  ? 26.35200 7.78900   -1.72300  1.000 26.96394 ?  83  ALA   A O     1 
ATOM   667  C  CB    . ALA   A 1 84  ? 24.47000 10.02600  -0.70900  1.000 27.53761 ?  83  ALA   A CB    1 
ATOM   668  N  N     . ILE   A 1 85  ? 24.30500 6.95000   -2.16200  1.000 29.57130 ?  84  ILE   A N     1 
ATOM   669  C  CA    . ILE   A 1 85  ? 24.82500 6.01900   -3.15900  1.000 36.30770 ?  84  ILE   A CA    1 
ATOM   670  C  C     . ILE   A 1 85  ? 25.40400 6.71700   -4.38300  1.000 33.61263 ?  84  ILE   A C     1 
ATOM   671  O  O     . ILE   A 1 85  ? 26.03100 6.04700   -5.21300  1.000 36.38266 ?  84  ILE   A O     1 
ATOM   672  C  CB    . ILE   A 1 85  ? 23.75400 4.99400   -3.60100  1.000 33.28199 ?  84  ILE   A CB    1 
ATOM   673  C  CG1   . ILE   A 1 85  ? 22.52500 5.69500   -4.17800  1.000 35.54719 ?  84  ILE   A CG1   1 
ATOM   674  C  CG2   . ILE   A 1 85  ? 23.39500 4.05600   -2.43400  1.000 33.27356 ?  84  ILE   A CG2   1 
ATOM   675  C  CD1   . ILE   A 1 85  ? 22.54800 5.86400   -5.68700  1.000 44.24417 ?  84  ILE   A CD1   1 
ATOM   676  N  N     . ASN   A 1 86  ? 25.21000 8.03100   -4.52600  1.000 33.06762 ?  85  ASN   A N     1 
ATOM   677  C  CA    . ASN   A 1 86  ? 25.82300 8.81200   -5.59800  1.000 35.90431 ?  85  ASN   A CA    1 
ATOM   678  C  C     . ASN   A 1 86  ? 26.97900 9.68600   -5.11300  1.000 35.46967 ?  85  ASN   A C     1 
ATOM   679  O  O     . ASN   A 1 86  ? 27.26500 10.70900  -5.73900  1.000 41.57832 ?  85  ASN   A O     1 
ATOM   680  C  CB    . ASN   A 1 86  ? 24.77400 9.69300   -6.28000  1.000 34.26243 ?  85  ASN   A CB    1 
ATOM   681  C  CG    . ASN   A 1 86  ? 24.23000 10.77500  -5.34900  1.000 32.62909 ?  85  ASN   A CG    1 
ATOM   682  O  OD1   . ASN   A 1 86  ? 24.27800 10.63500  -4.11900  1.000 34.48654 ?  85  ASN   A OD1   1 
ATOM   683  N  ND2   . ASN   A 1 86  ? 23.70100 11.84000  -5.92100  1.000 38.25527 ?  85  ASN   A ND2   1 
ATOM   684  N  N     . ASN   A 1 87  ? 27.62600 9.32700   -3.98900  1.000 32.09173 ?  86  ASN   A N     1 
ATOM   685  C  CA    . ASN   A 1 87  ? 28.67100 10.14100  -3.35600  1.000 32.61815 ?  86  ASN   A CA    1 
ATOM   686  C  C     . ASN   A 1 87  ? 29.69400 9.17800   -2.73400  1.000 32.77507 ?  86  ASN   A C     1 
ATOM   687  O  O     . ASN   A 1 87  ? 29.59000 8.78600   -1.56400  1.000 30.68874 ?  86  ASN   A O     1 
ATOM   688  C  CB    . ASN   A 1 87  ? 28.06700 11.11000  -2.34300  1.000 32.32975 ?  86  ASN   A CB    1 
ATOM   689  C  CG    . ASN   A 1 87  ? 29.10300 11.97000  -1.61000  1.000 36.90605 ?  86  ASN   A CG    1 
ATOM   690  O  OD1   . ASN   A 1 87  ? 30.28000 11.64800  -1.54300  1.000 37.55959 ?  86  ASN   A OD1   1 
ATOM   691  N  ND2   . ASN   A 1 87  ? 28.62600 13.04500  -0.98400  1.000 39.96851 ?  86  ASN   A ND2   1 
ATOM   692  N  N     A THR   A 1 88  ? 30.70400 8.82100   -3.53600  0.500 35.51372 ?  87  THR   A N     1 
ATOM   693  N  N     B THR   A 1 88  ? 30.70600 8.82600   -3.53400  0.500 35.51467 ?  87  THR   A N     1 
ATOM   694  C  CA    A THR   A 1 88  ? 31.74700 7.90300   -3.08300  0.500 32.82966 ?  87  THR   A CA    1 
ATOM   695  C  CA    B THR   A 1 88  ? 31.74600 7.90400   -3.08300  0.500 32.82917 ?  87  THR   A CA    1 
ATOM   696  C  C     A THR   A 1 88  ? 32.46800 8.42000   -1.84600  0.500 32.26001 ?  87  THR   A C     1 
ATOM   697  C  C     B THR   A 1 88  ? 32.46400 8.42000   -1.84100  0.500 32.26232 ?  87  THR   A C     1 
ATOM   698  O  O     A THR   A 1 88  ? 32.86600 7.63200   -0.97900  0.500 32.51426 ?  87  THR   A O     1 
ATOM   699  O  O     B THR   A 1 88  ? 32.86500 7.63500   -0.97300  0.500 32.51374 ?  87  THR   A O     1 
ATOM   700  C  CB    A THR   A 1 88  ? 32.74900 7.66700   -4.22000  0.500 34.67286 ?  87  THR   A CB    1 
ATOM   701  C  CB    B THR   A 1 88  ? 32.74800 7.67400   -4.21800  0.500 34.67498 ?  87  THR   A CB    1 
ATOM   702  O  OG1   A THR   A 1 88  ? 32.03300 7.38100   -5.42600  0.500 38.04641 ?  87  THR   A OG1   1 
ATOM   703  O  OG1   B THR   A 1 88  ? 33.26100 8.94100   -4.64600  0.500 35.51821 ?  87  THR   A OG1   1 
ATOM   704  C  CG2   A THR   A 1 88  ? 33.68700 6.51200   -3.88100  0.500 33.44144 ?  87  THR   A CG2   1 
ATOM   705  C  CG2   B THR   A 1 88  ? 32.07000 7.00200   -5.38200  0.500 38.27479 ?  87  THR   A CG2   1 
ATOM   706  N  N     . LYS   A 1 89  ? 32.63700 9.73700   -1.73500  1.000 31.79456 ?  88  LYS   A N     1 
ATOM   707  C  CA    . LYS   A 1 89  ? 33.29300 10.29500  -0.56200  1.000 33.76617 ?  88  LYS   A CA    1 
ATOM   708  C  C     . LYS   A 1 89  ? 32.48100 10.02500  0.70500   1.000 34.18644 ?  88  LYS   A C     1 
ATOM   709  O  O     . LYS   A 1 89  ? 33.04700 9.72600   1.76200   1.000 33.68247 ?  88  LYS   A O     1 
ATOM   710  C  CB    . LYS   A 1 89  ? 33.51400 11.79300  -0.77100  1.000 36.12410 ?  88  LYS   A CB    1 
ATOM   711  C  CG    . LYS   A 1 89  ? 33.91600 12.57500  0.46300   1.000 40.41317 ?  88  LYS   A CG    1 
ATOM   712  C  CD    . LYS   A 1 89  ? 35.35700 12.35100  0.87800   1.000 42.55550 ?  88  LYS   A CD    1 
ATOM   713  C  CE    . LYS   A 1 89  ? 35.89900 13.60000  1.59200   1.000 44.54269 ?  88  LYS   A CE    1 
ATOM   714  N  NZ    . LYS   A 1 89  ? 35.03100 14.06600  2.73300   1.000 49.18818 ?  88  LYS   A NZ    1 
ATOM   715  N  N     . SER   A 1 90  ? 31.14700 10.08300  0.61200   1.000 32.23019 ?  89  SER   A N     1 
ATOM   716  C  CA    . SER   A 1 90  ? 30.34600 9.81400   1.80900   1.000 30.53020 ?  89  SER   A CA    1 
ATOM   717  C  C     . SER   A 1 90  ? 30.48200 8.36600   2.24200   1.000 29.86116 ?  89  SER   A C     1 
ATOM   718  O  O     . SER   A 1 90  ? 30.39700 8.07600   3.44400   1.000 29.30665 ?  89  SER   A O     1 
ATOM   719  C  CB    . SER   A 1 90  ? 28.86300 10.17800  1.58100   1.000 25.97901 ?  89  SER   A CB    1 
ATOM   720  O  OG    . SER   A 1 90  ? 28.20300 9.33000   0.64700   1.000 27.60090 ?  89  SER   A OG    1 
ATOM   721  N  N     . PHE   A 1 91  ? 30.70000 7.45800   1.28000   1.000 28.22182 ?  90  PHE   A N     1 
ATOM   722  C  CA    . PHE   A 1 91  ? 30.94000 6.05700   1.60300   1.000 30.46715 ?  90  PHE   A CA    1 
ATOM   723  C  C     . PHE   A 1 91  ? 32.29000 5.88100   2.30300   1.000 32.88168 ?  90  PHE   A C     1 
ATOM   724  O  O     . PHE   A 1 91  ? 32.38900 5.15900   3.30000   1.000 34.63107 ?  90  PHE   A O     1 
ATOM   725  C  CB    . PHE   A 1 91  ? 30.84500 5.22200   0.33000   1.000 27.80711 ?  90  PHE   A CB    1 
ATOM   726  C  CG    . PHE   A 1 91  ? 30.97700 3.74800   0.57000   1.000 36.09385 ?  90  PHE   A CG    1 
ATOM   727  C  CD1   . PHE   A 1 91  ? 30.03000 3.06100   1.31700   1.000 30.11258 ?  90  PHE   A CD1   1 
ATOM   728  C  CD2   . PHE   A 1 91  ? 32.05900 3.04500   0.05700   1.000 34.55154 ?  90  PHE   A CD2   1 
ATOM   729  C  CE1   . PHE   A 1 91  ? 30.15000 1.70000   1.53800   1.000 33.75032 ?  90  PHE   A CE1   1 
ATOM   730  C  CE2   . PHE   A 1 91  ? 32.17600 1.69600   0.27900   1.000 35.64081 ?  90  PHE   A CE2   1 
ATOM   731  C  CZ    . PHE   A 1 91  ? 31.22300 1.01800   1.01500   1.000 39.03276 ?  90  PHE   A CZ    1 
ATOM   732  N  N     . GLU   A 1 92  ? 33.33200 6.56500   1.81400   1.000 38.14388 ?  91  GLU   A N     1 
ATOM   733  C  CA    . GLU   A 1 92  ? 34.62200 6.54600   2.50800   1.000 35.72443 ?  91  GLU   A CA    1 
ATOM   734  C  C     . GLU   A 1 92  ? 34.49200 7.11700   3.91400   1.000 34.84221 ?  91  GLU   A C     1 
ATOM   735  O  O     . GLU   A 1 92  ? 35.05700 6.57700   4.87200   1.000 39.52177 ?  91  GLU   A O     1 
ATOM   736  C  CB    . GLU   A 1 92  ? 35.66100 7.34200   1.70900   1.000 37.51955 ?  91  GLU   A CB    1 
ATOM   737  C  CG    . GLU   A 1 92  ? 35.87500 6.86100   0.29000   1.000 42.77148 ?  91  GLU   A CG    1 
ATOM   738  C  CD    . GLU   A 1 92  ? 36.65400 7.87400   -0.56500  1.000 47.86558 ?  91  GLU   A CD    1 
ATOM   739  O  OE1   . GLU   A 1 92  ? 37.29500 8.79000   0.01700   1.000 52.31080 ?  91  GLU   A OE1   1 
ATOM   740  O  OE2   . GLU   A 1 92  ? 36.61400 7.76200   -1.81700  1.000 51.96656 -1 91  GLU   A OE2   1 
ATOM   741  N  N     . ASP   A 1 93  ? 33.74500 8.20900   4.06200   1.000 38.90385 ?  92  ASP   A N     1 
ATOM   742  C  CA    . ASP   A 1 93  ? 33.57300 8.80600   5.38300   1.000 36.74834 ?  92  ASP   A CA    1 
ATOM   743  C  C     . ASP   A 1 93  ? 32.89600 7.84700   6.35600   1.000 36.75905 ?  92  ASP   A C     1 
ATOM   744  O  O     . ASP   A 1 93  ? 33.09800 7.97000   7.56800   1.000 31.72746 ?  92  ASP   A O     1 
ATOM   745  C  CB    . ASP   A 1 93  ? 32.77200 10.11100  5.28400   1.000 38.21392 ?  92  ASP   A CB    1 
ATOM   746  C  CG    . ASP   A 1 93  ? 33.44500 11.15000  4.38100   1.000 46.56455 ?  92  ASP   A CG    1 
ATOM   747  O  OD1   . ASP   A 1 93  ? 34.70200 11.10200  4.21100   1.000 46.16835 -1 92  ASP   A OD1   1 
ATOM   748  O  OD2   . ASP   A 1 93  ? 32.71200 12.00500  3.81800   1.000 47.02621 ?  92  ASP   A OD2   1 
ATOM   749  N  N     . ILE   A 1 94  ? 32.15600 6.85800   5.84300   1.000 39.34705 ?  93  ILE   A N     1 
ATOM   750  C  CA    . ILE   A 1 94  ? 31.40500 5.93800   6.69700   1.000 39.31081 ?  93  ILE   A CA    1 
ATOM   751  C  C     . ILE   A 1 94  ? 32.33400 5.14200   7.59500   1.000 36.94058 ?  93  ILE   A C     1 
ATOM   752  O  O     . ILE   A 1 94  ? 32.06000 4.95700   8.78900   1.000 34.40775 ?  93  ILE   A O     1 
ATOM   753  C  CB    . ILE   A 1 94  ? 30.51700 5.01600   5.83200   1.000 37.54916 ?  93  ILE   A CB    1 
ATOM   754  C  CG1   . ILE   A 1 94  ? 29.14200 5.63700   5.72800   1.000 38.56777 ?  93  ILE   A CG1   1 
ATOM   755  C  CG2   . ILE   A 1 94  ? 30.40700 3.62000   6.44200   1.000 39.80326 ?  93  ILE   A CG2   1 
ATOM   756  C  CD1   . ILE   A 1 94  ? 28.64300 6.07000   7.11500   1.000 28.42016 ?  93  ILE   A CD1   1 
ATOM   757  N  N     A HIS   A 1 95  ? 33.44500 4.65400   7.03500   0.500 37.02863 ?  94  HIS   A N     1 
ATOM   758  N  N     B HIS   A 1 95  ? 33.45200 4.64800   7.04600   0.500 37.03126 ?  94  HIS   A N     1 
ATOM   759  C  CA    A HIS   A 1 95  ? 34.40600 3.89600   7.82700   0.500 36.42275 ?  94  HIS   A CA    1 
ATOM   760  C  CA    B HIS   A 1 95  ? 34.37800 3.88000   7.87600   0.500 36.40185 ?  94  HIS   A CA    1 
ATOM   761  C  C     A HIS   A 1 95  ? 34.87200 4.71300   9.02400   0.500 35.30757 ?  94  HIS   A C     1 
ATOM   762  C  C     B HIS   A 1 95  ? 34.86700 4.71800   9.04700   0.500 35.30800 ?  94  HIS   A C     1 
ATOM   763  O  O     A HIS   A 1 95  ? 35.03900 4.18600   10.12900  0.500 34.42389 ?  94  HIS   A O     1 
ATOM   764  O  O     B HIS   A 1 95  ? 35.04900 4.20900   10.15800  0.500 34.41271 ?  94  HIS   A O     1 
ATOM   765  C  CB    A HIS   A 1 95  ? 35.60500 3.49500   6.95200   0.500 36.27268 ?  94  HIS   A CB    1 
ATOM   766  C  CB    B HIS   A 1 95  ? 35.56100 3.36700   7.03500   0.500 36.28341 ?  94  HIS   A CB    1 
ATOM   767  C  CG    A HIS   A 1 95  ? 35.23400 2.83800   5.65200   0.500 34.43459 ?  94  HIS   A CG    1 
ATOM   768  C  CG    B HIS   A 1 95  ? 36.81000 4.18700   7.16600   0.500 37.08467 ?  94  HIS   A CG    1 
ATOM   769  N  ND1   A HIS   A 1 95  ? 34.31900 3.37200   4.76700   0.500 30.87994 ?  94  HIS   A ND1   1 
ATOM   770  N  ND1   B HIS   A 1 95  ? 37.19700 5.11400   6.21900   0.500 41.13604 ?  94  HIS   A ND1   1 
ATOM   771  C  CD2   A HIS   A 1 95  ? 35.68300 1.69600   5.07900   0.500 32.41723 ?  94  HIS   A CD2   1 
ATOM   772  C  CD2   B HIS   A 1 95  ? 37.76300 4.21700   8.13000   0.500 40.14299 ?  94  HIS   A CD2   1 
ATOM   773  C  CE1   A HIS   A 1 95  ? 34.21200 2.58100   3.71500   0.500 35.84398 ?  94  HIS   A CE1   1 
ATOM   774  C  CE1   B HIS   A 1 95  ? 38.32600 5.68600   6.60100   0.500 37.48364 ?  94  HIS   A CE1   1 
ATOM   775  N  NE2   A HIS   A 1 95  ? 35.03200 1.55800   3.87900   0.500 34.64057 ?  94  HIS   A NE2   1 
ATOM   776  N  NE2   B HIS   A 1 95  ? 38.68500 5.16500   7.76100   0.500 37.63236 ?  94  HIS   A NE2   1 
ATOM   777  N  N     . HIS   A 1 96  ? 35.05600 6.01800   8.82200   1.000 33.86157 ?  95  HIS   A N     1 
ATOM   778  C  CA    . HIS   A 1 96  ? 35.53300 6.89500   9.88100   1.000 37.57715 ?  95  HIS   A CA    1 
ATOM   779  C  C     . HIS   A 1 96  ? 34.52500 6.97600   11.01900  1.000 33.88534 ?  95  HIS   A C     1 
ATOM   780  O  O     . HIS   A 1 96  ? 34.87800 6.86600   12.20000  1.000 29.96075 ?  95  HIS   A O     1 
ATOM   781  C  CB    . HIS   A 1 96  ? 35.79500 8.27400   9.27000   1.000 36.15724 ?  95  HIS   A CB    1 
ATOM   782  C  CG    . HIS   A 1 96  ? 36.31000 9.29000   10.23700  1.000 44.81721 ?  95  HIS   A CG    1 
ATOM   783  N  ND1   . HIS   A 1 96  ? 35.48500 10.00100  11.08300  1.000 52.05484 ?  95  HIS   A ND1   1 
ATOM   784  C  CD2   . HIS   A 1 96  ? 37.56700 9.74000   10.46800  1.000 46.00007 ?  95  HIS   A CD2   1 
ATOM   785  C  CE1   . HIS   A 1 96  ? 36.21600 10.82600  11.81300  1.000 49.04235 ?  95  HIS   A CE1   1 
ATOM   786  N  NE2   . HIS   A 1 96  ? 37.48100 10.69200  11.45500  1.000 50.72825 ?  95  HIS   A NE2   1 
ATOM   787  N  N     . TYR   A 1 97  ? 33.24600 7.16400   10.68000  1.000 31.74002 ?  96  TYR   A N     1 
ATOM   788  C  CA    . TYR   A 1 97  ? 32.21500 7.22000   11.71300  1.000 29.64683 ?  96  TYR   A CA    1 
ATOM   789  C  C     . TYR   A 1 97  ? 32.13100 5.90400   12.48000  1.000 24.54452 ?  96  TYR   A C     1 
ATOM   790  O  O     . TYR   A 1 97  ? 31.94700 5.90200   13.69000  1.000 27.22953 ?  96  TYR   A O     1 
ATOM   791  C  CB    . TYR   A 1 97  ? 30.85000 7.56900   11.08100  1.000 25.02189 ?  96  TYR   A CB    1 
ATOM   792  C  CG    . TYR   A 1 97  ? 30.55000 9.04200   10.97300  1.000 25.87823 ?  96  TYR   A CG    1 
ATOM   793  C  CD1   . TYR   A 1 97  ? 30.09300 9.74500   12.08400  1.000 26.33974 ?  96  TYR   A CD1   1 
ATOM   794  C  CD2   . TYR   A 1 97  ? 30.62200 9.71000   9.76300   1.000 28.52825 ?  96  TYR   A CD2   1 
ATOM   795  C  CE1   . TYR   A 1 97  ? 29.78900 11.09000  12.00600  1.000 29.41323 ?  96  TYR   A CE1   1 
ATOM   796  C  CE2   . TYR   A 1 97  ? 30.31100 11.06500  9.67200   1.000 27.16609 ?  96  TYR   A CE2   1 
ATOM   797  C  CZ    . TYR   A 1 97  ? 29.89400 11.73800  10.80400  1.000 26.81378 ?  96  TYR   A CZ    1 
ATOM   798  O  OH    . TYR   A 1 97  ? 29.58000 13.08500  10.73800  1.000 33.41311 ?  96  TYR   A OH    1 
ATOM   799  N  N     . ARG   A 1 98  ? 32.23900 4.76800   11.78600  1.000 28.75658 ?  97  ARG   A N     1 
ATOM   800  C  CA    . ARG   A 1 98  ? 32.14200 3.48900   12.47900  1.000 28.88771 ?  97  ARG   A CA    1 
ATOM   801  C  C     . ARG   A 1 98  ? 33.31000 3.29600   13.43200  1.000 33.13650 ?  97  ARG   A C     1 
ATOM   802  O  O     . ARG   A 1 98  ? 33.12100 2.87500   14.58200  1.000 32.74478 ?  97  ARG   A O     1 
ATOM   803  C  CB    . ARG   A 1 98  ? 32.06700 2.33400   11.47900  1.000 38.52370 ?  97  ARG   A CB    1 
ATOM   804  C  CG    . ARG   A 1 98  ? 31.78100 0.99300   12.13800  1.000 40.52333 ?  97  ARG   A CG    1 
ATOM   805  C  CD    . ARG   A 1 98  ? 32.96400 0.05500   12.04600  1.000 44.54740 ?  97  ARG   A CD    1 
ATOM   806  N  NE    . ARG   A 1 98  ? 32.65300 -1.28700  12.53200  1.000 49.74834 ?  97  ARG   A NE    1 
ATOM   807  C  CZ    . ARG   A 1 98  ? 33.56700 -2.23900  12.69400  1.000 52.21568 ?  97  ARG   A CZ    1 
ATOM   808  N  NH1   . ARG   A 1 98  ? 34.84100 -2.02800  12.39400  1.000 38.94655 ?  97  ARG   A NH1   1 
ATOM   809  N  NH2   . ARG   A 1 98  ? 33.19900 -3.42000  13.18700  1.000 51.53528 ?  97  ARG   A NH2   1 
ATOM   810  N  N     . GLU   A 1 99  ? 34.53300 3.62300   12.97600  1.000 36.07717 ?  98  GLU   A N     1 
ATOM   811  C  CA    . GLU   A 1 99  ? 35.69400 3.53300   13.85800  1.000 37.07392 ?  98  GLU   A CA    1 
ATOM   812  C  C     . GLU   A 1 99  ? 35.56400 4.49000   15.02500  1.000 32.74160 ?  98  GLU   A C     1 
ATOM   813  O  O     . GLU   A 1 99  ? 35.97400 4.17700   16.14700  1.000 36.32846 ?  98  GLU   A O     1 
ATOM   814  C  CB    . GLU   A 1 99  ? 36.99800 3.82100   13.09300  1.000 32.93944 ?  98  GLU   A CB    1 
ATOM   815  C  CG    . GLU   A 1 99  ? 37.27000 2.91100   11.90600  1.000 39.39443 ?  98  GLU   A CG    1 
ATOM   816  C  CD    . GLU   A 1 99  ? 37.18200 1.41500   12.24400  1.000 51.51968 ?  98  GLU   A CD    1 
ATOM   817  O  OE1   . GLU   A 1 99  ? 37.56800 1.02200   13.37800  1.000 51.68069 ?  98  GLU   A OE1   1 
ATOM   818  O  OE2   . GLU   A 1 99  ? 36.71700 0.63700   11.36800  1.000 51.11821 -1 98  GLU   A OE2   1 
ATOM   819  N  N     . GLN   A 1 100 ? 35.01500 5.67900   14.78300  1.000 33.67098 ?  99  GLN   A N     1 
ATOM   820  C  CA    . GLN   A 1 100 ? 34.87300 6.64000   15.87100  1.000 28.53540 ?  99  GLN   A CA    1 
ATOM   821  C  C     . GLN   A 1 100 ? 33.87700 6.14600   16.91300  1.000 30.93055 ?  99  GLN   A C     1 
ATOM   822  O  O     . GLN   A 1 100 ? 34.14000 6.22900   18.11300  1.000 29.23030 ?  99  GLN   A O     1 
ATOM   823  C  CB    . GLN   A 1 100 ? 34.47400 8.01200   15.30400  1.000 34.60298 ?  99  GLN   A CB    1 
ATOM   824  C  CG    . GLN   A 1 100 ? 34.38800 9.12300   16.33600  1.000 32.66717 ?  99  GLN   A CG    1 
ATOM   825  C  CD    . GLN   A 1 100 ? 34.18700 10.50700  15.73100  1.000 36.22949 ?  99  GLN   A CD    1 
ATOM   826  O  OE1   . GLN   A 1 100 ? 33.82000 10.64500  14.56200  1.000 43.36055 ?  99  GLN   A OE1   1 
ATOM   827  N  NE2   . GLN   A 1 100 ? 34.41000 11.54300  16.54200  1.000 44.09614 ?  99  GLN   A NE2   1 
ATOM   828  N  N     . ILE   A 1 101 ? 32.72600 5.60200   16.48300  1.000 28.42356 ?  100 ILE   A N     1 
ATOM   829  C  CA    . ILE   A 1 101 ? 31.75000 5.09400   17.44900  1.000 25.15465 ?  100 ILE   A CA    1 
ATOM   830  C  C     . ILE   A 1 101 ? 32.34600 3.95900   18.26400  1.000 29.65595 ?  100 ILE   A C     1 
ATOM   831  O  O     . ILE   A 1 101 ? 32.23100 3.92600   19.49100  1.000 31.06713 ?  100 ILE   A O     1 
ATOM   832  C  CB    . ILE   A 1 101 ? 30.46000 4.63600   16.73300  1.000 24.61766 ?  100 ILE   A CB    1 
ATOM   833  C  CG1   . ILE   A 1 101 ? 29.79000 5.82000   16.05500  1.000 27.36784 ?  100 ILE   A CG1   1 
ATOM   834  C  CG2   . ILE   A 1 101 ? 29.54900 3.93600   17.73500  1.000 27.72819 ?  100 ILE   A CG2   1 
ATOM   835  C  CD1   . ILE   A 1 101 ? 28.79700 5.38700   14.93600  1.000 24.66936 ?  100 ILE   A CD1   1 
ATOM   836  N  N     . LYS   A 1 102 ? 32.99700 3.00800   17.58400  1.000 34.88654 ?  101 LYS   A N     1 
ATOM   837  C  CA    . LYS   A 1 102 ? 33.61800 1.87400   18.26400  1.000 35.16028 ?  101 LYS   A CA    1 
ATOM   838  C  C     . LYS   A 1 102 ? 34.64100 2.32700   19.29500  1.000 36.10771 ?  101 LYS   A C     1 
ATOM   839  O  O     . LYS   A 1 102 ? 34.66700 1.83200   20.43000  1.000 35.23499 ?  101 LYS   A O     1 
ATOM   840  C  CB    . LYS   A 1 102 ? 34.28800 0.97700   17.24100  1.000 38.92318 ?  101 LYS   A CB    1 
ATOM   841  C  CG    . LYS   A 1 102 ? 33.37800 -0.03800  16.59600  1.000 38.94827 ?  101 LYS   A CG    1 
ATOM   842  C  CD    . LYS   A 1 102 ? 34.17400 -0.82500  15.55900  1.000 45.11442 ?  101 LYS   A CD    1 
ATOM   843  C  CE    . LYS   A 1 102 ? 35.62700 -1.06000  16.01400  1.000 47.84798 ?  101 LYS   A CE    1 
ATOM   844  N  NZ    . LYS   A 1 102 ? 36.56800 -1.39100  14.88900  1.000 55.03326 ?  101 LYS   A NZ    1 
ATOM   845  N  N     . ARG   A 1 103 ? 35.50100 3.26600   18.90400  1.000 36.81723 ?  102 ARG   A N     1 
ATOM   846  C  CA    . ARG   A 1 103 ? 36.49900 3.80700   19.82100  1.000 39.02089 ?  102 ARG   A CA    1 
ATOM   847  C  C     . ARG   A 1 103 ? 35.84700 4.48500   21.02700  1.000 40.54453 ?  102 ARG   A C     1 
ATOM   848  O  O     . ARG   A 1 103 ? 36.22400 4.23100   22.17800  1.000 37.51554 ?  102 ARG   A O     1 
ATOM   849  C  CB    . ARG   A 1 103 ? 37.39700 4.78000   19.06000  1.000 38.92148 ?  102 ARG   A CB    1 
ATOM   850  C  CG    . ARG   A 1 103 ? 38.64000 5.22900   19.81900  1.000 42.72077 ?  102 ARG   A CG    1 
ATOM   851  C  CD    . ARG   A 1 103 ? 39.62700 5.94600   18.88000  1.000 42.81302 ?  102 ARG   A CD    1 
ATOM   852  N  NE    . ARG   A 1 103 ? 38.97400 6.92800   18.01500  1.000 47.18524 ?  102 ARG   A NE    1 
ATOM   853  C  CZ    . ARG   A 1 103 ? 38.38500 8.03700   18.45100  1.000 41.51045 ?  102 ARG   A CZ    1 
ATOM   854  N  NH1   . ARG   A 1 103 ? 38.37400 8.35800   19.74200  1.000 44.97069 ?  102 ARG   A NH1   1 
ATOM   855  N  NH2   . ARG   A 1 103 ? 37.78300 8.83900   17.57600  1.000 45.09797 ?  102 ARG   A NH2   1 
ATOM   856  N  N     . VAL   A 1 104 ? 34.85200 5.35000   20.78700  1.000 36.72372 ?  103 VAL   A N     1 
ATOM   857  C  CA    . VAL   A 1 104 ? 34.26600 6.12300   21.88500  1.000 32.58166 ?  103 VAL   A CA    1 
ATOM   858  C  C     . VAL   A 1 104 ? 33.49700 5.22700   22.85100  1.000 36.83634 ?  103 VAL   A C     1 
ATOM   859  O  O     . VAL   A 1 104 ? 33.55800 5.42500   24.07400  1.000 38.52332 ?  103 VAL   A O     1 
ATOM   860  C  CB    . VAL   A 1 104 ? 33.38300 7.26600   21.34000  1.000 28.93075 ?  103 VAL   A CB    1 
ATOM   861  C  CG1   . VAL   A 1 104 ? 32.54000 7.86300   22.45900  1.000 33.66790 ?  103 VAL   A CG1   1 
ATOM   862  C  CG2   . VAL   A 1 104 ? 34.25900 8.34800   20.67800  1.000 34.96596 ?  103 VAL   A CG2   1 
ATOM   863  N  N     . LYS   A 1 105 ? 32.73900 4.24900   22.33500  1.000 36.33386 ?  104 LYS   A N     1 
ATOM   864  C  CA    . LYS   A 1 105 ? 32.00100 3.32600   23.19500  1.000 36.28274 ?  104 LYS   A CA    1 
ATOM   865  C  C     . LYS   A 1 105 ? 32.85400 2.17400   23.69100  1.000 39.65990 ?  104 LYS   A C     1 
ATOM   866  O  O     . LYS   A 1 105 ? 32.35300 1.35200   24.47800  1.000 39.84071 ?  104 LYS   A O     1 
ATOM   867  C  CB    . LYS   A 1 105 ? 30.78900 2.69100   22.48600  1.000 36.36345 ?  104 LYS   A CB    1 
ATOM   868  C  CG    . LYS   A 1 105 ? 30.04700 3.58700   21.56000  1.000 39.89473 ?  104 LYS   A CG    1 
ATOM   869  C  CD    . LYS   A 1 105 ? 28.90500 4.26200   22.22200  1.000 41.26280 ?  104 LYS   A CD    1 
ATOM   870  C  CE    . LYS   A 1 105 ? 27.67500 3.39400   22.40800  1.000 27.97881 ?  104 LYS   A CE    1 
ATOM   871  N  NZ    . LYS   A 1 105 ? 26.89100 4.05600   23.45700  1.000 26.68388 ?  104 LYS   A NZ    1 
ATOM   872  N  N     . ASP   A 1 106 ? 34.09000 2.05400   23.20400  1.000 40.39310 ?  105 ASP   A N     1 
ATOM   873  C  CA    . ASP   A 1 106 ? 35.01400 1.04200   23.70800  1.000 39.49137 ?  105 ASP   A CA    1 
ATOM   874  C  C     . ASP   A 1 106 ? 34.40200 -0.35100  23.55400  1.000 40.78134 ?  105 ASP   A C     1 
ATOM   875  O  O     . ASP   A 1 106 ? 34.37300 -1.15000  24.49100  1.000 42.58178 ?  105 ASP   A O     1 
ATOM   876  C  CB    . ASP   A 1 106 ? 35.36100 1.35500   25.16700  1.000 43.06676 ?  105 ASP   A CB    1 
ATOM   877  C  CG    . ASP   A 1 106 ? 36.47800 0.49500   25.71600  1.000 50.30366 ?  105 ASP   A CG    1 
ATOM   878  O  OD1   . ASP   A 1 106 ? 37.20000 -0.15700  24.91800  1.000 48.95284 -1 105 ASP   A OD1   1 
ATOM   879  O  OD2   . ASP   A 1 106 ? 36.61100 0.47600   26.96500  1.000 55.14492 ?  105 ASP   A OD2   1 
ATOM   880  N  N     . SER   A 1 107 ? 33.87500 -0.63400  22.36100  1.000 37.26085 ?  106 SER   A N     1 
ATOM   881  C  CA    . SER   A 1 107 ? 33.13700 -1.87100  22.16600  1.000 35.82892 ?  106 SER   A CA    1 
ATOM   882  C  C     . SER   A 1 107 ? 33.19000 -2.25800  20.69800  1.000 38.32799 ?  106 SER   A C     1 
ATOM   883  O  O     . SER   A 1 107 ? 33.12500 -1.39600  19.81800  1.000 39.61569 ?  106 SER   A O     1 
ATOM   884  C  CB    . SER   A 1 107 ? 31.67400 -1.71800  22.62200  1.000 33.75827 ?  106 SER   A CB    1 
ATOM   885  O  OG    . SER   A 1 107 ? 30.94800 -2.90600  22.36600  1.000 36.30177 ?  106 SER   A OG    1 
ATOM   886  N  N     . GLU   A 1 108 ? 33.32900 -3.55000  20.44400  1.000 32.66969 ?  107 GLU   A N     1 
ATOM   887  C  CA    . GLU   A 1 108 ? 33.14300 -4.08700  19.10400  1.000 40.19721 ?  107 GLU   A CA    1 
ATOM   888  C  C     . GLU   A 1 108 ? 31.68900 -4.41400  18.84400  1.000 32.96451 ?  107 GLU   A C     1 
ATOM   889  O  O     . GLU   A 1 108 ? 31.34600 -4.86600  17.74500  1.000 43.58421 ?  107 GLU   A O     1 
ATOM   890  C  CB    . GLU   A 1 108 ? 33.99400 -5.34700  18.89900  1.000 39.25566 ?  107 GLU   A CB    1 
ATOM   891  C  CG    . GLU   A 1 108 ? 35.43600 -5.06900  18.49000  1.000 43.54536 ?  107 GLU   A CG    1 
ATOM   892  C  CD    . GLU   A 1 108 ? 35.58800 -4.91700  16.98400  1.000 50.48362 ?  107 GLU   A CD    1 
ATOM   893  O  OE1   . GLU   A 1 108 ? 35.28000 -5.89000  16.25600  1.000 59.17971 ?  107 GLU   A OE1   1 
ATOM   894  O  OE2   . GLU   A 1 108 ? 36.00300 -3.82900  16.52500  1.000 58.14840 -1 107 GLU   A OE2   1 
ATOM   895  N  N     . ASP   A 1 109 ? 30.83100 -4.20100  19.83500  1.000 32.49902 ?  108 ASP   A N     1 
ATOM   896  C  CA    . ASP   A 1 109 ? 29.47500 -4.71100  19.75700  1.000 41.02054 ?  108 ASP   A CA    1 
ATOM   897  C  C     . ASP   A 1 109 ? 28.46700 -3.57900  19.87000  1.000 40.72789 ?  108 ASP   A C     1 
ATOM   898  O  O     . ASP   A 1 109 ? 27.63400 -3.59400  20.77500  1.000 40.84016 ?  108 ASP   A O     1 
ATOM   899  C  CB    . ASP   A 1 109 ? 29.24300 -5.74600  20.85800  1.000 43.06762 ?  108 ASP   A CB    1 
ATOM   900  C  CG    . ASP   A 1 109 ? 27.96700 -6.51800  20.65300  1.000 44.91587 ?  108 ASP   A CG    1 
ATOM   901  O  OD1   . ASP   A 1 109 ? 27.64800 -6.80100  19.47700  1.000 53.62147 ?  108 ASP   A OD1   1 
ATOM   902  O  OD2   . ASP   A 1 109 ? 27.28700 -6.83000  21.65500  1.000 54.07344 -1 108 ASP   A OD2   1 
ATOM   903  N  N     . VAL   A 1 110 ? 28.54300 -2.59400  18.98200  1.000 32.12462 ?  109 VAL   A N     1 
ATOM   904  C  CA    . VAL   A 1 110 ? 27.65900 -1.43300  19.02100  1.000 33.11805 ?  109 VAL   A CA    1 
ATOM   905  C  C     . VAL   A 1 110 ? 26.55100 -1.65800  17.99700  1.000 28.28280 ?  109 VAL   A C     1 
ATOM   906  O  O     . VAL   A 1 110 ? 26.85800 -1.88500  16.82200  1.000 28.68021 ?  109 VAL   A O     1 
ATOM   907  C  CB    . VAL   A 1 110 ? 28.40400 -0.12600  18.71900  1.000 28.40463 ?  109 VAL   A CB    1 
ATOM   908  C  CG1   . VAL   A 1 110 ? 27.41100 1.04100   18.83400  1.000 34.61868 ?  109 VAL   A CG1   1 
ATOM   909  C  CG2   . VAL   A 1 110 ? 29.62500 0.07400   19.67400  1.000 31.17426 ?  109 VAL   A CG2   1 
ATOM   910  N  N     . PRO   A 1 111 ? 25.27900 -1.61400  18.38400  1.000 27.71157 ?  110 PRO   A N     1 
ATOM   911  C  CA    . PRO   A 1 111 ? 24.21000 -1.77000  17.37200  1.000 25.81097 ?  110 PRO   A CA    1 
ATOM   912  C  C     . PRO   A 1 111 ? 24.31500 -0.67000  16.32800  1.000 24.16757 ?  110 PRO   A C     1 
ATOM   913  O  O     . PRO   A 1 111 ? 24.34000 0.51600   16.65500  1.000 25.27045 ?  110 PRO   A O     1 
ATOM   914  C  CB    . PRO   A 1 111 ? 22.92600 -1.67300  18.20500  1.000 28.69734 ?  110 PRO   A CB    1 
ATOM   915  C  CG    . PRO   A 1 111 ? 23.37300 -2.11000  19.62100  1.000 28.33898 ?  110 PRO   A CG    1 
ATOM   916  C  CD    . PRO   A 1 111 ? 24.74100 -1.48900  19.74900  1.000 30.84286 ?  110 PRO   A CD    1 
ATOM   917  N  N     . MET   A 1 112 ? 24.41100 -1.06800  15.05400  1.000 25.04862 ?  111 MET   A N     1 
ATOM   918  C  CA    . MET   A 1 112 ? 24.33900 -0.09000  13.98900  1.000 24.88678 ?  111 MET   A CA    1 
ATOM   919  C  C     . MET   A 1 112 ? 23.82400 -0.74800  12.72400  1.000 24.08993 ?  111 MET   A C     1 
ATOM   920  O  O     . MET   A 1 112 ? 23.73700 -1.97600  12.61300  1.000 26.93091 ?  111 MET   A O     1 
ATOM   921  C  CB    . MET   A 1 112 ? 25.66900 0.67700   13.76200  1.000 36.56489 ?  111 MET   A CB    1 
ATOM   922  C  CG    . MET   A 1 112 ? 26.93800 -0.03800  13.48200  1.000 39.55833 ?  111 MET   A CG    1 
ATOM   923  S  SD    . MET   A 1 112 ? 28.34500 1.15700   13.64700  1.000 35.22308 ?  111 MET   A SD    1 
ATOM   924  C  CE    . MET   A 1 112 ? 28.74400 1.13600   15.38800  1.000 36.96463 ?  111 MET   A CE    1 
ATOM   925  N  N     . VAL   A 1 113 ? 23.39200 0.11200   11.81100  1.000 23.28661 ?  112 VAL   A N     1 
ATOM   926  C  CA    . VAL   A 1 113 ? 22.85300 -0.25000  10.50900  1.000 24.91236 ?  112 VAL   A CA    1 
ATOM   927  C  C     . VAL   A 1 113 ? 23.51500 0.65800   9.50600   1.000 25.30156 ?  112 VAL   A C     1 
ATOM   928  O  O     . VAL   A 1 113 ? 23.61500 1.86700   9.74600   1.000 24.56262 ?  112 VAL   A O     1 
ATOM   929  C  CB    . VAL   A 1 113 ? 21.32300 -0.07700  10.43400  1.000 23.90188 ?  112 VAL   A CB    1 
ATOM   930  C  CG1   . VAL   A 1 113 ? 20.82100 -0.36200  8.99900   1.000 24.46060 ?  112 VAL   A CG1   1 
ATOM   931  C  CG2   . VAL   A 1 113 ? 20.67200 -0.99900  11.40400  1.000 24.61276 ?  112 VAL   A CG2   1 
ATOM   932  N  N     . LEU   A 1 114 ? 24.04600 0.06700   8.44400   1.000 24.67561 ?  113 LEU   A N     1 
ATOM   933  C  CA    . LEU   A 1 114 ? 24.58100 0.81700   7.33000   1.000 23.85877 ?  113 LEU   A CA    1 
ATOM   934  C  C     . LEU   A 1 114 ? 23.45200 1.12400   6.36000   1.000 24.25177 ?  113 LEU   A C     1 
ATOM   935  O  O     . LEU   A 1 114 ? 22.71700 0.22200   5.94600   1.000 28.32812 ?  113 LEU   A O     1 
ATOM   936  C  CB    . LEU   A 1 114 ? 25.69700 0.02700   6.63500   1.000 26.99595 ?  113 LEU   A CB    1 
ATOM   937  C  CG    . LEU   A 1 114 ? 26.33500 0.71100   5.42300   1.000 26.95846 ?  113 LEU   A CG    1 
ATOM   938  C  CD1   . LEU   A 1 114 ? 27.09200 1.98400   5.82700   1.000 28.39539 ?  113 LEU   A CD1   1 
ATOM   939  C  CD2   . LEU   A 1 114 ? 27.26700 -0.28700  4.68800   1.000 32.27404 ?  113 LEU   A CD2   1 
ATOM   940  N  N     . VAL   A 1 115 ? 23.34100 2.38500   5.97200   1.000 24.03093 ?  114 VAL   A N     1 
ATOM   941  C  CA    . VAL   A 1 115 ? 22.23700 2.87000   5.14300   1.000 24.33011 ?  114 VAL   A CA    1 
ATOM   942  C  C     . VAL   A 1 115 ? 22.81200 3.55600   3.91100   1.000 24.43894 ?  114 VAL   A C     1 
ATOM   943  O  O     . VAL   A 1 115 ? 23.53000 4.55800   4.03600   1.000 25.23515 ?  114 VAL   A O     1 
ATOM   944  C  CB    . VAL   A 1 115 ? 21.33900 3.86400   5.90700   1.000 23.96687 ?  114 VAL   A CB    1 
ATOM   945  C  CG1   . VAL   A 1 115 ? 20.20500 4.36100   5.02900   1.000 24.28611 ?  114 VAL   A CG1   1 
ATOM   946  C  CG2   . VAL   A 1 115 ? 20.77400 3.20800   7.15800   1.000 23.90554 ?  114 VAL   A CG2   1 
ATOM   947  N  N     . GLY   A 1 116 ? 22.42600 3.07600   2.74100   1.000 25.18038 ?  115 GLY   A N     1 
ATOM   948  C  CA    . GLY   A 1 116 ? 22.76400 3.70000   1.47500   1.000 27.00155 ?  115 GLY   A CA    1 
ATOM   949  C  C     . GLY   A 1 116 ? 21.54800 4.45300   0.96900   1.000 25.39475 ?  115 GLY   A C     1 
ATOM   950  O  O     . GLY   A 1 116 ? 20.61200 3.84300   0.44600   1.000 25.92801 ?  115 GLY   A O     1 
ATOM   951  N  N     . ASN   A 1 117 ? 21.53700 5.76800   1.16100   1.000 24.93110 ?  116 ASN   A N     1 
ATOM   952  C  CA    . ASN   A 1 117 ? 20.40400 6.61500   0.82300   1.000 24.96279 ?  116 ASN   A CA    1 
ATOM   953  C  C     . ASN   A 1 117 ? 20.50600 7.15100   -0.61600  1.000 25.96955 ?  116 ASN   A C     1 
ATOM   954  O  O     . ASN   A 1 117 ? 21.53600 7.04500   -1.27900  1.000 28.98258 ?  116 ASN   A O     1 
ATOM   955  C  CB    . ASN   A 1 117 ? 20.30700 7.76000   1.84100   1.000 24.29169 ?  116 ASN   A CB    1 
ATOM   956  C  CG    . ASN   A 1 117 ? 19.01000 8.53800   1.71300   1.000 24.54731 ?  116 ASN   A CG    1 
ATOM   957  O  OD1   . ASN   A 1 117 ? 17.93100 7.94600   1.57400   1.000 24.70265 ?  116 ASN   A OD1   1 
ATOM   958  N  ND2   . ASN   A 1 117 ? 19.10600 9.86500   1.72900   1.000 23.90753 ?  116 ASN   A ND2   1 
ATOM   959  N  N     . LYS   A 1 118 ? 19.39600 7.73700   -1.08600  1.000 27.83870 ?  117 LYS   A N     1 
ATOM   960  C  CA    . LYS   A 1 118 ? 19.22700 8.31900   -2.42300  1.000 29.10523 ?  117 LYS   A CA    1 
ATOM   961  C  C     . LYS   A 1 118 ? 19.18300 7.26400   -3.52200  1.000 33.91309 ?  117 LYS   A C     1 
ATOM   962  O  O     . LYS   A 1 118 ? 19.63400 7.51900   -4.64000  1.000 29.90880 ?  117 LYS   A O     1 
ATOM   963  C  CB    . LYS   A 1 118 ? 20.30900 9.35700   -2.75600  1.000 27.33138 ?  117 LYS   A CB    1 
ATOM   964  C  CG    . LYS   A 1 118 ? 20.58900 10.34900  -1.62600  1.000 25.13266 ?  117 LYS   A CG    1 
ATOM   965  C  CD    . LYS   A 1 118 ? 21.06800 11.67500  -2.13100  1.000 24.58118 ?  117 LYS   A CD    1 
ATOM   966  C  CE    . LYS   A 1 118 ? 21.58600 12.53600  -0.95800  1.000 23.83126 ?  117 LYS   A CE    1 
ATOM   967  N  NZ    . LYS   A 1 118 ? 21.98400 13.91000  -1.38000  1.000 27.92826 ?  117 LYS   A NZ    1 
ATOM   968  N  N     A CYS   A 1 119 ? 18.62800 6.08600   -3.22600  0.500 29.76727 ?  118 CYS   A N     1 
ATOM   969  N  N     B CYS   A 1 119 ? 18.62700 6.08500   -3.23800  0.500 29.77274 ?  118 CYS   A N     1 
ATOM   970  C  CA    A CYS   A 1 119 ? 18.56400 5.01500   -4.21900  0.500 30.53973 ?  118 CYS   A CA    1 
ATOM   971  C  CA    B CYS   A 1 119 ? 18.57500 5.03100   -4.24900  0.500 30.54055 ?  118 CYS   A CA    1 
ATOM   972  C  C     A CYS   A 1 119 ? 17.56200 5.29300   -5.33400  0.500 34.28948 ?  118 CYS   A C     1 
ATOM   973  C  C     B CYS   A 1 119 ? 17.59400 5.32300   -5.37100  0.500 34.30168 ?  118 CYS   A C     1 
ATOM   974  O  O     A CYS   A 1 119 ? 17.46100 4.48400   -6.26500  0.500 36.15231 ?  118 CYS   A O     1 
ATOM   975  O  O     B CYS   A 1 119 ? 17.52500 4.54700   -6.33200  0.500 36.16181 ?  118 CYS   A O     1 
ATOM   976  C  CB    A CYS   A 1 119 ? 18.24100 3.68100   -3.54000  0.500 29.79798 ?  118 CYS   A CB    1 
ATOM   977  C  CB    B CYS   A 1 119 ? 18.21800 3.70300   -3.60400  0.500 29.79783 ?  118 CYS   A CB    1 
ATOM   978  S  SG    A CYS   A 1 119 ? 16.54900 3.50200   -2.89900  0.500 35.80150 ?  118 CYS   A SG    1 
ATOM   979  S  SG    B CYS   A 1 119 ? 19.53000 3.07000   -2.60100  0.500 39.78796 ?  118 CYS   A SG    1 
ATOM   980  N  N     . ASP   A 1 120 ? 16.83000 6.40400   -5.27100  1.000 36.53312 ?  119 ASP   A N     1 
ATOM   981  C  CA    . ASP   A 1 120 ? 16.00500 6.83200   -6.38400  1.000 37.21654 ?  119 ASP   A CA    1 
ATOM   982  C  C     . ASP   A 1 120 ? 16.82400 7.48500   -7.49000  1.000 39.30802 ?  119 ASP   A C     1 
ATOM   983  O  O     . ASP   A 1 120 ? 16.27700 7.71800   -8.57500  1.000 40.50145 ?  119 ASP   A O     1 
ATOM   984  C  CB    . ASP   A 1 120 ? 14.95500 7.82600   -5.90900  1.000 32.48130 ?  119 ASP   A CB    1 
ATOM   985  C  CG    . ASP   A 1 120 ? 15.58000 8.99600   -5.24200  1.000 34.17720 ?  119 ASP   A CG    1 
ATOM   986  O  OD1   . ASP   A 1 120 ? 16.10400 8.79800   -4.10800  1.000 32.35817 -1 119 ASP   A OD1   1 
ATOM   987  O  OD2   . ASP   A 1 120 ? 15.61500 10.08100  -5.86500  1.000 34.75394 ?  119 ASP   A OD2   1 
ATOM   988  N  N     . LEU   A 1 121 ? 18.11000 7.79700   -7.23600  1.000 36.19109 ?  120 LEU   A N     1 
ATOM   989  C  CA    . LEU   A 1 121 ? 18.86800 8.61600   -8.18800  1.000 42.58633 ?  120 LEU   A CA    1 
ATOM   990  C  C     . LEU   A 1 121 ? 19.59500 7.74100   -9.20000  1.000 40.13115 ?  120 LEU   A C     1 
ATOM   991  O  O     . LEU   A 1 121 ? 20.11300 6.68400   -8.84600  1.000 45.17328 ?  120 LEU   A O     1 
ATOM   992  C  CB    . LEU   A 1 121 ? 19.89400 9.49500   -7.47300  1.000 41.57908 ?  120 LEU   A CB    1 
ATOM   993  C  CG    . LEU   A 1 121 ? 19.31800 10.65000  -6.64800  1.000 36.77577 ?  120 LEU   A CG    1 
ATOM   994  C  CD1   . LEU   A 1 121 ? 20.42200 11.51800  -6.08800  1.000 37.52783 ?  120 LEU   A CD1   1 
ATOM   995  C  CD2   . LEU   A 1 121 ? 18.34100 11.48400  -7.48000  1.000 37.81839 ?  120 LEU   A CD2   1 
ATOM   996  N  N     . PRO   A 1 122 ? 19.66700 8.20400   -10.45000 1.000 45.47418 ?  121 PRO   A N     1 
ATOM   997  C  CA    . PRO   A 1 122 ? 20.39200 7.43200   -11.47700 1.000 47.42890 ?  121 PRO   A CA    1 
ATOM   998  C  C     . PRO   A 1 122 ? 21.91600 7.49500   -11.34900 1.000 45.43640 ?  121 PRO   A C     1 
ATOM   999  O  O     . PRO   A 1 122 ? 22.60600 6.54100   -11.73700 1.000 51.13879 ?  121 PRO   A O     1 
ATOM   1000 C  CB    . PRO   A 1 122 ? 19.90700 8.07700   -12.78200 1.000 46.07299 ?  121 PRO   A CB    1 
ATOM   1001 C  CG    . PRO   A 1 122 ? 19.61800 9.49400   -12.40000 1.000 44.33075 ?  121 PRO   A CG    1 
ATOM   1002 C  CD    . PRO   A 1 122 ? 19.10200 9.45700   -10.97700 1.000 42.53595 ?  121 PRO   A CD    1 
ATOM   1003 N  N     . SER   A 1 123 ? 22.46500 8.57700   -10.80500 1.000 50.85654 ?  122 SER   A N     1 
ATOM   1004 C  CA    . SER   A 1 123 ? 23.90600 8.81200   -10.83000 1.000 53.34019 ?  122 SER   A CA    1 
ATOM   1005 C  C     . SER   A 1 123 ? 24.66700 7.97400   -9.80900  1.000 51.13835 ?  122 SER   A C     1 
ATOM   1006 O  O     . SER   A 1 123 ? 25.53700 8.49200   -9.10300  1.000 54.00008 ?  122 SER   A O     1 
ATOM   1007 C  CB    . SER   A 1 123 ? 24.18500 10.29800  -10.59200 1.000 51.85933 ?  122 SER   A CB    1 
ATOM   1008 O  OG    . SER   A 1 123 ? 23.37800 10.80100  -9.53400  1.000 56.19639 ?  122 SER   A OG    1 
ATOM   1009 N  N     . ARG   A 1 124 ? 24.38300 6.67700   -9.75800  1.000 52.78374 ?  123 ARG   A N     1 
ATOM   1010 C  CA    . ARG   A 1 124 ? 24.90900 5.81500   -8.70900  1.000 43.20678 ?  123 ARG   A CA    1 
ATOM   1011 C  C     . ARG   A 1 124 ? 26.40200 5.56000   -8.88600  1.000 47.99403 ?  123 ARG   A C     1 
ATOM   1012 O  O     . ARG   A 1 124 ? 26.84600 5.15100   -9.96300  1.000 53.11712 ?  123 ARG   A O     1 
ATOM   1013 C  CB    . ARG   A 1 124 ? 24.14900 4.49600   -8.72100  1.000 48.17171 ?  123 ARG   A CB    1 
ATOM   1014 C  CG    . ARG   A 1 124 ? 24.72800 3.44400   -7.84300  1.000 46.20356 ?  123 ARG   A CG    1 
ATOM   1015 C  CD    . ARG   A 1 124 ? 23.69500 2.38300   -7.54300  1.000 44.00812 ?  123 ARG   A CD    1 
ATOM   1016 N  NE    . ARG   A 1 124 ? 24.00200 1.75800   -6.26500  1.000 48.44712 ?  123 ARG   A NE    1 
ATOM   1017 C  CZ    . ARG   A 1 124 ? 23.10700 1.19900   -5.46500  1.000 51.23332 ?  123 ARG   A CZ    1 
ATOM   1018 N  NH1   . ARG   A 1 124 ? 21.82200 1.14900   -5.79000  1.000 49.42710 ?  123 ARG   A NH1   1 
ATOM   1019 N  NH2   . ARG   A 1 124 ? 23.50700 0.69100   -4.30100  1.000 47.24114 ?  123 ARG   A NH2   1 
ATOM   1020 N  N     . THR   A 1 125 ? 27.18400 5.78600   -7.81800  1.000 42.41482 ?  124 THR   A N     1 
ATOM   1021 C  CA    . THR   A 1 125 ? 28.62100 5.54900   -7.86900  1.000 41.97073 ?  124 THR   A CA    1 
ATOM   1022 C  C     . THR   A 1 125 ? 29.11400 4.54800   -6.83600  1.000 49.55529 ?  124 THR   A C     1 
ATOM   1023 O  O     . THR   A 1 125 ? 30.29200 4.17500   -6.87900  1.000 43.93330 ?  124 THR   A O     1 
ATOM   1024 C  CB    . THR   A 1 125 ? 29.40900 6.87000   -7.71800  1.000 40.15959 ?  124 THR   A CB    1 
ATOM   1025 O  OG1   . THR   A 1 125 ? 29.07800 7.52200   -6.48200  1.000 42.22992 ?  124 THR   A OG1   1 
ATOM   1026 C  CG2   . THR   A 1 125 ? 29.11300 7.81100   -8.87200  1.000 48.48828 ?  124 THR   A CG2   1 
ATOM   1027 N  N     . VAL   A 1 126 ? 28.26200 4.09600   -5.91800  1.000 41.14896 ?  125 VAL   A N     1 
ATOM   1028 C  CA    . VAL   A 1 126 ? 28.63100 3.08700   -4.94000  1.000 40.63421 ?  125 VAL   A CA    1 
ATOM   1029 C  C     . VAL   A 1 126 ? 27.78900 1.84800   -5.21500  1.000 47.05689 ?  125 VAL   A C     1 
ATOM   1030 O  O     . VAL   A 1 126 ? 26.55100 1.90900   -5.16800  1.000 43.95488 ?  125 VAL   A O     1 
ATOM   1031 C  CB    . VAL   A 1 126 ? 28.44100 3.59100   -3.49800  1.000 34.87276 ?  125 VAL   A CB    1 
ATOM   1032 C  CG1   . VAL   A 1 126 ? 28.69900 2.45300   -2.50000  1.000 35.02157 ?  125 VAL   A CG1   1 
ATOM   1033 C  CG2   . VAL   A 1 126 ? 29.35300 4.79600   -3.23200  1.000 39.85464 ?  125 VAL   A CG2   1 
ATOM   1034 N  N     . ASP   A 1 127 ? 28.46300 0.73300   -5.51500  1.000 45.93563 ?  126 ASP   A N     1 
ATOM   1035 C  CA    . ASP   A 1 127 ? 27.78900 -0.51300  -5.85600  1.000 49.54348 ?  126 ASP   A CA    1 
ATOM   1036 C  C     . ASP   A 1 127 ? 27.10400 -1.11600  -4.64100  1.000 44.14404 ?  126 ASP   A C     1 
ATOM   1037 O  O     . ASP   A 1 127 ? 27.62900 -1.06600  -3.52300  1.000 46.28637 ?  126 ASP   A O     1 
ATOM   1038 C  CB    . ASP   A 1 127 ? 28.78300 -1.55000  -6.39900  1.000 46.02224 ?  126 ASP   A CB    1 
ATOM   1039 C  CG    . ASP   A 1 127 ? 29.28100 -1.23300  -7.79200  1.000 56.15834 ?  126 ASP   A CG    1 
ATOM   1040 O  OD1   . ASP   A 1 127 ? 29.04200 -0.10500  -8.28300  1.000 60.89018 ?  126 ASP   A OD1   1 
ATOM   1041 O  OD2   . ASP   A 1 127 ? 29.91600 -2.12900  -8.39900  1.000 61.28464 -1 126 ASP   A OD2   1 
ATOM   1042 N  N     . THR   A 1 128 ? 25.95000 -1.74300  -4.88000  1.000 45.71675 ?  127 THR   A N     1 
ATOM   1043 C  CA    . THR   A 1 128 ? 25.30000 -2.53000  -3.83700  1.000 45.94542 ?  127 THR   A CA    1 
ATOM   1044 C  C     . THR   A 1 128 ? 26.27500 -3.51700  -3.21200  1.000 45.54861 ?  127 THR   A C     1 
ATOM   1045 O  O     . THR   A 1 128 ? 26.35800 -3.64100  -1.98400  1.000 39.48649 ?  127 THR   A O     1 
ATOM   1046 C  CB    . THR   A 1 128 ? 24.08500 -3.25800  -4.41600  1.000 47.72233 ?  127 THR   A CB    1 
ATOM   1047 O  OG1   . THR   A 1 128 ? 23.12700 -2.29300  -4.86100  1.000 56.55470 ?  127 THR   A OG1   1 
ATOM   1048 C  CG2   . THR   A 1 128 ? 23.43900 -4.15000  -3.37200  1.000 51.53060 ?  127 THR   A CG2   1 
ATOM   1049 N  N     . LYS   A 1 129 ? 27.06000 -4.20100  -4.04900  1.000 46.97147 ?  128 LYS   A N     1 
ATOM   1050 C  CA    . LYS   A 1 129 ? 27.97800 -5.20700  -3.53200  1.000 41.67318 ?  128 LYS   A CA    1 
ATOM   1051 C  C     . LYS   A 1 129 ? 29.06900 -4.58300  -2.66200  1.000 39.54095 ?  128 LYS   A C     1 
ATOM   1052 O  O     . LYS   A 1 129 ? 29.52700 -5.20200  -1.70000  1.000 44.90864 ?  128 LYS   A O     1 
ATOM   1053 C  CB    . LYS   A 1 129 ? 28.58600 -5.99700  -4.69300  1.000 46.64100 ?  128 LYS   A CB    1 
ATOM   1054 C  CG    . LYS   A 1 129 ? 29.46000 -7.17200  -4.25100  1.000 49.81206 ?  128 LYS   A CG    1 
ATOM   1055 C  CD    . LYS   A 1 129 ? 29.61500 -8.21900  -5.36400  1.000 49.92100 ?  128 LYS   A CD    1 
ATOM   1056 C  CE    . LYS   A 1 129 ? 30.38400 -9.43100  -4.86100  1.000 49.65965 ?  128 LYS   A CE    1 
ATOM   1057 N  NZ    . LYS   A 1 129 ? 31.59200 -8.98500  -4.09800  1.000 52.07321 ?  128 LYS   A NZ    1 
ATOM   1058 N  N     . GLN   A 1 130 ? 29.50000 -3.36100  -2.98300  1.000 41.98832 ?  129 GLN   A N     1 
ATOM   1059 C  CA    . GLN   A 1 130 ? 30.48200 -2.68700  -2.13800  1.000 39.86444 ?  129 GLN   A CA    1 
ATOM   1060 C  C     . GLN   A 1 130 ? 29.96200 -2.49200  -0.72000  1.000 38.43347 ?  129 GLN   A C     1 
ATOM   1061 O  O     . GLN   A 1 130 ? 30.70100 -2.67500  0.25600   1.000 39.14988 ?  129 GLN   A O     1 
ATOM   1062 C  CB    . GLN   A 1 130 ? 30.83700 -1.32700  -2.72200  1.000 44.89854 ?  129 GLN   A CB    1 
ATOM   1063 C  CG    . GLN   A 1 130 ? 31.76100 -1.34500  -3.89800  1.000 49.92785 ?  129 GLN   A CG    1 
ATOM   1064 C  CD    . GLN   A 1 130 ? 31.94500 0.04700   -4.44100  1.000 48.75497 ?  129 GLN   A CD    1 
ATOM   1065 O  OE1   . GLN   A 1 130 ? 31.37500 0.39700   -5.47500  1.000 49.15138 ?  129 GLN   A OE1   1 
ATOM   1066 N  NE2   . GLN   A 1 130 ? 32.72100 0.86900   -3.72500  1.000 50.27681 ?  129 GLN   A NE2   1 
ATOM   1067 N  N     . ALA   A 1 131 ? 28.70200 -2.08000  -0.58900  1.000 38.10227 ?  130 ALA   A N     1 
ATOM   1068 C  CA    . ALA   A 1 131 ? 28.15800 -1.76500  0.72700   1.000 34.38649 ?  130 ALA   A CA    1 
ATOM   1069 C  C     . ALA   A 1 131 ? 27.84700 -3.03400  1.50100   1.000 34.30708 ?  130 ALA   A C     1 
ATOM   1070 O  O     . ALA   A 1 131 ? 28.12900 -3.10400  2.70300   1.000 34.01562 ?  130 ALA   A O     1 
ATOM   1071 C  CB    . ALA   A 1 131 ? 26.90400 -0.89700  0.58700   1.000 36.10507 ?  130 ALA   A CB    1 
ATOM   1072 N  N     . GLN   A 1 132 ? 27.29400 -4.04800  0.81800   1.000 37.15466 ?  131 GLN   A N     1 
ATOM   1073 C  CA    . GLN   A 1 132 ? 27.05400 -5.33700  1.46000   1.000 41.91277 ?  131 GLN   A CA    1 
ATOM   1074 C  C     . GLN   A 1 132 ? 28.34700 -5.91600  2.01000   1.000 42.14078 ?  131 GLN   A C     1 
ATOM   1075 O  O     . GLN   A 1 132 ? 28.36600 -6.46800  3.11800   1.000 44.54277 ?  131 GLN   A O     1 
ATOM   1076 C  CB    . GLN   A 1 132 ? 26.42000 -6.32300  0.47100   1.000 44.51378 ?  131 GLN   A CB    1 
ATOM   1077 C  CG    . GLN   A 1 132 ? 24.99400 -5.99600  0.05400   1.000 46.28634 ?  131 GLN   A CG    1 
ATOM   1078 C  CD    . GLN   A 1 132 ? 24.43300 -6.95900  -0.99700  1.000 50.96944 ?  131 GLN   A CD    1 
ATOM   1079 O  OE1   . GLN   A 1 132 ? 25.17200 -7.74000  -1.60900  1.000 57.70977 ?  131 GLN   A OE1   1 
ATOM   1080 N  NE2   . GLN   A 1 132 ? 23.11900 -6.90400  -1.20800  1.000 48.58278 ?  131 GLN   A NE2   1 
ATOM   1081 N  N     . ASP   A 1 133 ? 29.43800 -5.80600  1.24600   1.000 42.78732 ?  132 ASP   A N     1 
ATOM   1082 C  CA    . ASP   A 1 133 ? 30.71600 -6.33700  1.71100   1.000 45.15267 ?  132 ASP   A CA    1 
ATOM   1083 C  C     . ASP   A 1 133 ? 31.21400 -5.57000  2.93100   1.000 42.10553 ?  132 ASP   A C     1 
ATOM   1084 O  O     . ASP   A 1 133 ? 31.65300 -6.17500  3.91700   1.000 42.80373 ?  132 ASP   A O     1 
ATOM   1085 C  CB    . ASP   A 1 133 ? 31.74900 -6.29900  0.57700   1.000 45.77809 ?  132 ASP   A CB    1 
ATOM   1086 C  CG    . ASP   A 1 133 ? 31.43000 -7.28400  -0.55400  1.000 51.12796 ?  132 ASP   A CG    1 
ATOM   1087 O  OD1   . ASP   A 1 133 ? 30.55800 -8.16600  -0.37000  1.000 51.60671 ?  132 ASP   A OD1   1 
ATOM   1088 O  OD2   . ASP   A 1 133 ? 32.05500 -7.16900  -1.64000  1.000 54.83104 -1 132 ASP   A OD2   1 
ATOM   1089 N  N     . LEU   A 1 134 ? 31.11300 -4.23700  2.91000   1.000 41.48893 ?  133 LEU   A N     1 
ATOM   1090 C  CA    . LEU   A 1 134 ? 31.51800 -3.47300  4.08400   1.000 39.35790 ?  133 LEU   A CA    1 
ATOM   1091 C  C     . LEU   A 1 134 ? 30.65100 -3.83100  5.28800   1.000 34.17380 ?  133 LEU   A C     1 
ATOM   1092 O  O     . LEU   A 1 134 ? 31.16500 -4.08800  6.38200   1.000 39.65959 ?  133 LEU   A O     1 
ATOM   1093 C  CB    . LEU   A 1 134 ? 31.47400 -1.97500  3.79400   1.000 37.45546 ?  133 LEU   A CB    1 
ATOM   1094 C  CG    . LEU   A 1 134 ? 32.04200 -1.10700  4.91600   1.000 37.21571 ?  133 LEU   A CG    1 
ATOM   1095 C  CD1   . LEU   A 1 134 ? 33.56000 -1.25500  4.97200   1.000 39.24848 ?  133 LEU   A CD1   1 
ATOM   1096 C  CD2   . LEU   A 1 134 ? 31.64100 0.35500   4.77600   1.000 38.86918 ?  133 LEU   A CD2   1 
ATOM   1097 N  N     . ALA   A 1 135 ? 29.33100 -3.87300  5.09900   1.000 40.40257 ?  134 ALA   A N     1 
ATOM   1098 C  CA    . ALA   A 1 135 ? 28.44000 -4.25800  6.19200   1.000 36.90912 ?  134 ALA   A CA    1 
ATOM   1099 C  C     . ALA   A 1 135 ? 28.81400 -5.63000  6.73500   1.000 38.26671 ?  134 ALA   A C     1 
ATOM   1100 O  O     . ALA   A 1 135 ? 28.88500 -5.83800  7.95500   1.000 35.65568 ?  134 ALA   A O     1 
ATOM   1101 C  CB    . ALA   A 1 135 ? 26.98800 -4.24900  5.69800   1.000 38.57043 ?  134 ALA   A CB    1 
ATOM   1102 N  N     . ARG   A 1 136 ? 29.04200 -6.59000  5.83800   1.000 39.15835 ?  135 ARG   A N     1 
ATOM   1103 C  CA    . ARG   A 1 136 ? 29.46200 -7.91600  6.28400   1.000 44.37072 ?  135 ARG   A CA    1 
ATOM   1104 C  C     . ARG   A 1 136 ? 30.75200 -7.82500  7.09800   1.000 37.05010 ?  135 ARG   A C     1 
ATOM   1105 O  O     . ARG   A 1 136 ? 30.83900 -8.36300  8.20900   1.000 40.72098 ?  135 ARG   A O     1 
ATOM   1106 C  CB    . ARG   A 1 136 ? 29.62500 -8.83800  5.07500   1.000 41.81029 ?  135 ARG   A CB    1 
ATOM   1107 C  CG    . ARG   A 1 136 ? 29.53200 -10.32100 5.42300   1.000 47.60246 ?  135 ARG   A CG    1 
ATOM   1108 C  CD    . ARG   A 1 136 ? 29.82100 -11.18500 4.21300   1.000 42.17009 ?  135 ARG   A CD    1 
ATOM   1109 N  NE    . ARG   A 1 136 ? 29.02000 -10.79100 3.06500   1.000 47.33787 ?  135 ARG   A NE    1 
ATOM   1110 C  CZ    . ARG   A 1 136 ? 29.52400 -10.28300 1.95000   1.000 51.11633 ?  135 ARG   A CZ    1 
ATOM   1111 N  NH1   . ARG   A 1 136 ? 30.82800 -10.11400 1.79900   1.000 55.83159 ?  135 ARG   A NH1   1 
ATOM   1112 N  NH2   . ARG   A 1 136 ? 28.70100 -9.95000  0.95800   1.000 51.86391 ?  135 ARG   A NH2   1 
ATOM   1113 N  N     . SER   A 1 137 ? 31.74600 -7.08400  6.59300   1.000 37.77835 ?  136 SER   A N     1 
ATOM   1114 C  CA    . SER   A 1 137 ? 32.99700 -6.94300  7.33900   1.000 42.01534 ?  136 SER   A CA    1 
ATOM   1115 C  C     . SER   A 1 137 ? 32.76300 -6.32900  8.71800   1.000 40.29476 ?  136 SER   A C     1 
ATOM   1116 O  O     . SER   A 1 137 ? 33.52800 -6.58700  9.65900   1.000 41.20694 ?  136 SER   A O     1 
ATOM   1117 C  CB    . SER   A 1 137 ? 33.99800 -6.11200  6.52900   1.000 39.98994 ?  136 SER   A CB    1 
ATOM   1118 O  OG    . SER   A 1 137 ? 33.95100 -4.73400  6.87700   1.000 43.49479 ?  136 SER   A OG    1 
ATOM   1119 N  N     . TYR   A 1 138 ? 31.69500 -5.54200  8.87700   1.000 40.53708 ?  137 TYR   A N     1 
ATOM   1120 C  CA    . TYR   A 1 138 ? 31.37200 -4.95000  10.16800  1.000 37.25913 ?  137 TYR   A CA    1 
ATOM   1121 C  C     . TYR   A 1 138 ? 30.46200 -5.82400  11.02700  1.000 35.29759 ?  137 TYR   A C     1 
ATOM   1122 O  O     . TYR   A 1 138 ? 30.32200 -5.56300  12.22500  1.000 35.27832 ?  137 TYR   A O     1 
ATOM   1123 C  CB    . TYR   A 1 138 ? 30.68400 -3.58700  9.98500   1.000 39.30837 ?  137 TYR   A CB    1 
ATOM   1124 C  CG    . TYR   A 1 138 ? 31.54000 -2.46300  9.43700   1.000 36.87717 ?  137 TYR   A CG    1 
ATOM   1125 C  CD1   . TYR   A 1 138 ? 32.93300 -2.53500  9.43300   1.000 43.41734 ?  137 TYR   A CD1   1 
ATOM   1126 C  CD2   . TYR   A 1 138 ? 30.94600 -1.33200  8.92400   1.000 35.89484 ?  137 TYR   A CD2   1 
ATOM   1127 C  CE1   . TYR   A 1 138 ? 33.69400 -1.48600  8.92800   1.000 42.57981 ?  137 TYR   A CE1   1 
ATOM   1128 C  CE2   . TYR   A 1 138 ? 31.67700 -0.29900  8.41600   1.000 42.62381 ?  137 TYR   A CE2   1 
ATOM   1129 C  CZ    . TYR   A 1 138 ? 33.05200 -0.36800  8.41600   1.000 41.94300 ?  137 TYR   A CZ    1 
ATOM   1130 O  OH    . TYR   A 1 138 ? 33.75600 0.70800   7.91300   1.000 40.62723 ?  137 TYR   A OH    1 
ATOM   1131 N  N     . GLY   A 1 139 ? 29.82200 -6.82900  10.44500  1.000 38.35468 ?  138 GLY   A N     1 
ATOM   1132 C  CA    . GLY   A 1 139 ? 28.82400 -7.59600  11.16400  1.000 37.98495 ?  138 GLY   A CA    1 
ATOM   1133 C  C     . GLY   A 1 139 ? 27.49600 -6.89300  11.37200  1.000 37.62055 ?  138 GLY   A C     1 
ATOM   1134 O  O     . GLY   A 1 139 ? 26.79100 -7.20000  12.33600  1.000 36.84337 ?  138 GLY   A O     1 
ATOM   1135 N  N     . ILE   A 1 140 ? 27.11300 -5.98700  10.47700  1.000 34.83652 ?  139 ILE   A N     1 
ATOM   1136 C  CA    . ILE   A 1 140 ? 25.89400 -5.20100  10.67700  1.000 35.41058 ?  139 ILE   A CA    1 
ATOM   1137 C  C     . ILE   A 1 140 ? 25.02800 -5.29900  9.42400   1.000 35.55131 ?  139 ILE   A C     1 
ATOM   1138 O  O     . ILE   A 1 140 ? 25.51200 -5.65800  8.34100   1.000 33.23868 ?  139 ILE   A O     1 
ATOM   1139 C  CB    . ILE   A 1 140 ? 26.21700 -3.72300  11.02100  1.000 28.84487 ?  139 ILE   A CB    1 
ATOM   1140 C  CG1   . ILE   A 1 140 ? 26.92900 -3.04500  9.83700   1.000 33.02532 ?  139 ILE   A CG1   1 
ATOM   1141 C  CG2   . ILE   A 1 140 ? 26.97400 -3.61500  12.33900  1.000 30.20327 ?  139 ILE   A CG2   1 
ATOM   1142 C  CD1   . ILE   A 1 140 ? 27.25900 -1.55500  10.07700  1.000 26.83850 ?  139 ILE   A CD1   1 
ATOM   1143 N  N     . PRO   A 1 141 ? 23.72600 -5.03200  9.54600   1.000 32.74874 ?  140 PRO   A N     1 
ATOM   1144 C  CA    . PRO   A 1 141 ? 22.87200 -5.03000  8.35500   1.000 30.13719 ?  140 PRO   A CA    1 
ATOM   1145 C  C     . PRO   A 1 141 ? 23.14600 -3.81800  7.47500   1.000 25.47024 ?  140 PRO   A C     1 
ATOM   1146 O  O     . PRO   A 1 141 ? 23.66200 -2.78900  7.92800   1.000 28.74141 ?  140 PRO   A O     1 
ATOM   1147 C  CB    . PRO   A 1 141 ? 21.44300 -4.97500  8.92600   1.000 33.35680 ?  140 PRO   A CB    1 
ATOM   1148 C  CG    . PRO   A 1 141 ? 21.56100 -5.35400  10.35000  1.000 32.85516 ?  140 PRO   A CG    1 
ATOM   1149 C  CD    . PRO   A 1 141 ? 22.94000 -4.91300  10.78700  1.000 31.90295 ?  140 PRO   A CD    1 
ATOM   1150 N  N     . PHE   A 1 142 ? 22.79100 -3.97700  6.19500   1.000 30.55169 ?  141 PHE   A N     1 
ATOM   1151 C  CA    . PHE   A 1 142 ? 22.81300 -2.93500  5.17100   1.000 29.80201 ?  141 PHE   A CA    1 
ATOM   1152 C  C     . PHE   A 1 142 ? 21.43400 -2.82000  4.54700   1.000 31.80291 ?  141 PHE   A C     1 
ATOM   1153 O  O     . PHE   A 1 142 ? 20.87000 -3.82400  4.09200   1.000 31.72884 ?  141 PHE   A O     1 
ATOM   1154 C  CB    . PHE   A 1 142 ? 23.83700 -3.24000  4.05900   1.000 34.10586 ?  141 PHE   A CB    1 
ATOM   1155 C  CG    . PHE   A 1 142 ? 23.68900 -2.35600  2.83700   1.000 33.47291 ?  141 PHE   A CG    1 
ATOM   1156 C  CD1   . PHE   A 1 142 ? 23.90200 -0.98400  2.92400   1.000 30.83765 ?  141 PHE   A CD1   1 
ATOM   1157 C  CD2   . PHE   A 1 142 ? 23.31900 -2.89400  1.60500   1.000 32.50597 ?  141 PHE   A CD2   1 
ATOM   1158 C  CE1   . PHE   A 1 142 ? 23.75200 -0.15300  1.80400   1.000 28.33421 ?  141 PHE   A CE1   1 
ATOM   1159 C  CE2   . PHE   A 1 142 ? 23.17200 -2.08400  0.48800   1.000 35.77336 ?  141 PHE   A CE2   1 
ATOM   1160 C  CZ    . PHE   A 1 142 ? 23.38800 -0.71400  0.58100   1.000 35.37950 ?  141 PHE   A CZ    1 
ATOM   1161 N  N     . ILE   A 1 143 ? 20.91900 -1.59100  4.47800   1.000 28.22223 ?  142 ILE   A N     1 
ATOM   1162 C  CA    . ILE   A 1 143 ? 19.60000 -1.29300  3.91800   1.000 30.50969 ?  142 ILE   A CA    1 
ATOM   1163 C  C     . ILE   A 1 143 ? 19.76700 -0.17100  2.90100   1.000 29.17296 ?  142 ILE   A C     1 
ATOM   1164 O  O     . ILE   A 1 143 ? 20.44400 0.82500   3.18700   1.000 32.07331 ?  142 ILE   A O     1 
ATOM   1165 C  CB    . ILE   A 1 143 ? 18.58100 -0.87800  5.00500   1.000 28.01124 ?  142 ILE   A CB    1 
ATOM   1166 C  CG1   . ILE   A 1 143 ? 18.55800 -1.91600  6.14800   1.000 32.91129 ?  142 ILE   A CG1   1 
ATOM   1167 C  CG2   . ILE   A 1 143 ? 17.15500 -0.75800  4.36900   1.000 32.16206 ?  142 ILE   A CG2   1 
ATOM   1168 C  CD1   . ILE   A 1 143 ? 17.88600 -3.21000  5.74400   1.000 38.61940 ?  142 ILE   A CD1   1 
ATOM   1169 N  N     . GLU   A 1 144 ? 19.17700 -0.33900  1.71200   1.000 28.39679 ?  143 GLU   A N     1 
ATOM   1170 C  CA    . GLU   A 1 144 ? 19.07900 0.73800   0.72400   1.000 30.57501 ?  143 GLU   A CA    1 
ATOM   1171 C  C     . GLU   A 1 144 ? 17.82800 1.56900   0.96200   1.000 30.27017 ?  143 GLU   A C     1 
ATOM   1172 O  O     . GLU   A 1 144 ? 16.73700 1.01900   1.17200   1.000 29.69096 ?  143 GLU   A O     1 
ATOM   1173 C  CB    . GLU   A 1 144 ? 19.01100 0.19200   -0.70600  1.000 31.82474 ?  143 GLU   A CB    1 
ATOM   1174 C  CG    . GLU   A 1 144 ? 20.19600 -0.61000  -1.13800  1.000 42.62378 ?  143 GLU   A CG    1 
ATOM   1175 C  CD    . GLU   A 1 144 ? 20.24600 -0.76000  -2.64900  1.000 50.71698 ?  143 GLU   A CD    1 
ATOM   1176 O  OE1   . GLU   A 1 144 ? 19.16800 -0.92000  -3.28000  1.000 55.22196 ?  143 GLU   A OE1   1 
ATOM   1177 O  OE2   . GLU   A 1 144 ? 21.37000 -0.69400  -3.20100  1.000 60.19214 -1 143 GLU   A OE2   1 
ATOM   1178 N  N     . THR   A 1 145 ? 17.96400 2.89600   0.87400   1.000 30.23472 ?  144 THR   A N     1 
ATOM   1179 C  CA    . THR   A 1 145 ? 16.79800 3.74600   1.13300   1.000 28.81069 ?  144 THR   A CA    1 
ATOM   1180 C  C     . THR   A 1 145 ? 16.67300 4.86900   0.12000   1.000 26.74975 ?  144 THR   A C     1 
ATOM   1181 O  O     . THR   A 1 145 ? 17.63500 5.25000   -0.55300  1.000 26.36872 ?  144 THR   A O     1 
ATOM   1182 C  CB    . THR   A 1 145 ? 16.83800 4.40600   2.52300   1.000 25.73707 ?  144 THR   A CB    1 
ATOM   1183 O  OG1   . THR   A 1 145 ? 17.95400 5.28000   2.59000   1.000 25.19609 ?  144 THR   A OG1   1 
ATOM   1184 C  CG2   . THR   A 1 145 ? 16.94800 3.37200   3.66700   1.000 25.69197 ?  144 THR   A CG2   1 
ATOM   1185 N  N     . SER   A 1 146 ? 15.47500 5.46100   0.09900   1.000 26.50365 ?  145 SER   A N     1 
ATOM   1186 C  CA    . SER   A 1 146 ? 15.23900 6.75500   -0.53000  1.000 26.32924 ?  145 SER   A CA    1 
ATOM   1187 C  C     . SER   A 1 146 ? 14.32400 7.54600   0.39100   1.000 25.93900 ?  145 SER   A C     1 
ATOM   1188 O  O     . SER   A 1 146 ? 13.17000 7.15800   0.59400   1.000 26.27504 ?  145 SER   A O     1 
ATOM   1189 C  CB    . SER   A 1 146 ? 14.59700 6.61200   -1.92700  1.000 27.03121 ?  145 SER   A CB    1 
ATOM   1190 O  OG    . SER   A 1 146 ? 14.21500 7.89800   -2.40200  1.000 26.89089 ?  145 SER   A OG    1 
ATOM   1191 N  N     . ALA   A 1 147 ? 14.82300 8.66500   0.92900   1.000 25.82293 ?  146 ALA   A N     1 
ATOM   1192 C  CA    . ALA   A 1 147 ? 13.95300 9.58600   1.63900   1.000 26.72203 ?  146 ALA   A CA    1 
ATOM   1193 C  C     . ALA   A 1 147 ? 12.93300 10.20400  0.69500   1.000 26.86524 ?  146 ALA   A C     1 
ATOM   1194 O  O     . ALA   A 1 147 ? 11.85500 10.63000  1.14100   1.000 26.67146 ?  146 ALA   A O     1 
ATOM   1195 C  CB    . ALA   A 1 147 ? 14.79300 10.66100  2.34300   1.000 24.23219 ?  146 ALA   A CB    1 
ATOM   1196 N  N     . LYS   A 1 148 ? 13.23500 10.21800  -0.60700  1.000 25.81994 ?  147 LYS   A N     1 
ATOM   1197 C  CA    . LYS   A 1 148 ? 12.34900 10.85800  -1.56900  1.000 32.11508 ?  147 LYS   A CA    1 
ATOM   1198 C  C     . LYS   A 1 148 ? 11.14800 9.98400   -1.89400  1.000 26.59659 ?  147 LYS   A C     1 
ATOM   1199 O  O     . LYS   A 1 148 ? 10.01600 10.47500  -1.93200  1.000 30.87700 ?  147 LYS   A O     1 
ATOM   1200 C  CB    . LYS   A 1 148 ? 13.11700 11.22200  -2.84300  1.000 26.06863 ?  147 LYS   A CB    1 
ATOM   1201 C  CG    . LYS   A 1 148 ? 12.24700 12.03300  -3.81000  1.000 30.36752 ?  147 LYS   A CG    1 
ATOM   1202 C  CD    . LYS   A 1 148 ? 13.00600 12.38800  -5.07000  1.000 33.00164 ?  147 LYS   A CD    1 
ATOM   1203 C  CE    . LYS   A 1 148 ? 12.04000 12.71400  -6.18200  1.000 34.58749 ?  147 LYS   A CE    1 
ATOM   1204 N  NZ    . LYS   A 1 148 ? 11.48400 14.08600  -5.97100  1.000 41.45663 ?  147 LYS   A NZ    1 
ATOM   1205 N  N     . THR   A 1 149 ? 11.36400 8.69200   -2.10800  1.000 27.27097 ?  148 THR   A N     1 
ATOM   1206 C  CA    . THR   A 1 149 ? 10.27800 7.78400   -2.44000  1.000 27.82932 ?  148 THR   A CA    1 
ATOM   1207 C  C     . THR   A 1 149 ? 9.73300  7.04100   -1.22400  1.000 27.83704 ?  148 THR   A C     1 
ATOM   1208 O  O     . THR   A 1 149 ? 8.72000  6.35200   -1.35800  1.000 28.45426 ?  148 THR   A O     1 
ATOM   1209 C  CB    . THR   A 1 149 ? 10.71500 6.73600   -3.49100  1.000 28.51770 ?  148 THR   A CB    1 
ATOM   1210 O  OG1   . THR   A 1 149 ? 11.64200 5.80100   -2.92600  1.000 30.52431 ?  148 THR   A OG1   1 
ATOM   1211 C  CG2   . THR   A 1 149 ? 11.33400 7.37900   -4.71100  1.000 33.09095 ?  148 THR   A CG2   1 
ATOM   1212 N  N     . ARG   A 1 150 ? 10.41300 7.11100   -0.06800  1.000 27.22935 ?  149 ARG   A N     1 
ATOM   1213 C  CA    . ARG   A 1 150 ? 10.14900 6.36900   1.17700   1.000 27.18708 ?  149 ARG   A CA    1 
ATOM   1214 C  C     . ARG   A 1 150 ? 10.63000 4.91600   1.11500   1.000 27.61942 ?  149 ARG   A C     1 
ATOM   1215 O  O     . ARG   A 1 150 ? 10.51100 4.19800   2.11600   1.000 27.66624 ?  149 ARG   A O     1 
ATOM   1216 C  CB    . ARG   A 1 150 ? 8.66900  6.39200   1.61500   1.000 27.71727 ?  149 ARG   A CB    1 
ATOM   1217 C  CG    . ARG   A 1 150 ? 8.06600  7.77100   1.55800   1.000 30.60843 ?  149 ARG   A CG    1 
ATOM   1218 C  CD    . ARG   A 1 150 ? 6.66500  7.84900   2.19700   1.000 29.84693 ?  149 ARG   A CD    1 
ATOM   1219 N  NE    . ARG   A 1 150 ? 6.83500  8.15800   3.59700   1.000 41.21502 ?  149 ARG   A NE    1 
ATOM   1220 C  CZ    . ARG   A 1 150 ? 6.88400  7.25700   4.55800   1.000 37.81727 ?  149 ARG   A CZ    1 
ATOM   1221 N  NH1   . ARG   A 1 150 ? 6.55800  5.99700   4.33700   1.000 42.16790 ?  149 ARG   A NH1   1 
ATOM   1222 N  NH2   . ARG   A 1 150 ? 7.30500  7.62400   5.76000   1.000 37.47025 ?  149 ARG   A NH2   1 
ATOM   1223 N  N     . GLN   A 1 151 ? 11.22800 4.46200   0.00800   1.000 27.98953 ?  150 GLN   A N     1 
ATOM   1224 C  CA    . GLN   A 1 151 ? 11.69600 3.08700   -0.03000  1.000 28.40945 ?  150 GLN   A CA    1 
ATOM   1225 C  C     . GLN   A 1 151 ? 12.66500 2.83200   1.12200   1.000 27.82830 ?  150 GLN   A C     1 
ATOM   1226 O  O     . GLN   A 1 151 ? 13.60500 3.59800   1.34000   1.000 28.17051 ?  150 GLN   A O     1 
ATOM   1227 C  CB    . GLN   A 1 151 ? 12.36500 2.78600   -1.37000  1.000 32.18974 ?  150 GLN   A CB    1 
ATOM   1228 C  CG    . GLN   A 1 151 ? 12.85200 1.35900   -1.49600  1.000 39.80116 ?  150 GLN   A CG    1 
ATOM   1229 C  CD    . GLN   A 1 151 ? 13.82200 1.20700   -2.65000  1.000 46.65864 ?  150 GLN   A CD    1 
ATOM   1230 O  OE1   . GLN   A 1 151 ? 13.62600 1.79300   -3.72400  1.000 45.19828 ?  150 GLN   A OE1   1 
ATOM   1231 N  NE2   . GLN   A 1 151 ? 14.89600 0.44300   -2.42700  1.000 46.57675 ?  150 GLN   A NE2   1 
ATOM   1232 N  N     . GLY   A 1 152 ? 12.39200 1.79200   1.89800   1.000 28.58095 ?  151 GLY   A N     1 
ATOM   1233 C  CA    . GLY   A 1 152 ? 13.29000 1.36100   2.93900   1.000 27.60978 ?  151 GLY   A CA    1 
ATOM   1234 C  C     . GLY   A 1 152 ? 13.33200 2.20100   4.20500   1.000 28.42044 ?  151 GLY   A C     1 
ATOM   1235 O  O     . GLY   A 1 152 ? 14.05700 1.81800   5.12600   1.000 28.88182 ?  151 GLY   A O     1 
ATOM   1236 N  N     . VAL   A 1 153 ? 12.58400 3.31300   4.30100   1.000 27.12286 ?  152 VAL   A N     1 
ATOM   1237 C  CA    . VAL   A 1 153 ? 12.78700 4.24000   5.42500   1.000 26.92018 ?  152 VAL   A CA    1 
ATOM   1238 C  C     . VAL   A 1 153 ? 12.41600 3.57400   6.75100   1.000 25.97990 ?  152 VAL   A C     1 
ATOM   1239 O  O     . VAL   A 1 153 ? 13.22500 3.52700   7.68500   1.000 25.52914 ?  152 VAL   A O     1 
ATOM   1240 C  CB    . VAL   A 1 153 ? 12.00000 5.54600   5.21700   1.000 26.59493 ?  152 VAL   A CB    1 
ATOM   1241 C  CG1   . VAL   A 1 153 ? 12.03500 6.39100   6.50600   1.000 25.18586 ?  152 VAL   A CG1   1 
ATOM   1242 C  CG2   . VAL   A 1 153 ? 12.57600 6.32500   4.03800   1.000 25.68027 ?  152 VAL   A CG2   1 
ATOM   1243 N  N     . ASP   A 1 154 ? 11.17200 3.09700   6.88300   1.000 26.51248 ?  153 ASP   A N     1 
ATOM   1244 C  CA    . ASP   A 1 154 ? 10.81000 2.37600   8.10500   1.000 29.09451 ?  153 ASP   A CA    1 
ATOM   1245 C  C     . ASP   A 1 154 ? 11.76000 1.22600   8.36000   1.000 28.82743 ?  153 ASP   A C     1 
ATOM   1246 O  O     . ASP   A 1 154 ? 12.16200 0.97500   9.50300   1.000 29.90486 ?  153 ASP   A O     1 
ATOM   1247 C  CB    . ASP   A 1 154 ? 9.37700  1.83300   8.02600   1.000 27.34365 ?  153 ASP   A CB    1 
ATOM   1248 C  CG    . ASP   A 1 154 ? 8.32000  2.94700   8.15200   1.000 37.50658 ?  153 ASP   A CG    1 
ATOM   1249 O  OD1   . ASP   A 1 154 ? 8.59000  3.98200   8.79100   1.000 43.96594 ?  153 ASP   A OD1   1 
ATOM   1250 O  OD2   . ASP   A 1 154 ? 7.21600  2.79200   7.60900   1.000 42.89510 -1 153 ASP   A OD2   1 
ATOM   1251 N  N     . ASP   A 1 155 ? 12.09600 0.48300   7.30700   1.000 27.49710 ?  154 ASP   A N     1 
ATOM   1252 C  CA    . ASP   A 1 155 ? 12.88500 -0.73100  7.48700   1.000 29.57996 ?  154 ASP   A CA    1 
ATOM   1253 C  C     . ASP   A 1 155 ? 14.25300 -0.41100  8.09200   1.000 26.49622 ?  154 ASP   A C     1 
ATOM   1254 O  O     . ASP   A 1 155 ? 14.74300 -1.13800  8.95900   1.000 28.40362 ?  154 ASP   A O     1 
ATOM   1255 C  CB    . ASP   A 1 155 ? 13.03400 -1.42600  6.13600   1.000 30.74880 ?  154 ASP   A CB    1 
ATOM   1256 C  CG    . ASP   A 1 155 ? 13.74600 -2.75600  6.22900   1.000 44.96839 ?  154 ASP   A CG    1 
ATOM   1257 O  OD1   . ASP   A 1 155 ? 13.70500 -3.39300  7.31300   1.000 50.61670 -1 154 ASP   A OD1   1 
ATOM   1258 O  OD2   . ASP   A 1 155 ? 14.33600 -3.17200  5.19600   1.000 49.82411 ?  154 ASP   A OD2   1 
ATOM   1259 N  N     . ALA   A 1 156 ? 14.85100 0.70000   7.66900   1.000 28.35499 ?  155 ALA   A N     1 
ATOM   1260 C  CA    . ALA   A 1 156 ? 16.14500 1.10400   8.20000   1.000 25.37997 ?  155 ALA   A CA    1 
ATOM   1261 C  C     . ALA   A 1 156 ? 16.05800 1.35500   9.70300   1.000 24.96736 ?  155 ALA   A C     1 
ATOM   1262 O  O     . ALA   A 1 156 ? 16.83900 0.80200   10.48800  1.000 24.75272 ?  155 ALA   A O     1 
ATOM   1263 C  CB    . ALA   A 1 156 ? 16.63700 2.33700   7.44000   1.000 25.04856 ?  155 ALA   A CB    1 
ATOM   1264 N  N     . PHE   A 1 157 ? 15.10000 2.18200   10.12900  1.000 24.88404 ?  156 PHE   A N     1 
ATOM   1265 C  CA    . PHE   A 1 157 ? 14.96300 2.46100   11.55200  1.000 24.55867 ?  156 PHE   A CA    1 
ATOM   1266 C  C     . PHE   A 1 157 ? 14.53400 1.22500   12.32100  1.000 24.94715 ?  156 PHE   A C     1 
ATOM   1267 O  O     . PHE   A 1 157 ? 15.06500 0.95600   13.40600  1.000 24.68355 ?  156 PHE   A O     1 
ATOM   1268 C  CB    . PHE   A 1 157 ? 13.97600 3.61600   11.79400  1.000 24.45206 ?  156 PHE   A CB    1 
ATOM   1269 C  CG    . PHE   A 1 157 ? 14.53500 4.95700   11.42700  1.000 23.94035 ?  156 PHE   A CG    1 
ATOM   1270 C  CD1   . PHE   A 1 157 ? 15.30700 5.69300   12.33100  1.000 23.36706 ?  156 PHE   A CD1   1 
ATOM   1271 C  CD2   . PHE   A 1 157 ? 14.29000 5.49700   10.16400  1.000 24.07010 ?  156 PHE   A CD2   1 
ATOM   1272 C  CE1   . PHE   A 1 157 ? 15.81800 6.95300   11.97400  1.000 22.93994 ?  156 PHE   A CE1   1 
ATOM   1273 C  CE2   . PHE   A 1 157 ? 14.82100 6.74500   9.82200   1.000 23.61960 ?  156 PHE   A CE2   1 
ATOM   1274 C  CZ    . PHE   A 1 157 ? 15.59900 7.45400   10.73500  1.000 23.05892 ?  156 PHE   A CZ    1 
ATOM   1275 N  N     . TYR   A 1 158 ? 13.59700 0.44000   11.77300  1.000 25.60980 ?  157 TYR   A N     1 
ATOM   1276 C  CA    . TYR   A 1 158 ? 13.12500 -0.72400  12.52300  1.000 26.21959 ?  157 TYR   A CA    1 
ATOM   1277 C  C     . TYR   A 1 158 ? 14.22500 -1.76500  12.66100  1.000 25.98951 ?  157 TYR   A C     1 
ATOM   1278 O  O     . TYR   A 1 158 ? 14.32000 -2.43400  13.69300  1.000 27.58102 ?  157 TYR   A O     1 
ATOM   1279 C  CB    . TYR   A 1 158 ? 11.90600 -1.38100  11.86000  1.000 26.83202 ?  157 TYR   A CB    1 
ATOM   1280 C  CG    . TYR   A 1 158 ? 10.62900 -0.59600  11.84700  1.000 30.12355 ?  157 TYR   A CG    1 
ATOM   1281 C  CD1   . TYR   A 1 158 ? 10.57000 0.72900   12.27300  1.000 28.71706 ?  157 TYR   A CD1   1 
ATOM   1282 C  CD2   . TYR   A 1 158 ? 9.47000  -1.17700  11.38300  1.000 32.14462 ?  157 TYR   A CD2   1 
ATOM   1283 C  CE1   . TYR   A 1 158 ? 9.39000  1.44900   12.23100  1.000 34.96867 ?  157 TYR   A CE1   1 
ATOM   1284 C  CE2   . TYR   A 1 158 ? 8.28500  -0.46100  11.33200  1.000 33.70995 ?  157 TYR   A CE2   1 
ATOM   1285 C  CZ    . TYR   A 1 158 ? 8.24500  0.84200   11.77000  1.000 34.73145 ?  157 TYR   A CZ    1 
ATOM   1286 O  OH    . TYR   A 1 158 ? 7.05000  1.53500   11.71400  1.000 38.67400 ?  157 TYR   A OH    1 
ATOM   1287 N  N     . THR   A 1 159 ? 15.03200 -1.95100  11.60900  1.000 25.98604 ?  158 THR   A N     1 
ATOM   1288 C  CA    . THR   A 1 159 ? 16.15500 -2.88000  11.70600  1.000 26.18277 ?  158 THR   A CA    1 
ATOM   1289 C  C     . THR   A 1 159 ? 17.11200 -2.46600  12.81000  1.000 25.25064 ?  158 THR   A C     1 
ATOM   1290 O  O     . THR   A 1 159 ? 17.63600 -3.31800  13.54800  1.000 27.36539 ?  158 THR   A O     1 
ATOM   1291 C  CB    . THR   A 1 159 ? 16.88400 -2.96900  10.36200  1.000 28.53064 ?  158 THR   A CB    1 
ATOM   1292 O  OG1   . THR   A 1 159 ? 15.96900 -3.46200  9.36600   1.000 28.50712 ?  158 THR   A OG1   1 
ATOM   1293 C  CG2   . THR   A 1 159 ? 18.07700 -3.90900  10.46900  1.000 29.19046 ?  158 THR   A CG2   1 
ATOM   1294 N  N     . LEU   A 1 160 ? 17.36900 -1.15900  12.93000  1.000 24.72754 ?  159 LEU   A N     1 
ATOM   1295 C  CA    . LEU   A 1 160 ? 18.25500 -0.68400  13.98800  1.000 24.13145 ?  159 LEU   A CA    1 
ATOM   1296 C  C     . LEU   A 1 160 ? 17.69200 -1.03200  15.35900  1.000 24.72085 ?  159 LEU   A C     1 
ATOM   1297 O  O     . LEU   A 1 160 ? 18.43200 -1.47000  16.24300  1.000 23.95935 ?  159 LEU   A O     1 
ATOM   1298 C  CB    . LEU   A 1 160 ? 18.49400 0.82400   13.83500  1.000 23.64843 ?  159 LEU   A CB    1 
ATOM   1299 C  CG    . LEU   A 1 160 ? 19.47100 1.35200   14.91500  1.000 23.07185 ?  159 LEU   A CG    1 
ATOM   1300 C  CD1   . LEU   A 1 160 ? 20.85000 0.64900   14.90400  1.000 23.38984 ?  159 LEU   A CD1   1 
ATOM   1301 C  CD2   . LEU   A 1 160 ? 19.64300 2.88400   14.69600  1.000 22.95883 ?  159 LEU   A CD2   1 
ATOM   1302 N  N     . VAL   A 1 161 ? 16.37200 -0.90800  15.54000  1.000 24.52702 ?  160 VAL   A N     1 
ATOM   1303 C  CA    . VAL   A 1 161 ? 15.75500 -1.31400  16.80700  1.000 24.68972 ?  160 VAL   A CA    1 
ATOM   1304 C  C     . VAL   A 1 161 ? 15.96700 -2.80300  17.06200  1.000 25.05190 ?  160 VAL   A C     1 
ATOM   1305 O  O     . VAL   A 1 161 ? 16.28700 -3.22000  18.18200  1.000 27.04764 ?  160 VAL   A O     1 
ATOM   1306 C  CB    . VAL   A 1 161 ? 14.26000 -0.94700  16.82200  1.000 25.09054 ?  160 VAL   A CB    1 
ATOM   1307 C  CG1   . VAL   A 1 161 ? 13.58700 -1.53400  18.05800  1.000 25.79906 ?  160 VAL   A CG1   1 
ATOM   1308 C  CG2   . VAL   A 1 161 ? 14.09900 0.56700   16.81100  1.000 24.67593 ?  160 VAL   A CG2   1 
ATOM   1309 N  N     . ARG   A 1 162 ? 15.79400 -3.62700  16.03400  1.000 25.77042 ?  161 ARG   A N     1 
ATOM   1310 C  CA    . ARG   A 1 162 ? 16.05800 -5.05300  16.19500  1.000 27.91421 ?  161 ARG   A CA    1 
ATOM   1311 C  C     . ARG   A 1 162 ? 17.49600 -5.31300  16.60900  1.000 31.65551 ?  161 ARG   A C     1 
ATOM   1312 O  O     . ARG   A 1 162 ? 17.76600 -6.20300  17.43200  1.000 32.81004 ?  161 ARG   A O     1 
ATOM   1313 C  CB    . ARG   A 1 162 ? 15.75400 -5.78800  14.89600  1.000 27.93816 ?  161 ARG   A CB    1 
ATOM   1314 C  CG    . ARG   A 1 162 ? 14.29500 -5.73600  14.55900  1.000 32.62791 ?  161 ARG   A CG    1 
ATOM   1315 C  CD    . ARG   A 1 162 ? 13.96200 -6.57400  13.32600  1.000 33.81941 ?  161 ARG   A CD    1 
ATOM   1316 N  NE    . ARG   A 1 162 ? 12.57300 -6.35500  12.96000  1.000 33.59205 ?  161 ARG   A NE    1 
ATOM   1317 C  CZ    . ARG   A 1 162 ? 12.17800 -5.64800  11.91500  1.000 34.93009 ?  161 ARG   A CZ    1 
ATOM   1318 N  NH1   . ARG   A 1 162 ? 13.04300 -5.18500  11.03100  1.000 36.66536 ?  161 ARG   A NH1   1 
ATOM   1319 N  NH2   . ARG   A 1 162 ? 10.87600 -5.42100  11.73800  1.000 37.44046 ?  161 ARG   A NH2   1 
ATOM   1320 N  N     . GLU   A 1 163 ? 18.44100 -4.56400  16.03700  1.000 29.95036 ?  162 GLU   A N     1 
ATOM   1321 C  CA    . GLU   A 1 163 ? 19.83900 -4.74400  16.42500  1.000 28.75666 ?  162 GLU   A CA    1 
ATOM   1322 C  C     . GLU   A 1 163 ? 20.04300 -4.40600  17.90400  1.000 30.07424 ?  162 GLU   A C     1 
ATOM   1323 O  O     . GLU   A 1 163 ? 20.75300 -5.12200  18.61700  1.000 31.23209 ?  162 GLU   A O     1 
ATOM   1324 C  CB    . GLU   A 1 163 ? 20.74600 -3.88000  15.54400  1.000 30.56870 ?  162 GLU   A CB    1 
ATOM   1325 C  CG    . GLU   A 1 163 ? 20.90400 -4.37600  14.11600  1.000 31.43648 ?  162 GLU   A CG    1 
ATOM   1326 C  CD    . GLU   A 1 163 ? 21.45600 -5.81000  14.03700  1.000 37.84735 ?  162 GLU   A CD    1 
ATOM   1327 O  OE1   . GLU   A 1 163 ? 22.59200 -6.07100  14.52200  1.000 38.66065 ?  162 GLU   A OE1   1 
ATOM   1328 O  OE2   . GLU   A 1 163 ? 20.74300 -6.67900  13.48900  1.000 36.99665 -1 162 GLU   A OE2   1 
ATOM   1329 N  N     . ILE   A 1 164 ? 19.45300 -3.29600  18.37100  1.000 28.77336 ?  163 ILE   A N     1 
ATOM   1330 C  CA    . ILE   A 1 164 ? 19.54500 -2.93300  19.78300  1.000 29.51882 ?  163 ILE   A CA    1 
ATOM   1331 C  C     . ILE   A 1 164 ? 18.90400 -4.01200  20.64300  1.000 32.70384 ?  163 ILE   A C     1 
ATOM   1332 O  O     . ILE   A 1 164 ? 19.43400 -4.38300  21.69700  1.000 35.00802 ?  163 ILE   A O     1 
ATOM   1333 C  CB    . ILE   A 1 164 ? 18.89000 -1.56400  20.04000  1.000 34.51887 ?  163 ILE   A CB    1 
ATOM   1334 C  CG1   . ILE   A 1 164 ? 19.68000 -0.43900  19.36200  1.000 23.57374 ?  163 ILE   A CG1   1 
ATOM   1335 C  CG2   . ILE   A 1 164 ? 18.73300 -1.30900  21.55800  1.000 28.81832 ?  163 ILE   A CG2   1 
ATOM   1336 C  CD1   . ILE   A 1 164 ? 18.88600 0.84300   19.30300  1.000 26.02789 ?  163 ILE   A CD1   1 
ATOM   1337 N  N     . ARG   A 1 165 ? 17.75200 -4.52400  20.20400  1.000 28.96751 ?  164 ARG   A N     1 
ATOM   1338 C  CA    . ARG   A 1 165 ? 17.04900 -5.55500  20.96400  1.000 34.30243 ?  164 ARG   A CA    1 
ATOM   1339 C  C     . ARG   A 1 165 ? 17.91400 -6.78500  21.17000  1.000 37.47106 ?  164 ARG   A C     1 
ATOM   1340 O  O     . ARG   A 1 165 ? 17.97100 -7.33300  22.27900  1.000 40.20587 ?  164 ARG   A O     1 
ATOM   1341 C  CB    . ARG   A 1 165 ? 15.75700 -5.93600  20.25600  1.000 31.00767 ?  164 ARG   A CB    1 
ATOM   1342 C  CG    . ARG   A 1 165 ? 14.60900 -5.07400  20.63200  1.000 33.79008 ?  164 ARG   A CG    1 
ATOM   1343 C  CD    . ARG   A 1 165 ? 13.37600 -5.41700  19.80100  1.000 33.65735 ?  164 ARG   A CD    1 
ATOM   1344 N  NE    . ARG   A 1 165 ? 12.25200 -4.55000  20.13700  1.000 37.69489 ?  164 ARG   A NE    1 
ATOM   1345 C  CZ    . ARG   A 1 165 ? 11.10500 -4.53400  19.46700  1.000 33.19309 ?  164 ARG   A CZ    1 
ATOM   1346 N  NH1   . ARG   A 1 165 ? 10.89600 -5.33800  18.44400  1.000 37.49784 ?  164 ARG   A NH1   1 
ATOM   1347 N  NH2   . ARG   A 1 165 ? 10.14800 -3.68800  19.83500  1.000 42.31679 ?  164 ARG   A NH2   1 
ATOM   1348 N  N     . LYS   A 1 166 ? 18.59700 -7.23500  20.11500  1.000 37.73003 ?  165 LYS   A N     1 
ATOM   1349 C  CA    . LYS   A 1 166 ? 19.46900 -8.39900  20.24400  1.000 41.30103 ?  165 LYS   A CA    1 
ATOM   1350 C  C     . LYS   A 1 166 ? 20.64300 -8.12500  21.17300  1.000 44.72646 ?  165 LYS   A C     1 
ATOM   1351 O  O     . LYS   A 1 166 ? 21.05700 -9.01500  21.92500  1.000 48.00528 ?  165 LYS   A O     1 
ATOM   1352 C  CB    . LYS   A 1 166 ? 19.94500 -8.84600  18.86300  1.000 42.39911 ?  165 LYS   A CB    1 
ATOM   1353 C  CG    . LYS   A 1 166 ? 18.79200 -9.33800  18.00100  1.000 38.93052 ?  165 LYS   A CG    1 
ATOM   1354 C  CD    . LYS   A 1 166 ? 19.24100 -9.94100  16.66200  1.000 49.98410 ?  165 LYS   A CD    1 
ATOM   1355 C  CE    . LYS   A 1 166 ? 20.18800 -9.02800  15.90600  1.000 43.62727 ?  165 LYS   A CE    1 
ATOM   1356 N  NZ    . LYS   A 1 166 ? 20.28600 -9.41400  14.46100  1.000 47.34270 ?  165 LYS   A NZ    1 
ATOM   1357 N  N     . HIS   A 1 167 ? 21.16100 -6.89600  21.15700  1.000 40.50354 ?  166 HIS   A N     1 
ATOM   1358 C  CA    . HIS   A 1 167 ? 22.26700 -6.51200  22.02600  1.000 40.34503 ?  166 HIS   A CA    1 
ATOM   1359 C  C     . HIS   A 1 167 ? 21.86100 -6.55200  23.49600  1.000 41.39564 ?  166 HIS   A C     1 
ATOM   1360 O  O     . HIS   A 1 167 ? 22.65100 -6.96500  24.35200  1.000 46.34234 ?  166 HIS   A O     1 
ATOM   1361 C  CB    . HIS   A 1 167 ? 22.74800 -5.11900  21.62100  1.000 39.39135 ?  166 HIS   A CB    1 
ATOM   1362 C  CG    . HIS   A 1 167 ? 23.81700 -4.54300  22.50400  1.000 40.57210 ?  166 HIS   A CG    1 
ATOM   1363 N  ND1   . HIS   A 1 167 ? 25.15800 -4.82300  22.33300  1.000 48.68672 ?  166 HIS   A ND1   1 
ATOM   1364 C  CD2   . HIS   A 1 167 ? 23.75000 -3.64900  23.52100  1.000 44.34172 ?  166 HIS   A CD2   1 
ATOM   1365 C  CE1   . HIS   A 1 167 ? 25.86600 -4.15500  23.22800  1.000 45.61401 ?  166 HIS   A CE1   1 
ATOM   1366 N  NE2   . HIS   A 1 167 ? 25.03500 -3.43700  23.96300  1.000 48.45914 ?  166 HIS   A NE2   1 
ATOM   1367 N  N     . LYS   A 1 168 ? 20.63900 -6.13500  23.80900  1.000 42.50267 ?  167 LYS   A N     1 
ATOM   1368 C  CA    . LYS   A 1 168 ? 20.15700 -6.15800  25.18600  1.000 44.19279 ?  167 LYS   A CA    1 
ATOM   1369 C  C     . LYS   A 1 168 ? 19.57400 -7.53000  25.49800  1.000 49.68241 ?  167 LYS   A C     1 
ATOM   1370 O  O     . LYS   A 1 168 ? 19.66200 -8.00100  26.62800  1.000 58.05057 ?  167 LYS   A O     1 
ATOM   1371 C  CB    . LYS   A 1 168 ? 19.10900 -5.06200  25.43200  1.000 43.23555 ?  167 LYS   A CB    1 
ATOM   1372 C  CG    . LYS   A 1 168 ? 19.44700 -3.74400  24.76200  1.000 45.46428 ?  167 LYS   A CG    1 
ATOM   1373 C  CD    . LYS   A 1 168 ? 19.05800 -2.52300  25.57200  1.000 43.73855 ?  167 LYS   A CD    1 
ATOM   1374 C  CE    . LYS   A 1 168 ? 19.93600 -1.35000  25.13500  1.000 46.85437 ?  167 LYS   A CE    1 
ATOM   1375 N  NZ    . LYS   A 1 168 ? 20.03500 -0.26200  26.14800  1.000 53.30089 ?  167 LYS   A NZ    1 
ATOM   1376 N  N     . SER   B 1 1   ? 29.74200 -13.74800 40.72500  1.000 47.81431 ?  0   SER   B N     1 
ATOM   1377 C  CA    . SER   B 1 1   ? 31.13400 -13.48200 40.39200  1.000 44.86587 ?  0   SER   B CA    1 
ATOM   1378 C  C     . SER   B 1 1   ? 31.35000 -13.36700 38.89900  1.000 44.00735 ?  0   SER   B C     1 
ATOM   1379 O  O     . SER   B 1 1   ? 30.63800 -13.98500 38.10500  1.000 44.25496 ?  0   SER   B O     1 
ATOM   1380 C  CB    . SER   B 1 1   ? 32.03700 -14.57600 40.95300  1.000 48.15759 ?  0   SER   B CB    1 
ATOM   1381 O  OG    . SER   B 1 1   ? 32.76100 -14.08500 42.05500  1.000 53.73589 ?  0   SER   B OG    1 
ATOM   1382 N  N     . MET   B 1 2   ? 32.35000 -12.57600 38.51600  1.000 45.12647 ?  1   MET   B N     1 
ATOM   1383 C  CA    . MET   B 1 2   ? 32.62100 -12.37500 37.10500  1.000 41.58325 ?  1   MET   B CA    1 
ATOM   1384 C  C     . MET   B 1 2   ? 33.03000 -13.69200 36.45600  1.000 36.74492 ?  1   MET   B C     1 
ATOM   1385 O  O     . MET   B 1 2   ? 33.58900 -14.58200 37.10400  1.000 38.47770 ?  1   MET   B O     1 
ATOM   1386 C  CB    . MET   B 1 2   ? 33.71500 -11.31800 36.90100  1.000 36.81410 ?  1   MET   B CB    1 
ATOM   1387 C  CG    . MET   B 1 2   ? 35.10800 -11.73800 37.30700  1.000 32.76792 ?  1   MET   B CG    1 
ATOM   1388 S  SD    . MET   B 1 2   ? 36.27800 -10.38400 37.02400  1.000 33.49729 ?  1   MET   B SD    1 
ATOM   1389 C  CE    . MET   B 1 2   ? 35.77200 -9.33500  38.38400  1.000 32.88684 ?  1   MET   B CE    1 
ATOM   1390 N  N     . THR   B 1 3   ? 32.72700 -13.80200 35.16400  1.000 34.00645 ?  2   THR   B N     1 
ATOM   1391 C  CA    . THR   B 1 3   ? 33.08800 -14.97200 34.37800  1.000 31.99734 ?  2   THR   B CA    1 
ATOM   1392 C  C     . THR   B 1 3   ? 34.60400 -15.10100 34.25400  1.000 28.82979 ?  2   THR   B C     1 
ATOM   1393 O  O     . THR   B 1 3   ? 35.31200 -14.11800 33.99800  1.000 30.55661 ?  2   THR   B O     1 
ATOM   1394 C  CB    . THR   B 1 3   ? 32.45300 -14.86000 32.99200  1.000 32.32525 ?  2   THR   B CB    1 
ATOM   1395 O  OG1   . THR   B 1 3   ? 31.03500 -14.70900 33.15600  1.000 35.38662 ?  2   THR   B OG1   1 
ATOM   1396 C  CG2   . THR   B 1 3   ? 32.73000 -16.09900 32.16300  1.000 32.57638 ?  2   THR   B CG2   1 
ATOM   1397 N  N     . GLU   B 1 4   ? 35.10200 -16.32500 34.43300  1.000 28.72597 ?  3   GLU   B N     1 
ATOM   1398 C  CA    . GLU   B 1 4   ? 36.51600 -16.61800 34.23300  1.000 25.68160 ?  3   GLU   B CA    1 
ATOM   1399 C  C     . GLU   B 1 4   ? 36.72200 -17.33400 32.90600  1.000 28.85581 ?  3   GLU   B C     1 
ATOM   1400 O  O     . GLU   B 1 4   ? 35.95900 -18.24000 32.55400  1.000 29.06067 ?  3   GLU   B O     1 
ATOM   1401 C  CB    . GLU   B 1 4   ? 37.07100 -17.48200 35.36500  1.000 31.53188 ?  3   GLU   B CB    1 
ATOM   1402 C  CG    . GLU   B 1 4   ? 36.92100 -16.81800 36.72700  1.000 38.54452 ?  3   GLU   B CG    1 
ATOM   1403 C  CD    . GLU   B 1 4   ? 37.26000 -17.76600 37.87300  1.000 44.23944 ?  3   GLU   B CD    1 
ATOM   1404 O  OE1   . GLU   B 1 4   ? 37.92000 -18.79700 37.59900  1.000 46.60500 ?  3   GLU   B OE1   1 
ATOM   1405 O  OE2   . GLU   B 1 4   ? 36.84200 -17.49300 39.02700  1.000 40.75170 -1 3   GLU   B OE2   1 
ATOM   1406 N  N     . TYR   B 1 5   ? 37.74200 -16.90600 32.16500  1.000 25.56596 ?  4   TYR   B N     1 
ATOM   1407 C  CA    . TYR   B 1 5   ? 38.09800 -17.51600 30.88400  1.000 24.85352 ?  4   TYR   B CA    1 
ATOM   1408 C  C     . TYR   B 1 5   ? 39.49200 -18.12500 30.97400  1.000 26.80025 ?  4   TYR   B C     1 
ATOM   1409 O  O     . TYR   B 1 5   ? 40.47100 -17.40600 31.20400  1.000 26.61141 ?  4   TYR   B O     1 
ATOM   1410 C  CB    . TYR   B 1 5   ? 38.06900 -16.49200 29.74900  1.000 24.80360 ?  4   TYR   B CB    1 
ATOM   1411 C  CG    . TYR   B 1 5   ? 36.68500 -15.96000 29.49300  1.000 28.36076 ?  4   TYR   B CG    1 
ATOM   1412 C  CD1   . TYR   B 1 5   ? 35.75800 -16.71400 28.77800  1.000 32.20535 ?  4   TYR   B CD1   1 
ATOM   1413 C  CD2   . TYR   B 1 5   ? 36.28100 -14.74000 30.02400  1.000 25.87015 ?  4   TYR   B CD2   1 
ATOM   1414 C  CE1   . TYR   B 1 5   ? 34.46700 -16.22900 28.55800  1.000 34.43564 ?  4   TYR   B CE1   1 
ATOM   1415 C  CE2   . TYR   B 1 5   ? 35.02600 -14.24300 29.80700  1.000 31.99233 ?  4   TYR   B CE2   1 
ATOM   1416 C  CZ    . TYR   B 1 5   ? 34.11700 -14.99500 29.08200  1.000 30.20683 ?  4   TYR   B CZ    1 
ATOM   1417 O  OH    . TYR   B 1 5   ? 32.87500 -14.47700 28.89500  1.000 29.30817 ?  4   TYR   B OH    1 
ATOM   1418 N  N     . LYS   B 1 6   ? 39.58700 -19.42700 30.73900  1.000 25.71633 ?  5   LYS   B N     1 
ATOM   1419 C  CA    . LYS   B 1 6   ? 40.87400 -20.12700 30.74200  1.000 24.40397 ?  5   LYS   B CA    1 
ATOM   1420 C  C     . LYS   B 1 6   ? 41.48300 -20.12200 29.34800  1.000 24.69378 ?  5   LYS   B C     1 
ATOM   1421 O  O     . LYS   B 1 6   ? 41.09300 -20.90800 28.48100  1.000 28.48199 ?  5   LYS   B O     1 
ATOM   1422 C  CB    . LYS   B 1 6   ? 40.69200 -21.54500 31.26300  1.000 29.06831 ?  5   LYS   B CB    1 
ATOM   1423 C  CG    . LYS   B 1 6   ? 40.08500 -21.54400 32.65700  1.000 29.67823 ?  5   LYS   B CG    1 
ATOM   1424 C  CD    . LYS   B 1 6   ? 40.04200 -22.96300 33.22600  1.000 38.01322 ?  5   LYS   B CD    1 
ATOM   1425 C  CE    . LYS   B 1 6   ? 38.81600 -23.20000 34.09400  1.000 42.88192 ?  5   LYS   B CE    1 
ATOM   1426 N  NZ    . LYS   B 1 6   ? 38.66700 -22.22500 35.21800  1.000 44.00781 ?  5   LYS   B NZ    1 
ATOM   1427 N  N     . LEU   B 1 7   ? 42.44300 -19.22300 29.11800  1.000 24.14014 ?  6   LEU   B N     1 
ATOM   1428 C  CA    . LEU   B 1 7   ? 43.09900 -19.07900 27.82700  1.000 23.10059 ?  6   LEU   B CA    1 
ATOM   1429 C  C     . LEU   B 1 7   ? 44.45400 -19.77400 27.89300  1.000 26.45805 ?  6   LEU   B C     1 
ATOM   1430 O  O     . LEU   B 1 7   ? 45.13600 -19.72100 28.92300  1.000 26.92219 ?  6   LEU   B O     1 
ATOM   1431 C  CB    . LEU   B 1 7   ? 43.28300 -17.59400 27.46900  1.000 25.02363 ?  6   LEU   B CB    1 
ATOM   1432 C  CG    . LEU   B 1 7   ? 42.10900 -16.63500 27.72700  1.000 27.04647 ?  6   LEU   B CG    1 
ATOM   1433 C  CD1   . LEU   B 1 7   ? 42.39300 -15.20200 27.23600  1.000 28.91458 ?  6   LEU   B CD1   1 
ATOM   1434 C  CD2   . LEU   B 1 7   ? 40.87100 -17.19800 27.08500  1.000 30.02083 ?  6   LEU   B CD2   1 
ATOM   1435 N  N     . VAL   B 1 8   ? 44.84500 -20.42300 26.80200  1.000 21.23597 ?  7   VAL   B N     1 
ATOM   1436 C  CA    . VAL   B 1 8   ? 46.11700 -21.13600 26.71300  1.000 21.23597 ?  7   VAL   B CA    1 
ATOM   1437 C  C     . VAL   B 1 8   ? 46.83600 -20.65100 25.46400  1.000 23.20696 ?  7   VAL   B C     1 
ATOM   1438 O  O     . VAL   B 1 8   ? 46.24600 -20.65400 24.37300  1.000 23.29125 ?  7   VAL   B O     1 
ATOM   1439 C  CB    . VAL   B 1 8   ? 45.92200 -22.65900 26.64700  1.000 22.48490 ?  7   VAL   B CB    1 
ATOM   1440 C  CG1   . VAL   B 1 8   ? 47.29300 -23.35700 26.50000  1.000 23.01523 ?  7   VAL   B CG1   1 
ATOM   1441 C  CG2   . VAL   B 1 8   ? 45.11900 -23.15300 27.86200  1.000 24.84634 ?  7   VAL   B CG2   1 
ATOM   1442 N  N     . VAL   B 1 9   ? 48.08100 -20.21800 25.61900  1.000 21.13212 ?  8   VAL   B N     1 
ATOM   1443 C  CA    . VAL   B 1 9   ? 48.84900 -19.68400 24.49100  1.000 21.51326 ?  8   VAL   B CA    1 
ATOM   1444 C  C     . VAL   B 1 9   ? 49.79200 -20.78000 24.03300  1.000 22.73465 ?  8   VAL   B C     1 
ATOM   1445 O  O     . VAL   B 1 9   ? 50.61000 -21.27200 24.82900  1.000 22.66928 ?  8   VAL   B O     1 
ATOM   1446 C  CB    . VAL   B 1 9   ? 49.61300 -18.40700 24.88600  1.000 20.94963 ?  8   VAL   B CB    1 
ATOM   1447 C  CG1   . VAL   B 1 9   ? 50.33400 -17.79900 23.66400  1.000 21.13196 ?  8   VAL   B CG1   1 
ATOM   1448 C  CG2   . VAL   B 1 9   ? 48.67400 -17.39400 25.54100  1.000 22.71847 ?  8   VAL   B CG2   1 
ATOM   1449 N  N     . VAL   B 1 10  ? 49.66700 -21.18500 22.76000  1.000 21.88643 ?  9   VAL   B N     1 
ATOM   1450 C  CA    . VAL   B 1 10  ? 50.42900 -22.30900 22.21500  1.000 25.58944 ?  9   VAL   B CA    1 
ATOM   1451 C  C     . VAL   B 1 10  ? 51.11600 -21.89000 20.91800  1.000 28.00945 ?  9   VAL   B C     1 
ATOM   1452 O  O     . VAL   B 1 10  ? 50.73500 -20.91100 20.27400  1.000 26.31701 ?  9   VAL   B O     1 
ATOM   1453 C  CB    . VAL   B 1 10  ? 49.54400 -23.55000 21.96000  1.000 26.52286 ?  9   VAL   B CB    1 
ATOM   1454 C  CG1   . VAL   B 1 10  ? 48.81400 -23.95800 23.23100  1.000 22.80194 ?  9   VAL   B CG1   1 
ATOM   1455 C  CG2   . VAL   B 1 10  ? 48.50500 -23.29700 20.81500  1.000 24.83708 ?  9   VAL   B CG2   1 
ATOM   1456 N  N     . GLY   B 1 11  ? 52.12200 -22.66900 20.52300  1.000 24.19098 ?  10  GLY   B N     1 
ATOM   1457 C  CA    . GLY   B 1 11  ? 52.89700 -22.36700 19.31600  1.000 25.48704 ?  10  GLY   B CA    1 
ATOM   1458 C  C     . GLY   B 1 11  ? 54.36800 -22.72800 19.45000  1.000 26.27916 ?  10  GLY   B C     1 
ATOM   1459 O  O     . GLY   B 1 11  ? 54.84500 -22.99500 20.54700  1.000 26.19730 ?  10  GLY   B O     1 
ATOM   1460 N  N     . ALA   B 1 12  ? 55.08600 -22.76500 18.33100  1.000 27.75112 ?  11  ALA   B N     1 
ATOM   1461 C  CA    . ALA   B 1 12  ? 56.45800 -23.23300 18.27600  1.000 29.66320 ?  11  ALA   B CA    1 
ATOM   1462 C  C     . ALA   B 1 12  ? 57.37100 -22.36500 19.14200  1.000 27.69798 ?  11  ALA   B C     1 
ATOM   1463 O  O     . ALA   B 1 12  ? 57.01900 -21.25500 19.55800  1.000 27.48561 ?  11  ALA   B O     1 
ATOM   1464 C  CB    . ALA   B 1 12  ? 56.94200 -23.22000 16.81900  1.000 28.23686 ?  11  ALA   B CB    1 
ATOM   1465 N  N     . VAL   B 1 13  ? 58.58300 -22.87500 19.39300  1.000 28.12840 ?  12  VAL   B N     1 
ATOM   1466 C  CA    . VAL   B 1 13  ? 59.54100 -22.15000 20.22500  1.000 28.83916 ?  12  VAL   B CA    1 
ATOM   1467 C  C     . VAL   B 1 13  ? 59.84600 -20.80500 19.57300  1.000 33.82004 ?  12  VAL   B C     1 
ATOM   1468 O  O     . VAL   B 1 13  ? 60.02300 -20.72800 18.35400  1.000 31.26313 ?  12  VAL   B O     1 
ATOM   1469 C  CB    . VAL   B 1 13  ? 60.81400 -22.99100 20.41300  1.000 32.24964 ?  12  VAL   B CB    1 
ATOM   1470 C  CG1   . VAL   B 1 13  ? 61.96500 -22.13500 20.89000  1.000 33.90304 ?  12  VAL   B CG1   1 
ATOM   1471 C  CG2   . VAL   B 1 13  ? 60.55000 -24.15100 21.41600  1.000 36.22169 ?  12  VAL   B CG2   1 
ATOM   1472 N  N     . GLY   B 1 14  ? 59.86500 -19.73100 20.37600  1.000 30.33493 ?  13  GLY   B N     1 
ATOM   1473 C  CA    . GLY   B 1 14  ? 60.32200 -18.42600 19.91200  1.000 32.17460 ?  13  GLY   B CA    1 
ATOM   1474 C  C     . GLY   B 1 14  ? 59.36400 -17.61300 19.06400  1.000 30.73355 ?  13  GLY   B C     1 
ATOM   1475 O  O     . GLY   B 1 14  ? 59.77300 -16.58800 18.51700  1.000 30.62373 ?  13  GLY   B O     1 
ATOM   1476 N  N     . VAL   B 1 15  ? 58.10700 -18.01800 18.92100  1.000 27.88558 ?  14  VAL   B N     1 
ATOM   1477 C  CA    . VAL   B 1 15  ? 57.19600 -17.23500 18.09400  1.000 30.18268 ?  14  VAL   B CA    1 
ATOM   1478 C  C     . VAL   B 1 15  ? 56.72100 -15.97300 18.80300  1.000 33.13499 ?  14  VAL   B C     1 
ATOM   1479 O  O     . VAL   B 1 15  ? 56.16500 -15.07900 18.15000  1.000 29.32376 ?  14  VAL   B O     1 
ATOM   1480 C  CB    . VAL   B 1 15  ? 55.98500 -18.06900 17.63300  1.000 27.56699 ?  14  VAL   B CB    1 
ATOM   1481 C  CG1   . VAL   B 1 15  ? 56.44400 -19.23600 16.76500  1.000 28.58932 ?  14  VAL   B CG1   1 
ATOM   1482 C  CG2   . VAL   B 1 15  ? 55.20200 -18.60700 18.82300  1.000 29.27290 ?  14  VAL   B CG2   1 
ATOM   1483 N  N     . GLY   B 1 16  ? 56.91300 -15.88500 20.10400  1.000 26.82690 ?  15  GLY   B N     1 
ATOM   1484 C  CA    . GLY   B 1 16  ? 56.47300 -14.74900 20.89200  1.000 27.75075 ?  15  GLY   B CA    1 
ATOM   1485 C  C     . GLY   B 1 16  ? 55.30100 -14.99000 21.85300  1.000 29.09495 ?  15  GLY   B C     1 
ATOM   1486 O  O     . GLY   B 1 16  ? 54.62900 -14.02100 22.23300  1.000 29.54101 ?  15  GLY   B O     1 
ATOM   1487 N  N     . LYS   B 1 17  ? 55.03600 -16.24000 22.23400  1.000 27.74701 ?  16  LYS   B N     1 
ATOM   1488 C  CA    . LYS   B 1 17  ? 53.97100 -16.53100 23.19500  1.000 25.94779 ?  16  LYS   B CA    1 
ATOM   1489 C  C     . LYS   B 1 17  ? 54.14300 -15.73600 24.49100  1.000 27.06623 ?  16  LYS   B C     1 
ATOM   1490 O  O     . LYS   B 1 17  ? 53.18500 -15.13100 25.00400  1.000 24.71363 ?  16  LYS   B O     1 
ATOM   1491 C  CB    . LYS   B 1 17  ? 53.95800 -18.03100 23.49500  1.000 25.58611 ?  16  LYS   B CB    1 
ATOM   1492 C  CG    . LYS   B 1 17  ? 53.59900 -18.90700 22.30900  1.000 26.76118 ?  16  LYS   B CG    1 
ATOM   1493 C  CD    . LYS   B 1 17  ? 53.61100 -20.36700 22.71200  1.000 27.64752 ?  16  LYS   B CD    1 
ATOM   1494 C  CE    . LYS   B 1 17  ? 54.97700 -20.80800 23.27000  1.000 24.70381 ?  16  LYS   B CE    1 
ATOM   1495 N  NZ    . LYS   B 1 17  ? 56.09500 -20.80900 22.23000  1.000 27.29393 ?  16  LYS   B NZ    1 
ATOM   1496 N  N     . SER   B 1 18  ? 55.34200 -15.79100 25.07300  1.000 24.76786 ?  17  SER   B N     1 
ATOM   1497 C  CA    . SER   B 1 18  ? 55.63700 -15.05500 26.29600  1.000 25.56424 ?  17  SER   B CA    1 
ATOM   1498 C  C     . SER   B 1 18  ? 55.59000 -13.54100 26.07500  1.000 29.14051 ?  17  SER   B C     1 
ATOM   1499 O  O     . SER   B 1 18  ? 54.98900 -12.80900 26.87100  1.000 27.26389 ?  17  SER   B O     1 
ATOM   1500 C  CB    . SER   B 1 18  ? 56.99700 -15.48800 26.84000  1.000 26.22495 ?  17  SER   B CB    1 
ATOM   1501 O  OG    . SER   B 1 18  ? 56.90600 -16.83200 27.27500  1.000 26.16154 ?  17  SER   B OG    1 
ATOM   1502 N  N     . ALA   B 1 19  ? 56.24700 -13.05100 25.01600  1.000 27.86279 ?  18  ALA   B N     1 
ATOM   1503 C  CA    . ALA   B 1 19  ? 56.26600 -11.61500 24.75900  1.000 32.79549 ?  18  ALA   B CA    1 
ATOM   1504 C  C     . ALA   B 1 19  ? 54.85200 -11.03900 24.66300  1.000 26.59460 ?  18  ALA   B C     1 
ATOM   1505 O  O     . ALA   B 1 19  ? 54.57300 -9.95400  25.19200  1.000 31.26920 ?  18  ALA   B O     1 
ATOM   1506 C  CB    . ALA   B 1 19  ? 57.06800 -11.33100 23.48300  1.000 31.28048 ?  18  ALA   B CB    1 
ATOM   1507 N  N     . LEU   B 1 20  ? 53.94600 -11.74800 24.00600  1.000 25.68212 ?  19  LEU   B N     1 
ATOM   1508 C  CA    . LEU   B 1 20  ? 52.57100 -11.29200 23.92300  1.000 24.21039 ?  19  LEU   B CA    1 
ATOM   1509 C  C     . LEU   B 1 20  ? 51.94700 -11.26200 25.29700  1.000 25.94343 ?  19  LEU   B C     1 
ATOM   1510 O  O     . LEU   B 1 20  ? 51.30500 -10.28100 25.67700  1.000 25.45999 ?  19  LEU   B O     1 
ATOM   1511 C  CB    . LEU   B 1 20  ? 51.76200 -12.20400 23.00300  1.000 24.55010 ?  19  LEU   B CB    1 
ATOM   1512 C  CG    . LEU   B 1 20  ? 52.09200 -12.11700 21.51300  1.000 30.42945 ?  19  LEU   B CG    1 
ATOM   1513 C  CD1   . LEU   B 1 20  ? 51.48600 -13.30900 20.79500  1.000 31.71750 ?  19  LEU   B CD1   1 
ATOM   1514 C  CD2   . LEU   B 1 20  ? 51.48600 -10.80900 20.98400  1.000 27.98460 ?  19  LEU   B CD2   1 
ATOM   1515 N  N     . THR   B 1 21  ? 52.16900 -12.33000 26.07100  1.000 24.93904 ?  20  THR   B N     1 
ATOM   1516 C  CA    . THR   B 1 21  ? 51.55500 -12.43300 27.39700  1.000 24.70618 ?  20  THR   B CA    1 
ATOM   1517 C  C     . THR   B 1 21  ? 52.10500 -11.37700 28.34600  1.000 24.17610 ?  20  THR   B C     1 
ATOM   1518 O  O     . THR   B 1 21  ? 51.34100 -10.74600 29.07800  1.000 25.28025 ?  20  THR   B O     1 
ATOM   1519 C  CB    . THR   B 1 21  ? 51.79600 -13.83100 27.96200  1.000 26.56303 ?  20  THR   B CB    1 
ATOM   1520 O  OG1   . THR   B 1 21  ? 51.24500 -14.80800 27.07300  1.000 24.87378 ?  20  THR   B OG1   1 
ATOM   1521 C  CG2   . THR   B 1 21  ? 51.17700 -13.98500 29.36300  1.000 24.95857 ?  20  THR   B CG2   1 
ATOM   1522 N  N     . ILE   B 1 22  ? 53.43000 -11.17900 28.34100  1.000 23.34780 ?  21  ILE   B N     1 
ATOM   1523 C  CA    . ILE   B 1 22  ? 54.07700 -10.20500 29.20500  1.000 25.18558 ?  21  ILE   B CA    1 
ATOM   1524 C  C     . ILE   B 1 22  ? 53.63800 -8.78600  28.82800  1.000 25.10964 ?  21  ILE   B C     1 
ATOM   1525 O  O     . ILE   B 1 22  ? 53.45200 -7.94900  29.70800  1.000 26.55086 ?  21  ILE   B O     1 
ATOM   1526 C  CB    . ILE   B 1 22  ? 55.60600 -10.38400 29.14300  1.000 26.73893 ?  21  ILE   B CB    1 
ATOM   1527 C  CG1   . ILE   B 1 22  ? 56.00200 -11.72500 29.78800  1.000 29.66127 ?  21  ILE   B CG1   1 
ATOM   1528 C  CG2   . ILE   B 1 22  ? 56.36800 -9.16400  29.77100  1.000 28.46407 ?  21  ILE   B CG2   1 
ATOM   1529 C  CD1   . ILE   B 1 22  ? 55.51100 -11.88500 31.23500  1.000 34.43526 ?  21  ILE   B CD1   1 
ATOM   1530 N  N     . GLN   B 1 23  ? 53.43700 -8.49900  27.52600  1.000 25.58535 ?  22  GLN   B N     1 
ATOM   1531 C  CA    . GLN   B 1 23  ? 52.85900 -7.20200  27.15400  1.000 27.68740 ?  22  GLN   B CA    1 
ATOM   1532 C  C     . GLN   B 1 23  ? 51.47600 -7.02400  27.77800  1.000 26.82126 ?  22  GLN   B C     1 
ATOM   1533 O  O     . GLN   B 1 23  ? 51.16300 -5.96300  28.33300  1.000 30.37344 ?  22  GLN   B O     1 
ATOM   1534 C  CB    . GLN   B 1 23  ? 52.77500 -7.03800  25.63500  1.000 30.79641 ?  22  GLN   B CB    1 
ATOM   1535 C  CG    . GLN   B 1 23  ? 54.06400 -6.48000  25.00100  1.000 32.63126 ?  22  GLN   B CG    1 
ATOM   1536 C  CD    . GLN   B 1 23  ? 54.24900 -4.96700  25.22600  1.000 37.34628 ?  22  GLN   B CD    1 
ATOM   1537 O  OE1   . GLN   B 1 23  ? 53.70100 -4.36600  26.17600  1.000 32.48806 ?  22  GLN   B OE1   1 
ATOM   1538 N  NE2   . GLN   B 1 23  ? 55.02600 -4.34400  24.33700  1.000 33.39026 ?  22  GLN   B NE2   1 
ATOM   1539 N  N     . LEU   B 1 24  ? 50.62800 -8.05000  27.67900  1.000 26.65246 ?  23  LEU   B N     1 
ATOM   1540 C  CA    . LEU   B 1 24  ? 49.27600 -7.96600  28.22600  1.000 26.78723 ?  23  LEU   B CA    1 
ATOM   1541 C  C     . LEU   B 1 24  ? 49.31700 -7.74200  29.73300  1.000 27.87980 ?  23  LEU   B C     1 
ATOM   1542 O  O     . LEU   B 1 24  ? 48.55900 -6.91900  30.27400  1.000 27.61664 ?  23  LEU   B O     1 
ATOM   1543 C  CB    . LEU   B 1 24  ? 48.50000 -9.24200  27.89900  1.000 24.66743 ?  23  LEU   B CB    1 
ATOM   1544 C  CG    . LEU   B 1 24  ? 47.03700 -9.24500  28.39900  1.000 27.77165 ?  23  LEU   B CG    1 
ATOM   1545 C  CD1   . LEU   B 1 24  ? 46.17300 -8.38600  27.48800  1.000 28.43513 ?  23  LEU   B CD1   1 
ATOM   1546 C  CD2   . LEU   B 1 24  ? 46.48100 -10.65100 28.48700  1.000 25.19813 ?  23  LEU   B CD2   1 
ATOM   1547 N  N     . ILE   B 1 25  ? 50.18500 -8.47100  30.43000  1.000 24.61621 ?  24  ILE   B N     1 
ATOM   1548 C  CA    . ILE   B 1 25  ? 50.14500 -8.46900  31.89600  1.000 24.43717 ?  24  ILE   B CA    1 
ATOM   1549 C  C     . ILE   B 1 25  ? 50.99900 -7.36200  32.48400  1.000 27.83851 ?  24  ILE   B C     1 
ATOM   1550 O  O     . ILE   B 1 25  ? 50.60100 -6.72500  33.46700  1.000 27.22031 ?  24  ILE   B O     1 
ATOM   1551 C  CB    . ILE   B 1 25  ? 50.59200 -9.84200  32.43900  1.000 28.33572 ?  24  ILE   B CB    1 
ATOM   1552 C  CG1   . ILE   B 1 25  ? 49.73000 -10.99300 31.88100  1.000 24.88158 ?  24  ILE   B CG1   1 
ATOM   1553 C  CG2   . ILE   B 1 25  ? 50.75800 -9.81000  34.00200  1.000 26.41476 ?  24  ILE   B CG2   1 
ATOM   1554 C  CD1   . ILE   B 1 25  ? 48.19900 -11.02200 32.25700  1.000 21.98095 ?  24  ILE   B CD1   1 
ATOM   1555 N  N     . GLN   B 1 26  ? 52.22000 -7.18300  31.96500  1.000 27.82393 ?  25  GLN   B N     1 
ATOM   1556 C  CA    . GLN   B 1 26  ? 53.20400 -6.31400  32.60100  1.000 31.94450 ?  25  GLN   B CA    1 
ATOM   1557 C  C     . GLN   B 1 26  ? 53.54700 -5.06200  31.80000  1.000 29.97029 ?  25  GLN   B C     1 
ATOM   1558 O  O     . GLN   B 1 26  ? 54.32100 -4.23300  32.29600  1.000 29.37388 ?  25  GLN   B O     1 
ATOM   1559 C  CB    . GLN   B 1 26  ? 54.48200 -7.10400  32.88100  1.000 25.74122 ?  25  GLN   B CB    1 
ATOM   1560 C  CG    . GLN   B 1 26  ? 54.20800 -8.35500  33.73000  1.000 32.23625 ?  25  GLN   B CG    1 
ATOM   1561 C  CD    . GLN   B 1 26  ? 55.44800 -9.15000  33.94800  1.000 33.37858 ?  25  GLN   B CD    1 
ATOM   1562 O  OE1   . GLN   B 1 26  ? 56.50800 -8.78400  33.45800  1.000 35.13243 ?  25  GLN   B OE1   1 
ATOM   1563 N  NE2   . GLN   B 1 26  ? 55.33800 -10.24400 34.68800  1.000 35.31250 ?  25  GLN   B NE2   1 
ATOM   1564 N  N     . ASN   B 1 27  ? 52.99400 -4.90400  30.59100  1.000 29.46221 ?  26  ASN   B N     1 
ATOM   1565 C  CA    . ASN   B 1 27  ? 53.08300 -3.65400  29.81700  1.000 29.75925 ?  26  ASN   B CA    1 
ATOM   1566 C  C     . ASN   B 1 27  ? 54.51700 -3.30000  29.42400  1.000 35.93354 ?  26  ASN   B C     1 
ATOM   1567 O  O     . ASN   B 1 27  ? 54.90600 -2.13100  29.44300  1.000 31.82744 ?  26  ASN   B O     1 
ATOM   1568 C  CB    . ASN   B 1 27  ? 52.45900 -2.48800  30.58400  1.000 30.88128 ?  26  ASN   B CB    1 
ATOM   1569 C  CG    . ASN   B 1 27  ? 52.19100 -1.28800  29.70200  1.000 34.07239 ?  26  ASN   B CG    1 
ATOM   1570 O  OD1   . ASN   B 1 27  ? 51.75900 -1.43200  28.55700  1.000 35.97382 ?  26  ASN   B OD1   1 
ATOM   1571 N  ND2   . ASN   B 1 27  ? 52.43100 -0.08900  30.23800  1.000 33.93879 ?  26  ASN   B ND2   1 
ATOM   1572 N  N     . HIS   B 1 28  ? 55.31300 -4.30400  29.07100  1.000 29.11386 ?  27  HIS   B N     1 
ATOM   1573 C  CA    . HIS   B 1 28  ? 56.64000 -4.03100  28.55100  1.000 34.45982 ?  27  HIS   B CA    1 
ATOM   1574 C  C     . HIS   B 1 28  ? 57.06500 -5.17200  27.63500  1.000 35.42465 ?  27  HIS   B C     1 
ATOM   1575 O  O     . HIS   B 1 28  ? 56.42600 -6.22300  27.56400  1.000 31.44516 ?  27  HIS   B O     1 
ATOM   1576 C  CB    . HIS   B 1 28  ? 57.67300 -3.80500  29.66700  1.000 35.12034 ?  27  HIS   B CB    1 
ATOM   1577 C  CG    . HIS   B 1 28  ? 57.92500 -5.00400  30.52500  1.000 35.50980 ?  27  HIS   B CG    1 
ATOM   1578 N  ND1   . HIS   B 1 28  ? 58.77400 -6.02700  30.15300  1.000 42.39670 ?  27  HIS   B ND1   1 
ATOM   1579 C  CD2   . HIS   B 1 28  ? 57.44700 -5.33600  31.74800  1.000 39.30153 ?  27  HIS   B CD2   1 
ATOM   1580 C  CE1   . HIS   B 1 28  ? 58.80000 -6.93900  31.11000  1.000 40.42764 ?  27  HIS   B CE1   1 
ATOM   1581 N  NE2   . HIS   B 1 28  ? 58.01000 -6.54100  32.09000  1.000 38.62041 ?  27  HIS   B NE2   1 
ATOM   1582 N  N     . PHE   B 1 29  ? 58.13100 -4.91700  26.89100  1.000 30.37730 ?  28  PHE   B N     1 
ATOM   1583 C  CA    . PHE   B 1 29  ? 58.73000 -5.89300  25.98700  1.000 30.11316 ?  28  PHE   B CA    1 
ATOM   1584 C  C     . PHE   B 1 29  ? 60.23900 -5.88200  26.19300  1.000 39.13667 ?  28  PHE   B C     1 
ATOM   1585 O  O     . PHE   B 1 29  ? 60.85800 -4.81300  26.20200  1.000 39.63774 ?  28  PHE   B O     1 
ATOM   1586 C  CB    . PHE   B 1 29  ? 58.36300 -5.55200  24.53000  1.000 39.76855 ?  28  PHE   B CB    1 
ATOM   1587 C  CG    . PHE   B 1 29  ? 59.14600 -6.31900  23.48100  1.000 38.31326 ?  28  PHE   B CG    1 
ATOM   1588 C  CD1   . PHE   B 1 29  ? 60.33700 -5.80900  22.97200  1.000 40.22286 ?  28  PHE   B CD1   1 
ATOM   1589 C  CD2   . PHE   B 1 29  ? 58.67000 -7.52300  22.97900  1.000 33.73672 ?  28  PHE   B CD2   1 
ATOM   1590 C  CE1   . PHE   B 1 29  ? 61.05000 -6.49800  21.99500  1.000 36.47815 ?  28  PHE   B CE1   1 
ATOM   1591 C  CE2   . PHE   B 1 29  ? 59.38500 -8.23100  21.99900  1.000 36.54144 ?  28  PHE   B CE2   1 
ATOM   1592 C  CZ    . PHE   B 1 29  ? 60.56700 -7.70500  21.49700  1.000 37.77021 ?  28  PHE   B CZ    1 
ATOM   1593 N  N     . VAL   B 1 30  ? 60.82600 -7.07500  26.29100  1.000 42.44846 ?  29  VAL   B N     1 
ATOM   1594 C  CA    . VAL   B 1 30  ? 62.31400 -7.19600  26.36500  1.000 41.95440 ?  29  VAL   B CA    1 
ATOM   1595 C  C     . VAL   B 1 30  ? 62.71700 -8.18100  25.25800  1.000 41.38385 ?  29  VAL   B C     1 
ATOM   1596 O  O     . VAL   B 1 30  ? 61.97100 -9.14100  25.04100  1.000 41.85369 ?  29  VAL   B O     1 
ATOM   1597 C  CB    . VAL   B 1 30  ? 62.81600 -7.67900  27.73500  1.000 40.80979 ?  29  VAL   B CB    1 
ATOM   1598 C  CG1   . VAL   B 1 30  ? 64.33000 -7.58300  27.86600  1.000 46.72843 ?  29  VAL   B CG1   1 
ATOM   1599 C  CG2   . VAL   B 1 30  ? 62.12500 -6.96100  28.88600  1.000 48.59950 ?  29  VAL   B CG2   1 
ATOM   1600 N  N     . ASP   B 1 31  ? 63.83800 -7.92900  24.58200  1.000 42.14064 ?  30  ASP   B N     1 
ATOM   1601 C  CA    . ASP   B 1 31  ? 64.23600 -8.80500  23.45000  1.000 43.59735 ?  30  ASP   B CA    1 
ATOM   1602 C  C     . ASP   B 1 31  ? 65.00200 -10.02700 23.96500  1.000 46.74684 ?  30  ASP   B C     1 
ATOM   1603 O  O     . ASP   B 1 31  ? 65.25200 -10.91800 23.13900  1.000 56.27267 ?  30  ASP   B O     1 
ATOM   1604 C  CB    . ASP   B 1 31  ? 64.98900 -8.05400  22.36500  1.000 47.19758 ?  30  ASP   B CB    1 
ATOM   1605 C  CG    . ASP   B 1 31  ? 65.01000 -8.73000  21.00100  1.000 53.08412 ?  30  ASP   B CG    1 
ATOM   1606 O  OD1   . ASP   B 1 31  ? 63.92900 -8.88100  20.40000  1.000 53.88908 ?  30  ASP   B OD1   1 
ATOM   1607 O  OD2   . ASP   B 1 31  ? 66.11200 -9.11500  20.55800  1.000 55.32854 ?  30  ASP   B OD2   1 
ATOM   1608 N  N     . GLU   B 1 32  ? 65.31600 -10.11200 25.25700  1.000 45.14689 ?  31  GLU   B N     1 
ATOM   1609 C  CA    . GLU   B 1 32  ? 66.12100 -11.27100 25.71600  1.000 44.04785 ?  31  GLU   B CA    1 
ATOM   1610 C  C     . GLU   B 1 32  ? 65.31600 -12.56100 25.52100  1.000 47.53405 ?  31  GLU   B C     1 
ATOM   1611 O  O     . GLU   B 1 32  ? 64.08000 -12.50900 25.58300  1.000 54.13734 ?  31  GLU   B O     1 
ATOM   1612 C  CB    . GLU   B 1 32  ? 66.53800 -11.19500 27.18100  1.000 47.40569 ?  31  GLU   B CB    1 
ATOM   1613 C  CG    . GLU   B 1 32  ? 67.68900 -10.23200 27.44700  1.000 54.33386 ?  31  GLU   B CG    1 
ATOM   1614 C  CD    . GLU   B 1 32  ? 67.91700 -9.96500  28.92400  1.000 53.75407 ?  31  GLU   B CD    1 
ATOM   1615 O  OE1   . GLU   B 1 32  ? 67.13900 -10.48400 29.74700  1.000 57.07787 ?  31  GLU   B OE1   1 
ATOM   1616 O  OE2   . GLU   B 1 32  ? 68.87000 -9.23400  29.24800  1.000 57.12466 -1 31  GLU   B OE2   1 
ATOM   1617 N  N     . TYR   B 1 33  ? 66.00500 -13.68000 25.33700  1.000 49.34585 ?  32  TYR   B N     1 
ATOM   1618 C  CA    . TYR   B 1 33  ? 65.27700 -14.97200 25.23900  1.000 50.10788 ?  32  TYR   B CA    1 
ATOM   1619 C  C     . TYR   B 1 33  ? 65.21800 -15.64600 26.60300  1.000 42.85278 ?  32  TYR   B C     1 
ATOM   1620 O  O     . TYR   B 1 33  ? 66.27100 -15.93500 27.18400  1.000 48.17409 ?  32  TYR   B O     1 
ATOM   1621 C  CB    . TYR   B 1 33  ? 65.84600 -15.94500 24.21100  1.000 47.65376 ?  32  TYR   B CB    1 
ATOM   1622 C  CG    . TYR   B 1 33  ? 64.84200 -17.04500 23.90600  1.000 46.78461 ?  32  TYR   B CG    1 
ATOM   1623 C  CD1   . TYR   B 1 33  ? 63.48000 -16.83700 24.09100  1.000 45.50311 ?  32  TYR   B CD1   1 
ATOM   1624 C  CD2   . TYR   B 1 33  ? 65.25600 -18.28900 23.45500  1.000 49.39308 ?  32  TYR   B CD2   1 
ATOM   1625 C  CE1   . TYR   B 1 33  ? 62.55700 -17.83500 23.83500  1.000 40.65506 ?  32  TYR   B CE1   1 
ATOM   1626 C  CE2   . TYR   B 1 33  ? 64.34300 -19.29500 23.19300  1.000 53.09387 ?  32  TYR   B CE2   1 
ATOM   1627 C  CZ    . TYR   B 1 33  ? 62.99400 -19.06300 23.38400  1.000 42.96707 ?  32  TYR   B CZ    1 
ATOM   1628 O  OH    . TYR   B 1 33  ? 62.10000 -20.04700 23.12200  1.000 50.72541 ?  32  TYR   B OH    1 
ATOM   1629 N  N     . ASP   B 1 34  ? 64.00900 -15.84900 27.10900  1.000 41.85962 ?  33  ASP   B N     1 
ATOM   1630 C  CA    . ASP   B 1 34  ? 63.79600 -16.56700 28.38900  1.000 44.09315 ?  33  ASP   B CA    1 
ATOM   1631 C  C     . ASP   B 1 34  ? 62.81800 -17.69400 28.06600  1.000 39.60468 ?  33  ASP   B C     1 
ATOM   1632 O  O     . ASP   B 1 34  ? 61.60200 -17.47300 28.13200  1.000 33.49924 ?  33  ASP   B O     1 
ATOM   1633 C  CB    . ASP   B 1 34  ? 63.26200 -15.67800 29.49900  1.000 44.05319 ?  33  ASP   B CB    1 
ATOM   1634 C  CG    . ASP   B 1 34  ? 63.22000 -16.31700 30.87700  1.000 46.70262 ?  33  ASP   B CG    1 
ATOM   1635 O  OD1   . ASP   B 1 34  ? 63.72300 -17.44900 31.01300  1.000 45.67231 -1 33  ASP   B OD1   1 
ATOM   1636 O  OD2   . ASP   B 1 34  ? 62.68900 -15.67200 31.80000  1.000 52.11677 ?  33  ASP   B OD2   1 
ATOM   1637 N  N     . PRO   B 1 35  ? 63.29700 -18.89900 27.71500  1.000 34.93968 ?  34  PRO   B N     1 
ATOM   1638 C  CA    . PRO   B 1 35  ? 62.38300 -19.95400 27.28700  1.000 29.62632 ?  34  PRO   B CA    1 
ATOM   1639 C  C     . PRO   B 1 35  ? 61.50300 -20.41200 28.44000  1.000 32.12708 ?  34  PRO   B C     1 
ATOM   1640 O  O     . PRO   B 1 35  ? 61.90900 -20.45500 29.60500  1.000 28.31584 ?  34  PRO   B O     1 
ATOM   1641 C  CB    . PRO   B 1 35  ? 63.32500 -21.06700 26.79100  1.000 30.35724 ?  34  PRO   B CB    1 
ATOM   1642 C  CG    . PRO   B 1 35  ? 64.55800 -20.87600 27.62300  1.000 35.14077 ?  34  PRO   B CG    1 
ATOM   1643 C  CD    . PRO   B 1 35  ? 64.68300 -19.38700 27.84900  1.000 37.80613 ?  34  PRO   B CD    1 
ATOM   1644 N  N     . THR   B 1 36  ? 60.25900 -20.71300 28.11100  1.000 26.82738 ?  35  THR   B N     1 
ATOM   1645 C  CA    . THR   B 1 36  ? 59.28900 -21.00200 29.15100  1.000 27.56834 ?  35  THR   B CA    1 
ATOM   1646 C  C     . THR   B 1 36  ? 59.27000 -22.48500 29.50300  1.000 25.12897 ?  35  THR   B C     1 
ATOM   1647 O  O     . THR   B 1 36  ? 59.47100 -23.34600 28.64400  1.000 25.31003 ?  35  THR   B O     1 
ATOM   1648 C  CB    . THR   B 1 36  ? 57.92300 -20.53300 28.64800  1.000 25.09766 ?  35  THR   B CB    1 
ATOM   1649 O  OG1   . THR   B 1 36  ? 58.04600 -19.14600 28.29400  1.000 24.80893 ?  35  THR   B OG1   1 
ATOM   1650 C  CG2   . THR   B 1 36  ? 56.81400 -20.72400 29.69000  1.000 24.63895 ?  35  THR   B CG2   1 
ATOM   1651 N  N     . ILE   B 1 37  ? 59.02500 -22.77500 30.79100  1.000 24.04421 ?  36  ILE   B N     1 
ATOM   1652 C  CA    . ILE   B 1 37  ? 58.63500 -24.12400 31.21300  1.000 22.61110 ?  36  ILE   B CA    1 
ATOM   1653 C  C     . ILE   B 1 37  ? 57.10900 -24.16400 31.20500  1.000 21.96112 ?  36  ILE   B C     1 
ATOM   1654 O  O     . ILE   B 1 37  ? 56.50200 -24.84000 30.37800  1.000 23.35048 ?  36  ILE   B O     1 
ATOM   1655 C  CB    . ILE   B 1 37  ? 59.18600 -24.48800 32.61200  1.000 22.56290 ?  36  ILE   B CB    1 
ATOM   1656 C  CG1   . ILE   B 1 37  ? 60.73600 -24.35900 32.68600  1.000 23.90123 ?  36  ILE   B CG1   1 
ATOM   1657 C  CG2   . ILE   B 1 37  ? 58.71000 -25.87700 32.99300  1.000 25.71972 ?  36  ILE   B CG2   1 
ATOM   1658 C  CD1   . ILE   B 1 37  ? 61.47200 -25.19400 31.72600  1.000 24.32902 ?  36  ILE   B CD1   1 
ATOM   1659 N  N     . GLU   B 1 38  ? 56.48200 -23.38800 32.10000  1.000 21.58121 ?  37  GLU   B N     1 
ATOM   1660 C  CA    . GLU   B 1 38  ? 55.04400 -23.14500 32.09700  1.000 22.99452 ?  37  GLU   B CA    1 
ATOM   1661 C  C     . GLU   B 1 38  ? 54.77000 -21.99000 33.05100  1.000 25.44165 ?  37  GLU   B C     1 
ATOM   1662 O  O     . GLU   B 1 38  ? 55.22800 -22.03700 34.19200  1.000 25.61453 ?  37  GLU   B O     1 
ATOM   1663 C  CB    . GLU   B 1 38  ? 54.26300 -24.39600 32.52500  1.000 23.25270 ?  37  GLU   B CB    1 
ATOM   1664 C  CG    . GLU   B 1 38  ? 52.74700 -24.22700 32.59300  1.000 27.22788 ?  37  GLU   B CG    1 
ATOM   1665 C  CD    . GLU   B 1 38  ? 52.06200 -25.38400 33.32300  1.000 37.96969 ?  37  GLU   B CD    1 
ATOM   1666 O  OE1   . GLU   B 1 38  ? 52.00100 -26.50100 32.74900  1.000 38.48525 ?  37  GLU   B OE1   1 
ATOM   1667 O  OE2   . GLU   B 1 38  ? 51.60200 -25.16700 34.47700  1.000 44.87937 -1 37  GLU   B OE2   1 
ATOM   1668 N  N     . ASP   B 1 39  ? 54.04500 -20.95500 32.61300  1.000 23.71474 ?  38  ASP   B N     1 
ATOM   1669 C  CA    . ASP   B 1 39  ? 53.69300 -19.84700 33.48900  1.000 26.60494 ?  38  ASP   B CA    1 
ATOM   1670 C  C     . ASP   B 1 39  ? 52.19300 -19.60000 33.43500  1.000 23.52144 ?  38  ASP   B C     1 
ATOM   1671 O  O     . ASP   B 1 39  ? 51.55400 -19.83400 32.40400  1.000 21.77069 ?  38  ASP   B O     1 
ATOM   1672 C  CB    . ASP   B 1 39  ? 54.43900 -18.57300 33.08500  1.000 26.57865 ?  38  ASP   B CB    1 
ATOM   1673 C  CG    . ASP   B 1 39  ? 55.94400 -18.69000 33.32100  1.000 34.88340 ?  38  ASP   B CG    1 
ATOM   1674 O  OD1   . ASP   B 1 39  ? 56.31300 -19.25900 34.37100  1.000 39.39462 ?  38  ASP   B OD1   1 
ATOM   1675 O  OD2   . ASP   B 1 39  ? 56.73300 -18.22200 32.46100  1.000 34.25270 -1 38  ASP   B OD2   1 
ATOM   1676 N  N     . SER   B 1 40  ? 51.61400 -19.14700 34.55800  1.000 22.14116 ?  39  SER   B N     1 
ATOM   1677 C  CA    . SER   B 1 40  ? 50.18800 -18.83400 34.62100  1.000 21.34176 ?  39  SER   B CA    1 
ATOM   1678 C  C     . SER   B 1 40  ? 50.00700 -17.41500 35.13600  1.000 24.80905 ?  39  SER   B C     1 
ATOM   1679 O  O     . SER   B 1 40  ? 50.74300 -16.97300 36.02000  1.000 23.39413 ?  39  SER   B O     1 
ATOM   1680 C  CB    . SER   B 1 40  ? 49.42600 -19.79800 35.56100  1.000 28.62390 ?  39  SER   B CB    1 
ATOM   1681 O  OG    . SER   B 1 40  ? 49.60100 -21.14400 35.16000  1.000 37.73518 ?  39  SER   B OG    1 
ATOM   1682 N  N     . TYR   B 1 41  ? 48.98600 -16.72600 34.63600  1.000 23.21721 ?  40  TYR   B N     1 
ATOM   1683 C  CA    . TYR   B 1 41  ? 48.77000 -15.33000 34.99400  1.000 22.02330 ?  40  TYR   B CA    1 
ATOM   1684 C  C     . TYR   B 1 41  ? 47.27600 -15.10800 35.14300  1.000 22.41757 ?  40  TYR   B C     1 
ATOM   1685 O  O     . TYR   B 1 41  ? 46.48100 -15.76700 34.47900  1.000 24.87723 ?  40  TYR   B O     1 
ATOM   1686 C  CB    . TYR   B 1 41  ? 49.30700 -14.35600 33.94000  1.000 24.89053 ?  40  TYR   B CB    1 
ATOM   1687 C  CG    . TYR   B 1 41  ? 50.77600 -14.51800 33.66100  1.000 24.35169 ?  40  TYR   B CG    1 
ATOM   1688 C  CD1   . TYR   B 1 41  ? 51.72800 -13.88600 34.46700  1.000 23.71257 ?  40  TYR   B CD1   1 
ATOM   1689 C  CD2   . TYR   B 1 41  ? 51.20900 -15.33200 32.62800  1.000 22.52358 ?  40  TYR   B CD2   1 
ATOM   1690 C  CE1   . TYR   B 1 41  ? 53.08500 -14.05100 34.20900  1.000 31.30336 ?  40  TYR   B CE1   1 
ATOM   1691 C  CE2   . TYR   B 1 41  ? 52.54600 -15.52100 32.38400  1.000 26.70225 ?  40  TYR   B CE2   1 
ATOM   1692 C  CZ    . TYR   B 1 41  ? 53.48100 -14.87500 33.17300  1.000 30.43362 ?  40  TYR   B CZ    1 
ATOM   1693 O  OH    . TYR   B 1 41  ? 54.81800 -15.04100 32.91400  1.000 27.61813 ?  40  TYR   B OH    1 
ATOM   1694 N  N     . ARG   B 1 42  ? 46.88700 -14.19000 36.02600  1.000 20.38250 ?  41  ARG   B N     1 
ATOM   1695 C  CA    . ARG   B 1 42  ? 45.48600 -13.80800 36.12200  1.000 20.89457 ?  41  ARG   B CA    1 
ATOM   1696 C  C     . ARG   B 1 42  ? 45.34500 -12.31400 35.91600  1.000 22.52212 ?  41  ARG   B C     1 
ATOM   1697 O  O     . ARG   B 1 42  ? 46.12500 -11.51800 36.44500  1.000 24.17393 ?  41  ARG   B O     1 
ATOM   1698 C  CB    . ARG   B 1 42  ? 44.87000 -14.22200 37.46900  1.000 26.56477 ?  41  ARG   B CB    1 
ATOM   1699 C  CG    . ARG   B 1 42  ? 44.50800 -15.67900 37.44600  1.000 33.32228 ?  41  ARG   B CG    1 
ATOM   1700 C  CD    . ARG   B 1 42  ? 44.07000 -16.18200 38.76900  1.000 40.06864 ?  41  ARG   B CD    1 
ATOM   1701 N  NE    . ARG   B 1 42  ? 42.94000 -15.48600 39.35900  1.000 37.59650 ?  41  ARG   B NE    1 
ATOM   1702 C  CZ    . ARG   B 1 42  ? 41.78500 -16.06800 39.65100  1.000 35.06909 ?  41  ARG   B CZ    1 
ATOM   1703 N  NH1   . ARG   B 1 42  ? 41.48200 -17.28100 39.21100  1.000 28.56950 ?  41  ARG   B NH1   1 
ATOM   1704 N  NH2   . ARG   B 1 42  ? 40.91800 -15.42400 40.41900  1.000 41.06265 ?  41  ARG   B NH2   1 
ATOM   1705 N  N     . LYS   B 1 43  ? 44.33600 -11.91900 35.15700  1.000 22.74031 ?  42  LYS   B N     1 
ATOM   1706 C  CA    . LYS   B 1 43  ? 44.13200 -10.49200 34.92700  1.000 19.98148 ?  42  LYS   B CA    1 
ATOM   1707 C  C     . LYS   B 1 43  ? 42.64800 -10.22200 34.75400  1.000 22.11581 ?  42  LYS   B C     1 
ATOM   1708 O  O     . LYS   B 1 43  ? 41.98000 -10.93300 34.00000  1.000 25.14515 ?  42  LYS   B O     1 
ATOM   1709 C  CB    . LYS   B 1 43  ? 44.86200 -10.00400 33.67800  1.000 23.34049 ?  42  LYS   B CB    1 
ATOM   1710 C  CG    . LYS   B 1 43  ? 44.79600 -8.48400  33.50100  1.000 25.73520 ?  42  LYS   B CG    1 
ATOM   1711 C  CD    . LYS   B 1 43  ? 45.49600 -8.07000  32.18400  1.000 25.94895 ?  42  LYS   B CD    1 
ATOM   1712 C  CE    . LYS   B 1 43  ? 45.46500 -6.56200  31.97600  1.000 25.98088 ?  42  LYS   B CE    1 
ATOM   1713 N  NZ    . LYS   B 1 43  ? 46.02300 -5.78500  33.15400  1.000 36.35077 ?  42  LYS   B NZ    1 
ATOM   1714 N  N     . GLN   B 1 44  ? 42.15800 -9.19400  35.43100  1.000 23.13423 ?  43  GLN   B N     1 
ATOM   1715 C  CA    . GLN   B 1 44  ? 40.76600 -8.76300  35.30200  1.000 27.06580 ?  43  GLN   B CA    1 
ATOM   1716 C  C     . GLN   B 1 44  ? 40.68100 -7.70500  34.20000  1.000 26.76974 ?  43  GLN   B C     1 
ATOM   1717 O  O     . GLN   B 1 44  ? 41.50500 -6.78800  34.16100  1.000 26.49693 ?  43  GLN   B O     1 
ATOM   1718 C  CB    . GLN   B 1 44  ? 40.29000 -8.21300  36.65000  1.000 30.20151 ?  43  GLN   B CB    1 
ATOM   1719 C  CG    . GLN   B 1 44  ? 38.83800 -7.88800  36.74800  1.000 42.10848 ?  43  GLN   B CG    1 
ATOM   1720 C  CD    . GLN   B 1 44  ? 38.56800 -6.84800  37.82000  1.000 40.09536 ?  43  GLN   B CD    1 
ATOM   1721 O  OE1   . GLN   B 1 44  ? 37.82000 -5.92300  37.57700  1.000 42.63561 ?  43  GLN   B OE1   1 
ATOM   1722 N  NE2   . GLN   B 1 44  ? 39.20700 -6.98000  39.00000  1.000 39.26759 ?  43  GLN   B NE2   1 
ATOM   1723 N  N     . VAL   B 1 45  ? 39.73200 -7.85500  33.26600  1.000 26.60747 ?  44  VAL   B N     1 
ATOM   1724 C  CA    . VAL   B 1 45  ? 39.63700 -6.96400  32.10700  1.000 29.07185 ?  44  VAL   B CA    1 
ATOM   1725 C  C     . VAL   B 1 45  ? 38.17900 -6.59700  31.84600  1.000 28.19312 ?  44  VAL   B C     1 
ATOM   1726 O  O     . VAL   B 1 45  ? 37.26000 -7.16200  32.43300  1.000 29.03851 ?  44  VAL   B O     1 
ATOM   1727 C  CB    . VAL   B 1 45  ? 40.22500 -7.59700  30.83800  1.000 29.21639 ?  44  VAL   B CB    1 
ATOM   1728 C  CG1   . VAL   B 1 45  ? 41.76300 -7.74900  30.96400  1.000 29.19866 ?  44  VAL   B CG1   1 
ATOM   1729 C  CG2   . VAL   B 1 45  ? 39.52700 -8.95100  30.60100  1.000 27.64499 ?  44  VAL   B CG2   1 
ATOM   1730 N  N     . VAL   B 1 46  ? 37.97100 -5.65300  30.92400  1.000 28.42548 ?  45  VAL   B N     1 
ATOM   1731 C  CA    . VAL   B 1 46  ? 36.61600 -5.30300  30.47600  1.000 28.89742 ?  45  VAL   B CA    1 
ATOM   1732 C  C     . VAL   B 1 46  ? 36.59400 -5.41700  28.96300  1.000 31.21909 ?  45  VAL   B C     1 
ATOM   1733 O  O     . VAL   B 1 46  ? 37.39600 -4.77100  28.28100  1.000 33.94524 ?  45  VAL   B O     1 
ATOM   1734 C  CB    . VAL   B 1 46  ? 36.18600 -3.89900  30.94200  1.000 39.13833 ?  45  VAL   B CB    1 
ATOM   1735 C  CG1   . VAL   B 1 46  ? 34.79200 -3.54900  30.43300  1.000 32.64159 ?  45  VAL   B CG1   1 
ATOM   1736 C  CG2   . VAL   B 1 46  ? 36.18600 -3.82800  32.45400  1.000 36.76924 ?  45  VAL   B CG2   1 
ATOM   1737 N  N     . ILE   B 1 47  ? 35.71200 -6.27200  28.44100  1.000 29.42827 ?  46  ILE   B N     1 
ATOM   1738 C  CA    . ILE   B 1 47  ? 35.65700 -6.57900  27.01100  1.000 27.71721 ?  46  ILE   B CA    1 
ATOM   1739 C  C     . ILE   B 1 47  ? 34.22000 -6.34100  26.55000  1.000 33.76891 ?  46  ILE   B C     1 
ATOM   1740 O  O     . ILE   B 1 47  ? 33.29000 -6.99400  27.04300  1.000 34.12874 ?  46  ILE   B O     1 
ATOM   1741 C  CB    . ILE   B 1 47  ? 36.11700 -8.01200  26.70700  1.000 30.49255 ?  46  ILE   B CB    1 
ATOM   1742 C  CG1   . ILE   B 1 47  ? 37.58300 -8.17700  27.13500  1.000 32.29335 ?  46  ILE   B CG1   1 
ATOM   1743 C  CG2   . ILE   B 1 47  ? 36.03600 -8.31000  25.18000  1.000 32.95018 ?  46  ILE   B CG2   1 
ATOM   1744 C  CD1   . ILE   B 1 47  ? 38.07400 -9.58800  27.04800  1.000 24.05310 ?  46  ILE   B CD1   1 
ATOM   1745 N  N     . ASP   B 1 48  ? 34.03900 -5.39300  25.62700  1.000 35.16627 ?  47  ASP   B N     1 
ATOM   1746 C  CA    . ASP   B 1 48  ? 32.69100 -5.02100  25.15800  1.000 37.91257 ?  47  ASP   B CA    1 
ATOM   1747 C  C     . ASP   B 1 48  ? 31.77600 -4.68700  26.33900  1.000 36.29393 ?  47  ASP   B C     1 
ATOM   1748 O  O     . ASP   B 1 48  ? 30.60700 -5.08700  26.39500  1.000 40.28881 ?  47  ASP   B O     1 
ATOM   1749 C  CB    . ASP   B 1 48  ? 32.08700 -6.12200  24.28500  1.000 33.65147 ?  47  ASP   B CB    1 
ATOM   1750 C  CG    . ASP   B 1 48  ? 32.91100 -6.39500  23.03100  1.000 31.49606 ?  47  ASP   B CG    1 
ATOM   1751 O  OD1   . ASP   B 1 48  ? 33.60500 -5.46600  22.55800  1.000 36.00075 ?  47  ASP   B OD1   1 
ATOM   1752 O  OD2   . ASP   B 1 48  ? 32.88000 -7.53400  22.51500  1.000 38.31928 -1 47  ASP   B OD2   1 
ATOM   1753 N  N     . GLY   B 1 49  ? 32.32400 -3.94800  27.30100  1.000 38.23192 ?  48  GLY   B N     1 
ATOM   1754 C  CA    . GLY   B 1 49  ? 31.58500 -3.49600  28.46000  1.000 34.14215 ?  48  GLY   B CA    1 
ATOM   1755 C  C     . GLY   B 1 49  ? 31.31300 -4.53300  29.52500  1.000 38.14569 ?  48  GLY   B C     1 
ATOM   1756 O  O     . GLY   B 1 49  ? 30.66900 -4.20300  30.52400  1.000 41.76685 ?  48  GLY   B O     1 
ATOM   1757 N  N     . GLU   B 1 50  ? 31.77000 -5.77400  29.37100  1.000 34.58275 ?  49  GLU   B N     1 
ATOM   1758 C  CA    . GLU   B 1 50  ? 31.52500 -6.80000  30.38000  1.000 35.35853 ?  49  GLU   B CA    1 
ATOM   1759 C  C     . GLU   B 1 50  ? 32.83200 -7.17400  31.06500  1.000 38.29551 ?  49  GLU   B C     1 
ATOM   1760 O  O     . GLU   B 1 50  ? 33.80800 -7.50400  30.39000  1.000 33.96177 ?  49  GLU   B O     1 
ATOM   1761 C  CB    . GLU   B 1 50  ? 30.87800 -8.03800  29.76700  1.000 38.72849 ?  49  GLU   B CB    1 
ATOM   1762 C  CG    . GLU   B 1 50  ? 29.44900 -7.79100  29.29000  1.000 45.14303 ?  49  GLU   B CG    1 
ATOM   1763 C  CD    . GLU   B 1 50  ? 28.73500 -9.07600  28.88400  1.000 53.70084 ?  49  GLU   B CD    1 
ATOM   1764 O  OE1   . GLU   B 1 50  ? 29.38400 -10.15600 28.92200  1.000 57.49107 ?  49  GLU   B OE1   1 
ATOM   1765 O  OE2   . GLU   B 1 50  ? 27.53000 -9.00100  28.53800  1.000 56.58321 ?  49  GLU   B OE2   1 
ATOM   1766 N  N     . THR   B 1 51  ? 32.82800 -7.12700  32.39700  1.000 32.03550 ?  50  THR   B N     1 
ATOM   1767 C  CA    . THR   B 1 51  ? 34.01000 -7.43000  33.19500  1.000 36.80549 ?  50  THR   B CA    1 
ATOM   1768 C  C     . THR   B 1 51  ? 34.24800 -8.93400  33.22100  1.000 35.85463 ?  50  THR   B C     1 
ATOM   1769 O  O     . THR   B 1 51  ? 33.31300 -9.72600  33.34400  1.000 35.11420 ?  50  THR   B O     1 
ATOM   1770 C  CB    . THR   B 1 51  ? 33.84800 -6.89300  34.62000  1.000 39.91576 ?  50  THR   B CB    1 
ATOM   1771 O  OG1   . THR   B 1 51  ? 33.69300 -5.47100  34.56900  1.000 40.18554 ?  50  THR   B OG1   1 
ATOM   1772 C  CG2   . THR   B 1 51  ? 35.07400 -7.22000  35.48300  1.000 36.91681 ?  50  THR   B CG2   1 
ATOM   1773 N  N     . CYS   B 1 52  ? 35.50800 -9.33900  33.09200  1.000 29.40287 ?  51  CYS   B N     1 
ATOM   1774 C  CA    . CYS   B 1 52  ? 35.77700 -10.75800 33.21600  1.000 27.34585 ?  51  CYS   B CA    1 
ATOM   1775 C  C     . CYS   B 1 52  ? 37.21800 -10.95600 33.65600  1.000 28.97385 ?  51  CYS   B C     1 
ATOM   1776 O  O     . CYS   B 1 52  ? 38.03500 -10.03300 33.62500  1.000 28.40084 ?  51  CYS   B O     1 
ATOM   1777 C  CB    . CYS   B 1 52  ? 35.52000 -11.50500 31.90500  1.000 26.23632 ?  51  CYS   B CB    1 
ATOM   1778 S  SG    . CYS   B 1 52  ? 36.46400 -10.82600 30.55400  1.000 33.15598 ?  51  CYS   B SG    1 
ATOM   1779 N  N     . LEU   B 1 53  ? 37.51600 -12.19800 34.02700  1.000 26.30489 ?  52  LEU   B N     1 
ATOM   1780 C  CA    . LEU   B 1 53  ? 38.81200 -12.60600 34.57200  1.000 23.78052 ?  52  LEU   B CA    1 
ATOM   1781 C  C     . LEU   B 1 53  ? 39.49900 -13.53100 33.57100  1.000 28.65882 ?  52  LEU   B C     1 
ATOM   1782 O  O     . LEU   B 1 53  ? 38.95200 -14.58000 33.22000  1.000 28.13421 ?  52  LEU   B O     1 
ATOM   1783 C  CB    . LEU   B 1 53  ? 38.59400 -13.31600 35.91200  1.000 22.90300 ?  52  LEU   B CB    1 
ATOM   1784 C  CG    . LEU   B 1 53  ? 39.80500 -13.65800 36.79200  1.000 29.66283 ?  52  LEU   B CG    1 
ATOM   1785 C  CD1   . LEU   B 1 53  ? 40.68500 -12.42500 36.98100  1.000 23.68830 ?  52  LEU   B CD1   1 
ATOM   1786 C  CD2   . LEU   B 1 53  ? 39.26900 -14.15100 38.11100  1.000 37.48138 ?  52  LEU   B CD2   1 
ATOM   1787 N  N     . LEU   B 1 54  ? 40.69800 -13.14900 33.12500  1.000 23.99853 ?  53  LEU   B N     1 
ATOM   1788 C  CA    . LEU   B 1 54  ? 41.49400 -13.99300 32.23400  1.000 25.05334 ?  53  LEU   B CA    1 
ATOM   1789 C  C     . LEU   B 1 54  ? 42.45300 -14.83000 33.07100  1.000 24.37545 ?  53  LEU   B C     1 
ATOM   1790 O  O     . LEU   B 1 54  ? 43.17700 -14.29400 33.89300  1.000 25.31702 ?  53  LEU   B O     1 
ATOM   1791 C  CB    . LEU   B 1 54  ? 42.28300 -13.15100 31.23600  1.000 25.90184 ?  53  LEU   B CB    1 
ATOM   1792 C  CG    . LEU   B 1 54  ? 41.43300 -12.10700 30.50100  1.000 28.98808 ?  53  LEU   B CG    1 
ATOM   1793 C  CD1   . LEU   B 1 54  ? 42.24700 -11.29400 29.47100  1.000 25.98669 ?  53  LEU   B CD1   1 
ATOM   1794 C  CD2   . LEU   B 1 54  ? 40.13500 -12.74000 29.87300  1.000 26.43801 ?  53  LEU   B CD2   1 
ATOM   1795 N  N     . ASP   B 1 55  ? 42.42800 -16.13400 32.86800  1.000 24.67137 ?  54  ASP   B N     1 
ATOM   1796 C  CA    . ASP   B 1 55  ? 43.36600 -17.08300 33.45100  1.000 23.28879 ?  54  ASP   B CA    1 
ATOM   1797 C  C     . ASP   B 1 55  ? 44.23500 -17.56900 32.30500  1.000 23.70629 ?  54  ASP   B C     1 
ATOM   1798 O  O     . ASP   B 1 55  ? 43.77000 -18.35800 31.48700  1.000 27.73565 ?  54  ASP   B O     1 
ATOM   1799 C  CB    . ASP   B 1 55  ? 42.56600 -18.22700 34.04300  1.000 28.03090 ?  54  ASP   B CB    1 
ATOM   1800 C  CG    . ASP   B 1 55  ? 43.24400 -18.86900 35.18700  1.000 42.87553 ?  54  ASP   B CG    1 
ATOM   1801 O  OD1   . ASP   B 1 55  ? 44.49800 -18.94900 35.15700  1.000 45.13194 -1 54  ASP   B OD1   1 
ATOM   1802 O  OD2   . ASP   B 1 55  ? 42.51200 -19.27800 36.11800  1.000 47.15450 ?  54  ASP   B OD2   1 
ATOM   1803 N  N     . ILE   B 1 56  ? 45.47500 -17.10900 32.21000  1.000 22.59288 ?  55  ILE   B N     1 
ATOM   1804 C  CA    . ILE   B 1 56  ? 46.26100 -17.34300 31.00300  1.000 22.49570 ?  55  ILE   B CA    1 
ATOM   1805 C  C     . ILE   B 1 56  ? 47.37400 -18.32100 31.32500  1.000 23.31656 ?  55  ILE   B C     1 
ATOM   1806 O  O     . ILE   B 1 56  ? 48.14800 -18.10300 32.26500  1.000 23.44004 ?  55  ILE   B O     1 
ATOM   1807 C  CB    . ILE   B 1 56  ? 46.82300 -16.03600 30.43800  1.000 24.82267 ?  55  ILE   B CB    1 
ATOM   1808 C  CG1   . ILE   B 1 56  ? 45.64000 -15.15100 30.01500  1.000 26.54805 ?  55  ILE   B CG1   1 
ATOM   1809 C  CG2   . ILE   B 1 56  ? 47.73800 -16.31000 29.23700  1.000 25.65981 ?  55  ILE   B CG2   1 
ATOM   1810 C  CD1   . ILE   B 1 56  ? 46.06300 -13.75700 29.77700  1.000 29.94029 ?  55  ILE   B CD1   1 
ATOM   1811 N  N     . LEU   B 1 57  ? 47.48800 -19.36100 30.51700  1.000 20.24559 ?  56  LEU   B N     1 
ATOM   1812 C  CA    . LEU   B 1 57  ? 48.55900 -20.33100 30.64600  1.000 20.94497 ?  56  LEU   B CA    1 
ATOM   1813 C  C     . LEU   B 1 57  ? 49.49000 -20.14000 29.45600  1.000 23.89293 ?  56  LEU   B C     1 
ATOM   1814 O  O     . LEU   B 1 57  ? 49.07700 -20.31300 28.29000  1.000 23.24311 ?  56  LEU   B O     1 
ATOM   1815 C  CB    . LEU   B 1 57  ? 48.01500 -21.76100 30.69700  1.000 20.66158 ?  56  LEU   B CB    1 
ATOM   1816 C  CG    . LEU   B 1 57  ? 49.04300 -22.87800 30.89200  1.000 24.16087 ?  56  LEU   B CG    1 
ATOM   1817 C  CD1   . LEU   B 1 57  ? 49.44800 -22.92400 32.36800  1.000 30.91752 ?  56  LEU   B CD1   1 
ATOM   1818 C  CD2   . LEU   B 1 57  ? 48.40200 -24.18200 30.47500  1.000 24.29596 ?  56  LEU   B CD2   1 
ATOM   1819 N  N     . ASP   B 1 58  ? 50.72900 -19.79600 29.75600  1.000 20.19004 ?  57  ASP   B N     1 
ATOM   1820 C  CA    . ASP   B 1 58  ? 51.76500 -19.53800 28.75200  1.000 20.49936 ?  57  ASP   B CA    1 
ATOM   1821 C  C     . ASP   B 1 58  ? 52.59600 -20.81700 28.68700  1.000 25.24895 ?  57  ASP   B C     1 
ATOM   1822 O  O     . ASP   B 1 58  ? 53.26700 -21.17100 29.65400  1.000 24.84241 ?  57  ASP   B O     1 
ATOM   1823 C  CB    . ASP   B 1 58  ? 52.56100 -18.29500 29.19700  1.000 23.72598 ?  57  ASP   B CB    1 
ATOM   1824 C  CG    . ASP   B 1 58  ? 53.70900 -17.90100 28.26100  1.000 25.48843 ?  57  ASP   B CG    1 
ATOM   1825 O  OD1   . ASP   B 1 58  ? 53.68200 -18.29500 27.07600  1.000 29.92486 ?  57  ASP   B OD1   1 
ATOM   1826 O  OD2   . ASP   B 1 58  ? 54.66700 -17.22100 28.74300  1.000 28.33107 -1 57  ASP   B OD2   1 
ATOM   1827 N  N     . THR   B 1 59  ? 52.52800 -21.53800 27.57400  1.000 22.83521 ?  58  THR   B N     1 
ATOM   1828 C  CA    . THR   B 1 59  ? 53.14300 -22.85700 27.50700  1.000 22.97219 ?  58  THR   B CA    1 
ATOM   1829 C  C     . THR   B 1 59  ? 54.51600 -22.83200 26.82200  1.000 23.76401 ?  58  THR   B C     1 
ATOM   1830 O  O     . THR   B 1 59  ? 54.96100 -21.82800 26.23100  1.000 26.03234 ?  58  THR   B O     1 
ATOM   1831 C  CB    . THR   B 1 59  ? 52.23100 -23.82400 26.75500  1.000 22.74413 ?  58  THR   B CB    1 
ATOM   1832 O  OG1   . THR   B 1 59  ? 52.15800 -23.39300 25.37400  1.000 21.97919 ?  58  THR   B OG1   1 
ATOM   1833 C  CG2   . THR   B 1 59  ? 50.82200 -23.84200 27.40100  1.000 23.52739 ?  58  THR   B CG2   1 
ATOM   1834 N  N     . ALA   B 1 60  ? 55.18400 -23.98600 26.86500  1.000 24.17093 ?  59  ALA   B N     1 
ATOM   1835 C  CA    . ALA   B 1 60  ? 56.48400 -24.14600 26.21700  1.000 23.06806 ?  59  ALA   B CA    1 
ATOM   1836 C  C     . ALA   B 1 60  ? 56.29900 -24.64800 24.78700  1.000 25.52027 ?  59  ALA   B C     1 
ATOM   1837 O  O     . ALA   B 1 60  ? 55.54100 -25.58100 24.54700  1.000 26.55339 ?  59  ALA   B O     1 
ATOM   1838 C  CB    . ALA   B 1 60  ? 57.36000 -25.13000 27.00500  1.000 25.40314 ?  59  ALA   B CB    1 
ATOM   1839 N  N     . GLY   B 1 61  ? 57.00300 -24.04700 23.84900  1.000 27.80962 ?  60  GLY   B N     1 
ATOM   1840 C  CA    . GLY   B 1 61  ? 56.85900 -24.57500 22.50100  1.000 28.47922 ?  60  GLY   B CA    1 
ATOM   1841 C  C     . GLY   B 1 61  ? 57.66300 -25.82200 22.19300  1.000 30.59351 ?  60  GLY   B C     1 
ATOM   1842 O  O     . GLY   B 1 61  ? 57.53800 -26.35300 21.09100  1.000 33.20617 ?  60  GLY   B O     1 
ATOM   1843 N  N     . GLN   B 1 62  ? 58.46600 -26.32500 23.14000  1.000 27.69395 ?  61  GLN   B N     1 
ATOM   1844 C  CA    . GLN   B 1 62  ? 59.47800 -27.33800 22.83100  1.000 33.60812 ?  61  GLN   B CA    1 
ATOM   1845 C  C     . GLN   B 1 62  ? 58.83100 -28.60100 22.26600  1.000 32.94542 ?  61  GLN   B C     1 
ATOM   1846 O  O     . GLN   B 1 62  ? 57.97600 -29.20900 22.90500  1.000 37.47806 ?  61  GLN   B O     1 
ATOM   1847 C  CB    . GLN   B 1 62  ? 60.28400 -27.65100 24.09200  1.000 31.36709 ?  61  GLN   B CB    1 
ATOM   1848 C  CG    . GLN   B 1 62  ? 60.76900 -26.39100 24.83100  1.000 34.22811 ?  61  GLN   B CG    1 
ATOM   1849 C  CD    . GLN   B 1 62  ? 62.19700 -26.08300 24.48300  1.000 37.63682 ?  61  GLN   B CD    1 
ATOM   1850 O  OE1   . GLN   B 1 62  ? 62.94500 -26.98400 24.09900  1.000 47.85881 ?  61  GLN   B OE1   1 
ATOM   1851 N  NE2   . GLN   B 1 62  ? 62.58500 -24.81200 24.56300  1.000 35.13241 ?  61  GLN   B NE2   1 
ATOM   1852 N  N     . GLU   B 1 63  ? 59.23100 -28.98700 21.05300  1.000 37.63800 ?  62  GLU   B N     1 
ATOM   1853 C  CA    . GLU   B 1 63  ? 58.56100 -30.09700 20.37300  1.000 42.87264 ?  62  GLU   B CA    1 
ATOM   1854 C  C     . GLU   B 1 63  ? 58.83000 -31.44000 21.05800  1.000 40.88613 ?  62  GLU   B C     1 
ATOM   1855 O  O     . GLU   B 1 63  ? 57.99800 -32.35700 20.97900  1.000 39.47100 ?  62  GLU   B O     1 
ATOM   1856 C  CB    . GLU   B 1 63  ? 58.99400 -30.13300 18.90300  1.000 39.54533 ?  62  GLU   B CB    1 
ATOM   1857 C  CG    . GLU   B 1 63  ? 58.11800 -30.98300 17.98400  1.000 47.48973 ?  62  GLU   B CG    1 
ATOM   1858 C  CD    . GLU   B 1 63  ? 56.63600 -30.58700 17.98900  1.000 54.46666 ?  62  GLU   B CD    1 
ATOM   1859 O  OE1   . GLU   B 1 63  ? 56.30800 -29.38600 18.17600  1.000 54.51084 ?  62  GLU   B OE1   1 
ATOM   1860 O  OE2   . GLU   B 1 63  ? 55.79200 -31.49700 17.80700  1.000 60.80921 ?  62  GLU   B OE2   1 
ATOM   1861 N  N     . GLU   B 1 64  ? 59.95900 -31.57000 21.75700  1.000 40.39646 ?  63  GLU   B N     1 
ATOM   1862 C  CA    . GLU   B 1 64  ? 60.26700 -32.83600 22.41800  1.000 39.01915 ?  63  GLU   B CA    1 
ATOM   1863 C  C     . GLU   B 1 64  ? 59.29700 -33.16900 23.55400  1.000 40.08249 ?  63  GLU   B C     1 
ATOM   1864 O  O     . GLU   B 1 64  ? 59.26600 -34.32100 23.99900  1.000 40.27794 ?  63  GLU   B O     1 
ATOM   1865 C  CB    . GLU   B 1 64  ? 61.70900 -32.82100 22.93800  1.000 37.58390 ?  63  GLU   B CB    1 
ATOM   1866 C  CG    . GLU   B 1 64  ? 61.96000 -31.88600 24.09900  1.000 39.89512 ?  63  GLU   B CG    1 
ATOM   1867 C  CD    . GLU   B 1 64  ? 63.43400 -31.54900 24.31000  1.000 49.76770 ?  63  GLU   B CD    1 
ATOM   1868 O  OE1   . GLU   B 1 64  ? 64.18400 -32.36100 24.92200  1.000 46.77747 ?  63  GLU   B OE1   1 
ATOM   1869 O  OE2   . GLU   B 1 64  ? 63.83500 -30.44100 23.88000  1.000 53.88933 -1 63  GLU   B OE2   1 
ATOM   1870 N  N     . TYR   B 1 65  ? 58.49600 -32.21400 24.03500  1.000 36.52130 ?  64  TYR   B N     1 
ATOM   1871 C  CA    . TYR   B 1 65  ? 57.52400 -32.50900 25.08400  1.000 40.43253 ?  64  TYR   B CA    1 
ATOM   1872 C  C     . TYR   B 1 65  ? 56.08200 -32.50700 24.56100  1.000 39.98257 ?  64  TYR   B C     1 
ATOM   1873 O  O     . TYR   B 1 65  ? 55.14700 -32.17600 25.30100  1.000 36.38450 ?  64  TYR   B O     1 
ATOM   1874 C  CB    . TYR   B 1 65  ? 57.70300 -31.54800 26.26400  1.000 36.49244 ?  64  TYR   B CB    1 
ATOM   1875 C  CG    . TYR   B 1 65  ? 59.11200 -31.58500 26.82800  1.000 31.42004 ?  64  TYR   B CG    1 
ATOM   1876 C  CD1   . TYR   B 1 65  ? 59.61100 -32.73900 27.41100  1.000 28.60988 ?  64  TYR   B CD1   1 
ATOM   1877 C  CD2   . TYR   B 1 65  ? 59.95600 -30.46900 26.75200  1.000 32.73009 ?  64  TYR   B CD2   1 
ATOM   1878 C  CE1   . TYR   B 1 65  ? 60.91700 -32.80200 27.88600  1.000 30.43284 ?  64  TYR   B CE1   1 
ATOM   1879 C  CE2   . TYR   B 1 65  ? 61.25400 -30.50600 27.24300  1.000 28.22617 ?  64  TYR   B CE2   1 
ATOM   1880 C  CZ    . TYR   B 1 65  ? 61.73200 -31.68600 27.83000  1.000 26.77465 ?  64  TYR   B CZ    1 
ATOM   1881 O  OH    . TYR   B 1 65  ? 63.02700 -31.78500 28.31700  1.000 27.71080 ?  64  TYR   B OH    1 
ATOM   1882 N  N     . SER   B 1 66  ? 55.88900 -32.95500 23.30600  1.000 40.04933 ?  65  SER   B N     1 
ATOM   1883 C  CA    . SER   B 1 66  ? 54.55900 -32.95800 22.68200  1.000 41.29271 ?  65  SER   B CA    1 
ATOM   1884 C  C     . SER   B 1 66  ? 53.53100 -33.75800 23.48300  1.000 46.17300 ?  65  SER   B C     1 
ATOM   1885 O  O     . SER   B 1 66  ? 52.34700 -33.39000 23.52900  1.000 49.13798 ?  65  SER   B O     1 
ATOM   1886 C  CB    . SER   B 1 66  ? 54.64000 -33.52800 21.26600  1.000 46.43901 ?  65  SER   B CB    1 
ATOM   1887 O  OG    . SER   B 1 66  ? 55.84800 -33.16000 20.62500  1.000 53.11150 ?  65  SER   B OG    1 
ATOM   1888 N  N     . ALA   B 1 67  ? 53.93800 -34.88500 24.07500  1.000 44.99228 ?  66  ALA   B N     1 
ATOM   1889 C  CA    . ALA   B 1 67  ? 52.96600 -35.70400 24.79500  1.000 46.87652 ?  66  ALA   B CA    1 
ATOM   1890 C  C     . ALA   B 1 67  ? 52.49900 -35.04700 26.08800  1.000 48.35038 ?  66  ALA   B C     1 
ATOM   1891 O  O     . ALA   B 1 67  ? 51.40300 -35.36200 26.57200  1.000 54.98143 ?  66  ALA   B O     1 
ATOM   1892 C  CB    . ALA   B 1 67  ? 53.54800 -37.09100 25.08600  1.000 47.38300 ?  66  ALA   B CB    1 
ATOM   1893 N  N     . MET   B 1 68  ? 53.29300 -34.13800 26.65300  1.000 43.60683 ?  67  MET   B N     1 
ATOM   1894 C  CA    . MET   B 1 68  ? 52.92200 -33.45600 27.88600  1.000 37.20305 ?  67  MET   B CA    1 
ATOM   1895 C  C     . MET   B 1 68  ? 51.83600 -32.39600 27.68600  1.000 39.49266 ?  67  MET   B C     1 
ATOM   1896 O  O     . MET   B 1 68  ? 51.40300 -31.78100 28.66800  1.000 38.95185 ?  67  MET   B O     1 
ATOM   1897 C  CB    . MET   B 1 68  ? 54.17000 -32.82100 28.51600  1.000 40.37305 ?  67  MET   B CB    1 
ATOM   1898 C  CG    . MET   B 1 68  ? 55.11700 -33.82300 29.20900  1.000 42.08148 ?  67  MET   B CG    1 
ATOM   1899 S  SD    . MET   B 1 68  ? 56.04000 -34.81700 28.01900  1.000 64.74821 ?  67  MET   B SD    1 
ATOM   1900 C  CE    . MET   B 1 68  ? 56.81800 -36.04700 29.07300  1.000 44.56231 ?  67  MET   B CE    1 
ATOM   1901 N  N     . ARG   B 1 69  ? 51.36200 -32.17900 26.45800  1.000 40.83668 ?  68  ARG   B N     1 
ATOM   1902 C  CA    . ARG   B 1 69  ? 50.42500 -31.09000 26.21200  1.000 40.09665 ?  68  ARG   B CA    1 
ATOM   1903 C  C     . ARG   B 1 69  ? 48.98300 -31.46600 26.49500  1.000 40.14004 ?  68  ARG   B C     1 
ATOM   1904 O  O     . ARG   B 1 69  ? 48.17300 -30.57700 26.78700  1.000 40.50295 ?  68  ARG   B O     1 
ATOM   1905 C  CB    . ARG   B 1 69  ? 50.53200 -30.61300 24.76400  1.000 38.25171 ?  68  ARG   B CB    1 
ATOM   1906 C  CG    . ARG   B 1 69  ? 51.87300 -30.02200 24.41700  1.000 38.09868 ?  68  ARG   B CG    1 
ATOM   1907 C  CD    . ARG   B 1 69  ? 51.88600 -29.58200 22.95500  1.000 38.88289 ?  68  ARG   B CD    1 
ATOM   1908 N  NE    . ARG   B 1 69  ? 53.24000 -29.32100 22.49200  1.000 42.16988 ?  68  ARG   B NE    1 
ATOM   1909 C  CZ    . ARG   B 1 69  ? 53.62200 -29.43400 21.22900  1.000 39.34504 ?  68  ARG   B CZ    1 
ATOM   1910 N  NH1   . ARG   B 1 69  ? 52.76600 -29.78100 20.28000  1.000 42.39008 ?  68  ARG   B NH1   1 
ATOM   1911 N  NH2   . ARG   B 1 69  ? 54.89400 -29.20700 20.91300  1.000 46.85910 ?  68  ARG   B NH2   1 
ATOM   1912 N  N     . ASP   B 1 70  ? 48.64500 -32.75000 26.41400  1.000 38.50214 ?  69  ASP   B N     1 
ATOM   1913 C  CA    . ASP   B 1 70  ? 47.24400 -33.15100 26.46700  1.000 41.10920 ?  69  ASP   B CA    1 
ATOM   1914 C  C     . ASP   B 1 70  ? 46.54500 -32.61000 27.71800  1.000 39.67890 ?  69  ASP   B C     1 
ATOM   1915 O  O     . ASP   B 1 70  ? 45.41200 -32.12400 27.63700  1.000 36.27296 ?  69  ASP   B O     1 
ATOM   1916 C  CB    . ASP   B 1 70  ? 47.14500 -34.67800 26.38200  1.000 42.21601 ?  69  ASP   B CB    1 
ATOM   1917 C  CG    . ASP   B 1 70  ? 47.77300 -35.23900 25.10000  1.000 50.91865 ?  69  ASP   B CG    1 
ATOM   1918 O  OD1   . ASP   B 1 70  ? 48.67600 -34.59200 24.51700  1.000 49.90274 ?  69  ASP   B OD1   1 
ATOM   1919 O  OD2   . ASP   B 1 70  ? 47.34800 -36.33000 24.66600  1.000 56.65064 -1 69  ASP   B OD2   1 
ATOM   1920 N  N     . GLN   B 1 71  ? 47.22700 -32.62400 28.87100  1.000 43.36997 ?  70  GLN   B N     1 
ATOM   1921 C  CA    . GLN   B 1 71  ? 46.57600 -32.23400 30.12400  1.000 41.88719 ?  70  GLN   B CA    1 
ATOM   1922 C  C     . GLN   B 1 71  ? 46.13400 -30.77400 30.10700  1.000 36.58941 ?  70  GLN   B C     1 
ATOM   1923 O  O     . GLN   B 1 71  ? 45.02400 -30.45000 30.55300  1.000 39.17912 ?  70  GLN   B O     1 
ATOM   1924 C  CB    . GLN   B 1 71  ? 47.50700 -32.49000 31.31100  1.000 40.83177 ?  70  GLN   B CB    1 
ATOM   1925 C  CG    . GLN   B 1 71  ? 48.95000 -32.00600 31.06700  1.000 41.71972 ?  70  GLN   B CG    1 
ATOM   1926 C  CD    . GLN   B 1 71  ? 49.55400 -31.29600 32.26000  1.000 46.51360 ?  70  GLN   B CD    1 
ATOM   1927 O  OE1   . GLN   B 1 71  ? 49.53000 -30.05800 32.34700  1.000 49.13663 ?  70  GLN   B OE1   1 
ATOM   1928 N  NE2   . GLN   B 1 71  ? 50.11500 -32.07200 33.18400  1.000 50.07555 ?  70  GLN   B NE2   1 
ATOM   1929 N  N     . TYR   B 1 72  ? 46.96500 -29.86600 29.59500  1.000 35.50388 ?  71  TYR   B N     1 
ATOM   1930 C  CA    . TYR   B 1 72  ? 46.48000 -28.49400 29.62600  1.000 34.40685 ?  71  TYR   B CA    1 
ATOM   1931 C  C     . TYR   B 1 72  ? 45.53000 -28.18300 28.47200  1.000 28.42746 ?  71  TYR   B C     1 
ATOM   1932 O  O     . TYR   B 1 72  ? 44.71600 -27.25900 28.59000  1.000 31.04745 ?  71  TYR   B O     1 
ATOM   1933 C  CB    . TYR   B 1 72  ? 47.65100 -27.51300 29.70500  1.000 32.94511 ?  71  TYR   B CB    1 
ATOM   1934 C  CG    . TYR   B 1 72  ? 48.58800 -27.44100 28.53600  1.000 35.33855 ?  71  TYR   B CG    1 
ATOM   1935 C  CD1   . TYR   B 1 72  ? 48.14800 -27.03100 27.28600  1.000 32.44803 ?  71  TYR   B CD1   1 
ATOM   1936 C  CD2   . TYR   B 1 72  ? 49.93800 -27.71300 28.70900  1.000 35.84758 ?  71  TYR   B CD2   1 
ATOM   1937 C  CE1   . TYR   B 1 72  ? 49.04000 -26.94500 26.22200  1.000 34.99846 ?  71  TYR   B CE1   1 
ATOM   1938 C  CE2   . TYR   B 1 72  ? 50.82400 -27.61900 27.67500  1.000 37.35318 ?  71  TYR   B CE2   1 
ATOM   1939 C  CZ    . TYR   B 1 72  ? 50.37600 -27.23500 26.43900  1.000 31.89570 ?  71  TYR   B CZ    1 
ATOM   1940 O  OH    . TYR   B 1 72  ? 51.26600 -27.13900 25.39400  1.000 46.72134 ?  71  TYR   B OH    1 
ATOM   1941 N  N     . MET   B 1 73  ? 45.55100 -28.97000 27.39500  1.000 31.03209 ?  72  MET   B N     1 
ATOM   1942 C  CA    . MET   B 1 73  ? 44.52400 -28.78200 26.37300  1.000 29.36278 ?  72  MET   B CA    1 
ATOM   1943 C  C     . MET   B 1 73  ? 43.15900 -29.25200 26.86000  1.000 34.31256 ?  72  MET   B C     1 
ATOM   1944 O  O     . MET   B 1 73  ? 42.14000 -28.68300 26.46700  1.000 32.22668 ?  72  MET   B O     1 
ATOM   1945 C  CB    . MET   B 1 73  ? 44.92800 -29.49300 25.08400  1.000 32.29981 ?  72  MET   B CB    1 
ATOM   1946 C  CG    . MET   B 1 73  ? 46.17100 -28.87200 24.44300  1.000 31.69735 ?  72  MET   B CG    1 
ATOM   1947 S  SD    . MET   B 1 73  ? 46.80300 -29.83800 23.04400  1.000 36.35564 ?  72  MET   B SD    1 
ATOM   1948 C  CE    . MET   B 1 73  ? 48.12800 -28.75700 22.51600  1.000 34.35654 ?  72  MET   B CE    1 
ATOM   1949 N  N     . ARG   B 1 74  ? 43.11100 -30.26400 27.73200  1.000 35.23855 ?  73  ARG   B N     1 
ATOM   1950 C  CA    . ARG   B 1 74  ? 41.82400 -30.66700 28.29600  1.000 35.10041 ?  73  ARG   B CA    1 
ATOM   1951 C  C     . ARG   B 1 74  ? 41.23800 -29.55500 29.15200  1.000 35.15503 ?  73  ARG   B C     1 
ATOM   1952 O  O     . ARG   B 1 74  ? 40.03500 -29.26700 29.07600  1.000 35.03111 ?  73  ARG   B O     1 
ATOM   1953 C  CB    . ARG   B 1 74  ? 41.96800 -31.95400 29.11400  1.000 37.09663 ?  73  ARG   B CB    1 
ATOM   1954 C  CG    . ARG   B 1 74  ? 41.82200 -33.23600 28.29100  1.000 47.91667 ?  73  ARG   B CG    1 
ATOM   1955 C  CD    . ARG   B 1 74  ? 41.76700 -34.53000 29.13700  1.000 44.52037 ?  73  ARG   B CD    1 
ATOM   1956 N  NE    . ARG   B 1 74  ? 43.05800 -34.84200 29.73900  1.000 49.18239 ?  73  ARG   B NE    1 
ATOM   1957 C  CZ    . ARG   B 1 74  ? 44.01600 -35.55300 29.15400  1.000 49.35599 ?  73  ARG   B CZ    1 
ATOM   1958 N  NH1   . ARG   B 1 74  ? 43.84100 -36.09400 27.95800  1.000 50.35950 ?  73  ARG   B NH1   1 
ATOM   1959 N  NH2   . ARG   B 1 74  ? 45.17800 -35.72700 29.78900  1.000 42.90405 ?  73  ARG   B NH2   1 
ATOM   1960 N  N     . THR   B 1 75  ? 42.09700 -28.88300 29.93300  1.000 33.26173 ?  74  THR   B N     1 
ATOM   1961 C  CA    . THR   B 1 75  ? 41.65200 -27.85700 30.85800  1.000 31.54980 ?  74  THR   B CA    1 
ATOM   1962 C  C     . THR   B 1 75  ? 41.31200 -26.55200 30.14500  1.000 32.61547 ?  74  THR   B C     1 
ATOM   1963 O  O     . THR   B 1 75  ? 40.35400 -25.87100 30.52700  1.000 35.13594 ?  74  THR   B O     1 
ATOM   1964 C  CB    . THR   B 1 75  ? 42.74200 -27.62900 31.90900  1.000 31.12796 ?  74  THR   B CB    1 
ATOM   1965 O  OG1   . THR   B 1 75  ? 43.00600 -28.87000 32.56800  1.000 39.72395 ?  74  THR   B OG1   1 
ATOM   1966 C  CG2   . THR   B 1 75  ? 42.30200 -26.61600 32.92800  1.000 35.20375 ?  74  THR   B CG2   1 
ATOM   1967 N  N     . GLY   B 1 76  ? 42.08300 -26.18300 29.12000  1.000 29.14773 ?  75  GLY   B N     1 
ATOM   1968 C  CA    . GLY   B 1 76  ? 41.86800 -24.89400 28.46300  1.000 26.48786 ?  75  GLY   B CA    1 
ATOM   1969 C  C     . GLY   B 1 76  ? 40.51200 -24.79000 27.79000  1.000 31.43839 ?  75  GLY   B C     1 
ATOM   1970 O  O     . GLY   B 1 76  ? 39.98100 -25.76500 27.25800  1.000 31.81767 ?  75  GLY   B O     1 
ATOM   1971 N  N     . GLU   B 1 77  ? 39.96500 -23.56600 27.78500  1.000 28.98977 ?  76  GLU   B N     1 
ATOM   1972 C  CA    . GLU   B 1 77  ? 38.72400 -23.19300 27.07400  1.000 25.90157 ?  76  GLU   B CA    1 
ATOM   1973 C  C     . GLU   B 1 77  ? 38.94300 -22.54600 25.70900  1.000 33.33318 ?  76  GLU   B C     1 
ATOM   1974 O  O     . GLU   B 1 77  ? 38.11400 -22.73500 24.81300  1.000 36.87686 ?  76  GLU   B O     1 
ATOM   1975 C  CB    . GLU   B 1 77  ? 37.90300 -22.22900 27.93500  1.000 30.55788 ?  76  GLU   B CB    1 
ATOM   1976 C  CG    . GLU   B 1 77  ? 37.44400 -22.86000 29.25500  1.000 35.94182 ?  76  GLU   B CG    1 
ATOM   1977 C  CD    . GLU   B 1 77  ? 36.93800 -21.85100 30.29600  1.000 40.70612 ?  76  GLU   B CD    1 
ATOM   1978 O  OE1   . GLU   B 1 77  ? 37.04900 -20.62400 30.08200  1.000 39.46776 ?  76  GLU   B OE1   1 
ATOM   1979 O  OE2   . GLU   B 1 77  ? 36.43500 -22.30600 31.34800  1.000 51.79086 -1 76  GLU   B OE2   1 
ATOM   1980 N  N     . GLY   B 1 78  ? 39.98200 -21.72200 25.55000  1.000 30.77287 ?  77  GLY   B N     1 
ATOM   1981 C  CA    . GLY   B 1 78  ? 40.28200 -21.10500 24.27100  1.000 32.54204 ?  77  GLY   B CA    1 
ATOM   1982 C  C     . GLY   B 1 78  ? 41.78500 -21.07000 24.08000  1.000 26.14503 ?  77  GLY   B C     1 
ATOM   1983 O  O     . GLY   B 1 78  ? 42.54300 -21.05800 25.05300  1.000 27.80293 ?  77  GLY   B O     1 
ATOM   1984 N  N     . PHE   B 1 79  ? 42.21500 -21.03300 22.81700  1.000 24.30541 ?  78  PHE   B N     1 
ATOM   1985 C  CA    . PHE   B 1 79  ? 43.62900 -21.20800 22.48100  1.000 25.08513 ?  78  PHE   B CA    1 
ATOM   1986 C  C     . PHE   B 1 79  ? 44.08000 -20.11600 21.52100  1.000 28.25643 ?  78  PHE   B C     1 
ATOM   1987 O  O     . PHE   B 1 79  ? 43.45200 -19.89300 20.48100  1.000 27.92739 ?  78  PHE   B O     1 
ATOM   1988 C  CB    . PHE   B 1 79  ? 43.88500 -22.60500 21.88400  1.000 25.61596 ?  78  PHE   B CB    1 
ATOM   1989 C  CG    . PHE   B 1 79  ? 43.56200 -23.72800 22.83700  1.000 25.83342 ?  78  PHE   B CG    1 
ATOM   1990 C  CD1   . PHE   B 1 79  ? 42.26100 -24.16700 22.98800  1.000 29.51285 ?  78  PHE   B CD1   1 
ATOM   1991 C  CD2   . PHE   B 1 79  ? 44.55900 -24.27300 23.65300  1.000 27.34801 ?  78  PHE   B CD2   1 
ATOM   1992 C  CE1   . PHE   B 1 79  ? 41.93200 -25.17000 23.90300  1.000 27.89917 ?  78  PHE   B CE1   1 
ATOM   1993 C  CE2   . PHE   B 1 79  ? 44.23000 -25.27800 24.57000  1.000 23.13024 ?  78  PHE   B CE2   1 
ATOM   1994 C  CZ    . PHE   B 1 79  ? 42.92900 -25.71500 24.69000  1.000 26.02835 ?  78  PHE   B CZ    1 
ATOM   1995 N  N     . LEU   B 1 80  ? 45.12400 -19.39800 21.90400  1.000 22.07189 ?  79  LEU   B N     1 
ATOM   1996 C  CA    . LEU   B 1 80  ? 45.84800 -18.49900 21.00400  1.000 25.91213 ?  79  LEU   B CA    1 
ATOM   1997 C  C     . LEU   B 1 80  ? 46.92900 -19.32200 20.32200  1.000 28.94833 ?  79  LEU   B C     1 
ATOM   1998 O  O     . LEU   B 1 80  ? 47.87700 -19.76400 20.97500  1.000 27.03697 ?  79  LEU   B O     1 
ATOM   1999 C  CB    . LEU   B 1 80  ? 46.48600 -17.33400 21.75600  1.000 28.68241 ?  79  LEU   B CB    1 
ATOM   2000 C  CG    . LEU   B 1 80  ? 45.75000 -16.06800 22.13100  1.000 32.75058 ?  79  LEU   B CG    1 
ATOM   2001 C  CD1   . LEU   B 1 80  ? 46.81500 -14.99900 22.44100  1.000 35.26664 ?  79  LEU   B CD1   1 
ATOM   2002 C  CD2   . LEU   B 1 80  ? 44.82300 -15.64600 20.97700  1.000 29.66566 ?  79  LEU   B CD2   1 
ATOM   2003 N  N     . CYS   B 1 81  ? 46.79300 -19.52700 19.01500  1.000 26.18336 ?  80  CYS   B N     1 
ATOM   2004 C  CA    . CYS   B 1 81  ? 47.74400 -20.32200 18.25100  1.000 28.52471 ?  80  CYS   B CA    1 
ATOM   2005 C  C     . CYS   B 1 81  ? 48.64800 -19.33400 17.53800  1.000 33.37745 ?  80  CYS   B C     1 
ATOM   2006 O  O     . CYS   B 1 81  ? 48.24400 -18.69000 16.56600  1.000 29.79922 ?  80  CYS   B O     1 
ATOM   2007 C  CB    . CYS   B 1 81  ? 47.03000 -21.25200 17.27700  1.000 31.57828 ?  80  CYS   B CB    1 
ATOM   2008 S  SG    . CYS   B 1 81  ? 45.91900 -22.42300 18.12100  1.000 34.63659 ?  80  CYS   B SG    1 
ATOM   2009 N  N     . VAL   B 1 82  ? 49.85800 -19.20800 18.03500  1.000 24.63051 ?  81  VAL   B N     1 
ATOM   2010 C  CA    . VAL   B 1 82  ? 50.77900 -18.16300 17.61900  1.000 31.93437 ?  81  VAL   B CA    1 
ATOM   2011 C  C     . VAL   B 1 82  ? 51.82800 -18.75500 16.68600  1.000 31.88394 ?  81  VAL   B C     1 
ATOM   2012 O  O     . VAL   B 1 82  ? 52.45900 -19.77400 17.00600  1.000 27.93710 ?  81  VAL   B O     1 
ATOM   2013 C  CB    . VAL   B 1 82  ? 51.43800 -17.51100 18.84100  1.000 27.21930 ?  81  VAL   B CB    1 
ATOM   2014 C  CG1   . VAL   B 1 82  ? 52.22200 -16.29000 18.45000  1.000 30.64478 ?  81  VAL   B CG1   1 
ATOM   2015 C  CG2   . VAL   B 1 82  ? 50.36900 -17.18600 19.90000  1.000 23.87413 ?  81  VAL   B CG2   1 
ATOM   2016 N  N     . PHE   B 1 83  ? 52.02000 -18.12200 15.53000  1.000 28.19303 ?  82  PHE   B N     1 
ATOM   2017 C  CA    . PHE   B 1 83  ? 53.20600 -18.35100 14.71900  1.000 31.81328 ?  82  PHE   B CA    1 
ATOM   2018 C  C     . PHE   B 1 83  ? 53.89000 -17.00500 14.54200  1.000 27.83863 ?  82  PHE   B C     1 
ATOM   2019 O  O     . PHE   B 1 83  ? 53.33200 -15.95500 14.89500  1.000 31.27172 ?  82  PHE   B O     1 
ATOM   2020 C  CB    . PHE   B 1 83  ? 52.87200 -18.99100 13.36100  1.000 30.60136 ?  82  PHE   B CB    1 
ATOM   2021 C  CG    . PHE   B 1 83  ? 52.06800 -18.10300 12.44800  1.000 30.99556 ?  82  PHE   B CG    1 
ATOM   2022 C  CD1   . PHE   B 1 83  ? 50.69100 -18.03500 12.56200  1.000 30.85780 ?  82  PHE   B CD1   1 
ATOM   2023 C  CD2   . PHE   B 1 83  ? 52.69800 -17.36700 11.45800  1.000 38.05306 ?  82  PHE   B CD2   1 
ATOM   2024 C  CE1   . PHE   B 1 83  ? 49.94000 -17.22100 11.69700  1.000 36.03923 ?  82  PHE   B CE1   1 
ATOM   2025 C  CE2   . PHE   B 1 83  ? 51.97900 -16.56000 10.60800  1.000 36.66887 ?  82  PHE   B CE2   1 
ATOM   2026 C  CZ    . PHE   B 1 83  ? 50.60000 -16.48300 10.71400  1.000 33.46833 ?  82  PHE   B CZ    1 
ATOM   2027 N  N     . ALA   B 1 84  ? 55.10700 -17.02800 14.02300  1.000 29.74111 ?  83  ALA   B N     1 
ATOM   2028 C  CA    . ALA   B 1 84  ? 55.78400 -15.79300 13.66900  1.000 35.02031 ?  83  ALA   B CA    1 
ATOM   2029 C  C     . ALA   B 1 84  ? 55.77600 -15.64000 12.14900  1.000 37.40393 ?  83  ALA   B C     1 
ATOM   2030 O  O     . ALA   B 1 84  ? 55.94300 -16.61900 11.41300  1.000 32.84856 ?  83  ALA   B O     1 
ATOM   2031 C  CB    . ALA   B 1 84  ? 57.19900 -15.77000 14.23400  1.000 30.02928 ?  83  ALA   B CB    1 
ATOM   2032 N  N     . ILE   B 1 85  ? 55.55700 -14.40900 11.67600  1.000 37.27377 ?  84  ILE   B N     1 
ATOM   2033 C  CA    . ILE   B 1 85  ? 55.33900 -14.22800 10.23600  1.000 38.78980 ?  84  ILE   B CA    1 
ATOM   2034 C  C     . ILE   B 1 85  ? 56.61800 -14.29600 9.42000   1.000 45.86195 ?  84  ILE   B C     1 
ATOM   2035 O  O     . ILE   B 1 85  ? 56.54500 -14.31400 8.18300   1.000 41.35108 ?  84  ILE   B O     1 
ATOM   2036 C  CB    . ILE   B 1 85  ? 54.61000 -12.90400 9.92600   1.000 38.08679 ?  84  ILE   B CB    1 
ATOM   2037 C  CG1   . ILE   B 1 85  ? 55.21800 -11.73400 10.69900  1.000 40.94373 ?  84  ILE   B CG1   1 
ATOM   2038 C  CG2   . ILE   B 1 85  ? 53.13000 -13.02300 10.24100  1.000 39.97526 ?  84  ILE   B CG2   1 
ATOM   2039 C  CD1   . ILE   B 1 85  ? 56.33200 -11.01100 9.98700   1.000 40.21197 ?  84  ILE   B CD1   1 
ATOM   2040 N  N     . ASN   B 1 86  ? 57.77900 -14.34800 10.06800  1.000 40.37382 ?  85  ASN   B N     1 
ATOM   2041 C  CA    . ASN   B 1 86  ? 59.05700 -14.56100 9.40600   1.000 45.33577 ?  85  ASN   B CA    1 
ATOM   2042 C  C     . ASN   B 1 86  ? 59.58100 -15.98100 9.61000   1.000 44.54106 ?  85  ASN   B C     1 
ATOM   2043 O  O     . ASN   B 1 86  ? 60.77400 -16.22700 9.40300   1.000 48.59627 ?  85  ASN   B O     1 
ATOM   2044 C  CB    . ASN   B 1 86  ? 60.09300 -13.56800 9.93100   1.000 45.02873 ?  85  ASN   B CB    1 
ATOM   2045 C  CG    . ASN   B 1 86  ? 60.35700 -13.76600 11.40200  1.000 45.59198 ?  85  ASN   B CG    1 
ATOM   2046 O  OD1   . ASN   B 1 86  ? 59.51600 -14.31800 12.09800  1.000 43.07093 ?  85  ASN   B OD1   1 
ATOM   2047 N  ND2   . ASN   B 1 86  ? 61.52100 -13.34400 11.88100  1.000 47.82939 ?  85  ASN   B ND2   1 
ATOM   2048 N  N     . ASN   B 1 87  ? 58.71900 -16.90700 10.04300  1.000 44.27532 ?  86  ASN   B N     1 
ATOM   2049 C  CA    . ASN   B 1 87  ? 59.11200 -18.27300 10.38800  1.000 41.61293 ?  86  ASN   B CA    1 
ATOM   2050 C  C     . ASN   B 1 87  ? 58.11400 -19.23100 9.74500   1.000 43.14482 ?  86  ASN   B C     1 
ATOM   2051 O  O     . ASN   B 1 87  ? 57.07900 -19.55400 10.33300  1.000 38.93992 ?  86  ASN   B O     1 
ATOM   2052 C  CB    . ASN   B 1 87  ? 59.17000 -18.47100 11.89800  1.000 41.68639 ?  86  ASN   B CB    1 
ATOM   2053 C  CG    . ASN   B 1 87  ? 59.79000 -19.80400 12.28400  1.000 43.62865 ?  86  ASN   B CG    1 
ATOM   2054 O  OD1   . ASN   B 1 87  ? 59.83200 -20.73000 11.48400  1.000 47.21928 ?  86  ASN   B OD1   1 
ATOM   2055 N  ND2   . ASN   B 1 87  ? 60.27700 -19.90200 13.51200  1.000 44.70766 ?  86  ASN   B ND2   1 
ATOM   2056 N  N     . THR   B 1 88  ? 58.44300 -19.70800 8.54300   1.000 39.74941 ?  87  THR   B N     1 
ATOM   2057 C  CA    . THR   B 1 88  ? 57.53100 -20.59500 7.83100   1.000 44.36138 ?  87  THR   B CA    1 
ATOM   2058 C  C     . THR   B 1 88  ? 57.28400 -21.87900 8.61800   1.000 37.90659 ?  87  THR   B C     1 
ATOM   2059 O  O     . THR   B 1 88  ? 56.15900 -22.39300 8.64600   1.000 42.89850 ?  87  THR   B O     1 
ATOM   2060 C  CB    . THR   B 1 88  ? 58.09000 -20.88900 6.43100   1.000 44.39445 ?  87  THR   B CB    1 
ATOM   2061 O  OG1   . THR   B 1 88  ? 58.03300 -19.68600 5.65400   1.000 51.66613 ?  87  THR   B OG1   1 
ATOM   2062 C  CG2   . THR   B 1 88  ? 57.25900 -21.93000 5.73700   1.000 44.61525 ?  87  THR   B CG2   1 
ATOM   2063 N  N     . LYS   B 1 89  ? 58.31300 -22.39200 9.28700   1.000 40.17223 ?  88  LYS   B N     1 
ATOM   2064 C  CA    . LYS   B 1 89  ? 58.15500 -23.64400 10.01500  1.000 40.74158 ?  88  LYS   B CA    1 
ATOM   2065 C  C     . LYS   B 1 89  ? 57.13700 -23.48800 11.14100  1.000 40.36993 ?  88  LYS   B C     1 
ATOM   2066 O  O     . LYS   B 1 89  ? 56.28600 -24.36200 11.35300  1.000 34.53245 ?  88  LYS   B O     1 
ATOM   2067 C  CB    . LYS   B 1 89  ? 59.50700 -24.08500 10.56400  1.000 36.46846 ?  88  LYS   B CB    1 
ATOM   2068 C  CG    . LYS   B 1 89  ? 59.49700 -25.40400 11.33500  1.000 47.38302 ?  88  LYS   B CG    1 
ATOM   2069 C  CD    . LYS   B 1 89  ? 58.95100 -26.56100 10.50300  1.000 47.67980 ?  88  LYS   B CD    1 
ATOM   2070 C  CE    . LYS   B 1 89  ? 59.25500 -27.90300 11.18200  1.000 48.97679 ?  88  LYS   B CE    1 
ATOM   2071 N  NZ    . LYS   B 1 89  ? 59.32000 -27.77600 12.67800  1.000 51.13844 ?  88  LYS   B NZ    1 
ATOM   2072 N  N     . SER   B 1 90  ? 57.18000 -22.35400 11.83800  1.000 38.89925 ?  89  SER   B N     1 
ATOM   2073 C  CA    . SER   B 1 90  ? 56.23400 -22.13000 12.92400  1.000 34.17631 ?  89  SER   B CA    1 
ATOM   2074 C  C     . SER   B 1 90  ? 54.81100 -22.04600 12.38800  1.000 33.88661 ?  89  SER   B C     1 
ATOM   2075 O  O     . SER   B 1 90  ? 53.85900 -22.45600 13.05900  1.000 30.04666 ?  89  SER   B O     1 
ATOM   2076 C  CB    . SER   B 1 90  ? 56.63900 -20.87600 13.70700  1.000 35.25305 ?  89  SER   B CB    1 
ATOM   2077 O  OG    . SER   B 1 90  ? 56.15900 -19.68500 13.10800  1.000 33.58499 ?  89  SER   B OG    1 
ATOM   2078 N  N     . PHE   B 1 91  ? 54.64900 -21.59200 11.14200  1.000 34.40172 ?  90  PHE   B N     1 
ATOM   2079 C  CA    . PHE   B 1 91  ? 53.31800 -21.57800 10.56200  1.000 36.26038 ?  90  PHE   B CA    1 
ATOM   2080 C  C     . PHE   B 1 91  ? 52.86500 -22.99100 10.21600  1.000 34.98682 ?  90  PHE   B C     1 
ATOM   2081 O  O     . PHE   B 1 91  ? 51.69400 -23.33800 10.41500  1.000 37.81308 ?  90  PHE   B O     1 
ATOM   2082 C  CB    . PHE   B 1 91  ? 53.30500 -20.65900 9.33400   1.000 35.31976 ?  90  PHE   B CB    1 
ATOM   2083 C  CG    . PHE   B 1 91  ? 51.96800 -20.54700 8.67100   1.000 33.43174 ?  90  PHE   B CG    1 
ATOM   2084 C  CD1   . PHE   B 1 91  ? 50.93400 -19.85500 9.27300   1.000 35.75312 ?  90  PHE   B CD1   1 
ATOM   2085 C  CD2   . PHE   B 1 91  ? 51.75600 -21.11400 7.41800   1.000 38.22352 ?  90  PHE   B CD2   1 
ATOM   2086 C  CE1   . PHE   B 1 91  ? 49.69900 -19.74900 8.66000   1.000 38.87860 ?  90  PHE   B CE1   1 
ATOM   2087 C  CE2   . PHE   B 1 91  ? 50.52300 -21.01300 6.79800   1.000 40.20152 ?  90  PHE   B CE2   1 
ATOM   2088 C  CZ    . PHE   B 1 91  ? 49.49100 -20.32500 7.40700   1.000 39.05786 ?  90  PHE   B CZ    1 
ATOM   2089 N  N     . GLU   B 1 92  ? 53.77500 -23.82900 9.70700   1.000 41.30957 ?  91  GLU   B N     1 
ATOM   2090 C  CA    . GLU   B 1 92  ? 53.40200 -25.21200 9.41300   1.000 42.97188 ?  91  GLU   B CA    1 
ATOM   2091 C  C     . GLU   B 1 92  ? 53.10400 -25.98400 10.67800  1.000 39.02241 ?  91  GLU   B C     1 
ATOM   2092 O  O     . GLU   B 1 92  ? 52.32100 -26.93600 10.64100  1.000 40.09437 ?  91  GLU   B O     1 
ATOM   2093 C  CB    . GLU   B 1 92  ? 54.50400 -25.95800 8.65900   1.000 43.14958 ?  91  GLU   B CB    1 
ATOM   2094 C  CG    . GLU   B 1 92  ? 55.27700 -25.13900 7.67500   1.000 49.21193 ?  91  GLU   B CG    1 
ATOM   2095 C  CD    . GLU   B 1 92  ? 54.43000 -24.59900 6.54900   1.000 57.13139 ?  91  GLU   B CD    1 
ATOM   2096 O  OE1   . GLU   B 1 92  ? 53.24100 -25.00000 6.42600   1.000 63.18186 ?  91  GLU   B OE1   1 
ATOM   2097 O  OE2   . GLU   B 1 92  ? 54.96400 -23.76800 5.77700   1.000 60.48355 -1 91  GLU   B OE2   1 
ATOM   2098 N  N     . ASP   B 1 93  ? 53.74600 -25.61400 11.79200  1.000 39.32483 ?  92  ASP   B N     1 
ATOM   2099 C  CA    . ASP   B 1 93  ? 53.47700 -26.27000 13.06100  1.000 38.47127 ?  92  ASP   B CA    1 
ATOM   2100 C  C     . ASP   B 1 93  ? 52.07800 -25.97100 13.57500  1.000 40.05421 ?  92  ASP   B C     1 
ATOM   2101 O  O     . ASP   B 1 93  ? 51.55900 -26.75200 14.37100  1.000 39.29590 ?  92  ASP   B O     1 
ATOM   2102 C  CB    . ASP   B 1 93  ? 54.50500 -25.85300 14.12300  1.000 37.90472 ?  92  ASP   B CB    1 
ATOM   2103 C  CG    . ASP   B 1 93  ? 55.91800 -26.31000 13.79400  1.000 41.94295 ?  92  ASP   B CG    1 
ATOM   2104 O  OD1   . ASP   B 1 93  ? 56.09400 -27.25400 12.98000  1.000 46.49798 ?  92  ASP   B OD1   1 
ATOM   2105 O  OD2   . ASP   B 1 93  ? 56.86900 -25.72000 14.36100  1.000 48.95220 -1 92  ASP   B OD2   1 
ATOM   2106 N  N     . ILE   B 1 94  ? 51.45700 -24.87100 13.12900  1.000 40.77399 ?  93  ILE   B N     1 
ATOM   2107 C  CA    . ILE   B 1 94  ? 50.13500 -24.49400 13.63600  1.000 38.27241 ?  93  ILE   B CA    1 
ATOM   2108 C  C     . ILE   B 1 94  ? 49.14300 -25.62800 13.44600  1.000 37.87186 ?  93  ILE   B C     1 
ATOM   2109 O  O     . ILE   B 1 94  ? 48.27500 -25.85800 14.29600  1.000 38.27837 ?  93  ILE   B O     1 
ATOM   2110 C  CB    . ILE   B 1 94  ? 49.63200 -23.20500 12.95400  1.000 36.93483 ?  93  ILE   B CB    1 
ATOM   2111 C  CG1   . ILE   B 1 94  ? 50.41000 -21.99600 13.45200  1.000 39.09775 ?  93  ILE   B CG1   1 
ATOM   2112 C  CG2   . ILE   B 1 94  ? 48.12000 -23.03600 13.14700  1.000 40.77283 ?  93  ILE   B CG2   1 
ATOM   2113 C  CD1   . ILE   B 1 94  ? 50.31200 -21.79500 14.94900  1.000 34.17802 ?  93  ILE   B CD1   1 
ATOM   2114 N  N     . HIS   B 1 95  ? 49.23900 -26.35600 12.32900  1.000 37.64045 ?  94  HIS   B N     1 
ATOM   2115 C  CA    . HIS   B 1 95  ? 48.20100 -27.35300 12.10300  1.000 43.12083 ?  94  HIS   B CA    1 
ATOM   2116 C  C     . HIS   B 1 95  ? 48.37800 -28.55000 13.03500  1.000 40.37404 ?  94  HIS   B C     1 
ATOM   2117 O  O     . HIS   B 1 95  ? 47.38100 -29.16300 13.43400  1.000 44.17187 ?  94  HIS   B O     1 
ATOM   2118 C  CB    . HIS   B 1 95  ? 48.14400 -27.75100 10.61300  1.000 46.01207 ?  94  HIS   B CB    1 
ATOM   2119 C  CG    . HIS   B 1 95  ? 49.14400 -28.78100 10.20100  1.000 49.60380 ?  94  HIS   B CG    1 
ATOM   2120 N  ND1   . HIS   B 1 95  ? 48.99800 -30.12100 10.49100  1.000 55.72319 ?  94  HIS   B ND1   1 
ATOM   2121 C  CD2   . HIS   B 1 95  ? 50.28300 -28.67600 9.47500   1.000 52.58685 ?  94  HIS   B CD2   1 
ATOM   2122 C  CE1   . HIS   B 1 95  ? 50.02000 -30.79400 9.98900   1.000 56.16210 ?  94  HIS   B CE1   1 
ATOM   2123 N  NE2   . HIS   B 1 95  ? 50.81500 -29.94000 9.36900   1.000 58.44944 ?  94  HIS   B NE2   1 
ATOM   2124 N  N     . HIS   B 1 96  ? 49.61800 -28.85500 13.44700  1.000 37.93686 ?  95  HIS   B N     1 
ATOM   2125 C  CA    . HIS   B 1 96  ? 49.83700 -29.85200 14.49700  1.000 38.94974 ?  95  HIS   B CA    1 
ATOM   2126 C  C     . HIS   B 1 96  ? 49.07100 -29.48200 15.76900  1.000 38.23976 ?  95  HIS   B C     1 
ATOM   2127 O  O     . HIS   B 1 96  ? 48.39200 -30.32500 16.37500  1.000 37.45596 ?  95  HIS   B O     1 
ATOM   2128 C  CB    . HIS   B 1 96  ? 51.33900 -29.98800 14.82900  1.000 41.22500 ?  95  HIS   B CB    1 
ATOM   2129 C  CG    . HIS   B 1 96  ? 52.21200 -30.41800 13.68400  1.000 48.36888 ?  95  HIS   B CG    1 
ATOM   2130 N  ND1   . HIS   B 1 96  ? 51.78800 -30.44200 12.37000  1.000 52.28683 ?  95  HIS   B ND1   1 
ATOM   2131 C  CD2   . HIS   B 1 96  ? 53.49900 -30.84700 13.66500  1.000 45.37918 ?  95  HIS   B CD2   1 
ATOM   2132 C  CE1   . HIS   B 1 96  ? 52.77000 -30.87100 11.59400  1.000 47.12689 ?  95  HIS   B CE1   1 
ATOM   2133 N  NE2   . HIS   B 1 96  ? 53.81800 -31.12400 12.35500  1.000 52.58430 ?  95  HIS   B NE2   1 
ATOM   2134 N  N     . TYR   B 1 97  ? 49.18600 -28.22100 16.19800  1.000 35.67954 ?  96  TYR   B N     1 
ATOM   2135 C  CA    . TYR   B 1 97  ? 48.53100 -27.77300 17.42600  1.000 34.33163 ?  96  TYR   B CA    1 
ATOM   2136 C  C     . TYR   B 1 97  ? 47.01400 -27.84000 17.30400  1.000 34.65208 ?  96  TYR   B C     1 
ATOM   2137 O  O     . TYR   B 1 97  ? 46.32700 -28.32000 18.21100  1.000 37.21155 ?  96  TYR   B O     1 
ATOM   2138 C  CB    . TYR   B 1 97  ? 48.97900 -26.34400 17.76800  1.000 38.74789 ?  96  TYR   B CB    1 
ATOM   2139 C  CG    . TYR   B 1 97  ? 50.29200 -26.31000 18.50600  1.000 36.65890 ?  96  TYR   B CG    1 
ATOM   2140 C  CD1   . TYR   B 1 97  ? 50.35000 -26.62500 19.85600  1.000 35.51978 ?  96  TYR   B CD1   1 
ATOM   2141 C  CD2   . TYR   B 1 97  ? 51.47200 -25.98900 17.86200  1.000 30.80441 ?  96  TYR   B CD2   1 
ATOM   2142 C  CE1   . TYR   B 1 97  ? 51.55100 -26.62800 20.52700  1.000 36.32793 ?  96  TYR   B CE1   1 
ATOM   2143 C  CE2   . TYR   B 1 97  ? 52.67900 -25.99100 18.53500  1.000 32.06615 ?  96  TYR   B CE2   1 
ATOM   2144 C  CZ    . TYR   B 1 97  ? 52.71300 -26.31100 19.87200  1.000 36.92913 ?  96  TYR   B CZ    1 
ATOM   2145 O  OH    . TYR   B 1 97  ? 53.90500 -26.29900 20.58500  1.000 37.66177 ?  96  TYR   B OH    1 
ATOM   2146 N  N     . ARG   B 1 98  ? 46.46900 -27.33400 16.19900  1.000 32.72936 ?  97  ARG   B N     1 
ATOM   2147 C  CA    . ARG   B 1 98  ? 45.02600 -27.41900 15.99500  1.000 39.93168 ?  97  ARG   B CA    1 
ATOM   2148 C  C     . ARG   B 1 98  ? 44.54500 -28.86600 16.02400  1.000 39.62310 ?  97  ARG   B C     1 
ATOM   2149 O  O     . ARG   B 1 98  ? 43.52300 -29.17600 16.64400  1.000 41.04055 ?  97  ARG   B O     1 
ATOM   2150 C  CB    . ARG   B 1 98  ? 44.62300 -26.74900 14.67700  1.000 40.41021 ?  97  ARG   B CB    1 
ATOM   2151 C  CG    . ARG   B 1 98  ? 43.10800 -26.59400 14.48800  1.000 45.46819 ?  97  ARG   B CG    1 
ATOM   2152 C  CD    . ARG   B 1 98  ? 42.51300 -27.68800 13.60000  1.000 45.48287 ?  97  ARG   B CD    1 
ATOM   2153 N  NE    . ARG   B 1 98  ? 41.07900 -27.49800 13.42100  1.000 50.38780 ?  97  ARG   B NE    1 
ATOM   2154 C  CZ    . ARG   B 1 98  ? 40.31900 -28.21400 12.60000  1.000 51.84209 ?  97  ARG   B CZ    1 
ATOM   2155 N  NH1   . ARG   B 1 98  ? 40.82400 -29.19100 11.86000  1.000 49.20919 ?  97  ARG   B NH1   1 
ATOM   2156 N  NH2   . ARG   B 1 98  ? 39.01800 -27.94200 12.51900  1.000 52.66720 ?  97  ARG   B NH2   1 
ATOM   2157 N  N     . GLU   B 1 99  ? 45.24800 -29.77000 15.33000  1.000 39.04863 ?  98  GLU   B N     1 
ATOM   2158 C  CA    . GLU   B 1 99  ? 44.75900 -31.14300 15.28500  1.000 41.74995 ?  98  GLU   B CA    1 
ATOM   2159 C  C     . GLU   B 1 99  ? 44.91900 -31.83300 16.63200  1.000 39.78271 ?  98  GLU   B C     1 
ATOM   2160 O  O     . GLU   B 1 99  ? 44.15400 -32.74300 16.95700  1.000 47.15270 ?  98  GLU   B O     1 
ATOM   2161 C  CB    . GLU   B 1 99  ? 45.46500 -31.93400 14.17800  1.000 41.41402 ?  98  GLU   B CB    1 
ATOM   2162 C  CG    . GLU   B 1 99  ? 45.11500 -31.47000 12.73800  1.000 43.65979 ?  98  GLU   B CG    1 
ATOM   2163 C  CD    . GLU   B 1 99  ? 43.61000 -31.53500 12.40100  1.000 52.31802 ?  98  GLU   B CD    1 
ATOM   2164 O  OE1   . GLU   B 1 99  ? 42.92700 -32.50800 12.81000  1.000 57.40104 ?  98  GLU   B OE1   1 
ATOM   2165 O  OE2   . GLU   B 1 99  ? 43.10200 -30.60900 11.71600  1.000 55.51274 -1 98  GLU   B OE2   1 
ATOM   2166 N  N     . GLN   B 1 100 ? 45.89600 -31.41900 17.42700  1.000 33.82807 ?  99  GLN   B N     1 
ATOM   2167 C  CA    . GLN   B 1 100 ? 46.04200 -32.00000 18.75500  1.000 38.64940 ?  99  GLN   B CA    1 
ATOM   2168 C  C     . GLN   B 1 100 ? 44.92500 -31.51200 19.67000  1.000 37.76998 ?  99  GLN   B C     1 
ATOM   2169 O  O     . GLN   B 1 100 ? 44.30100 -32.31000 20.37500  1.000 35.36746 ?  99  GLN   B O     1 
ATOM   2170 C  CB    . GLN   B 1 100 ? 47.41900 -31.64500 19.31200  1.000 32.71735 ?  99  GLN   B CB    1 
ATOM   2171 C  CG    . GLN   B 1 100 ? 47.91800 -32.48600 20.46100  1.000 38.46560 ?  99  GLN   B CG    1 
ATOM   2172 C  CD    . GLN   B 1 100 ? 49.26900 -31.99900 20.97900  1.000 45.26673 ?  99  GLN   B CD    1 
ATOM   2173 O  OE1   . GLN   B 1 100 ? 49.89000 -31.09400 20.40700  1.000 45.83028 ?  99  GLN   B OE1   1 
ATOM   2174 N  NE2   . GLN   B 1 100 ? 49.71600 -32.58300 22.08000  1.000 42.72520 ?  99  GLN   B NE2   1 
ATOM   2175 N  N     . ILE   B 1 101 ? 44.65100 -30.20000 19.64300  1.000 40.91282 ?  100 ILE   B N     1 
ATOM   2176 C  CA    . ILE   B 1 101 ? 43.55400 -29.62000 20.42100  1.000 35.88912 ?  100 ILE   B CA    1 
ATOM   2177 C  C     . ILE   B 1 101 ? 42.22200 -30.23300 20.00600  1.000 38.77000 ?  100 ILE   B C     1 
ATOM   2178 O  O     . ILE   B 1 101 ? 41.45800 -30.72100 20.84400  1.000 38.68238 ?  100 ILE   B O     1 
ATOM   2179 C  CB    . ILE   B 1 101 ? 43.54500 -28.08700 20.26700  1.000 34.24464 ?  100 ILE   B CB    1 
ATOM   2180 C  CG1   . ILE   B 1 101 ? 44.82100 -27.49400 20.86300  1.000 35.70394 ?  100 ILE   B CG1   1 
ATOM   2181 C  CG2   . ILE   B 1 101 ? 42.27600 -27.46600 20.88800  1.000 38.51224 ?  100 ILE   B CG2   1 
ATOM   2182 C  CD1   . ILE   B 1 101 ? 45.11100 -26.09400 20.37400  1.000 34.34815 ?  100 ILE   B CD1   1 
ATOM   2183 N  N     . LYS   B 1 102 ? 41.93800 -30.23900 18.70100  1.000 43.03793 ?  101 LYS   B N     1 
ATOM   2184 C  CA    . LYS   B 1 102 ? 40.71700 -30.87300 18.21100  1.000 41.14305 ?  101 LYS   B CA    1 
ATOM   2185 C  C     . LYS   B 1 102 ? 40.60200 -32.30500 18.71600  1.000 43.49837 ?  101 LYS   B C     1 
ATOM   2186 O  O     . LYS   B 1 102 ? 39.52100 -32.73900 19.12800  1.000 47.03620 ?  101 LYS   B O     1 
ATOM   2187 C  CB    . LYS   B 1 102 ? 40.67200 -30.84000 16.67600  1.000 45.17212 ?  101 LYS   B CB    1 
ATOM   2188 C  CG    . LYS   B 1 102 ? 39.83400 -31.95200 16.05000  1.000 45.06053 ?  101 LYS   B CG    1 
ATOM   2189 C  CD    . LYS   B 1 102 ? 39.52300 -31.69200 14.57600  1.000 50.34972 ?  101 LYS   B CD    1 
ATOM   2190 C  CE    . LYS   B 1 102 ? 38.84600 -32.91300 13.92700  1.000 44.83346 ?  101 LYS   B CE    1 
ATOM   2191 N  NZ    . LYS   B 1 102 ? 38.38300 -32.60900 12.54900  1.000 54.34372 ?  101 LYS   B NZ    1 
ATOM   2192 N  N     . ARG   B 1 103 ? 41.71200 -33.04500 18.70900  1.000 40.36193 ?  102 ARG   B N     1 
ATOM   2193 C  CA    . ARG   B 1 103 ? 41.68300 -34.44600 19.12500  1.000 40.91421 ?  102 ARG   B CA    1 
ATOM   2194 C  C     . ARG   B 1 103 ? 41.43900 -34.57700 20.62000  1.000 46.85996 ?  102 ARG   B C     1 
ATOM   2195 O  O     . ARG   B 1 103 ? 40.59000 -35.36400 21.05700  1.000 50.23784 ?  102 ARG   B O     1 
ATOM   2196 C  CB    . ARG   B 1 103 ? 42.98900 -35.14000 18.75500  1.000 45.22497 ?  102 ARG   B CB    1 
ATOM   2197 C  CG    . ARG   B 1 103 ? 43.12300 -36.50000 19.40300  1.000 48.09818 ?  102 ARG   B CG    1 
ATOM   2198 C  CD    . ARG   B 1 103 ? 44.51100 -37.09200 19.26000  1.000 48.59752 ?  102 ARG   B CD    1 
ATOM   2199 N  NE    . ARG   B 1 103 ? 45.39600 -36.70900 20.35600  1.000 49.13037 ?  102 ARG   B NE    1 
ATOM   2200 C  CZ    . ARG   B 1 103 ? 46.59400 -36.16100 20.19600  1.000 49.95691 ?  102 ARG   B CZ    1 
ATOM   2201 N  NH1   . ARG   B 1 103 ? 47.09900 -35.94100 18.99100  1.000 54.10277 ?  102 ARG   B NH1   1 
ATOM   2202 N  NH2   . ARG   B 1 103 ? 47.30900 -35.83300 21.27200  1.000 47.21319 ?  102 ARG   B NH2   1 
ATOM   2203 N  N     . VAL   B 1 104 ? 42.18400 -33.81900 21.42300  1.000 45.64725 ?  103 VAL   B N     1 
ATOM   2204 C  CA    . VAL   B 1 104 ? 42.10100 -33.97700 22.87200  1.000 45.40262 ?  103 VAL   B CA    1 
ATOM   2205 C  C     . VAL   B 1 104 ? 40.73200 -33.55100 23.38300  1.000 42.72562 ?  103 VAL   B C     1 
ATOM   2206 O  O     . VAL   B 1 104 ? 40.16600 -34.18400 24.28000  1.000 46.46836 ?  103 VAL   B O     1 
ATOM   2207 C  CB    . VAL   B 1 104 ? 43.22900 -33.19100 23.56000  1.000 44.11619 ?  103 VAL   B CB    1 
ATOM   2208 C  CG1   . VAL   B 1 104 ? 42.88500 -32.95500 25.00400  1.000 41.52045 ?  103 VAL   B CG1   1 
ATOM   2209 C  CG2   . VAL   B 1 104 ? 44.54600 -33.94300 23.45700  1.000 46.63062 ?  103 VAL   B CG2   1 
ATOM   2210 N  N     . LYS   B 1 105 ? 40.17500 -32.48100 22.82500  1.000 40.10097 ?  104 LYS   B N     1 
ATOM   2211 C  CA    . LYS   B 1 105 ? 38.90900 -31.95200 23.30000  1.000 43.73228 ?  104 LYS   B CA    1 
ATOM   2212 C  C     . LYS   B 1 105 ? 37.72500 -32.49200 22.51300  1.000 43.70845 ?  104 LYS   B C     1 
ATOM   2213 O  O     . LYS   B 1 105 ? 36.58900 -32.08100 22.77300  1.000 44.63987 ?  104 LYS   B O     1 
ATOM   2214 C  CB    . LYS   B 1 105 ? 38.93000 -30.41500 23.25100  1.000 36.34271 ?  104 LYS   B CB    1 
ATOM   2215 C  CG    . LYS   B 1 105 ? 40.07300 -29.80600 24.06500  1.000 38.43396 ?  104 LYS   B CG    1 
ATOM   2216 C  CD    . LYS   B 1 105 ? 39.92600 -28.30600 24.18300  1.000 39.33555 ?  104 LYS   B CD    1 
ATOM   2217 C  CE    . LYS   B 1 105 ? 38.78000 -27.94700 25.12900  1.000 33.63455 ?  104 LYS   B CE    1 
ATOM   2218 N  NZ    . LYS   B 1 105 ? 39.09800 -28.27400 26.55200  1.000 31.77329 ?  104 LYS   B NZ    1 
ATOM   2219 N  N     . ASP   B 1 106 ? 37.97600 -33.38200 21.54900  1.000 47.82568 ?  105 ASP   B N     1 
ATOM   2220 C  CA    . ASP   B 1 106 ? 36.92300 -34.03700 20.78000  1.000 43.10953 ?  105 ASP   B CA    1 
ATOM   2221 C  C     . ASP   B 1 106 ? 35.92900 -33.01400 20.23300  1.000 46.06024 ?  105 ASP   B C     1 
ATOM   2222 O  O     . ASP   B 1 106 ? 34.71900 -33.08700 20.46600  1.000 49.66869 ?  105 ASP   B O     1 
ATOM   2223 C  CB    . ASP   B 1 106 ? 36.22600 -35.09300 21.63900  1.000 48.91455 ?  105 ASP   B CB    1 
ATOM   2224 C  CG    . ASP   B 1 106 ? 35.29900 -35.98700 20.84000  1.000 57.09085 ?  105 ASP   B CG    1 
ATOM   2225 O  OD1   . ASP   B 1 106 ? 35.32500 -35.94100 19.58400  1.000 53.30761 ?  105 ASP   B OD1   1 
ATOM   2226 O  OD2   . ASP   B 1 106 ? 34.53100 -36.73500 21.48200  1.000 64.61877 -1 105 ASP   B OD2   1 
ATOM   2227 N  N     . SER   B 1 107 ? 36.44600 -32.02200 19.51900  1.000 44.92104 ?  106 SER   B N     1 
ATOM   2228 C  CA    . SER   B 1 107 ? 35.55400 -31.00100 18.99000  1.000 46.87262 ?  106 SER   B CA    1 
ATOM   2229 C  C     . SER   B 1 107 ? 36.18700 -30.34400 17.77800  1.000 47.87153 ?  106 SER   B C     1 
ATOM   2230 O  O     . SER   B 1 107 ? 37.40400 -30.12500 17.73800  1.000 45.23961 ?  106 SER   B O     1 
ATOM   2231 C  CB    . SER   B 1 107 ? 35.21400 -29.94000 20.04700  1.000 45.53183 ?  106 SER   B CB    1 
ATOM   2232 O  OG    . SER   B 1 107 ? 34.35900 -28.93800 19.50600  1.000 44.57142 ?  106 SER   B OG    1 
ATOM   2233 N  N     . GLU   B 1 108 ? 35.34800 -30.02900 16.79100  1.000 47.15321 ?  107 GLU   B N     1 
ATOM   2234 C  CA    . GLU   B 1 108 ? 35.77600 -29.24100 15.64800  1.000 48.00018 ?  107 GLU   B CA    1 
ATOM   2235 C  C     . GLU   B 1 108 ? 35.45900 -27.75900 15.81000  1.000 48.82808 ?  107 GLU   B C     1 
ATOM   2236 O  O     . GLU   B 1 108 ? 35.65000 -26.99000 14.86000  1.000 54.43426 ?  107 GLU   B O     1 
ATOM   2237 C  CB    . GLU   B 1 108 ? 35.14700 -29.80100 14.36900  1.000 47.41680 ?  107 GLU   B CB    1 
ATOM   2238 C  CG    . GLU   B 1 108 ? 35.76000 -31.14800 13.97700  1.000 47.03439 ?  107 GLU   B CG    1 
ATOM   2239 C  CD    . GLU   B 1 108 ? 34.80900 -32.03800 13.18600  1.000 48.10204 ?  107 GLU   B CD    1 
ATOM   2240 O  OE1   . GLU   B 1 108 ? 33.80000 -31.51600 12.65100  1.000 54.19780 ?  107 GLU   B OE1   1 
ATOM   2241 O  OE2   . GLU   B 1 108 ? 35.07000 -33.26100 13.11400  1.000 47.46000 -1 107 GLU   B OE2   1 
ATOM   2242 N  N     . ASP   B 1 109 ? 35.01400 -27.33700 17.00500  1.000 40.62850 ?  108 ASP   B N     1 
ATOM   2243 C  CA    . ASP   B 1 109 ? 34.53700 -25.98000 17.25300  1.000 44.37854 ?  108 ASP   B CA    1 
ATOM   2244 C  C     . ASP   B 1 109 ? 35.23200 -25.33600 18.44900  1.000 42.65552 ?  108 ASP   B C     1 
ATOM   2245 O  O     . ASP   B 1 109 ? 34.66900 -24.43700 19.08300  1.000 43.87368 ?  108 ASP   B O     1 
ATOM   2246 C  CB    . ASP   B 1 109 ? 33.02300 -25.96600 17.47700  1.000 43.57572 ?  108 ASP   B CB    1 
ATOM   2247 C  CG    . ASP   B 1 109 ? 32.24600 -26.39000 16.24600  1.000 57.21387 ?  108 ASP   B CG    1 
ATOM   2248 O  OD1   . ASP   B 1 109 ? 32.56100 -25.88200 15.14100  1.000 62.85215 -1 108 ASP   B OD1   1 
ATOM   2249 O  OD2   . ASP   B 1 109 ? 31.33000 -27.24000 16.38200  1.000 59.71905 ?  108 ASP   B OD2   1 
ATOM   2250 N  N     . VAL   B 1 110 ? 36.44100 -25.77200 18.76600  1.000 45.49987 ?  109 VAL   B N     1 
ATOM   2251 C  CA    . VAL   B 1 110 ? 37.13700 -25.25100 19.95500  1.000 37.51275 ?  109 VAL   B CA    1 
ATOM   2252 C  C     . VAL   B 1 110 ? 37.47500 -23.77800 19.73200  1.000 39.76552 ?  109 VAL   B C     1 
ATOM   2253 O  O     . VAL   B 1 110 ? 38.05500 -23.42900 18.68700  1.000 38.29337 ?  109 VAL   B O     1 
ATOM   2254 C  CB    . VAL   B 1 110 ? 38.39300 -26.08200 20.23100  1.000 41.36403 ?  109 VAL   B CB    1 
ATOM   2255 C  CG1   . VAL   B 1 110 ? 39.11400 -25.61500 21.52100  1.000 36.55463 ?  109 VAL   B CG1   1 
ATOM   2256 C  CG2   . VAL   B 1 110 ? 38.03000 -27.56600 20.31500  1.000 44.00323 ?  109 VAL   B CG2   1 
ATOM   2257 N  N     . PRO   B 1 111 ? 37.13600 -22.87100 20.65500  1.000 34.18151 ?  110 PRO   B N     1 
ATOM   2258 C  CA    . PRO   B 1 111 ? 37.51400 -21.46400 20.45500  1.000 34.14958 ?  110 PRO   B CA    1 
ATOM   2259 C  C     . PRO   B 1 111 ? 39.01400 -21.32400 20.25700  1.000 32.23020 ?  110 PRO   B C     1 
ATOM   2260 O  O     . PRO   B 1 111 ? 39.81800 -21.77800 21.07900  1.000 33.55296 ?  110 PRO   B O     1 
ATOM   2261 C  CB    . PRO   B 1 111 ? 37.03300 -20.78200 21.73500  1.000 32.37860 ?  110 PRO   B CB    1 
ATOM   2262 C  CG    . PRO   B 1 111 ? 35.89300 -21.65400 22.20400  1.000 37.99879 ?  110 PRO   B CG    1 
ATOM   2263 C  CD    . PRO   B 1 111 ? 36.29000 -23.05900 21.84100  1.000 32.92978 ?  110 PRO   B CD    1 
ATOM   2264 N  N     . MET   B 1 112 ? 39.38900 -20.73800 19.12300  1.000 30.99829 ?  111 MET   B N     1 
ATOM   2265 C  CA    . MET   B 1 112 ? 40.77700 -20.46200 18.80300  1.000 27.68081 ?  111 MET   B CA    1 
ATOM   2266 C  C     . MET   B 1 112 ? 40.87300 -19.15700 18.03800  1.000 35.38546 ?  111 MET   B C     1 
ATOM   2267 O  O     . MET   B 1 112 ? 39.92200 -18.73300 17.36500  1.000 35.68045 ?  111 MET   B O     1 
ATOM   2268 C  CB    . MET   B 1 112 ? 41.43200 -21.56500 17.97000  1.000 32.98772 ?  111 MET   B CB    1 
ATOM   2269 C  CG    . MET   B 1 112 ? 41.36400 -22.94300 18.59500  1.000 36.05027 ?  111 MET   B CG    1 
ATOM   2270 S  SD    . MET   B 1 112 ? 42.17400 -24.14800 17.52100  1.000 50.02682 ?  111 MET   B SD    1 
ATOM   2271 C  CE    . MET   B 1 112 ? 43.05300 -23.07300 16.41900  1.000 41.51904 ?  111 MET   B CE    1 
ATOM   2272 N  N     . VAL   B 1 113 ? 42.03800 -18.53500 18.14400  1.000 28.88964 ?  112 VAL   B N     1 
ATOM   2273 C  CA    . VAL   B 1 113 ? 42.43300 -17.42000 17.30100  1.000 29.09722 ?  112 VAL   B CA    1 
ATOM   2274 C  C     . VAL   B 1 113 ? 43.81000 -17.73500 16.73600  1.000 34.53947 ?  112 VAL   B C     1 
ATOM   2275 O  O     . VAL   B 1 113 ? 44.69800 -18.18100 17.47000  1.000 30.46622 ?  112 VAL   B O     1 
ATOM   2276 C  CB    . VAL   B 1 113 ? 42.45500 -16.09200 18.06900  1.000 26.53938 ?  112 VAL   B CB    1 
ATOM   2277 C  CG1   . VAL   B 1 113 ? 43.02400 -14.98100 17.19900  1.000 31.53508 ?  112 VAL   B CG1   1 
ATOM   2278 C  CG2   . VAL   B 1 113 ? 41.08200 -15.74500 18.52600  1.000 31.73291 ?  112 VAL   B CG2   1 
ATOM   2279 N  N     . LEU   B 1 114 ? 43.98100 -17.53800 15.42400  1.000 31.13969 ?  113 LEU   B N     1 
ATOM   2280 C  CA    . LEU   B 1 114 ? 45.29700 -17.65500 14.81700  1.000 28.89375 ?  113 LEU   B CA    1 
ATOM   2281 C  C     . LEU   B 1 114 ? 46.00600 -16.31200 14.92900  1.000 33.48098 ?  113 LEU   B C     1 
ATOM   2282 O  O     . LEU   B 1 114 ? 45.46800 -15.28000 14.52800  1.000 32.90098 ?  113 LEU   B O     1 
ATOM   2283 C  CB    . LEU   B 1 114 ? 45.17200 -18.07700 13.34100  1.000 27.99913 ?  113 LEU   B CB    1 
ATOM   2284 C  CG    . LEU   B 1 114 ? 46.43200 -18.37800 12.55000  1.000 30.71705 ?  113 LEU   B CG    1 
ATOM   2285 C  CD1   . LEU   B 1 114 ? 47.05900 -19.67000 12.99900  1.000 28.54803 ?  113 LEU   B CD1   1 
ATOM   2286 C  CD2   . LEU   B 1 114 ? 46.07100 -18.49200 11.05600  1.000 32.17059 ?  113 LEU   B CD2   1 
ATOM   2287 N  N     . VAL   B 1 115 ? 47.21300 -16.31800 15.46000  1.000 31.17029 ?  114 VAL   B N     1 
ATOM   2288 C  CA    . VAL   B 1 115 ? 47.94000 -15.09700 15.75000  1.000 33.88210 ?  114 VAL   B CA    1 
ATOM   2289 C  C     . VAL   B 1 115 ? 49.24800 -15.11100 14.98800  1.000 35.54065 ?  114 VAL   B C     1 
ATOM   2290 O  O     . VAL   B 1 115 ? 50.14400 -15.92200 15.27600  1.000 30.46217 ?  114 VAL   B O     1 
ATOM   2291 C  CB    . VAL   B 1 115 ? 48.20900 -14.92500 17.25500  1.000 35.02279 ?  114 VAL   B CB    1 
ATOM   2292 C  CG1   . VAL   B 1 115 ? 49.09000 -13.71200 17.46900  1.000 33.49497 ?  114 VAL   B CG1   1 
ATOM   2293 C  CG2   . VAL   B 1 115 ? 46.92300 -14.82400 18.05000  1.000 32.06678 ?  114 VAL   B CG2   1 
ATOM   2294 N  N     . GLY   B 1 116 ? 49.38400 -14.18000 14.04500  1.000 31.21672 ?  115 GLY   B N     1 
ATOM   2295 C  CA    . GLY   B 1 116 ? 50.65100 -14.00600 13.37800  1.000 38.15772 ?  115 GLY   B CA    1 
ATOM   2296 C  C     . GLY   B 1 116 ? 51.42100 -12.88800 14.03100  1.000 36.53337 ?  115 GLY   B C     1 
ATOM   2297 O  O     . GLY   B 1 116 ? 51.04500 -11.71500 13.91200  1.000 40.69091 ?  115 GLY   B O     1 
ATOM   2298 N  N     . ASN   B 1 117 ? 52.49600 -13.23600 14.72600  1.000 30.22984 ?  116 ASN   B N     1 
ATOM   2299 C  CA    . ASN   B 1 117 ? 53.24500 -12.28400 15.52500  1.000 33.25241 ?  116 ASN   B CA    1 
ATOM   2300 C  C     . ASN   B 1 117 ? 54.50100 -11.84100 14.79300  1.000 38.60233 ?  116 ASN   B C     1 
ATOM   2301 O  O     . ASN   B 1 117 ? 54.89300 -12.41900 13.77300  1.000 33.59251 ?  116 ASN   B O     1 
ATOM   2302 C  CB    . ASN   B 1 117 ? 53.60000 -12.89400 16.89200  1.000 33.29517 ?  116 ASN   B CB    1 
ATOM   2303 C  CG    . ASN   B 1 117 ? 54.17000 -11.87100 17.84900  1.000 33.62949 ?  116 ASN   B CG    1 
ATOM   2304 O  OD1   . ASN   B 1 117 ? 53.65700 -10.75300 17.95200  1.000 35.22844 ?  116 ASN   B OD1   1 
ATOM   2305 N  ND2   . ASN   B 1 117 ? 55.23700 -12.22900 18.54100  1.000 26.75947 ?  116 ASN   B ND2   1 
ATOM   2306 N  N     . LYS   B 1 118 ? 55.14800 -10.81800 15.36200  1.000 34.22820 ?  117 LYS   B N     1 
ATOM   2307 C  CA    . LYS   B 1 118 ? 56.33400 -10.15500 14.80000  1.000 37.48507 ?  117 LYS   B CA    1 
ATOM   2308 C  C     . LYS   B 1 118 ? 56.01600 -9.39400  13.50900  1.000 32.76396 ?  117 LYS   B C     1 
ATOM   2309 O  O     . LYS   B 1 118 ? 56.84600 -9.32600  12.59200  1.000 34.54658 ?  117 LYS   B O     1 
ATOM   2310 C  CB    . LYS   B 1 118 ? 57.48800 -11.14100 14.56700  1.000 36.13248 ?  117 LYS   B CB    1 
ATOM   2311 C  CG    . LYS   B 1 118 ? 57.66300 -12.11800 15.70000  1.000 35.89997 ?  117 LYS   B CG    1 
ATOM   2312 C  CD    . LYS   B 1 118 ? 59.07600 -12.65000 15.84000  1.000 38.50277 ?  117 LYS   B CD    1 
ATOM   2313 C  CE    . LYS   B 1 118 ? 59.11100 -13.81300 16.84200  1.000 37.43427 ?  117 LYS   B CE    1 
ATOM   2314 N  NZ    . LYS   B 1 118 ? 60.48600 -14.33200 17.04800  1.000 31.57121 ?  117 LYS   B NZ    1 
ATOM   2315 N  N     A CYS   B 1 119 ? 54.81500 -8.80700  13.43400  0.500 37.71146 ?  118 CYS   B N     1 
ATOM   2316 N  N     B CYS   B 1 119 ? 54.81800 -8.81400  13.42100  0.500 37.71169 ?  118 CYS   B N     1 
ATOM   2317 C  CA    A CYS   B 1 119 ? 54.42900 -8.05500  12.24100  0.500 37.96114 ?  118 CYS   B CA    1 
ATOM   2318 C  CA    B CYS   B 1 119 ? 54.48800 -8.10100  12.19100  0.500 37.96478 ?  118 CYS   B CA    1 
ATOM   2319 C  C     A CYS   B 1 119 ? 55.22000 -6.76400  12.05900  0.500 41.32111 ?  118 CYS   B C     1 
ATOM   2320 C  C     B CYS   B 1 119 ? 55.27400 -6.80100  12.02500  0.500 41.33185 ?  118 CYS   B C     1 
ATOM   2321 O  O     A CYS   B 1 119 ? 55.10200 -6.12300  11.00200  0.500 42.96835 ?  118 CYS   B O     1 
ATOM   2322 O  O     B CYS   B 1 119 ? 55.21100 -6.19000  10.94600  0.500 42.94194 ?  118 CYS   B O     1 
ATOM   2323 C  CB    A CYS   B 1 119 ? 52.93600 -7.74900  12.27200  0.500 37.95901 ?  118 CYS   B CB    1 
ATOM   2324 C  CB    B CYS   B 1 119 ? 52.99100 -7.83000  12.13100  0.500 37.95515 ?  118 CYS   B CB    1 
ATOM   2325 S  SG    A CYS   B 1 119 ? 51.91300 -9.12800  11.74000  0.500 36.23991 ?  118 CYS   B SG    1 
ATOM   2326 S  SG    B CYS   B 1 119 ? 52.45000 -6.59200  13.28800  0.500 46.43168 ?  118 CYS   B SG    1 
ATOM   2327 N  N     . ASP   B 1 120 ? 56.02500 -6.37300  13.04700  1.000 36.78549 ?  119 ASP   B N     1 
ATOM   2328 C  CA    . ASP   B 1 120 ? 56.94000 -5.24900  12.87200  1.000 37.96426 ?  119 ASP   B CA    1 
ATOM   2329 C  C     . ASP   B 1 120 ? 58.09000 -5.59300  11.94700  1.000 42.26221 ?  119 ASP   B C     1 
ATOM   2330 O  O     . ASP   B 1 120 ? 58.70000 -4.68500  11.36700  1.000 45.99881 ?  119 ASP   B O     1 
ATOM   2331 C  CB    . ASP   B 1 120 ? 57.51800 -4.79900  14.21900  1.000 38.22002 ?  119 ASP   B CB    1 
ATOM   2332 C  CG    . ASP   B 1 120 ? 58.19900 -5.93600  14.98100  1.000 39.37445 ?  119 ASP   B CG    1 
ATOM   2333 O  OD1   . ASP   B 1 120 ? 57.49100 -6.90100  15.37300  1.000 40.69023 ?  119 ASP   B OD1   1 
ATOM   2334 O  OD2   . ASP   B 1 120 ? 59.43300 -5.86100  15.20600  1.000 43.47624 -1 119 ASP   B OD2   1 
ATOM   2335 N  N     . LEU   B 1 121 ? 58.39700 -6.88300  11.79200  1.000 39.71645 ?  120 LEU   B N     1 
ATOM   2336 C  CA    . LEU   B 1 121 ? 59.62400 -7.28800  11.12400  1.000 43.07547 ?  120 LEU   B CA    1 
ATOM   2337 C  C     . LEU   B 1 121 ? 59.48400 -7.25100  9.60100   1.000 40.02507 ?  120 LEU   B C     1 
ATOM   2338 O  O     . LEU   B 1 121 ? 58.37600 -7.35200  9.05700   1.000 40.90843 ?  120 LEU   B O     1 
ATOM   2339 C  CB    . LEU   B 1 121 ? 60.04200 -8.69200  11.57300  1.000 32.81497 ?  120 LEU   B CB    1 
ATOM   2340 C  CG    . LEU   B 1 121 ? 60.63400 -8.73100  12.99400  1.000 44.21807 ?  120 LEU   B CG    1 
ATOM   2341 C  CD1   . LEU   B 1 121 ? 61.26800 -10.08400 13.29700  1.000 38.66547 ?  120 LEU   B CD1   1 
ATOM   2342 C  CD2   . LEU   B 1 121 ? 61.63800 -7.61300  13.16500  1.000 42.84677 ?  120 LEU   B CD2   1 
ATOM   2343 N  N     . PRO   B 1 122 ? 60.59700 -7.08700  8.89800   1.000 45.36261 ?  121 PRO   B N     1 
ATOM   2344 C  CA    . PRO   B 1 122 ? 60.55600 -7.06700  7.43500   1.000 37.67402 ?  121 PRO   B CA    1 
ATOM   2345 C  C     . PRO   B 1 122 ? 60.54500 -8.47200  6.84000   1.000 46.30165 ?  121 PRO   B C     1 
ATOM   2346 O  O     . PRO   B 1 122 ? 60.82200 -9.47800  7.50100   1.000 41.35237 ?  121 PRO   B O     1 
ATOM   2347 C  CB    . PRO   B 1 122 ? 61.83700 -6.31400  7.05600   1.000 40.85870 ?  121 PRO   B CB    1 
ATOM   2348 C  CG    . PRO   B 1 122 ? 62.76300 -6.54300  8.23200   1.000 38.08351 ?  121 PRO   B CG    1 
ATOM   2349 C  CD    . PRO   B 1 122 ? 61.88600 -6.60800  9.43800   1.000 39.34625 ?  121 PRO   B CD    1 
ATOM   2350 N  N     . SER   B 1 123 ? 60.18900 -8.51100  5.55600   1.000 40.73114 ?  122 SER   B N     1 
ATOM   2351 C  CA    . SER   B 1 123 ? 60.40200 -9.68700  4.70900   1.000 45.78763 ?  122 SER   B CA    1 
ATOM   2352 C  C     . SER   B 1 123 ? 59.66600 -10.91200 5.25700   1.000 42.28577 ?  122 SER   B C     1 
ATOM   2353 O  O     . SER   B 1 123 ? 60.19300 -12.03100 5.26600   1.000 47.05812 ?  122 SER   B O     1 
ATOM   2354 C  CB    . SER   B 1 123 ? 61.90000 -9.96600  4.53200   1.000 48.12315 ?  122 SER   B CB    1 
ATOM   2355 O  OG    . SER   B 1 123 ? 62.52300 -8.90800  3.82300   1.000 49.08821 ?  122 SER   B OG    1 
ATOM   2356 N  N     . ARG   B 1 124 ? 58.42300 -10.69000 5.69600   1.000 40.18539 ?  123 ARG   B N     1 
ATOM   2357 C  CA    . ARG   B 1 124 ? 57.60400 -11.77700 6.20200   1.000 41.84547 ?  123 ARG   B CA    1 
ATOM   2358 C  C     . ARG   B 1 124 ? 57.48700 -12.87900 5.16200   1.000 44.43872 ?  123 ARG   B C     1 
ATOM   2359 O  O     . ARG   B 1 124 ? 57.29500 -12.61600 3.97100   1.000 46.71413 ?  123 ARG   B O     1 
ATOM   2360 C  CB    . ARG   B 1 124 ? 56.21900 -11.27500 6.60700   1.000 46.29931 ?  123 ARG   B CB    1 
ATOM   2361 C  CG    . ARG   B 1 124 ? 55.37100 -10.70400 5.51600   1.000 41.19822 ?  123 ARG   B CG    1 
ATOM   2362 C  CD    . ARG   B 1 124 ? 54.17700 -10.00000 6.15600   1.000 43.90480 ?  123 ARG   B CD    1 
ATOM   2363 N  NE    . ARG   B 1 124 ? 53.08100 -10.90400 6.50300   1.000 50.57722 ?  123 ARG   B NE    1 
ATOM   2364 C  CZ    . ARG   B 1 124 ? 51.97700 -10.52900 7.14000   1.000 46.88393 ?  123 ARG   B CZ    1 
ATOM   2365 N  NH1   . ARG   B 1 124 ? 51.81500 -9.28200  7.56300   1.000 48.39233 ?  123 ARG   B NH1   1 
ATOM   2366 N  NH2   . ARG   B 1 124 ? 51.01700 -11.42900 7.36700   1.000 47.61519 ?  123 ARG   B NH2   1 
ATOM   2367 N  N     . THR   B 1 125 ? 57.64400 -14.11100 5.62000   1.000 43.04932 ?  124 THR   B N     1 
ATOM   2368 C  CA    . THR   B 1 125 ? 57.61200 -15.27600 4.75300   1.000 44.21583 ?  124 THR   B CA    1 
ATOM   2369 C  C     . THR   B 1 125 ? 56.23100 -15.91800 4.69500   1.000 47.33133 ?  124 THR   B C     1 
ATOM   2370 O  O     . THR   B 1 125 ? 55.99900 -16.80300 3.85900   1.000 46.74296 ?  124 THR   B O     1 
ATOM   2371 C  CB    . THR   B 1 125 ? 58.64000 -16.28400 5.24700   1.000 42.78692 ?  124 THR   B CB    1 
ATOM   2372 O  OG1   . THR   B 1 125 ? 58.34600 -16.58400 6.61800   1.000 46.65435 ?  124 THR   B OG1   1 
ATOM   2373 C  CG2   . THR   B 1 125 ? 60.04400 -15.68900 5.17300   1.000 41.28143 ?  124 THR   B CG2   1 
ATOM   2374 N  N     . VAL   B 1 126 ? 55.32300 -15.49600 5.57000   1.000 39.39487 ?  125 VAL   B N     1 
ATOM   2375 C  CA    . VAL   B 1 126 ? 53.95400 -15.98000 5.61100   1.000 40.25742 ?  125 VAL   B CA    1 
ATOM   2376 C  C     . VAL   B 1 126 ? 53.07200 -14.79900 5.25200   1.000 43.70835 ?  125 VAL   B C     1 
ATOM   2377 O  O     . VAL   B 1 126 ? 52.93800 -13.85600 6.04100   1.000 40.21437 ?  125 VAL   B O     1 
ATOM   2378 C  CB    . VAL   B 1 126 ? 53.58900 -16.54700 6.98800   1.000 40.94791 ?  125 VAL   B CB    1 
ATOM   2379 C  CG1   . VAL   B 1 126 ? 52.21000 -17.21100 6.92800   1.000 40.91529 ?  125 VAL   B CG1   1 
ATOM   2380 C  CG2   . VAL   B 1 126 ? 54.67500 -17.50500 7.46600   1.000 40.29016 ?  125 VAL   B CG2   1 
ATOM   2381 N  N     . ASP   B 1 127 ? 52.49400 -14.81800 4.05600   1.000 47.33149 ?  126 ASP   B N     1 
ATOM   2382 C  CA    . ASP   B 1 127 ? 51.71000 -13.65000 3.71200   1.000 45.69991 ?  126 ASP   B CA    1 
ATOM   2383 C  C     . ASP   B 1 127 ? 50.32300 -13.74800 4.33900   1.000 47.84685 ?  126 ASP   B C     1 
ATOM   2384 O  O     . ASP   B 1 127 ? 49.92000 -14.78100 4.87800   1.000 45.52480 ?  126 ASP   B O     1 
ATOM   2385 C  CB    . ASP   B 1 127 ? 51.64600 -13.46000 2.19000   1.000 52.34595 ?  126 ASP   B CB    1 
ATOM   2386 C  CG    . ASP   B 1 127 ? 50.77300 -14.49300 1.48900   1.000 49.32437 ?  126 ASP   B CG    1 
ATOM   2387 O  OD1   . ASP   B 1 127 ? 49.53300 -14.43100 1.64900   1.000 56.81651 ?  126 ASP   B OD1   1 
ATOM   2388 O  OD2   . ASP   B 1 127 ? 51.33300 -15.34300 0.75200   1.000 56.87063 -1 126 ASP   B OD2   1 
ATOM   2389 N  N     . THR   B 1 128 ? 49.59600 -12.63400 4.27900   1.000 49.64656 ?  127 THR   B N     1 
ATOM   2390 C  CA    . THR   B 1 128 ? 48.30900 -12.55100 4.96100   1.000 50.30097 ?  127 THR   B CA    1 
ATOM   2391 C  C     . THR   B 1 128 ? 47.30300 -13.54400 4.38400   1.000 52.84343 ?  127 THR   B C     1 
ATOM   2392 O  O     . THR   B 1 128 ? 46.46600 -14.08400 5.11800   1.000 54.19279 ?  127 THR   B O     1 
ATOM   2393 C  CB    . THR   B 1 128 ? 47.77400 -11.11700 4.88200   1.000 50.51066 ?  127 THR   B CB    1 
ATOM   2394 O  OG1   . THR   B 1 128 ? 48.75100 -10.21700 5.42500   1.000 53.08786 ?  127 THR   B OG1   1 
ATOM   2395 C  CG2   . THR   B 1 128 ? 46.46500 -10.96500 5.66100   1.000 47.01497 ?  127 THR   B CG2   1 
ATOM   2396 N  N     . LYS   B 1 129 ? 47.37400 -13.80700 3.07200   1.000 48.76355 ?  128 LYS   B N     1 
ATOM   2397 C  CA    . LYS   B 1 129 ? 46.41000 -14.72200 2.46800   1.000 48.75719 ?  128 LYS   B CA    1 
ATOM   2398 C  C     . LYS   B 1 129 ? 46.69200 -16.16200 2.87100   1.000 46.79491 ?  128 LYS   B C     1 
ATOM   2399 O  O     . LYS   B 1 129 ? 45.76300 -16.96800 2.99400   1.000 50.86777 ?  128 LYS   B O     1 
ATOM   2400 C  CB    . LYS   B 1 129 ? 46.41400 -14.59200 0.94300   1.000 49.50691 ?  128 LYS   B CB    1 
ATOM   2401 C  CG    . LYS   B 1 129 ? 45.45400 -15.55700 0.26200   1.000 48.82499 ?  128 LYS   B CG    1 
ATOM   2402 C  CD    . LYS   B 1 129 ? 45.66300 -15.60800 -1.25100  1.000 51.18872 ?  128 LYS   B CD    1 
ATOM   2403 C  CE    . LYS   B 1 129 ? 44.75500 -16.66000 -1.88900  1.000 49.42316 ?  128 LYS   B CE    1 
ATOM   2404 N  NZ    . LYS   B 1 129 ? 43.32900 -16.51000 -1.45000  1.000 57.04157 ?  128 LYS   B NZ    1 
ATOM   2405 N  N     . GLN   B 1 130 ? 47.96700 -16.51200 3.05100   1.000 47.51391 ?  129 GLN   B N     1 
ATOM   2406 C  CA    . GLN   B 1 130 ? 48.29700 -17.80500 3.63800   1.000 47.59895 ?  129 GLN   B CA    1 
ATOM   2407 C  C     . GLN   B 1 130 ? 47.59300 -17.96200 4.98000   1.000 45.83713 ?  129 GLN   B C     1 
ATOM   2408 O  O     . GLN   B 1 130 ? 46.82800 -18.91000 5.20400   1.000 47.61436 ?  129 GLN   B O     1 
ATOM   2409 C  CB    . GLN   B 1 130 ? 49.81300 -17.94000 3.81900   1.000 44.45581 ?  129 GLN   B CB    1 
ATOM   2410 C  CG    . GLN   B 1 130 ? 50.62000 -18.25700 2.57100   1.000 52.99070 ?  129 GLN   B CG    1 
ATOM   2411 C  CD    . GLN   B 1 130 ? 52.09200 -18.46100 2.89900   1.000 54.48168 ?  129 GLN   B CD    1 
ATOM   2412 O  OE1   . GLN   B 1 130 ? 52.89700 -17.52800 2.80400   1.000 55.95500 ?  129 GLN   B OE1   1 
ATOM   2413 N  NE2   . GLN   B 1 130 ? 52.45000 -19.68400 3.30800   1.000 51.90065 ?  129 GLN   B NE2   1 
ATOM   2414 N  N     . ALA   B 1 131 ? 47.82000 -16.99800 5.87700   1.000 49.18858 ?  130 ALA   B N     1 
ATOM   2415 C  CA    . ALA   B 1 131 ? 47.24700 -17.09000 7.21400   1.000 41.24401 ?  130 ALA   B CA    1 
ATOM   2416 C  C     . ALA   B 1 131 ? 45.73000 -16.95700 7.17900   1.000 45.11841 ?  130 ALA   B C     1 
ATOM   2417 O  O     . ALA   B 1 131 ? 45.02700 -17.68500 7.89300   1.000 43.33796 ?  130 ALA   B O     1 
ATOM   2418 C  CB    . ALA   B 1 131 ? 47.87000 -16.03800 8.11800   1.000 44.67840 ?  130 ALA   B CB    1 
ATOM   2419 N  N     . GLN   B 1 132 ? 45.19600 -16.06300 6.32900   1.000 48.14896 ?  131 GLN   B N     1 
ATOM   2420 C  CA    . GLN   B 1 132 ? 43.74300 -15.90300 6.25900   1.000 40.68695 ?  131 GLN   B CA    1 
ATOM   2421 C  C     . GLN   B 1 132 ? 43.06900 -17.14000 5.68200   1.000 47.68886 ?  131 GLN   B C     1 
ATOM   2422 O  O     . GLN   B 1 132 ? 41.99000 -17.53000 6.14800   1.000 47.68780 ?  131 GLN   B O     1 
ATOM   2423 C  CB    . GLN   B 1 132 ? 43.36600 -14.67300 5.43600   1.000 47.80879 ?  131 GLN   B CB    1 
ATOM   2424 C  CG    . GLN   B 1 132 ? 43.56600 -13.36400 6.16700   1.000 45.25225 ?  131 GLN   B CG    1 
ATOM   2425 C  CD    . GLN   B 1 132 ? 43.36900 -12.14800 5.27500   1.000 57.98529 ?  131 GLN   B CD    1 
ATOM   2426 O  OE1   . GLN   B 1 132 ? 43.47800 -12.22600 4.04200   1.000 55.76704 ?  131 GLN   B OE1   1 
ATOM   2427 N  NE2   . GLN   B 1 132 ? 43.09100 -11.00500 5.90000   1.000 58.64743 ?  131 GLN   B NE2   1 
ATOM   2428 N  N     . ASP   B 1 133 ? 43.67800 -17.76700 4.66400   1.000 41.63368 ?  132 ASP   B N     1 
ATOM   2429 C  CA    . ASP   B 1 133 ? 43.09900 -18.99800 4.13600   1.000 43.95226 ?  132 ASP   B CA    1 
ATOM   2430 C  C     . ASP   B 1 133 ? 43.05500 -20.08500 5.19800   1.000 44.53774 ?  132 ASP   B C     1 
ATOM   2431 O  O     . ASP   B 1 133 ? 42.04600 -20.79100 5.33300   1.000 49.63723 ?  132 ASP   B O     1 
ATOM   2432 C  CB    . ASP   B 1 133 ? 43.87600 -19.48400 2.91000   1.000 38.02778 ?  132 ASP   B CB    1 
ATOM   2433 C  CG    . ASP   B 1 133 ? 43.53200 -18.68600 1.65600   1.000 49.33467 ?  132 ASP   B CG    1 
ATOM   2434 O  OD1   . ASP   B 1 133 ? 42.67800 -17.75800 1.74500   1.000 48.94777 ?  132 ASP   B OD1   1 
ATOM   2435 O  OD2   . ASP   B 1 133 ? 44.11900 -18.98600 0.59000   1.000 51.79532 -1 132 ASP   B OD2   1 
ATOM   2436 N  N     . LEU   B 1 134 ? 44.14000 -20.23200 5.96600   1.000 40.06692 ?  133 LEU   B N     1 
ATOM   2437 C  CA    . LEU   B 1 134 ? 44.17200 -21.24000 7.02500   1.000 45.64689 ?  133 LEU   B CA    1 
ATOM   2438 C  C     . LEU   B 1 134 ? 43.07000 -20.99600 8.05500   1.000 40.58899 ?  133 LEU   B C     1 
ATOM   2439 O  O     . LEU   B 1 134 ? 42.35000 -21.92400 8.45500   1.000 41.44582 ?  133 LEU   B O     1 
ATOM   2440 C  CB    . LEU   B 1 134 ? 45.54600 -21.24700 7.70100   1.000 39.95178 ?  133 LEU   B CB    1 
ATOM   2441 C  CG    . LEU   B 1 134 ? 45.73200 -22.40200 8.67600   1.000 42.51094 ?  133 LEU   B CG    1 
ATOM   2442 C  CD1   . LEU   B 1 134 ? 45.68800 -23.74800 7.93300   1.000 43.81002 ?  133 LEU   B CD1   1 
ATOM   2443 C  CD2   . LEU   B 1 134 ? 47.04200 -22.23600 9.45200   1.000 42.82339 ?  133 LEU   B CD2   1 
ATOM   2444 N  N     . ALA   B 1 135 ? 42.92200 -19.74600 8.49400   1.000 38.80117 ?  134 ALA   B N     1 
ATOM   2445 C  CA    . ALA   B 1 135 ? 41.90800 -19.43300 9.49800   1.000 41.44792 ?  134 ALA   B CA    1 
ATOM   2446 C  C     . ALA   B 1 135 ? 40.50900 -19.72000 8.97100   1.000 46.20847 ?  134 ALA   B C     1 
ATOM   2447 O  O     . ALA   B 1 135 ? 39.69000 -20.34500 9.65600   1.000 44.04638 ?  134 ALA   B O     1 
ATOM   2448 C  CB    . ALA   B 1 135 ? 42.03500 -17.97400 9.92700   1.000 39.10902 ?  134 ALA   B CB    1 
ATOM   2449 N  N     . ARG   B 1 136 ? 40.22700 -19.27000 7.74200   1.000 45.72620 ?  135 ARG   B N     1 
ATOM   2450 C  CA    . ARG   B 1 136 ? 38.98100 -19.60400 7.06300   1.000 42.47121 ?  135 ARG   B CA    1 
ATOM   2451 C  C     . ARG   B 1 136 ? 38.72600 -21.10400 7.09200   1.000 47.21694 ?  135 ARG   B C     1 
ATOM   2452 O  O     . ARG   B 1 136 ? 37.61500 -21.55300 7.40400   1.000 49.83026 ?  135 ARG   B O     1 
ATOM   2453 C  CB    . ARG   B 1 136 ? 39.04500 -19.09200 5.61600   1.000 46.79802 ?  135 ARG   B CB    1 
ATOM   2454 C  CG    . ARG   B 1 136 ? 37.70500 -18.96400 4.88800   1.000 55.26208 ?  135 ARG   B CG    1 
ATOM   2455 C  CD    . ARG   B 1 136 ? 37.85700 -18.24700 3.52800   1.000 54.27781 ?  135 ARG   B CD    1 
ATOM   2456 N  NE    . ARG   B 1 136 ? 38.57800 -16.98100 3.64200   1.000 50.12599 ?  135 ARG   B NE    1 
ATOM   2457 C  CZ    . ARG   B 1 136 ? 38.05500 -15.85500 4.11100   1.000 56.54857 ?  135 ARG   B CZ    1 
ATOM   2458 N  NH1   . ARG   B 1 136 ? 36.78600 -15.78100 4.48100   1.000 61.61114 ?  135 ARG   B NH1   1 
ATOM   2459 N  NH2   . ARG   B 1 136 ? 38.82700 -14.77500 4.22000   1.000 59.31780 ?  135 ARG   B NH2   1 
ATOM   2460 N  N     . SER   B 1 137 ? 39.75100 -21.90000 6.76600   1.000 43.20227 ?  136 SER   B N     1 
ATOM   2461 C  CA    . SER   B 1 137 ? 39.57100 -23.34500 6.72000   1.000 44.82129 ?  136 SER   B CA    1 
ATOM   2462 C  C     . SER   B 1 137 ? 39.27800 -23.92700 8.09000   1.000 48.74515 ?  136 SER   B C     1 
ATOM   2463 O  O     . SER   B 1 137 ? 38.67800 -25.00600 8.17800   1.000 51.66108 ?  136 SER   B O     1 
ATOM   2464 C  CB    . SER   B 1 137 ? 40.80500 -24.02200 6.12700   1.000 44.57117 ?  136 SER   B CB    1 
ATOM   2465 O  OG    . SER   B 1 137 ? 41.84400 -24.11900 7.08200   1.000 51.78204 ?  136 SER   B OG    1 
ATOM   2466 N  N     . TYR   B 1 138 ? 39.70300 -23.24100 9.15600   1.000 44.01955 ?  137 TYR   B N     1 
ATOM   2467 C  CA    . TYR   B 1 138 ? 39.39800 -23.65100 10.51400  1.000 46.74352 ?  137 TYR   B CA    1 
ATOM   2468 C  C     . TYR   B 1 138 ? 38.13200 -23.00400 11.05100  1.000 44.89434 ?  137 TYR   B C     1 
ATOM   2469 O  O     . TYR   B 1 138 ? 37.56800 -23.49900 12.03100  1.000 49.95186 ?  137 TYR   B O     1 
ATOM   2470 C  CB    . TYR   B 1 138 ? 40.57700 -23.31000 11.43700  1.000 45.35783 ?  137 TYR   B CB    1 
ATOM   2471 C  CG    . TYR   B 1 138 ? 41.84100 -24.12500 11.19100  1.000 44.97183 ?  137 TYR   B CG    1 
ATOM   2472 C  CD1   . TYR   B 1 138 ? 41.78300 -25.42400 10.67200  1.000 42.02829 ?  137 TYR   B CD1   1 
ATOM   2473 C  CD2   . TYR   B 1 138 ? 43.09300 -23.60000 11.50100  1.000 46.42161 ?  137 TYR   B CD2   1 
ATOM   2474 C  CE1   . TYR   B 1 138 ? 42.94800 -26.16700 10.45900  1.000 44.37516 ?  137 TYR   B CE1   1 
ATOM   2475 C  CE2   . TYR   B 1 138 ? 44.25100 -24.32900 11.29900  1.000 43.12086 ?  137 TYR   B CE2   1 
ATOM   2476 C  CZ    . TYR   B 1 138 ? 44.17800 -25.61100 10.78200  1.000 43.40335 ?  137 TYR   B CZ    1 
ATOM   2477 O  OH    . TYR   B 1 138 ? 45.34900 -26.31900 10.60400  1.000 42.01943 ?  137 TYR   B OH    1 
ATOM   2478 N  N     . GLY   B 1 139 ? 37.66400 -21.92400 10.43200  1.000 44.69302 ?  138 GLY   B N     1 
ATOM   2479 C  CA    . GLY   B 1 139 ? 36.51700 -21.21400 10.96100  1.000 42.13846 ?  138 GLY   B CA    1 
ATOM   2480 C  C     . GLY   B 1 139 ? 36.82100 -20.36600 12.17700  1.000 43.70764 ?  138 GLY   B C     1 
ATOM   2481 O  O     . GLY   B 1 139 ? 35.97800 -20.24500 13.07800  1.000 42.34856 ?  138 GLY   B O     1 
ATOM   2482 N  N     . ILE   B 1 140 ? 38.00100 -19.75500 12.22400  1.000 42.97840 ?  139 ILE   B N     1 
ATOM   2483 C  CA    . ILE   B 1 140 ? 38.42600 -18.95600 13.37200  1.000 40.44142 ?  139 ILE   B CA    1 
ATOM   2484 C  C     . ILE   B 1 140 ? 39.03100 -17.64900 12.87200  1.000 36.77357 ?  139 ILE   B C     1 
ATOM   2485 O  O     . ILE   B 1 140 ? 39.40700 -17.52600 11.70300  1.000 40.67024 ?  139 ILE   B O     1 
ATOM   2486 C  CB    . ILE   B 1 140 ? 39.45700 -19.70400 14.24100  1.000 35.22285 ?  139 ILE   B CB    1 
ATOM   2487 C  CG1   . ILE   B 1 140 ? 40.81200 -19.74100 13.50900  1.000 36.42890 ?  139 ILE   B CG1   1 
ATOM   2488 C  CG2   . ILE   B 1 140 ? 38.90300 -21.05600 14.67100  1.000 34.30006 ?  139 ILE   B CG2   1 
ATOM   2489 C  CD1   . ILE   B 1 140 ? 41.91800 -20.50500 14.25300  1.000 33.33279 ?  139 ILE   B CD1   1 
ATOM   2490 N  N     . PRO   B 1 141 ? 39.15700 -16.66700 13.76500  1.000 37.93672 ?  140 PRO   B N     1 
ATOM   2491 C  CA    . PRO   B 1 141 ? 39.75300 -15.38100 13.38200  1.000 35.39424 ?  140 PRO   B CA    1 
ATOM   2492 C  C     . PRO   B 1 141 ? 41.25800 -15.44800 13.20000  1.000 41.65134 ?  140 PRO   B C     1 
ATOM   2493 O  O     . PRO   B 1 141 ? 41.95000 -16.31900 13.73200  1.000 40.03638 ?  140 PRO   B O     1 
ATOM   2494 C  CB    . PRO   B 1 141 ? 39.40200 -14.46300 14.56800  1.000 36.81861 ?  140 PRO   B CB    1 
ATOM   2495 C  CG    . PRO   B 1 141 ? 38.25800 -15.07300 15.20500  1.000 32.88139 ?  140 PRO   B CG    1 
ATOM   2496 C  CD    . PRO   B 1 141 ? 38.43500 -16.55800 15.04600  1.000 37.02567 ?  140 PRO   B CD    1 
ATOM   2497 N  N     . PHE   B 1 142 ? 41.77000 -14.46300 12.46200  1.000 40.23443 ?  141 PHE   B N     1 
ATOM   2498 C  CA    . PHE   B 1 142 ? 43.20000 -14.27300 12.28300  1.000 37.59041 ?  141 PHE   B CA    1 
ATOM   2499 C  C     . PHE   B 1 142 ? 43.56500 -12.85700 12.69000  1.000 37.25579 ?  141 PHE   B C     1 
ATOM   2500 O  O     . PHE   B 1 142 ? 43.02500 -11.88400 12.14300  1.000 36.37310 ?  141 PHE   B O     1 
ATOM   2501 C  CB    . PHE   B 1 142 ? 43.65100 -14.53800 10.84500  1.000 38.17278 ?  141 PHE   B CB    1 
ATOM   2502 C  CG    . PHE   B 1 142 ? 45.06300 -14.08900 10.58300  1.000 38.74370 ?  141 PHE   B CG    1 
ATOM   2503 C  CD1   . PHE   B 1 142 ? 46.11500 -14.61000 11.32100  1.000 36.09216 ?  141 PHE   B CD1   1 
ATOM   2504 C  CD2   . PHE   B 1 142 ? 45.34500 -13.13000 9.61800   1.000 41.41797 ?  141 PHE   B CD2   1 
ATOM   2505 C  CE1   . PHE   B 1 142 ? 47.41000 -14.19700 11.10200  1.000 37.96724 ?  141 PHE   B CE1   1 
ATOM   2506 C  CE2   . PHE   B 1 142 ? 46.64300 -12.71600 9.39000   1.000 42.52965 ?  141 PHE   B CE2   1 
ATOM   2507 C  CZ    . PHE   B 1 142 ? 47.68100 -13.25400 10.14200  1.000 41.82616 ?  141 PHE   B CZ    1 
ATOM   2508 N  N     . ILE   B 1 143 ? 44.47000 -12.74600 13.65500  1.000 37.25976 ?  142 ILE   B N     1 
ATOM   2509 C  CA    . ILE   B 1 143 ? 44.91800 -11.46500 14.18500  1.000 41.20938 ?  142 ILE   B CA    1 
ATOM   2510 C  C     . ILE   B 1 143 ? 46.41500 -11.35200 13.97500  1.000 38.50754 ?  142 ILE   B C     1 
ATOM   2511 O  O     . ILE   B 1 143 ? 47.17900 -12.23500 14.38500  1.000 38.06720 ?  142 ILE   B O     1 
ATOM   2512 C  CB    . ILE   B 1 143 ? 44.58500 -11.30100 15.68000  1.000 37.19323 ?  142 ILE   B CB    1 
ATOM   2513 C  CG1   . ILE   B 1 143 ? 43.08400 -11.49300 15.92100  1.000 40.35964 ?  142 ILE   B CG1   1 
ATOM   2514 C  CG2   . ILE   B 1 143 ? 45.04400 -9.93500  16.15200  1.000 36.00662 ?  142 ILE   B CG2   1 
ATOM   2515 C  CD1   . ILE   B 1 143 ? 42.20400 -10.35100 15.35100  1.000 44.97229 ?  142 ILE   B CD1   1 
ATOM   2516 N  N     . GLU   B 1 144 ? 46.83400 -10.26800 13.34100  1.000 38.16646 ?  143 GLU   B N     1 
ATOM   2517 C  CA    . GLU   B 1 144 ? 48.24100 -9.93300  13.25400  1.000 35.99049 ?  143 GLU   B CA    1 
ATOM   2518 C  C     . GLU   B 1 144 ? 48.63500 -9.15100  14.49000  1.000 38.44807 ?  143 GLU   B C     1 
ATOM   2519 O  O     . GLU   B 1 144 ? 47.86800 -8.30800  14.97600  1.000 35.34971 ?  143 GLU   B O     1 
ATOM   2520 C  CB    . GLU   B 1 144 ? 48.52500 -9.10600  12.00200  1.000 40.00081 ?  143 GLU   B CB    1 
ATOM   2521 C  CG    . GLU   B 1 144 ? 48.00500 -9.74900  10.73400  1.000 46.04833 ?  143 GLU   B CG    1 
ATOM   2522 C  CD    . GLU   B 1 144 ? 48.39400 -8.97900  9.47500   1.000 51.33840 ?  143 GLU   B CD    1 
ATOM   2523 O  OE1   . GLU   B 1 144 ? 49.41900 -8.25200  9.50600   1.000 54.42706 ?  143 GLU   B OE1   1 
ATOM   2524 O  OE2   . GLU   B 1 144 ? 47.66800 -9.11100  8.46100   1.000 52.89424 -1 143 GLU   B OE2   1 
ATOM   2525 N  N     . THR   B 1 145 ? 49.82500 -9.44100  15.00700  1.000 38.38448 ?  144 THR   B N     1 
ATOM   2526 C  CA    . THR   B 1 145 ? 50.28400 -8.80500  16.23000  1.000 37.04011 ?  144 THR   B CA    1 
ATOM   2527 C  C     . THR   B 1 145 ? 51.75300 -8.47500  16.11600  1.000 35.23544 ?  144 THR   B C     1 
ATOM   2528 O  O     . THR   B 1 145 ? 52.50800 -9.08500  15.34700  1.000 37.49507 ?  144 THR   B O     1 
ATOM   2529 C  CB    . THR   B 1 145 ? 50.10500 -9.69300  17.48900  1.000 34.62007 ?  144 THR   B CB    1 
ATOM   2530 O  OG1   . THR   B 1 145 ? 50.90500 -10.87500 17.33500  1.000 30.80229 ?  144 THR   B OG1   1 
ATOM   2531 C  CG2   . THR   B 1 145 ? 48.65500 -10.06500 17.70800  1.000 33.00379 ?  144 THR   B CG2   1 
ATOM   2532 N  N     . SER   B 1 146 ? 52.15400 -7.50700  16.92200  1.000 34.71115 ?  145 SER   B N     1 
ATOM   2533 C  CA    . SER   B 1 146 ? 53.55400 -7.27600  17.22500  1.000 34.14444 ?  145 SER   B CA    1 
ATOM   2534 C  C     . SER   B 1 146 ? 53.68900 -7.09800  18.72900  1.000 34.61527 ?  145 SER   B C     1 
ATOM   2535 O  O     . SER   B 1 146 ? 53.25100 -6.08100  19.27700  1.000 36.92734 ?  145 SER   B O     1 
ATOM   2536 C  CB    . SER   B 1 146 ? 54.08500 -6.04800  16.50200  1.000 35.42251 ?  145 SER   B CB    1 
ATOM   2537 O  OG    . SER   B 1 146 ? 55.35400 -5.73800  17.04700  1.000 34.81837 ?  145 SER   B OG    1 
ATOM   2538 N  N     . ALA   B 1 147 ? 54.32300 -8.05200  19.40500  1.000 34.27902 ?  146 ALA   B N     1 
ATOM   2539 C  CA    . ALA   B 1 147 ? 54.58500 -7.83700  20.82800  1.000 33.79639 ?  146 ALA   B CA    1 
ATOM   2540 C  C     . ALA   B 1 147 ? 55.57400 -6.70500  21.07800  1.000 36.24040 ?  146 ALA   B C     1 
ATOM   2541 O  O     . ALA   B 1 147 ? 55.57500 -6.13400  22.16600  1.000 35.80430 ?  146 ALA   B O     1 
ATOM   2542 C  CB    . ALA   B 1 147 ? 55.11600 -9.11400  21.48700  1.000 32.69950 ?  146 ALA   B CB    1 
ATOM   2543 N  N     . LYS   B 1 148 ? 56.42700 -6.37400  20.10800  1.000 38.79997 ?  147 LYS   B N     1 
ATOM   2544 C  CA    . LYS   B 1 148 ? 57.43300 -5.33500  20.32700  1.000 41.07290 ?  147 LYS   B CA    1 
ATOM   2545 C  C     . LYS   B 1 148 ? 56.82500 -3.93100  20.35900  1.000 36.46533 ?  147 LYS   B C     1 
ATOM   2546 O  O     . LYS   B 1 148 ? 57.20100 -3.11500  21.20600  1.000 36.93893 ?  147 LYS   B O     1 
ATOM   2547 C  CB    . LYS   B 1 148 ? 58.51000 -5.41400  19.24300  1.000 39.83259 ?  147 LYS   B CB    1 
ATOM   2548 C  CG    . LYS   B 1 148 ? 59.73900 -4.58300  19.53800  1.000 41.35626 ?  147 LYS   B CG    1 
ATOM   2549 C  CD    . LYS   B 1 148 ? 60.54700 -4.37600  18.26700  1.000 37.47686 ?  147 LYS   B CD    1 
ATOM   2550 C  CE    . LYS   B 1 148 ? 61.84000 -3.63600  18.54800  1.000 44.05868 ?  147 LYS   B CE    1 
ATOM   2551 N  NZ    . LYS   B 1 148 ? 62.44100 -3.20300  17.26300  1.000 50.30663 ?  147 LYS   B NZ    1 
ATOM   2552 N  N     . THR   B 1 149 ? 55.91800 -3.62300  19.43100  1.000 41.88774 ?  148 THR   B N     1 
ATOM   2553 C  CA    . THR   B 1 149 ? 55.21500 -2.34100  19.40200  1.000 38.94012 ?  148 THR   B CA    1 
ATOM   2554 C  C     . THR   B 1 149 ? 53.90000 -2.36100  20.17400  1.000 38.92302 ?  148 THR   B C     1 
ATOM   2555 O  O     . THR   B 1 149 ? 53.23800 -1.32100  20.27000  1.000 43.64330 ?  148 THR   B O     1 
ATOM   2556 C  CB    . THR   B 1 149 ? 54.90100 -1.93600  17.96500  1.000 35.05175 ?  148 THR   B CB    1 
ATOM   2557 O  OG1   . THR   B 1 149 ? 53.84500 -2.77100  17.46600  1.000 43.73591 ?  148 THR   B OG1   1 
ATOM   2558 C  CG2   . THR   B 1 149 ? 56.13100 -2.07300  17.07600  1.000 38.61676 ?  148 THR   B CG2   1 
ATOM   2559 N  N     . ARG   B 1 150 ? 53.50000 -3.52600  20.68700  1.000 41.79994 ?  149 ARG   B N     1 
ATOM   2560 C  CA    . ARG   B 1 150 ? 52.21900 -3.81800  21.33000  1.000 33.07852 ?  149 ARG   B CA    1 
ATOM   2561 C  C     . ARG   B 1 150 ? 51.04500 -3.76900  20.36700  1.000 41.00367 ?  149 ARG   B C     1 
ATOM   2562 O  O     . ARG   B 1 150 ? 49.88900 -3.86400  20.80600  1.000 39.71745 ?  149 ARG   B O     1 
ATOM   2563 C  CB    . ARG   B 1 150 ? 51.94800 -2.89700  22.52700  1.000 38.90248 ?  149 ARG   B CB    1 
ATOM   2564 C  CG    . ARG   B 1 150 ? 51.22300 -3.58300  23.67200  1.000 40.82323 ?  149 ARG   B CG    1 
ATOM   2565 C  CD    . ARG   B 1 150 ? 51.08300 -2.64600  24.87800  1.000 43.09289 ?  149 ARG   B CD    1 
ATOM   2566 N  NE    . ARG   B 1 150 ? 50.49500 -3.30300  26.04600  1.000 43.59931 ?  149 ARG   B NE    1 
ATOM   2567 C  CZ    . ARG   B 1 150 ? 49.19700 -3.53800  26.19300  1.000 40.82864 ?  149 ARG   B CZ    1 
ATOM   2568 N  NH1   . ARG   B 1 150 ? 48.33400 -3.26800  25.22800  1.000 40.93358 ?  149 ARG   B NH1   1 
ATOM   2569 N  NH2   . ARG   B 1 150 ? 48.75300 -4.04500  27.34200  1.000 45.50075 ?  149 ARG   B NH2   1 
ATOM   2570 N  N     . GLN   B 1 151 ? 51.29500 -3.64800  19.06000  1.000 36.01738 ?  150 GLN   B N     1 
ATOM   2571 C  CA    . GLN   B 1 151 ? 50.18800 -3.65400  18.12300  1.000 41.64082 ?  150 GLN   B CA    1 
ATOM   2572 C  C     . GLN   B 1 151 ? 49.45000 -4.98300  18.20900  1.000 38.27527 ?  150 GLN   B C     1 
ATOM   2573 O  O     . GLN   B 1 151 ? 50.06700 -6.05600  18.16400  1.000 39.32097 ?  150 GLN   B O     1 
ATOM   2574 C  CB    . GLN   B 1 151 ? 50.68800 -3.40800  16.69300  1.000 36.24035 ?  150 GLN   B CB    1 
ATOM   2575 C  CG    . GLN   B 1 151 ? 49.71500 -3.88400  15.61800  1.000 44.53420 ?  150 GLN   B CG    1 
ATOM   2576 C  CD    . GLN   B 1 151 ? 50.45000 -4.33300  14.36200  1.000 53.01124 ?  150 GLN   B CD    1 
ATOM   2577 O  OE1   . GLN   B 1 151 ? 51.59500 -3.92000  14.12000  1.000 57.07265 ?  150 GLN   B OE1   1 
ATOM   2578 N  NE2   . GLN   B 1 151 ? 49.81300 -5.20600  13.57000  1.000 52.68220 ?  150 GLN   B NE2   1 
ATOM   2579 N  N     . GLY   B 1 152 ? 48.13600 -4.89800  18.37900  1.000 33.79700 ?  151 GLY   B N     1 
ATOM   2580 C  CA    . GLY   B 1 152 ? 47.22500 -6.01900  18.35900  1.000 32.21884 ?  151 GLY   B CA    1 
ATOM   2581 C  C     . GLY   B 1 152 ? 47.30200 -6.95200  19.55000  1.000 36.65758 ?  151 GLY   B C     1 
ATOM   2582 O  O     . GLY   B 1 152 ? 46.64200 -7.99000  19.53300  1.000 32.10307 ?  151 GLY   B O     1 
ATOM   2583 N  N     . VAL   B 1 153 ? 48.07800 -6.62300  20.58200  1.000 34.07335 ?  152 VAL   B N     1 
ATOM   2584 C  CA    . VAL   B 1 153 ? 48.21800 -7.53800  21.72500  1.000 37.41721 ?  152 VAL   B CA    1 
ATOM   2585 C  C     . VAL   B 1 153 ? 46.87800 -7.70900  22.44100  1.000 39.88811 ?  152 VAL   B C     1 
ATOM   2586 O  O     . VAL   B 1 153 ? 46.37100 -8.83100  22.59100  1.000 30.61008 ?  152 VAL   B O     1 
ATOM   2587 C  CB    . VAL   B 1 153 ? 49.31300 -7.04500  22.68800  1.000 30.19248 ?  152 VAL   B CB    1 
ATOM   2588 C  CG1   . VAL   B 1 153 ? 49.26600 -7.83300  24.01900  1.000 36.99950 ?  152 VAL   B CG1   1 
ATOM   2589 C  CG2   . VAL   B 1 153 ? 50.68100 -7.16200  22.04200  1.000 34.68355 ?  152 VAL   B CG2   1 
ATOM   2590 N  N     . ASP   B 1 154 ? 46.26600 -6.59600  22.87100  1.000 36.22752 ?  153 ASP   B N     1 
ATOM   2591 C  CA    . ASP   B 1 154 ? 44.93400 -6.68900  23.46800  1.000 35.42323 ?  153 ASP   B CA    1 
ATOM   2592 C  C     . ASP   B 1 154 ? 43.95500 -7.34600  22.51100  1.000 38.01085 ?  153 ASP   B C     1 
ATOM   2593 O  O     . ASP   B 1 154 ? 43.15900 -8.20700  22.90300  1.000 36.35243 ?  153 ASP   B O     1 
ATOM   2594 C  CB    . ASP   B 1 154 ? 44.40200 -5.30100  23.86400  1.000 40.30131 ?  153 ASP   B CB    1 
ATOM   2595 C  CG    . ASP   B 1 154 ? 45.29000 -4.58000  24.86500  1.000 46.28408 ?  153 ASP   B CG    1 
ATOM   2596 O  OD1   . ASP   B 1 154 ? 46.05300 -5.24900  25.58900  1.000 47.07419 ?  153 ASP   B OD1   1 
ATOM   2597 O  OD2   . ASP   B 1 154 ? 45.21100 -3.33000  24.93900  1.000 52.49398 -1 153 ASP   B OD2   1 
ATOM   2598 N  N     . ASP   B 1 155 ? 43.98800 -6.92600  21.24500  1.000 37.47740 ?  154 ASP   B N     1 
ATOM   2599 C  CA    . ASP   B 1 155 ? 43.06300 -7.43800  20.24700  1.000 40.39377 ?  154 ASP   B CA    1 
ATOM   2600 C  C     . ASP   B 1 155 ? 43.11400 -8.96000  20.17500  1.000 34.03098 ?  154 ASP   B C     1 
ATOM   2601 O  O     . ASP   B 1 155 ? 42.07200 -9.62200  20.09800  1.000 30.22526 ?  154 ASP   B O     1 
ATOM   2602 C  CB    . ASP   B 1 155 ? 43.40200 -6.81100  18.89100  1.000 39.27202 ?  154 ASP   B CB    1 
ATOM   2603 C  CG    . ASP   B 1 155 ? 42.34400 -7.05400  17.84200  1.000 48.36084 ?  154 ASP   B CG    1 
ATOM   2604 O  OD1   . ASP   B 1 155 ? 41.23100 -7.53200  18.18000  1.000 50.78294 ?  154 ASP   B OD1   1 
ATOM   2605 O  OD2   . ASP   B 1 155 ? 42.63700 -6.76300  16.65700  1.000 56.68926 -1 154 ASP   B OD2   1 
ATOM   2606 N  N     . ALA   B 1 156 ? 44.32000 -9.53500  20.23700  1.000 31.25836 ?  155 ALA   B N     1 
ATOM   2607 C  CA    . ALA   B 1 156 ? 44.44700 -10.98800 20.11900  1.000 36.29658 ?  155 ALA   B CA    1 
ATOM   2608 C  C     . ALA   B 1 156 ? 43.76500 -11.70500 21.28300  1.000 26.79757 ?  155 ALA   B C     1 
ATOM   2609 O  O     . ALA   B 1 156 ? 42.97100 -12.63800 21.08500  1.000 26.47383 ?  155 ALA   B O     1 
ATOM   2610 C  CB    . ALA   B 1 156 ? 45.92700 -11.36500 20.05300  1.000 27.41328 ?  155 ALA   B CB    1 
ATOM   2611 N  N     . PHE   B 1 157 ? 44.07000 -11.28500 22.51400  1.000 28.11710 ?  156 PHE   B N     1 
ATOM   2612 C  CA    . PHE   B 1 157 ? 43.45300 -11.91600 23.67800  1.000 26.83836 ?  156 PHE   B CA    1 
ATOM   2613 C  C     . PHE   B 1 157 ? 41.95900 -11.61700 23.76800  1.000 30.10623 ?  156 PHE   B C     1 
ATOM   2614 O  O     . PHE   B 1 157 ? 41.15500 -12.50300 24.09100  1.000 24.58715 ?  156 PHE   B O     1 
ATOM   2615 C  CB    . PHE   B 1 157 ? 44.16000 -11.44900 24.95500  1.000 25.61305 ?  156 PHE   B CB    1 
ATOM   2616 C  CG    . PHE   B 1 157 ? 45.52100 -12.05000 25.14900  1.000 26.45467 ?  156 PHE   B CG    1 
ATOM   2617 C  CD1   . PHE   B 1 157 ? 45.66600 -13.29400 25.74300  1.000 27.96156 ?  156 PHE   B CD1   1 
ATOM   2618 C  CD2   . PHE   B 1 157 ? 46.66500 -11.37000 24.74800  1.000 27.69970 ?  156 PHE   B CD2   1 
ATOM   2619 C  CE1   . PHE   B 1 157 ? 46.95700 -13.85000 25.91200  1.000 24.11858 ?  156 PHE   B CE1   1 
ATOM   2620 C  CE2   . PHE   B 1 157 ? 47.93100 -11.92300 24.92000  1.000 32.43409 ?  156 PHE   B CE2   1 
ATOM   2621 C  CZ    . PHE   B 1 157 ? 48.05900 -13.17700 25.51200  1.000 29.59669 ?  156 PHE   B CZ    1 
ATOM   2622 N  N     . TYR   B 1 158 ? 41.57100 -10.37000 23.50900  1.000 28.13027 ?  157 TYR   B N     1 
ATOM   2623 C  CA    . TYR   B 1 158 ? 40.15300 -10.01400 23.56300  1.000 31.69588 ?  157 TYR   B CA    1 
ATOM   2624 C  C     . TYR   B 1 158 ? 39.36100 -10.76500 22.50800  1.000 32.28672 ?  157 TYR   B C     1 
ATOM   2625 O  O     . TYR   B 1 158 ? 38.23900 -11.20300 22.76100  1.000 27.70562 ?  157 TYR   B O     1 
ATOM   2626 C  CB    . TYR   B 1 158 ? 39.97100 -8.51500  23.36000  1.000 33.50090 ?  157 TYR   B CB    1 
ATOM   2627 C  CG    . TYR   B 1 158 ? 40.43800 -7.64700  24.48200  1.000 33.39956 ?  157 TYR   B CG    1 
ATOM   2628 C  CD1   . TYR   B 1 158 ? 41.20600 -8.15600  25.52300  1.000 34.04648 ?  157 TYR   B CD1   1 
ATOM   2629 C  CD2   . TYR   B 1 158 ? 40.08400 -6.30200  24.52400  1.000 42.01194 ?  157 TYR   B CD2   1 
ATOM   2630 C  CE1   . TYR   B 1 158 ? 41.61400 -7.35800  26.56200  1.000 38.57637 ?  157 TYR   B CE1   1 
ATOM   2631 C  CE2   . TYR   B 1 158 ? 40.49100 -5.49200  25.57200  1.000 40.96868 ?  157 TYR   B CE2   1 
ATOM   2632 C  CZ    . TYR   B 1 158 ? 41.25600 -6.02600  26.58200  1.000 42.36218 ?  157 TYR   B CZ    1 
ATOM   2633 O  OH    . TYR   B 1 158 ? 41.67200 -5.22900  27.62800  1.000 51.88767 ?  157 TYR   B OH    1 
ATOM   2634 N  N     . THR   B 1 159 ? 39.92800 -10.92200 21.30700  1.000 30.14569 ?  158 THR   B N     1 
ATOM   2635 C  CA    . THR   B 1 159 ? 39.20500 -11.63900 20.26800  1.000 29.33185 ?  158 THR   B CA    1 
ATOM   2636 C  C     . THR   B 1 159 ? 38.98700 -13.09600 20.65900  1.000 25.92175 ?  158 THR   B C     1 
ATOM   2637 O  O     . THR   B 1 159 ? 37.90900 -13.64700 20.44100  1.000 28.92243 ?  158 THR   B O     1 
ATOM   2638 C  CB    . THR   B 1 159 ? 39.94100 -11.51400 18.94300  1.000 32.69580 ?  158 THR   B CB    1 
ATOM   2639 O  OG1   . THR   B 1 159 ? 39.95600 -10.12800 18.57700  1.000 35.64207 ?  158 THR   B OG1   1 
ATOM   2640 C  CG2   . THR   B 1 159 ? 39.24600 -12.33000 17.86100  1.000 31.68998 ?  158 THR   B CG2   1 
ATOM   2641 N  N     . LEU   B 1 160 ? 39.96000 -13.71500 21.33500  1.000 32.53677 ?  159 LEU   B N     1 
ATOM   2642 C  CA    . LEU   B 1 160 ? 39.72800 -15.08000 21.79800  1.000 25.52201 ?  159 LEU   B CA    1 
ATOM   2643 C  C     . LEU   B 1 160 ? 38.59600 -15.13700 22.82800  1.000 25.12553 ?  159 LEU   B C     1 
ATOM   2644 O  O     . LEU   B 1 160 ? 37.78000 -16.06700 22.81900  1.000 28.10631 ?  159 LEU   B O     1 
ATOM   2645 C  CB    . LEU   B 1 160 ? 41.02900 -15.67700 22.36800  1.000 26.29871 ?  159 LEU   B CB    1 
ATOM   2646 C  CG    . LEU   B 1 160 ? 40.89300 -17.09900 22.94500  1.000 23.40145 ?  159 LEU   B CG    1 
ATOM   2647 C  CD1   . LEU   B 1 160 ? 40.49000 -18.18500 21.93900  1.000 23.85065 ?  159 LEU   B CD1   1 
ATOM   2648 C  CD2   . LEU   B 1 160 ? 42.22500 -17.51100 23.63900  1.000 27.14893 ?  159 LEU   B CD2   1 
ATOM   2649 N  N     . VAL   B 1 161 ? 38.53100 -14.16400 23.74100  1.000 26.69223 ?  160 VAL   B N     1 
ATOM   2650 C  CA    . VAL   B 1 161 ? 37.39700 -14.13900 24.67100  1.000 25.30822 ?  160 VAL   B CA    1 
ATOM   2651 C  C     . VAL   B 1 161 ? 36.07300 -13.97100 23.91700  1.000 27.92477 ?  160 VAL   B C     1 
ATOM   2652 O  O     . VAL   B 1 161 ? 35.07600 -14.62800 24.24100  1.000 31.02819 ?  160 VAL   B O     1 
ATOM   2653 C  CB    . VAL   B 1 161 ? 37.59800 -13.04200 25.73000  1.000 26.98489 ?  160 VAL   B CB    1 
ATOM   2654 C  CG1   . VAL   B 1 161 ? 36.32000 -12.84300 26.52900  1.000 29.08414 ?  160 VAL   B CG1   1 
ATOM   2655 C  CG2   . VAL   B 1 161 ? 38.74400 -13.40300 26.63000  1.000 27.28535 ?  160 VAL   B CG2   1 
ATOM   2656 N  N     . ARG   B 1 162 ? 36.05100 -13.13900 22.86900  1.000 28.31571 ?  161 ARG   B N     1 
ATOM   2657 C  CA    . ARG   B 1 162 ? 34.81100 -13.02600 22.08300  1.000 30.62405 ?  161 ARG   B CA    1 
ATOM   2658 C  C     . ARG   B 1 162 ? 34.49100 -14.31800 21.35200  1.000 34.53224 ?  161 ARG   B C     1 
ATOM   2659 O  O     . ARG   B 1 162 ? 33.31200 -14.66300 21.20400  1.000 37.67185 ?  161 ARG   B O     1 
ATOM   2660 C  CB    . ARG   B 1 162 ? 34.89100 -11.86700 21.09900  1.000 34.34236 ?  161 ARG   B CB    1 
ATOM   2661 C  CG    . ARG   B 1 162 ? 34.97300 -10.50100 21.78100  1.000 36.31411 ?  161 ARG   B CG    1 
ATOM   2662 C  CD    . ARG   B 1 162 ? 35.15600 -9.37500  20.76300  1.000 35.72785 ?  161 ARG   B CD    1 
ATOM   2663 N  NE    . ARG   B 1 162 ? 35.40600 -8.08200  21.39100  1.000 38.87880 ?  161 ARG   B NE    1 
ATOM   2664 C  CZ    . ARG   B 1 162 ? 36.49000 -7.35000  21.17900  1.000 37.97212 ?  161 ARG   B CZ    1 
ATOM   2665 N  NH1   . ARG   B 1 162 ? 37.46300 -7.77000  20.38100  1.000 41.34227 ?  161 ARG   B NH1   1 
ATOM   2666 N  NH2   . ARG   B 1 162 ? 36.60500 -6.17000  21.78300  1.000 43.14725 ?  161 ARG   B NH2   1 
ATOM   2667 N  N     . GLU   B 1 163 ? 35.51800 -15.05200 20.90400  1.000 36.68091 ?  162 GLU   B N     1 
ATOM   2668 C  CA    . GLU   B 1 163 ? 35.28600 -16.38600 20.34700  1.000 35.63969 ?  162 GLU   B CA    1 
ATOM   2669 C  C     . GLU   B 1 163 ? 34.66000 -17.31700 21.37000  1.000 35.10158 ?  162 GLU   B C     1 
ATOM   2670 O  O     . GLU   B 1 163 ? 33.73500 -18.07300 21.05300  1.000 34.69335 ?  162 GLU   B O     1 
ATOM   2671 C  CB    . GLU   B 1 163 ? 36.59700 -16.98400 19.83300  1.000 30.89734 ?  162 GLU   B CB    1 
ATOM   2672 C  CG    . GLU   B 1 163 ? 37.01300 -16.39400 18.51000  1.000 33.22183 ?  162 GLU   B CG    1 
ATOM   2673 C  CD    . GLU   B 1 163 ? 35.88100 -16.48700 17.46700  1.000 41.17486 ?  162 GLU   B CD    1 
ATOM   2674 O  OE1   . GLU   B 1 163 ? 35.43500 -17.62100 17.14400  1.000 40.38415 ?  162 GLU   B OE1   1 
ATOM   2675 O  OE2   . GLU   B 1 163 ? 35.41500 -15.42100 17.01600  1.000 45.03578 -1 162 GLU   B OE2   1 
ATOM   2676 N  N     . ILE   B 1 164 ? 35.16700 -17.31200 22.60400  1.000 35.43151 ?  163 ILE   B N     1 
ATOM   2677 C  CA    . ILE   B 1 164 ? 34.57300 -18.17700 23.61700  1.000 31.90306 ?  163 ILE   B CA    1 
ATOM   2678 C  C     . ILE   B 1 164 ? 33.13100 -17.75800 23.89400  1.000 32.33766 ?  163 ILE   B C     1 
ATOM   2679 O  O     . ILE   B 1 164 ? 32.26300 -18.59900 24.14500  1.000 36.00254 ?  163 ILE   B O     1 
ATOM   2680 C  CB    . ILE   B 1 164 ? 35.41400 -18.17600 24.91300  1.000 30.31360 ?  163 ILE   B CB    1 
ATOM   2681 C  CG1   . ILE   B 1 164 ? 36.81200 -18.73700 24.66600  1.000 29.59323 ?  163 ILE   B CG1   1 
ATOM   2682 C  CG2   . ILE   B 1 164 ? 34.75800 -19.04300 25.94500  1.000 34.27103 ?  163 ILE   B CG2   1 
ATOM   2683 C  CD1   . ILE   B 1 164 ? 37.78600 -18.61500 25.90000  1.000 32.54983 ?  163 ILE   B CD1   1 
ATOM   2684 N  N     . ARG   B 1 165 ? 32.86000 -16.44900 23.88300  1.000 34.27222 ?  164 ARG   B N     1 
ATOM   2685 C  CA    . ARG   B 1 165 ? 31.50800 -15.97600 24.15200  1.000 35.82221 ?  164 ARG   B CA    1 
ATOM   2686 C  C     . ARG   B 1 165 ? 30.56700 -16.39200 23.02800  1.000 42.09334 ?  164 ARG   B C     1 
ATOM   2687 O  O     . ARG   B 1 165 ? 29.46900 -16.89800 23.28000  1.000 44.39401 ?  164 ARG   B O     1 
ATOM   2688 C  CB    . ARG   B 1 165 ? 31.50700 -14.45300 24.34600  1.000 33.55185 ?  164 ARG   B CB    1 
ATOM   2689 C  CG    . ARG   B 1 165 ? 32.09800 -13.97400 25.69100  1.000 34.33062 ?  164 ARG   B CG    1 
ATOM   2690 C  CD    . ARG   B 1 165 ? 32.16600 -12.43900 25.76600  1.000 34.68560 ?  164 ARG   B CD    1 
ATOM   2691 N  NE    . ARG   B 1 165 ? 32.60800 -11.95600 27.07100  1.000 33.68738 ?  164 ARG   B NE    1 
ATOM   2692 C  CZ    . ARG   B 1 165 ? 32.96300 -10.70200 27.33300  1.000 35.61821 ?  164 ARG   B CZ    1 
ATOM   2693 N  NH1   . ARG   B 1 165 ? 32.90300 -9.75400  26.40900  1.000 37.93205 ?  164 ARG   B NH1   1 
ATOM   2694 N  NH2   . ARG   B 1 165 ? 33.36500 -10.38300 28.56500  1.000 34.14527 ?  164 ARG   B NH2   1 
ATOM   2695 N  N     . LYS   B 1 166 ? 30.99900 -16.20700 21.77600  1.000 37.95279 ?  165 LYS   B N     1 
ATOM   2696 C  CA    . LYS   B 1 166 ? 30.18900 -16.63200 20.63800  1.000 44.53833 ?  165 LYS   B CA    1 
ATOM   2697 C  C     . LYS   B 1 166 ? 29.95200 -18.13700 20.65000  1.000 44.43400 ?  165 LYS   B C     1 
ATOM   2698 O  O     . LYS   B 1 166 ? 28.86300 -18.60500 20.29400  1.000 51.22223 ?  165 LYS   B O     1 
ATOM   2699 C  CB    . LYS   B 1 166 ? 30.86000 -16.20400 19.33600  1.000 43.58356 ?  165 LYS   B CB    1 
ATOM   2700 C  CG    . LYS   B 1 166 ? 30.79300 -14.70600 19.08400  1.000 40.33870 ?  165 LYS   B CG    1 
ATOM   2701 C  CD    . LYS   B 1 166 ? 31.78800 -14.28200 18.01400  1.000 44.50535 ?  165 LYS   B CD    1 
ATOM   2702 C  CE    . LYS   B 1 166 ? 31.78300 -15.23200 16.81800  1.000 48.56617 ?  165 LYS   B CE    1 
ATOM   2703 N  NZ    . LYS   B 1 166 ? 32.85200 -14.87700 15.81800  1.000 50.97218 ?  165 LYS   B NZ    1 
ATOM   2704 N  N     . HIS   B 1 167 ? 30.95400 -18.91300 21.06400  1.000 44.57782 ?  166 HIS   B N     1 
ATOM   2705 C  CA    . HIS   B 1 167 ? 30.81300 -20.36500 21.05400  1.000 44.54303 ?  166 HIS   B CA    1 
ATOM   2706 C  C     . HIS   B 1 167 ? 29.78800 -20.84200 22.07600  1.000 51.40564 ?  166 HIS   B C     1 
ATOM   2707 O  O     . HIS   B 1 167 ? 29.15300 -21.88400 21.86600  1.000 55.88657 ?  166 HIS   B O     1 
ATOM   2708 C  CB    . HIS   B 1 167 ? 32.17200 -21.02900 21.29200  1.000 46.21180 ?  166 HIS   B CB    1 
ATOM   2709 C  CG    . HIS   B 1 167 ? 32.10500 -22.52000 21.45900  1.000 52.38850 ?  166 HIS   B CG    1 
ATOM   2710 N  ND1   . HIS   B 1 167 ? 31.93800 -23.12500 22.68900  1.000 56.21852 ?  166 HIS   B ND1   1 
ATOM   2711 C  CD2   . HIS   B 1 167 ? 32.20100 -23.52600 20.55700  1.000 49.89387 ?  166 HIS   B CD2   1 
ATOM   2712 C  CE1   . HIS   B 1 167 ? 31.92200 -24.43800 22.53500  1.000 52.90241 ?  166 HIS   B CE1   1 
ATOM   2713 N  NE2   . HIS   B 1 167 ? 32.08400 -24.70700 21.25200  1.000 55.70976 ?  166 HIS   B NE2   1 
ATOM   2714 N  N     . LYS   B 1 168 ? 29.60300 -20.10400 23.17000  1.000 51.15271 ?  167 LYS   B N     1 
ATOM   2715 C  CA    . LYS   B 1 168 ? 28.55800 -20.43700 24.14500  1.000 47.65041 ?  167 LYS   B CA    1 
ATOM   2716 C  C     . LYS   B 1 168 ? 27.17200 -20.18000 23.54100  1.000 50.24931 ?  167 LYS   B C     1 
ATOM   2717 O  O     . LYS   B 1 168 ? 26.14700 -20.52900 24.13000  1.000 56.13008 ?  167 LYS   B O     1 
ATOM   2718 C  CB    . LYS   B 1 168 ? 28.71500 -19.62900 25.44300  1.000 46.34854 ?  167 LYS   B CB    1 
ATOM   2719 C  CG    . LYS   B 1 168 ? 30.06800 -19.73400 26.13900  1.000 49.62242 ?  167 LYS   B CG    1 
ATOM   2720 C  CD    . LYS   B 1 168 ? 30.58500 -21.16800 26.20000  1.000 51.70993 ?  167 LYS   B CD    1 
ATOM   2721 C  CE    . LYS   B 1 168 ? 31.75100 -21.30100 27.18000  1.000 48.02741 ?  167 LYS   B CE    1 
ATOM   2722 N  NZ    . LYS   B 1 168 ? 31.29100 -21.34800 28.59500  1.000 53.58253 ?  167 LYS   B NZ    1 
ATOM   2723 N  N     . VAL   C 2 3   ? 94.62700 -35.82600 35.63000  1.000 38.91787 ?  2   VAL   C N     1 
ATOM   2724 C  CA    . VAL   C 2 3   ? 93.84000 -36.09200 36.83700  1.000 42.26530 ?  2   VAL   C CA    1 
ATOM   2725 C  C     . VAL   C 2 3   ? 92.70000 -35.10600 37.00700  1.000 39.94122 ?  2   VAL   C C     1 
ATOM   2726 O  O     . VAL   C 2 3   ? 92.91600 -33.88700 37.01500  1.000 42.47245 ?  2   VAL   C O     1 
ATOM   2727 C  CB    . VAL   C 2 3   ? 94.69700 -36.06400 38.09500  1.000 42.35273 ?  2   VAL   C CB    1 
ATOM   2728 C  CG1   . VAL   C 2 3   ? 93.80200 -36.20400 39.32600  1.000 39.91027 ?  2   VAL   C CG1   1 
ATOM   2729 C  CG2   . VAL   C 2 3   ? 95.71600 -37.18500 38.05200  1.000 41.80939 ?  2   VAL   C CG2   1 
ATOM   2730 N  N     . ASN   C 2 4   ? 91.50200 -35.65000 37.22100  1.000 37.75483 ?  3   ASN   C N     1 
ATOM   2731 C  CA    . ASN   C 2 4   ? 90.27600 -34.84500 37.16300  1.000 33.91734 ?  3   ASN   C CA    1 
ATOM   2732 C  C     . ASN   C 2 4   ? 90.19500 -33.83900 38.30900  1.000 34.48913 ?  3   ASN   C C     1 
ATOM   2733 O  O     . ASN   C 2 4   ? 90.32400 -34.22100 39.47800  1.000 40.51149 ?  3   ASN   C O     1 
ATOM   2734 C  CB    . ASN   C 2 4   ? 89.05800 -35.77400 37.19200  1.000 37.05707 ?  3   ASN   C CB    1 
ATOM   2735 C  CG    . ASN   C 2 4   ? 88.87400 -36.52700 35.87900  1.000 35.55992 ?  3   ASN   C CG    1 
ATOM   2736 O  OD1   . ASN   C 2 4   ? 89.37500 -36.10500 34.82800  1.000 37.98204 ?  3   ASN   C OD1   1 
ATOM   2737 N  ND2   . ASN   C 2 4   ? 88.15900 -37.63900 35.93700  1.000 38.66842 ?  3   ASN   C ND2   1 
ATOM   2738 N  N     . PRO   C 2 5   ? 89.95300 -32.56600 38.02700  1.000 36.01957 ?  4   PRO   C N     1 
ATOM   2739 C  CA    . PRO   C 2 5   ? 89.76700 -31.59400 39.10800  1.000 34.61727 ?  4   PRO   C CA    1 
ATOM   2740 C  C     . PRO   C 2 5   ? 88.47000 -31.84000 39.88100  1.000 37.28132 ?  4   PRO   C C     1 
ATOM   2741 O  O     . PRO   C 2 5   ? 87.50600 -32.43900 39.39000  1.000 30.74388 ?  4   PRO   C O     1 
ATOM   2742 C  CB    . PRO   C 2 5   ? 89.73200 -30.24800 38.37600  1.000 34.64037 ?  4   PRO   C CB    1 
ATOM   2743 C  CG    . PRO   C 2 5   ? 89.34800 -30.58900 36.94600  1.000 36.09094 ?  4   PRO   C CG    1 
ATOM   2744 C  CD    . PRO   C 2 5   ? 89.94000 -31.94400 36.69100  1.000 33.57785 ?  4   PRO   C CD    1 
ATOM   2745 N  N     . THR   C 2 6   ? 88.47800 -31.37400 41.12900  1.000 34.74352 ?  5   THR   C N     1 
ATOM   2746 C  CA    . THR   C 2 6   ? 87.31700 -31.34400 42.01500  1.000 34.93735 ?  5   THR   C CA    1 
ATOM   2747 C  C     . THR   C 2 6   ? 87.01400 -29.88600 42.37600  1.000 32.92955 ?  5   THR   C C     1 
ATOM   2748 O  O     . THR   C 2 6   ? 87.92600 -29.09900 42.65000  1.000 31.91443 ?  5   THR   C O     1 
ATOM   2749 C  CB    . THR   C 2 6   ? 87.57600 -32.18800 43.29100  1.000 34.47724 ?  5   THR   C CB    1 
ATOM   2750 O  OG1   . THR   C 2 6   ? 87.68700 -33.58100 42.96100  1.000 40.89455 ?  5   THR   C OG1   1 
ATOM   2751 C  CG2   . THR   C 2 6   ? 86.45600 -32.02500 44.28200  1.000 38.24807 ?  5   THR   C CG2   1 
ATOM   2752 N  N     . VAL   C 2 7   ? 85.73600 -29.49600 42.36400  1.000 25.79653 ?  6   VAL   C N     1 
ATOM   2753 C  CA    . VAL   C 2 7   ? 85.36100 -28.13800 42.76100  1.000 25.97032 ?  6   VAL   C CA    1 
ATOM   2754 C  C     . VAL   C 2 7   ? 84.21200 -28.23700 43.75600  1.000 26.99237 ?  6   VAL   C C     1 
ATOM   2755 O  O     . VAL   C 2 7   ? 83.60500 -29.28500 43.92200  1.000 25.86457 ?  6   VAL   C O     1 
ATOM   2756 C  CB    . VAL   C 2 7   ? 84.97500 -27.23300 41.57200  1.000 33.18709 ?  6   VAL   C CB    1 
ATOM   2757 C  CG1   . VAL   C 2 7   ? 86.13200 -27.10300 40.57200  1.000 30.52323 ?  6   VAL   C CG1   1 
ATOM   2758 C  CG2   . VAL   C 2 7   ? 83.75400 -27.76700 40.89100  1.000 27.96750 ?  6   VAL   C CG2   1 
ATOM   2759 N  N     . PHE   C 2 8   ? 83.96000 -27.12500 44.43300  1.000 26.40646 ?  7   PHE   C N     1 
ATOM   2760 C  CA    . PHE   C 2 8   ? 82.91400 -27.12500 45.47600  1.000 27.46637 ?  7   PHE   C CA    1 
ATOM   2761 C  C     . PHE   C 2 8   ? 82.05600 -25.89300 45.38700  1.000 25.59303 ?  7   PHE   C C     1 
ATOM   2762 O  O     . PHE   C 2 8   ? 82.50900 -24.85600 44.91900  1.000 27.91125 ?  7   PHE   C O     1 
ATOM   2763 C  CB    . PHE   C 2 8   ? 83.53100 -27.14600 46.87600  1.000 29.73908 ?  7   PHE   C CB    1 
ATOM   2764 C  CG    . PHE   C 2 8   ? 84.15900 -25.83600 47.33100  1.000 31.26075 ?  7   PHE   C CG    1 
ATOM   2765 C  CD1   . PHE   C 2 8   ? 83.40400 -24.85900 47.96900  1.000 32.74247 ?  7   PHE   C CD1   1 
ATOM   2766 C  CD2   . PHE   C 2 8   ? 85.51000 -25.59000 47.12300  1.000 33.90005 ?  7   PHE   C CD2   1 
ATOM   2767 C  CE1   . PHE   C 2 8   ? 83.97700 -23.66500 48.36300  1.000 36.58137 ?  7   PHE   C CE1   1 
ATOM   2768 C  CE2   . PHE   C 2 8   ? 86.08000 -24.40100 47.53800  1.000 35.16246 ?  7   PHE   C CE2   1 
ATOM   2769 C  CZ    . PHE   C 2 8   ? 85.31400 -23.44200 48.15400  1.000 34.38514 ?  7   PHE   C CZ    1 
ATOM   2770 N  N     . PHE   C 2 9   ? 80.81500 -26.03600 45.82500  1.000 24.33857 ?  8   PHE   C N     1 
ATOM   2771 C  CA    . PHE   C 2 9   ? 79.90000 -24.88700 45.93100  1.000 23.81230 ?  8   PHE   C CA    1 
ATOM   2772 C  C     . PHE   C 2 9   ? 79.39300 -24.86600 47.36400  1.000 25.40321 ?  8   PHE   C C     1 
ATOM   2773 O  O     . PHE   C 2 9   ? 79.00800 -25.93800 47.84500  1.000 26.09928 ?  8   PHE   C O     1 
ATOM   2774 C  CB    . PHE   C 2 9   ? 78.64200 -25.04400 45.07900  1.000 24.44662 ?  8   PHE   C CB    1 
ATOM   2775 C  CG    . PHE   C 2 9   ? 78.73300 -24.86600 43.57200  1.000 24.22935 ?  8   PHE   C CG    1 
ATOM   2776 C  CD1   . PHE   C 2 9   ? 79.87600 -24.36400 42.96700  1.000 25.60080 ?  8   PHE   C CD1   1 
ATOM   2777 C  CD2   . PHE   C 2 9   ? 77.65100 -25.19200 42.76600  1.000 27.41409 ?  8   PHE   C CD2   1 
ATOM   2778 C  CE1   . PHE   C 2 9   ? 79.93200 -24.19600 41.59600  1.000 26.27738 ?  8   PHE   C CE1   1 
ATOM   2779 C  CE2   . PHE   C 2 9   ? 77.71800 -25.03300 41.39500  1.000 29.52904 ?  8   PHE   C CE2   1 
ATOM   2780 C  CZ    . PHE   C 2 9   ? 78.85500 -24.53100 40.81500  1.000 26.40425 ?  8   PHE   C CZ    1 
ATOM   2781 N  N     . ASP   C 2 10  ? 79.48500 -23.72600 48.05000  1.000 26.08103 ?  9   ASP   C N     1 
ATOM   2782 C  CA    . ASP   C 2 10  ? 78.85500 -23.57900 49.38600  1.000 27.48262 ?  9   ASP   C CA    1 
ATOM   2783 C  C     . ASP   C 2 10  ? 77.47900 -22.96800 49.12000  1.000 28.36395 ?  9   ASP   C C     1 
ATOM   2784 O  O     . ASP   C 2 10  ? 77.43200 -21.84400 48.60800  1.000 30.47173 ?  9   ASP   C O     1 
ATOM   2785 C  CB    . ASP   C 2 10  ? 79.71900 -22.79200 50.35300  1.000 24.59163 ?  9   ASP   C CB    1 
ATOM   2786 C  CG    . ASP   C 2 10  ? 80.88300 -23.56400 50.94700  1.000 34.98620 ?  9   ASP   C CG    1 
ATOM   2787 O  OD1   . ASP   C 2 10  ? 80.68800 -24.74600 51.28200  1.000 35.53571 ?  9   ASP   C OD1   1 
ATOM   2788 O  OD2   . ASP   C 2 10  ? 81.97000 -22.97100 51.06600  1.000 45.40028 -1 9   ASP   C OD2   1 
ATOM   2789 N  N     . ILE   C 2 11  ? 76.41800 -23.71400 49.41700  1.000 27.29443 ?  10  ILE   C N     1 
ATOM   2790 C  CA    . ILE   C 2 11  ? 75.04500 -23.27200 49.06900  1.000 23.64959 ?  10  ILE   C CA    1 
ATOM   2791 C  C     . ILE   C 2 11  ? 74.41200 -22.57900 50.27200  1.000 24.80740 ?  10  ILE   C C     1 
ATOM   2792 O  O     . ILE   C 2 11  ? 74.59800 -23.05000 51.38900  1.000 29.46202 ?  10  ILE   C O     1 
ATOM   2793 C  CB    . ILE   C 2 11  ? 74.20100 -24.47500 48.60500  1.000 24.36436 ?  10  ILE   C CB    1 
ATOM   2794 C  CG1   . ILE   C 2 11  ? 74.85400 -25.19800 47.43300  1.000 24.93816 ?  10  ILE   C CG1   1 
ATOM   2795 C  CG2   . ILE   C 2 11  ? 72.76300 -24.07000 48.28700  1.000 23.73647 ?  10  ILE   C CG2   1 
ATOM   2796 C  CD1   . ILE   C 2 11  ? 75.01700 -24.33500 46.20000  1.000 25.51315 ?  10  ILE   C CD1   1 
ATOM   2797 N  N     . ALA   C 2 12  ? 73.74500 -21.47000 50.01300  1.000 25.00357 ?  11  ALA   C N     1 
ATOM   2798 C  CA    . ALA   C 2 12  ? 73.00600 -20.78400 51.07000  1.000 28.23504 ?  11  ALA   C CA    1 
ATOM   2799 C  C     . ALA   C 2 12  ? 71.53400 -20.64700 50.70600  1.000 30.38855 ?  11  ALA   C C     1 
ATOM   2800 O  O     . ALA   C 2 12  ? 71.16500 -20.60600 49.52400  1.000 27.60154 ?  11  ALA   C O     1 
ATOM   2801 C  CB    . ALA   C 2 12  ? 73.61400 -19.40400 51.34400  1.000 27.57214 ?  11  ALA   C CB    1 
ATOM   2802 N  N     . VAL   C 2 13  ? 70.68300 -20.58500 51.73600  1.000 25.39987 ?  12  VAL   C N     1 
ATOM   2803 C  CA    . VAL   C 2 13  ? 69.25100 -20.42900 51.56600  1.000 27.89238 ?  12  VAL   C CA    1 
ATOM   2804 C  C     . VAL   C 2 13  ? 68.87600 -19.12800 52.24700  1.000 33.91078 ?  12  VAL   C C     1 
ATOM   2805 O  O     . VAL   C 2 13  ? 68.94400 -19.03200 53.48200  1.000 32.38491 ?  12  VAL   C O     1 
ATOM   2806 C  CB    . VAL   C 2 13  ? 68.45700 -21.61200 52.14500  1.000 31.69799 ?  12  VAL   C CB    1 
ATOM   2807 C  CG1   . VAL   C 2 13  ? 66.95800 -21.36700 52.01900  1.000 33.74739 ?  12  VAL   C CG1   1 
ATOM   2808 C  CG2   . VAL   C 2 13  ? 68.86600 -22.90900 51.45200  1.000 36.44871 ?  12  VAL   C CG2   1 
ATOM   2809 N  N     . ASP   C 2 14  ? 68.49600 -18.12500 51.44900  1.000 31.80564 ?  13  ASP   C N     1 
ATOM   2810 C  CA    . ASP   C 2 14  ? 68.16300 -16.78600 51.96700  1.000 33.20428 ?  13  ASP   C CA    1 
ATOM   2811 C  C     . ASP   C 2 14  ? 69.31800 -16.24000 52.80300  1.000 39.23228 ?  13  ASP   C C     1 
ATOM   2812 O  O     . ASP   C 2 14  ? 69.12600 -15.60500 53.84700  1.000 38.62343 ?  13  ASP   C O     1 
ATOM   2813 C  CB    . ASP   C 2 14  ? 66.85300 -16.80800 52.77100  1.000 34.57949 ?  13  ASP   C CB    1 
ATOM   2814 C  CG    . ASP   C 2 14  ? 65.60600 -16.82800 51.87800  1.000 40.90193 ?  13  ASP   C CG    1 
ATOM   2815 O  OD1   . ASP   C 2 14  ? 65.70100 -16.48100 50.66500  1.000 38.18805 ?  13  ASP   C OD1   1 
ATOM   2816 O  OD2   . ASP   C 2 14  ? 64.51500 -17.17900 52.39300  1.000 46.55554 -1 13  ASP   C OD2   1 
ATOM   2817 N  N     . GLY   C 2 15  ? 70.54100 -16.52400 52.35300  1.000 32.50357 ?  14  GLY   C N     1 
ATOM   2818 C  CA    . GLY   C 2 15  ? 71.74400 -16.06600 53.01800  1.000 32.86113 ?  14  GLY   C CA    1 
ATOM   2819 C  C     . GLY   C 2 15  ? 72.26900 -16.96200 54.12000  1.000 37.41246 ?  14  GLY   C C     1 
ATOM   2820 O  O     . GLY   C 2 15  ? 73.40300 -16.75900 54.57200  1.000 43.50118 ?  14  GLY   C O     1 
ATOM   2821 N  N     . GLU   C 2 16  ? 71.50200 -17.91000 54.56300  1.000 33.54127 ?  15  GLU   C N     1 
ATOM   2822 C  CA    . GLU   C 2 16  ? 71.86100 -18.85800 55.61300  1.000 39.39502 ?  15  GLU   C CA    1 
ATOM   2823 C  C     . GLU   C 2 16  ? 72.55800 -20.07000 55.01500  1.000 39.39232 ?  15  GLU   C C     1 
ATOM   2824 O  O     . GLU   C 2 16  ? 72.05100 -20.64700 54.04800  1.000 35.69842 ?  15  GLU   C O     1 
ATOM   2825 C  CB    . GLU   C 2 16  ? 70.62400 -19.31300 56.36800  1.000 39.16934 ?  15  GLU   C CB    1 
ATOM   2826 C  CG    . GLU   C 2 16  ? 69.96100 -18.18500 57.16700  1.000 43.93276 ?  15  GLU   C CG    1 
ATOM   2827 C  CD    . GLU   C 2 16  ? 70.96900 -17.39400 57.98500  1.000 46.62264 ?  15  GLU   C CD    1 
ATOM   2828 O  OE1   . GLU   C 2 16  ? 71.88900 -18.01000 58.58700  1.000 53.74438 ?  15  GLU   C OE1   1 
ATOM   2829 O  OE2   . GLU   C 2 16  ? 70.85400 -16.14500 58.01600  1.000 55.73500 -1 15  GLU   C OE2   1 
ATOM   2830 N  N     . PRO   C 2 17  ? 73.69100 -20.49400 55.56600  1.000 34.96658 ?  16  PRO   C N     1 
ATOM   2831 C  CA    . PRO   C 2 17  ? 74.41400 -21.63300 54.99000  1.000 32.32203 ?  16  PRO   C CA    1 
ATOM   2832 C  C     . PRO   C 2 17  ? 73.61800 -22.92700 55.04400  1.000 38.88618 ?  16  PRO   C C     1 
ATOM   2833 O  O     . PRO   C 2 17  ? 73.06400 -23.31100 56.08200  1.000 37.86850 ?  16  PRO   C O     1 
ATOM   2834 C  CB    . PRO   C 2 17  ? 75.68600 -21.71400 55.83900  1.000 36.87387 ?  16  PRO   C CB    1 
ATOM   2835 C  CG    . PRO   C 2 17  ? 75.88000 -20.31600 56.30300  1.000 37.63528 ?  16  PRO   C CG    1 
ATOM   2836 C  CD    . PRO   C 2 17  ? 74.51300 -19.76600 56.55000  1.000 39.85768 ?  16  PRO   C CD    1 
ATOM   2837 N  N     . LEU   C 2 18  ? 73.55500 -23.59400 53.89700  1.000 30.02066 ?  17  LEU   C N     1 
ATOM   2838 C  CA    . LEU   C 2 18  ? 72.90500 -24.89200 53.79800  1.000 30.42397 ?  17  LEU   C CA    1 
ATOM   2839 C  C     . LEU   C 2 18  ? 73.91800 -26.02800 53.83400  1.000 32.74774 ?  17  LEU   C C     1 
ATOM   2840 O  O     . LEU   C 2 18  ? 73.83600 -26.90000 54.69700  1.000 34.74798 ?  17  LEU   C O     1 
ATOM   2841 C  CB    . LEU   C 2 18  ? 72.05400 -24.96700 52.52200  1.000 28.30057 ?  17  LEU   C CB    1 
ATOM   2842 C  CG    . LEU   C 2 18  ? 71.25600 -26.26100 52.33200  1.000 33.02957 ?  17  LEU   C CG    1 
ATOM   2843 C  CD1   . LEU   C 2 18  ? 70.18200 -26.42000 53.42000  1.000 33.84597 ?  17  LEU   C CD1   1 
ATOM   2844 C  CD2   . LEU   C 2 18  ? 70.65200 -26.33100 50.90700  1.000 30.66040 ?  17  LEU   C CD2   1 
ATOM   2845 N  N     . GLY   C 2 19  ? 74.89700 -25.98800 52.94300  1.000 29.30036 ?  18  GLY   C N     1 
ATOM   2846 C  CA    . GLY   C 2 19  ? 75.89000 -27.06400 52.91300  1.000 28.09834 ?  18  GLY   C CA    1 
ATOM   2847 C  C     . GLY   C 2 19  ? 76.83500 -26.97900 51.73700  1.000 26.40988 ?  18  GLY   C C     1 
ATOM   2848 O  O     . GLY   C 2 19  ? 76.68300 -26.08100 50.90300  1.000 27.54337 ?  18  GLY   C O     1 
ATOM   2849 N  N     . ARG   C 2 20  ? 77.76200 -27.92800 51.67900  1.000 29.39378 ?  19  ARG   C N     1 
ATOM   2850 C  CA    . ARG   C 2 20  ? 78.76700 -27.92300 50.59700  1.000 27.09739 ?  19  ARG   C CA    1 
ATOM   2851 C  C     . ARG   C 2 20  ? 78.51700 -29.06700 49.60500  1.000 26.82732 ?  19  ARG   C C     1 
ATOM   2852 O  O     . ARG   C 2 20  ? 78.32000 -30.20900 50.03800  1.000 29.06682 ?  19  ARG   C O     1 
ATOM   2853 C  CB    . ARG   C 2 20  ? 80.21500 -28.03300 51.08500  1.000 27.44046 ?  19  ARG   C CB    1 
ATOM   2854 C  CG    . ARG   C 2 20  ? 81.27200 -28.09600 49.99200  1.000 25.82746 ?  19  ARG   C CG    1 
ATOM   2855 C  CD    . ARG   C 2 20  ? 82.68400 -27.89800 50.52400  1.000 30.14471 ?  19  ARG   C CD    1 
ATOM   2856 N  NE    . ARG   C 2 20  ? 82.91200 -26.54600 51.04400  1.000 33.54666 ?  19  ARG   C NE    1 
ATOM   2857 C  CZ    . ARG   C 2 20  ? 84.10000 -25.97000 51.17000  1.000 36.04404 ?  19  ARG   C CZ    1 
ATOM   2858 N  NH1   . ARG   C 2 20  ? 85.19800 -26.66200 50.93400  1.000 38.01550 ?  19  ARG   C NH1   1 
ATOM   2859 N  NH2   . ARG   C 2 20  ? 84.18800 -24.70300 51.52400  1.000 35.93101 ?  19  ARG   C NH2   1 
ATOM   2860 N  N     . VAL   C 2 21  ? 78.50100 -28.72900 48.32500  1.000 24.31909 ?  20  VAL   C N     1 
ATOM   2861 C  CA    . VAL   C 2 21  ? 78.40900 -29.76800 47.27400  1.000 23.66033 ?  20  VAL   C CA    1 
ATOM   2862 C  C     . VAL   C 2 21  ? 79.75100 -29.74800 46.54800  1.000 22.57655 ?  20  VAL   C C     1 
ATOM   2863 O  O     . VAL   C 2 21  ? 80.18800 -28.66300 46.18800  1.000 27.04679 ?  20  VAL   C O     1 
ATOM   2864 C  CB    . VAL   C 2 21  ? 77.27400 -29.49600 46.27500  1.000 21.89249 ?  20  VAL   C CB    1 
ATOM   2865 C  CG1   . VAL   C 2 21  ? 77.09500 -30.65600 45.30700  1.000 25.45427 ?  20  VAL   C CG1   1 
ATOM   2866 C  CG2   . VAL   C 2 21  ? 75.96500 -29.18000 46.98200  1.000 25.28895 ?  20  VAL   C CG2   1 
ATOM   2867 N  N     . SER   C 2 22  ? 80.37500 -30.90700 46.40100  1.000 22.41280 ?  21  SER   C N     1 
ATOM   2868 C  CA    . SER   C 2 22  ? 81.58900 -30.98000 45.59300  1.000 21.70230 ?  21  SER   C CA    1 
ATOM   2869 C  C     . SER   C 2 22  ? 81.35900 -31.86700 44.38100  1.000 23.43049 ?  21  SER   C C     1 
ATOM   2870 O  O     . SER   C 2 22  ? 80.56700 -32.80400 44.43100  1.000 24.77767 ?  21  SER   C O     1 
ATOM   2871 C  CB    . SER   C 2 22  ? 82.78300 -31.48900 46.42600  1.000 29.59102 ?  21  SER   C CB    1 
ATOM   2872 O  OG    . SER   C 2 22  ? 82.58300 -32.83200 46.81000  1.000 29.44264 ?  21  SER   C OG    1 
ATOM   2873 N  N     . PHE   C 2 23  ? 82.11800 -31.56000 43.33400  1.000 23.43313 ?  22  PHE   C N     1 
ATOM   2874 C  CA    . PHE   C 2 23  ? 81.92900 -32.25200 42.05300  1.000 23.96817 ?  22  PHE   C CA    1 
ATOM   2875 C  C     . PHE   C 2 23  ? 83.23100 -32.70500 41.45300  1.000 25.51025 ?  22  PHE   C C     1 
ATOM   2876 O  O     . PHE   C 2 23  ? 84.22900 -32.01100 41.57600  1.000 27.91993 ?  22  PHE   C O     1 
ATOM   2877 C  CB    . PHE   C 2 23  ? 81.40300 -31.22100 41.05400  1.000 21.82200 ?  22  PHE   C CB    1 
ATOM   2878 C  CG    . PHE   C 2 23  ? 80.15300 -30.45500 41.45300  1.000 22.31935 ?  22  PHE   C CG    1 
ATOM   2879 C  CD1   . PHE   C 2 23  ? 78.89200 -30.97100 41.19500  1.000 23.15698 ?  22  PHE   C CD1   1 
ATOM   2880 C  CD2   . PHE   C 2 23  ? 80.24500 -29.21300 42.06200  1.000 24.46681 ?  22  PHE   C CD2   1 
ATOM   2881 C  CE1   . PHE   C 2 23  ? 77.75800 -30.26800 41.55400  1.000 22.51628 ?  22  PHE   C CE1   1 
ATOM   2882 C  CE2   . PHE   C 2 23  ? 79.10800 -28.51600 42.42300  1.000 24.38694 ?  22  PHE   C CE2   1 
ATOM   2883 C  CZ    . PHE   C 2 23  ? 77.86900 -29.04200 42.16400  1.000 26.22960 ?  22  PHE   C CZ    1 
ATOM   2884 N  N     . GLU   C 2 24  ? 83.21500 -33.89200 40.87900  1.000 25.03186 ?  23  GLU   C N     1 
ATOM   2885 C  CA    . GLU   C 2 24  ? 84.32600 -34.34200 40.05500  1.000 23.97818 ?  23  GLU   C CA    1 
ATOM   2886 C  C     . GLU   C 2 24  ? 84.02400 -33.90600 38.62000  1.000 27.33202 ?  23  GLU   C C     1 
ATOM   2887 O  O     . GLU   C 2 24  ? 82.89200 -34.05200 38.14200  1.000 24.49761 ?  23  GLU   C O     1 
ATOM   2888 C  CB    . GLU   C 2 24  ? 84.50400 -35.85800 40.15100  1.000 25.31971 ?  23  GLU   C CB    1 
ATOM   2889 C  CG    . GLU   C 2 24  ? 85.52400 -36.31500 39.09100  1.000 32.56981 ?  23  GLU   C CG    1 
ATOM   2890 C  CD    . GLU   C 2 24  ? 85.83900 -37.80200 39.09900  1.000 41.10846 ?  23  GLU   C CD    1 
ATOM   2891 O  OE1   . GLU   C 2 24  ? 85.13400 -38.57900 39.78700  1.000 39.77273 ?  23  GLU   C OE1   1 
ATOM   2892 O  OE2   . GLU   C 2 24  ? 86.81200 -38.18300 38.40500  1.000 42.05553 -1 23  GLU   C OE2   1 
ATOM   2893 N  N     . LEU   C 2 25  ? 85.00500 -33.30800 37.95800  1.000 27.18217 ?  24  LEU   C N     1 
ATOM   2894 C  CA    . LEU   C 2 25  ? 84.86300 -32.85600 36.58300  1.000 26.73770 ?  24  LEU   C CA    1 
ATOM   2895 C  C     . LEU   C 2 25  ? 85.68000 -33.79200 35.69800  1.000 27.63824 ?  24  LEU   C C     1 
ATOM   2896 O  O     . LEU   C 2 25  ? 86.87100 -33.98200 35.93500  1.000 28.77010 ?  24  LEU   C O     1 
ATOM   2897 C  CB    . LEU   C 2 25  ? 85.33900 -31.41300 36.43500  1.000 23.82133 ?  24  LEU   C CB    1 
ATOM   2898 C  CG    . LEU   C 2 25  ? 84.80900 -30.44300 37.48500  1.000 25.08582 ?  24  LEU   C CG    1 
ATOM   2899 C  CD1   . LEU   C 2 25  ? 85.34600 -29.03900 37.22300  1.000 25.55632 ?  24  LEU   C CD1   1 
ATOM   2900 C  CD2   . LEU   C 2 25  ? 83.24700 -30.46900 37.46900  1.000 23.02908 ?  24  LEU   C CD2   1 
ATOM   2901 N  N     . PHE   C 2 26  ? 85.04200 -34.40100 34.70200  1.000 28.74348 ?  25  PHE   C N     1 
ATOM   2902 C  CA    . PHE   C 2 26  ? 85.72000 -35.41300 33.90300  1.000 30.25085 ?  25  PHE   C CA    1 
ATOM   2903 C  C     . PHE   C 2 26  ? 86.51600 -34.73000 32.78100  1.000 30.06700 ?  25  PHE   C C     1 
ATOM   2904 O  O     . PHE   C 2 26  ? 86.20300 -34.80200 31.58800  1.000 28.19702 ?  25  PHE   C O     1 
ATOM   2905 C  CB    . PHE   C 2 26  ? 84.72300 -36.44200 33.38700  1.000 33.26640 ?  25  PHE   C CB    1 
ATOM   2906 C  CG    . PHE   C 2 26  ? 83.86400 -37.04000 34.46500  1.000 32.95138 ?  25  PHE   C CG    1 
ATOM   2907 C  CD1   . PHE   C 2 26  ? 84.43200 -37.77100 35.50300  1.000 36.18330 ?  25  PHE   C CD1   1 
ATOM   2908 C  CD2   . PHE   C 2 26  ? 82.48600 -36.87900 34.42900  1.000 30.10595 ?  25  PHE   C CD2   1 
ATOM   2909 C  CE1   . PHE   C 2 26  ? 83.60900 -38.31300 36.50700  1.000 37.03742 ?  25  PHE   C CE1   1 
ATOM   2910 C  CE2   . PHE   C 2 26  ? 81.66500 -37.42300 35.42100  1.000 30.28920 ?  25  PHE   C CE2   1 
ATOM   2911 C  CZ    . PHE   C 2 26  ? 82.24100 -38.13600 36.46000  1.000 37.70489 ?  25  PHE   C CZ    1 
ATOM   2912 N  N     . ALA   C 2 27  ? 87.57900 -34.03900 33.19800  1.000 30.31673 ?  26  ALA   C N     1 
ATOM   2913 C  CA    . ALA   C 2 27  ? 88.51600 -33.45300 32.23800  1.000 34.66947 ?  26  ALA   C CA    1 
ATOM   2914 C  C     . ALA   C 2 27  ? 89.20500 -34.51700 31.37200  1.000 30.16331 ?  26  ALA   C C     1 
ATOM   2915 O  O     . ALA   C 2 27  ? 89.64100 -34.20500 30.25900  1.000 33.89042 ?  26  ALA   C O     1 
ATOM   2916 C  CB    . ALA   C 2 27  ? 89.55700 -32.60700 32.97200  1.000 35.49159 ?  26  ALA   C CB    1 
ATOM   2917 N  N     . ASP   C 2 28  ? 89.25300 -35.77100 31.82500  1.000 33.29772 ?  27  ASP   C N     1 
ATOM   2918 C  CA    . ASP   C 2 28  ? 89.80500 -36.83000 30.98200  1.000 36.40522 ?  27  ASP   C CA    1 
ATOM   2919 C  C     . ASP   C 2 28  ? 88.91600 -37.20000 29.79500  1.000 37.63875 ?  27  ASP   C C     1 
ATOM   2920 O  O     . ASP   C 2 28  ? 89.38300 -37.91100 28.89900  1.000 40.71568 ?  27  ASP   C O     1 
ATOM   2921 C  CB    . ASP   C 2 28  ? 90.10400 -38.09200 31.80800  1.000 37.12536 ?  27  ASP   C CB    1 
ATOM   2922 C  CG    . ASP   C 2 28  ? 88.92000 -38.59900 32.60700  1.000 40.66703 ?  27  ASP   C CG    1 
ATOM   2923 O  OD1   . ASP   C 2 28  ? 87.87200 -37.91900 32.73600  1.000 39.40863 ?  27  ASP   C OD1   1 
ATOM   2924 O  OD2   . ASP   C 2 28  ? 89.04300 -39.72500 33.14200  1.000 54.43800 -1 27  ASP   C OD2   1 
ATOM   2925 N  N     . LYS   C 2 29  ? 87.66000 -36.75300 29.76400  1.000 34.82671 ?  28  LYS   C N     1 
ATOM   2926 C  CA    . LYS   C 2 29  ? 86.74000 -37.00600 28.66900  1.000 33.42848 ?  28  LYS   C CA    1 
ATOM   2927 C  C     . LYS   C 2 29  ? 86.21300 -35.73100 28.02700  1.000 33.03629 ?  28  LYS   C C     1 
ATOM   2928 O  O     . LYS   C 2 29  ? 85.96500 -35.71500 26.81900  1.000 30.87577 ?  28  LYS   C O     1 
ATOM   2929 C  CB    . LYS   C 2 29  ? 85.56000 -37.87400 29.15100  1.000 38.03139 ?  28  LYS   C CB    1 
ATOM   2930 C  CG    . LYS   C 2 29  ? 85.96900 -39.33300 29.40400  1.000 39.04934 ?  28  LYS   C CG    1 
ATOM   2931 C  CD    . LYS   C 2 29  ? 84.75000 -40.22500 29.57200  1.000 39.35920 ?  28  LYS   C CD    1 
ATOM   2932 C  CE    . LYS   C 2 29  ? 85.13300 -41.67400 29.87200  1.000 48.08795 ?  28  LYS   C CE    1 
ATOM   2933 N  NZ    . LYS   C 2 29  ? 85.89200 -41.80400 31.15200  1.000 49.92585 ?  28  LYS   C NZ    1 
ATOM   2934 N  N     . VAL   C 2 30  ? 86.04000 -34.66000 28.79000  1.000 29.37057 ?  29  VAL   C N     1 
ATOM   2935 C  CA    . VAL   C 2 30  ? 85.56400 -33.39600 28.23100  1.000 29.61156 ?  29  VAL   C CA    1 
ATOM   2936 C  C     . VAL   C 2 30  ? 86.41500 -32.26100 28.77800  1.000 32.05206 ?  29  VAL   C C     1 
ATOM   2937 O  O     . VAL   C 2 30  ? 85.92100 -31.41100 29.53600  1.000 28.05492 ?  29  VAL   C O     1 
ATOM   2938 C  CB    . VAL   C 2 30  ? 84.06900 -33.16400 28.50500  1.000 30.81483 ?  29  VAL   C CB    1 
ATOM   2939 C  CG1   . VAL   C 2 30  ? 83.25700 -33.89300 27.46200  1.000 29.66380 ?  29  VAL   C CG1   1 
ATOM   2940 C  CG2   . VAL   C 2 30  ? 83.70200 -33.61000 29.88400  1.000 31.76763 ?  29  VAL   C CG2   1 
ATOM   2941 N  N     . PRO   C 2 31  ? 87.68600 -32.18900 28.36400  1.000 30.94135 ?  30  PRO   C N     1 
ATOM   2942 C  CA    . PRO   C 2 31  ? 88.60700 -31.20400 28.95800  1.000 31.76195 ?  30  PRO   C CA    1 
ATOM   2943 C  C     . PRO   C 2 31  ? 88.12900 -29.78300 28.80700  1.000 31.09423 ?  30  PRO   C C     1 
ATOM   2944 O  O     . PRO   C 2 31  ? 88.23400 -28.98800 29.75300  1.000 29.24003 ?  30  PRO   C O     1 
ATOM   2945 C  CB    . PRO   C 2 31  ? 89.93600 -31.44200 28.18800  1.000 29.33696 ?  30  PRO   C CB    1 
ATOM   2946 C  CG    . PRO   C 2 31  ? 89.51200 -32.16100 26.90700  1.000 31.60874 ?  30  PRO   C CG    1 
ATOM   2947 C  CD    . PRO   C 2 31  ? 88.32300 -33.02500 27.33100  1.000 29.47948 ?  30  PRO   C CD    1 
ATOM   2948 N  N     . LYS   C 2 32  ? 87.60100 -29.43500 27.63300  1.000 28.94079 ?  31  LYS   C N     1 
ATOM   2949 C  CA    . LYS   C 2 32  ? 87.25000 -28.04700 27.38400  1.000 31.67799 ?  31  LYS   C CA    1 
ATOM   2950 C  C     . LYS   C 2 32  ? 86.04500 -27.63400 28.21400  1.000 32.59548 ?  31  LYS   C C     1 
ATOM   2951 O  O     . LYS   C 2 32  ? 86.00200 -26.51200 28.73900  1.000 28.07636 ?  31  LYS   C O     1 
ATOM   2952 C  CB    . LYS   C 2 32  ? 86.99400 -27.82800 25.89200  1.000 38.93422 ?  31  LYS   C CB    1 
ATOM   2953 C  CG    . LYS   C 2 32  ? 86.63200 -26.39000 25.56400  1.000 39.91531 ?  31  LYS   C CG    1 
ATOM   2954 C  CD    . LYS   C 2 32  ? 86.71400 -26.06100 24.06400  1.000 43.74514 ?  31  LYS   C CD    1 
ATOM   2955 C  CE    . LYS   C 2 32  ? 86.46400 -24.55000 23.84700  1.000 42.22010 ?  31  LYS   C CE    1 
ATOM   2956 N  NZ    . LYS   C 2 32  ? 86.30400 -24.14300 22.41400  1.000 47.71646 ?  31  LYS   C NZ    1 
ATOM   2957 N  N     . THR   C 2 33  ? 85.07600 -28.54800 28.38800  1.000 26.90486 ?  32  THR   C N     1 
ATOM   2958 C  CA    . THR   C 2 33  ? 83.89100 -28.22200 29.16800  1.000 29.45781 ?  32  THR   C CA    1 
ATOM   2959 C  C     . THR   C 2 33  ? 84.20100 -28.26100 30.65600  1.000 25.59884 ?  32  THR   C C     1 
ATOM   2960 O  O     . THR   C 2 33  ? 83.70700 -27.42300 31.43500  1.000 25.00158 ?  32  THR   C O     1 
ATOM   2961 C  CB    . THR   C 2 33  ? 82.76000 -29.19100 28.81000  1.000 28.86074 ?  32  THR   C CB    1 
ATOM   2962 O  OG1   . THR   C 2 33  ? 82.55100 -29.18900 27.37000  1.000 25.82495 ?  32  THR   C OG1   1 
ATOM   2963 C  CG2   . THR   C 2 33  ? 81.49300 -28.79300 29.52200  1.000 27.24816 ?  32  THR   C CG2   1 
ATOM   2964 N  N     . ALA   C 2 34  ? 85.01000 -29.23600 31.05800  1.000 25.87143 ?  33  ALA   C N     1 
ATOM   2965 C  CA    . ALA   C 2 34  ? 85.44200 -29.29900 32.44800  1.000 27.75893 ?  33  ALA   C CA    1 
ATOM   2966 C  C     . ALA   C 2 34  ? 86.23600 -28.06000 32.82500  1.000 30.40773 ?  33  ALA   C C     1 
ATOM   2967 O  O     . ALA   C 2 34  ? 86.01000 -27.47200 33.88600  1.000 27.69326 ?  33  ALA   C O     1 
ATOM   2968 C  CB    . ALA   C 2 34  ? 86.26800 -30.55900 32.68200  1.000 28.25924 ?  33  ALA   C CB    1 
ATOM   2969 N  N     . GLU   C 2 35  ? 87.15600 -27.63200 31.95700  1.000 31.01210 ?  34  GLU   C N     1 
ATOM   2970 C  CA    . GLU   C 2 35  ? 87.95000 -26.44400 32.26800  1.000 31.21044 ?  34  GLU   C CA    1 
ATOM   2971 C  C     . GLU   C 2 35  ? 87.08400 -25.19500 32.43100  1.000 30.38216 ?  34  GLU   C C     1 
ATOM   2972 O  O     . GLU   C 2 35  ? 87.32900 -24.37300 33.32400  1.000 31.23626 ?  34  GLU   C O     1 
ATOM   2973 C  CB    . GLU   C 2 35  ? 89.00500 -26.23100 31.18100  1.000 30.64853 ?  34  GLU   C CB    1 
ATOM   2974 C  CG    . GLU   C 2 35  ? 89.75700 -24.92100 31.34300  1.000 36.46808 ?  34  GLU   C CG    1 
ATOM   2975 C  CD    . GLU   C 2 35  ? 90.58000 -24.84100 32.64300  1.000 38.60325 ?  34  GLU   C CD    1 
ATOM   2976 O  OE1   . GLU   C 2 35  ? 90.79800 -25.87600 33.32500  1.000 43.94849 ?  34  GLU   C OE1   1 
ATOM   2977 O  OE2   . GLU   C 2 35  ? 91.00400 -23.71800 32.98900  1.000 49.39184 -1 34  GLU   C OE2   1 
ATOM   2978 N  N     . ASN   C 2 36  ? 86.08100 -25.01800 31.56900  1.000 26.91512 ?  35  ASN   C N     1 
ATOM   2979 C  CA    . ASN   C 2 36  ? 85.18000 -23.88200 31.70100  1.000 27.54623 ?  35  ASN   C CA    1 
ATOM   2980 C  C     . ASN   C 2 36  ? 84.56500 -23.83100 33.09000  1.000 27.82603 ?  35  ASN   C C     1 
ATOM   2981 O  O     . ASN   C 2 36  ? 84.52600 -22.77800 33.73400  1.000 27.56517 ?  35  ASN   C O     1 
ATOM   2982 C  CB    . ASN   C 2 36  ? 84.05900 -23.97300 30.67500  1.000 30.07440 ?  35  ASN   C CB    1 
ATOM   2983 C  CG    . ASN   C 2 36  ? 83.12400 -22.80600 30.76100  1.000 31.31820 ?  35  ASN   C CG    1 
ATOM   2984 O  OD1   . ASN   C 2 36  ? 83.56500 -21.66400 30.73700  1.000 32.27790 ?  35  ASN   C OD1   1 
ATOM   2985 N  ND2   . ASN   C 2 36  ? 81.81800 -23.07400 30.88000  1.000 26.33898 ?  35  ASN   C ND2   1 
ATOM   2986 N  N     . PHE   C 2 37  ? 84.04800 -24.95900 33.55600  1.000 27.95504 ?  36  PHE   C N     1 
ATOM   2987 C  CA    . PHE   C 2 37  ? 83.34600 -24.96800 34.86600  1.000 26.75838 ?  36  PHE   C CA    1 
ATOM   2988 C  C     . PHE   C 2 37  ? 84.37300 -24.77100 35.97200  1.000 32.30484 ?  36  PHE   C C     1 
ATOM   2989 O  O     . PHE   C 2 37  ? 84.10400 -24.06300 36.94200  1.000 27.99762 ?  36  PHE   C O     1 
ATOM   2990 C  CB    . PHE   C 2 37  ? 82.58800 -26.28600 35.03400  1.000 28.22908 ?  36  PHE   C CB    1 
ATOM   2991 C  CG    . PHE   C 2 37  ? 81.60700 -26.35800 36.19200  1.000 23.22434 ?  36  PHE   C CG    1 
ATOM   2992 C  CD1   . PHE   C 2 37  ? 80.28700 -25.96400 36.02700  1.000 24.23653 ?  36  PHE   C CD1   1 
ATOM   2993 C  CD2   . PHE   C 2 37  ? 82.00300 -26.83900 37.43100  1.000 23.05039 ?  36  PHE   C CD2   1 
ATOM   2994 C  CE1   . PHE   C 2 37  ? 79.39200 -26.04500 37.07900  1.000 24.58882 ?  36  PHE   C CE1   1 
ATOM   2995 C  CE2   . PHE   C 2 37  ? 81.10300 -26.91300 38.47700  1.000 22.77311 ?  36  PHE   C CE2   1 
ATOM   2996 C  CZ    . PHE   C 2 37  ? 79.80100 -26.52000 38.29600  1.000 25.58409 ?  36  PHE   C CZ    1 
ATOM   2997 N  N     . ARG   C 2 38  ? 85.53400 -25.41700 35.80800  1.000 31.55759 ?  37  ARG   C N     1 
ATOM   2998 C  CA    . ARG   C 2 38  ? 86.58000 -25.26400 36.81200  1.000 30.17676 ?  37  ARG   C CA    1 
ATOM   2999 C  C     . ARG   C 2 38  ? 86.92700 -23.79300 37.00700  1.000 35.32288 ?  37  ARG   C C     1 
ATOM   3000 O  O     . ARG   C 2 38  ? 86.91300 -23.28400 38.13200  1.000 30.75598 ?  37  ARG   C O     1 
ATOM   3001 C  CB    . ARG   C 2 38  ? 87.82900 -26.04900 36.40700  1.000 28.27736 ?  37  ARG   C CB    1 
ATOM   3002 C  CG    . ARG   C 2 38  ? 88.83500 -26.21800 37.55300  1.000 32.70179 ?  37  ARG   C CG    1 
ATOM   3003 C  CD    . ARG   C 2 38  ? 90.27100 -26.49600 37.03600  1.000 32.60127 ?  37  ARG   C CD    1 
ATOM   3004 N  NE    . ARG   C 2 38  ? 90.73800 -25.42500 36.16000  1.000 37.57145 ?  37  ARG   C NE    1 
ATOM   3005 C  CZ    . ARG   C 2 38  ? 91.12600 -24.23500 36.59600  1.000 40.24668 ?  37  ARG   C CZ    1 
ATOM   3006 N  NH1   . ARG   C 2 38  ? 91.26300 -23.99000 37.88800  1.000 38.58439 ?  37  ARG   C NH1   1 
ATOM   3007 N  NH2   . ARG   C 2 38  ? 91.37700 -23.26500 35.71500  1.000 45.10254 ?  37  ARG   C NH2   1 
ATOM   3008 N  N     . ALA   C 2 39  ? 87.21100 -23.08900 35.91000  1.000 30.52036 ?  38  ALA   C N     1 
ATOM   3009 C  CA    . ALA   C 2 39  ? 87.62200 -21.69100 36.00500  1.000 38.68360 ?  38  ALA   C CA    1 
ATOM   3010 C  C     . ALA   C 2 39  ? 86.50400 -20.79100 36.53100  1.000 35.65635 ?  38  ALA   C C     1 
ATOM   3011 O  O     . ALA   C 2 39  ? 86.77100 -19.85700 37.29700  1.000 38.91334 ?  38  ALA   C O     1 
ATOM   3012 C  CB    . ALA   C 2 39  ? 88.11100 -21.19900 34.64400  1.000 39.21406 ?  38  ALA   C CB    1 
ATOM   3013 N  N     . LEU   C 2 40  ? 85.24200 -21.03300 36.12900  1.000 29.80780 ?  39  LEU   C N     1 
ATOM   3014 C  CA    . LEU   C 2 40  ? 84.13200 -20.21600 36.63100  1.000 29.72177 ?  39  LEU   C CA    1 
ATOM   3015 C  C     . LEU   C 2 40  ? 83.91200 -20.44100 38.12600  1.000 32.97179 ?  39  LEU   C C     1 
ATOM   3016 O  O     . LEU   C 2 40  ? 83.42900 -19.54300 38.83000  1.000 32.89262 ?  39  LEU   C O     1 
ATOM   3017 C  CB    . LEU   C 2 40  ? 82.84600 -20.52600 35.85300  1.000 31.12790 ?  39  LEU   C CB    1 
ATOM   3018 C  CG    . LEU   C 2 40  ? 82.84100 -20.09500 34.37600  1.000 33.03861 ?  39  LEU   C CG    1 
ATOM   3019 C  CD1   . LEU   C 2 40  ? 81.62900 -20.64600 33.62900  1.000 29.38744 ?  39  LEU   C CD1   1 
ATOM   3020 C  CD2   . LEU   C 2 40  ? 82.89100 -18.58500 34.24900  1.000 37.47674 ?  39  LEU   C CD2   1 
ATOM   3021 N  N     . SER   C 2 41  ? 84.28700 -21.62300 38.60700  1.000 33.36984 ?  40  SER   C N     1 
ATOM   3022 C  CA    . SER   C 2 41  ? 84.12300 -21.95700 40.03900  1.000 29.66496 ?  40  SER   C CA    1 
ATOM   3023 C  C     . SER   C 2 41  ? 85.23500 -21.30900 40.88600  1.000 36.45380 ?  40  SER   C C     1 
ATOM   3024 O  O     . SER   C 2 41  ? 84.94700 -20.95800 42.03200  1.000 33.06508 ?  40  SER   C O     1 
ATOM   3025 C  CB    . SER   C 2 41  ? 84.03700 -23.45300 40.22900  1.000 29.26016 ?  40  SER   C CB    1 
ATOM   3026 O  OG    . SER   C 2 41  ? 83.03400 -24.02300 39.40500  1.000 30.32879 ?  40  SER   C OG    1 
ATOM   3027 N  N     . THR   C 2 42  ? 86.44600 -21.12700 40.34200  1.000 34.49098 ?  41  THR   C N     1 
ATOM   3028 C  CA    . THR   C 2 42  ? 87.47900 -20.42600 41.11300  1.000 39.96124 ?  41  THR   C CA    1 
ATOM   3029 C  C     . THR   C 2 42  ? 87.37500 -18.90900 40.98300  1.000 40.83740 ?  41  THR   C C     1 
ATOM   3030 O  O     . THR   C 2 42  ? 87.82700 -18.18500 41.87700  1.000 46.81052 ?  41  THR   C O     1 
ATOM   3031 C  CB    . THR   C 2 42  ? 88.89200 -20.83600 40.69100  1.000 39.72749 ?  41  THR   C CB    1 
ATOM   3032 O  OG1   . THR   C 2 42  ? 89.11800 -20.43400 39.33400  1.000 43.04239 ?  41  THR   C OG1   1 
ATOM   3033 C  CG2   . THR   C 2 42  ? 89.14400 -22.33900 40.88000  1.000 38.78658 ?  41  THR   C CG2   1 
ATOM   3034 N  N     . GLY   C 2 43  ? 86.81900 -18.41100 39.88500  1.000 39.10775 ?  42  GLY   C N     1 
ATOM   3035 C  CA    . GLY   C 2 43  ? 86.77200 -16.98200 39.63900  1.000 41.22726 ?  42  GLY   C CA    1 
ATOM   3036 C  C     . GLY   C 2 43  ? 88.02800 -16.39400 39.02300  1.000 39.13098 ?  42  GLY   C C     1 
ATOM   3037 O  O     . GLY   C 2 43  ? 88.10300 -15.17400 38.85200  1.000 43.14357 ?  42  GLY   C O     1 
ATOM   3038 N  N     . GLU   C 2 44  ? 88.99300 -17.22700 38.65100  1.000 43.32760 ?  43  GLU   C N     1 
ATOM   3039 C  CA    . GLU   C 2 44  ? 90.31300 -16.77300 38.23800  1.000 42.97246 ?  43  GLU   C CA    1 
ATOM   3040 C  C     . GLU   C 2 44  ? 90.31800 -15.95000 36.95300  1.000 43.44115 ?  43  GLU   C C     1 
ATOM   3041 O  O     . GLU   C 2 44  ? 91.36400 -15.39500 36.61300  1.000 49.79858 ?  43  GLU   C O     1 
ATOM   3042 C  CB    . GLU   C 2 44  ? 91.22100 -17.98500 38.08600  1.000 45.88474 ?  43  GLU   C CB    1 
ATOM   3043 C  CG    . GLU   C 2 44  ? 90.71600 -18.96800 37.04300  1.000 43.75797 ?  43  GLU   C CG    1 
ATOM   3044 C  CD    . GLU   C 2 44  ? 91.55300 -20.22100 36.99100  1.000 50.10901 ?  43  GLU   C CD    1 
ATOM   3045 O  OE1   . GLU   C 2 44  ? 91.58600 -20.94900 38.00400  1.000 51.91771 ?  43  GLU   C OE1   1 
ATOM   3046 O  OE2   . GLU   C 2 44  ? 92.18800 -20.47000 35.94400  1.000 51.57295 -1 43  GLU   C OE2   1 
ATOM   3047 N  N     . LYS   C 2 45  ? 89.20200 -15.84800 36.23100  1.000 46.05654 ?  44  LYS   C N     1 
ATOM   3048 C  CA    . LYS   C 2 45  ? 89.11300 -14.96400 35.07600  1.000 47.79121 ?  44  LYS   C CA    1 
ATOM   3049 C  C     . LYS   C 2 45  ? 88.50100 -13.61600 35.42500  1.000 45.74319 ?  44  LYS   C C     1 
ATOM   3050 O  O     . LYS   C 2 45  ? 88.33600 -12.77400 34.53400  1.000 53.91453 ?  44  LYS   C O     1 
ATOM   3051 C  CB    . LYS   C 2 45  ? 88.29000 -15.60300 33.94600  1.000 45.48672 ?  44  LYS   C CB    1 
ATOM   3052 C  CG    . LYS   C 2 45  ? 88.73200 -16.97900 33.50500  1.000 48.63189 ?  44  LYS   C CG    1 
ATOM   3053 C  CD    . LYS   C 2 45  ? 90.07400 -16.97600 32.78900  1.000 38.89195 ?  44  LYS   C CD    1 
ATOM   3054 C  CE    . LYS   C 2 45  ? 90.58200 -18.41900 32.62500  1.000 44.28029 ?  44  LYS   C CE    1 
ATOM   3055 N  NZ    . LYS   C 2 45  ? 91.84100 -18.54000 31.82600  1.000 51.60225 ?  44  LYS   C NZ    1 
ATOM   3056 N  N     . GLY   C 2 46  ? 88.15900 -13.38700 36.69300  1.000 42.22589 ?  45  GLY   C N     1 
ATOM   3057 C  CA    . GLY   C 2 46  ? 87.50200 -12.15000 37.07400  1.000 40.69677 ?  45  GLY   C CA    1 
ATOM   3058 C  C     . GLY   C 2 46  ? 85.99400 -12.19700 37.08100  1.000 43.13393 ?  45  GLY   C C     1 
ATOM   3059 O  O     . GLY   C 2 46  ? 85.36100 -11.17000 37.37200  1.000 43.77787 ?  45  GLY   C O     1 
ATOM   3060 N  N     . PHE   C 2 47  ? 85.39700 -13.34500 36.75200  1.000 40.82467 ?  46  PHE   C N     1 
ATOM   3061 C  CA    . PHE   C 2 47  ? 83.95200 -13.53700 36.83100  1.000 40.68650 ?  46  PHE   C CA    1 
ATOM   3062 C  C     . PHE   C 2 47  ? 83.70800 -15.02100 37.08200  1.000 35.64163 ?  46  PHE   C C     1 
ATOM   3063 O  O     . PHE   C 2 47  ? 84.62000 -15.84200 36.98400  1.000 36.08103 ?  46  PHE   C O     1 
ATOM   3064 C  CB    . PHE   C 2 47  ? 83.24200 -13.05100 35.55000  1.000 39.24404 ?  46  PHE   C CB    1 
ATOM   3065 C  CG    . PHE   C 2 47  ? 83.83000 -13.62900 34.27600  1.000 42.80701 ?  46  PHE   C CG    1 
ATOM   3066 C  CD1   . PHE   C 2 47  ? 83.43800 -14.88800 33.81600  1.000 41.15951 ?  46  PHE   C CD1   1 
ATOM   3067 C  CD2   . PHE   C 2 47  ? 84.78600 -12.92100 33.54600  1.000 41.74280 ?  46  PHE   C CD2   1 
ATOM   3068 C  CE1   . PHE   C 2 47  ? 83.98700 -15.42600 32.64000  1.000 38.15205 ?  46  PHE   C CE1   1 
ATOM   3069 C  CE2   . PHE   C 2 47  ? 85.34900 -13.45600 32.37900  1.000 45.44209 ?  46  PHE   C CE2   1 
ATOM   3070 C  CZ    . PHE   C 2 47  ? 84.95400 -14.70700 31.92500  1.000 45.57928 ?  46  PHE   C CZ    1 
ATOM   3071 N  N     . GLY   C 2 48  ? 82.47500 -15.37300 37.41900  1.000 35.74910 ?  47  GLY   C N     1 
ATOM   3072 C  CA    . GLY   C 2 48  ? 82.23600 -16.76500 37.77200  1.000 35.63946 ?  47  GLY   C CA    1 
ATOM   3073 C  C     . GLY   C 2 48  ? 80.95600 -16.93200 38.57800  1.000 30.64028 ?  47  GLY   C C     1 
ATOM   3074 O  O     . GLY   C 2 48  ? 80.13400 -16.02300 38.66300  1.000 30.75071 ?  47  GLY   C O     1 
ATOM   3075 N  N     . TYR   C 2 49  ? 80.81100 -18.12200 39.16200  1.000 31.60536 ?  48  TYR   C N     1 
ATOM   3076 C  CA    . TYR   C 2 49  ? 79.54400 -18.51000 39.83600  1.000 32.50391 ?  48  TYR   C CA    1 
ATOM   3077 C  C     . TYR   C 2 49  ? 79.35800 -17.90300 41.21400  1.000 33.49076 ?  48  TYR   C C     1 
ATOM   3078 O  O     . TYR   C 2 49  ? 78.21900 -17.87200 41.67700  1.000 29.81469 ?  48  TYR   C O     1 
ATOM   3079 C  CB    . TYR   C 2 49  ? 79.59600 -20.03700 39.95300  1.000 29.23158 ?  48  TYR   C CB    1 
ATOM   3080 C  CG    . TYR   C 2 49  ? 79.52200 -20.80300 38.64200  1.000 28.33857 ?  48  TYR   C CG    1 
ATOM   3081 C  CD1   . TYR   C 2 49  ? 78.62100 -20.44100 37.65300  1.000 29.94943 ?  48  TYR   C CD1   1 
ATOM   3082 C  CD2   . TYR   C 2 49  ? 80.34200 -21.89500 38.40400  1.000 29.13602 ?  48  TYR   C CD2   1 
ATOM   3083 C  CE1   . TYR   C 2 49  ? 78.54100 -21.13900 36.46200  1.000 29.50263 ?  48  TYR   C CE1   1 
ATOM   3084 C  CE2   . TYR   C 2 49  ? 80.27100 -22.60200 37.21800  1.000 27.96430 ?  48  TYR   C CE2   1 
ATOM   3085 C  CZ    . TYR   C 2 49  ? 79.36900 -22.22200 36.24300  1.000 27.58362 ?  48  TYR   C CZ    1 
ATOM   3086 O  OH    . TYR   C 2 49  ? 79.29200 -22.91100 35.07200  1.000 26.12206 ?  48  TYR   C OH    1 
ATOM   3087 N  N     . LYS   C 2 50  ? 80.42800 -17.43400 41.85000  1.000 33.22889 ?  49  LYS   C N     1 
ATOM   3088 C  CA    . LYS   C 2 50  ? 80.24000 -16.96900 43.22100  1.000 36.25952 ?  49  LYS   C CA    1 
ATOM   3089 C  C     . LYS   C 2 50  ? 79.18900 -15.86500 43.26800  1.000 30.26102 ?  49  LYS   C C     1 
ATOM   3090 O  O     . LYS   C 2 50  ? 79.22200 -14.92100 42.47300  1.000 35.58486 ?  49  LYS   C O     1 
ATOM   3091 C  CB    . LYS   C 2 50  ? 81.57000 -16.47800 43.80000  1.000 37.31563 ?  49  LYS   C CB    1 
ATOM   3092 C  CG    . LYS   C 2 50  ? 81.48100 -16.01000 45.24600  1.000 36.38597 ?  49  LYS   C CG    1 
ATOM   3093 C  CD    . LYS   C 2 50  ? 82.88800 -15.71000 45.77200  1.000 42.74519 ?  49  LYS   C CD    1 
ATOM   3094 C  CE    . LYS   C 2 50  ? 82.84400 -15.14000 47.18600  1.000 44.56162 ?  49  LYS   C CE    1 
ATOM   3095 N  NZ    . LYS   C 2 50  ? 84.23300 -15.03700 47.74500  1.000 41.92107 ?  49  LYS   C NZ    1 
ATOM   3096 N  N     . GLY   C 2 51  ? 78.21500 -16.00600 44.17100  1.000 29.96004 ?  50  GLY   C N     1 
ATOM   3097 C  CA    . GLY   C 2 51  ? 77.14900 -15.03700 44.28400  1.000 33.91303 ?  50  GLY   C CA    1 
ATOM   3098 C  C     . GLY   C 2 51  ? 75.91600 -15.32300 43.45500  1.000 32.32274 ?  50  GLY   C C     1 
ATOM   3099 O  O     . GLY   C 2 51  ? 74.86600 -14.72600 43.71100  1.000 35.29080 ?  50  GLY   C O     1 
ATOM   3100 N  N     . SER   C 2 52  ? 75.99900 -16.21900 42.47600  1.000 30.25403 ?  51  SER   C N     1 
ATOM   3101 C  CA    . SER   C 2 52  ? 74.87700 -16.44100 41.58700  1.000 28.07650 ?  51  SER   C CA    1 
ATOM   3102 C  C     . SER   C 2 52  ? 73.91800 -17.45100 42.20600  1.000 30.16052 ?  51  SER   C C     1 
ATOM   3103 O  O     . SER   C 2 52  ? 74.22300 -18.10300 43.20700  1.000 28.13150 ?  51  SER   C O     1 
ATOM   3104 C  CB    . SER   C 2 52  ? 75.36900 -16.92400 40.22300  1.000 28.60344 ?  51  SER   C CB    1 
ATOM   3105 O  OG    . SER   C 2 52  ? 75.84200 -18.26300 40.30300  1.000 31.00783 ?  51  SER   C OG    1 
ATOM   3106 N  N     . CYS   C 2 53  ? 72.75700 -17.60400 41.57900  1.000 27.65369 ?  52  CYS   C N     1 
ATOM   3107 C  CA    . CYS   C 2 53  ? 71.69700 -18.37800 42.18800  1.000 27.16749 ?  52  CYS   C CA    1 
ATOM   3108 C  C     . CYS   C 2 53  ? 71.28600 -19.55500 41.31800  1.000 27.21706 ?  52  CYS   C C     1 
ATOM   3109 O  O     . CYS   C 2 53  ? 71.57900 -19.61500 40.10900  1.000 27.06032 ?  52  CYS   C O     1 
ATOM   3110 C  CB    . CYS   C 2 53  ? 70.49700 -17.48900 42.48800  1.000 30.71812 ?  52  CYS   C CB    1 
ATOM   3111 S  SG    . CYS   C 2 53  ? 69.42000 -17.19500 41.13200  1.000 42.80144 ?  52  CYS   C SG    1 
ATOM   3112 N  N     . PHE   C 2 54  ? 70.58400 -20.48400 41.96600  1.000 27.13326 ?  53  PHE   C N     1 
ATOM   3113 C  CA    . PHE   C 2 54  ? 69.94000 -21.58800 41.22700  1.000 26.20821 ?  53  PHE   C CA    1 
ATOM   3114 C  C     . PHE   C 2 54  ? 68.55600 -21.05300 40.92600  1.000 25.97973 ?  53  PHE   C C     1 
ATOM   3115 O  O     . PHE   C 2 54  ? 67.73600 -20.92600 41.84100  1.000 26.98393 ?  53  PHE   C O     1 
ATOM   3116 C  CB    . PHE   C 2 54  ? 69.92100 -22.85700 42.07300  1.000 27.30013 ?  53  PHE   C CB    1 
ATOM   3117 C  CG    . PHE   C 2 54  ? 71.21100 -23.65800 42.03000  1.000 24.83439 ?  53  PHE   C CG    1 
ATOM   3118 C  CD1   . PHE   C 2 54  ? 72.25700 -23.37000 42.89400  1.000 23.19170 ?  53  PHE   C CD1   1 
ATOM   3119 C  CD2   . PHE   C 2 54  ? 71.36900 -24.69700 41.12500  1.000 23.42462 ?  53  PHE   C CD2   1 
ATOM   3120 C  CE1   . PHE   C 2 54  ? 73.42900 -24.10100 42.85000  1.000 23.82424 ?  53  PHE   C CE1   1 
ATOM   3121 C  CE2   . PHE   C 2 54  ? 72.54200 -25.42600 41.08700  1.000 26.15696 ?  53  PHE   C CE2   1 
ATOM   3122 C  CZ    . PHE   C 2 54  ? 73.56800 -25.12600 41.94900  1.000 26.54613 ?  53  PHE   C CZ    1 
ATOM   3123 N  N     . HIS   C 2 55  ? 68.31000 -20.72000 39.67300  1.000 23.98861 ?  54  HIS   C N     1 
ATOM   3124 C  CA    . HIS   C 2 55  ? 67.08100 -20.04200 39.31500  1.000 24.64670 ?  54  HIS   C CA    1 
ATOM   3125 C  C     . HIS   C 2 55  ? 65.95100 -20.99900 38.99200  1.000 26.58283 ?  54  HIS   C C     1 
ATOM   3126 O  O     . HIS   C 2 55  ? 64.80800 -20.56400 38.97700  1.000 27.87579 ?  54  HIS   C O     1 
ATOM   3127 C  CB    . HIS   C 2 55  ? 67.31100 -19.10400 38.12000  1.000 25.39329 ?  54  HIS   C CB    1 
ATOM   3128 C  CG    . HIS   C 2 55  ? 67.84300 -19.78400 36.89300  1.000 28.64082 ?  54  HIS   C CG    1 
ATOM   3129 N  ND1   . HIS   C 2 55  ? 69.16700 -20.13500 36.75300  1.000 26.75158 ?  54  HIS   C ND1   1 
ATOM   3130 C  CD2   . HIS   C 2 55  ? 67.23400 -20.14400 35.73500  1.000 30.16291 ?  54  HIS   C CD2   1 
ATOM   3131 C  CE1   . HIS   C 2 55  ? 69.35100 -20.70800 35.57200  1.000 27.72529 ?  54  HIS   C CE1   1 
ATOM   3132 N  NE2   . HIS   C 2 55  ? 68.19700 -20.71300 34.92700  1.000 28.95818 ?  54  HIS   C NE2   1 
ATOM   3133 N  N     . ARG   C 2 56  ? 66.23500 -22.28000 38.74300  1.000 24.39839 ?  55  ARG   C N     1 
ATOM   3134 C  CA    . ARG   C 2 56  ? 65.21700 -23.23100 38.30300  1.000 24.00763 ?  55  ARG   C CA    1 
ATOM   3135 C  C     . ARG   C 2 56  ? 65.47400 -24.55100 39.00500  1.000 23.05664 ?  55  ARG   C C     1 
ATOM   3136 O  O     . ARG   C 2 56  ? 66.45300 -25.24800 38.69300  1.000 23.57326 ?  55  ARG   C O     1 
ATOM   3137 C  CB    . ARG   C 2 56  ? 65.24500 -23.42500 36.78100  1.000 26.31661 ?  55  ARG   C CB    1 
ATOM   3138 C  CG    . ARG   C 2 56  ? 64.10600 -24.25300 36.26200  1.000 30.05545 ?  55  ARG   C CG    1 
ATOM   3139 C  CD    . ARG   C 2 56  ? 64.27600 -24.51000 34.72900  1.000 26.91411 ?  55  ARG   C CD    1 
ATOM   3140 N  NE    . ARG   C 2 56  ? 64.15500 -23.27300 33.97600  1.000 30.67076 ?  55  ARG   C NE    1 
ATOM   3141 C  CZ    . ARG   C 2 56  ? 64.66400 -23.09100 32.76600  1.000 34.93469 ?  55  ARG   C CZ    1 
ATOM   3142 N  NH1   . ARG   C 2 56  ? 65.27200 -24.07500 32.11100  1.000 28.90776 ?  55  ARG   C NH1   1 
ATOM   3143 N  NH2   . ARG   C 2 56  ? 64.56500 -21.89300 32.20300  1.000 44.89513 ?  55  ARG   C NH2   1 
ATOM   3144 N  N     . ILE   C 2 57  ? 64.59500 -24.90900 39.92300  1.000 19.54560 ?  56  ILE   C N     1 
ATOM   3145 C  CA    . ILE   C 2 57  ? 64.69500 -26.15900 40.68600  1.000 19.52137 ?  56  ILE   C CA    1 
ATOM   3146 C  C     . ILE   C 2 57  ? 63.35300 -26.85300 40.53600  1.000 22.50969 ?  56  ILE   C C     1 
ATOM   3147 O  O     . ILE   C 2 57  ? 62.32700 -26.34600 41.01200  1.000 19.64234 ?  56  ILE   C O     1 
ATOM   3148 C  CB    . ILE   C 2 57  ? 65.01800 -25.88200 42.15400  1.000 22.18599 ?  56  ILE   C CB    1 
ATOM   3149 C  CG1   . ILE   C 2 57  ? 66.39900 -25.20100 42.22900  1.000 22.45909 ?  56  ILE   C CG1   1 
ATOM   3150 C  CG2   . ILE   C 2 57  ? 64.90500 -27.15600 42.98300  1.000 24.52964 ?  56  ILE   C CG2   1 
ATOM   3151 C  CD1   . ILE   C 2 57  ? 66.78900 -24.81400 43.68400  1.000 25.36967 ?  56  ILE   C CD1   1 
ATOM   3152 N  N     . ILE   C 2 58  ? 63.34900 -27.98900 39.86300  1.000 20.12852 ?  57  ILE   C N     1 
ATOM   3153 C  CA    . ILE   C 2 58  ? 62.14000 -28.73900 39.59100  1.000 21.27201 ?  57  ILE   C CA    1 
ATOM   3154 C  C     . ILE   C 2 58  ? 62.28300 -30.11200 40.21800  1.000 20.04952 ?  57  ILE   C C     1 
ATOM   3155 O  O     . ILE   C 2 58  ? 62.99400 -30.97200 39.69900  1.000 19.62923 ?  57  ILE   C O     1 
ATOM   3156 C  CB    . ILE   C 2 58  ? 61.86800 -28.83700 38.07800  1.000 22.24629 ?  57  ILE   C CB    1 
ATOM   3157 C  CG1   . ILE   C 2 58  ? 61.87700 -27.42200 37.47100  1.000 22.74343 ?  57  ILE   C CG1   1 
ATOM   3158 C  CG2   . ILE   C 2 58  ? 60.56300 -29.59600 37.86000  1.000 23.88908 ?  57  ILE   C CG2   1 
ATOM   3159 C  CD1   . ILE   C 2 58  ? 61.46900 -27.39200 36.00600  1.000 23.55541 ?  57  ILE   C CD1   1 
ATOM   3160 N  N     . PRO   C 2 59  ? 61.59700 -30.35800 41.33500  1.000 21.82489 ?  58  PRO   C N     1 
ATOM   3161 C  CA    . PRO   C 2 59  ? 61.70200 -31.66400 42.00400  1.000 23.49714 ?  58  PRO   C CA    1 
ATOM   3162 C  C     . PRO   C 2 59  ? 61.32700 -32.81300 41.08600  1.000 22.81784 ?  58  PRO   C C     1 
ATOM   3163 O  O     . PRO   C 2 59  ? 60.39000 -32.72200 40.29000  1.000 21.73760 ?  58  PRO   C O     1 
ATOM   3164 C  CB    . PRO   C 2 59  ? 60.71100 -31.53800 43.17700  1.000 22.31731 ?  58  PRO   C CB    1 
ATOM   3165 C  CG    . PRO   C 2 59  ? 60.59700 -30.06700 43.45400  1.000 23.79539 ?  58  PRO   C CG    1 
ATOM   3166 C  CD    . PRO   C 2 59  ? 60.82100 -29.37600 42.11400  1.000 23.81715 ?  58  PRO   C CD    1 
ATOM   3167 N  N     . GLY   C 2 60  ? 62.07700 -33.90700 41.18800  1.000 22.52579 ?  59  GLY   C N     1 
ATOM   3168 C  CA    . GLY   C 2 60  ? 61.94900 -35.00700 40.26200  1.000 23.39532 ?  59  GLY   C CA    1 
ATOM   3169 C  C     . GLY   C 2 60  ? 62.87100 -34.94700 39.06100  1.000 21.37070 ?  59  GLY   C C     1 
ATOM   3170 O  O     . GLY   C 2 60  ? 62.94000 -35.94000 38.31500  1.000 22.60435 ?  59  GLY   C O     1 
ATOM   3171 N  N     . PHE   C 2 61  ? 63.59600 -33.83800 38.87600  1.000 21.07194 ?  60  PHE   C N     1 
ATOM   3172 C  CA    . PHE   C 2 61  ? 64.33400 -33.62500 37.63100  1.000 21.87607 ?  60  PHE   C CA    1 
ATOM   3173 C  C     . PHE   C 2 61  ? 65.70600 -33.02600 37.89800  1.000 19.99383 ?  60  PHE   C C     1 
ATOM   3174 O  O     . PHE   C 2 61  ? 66.69900 -33.72900 37.71600  1.000 21.27521 ?  60  PHE   C O     1 
ATOM   3175 C  CB    . PHE   C 2 61  ? 63.53600 -32.72800 36.67000  1.000 22.57905 ?  60  PHE   C CB    1 
ATOM   3176 C  CG    . PHE   C 2 61  ? 62.25300 -33.37500 36.16900  1.000 21.88448 ?  60  PHE   C CG    1 
ATOM   3177 C  CD1   . PHE   C 2 61  ? 62.27500 -34.25200 35.10600  1.000 24.58667 ?  60  PHE   C CD1   1 
ATOM   3178 C  CD2   . PHE   C 2 61  ? 61.04400 -33.13100 36.80800  1.000 24.99217 ?  60  PHE   C CD2   1 
ATOM   3179 C  CE1   . PHE   C 2 61  ? 61.11700 -34.83600 34.64200  1.000 28.20303 ?  60  PHE   C CE1   1 
ATOM   3180 C  CE2   . PHE   C 2 61  ? 59.88000 -33.72900 36.35100  1.000 28.62966 ?  60  PHE   C CE2   1 
ATOM   3181 C  CZ    . PHE   C 2 61  ? 59.92400 -34.59000 35.27900  1.000 26.04007 ?  60  PHE   C CZ    1 
ATOM   3182 N  N     . MET   C 2 62  ? 65.79000 -31.74100 38.25700  1.000 20.44163 ?  61  MET   C N     1 
ATOM   3183 C  CA    . MET   C 2 62  ? 67.12600 -31.13700 38.30400  1.000 22.33610 ?  61  MET   C CA    1 
ATOM   3184 C  C     . MET   C 2 62  ? 67.10300 -29.81500 39.04300  1.000 21.47853 ?  61  MET   C C     1 
ATOM   3185 O  O     . MET   C 2 62  ? 66.04900 -29.20800 39.25100  1.000 19.95079 ?  61  MET   C O     1 
ATOM   3186 C  CB    . MET   C 2 62  ? 67.70900 -30.90800 36.89900  1.000 20.46082 ?  61  MET   C CB    1 
ATOM   3187 C  CG    . MET   C 2 62  ? 67.29300 -29.52100 36.32200  1.000 24.24932 ?  61  MET   C CG    1 
ATOM   3188 S  SD    . MET   C 2 62  ? 65.55100 -29.42000 35.84400  1.000 27.84463 ?  61  MET   C SD    1 
ATOM   3189 C  CE    . MET   C 2 62  ? 65.31300 -27.66200 36.04000  1.000 25.68292 ?  61  MET   C CE    1 
ATOM   3190 N  N     . CYS   C 2 63  ? 68.30200 -29.36400 39.41700  1.000 19.85896 ?  62  CYS   C N     1 
ATOM   3191 C  CA    . CYS   C 2 63  ? 68.58200 -28.01100 39.90800  1.000 21.04389 ?  62  CYS   C CA    1 
ATOM   3192 C  C     . CYS   C 2 63  ? 69.45300 -27.30000 38.87900  1.000 21.31160 ?  62  CYS   C C     1 
ATOM   3193 O  O     . CYS   C 2 63  ? 70.55700 -27.76400 38.60700  1.000 23.14179 ?  62  CYS   C O     1 
ATOM   3194 C  CB    . CYS   C 2 63  ? 69.33600 -28.05500 41.23300  1.000 21.64206 ?  62  CYS   C CB    1 
ATOM   3195 S  SG    . CYS   C 2 63  ? 68.46800 -28.89200 42.58200  1.000 25.97389 ?  62  CYS   C SG    1 
ATOM   3196 N  N     . GLN   C 2 64  ? 68.99300 -26.16200 38.34600  1.000 20.10636 ?  63  GLN   C N     1 
ATOM   3197 C  CA    . GLN   C 2 64  ? 69.72200 -25.46000 37.29300  1.000 20.36025 ?  63  GLN   C CA    1 
ATOM   3198 C  C     . GLN   C 2 64  ? 70.14800 -24.06900 37.75400  1.000 22.05132 ?  63  GLN   C C     1 
ATOM   3199 O  O     . GLN   C 2 64  ? 69.37000 -23.35300 38.40900  1.000 20.80841 ?  63  GLN   C O     1 
ATOM   3200 C  CB    . GLN   C 2 64  ? 68.88900 -25.37400 36.00500  1.000 20.42329 ?  63  GLN   C CB    1 
ATOM   3201 C  CG    . GLN   C 2 64  ? 69.51200 -24.54900 34.92500  1.000 20.82409 ?  63  GLN   C CG    1 
ATOM   3202 C  CD    . GLN   C 2 64  ? 68.67700 -24.55400 33.64100  1.000 22.45271 ?  63  GLN   C CD    1 
ATOM   3203 O  OE1   . GLN   C 2 64  ? 67.82500 -25.39800 33.45800  1.000 24.16344 ?  63  GLN   C OE1   1 
ATOM   3204 N  NE2   . GLN   C 2 64  ? 68.90600 -23.56400 32.78000  1.000 24.49634 ?  63  GLN   C NE2   1 
ATOM   3205 N  N     . GLY   C 2 65  ? 71.39400 -23.70900 37.42500  1.000 21.42342 ?  64  GLY   C N     1 
ATOM   3206 C  CA    . GLY   C 2 65  ? 71.97900 -22.43300 37.83200  1.000 24.12516 ?  64  GLY   C CA    1 
ATOM   3207 C  C     . GLY   C 2 65  ? 72.98500 -21.92100 36.84100  1.000 26.44959 ?  64  GLY   C C     1 
ATOM   3208 O  O     . GLY   C 2 65  ? 73.04300 -22.41500 35.70000  1.000 25.95141 ?  64  GLY   C O     1 
ATOM   3209 N  N     . GLY   C 2 66  ? 73.77200 -20.92400 37.25600  1.000 24.90481 ?  65  GLY   C N     1 
ATOM   3210 C  CA    . GLY   C 2 66  ? 74.95000 -20.50400 36.52800  1.000 28.23211 ?  65  GLY   C CA    1 
ATOM   3211 C  C     . GLY   C 2 66  ? 74.83300 -19.19500 35.78000  1.000 27.64643 ?  65  GLY   C C     1 
ATOM   3212 O  O     . GLY   C 2 66  ? 75.79800 -18.82200 35.09500  1.000 28.37157 ?  65  GLY   C O     1 
ATOM   3213 N  N     . ASP   C 2 67  ? 73.70500 -18.47400 35.87800  1.000 32.58135 ?  66  ASP   C N     1 
ATOM   3214 C  CA    . ASP   C 2 67  ? 73.57000 -17.15200 35.24900  1.000 33.23737 ?  66  ASP   C CA    1 
ATOM   3215 C  C     . ASP   C 2 67  ? 74.12600 -16.09600 36.19700  1.000 35.89765 ?  66  ASP   C C     1 
ATOM   3216 O  O     . ASP   C 2 67  ? 73.43300 -15.64000 37.10500  1.000 40.31388 ?  66  ASP   C O     1 
ATOM   3217 C  CB    . ASP   C 2 67  ? 72.11900 -16.84700 34.90400  1.000 34.71567 ?  66  ASP   C CB    1 
ATOM   3218 C  CG    . ASP   C 2 67  ? 71.92100 -15.42500 34.35200  1.000 37.00397 ?  66  ASP   C CG    1 
ATOM   3219 O  OD1   . ASP   C 2 67  ? 72.92900 -14.69900 34.10200  1.000 36.86550 ?  66  ASP   C OD1   1 
ATOM   3220 O  OD2   . ASP   C 2 67  ? 70.74200 -15.04700 34.14300  1.000 38.93511 -1 66  ASP   C OD2   1 
ATOM   3221 N  N     . PHE   C 2 68  ? 75.36700 -15.68000 35.96700  1.000 32.30829 ?  67  PHE   C N     1 
ATOM   3222 C  CA    . PHE   C 2 68  ? 75.99700 -14.64800 36.77700  1.000 36.42150 ?  67  PHE   C CA    1 
ATOM   3223 C  C     . PHE   C 2 68  ? 76.13600 -13.31800 36.05000  1.000 42.27554 ?  67  PHE   C C     1 
ATOM   3224 O  O     . PHE   C 2 68  ? 76.77200 -12.39900 36.58400  1.000 43.93184 ?  67  PHE   C O     1 
ATOM   3225 C  CB    . PHE   C 2 68  ? 77.38600 -15.10700 37.24300  1.000 35.12347 ?  67  PHE   C CB    1 
ATOM   3226 C  CG    . PHE   C 2 68  ? 78.31900 -15.46400 36.11700  1.000 32.86106 ?  67  PHE   C CG    1 
ATOM   3227 C  CD1   . PHE   C 2 68  ? 78.99300 -14.48000 35.41400  1.000 34.74647 ?  67  PHE   C CD1   1 
ATOM   3228 C  CD2   . PHE   C 2 68  ? 78.53100 -16.78700 35.77000  1.000 38.95492 ?  67  PHE   C CD2   1 
ATOM   3229 C  CE1   . PHE   C 2 68  ? 79.87000 -14.81700 34.37200  1.000 41.58665 ?  67  PHE   C CE1   1 
ATOM   3230 C  CE2   . PHE   C 2 68  ? 79.38700 -17.13300 34.73300  1.000 37.27537 ?  67  PHE   C CE2   1 
ATOM   3231 C  CZ    . PHE   C 2 68  ? 80.06000 -16.14400 34.02700  1.000 36.14277 ?  67  PHE   C CZ    1 
ATOM   3232 N  N     . THR   C 2 69  ? 75.63100 -13.20500 34.82600  1.000 39.37652 ?  68  THR   C N     1 
ATOM   3233 C  CA    . THR   C 2 69  ? 75.76700 -11.97000 34.06000  1.000 41.34405 ?  68  THR   C CA    1 
ATOM   3234 C  C     . THR   C 2 69  ? 74.48900 -11.14400 34.03200  1.000 40.63530 ?  68  THR   C C     1 
ATOM   3235 O  O     . THR   C 2 69  ? 74.55400 -9.91100  34.06400  1.000 44.89614 ?  68  THR   C O     1 
ATOM   3236 C  CB    . THR   C 2 69  ? 76.19500 -12.26300 32.61600  1.000 39.93298 ?  68  THR   C CB    1 
ATOM   3237 O  OG1   . THR   C 2 69  ? 75.15000 -12.98700 31.94900  1.000 42.02413 ?  68  THR   C OG1   1 
ATOM   3238 C  CG2   . THR   C 2 69  ? 77.49200 -13.05600 32.58700  1.000 35.23545 ?  68  THR   C CG2   1 
ATOM   3239 N  N     . ARG   C 2 70  ? 73.32800 -11.80000 33.99900  1.000 39.87734 ?  69  ARG   C N     1 
ATOM   3240 C  CA    . ARG   C 2 70  ? 72.02800 -11.07300 33.93400  1.000 42.54093 ?  69  ARG   C CA    1 
ATOM   3241 C  C     . ARG   C 2 70  ? 71.20000 -11.36000 35.19300  1.000 42.36786 ?  69  ARG   C C     1 
ATOM   3242 O  O     . ARG   C 2 70  ? 70.30300 -10.55900 35.48000  1.000 44.36014 ?  69  ARG   C O     1 
ATOM   3243 C  CB    . ARG   C 2 70  ? 71.27600 -11.44600 32.65600  1.000 38.77707 ?  69  ARG   C CB    1 
ATOM   3244 C  CG    . ARG   C 2 70  ? 72.06300 -11.25300 31.37000  1.000 45.58554 ?  69  ARG   C CG    1 
ATOM   3245 C  CD    . ARG   C 2 70  ? 71.13700 -11.32000 30.17800  1.000 45.90968 ?  69  ARG   C CD    1 
ATOM   3246 N  NE    . ARG   C 2 70  ? 71.83100 -11.65900 28.93200  1.000 49.86866 ?  69  ARG   C NE    1 
ATOM   3247 C  CZ    . ARG   C 2 70  ? 71.27100 -12.31000 27.92500  1.000 51.12228 ?  69  ARG   C CZ    1 
ATOM   3248 N  NH1   . ARG   C 2 70  ? 70.11300 -12.91900 28.09300  1.000 47.95839 ?  69  ARG   C NH1   1 
ATOM   3249 N  NH2   . ARG   C 2 70  ? 71.87000 -12.34800 26.75000  1.000 52.89744 ?  69  ARG   C NH2   1 
ATOM   3250 N  N     . HIS   C 2 71  ? 71.47400 -12.47200 35.87100  1.000 41.83454 ?  70  HIS   C N     1 
ATOM   3251 C  CA    . HIS   C 2 71  ? 70.81400 -12.84200 37.12200  1.000 41.60261 ?  70  HIS   C CA    1 
ATOM   3252 C  C     . HIS   C 2 71  ? 69.30700 -12.98400 36.97000  1.000 39.08152 ?  70  HIS   C C     1 
ATOM   3253 O  O     . HIS   C 2 71  ? 68.55900 -12.70200 37.90400  1.000 44.86603 ?  70  HIS   C O     1 
ATOM   3254 C  CB    . HIS   C 2 71  ? 71.14600 -11.84300 38.23300  1.000 43.40851 ?  70  HIS   C CB    1 
ATOM   3255 C  CG    . HIS   C 2 71  ? 72.60900 -11.73900 38.51000  1.000 45.03556 ?  70  HIS   C CG    1 
ATOM   3256 N  ND1   . HIS   C 2 71  ? 73.24400 -12.52100 39.45000  1.000 46.13591 ?  70  HIS   C ND1   1 
ATOM   3257 C  CD2   . HIS   C 2 71  ? 73.56800 -10.96400 37.95100  1.000 35.66803 ?  70  HIS   C CD2   1 
ATOM   3258 C  CE1   . HIS   C 2 71  ? 74.53300 -12.23000 39.46200  1.000 42.12944 ?  70  HIS   C CE1   1 
ATOM   3259 N  NE2   . HIS   C 2 71  ? 74.75300 -11.28500 38.56400  1.000 45.49271 ?  70  HIS   C NE2   1 
ATOM   3260 N  N     . ASN   C 2 72  ? 68.87900 -13.46800 35.80400  1.000 39.32591 ?  71  ASN   C N     1 
ATOM   3261 C  CA    . ASN   C 2 72  ? 67.43000 -13.63600 35.51100  1.000 40.00821 ?  71  ASN   C CA    1 
ATOM   3262 C  C     . ASN   C 2 72  ? 67.17300 -14.99000 34.83600  1.000 42.90393 ?  71  ASN   C C     1 
ATOM   3263 O  O     . ASN   C 2 72  ? 66.06500 -15.18400 34.31500  1.000 41.89209 ?  71  ASN   C O     1 
ATOM   3264 C  CB    . ASN   C 2 72  ? 66.92300 -12.48500 34.65500  1.000 41.36725 ?  71  ASN   C CB    1 
ATOM   3265 C  CG    . ASN   C 2 72  ? 67.67900 -12.33300 33.35700  1.000 40.90813 ?  71  ASN   C CG    1 
ATOM   3266 O  OD1   . ASN   C 2 72  ? 68.56500 -13.13300 33.05000  1.000 45.98142 ?  71  ASN   C OD1   1 
ATOM   3267 N  ND2   . ASN   C 2 72  ? 67.34600 -11.31500 32.58100  1.000 48.76130 ?  71  ASN   C ND2   1 
ATOM   3268 N  N     . GLY   C 2 73  ? 68.16400 -15.88100 34.82500  1.000 40.65344 ?  72  GLY   C N     1 
ATOM   3269 C  CA    . GLY   C 2 73  ? 68.02000 -17.16000 34.16500  1.000 35.28835 ?  72  GLY   C CA    1 
ATOM   3270 C  C     . GLY   C 2 73  ? 68.26500 -17.16500 32.67300  1.000 37.88888 ?  72  GLY   C C     1 
ATOM   3271 O  O     . GLY   C 2 73  ? 68.15900 -18.23200 32.05100  1.000 39.01511 ?  72  GLY   C O     1 
ATOM   3272 N  N     . THR   C 2 74  ? 68.63200 -16.02300 32.07800  1.000 37.07017 ?  73  THR   C N     1 
ATOM   3273 C  CA    . THR   C 2 74  ? 68.78300 -15.92600 30.60500  1.000 42.18535 ?  73  THR   C CA    1 
ATOM   3274 C  C     . THR   C 2 74  ? 70.21900 -15.70000 30.20900  1.000 40.55611 ?  73  THR   C C     1 
ATOM   3275 O  O     . THR   C 2 74  ? 70.50900 -15.81400 29.01000  1.000 43.86294 ?  73  THR   C O     1 
ATOM   3276 C  CB    . THR   C 2 74  ? 67.93200 -14.75900 30.09200  1.000 42.09689 ?  73  THR   C CB    1 
ATOM   3277 O  OG1   . THR   C 2 74  ? 68.64300 -13.56200 30.38700  1.000 44.98285 ?  73  THR   C OG1   1 
ATOM   3278 C  CG2   . THR   C 2 74  ? 66.55700 -14.71400 30.73200  1.000 40.50842 ?  73  THR   C CG2   1 
ATOM   3279 N  N     . GLY   C 2 75  ? 71.09900 -15.45900 31.16500  1.000 38.42455 ?  74  GLY   C N     1 
ATOM   3280 C  CA    . GLY   C 2 75  ? 72.44900 -15.04700 30.87700  1.000 35.81650 ?  74  GLY   C CA    1 
ATOM   3281 C  C     . GLY   C 2 75  ? 73.49600 -16.09800 31.18400  1.000 42.34573 ?  74  GLY   C C     1 
ATOM   3282 O  O     . GLY   C 2 75  ? 73.23100 -17.31000 31.17200  1.000 32.56442 ?  74  GLY   C O     1 
ATOM   3283 N  N     . GLY   C 2 76  ? 74.69800 -15.61800 31.48500  1.000 41.15487 ?  75  GLY   C N     1 
ATOM   3284 C  CA    . GLY   C 2 76  ? 75.88700 -16.42800 31.61400  1.000 40.16158 ?  75  GLY   C CA    1 
ATOM   3285 C  C     . GLY   C 2 76  ? 76.76800 -16.35400 30.37400  1.000 36.80730 ?  75  GLY   C C     1 
ATOM   3286 O  O     . GLY   C 2 76  ? 76.33000 -16.01100 29.27300  1.000 42.07336 ?  75  GLY   C O     1 
ATOM   3287 N  N     . LYS   C 2 77  ? 78.04400 -16.68000 30.57200  1.000 39.07734 ?  76  LYS   C N     1 
ATOM   3288 C  CA    . LYS   C 2 77  ? 79.03800 -16.67600 29.50900  1.000 40.82557 ?  76  LYS   C CA    1 
ATOM   3289 C  C     . LYS   C 2 77  ? 80.14900 -17.62300 29.91400  1.000 34.53842 ?  76  LYS   C C     1 
ATOM   3290 O  O     . LYS   C 2 77  ? 80.37200 -17.86400 31.10300  1.000 33.73649 ?  76  LYS   C O     1 
ATOM   3291 C  CB    . LYS   C 2 77  ? 79.59700 -15.27000 29.24400  1.000 38.41670 ?  76  LYS   C CB    1 
ATOM   3292 C  CG    . LYS   C 2 77  ? 80.40600 -14.71300 30.40200  1.000 43.14309 ?  76  LYS   C CG    1 
ATOM   3293 C  CD    . LYS   C 2 77  ? 80.83800 -13.28100 30.14000  1.000 44.66143 ?  76  LYS   C CD    1 
ATOM   3294 C  CE    . LYS   C 2 77  ? 81.53500 -12.70300 31.36500  1.000 45.20007 ?  76  LYS   C CE    1 
ATOM   3295 N  NZ    . LYS   C 2 77  ? 82.10900 -11.35000 31.06700  1.000 49.37425 ?  76  LYS   C NZ    1 
ATOM   3296 N  N     . SER   C 2 78  ? 80.83400 -18.16900 28.90700  1.000 32.63448 ?  77  SER   C N     1 
ATOM   3297 C  CA    . SER   C 2 78  ? 81.92100 -19.09500 29.12200  1.000 33.23866 ?  77  SER   C CA    1 
ATOM   3298 C  C     . SER   C 2 78  ? 83.23400 -18.32500 29.20800  1.000 34.11140 ?  77  SER   C C     1 
ATOM   3299 O  O     . SER   C 2 78  ? 83.27900 -17.10400 29.03700  1.000 41.15249 ?  77  SER   C O     1 
ATOM   3300 C  CB    . SER   C 2 78  ? 81.99100 -20.11300 27.98500  1.000 32.03443 ?  77  SER   C CB    1 
ATOM   3301 O  OG    . SER   C 2 78  ? 82.59100 -19.50500 26.83700  1.000 37.07365 ?  77  SER   C OG    1 
ATOM   3302 N  N     . ILE   C 2 79  ? 84.31000 -19.05000 29.48600  1.000 33.30067 ?  78  ILE   C N     1 
ATOM   3303 C  CA    . ILE   C 2 79  ? 85.64800 -18.45700 29.54500  1.000 39.24116 ?  78  ILE   C CA    1 
ATOM   3304 C  C     . ILE   C 2 79  ? 86.25000 -18.37000 28.14300  1.000 41.44441 ?  78  ILE   C C     1 
ATOM   3305 O  O     . ILE   C 2 79  ? 87.41800 -18.00300 27.98500  1.000 45.16041 ?  78  ILE   C O     1 
ATOM   3306 C  CB    . ILE   C 2 79  ? 86.56900 -19.26300 30.48000  1.000 36.17396 ?  78  ILE   C CB    1 
ATOM   3307 C  CG1   . ILE   C 2 79  ? 86.80000 -20.66500 29.90500  1.000 37.27866 ?  78  ILE   C CG1   1 
ATOM   3308 C  CG2   . ILE   C 2 79  ? 85.96800 -19.31900 31.88800  1.000 37.99411 ?  78  ILE   C CG2   1 
ATOM   3309 C  CD1   . ILE   C 2 79  ? 88.02300 -21.37500 30.40500  1.000 39.21232 ?  78  ILE   C CD1   1 
ATOM   3310 N  N     . TYR   C 2 80  ? 85.46600 -18.71000 27.11900  1.000 40.47086 ?  79  TYR   C N     1 
ATOM   3311 C  CA    . TYR   C 2 80  ? 85.93900 -18.73800 25.73800  1.000 45.21506 ?  79  TYR   C CA    1 
ATOM   3312 C  C     . TYR   C 2 80  ? 85.26400 -17.69100 24.86600  1.000 49.84410 ?  79  TYR   C C     1 
ATOM   3313 O  O     . TYR   C 2 80  ? 85.35300 -17.77800 23.63300  1.000 53.52444 ?  79  TYR   C O     1 
ATOM   3314 C  CB    . TYR   C 2 80  ? 85.70700 -20.11600 25.11200  1.000 36.61343 ?  79  TYR   C CB    1 
ATOM   3315 C  CG    . TYR   C 2 80  ? 86.22100 -21.26200 25.92800  1.000 37.81940 ?  79  TYR   C CG    1 
ATOM   3316 C  CD1   . TYR   C 2 80  ? 87.58000 -21.40000 26.18000  1.000 39.00648 ?  79  TYR   C CD1   1 
ATOM   3317 C  CD2   . TYR   C 2 80  ? 85.34600 -22.22300 26.44300  1.000 36.85714 ?  79  TYR   C CD2   1 
ATOM   3318 C  CE1   . TYR   C 2 80  ? 88.06500 -22.44100 26.91800  1.000 35.91964 ?  79  TYR   C CE1   1 
ATOM   3319 C  CE2   . TYR   C 2 80  ? 85.82100 -23.27800 27.18900  1.000 35.44833 ?  79  TYR   C CE2   1 
ATOM   3320 C  CZ    . TYR   C 2 80  ? 87.17300 -23.38000 27.43300  1.000 36.91251 ?  79  TYR   C CZ    1 
ATOM   3321 O  OH    . TYR   C 2 80  ? 87.66000 -24.42100 28.15900  1.000 35.93368 ?  79  TYR   C OH    1 
ATOM   3322 N  N     . GLY   C 2 81  ? 84.58800 -16.71500 25.46000  1.000 48.08348 ?  80  GLY   C N     1 
ATOM   3323 C  CA    . GLY   C 2 81  ? 83.61900 -15.91500 24.74400  1.000 44.90791 ?  80  GLY   C CA    1 
ATOM   3324 C  C     . GLY   C 2 81  ? 82.21200 -16.33700 25.11400  1.000 47.88222 ?  80  GLY   C C     1 
ATOM   3325 O  O     . GLY   C 2 81  ? 81.98200 -17.13600 26.03100  1.000 51.38991 ?  80  GLY   C O     1 
ATOM   3326 N  N     . GLU   C 2 82  ? 81.25000 -15.80000 24.36400  1.000 50.32739 ?  81  GLU   C N     1 
ATOM   3327 C  CA    . GLU   C 2 82  ? 79.84900 -15.94500 24.74900  1.000 44.29139 ?  81  GLU   C CA    1 
ATOM   3328 C  C     . GLU   C 2 82  ? 79.42300 -17.41100 24.79200  1.000 48.93348 ?  81  GLU   C C     1 
ATOM   3329 O  O     . GLU   C 2 82  ? 78.85700 -17.86300 25.79500  1.000 50.80994 ?  81  GLU   C O     1 
ATOM   3330 C  CB    . GLU   C 2 82  ? 78.95200 -15.14300 23.80600  1.000 47.95494 ?  81  GLU   C CB    1 
ATOM   3331 C  CG    . GLU   C 2 82  ? 78.99300 -13.63200 24.03700  1.000 52.67031 ?  81  GLU   C CG    1 
ATOM   3332 C  CD    . GLU   C 2 82  ? 79.02300 -12.83300 22.73400  1.000 58.38399 ?  81  GLU   C CD    1 
ATOM   3333 O  OE1   . GLU   C 2 82  ? 80.06000 -12.88400 22.02600  1.000 59.81079 ?  81  GLU   C OE1   1 
ATOM   3334 O  OE2   . GLU   C 2 82  ? 78.00900 -12.16300 22.42300  1.000 62.65973 -1 81  GLU   C OE2   1 
ATOM   3335 N  N     . LYS   C 2 83  ? 79.68800 -18.17500 23.71900  1.000 43.32926 ?  82  LYS   C N     1 
ATOM   3336 C  CA    . LYS   C 2 83  ? 79.19300 -19.54600 23.62300  1.000 39.86282 ?  82  LYS   C CA    1 
ATOM   3337 C  C     . LYS   C 2 83  ? 80.24700 -20.44700 22.98500  1.000 40.19396 ?  82  LYS   C C     1 
ATOM   3338 O  O     . LYS   C 2 83  ? 81.08600 -19.98900 22.20600  1.000 43.25923 ?  82  LYS   C O     1 
ATOM   3339 C  CB    . LYS   C 2 83  ? 77.88100 -19.61700 22.81800  1.000 40.36239 ?  82  LYS   C CB    1 
ATOM   3340 C  CG    . LYS   C 2 83  ? 76.81400 -18.63700 23.26800  1.000 44.14744 ?  82  LYS   C CG    1 
ATOM   3341 C  CD    . LYS   C 2 83  ? 76.25500 -18.99400 24.65300  1.000 46.18300 ?  82  LYS   C CD    1 
ATOM   3342 C  CE    . LYS   C 2 83  ? 75.26100 -17.93800 25.14100  1.000 45.00951 ?  82  LYS   C CE    1 
ATOM   3343 N  NZ    . LYS   C 2 83  ? 74.24000 -17.64200 24.09200  1.000 52.24743 ?  82  LYS   C NZ    1 
ATOM   3344 N  N     . PHE   C 2 84  ? 80.21300 -21.73800 23.33100  1.000 34.77805 ?  83  PHE   C N     1 
ATOM   3345 C  CA    . PHE   C 2 84  ? 81.15400 -22.67600 22.73900  1.000 33.59776 ?  83  PHE   C CA    1 
ATOM   3346 C  C     . PHE   C 2 84  ? 80.44300 -23.96700 22.36200  1.000 33.25439 ?  83  PHE   C C     1 
ATOM   3347 O  O     . PHE   C 2 84  ? 79.28600 -24.21100 22.73200  1.000 31.46943 ?  83  PHE   C O     1 
ATOM   3348 C  CB    . PHE   C 2 84  ? 82.38700 -22.93000 23.62800  1.000 32.24799 ?  83  PHE   C CB    1 
ATOM   3349 C  CG    . PHE   C 2 84  ? 82.09900 -23.59900 24.96200  1.000 34.36236 ?  83  PHE   C CG    1 
ATOM   3350 C  CD1   . PHE   C 2 84  ? 81.54000 -22.88600 26.00300  1.000 29.63106 ?  83  PHE   C CD1   1 
ATOM   3351 C  CD2   . PHE   C 2 84  ? 82.46700 -24.92200 25.17600  1.000 35.55034 ?  83  PHE   C CD2   1 
ATOM   3352 C  CE1   . PHE   C 2 84  ? 81.31200 -23.49800 27.26600  1.000 32.82202 ?  83  PHE   C CE1   1 
ATOM   3353 C  CE2   . PHE   C 2 84  ? 82.24900 -25.54600 26.41300  1.000 30.56746 ?  83  PHE   C CE2   1 
ATOM   3354 C  CZ    . PHE   C 2 84  ? 81.66100 -24.82100 27.45700  1.000 29.92964 ?  83  PHE   C CZ    1 
ATOM   3355 N  N     . GLU   C 2 85  ? 81.16500 -24.77800 21.58800  1.000 34.37756 ?  84  GLU   C N     1 
ATOM   3356 C  CA    . GLU   C 2 85  ? 80.62200 -25.93400 20.90200  1.000 34.71129 ?  84  GLU   C CA    1 
ATOM   3357 C  C     . GLU   C 2 85  ? 80.38100 -27.08700 21.87700  1.000 34.37362 ?  84  GLU   C C     1 
ATOM   3358 O  O     . GLU   C 2 85  ? 80.98000 -27.15900 22.95700  1.000 29.65672 ?  84  GLU   C O     1 
ATOM   3359 C  CB    . GLU   C 2 85  ? 81.57300 -26.36700 19.78300  1.000 35.88325 ?  84  GLU   C CB    1 
ATOM   3360 C  CG    . GLU   C 2 85  ? 82.93600 -26.84800 20.30100  1.000 43.48414 ?  84  GLU   C CG    1 
ATOM   3361 C  CD    . GLU   C 2 85  ? 83.84500 -25.71500 20.81700  1.000 48.32641 ?  84  GLU   C CD    1 
ATOM   3362 O  OE1   . GLU   C 2 85  ? 83.61300 -24.52100 20.47800  1.000 42.25379 ?  84  GLU   C OE1   1 
ATOM   3363 O  OE2   . GLU   C 2 85  ? 84.79100 -26.03000 21.57900  1.000 56.97898 -1 84  GLU   C OE2   1 
ATOM   3364 N  N     . ASP   C 2 86  ? 79.46700 -27.98000 21.48900  1.000 31.31004 ?  85  ASP   C N     1 
ATOM   3365 C  CA    . ASP   C 2 86  ? 79.26600 -29.24200 22.21500  1.000 28.14327 ?  85  ASP   C CA    1 
ATOM   3366 C  C     . ASP   C 2 86  ? 80.50200 -30.10500 22.02200  1.000 33.31946 ?  85  ASP   C C     1 
ATOM   3367 O  O     . ASP   C 2 86  ? 80.83800 -30.49900 20.89600  1.000 31.15165 ?  85  ASP   C O     1 
ATOM   3368 C  CB    . ASP   C 2 86  ? 77.99500 -29.95300 21.73000  1.000 28.69817 ?  85  ASP   C CB    1 
ATOM   3369 C  CG    . ASP   C 2 86  ? 76.74900 -29.15000 22.00300  1.000 30.04169 ?  85  ASP   C CG    1 
ATOM   3370 O  OD1   . ASP   C 2 86  ? 76.65200 -28.62500 23.12200  1.000 29.11561 ?  85  ASP   C OD1   1 
ATOM   3371 O  OD2   . ASP   C 2 86  ? 75.84900 -29.04100 21.12000  1.000 31.65671 -1 85  ASP   C OD2   1 
ATOM   3372 N  N     . GLU   C 2 87  ? 81.23200 -30.33100 23.10800  1.000 29.92950 ?  86  GLU   C N     1 
ATOM   3373 C  CA    . GLU   C 2 87  ? 82.54300 -30.95500 22.98900  1.000 27.55890 ?  86  GLU   C CA    1 
ATOM   3374 C  C     . GLU   C 2 87  ? 82.42000 -32.40000 22.51900  1.000 31.11385 ?  86  GLU   C C     1 
ATOM   3375 O  O     . GLU   C 2 87  ? 83.09900 -32.81800 21.57000  1.000 30.06178 ?  86  GLU   C O     1 
ATOM   3376 C  CB    . GLU   C 2 87  ? 83.28900 -30.86800 24.31700  1.000 27.23524 ?  86  GLU   C CB    1 
ATOM   3377 C  CG    . GLU   C 2 87  ? 84.71700 -31.32300 24.24100  1.000 31.69325 ?  86  GLU   C CG    1 
ATOM   3378 C  CD    . GLU   C 2 87  ? 85.52400 -30.97100 25.49200  1.000 33.55285 ?  86  GLU   C CD    1 
ATOM   3379 O  OE1   . GLU   C 2 87  ? 84.89700 -30.54100 26.48000  1.000 32.25476 ?  86  GLU   C OE1   1 
ATOM   3380 O  OE2   . GLU   C 2 87  ? 86.77800 -31.14700 25.49400  1.000 33.95261 -1 86  GLU   C OE2   1 
ATOM   3381 N  N     . ASN   C 2 88  ? 81.58300 -33.18200 23.19000  1.000 29.34192 ?  87  ASN   C N     1 
ATOM   3382 C  CA    . ASN   C 2 88  ? 81.22700 -34.52500 22.75000  1.000 28.72147 ?  87  ASN   C CA    1 
ATOM   3383 C  C     . ASN   C 2 88  ? 80.05800 -34.97400 23.61800  1.000 26.56413 ?  87  ASN   C C     1 
ATOM   3384 O  O     . ASN   C 2 88  ? 79.68100 -34.29000 24.57500  1.000 26.01717 ?  87  ASN   C O     1 
ATOM   3385 C  CB    . ASN   C 2 88  ? 82.40100 -35.50400 22.84300  1.000 28.71243 ?  87  ASN   C CB    1 
ATOM   3386 C  CG    . ASN   C 2 88  ? 82.91500 -35.66900 24.27200  1.000 27.11725 ?  87  ASN   C CG    1 
ATOM   3387 O  OD1   . ASN   C 2 88  ? 82.17300 -36.11500 25.18600  1.000 27.27951 ?  87  ASN   C OD1   1 
ATOM   3388 N  ND2   . ASN   C 2 88  ? 84.19600 -35.35300 24.47800  1.000 27.50169 ?  87  ASN   C ND2   1 
ATOM   3389 N  N     . PHE   C 2 89  ? 79.49700 -36.13700 23.28900  1.000 26.61648 ?  88  PHE   C N     1 
ATOM   3390 C  CA    . PHE   C 2 89  ? 78.43500 -36.72600 24.10900  1.000 26.04269 ?  88  PHE   C CA    1 
ATOM   3391 C  C     . PHE   C 2 89  ? 78.83500 -38.11000 24.61000  1.000 25.97248 ?  88  PHE   C C     1 
ATOM   3392 O  O     . PHE   C 2 89  ? 78.00900 -39.02700 24.69500  1.000 25.85510 ?  88  PHE   C O     1 
ATOM   3393 C  CB    . PHE   C 2 89  ? 77.12000 -36.76600 23.32700  1.000 28.28998 ?  88  PHE   C CB    1 
ATOM   3394 C  CG    . PHE   C 2 89  ? 76.62200 -35.40100 22.90100  1.000 27.24146 ?  88  PHE   C CG    1 
ATOM   3395 C  CD1   . PHE   C 2 89  ? 76.10200 -34.49900 23.84400  1.000 25.45827 ?  88  PHE   C CD1   1 
ATOM   3396 C  CD2   . PHE   C 2 89  ? 76.71900 -34.98800 21.56600  1.000 30.72496 ?  88  PHE   C CD2   1 
ATOM   3397 C  CE1   . PHE   C 2 89  ? 75.64900 -33.24400 23.45700  1.000 27.06528 ?  88  PHE   C CE1   1 
ATOM   3398 C  CE2   . PHE   C 2 89  ? 76.26000 -33.73400 21.18100  1.000 31.99734 ?  88  PHE   C CE2   1 
ATOM   3399 C  CZ    . PHE   C 2 89  ? 75.72700 -32.86400 22.11300  1.000 30.14312 ?  88  PHE   C CZ    1 
ATOM   3400 N  N     . ILE   C 2 90  ? 80.09800 -38.25700 25.02200  1.000 26.09660 ?  89  ILE   C N     1 
ATOM   3401 C  CA    . ILE   C 2 90  ? 80.56200 -39.54000 25.56700  1.000 27.11055 ?  89  ILE   C CA    1 
ATOM   3402 C  C     . ILE   C 2 90  ? 79.75100 -39.94100 26.79800  1.000 29.72314 ?  89  ILE   C C     1 
ATOM   3403 O  O     . ILE   C 2 90  ? 79.35700 -41.10900 26.95100  1.000 27.52309 ?  89  ILE   C O     1 
ATOM   3404 C  CB    . ILE   C 2 90  ? 82.06200 -39.47200 25.90400  1.000 26.51265 ?  89  ILE   C CB    1 
ATOM   3405 C  CG1   . ILE   C 2 90  ? 82.89500 -39.31300 24.62400  1.000 27.05958 ?  89  ILE   C CG1   1 
ATOM   3406 C  CG2   . ILE   C 2 90  ? 82.47800 -40.70500 26.67800  1.000 26.16661 ?  89  ILE   C CG2   1 
ATOM   3407 C  CD1   . ILE   C 2 90  ? 84.31500 -38.96100 24.92700  1.000 27.31308 ?  89  ILE   C CD1   1 
ATOM   3408 N  N     . LEU   C 2 91  ? 79.51200 -38.99200 27.70400  1.000 25.01548 ?  90  LEU   C N     1 
ATOM   3409 C  CA    . LEU   C 2 91  ? 78.88300 -39.28500 28.98900  1.000 25.45281 ?  90  LEU   C CA    1 
ATOM   3410 C  C     . LEU   C 2 91  ? 77.37300 -39.07800 28.91100  1.000 27.28310 ?  90  LEU   C C     1 
ATOM   3411 O  O     . LEU   C 2 91  ? 76.88300 -38.19700 28.20000  1.000 24.08623 ?  90  LEU   C O     1 
ATOM   3412 C  CB    . LEU   C 2 91  ? 79.48200 -38.40800 30.08900  1.000 24.12660 ?  90  LEU   C CB    1 
ATOM   3413 C  CG    . LEU   C 2 91  ? 80.98100 -38.72300 30.35100  1.000 29.04691 ?  90  LEU   C CG    1 
ATOM   3414 C  CD1   . LEU   C 2 91  ? 81.62300 -37.70600 31.25400  1.000 30.64122 ?  90  LEU   C CD1   1 
ATOM   3415 C  CD2   . LEU   C 2 91  ? 81.15200 -40.13000 30.95200  1.000 31.63695 ?  90  LEU   C CD2   1 
ATOM   3416 N  N     . LYS   C 2 92  ? 76.63500 -39.91100 29.65100  1.000 26.22384 ?  91  LYS   C N     1 
ATOM   3417 C  CA    . LYS   C 2 92  ? 75.18400 -39.95400 29.60700  1.000 25.78304 ?  91  LYS   C CA    1 
ATOM   3418 C  C     . LYS   C 2 92  ? 74.57800 -39.47400 30.93000  1.000 24.64278 ?  91  LYS   C C     1 
ATOM   3419 O  O     . LYS   C 2 92  ? 75.25800 -39.36000 31.96300  1.000 26.47665 ?  91  LYS   C O     1 
ATOM   3420 C  CB    . LYS   C 2 92  ? 74.69300 -41.37200 29.25800  1.000 28.55222 ?  91  LYS   C CB    1 
ATOM   3421 C  CG    . LYS   C 2 92  ? 75.32600 -41.93000 27.94100  1.000 29.48258 ?  91  LYS   C CG    1 
ATOM   3422 C  CD    . LYS   C 2 92  ? 75.04700 -41.03500 26.71500  1.000 33.42202 ?  91  LYS   C CD    1 
ATOM   3423 C  CE    . LYS   C 2 92  ? 75.74900 -41.62400 25.44500  1.000 36.01112 ?  91  LYS   C CE    1 
ATOM   3424 N  NZ    . LYS   C 2 92  ? 75.82700 -40.65100 24.31300  1.000 40.66586 ?  91  LYS   C NZ    1 
ATOM   3425 N  N     . HIS   C 2 93  ? 73.28800 -39.13900 30.87500  1.000 23.31432 ?  92  HIS   C N     1 
ATOM   3426 C  CA    . HIS   C 2 93  ? 72.54200 -38.66600 32.05300  1.000 22.68927 ?  92  HIS   C CA    1 
ATOM   3427 C  C     . HIS   C 2 93  ? 72.00200 -39.92200 32.71600  1.000 24.79812 ?  92  HIS   C C     1 
ATOM   3428 O  O     . HIS   C 2 93  ? 70.89900 -40.38600 32.40800  1.000 27.93127 ?  92  HIS   C O     1 
ATOM   3429 C  CB    . HIS   C 2 93  ? 71.41500 -37.70200 31.65600  1.000 23.38817 ?  92  HIS   C CB    1 
ATOM   3430 C  CG    . HIS   C 2 93  ? 71.87800 -36.43900 30.97000  1.000 24.92933 ?  92  HIS   C CG    1 
ATOM   3431 N  ND1   . HIS   C 2 93  ? 72.24900 -36.40400 29.63700  1.000 27.38945 ?  92  HIS   C ND1   1 
ATOM   3432 C  CD2   . HIS   C 2 93  ? 72.00200 -35.16500 31.42900  1.000 23.10302 ?  92  HIS   C CD2   1 
ATOM   3433 C  CE1   . HIS   C 2 93  ? 72.60400 -35.17000 29.31000  1.000 24.29525 ?  92  HIS   C CE1   1 
ATOM   3434 N  NE2   . HIS   C 2 93  ? 72.46700 -34.39800 30.37700  1.000 22.91068 ?  92  HIS   C NE2   1 
ATOM   3435 N  N     . THR   C 2 94  ? 72.79300 -40.51500 33.60100  1.000 23.44956 ?  93  THR   C N     1 
ATOM   3436 C  CA    . THR   C 2 94  ? 72.47900 -41.86200 34.06900  1.000 24.90281 ?  93  THR   C CA    1 
ATOM   3437 C  C     . THR   C 2 94  ? 71.72600 -41.89800 35.39400  1.000 29.32464 ?  93  THR   C C     1 
ATOM   3438 O  O     . THR   C 2 94  ? 71.30000 -42.98700 35.80100  1.000 29.43945 ?  93  THR   C O     1 
ATOM   3439 C  CB    . THR   C 2 94  ? 73.77600 -42.65600 34.24500  1.000 26.76352 ?  93  THR   C CB    1 
ATOM   3440 O  OG1   . THR   C 2 94  ? 74.63900 -41.91000 35.09900  1.000 30.29136 ?  93  THR   C OG1   1 
ATOM   3441 C  CG2   . THR   C 2 94  ? 74.47500 -42.88400 32.91800  1.000 28.77312 ?  93  THR   C CG2   1 
ATOM   3442 N  N     . GLY   C 2 95  ? 71.62800 -40.77400 36.11300  1.000 26.85679 ?  94  GLY   C N     1 
ATOM   3443 C  CA    . GLY   C 2 95  ? 71.04200 -40.76700 37.43900  1.000 31.53426 ?  94  GLY   C CA    1 
ATOM   3444 C  C     . GLY   C 2 95  ? 71.27800 -39.49700 38.23400  1.000 23.76253 ?  94  GLY   C C     1 
ATOM   3445 O  O     . GLY   C 2 95  ? 71.87000 -38.52000 37.75000  1.000 24.41558 ?  94  GLY   C O     1 
ATOM   3446 N  N     . PRO   C 2 96  ? 70.81400 -39.49000 39.48900  1.000 23.44023 ?  95  PRO   C N     1 
ATOM   3447 C  CA    . PRO   C 2 96  ? 71.05700 -38.34000 40.36100  1.000 23.99186 ?  95  PRO   C CA    1 
ATOM   3448 C  C     . PRO   C 2 96  ? 72.55100 -38.04900 40.47500  1.000 23.94350 ?  95  PRO   C C     1 
ATOM   3449 O  O     . PRO   C 2 96  ? 73.38200 -38.96200 40.54000  1.000 26.10094 ?  95  PRO   C O     1 
ATOM   3450 C  CB    . PRO   C 2 96  ? 70.48200 -38.77800 41.71200  1.000 24.75082 ?  95  PRO   C CB    1 
ATOM   3451 C  CG    . PRO   C 2 96  ? 69.73300 -40.01400 41.46700  1.000 26.28644 ?  95  PRO   C CG    1 
ATOM   3452 C  CD    . PRO   C 2 96  ? 70.25400 -40.64000 40.21400  1.000 28.89777 ?  95  PRO   C CD    1 
ATOM   3453 N  N     . GLY   C 2 97  ? 72.87400 -36.76600 40.52300  1.000 22.98838 ?  96  GLY   C N     1 
ATOM   3454 C  CA    . GLY   C 2 97  ? 74.23400 -36.29800 40.71800  1.000 24.24229 ?  96  GLY   C CA    1 
ATOM   3455 C  C     . GLY   C 2 97  ? 74.96600 -35.91000 39.44900  1.000 24.29961 ?  96  GLY   C C     1 
ATOM   3456 O  O     . GLY   C 2 97  ? 76.03800 -35.28600 39.53100  1.000 21.70113 ?  96  GLY   C O     1 
ATOM   3457 N  N     . ILE   C 2 98  ? 74.43100 -36.24600 38.27900  1.000 21.58940 ?  97  ILE   C N     1 
ATOM   3458 C  CA    . ILE   C 2 98  ? 75.08600 -35.86900 37.02500  1.000 21.07208 ?  97  ILE   C CA    1 
ATOM   3459 C  C     . ILE   C 2 98  ? 75.07700 -34.34900 36.87500  1.000 21.09759 ?  97  ILE   C C     1 
ATOM   3460 O  O     . ILE   C 2 98  ? 74.06400 -33.68200 37.10600  1.000 20.89737 ?  97  ILE   C O     1 
ATOM   3461 C  CB    . ILE   C 2 98  ? 74.38000 -36.55100 35.83600  1.000 22.61285 ?  97  ILE   C CB    1 
ATOM   3462 C  CG1   . ILE   C 2 98  ? 74.61700 -38.07400 35.79800  1.000 24.71148 ?  97  ILE   C CG1   1 
ATOM   3463 C  CG2   . ILE   C 2 98  ? 74.72400 -35.89100 34.50900  1.000 25.36739 ?  97  ILE   C CG2   1 
ATOM   3464 C  CD1   . ILE   C 2 98  ? 76.06200 -38.51900 35.49900  1.000 27.61186 ?  97  ILE   C CD1   1 
ATOM   3465 N  N     . LEU   C 2 99  ? 76.20300 -33.80400 36.44400  1.000 21.38299 ?  98  LEU   C N     1 
ATOM   3466 C  CA    . LEU   C 2 99  ? 76.42100 -32.38900 36.17600  1.000 21.50777 ?  98  LEU   C CA    1 
ATOM   3467 C  C     . LEU   C 2 99  ? 76.55400 -32.18700 34.66900  1.000 21.88249 ?  98  LEU   C C     1 
ATOM   3468 O  O     . LEU   C 2 99  ? 77.42200 -32.80200 34.03300  1.000 22.21071 ?  98  LEU   C O     1 
ATOM   3469 C  CB    . LEU   C 2 99  ? 77.70100 -31.94800 36.88500  1.000 21.63161 ?  98  LEU   C CB    1 
ATOM   3470 C  CG    . LEU   C 2 99  ? 78.10500 -30.47900 36.76300  1.000 21.81654 ?  98  LEU   C CG    1 
ATOM   3471 C  CD1   . LEU   C 2 99  ? 77.03000 -29.55900 37.36900  1.000 21.50990 ?  98  LEU   C CD1   1 
ATOM   3472 C  CD2   . LEU   C 2 99  ? 79.51400 -30.23700 37.44000  1.000 23.09029 ?  98  LEU   C CD2   1 
ATOM   3473 N  N     . SER   C 2 100 ? 75.70400 -31.32700 34.09900  1.000 21.86289 ?  99  SER   C N     1 
ATOM   3474 C  CA    . SER   C 2 100 ? 75.58800 -31.24400 32.64400  1.000 22.20846 ?  99  SER   C CA    1 
ATOM   3475 C  C     . SER   C 2 100 ? 75.32800 -29.78900 32.23600  1.000 22.27672 ?  99  SER   C C     1 
ATOM   3476 O  O     . SER   C 2 100 ? 74.87600 -28.97100 33.03200  1.000 21.99421 ?  99  SER   C O     1 
ATOM   3477 C  CB    . SER   C 2 100 ? 74.46400 -32.20000 32.18000  1.000 22.11695 ?  99  SER   C CB    1 
ATOM   3478 O  OG    . SER   C 2 100 ? 74.28100 -32.14600 30.78600  1.000 22.47767 ?  99  SER   C OG    1 
ATOM   3479 N  N     . MET   C 2 101 ? 75.64100 -29.45400 30.99100  1.000 22.68864 ?  100 MET   C N     1 
ATOM   3480 C  CA    . MET   C 2 101 ? 75.47800 -28.07900 30.53500  1.000 22.80096 ?  100 MET   C CA    1 
ATOM   3481 C  C     . MET   C 2 101 ? 74.04700 -27.79400 30.07100  1.000 22.60865 ?  100 MET   C C     1 
ATOM   3482 O  O     . MET   C 2 101 ? 73.49000 -28.53000 29.24600  1.000 22.72687 ?  100 MET   C O     1 
ATOM   3483 C  CB    . MET   C 2 101 ? 76.44000 -27.79100 29.37000  1.000 23.38394 ?  100 MET   C CB    1 
ATOM   3484 C  CG    . MET   C 2 101 ? 77.90700 -27.78800 29.73700  1.000 24.34278 ?  100 MET   C CG    1 
ATOM   3485 S  SD    . MET   C 2 101 ? 78.25300 -26.55500 31.03500  1.000 26.53301 ?  100 MET   C SD    1 
ATOM   3486 C  CE    . MET   C 2 101 ? 78.11400 -25.02200 30.09900  1.000 26.78419 ?  100 MET   C CE    1 
ATOM   3487 N  N     . ALA   C 2 102 ? 73.50200 -26.67500 30.51500  1.000 22.37997 ?  101 ALA   C N     1 
ATOM   3488 C  CA    . ALA   C 2 102 ? 72.29700 -26.09900 29.90100  1.000 22.60964 ?  101 ALA   C CA    1 
ATOM   3489 C  C     . ALA   C 2 102 ? 72.67000 -25.40500 28.59200  1.000 24.70396 ?  101 ALA   C C     1 
ATOM   3490 O  O     . ALA   C 2 102 ? 73.81400 -25.00600 28.37700  1.000 25.97159 ?  101 ALA   C O     1 
ATOM   3491 C  CB    . ALA   C 2 102 ? 71.61500 -25.10200 30.85200  1.000 22.48246 ?  101 ALA   C CB    1 
ATOM   3492 N  N     . ASN   C 2 103 ? 71.70300 -25.27900 27.69000  1.000 22.97691 ?  102 ASN   C N     1 
ATOM   3493 C  CA    . ASN   C 2 103 ? 72.01700 -24.60100 26.42800  1.000 24.27883 ?  102 ASN   C CA    1 
ATOM   3494 C  C     . ASN   C 2 103 ? 70.73500 -24.14900 25.74400  1.000 27.17114 ?  102 ASN   C C     1 
ATOM   3495 O  O     . ASN   C 2 103 ? 69.62000 -24.44000 26.19800  1.000 26.19362 ?  102 ASN   C O     1 
ATOM   3496 C  CB    . ASN   C 2 103 ? 72.84700 -25.50000 25.51300  1.000 23.74493 ?  102 ASN   C CB    1 
ATOM   3497 C  CG    . ASN   C 2 103 ? 72.12100 -26.77900 25.13700  1.000 23.72939 ?  102 ASN   C CG    1 
ATOM   3498 O  OD1   . ASN   C 2 103 ? 70.99400 -26.75000 24.66700  1.000 29.27223 ?  102 ASN   C OD1   1 
ATOM   3499 N  ND2   . ASN   C 2 103 ? 72.77400 -27.91200 25.35700  1.000 24.83291 ?  102 ASN   C ND2   1 
ATOM   3500 N  N     . ALA   C 2 104 ? 70.91300 -23.43000 24.63000  1.000 29.02833 ?  103 ALA   C N     1 
ATOM   3501 C  CA    . ALA   C 2 104 ? 69.81100 -22.91400 23.82000  1.000 34.89909 ?  103 ALA   C CA    1 
ATOM   3502 C  C     . ALA   C 2 104 ? 69.74800 -23.62900 22.47100  1.000 38.37294 ?  103 ALA   C C     1 
ATOM   3503 O  O     . ALA   C 2 104 ? 69.36600 -23.04200 21.45500  1.000 40.94440 ?  103 ALA   C O     1 
ATOM   3504 C  CB    . ALA   C 2 104 ? 69.94400 -21.40400 23.61900  1.000 35.75860 ?  103 ALA   C CB    1 
ATOM   3505 N  N     . GLY   C 2 105 ? 70.10200 -24.90100 22.45500  1.000 29.77507 ?  104 GLY   C N     1 
ATOM   3506 C  CA    . GLY   C 2 105 ? 70.28800 -25.61800 21.22500  1.000 30.38546 ?  104 GLY   C CA    1 
ATOM   3507 C  C     . GLY   C 2 105 ? 71.74300 -25.94200 20.98000  1.000 36.13690 ?  104 GLY   C C     1 
ATOM   3508 O  O     . GLY   C 2 105 ? 72.63100 -25.58800 21.77300  1.000 31.37725 ?  104 GLY   C O     1 
ATOM   3509 N  N     . PRO   C 2 106 ? 72.01700 -26.59000 19.84000  1.000 33.43331 ?  105 PRO   C N     1 
ATOM   3510 C  CA    . PRO   C 2 106 ? 73.36900 -27.08800 19.56200  1.000 32.02183 ?  105 PRO   C CA    1 
ATOM   3511 C  C     . PRO   C 2 106 ? 74.43200 -25.99500 19.60400  1.000 32.47501 ?  105 PRO   C C     1 
ATOM   3512 O  O     . PRO   C 2 106 ? 74.23000 -24.88700 19.10500  1.000 32.89362 ?  105 PRO   C O     1 
ATOM   3513 C  CB    . PRO   C 2 106 ? 73.24000 -27.66700 18.14300  1.000 34.62316 ?  105 PRO   C CB    1 
ATOM   3514 C  CG    . PRO   C 2 106 ? 71.81000 -28.06000 18.04000  1.000 38.66374 ?  105 PRO   C CG    1 
ATOM   3515 C  CD    . PRO   C 2 106 ? 71.03200 -27.05600 18.84800  1.000 33.09820 ?  105 PRO   C CD    1 
ATOM   3516 N  N     . ASN   C 2 107 ? 75.58000 -26.34500 20.20000  1.000 31.09885 ?  106 ASN   C N     1 
ATOM   3517 C  CA    . ASN   C 2 107 ? 76.78400 -25.51000 20.25700  1.000 30.14286 ?  106 ASN   C CA    1 
ATOM   3518 C  C     . ASN   C 2 107 ? 76.50600 -24.12900 20.84400  1.000 30.64278 ?  106 ASN   C C     1 
ATOM   3519 O  O     . ASN   C 2 107 ? 77.00200 -23.12200 20.33700  1.000 32.90071 ?  106 ASN   C O     1 
ATOM   3520 C  CB    . ASN   C 2 107 ? 77.43700 -25.36700 18.86800  1.000 33.96318 ?  106 ASN   C CB    1 
ATOM   3521 C  CG    . ASN   C 2 107 ? 77.68800 -26.70100 18.20400  1.000 37.45171 ?  106 ASN   C CG    1 
ATOM   3522 O  OD1   . ASN   C 2 107 ? 78.24200 -27.61400 18.81500  1.000 31.96336 ?  106 ASN   C OD1   1 
ATOM   3523 N  ND2   . ASN   C 2 107 ? 77.26200 -26.83300 16.94400  1.000 44.04892 ?  106 ASN   C ND2   1 
ATOM   3524 N  N     . THR   C 2 108 ? 75.74000 -24.06700 21.94100  1.000 29.18021 ?  107 THR   C N     1 
ATOM   3525 C  CA    . THR   C 2 108 ? 75.47500 -22.78700 22.60400  1.000 32.91961 ?  107 THR   C CA    1 
ATOM   3526 C  C     . THR   C 2 108 ? 75.75300 -22.87100 24.10900  1.000 28.71309 ?  107 THR   C C     1 
ATOM   3527 O  O     . THR   C 2 108 ? 75.02900 -22.28100 24.91500  1.000 30.62087 ?  107 THR   C O     1 
ATOM   3528 C  CB    . THR   C 2 108 ? 74.04100 -22.28800 22.35300  1.000 35.09289 ?  107 THR   C CB    1 
ATOM   3529 O  OG1   . THR   C 2 108 ? 73.08500 -23.24700 22.81400  1.000 29.65445 ?  107 THR   C OG1   1 
ATOM   3530 C  CG2   . THR   C 2 108 ? 73.78800 -22.04800 20.87000  1.000 34.97161 ?  107 THR   C CG2   1 
ATOM   3531 N  N     . ASN   C 2 109 ? 76.80800 -23.58400 24.51200  1.000 28.00252 ?  108 ASN   C N     1 
ATOM   3532 C  CA    . ASN   C 2 109 ? 77.18000 -23.62800 25.92800  1.000 28.46089 ?  108 ASN   C CA    1 
ATOM   3533 C  C     . ASN   C 2 109 ? 77.76900 -22.29700 26.39000  1.000 34.88575 ?  108 ASN   C C     1 
ATOM   3534 O  O     . ASN   C 2 109 ? 78.61000 -21.68900 25.71000  1.000 31.97002 ?  108 ASN   C O     1 
ATOM   3535 C  CB    . ASN   C 2 109 ? 78.18600 -24.73400 26.19600  1.000 28.26197 ?  108 ASN   C CB    1 
ATOM   3536 C  CG    . ASN   C 2 109 ? 77.71400 -26.07300 25.70400  1.000 27.91588 ?  108 ASN   C CG    1 
ATOM   3537 O  OD1   . ASN   C 2 109 ? 76.88700 -26.70000 26.33300  1.000 29.26207 ?  108 ASN   C OD1   1 
ATOM   3538 N  ND2   . ASN   C 2 109 ? 78.20600 -26.48500 24.52900  1.000 27.42724 ?  108 ASN   C ND2   1 
ATOM   3539 N  N     . GLY   C 2 110 ? 77.32700 -21.84600 27.57000  1.000 28.09069 ?  109 GLY   C N     1 
ATOM   3540 C  CA    . GLY   C 2 110 ? 77.93800 -20.68500 28.17100  1.000 30.49464 ?  109 GLY   C CA    1 
ATOM   3541 C  C     . GLY   C 2 110 ? 78.40700 -21.00000 29.57300  1.000 24.61739 ?  109 GLY   C C     1 
ATOM   3542 O  O     . GLY   C 2 110 ? 79.46900 -21.58900 29.76800  1.000 27.71185 ?  109 GLY   C O     1 
ATOM   3543 N  N     . SER   C 2 111 ? 77.59400 -20.63400 30.56700  1.000 27.05690 ?  110 SER   C N     1 
ATOM   3544 C  CA    . SER   C 2 111 ? 77.88500 -21.00900 31.93900  1.000 27.32352 ?  110 SER   C CA    1 
ATOM   3545 C  C     . SER   C 2 111 ? 76.74800 -21.73600 32.65000  1.000 26.95757 ?  110 SER   C C     1 
ATOM   3546 O  O     . SER   C 2 111 ? 76.99200 -22.31000 33.71200  1.000 25.87879 ?  110 SER   C O     1 
ATOM   3547 C  CB    . SER   C 2 111 ? 78.24900 -19.77000 32.77400  1.000 29.23786 ?  110 SER   C CB    1 
ATOM   3548 O  OG    . SER   C 2 111 ? 77.17300 -18.86100 32.77200  1.000 28.76929 ?  110 SER   C OG    1 
ATOM   3549 N  N     . GLN   C 2 112 ? 75.52500 -21.72400 32.12800  1.000 26.03513 ?  111 GLN   C N     1 
ATOM   3550 C  CA    . GLN   C 2 112 ? 74.44400 -22.38300 32.85200  1.000 22.60786 ?  111 GLN   C CA    1 
ATOM   3551 C  C     . GLN   C 2 112 ? 74.62200 -23.90800 32.81700  1.000 23.74537 ?  111 GLN   C C     1 
ATOM   3552 O  O     . GLN   C 2 112 ? 75.08800 -24.47400 31.83300  1.000 23.57429 ?  111 GLN   C O     1 
ATOM   3553 C  CB    . GLN   C 2 112 ? 73.10000 -21.97500 32.27700  1.000 24.19006 ?  111 GLN   C CB    1 
ATOM   3554 C  CG    . GLN   C 2 112 ? 72.70000 -20.53000 32.59600  1.000 25.87382 ?  111 GLN   C CG    1 
ATOM   3555 C  CD    . GLN   C 2 112 ? 71.23400 -20.29000 32.37300  1.000 27.55179 ?  111 GLN   C CD    1 
ATOM   3556 O  OE1   . GLN   C 2 112 ? 70.40200 -21.15100 32.67700  1.000 24.28021 ?  111 GLN   C OE1   1 
ATOM   3557 N  NE2   . GLN   C 2 112 ? 70.89400 -19.10600 31.82900  1.000 26.80232 ?  111 GLN   C NE2   1 
ATOM   3558 N  N     . PHE   C 2 113 ? 74.31000 -24.51800 33.95600  1.000 21.83752 ?  112 PHE   C N     1 
ATOM   3559 C  CA    . PHE   C 2 113 ? 74.48100 -25.97200 34.12200  1.000 21.76683 ?  112 PHE   C CA    1 
ATOM   3560 C  C     . PHE   C 2 113 ? 73.32200 -26.48900 34.94300  1.000 21.33449 ?  112 PHE   C C     1 
ATOM   3561 O  O     . PHE   C 2 113 ? 72.55800 -25.69100 35.49300  1.000 21.11548 ?  112 PHE   C O     1 
ATOM   3562 C  CB    . PHE   C 2 113 ? 75.75600 -26.21300 34.92700  1.000 21.88413 ?  112 PHE   C CB    1 
ATOM   3563 C  CG    . PHE   C 2 113 ? 75.71100 -25.59000 36.31500  1.000 21.65535 ?  112 PHE   C CG    1 
ATOM   3564 C  CD1   . PHE   C 2 113 ? 76.06900 -24.26400 36.51400  1.000 23.58609 ?  112 PHE   C CD1   1 
ATOM   3565 C  CD2   . PHE   C 2 113 ? 75.28300 -26.32400 37.41400  1.000 22.35052 ?  112 PHE   C CD2   1 
ATOM   3566 C  CE1   . PHE   C 2 113 ? 75.99800 -23.69500 37.77300  1.000 27.72850 ?  112 PHE   C CE1   1 
ATOM   3567 C  CE2   . PHE   C 2 113 ? 75.21100 -25.74600 38.66800  1.000 24.67871 ?  112 PHE   C CE2   1 
ATOM   3568 C  CZ    . PHE   C 2 113 ? 75.56900 -24.43400 38.84300  1.000 25.29528 ?  112 PHE   C CZ    1 
ATOM   3569 N  N     . PHE   C 2 114 ? 73.20800 -27.80200 35.02500  1.000 21.25181 ?  113 PHE   C N     1 
ATOM   3570 C  CA    . PHE   C 2 114 ? 72.18600 -28.38900 35.88000  1.000 20.89368 ?  113 PHE   C CA    1 
ATOM   3571 C  C     . PHE   C 2 114 ? 72.74900 -29.62800 36.54900  1.000 20.84015 ?  113 PHE   C C     1 
ATOM   3572 O  O     . PHE   C 2 114 ? 73.59100 -30.34300 35.99300  1.000 21.07209 ?  113 PHE   C O     1 
ATOM   3573 C  CB    . PHE   C 2 114 ? 70.86500 -28.68700 35.12100  1.000 20.82333 ?  113 PHE   C CB    1 
ATOM   3574 C  CG    . PHE   C 2 114 ? 70.99700 -29.66800 33.98700  1.000 21.07560 ?  113 PHE   C CG    1 
ATOM   3575 C  CD1   . PHE   C 2 114 ? 71.54500 -29.28200 32.75900  1.000 21.43441 ?  113 PHE   C CD1   1 
ATOM   3576 C  CD2   . PHE   C 2 114 ? 70.53500 -30.97000 34.14200  1.000 20.99755 ?  113 PHE   C CD2   1 
ATOM   3577 C  CE1   . PHE   C 2 114 ? 71.65800 -30.20800 31.70900  1.000 21.72539 ?  113 PHE   C CE1   1 
ATOM   3578 C  CE2   . PHE   C 2 114 ? 70.60600 -31.88500 33.09200  1.000 21.27318 ?  113 PHE   C CE2   1 
ATOM   3579 C  CZ    . PHE   C 2 114 ? 71.17600 -31.51000 31.87600  1.000 21.64330 ?  113 PHE   C CZ    1 
ATOM   3580 N  N     . ILE   C 2 115 ? 72.25900 -29.87400 37.76600  1.000 20.55226 ?  114 ILE   C N     1 
ATOM   3581 C  CA    . ILE   C 2 115 ? 72.57700 -31.09000 38.50500  1.000 20.45894 ?  114 ILE   C CA    1 
ATOM   3582 C  C     . ILE   C 2 115 ? 71.31900 -31.92800 38.51100  1.000 20.28860 ?  114 ILE   C C     1 
ATOM   3583 O  O     . ILE   C 2 115 ? 70.28100 -31.46000 38.98200  1.000 20.10463 ?  114 ILE   C O     1 
ATOM   3584 C  CB    . ILE   C 2 115 ? 72.99000 -30.80000 39.94800  1.000 20.31684 ?  114 ILE   C CB    1 
ATOM   3585 C  CG1   . ILE   C 2 115 ? 73.99700 -29.63900 40.01200  1.000 22.19233 ?  114 ILE   C CG1   1 
ATOM   3586 C  CG2   . ILE   C 2 115 ? 73.40400 -32.12200 40.60100  1.000 20.82708 ?  114 ILE   C CG2   1 
ATOM   3587 C  CD1   . ILE   C 2 115 ? 74.09400 -28.96100 41.43000  1.000 24.43580 ?  114 ILE   C CD1   1 
ATOM   3588 N  N     . CYS   C 2 116 ? 71.39700 -33.13700 37.96700  1.000 20.39209 ?  115 CYS   C N     1 
ATOM   3589 C  CA    . CYS   C 2 116 ? 70.22100 -34.00100 37.93500  1.000 20.29741 ?  115 CYS   C CA    1 
ATOM   3590 C  C     . CYS   C 2 116 ? 69.93200 -34.55200 39.31700  1.000 22.36305 ?  115 CYS   C C     1 
ATOM   3591 O  O     . CYS   C 2 116 ? 70.85200 -34.85900 40.07700  1.000 22.35760 ?  115 CYS   C O     1 
ATOM   3592 C  CB    . CYS   C 2 116 ? 70.43700 -35.20000 37.01200  1.000 20.52465 ?  115 CYS   C CB    1 
ATOM   3593 S  SG    . CYS   C 2 116 ? 70.81400 -34.80100 35.28900  1.000 26.56565 ?  115 CYS   C SG    1 
ATOM   3594 N  N     . THR   C 2 117 ? 68.64200 -34.68000 39.63500  1.000 23.76137 ?  116 THR   C N     1 
ATOM   3595 C  CA    . THR   C 2 117 ? 68.22500 -35.39800 40.83600  1.000 24.17778 ?  116 THR   C CA    1 
ATOM   3596 C  C     . THR   C 2 117 ? 67.55900 -36.72000 40.49800  1.000 25.11599 ?  116 THR   C C     1 
ATOM   3597 O  O     . THR   C 2 117 ? 67.09600 -37.44200 41.39100  1.000 26.51159 ?  116 THR   C O     1 
ATOM   3598 C  CB    . THR   C 2 117 ? 67.32500 -34.49800 41.67100  1.000 26.19277 ?  116 THR   C CB    1 
ATOM   3599 O  OG1   . THR   C 2 117 ? 66.17500 -34.13300 40.88700  1.000 23.13001 ?  116 THR   C OG1   1 
ATOM   3600 C  CG2   . THR   C 2 117 ? 68.11300 -33.23900 42.02200  1.000 25.90926 ?  116 THR   C CG2   1 
ATOM   3601 N  N     . ALA   C 2 118 ? 67.55500 -37.08200 39.22500  1.000 22.97225 ?  117 ALA   C N     1 
ATOM   3602 C  CA    . ALA   C 2 118 ? 66.97200 -38.32400 38.76400  1.000 23.64071 ?  117 ALA   C CA    1 
ATOM   3603 C  C     . ALA   C 2 118 ? 67.60400 -38.62100 37.42000  1.000 25.34171 ?  117 ALA   C C     1 
ATOM   3604 O  O     . ALA   C 2 118 ? 68.32100 -37.79000 36.86400  1.000 24.89430 ?  117 ALA   C O     1 
ATOM   3605 C  CB    . ALA   C 2 118 ? 65.44800 -38.22200 38.63400  1.000 28.23273 ?  117 ALA   C CB    1 
ATOM   3606 N  N     . LYS   C 2 119 ? 67.34300 -39.80800 36.90400  1.000 25.30512 ?  118 LYS   C N     1 
ATOM   3607 C  CA    . LYS   C 2 119 ? 67.82500 -40.14300 35.56800  1.000 27.27761 ?  118 LYS   C CA    1 
ATOM   3608 C  C     . LYS   C 2 119 ? 67.02900 -39.36300 34.52600  1.000 30.11836 ?  118 LYS   C C     1 
ATOM   3609 O  O     . LYS   C 2 119 ? 65.79000 -39.38900 34.53600  1.000 29.19864 ?  118 LYS   C O     1 
ATOM   3610 C  CB    . LYS   C 2 119 ? 67.67800 -41.64100 35.34600  1.000 33.10590 ?  118 LYS   C CB    1 
ATOM   3611 C  CG    . LYS   C 2 119 ? 68.15400 -42.15300 34.03200  1.000 31.19048 ?  118 LYS   C CG    1 
ATOM   3612 C  CD    . LYS   C 2 119 ? 68.20700 -43.66900 34.10300  1.000 39.12255 ?  118 LYS   C CD    1 
ATOM   3613 C  CE    . LYS   C 2 119 ? 67.60900 -44.29300 32.85300  1.000 43.21455 ?  118 LYS   C CE    1 
ATOM   3614 N  NZ    . LYS   C 2 119 ? 68.45200 -45.44300 32.39600  1.000 50.85710 ?  118 LYS   C NZ    1 
ATOM   3615 N  N     . THR   C 2 120 ? 67.73400 -38.66100 33.62700  1.000 26.47783 ?  119 THR   C N     1 
ATOM   3616 C  CA    . THR   C 2 120 ? 67.10000 -37.80800 32.60100  1.000 26.64307 ?  119 THR   C CA    1 
ATOM   3617 C  C     . THR   C 2 120 ? 67.65000 -38.21100 31.23600  1.000 27.48373 ?  119 THR   C C     1 
ATOM   3618 O  O     . THR   C 2 120 ? 68.31300 -37.42100 30.54300  1.000 26.34559 ?  119 THR   C O     1 
ATOM   3619 C  CB    . THR   C 2 120 ? 67.34500 -36.31400 32.85200  1.000 25.35294 ?  119 THR   C CB    1 
ATOM   3620 O  OG1   . THR   C 2 120 ? 68.75600 -36.07100 32.87000  1.000 26.12748 ?  119 THR   C OG1   1 
ATOM   3621 C  CG2   . THR   C 2 120 ? 66.73000 -35.87600 34.17200  1.000 21.99958 ?  119 THR   C CG2   1 
ATOM   3622 N  N     . GLU   C 2 121 ? 67.30800 -39.42700 30.82600  1.000 27.76176 ?  120 GLU   C N     1 
ATOM   3623 C  CA    . GLU   C 2 121 ? 67.92900 -40.02400 29.65800  1.000 31.17093 ?  120 GLU   C CA    1 
ATOM   3624 C  C     . GLU   C 2 121 ? 67.56900 -39.29000 28.36800  1.000 29.19363 ?  120 GLU   C C     1 
ATOM   3625 O  O     . GLU   C 2 121 ? 68.36700 -39.29200 27.43700  1.000 30.06678 ?  120 GLU   C O     1 
ATOM   3626 C  CB    . GLU   C 2 121 ? 67.53700 -41.49900 29.58800  1.000 34.60402 ?  120 GLU   C CB    1 
ATOM   3627 C  CG    . GLU   C 2 121 ? 66.05200 -41.75000 29.24000  1.000 40.19765 ?  120 GLU   C CG    1 
ATOM   3628 C  CD    . GLU   C 2 121 ? 65.05200 -41.51800 30.38500  1.000 41.02152 ?  120 GLU   C CD    1 
ATOM   3629 O  OE1   . GLU   C 2 121 ? 65.44500 -41.36500 31.57400  1.000 35.92668 ?  120 GLU   C OE1   1 
ATOM   3630 O  OE2   . GLU   C 2 121 ? 63.83300 -41.49800 30.07900  1.000 51.22503 -1 120 GLU   C OE2   1 
ATOM   3631 N  N     . TRP   C 2 122 ? 66.40700 -38.63500 28.30600  1.000 31.78994 ?  121 TRP   C N     1 
ATOM   3632 C  CA    . TRP   C 2 122 ? 65.99300 -37.93800 27.08600  1.000 30.13579 ?  121 TRP   C CA    1 
ATOM   3633 C  C     . TRP   C 2 122 ? 66.88400 -36.73100 26.77700  1.000 29.17461 ?  121 TRP   C C     1 
ATOM   3634 O  O     . TRP   C 2 122 ? 66.83900 -36.20400 25.66100  1.000 31.93920 ?  121 TRP   C O     1 
ATOM   3635 C  CB    . TRP   C 2 122 ? 64.52000 -37.50500 27.20100  1.000 29.83319 ?  121 TRP   C CB    1 
ATOM   3636 C  CG    . TRP   C 2 122 ? 64.23900 -36.47400 28.27700  1.000 29.60510 ?  121 TRP   C CG    1 
ATOM   3637 C  CD1   . TRP   C 2 122 ? 64.19700 -35.11700 28.12500  1.000 31.22591 ?  121 TRP   C CD1   1 
ATOM   3638 C  CD2   . TRP   C 2 122 ? 63.99400 -36.72700 29.67100  1.000 30.17148 ?  121 TRP   C CD2   1 
ATOM   3639 N  NE1   . TRP   C 2 122 ? 63.93500 -34.51100 29.33100  1.000 28.28009 ?  121 TRP   C NE1   1 
ATOM   3640 C  CE2   . TRP   C 2 122 ? 63.80900 -35.47500 30.29700  1.000 33.36187 ?  121 TRP   C CE2   1 
ATOM   3641 C  CE3   . TRP   C 2 122 ? 63.89600 -37.89100 30.44600  1.000 31.71971 ?  121 TRP   C CE3   1 
ATOM   3642 C  CZ2   . TRP   C 2 122 ? 63.52900 -35.35500 31.66000  1.000 32.28587 ?  121 TRP   C CZ2   1 
ATOM   3643 C  CZ3   . TRP   C 2 122 ? 63.63000 -37.76600 31.80800  1.000 31.38142 ?  121 TRP   C CZ3   1 
ATOM   3644 C  CH2   . TRP   C 2 122 ? 63.44600 -36.50600 32.39500  1.000 36.24929 ?  121 TRP   C CH2   1 
ATOM   3645 N  N     . LEU   C 2 123 ? 67.66500 -36.25500 27.74900  1.000 27.27041 ?  122 LEU   C N     1 
ATOM   3646 C  CA    . LEU   C 2 123 ? 68.61200 -35.17900 27.47800  1.000 28.79073 ?  122 LEU   C CA    1 
ATOM   3647 C  C     . LEU   C 2 123 ? 69.88600 -35.67800 26.81100  1.000 27.50714 ?  122 LEU   C C     1 
ATOM   3648 O  O     . LEU   C 2 123 ? 70.70400 -34.85900 26.37200  1.000 29.11383 ?  122 LEU   C O     1 
ATOM   3649 C  CB    . LEU   C 2 123 ? 68.93300 -34.45600 28.80000  1.000 26.85069 ?  122 LEU   C CB    1 
ATOM   3650 C  CG    . LEU   C 2 123 ? 67.68600 -33.83400 29.46300  1.000 28.34127 ?  122 LEU   C CG    1 
ATOM   3651 C  CD1   . LEU   C 2 123 ? 67.99100 -33.29600 30.87400  1.000 27.45969 ?  122 LEU   C CD1   1 
ATOM   3652 C  CD2   . LEU   C 2 123 ? 67.04200 -32.73700 28.57400  1.000 23.60043 ?  122 LEU   C CD2   1 
ATOM   3653 N  N     . ASP   C 2 124 ? 70.06300 -36.99300 26.71400  1.000 27.38447 ?  123 ASP   C N     1 
ATOM   3654 C  CA    . ASP   C 2 124 ? 71.26100 -37.56700 26.12000  1.000 30.90707 ?  123 ASP   C CA    1 
ATOM   3655 C  C     . ASP   C 2 124 ? 71.42100 -37.08600 24.68300  1.000 36.73382 ?  123 ASP   C C     1 
ATOM   3656 O  O     . ASP   C 2 124 ? 70.45800 -37.06400 23.89900  1.000 36.79239 ?  123 ASP   C O     1 
ATOM   3657 C  CB    . ASP   C 2 124 ? 71.21700 -39.09700 26.17000  1.000 32.36449 ?  123 ASP   C CB    1 
ATOM   3658 C  CG    . ASP   C 2 124 ? 71.56000 -39.65900 27.55100  1.000 32.26632 ?  123 ASP   C CG    1 
ATOM   3659 O  OD1   . ASP   C 2 124 ? 71.86700 -38.86300 28.47200  1.000 29.05446 ?  123 ASP   C OD1   1 
ATOM   3660 O  OD2   . ASP   C 2 124 ? 71.51400 -40.90800 27.72600  1.000 31.07117 -1 123 ASP   C OD2   1 
ATOM   3661 N  N     . GLY   C 2 125 ? 72.62900 -36.63700 24.36500  1.000 32.38927 ?  124 GLY   C N     1 
ATOM   3662 C  CA    . GLY   C 2 125 ? 72.92500 -36.10400 23.04300  1.000 34.35519 ?  124 GLY   C CA    1 
ATOM   3663 C  C     . GLY   C 2 125 ? 72.42800 -34.69200 22.79800  1.000 34.90516 ?  124 GLY   C C     1 
ATOM   3664 O  O     . GLY   C 2 125 ? 72.66400 -34.14800 21.70500  1.000 42.08987 ?  124 GLY   C O     1 
ATOM   3665 N  N     . LYS   C 2 126 ? 71.73100 -34.08000 23.75200  1.000 31.59100 ?  125 LYS   C N     1 
ATOM   3666 C  CA    . LYS   C 2 126 ? 71.33900 -32.68000 23.63500  1.000 33.09508 ?  125 LYS   C CA    1 
ATOM   3667 C  C     . LYS   C 2 126 ? 72.09100 -31.77400 24.61100  1.000 32.95989 ?  125 LYS   C C     1 
ATOM   3668 O  O     . LYS   C 2 126 ? 72.11700 -30.55000 24.41200  1.000 33.33564 ?  125 LYS   C O     1 
ATOM   3669 C  CB    . LYS   C 2 126 ? 69.82300 -32.51500 23.84800  1.000 36.85696 ?  125 LYS   C CB    1 
ATOM   3670 C  CG    . LYS   C 2 126 ? 68.95100 -32.86300 22.62200  1.000 37.90530 ?  125 LYS   C CG    1 
ATOM   3671 C  CD    . LYS   C 2 126 ? 68.60100 -34.35400 22.54800  1.000 45.74558 ?  125 LYS   C CD    1 
ATOM   3672 C  CE    . LYS   C 2 126 ? 67.91400 -34.70300 21.20100  1.000 51.51972 ?  125 LYS   C CE    1 
ATOM   3673 N  NZ    . LYS   C 2 126 ? 67.62400 -36.16500 20.98300  1.000 52.39871 ?  125 LYS   C NZ    1 
ATOM   3674 N  N     . HIS   C 2 127 ? 72.70500 -32.35300 25.64100  1.000 27.66000 ?  126 HIS   C N     1 
ATOM   3675 C  CA    . HIS   C 2 127 ? 73.39100 -31.62700 26.70300  1.000 23.98366 ?  126 HIS   C CA    1 
ATOM   3676 C  C     . HIS   C 2 127 ? 74.68000 -32.35700 27.01300  1.000 25.08377 ?  126 HIS   C C     1 
ATOM   3677 O  O     . HIS   C 2 127 ? 74.67200 -33.58000 27.16500  1.000 27.34867 ?  126 HIS   C O     1 
ATOM   3678 C  CB    . HIS   C 2 127 ? 72.51300 -31.55500 27.94500  1.000 23.02370 ?  126 HIS   C CB    1 
ATOM   3679 C  CG    . HIS   C 2 127 ? 71.25500 -30.79100 27.70500  1.000 22.84850 ?  126 HIS   C CG    1 
ATOM   3680 N  ND1   . HIS   C 2 127 ? 71.15400 -29.43800 27.95200  1.000 22.69194 ?  126 HIS   C ND1   1 
ATOM   3681 C  CD2   . HIS   C 2 127 ? 70.09600 -31.15500 27.10900  1.000 23.77743 ?  126 HIS   C CD2   1 
ATOM   3682 C  CE1   . HIS   C 2 127 ? 69.95700 -29.01600 27.57400  1.000 26.86102 ?  126 HIS   C CE1   1 
ATOM   3683 N  NE2   . HIS   C 2 127 ? 69.29100 -30.04000 27.07500  1.000 26.79496 ?  126 HIS   C NE2   1 
ATOM   3684 N  N     . VAL   C 2 128 ? 75.78800 -31.62800 27.07100  1.000 23.99131 ?  127 VAL   C N     1 
ATOM   3685 C  CA    . VAL   C 2 128 ? 77.08800 -32.23300 27.36400  1.000 24.20198 ?  127 VAL   C CA    1 
ATOM   3686 C  C     . VAL   C 2 128 ? 77.22200 -32.51600 28.86600  1.000 23.71046 ?  127 VAL   C C     1 
ATOM   3687 O  O     . VAL   C 2 128 ? 77.24500 -31.59100 29.69200  1.000 23.43803 ?  127 VAL   C O     1 
ATOM   3688 C  CB    . VAL   C 2 128 ? 78.22500 -31.32900 26.87600  1.000 24.65635 ?  127 VAL   C CB    1 
ATOM   3689 C  CG1   . VAL   C 2 128 ? 79.55400 -31.92200 27.21900  1.000 24.88925 ?  127 VAL   C CG1   1 
ATOM   3690 C  CG2   . VAL   C 2 128 ? 78.09600 -31.10700 25.35700  1.000 27.29469 ?  127 VAL   C CG2   1 
ATOM   3691 N  N     . VAL   C 2 129 ? 77.32300 -33.80000 29.21200  1.000 23.63461 ?  128 VAL   C N     1 
ATOM   3692 C  CA    . VAL   C 2 129 ? 77.61000 -34.21100 30.58900  1.000 23.26378 ?  128 VAL   C CA    1 
ATOM   3693 C  C     . VAL   C 2 129 ? 79.10500 -34.09100 30.83500  1.000 23.50909 ?  128 VAL   C C     1 
ATOM   3694 O  O     . VAL   C 2 129 ? 79.90900 -34.54900 30.02100  1.000 23.97679 ?  128 VAL   C O     1 
ATOM   3695 C  CB    . VAL   C 2 129 ? 77.13800 -35.65200 30.84700  1.000 23.09161 ?  128 VAL   C CB    1 
ATOM   3696 C  CG1   . VAL   C 2 129 ? 77.62600 -36.11100 32.24700  1.000 22.75717 ?  128 VAL   C CG1   1 
ATOM   3697 C  CG2   . VAL   C 2 129 ? 75.62300 -35.72500 30.69800  1.000 22.85542 ?  128 VAL   C CG2   1 
ATOM   3698 N  N     . PHE   C 2 130 ? 79.48800 -33.52100 31.98400  1.000 23.24645 ?  129 PHE   C N     1 
ATOM   3699 C  CA    . PHE   C 2 130 ? 80.90200 -33.27100 32.22300  1.000 23.53998 ?  129 PHE   C CA    1 
ATOM   3700 C  C     . PHE   C 2 130 ? 81.30600 -33.46000 33.68100  1.000 23.21286 ?  129 PHE   C C     1 
ATOM   3701 O  O     . PHE   C 2 130 ? 82.48400 -33.27900 34.00300  1.000 24.93293 ?  129 PHE   C O     1 
ATOM   3702 C  CB    . PHE   C 2 130 ? 81.30900 -31.84100 31.73000  1.000 23.85293 ?  129 PHE   C CB    1 
ATOM   3703 C  CG    . PHE   C 2 130 ? 80.66700 -30.73000 32.50000  1.000 23.58115 ?  129 PHE   C CG    1 
ATOM   3704 C  CD1   . PHE   C 2 130 ? 79.37200 -30.29700 32.20900  1.000 23.24267 ?  129 PHE   C CD1   1 
ATOM   3705 C  CD2   . PHE   C 2 130 ? 81.34400 -30.13300 33.56500  1.000 25.62515 ?  129 PHE   C CD2   1 
ATOM   3706 C  CE1   . PHE   C 2 130 ? 78.77400 -29.30700 32.97400  1.000 22.92107 ?  129 PHE   C CE1   1 
ATOM   3707 C  CE2   . PHE   C 2 130 ? 80.75000 -29.13400 34.32400  1.000 23.13243 ?  129 PHE   C CE2   1 
ATOM   3708 C  CZ    . PHE   C 2 130 ? 79.48400 -28.70500 34.02100  1.000 23.41649 ?  129 PHE   C CZ    1 
ATOM   3709 N  N     . GLY   C 2 131 ? 80.40700 -33.87900 34.56200  1.000 23.04168 ?  130 GLY   C N     1 
ATOM   3710 C  CA    . GLY   C 2 131 ? 80.87000 -34.07400 35.92700  1.000 23.05448 ?  130 GLY   C CA    1 
ATOM   3711 C  C     . GLY   C 2 131 ? 79.84300 -34.84400 36.72800  1.000 22.06715 ?  130 GLY   C C     1 
ATOM   3712 O  O     . GLY   C 2 131 ? 78.81400 -35.27800 36.20600  1.000 21.91396 ?  130 GLY   C O     1 
ATOM   3713 N  N     . LYS   C 2 132 ? 80.14100 -35.02700 38.01200  1.000 21.78960 ?  131 LYS   C N     1 
ATOM   3714 C  CA    . LYS   C 2 132 ? 79.17000 -35.64900 38.90600  1.000 21.37870 ?  131 LYS   C CA    1 
ATOM   3715 C  C     . LYS   C 2 132 ? 79.43100 -35.18300 40.33300  1.000 21.92389 ?  131 LYS   C C     1 
ATOM   3716 O  O     . LYS   C 2 132 ? 80.57400 -34.86700 40.70300  1.000 24.92242 ?  131 LYS   C O     1 
ATOM   3717 C  CB    . LYS   C 2 132 ? 79.22300 -37.17200 38.82200  1.000 24.32109 ?  131 LYS   C CB    1 
ATOM   3718 C  CG    . LYS   C 2 132 ? 80.39600 -37.81300 39.48200  1.000 32.83805 ?  131 LYS   C CG    1 
ATOM   3719 C  CD    . LYS   C 2 132 ? 80.14700 -39.33200 39.55800  1.000 41.63537 ?  131 LYS   C CD    1 
ATOM   3720 C  CE    . LYS   C 2 132 ? 81.38300 -40.12100 39.97500  1.000 42.04157 ?  131 LYS   C CE    1 
ATOM   3721 N  NZ    . LYS   C 2 132 ? 81.06900 -41.58500 40.10300  1.000 50.67449 ?  131 LYS   C NZ    1 
ATOM   3722 N  N     . VAL   C 2 133 ? 78.35200 -35.09400 41.10500  1.000 20.85257 ?  132 VAL   C N     1 
ATOM   3723 C  CA    . VAL   C 2 133 ? 78.46800 -34.81400 42.53700  1.000 22.22002 ?  132 VAL   C CA    1 
ATOM   3724 C  C     . VAL   C 2 133 ? 79.32300 -35.86900 43.21100  1.000 24.28199 ?  132 VAL   C C     1 
ATOM   3725 O  O     . VAL   C 2 133 ? 79.10600 -37.07700 43.06500  1.000 24.67364 ?  132 VAL   C O     1 
ATOM   3726 C  CB    . VAL   C 2 133 ? 77.07700 -34.73000 43.17300  1.000 22.25038 ?  132 VAL   C CB    1 
ATOM   3727 C  CG1   . VAL   C 2 133 ? 77.21900 -34.63500 44.70600  1.000 21.01438 ?  132 VAL   C CG1   1 
ATOM   3728 C  CG2   . VAL   C 2 133 ? 76.38700 -33.51200 42.64800  1.000 21.31180 ?  132 VAL   C CG2   1 
ATOM   3729 N  N     . LYS   C 2 134 ? 80.31200 -35.41000 43.95900  1.000 24.72535 ?  133 LYS   C N     1 
ATOM   3730 C  CA    . LYS   C 2 134 ? 81.17900 -36.32300 44.67600  1.000 29.99224 ?  133 LYS   C CA    1 
ATOM   3731 C  C     . LYS   C 2 134 ? 80.77400 -36.42800 46.14200  1.000 32.45044 ?  133 LYS   C C     1 
ATOM   3732 O  O     . LYS   C 2 134 ? 80.66300 -37.54100 46.66800  1.000 37.98438 ?  133 LYS   C O     1 
ATOM   3733 C  CB    . LYS   C 2 134 ? 82.63600 -35.85100 44.49500  1.000 28.84495 ?  133 LYS   C CB    1 
ATOM   3734 C  CG    . LYS   C 2 134 ? 83.71100 -36.68100 45.18500  1.000 39.69671 ?  133 LYS   C CG    1 
ATOM   3735 C  CD    . LYS   C 2 134 ? 85.08700 -36.07300 44.88400  1.000 38.49206 ?  133 LYS   C CD    1 
ATOM   3736 C  CE    . LYS   C 2 134 ? 86.22600 -36.90100 45.47100  1.000 39.20789 ?  133 LYS   C CE    1 
ATOM   3737 N  NZ    . LYS   C 2 134 ? 87.53100 -36.22400 45.20900  1.000 51.06391 ?  133 LYS   C NZ    1 
ATOM   3738 N  N     . GLU   C 2 135 ? 80.48900 -35.29100 46.77700  1.000 29.16093 ?  134 GLU   C N     1 
ATOM   3739 C  CA    . GLU   C 2 135 ? 80.02800 -35.19300 48.15900  1.000 28.85914 ?  134 GLU   C CA    1 
ATOM   3740 C  C     . GLU   C 2 135 ? 78.91900 -34.16000 48.23700  1.000 25.48481 ?  134 GLU   C C     1 
ATOM   3741 O  O     . GLU   C 2 135 ? 78.89200 -33.19700 47.46500  1.000 26.82144 ?  134 GLU   C O     1 
ATOM   3742 C  CB    . GLU   C 2 135 ? 81.15200 -34.77900 49.13200  1.000 32.14609 ?  134 GLU   C CB    1 
ATOM   3743 C  CG    . GLU   C 2 135 ? 82.26400 -35.80700 49.23700  1.000 34.57055 ?  134 GLU   C CG    1 
ATOM   3744 C  CD    . GLU   C 2 135 ? 82.11000 -36.70600 50.45800  1.000 48.03710 ?  134 GLU   C CD    1 
ATOM   3745 O  OE1   . GLU   C 2 135 ? 81.35500 -37.70800 50.37100  1.000 51.84152 ?  134 GLU   C OE1   1 
ATOM   3746 O  OE2   . GLU   C 2 135 ? 82.73700 -36.40000 51.50600  1.000 52.56643 -1 134 GLU   C OE2   1 
ATOM   3747 N  N     . GLY   C 2 136 ? 78.02600 -34.33500 49.20100  1.000 27.36507 ?  135 GLY   C N     1 
ATOM   3748 C  CA    . GLY   C 2 136 ? 76.97900 -33.36200 49.40000  1.000 28.01724 ?  135 GLY   C CA    1 
ATOM   3749 C  C     . GLY   C 2 136 ? 75.75500 -33.56700 48.54800  1.000 24.24930 ?  135 GLY   C C     1 
ATOM   3750 O  O     . GLY   C 2 136 ? 74.99700 -32.61000 48.34500  1.000 24.85859 ?  135 GLY   C O     1 
ATOM   3751 N  N     . MET   C 2 137 ? 75.52000 -34.78800 48.05400  1.000 22.85172 ?  136 MET   C N     1 
ATOM   3752 C  CA    . MET   C 2 137 ? 74.28300 -35.04000 47.34100  1.000 23.57744 ?  136 MET   C CA    1 
ATOM   3753 C  C     . MET   C 2 137 ? 73.08300 -34.78200 48.24700  1.000 25.56265 ?  136 MET   C C     1 
ATOM   3754 O  O     . MET   C 2 137 ? 72.02500 -34.38900 47.77200  1.000 22.89791 ?  136 MET   C O     1 
ATOM   3755 C  CB    . MET   C 2 137 ? 74.25900 -36.46600 46.78500  1.000 24.63078 ?  136 MET   C CB    1 
ATOM   3756 C  CG    . MET   C 2 137 ? 73.09000 -36.72600 45.78500  1.000 35.15615 ?  136 MET   C CG    1 
ATOM   3757 S  SD    . MET   C 2 137 ? 73.16400 -35.67600 44.28100  1.000 29.21130 ?  136 MET   C SD    1 
ATOM   3758 C  CE    . MET   C 2 137 ? 71.39900 -35.53200 43.84100  1.000 27.17974 ?  136 MET   C CE    1 
ATOM   3759 N  N     . ASN   C 2 138 ? 73.23500 -34.94000 49.57300  1.000 23.63194 ?  137 ASN   C N     1 
ATOM   3760 C  CA    . ASN   C 2 138 ? 72.10500 -34.63300 50.44400  1.000 25.87910 ?  137 ASN   C CA    1 
ATOM   3761 C  C     . ASN   C 2 138 ? 71.76700 -33.14400 50.42100  1.000 24.48914 ?  137 ASN   C C     1 
ATOM   3762 O  O     . ASN   C 2 138 ? 70.62800 -32.75500 50.72400  1.000 26.05096 ?  137 ASN   C O     1 
ATOM   3763 C  CB    . ASN   C 2 138 ? 72.44000 -35.05800 51.88400  1.000 28.65317 ?  137 ASN   C CB    1 
ATOM   3764 C  CG    . ASN   C 2 138 ? 73.53700 -34.17500 52.50900  1.000 26.75472 ?  137 ASN   C CG    1 
ATOM   3765 O  OD1   . ASN   C 2 138 ? 74.62200 -34.00700 51.95100  1.000 28.19675 ?  137 ASN   C OD1   1 
ATOM   3766 N  ND2   . ASN   C 2 138 ? 73.24500 -33.59600 53.65900  1.000 29.52022 ?  137 ASN   C ND2   1 
ATOM   3767 N  N     . ILE   C 2 139 ? 72.74600 -32.29800 50.09600  1.000 23.76788 ?  138 ILE   C N     1 
ATOM   3768 C  CA    . ILE   C 2 139 ? 72.49100 -30.87700 49.97100  1.000 23.45207 ?  138 ILE   C CA    1 
ATOM   3769 C  C     . ILE   C 2 139 ? 71.67600 -30.61300 48.71200  1.000 22.95623 ?  138 ILE   C C     1 
ATOM   3770 O  O     . ILE   C 2 139 ? 70.71600 -29.84300 48.72700  1.000 24.48117 ?  138 ILE   C O     1 
ATOM   3771 C  CB    . ILE   C 2 139 ? 73.82600 -30.11100 49.95500  1.000 24.14462 ?  138 ILE   C CB    1 
ATOM   3772 C  CG1   . ILE   C 2 139 ? 74.57200 -30.36000 51.26900  1.000 26.25190 ?  138 ILE   C CG1   1 
ATOM   3773 C  CG2   . ILE   C 2 139 ? 73.57600 -28.65300 49.70300  1.000 27.14952 ?  138 ILE   C CG2   1 
ATOM   3774 C  CD1   . ILE   C 2 139 ? 73.68900 -29.94800 52.49100  1.000 27.04061 ?  138 ILE   C CD1   1 
ATOM   3775 N  N     . VAL   C 2 140 ? 72.04300 -31.27100 47.61400  1.000 21.62213 ?  139 VAL   C N     1 
ATOM   3776 C  CA    . VAL   C 2 140 ? 71.26900 -31.13800 46.37600  1.000 24.02406 ?  139 VAL   C CA    1 
ATOM   3777 C  C     . VAL   C 2 140 ? 69.83400 -31.58500 46.61300  1.000 26.11251 ?  139 VAL   C C     1 
ATOM   3778 O  O     . VAL   C 2 140 ? 68.87900 -30.92200 46.18900  1.000 24.75907 ?  139 VAL   C O     1 
ATOM   3779 C  CB    . VAL   C 2 140 ? 71.94600 -31.94300 45.25000  1.000 21.88478 ?  139 VAL   C CB    1 
ATOM   3780 C  CG1   . VAL   C 2 140 ? 71.06100 -31.94600 43.98700  1.000 24.73145 ?  139 VAL   C CG1   1 
ATOM   3781 C  CG2   . VAL   C 2 140 ? 73.34800 -31.37200 44.93700  1.000 22.89768 ?  139 VAL   C CG2   1 
ATOM   3782 N  N     . GLU   C 2 141 ? 69.64700 -32.69600 47.32700  1.000 24.64560 ?  140 GLU   C N     1 
ATOM   3783 C  CA    . GLU   C 2 141 ? 68.29100 -33.12300 47.64000  1.000 26.56361 ?  140 GLU   C CA    1 
ATOM   3784 C  C     . GLU   C 2 141 ? 67.57800 -32.09000 48.50100  1.000 27.42982 ?  140 GLU   C C     1 
ATOM   3785 O  O     . GLU   C 2 141 ? 66.37300 -31.85900 48.33900  1.000 25.96490 ?  140 GLU   C O     1 
ATOM   3786 C  CB    . GLU   C 2 141 ? 68.29600 -34.48200 48.33900  1.000 26.16649 ?  140 GLU   C CB    1 
ATOM   3787 C  CG    . GLU   C 2 141 ? 68.78400 -35.64000 47.47700  1.000 26.31221 ?  140 GLU   C CG    1 
ATOM   3788 C  CD    . GLU   C 2 141 ? 69.25300 -36.83700 48.31700  1.000 44.69667 ?  140 GLU   C CD    1 
ATOM   3789 O  OE1   . GLU   C 2 141 ? 68.94900 -36.86700 49.54300  1.000 44.37821 ?  140 GLU   C OE1   1 
ATOM   3790 O  OE2   . GLU   C 2 141 ? 69.95200 -37.72800 47.76400  1.000 44.78440 -1 140 GLU   C OE2   1 
ATOM   3791 N  N     . ALA   C 2 142 ? 68.29300 -31.44600 49.42800  1.000 24.23777 ?  141 ALA   C N     1 
ATOM   3792 C  CA    . ALA   C 2 142 ? 67.59900 -30.46700 50.26200  1.000 26.67788 ?  141 ALA   C CA    1 
ATOM   3793 C  C     . ALA   C 2 142 ? 67.21100 -29.24000 49.45700  1.000 27.90278 ?  141 ALA   C C     1 
ATOM   3794 O  O     . ALA   C 2 142 ? 66.26200 -28.53400 49.81600  1.000 29.00349 ?  141 ALA   C O     1 
ATOM   3795 C  CB    . ALA   C 2 142 ? 68.47300 -30.05500 51.45600  1.000 27.03672 ?  141 ALA   C CB    1 
ATOM   3796 N  N     . MET   C 2 143 ? 67.94900 -28.96400 48.38100  1.000 25.15642 ?  142 MET   C N     1 
ATOM   3797 C  CA    . MET   C 2 143 ? 67.61600 -27.83600 47.52400  1.000 23.79446 ?  142 MET   C CA    1 
ATOM   3798 C  C     . MET   C 2 143 ? 66.25100 -28.03500 46.87600  1.000 23.70515 ?  142 MET   C C     1 
ATOM   3799 O  O     . MET   C 2 143 ? 65.54100 -27.05500 46.64500  1.000 23.43657 ?  142 MET   C O     1 
ATOM   3800 C  CB    . MET   C 2 143 ? 68.72500 -27.62700 46.47300  1.000 25.51695 ?  142 MET   C CB    1 
ATOM   3801 C  CG    . MET   C 2 143 ? 70.02700 -27.10000 47.09900  1.000 29.47965 ?  142 MET   C CG    1 
ATOM   3802 S  SD    . MET   C 2 143 ? 71.44200 -27.13100 45.99700  1.000 32.15413 ?  142 MET   C SD    1 
ATOM   3803 C  CE    . MET   C 2 143 ? 70.74700 -26.09600 44.74800  1.000 25.89572 ?  142 MET   C CE    1 
ATOM   3804 N  N     . GLU   C 2 144 ? 65.86200 -29.29700 46.61700  1.000 27.34177 ?  143 GLU   C N     1 
ATOM   3805 C  CA    . GLU   C 2 144 ? 64.57800 -29.59300 45.97800  1.000 28.51939 ?  143 GLU   C CA    1 
ATOM   3806 C  C     . GLU   C 2 144 ? 63.37500 -29.08900 46.76000  1.000 32.76125 ?  143 GLU   C C     1 
ATOM   3807 O  O     . GLU   C 2 144 ? 62.31000 -28.86900 46.17000  1.000 32.10017 ?  143 GLU   C O     1 
ATOM   3808 C  CB    . GLU   C 2 144 ? 64.41300 -31.09900 45.76800  1.000 28.77838 ?  143 GLU   C CB    1 
ATOM   3809 C  CG    . GLU   C 2 144 ? 65.24500 -31.72100 44.63400  1.000 28.60153 ?  143 GLU   C CG    1 
ATOM   3810 C  CD    . GLU   C 2 144 ? 64.64400 -33.08100 44.17300  1.000 36.18322 ?  143 GLU   C CD    1 
ATOM   3811 O  OE1   . GLU   C 2 144 ? 64.29000 -33.90500 45.04500  1.000 47.91881 ?  143 GLU   C OE1   1 
ATOM   3812 O  OE2   . GLU   C 2 144 ? 64.50900 -33.33900 42.94600  1.000 32.28001 -1 143 GLU   C OE2   1 
ATOM   3813 N  N     . ARG   C 2 145 ? 63.48600 -28.95600 48.08600  1.000 29.42841 ?  144 ARG   C N     1 
ATOM   3814 C  CA    . ARG   C 2 145 ? 62.36600 -28.48000 48.88600  1.000 31.84381 ?  144 ARG   C CA    1 
ATOM   3815 C  C     . ARG   C 2 145 ? 61.94800 -27.07600 48.51400  1.000 32.54982 ?  144 ARG   C C     1 
ATOM   3816 O  O     . ARG   C 2 145 ? 60.84300 -26.64600 48.87100  1.000 37.73418 ?  144 ARG   C O     1 
ATOM   3817 C  CB    . ARG   C 2 145 ? 62.76100 -28.49100 50.36700  1.000 31.87756 ?  144 ARG   C CB    1 
ATOM   3818 C  CG    . ARG   C 2 145 ? 63.34800 -29.80800 50.83800  1.000 36.48810 ?  144 ARG   C CG    1 
ATOM   3819 C  CD    . ARG   C 2 145 ? 64.01200 -29.62600 52.20000  1.000 39.29926 ?  144 ARG   C CD    1 
ATOM   3820 N  NE    . ARG   C 2 145 ? 64.04900 -30.88800 52.93000  1.000 43.18385 ?  144 ARG   C NE    1 
ATOM   3821 C  CZ    . ARG   C 2 145 ? 64.84500 -31.14000 53.96300  1.000 51.54404 ?  144 ARG   C CZ    1 
ATOM   3822 N  NH1   . ARG   C 2 145 ? 65.75600 -30.26500 54.36600  1.000 48.47207 ?  144 ARG   C NH1   1 
ATOM   3823 N  NH2   . ARG   C 2 145 ? 64.72400 -32.30100 54.60600  1.000 54.69209 ?  144 ARG   C NH2   1 
ATOM   3824 N  N     . PHE   C 2 146 ? 62.81900 -26.33100 47.84600  1.000 25.55217 ?  145 PHE   C N     1 
ATOM   3825 C  CA    . PHE   C 2 146 ? 62.56400 -24.94800 47.51600  1.000 26.53566 ?  145 PHE   C CA    1 
ATOM   3826 C  C     . PHE   C 2 146 ? 62.16000 -24.77900 46.06100  1.000 27.10502 ?  145 PHE   C C     1 
ATOM   3827 O  O     . PHE   C 2 146 ? 62.01900 -23.64700 45.59600  1.000 27.00999 ?  145 PHE   C O     1 
ATOM   3828 C  CB    . PHE   C 2 146 ? 63.80100 -24.09700 47.85000  1.000 29.40814 ?  145 PHE   C CB    1 
ATOM   3829 C  CG    . PHE   C 2 146 ? 64.25500 -24.27100 49.27800  1.000 31.23563 ?  145 PHE   C CG    1 
ATOM   3830 C  CD1   . PHE   C 2 146 ? 63.52900 -23.71000 50.31400  1.000 30.20383 ?  145 PHE   C CD1   1 
ATOM   3831 C  CD2   . PHE   C 2 146 ? 65.33500 -25.07800 49.58000  1.000 29.58688 ?  145 PHE   C CD2   1 
ATOM   3832 C  CE1   . PHE   C 2 146 ? 63.92100 -23.89700 51.63400  1.000 37.95240 ?  145 PHE   C CE1   1 
ATOM   3833 C  CE2   . PHE   C 2 146 ? 65.72400 -25.27400 50.91500  1.000 29.12224 ?  145 PHE   C CE2   1 
ATOM   3834 C  CZ    . PHE   C 2 146 ? 65.01500 -24.68300 51.92400  1.000 30.27298 ?  145 PHE   C CZ    1 
ATOM   3835 N  N     . GLY   C 2 147 ? 61.97400 -25.88200 45.33700  1.000 28.14696 ?  146 GLY   C N     1 
ATOM   3836 C  CA    . GLY   C 2 147 ? 61.59400 -25.83400 43.94100  1.000 25.67324 ?  146 GLY   C CA    1 
ATOM   3837 C  C     . GLY   C 2 147 ? 60.09300 -25.95800 43.75500  1.000 27.69267 ?  146 GLY   C C     1 
ATOM   3838 O  O     . GLY   C 2 147 ? 59.30100 -25.93200 44.70200  1.000 27.06353 ?  146 GLY   C O     1 
ATOM   3839 N  N     . SER   C 2 148 ? 59.69800 -26.10000 42.49600  1.000 23.77140 ?  147 SER   C N     1 
ATOM   3840 C  CA    . SER   C 2 148 ? 58.28400 -26.12700 42.16500  1.000 24.75137 ?  147 SER   C CA    1 
ATOM   3841 C  C     . SER   C 2 148 ? 58.14900 -26.71000 40.76800  1.000 26.18977 ?  147 SER   C C     1 
ATOM   3842 O  O     . SER   C 2 148 ? 59.14900 -26.90800 40.06000  1.000 24.88094 ?  147 SER   C O     1 
ATOM   3843 C  CB    . SER   C 2 148 ? 57.67100 -24.72100 42.19400  1.000 23.95249 ?  147 SER   C CB    1 
ATOM   3844 O  OG    . SER   C 2 148 ? 58.15300 -23.92600 41.10300  1.000 26.07912 ?  147 SER   C OG    1 
ATOM   3845 N  N     . ARG   C 2 149 ? 56.88800 -26.91900 40.36200  1.000 24.98303 ?  148 ARG   C N     1 
ATOM   3846 C  CA    . ARG   C 2 149 ? 56.59900 -27.56400 39.08000  1.000 26.29441 ?  148 ARG   C CA    1 
ATOM   3847 C  C     . ARG   C 2 149 ? 57.22800 -26.81400 37.91600  1.000 23.42920 ?  148 ARG   C C     1 
ATOM   3848 O  O     . ARG   C 2 149 ? 57.75700 -27.43300 36.97800  1.000 26.49427 ?  148 ARG   C O     1 
ATOM   3849 C  CB    . ARG   C 2 149 ? 55.07900 -27.67700 38.88700  1.000 29.39115 ?  148 ARG   C CB    1 
ATOM   3850 C  CG    . ARG   C 2 149 ? 54.68400 -28.36100 37.61300  1.000 31.93322 ?  148 ARG   C CG    1 
ATOM   3851 C  CD    . ARG   C 2 149 ? 53.23900 -28.87800 37.71200  1.000 34.06007 ?  148 ARG   C CD    1 
ATOM   3852 N  NE    . ARG   C 2 149 ? 52.82700 -29.38100 36.40900  1.000 34.88878 ?  148 ARG   C NE    1 
ATOM   3853 C  CZ    . ARG   C 2 149 ? 52.46400 -28.56400 35.43500  1.000 31.51745 ?  148 ARG   C CZ    1 
ATOM   3854 N  NH1   . ARG   C 2 149 ? 52.39800 -27.25700 35.64000  1.000 36.25790 ?  148 ARG   C NH1   1 
ATOM   3855 N  NH2   . ARG   C 2 149 ? 52.15100 -29.06800 34.24500  1.000 31.56747 ?  148 ARG   C NH2   1 
ATOM   3856 N  N     . ASN   C 2 150 ? 57.21400 -25.49900 37.94900  1.000 24.80235 ?  149 ASN   C N     1 
ATOM   3857 C  CA    . ASN   C 2 150 ? 57.83000 -24.76700 36.85000  1.000 27.93566 ?  149 ASN   C CA    1 
ATOM   3858 C  C     . ASN   C 2 150 ? 59.24400 -24.28800 37.15500  1.000 29.12050 ?  149 ASN   C C     1 
ATOM   3859 O  O     . ASN   C 2 150 ? 59.85600 -23.63800 36.30000  1.000 28.15143 ?  149 ASN   C O     1 
ATOM   3860 C  CB    . ASN   C 2 150 ? 56.94700 -23.58700 36.38800  1.000 29.69642 ?  149 ASN   C CB    1 
ATOM   3861 C  CG    . ASN   C 2 150 ? 57.11900 -22.30900 37.22100  1.000 38.21068 ?  149 ASN   C CG    1 
ATOM   3862 O  OD1   . ASN   C 2 150 ? 57.67800 -22.32300 38.31500  1.000 28.82721 ?  149 ASN   C OD1   1 
ATOM   3863 N  ND2   . ASN   C 2 150 ? 56.62000 -21.17900 36.68500  1.000 36.17576 ?  149 ASN   C ND2   1 
ATOM   3864 N  N     . GLY   C 2 151 ? 59.79800 -24.61000 38.33400  1.000 25.19664 ?  150 GLY   C N     1 
ATOM   3865 C  CA    . GLY   C 2 151 ? 61.17000 -24.27600 38.63900  1.000 21.55762 ?  150 GLY   C CA    1 
ATOM   3866 C  C     . GLY   C 2 151 ? 61.36000 -23.05400 39.51500  1.000 26.02169 ?  150 GLY   C C     1 
ATOM   3867 O  O     . GLY   C 2 151 ? 62.43200 -22.90000 40.12200  1.000 22.60908 ?  150 GLY   C O     1 
ATOM   3868 N  N     . LYS   C 2 152 ? 60.35900 -22.18000 39.59700  1.000 26.49238 ?  151 LYS   C N     1 
ATOM   3869 C  CA    . LYS   C 2 152 ? 60.48200 -21.01000 40.44200  1.000 28.48696 ?  151 LYS   C CA    1 
ATOM   3870 C  C     . LYS   C 2 152 ? 60.75600 -21.45100 41.87000  1.000 27.82618 ?  151 LYS   C C     1 
ATOM   3871 O  O     . LYS   C 2 152 ? 60.12300 -22.37600 42.37000  1.000 25.39955 ?  151 LYS   C O     1 
ATOM   3872 C  CB    . LYS   C 2 152 ? 59.19800 -20.17600 40.37800  1.000 33.92864 ?  151 LYS   C CB    1 
ATOM   3873 C  CG    . LYS   C 2 152 ? 59.31200 -18.97600 39.44300  1.000 41.96079 ?  151 LYS   C CG    1 
ATOM   3874 C  CD    . LYS   C 2 152 ? 59.46300 -19.38000 37.95800  1.000 47.42418 ?  151 LYS   C CD    1 
ATOM   3875 C  CE    . LYS   C 2 152 ? 59.65400 -18.15900 37.04800  1.000 46.98870 ?  151 LYS   C CE    1 
ATOM   3876 N  NZ    . LYS   C 2 152 ? 59.12800 -18.35300 35.64100  1.000 44.82944 ?  151 LYS   C NZ    1 
ATOM   3877 N  N     . THR   C 2 153 ? 61.75200 -20.83300 42.49000  1.000 28.07579 ?  152 THR   C N     1 
ATOM   3878 C  CA    . THR   C 2 153 ? 62.14200 -21.20000 43.83700  1.000 27.90704 ?  152 THR   C CA    1 
ATOM   3879 C  C     . THR   C 2 153 ? 61.39900 -20.34900 44.86300  1.000 31.25890 ?  152 THR   C C     1 
ATOM   3880 O  O     . THR   C 2 153 ? 61.12700 -19.16200 44.65100  1.000 34.12476 ?  152 THR   C O     1 
ATOM   3881 C  CB    . THR   C 2 153 ? 63.65300 -21.06600 44.05900  1.000 32.62753 ?  152 THR   C CB    1 
ATOM   3882 O  OG1   . THR   C 2 153 ? 64.05100 -19.69600 43.94400  1.000 26.73061 ?  152 THR   C OG1   1 
ATOM   3883 C  CG2   . THR   C 2 153 ? 64.41700 -21.93900 43.02800  1.000 29.70637 ?  152 THR   C CG2   1 
ATOM   3884 N  N     . SER   C 2 154 ? 61.09300 -20.97300 45.98500  1.000 29.30382 ?  153 SER   C N     1 
ATOM   3885 C  CA    . SER   C 2 154 ? 60.35600 -20.29800 47.04700  1.000 35.01827 ?  153 SER   C CA    1 
ATOM   3886 C  C     . SER   C 2 154 ? 61.26400 -19.59400 48.04300  1.000 36.52845 ?  153 SER   C C     1 
ATOM   3887 O  O     . SER   C 2 154 ? 60.76400 -18.83500 48.87800  1.000 33.51023 ?  153 SER   C O     1 
ATOM   3888 C  CB    . SER   C 2 154 ? 59.47800 -21.30300 47.78000  1.000 35.80343 ?  153 SER   C CB    1 
ATOM   3889 O  OG    . SER   C 2 154 ? 60.26900 -22.29400 48.40900  1.000 34.12115 ?  153 SER   C OG    1 
ATOM   3890 N  N     . LYS   C 2 155 ? 62.57100 -19.84600 47.98800  1.000 32.65540 ?  154 LYS   C N     1 
ATOM   3891 C  CA    . LYS   C 2 155 ? 63.57200 -19.06500 48.70300  1.000 34.98890 ?  154 LYS   C CA    1 
ATOM   3892 C  C     . LYS   C 2 155 ? 64.76700 -18.88100 47.78500  1.000 34.78946 ?  154 LYS   C C     1 
ATOM   3893 O  O     . LYS   C 2 155 ? 64.94300 -19.62500 46.81400  1.000 34.37137 ?  154 LYS   C O     1 
ATOM   3894 C  CB    . LYS   C 2 155 ? 64.01100 -19.75300 50.00200  1.000 34.43283 ?  154 LYS   C CB    1 
ATOM   3895 C  CG    . LYS   C 2 155 ? 62.87900 -19.89200 51.02500  1.000 29.98844 ?  154 LYS   C CG    1 
ATOM   3896 C  CD    . LYS   C 2 155 ? 63.39000 -20.40000 52.37200  1.000 40.60343 ?  154 LYS   C CD    1 
ATOM   3897 C  CE    . LYS   C 2 155 ? 62.25500 -20.46200 53.41300  1.000 38.49301 ?  154 LYS   C CE    1 
ATOM   3898 N  NZ    . LYS   C 2 155 ? 62.72800 -21.12600 54.66400  1.000 45.53086 ?  154 LYS   C NZ    1 
ATOM   3899 N  N     . LYS   C 2 156 ? 65.59300 -17.89500 48.09500  1.000 33.32736 ?  155 LYS   C N     1 
ATOM   3900 C  CA    . LYS   C 2 156 ? 66.73100 -17.56600 47.24300  1.000 37.29803 ?  155 LYS   C CA    1 
ATOM   3901 C  C     . LYS   C 2 156 ? 67.85900 -18.56100 47.52200  1.000 31.96399 ?  155 LYS   C C     1 
ATOM   3902 O  O     . LYS   C 2 156 ? 68.41700 -18.57700 48.61600  1.000 27.68644 ?  155 LYS   C O     1 
ATOM   3903 C  CB    . LYS   C 2 156 ? 67.17900 -16.12900 47.49900  1.000 34.70754 ?  155 LYS   C CB    1 
ATOM   3904 C  CG    . LYS   C 2 156 ? 67.99000 -15.51500 46.38700  1.000 44.21846 ?  155 LYS   C CG    1 
ATOM   3905 C  CD    . LYS   C 2 156 ? 67.26700 -15.64000 45.03000  1.000 47.29298 ?  155 LYS   C CD    1 
ATOM   3906 C  CE    . LYS   C 2 156 ? 67.92400 -14.74400 43.98400  1.000 41.39219 ?  155 LYS   C CE    1 
ATOM   3907 N  NZ    . LYS   C 2 156 ? 69.37700 -14.60500 44.30900  1.000 45.47865 ?  155 LYS   C NZ    1 
ATOM   3908 N  N     . ILE   C 2 157 ? 68.23200 -19.37300 46.53300  1.000 28.60066 ?  156 ILE   C N     1 
ATOM   3909 C  CA    . ILE   C 2 157 ? 69.22900 -20.42200 46.72000  1.000 28.23694 ?  156 ILE   C CA    1 
ATOM   3910 C  C     . ILE   C 2 157 ? 70.47700 -19.97400 45.98500  1.000 29.73447 ?  156 ILE   C C     1 
ATOM   3911 O  O     . ILE   C 2 157 ? 70.48400 -19.91100 44.75100  1.000 30.13802 ?  156 ILE   C O     1 
ATOM   3912 C  CB    . ILE   C 2 157 ? 68.76100 -21.78100 46.18100  1.000 30.51348 ?  156 ILE   C CB    1 
ATOM   3913 C  CG1   . ILE   C 2 157 ? 67.35100 -22.13100 46.67000  1.000 28.94247 ?  156 ILE   C CG1   1 
ATOM   3914 C  CG2   . ILE   C 2 157 ? 69.80000 -22.86700 46.51700  1.000 27.32848 ?  156 ILE   C CG2   1 
ATOM   3915 C  CD1   . ILE   C 2 157 ? 67.17800 -22.17400 48.19400  1.000 34.09843 ?  156 ILE   C CD1   1 
ATOM   3916 N  N     . THR   C 2 158 ? 71.54400 -19.68000 46.70700  1.000 26.64969 ?  157 THR   C N     1 
ATOM   3917 C  CA    . THR   C 2 158 ? 72.68900 -19.05000 46.07800  1.000 29.17984 ?  157 THR   C CA    1 
ATOM   3918 C  C     . THR   C 2 158 ? 73.96400 -19.84900 46.29400  1.000 28.35366 ?  157 THR   C C     1 
ATOM   3919 O  O     . THR   C 2 158 ? 74.07200 -20.68400 47.20300  1.000 28.43329 ?  157 THR   C O     1 
ATOM   3920 C  CB    . THR   C 2 158 ? 72.90700 -17.62400 46.60900  1.000 30.69085 ?  157 THR   C CB    1 
ATOM   3921 O  OG1   . THR   C 2 158 ? 73.13400 -17.67500 48.03500  1.000 29.94781 ?  157 THR   C OG1   1 
ATOM   3922 C  CG2   . THR   C 2 158 ? 71.69600 -16.72800 46.29100  1.000 32.77422 ?  157 THR   C CG2   1 
ATOM   3923 N  N     . ILE   C 2 159 ? 74.94700 -19.54800 45.43900  1.000 27.43353 ?  158 ILE   C N     1 
ATOM   3924 C  CA    . ILE   C 2 159 ? 76.30700 -20.11900 45.59600  1.000 26.49806 ?  158 ILE   C CA    1 
ATOM   3925 C  C     . ILE   C 2 159 ? 77.06500 -19.06600 46.40900  1.000 30.00092 ?  158 ILE   C C     1 
ATOM   3926 O  O     . ILE   C 2 159 ? 77.56200 -18.10500 45.82700  1.000 30.33691 ?  158 ILE   C O     1 
ATOM   3927 C  CB    . ILE   C 2 159 ? 76.96400 -20.40000 44.23800  1.000 24.28992 ?  158 ILE   C CB    1 
ATOM   3928 C  CG1   . ILE   C 2 159 ? 76.09900 -21.33400 43.39600  1.000 30.17991 ?  158 ILE   C CG1   1 
ATOM   3929 C  CG2   . ILE   C 2 159 ? 78.37800 -20.94600 44.41300  1.000 27.69979 ?  158 ILE   C CG2   1 
ATOM   3930 C  CD1   . ILE   C 2 159 ? 76.63300 -21.59800 42.00300  1.000 27.23578 ?  158 ILE   C CD1   1 
ATOM   3931 N  N     . ALA   C 2 160 ? 77.06600 -19.23900 47.72200  1.000 26.88528 ?  159 ALA   C N     1 
ATOM   3932 C  CA    . ALA   C 2 160 ? 77.67700 -18.25200 48.60300  1.000 31.93426 ?  159 ALA   C CA    1 
ATOM   3933 C  C     . ALA   C 2 160 ? 79.18700 -18.22300 48.43500  1.000 36.97083 ?  159 ALA   C C     1 
ATOM   3934 O  O     . ALA   C 2 160 ? 79.80300 -17.15500 48.55300  1.000 35.99976 ?  159 ALA   C O     1 
ATOM   3935 C  CB    . ALA   C 2 160 ? 77.29800 -18.53200 50.05200  1.000 36.31841 ?  159 ALA   C CB    1 
ATOM   3936 N  N     . ASP   C 2 161 ? 79.73900 -19.39600 48.15200  1.000 31.89541 ?  160 ASP   C N     1 
ATOM   3937 C  CA    . ASP   C 2 161 ? 81.18200 -19.48600 47.87000  1.000 36.25438 ?  160 ASP   C CA    1 
ATOM   3938 C  C     . ASP   C 2 161 ? 81.44200 -20.68900 46.96600  1.000 35.03464 ?  160 ASP   C C     1 
ATOM   3939 O  O     . ASP   C 2 161 ? 80.69400 -21.67000 47.03400  1.000 30.69812 ?  160 ASP   C O     1 
ATOM   3940 C  CB    . ASP   C 2 161 ? 82.00400 -19.56200 49.14000  1.000 34.92001 ?  160 ASP   C CB    1 
ATOM   3941 C  CG    . ASP   C 2 161 ? 83.48500 -19.25800 48.97700  1.000 42.35799 ?  160 ASP   C CG    1 
ATOM   3942 O  OD1   . ASP   C 2 161 ? 83.85400 -18.69300 47.93000  1.000 42.43379 ?  160 ASP   C OD1   1 
ATOM   3943 O  OD2   . ASP   C 2 161 ? 84.25400 -19.59300 49.89800  1.000 48.77825 -1 160 ASP   C OD2   1 
ATOM   3944 N  N     . CYS   C 2 162 ? 82.48600 -20.58500 46.16000  1.000 37.32429 ?  161 CYS   C N     1 
ATOM   3945 C  CA    . CYS   C 2 162 ? 82.87900 -21.72400 45.31300  1.000 29.87167 ?  161 CYS   C CA    1 
ATOM   3946 C  C     . CYS   C 2 162 ? 84.38500 -21.67000 45.06700  1.000 32.95751 ?  161 CYS   C C     1 
ATOM   3947 O  O     . CYS   C 2 162 ? 84.97800 -20.60100 45.20600  1.000 34.95287 ?  161 CYS   C O     1 
ATOM   3948 C  CB    . CYS   C 2 162 ? 82.15200 -21.71400 43.97800  1.000 25.70872 ?  161 CYS   C CB    1 
ATOM   3949 S  SG    . CYS   C 2 162 ? 82.03800 -20.09400 43.18900  1.000 34.47934 ?  161 CYS   C SG    1 
ATOM   3950 N  N     . GLY   C 2 163 ? 84.95600 -22.80700 44.72400  1.000 28.41683 ?  162 GLY   C N     1 
ATOM   3951 C  CA    . GLY   C 2 163 ? 86.36800 -22.83400 44.37500  1.000 29.89831 ?  162 GLY   C CA    1 
ATOM   3952 C  C     . GLY   C 2 163 ? 86.80400 -24.23000 43.99800  1.000 32.42691 ?  162 GLY   C C     1 
ATOM   3953 O  O     . GLY   C 2 163 ? 85.97900 -25.09200 43.69100  1.000 32.50808 ?  162 GLY   C O     1 
ATOM   3954 N  N     . GLN   C 2 164 ? 88.11600 -24.44600 43.98900  1.000 32.55155 ?  163 GLN   C N     1 
ATOM   3955 C  CA    . GLN   C 2 164 ? 88.68400 -25.73000 43.62500  1.000 32.09727 ?  163 GLN   C CA    1 
ATOM   3956 C  C     . GLN   C 2 164 ? 89.24800 -26.40600 44.86000  1.000 35.59150 ?  163 GLN   C C     1 
ATOM   3957 O  O     . GLN   C 2 164 ? 89.88300 -25.76100 45.69500  1.000 45.64545 ?  163 GLN   C O     1 
ATOM   3958 C  CB    . GLN   C 2 164 ? 89.77900 -25.56600 42.56300  1.000 36.45334 ?  163 GLN   C CB    1 
ATOM   3959 C  CG    . GLN   C 2 164 ? 90.39900 -26.84700 42.10700  1.000 29.72283 ?  163 GLN   C CG    1 
ATOM   3960 C  CD    . GLN   C 2 164 ? 91.15700 -26.69700 40.77800  1.000 30.96656 ?  163 GLN   C CD    1 
ATOM   3961 O  OE1   . GLN   C 2 164 ? 91.26800 -25.58700 40.21200  1.000 33.19026 ?  163 GLN   C OE1   1 
ATOM   3962 N  NE2   . GLN   C 2 164 ? 91.67200 -27.81000 40.27300  1.000 33.47120 ?  163 GLN   C NE2   1 
ATOM   3963 N  N     . LEU   C 2 165 ? 89.02300 -27.70300 44.97700  1.000 35.10948 ?  164 LEU   C N     1 
ATOM   3964 C  CA    . LEU   C 2 165 ? 89.61300 -28.44100 46.08300  1.000 40.45292 ?  164 LEU   C CA    1 
ATOM   3965 C  C     . LEU   C 2 165 ? 91.02600 -28.94200 45.71800  1.000 39.77967 ?  164 LEU   C C     1 
ATOM   3966 O  O     . LEU   C 2 165 ? 91.23000 -30.13600 45.47400  1.000 48.02135 ?  164 LEU   C O     1 
ATOM   3967 C  CB    . LEU   C 2 165 ? 88.69900 -29.59200 46.49100  1.000 40.35574 ?  164 LEU   C CB    1 
ATOM   3968 C  CG    . LEU   C 2 165 ? 87.42100 -29.03500 47.12200  1.000 41.86271 ?  164 LEU   C CG    1 
ATOM   3969 C  CD1   . LEU   C 2 165 ? 86.43700 -30.12500 47.55800  1.000 37.43626 ?  164 LEU   C CD1   1 
ATOM   3970 C  CD2   . LEU   C 2 165 ? 87.79100 -28.11800 48.29800  1.000 38.66334 ?  164 LEU   C CD2   1 
ATOM   3971 N  N     . ASN   D 2 4   ? 33.35900 54.26700  4.55400   1.000 36.69662 ?  3   ASN   D N     1 
ATOM   3972 C  CA    . ASN   D 2 4   ? 32.58500 53.05700  4.85100   1.000 37.93265 ?  3   ASN   D CA    1 
ATOM   3973 C  C     . ASN   D 2 4   ? 31.12700 53.35700  5.13600   1.000 30.36299 ?  3   ASN   D C     1 
ATOM   3974 O  O     . ASN   D 2 4   ? 30.78800 54.16100  6.00500   1.000 33.29269 ?  3   ASN   D O     1 
ATOM   3975 C  CB    . ASN   D 2 4   ? 33.16000 52.29000  6.04100   1.000 32.67275 ?  3   ASN   D CB    1 
ATOM   3976 C  CG    . ASN   D 2 4   ? 34.36800 51.47300  5.68300   1.000 34.45673 ?  3   ASN   D CG    1 
ATOM   3977 O  OD1   . ASN   D 2 4   ? 34.65600 51.22400  4.50900   1.000 35.25465 ?  3   ASN   D OD1   1 
ATOM   3978 N  ND2   . ASN   D 2 4   ? 35.08800 51.04400  6.69400   1.000 28.22200 ?  3   ASN   D ND2   1 
ATOM   3979 N  N     . PRO   D 2 5   ? 30.24800 52.69900  4.40000   1.000 30.80684 ?  4   PRO   D N     1 
ATOM   3980 C  CA    . PRO   D 2 5   ? 28.81900 52.90800  4.60300   1.000 29.54983 ?  4   PRO   D CA    1 
ATOM   3981 C  C     . PRO   D 2 5   ? 28.33400 52.32500  5.92200   1.000 30.86822 ?  4   PRO   D C     1 
ATOM   3982 O  O     . PRO   D 2 5   ? 28.92700 51.40500  6.49100   1.000 31.17730 ?  4   PRO   D O     1 
ATOM   3983 C  CB    . PRO   D 2 5   ? 28.17700 52.18600  3.41800   1.000 36.60801 ?  4   PRO   D CB    1 
ATOM   3984 C  CG    . PRO   D 2 5   ? 29.25000 51.22100  2.92800   1.000 30.78945 ?  4   PRO   D CG    1 
ATOM   3985 C  CD    . PRO   D 2 5   ? 30.55900 51.81200  3.26500   1.000 33.03142 ?  4   PRO   D CD    1 
ATOM   3986 N  N     A THR   D 2 6   ? 27.23300 52.90500  6.40200   0.500 29.71718 ?  5   THR   D N     1 
ATOM   3987 N  N     B THR   D 2 6   ? 27.24100 52.90000  6.41200   0.500 29.71551 ?  5   THR   D N     1 
ATOM   3988 C  CA    A THR   D 2 6   ? 26.51200 52.47000  7.58900   0.500 30.12007 ?  5   THR   D CA    1 
ATOM   3989 C  CA    B THR   D 2 6   ? 26.54300 52.40800  7.58800   0.500 30.10656 ?  5   THR   D CA    1 
ATOM   3990 C  C     A THR   D 2 6   ? 25.09400 52.07700  7.19800   0.500 31.33338 ?  5   THR   D C     1 
ATOM   3991 C  C     B THR   D 2 6   ? 25.10600 52.07500  7.21500   0.500 31.32880 ?  5   THR   D C     1 
ATOM   3992 O  O     A THR   D 2 6   ? 24.43800 52.78700  6.42800   0.500 31.20421 ?  5   THR   D O     1 
ATOM   3993 O  O     B THR   D 2 6   ? 24.45800 52.82000  6.47200   0.500 31.21975 ?  5   THR   D O     1 
ATOM   3994 C  CB    A THR   D 2 6   ? 26.45100 53.58800  8.64600   0.500 30.92007 ?  5   THR   D CB    1 
ATOM   3995 C  CB    B THR   D 2 6   ? 26.55000 53.44200  8.72100   0.500 30.93006 ?  5   THR   D CB    1 
ATOM   3996 O  OG1   A THR   D 2 6   ? 27.77600 54.02400  8.98300   0.500 34.33192 ?  5   THR   D OG1   1 
ATOM   3997 O  OG1   B THR   D 2 6   ? 25.81600 54.59400  8.30600   0.500 32.34763 ?  5   THR   D OG1   1 
ATOM   3998 C  CG2   A THR   D 2 6   ? 25.73000 53.10300  9.89900   0.500 29.81730 ?  5   THR   D CG2   1 
ATOM   3999 C  CG2   B THR   D 2 6   ? 27.97400 53.85800  9.07200   0.500 34.26788 ?  5   THR   D CG2   1 
ATOM   4000 N  N     . VAL   D 2 7   ? 24.61300 50.94600  7.72400   1.000 27.57323 ?  6   VAL   D N     1 
ATOM   4001 C  CA    . VAL   D 2 7   ? 23.23300 50.53200  7.51300   1.000 26.34301 ?  6   VAL   D CA    1 
ATOM   4002 C  C     . VAL   D 2 7   ? 22.62200 50.25200  8.87900   1.000 25.94817 ?  6   VAL   D C     1 
ATOM   4003 O  O     . VAL   D 2 7   ? 23.33100 50.04500  9.86800   1.000 25.43882 ?  6   VAL   D O     1 
ATOM   4004 C  CB    . VAL   D 2 7   ? 23.10000 49.29600  6.60800   1.000 30.27168 ?  6   VAL   D CB    1 
ATOM   4005 C  CG1   . VAL   D 2 7   ? 23.46300 49.66400  5.16900   1.000 30.27018 ?  6   VAL   D CG1   1 
ATOM   4006 C  CG2   . VAL   D 2 7   ? 24.01100 48.20800  7.07900   1.000 28.93201 ?  6   VAL   D CG2   1 
ATOM   4007 N  N     . PHE   D 2 8   ? 21.29000 50.22400  8.91100   1.000 26.50430 ?  7   PHE   D N     1 
ATOM   4008 C  CA    . PHE   D 2 8   ? 20.53400 49.94400  10.13400  1.000 25.59018 ?  7   PHE   D CA    1 
ATOM   4009 C  C     . PHE   D 2 8   ? 19.50400 48.86400  9.87400   1.000 28.73361 ?  7   PHE   D C     1 
ATOM   4010 O  O     . PHE   D 2 8   ? 19.03000 48.70500  8.74500   1.000 23.93854 ?  7   PHE   D O     1 
ATOM   4011 C  CB    . PHE   D 2 8   ? 19.81500 51.21200  10.66900  1.000 29.14518 ?  7   PHE   D CB    1 
ATOM   4012 C  CG    . PHE   D 2 8   ? 18.66300 51.65900  9.81700   1.000 31.10146 ?  7   PHE   D CG    1 
ATOM   4013 C  CD1   . PHE   D 2 8   ? 18.86200 52.48500  8.71900   1.000 34.90219 ?  7   PHE   D CD1   1 
ATOM   4014 C  CD2   . PHE   D 2 8   ? 17.36600 51.26300  10.12100  1.000 29.79513 ?  7   PHE   D CD2   1 
ATOM   4015 C  CE1   . PHE   D 2 8   ? 17.77100 52.89800  7.92700   1.000 33.41316 ?  7   PHE   D CE1   1 
ATOM   4016 C  CE2   . PHE   D 2 8   ? 16.27700 51.66700  9.33000   1.000 32.87725 ?  7   PHE   D CE2   1 
ATOM   4017 C  CZ    . PHE   D 2 8   ? 16.48600 52.48600  8.23800   1.000 34.53284 ?  7   PHE   D CZ    1 
ATOM   4018 N  N     . PHE   D 2 9   ? 19.17400 48.12600  10.94400  1.000 26.75362 ?  8   PHE   D N     1 
ATOM   4019 C  CA    . PHE   D 2 9   ? 18.02500 47.22800  11.03200  1.000 24.11046 ?  8   PHE   D CA    1 
ATOM   4020 C  C     . PHE   D 2 9   ? 17.15000 47.71000  12.18500  1.000 24.45371 ?  8   PHE   D C     1 
ATOM   4021 O  O     . PHE   D 2 9   ? 17.64500 47.86100  13.30100  1.000 24.55410 ?  8   PHE   D O     1 
ATOM   4022 C  CB    . PHE   D 2 9   ? 18.41700 45.78200  11.37500  1.000 25.31887 ?  8   PHE   D CB    1 
ATOM   4023 C  CG    . PHE   D 2 9   ? 19.13300 45.01200  10.30300  1.000 23.13250 ?  8   PHE   D CG    1 
ATOM   4024 C  CD1   . PHE   D 2 9   ? 19.29600 45.48800  8.99000   1.000 25.10775 ?  8   PHE   D CD1   1 
ATOM   4025 C  CD2   . PHE   D 2 9   ? 19.66900 43.76900  10.62900  1.000 26.17223 ?  8   PHE   D CD2   1 
ATOM   4026 C  CE1   . PHE   D 2 9   ? 19.98900 44.71600  8.05900   1.000 27.47542 ?  8   PHE   D CE1   1 
ATOM   4027 C  CE2   . PHE   D 2 9   ? 20.33400 42.99500  9.68900   1.000 23.70324 ?  8   PHE   D CE2   1 
ATOM   4028 C  CZ    . PHE   D 2 9   ? 20.51500 43.47100  8.41200   1.000 24.91847 ?  8   PHE   D CZ    1 
ATOM   4029 N  N     . ASP   D 2 10  ? 15.84900 47.87400  11.95800  1.000 26.18201 ?  9   ASP   D N     1 
ATOM   4030 C  CA    . ASP   D 2 10  ? 14.91600 48.00800  13.06900  1.000 29.69195 ?  9   ASP   D CA    1 
ATOM   4031 C  C     . ASP   D 2 10  ? 14.37300 46.62500  13.38800  1.000 27.29711 ?  9   ASP   D C     1 
ATOM   4032 O  O     . ASP   D 2 10  ? 13.72400 46.00600  12.54400  1.000 26.66472 ?  9   ASP   D O     1 
ATOM   4033 C  CB    . ASP   D 2 10  ? 13.78000 48.97900  12.74200  1.000 31.27118 ?  9   ASP   D CB    1 
ATOM   4034 C  CG    . ASP   D 2 10  ? 14.24700 50.43300  12.68600  1.000 33.50214 ?  9   ASP   D CG    1 
ATOM   4035 O  OD1   . ASP   D 2 10  ? 14.89400 50.91800  13.63500  1.000 36.42027 -1 9   ASP   D OD1   1 
ATOM   4036 O  OD2   . ASP   D 2 10  ? 14.00000 51.10400  11.65600  1.000 36.43267 ?  9   ASP   D OD2   1 
ATOM   4037 N  N     . ILE   D 2 11  ? 14.65400 46.13000  14.60000  1.000 24.55560 ?  10  ILE   D N     1 
ATOM   4038 C  CA    . ILE   D 2 11  ? 14.31300 44.76300  14.97400  1.000 24.00211 ?  10  ILE   D CA    1 
ATOM   4039 C  C     . ILE   D 2 11  ? 12.95200 44.74300  15.66000  1.000 25.99697 ?  10  ILE   D C     1 
ATOM   4040 O  O     . ILE   D 2 11  ? 12.65700 45.59400  16.50800  1.000 25.48737 ?  10  ILE   D O     1 
ATOM   4041 C  CB    . ILE   D 2 11  ? 15.40300 44.17200  15.88900  1.000 26.56146 ?  10  ILE   D CB    1 
ATOM   4042 C  CG1   . ILE   D 2 11  ? 16.78200 44.15300  15.17700  1.000 24.64280 ?  10  ILE   D CG1   1 
ATOM   4043 C  CG2   . ILE   D 2 11  ? 15.04200 42.78700  16.37700  1.000 23.44209 ?  10  ILE   D CG2   1 
ATOM   4044 C  CD1   . ILE   D 2 11  ? 16.84600 43.25100  13.95900  1.000 25.66034 ?  10  ILE   D CD1   1 
ATOM   4045 N  N     . ALA   D 2 12  ? 12.12700 43.75100  15.31600  1.000 23.79099 ?  11  ALA   D N     1 
ATOM   4046 C  CA    . ALA   D 2 12  ? 10.88900 43.49800  16.04000  1.000 26.88196 ?  11  ALA   D CA    1 
ATOM   4047 C  C     . ALA   D 2 12  ? 10.84900 42.06800  16.57300  1.000 26.77824 ?  11  ALA   D C     1 
ATOM   4048 O  O     . ALA   D 2 12  ? 11.47900 41.16500  16.02900  1.000 25.25424 ?  11  ALA   D O     1 
ATOM   4049 C  CB    . ALA   D 2 12  ? 9.67200  43.73000  15.13700  1.000 26.22492 ?  11  ALA   D CB    1 
ATOM   4050 N  N     . VAL   D 2 13  ? 10.06100 41.87600  17.63300  1.000 24.44494 ?  12  VAL   D N     1 
ATOM   4051 C  CA    . VAL   D 2 13  ? 9.85900  40.58500  18.29400  1.000 27.68589 ?  12  VAL   D CA    1 
ATOM   4052 C  C     . VAL   D 2 13  ? 8.36200  40.32200  18.31800  1.000 31.21883 ?  12  VAL   D C     1 
ATOM   4053 O  O     . VAL   D 2 13  ? 7.62400  41.02800  19.01500  1.000 31.05473 ?  12  VAL   D O     1 
ATOM   4054 C  CB    . VAL   D 2 13  ? 10.41400 40.58600  19.72200  1.000 27.30167 ?  12  VAL   D CB    1 
ATOM   4055 C  CG1   . VAL   D 2 13  ? 10.12700 39.24000  20.42800  1.000 27.33198 ?  12  VAL   D CG1   1 
ATOM   4056 C  CG2   . VAL   D 2 13  ? 11.90500 40.94500  19.74500  1.000 30.19087 ?  12  VAL   D CG2   1 
ATOM   4057 N  N     . ASP   D 2 14  ? 7.92100  39.29300  17.60200  1.000 30.87182 ?  13  ASP   D N     1 
ATOM   4058 C  CA    . ASP   D 2 14  ? 6.48300  39.04200  17.38300  1.000 33.96500 ?  13  ASP   D CA    1 
ATOM   4059 C  C     . ASP   D 2 14  ? 5.74200  40.31900  16.97700  1.000 38.66335 ?  13  ASP   D C     1 
ATOM   4060 O  O     . ASP   D 2 14  ? 4.60000  40.55700  17.38900  1.000 38.11838 ?  13  ASP   D O     1 
ATOM   4061 C  CB    . ASP   D 2 14  ? 5.83500  38.39800  18.61300  1.000 34.46319 ?  13  ASP   D CB    1 
ATOM   4062 C  CG    . ASP   D 2 14  ? 6.03600  36.90100  18.64300  1.000 38.51169 ?  13  ASP   D CG    1 
ATOM   4063 O  OD1   . ASP   D 2 14  ? 6.46700  36.34200  17.60600  1.000 37.28271 ?  13  ASP   D OD1   1 
ATOM   4064 O  OD2   . ASP   D 2 14  ? 5.76600  36.28100  19.69300  1.000 44.78726 -1 13  ASP   D OD2   1 
ATOM   4065 N  N     . GLY   D 2 15  ? 6.39400  41.14500  16.15500  1.000 37.12223 ?  14  GLY   D N     1 
ATOM   4066 C  CA    . GLY   D 2 15  ? 5.83000  42.40200  15.68400  1.000 37.29462 ?  14  GLY   D CA    1 
ATOM   4067 C  C     . GLY   D 2 15  ? 5.98100  43.59700  16.61400  1.000 35.27207 ?  14  GLY   D C     1 
ATOM   4068 O  O     . GLY   D 2 15  ? 5.76100  44.73100  16.16900  1.000 49.38425 ?  14  GLY   D O     1 
ATOM   4069 N  N     . GLU   D 2 16  ? 6.34800  43.39300  17.86100  1.000 34.24900 ?  15  GLU   D N     1 
ATOM   4070 C  CA    . GLU   D 2 16  ? 6.56000  44.47700  18.82900  1.000 38.38621 ?  15  GLU   D CA    1 
ATOM   4071 C  C     . GLU   D 2 16  ? 7.97200  45.02900  18.68200  1.000 39.03141 ?  15  GLU   D C     1 
ATOM   4072 O  O     . GLU   D 2 16  ? 8.93200  44.25000  18.70200  1.000 29.95337 ?  15  GLU   D O     1 
ATOM   4073 C  CB    . GLU   D 2 16  ? 6.34800  43.97100  20.24900  1.000 40.89145 ?  15  GLU   D CB    1 
ATOM   4074 C  CG    . GLU   D 2 16  ? 4.88300  43.76300  20.58200  1.000 49.47827 ?  15  GLU   D CG    1 
ATOM   4075 C  CD    . GLU   D 2 16  ? 4.05000  45.00700  20.26500  1.000 56.85530 ?  15  GLU   D CD    1 
ATOM   4076 O  OE1   . GLU   D 2 16  ? 4.46900  46.12500  20.65700  1.000 54.75270 ?  15  GLU   D OE1   1 
ATOM   4077 O  OE2   . GLU   D 2 16  ? 2.99100  44.87000  19.60300  1.000 63.43895 -1 15  GLU   D OE2   1 
ATOM   4078 N  N     . PRO   D 2 17  ? 8.14200  46.34400  18.53200  1.000 39.13966 ?  16  PRO   D N     1 
ATOM   4079 C  CA    . PRO   D 2 17  ? 9.48600  46.87700  18.26800  1.000 35.53529 ?  16  PRO   D CA    1 
ATOM   4080 C  C     . PRO   D 2 17  ? 10.42100 46.62300  19.44000  1.000 36.05920 ?  16  PRO   D C     1 
ATOM   4081 O  O     . PRO   D 2 17  ? 10.02800 46.67500  20.60800  1.000 29.16133 ?  16  PRO   D O     1 
ATOM   4082 C  CB    . PRO   D 2 17  ? 9.25000  48.37900  18.04800  1.000 39.07177 ?  16  PRO   D CB    1 
ATOM   4083 C  CG    . PRO   D 2 17  ? 7.75000  48.53600  17.82600  1.000 44.28689 ?  16  PRO   D CG    1 
ATOM   4084 C  CD    . PRO   D 2 17  ? 7.14000  47.42200  18.65200  1.000 39.91894 ?  16  PRO   D CD    1 
ATOM   4085 N  N     . LEU   D 2 18  ? 11.67200 46.30600  19.10500  1.000 26.31345 ?  17  LEU   D N     1 
ATOM   4086 C  CA    . LEU   D 2 18  ? 12.71900 46.11300  20.09000  1.000 28.88565 ?  17  LEU   D CA    1 
ATOM   4087 C  C     . LEU   D 2 18  ? 13.71400 47.25800  20.04800  1.000 25.77766 ?  17  LEU   D C     1 
ATOM   4088 O  O     . LEU   D 2 18  ? 13.95300 47.90800  21.05600  1.000 28.07956 ?  17  LEU   D O     1 
ATOM   4089 C  CB    . LEU   D 2 18  ? 13.41900 44.76700  19.84300  1.000 27.01379 ?  17  LEU   D CB    1 
ATOM   4090 C  CG    . LEU   D 2 18  ? 14.54800 44.38600  20.79400  1.000 24.59473 ?  17  LEU   D CG    1 
ATOM   4091 C  CD1   . LEU   D 2 18  ? 14.02400 44.24700  22.26500  1.000 28.09206 ?  17  LEU   D CD1   1 
ATOM   4092 C  CD2   . LEU   D 2 18  ? 15.18900 43.09700  20.30900  1.000 26.11238 ?  17  LEU   D CD2   1 
ATOM   4093 N  N     . GLY   D 2 19  ? 14.30000 47.53700  18.89400  1.000 27.04715 ?  18  GLY   D N     1 
ATOM   4094 C  CA    . GLY   D 2 19  ? 15.20200 48.66600  18.77900  1.000 23.34899 ?  18  GLY   D CA    1 
ATOM   4095 C  C     . GLY   D 2 19  ? 16.05200 48.55100  17.52600  1.000 25.27151 ?  18  GLY   D C     1 
ATOM   4096 O  O     . GLY   D 2 19  ? 15.94500 47.59900  16.75600  1.000 24.40778 ?  18  GLY   D O     1 
ATOM   4097 N  N     . ARG   D 2 20  ? 16.92200 49.53900  17.36200  1.000 28.21294 ?  19  ARG   D N     1 
ATOM   4098 C  CA    . ARG   D 2 20  ? 17.72200 49.68600  16.14900  1.000 27.04735 ?  19  ARG   D CA    1 
ATOM   4099 C  C     . ARG   D 2 20  ? 19.14400 49.19800  16.35600  1.000 24.75408 ?  19  ARG   D C     1 
ATOM   4100 O  O     . ARG   D 2 20  ? 19.81800 49.61400  17.30800  1.000 25.03722 ?  19  ARG   D O     1 
ATOM   4101 C  CB    . ARG   D 2 20  ? 17.77000 51.14400  15.70600  1.000 28.57811 ?  19  ARG   D CB    1 
ATOM   4102 C  CG    . ARG   D 2 20  ? 18.43500 51.30400  14.37400  1.000 29.13278 ?  19  ARG   D CG    1 
ATOM   4103 C  CD    . ARG   D 2 20  ? 18.23300 52.68700  13.78300  1.000 32.37193 ?  19  ARG   D CD    1 
ATOM   4104 N  NE    . ARG   D 2 20  ? 16.94400 52.80900  13.13200  1.000 36.97176 ?  19  ARG   D NE    1 
ATOM   4105 C  CZ    . ARG   D 2 20  ? 16.65300 53.75100  12.24600  1.000 40.90856 ?  19  ARG   D CZ    1 
ATOM   4106 N  NH1   . ARG   D 2 20  ? 17.55200 54.65700  11.88300  1.000 34.76746 ?  19  ARG   D NH1   1 
ATOM   4107 N  NH2   . ARG   D 2 20  ? 15.43900 53.77700  11.70300  1.000 39.79600 ?  19  ARG   D NH2   1 
ATOM   4108 N  N     . VAL   D 2 21  ? 19.63500 48.41800  15.39200  1.000 23.86497 ?  20  VAL   D N     1 
ATOM   4109 C  CA    . VAL   D 2 21  ? 21.03000 47.99800  15.33100  1.000 21.34675 ?  20  VAL   D CA    1 
ATOM   4110 C  C     . VAL   D 2 21  ? 21.63100 48.63800  14.08400  1.000 22.25273 ?  20  VAL   D C     1 
ATOM   4111 O  O     . VAL   D 2 21  ? 21.04600 48.53200  13.00300  1.000 23.47741 ?  20  VAL   D O     1 
ATOM   4112 C  CB    . VAL   D 2 21  ? 21.20500 46.47000  15.22200  1.000 24.69883 ?  20  VAL   D CB    1 
ATOM   4113 C  CG1   . VAL   D 2 21  ? 22.71100 46.14300  15.35500  1.000 24.95276 ?  20  VAL   D CG1   1 
ATOM   4114 C  CG2   . VAL   D 2 21  ? 20.36900 45.69000  16.17400  1.000 26.11969 ?  20  VAL   D CG2   1 
ATOM   4115 N  N     . SER   D 2 22  ? 22.79800 49.25700  14.22200  1.000 24.23581 ?  21  SER   D N     1 
ATOM   4116 C  CA    . SER   D 2 22  ? 23.43700 49.83700  13.05800  1.000 25.81289 ?  21  SER   D CA    1 
ATOM   4117 C  C     . SER   D 2 22  ? 24.79100 49.18000  12.83000  1.000 23.17001 ?  21  SER   D C     1 
ATOM   4118 O  O     . SER   D 2 22  ? 25.44300 48.72200  13.76900  1.000 25.88482 ?  21  SER   D O     1 
ATOM   4119 C  CB    . SER   D 2 22  ? 23.57100 51.34800  13.19200  1.000 28.76635 ?  21  SER   D CB    1 
ATOM   4120 O  OG    . SER   D 2 22  ? 24.59900 51.67500  14.08300  1.000 30.51171 ?  21  SER   D OG    1 
ATOM   4121 N  N     . PHE   D 2 23  ? 25.20500 49.12400  11.56800  1.000 23.97771 ?  22  PHE   D N     1 
ATOM   4122 C  CA    . PHE   D 2 23  ? 26.42300 48.39700  11.21800  1.000 22.36541 ?  22  PHE   D CA    1 
ATOM   4123 C  C     . PHE   D 2 23  ? 27.34800 49.27800  10.41200  1.000 24.12206 ?  22  PHE   D C     1 
ATOM   4124 O  O     . PHE   D 2 23  ? 26.88800 50.02200  9.55100   1.000 26.19073 ?  22  PHE   D O     1 
ATOM   4125 C  CB    . PHE   D 2 23  ? 26.12000 47.13800  10.34400  1.000 22.91518 ?  22  PHE   D CB    1 
ATOM   4126 C  CG    . PHE   D 2 23  ? 25.06500 46.22800  10.91400  1.000 20.71403 ?  22  PHE   D CG    1 
ATOM   4127 C  CD1   . PHE   D 2 23  ? 25.40500 45.22800  11.80200  1.000 23.16303 ?  22  PHE   D CD1   1 
ATOM   4128 C  CD2   . PHE   D 2 23  ? 23.75900 46.35000  10.51400  1.000 21.56200 ?  22  PHE   D CD2   1 
ATOM   4129 C  CE1   . PHE   D 2 23  ? 24.44800 44.38200  12.31400  1.000 23.04833 ?  22  PHE   D CE1   1 
ATOM   4130 C  CE2   . PHE   D 2 23  ? 22.77300 45.51500  11.01200  1.000 24.80618 ?  22  PHE   D CE2   1 
ATOM   4131 C  CZ    . PHE   D 2 23  ? 23.12500 44.51300  11.92800  1.000 25.84656 ?  22  PHE   D CZ    1 
ATOM   4132 N  N     . GLU   D 2 24  ? 28.64600 49.15900  10.64900  1.000 22.87643 ?  23  GLU   D N     1 
ATOM   4133 C  CA    . GLU   D 2 24  ? 29.62700 49.68800  9.70700   1.000 25.66780 ?  23  GLU   D CA    1 
ATOM   4134 C  C     . GLU   D 2 24  ? 30.04600 48.56100  8.77100   1.000 26.95480 ?  23  GLU   D C     1 
ATOM   4135 O  O     . GLU   D 2 24  ? 30.35900 47.46000  9.23400   1.000 22.97125 ?  23  GLU   D O     1 
ATOM   4136 C  CB    . GLU   D 2 24  ? 30.83700 50.24600  10.44500  1.000 27.50146 ?  23  GLU   D CB    1 
ATOM   4137 C  CG    . GLU   D 2 24  ? 31.99300 50.66100  9.51300   1.000 28.68722 ?  23  GLU   D CG    1 
ATOM   4138 C  CD    . GLU   D 2 24  ? 33.24000 51.14200  10.24600  1.000 34.87216 ?  23  GLU   D CD    1 
ATOM   4139 O  OE1   . GLU   D 2 24  ? 33.32800 51.04800  11.50400  1.000 38.56893 ?  23  GLU   D OE1   1 
ATOM   4140 O  OE2   . GLU   D 2 24  ? 34.16100 51.60000  9.54200   1.000 40.26947 -1 23  GLU   D OE2   1 
ATOM   4141 N  N     . LEU   D 2 25  ? 30.08000 48.84100  7.46900   1.000 27.75356 ?  24  LEU   D N     1 
ATOM   4142 C  CA    . LEU   D 2 25  ? 30.42200 47.86200  6.44900   1.000 25.64196 ?  24  LEU   D CA    1 
ATOM   4143 C  C     . LEU   D 2 25  ? 31.78500 48.21100  5.91200   1.000 23.59310 ?  24  LEU   D C     1 
ATOM   4144 O  O     . LEU   D 2 25  ? 32.01100 49.36300  5.53300   1.000 26.35553 ?  24  LEU   D O     1 
ATOM   4145 C  CB    . LEU   D 2 25  ? 29.41000 47.87400  5.30500   1.000 24.59340 ?  24  LEU   D CB    1 
ATOM   4146 C  CG    . LEU   D 2 25  ? 27.96400 47.71300  5.76800   1.000 23.03810 ?  24  LEU   D CG    1 
ATOM   4147 C  CD1   . LEU   D 2 25  ? 26.94500 47.74500  4.55800   1.000 24.26618 ?  24  LEU   D CD1   1 
ATOM   4148 C  CD2   . LEU   D 2 25  ? 27.84000 46.42100  6.54900   1.000 26.06435 ?  24  LEU   D CD2   1 
ATOM   4149 N  N     . PHE   D 2 26  ? 32.70200 47.24200  5.93800   1.000 25.28728 ?  25  PHE   D N     1 
ATOM   4150 C  CA    . PHE   D 2 26  ? 34.10800 47.49300  5.62400   1.000 25.67024 ?  25  PHE   D CA    1 
ATOM   4151 C  C     . PHE   D 2 26  ? 34.34200 47.50700  4.11100   1.000 24.74459 ?  25  PHE   D C     1 
ATOM   4152 O  O     . PHE   D 2 26  ? 35.05900 46.67800  3.55600   1.000 26.49090 ?  25  PHE   D O     1 
ATOM   4153 C  CB    . PHE   D 2 26  ? 34.97600 46.45100  6.30400   1.000 29.65505 ?  25  PHE   D CB    1 
ATOM   4154 C  CG    . PHE   D 2 26  ? 34.87800 46.47800  7.79600   1.000 30.37352 ?  25  PHE   D CG    1 
ATOM   4155 C  CD1   . PHE   D 2 26  ? 34.77700 47.68800  8.46500   1.000 33.27569 ?  25  PHE   D CD1   1 
ATOM   4156 C  CD2   . PHE   D 2 26  ? 34.80000 45.30100  8.52700   1.000 32.15039 ?  25  PHE   D CD2   1 
ATOM   4157 C  CE1   . PHE   D 2 26  ? 34.68100 47.73400  9.83900   1.000 33.80111 ?  25  PHE   D CE1   1 
ATOM   4158 C  CE2   . PHE   D 2 26  ? 34.70700 45.33900  9.90100   1.000 33.52186 ?  25  PHE   D CE2   1 
ATOM   4159 C  CZ    . PHE   D 2 26  ? 34.64500 46.56300  10.55800  1.000 30.95896 ?  25  PHE   D CZ    1 
ATOM   4160 N  N     . ALA   D 2 27  ? 33.71100 48.47400  3.45700   1.000 27.33244 ?  26  ALA   D N     1 
ATOM   4161 C  CA    . ALA   D 2 27  ? 33.88300 48.63400  2.01400   1.000 33.75125 ?  26  ALA   D CA    1 
ATOM   4162 C  C     . ALA   D 2 27  ? 35.34400 48.88200  1.64200   1.000 34.40096 ?  26  ALA   D C     1 
ATOM   4163 O  O     . ALA   D 2 27  ? 35.77700 48.49800  0.54600   1.000 33.00185 ?  26  ALA   D O     1 
ATOM   4164 C  CB    . ALA   D 2 27  ? 32.99800 49.77400  1.50500   1.000 34.25998 ?  26  ALA   D CB    1 
ATOM   4165 N  N     . ASP   D 2 28  ? 36.13800 49.46100  2.55900   1.000 33.24171 ?  27  ASP   D N     1 
ATOM   4166 C  CA    . ASP   D 2 28  ? 37.55200 49.67100  2.28200   1.000 33.20865 ?  27  ASP   D CA    1 
ATOM   4167 C  C     . ASP   D 2 28  ? 38.33300 48.36200  2.18100   1.000 35.00222 ?  27  ASP   D C     1 
ATOM   4168 O  O     . ASP   D 2 28  ? 39.38900 48.34700  1.54900   1.000 41.75836 ?  27  ASP   D O     1 
ATOM   4169 C  CB    . ASP   D 2 28  ? 38.17600 50.57900  3.35700   1.000 38.00188 ?  27  ASP   D CB    1 
ATOM   4170 C  CG    . ASP   D 2 28  ? 37.91700 50.08000  4.78000   1.000 42.40833 ?  27  ASP   D CG    1 
ATOM   4171 O  OD1   . ASP   D 2 28  ? 36.93600 49.32900  4.97800   1.000 38.40343 ?  27  ASP   D OD1   1 
ATOM   4172 O  OD2   . ASP   D 2 28  ? 38.68700 50.44700  5.70200   1.000 49.30985 -1 27  ASP   D OD2   1 
ATOM   4173 N  N     . LYS   D 2 29  ? 37.84000 47.25900  2.75600   1.000 32.73129 ?  28  LYS   D N     1 
ATOM   4174 C  CA    . LYS   D 2 29  ? 38.57900 46.00400  2.71400   1.000 30.49593 ?  28  LYS   D CA    1 
ATOM   4175 C  C     . LYS   D 2 29  ? 37.88400 44.89100  1.94000   1.000 30.40576 ?  28  LYS   D C     1 
ATOM   4176 O  O     . LYS   D 2 29  ? 38.58300 44.01900  1.38900   1.000 28.78284 ?  28  LYS   D O     1 
ATOM   4177 C  CB    . LYS   D 2 29  ? 38.85900 45.50300  4.14400   1.000 36.71864 ?  28  LYS   D CB    1 
ATOM   4178 C  CG    . LYS   D 2 29  ? 39.77000 46.44500  4.95000   1.000 40.54711 ?  28  LYS   D CG    1 
ATOM   4179 C  CD    . LYS   D 2 29  ? 40.95000 45.69800  5.54800   1.000 44.35136 ?  28  LYS   D CD    1 
ATOM   4180 C  CE    . LYS   D 2 29  ? 42.18300 46.57900  5.64600   1.000 44.01916 ?  28  LYS   D CE    1 
ATOM   4181 N  NZ    . LYS   D 2 29  ? 43.37900 45.76200  6.04200   1.000 51.24377 ?  28  LYS   D NZ    1 
ATOM   4182 N  N     . VAL   D 2 30  ? 36.55200 44.87800  1.90800   1.000 26.58590 ?  29  VAL   D N     1 
ATOM   4183 C  CA    . VAL   D 2 30  ? 35.76700 43.85300  1.21400   1.000 30.91322 ?  29  VAL   D CA    1 
ATOM   4184 C  C     . VAL   D 2 30  ? 34.66200 44.58600  0.46600   1.000 26.48787 ?  29  VAL   D C     1 
ATOM   4185 O  O     . VAL   D 2 30  ? 33.47700 44.52100  0.84500   1.000 25.26670 ?  29  VAL   D O     1 
ATOM   4186 C  CB    . VAL   D 2 30  ? 35.18500 42.78300  2.16800   1.000 28.52949 ?  29  VAL   D CB    1 
ATOM   4187 C  CG1   . VAL   D 2 30  ? 36.06800 41.54000  2.23400   1.000 29.70411 ?  29  VAL   D CG1   1 
ATOM   4188 C  CG2   . VAL   D 2 30  ? 34.99500 43.34600  3.53800   1.000 32.84471 ?  29  VAL   D CG2   1 
ATOM   4189 N  N     . PRO   D 2 31  ? 35.00200 45.31800  -0.59800  1.000 29.61024 ?  30  PRO   D N     1 
ATOM   4190 C  CA    . PRO   D 2 31  ? 33.99400 46.16300  -1.23600  1.000 26.64050 ?  30  PRO   D CA    1 
ATOM   4191 C  C     . PRO   D 2 31  ? 32.83700 45.39100  -1.83700  1.000 27.05982 ?  30  PRO   D C     1 
ATOM   4192 O  O     . PRO   D 2 31  ? 31.69500 45.83900  -1.74700  1.000 28.54219 ?  30  PRO   D O     1 
ATOM   4193 C  CB    . PRO   D 2 31  ? 34.80100 46.90700  -2.32400  1.000 25.25301 ?  30  PRO   D CB    1 
ATOM   4194 C  CG    . PRO   D 2 31  ? 36.04600 46.04100  -2.56600  1.000 31.33436 ?  30  PRO   D CG    1 
ATOM   4195 C  CD    . PRO   D 2 31  ? 36.34600 45.47300  -1.18400  1.000 29.87416 ?  30  PRO   D CD    1 
ATOM   4196 N  N     . LYS   D 2 32  ? 33.07700 44.22400  -2.40800  1.000 27.85460 ?  31  LYS   D N     1 
ATOM   4197 C  CA    . LYS   D 2 32  ? 31.96200 43.54100  -3.11700  1.000 27.93730 ?  31  LYS   D CA    1 
ATOM   4198 C  C     . LYS   D 2 32  ? 30.96800 42.97200  -2.09600  1.000 24.09569 ?  31  LYS   D C     1 
ATOM   4199 O  O     . LYS   D 2 32  ? 29.76300 43.07700  -2.31000  1.000 24.28436 ?  31  LYS   D O     1 
ATOM   4200 C  CB    . LYS   D 2 32  ? 32.53600 42.47100  -4.04000  1.000 27.38258 ?  31  LYS   D CB    1 
ATOM   4201 C  CG    . LYS   D 2 32  ? 31.58300 41.42400  -4.56300  1.000 34.41998 ?  31  LYS   D CG    1 
ATOM   4202 C  CD    . LYS   D 2 32  ? 32.14600 40.71500  -5.78600  1.000 42.87282 ?  31  LYS   D CD    1 
ATOM   4203 C  CE    . LYS   D 2 32  ? 31.07400 40.10900  -6.62800  1.000 43.20042 ?  31  LYS   D CE    1 
ATOM   4204 N  NZ    . LYS   D 2 32  ? 31.62400 39.33200  -7.73900  1.000 44.17580 ?  31  LYS   D NZ    1 
ATOM   4205 N  N     . THR   D 2 33  ? 31.49800 42.43800  -1.00700  1.000 24.94078 ?  32  THR   D N     1 
ATOM   4206 C  CA    . THR   D 2 33  ? 30.63400 41.85600  0.01300   1.000 23.55245 ?  32  THR   D CA    1 
ATOM   4207 C  C     . THR   D 2 33  ? 29.90800 42.93700  0.79300   1.000 22.57097 ?  32  THR   D C     1 
ATOM   4208 O  O     . THR   D 2 33  ? 28.72300 42.80100  1.11400   1.000 22.82687 ?  32  THR   D O     1 
ATOM   4209 C  CB    . THR   D 2 33  ? 31.50200 40.99800  0.94900   1.000 22.54377 ?  32  THR   D CB    1 
ATOM   4210 O  OG1   . THR   D 2 33  ? 32.32100 40.12000  0.16000   1.000 24.30566 ?  32  THR   D OG1   1 
ATOM   4211 C  CG2   . THR   D 2 33  ? 30.62400 40.20100  1.95100   1.000 23.28540 ?  32  THR   D CG2   1 
ATOM   4212 N  N     . ALA   D 2 34  ? 30.60400 44.02700  1.13200   1.000 22.94740 ?  33  ALA   D N     1 
ATOM   4213 C  CA    . ALA   D 2 34  ? 29.91300 45.15000  1.75200   1.000 24.81364 ?  33  ALA   D CA    1 
ATOM   4214 C  C     . ALA   D 2 34  ? 28.78300 45.66300  0.86000   1.000 24.21633 ?  33  ALA   D C     1 
ATOM   4215 O  O     . ALA   D 2 34  ? 27.70300 46.00600  1.34300   1.000 26.23543 ?  33  ALA   D O     1 
ATOM   4216 C  CB    . ALA   D 2 34  ? 30.92700 46.25300  2.07500   1.000 22.93546 ?  33  ALA   D CB    1 
ATOM   4217 N  N     . GLU   D 2 35  ? 29.03000 45.75000  -0.45100  1.000 25.57242 ?  34  GLU   D N     1 
ATOM   4218 C  CA    . GLU   D 2 35  ? 28.04100 46.33500  -1.34600  1.000 26.46586 ?  34  GLU   D CA    1 
ATOM   4219 C  C     . GLU   D 2 35  ? 26.80700 45.45700  -1.42500  1.000 23.12265 ?  34  GLU   D C     1 
ATOM   4220 O  O     . GLU   D 2 35  ? 25.68000 45.96000  -1.50000  1.000 22.62186 ?  34  GLU   D O     1 
ATOM   4221 C  CB    . GLU   D 2 35  ? 28.67300 46.52600  -2.73600  1.000 27.44887 ?  34  GLU   D CB    1 
ATOM   4222 C  CG    . GLU   D 2 35  ? 27.71400 46.92900  -3.80500  1.000 32.53784 ?  34  GLU   D CG    1 
ATOM   4223 C  CD    . GLU   D 2 35  ? 27.09200 48.30800  -3.60300  1.000 36.56833 ?  34  GLU   D CD    1 
ATOM   4224 O  OE1   . GLU   D 2 35  ? 27.54500 49.12000  -2.74000  1.000 35.14581 ?  34  GLU   D OE1   1 
ATOM   4225 O  OE2   . GLU   D 2 35  ? 26.12800 48.58600  -4.33500  1.000 37.92418 -1 34  GLU   D OE2   1 
ATOM   4226 N  N     . ASN   D 2 36  ? 27.01400 44.13500  -1.46000  1.000 26.17785 ?  35  ASN   D N     1 
ATOM   4227 C  CA    . ASN   D 2 36  ? 25.88600 43.20500  -1.43000  1.000 26.66041 ?  35  ASN   D CA    1 
ATOM   4228 C  C     . ASN   D 2 36  ? 24.98800 43.47300  -0.22100  1.000 24.04967 ?  35  ASN   D C     1 
ATOM   4229 O  O     . ASN   D 2 36  ? 23.76600 43.61800  -0.34300  1.000 23.61521 ?  35  ASN   D O     1 
ATOM   4230 C  CB    . ASN   D 2 36  ? 26.42900 41.77600  -1.43200  1.000 24.36266 ?  35  ASN   D CB    1 
ATOM   4231 C  CG    . ASN   D 2 36  ? 25.32400 40.74200  -1.42100  1.000 28.58324 ?  35  ASN   D CG    1 
ATOM   4232 O  OD1   . ASN   D 2 36  ? 24.48200 40.70900  -2.32000  1.000 24.52926 ?  35  ASN   D OD1   1 
ATOM   4233 N  ND2   . ASN   D 2 36  ? 25.32500 39.88600  -0.41400  1.000 24.30720 ?  35  ASN   D ND2   1 
ATOM   4234 N  N     . PHE   D 2 37  ? 25.59500 43.58100  0.96600   1.000 23.06667 ?  36  PHE   D N     1 
ATOM   4235 C  CA    . PHE   D 2 37  ? 24.82000 43.80800  2.17600   1.000 24.46166 ?  36  PHE   D CA    1 
ATOM   4236 C  C     . PHE   D 2 37  ? 24.16900 45.19200  2.18300   1.000 22.21255 ?  36  PHE   D C     1 
ATOM   4237 O  O     . PHE   D 2 37  ? 23.01400 45.31400  2.56300   1.000 22.93098 ?  36  PHE   D O     1 
ATOM   4238 C  CB    . PHE   D 2 37  ? 25.73100 43.61300  3.37600   1.000 21.94440 ?  36  PHE   D CB    1 
ATOM   4239 C  CG    . PHE   D 2 37  ? 25.01300 43.49100  4.67300   1.000 22.71420 ?  36  PHE   D CG    1 
ATOM   4240 C  CD1   . PHE   D 2 37  ? 24.60600 42.23700  5.15300   1.000 20.26727 ?  36  PHE   D CD1   1 
ATOM   4241 C  CD2   . PHE   D 2 37  ? 24.75600 44.62700  5.43300   1.000 20.74446 ?  36  PHE   D CD2   1 
ATOM   4242 C  CE1   . PHE   D 2 37  ? 23.96800 42.13500  6.39600   1.000 25.23345 ?  36  PHE   D CE1   1 
ATOM   4243 C  CE2   . PHE   D 2 37  ? 24.13800 44.52600  6.69100   1.000 24.87116 ?  36  PHE   D CE2   1 
ATOM   4244 C  CZ    . PHE   D 2 37  ? 23.72600 43.27900  7.16100   1.000 23.97763 ?  36  PHE   D CZ    1 
ATOM   4245 N  N     . ARG   D 2 38  ? 24.88800 46.23000  1.72200   1.000 23.63917 ?  37  ARG   D N     1 
ATOM   4246 C  CA    . ARG   D 2 38  ? 24.32300 47.57500  1.65000   1.000 24.96316 ?  37  ARG   D CA    1 
ATOM   4247 C  C     . ARG   D 2 38  ? 23.07400 47.59100  0.77000   1.000 25.15895 ?  37  ARG   D C     1 
ATOM   4248 O  O     . ARG   D 2 38  ? 22.00100 48.05400  1.18300   1.000 24.46611 ?  37  ARG   D O     1 
ATOM   4249 C  CB    . ARG   D 2 38  ? 25.38600 48.53900  1.07800   1.000 25.44846 ?  37  ARG   D CB    1 
ATOM   4250 C  CG    . ARG   D 2 38  ? 25.00200 49.99400  1.23400   1.000 28.96491 ?  37  ARG   D CG    1 
ATOM   4251 C  CD    . ARG   D 2 38  ? 25.77000 50.90500  0.27500   1.000 32.69941 ?  37  ARG   D CD    1 
ATOM   4252 N  NE    . ARG   D 2 38  ? 25.52100 50.53700  -1.12000  1.000 30.89087 ?  37  ARG   D NE    1 
ATOM   4253 C  CZ    . ARG   D 2 38  ? 24.36900 50.73200  -1.75800  1.000 33.30898 ?  37  ARG   D CZ    1 
ATOM   4254 N  NH1   . ARG   D 2 38  ? 23.35400 51.36000  -1.18600  1.000 36.99079 ?  37  ARG   D NH1   1 
ATOM   4255 N  NH2   . ARG   D 2 38  ? 24.22400 50.25300  -2.99400  1.000 31.07289 ?  37  ARG   D NH2   1 
ATOM   4256 N  N     . ALA   D 2 39  ? 23.20800 47.05100  -0.44300  1.000 26.39259 ?  38  ALA   D N     1 
ATOM   4257 C  CA    . ALA   D 2 39  ? 22.11600 47.04400  -1.41300  1.000 26.76174 ?  38  ALA   D CA    1 
ATOM   4258 C  C     . ALA   D 2 39  ? 20.93600 46.23700  -0.91100  1.000 29.68592 ?  38  ALA   D C     1 
ATOM   4259 O  O     . ALA   D 2 39  ? 19.78100 46.60800  -1.14000  1.000 28.75582 ?  38  ALA   D O     1 
ATOM   4260 C  CB    . ALA   D 2 39  ? 22.60400 46.46700  -2.74600  1.000 29.77211 ?  38  ALA   D CB    1 
ATOM   4261 N  N     . LEU   D 2 40  ? 21.21000 45.10000  -0.25000  1.000 25.96296 ?  39  LEU   D N     1 
ATOM   4262 C  CA    . LEU   D 2 40  ? 20.13000 44.28300  0.29300   1.000 26.01085 ?  39  LEU   D CA    1 
ATOM   4263 C  C     . LEU   D 2 40  ? 19.43600 44.97800  1.46500   1.000 27.55480 ?  39  LEU   D C     1 
ATOM   4264 O  O     . LEU   D 2 40  ? 18.22500 44.76400  1.69600   1.000 26.62107 ?  39  LEU   D O     1 
ATOM   4265 C  CB    . LEU   D 2 40  ? 20.67300 42.90100  0.69600   1.000 24.00821 ?  39  LEU   D CB    1 
ATOM   4266 C  CG    . LEU   D 2 40  ? 21.12200 41.96600  -0.42700  1.000 29.29245 ?  39  LEU   D CG    1 
ATOM   4267 C  CD1   . LEU   D 2 40  ? 21.80700 40.71400  0.11800   1.000 22.19169 ?  39  LEU   D CD1   1 
ATOM   4268 C  CD2   . LEU   D 2 40  ? 19.92500 41.63200  -1.35800  1.000 25.07527 ?  39  LEU   D CD2   1 
ATOM   4269 N  N     . SER   D 2 41  ? 20.16800 45.82400  2.20400   1.000 28.24987 ?  40  SER   D N     1 
ATOM   4270 C  CA    . SER   D 2 41  ? 19.55300 46.60300  3.26900   1.000 27.05386 ?  40  SER   D CA    1 
ATOM   4271 C  C     . SER   D 2 41  ? 18.70300 47.75300  2.73200   1.000 33.05292 ?  40  SER   D C     1 
ATOM   4272 O  O     . SER   D 2 41  ? 17.74300 48.16300  3.39400   1.000 28.65238 ?  40  SER   D O     1 
ATOM   4273 C  CB    . SER   D 2 41  ? 20.61600 47.14700  4.22500   1.000 27.38585 ?  40  SER   D CB    1 
ATOM   4274 O  OG    . SER   D 2 41  ? 21.40100 46.09700  4.79500   1.000 27.82547 ?  40  SER   D OG    1 
ATOM   4275 N  N     . THR   D 2 42  ? 19.02400 48.29300  1.55100   1.000 28.75624 ?  41  THR   D N     1 
ATOM   4276 C  CA    . THR   D 2 42  ? 18.18500 49.36400  1.03000   1.000 34.68595 ?  41  THR   D CA    1 
ATOM   4277 C  C     . THR   D 2 42  ? 17.01800 48.82900  0.21600   1.000 35.20094 ?  41  THR   D C     1 
ATOM   4278 O  O     . THR   D 2 42  ? 16.02400 49.54200  0.04500   1.000 37.99046 ?  41  THR   D O     1 
ATOM   4279 C  CB    . THR   D 2 42  ? 18.99300 50.33300  0.15100   1.000 35.35760 ?  41  THR   D CB    1 
ATOM   4280 O  OG1   . THR   D 2 42  ? 19.46300 49.63500  -1.00300  1.000 31.46964 ?  41  THR   D OG1   1 
ATOM   4281 C  CG2   . THR   D 2 42  ? 20.17300 50.94400  0.91100   1.000 35.08636 ?  41  THR   D CG2   1 
ATOM   4282 N  N     . GLY   D 2 43  ? 17.12100 47.58900  -0.27600  1.000 32.43513 ?  42  GLY   D N     1 
ATOM   4283 C  CA    . GLY   D 2 43  ? 16.12000 46.99200  -1.13300  1.000 35.68233 ?  42  GLY   D CA    1 
ATOM   4284 C  C     . GLY   D 2 43  ? 16.16000 47.49200  -2.56000  1.000 36.03113 ?  42  GLY   D C     1 
ATOM   4285 O  O     . GLY   D 2 43  ? 15.22100 47.23100  -3.32100  1.000 38.72592 ?  42  GLY   D O     1 
ATOM   4286 N  N     . GLU   D 2 44  ? 17.22900 48.18400  -2.94600  1.000 34.26612 ?  43  GLU   D N     1 
ATOM   4287 C  CA    . GLU   D 2 44  ? 17.23900 48.94100  -4.19600  1.000 38.01564 ?  43  GLU   D CA    1 
ATOM   4288 C  C     . GLU   D 2 44  ? 17.20200 48.05500  -5.43200  1.000 42.71073 ?  43  GLU   D C     1 
ATOM   4289 O  O     . GLU   D 2 44  ? 16.80900 48.52900  -6.51200  1.000 39.05327 ?  43  GLU   D O     1 
ATOM   4290 C  CB    . GLU   D 2 44  ? 18.47000 49.84600  -4.21300  1.000 38.20688 ?  43  GLU   D CB    1 
ATOM   4291 C  CG    . GLU   D 2 44  ? 19.78400 49.09500  -4.23700  1.000 33.94660 ?  43  GLU   D CG    1 
ATOM   4292 C  CD    . GLU   D 2 44  ? 20.97500 49.97400  -3.93700  1.000 36.13629 ?  43  GLU   D CD    1 
ATOM   4293 O  OE1   . GLU   D 2 44  ? 20.92100 50.73100  -2.94700  1.000 36.32920 ?  43  GLU   D OE1   1 
ATOM   4294 O  OE2   . GLU   D 2 44  ? 21.96700 49.88700  -4.68200  1.000 43.07656 -1 43  GLU   D OE2   1 
ATOM   4295 N  N     . LYS   D 2 45  ? 17.64200 46.80000  -5.32400  1.000 31.06604 ?  44  LYS   D N     1 
ATOM   4296 C  CA    . LYS   D 2 45  ? 17.52400 45.86900  -6.44600  1.000 34.81914 ?  44  LYS   D CA    1 
ATOM   4297 C  C     . LYS   D 2 45  ? 16.11100 45.31500  -6.59100  1.000 35.11850 ?  44  LYS   D C     1 
ATOM   4298 O  O     . LYS   D 2 45  ? 15.85600 44.54000  -7.52000  1.000 41.60424 ?  44  LYS   D O     1 
ATOM   4299 C  CB    . LYS   D 2 45  ? 18.50800 44.71100  -6.28100  1.000 38.99490 ?  44  LYS   D CB    1 
ATOM   4300 C  CG    . LYS   D 2 45  ? 19.89900 44.90200  -6.89800  1.000 43.25952 ?  44  LYS   D CG    1 
ATOM   4301 C  CD    . LYS   D 2 45  ? 20.31300 46.37400  -7.12800  1.000 44.23831 ?  44  LYS   D CD    1 
ATOM   4302 C  CE    . LYS   D 2 45  ? 21.72900 46.47300  -7.72800  1.000 41.72207 ?  44  LYS   D CE    1 
ATOM   4303 N  NZ    . LYS   D 2 45  ? 21.84000 45.97300  -9.14500  1.000 48.62925 ?  44  LYS   D NZ    1 
ATOM   4304 N  N     . GLY   D 2 46  ? 15.18800 45.69900  -5.71200  1.000 33.25468 ?  45  GLY   D N     1 
ATOM   4305 C  CA    . GLY   D 2 46  ? 13.84800 45.16200  -5.71900  1.000 35.76259 ?  45  GLY   D CA    1 
ATOM   4306 C  C     . GLY   D 2 46  ? 13.62900 44.05000  -4.72400  1.000 42.90237 ?  45  GLY   D C     1 
ATOM   4307 O  O     . GLY   D 2 46  ? 12.50600 43.53900  -4.62100  1.000 39.70150 ?  45  GLY   D O     1 
ATOM   4308 N  N     . PHE   D 2 47  ? 14.66900 43.66500  -3.98300  1.000 33.32878 ?  46  PHE   D N     1 
ATOM   4309 C  CA    . PHE   D 2 47  ? 14.55100 42.61600  -2.98100  1.000 30.66527 ?  46  PHE   D CA    1 
ATOM   4310 C  C     . PHE   D 2 47  ? 15.59500 42.88000  -1.91000  1.000 31.19807 ?  46  PHE   D C     1 
ATOM   4311 O  O     . PHE   D 2 47  ? 16.53400 43.65100  -2.11900  1.000 30.06325 ?  46  PHE   D O     1 
ATOM   4312 C  CB    . PHE   D 2 47  ? 14.74500 41.23000  -3.59800  1.000 30.81299 ?  46  PHE   D CB    1 
ATOM   4313 C  CG    . PHE   D 2 47  ? 15.97300 41.11600  -4.48400  1.000 30.93213 ?  46  PHE   D CG    1 
ATOM   4314 C  CD1   . PHE   D 2 47  ? 17.24500 41.00400  -3.93000  1.000 32.84217 ?  46  PHE   D CD1   1 
ATOM   4315 C  CD2   . PHE   D 2 47  ? 15.86000 41.10800  -5.87100  1.000 32.56640 ?  46  PHE   D CD2   1 
ATOM   4316 C  CE1   . PHE   D 2 47  ? 18.36700 40.88700  -4.72800  1.000 33.79341 ?  46  PHE   D CE1   1 
ATOM   4317 C  CE2   . PHE   D 2 47  ? 16.98100 40.98800  -6.68800  1.000 39.46450 ?  46  PHE   D CE2   1 
ATOM   4318 C  CZ    . PHE   D 2 47  ? 18.24400 40.88900  -6.11900  1.000 38.44188 ?  46  PHE   D CZ    1 
ATOM   4319 N  N     . GLY   D 2 48  ? 15.43900 42.23300  -0.76000  1.000 30.88044 ?  47  GLY   D N     1 
ATOM   4320 C  CA    . GLY   D 2 48  ? 16.41800 42.43100  0.30100   1.000 26.06596 ?  47  GLY   D CA    1 
ATOM   4321 C  C     . GLY   D 2 48  ? 15.84000 42.04900  1.65600   1.000 25.25386 ?  47  GLY   D C     1 
ATOM   4322 O  O     . GLY   D 2 48  ? 14.86400 41.31900  1.74900   1.000 26.59216 ?  47  GLY   D O     1 
ATOM   4323 N  N     . TYR   D 2 49  ? 16.48400 42.57500  2.69900   1.000 26.40786 ?  48  TYR   D N     1 
ATOM   4324 C  CA    . TYR   D 2 49  ? 16.30700 42.05700  4.04600   1.000 27.09648 ?  48  TYR   D CA    1 
ATOM   4325 C  C     . TYR   D 2 49  ? 14.99100 42.46100  4.68500   1.000 26.60922 ?  48  TYR   D C     1 
ATOM   4326 O  O     . TYR   D 2 49  ? 14.52900 41.76500  5.59700   1.000 25.69524 ?  48  TYR   D O     1 
ATOM   4327 C  CB    . TYR   D 2 49  ? 17.45800 42.53300  4.92900   1.000 24.45156 ?  48  TYR   D CB    1 
ATOM   4328 C  CG    . TYR   D 2 49  ? 18.79600 41.91500  4.58500   1.000 21.64543 ?  48  TYR   D CG    1 
ATOM   4329 C  CD1   . TYR   D 2 49  ? 18.91300 40.54900  4.33800   1.000 26.47399 ?  48  TYR   D CD1   1 
ATOM   4330 C  CD2   . TYR   D 2 49  ? 19.94200 42.67900  4.53300   1.000 20.97082 ?  48  TYR   D CD2   1 
ATOM   4331 C  CE1   . TYR   D 2 49  ? 20.15000 39.96800  4.02700   1.000 23.44978 ?  48  TYR   D CE1   1 
ATOM   4332 C  CE2   . TYR   D 2 49  ? 21.19000 42.11300  4.20000   1.000 23.08233 ?  48  TYR   D CE2   1 
ATOM   4333 C  CZ    . TYR   D 2 49  ? 21.28600 40.75400  3.97800   1.000 21.21349 ?  48  TYR   D CZ    1 
ATOM   4334 O  OH    . TYR   D 2 49  ? 22.48200 40.16700  3.67900   1.000 21.45056 ?  48  TYR   D OH    1 
ATOM   4335 N  N     . LYS   D 2 50  ? 14.38400 43.57300  4.26100   1.000 28.02128 ?  49  LYS   D N     1 
ATOM   4336 C  CA    . LYS   D 2 50  ? 13.17800 44.04700  4.94600   1.000 29.72999 ?  49  LYS   D CA    1 
ATOM   4337 C  C     . LYS   D 2 50  ? 12.12200 42.94700  5.04000   1.000 29.21919 ?  49  LYS   D C     1 
ATOM   4338 O  O     . LYS   D 2 50  ? 11.78500 42.30400  4.05000   1.000 29.55472 ?  49  LYS   D O     1 
ATOM   4339 C  CB    . LYS   D 2 50  ? 12.60300 45.26600  4.22100   1.000 36.11899 ?  49  LYS   D CB    1 
ATOM   4340 C  CG    . LYS   D 2 50  ? 11.43400 45.86500  4.96500   1.000 35.15806 ?  49  LYS   D CG    1 
ATOM   4341 C  CD    . LYS   D 2 50  ? 11.00300 47.14500  4.29700   1.000 37.62648 ?  49  LYS   D CD    1 
ATOM   4342 C  CE    . LYS   D 2 50  ? 9.81500  47.74600  5.03500   1.000 44.49839 ?  49  LYS   D CE    1 
ATOM   4343 N  NZ    . LYS   D 2 50  ? 9.54000  49.08200  4.46700   1.000 51.62293 ?  49  LYS   D NZ    1 
ATOM   4344 N  N     . GLY   D 2 51  ? 11.63000 42.70600  6.25800   1.000 28.77395 ?  50  GLY   D N     1 
ATOM   4345 C  CA    . GLY   D 2 51  ? 10.63000 41.69400  6.51000   1.000 26.26195 ?  50  GLY   D CA    1 
ATOM   4346 C  C     . GLY   D 2 51  ? 11.14700 40.30500  6.84900   1.000 32.90876 ?  50  GLY   D C     1 
ATOM   4347 O  O     . GLY   D 2 51  ? 10.37200 39.48000  7.34700   1.000 31.27873 ?  50  GLY   D O     1 
ATOM   4348 N  N     . SER   D 2 52  ? 12.41100 40.01000  6.58000   1.000 29.00637 ?  51  SER   D N     1 
ATOM   4349 C  CA    . SER   D 2 52  ? 12.94900 38.68600  6.84300   1.000 31.39328 ?  51  SER   D CA    1 
ATOM   4350 C  C     . SER   D 2 52  ? 13.27700 38.55100  8.33400   1.000 29.98619 ?  51  SER   D C     1 
ATOM   4351 O  O     . SER   D 2 52  ? 13.24900 39.52200  9.09300   1.000 26.54271 ?  51  SER   D O     1 
ATOM   4352 C  CB    . SER   D 2 52  ? 14.18700 38.44000  5.98000   1.000 27.73190 ?  51  SER   D CB    1 
ATOM   4353 O  OG    . SER   D 2 52  ? 15.28300 39.25900  6.39400   1.000 26.09713 ?  51  SER   D OG    1 
ATOM   4354 N  N     . CYS   D 2 53  ? 13.57900 37.33300  8.76100   1.000 28.12515 ?  52  CYS   D N     1 
ATOM   4355 C  CA    . CYS   D 2 53  ? 13.71100 37.07400  10.18900  1.000 26.92992 ?  52  CYS   D CA    1 
ATOM   4356 C  C     . CYS   D 2 53  ? 15.11300 36.56800  10.51500  1.000 24.86260 ?  52  CYS   D C     1 
ATOM   4357 O  O     . CYS   D 2 53  ? 15.89600 36.21400  9.63200   1.000 25.81230 ?  52  CYS   D O     1 
ATOM   4358 C  CB    . CYS   D 2 53  ? 12.64400 36.07700  10.64600  1.000 32.16774 ?  52  CYS   D CB    1 
ATOM   4359 S  SG    . CYS   D 2 53  ? 13.09100 34.40300  10.29000  1.000 41.77449 ?  52  CYS   D SG    1 
ATOM   4360 N  N     . PHE   D 2 54  ? 15.44200 36.56700  11.80500  1.000 26.10693 ?  53  PHE   D N     1 
ATOM   4361 C  CA    . PHE   D 2 54  ? 16.64100 35.87600  12.32800  1.000 21.10290 ?  53  PHE   D CA    1 
ATOM   4362 C  C     . PHE   D 2 54  ? 16.21100 34.47300  12.69300  1.000 22.03979 ?  53  PHE   D C     1 
ATOM   4363 O  O     . PHE   D 2 54  ? 15.53800 34.27400  13.71000  1.000 26.20256 ?  53  PHE   D O     1 
ATOM   4364 C  CB    . PHE   D 2 54  ? 17.21500 36.59300  13.54900  1.000 22.27071 ?  53  PHE   D CB    1 
ATOM   4365 C  CG    . PHE   D 2 54  ? 18.08900 37.78600  13.20600  1.000 21.90172 ?  53  PHE   D CG    1 
ATOM   4366 C  CD1   . PHE   D 2 54  ? 17.53700 39.05300  13.01100  1.000 23.13801 ?  53  PHE   D CD1   1 
ATOM   4367 C  CD2   . PHE   D 2 54  ? 19.47500 37.64200  13.10500  1.000 19.30481 ?  53  PHE   D CD2   1 
ATOM   4368 C  CE1   . PHE   D 2 54  ? 18.35400 40.14500  12.65700  1.000 24.81478 ?  53  PHE   D CE1   1 
ATOM   4369 C  CE2   . PHE   D 2 54  ? 20.29300 38.72200  12.79000  1.000 25.71051 ?  53  PHE   D CE2   1 
ATOM   4370 C  CZ    . PHE   D 2 54  ? 19.73700 39.99200  12.58400  1.000 25.22099 ?  53  PHE   D CZ    1 
ATOM   4371 N  N     . HIS   D 2 55  ? 16.54400 33.50300  11.84600  1.000 19.60560 ?  54  HIS   D N     1 
ATOM   4372 C  CA    . HIS   D 2 55  ? 16.01900 32.15200  11.99400  1.000 23.16855 ?  54  HIS   D CA    1 
ATOM   4373 C  C     . HIS   D 2 55  ? 16.84600 31.26600  12.90400  1.000 25.36722 ?  54  HIS   D C     1 
ATOM   4374 O  O     . HIS   D 2 55  ? 16.36500 30.19100  13.28400  1.000 25.07403 ?  54  HIS   D O     1 
ATOM   4375 C  CB    . HIS   D 2 55  ? 15.88600 31.46200  10.64200  1.000 25.15979 ?  54  HIS   D CB    1 
ATOM   4376 C  CG    . HIS   D 2 55  ? 17.18200 31.30900  9.91900   1.000 23.94177 ?  54  HIS   D CG    1 
ATOM   4377 N  ND1   . HIS   D 2 55  ? 17.76000 32.34200  9.21900   1.000 21.30937 ?  54  HIS   D ND1   1 
ATOM   4378 C  CD2   . HIS   D 2 55  ? 18.02200 30.25600  9.81000   1.000 24.83889 ?  54  HIS   D CD2   1 
ATOM   4379 C  CE1   . HIS   D 2 55  ? 18.88500 31.92100  8.66500   1.000 23.66127 ?  54  HIS   D CE1   1 
ATOM   4380 N  NE2   . HIS   D 2 55  ? 19.05800 30.65300  8.99200   1.000 22.63925 ?  54  HIS   D NE2   1 
ATOM   4381 N  N     . ARG   D 2 56  ? 18.06800 31.67500  13.25600  1.000 21.16456 ?  55  ARG   D N     1 
ATOM   4382 C  CA    . ARG   D 2 56  ? 18.94700 30.83200  14.06200  1.000 21.85833 ?  55  ARG   D CA    1 
ATOM   4383 C  C     . ARG   D 2 56  ? 19.64900 31.73200  15.05900  1.000 19.72290 ?  55  ARG   D C     1 
ATOM   4384 O  O     . ARG   D 2 56  ? 20.51300 32.52000  14.67900  1.000 22.45169 ?  55  ARG   D O     1 
ATOM   4385 C  CB    . ARG   D 2 56  ? 19.94800 30.08200  13.17500  1.000 23.53843 ?  55  ARG   D CB    1 
ATOM   4386 C  CG    . ARG   D 2 56  ? 20.80000 29.06800  13.94300  1.000 22.70300 ?  55  ARG   D CG    1 
ATOM   4387 C  CD    . ARG   D 2 56  ? 21.80100 28.42000  12.96800  1.000 22.34310 ?  55  ARG   D CD    1 
ATOM   4388 N  NE    . ARG   D 2 56  ? 21.12300 27.52400  12.05000  1.000 24.60959 ?  55  ARG   D NE    1 
ATOM   4389 C  CZ    . ARG   D 2 56  ? 21.66200 27.13500  10.90900  1.000 31.83473 ?  55  ARG   D CZ    1 
ATOM   4390 N  NH1   . ARG   D 2 56  ? 22.83400 27.60900  10.50800  1.000 27.68264 ?  55  ARG   D NH1   1 
ATOM   4391 N  NH2   . ARG   D 2 56  ? 21.02800 26.23200  10.17100  1.000 32.99384 ?  55  ARG   D NH2   1 
ATOM   4392 N  N     . ILE   D 2 57  ? 19.30100 31.60300  16.33900  1.000 20.81639 ?  56  ILE   D N     1 
ATOM   4393 C  CA    . ILE   D 2 57  ? 19.91200 32.39600  17.39000  1.000 18.69267 ?  56  ILE   D CA    1 
ATOM   4394 C  C     . ILE   D 2 57  ? 20.45500 31.42300  18.41700  1.000 23.22063 ?  56  ILE   D C     1 
ATOM   4395 O  O     . ILE   D 2 57  ? 19.67600 30.66200  18.99700  1.000 21.36942 ?  56  ILE   D O     1 
ATOM   4396 C  CB    . ILE   D 2 57  ? 18.90000 33.35500  18.04100  1.000 19.43648 ?  56  ILE   D CB    1 
ATOM   4397 C  CG1   . ILE   D 2 57  ? 18.47600 34.41600  17.00400  1.000 20.29435 ?  56  ILE   D CG1   1 
ATOM   4398 C  CG2   . ILE   D 2 57  ? 19.53100 34.00100  19.31200  1.000 22.58683 ?  56  ILE   D CG2   1 
ATOM   4399 C  CD1   . ILE   D 2 57  ? 17.28000 35.28000  17.41600  1.000 21.70463 ?  56  ILE   D CD1   1 
ATOM   4400 N  N     . ILE   D 2 58  ? 21.77000 31.46500  18.66200  1.000 21.13181 ?  57  ILE   D N     1 
ATOM   4401 C  CA    . ILE   D 2 58  ? 22.35200 30.52500  19.63100  1.000 23.76436 ?  57  ILE   D CA    1 
ATOM   4402 C  C     . ILE   D 2 58  ? 23.10300 31.32900  20.67900  1.000 22.41007 ?  57  ILE   D C     1 
ATOM   4403 O  O     . ILE   D 2 58  ? 24.19000 31.85700  20.38200  1.000 22.61722 ?  57  ILE   D O     1 
ATOM   4404 C  CB    . ILE   D 2 58  ? 23.26200 29.48600  18.96500  1.000 23.07698 ?  57  ILE   D CB    1 
ATOM   4405 C  CG1   . ILE   D 2 58  ? 22.44400 28.65400  17.98400  1.000 21.53068 ?  57  ILE   D CG1   1 
ATOM   4406 C  CG2   . ILE   D 2 58  ? 23.84100 28.50500  20.01700  1.000 23.03228 ?  57  ILE   D CG2   1 
ATOM   4407 C  CD1   . ILE   D 2 58  ? 23.29000 27.69600  17.19800  1.000 25.04347 ?  57  ILE   D CD1   1 
ATOM   4408 N  N     . PRO   D 2 59  ? 22.55600 31.44900  21.89100  1.000 23.26911 ?  58  PRO   D N     1 
ATOM   4409 C  CA    . PRO   D 2 59  ? 23.24300 32.22600  22.92900  1.000 25.65656 ?  58  PRO   D CA    1 
ATOM   4410 C  C     . PRO   D 2 59  ? 24.65000 31.70000  23.15200  1.000 22.61006 ?  58  PRO   D C     1 
ATOM   4411 O  O     . PRO   D 2 59  ? 24.89800 30.48900  23.10000  1.000 22.35106 ?  58  PRO   D O     1 
ATOM   4412 C  CB    . PRO   D 2 59  ? 22.35700 32.03700  24.15800  1.000 24.28876 ?  58  PRO   D CB    1 
ATOM   4413 C  CG    . PRO   D 2 59  ? 21.00000 31.71500  23.61800  1.000 23.47024 ?  58  PRO   D CG    1 
ATOM   4414 C  CD    . PRO   D 2 59  ? 21.28300 30.88000  22.38100  1.000 25.80874 ?  58  PRO   D CD    1 
ATOM   4415 N  N     . GLY   D 2 60  ? 25.58000 32.63400  23.34700  1.000 24.08216 ?  59  GLY   D N     1 
ATOM   4416 C  CA    . GLY   D 2 60  ? 26.98000 32.29900  23.45800  1.000 27.74802 ?  59  GLY   D CA    1 
ATOM   4417 C  C     . GLY   D 2 60  ? 27.72600 32.31000  22.15000  1.000 26.23070 ?  59  GLY   D C     1 
ATOM   4418 O  O     . GLY   D 2 60  ? 28.95300 32.16300  22.16200  1.000 25.09454 ?  59  GLY   D O     1 
ATOM   4419 N  N     . PHE   D 2 61  ? 27.01700 32.45800  21.01500  1.000 23.29451 ?  60  PHE   D N     1 
ATOM   4420 C  CA    . PHE   D 2 61  ? 27.67300 32.28300  19.72500  1.000 21.41872 ?  60  PHE   D CA    1 
ATOM   4421 C  C     . PHE   D 2 61  ? 27.28200 33.35000  18.71700  1.000 23.38787 ?  60  PHE   D C     1 
ATOM   4422 O  O     . PHE   D 2 61  ? 28.11700 34.20200  18.39000  1.000 20.17821 ?  60  PHE   D O     1 
ATOM   4423 C  CB    . PHE   D 2 61  ? 27.37800 30.89900  19.12900  1.000 21.22117 ?  60  PHE   D CB    1 
ATOM   4424 C  CG    . PHE   D 2 61  ? 28.07500 29.79000  19.86200  1.000 22.81725 ?  60  PHE   D CG    1 
ATOM   4425 C  CD1   . PHE   D 2 61  ? 29.39700 29.50900  19.60800  1.000 23.04512 ?  60  PHE   D CD1   1 
ATOM   4426 C  CD2   . PHE   D 2 61  ? 27.41200 29.09300  20.88000  1.000 27.58511 ?  60  PHE   D CD2   1 
ATOM   4427 C  CE1   . PHE   D 2 61  ? 30.04700 28.52000  20.30700  1.000 28.69381 ?  60  PHE   D CE1   1 
ATOM   4428 C  CE2   . PHE   D 2 61  ? 28.07300 28.10400  21.59300  1.000 29.14809 ?  60  PHE   D CE2   1 
ATOM   4429 C  CZ    . PHE   D 2 61  ? 29.37400 27.82700  21.30900  1.000 31.07053 ?  60  PHE   D CZ    1 
ATOM   4430 N  N     A MET   D 2 62  ? 26.04900 33.32400  18.21400  0.500 21.46255 ?  61  MET   D N     1 
ATOM   4431 N  N     B MET   D 2 62  ? 26.04400 33.33100  18.22300  0.500 23.27087 ?  61  MET   D N     1 
ATOM   4432 C  CA    A MET   D 2 62  ? 25.72600 34.25200  17.13600  0.500 22.70446 ?  61  MET   D CA    1 
ATOM   4433 C  CA    B MET   D 2 62  ? 25.73200 34.26500  17.14700  0.500 20.18365 ?  61  MET   D CA    1 
ATOM   4434 C  C     A MET   D 2 62  ? 24.22200 34.32900  16.91600  0.500 22.31592 ?  61  MET   D C     1 
ATOM   4435 C  C     B MET   D 2 62  ? 24.23800 34.29200  16.86000  0.500 21.35092 ?  61  MET   D C     1 
ATOM   4436 O  O     A MET   D 2 62  ? 23.44900 33.48300  17.37600  0.500 22.82781 ?  61  MET   D O     1 
ATOM   4437 O  O     B MET   D 2 62  ? 23.48900 33.37500  17.22100  0.500 22.62154 ?  61  MET   D O     1 
ATOM   4438 C  CB    A MET   D 2 62  ? 26.41800 33.84100  15.82700  0.500 20.52927 ?  61  MET   D CB    1 
ATOM   4439 C  CB    B MET   D 2 62  ? 26.51400 33.90800  15.87000  0.500 20.51545 ?  61  MET   D CB    1 
ATOM   4440 C  CG    A MET   D 2 62  ? 25.57600 32.90100  14.95500  0.500 22.72971 ?  61  MET   D CG    1 
ATOM   4441 C  CG    B MET   D 2 62  ? 26.26300 32.49200  15.36300  0.500 23.57350 ?  61  MET   D CG    1 
ATOM   4442 S  SD    A MET   D 2 62  ? 25.36500 31.21500  15.62200  0.500 18.58801 ?  61  MET   D SD    1 
ATOM   4443 S  SD    B MET   D 2 62  ? 24.85600 32.45700  14.21800  0.500 25.28013 ?  61  MET   D SD    1 
ATOM   4444 C  CE    A MET   D 2 62  ? 23.78500 30.72200  14.92900  0.500 23.96550 ?  61  MET   D CE    1 
ATOM   4445 C  CE    B MET   D 2 62  ? 24.11900 30.87300  14.58700  0.500 24.31062 ?  61  MET   D CE    1 
ATOM   4446 N  N     . CYS   D 2 63  ? 23.82900 35.34800  16.14600  1.000 20.61221 ?  62  CYS   D N     1 
ATOM   4447 C  CA    . CYS   D 2 63  ? 22.47800 35.51100  15.60300  1.000 20.77371 ?  62  CYS   D CA    1 
ATOM   4448 C  C     . CYS   D 2 63  ? 22.58800 35.50100  14.08400  1.000 18.49325 ?  62  CYS   D C     1 
ATOM   4449 O  O     . CYS   D 2 63  ? 23.32200 36.32900  13.52900  1.000 21.85410 ?  62  CYS   D O     1 
ATOM   4450 C  CB    . CYS   D 2 63  ? 21.86800 36.85500  16.01200  1.000 20.42508 ?  62  CYS   D CB    1 
ATOM   4451 S  SG    . CYS   D 2 63  ? 21.59600 37.04300  17.83500  1.000 26.37935 ?  62  CYS   D SG    1 
ATOM   4452 N  N     . GLN   D 2 64  ? 21.81400 34.64400  13.41700  1.000 18.44718 ?  63  GLN   D N     1 
ATOM   4453 C  CA    . GLN   D 2 64  ? 21.92300 34.47600  11.96800  1.000 18.91188 ?  63  GLN   D CA    1 
ATOM   4454 C  C     . GLN   D 2 64  ? 20.58900 34.74800  11.29800  1.000 20.46007 ?  63  GLN   D C     1 
ATOM   4455 O  O     . GLN   D 2 64  ? 19.53100 34.34900  11.79800  1.000 18.41226 ?  63  GLN   D O     1 
ATOM   4456 C  CB    . GLN   D 2 64  ? 22.40800 33.07300  11.61000  1.000 21.88667 ?  63  GLN   D CB    1 
ATOM   4457 C  CG    . GLN   D 2 64  ? 22.38900 32.72400  10.12700  1.000 20.67530 ?  63  GLN   D CG    1 
ATOM   4458 C  CD    . GLN   D 2 64  ? 22.97000 31.37000  9.86500   1.000 22.32602 ?  63  GLN   D CD    1 
ATOM   4459 O  OE1   . GLN   D 2 64  ? 23.62000 30.80200  10.73700  1.000 22.76935 ?  63  GLN   D OE1   1 
ATOM   4460 N  NE2   . GLN   D 2 64  ? 22.74600 30.83400  8.67100   1.000 20.25301 ?  63  GLN   D NE2   1 
ATOM   4461 N  N     . GLY   D 2 65  ? 20.65200 35.43300  10.17200  1.000 18.78344 ?  64  GLY   D N     1 
ATOM   4462 C  CA    . GLY   D 2 65  ? 19.43500 35.74900  9.42100   1.000 18.53493 ?  64  GLY   D CA    1 
ATOM   4463 C  C     . GLY   D 2 65  ? 19.68800 35.95500  7.95200   1.000 22.64043 ?  64  GLY   D C     1 
ATOM   4464 O  O     . GLY   D 2 65  ? 20.72600 35.52000  7.42600   1.000 19.46845 ?  64  GLY   D O     1 
ATOM   4465 N  N     . GLY   D 2 66  ? 18.71100 36.57200  7.27200   1.000 20.45631 ?  65  GLY   D N     1 
ATOM   4466 C  CA    . GLY   D 2 66  ? 18.90000 37.02600  5.91900   1.000 19.49044 ?  65  GLY   D CA    1 
ATOM   4467 C  C     . GLY   D 2 66  ? 18.26000 36.19700  4.83300   1.000 24.78689 ?  65  GLY   D C     1 
ATOM   4468 O  O     . GLY   D 2 66  ? 18.49800 36.48800  3.65100   1.000 24.06730 ?  65  GLY   D O     1 
ATOM   4469 N  N     . ASP   D 2 67  ? 17.49600 35.15900  5.16400   1.000 23.86565 ?  66  ASP   D N     1 
ATOM   4470 C  CA    . ASP   D 2 67  ? 16.81300 34.39200  4.10400   1.000 24.61577 ?  66  ASP   D CA    1 
ATOM   4471 C  C     . ASP   D 2 67  ? 15.50200 35.08500  3.76300   1.000 28.63710 ?  66  ASP   D C     1 
ATOM   4472 O  O     . ASP   D 2 67  ? 14.45400 34.82600  4.36200   1.000 30.18697 ?  66  ASP   D O     1 
ATOM   4473 C  CB    . ASP   D 2 67  ? 16.56300 32.95700  4.53300   1.000 22.56935 ?  66  ASP   D CB    1 
ATOM   4474 C  CG    . ASP   D 2 67  ? 15.72000 32.17900  3.52300   1.000 29.32236 ?  66  ASP   D CG    1 
ATOM   4475 O  OD1   . ASP   D 2 67  ? 15.46000 32.72500  2.41900   1.000 29.28113 ?  66  ASP   D OD1   1 
ATOM   4476 O  OD2   . ASP   D 2 67  ? 15.35200 31.01900  3.83700   1.000 29.16591 -1 66  ASP   D OD2   1 
ATOM   4477 N  N     . PHE   D 2 68  ? 15.54300 35.97500  2.78500   1.000 25.95118 ?  67  PHE   D N     1 
ATOM   4478 C  CA    . PHE   D 2 68  ? 14.33100 36.65500  2.34600   1.000 28.60135 ?  67  PHE   D CA    1 
ATOM   4479 C  C     . PHE   D 2 68  ? 13.68400 35.99100  1.14500   1.000 31.58337 ?  67  PHE   D C     1 
ATOM   4480 O  O     . PHE   D 2 68  ? 12.70500 36.52400  0.62500   1.000 31.27735 ?  67  PHE   D O     1 
ATOM   4481 C  CB    . PHE   D 2 68  ? 14.64000 38.12400  2.00800   1.000 28.49742 ?  67  PHE   D CB    1 
ATOM   4482 C  CG    . PHE   D 2 68  ? 15.68200 38.29100  0.92200   1.000 30.43147 ?  67  PHE   D CG    1 
ATOM   4483 C  CD1   . PHE   D 2 68  ? 15.32600 38.20100  -0.41900  1.000 30.14075 ?  67  PHE   D CD1   1 
ATOM   4484 C  CD2   . PHE   D 2 68  ? 17.02300 38.54800  1.24000   1.000 27.35865 ?  67  PHE   D CD2   1 
ATOM   4485 C  CE1   . PHE   D 2 68  ? 16.26200 38.35200  -1.41100  1.000 31.41934 ?  67  PHE   D CE1   1 
ATOM   4486 C  CE2   . PHE   D 2 68  ? 17.99100 38.70300  0.22600   1.000 26.03880 ?  67  PHE   D CE2   1 
ATOM   4487 C  CZ    . PHE   D 2 68  ? 17.59900 38.59000  -1.10700  1.000 28.29941 ?  67  PHE   D CZ    1 
ATOM   4488 N  N     . THR   D 2 69  ? 14.22500 34.88100  0.64300   1.000 29.16725 ?  68  THR   D N     1 
ATOM   4489 C  CA    . THR   D 2 69  ? 13.55700 34.29800  -0.52300  1.000 32.46557 ?  68  THR   D CA    1 
ATOM   4490 C  C     . THR   D 2 69  ? 12.65800 33.13000  -0.16300  1.000 35.41763 ?  68  THR   D C     1 
ATOM   4491 O  O     . THR   D 2 69  ? 11.57500 32.98000  -0.74600  1.000 35.79800 ?  68  THR   D O     1 
ATOM   4492 C  CB    . THR   D 2 69  ? 14.57700 33.85200  -1.57800  1.000 32.35201 ?  68  THR   D CB    1 
ATOM   4493 O  OG1   . THR   D 2 69  ? 15.33500 32.74200  -1.09500  1.000 30.80508 ?  68  THR   D OG1   1 
ATOM   4494 C  CG2   . THR   D 2 69  ? 15.52200 34.99300  -1.95600  1.000 32.11633 ?  68  THR   D CG2   1 
ATOM   4495 N  N     . ARG   D 2 70  ? 13.07200 32.33800  0.81800   1.000 32.86289 ?  69  ARG   D N     1 
ATOM   4496 C  CA    . ARG   D 2 70  ? 12.28600 31.14500  1.21400   1.000 31.70047 ?  69  ARG   D CA    1 
ATOM   4497 C  C     . ARG   D 2 70  ? 11.73300 31.29600  2.63800   1.000 35.54438 ?  69  ARG   D C     1 
ATOM   4498 O  O     . ARG   D 2 70  ? 10.85900 30.50000  3.00800   1.000 36.05967 ?  69  ARG   D O     1 
ATOM   4499 C  CB    . ARG   D 2 70  ? 13.17900 29.91400  1.09700   1.000 34.77350 ?  69  ARG   D CB    1 
ATOM   4500 C  CG    . ARG   D 2 70  ? 13.76000 29.72400  -0.29200  1.000 34.31326 ?  69  ARG   D CG    1 
ATOM   4501 C  CD    . ARG   D 2 70  ? 14.42600 28.37800  -0.35000  1.000 39.47259 ?  69  ARG   D CD    1 
ATOM   4502 N  NE    . ARG   D 2 70  ? 15.14600 28.17200  -1.60700  1.000 38.27496 ?  69  ARG   D NE    1 
ATOM   4503 C  CZ    . ARG   D 2 70  ? 16.23200 27.43100  -1.70600  1.000 43.16665 ?  69  ARG   D CZ    1 
ATOM   4504 N  NH1   . ARG   D 2 70  ? 16.58100 26.64000  -0.71200  1.000 35.08935 ?  69  ARG   D NH1   1 
ATOM   4505 N  NH2   . ARG   D 2 70  ? 16.96200 27.48900  -2.80200  1.000 48.84299 ?  69  ARG   D NH2   1 
ATOM   4506 N  N     . HIS   D 2 71  ? 12.24600 32.25300  3.39900   1.000 32.12441 ?  70  HIS   D N     1 
ATOM   4507 C  CA    . HIS   D 2 71  ? 11.76500 32.49400  4.75600   1.000 34.24930 ?  70  HIS   D CA    1 
ATOM   4508 C  C     . HIS   D 2 71  ? 11.79000 31.21600  5.58400   1.000 34.18373 ?  70  HIS   D C     1 
ATOM   4509 O  O     . HIS   D 2 71  ? 10.90600 30.96600  6.40800   1.000 38.19485 ?  70  HIS   D O     1 
ATOM   4510 C  CB    . HIS   D 2 71  ? 10.36800 33.12200  4.74500   1.000 33.47953 ?  70  HIS   D CB    1 
ATOM   4511 C  CG    . HIS   D 2 71  ? 10.33000 34.44700  4.05700   1.000 38.72009 ?  70  HIS   D CG    1 
ATOM   4512 N  ND1   . HIS   D 2 71  ? 9.97900  34.58600  2.73100   1.000 41.85628 ?  70  HIS   D ND1   1 
ATOM   4513 C  CD2   . HIS   D 2 71  ? 10.67500 35.68500  4.49000   1.000 37.46876 ?  70  HIS   D CD2   1 
ATOM   4514 C  CE1   . HIS   D 2 71  ? 10.06800 35.86300  2.38900   1.000 41.51981 ?  70  HIS   D CE1   1 
ATOM   4515 N  NE2   . HIS   D 2 71  ? 10.49700 36.54800  3.43600   1.000 39.34762 ?  70  HIS   D NE2   1 
ATOM   4516 N  N     . ASN   D 2 72  ? 12.83200 30.39600  5.38000   1.000 35.64863 ?  71  ASN   D N     1 
ATOM   4517 C  CA    . ASN   D 2 72  ? 12.92900 29.20500  6.22000   1.000 38.25968 ?  71  ASN   D CA    1 
ATOM   4518 C  C     . ASN   D 2 72  ? 14.35900 28.79100  6.56500   1.000 35.29967 ?  71  ASN   D C     1 
ATOM   4519 O  O     . ASN   D 2 72  ? 14.56500 27.64700  6.98300   1.000 39.59426 ?  71  ASN   D O     1 
ATOM   4520 C  CB    . ASN   D 2 72  ? 12.17300 28.02200  5.55500   1.000 35.13547 ?  71  ASN   D CB    1 
ATOM   4521 C  CG    . ASN   D 2 72  ? 12.79200 27.58600  4.24800   1.000 36.12274 ?  71  ASN   D CG    1 
ATOM   4522 O  OD1   . ASN   D 2 72  ? 13.91800 27.94700  3.91800   1.000 31.18027 ?  71  ASN   D OD1   1 
ATOM   4523 N  ND2   . ASN   D 2 72  ? 12.04900 26.79200  3.49000   1.000 35.07858 ?  71  ASN   D ND2   1 
ATOM   4524 N  N     . GLY   D 2 73  ? 15.34900 29.66200  6.41300   1.000 28.84457 ?  72  GLY   D N     1 
ATOM   4525 C  CA    . GLY   D 2 73  ? 16.71200 29.30100  6.74000   1.000 28.77237 ?  72  GLY   D CA    1 
ATOM   4526 C  C     . GLY   D 2 73  ? 17.51000 28.69500  5.61300   1.000 30.62075 ?  72  GLY   D C     1 
ATOM   4527 O  O     . GLY   D 2 73  ? 18.73100 28.50800  5.76200   1.000 29.63279 ?  72  GLY   D O     1 
ATOM   4528 N  N     . THR   D 2 74  ? 16.87600 28.35300  4.48200   1.000 27.60920 ?  73  THR   D N     1 
ATOM   4529 C  CA    . THR   D 2 74  ? 17.60400 27.66900  3.43300   1.000 27.80089 ?  73  THR   D CA    1 
ATOM   4530 C  C     . THR   D 2 74  ? 17.91800 28.56500  2.23900   1.000 29.41174 ?  73  THR   D C     1 
ATOM   4531 O  O     . THR   D 2 74  ? 18.76400 28.19200  1.41300   1.000 36.19652 ?  73  THR   D O     1 
ATOM   4532 C  CB    . THR   D 2 74  ? 16.81200 26.45000  2.94400   1.000 30.61433 ?  73  THR   D CB    1 
ATOM   4533 O  OG1   . THR   D 2 74  ? 15.67200 26.90000  2.20800   1.000 31.28357 ?  73  THR   D OG1   1 
ATOM   4534 C  CG2   . THR   D 2 74  ? 16.34500 25.61100  4.13600   1.000 26.04986 ?  73  THR   D CG2   1 
ATOM   4535 N  N     . GLY   D 2 75  ? 17.28200 29.72600  2.13800   1.000 29.59138 ?  74  GLY   D N     1 
ATOM   4536 C  CA    . GLY   D 2 75  ? 17.36500 30.51000  0.92300   1.000 33.20327 ?  74  GLY   D CA    1 
ATOM   4537 C  C     . GLY   D 2 75  ? 18.24300 31.73900  1.04300   1.000 34.71160 ?  74  GLY   D C     1 
ATOM   4538 O  O     . GLY   D 2 75  ? 19.23300 31.74700  1.79100   1.000 27.69989 ?  74  GLY   D O     1 
ATOM   4539 N  N     . GLY   D 2 76  ? 17.85200 32.76700  0.30300   1.000 30.36306 ?  75  GLY   D N     1 
ATOM   4540 C  CA    . GLY   D 2 76  ? 18.68800 33.96100  0.21900   1.000 30.19904 ?  75  GLY   D CA    1 
ATOM   4541 C  C     . GLY   D 2 76  ? 19.34000 34.04600  -1.15100  1.000 30.22763 ?  75  GLY   D C     1 
ATOM   4542 O  O     . GLY   D 2 76  ? 19.53000 33.00000  -1.78700  1.000 30.55722 ?  75  GLY   D O     1 
ATOM   4543 N  N     . LYS   D 2 77  ? 19.64200 35.25800  -1.58800  1.000 28.16039 ?  76  LYS   D N     1 
ATOM   4544 C  CA    . LYS   D 2 77  ? 20.35000 35.44200  -2.87100  1.000 27.85258 ?  76  LYS   D CA    1 
ATOM   4545 C  C     . LYS   D 2 77  ? 21.12600 36.75200  -2.79500  1.000 23.49324 ?  76  LYS   D C     1 
ATOM   4546 O  O     . LYS   D 2 77  ? 20.73600 37.62400  -2.03500  1.000 24.21858 ?  76  LYS   D O     1 
ATOM   4547 C  CB    . LYS   D 2 77  ? 19.38100 35.48600  -4.05600  1.000 29.12904 ?  76  LYS   D CB    1 
ATOM   4548 C  CG    . LYS   D 2 77  ? 18.43000 36.65700  -4.11200  1.000 27.76102 ?  76  LYS   D CG    1 
ATOM   4549 C  CD    . LYS   D 2 77  ? 17.64000 36.62600  -5.41000  1.000 30.56869 ?  76  LYS   D CD    1 
ATOM   4550 C  CE    . LYS   D 2 77  ? 16.41400 37.46200  -5.34800  1.000 34.65586 ?  76  LYS   D CE    1 
ATOM   4551 N  NZ    . LYS   D 2 77  ? 15.64200 37.33800  -6.58500  1.000 41.54793 ?  76  LYS   D NZ    1 
ATOM   4552 N  N     . SER   D 2 78  ? 22.17400 36.85500  -3.59900  1.000 24.59795 ?  77  SER   D N     1 
ATOM   4553 C  CA    . SER   D 2 78  ? 22.99500 38.07800  -3.61300  1.000 26.42278 ?  77  SER   D CA    1 
ATOM   4554 C  C     . SER   D 2 78  ? 22.54900 38.99000  -4.74600  1.000 34.18488 ?  77  SER   D C     1 
ATOM   4555 O  O     . SER   D 2 78  ? 21.73800 38.57100  -5.57600  1.000 27.16470 ?  77  SER   D O     1 
ATOM   4556 C  CB    . SER   D 2 78  ? 24.44200 37.75000  -3.82300  1.000 24.39049 ?  77  SER   D CB    1 
ATOM   4557 O  OG    . SER   D 2 78  ? 24.74500 37.50800  -5.18800  1.000 27.71410 ?  77  SER   D OG    1 
ATOM   4558 N  N     . ILE   D 2 79  ? 23.05500 40.20400  -4.72200  1.000 27.41155 ?  78  ILE   D N     1 
ATOM   4559 C  CA    . ILE   D 2 79  ? 22.82500 41.08300  -5.86900  1.000 26.08716 ?  78  ILE   D CA    1 
ATOM   4560 C  C     . ILE   D 2 79  ? 23.63800 40.71400  -7.10100  1.000 28.54703 ?  78  ILE   D C     1 
ATOM   4561 O  O     . ILE   D 2 79  ? 23.46500 41.35900  -8.14200  1.000 32.79174 ?  78  ILE   D O     1 
ATOM   4562 C  CB    . ILE   D 2 79  ? 23.13800 42.54600  -5.49000  1.000 29.46570 ?  78  ILE   D CB    1 
ATOM   4563 C  CG1   . ILE   D 2 79  ? 24.63300 42.70800  -5.17000  1.000 30.12040 ?  78  ILE   D CG1   1 
ATOM   4564 C  CG2   . ILE   D 2 79  ? 22.22600 43.01000  -4.33500  1.000 30.04523 ?  78  ILE   D CG2   1 
ATOM   4565 C  CD1   . ILE   D 2 79  ? 25.07100 44.15700  -5.01500  1.000 33.16927 ?  78  ILE   D CD1   1 
ATOM   4566 N  N     . TYR   D 2 80  ? 24.51700 39.71400  -7.02900  1.000 27.30862 ?  79  TYR   D N     1 
ATOM   4567 C  CA    . TYR   D 2 80  ? 25.32600 39.29700  -8.17700  1.000 31.51393 ?  79  TYR   D CA    1 
ATOM   4568 C  C     . TYR   D 2 80  ? 24.82000 38.03000  -8.86000  1.000 30.24919 ?  79  TYR   D C     1 
ATOM   4569 O  O     . TYR   D 2 80  ? 25.41600 37.58900  -9.85500  1.000 31.22250 ?  79  TYR   D O     1 
ATOM   4570 C  CB    . TYR   D 2 80  ? 26.76800 39.07300  -7.74800  1.000 30.16147 ?  79  TYR   D CB    1 
ATOM   4571 C  CG    . TYR   D 2 80  ? 27.31900 40.21000  -6.94900  1.000 31.24369 ?  79  TYR   D CG    1 
ATOM   4572 C  CD1   . TYR   D 2 80  ? 27.50700 41.45600  -7.52800  1.000 32.25345 ?  79  TYR   D CD1   1 
ATOM   4573 C  CD2   . TYR   D 2 80  ? 27.66000 40.04400  -5.61100  1.000 29.19238 ?  79  TYR   D CD2   1 
ATOM   4574 C  CE1   . TYR   D 2 80  ? 28.01200 42.53500  -6.79900  1.000 35.14060 ?  79  TYR   D CE1   1 
ATOM   4575 C  CE2   . TYR   D 2 80  ? 28.17100 41.10600  -4.88100  1.000 30.43166 ?  79  TYR   D CE2   1 
ATOM   4576 C  CZ    . TYR   D 2 80  ? 28.34400 42.35000  -5.47400  1.000 35.34073 ?  79  TYR   D CZ    1 
ATOM   4577 O  OH    . TYR   D 2 80  ? 28.85400 43.41200  -4.74700  1.000 30.25645 ?  79  TYR   D OH    1 
ATOM   4578 N  N     . GLY   D 2 81  ? 23.81500 37.41300  -8.25800  1.000 31.27672 ?  80  GLY   D N     1 
ATOM   4579 C  CA    . GLY   D 2 81  ? 23.33200 36.10000  -8.69100  1.000 29.45909 ?  80  GLY   D CA    1 
ATOM   4580 C  C     . GLY   D 2 81  ? 23.01000 35.31800  -7.42900  1.000 30.37410 ?  80  GLY   D C     1 
ATOM   4581 O  O     . GLY   D 2 81  ? 23.13200 35.88700  -6.33800  1.000 27.22379 ?  80  GLY   D O     1 
ATOM   4582 N  N     . GLU   D 2 82  ? 22.61600 34.06200  -7.55900  1.000 30.80393 ?  81  GLU   D N     1 
ATOM   4583 C  CA    . GLU   D 2 82  ? 22.20600 33.30900  -6.35500  1.000 32.49759 ?  81  GLU   D CA    1 
ATOM   4584 C  C     . GLU   D 2 82  ? 23.36500 33.35200  -5.35300  1.000 30.55279 ?  81  GLU   D C     1 
ATOM   4585 O  O     . GLU   D 2 82  ? 23.13300 33.64100  -4.17300  1.000 29.56357 ?  81  GLU   D O     1 
ATOM   4586 C  CB    . GLU   D 2 82  ? 21.88100 31.85400  -6.67900  1.000 36.97598 ?  81  GLU   D CB    1 
ATOM   4587 C  CG    . GLU   D 2 82  ? 21.84600 30.95600  -5.44600  1.000 42.18056 ?  81  GLU   D CG    1 
ATOM   4588 C  CD    . GLU   D 2 82  ? 21.15300 29.61500  -5.60400  1.000 50.46710 ?  81  GLU   D CD    1 
ATOM   4589 O  OE1   . GLU   D 2 82  ? 21.62600 28.79500  -6.41500  1.000 49.26044 ?  81  GLU   D OE1   1 
ATOM   4590 O  OE2   . GLU   D 2 82  ? 20.13800 29.39400  -4.91600  1.000 51.19429 -1 81  GLU   D OE2   1 
ATOM   4591 N  N     . LYS   D 2 83  ? 24.56300 33.05300  -5.82500  1.000 24.97066 ?  82  LYS   D N     1 
ATOM   4592 C  CA    . LYS   D 2 83  ? 25.73000 33.01300  -4.92800  1.000 26.62853 ?  82  LYS   D CA    1 
ATOM   4593 C  C     . LYS   D 2 83  ? 26.92000 33.73600  -5.56300  1.000 32.49333 ?  82  LYS   D C     1 
ATOM   4594 O  O     . LYS   D 2 83  ? 26.91300 33.92700  -6.78400  1.000 28.75164 ?  82  LYS   D O     1 
ATOM   4595 C  CB    . LYS   D 2 83  ? 26.11600 31.56400  -4.64900  1.000 34.04087 ?  82  LYS   D CB    1 
ATOM   4596 C  CG    . LYS   D 2 83  ? 25.24400 30.87900  -3.61400  1.000 36.06627 ?  82  LYS   D CG    1 
ATOM   4597 C  CD    . LYS   D 2 83  ? 25.16700 29.36600  -3.75700  1.000 37.86568 ?  82  LYS   D CD    1 
ATOM   4598 C  CE    . LYS   D 2 83  ? 24.06300 28.79500  -2.93100  1.000 45.03225 ?  82  LYS   D CE    1 
ATOM   4599 N  NZ    . LYS   D 2 83  ? 24.48100 27.59300  -2.20400  1.000 51.32952 ?  82  LYS   D NZ    1 
ATOM   4600 N  N     . PHE   D 2 84  ? 27.86400 34.15300  -4.72100  1.000 24.25251 ?  83  PHE   D N     1 
ATOM   4601 C  CA    . PHE   D 2 84  ? 29.09800 34.80900  -5.21700  1.000 25.49548 ?  83  PHE   D CA    1 
ATOM   4602 C  C     . PHE   D 2 84  ? 30.28900 34.29600  -4.42000  1.000 28.63489 ?  83  PHE   D C     1 
ATOM   4603 O  O     . PHE   D 2 84  ? 30.14900 33.75400  -3.32000  1.000 23.48171 ?  83  PHE   D O     1 
ATOM   4604 C  CB    . PHE   D 2 84  ? 29.01500 36.33800  -5.22900  1.000 23.73151 ?  83  PHE   D CB    1 
ATOM   4605 C  CG    . PHE   D 2 84  ? 28.93500 37.04200  -3.88300  1.000 26.31459 ?  83  PHE   D CG    1 
ATOM   4606 C  CD1   . PHE   D 2 84  ? 27.75300 37.06000  -3.15800  1.000 22.18786 ?  83  PHE   D CD1   1 
ATOM   4607 C  CD2   . PHE   D 2 84  ? 30.03700 37.70800  -3.36300  1.000 27.71666 ?  83  PHE   D CD2   1 
ATOM   4608 C  CE1   . PHE   D 2 84  ? 27.68200 37.71600  -1.94200  1.000 25.86037 ?  83  PHE   D CE1   1 
ATOM   4609 C  CE2   . PHE   D 2 84  ? 29.95900 38.35400  -2.14300  1.000 25.21825 ?  83  PHE   D CE2   1 
ATOM   4610 C  CZ    . PHE   D 2 84  ? 28.78400 38.35600  -1.43600  1.000 21.82964 ?  83  PHE   D CZ    1 
ATOM   4611 N  N     . GLU   D 2 85  ? 31.46500 34.50400  -4.98000  1.000 26.42722 ?  84  GLU   D N     1 
ATOM   4612 C  CA    . GLU   D 2 85  ? 32.69400 33.94700  -4.38700  1.000 26.35703 ?  84  GLU   D CA    1 
ATOM   4613 C  C     . GLU   D 2 85  ? 33.14800 34.64200  -3.09700  1.000 27.89152 ?  84  GLU   D C     1 
ATOM   4614 O  O     . GLU   D 2 85  ? 32.69300 35.74600  -2.80100  1.000 27.59008 ?  84  GLU   D O     1 
ATOM   4615 C  CB    . GLU   D 2 85  ? 33.78500 34.07100  -5.45000  1.000 33.47896 ?  84  GLU   D CB    1 
ATOM   4616 C  CG    . GLU   D 2 85  ? 34.12600 35.51300  -5.81000  1.000 38.00899 ?  84  GLU   D CG    1 
ATOM   4617 C  CD    . GLU   D 2 85  ? 33.07800 36.23600  -6.63500  1.000 48.10518 ?  84  GLU   D CD    1 
ATOM   4618 O  OE1   . GLU   D 2 85  ? 32.28800 35.55800  -7.32200  1.000 43.60083 ?  84  GLU   D OE1   1 
ATOM   4619 O  OE2   . GLU   D 2 85  ? 33.04000 37.47500  -6.56800  1.000 50.39271 -1 84  GLU   D OE2   1 
ATOM   4620 N  N     . ASP   D 2 86  ? 33.99800 33.94700  -2.35300  1.000 26.12362 ?  85  ASP   D N     1 
ATOM   4621 C  CA    . ASP   D 2 86  ? 34.59600 34.54800  -1.14300  1.000 24.19445 ?  85  ASP   D CA    1 
ATOM   4622 C  C     . ASP   D 2 86  ? 35.57800 35.63200  -1.59600  1.000 27.27574 ?  85  ASP   D C     1 
ATOM   4623 O  O     . ASP   D 2 86  ? 36.56500 35.29400  -2.25400  1.000 30.20472 ?  85  ASP   D O     1 
ATOM   4624 C  CB    . ASP   D 2 86  ? 35.24100 33.46300  -0.31300  1.000 25.55629 ?  85  ASP   D CB    1 
ATOM   4625 C  CG    . ASP   D 2 86  ? 34.28600 32.40000  0.20200   1.000 28.43456 ?  85  ASP   D CG    1 
ATOM   4626 O  OD1   . ASP   D 2 86  ? 33.21800 32.78200  0.70900   1.000 23.52670 ?  85  ASP   D OD1   1 
ATOM   4627 O  OD2   . ASP   D 2 86  ? 34.62100 31.20700  0.08600   1.000 29.43852 -1 85  ASP   D OD2   1 
ATOM   4628 N  N     . GLU   D 2 87  ? 35.30100 36.88300  -1.25600  1.000 25.11783 ?  86  GLU   D N     1 
ATOM   4629 C  CA    . GLU   D 2 87  ? 36.16500 38.00900  -1.68700  1.000 27.50948 ?  86  GLU   D CA    1 
ATOM   4630 C  C     . GLU   D 2 87  ? 37.56000 37.87000  -1.07800  1.000 26.80640 ?  86  GLU   D C     1 
ATOM   4631 O  O     . GLU   D 2 87  ? 38.52200 37.84300  -1.84200  1.000 27.56702 ?  86  GLU   D O     1 
ATOM   4632 C  CB    . GLU   D 2 87  ? 35.50300 39.31000  -1.26500  1.000 25.83760 ?  86  GLU   D CB    1 
ATOM   4633 C  CG    . GLU   D 2 87  ? 36.19900 40.55900  -1.79200  1.000 33.78818 ?  86  GLU   D CG    1 
ATOM   4634 C  CD    . GLU   D 2 87  ? 35.25600 41.74400  -1.81000  1.000 29.39904 ?  86  GLU   D CD    1 
ATOM   4635 O  OE1   . GLU   D 2 87  ? 34.19200 41.67600  -1.16700  1.000 28.20739 ?  86  GLU   D OE1   1 
ATOM   4636 O  OE2   . GLU   D 2 87  ? 35.58700 42.73000  -2.48200  1.000 34.10787 -1 86  GLU   D OE2   1 
ATOM   4637 N  N     . ASN   D 2 88  ? 37.65400 37.89200  0.24600   1.000 23.29060 ?  87  ASN   D N     1 
ATOM   4638 C  CA    . ASN   D 2 88  ? 38.92000 37.64500  0.92600   1.000 23.52971 ?  87  ASN   D CA    1 
ATOM   4639 C  C     . ASN   D 2 88  ? 38.61000 37.25900  2.36900   1.000 23.03344 ?  87  ASN   D C     1 
ATOM   4640 O  O     . ASN   D 2 88  ? 37.47300 37.35700  2.82900   1.000 25.25229 ?  87  ASN   D O     1 
ATOM   4641 C  CB    . ASN   D 2 88  ? 39.85600 38.86400  0.85300   1.000 26.26023 ?  87  ASN   D CB    1 
ATOM   4642 C  CG    . ASN   D 2 88  ? 39.31300 40.06600  1.59400   1.000 26.99396 ?  87  ASN   D CG    1 
ATOM   4643 O  OD1   . ASN   D 2 88  ? 39.09800 40.00500  2.80400   1.000 25.77480 ?  87  ASN   D OD1   1 
ATOM   4644 N  ND2   . ASN   D 2 88  ? 39.10600 41.16900  0.87700   1.000 29.23925 ?  87  ASN   D ND2   1 
ATOM   4645 N  N     . PHE   D 2 89  ? 39.63600 36.81000  3.07100   1.000 24.84773 ?  88  PHE   D N     1 
ATOM   4646 C  CA    . PHE   D 2 89  ? 39.52400 36.42200  4.46000   1.000 24.17733 ?  88  PHE   D CA    1 
ATOM   4647 C  C     . PHE   D 2 89  ? 40.46800 37.27200  5.30200   1.000 26.02047 ?  88  PHE   D C     1 
ATOM   4648 O  O     . PHE   D 2 89  ? 41.09400 36.78700  6.24900   1.000 28.42545 ?  88  PHE   D O     1 
ATOM   4649 C  CB    . PHE   D 2 89  ? 39.79700 34.93000  4.63300   1.000 24.86388 ?  88  PHE   D CB    1 
ATOM   4650 C  CG    . PHE   D 2 89  ? 38.80200 34.03600  3.91200   1.000 29.51790 ?  88  PHE   D CG    1 
ATOM   4651 C  CD1   . PHE   D 2 89  ? 37.48100 33.91900  4.36100   1.000 24.80106 ?  88  PHE   D CD1   1 
ATOM   4652 C  CD2   . PHE   D 2 89  ? 39.19000 33.32500  2.77800   1.000 30.44356 ?  88  PHE   D CD2   1 
ATOM   4653 C  CE1   . PHE   D 2 89  ? 36.58500 33.10500  3.70500   1.000 26.42849 ?  88  PHE   D CE1   1 
ATOM   4654 C  CE2   . PHE   D 2 89  ? 38.29500 32.51500  2.11400   1.000 27.67149 ?  88  PHE   D CE2   1 
ATOM   4655 C  CZ    . PHE   D 2 89  ? 36.98600 32.38200  2.59600   1.000 28.74400 ?  88  PHE   D CZ    1 
ATOM   4656 N  N     . ILE   D 2 90  ? 40.57600 38.56100  4.95800   1.000 26.21939 ?  89  ILE   D N     1 
ATOM   4657 C  CA    . ILE   D 2 90  ? 41.53600 39.42100  5.65400   1.000 30.23435 ?  89  ILE   D CA    1 
ATOM   4658 C  C     . ILE   D 2 90  ? 41.10300 39.63900  7.09600   1.000 27.22940 ?  89  ILE   D C     1 
ATOM   4659 O  O     . ILE   D 2 90  ? 41.91800 39.53000  8.01300   1.000 27.31283 ?  89  ILE   D O     1 
ATOM   4660 C  CB    . ILE   D 2 90  ? 41.71800 40.75600  4.92500   1.000 29.05709 ?  89  ILE   D CB    1 
ATOM   4661 C  CG1   . ILE   D 2 90  ? 42.45100 40.54700  3.58800   1.000 26.33645 ?  89  ILE   D CG1   1 
ATOM   4662 C  CG2   . ILE   D 2 90  ? 42.54700 41.72800  5.80400   1.000 30.04011 ?  89  ILE   D CG2   1 
ATOM   4663 C  CD1   . ILE   D 2 90  ? 42.24300 41.66200  2.67000   1.000 32.20316 ?  89  ILE   D CD1   1 
ATOM   4664 N  N     . LEU   D 2 91  ? 39.81000 39.89000  7.31700   1.000 25.08101 ?  90  LEU   D N     1 
ATOM   4665 C  CA    . LEU   D 2 91  ? 39.28400 40.21800  8.64700   1.000 24.03798 ?  90  LEU   D CA    1 
ATOM   4666 C  C     . LEU   D 2 91  ? 38.87700 38.95600  9.37600   1.000 27.31237 ?  90  LEU   D C     1 
ATOM   4667 O  O     . LEU   D 2 91  ? 38.43000 37.98200  8.75900   1.000 23.81086 ?  90  LEU   D O     1 
ATOM   4668 C  CB    . LEU   D 2 91  ? 38.11200 41.17600  8.52500   1.000 23.22963 ?  90  LEU   D CB    1 
ATOM   4669 C  CG    . LEU   D 2 91  ? 38.57100 42.50900  7.94500   1.000 28.50823 ?  90  LEU   D CG    1 
ATOM   4670 C  CD1   . LEU   D 2 91  ? 37.39300 43.39700  7.60900   1.000 27.91995 ?  90  LEU   D CD1   1 
ATOM   4671 C  CD2   . LEU   D 2 91  ? 39.50000 43.23400  8.91900   1.000 33.22452 ?  90  LEU   D CD2   1 
ATOM   4672 N  N     . LYS   D 2 92  ? 39.06000 38.96500  10.70100  1.000 22.84459 ?  91  LYS   D N     1 
ATOM   4673 C  CA    . LYS   D 2 92  ? 38.83500 37.77900  11.50300  1.000 23.91595 ?  91  LYS   D CA    1 
ATOM   4674 C  C     . LYS   D 2 92  ? 37.61600 37.96200  12.40000  1.000 22.43209 ?  91  LYS   D C     1 
ATOM   4675 O  O     . LYS   D 2 92  ? 37.14600 39.07300  12.64000  1.000 23.92082 ?  91  LYS   D O     1 
ATOM   4676 C  CB    . LYS   D 2 92  ? 40.07100 37.45500  12.36200  1.000 25.24373 ?  91  LYS   D CB    1 
ATOM   4677 C  CG    . LYS   D 2 92  ? 41.39400 37.35600  11.58700  1.000 33.13760 ?  91  LYS   D CG    1 
ATOM   4678 C  CD    . LYS   D 2 92  ? 41.36800 36.32500  10.45600  1.000 29.24780 ?  91  LYS   D CD    1 
ATOM   4679 C  CE    . LYS   D 2 92  ? 42.80100 36.19800  9.84300   1.000 35.21757 ?  91  LYS   D CE    1 
ATOM   4680 N  NZ    . LYS   D 2 92  ? 42.81800 36.09600  8.32800   1.000 37.24945 ?  91  LYS   D NZ    1 
ATOM   4681 N  N     . HIS   D 2 93  ? 37.13100 36.84200  12.91400  1.000 21.74261 ?  92  HIS   D N     1 
ATOM   4682 C  CA    . HIS   D 2 93  ? 36.02600 36.80100  13.88500  1.000 21.50314 ?  92  HIS   D CA    1 
ATOM   4683 C  C     . HIS   D 2 93  ? 36.57400 37.02500  15.30000  1.000 23.54613 ?  92  HIS   D C     1 
ATOM   4684 O  O     . HIS   D 2 93  ? 36.79000 36.09200  16.07300  1.000 28.75963 ?  92  HIS   D O     1 
ATOM   4685 C  CB    . HIS   D 2 93  ? 35.30500 35.46900  13.77300  1.000 20.97691 ?  92  HIS   D CB    1 
ATOM   4686 C  CG    . HIS   D 2 93  ? 34.73300 35.19100  12.40400  1.000 22.54196 ?  92  HIS   D CG    1 
ATOM   4687 N  ND1   . HIS   D 2 93  ? 35.48300 34.68300  11.35700  1.000 22.29587 ?  92  HIS   D ND1   1 
ATOM   4688 C  CD2   . HIS   D 2 93  ? 33.47100 35.32300  11.92800  1.000 20.97986 ?  92  HIS   D CD2   1 
ATOM   4689 C  CE1   . HIS   D 2 93  ? 34.70500 34.54100  10.28500  1.000 20.85432 ?  92  HIS   D CE1   1 
ATOM   4690 N  NE2   . HIS   D 2 93  ? 33.47700 34.90800  10.61400  1.000 20.06909 ?  92  HIS   D NE2   1 
ATOM   4691 N  N     . THR   D 2 94  ? 36.77800 38.29700  15.65100  1.000 24.06731 ?  93  THR   D N     1 
ATOM   4692 C  CA    . THR   D 2 94  ? 37.58400 38.64400  16.81500  1.000 26.22386 ?  93  THR   D CA    1 
ATOM   4693 C  C     . THR   D 2 94  ? 36.78200 38.82100  18.09300  1.000 26.83895 ?  93  THR   D C     1 
ATOM   4694 O  O     . THR   D 2 94  ? 37.38600 38.87200  19.17800  1.000 28.81835 ?  93  THR   D O     1 
ATOM   4695 C  CB    . THR   D 2 94  ? 38.34600 39.94200  16.55800  1.000 23.23188 ?  93  THR   D CB    1 
ATOM   4696 O  OG1   . THR   D 2 94  ? 37.41500 40.94800  16.15700  1.000 29.29311 ?  93  THR   D OG1   1 
ATOM   4697 C  CG2   . THR   D 2 94  ? 39.38300 39.78000  15.43400  1.000 28.06897 ?  93  THR   D CG2   1 
ATOM   4698 N  N     . GLY   D 2 95  ? 35.46100 38.91700  18.01500  1.000 24.62003 ?  94  GLY   D N     1 
ATOM   4699 C  CA    . GLY   D 2 95  ? 34.69000 39.17700  19.20900  1.000 23.68839 ?  94  GLY   D CA    1 
ATOM   4700 C  C     . GLY   D 2 95  ? 33.26800 39.54800  18.87900  1.000 23.52968 ?  94  GLY   D C     1 
ATOM   4701 O  O     . GLY   D 2 95  ? 32.84100 39.55100  17.71800  1.000 24.14462 ?  94  GLY   D O     1 
ATOM   4702 N  N     . PRO   D 2 96  ? 32.50100 39.89200  19.91400  1.000 21.98154 ?  95  PRO   D N     1 
ATOM   4703 C  CA    . PRO   D 2 96  ? 31.09100 40.22500  19.71700  1.000 22.65411 ?  95  PRO   D CA    1 
ATOM   4704 C  C     . PRO   D 2 96  ? 30.94300 41.40000  18.76900  1.000 22.24838 ?  95  PRO   D C     1 
ATOM   4705 O  O     . PRO   D 2 96  ? 31.72800 42.34900  18.80000  1.000 25.73949 ?  95  PRO   D O     1 
ATOM   4706 C  CB    . PRO   D 2 96  ? 30.60200 40.59000  21.13100  1.000 23.80803 ?  95  PRO   D CB    1 
ATOM   4707 C  CG    . PRO   D 2 96  ? 31.60300 40.01100  22.06100  1.000 24.18540 ?  95  PRO   D CG    1 
ATOM   4708 C  CD    . PRO   D 2 96  ? 32.92000 39.98900  21.32500  1.000 24.95165 ?  95  PRO   D CD    1 
ATOM   4709 N  N     . GLY   D 2 97  ? 29.87800 41.36500  17.95900  1.000 20.98234 ?  96  GLY   D N     1 
ATOM   4710 C  CA    . GLY   D 2 97  ? 29.58400 42.47300  17.07900  1.000 22.82533 ?  96  GLY   D CA    1 
ATOM   4711 C  C     . GLY   D 2 97  ? 30.06000 42.27400  15.65500  1.000 20.75734 ?  96  GLY   D C     1 
ATOM   4712 O  O     . GLY   D 2 97  ? 29.62100 43.00000  14.76800  1.000 21.35921 ?  96  GLY   D O     1 
ATOM   4713 N  N     . ILE   D 2 98  ? 30.91300 41.28400  15.41800  1.000 21.12662 ?  97  ILE   D N     1 
ATOM   4714 C  CA    . ILE   D 2 98  ? 31.42200 41.04600  14.07100  1.000 20.10111 ?  97  ILE   D CA    1 
ATOM   4715 C  C     . ILE   D 2 98  ? 30.28500 40.60200  13.16500  1.000 19.80731 ?  97  ILE   D C     1 
ATOM   4716 O  O     . ILE   D 2 98  ? 29.46700 39.76700  13.55200  1.000 19.55873 ?  97  ILE   D O     1 
ATOM   4717 C  CB    . ILE   D 2 98  ? 32.52500 39.98300  14.12900  1.000 20.60191 ?  97  ILE   D CB    1 
ATOM   4718 C  CG1   . ILE   D 2 98  ? 33.79300 40.54900  14.80600  1.000 21.28431 ?  97  ILE   D CG1   1 
ATOM   4719 C  CG2   . ILE   D 2 98  ? 32.79800 39.45500  12.73000  1.000 20.68541 ?  97  ILE   D CG2   1 
ATOM   4720 C  CD1   . ILE   D 2 98  ? 34.42400 41.71000  14.00600  1.000 30.66950 ?  97  ILE   D CD1   1 
ATOM   4721 N  N     . LEU   D 2 99  ? 30.27000 41.12100  11.92600  1.000 21.68967 ?  98  LEU   D N     1 
ATOM   4722 C  CA    . LEU   D 2 99  ? 29.26200 40.79800  10.91500  1.000 21.07974 ?  98  LEU   D CA    1 
ATOM   4723 C  C     . LEU   D 2 99  ? 29.93400 40.02100  9.78600   1.000 19.79699 ?  98  LEU   D C     1 
ATOM   4724 O  O     . LEU   D 2 99  ? 30.93500 40.48600  9.22300   1.000 20.09563 ?  98  LEU   D O     1 
ATOM   4725 C  CB    . LEU   D 2 99  ? 28.62800 42.07200  10.36900  1.000 19.68180 ?  98  LEU   D CB    1 
ATOM   4726 C  CG    . LEU   D 2 99  ? 27.55900 41.93300  9.27400   1.000 19.92558 ?  98  LEU   D CG    1 
ATOM   4727 C  CD1   . LEU   D 2 99  ? 26.33400 41.16900  9.74700   1.000 22.52175 ?  98  LEU   D CD1   1 
ATOM   4728 C  CD2   . LEU   D 2 99  ? 27.17200 43.35600  8.78600   1.000 20.88331 ?  98  LEU   D CD2   1 
ATOM   4729 N  N     . SER   D 2 100 ? 29.38800 38.84900  9.46200   1.000 19.61917 ?  99  SER   D N     1 
ATOM   4730 C  CA    . SER   D 2 100 ? 30.14600 37.89900  8.63200   1.000 20.23658 ?  99  SER   D CA    1 
ATOM   4731 C  C     . SER   D 2 100 ? 29.12700 37.13200  7.78700   1.000 19.62452 ?  99  SER   D C     1 
ATOM   4732 O  O     . SER   D 2 100 ? 27.95700 37.04800  8.14500   1.000 19.38084 ?  99  SER   D O     1 
ATOM   4733 C  CB    . SER   D 2 100 ? 31.02000 36.98400  9.51600   1.000 19.94762 ?  99  SER   D CB    1 
ATOM   4734 O  OG    . SER   D 2 100 ? 31.73700 36.00900  8.73500   1.000 20.83607 ?  99  SER   D OG    1 
ATOM   4735 N  N     . MET   D 2 101 ? 29.55700 36.62100  6.62900   1.000 19.82330 ?  100 MET   D N     1 
ATOM   4736 C  CA    . MET   D 2 101 ? 28.62200 35.92300  5.72900   1.000 19.75888 ?  100 MET   D CA    1 
ATOM   4737 C  C     . MET   D 2 101 ? 28.44300 34.45800  6.09600   1.000 19.65275 ?  100 MET   D C     1 
ATOM   4738 O  O     . MET   D 2 101 ? 29.41000 33.75300  6.37500   1.000 21.21135 ?  100 MET   D O     1 
ATOM   4739 C  CB    . MET   D 2 101 ? 29.11700 35.97200  4.28700   1.000 22.55443 ?  100 MET   D CB    1 
ATOM   4740 C  CG    . MET   D 2 101 ? 29.06100 37.34400  3.71800   1.000 20.19588 ?  100 MET   D CG    1 
ATOM   4741 S  SD    . MET   D 2 101 ? 27.43000 38.04500  3.65000   1.000 23.98957 ?  100 MET   D SD    1 
ATOM   4742 C  CE    . MET   D 2 101 ? 26.67400 37.06600  2.30600   1.000 23.27963 ?  100 MET   D CE    1 
ATOM   4743 N  N     . ALA   D 2 102 ? 27.20000 33.99200  6.04600   1.000 19.47382 ?  101 ALA   D N     1 
ATOM   4744 C  CA    . ALA   D 2 102 ? 26.96900 32.56100  6.17400   1.000 19.43882 ?  101 ALA   D CA    1 
ATOM   4745 C  C     . ALA   D 2 102 ? 27.20300 31.92500  4.80500   1.000 22.64562 ?  101 ALA   D C     1 
ATOM   4746 O  O     . ALA   D 2 102 ? 27.11500 32.59400  3.78000   1.000 23.00404 ?  101 ALA   D O     1 
ATOM   4747 C  CB    . ALA   D 2 102 ? 25.53300 32.26100  6.61600   1.000 20.44504 ?  101 ALA   D CB    1 
ATOM   4748 N  N     . ASN   D 2 103 ? 27.44600 30.62400  4.79300   1.000 21.84372 ?  102 ASN   D N     1 
ATOM   4749 C  CA    . ASN   D 2 103 ? 27.64700 29.93900  3.52100   1.000 25.14201 ?  102 ASN   D CA    1 
ATOM   4750 C  C     . ASN   D 2 103 ? 27.47500 28.43800  3.72300   1.000 24.01651 ?  102 ASN   D C     1 
ATOM   4751 O  O     . ASN   D 2 103 ? 27.29500 27.94800  4.84100   1.000 24.98847 ?  102 ASN   D O     1 
ATOM   4752 C  CB    . ASN   D 2 103 ? 29.01800 30.29300  2.91800   1.000 24.42683 ?  102 ASN   D CB    1 
ATOM   4753 C  CG    . ASN   D 2 103 ? 30.16900 29.78800  3.74200   1.000 23.59289 ?  102 ASN   D CG    1 
ATOM   4754 O  OD1   . ASN   D 2 103 ? 30.24100 28.60700  4.08600   1.000 26.72693 ?  102 ASN   D OD1   1 
ATOM   4755 N  ND2   . ASN   D 2 103 ? 31.13100 30.68700  4.03400   1.000 26.21640 ?  102 ASN   D ND2   1 
ATOM   4756 N  N     . ALA   D 2 104 ? 27.51800 27.71800  2.61400   1.000 26.55560 ?  103 ALA   D N     1 
ATOM   4757 C  CA    . ALA   D 2 104 ? 27.42100 26.27100  2.58900   1.000 29.20440 ?  103 ALA   D CA    1 
ATOM   4758 C  C     . ALA   D 2 104 ? 28.69600 25.65500  2.01700   1.000 36.28561 ?  103 ALA   D C     1 
ATOM   4759 O  O     . ALA   D 2 104 ? 28.65000 24.63900  1.32300   1.000 33.54159 ?  103 ALA   D O     1 
ATOM   4760 C  CB    . ALA   D 2 104 ? 26.19500 25.83300  1.78800   1.000 29.57701 ?  103 ALA   D CB    1 
ATOM   4761 N  N     . GLY   D 2 105 ? 29.84900 26.27400  2.29500   1.000 28.94630 ?  104 GLY   D N     1 
ATOM   4762 C  CA    . GLY   D 2 105 ? 31.12900 25.84400  1.76500   1.000 30.89157 ?  104 GLY   D CA    1 
ATOM   4763 C  C     . GLY   D 2 105 ? 31.75500 26.94300  0.91100   1.000 25.67408 ?  104 GLY   D C     1 
ATOM   4764 O  O     . GLY   D 2 105 ? 31.18100 28.02900  0.75200   1.000 26.27278 ?  104 GLY   D O     1 
ATOM   4765 N  N     . PRO   D 2 106 ? 32.93600 26.69300  0.34800   1.000 30.65054 ?  105 PRO   D N     1 
ATOM   4766 C  CA    . PRO   D 2 106 ? 33.62300 27.74300  -0.41800  1.000 26.16749 ?  105 PRO   D CA    1 
ATOM   4767 C  C     . PRO   D 2 106 ? 32.75100 28.37000  -1.49000  1.000 26.30940 ?  105 PRO   D C     1 
ATOM   4768 O  O     . PRO   D 2 106 ? 32.04400 27.67500  -2.21600  1.000 26.01848 ?  105 PRO   D O     1 
ATOM   4769 C  CB    . PRO   D 2 106 ? 34.80200 26.99800  -1.05600  1.000 30.19887 ?  105 PRO   D CB    1 
ATOM   4770 C  CG    . PRO   D 2 106 ? 35.11900 25.92000  -0.05300  1.000 32.35196 ?  105 PRO   D CG    1 
ATOM   4771 C  CD    . PRO   D 2 106 ? 33.76100 25.47900  0.48800   1.000 34.28138 ?  105 PRO   D CD    1 
ATOM   4772 N  N     . ASN   D 2 107 ? 32.86300 29.69400  -1.62200  1.000 23.63977 ?  106 ASN   D N     1 
ATOM   4773 C  CA    . ASN   D 2 107 ? 32.22800 30.44000  -2.73800  1.000 25.82282 ?  106 ASN   D CA    1 
ATOM   4774 C  C     . ASN   D 2 107 ? 30.72100 30.21500  -2.83600  1.000 27.39270 ?  106 ASN   D C     1 
ATOM   4775 O  O     . ASN   D 2 107 ? 30.22300 30.03500  -3.95300  1.000 27.90162 ?  106 ASN   D O     1 
ATOM   4776 C  CB    . ASN   D 2 107 ? 32.93300 30.11100  -4.04600  1.000 27.58623 ?  106 ASN   D CB    1 
ATOM   4777 C  CG    . ASN   D 2 107 ? 34.41400 30.39300  -3.97100  1.000 30.43791 ?  106 ASN   D CG    1 
ATOM   4778 O  OD1   . ASN   D 2 107 ? 34.82000 31.44900  -3.48100  1.000 26.40955 ?  106 ASN   D OD1   1 
ATOM   4779 N  ND2   . ASN   D 2 107 ? 35.23300 29.46800  -4.44500  1.000 29.21398 ?  106 ASN   D ND2   1 
ATOM   4780 N  N     . THR   D 2 108 ? 30.02500 30.30900  -1.70700  1.000 24.75643 ?  107 THR   D N     1 
ATOM   4781 C  CA    . THR   D 2 108 ? 28.56300 30.17600  -1.75400  1.000 27.38960 ?  107 THR   D CA    1 
ATOM   4782 C  C     . THR   D 2 108 ? 27.88100 31.28200  -0.95200  1.000 25.82495 ?  107 THR   D C     1 
ATOM   4783 O  O     . THR   D 2 108 ? 26.83100 31.06700  -0.32200  1.000 25.11834 ?  107 THR   D O     1 
ATOM   4784 C  CB    . THR   D 2 108 ? 28.11000 28.79500  -1.25700  1.000 29.27847 ?  107 THR   D CB    1 
ATOM   4785 O  OG1   . THR   D 2 108 ? 28.60900 28.55300  0.06100   1.000 28.50079 ?  107 THR   D OG1   1 
ATOM   4786 C  CG2   . THR   D 2 108 ? 28.59300 27.71400  -2.18500  1.000 28.94469 ?  107 THR   D CG2   1 
ATOM   4787 N  N     . ASN   D 2 109 ? 28.45700 32.47000  -0.98700  1.000 25.10554 ?  108 ASN   D N     1 
ATOM   4788 C  CA    . ASN   D 2 109 ? 27.81000 33.60800  -0.29800  1.000 23.59465 ?  108 ASN   D CA    1 
ATOM   4789 C  C     . ASN   D 2 109 ? 26.52800 34.01000  -1.02500  1.000 24.20938 ?  108 ASN   D C     1 
ATOM   4790 O  O     . ASN   D 2 109 ? 26.56700 34.12600  -2.24400  1.000 27.19304 ?  108 ASN   D O     1 
ATOM   4791 C  CB    . ASN   D 2 109 ? 28.74200 34.80000  -0.20100  1.000 24.62657 ?  108 ASN   D CB    1 
ATOM   4792 C  CG    . ASN   D 2 109 ? 30.04900 34.46200  0.46200   1.000 23.66391 ?  108 ASN   D CG    1 
ATOM   4793 O  OD1   . ASN   D 2 109 ? 30.09700 34.33500  1.68600   1.000 23.93010 ?  108 ASN   D OD1   1 
ATOM   4794 N  ND2   . ASN   D 2 109 ? 31.10700 34.32400  -0.32200  1.000 23.99416 ?  108 ASN   D ND2   1 
ATOM   4795 N  N     . GLY   D 2 110 ? 25.43700 34.21700  -0.28700  1.000 20.45594 ?  109 GLY   D N     1 
ATOM   4796 C  CA    . GLY   D 2 110 ? 24.20500 34.72700  -0.90000  1.000 25.66681 ?  109 GLY   D CA    1 
ATOM   4797 C  C     . GLY   D 2 110 ? 23.75300 35.96000  -0.15300  1.000 23.56763 ?  109 GLY   D C     1 
ATOM   4798 O  O     . GLY   D 2 110 ? 24.35200 37.01900  -0.35500  1.000 22.77864 ?  109 GLY   D O     1 
ATOM   4799 N  N     . SER   D 2 111 ? 22.74700 35.80900  0.69900   1.000 21.09623 ?  110 SER   D N     1 
ATOM   4800 C  CA    . SER   D 2 111 ? 22.36600 36.93700  1.54800   1.000 21.37455 ?  110 SER   D CA    1 
ATOM   4801 C  C     . SER   D 2 111 ? 22.42700 36.63300  3.03300   1.000 21.29963 ?  110 SER   D C     1 
ATOM   4802 O  O     . SER   D 2 111 ? 22.40700 37.59100  3.84200   1.000 19.54302 ?  110 SER   D O     1 
ATOM   4803 C  CB    . SER   D 2 111 ? 20.94400 37.40600  1.23100   1.000 23.63064 ?  110 SER   D CB    1 
ATOM   4804 O  OG    . SER   D 2 111 ? 20.09000 36.29700  1.34900   1.000 22.39066 ?  110 SER   D OG    1 
ATOM   4805 N  N     . GLN   D 2 112 ? 22.44100 35.35500  3.42400   1.000 19.29769 ?  111 GLN   D N     1 
ATOM   4806 C  CA    . GLN   D 2 112 ? 22.47700 35.05000  4.86300   1.000 19.09374 ?  111 GLN   D CA    1 
ATOM   4807 C  C     . GLN   D 2 112 ? 23.78000 35.53900  5.50600   1.000 19.57741 ?  111 GLN   D C     1 
ATOM   4808 O  O     . GLN   D 2 112 ? 24.86300 35.50400  4.92000   1.000 19.32032 ?  111 GLN   D O     1 
ATOM   4809 C  CB    . GLN   D 2 112 ? 22.27700 33.56900  5.13100   1.000 19.41816 ?  111 GLN   D CB    1 
ATOM   4810 C  CG    . GLN   D 2 112 ? 20.85400 33.09200  4.84100   1.000 20.61125 ?  111 GLN   D CG    1 
ATOM   4811 C  CD    . GLN   D 2 112 ? 20.59600 31.68400  5.37200   1.000 22.85746 ?  111 GLN   D CD    1 
ATOM   4812 O  OE1   . GLN   D 2 112 ? 20.97800 31.35100  6.50600   1.000 20.33209 ?  111 GLN   D OE1   1 
ATOM   4813 N  NE2   . GLN   D 2 112 ? 19.96200 30.85700  4.56100   1.000 23.68067 ?  111 GLN   D NE2   1 
ATOM   4814 N  N     . PHE   D 2 113 ? 23.64400 35.97700  6.75400   1.000 18.94047 ?  112 PHE   D N     1 
ATOM   4815 C  CA    . PHE   D 2 113 ? 24.74000 36.60800  7.46800   1.000 19.37579 ?  112 PHE   D CA    1 
ATOM   4816 C  C     . PHE   D 2 113 ? 24.58100 36.20700  8.92000   1.000 18.83427 ?  112 PHE   D C     1 
ATOM   4817 O  O     . PHE   D 2 113 ? 23.53400 35.71200  9.32700   1.000 18.70032 ?  112 PHE   D O     1 
ATOM   4818 C  CB    . PHE   D 2 113 ? 24.70200 38.13900  7.35100   1.000 19.04615 ?  112 PHE   D CB    1 
ATOM   4819 C  CG    . PHE   D 2 113 ? 23.42800 38.73000  7.91900   1.000 19.31326 ?  112 PHE   D CG    1 
ATOM   4820 C  CD1   . PHE   D 2 113 ? 22.28400 38.85300  7.13200   1.000 21.04176 ?  112 PHE   D CD1   1 
ATOM   4821 C  CD2   . PHE   D 2 113 ? 23.35200 39.08500  9.26900   1.000 20.27443 ?  112 PHE   D CD2   1 
ATOM   4822 C  CE1   . PHE   D 2 113 ? 21.11200 39.34000  7.67800   1.000 20.15757 ?  112 PHE   D CE1   1 
ATOM   4823 C  CE2   . PHE   D 2 113 ? 22.20600 39.56200  9.82400   1.000 20.62170 ?  112 PHE   D CE2   1 
ATOM   4824 C  CZ    . PHE   D 2 113 ? 21.05600 39.69000  9.03000   1.000 23.46479 ?  112 PHE   D CZ    1 
ATOM   4825 N  N     . PHE   D 2 114 ? 25.59700 36.50500  9.71500   1.000 18.89765 ?  113 PHE   D N     1 
ATOM   4826 C  CA    . PHE   D 2 114 ? 25.46800 36.30500  11.16000  1.000 18.79737 ?  113 PHE   D CA    1 
ATOM   4827 C  C     . PHE   D 2 114 ? 26.19200 37.43100  11.87400  1.000 18.90088 ?  113 PHE   D C     1 
ATOM   4828 O  O     . PHE   D 2 114 ? 27.11000 38.04800  11.32200  1.000 19.07750 ?  113 PHE   D O     1 
ATOM   4829 C  CB    . PHE   D 2 114 ? 25.94100 34.87700  11.60800  1.000 19.25681 ?  113 PHE   D CB    1 
ATOM   4830 C  CG    . PHE   D 2 114 ? 27.40400 34.58700  11.35000  1.000 18.96470 ?  113 PHE   D CG    1 
ATOM   4831 C  CD1   . PHE   D 2 114 ? 27.86900 34.28300  10.07700  1.000 21.88149 ?  113 PHE   D CD1   1 
ATOM   4832 C  CD2   . PHE   D 2 114 ? 28.33400 34.61200  12.38800  1.000 20.37933 ?  113 PHE   D CD2   1 
ATOM   4833 C  CE1   . PHE   D 2 114 ? 29.21400 34.03600  9.84000   1.000 19.31116 ?  113 PHE   D CE1   1 
ATOM   4834 C  CE2   . PHE   D 2 114 ? 29.67900 34.36800  12.16900  1.000 19.22367 ?  113 PHE   D CE2   1 
ATOM   4835 C  CZ    . PHE   D 2 114 ? 30.13900 34.06400  10.90500  1.000 19.44589 ?  113 PHE   D CZ    1 
ATOM   4836 N  N     . ILE   D 2 115 ? 25.72900 37.72100  13.08800  1.000 18.83746 ?  114 ILE   D N     1 
ATOM   4837 C  CA    . ILE   D 2 115 ? 26.33300 38.70700  13.98500  1.000 18.97617 ?  114 ILE   D CA    1 
ATOM   4838 C  C     . ILE   D 2 115 ? 26.87000 37.89700  15.15300  1.000 19.54103 ?  114 ILE   D C     1 
ATOM   4839 O  O     . ILE   D 2 115 ? 26.10100 37.17600  15.79700  1.000 20.34559 ?  114 ILE   D O     1 
ATOM   4840 C  CB    . ILE   D 2 115 ? 25.29100 39.72500  14.47200  1.000 18.92682 ?  114 ILE   D CB    1 
ATOM   4841 C  CG1   . ILE   D 2 115 ? 24.59800 40.42800  13.31100  1.000 19.11443 ?  114 ILE   D CG1   1 
ATOM   4842 C  CG2   . ILE   D 2 115 ? 25.95500 40.75300  15.41800  1.000 21.91005 ?  114 ILE   D CG2   1 
ATOM   4843 C  CD1   . ILE   D 2 115 ? 23.31000 41.17300  13.75300  1.000 21.94622 ?  114 ILE   D CD1   1 
ATOM   4844 N  N     . CYS   D 2 116 ? 28.16600 37.96700  15.39600  1.000 19.76251 ?  115 CYS   D N     1 
ATOM   4845 C  CA    . CYS   D 2 116 ? 28.74100 37.22500  16.51100  1.000 21.86043 ?  115 CYS   D CA    1 
ATOM   4846 C  C     . CYS   D 2 116 ? 28.36600 37.87200  17.82800  1.000 22.49339 ?  115 CYS   D C     1 
ATOM   4847 O  O     . CYS   D 2 116 ? 28.34000 39.09600  17.94200  1.000 23.95337 ?  115 CYS   D O     1 
ATOM   4848 C  CB    . CYS   D 2 116 ? 30.24800 37.22100  16.42800  1.000 21.04338 ?  115 CYS   D CB    1 
ATOM   4849 S  SG    . CYS   D 2 116 ? 30.86200 36.45200  14.92500  1.000 26.01930 ?  115 CYS   D SG    1 
ATOM   4850 N  N     . THR   D 2 117 ? 28.10300 37.04400  18.83300  1.000 21.12691 ?  116 THR   D N     1 
ATOM   4851 C  CA    . THR   D 2 117 ? 27.91500 37.53800  20.19500  1.000 22.83354 ?  116 THR   D CA    1 
ATOM   4852 C  C     . THR   D 2 117 ? 29.09300 37.13500  21.07500  1.000 25.31263 ?  116 THR   D C     1 
ATOM   4853 O  O     . THR   D 2 117 ? 29.06000 37.35200  22.29700  1.000 28.03474 ?  116 THR   D O     1 
ATOM   4854 C  CB    . THR   D 2 117 ? 26.59000 37.05500  20.78600  1.000 25.84520 ?  116 THR   D CB    1 
ATOM   4855 O  OG1   . THR   D 2 117 ? 26.56500 35.62000  20.84500  1.000 23.98574 ?  116 THR   D OG1   1 
ATOM   4856 C  CG2   . THR   D 2 117 ? 25.38500 37.56100  19.94800  1.000 30.17757 ?  116 THR   D CG2   1 
ATOM   4857 N  N     . ALA   D 2 118 ? 30.14700 36.59600  20.46400  1.000 23.45950 ?  117 ALA   D N     1 
ATOM   4858 C  CA    . ALA   D 2 118 ? 31.35700 36.13700  21.13500  1.000 22.18890 ?  117 ALA   D CA    1 
ATOM   4859 C  C     . ALA   D 2 118 ? 32.43100 35.95800  20.06500  1.000 23.04688 ?  117 ALA   D C     1 
ATOM   4860 O  O     . ALA   D 2 118 ? 32.15100 35.99500  18.86500  1.000 25.44751 ?  117 ALA   D O     1 
ATOM   4861 C  CB    . ALA   D 2 118 ? 31.11200 34.81400  21.87000  1.000 23.48203 ?  117 ALA   D CB    1 
ATOM   4862 N  N     . LYS   D 2 119 ? 33.65900 35.73500  20.49700  1.000 24.09429 ?  118 LYS   D N     1 
ATOM   4863 C  CA    . LYS   D 2 119 ? 34.70500 35.38300  19.53000  1.000 24.34048 ?  118 LYS   D CA    1 
ATOM   4864 C  C     . LYS   D 2 119 ? 34.44100 33.98800  18.93800  1.000 24.16640 ?  118 LYS   D C     1 
ATOM   4865 O  O     . LYS   D 2 119 ? 34.18900 33.02600  19.66900  1.000 27.50173 ?  118 LYS   D O     1 
ATOM   4866 C  CB    . LYS   D 2 119 ? 36.08000 35.42300  20.21200  1.000 24.50789 ?  118 LYS   D CB    1 
ATOM   4867 C  CG    . LYS   D 2 119 ? 37.26700 35.17900  19.28500  1.000 30.30225 ?  118 LYS   D CG    1 
ATOM   4868 C  CD    . LYS   D 2 119 ? 38.60500 35.47200  20.01500  1.000 38.56033 ?  118 LYS   D CD    1 
ATOM   4869 C  CE    . LYS   D 2 119 ? 39.31700 34.18700  20.42400  1.000 41.09997 ?  118 LYS   D CE    1 
ATOM   4870 N  NZ    . LYS   D 2 119 ? 40.48600 33.88000  19.53700  1.000 50.71861 ?  118 LYS   D NZ    1 
ATOM   4871 N  N     . THR   D 2 120 ? 34.51700 33.85900  17.61200  1.000 26.87284 ?  119 THR   D N     1 
ATOM   4872 C  CA    . THR   D 2 120 ? 34.29100 32.56900  16.92700  1.000 24.73423 ?  119 THR   D CA    1 
ATOM   4873 C  C     . THR   D 2 120 ? 35.45500 32.31400  15.95100  1.000 25.21598 ?  119 THR   D C     1 
ATOM   4874 O  O     . THR   D 2 120 ? 35.27800 32.29800  14.72400  1.000 26.05658 ?  119 THR   D O     1 
ATOM   4875 C  CB    . THR   D 2 120 ? 32.95000 32.53700  16.18500  1.000 24.90901 ?  119 THR   D CB    1 
ATOM   4876 O  OG1   . THR   D 2 120 ? 32.93700 33.59400  15.19800  1.000 24.48176 ?  119 THR   D OG1   1 
ATOM   4877 C  CG2   . THR   D 2 120 ? 31.83600 32.69200  17.16300  1.000 24.19523 ?  119 THR   D CG2   1 
ATOM   4878 N  N     . GLU   D 2 121 ? 36.63900 32.07200  16.51800  1.000 27.28276 ?  120 GLU   D N     1 
ATOM   4879 C  CA    . GLU   D 2 121 ? 37.86700 32.10800  15.73100  1.000 28.36561 ?  120 GLU   D CA    1 
ATOM   4880 C  C     . GLU   D 2 121 ? 37.95700 30.94800  14.74500  1.000 23.36657 ?  120 GLU   D C     1 
ATOM   4881 O  O     . GLU   D 2 121 ? 38.62300 31.08300  13.71600  1.000 24.58380 ?  120 GLU   D O     1 
ATOM   4882 C  CB    . GLU   D 2 121 ? 39.08700 32.12300  16.66300  1.000 31.95320 ?  120 GLU   D CB    1 
ATOM   4883 C  CG    . GLU   D 2 121 ? 39.28900 30.86700  17.52600  1.000 41.06205 ?  120 GLU   D CG    1 
ATOM   4884 C  CD    . GLU   D 2 121 ? 38.32200 30.71600  18.74300  1.000 46.29767 ?  120 GLU   D CD    1 
ATOM   4885 O  OE1   . GLU   D 2 121 ? 37.52300 31.63700  19.07700  1.000 37.47497 ?  120 GLU   D OE1   1 
ATOM   4886 O  OE2   . GLU   D 2 121 ? 38.37400 29.63400  19.38300  1.000 52.11586 -1 120 GLU   D OE2   1 
ATOM   4887 N  N     . TRP   D 2 122 ? 37.32700 29.80800  15.04700  1.000 25.22758 ?  121 TRP   D N     1 
ATOM   4888 C  CA    . TRP   D 2 122 ? 37.38700 28.65300  14.15000  1.000 27.65775 ?  121 TRP   D CA    1 
ATOM   4889 C  C     . TRP   D 2 122 ? 36.65300 28.89800  12.82900  1.000 26.88601 ?  121 TRP   D C     1 
ATOM   4890 O  O     . TRP   D 2 122 ? 36.78100 28.07900  11.90600  1.000 28.87794 ?  121 TRP   D O     1 
ATOM   4891 C  CB    . TRP   D 2 122 ? 36.79700 27.40900  14.84800  1.000 27.06287 ?  121 TRP   D CB    1 
ATOM   4892 C  CG    . TRP   D 2 122 ? 35.30300 27.49800  15.10600  1.000 28.74920 ?  121 TRP   D CG    1 
ATOM   4893 C  CD1   . TRP   D 2 122 ? 34.27800 27.04100  14.28500  1.000 28.21201 ?  121 TRP   D CD1   1 
ATOM   4894 C  CD2   . TRP   D 2 122 ? 34.66000 28.11700  16.23500  1.000 27.28422 ?  121 TRP   D CD2   1 
ATOM   4895 N  NE1   . TRP   D 2 122 ? 33.06500 27.33600  14.86400  1.000 27.26097 ?  121 TRP   D NE1   1 
ATOM   4896 C  CE2   . TRP   D 2 122 ? 33.26600 27.97300  16.06100  1.000 31.06481 ?  121 TRP   D CE2   1 
ATOM   4897 C  CE3   . TRP   D 2 122 ? 35.13000 28.75500  17.38900  1.000 29.03612 ?  121 TRP   D CE3   1 
ATOM   4898 C  CZ2   . TRP   D 2 122 ? 32.34500 28.46200  16.98700  1.000 32.13290 ?  121 TRP   D CZ2   1 
ATOM   4899 C  CZ3   . TRP   D 2 122 ? 34.20900 29.23600  18.31800  1.000 36.47002 ?  121 TRP   D CZ3   1 
ATOM   4900 C  CH2   . TRP   D 2 122 ? 32.83300 29.08100  18.10700  1.000 33.48144 ?  121 TRP   D CH2   1 
ATOM   4901 N  N     . LEU   D 2 123 ? 35.86100 29.98100  12.73100  1.000 24.86789 ?  122 LEU   D N     1 
ATOM   4902 C  CA    . LEU   D 2 123 ? 35.24600 30.38900  11.46100  1.000 21.36732 ?  122 LEU   D CA    1 
ATOM   4903 C  C     . LEU   D 2 123 ? 36.18900 31.21400  10.59300  1.000 22.86765 ?  122 LEU   D C     1 
ATOM   4904 O  O     . LEU   D 2 123 ? 35.90000 31.40600  9.41000   1.000 22.26344 ?  122 LEU   D O     1 
ATOM   4905 C  CB    . LEU   D 2 123 ? 33.95000 31.17300  11.73800  1.000 21.73134 ?  122 LEU   D CB    1 
ATOM   4906 C  CG    . LEU   D 2 123 ? 32.97300 30.37500  12.59500  1.000 23.61451 ?  122 LEU   D CG    1 
ATOM   4907 C  CD1   . LEU   D 2 123 ? 31.72500 31.22900  12.80200  1.000 23.53260 ?  122 LEU   D CD1   1 
ATOM   4908 C  CD2   . LEU   D 2 123 ? 32.65500 29.03500  11.87600  1.000 25.47789 ?  122 LEU   D CD2   1 
ATOM   4909 N  N     . ASP   D 2 124 ? 37.31800 31.66300  11.14700  1.000 23.89634 ?  123 ASP   D N     1 
ATOM   4910 C  CA    . ASP   D 2 124 ? 38.30200 32.42700  10.37500  1.000 23.57065 ?  123 ASP   D CA    1 
ATOM   4911 C  C     . ASP   D 2 124 ? 38.74100 31.64900  9.14300   1.000 24.62690 ?  123 ASP   D C     1 
ATOM   4912 O  O     . ASP   D 2 124 ? 39.02200 30.45100  9.22000   1.000 23.63132 ?  123 ASP   D O     1 
ATOM   4913 C  CB    . ASP   D 2 124 ? 39.52600 32.75600  11.22100  1.000 23.68219 ?  123 ASP   D CB    1 
ATOM   4914 C  CG    . ASP   D 2 124 ? 39.22700 33.76200  12.31300  1.000 28.01989 ?  123 ASP   D CG    1 
ATOM   4915 O  OD1   . ASP   D 2 124 ? 38.13200 34.36800  12.27300  1.000 23.34310 ?  123 ASP   D OD1   1 
ATOM   4916 O  OD2   . ASP   D 2 124 ? 40.07300 33.91400  13.23700  1.000 29.69411 -1 123 ASP   D OD2   1 
ATOM   4917 N  N     . GLY   D 2 125 ? 38.81700 32.35100  8.01400   1.000 23.46840 ?  124 GLY   D N     1 
ATOM   4918 C  CA    . GLY   D 2 125 ? 39.20600 31.77100  6.74800   1.000 25.74429 ?  124 GLY   D CA    1 
ATOM   4919 C  C     . GLY   D 2 125 ? 38.15400 30.88800  6.12500   1.000 28.83485 ?  124 GLY   D C     1 
ATOM   4920 O  O     . GLY   D 2 125 ? 38.41800 30.27700  5.08300   1.000 29.79625 ?  124 GLY   D O     1 
ATOM   4921 N  N     . LYS   D 2 126 ? 36.96600 30.79700  6.72200   1.000 25.60009 ?  125 LYS   D N     1 
ATOM   4922 C  CA    . LYS   D 2 126 ? 35.85600 30.06100  6.12500   1.000 24.26397 ?  125 LYS   D CA    1 
ATOM   4923 C  C     . LYS   D 2 126 ? 34.64500 30.93300  5.82000   1.000 27.89720 ?  125 LYS   D C     1 
ATOM   4924 O  O     . LYS   D 2 126 ? 33.94300 30.67300  4.84100   1.000 26.54255 ?  125 LYS   D O     1 
ATOM   4925 C  CB    . LYS   D 2 126 ? 35.42500 28.89600  7.03100   1.000 26.20996 ?  125 LYS   D CB    1 
ATOM   4926 C  CG    . LYS   D 2 126 ? 36.49500 27.78300  7.16600   1.000 30.61233 ?  125 LYS   D CG    1 
ATOM   4927 C  CD    . LYS   D 2 126 ? 36.04200 26.70600  8.15500   1.000 38.69183 ?  125 LYS   D CD    1 
ATOM   4928 C  CE    . LYS   D 2 126 ? 37.20200 25.76900  8.56700   1.000 38.51668 ?  125 LYS   D CE    1 
ATOM   4929 N  NZ    . LYS   D 2 126 ? 37.90900 25.18500  7.38700   1.000 52.48881 ?  125 LYS   D NZ    1 
ATOM   4930 N  N     . HIS   D 2 127 ? 34.41600 31.98500  6.60100   1.000 22.00763 ?  126 HIS   D N     1 
ATOM   4931 C  CA    . HIS   D 2 127 ? 33.33800 32.93900  6.41100   1.000 22.07521 ?  126 HIS   D CA    1 
ATOM   4932 C  C     . HIS   D 2 127 ? 33.94900 34.31800  6.25200   1.000 22.56328 ?  126 HIS   D C     1 
ATOM   4933 O  O     . HIS   D 2 127 ? 34.86500 34.66400  6.98800   1.000 21.62358 ?  126 HIS   D O     1 
ATOM   4934 C  CB    . HIS   D 2 127 ? 32.39600 32.91700  7.61700   1.000 20.88376 ?  126 HIS   D CB    1 
ATOM   4935 C  CG    . HIS   D 2 127 ? 31.76800 31.58800  7.82000   1.000 19.90818 ?  126 HIS   D CG    1 
ATOM   4936 N  ND1   . HIS   D 2 127 ? 30.51700 31.28600  7.32900   1.000 20.42548 ?  126 HIS   D ND1   1 
ATOM   4937 C  CD2   . HIS   D 2 127 ? 32.24900 30.45400  8.37700   1.000 21.76278 ?  126 HIS   D CD2   1 
ATOM   4938 C  CE1   . HIS   D 2 127 ? 30.24600 30.02000  7.58600   1.000 23.82963 ?  126 HIS   D CE1   1 
ATOM   4939 N  NE2   . HIS   D 2 127 ? 31.27800 29.49000  8.22100   1.000 21.75818 ?  126 HIS   D NE2   1 
ATOM   4940 N  N     . VAL   D 2 128 ? 33.45800 35.08500  5.28400   1.000 20.99433 ?  127 VAL   D N     1 
ATOM   4941 C  CA    . VAL   D 2 128 ? 33.99400 36.42100  4.99900   1.000 21.05546 ?  127 VAL   D CA    1 
ATOM   4942 C  C     . VAL   D 2 128 ? 33.40900 37.40800  6.01200   1.000 20.80392 ?  127 VAL   D C     1 
ATOM   4943 O  O     . VAL   D 2 128 ? 32.21200 37.69100  5.99900   1.000 20.53214 ?  127 VAL   D O     1 
ATOM   4944 C  CB    . VAL   D 2 128 ? 33.66300 36.85200  3.56200   1.000 21.26515 ?  127 VAL   D CB    1 
ATOM   4945 C  CG1   . VAL   D 2 128 ? 34.09200 38.32900  3.28800   1.000 21.53766 ?  127 VAL   D CG1   1 
ATOM   4946 C  CG2   . VAL   D 2 128 ? 34.25800 35.86300  2.57000   1.000 22.89623 ?  127 VAL   D CG2   1 
ATOM   4947 N  N     . VAL   D 2 129 ? 34.28100 37.97100  6.85100   1.000 21.00093 ?  128 VAL   D N     1 
ATOM   4948 C  CA    . VAL   D 2 129 ? 33.94600 39.07900  7.73400   1.000 21.55559 ?  128 VAL   D CA    1 
ATOM   4949 C  C     . VAL   D 2 129 ? 33.90700 40.36700  6.92900   1.000 21.06398 ?  128 VAL   D C     1 
ATOM   4950 O  O     . VAL   D 2 129 ? 34.84400 40.66600  6.16600   1.000 21.72886 ?  128 VAL   D O     1 
ATOM   4951 C  CB    . VAL   D 2 129 ? 34.99200 39.17400  8.86900   1.000 21.01529 ?  128 VAL   D CB    1 
ATOM   4952 C  CG1   . VAL   D 2 129 ? 34.76200 40.45600  9.71800   1.000 21.98416 ?  128 VAL   D CG1   1 
ATOM   4953 C  CG2   . VAL   D 2 129 ? 34.94800 37.94600  9.73600   1.000 20.78232 ?  128 VAL   D CG2   1 
ATOM   4954 N  N     . PHE   D 2 130 ? 32.83700 41.14200  7.07300   1.000 20.83343 ?  129 PHE   D N     1 
ATOM   4955 C  CA    . PHE   D 2 130 ? 32.74600 42.34500  6.24700   1.000 21.52092 ?  129 PHE   D CA    1 
ATOM   4956 C  C     . PHE   D 2 130 ? 32.17000 43.54100  6.98800   1.000 22.66925 ?  129 PHE   D C     1 
ATOM   4957 O  O     . PHE   D 2 130 ? 31.99600 44.60000  6.36800   1.000 22.18480 ?  129 PHE   D O     1 
ATOM   4958 C  CB    . PHE   D 2 130 ? 31.89800 42.08300  4.96400   1.000 20.94687 ?  129 PHE   D CB    1 
ATOM   4959 C  CG    . PHE   D 2 130 ? 30.45900 41.74100  5.27100   1.000 21.03739 ?  129 PHE   D CG    1 
ATOM   4960 C  CD1   . PHE   D 2 130 ? 30.08500 40.44200  5.59100   1.000 20.26965 ?  129 PHE   D CD1   1 
ATOM   4961 C  CD2   . PHE   D 2 130 ? 29.47500 42.74300  5.30100   1.000 20.32791 ?  129 PHE   D CD2   1 
ATOM   4962 C  CE1   . PHE   D 2 130 ? 28.77700 40.12200  5.90000   1.000 19.92418 ?  129 PHE   D CE1   1 
ATOM   4963 C  CE2   . PHE   D 2 130 ? 28.16000 42.44100  5.60800   1.000 22.88694 ?  129 PHE   D CE2   1 
ATOM   4964 C  CZ    . PHE   D 2 130 ? 27.78300 41.12100  5.90900   1.000 21.81215 ?  129 PHE   D CZ    1 
ATOM   4965 N  N     . GLY   D 2 131 ? 31.90800 43.43900  8.29600   1.000 22.54686 ?  130 GLY   D N     1 
ATOM   4966 C  CA    . GLY   D 2 131 ? 31.28800 44.56300  8.97100   1.000 24.11719 ?  130 GLY   D CA    1 
ATOM   4967 C  C     . GLY   D 2 131 ? 31.32300 44.35900  10.47500  1.000 21.51489 ?  130 GLY   D C     1 
ATOM   4968 O  O     . GLY   D 2 131 ? 31.86500 43.37200  10.97800  1.000 21.33492 ?  130 GLY   D O     1 
ATOM   4969 N  N     . LYS   D 2 132 ? 30.77200 45.33400  11.19000  1.000 21.06861 ?  131 LYS   D N     1 
ATOM   4970 C  CA    . LYS   D 2 132 ? 30.64000 45.20400  12.64300  1.000 20.47831 ?  131 LYS   D CA    1 
ATOM   4971 C  C     . LYS   D 2 132 ? 29.50200 46.09700  13.13100  1.000 21.74997 ?  131 LYS   D C     1 
ATOM   4972 O  O     . LYS   D 2 132 ? 29.18000 47.13200  12.53200  1.000 22.04294 ?  131 LYS   D O     1 
ATOM   4973 C  CB    . LYS   D 2 132 ? 31.93000 45.58800  13.39700  1.000 21.80998 ?  131 LYS   D CB    1 
ATOM   4974 C  CG    . LYS   D 2 132 ? 32.28800 47.00500  13.18600  1.000 25.57756 ?  131 LYS   D CG    1 
ATOM   4975 C  CD    . LYS   D 2 132 ? 33.37800 47.44700  14.15200  1.000 32.00165 ?  131 LYS   D CD    1 
ATOM   4976 C  CE    . LYS   D 2 132 ? 33.93600 48.80500  13.79300  1.000 38.58160 ?  131 LYS   D CE    1 
ATOM   4977 N  NZ    . LYS   D 2 132 ? 34.97100 49.15700  14.81600  1.000 48.48974 ?  131 LYS   D NZ    1 
ATOM   4978 N  N     . VAL   D 2 133 ? 28.89700 45.67600  14.23200  1.000 20.25322 ?  132 VAL   D N     1 
ATOM   4979 C  CA    . VAL   D 2 133 ? 27.88800 46.51400  14.87700  1.000 22.39271 ?  132 VAL   D CA    1 
ATOM   4980 C  C     . VAL   D 2 133 ? 28.53100 47.80700  15.33900  1.000 21.27866 ?  132 VAL   D C     1 
ATOM   4981 O  O     . VAL   D 2 133 ? 29.54700 47.79100  16.03800  1.000 26.39017 ?  132 VAL   D O     1 
ATOM   4982 C  CB    . VAL   D 2 133 ? 27.27700 45.79000  16.07600  1.000 20.82819 ?  132 VAL   D CB    1 
ATOM   4983 C  CG1   . VAL   D 2 133 ? 26.33000 46.73100  16.79900  1.000 22.85520 ?  132 VAL   D CG1   1 
ATOM   4984 C  CG2   . VAL   D 2 133 ? 26.51400 44.54300  15.60700  1.000 23.00608 ?  132 VAL   D CG2   1 
ATOM   4985 N  N     . LYS   D 2 134 ? 27.89700 48.92900  15.00400  1.000 23.96229 ?  133 LYS   D N     1 
ATOM   4986 C  CA    . LYS   D 2 134 ? 28.32600 50.24000  15.46200  1.000 24.81755 ?  133 LYS   D CA    1 
ATOM   4987 C  C     . LYS   D 2 134 ? 27.48500 50.75600  16.62700  1.000 27.99106 ?  133 LYS   D C     1 
ATOM   4988 O  O     . LYS   D 2 134 ? 28.03200 51.22900  17.62400  1.000 33.41223 ?  133 LYS   D O     1 
ATOM   4989 C  CB    . LYS   D 2 134 ? 28.23900 51.20300  14.27100  1.000 31.44415 ?  133 LYS   D CB    1 
ATOM   4990 C  CG    . LYS   D 2 134 ? 28.65300 52.60700  14.52700  1.000 39.21034 ?  133 LYS   D CG    1 
ATOM   4991 C  CD    . LYS   D 2 134 ? 28.40700 53.42600  13.28300  1.000 42.19187 ?  133 LYS   D CD    1 
ATOM   4992 C  CE    . LYS   D 2 134 ? 28.80700 54.87200  13.51900  1.000 40.32870 ?  133 LYS   D CE    1 
ATOM   4993 N  NZ    . LYS   D 2 134 ? 28.38000 55.73600  12.39500  1.000 46.95467 ?  133 LYS   D NZ    1 
ATOM   4994 N  N     . GLU   D 2 135 ? 26.16000 50.72000  16.50100  1.000 29.73737 ?  134 GLU   D N     1 
ATOM   4995 C  CA    . GLU   D 2 135 ? 25.27900 51.05000  17.61700  1.000 29.98539 ?  134 GLU   D CA    1 
ATOM   4996 C  C     . GLU   D 2 135 ? 24.24100 49.94800  17.76700  1.000 28.51433 ?  134 GLU   D C     1 
ATOM   4997 O  O     . GLU   D 2 135 ? 23.86300 49.26000  16.80700  1.000 24.00049 ?  134 GLU   D O     1 
ATOM   4998 C  CB    . GLU   D 2 135 ? 24.55100 52.40900  17.44800  1.000 33.54774 ?  134 GLU   D CB    1 
ATOM   4999 C  CG    . GLU   D 2 135 ? 25.39800 53.59100  16.96200  1.000 39.45381 ?  134 GLU   D CG    1 
ATOM   5000 C  CD    . GLU   D 2 135 ? 26.38300 54.11900  18.00900  1.000 51.32038 ?  134 GLU   D CD    1 
ATOM   5001 O  OE1   . GLU   D 2 135 ? 26.21600 53.80500  19.21900  1.000 49.99866 ?  134 GLU   D OE1   1 
ATOM   5002 O  OE2   . GLU   D 2 135 ? 27.33000 54.85000  17.60900  1.000 56.53333 -1 134 GLU   D OE2   1 
ATOM   5003 N  N     . GLY   D 2 136 ? 23.76300 49.78900  18.98800  1.000 28.26450 ?  135 GLY   D N     1 
ATOM   5004 C  CA    . GLY   D 2 136 ? 22.69400 48.85100  19.20200  1.000 29.13005 ?  135 GLY   D CA    1 
ATOM   5005 C  C     . GLY   D 2 136 ? 23.14500 47.46600  19.56800  1.000 23.06455 ?  135 GLY   D C     1 
ATOM   5006 O  O     . GLY   D 2 136 ? 22.32700 46.54700  19.50800  1.000 24.98587 ?  135 GLY   D O     1 
ATOM   5007 N  N     . MET   D 2 137 ? 24.39700 47.28200  19.99000  1.000 24.65928 ?  136 MET   D N     1 
ATOM   5008 C  CA    . MET   D 2 137 ? 24.79300 45.95600  20.42800  1.000 22.83657 ?  136 MET   D CA    1 
ATOM   5009 C  C     . MET   D 2 137 ? 23.90000 45.47000  21.56300  1.000 22.87326 ?  136 MET   D C     1 
ATOM   5010 O  O     . MET   D 2 137 ? 23.64100 44.27000  21.66200  1.000 24.58256 ?  136 MET   D O     1 
ATOM   5011 C  CB    . MET   D 2 137 ? 26.27300 45.92800  20.83100  1.000 21.94945 ?  136 MET   D CB    1 
ATOM   5012 C  CG    . MET   D 2 137 ? 26.81200 44.53800  21.06000  1.000 27.87087 ?  136 MET   D CG    1 
ATOM   5013 S  SD    . MET   D 2 137 ? 26.85400 43.55400  19.51200  1.000 28.07109 ?  136 MET   D SD    1 
ATOM   5014 C  CE    . MET   D 2 137 ? 26.89000 41.84900  20.10700  1.000 29.45303 ?  136 MET   D CE    1 
ATOM   5015 N  N     . ASN   D 2 138 ? 23.36700 46.37300  22.40100  1.000 25.13148 ?  137 ASN   D N     1 
ATOM   5016 C  CA    . ASN   D 2 138 ? 22.46700 45.84600  23.43200  1.000 26.60805 ?  137 ASN   D CA    1 
ATOM   5017 C  C     . ASN   D 2 138 ? 21.17800 45.25400  22.84900  1.000 22.74392 ?  137 ASN   D C     1 
ATOM   5018 O  O     . ASN   D 2 138 ? 20.56300 44.40300  23.50200  1.000 22.57528 ?  137 ASN   D O     1 
ATOM   5019 C  CB    . ASN   D 2 138 ? 22.13500 46.90000  24.50200  1.000 28.31205 ?  137 ASN   D CB    1 
ATOM   5020 C  CG    . ASN   D 2 138 ? 21.80300 48.24400  23.95400  1.000 30.01642 ?  137 ASN   D CG    1 
ATOM   5021 O  OD1   . ASN   D 2 138 ? 21.44000 48.42300  22.77600  1.000 33.93215 ?  137 ASN   D OD1   1 
ATOM   5022 N  ND2   . ASN   D 2 138 ? 21.88200 49.23900  24.83800  1.000 38.47508 ?  137 ASN   D ND2   1 
ATOM   5023 N  N     . ILE   D 2 139 ? 20.76500 45.66800  21.64700  1.000 19.87729 ?  138 ILE   D N     1 
ATOM   5024 C  CA    . ILE   D 2 139 ? 19.63900 45.02400  20.95800  1.000 21.11327 ?  138 ILE   D CA    1 
ATOM   5025 C  C     . ILE   D 2 139 ? 20.01000 43.59500  20.55500  1.000 23.61164 ?  138 ILE   D C     1 
ATOM   5026 O  O     . ILE   D 2 139 ? 19.23700 42.65200  20.75900  1.000 22.17637 ?  138 ILE   D O     1 
ATOM   5027 C  CB    . ILE   D 2 139 ? 19.21500 45.83800  19.71300  1.000 22.36534 ?  138 ILE   D CB    1 
ATOM   5028 C  CG1   . ILE   D 2 139 ? 18.92000 47.31000  20.04100  1.000 26.41591 ?  138 ILE   D CG1   1 
ATOM   5029 C  CG2   . ILE   D 2 139 ? 18.02900 45.16600  18.97900  1.000 23.94013 ?  138 ILE   D CG2   1 
ATOM   5030 C  CD1   . ILE   D 2 139 ? 17.86400 47.50000  21.14000  1.000 25.09272 ?  138 ILE   D CD1   1 
ATOM   5031 N  N     . VAL   D 2 140 ? 21.21300 43.40400  20.01300  1.000 20.80239 ?  139 VAL   D N     1 
ATOM   5032 C  CA    . VAL   D 2 140 ? 21.64900 42.05000  19.68200  1.000 23.73824 ?  139 VAL   D CA    1 
ATOM   5033 C  C     . VAL   D 2 140 ? 21.72200 41.18800  20.93000  1.000 23.13302 ?  139 VAL   D C     1 
ATOM   5034 O  O     . VAL   D 2 140 ? 21.26100 40.04400  20.94700  1.000 19.90265 ?  139 VAL   D O     1 
ATOM   5035 C  CB    . VAL   D 2 140 ? 23.00500 42.10200  18.95800  1.000 24.78631 ?  139 VAL   D CB    1 
ATOM   5036 C  CG1   . VAL   D 2 140 ? 23.45600 40.69200  18.64700  1.000 24.39549 ?  139 VAL   D CG1   1 
ATOM   5037 C  CG2   . VAL   D 2 140 ? 22.83900 42.99500  17.71900  1.000 22.43726 ?  139 VAL   D CG2   1 
ATOM   5038 N  N     . GLU   D 2 141 ? 22.25000 41.73800  22.01100  1.000 22.15350 ?  140 GLU   D N     1 
ATOM   5039 C  CA    . GLU   D 2 141 ? 22.27900 40.98500  23.24600  1.000 22.82079 ?  140 GLU   D CA    1 
ATOM   5040 C  C     . GLU   D 2 141 ? 20.87200 40.63400  23.70700  1.000 23.73360 ?  140 GLU   D C     1 
ATOM   5041 O  O     . GLU   D 2 141 ? 20.64100 39.52600  24.19400  1.000 22.96765 ?  140 GLU   D O     1 
ATOM   5042 C  CB    . GLU   D 2 141 ? 23.01600 41.78600  24.31300  1.000 23.85465 ?  140 GLU   D CB    1 
ATOM   5043 C  CG    . GLU   D 2 141 ? 24.49900 41.96400  23.98900  1.000 28.92381 ?  140 GLU   D CG    1 
ATOM   5044 C  CD    . GLU   D 2 141 ? 25.12800 43.03300  24.84500  1.000 34.84662 ?  140 GLU   D CD    1 
ATOM   5045 O  OE1   . GLU   D 2 141 ? 24.43600 43.55900  25.74000  1.000 39.21717 ?  140 GLU   D OE1   1 
ATOM   5046 O  OE2   . GLU   D 2 141 ? 26.31100 43.36700  24.61300  1.000 41.98999 -1 140 GLU   D OE2   1 
ATOM   5047 N  N     . ALA   D 2 142 ? 19.91000 41.55000  23.51400  1.000 22.38211 ?  141 ALA   D N     1 
ATOM   5048 C  CA    . ALA   D 2 142 ? 18.53900 41.26500  23.92600  1.000 25.88906 ?  141 ALA   D CA    1 
ATOM   5049 C  C     . ALA   D 2 142 ? 17.87200 40.21300  23.05300  1.000 22.87694 ?  141 ALA   D C     1 
ATOM   5050 O  O     . ALA   D 2 142 ? 16.92000 39.56500  23.50800  1.000 25.50272 ?  141 ALA   D O     1 
ATOM   5051 C  CB    . ALA   D 2 142 ? 17.68300 42.54400  23.90700  1.000 24.83735 ?  141 ALA   D CB    1 
ATOM   5052 N  N     . MET   D 2 143 ? 18.33900 40.04100  21.80700  1.000 20.36861 ?  142 MET   D N     1 
ATOM   5053 C  CA    . MET   D 2 143 ? 17.78900 39.01800  20.92500  1.000 25.06408 ?  142 MET   D CA    1 
ATOM   5054 C  C     . MET   D 2 143 ? 18.13500 37.61800  21.41100  1.000 25.47131 ?  142 MET   D C     1 
ATOM   5055 O  O     . MET   D 2 143 ? 17.40500 36.67500  21.10200  1.000 22.34253 ?  142 MET   D O     1 
ATOM   5056 C  CB    . MET   D 2 143 ? 18.31000 39.21900  19.49100  1.000 24.75596 ?  142 MET   D CB    1 
ATOM   5057 C  CG    . MET   D 2 143 ? 17.70100 40.46900  18.79900  1.000 23.79698 ?  142 MET   D CG    1 
ATOM   5058 S  SD    . MET   D 2 143 ? 18.63700 41.06700  17.38500  1.000 27.88283 ?  142 MET   D SD    1 
ATOM   5059 C  CE    . MET   D 2 143 ? 18.61800 39.60600  16.38000  1.000 24.85325 ?  142 MET   D CE    1 
ATOM   5060 N  N     . GLU   D 2 144 ? 19.23400 37.46700  22.16700  1.000 24.41273 ?  143 GLU   D N     1 
ATOM   5061 C  CA    . GLU   D 2 144 ? 19.75800 36.13800  22.47100  1.000 24.69224 ?  143 GLU   D CA    1 
ATOM   5062 C  C     . GLU   D 2 144 ? 18.76400 35.26400  23.21300  1.000 23.89869 ?  143 GLU   D C     1 
ATOM   5063 O  O     . GLU   D 2 144 ? 18.70400 34.05800  22.97000  1.000 24.63115 ?  143 GLU   D O     1 
ATOM   5064 C  CB    . GLU   D 2 144 ? 21.05000 36.24100  23.29100  1.000 27.73062 ?  143 GLU   D CB    1 
ATOM   5065 C  CG    . GLU   D 2 144 ? 22.24200 36.62600  22.46800  1.000 27.44653 ?  143 GLU   D CG    1 
ATOM   5066 C  CD    . GLU   D 2 144 ? 23.55000 36.25300  23.17600  1.000 32.59594 ?  143 GLU   D CD    1 
ATOM   5067 O  OE1   . GLU   D 2 144 ? 23.76900 36.70900  24.32800  1.000 37.45955 ?  143 GLU   D OE1   1 
ATOM   5068 O  OE2   . GLU   D 2 144 ? 24.35100 35.47000  22.58700  1.000 39.72613 -1 143 GLU   D OE2   1 
ATOM   5069 N  N     . ARG   D 2 145 ? 18.01800 35.81900  24.15900  1.000 20.97367 ?  144 ARG   D N     1 
ATOM   5070 C  CA    . ARG   D 2 145 ? 17.14400 34.96500  24.96500  1.000 25.71326 ?  144 ARG   D CA    1 
ATOM   5071 C  C     . ARG   D 2 145 ? 15.99200 34.34700  24.17400  1.000 25.08775 ?  144 ARG   D C     1 
ATOM   5072 O  O     . ARG   D 2 145 ? 15.29900 33.46000  24.70400  1.000 25.12845 ?  144 ARG   D O     1 
ATOM   5073 C  CB    . ARG   D 2 145 ? 16.56900 35.75100  26.14400  1.000 28.69035 ?  144 ARG   D CB    1 
ATOM   5074 C  CG    . ARG   D 2 145 ? 15.56200 36.86500  25.81600  1.000 28.29306 ?  144 ARG   D CG    1 
ATOM   5075 C  CD    . ARG   D 2 145 ? 14.98100 37.34800  27.18300  1.000 32.05034 ?  144 ARG   D CD    1 
ATOM   5076 N  NE    . ARG   D 2 145 ? 14.07700 38.48500  27.07100  1.000 37.01037 ?  144 ARG   D NE    1 
ATOM   5077 C  CZ    . ARG   D 2 145 ? 12.75200 38.40500  27.16700  1.000 43.20039 ?  144 ARG   D CZ    1 
ATOM   5078 N  NH1   . ARG   D 2 145 ? 12.13000 37.23600  27.30000  1.000 34.49619 ?  144 ARG   D NH1   1 
ATOM   5079 N  NH2   . ARG   D 2 145 ? 12.03300 39.52700  27.15000  1.000 43.45059 ?  144 ARG   D NH2   1 
ATOM   5080 N  N     . PHE   D 2 146 ? 15.75100 34.79900  22.94900  1.000 20.59637 ?  145 PHE   D N     1 
ATOM   5081 C  CA    . PHE   D 2 146 ? 14.75700 34.17000  22.10700  1.000 22.15435 ?  145 PHE   D CA    1 
ATOM   5082 C  C     . PHE   D 2 146 ? 15.32600 32.99100  21.34000  1.000 23.96365 ?  145 PHE   D C     1 
ATOM   5083 O  O     . PHE   D 2 146 ? 14.59100 32.37500  20.56700  1.000 22.33702 ?  145 PHE   D O     1 
ATOM   5084 C  CB    . PHE   D 2 146 ? 14.15800 35.22600  21.16100  1.000 22.50964 ?  145 PHE   D CB    1 
ATOM   5085 C  CG    . PHE   D 2 146 ? 13.57100 36.39700  21.92100  1.000 20.26527 ?  145 PHE   D CG    1 
ATOM   5086 C  CD1   . PHE   D 2 146 ? 12.43800 36.19800  22.68800  1.000 24.53766 ?  145 PHE   D CD1   1 
ATOM   5087 C  CD2   . PHE   D 2 146 ? 14.19300 37.65000  21.93600  1.000 24.34512 ?  145 PHE   D CD2   1 
ATOM   5088 C  CE1   . PHE   D 2 146 ? 11.89600 37.24800  23.45500  1.000 26.94084 ?  145 PHE   D CE1   1 
ATOM   5089 C  CE2   . PHE   D 2 146 ? 13.65500 38.70700  22.66800  1.000 29.42672 ?  145 PHE   D CE2   1 
ATOM   5090 C  CZ    . PHE   D 2 146 ? 12.50500 38.49100  23.44600  1.000 31.43390 ?  145 PHE   D CZ    1 
ATOM   5091 N  N     . GLY   D 2 147 ? 16.60400 32.66200  21.55900  1.000 19.14070 ?  146 GLY   D N     1 
ATOM   5092 C  CA    . GLY   D 2 147 ? 17.24100 31.54700  20.91000  1.000 22.09078 ?  146 GLY   D CA    1 
ATOM   5093 C  C     . GLY   D 2 147 ? 17.34700 30.34300  21.82000  1.000 27.88909 ?  146 GLY   D C     1 
ATOM   5094 O  O     . GLY   D 2 147 ? 16.66800 30.23300  22.84800  1.000 25.60118 ?  146 GLY   D O     1 
ATOM   5095 N  N     . SER   D 2 148 ? 18.18200 29.39800  21.40100  1.000 21.92265 ?  147 SER   D N     1 
ATOM   5096 C  CA    . SER   D 2 148 ? 18.29000 28.12000  22.07500  1.000 25.42740 ?  147 SER   D CA    1 
ATOM   5097 C  C     . SER   D 2 148 ? 19.57100 27.44100  21.63000  1.000 24.53357 ?  147 SER   D C     1 
ATOM   5098 O  O     . SER   D 2 148 ? 20.27000 27.90400  20.71700  1.000 24.13840 ?  147 SER   D O     1 
ATOM   5099 C  CB    . SER   D 2 148 ? 17.08800 27.23000  21.76200  1.000 22.33640 ?  147 SER   D CB    1 
ATOM   5100 O  OG    . SER   D 2 148 ? 17.04900 26.84900  20.37700  1.000 25.03663 ?  147 SER   D OG    1 
ATOM   5101 N  N     . ARG   D 2 149 ? 19.85600 26.30200  22.26800  1.000 26.67458 ?  148 ARG   D N     1 
ATOM   5102 C  CA    . ARG   D 2 149 ? 21.05600 25.53500  21.93700  1.000 29.44484 ?  148 ARG   D CA    1 
ATOM   5103 C  C     . ARG   D 2 149 ? 21.18000 25.22500  20.44400  1.000 27.35194 ?  148 ARG   D C     1 
ATOM   5104 O  O     . ARG   D 2 149 ? 22.26700 25.36500  19.86500  1.000 25.57541 ?  148 ARG   D O     1 
ATOM   5105 C  CB    . ARG   D 2 149 ? 21.07200 24.23400  22.74700  1.000 33.72852 ?  148 ARG   D CB    1 
ATOM   5106 C  CG    . ARG   D 2 149 ? 22.31000 23.41300  22.46500  1.000 29.24006 ?  148 ARG   D CG    1 
ATOM   5107 C  CD    . ARG   D 2 149 ? 22.52600 22.33400  23.55100  1.000 36.81249 ?  148 ARG   D CD    1 
ATOM   5108 N  NE    . ARG   D 2 149 ? 23.55500 21.35300  23.19900  1.000 34.91734 ?  148 ARG   D NE    1 
ATOM   5109 C  CZ    . ARG   D 2 149 ? 23.30300 20.27800  22.46400  1.000 34.00286 ?  148 ARG   D CZ    1 
ATOM   5110 N  NH1   . ARG   D 2 149 ? 22.09100 20.04100  21.99400  1.000 34.50776 ?  148 ARG   D NH1   1 
ATOM   5111 N  NH2   . ARG   D 2 149 ? 24.28800 19.41600  22.20300  1.000 37.80664 ?  148 ARG   D NH2   1 
ATOM   5112 N  N     . ASN   D 2 150 ? 20.10000 24.78000  19.79900  1.000 27.25928 ?  149 ASN   D N     1 
ATOM   5113 C  CA    . ASN   D 2 150 ? 20.18200 24.47700  18.37800  1.000 28.10500 ?  149 ASN   D CA    1 
ATOM   5114 C  C     . ASN   D 2 150 ? 19.73200 25.63100  17.48700  1.000 26.84907 ?  149 ASN   D C     1 
ATOM   5115 O  O     . ASN   D 2 150 ? 19.69300 25.48100  16.25600  1.000 27.73649 ?  149 ASN   D O     1 
ATOM   5116 C  CB    . ASN   D 2 150 ? 19.40000 23.19300  18.05200  1.000 27.81264 ?  149 ASN   D CB    1 
ATOM   5117 C  CG    . ASN   D 2 150 ? 17.91400 23.41300  17.83900  1.000 32.42906 ?  149 ASN   D CG    1 
ATOM   5118 O  OD1   . ASN   D 2 150 ? 17.33900 24.45000  18.18000  1.000 30.22195 ?  149 ASN   D OD1   1 
ATOM   5119 N  ND2   . ASN   D 2 150 ? 17.27200 22.39000  17.28400  1.000 37.92178 ?  149 ASN   D ND2   1 
ATOM   5120 N  N     . GLY   D 2 151 ? 19.36200 26.76000  18.07500  1.000 22.68101 ?  150 GLY   D N     1 
ATOM   5121 C  CA    . GLY   D 2 151 ? 19.11200 27.97500  17.33100  1.000 23.88397 ?  150 GLY   D CA    1 
ATOM   5122 C  C     . GLY   D 2 151 ? 17.65700 28.25300  17.00000  1.000 24.82307 ?  150 GLY   D C     1 
ATOM   5123 O  O     . GLY   D 2 151 ? 17.33200 29.38700  16.63500  1.000 22.42823 ?  150 GLY   D O     1 
ATOM   5124 N  N     . LYS   D 2 152 ? 16.75600 27.28700  17.17200  1.000 22.15263 ?  151 LYS   D N     1 
ATOM   5125 C  CA    . LYS   D 2 152 ? 15.35500 27.56800  16.90300  1.000 26.62560 ?  151 LYS   D CA    1 
ATOM   5126 C  C     . LYS   D 2 152 ? 14.86900 28.68200  17.83600  1.000 23.42038 ?  151 LYS   D C     1 
ATOM   5127 O  O     . LYS   D 2 152 ? 15.23700 28.73100  19.00900  1.000 26.27483 ?  151 LYS   D O     1 
ATOM   5128 C  CB    . LYS   D 2 152 ? 14.52300 26.29300  17.08900  1.000 28.22211 ?  151 LYS   D CB    1 
ATOM   5129 C  CG    . LYS   D 2 152 ? 13.05100 26.50300  16.78900  1.000 39.73082 ?  151 LYS   D CG    1 
ATOM   5130 C  CD    . LYS   D 2 152 ? 12.28200 25.20200  16.94900  1.000 45.36414 ?  151 LYS   D CD    1 
ATOM   5131 C  CE    . LYS   D 2 152 ? 10.78800 25.39900  16.73000  1.000 51.23984 ?  151 LYS   D CE    1 
ATOM   5132 N  NZ    . LYS   D 2 152 ? 10.07000 24.08400  16.76800  1.000 55.42416 ?  151 LYS   D NZ    1 
ATOM   5133 N  N     . THR   D 2 153 ? 14.10300 29.62800  17.30200  1.000 23.86552 ?  152 THR   D N     1 
ATOM   5134 C  CA    . THR   D 2 153 ? 13.71500 30.76900  18.11300  1.000 22.50978 ?  152 THR   D CA    1 
ATOM   5135 C  C     . THR   D 2 153 ? 12.33600 30.53300  18.74000  1.000 27.94160 ?  152 THR   D C     1 
ATOM   5136 O  O     . THR   D 2 153 ? 11.52400 29.75400  18.24300  1.000 26.08164 ?  152 THR   D O     1 
ATOM   5137 C  CB    . THR   D 2 153 ? 13.73100 32.07200  17.28800  1.000 23.49099 ?  152 THR   D CB    1 
ATOM   5138 O  OG1   . THR   D 2 153 ? 12.83700 31.96000  16.17200  1.000 24.95671 ?  152 THR   D OG1   1 
ATOM   5139 C  CG2   . THR   D 2 153 ? 15.15900 32.35200  16.74100  1.000 22.49059 ?  152 THR   D CG2   1 
ATOM   5140 N  N     . SER   D 2 154 ? 12.08100 31.22100  19.84700  1.000 23.36208 ?  153 SER   D N     1 
ATOM   5141 C  CA    . SER   D 2 154 ? 10.81000 31.04000  20.54300  1.000 26.38003 ?  153 SER   D CA    1 
ATOM   5142 C  C     . SER   D 2 154 ? 9.80600  32.14200  20.23000  1.000 29.62287 ?  153 SER   D C     1 
ATOM   5143 O  O     . SER   D 2 154 ? 8.63500  32.03000  20.63100  1.000 29.41634 ?  153 SER   D O     1 
ATOM   5144 C  CB    . SER   D 2 154 ? 11.04500 30.96100  22.06200  1.000 27.70270 ?  153 SER   D CB    1 
ATOM   5145 O  OG    . SER   D 2 154 ? 11.75400 32.09800  22.53900  1.000 27.05399 ?  153 SER   D OG    1 
ATOM   5146 N  N     . LYS   D 2 155 ? 10.26500 33.23600  19.62700  1.000 27.62116 ?  154 LYS   D N     1 
ATOM   5147 C  CA    . LYS   D 2 155 ? 9.42600  34.28700  19.07200  1.000 32.08376 ?  154 LYS   D CA    1 
ATOM   5148 C  C     . LYS   D 2 155 ? 9.99600  34.62100  17.70000  1.000 30.20479 ?  154 LYS   D C     1 
ATOM   5149 O  O     . LYS   D 2 155 ? 11.14600 34.29000  17.40600  1.000 27.07802 ?  154 LYS   D O     1 
ATOM   5150 C  CB    . LYS   D 2 155 ? 9.38600  35.51700  19.99200  1.000 28.35840 ?  154 LYS   D CB    1 
ATOM   5151 C  CG    . LYS   D 2 155 ? 8.87200  35.19000  21.38300  1.000 33.92216 ?  154 LYS   D CG    1 
ATOM   5152 C  CD    . LYS   D 2 155 ? 8.58100  36.42300  22.21500  1.000 35.93274 ?  154 LYS   D CD    1 
ATOM   5153 C  CE    . LYS   D 2 155 ? 7.96000  35.99900  23.54400  1.000 39.92623 ?  154 LYS   D CE    1 
ATOM   5154 N  NZ    . LYS   D 2 155 ? 7.71500  37.19400  24.38500  1.000 46.55120 ?  154 LYS   D NZ    1 
ATOM   5155 N  N     . LYS   D 2 156 ? 9.18500  35.24500  16.83400  1.000 25.93123 ?  155 LYS   D N     1 
ATOM   5156 C  CA    . LYS   D 2 156 ? 9.65500  35.63000  15.51400  1.000 32.60172 ?  155 LYS   D CA    1 
ATOM   5157 C  C     . LYS   D 2 156 ? 10.43000 36.93500  15.61700  1.000 25.41147 ?  155 LYS   D C     1 
ATOM   5158 O  O     . LYS   D 2 156 ? 9.86800  37.96300  16.00400  1.000 26.00984 ?  155 LYS   D O     1 
ATOM   5159 C  CB    . LYS   D 2 156 ? 8.47300  35.77500  14.55500  1.000 32.96138 ?  155 LYS   D CB    1 
ATOM   5160 C  CG    . LYS   D 2 156 ? 7.52900  34.60400  14.54300  1.000 35.79495 ?  155 LYS   D CG    1 
ATOM   5161 C  CD    . LYS   D 2 156 ? 6.46000  34.82800  13.47500  1.000 40.41040 ?  155 LYS   D CD    1 
ATOM   5162 C  CE    . LYS   D 2 156 ? 5.06300  34.93100  14.07400  1.000 45.98833 ?  155 LYS   D CE    1 
ATOM   5163 N  NZ    . LYS   D 2 156 ? 4.94300  35.94200  15.18100  1.000 46.93480 ?  155 LYS   D NZ    1 
ATOM   5164 N  N     . ILE   D 2 157 ? 11.73300 36.88700  15.31000  1.000 22.34543 ?  156 ILE   D N     1 
ATOM   5165 C  CA    . ILE   D 2 157 ? 12.62300 38.03200  15.40900  1.000 24.43488 ?  156 ILE   D CA    1 
ATOM   5166 C  C     . ILE   D 2 157 ? 12.82400 38.53200  13.98700  1.000 26.39038 ?  156 ILE   D C     1 
ATOM   5167 O  O     . ILE   D 2 157 ? 13.48800 37.86200  13.19500  1.000 28.33436 ?  156 ILE   D O     1 
ATOM   5168 C  CB    . ILE   D 2 157 ? 13.98000 37.66100  16.02700  1.000 23.74781 ?  156 ILE   D CB    1 
ATOM   5169 C  CG1   . ILE   D 2 157 ? 13.81200 36.88700  17.34100  1.000 23.79677 ?  156 ILE   D CG1   1 
ATOM   5170 C  CG2   . ILE   D 2 157 ? 14.78800 38.92100  16.21800  1.000 29.88792 ?  156 ILE   D CG2   1 
ATOM   5171 C  CD1   . ILE   D 2 157 ? 12.94800 37.56000  18.33400  1.000 29.84992 ?  156 ILE   D CD1   1 
ATOM   5172 N  N     . THR   D 2 158 ? 12.27800 39.69700  13.66000  1.000 25.09328 ?  157 THR   D N     1 
ATOM   5173 C  CA    . THR   D 2 158 ? 12.23300 40.15100  12.27600  1.000 24.22642 ?  157 THR   D CA    1 
ATOM   5174 C  C     . THR   D 2 158 ? 12.93900 41.48000  12.09300  1.000 21.95219 ?  157 THR   D C     1 
ATOM   5175 O  O     . THR   D 2 158 ? 13.07300 42.28200  13.03000  1.000 24.81802 ?  157 THR   D O     1 
ATOM   5176 C  CB    . THR   D 2 158 ? 10.76600 40.30000  11.78800  1.000 28.95081 ?  157 THR   D CB    1 
ATOM   5177 O  OG1   . THR   D 2 158 ? 10.09800 41.24000  12.63600  1.000 26.39006 ?  157 THR   D OG1   1 
ATOM   5178 C  CG2   . THR   D 2 158 ? 10.04900 38.96800  11.85600  1.000 31.79273 ?  157 THR   D CG2   1 
ATOM   5179 N  N     . ILE   D 2 159 ? 13.40400 41.68300  10.85700  1.000 25.79480 ?  158 ILE   D N     1 
ATOM   5180 C  CA    . ILE   D 2 159 ? 13.91800 42.97100  10.40600  1.000 23.64488 ?  158 ILE   D CA    1 
ATOM   5181 C  C     . ILE   D 2 159 ? 12.70900 43.74900  9.88900   1.000 25.41709 ?  158 ILE   D C     1 
ATOM   5182 O  O     . ILE   D 2 159 ? 12.34600 43.65500  8.72200   1.000 26.72436 ?  158 ILE   D O     1 
ATOM   5183 C  CB    . ILE   D 2 159 ? 14.97500 42.79400  9.33200   1.000 25.07311 ?  158 ILE   D CB    1 
ATOM   5184 C  CG1   . ILE   D 2 159 ? 16.13200 41.93700  9.88900   1.000 24.16033 ?  158 ILE   D CG1   1 
ATOM   5185 C  CG2   . ILE   D 2 159 ? 15.38800 44.14300  8.79400   1.000 25.55832 ?  158 ILE   D CG2   1 
ATOM   5186 C  CD1   . ILE   D 2 159 ? 17.18000 41.58700  8.81300   1.000 23.75226 ?  158 ILE   D CD1   1 
ATOM   5187 N  N     . ALA   D 2 160 ? 12.10500 44.55400  10.76300  1.000 27.79354 ?  159 ALA   D N     1 
ATOM   5188 C  CA    . ALA   D 2 160 ? 10.88400 45.28000  10.39700  1.000 31.60503 ?  159 ALA   D CA    1 
ATOM   5189 C  C     . ALA   D 2 160 ? 11.17600 46.37500  9.37600   1.000 32.45982 ?  159 ALA   D C     1 
ATOM   5190 O  O     . ALA   D 2 160 ? 10.37300 46.62200  8.46500   1.000 37.43506 ?  159 ALA   D O     1 
ATOM   5191 C  CB    . ALA   D 2 160 ? 10.23700 45.87400  11.64700  1.000 28.86825 ?  159 ALA   D CB    1 
ATOM   5192 N  N     . ASP   D 2 161 ? 12.33300 47.00400  9.48000   1.000 30.22509 ?  160 ASP   D N     1 
ATOM   5193 C  CA    . ASP   D 2 161 ? 12.76700 48.00000  8.51500   1.000 35.72504 ?  160 ASP   D CA    1 
ATOM   5194 C  C     . ASP   D 2 161 ? 14.29100 48.02200  8.48700   1.000 33.51785 ?  160 ASP   D C     1 
ATOM   5195 O  O     . ASP   D 2 161 ? 14.95600 47.63900  9.45100   1.000 28.97493 ?  160 ASP   D O     1 
ATOM   5196 C  CB    . ASP   D 2 161 ? 12.19400 49.37500  8.87500   1.000 36.38823 ?  160 ASP   D CB    1 
ATOM   5197 C  CG    . ASP   D 2 161 ? 12.23000 50.34800  7.71200   1.000 37.24714 ?  160 ASP   D CG    1 
ATOM   5198 O  OD1   . ASP   D 2 161 ? 12.54800 49.94100  6.56200   1.000 41.16509 ?  160 ASP   D OD1   1 
ATOM   5199 O  OD2   . ASP   D 2 161 ? 11.95400 51.53700  7.97600   1.000 48.00827 -1 160 ASP   D OD2   1 
ATOM   5200 N  N     . CYS   D 2 162 ? 14.84100 48.48700  7.37500   1.000 26.81554 ?  161 CYS   D N     1 
ATOM   5201 C  CA    . CYS   D 2 162 ? 16.28400 48.54400  7.23900   1.000 30.11099 ?  161 CYS   D CA    1 
ATOM   5202 C  C     . CYS   D 2 162 ? 16.58800 49.53200  6.13100   1.000 29.54723 ?  161 CYS   D C     1 
ATOM   5203 O  O     . CYS   D 2 162 ? 15.73700 49.80200  5.27400   1.000 30.58015 ?  161 CYS   D O     1 
ATOM   5204 C  CB    . CYS   D 2 162 ? 16.87400 47.15400  6.94500   1.000 29.51884 ?  161 CYS   D CB    1 
ATOM   5205 S  SG    . CYS   D 2 162 ? 16.12700 46.19100  5.56700   1.000 28.30629 ?  161 CYS   D SG    1 
ATOM   5206 N  N     . GLY   D 2 163 ? 17.78100 50.10100  6.18400   1.000 30.19277 ?  162 GLY   D N     1 
ATOM   5207 C  CA    . GLY   D 2 163 ? 18.19300 51.03000  5.14700   1.000 28.54026 ?  162 GLY   D CA    1 
ATOM   5208 C  C     . GLY   D 2 163 ? 19.61600 51.49200  5.36400   1.000 30.68751 ?  162 GLY   D C     1 
ATOM   5209 O  O     . GLY   D 2 163 ? 20.34300 50.96400  6.21300   1.000 28.47364 ?  162 GLY   D O     1 
ATOM   5210 N  N     . GLN   D 2 164 ? 20.01300 52.49400  4.57800   1.000 30.56292 ?  163 GLN   D N     1 
ATOM   5211 C  CA    . GLN   D 2 164 ? 21.33900 53.08500  4.69000   1.000 30.71908 ?  163 GLN   D CA    1 
ATOM   5212 C  C     . GLN   D 2 164 ? 21.27700 54.40700  5.44300   1.000 31.38004 ?  163 GLN   D C     1 
ATOM   5213 O  O     . GLN   D 2 164 ? 20.38200 55.21800  5.20500   1.000 35.04984 ?  163 GLN   D O     1 
ATOM   5214 C  CB    . GLN   D 2 164 ? 21.94200 53.31200  3.30000   1.000 30.33431 ?  163 GLN   D CB    1 
ATOM   5215 C  CG    . GLN   D 2 164 ? 23.37200 53.80500  3.38200   1.000 27.48428 ?  163 GLN   D CG    1 
ATOM   5216 C  CD    . GLN   D 2 164 ? 24.08000 53.72800  2.04500   1.000 31.21372 ?  163 GLN   D CD    1 
ATOM   5217 O  OE1   . GLN   D 2 164 ? 23.48800 53.30700  1.03800   1.000 35.00851 ?  163 GLN   D OE1   1 
ATOM   5218 N  NE2   . GLN   D 2 164 ? 25.36500 54.12500  2.02300   1.000 33.95182 ?  163 GLN   D NE2   1 
ATOM   5219 N  N     . LEU   D 2 165 ? 22.22700 54.62400  6.36000   1.000 32.03068 ?  164 LEU   D N     1 
ATOM   5220 C  CA    . LEU   D 2 165 ? 22.27800 55.89700  7.09600   1.000 35.02406 ?  164 LEU   D CA    1 
ATOM   5221 C  C     . LEU   D 2 165 ? 23.12200 56.91000  6.31400   1.000 35.60382 ?  164 LEU   D C     1 
ATOM   5222 O  O     . LEU   D 2 165 ? 24.15700 56.54200  5.74700   1.000 37.77284 ?  164 LEU   D O     1 
ATOM   5223 C  CB    . LEU   D 2 165 ? 22.84200 55.69000  8.50900   1.000 36.10695 ?  164 LEU   D CB    1 
ATOM   5224 C  CG    . LEU   D 2 165 ? 21.91800 54.86900  9.43800   1.000 36.14138 ?  164 LEU   D CG    1 
ATOM   5225 C  CD1   . LEU   D 2 165 ? 22.58200 54.49000  10.74200  1.000 36.70465 ?  164 LEU   D CD1   1 
ATOM   5226 C  CD2   . LEU   D 2 165 ? 20.62400 55.58900  9.71200   1.000 36.71258 ?  164 LEU   D CD2   1 
HETATM 5227 P  PG    . GNP   E 3 .   ? 23.45800 17.80500  7.24800   1.000 24.88359 ?  201 GNP   A PG    1 
HETATM 5228 O  O1G   . GNP   E 3 .   ? 22.39700 18.02500  8.26400   1.000 24.63190 ?  201 GNP   A O1G   1 
HETATM 5229 O  O2G   . GNP   E 3 .   ? 24.52500 16.94700  7.82900   1.000 25.72518 ?  201 GNP   A O2G   1 
HETATM 5230 O  O3G   . GNP   E 3 .   ? 24.06600 19.12800  6.93100   1.000 27.47988 ?  201 GNP   A O3G   1 
HETATM 5231 N  N3B   . GNP   E 3 .   ? 22.82600 17.10800  5.91300   1.000 23.06609 ?  201 GNP   A N3B   1 
HETATM 5232 P  PB    . GNP   E 3 .   ? 21.82900 15.82000  5.86600   1.000 23.33621 ?  201 GNP   A PB    1 
HETATM 5233 O  O1B   . GNP   E 3 .   ? 22.56000 14.51700  5.79800   1.000 24.21388 ?  201 GNP   A O1B   1 
HETATM 5234 O  O2B   . GNP   E 3 .   ? 20.72200 15.96100  6.86500   1.000 20.93647 ?  201 GNP   A O2B   1 
HETATM 5235 O  O3A   . GNP   E 3 .   ? 21.08200 15.95000  4.46200   1.000 25.71125 ?  201 GNP   A O3A   1 
HETATM 5236 P  PA    . GNP   E 3 .   ? 19.59700 16.42500  4.12200   1.000 24.08442 ?  201 GNP   A PA    1 
HETATM 5237 O  O1A   . GNP   E 3 .   ? 18.63600 15.47200  4.72800   1.000 23.97577 -1 201 GNP   A O1A   1 
HETATM 5238 O  O2A   . GNP   E 3 .   ? 19.47500 17.86400  4.46500   1.000 23.85703 ?  201 GNP   A O2A   1 
HETATM 5239 O  "O5'" . GNP   E 3 .   ? 19.58100 16.24500  2.53900   1.000 25.56308 ?  201 GNP   A "O5'" 1 
HETATM 5240 C  "C5'" . GNP   E 3 .   ? 20.48800 17.01200  1.72200   1.000 27.28414 ?  201 GNP   A "C5'" 1 
HETATM 5241 C  "C4'" . GNP   E 3 .   ? 19.90000 17.13800  0.34000   1.000 28.43574 ?  201 GNP   A "C4'" 1 
HETATM 5242 O  "O4'" . GNP   E 3 .   ? 19.73400 15.81200  -0.22200  1.000 26.39428 ?  201 GNP   A "O4'" 1 
HETATM 5243 C  "C3'" . GNP   E 3 .   ? 18.51700 17.79900  0.26600   1.000 35.98692 ?  201 GNP   A "C3'" 1 
HETATM 5244 O  "O3'" . GNP   E 3 .   ? 18.40000 18.62300  -0.88600  1.000 39.04857 ?  201 GNP   A "O3'" 1 
HETATM 5245 C  "C2'" . GNP   E 3 .   ? 17.57000 16.59800  0.20700   1.000 28.93526 ?  201 GNP   A "C2'" 1 
HETATM 5246 O  "O2'" . GNP   E 3 .   ? 16.34600 16.89000  -0.42500  1.000 31.63045 ?  201 GNP   A "O2'" 1 
HETATM 5247 C  "C1'" . GNP   E 3 .   ? 18.39400 15.60600  -0.60100  1.000 28.29109 ?  201 GNP   A "C1'" 1 
HETATM 5248 N  N9    . GNP   E 3 .   ? 18.04500 14.21500  -0.34700  1.000 24.79464 ?  201 GNP   A N9    1 
HETATM 5249 C  C8    . GNP   E 3 .   ? 18.04400 13.57400  0.86500   1.000 23.31823 ?  201 GNP   A C8    1 
HETATM 5250 N  N7    . GNP   E 3 .   ? 17.67700 12.32100  0.78900   1.000 24.31482 ?  201 GNP   A N7    1 
HETATM 5251 C  C5    . GNP   E 3 .   ? 17.41500 12.12300  -0.55900  1.000 24.25959 ?  201 GNP   A C5    1 
HETATM 5252 C  C6    . GNP   E 3 .   ? 16.98300 10.96100  -1.24300  1.000 25.19132 ?  201 GNP   A C6    1 
HETATM 5253 O  O6    . GNP   E 3 .   ? 16.73600 9.84200   -0.77900  1.000 25.48479 ?  201 GNP   A O6    1 
HETATM 5254 N  N1    . GNP   E 3 .   ? 16.84700 11.19900  -2.60800  1.000 31.45859 ?  201 GNP   A N1    1 
HETATM 5255 C  C2    . GNP   E 3 .   ? 17.09100 12.39400  -3.23300  1.000 29.74713 ?  201 GNP   A C2    1 
HETATM 5256 N  N2    . GNP   E 3 .   ? 16.90000 12.42500  -4.55600  1.000 33.30176 ?  201 GNP   A N2    1 
HETATM 5257 N  N3    . GNP   E 3 .   ? 17.49700 13.48800  -2.59700  1.000 28.10512 ?  201 GNP   A N3    1 
HETATM 5258 C  C4    . GNP   E 3 .   ? 17.63800 13.28100  -1.26900  1.000 26.30877 ?  201 GNP   A C4    1 
HETATM 5259 MG MG    . MG    F 4 .   ? 20.60900 17.27900  8.46300   1.000 22.26578 ?  202 MG    A MG    1 
HETATM 5260 P  PG    . GNP   G 3 .   ? 59.09900 -20.50900 24.27600  1.000 28.25802 ?  201 GNP   B PG    1 
HETATM 5261 O  O1G   . GNP   G 3 .   ? 58.53200 -20.12200 25.59700  1.000 28.18428 ?  201 GNP   B O1G   1 
HETATM 5262 O  O2G   . GNP   G 3 .   ? 58.24200 -21.55400 23.65600  1.000 27.15257 ?  201 GNP   B O2G   1 
HETATM 5263 O  O3G   . GNP   G 3 .   ? 60.44000 -21.11200 24.52100  1.000 31.20890 ?  201 GNP   B O3G   1 
HETATM 5264 N  N3B   . GNP   G 3 .   ? 59.22400 -19.18900 23.32800  1.000 30.96832 ?  201 GNP   B N3B   1 
HETATM 5265 P  PB    . GNP   G 3 .   ? 58.08500 -18.04300 23.12000  1.000 26.66316 ?  201 GNP   B PB    1 
HETATM 5266 O  O1B   . GNP   G 3 .   ? 57.14300 -18.36900 22.00700  1.000 27.71272 ?  201 GNP   B O1B   1 
HETATM 5267 O  O2B   . GNP   G 3 .   ? 57.50500 -17.62000 24.43300  1.000 27.07467 ?  201 GNP   B O2B   1 
HETATM 5268 O  O3A   . GNP   G 3 .   ? 58.89100 -16.75900 22.61100  1.000 29.56411 ?  201 GNP   B O3A   1 
HETATM 5269 P  PA    . GNP   G 3 .   ? 59.29300 -15.38000 23.31500  1.000 30.81080 ?  201 GNP   B PA    1 
HETATM 5270 O  O1A   . GNP   G 3 .   ? 58.05500 -14.65400 23.69700  1.000 26.87398 -1 201 GNP   B O1A   1 
HETATM 5271 O  O2A   . GNP   G 3 .   ? 60.29800 -15.63800 24.37500  1.000 24.78333 ?  201 GNP   B O2A   1 
HETATM 5272 O  "O5'" . GNP   G 3 .   ? 59.98600 -14.61000 22.09600  1.000 28.18652 ?  201 GNP   B "O5'" 1 
HETATM 5273 C  "C5'" . GNP   G 3 .   ? 61.17300 -15.16000 21.48200  1.000 34.41721 ?  201 GNP   B "C5'" 1 
HETATM 5274 C  "C4'" . GNP   G 3 .   ? 62.02300 -14.04900 20.91200  1.000 34.62370 ?  201 GNP   B "C4'" 1 
HETATM 5275 O  "O4'" . GNP   G 3 .   ? 61.26700 -13.31600 19.91200  1.000 32.38584 ?  201 GNP   B "O4'" 1 
HETATM 5276 C  "C3'" . GNP   G 3 .   ? 62.51100 -12.99400 21.91200  1.000 35.13179 ?  201 GNP   B "C3'" 1 
HETATM 5277 O  "O3'" . GNP   G 3 .   ? 63.81500 -12.54200 21.57600  1.000 39.29275 ?  201 GNP   B "O3'" 1 
HETATM 5278 C  "C2'" . GNP   G 3 .   ? 61.47900 -11.87800 21.74800  1.000 37.46553 ?  201 GNP   B "C2'" 1 
HETATM 5279 O  "O2'" . GNP   G 3 .   ? 61.97500 -10.61800 22.12900  1.000 38.38784 ?  201 GNP   B "O2'" 1 
HETATM 5280 C  "C1'" . GNP   G 3 .   ? 61.20200 -11.95000 20.25300  1.000 38.12244 ?  201 GNP   B "C1'" 1 
HETATM 5281 N  N9    . GNP   G 3 .   ? 59.88600 -11.44600 19.89200  1.000 34.78801 ?  201 GNP   B N9    1 
HETATM 5282 C  C8    . GNP   G 3 .   ? 58.68800 -11.87200 20.40100  1.000 34.35272 ?  201 GNP   B C8    1 
HETATM 5283 N  N7    . GNP   G 3 .   ? 57.65800 -11.24200 19.89800  1.000 33.73493 ?  201 GNP   B N7    1 
HETATM 5284 C  C5    . GNP   G 3 .   ? 58.21600 -10.33800 19.00700  1.000 32.22040 ?  201 GNP   B C5    1 
HETATM 5285 C  C6    . GNP   G 3 .   ? 57.58700 -9.38600  18.17300  1.000 33.40064 ?  201 GNP   B C6    1 
HETATM 5286 O  O6    . GNP   G 3 .   ? 56.37900 -9.15700  18.05200  1.000 33.57824 ?  201 GNP   B O6    1 
HETATM 5287 N  N1    . GNP   G 3 .   ? 58.52000 -8.67800  17.41900  1.000 35.72124 ?  201 GNP   B N1    1 
HETATM 5288 C  C2    . GNP   G 3 .   ? 59.87800 -8.85600  17.46600  1.000 36.63076 ?  201 GNP   B C2    1 
HETATM 5289 N  N2    . GNP   G 3 .   ? 60.61100 -8.07100  16.66600  1.000 38.96344 ?  201 GNP   B N2    1 
HETATM 5290 N  N3    . GNP   G 3 .   ? 60.47700 -9.74900  18.25100  1.000 32.96874 ?  201 GNP   B N3    1 
HETATM 5291 C  C4    . GNP   G 3 .   ? 59.58600 -10.45300 18.99100  1.000 36.69157 ?  201 GNP   B C4    1 
HETATM 5292 MG MG    . MG    H 4 .   ? 57.73300 -18.43500 26.26700  1.000 25.92265 ?  202 MG    B MG    1 
HETATM 5293 C  C1    . A1AOJ I 5 .   ? 66.86700 -29.33300 31.82000  1.000 21.03772 ?  201 A1AOJ C C1    1 
HETATM 5294 C  C10   . A1AOJ I 5 .   ? 70.82500 -20.88900 28.60200  1.000 33.47260 ?  201 A1AOJ C C10   1 
HETATM 5295 C  C11   . A1AOJ I 5 .   ? 68.24100 -20.67600 28.97100  1.000 29.15390 ?  201 A1AOJ C C11   1 
HETATM 5296 C  C12   . A1AOJ I 5 .   ? 66.29300 -26.31800 27.87100  1.000 22.53357 ?  201 A1AOJ C C12   1 
HETATM 5297 C  C13   . A1AOJ I 5 .   ? 64.83900 -25.99700 27.98800  1.000 24.90848 ?  201 A1AOJ C C13   1 
HETATM 5298 C  C14   . A1AOJ I 5 .   ? 62.68600 -26.22100 28.46800  1.000 24.97509 ?  201 A1AOJ C C14   1 
HETATM 5299 C  C15   . A1AOJ I 5 .   ? 62.68000 -24.90700 28.12000  1.000 28.63174 ?  201 A1AOJ C C15   1 
HETATM 5300 C  C16   . A1AOJ I 5 .   ? 61.53800 -27.00700 28.94900  1.000 24.35419 ?  201 A1AOJ C C16   1 
HETATM 5301 C  C17   . A1AOJ I 5 .   ? 61.75200 -28.17200 29.67600  1.000 23.27956 ?  201 A1AOJ C C17   1 
HETATM 5302 C  C18   . A1AOJ I 5 .   ? 60.66900 -28.89700 30.16400  1.000 23.67602 ?  201 A1AOJ C C18   1 
HETATM 5303 C  C19   . A1AOJ I 5 .   ? 59.36100 -28.42100 29.92100  1.000 23.40357 ?  201 A1AOJ C C19   1 
HETATM 5304 C  C2    . A1AOJ I 5 .   ? 66.00600 -28.20200 31.22800  1.000 21.42247 ?  201 A1AOJ C C2    1 
HETATM 5305 C  C20   . A1AOJ I 5 .   ? 59.13000 -27.24000 29.21600  1.000 24.60956 ?  201 A1AOJ C C20   1 
HETATM 5306 C  C21   . A1AOJ I 5 .   ? 60.23000 -26.56200 28.72500  1.000 26.75676 ?  201 A1AOJ C C21   1 
HETATM 5307 C  C22   . A1AOJ I 5 .   ? 57.00200 -29.17700 30.44900  1.000 26.91203 ?  201 A1AOJ C C22   1 
HETATM 5308 C  C23   . A1AOJ I 5 .   ? 56.45100 -29.61400 29.12200  1.000 34.29522 ?  201 A1AOJ C C23   1 
HETATM 5309 C  C24   . A1AOJ I 5 .   ? 59.19400 -30.32500 31.11600  1.000 23.40327 ?  201 A1AOJ C C24   1 
HETATM 5310 C  C25   . A1AOJ I 5 .   ? 58.57900 -31.48900 31.75800  1.000 24.40865 ?  201 A1AOJ C C25   1 
HETATM 5311 C  C26   . A1AOJ I 5 .   ? 57.81500 -31.41500 32.93500  1.000 25.03636 ?  201 A1AOJ C C26   1 
HETATM 5312 C  C27   . A1AOJ I 5 .   ? 57.56400 -30.11400 33.66100  1.000 26.87926 ?  201 A1AOJ C C27   1 
HETATM 5313 C  C28   . A1AOJ I 5 .   ? 55.86800 -28.46000 33.80200  1.000 27.17375 ?  201 A1AOJ C C28   1 
HETATM 5314 C  C29   . A1AOJ I 5 .   ? 57.92500 -30.21500 35.12700  1.000 26.39785 ?  201 A1AOJ C C29   1 
HETATM 5315 C  C3    . A1AOJ I 5 .   ? 68.90500 -28.06200 31.17300  1.000 23.26002 ?  201 A1AOJ C C3    1 
HETATM 5316 C  C30   . A1AOJ I 5 .   ? 57.44500 -33.68500 32.85700  1.000 26.12943 ?  201 A1AOJ C C30   1 
HETATM 5317 C  C31   . A1AOJ I 5 .   ? 58.17200 -33.84400 31.70300  1.000 29.47060 ?  201 A1AOJ C C31   1 
HETATM 5318 C  C32   . A1AOJ I 5 .   ? 58.73800 -32.73400 31.15200  1.000 23.27213 ?  201 A1AOJ C C32   1 
HETATM 5319 C  C33   . A1AOJ I 5 .   ? 60.55300 -30.11800 30.90100  1.000 21.65981 ?  201 A1AOJ C C33   1 
HETATM 5320 C  C34   . A1AOJ I 5 .   ? 61.68400 -30.98100 31.38200  1.000 20.95870 ?  201 A1AOJ C C34   1 
HETATM 5321 C  C35   . A1AOJ I 5 .   ? 62.27400 -30.61100 32.75300  1.000 21.05542 ?  201 A1AOJ C C35   1 
HETATM 5322 C  C36   . A1AOJ I 5 .   ? 63.42700 -31.58100 33.05400  1.000 20.99557 ?  201 A1AOJ C C36   1 
HETATM 5323 C  C37   . A1AOJ I 5 .   ? 61.19300 -30.77300 33.82500  1.000 23.15367 ?  201 A1AOJ C C37   1 
HETATM 5324 C  C38   . A1AOJ I 5 .   ? 62.80400 -29.17900 32.78600  1.000 20.53609 ?  201 A1AOJ C C38   1 
HETATM 5325 C  C39   . A1AOJ I 5 .   ? 64.75300 -28.06000 32.04700  1.000 20.72832 ?  201 A1AOJ C C39   1 
HETATM 5326 C  C4    . A1AOJ I 5 .   ? 68.22600 -29.42100 31.13500  1.000 21.85355 ?  201 A1AOJ C C4    1 
HETATM 5327 C  C5    . A1AOJ I 5 .   ? 68.21600 -26.31300 29.47600  1.000 22.06569 ?  201 A1AOJ C C5    1 
HETATM 5328 C  C6    . A1AOJ I 5 .   ? 67.06200 -25.49200 28.90900  1.000 25.03937 ?  201 A1AOJ C C6    1 
HETATM 5329 C  C7    . A1AOJ I 5 .   ? 67.73800 -23.17300 29.07600  1.000 22.10287 ?  201 A1AOJ C C7    1 
HETATM 5330 C  C8    . A1AOJ I 5 .   ? 68.47300 -22.06800 28.44300  1.000 23.44472 ?  201 A1AOJ C C8    1 
HETATM 5331 C  C9    . A1AOJ I 5 .   ? 69.54000 -21.34200 29.25400  1.000 26.14217 ?  201 A1AOJ C C9    1 
HETATM 5332 N  N1    . A1AOJ I 5 .   ? 66.73500 -26.92600 31.30300  1.000 21.70678 ?  201 A1AOJ C N1    1 
HETATM 5333 N  N2    . A1AOJ I 5 .   ? 67.97200 -27.06800 30.62400  1.000 22.36344 ?  201 A1AOJ C N2    1 
HETATM 5334 N  N3    . A1AOJ I 5 .   ? 67.58100 -24.26500 28.32700  1.000 22.91033 ?  201 A1AOJ C N3    1 
HETATM 5335 N  N4    . A1AOJ I 5 .   ? 63.93700 -26.84200 28.42000  1.000 22.37888 ?  201 A1AOJ C N4    1 
HETATM 5336 N  N5    . A1AOJ I 5 .   ? 58.47100 -29.31000 30.49800  1.000 24.81668 ?  201 A1AOJ C N5    1 
HETATM 5337 N  N6    . A1AOJ I 5 .   ? 57.26600 -32.52100 33.46200  1.000 26.95453 ?  201 A1AOJ C N6    1 
HETATM 5338 O  O1    . A1AOJ I 5 .   ? 69.30700 -26.36600 28.92000  1.000 21.99221 ?  201 A1AOJ C O1    1 
HETATM 5339 O  O2    . A1AOJ I 5 .   ? 67.30800 -23.10800 30.22700  1.000 24.25273 ?  201 A1AOJ C O2    1 
HETATM 5340 O  O3    . A1AOJ I 5 .   ? 56.17000 -29.80700 33.51700  1.000 25.82664 ?  201 A1AOJ C O3    1 
HETATM 5341 O  O4    . A1AOJ I 5 .   ? 63.98700 -29.14400 31.93400  1.000 23.20190 ?  201 A1AOJ C O4    1 
HETATM 5342 O  O5    . A1AOJ I 5 .   ? 64.51500 -27.13400 32.76000  1.000 21.37051 ?  201 A1AOJ C O5    1 
HETATM 5343 S  S1    . A1AOJ I 5 .   ? 64.25100 -24.39600 27.67500  1.000 30.77099 ?  201 A1AOJ C S1    1 
HETATM 5344 C  C1    . A1AOJ J 5 .   ? 27.68700 30.08600  12.26400  1.000 22.00288 ?  201 A1AOJ D C1    1 
HETATM 5345 C  C10   . A1AOJ J 5 .   ? 23.25000 29.47700  3.50700   1.000 31.55832 ?  201 A1AOJ D C10   1 
HETATM 5346 C  C11   . A1AOJ J 5 .   ? 22.43800 27.52700  5.07000   1.000 24.23558 ?  201 A1AOJ D C11   1 
HETATM 5347 C  C12   . A1AOJ J 5 .   ? 27.30900 26.76400  8.63500   1.000 21.97345 ?  201 A1AOJ D C12   1 
HETATM 5348 C  C13   . A1AOJ J 5 .   ? 26.81700 25.55600  9.38100   1.000 21.80111 ?  201 A1AOJ D C13   1 
HETATM 5349 C  C14   . A1AOJ J 5 .   ? 26.51600 24.13200  11.05900  1.000 23.54725 ?  201 A1AOJ D C14   1 
HETATM 5350 C  C15   . A1AOJ J 5 .   ? 25.61200 23.60000  10.20200  1.000 24.07086 ?  201 A1AOJ D C15   1 
HETATM 5351 C  C16   . A1AOJ J 5 .   ? 26.80300 23.69500  12.42600  1.000 21.07360 ?  201 A1AOJ D C16   1 
HETATM 5352 C  C17   . A1AOJ J 5 .   ? 27.38100 24.58400  13.34000  1.000 18.84684 ?  201 A1AOJ D C17   1 
HETATM 5353 C  C18   . A1AOJ J 5 .   ? 27.62800 24.16400  14.64400  1.000 21.43606 ?  201 A1AOJ D C18   1 
HETATM 5354 C  C19   . A1AOJ J 5 .   ? 27.25800 22.84900  15.00900  1.000 22.54628 ?  201 A1AOJ D C19   1 
HETATM 5355 C  C2    . A1AOJ J 5 .   ? 26.96900 28.78700  11.85800  1.000 21.25025 ?  201 A1AOJ D C2    1 
HETATM 5356 C  C20   . A1AOJ J 5 .   ? 26.66400 21.96300  14.11200  1.000 23.12369 ?  201 A1AOJ D C20   1 
HETATM 5357 C  C21   . A1AOJ J 5 .   ? 26.44800 22.40300  12.82400  1.000 24.08524 ?  201 A1AOJ D C21   1 
HETATM 5358 C  C22   . A1AOJ J 5 .   ? 27.40600 21.40100  17.05300  1.000 27.46846 ?  201 A1AOJ D C22   1 
HETATM 5359 C  C23   . A1AOJ J 5 .   ? 28.52700 20.46100  16.68400  1.000 28.22996 ?  201 A1AOJ D C23   1 
HETATM 5360 C  C24   . A1AOJ J 5 .   ? 28.16500 23.83100  16.83900  1.000 20.88055 ?  201 A1AOJ D C24   1 
HETATM 5361 C  C25   . A1AOJ J 5 .   ? 28.67900 23.93200  18.21900  1.000 22.82459 ?  201 A1AOJ D C25   1 
HETATM 5362 C  C26   . A1AOJ J 5 .   ? 27.83700 23.92000  19.37400  1.000 23.90184 ?  201 A1AOJ D C26   1 
HETATM 5363 C  C27   . A1AOJ J 5 .   ? 26.33800 23.77300  19.30200  1.000 20.97006 ?  201 A1AOJ D C27   1 
HETATM 5364 C  C28   . A1AOJ J 5 .   ? 24.79200 21.97100  19.53700  1.000 26.94375 ?  201 A1AOJ D C28   1 
HETATM 5365 C  C29   . A1AOJ J 5 .   ? 25.68800 24.84500  20.15100  1.000 22.83873 ?  201 A1AOJ D C29   1 
HETATM 5366 C  C3    . A1AOJ J 5 .   ? 27.13400 31.07000  10.08400  1.000 22.19704 ?  201 A1AOJ D C3    1 
HETATM 5367 C  C30   . A1AOJ J 5 .   ? 29.65200 24.13600  20.75900  1.000 28.43280 ?  201 A1AOJ D C30   1 
HETATM 5368 C  C31   . A1AOJ J 5 .   ? 30.53900 24.16900  19.71200  1.000 28.59820 ?  201 A1AOJ D C31   1 
HETATM 5369 C  C32   . A1AOJ J 5 .   ? 30.05100 24.05400  18.42300  1.000 26.63990 ?  201 A1AOJ D C32   1 
HETATM 5370 C  C33   . A1AOJ J 5 .   ? 28.20900 24.79400  15.80100  1.000 19.06458 ?  201 A1AOJ D C33   1 
HETATM 5371 C  C34   . A1AOJ J 5 .   ? 28.75400 26.20000  15.87900  1.000 21.57772 ?  201 A1AOJ D C34   1 
HETATM 5372 C  C35   . A1AOJ J 5 .   ? 27.70800 27.28100  16.27100  1.000 18.70467 ?  201 A1AOJ D C35   1 
HETATM 5373 C  C36   . A1AOJ J 5 .   ? 28.39400 28.65000  16.30200  1.000 21.20379 ?  201 A1AOJ D C36   1 
HETATM 5374 C  C37   . A1AOJ J 5 .   ? 27.10700 27.03300  17.65600  1.000 20.94921 ?  201 A1AOJ D C37   1 
HETATM 5375 C  C38   . A1AOJ J 5 .   ? 26.57700 27.34900  15.24500  1.000 20.14517 ?  201 A1AOJ D C38   1 
HETATM 5376 C  C39   . A1AOJ J 5 .   ? 26.28400 28.17400  13.05500  1.000 20.72273 ?  201 A1AOJ D C39   1 
HETATM 5377 C  C4    . A1AOJ J 5 .   ? 28.26700 30.79900  11.04000  1.000 21.32583 ?  201 A1AOJ D C4    1 
HETATM 5378 C  C5    . A1AOJ J 5 .   ? 26.61400 29.17600  8.54400   1.000 20.66007 ?  201 A1AOJ D C5    1 
HETATM 5379 C  C6    . A1AOJ J 5 .   ? 26.13400 27.73000  8.40300   1.000 20.68700 ?  201 A1AOJ D C6    1 
HETATM 5380 C  C7    . A1AOJ J 5 .   ? 24.25300 27.79200  6.82500   1.000 22.50172 ?  201 A1AOJ D C7    1 
HETATM 5381 C  C8    . A1AOJ J 5 .   ? 23.89100 27.76700  5.40000   1.000 23.54736 ?  201 A1AOJ D C8    1 
HETATM 5382 C  C9    . A1AOJ J 5 .   ? 23.00800 28.88900  4.87600   1.000 25.62236 ?  201 A1AOJ D C9    1 
HETATM 5383 N  N1    . A1AOJ J 5 .   ? 25.94200 29.05400  10.84600  1.000 19.13635 ?  201 A1AOJ D N1    1 
HETATM 5384 N  N2    . A1AOJ J 5 .   ? 26.52900 29.76700  9.77800   1.000 19.26032 ?  201 A1AOJ D N2    1 
HETATM 5385 N  N3    . A1AOJ J 5 .   ? 25.54800 27.54100  7.08100   1.000 19.82052 ?  201 A1AOJ D N3    1 
HETATM 5386 N  N4    . A1AOJ J 5 .   ? 27.22800 25.22200  10.56800  1.000 19.10915 ?  201 A1AOJ D N4    1 
HETATM 5387 N  N5    . A1AOJ J 5 .   ? 27.58300 22.67000  16.33700  1.000 23.00208 ?  201 A1AOJ D N5    1 
HETATM 5388 N  N6    . A1AOJ J 5 .   ? 28.33500 24.02500  20.61600  1.000 25.13267 ?  201 A1AOJ D N6    1 
HETATM 5389 O  O1    . A1AOJ J 5 .   ? 27.10300 29.78400  7.59800   1.000 20.55552 ?  201 A1AOJ D O1    1 
HETATM 5390 O  O2    . A1AOJ J 5 .   ? 23.42600 28.08300  7.69100   1.000 19.42465 ?  201 A1AOJ D O2    1 
HETATM 5391 O  O3    . A1AOJ J 5 .   ? 26.06600 22.49100  19.87000  1.000 27.61227 ?  201 A1AOJ D O3    1 
HETATM 5392 O  O4    . A1AOJ J 5 .   ? 27.16200 27.83700  14.00200  1.000 20.73828 ?  201 A1AOJ D O4    1 
HETATM 5393 O  O5    . A1AOJ J 5 .   ? 25.09400 28.04400  13.16200  1.000 19.05092 ?  201 A1AOJ D O5    1 
HETATM 5394 S  S1    . A1AOJ J 5 .   ? 25.57700 24.52000  8.75500   1.000 26.45101 ?  201 A1AOJ D S1    1 
HETATM 5395 O  O     . HOH   K 6 .   ? 25.14800 17.30400  18.24500  1.000 47.12789 ?  301 HOH   A O     1 
HETATM 5396 O  O     . HOH   K 6 .   ? 10.74800 27.29800  -0.55400  1.000 42.75534 ?  302 HOH   A O     1 
HETATM 5397 O  O     . HOH   K 6 .   ? 16.11300 17.73400  11.52600  1.000 30.72263 ?  303 HOH   A O     1 
HETATM 5398 O  O     . HOH   K 6 .   ? 33.70600 15.17900  21.45300  1.000 39.10430 ?  304 HOH   A O     1 
HETATM 5399 O  O     . HOH   K 6 .   ? 14.57200 8.05800   25.75100  1.000 42.66085 ?  305 HOH   A O     1 
HETATM 5400 O  O     . HOH   K 6 .   ? 27.07700 6.72200   -11.86300 1.000 56.15448 ?  306 HOH   A O     1 
HETATM 5401 O  O     . HOH   K 6 .   ? 7.93800  -1.40900  24.73900  1.000 46.04473 ?  307 HOH   A O     1 
HETATM 5402 O  O     . HOH   K 6 .   ? 34.27500 13.79600  18.57000  1.000 39.64779 ?  308 HOH   A O     1 
HETATM 5403 O  O     . HOH   K 6 .   ? 8.40400  12.31400  -1.52400  1.000 41.19520 ?  309 HOH   A O     1 
HETATM 5404 O  O     . HOH   K 6 .   ? 20.33500 25.56700  1.68800   1.000 40.03686 ?  310 HOH   A O     1 
HETATM 5405 O  O     . HOH   K 6 .   ? 12.73500 4.13500   -4.43900  1.000 37.26082 ?  311 HOH   A O     1 
HETATM 5406 O  O     . HOH   K 6 .   ? 7.09700  4.03200   11.30100  1.000 44.80487 ?  312 HOH   A O     1 
HETATM 5407 O  O     . HOH   K 6 .   ? 18.43100 -6.97600  12.50000  1.000 42.08627 ?  313 HOH   A O     1 
HETATM 5408 O  O     . HOH   K 6 .   ? 13.20700 -2.61200  2.99900   1.000 50.00996 ?  314 HOH   A O     1 
HETATM 5409 O  O     . HOH   K 6 .   ? 6.26800  0.43100   7.60100   1.000 46.45879 ?  315 HOH   A O     1 
HETATM 5410 O  O     . HOH   K 6 .   ? 30.94100 14.07800  8.63200   1.000 37.82496 ?  316 HOH   A O     1 
HETATM 5411 O  O     . HOH   K 6 .   ? 29.24500 -5.46400  14.56100  1.000 43.80107 ?  317 HOH   A O     1 
HETATM 5412 O  O     . HOH   K 6 .   ? 16.33600 0.67500   25.02800  1.000 40.85730 ?  318 HOH   A O     1 
HETATM 5413 O  O     . HOH   K 6 .   ? 21.13000 15.95400  9.97200   1.000 22.86711 ?  319 HOH   A O     1 
HETATM 5414 O  O     . HOH   K 6 .   ? 29.72400 26.51700  11.35400  1.000 24.00357 ?  320 HOH   A O     1 
HETATM 5415 O  O     . HOH   K 6 .   ? 4.92500  3.79700   8.28300   1.000 43.30089 ?  321 HOH   A O     1 
HETATM 5416 O  O     . HOH   K 6 .   ? 36.11100 19.61300  15.41500  1.000 35.73891 ?  322 HOH   A O     1 
HETATM 5417 O  O     . HOH   K 6 .   ? 17.41600 19.45500  4.45900   1.000 32.20558 ?  323 HOH   A O     1 
HETATM 5418 O  O     . HOH   K 6 .   ? 10.32100 -2.76800  22.59300  1.000 40.50578 ?  324 HOH   A O     1 
HETATM 5419 O  O     . HOH   K 6 .   ? 14.55900 11.01100  -8.06300  1.000 42.33018 ?  325 HOH   A O     1 
HETATM 5420 O  O     . HOH   K 6 .   ? 12.57400 16.67900  3.28600   1.000 42.86385 ?  326 HOH   A O     1 
HETATM 5421 O  O     . HOH   K 6 .   ? 33.16800 5.01600   26.62500  1.000 49.21355 ?  327 HOH   A O     1 
HETATM 5422 O  O     . HOH   K 6 .   ? 18.79800 24.27700  10.41700  1.000 37.59819 ?  328 HOH   A O     1 
HETATM 5423 O  O     . HOH   K 6 .   ? 16.05300 3.69000   -8.32500  1.000 47.64295 ?  329 HOH   A O     1 
HETATM 5424 O  O     . HOH   K 6 .   ? 13.57500 10.37400  28.12500  1.000 46.27194 ?  330 HOH   A O     1 
HETATM 5425 O  O     . HOH   K 6 .   ? 11.09800 16.83400  18.85500  1.000 35.75027 ?  331 HOH   A O     1 
HETATM 5426 O  O     . HOH   K 6 .   ? 28.44700 15.05800  21.30300  1.000 32.01435 ?  332 HOH   A O     1 
HETATM 5427 O  O     . HOH   K 6 .   ? 25.15500 20.25700  9.08300   1.000 25.39734 ?  333 HOH   A O     1 
HETATM 5428 O  O     . HOH   K 6 .   ? 24.29200 -4.01200  14.54400  1.000 32.44581 ?  334 HOH   A O     1 
HETATM 5429 O  O     . HOH   K 6 .   ? 12.23500 14.20600  4.25000   1.000 27.78726 ?  335 HOH   A O     1 
HETATM 5430 O  O     . HOH   K 6 .   ? 24.97600 -1.62500  -7.37000  1.000 52.79484 ?  336 HOH   A O     1 
HETATM 5431 O  O     . HOH   K 6 .   ? 32.48700 21.49800  7.59400   1.000 51.98150 ?  337 HOH   A O     1 
HETATM 5432 O  O     . HOH   K 6 .   ? 10.24700 2.64000   29.50600  1.000 51.41871 ?  338 HOH   A O     1 
HETATM 5433 O  O     . HOH   K 6 .   ? 18.72600 17.78300  20.55300  1.000 45.18904 ?  339 HOH   A O     1 
HETATM 5434 O  O     . HOH   K 6 .   ? 24.94100 17.59800  15.81200  1.000 25.68856 ?  340 HOH   A O     1 
HETATM 5435 O  O     . HOH   K 6 .   ? 3.61500  7.14900   15.26200  1.000 42.14335 ?  341 HOH   A O     1 
HETATM 5436 O  O     . HOH   K 6 .   ? 28.47300 9.31000   5.11900   1.000 27.13480 ?  342 HOH   A O     1 
HETATM 5437 O  O     . HOH   K 6 .   ? 6.92300  6.66600   8.25400   1.000 40.80195 ?  343 HOH   A O     1 
HETATM 5438 O  O     . HOH   K 6 .   ? 12.72300 -7.68100  17.50900  1.000 41.72128 ?  344 HOH   A O     1 
HETATM 5439 O  O     . HOH   K 6 .   ? 29.94300 16.47000  12.56100  1.000 34.17769 ?  345 HOH   A O     1 
HETATM 5440 O  O     . HOH   K 6 .   ? 19.75400 18.60800  7.06400   1.000 25.24186 ?  346 HOH   A O     1 
HETATM 5441 O  O     . HOH   K 6 .   ? 24.43800 12.87200  -2.57800  1.000 31.58713 ?  347 HOH   A O     1 
HETATM 5442 O  O     . HOH   K 6 .   ? 14.86300 -3.76700  24.18000  1.000 43.85276 ?  348 HOH   A O     1 
HETATM 5443 O  O     . HOH   K 6 .   ? 33.39100 -2.69200  0.73800   1.000 45.17143 ?  349 HOH   A O     1 
HETATM 5444 O  O     . HOH   K 6 .   ? 15.97700 -5.70700  7.79700   1.000 50.32358 ?  350 HOH   A O     1 
HETATM 5445 O  O     . HOH   K 6 .   ? 15.25200 -1.21500  0.61200   1.000 41.04698 ?  351 HOH   A O     1 
HETATM 5446 O  O     . HOH   K 6 .   ? 5.87800  11.62100  16.47000  1.000 34.31622 ?  352 HOH   A O     1 
HETATM 5447 O  O     . HOH   K 6 .   ? 35.55100 25.60500  11.80500  1.000 44.20973 ?  353 HOH   A O     1 
HETATM 5448 O  O     . HOH   K 6 .   ? 33.42700 -10.74700 -5.15400  1.000 48.29566 ?  354 HOH   A O     1 
HETATM 5449 O  O     . HOH   K 6 .   ? 18.63800 9.45200   20.54200  1.000 28.33014 ?  355 HOH   A O     1 
HETATM 5450 O  O     . HOH   K 6 .   ? 38.59200 2.92700   22.72800  1.000 42.35701 ?  356 HOH   A O     1 
HETATM 5451 O  O     . HOH   K 6 .   ? 26.03300 -7.56400  4.11700   1.000 47.23689 ?  357 HOH   A O     1 
HETATM 5452 O  O     . HOH   K 6 .   ? 37.93600 2.22700   16.18900  1.000 42.31700 ?  358 HOH   A O     1 
HETATM 5453 O  O     . HOH   K 6 .   ? 24.06500 0.22400   22.80700  1.000 35.45526 ?  359 HOH   A O     1 
HETATM 5454 O  O     . HOH   K 6 .   ? 18.17000 20.52400  9.69200   1.000 31.43828 ?  360 HOH   A O     1 
HETATM 5455 O  O     . HOH   K 6 .   ? 8.12700  16.96100  -2.33800  1.000 53.74990 ?  361 HOH   A O     1 
HETATM 5456 O  O     . HOH   K 6 .   ? 4.58100  -5.40400  14.50300  1.000 52.98675 ?  362 HOH   A O     1 
HETATM 5457 O  O     . HOH   K 6 .   ? 27.85300 18.01300  19.39200  1.000 38.27290 ?  363 HOH   A O     1 
HETATM 5458 O  O     . HOH   K 6 .   ? 18.09300 27.14900  8.82500   1.000 45.51075 ?  364 HOH   A O     1 
HETATM 5459 O  O     . HOH   K 6 .   ? 15.41800 -6.58600  10.59700  1.000 47.22718 ?  365 HOH   A O     1 
HETATM 5460 O  O     . HOH   K 6 .   ? 21.96700 -6.49700  5.29300   1.000 40.14052 ?  366 HOH   A O     1 
HETATM 5461 O  O     . HOH   K 6 .   ? 8.31500  5.47700   27.51600  1.000 42.90476 ?  367 HOH   A O     1 
HETATM 5462 O  O     . HOH   K 6 .   ? 23.29500 -6.20500  18.06500  1.000 40.68716 ?  368 HOH   A O     1 
HETATM 5463 O  O     . HOH   K 6 .   ? 0.53000  2.15000   22.53200  1.000 45.86990 ?  369 HOH   A O     1 
HETATM 5464 O  O     A HOH   K 6 .   ? 18.22000 13.95500  22.40300  0.500 26.53620 ?  370 HOH   A O     1 
HETATM 5465 O  O     B HOH   K 6 .   ? 17.39500 12.60500  21.09300  0.500 26.55746 ?  370 HOH   A O     1 
HETATM 5466 O  O     . HOH   K 6 .   ? 25.60300 -8.00300  6.76000   1.000 42.76315 ?  371 HOH   A O     1 
HETATM 5467 O  O     . HOH   K 6 .   ? 37.42400 7.80000   13.01800  1.000 39.64905 ?  372 HOH   A O     1 
HETATM 5468 O  O     . HOH   K 6 .   ? 26.85200 12.92400  11.53400  1.000 25.87642 ?  373 HOH   A O     1 
HETATM 5469 O  O     . HOH   K 6 .   ? 18.04500 -2.87100  1.05900   1.000 43.09202 ?  374 HOH   A O     1 
HETATM 5470 O  O     . HOH   K 6 .   ? 9.27600  2.96900   4.37500   1.000 30.70301 ?  375 HOH   A O     1 
HETATM 5471 O  O     . HOH   K 6 .   ? 30.69000 10.05500  -6.11300  1.000 39.86686 ?  376 HOH   A O     1 
HETATM 5472 O  O     . HOH   K 6 .   ? 23.42000 16.38200  -1.54900  1.000 43.19654 ?  377 HOH   A O     1 
HETATM 5473 O  O     . HOH   K 6 .   ? 2.81200  15.71100  7.97900   1.000 48.87346 ?  378 HOH   A O     1 
HETATM 5474 O  O     . HOH   K 6 .   ? 11.07200 -4.17200  9.16600   1.000 47.63417 ?  379 HOH   A O     1 
HETATM 5475 O  O     . HOH   K 6 .   ? 31.76600 18.55000  6.17600   1.000 41.03180 ?  380 HOH   A O     1 
HETATM 5476 O  O     . HOH   K 6 .   ? 38.81200 5.94000   10.53500  1.000 48.66392 ?  381 HOH   A O     1 
HETATM 5477 O  O     . HOH   K 6 .   ? 19.35900 21.98500  13.83000  1.000 24.38101 ?  382 HOH   A O     1 
HETATM 5478 O  O     . HOH   K 6 .   ? 9.37900  14.79000  17.95200  1.000 33.73085 ?  383 HOH   A O     1 
HETATM 5479 O  O     . HOH   K 6 .   ? 18.30800 19.81200  19.61600  1.000 35.00896 ?  384 HOH   A O     1 
HETATM 5480 O  O     . HOH   K 6 .   ? 34.17600 13.06800  10.05700  1.000 46.52834 ?  385 HOH   A O     1 
HETATM 5481 O  O     . HOH   K 6 .   ? 20.18700 14.95900  -3.40500  1.000 35.36246 ?  386 HOH   A O     1 
HETATM 5482 O  O     . HOH   K 6 .   ? 23.96600 -7.94500  12.77400  1.000 46.06647 ?  387 HOH   A O     1 
HETATM 5483 O  O     . HOH   K 6 .   ? 24.47500 13.31500  24.89200  1.000 42.78816 ?  388 HOH   A O     1 
HETATM 5484 O  O     . HOH   K 6 .   ? 29.04900 4.12900   25.41800  1.000 40.36841 ?  389 HOH   A O     1 
HETATM 5485 O  O     . HOH   K 6 .   ? 15.61200 -8.16800  17.52300  1.000 43.33785 ?  390 HOH   A O     1 
HETATM 5486 O  O     . HOH   K 6 .   ? 4.45300  9.15800   17.61700  1.000 27.62624 ?  391 HOH   A O     1 
HETATM 5487 O  O     . HOH   K 6 .   ? 25.81100 13.25700  -0.20100  1.000 38.52595 ?  392 HOH   A O     1 
HETATM 5488 O  O     . HOH   K 6 .   ? 4.71500  1.20300   13.56300  1.000 36.69680 ?  393 HOH   A O     1 
HETATM 5489 O  O     . HOH   K 6 .   ? 13.63200 13.78000  22.27500  1.000 38.66082 ?  394 HOH   A O     1 
HETATM 5490 O  O     . HOH   K 6 .   ? 16.69000 3.86700   26.46000  1.000 38.41252 ?  395 HOH   A O     1 
HETATM 5491 O  O     . HOH   K 6 .   ? 22.80100 10.64500  21.93500  1.000 28.88910 ?  396 HOH   A O     1 
HETATM 5492 O  O     . HOH   K 6 .   ? 34.87200 -0.09300  1.44500   1.000 47.04481 ?  397 HOH   A O     1 
HETATM 5493 O  O     . HOH   K 6 .   ? 15.30100 19.33200  18.70700  1.000 37.52403 ?  398 HOH   A O     1 
HETATM 5494 O  O     . HOH   K 6 .   ? 34.67300 7.79400   25.43600  1.000 39.92418 ?  399 HOH   A O     1 
HETATM 5495 O  O     . HOH   K 6 .   ? 33.16400 -8.68000  3.52400   1.000 47.47223 ?  400 HOH   A O     1 
HETATM 5496 O  O     . HOH   K 6 .   ? 29.53200 17.06500  15.52000  1.000 42.27784 ?  401 HOH   A O     1 
HETATM 5497 O  O     . HOH   K 6 .   ? 22.34000 14.31200  -4.99700  1.000 45.42012 ?  402 HOH   A O     1 
HETATM 5498 O  O     . HOH   K 6 .   ? 15.71600 23.12100  13.81300  1.000 44.12175 ?  403 HOH   A O     1 
HETATM 5499 O  O     . HOH   K 6 .   ? 5.10000  10.45200  13.96300  1.000 37.97527 ?  404 HOH   A O     1 
HETATM 5500 O  O     . HOH   K 6 .   ? 13.13200 2.31100   28.22900  1.000 41.02012 ?  405 HOH   A O     1 
HETATM 5501 O  O     . HOH   K 6 .   ? 32.58400 11.79500  -4.08200  1.000 42.83006 ?  406 HOH   A O     1 
HETATM 5502 O  O     . HOH   K 6 .   ? 17.44200 14.92300  -6.10300  1.000 48.79546 ?  407 HOH   A O     1 
HETATM 5503 O  O     . HOH   K 6 .   ? 27.40900 10.98600  -8.71900  1.000 44.23476 ?  408 HOH   A O     1 
HETATM 5504 O  O     . HOH   K 6 .   ? 6.28900  3.02700   4.02300   1.000 43.53390 ?  409 HOH   A O     1 
HETATM 5505 O  O     . HOH   K 6 .   ? 35.86700 23.95100  14.25300  1.000 47.40356 ?  410 HOH   A O     1 
HETATM 5506 O  O     . HOH   K 6 .   ? 38.33000 6.18800   15.16900  1.000 44.55132 ?  411 HOH   A O     1 
HETATM 5507 O  O     . HOH   K 6 .   ? 15.55300 9.77800   -10.66700 1.000 50.74413 ?  412 HOH   A O     1 
HETATM 5508 O  O     . HOH   K 6 .   ? 30.79700 16.25200  5.41900   1.000 33.98675 ?  413 HOH   A O     1 
HETATM 5509 O  O     . HOH   K 6 .   ? 15.37200 1.27900   -6.14900  1.000 53.52574 ?  414 HOH   A O     1 
HETATM 5510 O  O     . HOH   K 6 .   ? 6.87000  13.91600  16.81100  1.000 40.76404 ?  415 HOH   A O     1 
HETATM 5511 O  O     . HOH   K 6 .   ? 6.70700  11.31000  0.50300   1.000 39.87678 ?  416 HOH   A O     1 
HETATM 5512 O  O     . HOH   K 6 .   ? 20.72800 3.70500   -9.09700  1.000 52.81720 ?  417 HOH   A O     1 
HETATM 5513 O  O     . HOH   K 6 .   ? 26.71600 22.65100  4.87900   1.000 36.23949 ?  418 HOH   A O     1 
HETATM 5514 O  O     . HOH   K 6 .   ? 22.88300 15.91100  22.39100  1.000 46.70954 ?  419 HOH   A O     1 
HETATM 5515 O  O     . HOH   K 6 .   ? 12.98400 -10.23400 14.42700  1.000 49.12993 ?  420 HOH   A O     1 
HETATM 5516 O  O     . HOH   K 6 .   ? 9.85200  0.30000   1.02700   1.000 34.35522 ?  421 HOH   A O     1 
HETATM 5517 O  O     . HOH   K 6 .   ? 21.09300 3.75600   27.40500  1.000 44.16257 ?  422 HOH   A O     1 
HETATM 5518 O  O     . HOH   K 6 .   ? 21.34700 -5.92000  1.87400   1.000 49.92468 ?  423 HOH   A O     1 
HETATM 5519 O  O     . HOH   K 6 .   ? 30.88000 13.70100  1.02400   1.000 42.88881 ?  424 HOH   A O     1 
HETATM 5520 O  O     . HOH   K 6 .   ? 10.54800 0.66400   4.63700   1.000 31.09672 ?  425 HOH   A O     1 
HETATM 5521 O  O     . HOH   K 6 .   ? 13.56300 24.66800  6.67000   1.000 49.26444 ?  426 HOH   A O     1 
HETATM 5522 O  O     . HOH   K 6 .   ? 32.66900 14.85800  25.60500  1.000 45.81909 ?  427 HOH   A O     1 
HETATM 5523 O  O     . HOH   K 6 .   ? 3.91500  4.85200   12.07700  1.000 53.96032 ?  428 HOH   A O     1 
HETATM 5524 O  O     . HOH   K 6 .   ? 7.00100  -3.87800  12.23500  1.000 47.75978 ?  429 HOH   A O     1 
HETATM 5525 O  O     . HOH   K 6 .   ? 10.18600 -8.01600  21.27300  1.000 55.66682 ?  430 HOH   A O     1 
HETATM 5526 O  O     . HOH   K 6 .   ? 29.95000 -7.66300  17.22900  1.000 47.91791 ?  431 HOH   A O     1 
HETATM 5527 O  O     . HOH   K 6 .   ? 15.94300 -6.42800  24.54900  1.000 48.07387 ?  432 HOH   A O     1 
HETATM 5528 O  O     . HOH   K 6 .   ? 31.61500 15.66900  23.06700  1.000 45.08060 ?  433 HOH   A O     1 
HETATM 5529 O  O     . HOH   K 6 .   ? 25.35000 -4.97200  18.20900  1.000 42.18974 ?  434 HOH   A O     1 
HETATM 5530 O  O     . HOH   K 6 .   ? 37.39500 13.22400  13.93300  1.000 48.08837 ?  435 HOH   A O     1 
HETATM 5531 O  O     . HOH   K 6 .   ? 34.38200 -4.85600  2.32100   1.000 49.23165 ?  436 HOH   A O     1 
HETATM 5532 O  O     . HOH   K 6 .   ? 30.21800 15.74900  2.47800   1.000 48.57329 ?  437 HOH   A O     1 
HETATM 5533 O  O     . HOH   K 6 .   ? 34.08500 11.34700  8.20900   1.000 43.80183 ?  438 HOH   A O     1 
HETATM 5534 O  O     . HOH   K 6 .   ? 26.44900 -5.17300  15.73000  1.000 41.69108 ?  439 HOH   A O     1 
HETATM 5535 O  O     . HOH   K 6 .   ? 17.04900 -9.07700  13.12800  1.000 45.37267 ?  440 HOH   A O     1 
HETATM 5536 O  O     . HOH   K 6 .   ? 22.09600 14.41000  -7.86800  1.000 46.54666 ?  441 HOH   A O     1 
HETATM 5537 O  O     . HOH   K 6 .   ? 15.86900 19.07500  9.27400   1.000 39.13791 ?  442 HOH   A O     1 
HETATM 5538 O  O     . HOH   K 6 .   ? 26.42400 14.24400  -3.71500  1.000 49.05148 ?  443 HOH   A O     1 
HETATM 5539 O  O     . HOH   K 6 .   ? 12.64500 -9.82400  11.35600  1.000 50.35349 ?  444 HOH   A O     1 
HETATM 5540 O  O     . HOH   K 6 .   ? 12.14500 9.58400   -7.41300  1.000 47.77423 ?  445 HOH   A O     1 
HETATM 5541 O  O     . HOH   K 6 .   ? 10.15200 1.18800   31.49000  1.000 57.99754 ?  446 HOH   A O     1 
HETATM 5542 O  O     . HOH   K 6 .   ? 21.85700 20.40300  -1.27100  1.000 49.61609 ?  447 HOH   A O     1 
HETATM 5543 O  O     . HOH   K 6 .   ? 15.83000 19.26200  6.73200   1.000 40.43129 ?  448 HOH   A O     1 
HETATM 5544 O  O     . HOH   K 6 .   ? 15.64400 -9.83500  19.67500  1.000 46.47037 ?  449 HOH   A O     1 
HETATM 5545 O  O     . HOH   K 6 .   ? 14.03100 5.11600   28.99700  1.000 44.71599 ?  450 HOH   A O     1 
HETATM 5546 O  O     . HOH   K 6 .   ? 13.41400 19.02600  4.48600   1.000 46.98266 ?  451 HOH   A O     1 
HETATM 5547 O  O     . HOH   K 6 .   ? 19.04400 10.63600  24.47900  1.000 45.61537 ?  452 HOH   A O     1 
HETATM 5548 O  O     . HOH   K 6 .   ? 23.56500 -7.07000  2.76600   1.000 46.52702 ?  453 HOH   A O     1 
HETATM 5549 O  O     . HOH   K 6 .   ? 22.98600 -8.63500  7.25600   1.000 45.34452 ?  454 HOH   A O     1 
HETATM 5550 O  O     . HOH   K 6 .   ? 8.11000  16.25000  15.41200  1.000 45.32773 ?  455 HOH   A O     1 
HETATM 5551 O  O     . HOH   K 6 .   ? 20.61600 9.45700   22.23900  1.000 27.58995 ?  456 HOH   A O     1 
HETATM 5552 O  O     . HOH   K 6 .   ? 27.09700 -10.09200 8.62100   1.000 43.63746 ?  457 HOH   A O     1 
HETATM 5553 O  O     . HOH   K 6 .   ? 35.43900 23.83200  16.73200  1.000 42.11669 ?  458 HOH   A O     1 
HETATM 5554 O  O     . HOH   K 6 .   ? 22.63100 13.10600  23.05700  1.000 36.40494 ?  459 HOH   A O     1 
HETATM 5555 O  O     . HOH   K 6 .   ? 1.35300  15.84800  5.48600   1.000 44.21025 ?  460 HOH   A O     1 
HETATM 5556 O  O     . HOH   K 6 .   ? 15.47700 -9.75200  15.27000  1.000 49.53555 ?  461 HOH   A O     1 
HETATM 5557 O  O     . HOH   K 6 .   ? 20.20800 13.78200  23.56800  1.000 46.69251 ?  462 HOH   A O     1 
HETATM 5558 O  O     . HOH   K 6 .   ? 0.54300  1.22800   25.07700  1.000 41.02980 ?  463 HOH   A O     1 
HETATM 5559 O  O     . HOH   K 6 .   ? 16.06500 -12.27800 19.82400  1.000 51.14570 ?  464 HOH   A O     1 
HETATM 5560 O  O     . HOH   L 6 .   ? 62.59500 -16.70900 10.69800  1.000 51.35629 ?  301 HOH   B O     1 
HETATM 5561 O  O     . HOH   L 6 .   ? 62.15600 -15.67300 7.63900   1.000 53.36972 ?  302 HOH   B O     1 
HETATM 5562 O  O     . HOH   L 6 .   ? 45.11400 -37.40700 22.58400  1.000 49.24174 ?  303 HOH   B O     1 
HETATM 5563 O  O     . HOH   L 6 .   ? 60.65100 -4.31300  13.83500  1.000 51.50686 ?  304 HOH   B O     1 
HETATM 5564 O  O     . HOH   L 6 .   ? 56.25300 -26.60300 19.05000  1.000 50.51807 ?  305 HOH   B O     1 
HETATM 5565 O  O     . HOH   L 6 .   ? 54.88200 -19.63900 3.67700   1.000 52.17901 ?  306 HOH   B O     1 
HETATM 5566 O  O     . HOH   L 6 .   ? 55.79400 -16.38900 30.77300  1.000 33.39169 ?  307 HOH   B O     1 
HETATM 5567 O  O     . HOH   L 6 .   ? 31.65200 -11.53400 33.68700  1.000 40.51280 ?  308 HOH   B O     1 
HETATM 5568 O  O     . HOH   L 6 .   ? 46.28900 -18.33300 36.78600  1.000 41.66051 ?  309 HOH   B O     1 
HETATM 5569 O  O     . HOH   L 6 .   ? 32.06400 -9.54800  23.78800  1.000 37.98063 ?  310 HOH   B O     1 
HETATM 5570 O  O     . HOH   L 6 .   ? 62.72700 -12.95700 14.07600  1.000 46.10435 ?  311 HOH   B O     1 
HETATM 5571 O  O     . HOH   L 6 .   ? 36.25800 -20.76800 33.36900  1.000 34.66483 ?  312 HOH   B O     1 
HETATM 5572 O  O     . HOH   L 6 .   ? 47.79200 -9.61000  36.10600  1.000 28.76657 ?  313 HOH   B O     1 
HETATM 5573 O  O     . HOH   L 6 .   ? 60.28400 -23.23900 25.94800  1.000 26.95661 ?  314 HOH   B O     1 
HETATM 5574 O  O     . HOH   L 6 .   ? 59.62400 -17.48200 26.49500  1.000 29.09671 ?  315 HOH   B O     1 
HETATM 5575 O  O     . HOH   L 6 .   ? 42.17700 -26.66600 7.14500   1.000 49.35216 ?  316 HOH   B O     1 
HETATM 5576 O  O     . HOH   L 6 .   ? 42.90600 -33.97100 15.07100  1.000 48.02175 ?  317 HOH   B O     1 
HETATM 5577 O  O     . HOH   L 6 .   ? 28.35400 -12.32000 39.08600  1.000 47.28582 ?  318 HOH   B O     1 
HETATM 5578 O  O     . HOH   L 6 .   ? 50.07900 -25.14200 9.51600   1.000 48.99015 ?  319 HOH   B O     1 
HETATM 5579 O  O     . HOH   L 6 .   ? 61.29500 -14.00200 26.11600  1.000 40.73215 ?  320 HOH   B O     1 
HETATM 5580 O  O     . HOH   L 6 .   ? 35.70400 -5.51900  39.01800  1.000 38.78426 ?  321 HOH   B O     1 
HETATM 5581 O  O     . HOH   L 6 .   ? 55.90400 -19.39400 26.31000  1.000 24.98468 ?  322 HOH   B O     1 
HETATM 5582 O  O     . HOH   L 6 .   ? 37.90700 -24.65000 16.39900  1.000 46.65373 ?  323 HOH   B O     1 
HETATM 5583 O  O     . HOH   L 6 .   ? 39.82500 -19.80800 36.14600  1.000 39.72230 ?  324 HOH   B O     1 
HETATM 5584 O  O     . HOH   L 6 .   ? 31.78600 -18.92000 29.43800  1.000 43.73267 ?  325 HOH   B O     1 
HETATM 5585 O  O     . HOH   L 6 .   ? 62.38400 -29.84000 21.76100  1.000 46.00898 ?  326 HOH   B O     1 
HETATM 5586 O  O     . HOH   L 6 .   ? 61.79200 -19.93700 32.19100  1.000 39.68713 ?  327 HOH   B O     1 
HETATM 5587 O  O     . HOH   L 6 .   ? 60.61200 -15.57600 14.15000  1.000 43.86377 ?  328 HOH   B O     1 
HETATM 5588 O  O     . HOH   L 6 .   ? 57.16700 -12.01400 35.41100  1.000 46.22108 ?  329 HOH   B O     1 
HETATM 5589 O  O     . HOH   L 6 .   ? 50.32400 -15.72200 38.31700  1.000 31.12175 ?  330 HOH   B O     1 
HETATM 5590 O  O     . HOH   L 6 .   ? 59.36500 -17.90900 32.51000  1.000 45.75539 ?  331 HOH   B O     1 
HETATM 5591 O  O     . HOH   L 6 .   ? 55.50600 0.27900   28.50600  1.000 37.32255 ?  332 HOH   B O     1 
HETATM 5592 O  O     . HOH   L 6 .   ? 56.71200 -8.65000  26.09400  1.000 28.11738 ?  333 HOH   B O     1 
HETATM 5593 O  O     . HOH   L 6 .   ? 34.25300 -19.31700 30.78300  1.000 33.90025 ?  334 HOH   B O     1 
HETATM 5594 O  O     . HOH   L 6 .   ? 39.62100 -3.36200  27.74100  1.000 51.40103 ?  335 HOH   B O     1 
HETATM 5595 O  O     . HOH   L 6 .   ? 43.39600 -21.79900 36.43900  1.000 45.47801 ?  336 HOH   B O     1 
HETATM 5596 O  O     . HOH   L 6 .   ? 34.92600 -21.74500 7.12400   1.000 55.84949 ?  337 HOH   B O     1 
HETATM 5597 O  O     . HOH   L 6 .   ? 29.47000 -14.63400 30.94300  1.000 47.18085 ?  338 HOH   B O     1 
HETATM 5598 O  O     . HOH   L 6 .   ? 64.58800 -29.58000 28.04000  1.000 25.65328 ?  339 HOH   B O     1 
HETATM 5599 O  O     . HOH   L 6 .   ? 59.43900 -17.61000 30.05200  1.000 33.46746 ?  340 HOH   B O     1 
HETATM 5600 O  O     . HOH   L 6 .   ? 60.62800 -11.50100 24.89100  1.000 41.75674 ?  341 HOH   B O     1 
HETATM 5601 O  O     . HOH   L 6 .   ? 37.68900 -2.77800  26.45100  1.000 50.36698 ?  342 HOH   B O     1 
HETATM 5602 O  O     . HOH   L 6 .   ? 35.23900 -14.56300 39.27300  1.000 43.07056 ?  343 HOH   B O     1 
HETATM 5603 O  O     . HOH   L 6 .   ? 37.37400 -19.70500 17.18600  1.000 37.16806 ?  344 HOH   B O     1 
HETATM 5604 O  O     . HOH   L 6 .   ? 32.72400 -17.10200 37.72400  1.000 45.12432 ?  345 HOH   B O     1 
HETATM 5605 O  O     . HOH   L 6 .   ? 53.76500 -21.97100 16.02800  1.000 28.68785 ?  346 HOH   B O     1 
HETATM 5606 O  O     . HOH   L 6 .   ? 53.65500 -1.63000  26.27900  1.000 43.81379 ?  347 HOH   B O     1 
HETATM 5607 O  O     . HOH   L 6 .   ? 34.54200 -2.35200  27.54400  1.000 44.25301 ?  348 HOH   B O     1 
HETATM 5608 O  O     . HOH   L 6 .   ? 39.62500 -6.10600  20.73600  1.000 46.69518 ?  349 HOH   B O     1 
HETATM 5609 O  O     . HOH   L 6 .   ? 56.84100 -7.95800  6.85400   1.000 46.23686 ?  350 HOH   B O     1 
HETATM 5610 O  O     . HOH   L 6 .   ? 52.93100 -24.39100 22.92300  1.000 27.49431 ?  351 HOH   B O     1 
HETATM 5611 O  O     . HOH   L 6 .   ? 32.07800 -12.01900 30.37500  1.000 39.49677 ?  352 HOH   B O     1 
HETATM 5612 O  O     . HOH   L 6 .   ? 48.48700 -11.97200 0.95600   1.000 49.93265 ?  353 HOH   B O     1 
HETATM 5613 O  O     . HOH   L 6 .   ? 68.86400 -8.34500  31.86500  1.000 51.98190 ?  354 HOH   B O     1 
HETATM 5614 O  O     . HOH   L 6 .   ? 54.37400 -25.85900 28.93600  1.000 28.08238 ?  355 HOH   B O     1 
HETATM 5615 O  O     . HOH   L 6 .   ? 55.79500 -2.06200  33.17400  1.000 42.96849 ?  356 HOH   B O     1 
HETATM 5616 O  O     . HOH   L 6 .   ? 51.66000 2.33000   29.12800  1.000 46.65370 ?  357 HOH   B O     1 
HETATM 5617 O  O     . HOH   L 6 .   ? 60.73500 -18.98700 7.15800   1.000 43.66290 ?  358 HOH   B O     1 
HETATM 5618 O  O     . HOH   L 6 .   ? 58.56500 -10.99300 2.10900   1.000 45.93818 ?  359 HOH   B O     1 
HETATM 5619 O  O     . HOH   L 6 .   ? 38.69900 -26.13700 32.74600  1.000 45.59066 ?  360 HOH   B O     1 
HETATM 5620 O  O     . HOH   L 6 .   ? 44.42600 -21.07200 31.36300  1.000 27.18004 ?  361 HOH   B O     1 
HETATM 5621 O  O     . HOH   L 6 .   ? 59.52100 -17.94200 15.35600  1.000 44.42783 ?  362 HOH   B O     1 
HETATM 5622 O  O     . HOH   L 6 .   ? 36.12500 -3.81400  24.63100  1.000 42.78774 ?  363 HOH   B O     1 
HETATM 5623 O  O     . HOH   L 6 .   ? 63.40100 -8.32400  16.63300  1.000 51.29045 ?  364 HOH   B O     1 
HETATM 5624 O  O     . HOH   L 6 .   ? 31.14400 -16.64900 28.51600  1.000 47.18041 ?  365 HOH   B O     1 
HETATM 5625 O  O     . HOH   L 6 .   ? 60.97000 -27.56400 19.37700  1.000 41.05434 ?  366 HOH   B O     1 
HETATM 5626 O  O     . HOH   L 6 .   ? 40.14100 -3.97700  30.33100  1.000 49.49181 ?  367 HOH   B O     1 
HETATM 5627 O  O     . HOH   L 6 .   ? 56.56200 -35.83600 23.70500  1.000 48.48314 ?  368 HOH   B O     1 
HETATM 5628 O  O     . HOH   L 6 .   ? 43.74200 -5.30500  35.01300  1.000 38.90612 ?  369 HOH   B O     1 
HETATM 5629 O  O     . HOH   L 6 .   ? 39.11000 -6.37400  16.72200  1.000 42.24309 ?  370 HOH   B O     1 
HETATM 5630 O  O     . HOH   L 6 .   ? 48.04300 -7.30400  34.51800  1.000 27.94474 ?  371 HOH   B O     1 
HETATM 5631 O  O     . HOH   L 6 .   ? 54.06900 -27.04900 26.46700  1.000 38.54111 ?  372 HOH   B O     1 
HETATM 5632 O  O     . HOH   L 6 .   ? 54.12400 -15.80500 0.84700   1.000 52.97515 ?  373 HOH   B O     1 
HETATM 5633 O  O     . HOH   L 6 .   ? 45.07200 -25.40700 30.70100  1.000 30.91609 ?  374 HOH   B O     1 
HETATM 5634 O  O     . HOH   L 6 .   ? 59.25400 -9.43800  26.19200  1.000 34.63757 ?  375 HOH   B O     1 
HETATM 5635 O  O     . HOH   L 6 .   ? 46.99100 -21.46600 3.97100   1.000 46.24472 ?  376 HOH   B O     1 
HETATM 5636 O  O     . HOH   L 6 .   ? 30.31600 -6.38900  33.52800  1.000 41.78837 ?  377 HOH   B O     1 
HETATM 5637 O  O     . HOH   L 6 .   ? 33.61600 -18.50000 35.53600  1.000 37.92724 ?  378 HOH   B O     1 
HETATM 5638 O  O     . HOH   L 6 .   ? 45.68200 -28.81100 33.58000  1.000 42.16011 ?  379 HOH   B O     1 
HETATM 5639 O  O     . HOH   L 6 .   ? 50.48500 -3.85600  33.46900  1.000 40.72096 ?  380 HOH   B O     1 
HETATM 5640 O  O     . HOH   L 6 .   ? 54.95800 -29.32900 25.69000  1.000 44.48593 ?  381 HOH   B O     1 
HETATM 5641 O  O     . HOH   L 6 .   ? 33.71000 -37.37500 17.67400  1.000 48.76569 ?  382 HOH   B O     1 
HETATM 5642 O  O     . HOH   L 6 .   ? 51.16600 0.56500   26.55300  1.000 46.69380 ?  383 HOH   B O     1 
HETATM 5643 O  O     . HOH   L 6 .   ? 60.51300 -19.38400 4.19300   1.000 52.39239 ?  384 HOH   B O     1 
HETATM 5644 O  O     . HOH   L 6 .   ? 48.97800 -13.36000 37.85100  1.000 27.41979 ?  385 HOH   B O     1 
HETATM 5645 O  O     . HOH   L 6 .   ? 50.11100 -36.54800 22.93200  1.000 42.46430 ?  386 HOH   B O     1 
HETATM 5646 O  O     . HOH   L 6 .   ? 53.29500 -15.87600 36.93400  1.000 39.36650 ?  387 HOH   B O     1 
HETATM 5647 O  O     . HOH   L 6 .   ? 48.02400 -36.29100 29.37600  1.000 53.02612 ?  388 HOH   B O     1 
HETATM 5648 O  O     . HOH   L 6 .   ? 45.09400 -26.86100 7.72900   1.000 51.01757 ?  389 HOH   B O     1 
HETATM 5649 O  O     . HOH   L 6 .   ? 59.29700 -25.47800 18.22700  1.000 33.22801 ?  390 HOH   B O     1 
HETATM 5650 O  O     . HOH   L 6 .   ? 43.80100 -7.60800  37.31000  1.000 27.43442 ?  391 HOH   B O     1 
HETATM 5651 O  O     . HOH   L 6 .   ? 52.89000 -10.77600 36.27800  1.000 32.45209 ?  392 HOH   B O     1 
HETATM 5652 O  O     . HOH   L 6 .   ? 53.54600 -22.75800 36.53900  1.000 40.96395 ?  393 HOH   B O     1 
HETATM 5653 O  O     . HOH   L 6 .   ? 52.42300 -30.09400 30.90300  1.000 43.08482 ?  394 HOH   B O     1 
HETATM 5654 O  O     . HOH   L 6 .   ? 58.33500 -21.10200 33.17400  1.000 27.72696 ?  395 HOH   B O     1 
HETATM 5655 O  O     . HOH   L 6 .   ? 40.19900 -21.88000 3.24100   1.000 48.70217 ?  396 HOH   B O     1 
HETATM 5656 O  O     . HOH   L 6 .   ? 29.15000 -13.71400 35.27900  1.000 45.73604 ?  397 HOH   B O     1 
HETATM 5657 O  O     . HOH   L 6 .   ? 47.10800 -3.71400  21.99000  1.000 42.46881 ?  398 HOH   B O     1 
HETATM 5658 O  O     . HOH   L 6 .   ? 62.39300 -11.77000 17.03000  1.000 36.24765 ?  399 HOH   B O     1 
HETATM 5659 O  O     A HOH   L 6 .   ? 52.64000 -20.00400 37.32000  0.500 29.91566 ?  400 HOH   B O     1 
HETATM 5660 O  O     B HOH   L 6 .   ? 53.67400 -18.43000 36.70600  0.500 33.04636 ?  400 HOH   B O     1 
HETATM 5661 O  O     . HOH   L 6 .   ? 49.16500 -34.88700 33.97700  1.000 44.36200 ?  401 HOH   B O     1 
HETATM 5662 O  O     . HOH   L 6 .   ? 49.04900 -27.09000 33.40700  1.000 38.81672 ?  402 HOH   B O     1 
HETATM 5663 O  O     . HOH   L 6 .   ? 51.31000 -5.77600  9.21200   1.000 49.76895 ?  403 HOH   B O     1 
HETATM 5664 O  O     . HOH   L 6 .   ? 54.32100 -7.46600  8.04100   1.000 50.17335 ?  404 HOH   B O     1 
HETATM 5665 O  O     . HOH   L 6 .   ? 46.42200 -21.16200 34.01200  1.000 40.88812 ?  405 HOH   B O     1 
HETATM 5666 O  O     . HOH   L 6 .   ? 64.33800 -24.74900 21.92200  1.000 47.22360 ?  406 HOH   B O     1 
HETATM 5667 O  O     . HOH   L 6 .   ? 67.73800 -18.24800 25.49600  1.000 44.64288 ?  407 HOH   B O     1 
HETATM 5668 O  O     . HOH   L 6 .   ? 32.43400 -10.03800 40.50600  1.000 48.91891 ?  408 HOH   B O     1 
HETATM 5669 O  O     . HOH   L 6 .   ? 49.72000 -34.65900 29.24600  1.000 41.29903 ?  409 HOH   B O     1 
HETATM 5670 O  O     . HOH   L 6 .   ? 45.55300 -4.22900  20.32900  1.000 42.48331 ?  410 HOH   B O     1 
HETATM 5671 O  O     . HOH   L 6 .   ? 61.61600 -36.12100 25.47500  1.000 41.33190 ?  411 HOH   B O     1 
HETATM 5672 O  O     . HOH   L 6 .   ? 30.03400 -1.75200  26.26900  1.000 45.51546 ?  412 HOH   B O     1 
HETATM 5673 O  O     . HOH   L 6 .   ? 49.08900 -3.67400  30.93800  1.000 43.96606 ?  413 HOH   B O     1 
HETATM 5674 O  O     . HOH   L 6 .   ? 62.42000 -17.29500 13.51400  1.000 48.70799 ?  414 HOH   B O     1 
HETATM 5675 O  O     . HOH   L 6 .   ? 41.78000 -4.40400  21.86100  1.000 54.15724 ?  415 HOH   B O     1 
HETATM 5676 O  O     . HOH   L 6 .   ? 32.69600 -32.16900 16.30600  1.000 47.87229 ?  416 HOH   B O     1 
HETATM 5677 O  O     . HOH   L 6 .   ? 60.48900 -13.43300 2.07200   1.000 55.14050 ?  417 HOH   B O     1 
HETATM 5678 O  O     . HOH   L 6 .   ? 45.14500 -23.25100 4.12400   1.000 54.00890 ?  418 HOH   B O     1 
HETATM 5679 O  O     . HOH   L 6 .   ? 28.28000 -2.04200  28.74800  1.000 52.99295 ?  419 HOH   B O     1 
HETATM 5680 O  O     . HOH   L 6 .   ? 58.16500 -15.19100 30.32200  1.000 36.84946 ?  420 HOH   B O     1 
HETATM 5681 O  O     . HOH   L 6 .   ? 58.13300 -25.51700 6.63900   1.000 51.28486 ?  421 HOH   B O     1 
HETATM 5682 O  O     . HOH   L 6 .   ? 59.88900 -9.56300  30.76100  1.000 46.84140 ?  422 HOH   B O     1 
HETATM 5683 O  O     . HOH   L 6 .   ? 49.20400 1.90000   29.83700  1.000 45.31626 ?  423 HOH   B O     1 
HETATM 5684 O  O     . HOH   L 6 .   ? 59.82300 -10.20000 28.32000  1.000 48.54062 ?  424 HOH   B O     1 
HETATM 5685 O  O     . HOH   L 6 .   ? 44.82800 -29.68100 36.01000  1.000 42.95621 ?  425 HOH   B O     1 
HETATM 5686 O  O     . HOH   L 6 .   ? 43.71600 -23.41700 31.58100  1.000 34.98283 ?  426 HOH   B O     1 
HETATM 5687 O  O     . HOH   L 6 .   ? 50.77500 -1.27000  33.79100  1.000 38.41928 ?  427 HOH   B O     1 
HETATM 5688 O  O     . HOH   L 6 .   ? 56.18000 -12.75900 37.83600  1.000 45.37241 ?  428 HOH   B O     1 
HETATM 5689 O  O     . HOH   L 6 .   ? 58.16200 -2.81600  33.85400  1.000 50.52994 ?  429 HOH   B O     1 
HETATM 5690 O  O     . HOH   L 6 .   ? 62.71000 -4.04300  12.25000  1.000 47.75793 ?  430 HOH   B O     1 
HETATM 5691 O  O     . HOH   L 6 .   ? 59.62400 -13.75300 28.34600  1.000 45.58196 ?  431 HOH   B O     1 
HETATM 5692 O  O     . HOH   L 6 .   ? 39.75000 -24.05700 3.08500   1.000 53.96837 ?  432 HOH   B O     1 
HETATM 5693 O  O     . HOH   L 6 .   ? 58.81400 -13.57900 32.29700  1.000 44.59446 ?  433 HOH   B O     1 
HETATM 5694 O  O     . HOH   L 6 .   ? 43.15800 -23.22400 34.43700  1.000 44.37104 ?  434 HOH   B O     1 
HETATM 5695 O  O     . HOH   L 6 .   ? 46.70700 -24.41500 34.79300  1.000 45.77870 ?  435 HOH   B O     1 
HETATM 5696 O  O     . HOH   L 6 .   ? 48.91500 -25.36000 7.22200   1.000 46.46175 ?  436 HOH   B O     1 
HETATM 5697 O  O     . HOH   L 6 .   ? 46.57000 -26.21500 32.90400  1.000 39.02742 ?  437 HOH   B O     1 
HETATM 5698 O  O     . HOH   L 6 .   ? 55.54500 -14.76800 -1.77800  1.000 52.50880 ?  438 HOH   B O     1 
HETATM 5699 O  O     . HOH   L 6 .   ? 48.22000 -23.88300 4.99300   1.000 50.76344 ?  439 HOH   B O     1 
HETATM 5700 O  O     . HOH   M 6 .   ? 68.96200 -36.84600 51.91400  1.000 46.97570 ?  301 HOH   C O     1 
HETATM 5701 O  O     . HOH   M 6 .   ? 73.57500 -29.64800 21.77700  1.000 39.38447 ?  302 HOH   C O     1 
HETATM 5702 O  O     . HOH   M 6 .   ? 85.71300 -40.27800 33.14900  1.000 47.77457 ?  303 HOH   C O     1 
HETATM 5703 O  O     . HOH   M 6 .   ? 78.19200 -12.02000 38.66000  1.000 45.03503 ?  304 HOH   C O     1 
HETATM 5704 O  O     . HOH   M 6 .   ? 75.60300 -28.89700 26.07100  1.000 24.25703 ?  305 HOH   C O     1 
HETATM 5705 O  O     . HOH   M 6 .   ? 86.60300 -17.31100 36.26900  1.000 43.58358 ?  306 HOH   C O     1 
HETATM 5706 O  O     . HOH   M 6 .   ? 75.37300 -23.14300 29.25100  1.000 29.81403 ?  307 HOH   C O     1 
HETATM 5707 O  O     . HOH   M 6 .   ? 80.58200 -29.84200 18.40900  1.000 45.52473 ?  308 HOH   C O     1 
HETATM 5708 O  O     . HOH   M 6 .   ? 67.04200 -20.57000 32.04700  1.000 35.98319 ?  309 HOH   C O     1 
HETATM 5709 O  O     . HOH   M 6 .   ? 79.40700 -22.34200 19.64200  1.000 42.75194 ?  310 HOH   C O     1 
HETATM 5710 O  O     . HOH   M 6 .   ? 84.65300 -33.85000 48.06400  1.000 43.63027 ?  311 HOH   C O     1 
HETATM 5711 O  O     . HOH   M 6 .   ? 78.35500 -31.42900 52.36300  1.000 37.85822 ?  312 HOH   C O     1 
HETATM 5712 O  O     . HOH   M 6 .   ? 92.47000 -25.31000 45.73600  1.000 44.97225 ?  313 HOH   C O     1 
HETATM 5713 O  O     . HOH   M 6 .   ? 59.78900 -22.71400 50.96100  1.000 48.94231 ?  314 HOH   C O     1 
HETATM 5714 O  O     . HOH   M 6 .   ? 62.60100 -21.28200 34.74500  1.000 45.14471 ?  315 HOH   C O     1 
HETATM 5715 O  O     . HOH   M 6 .   ? 60.10300 -21.24600 35.20800  1.000 39.57293 ?  316 HOH   C O     1 
HETATM 5716 O  O     . HOH   M 6 .   ? 71.48000 -45.57900 35.28700  1.000 37.46656 ?  317 HOH   C O     1 
HETATM 5717 O  O     . HOH   M 6 .   ? 77.78600 -13.94700 40.44500  1.000 44.71044 ?  318 HOH   C O     1 
HETATM 5718 O  O     . HOH   M 6 .   ? 71.23700 -18.64200 37.64500  1.000 27.13437 ?  319 HOH   C O     1 
HETATM 5719 O  O     . HOH   M 6 .   ? 74.56700 -41.81500 37.76800  1.000 45.78561 ?  320 HOH   C O     1 
HETATM 5720 O  O     . HOH   M 6 .   ? 63.52900 -19.14200 40.84300  1.000 35.66972 ?  321 HOH   C O     1 
HETATM 5721 O  O     . HOH   M 6 .   ? 59.23000 -24.41700 47.15600  1.000 43.16299 ?  322 HOH   C O     1 
HETATM 5722 O  O     . HOH   M 6 .   ? 74.25000 -20.38500 39.93000  1.000 31.60816 ?  323 HOH   C O     1 
HETATM 5723 O  O     . HOH   M 6 .   ? 79.31000 -39.08300 49.31800  1.000 47.82504 ?  324 HOH   C O     1 
HETATM 5724 O  O     . HOH   M 6 .   ? 75.92000 -25.29800 15.20200  1.000 47.10164 ?  325 HOH   C O     1 
HETATM 5725 O  O     . HOH   M 6 .   ? 73.38700 -22.73300 58.68700  1.000 51.59540 ?  326 HOH   C O     1 
HETATM 5726 O  O     . HOH   M 6 .   ? 82.98600 -33.62000 19.00600  1.000 38.70732 ?  327 HOH   C O     1 
HETATM 5727 O  O     . HOH   M 6 .   ? 67.66200 -37.80200 44.00100  1.000 32.67944 ?  328 HOH   C O     1 
HETATM 5728 O  O     . HOH   M 6 .   ? 69.72800 -38.80100 45.30100  1.000 43.03054 ?  329 HOH   C O     1 
HETATM 5729 O  O     . HOH   M 6 .   ? 80.68900 -28.80800 25.45100  1.000 28.40999 ?  330 HOH   C O     1 
HETATM 5730 O  O     . HOH   M 6 .   ? 72.10100 -15.82500 39.46000  1.000 38.19407 ?  331 HOH   C O     1 
HETATM 5731 O  O     . HOH   M 6 .   ? 66.72600 -29.91400 26.18200  1.000 28.00560 ?  332 HOH   C O     1 
HETATM 5732 O  O     . HOH   M 6 .   ? 91.89400 -22.14200 30.95400  1.000 49.37014 ?  333 HOH   C O     1 
HETATM 5733 O  O     . HOH   M 6 .   ? 66.89200 -19.37900 43.93000  1.000 26.35491 ?  334 HOH   C O     1 
HETATM 5734 O  O     . HOH   M 6 .   ? 90.35800 -29.57400 31.37300  1.000 43.57585 ?  335 HOH   C O     1 
HETATM 5735 O  O     . HOH   M 6 .   ? 79.54800 -43.27500 28.61200  1.000 34.66016 ?  336 HOH   C O     1 
HETATM 5736 O  O     . HOH   M 6 .   ? 69.37500 -41.82600 26.21900  1.000 44.74815 ?  337 HOH   C O     1 
HETATM 5737 O  O     . HOH   M 6 .   ? 82.86500 -10.62600 38.45500  1.000 43.77994 ?  338 HOH   C O     1 
HETATM 5738 O  O     . HOH   M 6 .   ? 63.84200 -17.04600 44.74200  1.000 40.20586 ?  339 HOH   C O     1 
HETATM 5739 O  O     . HOH   M 6 .   ? 74.85600 -26.50600 23.28500  1.000 30.11137 ?  340 HOH   C O     1 
HETATM 5740 O  O     . HOH   M 6 .   ? 81.25200 -13.78800 40.93600  1.000 36.96325 ?  341 HOH   C O     1 
HETATM 5741 O  O     . HOH   M 6 .   ? 86.18500 -13.69600 40.23900  1.000 44.55831 ?  342 HOH   C O     1 
HETATM 5742 O  O     . HOH   M 6 .   ? 77.67800 -35.74500 27.12700  1.000 24.81841 ?  343 HOH   C O     1 
HETATM 5743 O  O     . HOH   M 6 .   ? 79.47100 -43.25700 25.17000  1.000 29.00650 ?  344 HOH   C O     1 
HETATM 5744 O  O     . HOH   M 6 .   ? 73.62300 -41.70900 40.06100  1.000 40.04487 ?  345 HOH   C O     1 
HETATM 5745 O  O     . HOH   M 6 .   ? 81.38200 -25.85800 31.34900  1.000 27.76939 ?  346 HOH   C O     1 
HETATM 5746 O  O     . HOH   M 6 .   ? 69.81800 -43.89400 38.00300  1.000 47.06092 ?  347 HOH   C O     1 
HETATM 5747 O  O     . HOH   M 6 .   ? 71.06000 -42.20400 30.27600  1.000 34.40262 ?  348 HOH   C O     1 
HETATM 5748 O  O     . HOH   M 6 .   ? 86.89500 -20.26200 47.23000  1.000 47.49028 ?  349 HOH   C O     1 
HETATM 5749 O  O     . HOH   M 6 .   ? 62.61500 -20.20500 37.25000  1.000 46.51173 ?  350 HOH   C O     1 
HETATM 5750 O  O     . HOH   M 6 .   ? 63.98200 -32.61900 49.62800  1.000 44.76604 ?  351 HOH   C O     1 
HETATM 5751 O  O     . HOH   M 6 .   ? 90.30900 -25.29800 27.73900  1.000 40.98835 ?  352 HOH   C O     1 
HETATM 5752 O  O     . HOH   M 6 .   ? 91.15700 -30.06500 41.89000  1.000 32.50816 ?  353 HOH   C O     1 
HETATM 5753 O  O     . HOH   M 6 .   ? 70.76200 -17.16800 49.48200  1.000 29.79790 ?  354 HOH   C O     1 
HETATM 5754 O  O     . HOH   M 6 .   ? 78.34400 -29.95900 17.24200  1.000 48.35580 ?  355 HOH   C O     1 
HETATM 5755 O  O     . HOH   M 6 .   ? 76.36300 -41.83800 21.80500  1.000 36.37533 ?  356 HOH   C O     1 
HETATM 5756 O  O     . HOH   M 6 .   ? 72.11600 -23.60800 17.73000  1.000 40.12113 ?  357 HOH   C O     1 
HETATM 5757 O  O     . HOH   M 6 .   ? 55.74700 -33.17100 35.76800  1.000 31.99603 ?  358 HOH   C O     1 
HETATM 5758 O  O     . HOH   M 6 .   ? 74.67700 -36.37700 26.68700  1.000 26.08130 ?  359 HOH   C O     1 
HETATM 5759 O  O     . HOH   M 6 .   ? 75.89500 -30.52100 18.69800  1.000 41.49938 ?  360 HOH   C O     1 
HETATM 5760 O  O     . HOH   M 6 .   ? 66.94600 -18.64500 55.46200  1.000 44.71779 ?  361 HOH   C O     1 
HETATM 5761 O  O     . HOH   M 6 .   ? 72.06900 -14.41800 43.31800  1.000 45.99916 ?  362 HOH   C O     1 
HETATM 5762 O  O     . HOH   M 6 .   ? 77.89600 -29.54800 54.01200  1.000 41.80402 ?  363 HOH   C O     1 
HETATM 5763 O  O     . HOH   M 6 .   ? 63.56900 -40.16400 36.13400  1.000 36.12516 ?  364 HOH   C O     1 
HETATM 5764 O  O     . HOH   M 6 .   ? 72.28400 -42.69800 25.65100  1.000 45.99978 ?  365 HOH   C O     1 
HETATM 5765 O  O     . HOH   M 6 .   ? 58.21700 -21.83300 44.41800  1.000 36.25627 ?  366 HOH   C O     1 
HETATM 5766 O  O     . HOH   M 6 .   ? 83.50100 -17.66500 40.97800  1.000 31.91786 ?  367 HOH   C O     1 
HETATM 5767 O  O     . HOH   M 6 .   ? 77.79900 -40.13600 33.00700  1.000 31.08649 ?  368 HOH   C O     1 
HETATM 5768 O  O     . HOH   M 6 .   ? 77.05500 -22.81800 52.82800  1.000 33.80371 ?  369 HOH   C O     1 
HETATM 5769 O  O     . HOH   M 6 .   ? 55.84000 -22.10100 40.49100  1.000 39.24091 ?  370 HOH   C O     1 
HETATM 5770 O  O     . HOH   M 6 .   ? 85.71900 -29.47900 51.11700  1.000 42.20794 ?  371 HOH   C O     1 
HETATM 5771 O  O     . HOH   M 6 .   ? 89.59100 -22.02100 44.47100  1.000 42.51473 ?  372 HOH   C O     1 
HETATM 5772 O  O     . HOH   M 6 .   ? 54.20400 -31.47800 32.23600  1.000 36.96917 ?  373 HOH   C O     1 
HETATM 5773 O  O     . HOH   M 6 .   ? 85.27300 -28.85100 21.22000  1.000 46.11644 ?  374 HOH   C O     1 
HETATM 5774 O  O     . HOH   M 6 .   ? 93.37600 -28.00900 37.94700  1.000 44.64982 ?  375 HOH   C O     1 
HETATM 5775 O  O     . HOH   M 6 .   ? 74.96700 -19.68600 29.79400  1.000 33.31456 ?  376 HOH   C O     1 
HETATM 5776 O  O     . HOH   M 6 .   ? 90.36100 -28.68400 33.90500  1.000 39.38240 ?  377 HOH   C O     1 
HETATM 5777 O  O     . HOH   M 6 .   ? 76.93900 -38.48500 41.74600  1.000 33.83363 ?  378 HOH   C O     1 
HETATM 5778 O  O     . HOH   M 6 .   ? 81.79600 -16.97100 21.75700  1.000 54.03378 ?  379 HOH   C O     1 
HETATM 5779 O  O     . HOH   M 6 .   ? 77.93600 -36.07400 51.53400  1.000 36.29520 ?  380 HOH   C O     1 
HETATM 5780 O  O     . HOH   M 6 .   ? 93.44800 -31.73300 38.90200  1.000 50.78755 ?  381 HOH   C O     1 
HETATM 5781 O  O     . HOH   M 6 .   ? 80.42700 -36.11800 27.54600  1.000 26.60112 ?  382 HOH   C O     1 
HETATM 5782 O  O     . HOH   M 6 .   ? 80.22800 -33.18400 19.86800  1.000 42.69466 ?  383 HOH   C O     1 
HETATM 5783 O  O     . HOH   M 6 .   ? 54.69600 -26.91300 42.32400  1.000 28.52654 ?  384 HOH   C O     1 
HETATM 5784 O  O     . HOH   M 6 .   ? 79.55500 -19.06000 19.86600  1.000 54.50559 ?  385 HOH   C O     1 
HETATM 5785 O  O     . HOH   M 6 .   ? 91.01600 -38.50900 37.78600  1.000 43.02094 ?  386 HOH   C O     1 
HETATM 5786 O  O     . HOH   M 6 .   ? 77.10700 -37.29500 47.99800  1.000 31.60907 ?  387 HOH   C O     1 
HETATM 5787 O  O     . HOH   M 6 .   ? 84.75900 -30.79600 20.13400  1.000 45.97862 ?  388 HOH   C O     1 
HETATM 5788 O  O     . HOH   M 6 .   ? 62.08100 -37.74300 36.09400  1.000 35.41049 ?  389 HOH   C O     1 
HETATM 5789 O  O     . HOH   M 6 .   ? 76.00500 -21.72000 17.85900  1.000 48.78270 ?  390 HOH   C O     1 
HETATM 5790 O  O     . HOH   M 6 .   ? 91.17800 -35.38400 27.94600  1.000 44.31455 ?  391 HOH   C O     1 
HETATM 5791 O  O     . HOH   M 6 .   ? 70.66400 -38.03900 34.95700  1.000 27.33095 ?  392 HOH   C O     1 
HETATM 5792 O  O     . HOH   M 6 .   ? 85.10400 -18.18100 43.35900  1.000 40.18603 ?  393 HOH   C O     1 
HETATM 5793 O  O     . HOH   M 6 .   ? 72.87300 -17.08300 27.51500  1.000 49.55376 ?  394 HOH   C O     1 
HETATM 5794 O  O     . HOH   M 6 .   ? 67.41400 -15.26200 39.19000  1.000 45.00391 ?  395 HOH   C O     1 
HETATM 5795 O  O     . HOH   M 6 .   ? 72.03000 -31.36600 20.26600  1.000 43.09255 ?  396 HOH   C O     1 
HETATM 5796 O  O     . HOH   M 6 .   ? 54.72400 -23.77100 39.05000  1.000 40.86173 ?  397 HOH   C O     1 
HETATM 5797 O  O     . HOH   M 6 .   ? 74.04800 -20.38900 27.34300  1.000 43.32285 ?  398 HOH   C O     1 
HETATM 5798 O  O     . HOH   M 6 .   ? 80.95200 -12.67400 38.33500  1.000 45.76583 ?  399 HOH   C O     1 
HETATM 5799 O  O     . HOH   M 6 .   ? 78.05200 -42.48400 31.04400  1.000 24.73292 ?  400 HOH   C O     1 
HETATM 5800 O  O     . HOH   M 6 .   ? 70.98900 -13.21300 46.79500  1.000 51.74102 ?  401 HOH   C O     1 
HETATM 5801 O  O     . HOH   M 6 .   ? 69.84700 -16.16400 37.62400  1.000 42.63038 ?  402 HOH   C O     1 
HETATM 5802 O  O     . HOH   M 6 .   ? 75.68600 -16.37700 52.24400  1.000 46.75860 ?  403 HOH   C O     1 
HETATM 5803 O  O     . HOH   M 6 .   ? 87.50200 -33.46200 46.98700  1.000 51.52963 ?  404 HOH   C O     1 
HETATM 5804 O  O     . HOH   M 6 .   ? 67.21000 -41.03200 24.87900  1.000 45.55594 ?  405 HOH   C O     1 
HETATM 5805 O  O     A HOH   M 6 .   ? 70.68100 -22.49600 58.24500  0.500 35.32001 ?  406 HOH   C O     1 
HETATM 5806 O  O     B HOH   M 6 .   ? 70.55600 -20.89300 59.38700  0.500 35.84630 ?  406 HOH   C O     1 
HETATM 5807 O  O     . HOH   M 6 .   ? 90.56000 -27.85900 27.20500  1.000 47.44101 ?  407 HOH   C O     1 
HETATM 5808 O  O     . HOH   M 6 .   ? 76.52700 -17.77900 53.76300  1.000 41.69819 ?  408 HOH   C O     1 
HETATM 5809 O  O     . HOH   M 6 .   ? 77.94700 -24.72600 53.93800  1.000 46.74881 ?  409 HOH   C O     1 
HETATM 5810 O  O     . HOH   M 6 .   ? 74.22400 -44.70200 37.15000  1.000 40.08674 ?  410 HOH   C O     1 
HETATM 5811 O  O     . HOH   M 6 .   ? 66.03000 -36.82400 45.93100  1.000 43.43237 ?  411 HOH   C O     1 
HETATM 5812 O  O     . HOH   M 6 .   ? 77.46900 -43.68000 23.14000  1.000 31.86664 ?  412 HOH   C O     1 
HETATM 5813 O  O     . HOH   M 6 .   ? 83.95800 -15.30300 40.79600  1.000 35.73740 ?  413 HOH   C O     1 
HETATM 5814 O  O     . HOH   M 6 .   ? 78.88800 -34.21400 52.90300  1.000 35.60196 ?  414 HOH   C O     1 
HETATM 5815 O  O     . HOH   M 6 .   ? 79.94900 -12.99200 45.96100  1.000 47.27126 ?  415 HOH   C O     1 
HETATM 5816 O  O     . HOH   M 6 .   ? 56.40800 -23.40900 45.58800  1.000 45.55941 ?  416 HOH   C O     1 
HETATM 5817 O  O     . HOH   M 6 .   ? 53.87300 -34.01100 32.08000  1.000 43.28528 ?  417 HOH   C O     1 
HETATM 5818 O  O     . HOH   M 6 .   ? 91.81700 -27.40600 29.10300  1.000 50.66167 ?  418 HOH   C O     1 
HETATM 5819 O  O     . HOH   M 6 .   ? 76.15100 -23.13200 16.00300  1.000 54.73357 ?  419 HOH   C O     1 
HETATM 5820 O  O     . HOH   M 6 .   ? 72.11700 -39.79800 45.07200  1.000 48.60552 ?  420 HOH   C O     1 
HETATM 5821 O  O     . HOH   M 6 .   ? 48.36400 -27.61100 36.26200  1.000 44.88168 ?  421 HOH   C O     1 
HETATM 5822 O  O     . HOH   M 6 .   ? 94.77300 -26.32200 36.61000  1.000 53.39919 ?  422 HOH   C O     1 
HETATM 5823 O  O     . HOH   M 6 .   ? 65.38900 -15.92000 38.41100  1.000 51.89383 ?  423 HOH   C O     1 
HETATM 5824 O  O     . HOH   M 6 .   ? 77.44000 -25.59600 56.53200  1.000 46.23537 ?  424 HOH   C O     1 
HETATM 5825 O  O     . HOH   M 6 .   ? 60.47200 -36.65500 27.83300  1.000 47.46301 ?  425 HOH   C O     1 
HETATM 5826 O  O     . HOH   M 6 .   ? 92.33900 -29.49100 35.44500  1.000 46.44340 ?  426 HOH   C O     1 
HETATM 5827 O  O     . HOH   M 6 .   ? 75.45300 -45.10600 23.82600  1.000 39.50673 ?  427 HOH   C O     1 
HETATM 5828 O  O     . HOH   M 6 .   ? 78.44900 -32.95600 17.93200  1.000 48.82947 ?  428 HOH   C O     1 
HETATM 5829 O  O     . HOH   M 6 .   ? 86.18000 -44.03200 27.14200  1.000 46.96983 ?  429 HOH   C O     1 
HETATM 5830 O  O     . HOH   M 6 .   ? 72.59000 -44.57600 30.41500  1.000 49.41593 ?  430 HOH   C O     1 
HETATM 5831 O  O     . HOH   M 6 .   ? 77.87800 -20.33600 53.33700  1.000 39.87537 ?  431 HOH   C O     1 
HETATM 5832 O  O     . HOH   M 6 .   ? 75.62800 -33.83600 18.06500  1.000 48.53211 ?  432 HOH   C O     1 
HETATM 5833 O  O     . HOH   M 6 .   ? 77.71000 -40.71300 51.02600  1.000 49.90719 ?  433 HOH   C O     1 
HETATM 5834 O  O     . HOH   M 6 .   ? 67.19200 -20.37100 24.97900  1.000 41.94615 ?  434 HOH   C O     1 
HETATM 5835 O  O     . HOH   M 6 .   ? 55.48800 -23.08200 47.74900  1.000 48.62199 ?  435 HOH   C O     1 
HETATM 5836 O  O     . HOH   M 6 .   ? 73.45500 -44.54600 21.99100  1.000 46.61057 ?  436 HOH   C O     1 
HETATM 5837 O  O     . HOH   M 6 .   ? 83.46300 -44.51800 27.45600  1.000 44.76410 ?  437 HOH   C O     1 
HETATM 5838 O  O     . HOH   M 6 .   ? 74.99400 -34.68200 15.37100  1.000 47.05160 ?  438 HOH   C O     1 
HETATM 5839 O  O     . HOH   N 6 .   ? 16.66300 27.76400  13.31600  1.000 35.00425 ?  301 HOH   D O     1 
HETATM 5840 O  O     . HOH   N 6 .   ? 31.82600 33.52600  3.32100   1.000 25.74635 ?  302 HOH   D O     1 
HETATM 5841 O  O     . HOH   N 6 .   ? 36.61400 31.47200  21.42400  1.000 46.27187 ?  303 HOH   D O     1 
HETATM 5842 O  O     . HOH   N 6 .   ? 15.99400 31.08800  -2.93100  1.000 43.03829 ?  304 HOH   D O     1 
HETATM 5843 O  O     . HOH   N 6 .   ? 36.35400 42.29300  18.07100  1.000 40.42330 ?  305 HOH   D O     1 
HETATM 5844 O  O     . HOH   N 6 .   ? 23.65400 29.06000  -7.99400  1.000 39.61670 ?  306 HOH   D O     1 
HETATM 5845 O  O     . HOH   N 6 .   ? 25.22600 33.95700  2.62000   1.000 19.80254 ?  307 HOH   D O     1 
HETATM 5846 O  O     . HOH   N 6 .   ? 14.80100 51.53900  3.57700   1.000 49.94906 ?  308 HOH   D O     1 
HETATM 5847 O  O     . HOH   N 6 .   ? 19.01400 30.50100  -2.31500  1.000 39.73176 ?  309 HOH   D O     1 
HETATM 5848 O  O     . HOH   N 6 .   ? 19.99000 50.52300  22.23000  1.000 26.29999 ?  310 HOH   D O     1 
HETATM 5849 O  O     A HOH   N 6 .   ? 18.59100 24.40400  14.14700  0.500 30.66001 ?  311 HOH   D O     1 
HETATM 5850 O  O     B HOH   N 6 .   ? 19.16400 26.24200  13.76100  0.500 23.01355 ?  311 HOH   D O     1 
HETATM 5851 O  O     . HOH   N 6 .   ? 8.61800  40.06900  14.44300  1.000 30.43518 ?  312 HOH   D O     1 
HETATM 5852 O  O     . HOH   N 6 .   ? 20.75600 28.85800  -0.15300  1.000 46.48849 ?  313 HOH   D O     1 
HETATM 5853 O  O     . HOH   N 6 .   ? 34.42400 29.64800  2.47500   1.000 31.50680 ?  314 HOH   D O     1 
HETATM 5854 O  O     . HOH   N 6 .   ? 22.92400 44.86300  27.44700  1.000 41.73916 ?  315 HOH   D O     1 
HETATM 5855 O  O     . HOH   N 6 .   ? 13.97700 42.89100  -8.35800  1.000 51.01681 ?  316 HOH   D O     1 
HETATM 5856 O  O     . HOH   N 6 .   ? 42.98900 40.86300  10.02800  1.000 45.98896 ?  317 HOH   D O     1 
HETATM 5857 O  O     . HOH   N 6 .   ? 19.36600 55.67900  13.51800  1.000 44.65542 ?  318 HOH   D O     1 
HETATM 5858 O  O     . HOH   N 6 .   ? 18.52600 45.07000  -3.14600  1.000 28.49816 ?  319 HOH   D O     1 
HETATM 5859 O  O     . HOH   N 6 .   ? 32.31800 27.57800  5.37700   1.000 38.24932 ?  320 HOH   D O     1 
HETATM 5860 O  O     . HOH   N 6 .   ? 11.71700 50.51900  3.96400   1.000 51.73922 ?  321 HOH   D O     1 
HETATM 5861 O  O     . HOH   N 6 .   ? 28.26100 35.20000  -8.69000  1.000 42.51011 ?  322 HOH   D O     1 
HETATM 5862 O  O     . HOH   N 6 .   ? 11.68800 52.07800  10.56600  1.000 44.30928 ?  323 HOH   D O     1 
HETATM 5863 O  O     . HOH   N 6 .   ? 33.58300 38.23200  -4.07500  1.000 40.10047 ?  324 HOH   D O     1 
HETATM 5864 O  O     . HOH   N 6 .   ? 11.31500 38.79300  0.76500   1.000 37.39555 ?  325 HOH   D O     1 
HETATM 5865 O  O     . HOH   N 6 .   ? 8.67600  44.87200  7.38500   1.000 42.11688 ?  326 HOH   D O     1 
HETATM 5866 O  O     . HOH   N 6 .   ? 41.96300 33.57200  8.20600   1.000 44.32604 ?  327 HOH   D O     1 
HETATM 5867 O  O     . HOH   N 6 .   ? 16.03600 31.81600  26.67300  1.000 26.04553 ?  328 HOH   D O     1 
HETATM 5868 O  O     . HOH   N 6 .   ? 13.30300 38.59000  -6.29200  1.000 44.55833 ?  329 HOH   D O     1 
HETATM 5869 O  O     . HOH   N 6 .   ? 31.89100 48.48700  -1.46800  1.000 33.95859 ?  330 HOH   D O     1 
HETATM 5870 O  O     . HOH   N 6 .   ? 22.61200 38.42400  26.01900  1.000 45.48452 ?  331 HOH   D O     1 
HETATM 5871 O  O     . HOH   N 6 .   ? 39.72400 35.62200  15.26300  1.000 34.83559 ?  332 HOH   D O     1 
HETATM 5872 O  O     . HOH   N 6 .   ? 36.91700 39.32900  21.77000  1.000 43.17420 ?  333 HOH   D O     1 
HETATM 5873 O  O     . HOH   N 6 .   ? 10.47000 33.46900  24.45100  1.000 30.82128 ?  334 HOH   D O     1 
HETATM 5874 O  O     . HOH   N 6 .   ? 31.91500 54.78100  8.35700   1.000 42.51294 ?  335 HOH   D O     1 
HETATM 5875 O  O     . HOH   N 6 .   ? 31.21700 30.79100  22.59400  1.000 41.38002 ?  336 HOH   D O     1 
HETATM 5876 O  O     . HOH   N 6 .   ? 31.26000 30.94800  0.72100   1.000 22.51223 ?  337 HOH   D O     1 
HETATM 5877 O  O     . HOH   N 6 .   ? 42.50800 33.01400  12.51700  1.000 47.08790 ?  338 HOH   D O     1 
HETATM 5878 O  O     . HOH   N 6 .   ? 26.16100 55.12900  4.62800   1.000 31.23614 ?  339 HOH   D O     1 
HETATM 5879 O  O     . HOH   N 6 .   ? 16.89400 38.38100  8.36900   1.000 30.07469 ?  340 HOH   D O     1 
HETATM 5880 O  O     . HOH   N 6 .   ? 19.22500 50.93100  19.58600  1.000 35.21636 ?  341 HOH   D O     1 
HETATM 5881 O  O     . HOH   N 6 .   ? 14.09000 30.71500  23.48700  1.000 24.94248 ?  342 HOH   D O     1 
HETATM 5882 O  O     . HOH   N 6 .   ? 28.63600 24.13900  -1.34600  1.000 48.09669 ?  343 HOH   D O     1 
HETATM 5883 O  O     . HOH   N 6 .   ? 37.76100 49.22900  -1.15900  1.000 46.28303 ?  344 HOH   D O     1 
HETATM 5884 O  O     . HOH   N 6 .   ? 20.47600 28.42700  7.84700   1.000 25.32101 ?  345 HOH   D O     1 
HETATM 5885 O  O     . HOH   N 6 .   ? 13.83200 29.95200  14.27100  1.000 27.39751 ?  346 HOH   D O     1 
HETATM 5886 O  O     . HOH   N 6 .   ? 27.20600 40.59000  1.63200   1.000 26.58679 ?  347 HOH   D O     1 
HETATM 5887 O  O     . HOH   N 6 .   ? 18.09400 24.36200  -0.79000  1.000 41.32184 ?  348 HOH   D O     1 
HETATM 5888 O  O     . HOH   N 6 .   ? 24.64300 43.65700  -9.06000  1.000 44.59820 ?  349 HOH   D O     1 
HETATM 5889 O  O     . HOH   N 6 .   ? 34.33500 42.61000  19.63500  1.000 37.39133 ?  350 HOH   D O     1 
HETATM 5890 O  O     . HOH   N 6 .   ? 16.37700 34.28000  7.73700   1.000 23.67095 ?  351 HOH   D O     1 
HETATM 5891 O  O     . HOH   N 6 .   ? 12.90900 34.29000  14.54200  1.000 25.54833 ?  352 HOH   D O     1 
HETATM 5892 O  O     . HOH   N 6 .   ? 29.80600 31.51000  -6.24600  1.000 36.60031 ?  353 HOH   D O     1 
HETATM 5893 O  O     . HOH   N 6 .   ? 20.17400 53.37600  -2.70500  1.000 43.14576 ?  354 HOH   D O     1 
HETATM 5894 O  O     . HOH   N 6 .   ? 37.12700 37.50600  6.37000   1.000 22.49450 ?  355 HOH   D O     1 
HETATM 5895 O  O     . HOH   N 6 .   ? 45.52300 35.52000  8.29200   1.000 41.81425 ?  356 HOH   D O     1 
HETATM 5896 O  O     . HOH   N 6 .   ? 10.12700 31.75500  15.65000  1.000 30.22615 ?  357 HOH   D O     1 
HETATM 5897 O  O     . HOH   N 6 .   ? 31.49600 24.97800  -2.51700  1.000 41.77192 ?  358 HOH   D O     1 
HETATM 5898 O  O     . HOH   N 6 .   ? 20.44300 37.65700  -7.85100  1.000 35.97448 ?  359 HOH   D O     1 
HETATM 5899 O  O     . HOH   N 6 .   ? 29.10400 49.71700  -0.52300  1.000 35.06471 ?  360 HOH   D O     1 
HETATM 5900 O  O     . HOH   N 6 .   ? 27.80000 39.46800  23.58200  1.000 44.73973 ?  361 HOH   D O     1 
HETATM 5901 O  O     . HOH   N 6 .   ? 15.37400 40.51800  25.68800  1.000 29.23348 ?  362 HOH   D O     1 
HETATM 5902 O  O     . HOH   N 6 .   ? 27.45700 24.77900  23.14500  1.000 31.23549 ?  363 HOH   D O     1 
HETATM 5903 O  O     . HOH   N 6 .   ? 13.67900 28.27400  21.27800  1.000 28.91407 ?  364 HOH   D O     1 
HETATM 5904 O  O     . HOH   N 6 .   ? 30.12800 37.21600  -8.77800  1.000 43.10622 ?  365 HOH   D O     1 
HETATM 5905 O  O     . HOH   N 6 .   ? 37.51000 34.81300  8.19200   1.000 25.40248 ?  366 HOH   D O     1 
HETATM 5906 O  O     . HOH   N 6 .   ? 20.53700 44.01300  26.27200  1.000 26.49204 ?  367 HOH   D O     1 
HETATM 5907 O  O     . HOH   N 6 .   ? 28.62200 41.99200  23.83900  1.000 41.05462 ?  368 HOH   D O     1 
HETATM 5908 O  O     . HOH   N 6 .   ? 29.97300 45.48400  -6.26000  1.000 34.93296 ?  369 HOH   D O     1 
HETATM 5909 O  O     . HOH   N 6 .   ? 31.10000 26.80800  9.00500   1.000 28.04440 ?  370 HOH   D O     1 
HETATM 5910 O  O     . HOH   N 6 .   ? 37.59300 40.10500  5.19400   1.000 24.89061 ?  371 HOH   D O     1 
HETATM 5911 O  O     . HOH   N 6 .   ? 37.66100 41.84700  12.46400  1.000 37.43957 ?  372 HOH   D O     1 
HETATM 5912 O  O     . HOH   N 6 .   ? 21.37500 54.40600  -0.49800  1.000 47.63366 ?  373 HOH   D O     1 
HETATM 5913 O  O     . HOH   N 6 .   ? 12.21300 42.76900  1.27900   1.000 34.33443 ?  374 HOH   D O     1 
HETATM 5914 O  O     . HOH   N 6 .   ? 10.76500 39.71900  3.45300   1.000 42.02975 ?  375 HOH   D O     1 
HETATM 5915 O  O     . HOH   N 6 .   ? 18.91900 37.95500  25.82200  1.000 27.20560 ?  376 HOH   D O     1 
HETATM 5916 O  O     . HOH   N 6 .   ? 41.24800 44.21000  0.41600   1.000 36.89953 ?  377 HOH   D O     1 
HETATM 5917 O  O     . HOH   N 6 .   ? 30.97400 45.74700  17.40800  1.000 33.00914 ?  378 HOH   D O     1 
HETATM 5918 O  O     . HOH   N 6 .   ? 27.52700 38.81900  -11.31800 1.000 35.23805 ?  379 HOH   D O     1 
HETATM 5919 O  O     . HOH   N 6 .   ? 25.04500 31.59900  -8.22600  1.000 29.59830 ?  380 HOH   D O     1 
HETATM 5920 O  O     . HOH   N 6 .   ? 18.05300 53.41600  2.72200   1.000 34.04276 ?  381 HOH   D O     1 
HETATM 5921 O  O     . HOH   N 6 .   ? 22.38500 31.74900  -2.16700  1.000 38.14048 ?  382 HOH   D O     1 
HETATM 5922 O  O     . HOH   N 6 .   ? 27.92400 20.57800  20.90400  1.000 45.94085 ?  383 HOH   D O     1 
HETATM 5923 O  O     . HOH   N 6 .   ? 14.31900 53.31800  15.08600  1.000 45.45838 ?  384 HOH   D O     1 
HETATM 5924 O  O     . HOH   N 6 .   ? 12.95600 35.31100  6.75300   1.000 33.78176 ?  385 HOH   D O     1 
HETATM 5925 O  O     . HOH   N 6 .   ? 32.60200 37.28100  -0.17600  1.000 22.83240 ?  386 HOH   D O     1 
HETATM 5926 O  O     . HOH   N 6 .   ? 34.44500 36.56900  23.13400  1.000 40.66471 ?  387 HOH   D O     1 
HETATM 5927 O  O     . HOH   N 6 .   ? 34.49600 54.43400  9.15100   1.000 48.21805 ?  388 HOH   D O     1 
HETATM 5928 O  O     . HOH   N 6 .   ? 22.74800 32.98000  -10.23200 1.000 30.06023 ?  389 HOH   D O     1 
HETATM 5929 O  O     . HOH   N 6 .   ? 25.83400 38.64200  24.93500  1.000 44.74567 ?  390 HOH   D O     1 
HETATM 5930 O  O     . HOH   N 6 .   ? 27.28100 53.95300  -0.15400  1.000 44.34029 ?  391 HOH   D O     1 
HETATM 5931 O  O     . HOH   N 6 .   ? 15.44400 45.47500  2.26500   1.000 27.30077 ?  392 HOH   D O     1 
HETATM 5932 O  O     . HOH   N 6 .   ? 18.31200 25.54800  24.63700  1.000 27.32726 ?  393 HOH   D O     1 
HETATM 5933 O  O     . HOH   N 6 .   ? 11.91200 48.28900  15.64100  1.000 37.63741 ?  394 HOH   D O     1 
HETATM 5934 O  O     . HOH   N 6 .   ? 37.14900 30.60300  -1.27000  1.000 36.56651 ?  395 HOH   D O     1 
HETATM 5935 O  O     . HOH   N 6 .   ? 30.44700 27.64000  -5.63500  1.000 46.93893 ?  396 HOH   D O     1 
HETATM 5936 O  O     . HOH   N 6 .   ? 40.10000 41.39000  -1.88700  1.000 33.00026 ?  397 HOH   D O     1 
HETATM 5937 O  O     . HOH   N 6 .   ? 24.55800 51.78500  21.01000  1.000 37.68633 ?  398 HOH   D O     1 
HETATM 5938 O  O     . HOH   N 6 .   ? 22.08000 33.05200  1.52300   1.000 25.54054 ?  399 HOH   D O     1 
HETATM 5939 O  O     . HOH   N 6 .   ? 40.59200 41.15600  11.96900  1.000 28.77632 ?  400 HOH   D O     1 
HETATM 5940 O  O     . HOH   N 6 .   ? 40.26000 38.20100  19.40200  1.000 44.40080 ?  401 HOH   D O     1 
HETATM 5941 O  O     . HOH   N 6 .   ? 32.82100 44.25800  16.79300  1.000 37.81434 ?  402 HOH   D O     1 
HETATM 5942 O  O     . HOH   N 6 .   ? 35.41000 54.66700  6.68800   1.000 47.21471 ?  403 HOH   D O     1 
HETATM 5943 O  O     . HOH   N 6 .   ? 24.47100 49.12700  22.75900  1.000 39.85905 ?  404 HOH   D O     1 
HETATM 5944 O  O     . HOH   N 6 .   ? 27.84500 22.01100  2.49700   1.000 45.76112 ?  405 HOH   D O     1 
HETATM 5945 O  O     . HOH   N 6 .   ? 41.16100 29.85400  20.44500  1.000 49.99317 ?  406 HOH   D O     1 
HETATM 5946 O  O     . HOH   N 6 .   ? 41.26200 30.57100  4.19200   1.000 42.15185 ?  407 HOH   D O     1 
HETATM 5947 O  O     . HOH   N 6 .   ? 21.21800 52.11600  16.43300  1.000 45.10366 ?  408 HOH   D O     1 
HETATM 5948 O  O     . HOH   N 6 .   ? 13.02000 45.78000  -1.86300  1.000 43.46609 ?  409 HOH   D O     1 
HETATM 5949 O  O     . HOH   N 6 .   ? 12.74900 40.87300  -0.75800  1.000 30.89961 ?  410 HOH   D O     1 
HETATM 5950 O  O     . HOH   N 6 .   ? 7.56400  40.35500  8.01900   1.000 49.97490 ?  411 HOH   D O     1 
HETATM 5951 O  O     . HOH   N 6 .   ? 12.89000 34.30200  26.31500  1.000 33.86792 ?  412 HOH   D O     1 
HETATM 5952 O  O     . HOH   N 6 .   ? 26.60800 49.23500  20.62800  1.000 31.52062 ?  413 HOH   D O     1 
HETATM 5953 O  O     . HOH   N 6 .   ? 19.40500 46.78300  -10.73500 1.000 47.74060 ?  414 HOH   D O     1 
HETATM 5954 O  O     A HOH   N 6 .   ? 25.74600 58.71800  7.12800   0.500 36.62162 ?  415 HOH   D O     1 
HETATM 5955 O  O     B HOH   N 6 .   ? 26.81700 57.17900  7.22900   0.500 33.56911 ?  415 HOH   D O     1 
HETATM 5956 O  O     . HOH   N 6 .   ? 35.52300 23.88800  6.01500   1.000 47.16591 ?  416 HOH   D O     1 
HETATM 5957 O  O     . HOH   N 6 .   ? 37.19300 28.71100  2.76900   1.000 40.58906 ?  417 HOH   D O     1 
HETATM 5958 O  O     . HOH   N 6 .   ? 10.86000 41.69100  -2.83000  1.000 43.04488 ?  418 HOH   D O     1 
HETATM 5959 O  O     . HOH   N 6 .   ? 14.23600 34.62600  -6.28400  1.000 51.68293 ?  419 HOH   D O     1 
HETATM 5960 O  O     . HOH   N 6 .   ? 33.73600 36.71700  16.32800  1.000 25.10223 ?  420 HOH   D O     1 
HETATM 5961 O  O     . HOH   N 6 .   ? 14.08900 32.40500  7.38300   1.000 34.78575 ?  421 HOH   D O     1 
HETATM 5962 O  O     . HOH   N 6 .   ? 24.25900 36.60600  -12.57400 1.000 35.10477 ?  422 HOH   D O     1 
HETATM 5963 O  O     . HOH   N 6 .   ? 34.06500 27.09900  3.26500   1.000 41.75004 ?  423 HOH   D O     1 
HETATM 5964 O  O     . HOH   N 6 .   ? 13.48000 50.11400  16.33900  1.000 42.30426 ?  424 HOH   D O     1 
HETATM 5965 O  O     . HOH   N 6 .   ? 14.65400 48.07800  2.72800   1.000 34.48854 ?  425 HOH   D O     1 
HETATM 5966 O  O     A HOH   N 6 .   ? 17.55300 23.50300  21.20700  0.500 31.86047 ?  426 HOH   D O     1 
HETATM 5967 O  O     B HOH   N 6 .   ? 15.75300 23.94900  20.29000  0.500 27.87961 ?  426 HOH   D O     1 
HETATM 5968 O  O     . HOH   N 6 .   ? 7.59800  42.98900  11.74100  1.000 49.09768 ?  427 HOH   D O     1 
HETATM 5969 O  O     . HOH   N 6 .   ? 19.22400 21.39900  21.54300  1.000 42.89504 ?  428 HOH   D O     1 
HETATM 5970 O  O     . HOH   N 6 .   ? 6.75300  44.81500  13.12000  1.000 44.97496 ?  429 HOH   D O     1 
HETATM 5971 O  O     . HOH   N 6 .   ? 16.78800 56.53600  9.34100   1.000 54.32394 ?  430 HOH   D O     1 
HETATM 5972 O  O     . HOH   N 6 .   ? 5.82400  33.16000  17.91500  1.000 45.30979 ?  431 HOH   D O     1 
HETATM 5973 O  O     . HOH   N 6 .   ? 35.86100 38.73800  -5.35300  1.000 46.22094 ?  432 HOH   D O     1 
HETATM 5974 O  O     . HOH   N 6 .   ? 10.12700 29.26400  15.25900  1.000 48.68978 ?  433 HOH   D O     1 
HETATM 5975 O  O     . HOH   N 6 .   ? 23.97800 51.57000  23.63900  1.000 38.15090 ?  434 HOH   D O     1 
HETATM 5976 O  O     . HOH   N 6 .   ? 28.24900 24.86000  5.76900   1.000 43.73317 ?  435 HOH   D O     1 
HETATM 5977 O  O     . HOH   N 6 .   ? 9.95200  52.43900  4.01100   1.000 55.18093 ?  436 HOH   D O     1 
HETATM 5978 O  O     . HOH   N 6 .   ? 19.45200 35.03800  -8.41100  1.000 42.21066 ?  437 HOH   D O     1 
HETATM 5979 O  O     . HOH   N 6 .   ? 13.47800 44.84900  0.37400   1.000 32.59832 ?  438 HOH   D O     1 
HETATM 5980 O  O     . HOH   N 6 .   ? 30.86000 22.54600  -0.35100  1.000 49.10951 ?  439 HOH   D O     1 
HETATM 5981 O  O     . HOH   N 6 .   ? 12.64500 31.16400  9.41600   1.000 41.69158 ?  440 HOH   D O     1 
HETATM 5982 O  O     . HOH   N 6 .   ? 23.37700 31.19900  0.24600   1.000 42.14558 ?  441 HOH   D O     1 
HETATM 5983 O  O     . HOH   N 6 .   ? 10.96100 27.45500  20.86100  1.000 42.17837 ?  442 HOH   D O     1 
HETATM 5984 O  O     . HOH   N 6 .   ? 20.15300 35.88600  26.96900  1.000 39.21760 ?  443 HOH   D O     1 
HETATM 5985 O  O     . HOH   N 6 .   ? 7.69200  46.85300  13.85500  1.000 47.38921 ?  444 HOH   D O     1 
HETATM 5986 O  O     . HOH   N 6 .   ? 28.00000 30.60300  -7.94900  1.000 46.47448 ?  445 HOH   D O     1 
HETATM 5987 O  O     . HOH   N 6 .   ? 26.26100 16.28700  22.53200  1.000 43.42647 ?  446 HOH   D O     1 
HETATM 5988 O  O     . HOH   N 6 .   ? 6.40800  38.74300  13.20900  1.000 37.38869 ?  447 HOH   D O     1 
HETATM 5989 O  O     . HOH   N 6 .   ? 33.44700 25.54300  18.11400  1.000 38.08910 ?  448 HOH   D O     1 
HETATM 5990 O  O     . HOH   N 6 .   ? 21.71600 54.06200  14.33400  1.000 42.29017 ?  449 HOH   D O     1 
HETATM 5991 O  O     . HOH   N 6 .   ? 21.24400 52.72500  23.52000  1.000 41.19959 ?  450 HOH   D O     1 
HETATM 5992 O  O     . HOH   N 6 .   ? 41.22800 36.61500  17.02600  1.000 43.14778 ?  451 HOH   D O     1 
HETATM 5993 O  O     . HOH   N 6 .   ? 12.82400 28.57700  10.25200  1.000 54.75488 ?  452 HOH   D O     1 
HETATM 5994 O  O     . HOH   N 6 .   ? 12.57800 49.49500  1.74800   1.000 46.74019 ?  453 HOH   D O     1 
HETATM 5995 O  O     . HOH   N 6 .   ? 7.75100  31.65700  16.81400  1.000 44.99037 ?  454 HOH   D O     1 
HETATM 5996 O  O     . HOH   N 6 .   ? 22.36800 16.99100  24.57200  1.000 50.30253 ?  455 HOH   D O     1 
HETATM 5997 O  O     . HOH   N 6 .   ? 46.17200 37.94300  7.44800   1.000 47.68934 ?  456 HOH   D O     1 
HETATM 5998 O  O     . HOH   N 6 .   ? 24.50600 39.79600  27.05200  1.000 44.32616 ?  457 HOH   D O     1 
HETATM 5999 O  O     . HOH   N 6 .   ? 30.21900 46.06500  19.56900  1.000 47.43048 ?  458 HOH   D O     1 
HETATM 6000 O  O     . HOH   N 6 .   ? 12.77700 29.80400  25.64000  1.000 32.83926 ?  459 HOH   D O     1 
HETATM 6001 O  O     . HOH   N 6 .   ? 29.16300 52.26500  -0.81200  1.000 39.42038 ?  460 HOH   D O     1 
HETATM 6002 O  O     . HOH   N 6 .   ? 29.13900 48.22100  20.15800  1.000 42.61611 ?  461 HOH   D O     1 
HETATM 6003 O  O     . HOH   N 6 .   ? 8.10600  44.11800  4.73100   1.000 48.75846 ?  462 HOH   D O     1 
HETATM 6004 O  O     . HOH   N 6 .   ? 35.86400 25.20600  3.79800   1.000 46.87722 ?  463 HOH   D O     1 
HETATM 6005 O  O     . HOH   N 6 .   ? 26.16800 21.36100  0.79300   1.000 45.51473 ?  464 HOH   D O     1 
HETATM 6006 O  O     . HOH   N 6 .   ? 16.31100 32.73000  -5.16300  1.000 45.85912 ?  465 HOH   D O     1 
HETATM 6007 O  O     . HOH   N 6 .   ? 9.70800  44.21200  0.95000   1.000 44.80195 ?  466 HOH   D O     1 
HETATM 6008 O  O     . HOH   N 6 .   ? 35.21000 44.51700  16.10600  1.000 47.14051 ?  467 HOH   D O     1 
HETATM 6009 O  O     . HOH   N 6 .   ? 18.19200 55.78200  15.94900  1.000 48.08767 ?  468 HOH   D O     1 
HETATM 6010 O  O     . HOH   N 6 .   ? 31.87400 31.33000  -7.81500  1.000 49.78767 ?  469 HOH   D O     1 
HETATM 6011 O  O     . HOH   N 6 .   ? 42.44100 32.45000  5.71000   1.000 36.31791 ?  470 HOH   D O     1 
HETATM 6012 O  O     . HOH   N 6 .   ? 6.91900  41.68300  6.00300   1.000 48.88244 ?  471 HOH   D O     1 
HETATM 6013 O  O     . HOH   N 6 .   ? 7.80900  43.00900  9.04000   1.000 48.90038 ?  472 HOH   D O     1 
HETATM 6014 O  O     . HOH   N 6 .   ? 35.48200 50.05600  -3.63800  1.000 47.78437 ?  473 HOH   D O     1 
HETATM 6015 O  O     . HOH   N 6 .   ? 19.15700 55.10700  0.90000   1.000 48.14245 ?  474 HOH   D O     1 
HETATM 6016 O  O     . HOH   N 6 .   ? 11.39600 47.44000  0.73100   1.000 52.20542 ?  475 HOH   D O     1 
HETATM 6017 O  O     . HOH   N 6 .   ? 37.44200 32.84200  23.40000  1.000 49.39650 ?  476 HOH   D O     1 
HETATM 6018 O  O     . HOH   N 6 .   ? 18.37700 39.11300  28.30900  1.000 43.83838 ?  477 HOH   D O     1 
HETATM 6019 O  O     . HOH   N 6 .   ? 24.04400 23.46400  -0.40500  1.000 47.52246 ?  478 HOH   D O     1 
HETATM 6020 O  O     . HOH   N 6 .   ? 37.88500 28.04300  0.36700   1.000 45.80252 ?  479 HOH   D O     1 
HETATM 6021 O  O     . HOH   N 6 .   ? 31.00700 29.11800  -8.37000  1.000 42.91700 ?  480 HOH   D O     1 
HETATM 6022 O  O     . HOH   N 6 .   ? 42.43200 40.11900  13.69800  1.000 32.60049 ?  481 HOH   D O     1 
HETATM 6023 O  O     . HOH   N 6 .   ? 9.83200  48.68000  14.08900  1.000 45.78645 ?  482 HOH   D O     1 
HETATM 6024 O  O     . HOH   N 6 .   ? 42.35000 37.85600  15.21100  1.000 47.75941 ?  483 HOH   D O     1 
HETATM 6025 O  O     . HOH   N 6 .   ? 38.30600 35.17000  23.83300  1.000 47.53073 ?  484 HOH   D O     1 
HETATM 6026 O  O     . HOH   N 6 .   ? 9.97200  27.56500  23.81600  1.000 50.92135 ?  485 HOH   D O     1 
HETATM 6027 O  O     . HOH   N 6 .   ? 38.08600 46.82000  9.22500   1.000 46.17865 ?  486 HOH   D O     1 
HETATM 6028 O  O     . HOH   N 6 .   ? 37.98600 46.19900  11.57400  1.000 46.71523 ?  487 HOH   D O     1 
HETATM 6029 O  O     . HOH   N 6 .   ? 38.57600 25.38000  -0.63400  1.000 47.76440 ?  488 HOH   D O     1 
HETATM 6030 O  O     . HOH   N 6 .   ? 37.51500 47.46500  -5.51200  1.000 52.93681 ?  489 HOH   D O     1 
HETATM 6031 O  O     . HOH   N 6 .   ? 39.77400 27.75100  -0.72200  1.000 47.53815 ?  490 HOH   D O     1 
HETATM 6032 O  O     . HOH   N 6 .   ? 35.78400 49.17300  -5.71900  1.000 53.42808 ?  491 HOH   D O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . SER   A 1   ? 0.49201 0.62485 0.76982 0.00496  0.03947  0.16480  0   SER   A N     
2    C  CA    . SER   A 1   ? 0.46843 0.59373 0.73173 0.00135  0.03424  0.15317  0   SER   A CA    
3    C  C     . SER   A 1   ? 0.45420 0.57003 0.71258 -0.00500 0.02395  0.14231  0   SER   A C     
4    O  O     . SER   A 1   ? 0.55976 0.67418 0.81836 -0.00558 0.02265  0.14088  0   SER   A O     
5    C  CB    . SER   A 1   ? 0.48050 0.60500 0.71941 0.00659  0.04197  0.14631  0   SER   A CB    
6    O  OG    . SER   A 1   ? 0.50880 0.62708 0.73574 0.00336  0.03752  0.13659  0   SER   A OG    
7    N  N     . MET   A 2   ? 0.40858 0.51767 0.66165 -0.00928 0.01683  0.13462  1   MET   A N     
8    C  CA    . MET   A 2   ? 0.37519 0.47502 0.62566 -0.01472 0.00644  0.12581  1   MET   A CA    
9    C  C     . MET   A 2   ? 0.33332 0.42786 0.56062 -0.01375 0.00830  0.11402  1   MET   A C     
10   O  O     . MET   A 2   ? 0.29900 0.39504 0.51031 -0.01000 0.01560  0.11035  1   MET   A O     
11   C  CB    . MET   A 2   ? 0.38082 0.47480 0.63365 -0.01894 -0.00201 0.12217  1   MET   A CB    
12   C  CG    . MET   A 2   ? 0.29837 0.38982 0.53231 -0.01775 0.00098  0.11426  1   MET   A CG    
13   S  SD    . MET   A 2   ? 0.29541 0.38065 0.53559 -0.02239 -0.00909 0.11208  1   MET   A SD    
14   C  CE    . MET   A 2   ? 0.29228 0.38749 0.55856 -0.02142 -0.00643 0.12813  1   MET   A CE    
15   N  N     . THR   A 3   ? 0.31623 0.40430 0.54229 -0.01699 0.00129  0.10834  2   THR   A N     
16   C  CA    . THR   A 3   ? 0.30706 0.38975 0.51262 -0.01646 0.00223  0.09736  2   THR   A CA    
17   C  C     . THR   A 3   ? 0.27545 0.35262 0.46452 -0.01721 0.00094  0.08797  2   THR   A C     
18   O  O     . THR   A 3   ? 0.30815 0.38115 0.50102 -0.02011 -0.00560 0.08658  2   THR   A O     
19   C  CB    . THR   A 3   ? 0.33256 0.40894 0.54101 -0.01974 -0.00576 0.09356  2   THR   A CB    
20   O  OG1   . THR   A 3   ? 0.42656 0.50855 0.65084 -0.01897 -0.00420 0.10267  2   THR   A OG1   
21   C  CG2   . THR   A 3   ? 0.31158 0.38249 0.49938 -0.01911 -0.00473 0.08254  2   THR   A CG2   
22   N  N     . GLU   A 4   ? 0.27215 0.34919 0.44322 -0.01440 0.00707  0.08180  3   GLU   A N     
23   C  CA    . GLU   A 4   ? 0.28045 0.35239 0.43582 -0.01500 0.00614  0.07289  3   GLU   A CA    
24   C  C     . GLU   A 4   ? 0.29362 0.35842 0.43602 -0.01632 0.00277  0.06322  3   GLU   A C     
25   O  O     . GLU   A 4   ? 0.29107 0.35657 0.43057 -0.01513 0.00510  0.06239  3   GLU   A O     
26   C  CB    . GLU   A 4   ? 0.30942 0.38580 0.45422 -0.01089 0.01472  0.07288  3   GLU   A CB    
27   C  CG    . GLU   A 4   ? 0.38115 0.46458 0.53763 -0.00876 0.01870  0.08267  3   GLU   A CG    
28   C  CD    . GLU   A 4   ? 0.48142 0.56842 0.62643 -0.00394 0.02681  0.08260  3   GLU   A CD    
29   O  OE1   . GLU   A 4   ? 0.52760 0.61042 0.65705 -0.00396 0.02698  0.07413  3   GLU   A OE1   
30   O  OE2   . GLU   A 4   ? 0.52988 0.62364 0.68155 0.00020  0.03289  0.09128  3   GLU   A OE2   
31   N  N     . TYR   A 5   ? 0.25003 0.30795 0.38465 -0.01844 -0.00254 0.05624  4   TYR   A N     
32   C  CA    . TYR   A 5   ? 0.23663 0.28730 0.35858 -0.01924 -0.00585 0.04727  4   TYR   A CA    
33   C  C     . TYR   A 5   ? 0.23661 0.28551 0.34281 -0.01805 -0.00259 0.04070  4   TYR   A C     
34   O  O     . TYR   A 5   ? 0.27467 0.32224 0.38019 -0.01877 -0.00429 0.04011  4   TYR   A O     
35   C  CB    . TYR   A 5   ? 0.26609 0.30878 0.39272 -0.02215 -0.01606 0.04497  4   TYR   A CB    
36   C  CG    . TYR   A 5   ? 0.24339 0.28679 0.38596 -0.02363 -0.02053 0.05094  4   TYR   A CG    
37   C  CD1   . TYR   A 5   ? 0.29486 0.33702 0.43569 -0.02334 -0.02071 0.04929  4   TYR   A CD1   
38   C  CD2   . TYR   A 5   ? 0.29228 0.33826 0.45270 -0.02523 -0.02415 0.05892  4   TYR   A CD2   
39   C  CE1   . TYR   A 5   ? 0.36946 0.41239 0.52537 -0.02472 -0.02485 0.05497  4   TYR   A CE1   
40   C  CE2   . TYR   A 5   ? 0.30531 0.35232 0.48205 -0.02666 -0.02837 0.06516  4   TYR   A CE2   
41   C  CZ    . TYR   A 5   ? 0.30860 0.35406 0.48277 -0.02639 -0.02867 0.06305  4   TYR   A CZ    
42   O  OH    . TYR   A 5   ? 0.35315 0.39974 0.54385 -0.02781 -0.03285 0.06937  4   TYR   A OH    
43   N  N     . LYS   A 6   ? 0.24942 0.29805 0.34358 -0.01634 0.00164  0.03584  5   LYS   A N     
44   C  CA    . LYS   A 6   ? 0.26634 0.31360 0.34673 -0.01519 0.00474  0.03009  5   LYS   A CA    
45   C  C     . LYS   A 6   ? 0.25968 0.29916 0.33120 -0.01634 -0.00015 0.02289  5   LYS   A C     
46   O  O     . LYS   A 6   ? 0.26742 0.30434 0.33326 -0.01591 -0.00026 0.01925  5   LYS   A O     
47   C  CB    . LYS   A 6   ? 0.33214 0.38309 0.40511 -0.01246 0.01155  0.02919  5   LYS   A CB    
48   C  CG    . LYS   A 6   ? 0.34013 0.39819 0.41909 -0.00988 0.01707  0.03618  5   LYS   A CG    
49   C  CD    . LYS   A 6   ? 0.39195 0.45212 0.46146 -0.00647 0.02300  0.03446  5   LYS   A CD    
50   C  CE    . LYS   A 6   ? 0.53384 0.59387 0.60378 -0.00593 0.02346  0.03421  5   LYS   A CE    
51   N  NZ    . LYS   A 6   ? 0.58369 0.64390 0.64331 -0.00301 0.02767  0.03100  5   LYS   A NZ    
52   N  N     . LEU   A 7   ? 0.24046 0.27607 0.31046 -0.01735 -0.00402 0.02104  6   LEU   A N     
53   C  CA    . LEU   A 7   ? 0.25385 0.28149 0.31463 -0.01750 -0.00867 0.01466  6   LEU   A CA    
54   C  C     . LEU   A 7   ? 0.27030 0.29791 0.31900 -0.01610 -0.00442 0.01031  6   LEU   A C     
55   O  O     . LEU   A 7   ? 0.27379 0.30577 0.32306 -0.01584 -0.00072 0.01227  6   LEU   A O     
56   C  CB    . LEU   A 7   ? 0.25093 0.27315 0.31697 -0.01898 -0.01638 0.01518  6   LEU   A CB    
57   C  CG    . LEU   A 7   ? 0.28253 0.30603 0.36452 -0.02082 -0.02091 0.02138  6   LEU   A CG    
58   C  CD1   . LEU   A 7   ? 0.27212 0.28847 0.35778 -0.02214 -0.02981 0.02074  6   LEU   A CD1   
59   C  CD2   . LEU   A 7   ? 0.26476 0.28657 0.34848 -0.02082 -0.02268 0.02096  6   LEU   A CD2   
60   N  N     . VAL   A 8   ? 0.24749 0.27026 0.28568 -0.01496 -0.00487 0.00481  7   VAL   A N     
61   C  CA    . VAL   A 8   ? 0.24885 0.27123 0.27644 -0.01357 -0.00123 0.00098  7   VAL   A CA    
62   C  C     . VAL   A 8   ? 0.26567 0.28007 0.28535 -0.01252 -0.00570 -0.00342 7   VAL   A C     
63   O  O     . VAL   A 8   ? 0.26612 0.27539 0.28362 -0.01179 -0.00933 -0.00540 7   VAL   A O     
64   C  CB    . VAL   A 8   ? 0.24351 0.26886 0.26614 -0.01234 0.00410  -0.00055 7   VAL   A CB    
65   C  CG1   . VAL   A 8   ? 0.24273 0.26820 0.25683 -0.01113 0.00754  -0.00351 7   VAL   A CG1   
66   C  CG2   . VAL   A 8   ? 0.23828 0.27021 0.26778 -0.01255 0.00775  0.00375  7   VAL   A CG2   
67   N  N     . VAL   A 9   ? 0.26210 0.27511 0.27691 -0.01199 -0.00547 -0.00490 8   VAL   A N     
68   C  CA    . VAL   A 9   ? 0.27440 0.27952 0.28054 -0.01013 -0.00938 -0.00883 8   VAL   A CA    
69   C  C     . VAL   A 9   ? 0.27706 0.28263 0.27316 -0.00786 -0.00419 -0.01177 8   VAL   A C     
70   O  O     . VAL   A 9   ? 0.27162 0.28193 0.26712 -0.00818 0.00035  -0.01108 8   VAL   A O     
71   C  CB    . VAL   A 9   ? 0.27347 0.27641 0.28142 -0.01084 -0.01295 -0.00813 8   VAL   A CB    
72   C  CG1   . VAL   A 9   ? 0.28270 0.27650 0.28068 -0.00817 -0.01741 -0.01228 8   VAL   A CG1   
73   C  CG2   . VAL   A 9   ? 0.26985 0.27379 0.29093 -0.01346 -0.01774 -0.00380 8   VAL   A CG2   
74   N  N     . VAL   A 10  ? 0.27819 0.27873 0.26677 -0.00534 -0.00498 -0.01473 9   VAL   A N     
75   C  CA    . VAL   A 10  ? 0.26822 0.26952 0.24868 -0.00291 0.00016  -0.01664 9   VAL   A CA    
76   C  C     . VAL   A 10  ? 0.27817 0.27131 0.24793 0.00104  -0.00229 -0.01975 9   VAL   A C     
77   O  O     . VAL   A 10  ? 0.29804 0.28390 0.26558 0.00220  -0.00858 -0.02117 9   VAL   A O     
78   C  CB    . VAL   A 10  ? 0.26471 0.26919 0.24624 -0.00284 0.00355  -0.01645 9   VAL   A CB    
79   C  CG1   . VAL   A 10  ? 0.28539 0.29753 0.27593 -0.00580 0.00638  -0.01341 9   VAL   A CG1   
80   C  CG2   . VAL   A 10  ? 0.27101 0.26958 0.25071 -0.00157 -0.00088 -0.01792 9   VAL   A CG2   
81   N  N     . GLY   A 11  ? 0.27855 0.27270 0.24165 0.00356  0.00263  -0.02055 10  GLY   A N     
82   C  CA    . GLY   A 11  ? 0.30530 0.29224 0.25729 0.00833  0.00164  -0.02286 10  GLY   A CA    
83   C  C     . GLY   A 11  ? 0.29608 0.28580 0.24427 0.00990  0.00676  -0.02229 10  GLY   A C     
84   O  O     . GLY   A 11  ? 0.30362 0.30013 0.25797 0.00689  0.00995  -0.02047 10  GLY   A O     
85   N  N     . ALA   A 12  ? 0.32052 0.30484 0.25840 0.01504  0.00761  -0.02361 11  ALA   A N     
86   C  CA    . ALA   A 12  ? 0.33214 0.31903 0.26643 0.01728  0.01299  -0.02248 11  ALA   A CA    
87   C  C     . ALA   A 12  ? 0.36290 0.35026 0.29834 0.01563  0.01164  -0.02232 11  ALA   A C     
88   O  O     . ALA   A 12  ? 0.30323 0.28701 0.24003 0.01395  0.00595  -0.02340 11  ALA   A O     
89   C  CB    . ALA   A 12  ? 0.32887 0.30890 0.25091 0.02427  0.01401  -0.02353 11  ALA   A CB    
90   N  N     . VAL   A 13  ? 0.34980 0.34141 0.28499 0.01632  0.01677  -0.02070 12  VAL   A N     
91   C  CA    . VAL   A 13  ? 0.35143 0.34380 0.28739 0.01495  0.01604  -0.02047 12  VAL   A CA    
92   C  C     . VAL   A 13  ? 0.38046 0.36348 0.30718 0.01858  0.01094  -0.02284 12  VAL   A C     
93   O  O     . VAL   A 13  ? 0.39563 0.37223 0.31213 0.02429  0.01095  -0.02401 12  VAL   A O     
94   C  CB    . VAL   A 13  ? 0.38292 0.38067 0.31961 0.01576  0.02226  -0.01825 12  VAL   A CB    
95   C  CG1   . VAL   A 13  ? 0.47887 0.47553 0.41338 0.01586  0.02142  -0.01839 12  VAL   A CG1   
96   C  CG2   . VAL   A 13  ? 0.43071 0.43684 0.37760 0.01132  0.02521  -0.01631 12  VAL   A CG2   
97   N  N     . GLY   A 14  ? 0.36504 0.34681 0.29514 0.01565  0.00627  -0.02342 13  GLY   A N     
98   C  CA    . GLY   A 14  ? 0.32918 0.30203 0.25148 0.01865  0.00073  -0.02563 13  GLY   A CA    
99   C  C     . GLY   A 14  ? 0.34639 0.30997 0.26450 0.02064  -0.00672 -0.02812 13  GLY   A C     
100  O  O     . GLY   A 14  ? 0.40274 0.35729 0.31288 0.02406  -0.01211 -0.03035 13  GLY   A O     
101  N  N     . VAL   A 15  ? 0.35186 0.31671 0.27486 0.01883  -0.00778 -0.02793 14  VAL   A N     
102  C  CA    . VAL   A 15  ? 0.33364 0.28889 0.25255 0.02098  -0.01553 -0.03037 14  VAL   A CA    
103  C  C     . VAL   A 15  ? 0.32743 0.28005 0.25422 0.01710  -0.02346 -0.03035 14  VAL   A C     
104  O  O     . VAL   A 15  ? 0.35686 0.29972 0.27996 0.01918  -0.03163 -0.03257 14  VAL   A O     
105  C  CB    . VAL   A 15  ? 0.32557 0.28218 0.24714 0.02051  -0.01488 -0.03021 14  VAL   A CB    
106  C  CG1   . VAL   A 15  ? 0.32847 0.28562 0.24127 0.02547  -0.00821 -0.03027 14  VAL   A CG1   
107  C  CG2   . VAL   A 15  ? 0.33387 0.30063 0.26989 0.01389  -0.01246 -0.02733 14  VAL   A CG2   
108  N  N     . GLY   A 16  ? 0.32828 0.28889 0.26590 0.01187  -0.02159 -0.02770 15  GLY   A N     
109  C  CA    . GLY   A 16  ? 0.31847 0.27781 0.26526 0.00815  -0.02830 -0.02660 15  GLY   A CA    
110  C  C     . GLY   A 16  ? 0.31930 0.28655 0.28060 0.00277  -0.02766 -0.02313 15  GLY   A C     
111  O  O     . GLY   A 16  ? 0.30713 0.27205 0.27696 0.00031  -0.03434 -0.02179 15  GLY   A O     
112  N  N     . LYS   A 17  ? 0.30111 0.27709 0.26565 0.00125  -0.02024 -0.02142 16  LYS   A N     
113  C  CA    . LYS   A 17  ? 0.29650 0.27981 0.27357 -0.00299 -0.01907 -0.01799 16  LYS   A CA    
114  C  C     . LYS   A 17  ? 0.29353 0.28104 0.28042 -0.00643 -0.02026 -0.01478 16  LYS   A C     
115  O  O     . LYS   A 17  ? 0.28676 0.27544 0.28427 -0.00906 -0.02401 -0.01188 16  LYS   A O     
116  C  CB    . LYS   A 17  ? 0.28167 0.27304 0.25896 -0.00342 -0.01087 -0.01703 16  LYS   A CB    
117  C  CG    . LYS   A 17  ? 0.30521 0.29338 0.27482 -0.00031 -0.00943 -0.01937 16  LYS   A CG    
118  C  CD    . LYS   A 17  ? 0.27931 0.27537 0.25061 -0.00104 -0.00197 -0.01816 16  LYS   A CD    
119  C  CE    . LYS   A 17  ? 0.30251 0.30284 0.27140 -0.00071 0.00331  -0.01777 16  LYS   A CE    
120  N  NZ    . LYS   A 17  ? 0.30759 0.30280 0.26585 0.00348  0.00416  -0.01991 16  LYS   A NZ    
121  N  N     . SER   A 18  ? 0.29011 0.28062 0.27433 -0.00638 -0.01656 -0.01471 17  SER   A N     
122  C  CA    . SER   A 18  ? 0.29114 0.28596 0.28413 -0.00930 -0.01705 -0.01152 17  SER   A CA    
123  C  C     . SER   A 18  ? 0.28881 0.27653 0.28416 -0.00955 -0.02532 -0.01171 17  SER   A C     
124  O  O     . SER   A 18  ? 0.29793 0.28834 0.30491 -0.01242 -0.02805 -0.00794 17  SER   A O     
125  C  CB    . SER   A 18  ? 0.28005 0.27937 0.26923 -0.00906 -0.01141 -0.01162 17  SER   A CB    
126  O  OG    . SER   A 18  ? 0.28183 0.28733 0.27008 -0.00898 -0.00471 -0.01123 17  SER   A OG    
127  N  N     . ALA   A 19  ? 0.30413 0.28263 0.28869 -0.00620 -0.02939 -0.01574 18  ALA   A N     
128  C  CA    . ALA   A 19  ? 0.30033 0.27055 0.28635 -0.00604 -0.03845 -0.01641 18  ALA   A CA    
129  C  C     . ALA   A 19  ? 0.30764 0.27509 0.30375 -0.00793 -0.04542 -0.01453 18  ALA   A C     
130  O  O     . ALA   A 19  ? 0.30862 0.27475 0.31498 -0.01033 -0.05149 -0.01189 18  ALA   A O     
131  C  CB    . ALA   A 19  ? 0.31238 0.27204 0.28301 -0.00095 -0.04168 -0.02138 18  ALA   A CB    
132  N  N     . LEU   A 20  ? 0.30322 0.27018 0.29765 -0.00700 -0.04460 -0.01540 19  LEU   A N     
133  C  CA    . LEU   A 20  ? 0.30452 0.26983 0.30942 -0.00897 -0.05055 -0.01320 19  LEU   A CA    
134  C  C     . LEU   A 20  ? 0.29381 0.26949 0.31521 -0.01344 -0.04758 -0.00691 19  LEU   A C     
135  O  O     . LEU   A 20  ? 0.29502 0.26965 0.32902 -0.01582 -0.05392 -0.00336 19  LEU   A O     
136  C  CB    . LEU   A 20  ? 0.30621 0.27000 0.30542 -0.00701 -0.04893 -0.01532 19  LEU   A CB    
137  C  CG    . LEU   A 20  ? 0.31971 0.27114 0.30468 -0.00203 -0.05450 -0.02075 19  LEU   A CG    
138  C  CD1   . LEU   A 20  ? 0.34296 0.29529 0.32198 -0.00004 -0.05026 -0.02233 19  LEU   A CD1   
139  C  CD2   . LEU   A 20  ? 0.32925 0.27106 0.31968 -0.00234 -0.06652 -0.02093 19  LEU   A CD2   
140  N  N     . THR   A 21  ? 0.28397 0.26944 0.30559 -0.01422 -0.03813 -0.00517 20  THR   A N     
141  C  CA    . THR   A 21  ? 0.28548 0.28046 0.32099 -0.01728 -0.03465 0.00090  20  THR   A CA    
142  C  C     . THR   A 21  ? 0.29138 0.28826 0.33520 -0.01913 -0.03667 0.00440  20  THR   A C     
143  O  O     . THR   A 21  ? 0.27254 0.27302 0.33082 -0.02145 -0.03884 0.01003  20  THR   A O     
144  C  CB    . THR   A 21  ? 0.26964 0.27300 0.30140 -0.01682 -0.02486 0.00124  20  THR   A CB    
145  O  OG1   . THR   A 21  ? 0.27048 0.27191 0.29583 -0.01526 -0.02355 -0.00165 20  THR   A OG1   
146  C  CG2   . THR   A 21  ? 0.26836 0.28079 0.31280 -0.01883 -0.02110 0.00753  20  THR   A CG2   
147  N  N     . ILE   A 22  ? 0.27513 0.27016 0.31056 -0.01802 -0.03556 0.00164  21  ILE   A N     
148  C  CA    . ILE   A 22  ? 0.30141 0.29775 0.34392 -0.01965 -0.03765 0.00461  21  ILE   A CA    
149  C  C     . ILE   A 22  ? 0.29876 0.28690 0.34823 -0.02055 -0.04847 0.00521  21  ILE   A C     
150  O  O     . ILE   A 22  ? 0.29393 0.28465 0.35615 -0.02287 -0.05120 0.01012  21  ILE   A O     
151  C  CB    . ILE   A 22  ? 0.30693 0.30293 0.33808 -0.01810 -0.03388 0.00119  21  ILE   A CB    
152  C  CG1   . ILE   A 22  ? 0.32988 0.33432 0.35703 -0.01764 -0.02406 0.00151  21  ILE   A CG1   
153  C  CG2   . ILE   A 22  ? 0.37174 0.36784 0.40929 -0.01964 -0.03693 0.00370  21  ILE   A CG2   
154  C  CD1   . ILE   A 22  ? 0.39390 0.39805 0.40969 -0.01595 -0.02005 -0.00198 21  ILE   A CD1   
155  N  N     . GLN   A 23  ? 0.29218 0.27008 0.33413 -0.01853 -0.05521 0.00063  22  GLN   A N     
156  C  CA    . GLN   A 23  ? 0.30128 0.27092 0.35147 -0.01945 -0.06664 0.00157  22  GLN   A CA    
157  C  C     . GLN   A 23  ? 0.32671 0.30161 0.39509 -0.02260 -0.06841 0.00807  22  GLN   A C     
158  O  O     . GLN   A 23  ? 0.29744 0.27169 0.38023 -0.02498 -0.07480 0.01265  22  GLN   A O     
159  C  CB    . GLN   A 23  ? 0.36234 0.31915 0.39997 -0.01592 -0.07389 -0.00470 22  GLN   A CB    
160  C  CG    . GLN   A 23  ? 0.37265 0.32018 0.39677 -0.01265 -0.07772 -0.00984 22  GLN   A CG    
161  C  CD    . GLN   A 23  ? 0.36421 0.30593 0.39665 -0.01412 -0.08728 -0.00826 22  GLN   A CD    
162  O  OE1   . GLN   A 23  ? 0.37583 0.32241 0.42634 -0.01816 -0.08999 -0.00224 22  GLN   A OE1   
163  N  NE2   . GLN   A 23  ? 0.35672 0.28759 0.37581 -0.01040 -0.09257 -0.01351 22  GLN   A NE2   
164  N  N     . LEU   A 24  ? 0.29169 0.27107 0.35979 -0.02241 -0.06346 0.00858  23  LEU   A N     
165  C  CA    . LEU   A 24  ? 0.28677 0.27231 0.37168 -0.02498 -0.06357 0.01520  23  LEU   A CA    
166  C  C     . LEU   A 24  ? 0.29149 0.28730 0.39048 -0.02729 -0.05893 0.02275  23  LEU   A C     
167  O  O     . LEU   A 24  ? 0.30357 0.30110 0.41986 -0.02958 -0.06360 0.02917  23  LEU   A O     
168  C  CB    . LEU   A 24  ? 0.28196 0.27220 0.36188 -0.02397 -0.05655 0.01427  23  LEU   A CB    
169  C  CG    . LEU   A 24  ? 0.27733 0.27391 0.37445 -0.02621 -0.05642 0.02141  23  LEU   A CG    
170  C  CD1   . LEU   A 24  ? 0.29078 0.27877 0.39537 -0.02707 -0.06762 0.02153  23  LEU   A CD1   
171  C  CD2   . LEU   A 24  ? 0.30566 0.30929 0.39894 -0.02527 -0.04755 0.02165  23  LEU   A CD2   
172  N  N     . ILE   A 25  ? 0.29966 0.30254 0.39182 -0.02643 -0.04957 0.02249  24  ILE   A N     
173  C  CA    . ILE   A 25  ? 0.31289 0.32637 0.41625 -0.02757 -0.04328 0.02969  24  ILE   A CA    
174  C  C     . ILE   A 25  ? 0.32209 0.33449 0.43074 -0.02872 -0.04682 0.03167  24  ILE   A C     
175  O  O     . ILE   A 25  ? 0.38010 0.39783 0.50474 -0.03036 -0.04727 0.03922  24  ILE   A O     
176  C  CB    . ILE   A 25  ? 0.32212 0.34308 0.41557 -0.02574 -0.03218 0.02849  24  ILE   A CB    
177  C  CG1   . ILE   A 25  ? 0.29449 0.31652 0.38161 -0.02445 -0.02827 0.02610  24  ILE   A CG1   
178  C  CG2   . ILE   A 25  ? 0.33089 0.36195 0.43440 -0.02591 -0.02581 0.03592  24  ILE   A CG2   
179  C  CD1   . ILE   A 25  ? 0.30138 0.32634 0.40133 -0.02540 -0.02952 0.03144  24  ILE   A CD1   
180  N  N     . GLN   A 26  ? 0.28877 0.29423 0.38477 -0.02769 -0.04946 0.02540  25  GLN   A N     
181  C  CA    . GLN   A 26  ? 0.32428 0.32936 0.42355 -0.02855 -0.05157 0.02686  25  GLN   A CA    
182  C  C     . GLN   A 26  ? 0.38457 0.37824 0.48474 -0.02902 -0.06341 0.02417  25  GLN   A C     
183  O  O     . GLN   A 26  ? 0.39695 0.38976 0.50204 -0.03005 -0.06650 0.02595  25  GLN   A O     
184  C  CB    . GLN   A 26  ? 0.36375 0.37117 0.44843 -0.02680 -0.04422 0.02266  25  GLN   A CB    
185  C  CG    . GLN   A 26  ? 0.48082 0.49945 0.56708 -0.02634 -0.03364 0.02647  25  GLN   A CG    
186  C  CD    . GLN   A 26  ? 0.49642 0.51686 0.56808 -0.02454 -0.02680 0.02193  25  GLN   A CD    
187  O  OE1   . GLN   A 26  ? 0.56557 0.57992 0.62662 -0.02371 -0.02911 0.01657  25  GLN   A OE1   
188  N  NE2   . GLN   A 26  ? 0.62228 0.65086 0.69338 -0.02358 -0.01850 0.02426  25  GLN   A NE2   
189  N  N     . ASN   A 27  ? 0.32667 0.31111 0.42200 -0.02801 -0.07045 0.01994  26  ASN   A N     
190  C  CA    . ASN   A 27  ? 0.33881 0.31039 0.43352 -0.02763 -0.08305 0.01677  26  ASN   A CA    
191  C  C     . ASN   A 27  ? 0.43147 0.39675 0.51181 -0.02547 -0.08418 0.01113  26  ASN   A C     
192  O  O     . ASN   A 27  ? 0.45213 0.41035 0.53624 -0.02592 -0.09288 0.01102  26  ASN   A O     
193  C  CB    . ASN   A 27  ? 0.32484 0.29667 0.44156 -0.03094 -0.09116 0.02404  26  ASN   A CB    
194  C  CG    . ASN   A 27  ? 0.37307 0.33206 0.49297 -0.03074 -0.10495 0.02181  26  ASN   A CG    
195  O  OD1   . ASN   A 27  ? 0.44173 0.40173 0.57090 -0.03182 -0.10707 0.02471  26  ASN   A OD1   
196  N  ND2   . ASN   A 27  ? 0.38144 0.32776 0.49355 -0.02910 -0.11486 0.01667  26  ASN   A ND2   
197  N  N     . HIS   A 28  ? 0.39774 0.36538 0.46203 -0.02302 -0.07565 0.00664  27  HIS   A N     
198  C  CA    . HIS   A 28  ? 0.47552 0.43685 0.52478 -0.02033 -0.07623 0.00110  27  HIS   A CA    
199  C  C     . HIS   A 28  ? 0.43946 0.39835 0.46964 -0.01639 -0.07067 -0.00506 27  HIS   A C     
200  O  O     . HIS   A 28  ? 0.37084 0.33612 0.40023 -0.01647 -0.06376 -0.00441 27  HIS   A O     
201  C  CB    . HIS   A 28  ? 0.50446 0.47355 0.55812 -0.02209 -0.07090 0.00431  27  HIS   A CB    
202  C  CG    . HIS   A 28  ? 0.43765 0.41786 0.48776 -0.02216 -0.05869 0.00546  27  HIS   A CG    
203  N  ND1   . HIS   A 28  ? 0.55156 0.53143 0.58565 -0.01944 -0.05270 0.00047  27  HIS   A ND1   
204  C  CD2   . HIS   A 28  ? 0.50349 0.49494 0.56409 -0.02425 -0.05182 0.01123  27  HIS   A CD2   
205  C  CE1   . HIS   A 28  ? 0.53440 0.52462 0.56984 -0.02025 -0.04326 0.00289  27  HIS   A CE1   
206  N  NE2   . HIS   A 28  ? 0.56250 0.55956 0.61303 -0.02286 -0.04255 0.00919  27  HIS   A NE2   
207  N  N     . PHE   A 29  ? 0.45667 0.40667 0.47232 -0.01282 -0.07348 -0.01045 28  PHE   A N     
208  C  CA    . PHE   A 29  ? 0.48933 0.43653 0.48679 -0.00834 -0.06823 -0.01574 28  PHE   A CA    
209  C  C     . PHE   A 29  ? 0.48877 0.43590 0.47603 -0.00638 -0.06425 -0.01796 28  PHE   A C     
210  O  O     . PHE   A 29  ? 0.58816 0.52996 0.57640 -0.00642 -0.07030 -0.01830 28  PHE   A O     
211  C  CB    . PHE   A 29  ? 0.47034 0.40395 0.45739 -0.00403 -0.07664 -0.02055 28  PHE   A CB    
212  C  CG    . PHE   A 29  ? 0.43233 0.36147 0.39991 0.00171  -0.07204 -0.02564 28  PHE   A CG    
213  C  CD1   . PHE   A 29  ? 0.40006 0.33361 0.36381 0.00274  -0.06542 -0.02603 28  PHE   A CD1   
214  C  CD2   . PHE   A 29  ? 0.48698 0.40760 0.44053 0.00636  -0.07421 -0.02957 28  PHE   A CD2   
215  C  CE1   . PHE   A 29  ? 0.39802 0.32804 0.34543 0.00815  -0.06092 -0.02975 28  PHE   A CE1   
216  C  CE2   . PHE   A 29  ? 0.51669 0.43389 0.45329 0.01212  -0.06928 -0.03320 28  PHE   A CE2   
217  C  CZ    . PHE   A 29  ? 0.44971 0.37176 0.38374 0.01296  -0.06263 -0.03306 28  PHE   A CZ    
218  N  N     . VAL   A 30  ? 0.55760 0.51023 0.53594 -0.00470 -0.05479 -0.01925 29  VAL   A N     
219  C  CA    . VAL   A 30  ? 0.60430 0.55691 0.57219 -0.00235 -0.05040 -0.02134 29  VAL   A CA    
220  C  C     . VAL   A 30  ? 0.54838 0.49813 0.50133 0.00261  -0.04570 -0.02491 29  VAL   A C     
221  O  O     . VAL   A 30  ? 0.52818 0.48219 0.48251 0.00225  -0.04165 -0.02425 29  VAL   A O     
222  C  CB    . VAL   A 30  ? 0.58177 0.54651 0.55709 -0.00592 -0.04238 -0.01773 29  VAL   A CB    
223  C  CG1   . VAL   A 30  ? 0.63079 0.59565 0.59593 -0.00360 -0.03792 -0.01974 29  VAL   A CG1   
224  C  CG2   . VAL   A 30  ? 0.58849 0.55716 0.57920 -0.01036 -0.04586 -0.01325 29  VAL   A CG2   
225  N  N     . ASP   A 31  ? 0.58759 0.53036 0.52708 0.00734  -0.04619 -0.02819 30  ASP   A N     
226  C  CA    . ASP   A 31  ? 0.57125 0.51088 0.49640 0.01299  -0.04157 -0.03087 30  ASP   A CA    
227  C  C     . ASP   A 31  ? 0.53959 0.49026 0.46537 0.01191  -0.03066 -0.02886 30  ASP   A C     
228  O  O     . ASP   A 31  ? 0.66512 0.61510 0.58115 0.01620  -0.02561 -0.02996 30  ASP   A O     
229  C  CB    . ASP   A 31  ? 0.62034 0.54757 0.53009 0.01959  -0.04623 -0.03472 30  ASP   A CB    
230  C  CG    . ASP   A 31  ? 0.72756 0.64812 0.62275 0.02653  -0.04463 -0.03738 30  ASP   A CG    
231  O  OD1   . ASP   A 31  ? 0.65679 0.57586 0.55367 0.02652  -0.04659 -0.03772 30  ASP   A OD1   
232  O  OD2   . ASP   A 31  ? 0.80533 0.72248 0.68776 0.03214  -0.04111 -0.03874 30  ASP   A OD2   
233  N  N     . GLU   A 32  ? 0.59763 0.55786 0.53464 0.00670  -0.02733 -0.02575 31  GLU   A N     
234  C  CA    . GLU   A 32  ? 0.53397 0.50338 0.47090 0.00606  -0.01802 -0.02420 31  GLU   A CA    
235  C  C     . GLU   A 32  ? 0.56210 0.53737 0.50264 0.00504  -0.01332 -0.02299 31  GLU   A C     
236  O  O     . GLU   A 32  ? 0.56444 0.54022 0.51211 0.00269  -0.01637 -0.02210 31  GLU   A O     
237  C  CB    . GLU   A 32  ? 0.55043 0.52730 0.49599 0.00181  -0.01584 -0.02165 31  GLU   A CB    
238  C  CG    . GLU   A 32  ? 0.62337 0.59643 0.56273 0.00365  -0.01701 -0.02289 31  GLU   A CG    
239  C  CD    . GLU   A 32  ? 0.63102 0.61086 0.57890 -0.00045 -0.01550 -0.02041 31  GLU   A CD    
240  O  OE1   . GLU   A 32  ? 0.68451 0.67269 0.64176 -0.00406 -0.01214 -0.01762 31  GLU   A OE1   
241  O  OE2   . GLU   A 32  ? 0.71491 0.69115 0.65920 0.00048  -0.01777 -0.02132 31  GLU   A OE2   
242  N  N     . TYR   A 33  ? 0.45953 0.43910 0.39596 0.00677  -0.00628 -0.02266 32  TYR   A N     
243  C  CA    . TYR   A 33  ? 0.47454 0.45920 0.41390 0.00614  -0.00192 -0.02162 32  TYR   A CA    
244  C  C     . TYR   A 33  ? 0.45232 0.44713 0.40075 0.00204  0.00310  -0.01894 32  TYR   A C     
245  O  O     . TYR   A 33  ? 0.44262 0.44129 0.38971 0.00245  0.00777  -0.01820 32  TYR   A O     
246  C  CB    . TYR   A 33  ? 0.44045 0.42279 0.37013 0.01118  0.00220  -0.02257 32  TYR   A CB    
247  C  CG    . TYR   A 33  ? 0.47939 0.46773 0.41332 0.01015  0.00693  -0.02115 32  TYR   A CG    
248  C  CD1   . TYR   A 33  ? 0.46025 0.45044 0.40129 0.00707  0.00476  -0.02073 32  TYR   A CD1   
249  C  CD2   . TYR   A 33  ? 0.52499 0.51723 0.45670 0.01224  0.01340  -0.01986 32  TYR   A CD2   
250  C  CE1   . TYR   A 33  ? 0.44439 0.43958 0.38889 0.00630  0.00877  -0.01962 32  TYR   A CE1   
251  C  CE2   . TYR   A 33  ? 0.54164 0.53899 0.47785 0.01123  0.01714  -0.01851 32  TYR   A CE2   
252  C  CZ    . TYR   A 33  ? 0.50534 0.50390 0.44739 0.00829  0.01470  -0.01868 32  TYR   A CZ    
253  O  OH    . TYR   A 33  ? 0.50860 0.51180 0.45480 0.00738  0.01805  -0.01753 32  TYR   A OH    
254  N  N     . ASP   A 34  ? 0.40748 0.40626 0.36492 -0.00148 0.00204  -0.01732 33  ASP   A N     
255  C  CA    . ASP   A 34  ? 0.41628 0.42368 0.38108 -0.00446 0.00641  -0.01491 33  ASP   A CA    
256  C  C     . ASP   A 34  ? 0.41414 0.42443 0.38097 -0.00456 0.00900  -0.01448 33  ASP   A C     
257  O  O     . ASP   A 34  ? 0.33846 0.34892 0.31034 -0.00601 0.00666  -0.01367 33  ASP   A O     
258  C  CB    . ASP   A 34  ? 0.42615 0.43615 0.39955 -0.00771 0.00375  -0.01269 33  ASP   A CB    
259  C  CG    . ASP   A 34  ? 0.46271 0.48076 0.44218 -0.00978 0.00810  -0.01020 33  ASP   A CG    
260  O  OD1   . ASP   A 34  ? 0.47643 0.49768 0.45359 -0.00909 0.01249  -0.01051 33  ASP   A OD1   
261  O  OD2   . ASP   A 34  ? 0.56353 0.58438 0.55029 -0.01179 0.00683  -0.00763 33  ASP   A OD2   
262  N  N     . PRO   A 35  ? 0.38376 0.39645 0.34764 -0.00309 0.01365  -0.01466 34  PRO   A N     
263  C  CA    . PRO   A 35  ? 0.35740 0.37204 0.32275 -0.00288 0.01574  -0.01443 34  PRO   A CA    
264  C  C     . PRO   A 35  ? 0.32310 0.34322 0.29645 -0.00582 0.01642  -0.01259 34  PRO   A C     
265  O  O     . PRO   A 35  ? 0.35184 0.37615 0.32884 -0.00740 0.01779  -0.01120 34  PRO   A O     
266  C  CB    . PRO   A 35  ? 0.36562 0.38235 0.32790 -0.00095 0.02052  -0.01420 34  PRO   A CB    
267  C  CG    . PRO   A 35  ? 0.38065 0.39888 0.34251 -0.00132 0.02155  -0.01369 34  PRO   A CG    
268  C  CD    . PRO   A 35  ? 0.40222 0.41663 0.36292 -0.00191 0.01718  -0.01450 34  PRO   A CD    
269  N  N     . THR   A 36  ? 0.31384 0.33346 0.28940 -0.00610 0.01528  -0.01252 35  THR   A N     
270  C  CA    . THR   A 36  ? 0.26616 0.29022 0.24878 -0.00819 0.01567  -0.01049 35  THR   A CA    
271  C  C     . THR   A 36  ? 0.24901 0.27744 0.23250 -0.00804 0.01976  -0.01009 35  THR   A C     
272  O  O     . THR   A 36  ? 0.26112 0.28864 0.24157 -0.00666 0.02142  -0.01119 35  THR   A O     
273  C  CB    . THR   A 36  ? 0.25753 0.27911 0.24274 -0.00854 0.01246  -0.01032 35  THR   A CB    
274  O  OG1   . THR   A 36  ? 0.31519 0.33180 0.30019 -0.00864 0.00750  -0.01073 35  THR   A OG1   
275  C  CG2   . THR   A 36  ? 0.28731 0.31380 0.28002 -0.01016 0.01342  -0.00758 35  THR   A CG2   
276  N  N     . ILE   A 37  ? 0.28557 0.31834 0.27315 -0.00910 0.02112  -0.00833 36  ILE   A N     
277  C  CA    . ILE   A 37  ? 0.26028 0.29626 0.24949 -0.00883 0.02353  -0.00782 36  ILE   A CA    
278  C  C     . ILE   A 37  ? 0.25202 0.28848 0.24473 -0.00915 0.02265  -0.00670 36  ILE   A C     
279  O  O     . ILE   A 37  ? 0.29538 0.33101 0.28743 -0.00866 0.02303  -0.00759 36  ILE   A O     
280  C  CB    . ILE   A 37  ? 0.28073 0.32002 0.27125 -0.00886 0.02494  -0.00661 36  ILE   A CB    
281  C  CG1   . ILE   A 37  ? 0.35662 0.39546 0.34463 -0.00889 0.02527  -0.00733 36  ILE   A CG1   
282  C  CG2   . ILE   A 37  ? 0.27791 0.31913 0.26897 -0.00795 0.02656  -0.00657 36  ILE   A CG2   
283  C  CD1   . ILE   A 37  ? 0.35571 0.39353 0.34118 -0.00813 0.02657  -0.00868 36  ILE   A CD1   
284  N  N     . GLU   A 38  ? 0.24639 0.28445 0.24343 -0.00983 0.02165  -0.00430 37  GLU   A N     
285  C  CA    . GLU   A 38  ? 0.27499 0.31377 0.27664 -0.01010 0.02074  -0.00241 37  GLU   A CA    
286  C  C     . GLU   A 38  ? 0.31690 0.35750 0.32423 -0.01079 0.01960  0.00101  37  GLU   A C     
287  O  O     . GLU   A 38  ? 0.30867 0.35209 0.31638 -0.01018 0.02147  0.00261  37  GLU   A O     
288  C  CB    . GLU   A 38  ? 0.30243 0.34390 0.30440 -0.00894 0.02333  -0.00183 37  GLU   A CB    
289  C  CG    . GLU   A 38  ? 0.36481 0.40710 0.37127 -0.00896 0.02281  0.00020  37  GLU   A CG    
290  C  CD    . GLU   A 38  ? 0.46202 0.50693 0.46825 -0.00718 0.02547  0.00115  37  GLU   A CD    
291  O  OE1   . GLU   A 38  ? 0.49576 0.53962 0.49889 -0.00672 0.02614  -0.00118 37  GLU   A OE1   
292  O  OE2   . GLU   A 38  ? 0.49899 0.54673 0.50796 -0.00586 0.02687  0.00442  37  GLU   A OE2   
293  N  N     . ASP   A 39  ? 0.26985 0.30872 0.28195 -0.01188 0.01635  0.00240  38  ASP   A N     
294  C  CA    . ASP   A 39  ? 0.26381 0.30474 0.28335 -0.01266 0.01506  0.00653  38  ASP   A CA    
295  C  C     . ASP   A 39  ? 0.29373 0.33567 0.32095 -0.01309 0.01368  0.00978  38  ASP   A C     
296  O  O     . ASP   A 39  ? 0.28672 0.32571 0.31312 -0.01342 0.01169  0.00792  38  ASP   A O     
297  C  CB    . ASP   A 39  ? 0.28067 0.31795 0.30058 -0.01395 0.01104  0.00577  38  ASP   A CB    
298  C  CG    . ASP   A 39  ? 0.37757 0.41463 0.39102 -0.01347 0.01276  0.00345  38  ASP   A CG    
299  O  OD1   . ASP   A 39  ? 0.45229 0.49344 0.46617 -0.01280 0.01597  0.00524  38  ASP   A OD1   
300  O  OD2   . ASP   A 39  ? 0.37727 0.40985 0.38499 -0.01336 0.01089  0.00003  38  ASP   A OD2   
301  N  N     . SER   A 40  ? 0.24521 0.29160 0.27996 -0.01273 0.01513  0.01501  39  SER   A N     
302  C  CA    . SER   A 40  ? 0.25077 0.29921 0.29481 -0.01296 0.01432  0.01952  39  SER   A CA    
303  C  C     . SER   A 40  ? 0.25449 0.30374 0.30877 -0.01440 0.01122  0.02419  39  SER   A C     
304  O  O     . SER   A 40  ? 0.28303 0.33418 0.33792 -0.01414 0.01239  0.02583  39  SER   A O     
305  C  CB    . SER   A 40  ? 0.28401 0.33775 0.32900 -0.01029 0.01963  0.02301  39  SER   A CB    
306  O  OG    . SER   A 40  ? 0.51128 0.56380 0.54874 -0.00922 0.02141  0.01910  39  SER   A OG    
307  N  N     . TYR   A 41  ? 0.23899 0.28680 0.30201 -0.01590 0.00705  0.02661  40  TYR   A N     
308  C  CA    . TYR   A 41  ? 0.23387 0.28205 0.30901 -0.01759 0.00296  0.03162  40  TYR   A CA    
309  C  C     . TYR   A 41  ? 0.25433 0.30548 0.34192 -0.01786 0.00222  0.03760  40  TYR   A C     
310  O  O     . TYR   A 41  ? 0.23338 0.28415 0.31918 -0.01735 0.00298  0.03638  40  TYR   A O     
311  C  CB    . TYR   A 41  ? 0.23875 0.27929 0.31256 -0.01970 -0.00456 0.02768  40  TYR   A CB    
312  C  CG    . TYR   A 41  ? 0.25472 0.29168 0.31634 -0.01924 -0.00423 0.02184  40  TYR   A CG    
313  C  CD1   . TYR   A 41  ? 0.26745 0.30043 0.31687 -0.01825 -0.00350 0.01554  40  TYR   A CD1   
314  C  CD2   . TYR   A 41  ? 0.30427 0.34212 0.36700 -0.01963 -0.00435 0.02305  40  TYR   A CD2   
315  C  CE1   . TYR   A 41  ? 0.28297 0.31297 0.32220 -0.01758 -0.00297 0.01095  40  TYR   A CE1   
316  C  CE2   . TYR   A 41  ? 0.37678 0.41147 0.42866 -0.01913 -0.00394 0.01797  40  TYR   A CE2   
317  C  CZ    . TYR   A 41  ? 0.37890 0.40985 0.41933 -0.01805 -0.00313 0.01215  40  TYR   A CZ    
318  O  OH    . TYR   A 41  ? 0.40847 0.43669 0.43927 -0.01732 -0.00247 0.00797  40  TYR   A OH    
319  N  N     A ARG   A 42  ? 0.23328 0.28773 0.33426 -0.01861 0.00089  0.04457  41  ARG   A N     
320  N  N     B ARG   A 42  ? 0.23342 0.28762 0.33445 -0.01870 0.00062  0.04445  41  ARG   A N     
321  C  CA    A ARG   A 42  ? 0.23318 0.29088 0.34915 -0.01909 -0.00037 0.05176  41  ARG   A CA    
322  C  CA    B ARG   A 42  ? 0.23319 0.29080 0.34889 -0.01907 -0.00035 0.05161  41  ARG   A CA    
323  C  C     A ARG   A 42  ? 0.23643 0.29075 0.36505 -0.02213 -0.00853 0.05463  41  ARG   A C     
324  C  C     B ARG   A 42  ? 0.23615 0.29111 0.36545 -0.02200 -0.00808 0.05522  41  ARG   A C     
325  O  O     A ARG   A 42  ? 0.23825 0.29154 0.36771 -0.02296 -0.01044 0.05472  41  ARG   A O     
326  O  O     B ARG   A 42  ? 0.23836 0.29319 0.36955 -0.02267 -0.00937 0.05618  41  ARG   A O     
327  C  CB    A ARG   A 42  ? 0.22989 0.29648 0.35271 -0.01613 0.00703  0.05990  41  ARG   A CB    
328  C  CB    B ARG   A 42  ? 0.23116 0.29760 0.35191 -0.01584 0.00764  0.05904  41  ARG   A CB    
329  C  CG    A ARG   A 42  ? 0.28245 0.35199 0.39594 -0.01271 0.01392  0.05860  41  ARG   A CG    
330  C  CG    B ARG   A 42  ? 0.28079 0.34888 0.38860 -0.01259 0.01421  0.05557  41  ARG   A CG    
331  C  CD    A ARG   A 42  ? 0.26786 0.34441 0.38338 -0.00876 0.02107  0.06505  41  ARG   A CD    
332  C  CD    B ARG   A 42  ? 0.29083 0.36514 0.40582 -0.00960 0.01931  0.06274  41  ARG   A CD    
333  N  NE    A ARG   A 42  ? 0.30275 0.38516 0.43435 -0.00761 0.02268  0.07517  41  ARG   A NE    
334  N  NE    B ARG   A 42  ? 0.32310 0.39709 0.42798 -0.00729 0.02297  0.05907  41  ARG   A NE    
335  C  CZ    A ARG   A 42  ? 0.32285 0.40838 0.45695 -0.00519 0.02617  0.07866  41  ARG   A CZ    
336  C  CZ    B ARG   A 42  ? 0.36407 0.44267 0.47296 -0.00413 0.02752  0.06446  41  ARG   A CZ    
337  N  NH1   A ARG   A 42  ? 0.30690 0.38978 0.42905 -0.00415 0.02761  0.07254  41  ARG   A NH1   
338  N  NH1   B ARG   A 42  ? 0.35097 0.43522 0.47385 -0.00276 0.02946  0.07402  41  ARG   A NH1   
339  N  NH2   A ARG   A 42  ? 0.34684 0.43843 0.49616 -0.00361 0.02843  0.08887  41  ARG   A NH2   
340  N  NH2   B ARG   A 42  ? 0.29375 0.37132 0.39277 -0.00206 0.03028  0.06055  41  ARG   A NH2   
341  N  N     . LYS   A 43  ? 0.23863 0.29094 0.37737 -0.02374 -0.01375 0.05703  42  LYS   A N     
342  C  CA    . LYS   A 43  ? 0.24409 0.29288 0.39701 -0.02658 -0.02254 0.06054  42  LYS   A CA    
343  C  C     . LYS   A 43  ? 0.24267 0.29369 0.41114 -0.02747 -0.02499 0.06703  42  LYS   A C     
344  O  O     . LYS   A 43  ? 0.24308 0.29235 0.40671 -0.02704 -0.02478 0.06405  42  LYS   A O     
345  C  CB    . LYS   A 43  ? 0.26872 0.30640 0.41303 -0.02822 -0.03145 0.05232  42  LYS   A CB    
346  C  CG    . LYS   A 43  ? 0.28701 0.31978 0.44580 -0.03092 -0.04180 0.05569  42  LYS   A CG    
347  C  CD    . LYS   A 43  ? 0.29072 0.31110 0.43819 -0.03142 -0.05086 0.04690  42  LYS   A CD    
348  C  CE    . LYS   A 43  ? 0.40342 0.41711 0.56500 -0.03384 -0.06285 0.04969  42  LYS   A CE    
349  N  NZ    . LYS   A 43  ? 0.46557 0.48437 0.64071 -0.03521 -0.06271 0.05670  42  LYS   A NZ    
350  N  N     . GLN   A 44  ? 0.24664 0.30170 0.43450 -0.02872 -0.02733 0.07626  43  GLN   A N     
351  C  CA    . GLN   A 44  ? 0.25104 0.30798 0.45736 -0.03008 -0.03117 0.08367  43  GLN   A CA    
352  C  C     . GLN   A 44  ? 0.26298 0.30943 0.47447 -0.03343 -0.04436 0.08022  43  GLN   A C     
353  O  O     . GLN   A 44  ? 0.28345 0.32445 0.49486 -0.03491 -0.05060 0.07793  43  GLN   A O     
354  C  CB    . GLN   A 44  ? 0.31105 0.37747 0.53686 -0.02953 -0.02742 0.09605  43  GLN   A CB    
355  C  CG    . GLN   A 44  ? 0.39236 0.46309 0.63899 -0.03030 -0.02924 0.10570  43  GLN   A CG    
356  C  CD    . GLN   A 44  ? 0.26428 0.34337 0.53216 -0.03004 -0.02713 0.11841  43  GLN   A CD    
357  O  OE1   . GLN   A 44  ? 0.36011 0.44456 0.62459 -0.02769 -0.02018 0.12091  43  GLN   A OE1   
358  N  NE2   . GLN   A 44  ? 0.35186 0.43172 0.64171 -0.03239 -0.03346 0.12643  43  GLN   A NE2   
359  N  N     . VAL   A 45  ? 0.31059 0.35359 0.52581 -0.03429 -0.04894 0.07959  44  VAL   A N     
360  C  CA    . VAL   A 45  ? 0.29476 0.32674 0.51437 -0.03684 -0.06225 0.07620  44  VAL   A CA    
361  C  C     . VAL   A 45  ? 0.32746 0.36119 0.56578 -0.03833 -0.06642 0.08334  44  VAL   A C     
362  O  O     . VAL   A 45  ? 0.34777 0.39089 0.59302 -0.03708 -0.05835 0.08986  44  VAL   A O     
363  C  CB    . VAL   A 45  ? 0.26591 0.28752 0.46286 -0.03574 -0.06531 0.06375  44  VAL   A CB    
364  C  CG1   . VAL   A 45  ? 0.27216 0.29156 0.45263 -0.03443 -0.06228 0.05736  44  VAL   A CG1   
365  C  CG2   . VAL   A 45  ? 0.29001 0.31478 0.47770 -0.03393 -0.05831 0.06126  44  VAL   A CG2   
366  N  N     . VAL   A 46  ? 0.31477 0.33874 0.56104 -0.04071 -0.07959 0.08203  45  VAL   A N     
367  C  CA    . VAL   A 46  ? 0.28983 0.31295 0.55213 -0.04231 -0.08568 0.08704  45  VAL   A CA    
368  C  C     . VAL   A 46  ? 0.37856 0.38890 0.62650 -0.04206 -0.09414 0.07673  45  VAL   A C     
369  O  O     . VAL   A 46  ? 0.38311 0.38198 0.62244 -0.04221 -0.10345 0.06975  45  VAL   A O     
370  C  CB    . VAL   A 46  ? 0.29645 0.31935 0.58538 -0.04538 -0.09520 0.09654  45  VAL   A CB    
371  C  CG1   . VAL   A 46  ? 0.33579 0.36007 0.64341 -0.04691 -0.09975 0.10336  45  VAL   A CG1   
372  C  CG2   . VAL   A 46  ? 0.31078 0.34526 0.61193 -0.04512 -0.08710 0.10611  45  VAL   A CG2   
373  N  N     . ILE   A 47  ? 0.34600 0.35797 0.59089 -0.04123 -0.09095 0.07586  46  ILE   A N     
374  C  CA    . ILE   A 47  ? 0.40407 0.40479 0.63432 -0.04036 -0.09751 0.06636  46  ILE   A CA    
375  C  C     . ILE   A 47  ? 0.43316 0.43359 0.67910 -0.04190 -0.10298 0.07136  46  ILE   A C     
376  O  O     . ILE   A 47  ? 0.37428 0.38477 0.62734 -0.04161 -0.09454 0.07729  46  ILE   A O     
377  C  CB    . ILE   A 47  ? 0.34192 0.34408 0.54800 -0.03733 -0.08731 0.05825  46  ILE   A CB    
378  C  CG1   . ILE   A 47  ? 0.34959 0.35105 0.54081 -0.03593 -0.08314 0.05321  46  ILE   A CG1   
379  C  CG2   . ILE   A 47  ? 0.36169 0.35327 0.55364 -0.03597 -0.09303 0.04951  46  ILE   A CG2   
380  C  CD1   . ILE   A 47  ? 0.30935 0.31569 0.48155 -0.03327 -0.07118 0.04806  46  ILE   A CD1   
381  N  N     . ASP   A 48  ? 0.48339 0.47171 0.73424 -0.04320 -0.11748 0.06886  47  ASP   A N     
382  C  CA    . ASP   A 48  ? 0.50097 0.48723 0.76790 -0.04493 -0.12506 0.07338  47  ASP   A CA    
383  C  C     . ASP   A 48  ? 0.44406 0.44366 0.73794 -0.04710 -0.12030 0.08739  47  ASP   A C     
384  O  O     . ASP   A 48  ? 0.52499 0.53191 0.82572 -0.04693 -0.11454 0.09220  47  ASP   A O     
385  C  CB    . ASP   A 48  ? 0.40018 0.38469 0.65249 -0.04298 -0.12138 0.06731  47  ASP   A CB    
386  C  CG    . ASP   A 48  ? 0.46348 0.43605 0.68881 -0.04005 -0.12425 0.05433  47  ASP   A CG    
387  O  OD1   . ASP   A 48  ? 0.50518 0.46709 0.72407 -0.03948 -0.13325 0.04932  47  ASP   A OD1   
388  O  OD2   . ASP   A 48  ? 0.50582 0.47961 0.71640 -0.03797 -0.11741 0.04938  47  ASP   A OD2   
389  N  N     . GLY   A 49  ? 0.51376 0.51694 0.82245 -0.04869 -0.12190 0.09425  48  GLY   A N     
390  C  CA    . GLY   A 49  ? 0.53820 0.55407 0.87355 -0.05023 -0.11741 0.10859  48  GLY   A CA    
391  C  C     . GLY   A 49  ? 0.51649 0.54724 0.84866 -0.04772 -0.10008 0.11380  48  GLY   A C     
392  O  O     . GLY   A 49  ? 0.50190 0.54346 0.85485 -0.04806 -0.09530 0.12613  48  GLY   A O     
393  N  N     . GLU   A 50  ? 0.46364 0.49514 0.77086 -0.04484 -0.09066 0.10523  49  GLU   A N     
394  C  CA    . GLU   A 50  ? 0.39377 0.43805 0.69691 -0.04190 -0.07513 0.10957  49  GLU   A CA    
395  C  C     . GLU   A 50  ? 0.42916 0.47596 0.71708 -0.03996 -0.06752 0.10571  49  GLU   A C     
396  O  O     . GLU   A 50  ? 0.46732 0.50651 0.73379 -0.03927 -0.06867 0.09455  49  GLU   A O     
397  C  CB    . GLU   A 50  ? 0.43884 0.48292 0.72755 -0.04002 -0.07001 0.10395  49  GLU   A CB    
398  C  CG    . GLU   A 50  ? 0.47996 0.53542 0.76228 -0.03648 -0.05503 0.10728  49  GLU   A CG    
399  C  CD    . GLU   A 50  ? 0.52521 0.58344 0.80760 -0.03534 -0.05144 0.10834  49  GLU   A CD    
400  O  OE1   . GLU   A 50  ? 0.66593 0.72478 0.96771 -0.03722 -0.05714 0.11537  49  GLU   A OE1   
401  O  OE2   . GLU   A 50  ? 0.59610 0.65559 0.85979 -0.03266 -0.04346 0.10224  49  GLU   A OE2   
402  N  N     . THR   A 51  ? 0.43200 0.48956 0.73111 -0.03873 -0.05953 0.11529  50  THR   A N     
403  C  CA    . THR   A 51  ? 0.41769 0.47855 0.70370 -0.03663 -0.05177 0.11269  50  THR   A CA    
404  C  C     . THR   A 51  ? 0.36587 0.42947 0.62972 -0.03308 -0.04099 0.10620  50  THR   A C     
405  O  O     . THR   A 51  ? 0.36500 0.43327 0.62963 -0.03133 -0.03555 0.10885  50  THR   A O     
406  C  CB    . THR   A 51  ? 0.37251 0.44420 0.67741 -0.03570 -0.04613 0.12560  50  THR   A CB    
407  O  OG1   . THR   A 51  ? 0.54324 0.61205 0.87062 -0.03936 -0.05714 0.13195  50  THR   A OG1   
408  C  CG2   . THR   A 51  ? 0.39693 0.47138 0.68951 -0.03364 -0.03927 0.12322  50  THR   A CG2   
409  N  N     . CYS   A 52  ? 0.32460 0.38470 0.56880 -0.03206 -0.03852 0.09750  51  CYS   A N     
410  C  CA    . CYS   A 52  ? 0.35982 0.42193 0.58366 -0.02887 -0.02920 0.09124  51  CYS   A CA    
411  C  C     . CYS   A 52  ? 0.27816 0.33905 0.48657 -0.02775 -0.02577 0.08537  51  CYS   A C     
412  O  O     . CYS   A 52  ? 0.31786 0.37492 0.52882 -0.02959 -0.03132 0.08446  51  CYS   A O     
413  C  CB    . CYS   A 52  ? 0.39384 0.44868 0.60556 -0.02935 -0.03276 0.08260  51  CYS   A CB    
414  S  SG    . CYS   A 52  ? 0.38629 0.42674 0.58626 -0.03170 -0.04462 0.07135  51  CYS   A SG    
415  N  N     . LEU   A 53  ? 0.25667 0.32102 0.44982 -0.02459 -0.01663 0.08187  52  LEU   A N     
416  C  CA    . LEU   A 53  ? 0.23606 0.30037 0.41458 -0.02305 -0.01212 0.07691  52  LEU   A CA    
417  C  C     . LEU   A 53  ? 0.24581 0.30306 0.40435 -0.02297 -0.01302 0.06550  52  LEU   A C     
418  O  O     . LEU   A 53  ? 0.25550 0.31312 0.40749 -0.02165 -0.00990 0.06304  52  LEU   A O     
419  C  CB    . LEU   A 53  ? 0.30072 0.37433 0.47780 -0.01887 -0.00113 0.08243  52  LEU   A CB    
420  C  CG    . LEU   A 53  ? 0.32853 0.40416 0.49433 -0.01658 0.00453  0.08024  52  LEU   A CG    
421  C  CD1   . LEU   A 53  ? 0.26022 0.33372 0.43131 -0.01894 -0.00032 0.08087  52  LEU   A CD1   
422  C  CD2   . LEU   A 53  ? 0.36285 0.44776 0.53309 -0.01186 0.01399  0.08887  52  LEU   A CD2   
423  N  N     . LEU   A 54  ? 0.24023 0.29112 0.38963 -0.02416 -0.01720 0.05898  53  LEU   A N     
424  C  CA    . LEU   A 54  ? 0.24163 0.28670 0.37204 -0.02344 -0.01683 0.04901  53  LEU   A CA    
425  C  C     . LEU   A 54  ? 0.24976 0.29898 0.36876 -0.02108 -0.00874 0.04706  53  LEU   A C     
426  O  O     . LEU   A 54  ? 0.25216 0.30324 0.37271 -0.02107 -0.00778 0.04895  53  LEU   A O     
427  C  CB    . LEU   A 54  ? 0.24781 0.28303 0.37299 -0.02517 -0.02561 0.04283  53  LEU   A CB    
428  C  CG    . LEU   A 54  ? 0.25342 0.28267 0.38998 -0.02738 -0.03565 0.04446  53  LEU   A CG    
429  C  CD1   . LEU   A 54  ? 0.31918 0.33737 0.44721 -0.02791 -0.04430 0.03748  53  LEU   A CD1   
430  C  CD2   . LEU   A 54  ? 0.26151 0.29082 0.40024 -0.02722 -0.03580 0.04480  53  LEU   A CD2   
431  N  N     . ASP   A 55  ? 0.23573 0.28619 0.34393 -0.01909 -0.00336 0.04347  54  ASP   A N     
432  C  CA    . ASP   A 55  ? 0.23428 0.28714 0.33021 -0.01679 0.00320  0.04038  54  ASP   A CA    
433  C  C     . ASP   A 55  ? 0.25433 0.30043 0.33636 -0.01727 0.00095  0.03149  54  ASP   A C     
434  O  O     . ASP   A 55  ? 0.27984 0.32368 0.35716 -0.01699 0.00074  0.02824  54  ASP   A O     
435  C  CB    . ASP   A 55  ? 0.32419 0.38296 0.41932 -0.01380 0.01026  0.04349  54  ASP   A CB    
436  C  CG    . ASP   A 55  ? 0.47545 0.53689 0.56000 -0.01088 0.01657  0.04173  54  ASP   A CG    
437  O  OD1   . ASP   A 55  ? 0.52559 0.58472 0.60302 -0.01140 0.01597  0.03776  54  ASP   A OD1   
438  O  OD2   . ASP   A 55  ? 0.54411 0.60972 0.62747 -0.00772 0.02195  0.04450  54  ASP   A OD2   
439  N  N     . ILE   A 56  ? 0.23678 0.27961 0.31269 -0.01780 -0.00078 0.02793  55  ILE   A N     
440  C  CA    . ILE   A 56  ? 0.24024 0.27614 0.30437 -0.01793 -0.00358 0.02045  55  ILE   A CA    
441  C  C     . ILE   A 56  ? 0.24574 0.28323 0.29839 -0.01630 0.00195  0.01679  55  ILE   A C     
442  O  O     . ILE   A 56  ? 0.29314 0.33361 0.34561 -0.01592 0.00448  0.01830  55  ILE   A O     
443  C  CB    . ILE   A 56  ? 0.24555 0.27504 0.31119 -0.01943 -0.01090 0.01897  55  ILE   A CB    
444  C  CG1   . ILE   A 56  ? 0.24977 0.27732 0.32825 -0.02113 -0.01730 0.02292  55  ILE   A CG1   
445  C  CG2   . ILE   A 56  ? 0.25066 0.27249 0.30291 -0.01847 -0.01344 0.01158  55  ILE   A CG2   
446  C  CD1   . ILE   A 56  ? 0.31877 0.34130 0.40172 -0.02251 -0.02435 0.02320  55  ILE   A CD1   
447  N  N     . LEU   A 57  ? 0.24343 0.27890 0.28715 -0.01530 0.00360  0.01226  56  LEU   A N     
448  C  CA    . LEU   A 57  ? 0.24811 0.28412 0.28169 -0.01396 0.00775  0.00857  56  LEU   A CA    
449  C  C     . LEU   A 57  ? 0.25459 0.28428 0.27998 -0.01390 0.00474  0.00350  56  LEU   A C     
450  O  O     . LEU   A 57  ? 0.25561 0.28081 0.27755 -0.01351 0.00227  0.00075  56  LEU   A O     
451  C  CB    . LEU   A 57  ? 0.25280 0.29113 0.28286 -0.01260 0.01182  0.00759  56  LEU   A CB    
452  C  CG    . LEU   A 57  ? 0.28300 0.32215 0.30454 -0.01130 0.01565  0.00450  56  LEU   A CG    
453  C  CD1   . LEU   A 57  ? 0.27540 0.31860 0.29798 -0.01052 0.01852  0.00702  56  LEU   A CD1   
454  C  CD2   . LEU   A 57  ? 0.30396 0.34422 0.32227 -0.01007 0.01849  0.00311  56  LEU   A CD2   
455  N  N     . ASP   A 58  ? 0.24413 0.27337 0.26585 -0.01379 0.00519  0.00241  57  ASP   A N     
456  C  CA    . ASP   A 58  ? 0.27258 0.29616 0.28592 -0.01301 0.00311  -0.00186 57  ASP   A CA    
457  C  C     . ASP   A 58  ? 0.28309 0.30846 0.28877 -0.01160 0.00813  -0.00434 57  ASP   A C     
458  O  O     . ASP   A 58  ? 0.29205 0.32152 0.29777 -0.01161 0.01152  -0.00331 57  ASP   A O     
459  C  CB    . ASP   A 58  ? 0.28904 0.31116 0.30418 -0.01380 0.00033  -0.00099 57  ASP   A CB    
460  C  CG    . ASP   A 58  ? 0.32546 0.34122 0.33146 -0.01240 -0.00200 -0.00513 57  ASP   A CG    
461  O  OD1   . ASP   A 58  ? 0.35262 0.36397 0.35208 -0.01070 -0.00284 -0.00818 57  ASP   A OD1   
462  O  OD2   . ASP   A 58  ? 0.32060 0.33566 0.32561 -0.01262 -0.00283 -0.00515 57  ASP   A OD2   
463  N  N     . THR   A 59  ? 0.26148 0.28390 0.26134 -0.01024 0.00852  -0.00721 58  THR   A N     
464  C  CA    . THR   A 59  ? 0.25614 0.28083 0.25119 -0.00907 0.01313  -0.00866 58  THR   A CA    
465  C  C     . THR   A 59  ? 0.27832 0.29997 0.26609 -0.00750 0.01371  -0.01104 58  THR   A C     
466  O  O     . THR   A 59  ? 0.31104 0.32772 0.29549 -0.00671 0.01041  -0.01229 58  THR   A O     
467  C  CB    . THR   A 59  ? 0.26957 0.29396 0.26370 -0.00833 0.01416  -0.00956 58  THR   A CB    
468  O  OG1   . THR   A 59  ? 0.26114 0.27952 0.25062 -0.00694 0.01113  -0.01180 58  THR   A OG1   
469  C  CG2   . THR   A 59  ? 0.30140 0.32879 0.30259 -0.00954 0.01381  -0.00697 58  THR   A CG2   
470  N  N     . ALA   A 60  ? 0.27271 0.29709 0.25815 -0.00674 0.01777  -0.01147 59  ALA   A N     
471  C  CA    . ALA   A 60  ? 0.28468 0.30717 0.26420 -0.00491 0.01933  -0.01288 59  ALA   A CA    
472  C  C     . ALA   A 60  ? 0.30852 0.32744 0.28295 -0.00241 0.01978  -0.01436 59  ALA   A C     
473  O  O     . ALA   A 60  ? 0.29031 0.31052 0.26635 -0.00238 0.02097  -0.01424 59  ALA   A O     
474  C  CB    . ALA   A 60  ? 0.28480 0.31192 0.26572 -0.00524 0.02309  -0.01202 59  ALA   A CB    
475  N  N     . GLY   A 61  ? 0.29698 0.31120 0.26480 0.00014  0.01897  -0.01564 60  GLY   A N     
476  C  CA    . GLY   A 61  ? 0.33067 0.34115 0.29221 0.00367  0.02001  -0.01670 60  GLY   A CA    
477  C  C     . GLY   A 61  ? 0.45161 0.46565 0.41285 0.00518  0.02531  -0.01542 60  GLY   A C     
478  O  O     . GLY   A 61  ? 0.42270 0.43475 0.38001 0.00823  0.02703  -0.01551 60  GLY   A O     
479  N  N     . GLN   A 62  ? 0.37073 0.38979 0.33645 0.00331  0.02768  -0.01397 61  GLN   A N     
480  C  CA    . GLN   A 62  ? 0.43627 0.45833 0.40279 0.00477  0.03203  -0.01224 61  GLN   A CA    
481  C  C     . GLN   A 62  ? 0.38926 0.41295 0.35814 0.00548  0.03416  -0.01142 61  GLN   A C     
482  O  O     . GLN   A 62  ? 0.38438 0.41070 0.35838 0.00301  0.03349  -0.01144 61  GLN   A O     
483  C  CB    . GLN   A 62  ? 0.43857 0.46552 0.41088 0.00213  0.03306  -0.01098 61  GLN   A CB    
484  C  CG    . GLN   A 62  ? 0.42752 0.45388 0.39874 0.00096  0.03124  -0.01148 61  GLN   A CG    
485  C  CD    . GLN   A 62  ? 0.43714 0.46040 0.40233 0.00387  0.03213  -0.01150 61  GLN   A CD    
486  O  OE1   . GLN   A 62  ? 0.48985 0.51368 0.45377 0.00649  0.03551  -0.00999 61  GLN   A OE1   
487  N  NE2   . GLN   A 62  ? 0.37071 0.39043 0.33224 0.00385  0.02909  -0.01288 61  GLN   A NE2   
488  N  N     . GLU   A 63  ? 0.42903 0.45106 0.39399 0.00927  0.03690  -0.01046 62  GLU   A N     
489  C  CA    . GLU   A 63  ? 0.46645 0.49015 0.43408 0.01013  0.03911  -0.00930 62  GLU   A CA    
490  C  C     . GLU   A 63  ? 0.41689 0.44641 0.39351 0.00770  0.04103  -0.00712 62  GLU   A C     
491  O  O     . GLU   A 63  ? 0.46214 0.49347 0.44300 0.00681  0.04139  -0.00669 62  GLU   A O     
492  C  CB    . GLU   A 63  ? 0.52853 0.54942 0.49004 0.01546  0.04222  -0.00799 62  GLU   A CB    
493  C  CG    . GLU   A 63  ? 0.58336 0.59805 0.53695 0.01817  0.03980  -0.01040 62  GLU   A CG    
494  C  CD    . GLU   A 63  ? 0.69074 0.70105 0.63529 0.02481  0.04255  -0.00942 62  GLU   A CD    
495  O  OE1   . GLU   A 63  ? 0.72103 0.73145 0.66290 0.02765  0.04532  -0.00756 62  GLU   A OE1   
496  O  OE2   . GLU   A 63  ? 0.71888 0.72545 0.65860 0.02760  0.04200  -0.01038 62  GLU   A OE2   
497  N  N     . GLU   A 64  ? 0.36234 0.39437 0.34203 0.00662  0.04171  -0.00587 63  GLU   A N     
498  C  CA    . GLU   A 64  ? 0.43028 0.46683 0.41862 0.00467  0.04260  -0.00385 63  GLU   A CA    
499  C  C     . GLU   A 64  ? 0.43609 0.47379 0.42810 0.00143  0.03965  -0.00549 63  GLU   A C     
500  O  O     . GLU   A 64  ? 0.40571 0.44587 0.40409 0.00031  0.03955  -0.00433 63  GLU   A O     
501  C  CB    . GLU   A 64  ? 0.48145 0.52006 0.47251 0.00439  0.04355  -0.00207 63  GLU   A CB    
502  C  CG    . GLU   A 64  ? 0.47956 0.51683 0.46693 0.00299  0.04129  -0.00407 63  GLU   A CG    
503  C  CD    . GLU   A 64  ? 0.54919 0.58759 0.53711 0.00375  0.04283  -0.00229 63  GLU   A CD    
504  O  OE1   . GLU   A 64  ? 0.56331 0.60465 0.55756 0.00187  0.04235  -0.00105 63  GLU   A OE1   
505  O  OE2   . GLU   A 64  ? 0.60073 0.63659 0.58238 0.00646  0.04417  -0.00224 63  GLU   A OE2   
506  N  N     . TYR   A 65  ? 0.40471 0.44047 0.39315 0.00026  0.03712  -0.00784 64  TYR   A N     
507  C  CA    . TYR   A 65  ? 0.37021 0.40700 0.36140 -0.00192 0.03494  -0.00886 64  TYR   A CA    
508  C  C     . TYR   A 65  ? 0.34426 0.37942 0.33395 -0.00168 0.03420  -0.00992 64  TYR   A C     
509  O  O     . TYR   A 65  ? 0.36638 0.40174 0.35695 -0.00304 0.03237  -0.01069 64  TYR   A O     
510  C  CB    . TYR   A 65  ? 0.36076 0.39759 0.35093 -0.00340 0.03299  -0.00964 64  TYR   A CB    
511  C  CG    . TYR   A 65  ? 0.34978 0.38803 0.34120 -0.00362 0.03355  -0.00874 64  TYR   A CG    
512  C  CD1   . TYR   A 65  ? 0.31462 0.35495 0.31072 -0.00422 0.03335  -0.00787 64  TYR   A CD1   
513  C  CD2   . TYR   A 65  ? 0.32262 0.35963 0.31059 -0.00306 0.03382  -0.00881 64  TYR   A CD2   
514  C  CE1   . TYR   A 65  ? 0.37800 0.41941 0.37584 -0.00444 0.03345  -0.00694 64  TYR   A CE1   
515  C  CE2   . TYR   A 65  ? 0.33060 0.36903 0.31996 -0.00325 0.03444  -0.00785 64  TYR   A CE2   
516  C  CZ    . TYR   A 65  ? 0.31313 0.35389 0.30768 -0.00405 0.03425  -0.00686 64  TYR   A CZ    
517  O  OH    . TYR   A 65  ? 0.26822 0.31016 0.26466 -0.00430 0.03440  -0.00584 64  TYR   A OH    
518  N  N     . SER   A 66  ? 0.37648 0.41016 0.36412 0.00038  0.03582  -0.00960 65  SER   A N     
519  C  CA    . SER   A 66  ? 0.44891 0.48057 0.43470 0.00087  0.03496  -0.01070 65  SER   A CA    
520  C  C     . SER   A 66  ? 0.42508 0.45896 0.41571 -0.00068 0.03451  -0.01063 65  SER   A C     
521  O  O     . SER   A 66  ? 0.51763 0.55031 0.50754 -0.00098 0.03325  -0.01160 65  SER   A O     
522  C  CB    . SER   A 66  ? 0.44760 0.47711 0.42964 0.00414  0.03716  -0.01012 65  SER   A CB    
523  O  OG    . SER   A 66  ? 0.46187 0.49440 0.44845 0.00496  0.04020  -0.00769 65  SER   A OG    
524  N  N     . ALA   A 67  ? 0.40297 0.43959 0.39844 -0.00153 0.03501  -0.00956 66  ALA   A N     
525  C  CA    . ALA   A 67  ? 0.43587 0.47370 0.43513 -0.00249 0.03401  -0.00972 66  ALA   A CA    
526  C  C     . ALA   A 67  ? 0.44904 0.48720 0.44813 -0.00367 0.03194  -0.01055 66  ALA   A C     
527  O  O     . ALA   A 67  ? 0.46736 0.50595 0.46838 -0.00379 0.03101  -0.01077 66  ALA   A O     
528  C  CB    . ALA   A 67  ? 0.47549 0.51512 0.48029 -0.00244 0.03457  -0.00815 66  ALA   A CB    
529  N  N     . MET   A 68  ? 0.44364 0.48147 0.44036 -0.00412 0.03129  -0.01077 67  MET   A N     
530  C  CA    . MET   A 68  ? 0.44928 0.48783 0.44607 -0.00466 0.02997  -0.01071 67  MET   A CA    
531  C  C     . MET   A 68  ? 0.43489 0.47268 0.43063 -0.00508 0.02910  -0.01064 67  MET   A C     
532  O  O     . MET   A 68  ? 0.44482 0.48346 0.44097 -0.00538 0.02843  -0.00978 67  MET   A O     
533  C  CB    . MET   A 68  ? 0.50026 0.53951 0.49659 -0.00488 0.02974  -0.01034 67  MET   A CB    
534  C  CG    . MET   A 68  ? 0.58892 0.62885 0.58722 -0.00449 0.02921  -0.01018 67  MET   A CG    
535  S  SD    . MET   A 68  ? 0.79354 0.83381 0.79385 -0.00459 0.03042  -0.00945 67  MET   A SD    
536  C  CE    . MET   A 68  ? 0.57520 0.61575 0.57836 -0.00450 0.02836  -0.00919 67  MET   A CE    
537  N  N     . ARG   A 69  ? 0.40708 0.44314 0.40187 -0.00494 0.02890  -0.01123 68  ARG   A N     
538  C  CA    . ARG   A 69  ? 0.37125 0.40598 0.36610 -0.00546 0.02715  -0.01104 68  ARG   A CA    
539  C  C     . ARG   A 69  ? 0.37801 0.41381 0.37555 -0.00561 0.02685  -0.01031 68  ARG   A C     
540  O  O     . ARG   A 69  ? 0.34849 0.38394 0.34796 -0.00620 0.02530  -0.00931 68  ARG   A O     
541  C  CB    . ARG   A 69  ? 0.33813 0.36929 0.32967 -0.00471 0.02628  -0.01226 68  ARG   A CB    
542  C  CG    . ARG   A 69  ? 0.43178 0.46130 0.41968 -0.00382 0.02668  -0.01278 68  ARG   A CG    
543  C  CD    . ARG   A 69  ? 0.39904 0.42405 0.38188 -0.00184 0.02585  -0.01405 68  ARG   A CD    
544  N  NE    . ARG   A 69  ? 0.39179 0.41510 0.37032 -0.00016 0.02678  -0.01428 68  ARG   A NE    
545  C  CZ    . ARG   A 69  ? 0.41201 0.43262 0.38554 0.00283  0.02825  -0.01466 68  ARG   A CZ    
546  N  NH1   . ARG   A 69  ? 0.40224 0.42165 0.37451 0.00437  0.02903  -0.01493 68  ARG   A NH1   
547  N  NH2   . ARG   A 69  ? 0.47426 0.49349 0.44383 0.00472  0.02934  -0.01446 68  ARG   A NH2   
548  N  N     . ASP   A 70  ? 0.39448 0.43141 0.39273 -0.00502 0.02803  -0.01055 69  ASP   A N     
549  C  CA    . ASP   A 70  ? 0.40014 0.43744 0.40013 -0.00482 0.02784  -0.01013 69  ASP   A CA    
550  C  C     . ASP   A 70  ? 0.36269 0.40179 0.36497 -0.00465 0.02759  -0.00799 69  ASP   A C     
551  O  O     . ASP   A 70  ? 0.37479 0.41400 0.37946 -0.00491 0.02691  -0.00683 69  ASP   A O     
552  C  CB    . ASP   A 70  ? 0.39060 0.42834 0.39081 -0.00401 0.02877  -0.01084 69  ASP   A CB    
553  C  CG    . ASP   A 70  ? 0.49183 0.52835 0.49134 -0.00392 0.02947  -0.01196 69  ASP   A CG    
554  O  OD1   . ASP   A 70  ? 0.43749 0.47276 0.43506 -0.00391 0.02966  -0.01228 69  ASP   A OD1   
555  O  OD2   . ASP   A 70  ? 0.50136 0.53804 0.50218 -0.00348 0.02989  -0.01227 69  ASP   A OD2   
556  N  N     . GLN   A 71  ? 0.33694 0.37751 0.33880 -0.00388 0.02824  -0.00703 70  GLN   A N     
557  C  CA    . GLN   A 71  ? 0.41006 0.45259 0.41387 -0.00277 0.02877  -0.00430 70  GLN   A CA    
558  C  C     . GLN   A 71  ? 0.37912 0.42217 0.38660 -0.00412 0.02769  -0.00221 70  GLN   A C     
559  O  O     . GLN   A 71  ? 0.34222 0.38662 0.35365 -0.00386 0.02769  0.00043  70  GLN   A O     
560  C  CB    . GLN   A 71  ? 0.42302 0.46645 0.42461 -0.00092 0.02964  -0.00367 70  GLN   A CB    
561  C  CG    . GLN   A 71  ? 0.40980 0.45529 0.41266 0.00142  0.03096  -0.00025 70  GLN   A CG    
562  C  CD    . GLN   A 71  ? 0.55144 0.59707 0.55488 0.00293  0.03163  0.00049  70  GLN   A CD    
563  O  OE1   . GLN   A 71  ? 0.60967 0.65361 0.61008 0.00410  0.03136  -0.00166 70  GLN   A OE1   
564  N  NE2   . GLN   A 71  ? 0.52079 0.56838 0.52881 0.00291  0.03227  0.00378  70  GLN   A NE2   
565  N  N     . TYR   A 72  ? 0.35415 0.39588 0.36093 -0.00549 0.02643  -0.00314 71  TYR   A N     
566  C  CA    . TYR   A 72  ? 0.31451 0.35613 0.32550 -0.00670 0.02450  -0.00103 71  TYR   A CA    
567  C  C     . TYR   A 72  ? 0.32564 0.36496 0.33862 -0.00768 0.02220  -0.00155 71  TYR   A C     
568  O  O     . TYR   A 72  ? 0.32142 0.36108 0.34003 -0.00846 0.02032  0.00108  71  TYR   A O     
569  C  CB    . TYR   A 72  ? 0.33818 0.37853 0.34766 -0.00759 0.02331  -0.00180 71  TYR   A CB    
570  C  CG    . TYR   A 72  ? 0.30004 0.33660 0.30513 -0.00811 0.02185  -0.00503 71  TYR   A CG    
571  C  CD1   . TYR   A 72  ? 0.31999 0.35296 0.32476 -0.00849 0.01918  -0.00621 71  TYR   A CD1   
572  C  CD2   . TYR   A 72  ? 0.37431 0.41051 0.37532 -0.00775 0.02299  -0.00663 71  TYR   A CD2   
573  C  CE1   . TYR   A 72  ? 0.39729 0.42619 0.39667 -0.00787 0.01806  -0.00891 71  TYR   A CE1   
574  C  CE2   . TYR   A 72  ? 0.32837 0.36113 0.32501 -0.00744 0.02219  -0.00896 71  TYR   A CE2   
575  C  CZ    . TYR   A 72  ? 0.34740 0.37640 0.34267 -0.00718 0.01991  -0.01009 71  TYR   A CZ    
576  O  OH    . TYR   A 72  ? 0.42499 0.44997 0.41458 -0.00577 0.01932  -0.01220 71  TYR   A OH    
577  N  N     . MET   A 73  ? 0.31807 0.35512 0.32714 -0.00745 0.02226  -0.00451 72  MET   A N     
578  C  CA    . MET   A 73  ? 0.31826 0.35287 0.32844 -0.00788 0.02015  -0.00515 72  MET   A CA    
579  C  C     . MET   A 73  ? 0.34599 0.38314 0.36073 -0.00762 0.02100  -0.00276 72  MET   A C     
580  O  O     . MET   A 73  ? 0.33176 0.36817 0.35115 -0.00843 0.01862  -0.00115 72  MET   A O     
581  C  CB    . MET   A 73  ? 0.36571 0.39754 0.37028 -0.00713 0.02063  -0.00846 72  MET   A CB    
582  C  CG    . MET   A 73  ? 0.35120 0.37985 0.35116 -0.00676 0.01959  -0.01030 72  MET   A CG    
583  S  SD    . MET   A 73  ? 0.36874 0.39446 0.36243 -0.00489 0.02095  -0.01303 72  MET   A SD    
584  C  CE    . MET   A 73  ? 0.38628 0.40766 0.37448 -0.00369 0.01923  -0.01435 72  MET   A CE    
585  N  N     . ARG   A 74  ? 0.31728 0.35704 0.33084 -0.00626 0.02400  -0.00241 73  ARG   A N     
586  C  CA    . ARG   A 74  ? 0.37268 0.41487 0.38991 -0.00527 0.02519  0.00030  73  ARG   A CA    
587  C  C     . ARG   A 74  ? 0.35093 0.39564 0.37467 -0.00535 0.02489  0.00488  73  ARG   A C     
588  O  O     . ARG   A 74  ? 0.34164 0.38726 0.37110 -0.00566 0.02404  0.00760  73  ARG   A O     
589  C  CB    . ARG   A 74  ? 0.40999 0.45365 0.42368 -0.00300 0.02796  -0.00012 73  ARG   A CB    
590  C  CG    . ARG   A 74  ? 0.50358 0.54532 0.51344 -0.00288 0.02812  -0.00354 73  ARG   A CG    
591  C  CD    . ARG   A 74  ? 0.43847 0.48073 0.44527 -0.00047 0.02968  -0.00395 73  ARG   A CD    
592  N  NE    . ARG   A 74  ? 0.60347 0.64391 0.60762 -0.00087 0.02929  -0.00703 73  ARG   A NE    
593  C  CZ    . ARG   A 74  ? 0.51213 0.55205 0.51426 -0.00069 0.02918  -0.00820 73  ARG   A CZ    
594  N  NH1   . ARG   A 74  ? 0.52966 0.57039 0.53082 0.00017  0.02942  -0.00710 73  ARG   A NH1   
595  N  NH2   . ARG   A 74  ? 0.64055 0.67924 0.64218 -0.00124 0.02886  -0.01016 73  ARG   A NH2   
596  N  N     . THR   A 75  ? 0.33241 0.37841 0.35614 -0.00509 0.02552  0.00616  74  THR   A N     
597  C  CA    . THR   A 75  ? 0.34006 0.38919 0.37065 -0.00469 0.02593  0.01136  74  THR   A CA    
598  C  C     . THR   A 75  ? 0.37597 0.42363 0.41349 -0.00727 0.02186  0.01289  74  THR   A C     
599  O  O     . THR   A 75  ? 0.38069 0.43088 0.42677 -0.00732 0.02150  0.01788  74  THR   A O     
600  C  CB    . THR   A 75  ? 0.42625 0.47699 0.45452 -0.00345 0.02775  0.01225  74  THR   A CB    
601  O  OG1   . THR   A 75  ? 0.44824 0.49921 0.46977 -0.00082 0.03044  0.01049  74  THR   A OG1   
602  C  CG2   . THR   A 75  ? 0.41585 0.47041 0.45154 -0.00241 0.02894  0.01842  74  THR   A CG2   
603  N  N     . GLY   A 76  ? 0.35178 0.39509 0.38595 -0.00903 0.01855  0.00899  75  GLY   A N     
604  C  CA    . GLY   A 76  ? 0.30083 0.34139 0.34052 -0.01101 0.01364  0.01001  75  GLY   A CA    
605  C  C     . GLY   A 76  ? 0.34203 0.38122 0.38727 -0.01182 0.01076  0.01122  75  GLY   A C     
606  O  O     . GLY   A 76  ? 0.33555 0.37381 0.37715 -0.01122 0.01170  0.00895  75  GLY   A O     
607  N  N     . GLU   A 77  ? 0.29383 0.33283 0.34880 -0.01327 0.00686  0.01508  76  GLU   A N     
608  C  CA    . GLU   A 77  ? 0.29334 0.33049 0.35485 -0.01428 0.00305  0.01649  76  GLU   A CA    
609  C  C     . GLU   A 77  ? 0.35487 0.38416 0.41325 -0.01537 -0.00371 0.01226  76  GLU   A C     
610  O  O     . GLU   A 77  ? 0.31923 0.34544 0.37817 -0.01557 -0.00657 0.01105  76  GLU   A O     
611  C  CB    . GLU   A 77  ? 0.31617 0.35740 0.39197 -0.01510 0.00199  0.02391  76  GLU   A CB    
612  C  CG    . GLU   A 77  ? 0.37785 0.42644 0.45715 -0.01299 0.00859  0.02904  76  GLU   A CG    
613  C  CD    . GLU   A 77  ? 0.45905 0.51209 0.55345 -0.01339 0.00795  0.03741  76  GLU   A CD    
614  O  OE1   . GLU   A 77  ? 0.38280 0.43510 0.48299 -0.01489 0.00465  0.03940  76  GLU   A OE1   
615  O  OE2   . GLU   A 77  ? 0.62131 0.67861 0.72243 -0.01209 0.01070  0.04240  76  GLU   A OE2   
616  N  N     . GLY   A 78  ? 0.30021 0.32568 0.35501 -0.01570 -0.00663 0.01006  77  GLY   A N     
617  C  CA    . GLY   A 78  ? 0.28439 0.30132 0.33407 -0.01563 -0.01312 0.00573  77  GLY   A CA    
618  C  C     . GLY   A 78  ? 0.28171 0.29556 0.32125 -0.01450 -0.01253 0.00173  77  GLY   A C     
619  O  O     . GLY   A 78  ? 0.26076 0.27873 0.30083 -0.01473 -0.00912 0.00326  77  GLY   A O     
620  N  N     . PHE   A 79  ? 0.26917 0.27565 0.29907 -0.01285 -0.01567 -0.00323 78  PHE   A N     
621  C  CA    . PHE   A 79  ? 0.27389 0.27759 0.29311 -0.01104 -0.01416 -0.00692 78  PHE   A CA    
622  C  C     . PHE   A 79  ? 0.30480 0.29914 0.31925 -0.00973 -0.02145 -0.00975 78  PHE   A C     
623  O  O     . PHE   A 79  ? 0.29128 0.27892 0.30331 -0.00851 -0.02666 -0.01178 78  PHE   A O     
624  C  CB    . PHE   A 79  ? 0.29012 0.29448 0.30003 -0.00896 -0.00899 -0.01003 78  PHE   A CB    
625  C  CG    . PHE   A 79  ? 0.26222 0.27466 0.27587 -0.00989 -0.00263 -0.00772 78  PHE   A CG    
626  C  CD1   . PHE   A 79  ? 0.27591 0.29127 0.29605 -0.01083 -0.00219 -0.00541 78  PHE   A CD1   
627  C  CD2   . PHE   A 79  ? 0.27638 0.29314 0.28749 -0.00967 0.00235  -0.00759 78  PHE   A CD2   
628  C  CE1   . PHE   A 79  ? 0.27980 0.30198 0.30262 -0.01103 0.00342  -0.00325 78  PHE   A CE1   
629  C  CE2   . PHE   A 79  ? 0.25134 0.27443 0.26527 -0.01000 0.00731  -0.00564 78  PHE   A CE2   
630  C  CZ    . PHE   A 79  ? 0.29065 0.31628 0.31006 -0.01048 0.00784  -0.00349 78  PHE   A CZ    
631  N  N     . LEU   A 80  ? 0.27983 0.27307 0.29210 -0.00959 -0.02211 -0.01011 79  LEU   A N     
632  C  CA    . LEU   A 80  ? 0.29083 0.27445 0.29591 -0.00745 -0.02858 -0.01342 79  LEU   A CA    
633  C  C     . LEU   A 80  ? 0.29804 0.27977 0.28926 -0.00391 -0.02399 -0.01727 79  LEU   A C     
634  O  O     . LEU   A 80  ? 0.32418 0.31108 0.31356 -0.00410 -0.01828 -0.01677 79  LEU   A O     
635  C  CB    . LEU   A 80  ? 0.29842 0.28188 0.30923 -0.00915 -0.03190 -0.01139 79  LEU   A CB    
636  C  CG    . LEU   A 80  ? 0.37972 0.35401 0.39278 -0.00898 -0.04211 -0.01207 79  LEU   A CG    
637  C  CD1   . LEU   A 80  ? 0.32337 0.29674 0.34728 -0.01089 -0.04737 -0.00949 79  LEU   A CD1   
638  C  CD2   . LEU   A 80  ? 0.33276 0.30903 0.35221 -0.01095 -0.04352 -0.00949 79  LEU   A CD2   
639  N  N     . CYS   A 81  ? 0.31587 0.29040 0.29776 -0.00043 -0.02629 -0.02069 80  CYS   A N     
640  C  CA    . CYS   A 81  ? 0.32000 0.29288 0.28927 0.00363  -0.02148 -0.02353 80  CYS   A CA    
641  C  C     . CYS   A 81  ? 0.31018 0.27363 0.26910 0.00756  -0.02608 -0.02647 80  CYS   A C     
642  O  O     . CYS   A 81  ? 0.32107 0.27479 0.27411 0.01056  -0.03285 -0.02900 80  CYS   A O     
643  C  CB    . CYS   A 81  ? 0.31642 0.28759 0.28113 0.00586  -0.02013 -0.02500 80  CYS   A CB    
644  S  SG    . CYS   A 81  ? 0.37059 0.35244 0.34586 0.00189  -0.01430 -0.02185 80  CYS   A SG    
645  N  N     . VAL   A 82  ? 0.30835 0.27409 0.26444 0.00794  -0.02271 -0.02626 81  VAL   A N     
646  C  CA    . VAL   A 82  ? 0.31810 0.27566 0.26608 0.01107  -0.02729 -0.02846 81  VAL   A CA    
647  C  C     . VAL   A 82  ? 0.32660 0.28090 0.26049 0.01687  -0.02279 -0.03063 81  VAL   A C     
648  O  O     . VAL   A 82  ? 0.32696 0.28865 0.26082 0.01667  -0.01479 -0.02919 81  VAL   A O     
649  C  CB    . VAL   A 82  ? 0.31214 0.27426 0.26723 0.00758  -0.02705 -0.02635 81  VAL   A CB    
650  C  CG1   . VAL   A 82  ? 0.32276 0.27556 0.27083 0.01038  -0.03337 -0.02863 81  VAL   A CG1   
651  C  CG2   . VAL   A 82  ? 0.30476 0.27255 0.27532 0.00203  -0.02927 -0.02278 81  VAL   A CG2   
652  N  N     . PHE   A 83  ? 0.33853 0.28152 0.26073 0.02232  -0.02819 -0.03376 82  PHE   A N     
653  C  CA    . PHE   A 83  ? 0.35488 0.29389 0.26312 0.02871  -0.02436 -0.03526 82  PHE   A CA    
654  C  C     . PHE   A 83  ? 0.35810 0.28695 0.25874 0.03186  -0.03152 -0.03765 82  PHE   A C     
655  O  O     . PHE   A 83  ? 0.36064 0.28487 0.26685 0.02927  -0.03998 -0.03834 82  PHE   A O     
656  C  CB    . PHE   A 83  ? 0.35441 0.28883 0.25256 0.03439  -0.02260 -0.03671 82  PHE   A CB    
657  C  CG    . PHE   A 83  ? 0.36864 0.29013 0.25920 0.03828  -0.03221 -0.04010 82  PHE   A CG    
658  C  CD1   . PHE   A 83  ? 0.37314 0.29400 0.27224 0.03453  -0.03770 -0.04019 82  PHE   A CD1   
659  C  CD2   . PHE   A 83  ? 0.38611 0.29570 0.26089 0.04601  -0.03604 -0.04309 82  PHE   A CD2   
660  C  CE1   . PHE   A 83  ? 0.38545 0.29370 0.27797 0.03815  -0.04746 -0.04337 82  PHE   A CE1   
661  C  CE2   . PHE   A 83  ? 0.44082 0.33708 0.30774 0.05012  -0.04601 -0.04660 82  PHE   A CE2   
662  C  CZ    . PHE   A 83  ? 0.39673 0.29258 0.27319 0.04584  -0.05184 -0.04671 82  PHE   A CZ    
663  N  N     . ALA   A 84  ? 0.37513 0.30066 0.26392 0.03743  -0.02825 -0.03854 83  ALA   A N     
664  C  CA    . ALA   A 84  ? 0.38496 0.30015 0.26472 0.04132  -0.03477 -0.04104 83  ALA   A CA    
665  C  C     . ALA   A 84  ? 0.49463 0.39664 0.35673 0.05059  -0.03838 -0.04442 83  ALA   A C     
666  O  O     . ALA   A 84  ? 0.42252 0.32573 0.27626 0.05566  -0.03136 -0.04380 83  ALA   A O     
667  C  CB    . ALA   A 84  ? 0.41601 0.33611 0.29419 0.04159  -0.02886 -0.03955 83  ALA   A CB    
668  N  N     . ILE   A 85  ? 0.45930 0.34843 0.31584 0.05315  -0.04955 -0.04778 84  ILE   A N     
669  C  CA    . ILE   A 85  ? 0.55499 0.43029 0.39425 0.06233  -0.05424 -0.05136 84  ILE   A CA    
670  C  C     . ILE   A 85  ? 0.52856 0.39850 0.35007 0.07157  -0.04950 -0.05217 84  ILE   A C     
671  O  O     . ILE   A 85  ? 0.57262 0.43188 0.37788 0.08062  -0.05121 -0.05456 84  ILE   A O     
672  C  CB    . ILE   A 85  ? 0.52178 0.38325 0.35953 0.06305  -0.06881 -0.05497 84  ILE   A CB    
673  C  CG1   . ILE   A 85  ? 0.55151 0.40879 0.39033 0.06187  -0.07462 -0.05576 84  ILE   A CG1   
674  C  CG2   . ILE   A 85  ? 0.51468 0.38057 0.36899 0.05541  -0.07327 -0.05369 84  ILE   A CG2   
675  C  CD1   . ILE   A 85  ? 0.67336 0.51643 0.49129 0.07211  -0.07827 -0.05941 84  ILE   A CD1   
676  N  N     . ASN   A 86  ? 0.51861 0.39539 0.34242 0.07003  -0.04356 -0.05004 85  ASN   A N     
677  C  CA    . ASN   A 86  ? 0.56048 0.43437 0.36935 0.07844  -0.03738 -0.04967 85  ASN   A CA    
678  C  C     . ASN   A 86  ? 0.54876 0.43643 0.36250 0.07745  -0.02391 -0.04502 85  ASN   A C     
679  O  O     . ASN   A 86  ? 0.62728 0.51711 0.43539 0.08124  -0.01762 -0.04315 85  ASN   A O     
680  C  CB    . ASN   A 86  ? 0.54163 0.41188 0.34831 0.07845  -0.04096 -0.05063 85  ASN   A CB    
681  C  CG    . ASN   A 86  ? 0.51029 0.39466 0.33481 0.06850  -0.03650 -0.04735 85  ASN   A CG    
682  O  OD1   . ASN   A 86  ? 0.52535 0.41991 0.36507 0.06069  -0.03431 -0.04522 85  ASN   A OD1   
683  N  ND2   . ASN   A 86  ? 0.58225 0.46684 0.40443 0.06913  -0.03533 -0.04698 85  ASN   A ND2   
684  N  N     . ASN   A 87  ? 0.49910 0.39616 0.32408 0.07224  -0.01972 -0.04291 86  ASN   A N     
685  C  CA    . ASN   A 87  ? 0.49872 0.40927 0.33135 0.06996  -0.00817 -0.03838 86  ASN   A CA    
686  C  C     . ASN   A 87  ? 0.49942 0.41215 0.33374 0.07038  -0.00573 -0.03770 86  ASN   A C     
687  O  O     . ASN   A 87  ? 0.46648 0.38572 0.31383 0.06296  -0.00675 -0.03722 86  ASN   A O     
688  C  CB    . ASN   A 87  ? 0.48542 0.40793 0.33503 0.06014  -0.00592 -0.03611 86  ASN   A CB    
689  C  CG    . ASN   A 87  ? 0.53597 0.47174 0.39455 0.05732  0.00463  -0.03165 86  ASN   A CG    
690  O  OD1   . ASN   A 87  ? 0.54434 0.48218 0.40057 0.06066  0.00993  -0.02993 86  ASN   A OD1   
691  N  ND2   . ASN   A 87  ? 0.56800 0.51272 0.43790 0.05080  0.00704  -0.02973 86  ASN   A ND2   
692  N  N     A THR   A 88  ? 0.54045 0.44778 0.36113 0.07962  -0.00205 -0.03736 87  THR   A N     
693  N  N     B THR   A 88  ? 0.54043 0.44782 0.36115 0.07960  -0.00201 -0.03734 87  THR   A N     
694  C  CA    A THR   A 88  ? 0.50606 0.41467 0.32665 0.08120  0.00058  -0.03663 87  THR   A CA    
695  C  CA    B THR   A 88  ? 0.50605 0.41466 0.32665 0.08119  0.00058  -0.03663 87  THR   A CA    
696  C  C     A THR   A 88  ? 0.48842 0.41208 0.32524 0.07394  0.00849  -0.03250 87  THR   A C     
697  C  C     B THR   A 88  ? 0.48842 0.41210 0.32530 0.07389  0.00847  -0.03250 87  THR   A C     
698  O  O     A THR   A 88  ? 0.48845 0.41511 0.33183 0.07052  0.00800  -0.03258 87  THR   A O     
699  O  O     B THR   A 88  ? 0.48840 0.41511 0.33186 0.07048  0.00801  -0.03257 87  THR   A O     
700  C  CB    A THR   A 88  ? 0.53764 0.43905 0.34072 0.09321  0.00494  -0.03585 87  THR   A CB    
701  C  CB    B THR   A 88  ? 0.53763 0.43910 0.34077 0.09318  0.00497  -0.03583 87  THR   A CB    
702  O  OG1   A THR   A 88  ? 0.59069 0.47751 0.37739 0.10067  -0.00240 -0.03975 87  THR   A OG1   
703  O  OG1   B THR   A 88  ? 0.54611 0.45433 0.34909 0.09581  0.01419  -0.03147 87  THR   A OG1   
704  C  CG2   A THR   A 88  ? 0.52332 0.42327 0.32403 0.09580  0.00574  -0.03596 87  THR   A CG2   
705  C  CG2   B THR   A 88  ? 0.59469 0.47942 0.38016 0.10115  -0.00408 -0.04059 87  THR   A CG2   
706  N  N     . LYS   A 89  ? 0.47725 0.41005 0.32074 0.07157  0.01530  -0.02897 88  LYS   A N     
707  C  CA    . LYS   A 89  ? 0.49269 0.43880 0.35147 0.06489  0.02178  -0.02527 88  LYS   A CA    
708  C  C     . LYS   A 89  ? 0.49210 0.44266 0.36417 0.05528  0.01680  -0.02682 88  LYS   A C     
709  O  O     . LYS   A 89  ? 0.48033 0.43765 0.36180 0.05100  0.01910  -0.02548 88  LYS   A O     
710  C  CB    . LYS   A 89  ? 0.51863 0.47227 0.38165 0.06448  0.02867  -0.02143 88  LYS   A CB    
711  C  CG    . LYS   A 89  ? 0.56314 0.52962 0.44276 0.05673  0.03344  -0.01817 88  LYS   A CG    
712  C  CD    . LYS   A 89  ? 0.58702 0.55913 0.47077 0.05822  0.03986  -0.01465 88  LYS   A CD    
713  C  CE    . LYS   A 89  ? 0.60378 0.58742 0.50122 0.05342  0.04583  -0.01027 88  LYS   A CE    
714  N  NZ    . LYS   A 89  ? 0.65705 0.64593 0.56595 0.04442  0.04231  -0.01173 88  LYS   A NZ    
715  N  N     . SER   A 90  ? 0.46836 0.41493 0.34132 0.05221  0.00988  -0.02939 89  SER   A N     
716  C  CA    . SER   A 90  ? 0.44097 0.39208 0.32696 0.04374  0.00567  -0.02998 89  SER   A CA    
717  C  C     . SER   A 90  ? 0.43386 0.38079 0.31994 0.04349  0.00101  -0.03186 89  SER   A C     
718  O  O     . SER   A 90  ? 0.42084 0.37417 0.31851 0.03731  0.00084  -0.03096 89  SER   A O     
719  C  CB    . SER   A 90  ? 0.38375 0.33165 0.27168 0.04076  -0.00068 -0.03160 89  SER   A CB    
720  O  OG    . SER   A 90  ? 0.41186 0.34717 0.28968 0.04510  -0.00904 -0.03511 89  SER   A OG    
721  N  N     . PHE   A 91  ? 0.42118 0.35712 0.29400 0.05057  -0.00283 -0.03440 90  PHE   A N     
722  C  CA    . PHE   A 91  ? 0.45154 0.38277 0.32331 0.05114  -0.00728 -0.03624 90  PHE   A CA    
723  C  C     . PHE   A 91  ? 0.47837 0.41711 0.35387 0.05098  0.00022  -0.03376 90  PHE   A C     
724  O  O     . PHE   A 91  ? 0.49663 0.43874 0.38046 0.04650  -0.00115 -0.03373 90  PHE   A O     
725  C  CB    . PHE   A 91  ? 0.42829 0.34483 0.28342 0.05964  -0.01358 -0.03978 90  PHE   A CB    
726  C  CG    . PHE   A 91  ? 0.53599 0.44608 0.38934 0.06052  -0.01963 -0.04212 90  PHE   A CG    
727  C  CD1   . PHE   A 91  ? 0.45680 0.36646 0.32088 0.05399  -0.02732 -0.04322 90  PHE   A CD1   
728  C  CD2   . PHE   A 91  ? 0.52224 0.42691 0.36366 0.06809  -0.01743 -0.04278 90  PHE   A CD2   
729  C  CE1   . PHE   A 91  ? 0.50515 0.40887 0.36833 0.05468  -0.03317 -0.04516 90  PHE   A CE1   
730  C  CE2   . PHE   A 91  ? 0.53868 0.43718 0.37833 0.06891  -0.02326 -0.04506 90  PHE   A CE2   
731  C  CZ    . PHE   A 91  ? 0.57819 0.47608 0.42880 0.06207  -0.03135 -0.04637 90  PHE   A CZ    
732  N  N     . GLU   A 92  ? 0.54570 0.48751 0.41608 0.05576  0.00826  -0.03122 91  GLU   A N     
733  C  CA    . GLU   A 92  ? 0.51049 0.46038 0.38650 0.05511  0.01557  -0.02817 91  GLU   A CA    
734  C  C     . GLU   A 92  ? 0.49001 0.45129 0.38255 0.04605  0.01778  -0.02621 91  GLU   A C     
735  O  O     . GLU   A 92  ? 0.54546 0.51124 0.44495 0.04297  0.01904  -0.02551 91  GLU   A O     
736  C  CB    . GLU   A 92  ? 0.53457 0.48655 0.40445 0.06156  0.02388  -0.02473 91  GLU   A CB    
737  C  CG    . GLU   A 92  ? 0.61084 0.55153 0.46275 0.07202  0.02288  -0.02609 91  GLU   A CG    
738  C  CD    . GLU   A 92  ? 0.67616 0.61955 0.52297 0.07837  0.03136  -0.02186 91  GLU   A CD    
739  O  OE1   . GLU   A 92  ? 0.72488 0.67939 0.58330 0.07464  0.03836  -0.01747 91  GLU   A OE1   
740  O  OE2   . GLU   A 92  ? 0.73636 0.67045 0.56769 0.08734  0.03077  -0.02273 91  GLU   A OE2   
741  N  N     . ASP   A 93  ? 0.53807 0.50367 0.43642 0.04209  0.01812  -0.02539 92  ASP   A N     
742  C  CA    . ASP   A 93  ? 0.50274 0.47823 0.41529 0.03438  0.01995  -0.02364 92  ASP   A CA    
743  C  C     . ASP   A 93  ? 0.50074 0.47598 0.41996 0.02940  0.01439  -0.02531 92  ASP   A C     
744  O  O     . ASP   A 93  ? 0.43113 0.41383 0.36054 0.02446  0.01647  -0.02381 92  ASP   A O     
745  C  CB    . ASP   A 93  ? 0.51895 0.49786 0.43515 0.03166  0.02057  -0.02275 92  ASP   A CB    
746  C  CG    . ASP   A 93  ? 0.62595 0.60612 0.53717 0.03625  0.02648  -0.02042 92  ASP   A CG    
747  O  OD1   . ASP   A 93  ? 0.62082 0.60296 0.53041 0.03994  0.03191  -0.01810 92  ASP   A OD1   
748  O  OD2   . ASP   A 93  ? 0.63274 0.61198 0.54206 0.03637  0.02579  -0.02055 92  ASP   A OD2   
749  N  N     . ILE   A 94  ? 0.53835 0.50473 0.45193 0.03109  0.00723  -0.02816 93  ILE   A N     
750  C  CA    . ILE   A 94  ? 0.53550 0.50150 0.45663 0.02642  0.00147  -0.02910 93  ILE   A CA    
751  C  C     . ILE   A 94  ? 0.50294 0.47250 0.42814 0.02529  0.00380  -0.02842 93  ILE   A C     
752  O  O     . ILE   A 94  ? 0.46545 0.44074 0.40115 0.01997  0.00351  -0.02728 93  ILE   A O     
753  C  CB    . ILE   A 94  ? 0.51929 0.47391 0.43349 0.02911  -0.00748 -0.03217 93  ILE   A CB    
754  C  CG1   . ILE   A 94  ? 0.53069 0.48508 0.44963 0.02579  -0.01159 -0.03208 93  ILE   A CG1   
755  C  CG2   . ILE   A 94  ? 0.54739 0.49930 0.46565 0.02731  -0.01271 -0.03316 93  ILE   A CG2   
756  C  CD1   . ILE   A 94  ? 0.39376 0.35846 0.32761 0.01848  -0.00952 -0.02929 93  ILE   A CD1   
757  N  N     A HIS   A 95  ? 0.50804 0.47416 0.42473 0.03069  0.00630  -0.02890 94  HIS   A N     
758  N  N     B HIS   A 95  ? 0.50803 0.47420 0.42479 0.03066  0.00633  -0.02889 94  HIS   A N     
759  C  CA    A HIS   A 95  ? 0.49817 0.46746 0.41827 0.02997  0.00869  -0.02824 94  HIS   A CA    
760  C  CA    B HIS   A 95  ? 0.49770 0.46715 0.41825 0.02970  0.00855  -0.02824 94  HIS   A CA    
761  C  C     A HIS   A 95  ? 0.47663 0.45694 0.40796 0.02500  0.01446  -0.02539 94  HIS   A C     
762  C  C     B HIS   A 95  ? 0.47652 0.45697 0.40806 0.02489  0.01447  -0.02536 94  HIS   A C     
763  O  O     A HIS   A 95  ? 0.46164 0.44589 0.40042 0.02134  0.01432  -0.02493 94  HIS   A O     
764  O  O     B HIS   A 95  ? 0.46133 0.44584 0.40036 0.02123  0.01446  -0.02486 94  HIS   A O     
765  C  CB    A HIS   A 95  ? 0.50145 0.46625 0.41049 0.03725  0.01193  -0.02838 94  HIS   A CB    
766  C  CB    B HIS   A 95  ? 0.50149 0.46609 0.41102 0.03688  0.01133  -0.02858 94  HIS   A CB    
767  C  CG    A HIS   A 95  ? 0.48679 0.43952 0.38205 0.04377  0.00654  -0.03133 94  HIS   A CG    
768  C  CG    B HIS   A 95  ? 0.50851 0.48041 0.42013 0.03819  0.02001  -0.02525 94  HIS   A CG    
769  N  ND1   A HIS   A 95  ? 0.44539 0.39285 0.33506 0.04559  0.00314  -0.03260 94  HIS   A ND1   
770  N  ND1   B HIS   A 95  ? 0.56179 0.53362 0.46757 0.04278  0.02457  -0.02348 94  HIS   A ND1   
771  C  CD2   A HIS   A 95  ? 0.46746 0.41166 0.35259 0.04944  0.00365  -0.03339 94  HIS   A CD2   
772  C  CD2   B HIS   A 95  ? 0.54207 0.52144 0.46174 0.03559  0.02463  -0.02304 94  HIS   A CD2   
773  C  CE1   A HIS   A 95  ? 0.51655 0.45233 0.39303 0.05221  -0.00196 -0.03547 94  HIS   A CE1   
774  C  CE1   B HIS   A 95  ? 0.51119 0.49051 0.42251 0.04267  0.03157  -0.01996 94  HIS   A CE1   
775  N  NE2   A HIS   A 95  ? 0.50316 0.43663 0.37639 0.05481  -0.00176 -0.03602 94  HIS   A NE2   
776  N  NE2   B HIS   A 95  ? 0.50881 0.49256 0.42849 0.03827  0.03145  -0.01983 94  HIS   A NE2   
777  N  N     . HIS   A 96  ? 0.45639 0.44128 0.38892 0.02502  0.01912  -0.02348 95  HIS   A N     
778  C  CA    . HIS   A 96  ? 0.49705 0.49126 0.43945 0.02094  0.02387  -0.02094 95  HIS   A CA    
779  C  C     . HIS   A 96  ? 0.44601 0.44400 0.39747 0.01499  0.02096  -0.02101 95  HIS   A C     
780  O  O     . HIS   A 96  ? 0.39217 0.39532 0.35089 0.01185  0.02240  -0.02001 95  HIS   A O     
781  C  CB    . HIS   A 96  ? 0.47844 0.47549 0.41989 0.02254  0.02832  -0.01895 95  HIS   A CB    
782  C  CG    . HIS   A 96  ? 0.58205 0.58759 0.53322 0.01889  0.03242  -0.01640 95  HIS   A CG    
783  N  ND1   . HIS   A 96  ? 0.67001 0.67965 0.62820 0.01407  0.03109  -0.01627 95  HIS   A ND1   
784  C  CD2   . HIS   A 96  ? 0.59420 0.60437 0.54923 0.01973  0.03740  -0.01374 95  HIS   A CD2   
785  C  CE1   . HIS   A 96  ? 0.62754 0.64326 0.59258 0.01226  0.03460  -0.01414 95  HIS   A CE1   
786  N  NE2   . HIS   A 96  ? 0.64906 0.66532 0.61306 0.01534  0.03823  -0.01250 95  HIS   A NE2   
787  N  N     . TYR   A 97  ? 0.41989 0.41516 0.37093 0.01376  0.01684  -0.02193 96  TYR   A N     
788  C  CA    . TYR   A 97  ? 0.38923 0.38816 0.34905 0.00877  0.01441  -0.02123 96  TYR   A CA    
789  C  C     . TYR   A 97  ? 0.32361 0.32169 0.28728 0.00716  0.01133  -0.02158 96  TYR   A C     
790  O  O     . TYR   A 97  ? 0.35320 0.35660 0.32479 0.00375  0.01220  -0.02007 96  TYR   A O     
791  C  CB    . TYR   A 97  ? 0.33205 0.32767 0.29099 0.00815  0.01020  -0.02179 96  TYR   A CB    
792  C  CG    . TYR   A 97  ? 0.34111 0.34077 0.30137 0.00717  0.01321  -0.02058 96  TYR   A CG    
793  C  CD1   . TYR   A 97  ? 0.34196 0.34829 0.31054 0.00324  0.01480  -0.01872 96  TYR   A CD1   
794  C  CD2   . TYR   A 97  ? 0.37825 0.37458 0.33111 0.01049  0.01409  -0.02126 96  TYR   A CD2   
795  C  CE1   . TYR   A 97  ? 0.37943 0.38906 0.34908 0.00242  0.01709  -0.01775 96  TYR   A CE1   
796  C  CE2   . TYR   A 97  ? 0.35917 0.35926 0.31375 0.00940  0.01662  -0.02007 96  TYR   A CE2   
797  C  CZ    . TYR   A 97  ? 0.34967 0.35634 0.31279 0.00519  0.01790  -0.01844 96  TYR   A CZ    
798  O  OH    . TYR   A 97  ? 0.43162 0.44166 0.39626 0.00421  0.02005  -0.01739 96  TYR   A OH    
799  N  N     . ARG   A 98  ? 0.38129 0.37227 0.33906 0.00997  0.00751  -0.02351 97  ARG   A N     
800  C  CA    . ARG   A 98  ? 0.38192 0.37185 0.34383 0.00838  0.00418  -0.02373 97  ARG   A CA    
801  C  C     . ARG   A 98  ? 0.43297 0.42815 0.39792 0.00773  0.00888  -0.02278 97  ARG   A C     
802  O  O     . ARG   A 98  ? 0.42417 0.42327 0.39672 0.00456  0.00861  -0.02155 97  ARG   A O     
803  C  CB    . ARG   A 98  ? 0.50980 0.49000 0.46393 0.01201  -0.00155 -0.02630 97  ARG   A CB    
804  C  CG    . ARG   A 98  ? 0.53388 0.51243 0.49339 0.01003  -0.00621 -0.02639 97  ARG   A CG    
805  C  CD    . ARG   A 98  ? 0.58771 0.56335 0.54154 0.01314  -0.00522 -0.02782 97  ARG   A CD    
806  N  NE    . ARG   A 98  ? 0.65302 0.62590 0.61129 0.01162  -0.01051 -0.02814 97  ARG   A NE    
807  C  CZ    . ARG   A 98  ? 0.68584 0.65687 0.64124 0.01341  -0.01018 -0.02914 97  ARG   A CZ    
808  N  NH1   . ARG   A 98  ? 0.51997 0.49159 0.46824 0.01695  -0.00479 -0.02970 97  ARG   A NH1   
809  N  NH2   . ARG   A 98  ? 0.67619 0.64510 0.63682 0.01160  -0.01522 -0.02914 97  ARG   A NH2   
810  N  N     . GLU   A 99  ? 0.47197 0.46740 0.43141 0.01094  0.01336  -0.02294 98  GLU   A N     
811  C  CA    . GLU   A 99  ? 0.48171 0.48215 0.44478 0.01027  0.01768  -0.02182 98  GLU   A CA    
812  C  C     . GLU   A 99  ? 0.42154 0.42950 0.39299 0.00641  0.02042  -0.01990 98  GLU   A C     
813  O  O     . GLU   A 99  ? 0.46399 0.47562 0.44070 0.00447  0.02154  -0.01917 98  GLU   A O     
814  C  CB    . GLU   A 99  ? 0.43157 0.43137 0.38861 0.01458  0.02218  -0.02142 98  GLU   A CB    
815  C  CG    . GLU   A 99  ? 0.51947 0.51122 0.46612 0.01988  0.02016  -0.02321 98  GLU   A CG    
816  C  CD    . GLU   A 99  ? 0.67456 0.66221 0.62074 0.01965  0.01572  -0.02497 98  GLU   A CD    
817  O  OE1   . GLU   A 99  ? 0.67277 0.66496 0.62590 0.01659  0.01681  -0.02418 98  GLU   A OE1   
818  O  OE2   . GLU   A 99  ? 0.67473 0.65413 0.61340 0.02273  0.01074  -0.02719 98  GLU   A OE2   
819  N  N     . GLN   A 100 ? 0.43244 0.44231 0.40460 0.00566  0.02140  -0.01916 99  GLN   A N     
820  C  CA    . GLN   A 100 ? 0.36305 0.37916 0.34201 0.00266  0.02357  -0.01754 99  GLN   A CA    
821  C  C     . GLN   A 100 ? 0.39093 0.40867 0.37563 -0.00027 0.02095  -0.01691 99  GLN   A C     
822  O  O     . GLN   A 100 ? 0.36646 0.38827 0.35589 -0.00176 0.02252  -0.01586 99  GLN   A O     
823  C  CB    . GLN   A 100 ? 0.43981 0.45713 0.41781 0.00277  0.02493  -0.01693 99  GLN   A CB    
824  C  CG    . GLN   A 100 ? 0.41151 0.43438 0.39531 0.00038  0.02687  -0.01548 99  GLN   A CG    
825  C  CD    . GLN   A 100 ? 0.45656 0.48058 0.43941 0.00070  0.02840  -0.01486 99  GLN   A CD    
826  O  OE1   . GLN   A 100 ? 0.54956 0.57035 0.52759 0.00238  0.02772  -0.01544 99  GLN   A OE1   
827  N  NE2   . GLN   A 100 ? 0.55338 0.58153 0.54053 -0.00067 0.03008  -0.01375 99  GLN   A NE2   
828  N  N     . ILE   A 101 ? 0.36030 0.37469 0.34497 -0.00079 0.01676  -0.01720 100 ILE   A N     
829  C  CA    . ILE   A 101 ? 0.31590 0.33235 0.30751 -0.00332 0.01456  -0.01554 100 ILE   A CA    
830  C  C     . ILE   A 101 ? 0.37190 0.38890 0.36599 -0.00359 0.01448  -0.01540 100 ILE   A C     
831  O  O     . ILE   A 101 ? 0.38655 0.40783 0.38603 -0.00501 0.01592  -0.01358 100 ILE   A O     
832  C  CB    . ILE   A 101 ? 0.31020 0.32247 0.30268 -0.00383 0.00934  -0.01547 100 ILE   A CB    
833  C  CG1   . ILE   A 101 ? 0.34564 0.35791 0.33630 -0.00379 0.00955  -0.01540 100 ILE   A CG1   
834  C  CG2   . ILE   A 101 ? 0.34584 0.36058 0.34712 -0.00619 0.00724  -0.01279 100 ILE   A CG2   
835  C  CD1   . ILE   A 101 ? 0.31424 0.32012 0.30296 -0.00325 0.00376  -0.01634 100 ILE   A CD1   
836  N  N     . LYS   A 102 ? 0.44125 0.45356 0.43073 -0.00176 0.01283  -0.01729 101 LYS   A N     
837  C  CA    . LYS   A 102 ? 0.44408 0.45645 0.43541 -0.00188 0.01258  -0.01739 101 LYS   A CA    
838  C  C     . LYS   A 102 ? 0.45374 0.47121 0.44698 -0.00221 0.01725  -0.01670 101 LYS   A C     
839  O  O     . LYS   A 102 ? 0.44019 0.46042 0.43816 -0.00346 0.01765  -0.01553 101 LYS   A O     
840  C  CB    . LYS   A 102 ? 0.49617 0.50227 0.48047 0.00096  0.01057  -0.01978 101 LYS   A CB    
841  C  CG    . LYS   A 102 ? 0.49879 0.49861 0.48245 0.00123  0.00412  -0.02067 101 LYS   A CG    
842  C  CD    . LYS   A 102 ? 0.58232 0.57507 0.55676 0.00518  0.00239  -0.02339 101 LYS   A CD    
843  C  CE    . LYS   A 102 ? 0.61664 0.61199 0.58937 0.00646  0.00708  -0.02356 101 LYS   A CE    
844  N  NZ    . LYS   A 102 ? 0.71297 0.70264 0.67540 0.01141  0.00768  -0.02551 101 LYS   A NZ    
845  N  N     . ARG   A 103 ? 0.46351 0.48199 0.45339 -0.00087 0.02056  -0.01722 102 ARG   A N     
846  C  CA    . ARG   A 103 ? 0.48921 0.51187 0.48154 -0.00117 0.02412  -0.01654 102 ARG   A CA    
847  C  C     . ARG   A 103 ? 0.50547 0.53227 0.50276 -0.00302 0.02469  -0.01498 102 ARG   A C     
848  O  O     . ARG   A 103 ? 0.46540 0.49443 0.46559 -0.00344 0.02554  -0.01440 102 ARG   A O     
849  C  CB    . ARG   A 103 ? 0.48883 0.51179 0.47822 0.00053  0.02702  -0.01663 102 ARG   A CB    
850  C  CG    . ARG   A 103 ? 0.53481 0.56106 0.52732 0.00051  0.02990  -0.01585 102 ARG   A CG    
851  C  CD    . ARG   A 103 ? 0.53655 0.56286 0.52729 0.00260  0.03272  -0.01512 102 ARG   A CD    
852  N  NE    . ARG   A 103 ? 0.59278 0.61868 0.58137 0.00305  0.03295  -0.01479 102 ARG   A NE    
853  C  CZ    . ARG   A 103 ? 0.51911 0.54750 0.51060 0.00133  0.03281  -0.01419 102 ARG   A CZ    
854  N  NH1   . ARG   A 103 ? 0.56054 0.59162 0.55653 -0.00047 0.03240  -0.01387 102 ARG   A NH1   
855  N  NH2   . ARG   A 103 ? 0.56556 0.59326 0.55469 0.00185  0.03294  -0.01400 102 ARG   A NH2   
856  N  N     . VAL   A 104 ? 0.45668 0.48424 0.45441 -0.00366 0.02421  -0.01425 103 VAL   A N     
857  C  CA    . VAL   A 104 ? 0.40186 0.43304 0.40306 -0.00452 0.02515  -0.01263 103 VAL   A CA    
858  C  C     . VAL   A 104 ? 0.45396 0.48636 0.45929 -0.00519 0.02400  -0.01087 103 VAL   A C     
859  O  O     . VAL   A 104 ? 0.47381 0.50882 0.48108 -0.00479 0.02545  -0.00967 103 VAL   A O     
860  C  CB    . VAL   A 104 ? 0.35568 0.38734 0.35621 -0.00484 0.02505  -0.01213 103 VAL   A CB    
861  C  CG1   . VAL   A 104 ? 0.41358 0.44842 0.41723 -0.00517 0.02566  -0.01012 103 VAL   A CG1   
862  C  CG2   . VAL   A 104 ? 0.43308 0.46468 0.43079 -0.00402 0.02692  -0.01312 103 VAL   A CG2   
863  N  N     . LYS   A 105 ? 0.44778 0.47805 0.45469 -0.00589 0.02117  -0.01041 104 LYS   A N     
864  C  CA    . LYS   A 105 ? 0.44478 0.47652 0.45727 -0.00657 0.02002  -0.00793 104 LYS   A CA    
865  C  C     . LYS   A 105 ? 0.48763 0.51869 0.50057 -0.00630 0.01994  -0.00856 104 LYS   A C     
866  O  O     . LYS   A 105 ? 0.48775 0.52029 0.50572 -0.00669 0.01930  -0.00621 104 LYS   A O     
867  C  CB    . LYS   A 105 ? 0.44535 0.47490 0.46139 -0.00770 0.01606  -0.00663 104 LYS   A CB    
868  C  CG    . LYS   A 105 ? 0.49099 0.51936 0.50546 -0.00799 0.01496  -0.00690 104 LYS   A CG    
869  C  CD    . LYS   A 105 ? 0.50530 0.53765 0.52485 -0.00852 0.01604  -0.00345 104 LYS   A CD    
870  C  CE    . LYS   A 105 ? 0.33411 0.36695 0.36201 -0.00971 0.01303  0.00022  104 LYS   A CE    
871  N  NZ    . LYS   A 105 ? 0.31444 0.35256 0.34686 -0.00919 0.01612  0.00428  104 LYS   A NZ    
872  N  N     . ASP   A 106 ? 0.49916 0.52810 0.50749 -0.00551 0.02062  -0.01126 105 ASP   A N     
873  C  CA    . ASP   A 106 ? 0.48786 0.51632 0.49632 -0.00514 0.02088  -0.01197 105 ASP   A CA    
874  C  C     . ASP   A 106 ? 0.50392 0.53013 0.51545 -0.00586 0.01737  -0.01125 105 ASP   A C     
875  O  O     . ASP   A 106 ? 0.52484 0.55267 0.54041 -0.00621 0.01739  -0.00971 105 ASP   A O     
876  C  CB    . ASP   A 106 ? 0.53119 0.56334 0.54181 -0.00475 0.02348  -0.01072 105 ASP   A CB    
877  C  CG    . ASP   A 106 ? 0.62308 0.65483 0.63339 -0.00427 0.02408  -0.01171 105 ASP   A CG    
878  O  OD1   . ASP   A 106 ? 0.60774 0.63669 0.61555 -0.00406 0.02321  -0.01356 105 ASP   A OD1   
879  O  OD2   . ASP   A 106 ? 0.68305 0.71704 0.69516 -0.00369 0.02544  -0.01055 105 ASP   A OD2   
880  N  N     . SER   A 107 ? 0.46131 0.48337 0.47107 -0.00590 0.01394  -0.01223 106 SER   A N     
881  C  CA    . SER   A 107 ? 0.44282 0.46202 0.45650 -0.00672 0.00933  -0.01136 106 SER   A CA    
882  C  C     . SER   A 107 ? 0.47873 0.49108 0.48648 -0.00545 0.00534  -0.01418 106 SER   A C     
883  O  O     . SER   A 107 ? 0.49724 0.50790 0.50007 -0.00446 0.00570  -0.01549 106 SER   A O     
884  C  CB    . SER   A 107 ? 0.41300 0.43498 0.43468 -0.00834 0.00794  -0.00755 106 SER   A CB    
885  O  OG    . SER   A 107 ? 0.44441 0.46339 0.47149 -0.00933 0.00272  -0.00626 106 SER   A OG    
886  N  N     . GLU   A 108 ? 0.40854 0.41657 0.41619 -0.00505 0.00145  -0.01514 107 GLU   A N     
887  C  CA    . GLU   A 108 ? 0.50839 0.50849 0.51043 -0.00332 -0.00386 -0.01766 107 GLU   A CA    
888  C  C     . GLU   A 108 ? 0.41542 0.41314 0.42395 -0.00501 -0.00984 -0.01585 107 GLU   A C     
889  O  O     . GLU   A 108 ? 0.55382 0.54396 0.55822 -0.00356 -0.01565 -0.01792 107 GLU   A O     
890  C  CB    . GLU   A 108 ? 0.49934 0.49477 0.49743 -0.00158 -0.00601 -0.01980 107 GLU   A CB    
891  C  CG    . GLU   A 108 ? 0.55699 0.55163 0.54590 0.00145  -0.00161 -0.02224 107 GLU   A CG    
892  C  CD    . GLU   A 108 ? 0.65075 0.63814 0.62926 0.00528  -0.00369 -0.02496 107 GLU   A CD    
893  O  OE1   . GLU   A 108 ? 0.76470 0.74437 0.73949 0.00709  -0.00978 -0.02676 107 GLU   A OE1   
894  O  OE2   . GLU   A 108 ? 0.74882 0.73782 0.72273 0.00683  0.00049  -0.02519 107 GLU   A OE2   
895  N  N     . ASP   A 109 ? 0.40416 0.40788 0.42278 -0.00766 -0.00870 -0.01180 108 ASP   A N     
896  C  CA    . ASP   A 109 ? 0.50951 0.51181 0.53728 -0.00953 -0.01444 -0.00889 108 ASP   A CA    
897  C  C     . ASP   A 109 ? 0.50294 0.50942 0.53512 -0.01079 -0.01274 -0.00612 108 ASP   A C     
898  O  O     . ASP   A 109 ? 0.49911 0.51098 0.54164 -0.01256 -0.01180 -0.00135 108 ASP   A O     
899  C  CB    . ASP   A 109 ? 0.53088 0.53657 0.56892 -0.01123 -0.01509 -0.00523 108 ASP   A CB    
900  C  CG    . ASP   A 109 ? 0.55158 0.55475 0.60027 -0.01305 -0.02222 -0.00200 108 ASP   A CG    
901  O  OD1   . ASP   A 109 ? 0.66561 0.66088 0.71087 -0.01237 -0.02892 -0.00460 108 ASP   A OD1   
902  O  OD2   . ASP   A 109 ? 0.66173 0.67054 0.72228 -0.01481 -0.02128 0.00337  108 ASP   A OD2   
903  N  N     . VAL   A 110 ? 0.39729 0.40156 0.42174 -0.00956 -0.01197 -0.00869 109 VAL   A N     
904  C  CA    . VAL   A 110 ? 0.40763 0.41561 0.43509 -0.01056 -0.01017 -0.00650 109 VAL   A CA    
905  C  C     . VAL   A 110 ? 0.34753 0.34967 0.37742 -0.01107 -0.01739 -0.00642 109 VAL   A C     
906  O  O     . VAL   A 110 ? 0.35799 0.35237 0.37935 -0.00907 -0.02140 -0.01041 109 VAL   A O     
907  C  CB    . VAL   A 110 ? 0.35045 0.35997 0.36882 -0.00904 -0.00486 -0.00903 109 VAL   A CB    
908  C  CG1   . VAL   A 110 ? 0.42664 0.44004 0.44867 -0.01015 -0.00329 -0.00658 109 VAL   A CG1   
909  C  CG2   . VAL   A 110 ? 0.38478 0.39897 0.40073 -0.00838 0.00126  -0.00947 109 VAL   A CG2   
910  N  N     . PRO   A 111 ? 0.33555 0.34072 0.37664 -0.01325 -0.01938 -0.00184 110 PRO   A N     
911  C  CA    . PRO   A 111 ? 0.31250 0.31165 0.35655 -0.01385 -0.02695 -0.00173 110 PRO   A CA    
912  C  C     . PRO   A 111 ? 0.29628 0.29215 0.32983 -0.01217 -0.02624 -0.00537 110 PRO   A C     
913  O  O     . PRO   A 111 ? 0.30892 0.31039 0.34086 -0.01229 -0.02029 -0.00459 110 PRO   A O     
914  C  CB    . PRO   A 111 ? 0.34190 0.34748 0.40099 -0.01644 -0.02683 0.00499  110 PRO   A CB    
915  C  CG    . PRO   A 111 ? 0.33317 0.34587 0.39770 -0.01679 -0.02138 0.00829  110 PRO   A CG    
916  C  CD    . PRO   A 111 ? 0.36877 0.38253 0.42059 -0.01481 -0.01514 0.00384  110 PRO   A CD    
917  N  N     . MET   A 112 ? 0.31328 0.29953 0.33893 -0.01012 -0.03246 -0.00946 111 MET   A N     
918  C  CA    . MET   A 112 ? 0.31555 0.29807 0.33196 -0.00822 -0.03253 -0.01236 111 MET   A CA    
919  C  C     . MET   A 112 ? 0.31054 0.28173 0.32304 -0.00645 -0.04221 -0.01510 111 MET   A C     
920  O  O     . MET   A 112 ? 0.34753 0.31302 0.36271 -0.00629 -0.04882 -0.01553 111 MET   A O     
921  C  CB    . MET   A 112 ? 0.46721 0.45102 0.47107 -0.00543 -0.02545 -0.01569 111 MET   A CB    
922  C  CG    . MET   A 112 ? 0.50949 0.48922 0.50433 -0.00244 -0.02476 -0.01899 111 MET   A CG    
923  S  SD    . MET   A 112 ? 0.45547 0.44101 0.44183 -0.00054 -0.01460 -0.02022 111 MET   A SD    
924  C  CE    . MET   A 112 ? 0.47106 0.46664 0.46678 -0.00363 -0.00879 -0.01697 111 MET   A CE    
925  N  N     . VAL   A 113 ? 0.30338 0.27121 0.31020 -0.00517 -0.04345 -0.01670 112 VAL   A N     
926  C  CA    . VAL   A 113 ? 0.32971 0.28602 0.33083 -0.00276 -0.05260 -0.01971 112 VAL   A CA    
927  C  C     . VAL   A 113 ? 0.34101 0.29375 0.32658 0.00147  -0.04915 -0.02369 112 VAL   A C     
928  O  O     . VAL   A 113 ? 0.32945 0.28930 0.31452 0.00062  -0.04201 -0.02254 112 VAL   A O     
929  C  CB    . VAL   A 113 ? 0.31306 0.26909 0.32601 -0.00587 -0.05860 -0.01639 112 VAL   A CB    
930  C  CG1   . VAL   A 113 ? 0.32711 0.26986 0.33242 -0.00280 -0.06870 -0.02019 112 VAL   A CG1   
931  C  CG2   . VAL   A 113 ? 0.31526 0.27515 0.34476 -0.00968 -0.06176 -0.01149 112 VAL   A CG2   
932  N  N     . LEU   A 114 ? 0.34095 0.28295 0.31367 0.00643  -0.05370 -0.02810 113 LEU   A N     
933  C  CA    . LEU   A 114 ? 0.33734 0.27441 0.29477 0.01151  -0.05137 -0.03152 113 LEU   A CA    
934  C  C     . LEU   A 114 ? 0.34542 0.27485 0.30119 0.01239  -0.05887 -0.03262 113 LEU   A C     
935  O  O     . LEU   A 114 ? 0.39925 0.31974 0.35736 0.01267  -0.06916 -0.03360 113 LEU   A O     
936  C  CB    . LEU   A 114 ? 0.38459 0.31331 0.32783 0.01755  -0.05231 -0.03537 113 LEU   A CB    
937  C  CG    . LEU   A 114 ? 0.39160 0.31470 0.31799 0.02412  -0.04942 -0.03837 113 LEU   A CG    
938  C  CD1   . LEU   A 114 ? 0.40617 0.34021 0.33252 0.02329  -0.03786 -0.03630 113 LEU   A CD1   
939  C  CD2   . LEU   A 114 ? 0.46699 0.38000 0.37928 0.03096  -0.05199 -0.04189 113 LEU   A CD2   
940  N  N     . VAL   A 115 ? 0.34300 0.27538 0.29469 0.01301  -0.05420 -0.03256 114 VAL   A N     
941  C  CA    . VAL   A 115 ? 0.34892 0.27559 0.29993 0.01334  -0.06023 -0.03321 114 VAL   A CA    
942  C  C     . VAL   A 115 ? 0.35818 0.27858 0.29181 0.01971  -0.05801 -0.03674 114 VAL   A C     
943  O  O     . VAL   A 115 ? 0.36708 0.29474 0.29700 0.02034  -0.04855 -0.03594 114 VAL   A O     
944  C  CB    . VAL   A 115 ? 0.33638 0.27351 0.30075 0.00762  -0.05658 -0.02893 114 VAL   A CB    
945  C  CG1   . VAL   A 115 ? 0.34256 0.27373 0.30647 0.00793  -0.06291 -0.02955 114 VAL   A CG1   
946  C  CG2   . VAL   A 115 ? 0.32762 0.27151 0.30917 0.00211  -0.05780 -0.02457 114 VAL   A CG2   
947  N  N     . GLY   A 116 ? 0.37534 0.28229 0.29911 0.02445  -0.06696 -0.04026 115 GLY   A N     
948  C  CA    . GLY   A 116 ? 0.40650 0.30605 0.31339 0.03124  -0.06600 -0.04338 115 GLY   A CA    
949  C  C     . GLY   A 116 ? 0.38598 0.28319 0.29572 0.02970  -0.07055 -0.04318 115 GLY   A C     
950  O  O     . GLY   A 116 ? 0.39577 0.28289 0.30648 0.03016  -0.08170 -0.04478 115 GLY   A O     
951  N  N     . ASN   A 117 ? 0.37624 0.28271 0.28831 0.02761  -0.06243 -0.04106 116 ASN   A N     
952  C  CA    . ASN   A 117 ? 0.37529 0.28169 0.29149 0.02542  -0.06528 -0.04029 116 ASN   A CA    
953  C  C     . ASN   A 117 ? 0.39710 0.29360 0.29602 0.03261  -0.06671 -0.04378 116 ASN   A C     
954  O  O     . ASN   A 117 ? 0.44184 0.33353 0.32584 0.03938  -0.06341 -0.04604 116 ASN   A O     
955  C  CB    . ASN   A 117 ? 0.35790 0.27935 0.28571 0.01952  -0.05598 -0.03612 116 ASN   A CB    
956  C  CG    . ASN   A 117 ? 0.35824 0.28095 0.29350 0.01615  -0.05913 -0.03455 116 ASN   A CG    
957  O  OD1   . ASN   A 117 ? 0.35976 0.27678 0.30205 0.01427  -0.06860 -0.03429 116 ASN   A OD1   
958  N  ND2   . ASN   A 117 ? 0.34814 0.27796 0.28228 0.01547  -0.05162 -0.03335 116 ASN   A ND2   
959  N  N     . LYS   A 118 ? 0.42093 0.31454 0.32227 0.03131  -0.07155 -0.04383 117 LYS   A N     
960  C  CA    . LYS   A 118 ? 0.44509 0.32917 0.33161 0.03754  -0.07395 -0.04686 117 LYS   A CA    
961  C  C     . LYS   A 118 ? 0.51652 0.38304 0.38898 0.04484  -0.08472 -0.05155 117 LYS   A C     
962  O  O     . LYS   A 118 ? 0.47468 0.33250 0.32922 0.05295  -0.08423 -0.05451 117 LYS   A O     
963  C  CB    . LYS   A 118 ? 0.42442 0.31387 0.30017 0.04169  -0.06236 -0.04651 117 LYS   A CB    
964  C  CG    . LYS   A 118 ? 0.38684 0.29296 0.27512 0.03524  -0.05167 -0.04223 117 LYS   A CG    
965  C  CD    . LYS   A 118 ? 0.38088 0.29118 0.26191 0.03801  -0.04331 -0.04149 117 LYS   A CD    
966  C  CE    . LYS   A 118 ? 0.36239 0.28825 0.25484 0.03238  -0.03306 -0.03756 117 LYS   A CE    
967  N  NZ    . LYS   A 118 ? 0.41420 0.34488 0.30206 0.03423  -0.02534 -0.03631 117 LYS   A NZ    
968  N  N     A CYS   A 119 ? 0.46333 0.32410 0.34359 0.04248  -0.09472 -0.05208 118 CYS   A N     
969  N  N     B CYS   A 119 ? 0.46349 0.32413 0.34360 0.04255  -0.09478 -0.05212 118 CYS   A N     
970  C  CA    A CYS   A 119 ? 0.48340 0.32636 0.35060 0.04946  -0.10635 -0.05679 118 CYS   A CA    
971  C  CA    B CYS   A 119 ? 0.48364 0.32641 0.35034 0.04967  -0.10629 -0.05687 118 CYS   A CA    
972  C  C     A CYS   A 119 ? 0.53738 0.36782 0.39764 0.05283  -0.11622 -0.05962 118 CYS   A C     
973  C  C     B CYS   A 119 ? 0.53784 0.36816 0.39731 0.05315  -0.11594 -0.05971 118 CYS   A C     
974  O  O     A CYS   A 119 ? 0.57078 0.38459 0.41825 0.05961  -0.12688 -0.06404 118 CYS   A O     
975  O  O     B CYS   A 119 ? 0.57147 0.38512 0.41739 0.06022  -0.12625 -0.06420 118 CYS   A O     
976  C  CB    A CYS   A 119 ? 0.47079 0.31136 0.35004 0.04549  -0.11479 -0.05621 118 CYS   A CB    
977  C  CB    B CYS   A 119 ? 0.47121 0.31119 0.34978 0.04579  -0.11509 -0.05638 118 CYS   A CB    
978  S  SG    A CYS   A 119 ? 0.53771 0.38101 0.44157 0.03608  -0.12460 -0.05246 118 CYS   A SG    
979  S  SG    B CYS   A 119 ? 0.59392 0.44313 0.47472 0.04471  -0.10608 -0.05478 118 CYS   A SG    
980  N  N     . ASP   A 120 ? 0.56102 0.39833 0.42874 0.04867  -0.11334 -0.05736 119 ASP   A N     
981  C  CA    . ASP   A 120 ? 0.57621 0.40229 0.43556 0.05248  -0.12110 -0.06010 119 ASP   A CA    
982  C  C     . ASP   A 120 ? 0.61231 0.43245 0.44876 0.06210  -0.11534 -0.06313 119 ASP   A C     
983  O  O     . ASP   A 120 ? 0.63524 0.44326 0.46037 0.06742  -0.12235 -0.06627 119 ASP   A O     
984  C  CB    . ASP   A 120 ? 0.50748 0.34365 0.38301 0.04472  -0.11935 -0.05630 119 ASP   A CB    
985  C  CG    . ASP   A 120 ? 0.52232 0.37496 0.40130 0.04159  -0.10416 -0.05286 119 ASP   A CG    
986  O  OD1   . ASP   A 120 ? 0.49189 0.35619 0.38139 0.03684  -0.09723 -0.04972 119 ASP   A OD1   
987  O  OD2   . ASP   A 120 ? 0.53226 0.38556 0.40267 0.04437  -0.09934 -0.05343 119 ASP   A OD2   
988  N  N     . LEU   A 121 ? 0.57222 0.40067 0.40221 0.06460  -0.10276 -0.06186 120 LEU   A N     
989  C  CA    . LEU   A 121 ? 0.66024 0.48618 0.47167 0.07301  -0.09519 -0.06304 120 LEU   A CA    
990  C  C     . LEU   A 121 ? 0.64167 0.45194 0.43119 0.08452  -0.09941 -0.06727 120 LEU   A C     
991  O  O     . LEU   A 121 ? 0.70644 0.51421 0.49572 0.08536  -0.10159 -0.06807 120 LEU   A O     
992  C  CB    . LEU   A 121 ? 0.64031 0.48305 0.45646 0.07036  -0.07948 -0.05885 120 LEU   A CB    
993  C  CG    . LEU   A 121 ? 0.56880 0.42647 0.40205 0.06115  -0.07350 -0.05486 120 LEU   A CG    
994  C  CD1   . LEU   A 121 ? 0.57285 0.44469 0.40834 0.05999  -0.05913 -0.05128 120 LEU   A CD1   
995  C  CD2   . LEU   A 121 ? 0.58506 0.43739 0.41448 0.06233  -0.07769 -0.05604 120 LEU   A CD2   
996  N  N     . PRO   A 122 ? 0.71915 0.51902 0.48964 0.09389  -0.10001 -0.06981 121 PRO   A N     
997  C  CA    . PRO   A 122 ? 0.75692 0.54113 0.50403 0.10651  -0.10331 -0.07368 121 PRO   A CA    
998  C  C     . PRO   A 122 ? 0.73183 0.52336 0.47118 0.11148  -0.08998 -0.07121 121 PRO   A C     
999  O  O     . PRO   A 122 ? 0.81185 0.59361 0.53759 0.11940  -0.09235 -0.07351 121 PRO   A O     
1000 C  CB    . PRO   A 122 ? 0.74925 0.52156 0.47975 0.11460  -0.10710 -0.07639 121 PRO   A CB    
1001 C  CG    . PRO   A 122 ? 0.71810 0.50554 0.46073 0.10763  -0.09781 -0.07234 121 PRO   A CG    
1002 C  CD    . PRO   A 122 ? 0.68184 0.48364 0.45069 0.09390  -0.09741 -0.06909 121 PRO   A CD    
1003 N  N     . SER   A 123 ? 0.79200 0.60022 0.54010 0.10713  -0.07641 -0.06642 122 SER   A N     
1004 C  CA    . SER   A 123 ? 0.82363 0.63863 0.56442 0.11257  -0.06348 -0.06341 122 SER   A CA    
1005 C  C     . SER   A 123 ? 0.79026 0.61243 0.54033 0.10843  -0.06050 -0.06192 122 SER   A C     
1006 O  O     . SER   A 123 ? 0.81882 0.65541 0.57753 0.10495  -0.04886 -0.05755 122 SER   A O     
1007 C  CB    . SER   A 123 ? 0.79727 0.62730 0.54585 0.10890  -0.05110 -0.05863 122 SER   A CB    
1008 O  OG    . SER   A 123 ? 0.84114 0.68291 0.61116 0.09635  -0.05164 -0.05681 122 SER   A OG    
1009 N  N     . ARG   A 124 ? 0.81532 0.62694 0.56328 0.10923  -0.07121 -0.06550 123 ARG   A N     
1010 C  CA    . ARG   A 124 ? 0.68825 0.50639 0.44703 0.10406  -0.07002 -0.06435 123 ARG   A CA    
1011 C  C     . ARG   A 124 ? 0.75217 0.57177 0.49961 0.11176  -0.06052 -0.06279 123 ARG   A C     
1012 O  O     . ARG   A 124 ? 0.82838 0.63484 0.55498 0.12361  -0.06232 -0.06521 123 ARG   A O     
1013 C  CB    . ARG   A 124 ? 0.75535 0.56051 0.51445 0.10347  -0.08500 -0.06859 123 ARG   A CB    
1014 C  CG    . ARG   A 124 ? 0.72680 0.53546 0.49326 0.10030  -0.08502 -0.06807 123 ARG   A CG    
1015 C  CD    . ARG   A 124 ? 0.69877 0.49918 0.47416 0.09557  -0.09961 -0.07073 123 ARG   A CD    
1016 N  NE    . ARG   A 124 ? 0.74601 0.55695 0.53781 0.08765  -0.09717 -0.06824 123 ARG   A NE    
1017 C  CZ    . ARG   A 124 ? 0.77467 0.58775 0.58421 0.07902  -0.10501 -0.06752 123 ARG   A CZ    
1018 N  NH1   . ARG   A 124 ? 0.75263 0.55810 0.56727 0.07666  -0.11640 -0.06894 123 ARG   A NH1   
1019 N  NH2   . ARG   A 124 ? 0.71615 0.53950 0.53930 0.07268  -0.10119 -0.06489 123 ARG   A NH2   
1020 N  N     . THR   A 125 ? 0.67175 0.50702 0.43280 0.10543  -0.05053 -0.05859 124 THR   A N     
1021 C  CA    . THR   A 125 ? 0.66772 0.50593 0.42104 0.11170  -0.04121 -0.05634 124 THR   A CA    
1022 C  C     . THR   A 125 ? 0.75900 0.60185 0.52203 0.10680  -0.04160 -0.05601 124 THR   A C     
1023 O  O     . THR   A 125 ? 0.68964 0.53361 0.44601 0.11224  -0.03511 -0.05448 124 THR   A O     
1024 C  CB    . THR   A 125 ? 0.63836 0.49088 0.39665 0.11090  -0.02701 -0.05081 124 THR   A CB    
1025 O  OG1   . THR   A 125 ? 0.65227 0.51993 0.43234 0.09848  -0.02368 -0.04804 124 THR   A OG1   
1026 C  CG2   . THR   A 125 ? 0.74968 0.59691 0.49574 0.11773  -0.02547 -0.05076 124 THR   A CG2   
1027 N  N     . VAL   A 126 ? 0.64639 0.49204 0.42505 0.09706  -0.04875 -0.05702 125 VAL   A N     
1028 C  CA    . VAL   A 126 ? 0.63557 0.48484 0.42351 0.09244  -0.05003 -0.05684 125 VAL   A CA    
1029 C  C     . VAL   A 126 ? 0.72295 0.55768 0.50732 0.09353  -0.06471 -0.06150 125 VAL   A C     
1030 O  O     . VAL   A 126 ? 0.68204 0.51378 0.47426 0.08851  -0.07337 -0.06276 125 VAL   A O     
1031 C  CB    . VAL   A 126 ? 0.54938 0.41552 0.36010 0.08018  -0.04501 -0.05312 125 VAL   A CB    
1032 C  CG1   . VAL   A 126 ? 0.54735 0.41595 0.36736 0.07562  -0.04758 -0.05319 125 VAL   A CG1   
1033 C  CG2   . VAL   A 126 ? 0.60688 0.48640 0.42101 0.07949  -0.03136 -0.04864 125 VAL   A CG2   
1034 N  N     . ASP   A 127 ? 0.71564 0.54114 0.48856 0.10026  -0.06773 -0.06381 126 ASP   A N     
1035 C  CA    . ASP   A 127 ? 0.76816 0.57821 0.53605 0.10254  -0.08234 -0.06845 126 ASP   A CA    
1036 C  C     . ASP   A 127 ? 0.69044 0.50697 0.47987 0.09118  -0.08795 -0.06744 126 ASP   A C     
1037 O  O     . ASP   A 127 ? 0.70841 0.53890 0.51135 0.08449  -0.08009 -0.06398 126 ASP   A O     
1038 C  CB    . ASP   A 127 ? 0.73304 0.53234 0.48326 0.11276  -0.08332 -0.07091 126 ASP   A CB    
1039 C  CG    . ASP   A 127 ? 0.87338 0.66139 0.59900 0.12637  -0.08104 -0.07259 126 ASP   A CG    
1040 O  OD1   . ASP   A 127 ? 0.93328 0.72410 0.65618 0.12764  -0.07636 -0.07117 126 ASP   A OD1   
1041 O  OD2   . ASP   A 127 ? 0.94800 0.72403 0.65650 0.13628  -0.08389 -0.07521 126 ASP   A OD2   
1042 N  N     . THR   A 128 ? 0.71302 0.51861 0.50540 0.08960  -0.10204 -0.07033 127 THR   A N     
1043 C  CA    . THR   A 128 ? 0.70811 0.51761 0.52000 0.08030  -0.10877 -0.06915 127 THR   A CA    
1044 C  C     . THR   A 128 ? 0.70214 0.51395 0.51455 0.08066  -0.10605 -0.06890 127 THR   A C     
1045 O  O     . THR   A 128 ? 0.61523 0.43995 0.44512 0.07217  -0.10164 -0.06544 127 THR   A O     
1046 C  CB    . THR   A 128 ? 0.73582 0.52974 0.54768 0.08102  -0.12581 -0.07261 127 THR   A CB    
1047 O  OG1   . THR   A 128 ? 0.84704 0.64057 0.66121 0.07937  -0.12793 -0.07229 127 THR   A OG1   
1048 C  CG2   . THR   A 128 ? 0.77580 0.57349 0.60863 0.07197  -0.13297 -0.07066 127 THR   A CG2   
1049 N  N     . LYS   A 129 ? 0.73095 0.53034 0.52341 0.09106  -0.10810 -0.07241 128 LYS   A N     
1050 C  CA    . LYS   A 129 ? 0.66378 0.46402 0.45559 0.09205  -0.10632 -0.07249 128 LYS   A CA    
1051 C  C     . LYS   A 129 ? 0.62856 0.44650 0.42732 0.08851  -0.09044 -0.06799 128 LYS   A C     
1052 O  O     . LYS   A 129 ? 0.69081 0.51588 0.49963 0.08382  -0.08804 -0.06639 128 LYS   A O     
1053 C  CB    . LYS   A 129 ? 0.74084 0.52333 0.50798 0.10510  -0.11157 -0.07715 128 LYS   A CB    
1054 C  CG    . LYS   A 129 ? 0.78214 0.56315 0.54735 0.10685  -0.11164 -0.07782 128 LYS   A CG    
1055 C  CD    . LYS   A 129 ? 0.79810 0.55765 0.54102 0.11882  -0.12251 -0.08340 128 LYS   A CD    
1056 C  CE    . LYS   A 129 ? 0.79537 0.55348 0.53798 0.11972  -0.12354 -0.08410 128 LYS   A CE    
1057 N  NZ    . LYS   A 129 ? 0.81850 0.59365 0.56640 0.11731  -0.10715 -0.07954 128 LYS   A NZ    
1058 N  N     . GLN   A 130 ? 0.65883 0.48376 0.45278 0.09075  -0.07988 -0.06582 129 GLN   A N     
1059 C  CA    . GLN   A 130 ? 0.62356 0.46520 0.42591 0.08686  -0.06572 -0.06129 129 GLN   A CA    
1060 C  C     . GLN   A 130 ? 0.59292 0.44859 0.41878 0.07440  -0.06417 -0.05809 129 GLN   A C     
1061 O  O     . GLN   A 130 ? 0.59565 0.46156 0.43031 0.07037  -0.05752 -0.05561 129 GLN   A O     
1062 C  CB    . GLN   A 130 ? 0.68782 0.53448 0.48364 0.09045  -0.05607 -0.05911 129 GLN   A CB    
1063 C  CG    . GLN   A 130 ? 0.76174 0.59955 0.53574 0.10310  -0.05222 -0.06010 129 GLN   A CG    
1064 C  CD    . GLN   A 130 ? 0.74633 0.58968 0.51646 0.10575  -0.04331 -0.05733 129 GLN   A CD    
1065 O  OE1   . GLN   A 130 ? 0.75857 0.59214 0.51682 0.11154  -0.04760 -0.05948 129 GLN   A OE1   
1066 N  NE2   . GLN   A 130 ? 0.75683 0.61582 0.53765 0.10135  -0.03129 -0.05247 129 GLN   A NE2   
1067 N  N     . ALA   A 131 ? 0.58512 0.44150 0.42109 0.06862  -0.06989 -0.05785 130 ALA   A N     
1068 C  CA    . ALA   A 131 ? 0.52636 0.39633 0.38384 0.05771  -0.06749 -0.05419 130 ALA   A CA    
1069 C  C     . ALA   A 131 ? 0.52231 0.39084 0.39036 0.05329  -0.07480 -0.05433 130 ALA   A C     
1070 O  O     . ALA   A 131 ? 0.51026 0.39050 0.39169 0.04697  -0.06938 -0.05122 130 ALA   A O     
1071 C  CB    . ALA   A 131 ? 0.54522 0.41655 0.41006 0.05353  -0.07080 -0.05334 130 ALA   A CB    
1072 N  N     . GLN   A 132 ? 0.56535 0.41913 0.42723 0.05692  -0.08733 -0.05789 131 GLN   A N     
1073 C  CA    . GLN   A 132 ? 0.62330 0.47451 0.49468 0.05345  -0.09502 -0.05801 131 GLN   A CA    
1074 C  C     . GLN   A 132 ? 0.62562 0.48141 0.49413 0.05492  -0.08804 -0.05762 131 GLN   A C     
1075 O  O     . GLN   A 132 ? 0.64880 0.51219 0.53144 0.04870  -0.08733 -0.05523 131 GLN   A O     
1076 C  CB    . GLN   A 132 ? 0.66552 0.49803 0.52777 0.05875  -0.11013 -0.06246 131 GLN   A CB    
1077 C  CG    . GLN   A 132 ? 0.68760 0.51470 0.55637 0.05612  -0.11974 -0.06262 131 GLN   A CG    
1078 C  CD    . GLN   A 132 ? 0.75712 0.56401 0.61547 0.06222  -0.13571 -0.06748 131 GLN   A CD    
1079 O  OE1   . GLN   A 132 ? 0.85175 0.64730 0.69365 0.07022  -0.13892 -0.07137 131 GLN   A OE1   
1080 N  NE2   . GLN   A 132 ? 0.72537 0.52728 0.59328 0.05873  -0.14613 -0.06718 131 GLN   A NE2   
1081 N  N     . ASP   A 133 ? 0.64132 0.49262 0.49178 0.06343  -0.08267 -0.05960 132 ASP   A N     
1082 C  CA    . ASP   A 133 ? 0.67088 0.52639 0.51833 0.06531  -0.07580 -0.05899 132 ASP   A CA    
1083 C  C     . ASP   A 133 ? 0.62151 0.49512 0.48319 0.05807  -0.06388 -0.05437 132 ASP   A C     
1084 O  O     . ASP   A 133 ? 0.62520 0.50521 0.49594 0.05400  -0.06169 -0.05287 132 ASP   A O     
1085 C  CB    . ASP   A 133 ? 0.68898 0.53610 0.51428 0.07667  -0.07197 -0.06126 132 ASP   A CB    
1086 C  CG    . ASP   A 133 ? 0.76875 0.59623 0.57765 0.08522  -0.08434 -0.06637 132 ASP   A CG    
1087 O  OD1   . ASP   A 133 ? 0.77483 0.59531 0.59068 0.08189  -0.09625 -0.06821 132 ASP   A OD1   
1088 O  OD2   . ASP   A 133 ? 0.82526 0.64391 0.61416 0.09574  -0.08231 -0.06833 132 ASP   A OD2   
1089 N  N     . LEU   A 134 ? 0.61021 0.49188 0.47429 0.05631  -0.05667 -0.05214 133 LEU   A N     
1090 C  CA    . LEU   A 134 ? 0.57338 0.47115 0.45089 0.04957  -0.04658 -0.04801 133 LEU   A CA    
1091 C  C     . LEU   A 134 ? 0.49936 0.40365 0.39544 0.04057  -0.05029 -0.04596 133 LEU   A C     
1092 O  O     . LEU   A 134 ? 0.56284 0.47591 0.46814 0.03643  -0.04562 -0.04378 133 LEU   A O     
1093 C  CB    . LEU   A 134 ? 0.54744 0.45151 0.42418 0.04947  -0.03946 -0.04615 133 LEU   A CB    
1094 C  CG    . LEU   A 134 ? 0.53537 0.45483 0.42383 0.04377  -0.02910 -0.04219 133 LEU   A CG    
1095 C  CD1   . LEU   A 134 ? 0.56210 0.48453 0.44464 0.04784  -0.02125 -0.04131 133 LEU   A CD1   
1096 C  CD2   . LEU   A 134 ? 0.55336 0.47891 0.44458 0.04188  -0.02445 -0.04033 133 LEU   A CD2   
1097 N  N     . ALA   A 135 ? 0.57776 0.47767 0.47968 0.03782  -0.05876 -0.04629 134 ALA   A N     
1098 C  CA    . ALA   A 135 ? 0.52543 0.43130 0.44565 0.02993  -0.06241 -0.04348 134 ALA   A CA    
1099 C  C     . ALA   A 135 ? 0.54226 0.44580 0.46589 0.02934  -0.06620 -0.04388 134 ALA   A C     
1100 O  O     . ALA   A 135 ? 0.50162 0.41485 0.43828 0.02381  -0.06262 -0.04073 134 ALA   A O     
1101 C  CB    . ALA   A 135 ? 0.54707 0.44630 0.47213 0.02828  -0.07239 -0.04376 134 ALA   A CB    
1102 N  N     . ARG   A 136 ? 0.56206 0.45223 0.47355 0.03540  -0.07375 -0.04779 135 ARG   A N     
1103 C  CA    . ARG   A 136 ? 0.62840 0.51556 0.54193 0.03538  -0.07759 -0.04850 135 ARG   A CA    
1104 C  C     . ARG   A 136 ? 0.53219 0.42954 0.44600 0.03478  -0.06649 -0.04690 135 ARG   A C     
1105 O  O     . ARG   A 136 ? 0.57235 0.47669 0.49817 0.02978  -0.06520 -0.04455 135 ARG   A O     
1106 C  CB    . ARG   A 136 ? 0.60709 0.47722 0.50428 0.04343  -0.08694 -0.05345 135 ARG   A CB    
1107 C  CG    . ARG   A 136 ? 0.68085 0.54486 0.58297 0.04248  -0.09575 -0.05438 135 ARG   A CG    
1108 C  CD    . ARG   A 136 ? 0.62410 0.47050 0.50768 0.05154  -0.10464 -0.05969 135 ARG   A CD    
1109 N  NE    . ARG   A 136 ? 0.69626 0.53143 0.57094 0.05570  -0.11226 -0.06235 135 ARG   A NE    
1110 C  CZ    . ARG   A 136 ? 0.75316 0.58090 0.60813 0.06431  -0.10979 -0.06532 135 ARG   A CZ    
1111 N  NH1   . ARG   A 136 ? 0.81607 0.64652 0.65875 0.06980  -0.09984 -0.06562 135 ARG   A NH1   
1112 N  NH2   . ARG   A 136 ? 0.76856 0.58578 0.61625 0.06780  -0.11750 -0.06772 135 ARG   A NH2   
1113 N  N     . SER   A 137 ? 0.54492 0.44383 0.44665 0.03971  -0.05811 -0.04761 136 SER   A N     
1114 C  CA    . SER   A 137 ? 0.59500 0.50348 0.49791 0.03914  -0.04789 -0.04578 136 SER   A CA    
1115 C  C     . SER   A 137 ? 0.56279 0.48555 0.48267 0.03093  -0.04201 -0.04170 136 SER   A C     
1116 O  O     . SER   A 137 ? 0.57011 0.50016 0.49541 0.02863  -0.03672 -0.04010 136 SER   A O     
1117 C  CB    . SER   A 137 ? 0.57391 0.48233 0.46320 0.04561  -0.03991 -0.04618 136 SER   A CB    
1118 O  OG    . SER   A 137 ? 0.61271 0.53161 0.50829 0.04213  -0.03221 -0.04330 136 SER   A OG    
1119 N  N     . TYR   A 138 ? 0.56187 0.48835 0.49000 0.02675  -0.04313 -0.03995 137 TYR   A N     
1120 C  CA    . TYR   A 138 ? 0.51116 0.45022 0.45430 0.01983  -0.03802 -0.03602 137 TYR   A CA    
1121 C  C     . TYR   A 138 ? 0.48121 0.42158 0.43836 0.01467  -0.04403 -0.03395 137 TYR   A C     
1122 O  O     . TYR   A 138 ? 0.47365 0.42414 0.44263 0.00977  -0.03953 -0.03046 137 TYR   A O     
1123 C  CB    . TYR   A 138 ? 0.53490 0.47826 0.48037 0.01808  -0.03529 -0.03457 137 TYR   A CB    
1124 C  CG    . TYR   A 138 ? 0.50646 0.45227 0.44244 0.02165  -0.02746 -0.03502 137 TYR   A CG    
1125 C  CD1   . TYR   A 138 ? 0.59097 0.53846 0.52024 0.02503  -0.02118 -0.03538 137 TYR   A CD1   
1126 C  CD2   . TYR   A 138 ? 0.49417 0.44081 0.42886 0.02162  -0.02641 -0.03461 137 TYR   A CD2   
1127 C  CE1   . TYR   A 138 ? 0.58171 0.53193 0.50421 0.02824  -0.01404 -0.03486 137 TYR   A CE1   
1128 C  CE2   . TYR   A 138 ? 0.58107 0.53010 0.50834 0.02477  -0.01952 -0.03450 137 TYR   A CE2   
1129 C  CZ    . TYR   A 138 ? 0.57370 0.52465 0.49530 0.02809  -0.01330 -0.03439 137 TYR   A CZ    
1130 O  OH    . TYR   A 138 ? 0.55787 0.51183 0.47395 0.03111  -0.00635 -0.03337 137 TYR   A OH    
1131 N  N     . GLY   A 139 ? 0.52360 0.45378 0.47993 0.01597  -0.05427 -0.03571 138 GLY   A N     
1132 C  CA    . GLY   A 139 ? 0.51348 0.44482 0.48495 0.01102  -0.06064 -0.03291 138 GLY   A CA    
1133 C  C     . GLY   A 139 ? 0.50363 0.43908 0.48670 0.00675  -0.06248 -0.02955 138 GLY   A C     
1134 O  O     . GLY   A 139 ? 0.48661 0.42817 0.48510 0.00188  -0.06347 -0.02525 138 GLY   A O     
1135 N  N     . ILE   A 140 ? 0.47178 0.40387 0.44798 0.00876  -0.06303 -0.03106 139 ILE   A N     
1136 C  CA    . ILE   A 140 ? 0.47396 0.41065 0.46083 0.00481  -0.06386 -0.02773 139 ILE   A CA    
1137 C  C     . ILE   A 140 ? 0.48129 0.40616 0.46334 0.00727  -0.07396 -0.03024 139 ILE   A C     
1138 O  O     . ILE   A 140 ? 0.46066 0.37440 0.42785 0.01297  -0.07818 -0.03497 139 ILE   A O     
1139 C  CB    . ILE   A 140 ? 0.38807 0.33465 0.37325 0.00393  -0.05323 -0.02639 139 ILE   A CB    
1140 C  CG1   . ILE   A 140 ? 0.44862 0.38948 0.41671 0.00947  -0.05089 -0.03055 139 ILE   A CG1   
1141 C  CG2   . ILE   A 140 ? 0.39968 0.35730 0.39060 0.00142  -0.04442 -0.02380 139 ILE   A CG2   
1142 C  CD1   . ILE   A 140 ? 0.36771 0.31760 0.33443 0.00873  -0.04118 -0.02921 139 ILE   A CD1   
1143 N  N     . PRO   A 141 ? 0.44116 0.36760 0.43554 0.00346  -0.07842 -0.02699 140 PRO   A N     
1144 C  CA    . PRO   A 141 ? 0.41330 0.32834 0.40344 0.00570  -0.08833 -0.02937 140 PRO   A CA    
1145 C  C     . PRO   A 141 ? 0.35940 0.27287 0.33548 0.00943  -0.08371 -0.03229 140 PRO   A C     
1146 O  O     . PRO   A 141 ? 0.39802 0.32136 0.37267 0.00855  -0.07306 -0.03100 140 PRO   A O     
1147 C  CB    . PRO   A 141 ? 0.44586 0.36574 0.45581 -0.00012 -0.09261 -0.02381 140 PRO   A CB    
1148 C  CG    . PRO   A 141 ? 0.43105 0.36227 0.45503 -0.00450 -0.08708 -0.01879 140 PRO   A CG    
1149 C  CD    . PRO   A 141 ? 0.42037 0.35797 0.43383 -0.00263 -0.07579 -0.02067 140 PRO   A CD    
1150 N  N     . PHE   A 142 ? 0.43167 0.33188 0.39728 0.01392  -0.09246 -0.03624 141 PHE   A N     
1151 C  CA    . PHE   A 142 ? 0.42789 0.32413 0.38031 0.01803  -0.09053 -0.03898 141 PHE   A CA    
1152 C  C     . PHE   A 142 ? 0.45380 0.34303 0.41154 0.01688  -0.10063 -0.03878 141 PHE   A C     
1153 O  O     . PHE   A 142 ? 0.45604 0.33408 0.41542 0.01792  -0.11276 -0.04029 141 PHE   A O     
1154 C  CB    . PHE   A 142 ? 0.49338 0.37835 0.42414 0.02659  -0.09130 -0.04447 141 PHE   A CB    
1155 C  CG    . PHE   A 142 ? 0.49236 0.37038 0.40907 0.03183  -0.09179 -0.04732 141 PHE   A CG    
1156 C  CD1   . PHE   A 142 ? 0.45619 0.34369 0.37181 0.03091  -0.08161 -0.04562 141 PHE   A CD1   
1157 C  CD2   . PHE   A 142 ? 0.48969 0.35119 0.39419 0.03792  -0.10288 -0.05169 141 PHE   A CD2   
1158 C  CE1   . PHE   A 142 ? 0.43066 0.31211 0.33379 0.03576  -0.08178 -0.04790 141 PHE   A CE1   
1159 C  CE2   . PHE   A 142 ? 0.53780 0.39262 0.42881 0.04322  -0.10324 -0.05422 141 PHE   A CE2   
1160 C  CZ    . PHE   A 142 ? 0.52954 0.39465 0.42007 0.04207  -0.09242 -0.05219 141 PHE   A CZ    
1161 N  N     . ILE   A 143 ? 0.40575 0.30081 0.36575 0.01505  -0.09614 -0.03710 142 ILE   A N     
1162 C  CA    . ILE   A 143 ? 0.43457 0.32440 0.40026 0.01364  -0.10452 -0.03647 142 ILE   A CA    
1163 C  C     . ILE   A 143 ? 0.42389 0.31021 0.37434 0.01822  -0.10121 -0.03960 142 ILE   A C     
1164 O  O     . ILE   A 143 ? 0.45884 0.35458 0.40522 0.01824  -0.08970 -0.03878 142 ILE   A O     
1165 C  CB    . ILE   A 143 ? 0.39160 0.29374 0.37896 0.00592  -0.10223 -0.02990 142 ILE   A CB    
1166 C  CG1   . ILE   A 143 ? 0.44672 0.35448 0.44928 0.00171  -0.10305 -0.02593 142 ILE   A CG1   
1167 C  CG2   . ILE   A 143 ? 0.44393 0.33933 0.43875 0.00449  -0.11274 -0.02896 142 ILE   A CG2   
1168 C  CD1   . ILE   A 143 ? 0.52079 0.41699 0.52958 0.00179  -0.11733 -0.02641 142 ILE   A CD1   
1169 N  N     . GLU   A 144 ? 0.42154 0.29392 0.36348 0.02237  -0.11156 -0.04314 143 GLU   A N     
1170 C  CA    . GLU   A 144 ? 0.45460 0.32318 0.38393 0.02641  -0.10971 -0.04555 143 GLU   A CA    
1171 C  C     . GLU   A 144 ? 0.44412 0.31861 0.38740 0.02076  -0.11081 -0.04193 143 GLU   A C     
1172 O  O     . GLU   A 144 ? 0.43280 0.30483 0.39049 0.01673  -0.12016 -0.03963 143 GLU   A O     
1173 C  CB    . GLU   A 144 ? 0.48252 0.33216 0.39451 0.03444  -0.12069 -0.05130 143 GLU   A CB    
1174 C  CG    . GLU   A 144 ? 0.62750 0.46910 0.52291 0.04163  -0.12038 -0.05523 143 GLU   A CG    
1175 C  CD    . GLU   A 144 ? 0.74315 0.56685 0.61702 0.05137  -0.12818 -0.06092 143 GLU   A CD    
1176 O  OE1   . GLU   A 144 ? 0.80334 0.61635 0.67849 0.05178  -0.14020 -0.06254 143 GLU   A OE1   
1177 O  OE2   . GLU   A 144 ? 0.87035 0.69068 0.72600 0.05897  -0.12211 -0.06348 143 GLU   A OE2   
1178 N  N     . THR   A 145 ? 0.44258 0.32437 0.38182 0.02076  -0.10173 -0.04124 144 THR   A N     
1179 C  CA    . THR   A 145 ? 0.41817 0.30619 0.37032 0.01554  -0.10199 -0.03765 144 THR   A CA    
1180 C  C     . THR   A 145 ? 0.39744 0.28169 0.33724 0.01931  -0.10032 -0.04015 144 THR   A C     
1181 O  O     . THR   A 145 ? 0.39939 0.28046 0.32204 0.02529  -0.09513 -0.04344 144 THR   A O     
1182 C  CB    . THR   A 145 ? 0.36861 0.27413 0.33515 0.00916  -0.09109 -0.03217 144 THR   A CB    
1183 O  OG1   . THR   A 145 ? 0.36312 0.27514 0.31907 0.01148  -0.07950 -0.03323 144 THR   A OG1   
1184 C  CG2   . THR   A 145 ? 0.36177 0.27276 0.34165 0.00523  -0.09137 -0.02888 144 THR   A CG2   
1185 N  N     . SER   A 146 ? 0.39031 0.27637 0.34034 0.01550  -0.10375 -0.03776 145 SER   A N     
1186 C  CA    . SER   A 146 ? 0.39013 0.27715 0.33311 0.01700  -0.09986 -0.03857 145 SER   A CA    
1187 C  C     . SER   A 146 ? 0.37494 0.27468 0.33595 0.00974  -0.09587 -0.03302 145 SER   A C     
1188 O  O     . SER   A 146 ? 0.37483 0.27334 0.35016 0.00582  -0.10381 -0.03019 145 SER   A O     
1189 C  CB    . SER   A 146 ? 0.40797 0.27886 0.34024 0.02204  -0.11131 -0.04282 145 SER   A CB    
1190 O  OG    . SER   A 146 ? 0.40665 0.27996 0.33513 0.02238  -0.10747 -0.04277 145 SER   A OG    
1191 N  N     . ALA   A 147 ? 0.36969 0.28127 0.33020 0.00829  -0.08389 -0.03121 146 ALA   A N     
1192 C  CA    . ALA   A 147 ? 0.37294 0.29522 0.34716 0.00279  -0.07994 -0.02653 146 ALA   A CA    
1193 C  C     . ALA   A 147 ? 0.37746 0.29334 0.34996 0.00350  -0.08601 -0.02753 146 ALA   A C     
1194 O  O     . ALA   A 147 ? 0.36847 0.29000 0.35493 -0.00114 -0.08703 -0.02339 146 ALA   A O     
1195 C  CB    . ALA   A 147 ? 0.33803 0.27262 0.31006 0.00190  -0.06669 -0.02511 146 ALA   A CB    
1196 N  N     . LYS   A 148 ? 0.37390 0.27768 0.32945 0.00964  -0.09030 -0.03276 147 LYS   A N     
1197 C  CA    . LYS   A 148 ? 0.45712 0.35411 0.40900 0.01102  -0.09584 -0.03422 147 LYS   A CA    
1198 C  C     . LYS   A 148 ? 0.38727 0.27465 0.34863 0.00947  -0.10991 -0.03384 147 LYS   A C     
1199 O  O     . LYS   A 148 ? 0.43764 0.32638 0.40917 0.00611  -0.11353 -0.03129 147 LYS   A O     
1200 C  CB    . LYS   A 148 ? 0.39121 0.27854 0.32074 0.01895  -0.09492 -0.03964 147 LYS   A CB    
1201 C  CG    . LYS   A 148 ? 0.44926 0.33043 0.37413 0.02056  -0.09940 -0.04111 147 LYS   A CG    
1202 C  CD    . LYS   A 148 ? 0.49334 0.36493 0.39564 0.02918  -0.09802 -0.04597 147 LYS   A CD    
1203 C  CE    . LYS   A 148 ? 0.51916 0.37948 0.41553 0.03197  -0.10697 -0.04849 147 LYS   A CE    
1204 N  NZ    . LYS   A 148 ? 0.60055 0.47087 0.50374 0.02786  -0.10066 -0.04564 147 LYS   A NZ    
1205 N  N     . THR   A 149 ? 0.39979 0.27748 0.35890 0.01177  -0.11822 -0.03603 148 THR   A N     
1206 C  CA    . THR   A 149 ? 0.40710 0.27451 0.37578 0.01049  -0.13288 -0.03570 148 THR   A CA    
1207 C  C     . THR   A 149 ? 0.39673 0.27257 0.38839 0.00364  -0.13450 -0.02956 148 THR   A C     
1208 O  O     . THR   A 149 ? 0.40253 0.27195 0.40665 0.00141  -0.14635 -0.02772 148 THR   A O     
1209 C  CB    . THR   A 149 ? 0.42718 0.27656 0.37981 0.01765  -0.14344 -0.04191 148 THR   A CB    
1210 O  OG1   . THR   A 149 ? 0.45245 0.30336 0.40397 0.01832  -0.14097 -0.04220 148 THR   A OG1   
1211 C  CG2   . THR   A 149 ? 0.49616 0.33657 0.42458 0.02577  -0.14138 -0.04765 148 THR   A CG2   
1212 N  N     . ARG   A 150 ? 0.38265 0.27194 0.38000 0.00074  -0.12339 -0.02630 149 ARG   A N     
1213 C  CA    . ARG   A 150 ? 0.37269 0.27083 0.38946 -0.00468 -0.12274 -0.02045 149 ARG   A CA    
1214 C  C     . ARG   A 150 ? 0.38161 0.27110 0.39670 -0.00273 -0.13022 -0.02263 149 ARG   A C     
1215 O  O     . ARG   A 150 ? 0.37491 0.27106 0.40522 -0.00671 -0.12982 -0.01797 149 ARG   A O     
1216 C  CB    . ARG   A 150 ? 0.37051 0.27291 0.40971 -0.01035 -0.12818 -0.01385 149 ARG   A CB    
1217 C  CG    . ARG   A 150 ? 0.40438 0.31351 0.44510 -0.01193 -0.12256 -0.01192 149 ARG   A CG    
1218 C  CD    . ARG   A 150 ? 0.38445 0.30062 0.44897 -0.01764 -0.12550 -0.00402 149 ARG   A CD    
1219 N  NE    . ARG   A 150 ? 0.51956 0.45171 0.59471 -0.02105 -0.11381 0.00193  149 ARG   A NE    
1220 C  CZ    . ARG   A 150 ? 0.47045 0.40795 0.55849 -0.02344 -0.11327 0.00650  149 ARG   A CZ    
1221 N  NH1   . ARG   A 150 ? 0.52556 0.45479 0.62184 -0.02395 -0.12451 0.00709  149 ARG   A NH1   
1222 N  NH2   . ARG   A 150 ? 0.46026 0.41111 0.55233 -0.02500 -0.10145 0.01036  149 ARG   A NH2   
1223 N  N     . GLN   A 151 ? 0.39734 0.27244 0.39370 0.00375  -0.13636 -0.02942 150 GLN   A N     
1224 C  CA    . GLN   A 151 ? 0.40617 0.27284 0.40042 0.00588  -0.14350 -0.03158 150 GLN   A CA    
1225 C  C     . GLN   A 151 ? 0.39370 0.27235 0.39130 0.00383  -0.13264 -0.02920 150 GLN   A C     
1226 O  O     . GLN   A 151 ? 0.39886 0.28507 0.38643 0.00537  -0.12062 -0.03027 150 GLN   A O     
1227 C  CB    . GLN   A 151 ? 0.46763 0.31771 0.43772 0.01450  -0.14935 -0.03942 150 GLN   A CB    
1228 C  CG    . GLN   A 151 ? 0.56882 0.40860 0.53484 0.01753  -0.15753 -0.04221 150 GLN   A CG    
1229 C  CD    . GLN   A 151 ? 0.66912 0.49538 0.60832 0.02717  -0.15884 -0.04956 150 GLN   A CD    
1230 O  OE1   . GLN   A 151 ? 0.65829 0.47541 0.58363 0.03225  -0.16190 -0.05325 150 GLN   A OE1   
1231 N  NE2   . GLN   A 151 ? 0.67106 0.49626 0.60239 0.03017  -0.15591 -0.05143 150 GLN   A NE2   
1232 N  N     . GLY   A 152 ? 0.39733 0.27816 0.41045 0.00010  -0.13698 -0.02548 151 GLY   A N     
1233 C  CA    . GLY   A 152 ? 0.38099 0.27111 0.39694 -0.00138 -0.12856 -0.02362 151 GLY   A CA    
1234 C  C     . GLY   A 152 ? 0.38165 0.28970 0.40849 -0.00615 -0.11536 -0.01794 151 GLY   A C     
1235 O  O     . GLY   A 152 ? 0.38407 0.29962 0.41370 -0.00733 -0.10875 -0.01627 151 GLY   A O     
1236 N  N     . VAL   A 153 ? 0.36105 0.27576 0.39374 -0.00861 -0.11157 -0.01497 152 VAL   A N     
1237 C  CA    . VAL   A 153 ? 0.35125 0.28176 0.38983 -0.01169 -0.09838 -0.01066 152 VAL   A CA    
1238 C  C     . VAL   A 153 ? 0.32971 0.26970 0.38771 -0.01624 -0.09673 -0.00378 152 VAL   A C     
1239 O  O     . VAL   A 153 ? 0.32135 0.26967 0.37897 -0.01669 -0.08802 -0.00259 152 VAL   A O     
1240 C  CB    . VAL   A 153 ? 0.34501 0.27983 0.38564 -0.01304 -0.09544 -0.00892 152 VAL   A CB    
1241 C  CG1   . VAL   A 153 ? 0.31907 0.26973 0.36815 -0.01628 -0.08328 -0.00367 152 VAL   A CG1   
1242 C  CG2   . VAL   A 153 ? 0.34266 0.27017 0.36290 -0.00816 -0.09431 -0.01541 152 VAL   A CG2   
1243 N  N     . ASP   A 154 ? 0.33071 0.27002 0.40662 -0.01955 -0.10473 0.00140  153 ASP   A N     
1244 C  CA    . ASP   A 154 ? 0.35416 0.30214 0.44916 -0.02330 -0.10337 0.00865  153 ASP   A CA    
1245 C  C     . ASP   A 154 ? 0.35320 0.29793 0.44418 -0.02196 -0.10460 0.00629  153 ASP   A C     
1246 O  O     . ASP   A 154 ? 0.36149 0.31581 0.45894 -0.02349 -0.09727 0.01002  153 ASP   A O     
1247 C  CB    . ASP   A 154 ? 0.32596 0.27153 0.44145 -0.02657 -0.11385 0.01460  153 ASP   A CB    
1248 C  CG    . ASP   A 154 ? 0.44924 0.40189 0.57394 -0.02880 -0.11066 0.01950  153 ASP   A CG    
1249 O  OD1   . ASP   A 154 ? 0.52880 0.49193 0.64978 -0.02884 -0.09882 0.02087  153 ASP   A OD1   
1250 O  OD2   . ASP   A 154 ? 0.51557 0.46294 0.65131 -0.03039 -0.12036 0.02199  153 ASP   A OD2   
1251 N  N     . ASP   A 155 ? 0.34463 0.27530 0.42483 -0.01878 -0.11429 0.00019  154 ASP   A N     
1252 C  CA    . ASP   A 155 ? 0.37337 0.29968 0.45085 -0.01746 -0.11718 -0.00187 154 ASP   A CA    
1253 C  C     . ASP   A 155 ? 0.33591 0.26952 0.40130 -0.01571 -0.10473 -0.00421 154 ASP   A C     
1254 O  O     . ASP   A 155 ? 0.35664 0.29507 0.42750 -0.01686 -0.10180 -0.00209 154 ASP   A O     
1255 C  CB    . ASP   A 155 ? 0.39834 0.30704 0.46294 -0.01312 -0.12956 -0.00877 154 ASP   A CB    
1256 C  CG    . ASP   A 155 ? 0.58135 0.48389 0.64335 -0.01149 -0.13429 -0.01102 154 ASP   A CG    
1257 O  OD1   . ASP   A 155 ? 0.64522 0.55591 0.72208 -0.01507 -0.13196 -0.00571 154 ASP   A OD1   
1258 O  OD2   . ASP   A 155 ? 0.65314 0.54225 0.69770 -0.00615 -0.14046 -0.01804 154 ASP   A OD2   
1259 N  N     . ALA   A 156 ? 0.36415 0.29897 0.41424 -0.01306 -0.09743 -0.00813 155 ALA   A N     
1260 C  CA    . ALA   A 156 ? 0.32772 0.26936 0.36724 -0.01146 -0.08602 -0.01007 155 ALA   A CA    
1261 C  C     . ALA   A 156 ? 0.31317 0.26933 0.36615 -0.01537 -0.07703 -0.00375 155 ALA   A C     
1262 O  O     . ALA   A 156 ? 0.30887 0.26924 0.36238 -0.01550 -0.07267 -0.00318 155 ALA   A O     
1263 C  CB    . ALA   A 156 ? 0.32924 0.26982 0.35267 -0.00823 -0.08053 -0.01433 155 ALA   A CB    
1264 N  N     . PHE   A 157 ? 0.30610 0.26973 0.36965 -0.01815 -0.07422 0.00116  156 PHE   A N     
1265 C  CA    . PHE   A 157 ? 0.29377 0.27051 0.36884 -0.02082 -0.06564 0.00739  156 PHE   A CA    
1266 C  C     . PHE   A 157 ? 0.29266 0.27140 0.38383 -0.02315 -0.06960 0.01272  156 PHE   A C     
1267 O  O     . PHE   A 157 ? 0.28574 0.27195 0.38017 -0.02360 -0.06303 0.01526  156 PHE   A O     
1268 C  CB    . PHE   A 157 ? 0.28768 0.27138 0.37001 -0.02258 -0.06198 0.01172  156 PHE   A CB    
1269 C  CG    . PHE   A 157 ? 0.28548 0.27070 0.35344 -0.02064 -0.05515 0.00763  156 PHE   A CG    
1270 C  CD1   . PHE   A 157 ? 0.27678 0.27083 0.34023 -0.02013 -0.04454 0.00803  156 PHE   A CD1   
1271 C  CD2   . PHE   A 157 ? 0.29272 0.27010 0.35173 -0.01909 -0.05973 0.00344  156 PHE   A CD2   
1272 C  CE1   . PHE   A 157 ? 0.27497 0.27025 0.32639 -0.01849 -0.03885 0.00457  156 PHE   A CE1   
1273 C  CE2   . PHE   A 157 ? 0.29059 0.26973 0.33711 -0.01726 -0.05323 0.00013  156 PHE   A CE2   
1274 C  CZ    . PHE   A 157 ? 0.28153 0.26975 0.32485 -0.01714 -0.04290 0.00082  156 PHE   A CZ    
1275 N  N     . TYR   A 158 ? 0.29990 0.27165 0.40150 -0.02451 -0.08070 0.01455  157 TYR   A N     
1276 C  CA    . TYR   A 158 ? 0.30093 0.27514 0.42015 -0.02698 -0.08467 0.02061  157 TYR   A CA    
1277 C  C     . TYR   A 158 ? 0.30165 0.27196 0.41387 -0.02546 -0.08551 0.01690  157 TYR   A C     
1278 O  O     . TYR   A 158 ? 0.31617 0.29294 0.43884 -0.02693 -0.08264 0.02159  157 TYR   A O     
1279 C  CB    . TYR   A 158 ? 0.30657 0.27325 0.43967 -0.02887 -0.09770 0.02346  157 TYR   A CB    
1280 C  CG    . TYR   A 158 ? 0.34268 0.31379 0.48809 -0.03106 -0.09819 0.02906  157 TYR   A CG    
1281 C  CD1   . TYR   A 158 ? 0.32303 0.30338 0.46470 -0.03087 -0.08765 0.03052  157 TYR   A CD1   
1282 C  CD2   . TYR   A 158 ? 0.36490 0.33045 0.52600 -0.03321 -0.10980 0.03293  157 TYR   A CD2   
1283 C  CE1   . TYR   A 158 ? 0.39730 0.38146 0.54990 -0.03263 -0.08815 0.03565  157 TYR   A CE1   
1284 C  CE2   . TYR   A 158 ? 0.37944 0.34893 0.55246 -0.03519 -0.11050 0.03832  157 TYR   A CE2   
1285 C  CZ    . TYR   A 158 ? 0.39065 0.36970 0.55928 -0.03485 -0.09934 0.03976  157 TYR   A CZ    
1286 O  OH    . TYR   A 158 ? 0.43532 0.41822 0.61590 -0.03664 -0.10008 0.04529  157 TYR   A OH    
1287 N  N     . THR   A 159 ? 0.31105 0.27051 0.40579 -0.02215 -0.08965 0.00879  158 THR   A N     
1288 C  CA    . THR   A 159 ? 0.31753 0.27324 0.40406 -0.02020 -0.08977 0.00500  158 THR   A CA    
1289 C  C     . THR   A 159 ? 0.30327 0.26997 0.38617 -0.02014 -0.07707 0.00593  158 THR   A C     
1290 O  O     . THR   A 159 ? 0.32793 0.29721 0.41462 -0.02060 -0.07558 0.00728  158 THR   A O     
1291 C  CB    . THR   A 159 ? 0.35831 0.30095 0.42478 -0.01560 -0.09486 -0.00359 158 THR   A CB    
1292 O  OG1   . THR   A 159 ? 0.36079 0.29177 0.43058 -0.01524 -0.10810 -0.00463 158 THR   A OG1   
1293 C  CG2   . THR   A 159 ? 0.37082 0.30986 0.42842 -0.01319 -0.09440 -0.00728 158 THR   A CG2   
1294 N  N     . LEU   A 160 ? 0.29714 0.26988 0.37251 -0.01945 -0.06825 0.00509  159 LEU   A N     
1295 C  CA    . LEU   A 160 ? 0.28748 0.26995 0.35946 -0.01923 -0.05694 0.00590  159 LEU   A CA    
1296 C  C     . LEU   A 160 ? 0.28606 0.27833 0.37489 -0.02193 -0.05351 0.01360  159 LEU   A C     
1297 O  O     . LEU   A 160 ? 0.27489 0.27167 0.36379 -0.02169 -0.04861 0.01437  159 LEU   A O     
1298 C  CB    . LEU   A 160 ? 0.28320 0.26971 0.34562 -0.01812 -0.04946 0.00402  159 LEU   A CB    
1299 C  CG    . LEU   A 160 ? 0.27426 0.26972 0.33265 -0.01761 -0.03871 0.00442  159 LEU   A CG    
1300 C  CD1   . LEU   A 160 ? 0.28261 0.27488 0.33122 -0.01557 -0.03744 0.00007  159 LEU   A CD1   
1301 C  CD2   . LEU   A 160 ? 0.27460 0.27329 0.32444 -0.01661 -0.03248 0.00266  159 LEU   A CD2   
1302 N  N     . VAL   A 161 ? 0.27760 0.27301 0.38131 -0.02423 -0.05628 0.01975  160 VAL   A N     
1303 C  CA    . VAL   A 161 ? 0.27088 0.27550 0.39172 -0.02614 -0.05312 0.02817  160 VAL   A CA    
1304 C  C     . VAL   A 161 ? 0.27397 0.27561 0.40227 -0.02691 -0.05850 0.02945  160 VAL   A C     
1305 O  O     . VAL   A 161 ? 0.29512 0.30369 0.42888 -0.02700 -0.05303 0.03321  160 VAL   A O     
1306 C  CB    . VAL   A 161 ? 0.26966 0.27765 0.40602 -0.02818 -0.05571 0.03508  160 VAL   A CB    
1307 C  CG1   . VAL   A 161 ? 0.26930 0.28624 0.42471 -0.02959 -0.05308 0.04474  160 VAL   A CG1   
1308 C  CG2   . VAL   A 161 ? 0.26523 0.27787 0.39448 -0.02728 -0.04874 0.03446  160 VAL   A CG2   
1309 N  N     . ARG   A 162 ? 0.28672 0.27751 0.41493 -0.02714 -0.06958 0.02626  161 ARG   A N     
1310 C  CA    . ARG   A 162 ? 0.31324 0.30001 0.44736 -0.02767 -0.07552 0.02674  161 ARG   A CA    
1311 C  C     . ARG   A 162 ? 0.36471 0.35234 0.48571 -0.02561 -0.06935 0.02209  161 ARG   A C     
1312 O  O     . ARG   A 162 ? 0.37578 0.36676 0.50410 -0.02632 -0.06831 0.02511  161 ARG   A O     
1313 C  CB    . ARG   A 162 ? 0.31875 0.29169 0.45108 -0.02732 -0.08909 0.02255  161 ARG   A CB    
1314 C  CG    . ARG   A 162 ? 0.37320 0.34486 0.52165 -0.02979 -0.09676 0.02792  161 ARG   A CG    
1315 C  CD    . ARG   A 162 ? 0.39356 0.35026 0.54117 -0.02925 -0.11179 0.02388  161 ARG   A CD    
1316 N  NE    . ARG   A 162 ? 0.38610 0.34155 0.54869 -0.03161 -0.11900 0.02881  161 ARG   A NE    
1317 C  CZ    . ARG   A 162 ? 0.40805 0.35647 0.56266 -0.03045 -0.12351 0.02488  161 ARG   A CZ    
1318 N  NH1   . ARG   A 162 ? 0.44023 0.38100 0.57189 -0.02659 -0.12261 0.01590  161 ARG   A NH1   
1319 N  NH2   . ARG   A 162 ? 0.43437 0.38332 0.60487 -0.03301 -0.12919 0.03045  161 ARG   A NH2   
1320 N  N     . GLU   A 163 ? 0.35039 0.33502 0.45257 -0.02297 -0.06531 0.01505  162 GLU   A N     
1321 C  CA    . GLU   A 163 ? 0.33880 0.32462 0.42920 -0.02100 -0.05918 0.01102  162 GLU   A CA    
1322 C  C     . GLU   A 163 ? 0.34941 0.34742 0.44585 -0.02185 -0.04897 0.01597  162 GLU   A C     
1323 O  O     . GLU   A 163 ? 0.36320 0.36342 0.46006 -0.02159 -0.04646 0.01626  162 GLU   A O     
1324 C  CB    . GLU   A 163 ? 0.36970 0.35108 0.44070 -0.01793 -0.05617 0.00380  162 GLU   A CB    
1325 C  CG    . GLU   A 163 ? 0.38859 0.35668 0.44917 -0.01539 -0.06536 -0.00215 162 GLU   A CG    
1326 C  CD    . GLU   A 163 ? 0.47233 0.43375 0.53195 -0.01438 -0.07125 -0.00418 162 GLU   A CD    
1327 O  OE1   . GLU   A 163 ? 0.48397 0.44798 0.53697 -0.01311 -0.06557 -0.00606 162 GLU   A OE1   
1328 O  OE2   . GLU   A 163 ? 0.46219 0.41547 0.52805 -0.01485 -0.08204 -0.00386 162 GLU   A OE2   
1329 N  N     . ILE   A 164 ? 0.32924 0.33472 0.42929 -0.02238 -0.04304 0.01963  163 ILE   A N     
1330 C  CA    . ILE   A 164 ? 0.33347 0.34962 0.43849 -0.02230 -0.03381 0.02454  163 ILE   A CA    
1331 C  C     . ILE   A 164 ? 0.36680 0.38693 0.48887 -0.02382 -0.03567 0.03184  163 ILE   A C     
1332 O  O     . ILE   A 164 ? 0.39373 0.41914 0.51727 -0.02308 -0.03031 0.03397  163 ILE   A O     
1333 C  CB    . ILE   A 164 ? 0.39449 0.41676 0.50030 -0.02209 -0.02824 0.02734  163 ILE   A CB    
1334 C  CG1   . ILE   A 164 ? 0.26235 0.28194 0.35140 -0.02044 -0.02504 0.02051  163 ILE   A CG1   
1335 C  CG2   . ILE   A 164 ? 0.31654 0.34917 0.42926 -0.02129 -0.01981 0.03372  163 ILE   A CG2   
1336 C  CD1   . ILE   A 164 ? 0.29184 0.31523 0.38188 -0.02053 -0.02206 0.02263  163 ILE   A CD1   
1337 N  N     . ARG   A 165 ? 0.31578 0.33336 0.45150 -0.02586 -0.04347 0.03605  164 ARG   A N     
1338 C  CA    . ARG   A 165 ? 0.37578 0.39735 0.53021 -0.02746 -0.04578 0.04407  164 ARG   A CA    
1339 C  C     . ARG   A 165 ? 0.41756 0.43577 0.57040 -0.02733 -0.04827 0.04174  164 ARG   A C     
1340 O  O     . ARG   A 165 ? 0.44712 0.47195 0.60857 -0.02727 -0.04403 0.04708  164 ARG   A O     
1341 C  CB    . ARG   A 165 ? 0.33046 0.34801 0.49969 -0.02985 -0.05560 0.04816  164 ARG   A CB    
1342 C  CG    . ARG   A 165 ? 0.35952 0.38461 0.53974 -0.03042 -0.05185 0.05540  164 ARG   A CG    
1343 C  CD    . ARG   A 165 ? 0.35472 0.37477 0.54933 -0.03294 -0.06258 0.05886  164 ARG   A CD    
1344 N  NE    . ARG   A 165 ? 0.39969 0.42729 0.60525 -0.03339 -0.05870 0.06619  164 ARG   A NE    
1345 C  CZ    . ARG   A 165 ? 0.33951 0.36417 0.55750 -0.03546 -0.06651 0.06974  164 ARG   A CZ    
1346 N  NH1   . ARG   A 165 ? 0.39657 0.41044 0.61774 -0.03717 -0.07916 0.06663  164 ARG   A NH1   
1347 N  NH2   . ARG   A 165 ? 0.44946 0.48175 0.67664 -0.03551 -0.06179 0.07656  164 ARG   A NH2   
1348 N  N     . LYS   A 166 ? 0.42812 0.43593 0.56952 -0.02682 -0.05496 0.03393  165 LYS   A N     
1349 C  CA    . LYS   A 166 ? 0.47558 0.47951 0.61417 -0.02640 -0.05752 0.03119  165 LYS   A CA    
1350 C  C     . LYS   A 166 ? 0.52020 0.53020 0.64900 -0.02460 -0.04728 0.02934  165 LYS   A C     
1351 O  O     . LYS   A 166 ? 0.55944 0.57175 0.69279 -0.02471 -0.04615 0.03131  165 LYS   A O     
1352 C  CB    . LYS   A 166 ? 0.49786 0.48873 0.62438 -0.02524 -0.06657 0.02312  165 LYS   A CB    
1353 C  CG    . LYS   A 166 ? 0.45287 0.43621 0.59011 -0.02687 -0.07860 0.02495  165 LYS   A CG    
1354 C  CD    . LYS   A 166 ? 0.60189 0.57068 0.72660 -0.02479 -0.08877 0.01699  165 LYS   A CD    
1355 C  CE    . LYS   A 166 ? 0.53004 0.49501 0.63259 -0.02134 -0.08421 0.00906  165 LYS   A CE    
1356 N  NZ    . LYS   A 166 ? 0.58587 0.53612 0.67682 -0.01854 -0.09466 0.00237  165 LYS   A NZ    
1357 N  N     . HIS   A 167 ? 0.47006 0.48264 0.58625 -0.02296 -0.04012 0.02587  166 HIS   A N     
1358 C  CA    . HIS   A 167 ? 0.46934 0.48719 0.57640 -0.02119 -0.03098 0.02403  166 HIS   A CA    
1359 C  C     . HIS   A 167 ? 0.47559 0.50338 0.59387 -0.02118 -0.02453 0.03166  166 HIS   A C     
1360 O  O     . HIS   A 167 ? 0.53799 0.56875 0.65406 -0.02012 -0.02016 0.03165  166 HIS   A O     
1361 C  CB    . HIS   A 167 ? 0.46177 0.47984 0.55509 -0.01964 -0.02594 0.01940  166 HIS   A CB    
1362 C  CG    . HIS   A 167 ? 0.47785 0.50113 0.56258 -0.01786 -0.01713 0.01775  166 HIS   A CG    
1363 N  ND1   . HIS   A 167 ? 0.58547 0.60540 0.65901 -0.01655 -0.01597 0.01214  166 HIS   A ND1   
1364 C  CD2   . HIS   A 167 ? 0.52291 0.55379 0.60808 -0.01683 -0.00951 0.02080  166 HIS   A CD2   
1365 C  CE1   . HIS   A 167 ? 0.54637 0.57172 0.61503 -0.01522 -0.00843 0.01196  166 HIS   A CE1   
1366 N  NE2   . HIS   A 167 ? 0.57822 0.60984 0.65317 -0.01520 -0.00462 0.01692  166 HIS   A NE2   
1367 N  N     . LYS   A 168 ? 0.48398 0.51685 0.61409 -0.02191 -0.02372 0.03844  167 LYS   A N     
1368 C  CA    . LYS   A 168 ? 0.49870 0.54097 0.63946 -0.02093 -0.01723 0.04660  167 LYS   A CA    
1369 C  C     . LYS   A 168 ? 0.56240 0.60532 0.71998 -0.02258 -0.02218 0.05287  167 LYS   A C     
1370 O  O     . LYS   A 168 ? 0.66433 0.71324 0.82809 -0.02138 -0.01739 0.05797  167 LYS   A O     
1371 C  CB    . LYS   A 168 ? 0.48293 0.53093 0.62890 -0.02028 -0.01328 0.05186  167 LYS   A CB    
1372 C  CG    . LYS   A 168 ? 0.51678 0.56233 0.64833 -0.01952 -0.01130 0.04558  167 LYS   A CG    
1373 C  CD    . LYS   A 168 ? 0.49298 0.54576 0.62312 -0.01714 -0.00315 0.04924  167 LYS   A CD    
1374 C  CE    . LYS   A 168 ? 0.53911 0.58923 0.65192 -0.01597 -0.00020 0.04150  167 LYS   A CE    
1375 N  NZ    . LYS   A 168 ? 0.62055 0.67663 0.72802 -0.01282 0.00815  0.04328  167 LYS   A NZ    
1376 N  N     . SER   B 1   ? 0.54231 0.61913 0.65529 0.01440  0.04328  0.06320  0   SER   B N     
1377 C  CA    . SER   B 1   ? 0.51144 0.58251 0.61074 0.01304  0.04126  0.05323  0   SER   B CA    
1378 C  C     . SER   B 1   ? 0.50235 0.56898 0.60076 0.00747  0.03509  0.04700  0   SER   B C     
1379 O  O     . SER   B 1   ? 0.50189 0.56856 0.61104 0.00381  0.03063  0.04942  0   SER   B O     
1380 C  CB    . SER   B 1   ? 0.55372 0.62373 0.65232 0.01322  0.04105  0.05188  0   SER   B CB    
1381 O  OG    . SER   B 1   ? 0.62831 0.69777 0.71563 0.01839  0.04569  0.05023  0   SER   B OG    
1382 N  N     . MET   B 2   ? 0.52218 0.58461 0.60781 0.00716  0.03460  0.03913  1   MET   B N     
1383 C  CA    . MET   B 2   ? 0.47958 0.53766 0.56273 0.00287  0.02955  0.03329  1   MET   B CA    
1384 C  C     . MET   B 2   ? 0.41782 0.47285 0.50548 -0.00068 0.02441  0.03124  1   MET   B C     
1385 O  O     . MET   B 2   ? 0.43935 0.49467 0.52796 0.00000  0.02505  0.03168  1   MET   B O     
1386 C  CB    . MET   B 2   ? 0.42487 0.47952 0.49438 0.00362  0.03052  0.02604  1   MET   B CB    
1387 C  CG    . MET   B 2   ? 0.37680 0.42891 0.43932 0.00419  0.03085  0.02139  1   MET   B CG    
1388 S  SD    . MET   B 2   ? 0.39161 0.44017 0.44097 0.00491  0.03156  0.01416  1   MET   B SD    
1389 C  CE    . MET   B 2   ? 0.38420 0.43554 0.42981 0.01040  0.03656  0.01787  1   MET   B CE    
1390 N  N     . THR   B 3   ? 0.38352 0.43513 0.47343 -0.00411 0.01905  0.02895  2   THR   B N     
1391 C  CA    . THR   B 3   ? 0.35868 0.40587 0.45121 -0.00702 0.01317  0.02626  2   THR   B CA    
1392 C  C     . THR   B 3   ? 0.32358 0.36696 0.40486 -0.00676 0.01348  0.01927  2   THR   B C     
1393 O  O     . THR   B 3   ? 0.34931 0.39121 0.42049 -0.00593 0.01548  0.01463  2   THR   B O     
1394 C  CB    . THR   B 3   ? 0.36343 0.40661 0.45817 -0.00971 0.00728  0.02470  2   THR   B CB    
1395 O  OG1   . THR   B 3   ? 0.39701 0.44412 0.50339 -0.01002 0.00704  0.03173  2   THR   B OG1   
1396 C  CG2   . THR   B 3   ? 0.36778 0.40526 0.46471 -0.01198 0.00034  0.02205  2   THR   B CG2   
1397 N  N     . GLU   B 4   ? 0.32190 0.36382 0.40574 -0.00748 0.01138  0.01890  3   GLU   B N     
1398 C  CA    . GLU   B 4   ? 0.28770 0.32586 0.36222 -0.00738 0.01114  0.01273  3   GLU   B CA    
1399 C  C     . GLU   B 4   ? 0.33042 0.36229 0.40368 -0.00949 0.00470  0.00882  3   GLU   B C     
1400 O  O     . GLU   B 4   ? 0.33064 0.36096 0.41257 -0.01111 -0.00036 0.01147  3   GLU   B O     
1401 C  CB    . GLU   B 4   ? 0.36045 0.40072 0.43690 -0.00619 0.01343  0.01439  3   GLU   B CB    
1402 C  CG    . GLU   B 4   ? 0.44771 0.49315 0.52365 -0.00299 0.01966  0.01807  3   GLU   B CG    
1403 C  CD    . GLU   B 4   ? 0.51806 0.56569 0.59715 -0.00143 0.02175  0.02079  3   GLU   B CD    
1404 O  OE1   . GLU   B 4   ? 0.54883 0.59368 0.62827 -0.00306 0.01875  0.01830  3   GLU   B OE1   
1405 O  OE2   . GLU   B 4   ? 0.47186 0.52375 0.55277 0.00180  0.02637  0.02557  3   GLU   B OE2   
1406 N  N     . TYR   B 5   ? 0.29363 0.32159 0.35617 -0.00905 0.00471  0.00282  4   TYR   B N     
1407 C  CA    . TYR   B 5   ? 0.28827 0.30944 0.34662 -0.00974 -0.00076 -0.00140 4   TYR   B CA    
1408 C  C     . TYR   B 5   ? 0.31591 0.33480 0.36758 -0.00879 0.00015  -0.00531 4   TYR   B C     
1409 O  O     . TYR   B 5   ? 0.31548 0.33559 0.36004 -0.00753 0.00455  -0.00784 4   TYR   B O     
1410 C  CB    . TYR   B 5   ? 0.29105 0.30920 0.34217 -0.00932 -0.00139 -0.00462 4   TYR   B CB    
1411 C  CG    . TYR   B 5   ? 0.33351 0.35302 0.39105 -0.01039 -0.00317 -0.00116 4   TYR   B CG    
1412 C  CD1   . TYR   B 5   ? 0.38139 0.39695 0.44532 -0.01176 -0.01004 0.00024  4   TYR   B CD1   
1413 C  CD2   . TYR   B 5   ? 0.30017 0.32471 0.35807 -0.00992 0.00160  0.00101  4   TYR   B CD2   
1414 C  CE1   . TYR   B 5   ? 0.40679 0.42377 0.47783 -0.01287 -0.01188 0.00385  4   TYR   B CE1   
1415 C  CE2   . TYR   B 5   ? 0.37519 0.40126 0.43911 -0.01076 0.00030  0.00442  4   TYR   B CE2   
1416 C  CZ    . TYR   B 5   ? 0.35140 0.37396 0.42236 -0.01237 -0.00631 0.00602  4   TYR   B CZ    
1417 O  OH    . TYR   B 5   ? 0.33713 0.36147 0.41497 -0.01327 -0.00759 0.00978  4   TYR   B OH    
1418 N  N     . LYS   B 6   ? 0.30256 0.31778 0.35677 -0.00936 -0.00442 -0.00576 5   LYS   B N     
1419 C  CA    . LYS   B 6   ? 0.28887 0.30144 0.33693 -0.00836 -0.00406 -0.00938 5   LYS   B CA    
1420 C  C     . LYS   B 6   ? 0.29810 0.30380 0.33635 -0.00692 -0.00696 -0.01437 5   LYS   B C     
1421 O  O     . LYS   B 6   ? 0.34811 0.34775 0.38632 -0.00684 -0.01329 -0.01549 5   LYS   B O     
1422 C  CB    . LYS   B 6   ? 0.34559 0.35772 0.40115 -0.00935 -0.00733 -0.00716 5   LYS   B CB    
1423 C  CG    . LYS   B 6   ? 0.34779 0.36699 0.41286 -0.00996 -0.00372 -0.00148 5   LYS   B CG    
1424 C  CD    . LYS   B 6   ? 0.45082 0.47002 0.52348 -0.01076 -0.00634 0.00095  5   LYS   B CD    
1425 C  CE    . LYS   B 6   ? 0.50621 0.53082 0.59228 -0.01162 -0.00589 0.00832  5   LYS   B CE    
1426 N  NZ    . LYS   B 6   ? 0.51818 0.54956 0.60435 -0.00994 0.00144  0.01158  5   LYS   B NZ    
1427 N  N     . LEU   B 7   ? 0.29369 0.29996 0.32356 -0.00535 -0.00252 -0.01715 6   LEU   B N     
1428 C  CA    . LEU   B 7   ? 0.28572 0.28626 0.30574 -0.00310 -0.00379 -0.02116 6   LEU   B CA    
1429 C  C     . LEU   B 7   ? 0.33056 0.32938 0.34534 -0.00145 -0.00233 -0.02363 6   LEU   B C     
1430 O  O     . LEU   B 7   ? 0.33423 0.33762 0.35107 -0.00199 0.00181  -0.02284 6   LEU   B O     
1431 C  CB    . LEU   B 7   ? 0.31089 0.31360 0.32629 -0.00227 0.00043  -0.02180 6   LEU   B CB    
1432 C  CG    . LEU   B 7   ? 0.33350 0.33993 0.35421 -0.00392 0.00105  -0.01901 6   LEU   B CG    
1433 C  CD1   . LEU   B 7   ? 0.35854 0.36624 0.37384 -0.00288 0.00471  -0.02012 6   LEU   B CD1   
1434 C  CD2   . LEU   B 7   ? 0.37113 0.37364 0.39588 -0.00483 -0.00529 -0.01795 6   LEU   B CD2   
1435 N  N     . VAL   B 8   ? 0.26914 0.26099 0.27674 0.00095  -0.00588 -0.02657 7   VAL   B N     
1436 C  CA    . VAL   B 8   ? 0.27181 0.26135 0.27372 0.00311  -0.00471 -0.02882 7   VAL   B CA    
1437 C  C     . VAL   B 8   ? 0.30181 0.28705 0.29291 0.00704  -0.00336 -0.03139 7   VAL   B C     
1438 O  O     . VAL   B 8   ? 0.30650 0.28580 0.29266 0.00893  -0.00750 -0.03272 7   VAL   B O     
1439 C  CB    . VAL   B 8   ? 0.28888 0.27325 0.29219 0.00316  -0.01076 -0.02955 7   VAL   B CB    
1440 C  CG1   . VAL   B 8   ? 0.29876 0.28056 0.29515 0.00587  -0.00918 -0.03199 7   VAL   B CG1   
1441 C  CG2   . VAL   B 8   ? 0.31323 0.30227 0.32854 -0.00052 -0.01194 -0.02604 7   VAL   B CG2   
1442 N  N     . VAL   B 9   ? 0.27566 0.26378 0.26348 0.00853  0.00228  -0.03173 8   VAL   B N     
1443 C  CA    . VAL   B 9   ? 0.28453 0.26974 0.26314 0.01268  0.00481  -0.03306 8   VAL   B CA    
1444 C  C     . VAL   B 9   ? 0.30393 0.28408 0.27580 0.01628  0.00390  -0.03490 8   VAL   B C     
1445 O  O     . VAL   B 9   ? 0.30116 0.28422 0.27595 0.01543  0.00614  -0.03454 8   VAL   B O     
1446 C  CB    . VAL   B 9   ? 0.27450 0.26632 0.25517 0.01222  0.01156  -0.03143 8   VAL   B CB    
1447 C  CG1   . VAL   B 9   ? 0.28036 0.26976 0.25279 0.01674  0.01454  -0.03178 8   VAL   B CG1   
1448 C  CG2   . VAL   B 9   ? 0.29297 0.28977 0.28045 0.00866  0.01222  -0.02967 8   VAL   B CG2   
1449 N  N     . VAL   B 10  ? 0.29909 0.27114 0.26136 0.02067  0.00034  -0.03696 9   VAL   B N     
1450 C  CA    . VAL   B 10  ? 0.35082 0.31645 0.30501 0.02501  -0.00150 -0.03896 9   VAL   B CA    
1451 C  C     . VAL   B 10  ? 0.38690 0.34814 0.32919 0.03156  0.00131  -0.03963 9   VAL   B C     
1452 O  O     . VAL   B 10  ? 0.36634 0.32757 0.30601 0.03275  0.00262  -0.03909 9   VAL   B O     
1453 C  CB    . VAL   B 10  ? 0.36565 0.32338 0.31872 0.02502  -0.01043 -0.04105 9   VAL   B CB    
1454 C  CG1   . VAL   B 10  ? 0.31259 0.27523 0.27854 0.01887  -0.01274 -0.03938 9   VAL   B CG1   
1455 C  CG2   . VAL   B 10  ? 0.34871 0.29907 0.29591 0.02731  -0.01605 -0.04250 9   VAL   B CG2   
1456 N  N     . GLY   B 11  ? 0.34235 0.29966 0.27714 0.03626  0.00231  -0.04058 10  GLY   B N     
1457 C  CA    . GLY   B 11  ? 0.36405 0.31731 0.28703 0.04364  0.00588  -0.04047 10  GLY   B CA    
1458 C  C     . GLY   B 11  ? 0.37401 0.32951 0.29497 0.04682  0.01153  -0.03912 10  GLY   B C     
1459 O  O     . GLY   B 11  ? 0.36812 0.32945 0.29781 0.04262  0.01338  -0.03818 10  GLY   B O     
1460 N  N     . ALA   B 12  ? 0.39820 0.34879 0.30742 0.05468  0.01428  -0.03881 11  ALA   B N     
1461 C  CA    . ALA   B 12  ? 0.42325 0.37467 0.32915 0.05902  0.01931  -0.03726 11  ALA   B CA    
1462 C  C     . ALA   B 12  ? 0.39059 0.35336 0.30845 0.05518  0.02700  -0.03318 11  ALA   B C     
1463 O  O     . ALA   B 12  ? 0.38295 0.35211 0.30927 0.05068  0.02905  -0.03147 11  ALA   B O     
1464 C  CB    . ALA   B 12  ? 0.41263 0.35694 0.30330 0.06909  0.02161  -0.03682 11  ALA   B CB    
1465 N  N     . VAL   B 13  ? 0.39516 0.35997 0.31362 0.05732  0.03097  -0.03156 12  VAL   B N     
1466 C  CA    . VAL   B 13  ? 0.39691 0.37162 0.32723 0.05393  0.03737  -0.02765 12  VAL   B CA    
1467 C  C     . VAL   B 13  ? 0.45829 0.43699 0.38973 0.05642  0.04322  -0.02371 12  VAL   B C     
1468 O  O     . VAL   B 13  ? 0.43097 0.40504 0.35184 0.06379  0.04534  -0.02269 12  VAL   B O     
1469 C  CB    . VAL   B 13  ? 0.44017 0.41534 0.36983 0.05690  0.04046  -0.02635 12  VAL   B CB    
1470 C  CG1   . VAL   B 13  ? 0.45451 0.43874 0.39491 0.05562  0.04758  -0.02137 12  VAL   B CG1   
1471 C  CG2   . VAL   B 13  ? 0.48988 0.46365 0.42273 0.05231  0.03511  -0.02972 12  VAL   B CG2   
1472 N  N     . GLY   B 14  ? 0.40732 0.39412 0.35116 0.05062  0.04553  -0.02148 13  GLY   B N     
1473 C  CA    . GLY   B 14  ? 0.42767 0.41943 0.37539 0.05229  0.05129  -0.01702 13  GLY   B CA    
1474 C  C     . GLY   B 14  ? 0.41199 0.40129 0.35445 0.05373  0.05035  -0.01750 13  GLY   B C     
1475 O  O     . GLY   B 14  ? 0.40877 0.40155 0.35324 0.05617  0.05538  -0.01352 13  GLY   B O     
1476 N  N     . VAL   B 15  ? 0.37983 0.36335 0.31635 0.05235  0.04401  -0.02187 14  VAL   B N     
1477 C  CA    . VAL   B 15  ? 0.41144 0.39238 0.34299 0.05379  0.04291  -0.02232 14  VAL   B CA    
1478 C  C     . VAL   B 15  ? 0.44265 0.43077 0.38556 0.04732  0.04372  -0.02095 14  VAL   B C     
1479 O  O     . VAL   B 15  ? 0.39523 0.38302 0.33592 0.04838  0.04433  -0.02027 14  VAL   B O     
1480 C  CB    . VAL   B 15  ? 0.38458 0.35633 0.30651 0.05471  0.03518  -0.02717 14  VAL   B CB    
1481 C  CG1   . VAL   B 15  ? 0.40489 0.36794 0.31344 0.06243  0.03385  -0.02874 14  VAL   B CG1   
1482 C  CG2   . VAL   B 15  ? 0.40308 0.37615 0.33301 0.04722  0.02957  -0.02989 14  VAL   B CG2   
1483 N  N     . GLY   B 16  ? 0.35708 0.35104 0.31118 0.04114  0.04352  -0.02067 15  GLY   B N     
1484 C  CA    . GLY   B 16  ? 0.36343 0.36341 0.32756 0.03538  0.04368  -0.01971 15  GLY   B CA    
1485 C  C     . GLY   B 16  ? 0.37927 0.37913 0.34708 0.02951  0.03823  -0.02281 15  GLY   B C     
1486 O  O     . GLY   B 16  ? 0.38215 0.38522 0.35505 0.02598  0.03777  -0.02244 15  GLY   B O     
1487 N  N     . LYS   B 17  ? 0.36412 0.36045 0.32970 0.02872  0.03428  -0.02545 16  LYS   B N     
1488 C  CA    . LYS   B 17  ? 0.33956 0.33643 0.30991 0.02351  0.02968  -0.02738 16  LYS   B CA    
1489 C  C     . LYS   B 17  ? 0.34791 0.35181 0.32867 0.01876  0.03156  -0.02584 16  LYS   B C     
1490 O  O     . LYS   B 17  ? 0.31616 0.32204 0.30081 0.01541  0.02989  -0.02598 16  LYS   B O     
1491 C  CB    . LYS   B 17  ? 0.33706 0.32997 0.30513 0.02360  0.02595  -0.02956 16  LYS   B CB    
1492 C  CG    . LYS   B 17  ? 0.35836 0.34276 0.31569 0.02821  0.02219  -0.03177 16  LYS   B CG    
1493 C  CD    . LYS   B 17  ? 0.37113 0.35181 0.32754 0.02785  0.01805  -0.03380 16  LYS   B CD    
1494 C  CE    . LYS   B 17  ? 0.33211 0.31586 0.29066 0.02856  0.02203  -0.03274 16  LYS   B CE    
1495 N  NZ    . LYS   B 17  ? 0.36842 0.34977 0.31886 0.03511  0.02621  -0.03163 16  LYS   B NZ    
1496 N  N     . SER   B 18  ? 0.31627 0.32342 0.30138 0.01870  0.03459  -0.02441 17  SER   B N     
1497 C  CA    . SER   B 18  ? 0.32154 0.33412 0.31567 0.01496  0.03572  -0.02318 17  SER   B CA    
1498 C  C     . SER   B 18  ? 0.36463 0.38041 0.36216 0.01450  0.03791  -0.02115 17  SER   B C     
1499 O  O     . SER   B 18  ? 0.33856 0.35674 0.34060 0.01134  0.03668  -0.02126 17  SER   B O     
1500 C  CB    . SER   B 18  ? 0.32801 0.34250 0.32592 0.01543  0.03790  -0.02207 17  SER   B CB    
1501 O  OG    . SER   B 18  ? 0.32877 0.34073 0.32452 0.01502  0.03539  -0.02415 17  SER   B OG    
1502 N  N     . ALA   B 19  ? 0.34912 0.36495 0.34459 0.01802  0.04133  -0.01898 18  ALA   B N     
1503 C  CA    . ALA   B 19  ? 0.40920 0.42821 0.40867 0.01767  0.04347  -0.01662 18  ALA   B CA    
1504 C  C     . ALA   B 19  ? 0.33170 0.34975 0.32902 0.01577  0.04086  -0.01823 18  ALA   B C     
1505 O  O     . ALA   B 19  ? 0.38810 0.40922 0.39076 0.01322  0.04075  -0.01743 18  ALA   B O     
1506 C  CB    . ALA   B 19  ? 0.39105 0.40984 0.38762 0.02260  0.04780  -0.01360 18  ALA   B CB    
1507 N  N     . LEU   B 20  ? 0.32417 0.33768 0.31396 0.01707  0.03835  -0.02043 19  LEU   B N     
1508 C  CA    . LEU   B 20  ? 0.30627 0.31882 0.29480 0.01517  0.03556  -0.02169 19  LEU   B CA    
1509 C  C     . LEU   B 20  ? 0.32538 0.34048 0.31987 0.01078  0.03324  -0.02244 19  LEU   B C     
1510 O  O     . LEU   B 20  ? 0.31741 0.33487 0.31509 0.00869  0.03298  -0.02193 19  LEU   B O     
1511 C  CB    . LEU   B 20  ? 0.31543 0.32180 0.29555 0.01743  0.03224  -0.02389 19  LEU   B CB    
1512 C  CG    . LEU   B 20  ? 0.39402 0.39648 0.36568 0.02285  0.03405  -0.02343 19  LEU   B CG    
1513 C  CD1   . LEU   B 20  ? 0.41579 0.41068 0.37865 0.02550  0.02953  -0.02621 19  LEU   B CD1   
1514 C  CD2   . LEU   B 20  ? 0.36251 0.36641 0.33437 0.02266  0.03513  -0.02233 19  LEU   B CD2   
1515 N  N     . THR   B 21  ? 0.31241 0.32701 0.30815 0.00979  0.03179  -0.02344 20  THR   B N     
1516 C  CA    . THR   B 21  ? 0.30714 0.32385 0.30774 0.00647  0.02987  -0.02380 20  THR   B CA    
1517 C  C     . THR   B 21  ? 0.29716 0.31792 0.30350 0.00504  0.03168  -0.02254 20  THR   B C     
1518 O  O     . THR   B 21  ? 0.30979 0.33219 0.31855 0.00327  0.03071  -0.02235 20  THR   B O     
1519 C  CB    . THR   B 21  ? 0.33114 0.34637 0.33176 0.00619  0.02824  -0.02486 20  THR   B CB    
1520 O  OG1   . THR   B 21  ? 0.31306 0.32361 0.30841 0.00764  0.02549  -0.02619 20  THR   B OG1   
1521 C  CG2   . THR   B 21  ? 0.30844 0.32597 0.31390 0.00347  0.02679  -0.02465 20  THR   B CG2   
1522 N  N     . ILE   B 22  ? 0.28548 0.30751 0.29413 0.00610  0.03401  -0.02148 21  ILE   B N     
1523 C  CA    . ILE   B 22  ? 0.30577 0.33069 0.32048 0.00493  0.03472  -0.02031 21  ILE   B CA    
1524 C  C     . ILE   B 22  ? 0.30394 0.33022 0.31990 0.00463  0.03523  -0.01920 21  ILE   B C     
1525 O  O     . ILE   B 22  ? 0.32062 0.34820 0.33998 0.00321  0.03408  -0.01911 21  ILE   B O     
1526 C  CB    . ILE   B 22  ? 0.32400 0.34984 0.34212 0.00618  0.03678  -0.01885 21  ILE   B CB    
1527 C  CG1   . ILE   B 22  ? 0.36164 0.38630 0.37906 0.00604  0.03586  -0.02018 21  ILE   B CG1   
1528 C  CG2   . ILE   B 22  ? 0.34252 0.37084 0.36815 0.00522  0.03691  -0.01706 21  ILE   B CG2   
1529 C  CD1   . ILE   B 22  ? 0.42139 0.44631 0.44068 0.00390  0.03334  -0.02156 21  ILE   B CD1   
1530 N  N     . GLN   B 23  ? 0.31135 0.33687 0.32391 0.00633  0.03676  -0.01846 22  GLN   B N     
1531 C  CA    . GLN   B 23  ? 0.33732 0.36402 0.35066 0.00591  0.03705  -0.01757 22  GLN   B CA    
1532 C  C     . GLN   B 23  ? 0.32686 0.35325 0.33898 0.00392  0.03448  -0.01905 22  GLN   B C     
1533 O  O     . GLN   B 23  ? 0.37040 0.39833 0.38532 0.00276  0.03389  -0.01862 22  GLN   B O     
1534 C  CB    . GLN   B 23  ? 0.37868 0.40407 0.38738 0.00855  0.03906  -0.01665 22  GLN   B CB    
1535 C  CG    . GLN   B 23  ? 0.40010 0.42745 0.41228 0.01080  0.04269  -0.01348 22  GLN   B CG    
1536 C  CD    . GLN   B 23  ? 0.45648 0.48698 0.47553 0.00944  0.04321  -0.01131 22  GLN   B CD    
1537 O  OE1   . GLN   B 23  ? 0.39378 0.42499 0.41563 0.00676  0.04063  -0.01245 22  GLN   B OE1   
1538 N  NE2   . GLN   B 23  ? 0.40491 0.43712 0.42665 0.01174  0.04654  -0.00788 22  GLN   B NE2   
1539 N  N     . LEU   B 24  ? 0.32670 0.35098 0.33500 0.00376  0.03277  -0.02046 23  LEU   B N     
1540 C  CA    . LEU   B 24  ? 0.32836 0.35279 0.33664 0.00213  0.03066  -0.02094 23  LEU   B CA    
1541 C  C     . LEU   B 24  ? 0.34034 0.36666 0.35231 0.00097  0.03012  -0.02075 23  LEU   B C     
1542 O  O     . LEU   B 24  ? 0.33632 0.36379 0.34920 0.00037  0.02960  -0.02029 23  LEU   B O     
1543 C  CB    . LEU   B 24  ? 0.30335 0.32512 0.30878 0.00213  0.02845  -0.02190 23  LEU   B CB    
1544 C  CG    . LEU   B 24  ? 0.34196 0.36428 0.34896 0.00053  0.02634  -0.02141 23  LEU   B CG    
1545 C  CD1   . LEU   B 24  ? 0.35116 0.37292 0.35632 0.00060  0.02595  -0.02113 23  LEU   B CD1   
1546 C  CD2   . LEU   B 24  ? 0.30998 0.33026 0.31717 0.00009  0.02369  -0.02171 23  LEU   B CD2   
1547 N  N     . ILE   B 25  ? 0.29853 0.32479 0.31199 0.00110  0.03017  -0.02113 24  ILE   B N     
1548 C  CA    . ILE   B 25  ? 0.29530 0.32237 0.31083 0.00069  0.02928  -0.02118 24  ILE   B CA    
1549 C  C     . ILE   B 25  ? 0.33726 0.36493 0.35555 0.00100  0.02930  -0.02094 24  ILE   B C     
1550 O  O     . ILE   B 25  ? 0.32937 0.35705 0.34782 0.00130  0.02818  -0.02095 24  ILE   B O     
1551 C  CB    . ILE   B 25  ? 0.34487 0.37119 0.36058 0.00074  0.02886  -0.02179 24  ILE   B CB    
1552 C  CG1   . ILE   B 25  ? 0.30216 0.32725 0.31597 0.00038  0.02784  -0.02195 24  ILE   B CG1   
1553 C  CG2   . ILE   B 25  ? 0.31990 0.34663 0.33712 0.00107  0.02816  -0.02181 24  ILE   B CG2   
1554 C  CD1   . ILE   B 25  ? 0.26493 0.29077 0.27947 -0.00033 0.02661  -0.02080 24  ILE   B CD1   
1555 N  N     . GLN   B 26  ? 0.33620 0.36405 0.35693 0.00130  0.03029  -0.02048 25  GLN   B N     
1556 C  CA    . GLN   B 26  ? 0.38684 0.41486 0.41204 0.00140  0.02941  -0.01997 25  GLN   B CA    
1557 C  C     . GLN   B 26  ? 0.36043 0.38952 0.38879 0.00141  0.03013  -0.01839 25  GLN   B C     
1558 O  O     . GLN   B 26  ? 0.35125 0.38025 0.38457 0.00134  0.02864  -0.01766 25  GLN   B O     
1559 C  CB    . GLN   B 26  ? 0.30740 0.33518 0.33547 0.00165  0.02963  -0.01988 25  GLN   B CB    
1560 C  CG    . GLN   B 26  ? 0.39091 0.41766 0.41626 0.00167  0.02887  -0.02134 25  GLN   B CG    
1561 C  CD    . GLN   B 26  ? 0.40462 0.43108 0.43253 0.00188  0.02915  -0.02133 25  GLN   B CD    
1562 O  OE1   . GLN   B 26  ? 0.42516 0.45240 0.45732 0.00210  0.03005  -0.01991 25  GLN   B OE1   
1563 N  NE2   . GLN   B 26  ? 0.43002 0.45563 0.45606 0.00192  0.02852  -0.02247 25  GLN   B NE2   
1564 N  N     . ASN   B 27  ? 0.35459 0.38436 0.38048 0.00164  0.03198  -0.01774 26  ASN   B N     
1565 C  CA    . ASN   B 27  ? 0.35713 0.38810 0.38548 0.00179  0.03288  -0.01603 26  ASN   B CA    
1566 C  C     . ASN   B 27  ? 0.43268 0.46503 0.46760 0.00242  0.03426  -0.01347 26  ASN   B C     
1567 O  O     . ASN   B 27  ? 0.37851 0.41183 0.41895 0.00208  0.03354  -0.01177 26  ASN   B O     
1568 C  CB    . ASN   B 27  ? 0.37115 0.40182 0.40038 0.00108  0.03046  -0.01653 26  ASN   B CB    
1569 C  CG    . ASN   B 27  ? 0.41076 0.44256 0.44127 0.00105  0.03130  -0.01507 26  ASN   B CG    
1570 O  OD1   . ASN   B 27  ? 0.43568 0.46802 0.46314 0.00157  0.03352  -0.01454 26  ASN   B OD1   
1571 N  ND2   . ASN   B 27  ? 0.40773 0.43935 0.44244 0.00070  0.02911  -0.01452 26  ASN   B ND2   
1572 N  N     . HIS   B 28  ? 0.34624 0.37873 0.38122 0.00346  0.03616  -0.01282 27  HIS   B N     
1573 C  CA    . HIS   B 28  ? 0.41110 0.44547 0.45275 0.00455  0.03832  -0.00944 27  HIS   B CA    
1574 C  C     . HIS   B 28  ? 0.42472 0.45887 0.46239 0.00688  0.04166  -0.00872 27  HIS   B C     
1575 O  O     . HIS   B 28  ? 0.37744 0.40947 0.40786 0.00725  0.04131  -0.01128 27  HIS   B O     
1576 C  CB    . HIS   B 28  ? 0.41672 0.45125 0.46645 0.00343  0.03579  -0.00876 27  HIS   B CB    
1577 C  CG    . HIS   B 28  ? 0.42288 0.45587 0.47047 0.00317  0.03459  -0.01095 27  HIS   B CG    
1578 N  ND1   . HIS   B 28  ? 0.50977 0.54331 0.55781 0.00439  0.03698  -0.00988 27  HIS   B ND1   
1579 C  CD2   . HIS   B 28  ? 0.47251 0.50341 0.51735 0.00219  0.03144  -0.01390 27  HIS   B CD2   
1580 C  CE1   . HIS   B 28  ? 0.48606 0.51796 0.53205 0.00372  0.03510  -0.01231 27  HIS   B CE1   
1581 N  NE2   . HIS   B 28  ? 0.46431 0.49466 0.50842 0.00249  0.03185  -0.01463 27  HIS   B NE2   
1582 N  N     . PHE   B 29  ? 0.35844 0.39466 0.40110 0.00883  0.04484  -0.00483 28  PHE   B N     
1583 C  CA    . PHE   B 29  ? 0.35641 0.39234 0.39541 0.01211  0.04850  -0.00338 28  PHE   B CA    
1584 C  C     . PHE   B 29  ? 0.46662 0.50515 0.51524 0.01280  0.05022  0.00053  28  PHE   B C     
1585 O  O     . PHE   B 29  ? 0.46881 0.51012 0.52713 0.01227  0.05058  0.00424  28  PHE   B O     
1586 C  CB    . PHE   B 29  ? 0.48055 0.51629 0.51419 0.01537  0.05191  -0.00160 28  PHE   B CB    
1587 C  CG    . PHE   B 29  ? 0.46351 0.49881 0.49341 0.02016  0.05631  0.00096  28  PHE   B CG    
1588 C  CD1   . PHE   B 29  ? 0.48393 0.52277 0.52159 0.02267  0.06050  0.00669  28  PHE   B CD1   
1589 C  CD2   . PHE   B 29  ? 0.41066 0.44178 0.42940 0.02259  0.05615  -0.00201 28  PHE   B CD2   
1590 C  CE1   . PHE   B 29  ? 0.43804 0.47645 0.47152 0.02801  0.06516  0.00956  28  PHE   B CE1   
1591 C  CE2   . PHE   B 29  ? 0.44831 0.47811 0.46199 0.02792  0.06004  0.00018  28  PHE   B CE2   
1592 C  CZ    . PHE   B 29  ? 0.46033 0.49388 0.48089 0.03091  0.06494  0.00606  28  PHE   B CZ    
1593 N  N     . VAL   B 30  ? 0.50960 0.54722 0.55603 0.01412  0.05121  0.00005  29  VAL   B N     
1594 C  CA    . VAL   B 30  ? 0.49940 0.53965 0.55502 0.01529  0.05342  0.00433  29  VAL   B CA    
1595 C  C     . VAL   B 30  ? 0.49472 0.53423 0.54345 0.02009  0.05812  0.00594  29  VAL   B C     
1596 O  O     . VAL   B 30  ? 0.50559 0.54143 0.54323 0.02108  0.05730  0.00197  29  VAL   B O     
1597 C  CB    . VAL   B 30  ? 0.48348 0.52314 0.54396 0.01246  0.04977  0.00240  29  VAL   B CB    
1598 C  CG1   . VAL   B 30  ? 0.55356 0.59613 0.62577 0.01311  0.05129  0.00726  29  VAL   B CG1   
1599 C  CG2   . VAL   B 30  ? 0.58195 0.62034 0.64427 0.00874  0.04453  -0.00073 29  VAL   B CG2   
1600 N  N     . ASP   B 31  ? 0.50107 0.54374 0.55635 0.02330  0.06267  0.01185  30  ASP   B N     
1601 C  CA    . ASP   B 31  ? 0.52253 0.56407 0.56991 0.02917  0.06767  0.01383  30  ASP   B CA    
1602 C  C     . ASP   B 31  ? 0.56275 0.60344 0.60998 0.02965  0.06761  0.01303  30  ASP   B C     
1603 O  O     . ASP   B 31  ? 0.68690 0.72553 0.72568 0.03467  0.07096  0.01365  30  ASP   B O     
1604 C  CB    . ASP   B 31  ? 0.56513 0.61035 0.61782 0.03365  0.07358  0.02106  30  ASP   B CB    
1605 C  CG    . ASP   B 31  ? 0.64460 0.68729 0.68506 0.04095  0.07866  0.02249  30  ASP   B CG    
1606 O  OD1   . ASP   B 31  ? 0.66040 0.69876 0.68838 0.04246  0.07752  0.01859  30  ASP   B OD1   
1607 O  OD2   . ASP   B 31  ? 0.67141 0.71610 0.71472 0.04544  0.08353  0.02758  30  ASP   B OD2   
1608 N  N     . GLU   B 32  ? 0.53968 0.58117 0.59452 0.02512  0.06373  0.01138  31  GLU   B N     
1609 C  CA    . GLU   B 32  ? 0.52586 0.56674 0.58101 0.02574  0.06395  0.01097  31  GLU   B CA    
1610 C  C     . GLU   B 32  ? 0.57653 0.61238 0.61717 0.02713  0.06271  0.00557  31  GLU   B C     
1611 O  O     . GLU   B 32  ? 0.66344 0.69652 0.69701 0.02534  0.05963  0.00128  31  GLU   B O     
1612 C  CB    . GLU   B 32  ? 0.56496 0.60668 0.62956 0.02089  0.05944  0.00958  31  GLU   B CB    
1613 C  CG    . GLU   B 32  ? 0.64589 0.69193 0.72662 0.01994  0.05996  0.01544  31  GLU   B CG    
1614 C  CD    . GLU   B 32  ? 0.63605 0.68144 0.72493 0.01522  0.05400  0.01324  31  GLU   B CD    
1615 O  OE1   . GLU   B 32  ? 0.68173 0.72373 0.76323 0.01296  0.05015  0.00738  31  GLU   B OE1   
1616 O  OE2   . GLU   B 32  ? 0.67324 0.72125 0.77599 0.01414  0.05304  0.01765  31  GLU   B OE2   
1617 N  N     . TYR   B 33  ? 0.60101 0.63567 0.63824 0.03010  0.06468  0.00599  32  TYR   B N     
1618 C  CA    . TYR   B 33  ? 0.61672 0.64606 0.64109 0.03114  0.06246  0.00073  32  TYR   B CA    
1619 C  C     . TYR   B 33  ? 0.52413 0.55283 0.55126 0.02654  0.05809  -0.00305 32  TYR   B C     
1620 O  O     . TYR   B 33  ? 0.58844 0.61923 0.62272 0.02601  0.05883  -0.00115 32  TYR   B O     
1621 C  CB    . TYR   B 33  ? 0.58933 0.61611 0.60518 0.03763  0.06629  0.00223  32  TYR   B CB    
1622 C  CG    . TYR   B 33  ? 0.58517 0.60535 0.58708 0.03891  0.06288  -0.00337 32  TYR   B CG    
1623 C  CD1   . TYR   B 33  ? 0.57110 0.58882 0.56899 0.03564  0.05842  -0.00758 32  TYR   B CD1   
1624 C  CD2   . TYR   B 33  ? 0.62232 0.63857 0.61582 0.04340  0.06374  -0.00422 32  TYR   B CD2   
1625 C  CE1   . TYR   B 33  ? 0.51529 0.52699 0.50243 0.03649  0.05459  -0.01218 32  TYR   B CE1   
1626 C  CE2   . TYR   B 33  ? 0.67533 0.68495 0.65705 0.04443  0.05959  -0.00929 32  TYR   B CE2   
1627 C  CZ    . TYR   B 33  ? 0.54863 0.55607 0.52785 0.04080  0.05486  -0.01312 32  TYR   B CZ    
1628 O  OH    . TYR   B 33  ? 0.65235 0.65326 0.62172 0.04165  0.05022  -0.01756 32  TYR   B OH    
1629 N  N     . ASP   B 34  ? 0.51409 0.54013 0.53625 0.02345  0.05373  -0.00783 33  ASP   B N     
1630 C  CA    . ASP   B 34  ? 0.54228 0.56738 0.56568 0.01968  0.04977  -0.01138 33  ASP   B CA    
1631 C  C     . ASP   B 34  ? 0.49061 0.51096 0.50323 0.02059  0.04743  -0.01535 33  ASP   B C     
1632 O  O     . ASP   B 34  ? 0.41484 0.43372 0.42425 0.01873  0.04468  -0.01771 33  ASP   B O     
1633 C  CB    . ASP   B 34  ? 0.53922 0.56595 0.56865 0.01514  0.04651  -0.01259 33  ASP   B CB    
1634 C  CG    . ASP   B 34  ? 0.57239 0.59843 0.60366 0.01215  0.04312  -0.01535 33  ASP   B CG    
1635 O  OD1   . ASP   B 34  ? 0.56039 0.58523 0.58971 0.01307  0.04335  -0.01613 33  ASP   B OD1   
1636 O  OD2   . ASP   B 34  ? 0.63985 0.66633 0.67401 0.00936  0.04037  -0.01660 33  ASP   B OD2   
1637 N  N     . PRO   B 35  ? 0.43417 0.45187 0.44151 0.02346  0.04811  -0.01598 34  PRO   B N     
1638 C  CA    . PRO   B 35  ? 0.37198 0.38435 0.36933 0.02471  0.04511  -0.01957 34  PRO   B CA    
1639 C  C     . PRO   B 35  ? 0.40319 0.41509 0.40240 0.02004  0.04054  -0.02279 34  PRO   B C     
1640 O  O     . PRO   B 35  ? 0.35186 0.36638 0.35764 0.01708  0.03995  -0.02282 34  PRO   B O     
1641 C  CB    . PRO   B 35  ? 0.38367 0.39357 0.37620 0.02902  0.04696  -0.01909 34  PRO   B CB    
1642 C  CG    . PRO   B 35  ? 0.43938 0.45402 0.44178 0.02745  0.04936  -0.01643 34  PRO   B CG    
1643 C  CD    . PRO   B 35  ? 0.46863 0.48796 0.47987 0.02529  0.05090  -0.01355 34  PRO   B CD    
1644 N  N     . THR   B 36  ? 0.33906 0.34752 0.33273 0.01966  0.03721  -0.02518 35  THR   B N     
1645 C  CA    . THR   B 36  ? 0.34742 0.35614 0.34391 0.01551  0.03340  -0.02717 35  THR   B CA    
1646 C  C     . THR   B 36  ? 0.31829 0.32402 0.31247 0.01543  0.03065  -0.02917 35  THR   B C     
1647 O  O     . THR   B 36  ? 0.32431 0.32564 0.31171 0.01878  0.02995  -0.03013 35  THR   B O     
1648 C  CB    . THR   B 36  ? 0.31763 0.32468 0.31128 0.01486  0.03107  -0.02799 35  THR   B CB    
1649 O  OG1   . THR   B 36  ? 0.31231 0.32221 0.30811 0.01513  0.03388  -0.02602 35  THR   B OG1   
1650 C  CG2   . THR   B 36  ? 0.31023 0.31821 0.30773 0.01094  0.02769  -0.02901 35  THR   B CG2   
1651 N  N     . ILE   B 37  ? 0.30208 0.30991 0.30158 0.01196  0.02901  -0.02972 36  ILE   B N     
1652 C  CA    . ILE   B 37  ? 0.28515 0.29040 0.28357 0.01112  0.02565  -0.03141 36  ILE   B CA    
1653 C  C     . ILE   B 37  ? 0.27734 0.28124 0.27584 0.00931  0.02197  -0.03196 36  ILE   B C     
1654 O  O     . ILE   B 37  ? 0.29804 0.29730 0.29187 0.01069  0.01874  -0.03317 36  ILE   B O     
1655 C  CB    . ILE   B 37  ? 0.28167 0.28983 0.28578 0.00887  0.02605  -0.03125 36  ILE   B CB    
1656 C  CG1   . ILE   B 37  ? 0.29752 0.30735 0.30327 0.01034  0.02944  -0.03027 36  ILE   B CG1   
1657 C  CG2   . ILE   B 37  ? 0.32269 0.32837 0.32617 0.00807  0.02263  -0.03258 36  ILE   B CG2   
1658 C  CD1   . ILE   B 37  ? 0.30581 0.31248 0.30610 0.01383  0.03030  -0.03060 36  ILE   B CD1   
1659 N  N     . GLU   B 38  ? 0.26950 0.27715 0.27333 0.00658  0.02228  -0.03088 37  GLU   B N     
1660 C  CA    . GLU   B 38  ? 0.28700 0.29452 0.29216 0.00499  0.01975  -0.03045 37  GLU   B CA    
1661 C  C     . GLU   B 38  ? 0.31492 0.32698 0.32477 0.00319  0.02174  -0.02897 37  GLU   B C     
1662 O  O     . GLU   B 38  ? 0.31521 0.32963 0.32839 0.00235  0.02282  -0.02856 37  GLU   B O     
1663 C  CB    . GLU   B 38  ? 0.29013 0.29592 0.29744 0.00367  0.01588  -0.03059 37  GLU   B CB    
1664 C  CG    . GLU   B 38  ? 0.33923 0.34536 0.34994 0.00192  0.01316  -0.02922 37  GLU   B CG    
1665 C  CD    . GLU   B 38  ? 0.47358 0.47962 0.48947 0.00030  0.01003  -0.02808 37  GLU   B CD    
1666 O  OE1   . GLU   B 38  ? 0.48217 0.48372 0.49638 0.00090  0.00616  -0.02925 37  GLU   B OE1   
1667 O  OE2   . GLU   B 38  ? 0.55782 0.56806 0.57933 -0.00119 0.01141  -0.02581 37  GLU   B OE2   
1668 N  N     . ASP   B 39  ? 0.29290 0.30570 0.30246 0.00296  0.02200  -0.02829 38  ASP   B N     
1669 C  CA    . ASP   B 39  ? 0.32712 0.34351 0.34024 0.00173  0.02343  -0.02701 38  ASP   B CA    
1670 C  C     . ASP   B 39  ? 0.28752 0.30424 0.30195 0.00065  0.02164  -0.02590 38  ASP   B C     
1671 O  O     . ASP   B 39  ? 0.26698 0.28106 0.27915 0.00094  0.01957  -0.02628 38  ASP   B O     
1672 C  CB    . ASP   B 39  ? 0.32655 0.34421 0.33911 0.00257  0.02601  -0.02679 38  ASP   B CB    
1673 C  CG    . ASP   B 39  ? 0.43122 0.44938 0.44481 0.00344  0.02788  -0.02697 38  ASP   B CG    
1674 O  OD1   . ASP   B 39  ? 0.48741 0.50617 0.50323 0.00280  0.02747  -0.02723 38  ASP   B OD1   
1675 O  OD2   . ASP   B 39  ? 0.42362 0.44166 0.43617 0.00493  0.02982  -0.02648 38  ASP   B OD2   
1676 N  N     . SER   B 40  ? 0.26791 0.28752 0.28583 -0.00018 0.02227  -0.02434 39  SER   B N     
1677 C  CA    . SER   B 40  ? 0.25668 0.27738 0.27683 -0.00097 0.02119  -0.02248 39  SER   B CA    
1678 C  C     . SER   B 40  ? 0.29972 0.32288 0.32004 -0.00062 0.02327  -0.02164 39  SER   B C     
1679 O  O     . SER   B 40  ? 0.28147 0.30568 0.30172 0.00011  0.02479  -0.02193 39  SER   B O     
1680 C  CB    . SER   B 40  ? 0.34698 0.36892 0.37168 -0.00160 0.02002  -0.02033 39  SER   B CB    
1681 O  OG    . SER   B 40  ? 0.46311 0.48247 0.48819 -0.00201 0.01750  -0.02111 39  SER   B OG    
1682 N  N     . TYR   B 41  ? 0.27932 0.30295 0.29988 -0.00100 0.02283  -0.02061 40  TYR   B N     
1683 C  CA    . TYR   B 41  ? 0.26373 0.28920 0.28386 -0.00049 0.02448  -0.01999 40  TYR   B CA    
1684 C  C     . TYR   B 41  ? 0.26738 0.29439 0.29000 -0.00084 0.02395  -0.01745 40  TYR   B C     
1685 O  O     . TYR   B 41  ? 0.29821 0.32431 0.32271 -0.00184 0.02186  -0.01664 40  TYR   B O     
1686 C  CB    . TYR   B 41  ? 0.30127 0.32583 0.31863 -0.00035 0.02516  -0.02142 40  TYR   B CB    
1687 C  CG    . TYR   B 41  ? 0.29524 0.31874 0.31128 0.00025  0.02608  -0.02300 40  TYR   B CG    
1688 C  CD1   . TYR   B 41  ? 0.28645 0.31089 0.30363 0.00076  0.02720  -0.02324 40  TYR   B CD1   
1689 C  CD2   . TYR   B 41  ? 0.27362 0.29480 0.28737 0.00067  0.02554  -0.02405 40  TYR   B CD2   
1690 C  CE1   . TYR   B 41  ? 0.38268 0.40652 0.40018 0.00123  0.02802  -0.02401 40  TYR   B CE1   
1691 C  CE2   . TYR   B 41  ? 0.32702 0.34760 0.33994 0.00165  0.02688  -0.02483 40  TYR   B CE2   
1692 C  CZ    . TYR   B 41  ? 0.37284 0.39515 0.38836 0.00170  0.02827  -0.02456 40  TYR   B CZ    
1693 O  OH    . TYR   B 41  ? 0.33705 0.35914 0.35318 0.00261  0.02963  -0.02468 40  TYR   B OH    
1694 N  N     . ARG   B 42  ? 0.24089 0.26990 0.26365 0.00028  0.02554  -0.01604 41  ARG   B N     
1695 C  CA    . ARG   B 42  ? 0.24597 0.27682 0.27110 0.00036  0.02562  -0.01318 41  ARG   B CA    
1696 C  C     . ARG   B 42  ? 0.26735 0.29856 0.28983 0.00097  0.02662  -0.01368 41  ARG   B C     
1697 O  O     . ARG   B 42  ? 0.28933 0.32011 0.30906 0.00224  0.02756  -0.01504 41  ARG   B O     
1698 C  CB    . ARG   B 42  ? 0.31609 0.34924 0.34401 0.00202  0.02694  -0.00986 41  ARG   B CB    
1699 C  CG    . ARG   B 42  ? 0.39994 0.43336 0.43279 0.00085  0.02545  -0.00809 41  ARG   B CG    
1700 C  CD    . ARG   B 42  ? 0.48353 0.51942 0.51947 0.00282  0.02723  -0.00444 41  ARG   B CD    
1701 N  NE    . ARG   B 42  ? 0.45071 0.48939 0.48840 0.00480  0.02929  -0.00042 41  ARG   B NE    
1702 C  CZ    . ARG   B 42  ? 0.41541 0.45694 0.46012 0.00502  0.02965  0.00470  41  ARG   B CZ    
1703 N  NH1   . ARG   B 42  ? 0.33089 0.37243 0.38220 0.00268  0.02708  0.00615  41  ARG   B NH1   
1704 N  NH2   . ARG   B 42  ? 0.49014 0.53445 0.53560 0.00794  0.03252  0.00879  41  ARG   B NH2   
1705 N  N     . LYS   B 43  ? 0.26956 0.30125 0.29322 0.00008  0.02594  -0.01253 42  LYS   B N     
1706 C  CA    . LYS   B 43  ? 0.23527 0.26736 0.25657 0.00060  0.02682  -0.01289 42  LYS   B CA    
1707 C  C     . LYS   B 43  ? 0.26080 0.29460 0.28490 0.00035  0.02664  -0.00996 42  LYS   B C     
1708 O  O     . LYS   B 43  ? 0.29830 0.33161 0.32550 -0.00123 0.02469  -0.00905 42  LYS   B O     
1709 C  CB    . LYS   B 43  ? 0.27934 0.30952 0.29797 -0.00041 0.02626  -0.01560 42  LYS   B CB    
1710 C  CG    . LYS   B 43  ? 0.31014 0.34081 0.32686 0.00010  0.02714  -0.01593 42  LYS   B CG    
1711 C  CD    . LYS   B 43  ? 0.31400 0.34316 0.32879 -0.00060 0.02702  -0.01782 42  LYS   B CD    
1712 C  CE    . LYS   B 43  ? 0.31453 0.34432 0.32831 -0.00027 0.02776  -0.01790 42  LYS   B CE    
1713 N  NZ    . LYS   B 43  ? 0.44574 0.47588 0.45955 0.00098  0.02809  -0.01804 42  LYS   B NZ    
1714 N  N     . GLN   B 44  ? 0.27357 0.30889 0.29653 0.00211  0.02829  -0.00850 43  GLN   B N     
1715 C  CA    . GLN   B 44  ? 0.32181 0.35911 0.34745 0.00221  0.02859  -0.00537 43  GLN   B CA    
1716 C  C     . GLN   B 44  ? 0.31920 0.35547 0.34247 0.00102  0.02788  -0.00727 43  GLN   B C     
1717 O  O     . GLN   B 44  ? 0.31746 0.35261 0.33669 0.00161  0.02841  -0.00973 43  GLN   B O     
1718 C  CB    . GLN   B 44  ? 0.36123 0.40045 0.38584 0.00562  0.03109  -0.00259 43  GLN   B CB    
1719 C  CG    . GLN   B 44  ? 0.50995 0.55189 0.53809 0.00645  0.03217  0.00174  43  GLN   B CG    
1720 C  CD    . GLN   B 44  ? 0.48570 0.52828 0.50946 0.01063  0.03470  0.00322  43  GLN   B CD    
1721 O  OE1   . GLN   B 44  ? 0.51778 0.56121 0.54096 0.01119  0.03526  0.00438  43  GLN   B OE1   
1722 N  NE2   . GLN   B 44  ? 0.47686 0.51840 0.49673 0.01393  0.03592  0.00293  43  GLN   B NE2   
1723 N  N     . VAL   B 45  ? 0.31615 0.35248 0.34234 -0.00066 0.02629  -0.00609 44  VAL   B N     
1724 C  CA    . VAL   B 45  ? 0.34865 0.38363 0.37232 -0.00168 0.02547  -0.00792 44  VAL   B CA    
1725 C  C     . VAL   B 45  ? 0.33582 0.37238 0.36301 -0.00212 0.02494  -0.00493 44  VAL   B C     
1726 O  O     . VAL   B 45  ? 0.34402 0.38272 0.37659 -0.00188 0.02498  -0.00115 44  VAL   B O     
1727 C  CB    . VAL   B 45  ? 0.35215 0.38384 0.37410 -0.00308 0.02321  -0.01069 44  VAL   B CB    
1728 C  CG1   . VAL   B 45  ? 0.35350 0.38393 0.37199 -0.00245 0.02426  -0.01343 44  VAL   B CG1   
1729 C  CG2   . VAL   B 45  ? 0.33108 0.36172 0.35759 -0.00422 0.02030  -0.00913 44  VAL   B CG2   
1730 N  N     . VAL   B 46  ? 0.33990 0.37552 0.36463 -0.00273 0.02448  -0.00628 45  VAL   B N     
1731 C  CA    . VAL   B 46  ? 0.34442 0.38104 0.37251 -0.00345 0.02347  -0.00378 45  VAL   B CA    
1732 C  C     . VAL   B 46  ? 0.37560 0.40867 0.40191 -0.00499 0.02047  -0.00617 45  VAL   B C     
1733 O  O     . VAL   B 46  ? 0.41253 0.44382 0.43342 -0.00470 0.02104  -0.00921 45  VAL   B O     
1734 C  CB    . VAL   B 46  ? 0.47401 0.51283 0.50024 -0.00201 0.02591  -0.00269 45  VAL   B CB    
1735 C  CG1   . VAL   B 46  ? 0.39006 0.43004 0.42013 -0.00282 0.02494  0.00005  45  VAL   B CG1   
1736 C  CG2   . VAL   B 46  ? 0.44314 0.48437 0.46955 0.00062  0.02860  -0.00037 45  VAL   B CG2   
1737 N  N     . ILE   B 47  ? 0.35183 0.38350 0.38280 -0.00626 0.01702  -0.00461 46  ILE   B N     
1738 C  CA    . ILE   B 47  ? 0.33263 0.35947 0.36103 -0.00701 0.01316  -0.00708 46  ILE   B CA    
1739 C  C     . ILE   B 47  ? 0.40763 0.43450 0.44094 -0.00809 0.01052  -0.00451 46  ILE   B C     
1740 O  O     . ILE   B 47  ? 0.40885 0.43746 0.45042 -0.00899 0.00887  -0.00063 46  ILE   B O     
1741 C  CB    . ILE   B 47  ? 0.36894 0.39206 0.39758 -0.00722 0.00987  -0.00843 46  ILE   B CB    
1742 C  CG1   . ILE   B 47  ? 0.39328 0.41658 0.41715 -0.00610 0.01277  -0.01086 46  ILE   B CG1   
1743 C  CG2   . ILE   B 47  ? 0.40370 0.42043 0.42783 -0.00694 0.00532  -0.01127 46  ILE   B CG2   
1744 C  CD1   . ILE   B 47  ? 0.28981 0.31008 0.31402 -0.00610 0.01014  -0.01191 46  ILE   B CD1   
1745 N  N     . ASP   B 48  ? 0.42733 0.45253 0.45631 -0.00794 0.01022  -0.00623 47  ASP   B N     
1746 C  CA    . ASP   B 48  ? 0.46066 0.48584 0.49400 -0.00895 0.00776  -0.00394 47  ASP   B CA    
1747 C  C     . ASP   B 48  ? 0.43566 0.46677 0.47658 -0.00915 0.01042  0.00111  47  ASP   B C     
1748 O  O     . ASP   B 48  ? 0.48311 0.51526 0.53242 -0.01021 0.00798  0.00506  47  ASP   B O     
1749 C  CB    . ASP   B 48  ? 0.40735 0.42735 0.44391 -0.00990 0.00124  -0.00404 47  ASP   B CB    
1750 C  CG    . ASP   B 48  ? 0.38543 0.39861 0.41267 -0.00853 -0.00144 -0.00900 47  ASP   B CG    
1751 O  OD1   . ASP   B 48  ? 0.44517 0.45803 0.46466 -0.00716 0.00162  -0.01159 47  ASP   B OD1   
1752 O  OD2   . ASP   B 48  ? 0.47348 0.48142 0.50106 -0.00843 -0.00660 -0.01008 47  ASP   B OD2   
1753 N  N     . GLY   B 49  ? 0.45996 0.49470 0.49797 -0.00771 0.01534  0.00127  48  GLY   B N     
1754 C  CA    . GLY   B 49  ? 0.40498 0.44477 0.44750 -0.00658 0.01860  0.00577  48  GLY   B CA    
1755 C  C     . GLY   B 49  ? 0.45246 0.49500 0.50191 -0.00603 0.01932  0.00990  48  GLY   B C     
1756 O  O     . GLY   B 49  ? 0.49575 0.54252 0.54868 -0.00422 0.02252  0.01431  48  GLY   B O     
1757 N  N     . GLU   B 50  ? 0.40744 0.44771 0.45884 -0.00707 0.01667  0.00893  49  GLU   B N     
1758 C  CA    . GLU   B 50  ? 0.41393 0.45697 0.47257 -0.00657 0.01737  0.01316  49  GLU   B CA    
1759 C  C     . GLU   B 50  ? 0.45312 0.49568 0.50626 -0.00531 0.01955  0.01037  49  GLU   B C     
1760 O  O     . GLU   B 50  ? 0.40128 0.43995 0.44917 -0.00618 0.01764  0.00569  49  GLU   B O     
1761 C  CB    . GLU   B 50  ? 0.45445 0.49534 0.52172 -0.00888 0.01189  0.01510  49  GLU   B CB    
1762 C  CG    . GLU   B 50  ? 0.53261 0.57450 0.60812 -0.01011 0.00936  0.01922  49  GLU   B CG    
1763 C  CD    . GLU   B 50  ? 0.63804 0.67791 0.72443 -0.01227 0.00327  0.02219  49  GLU   B CD    
1764 O  OE1   . GLU   B 50  ? 0.68686 0.72420 0.77335 -0.01275 0.00098  0.02056  49  GLU   B OE1   
1765 O  OE2   . GLU   B 50  ? 0.67134 0.71198 0.76659 -0.01348 0.00046  0.02627  49  GLU   B OE2   
1766 N  N     . THR   B 51  ? 0.37224 0.41852 0.42644 -0.00285 0.02354  0.01351  50  THR   B N     
1767 C  CA    . THR   B 51  ? 0.43446 0.48030 0.48368 -0.00130 0.02558  0.01123  50  THR   B CA    
1768 C  C     . THR   B 51  ? 0.42106 0.46596 0.47529 -0.00266 0.02318  0.01186  50  THR   B C     
1769 O  O     . THR   B 51  ? 0.40798 0.45470 0.47150 -0.00342 0.02172  0.01659  50  THR   B O     
1770 C  CB    . THR   B 51  ? 0.47321 0.52244 0.52097 0.00258  0.03020  0.01444  50  THR   B CB    
1771 O  OG1   . THR   B 51  ? 0.47843 0.52771 0.52073 0.00401  0.03184  0.01332  50  THR   B OG1   
1772 C  CG2   . THR   B 51  ? 0.43737 0.48546 0.47984 0.00440  0.03171  0.01195  50  THR   B CG2   
1773 N  N     . CYS   B 52  ? 0.34213 0.38416 0.39089 -0.00298 0.02257  0.00737  51  CYS   B N     
1774 C  CA    . CYS   B 52  ? 0.31499 0.35607 0.36796 -0.00395 0.02046  0.00790  51  CYS   B CA    
1775 C  C     . CYS   B 52  ? 0.33829 0.37790 0.38469 -0.00298 0.02199  0.00404  51  CYS   B C     
1776 O  O     . CYS   B 52  ? 0.33373 0.37239 0.37297 -0.00206 0.02373  0.00066  51  CYS   B O     
1777 C  CB    . CYS   B 52  ? 0.30144 0.33844 0.35698 -0.00660 0.01491  0.00631  51  CYS   B CB    
1778 S  SG    . CYS   B 52  ? 0.39424 0.42621 0.43933 -0.00699 0.01353  -0.00031 51  CYS   B SG    
1779 N  N     . LEU   B 53  ? 0.30345 0.34277 0.35325 -0.00335 0.02090  0.00480  52  LEU   B N     
1780 C  CA    . LEU   B 53  ? 0.27339 0.31162 0.31854 -0.00245 0.02219  0.00191  52  LEU   B CA    
1781 C  C     . LEU   B 53  ? 0.33705 0.37107 0.38079 -0.00432 0.01850  -0.00167 52  LEU   B C     
1782 O  O     . LEU   B 53  ? 0.32890 0.36174 0.37833 -0.00572 0.01503  -0.00007 52  LEU   B O     
1783 C  CB    . LEU   B 53  ? 0.25969 0.30106 0.30946 -0.00073 0.02434  0.00603  52  LEU   B CB    
1784 C  CG    . LEU   B 53  ? 0.34699 0.38778 0.39228 0.00088  0.02619  0.00388  52  LEU   B CG    
1785 C  CD1   . LEU   B 53  ? 0.27452 0.31409 0.31143 0.00247  0.02813  0.00022  52  LEU   B CD1   
1786 C  CD2   . LEU   B 53  ? 0.44335 0.48761 0.49315 0.00336  0.02883  0.00901  52  LEU   B CD2   
1787 N  N     . LEU   B 54  ? 0.28127 0.31285 0.31772 -0.00402 0.01910  -0.00618 53  LEU   B N     
1788 C  CA    . LEU   B 54  ? 0.29696 0.32441 0.33055 -0.00475 0.01640  -0.00950 53  LEU   B CA    
1789 C  C     . LEU   B 54  ? 0.28834 0.31610 0.32172 -0.00417 0.01751  -0.01015 53  LEU   B C     
1790 O  O     . LEU   B 54  ? 0.30055 0.33000 0.33139 -0.00294 0.02060  -0.01074 53  LEU   B O     
1791 C  CB    . LEU   B 54  ? 0.31089 0.33590 0.33737 -0.00426 0.01697  -0.01318 53  LEU   B CB    
1792 C  CG    . LEU   B 54  ? 0.35019 0.37522 0.37600 -0.00455 0.01659  -0.01272 53  LEU   B CG    
1793 C  CD1   . LEU   B 54  ? 0.31517 0.33795 0.33425 -0.00372 0.01747  -0.01587 53  LEU   B CD1   
1794 C  CD2   . LEU   B 54  ? 0.31689 0.34015 0.34748 -0.00581 0.01227  -0.01083 53  LEU   B CD2   
1795 N  N     . ASP   B 55  ? 0.29185 0.31755 0.32800 -0.00498 0.01451  -0.01004 54  ASP   B N     
1796 C  CA    . ASP   B 55  ? 0.27464 0.29988 0.31035 -0.00462 0.01490  -0.01105 54  ASP   B CA    
1797 C  C     . ASP   B 55  ? 0.28338 0.30377 0.31358 -0.00450 0.01261  -0.01500 54  ASP   B C     
1798 O  O     . ASP   B 55  ? 0.33532 0.35205 0.36647 -0.00507 0.00831  -0.01537 54  ASP   B O     
1799 C  CB    . ASP   B 55  ? 0.33162 0.35811 0.37532 -0.00542 0.01293  -0.00739 54  ASP   B CB    
1800 C  CG    . ASP   B 55  ? 0.51872 0.54702 0.56334 -0.00459 0.01506  -0.00676 54  ASP   B CG    
1801 O  OD1   . ASP   B 55  ? 0.54974 0.57631 0.58876 -0.00401 0.01603  -0.01027 54  ASP   B OD1   
1802 O  OD2   . ASP   B 55  ? 0.56962 0.60118 0.62085 -0.00430 0.01593  -0.00238 54  ASP   B OD2   
1803 N  N     . ILE   B 56  ? 0.27131 0.29125 0.29587 -0.00341 0.01515  -0.01769 55  ILE   B N     
1804 C  CA    . ILE   B 56  ? 0.27351 0.28914 0.29209 -0.00240 0.01393  -0.02080 55  ILE   B CA    
1805 C  C     . ILE   B 56  ? 0.28473 0.29922 0.30198 -0.00177 0.01424  -0.02221 55  ILE   B C     
1806 O  O     . ILE   B 56  ? 0.28512 0.30238 0.30312 -0.00162 0.01719  -0.02208 55  ILE   B O     
1807 C  CB    . ILE   B 56  ? 0.30433 0.32044 0.31837 -0.00136 0.01676  -0.02203 55  ILE   B CB    
1808 C  CG1   . ILE   B 56  ? 0.32563 0.34237 0.34070 -0.00200 0.01598  -0.02079 55  ILE   B CG1   
1809 C  CG2   . ILE   B 56  ? 0.31843 0.33045 0.32608 0.00063  0.01647  -0.02448 55  ILE   B CG2   
1810 C  CD1   . ILE   B 56  ? 0.36896 0.38731 0.38132 -0.00132 0.01903  -0.02126 55  ILE   B CD1   
1811 N  N     . LEU   B 57  ? 0.24821 0.25808 0.26294 -0.00110 0.01089  -0.02375 56  LEU   B N     
1812 C  CA    . LEU   B 57  ? 0.25836 0.26650 0.27095 -0.00016 0.01096  -0.02531 56  LEU   B CA    
1813 C  C     . LEU   B 57  ? 0.29952 0.30405 0.30425 0.00251  0.01181  -0.02771 56  LEU   B C     
1814 O  O     . LEU   B 57  ? 0.29444 0.29413 0.29456 0.00404  0.00881  -0.02891 56  LEU   B O     
1815 C  CB    . LEU   B 57  ? 0.25474 0.25995 0.27035 -0.00090 0.00626  -0.02500 56  LEU   B CB    
1816 C  CG    . LEU   B 57  ? 0.30036 0.30362 0.31402 -0.00000 0.00593  -0.02656 56  LEU   B CG    
1817 C  CD1   . LEU   B 57  ? 0.38257 0.39099 0.40117 -0.00123 0.00923  -0.02495 56  LEU   B CD1   
1818 C  CD2   . LEU   B 57  ? 0.30319 0.30158 0.31836 -0.00025 -0.00014 -0.02681 56  LEU   B CD2   
1819 N  N     . ASP   B 58  ? 0.25237 0.25900 0.25576 0.00343  0.01575  -0.02810 57  ASP   B N     
1820 C  CA    . ASP   B 58  ? 0.25906 0.26355 0.25627 0.00640  0.01788  -0.02925 57  ASP   B CA    
1821 C  C     . ASP   B 58  ? 0.32109 0.32262 0.31563 0.00797  0.01698  -0.03053 57  ASP   B C     
1822 O  O     . ASP   B 58  ? 0.31389 0.31805 0.31196 0.00690  0.01847  -0.03020 57  ASP   B O     
1823 C  CB    . ASP   B 58  ? 0.29756 0.30672 0.29720 0.00614  0.02248  -0.02805 57  ASP   B CB    
1824 C  CG    . ASP   B 58  ? 0.32151 0.32987 0.31706 0.00923  0.02562  -0.02793 57  ASP   B CG    
1825 O  OD1   . ASP   B 58  ? 0.38136 0.38532 0.37033 0.01221  0.02470  -0.02881 57  ASP   B OD1   
1826 O  OD2   . ASP   B 58  ? 0.35513 0.36705 0.35428 0.00902  0.02887  -0.02668 57  ASP   B OD2   
1827 N  N     . THR   B 59  ? 0.29475 0.29028 0.28260 0.01078  0.01417  -0.03213 58  THR   B N     
1828 C  CA    . THR   B 59  ? 0.29872 0.29056 0.28356 0.01243  0.01237  -0.03353 58  THR   B CA    
1829 C  C     . THR   B 59  ? 0.31124 0.30183 0.28986 0.01657  0.01617  -0.03382 58  THR   B C     
1830 O  O     . THR   B 59  ? 0.34021 0.33228 0.31662 0.01855  0.01997  -0.03272 58  THR   B O     
1831 C  CB    . THR   B 59  ? 0.29949 0.28425 0.28043 0.01354  0.00588  -0.03522 58  THR   B CB    
1832 O  OG1   . THR   B 59  ? 0.29436 0.27416 0.26659 0.01752  0.00534  -0.03631 58  THR   B OG1   
1833 C  CG2   . THR   B 59  ? 0.30615 0.29268 0.29510 0.00947  0.00219  -0.03391 58  THR   B CG2   
1834 N  N     . ALA   B 60  ? 0.31820 0.30597 0.29421 0.01819  0.01516  -0.03493 59  ALA   B N     
1835 C  CA    . ALA   B 60  ? 0.30670 0.29300 0.27677 0.02270  0.01875  -0.03478 59  ALA   B CA    
1836 C  C     . ALA   B 60  ? 0.34430 0.32238 0.30298 0.02816  0.01601  -0.03653 59  ALA   B C     
1837 O  O     . ALA   B 60  ? 0.36043 0.33255 0.31594 0.02840  0.00992  -0.03873 59  ALA   B O     
1838 C  CB    . ALA   B 60  ? 0.33514 0.32242 0.30764 0.02211  0.01926  -0.03506 59  ALA   B CB    
1839 N  N     . GLY   B 61  ? 0.37553 0.35294 0.32816 0.03291  0.02024  -0.03532 60  GLY   B N     
1840 C  CA    . GLY   B 61  ? 0.39115 0.35975 0.33119 0.03921  0.01756  -0.03711 60  GLY   B CA    
1841 C  C     . GLY   B 61  ? 0.42216 0.38541 0.35484 0.04377  0.01668  -0.03843 60  GLY   B C     
1842 O  O     . GLY   B 61  ? 0.46209 0.41672 0.38288 0.04978  0.01372  -0.04028 60  GLY   B O     
1843 N  N     . GLN   B 62  ? 0.38198 0.34949 0.32078 0.04142  0.01875  -0.03769 61  GLN   B N     
1844 C  CA    . GLN   B 62  ? 0.46040 0.42408 0.39247 0.04629  0.01968  -0.03818 61  GLN   B CA    
1845 C  C     . GLN   B 62  ? 0.45852 0.41191 0.38134 0.04916  0.01191  -0.04199 61  GLN   B C     
1846 O  O     . GLN   B 62  ? 0.51460 0.46684 0.44255 0.04448  0.00596  -0.04383 61  GLN   B O     
1847 C  CB    . GLN   B 62  ? 0.42662 0.39682 0.36836 0.04211  0.02230  -0.03699 61  GLN   B CB    
1848 C  CG    . GLN   B 62  ? 0.45611 0.43581 0.40859 0.03830  0.02809  -0.03363 61  GLN   B CG    
1849 C  CD    . GLN   B 62  ? 0.49844 0.48106 0.45053 0.04246  0.03478  -0.03034 61  GLN   B CD    
1850 O  OE1   . GLN   B 62  ? 0.63113 0.61022 0.57707 0.04696  0.03554  -0.03054 61  GLN   B OE1   
1851 N  NE2   . GLN   B 62  ? 0.46242 0.45126 0.42119 0.04140  0.03957  -0.02695 61  GLN   B NE2   
1852 N  N     . GLU   B 63  ? 0.52512 0.47067 0.43428 0.05729  0.01176  -0.04289 62  GLU   B N     
1853 C  CA    . GLU   B 63  ? 0.59871 0.53269 0.49756 0.06092  0.00324  -0.04687 62  GLU   B CA    
1854 C  C     . GLU   B 63  ? 0.57357 0.50547 0.47444 0.05925  -0.00063 -0.04868 62  GLU   B C     
1855 O  O     . GLU   B 63  ? 0.55882 0.48329 0.45761 0.05859  -0.00932 -0.05177 62  GLU   B O     
1856 C  CB    . GLU   B 63  ? 0.56504 0.49045 0.44706 0.07125  0.00435  -0.04735 62  GLU   B CB    
1857 C  CG    . GLU   B 63  ? 0.67438 0.58611 0.54391 0.07595  -0.00547 -0.05175 62  GLU   B CG    
1858 C  CD    . GLU   B 63  ? 0.76168 0.67168 0.63613 0.07102  -0.01223 -0.05332 62  GLU   B CD    
1859 O  OE1   . GLU   B 63  ? 0.75737 0.67478 0.63902 0.06729  -0.00805 -0.05097 62  GLU   B OE1   
1860 O  OE2   . GLU   B 63  ? 0.84594 0.74696 0.71756 0.07091  -0.02213 -0.05673 62  GLU   B OE2   
1861 N  N     . GLU   B 64  ? 0.56355 0.50191 0.46942 0.05828  0.00528  -0.04664 63  GLU   B N     
1862 C  CA    . GLU   B 64  ? 0.54607 0.48270 0.45378 0.05679  0.00200  -0.04827 63  GLU   B CA    
1863 C  C     . GLU   B 64  ? 0.55441 0.49417 0.47437 0.04842  -0.00323 -0.04910 63  GLU   B C     
1864 O  O     . GLU   B 64  ? 0.55749 0.49421 0.47868 0.04718  -0.00783 -0.05079 63  GLU   B O     
1865 C  CB    . GLU   B 64  ? 0.52452 0.46784 0.43566 0.05746  0.00975  -0.04558 63  GLU   B CB    
1866 C  CG    . GLU   B 64  ? 0.54506 0.50000 0.47077 0.05053  0.01508  -0.04257 63  GLU   B CG    
1867 C  CD    . GLU   B 64  ? 0.66709 0.62818 0.59568 0.05243  0.02317  -0.03914 63  GLU   B CD    
1868 O  OE1   . GLU   B 64  ? 0.62807 0.59025 0.55901 0.05184  0.02377  -0.03925 63  GLU   B OE1   
1869 O  OE2   . GLU   B 64  ? 0.71765 0.68274 0.64715 0.05434  0.02885  -0.03600 63  GLU   B OE2   
1870 N  N     . TYR   B 65  ? 0.50432 0.44998 0.43335 0.04302  -0.00257 -0.04765 64  TYR   B N     
1871 C  CA    . TYR   B 65  ? 0.54903 0.49774 0.48949 0.03595  -0.00700 -0.04766 64  TYR   B CA    
1872 C  C     . TYR   B 65  ? 0.54532 0.48848 0.48536 0.03505  -0.01441 -0.04894 64  TYR   B C     
1873 O  O     . TYR   B 65  ? 0.49468 0.44250 0.44526 0.02934  -0.01595 -0.04751 64  TYR   B O     
1874 C  CB    . TYR   B 65  ? 0.49145 0.45133 0.44376 0.03032  -0.00092 -0.04473 64  TYR   B CB    
1875 C  CG    . TYR   B 65  ? 0.42499 0.38987 0.37896 0.03089  0.00535  -0.04342 64  TYR   B CG    
1876 C  CD1   . TYR   B 65  ? 0.38933 0.35321 0.34450 0.03037  0.00379  -0.04435 64  TYR   B CD1   
1877 C  CD2   . TYR   B 65  ? 0.43941 0.40983 0.39436 0.03201  0.01252  -0.04104 64  TYR   B CD2   
1878 C  CE1   . TYR   B 65  ? 0.41052 0.37856 0.36723 0.03107  0.00921  -0.04313 64  TYR   B CE1   
1879 C  CE2   . TYR   B 65  ? 0.38003 0.35477 0.33767 0.03252  0.01769  -0.03947 64  TYR   B CE2   
1880 C  CZ    . TYR   B 65  ? 0.36177 0.33533 0.32022 0.03199  0.01603  -0.04061 64  TYR   B CZ    
1881 O  OH    . TYR   B 65  ? 0.37135 0.34887 0.33267 0.03252  0.02078  -0.03906 64  TYR   B OH    
1882 N  N     . SER   B 66  ? 0.55378 0.48636 0.48155 0.04104  -0.01952 -0.05155 65  SER   B N     
1883 C  CA    . SER   B 66  ? 0.57214 0.49807 0.49872 0.04083  -0.02743 -0.05297 65  SER   B CA    
1884 C  C     . SER   B 66  ? 0.63013 0.55598 0.56825 0.03494  -0.03477 -0.05277 65  SER   B C     
1885 O  O     . SER   B 66  ? 0.66529 0.59158 0.61016 0.03149  -0.03872 -0.05183 65  SER   B O     
1886 C  CB    . SER   B 66  ? 0.64714 0.55998 0.55735 0.04909  -0.03281 -0.05633 65  SER   B CB    
1887 O  OG    . SER   B 66  ? 0.73537 0.64804 0.63458 0.05568  -0.02554 -0.05599 65  SER   B OG    
1888 N  N     . ALA   B 67  ? 0.61456 0.53960 0.55534 0.03398  -0.03690 -0.05332 66  ALA   B N     
1889 C  CA    . ALA   B 67  ? 0.63462 0.55945 0.58702 0.02880  -0.04398 -0.05250 66  ALA   B CA    
1890 C  C     . ALA   B 67  ? 0.64427 0.58094 0.61188 0.02180  -0.03928 -0.04852 66  ALA   B C     
1891 O  O     . ALA   B 67  ? 0.72432 0.66192 0.70281 0.01755  -0.04440 -0.04662 66  ALA   B O     
1892 C  CB    . ALA   B 67  ? 0.64277 0.56358 0.59398 0.02982  -0.04743 -0.05401 66  ALA   B CB    
1893 N  N     . MET   B 68  ? 0.58091 0.52630 0.54966 0.02090  -0.02992 -0.04695 67  MET   B N     
1894 C  CA    . MET   B 68  ? 0.49222 0.44795 0.47338 0.01531  -0.02536 -0.04349 67  MET   B CA    
1895 C  C     . MET   B 68  ? 0.51917 0.47714 0.50424 0.01339  -0.02563 -0.04182 67  MET   B C     
1896 O  O     . MET   B 68  ? 0.50645 0.47240 0.50115 0.00933  -0.02218 -0.03881 67  MET   B O     
1897 C  CB    . MET   B 68  ? 0.53015 0.49315 0.51069 0.01542  -0.01634 -0.04270 67  MET   B CB    
1898 C  CG    . MET   B 68  ? 0.55123 0.51503 0.53265 0.01537  -0.01526 -0.04318 67  MET   B CG    
1899 S  SD    . MET   B 68  ? 0.84625 0.80012 0.81377 0.02192  -0.01809 -0.04677 67  MET   B SD    
1900 C  CE    . MET   B 68  ? 0.58846 0.54424 0.56047 0.02024  -0.01789 -0.04681 67  MET   B CE    
1901 N  N     . ARG   B 69  ? 0.54111 0.49189 0.51860 0.01653  -0.02980 -0.04368 68  ARG   B N     
1902 C  CA    . ARG   B 69  ? 0.53002 0.48303 0.51043 0.01497  -0.02948 -0.04222 68  ARG   B CA    
1903 C  C     . ARG   B 69  ? 0.52725 0.47953 0.51836 0.01114  -0.03636 -0.04018 68  ARG   B C     
1904 O  O     . ARG   B 69  ? 0.52790 0.48529 0.52573 0.00833  -0.03465 -0.03762 68  ARG   B O     
1905 C  CB    . ARG   B 69  ? 0.51338 0.45911 0.48090 0.02029  -0.03066 -0.04485 68  ARG   B CB    
1906 C  CG    . ARG   B 69  ? 0.51387 0.46146 0.47224 0.02431  -0.02289 -0.04558 68  ARG   B CG    
1907 C  CD    . ARG   B 69  ? 0.53061 0.47071 0.47605 0.03027  -0.02403 -0.04761 68  ARG   B CD    
1908 N  NE    . ARG   B 69  ? 0.57526 0.51566 0.51135 0.03541  -0.01736 -0.04791 68  ARG   B NE    
1909 C  CZ    . ARG   B 69  ? 0.54688 0.47904 0.46901 0.04266  -0.01825 -0.04985 68  ARG   B CZ    
1910 N  NH1   . ARG   B 69  ? 0.59123 0.51336 0.50604 0.04575  -0.02610 -0.05233 68  ARG   B NH1   
1911 N  NH2   . ARG   B 69  ? 0.64378 0.57749 0.55917 0.04732  -0.01127 -0.04904 68  ARG   B NH2   
1912 N  N     . ASP   B 70  ? 0.50779 0.45389 0.50123 0.01108  -0.04416 -0.04091 69  ASP   B N     
1913 C  CA    . ASP   B 70  ? 0.53797 0.48199 0.54200 0.00797  -0.05200 -0.03866 69  ASP   B CA    
1914 C  C     . ASP   B 70  ? 0.51128 0.46626 0.53008 0.00272  -0.04758 -0.03341 69  ASP   B C     
1915 O  O     . ASP   B 70  ? 0.46535 0.42157 0.49129 0.00063  -0.04999 -0.03086 69  ASP   B O     
1916 C  CB    . ASP   B 70  ? 0.55380 0.49039 0.55982 0.00836  -0.06072 -0.03975 69  ASP   B CB    
1917 C  CG    . ASP   B 70  ? 0.67349 0.59783 0.66336 0.01459  -0.06583 -0.04511 69  ASP   B CG    
1918 O  OD1   . ASP   B 70  ? 0.66515 0.58876 0.64217 0.01882  -0.06005 -0.04756 69  ASP   B OD1   
1919 O  OD2   . ASP   B 70  ? 0.74908 0.66420 0.73919 0.01561  -0.07585 -0.04658 69  ASP   B OD2   
1920 N  N     . GLN   B 71  ? 0.55409 0.51691 0.57685 0.00105  -0.04079 -0.03170 70  GLN   B N     
1921 C  CA    . GLN   B 71  ? 0.52781 0.50017 0.56354 -0.00291 -0.03680 -0.02657 70  GLN   B CA    
1922 C  C     . GLN   B 71  ? 0.45905 0.43638 0.49479 -0.00348 -0.03193 -0.02514 70  GLN   B C     
1923 O  O     . GLN   B 71  ? 0.48707 0.46853 0.53303 -0.00600 -0.03248 -0.02096 70  GLN   B O     
1924 C  CB    . GLN   B 71  ? 0.51179 0.49036 0.54927 -0.00361 -0.03057 -0.02570 70  GLN   B CB    
1925 C  CG    . GLN   B 71  ? 0.52708 0.50554 0.55254 -0.00076 -0.02474 -0.02949 70  GLN   B CG    
1926 C  CD    . GLN   B 71  ? 0.58411 0.57114 0.61206 -0.00190 -0.01655 -0.02774 70  GLN   B CD    
1927 O  OE1   . GLN   B 71  ? 0.61643 0.60745 0.64309 -0.00193 -0.01189 -0.02714 70  GLN   B OE1   
1928 N  NE2   . GLN   B 71  ? 0.62736 0.61673 0.65856 -0.00261 -0.01515 -0.02706 70  GLN   B NE2   
1929 N  N     . TYR   B 72  ? 0.44893 0.42610 0.47395 -0.00103 -0.02708 -0.02812 71  TYR   B N     
1930 C  CA    . TYR   B 72  ? 0.43313 0.41502 0.45915 -0.00181 -0.02294 -0.02654 71  TYR   B CA    
1931 C  C     . TYR   B 72  ? 0.35992 0.33618 0.38401 -0.00111 -0.02847 -0.02728 71  TYR   B C     
1932 O  O     . TYR   B 72  ? 0.39030 0.37045 0.41892 -0.00266 -0.02690 -0.02488 71  TYR   B O     
1933 C  CB    . TYR   B 72  ? 0.41609 0.40141 0.43426 -0.00009 -0.01531 -0.02835 71  TYR   B CB    
1934 C  CG    . TYR   B 72  ? 0.45250 0.43193 0.45828 0.00386  -0.01517 -0.03232 71  TYR   B CG    
1935 C  CD1   . TYR   B 72  ? 0.41993 0.39373 0.41922 0.00611  -0.01826 -0.03400 71  TYR   B CD1   
1936 C  CD2   . TYR   B 72  ? 0.46054 0.44041 0.46110 0.00573  -0.01135 -0.03398 71  TYR   B CD2   
1937 C  CE1   . TYR   B 72  ? 0.45802 0.42654 0.44522 0.01069  -0.01733 -0.03710 71  TYR   B CE1   
1938 C  CE2   . TYR   B 72  ? 0.48478 0.45999 0.47449 0.00993  -0.01028 -0.03670 71  TYR   B CE2   
1939 C  CZ    . TYR   B 72  ? 0.41983 0.38943 0.40262 0.01263  -0.01303 -0.03814 71  TYR   B CZ    
1940 O  OH    . TYR   B 72  ? 0.61301 0.57790 0.58429 0.01775  -0.01137 -0.04033 71  TYR   B OH    
1941 N  N     . MET   B 73  ? 0.39823 0.36499 0.41586 0.00137  -0.03544 -0.03043 72  MET   B N     
1942 C  CA    . MET   B 73  ? 0.37942 0.34000 0.39624 0.00199  -0.04203 -0.03096 72  MET   B CA    
1943 C  C     . MET   B 73  ? 0.43664 0.39867 0.46841 -0.00186 -0.04770 -0.02661 72  MET   B C     
1944 O  O     . MET   B 73  ? 0.40908 0.37061 0.44478 -0.00289 -0.05040 -0.02503 72  MET   B O     
1945 C  CB    . MET   B 73  ? 0.42465 0.37345 0.42914 0.00660  -0.04850 -0.03573 72  MET   B CB    
1946 C  CG    . MET   B 73  ? 0.42232 0.36987 0.41217 0.01118  -0.04235 -0.03907 72  MET   B CG    
1947 S  SD    . MET   B 73  ? 0.49138 0.42494 0.46503 0.01807  -0.04890 -0.04432 72  MET   B SD    
1948 C  CE    . MET   B 73  ? 0.46955 0.40571 0.43013 0.02278  -0.03885 -0.04576 72  MET   B CE    
1949 N  N     . ARG   B 74  ? 0.44452 0.40878 0.48560 -0.00401 -0.04930 -0.02411 73  ARG   B N     
1950 C  CA    . ARG   B 74  ? 0.43639 0.40350 0.49376 -0.00763 -0.05364 -0.01863 73  ARG   B CA    
1951 C  C     . ARG   B 74  ? 0.43109 0.40841 0.49623 -0.00987 -0.04646 -0.01389 73  ARG   B C     
1952 O  O     . ARG   B 74  ? 0.42597 0.40454 0.50052 -0.01171 -0.04945 -0.01012 73  ARG   B O     
1953 C  CB    . ARG   B 74  ? 0.45844 0.42661 0.52445 -0.00918 -0.05590 -0.01639 73  ARG   B CB    
1954 C  CG    . ARG   B 74  ? 0.59936 0.55659 0.66466 -0.00814 -0.06705 -0.01888 73  ARG   B CG    
1955 C  CD    . ARG   B 74  ? 0.55203 0.51071 0.62883 -0.01028 -0.07014 -0.01566 73  ARG   B CD    
1956 N  NE    . ARG   B 74  ? 0.61251 0.57390 0.68229 -0.00903 -0.06391 -0.01793 73  ARG   B NE    
1957 C  CZ    . ARG   B 74  ? 0.62105 0.57485 0.67940 -0.00607 -0.06676 -0.02318 73  ARG   B CZ    
1958 N  NH1   . ARG   B 74  ? 0.63986 0.58206 0.69151 -0.00356 -0.07618 -0.02698 73  ARG   B NH1   
1959 N  NH2   . ARG   B 74  ? 0.53983 0.49734 0.59300 -0.00521 -0.06021 -0.02460 73  ARG   B NH2   
1960 N  N     . THR   B 75  ? 0.40630 0.39044 0.46705 -0.00936 -0.03722 -0.01415 74  THR   B N     
1961 C  CA    . THR   B 75  ? 0.37962 0.37288 0.44625 -0.01072 -0.03028 -0.00995 74  THR   B CA    
1962 C  C     . THR   B 75  ? 0.39502 0.38807 0.45615 -0.01001 -0.02863 -0.01123 74  THR   B C     
1963 O  O     . THR   B 75  ? 0.42277 0.42077 0.49146 -0.01142 -0.02692 -0.00706 74  THR   B O     
1964 C  CB    . THR   B 75  ? 0.37358 0.37260 0.43654 -0.01000 -0.02227 -0.01038 74  THR   B CB    
1965 O  OG1   . THR   B 75  ? 0.48060 0.47978 0.54895 -0.01066 -0.02395 -0.00904 74  THR   B OG1   
1966 C  CG2   . THR   B 75  ? 0.42079 0.42816 0.48863 -0.01058 -0.01562 -0.00625 74  THR   B CG2   
1967 N  N     . GLY   B 76  ? 0.35726 0.34484 0.40539 -0.00753 -0.02878 -0.01656 75  GLY   B N     
1968 C  CA    . GLY   B 76  ? 0.32541 0.31316 0.36785 -0.00664 -0.02650 -0.01775 75  GLY   B CA    
1969 C  C     . GLY   B 76  ? 0.38726 0.37186 0.43540 -0.00776 -0.03276 -0.01593 75  GLY   B C     
1970 O  O     . GLY   B 76  ? 0.39303 0.37123 0.44467 -0.00802 -0.04098 -0.01606 75  GLY   B O     
1971 N  N     . GLU   B 77  ? 0.35461 0.34330 0.40357 -0.00831 -0.02925 -0.01436 76  GLU   B N     
1972 C  CA    . GLU   B 77  ? 0.31494 0.30104 0.36816 -0.00919 -0.03426 -0.01285 76  GLU   B CA    
1973 C  C     . GLU   B 77  ? 0.41542 0.39482 0.45626 -0.00654 -0.03608 -0.01757 76  GLU   B C     
1974 O  O     . GLU   B 77  ? 0.46215 0.43514 0.50386 -0.00636 -0.04339 -0.01806 76  GLU   B O     
1975 C  CB    . GLU   B 77  ? 0.36804 0.36295 0.43007 -0.01115 -0.02911 -0.00774 76  GLU   B CB    
1976 C  CG    . GLU   B 77  ? 0.42962 0.43108 0.50493 -0.01310 -0.02752 -0.00186 76  GLU   B CG    
1977 C  CD    . GLU   B 77  ? 0.48509 0.49565 0.56590 -0.01357 -0.02031 0.00293  76  GLU   B CD    
1978 O  OE1   . GLU   B 77  ? 0.47111 0.48325 0.54523 -0.01268 -0.01627 0.00129  76  GLU   B OE1   
1979 O  OE2   . GLU   B 77  ? 0.62003 0.63603 0.71176 -0.01443 -0.01868 0.00856  76  GLU   B OE2   
1980 N  N     . GLY   B 78  ? 0.38605 0.36698 0.41620 -0.00440 -0.02961 -0.02053 77  GLY   B N     
1981 C  CA    . GLY   B 78  ? 0.41442 0.38946 0.43257 -0.00126 -0.03037 -0.02446 77  GLY   B CA    
1982 C  C     . GLY   B 78  ? 0.33738 0.31157 0.34445 0.00187  -0.02551 -0.02783 77  GLY   B C     
1983 O  O     . GLY   B 78  ? 0.35565 0.33582 0.36492 0.00094  -0.01995 -0.02685 77  GLY   B O     
1984 N  N     . PHE   B 79  ? 0.32059 0.28720 0.31571 0.00599  -0.02756 -0.03150 78  PHE   B N     
1985 C  CA    . PHE   B 79  ? 0.33462 0.29923 0.31927 0.00979  -0.02378 -0.03424 78  PHE   B CA    
1986 C  C     . PHE   B 79  ? 0.37857 0.34191 0.35314 0.01337  -0.01985 -0.03574 78  PHE   B C     
1987 O  O     . PHE   B 79  ? 0.37828 0.33540 0.34744 0.01556  -0.02406 -0.03712 78  PHE   B O     
1988 C  CB    . PHE   B 79  ? 0.34640 0.30164 0.32525 0.01276  -0.03051 -0.03701 78  PHE   B CB    
1989 C  CG    . PHE   B 79  ? 0.34522 0.30191 0.33443 0.00934  -0.03414 -0.03529 78  PHE   B CG    
1990 C  CD1   . PHE   B 79  ? 0.38895 0.34417 0.38823 0.00629  -0.04105 -0.03318 78  PHE   B CD1   
1991 C  CD2   . PHE   B 79  ? 0.36282 0.32326 0.35302 0.00898  -0.03012 -0.03515 78  PHE   B CD2   
1992 C  CE1   . PHE   B 79  ? 0.36409 0.32147 0.37448 0.00313  -0.04397 -0.03066 78  PHE   B CE1   
1993 C  CE2   . PHE   B 79  ? 0.30546 0.26769 0.30569 0.00585  -0.03311 -0.03316 78  PHE   B CE2   
1994 C  CZ    . PHE   B 79  ? 0.33924 0.30013 0.34959 0.00303  -0.03980 -0.03077 78  PHE   B CZ    
1995 N  N     . LEU   B 80  ? 0.29874 0.26813 0.27176 0.01385  -0.01199 -0.03510 79  LEU   B N     
1996 C  CA    . LEU   B 80  ? 0.35078 0.31927 0.31449 0.01790  -0.00746 -0.03598 79  LEU   B CA    
1997 C  C     . LEU   B 80  ? 0.39462 0.35713 0.34815 0.02317  -0.00745 -0.03813 79  LEU   B C     
1998 O  O     . LEU   B 80  ? 0.36877 0.33446 0.32404 0.02288  -0.00417 -0.03770 79  LEU   B O     
1999 C  CB    . LEU   B 80  ? 0.38122 0.35897 0.34961 0.01590  0.00045  -0.03374 79  LEU   B CB    
2000 C  CG    . LEU   B 80  ? 0.42885 0.41231 0.40321 0.01276  0.00266  -0.03177 79  LEU   B CG    
2001 C  CD1   . LEU   B 80  ? 0.45854 0.44813 0.43330 0.01312  0.00999  -0.03045 79  LEU   B CD1   
2002 C  CD2   . LEU   B 80  ? 0.39320 0.37140 0.36256 0.01451  -0.00098 -0.03272 79  LEU   B CD2   
2003 N  N     . CYS   B 81  ? 0.36631 0.31983 0.30870 0.02841  -0.01112 -0.04038 80  CYS   B N     
2004 C  CA    . CYS   B 81  ? 0.40215 0.34871 0.33295 0.03469  -0.01141 -0.04241 80  CYS   B CA    
2005 C  C     . CYS   B 81  ? 0.46548 0.41388 0.38883 0.03937  -0.00401 -0.04128 80  CYS   B C     
2006 O  O     . CYS   B 81  ? 0.42371 0.36828 0.34024 0.04264  -0.00455 -0.04173 80  CYS   B O     
2007 C  CB    . CYS   B 81  ? 0.44779 0.38201 0.37003 0.03848  -0.02083 -0.04562 80  CYS   B CB    
2008 S  SG    . CYS   B 81  ? 0.48324 0.41570 0.41709 0.03259  -0.03012 -0.04594 80  CYS   B SG    
2009 N  N     . VAL   B 82  ? 0.35200 0.30638 0.27746 0.03967  0.00280  -0.03945 81  VAL   B N     
2010 C  CA    . VAL   B 82  ? 0.44391 0.40265 0.36681 0.04281  0.01073  -0.03696 81  VAL   B CA    
2011 C  C     . VAL   B 82  ? 0.44926 0.40217 0.36001 0.05089  0.01289  -0.03727 81  VAL   B C     
2012 O  O     . VAL   B 82  ? 0.40020 0.35147 0.30981 0.05190  0.01223  -0.03805 81  VAL   B O     
2013 C  CB    . VAL   B 82  ? 0.37651 0.34615 0.31155 0.03766  0.01673  -0.03406 81  VAL   B CB    
2014 C  CG1   . VAL   B 82  ? 0.41820 0.39278 0.35338 0.03993  0.02399  -0.03094 81  VAL   B CG1   
2015 C  CG2   . VAL   B 82  ? 0.32892 0.30328 0.27490 0.03037  0.01394  -0.03397 81  VAL   B CG2   
2016 N  N     . PHE   B 83  ? 0.40672 0.35644 0.30804 0.05708  0.01574  -0.03643 82  PHE   B N     
2017 C  CA    . PHE   B 83  ? 0.45688 0.40377 0.34811 0.06530  0.02072  -0.03495 82  PHE   B CA    
2018 C  C     . PHE   B 83  ? 0.40250 0.35735 0.29789 0.06625  0.02943  -0.03031 82  PHE   B C     
2019 O  O     . PHE   B 83  ? 0.44132 0.40188 0.34498 0.06119  0.03034  -0.02917 82  PHE   B O     
2020 C  CB    . PHE   B 83  ? 0.45167 0.38558 0.32546 0.07397  0.01587  -0.03792 82  PHE   B CB    
2021 C  CG    . PHE   B 83  ? 0.45973 0.39023 0.32774 0.07639  0.01477  -0.03820 82  PHE   B CG    
2022 C  CD1   . PHE   B 83  ? 0.45792 0.38548 0.32906 0.07161  0.00725  -0.04096 82  PHE   B CD1   
2023 C  CD2   . PHE   B 83  ? 0.55203 0.48218 0.41163 0.08382  0.02133  -0.03534 82  PHE   B CD2   
2024 C  CE1   . PHE   B 83  ? 0.52655 0.45062 0.39215 0.07394  0.00597  -0.04134 82  PHE   B CE1   
2025 C  CE2   . PHE   B 83  ? 0.53753 0.46437 0.39136 0.08636  0.02042  -0.03559 82  PHE   B CE2   
2026 C  CZ    . PHE   B 83  ? 0.49722 0.42077 0.35365 0.08139  0.01259  -0.03885 82  PHE   B CZ    
2027 N  N     . ALA   B 84  ? 0.42802 0.38351 0.31850 0.07275  0.03585  -0.02722 83  ALA   B N     
2028 C  CA    . ALA   B 84  ? 0.49144 0.45364 0.38553 0.07486  0.04399  -0.02208 83  ALA   B CA    
2029 C  C     . ALA   B 84  ? 0.52933 0.48396 0.40789 0.08485  0.04559  -0.02146 83  ALA   B C     
2030 O  O     . ALA   B 84  ? 0.47936 0.42474 0.34400 0.09231  0.04336  -0.02350 83  ALA   B O     
2031 C  CB    . ALA   B 84  ? 0.42286 0.39273 0.32539 0.07479  0.05089  -0.01762 83  ALA   B CB    
2032 N  N     . ILE   B 85  ? 0.52598 0.48399 0.40627 0.08540  0.04918  -0.01875 84  ILE   B N     
2033 C  CA    . ILE   B 85  ? 0.55303 0.50305 0.41775 0.09481  0.04984  -0.01866 84  ILE   B CA    
2034 C  C     . ILE   B 85  ? 0.64522 0.59496 0.50237 0.10488  0.05793  -0.01371 84  ILE   B C     
2035 O  O     . ILE   B 85  ? 0.59586 0.53771 0.43758 0.11451  0.05879  -0.01355 84  ILE   B O     
2036 C  CB    . ILE   B 85  ? 0.54195 0.49508 0.41010 0.09253  0.05082  -0.01745 84  ILE   B CB    
2037 C  CG1   . ILE   B 85  ? 0.56803 0.53419 0.45346 0.08653  0.05751  -0.01218 84  ILE   B CG1   
2038 C  CG2   . ILE   B 85  ? 0.56700 0.51598 0.43590 0.08627  0.04170  -0.02292 84  ILE   B CG2   
2039 C  CD1   . ILE   B 85  ? 0.55728 0.52788 0.44272 0.09334  0.06694  -0.00531 84  ILE   B CD1   
2040 N  N     . ASN   B 86  ? 0.56963 0.52742 0.43697 0.10340  0.06382  -0.00945 85  ASN   B N     
2041 C  CA    . ASN   B 86  ? 0.63425 0.59234 0.49596 0.11283  0.07164  -0.00414 85  ASN   B CA    
2042 C  C     . ASN   B 86  ? 0.62810 0.58098 0.48327 0.11578  0.06939  -0.00653 85  ASN   B C     
2043 O  O     . ASN   B 86  ? 0.67884 0.63419 0.53341 0.12168  0.07618  -0.00169 85  ASN   B O     
2044 C  CB    . ASN   B 86  ? 0.62018 0.59133 0.49938 0.10959  0.08017  0.00340  85  ASN   B CB    
2045 C  CG    . ASN   B 86  ? 0.61952 0.59789 0.51488 0.09938  0.07814  0.00251  85  ASN   B CG    
2046 O  OD1   . ASN   B 86  ? 0.58845 0.56380 0.48425 0.09303  0.07058  -0.00352 85  ASN   B OD1   
2047 N  ND2   . ASN   B 86  ? 0.64029 0.62790 0.54911 0.09808  0.08465  0.00871  85  ASN   B ND2   
2048 N  N     . ASN   B 87  ? 0.62822 0.57438 0.47966 0.11159  0.06005  -0.01347 86  ASN   B N     
2049 C  CA    . ASN   B 87  ? 0.59755 0.53902 0.44454 0.11283  0.05677  -0.01629 86  ASN   B CA    
2050 C  C     . ASN   B 87  ? 0.62717 0.55443 0.45770 0.11687  0.04709  -0.02310 86  ASN   B C     
2051 O  O     . ASN   B 87  ? 0.57326 0.49826 0.40801 0.10947  0.03874  -0.02800 86  ASN   B O     
2052 C  CB    . ASN   B 87  ? 0.59012 0.53962 0.45415 0.10157  0.05477  -0.01726 86  ASN   B CB    
2053 C  CG    . ASN   B 87  ? 0.61680 0.56309 0.47780 0.10303  0.05299  -0.01901 86  ASN   B CG    
2054 O  OD1   . ASN   B 87  ? 0.67100 0.60697 0.51615 0.11124  0.05032  -0.02142 86  ASN   B OD1   
2055 N  ND2   . ASN   B 87  ? 0.62281 0.57740 0.49848 0.09540  0.05420  -0.01792 86  ASN   B ND2   
2056 N  N     . THR   B 88  ? 0.59369 0.51104 0.40556 0.12905  0.04802  -0.02311 87  THR   B N     
2057 C  CA    . THR   B 88  ? 0.66278 0.56502 0.45773 0.13405  0.03800  -0.02965 87  THR   B CA    
2058 C  C     . THR   B 88  ? 0.58161 0.47981 0.37885 0.12905  0.02978  -0.03462 87  THR   B C     
2059 O  O     . THR   B 88  ? 0.64843 0.53865 0.44286 0.12597  0.01934  -0.04022 87  THR   B O     
2060 C  CB    . THR   B 88  ? 0.67383 0.56582 0.44714 0.14936  0.04114  -0.02839 87  THR   B CB    
2061 O  OG1   . THR   B 88  ? 0.76595 0.66045 0.53668 0.15363  0.04716  -0.02441 87  THR   B OG1   
2062 C  CG2   . THR   B 88  ? 0.68841 0.56333 0.44343 0.15519  0.02974  -0.03553 87  THR   B CG2   
2063 N  N     . LYS   B 89  ? 0.60628 0.51023 0.40985 0.12790  0.03424  -0.03230 88  LYS   B N     
2064 C  CA    . LYS   B 89  ? 0.61413 0.51430 0.41957 0.12373  0.02693  -0.03667 88  LYS   B CA    
2065 C  C     . LYS   B 89  ? 0.60225 0.50782 0.42380 0.11075  0.02089  -0.03925 88  LYS   B C     
2066 O  O     . LYS   B 89  ? 0.53129 0.42954 0.35124 0.10789  0.01102  -0.04424 88  LYS   B O     
2067 C  CB    . LYS   B 89  ? 0.55610 0.46284 0.36669 0.12456  0.03390  -0.03305 88  LYS   B CB    
2068 C  CG    . LYS   B 89  ? 0.69477 0.59821 0.50735 0.12071  0.02734  -0.03706 88  LYS   B CG    
2069 C  CD    . LYS   B 89  ? 0.71021 0.59720 0.50420 0.12822  0.01772  -0.04281 88  LYS   B CD    
2070 C  CE    . LYS   B 89  ? 0.72715 0.61133 0.52242 0.12615  0.01299  -0.04562 88  LYS   B CE    
2071 N  NZ    . LYS   B 89  ? 0.74321 0.64008 0.55973 0.11366  0.01454  -0.04428 88  LYS   B NZ    
2072 N  N     . SER   B 90  ? 0.57432 0.49231 0.41137 0.10330  0.02652  -0.03561 89  SER   B N     
2073 C  CA    . SER   B 90  ? 0.50777 0.43123 0.35955 0.09183  0.02171  -0.03745 89  SER   B CA    
2074 C  C     . SER   B 90  ? 0.50856 0.42401 0.35497 0.09126  0.01325  -0.04137 89  SER   B C     
2075 O  O     . SER   B 90  ? 0.45776 0.37241 0.31147 0.08422  0.00587  -0.04428 89  SER   B O     
2076 C  CB    . SER   B 90  ? 0.51149 0.44881 0.37916 0.08532  0.02947  -0.03273 89  SER   B CB    
2077 O  OG    . SER   B 90  ? 0.49009 0.42891 0.35707 0.08615  0.03169  -0.03111 89  SER   B OG    
2078 N  N     . PHE   B 91  ? 0.52172 0.43047 0.35492 0.09925  0.01390  -0.04132 90  PHE   B N     
2079 C  CA    . PHE   B 91  ? 0.55023 0.45009 0.37741 0.09938  0.00509  -0.04527 90  PHE   B CA    
2080 C  C     . PHE   B 91  ? 0.54220 0.42845 0.35869 0.10301  -0.00552 -0.05050 90  PHE   B C     
2081 O  O     . PHE   B 91  ? 0.57831 0.45989 0.39852 0.09814  -0.01505 -0.05390 90  PHE   B O     
2082 C  CB    . PHE   B 91  ? 0.54330 0.43969 0.35900 0.10725  0.00892  -0.04368 90  PHE   B CB    
2083 C  CG    . PHE   B 91  ? 0.52471 0.41173 0.33382 0.10783  0.00005  -0.04757 90  PHE   B CG    
2084 C  CD1   . PHE   B 91  ? 0.54777 0.44060 0.37008 0.09847  -0.00274 -0.04780 90  PHE   B CD1   
2085 C  CD2   . PHE   B 91  ? 0.59710 0.46900 0.38622 0.11838  -0.00560 -0.05089 90  PHE   B CD2   
2086 C  CE1   . PHE   B 91  ? 0.59188 0.47625 0.40908 0.09889  -0.01104 -0.05105 90  PHE   B CE1   
2087 C  CE2   . PHE   B 91  ? 0.62719 0.48979 0.41049 0.11897  -0.01454 -0.05457 90  PHE   B CE2   
2088 C  CZ    . PHE   B 91  ? 0.60570 0.47477 0.40355 0.10903  -0.01722 -0.05452 90  PHE   B CZ    
2089 N  N     . GLU   B 92  ? 0.62873 0.50837 0.43248 0.11163  -0.00430 -0.05096 91  GLU   B N     
2090 C  CA    . GLU   B 92  ? 0.65770 0.52382 0.45122 0.11526  -0.01497 -0.05609 91  GLU   B CA    
2091 C  C     . GLU   B 92  ? 0.60121 0.47177 0.40969 0.10536  -0.01989 -0.05742 91  GLU   B C     
2092 O  O     . GLU   B 92  ? 0.61873 0.47970 0.42497 0.10454  -0.03096 -0.06161 91  GLU   B O     
2093 C  CB    . GLU   B 92  ? 0.66828 0.52657 0.44463 0.12701  -0.01214 -0.05612 91  GLU   B CB    
2094 C  CG    . GLU   B 92  ? 0.74874 0.60750 0.51359 0.13689  -0.00251 -0.05224 91  GLU   B CG    
2095 C  CD    . GLU   B 92  ? 0.85639 0.70568 0.60866 0.14277  -0.00669 -0.05422 91  GLU   B CD    
2096 O  OE1   . GLU   B 92  ? 0.93664 0.77680 0.68718 0.14017  -0.01842 -0.05923 91  GLU   B OE1   
2097 O  OE2   . GLU   B 92  ? 0.90086 0.75183 0.64541 0.15020  0.00178  -0.05040 91  GLU   B OE2   
2098 N  N     . ASP   B 93  ? 0.59531 0.47986 0.41899 0.09825  -0.01206 -0.05374 92  ASP   B N     
2099 C  CA    . ASP   B 93  ? 0.57795 0.46761 0.41618 0.08897  -0.01579 -0.05449 92  ASP   B CA    
2100 C  C     . ASP   B 93  ? 0.59347 0.48497 0.44344 0.08041  -0.02239 -0.05555 92  ASP   B C     
2101 O  O     . ASP   B 93  ? 0.58079 0.47239 0.43989 0.07444  -0.02853 -0.05688 92  ASP   B O     
2102 C  CB    . ASP   B 93  ? 0.56184 0.46555 0.41281 0.08397  -0.00587 -0.05028 92  ASP   B CB    
2103 C  CG    . ASP   B 93  ? 0.61618 0.51902 0.45844 0.09146  0.00037  -0.04868 92  ASP   B CG    
2104 O  OD1   . ASP   B 93  ? 0.68284 0.57396 0.50991 0.09968  -0.00403 -0.05145 92  ASP   B OD1   
2105 O  OD2   . ASP   B 93  ? 0.69846 0.61218 0.54931 0.08933  0.00952  -0.04446 92  ASP   B OD2   
2106 N  N     . ILE   B 94  ? 0.60200 0.49505 0.45218 0.07997  -0.02110 -0.05462 93  ILE   B N     
2107 C  CA    . ILE   B 94  ? 0.56543 0.46120 0.42755 0.07191  -0.02647 -0.05493 93  ILE   B CA    
2108 C  C     . ILE   B 94  ? 0.56469 0.44924 0.42502 0.07158  -0.03927 -0.05877 93  ILE   B C     
2109 O  O     . ILE   B 94  ? 0.56400 0.45213 0.43827 0.06365  -0.04407 -0.05838 93  ILE   B O     
2110 C  CB    . ILE   B 94  ? 0.54899 0.44586 0.40851 0.07315  -0.02387 -0.05383 93  ILE   B CB    
2111 C  CG1   . ILE   B 94  ? 0.56939 0.47954 0.43660 0.07057  -0.01219 -0.04940 93  ILE   B CG1   
2112 C  CG2   . ILE   B 94  ? 0.59525 0.49073 0.46320 0.06704  -0.03189 -0.05498 93  ILE   B CG2   
2113 C  CD1   . ILE   B 94  ? 0.49708 0.41907 0.38246 0.06062  -0.00978 -0.04727 93  ILE   B CD1   
2114 N  N     . HIS   B 95  ? 0.57211 0.44256 0.41550 0.08053  -0.04532 -0.06224 94  HIS   B N     
2115 C  CA    . HIS   B 95  ? 0.64563 0.50452 0.48825 0.08003  -0.05888 -0.06589 94  HIS   B CA    
2116 C  C     . HIS   B 95  ? 0.60759 0.46756 0.45889 0.07568  -0.06265 -0.06629 94  HIS   B C     
2117 O  O     . HIS   B 95  ? 0.65336 0.51049 0.51448 0.07040  -0.07204 -0.06713 94  HIS   B O     
2118 C  CB    . HIS   B 95  ? 0.69511 0.53694 0.51620 0.09129  -0.06574 -0.06996 94  HIS   B CB    
2119 C  CG    . HIS   B 95  ? 0.74819 0.58158 0.55495 0.09961  -0.06634 -0.07210 94  HIS   B CG    
2120 N  ND1   . HIS   B 95  ? 0.82781 0.65382 0.63560 0.09886  -0.07561 -0.07483 94  HIS   B ND1   
2121 C  CD2   . HIS   B 95  ? 0.79223 0.62289 0.58294 0.10946  -0.05901 -0.07168 94  HIS   B CD2   
2122 C  CE1   . HIS   B 95  ? 0.84077 0.65986 0.63328 0.10774  -0.07392 -0.07636 94  HIS   B CE1   
2123 N  NE2   . HIS   B 95  ? 0.87233 0.69422 0.65427 0.11445  -0.06366 -0.07429 94  HIS   B NE2   
2124 N  N     . HIS   B 96  ? 0.57564 0.44061 0.42518 0.07735  -0.05517 -0.06512 95  HIS   B N     
2125 C  CA    . HIS   B 96  ? 0.58389 0.45235 0.44368 0.07216  -0.05709 -0.06487 95  HIS   B CA    
2126 C  C     . HIS   B 96  ? 0.56393 0.44419 0.44482 0.06102  -0.05636 -0.06184 95  HIS   B C     
2127 O  O     . HIS   B 96  ? 0.55112 0.43003 0.44200 0.05609  -0.06386 -0.06213 95  HIS   B O     
2128 C  CB    . HIS   B 96  ? 0.61188 0.48625 0.46823 0.07495  -0.04732 -0.06330 95  HIS   B CB    
2129 C  CG    . HIS   B 96  ? 0.71266 0.57649 0.54865 0.08648  -0.04669 -0.06540 95  HIS   B CG    
2130 N  ND1   . HIS   B 96  ? 0.77219 0.62261 0.59186 0.09484  -0.05271 -0.06840 95  HIS   B ND1   
2131 C  CD2   . HIS   B 96  ? 0.67690 0.54146 0.50584 0.09160  -0.04056 -0.06468 95  HIS   B CD2   
2132 C  CE1   . HIS   B 96  ? 0.71490 0.55809 0.51762 0.10506  -0.05011 -0.06939 95  HIS   B CE1   
2133 N  NE2   . HIS   B 96  ? 0.77923 0.63109 0.58764 0.10319  -0.04260 -0.06700 95  HIS   B NE2   
2134 N  N     . TYR   B 97  ? 0.52529 0.41715 0.41323 0.05733  -0.04724 -0.05858 96  TYR   B N     
2135 C  CA    . TYR   B 97  ? 0.49828 0.40148 0.40469 0.04781  -0.04544 -0.05546 96  TYR   B CA    
2136 C  C     . TYR   B 97  ? 0.50144 0.40043 0.41475 0.04422  -0.05480 -0.05580 96  TYR   B C     
2137 O  O     . TYR   B 97  ? 0.52797 0.43064 0.45527 0.03787  -0.05864 -0.05412 96  TYR   B O     
2138 C  CB    . TYR   B 97  ? 0.54906 0.46376 0.45942 0.04579  -0.03452 -0.05234 96  TYR   B CB    
2139 C  CG    . TYR   B 97  ? 0.51907 0.44199 0.43181 0.04532  -0.02570 -0.05050 96  TYR   B CG    
2140 C  CD1   . TYR   B 97  ? 0.49757 0.42855 0.42347 0.03879  -0.02419 -0.04871 96  TYR   B CD1   
2141 C  CD2   . TYR   B 97  ? 0.44860 0.37104 0.35078 0.05168  -0.01902 -0.05020 96  TYR   B CD2   
2142 C  CE1   . TYR   B 97  ? 0.50488 0.44254 0.43287 0.03846  -0.01695 -0.04727 96  TYR   B CE1   
2143 C  CE2   . TYR   B 97  ? 0.46102 0.39077 0.36658 0.05113  -0.01153 -0.04821 96  TYR   B CE2   
2144 C  CZ    . TYR   B 97  ? 0.51589 0.45299 0.43427 0.04436  -0.01084 -0.04701 96  TYR   B CZ    
2145 O  OH    . TYR   B 97  ? 0.52156 0.46565 0.44377 0.04362  -0.00394 -0.04513 96  TYR   B OH    
2146 N  N     . ARG   B 98  ? 0.48258 0.37414 0.38685 0.04835  -0.05833 -0.05748 97  ARG   B N     
2147 C  CA    . ARG   B 98  ? 0.57327 0.45988 0.48407 0.04531  -0.06803 -0.05778 97  ARG   B CA    
2148 C  C     . ARG   B 98  ? 0.57157 0.44890 0.48503 0.04498  -0.07969 -0.05965 97  ARG   B C     
2149 O  O     . ARG   B 98  ? 0.58377 0.46330 0.51228 0.03872  -0.08550 -0.05755 97  ARG   B O     
2150 C  CB    . ARG   B 98  ? 0.58640 0.46449 0.48451 0.05106  -0.07075 -0.05996 97  ARG   B CB    
2151 C  CG    . ARG   B 98  ? 0.64894 0.52339 0.55525 0.04735  -0.07979 -0.05969 97  ARG   B CG    
2152 C  CD    . ARG   B 98  ? 0.65715 0.51505 0.55594 0.05176  -0.09395 -0.06360 97  ARG   B CD    
2153 N  NE    . ARG   B 98  ? 0.71725 0.57197 0.62529 0.04802  -0.10272 -0.06285 97  ARG   B NE    
2154 C  CZ    . ARG   B 98  ? 0.74202 0.58218 0.64556 0.05113  -0.11626 -0.06591 97  ARG   B CZ    
2155 N  NH1   . ARG   B 98  ? 0.71819 0.54469 0.60684 0.05850  -0.12309 -0.07032 97  ARG   B NH1   
2156 N  NH2   . ARG   B 98  ? 0.74935 0.58819 0.66358 0.04701  -0.12347 -0.06443 97  ARG   B NH2   
2157 N  N     . GLU   B 99  ? 0.57267 0.43919 0.47181 0.05204  -0.08354 -0.06331 98  GLU   B N     
2158 C  CA    . GLU   B 99  ? 0.60956 0.46593 0.51082 0.05204  -0.09584 -0.06538 98  GLU   B CA    
2159 C  C     . GLU   B 99  ? 0.57641 0.44180 0.49335 0.04520  -0.09410 -0.06253 98  GLU   B C     
2160 O  O     . GLU   B 99  ? 0.66758 0.52919 0.59482 0.04168  -0.10364 -0.06207 98  GLU   B O     
2161 C  CB    . GLU   B 99  ? 0.61721 0.45867 0.49767 0.06216  -0.10081 -0.07028 98  GLU   B CB    
2162 C  CG    . GLU   B 99  ? 0.65539 0.48444 0.51904 0.07010  -0.10556 -0.07357 98  GLU   B CG    
2163 C  CD    . GLU   B 99  ? 0.76510 0.58673 0.63602 0.06716  -0.11810 -0.07423 98  GLU   B CD    
2164 O  OE1   . GLU   B 99  ? 0.82705 0.64475 0.70917 0.06299  -0.12838 -0.07417 98  GLU   B OE1   
2165 O  OE2   . GLU   B 99  ? 0.80780 0.62752 0.67391 0.06903  -0.11786 -0.07453 98  GLU   B OE2   
2166 N  N     . GLN   B 100 ? 0.49627 0.37335 0.41569 0.04335  -0.08236 -0.06036 99  GLN   B N     
2167 C  CA    . GLN   B 100 ? 0.54952 0.43548 0.48350 0.03704  -0.08017 -0.05753 99  GLN   B CA    
2168 C  C     . GLN   B 100 ? 0.52890 0.42433 0.48186 0.02890  -0.08007 -0.05306 99  GLN   B C     
2169 O  O     . GLN   B 100 ? 0.49366 0.39022 0.45993 0.02428  -0.08558 -0.05093 99  GLN   B O     
2170 C  CB    . GLN   B 100 ? 0.47249 0.36747 0.40315 0.03782  -0.06810 -0.05663 99  GLN   B CB    
2171 C  CG    . GLN   B 100 ? 0.54030 0.44109 0.48014 0.03397  -0.06631 -0.05513 99  GLN   B CG    
2172 C  CD    . GLN   B 100 ? 0.62444 0.53409 0.56140 0.03473  -0.05451 -0.05411 99  GLN   B CD    
2173 O  OE1   . GLN   B 100 ? 0.63416 0.54511 0.56207 0.03858  -0.04791 -0.05439 99  GLN   B OE1   
2174 N  NE2   . GLN   B 100 ? 0.58731 0.50320 0.53285 0.03100  -0.05198 -0.05255 99  GLN   B NE2   
2175 N  N     . ILE   B 101 ? 0.56601 0.46812 0.52037 0.02747  -0.07382 -0.05129 100 ILE   B N     
2176 C  CA    . ILE   B 101 ? 0.49402 0.40472 0.46488 0.02070  -0.07329 -0.04692 100 ILE   B CA    
2177 C  C     . ILE   B 101 ? 0.53085 0.43343 0.50881 0.01925  -0.08574 -0.04662 100 ILE   B C     
2178 O  O     . ILE   B 101 ? 0.52287 0.42973 0.51715 0.01387  -0.08909 -0.04279 100 ILE   B O     
2179 C  CB    . ILE   B 101 ? 0.47182 0.38916 0.44017 0.02059  -0.06515 -0.04583 100 ILE   B CB    
2180 C  CG1   . ILE   B 101 ? 0.48837 0.41475 0.45347 0.02098  -0.05340 -0.04520 100 ILE   B CG1   
2181 C  CG2   . ILE   B 101 ? 0.51838 0.44280 0.50211 0.01460  -0.06567 -0.04153 100 ILE   B CG2   
2182 C  CD1   . ILE   B 101 ? 0.47231 0.40214 0.43062 0.02299  -0.04624 -0.04521 100 ILE   B CD1   
2183 N  N     . LYS   B 102 ? 0.59295 0.48334 0.55895 0.02439  -0.09300 -0.05040 101 LYS   B N     
2184 C  CA    . LYS   B 102 ? 0.57010 0.45092 0.54222 0.02353  -0.10637 -0.05057 101 LYS   B CA    
2185 C  C     . LYS   B 102 ? 0.59813 0.47541 0.57920 0.02149  -0.11422 -0.04990 101 LYS   B C     
2186 O  O     . LYS   B 102 ? 0.63718 0.51513 0.63485 0.01660  -0.12143 -0.04631 101 LYS   B O     
2187 C  CB    . LYS   B 102 ? 0.63216 0.49794 0.58624 0.03105  -0.11367 -0.05586 101 LYS   B CB    
2188 C  CG    . LYS   B 102 ? 0.63510 0.48639 0.59061 0.03244  -0.12984 -0.05795 101 LYS   B CG    
2189 C  CD    . LYS   B 102 ? 0.71242 0.54914 0.65150 0.03949  -0.13747 -0.06265 101 LYS   B CD    
2190 C  CE    . LYS   B 102 ? 0.64827 0.46844 0.58676 0.04189  -0.15479 -0.06554 101 LYS   B CE    
2191 N  NZ    . LYS   B 102 ? 0.77851 0.58413 0.70217 0.04851  -0.16319 -0.06988 101 LYS   B NZ    
2192 N  N     . ARG   B 103 ? 0.56284 0.43676 0.53397 0.02517  -0.11271 -0.05284 102 ARG   B N     
2193 C  CA    . ARG   B 103 ? 0.56888 0.43855 0.54713 0.02375  -0.12045 -0.05265 102 ARG   B CA    
2194 C  C     . ARG   B 103 ? 0.63280 0.51638 0.63128 0.01613  -0.11520 -0.04663 102 ARG   B C     
2195 O  O     . ARG   B 103 ? 0.67064 0.55352 0.68465 0.01206  -0.12313 -0.04341 102 ARG   B O     
2196 C  CB    . ARG   B 103 ? 0.63119 0.49429 0.59286 0.02995  -0.11915 -0.05724 102 ARG   B CB    
2197 C  CG    . ARG   B 103 ? 0.66537 0.52685 0.63529 0.02780  -0.12466 -0.05659 102 ARG   B CG    
2198 C  CD    . ARG   B 103 ? 0.67781 0.53577 0.63290 0.03320  -0.12090 -0.06030 102 ARG   B CD    
2199 N  NE    . ARG   B 103 ? 0.67819 0.55046 0.63808 0.02996  -0.10769 -0.05752 102 ARG   B NE    
2200 C  CZ    . ARG   B 103 ? 0.69185 0.56735 0.63894 0.03402  -0.09760 -0.05917 102 ARG   B CZ    
2201 N  NH1   . ARG   B 103 ? 0.75381 0.61987 0.68198 0.04192  -0.09810 -0.06324 102 ARG   B NH1   
2202 N  NH2   . ARG   B 103 ? 0.65067 0.53894 0.60428 0.03044  -0.08687 -0.05638 102 ARG   B NH2   
2203 N  N     . VAL   B 104 ? 0.61321 0.50925 0.61192 0.01448  -0.10202 -0.04478 103 VAL   B N     
2204 C  CA    . VAL   B 104 ? 0.60046 0.50896 0.61568 0.00850  -0.09643 -0.03947 103 VAL   B CA    
2205 C  C     . VAL   B 104 ? 0.55847 0.47331 0.59160 0.00309  -0.09817 -0.03371 103 VAL   B C     
2206 O  O     . VAL   B 104 ? 0.59873 0.51848 0.64838 -0.00126 -0.10028 -0.02884 103 VAL   B O     
2207 C  CB    . VAL   B 104 ? 0.58237 0.50142 0.59242 0.00863  -0.08269 -0.03926 103 VAL   B CB    
2208 C  CG1   . VAL   B 104 ? 0.53964 0.47183 0.56612 0.00284  -0.07639 -0.03339 103 VAL   B CG1   
2209 C  CG2   . VAL   B 104 ? 0.61936 0.53447 0.61792 0.01251  -0.08104 -0.04300 103 VAL   B CG2   
2210 N  N     . LYS   B 105 ? 0.52603 0.44106 0.55655 0.00350  -0.09709 -0.03373 104 LYS   B N     
2211 C  CA    . LYS   B 105 ? 0.56433 0.48608 0.61122 -0.00127 -0.09759 -0.02799 104 LYS   B CA    
2212 C  C     . LYS   B 105 ? 0.56516 0.47686 0.61870 -0.00165 -0.11122 -0.02759 104 LYS   B C     
2213 O  O     . LYS   B 105 ? 0.57070 0.48698 0.63844 -0.00535 -0.11276 -0.02256 104 LYS   B O     
2214 C  CB    . LYS   B 105 ? 0.47010 0.39880 0.51196 -0.00111 -0.08832 -0.02769 104 LYS   B CB    
2215 C  CG    . LYS   B 105 ? 0.49508 0.43355 0.53169 -0.00092 -0.07553 -0.02778 104 LYS   B CG    
2216 C  CD    . LYS   B 105 ? 0.50442 0.45045 0.53970 -0.00161 -0.06728 -0.02643 104 LYS   B CD    
2217 C  CE    . LYS   B 105 ? 0.42337 0.37845 0.47614 -0.00640 -0.06576 -0.01977 104 LYS   B CE    
2218 N  NZ    . LYS   B 105 ? 0.39359 0.35811 0.45554 -0.00888 -0.05955 -0.01581 104 LYS   B NZ    
2219 N  N     . ASP   B 106 ? 0.62537 0.52310 0.66868 0.00246  -0.12129 -0.03273 105 ASP   B N     
2220 C  CA    . ASP   B 106 ? 0.56758 0.45369 0.61670 0.00255  -0.13615 -0.03295 105 ASP   B CA    
2221 C  C     . ASP   B 106 ? 0.60414 0.49010 0.65584 0.00174  -0.13773 -0.03164 105 ASP   B C     
2222 O  O     . ASP   B 106 ? 0.64326 0.53110 0.71282 -0.00252 -0.14360 -0.02641 105 ASP   B O     
2223 C  CB    . ASP   B 106 ? 0.63287 0.52193 0.70374 -0.00255 -0.14236 -0.02710 105 ASP   B CB    
2224 C  CG    . ASP   B 106 ? 0.73891 0.61428 0.81601 -0.00219 -0.15943 -0.02771 105 ASP   B CG    
2225 O  OD1   . ASP   B 106 ? 0.70071 0.56238 0.76236 0.00293  -0.16724 -0.03382 105 ASP   B OD1   
2226 O  OD2   . ASP   B 106 ? 0.82637 0.70454 0.92431 -0.00681 -0.16525 -0.02174 105 ASP   B OD2   
2227 N  N     . SER   B 107 ? 0.59600 0.48033 0.63047 0.00587  -0.13198 -0.03590 106 SER   B N     
2228 C  CA    . SER   B 107 ? 0.62023 0.50457 0.65615 0.00528  -0.13291 -0.03491 106 SER   B CA    
2229 C  C     . SER   B 107 ? 0.64337 0.51925 0.65628 0.01205  -0.13153 -0.04144 106 SER   B C     
2230 O  O     . SER   B 107 ? 0.61422 0.49180 0.61287 0.01572  -0.12306 -0.04457 106 SER   B O     
2231 C  CB    . SER   B 107 ? 0.59361 0.49443 0.64196 0.00018  -0.12128 -0.02885 106 SER   B CB    
2232 O  OG    . SER   B 107 ? 0.58118 0.48185 0.63048 -0.00025 -0.12216 -0.02801 106 SER   B OG    
2233 N  N     . GLU   B 108 ? 0.63829 0.50511 0.64820 0.01387  -0.13988 -0.04307 107 GLU   B N     
2234 C  CA    . GLU   B 108 ? 0.65824 0.51798 0.64756 0.02027  -0.13797 -0.04830 107 GLU   B CA    
2235 C  C     . GLU   B 108 ? 0.66439 0.53462 0.65624 0.01789  -0.12839 -0.04564 107 GLU   B C     
2236 O  O     . GLU   B 108 ? 0.74207 0.60724 0.71894 0.02269  -0.12684 -0.04914 107 GLU   B O     
2237 C  CB    . GLU   B 108 ? 0.65964 0.50117 0.64082 0.02501  -0.15338 -0.05261 107 GLU   B CB    
2238 C  CG    . GLU   B 108 ? 0.66231 0.49110 0.63368 0.02989  -0.16197 -0.05703 107 GLU   B CG    
2239 C  CD    . GLU   B 108 ? 0.68063 0.49288 0.65415 0.03158  -0.18039 -0.05915 107 GLU   B CD    
2240 O  OE1   . GLU   B 108 ? 0.75785 0.56613 0.73529 0.03079  -0.18656 -0.05854 107 GLU   B OE1   
2241 O  OE2   . GLU   B 108 ? 0.67618 0.47921 0.64787 0.03364  -0.18908 -0.06139 107 GLU   B OE2   
2242 N  N     . ASP   B 109 ? 0.54974 0.43440 0.55956 0.01107  -0.12160 -0.03944 108 ASP   B N     
2243 C  CA    . ASP   B 109 ? 0.59237 0.48688 0.60694 0.00832  -0.11375 -0.03633 108 ASP   B CA    
2244 C  C     . ASP   B 109 ? 0.56409 0.47386 0.58276 0.00540  -0.09960 -0.03316 108 ASP   B C     
2245 O  O     . ASP   B 109 ? 0.57279 0.49279 0.60142 0.00156  -0.09363 -0.02880 108 ASP   B O     
2246 C  CB    . ASP   B 109 ? 0.57530 0.47146 0.60892 0.00327  -0.12077 -0.03115 108 ASP   B CB    
2247 C  CG    . ASP   B 109 ? 0.75438 0.63520 0.78429 0.00605  -0.13521 -0.03426 108 ASP   B CG    
2248 O  OD1   . ASP   B 109 ? 0.83464 0.70694 0.84652 0.01157  -0.13613 -0.03959 108 ASP   B OD1   
2249 O  OD2   . ASP   B 109 ? 0.78230 0.65929 0.82746 0.00299  -0.14587 -0.03120 108 ASP   B OD2   
2250 N  N     . VAL   B 110 ? 0.60231 0.51329 0.61319 0.00745  -0.09447 -0.03530 109 VAL   B N     
2251 C  CA    . VAL   B 110 ? 0.49523 0.41974 0.51034 0.00479  -0.08213 -0.03245 109 VAL   B CA    
2252 C  C     . VAL   B 110 ? 0.52468 0.45455 0.53168 0.00607  -0.07297 -0.03316 109 VAL   B C     
2253 O  O     . VAL   B 110 ? 0.51352 0.43664 0.50481 0.01118  -0.07264 -0.03753 109 VAL   B O     
2254 C  CB    . VAL   B 110 ? 0.54679 0.47014 0.55472 0.00707  -0.07960 -0.03495 109 VAL   B CB    
2255 C  CG1   . VAL   B 110 ? 0.47978 0.41640 0.49273 0.00430  -0.06784 -0.03204 109 VAL   B CG1   
2256 C  CG2   . VAL   B 110 ? 0.58009 0.49661 0.59522 0.00619  -0.08989 -0.03467 109 VAL   B CG2   
2257 N  N     . PRO   B 111 ? 0.44683 0.38835 0.46356 0.00211  -0.06549 -0.02886 110 PRO   B N     
2258 C  CA    . PRO   B 111 ? 0.44735 0.39368 0.45649 0.00335  -0.05715 -0.02965 110 PRO   B CA    
2259 C  C     . PRO   B 111 ? 0.42763 0.37372 0.42325 0.00725  -0.05061 -0.03311 110 PRO   B C     
2260 O  O     . PRO   B 111 ? 0.44226 0.39285 0.43974 0.00648  -0.04640 -0.03253 110 PRO   B O     
2261 C  CB    . PRO   B 111 ? 0.41635 0.37508 0.43881 -0.00137 -0.05054 -0.02431 110 PRO   B CB    
2262 C  CG    . PRO   B 111 ? 0.48239 0.44108 0.52031 -0.00485 -0.05757 -0.02014 110 PRO   B CG    
2263 C  CD    . PRO   B 111 ? 0.42206 0.37207 0.45705 -0.00313 -0.06496 -0.02282 110 PRO   B CD    
2264 N  N     . MET   B 112 ? 0.41843 0.35885 0.40052 0.01181  -0.05003 -0.03646 111 MET   B N     
2265 C  CA    . MET   B 112 ? 0.38054 0.32100 0.35021 0.01609  -0.04331 -0.03890 111 MET   B CA    
2266 C  C     . MET   B 112 ? 0.48059 0.42160 0.44230 0.01864  -0.03880 -0.03959 111 MET   B C     
2267 O  O     . MET   B 112 ? 0.48585 0.42289 0.44696 0.01886  -0.04323 -0.03988 111 MET   B O     
2268 C  CB    . MET   B 112 ? 0.45534 0.38491 0.41314 0.02157  -0.04845 -0.04278 111 MET   B CB    
2269 C  CG    . MET   B 112 ? 0.49249 0.42005 0.45721 0.01953  -0.05394 -0.04251 111 MET   B CG    
2270 S  SD    . MET   B 112 ? 0.67956 0.59323 0.62800 0.02699  -0.06004 -0.04753 111 MET   B SD    
2271 C  CE    . MET   B 112 ? 0.57823 0.48984 0.50946 0.03387  -0.05298 -0.04962 111 MET   B CE    
2272 N  N     . VAL   B 113 ? 0.39850 0.34443 0.35474 0.02057  -0.03018 -0.03960 112 VAL   B N     
2273 C  CA    . VAL   B 113 ? 0.40424 0.34999 0.35133 0.02425  -0.02535 -0.04024 112 VAL   B CA    
2274 C  C     . VAL   B 113 ? 0.47824 0.42062 0.41349 0.03019  -0.02158 -0.04195 112 VAL   B C     
2275 O  O     . VAL   B 113 ? 0.42435 0.37093 0.36231 0.02934  -0.01786 -0.04125 112 VAL   B O     
2276 C  CB    . VAL   B 113 ? 0.36559 0.32242 0.32037 0.02035  -0.01767 -0.03724 112 VAL   B CB    
2277 C  CG1   . VAL   B 113 ? 0.43179 0.38872 0.37768 0.02434  -0.01231 -0.03753 112 VAL   B CG1   
2278 C  CG2   . VAL   B 113 ? 0.42694 0.38666 0.39210 0.01552  -0.02099 -0.03529 112 VAL   B CG2   
2279 N  N     . LEU   B 114 ? 0.44225 0.37675 0.36416 0.03665  -0.02259 -0.04397 113 LEU   B N     
2280 C  CA    . LEU   B 114 ? 0.41845 0.35054 0.32884 0.04322  -0.01758 -0.04461 113 LEU   B CA    
2281 C  C     . LEU   B 114 ? 0.47293 0.41408 0.38512 0.04308  -0.00773 -0.04168 113 LEU   B C     
2282 O  O     . LEU   B 114 ? 0.46512 0.40769 0.37728 0.04275  -0.00652 -0.04090 113 LEU   B O     
2283 C  CB    . LEU   B 114 ? 0.41697 0.33580 0.31107 0.05141  -0.02300 -0.04778 113 LEU   B CB    
2284 C  CG    . LEU   B 114 ? 0.45769 0.37180 0.33761 0.05997  -0.01878 -0.04839 113 LEU   B CG    
2285 C  CD1   . LEU   B 114 ? 0.43123 0.34285 0.31061 0.06062  -0.02088 -0.04958 113 LEU   B CD1   
2286 C  CD2   . LEU   B 114 ? 0.48609 0.38699 0.34925 0.06845  -0.02406 -0.05130 113 LEU   B CD2   
2287 N  N     . VAL   B 115 ? 0.44100 0.38807 0.35525 0.04334  -0.00106 -0.03992 114 VAL   B N     
2288 C  CA    . VAL   B 115 ? 0.47074 0.42700 0.38962 0.04232  0.00763  -0.03666 114 VAL   B CA    
2289 C  C     . VAL   B 115 ? 0.49537 0.45002 0.40500 0.04947  0.01330  -0.03550 114 VAL   B C     
2290 O  O     . VAL   B 115 ? 0.43142 0.38594 0.34007 0.05107  0.01475  -0.03542 114 VAL   B O     
2291 C  CB    . VAL   B 115 ? 0.47732 0.44346 0.40993 0.03547  0.01072  -0.03470 114 VAL   B CB    
2292 C  CG1   . VAL   B 115 ? 0.45388 0.42809 0.39068 0.03520  0.01878  -0.03148 114 VAL   B CG1   
2293 C  CG2   . VAL   B 115 ? 0.43593 0.40453 0.37793 0.02908  0.00629  -0.03490 114 VAL   B CG2   
2294 N  N     . GLY   B 116 ? 0.44285 0.39689 0.34635 0.05388  0.01706  -0.03405 115 GLY   B N     
2295 C  CA    . GLY   B 116 ? 0.53289 0.48727 0.42967 0.06071  0.02393  -0.03148 115 GLY   B CA    
2296 C  C     . GLY   B 116 ? 0.50473 0.47043 0.41294 0.05727  0.03174  -0.02705 115 GLY   B C     
2297 O  O     . GLY   B 116 ? 0.55475 0.52445 0.46686 0.05544  0.03388  -0.02539 115 GLY   B O     
2298 N  N     . ASN   B 117 ? 0.42135 0.39194 0.33531 0.05635  0.03554  -0.02513 116 ASN   B N     
2299 C  CA    . ASN   B 117 ? 0.45201 0.43287 0.37856 0.05232  0.04148  -0.02117 116 ASN   B CA    
2300 C  C     . ASN   B 117 ? 0.51976 0.50290 0.44405 0.05866  0.04906  -0.01651 116 ASN   B C     
2301 O  O     . ASN   B 117 ? 0.46238 0.43929 0.37469 0.06656  0.05027  -0.01636 116 ASN   B O     
2302 C  CB    . ASN   B 117 ? 0.44791 0.43310 0.38405 0.04664  0.04037  -0.02175 116 ASN   B CB    
2303 C  CG    . ASN   B 117 ? 0.44453 0.43921 0.39403 0.04176  0.04457  -0.01845 116 ASN   B CG    
2304 O  OD1   . ASN   B 117 ? 0.46200 0.46017 0.41635 0.03892  0.04510  -0.01748 116 ASN   B OD1   
2305 N  ND2   . ASN   B 117 ? 0.35429 0.35272 0.30972 0.04094  0.04716  -0.01677 116 ASN   B ND2   
2306 N  N     . LYS   B 118 ? 0.45737 0.44940 0.39374 0.05537  0.05400  -0.01239 117 LYS   B N     
2307 C  CA    . LYS   B 118 ? 0.49639 0.49273 0.43514 0.06019  0.06164  -0.00651 117 LYS   B CA    
2308 C  C     . LYS   B 118 ? 0.44016 0.43387 0.37085 0.06597  0.06422  -0.00468 117 LYS   B C     
2309 O  O     . LYS   B 118 ? 0.46465 0.45781 0.39015 0.07359  0.06994  -0.00053 117 LYS   B O     
2310 C  CB    . LYS   B 118 ? 0.48119 0.47591 0.41577 0.06575  0.06486  -0.00471 117 LYS   B CB    
2311 C  CG    . LYS   B 118 ? 0.47648 0.47172 0.41583 0.06094  0.06135  -0.00751 117 LYS   B CG    
2312 C  CD    . LYS   B 118 ? 0.50756 0.50549 0.44988 0.06410  0.06612  -0.00391 117 LYS   B CD    
2313 C  CE    . LYS   B 118 ? 0.49390 0.49048 0.43796 0.06010  0.06178  -0.00765 117 LYS   B CE    
2314 N  NZ    . LYS   B 118 ? 0.41749 0.41690 0.36517 0.06272  0.06621  -0.00423 117 LYS   B NZ    
2315 N  N     A CYS   B 119 ? 0.50366 0.49586 0.43334 0.06272  0.06030  -0.00740 118 CYS   B N     
2316 N  N     B CYS   B 119 ? 0.50373 0.49587 0.43327 0.06281  0.06032  -0.00740 118 CYS   B N     
2317 C  CA    A CYS   B 119 ? 0.51031 0.49978 0.43226 0.06788  0.06229  -0.00601 118 CYS   B CA    
2318 C  CA    B CYS   B 119 ? 0.51062 0.49986 0.43200 0.06841  0.06252  -0.00588 118 CYS   B CA    
2319 C  C     A CYS   B 119 ? 0.54712 0.54459 0.47830 0.06869  0.06952  0.00052  118 CYS   B C     
2320 C  C     B CYS   B 119 ? 0.54742 0.54476 0.47825 0.06909  0.06975  0.00067  118 CYS   B C     
2321 O  O     A CYS   B 119 ? 0.57057 0.56645 0.49558 0.07404  0.07257  0.00282  118 CYS   B O     
2322 O  O     B CYS   B 119 ? 0.57048 0.56619 0.49493 0.07479  0.07304  0.00314  118 CYS   B O     
2323 C  CB    A CYS   B 119 ? 0.51208 0.49829 0.43190 0.06367  0.05602  -0.01043 118 CYS   B CB    
2324 C  CB    B CYS   B 119 ? 0.51286 0.49824 0.43102 0.06478  0.05624  -0.01038 118 CYS   B CB    
2325 S  SG    A CYS   B 119 ? 0.49944 0.47326 0.40425 0.06663  0.04763  -0.01692 118 CYS   B SG    
2326 S  SG    B CYS   B 119 ? 0.61192 0.60615 0.54612 0.05487  0.05547  -0.00975 118 CYS   B SG    
2327 N  N     . ASP   B 120 ? 0.48204 0.48766 0.42798 0.06376  0.07201  0.00372  119 ASP   B N     
2328 C  CA    . ASP   B 120 ? 0.49103 0.50410 0.44734 0.06489  0.07859  0.01072  119 ASP   B CA    
2329 C  C     . ASP   B 120 ? 0.54713 0.55988 0.49877 0.07390  0.08545  0.01615  119 ASP   B C     
2330 O  O     . ASP   B 120 ? 0.59119 0.60857 0.54799 0.07738  0.09154  0.02265  119 ASP   B O     
2331 C  CB    . ASP   B 120 ? 0.48592 0.50674 0.45953 0.05736  0.07823  0.01249  119 ASP   B CB    
2332 C  CG    . ASP   B 120 ? 0.50002 0.52058 0.47545 0.05626  0.07716  0.01123  119 ASP   B CG    
2333 O  OD1   . ASP   B 120 ? 0.52068 0.53620 0.48917 0.05422  0.07186  0.00536  119 ASP   B OD1   
2334 O  OD2   . ASP   B 120 ? 0.54723 0.57277 0.53190 0.05727  0.08144  0.01636  119 ASP   B OD2   
2335 N  N     . LEU   B 121 ? 0.51983 0.52724 0.46198 0.07806  0.08470  0.01401  120 LEU   B N     
2336 C  CA    . LEU   B 121 ? 0.56319 0.57110 0.50238 0.08639  0.09153  0.01961  120 LEU   B CA    
2337 C  C     . LEU   B 121 ? 0.53188 0.53368 0.45521 0.09702  0.09513  0.02135  120 LEU   B C     
2338 O  O     . LEU   B 121 ? 0.54969 0.54403 0.46061 0.09839  0.09047  0.01622  120 LEU   B O     
2339 C  CB    . LEU   B 121 ? 0.43591 0.44023 0.37068 0.08707  0.08931  0.01662  120 LEU   B CB    
2340 C  CG    . LEU   B 121 ? 0.57245 0.58386 0.52377 0.07878  0.08819  0.01721  120 LEU   B CG    
2341 C  CD1   . LEU   B 121 ? 0.50447 0.51300 0.45164 0.08083  0.08761  0.01568  120 LEU   B CD1   
2342 C  CD2   . LEU   B 121 ? 0.54644 0.56739 0.51415 0.07776  0.09429  0.02522  120 LEU   B CD2   
2343 N  N     . PRO   B 122 ? 0.59836 0.60312 0.52209 0.10496  0.10342  0.02892  121 PRO   B N     
2344 C  CA    . PRO   B 122 ? 0.50839 0.50710 0.41595 0.11650  0.10766  0.03125  121 PRO   B CA    
2345 C  C     . PRO   B 122 ? 0.62782 0.61571 0.51573 0.12476  0.10557  0.02715  121 PRO   B C     
2346 O  O     . PRO   B 122 ? 0.56553 0.55190 0.45378 0.12237  0.10252  0.02410  121 PRO   B O     
2347 C  CB    . PRO   B 122 ? 0.54214 0.54967 0.46063 0.12146  0.11796  0.04217  121 PRO   B CB    
2348 C  CG    . PRO   B 122 ? 0.49866 0.51387 0.43446 0.11484  0.11849  0.04458  121 PRO   B CG    
2349 C  CD    . PRO   B 122 ? 0.51267 0.52773 0.45458 0.10308  0.10952  0.03678  121 PRO   B CD    
2350 N  N     . SER   B 123 ? 0.56598 0.54565 0.43596 0.13489  0.10684  0.02694  122 SER   B N     
2351 C  CA    . SER   B 123 ? 0.64047 0.60932 0.48993 0.14614  0.10669  0.02502  122 SER   B CA    
2352 C  C     . SER   B 123 ? 0.60151 0.56178 0.44338 0.14182  0.09635  0.01555  122 SER   B C     
2353 O  O     . SER   B 123 ? 0.66600 0.62160 0.50039 0.14624  0.09579  0.01431  122 SER   B O     
2354 C  CB    . SER   B 123 ? 0.66732 0.64114 0.52000 0.15339  0.11607  0.03321  122 SER   B CB    
2355 O  OG    . SER   B 123 ? 0.67570 0.65608 0.53335 0.15935  0.12570  0.04256  122 SER   B OG    
2356 N  N     . ARG   B 124 ? 0.57484 0.53304 0.41898 0.13338  0.08815  0.00919  123 ARG   B N     
2357 C  CA    . ARG   B 124 ? 0.60029 0.55071 0.43894 0.12889  0.07799  0.00080  123 ARG   B CA    
2358 C  C     . ARG   B 124 ? 0.64552 0.58171 0.46124 0.14023  0.07459  -0.00283 123 ARG   B C     
2359 O  O     . ARG   B 124 ? 0.68159 0.61081 0.48252 0.14984  0.07616  -0.00204 123 ARG   B O     
2360 C  CB    . ARG   B 124 ? 0.65534 0.60517 0.49865 0.11997  0.07044  -0.00435 123 ARG   B CB    
2361 C  CG    . ARG   B 124 ? 0.59699 0.54003 0.42832 0.12520  0.06878  -0.00568 123 ARG   B CG    
2362 C  CD    . ARG   B 124 ? 0.62679 0.57306 0.46834 0.11458  0.06310  -0.00905 123 ARG   B CD    
2363 N  NE    . ARG   B 124 ? 0.71536 0.65364 0.55271 0.11024  0.05233  -0.01651 123 ARG   B NE    
2364 C  CZ    . ARG   B 124 ? 0.66505 0.60533 0.51100 0.10113  0.04654  -0.01971 123 ARG   B CZ    
2365 N  NH1   . ARG   B 124 ? 0.67681 0.62650 0.53537 0.09508  0.05009  -0.01677 123 ARG   B NH1   
2366 N  NH2   . ARG   B 124 ? 0.67807 0.61071 0.52038 0.09818  0.03687  -0.02565 123 ARG   B NH2   
2367 N  N     . THR   B 125 ? 0.63051 0.56214 0.44302 0.13953  0.06992  -0.00667 124 THR   B N     
2368 C  CA    . THR   B 125 ? 0.65711 0.57464 0.44825 0.15010  0.06577  -0.01048 124 THR   B CA    
2369 C  C     . THR   B 125 ? 0.70324 0.60929 0.48584 0.14726  0.05302  -0.01917 124 THR   B C     
2370 O  O     . THR   B 125 ? 0.70683 0.59899 0.47020 0.15634  0.04760  -0.02319 124 THR   B O     
2371 C  CB    . THR   B 125 ? 0.63811 0.55694 0.43066 0.15153  0.06795  -0.00934 124 THR   B CB    
2372 O  OG1   . THR   B 125 ? 0.67976 0.60457 0.48832 0.13869  0.06294  -0.01246 124 THR   B OG1   
2373 C  CG2   . THR   B 125 ? 0.61286 0.54225 0.41339 0.15570  0.08057  0.00001  124 THR   B CG2   
2374 N  N     . VAL   B 126 ? 0.59628 0.50756 0.39299 0.13521  0.04795  -0.02183 125 VAL   B N     
2375 C  CA    . VAL   B 126 ? 0.61156 0.51383 0.40420 0.13116  0.03611  -0.02896 125 VAL   B CA    
2376 C  C     . VAL   B 126 ? 0.65393 0.55790 0.44889 0.12871  0.03577  -0.02864 125 VAL   B C     
2377 O  O     . VAL   B 126 ? 0.60021 0.51578 0.41198 0.11959  0.03901  -0.02611 125 VAL   B O     
2378 C  CB    . VAL   B 126 ? 0.61365 0.52081 0.42138 0.11935  0.03058  -0.03183 125 VAL   B CB    
2379 C  CG1   . VAL   B 126 ? 0.61825 0.51500 0.42135 0.11652  0.01797  -0.03853 125 VAL   B CG1   
2380 C  CG2   . VAL   B 126 ? 0.60454 0.51320 0.41310 0.12095  0.03328  -0.03075 125 VAL   B CG2   
2381 N  N     . ASP   B 127 ? 0.70952 0.60165 0.48721 0.13725  0.03186  -0.03118 126 ASP   B N     
2382 C  CA    . ASP   B 127 ? 0.68726 0.58159 0.46754 0.13498  0.03216  -0.03052 126 ASP   B CA    
2383 C  C     . ASP   B 127 ? 0.71223 0.60496 0.50076 0.12484  0.02184  -0.03571 126 ASP   B C     
2384 O  O     . ASP   B 127 ? 0.68377 0.57198 0.47398 0.12095  0.01386  -0.03990 126 ASP   B O     
2385 C  CB    . ASP   B 127 ? 0.78211 0.66535 0.54144 0.14815  0.03291  -0.03051 126 ASP   B CB    
2386 C  CG    . ASP   B 127 ? 0.75563 0.62120 0.49727 0.15381  0.02074  -0.03774 126 ASP   B CG    
2387 O  OD1   . ASP   B 127 ? 0.85056 0.71241 0.59579 0.14744  0.01160  -0.04215 126 ASP   B OD1   
2388 O  OD2   . ASP   B 127 ? 0.86056 0.71564 0.58463 0.16509  0.02021  -0.03873 126 ASP   B OD2   
2389 N  N     . THR   B 128 ? 0.73157 0.62858 0.52619 0.12056  0.02236  -0.03487 127 THR   B N     
2390 C  CA    . THR   B 128 ? 0.73607 0.63393 0.54121 0.11041  0.01416  -0.03843 127 THR   B CA    
2391 C  C     . THR   B 128 ? 0.77737 0.65997 0.57047 0.11355  0.00177  -0.04466 127 THR   B C     
2392 O  O     . THR   B 128 ? 0.79168 0.67361 0.59379 0.10573  -0.00629 -0.04770 127 THR   B O     
2393 C  CB    . THR   B 128 ? 0.73403 0.63882 0.54633 0.10654  0.01763  -0.03607 127 THR   B CB    
2394 O  OG1   . THR   B 128 ? 0.75822 0.67654 0.58234 0.10375  0.02830  -0.03019 127 THR   B OG1   
2395 C  CG2   . THR   B 128 ? 0.68499 0.59195 0.50942 0.09598  0.01015  -0.03891 127 THR   B CG2   
2396 N  N     . LYS   B 129 ? 0.73670 0.60655 0.50954 0.12535  -0.00019 -0.04637 128 LYS   B N     
2397 C  CA    . LYS   B 129 ? 0.74594 0.59982 0.50679 0.12888  -0.01316 -0.05252 128 LYS   B CA    
2398 C  C     . LYS   B 129 ? 0.72375 0.57167 0.48258 0.12926  -0.01914 -0.05549 128 LYS   B C     
2399 O  O     . LYS   B 129 ? 0.77798 0.61735 0.53741 0.12624  -0.03098 -0.06008 128 LYS   B O     
2400 C  CB    . LYS   B 129 ? 0.76742 0.60808 0.50554 0.14233  -0.01407 -0.05382 128 LYS   B CB    
2401 C  CG    . LYS   B 129 ? 0.76943 0.59178 0.49392 0.14690  -0.02864 -0.06052 128 LYS   B CG    
2402 C  CD    . LYS   B 129 ? 0.81294 0.62040 0.51160 0.16240  -0.02944 -0.06205 128 LYS   B CD    
2403 C  CE    . LYS   B 129 ? 0.80178 0.58952 0.48656 0.16725  -0.04540 -0.06919 128 LYS   B CE    
2404 N  NZ    . LYS   B 129 ? 0.89372 0.68129 0.59231 0.15651  -0.05577 -0.07204 128 LYS   B NZ    
2405 N  N     . GLN   B 130 ? 0.73217 0.58423 0.48890 0.13317  -0.01134 -0.05267 129 GLN   B N     
2406 C  CA    . GLN   B 130 ? 0.73383 0.58288 0.49184 0.13181  -0.01589 -0.05492 129 GLN   B CA    
2407 C  C     . GLN   B 130 ? 0.70170 0.55916 0.48074 0.11793  -0.02037 -0.05565 129 GLN   B C     
2408 O  O     . GLN   B 130 ? 0.72635 0.57614 0.50664 0.11500  -0.03134 -0.05976 129 GLN   B O     
2409 C  CB    . GLN   B 130 ? 0.69212 0.54797 0.44902 0.13618  -0.00500 -0.05060 129 GLN   B CB    
2410 C  CG    . GLN   B 130 ? 0.81116 0.65664 0.54560 0.15144  -0.00166 -0.05005 129 GLN   B CG    
2411 C  CD    . GLN   B 130 ? 0.82670 0.68014 0.56322 0.15451  0.00888  -0.04520 129 GLN   B CD    
2412 O  OE1   . GLN   B 130 ? 0.84061 0.70408 0.58134 0.15640  0.02044  -0.03903 129 GLN   B OE1   
2413 N  NE2   . GLN   B 130 ? 0.79602 0.64524 0.53073 0.15476  0.00474  -0.04768 129 GLN   B NE2   
2414 N  N     . ALA   B 131 ? 0.73331 0.60641 0.52922 0.10958  -0.01207 -0.05135 130 ALA   B N     
2415 C  CA    . ALA   B 131 ? 0.62329 0.50516 0.43863 0.09726  -0.01488 -0.05135 130 ALA   B CA    
2416 C  C     . ALA   B 131 ? 0.67233 0.54982 0.49215 0.09221  -0.02443 -0.05412 130 ALA   B C     
2417 O  O     . ALA   B 131 ? 0.64693 0.52358 0.47614 0.08574  -0.03203 -0.05596 130 ALA   B O     
2418 C  CB    . ALA   B 131 ? 0.65633 0.55455 0.48670 0.09078  -0.00414 -0.04630 130 ALA   B CB    
2419 N  N     . GLN   B 132 ? 0.71385 0.58828 0.52731 0.09538  -0.02437 -0.05416 131 GLN   B N     
2420 C  CA    . GLN   B 132 ? 0.61918 0.48942 0.43732 0.09071  -0.03351 -0.05649 131 GLN   B CA    
2421 C  C     . GLN   B 132 ? 0.71637 0.57063 0.52496 0.09468  -0.04677 -0.06150 131 GLN   B C     
2422 O  O     . GLN   B 132 ? 0.71342 0.56607 0.53244 0.08798  -0.05571 -0.06295 131 GLN   B O     
2423 C  CB    . GLN   B 132 ? 0.71124 0.58133 0.52394 0.09365  -0.03048 -0.05551 131 GLN   B CB    
2424 C  CG    . GLN   B 132 ? 0.66892 0.55476 0.49569 0.08682  -0.02057 -0.05092 131 GLN   B CG    
2425 C  CD    . GLN   B 132 ? 0.83242 0.71811 0.65265 0.09079  -0.01659 -0.04959 131 GLN   B CD    
2426 O  OE1   . GLN   B 132 ? 0.81369 0.68865 0.61655 0.10068  -0.01800 -0.05118 131 GLN   B OE1   
2427 N  NE2   . GLN   B 132 ? 0.83244 0.72983 0.66607 0.08351  -0.01150 -0.04660 131 GLN   B NE2   
2428 N  N     . ASP   B 133 ? 0.65029 0.49231 0.43929 0.10590  -0.04850 -0.06391 132 ASP   B N     
2429 C  CA    . ASP   B 133 ? 0.68833 0.51399 0.46767 0.11013  -0.06205 -0.06900 132 ASP   B CA    
2430 C  C     . ASP   B 133 ? 0.69071 0.51885 0.48267 0.10313  -0.06691 -0.06955 132 ASP   B C     
2431 O  O     . ASP   B 133 ? 0.75580 0.57686 0.55333 0.09940  -0.07890 -0.07215 132 ASP   B O     
2432 C  CB    . ASP   B 133 ? 0.62606 0.43807 0.38076 0.12440  -0.06226 -0.07134 132 ASP   B CB    
2433 C  CG    . ASP   B 133 ? 0.77705 0.58093 0.51651 0.13266  -0.06249 -0.07226 132 ASP   B CG    
2434 O  OD1   . ASP   B 133 ? 0.76735 0.57637 0.51607 0.12671  -0.06276 -0.07125 132 ASP   B OD1   
2435 O  OD2   . ASP   B 133 ? 0.81927 0.61156 0.53716 0.14545  -0.06219 -0.07385 132 ASP   B OD2   
2436 N  N     . LEU   B 134 ? 0.62891 0.46715 0.42630 0.10124  -0.05787 -0.06680 133 LEU   B N     
2437 C  CA    . LEU   B 134 ? 0.69449 0.53592 0.50396 0.09468  -0.06150 -0.06700 133 LEU   B CA    
2438 C  C     . LEU   B 134 ? 0.62052 0.47048 0.45119 0.08273  -0.06502 -0.06540 133 LEU   B C     
2439 O  O     . LEU   B 134 ? 0.63033 0.47578 0.46864 0.07862  -0.07488 -0.06695 133 LEU   B O     
2440 C  CB    . LEU   B 134 ? 0.61780 0.46992 0.43027 0.09440  -0.05007 -0.06386 133 LEU   B CB    
2441 C  CG    . LEU   B 134 ? 0.64658 0.50037 0.46827 0.08945  -0.05367 -0.06443 133 LEU   B CG    
2442 C  CD1   . LEU   B 134 ? 0.67349 0.51041 0.48068 0.09699  -0.06444 -0.06912 133 LEU   B CD1   
2443 C  CD2   . LEU   B 134 ? 0.64470 0.51068 0.47172 0.08795  -0.04186 -0.06088 133 LEU   B CD2   
2444 N  N     . ALA   B 135 ? 0.59046 0.45272 0.43108 0.07738  -0.05702 -0.06193 134 ALA   B N     
2445 C  CA    . ALA   B 135 ? 0.61457 0.48557 0.47470 0.06679  -0.05913 -0.05983 134 ALA   B CA    
2446 C  C     . ALA   B 135 ? 0.67799 0.53878 0.53894 0.06604  -0.07167 -0.06219 134 ALA   B C     
2447 O  O     . ALA   B 135 ? 0.64591 0.50729 0.52035 0.05961  -0.07883 -0.06167 134 ALA   B O     
2448 C  CB    . ALA   B 135 ? 0.57787 0.46231 0.44579 0.06265  -0.04855 -0.05605 134 ALA   B CB    
2449 N  N     . ARG   B 136 ? 0.67977 0.53096 0.52666 0.07285  -0.07455 -0.06447 135 ARG   B N     
2450 C  CA    . ARG   B 136 ? 0.64325 0.48217 0.48829 0.07369  -0.08765 -0.06731 135 ARG   B CA    
2451 C  C     . ARG   B 136 ? 0.70704 0.53499 0.55201 0.07447  -0.09967 -0.07016 135 ARG   B C     
2452 O  O     . ARG   B 136 ? 0.73681 0.56220 0.59432 0.06886  -0.10963 -0.07000 135 ARG   B O     
2453 C  CB    . ARG   B 136 ? 0.70853 0.53629 0.53329 0.08367  -0.08862 -0.07010 135 ARG   B CB    
2454 C  CG    . ARG   B 136 ? 0.81960 0.63690 0.64321 0.08400  -0.10015 -0.07241 135 ARG   B CG    
2455 C  CD    . ARG   B 136 ? 0.81687 0.62518 0.62026 0.09395  -0.09872 -0.07457 135 ARG   B CD    
2456 N  NE    . ARG   B 136 ? 0.76002 0.58124 0.56331 0.09390  -0.08397 -0.07092 135 ARG   B NE    
2457 C  CZ    . ARG   B 136 ? 0.83318 0.66602 0.64938 0.08674  -0.07872 -0.06773 135 ARG   B CZ    
2458 N  NH1   . ARG   B 136 ? 0.89246 0.72612 0.72235 0.07934  -0.08622 -0.06744 135 ARG   B NH1   
2459 N  NH2   . ARG   B 136 ? 0.86464 0.70858 0.68058 0.08712  -0.06572 -0.06443 135 ARG   B NH2   
2460 N  N     . SER   B 137 ? 0.66289 0.48426 0.49435 0.08155  -0.09900 -0.07245 136 SER   B N     
2461 C  CA    . SER   B 137 ? 0.68784 0.49756 0.51760 0.08314  -0.11088 -0.07553 136 SER   B CA    
2462 C  C     . SER   B 137 ? 0.72695 0.54663 0.57851 0.07285  -0.11188 -0.07254 136 SER   B C     
2463 O  O     . SER   B 137 ? 0.76491 0.57628 0.62169 0.07131  -0.12382 -0.07408 136 SER   B O     
2464 C  CB    . SER   B 137 ? 0.69395 0.49539 0.50416 0.09326  -0.10869 -0.07829 136 SER   B CB    
2465 O  OG    . SER   B 137 ? 0.77877 0.59285 0.59586 0.08995  -0.09805 -0.07535 136 SER   B OG    
2466 N  N     . TYR   B 138 ? 0.65716 0.49402 0.52136 0.06619  -0.09983 -0.06817 137 TYR   B N     
2467 C  CA    . TYR   B 138 ? 0.68127 0.52867 0.56610 0.05670  -0.09946 -0.06474 137 TYR   B CA    
2468 C  C     . TYR   B 138 ? 0.64954 0.50422 0.55202 0.04856  -0.10132 -0.06131 137 TYR   B C     
2469 O  O     . TYR   B 138 ? 0.70587 0.56630 0.62577 0.04144  -0.10418 -0.05836 137 TYR   B O     
2470 C  CB    . TYR   B 138 ? 0.65793 0.51917 0.54629 0.05445  -0.08589 -0.06196 137 TYR   B CB    
2471 C  CG    . TYR   B 138 ? 0.65909 0.51527 0.53436 0.06100  -0.08377 -0.06427 137 TYR   B CG    
2472 C  CD1   . TYR   B 138 ? 0.62921 0.47134 0.49633 0.06566  -0.09469 -0.06800 137 TYR   B CD1   
2473 C  CD2   . TYR   B 138 ? 0.67555 0.54094 0.54732 0.06252  -0.07114 -0.06248 137 TYR   B CD2   
2474 C  CE1   . TYR   B 138 ? 0.66459 0.50215 0.51931 0.07200  -0.09243 -0.06998 137 TYR   B CE1   
2475 C  CE2   . TYR   B 138 ? 0.63874 0.50018 0.49948 0.06849  -0.06873 -0.06400 137 TYR   B CE2   
2476 C  CZ    . TYR   B 138 ? 0.64989 0.49754 0.50170 0.07334  -0.07907 -0.06778 137 TYR   B CZ    
2477 O  OH    . TYR   B 138 ? 0.63731 0.48134 0.47790 0.07954  -0.07615 -0.06911 137 TYR   B OH    
2478 N  N     . GLY   B 139 ? 0.64834 0.50294 0.54685 0.04977  -0.09963 -0.06129 138 GLY   B N     
2479 C  CA    . GLY   B 139 ? 0.60788 0.47035 0.52283 0.04232  -0.10011 -0.05767 138 GLY   B CA    
2480 C  C     . GLY   B 139 ? 0.61771 0.49780 0.54519 0.03585  -0.08770 -0.05303 138 GLY   B C     
2481 O  O     . GLY   B 139 ? 0.59196 0.48010 0.53699 0.02862  -0.08825 -0.04910 138 GLY   B O     
2482 N  N     . ILE   B 140 ? 0.60930 0.49536 0.52832 0.03864  -0.07664 -0.05309 139 ILE   B N     
2483 C  CA    . ILE   B 140 ? 0.56849 0.47012 0.49798 0.03324  -0.06533 -0.04916 139 ILE   B CA    
2484 C  C     . ILE   B 140 ? 0.52373 0.42935 0.44415 0.03645  -0.05615 -0.04907 139 ILE   B C     
2485 O  O     . ILE   B 140 ? 0.58116 0.47815 0.48597 0.04367  -0.05693 -0.05187 139 ILE   B O     
2486 C  CB    . ILE   B 140 ? 0.49996 0.40643 0.43192 0.03232  -0.06090 -0.04854 139 ILE   B CB    
2487 C  CG1   . ILE   B 140 ? 0.52229 0.42453 0.43732 0.03990  -0.05586 -0.05111 139 ILE   B CG1   
2488 C  CG2   . ILE   B 140 ? 0.48694 0.38885 0.42745 0.02963  -0.07024 -0.04857 139 ILE   B CG2   
2489 C  CD1   . ILE   B 140 ? 0.48143 0.38752 0.39755 0.03974  -0.05164 -0.05076 139 ILE   B CD1   
2490 N  N     . PRO   B 141 ? 0.53098 0.44950 0.46094 0.03155  -0.04739 -0.04565 140 PRO   B N     
2491 C  CA    . PRO   B 141 ? 0.49935 0.42259 0.42288 0.03397  -0.03864 -0.04498 140 PRO   B CA    
2492 C  C     . PRO   B 141 ? 0.58149 0.50559 0.49549 0.03891  -0.03148 -0.04547 140 PRO   B C     
2493 O  O     . PRO   B 141 ? 0.56042 0.48520 0.47559 0.03881  -0.03091 -0.04565 140 PRO   B O     
2494 C  CB    . PRO   B 141 ? 0.50816 0.44447 0.44631 0.02681  -0.03275 -0.04115 140 PRO   B CB    
2495 C  CG    . PRO   B 141 ? 0.45412 0.39067 0.40456 0.02167  -0.03954 -0.03981 140 PRO   B CG    
2496 C  CD    . PRO   B 141 ? 0.51032 0.43854 0.45795 0.02370  -0.04665 -0.04197 140 PRO   B CD    
2497 N  N     . PHE   B 142 ? 0.56617 0.49094 0.47161 0.04320  -0.02554 -0.04515 141 PHE   B N     
2498 C  CA    . PHE   B 142 ? 0.53413 0.46158 0.43255 0.04780  -0.01730 -0.04424 141 PHE   B CA    
2499 C  C     . PHE   B 142 ? 0.52406 0.46259 0.42890 0.04503  -0.00825 -0.04087 141 PHE   B C     
2500 O  O     . PHE   B 142 ? 0.51340 0.45205 0.41656 0.04551  -0.00753 -0.04042 141 PHE   B O     
2501 C  CB    . PHE   B 142 ? 0.55126 0.46762 0.43152 0.05764  -0.01856 -0.04650 141 PHE   B CB    
2502 C  CG    . PHE   B 142 ? 0.55908 0.47961 0.43339 0.06269  -0.00871 -0.04420 141 PHE   B CG    
2503 C  CD1   . PHE   B 142 ? 0.52245 0.44811 0.40078 0.06180  -0.00426 -0.04283 141 PHE   B CD1   
2504 C  CD2   . PHE   B 142 ? 0.59608 0.51582 0.46179 0.06830  -0.00373 -0.04288 141 PHE   B CD2   
2505 C  CE1   . PHE   B 142 ? 0.54598 0.47591 0.42069 0.06624  0.00466  -0.04001 141 PHE   B CE1   
2506 C  CE2   . PHE   B 142 ? 0.60985 0.53409 0.47199 0.07297  0.00554  -0.03974 141 PHE   B CE2   
2507 C  CZ    . PHE   B 142 ? 0.59754 0.52699 0.46468 0.07181  0.00967  -0.03818 141 PHE   B CZ    
2508 N  N     . ILE   B 143 ? 0.51865 0.46604 0.43100 0.04214  -0.00190 -0.03859 142 ILE   B N     
2509 C  CA    . ILE   B 143 ? 0.56277 0.52052 0.48249 0.03922  0.00597  -0.03536 142 ILE   B CA    
2510 C  C     . ILE   B 143 ? 0.52906 0.48933 0.44472 0.04368  0.01325  -0.03347 142 ILE   B C     
2511 O  O     . ILE   B 143 ? 0.52347 0.48365 0.43926 0.04436  0.01384  -0.03366 142 ILE   B O     
2512 C  CB    . ILE   B 143 ? 0.50414 0.47065 0.43839 0.03132  0.00658  -0.03386 142 ILE   B CB    
2513 C  CG1   . ILE   B 143 ? 0.54314 0.50765 0.48269 0.02718  -0.00033 -0.03479 142 ILE   B CG1   
2514 C  CG2   . ILE   B 143 ? 0.48394 0.45960 0.42454 0.02902  0.01367  -0.03093 142 ILE   B CG2   
2515 C  CD1   . ILE   B 143 ? 0.60167 0.56637 0.54070 0.02677  -0.00058 -0.03433 142 ILE   B CD1   
2516 N  N     . GLU   B 144 ? 0.52486 0.48761 0.43768 0.04672  0.01885  -0.03123 143 GLU   B N     
2517 C  CA    . GLU   B 144 ? 0.49584 0.46316 0.40848 0.05010  0.02664  -0.02799 143 GLU   B CA    
2518 C  C     . GLU   B 144 ? 0.51858 0.49672 0.44555 0.04355  0.03088  -0.02525 143 GLU   B C     
2519 O  O     . GLU   B 144 ? 0.47559 0.45788 0.40965 0.03855  0.03007  -0.02498 143 GLU   B O     
2520 C  CB    . GLU   B 144 ? 0.55016 0.51545 0.45424 0.05669  0.03089  -0.02604 143 GLU   B CB    
2521 C  CG    . GLU   B 144 ? 0.63596 0.58932 0.52434 0.06382  0.02600  -0.02911 143 GLU   B CG    
2522 C  CD    . GLU   B 144 ? 0.70699 0.65809 0.58555 0.07164  0.03102  -0.02676 143 GLU   B CD    
2523 O  OE1   . GLU   B 144 ? 0.74212 0.70057 0.62529 0.07303  0.03921  -0.02208 143 GLU   B OE1   
2524 O  OE2   . GLU   B 144 ? 0.73378 0.67556 0.60040 0.07653  0.02653  -0.02936 143 GLU   B OE2   
2525 N  N     . THR   B 145 ? 0.51511 0.49730 0.44603 0.04388  0.03503  -0.02327 144 THR   B N     
2526 C  CA    . THR   B 145 ? 0.49070 0.48194 0.43471 0.03813  0.03809  -0.02100 144 THR   B CA    
2527 C  C     . THR   B 145 ? 0.46550 0.46109 0.41220 0.04120  0.04480  -0.01699 144 THR   B C     
2528 O  O     . THR   B 145 ? 0.49786 0.48987 0.43692 0.04738  0.04711  -0.01610 144 THR   B O     
2529 C  CB    . THR   B 145 ? 0.45757 0.45008 0.40775 0.03305  0.03452  -0.02294 144 THR   B CB    
2530 O  OG1   . THR   B 145 ? 0.41204 0.40103 0.35728 0.03656  0.03459  -0.02359 144 THR   B OG1   
2531 C  CG2   . THR   B 145 ? 0.43830 0.42742 0.38827 0.02973  0.02802  -0.02589 144 THR   B CG2   
2532 N  N     . SER   B 146 ? 0.45254 0.45573 0.41059 0.03699  0.04766  -0.01433 145 SER   B N     
2533 C  CA    . SER   B 146 ? 0.44129 0.44971 0.40633 0.03788  0.05280  -0.01035 145 SER   B CA    
2534 C  C     . SER   B 146 ? 0.44167 0.45532 0.41824 0.03129  0.05129  -0.01064 145 SER   B C     
2535 O  O     . SER   B 146 ? 0.46750 0.48479 0.45079 0.02726  0.05058  -0.01023 145 SER   B O     
2536 C  CB    . SER   B 146 ? 0.45531 0.46740 0.42318 0.04067  0.05809  -0.00567 145 SER   B CB    
2537 O  OG    . SER   B 146 ? 0.44218 0.46023 0.42052 0.03992  0.06201  -0.00149 145 SER   B OG    
2538 N  N     . ALA   B 147 ? 0.43675 0.45049 0.41521 0.03059  0.05077  -0.01130 146 ALA   B N     
2539 C  CA    . ALA   B 147 ? 0.42562 0.44397 0.41452 0.02519  0.04963  -0.01128 146 ALA   B CA    
2540 C  C     . ALA   B 147 ? 0.45127 0.47537 0.45034 0.02450  0.05323  -0.00694 146 ALA   B C     
2541 O  O     . ALA   B 147 ? 0.44195 0.46921 0.44924 0.02014  0.05151  -0.00704 146 ALA   B O     
2542 C  CB    . ALA   B 147 ? 0.41216 0.42931 0.40096 0.02482  0.04841  -0.01276 146 ALA   B CB    
2543 N  N     . LYS   B 148 ? 0.48335 0.50859 0.48228 0.02905  0.05799  -0.00284 147 LYS   B N     
2544 C  CA    . LYS   B 148 ? 0.50634 0.53726 0.51698 0.02838  0.06116  0.00213  147 LYS   B CA    
2545 C  C     . LYS   B 148 ? 0.44561 0.47890 0.46100 0.02577  0.06035  0.00295  147 LYS   B C     
2546 O  O     . LYS   B 148 ? 0.44682 0.48378 0.47292 0.02220  0.05924  0.00449  147 LYS   B O     
2547 C  CB    . LYS   B 148 ? 0.49055 0.52248 0.50042 0.03457  0.06710  0.00728  147 LYS   B CB    
2548 C  CG    . LYS   B 148 ? 0.50302 0.54109 0.52723 0.03394  0.07026  0.01332  147 LYS   B CG    
2549 C  CD    . LYS   B 148 ? 0.45360 0.49326 0.47710 0.04069  0.07694  0.01953  147 LYS   B CD    
2550 C  CE    . LYS   B 148 ? 0.52935 0.57551 0.56917 0.04016  0.08008  0.02654  147 LYS   B CE    
2551 N  NZ    . LYS   B 148 ? 0.60766 0.65609 0.64767 0.04683  0.08702  0.03347  147 LYS   B NZ    
2552 N  N     . THR   B 149 ? 0.51777 0.54856 0.52521 0.02777  0.06056  0.00194  148 THR   B N     
2553 C  CA    . THR   B 149 ? 0.47876 0.51134 0.48944 0.02542  0.05963  0.00230  148 THR   B CA    
2554 C  C     . THR   B 149 ? 0.48006 0.51069 0.48815 0.02097  0.05443  -0.00262 148 THR   B C     
2555 O  O     . THR   B 149 ? 0.53861 0.57054 0.54910 0.01879  0.05326  -0.00271 148 THR   B O     
2556 C  CB    . THR   B 149 ? 0.43248 0.46340 0.43592 0.03018  0.06274  0.00407  148 THR   B CB    
2557 O  OG1   . THR   B 149 ? 0.54867 0.57356 0.53953 0.03172  0.06000  -0.00046 148 THR   B OG1   
2558 C  CG2   . THR   B 149 ? 0.47699 0.50933 0.48094 0.03607  0.06866  0.00939  148 THR   B CG2   
2559 N  N     . ARG   B 150 ? 0.51906 0.54667 0.52248 0.01991  0.05151  -0.00629 149 ARG   B N     
2560 C  CA    . ARG   B 150 ? 0.41027 0.43580 0.41075 0.01658  0.04700  -0.01033 149 ARG   B CA    
2561 C  C     . ARG   B 150 ? 0.51460 0.53651 0.50684 0.01804  0.04571  -0.01203 149 ARG   B C     
2562 O  O     . ARG   B 150 ? 0.49914 0.51979 0.49015 0.01531  0.04212  -0.01458 149 ARG   B O     
2563 C  CB    . ARG   B 150 ? 0.48036 0.50913 0.48863 0.01219  0.04499  -0.01049 149 ARG   B CB    
2564 C  CG    . ARG   B 150 ? 0.50518 0.53289 0.51302 0.00922  0.04131  -0.01357 149 ARG   B CG    
2565 C  CD    . ARG   B 150 ? 0.53094 0.56118 0.54521 0.00617  0.03959  -0.01351 149 ARG   B CD    
2566 N  NE    . ARG   B 150 ? 0.53774 0.56723 0.55160 0.00420  0.03681  -0.01574 149 ARG   B NE    
2567 C  CZ    . ARG   B 150 ? 0.50419 0.53249 0.51462 0.00321  0.03488  -0.01728 149 ARG   B CZ    
2568 N  NH1   . ARG   B 150 ? 0.50719 0.53433 0.51377 0.00378  0.03484  -0.01743 149 ARG   B NH1   
2569 N  NH2   . ARG   B 150 ? 0.56308 0.59140 0.57434 0.00183  0.03298  -0.01834 149 ARG   B NH2   
2570 N  N     . GLN   B 151 ? 0.45402 0.47399 0.44049 0.02267  0.04848  -0.01045 150 GLN   B N     
2571 C  CA    . GLN   B 151 ? 0.52960 0.54510 0.50746 0.02446  0.04658  -0.01240 150 GLN   B CA    
2572 C  C     . GLN   B 151 ? 0.49085 0.50102 0.46242 0.02429  0.04200  -0.01619 150 GLN   B C     
2573 O  O     . GLN   B 151 ? 0.50596 0.51371 0.47435 0.02650  0.04203  -0.01676 150 GLN   B O     
2574 C  CB    . GLN   B 151 ? 0.46407 0.47756 0.43534 0.03065  0.05050  -0.00998 150 GLN   B CB    
2575 C  CG    . GLN   B 151 ? 0.57552 0.58183 0.53474 0.03415  0.04770  -0.01276 150 GLN   B CG    
2576 C  CD    . GLN   B 151 ? 0.68752 0.68962 0.63705 0.04195  0.05103  -0.01119 150 GLN   B CD    
2577 O  OE1   . GLN   B 151 ? 0.73653 0.74247 0.68950 0.04484  0.05669  -0.00683 150 GLN   B OE1   
2578 N  NE2   . GLN   B 151 ? 0.69009 0.68397 0.62762 0.04579  0.04734  -0.01445 150 GLN   B NE2   
2579 N  N     . GLY   B 152 ? 0.43493 0.44348 0.40572 0.02153  0.03793  -0.01843 151 GLY   B N     
2580 C  CA    . GLY   B 152 ? 0.41818 0.42154 0.38445 0.02110  0.03280  -0.02147 151 GLY   B CA    
2581 C  C     . GLY   B 152 ? 0.47234 0.47696 0.44352 0.01791  0.03074  -0.02246 151 GLY   B C     
2582 O  O     . GLY   B 152 ? 0.41701 0.41733 0.38543 0.01768  0.02636  -0.02452 151 GLY   B O     
2583 N  N     . VAL   B 153 ? 0.43536 0.44536 0.41391 0.01559  0.03335  -0.02095 152 VAL   B N     
2584 C  CA    . VAL   B 153 ? 0.47605 0.48703 0.45861 0.01310  0.03165  -0.02182 152 VAL   B CA    
2585 C  C     . VAL   B 153 ? 0.50632 0.51742 0.49182 0.00957  0.02777  -0.02285 152 VAL   B C     
2586 O  O     . VAL   B 153 ? 0.39013 0.39827 0.37465 0.00909  0.02430  -0.02415 152 VAL   B O     
2587 C  CB    . VAL   B 153 ? 0.38047 0.39659 0.37011 0.01164  0.03477  -0.02004 152 VAL   B CB    
2588 C  CG1   . VAL   B 153 ? 0.46490 0.48219 0.45872 0.00885  0.03281  -0.02100 152 VAL   B CG1   
2589 C  CG2   . VAL   B 153 ? 0.43784 0.45397 0.42602 0.01521  0.03846  -0.01836 152 VAL   B CG2   
2590 N  N     . ASP   B 154 ? 0.45750 0.47198 0.44700 0.00731  0.02827  -0.02189 153 ASP   B N     
2591 C  CA    . ASP   B 154 ? 0.44622 0.46111 0.43859 0.00462  0.02519  -0.02206 153 ASP   B CA    
2592 C  C     . ASP   B 154 ? 0.48214 0.49190 0.47020 0.00555  0.02125  -0.02325 153 ASP   B C     
2593 O  O     . ASP   B 154 ? 0.46077 0.46920 0.45125 0.00403  0.01770  -0.02343 153 ASP   B O     
2594 C  CB    . ASP   B 154 ? 0.50565 0.52423 0.50139 0.00297  0.02647  -0.02083 153 ASP   B CB    
2595 C  CG    . ASP   B 154 ? 0.57863 0.60123 0.57872 0.00218  0.02910  -0.01986 153 ASP   B CG    
2596 O  OD1   . ASP   B 154 ? 0.58784 0.61102 0.58974 0.00207  0.02946  -0.02003 153 ASP   B OD1   
2597 O  OD2   . ASP   B 154 ? 0.65600 0.68078 0.65775 0.00174  0.03033  -0.01900 153 ASP   B OD2   
2598 N  N     . ASP   B 155 ? 0.47846 0.48506 0.46045 0.00826  0.02155  -0.02382 154 ASP   B N     
2599 C  CA    . ASP   B 155 ? 0.51910 0.51965 0.49602 0.00969  0.01708  -0.02526 154 ASP   B CA    
2600 C  C     . ASP   B 155 ? 0.44092 0.43652 0.41558 0.01069  0.01313  -0.02681 154 ASP   B C     
2601 O  O     . ASP   B 155 ? 0.39342 0.38560 0.36940 0.00953  0.00782  -0.02740 154 ASP   B O     
2602 C  CB    . ASP   B 155 ? 0.50859 0.50597 0.47760 0.01374  0.01878  -0.02567 154 ASP   B CB    
2603 C  CG    . ASP   B 155 ? 0.62782 0.61856 0.59111 0.01541  0.01383  -0.02728 154 ASP   B CG    
2604 O  OD1   . ASP   B 155 ? 0.65762 0.64700 0.62490 0.01270  0.00895  -0.02763 154 ASP   B OD1   
2605 O  OD2   . ASP   B 155 ? 0.73746 0.72411 0.69236 0.01980  0.01474  -0.02790 154 ASP   B OD2   
2606 N  N     . ALA   B 156 ? 0.40675 0.40201 0.37891 0.01273  0.01540  -0.02719 155 ALA   B N     
2607 C  CA    . ALA   B 156 ? 0.47327 0.46335 0.44249 0.01409  0.01158  -0.02885 155 ALA   B CA    
2608 C  C     . ALA   B 156 ? 0.34942 0.34173 0.32704 0.00992  0.00856  -0.02822 155 ALA   B C     
2609 O  O     . ALA   B 156 ? 0.34675 0.33441 0.32472 0.00955  0.00282  -0.02906 155 ALA   B O     
2610 C  CB    . ALA   B 156 ? 0.36190 0.35216 0.32752 0.01705  0.01543  -0.02890 155 ALA   B CB    
2611 N  N     . PHE   B 157 ? 0.36151 0.36066 0.34616 0.00707  0.01214  -0.02649 156 PHE   B N     
2612 C  CA    . PHE   B 157 ? 0.34187 0.34361 0.33426 0.00382  0.01018  -0.02526 156 PHE   B CA    
2613 C  C     . PHE   B 157 ? 0.38141 0.38377 0.37873 0.00156  0.00715  -0.02376 156 PHE   B C     
2614 O  O     . PHE   B 157 ? 0.31025 0.31142 0.31254 0.00001  0.00306  -0.02281 156 PHE   B O     
2615 C  CB    . PHE   B 157 ? 0.32265 0.33073 0.31980 0.00227  0.01473  -0.02389 156 PHE   B CB    
2616 C  CG    . PHE   B 157 ? 0.33408 0.34192 0.32916 0.00371  0.01678  -0.02481 156 PHE   B CG    
2617 C  CD1   . PHE   B 157 ? 0.35278 0.35969 0.34995 0.00308  0.01486  -0.02509 156 PHE   B CD1   
2618 C  CD2   . PHE   B 157 ? 0.35059 0.35939 0.34249 0.00569  0.02069  -0.02497 156 PHE   B CD2   
2619 C  CE1   . PHE   B 157 ? 0.30484 0.31152 0.30004 0.00449  0.01684  -0.02592 156 PHE   B CE1   
2620 C  CE2   . PHE   B 157 ? 0.41088 0.41971 0.40175 0.00709  0.02269  -0.02531 156 PHE   B CE2   
2621 C  CZ    . PHE   B 157 ? 0.37489 0.38255 0.36710 0.00645  0.02069  -0.02599 156 PHE   B CZ    
2622 N  N     . TYR   B 158 ? 0.35581 0.36029 0.35272 0.00132  0.00912  -0.02310 157 TYR   B N     
2623 C  CA    . TYR   B 158 ? 0.39907 0.40440 0.40083 -0.00064 0.00657  -0.02137 157 TYR   B CA    
2624 C  C     . TYR   B 158 ? 0.40955 0.40800 0.40920 0.00015  0.00023  -0.02251 157 TYR   B C     
2625 O  O     . TYR   B 158 ? 0.34933 0.34758 0.35577 -0.00187 -0.00375 -0.02064 157 TYR   B O     
2626 C  CB    . TYR   B 158 ? 0.42135 0.42959 0.42193 -0.00067 0.00976  -0.02083 157 TYR   B CB    
2627 C  CG    . TYR   B 158 ? 0.41695 0.43135 0.42073 -0.00166 0.01456  -0.01944 157 TYR   B CG    
2628 C  CD1   . TYR   B 158 ? 0.42356 0.44035 0.42969 -0.00197 0.01637  -0.01911 157 TYR   B CD1   
2629 C  CD2   . TYR   B 158 ? 0.52490 0.54222 0.52914 -0.00207 0.01678  -0.01855 157 TYR   B CD2   
2630 C  CE1   . TYR   B 158 ? 0.47870 0.49995 0.48707 -0.00239 0.01984  -0.01812 157 TYR   B CE1   
2631 C  CE2   . TYR   B 158 ? 0.50939 0.53125 0.51599 -0.00254 0.02024  -0.01752 157 TYR   B CE2   
2632 C  CZ    . TYR   B 158 ? 0.52588 0.54938 0.53431 -0.00256 0.02154  -0.01740 157 TYR   B CZ    
2633 O  OH    . TYR   B 158 ? 0.64490 0.67172 0.65488 -0.00252 0.02411  -0.01670 157 TYR   B OH    
2634 N  N     . THR   B 159 ? 0.38756 0.37994 0.37790 0.00350  -0.00101 -0.02531 158 THR   B N     
2635 C  CA    . THR   B 159 ? 0.38111 0.36540 0.36797 0.00500  -0.00797 -0.02691 158 THR   B CA    
2636 C  C     . THR   B 159 ? 0.33745 0.31876 0.32870 0.00400  -0.01314 -0.02684 158 THR   B C     
2637 O  O     . THR   B 159 ? 0.37516 0.35278 0.37099 0.00276  -0.01964 -0.02617 158 THR   B O     
2638 C  CB    . THR   B 159 ? 0.43001 0.40792 0.40437 0.00996  -0.00776 -0.02985 158 THR   B CB    
2639 O  OG1   . THR   B 159 ? 0.46707 0.44805 0.43911 0.01050  -0.00343 -0.02926 158 THR   B OG1   
2640 C  CG2   . THR   B 159 ? 0.42242 0.39023 0.39143 0.01240  -0.01591 -0.03209 158 THR   B CG2   
2641 N  N     . LEU   B 160 ? 0.42045 0.40385 0.41194 0.00413  -0.01047 -0.02704 159 LEU   B N     
2642 C  CA    . LEU   B 160 ? 0.33060 0.31181 0.32731 0.00288  -0.01521 -0.02660 159 LEU   B CA    
2643 C  C     . LEU   B 160 ? 0.31941 0.30603 0.32922 -0.00130 -0.01635 -0.02254 159 LEU   B C     
2644 O  O     . LEU   B 160 ? 0.35612 0.33957 0.37222 -0.00260 -0.02267 -0.02132 159 LEU   B O     
2645 C  CB    . LEU   B 160 ? 0.34065 0.32351 0.33507 0.00384  -0.01160 -0.02749 159 LEU   B CB    
2646 C  CG    . LEU   B 160 ? 0.30263 0.28382 0.30270 0.00248  -0.01594 -0.02692 159 LEU   B CG    
2647 C  CD1   . LEU   B 160 ? 0.31297 0.28413 0.30912 0.00450  -0.02453 -0.02920 159 LEU   B CD1   
2648 C  CD2   . LEU   B 160 ? 0.34974 0.33383 0.34797 0.00317  -0.01127 -0.02757 159 LEU   B CD2   
2649 N  N     . VAL   B 161 ? 0.33507 0.32968 0.34943 -0.00308 -0.01043 -0.02003 160 VAL   B N     
2650 C  CA    . VAL   B 161 ? 0.31194 0.31169 0.33797 -0.00606 -0.01087 -0.01556 160 VAL   B CA    
2651 C  C     . VAL   B 161 ? 0.34490 0.34150 0.37461 -0.00693 -0.01629 -0.01435 160 VAL   B C     
2652 O  O     . VAL   B 161 ? 0.38069 0.37762 0.42062 -0.00892 -0.02053 -0.01097 160 VAL   B O     
2653 C  CB    . VAL   B 161 ? 0.32984 0.33761 0.35785 -0.00673 -0.00366 -0.01349 160 VAL   B CB    
2654 C  CG1   . VAL   B 161 ? 0.35126 0.36396 0.38984 -0.00873 -0.00362 -0.00851 160 VAL   B CG1   
2655 C  CG2   . VAL   B 161 ? 0.33318 0.34365 0.35990 -0.00622 0.00027  -0.01408 160 VAL   B CG2   
2656 N  N     . ARG   B 162 ? 0.35355 0.34677 0.37555 -0.00533 -0.01657 -0.01684 161 ARG   B N     
2657 C  CA    . ARG   B 162 ? 0.38311 0.37236 0.40811 -0.00597 -0.02249 -0.01606 161 ARG   B CA    
2658 C  C     . ARG   B 162 ? 0.43547 0.41592 0.46068 -0.00528 -0.03146 -0.01755 161 ARG   B C     
2659 O  O     . ARG   B 162 ? 0.47300 0.45145 0.50691 -0.00709 -0.03764 -0.01510 161 ARG   B O     
2660 C  CB    . ARG   B 162 ? 0.43393 0.42106 0.44986 -0.00404 -0.02087 -0.01854 161 ARG   B CB    
2661 C  CG    . ARG   B 162 ? 0.45576 0.45106 0.47296 -0.00504 -0.01335 -0.01671 161 ARG   B CG    
2662 C  CD    . ARG   B 162 ? 0.45203 0.44518 0.46028 -0.00301 -0.01166 -0.01913 161 ARG   B CD    
2663 N  NE    . ARG   B 162 ? 0.48939 0.48965 0.49818 -0.00371 -0.00485 -0.01782 161 ARG   B NE    
2664 C  CZ    . ARG   B 162 ? 0.47991 0.48125 0.48161 -0.00187 -0.00003 -0.01968 161 ARG   B CZ    
2665 N  NH1   . ARG   B 162 ? 0.52698 0.52351 0.52033 0.00108  -0.00024 -0.02254 161 ARG   B NH1   
2666 N  NH2   . ARG   B 162 ? 0.54295 0.55020 0.54625 -0.00270 0.00499  -0.01834 161 ARG   B NH2   
2667 N  N     . GLU   B 163 ? 0.46754 0.44244 0.48373 -0.00252 -0.03264 -0.02132 162 GLU   B N     
2668 C  CA    . GLU   B 163 ? 0.45728 0.42335 0.47352 -0.00157 -0.04159 -0.02285 162 GLU   B CA    
2669 C  C     . GLU   B 163 ? 0.44437 0.41404 0.47529 -0.00515 -0.04439 -0.01856 162 GLU   B C     
2670 O  O     . GLU   B 163 ? 0.43848 0.40305 0.47666 -0.00628 -0.05294 -0.01726 162 GLU   B O     
2671 C  CB    . GLU   B 163 ? 0.40333 0.36371 0.40692 0.00247  -0.04110 -0.02728 162 GLU   B CB    
2672 C  CG    . GLU   B 163 ? 0.43990 0.39352 0.42886 0.00718  -0.04117 -0.03125 162 GLU   B CG    
2673 C  CD    . GLU   B 163 ? 0.54391 0.48873 0.53181 0.00817  -0.05026 -0.03234 162 GLU   B CD    
2674 O  OE1   . GLU   B 163 ? 0.53597 0.47277 0.52568 0.00862  -0.05943 -0.03329 162 GLU   B OE1   
2675 O  OE2   . GLU   B 163 ? 0.59308 0.53898 0.57909 0.00831  -0.04861 -0.03210 162 GLU   B OE2   
2676 N  N     . ILE   B 164 ? 0.44411 0.42221 0.47992 -0.00674 -0.03762 -0.01610 163 ILE   B N     
2677 C  CA    . ILE   B 164 ? 0.39338 0.37548 0.44331 -0.00966 -0.03948 -0.01135 163 ILE   B CA    
2678 C  C     . ILE   B 164 ? 0.39324 0.37938 0.45606 -0.01237 -0.04113 -0.00595 163 ILE   B C     
2679 O  O     . ILE   B 164 ? 0.43560 0.42129 0.51104 -0.01442 -0.04678 -0.00195 163 ILE   B O     
2680 C  CB    . ILE   B 164 ? 0.37009 0.36020 0.42148 -0.01016 -0.03148 -0.00980 163 ILE   B CB    
2681 C  CG1   . ILE   B 164 ? 0.36591 0.35204 0.40646 -0.00771 -0.03045 -0.01452 163 ILE   B CG1   
2682 C  CG2   . ILE   B 164 ? 0.41396 0.40837 0.47981 -0.01262 -0.03293 -0.00434 163 ILE   B CG2   
2683 C  CD1   . ILE   B 164 ? 0.40086 0.39440 0.44148 -0.00793 -0.02245 -0.01363 163 ILE   B CD1   
2684 N  N     . ARG   B 165 ? 0.41703 0.40749 0.47767 -0.01237 -0.03612 -0.00530 164 ARG   B N     
2685 C  CA    . ARG   B 165 ? 0.43129 0.42601 0.50378 -0.01458 -0.03698 0.00007  164 ARG   B CA    
2686 C  C     . ARG   B 165 ? 0.51239 0.49884 0.58812 -0.01505 -0.04709 -0.00042 164 ARG   B C     
2687 O  O     . ARG   B 165 ? 0.53634 0.52382 0.62661 -0.01738 -0.05193 0.00478  164 ARG   B O     
2688 C  CB    . ARG   B 165 ? 0.40214 0.40261 0.47006 -0.01410 -0.02951 0.00027  164 ARG   B CB    
2689 C  CG    . ARG   B 165 ? 0.40895 0.41821 0.47724 -0.01387 -0.02038 0.00238  164 ARG   B CG    
2690 C  CD    . ARG   B 165 ? 0.41403 0.42739 0.47648 -0.01303 -0.01416 0.00177  164 ARG   B CD    
2691 N  NE    . ARG   B 165 ? 0.39880 0.41946 0.46171 -0.01239 -0.00663 0.00388  164 ARG   B NE    
2692 C  CZ    . ARG   B 165 ? 0.42420 0.44812 0.48101 -0.01127 -0.00104 0.00281  164 ARG   B CZ    
2693 N  NH1   . ARG   B 165 ? 0.45636 0.47794 0.50695 -0.01093 -0.00136 0.00012  164 ARG   B NH1   
2694 N  NH2   . ARG   B 165 ? 0.40370 0.43299 0.46067 -0.01022 0.00468  0.00458  164 ARG   B NH2   
2695 N  N     . LYS   B 166 ? 0.46727 0.44507 0.52969 -0.01249 -0.05061 -0.00640 165 LYS   B N     
2696 C  CA    . LYS   B 166 ? 0.55366 0.52171 0.61689 -0.01211 -0.06118 -0.00778 165 LYS   B CA    
2697 C  C     . LYS   B 166 ? 0.55161 0.51393 0.62275 -0.01294 -0.07010 -0.00684 165 LYS   B C     
2698 O  O     . LYS   B 166 ? 0.63553 0.59353 0.71715 -0.01457 -0.07901 -0.00427 165 LYS   B O     
2699 C  CB    . LYS   B 166 ? 0.55049 0.50986 0.59563 -0.00799 -0.06251 -0.01459 165 LYS   B CB    
2700 C  CG    . LYS   B 166 ? 0.50995 0.47343 0.54931 -0.00743 -0.05616 -0.01506 165 LYS   B CG    
2701 C  CD    . LYS   B 166 ? 0.57100 0.52803 0.59197 -0.00278 -0.05461 -0.02114 165 LYS   B CD    
2702 C  CE    . LYS   B 166 ? 0.62970 0.57316 0.64244 0.00072  -0.06472 -0.02540 165 LYS   B CE    
2703 N  NZ    . LYS   B 166 ? 0.66845 0.60589 0.66237 0.00636  -0.06210 -0.03072 165 LYS   B NZ    
2704 N  N     . HIS   B 167 ? 0.55487 0.51698 0.62190 -0.01193 -0.06822 -0.00868 166 HIS   B N     
2705 C  CA    . HIS   B 167 ? 0.55418 0.51034 0.62791 -0.01251 -0.07689 -0.00818 166 HIS   B CA    
2706 C  C     . HIS   B 167 ? 0.63158 0.59492 0.72667 -0.01670 -0.07819 -0.00012 166 HIS   B C     
2707 O  O     . HIS   B 167 ? 0.68680 0.64455 0.79208 -0.01799 -0.08802 0.00180  166 HIS   B O     
2708 C  CB    . HIS   B 167 ? 0.57902 0.53386 0.64296 -0.01032 -0.07376 -0.01194 166 HIS   B CB    
2709 C  CG    . HIS   B 167 ? 0.65641 0.60635 0.72776 -0.01110 -0.08166 -0.01110 166 HIS   B CG    
2710 N  ND1   . HIS   B 167 ? 0.69748 0.65535 0.78322 -0.01421 -0.07919 -0.00553 166 HIS   B ND1   
2711 C  CD2   . HIS   B 167 ? 0.63074 0.56832 0.69668 -0.00881 -0.09207 -0.01512 166 HIS   B CD2   
2712 C  CE1   . HIS   B 167 ? 0.65634 0.60741 0.74631 -0.01430 -0.08778 -0.00596 166 HIS   B CE1   
2713 N  NE2   . HIS   B 167 ? 0.70012 0.63856 0.77804 -0.01104 -0.09596 -0.01193 166 HIS   B NE2   
2714 N  N     . LYS   B 168 ? 0.62203 0.59729 0.72425 -0.01845 -0.06870 0.00493  167 LYS   B N     
2715 C  CA    . LYS   B 168 ? 0.56833 0.55124 0.69093 -0.02163 -0.06873 0.01365  167 LYS   B CA    
2716 C  C     . LYS   B 168 ? 0.59843 0.57896 0.73186 -0.02336 -0.07577 0.01721  167 LYS   B C     
2717 O  O     . LYS   B 168 ? 0.66499 0.65049 0.81721 -0.02593 -0.07774 0.02507  167 LYS   B O     
2718 C  CB    . LYS   B 168 ? 0.54679 0.54224 0.67200 -0.02186 -0.05651 0.01799  167 LYS   B CB    
2719 C  CG    . LYS   B 168 ? 0.59062 0.58908 0.70572 -0.02019 -0.04908 0.01482  167 LYS   B CG    
2720 C  CD    . LYS   B 168 ? 0.61798 0.61179 0.73497 -0.02033 -0.05431 0.01361  167 LYS   B CD    
2721 C  CE    . LYS   B 168 ? 0.57160 0.57055 0.68268 -0.01918 -0.04620 0.01249  167 LYS   B CE    
2722 N  NZ    . LYS   B 168 ? 0.63424 0.64338 0.75827 -0.02022 -0.04022 0.02016  167 LYS   B NZ    
2723 N  N     . VAL   C 3   ? 0.41474 0.47850 0.58546 0.05348  0.09562  0.06001  2   VAL   C N     
2724 C  CA    . VAL   C 3   ? 0.46102 0.51922 0.62565 0.04635  0.08663  0.04954  2   VAL   C CA    
2725 C  C     . VAL   C 3   ? 0.43318 0.48939 0.59501 0.04235  0.08210  0.04514  2   VAL   C C     
2726 O  O     . VAL   C 3   ? 0.45922 0.51895 0.63560 0.04041  0.08129  0.05021  2   VAL   C O     
2727 C  CB    . VAL   C 3   ? 0.45644 0.51547 0.63730 0.04085  0.08102  0.05006  2   VAL   C CB    
2728 C  CG1   . VAL   C 3   ? 0.42986 0.48295 0.60360 0.03429  0.07204  0.03961  2   VAL   C CG1   
2729 C  CG2   . VAL   C 3   ? 0.44885 0.50909 0.63063 0.04425  0.08475  0.05296  2   VAL   C CG2   
2730 N  N     . ASN   C 4   ? 0.41328 0.46378 0.55745 0.04082  0.07864  0.03579  3   ASN   C N     
2731 C  CA    . ASN   C 4   ? 0.36740 0.41582 0.50548 0.03835  0.07562  0.03159  3   ASN   C CA    
2732 C  C     . ASN   C 4   ? 0.37041 0.41879 0.52123 0.03154  0.06841  0.03012  3   ASN   C C     
2733 O  O     . ASN   C 4   ? 0.44685 0.49258 0.59982 0.02739  0.06272  0.02573  3   ASN   C O     
2734 C  CB    . ASN   C 4   ? 0.41601 0.45838 0.53362 0.03828  0.07329  0.02243  3   ASN   C CB    
2735 C  CG    . ASN   C 4   ? 0.40245 0.44337 0.50529 0.04561  0.07940  0.02332  3   ASN   C CG    
2736 O  OD1   . ASN   C 4   ? 0.43104 0.47538 0.53673 0.05110  0.08582  0.03047  3   ASN   C OD1   
2737 N  ND2   . ASN   C 4   ? 0.44888 0.48439 0.53595 0.04613  0.07722  0.01630  3   ASN   C ND2   
2738 N  N     . PRO   C 5   ? 0.38651 0.43712 0.54495 0.03057  0.06813  0.03337  4   PRO   C N     
2739 C  CA    . PRO   C 5   ? 0.36587 0.41513 0.53429 0.02460  0.06048  0.03118  4   PRO   C CA    
2740 C  C     . PRO   C 5   ? 0.40631 0.44975 0.56046 0.02115  0.05478  0.02125  4   PRO   C C     
2741 O  O     . PRO   C 5   ? 0.32970 0.37081 0.46761 0.02296  0.05676  0.01675  4   PRO   C O     
2742 C  CB    . PRO   C 5   ? 0.36175 0.41484 0.53959 0.02544  0.06264  0.03734  4   PRO   C CB    
2743 C  CG    . PRO   C 5   ? 0.38366 0.43834 0.54929 0.03157  0.07078  0.03952  4   PRO   C CG    
2744 C  CD    . PRO   C 5   ? 0.35416 0.40857 0.51307 0.03547  0.07492  0.03985  4   PRO   C CD    
2745 N  N     . THR   C 6   ? 0.37282 0.41360 0.53368 0.01646  0.04735  0.01817  5   THR   C N     
2746 C  CA    . THR   C 6   ? 0.38050 0.41612 0.53084 0.01328  0.04156  0.00999  5   THR   C CA    
2747 C  C     . THR   C 6   ? 0.35256 0.38759 0.51102 0.01066  0.03686  0.01065  5   THR   C C     
2748 O  O     . THR   C 6   ? 0.33380 0.37032 0.50848 0.00943  0.03421  0.01549  5   THR   C O     
2749 C  CB    . THR   C 6   ? 0.37653 0.40828 0.52517 0.01099  0.03660  0.00512  5   THR   C CB    
2750 O  OG1   . THR   C 6   ? 0.46091 0.49267 0.60022 0.01331  0.04060  0.00366  5   THR   C OG1   
2751 C  CG2   . THR   C 6   ? 0.42901 0.45572 0.56853 0.00831  0.03079  -0.00213 5   THR   C CG2   
2752 N  N     . VAL   C 7   ? 0.26651 0.29922 0.41442 0.00987  0.03550  0.00610  6   VAL   C N     
2753 C  CA    . VAL   C 7   ? 0.26714 0.29857 0.42104 0.00760  0.03066  0.00602  6   VAL   C CA    
2754 C  C     . VAL   C 7   ? 0.28590 0.31190 0.42779 0.00568  0.02555  -0.00183 6   VAL   C C     
2755 O  O     . VAL   C 7   ? 0.27634 0.30058 0.40581 0.00615  0.02672  -0.00637 6   VAL   C O     
2756 C  CB    . VAL   C 7   ? 0.35684 0.39191 0.51221 0.00920  0.03496  0.01019  6   VAL   C CB    
2757 C  CG1   . VAL   C 7   ? 0.31703 0.35790 0.48481 0.01193  0.04077  0.01903  6   VAL   C CG1   
2758 C  CG2   . VAL   C 7   ? 0.29667 0.33098 0.43499 0.01092  0.03873  0.00620  6   VAL   C CG2   
2759 N  N     . PHE   C 8   ? 0.27788 0.30115 0.42429 0.00381  0.01973  -0.00292 7   PHE   C N     
2760 C  CA    . PHE   C 8   ? 0.29676 0.31464 0.43219 0.00272  0.01483  -0.00976 7   PHE   C CA    
2761 C  C     . PHE   C 8   ? 0.27378 0.29061 0.40802 0.00220  0.01270  -0.01038 7   PHE   C C     
2762 O  O     . PHE   C 8   ? 0.29877 0.31766 0.44407 0.00188  0.01222  -0.00584 7   PHE   C O     
2763 C  CB    . PHE   C 8   ? 0.32573 0.33861 0.46562 0.00157  0.00765  -0.01211 7   PHE   C CB    
2764 C  CG    . PHE   C 8   ? 0.34131 0.35192 0.49453 0.00045  0.00117  -0.00962 7   PHE   C CG    
2765 C  CD1   . PHE   C 8   ? 0.36289 0.36878 0.51240 0.00016  -0.00439 -0.01283 7   PHE   C CD1   
2766 C  CD2   . PHE   C 8   ? 0.36838 0.38136 0.53830 -0.00011 0.00033  -0.00379 7   PHE   C CD2   
2767 C  CE1   . PHE   C 8   ? 0.40844 0.41145 0.57004 -0.00068 -0.01115 -0.01072 7   PHE   C CE1   
2768 C  CE2   . PHE   C 8   ? 0.38072 0.39122 0.56408 -0.00130 -0.00650 -0.00129 7   PHE   C CE2   
2769 C  CZ    . PHE   C 8   ? 0.37412 0.37931 0.55304 -0.00159 -0.01253 -0.00499 7   PHE   C CZ    
2770 N  N     . PHE   C 9   ? 0.26319 0.27708 0.38448 0.00225  0.01165  -0.01561 8   PHE   C N     
2771 C  CA    . PHE   C 9   ? 0.25800 0.27007 0.37669 0.00193  0.00901  -0.01695 8   PHE   C CA    
2772 C  C     . PHE   C 9   ? 0.28256 0.28836 0.39429 0.00203  0.00296  -0.02220 8   PHE   C C     
2773 O  O     . PHE   C 9   ? 0.29481 0.29936 0.39749 0.00258  0.00399  -0.02549 8   PHE   C O     
2774 C  CB    . PHE   C 9   ? 0.26888 0.28319 0.37679 0.00261  0.01390  -0.01818 8   PHE   C CB    
2775 C  CG    . PHE   C 9   ? 0.26347 0.28297 0.37416 0.00348  0.01994  -0.01374 8   PHE   C CG    
2776 C  CD1   . PHE   C 9   ? 0.27536 0.29818 0.39918 0.00376  0.02142  -0.00789 8   PHE   C CD1   
2777 C  CD2   . PHE   C 9   ? 0.30687 0.32766 0.40708 0.00441  0.02402  -0.01515 8   PHE   C CD2   
2778 C  CE1   . PHE   C 9   ? 0.28190 0.30929 0.40723 0.00545  0.02744  -0.00350 8   PHE   C CE1   
2779 C  CE2   . PHE   C 9   ? 0.33205 0.35666 0.43326 0.00598  0.02931  -0.01135 8   PHE   C CE2   
2780 C  CZ    . PHE   C 9   ? 0.28735 0.31529 0.40060 0.00675  0.03131  -0.00551 8   PHE   C CZ    
2781 N  N     . ASP   C 10  ? 0.29105 0.29268 0.40724 0.00191  -0.00337 -0.02268 9   ASP   C N     
2782 C  CA    . ASP   C 10  ? 0.31406 0.30889 0.42126 0.00322  -0.00900 -0.02773 9   ASP   C CA    
2783 C  C     . ASP   C 10  ? 0.32811 0.32314 0.42645 0.00391  -0.00745 -0.02926 9   ASP   C C     
2784 O  O     . ASP   C 10  ? 0.35264 0.34851 0.45663 0.00335  -0.00849 -0.02707 9   ASP   C O     
2785 C  CB    . ASP   C 10  ? 0.27681 0.26555 0.39201 0.00349  -0.01754 -0.02799 9   ASP   C CB    
2786 C  CG    . ASP   C 10  ? 0.40712 0.39411 0.52808 0.00324  -0.02002 -0.02783 9   ASP   C CG    
2787 O  OD1   . ASP   C 10  ? 0.41675 0.40394 0.52950 0.00389  -0.01725 -0.03026 9   ASP   C OD1   
2788 O  OD2   . ASP   C 10  ? 0.53508 0.52055 0.66938 0.00232  -0.02490 -0.02504 9   ASP   C OD2   
2789 N  N     . ILE   C 11  ? 0.31881 0.31352 0.40473 0.00501  -0.00486 -0.03240 10  ILE   C N     
2790 C  CA    . ILE   C 11  ? 0.27499 0.27074 0.35284 0.00558  -0.00255 -0.03333 10  ILE   C CA    
2791 C  C     . ILE   C 11  ? 0.29404 0.28348 0.36505 0.00797  -0.00784 -0.03645 10  ILE   C C     
2792 O  O     . ILE   C 11  ? 0.35594 0.34084 0.42265 0.00977  -0.01097 -0.03892 10  ILE   C O     
2793 C  CB    . ILE   C 11  ? 0.28560 0.28493 0.35521 0.00549  0.00329  -0.03413 10  ILE   C CB    
2794 C  CG1   . ILE   C 11  ? 0.28952 0.29387 0.36414 0.00410  0.00809  -0.03139 10  ILE   C CG1   
2795 C  CG2   . ILE   C 11  ? 0.27979 0.28014 0.34195 0.00600  0.00532  -0.03483 10  ILE   C CG2   
2796 C  CD1   . ILE   C 11  ? 0.29348 0.30146 0.37445 0.00335  0.01048  -0.02786 10  ILE   C CD1   
2797 N  N     . ALA   C 12  ? 0.29701 0.28598 0.36704 0.00832  -0.00879 -0.03614 11  ALA   C N     
2798 C  CA    . ALA   C 12  ? 0.34269 0.32559 0.40452 0.01136  -0.01321 -0.03898 11  ALA   C CA    
2799 C  C     . ALA   C 12  ? 0.37195 0.35737 0.42531 0.01209  -0.00907 -0.03925 11  ALA   C C     
2800 O  O     . ALA   C 12  ? 0.33396 0.32495 0.38982 0.00991  -0.00448 -0.03715 11  ALA   C O     
2801 C  CB    . ALA   C 12  ? 0.33366 0.31173 0.40223 0.01178  -0.02017 -0.03867 11  ALA   C CB    
2802 N  N     . VAL   C 13  ? 0.31361 0.29472 0.35675 0.01560  -0.01068 -0.04160 12  VAL   C N     
2803 C  CA    . VAL   C 13  ? 0.34710 0.33018 0.38250 0.01681  -0.00717 -0.04151 12  VAL   C CA    
2804 C  C     . VAL   C 13  ? 0.42673 0.40391 0.45782 0.02006  -0.01209 -0.04283 12  VAL   C C     
2805 O  O     . VAL   C 13  ? 0.41179 0.38225 0.43644 0.02415  -0.01635 -0.04503 12  VAL   C O     
2806 C  CB    . VAL   C 13  ? 0.39771 0.38176 0.42490 0.01866  -0.00363 -0.04212 12  VAL   C CB    
2807 C  CG1   . VAL   C 13  ? 0.42519 0.41126 0.44580 0.02010  -0.00037 -0.04131 12  VAL   C CG1   
2808 C  CG2   . VAL   C 13  ? 0.45477 0.44394 0.48618 0.01550  0.00046  -0.04107 12  VAL   C CG2   
2809 N  N     . ASP   C 14  ? 0.39842 0.37757 0.43248 0.01867  -0.01173 -0.04157 13  ASP   C N     
2810 C  CA    . ASP   C 14  ? 0.41918 0.39265 0.44978 0.02157  -0.01674 -0.04274 13  ASP   C CA    
2811 C  C     . ASP   C 14  ? 0.49692 0.46273 0.53100 0.02315  -0.02491 -0.04441 13  ASP   C C     
2812 O  O     . ASP   C 14  ? 0.49431 0.45221 0.52099 0.02772  -0.03041 -0.04679 13  ASP   C O     
2813 C  CB    . ASP   C 14  ? 0.44165 0.41278 0.45943 0.02618  -0.01529 -0.04390 13  ASP   C CB    
2814 C  CG    . ASP   C 14  ? 0.52014 0.49779 0.53616 0.02464  -0.00906 -0.04191 13  ASP   C CG    
2815 O  OD1   . ASP   C 14  ? 0.48173 0.46419 0.50505 0.02066  -0.00708 -0.04023 13  ASP   C OD1   
2816 O  OD2   . ASP   C 14  ? 0.59450 0.57239 0.60202 0.02772  -0.00618 -0.04172 13  ASP   C OD2   
2817 N  N     . GLY   C 15  ? 0.40730 0.37506 0.45263 0.01973  -0.02594 -0.04302 14  GLY   C N     
2818 C  CA    . GLY   C 15  ? 0.41197 0.37308 0.46352 0.02042  -0.03398 -0.04393 14  GLY   C CA    
2819 C  C     . GLY   C 15  ? 0.47274 0.42899 0.51977 0.02286  -0.03660 -0.04628 14  GLY   C C     
2820 O  O     . GLY   C 15  ? 0.54920 0.50052 0.60313 0.02278  -0.04315 -0.04674 14  GLY   C O     
2821 N  N     . GLU   C 16  ? 0.42682 0.38420 0.46340 0.02504  -0.03205 -0.04747 15  GLU   C N     
2822 C  CA    . GLU   C 16  ? 0.50417 0.45750 0.53516 0.02774  -0.03348 -0.04953 15  GLU   C CA    
2823 C  C     . GLU   C 16  ? 0.49948 0.45928 0.53797 0.02362  -0.02893 -0.04784 15  GLU   C C     
2824 O  O     . GLU   C 16  ? 0.44959 0.41728 0.48950 0.02073  -0.02185 -0.04581 15  GLU   C O     
2825 C  CB    . GLU   C 16  ? 0.50655 0.45861 0.52309 0.03243  -0.03008 -0.05081 15  GLU   C CB    
2826 C  CG    . GLU   C 16  ? 0.57275 0.51701 0.57949 0.03808  -0.03481 -0.05270 15  GLU   C CG    
2827 C  CD    . GLU   C 16  ? 0.60993 0.54376 0.61776 0.04075  -0.04506 -0.05530 15  GLU   C CD    
2828 O  OE1   . GLU   C 16  ? 0.70079 0.63100 0.71025 0.04123  -0.04838 -0.05659 15  GLU   C OE1   
2829 O  OE2   . GLU   C 16  ? 0.72711 0.65601 0.73456 0.04233  -0.05032 -0.05605 15  GLU   C OE2   
2830 N  N     . PRO   C 17  ? 0.44315 0.39941 0.48602 0.02358  -0.03303 -0.04870 16  PRO   C N     
2831 C  CA    . PRO   C 17  ? 0.40525 0.36750 0.45534 0.01991  -0.02876 -0.04697 16  PRO   C CA    
2832 C  C     . PRO   C 17  ? 0.48976 0.45617 0.53157 0.02043  -0.02203 -0.04731 16  PRO   C C     
2833 O  O     . PRO   C 17  ? 0.48168 0.44406 0.51309 0.02443  -0.02260 -0.04938 16  PRO   C O     
2834 C  CB    . PRO   C 17  ? 0.46345 0.41931 0.51827 0.02077  -0.03576 -0.04829 16  PRO   C CB    
2835 C  CG    . PRO   C 17  ? 0.47514 0.42341 0.53142 0.02284  -0.04407 -0.04939 16  PRO   C CG    
2836 C  CD    . PRO   C 17  ? 0.50798 0.45447 0.55196 0.02633  -0.04269 -0.05086 16  PRO   C CD    
2837 N  N     . LEU   C 18  ? 0.37324 0.34758 0.41983 0.01671  -0.01574 -0.04497 17  LEU   C N     
2838 C  CA    . LEU   C 18  ? 0.37882 0.35733 0.41982 0.01650  -0.00992 -0.04492 17  LEU   C CA    
2839 C  C     . LEU   C 18  ? 0.40636 0.38612 0.45179 0.01491  -0.00920 -0.04483 17  LEU   C C     
2840 O  O     . LEU   C 18  ? 0.43430 0.41198 0.47399 0.01683  -0.00919 -0.04638 17  LEU   C O     
2841 C  CB    . LEU   C 18  ? 0.34944 0.33478 0.39108 0.01403  -0.00403 -0.04283 17  LEU   C CB    
2842 C  CG    . LEU   C 18  ? 0.40967 0.39901 0.44629 0.01367  0.00123  -0.04256 17  LEU   C CG    
2843 C  CD1   . LEU   C 18  ? 0.42414 0.41077 0.45108 0.01741  0.00122  -0.04364 17  LEU   C CD1   
2844 C  CD2   . LEU   C 18  ? 0.37700 0.37225 0.41571 0.01099  0.00591  -0.04058 17  LEU   C CD2   
2845 N  N     . GLY   C 19  ? 0.35820 0.34119 0.41389 0.01181  -0.00861 -0.04275 18  GLY   C N     
2846 C  CA    . GLY   C 19  ? 0.34098 0.32545 0.40118 0.01044  -0.00759 -0.04233 18  GLY   C CA    
2847 C  C     . GLY   C 19  ? 0.31432 0.30346 0.38568 0.00755  -0.00549 -0.03902 18  GLY   C C     
2848 O  O     . GLY   C 19  ? 0.32646 0.31796 0.40210 0.00656  -0.00458 -0.03691 18  GLY   C O     
2849 N  N     . ARG   C 20  ? 0.35023 0.34079 0.42581 0.00661  -0.00436 -0.03832 19  ARG   C N     
2850 C  CA    . ARG   C 20  ? 0.31602 0.31112 0.40243 0.00465  -0.00184 -0.03446 19  ARG   C CA    
2851 C  C     . ARG   C 20  ? 0.31199 0.31230 0.39502 0.00405  0.00489  -0.03349 19  ARG   C C     
2852 O  O     . ARG   C 20  ? 0.34259 0.34233 0.41949 0.00447  0.00600  -0.03560 19  ARG   C O     
2853 C  CB    . ARG   C 20  ? 0.31775 0.31090 0.41396 0.00419  -0.00560 -0.03329 19  ARG   C CB    
2854 C  CG    . ARG   C 20  ? 0.29165 0.29006 0.39961 0.00275  -0.00223 -0.02838 19  ARG   C CG    
2855 C  CD    . ARG   C 20  ? 0.34296 0.33920 0.46320 0.00217  -0.00706 -0.02644 19  ARG   C CD    
2856 N  NE    . ARG   C 20  ? 0.38520 0.37706 0.51236 0.00208  -0.01410 -0.02606 19  ARG   C NE    
2857 C  CZ    . ARG   C 20  ? 0.41234 0.40313 0.55404 0.00115  -0.01868 -0.02275 19  ARG   C CZ    
2858 N  NH1   . ARG   C 20  ? 0.43335 0.42710 0.58397 0.00037  -0.01685 -0.01960 19  ARG   C NH1   
2859 N  NH2   . ARG   C 20  ? 0.41025 0.39690 0.55806 0.00108  -0.02532 -0.02235 19  ARG   C NH2   
2860 N  N     . VAL   C 21  ? 0.27758 0.28229 0.36415 0.00345  0.00887  -0.03038 20  VAL   C N     
2861 C  CA    . VAL   C 21  ? 0.26899 0.27767 0.35232 0.00361  0.01469  -0.02929 20  VAL   C CA    
2862 C  C     . VAL   C 21  ? 0.25076 0.26246 0.34459 0.00362  0.01674  -0.02492 20  VAL   C C     
2863 O  O     . VAL   C 21  ? 0.30408 0.31702 0.40656 0.00333  0.01599  -0.02169 20  VAL   C O     
2864 C  CB    . VAL   C 21  ? 0.24782 0.25874 0.32526 0.00389  0.01811  -0.02902 20  VAL   C CB    
2865 C  CG1   . VAL   C 21  ? 0.29392 0.30713 0.36609 0.00465  0.02279  -0.02875 20  VAL   C CG1   
2866 C  CG2   . VAL   C 21  ? 0.29428 0.30268 0.36391 0.00394  0.01590  -0.03216 20  VAL   C CG2   
2867 N  N     . SER   C 22  ? 0.24845 0.26123 0.34190 0.00410  0.01911  -0.02459 21  SER   C N     
2868 C  CA    . SER   C 22  ? 0.23521 0.25146 0.33792 0.00484  0.02225  -0.01975 21  SER   C CA    
2869 C  C     . SER   C 22  ? 0.25845 0.27738 0.35443 0.00680  0.02827  -0.01877 21  SER   C C     
2870 O  O     . SER   C 22  ? 0.27950 0.29692 0.36502 0.00708  0.02890  -0.02236 21  SER   C O     
2871 C  CB    . SER   C 22  ? 0.33319 0.34816 0.44298 0.00431  0.01962  -0.01935 21  SER   C CB    
2872 O  OG    . SER   C 22  ? 0.33460 0.34817 0.43591 0.00463  0.02039  -0.02275 21  SER   C OG    
2873 N  N     . PHE   C 23  ? 0.25503 0.27760 0.35772 0.00849  0.03233  -0.01355 22  PHE   C N     
2874 C  CA    . PHE   C 23  ? 0.26362 0.28800 0.35906 0.01151  0.03806  -0.01223 22  PHE   C CA    
2875 C  C     . PHE   C 23  ? 0.28001 0.30727 0.38200 0.01403  0.04216  -0.00727 22  PHE   C C     
2876 O  O     . PHE   C 23  ? 0.30532 0.33500 0.42052 0.01361  0.04191  -0.00261 22  PHE   C O     
2877 C  CB    . PHE   C 23  ? 0.23577 0.26213 0.33124 0.01265  0.04052  -0.00963 22  PHE   C CB    
2878 C  CG    . PHE   C 23  ? 0.24424 0.26863 0.33517 0.01051  0.03713  -0.01313 22  PHE   C CG    
2879 C  CD1   . PHE   C 23  ? 0.25961 0.28203 0.33822 0.01081  0.03738  -0.01708 22  PHE   C CD1   
2880 C  CD2   . PHE   C 23  ? 0.26866 0.29295 0.36802 0.00845  0.03345  -0.01219 22  PHE   C CD2   
2881 C  CE1   . PHE   C 23  ? 0.25313 0.27415 0.32823 0.00910  0.03469  -0.01966 22  PHE   C CE1   
2882 C  CE2   . PHE   C 23  ? 0.26990 0.29223 0.36446 0.00704  0.03060  -0.01524 22  PHE   C CE2   
2883 C  CZ    . PHE   C 23  ? 0.29766 0.31870 0.38024 0.00739  0.03159  -0.01878 22  PHE   C CZ    
2884 N  N     . GLU   C 24  ? 0.27712 0.30376 0.37022 0.01668  0.04541  -0.00826 23  GLU   C N     
2885 C  CA    . GLU   C 24  ? 0.26163 0.29100 0.35843 0.02045  0.05058  -0.00312 23  GLU   C CA    
2886 C  C     . GLU   C 24  ? 0.30496 0.33606 0.39748 0.02454  0.05575  0.00033  23  GLU   C C     
2887 O  O     . GLU   C 24  ? 0.27382 0.30239 0.35458 0.02532  0.05560  -0.00324 23  GLU   C O     
2888 C  CB    . GLU   C 24  ? 0.28216 0.30925 0.37062 0.02194  0.05124  -0.00599 23  GLU   C CB    
2889 C  CG    . GLU   C 24  ? 0.37275 0.40233 0.46242 0.02718  0.05748  -0.00046 23  GLU   C CG    
2890 C  CD    . GLU   C 24  ? 0.48432 0.51155 0.56606 0.02931  0.05836  -0.00275 23  GLU   C CD    
2891 O  OE1   . GLU   C 24  ? 0.47125 0.49476 0.54518 0.02688  0.05434  -0.00887 23  GLU   C OE1   
2892 O  OE2   . GLU   C 24  ? 0.49498 0.52423 0.57871 0.03373  0.06330  0.00206  23  GLU   C OE2   
2893 N  N     . LEU   C 25  ? 0.29822 0.33360 0.40098 0.02717  0.06008  0.00756  24  LEU   C N     
2894 C  CA    . LEU   C 25  ? 0.29305 0.33036 0.39249 0.03190  0.06567  0.01184  24  LEU   C CA    
2895 C  C     . LEU   C 25  ? 0.30555 0.34368 0.40090 0.03806  0.07173  0.01563  24  LEU   C C     
2896 O  O     . LEU   C 25  ? 0.31540 0.35649 0.42125 0.03872  0.07353  0.02023  24  LEU   C O     
2897 C  CB    . LEU   C 25  ? 0.24955 0.29143 0.36412 0.03100  0.06661  0.01820  24  LEU   C CB    
2898 C  CG    . LEU   C 25  ? 0.26378 0.30459 0.38478 0.02505  0.05991  0.01506  24  LEU   C CG    
2899 C  CD1   . LEU   C 25  ? 0.26312 0.30823 0.39967 0.02462  0.06070  0.02190  24  LEU   C CD1   
2900 C  CD2   . LEU   C 25  ? 0.24395 0.28077 0.35028 0.02377  0.05739  0.00815  24  LEU   C CD2   
2901 N  N     . PHE   C 26  ? 0.32578 0.36075 0.40559 0.04284  0.07447  0.01365  25  PHE   C N     
2902 C  CA    . PHE   C 26  ? 0.34746 0.38166 0.42027 0.04944  0.07956  0.01618  25  PHE   C CA    
2903 C  C     . PHE   C 26  ? 0.34159 0.38042 0.42040 0.05559  0.08711  0.02533  25  PHE   C C     
2904 O  O     . PHE   C 26  ? 0.32222 0.35931 0.38982 0.06206  0.09141  0.02677  25  PHE   C O     
2905 C  CB    . PHE   C 26  ? 0.39443 0.42197 0.44757 0.05228  0.07810  0.00974  25  PHE   C CB    
2906 C  CG    . PHE   C 26  ? 0.39319 0.41688 0.44193 0.04628  0.07101  0.00172  25  PHE   C CG    
2907 C  CD1   . PHE   C 26  ? 0.43252 0.45626 0.48603 0.04312  0.06846  -0.00009 25  PHE   C CD1   
2908 C  CD2   . PHE   C 26  ? 0.36121 0.38135 0.40132 0.04412  0.06712  -0.00354 25  PHE   C CD2   
2909 C  CE1   . PHE   C 26  ? 0.44579 0.46619 0.49527 0.03805  0.06234  -0.00695 25  PHE   C CE1   
2910 C  CE2   . PHE   C 26  ? 0.36561 0.38272 0.40251 0.03899  0.06109  -0.01000 25  PHE   C CE2   
2911 C  CZ    . PHE   C 26  ? 0.45791 0.47524 0.49946 0.03613  0.05892  -0.01154 25  PHE   C CZ    
2912 N  N     . ALA   C 27  ? 0.33656 0.38127 0.43407 0.05370  0.08850  0.03197  26  ALA   C N     
2913 C  CA    . ALA   C 27  ? 0.38684 0.43707 0.49337 0.05954  0.09614  0.04218  26  ALA   C CA    
2914 C  C     . ALA   C 27  ? 0.33301 0.38251 0.43055 0.06800  0.10274  0.04558  26  ALA   C C     
2915 O  O     . ALA   C 27  ? 0.37932 0.43161 0.47675 0.07531  0.11012  0.05303  26  ALA   C O     
2916 C  CB    . ALA   C 27  ? 0.38731 0.44367 0.51754 0.05528  0.09518  0.04870  26  ALA   C CB    
2917 N  N     . ASP   C 28  ? 0.37699 0.42238 0.46579 0.06774  0.10031  0.04020  27  ASP   C N     
2918 C  CA    . ASP   C 28  ? 0.42067 0.46414 0.49843 0.07629  0.10601  0.04253  27  ASP   C CA    
2919 C  C     . ASP   C 28  ? 0.44544 0.48286 0.50180 0.08335  0.10799  0.03942  27  ASP   C C     
2920 O  O     . ASP   C 28  ? 0.48850 0.52391 0.53460 0.09221  0.11344  0.04237  27  ASP   C O     
2921 C  CB    . ASP   C 28  ? 0.43196 0.47235 0.50629 0.07400  0.10241  0.03745  27  ASP   C CB    
2922 C  CG    . ASP   C 28  ? 0.48215 0.51653 0.54649 0.06775  0.09410  0.02665  27  ASP   C CG    
2923 O  OD1   . ASP   C 28  ? 0.46739 0.50038 0.52958 0.06383  0.09029  0.02277  27  ASP   C OD1   
2924 O  OD2   . ASP   C 28  ? 0.65943 0.69057 0.71840 0.06679  0.09140  0.02221  27  ASP   C OD2   
2925 N  N     . LYS   C 29  ? 0.41343 0.44741 0.46242 0.08010  0.10350  0.03361  28  LYS   C N     
2926 C  CA    . LYS   C 29  ? 0.40430 0.43198 0.43385 0.08623  0.10421  0.03038  28  LYS   C CA    
2927 C  C     . LYS   C 29  ? 0.39782 0.42776 0.42965 0.08694  0.10624  0.03346  28  LYS   C C     
2928 O  O     . LYS   C 29  ? 0.37564 0.40256 0.39493 0.09505  0.11035  0.03526  28  LYS   C O     
2929 C  CB    . LYS   C 29  ? 0.46966 0.48966 0.48570 0.08215  0.09612  0.01964  28  LYS   C CB    
2930 C  CG    . LYS   C 29  ? 0.48656 0.50237 0.49476 0.08420  0.09476  0.01638  28  LYS   C CG    
2931 C  CD    . LYS   C 29  ? 0.49823 0.50574 0.49150 0.08211  0.08737  0.00681  28  LYS   C CD    
2932 C  CE    . LYS   C 29  ? 0.61256 0.61580 0.59877 0.08369  0.08540  0.00343  28  LYS   C CE    
2933 N  NZ    . LYS   C 29  ? 0.62909 0.63755 0.63031 0.07704  0.08427  0.00417  28  LYS   C NZ    
2934 N  N     . VAL   C 30  ? 0.34480 0.37949 0.39166 0.07913  0.10332  0.03406  29  VAL   C N     
2935 C  CA    . VAL   C 30  ? 0.34588 0.38306 0.39616 0.07935  0.10505  0.03715  29  VAL   C CA    
2936 C  C     . VAL   C 30  ? 0.36626 0.41180 0.43978 0.07504  0.10654  0.04451  29  VAL   C C     
2937 O  O     . VAL   C 30  ? 0.31218 0.35916 0.39462 0.06758  0.10143  0.04211  29  VAL   C O     
2938 C  CB    . VAL   C 30  ? 0.36562 0.39804 0.40716 0.07412  0.09820  0.02867  29  VAL   C CB    
2939 C  CG1   . VAL   C 30  ? 0.36083 0.38556 0.38070 0.08080  0.09838  0.02444  29  VAL   C CG1   
2940 C  CG2   . VAL   C 30  ? 0.37709 0.40797 0.42196 0.06563  0.09070  0.02173  29  VAL   C CG2   
2941 N  N     . PRO   C 31  ? 0.34696 0.39788 0.43079 0.08008  0.11343  0.05396  30  PRO   C N     
2942 C  CA    . PRO   C 31  ? 0.34660 0.40531 0.45490 0.07568  0.11394  0.06144  30  PRO   C CA    
2943 C  C     . PRO   C 31  ? 0.33425 0.39598 0.45121 0.07277  0.11314  0.06390  30  PRO   C C     
2944 O  O     . PRO   C 31  ? 0.30457 0.36904 0.43737 0.06524  0.10799  0.06399  30  PRO   C O     
2945 C  CB    . PRO   C 31  ? 0.31200 0.37570 0.42697 0.08395  0.12311  0.07227  30  PRO   C CB    
2946 C  CG    . PRO   C 31  ? 0.35013 0.40864 0.44222 0.09404  0.12846  0.07118  30  PRO   C CG    
2947 C  CD    . PRO   C 31  ? 0.33230 0.38204 0.40575 0.09046  0.12082  0.05840  30  PRO   C CD    
2948 N  N     . LYS   C 32  ? 0.31081 0.37157 0.41723 0.07891  0.11779  0.06577  31  LYS   C N     
2949 C  CA    . LYS   C 32  ? 0.34124 0.40554 0.45684 0.07690  0.11800  0.06934  31  LYS   C CA    
2950 C  C     . LYS   C 32  ? 0.35523 0.41571 0.46754 0.06847  0.10919  0.05996  31  LYS   C C     
2951 O  O     . LYS   C 32  ? 0.29206 0.35587 0.41884 0.06282  0.10594  0.06170  31  LYS   C O     
2952 C  CB    . LYS   C 32  ? 0.43717 0.50102 0.54113 0.08627  0.12549  0.07372  31  LYS   C CB    
2953 C  CG    . LYS   C 32  ? 0.44521 0.51292 0.55847 0.08459  0.12617  0.07778  31  LYS   C CG    
2954 C  CD    . LYS   C 32  ? 0.49565 0.56472 0.60175 0.09492  0.13525  0.08513  31  LYS   C CD    
2955 C  CE    . LYS   C 32  ? 0.47046 0.54440 0.58931 0.09237  0.13575  0.09002  31  LYS   C CE    
2956 N  NZ    . LYS   C 32  ? 0.54287 0.61732 0.65282 0.10194  0.14378  0.09590  31  LYS   C NZ    
2957 N  N     . THR   C 33  ? 0.29162 0.34499 0.38565 0.06757  0.10494  0.05020  32  THR   C N     
2958 C  CA    . THR   C 33  ? 0.32630 0.37620 0.41677 0.06021  0.09714  0.04179  32  THR   C CA    
2959 C  C     . THR   C 33  ? 0.27322 0.32391 0.37550 0.05231  0.09074  0.03883  32  THR   C C     
2960 O  O     . THR   C 33  ? 0.26324 0.31419 0.37252 0.04601  0.08530  0.03621  32  THR   C O     
2961 C  CB    . THR   C 33  ? 0.32860 0.37090 0.39707 0.06225  0.09483  0.03339  32  THR   C CB    
2962 O  OG1   . THR   C 33  ? 0.29477 0.33530 0.35115 0.07071  0.10057  0.03625  32  THR   C OG1   
2963 C  CG2   . THR   C 33  ? 0.31014 0.34954 0.37562 0.05531  0.08766  0.02589  32  THR   C CG2   
2964 N  N     . ALA   C 34  ? 0.27624 0.32681 0.37995 0.05306  0.09122  0.03912  33  ALA   C N     
2965 C  CA    . ALA   C 34  ? 0.29612 0.34727 0.41132 0.04636  0.08542  0.03695  33  ALA   C CA    
2966 C  C     . ALA   C 34  ? 0.32058 0.37732 0.45745 0.04332  0.08478  0.04390  33  ALA   C C     
2967 O  O     . ALA   C 34  ? 0.28389 0.33978 0.42855 0.03691  0.07801  0.04072  33  ALA   C O     
2968 C  CB    . ALA   C 34  ? 0.30332 0.35373 0.41668 0.04845  0.08686  0.03698  33  ALA   C CB    
2969 N  N     . GLU   C 35  ? 0.32308 0.38527 0.46997 0.04824  0.09160  0.05372  34  GLU   C N     
2970 C  CA    . GLU   C 35  ? 0.31619 0.38388 0.48578 0.04539  0.09068  0.06127  34  GLU   C CA    
2971 C  C     . GLU   C 35  ? 0.30494 0.37210 0.47734 0.04123  0.08635  0.05920  34  GLU   C C     
2972 O  O     . GLU   C 35  ? 0.31055 0.37851 0.49778 0.03567  0.08031  0.05978  34  GLU   C O     
2973 C  CB    . GLU   C 35  ? 0.30365 0.37776 0.48310 0.05226  0.09978  0.07310  34  GLU   C CB    
2974 C  CG    . GLU   C 35  ? 0.36709 0.44728 0.57125 0.04966  0.09907  0.08202  34  GLU   C CG    
2975 C  CD    . GLU   C 35  ? 0.38800 0.46872 0.61003 0.04337  0.09205  0.08238  34  GLU   C CD    
2976 O  OE1   . GLU   C 35  ? 0.45853 0.53616 0.67515 0.04205  0.08953  0.07745  34  GLU   C OE1   
2977 O  OE2   . GLU   C 35  ? 0.51704 0.60086 0.75877 0.03979  0.08854  0.08758  34  GLU   C OE2   
2978 N  N     . ASN   C 36  ? 0.26633 0.33172 0.42461 0.04412  0.08899  0.05683  35  ASN   C N     
2979 C  CA    . ASN   C 36  ? 0.27419 0.33882 0.43362 0.04035  0.08501  0.05440  35  ASN   C CA    
2980 C  C     . ASN   C 36  ? 0.27950 0.33968 0.43808 0.03307  0.07568  0.04591  35  ASN   C C     
2981 O  O     . ASN   C 36  ? 0.27220 0.33287 0.44228 0.02855  0.07049  0.04633  35  ASN   C O     
2982 C  CB    . ASN   C 36  ? 0.31326 0.37517 0.45426 0.04433  0.08832  0.05113  35  ASN   C CB    
2983 C  CG    . ASN   C 36  ? 0.32886 0.39022 0.47088 0.04070  0.08466  0.04890  35  ASN   C CG    
2984 O  OD1   . ASN   C 36  ? 0.33437 0.39996 0.49209 0.03934  0.08468  0.05501  35  ASN   C OD1   
2985 N  ND2   . ASN   C 36  ? 0.27285 0.32900 0.39892 0.03902  0.08121  0.04036  35  ASN   C ND2   
2986 N  N     . PHE   C 37  ? 0.28743 0.34284 0.43189 0.03229  0.07335  0.03822  36  PHE   C N     
2987 C  CA    . PHE   C 37  ? 0.27472 0.32566 0.41631 0.02623  0.06509  0.03013  36  PHE   C CA    
2988 C  C     . PHE   C 37  ? 0.33930 0.39112 0.49702 0.02259  0.06044  0.03213  36  PHE   C C     
2989 O  O     . PHE   C 37  ? 0.28370 0.33330 0.44678 0.01806  0.05361  0.02917  36  PHE   C O     
2990 C  CB    . PHE   C 37  ? 0.30091 0.34707 0.42460 0.02676  0.06430  0.02247  36  PHE   C CB    
2991 C  CG    . PHE   C 37  ? 0.24110 0.28271 0.35861 0.02177  0.05720  0.01433  36  PHE   C CG    
2992 C  CD1   . PHE   C 37  ? 0.25794 0.29723 0.36571 0.02079  0.05559  0.01004  36  PHE   C CD1   
2993 C  CD2   . PHE   C 37  ? 0.23833 0.27796 0.35952 0.01856  0.05243  0.01132  36  PHE   C CD2   
2994 C  CE1   . PHE   C 37  ? 0.26546 0.30099 0.36781 0.01693  0.04981  0.00345  36  PHE   C CE1   
2995 C  CE2   . PHE   C 37  ? 0.23829 0.27380 0.35318 0.01497  0.04662  0.00449  36  PHE   C CE2   
2996 C  CZ    . PHE   C 37  ? 0.27759 0.31126 0.38323 0.01429  0.04556  0.00082  36  PHE   C CZ    
2997 N  N     . ARG   C 38  ? 0.32660 0.38115 0.49129 0.02504  0.06399  0.03710  37  ARG   C N     
2998 C  CA    . ARG   C 38  ? 0.30346 0.35871 0.48441 0.02178  0.05937  0.03947  37  ARG   C CA    
2999 C  C     . ARG   C 38  ? 0.36192 0.41947 0.56072 0.01915  0.05583  0.04455  37  ARG   C C     
3000 O  O     . ARG   C 38  ? 0.30302 0.35726 0.50830 0.01463  0.04769  0.04134  37  ARG   C O     
3001 C  CB    . ARG   C 38  ? 0.27590 0.33488 0.46363 0.02542  0.06484  0.04581  37  ARG   C CB    
3002 C  CG    . ARG   C 38  ? 0.32747 0.38596 0.52909 0.02192  0.05942  0.04659  37  ARG   C CG    
3003 C  CD    . ARG   C 38  ? 0.31949 0.38371 0.53550 0.02539  0.06511  0.05639  37  ARG   C CD    
3004 N  NE    . ARG   C 38  ? 0.37563 0.44578 0.60613 0.02764  0.06944  0.06623  37  ARG   C NE    
3005 C  CZ    . ARG   C 38  ? 0.40277 0.47442 0.65200 0.02403  0.06432  0.07041  37  ARG   C CZ    
3006 N  NH1   . ARG   C 38  ? 0.38072 0.44817 0.63714 0.01859  0.05472  0.06615  37  ARG   C NH1   
3007 N  NH2   . ARG   C 38  ? 0.45861 0.53567 0.71942 0.02627  0.06864  0.07910  37  ARG   C NH2   
3008 N  N     . ALA   C 39  ? 0.29685 0.35959 0.50319 0.02234  0.06164  0.05249  38  ALA   C N     
3009 C  CA    . ALA   C 39  ? 0.39302 0.45848 0.61830 0.02006  0.05850  0.05847  38  ALA   C CA    
3010 C  C     . ALA   C 39  ? 0.35787 0.41901 0.57790 0.01620  0.05185  0.05211  38  ALA   C C     
3011 O  O     . ALA   C 39  ? 0.39512 0.45487 0.62854 0.01244  0.04461  0.05290  38  ALA   C O     
3012 C  CB    . ALA   C 39  ? 0.39470 0.46705 0.62821 0.02498  0.06718  0.06880  38  ALA   C CB    
3013 N  N     . LEU   C 40  ? 0.29101 0.34964 0.49192 0.01729  0.05381  0.04593  39  LEU   C N     
3014 C  CA    . LEU   C 40  ? 0.29313 0.34779 0.48837 0.01397  0.04794  0.04000  39  LEU   C CA    
3015 C  C     . LEU   C 40  ? 0.33720 0.38581 0.52976 0.00986  0.03921  0.03255  39  LEU   C C     
3016 O  O     . LEU   C 40  ? 0.33668 0.38188 0.53120 0.00693  0.03253  0.02950  39  LEU   C O     
3017 C  CB    . LEU   C 40  ? 0.31782 0.37123 0.49367 0.01622  0.05210  0.03542  39  LEU   C CB    
3018 C  CG    . LEU   C 40  ? 0.34033 0.39847 0.51652 0.02068  0.05994  0.04193  39  LEU   C CG    
3019 C  CD1   . LEU   C 40  ? 0.30177 0.35747 0.45734 0.02335  0.06344  0.03674  39  LEU   C CD1   
3020 C  CD2   . LEU   C 40  ? 0.39118 0.45176 0.58101 0.01898  0.05791  0.04664  39  LEU   C CD2   
3021 N  N     . SER   C 41  ? 0.34433 0.39138 0.53219 0.01012  0.03928  0.02986  40  SER   C N     
3022 C  CA    . SER   C 41  ? 0.30055 0.34171 0.48487 0.00696  0.03154  0.02297  40  SER   C CA    
3023 C  C     . SER   C 41  ? 0.38060 0.42082 0.58366 0.00457  0.02484  0.02644  40  SER   C C     
3024 O  O     . SER   C 41  ? 0.34000 0.37445 0.54188 0.00208  0.01675  0.02131  40  SER   C O     
3025 C  CB    . SER   C 41  ? 0.30004 0.33970 0.47201 0.00811  0.03394  0.01866  40  SER   C CB    
3026 O  OG    . SER   C 41  ? 0.31883 0.35878 0.47475 0.01039  0.03919  0.01579  40  SER   C OG    
3027 N  N     . THR   C 42  ? 0.34841 0.39377 0.56832 0.00565  0.02782  0.03514  41  THR   C N     
3028 C  CA    . THR   C 42  ? 0.41150 0.45573 0.65112 0.00314  0.02052  0.03894  41  THR   C CA    
3029 C  C     . THR   C 42  ? 0.41855 0.46305 0.67004 0.00164  0.01644  0.04247  41  THR   C C     
3030 O  O     . THR   C 42  ? 0.49152 0.53199 0.75507 -0.00100 0.00732  0.04254  41  THR   C O     
3031 C  CB    . THR   C 42  ? 0.40134 0.45111 0.65701 0.00464  0.02464  0.04764  41  THR   C CB    
3032 O  OG1   . THR   C 42  ? 0.43866 0.49573 0.70102 0.00773  0.03306  0.05615  41  THR   C OG1   
3033 C  CG2   . THR   C 42  ? 0.39297 0.44222 0.63852 0.00610  0.02805  0.04451  41  THR   C CG2   
3034 N  N     . GLY   C 43  ? 0.39622 0.44493 0.64476 0.00346  0.02258  0.04548  42  GLY   C N     
3035 C  CA    . GLY   C 43  ? 0.41861 0.46842 0.67942 0.00225  0.01955  0.04975  42  GLY   C CA    
3036 C  C     . GLY   C 43  ? 0.38183 0.43815 0.66682 0.00293  0.02182  0.06150  42  GLY   C C     
3037 O  O     . GLY   C 43  ? 0.42794 0.48533 0.72599 0.00169  0.01866  0.06593  42  GLY   C O     
3038 N  N     . GLU   C 44  ? 0.43128 0.49220 0.72277 0.00512  0.02752  0.06709  43  GLU   C N     
3039 C  CA    . GLU   C 44  ? 0.41633 0.48347 0.73296 0.00576  0.02920  0.07894  43  GLU   C CA    
3040 C  C     . GLU   C 44  ? 0.41708 0.49141 0.74208 0.00854  0.03656  0.08796  43  GLU   C C     
3041 O  O     . GLU   C 44  ? 0.48803 0.56791 0.83618 0.00898  0.03763  0.09881  43  GLU   C O     
3042 C  CB    . GLU   C 44  ? 0.45154 0.52201 0.76985 0.00826  0.03489  0.08235  43  GLU   C CB    
3043 C  CG    . GLU   C 44  ? 0.42997 0.50356 0.72907 0.01329  0.04616  0.08133  43  GLU   C CG    
3044 C  CD    . GLU   C 44  ? 0.50987 0.58558 0.80847 0.01588  0.05099  0.08353  43  GLU   C CD    
3045 O  OE1   . GLU   C 44  ? 0.53647 0.60701 0.82915 0.01339  0.04547  0.07659  43  GLU   C OE1   
3046 O  OE2   . GLU   C 44  ? 0.52436 0.60681 0.82837 0.02077  0.06040  0.09242  43  GLU   C OE2   
3047 N  N     . LYS   C 45  ? 0.45589 0.53036 0.76369 0.01057  0.04158  0.08432  44  LYS   C N     
3048 C  CA    . LYS   C 45  ? 0.47355 0.55398 0.78832 0.01317  0.04774  0.09221  44  LYS   C CA    
3049 C  C     . LYS   C 45  ? 0.44692 0.52428 0.76683 0.00949  0.04007  0.09017  44  LYS   C C     
3050 O  O     . LYS   C 45  ? 0.54700 0.62883 0.87268 0.01116  0.04426  0.09615  44  LYS   C O     
3051 C  CB    . LYS   C 45  ? 0.45090 0.53320 0.74419 0.01828  0.05801  0.09020  44  LYS   C CB    
3052 C  CG    . LYS   C 45  ? 0.49312 0.57737 0.77730 0.02279  0.06575  0.09117  44  LYS   C CG    
3053 C  CD    . LYS   C 45  ? 0.36074 0.45295 0.66403 0.02682  0.07288  0.10438  44  LYS   C CD    
3054 C  CE    . LYS   C 45  ? 0.43183 0.52459 0.72603 0.03079  0.07872  0.10414  44  LYS   C CE    
3055 N  NZ    . LYS   C 45  ? 0.51656 0.61732 0.82677 0.03606  0.08729  0.11734  44  LYS   C NZ    
3056 N  N     . GLY   C 46  ? 0.40582 0.47540 0.72318 0.00501  0.02900  0.08198  45  GLY   C N     
3057 C  CA    . GLY   C 46  ? 0.38706 0.45259 0.70664 0.00203  0.02131  0.07906  45  GLY   C CA    
3058 C  C     . GLY   C 46  ? 0.42746 0.48862 0.72281 0.00210  0.02166  0.06922  45  GLY   C C     
3059 O  O     . GLY   C 46  ? 0.43674 0.49442 0.73220 0.00002  0.01570  0.06647  45  GLY   C O     
3060 N  N     . PHE   C 47  ? 0.40493 0.46609 0.68013 0.00455  0.02827  0.06415  46  PHE   C N     
3061 C  CA    . PHE   C 47  ? 0.41220 0.46903 0.66467 0.00450  0.02828  0.05472  46  PHE   C CA    
3062 C  C     . PHE   C 47  ? 0.35459 0.40930 0.59032 0.00577  0.03118  0.04861  46  PHE   C C     
3063 O  O     . PHE   C 47  ? 0.35761 0.41490 0.59840 0.00724  0.03450  0.05216  46  PHE   C O     
3064 C  CB    . PHE   C 47  ? 0.39450 0.45555 0.64105 0.00715  0.03566  0.05754  46  PHE   C CB    
3065 C  CG    . PHE   C 47  ? 0.43674 0.50474 0.68499 0.01200  0.04656  0.06522  46  PHE   C CG    
3066 C  CD1   . PHE   C 47  ? 0.42204 0.48967 0.65216 0.01529  0.05285  0.06145  46  PHE   C CD1   
3067 C  CD2   . PHE   C 47  ? 0.41445 0.48906 0.68252 0.01374  0.05037  0.07654  46  PHE   C CD2   
3068 C  CE1   . PHE   C 47  ? 0.38217 0.45521 0.61222 0.02076  0.06269  0.06838  46  PHE   C CE1   
3069 C  CE2   . PHE   C 47  ? 0.45894 0.53981 0.72784 0.01927  0.06096  0.08418  46  PHE   C CE2   
3070 C  CZ    . PHE   C 47  ? 0.46765 0.54739 0.71676 0.02304  0.06708  0.07988  46  PHE   C CZ    
3071 N  N     . GLY   C 48  ? 0.36396 0.41402 0.58032 0.00523  0.02982  0.03969  47  GLY   C N     
3072 C  CA    . GLY   C 48  ? 0.36821 0.41585 0.57008 0.00602  0.03145  0.03389  47  GLY   C CA    
3073 C  C     . GLY   C 48  ? 0.31252 0.35402 0.49765 0.00434  0.02687  0.02426  47  GLY   C C     
3074 O  O     . GLY   C 48  ? 0.31553 0.35511 0.49776 0.00324  0.02393  0.02203  47  GLY   C O     
3075 N  N     . TYR   C 49  ? 0.32919 0.36789 0.50377 0.00441  0.02657  0.01904  48  TYR   C N     
3076 C  CA    . TYR   C 49  ? 0.34786 0.38158 0.50556 0.00356  0.02383  0.01059  48  TYR   C CA    
3077 C  C     . TYR   C 49  ? 0.36192 0.38967 0.52090 0.00126  0.01482  0.00626  48  TYR   C C     
3078 O  O     . TYR   C 49  ? 0.32069 0.34488 0.46726 0.00100  0.01282  0.00058  48  TYR   C O     
3079 C  CB    . TYR   C 49  ? 0.30982 0.34303 0.45782 0.00468  0.02683  0.00761  48  TYR   C CB    
3080 C  CG    . TYR   C 49  ? 0.29937 0.33653 0.44084 0.00780  0.03515  0.01005  48  TYR   C CG    
3081 C  CD1   . TYR   C 49  ? 0.32182 0.36036 0.45577 0.00932  0.03896  0.01021  48  TYR   C CD1   
3082 C  CD2   . TYR   C 49  ? 0.30874 0.34755 0.45075 0.00965  0.03882  0.01198  48  TYR   C CD2   
3083 C  CE1   . TYR   C 49  ? 0.31785 0.35868 0.44443 0.01292  0.04583  0.01205  48  TYR   C CE1   
3084 C  CE2   . TYR   C 49  ? 0.29557 0.33684 0.43010 0.01335  0.04592  0.01391  48  TYR   C CE2   
3085 C  CZ    . TYR   C 49  ? 0.29320 0.33516 0.41969 0.01516  0.04924  0.01385  48  TYR   C CZ    
3086 O  OH    . TYR   C 49  ? 0.27716 0.32033 0.39503 0.01951  0.05557  0.01544  48  TYR   C OH    
3087 N  N     . LYS   C 50  ? 0.35427 0.38060 0.52767 0.00003  0.00933  0.00903  49  LYS   C N     
3088 C  CA    . LYS   C 50  ? 0.39550 0.41460 0.56760 -0.00126 0.00011  0.00410  49  LYS   C CA    
3089 C  C     . LYS   C 50  ? 0.32211 0.33869 0.48898 -0.00149 -0.00273 0.00169  49  LYS   C C     
3090 O  O     . LYS   C 50  ? 0.38576 0.40562 0.56068 -0.00176 -0.00133 0.00613  49  LYS   C O     
3091 C  CB    . LYS   C 50  ? 0.40352 0.42084 0.59347 -0.00247 -0.00642 0.00791  49  LYS   C CB    
3092 C  CG    . LYS   C 50  ? 0.39533 0.40373 0.58344 -0.00302 -0.01695 0.00267  49  LYS   C CG    
3093 C  CD    . LYS   C 50  ? 0.47048 0.47683 0.67681 -0.00418 -0.02371 0.00656  49  LYS   C CD    
3094 C  CE    . LYS   C 50  ? 0.49756 0.49365 0.70193 -0.00405 -0.03534 0.00133  49  LYS   C CE    
3095 N  NZ    . LYS   C 50  ? 0.45931 0.45267 0.68084 -0.00514 -0.04247 0.00465  49  LYS   C NZ    
3096 N  N     . GLY   C 51  ? 0.32477 0.33582 0.47776 -0.00103 -0.00616 -0.00506 50  GLY   C N     
3097 C  CA    . GLY   C 51  ? 0.37788 0.38628 0.52438 -0.00080 -0.00863 -0.00765 50  GLY   C CA    
3098 C  C     . GLY   C 51  ? 0.36068 0.37259 0.49485 -0.00013 -0.00175 -0.00907 50  GLY   C C     
3099 O  O     . GLY   C 51  ? 0.40188 0.41112 0.52789 0.00029  -0.00358 -0.01220 50  GLY   C O     
3100 N  N     . SER   C 52  ? 0.33332 0.35061 0.46559 0.00028  0.00576  -0.00691 51  SER   C N     
3101 C  CA    . SER   C 52  ? 0.30837 0.32844 0.42997 0.00104  0.01154  -0.00793 51  SER   C CA    
3102 C  C     . SER   C 52  ? 0.34052 0.35791 0.44754 0.00156  0.01189  -0.01356 51  SER   C C     
3103 O  O     . SER   C 52  ? 0.31653 0.33072 0.42162 0.00161  0.00890  -0.01618 51  SER   C O     
3104 C  CB    . SER   C 52  ? 0.31194 0.33792 0.43694 0.00209  0.01892  -0.00313 51  SER   C CB    
3105 O  OG    . SER   C 52  ? 0.34327 0.36975 0.46514 0.00282  0.02145  -0.00385 51  SER   C OG    
3106 N  N     . CYS   C 53  ? 0.31153 0.33035 0.40883 0.00205  0.01561  -0.01505 52  CYS   C N     
3107 C  CA    . CYS   C 53  ? 0.31026 0.32671 0.39527 0.00245  0.01545  -0.01969 52  CYS   C CA    
3108 C  C     . CYS   C 53  ? 0.31228 0.33143 0.39041 0.00303  0.02094  -0.01988 52  CYS   C C     
3109 O  O     . CYS   C 53  ? 0.30845 0.33095 0.38877 0.00370  0.02524  -0.01681 52  CYS   C O     
3110 C  CB    . CYS   C 53  ? 0.35785 0.37227 0.43703 0.00260  0.01334  -0.02183 52  CYS   C CB    
3111 S  SG    . CYS   C 53  ? 0.51130 0.52929 0.58567 0.00265  0.01823  -0.02070 52  CYS   C SG    
3112 N  N     . PHE   C 54  ? 0.31472 0.33194 0.38428 0.00320  0.02049  -0.02339 53  PHE   C N     
3113 C  CA    . PHE   C 54  ? 0.30500 0.32369 0.36711 0.00370  0.02438  -0.02420 53  PHE   C CA    
3114 C  C     . PHE   C 54  ? 0.30410 0.32276 0.36026 0.00362  0.02468  -0.02527 53  PHE   C C     
3115 O  O     . PHE   C 54  ? 0.31889 0.33551 0.37087 0.00352  0.02229  -0.02751 53  PHE   C O     
3116 C  CB    . PHE   C 54  ? 0.32087 0.33779 0.37862 0.00373  0.02350  -0.02677 53  PHE   C CB    
3117 C  CG    . PHE   C 54  ? 0.28790 0.30545 0.35024 0.00397  0.02445  -0.02556 53  PHE   C CG    
3118 C  CD1   . PHE   C 54  ? 0.26520 0.28137 0.33460 0.00359  0.02137  -0.02507 53  PHE   C CD1   
3119 C  CD2   . PHE   C 54  ? 0.27055 0.28957 0.32991 0.00486  0.02806  -0.02493 53  PHE   C CD2   
3120 C  CE1   . PHE   C 54  ? 0.27133 0.28833 0.34555 0.00378  0.02233  -0.02365 53  PHE   C CE1   
3121 C  CE2   . PHE   C 54  ? 0.30366 0.32328 0.36691 0.00543  0.02919  -0.02363 53  PHE   C CE2   
3122 C  CZ    . PHE   C 54  ? 0.30619 0.32517 0.37727 0.00473  0.02655  -0.02283 53  PHE   C CZ    
3123 N  N     . HIS   C 55  ? 0.27830 0.29911 0.33404 0.00407  0.02768  -0.02342 54  HIS   C N     
3124 C  CA    . HIS   C 55  ? 0.28806 0.30895 0.33946 0.00390  0.02777  -0.02404 54  HIS   C CA    
3125 C  C     . HIS   C 55  ? 0.31548 0.33587 0.35867 0.00409  0.02888  -0.02592 54  HIS   C C     
3126 O  O     . HIS   C 55  ? 0.33312 0.35326 0.37277 0.00375  0.02830  -0.02670 54  HIS   C O     
3127 C  CB    . HIS   C 55  ? 0.29554 0.31870 0.35059 0.00446  0.03015  -0.02099 54  HIS   C CB    
3128 C  CG    . HIS   C 55  ? 0.33643 0.36118 0.39060 0.00621  0.03424  -0.01895 54  HIS   C CG    
3129 N  ND1   . HIS   C 55  ? 0.31013 0.33614 0.37017 0.00713  0.03581  -0.01646 54  HIS   C ND1   
3130 C  CD2   . HIS   C 55  ? 0.35785 0.38267 0.40553 0.00779  0.03694  -0.01888 54  HIS   C CD2   
3131 C  CE1   . HIS   C 55  ? 0.32337 0.35022 0.37985 0.00959  0.03976  -0.01487 54  HIS   C CE1   
3132 N  NE2   . HIS   C 55  ? 0.34197 0.36774 0.39057 0.01014  0.04024  -0.01649 54  HIS   C NE2   
3133 N  N     . ARG   C 56  ? 0.28880 0.30883 0.32940 0.00464  0.03010  -0.02649 55  ARG   C N     
3134 C  CA    . ARG   C 56  ? 0.28643 0.30548 0.32027 0.00486  0.03043  -0.02798 55  ARG   C CA    
3135 C  C     . ARG   C 56  ? 0.27521 0.29307 0.30776 0.00468  0.02950  -0.02946 55  ARG   C C     
3136 O  O     . ARG   C 56  ? 0.28150 0.29926 0.31491 0.00557  0.03073  -0.02902 55  ARG   C O     
3137 C  CB    . ARG   C 56  ? 0.31674 0.33579 0.34738 0.00661  0.03292  -0.02691 55  ARG   C CB    
3138 C  CG    . ARG   C 56  ? 0.36699 0.38403 0.39095 0.00689  0.03200  -0.02855 55  ARG   C CG    
3139 C  CD    . ARG   C 56  ? 0.32925 0.34489 0.34847 0.00968  0.03401  -0.02782 55  ARG   C CD    
3140 N  NE    . ARG   C 56  ? 0.37611 0.39310 0.39615 0.01046  0.03574  -0.02602 55  ARG   C NE    
3141 C  CZ    . ARG   C 56  ? 0.43093 0.44769 0.44874 0.01352  0.03859  -0.02419 55  ARG   C CZ    
3142 N  NH1   . ARG   C 56  ? 0.35671 0.37145 0.37019 0.01652  0.03994  -0.02411 55  ARG   C NH1   
3143 N  NH2   . ARG   C 56  ? 0.55591 0.57437 0.57553 0.01403  0.04024  -0.02221 55  ARG   C NH2   
3144 N  N     . ILE   C 57  ? 0.23165 0.24877 0.26222 0.00383  0.02765  -0.03083 56  ILE   C N     
3145 C  CA    . ILE   C 57  ? 0.23201 0.24814 0.26157 0.00363  0.02669  -0.03201 56  ILE   C CA    
3146 C  C     . ILE   C 57  ? 0.27121 0.28684 0.29722 0.00321  0.02586  -0.03246 56  ILE   C C     
3147 O  O     . ILE   C 57  ? 0.23480 0.25100 0.26051 0.00283  0.02516  -0.03206 56  ILE   C O     
3148 C  CB    . ILE   C 57  ? 0.26518 0.28083 0.29696 0.00353  0.02510  -0.03253 56  ILE   C CB    
3149 C  CG1   . ILE   C 57  ? 0.26695 0.28265 0.30374 0.00373  0.02500  -0.03184 56  ILE   C CG1   
3150 C  CG2   . ILE   C 57  ? 0.29564 0.31046 0.32592 0.00352  0.02433  -0.03350 56  ILE   C CG2   
3151 C  CD1   . ILE   C 57  ? 0.30383 0.31770 0.34240 0.00408  0.02230  -0.03271 56  ILE   C CD1   
3152 N  N     . ILE   C 58  ? 0.24225 0.25662 0.26592 0.00351  0.02569  -0.03302 57  ILE   C N     
3153 C  CA    . ILE   C 58  ? 0.25779 0.27113 0.27932 0.00302  0.02401  -0.03320 57  ILE   C CA    
3154 C  C     . ILE   C 58  ? 0.24249 0.25491 0.26440 0.00271  0.02275  -0.03382 57  ILE   C C     
3155 O  O     . ILE   C 58  ? 0.23833 0.24902 0.25847 0.00348  0.02263  -0.03474 57  ILE   C O     
3156 C  CB    . ILE   C 58  ? 0.27207 0.28342 0.28977 0.00405  0.02380  -0.03348 57  ILE   C CB    
3157 C  CG1   . ILE   C 58  ? 0.27795 0.29056 0.29563 0.00454  0.02555  -0.03259 57  ILE   C CG1   
3158 C  CG2   . ILE   C 58  ? 0.29377 0.30346 0.31045 0.00332  0.02088  -0.03358 57  ILE   C CG2   
3159 C  CD1   . ILE   C 58  ? 0.29052 0.30089 0.30359 0.00607  0.02537  -0.03275 57  ILE   C CD1   
3160 N  N     . PRO   C 59  ? 0.26389 0.27741 0.28794 0.00195  0.02195  -0.03307 58  PRO   C N     
3161 C  CA    . PRO   C 59  ? 0.28491 0.29787 0.31000 0.00167  0.02086  -0.03325 58  PRO   C CA    
3162 C  C     . PRO   C 59  ? 0.27754 0.28813 0.30130 0.00144  0.01863  -0.03377 58  PRO   C C     
3163 O  O     . PRO   C 59  ? 0.26442 0.27402 0.28749 0.00118  0.01707  -0.03331 58  PRO   C O     
3164 C  CB    . PRO   C 59  ? 0.26851 0.28337 0.29607 0.00151  0.02082  -0.03135 58  PRO   C CB    
3165 C  CG    . PRO   C 59  ? 0.28703 0.30303 0.31406 0.00217  0.02215  -0.03093 58  PRO   C CG    
3166 C  CD    . PRO   C 59  ? 0.28806 0.30341 0.31347 0.00189  0.02242  -0.03176 58  PRO   C CD    
3167 N  N     . GLY   C 60  ? 0.27452 0.28364 0.29772 0.00171  0.01799  -0.03485 59  GLY   C N     
3168 C  CA    . GLY   C 60  ? 0.28748 0.29318 0.30826 0.00212  0.01536  -0.03588 59  GLY   C CA    
3169 C  C     . GLY   C 60  ? 0.26446 0.26755 0.27998 0.00422  0.01620  -0.03745 59  GLY   C C     
3170 O  O     . GLY   C 60  ? 0.28256 0.28180 0.29450 0.00545  0.01386  -0.03869 59  GLY   C O     
3171 N  N     . PHE   C 61  ? 0.26023 0.26510 0.27530 0.00503  0.01937  -0.03712 60  PHE   C N     
3172 C  CA    . PHE   C 61  ? 0.27259 0.27554 0.28306 0.00764  0.02089  -0.03755 60  PHE   C CA    
3173 C  C     . PHE   C 61  ? 0.24716 0.25257 0.25995 0.00837  0.02444  -0.03670 60  PHE   C C     
3174 O  O     . PHE   C 61  ? 0.26419 0.26853 0.27565 0.00993  0.02537  -0.03702 60  PHE   C O     
3175 C  CB    . PHE   C 61  ? 0.28254 0.28482 0.29054 0.00832  0.02079  -0.03709 60  PHE   C CB    
3176 C  CG    . PHE   C 61  ? 0.27563 0.27451 0.28137 0.00801  0.01658  -0.03784 60  PHE   C CG    
3177 C  CD1   . PHE   C 61  ? 0.31371 0.30725 0.31322 0.01057  0.01406  -0.03935 60  PHE   C CD1   
3178 C  CD2   . PHE   C 61  ? 0.31290 0.31362 0.32307 0.00546  0.01484  -0.03680 60  PHE   C CD2   
3179 C  CE1   . PHE   C 61  ? 0.36126 0.35090 0.35943 0.01028  0.00913  -0.04006 60  PHE   C CE1   
3180 C  CE2   . PHE   C 61  ? 0.36006 0.35779 0.36995 0.00498  0.01055  -0.03690 60  PHE   C CE2   
3181 C  CZ    . PHE   C 61  ? 0.33106 0.32305 0.33529 0.00717  0.00729  -0.03866 60  PHE   C CZ    
3182 N  N     . MET   C 62  ? 0.25061 0.25899 0.26709 0.00747  0.02616  -0.03544 61  MET   C N     
3183 C  CA    . MET   C 62  ? 0.27287 0.28314 0.29266 0.00834  0.02892  -0.03413 61  MET   C CA    
3184 C  C     . MET   C 62  ? 0.25945 0.27232 0.28432 0.00680  0.02924  -0.03310 61  MET   C C     
3185 O  O     . MET   C 62  ? 0.24008 0.25335 0.26460 0.00570  0.02814  -0.03324 61  MET   C O     
3186 C  CB    . MET   C 62  ? 0.25039 0.25993 0.26710 0.01143  0.03152  -0.03282 61  MET   C CB    
3187 C  CG    . MET   C 62  ? 0.29754 0.30865 0.31518 0.01159  0.03284  -0.03129 61  MET   C CG    
3188 S  SD    . MET   C 62  ? 0.34542 0.35445 0.35810 0.01086  0.03017  -0.03273 61  MET   C SD    
3189 C  CE    . MET   C 62  ? 0.31534 0.32773 0.33277 0.00949  0.03149  -0.03100 61  MET   C CE    
3190 N  N     . CYS   C 63  ? 0.23679 0.25112 0.26664 0.00695  0.03046  -0.03190 62  CYS   C N     
3191 C  CA    . CYS   C 63  ? 0.24943 0.26545 0.28470 0.00609  0.03035  -0.03064 62  CYS   C CA    
3192 C  C     . CYS   C 63  ? 0.25120 0.26882 0.28973 0.00763  0.03311  -0.02785 62  CYS   C C     
3193 O  O     . CYS   C 63  ? 0.27343 0.29156 0.31429 0.00892  0.03485  -0.02645 62  CYS   C O     
3194 C  CB    . CYS   C 63  ? 0.25556 0.27139 0.29535 0.00516  0.02861  -0.03112 62  CYS   C CB    
3195 S  SG    . CYS   C 63  ? 0.31211 0.32631 0.34847 0.00422  0.02604  -0.03360 62  CYS   C SG    
3196 N  N     . GLN   C 64  ? 0.23532 0.25399 0.27463 0.00766  0.03373  -0.02661 63  GLN   C N     
3197 C  CA    . GLN   C 64  ? 0.23682 0.25736 0.27941 0.00949  0.03681  -0.02330 63  GLN   C CA    
3198 C  C     . GLN   C 64  ? 0.25481 0.27719 0.30585 0.00820  0.03590  -0.02127 63  GLN   C C     
3199 O  O     . GLN   C 64  ? 0.23933 0.26106 0.29023 0.00653  0.03329  -0.02274 63  GLN   C O     
3200 C  CB    . GLN   C 64  ? 0.24011 0.25993 0.27596 0.01136  0.03855  -0.02316 63  GLN   C CB    
3201 C  CG    . GLN   C 64  ? 0.24355 0.26541 0.28226 0.01374  0.04212  -0.01935 63  GLN   C CG    
3202 C  CD    . GLN   C 64  ? 0.26750 0.28770 0.29790 0.01627  0.04359  -0.01959 63  GLN   C CD    
3203 O  OE1   . GLN   C 64  ? 0.29278 0.30986 0.31546 0.01654  0.04180  -0.02252 63  GLN   C OE1   
3204 N  NE2   . GLN   C 64  ? 0.29201 0.31412 0.32462 0.01810  0.04647  -0.01632 63  GLN   C NE2   
3205 N  N     . GLY   C 65  ? 0.24359 0.26807 0.30233 0.00921  0.03785  -0.01761 64  GLY   C N     
3206 C  CA    . GLY   C 65  ? 0.27396 0.29993 0.34275 0.00799  0.03631  -0.01510 64  GLY   C CA    
3207 C  C     . GLY   C 65  ? 0.29978 0.32901 0.37617 0.00993  0.04006  -0.00969 64  GLY   C C     
3208 O  O     . GLY   C 65  ? 0.29470 0.32488 0.36646 0.01286  0.04443  -0.00800 64  GLY   C O     
3209 N  N     . GLY   C 66  ? 0.27583 0.30650 0.36394 0.00873  0.03822  -0.00665 65  GLY   C N     
3210 C  CA    . GLY   C 66  ? 0.31321 0.34755 0.41193 0.01039  0.04154  -0.00040 65  GLY   C CA    
3211 C  C     . GLY   C 66  ? 0.30306 0.33991 0.40746 0.01084  0.04296  0.00352  65  GLY   C C     
3212 O  O     . GLY   C 66  ? 0.30779 0.34832 0.42188 0.01264  0.04639  0.00971  65  GLY   C O     
3213 N  N     . ASP   C 67  ? 0.36776 0.40305 0.46714 0.00947  0.04071  0.00064  66  ASP   C N     
3214 C  CA    . ASP   C 67  ? 0.37338 0.41089 0.47860 0.00959  0.04151  0.00417  66  ASP   C CA    
3215 C  C     . ASP   C 67  ? 0.40306 0.44001 0.52087 0.00694  0.03597  0.00549  66  ASP   C C     
3216 O  O     . ASP   C 67  ? 0.46114 0.49465 0.57595 0.00489  0.03079  0.00133  66  ASP   C O     
3217 C  CB    . ASP   C 67  ? 0.39626 0.43219 0.49059 0.00943  0.04143  0.00060  66  ASP   C CB    
3218 C  CG    . ASP   C 67  ? 0.42263 0.46055 0.52281 0.00927  0.04174  0.00382  66  ASP   C CG    
3219 O  OD1   . ASP   C 67  ? 0.41555 0.45649 0.52868 0.00959  0.04257  0.00948  66  ASP   C OD1   
3220 O  OD2   . ASP   C 67  ? 0.45013 0.48676 0.54247 0.00887  0.04121  0.00102  66  ASP   C OD2   
3221 N  N     . PHE   C 68  ? 0.35181 0.39186 0.48389 0.00736  0.03687  0.01162  67  PHE   C N     
3222 C  CA    . PHE   C 68  ? 0.39963 0.43873 0.54549 0.00498  0.03082  0.01353  67  PHE   C CA    
3223 C  C     . PHE   C 68  ? 0.46926 0.51152 0.62550 0.00510  0.03167  0.01904  67  PHE   C C     
3224 O  O     . PHE   C 68  ? 0.48585 0.52753 0.65582 0.00329  0.02646  0.02173  67  PHE   C O     
3225 C  CB    . PHE   C 68  ? 0.37899 0.41892 0.53663 0.00474  0.02960  0.01685  67  PHE   C CB    
3226 C  CG    . PHE   C 68  ? 0.34605 0.39170 0.51082 0.00760  0.03688  0.02409  67  PHE   C CG    
3227 C  CD1   . PHE   C 68  ? 0.36353 0.41366 0.54301 0.00835  0.03891  0.03192  67  PHE   C CD1   
3228 C  CD2   . PHE   C 68  ? 0.42560 0.47204 0.58246 0.00995  0.04174  0.02343  67  PHE   C CD2   
3229 C  CE1   . PHE   C 68  ? 0.44615 0.50183 0.63213 0.01188  0.04639  0.03943  67  PHE   C CE1   
3230 C  CE2   . PHE   C 68  ? 0.40098 0.45225 0.56307 0.01354  0.04876  0.03025  67  PHE   C CE2   
3231 C  CZ    . PHE   C 68  ? 0.38020 0.43628 0.55678 0.01475  0.05145  0.03850  67  PHE   C CZ    
3232 N  N     . THR   C 69  ? 0.43330 0.47869 0.58414 0.00741  0.03786  0.02118  68  THR   C N     
3233 C  CA    . THR   C 69  ? 0.45379 0.50263 0.61446 0.00788  0.03940  0.02693  68  THR   C CA    
3234 C  C     . THR   C 69  ? 0.44821 0.49484 0.60091 0.00672  0.03718  0.02300  68  THR   C C     
3235 O  O     . THR   C 69  ? 0.49876 0.54595 0.66113 0.00538  0.03417  0.02567  68  THR   C O     
3236 C  CB    . THR   C 69  ? 0.43393 0.48805 0.59528 0.01215  0.04836  0.03332  68  THR   C CB    
3237 O  OG1   . THR   C 69  ? 0.46699 0.51960 0.61013 0.01446  0.05236  0.02893  68  THR   C OG1   
3238 C  CG2   . THR   C 69  ? 0.37079 0.42753 0.54046 0.01386  0.05123  0.03802  68  THR   C CG2   
3239 N  N     . ARG   C 70  ? 0.44506 0.48909 0.58100 0.00714  0.03823  0.01689  69  ARG   C N     
3240 C  CA    . ARG   C 70  ? 0.48215 0.52428 0.60993 0.00623  0.03656  0.01327  69  ARG   C CA    
3241 C  C     . ARG   C 70  ? 0.48468 0.52161 0.60349 0.00415  0.03087  0.00604  69  ARG   C C     
3242 O  O     . ARG   C 70  ? 0.51179 0.54667 0.62702 0.00306  0.02783  0.00344  69  ARG   C O     
3243 C  CB    . ARG   C 70  ? 0.43760 0.48141 0.55434 0.00902  0.04291  0.01338  69  ARG   C CB    
3244 C  CG    . ARG   C 70  ? 0.52002 0.56863 0.64340 0.01239  0.04940  0.02071  69  ARG   C CG    
3245 C  CD    . ARG   C 70  ? 0.52802 0.57685 0.63949 0.01530  0.05415  0.02010  69  ARG   C CD    
3246 N  NE    . ARG   C 70  ? 0.57685 0.62897 0.68896 0.02021  0.06138  0.02597  69  ARG   C NE    
3247 C  CZ    . ARG   C 70  ? 0.59763 0.64846 0.69632 0.02417  0.06574  0.02476  69  ARG   C CZ    
3248 N  NH1   . ARG   C 70  ? 0.56364 0.61012 0.64843 0.02325  0.06332  0.01786  69  ARG   C NH1   
3249 N  NH2   . ARG   C 70  ? 0.61898 0.67256 0.71832 0.02944  0.07235  0.03076  69  ARG   C NH2   
3250 N  N     . HIS   C 71  ? 0.47982 0.51487 0.59483 0.00404  0.02999  0.00326  70  HIS   C N     
3251 C  CA    . HIS   C 71  ? 0.48108 0.51143 0.58820 0.00273  0.02513  -0.00280 70  HIS   C CA    
3252 C  C     . HIS   C 71  ? 0.45405 0.48306 0.54781 0.00292  0.02614  -0.00696 70  HIS   C C     
3253 O  O     . HIS   C 71  ? 0.53008 0.55568 0.61894 0.00212  0.02204  -0.01075 70  HIS   C O     
3254 C  CB    . HIS   C 71  ? 0.50255 0.52945 0.61732 0.00120  0.01788  -0.00342 70  HIS   C CB    
3255 C  CG    . HIS   C 71  ? 0.51822 0.54574 0.64719 0.00070  0.01561  0.00053  70  HIS   C CG    
3256 N  ND1   . HIS   C 71  ? 0.53277 0.55764 0.66255 0.00042  0.01268  -0.00134 70  HIS   C ND1   
3257 C  CD2   . HIS   C 71  ? 0.39357 0.42428 0.53737 0.00047  0.01593  0.00676  70  HIS   C CD2   
3258 C  CE1   . HIS   C 71  ? 0.47665 0.50286 0.62122 -0.00009 0.01099  0.00338  70  HIS   C CE1   
3259 N  NE2   . HIS   C 71  ? 0.51492 0.54485 0.66874 -0.00008 0.01295  0.00861  70  HIS   C NE2   
3260 N  N     . ASN   C 72  ? 0.45835 0.48974 0.54612 0.00441  0.03151  -0.00606 71  ASN   C N     
3261 C  CA    . ASN   C 72  ? 0.47127 0.50150 0.54736 0.00458  0.03240  -0.00947 71  ASN   C CA    
3262 C  C     . ASN   C 72  ? 0.51076 0.54110 0.57830 0.00619  0.03612  -0.01061 71  ASN   C C     
3263 O  O     . ASN   C 72  ? 0.50104 0.53061 0.56005 0.00665  0.03717  -0.01255 71  ASN   C O     
3264 C  CB    . ASN   C 72  ? 0.48756 0.51944 0.56476 0.00485  0.03375  -0.00742 71  ASN   C CB    
3265 C  CG    . ASN   C 72  ? 0.47891 0.51436 0.56106 0.00697  0.03874  -0.00227 71  ASN   C CG    
3266 O  OD1   . ASN   C 72  ? 0.54207 0.57877 0.62624 0.00853  0.04150  -0.00017 71  ASN   C OD1   
3267 N  ND2   . ASN   C 72  ? 0.57721 0.61435 0.66115 0.00746  0.04022  0.00009  71  ASN   C ND2   
3268 N  N     . GLY   C 73  ? 0.48125 0.51217 0.55122 0.00715  0.03768  -0.00936 72  GLY   C N     
3269 C  CA    . GLY   C 73  ? 0.41619 0.44653 0.47807 0.00912  0.04071  -0.01039 72  GLY   C CA    
3270 C  C     . GLY   C 73  ? 0.44921 0.48123 0.50917 0.01248  0.04571  -0.00701 72  GLY   C C     
3271 O  O     . GLY   C 73  ? 0.46658 0.49714 0.51867 0.01486  0.04782  -0.00801 72  GLY   C O     
3272 N  N     . THR   C 74  ? 0.43564 0.47038 0.50248 0.01321  0.04758  -0.00282 73  THR   C N     
3273 C  CA    . THR   C 74  ? 0.50084 0.53709 0.56493 0.01725  0.05285  0.00083  73  THR   C CA    
3274 C  C     . THR   C 74  ? 0.47546 0.51540 0.55009 0.01947  0.05657  0.00719  73  THR   C C     
3275 O  O     . THR   C 74  ? 0.51790 0.55905 0.58965 0.02394  0.06176  0.01080  73  THR   C O     
3276 C  CB    . THR   C 74  ? 0.49981 0.53662 0.56306 0.01686  0.05280  0.00128  73  THR   C CB    
3277 O  OG1   . THR   C 74  ? 0.53095 0.57088 0.60731 0.01537  0.05215  0.00536  73  THR   C OG1   
3278 C  CG2   . THR   C 74  ? 0.48296 0.51690 0.53928 0.01394  0.04854  -0.00418 73  THR   C CG2   
3279 N  N     . GLY   C 75  ? 0.44417 0.48553 0.53025 0.01698  0.05404  0.00872  74  GLY   C N     
3280 C  CA    . GLY   C 75  ? 0.40536 0.45078 0.50473 0.01845  0.05688  0.01565  74  GLY   C CA    
3281 C  C     . GLY   C 75  ? 0.48696 0.53279 0.58920 0.01953  0.05807  0.01688  74  GLY   C C     
3282 O  O     . GLY   C 75  ? 0.36754 0.41073 0.45903 0.02081  0.05871  0.01314  74  GLY   C O     
3283 N  N     . GLY   C 76  ? 0.46565 0.51469 0.58335 0.01888  0.05793  0.02233  75  GLY   C N     
3284 C  CA    . GLY   C 76  ? 0.45060 0.50120 0.57416 0.02038  0.05997  0.02547  75  GLY   C CA    
3285 C  C     . GLY   C 76  ? 0.40473 0.46000 0.53378 0.02555  0.06751  0.03374  75  GLY   C C     
3286 O  O     . GLY   C 76  ? 0.47296 0.52927 0.59636 0.02904  0.07198  0.03589  75  GLY   C O     
3287 N  N     . LYS   C 77  ? 0.42876 0.48683 0.56916 0.02639  0.06905  0.03878  76  LYS   C N     
3288 C  CA    . LYS   C 77  ? 0.44691 0.50995 0.59432 0.03178  0.07666  0.04777  76  LYS   C CA    
3289 C  C     . LYS   C 77  ? 0.36512 0.42917 0.51802 0.03265  0.07768  0.04993  76  LYS   C C     
3290 O  O     . LYS   C 77  ? 0.35406 0.41609 0.51169 0.02812  0.07166  0.04628  76  LYS   C O     
3291 C  CB    . LYS   C 77  ? 0.40862 0.47676 0.57428 0.03119  0.07741  0.05589  76  LYS   C CB    
3292 C  CG    . LYS   C 77  ? 0.46186 0.53100 0.64638 0.02604  0.07093  0.05784  76  LYS   C CG    
3293 C  CD    . LYS   C 77  ? 0.47354 0.54706 0.67633 0.02511  0.07055  0.06555  76  LYS   C CD    
3294 C  CE    . LYS   C 77  ? 0.47465 0.54742 0.69533 0.01977  0.06216  0.06638  76  LYS   C CE    
3295 N  NZ    . LYS   C 77  ? 0.51917 0.59645 0.76038 0.01904  0.06153  0.07512  76  LYS   C NZ    
3296 N  N     . SER   C 78  ? 0.34055 0.40743 0.49198 0.03902  0.08547  0.05591  77  SER   C N     
3297 C  CA    . SER   C 78  ? 0.34619 0.41445 0.50228 0.04086  0.08765  0.05884  77  SER   C CA    
3298 C  C     . SER   C 78  ? 0.34716 0.42183 0.52708 0.04053  0.08913  0.06906  77  SER   C C     
3299 O  O     . SER   C 78  ? 0.43118 0.50905 0.62337 0.03916  0.08859  0.07389  77  SER   C O     
3300 C  CB    . SER   C 78  ? 0.33609 0.40357 0.47750 0.04874  0.09529  0.06022  77  SER   C CB    
3301 O  OG    . SER   C 78  ? 0.39588 0.46860 0.54415 0.05481  0.10313  0.07018  77  SER   C OG    
3302 N  N     . ILE   C 79  ? 0.33383 0.41035 0.52109 0.04168  0.09071  0.07259  78  ILE   C N     
3303 C  CA    . ILE   C 79  ? 0.39897 0.48182 0.61020 0.04172  0.09232  0.08319  78  ILE   C CA    
3304 C  C     . ILE   C 79  ? 0.42401 0.51266 0.63803 0.04988  0.10307  0.09375  78  ILE   C C     
3305 O  O     . ILE   C 79  ? 0.46239 0.55728 0.69622 0.05145  0.10642  0.10429  78  ILE   C O     
3306 C  CB    . ILE   C 79  ? 0.35772 0.44014 0.57659 0.03945  0.08924  0.08280  78  ILE   C CB    
3307 C  CG1   . ILE   C 79  ? 0.37680 0.45838 0.58124 0.04547  0.09582  0.08219  78  ILE   C CG1   
3308 C  CG2   . ILE   C 79  ? 0.38395 0.46028 0.59937 0.03213  0.07875  0.07259  78  ILE   C CG2   
3309 C  CD1   . ILE   C 79  ? 0.39692 0.48064 0.61233 0.04560  0.09628  0.08610  78  ILE   C CD1   
3310 N  N     . TYR   C 80  ? 0.41895 0.50538 0.61338 0.05553  0.10845  0.09136  79  TYR   C N     
3311 C  CA    . TYR   C 80  ? 0.47823 0.56884 0.67091 0.06476  0.11906  0.10057  79  TYR   C CA    
3312 C  C     . TYR   C 80  ? 0.53712 0.62908 0.72764 0.06696  0.12185  0.10316  79  TYR   C C     
3313 O  O     . TYR   C 80  ? 0.58574 0.67934 0.76860 0.07554  0.13054  0.10880  79  TYR   C O     
3314 C  CB    . TYR   C 80  ? 0.37845 0.46443 0.54826 0.07161  0.12369  0.09638  79  TYR   C CB    
3315 C  CG    . TYR   C 80  ? 0.39488 0.47865 0.56343 0.06968  0.12088  0.09254  79  TYR   C CG    
3316 C  CD1   . TYR   C 80  ? 0.40214 0.49139 0.58854 0.07051  0.12364  0.10100  79  TYR   C CD1   
3317 C  CD2   . TYR   C 80  ? 0.39132 0.46764 0.54144 0.06707  0.11548  0.08079  79  TYR   C CD2   
3318 C  CE1   . TYR   C 80  ? 0.36407 0.45132 0.54939 0.06881  0.12113  0.09756  79  TYR   C CE1   
3319 C  CE2   . TYR   C 80  ? 0.37446 0.44885 0.52356 0.06538  0.11303  0.07744  79  TYR   C CE2   
3320 C  CZ    . TYR   C 80  ? 0.38553 0.46523 0.55175 0.06619  0.11578  0.08552  79  TYR   C CZ    
3321 O  OH    . TYR   C 80  ? 0.37409 0.45190 0.53932 0.06462  0.11344  0.08229  79  TYR   C OH    
3322 N  N     . GLY   C 81  ? 0.51329 0.60423 0.70943 0.06000  0.11481  0.09918  80  GLY   C N     
3323 C  CA    . GLY   C 81  ? 0.47601 0.56608 0.66421 0.06126  0.11595  0.09803  80  GLY   C CA    
3324 C  C     . GLY   C 81  ? 0.52322 0.60546 0.69062 0.05787  0.10995  0.08503  80  GLY   C C     
3325 O  O     . GLY   C 81  ? 0.57120 0.64907 0.73232 0.05381  0.10435  0.07714  80  GLY   C O     
3326 N  N     . GLU   C 82  ? 0.55825 0.63885 0.71512 0.05984  0.11138  0.08321  81  GLU   C N     
3327 C  CA    . GLU   C 82  ? 0.48937 0.56337 0.63013 0.05577  0.10509  0.07190  81  GLU   C CA    
3328 C  C     . GLU   C 82  ? 0.55669 0.62455 0.67801 0.05782  0.10440  0.06418  81  GLU   C C     
3329 O  O     . GLU   C 82  ? 0.58339 0.64715 0.70001 0.05212  0.09746  0.05584  81  GLU   C O     
3330 C  CB    . GLU   C 82  ? 0.53852 0.61201 0.67154 0.05835  0.10743  0.07217  81  GLU   C CB    
3331 C  CG    . GLU   C 82  ? 0.59096 0.66887 0.74140 0.05398  0.10513  0.07662  81  GLU   C CG    
3332 C  CD    . GLU   C 82  ? 0.66165 0.74333 0.81335 0.06008  0.11247  0.08449  81  GLU   C CD    
3333 O  OE1   . GLU   C 82  ? 0.67537 0.76208 0.83510 0.06623  0.12010  0.09436  81  GLU   C OE1   
3334 O  OE2   . GLU   C 82  ? 0.71881 0.79850 0.86348 0.05901  0.11083  0.08107  81  GLU   C OE2   
3335 N  N     . LYS   C 83  ? 0.48993 0.55677 0.59962 0.06633  0.11138  0.06700  82  LYS   C N     
3336 C  CA    . LYS   C 83  ? 0.45489 0.51492 0.54479 0.06894  0.11025  0.05952  82  LYS   C CA    
3337 C  C     . LYS   C 83  ? 0.45967 0.52069 0.54683 0.07695  0.11725  0.06521  82  LYS   C C     
3338 O  O     . LYS   C 83  ? 0.49411 0.56030 0.58925 0.08288  0.12472  0.07508  82  LYS   C O     
3339 C  CB    . LYS   C 83  ? 0.46979 0.52378 0.54001 0.07187  0.10958  0.05369  82  LYS   C CB    
3340 C  CG    . LYS   C 83  ? 0.51714 0.57061 0.58965 0.06512  0.10389  0.04919  82  LYS   C CG    
3341 C  CD    . LYS   C 83  ? 0.54361 0.59430 0.61684 0.05665  0.09541  0.04086  82  LYS   C CD    
3342 C  CE    . LYS   C 83  ? 0.52772 0.57829 0.60414 0.05047  0.09018  0.03725  82  LYS   C CE    
3343 N  NZ    . LYS   C 83  ? 0.62477 0.67233 0.68807 0.05408  0.09177  0.03556  82  LYS   C NZ    
3344 N  N     . PHE   C 84  ? 0.39636 0.45250 0.47254 0.07735  0.11495  0.05936  83  PHE   C N     
3345 C  CA    . PHE   C 84  ? 0.38296 0.43913 0.45448 0.08533  0.12124  0.06398  83  PHE   C CA    
3346 C  C     . PHE   C 84  ? 0.38942 0.43666 0.43743 0.08943  0.11933  0.05590  83  PHE   C C     
3347 O  O     . PHE   C 84  ? 0.37205 0.41369 0.40996 0.08490  0.11253  0.04678  83  PHE   C O     
3348 C  CB    . PHE   C 84  ? 0.35842 0.41966 0.44720 0.08212  0.12133  0.06830  83  PHE   C CB    
3349 C  CG    . PHE   C 84  ? 0.38628 0.44427 0.47506 0.07402  0.11303  0.05964  83  PHE   C CG    
3350 C  CD1   . PHE   C 84  ? 0.32337 0.38174 0.42074 0.06493  0.10575  0.05519  83  PHE   C CD1   
3351 C  CD2   . PHE   C 84  ? 0.40511 0.45982 0.48582 0.07609  0.11291  0.05668  83  PHE   C CD2   
3352 C  CE1   . PHE   C 84  ? 0.36480 0.42020 0.46209 0.05820  0.09856  0.04779  83  PHE   C CE1   
3353 C  CE2   . PHE   C 84  ? 0.34269 0.39475 0.42399 0.06896  0.10572  0.04933  83  PHE   C CE2   
3354 C  CZ    . PHE   C 84  ? 0.33174 0.38421 0.42124 0.06016  0.09870  0.04501  83  PHE   C CZ    
3355 N  N     . GLU   C 85  ? 0.40682 0.45273 0.44664 0.09857  0.12547  0.05991  84  GLU   C N     
3356 C  CA    . GLU   C 85  ? 0.42191 0.45873 0.43823 0.10528  0.12485  0.05404  84  GLU   C CA    
3357 C  C     . GLU   C 85  ? 0.42074 0.45296 0.43234 0.09989  0.11783  0.04558  84  GLU   C C     
3358 O  O     . GLU   C 85  ? 0.35475 0.39136 0.38071 0.09338  0.11573  0.04610  84  GLU   C O     
3359 C  CB    . GLU   C 85  ? 0.43897 0.47591 0.44852 0.11764  0.13407  0.06189  84  GLU   C CB    
3360 C  CG    . GLU   C 85  ? 0.52908 0.57151 0.55161 0.11797  0.13774  0.06782  84  GLU   C CG    
3361 C  CD    . GLU   C 85  ? 0.57774 0.63117 0.62727 0.11310  0.14081  0.07714  84  GLU   C CD    
3362 O  OE1   . GLU   C 85  ? 0.49684 0.55427 0.55434 0.11228  0.14261  0.08139  84  GLU   C OE1   
3363 O  OE2   . GLU   C 85  ? 0.68134 0.73908 0.74452 0.10995  0.14089  0.08013  84  GLU   C OE2   
3364 N  N     . ASP   C 86  ? 0.39173 0.41470 0.38322 0.10268  0.11375  0.03777  85  ASP   C N     
3365 C  CA    . ASP   C 86  ? 0.35555 0.37336 0.34041 0.09949  0.10779  0.03038  85  ASP   C CA    
3366 C  C     . ASP   C 86  ? 0.42107 0.43964 0.40527 0.10590  0.11303  0.03497  85  ASP   C C     
3367 O  O     . ASP   C 86  ? 0.39905 0.41405 0.37053 0.11664  0.11840  0.03825  85  ASP   C O     
3368 C  CB    . ASP   C 86  ? 0.37285 0.38028 0.33727 0.10157  0.10193  0.02180  85  ASP   C CB    
3369 C  CG    . ASP   C 86  ? 0.38951 0.39646 0.35548 0.09476  0.09655  0.01730  85  ASP   C CG    
3370 O  OD1   . ASP   C 86  ? 0.37123 0.38342 0.35162 0.08551  0.09344  0.01634  85  ASP   C OD1   
3371 O  OD2   . ASP   C 86  ? 0.41645 0.41740 0.36896 0.09883  0.09513  0.01461  85  ASP   C OD2   
3372 N  N     . GLU   C 87  ? 0.37182 0.39523 0.37014 0.09987  0.11186  0.03586  86  GLU   C N     
3373 C  CA    . GLU   C 87  ? 0.33974 0.36580 0.34158 0.10533  0.11763  0.04184  86  GLU   C CA    
3374 C  C     . GLU   C 87  ? 0.39445 0.41160 0.37614 0.11207  0.11646  0.03691  86  GLU   C C     
3375 O  O     . GLU   C 87  ? 0.38454 0.40009 0.35758 0.12259  0.12300  0.04191  86  GLU   C O     
3376 C  CB    . GLU   C 87  ? 0.32689 0.35945 0.34847 0.09680  0.11553  0.04322  86  GLU   C CB    
3377 C  CG    . GLU   C 87  ? 0.37942 0.41624 0.40855 0.10168  0.12182  0.05074  86  GLU   C CG    
3378 C  CD    . GLU   C 87  ? 0.39312 0.43704 0.44470 0.09330  0.11985  0.05353  86  GLU   C CD    
3379 O  OE1   . GLU   C 87  ? 0.37444 0.41850 0.43259 0.08398  0.11283  0.04814  86  GLU   C OE1   
3380 O  OE2   . GLU   C 87  ? 0.39298 0.44188 0.45519 0.09641  0.12508  0.06110  86  GLU   C OE2   
3381 N  N     . ASN   C 88  ? 0.37640 0.38764 0.35082 0.10644  0.10815  0.02748  87  ASN   C N     
3382 C  CA    . ASN   C 88  ? 0.37841 0.37981 0.33307 0.11199  0.10502  0.02154  87  ASN   C CA    
3383 C  C     . ASN   C 88  ? 0.35351 0.35035 0.30546 0.10317  0.09509  0.01185  87  ASN   C C     
3384 O  O     . ASN   C 88  ? 0.34057 0.34230 0.30565 0.09370  0.09178  0.01044  87  ASN   C O     
3385 C  CB    . ASN   C 88  ? 0.37820 0.38005 0.33269 0.11657  0.10867  0.02451  87  ASN   C CB    
3386 C  CG    . ASN   C 88  ? 0.35040 0.35812 0.32181 0.10691  0.10588  0.02377  87  ASN   C CG    
3387 O  OD1   . ASN   C 88  ? 0.35346 0.35839 0.32465 0.09906  0.09807  0.01613  87  ASN   C OD1   
3388 N  ND2   . ASN   C 88  ? 0.34772 0.36332 0.33390 0.10781  0.11213  0.03194  87  ASN   C ND2   
3389 N  N     . PHE   C 89  ? 0.36301 0.35024 0.29806 0.10669  0.09024  0.00552  88  PHE   C N     
3390 C  CA    . PHE   C 89  ? 0.35784 0.34072 0.29094 0.09889  0.08092  -0.00295 88  PHE   C CA    
3391 C  C     . PHE   C 89  ? 0.35950 0.33869 0.28865 0.09896  0.07796  -0.00631 88  PHE   C C     
3392 O  O     . PHE   C 89  ? 0.36390 0.33536 0.28312 0.09794  0.07074  -0.01309 88  PHE   C O     
3393 C  CB    . PHE   C 89  ? 0.39409 0.36836 0.31243 0.10135  0.07570  -0.00813 88  PHE   C CB    
3394 C  CG    . PHE   C 89  ? 0.37831 0.35611 0.30063 0.10050  0.07800  -0.00543 88  PHE   C CG    
3395 C  CD1   . PHE   C 89  ? 0.34881 0.33298 0.28551 0.09051  0.07563  -0.00615 88  PHE   C CD1   
3396 C  CD2   . PHE   C 89  ? 0.42699 0.40181 0.33861 0.11018  0.08287  -0.00182 88  PHE   C CD2   
3397 C  CE1   . PHE   C 89  ? 0.36691 0.35419 0.30726 0.08974  0.07757  -0.00373 88  PHE   C CE1   
3398 C  CE2   . PHE   C 89  ? 0.44067 0.41885 0.35623 0.10930  0.08498  0.00072  88  PHE   C CE2   
3399 C  CZ    . PHE   C 89  ? 0.41027 0.39471 0.34032 0.09895  0.08226  -0.00028 88  PHE   C CZ    
3400 N  N     . ILE   C 90  ? 0.35598 0.34102 0.29455 0.09947  0.08308  -0.00142 89  ILE   C N     
3401 C  CA    . ILE   C 90  ? 0.37057 0.35286 0.30664 0.09918  0.08064  -0.00427 89  ILE   C CA    
3402 C  C     . ILE   C 90  ? 0.40207 0.38376 0.34351 0.08898  0.07248  -0.01098 89  ILE   C C     
3403 O  O     . ILE   C 90  ? 0.37943 0.35440 0.31193 0.08907  0.06694  -0.01646 89  ILE   C O     
3404 C  CB    . ILE   C 90  ? 0.35641 0.34632 0.30462 0.10038  0.08761  0.00273  89  ILE   C CB    
3405 C  CG1   . ILE   C 90  ? 0.36572 0.35551 0.30691 0.11211  0.09617  0.00989  89  ILE   C CG1   
3406 C  CG2   . ILE   C 90  ? 0.35274 0.34073 0.30074 0.09817  0.08445  -0.00065 89  ILE   C CG2   
3407 C  CD1   . ILE   C 90  ? 0.36064 0.35960 0.31753 0.11269  0.10357  0.01841  89  ILE   C CD1   
3408 N  N     . LEU   C 91  ? 0.33524 0.32381 0.29142 0.08047  0.07161  -0.01033 90  LEU   C N     
3409 C  CA    . LEU   C 91  ? 0.33835 0.32757 0.30118 0.07124  0.06510  -0.01545 90  LEU   C CA    
3410 C  C     . LEU   C 91  ? 0.36478 0.34979 0.32207 0.06803  0.05910  -0.02046 90  LEU   C C     
3411 O  O     . LEU   C 91  ? 0.32510 0.31007 0.27999 0.06990  0.06049  -0.01907 90  LEU   C O     
3412 C  CB    . LEU   C 91  ? 0.31250 0.31059 0.29361 0.06440  0.06696  -0.01212 90  LEU   C CB    
3413 C  CG    . LEU   C 91  ? 0.37083 0.37317 0.35965 0.06643  0.07179  -0.00732 90  LEU   C CG    
3414 C  CD1   . LEU   C 91  ? 0.38224 0.39262 0.38936 0.06072  0.07338  -0.00326 90  LEU   C CD1   
3415 C  CD2   . LEU   C 91  ? 0.40635 0.40494 0.39077 0.06548  0.06822  -0.01156 90  LEU   C CD2   
3416 N  N     . LYS   C 92  ? 0.35298 0.33459 0.30883 0.06325  0.05244  -0.02595 91  LYS   C N     
3417 C  CA    . LYS   C 92  ? 0.35056 0.32762 0.30146 0.06040  0.04609  -0.03059 91  LYS   C CA    
3418 C  C     . LYS   C 92  ? 0.33037 0.31253 0.29341 0.05121  0.04310  -0.03199 91  LYS   C C     
3419 O  O     . LYS   C 92  ? 0.34827 0.33590 0.32181 0.04712  0.04464  -0.03058 91  LYS   C O     
3420 C  CB    . LYS   C 92  ? 0.39274 0.36067 0.33145 0.06333  0.04020  -0.03536 91  LYS   C CB    
3421 C  CG    . LYS   C 92  ? 0.41147 0.37291 0.33582 0.07374  0.04281  -0.03431 91  LYS   C CG    
3422 C  CD    . LYS   C 92  ? 0.46452 0.42397 0.38139 0.07961  0.04572  -0.03215 91  LYS   C CD    
3423 C  CE    . LYS   C 92  ? 0.50474 0.45737 0.40615 0.09121  0.04887  -0.03070 91  LYS   C CE    
3424 N  NZ    . LYS   C 92  ? 0.56558 0.51820 0.46134 0.09790  0.05420  -0.02678 91  LYS   C NZ    
3425 N  N     . HIS   C 93  ? 0.31480 0.29490 0.27614 0.04847  0.03886  -0.03454 92  HIS   C N     
3426 C  CA    . HIS   C 93  ? 0.30224 0.28645 0.27339 0.04074  0.03602  -0.03576 92  HIS   C CA    
3427 C  C     . HIS   C 93  ? 0.33061 0.31123 0.30037 0.03803  0.03032  -0.03957 92  HIS   C C     
3428 O  O     . HIS   C 93  ? 0.37373 0.34928 0.33825 0.03779  0.02508  -0.04238 92  HIS   C O     
3429 C  CB    . HIS   C 93  ? 0.31137 0.29543 0.28184 0.03943  0.03461  -0.03605 92  HIS   C CB    
3430 C  CG    . HIS   C 93  ? 0.32918 0.31675 0.30128 0.04208  0.04006  -0.03213 92  HIS   C CG    
3431 N  ND1   . HIS   C 93  ? 0.36451 0.34873 0.32743 0.04933  0.04313  -0.03041 92  HIS   C ND1   
3432 C  CD2   . HIS   C 93  ? 0.30073 0.29456 0.28252 0.03876  0.04275  -0.02943 92  HIS   C CD2   
3433 C  CE1   . HIS   C 93  ? 0.32210 0.31107 0.28993 0.05015  0.04796  -0.02638 92  HIS   C CE1   
3434 N  NE2   . HIS   C 93  ? 0.29873 0.29347 0.27830 0.04359  0.04752  -0.02583 92  HIS   C NE2   
3435 N  N     . THR   C 94  ? 0.31105 0.29405 0.28587 0.03616  0.03106  -0.03944 93  THR   C N     
3436 C  CA    . THR   C 94  ? 0.33155 0.31063 0.30402 0.03487  0.02619  -0.04261 93  THR   C CA    
3437 C  C     . THR   C 94  ? 0.38371 0.36585 0.36464 0.02821  0.02298  -0.04379 93  THR   C C     
3438 O  O     . THR   C 94  ? 0.38644 0.36561 0.36651 0.02679  0.01863  -0.04602 93  THR   C O     
3439 C  CB    . THR   C 94  ? 0.35519 0.33446 0.32724 0.03724  0.02869  -0.04192 93  THR   C CB    
3440 O  OG1   . THR   C 94  ? 0.39405 0.38037 0.37652 0.03436  0.03289  -0.03911 93  THR   C OG1   
3441 C  CG2   . THR   C 94  ? 0.38537 0.36056 0.34732 0.04502  0.03164  -0.04070 93  THR   C CG2   
3442 N  N     . GLY   C 95  ? 0.34784 0.33568 0.33692 0.02455  0.02511  -0.04208 94  GLY   C N     
3443 C  CA    . GLY   C 95  ? 0.40368 0.39445 0.40003 0.01932  0.02292  -0.04272 94  GLY   C CA    
3444 C  C     . GLY   C 95  ? 0.30075 0.29713 0.30498 0.01659  0.02570  -0.04076 94  GLY   C C     
3445 O  O     . GLY   C 95  ? 0.30786 0.30640 0.31343 0.01812  0.02920  -0.03864 94  GLY   C O     
3446 N  N     . PRO   C 96  ? 0.29416 0.29270 0.30377 0.01283  0.02400  -0.04125 95  PRO   C N     
3447 C  CA    . PRO   C 96  ? 0.29758 0.30025 0.31375 0.01071  0.02574  -0.03985 95  PRO   C CA    
3448 C  C     . PRO   C 96  ? 0.29506 0.29970 0.31499 0.01180  0.02877  -0.03829 95  PRO   C C     
3449 O  O     . PRO   C 96  ? 0.32290 0.32662 0.34220 0.01290  0.02920  -0.03862 95  PRO   C O     
3450 C  CB    . PRO   C 96  ? 0.30590 0.30930 0.32522 0.00787  0.02336  -0.04079 95  PRO   C CB    
3451 C  CG    . PRO   C 96  ? 0.32751 0.32792 0.34334 0.00789  0.02038  -0.04213 95  PRO   C CG    
3452 C  CD    . PRO   C 96  ? 0.36370 0.36068 0.37360 0.01102  0.02055  -0.04283 95  PRO   C CD    
3453 N  N     . GLY   C 97  ? 0.28050 0.28785 0.30510 0.01141  0.03058  -0.03637 96  GLY   C N     
3454 C  CA    . GLY   C 97  ? 0.29357 0.30319 0.32434 0.01195  0.03288  -0.03414 96  GLY   C CA    
3455 C  C     . GLY   C 97  ? 0.29411 0.30460 0.32456 0.01530  0.03663  -0.03119 96  GLY   C C     
3456 O  O     . GLY   C 97  ? 0.25791 0.27106 0.29558 0.01567  0.03875  -0.02823 96  GLY   C O     
3457 N  N     . ILE   C 98  ? 0.26319 0.27132 0.28579 0.01811  0.03739  -0.03157 97  ILE   C N     
3458 C  CA    . ILE   C 98  ? 0.25699 0.26567 0.27798 0.02237  0.04150  -0.02840 97  ILE   C CA    
3459 C  C     . ILE   C 98  ? 0.25410 0.26619 0.28132 0.02154  0.04320  -0.02555 97  ILE   C C     
3460 O  O     . ILE   C 98  ? 0.25163 0.26372 0.27866 0.01916  0.04109  -0.02692 97  ILE   C O     
3461 C  CB    . ILE   C 98  ? 0.28189 0.28592 0.29138 0.02610  0.04102  -0.03004 97  ILE   C CB    
3462 C  CG1   . ILE   C 98  ? 0.31185 0.31196 0.31512 0.02795  0.03944  -0.03231 97  ILE   C CG1   
3463 C  CG2   . ILE   C 98  ? 0.31772 0.32199 0.32414 0.03093  0.04522  -0.02675 97  ILE   C CG2   
3464 C  CD1   . ILE   C 98  ? 0.34800 0.34901 0.35212 0.03166  0.04339  -0.02964 97  ILE   C CD1   
3465 N  N     . LEU   C 99  ? 0.25477 0.26981 0.28788 0.02376  0.04711  -0.02117 98  LEU   C N     
3466 C  CA    . LEU   C 99  ? 0.25273 0.27126 0.29320 0.02354  0.04913  -0.01744 98  LEU   C CA    
3467 C  C     . LEU   C 99  ? 0.25920 0.27766 0.29457 0.02889  0.05367  -0.01423 98  LEU   C C     
3468 O  O     . LEU   C 99  ? 0.26406 0.28242 0.29742 0.03325  0.05723  -0.01171 98  LEU   C O     
3469 C  CB    . LEU   C 99  ? 0.24888 0.27099 0.30204 0.02213  0.04988  -0.01397 98  LEU   C CB    
3470 C  CG    . LEU   C 99  ? 0.24644 0.27229 0.31020 0.02145  0.05113  -0.00952 98  LEU   C CG    
3471 C  CD1   . LEU   C 99  ? 0.24270 0.26784 0.30674 0.01775  0.04719  -0.01230 98  LEU   C CD1   
3472 C  CD2   . LEU   C 99  ? 0.25702 0.28581 0.33450 0.02033  0.05117  -0.00570 98  LEU   C CD2   
3473 N  N     . SER   C 100 ? 0.25983 0.27820 0.29266 0.02903  0.05372  -0.01416 99  SER   C N     
3474 C  CA    . SER   C 100 ? 0.26729 0.28424 0.29229 0.03463  0.05741  -0.01208 99  SER   C CA    
3475 C  C     . SER   C 100 ? 0.26544 0.28544 0.29554 0.03422  0.05908  -0.00903 99  SER   C C     
3476 O  O     . SER   C 100 ? 0.25912 0.28087 0.29568 0.02944  0.05620  -0.01006 99  SER   C O     
3477 C  CB    . SER   C 100 ? 0.27279 0.28361 0.28394 0.03609  0.05427  -0.01710 99  SER   C CB    
3478 O  OG    . SER   C 100 ? 0.28136 0.28945 0.28324 0.04201  0.05697  -0.01575 99  SER   C OG    
3479 N  N     . MET   C 101 ? 0.27154 0.29203 0.29850 0.03971  0.06387  -0.00502 100 MET   C N     
3480 C  CA    . MET   C 101 ? 0.27011 0.29379 0.30244 0.03970  0.06592  -0.00150 100 MET   C CA    
3481 C  C     . MET   C 101 ? 0.27198 0.29218 0.29486 0.03930  0.06334  -0.00531 100 MET   C C     
3482 O  O     . MET   C 101 ? 0.27944 0.29463 0.28945 0.04325  0.06308  -0.00775 100 MET   C O     
3483 C  CB    . MET   C 101 ? 0.27626 0.30241 0.30981 0.04636  0.07285  0.00534  100 MET   C CB    
3484 C  CG    . MET   C 101 ? 0.28258 0.31352 0.32881 0.04682  0.07608  0.01094  100 MET   C CG    
3485 S  SD    . MET   C 101 ? 0.30216 0.33826 0.36772 0.03919  0.07258  0.01273  100 MET   C SD    
3486 C  CE    . MET   C 101 ? 0.30223 0.34203 0.37342 0.04110  0.07620  0.01844  100 MET   C CE    
3487 N  N     . ALA   C 102 ? 0.26615 0.28872 0.29547 0.03510  0.06145  -0.00540 101 ALA   C N     
3488 C  CA    . ALA   C 102 ? 0.27198 0.29252 0.29457 0.03528  0.06028  -0.00725 101 ALA   C CA    
3489 C  C     . ALA   C 102 ? 0.29844 0.32042 0.31979 0.04080  0.06573  -0.00217 101 ALA   C C     
3490 O  O     . ALA   C 102 ? 0.31030 0.33646 0.34004 0.04303  0.07022  0.00362  101 ALA   C O     
3491 C  CB    . ALA   C 102 ? 0.26726 0.28988 0.29709 0.02928  0.05663  -0.00882 101 ALA   C CB    
3492 N  N     . ASN   C 103 ? 0.28119 0.29961 0.29222 0.04336  0.06538  -0.00396 102 ASN   C N     
3493 C  CA    . ASN   C 103 ? 0.29803 0.31753 0.30692 0.04921  0.07078  0.00097  102 ASN   C CA    
3494 C  C     . ASN   C 103 ? 0.33879 0.35480 0.33879 0.04983  0.06881  -0.00177 102 ASN   C C     
3495 O  O     . ASN   C 103 ? 0.32896 0.34169 0.32459 0.04597  0.06335  -0.00723 102 ASN   C O     
3496 C  CB    . ASN   C 103 ? 0.29472 0.31184 0.29564 0.05702  0.07525  0.00353  102 ASN   C CB    
3497 C  CG    . ASN   C 103 ? 0.30253 0.31155 0.28752 0.05980  0.07153  -0.00231 102 ASN   C CG    
3498 O  OD1   . ASN   C 103 ? 0.37734 0.38168 0.35318 0.06018  0.06826  -0.00599 102 ASN   C OD1   
3499 N  ND2   . ASN   C 103 ? 0.31806 0.32519 0.30029 0.06165  0.07157  -0.00308 102 ASN   C ND2   
3500 N  N     . ALA   C 104 ? 0.36272 0.37965 0.36057 0.05502  0.07354  0.00256  103 ALA   C N     
3501 C  CA    . ALA   C 104 ? 0.44103 0.45466 0.43031 0.05660  0.07240  0.00074  103 ALA   C CA    
3502 C  C     . ALA   C 104 ? 0.49257 0.49967 0.46576 0.06545  0.07445  0.00054  103 ALA   C C     
3503 O  O     . ALA   C 104 ? 0.52784 0.53322 0.49464 0.06986  0.07656  0.00205  103 ALA   C O     
3504 C  CB    . ALA   C 104 ? 0.44675 0.46609 0.44582 0.05557  0.07566  0.00563  103 ALA   C CB    
3505 N  N     . GLY   C 105 ? 0.38755 0.39038 0.35339 0.06845  0.07350  -0.00152 104 GLY   C N     
3506 C  CA    . GLY   C 105 ? 0.40255 0.39885 0.35311 0.07795  0.07575  -0.00114 104 GLY   C CA    
3507 C  C     . GLY   C 105 ? 0.47353 0.47284 0.42666 0.08362  0.08245  0.00470  104 GLY   C C     
3508 O  O     . GLY   C 105 ? 0.40575 0.41253 0.37391 0.07966  0.08512  0.00865  104 GLY   C O     
3509 N  N     . PRO   C 106 ? 0.44627 0.43947 0.38458 0.09358  0.08526  0.00565  105 PRO   C N     
3510 C  CA    . PRO   C 106 ? 0.42761 0.42275 0.36633 0.10009  0.09169  0.01111  105 PRO   C CA    
3511 C  C     . PRO   C 106 ? 0.42452 0.42986 0.37952 0.10019  0.09950  0.02026  105 PRO   C C     
3512 O  O     . PRO   C 106 ? 0.42761 0.43606 0.38614 0.10107  0.10247  0.02393  105 PRO   C O     
3513 C  CB    . PRO   C 106 ? 0.47054 0.45653 0.38845 0.11196  0.09342  0.01075  105 PRO   C CB    
3514 C  CG    . PRO   C 106 ? 0.52854 0.50575 0.43476 0.10965  0.08461  0.00235  105 PRO   C CG    
3515 C  CD    . PRO   C 106 ? 0.45172 0.43467 0.37119 0.09926  0.08138  0.00088  105 PRO   C CD    
3516 N  N     . ASN   C 107 ? 0.40194 0.41231 0.36736 0.09933  0.10252  0.02412  106 ASN   C N     
3517 C  CA    . ASN   C 107 ? 0.38103 0.40089 0.36337 0.10003  0.10978  0.03369  106 ASN   C CA    
3518 C  C     . ASN   C 107 ? 0.37966 0.40627 0.37836 0.09203  0.10844  0.03553  106 ASN   C C     
3519 O  O     . ASN   C 107 ? 0.40337 0.43567 0.41105 0.09468  0.11419  0.04321  106 ASN   C O     
3520 C  CB    . ASN   C 107 ? 0.43192 0.45167 0.40686 0.11214  0.11866  0.04136  106 ASN   C CB    
3521 C  CG    . ASN   C 107 ? 0.48484 0.49674 0.44142 0.12140  0.11989  0.03947  106 ASN   C CG    
3522 O  OD1   . ASN   C 107 ? 0.41487 0.42647 0.37312 0.12000  0.11861  0.03803  106 ASN   C OD1   
3523 N  ND2   . ASN   C 107 ? 0.57694 0.58171 0.51501 0.13125  0.12195  0.03917  106 ASN   C ND2   
3524 N  N     . THR   C 108 ? 0.35983 0.38592 0.36296 0.08248  0.10089  0.02889  107 THR   C N     
3525 C  CA    . THR   C 108 ? 0.40037 0.43207 0.41836 0.07494  0.09885  0.03007  107 THR   C CA    
3526 C  C     . THR   C 108 ? 0.34168 0.37641 0.37287 0.06616  0.09393  0.02770  107 THR   C C     
3527 O  O     . THR   C 108 ? 0.36396 0.39923 0.40027 0.05898  0.08864  0.02387  107 THR   C O     
3528 C  CB    . THR   C 108 ? 0.43207 0.45982 0.44148 0.07267  0.09457  0.02466  107 THR   C CB    
3529 O  OG1   . THR   C 108 ? 0.36900 0.39019 0.36754 0.06959  0.08780  0.01600  107 THR   C OG1   
3530 C  CG2   . THR   C 108 ? 0.43563 0.46035 0.43278 0.08145  0.09926  0.02735  107 THR   C CG2   
3531 N  N     . ASN   C 109 ? 0.33032 0.36683 0.36682 0.06701  0.09564  0.03007  108 ASN   C N     
3532 C  CA    . ASN   C 109 ? 0.33096 0.37015 0.38028 0.05931  0.09112  0.02835  108 ASN   C CA    
3533 C  C     . ASN   C 109 ? 0.40350 0.44956 0.47245 0.05529  0.09165  0.03423  108 ASN   C C     
3534 O  O     . ASN   C 109 ? 0.36202 0.41294 0.43976 0.05944  0.09763  0.04265  108 ASN   C O     
3535 C  CB    . ASN   C 109 ? 0.32819 0.36738 0.37825 0.06151  0.09281  0.02957  108 ASN   C CB    
3536 C  CG    . ASN   C 109 ? 0.33249 0.36452 0.36367 0.06605  0.09206  0.02423  108 ASN   C CG    
3537 O  OD1   . ASN   C 109 ? 0.35328 0.38087 0.37767 0.06187  0.08601  0.01679  108 ASN   C OD1   
3538 N  ND2   . ASN   C 109 ? 0.32974 0.36029 0.35208 0.07520  0.09816  0.02833  108 ASN   C ND2   
3539 N  N     . GLY   C 110 ? 0.31502 0.36121 0.39108 0.04746  0.08512  0.03001  109 GLY   C N     
3540 C  CA    . GLY   C 110 ? 0.33747 0.38888 0.43230 0.04333  0.08393  0.03479  109 GLY   C CA    
3541 C  C     . GLY   C 110 ? 0.26011 0.31144 0.36380 0.03770  0.07854  0.03221  109 GLY   C C     
3542 O  O     . GLY   C 110 ? 0.29661 0.34974 0.40657 0.03903  0.08042  0.03549  109 GLY   C O     
3543 N  N     . SER   C 111 ? 0.29191 0.34078 0.39535 0.03179  0.07181  0.02624  110 SER   C N     
3544 C  CA    . SER   C 111 ? 0.29400 0.34146 0.40271 0.02705  0.06622  0.02271  110 SER   C CA    
3545 C  C     . SER   C 111 ? 0.29545 0.33772 0.39110 0.02425  0.06144  0.01394  110 SER   C C     
3546 O  O     . SER   C 111 ? 0.28177 0.32240 0.37910 0.02146  0.05767  0.01085  110 SER   C O     
3547 C  CB    . SER   C 111 ? 0.31226 0.36171 0.43693 0.02258  0.06167  0.02497  110 SER   C CB    
3548 O  OG    . SER   C 111 ? 0.30797 0.35607 0.42906 0.02054  0.05903  0.02216  110 SER   C OG    
3549 N  N     . GLN   C 112 ? 0.28866 0.32837 0.37219 0.02496  0.06137  0.01021  111 GLN   C N     
3550 C  CA    . GLN   C 112 ? 0.25008 0.28545 0.32346 0.02215  0.05677  0.00285  111 GLN   C CA    
3551 C  C     . GLN   C 112 ? 0.26820 0.30097 0.33305 0.02418  0.05757  0.00032  111 GLN   C C     
3552 O  O     . GLN   C 112 ? 0.26752 0.30033 0.32787 0.02900  0.06208  0.00290  111 GLN   C O     
3553 C  CB    . GLN   C 112 ? 0.27388 0.30732 0.33792 0.02233  0.05626  0.00010  111 GLN   C CB    
3554 C  CG    . GLN   C 112 ? 0.29226 0.32738 0.36344 0.01936  0.05401  0.00097  111 GLN   C CG    
3555 C  CD    . GLN   C 112 ? 0.31754 0.35019 0.37911 0.01850  0.05223  -0.00305 111 GLN   C CD    
3556 O  OE1   . GLN   C 112 ? 0.28022 0.30961 0.33271 0.01769  0.04996  -0.00783 111 GLN   C OE1   
3557 N  NE2   . GLN   C 112 ? 0.30659 0.34092 0.37086 0.01865  0.05320  -0.00077 111 GLN   C NE2   
3558 N  N     . PHE   C 113 ? 0.24533 0.27581 0.30859 0.02071  0.05309  -0.00440 112 PHE   C N     
3559 C  CA    . PHE   C 113 ? 0.24753 0.27550 0.30401 0.02185  0.05295  -0.00708 112 PHE   C CA    
3560 C  C     . PHE   C 113 ? 0.24548 0.27008 0.29505 0.01867  0.04824  -0.01308 112 PHE   C C     
3561 O  O     . PHE   C 113 ? 0.24219 0.26679 0.29332 0.01576  0.04540  -0.01467 112 PHE   C O     
3562 C  CB    . PHE   C 113 ? 0.24502 0.27489 0.31158 0.02073  0.05263  -0.00495 112 PHE   C CB    
3563 C  CG    . PHE   C 113 ? 0.23955 0.26937 0.31388 0.01597  0.04749  -0.00679 112 PHE   C CG    
3564 C  CD1   . PHE   C 113 ? 0.25959 0.29173 0.34484 0.01446  0.04642  -0.00355 112 PHE   C CD1   
3565 C  CD2   . PHE   C 113 ? 0.25067 0.27763 0.32092 0.01348  0.04349  -0.01169 112 PHE   C CD2   
3566 C  CE1   . PHE   C 113 ? 0.31070 0.34146 0.40140 0.01090  0.04099  -0.00567 112 PHE   C CE1   
3567 C  CE2   . PHE   C 113 ? 0.27871 0.30475 0.35422 0.01022  0.03881  -0.01345 112 PHE   C CE2   
3568 C  CZ    . PHE   C 113 ? 0.28281 0.31033 0.36796 0.00910  0.03733  -0.01067 112 PHE   C CZ    
3569 N  N     . PHE   C 114 ? 0.24772 0.26958 0.29017 0.01951  0.04753  -0.01593 113 PHE   C N     
3570 C  CA    . PHE   C 114 ? 0.24568 0.26488 0.28331 0.01657  0.04326  -0.02075 113 PHE   C CA    
3571 C  C     . PHE   C 114 ? 0.24560 0.26354 0.28269 0.01626  0.04221  -0.02239 113 PHE   C C     
3572 O  O     . PHE   C 114 ? 0.24910 0.26678 0.28476 0.01922  0.04478  -0.02089 113 PHE   C O     
3573 C  CB    . PHE   C 114 ? 0.24915 0.26533 0.27672 0.01759  0.04228  -0.02326 113 PHE   C CB    
3574 C  CG    . PHE   C 114 ? 0.25625 0.26939 0.27513 0.02196  0.04402  -0.02341 113 PHE   C CG    
3575 C  CD1   . PHE   C 114 ? 0.26130 0.27491 0.27820 0.02649  0.04824  -0.02003 113 PHE   C CD1   
3576 C  CD2   . PHE   C 114 ? 0.25872 0.26807 0.27103 0.02199  0.04123  -0.02680 113 PHE   C CD2   
3577 C  CE1   . PHE   C 114 ? 0.26959 0.27928 0.27659 0.03160  0.04962  -0.02038 113 PHE   C CE1   
3578 C  CE2   . PHE   C 114 ? 0.26662 0.27188 0.26978 0.02648  0.04186  -0.02741 113 PHE   C CE2   
3579 C  CZ    . PHE   C 114 ? 0.27251 0.27760 0.27224 0.03158  0.04603  -0.02439 113 PHE   C CZ    
3580 N  N     . ILE   C 115 ? 0.24197 0.25905 0.27987 0.01301  0.03857  -0.02532 114 ILE   C N     
3581 C  CA    . ILE   C 115 ? 0.24168 0.25729 0.27838 0.01238  0.03707  -0.02737 114 ILE   C CA    
3582 C  C     . ILE   C 115 ? 0.24305 0.25583 0.27200 0.01181  0.03468  -0.03061 114 ILE   C C     
3583 O  O     . ILE   C 115 ? 0.24084 0.25360 0.26944 0.00981  0.03262  -0.03181 114 ILE   C O     
3584 C  CB    . ILE   C 115 ? 0.23737 0.25376 0.28082 0.00967  0.03461  -0.02793 114 ILE   C CB    
3585 C  CG1   . ILE   C 115 ? 0.25713 0.27598 0.31009 0.00954  0.03548  -0.02457 114 ILE   C CG1   
3586 C  CG2   . ILE   C 115 ? 0.24481 0.25976 0.28676 0.00945  0.03357  -0.02976 114 ILE   C CG2   
3587 C  CD1   . ILE   C 115 ? 0.28386 0.30211 0.34248 0.00705  0.03155  -0.02563 114 ILE   C CD1   
3588 N  N     . CYS   C 116 ? 0.24712 0.25741 0.27028 0.01377  0.03478  -0.03171 115 CYS   C N     
3589 C  CA    . CYS   C 116 ? 0.24895 0.25619 0.26607 0.01316  0.03173  -0.03443 115 CYS   C CA    
3590 C  C     . CYS   C 116 ? 0.27405 0.28161 0.29404 0.01022  0.02912  -0.03604 115 CYS   C C     
3591 O  O     . CYS   C 116 ? 0.27244 0.28095 0.29609 0.00971  0.02953  -0.03591 115 CYS   C O     
3592 C  CB    . CYS   C 116 ? 0.25546 0.25896 0.26542 0.01640  0.03163  -0.03538 115 CYS   C CB    
3593 S  SG    . CYS   C 116 ? 0.33459 0.33644 0.33834 0.02169  0.03501  -0.03342 115 CYS   C SG    
3594 N  N     . THR   C 117 ? 0.29249 0.29927 0.31107 0.00854  0.02655  -0.03720 116 THR   C N     
3595 C  CA    . THR   C 117 ? 0.29713 0.30396 0.31756 0.00654  0.02435  -0.03822 116 THR   C CA    
3596 C  C     . THR   C 117 ? 0.31120 0.31508 0.32801 0.00673  0.02171  -0.03948 116 THR   C C     
3597 O  O     . THR   C 117 ? 0.32820 0.33218 0.34693 0.00522  0.01985  -0.03982 116 THR   C O     
3598 C  CB    . THR   C 117 ? 0.32109 0.32983 0.34429 0.00480  0.02370  -0.03765 116 THR   C CB    
3599 O  OG1   . THR   C 117 ? 0.28326 0.29143 0.30414 0.00476  0.02290  -0.03734 116 THR   C OG1   
3600 C  CG2   . THR   C 117 ? 0.31565 0.32630 0.34248 0.00483  0.02535  -0.03668 116 THR   C CG2   
3601 N  N     . ALA   C 118 ? 0.28680 0.28767 0.29836 0.00897  0.02132  -0.04003 117 ALA   C N     
3602 C  CA    . ALA   C 118 ? 0.29793 0.29471 0.30560 0.00961  0.01777  -0.04146 117 ALA   C CA    
3603 C  C     . ALA   C 118 ? 0.32310 0.31610 0.32367 0.01359  0.01846  -0.04213 117 ALA   C C     
3604 O  O     . ALA   C 118 ? 0.31731 0.31168 0.31688 0.01560  0.02208  -0.04089 117 ALA   C O     
3605 C  CB    . ALA   C 118 ? 0.35619 0.35206 0.36446 0.00809  0.01454  -0.04129 117 ALA   C CB    
3606 N  N     . LYS   C 119 ? 0.32594 0.31395 0.32159 0.01513  0.01489  -0.04383 118 LYS   C N     
3607 C  CA    . LYS   C 119 ? 0.35551 0.33858 0.34233 0.02002  0.01504  -0.04467 118 LYS   C CA    
3608 C  C     . LYS   C 119 ? 0.39365 0.37456 0.37615 0.02172  0.01433  -0.04454 118 LYS   C C     
3609 O  O     . LYS   C 119 ? 0.38211 0.36152 0.36578 0.01966  0.01025  -0.04516 118 LYS   C O     
3610 C  CB    . LYS   C 119 ? 0.43281 0.41003 0.41503 0.02140  0.01029  -0.04690 118 LYS   C CB    
3611 C  CG    . LYS   C 119 ? 0.41431 0.38505 0.38574 0.02734  0.00970  -0.04816 118 LYS   C CG    
3612 C  CD    . LYS   C 119 ? 0.51762 0.48305 0.48581 0.02824  0.00499  -0.05040 118 LYS   C CD    
3613 C  CE    . LYS   C 119 ? 0.57600 0.53212 0.53383 0.03269  -0.00061 -0.05274 118 LYS   C CE    
3614 N  NZ    . LYS   C 119 ? 0.67752 0.62778 0.62704 0.03746  -0.00184 -0.05448 118 LYS   C NZ    
3615 N  N     . THR   C 120 ? 0.34901 0.32994 0.32709 0.02560  0.01840  -0.04332 119 THR   C N     
3616 C  CA    . THR   C 120 ? 0.35320 0.33234 0.32678 0.02772  0.01851  -0.04293 119 THR   C CA    
3617 C  C     . THR   C 120 ? 0.36959 0.34277 0.33189 0.03466  0.01926  -0.04337 119 THR   C C     
3618 O  O     . THR   C 120 ? 0.35549 0.33018 0.31534 0.03828  0.02424  -0.04110 119 THR   C O     
3619 C  CB    . THR   C 120 ? 0.33267 0.31821 0.31241 0.02605  0.02333  -0.04022 119 THR   C CB    
3620 O  OG1   . THR   C 120 ? 0.34081 0.32947 0.32245 0.02813  0.02852  -0.03798 119 THR   C OG1   
3621 C  CG2   . THR   C 120 ? 0.28551 0.27584 0.27453 0.02023  0.02228  -0.03997 119 THR   C CG2   
3622 N  N     . GLU   C 121 ? 0.37787 0.34384 0.33311 0.03689  0.01401  -0.04611 120 GLU   C N     
3623 C  CA    . GLU   C 121 ? 0.42734 0.38655 0.37046 0.04432  0.01428  -0.04690 120 GLU   C CA    
3624 C  C     . GLU   C 121 ? 0.40645 0.36183 0.34094 0.04931  0.01500  -0.04652 120 GLU   C C     
3625 O  O     . GLU   C 121 ? 0.42142 0.37393 0.34705 0.05623  0.01859  -0.04541 120 GLU   C O     
3626 C  CB    . GLU   C 121 ? 0.47520 0.42667 0.41293 0.04531  0.00714  -0.05032 120 GLU   C CB    
3627 C  CG    . GLU   C 121 ? 0.54865 0.49413 0.48455 0.04390  -0.00087 -0.05273 120 GLU   C CG    
3628 C  CD    . GLU   C 121 ? 0.55296 0.50396 0.50171 0.03595  -0.00331 -0.05209 120 GLU   C CD    
3629 O  OE1   . GLU   C 121 ? 0.48275 0.44122 0.44108 0.03143  0.00014  -0.05049 120 GLU   C OE1   
3630 O  OE2   . GLU   C 121 ? 0.68329 0.63070 0.63233 0.03464  -0.00893 -0.05304 120 GLU   C OE2   
3631 N  N     . TRP   C 122 ? 0.43846 0.39398 0.37544 0.04628  0.01211  -0.04702 121 TRP   C N     
3632 C  CA    . TRP   C 122 ? 0.42164 0.37315 0.35023 0.05093  0.01236  -0.04687 121 TRP   C CA    
3633 C  C     . TRP   C 122 ? 0.40690 0.36454 0.33706 0.05328  0.02086  -0.04290 121 TRP   C C     
3634 O  O     . TRP   C 122 ? 0.44575 0.40015 0.36764 0.05875  0.02260  -0.04208 121 TRP   C O     
3635 C  CB    . TRP   C 122 ? 0.41668 0.36761 0.34924 0.04642  0.00722  -0.04807 121 TRP   C CB    
3636 C  CG    . TRP   C 122 ? 0.40620 0.36674 0.35192 0.03946  0.01037  -0.04581 121 TRP   C CG    
3637 C  CD1   . TRP   C 122 ? 0.42407 0.38956 0.37281 0.03879  0.01483  -0.04350 121 TRP   C CD1   
3638 C  CD2   . TRP   C 122 ? 0.40793 0.37372 0.36472 0.03290  0.00925  -0.04560 121 TRP   C CD2   
3639 N  NE1   . TRP   C 122 ? 0.38039 0.35331 0.34081 0.03236  0.01612  -0.04218 121 TRP   C NE1   
3640 C  CE2   . TRP   C 122 ? 0.44307 0.41630 0.40823 0.02894  0.01297  -0.04336 121 TRP   C CE2   
3641 C  CE3   . TRP   C 122 ? 0.42681 0.39146 0.38694 0.03036  0.00538  -0.04697 121 TRP   C CE3   
3642 C  CZ2   . TRP   C 122 ? 0.42409 0.40305 0.39957 0.02319  0.01297  -0.04258 121 TRP   C CZ2   
3643 C  CZ3   . TRP   C 122 ? 0.41669 0.38777 0.38790 0.02441  0.00589  -0.04582 121 TRP   C CZ3   
3644 C  CH2   . TRP   C 122 ? 0.47376 0.45163 0.45191 0.02120  0.00967  -0.04371 121 TRP   C CH2   
3645 N  N     . LEU   C 123 ? 0.37627 0.34251 0.31737 0.04930  0.02585  -0.04020 122 LEU   C N     
3646 C  CA    . LEU   C 123 ? 0.39251 0.36455 0.33686 0.05150  0.03344  -0.03586 122 LEU   C CA    
3647 C  C     . LEU   C 123 ? 0.37899 0.34929 0.31687 0.05863  0.03801  -0.03372 122 LEU   C C     
3648 O  O     . LEU   C 123 ? 0.39730 0.37174 0.33715 0.06186  0.04457  -0.02931 122 LEU   C O     
3649 C  CB    . LEU   C 123 ? 0.36004 0.34108 0.31908 0.04456  0.03588  -0.03386 122 LEU   C CB    
3650 C  CG    . LEU   C 123 ? 0.37621 0.35936 0.34127 0.03833  0.03226  -0.03531 122 LEU   C CG    
3651 C  CD1   . LEU   C 123 ? 0.35841 0.34884 0.33610 0.03226  0.03370  -0.03401 122 LEU   C CD1   
3652 C  CD2   . LEU   C 123 ? 0.31730 0.30004 0.27936 0.04001  0.03328  -0.03428 122 LEU   C CD2   
3653 N  N     . ASP   C 124 ? 0.38188 0.34617 0.31243 0.06138  0.03475  -0.03637 123 ASP   C N     
3654 C  CA    . ASP   C 124 ? 0.42947 0.39171 0.35315 0.06861  0.03902  -0.03438 123 ASP   C CA    
3655 C  C     . ASP   C 124 ? 0.50833 0.46666 0.42072 0.07742  0.04271  -0.03214 123 ASP   C C     
3656 O  O     . ASP   C 124 ? 0.51458 0.46602 0.41734 0.08008  0.03845  -0.03482 123 ASP   C O     
3657 C  CB    . ASP   C 124 ? 0.45303 0.40781 0.36886 0.07045  0.03354  -0.03839 123 ASP   C CB    
3658 C  CG    . ASP   C 124 ? 0.44651 0.40616 0.37330 0.06367  0.03245  -0.03908 123 ASP   C CG    
3659 O  OD1   . ASP   C 124 ? 0.39862 0.36692 0.33839 0.05798  0.03581  -0.03660 123 ASP   C OD1   
3660 O  OD2   . ASP   C 124 ? 0.43468 0.38902 0.35686 0.06424  0.02782  -0.04222 123 ASP   C OD2   
3661 N  N     . GLY   C 125 ? 0.45101 0.41408 0.36555 0.08190  0.05074  -0.02675 124 GLY   C N     
3662 C  CA    . GLY   C 125 ? 0.47990 0.44057 0.38487 0.09092  0.05583  -0.02328 124 GLY   C CA    
3663 C  C     . GLY   C 125 ? 0.48351 0.44875 0.39398 0.08881  0.05819  -0.02082 124 GLY   C C     
3664 O  O     . GLY   C 125 ? 0.57733 0.54124 0.48065 0.09630  0.06294  -0.01737 124 GLY   C O     
3665 N  N     . LYS   C 126 ? 0.43594 0.40620 0.35818 0.07943  0.05513  -0.02234 125 LYS   C N     
3666 C  CA    . LYS   C 126 ? 0.45105 0.42642 0.38000 0.07689  0.05756  -0.01975 125 LYS   C CA    
3667 C  C     . LYS   C 126 ? 0.43990 0.42586 0.38656 0.07094  0.06191  -0.01537 125 LYS   C C     
3668 O  O     . LYS   C 126 ? 0.44086 0.43177 0.39397 0.07023  0.06545  -0.01168 125 LYS   C O     
3669 C  CB    . LYS   C 126 ? 0.50017 0.47233 0.42790 0.07158  0.05042  -0.02467 125 LYS   C CB    
3670 C  CG    . LYS   C 126 ? 0.52223 0.48428 0.43372 0.07787  0.04640  -0.02782 125 LYS   C CG    
3671 C  CD    . LYS   C 126 ? 0.62799 0.58078 0.52935 0.07986  0.03946  -0.03292 125 LYS   C CD    
3672 C  CE    . LYS   C 126 ? 0.71080 0.65211 0.59461 0.08780  0.03527  -0.03577 125 LYS   C CE    
3673 N  NZ    . LYS   C 126 ? 0.72915 0.65987 0.60189 0.09098  0.02774  -0.04068 125 LYS   C NZ    
3674 N  N     . HIS   C 127 ? 0.36919 0.35815 0.32362 0.06692  0.06128  -0.01573 126 HIS   C N     
3675 C  CA    . HIS   C 127 ? 0.31423 0.31182 0.28522 0.06097  0.06368  -0.01247 126 HIS   C CA    
3676 C  C     . HIS   C 127 ? 0.32637 0.32585 0.30084 0.06298  0.06678  -0.00997 126 HIS   C C     
3677 O  O     . HIS   C 127 ? 0.35895 0.35373 0.32645 0.06400  0.06383  -0.01350 126 HIS   C O     
3678 C  CB    . HIS   C 127 ? 0.29944 0.29826 0.27709 0.05224  0.05776  -0.01677 126 HIS   C CB    
3679 C  CG    . HIS   C 127 ? 0.29833 0.29595 0.27385 0.05002  0.05496  -0.01874 126 HIS   C CG    
3680 N  ND1   . HIS   C 127 ? 0.29144 0.29451 0.27624 0.04676  0.05671  -0.01611 126 HIS   C ND1   
3681 C  CD2   . HIS   C 127 ? 0.31574 0.30701 0.28069 0.05135  0.05067  -0.02262 126 HIS   C CD2   
3682 C  CE1   . HIS   C 127 ? 0.34673 0.34723 0.32663 0.04589  0.05388  -0.01846 126 HIS   C CE1   
3683 N  NE2   . HIS   C 127 ? 0.35211 0.34554 0.32043 0.04847  0.05009  -0.02236 126 HIS   C NE2   
3684 N  N     . VAL   C 128 ? 0.30660 0.31279 0.29217 0.06374  0.07252  -0.00364 127 VAL   C N     
3685 C  CA    . VAL   C 128 ? 0.30669 0.31545 0.29743 0.06563  0.07589  -0.00034 127 VAL   C CA    
3686 C  C     . VAL   C 128 ? 0.29615 0.30750 0.29724 0.05764  0.07166  -0.00309 127 VAL   C C     
3687 O  O     . VAL   C 128 ? 0.28684 0.30314 0.30056 0.05176  0.07060  -0.00194 127 VAL   C O     
3688 C  CB    . VAL   C 128 ? 0.30695 0.32223 0.30764 0.06936  0.08341  0.00830  127 VAL   C CB    
3689 C  CG1   . VAL   C 128 ? 0.30660 0.32493 0.31415 0.07098  0.08676  0.01216  127 VAL   C CG1   
3690 C  CG2   . VAL   C 128 ? 0.34527 0.35760 0.33420 0.07840  0.08816  0.01130  127 VAL   C CG2   
3691 N  N     . VAL   C 129 ? 0.29843 0.30594 0.29364 0.05791  0.06906  -0.00672 128 VAL   C N     
3692 C  CA    . VAL   C 129 ? 0.29006 0.29974 0.29411 0.05158  0.06578  -0.00885 128 VAL   C CA    
3693 C  C     . VAL   C 129 ? 0.28770 0.30270 0.30284 0.05275  0.07048  -0.00307 128 VAL   C C     
3694 O  O     . VAL   C 129 ? 0.29520 0.30969 0.30611 0.05942  0.07527  0.00055  128 VAL   C O     
3695 C  CB    . VAL   C 129 ? 0.29324 0.29685 0.28729 0.05144  0.06115  -0.01465 128 VAL   C CB    
3696 C  CG1   . VAL   C 129 ? 0.28504 0.29126 0.28837 0.04583  0.05877  -0.01601 128 VAL   C CG1   
3697 C  CG2   . VAL   C 129 ? 0.29460 0.29339 0.28042 0.04951  0.05580  -0.01978 128 VAL   C CG2   
3698 N  N     . PHE   C 130 ? 0.27814 0.29778 0.30734 0.04662  0.06882  -0.00215 129 PHE   C N     
3699 C  CA    . PHE   C 130 ? 0.27585 0.30071 0.31786 0.04730  0.07266  0.00393  129 PHE   C CA    
3700 C  C     . PHE   C 130 ? 0.26782 0.29425 0.31992 0.04108  0.06854  0.00199  129 PHE   C C     
3701 O  O     . PHE   C 130 ? 0.28431 0.31473 0.34830 0.04097  0.07066  0.00677  129 PHE   C O     
3702 C  CB    . PHE   C 130 ? 0.27440 0.30464 0.32726 0.04825  0.07665  0.01073  129 PHE   C CB    
3703 C  CG    . PHE   C 130 ? 0.26772 0.29963 0.32863 0.04180  0.07232  0.00903  129 PHE   C CG    
3704 C  CD1   . PHE   C 130 ? 0.26702 0.29629 0.31981 0.04070  0.06999  0.00522  129 PHE   C CD1   
3705 C  CD2   . PHE   C 130 ? 0.28725 0.32276 0.36363 0.03693  0.06998  0.01099  129 PHE   C CD2   
3706 C  CE1   . PHE   C 130 ? 0.26027 0.29080 0.31982 0.03508  0.06596  0.00354  129 PHE   C CE1   
3707 C  CE2   . PHE   C 130 ? 0.25347 0.28948 0.33598 0.03157  0.06540  0.00901  129 PHE   C CE2   
3708 C  CZ    . PHE   C 130 ? 0.26061 0.29439 0.33473 0.03079  0.06375  0.00549  129 PHE   C CZ    
3709 N  N     . GLY   C 131 ? 0.26817 0.29139 0.31592 0.03641  0.06281  -0.00449 130 GLY   C N     
3710 C  CA    . GLY   C 131 ? 0.26506 0.28938 0.32152 0.03153  0.05929  -0.00598 130 GLY   C CA    
3711 C  C     . GLY   C 131 ? 0.25651 0.27673 0.30520 0.02808  0.05400  -0.01287 130 GLY   C C     
3712 O  O     . GLY   C 131 ? 0.25945 0.27611 0.29707 0.02928  0.05285  -0.01621 130 GLY   C O     
3713 N  N     . LYS   C 132 ? 0.25077 0.27136 0.30578 0.02402  0.05062  -0.01466 131 LYS   C N     
3714 C  CA    . LYS   C 132 ? 0.24852 0.26594 0.29784 0.02072  0.04588  -0.02035 131 LYS   C CA    
3715 C  C     . LYS   C 132 ? 0.25213 0.27055 0.31033 0.01644  0.04231  -0.02121 131 LYS   C C     
3716 O  O     . LYS   C 132 ? 0.28611 0.30670 0.35413 0.01610  0.04284  -0.01815 131 LYS   C O     
3717 C  CB    . LYS   C 132 ? 0.28950 0.30383 0.33077 0.02243  0.04557  -0.02298 131 LYS   C CB    
3718 C  CG    . LYS   C 132 ? 0.39517 0.41048 0.44205 0.02215  0.04590  -0.02203 131 LYS   C CG    
3719 C  CD    . LYS   C 132 ? 0.51081 0.52240 0.54875 0.02303  0.04436  -0.02574 131 LYS   C CD    
3720 C  CE    . LYS   C 132 ? 0.51439 0.52669 0.55631 0.02376  0.04546  -0.02457 131 LYS   C CE    
3721 N  NZ    . LYS   C 132 ? 0.62788 0.63631 0.66120 0.02433  0.04340  -0.02844 131 LYS   C NZ    
3722 N  N     . VAL   C 133 ? 0.24031 0.25687 0.29512 0.01361  0.03854  -0.02505 132 VAL   C N     
3723 C  CA    . VAL   C 133 ? 0.25599 0.27208 0.31618 0.01048  0.03470  -0.02666 132 VAL   C CA    
3724 C  C     . VAL   C 133 ? 0.28187 0.29716 0.34357 0.01033  0.03400  -0.02748 132 VAL   C C     
3725 O  O     . VAL   C 133 ? 0.28961 0.30332 0.34455 0.01120  0.03440  -0.02951 132 VAL   C O     
3726 C  CB    . VAL   C 133 ? 0.25895 0.27308 0.31338 0.00859  0.03164  -0.03028 132 VAL   C CB    
3727 C  CG1   . VAL   C 133 ? 0.24266 0.25538 0.30041 0.00657  0.02785  -0.03214 132 VAL   C CG1   
3728 C  CG2   . VAL   C 133 ? 0.24662 0.26175 0.30139 0.00847  0.03203  -0.02915 132 VAL   C CG2   
3729 N  N     . LYS   C 134 ? 0.28415 0.30019 0.35511 0.00922  0.03249  -0.02590 133 LYS   C N     
3730 C  CA    . LYS   C 134 ? 0.35036 0.36558 0.42363 0.00893  0.03149  -0.02660 133 LYS   C CA    
3731 C  C     . LYS   C 134 ? 0.38286 0.39521 0.45490 0.00674  0.02679  -0.03033 133 LYS   C C     
3732 O  O     . LYS   C 134 ? 0.45505 0.46580 0.52238 0.00657  0.02603  -0.03290 133 LYS   C O     
3733 C  CB    . LYS   C 134 ? 0.33108 0.34880 0.41610 0.00957  0.03282  -0.02186 133 LYS   C CB    
3734 C  CG    . LYS   C 134 ? 0.46723 0.48444 0.55661 0.00931  0.03185  -0.02181 133 LYS   C CG    
3735 C  CD    . LYS   C 134 ? 0.44647 0.46674 0.54931 0.00998  0.03330  -0.01603 133 LYS   C CD    
3736 C  CE    . LYS   C 134 ? 0.45386 0.47393 0.56194 0.00989  0.03262  -0.01539 133 LYS   C CE    
3737 N  NZ    . LYS   C 134 ? 0.59788 0.62123 0.72108 0.01036  0.03369  -0.00900 133 LYS   C NZ    
3738 N  N     . GLU   C 135 ? 0.34040 0.35179 0.41579 0.00554  0.02369  -0.03062 134 GLU   C N     
3739 C  CA    . GLU   C 135 ? 0.33850 0.34652 0.41150 0.00456  0.01927  -0.03389 134 GLU   C CA    
3740 C  C     . GLU   C 135 ? 0.29703 0.30432 0.36696 0.00433  0.01796  -0.03471 134 GLU   C C     
3741 O  O     . GLU   C 135 ? 0.31217 0.32126 0.38567 0.00434  0.01908  -0.03238 134 GLU   C O     
3742 C  CB    . GLU   C 135 ? 0.37804 0.38403 0.45934 0.00406  0.01530  -0.03341 134 GLU   C CB    
3743 C  CG    . GLU   C 135 ? 0.40743 0.41390 0.49219 0.00419  0.01615  -0.03271 134 GLU   C CG    
3744 C  CD    . GLU   C 135 ? 0.58091 0.58401 0.66027 0.00412  0.01346  -0.03643 134 GLU   C CD    
3745 O  OE1   . GLU   C 135 ? 0.63174 0.63508 0.70293 0.00440  0.01544  -0.03840 134 GLU   C OE1   
3746 O  OE2   . GLU   C 135 ? 0.63796 0.63787 0.72146 0.00397  0.00905  -0.03726 134 GLU   C OE2   
3747 N  N     . GLY   C 136 ? 0.32381 0.32853 0.38741 0.00441  0.01572  -0.03767 135 GLY   C N     
3748 C  CA    . GLY   C 136 ? 0.33344 0.33721 0.39388 0.00462  0.01442  -0.03834 135 GLY   C CA    
3749 C  C     . GLY   C 136 ? 0.28700 0.29285 0.34152 0.00455  0.01741  -0.03834 135 GLY   C C     
3750 O  O     . GLY   C 136 ? 0.29502 0.30107 0.34843 0.00460  0.01715  -0.03801 135 GLY   C O     
3751 N  N     . MET   C 137 ? 0.27019 0.27715 0.32092 0.00452  0.01972  -0.03877 136 MET   C N     
3752 C  CA    . MET   C 137 ? 0.28087 0.28884 0.32613 0.00449  0.02137  -0.03898 136 MET   C CA    
3753 C  C     . MET   C 137 ? 0.30766 0.31451 0.34910 0.00459  0.01974  -0.04013 136 MET   C C     
3754 O  O     . MET   C 137 ? 0.27446 0.28218 0.31337 0.00448  0.02043  -0.03971 136 MET   C O     
3755 C  CB    . MET   C 137 ? 0.29526 0.30343 0.33717 0.00465  0.02286  -0.03953 136 MET   C CB    
3756 C  CG    . MET   C 137 ? 0.43007 0.43862 0.46709 0.00477  0.02386  -0.03954 136 MET   C CG    
3757 S  SD    . MET   C 137 ? 0.35413 0.36407 0.39169 0.00572  0.02620  -0.03753 136 MET   C SD    
3758 C  CE    . MET   C 137 ? 0.33024 0.33979 0.36268 0.00527  0.02541  -0.03817 136 MET   C CE    
3759 N  N     . ASN   C 138 ? 0.28410 0.28884 0.32496 0.00525  0.01762  -0.04132 137 ASN   C N     
3760 C  CA    . ASN   C 138 ? 0.31429 0.31796 0.35104 0.00636  0.01666  -0.04175 137 ASN   C CA    
3761 C  C     . ASN   C 138 ? 0.29676 0.29981 0.33391 0.00694  0.01561  -0.04129 137 ASN   C C     
3762 O  O     . ASN   C 138 ? 0.31777 0.32078 0.35127 0.00791  0.01577  -0.04102 137 ASN   C O     
3763 C  CB    . ASN   C 138 ? 0.35091 0.35177 0.38601 0.00794  0.01468  -0.04300 137 ASN   C CB    
3764 C  CG    . ASN   C 138 ? 0.32693 0.32460 0.36503 0.00878  0.01149  -0.04382 137 ASN   C CG    
3765 O  OD1   . ASN   C 138 ? 0.34312 0.34134 0.38689 0.00750  0.01116  -0.04331 137 ASN   C OD1   
3766 N  ND2   . ASN   C 138 ? 0.36436 0.35843 0.39885 0.01129  0.00894  -0.04479 137 ASN   C ND2   
3767 N  N     . ILE   C 139 ? 0.28612 0.28871 0.32825 0.00648  0.01446  -0.04086 138 ILE   C N     
3768 C  CA    . ILE   C 139 ? 0.28192 0.28388 0.32527 0.00681  0.01315  -0.04028 138 ILE   C CA    
3769 C  C     . ILE   C 139 ? 0.27483 0.27999 0.31741 0.00580  0.01605  -0.03894 138 ILE   C C     
3770 O  O     . ILE   C 139 ? 0.29502 0.30014 0.33501 0.00630  0.01588  -0.03878 138 ILE   C O     
3771 C  CB    . ILE   C 139 ? 0.28863 0.28935 0.33941 0.00640  0.01073  -0.03958 138 ILE   C CB    
3772 C  CG1   . ILE   C 139 ? 0.31662 0.31317 0.36766 0.00764  0.00696  -0.04125 138 ILE   C CG1   
3773 C  CG2   . ILE   C 139 ? 0.32613 0.32635 0.37908 0.00652  0.00921  -0.03872 138 ILE   C CG2   
3774 C  CD1   . ILE   C 139 ? 0.33042 0.32287 0.37412 0.01037  0.00434  -0.04314 138 ILE   C CD1   
3775 N  N     . VAL   C 140 ? 0.25662 0.26416 0.30076 0.00479  0.01862  -0.03799 139 VAL   C N     
3776 C  CA    . VAL   C 140 ? 0.28695 0.29667 0.32918 0.00437  0.02104  -0.03699 139 VAL   C CA    
3777 C  C     . VAL   C 140 ? 0.31519 0.32491 0.35205 0.00443  0.02114  -0.03769 139 VAL   C C     
3778 O  O     . VAL   C 140 ? 0.29833 0.30883 0.33357 0.00435  0.02158  -0.03710 139 VAL   C O     
3779 C  CB    . VAL   C 140 ? 0.25914 0.27022 0.30216 0.00437  0.02350  -0.03611 139 VAL   C CB    
3780 C  CG1   . VAL   C 140 ? 0.29612 0.30822 0.33535 0.00461  0.02540  -0.03554 139 VAL   C CG1   
3781 C  CG2   . VAL   C 140 ? 0.26937 0.28132 0.31931 0.00460  0.02406  -0.03416 139 VAL   C CG2   
3782 N  N     . GLU   C 141 ? 0.29753 0.30655 0.33234 0.00460  0.02072  -0.03855 140 GLU   C N     
3783 C  CA    . GLU   C 141 ? 0.32276 0.33221 0.35432 0.00477  0.02081  -0.03828 140 GLU   C CA    
3784 C  C     . GLU   C 141 ? 0.33444 0.34325 0.36453 0.00608  0.02000  -0.03789 140 GLU   C C     
3785 O  O     . GLU   C 141 ? 0.31603 0.32599 0.34452 0.00621  0.02065  -0.03678 140 GLU   C O     
3786 C  CB    . GLU   C 141 ? 0.31816 0.32715 0.34889 0.00490  0.02051  -0.03871 140 GLU   C CB    
3787 C  CG    . GLU   C 141 ? 0.31985 0.32899 0.35090 0.00394  0.02100  -0.03918 140 GLU   C CG    
3788 C  CD    . GLU   C 141 ? 0.55293 0.56123 0.58411 0.00410  0.02039  -0.03991 140 GLU   C CD    
3789 O  OE1   . GLU   C 141 ? 0.54923 0.55709 0.57985 0.00508  0.01984  -0.03972 140 GLU   C OE1   
3790 O  OE2   . GLU   C 141 ? 0.55412 0.56199 0.58549 0.00369  0.02058  -0.04059 140 GLU   C OE2   
3791 N  N     . ALA   C 142 ? 0.29465 0.30118 0.32510 0.00741  0.01826  -0.03874 141 ALA   C N     
3792 C  CA    . ALA   C 142 ? 0.32705 0.33199 0.35459 0.00953  0.01717  -0.03858 141 ALA   C CA    
3793 C  C     . ALA   C 142 ? 0.34197 0.34780 0.37041 0.00891  0.01732  -0.03792 141 ALA   C C     
3794 O  O     . ALA   C 142 ? 0.35701 0.36248 0.38252 0.01041  0.01725  -0.03733 141 ALA   C O     
3795 C  CB    . ALA   C 142 ? 0.33321 0.33407 0.35999 0.01168  0.01420  -0.04004 141 ALA   C CB    
3796 N  N     . MET   C 143 ? 0.30545 0.31250 0.33788 0.00708  0.01777  -0.03772 142 MET   C N     
3797 C  CA    . MET   C 143 ? 0.28742 0.29559 0.32107 0.00647  0.01822  -0.03683 142 MET   C CA    
3798 C  C     . MET   C 143 ? 0.28653 0.29685 0.31731 0.00599  0.02015  -0.03591 142 MET   C C     
3799 O  O     . MET   C 143 ? 0.28329 0.29400 0.31320 0.00624  0.02018  -0.03530 142 MET   C O     
3800 C  CB    . MET   C 143 ? 0.30709 0.31652 0.34592 0.00516  0.01900  -0.03603 142 MET   C CB    
3801 C  CG    . MET   C 143 ? 0.35628 0.36366 0.40015 0.00548  0.01638  -0.03618 142 MET   C CG    
3802 S  SD    . MET   C 143 ? 0.38685 0.39646 0.43840 0.00438  0.01803  -0.03405 142 MET   C SD    
3803 C  CE    . MET   C 143 ? 0.30673 0.31872 0.35847 0.00406  0.02012  -0.03226 142 MET   C CE    
3804 N  N     . GLU   C 144 ? 0.33261 0.34399 0.36226 0.00532  0.02128  -0.03577 143 GLU   C N     
3805 C  CA    . GLU   C 144 ? 0.34751 0.36047 0.37563 0.00470  0.02224  -0.03471 143 GLU   C CA    
3806 C  C     . GLU   C 144 ? 0.40171 0.41502 0.42805 0.00596  0.02220  -0.03352 143 GLU   C C     
3807 O  O     . GLU   C 144 ? 0.39295 0.40766 0.41904 0.00542  0.02278  -0.03228 143 GLU   C O     
3808 C  CB    . GLU   C 144 ? 0.35076 0.36395 0.37874 0.00395  0.02234  -0.03473 143 GLU   C CB    
3809 C  CG    . GLU   C 144 ? 0.34860 0.36132 0.37681 0.00321  0.02270  -0.03557 143 GLU   C CG    
3810 C  CD    . GLU   C 144 ? 0.44514 0.45735 0.47231 0.00262  0.02190  -0.03556 143 GLU   C CD    
3811 O  OE1   . GLU   C 144 ? 0.59345 0.60579 0.62145 0.00253  0.02119  -0.03516 143 GLU   C OE1   
3812 O  OE2   . GLU   C 144 ? 0.39658 0.40787 0.42205 0.00254  0.02167  -0.03585 143 GLU   C OE2   
3813 N  N     . ARG   C 145 ? 0.36052 0.37236 0.38527 0.00806  0.02155  -0.03366 144 ARG   C N     
3814 C  CA    . ARG   C 145 ? 0.39191 0.40390 0.41411 0.01033  0.02202  -0.03208 144 ARG   C CA    
3815 C  C     . ARG   C 145 ? 0.40121 0.41307 0.42246 0.01070  0.02180  -0.03191 144 ARG   C C     
3816 O  O     . ARG   C 145 ? 0.46727 0.47986 0.48659 0.01237  0.02265  -0.03017 144 ARG   C O     
3817 C  CB    . ARG   C 145 ? 0.39430 0.40352 0.41338 0.01358  0.02113  -0.03262 144 ARG   C CB    
3818 C  CG    . ARG   C 145 ? 0.45248 0.46148 0.47242 0.01338  0.02117  -0.03305 144 ARG   C CG    
3819 C  CD    . ARG   C 145 ? 0.49056 0.49573 0.50690 0.01676  0.01958  -0.03431 144 ARG   C CD    
3820 N  NE    . ARG   C 145 ? 0.53981 0.54523 0.55576 0.01772  0.02044  -0.03363 144 ARG   C NE    
3821 C  CZ    . ARG   C 145 ? 0.64764 0.64974 0.66106 0.02003  0.01900  -0.03507 144 ARG   C CZ    
3822 N  NH1   . ARG   C 145 ? 0.61074 0.60860 0.62237 0.02139  0.01598  -0.03746 144 ARG   C NH1   
3823 N  NH2   . ARG   C 145 ? 0.68738 0.69019 0.70048 0.02105  0.02022  -0.03397 144 ARG   C NH2   
3824 N  N     . PHE   C 146 ? 0.31228 0.32334 0.33525 0.00943  0.02078  -0.03330 145 PHE   C N     
3825 C  CA    . PHE   C 146 ? 0.32497 0.33567 0.34760 0.00973  0.02021  -0.03320 145 PHE   C CA    
3826 C  C     . PHE   C 146 ? 0.33069 0.34392 0.35526 0.00736  0.02161  -0.03245 145 PHE   C C     
3827 O  O     . PHE   C 146 ? 0.32934 0.34265 0.35427 0.00722  0.02136  -0.03228 145 PHE   C O     
3828 C  CB    . PHE   C 146 ? 0.36179 0.36958 0.38601 0.01027  0.01762  -0.03471 145 PHE   C CB    
3829 C  CG    . PHE   C 146 ? 0.38707 0.39118 0.40857 0.01303  0.01544  -0.03588 145 PHE   C CG    
3830 C  CD1   . PHE   C 146 ? 0.37667 0.37821 0.39273 0.01664  0.01452  -0.03581 145 PHE   C CD1   
3831 C  CD2   . PHE   C 146 ? 0.36584 0.36890 0.38943 0.01251  0.01456  -0.03690 145 PHE   C CD2   
3832 C  CE1   . PHE   C 146 ? 0.47751 0.47488 0.48963 0.02005  0.01244  -0.03695 145 PHE   C CE1   
3833 C  CE2   . PHE   C 146 ? 0.36231 0.36147 0.38273 0.01537  0.01232  -0.03811 145 PHE   C CE2   
3834 C  CZ    . PHE   C 146 ? 0.37991 0.37604 0.39428 0.01928  0.01122  -0.03820 145 PHE   C CZ    
3835 N  N     . GLY   C 147 ? 0.34308 0.35786 0.36852 0.00581  0.02272  -0.03210 146 GLY   C N     
3836 C  CA    . GLY   C 147 ? 0.31112 0.32723 0.33711 0.00427  0.02358  -0.03166 146 GLY   C CA    
3837 C  C     . GLY   C 147 ? 0.33656 0.35396 0.36168 0.00406  0.02388  -0.03013 146 GLY   C C     
3838 O  O     . GLY   C 147 ? 0.32862 0.34651 0.35316 0.00529  0.02402  -0.02883 146 GLY   C O     
3839 N  N     . SER   C 148 ? 0.28678 0.30454 0.31188 0.00286  0.02397  -0.02998 147 SER   C N     
3840 C  CA    . SER   C 148 ? 0.29879 0.31754 0.32410 0.00239  0.02367  -0.02839 147 SER   C CA    
3841 C  C     . SER   C 148 ? 0.31763 0.33524 0.34222 0.00138  0.02274  -0.02899 147 SER   C C     
3842 O  O     . SER   C 148 ? 0.30198 0.31827 0.32511 0.00159  0.02303  -0.03043 147 SER   C O     
3843 C  CB    . SER   C 148 ? 0.28859 0.30824 0.31325 0.00294  0.02428  -0.02759 147 SER   C CB    
3844 O  OG    . SER   C 148 ? 0.31592 0.33514 0.33983 0.00244  0.02458  -0.02855 147 SER   C OG    
3845 N  N     . ARG   C 149 ? 0.30195 0.31980 0.32749 0.00071  0.02153  -0.02762 148 ARG   C N     
3846 C  CA    . ARG   C 149 ? 0.31978 0.33529 0.34400 0.00021  0.01950  -0.02834 148 ARG   C CA    
3847 C  C     . ARG   C 149 ? 0.28520 0.29935 0.30565 0.00102  0.02042  -0.02980 148 ARG   C C     
3848 O  O     . ARG   C 149 ? 0.32597 0.33739 0.34330 0.00191  0.01966  -0.03117 148 ARG   C O     
3849 C  CB    . ARG   C 149 ? 0.35795 0.37386 0.38492 -0.00069 0.01753  -0.02627 148 ARG   C CB    
3850 C  CG    . ARG   C 149 ? 0.39185 0.40417 0.41730 -0.00095 0.01419  -0.02720 148 ARG   C CG    
3851 C  CD    . ARG   C 149 ? 0.41688 0.42952 0.44773 -0.00223 0.01120  -0.02456 148 ARG   C CD    
3852 N  NE    . ARG   C 149 ? 0.42959 0.43762 0.45840 -0.00220 0.00698  -0.02583 148 ARG   C NE    
3853 C  CZ    . ARG   C 149 ? 0.38849 0.39499 0.41405 -0.00170 0.00652  -0.02657 148 ARG   C CZ    
3854 N  NH1   . ARG   C 149 ? 0.44763 0.45731 0.47270 -0.00163 0.00993  -0.02589 148 ARG   C NH1   
3855 N  NH2   . ARG   C 149 ? 0.39193 0.39314 0.41434 -0.00098 0.00221  -0.02809 148 ARG   C NH2   
3856 N  N     . ASN   C 150 ? 0.30203 0.31785 0.32249 0.00119  0.02214  -0.02934 149 ASN   C N     
3857 C  CA    . ASN   C 150 ? 0.34288 0.35788 0.36067 0.00215  0.02340  -0.03004 149 ASN   C CA    
3858 C  C     . ASN   C 150 ? 0.35720 0.37317 0.37608 0.00284  0.02553  -0.03028 149 ASN   C C     
3859 O  O     . ASN   C 150 ? 0.34522 0.36118 0.36322 0.00385  0.02710  -0.03002 149 ASN   C O     
3860 C  CB    . ASN   C 150 ? 0.36497 0.38088 0.38248 0.00190  0.02365  -0.02919 149 ASN   C CB    
3861 C  CG    . ASN   C 150 ? 0.47126 0.48960 0.49098 0.00173  0.02517  -0.02845 149 ASN   C CG    
3862 O  OD1   . ASN   C 150 ? 0.35158 0.37065 0.37307 0.00182  0.02547  -0.02851 149 ASN   C OD1   
3863 N  ND2   . ASN   C 150 ? 0.44543 0.46444 0.46464 0.00173  0.02569  -0.02787 149 ASN   C ND2   
3864 N  N     . GLY   C 151 ? 0.30647 0.32319 0.32770 0.00251  0.02552  -0.03045 150 GLY   C N     
3865 C  CA    . GLY   C 151 ? 0.25955 0.27671 0.28283 0.00303  0.02673  -0.03056 150 GLY   C CA    
3866 C  C     . GLY   C 151 ? 0.31483 0.33304 0.34084 0.00290  0.02661  -0.03011 150 GLY   C C     
3867 O  O     . GLY   C 151 ? 0.27074 0.28881 0.29949 0.00314  0.02645  -0.03024 150 GLY   C O     
3868 N  N     . LYS   C 152 ? 0.32081 0.33963 0.34615 0.00271  0.02626  -0.02958 151 LYS   C N     
3869 C  CA    . LYS   C 152 ? 0.34554 0.36441 0.37242 0.00311  0.02553  -0.02941 151 LYS   C CA    
3870 C  C     . LYS   C 152 ? 0.33756 0.35529 0.36442 0.00388  0.02427  -0.03010 151 LYS   C C     
3871 O  O     . LYS   C 152 ? 0.30733 0.32514 0.33259 0.00406  0.02426  -0.03002 151 LYS   C O     
3872 C  CB    . LYS   C 152 ? 0.41480 0.43433 0.44000 0.00315  0.02542  -0.02872 151 LYS   C CB    
3873 C  CG    . LYS   C 152 ? 0.51597 0.53613 0.54222 0.00291  0.02603  -0.02814 151 LYS   C CG    
3874 C  CD    . LYS   C 152 ? 0.58531 0.60585 0.61074 0.00266  0.02758  -0.02779 151 LYS   C CD    
3875 C  CE    . LYS   C 152 ? 0.57908 0.60048 0.60580 0.00285  0.02865  -0.02672 151 LYS   C CE    
3876 N  NZ    . LYS   C 152 ? 0.55290 0.57408 0.57633 0.00332  0.02988  -0.02640 151 LYS   C NZ    
3877 N  N     . THR   C 153 ? 0.34040 0.35685 0.36950 0.00447  0.02297  -0.03057 152 THR   C N     
3878 C  CA    . THR   C 153 ? 0.33916 0.35361 0.36757 0.00572  0.02132  -0.03150 152 THR   C CA    
3879 C  C     . THR   C 153 ? 0.38326 0.39596 0.40848 0.00780  0.01983  -0.03163 152 THR   C C     
3880 O  O     . THR   C 153 ? 0.41967 0.43200 0.44492 0.00809  0.01909  -0.03137 152 THR   C O     
3881 C  CB    . THR   C 153 ? 0.39801 0.41107 0.43062 0.00561  0.01983  -0.03201 152 THR   C CB    
3882 O  OG1   . THR   C 153 ? 0.32256 0.33477 0.35831 0.00570  0.01814  -0.03158 152 THR   C OG1   
3883 C  CG2   . THR   C 153 ? 0.35952 0.37441 0.39477 0.00430  0.02192  -0.03143 152 THR   C CG2   
3884 N  N     . SER   C 154 ? 0.35996 0.37138 0.38207 0.00967  0.01949  -0.03187 153 SER   C N     
3885 C  CA    . SER   C 154 ? 0.43455 0.44387 0.45212 0.01285  0.01853  -0.03169 153 SER   C CA    
3886 C  C     . SER   C 154 ? 0.45570 0.46027 0.47195 0.01523  0.01491  -0.03343 153 SER   C C     
3887 O  O     . SER   C 154 ? 0.42007 0.42168 0.43149 0.01861  0.01344  -0.03365 153 SER   C O     
3888 C  CB    . SER   C 154 ? 0.44512 0.45545 0.45980 0.01457  0.02037  -0.03031 153 SER   C CB    
3889 O  OG    . SER   C 154 ? 0.42414 0.43326 0.43905 0.01494  0.01985  -0.03118 153 SER   C OG    
3890 N  N     . LYS   C 155 ? 0.40570 0.40907 0.42599 0.01391  0.01318  -0.03456 154 LYS   C N     
3891 C  CA    . LYS   C 155 ? 0.43653 0.43511 0.45778 0.01543  0.00868  -0.03610 154 LYS   C CA    
3892 C  C     . LYS   C 155 ? 0.43074 0.43076 0.46034 0.01226  0.00799  -0.03569 154 LYS   C C     
3893 O  O     . LYS   C 155 ? 0.42302 0.42707 0.45586 0.00974  0.01123  -0.03461 154 LYS   C O     
3894 C  CB    . LYS   C 155 ? 0.43198 0.42672 0.44958 0.01821  0.00676  -0.03750 154 LYS   C CB    
3895 C  CG    . LYS   C 155 ? 0.37909 0.37217 0.38817 0.02250  0.00777  -0.03721 154 LYS   C CG    
3896 C  CD    . LYS   C 155 ? 0.51667 0.50490 0.52117 0.02620  0.00544  -0.03866 154 LYS   C CD    
3897 C  CE    . LYS   C 155 ? 0.49352 0.48003 0.48901 0.03159  0.00702  -0.03764 154 LYS   C CE    
3898 N  NZ    . LYS   C 155 ? 0.58576 0.56790 0.57631 0.03550  0.00549  -0.03875 154 LYS   C NZ    
3899 N  N     . LYS   C 156 ? 0.41221 0.40866 0.44542 0.01277  0.00361  -0.03625 155 LYS   C N     
3900 C  CA    . LYS   C 156 ? 0.45872 0.45690 0.50153 0.01008  0.00301  -0.03480 155 LYS   C CA    
3901 C  C     . LYS   C 156 ? 0.38998 0.38790 0.43660 0.00940  0.00260  -0.03498 155 LYS   C C     
3902 O  O     . LYS   C 156 ? 0.33765 0.33080 0.38351 0.01116  -0.00162 -0.03660 155 LYS   C O     
3903 C  CB    . LYS   C 156 ? 0.42582 0.42019 0.47271 0.01075  -0.00220 -0.03483 155 LYS   C CB    
3904 C  CG    . LYS   C 156 ? 0.54165 0.53921 0.59924 0.00803  -0.00176 -0.03203 155 LYS   C CG    
3905 C  CD    . LYS   C 156 ? 0.57881 0.58229 0.63582 0.00633  0.00420  -0.03014 155 LYS   C CD    
3906 C  CE    . LYS   C 156 ? 0.49994 0.50612 0.56665 0.00463  0.00459  -0.02696 155 LYS   C CE    
3907 N  NZ    . LYS   C 156 ? 0.54886 0.55349 0.62564 0.00409  0.00101  -0.02552 155 LYS   C NZ    
3908 N  N     . ILE   C 157 ? 0.34461 0.34711 0.39497 0.00721  0.00669  -0.03338 156 ILE   C N     
3909 C  CA    . ILE   C 157 ? 0.33890 0.34163 0.39234 0.00664  0.00699  -0.03340 156 ILE   C CA    
3910 C  C     . ILE   C 157 ? 0.35372 0.35821 0.41785 0.00507  0.00667  -0.03073 156 ILE   C C     
3911 O  O     . ILE   C 157 ? 0.35643 0.36513 0.42354 0.00396  0.01054  -0.02833 156 ILE   C O     
3912 C  CB    . ILE   C 157 ? 0.36796 0.37409 0.41732 0.00595  0.01170  -0.03339 156 ILE   C CB    
3913 C  CG1   . ILE   C 157 ? 0.35107 0.35676 0.39185 0.00721  0.01270  -0.03473 156 ILE   C CG1   
3914 C  CG2   . ILE   C 157 ? 0.32689 0.33268 0.37879 0.00567  0.01161  -0.03370 156 ILE   C CG2   
3915 C  CD1   . ILE   C 157 ? 0.41946 0.42076 0.45536 0.00985  0.00959  -0.03661 156 ILE   C CD1   
3916 N  N     . THR   C 158 ? 0.31369 0.31494 0.38393 0.00528  0.00211  -0.03073 157 THR   C N     
3917 C  CA    . THR   C 158 ? 0.34110 0.34408 0.42353 0.00390  0.00124  -0.02728 157 THR   C CA    
3918 C  C     . THR   C 158 ? 0.32836 0.33154 0.41742 0.00338  0.00076  -0.02619 157 THR   C C     
3919 O  O     . THR   C 158 ? 0.33185 0.33220 0.41629 0.00419  -0.00079 -0.02880 157 THR   C O     
3920 C  CB    . THR   C 158 ? 0.35995 0.35870 0.44746 0.00430  -0.00512 -0.02720 157 THR   C CB    
3921 O  OG1   . THR   C 158 ? 0.35391 0.34590 0.43807 0.00608  -0.01126 -0.03042 157 THR   C OG1   
3922 C  CG2   . THR   C 158 ? 0.38819 0.38710 0.46998 0.00481  -0.00444 -0.02784 157 THR   C CG2   
3923 N  N     . ILE   C 159 ? 0.31170 0.31844 0.41221 0.00224  0.00228  -0.02183 158 ILE   C N     
3924 C  CA    . ILE   C 159 ? 0.29665 0.30392 0.40623 0.00174  0.00155  -0.01971 158 ILE   C CA    
3925 C  C     . ILE   C 159 ? 0.33931 0.34199 0.45861 0.00143  -0.00626 -0.01909 158 ILE   C C     
3926 O  O     . ILE   C 159 ? 0.33920 0.34381 0.46965 0.00056  -0.00713 -0.01500 158 ILE   C O     
3927 C  CB    . ILE   C 159 ? 0.26412 0.27779 0.38100 0.00142  0.00779  -0.01459 158 ILE   C CB    
3928 C  CG1   . ILE   C 159 ? 0.34138 0.35808 0.44724 0.00225  0.01433  -0.01573 158 ILE   C CG1   
3929 C  CG2   . ILE   C 159 ? 0.30363 0.31814 0.43069 0.00113  0.00724  -0.01180 158 ILE   C CG2   
3930 C  CD1   . ILE   C 159 ? 0.30087 0.32289 0.41108 0.00316  0.02066  -0.01098 158 ILE   C CD1   
3931 N  N     . ALA   C 160 ? 0.30359 0.29992 0.41802 0.00248  -0.01199 -0.02312 159 ALA   C N     
3932 C  CA    . ALA   C 160 ? 0.36727 0.35731 0.48877 0.00281  -0.02082 -0.02351 159 ALA   C CA    
3933 C  C     . ALA   C 160 ? 0.42510 0.41650 0.56313 0.00125  -0.02302 -0.01910 159 ALA   C C     
3934 O  O     . ALA   C 160 ? 0.40972 0.39867 0.55944 0.00059  -0.02904 -0.01671 159 ALA   C O     
3935 C  CB    . ALA   C 160 ? 0.42912 0.41131 0.53950 0.00529  -0.02620 -0.02903 159 ALA   C CB    
3936 N  N     . ASP   C 161 ? 0.35915 0.35441 0.49832 0.00078  -0.01825 -0.01782 160 ASP   C N     
3937 C  CA    . ASP   C 161 ? 0.40808 0.40591 0.56351 -0.00053 -0.01888 -0.01270 160 ASP   C CA    
3938 C  C     . ASP   C 161 ? 0.39068 0.39539 0.54509 -0.00058 -0.01002 -0.01022 160 ASP   C C     
3939 O  O     . ASP   C 161 ? 0.34020 0.34514 0.48105 0.00026  -0.00617 -0.01399 160 ASP   C O     
3940 C  CB    . ASP   C 161 ? 0.39206 0.38295 0.55179 -0.00031 -0.02733 -0.01477 160 ASP   C CB    
3941 C  CG    . ASP   C 161 ? 0.47911 0.47144 0.65886 -0.00187 -0.03049 -0.00893 160 ASP   C CG    
3942 O  OD1   . ASP   C 161 ? 0.47406 0.47242 0.66581 -0.00294 -0.02699 -0.00275 160 ASP   C OD1   
3943 O  OD2   . ASP   C 161 ? 0.56079 0.54825 0.74431 -0.00179 -0.03636 -0.01030 160 ASP   C OD2   
3944 N  N     . CYS   C 162 ? 0.41314 0.42303 0.58198 -0.00123 -0.00721 -0.00370 161 CYS   C N     
3945 C  CA    . CYS   C 162 ? 0.31707 0.33282 0.48509 -0.00045 0.00091  -0.00096 161 CYS   C CA    
3946 C  C     . CYS   C 162 ? 0.34898 0.36794 0.53531 -0.00090 0.00082  0.00585  161 CYS   C C     
3947 O  O     . CYS   C 162 ? 0.36970 0.38791 0.57044 -0.00201 -0.00421 0.00959  161 CYS   C O     
3948 C  CB    . CYS   C 162 ? 0.26454 0.28568 0.42660 0.00071  0.00888  0.00103  161 CYS   C CB    
3949 S  SG    . CYS   C 162 ? 0.37130 0.39510 0.54366 0.00031  0.00863  0.00607  161 CYS   C SG    
3950 N  N     . GLY   C 163 ? 0.29054 0.31279 0.47637 0.00007  0.00604  0.00749  162 GLY   C N     
3951 C  CA    . GLY   C 163 ? 0.30215 0.32845 0.50541 0.00013  0.00735  0.01485  162 GLY   C CA    
3952 C  C     . GLY   C 163 ? 0.33470 0.36411 0.53327 0.00183  0.01377  0.01556  162 GLY   C C     
3953 O  O     . GLY   C 163 ? 0.34106 0.37051 0.52359 0.00316  0.01830  0.01139  162 GLY   C O     
3954 N  N     . GLN   C 164 ? 0.33050 0.36251 0.54380 0.00190  0.01400  0.02124  163 GLN   C N     
3955 C  CA    . GLN   C 164 ? 0.32468 0.35972 0.53515 0.00383  0.02000  0.02271  163 GLN   C CA    
3956 C  C     . GLN   C 164 ? 0.37008 0.40050 0.58173 0.00222  0.01407  0.01900  163 GLN   C C     
3957 O  O     . GLN   C 164 ? 0.49431 0.52153 0.71847 0.00018  0.00636  0.01993  163 GLN   C O     
3958 C  CB    . GLN   C 164 ? 0.37224 0.41459 0.59823 0.00599  0.02632  0.03295  163 GLN   C CB    
3959 C  CG    . GLN   C 164 ? 0.28701 0.33248 0.50984 0.00878  0.03297  0.03507  163 GLN   C CG    
3960 C  CD    . GLN   C 164 ? 0.29682 0.34993 0.52984 0.01264  0.04168  0.04524  163 GLN   C CD    
3961 O  OE1   . GLN   C 164 ? 0.32009 0.37663 0.56436 0.01290  0.04267  0.05129  163 GLN   C OE1   
3962 N  NE2   . GLN   C 164 ? 0.32908 0.38478 0.55790 0.01607  0.04817  0.04738  163 GLN   C NE2   
3963 N  N     . LEU   C 165 ? 0.36855 0.39817 0.56728 0.00329  0.01720  0.01481  164 LEU   C N     
3964 C  CA    . LEU   C 165 ? 0.43722 0.46292 0.63689 0.00212  0.01240  0.01169  164 LEU   C CA    
3965 C  C     . LEU   C 165 ? 0.42254 0.45277 0.63613 0.00308  0.01570  0.01863  164 LEU   C C     
3966 O  O     . LEU   C 165 ? 0.52869 0.56051 0.73540 0.00476  0.02061  0.01801  164 LEU   C O     
3967 C  CB    . LEU   C 165 ? 0.44356 0.46607 0.62371 0.00262  0.01358  0.00399  164 LEU   C CB    
3968 C  CG    . LEU   C 165 ? 0.46803 0.48556 0.63700 0.00162  0.00905  -0.00234 164 LEU   C CG    
3969 C  CD1   . LEU   C 165 ? 0.41889 0.43361 0.56990 0.00212  0.01014  -0.00921 164 LEU   C CD1   
3970 C  CD2   . LEU   C 165 ? 0.42655 0.43841 0.60406 -0.00012 -0.00056 -0.00360 164 LEU   C CD2   
3971 N  N     . ASN   D 4   ? 0.39337 0.46726 0.53367 -0.01497 0.01586  0.05495  3   ASN   D N     
3972 C  CA    . ASN   D 4   ? 0.41593 0.48701 0.53833 -0.01404 0.01827  0.04803  3   ASN   D CA    
3973 C  C     . ASN   D 4   ? 0.32632 0.39334 0.43399 -0.01471 0.01585  0.04085  3   ASN   D C     
3974 O  O     . ASN   D 4   ? 0.36450 0.42760 0.47287 -0.01635 0.00841  0.03773  3   ASN   D O     
3975 C  CB    . ASN   D 4   ? 0.34992 0.41803 0.47347 -0.01486 0.01378  0.04542  3   ASN   D CB    
3976 C  CG    . ASN   D 4   ? 0.36824 0.44035 0.50061 -0.01353 0.01846  0.05108  3   ASN   D CG    
3977 O  OD1   . ASN   D 4   ? 0.37625 0.45309 0.51018 -0.01118 0.02633  0.05623  3   ASN   D OD1   
3978 N  ND2   . ASN   D 4   ? 0.28821 0.35818 0.42592 -0.01455 0.01370  0.05027  3   ASN   D ND2   
3979 N  N     . PRO   D 5   ? 0.33630 0.40386 0.43036 -0.01310 0.02192  0.03831  4   PRO   D N     
3980 C  CA    . PRO   D 5   ? 0.32599 0.39020 0.40657 -0.01363 0.02024  0.03207  4   PRO   D CA    
3981 C  C     . PRO   D 5   ? 0.34700 0.40660 0.41926 -0.01440 0.01548  0.02577  4   PRO   D C     
3982 O  O     . PRO   D 5   ? 0.35091 0.40993 0.42375 -0.01414 0.01525  0.02525  4   PRO   D O     
3983 C  CB    . PRO   D 5   ? 0.41844 0.48429 0.48821 -0.01144 0.02787  0.03176  4   PRO   D CB    
3984 C  CG    . PRO   D 5   ? 0.34240 0.41108 0.41637 -0.00936 0.03303  0.03601  4   PRO   D CG    
3985 C  CD    . PRO   D 5   ? 0.36426 0.43533 0.45546 -0.01028 0.03044  0.04169  4   PRO   D CD    
3986 N  N     A THR   D 6   ? 0.33609 0.39247 0.40055 -0.01501 0.01186  0.02128  5   THR   D N     
3987 N  N     B THR   D 6   ? 0.33606 0.39243 0.40057 -0.01501 0.01182  0.02127  5   THR   D N     
3988 C  CA    A THR   D 6   ? 0.34592 0.39794 0.40057 -0.01491 0.00808  0.01549  5   THR   D CA    
3989 C  CA    B THR   D 6   ? 0.34572 0.39781 0.40038 -0.01488 0.00825  0.01553  5   THR   D CA    
3990 C  C     A THR   D 6   ? 0.36584 0.41757 0.40711 -0.01434 0.01163  0.01192  5   THR   D C     
3991 C  C     B THR   D 6   ? 0.36577 0.41747 0.40712 -0.01434 0.01156  0.01191  5   THR   D C     
3992 O  O     A THR   D 6   ? 0.36445 0.41724 0.40393 -0.01452 0.01317  0.01241  5   THR   D O     
3993 O  O     B THR   D 6   ? 0.36459 0.41728 0.40434 -0.01455 0.01289  0.01240  5   THR   D O     
3994 C  CB    A THR   D 6   ? 0.35660 0.40429 0.41393 -0.01537 -0.00016 0.01363  5   THR   D CB    
3995 C  CB    B THR   D 6   ? 0.35669 0.40434 0.41417 -0.01531 -0.00012 0.01361  5   THR   D CB    
3996 O  OG1   A THR   D 6   ? 0.39525 0.44267 0.46654 -0.01609 -0.00459 0.01720  5   THR   D OG1   
3997 O  OG1   B THR   D 6   ? 0.37507 0.42248 0.43151 -0.01571 -0.00130 0.01345  5   THR   D OG1   
3998 C  CG2   A THR   D 6   ? 0.34788 0.39091 0.39413 -0.01416 -0.00343 0.00814  5   THR   D CG2   
3999 C  CG2   B THR   D 6   ? 0.39410 0.44154 0.46638 -0.01606 -0.00466 0.01744  5   THR   D CG2   
4000 N  N     . VAL   D 7   ? 0.32159 0.37191 0.35416 -0.01369 0.01275  0.00859  6   VAL   D N     
4001 C  CA    . VAL   D 7   ? 0.30999 0.35971 0.33121 -0.01328 0.01512  0.00542  6   VAL   D CA    
4002 C  C     . VAL   D 7   ? 0.30825 0.35459 0.32307 -0.01263 0.01147  0.00162  6   VAL   D C     
4003 O  O     . VAL   D 7   ? 0.30155 0.34594 0.31907 -0.01217 0.00814  0.00114  6   VAL   D O     
4004 C  CB    . VAL   D 7   ? 0.36069 0.41219 0.37731 -0.01264 0.02086  0.00579  6   VAL   D CB    
4005 C  CG1   . VAL   D 7   ? 0.35860 0.41280 0.37874 -0.01214 0.02497  0.00943  6   VAL   D CG1   
4006 C  CG2   . VAL   D 7   ? 0.34295 0.39451 0.36182 -0.01223 0.02142  0.00620  6   VAL   D CG2   
4007 N  N     . PHE   D 8   ? 0.31838 0.36400 0.32467 -0.01223 0.01231  -0.00075 7   PHE   D N     
4008 C  CA    . PHE   D 8   ? 0.31000 0.35291 0.30940 -0.01085 0.00997  -0.00364 7   PHE   D CA    
4009 C  C     . PHE   D 8   ? 0.35171 0.39577 0.34426 -0.01070 0.01383  -0.00469 7   PHE   D C     
4010 O  O     . PHE   D 8   ? 0.29077 0.33665 0.28214 -0.01159 0.01708  -0.00401 7   PHE   D O     
4011 C  CB    . PHE   D 8   ? 0.35680 0.39723 0.35336 -0.00990 0.00611  -0.00498 7   PHE   D CB    
4012 C  CG    . PHE   D 8   ? 0.38231 0.42432 0.37508 -0.01053 0.00859  -0.00503 7   PHE   D CG    
4013 C  CD1   . PHE   D 8   ? 0.42833 0.47212 0.42568 -0.01197 0.00948  -0.00322 7   PHE   D CD1   
4014 C  CD2   . PHE   D 8   ? 0.36837 0.41018 0.35353 -0.00952 0.01004  -0.00649 7   PHE   D CD2   
4015 C  CE1   . PHE   D 8   ? 0.41041 0.45532 0.40382 -0.01243 0.01157  -0.00346 7   PHE   D CE1   
4016 C  CE2   . PHE   D 8   ? 0.40794 0.45108 0.39017 -0.01020 0.01200  -0.00642 7   PHE   D CE2   
4017 C  CZ    . PHE   D 8   ? 0.42724 0.47169 0.41316 -0.01167 0.01261  -0.00520 7   PHE   D CZ    
4018 N  N     . PHE   D 9   ? 0.32854 0.37115 0.31683 -0.00931 0.01308  -0.00615 8   PHE   D N     
4019 C  CA    . PHE   D 9   ? 0.29674 0.34006 0.27929 -0.00884 0.01557  -0.00684 8   PHE   D CA    
4020 C  C     . PHE   D 9   ? 0.30344 0.34480 0.28089 -0.00648 0.01340  -0.00787 8   PHE   D C     
4021 O  O     . PHE   D 9   ? 0.30587 0.34464 0.28244 -0.00445 0.01046  -0.00865 8   PHE   D O     
4022 C  CB    . PHE   D 9   ? 0.31196 0.35564 0.29440 -0.00866 0.01714  -0.00688 8   PHE   D CB    
4023 C  CG    . PHE   D 9   ? 0.28273 0.32795 0.26825 -0.01010 0.01984  -0.00591 8   PHE   D CG    
4024 C  CD1   . PHE   D 9   ? 0.30672 0.35310 0.29416 -0.01111 0.02153  -0.00480 8   PHE   D CD1   
4025 C  CD2   . PHE   D 9   ? 0.32110 0.36634 0.30699 -0.00989 0.02083  -0.00599 8   PHE   D CD2   
4026 C  CE1   . PHE   D 9   ? 0.33592 0.38315 0.32487 -0.01130 0.02426  -0.00372 8   PHE   D CE1   
4027 C  CE2   . PHE   D 9   ? 0.28893 0.33508 0.27661 -0.01051 0.02331  -0.00513 8   PHE   D CE2   
4028 C  CZ    . PHE   D 9   ? 0.30362 0.35062 0.29255 -0.01093 0.02507  -0.00395 8   PHE   D CZ    
4029 N  N     . ASP   D 10  ? 0.32627 0.36855 0.29998 -0.00625 0.01487  -0.00771 9   ASP   D N     
4030 C  CA    . ASP   D 10  ? 0.37290 0.41394 0.34132 -0.00327 0.01416  -0.00788 9   ASP   D CA    
4031 C  C     . ASP   D 10  ? 0.34240 0.38505 0.30971 -0.00281 0.01692  -0.00689 9   ASP   D C     
4032 O  O     . ASP   D 10  ? 0.33323 0.37809 0.30182 -0.00474 0.01933  -0.00600 9   ASP   D O     
4033 C  CB    . ASP   D 10  ? 0.39365 0.43506 0.35945 -0.00295 0.01426  -0.00761 9   ASP   D CB    
4034 C  CG    . ASP   D 10  ? 0.42243 0.46164 0.38886 -0.00274 0.01079  -0.00858 9   ASP   D CG    
4035 O  OD1   . ASP   D 10  ? 0.46090 0.49671 0.42620 -0.00047 0.00710  -0.00960 9   ASP   D OD1   
4036 O  OD2   . ASP   D 10  ? 0.45847 0.49899 0.42682 -0.00481 0.01134  -0.00829 9   ASP   D OD2   
4037 N  N     . ILE   D 11  ? 0.30891 0.35007 0.27402 -0.00010 0.01619  -0.00699 10  ILE   D N     
4038 C  CA    . ILE   D 11  ? 0.30134 0.34412 0.26651 0.00035  0.01868  -0.00571 10  ILE   D CA    
4039 C  C     . ILE   D 11  ? 0.32747 0.37117 0.28913 0.00327  0.02029  -0.00372 10  ILE   D C     
4040 O  O     . ILE   D 11  ? 0.32331 0.36492 0.28017 0.00694  0.01898  -0.00383 10  ILE   D O     
4041 C  CB    . ILE   D 11  ? 0.33443 0.37531 0.29948 0.00186  0.01737  -0.00654 10  ILE   D CB    
4042 C  CG1   . ILE   D 11  ? 0.30863 0.34915 0.27853 -0.00099 0.01614  -0.00771 10  ILE   D CG1   
4043 C  CG2   . ILE   D 11  ? 0.29435 0.33687 0.25947 0.00264  0.01987  -0.00502 10  ILE   D CG2   
4044 C  CD1   . ILE   D 11  ? 0.31944 0.36258 0.29295 -0.00425 0.01889  -0.00708 10  ILE   D CD1   
4045 N  N     . ALA   D 12  ? 0.29769 0.34430 0.26196 0.00202  0.02297  -0.00160 11  ALA   D N     
4046 C  CA    . ALA   D 12  ? 0.33670 0.38501 0.29968 0.00493  0.02507  0.00149  11  ALA   D CA    
4047 C  C     . ALA   D 12  ? 0.33400 0.38390 0.29955 0.00549  0.02692  0.00355  11  ALA   D C     
4048 O  O     . ALA   D 12  ? 0.31343 0.36362 0.28250 0.00256  0.02674  0.00264  11  ALA   D O     
4049 C  CB    . ALA   D 12  ? 0.32671 0.37739 0.29232 0.00293  0.02622  0.00321  11  ALA   D CB    
4050 N  N     . VAL   D 13  ? 0.30470 0.35568 0.26841 0.00968  0.02889  0.00671  12  VAL   D N     
4051 C  CA    . VAL   D 13  ? 0.34417 0.39711 0.31066 0.01101  0.03107  0.00967  12  VAL   D CA    
4052 C  C     . VAL   D 13  ? 0.38631 0.44301 0.35686 0.01194  0.03378  0.01469  12  VAL   D C     
4053 O  O     . VAL   D 13  ? 0.38534 0.44241 0.35219 0.01633  0.03532  0.01704  12  VAL   D O     
4054 C  CB    . VAL   D 13  ? 0.34211 0.39267 0.30256 0.01637  0.03119  0.00958  12  VAL   D CB    
4055 C  CG1   . VAL   D 13  ? 0.34058 0.39366 0.30426 0.01807  0.03397  0.01330  12  VAL   D CG1   
4056 C  CG2   . VAL   D 13  ? 0.38106 0.42757 0.33848 0.01549  0.02776  0.00487  12  VAL   D CG2   
4057 N  N     . ASP   D 14  ? 0.37851 0.43769 0.35679 0.00826  0.03415  0.01660  13  ASP   D N     
4058 C  CA    . ASP   D 14  ? 0.41436 0.47712 0.39903 0.00800  0.03581  0.02158  13  ASP   D CA    
4059 C  C     . ASP   D 14  ? 0.47462 0.53744 0.45698 0.00839  0.03568  0.02156  13  ASP   D C     
4060 O  O     . ASP   D 14  ? 0.46616 0.53169 0.45048 0.01108  0.03798  0.02620  13  ASP   D O     
4061 C  CB    . ASP   D 14  ? 0.41892 0.48468 0.40585 0.01259  0.03925  0.02734  13  ASP   D CB    
4062 C  CG    . ASP   D 14  ? 0.46740 0.53459 0.46127 0.01062  0.03930  0.02913  13  ASP   D CG    
4063 O  OD1   . ASP   D 14  ? 0.45113 0.51697 0.44847 0.00561  0.03649  0.02623  13  ASP   D OD1   
4064 O  OD2   . ASP   D 14  ? 0.54560 0.61501 0.54111 0.01444  0.04214  0.03354  13  ASP   D OD2   
4065 N  N     . GLY   D 15  ? 0.45727 0.51731 0.43590 0.00583  0.03319  0.01673  14  GLY   D N     
4066 C  CA    . GLY   D 15  ? 0.46040 0.52009 0.43653 0.00580  0.03267  0.01605  14  GLY   D CA    
4067 C  C     . GLY   D 15  ? 0.43815 0.49593 0.40609 0.01064  0.03295  0.01518  14  GLY   D C     
4068 O  O     . GLY   D 15  ? 0.61819 0.67489 0.58330 0.01031  0.03183  0.01360  14  GLY   D O     
4069 N  N     . GLU   D 16  ? 0.42698 0.48374 0.39059 0.01533  0.03401  0.01601  15  GLU   D N     
4070 C  CA    . GLU   D 16  ? 0.48356 0.53699 0.43796 0.02089  0.03339  0.01478  15  GLU   D CA    
4071 C  C     . GLU   D 16  ? 0.49455 0.54347 0.44500 0.01945  0.02940  0.00921  15  GLU   D C     
4072 O  O     . GLU   D 16  ? 0.37919 0.42738 0.33152 0.01764  0.02852  0.00757  15  GLU   D O     
4073 C  CB    . GLU   D 16  ? 0.51649 0.57001 0.46718 0.02738  0.03606  0.01822  15  GLU   D CB    
4074 C  CG    . GLU   D 16  ? 0.62272 0.68064 0.57659 0.03050  0.04035  0.02474  15  GLU   D CG    
4075 C  CD    . GLU   D 16  ? 0.71710 0.77496 0.66819 0.03168  0.04035  0.02517  15  GLU   D CD    
4076 O  OE1   . GLU   D 16  ? 0.69507 0.74835 0.63693 0.03504  0.03811  0.02182  15  GLU   D OE1   
4077 O  OE2   . GLU   D 16  ? 0.79664 0.85867 0.75507 0.02914  0.04208  0.02876  15  GLU   D OE2   
4078 N  N     . PRO   D 17  ? 0.49845 0.54440 0.44428 0.02016  0.02681  0.00656  16  PRO   D N     
4079 C  CA    . PRO   D 17  ? 0.45446 0.49662 0.39910 0.01813  0.02270  0.00200  16  PRO   D CA    
4080 C  C     . PRO   D 17  ? 0.46395 0.50223 0.40390 0.02208  0.02086  0.00061  16  PRO   D C     
4081 O  O     . PRO   D 17  ? 0.37938 0.41577 0.31285 0.02827  0.02166  0.00213  16  PRO   D O     
4082 C  CB    . PRO   D 17  ? 0.50134 0.54111 0.44210 0.01907  0.02029  0.00038  16  PRO   D CB    
4083 C  CG    . PRO   D 17  ? 0.56607 0.60930 0.50733 0.01994  0.02358  0.00384  16  PRO   D CG    
4084 C  CD    . PRO   D 17  ? 0.50970 0.55549 0.45154 0.02317  0.02735  0.00793  16  PRO   D CD    
4085 N  N     . LEU   D 18  ? 0.33984 0.37685 0.28310 0.01876  0.01853  -0.00203 17  LEU   D N     
4086 C  CA    . LEU   D 18  ? 0.37494 0.40780 0.31478 0.02170  0.01587  -0.00383 17  LEU   D CA    
4087 C  C     . LEU   D 18  ? 0.33761 0.36561 0.27621 0.02146  0.01035  -0.00730 17  LEU   D C     
4088 O  O     . LEU   D 18  ? 0.37089 0.39341 0.30260 0.02653  0.00681  -0.00872 17  LEU   D O     
4089 C  CB    . LEU   D 18  ? 0.34855 0.38376 0.29409 0.01837  0.01734  -0.00363 17  LEU   D CB    
4090 C  CG    . LEU   D 18  ? 0.31997 0.35137 0.26315 0.02079  0.01481  -0.00533 17  LEU   D CG    
4091 C  CD1   . LEU   D 18  ? 0.36791 0.39672 0.30275 0.02819  0.01565  -0.00384 17  LEU   D CD1   
4092 C  CD2   . LEU   D 18  ? 0.33605 0.37039 0.28571 0.01669  0.01656  -0.00507 17  LEU   D CD2   
4093 N  N     . GLY   D 19  ? 0.35096 0.38050 0.29621 0.01601  0.00928  -0.00845 18  GLY   D N     
4094 C  CA    . GLY   D 19  ? 0.30513 0.33071 0.25131 0.01543  0.00405  -0.01085 18  GLY   D CA    
4095 C  C     . GLY   D 19  ? 0.32555 0.35395 0.28070 0.00952  0.00423  -0.01103 18  GLY   D C     
4096 O  O     . GLY   D 19  ? 0.31184 0.34451 0.27104 0.00629  0.00814  -0.00980 18  GLY   D O     
4097 N  N     . ARG   D 20  ? 0.36274 0.38828 0.32094 0.00863  -0.00033 -0.01235 19  ARG   D N     
4098 C  CA    . ARG   D 20  ? 0.34417 0.37239 0.31112 0.00380  -0.00006 -0.01177 19  ARG   D CA    
4099 C  C     . ARG   D 20  ? 0.31361 0.34074 0.28619 0.00277  -0.00215 -0.01192 19  ARG   D C     
4100 O  O     . ARG   D 20  ? 0.31912 0.34135 0.29083 0.00523  -0.00736 -0.01322 19  ARG   D O     
4101 C  CB    . ARG   D 20  ? 0.36340 0.39004 0.33240 0.00310  -0.00347 -0.01212 19  ARG   D CB    
4102 C  CG    . ARG   D 20  ? 0.36630 0.39646 0.34415 -0.00133 -0.00203 -0.01064 19  ARG   D CG    
4103 C  CD    . ARG   D 20  ? 0.40677 0.43648 0.38673 -0.00225 -0.00421 -0.01041 19  ARG   D CD    
4104 N  NE    . ARG   D 20  ? 0.46552 0.49790 0.44134 -0.00276 -0.00045 -0.01012 19  ARG   D NE    
4105 C  CZ    . ARG   D 20  ? 0.51421 0.54784 0.49229 -0.00444 -0.00037 -0.00950 19  ARG   D CZ    
4106 N  NH1   . ARG   D 20  ? 0.43439 0.46723 0.41939 -0.00580 -0.00359 -0.00873 19  ARG   D NH1   
4107 N  NH2   . ARG   D 20  ? 0.50073 0.53654 0.47480 -0.00479 0.00290  -0.00931 19  ARG   D NH2   
4108 N  N     . VAL   D 21  ? 0.29898 0.33023 0.27755 -0.00073 0.00143  -0.01054 20  VAL   D N     
4109 C  CA    . VAL   D 21  ? 0.26477 0.29600 0.25031 -0.00220 0.00022  -0.00995 20  VAL   D CA    
4110 C  C     . VAL   D 21  ? 0.27265 0.30647 0.26638 -0.00531 0.00080  -0.00805 20  VAL   D C     
4111 O  O     . VAL   D 21  ? 0.28709 0.32433 0.28061 -0.00700 0.00496  -0.00707 20  VAL   D O     
4112 C  CB    . VAL   D 21  ? 0.30631 0.34019 0.29194 -0.00302 0.00438  -0.00942 20  VAL   D CB    
4113 C  CG1   . VAL   D 21  ? 0.30739 0.34065 0.30006 -0.00393 0.00249  -0.00878 20  VAL   D CG1   
4114 C  CG2   . VAL   D 21  ? 0.32707 0.36006 0.30531 -0.00033 0.00561  -0.01031 20  VAL   D CG2   
4115 N  N     . SER   D 22  ? 0.29583 0.32795 0.29707 -0.00584 -0.00335 -0.00720 21  SER   D N     
4116 C  CA    . SER   D 22  ? 0.31179 0.34691 0.32207 -0.00841 -0.00230 -0.00439 21  SER   D CA    
4117 C  C     . SER   D 22  ? 0.27485 0.31175 0.29376 -0.00961 -0.00144 -0.00205 21  SER   D C     
4118 O  O     . SER   D 22  ? 0.30980 0.34415 0.32956 -0.00863 -0.00439 -0.00291 21  SER   D O     
4119 C  CB    . SER   D 22  ? 0.34881 0.38123 0.36296 -0.00829 -0.00779 -0.00419 21  SER   D CB    
4120 O  OG    . SER   D 22  ? 0.37047 0.39884 0.39000 -0.00748 -0.01415 -0.00431 21  SER   D OG    
4121 N  N     . PHE   D 23  ? 0.28165 0.32283 0.30657 -0.01133 0.00281  0.00111  22  PHE   D N     
4122 C  CA    . PHE   D 23  ? 0.25789 0.30144 0.29045 -0.01199 0.00497  0.00395  22  PHE   D CA    
4123 C  C     . PHE   D 23  ? 0.27531 0.32134 0.31987 -0.01312 0.00478  0.00847  22  PHE   D C     
4124 O  O     . PHE   D 23  ? 0.30078 0.34858 0.34578 -0.01357 0.00655  0.00980  22  PHE   D O     
4125 C  CB    . PHE   D 23  ? 0.26547 0.31215 0.29305 -0.01193 0.01186  0.00425  22  PHE   D CB    
4126 C  CG    . PHE   D 23  ? 0.24166 0.28681 0.25857 -0.01110 0.01281  0.00064  22  PHE   D CG    
4127 C  CD1   . PHE   D 23  ? 0.27370 0.31751 0.28888 -0.01039 0.01210  -0.00070 22  PHE   D CD1   
4128 C  CD2   . PHE   D 23  ? 0.25476 0.30011 0.26439 -0.01101 0.01460  -0.00087 22  PHE   D CD2   
4129 C  CE1   . PHE   D 23  ? 0.27538 0.31827 0.28208 -0.00953 0.01323  -0.00320 22  PHE   D CE1   
4130 C  CE2   . PHE   D 23  ? 0.29881 0.34325 0.30046 -0.01028 0.01554  -0.00325 22  PHE   D CE2   
4131 C  CZ    . PHE   D 23  ? 0.31278 0.35612 0.31316 -0.00948 0.01497  -0.00426 22  PHE   D CZ    
4132 N  N     . GLU   D 24  ? 0.25597 0.30243 0.31080 -0.01349 0.00296  0.01130  23  GLU   D N     
4133 C  CA    . GLU   D 24  ? 0.28574 0.33608 0.35344 -0.01429 0.00477  0.01711  23  GLU   D CA    
4134 C  C     . GLU   D 24  ? 0.30075 0.35526 0.36815 -0.01351 0.01233  0.01977  23  GLU   D C     
4135 O  O     . GLU   D 24  ? 0.25144 0.30534 0.31602 -0.01301 0.01324  0.01841  23  GLU   D O     
4136 C  CB    . GLU   D 24  ? 0.30515 0.35374 0.38605 -0.01504 -0.00176 0.01956  23  GLU   D CB    
4137 C  CG    . GLU   D 24  ? 0.31324 0.36670 0.41004 -0.01573 0.00059  0.02693  23  GLU   D CG    
4138 C  CD    . GLU   D 24  ? 0.38709 0.43887 0.49902 -0.01671 -0.00641 0.02996  23  GLU   D CD    
4139 O  OE1   . GLU   D 24  ? 0.43658 0.48280 0.54606 -0.01661 -0.01332 0.02601  23  GLU   D OE1   
4140 O  OE2   . GLU   D 24  ? 0.44910 0.50506 0.57589 -0.01730 -0.00498 0.03675  23  GLU   D OE2   
4141 N  N     . LEU   D 25  ? 0.30873 0.36707 0.37870 -0.01295 0.01760  0.02363  24  LEU   D N     
4142 C  CA    . LEU   D 25  ? 0.28156 0.34311 0.34961 -0.01115 0.02492  0.02628  24  LEU   D CA    
4143 C  C     . LEU   D 25  ? 0.24933 0.31484 0.33226 -0.01060 0.02682  0.03352  24  LEU   D C     
4144 O  O     . LEU   D 25  ? 0.28068 0.34796 0.37275 -0.01117 0.02568  0.03732  24  LEU   D O     
4145 C  CB    . LEU   D 25  ? 0.27123 0.33354 0.32966 -0.00985 0.02981  0.02548  24  LEU   D CB    
4146 C  CG    . LEU   D 25  ? 0.25693 0.31582 0.30259 -0.01059 0.02773  0.01920  24  LEU   D CG    
4147 C  CD1   . LEU   D 25  ? 0.27534 0.33459 0.31207 -0.00935 0.03205  0.01854  24  LEU   D CD1   
4148 C  CD2   . LEU   D 25  ? 0.29814 0.35496 0.33722 -0.01045 0.02729  0.01561  24  LEU   D CD2   
4149 N  N     . PHE   D 26  ? 0.26920 0.33616 0.35544 -0.00952 0.02944  0.03575  25  PHE   D N     
4150 C  CA    . PHE   D 26  ? 0.26741 0.33831 0.36963 -0.00898 0.03085  0.04324  25  PHE   D CA    
4151 C  C     . PHE   D 26  ? 0.25383 0.32919 0.35716 -0.00580 0.03907  0.04908  25  PHE   D C     
4152 O  O     . PHE   D 26  ? 0.27479 0.35260 0.37915 -0.00308 0.04466  0.05276  25  PHE   D O     
4153 C  CB    . PHE   D 26  ? 0.31704 0.38759 0.42212 -0.00887 0.03032  0.04330  25  PHE   D CB    
4154 C  CG    . PHE   D 26  ? 0.32784 0.39375 0.43246 -0.01126 0.02220  0.03825  25  PHE   D CG    
4155 C  CD1   . PHE   D 26  ? 0.36334 0.42674 0.47424 -0.01324 0.01482  0.03753  25  PHE   D CD1   
4156 C  CD2   . PHE   D 26  ? 0.35388 0.41732 0.45037 -0.01107 0.02179  0.03391  25  PHE   D CD2   
4157 C  CE1   . PHE   D 26  ? 0.37242 0.43055 0.48132 -0.01442 0.00713  0.03278  25  PHE   D CE1   
4158 C  CE2   . PHE   D 26  ? 0.37321 0.43206 0.46840 -0.01248 0.01458  0.02949  25  PHE   D CE2   
4159 C  CZ    . PHE   D 26  ? 0.33984 0.39576 0.44069 -0.01388 0.00722  0.02884  25  PHE   D CZ    
4160 N  N     . ALA   D 27  ? 0.28668 0.36274 0.38909 -0.00573 0.03975  0.04990  26  ALA   D N     
4161 C  CA    . ALA   D 27  ? 0.36650 0.44638 0.46951 -0.00217 0.04736  0.05563  26  ALA   D CA    
4162 C  C     . ALA   D 27  ? 0.36709 0.45225 0.48774 -0.00066 0.05035  0.06513  26  ALA   D C     
4163 O  O     . ALA   D 27  ? 0.34852 0.43687 0.46853 0.00373  0.05818  0.07045  26  ALA   D O     
4164 C  CB    . ALA   D 27  ? 0.37376 0.45345 0.47451 -0.00280 0.04660  0.05503  26  ALA   D CB    
4165 N  N     . ASP   D 28  ? 0.34695 0.43272 0.48336 -0.00379 0.04410  0.06756  27  ASP   D N     
4166 C  CA    . ASP   D 28  ? 0.33848 0.42946 0.49384 -0.00268 0.04637  0.07718  27  ASP   D CA    
4167 C  C     . ASP   D 28  ? 0.36117 0.45364 0.51511 0.00007  0.05146  0.07919  27  ASP   D C     
4168 O  O     . ASP   D 28  ? 0.44092 0.53860 0.60711 0.00281  0.05672  0.08811  27  ASP   D O     
4169 C  CB    . ASP   D 28  ? 0.39369 0.48381 0.56640 -0.00690 0.03694  0.07874  27  ASP   D CB    
4170 C  CG    . ASP   D 28  ? 0.45368 0.53777 0.61987 -0.00978 0.02909  0.07054  27  ASP   D CG    
4171 O  OD1   . ASP   D 28  ? 0.41030 0.49078 0.55808 -0.00937 0.03004  0.06285  27  ASP   D OD1   
4172 O  OD2   . ASP   D 28  ? 0.53705 0.61977 0.71673 -0.01220 0.02176  0.07200  27  ASP   D OD2   
4173 N  N     . LYS   D 29  ? 0.33862 0.42686 0.47816 -0.00027 0.05038  0.07161  28  LYS   D N     
4174 C  CA    . LYS   D 29  ? 0.31048 0.39974 0.44849 0.00222  0.05466  0.07314  28  LYS   D CA    
4175 C  C     . LYS   D 29  ? 0.31649 0.40376 0.43503 0.00615  0.06101  0.06927  28  LYS   D C     
4176 O  O     . LYS   D 29  ? 0.29559 0.38477 0.41326 0.01013  0.06709  0.07309  28  LYS   D O     
4177 C  CB    . LYS   D 29  ? 0.38970 0.47564 0.52980 -0.00129 0.04754  0.06844  28  LYS   D CB    
4178 C  CG    . LYS   D 29  ? 0.43107 0.51805 0.59148 -0.00457 0.04046  0.07269  28  LYS   D CG    
4179 C  CD    . LYS   D 29  ? 0.47567 0.56368 0.64579 -0.00471 0.03957  0.07557  28  LYS   D CD    
4180 C  CE    . LYS   D 29  ? 0.46205 0.55391 0.65657 -0.00596 0.03661  0.08458  28  LYS   D CE    
4181 N  NZ    . LYS   D 29  ? 0.54969 0.64334 0.75399 -0.00549 0.03717  0.08844  28  LYS   D NZ    
4182 N  N     . VAL   D 30  ? 0.27456 0.35770 0.37788 0.00531  0.05935  0.06196  29  VAL   D N     
4183 C  CA    . VAL   D 30  ? 0.33654 0.41664 0.42138 0.00867  0.06375  0.05762  29  VAL   D CA    
4184 C  C     . VAL   D 30  ? 0.28368 0.36247 0.36027 0.00926  0.06450  0.05569  29  VAL   D C     
4185 O  O     . VAL   D 30  ? 0.27316 0.34794 0.33892 0.00699  0.06071  0.04850  29  VAL   D O     
4186 C  CB    . VAL   D 30  ? 0.31148 0.38697 0.38555 0.00649  0.05977  0.04955  29  VAL   D CB    
4187 C  CG1   . VAL   D 30  ? 0.32628 0.40219 0.40015 0.00882  0.06283  0.05107  29  VAL   D CG1   
4188 C  CG2   . VAL   D 30  ? 0.36465 0.43864 0.44466 0.00135  0.05179  0.04592  29  VAL   D CG2   
4189 N  N     . PRO   D 31  ? 0.32029 0.40257 0.40220 0.01242  0.06943  0.06235  30  PRO   D N     
4190 C  CA    . PRO   D 31  ? 0.28510 0.36630 0.36082 0.01255  0.06950  0.06075  30  PRO   D CA    
4191 C  C     . PRO   D 31  ? 0.29872 0.37490 0.35453 0.01500  0.07114  0.05449  30  PRO   D C     
4192 O  O     . PRO   D 31  ? 0.32072 0.39420 0.36955 0.01270  0.06778  0.04944  30  PRO   D O     
4193 C  CB    . PRO   D 31  ? 0.26240 0.34879 0.34831 0.01659  0.07575  0.07043  30  PRO   D CB    
4194 C  CG    . PRO   D 31  ? 0.33677 0.42594 0.42785 0.02059  0.08109  0.07634  30  PRO   D CG    
4195 C  CD    . PRO   D 31  ? 0.31732 0.40506 0.41270 0.01588  0.07496  0.07218  30  PRO   D CD    
4196 N  N     . LYS   D 32  ? 0.31248 0.38685 0.35901 0.01959  0.07561  0.05451  31  LYS   D N     
4197 C  CA    . LYS   D 32  ? 0.32165 0.39039 0.34945 0.02244  0.07652  0.04890  31  LYS   D CA    
4198 C  C     . LYS   D 32  ? 0.27678 0.34135 0.29740 0.01770  0.07007  0.04038  31  LYS   D C     
4199 O  O     . LYS   D 32  ? 0.28360 0.34463 0.29447 0.01690  0.06786  0.03556  31  LYS   D O     
4200 C  CB    . LYS   D 32  ? 0.31794 0.38506 0.33742 0.02941  0.08261  0.05145  31  LYS   D CB    
4201 C  CG    . LYS   D 32  ? 0.41576 0.47575 0.41630 0.03239  0.08207  0.04509  31  LYS   D CG    
4202 C  CD    . LYS   D 32  ? 0.52656 0.58442 0.51799 0.04104  0.08869  0.04881  31  LYS   D CD    
4203 C  CE    . LYS   D 32  ? 0.53962 0.58963 0.51218 0.04494  0.08779  0.04332  31  LYS   D CE    
4204 N  NZ    . LYS   D 32  ? 0.55669 0.60325 0.51854 0.05407  0.09347  0.04625  31  LYS   D NZ    
4205 N  N     . THR   D 33  ? 0.28530 0.35062 0.31172 0.01480  0.06727  0.03926  32  THR   D N     
4206 C  CA    . THR   D 33  ? 0.27090 0.33273 0.29125 0.01087  0.06177  0.03208  32  THR   D CA    
4207 C  C     . THR   D 33  ? 0.25694 0.31915 0.28151 0.00610  0.05653  0.02956  32  THR   D C     
4208 O  O     . THR   D 33  ? 0.26398 0.32305 0.28028 0.00418  0.05332  0.02409  32  THR   D O     
4209 C  CB    . THR   D 33  ? 0.25617 0.31873 0.28166 0.00969  0.06062  0.03210  32  THR   D CB    
4210 O  OG1   . THR   D 33  ? 0.27932 0.34205 0.30213 0.01466  0.06604  0.03551  32  THR   D OG1   
4211 C  CG2   . THR   D 33  ? 0.26924 0.32811 0.28739 0.00657  0.05580  0.02510  32  THR   D CG2   
4212 N  N     . ALA   D 34  ? 0.25604 0.32192 0.29393 0.00428  0.05530  0.03373  33  ALA   D N     
4213 C  CA    . ALA   D 34  ? 0.27874 0.34435 0.31972 0.00056  0.05028  0.03151  33  ALA   D CA    
4214 C  C     . ALA   D 34  ? 0.27456 0.33872 0.30683 0.00153  0.05155  0.02983  33  ALA   D C     
4215 O  O     . ALA   D 34  ? 0.30251 0.36448 0.32984 -0.00098 0.04769  0.02524  33  ALA   D O     
4216 C  CB    . ALA   D 34  ? 0.24827 0.31756 0.30561 -0.00095 0.04856  0.03695  33  ALA   D CB    
4217 N  N     . GLU   D 35  ? 0.29198 0.35732 0.32233 0.00558  0.05709  0.03385  34  GLU   D N     
4218 C  CA    . GLU   D 35  ? 0.30630 0.37018 0.32910 0.00678  0.05820  0.03270  34  GLU   D CA    
4219 C  C     . GLU   D 35  ? 0.27053 0.32936 0.27866 0.00693  0.05667  0.02621  34  GLU   D C     
4220 O  O     . GLU   D 35  ? 0.26652 0.32353 0.26949 0.00537  0.05433  0.02295  34  GLU   D O     
4221 C  CB    . GLU   D 35  ? 0.31795 0.38379 0.34119 0.01213  0.06488  0.03885  34  GLU   D CB    
4222 C  CG    . GLU   D 35  ? 0.38649 0.44997 0.39983 0.01454  0.06663  0.03765  34  GLU   D CG    
4223 C  CD    . GLU   D 35  ? 0.43532 0.50029 0.45382 0.01098  0.06347  0.03730  34  GLU   D CD    
4224 O  OE1   . GLU   D 35  ? 0.41205 0.48014 0.44319 0.00718  0.06016  0.03907  34  GLU   D OE1   
4225 O  OE2   . GLU   D 35  ? 0.45634 0.51881 0.46580 0.01223  0.06392  0.03511  34  GLU   D OE2   
4226 N  N     . ASN   D 36  ? 0.31212 0.36859 0.31392 0.00897  0.05792  0.02464  35  ASN   D N     
4227 C  CA    . ASN   D 36  ? 0.32392 0.37544 0.31362 0.00876  0.05556  0.01874  35  ASN   D CA    
4228 C  C     . ASN   D 36  ? 0.29051 0.34169 0.28158 0.00368  0.05008  0.01444  35  ASN   D C     
4229 O  O     . ASN   D 36  ? 0.28795 0.33670 0.27262 0.00261  0.04791  0.01106  35  ASN   D O     
4230 C  CB    . ASN   D 36  ? 0.29698 0.34642 0.28226 0.01120  0.05699  0.01812  35  ASN   D CB    
4231 C  CG    . ASN   D 36  ? 0.35593 0.40004 0.33006 0.01104  0.05407  0.01254  35  ASN   D CG    
4232 O  OD1   . ASN   D 36  ? 0.30883 0.34916 0.27401 0.01317  0.05398  0.01077  35  ASN   D OD1   
4233 N  ND2   . ASN   D 36  ? 0.30163 0.34523 0.27670 0.00864  0.05142  0.00999  35  ASN   D ND2   
4234 N  N     . PHE   D 37  ? 0.27447 0.32795 0.27401 0.00088  0.04774  0.01484  36  PHE   D N     
4235 C  CA    . PHE   D 37  ? 0.29223 0.34502 0.29219 -0.00285 0.04286  0.01112  36  PHE   D CA    
4236 C  C     . PHE   D 37  ? 0.26273 0.31637 0.26488 -0.00457 0.04090  0.01109  36  PHE   D C     
4237 O  O     . PHE   D 37  ? 0.27406 0.32597 0.27124 -0.00614 0.03828  0.00766  36  PHE   D O     
4238 C  CB    . PHE   D 37  ? 0.25731 0.31152 0.26496 -0.00448 0.04075  0.01171  36  PHE   D CB    
4239 C  CG    . PHE   D 37  ? 0.26818 0.32085 0.27400 -0.00698 0.03631  0.00780  36  PHE   D CG    
4240 C  CD1   . PHE   D 37  ? 0.23978 0.29048 0.23981 -0.00700 0.03581  0.00488  36  PHE   D CD1   
4241 C  CD2   . PHE   D 37  ? 0.24181 0.29476 0.25162 -0.00886 0.03261  0.00729  36  PHE   D CD2   
4242 C  CE1   . PHE   D 37  ? 0.30348 0.35311 0.30216 -0.00868 0.03227  0.00204  36  PHE   D CE1   
4243 C  CE2   . PHE   D 37  ? 0.29549 0.34670 0.30280 -0.01014 0.02881  0.00405  36  PHE   D CE2   
4244 C  CZ    . PHE   D 37  ? 0.28649 0.33630 0.28825 -0.00993 0.02901  0.00165  36  PHE   D CZ    
4245 N  N     . ARG   D 38  ? 0.27731 0.33368 0.28720 -0.00408 0.04230  0.01529  37  ARG   D N     
4246 C  CA    . ARG   D 38  ? 0.29305 0.35014 0.30530 -0.00555 0.04041  0.01550  37  ARG   D CA    
4247 C  C     . ARG   D 38  ? 0.29959 0.35451 0.30182 -0.00461 0.04157  0.01313  37  ARG   D C     
4248 O  O     . ARG   D 38  ? 0.29231 0.34599 0.29130 -0.00655 0.03856  0.01009  37  ARG   D O     
4249 C  CB    . ARG   D 38  ? 0.29447 0.35508 0.31738 -0.00464 0.04249  0.02137  37  ARG   D CB    
4250 C  CG    . ARG   D 38  ? 0.33710 0.39852 0.36492 -0.00665 0.03945  0.02186  37  ARG   D CG    
4251 C  CD    . ARG   D 38  ? 0.38029 0.44519 0.41695 -0.00513 0.04263  0.02807  37  ARG   D CD    
4252 N  NE    . ARG   D 38  ? 0.35998 0.42479 0.38894 -0.00142 0.04844  0.02952  37  ARG   D NE    
4253 C  CZ    . ARG   D 38  ? 0.39458 0.45718 0.41383 -0.00083 0.04891  0.02667  37  ARG   D CZ    
4254 N  NH1   . ARG   D 38  ? 0.44249 0.50362 0.45937 -0.00379 0.04458  0.02280  37  ARG   D NH1   
4255 N  NH2   . ARG   D 38  ? 0.36936 0.43075 0.38052 0.00324  0.05369  0.02769  37  ARG   D NH2   
4256 N  N     . ALA   D 39  ? 0.31729 0.37132 0.31418 -0.00119 0.04579  0.01458  38  ALA   D N     
4257 C  CA    . ALA   D 39  ? 0.32616 0.37731 0.31335 0.00032  0.04660  0.01254  38  ALA   D CA    
4258 C  C     . ALA   D 39  ? 0.36685 0.41459 0.34650 -0.00130 0.04333  0.00746  38  ALA   D C     
4259 O  O     . ALA   D 39  ? 0.35717 0.40323 0.33219 -0.00219 0.04163  0.00521  38  ALA   D O     
4260 C  CB    . ALA   D 39  ? 0.36664 0.41630 0.34827 0.00536  0.05139  0.01493  38  ALA   D CB    
4261 N  N     . LEU   D 40  ? 0.32026 0.36706 0.29915 -0.00159 0.04251  0.00601  39  LEU   D N     
4262 C  CA    . LEU   D 40  ? 0.32358 0.36766 0.29706 -0.00314 0.03946  0.00201  39  LEU   D CA    
4263 C  C     . LEU   D 40  ? 0.34148 0.38705 0.31843 -0.00653 0.03607  0.00050  39  LEU   D C     
4264 O  O     . LEU   D 40  ? 0.33153 0.37548 0.30447 -0.00769 0.03391  -0.00195 39  LEU   D O     
4265 C  CB    . LEU   D 40  ? 0.29897 0.34187 0.27136 -0.00240 0.03964  0.00128  39  LEU   D CB    
4266 C  CG    . LEU   D 40  ? 0.36896 0.40886 0.33516 0.00161  0.04233  0.00187  39  LEU   D CG    
4267 C  CD1   . LEU   D 40  ? 0.27910 0.31842 0.24566 0.00207  0.04242  0.00145  39  LEU   D CD1   
4268 C  CD2   . LEU   D 40  ? 0.32030 0.35530 0.27714 0.00307  0.04087  -0.00071 39  LEU   D CD2   
4269 N  N     . SER   D 41  ? 0.34687 0.39520 0.33130 -0.00776 0.03531  0.00217  40  SER   D N     
4270 C  CA    . SER   D 41  ? 0.33087 0.37975 0.31730 -0.00996 0.03191  0.00076  40  SER   D CA    
4271 C  C     . SER   D 41  ? 0.40729 0.45626 0.39231 -0.01044 0.03142  0.00067  40  SER   D C     
4272 O  O     . SER   D 41  ? 0.35229 0.40079 0.33557 -0.01167 0.02897  -0.00114 40  SER   D O     
4273 C  CB    . SER   D 41  ? 0.33191 0.38239 0.32624 -0.01071 0.03012  0.00222  40  SER   D CB    
4274 O  OG    . SER   D 41  ? 0.33702 0.38739 0.33283 -0.01034 0.03037  0.00223  40  SER   D OG    
4275 N  N     . THR   D 42  ? 0.35248 0.40208 0.33804 -0.00916 0.03394  0.00284  41  THR   D N     
4276 C  CA    . THR   D 42  ? 0.42812 0.47771 0.41208 -0.00964 0.03345  0.00264  41  THR   D CA    
4277 C  C     . THR   D 42  ? 0.43835 0.48522 0.41391 -0.00886 0.03394  0.00055  41  THR   D C     
4278 O  O     . THR   D 42  ? 0.47453 0.52098 0.44795 -0.00976 0.03269  -0.00048 41  THR   D O     
4279 C  CB    . THR   D 42  ? 0.43427 0.48591 0.42325 -0.00850 0.03579  0.00634  41  THR   D CB    
4280 O  OG1   . THR   D 42  ? 0.38640 0.43732 0.37198 -0.00545 0.03981  0.00805  41  THR   D OG1   
4281 C  CG2   . THR   D 42  ? 0.42656 0.48071 0.42586 -0.00948 0.03446  0.00898  41  THR   D CG2   
4282 N  N     . GLY   D 43  ? 0.40562 0.45023 0.37654 -0.00714 0.03525  -0.00012 42  GLY   D N     
4283 C  CA    . GLY   D 43  ? 0.45056 0.49148 0.41372 -0.00599 0.03485  -0.00207 42  GLY   D CA    
4284 C  C     . GLY   D 43  ? 0.45683 0.49624 0.41595 -0.00325 0.03717  -0.00083 42  GLY   D C     
4285 O  O     . GLY   D 43  ? 0.49444 0.53013 0.44684 -0.00223 0.03605  -0.00265 42  GLY   D O     
4286 N  N     . GLU   D 44  ? 0.43219 0.47422 0.39555 -0.00177 0.04025  0.00253  43  GLU   D N     
4287 C  CA    . GLU   D 44  ? 0.48073 0.52226 0.44143 0.00087  0.04283  0.00446  43  GLU   D CA    
4288 C  C     . GLU   D 44  ? 0.54505 0.58174 0.49603 0.00552  0.04469  0.00399  43  GLU   D C     
4289 O  O     . GLU   D 44  ? 0.50125 0.53576 0.44684 0.00810  0.04588  0.00436  43  GLU   D O     
4290 C  CB    . GLU   D 44  ? 0.47865 0.52476 0.44828 0.00139  0.04575  0.00912  43  GLU   D CB    
4291 C  CG    . GLU   D 44  ? 0.42333 0.47058 0.39590 0.00378  0.04875  0.01196  43  GLU   D CG    
4292 C  CD    . GLU   D 44  ? 0.44537 0.49769 0.42995 0.00317  0.05041  0.01686  43  GLU   D CD    
4293 O  OE1   . GLU   D 44  ? 0.44464 0.49916 0.43655 -0.00061 0.04704  0.01644  43  GLU   D OE1   
4294 O  OE2   . GLU   D 44  ? 0.53203 0.58585 0.51884 0.00680  0.05487  0.02133  43  GLU   D OE2   
4295 N  N     . LYS   D 45  ? 0.39926 0.43376 0.34734 0.00714  0.04487  0.00320  44  LYS   D N     
4296 C  CA    . LYS   D 45  ? 0.45240 0.48084 0.38973 0.01203  0.04555  0.00207  44  LYS   D CA    
4297 C  C     . LYS   D 45  ? 0.46033 0.48331 0.39071 0.01099  0.04068  -0.00237 44  LYS   D C     
4298 O  O     . LYS   D 45  ? 0.54783 0.56436 0.46859 0.01503  0.03975  -0.00401 44  LYS   D O     
4299 C  CB    . LYS   D 45  ? 0.50578 0.53344 0.44241 0.01434  0.04715  0.00280  44  LYS   D CB    
4300 C  CG    . LYS   D 45  ? 0.55841 0.58843 0.49683 0.01886  0.05294  0.00774  44  LYS   D CG    
4301 C  CD    . LYS   D 45  ? 0.56652 0.60181 0.51252 0.01850  0.05606  0.01206  44  LYS   D CD    
4302 C  CE    . LYS   D 45  ? 0.53255 0.57072 0.48198 0.02328  0.06216  0.01806  44  LYS   D CE    
4303 N  NZ    . LYS   D 45  ? 0.62584 0.65879 0.56306 0.03100  0.06572  0.01909  44  LYS   D NZ    
4304 N  N     . GLY   D 46  ? 0.43447 0.45952 0.36953 0.00608  0.03735  -0.00408 45  GLY   D N     
4305 C  CA    . GLY   D 46  ? 0.46898 0.48978 0.40005 0.00461  0.03266  -0.00741 45  GLY   D CA    
4306 C  C     . GLY   D 46  ? 0.55858 0.57916 0.49235 0.00220  0.02984  -0.00895 45  GLY   D C     
4307 O  O     . GLY   D 46  ? 0.51945 0.53706 0.45197 0.00066  0.02572  -0.01102 45  GLY   D O     
4308 N  N     . PHE   D 47  ? 0.43480 0.45857 0.37297 0.00184  0.03186  -0.00764 46  PHE   D N     
4309 C  CA    . PHE   D 47  ? 0.40006 0.42402 0.34107 -0.00027 0.02961  -0.00879 46  PHE   D CA    
4310 C  C     . PHE   D 47  ? 0.40253 0.43201 0.35085 -0.00186 0.03197  -0.00691 46  PHE   D C     
4311 O  O     . PHE   D 47  ? 0.38637 0.41862 0.33727 -0.00079 0.03514  -0.00460 46  PHE   D O     
4312 C  CB    . PHE   D 47  ? 0.40602 0.42419 0.34054 0.00286  0.02835  -0.01022 46  PHE   D CB    
4313 C  CG    . PHE   D 47  ? 0.40958 0.42631 0.33939 0.00768  0.03230  -0.00867 46  PHE   D CG    
4314 C  CD1   . PHE   D 47  ? 0.43081 0.45162 0.36542 0.00791  0.03572  -0.00643 46  PHE   D CD1   
4315 C  CD2   . PHE   D 47  ? 0.43528 0.44635 0.35574 0.01246  0.03264  -0.00915 46  PHE   D CD2   
4316 C  CE1   . PHE   D 47  ? 0.44425 0.46428 0.37547 0.01264  0.03982  -0.00418 46  PHE   D CE1   
4317 C  CE2   . PHE   D 47  ? 0.52468 0.53447 0.44032 0.01783  0.03692  -0.00707 46  PHE   D CE2   
4318 C  CZ    . PHE   D 47  ? 0.50813 0.52282 0.42967 0.01788  0.04080  -0.00427 46  PHE   D CZ    
4319 N  N     . GLY   D 48  ? 0.39678 0.42767 0.34888 -0.00424 0.03022  -0.00762 47  GLY   D N     
4320 C  CA    . GLY   D 48  ? 0.33226 0.36745 0.29067 -0.00547 0.03172  -0.00619 47  GLY   D CA    
4321 C  C     . GLY   D 48  ? 0.32027 0.35705 0.28222 -0.00813 0.02939  -0.00705 47  GLY   D C     
4322 O  O     . GLY   D 48  ? 0.33844 0.37320 0.29874 -0.00883 0.02709  -0.00825 47  GLY   D O     
4323 N  N     . TYR   D 49  ? 0.33201 0.37222 0.29915 -0.00925 0.02988  -0.00608 48  TYR   D N     
4324 C  CA    . TYR   D 49  ? 0.33943 0.38089 0.30922 -0.01057 0.02843  -0.00652 48  TYR   D CA    
4325 C  C     . TYR   D 49  ? 0.33295 0.37513 0.30294 -0.01190 0.02658  -0.00690 48  TYR   D C     
4326 O  O     . TYR   D 49  ? 0.32089 0.36349 0.29193 -0.01236 0.02560  -0.00694 48  TYR   D O     
4327 C  CB    . TYR   D 49  ? 0.30357 0.34743 0.27805 -0.01071 0.02894  -0.00552 48  TYR   D CB    
4328 C  CG    . TYR   D 49  ? 0.26760 0.31139 0.24344 -0.00944 0.03085  -0.00455 48  TYR   D CG    
4329 C  CD1   . TYR   D 49  ? 0.33035 0.37217 0.30337 -0.00852 0.03129  -0.00526 48  TYR   D CD1   
4330 C  CD2   . TYR   D 49  ? 0.25685 0.30251 0.23743 -0.00906 0.03202  -0.00260 48  TYR   D CD2   
4331 C  CE1   . TYR   D 49  ? 0.29178 0.33353 0.26567 -0.00694 0.03332  -0.00417 48  TYR   D CE1   
4332 C  CE2   . TYR   D 49  ? 0.28275 0.32881 0.26546 -0.00762 0.03421  -0.00095 48  TYR   D CE2   
4333 C  CZ    . TYR   D 49  ? 0.26099 0.30512 0.23990 -0.00647 0.03502  -0.00185 48  TYR   D CZ    
4334 O  OH    . TYR   D 49  ? 0.26336 0.30781 0.24385 -0.00471 0.03733  -0.00016 48  TYR   D OH    
4335 N  N     . LYS   D 50  ? 0.35095 0.39350 0.32023 -0.01227 0.02635  -0.00679 49  LYS   D N     
4336 C  CA    . LYS   D 50  ? 0.37210 0.41570 0.34181 -0.01314 0.02496  -0.00670 49  LYS   D CA    
4337 C  C     . LYS   D 50  ? 0.36608 0.40863 0.33549 -0.01358 0.02375  -0.00665 49  LYS   D C     
4338 O  O     . LYS   D 50  ? 0.37189 0.41177 0.33929 -0.01354 0.02297  -0.00724 49  LYS   D O     
4339 C  CB    . LYS   D 50  ? 0.45343 0.49706 0.42187 -0.01345 0.02486  -0.00670 49  LYS   D CB    
4340 C  CG    . LYS   D 50  ? 0.44068 0.48560 0.40956 -0.01395 0.02374  -0.00630 49  LYS   D CG    
4341 C  CD    . LYS   D 50  ? 0.47228 0.51731 0.44004 -0.01426 0.02363  -0.00638 49  LYS   D CD    
4342 C  CE    . LYS   D 50  ? 0.55887 0.60515 0.52671 -0.01435 0.02272  -0.00578 49  LYS   D CE    
4343 N  NZ    . LYS   D 50  ? 0.64939 0.69582 0.61623 -0.01463 0.02252  -0.00599 49  LYS   D NZ    
4344 N  N     . GLY   D 51  ? 0.35913 0.40345 0.33070 -0.01362 0.02338  -0.00568 50  GLY   D N     
4345 C  CA    . GLY   D 51  ? 0.32676 0.37093 0.30015 -0.01404 0.02236  -0.00459 50  GLY   D CA    
4346 C  C     . GLY   D 51  ? 0.41073 0.45419 0.38546 -0.01389 0.02220  -0.00455 50  GLY   D C     
4347 O  O     . GLY   D 51  ? 0.38889 0.43294 0.36662 -0.01416 0.02140  -0.00297 50  GLY   D O     
4348 N  N     . SER   D 52  ? 0.36216 0.40455 0.33540 -0.01340 0.02300  -0.00582 51  SER   D N     
4349 C  CA    . SER   D 52  ? 0.39240 0.43388 0.36652 -0.01318 0.02283  -0.00595 51  SER   D CA    
4350 C  C     . SER   D 52  ? 0.37294 0.41700 0.34940 -0.01264 0.02369  -0.00496 51  SER   D C     
4351 O  O     . SER   D 52  ? 0.32875 0.37456 0.30519 -0.01200 0.02423  -0.00452 51  SER   D O     
4352 C  CB    . SER   D 52  ? 0.34760 0.38703 0.31905 -0.01234 0.02373  -0.00731 51  SER   D CB    
4353 O  OG    . SER   D 52  ? 0.32598 0.36734 0.29825 -0.01189 0.02542  -0.00719 51  SER   D OG    
4354 N  N     . CYS   D 53  ? 0.34899 0.39273 0.32690 -0.01252 0.02354  -0.00469 52  CYS   D N     
4355 C  CA    . CYS   D 53  ? 0.33255 0.37837 0.31229 -0.01160 0.02427  -0.00350 52  CYS   D CA    
4356 C  C     . CYS   D 53  ? 0.30665 0.35196 0.28605 -0.01109 0.02490  -0.00461 52  CYS   D C     
4357 O  O     . CYS   D 53  ? 0.31961 0.36322 0.29792 -0.01142 0.02500  -0.00584 52  CYS   D O     
4358 C  CB    . CYS   D 53  ? 0.39743 0.44414 0.38065 -0.01177 0.02370  -0.00122 52  CYS   D CB    
4359 S  SG    . CYS   D 53  ? 0.51926 0.56388 0.50410 -0.01250 0.02251  -0.00171 52  CYS   D SG    
4360 N  N     . PHE   D 54  ? 0.32180 0.36837 0.30177 -0.00983 0.02535  -0.00403 53  PHE   D N     
4361 C  CA    . PHE   D 54  ? 0.25840 0.30456 0.23885 -0.00932 0.02565  -0.00473 53  PHE   D CA    
4362 C  C     . PHE   D 54  ? 0.26954 0.31597 0.25190 -0.00941 0.02568  -0.00358 53  PHE   D C     
4363 O  O     . PHE   D 54  ? 0.32139 0.36933 0.30486 -0.00822 0.02609  -0.00171 53  PHE   D O     
4364 C  CB    . PHE   D 54  ? 0.27336 0.31981 0.25301 -0.00755 0.02538  -0.00489 53  PHE   D CB    
4365 C  CG    . PHE   D 54  ? 0.26900 0.31470 0.24847 -0.00772 0.02460  -0.00606 53  PHE   D CG    
4366 C  CD1   . PHE   D 54  ? 0.28503 0.33078 0.26333 -0.00757 0.02395  -0.00607 53  PHE   D CD1   
4367 C  CD2   . PHE   D 54  ? 0.23569 0.28077 0.21703 -0.00799 0.02442  -0.00675 53  PHE   D CD2   
4368 C  CE1   . PHE   D 54  ? 0.30611 0.35124 0.28550 -0.00789 0.02293  -0.00672 53  PHE   D CE1   
4369 C  CE2   . PHE   D 54  ? 0.31634 0.36108 0.29946 -0.00822 0.02355  -0.00698 53  PHE   D CE2   
4370 C  CZ    . PHE   D 54  ? 0.31042 0.35513 0.29273 -0.00821 0.02264  -0.00696 53  PHE   D CZ    
4371 N  N     . HIS   D 55  ? 0.23915 0.28394 0.22183 -0.01043 0.02522  -0.00437 54  HIS   D N     
4372 C  CA    . HIS   D 55  ? 0.28354 0.32803 0.26872 -0.01084 0.02443  -0.00324 54  HIS   D CA    
4373 C  C     . HIS   D 55  ? 0.31090 0.35586 0.29708 -0.01011 0.02508  -0.00317 54  HIS   D C     
4374 O  O     . HIS   D 55  ? 0.30610 0.35141 0.29519 -0.01027 0.02456  -0.00166 54  HIS   D O     
4375 C  CB    . HIS   D 55  ? 0.31012 0.35144 0.29439 -0.01181 0.02270  -0.00438 54  HIS   D CB    
4376 C  CG    . HIS   D 55  ? 0.29651 0.33571 0.27745 -0.01123 0.02334  -0.00645 54  HIS   D CG    
4377 N  ND1   . HIS   D 55  ? 0.26417 0.30307 0.24242 -0.01076 0.02449  -0.00740 54  HIS   D ND1   
4378 C  CD2   . HIS   D 55  ? 0.30864 0.34620 0.28893 -0.01074 0.02328  -0.00727 54  HIS   D CD2   
4379 C  CE1   . HIS   D 55  ? 0.29514 0.33245 0.27143 -0.00980 0.02539  -0.00832 54  HIS   D CE1   
4380 N  NE2   . HIS   D 55  ? 0.28229 0.31857 0.25933 -0.00973 0.02463  -0.00846 54  HIS   D NE2   
4381 N  N     . ARG   D 56  ? 0.25822 0.30314 0.24280 -0.00937 0.02593  -0.00449 55  ARG   D N     
4382 C  CA    . ARG   D 56  ? 0.26671 0.31171 0.25210 -0.00869 0.02633  -0.00465 55  ARG   D CA    
4383 C  C     . ARG   D 56  ? 0.23981 0.28537 0.22420 -0.00723 0.02660  -0.00504 55  ARG   D C     
4384 O  O     . ARG   D 56  ? 0.27474 0.31965 0.25867 -0.00741 0.02639  -0.00620 55  ARG   D O     
4385 C  CB    . ARG   D 56  ? 0.28882 0.33193 0.27360 -0.00930 0.02632  -0.00612 55  ARG   D CB    
4386 C  CG    . ARG   D 56  ? 0.27785 0.32099 0.26377 -0.00879 0.02664  -0.00624 55  ARG   D CG    
4387 C  CD    . ARG   D 56  ? 0.27435 0.31550 0.25909 -0.00890 0.02692  -0.00750 55  ARG   D CD    
4388 N  NE    . ARG   D 56  ? 0.30419 0.34302 0.28784 -0.00930 0.02561  -0.00776 55  ARG   D NE    
4389 C  CZ    . ARG   D 56  ? 0.39764 0.43366 0.37828 -0.00860 0.02557  -0.00891 55  ARG   D CZ    
4390 N  NH1   . ARG   D 56  ? 0.34544 0.38159 0.32479 -0.00758 0.02749  -0.00924 55  ARG   D NH1   
4391 N  NH2   . ARG   D 56  ? 0.41393 0.44669 0.39300 -0.00853 0.02337  -0.00946 55  ARG   D NH2   
4392 N  N     . ILE   D 57  ? 0.25344 0.29984 0.23764 -0.00540 0.02681  -0.00384 56  ILE   D N     
4393 C  CA    . ILE   D 57  ? 0.22750 0.27312 0.20962 -0.00323 0.02617  -0.00447 56  ILE   D CA    
4394 C  C     . ILE   D 57  ? 0.28489 0.33023 0.26716 -0.00179 0.02640  -0.00421 56  ILE   D C     
4395 O  O     . ILE   D 57  ? 0.26083 0.30745 0.24366 -0.00070 0.02752  -0.00220 56  ILE   D O     
4396 C  CB    . ILE   D 57  ? 0.23766 0.28363 0.21722 -0.00099 0.02615  -0.00330 56  ILE   D CB    
4397 C  CG1   . ILE   D 57  ? 0.24853 0.29462 0.22794 -0.00256 0.02572  -0.00383 56  ILE   D CG1   
4398 C  CG2   . ILE   D 57  ? 0.27946 0.32323 0.25550 0.00232  0.02471  -0.00418 56  ILE   D CG2   
4399 C  CD1   . ILE   D 57  ? 0.26691 0.31366 0.24410 -0.00068 0.02600  -0.00238 56  ILE   D CD1   
4400 N  N     . ILE   D 58  ? 0.25889 0.30272 0.24131 -0.00168 0.02532  -0.00584 57  ILE   D N     
4401 C  CA    . ILE   D 58  ? 0.29241 0.33571 0.27481 -0.00030 0.02537  -0.00580 57  ILE   D CA    
4402 C  C     . ILE   D 58  ? 0.27695 0.31766 0.25688 0.00229  0.02316  -0.00699 57  ILE   D C     
4403 O  O     . ILE   D 58  ? 0.27940 0.31875 0.26120 0.00127  0.02136  -0.00839 57  ILE   D O     
4404 C  CB    . ILE   D 58  ? 0.28270 0.32614 0.26798 -0.00247 0.02585  -0.00651 57  ILE   D CB    
4405 C  CG1   . ILE   D 58  ? 0.26224 0.30688 0.24895 -0.00436 0.02701  -0.00561 57  ILE   D CG1   
4406 C  CG2   . ILE   D 58  ? 0.28230 0.32523 0.26760 -0.00107 0.02586  -0.00646 57  ILE   D CG2   
4407 C  CD1   . ILE   D 58  ? 0.30648 0.35045 0.29461 -0.00584 0.02727  -0.00651 57  ILE   D CD1   
4408 N  N     . PRO   D 59  ? 0.28952 0.32919 0.26542 0.00599  0.02302  -0.00621 58  PRO   D N     
4409 C  CA    . PRO   D 59  ? 0.32229 0.35805 0.29449 0.00924  0.01996  -0.00774 58  PRO   D CA    
4410 C  C     . PRO   D 59  ? 0.28342 0.31755 0.25811 0.00841  0.01824  -0.00921 58  PRO   D C     
4411 O  O     . PRO   D 59  ? 0.27885 0.31465 0.25574 0.00723  0.02007  -0.00866 58  PRO   D O     
4412 C  CB    . PRO   D 59  ? 0.30703 0.34211 0.27372 0.01409  0.02114  -0.00609 58  PRO   D CB    
4413 C  CG    . PRO   D 59  ? 0.29474 0.33386 0.26316 0.01306  0.02455  -0.00329 58  PRO   D CG    
4414 C  CD    . PRO   D 59  ? 0.32142 0.36314 0.29605 0.00792  0.02553  -0.00349 58  PRO   D CD    
4415 N  N     . GLY   D 60  ? 0.30301 0.33385 0.27816 0.00887  0.01441  -0.01092 59  GLY   D N     
4416 C  CA    . GLY   D 60  ? 0.34860 0.37798 0.32771 0.00776  0.01233  -0.01194 59  GLY   D CA    
4417 C  C     . GLY   D 60  ? 0.32618 0.35809 0.31238 0.00355  0.01320  -0.01151 59  GLY   D C     
4418 O  O     . GLY   D 60  ? 0.31055 0.34160 0.30132 0.00261  0.01153  -0.01177 59  GLY   D O     
4419 N  N     . PHE   D 61  ? 0.28766 0.32259 0.27484 0.00137  0.01588  -0.01058 60  PHE   D N     
4420 C  CA    . PHE   D 61  ? 0.26133 0.29858 0.25390 -0.00171 0.01758  -0.00982 60  PHE   D CA    
4421 C  C     . PHE   D 61  ? 0.28551 0.32383 0.27930 -0.00301 0.01787  -0.00925 60  PHE   D C     
4422 O  O     . PHE   D 61  ? 0.24347 0.28134 0.24187 -0.00374 0.01610  -0.00879 60  PHE   D O     
4423 C  CB    . PHE   D 61  ? 0.25816 0.29771 0.25043 -0.00297 0.02109  -0.00926 60  PHE   D CB    
4424 C  CG    . PHE   D 61  ? 0.27841 0.31736 0.27119 -0.00233 0.02107  -0.00958 60  PHE   D CG    
4425 C  CD1   . PHE   D 61  ? 0.27981 0.31874 0.27707 -0.00325 0.02082  -0.00941 60  PHE   D CD1   
4426 C  CD2   . PHE   D 61  ? 0.34018 0.37866 0.32926 -0.00046 0.02134  -0.00965 60  PHE   D CD2   
4427 C  CE1   . PHE   D 61  ? 0.35142 0.38968 0.34913 -0.00266 0.02064  -0.00978 60  PHE   D CE1   
4428 C  CE2   . PHE   D 61  ? 0.36007 0.39789 0.34954 0.00026  0.02125  -0.00994 60  PHE   D CE2   
4429 C  CZ    . PHE   D 61  ? 0.38315 0.42071 0.37668 -0.00095 0.02074  -0.01025 60  PHE   D CZ    
4430 N  N     A MET   D 62  ? 0.26172 0.30147 0.25228 -0.00334 0.01991  -0.00897 61  MET   D N     
4431 N  N     B MET   D 62  ? 0.28464 0.32437 0.27517 -0.00332 0.01989  -0.00897 61  MET   D N     
4432 C  CA    A MET   D 62  ? 0.27673 0.31752 0.26842 -0.00467 0.02045  -0.00844 61  MET   D CA    
4433 C  CA    B MET   D 62  ? 0.24481 0.28558 0.23650 -0.00465 0.02041  -0.00845 61  MET   D CA    
4434 C  C     A MET   D 62  ? 0.27287 0.31453 0.26050 -0.00451 0.02175  -0.00829 61  MET   D C     
4435 C  C     B MET   D 62  ? 0.26058 0.30233 0.24833 -0.00461 0.02186  -0.00826 61  MET   D C     
4436 O  O     A MET   D 62  ? 0.28000 0.32213 0.26522 -0.00379 0.02284  -0.00800 61  MET   D O     
4437 O  O     B MET   D 62  ? 0.27722 0.31953 0.26276 -0.00409 0.02309  -0.00797 61  MET   D O     
4438 C  CB    A MET   D 62  ? 0.24746 0.28991 0.24265 -0.00642 0.02281  -0.00747 61  MET   D CB    
4439 C  CB    B MET   D 62  ? 0.24719 0.28957 0.24274 -0.00639 0.02261  -0.00745 61  MET   D CB    
4440 C  CG    A MET   D 62  ? 0.27600 0.31942 0.26821 -0.00709 0.02548  -0.00742 61  MET   D CG    
4441 C  CG    B MET   D 62  ? 0.28628 0.32943 0.27997 -0.00683 0.02520  -0.00746 61  MET   D CG    
4442 S  SD    A MET   D 62  ? 0.22422 0.26739 0.21465 -0.00669 0.02617  -0.00787 61  MET   D SD    
4443 S  SD    B MET   D 62  ? 0.30892 0.35262 0.29899 -0.00756 0.02683  -0.00740 61  MET   D SD    
4444 C  CE    A MET   D 62  ? 0.29320 0.33671 0.28067 -0.00733 0.02710  -0.00763 61  MET   D CE    
4445 C  CE    B MET   D 62  ? 0.29746 0.34088 0.28535 -0.00749 0.02733  -0.00769 61  MET   D CE    
4446 N  N     . CYS   D 63  ? 0.25107 0.29319 0.23892 -0.00530 0.02168  -0.00806 62  CYS   D N     
4447 C  CA    . CYS   D 63  ? 0.25366 0.29681 0.23883 -0.00570 0.02295  -0.00768 62  CYS   D CA    
4448 C  C     . CYS   D 63  ? 0.22401 0.26807 0.21058 -0.00750 0.02462  -0.00732 62  CYS   D C     
4449 O  O     . CYS   D 63  ? 0.26568 0.30985 0.25483 -0.00795 0.02436  -0.00698 62  CYS   D O     
4450 C  CB    . CYS   D 63  ? 0.25018 0.29252 0.23336 -0.00454 0.02122  -0.00785 62  CYS   D CB    
4451 S  SG    . CYS   D 63  ? 0.32779 0.36780 0.30670 -0.00074 0.01909  -0.00826 62  CYS   D SG    
4452 N  N     . GLN   D 64  ? 0.22386 0.26825 0.20880 -0.00816 0.02603  -0.00717 63  GLN   D N     
4453 C  CA    . GLN   D 64  ? 0.22998 0.27406 0.21452 -0.00894 0.02734  -0.00711 63  GLN   D CA    
4454 C  C     . GLN   D 64  ? 0.25044 0.29430 0.23265 -0.00946 0.02721  -0.00709 63  GLN   D C     
4455 O  O     . GLN   D 64  ? 0.22460 0.26873 0.20626 -0.00955 0.02660  -0.00675 63  GLN   D O     
4456 C  CB    . GLN   D 64  ? 0.26808 0.31127 0.25225 -0.00882 0.02825  -0.00733 63  GLN   D CB    
4457 C  CG    . GLN   D 64  ? 0.25409 0.29570 0.23577 -0.00852 0.02930  -0.00748 63  GLN   D CG    
4458 C  CD    . GLN   D 64  ? 0.27587 0.31593 0.25649 -0.00780 0.02982  -0.00786 63  GLN   D CD    
4459 O  OE1   . GLN   D 64  ? 0.28054 0.32133 0.26326 -0.00781 0.02982  -0.00781 63  GLN   D OE1   
4460 N  NE2   . GLN   D 64  ? 0.25179 0.28917 0.22856 -0.00681 0.02996  -0.00838 63  GLN   D NE2   
4461 N  N     . GLY   D 65  ? 0.22960 0.27309 0.21100 -0.00962 0.02786  -0.00705 64  GLY   D N     
4462 C  CA    . GLY   D 65  ? 0.22744 0.27028 0.20652 -0.01008 0.02745  -0.00717 64  GLY   D CA    
4463 C  C     . GLY   D 65  ? 0.28068 0.32204 0.25752 -0.00956 0.02849  -0.00730 64  GLY   D C     
4464 O  O     . GLY   D 65  ? 0.24083 0.28148 0.21740 -0.00848 0.02990  -0.00707 64  GLY   D O     
4465 N  N     . GLY   D 66  ? 0.25390 0.29460 0.22875 -0.00988 0.02793  -0.00746 65  GLY   D N     
4466 C  CA    . GLY   D 66  ? 0.24307 0.28231 0.21517 -0.00885 0.02903  -0.00742 65  GLY   D CA    
4467 C  C     . GLY   D 66  ? 0.31305 0.34840 0.28034 -0.00788 0.02803  -0.00845 65  GLY   D C     
4468 O  O     . GLY   D 66  ? 0.30584 0.33920 0.26941 -0.00608 0.02911  -0.00845 65  GLY   D O     
4469 N  N     . ASP   D 67  ? 0.30191 0.33571 0.26916 -0.00860 0.02577  -0.00913 66  ASP   D N     
4470 C  CA    . ASP   D 67  ? 0.31446 0.34344 0.27738 -0.00762 0.02347  -0.01029 66  ASP   D CA    
4471 C  C     . ASP   D 67  ? 0.36557 0.39408 0.32842 -0.00873 0.02162  -0.01030 66  ASP   D C     
4472 O  O     . ASP   D 67  ? 0.38374 0.41309 0.35014 -0.01047 0.01952  -0.00967 66  ASP   D O     
4473 C  CB    . ASP   D 67  ? 0.28876 0.31588 0.25290 -0.00804 0.02113  -0.01069 66  ASP   D CB    
4474 C  CG    . ASP   D 67  ? 0.37744 0.39872 0.33795 -0.00718 0.01726  -0.01197 66  ASP   D CG    
4475 O  OD1   . ASP   D 67  ? 0.37956 0.39777 0.33522 -0.00571 0.01675  -0.01283 66  ASP   D OD1   
4476 O  OD2   . ASP   D 67  ? 0.37539 0.39481 0.33797 -0.00779 0.01444  -0.01207 66  ASP   D OD2   
4477 N  N     . PHE   D 68  ? 0.33314 0.36051 0.29238 -0.00754 0.02257  -0.01060 67  PHE   D N     
4478 C  CA    . PHE   D 68  ? 0.36716 0.39371 0.32586 -0.00844 0.02075  -0.01074 67  PHE   D CA    
4479 C  C     . PHE   D 68  ? 0.40877 0.42897 0.36228 -0.00689 0.01744  -0.01226 67  PHE   D C     
4480 O  O     . PHE   D 68  ? 0.40568 0.42441 0.35831 -0.00738 0.01556  -0.01252 67  PHE   D O     
4481 C  CB    . PHE   D 68  ? 0.36528 0.39418 0.32331 -0.00813 0.02332  -0.01014 67  PHE   D CB    
4482 C  CG    . PHE   D 68  ? 0.39201 0.41893 0.34532 -0.00511 0.02576  -0.01014 67  PHE   D CG    
4483 C  CD1   . PHE   D 68  ? 0.39225 0.41413 0.33883 -0.00261 0.02478  -0.01118 67  PHE   D CD1   
4484 C  CD2   . PHE   D 68  ? 0.35128 0.38120 0.30702 -0.00435 0.02902  -0.00873 67  PHE   D CD2   
4485 C  CE1   . PHE   D 68  ? 0.41069 0.43076 0.35234 0.00108  0.02762  -0.01060 67  PHE   D CE1   
4486 C  CE2   . PHE   D 68  ? 0.33611 0.36481 0.28843 -0.00108 0.03193  -0.00770 67  PHE   D CE2   
4487 C  CZ    . PHE   D 68  ? 0.36889 0.39268 0.31368 0.00193  0.03154  -0.00855 67  PHE   D CZ    
4488 N  N     . THR   D 69  ? 0.38101 0.39677 0.33044 -0.00467 0.01636  -0.01342 68  THR   D N     
4489 C  CA    . THR   D 69  ? 0.42725 0.43557 0.37072 -0.00263 0.01216  -0.01523 68  THR   D CA    
4490 C  C     . THR   D 69  ? 0.46431 0.46985 0.41155 -0.00431 0.00697  -0.01554 68  THR   D C     
4491 O  O     . THR   D 69  ? 0.47076 0.47190 0.41749 -0.00456 0.00231  -0.01624 68  THR   D O     
4492 C  CB    . THR   D 69  ? 0.43050 0.43368 0.36504 0.00212  0.01337  -0.01648 68  THR   D CB    
4493 O  OG1   . THR   D 69  ? 0.41082 0.41362 0.34601 0.00270  0.01355  -0.01661 68  THR   D OG1   
4494 C  CG2   . THR   D 69  ? 0.42711 0.43364 0.35953 0.00401  0.01891  -0.01512 68  THR   D CG2   
4495 N  N     . ARG   D 70  ? 0.42950 0.43773 0.38141 -0.00558 0.00756  -0.01471 69  ARG   D N     
4496 C  CA    . ARG   D 70  ? 0.41387 0.41988 0.37072 -0.00716 0.00274  -0.01435 69  ARG   D CA    
4497 C  C     . ARG   D 70  ? 0.45688 0.46999 0.42365 -0.01061 0.00408  -0.01143 69  ARG   D C     
4498 O  O     . ARG   D 70  ? 0.46155 0.47403 0.43453 -0.01223 0.00040  -0.00999 69  ARG   D O     
4499 C  CB    . ARG   D 70  ? 0.45519 0.45745 0.40859 -0.00508 0.00190  -0.01568 69  ARG   D CB    
4500 C  CG    . ARG   D 70  ? 0.45557 0.45033 0.39785 -0.00049 0.00097  -0.01827 69  ARG   D CG    
4501 C  CD    . ARG   D 70  ? 0.52338 0.51375 0.46265 0.00159  -0.00087 -0.01950 69  ARG   D CD    
4502 N  NE    . ARG   D 70  ? 0.51454 0.49779 0.44194 0.00710  -0.00083 -0.02168 69  ARG   D NE    
4503 C  CZ    . ARG   D 70  ? 0.57871 0.56002 0.50141 0.01014  0.00090  -0.02228 69  ARG   D CZ    
4504 N  NH1   . ARG   D 70  ? 0.47333 0.45783 0.40207 0.00789  0.00113  -0.02152 69  ARG   D NH1   
4505 N  NH2   . ARG   D 70  ? 0.65594 0.63214 0.56773 0.01580  0.00264  -0.02338 69  ARG   D NH2   
4506 N  N     . HIS   D 71  ? 0.41106 0.43027 0.37925 -0.01124 0.00893  -0.01035 70  HIS   D N     
4507 C  CA    . HIS   D 71  ? 0.43347 0.45877 0.40908 -0.01334 0.01052  -0.00765 70  HIS   D CA    
4508 C  C     . HIS   D 71  ? 0.43077 0.45671 0.41134 -0.01397 0.00936  -0.00635 70  HIS   D C     
4509 O  O     . HIS   D 71  ? 0.47823 0.50715 0.46585 -0.01537 0.00868  -0.00350 70  HIS   D O     
4510 C  CB    . HIS   D 71  ? 0.42197 0.44854 0.40156 -0.01480 0.00891  -0.00589 70  HIS   D CB    
4511 C  CG    . HIS   D 71  ? 0.48983 0.51638 0.46498 -0.01432 0.01032  -0.00699 70  HIS   D CG    
4512 N  ND1   . HIS   D 71  ? 0.53287 0.55419 0.50328 -0.01344 0.00763  -0.00879 70  HIS   D ND1   
4513 C  CD2   . HIS   D 71  ? 0.47289 0.50352 0.44723 -0.01430 0.01392  -0.00665 70  HIS   D CD2   
4514 C  CE1   . HIS   D 71  ? 0.52910 0.55196 0.49650 -0.01310 0.00998  -0.00921 70  HIS   D CE1   
4515 N  NE2   . HIS   D 71  ? 0.49884 0.52732 0.46886 -0.01374 0.01364  -0.00793 70  HIS   D NE2   
4516 N  N     . ASN   D 72  ? 0.45135 0.47471 0.42843 -0.01267 0.00947  -0.00807 71  ASN   D N     
4517 C  CA    . ASN   D 72  ? 0.48254 0.50677 0.46438 -0.01329 0.00860  -0.00683 71  ASN   D CA    
4518 C  C     . ASN   D 72  ? 0.44588 0.47065 0.42470 -0.01205 0.01134  -0.00807 71  ASN   D C     
4519 O  O     . ASN   D 72  ? 0.49973 0.52374 0.48093 -0.01218 0.01008  -0.00774 71  ASN   D O     
4520 C  CB    . ASN   D 72  ? 0.44425 0.46283 0.42790 -0.01355 0.00275  -0.00705 71  ASN   D CB    
4521 C  CG    . ASN   D 72  ? 0.46213 0.47334 0.43703 -0.01106 0.00035  -0.01053 71  ASN   D CG    
4522 O  OD1   . ASN   D 72  ? 0.40182 0.41278 0.37011 -0.00903 0.00374  -0.01225 71  ASN   D OD1   
4523 N  ND2   . ASN   D 72  ? 0.45104 0.45580 0.42598 -0.01079 -0.00577 -0.01132 71  ASN   D ND2   
4524 N  N     . GLY   D 73  ? 0.36507 0.39124 0.33965 -0.01092 0.01485  -0.00914 72  GLY   D N     
4525 C  CA    . GLY   D 73  ? 0.36446 0.39137 0.33739 -0.00980 0.01734  -0.00981 72  GLY   D CA    
4526 C  C     . GLY   D 73  ? 0.39167 0.41353 0.35825 -0.00734 0.01686  -0.01176 72  GLY   D C     
4527 O  O     . GLY   D 73  ? 0.37935 0.40203 0.34453 -0.00609 0.01945  -0.01198 72  GLY   D O     
4528 N  N     . THR   D 74  ? 0.35683 0.37301 0.31919 -0.00614 0.01343  -0.01308 73  THR   D N     
4529 C  CA    . THR   D 74  ? 0.36371 0.37405 0.31855 -0.00274 0.01271  -0.01495 73  THR   D CA    
4530 C  C     . THR   D 74  ? 0.38726 0.39526 0.33499 0.00016  0.01457  -0.01568 73  THR   D C     
4531 O  O     . THR   D 74  ? 0.47683 0.48090 0.41757 0.00399  0.01566  -0.01658 73  THR   D O     
4532 C  CB    . THR   D 74  ? 0.40200 0.40567 0.35553 -0.00227 0.00667  -0.01627 73  THR   D CB    
4533 O  OG1   . THR   D 74  ? 0.41195 0.41235 0.36434 -0.00249 0.00317  -0.01674 73  THR   D OG1   
4534 C  CG2   . THR   D 74  ? 0.34032 0.34692 0.30254 -0.00533 0.00484  -0.01470 73  THR   D CG2   
4535 N  N     . GLY   D 75  ? 0.38826 0.39864 0.33744 -0.00117 0.01524  -0.01501 74  GLY   D N     
4536 C  CA    . GLY   D 75  ? 0.43720 0.44471 0.37965 0.00166  0.01632  -0.01560 74  GLY   D CA    
4537 C  C     . GLY   D 75  ? 0.45404 0.46695 0.39790 0.00190  0.02171  -0.01387 74  GLY   D C     
4538 O  O     . GLY   D 75  ? 0.36255 0.37967 0.31025 0.00136  0.02476  -0.01261 74  GLY   D O     
4539 N  N     . GLY   D 76  ? 0.39997 0.41245 0.34125 0.00266  0.02236  -0.01371 75  GLY   D N     
4540 C  CA    . GLY   D 76  ? 0.39592 0.41283 0.33868 0.00330  0.02706  -0.01175 75  GLY   D CA    
4541 C  C     . GLY   D 76  ? 0.40024 0.41325 0.33502 0.00842  0.02940  -0.01141 75  GLY   D C     
4542 O  O     . GLY   D 76  ? 0.40860 0.41587 0.33657 0.01187  0.02807  -0.01272 75  GLY   D O     
4543 N  N     . LYS   D 77  ? 0.37294 0.38870 0.30833 0.00927  0.03268  -0.00953 76  LYS   D N     
4544 C  CA    . LYS   D 77  ? 0.37236 0.38527 0.30065 0.01485  0.03604  -0.00816 76  LYS   D CA    
4545 C  C     . LYS   D 77  ? 0.31294 0.33219 0.24750 0.01445  0.04073  -0.00454 76  LYS   D C     
4546 O  O     . LYS   D 77  ? 0.31831 0.34200 0.25989 0.01019  0.03996  -0.00423 76  LYS   D O     
4547 C  CB    . LYS   D 77  ? 0.39388 0.40002 0.31287 0.01772  0.03333  -0.01020 76  LYS   D CB    
4548 C  CG    . LYS   D 77  ? 0.37508 0.38317 0.29654 0.01496  0.03230  -0.01030 76  LYS   D CG    
4549 C  CD    . LYS   D 77  ? 0.41656 0.41709 0.32782 0.01875  0.02973  -0.01223 76  LYS   D CD    
4550 C  CE    . LYS   D 77  ? 0.46721 0.46855 0.38101 0.01527  0.02698  -0.01317 76  LYS   D CE    
4551 N  NZ    . LYS   D 77  ? 0.56052 0.55374 0.46438 0.01898  0.02369  -0.01532 76  LYS   D NZ    
4552 N  N     . SER   D 78  ? 0.32782 0.34704 0.25975 0.01925  0.04529  -0.00164 77  SER   D N     
4553 C  CA    . SER   D 78  ? 0.34642 0.37174 0.28578 0.01919  0.04974  0.00271  77  SER   D CA    
4554 C  C     . SER   D 78  ? 0.44692 0.47061 0.38134 0.02202  0.05122  0.00368  77  SER   D C     
4555 O  O     . SER   D 78  ? 0.36360 0.38079 0.28774 0.02478  0.04899  0.00093  77  SER   D O     
4556 C  CB    . SER   D 78  ? 0.31932 0.34666 0.26075 0.02292  0.05455  0.00661  77  SER   D CB    
4557 O  OG    . SER   D 78  ? 0.36610 0.38913 0.29778 0.03002  0.05787  0.00816  77  SER   D OG    
4558 N  N     . ILE   D 79  ? 0.35672 0.38594 0.29886 0.02117  0.05433  0.00748  78  ILE   D N     
4559 C  CA    . ILE   D 79  ? 0.34172 0.36990 0.27957 0.02459  0.05675  0.00932  78  ILE   D CA    
4560 C  C     . ILE   D 79  ? 0.37632 0.40171 0.30663 0.03246  0.06179  0.01252  78  ILE   D C     
4561 O  O     . ILE   D 79  ? 0.43228 0.45614 0.35751 0.03641  0.06421  0.01424  78  ILE   D O     
4562 C  CB    . ILE   D 79  ? 0.37839 0.41343 0.32774 0.02139  0.05840  0.01291  78  ILE   D CB    
4563 C  CG1   . ILE   D 79  ? 0.38141 0.42201 0.34102 0.02216  0.06250  0.01832  78  ILE   D CG1   
4564 C  CG2   . ILE   D 79  ? 0.38330 0.42020 0.33808 0.01464  0.05337  0.00960  78  ILE   D CG2   
4565 C  CD1   . ILE   D 79  ? 0.41409 0.46074 0.38545 0.02005  0.06405  0.02276  78  ILE   D CD1   
4566 N  N     . TYR   D 80  ? 0.36136 0.38593 0.29031 0.03534  0.06369  0.01358  79  TYR   D N     
4567 C  CA    . TYR   D 80  ? 0.41830 0.43993 0.33916 0.04380  0.06890  0.01696  79  TYR   D CA    
4568 C  C     . TYR   D 80  ? 0.41080 0.42265 0.31588 0.04880  0.06610  0.01251  79  TYR   D C     
4569 O  O     . TYR   D 80  ? 0.42761 0.43544 0.32326 0.05694  0.06998  0.01472  79  TYR   D O     
4570 C  CB    . TYR   D 80  ? 0.39630 0.42348 0.32622 0.04475  0.07349  0.02203  79  TYR   D CB    
4571 C  CG    . TYR   D 80  ? 0.40150 0.43750 0.34812 0.03946  0.07478  0.02615  79  TYR   D CG    
4572 C  CD1   . TYR   D 80  ? 0.41131 0.45113 0.36305 0.04076  0.07829  0.03090  79  TYR   D CD1   
4573 C  CD2   . TYR   D 80  ? 0.37063 0.41065 0.32790 0.03342  0.07206  0.02535  79  TYR   D CD2   
4574 C  CE1   . TYR   D 80  ? 0.44005 0.48733 0.40781 0.03589  0.07852  0.03472  79  TYR   D CE1   
4575 C  CE2   . TYR   D 80  ? 0.37907 0.42598 0.35122 0.02899  0.07220  0.02887  79  TYR   D CE2   
4576 C  CZ    . TYR   D 80  ? 0.43823 0.48865 0.41591 0.03009  0.07513  0.03351  79  TYR   D CZ    
4577 O  OH    . TYR   D 80  ? 0.36666 0.42325 0.35969 0.02568  0.07432  0.03699  79  TYR   D OH    
4578 N  N     . GLY   D 81  ? 0.42568 0.43390 0.32879 0.04421  0.05943  0.00678  80  GLY   D N     
4579 C  CA    . GLY   D 81  ? 0.40998 0.40882 0.30051 0.04775  0.05519  0.00229  80  GLY   D CA    
4580 C  C     . GLY   D 81  ? 0.41899 0.41911 0.31599 0.04122  0.05038  -0.00097 80  GLY   D C     
4581 O  O     . GLY   D 81  ? 0.37244 0.38011 0.28183 0.03490  0.05072  0.00024  80  GLY   D O     
4582 N  N     . GLU   D 82  ? 0.42962 0.42230 0.31849 0.04298  0.04582  -0.00483 81  GLU   D N     
4583 C  CA    . GLU   D 82  ? 0.44842 0.44240 0.34394 0.03674  0.04115  -0.00761 81  GLU   D CA    
4584 C  C     . GLU   D 82  ? 0.41750 0.41959 0.32377 0.03406  0.04535  -0.00437 81  GLU   D C     
4585 O  O     . GLU   D 82  ? 0.39968 0.40736 0.31625 0.02753  0.04386  -0.00464 81  GLU   D O     
4586 C  CB    . GLU   D 82  ? 0.51134 0.49622 0.39736 0.03979  0.03611  -0.01137 81  GLU   D CB    
4587 C  CG    . GLU   D 82  ? 0.57397 0.56117 0.46753 0.03454  0.03305  -0.01286 81  GLU   D CG    
4588 C  CD    . GLU   D 82  ? 0.68402 0.66248 0.57102 0.03555  0.02611  -0.01692 81  GLU   D CD    
4589 O  OE1   . GLU   D 82  ? 0.67474 0.64593 0.55100 0.04207  0.02578  -0.01784 81  GLU   D OE1   
4590 O  OE2   . GLU   D 82  ? 0.69117 0.66995 0.58403 0.03009  0.02094  -0.01888 81  GLU   D OE2   
4591 N  N     . LYS   D 83  ? 0.34770 0.34991 0.25117 0.03945  0.05029  -0.00129 82  LYS   D N     
4592 C  CA    . LYS   D 83  ? 0.36285 0.37218 0.27674 0.03729  0.05394  0.00200  82  LYS   D CA    
4593 C  C     . LYS   D 83  ? 0.43492 0.44842 0.35126 0.04198  0.06122  0.00804  82  LYS   D C     
4594 O  O     . LYS   D 83  ? 0.39203 0.40145 0.29895 0.04846  0.06375  0.00934  82  LYS   D O     
4595 C  CB    . LYS   D 83  ? 0.45926 0.46487 0.36926 0.03880  0.05230  0.00009  82  LYS   D CB    
4596 C  CG    . LYS   D 83  ? 0.48412 0.48881 0.39742 0.03276  0.04608  -0.00418 82  LYS   D CG    
4597 C  CD    . LYS   D 83  ? 0.51194 0.50950 0.41729 0.03538  0.04254  -0.00729 82  LYS   D CD    
4598 C  CE    . LYS   D 83  ? 0.60210 0.59823 0.51069 0.02980  0.03604  -0.01103 82  LYS   D CE    
4599 N  NZ    . LYS   D 83  ? 0.68139 0.67704 0.59186 0.02876  0.03452  -0.01205 82  LYS   D NZ    
4600 N  N     . PHE   D 84  ? 0.32368 0.34495 0.25286 0.03876  0.06410  0.01178  83  PHE   D N     
4601 C  CA    . PHE   D 84  ? 0.33592 0.36217 0.27063 0.04278  0.07103  0.01865  83  PHE   D CA    
4602 C  C     . PHE   D 84  ? 0.37119 0.40191 0.31490 0.04167  0.07307  0.02145  83  PHE   D C     
4603 O  O     . PHE   D 84  ? 0.30429 0.33570 0.25221 0.03654  0.06912  0.01826  83  PHE   D O     
4604 C  CB    . PHE   D 84  ? 0.30864 0.34055 0.25250 0.04011  0.07258  0.02194  83  PHE   D CB    
4605 C  CG    . PHE   D 84  ? 0.33477 0.37263 0.29243 0.03195  0.06937  0.02148  83  PHE   D CG    
4606 C  CD1   . PHE   D 84  ? 0.28345 0.31957 0.24001 0.02650  0.06350  0.01602  83  PHE   D CD1   
4607 C  CD2   . PHE   D 84  ? 0.34554 0.39032 0.31725 0.03025  0.07203  0.02682  83  PHE   D CD2   
4608 C  CE1   . PHE   D 84  ? 0.32478 0.36553 0.29226 0.02020  0.06068  0.01563  83  PHE   D CE1   
4609 C  CE2   . PHE   D 84  ? 0.30882 0.35763 0.29173 0.02355  0.06826  0.02598  83  PHE   D CE2   
4610 C  CZ    . PHE   D 84  ? 0.26763 0.31422 0.24758 0.01887  0.06275  0.02027  83  PHE   D CZ    
4611 N  N     . GLU   D 85  ? 0.34099 0.37498 0.28814 0.04670  0.07944  0.02788  84  GLU   D N     
4612 C  CA    . GLU   D 85  ? 0.33611 0.37398 0.29136 0.04677  0.08194  0.03125  84  GLU   D CA    
4613 C  C     . GLU   D 85  ? 0.34732 0.39250 0.31993 0.03935  0.08010  0.03300  84  GLU   D C     
4614 O  O     . GLU   D 85  ? 0.34031 0.38836 0.31963 0.03515  0.07813  0.03308  84  GLU   D O     
4615 C  CB    . GLU   D 85  ? 0.42595 0.46555 0.38055 0.05495  0.08983  0.03869  84  GLU   D CB    
4616 C  CG    . GLU   D 85  ? 0.47768 0.52356 0.44292 0.05499  0.09373  0.04514  84  GLU   D CG    
4617 C  CD    . GLU   D 85  ? 0.60949 0.65203 0.56626 0.05647  0.09297  0.04319  84  GLU   D CD    
4618 O  OE1   . GLU   D 85  ? 0.56058 0.59511 0.50094 0.06045  0.09121  0.03837  84  GLU   D OE1   
4619 O  OE2   . GLU   D 85  ? 0.63342 0.68102 0.60025 0.05351  0.09356  0.04634  84  GLU   D OE2   
4620 N  N     . ASP   D 86  ? 0.32226 0.36947 0.30084 0.03816  0.08022  0.03394  85  ASP   D N     
4621 C  CA    . ASP   D 86  ? 0.29035 0.34368 0.28526 0.03206  0.07823  0.03596  85  ASP   D CA    
4622 C  C     . ASP   D 86  ? 0.32320 0.38268 0.33048 0.03400  0.08310  0.04429  85  ASP   D C     
4623 O  O     . ASP   D 86  ? 0.35939 0.42049 0.36776 0.03960  0.08891  0.04997  85  ASP   D O     
4624 C  CB    . ASP   D 86  ? 0.30688 0.36015 0.30399 0.03087  0.07710  0.03477  85  ASP   D CB    
4625 C  CG    . ASP   D 86  ? 0.34863 0.39637 0.33539 0.02867  0.07216  0.02719  85  ASP   D CG    
4626 O  OD1   . ASP   D 86  ? 0.28726 0.33380 0.27284 0.02424  0.06751  0.02282  85  ASP   D OD1   
4627 O  OD2   . ASP   D 86  ? 0.36443 0.40922 0.34487 0.03160  0.07306  0.02610  85  ASP   D OD2   
4628 N  N     . GLU   D 87  ? 0.29174 0.35443 0.30819 0.02976  0.08076  0.04526  86  GLU   D N     
4629 C  CA    . GLU   D 87  ? 0.31556 0.38423 0.34545 0.03115  0.08473  0.05358  86  GLU   D CA    
4630 C  C     . GLU   D 87  ? 0.30001 0.37359 0.34492 0.03041  0.08599  0.05922  86  GLU   D C     
4631 O  O     . GLU   D 87  ? 0.30703 0.38384 0.35655 0.03571  0.09242  0.06670  86  GLU   D O     
4632 C  CB    . GLU   D 87  ? 0.29165 0.36188 0.32818 0.02593  0.08035  0.05231  86  GLU   D CB    
4633 C  CG    . GLU   D 87  ? 0.38595 0.46183 0.43602 0.02714  0.08376  0.06060  86  GLU   D CG    
4634 C  CD    . GLU   D 87  ? 0.33028 0.40593 0.38082 0.02390  0.08041  0.05848  86  GLU   D CD    
4635 O  OE1   . GLU   D 87  ? 0.31884 0.39075 0.36215 0.01984  0.07486  0.05101  86  GLU   D OE1   
4636 O  OE2   . GLU   D 87  ? 0.38606 0.46544 0.44444 0.02569  0.08362  0.06472  86  GLU   D OE2   
4637 N  N     . ASN   D 88  ? 0.25260 0.32679 0.30555 0.02428  0.08001  0.05623  87  ASN   D N     
4638 C  CA    . ASN   D 88  ? 0.24990 0.32773 0.31639 0.02321  0.08004  0.06059  87  ASN   D CA    
4639 C  C     . ASN   D 88  ? 0.24432 0.31965 0.31120 0.01737  0.07273  0.05393  87  ASN   D C     
4640 O  O     . ASN   D 88  ? 0.27630 0.34808 0.33510 0.01424  0.06812  0.04719  87  ASN   D O     
4641 C  CB    . ASN   D 88  ? 0.27595 0.35997 0.36185 0.02251  0.08116  0.06922  87  ASN   D CB    
4642 C  CG    . ASN   D 88  ? 0.28274 0.36683 0.37608 0.01664  0.07433  0.06685  87  ASN   D CG    
4643 O  OD1   . ASN   D 88  ? 0.26747 0.34936 0.36249 0.01178  0.06755  0.06172  87  ASN   D OD1   
4644 N  ND2   . ASN   D 88  ? 0.30903 0.39540 0.40653 0.01753  0.07609  0.07072  87  ASN   D ND2   
4645 N  N     . PHE   D 89  ? 0.26351 0.34075 0.33984 0.01636  0.07195  0.05626  88  PHE   D N     
4646 C  CA    . PHE   D 89  ? 0.25540 0.33036 0.33287 0.01161  0.06542  0.05083  88  PHE   D CA    
4647 C  C     . PHE   D 89  ? 0.27146 0.34961 0.36759 0.00821  0.06132  0.05504  88  PHE   D C     
4648 O  O     . PHE   D 89  ? 0.30020 0.37796 0.40188 0.00627  0.05812  0.05428  88  PHE   D O     
4649 C  CB    . PHE   D 89  ? 0.26739 0.34025 0.33707 0.01346  0.06709  0.04838  88  PHE   D CB    
4650 C  CG    . PHE   D 89  ? 0.33395 0.40238 0.38522 0.01649  0.06937  0.04345  88  PHE   D CG    
4651 C  CD1   . PHE   D 89  ? 0.27896 0.34326 0.32010 0.01359  0.06484  0.03607  88  PHE   D CD1   
4652 C  CD2   . PHE   D 89  ? 0.34811 0.41615 0.39246 0.02264  0.07579  0.04651  88  PHE   D CD2   
4653 C  CE1   . PHE   D 89  ? 0.30609 0.36603 0.33205 0.01615  0.06604  0.03192  88  PHE   D CE1   
4654 C  CE2   . PHE   D 89  ? 0.32034 0.38319 0.34786 0.02567  0.07673  0.04181  88  PHE   D CE2   
4655 C  CZ    . PHE   D 89  ? 0.33817 0.39692 0.35705 0.02207  0.07147  0.03441  88  PHE   D CZ    
4656 N  N     . ILE   D 90  ? 0.26967 0.35062 0.37592 0.00753  0.06091  0.05956  89  ILE   D N     
4657 C  CA    . ILE   D 90  ? 0.31316 0.39681 0.43879 0.00460  0.05644  0.06440  89  ILE   D CA    
4658 C  C     . ILE   D 90  ? 0.27667 0.35595 0.40197 -0.00023 0.04722  0.05768  89  ILE   D C     
4659 O  O     . ILE   D 90  ? 0.27451 0.35348 0.40977 -0.00217 0.04281  0.05856  89  ILE   D O     
4660 C  CB    . ILE   D 90  ? 0.29317 0.38068 0.43019 0.00505  0.05783  0.07104  89  ILE   D CB    
4661 C  CG1   . ILE   D 90  ? 0.25587 0.34841 0.39638 0.01070  0.06740  0.07968  89  ILE   D CG1   
4662 C  CG2   . ILE   D 90  ? 0.29840 0.38730 0.45569 0.00117  0.05079  0.07489  89  ILE   D CG2   
4663 C  CD1   . ILE   D 90  ? 0.32766 0.42314 0.47277 0.01219  0.07026  0.08466  89  ILE   D CD1   
4664 N  N     . LEU   D 91  ? 0.25479 0.33031 0.36787 -0.00171 0.04433  0.05092  90  LEU   D N     
4665 C  CA    . LEU   D 91  ? 0.24365 0.31472 0.35496 -0.00531 0.03597  0.04480  90  LEU   D CA    
4666 C  C     . LEU   D 91  ? 0.29029 0.35788 0.38957 -0.00543 0.03516  0.03853  90  LEU   D C     
4667 O  O     . LEU   D 91  ? 0.24979 0.31724 0.33768 -0.00328 0.04027  0.03672  90  LEU   D O     
4668 C  CB    . LEU   D 91  ? 0.23609 0.30530 0.34122 -0.00645 0.03365  0.04153  90  LEU   D CB    
4669 C  CG    . LEU   D 91  ? 0.29732 0.36980 0.41607 -0.00674 0.03339  0.04785  90  LEU   D CG    
4670 C  CD1   . LEU   D 91  ? 0.29270 0.36380 0.40433 -0.00737 0.03239  0.04499  90  LEU   D CD1   
4671 C  CD2   . LEU   D 91  ? 0.35189 0.42366 0.48683 -0.00927 0.02587  0.05035  90  LEU   D CD2   
4672 N  N     . LYS   D 92  ? 0.23388 0.29825 0.33585 -0.00765 0.02837  0.03536  91  LYS   D N     
4673 C  CA    . LYS   D 92  ? 0.25153 0.31294 0.34423 -0.00768 0.02742  0.03027  91  LYS   D CA    
4674 C  C     . LYS   D 92  ? 0.23785 0.29467 0.31980 -0.00890 0.02263  0.02347  91  LYS   D C     
4675 O  O     . LYS   D 92  ? 0.25677 0.31204 0.34007 -0.00993 0.01857  0.02258  91  LYS   D O     
4676 C  CB    . LYS   D 92  ? 0.26492 0.32603 0.36820 -0.00842 0.02398  0.03221  91  LYS   D CB    
4677 C  CG    . LYS   D 92  ? 0.35878 0.42489 0.47540 -0.00714 0.02841  0.04005  91  LYS   D CG    
4678 C  CD    . LYS   D 92  ? 0.31119 0.38009 0.42000 -0.00397 0.03719  0.04170  91  LYS   D CD    
4679 C  CE    . LYS   D 92  ? 0.38049 0.45435 0.50327 -0.00203 0.04160  0.05015  91  LYS   D CE    
4680 N  NZ    . LYS   D 92  ? 0.40596 0.48355 0.52580 0.00203  0.05028  0.05500  91  LYS   D NZ    
4681 N  N     . HIS   D 93  ? 0.23328 0.28797 0.30487 -0.00850 0.02320  0.01904  92  HIS   D N     
4682 C  CA    . HIS   D 93  ? 0.23499 0.28561 0.29642 -0.00901 0.01934  0.01320  92  HIS   D CA    
4683 C  C     . HIS   D 93  ? 0.26064 0.30760 0.32640 -0.00956 0.01244  0.01161  92  HIS   D C     
4684 O  O     . HIS   D 93  ? 0.32830 0.37354 0.39089 -0.00915 0.01158  0.00948  92  HIS   D O     
4685 C  CB    . HIS   D 93  ? 0.23229 0.28253 0.28221 -0.00814 0.02310  0.01005  92  HIS   D CB    
4686 C  CG    . HIS   D 93  ? 0.25324 0.30561 0.29765 -0.00710 0.02882  0.01102  92  HIS   D CG    
4687 N  ND1   . HIS   D 93  ? 0.24835 0.30336 0.29543 -0.00549 0.03389  0.01472  92  HIS   D ND1   
4688 C  CD2   . HIS   D 93  ? 0.23658 0.28822 0.27234 -0.00697 0.03000  0.00872  92  HIS   D CD2   
4689 C  CE1   . HIS   D 93  ? 0.23256 0.28778 0.27203 -0.00415 0.03762  0.01434  92  HIS   D CE1   
4690 N  NE2   . HIS   D 93  ? 0.22544 0.27868 0.25842 -0.00532 0.03514  0.01065  92  HIS   D NE2   
4691 N  N     . THR   D 94  ? 0.26553 0.31071 0.33821 -0.01026 0.00698  0.01251  93  THR   D N     
4692 C  CA    . THR   D 94  ? 0.29190 0.33311 0.37138 -0.01046 -0.00040 0.01209  93  THR   D CA    
4693 C  C     . THR   D 94  ? 0.30509 0.34020 0.37447 -0.00922 -0.00602 0.00653  93  THR   D C     
4694 O  O     . THR   D 94  ? 0.33082 0.36139 0.40275 -0.00856 -0.01227 0.00521  93  THR   D O     
4695 C  CB    . THR   D 94  ? 0.24910 0.29075 0.34286 -0.01158 -0.00455 0.01640  93  THR   D CB    
4696 O  OG1   . THR   D 94  ? 0.32720 0.36855 0.41726 -0.01173 -0.00499 0.01554  93  THR   D OG1   
4697 C  CG2   . THR   D 94  ? 0.30414 0.35196 0.41040 -0.01215 0.00081  0.02323  93  THR   D CG2   
4698 N  N     . GLY   D 95  ? 0.28096 0.31551 0.33898 -0.00847 -0.00412 0.00350  94  GLY   D N     
4699 C  CA    . GLY   D 95  ? 0.27420 0.30313 0.32272 -0.00648 -0.00898 -0.00096 94  GLY   D CA    
4700 C  C     . GLY   D 95  ? 0.27519 0.30465 0.31418 -0.00591 -0.00649 -0.00281 94  GLY   D C     
4701 O  O     . GLY   D 95  ? 0.28144 0.31530 0.32064 -0.00722 -0.00124 -0.00108 94  GLY   D O     
4702 N  N     . PRO   D 96  ? 0.26017 0.28473 0.29029 -0.00346 -0.01038 -0.00625 95  PRO   D N     
4703 C  CA    . PRO   D 96  ? 0.27158 0.29658 0.29259 -0.00257 -0.00807 -0.00780 95  PRO   D CA    
4704 C  C     . PRO   D 96  ? 0.26414 0.29094 0.29026 -0.00424 -0.00824 -0.00593 95  PRO   D C     
4705 O  O     . PRO   D 96  ? 0.30614 0.33111 0.34074 -0.00485 -0.01317 -0.00453 95  PRO   D O     
4706 C  CB    . PRO   D 96  ? 0.29129 0.30976 0.30355 0.00124  -0.01343 -0.01109 95  PRO   D CB    
4707 C  CG    . PRO   D 96  ? 0.29655 0.31160 0.31079 0.00244  -0.01705 -0.01185 95  PRO   D CG    
4708 C  CD    . PRO   D 96  ? 0.30075 0.31876 0.32853 -0.00084 -0.01718 -0.00867 95  PRO   D CD    
4709 N  N     . GLY   D 97  ? 0.24869 0.27877 0.26976 -0.00485 -0.00329 -0.00588 96  GLY   D N     
4710 C  CA    . GLY   D 97  ? 0.27040 0.30206 0.29480 -0.00612 -0.00314 -0.00438 96  GLY   D CA    
4711 C  C     . GLY   D 97  ? 0.24007 0.27710 0.27152 -0.00837 0.00204  -0.00083 96  GLY   D C     
4712 O  O     . GLY   D 97  ? 0.24669 0.28572 0.27914 -0.00920 0.00374  0.00045  96  GLY   D O     
4713 N  N     . ILE   D 98  ? 0.24268 0.28188 0.27815 -0.00889 0.00481  0.00081  97  ILE   D N     
4714 C  CA    . ILE   D 98  ? 0.22626 0.27011 0.26738 -0.00995 0.01010  0.00452  97  ILE   D CA    
4715 C  C     . ILE   D 98  ? 0.22478 0.27055 0.25726 -0.00978 0.01533  0.00352  97  ILE   D C     
4716 O  O     . ILE   D 98  ? 0.22483 0.26955 0.24877 -0.00921 0.01640  0.00069  97  ILE   D O     
4717 C  CB    . ILE   D 98  ? 0.23061 0.27579 0.27639 -0.00989 0.01190  0.00620  97  ILE   D CB    
4718 C  CG1   . ILE   D 98  ? 0.23593 0.27960 0.29317 -0.01035 0.00652  0.00828  97  ILE   D CG1   
4719 C  CG2   . ILE   D 98  ? 0.22972 0.27917 0.27706 -0.00974 0.01856  0.00943  97  ILE   D CG2   
4720 C  CD1   . ILE   D 98  ? 0.35003 0.39615 0.41913 -0.01133 0.00598  0.01301  97  ILE   D CD1   
4721 N  N     . LEU   D 99  ? 0.24676 0.29530 0.28204 -0.01011 0.01855  0.00622  98  LEU   D N     
4722 C  CA    . LEU   D 99  ? 0.24120 0.29094 0.26879 -0.00972 0.02296  0.00550  98  LEU   D CA    
4723 C  C     . LEU   D 99  ? 0.22362 0.27585 0.25272 -0.00868 0.02824  0.00838  98  LEU   D C     
4724 O  O     . LEU   D 99  ? 0.22376 0.27831 0.26148 -0.00832 0.02964  0.01258  98  LEU   D O     
4725 C  CB    . LEU   D 99  ? 0.22326 0.27340 0.25116 -0.01017 0.02232  0.00607  98  LEU   D CB    
4726 C  CG    . LEU   D 99  ? 0.22859 0.27947 0.24901 -0.00973 0.02614  0.00539  98  LEU   D CG    
4727 C  CD1   . LEU   D 99  ? 0.26529 0.31426 0.27618 -0.00970 0.02584  0.00161  98  LEU   D CD1   
4728 C  CD2   . LEU   D 99  ? 0.23973 0.29122 0.26252 -0.01026 0.02513  0.00654  98  LEU   D CD2   
4729 N  N     . SER   D 100 ? 0.22431 0.27584 0.24529 -0.00784 0.03100  0.00645  99  SER   D N     
4730 C  CA    . SER   D 100 ? 0.23169 0.28439 0.25282 -0.00611 0.03529  0.00863  99  SER   D CA    
4731 C  C     . SER   D 100 ? 0.22792 0.27900 0.23872 -0.00488 0.03779  0.00650  99  SER   D C     
4732 O  O     . SER   D 100 ? 0.22734 0.27671 0.23233 -0.00589 0.03584  0.00332  99  SER   D O     
4733 C  CB    . SER   D 100 ? 0.22712 0.27955 0.25125 -0.00624 0.03431  0.00842  99  SER   D CB    
4734 O  OG    . SER   D 100 ? 0.23828 0.29159 0.26181 -0.00420 0.03855  0.01045  99  SER   D OG    
4735 N  N     . MET   D 101 ? 0.23109 0.28240 0.23970 -0.00231 0.04191  0.00857  100 MET   D N     
4736 C  CA    . MET   D 101 ? 0.23461 0.28315 0.23299 -0.00062 0.04338  0.00643  100 MET   D CA    
4737 C  C     . MET   D 101 ? 0.23583 0.28194 0.22894 -0.00034 0.04268  0.00377  100 MET   D C     
4738 O  O     . MET   D 101 ? 0.25449 0.30118 0.25026 0.00044  0.04377  0.00488  100 MET   D O     
4739 C  CB    . MET   D 101 ? 0.27070 0.31931 0.26696 0.00314  0.04785  0.00957  100 MET   D CB    
4740 C  CG    . MET   D 101 ? 0.23887 0.28955 0.23893 0.00321  0.04886  0.01219  100 MET   D CG    
4741 S  SD    . MET   D 101 ? 0.28950 0.33826 0.28373 0.00122  0.04591  0.00862  100 MET   D SD    
4742 C  CE    . MET   D 101 ? 0.28642 0.33039 0.26771 0.00493  0.04773  0.00667  100 MET   D CE    
4743 N  N     . ALA   D 102 ? 0.23678 0.28016 0.22298 -0.00093 0.04081  0.00058  101 ALA   D N     
4744 C  CA    . ALA   D 102 ? 0.23888 0.27953 0.22017 -0.00036 0.04004  -0.00156 101 ALA   D CA    
4745 C  C     . ALA   D 102 ? 0.28272 0.32033 0.25737 0.00351  0.04249  -0.00105 101 ALA   D C     
4746 O  O     . ALA   D 102 ? 0.28827 0.32537 0.26041 0.00554  0.04431  0.00026  101 ALA   D O     
4747 C  CB    . ALA   D 102 ? 0.25338 0.29224 0.23120 -0.00231 0.03680  -0.00445 101 ALA   D CB    
4748 N  N     . ASN   D 103 ? 0.27463 0.30969 0.24564 0.00490  0.04229  -0.00220 102 ASN   D N     
4749 C  CA    . ASN   D 103 ? 0.32046 0.35137 0.28345 0.00942  0.04406  -0.00210 102 ASN   D CA    
4750 C  C     . ASN   D 103 ? 0.30901 0.33604 0.26747 0.00997  0.04178  -0.00464 102 ASN   D C     
4751 O  O     . ASN   D 103 ? 0.31956 0.34791 0.28198 0.00682  0.03954  -0.00590 102 ASN   D O     
4752 C  CB    . ASN   D 103 ? 0.30982 0.34303 0.27526 0.01288  0.04897  0.00203  102 ASN   D CB    
4753 C  CG    . ASN   D 103 ? 0.29615 0.33221 0.26806 0.01220  0.05015  0.00362  102 ASN   D CG    
4754 O  OD1   . ASN   D 103 ? 0.33755 0.37135 0.30660 0.01240  0.04886  0.00169  102 ASN   D OD1   
4755 N  ND2   . ASN   D 103 ? 0.32460 0.36556 0.30594 0.01150  0.05242  0.00746  102 ASN   D ND2   
4756 N  N     . ALA   D 104 ? 0.34585 0.36763 0.29551 0.01442  0.04219  -0.00530 103 ALA   D N     
4757 C  CA    . ALA   D 104 ? 0.38278 0.39972 0.32713 0.01582  0.03970  -0.00766 103 ALA   D CA    
4758 C  C     . ALA   D 104 ? 0.47413 0.48975 0.41481 0.02077  0.04339  -0.00583 103 ALA   D C     
4759 O  O     . ALA   D 104 ? 0.44442 0.45377 0.37624 0.02470  0.04201  -0.00753 103 ALA   D O     
4760 C  CB    . ALA   D 104 ? 0.39257 0.40263 0.32859 0.01718  0.03536  -0.01067 103 ALA   D CB    
4761 N  N     . GLY   D 105 ? 0.37698 0.39821 0.32464 0.02089  0.04788  -0.00210 104 GLY   D N     
4762 C  CA    . GLY   D 105 ? 0.40221 0.42341 0.34812 0.02576  0.05231  0.00085  104 GLY   D CA    
4763 C  C     . GLY   D 105 ? 0.33469 0.35872 0.28209 0.02917  0.05745  0.00541  104 GLY   D C     
4764 O  O     . GLY   D 105 ? 0.34094 0.36672 0.29058 0.02742  0.05717  0.00584  104 GLY   D O     
4765 N  N     . PRO   D 106 ? 0.39772 0.42247 0.34439 0.03428  0.06243  0.00932  105 PRO   D N     
4766 C  CA    . PRO   D 106 ? 0.33858 0.36701 0.28866 0.03774  0.06798  0.01491  105 PRO   D CA    
4767 C  C     . PRO   D 106 ? 0.34438 0.36920 0.28606 0.04061  0.06797  0.01415  105 PRO   D C     
4768 O  O     . PRO   D 106 ? 0.34748 0.36483 0.27627 0.04418  0.06565  0.01056  105 PRO   D O     
4769 C  CB    . PRO   D 106 ? 0.39119 0.41868 0.33755 0.04453  0.07307  0.01861  105 PRO   D CB    
4770 C  CG    . PRO   D 106 ? 0.41765 0.44500 0.36657 0.04156  0.07044  0.01615  105 PRO   D CG    
4771 C  CD    . PRO   D 106 ? 0.44501 0.46814 0.38938 0.03691  0.06352  0.00949  105 PRO   D CD    
4772 N  N     . ASN   D 107 ? 0.30638 0.33621 0.25561 0.03940  0.07039  0.01778  106 ASN   D N     
4773 C  CA    . ASN   D 107 ? 0.33723 0.36452 0.27941 0.04285  0.07163  0.01828  106 ASN   D CA    
4774 C  C     . ASN   D 107 ? 0.36214 0.38333 0.29533 0.04077  0.06561  0.01194  106 ASN   D C     
4775 O  O     . ASN   D 107 ? 0.37476 0.38962 0.29575 0.04609  0.06555  0.01063  106 ASN   D O     
4776 C  CB    . ASN   D 107 ? 0.36368 0.38786 0.29661 0.05221  0.07732  0.02204  106 ASN   D CB    
4777 C  CG    . ASN   D 107 ? 0.39396 0.42498 0.33757 0.05436  0.08373  0.02943  106 ASN   D CG    
4778 O  OD1   . ASN   D 107 ? 0.33584 0.37407 0.29353 0.05034  0.08507  0.03339  106 ASN   D OD1   
4779 N  ND2   . ASN   D 107 ? 0.38123 0.40992 0.31885 0.06077  0.08740  0.03158  106 ASN   D ND2   
4780 N  N     . THR   D 108 ? 0.32598 0.34912 0.26553 0.03358  0.06079  0.00863  107 THR   D N     
4781 C  CA    . THR   D 108 ? 0.36304 0.38134 0.29630 0.03127  0.05524  0.00355  107 THR   D CA    
4782 C  C     . THR   D 108 ? 0.33867 0.36176 0.28079 0.02491  0.05311  0.00310  107 THR   D C     
4783 O  O     . THR   D 108 ? 0.33014 0.35187 0.27237 0.02075  0.04830  -0.00057 107 THR   D O     
4784 C  CB    . THR   D 108 ? 0.38992 0.40357 0.31896 0.02997  0.05051  -0.00077 107 THR   D CB    
4785 O  OG1   . THR   D 108 ? 0.37509 0.39382 0.31399 0.02529  0.05013  -0.00038 107 THR   D OG1   
4786 C  CG2   . THR   D 108 ? 0.39157 0.39870 0.30949 0.03691  0.05158  -0.00111 107 THR   D CG2   
4787 N  N     . ASN   D 109 ? 0.32522 0.35376 0.27491 0.02448  0.05659  0.00715  108 ASN   D N     
4788 C  CA    . ASN   D 109 ? 0.30235 0.33471 0.25944 0.01912  0.05434  0.00668  108 ASN   D CA    
4789 C  C     . ASN   D 109 ? 0.31389 0.34240 0.26355 0.01951  0.05211  0.00413  108 ASN   D C     
4790 O  O     . ASN   D 109 ? 0.35516 0.38058 0.29747 0.02453  0.05453  0.00530  108 ASN   D O     
4791 C  CB    . ASN   D 109 ? 0.30987 0.34840 0.27743 0.01863  0.05783  0.01173  108 ASN   D CB    
4792 C  CG    . ASN   D 109 ? 0.29361 0.33587 0.26964 0.01835  0.05976  0.01476  108 ASN   D CG    
4793 O  OD1   . ASN   D 109 ? 0.29432 0.33842 0.27650 0.01400  0.05670  0.01316  108 ASN   D OD1   
4794 N  ND2   . ASN   D 109 ? 0.29734 0.34062 0.27372 0.02329  0.06486  0.01935  108 ASN   D ND2   
4795 N  N     . GLY   D 110 ? 0.26571 0.29433 0.21720 0.01474  0.04775  0.00102  109 GLY   D N     
4796 C  CA    . GLY   D 110 ? 0.33444 0.36011 0.28067 0.01454  0.04549  -0.00098 109 GLY   D CA    
4797 C  C     . GLY   D 110 ? 0.30366 0.33409 0.25771 0.00995  0.04446  -0.00051 109 GLY   D C     
4798 O  O     . GLY   D 110 ? 0.29079 0.32492 0.24977 0.01034  0.04735  0.00268  109 GLY   D O     
4799 N  N     . SER   D 111 ? 0.27194 0.30223 0.22739 0.00604  0.04047  -0.00324 110 SER   D N     
4800 C  CA    . SER   D 111 ? 0.27180 0.30628 0.23405 0.00222  0.03942  -0.00284 110 SER   D CA    
4801 C  C     . SER   D 111 ? 0.26811 0.30509 0.23608 -0.00103 0.03746  -0.00360 110 SER   D C     
4802 O  O     . SER   D 111 ? 0.24293 0.28313 0.21649 -0.00336 0.03674  -0.00295 110 SER   D O     
4803 C  CB    . SER   D 111 ? 0.30216 0.33473 0.26096 0.00097  0.03685  -0.00474 110 SER   D CB    
4804 O  OG    . SER   D 111 ? 0.28894 0.31786 0.24394 0.00048  0.03365  -0.00726 110 SER   D OG    
4805 N  N     . GLN   D 112 ? 0.24397 0.27907 0.21019 -0.00098 0.03627  -0.00502 111 GLN   D N     
4806 C  CA    . GLN   D 112 ? 0.23899 0.27634 0.21014 -0.00359 0.03464  -0.00556 111 GLN   D CA    
4807 C  C     . GLN   D 112 ? 0.24180 0.28258 0.21948 -0.00385 0.03625  -0.00350 111 GLN   D C     
4808 O  O     . GLN   D 112 ? 0.23796 0.27929 0.21683 -0.00182 0.03894  -0.00145 111 GLN   D O     
4809 C  CB    . GLN   D 112 ? 0.24477 0.27961 0.21343 -0.00342 0.03313  -0.00712 111 GLN   D CB    
4810 C  CG    . GLN   D 112 ? 0.26214 0.29387 0.22713 -0.00408 0.03012  -0.00887 111 GLN   D CG    
4811 C  CD    . GLN   D 112 ? 0.29119 0.32112 0.25617 -0.00460 0.02797  -0.00992 111 GLN   D CD    
4812 O  OE1   . GLN   D 112 ? 0.25697 0.28946 0.22609 -0.00585 0.02818  -0.00949 111 GLN   D OE1   
4813 N  NE2   . GLN   D 112 ? 0.30473 0.32988 0.26516 -0.00346 0.02554  -0.01124 111 GLN   D NE2   
4814 N  N     . PHE   D 113 ? 0.23163 0.27440 0.21361 -0.00605 0.03433  -0.00386 112 PHE   D N     
4815 C  CA    . PHE   D 113 ? 0.23411 0.27931 0.22277 -0.00654 0.03437  -0.00222 112 PHE   D CA    
4816 C  C     . PHE   D 113 ? 0.22680 0.27207 0.21675 -0.00779 0.03191  -0.00366 112 PHE   D C     
4817 O  O     . PHE   D 113 ? 0.22658 0.27087 0.21308 -0.00833 0.03068  -0.00527 112 PHE   D O     
4818 C  CB    . PHE   D 113 ? 0.22822 0.27500 0.22045 -0.00720 0.03385  -0.00094 112 PHE   D CB    
4819 C  CG    . PHE   D 113 ? 0.23256 0.27885 0.22241 -0.00856 0.03135  -0.00279 112 PHE   D CG    
4820 C  CD1   . PHE   D 113 ? 0.25644 0.30165 0.24140 -0.00853 0.03164  -0.00366 112 PHE   D CD1   
4821 C  CD2   . PHE   D 113 ? 0.24398 0.29045 0.23591 -0.00936 0.02861  -0.00361 112 PHE   D CD2   
4822 C  CE1   . PHE   D 113 ? 0.24582 0.29092 0.22915 -0.00958 0.02966  -0.00486 112 PHE   D CE1   
4823 C  CE2   . PHE   D 113 ? 0.24945 0.29545 0.23863 -0.00979 0.02683  -0.00488 112 PHE   D CE2   
4824 C  CZ    . PHE   D 113 ? 0.28686 0.33254 0.27215 -0.01006 0.02755  -0.00532 112 PHE   D CZ    
4825 N  N     . PHE   D 114 ? 0.22543 0.27178 0.22081 -0.00802 0.03103  -0.00273 113 PHE   D N     
4826 C  CA    . PHE   D 114 ? 0.22420 0.27001 0.22001 -0.00852 0.02840  -0.00411 113 PHE   D CA    
4827 C  C     . PHE   D 114 ? 0.22362 0.26965 0.22488 -0.00873 0.02585  -0.00333 113 PHE   D C     
4828 O  O     . PHE   D 114 ? 0.22361 0.27079 0.23046 -0.00881 0.02638  -0.00114 113 PHE   D O     
4829 C  CB    . PHE   D 114 ? 0.23040 0.27569 0.22558 -0.00813 0.02901  -0.00467 113 PHE   D CB    
4830 C  CG    . PHE   D 114 ? 0.22486 0.27095 0.22476 -0.00760 0.03036  -0.00293 113 PHE   D CG    
4831 C  CD1   . PHE   D 114 ? 0.26179 0.30831 0.26129 -0.00649 0.03350  -0.00134 113 PHE   D CD1   
4832 C  CD2   . PHE   D 114 ? 0.24118 0.28732 0.24582 -0.00774 0.02845  -0.00263 113 PHE   D CD2   
4833 C  CE1   . PHE   D 114 ? 0.22723 0.27493 0.23158 -0.00554 0.03529  0.00102  113 PHE   D CE1   
4834 C  CE2   . PHE   D 114 ? 0.22433 0.27151 0.23457 -0.00734 0.02962  -0.00052 113 PHE   D CE2   
4835 C  CZ    . PHE   D 114 ? 0.22668 0.27500 0.23717 -0.00624 0.03334  0.00158  113 PHE   D CZ    
4836 N  N     . ILE   D 115 ? 0.22385 0.26846 0.22343 -0.00844 0.02288  -0.00486 114 ILE   D N     
4837 C  CA    . ILE   D 115 ? 0.22483 0.26801 0.22817 -0.00807 0.01901  -0.00485 114 ILE   D CA    
4838 C  C     . ILE   D 115 ? 0.23259 0.27419 0.23569 -0.00713 0.01738  -0.00585 114 ILE   D C     
4839 O  O     . ILE   D 115 ? 0.24482 0.28574 0.24248 -0.00619 0.01782  -0.00721 114 ILE   D O     
4840 C  CB    . ILE   D 115 ? 0.22600 0.26769 0.22545 -0.00737 0.01664  -0.00610 114 ILE   D CB    
4841 C  CG1   . ILE   D 115 ? 0.22804 0.27132 0.22690 -0.00835 0.01847  -0.00534 114 ILE   D CG1   
4842 C  CG2   . ILE   D 115 ? 0.26368 0.30253 0.26628 -0.00644 0.01155  -0.00646 114 ILE   D CG2   
4843 C  CD1   . ILE   D 115 ? 0.26603 0.30816 0.25966 -0.00753 0.01701  -0.00661 114 ILE   D CD1   
4844 N  N     . CYS   D 116 ? 0.23341 0.27461 0.24287 -0.00730 0.01567  -0.00479 115 CYS   D N     
4845 C  CA    . CYS   D 116 ? 0.26067 0.29998 0.26995 -0.00632 0.01377  -0.00583 115 CYS   D CA    
4846 C  C     . CYS   D 116 ? 0.27127 0.30667 0.27671 -0.00429 0.00912  -0.00782 115 CYS   D C     
4847 O  O     . CYS   D 116 ? 0.28989 0.32346 0.29677 -0.00395 0.00572  -0.00790 115 CYS   D O     
4848 C  CB    . CYS   D 116 ? 0.24727 0.28697 0.26531 -0.00701 0.01265  -0.00388 115 CYS   D CB    
4849 S  SG    . CYS   D 116 ? 0.30760 0.35146 0.32955 -0.00808 0.01847  -0.00097 115 CYS   D SG    
4850 N  N     . THR   D 117 ? 0.25623 0.28998 0.25652 -0.00249 0.00885  -0.00930 116 THR   D N     
4851 C  CA    . THR   D 117 ? 0.28096 0.31010 0.27651 0.00064  0.00440  -0.01110 116 THR   D CA    
4852 C  C     . THR   D 117 ? 0.31243 0.33864 0.31069 0.00162  0.00104  -0.01169 116 THR   D C     
4853 O  O     . THR   D 117 ? 0.35015 0.37159 0.34346 0.00495  -0.00293 -0.01343 116 THR   D O     
4854 C  CB    . THR   D 117 ? 0.32203 0.35111 0.30886 0.00302  0.00662  -0.01184 116 THR   D CB    
4855 O  OG1   . THR   D 117 ? 0.29796 0.32922 0.28417 0.00259  0.01007  -0.01140 116 THR   D OG1   
4856 C  CG2   . THR   D 117 ? 0.37674 0.40837 0.36150 0.00205  0.00925  -0.01113 116 THR   D CG2   
4857 N  N     . ALA   D 118 ? 0.28564 0.31427 0.29145 -0.00078 0.00242  -0.01016 117 ALA   D N     
4858 C  CA    . ALA   D 118 ? 0.26881 0.29538 0.27888 -0.00043 -0.00037 -0.01024 117 ALA   D CA    
4859 C  C     . ALA   D 118 ? 0.27505 0.30537 0.29526 -0.00334 0.00178  -0.00737 117 ALA   D C     
4860 O  O     . ALA   D 118 ? 0.30360 0.33783 0.32546 -0.00501 0.00601  -0.00565 117 ALA   D O     
4861 C  CB    . ALA   D 118 ? 0.28724 0.31356 0.29140 0.00110  0.00174  -0.01145 117 ALA   D CB    
4862 N  N     . LYS   D 119 ? 0.28658 0.31557 0.31333 -0.00351 -0.00097 -0.00662 118 LYS   D N     
4863 C  CA    . LYS   D 119 ? 0.28515 0.31820 0.32148 -0.00564 0.00203  -0.00322 118 LYS   D CA    
4864 C  C     . LYS   D 119 ? 0.28321 0.31972 0.31529 -0.00602 0.00841  -0.00310 118 LYS   D C     
4865 O  O     . LYS   D 119 ? 0.32781 0.36302 0.35411 -0.00499 0.00877  -0.00516 118 LYS   D O     
4866 C  CB    . LYS   D 119 ? 0.28513 0.31586 0.33020 -0.00568 -0.00272 -0.00216 118 LYS   D CB    
4867 C  CG    . LYS   D 119 ? 0.35320 0.38828 0.40986 -0.00743 0.00021  0.00232  118 LYS   D CG    
4868 C  CD    . LYS   D 119 ? 0.45508 0.48751 0.52253 -0.00766 -0.00584 0.00387  118 LYS   D CD    
4869 C  CE    . LYS   D 119 ? 0.48701 0.51980 0.55480 -0.00740 -0.00431 0.00372  118 LYS   D CE    
4870 N  NZ    . LYS   D 119 ? 0.60325 0.64087 0.68295 -0.00867 -0.00072 0.00891  118 LYS   D NZ    
4871 N  N     . THR   D 120 ? 0.31526 0.35577 0.35002 -0.00710 0.01323  -0.00059 119 THR   D N     
4872 C  CA    . THR   D 120 ? 0.28887 0.33171 0.31921 -0.00703 0.01861  -0.00057 119 THR   D CA    
4873 C  C     . THR   D 120 ? 0.29140 0.33728 0.32941 -0.00724 0.02191  0.00327  119 THR   D C     
4874 O  O     . THR   D 120 ? 0.30156 0.34977 0.33869 -0.00690 0.02614  0.00509  119 THR   D O     
4875 C  CB    . THR   D 120 ? 0.29335 0.33704 0.31604 -0.00701 0.02154  -0.00170 119 THR   D CB    
4876 O  OG1   . THR   D 120 ? 0.28621 0.33154 0.31245 -0.00747 0.02250  0.00046  119 THR   D OG1   
4877 C  CG2   . THR   D 120 ? 0.28738 0.32867 0.30327 -0.00639 0.01902  -0.00461 119 THR   D CG2   
4878 N  N     . GLU   D 121 ? 0.31529 0.36091 0.36041 -0.00732 0.02003  0.00464  120 GLU   D N     
4879 C  CA    . GLU   D 121 ? 0.32468 0.37341 0.37967 -0.00727 0.02255  0.00937  120 GLU   D CA    
4880 C  C     . GLU   D 121 ? 0.26200 0.31298 0.31283 -0.00597 0.02876  0.01047  120 GLU   D C     
4881 O  O     . GLU   D 121 ? 0.27468 0.32861 0.33078 -0.00494 0.03259  0.01475  120 GLU   D O     
4882 C  CB    . GLU   D 121 ? 0.36740 0.41497 0.43171 -0.00774 0.01837  0.01063  120 GLU   D CB    
4883 C  CG    . GLU   D 121 ? 0.48485 0.53061 0.54471 -0.00731 0.01789  0.00797  120 GLU   D CG    
4884 C  CD    . GLU   D 121 ? 0.55577 0.59730 0.60603 -0.00692 0.01408  0.00285  120 GLU   D CD    
4885 O  OE1   . GLU   D 121 ? 0.44587 0.48526 0.49275 -0.00678 0.01107  0.00108  120 GLU   D OE1   
4886 O  OE2   . GLU   D 121 ? 0.63128 0.67165 0.67724 -0.00636 0.01437  0.00087  120 GLU   D OE2   
4887 N  N     . TRP   D 122 ? 0.28917 0.33856 0.33080 -0.00560 0.02969  0.00700  121 TRP   D N     
4888 C  CA    . TRP   D 122 ? 0.32124 0.37159 0.35804 -0.00406 0.03459  0.00752  121 TRP   D CA    
4889 C  C     . TRP   D 122 ? 0.31304 0.36402 0.34449 -0.00282 0.03808  0.00818  121 TRP   D C     
4890 O  O     . TRP   D 122 ? 0.33967 0.39074 0.36682 -0.00071 0.04198  0.00902  121 TRP   D O     
4891 C  CB    . TRP   D 122 ? 0.31707 0.36518 0.34602 -0.00418 0.03383  0.00363  121 TRP   D CB    
4892 C  CG    . TRP   D 122 ? 0.34165 0.38802 0.36267 -0.00482 0.03234  0.00026  121 TRP   D CG    
4893 C  CD1   . TRP   D 122 ? 0.33754 0.38328 0.35111 -0.00427 0.03438  -0.00099 121 TRP   D CD1   
4894 C  CD2   . TRP   D 122 ? 0.32396 0.36877 0.34395 -0.00571 0.02839  -0.00188 121 TRP   D CD2   
4895 N  NE1   . TRP   D 122 ? 0.32724 0.37184 0.33671 -0.00518 0.03213  -0.00332 121 TRP   D NE1   
4896 C  CE2   . TRP   D 122 ? 0.37451 0.41861 0.38720 -0.00577 0.02884  -0.00386 121 TRP   D CE2   
4897 C  CE3   . TRP   D 122 ? 0.34522 0.38862 0.36940 -0.00599 0.02422  -0.00226 121 TRP   D CE3   
4898 C  CZ2   . TRP   D 122 ? 0.38950 0.43225 0.39916 -0.00590 0.02612  -0.00567 121 TRP   D CZ2   
4899 C  CZ3   . TRP   D 122 ? 0.44161 0.48280 0.46128 -0.00571 0.02112  -0.00464 121 TRP   D CZ3   
4900 C  CH2   . TRP   D 122 ? 0.40612 0.44737 0.41865 -0.00557 0.02253  -0.00608 121 TRP   D CH2   
4901 N  N     . LEU   D 123 ? 0.28777 0.33859 0.31851 -0.00375 0.03649  0.00757  122 LEU   D N     
4902 C  CA    . LEU   D 123 ? 0.24462 0.29599 0.27126 -0.00252 0.03950  0.00854  122 LEU   D CA    
4903 C  C     . LEU   D 123 ? 0.25990 0.31424 0.29473 -0.00124 0.04226  0.01378  122 LEU   D C     
4904 O  O     . LEU   D 123 ? 0.25329 0.30813 0.28449 0.00076  0.04575  0.01531  122 LEU   D O     
4905 C  CB    . LEU   D 123 ? 0.25107 0.30114 0.27349 -0.00402 0.03676  0.00577  122 LEU   D CB    
4906 C  CG    . LEU   D 123 ? 0.27805 0.32578 0.29341 -0.00487 0.03457  0.00164  122 LEU   D CG    
4907 C  CD1   . LEU   D 123 ? 0.27843 0.32534 0.29036 -0.00587 0.03245  -0.00020 122 LEU   D CD1   
4908 C  CD2   . LEU   D 123 ? 0.30441 0.35090 0.31274 -0.00347 0.03724  0.00058  122 LEU   D CD2   
4909 N  N     . ASP   D 124 ? 0.26858 0.32474 0.31463 -0.00207 0.04069  0.01685  123 ASP   D N     
4910 C  CA    . ASP   D 124 ? 0.25985 0.31951 0.31621 -0.00087 0.04337  0.02298  123 ASP   D CA    
4911 C  C     . ASP   D 124 ? 0.27392 0.33500 0.32679 0.00296  0.04993  0.02610  123 ASP   D C     
4912 O  O     . ASP   D 124 ? 0.26317 0.32317 0.31155 0.00427  0.05148  0.02493  123 ASP   D O     
4913 C  CB    . ASP   D 124 ? 0.25633 0.31734 0.32614 -0.00231 0.04022  0.02598  123 ASP   D CB    
4914 C  CG    . ASP   D 124 ? 0.31061 0.36949 0.38453 -0.00514 0.03325  0.02368  123 ASP   D CG    
4915 O  OD1   . ASP   D 124 ? 0.25401 0.31135 0.32157 -0.00582 0.03178  0.02079  123 ASP   D OD1   
4916 O  OD2   . ASP   D 124 ? 0.32907 0.38724 0.41193 -0.00638 0.02891  0.02456  123 ASP   D OD2   
4917 N  N     . GLY   D 125 ? 0.25792 0.32116 0.31261 0.00518  0.05374  0.03023  124 GLY   D N     
4918 C  CA    . GLY   D 125 ? 0.28794 0.35202 0.33821 0.01002  0.06026  0.03368  124 GLY   D CA    
4919 C  C     . GLY   D 125 ? 0.33391 0.39373 0.36795 0.01221  0.06154  0.02894  124 GLY   D C     
4920 O  O     . GLY   D 125 ? 0.34844 0.40746 0.37622 0.01702  0.06638  0.03096  124 GLY   D O     
4921 N  N     . LYS   D 126 ? 0.29628 0.35301 0.32339 0.00924  0.05715  0.02295  125 LYS   D N     
4922 C  CA    . LYS   D 126 ? 0.28541 0.33786 0.29865 0.01087  0.05734  0.01868  125 LYS   D CA    
4923 C  C     . LYS   D 126 ? 0.33318 0.38449 0.34230 0.00955  0.05555  0.01653  125 LYS   D C     
4924 O  O     . LYS   D 126 ? 0.32024 0.36858 0.31967 0.01222  0.05697  0.01520  125 LYS   D O     
4925 C  CB    . LYS   D 126 ? 0.31269 0.36230 0.32087 0.00895  0.05405  0.01379  125 LYS   D CB    
4926 C  CG    . LYS   D 126 ? 0.36801 0.41776 0.37736 0.01088  0.05606  0.01518  125 LYS   D CG    
4927 C  CD    . LYS   D 126 ? 0.47249 0.51973 0.47789 0.00860  0.05251  0.01051  125 LYS   D CD    
4928 C  CE    . LYS   D 126 ? 0.46883 0.51688 0.47775 0.00956  0.05381  0.01195  125 LYS   D CE    
4929 N  NZ    . LYS   D 126 ? 0.64733 0.69474 0.65226 0.01473  0.05875  0.01498  125 LYS   D NZ    
4930 N  N     . HIS   D 127 ? 0.25564 0.30882 0.27173 0.00590  0.05227  0.01628  126 HIS   D N     
4931 C  CA    . HIS   D 127 ? 0.25756 0.31013 0.27107 0.00446  0.05048  0.01463  126 HIS   D CA    
4932 C  C     . HIS   D 127 ? 0.25907 0.31524 0.28299 0.00395  0.05107  0.01912  126 HIS   D C     
4933 O  O     . HIS   D 127 ? 0.24293 0.30136 0.27731 0.00241  0.04953  0.02148  126 HIS   D O     
4934 C  CB    . HIS   D 127 ? 0.24364 0.29460 0.25525 0.00082  0.04546  0.00997  126 HIS   D CB    
4935 C  CG    . HIS   D 127 ? 0.23509 0.28298 0.23835 0.00104  0.04465  0.00624  126 HIS   D CG    
4936 N  ND1   . HIS   D 127 ? 0.24548 0.29051 0.24009 0.00132  0.04389  0.00337  126 HIS   D ND1   
4937 C  CD2   . HIS   D 127 ? 0.25897 0.30610 0.26182 0.00117  0.04441  0.00529  126 HIS   D CD2   
4938 C  CE1   . HIS   D 127 ? 0.29101 0.33362 0.28079 0.00152  0.04294  0.00095  126 HIS   D CE1   
4939 N  NE2   . HIS   D 127 ? 0.26285 0.30674 0.25712 0.00147  0.04341  0.00197  126 HIS   D NE2   
4940 N  N     . VAL   D 128 ? 0.23993 0.29635 0.26141 0.00533  0.05297  0.02043  127 VAL   D N     
4941 C  CA    . VAL   D 128 ? 0.23610 0.29608 0.26783 0.00507  0.05378  0.02523  127 VAL   D CA    
4942 C  C     . VAL   D 128 ? 0.23162 0.29137 0.26747 0.00087  0.04811  0.02269  127 VAL   D C     
4943 O  O     . VAL   D 128 ? 0.23127 0.28895 0.25991 -0.00020 0.04629  0.01901  127 VAL   D O     
4944 C  CB    . VAL   D 128 ? 0.24038 0.30048 0.26712 0.00859  0.05815  0.02762  127 VAL   D CB    
4945 C  CG1   . VAL   D 128 ? 0.23875 0.30277 0.27681 0.00799  0.05872  0.03274  127 VAL   D CG1   
4946 C  CG2   . VAL   D 128 ? 0.26318 0.32255 0.28421 0.01389  0.06366  0.03009  127 VAL   D CG2   
4947 N  N     . VAL   D 129 ? 0.22956 0.29115 0.27723 -0.00111 0.04517  0.02499  128 VAL   D N     
4948 C  CA    . VAL   D 129 ? 0.23516 0.29607 0.28778 -0.00416 0.03952  0.02351  128 VAL   D CA    
4949 C  C     . VAL   D 129 ? 0.22636 0.28949 0.28448 -0.00392 0.04057  0.02720  128 VAL   D C     
4950 O  O     . VAL   D 129 ? 0.23075 0.29732 0.29753 -0.00218 0.04419  0.03326  128 VAL   D O     
4951 C  CB    . VAL   D 129 ? 0.22468 0.28573 0.28807 -0.00583 0.03524  0.02475  128 VAL   D CB    
4952 C  CG1   . VAL   D 129 ? 0.23567 0.29509 0.30453 -0.00821 0.02864  0.02363  128 VAL   D CG1   
4953 C  CG2   . VAL   D 129 ? 0.22453 0.28321 0.28189 -0.00607 0.03399  0.02081  128 VAL   D CG2   
4954 N  N     . PHE   D 130 ? 0.22551 0.28696 0.27910 -0.00538 0.03775  0.02410  129 PHE   D N     
4955 C  CA    . PHE   D 130 ? 0.23198 0.29549 0.29022 -0.00508 0.03895  0.02751  129 PHE   D CA    
4956 C  C     . PHE   D 130 ? 0.24623 0.30813 0.30696 -0.00769 0.03300  0.02535  129 PHE   D C     
4957 O  O     . PHE   D 130 ? 0.23838 0.30174 0.30280 -0.00776 0.03339  0.02777  129 PHE   D O     
4958 C  CB    . PHE   D 130 ? 0.22843 0.29167 0.27579 -0.00259 0.04403  0.02689  129 PHE   D CB    
4959 C  CG    . PHE   D 130 ? 0.23492 0.29458 0.26983 -0.00367 0.04186  0.02055  129 PHE   D CG    
4960 C  CD1   . PHE   D 130 ? 0.22881 0.28608 0.25527 -0.00329 0.04202  0.01685  129 PHE   D CD1   
4961 C  CD2   . PHE   D 130 ? 0.22695 0.28577 0.25964 -0.00517 0.03936  0.01863  129 PHE   D CD2   
4962 C  CE1   . PHE   D 130 ? 0.22851 0.28297 0.24554 -0.00432 0.03998  0.01196  129 PHE   D CE1   
4963 C  CE2   . PHE   D 130 ? 0.26366 0.31966 0.28628 -0.00606 0.03754  0.01360  129 PHE   D CE2   
4964 C  CZ    . PHE   D 130 ? 0.25324 0.30717 0.26835 -0.00567 0.03786  0.01043  129 PHE   D CZ    
4965 N  N     . GLY   D 131 ? 0.24639 0.30512 0.30517 -0.00939 0.02748  0.02114  130 GLY   D N     
4966 C  CA    . GLY   D 131 ? 0.26697 0.32334 0.32603 -0.01094 0.02188  0.01884  130 GLY   D CA    
4967 C  C     . GLY   D 131 ? 0.23575 0.28823 0.29349 -0.01165 0.01591  0.01512  130 GLY   D C     
4968 O  O     . GLY   D 131 ? 0.23368 0.28569 0.29126 -0.01131 0.01617  0.01454  130 GLY   D O     
4969 N  N     . LYS   D 132 ? 0.23153 0.28089 0.28809 -0.01223 0.01041  0.01273  131 LYS   D N     
4970 C  CA    . LYS   D 132 ? 0.22694 0.27158 0.27956 -0.01183 0.00465  0.00879  131 LYS   D CA    
4971 C  C     . LYS   D 132 ? 0.24657 0.28789 0.29194 -0.01135 0.00101  0.00543  131 LYS   D C     
4972 O  O     . LYS   D 132 ? 0.24920 0.29137 0.29695 -0.01195 0.00063  0.00670  131 LYS   D O     
4973 C  CB    . LYS   D 132 ? 0.24065 0.28329 0.30474 -0.01222 -0.00125 0.01071  131 LYS   D CB    
4974 C  CG    . LYS   D 132 ? 0.28515 0.32743 0.35926 -0.01315 -0.00556 0.01347  131 LYS   D CG    
4975 C  CD    . LYS   D 132 ? 0.36432 0.40280 0.44880 -0.01340 -0.01356 0.01440  131 LYS   D CD    
4976 C  CE    . LYS   D 132 ? 0.44302 0.48183 0.54108 -0.01468 -0.01790 0.01851  131 LYS   D CE    
4977 N  NZ    . LYS   D 132 ? 0.56676 0.60077 0.67486 -0.01484 -0.02691 0.01903  131 LYS   D NZ    
4978 N  N     . VAL   D 133 ? 0.23187 0.26944 0.26822 -0.00989 -0.00141 0.00140  132 VAL   D N     
4979 C  CA    . VAL   D 133 ? 0.26266 0.29646 0.29170 -0.00852 -0.00520 -0.00159 132 VAL   D CA    
4980 C  C     . VAL   D 133 ? 0.24732 0.27742 0.28375 -0.00843 -0.01258 -0.00095 132 VAL   D C     
4981 O  O     . VAL   D 133 ? 0.31096 0.33822 0.35352 -0.00814 -0.01742 -0.00056 132 VAL   D O     
4982 C  CB    . VAL   D 133 ? 0.24744 0.27778 0.26616 -0.00607 -0.00634 -0.00518 132 VAL   D CB    
4983 C  CG1   . VAL   D 133 ? 0.27706 0.30309 0.28824 -0.00373 -0.01035 -0.00774 132 VAL   D CG1   
4984 C  CG2   . VAL   D 133 ? 0.27600 0.30989 0.28824 -0.00635 0.00039  -0.00558 132 VAL   D CG2   
4985 N  N     . LYS   D 134 ? 0.28177 0.31130 0.31738 -0.00856 -0.01410 -0.00106 133 LYS   D N     
4986 C  CA    . LYS   D 134 ? 0.29207 0.31723 0.33365 -0.00825 -0.02194 -0.00088 133 LYS   D CA    
4987 C  C     . LYS   D 134 ? 0.33824 0.35665 0.36865 -0.00493 -0.02738 -0.00529 133 LYS   D C     
4988 O  O     . LYS   D 134 ? 0.40862 0.42064 0.44025 -0.00307 -0.03526 -0.00676 133 LYS   D O     
4989 C  CB    . LYS   D 134 ? 0.37238 0.40133 0.42102 -0.01035 -0.02012 0.00233  133 LYS   D CB    
4990 C  CG    . LYS   D 134 ? 0.46936 0.49456 0.52589 -0.01054 -0.02791 0.00323  133 LYS   D CG    
4991 C  CD    . LYS   D 134 ? 0.50373 0.53348 0.56589 -0.01247 -0.02466 0.00650  133 LYS   D CD    
4992 C  CE    . LYS   D 134 ? 0.47841 0.50441 0.54949 -0.01285 -0.03289 0.00768  133 LYS   D CE    
4993 N  NZ    . LYS   D 134 ? 0.55977 0.58977 0.63453 -0.01435 -0.02984 0.01036  133 LYS   D NZ    
4994 N  N     . GLU   D 135 ? 0.36366 0.38298 0.38325 -0.00377 -0.02359 -0.00721 134 GLU   D N     
4995 C  CA    . GLU   D 135 ? 0.37275 0.38620 0.38037 0.00028  -0.02728 -0.01089 134 GLU   D CA    
4996 C  C     . GLU   D 135 ? 0.35675 0.37272 0.35394 0.00167  -0.02082 -0.01208 134 GLU   D C     
4997 O  O     . GLU   D 135 ? 0.29728 0.31922 0.29541 -0.00079 -0.01400 -0.01053 134 GLU   D O     
4998 C  CB    . GLU   D 135 ? 0.41942 0.43067 0.42457 0.00104  -0.03030 -0.01159 134 GLU   D CB    
4999 C  CG    . GLU   D 135 ? 0.49047 0.50083 0.50777 -0.00121 -0.03563 -0.00946 134 GLU   D CG    
5000 C  CD    . GLU   D 135 ? 0.64195 0.64461 0.66338 0.00069  -0.04561 -0.01058 134 GLU   D CD    
5001 O  OE1   . GLU   D 135 ? 0.63053 0.62702 0.64217 0.00483  -0.04919 -0.01391 134 GLU   D OE1   
5002 O  OE2   . GLU   D 135 ? 0.70351 0.70613 0.73837 -0.00175 -0.05004 -0.00784 134 GLU   D OE2   
5003 N  N     . GLY   D 136 ? 0.35859 0.36959 0.34575 0.00605  -0.02326 -0.01465 135 GLY   D N     
5004 C  CA    . GLY   D 136 ? 0.37172 0.38515 0.34994 0.00774  -0.01744 -0.01507 135 GLY   D CA    
5005 C  C     . GLY   D 136 ? 0.29439 0.30927 0.27269 0.00773  -0.01469 -0.01486 135 GLY   D C     
5006 O  O     . GLY   D 136 ? 0.31916 0.33738 0.29281 0.00805  -0.00919 -0.01439 135 GLY   D O     
5007 N  N     . MET   D 137 ? 0.31365 0.32590 0.29739 0.00748  -0.01869 -0.01507 136 MET   D N     
5008 C  CA    . MET   D 137 ? 0.29047 0.30375 0.27347 0.00783  -0.01621 -0.01507 136 MET   D CA    
5009 C  C     . MET   D 137 ? 0.29583 0.30626 0.26699 0.01278  -0.01536 -0.01661 136 MET   D C     
5010 O  O     . MET   D 137 ? 0.31711 0.33063 0.28628 0.01275  -0.01060 -0.01595 136 MET   D O     
5011 C  CB    . MET   D 137 ? 0.27778 0.28790 0.26830 0.00727  -0.02144 -0.01509 136 MET   D CB    
5012 C  CG    . MET   D 137 ? 0.35175 0.36389 0.34333 0.00673  -0.01836 -0.01471 136 MET   D CG    
5013 S  SD    . MET   D 137 ? 0.34905 0.37015 0.34738 0.00173  -0.00984 -0.01179 136 MET   D SD    
5014 C  CE    . MET   D 137 ? 0.36759 0.38983 0.36167 0.00275  -0.00612 -0.01233 136 MET   D CE    
5015 N  N     . ASN   D 138 ? 0.32906 0.33373 0.29210 0.01744  -0.01959 -0.01832 137 ASN   D N     
5016 C  CA    . ASN   D 138 ? 0.35221 0.35492 0.30386 0.02285  -0.01749 -0.01887 137 ASN   D CA    
5017 C  C     . ASN   D 138 ? 0.30174 0.31109 0.25134 0.02173  -0.00973 -0.01672 137 ASN   D C     
5018 O  O     . ASN   D 138 ? 0.30123 0.31142 0.24511 0.02483  -0.00621 -0.01584 137 ASN   D O     
5019 C  CB    . ASN   D 138 ? 0.37989 0.37433 0.32151 0.02936  -0.02340 -0.02101 137 ASN   D CB    
5020 C  CG    . ASN   D 138 ? 0.40152 0.39477 0.34419 0.02848  -0.02630 -0.02141 137 ASN   D CG    
5021 O  OD1   . ASN   D 138 ? 0.44701 0.44638 0.39589 0.02366  -0.02245 -0.01977 137 ASN   D OD1   
5022 N  ND2   . ASN   D 138 ? 0.51390 0.49848 0.44950 0.03373  -0.03353 -0.02377 137 ASN   D ND2   
5023 N  N     . ILE   D 139 ? 0.26225 0.27615 0.21685 0.01753  -0.00723 -0.01559 138 ILE   D N     
5024 C  CA    . ILE   D 139 ? 0.27592 0.29594 0.23034 0.01572  -0.00058 -0.01351 138 ILE   D CA    
5025 C  C     . ILE   D 139 ? 0.30450 0.32881 0.26382 0.01263  0.00343  -0.01235 138 ILE   D C     
5026 O  O     . ILE   D 139 ? 0.28622 0.31322 0.24316 0.01356  0.00756  -0.01087 138 ILE   D O     
5027 C  CB    . ILE   D 139 ? 0.28942 0.31246 0.24790 0.01204  0.00044  -0.01290 138 ILE   D CB    
5028 C  CG1   . ILE   D 139 ? 0.34357 0.36222 0.29789 0.01475  -0.00400 -0.01415 138 ILE   D CG1   
5029 C  CG2   . ILE   D 139 ? 0.30750 0.33609 0.26602 0.01021  0.00644  -0.01088 138 ILE   D CG2   
5030 C  CD1   . ILE   D 139 ? 0.33137 0.34702 0.27502 0.02095  -0.00377 -0.01420 138 ILE   D CD1   
5031 N  N     . VAL   D 140 ? 0.26632 0.29119 0.23289 0.00921  0.00213  -0.01269 139 VAL   D N     
5032 C  CA    . VAL   D 140 ? 0.30111 0.32930 0.27153 0.00684  0.00553  -0.01181 139 VAL   D CA    
5033 C  C     . VAL   D 140 ? 0.29571 0.32176 0.26147 0.01037  0.00540  -0.01217 139 VAL   D C     
5034 O  O     . VAL   D 140 ? 0.25399 0.28301 0.21921 0.01013  0.00937  -0.01094 139 VAL   D O     
5035 C  CB    . VAL   D 140 ? 0.31134 0.34020 0.29022 0.00340  0.00412  -0.01168 139 VAL   D CB    
5036 C  CG1   . VAL   D 140 ? 0.30445 0.33624 0.28623 0.00155  0.00760  -0.01089 139 VAL   D CG1   
5037 C  CG2   . VAL   D 140 ? 0.27947 0.31061 0.26243 0.00058  0.00482  -0.01079 139 VAL   D CG2   
5038 N  N     . GLU   D 141 ? 0.28641 0.30685 0.24847 0.01408  0.00052  -0.01379 140 GLU   D N     
5039 C  CA    . GLU   D 141 ? 0.29766 0.31545 0.25398 0.01831  0.00036  -0.01414 140 GLU   D CA    
5040 C  C     . GLU   D 141 ? 0.31092 0.33044 0.26041 0.02180  0.00455  -0.01239 140 GLU   D C     
5041 O  O     . GLU   D 141 ? 0.30111 0.32234 0.24922 0.02318  0.00771  -0.01105 140 GLU   D O     
5042 C  CB    . GLU   D 141 ? 0.31470 0.32479 0.26688 0.02249  -0.00653 -0.01648 140 GLU   D CB    
5043 C  CG    . GLU   D 141 ? 0.37651 0.38507 0.33739 0.01911  -0.01092 -0.01743 140 GLU   D CG    
5044 C  CD    . GLU   D 141 ? 0.45514 0.45549 0.41338 0.02266  -0.01916 -0.01972 140 GLU   D CD    
5045 O  OE1   . GLU   D 141 ? 0.51560 0.51089 0.46358 0.02835  -0.02134 -0.02097 140 GLU   D OE1   
5046 O  OE2   . GLU   D 141 ? 0.54337 0.54205 0.51000 0.02005  -0.02373 -0.02004 140 GLU   D OE2   
5047 N  N     . ALA   D 142 ? 0.29491 0.31446 0.24104 0.02312  0.00488  -0.01190 141 ALA   D N     
5048 C  CA    . ALA   D 142 ? 0.34037 0.36208 0.28121 0.02659  0.00915  -0.00939 141 ALA   D CA    
5049 C  C     . ALA   D 142 ? 0.29790 0.32648 0.24484 0.02238  0.01463  -0.00671 141 ALA   D C     
5050 O  O     . ALA   D 142 ? 0.33099 0.36200 0.27600 0.02493  0.01841  -0.00383 141 ALA   D O     
5051 C  CB    . ALA   D 142 ? 0.32924 0.34925 0.26521 0.02911  0.00806  -0.00939 141 ALA   D CB    
5052 N  N     . MET   D 143 ? 0.26272 0.29415 0.21705 0.01642  0.01493  -0.00732 142 MET   D N     
5053 C  CA    . MET   D 143 ? 0.31873 0.35532 0.27827 0.01266  0.01900  -0.00533 142 MET   D CA    
5054 C  C     . MET   D 143 ? 0.32304 0.36069 0.28407 0.01290  0.02071  -0.00444 142 MET   D C     
5055 O  O     . MET   D 143 ? 0.28124 0.32245 0.24523 0.01156  0.02385  -0.00211 142 MET   D O     
5056 C  CB    . MET   D 143 ? 0.31236 0.35055 0.27771 0.00735  0.01861  -0.00643 142 MET   D CB    
5057 C  CG    . MET   D 143 ? 0.30035 0.33869 0.26514 0.00652  0.01790  -0.00662 142 MET   D CG    
5058 S  SD    . MET   D 143 ? 0.35006 0.38888 0.32048 0.00198  0.01662  -0.00795 142 MET   D SD    
5059 C  CE    . MET   D 143 ? 0.30926 0.35139 0.28366 -0.00134 0.02007  -0.00697 142 MET   D CE    
5060 N  N     . GLU   D 144 ? 0.31122 0.34561 0.27074 0.01454  0.01826  -0.00617 143 GLU   D N     
5061 C  CA    . GLU   D 144 ? 0.31367 0.34908 0.27543 0.01398  0.01963  -0.00572 143 GLU   D CA    
5062 C  C     . GLU   D 144 ? 0.30356 0.34107 0.26341 0.01701  0.02306  -0.00263 143 GLU   D C     
5063 O  O     . GLU   D 144 ? 0.31046 0.35085 0.27456 0.01492  0.02531  -0.00120 143 GLU   D O     
5064 C  CB    . GLU   D 144 ? 0.35423 0.38522 0.31419 0.01588  0.01598  -0.00803 143 GLU   D CB    
5065 C  CG    . GLU   D 144 ? 0.34901 0.37934 0.31449 0.01193  0.01336  -0.00992 143 GLU   D CG    
5066 C  CD    . GLU   D 144 ? 0.41500 0.44216 0.38134 0.01282  0.01044  -0.01140 143 GLU   D CD    
5067 O  OE1   . GLU   D 144 ? 0.48005 0.50227 0.44097 0.01725  0.00700  -0.01262 143 GLU   D OE1   
5068 O  OE2   . GLU   D 144 ? 0.50271 0.53195 0.47475 0.00945  0.01149  -0.01133 143 GLU   D OE2   
5069 N  N     . ARG   D 145 ? 0.26913 0.30506 0.22272 0.02238  0.02348  -0.00127 144 ARG   D N     
5070 C  CA    . ARG   D 145 ? 0.32880 0.36701 0.28117 0.02604  0.02723  0.00259  144 ARG   D CA    
5071 C  C     . ARG   D 145 ? 0.31678 0.36062 0.27582 0.02295  0.03081  0.00624  144 ARG   D C     
5072 O  O     . ARG   D 145 ? 0.31570 0.36238 0.27669 0.02500  0.03401  0.01024  144 ARG   D O     
5073 C  CB    . ARG   D 145 ? 0.37058 0.40564 0.31389 0.03355  0.02734  0.00377  144 ARG   D CB    
5074 C  CG    . ARG   D 145 ? 0.36612 0.40169 0.30720 0.03471  0.02780  0.00482  144 ARG   D CG    
5075 C  CD    . ARG   D 145 ? 0.41818 0.45047 0.34913 0.04372  0.02877  0.00677  144 ARG   D CD    
5076 N  NE    . ARG   D 145 ? 0.48247 0.51429 0.40947 0.04620  0.02900  0.00767  144 ARG   D NE    
5077 C  CZ    . ARG   D 145 ? 0.55921 0.59518 0.48703 0.04874  0.03362  0.01271  144 ARG   D CZ    
5078 N  NH1   . ARG   D 145 ? 0.44518 0.48650 0.37901 0.04860  0.03827  0.01764  144 ARG   D NH1   
5079 N  NH2   . ARG   D 145 ? 0.56437 0.59912 0.48744 0.05162  0.03346  0.01314  144 ARG   D NH2   
5080 N  N     . PHE   D 146 ? 0.25813 0.30343 0.22101 0.01838  0.03011  0.00529  145 PHE   D N     
5081 C  CA    . PHE   D 146 ? 0.27420 0.32380 0.24377 0.01510  0.03231  0.00822  145 PHE   D CA    
5082 C  C     . PHE   D 146 ? 0.29477 0.34548 0.27026 0.01045  0.03193  0.00733  145 PHE   D C     
5083 O  O     . PHE   D 146 ? 0.27142 0.32467 0.25261 0.00755  0.03268  0.00929  145 PHE   D O     
5084 C  CB    . PHE   D 146 ? 0.27846 0.32845 0.24835 0.01301  0.03154  0.00757  145 PHE   D CB    
5085 C  CG    . PHE   D 146 ? 0.25262 0.30120 0.21617 0.01793  0.03180  0.00842  145 PHE   D CG    
5086 C  CD1   . PHE   D 146 ? 0.30613 0.35704 0.26915 0.02217  0.03500  0.01314  145 PHE   D CD1   
5087 C  CD2   . PHE   D 146 ? 0.30735 0.35207 0.26559 0.01884  0.02877  0.00488  145 PHE   D CD2   
5088 C  CE1   . PHE   D 146 ? 0.33953 0.38870 0.29540 0.02780  0.03553  0.01414  145 PHE   D CE1   
5089 C  CE2   . PHE   D 146 ? 0.37469 0.41725 0.32614 0.02393  0.02850  0.00543  145 PHE   D CE2   
5090 C  CZ    . PHE   D 146 ? 0.40007 0.44470 0.34958 0.02873  0.03205  0.00998  145 PHE   D CZ    
5091 N  N     . GLY   D 147 ? 0.23487 0.28332 0.20906 0.01002  0.03044  0.00451  146 GLY   D N     
5092 C  CA    . GLY   D 147 ? 0.27054 0.31957 0.24925 0.00637  0.03014  0.00357  146 GLY   D CA    
5093 C  C     . GLY   D 147 ? 0.34328 0.39316 0.32322 0.00817  0.03153  0.00550  146 GLY   D C     
5094 O  O     . GLY   D 147 ? 0.31443 0.36538 0.29292 0.01216  0.03344  0.00863  146 GLY   D O     
5095 N  N     . SER   D 148 ? 0.26691 0.31642 0.24963 0.00547  0.03082  0.00397  147 SER   D N     
5096 C  CA    . SER   D 148 ? 0.31021 0.36073 0.29519 0.00635  0.03197  0.00576  147 SER   D CA    
5097 C  C     . SER   D 148 ? 0.29909 0.34802 0.28506 0.00379  0.03059  0.00278  147 SER   D C     
5098 O  O     . SER   D 148 ? 0.29467 0.34219 0.28029 0.00140  0.02918  0.00001  147 SER   D O     
5099 C  CB    . SER   D 148 ? 0.26793 0.32157 0.25918 0.00509  0.03327  0.00971  147 SER   D CB    
5100 O  OG    . SER   D 148 ? 0.30101 0.35429 0.29598 0.00069  0.03155  0.00833  147 SER   D OG    
5101 N  N     . ARG   D 149 ? 0.32551 0.37492 0.31308 0.00454  0.03133  0.00384  148 ARG   D N     
5102 C  CA    . ARG   D 149 ? 0.36072 0.40876 0.34929 0.00248  0.03030  0.00139  148 ARG   D CA    
5103 C  C     . ARG   D 149 ? 0.33344 0.38116 0.32465 -0.00138 0.02930  -0.00004 148 ARG   D C     
5104 O  O     . ARG   D 149 ? 0.31180 0.35791 0.30204 -0.00267 0.02847  -0.00265 148 ARG   D O     
5105 C  CB    . ARG   D 149 ? 0.41392 0.46298 0.40464 0.00362  0.03138  0.00334  148 ARG   D CB    
5106 C  CG    . ARG   D 149 ? 0.35729 0.40490 0.34880 0.00177  0.03040  0.00089  148 ARG   D CG    
5107 C  CD    . ARG   D 149 ? 0.45274 0.50089 0.44507 0.00368  0.03138  0.00241  148 ARG   D CD    
5108 N  NE    . ARG   D 149 ? 0.42856 0.47567 0.42247 0.00165  0.03057  0.00051  148 ARG   D NE    
5109 C  CZ    . ARG   D 149 ? 0.41548 0.46312 0.41336 -0.00078 0.03017  0.00113  148 ARG   D CZ    
5110 N  NH1   . ARG   D 149 ? 0.42019 0.46925 0.42170 -0.00181 0.03004  0.00359  148 ARG   D NH1   
5111 N  NH2   . ARG   D 149 ? 0.46393 0.51026 0.46229 -0.00201 0.02950  -0.00068 148 ARG   D NH2   
5112 N  N     . ASN   D 150 ? 0.33074 0.37965 0.32534 -0.00289 0.02922  0.00187  149 ASN   D N     
5113 C  CA    . ASN   D 150 ? 0.34163 0.38901 0.33722 -0.00570 0.02773  0.00025  149 ASN   D CA    
5114 C  C     . ASN   D 150 ? 0.32644 0.37337 0.32033 -0.00649 0.02727  -0.00055 149 ASN   D C     
5115 O  O     . ASN   D 150 ? 0.33832 0.38351 0.33203 -0.00818 0.02603  -0.00181 149 ASN   D O     
5116 C  CB    . ASN   D 150 ? 0.33627 0.38380 0.33668 -0.00702 0.02658  0.00224  149 ASN   D CB    
5117 C  CG    . ASN   D 150 ? 0.39299 0.44201 0.39716 -0.00746 0.02609  0.00523  149 ASN   D CG    
5118 O  OD1   . ASN   D 150 ? 0.36485 0.41551 0.36794 -0.00625 0.02735  0.00644  149 ASN   D OD1   
5119 N  ND2   . ASN   D 150 ? 0.46118 0.50939 0.47029 -0.00910 0.02386  0.00663  149 ASN   D ND2   
5120 N  N     . GLY   D 151 ? 0.27388 0.32192 0.26597 -0.00492 0.02810  0.00014  150 GLY   D N     
5121 C  CA    . GLY   D 151 ? 0.28991 0.33751 0.28006 -0.00553 0.02770  -0.00089 150 GLY   D CA    
5122 C  C     . GLY   D 151 ? 0.30072 0.34962 0.29282 -0.00594 0.02762  0.00136  150 GLY   D C     
5123 O  O     . GLY   D 151 ? 0.27104 0.31991 0.26122 -0.00592 0.02755  0.00086  150 GLY   D O     
5124 N  N     . LYS   D 152 ? 0.26497 0.31516 0.26157 -0.00624 0.02752  0.00420  151 LYS   D N     
5125 C  CA    . LYS   D 152 ? 0.32003 0.37172 0.31990 -0.00662 0.02729  0.00698  151 LYS   D CA    
5126 C  C     . LYS   D 152 ? 0.27953 0.33324 0.27709 -0.00379 0.02935  0.00874  151 LYS   D C     
5127 O  O     . LYS   D 152 ? 0.31623 0.37059 0.31151 -0.00088 0.03094  0.00945  151 LYS   D O     
5128 C  CB    . LYS   D 152 ? 0.33743 0.39048 0.34441 -0.00725 0.02663  0.01063  151 LYS   D CB    
5129 C  CG    . LYS   D 152 ? 0.48085 0.53560 0.49314 -0.00784 0.02602  0.01422  151 LYS   D CG    
5130 C  CD    . LYS   D 152 ? 0.54877 0.60483 0.57003 -0.00871 0.02474  0.01837  151 LYS   D CD    
5131 C  CE    . LYS   D 152 ? 0.62008 0.67827 0.64853 -0.00926 0.02403  0.02287  151 LYS   D CE    
5132 N  NZ    . LYS   D 152 ? 0.66923 0.72833 0.70830 -0.01056 0.02182  0.02721  151 LYS   D NZ    
5133 N  N     . THR   D 153 ? 0.28521 0.33925 0.28232 -0.00421 0.02911  0.00908  152 THR   D N     
5134 C  CA    . THR   D 153 ? 0.26879 0.32401 0.26247 -0.00115 0.03079  0.01026  152 THR   D CA    
5135 C  C     . THR   D 153 ? 0.33496 0.39349 0.33321 0.00079  0.03265  0.01571  152 THR   D C     
5136 O  O     . THR   D 153 ? 0.30861 0.36853 0.31385 -0.00125 0.03191  0.01843  152 THR   D O     
5137 C  CB    . THR   D 153 ? 0.28283 0.33668 0.27303 -0.00222 0.02976  0.00770  152 THR   D CB    
5138 O  OG1   . THR   D 153 ? 0.30006 0.35417 0.29401 -0.00488 0.02858  0.00853  152 THR   D OG1   
5139 C  CG2   . THR   D 153 ? 0.27219 0.32335 0.25899 -0.00361 0.02844  0.00334  152 THR   D CG2   
5140 N  N     . SER   D 154 ? 0.27791 0.33743 0.27231 0.00515  0.03489  0.01757  153 SER   D N     
5141 C  CA    . SER   D 154 ? 0.31355 0.37666 0.31211 0.00804  0.03758  0.02363  153 SER   D CA    
5142 C  C     . SER   D 154 ? 0.35444 0.41861 0.35248 0.00872  0.03812  0.02516  153 SER   D C     
5143 O  O     . SER   D 154 ? 0.34906 0.41668 0.35194 0.01081  0.04044  0.03084  153 SER   D O     
5144 C  CB    . SER   D 154 ? 0.33169 0.39514 0.32575 0.01379  0.04036  0.02573  153 SER   D CB    
5145 O  OG    . SER   D 154 ? 0.32787 0.38791 0.31215 0.01678  0.03972  0.02198  153 SER   D OG    
5146 N  N     . LYS   D 155 ? 0.33185 0.39336 0.32427 0.00752  0.03633  0.02068  154 LYS   D N     
5147 C  CA    . LYS   D 155 ? 0.38834 0.45038 0.38031 0.00714  0.03617  0.02115  154 LYS   D CA    
5148 C  C     . LYS   D 155 ? 0.36561 0.42512 0.35691 0.00248  0.03312  0.01636  154 LYS   D C     
5149 O  O     . LYS   D 155 ? 0.32739 0.38463 0.31683 0.00080  0.03168  0.01271  154 LYS   D O     
5150 C  CB    . LYS   D 155 ? 0.34419 0.40520 0.32810 0.01221  0.03754  0.02103  154 LYS   D CB    
5151 C  CG    . LYS   D 155 ? 0.41436 0.47730 0.39723 0.01812  0.04099  0.02594  154 LYS   D CG    
5152 C  CD    . LYS   D 155 ? 0.44322 0.50460 0.41746 0.02402  0.04222  0.02637  154 LYS   D CD    
5153 C  CE    . LYS   D 155 ? 0.49348 0.55695 0.46658 0.03076  0.04636  0.03219  154 LYS   D CE    
5154 N  NZ    . LYS   D 155 ? 0.58168 0.64255 0.54450 0.03758  0.04734  0.03233  154 LYS   D NZ    
5155 N  N     . LYS   D 156 ? 0.31078 0.37072 0.30377 0.00065  0.03233  0.01670  155 LYS   D N     
5156 C  CA    . LYS   D 156 ? 0.39656 0.45398 0.38818 -0.00299 0.02983  0.01257  155 LYS   D CA    
5157 C  C     . LYS   D 156 ? 0.30846 0.36396 0.29310 -0.00177 0.02956  0.00914  155 LYS   D C     
5158 O  O     . LYS   D 156 ? 0.31678 0.37281 0.29866 0.00045  0.03030  0.01007  155 LYS   D O     
5159 C  CB    . LYS   D 156 ? 0.39939 0.45757 0.39542 -0.00521 0.02874  0.01428  155 LYS   D CB    
5160 C  CG    . LYS   D 156 ? 0.43179 0.49187 0.43639 -0.00620 0.02831  0.01857  155 LYS   D CG    
5161 C  CD    . LYS   D 156 ? 0.48892 0.54870 0.49780 -0.00865 0.02615  0.01961  155 LYS   D CD    
5162 C  CE    . LYS   D 156 ? 0.55602 0.61984 0.57149 -0.00701 0.02790  0.02579  155 LYS   D CE    
5163 N  NZ    . LYS   D 156 ? 0.56891 0.63507 0.57933 -0.00267 0.03172  0.02743  155 LYS   D NZ    
5164 N  N     . ILE   D 157 ? 0.27118 0.32440 0.25344 -0.00299 0.02836  0.00551  156 ILE   D N     
5165 C  CA    . ILE   D 157 ? 0.29988 0.35114 0.27739 -0.00215 0.02744  0.00260  156 ILE   D CA    
5166 C  C     . ILE   D 157 ? 0.32485 0.37512 0.30275 -0.00524 0.02629  0.00049  156 ILE   D C     
5167 O  O     . ILE   D 157 ? 0.34934 0.39865 0.32859 -0.00729 0.02582  -0.00090 156 ILE   D O     
5168 C  CB    . ILE   D 157 ? 0.29222 0.34185 0.26824 -0.00130 0.02686  0.00072  156 ILE   D CB    
5169 C  CG1   . ILE   D 157 ? 0.29272 0.34310 0.26835 0.00180  0.02816  0.00289  156 ILE   D CG1   
5170 C  CG2   . ILE   D 157 ? 0.37189 0.41929 0.34442 -0.00027 0.02513  -0.00164 156 ILE   D CG2   
5171 C  CD1   . ILE   D 157 ? 0.37034 0.42120 0.34261 0.00597  0.02926  0.00514  156 ILE   D CD1   
5172 N  N     . THR   D 158 ? 0.30896 0.35926 0.28521 -0.00513 0.02597  0.00034  157 THR   D N     
5173 C  CA    . THR   D 158 ? 0.29810 0.34768 0.27471 -0.00768 0.02522  -0.00105 157 THR   D CA    
5174 C  C     . THR   D 158 ? 0.27048 0.31894 0.24466 -0.00748 0.02437  -0.00293 157 THR   D C     
5175 O  O     . THR   D 158 ? 0.30770 0.35567 0.27960 -0.00525 0.02374  -0.00306 157 THR   D O     
5176 C  CB    . THR   D 158 ? 0.35702 0.40777 0.33521 -0.00838 0.02533  0.00087  157 THR   D CB    
5177 O  OG1   . THR   D 158 ? 0.32483 0.37672 0.30115 -0.00598 0.02600  0.00230  157 THR   D OG1   
5178 C  CG2   . THR   D 158 ? 0.39124 0.44297 0.37378 -0.00898 0.02545  0.00325  157 THR   D CG2   
5179 N  N     . ILE   D 159 ? 0.31925 0.36692 0.29392 -0.00945 0.02414  -0.00422 158 ILE   D N     
5180 C  CA    . ILE   D 159 ? 0.29247 0.33955 0.26638 -0.00971 0.02346  -0.00527 158 ILE   D CA    
5181 C  C     . ILE   D 159 ? 0.31513 0.36271 0.28790 -0.01012 0.02340  -0.00475 158 ILE   D C     
5182 O  O     . ILE   D 159 ? 0.33178 0.37900 0.30462 -0.01157 0.02367  -0.00494 158 ILE   D O     
5183 C  CB    . ILE   D 159 ? 0.31036 0.35677 0.28554 -0.01095 0.02397  -0.00605 158 ILE   D CB    
5184 C  CG1   . ILE   D 159 ? 0.29837 0.34449 0.27513 -0.01051 0.02414  -0.00627 158 ILE   D CG1   
5185 C  CG2   . ILE   D 159 ? 0.31634 0.36270 0.29205 -0.01124 0.02351  -0.00627 158 ILE   D CG2   
5186 C  CD1   . ILE   D 159 ? 0.29293 0.33859 0.27095 -0.01112 0.02532  -0.00638 158 ILE   D CD1   
5187 N  N     . ALA   D 160 ? 0.34565 0.39361 0.31676 -0.00840 0.02290  -0.00416 159 ALA   D N     
5188 C  CA    . ALA   D 160 ? 0.39399 0.44268 0.36417 -0.00853 0.02301  -0.00333 159 ALA   D CA    
5189 C  C     . ALA   D 160 ? 0.40517 0.45318 0.37497 -0.00990 0.02232  -0.00459 159 ALA   D C     
5190 O  O     . ALA   D 160 ? 0.46814 0.51641 0.43782 -0.01112 0.02258  -0.00435 159 ALA   D O     
5191 C  CB    . ALA   D 160 ? 0.36007 0.40907 0.32772 -0.00548 0.02292  -0.00217 159 ALA   D CB    
5192 N  N     . ASP   D 161 ? 0.37703 0.42411 0.34727 -0.00971 0.02131  -0.00566 160 ASP   D N     
5193 C  CA    . ASP   D 161 ? 0.44645 0.49327 0.41767 -0.01090 0.02090  -0.00617 160 ASP   D CA    
5194 C  C     . ASP   D 161 ? 0.41760 0.46396 0.39197 -0.01111 0.02040  -0.00639 160 ASP   D C     
5195 O  O     . ASP   D 161 ? 0.36003 0.40573 0.33515 -0.01010 0.01940  -0.00662 160 ASP   D O     
5196 C  CB    . ASP   D 161 ? 0.45554 0.50199 0.42506 -0.00998 0.01934  -0.00632 160 ASP   D CB    
5197 C  CG    . ASP   D 161 ? 0.46600 0.51266 0.43656 -0.01144 0.01936  -0.00640 160 ASP   D CG    
5198 O  OD1   . ASP   D 161 ? 0.51507 0.56214 0.48687 -0.01276 0.02097  -0.00617 160 ASP   D OD1   
5199 O  OD2   . ASP   D 161 ? 0.60277 0.64888 0.57245 -0.01081 0.01769  -0.00664 160 ASP   D OD2   
5200 N  N     . CYS   D 162 ? 0.33187 0.37861 0.30839 -0.01218 0.02117  -0.00595 161 CYS   D N     
5201 C  CA    . CYS   D 162 ? 0.37204 0.41897 0.35308 -0.01231 0.02113  -0.00516 161 CYS   D CA    
5202 C  C     . CYS   D 162 ? 0.36378 0.41151 0.34736 -0.01293 0.02186  -0.00392 161 CYS   D C     
5203 O  O     . CYS   D 162 ? 0.37777 0.42564 0.35850 -0.01326 0.02303  -0.00406 161 CYS   D O     
5204 C  CB    . CYS   D 162 ? 0.36438 0.41149 0.34571 -0.01227 0.02321  -0.00490 161 CYS   D CB    
5205 S  SG    . CYS   D 162 ? 0.35060 0.39715 0.32775 -0.01243 0.02582  -0.00512 161 CYS   D SG    
5206 N  N     . GLY   D 163 ? 0.36981 0.41804 0.35933 -0.01300 0.02094  -0.00244 162 GLY   D N     
5207 C  CA    . GLY   D 163 ? 0.34714 0.39666 0.34060 -0.01336 0.02199  -0.00035 162 GLY   D CA    
5208 C  C     . GLY   D 163 ? 0.37114 0.42151 0.37334 -0.01347 0.02069  0.00208  162 GLY   D C     
5209 O  O     . GLY   D 163 ? 0.34245 0.39219 0.34722 -0.01328 0.01914  0.00192  162 GLY   D O     
5210 N  N     . GLN   D 164 ? 0.36729 0.41916 0.37481 -0.01374 0.02120  0.00469  163 GLN   D N     
5211 C  CA    . GLN   D 164 ? 0.36532 0.41840 0.38346 -0.01402 0.01966  0.00799  163 GLN   D CA    
5212 C  C     . GLN   D 164 ? 0.37294 0.42433 0.39503 -0.01482 0.01405  0.00750  163 GLN   D C     
5213 O  O     . GLN   D 164 ? 0.42074 0.47160 0.43939 -0.01508 0.01328  0.00641  163 GLN   D O     
5214 C  CB    . GLN   D 164 ? 0.35780 0.41395 0.38081 -0.01332 0.02415  0.01231  163 GLN   D CB    
5215 C  CG    . GLN   D 164 ? 0.31671 0.37486 0.35271 -0.01354 0.02307  0.01688  163 GLN   D CG    
5216 C  CD    . GLN   D 164 ? 0.36125 0.42291 0.40181 -0.01185 0.02887  0.02203  163 GLN   D CD    
5217 O  OE1   . GLN   D 164 ? 0.41195 0.47375 0.44447 -0.01016 0.03341  0.02163  163 GLN   D OE1   
5218 N  NE2   . GLN   D 164 ? 0.39071 0.45496 0.44434 -0.01185 0.02865  0.02724  163 GLN   D NE2   
5219 N  N     . LEU   D 165 ? 0.37929 0.42930 0.40843 -0.01503 0.00963  0.00818  164 LEU   D N     
5220 C  CA    . LEU   D 165 ? 0.41682 0.46401 0.44992 -0.01535 0.00310  0.00764  164 LEU   D CA    
5221 C  C     . LEU   D 165 ? 0.41924 0.46889 0.46465 -0.01640 0.00263  0.01244  164 LEU   D C     
5222 O  O     . LEU   D 165 ? 0.44283 0.49565 0.49672 -0.01656 0.00555  0.01661  164 LEU   D O     
5223 C  CB    . LEU   D 165 ? 0.43150 0.47473 0.46567 -0.01462 -0.00262 0.00576  164 LEU   D CB    
5224 C  CG    . LEU   D 165 ? 0.43691 0.47741 0.45888 -0.01300 -0.00262 0.00135  164 LEU   D CG    
5225 C  CD1   . LEU   D 165 ? 0.44517 0.48183 0.46761 -0.01170 -0.00735 -0.00017 164 LEU   D CD1   
5226 C  CD2   . LEU   D 165 ? 0.44769 0.48599 0.46122 -0.01199 -0.00419 -0.00136 164 LEU   D CD2   
5227 P  PG    . GNP   E .   ? 0.32760 0.33085 0.28702 0.00143  0.01004  -0.01771 201 GNP   A PG    
5228 O  O1G   . GNP   E .   ? 0.31988 0.32770 0.28832 -0.00256 0.00886  -0.01578 201 GNP   A O1G   
5229 O  O2G   . GNP   E .   ? 0.33775 0.34201 0.29769 0.00203  0.01178  -0.01775 201 GNP   A O2G   
5230 O  O3G   . GNP   E .   ? 0.36022 0.36669 0.31719 0.00254  0.01492  -0.01710 201 GNP   A O3G   
5231 N  N3B   . GNP   E .   ? 0.31021 0.30387 0.26232 0.00431  0.00412  -0.02004 201 GNP   A N3B   
5232 P  PB    . GNP   E .   ? 0.31466 0.30251 0.26950 0.00331  -0.00359 -0.02081 201 GNP   A PB    
5233 O  O1B   . GNP   E .   ? 0.32844 0.31181 0.27977 0.00551  -0.00547 -0.02226 201 GNP   A O1B   
5234 O  O2B   . GNP   E .   ? 0.27871 0.27180 0.24498 -0.00135 -0.00495 -0.01817 201 GNP   A O2B   
5235 O  O3A   . GNP   E .   ? 0.35010 0.32938 0.29742 0.00611  -0.00872 -0.02294 201 GNP   A O3A   
5236 P  PA    . GNP   E .   ? 0.32881 0.30631 0.27998 0.00404  -0.01351 -0.02246 201 GNP   A PA    
5237 O  O1A   . GNP   E .   ? 0.32438 0.30119 0.28540 0.00076  -0.01939 -0.02103 201 GNP   A O1A   
5238 O  O2A   . GNP   E .   ? 0.32246 0.30743 0.27657 0.00210  -0.00802 -0.02067 201 GNP   A O2A   
5239 O  "O5'" . GNP   E .   ? 0.35553 0.32193 0.29382 0.00941  -0.01795 -0.02584 201 GNP   A "O5'" 
5240 C  "C5'" . GNP   E .   ? 0.38121 0.34666 0.30880 0.01390  -0.01279 -0.02690 201 GNP   A "C5'" 
5241 C  "C4'" . GNP   E .   ? 0.40234 0.35805 0.32004 0.01805  -0.01781 -0.02936 201 GNP   A "C4'" 
5242 O  "O4'" . GNP   E .   ? 0.38192 0.32697 0.29397 0.02115  -0.02558 -0.03202 201 GNP   A "O4'" 
5243 C  "C3'" . GNP   E .   ? 0.49587 0.45199 0.41948 0.01466  -0.02160 -0.02870 201 GNP   A "C3'" 
5244 O  "O3'" . GNP   E .   ? 0.53941 0.49095 0.45330 0.01854  -0.02130 -0.03013 201 GNP   A "O3'" 
5245 C  "C2'" . GNP   E .   ? 0.40771 0.35648 0.33522 0.01354  -0.03139 -0.02973 201 GNP   A "C2'" 
5246 O  "O2'" . GNP   E .   ? 0.44325 0.38693 0.37164 0.01298  -0.03769 -0.03031 201 GNP   A "O2'" 
5247 C  "C1'" . GNP   E .   ? 0.40700 0.34598 0.32195 0.01969  -0.03411 -0.03292 201 GNP   A "C1'" 
5248 N  N9    . GNP   E .   ? 0.36317 0.29662 0.28228 0.01875  -0.04181 -0.03370 201 GNP   A N9    
5249 C  C8    . GNP   E .   ? 0.33826 0.27820 0.26952 0.01402  -0.04128 -0.03130 201 GNP   A C8    
5250 N  N7    . GNP   E .   ? 0.35268 0.28530 0.28588 0.01424  -0.04952 -0.03239 201 GNP   A N7    
5251 C  C5    . GNP   E .   ? 0.36031 0.28015 0.28129 0.01962  -0.05645 -0.03608 201 GNP   A C5    
5252 C  C6    . GNP   E .   ? 0.37787 0.28462 0.29467 0.02252  -0.06759 -0.03893 201 GNP   A C6    
5253 O  O6    . GNP   E .   ? 0.37985 0.28422 0.30423 0.02043  -0.07360 -0.03846 201 GNP   A O6    
5254 N  N1    . GNP   E .   ? 0.46600 0.36125 0.36803 0.02877  -0.07202 -0.04258 201 GNP   A N1    
5255 C  C2    . GNP   E .   ? 0.44678 0.34363 0.33985 0.03171  -0.06593 -0.04303 201 GNP   A C2    
5256 N  N2    . GNP   E .   ? 0.50091 0.38509 0.37932 0.03837  -0.07148 -0.04664 201 GNP   A N2    
5257 N  N3    . GNP   E .   ? 0.42004 0.32968 0.31814 0.02858  -0.05542 -0.04007 201 GNP   A N3    
5258 C  C4    . GNP   E .   ? 0.38917 0.30945 0.30100 0.02263  -0.05150 -0.03688 201 GNP   A C4    
5259 MG MG    . MG    F .   ? 0.28811 0.29377 0.26412 -0.00536 0.00203  -0.01446 202 MG    A MG    
5260 P  PG    . GNP   G .   ? 0.36948 0.36574 0.33846 0.03164  0.03729  -0.02586 201 GNP   B PG    
5261 O  O1G   . GNP   G .   ? 0.36395 0.36465 0.34227 0.02519  0.03533  -0.02639 201 GNP   B O1G   
5262 O  O2G   . GNP   G .   ? 0.36115 0.34971 0.32081 0.03374  0.03204  -0.02923 201 GNP   B O2G   
5263 O  O3G   . GNP   G .   ? 0.40587 0.40354 0.37638 0.03357  0.04040  -0.02436 201 GNP   B O3G   
5264 N  N3B   . GNP   G .   ? 0.40356 0.40162 0.37147 0.03451  0.04145  -0.02293 201 GNP   B N3B   
5265 P  PB    . GNP   G .   ? 0.34832 0.34735 0.31741 0.03219  0.04015  -0.02312 201 GNP   B PB    
5266 O  O1B   . GNP   G .   ? 0.36752 0.35953 0.32591 0.03562  0.03686  -0.02539 201 GNP   B O1B   
5267 O  O2B   . GNP   G .   ? 0.34899 0.35237 0.32735 0.02564  0.03800  -0.02380 201 GNP   B O2B   
5268 O  O3A   . GNP   G .   ? 0.38230 0.38593 0.35507 0.03438  0.04609  -0.01873 201 GNP   B O3A   
5269 P  PA    . GNP   G .   ? 0.39164 0.40263 0.37639 0.03060  0.04888  -0.01554 201 GNP   B PA    
5270 O  O1A   . GNP   G .   ? 0.34093 0.35255 0.32761 0.02645  0.04570  -0.01733 201 GNP   B O1A   
5271 O  O2A   . GNP   G .   ? 0.31123 0.32597 0.30446 0.02823  0.04983  -0.01436 201 GNP   B O2A   
5272 O  "O5'" . GNP   G .   ? 0.35865 0.37072 0.34159 0.03602  0.05436  -0.01121 201 GNP   B "O5'" 
5273 C  "C5'" . GNP   G .   ? 0.43860 0.45022 0.41888 0.04157  0.05866  -0.00827 201 GNP   B "C5'" 
5274 C  "C4'" . GNP   G .   ? 0.43759 0.45404 0.42392 0.04434  0.06458  -0.00229 201 GNP   B "C4'" 
5275 O  "O4'" . GNP   G .   ? 0.41194 0.42647 0.39210 0.04696  0.06527  -0.00199 201 GNP   B "O4'" 
5276 C  "C3'" . GNP   G .   ? 0.43656 0.45998 0.43831 0.03894  0.06512  0.00053  201 GNP   B "C3'" 
5277 O  "O3'" . GNP   G .   ? 0.48514 0.51308 0.49473 0.04200  0.07066  0.00692  201 GNP   B "O3'" 
5278 C  "C2'" . GNP   G .   ? 0.46582 0.48976 0.46794 0.03657  0.06351  -0.00030 201 GNP   B "C2'" 
5279 O  "O2'" . GNP   G .   ? 0.47145 0.50110 0.48601 0.03400  0.06513  0.00366  201 GNP   B "O2'" 
5280 C  "C1'" . GNP   G .   ? 0.47929 0.49932 0.46987 0.04320  0.06622  0.00057  201 GNP   B "C1'" 
5281 N  N9    . GNP   G .   ? 0.43984 0.45715 0.42479 0.04197  0.06323  -0.00238 201 GNP   B N9    
5282 C  C8    . GNP   G .   ? 0.43674 0.45067 0.41783 0.03807  0.05745  -0.00769 201 GNP   B C8    
5283 N  N7    . GNP   G .   ? 0.43079 0.44301 0.40796 0.03780  0.05587  -0.00896 201 GNP   B N7    
5284 C  C5    . GNP   G .   ? 0.41057 0.42509 0.38857 0.04179  0.06097  -0.00443 201 GNP   B C5    
5285 C  C6    . GNP   G .   ? 0.42671 0.44076 0.40160 0.04343  0.06195  -0.00348 201 GNP   B C6    
5286 O  O6    . GNP   G .   ? 0.43130 0.44259 0.40193 0.04151  0.05821  -0.00672 201 GNP   B O6    
5287 N  N1    . GNP   G .   ? 0.45407 0.47141 0.43177 0.04794  0.06811  0.00229  201 GNP   B N1    
5288 C  C2    . GNP   G .   ? 0.46242 0.48333 0.44606 0.05049  0.07275  0.00694  201 GNP   B C2    
5289 N  N2    . GNP   G .   ? 0.48969 0.51404 0.47670 0.05498  0.07876  0.01318  201 GNP   B N2    
5290 N  N3    . GNP   G .   ? 0.41490 0.43618 0.40158 0.04882  0.07167  0.00593  201 GNP   B N3    
5291 C  C4    . GNP   G .   ? 0.46436 0.48221 0.44754 0.04447  0.06567  -0.00004 201 GNP   B C4    
5292 MG MG    . MG    H .   ? 0.33057 0.33698 0.31739 0.02029  0.03572  -0.02509 202 MG    B MG    
5293 C  C1    . A1AOJ I .   ? 0.26644 0.26982 0.26307 0.02346  0.03722  -0.02944 201 A1AOJ C C1    
5294 C  C10   . A1AOJ I .   ? 0.40086 0.43095 0.44000 0.03218  0.06365  0.00153  201 A1AOJ C C10   
5295 C  C11   . A1AOJ I .   ? 0.35193 0.37672 0.37907 0.02714  0.05617  -0.00738 201 A1AOJ C C11   
5296 C  C12   . A1AOJ I .   ? 0.29006 0.29208 0.27403 0.03486  0.04579  -0.02290 201 A1AOJ C C12   
5297 C  C13   . A1AOJ I .   ? 0.32121 0.32157 0.30363 0.03163  0.04149  -0.02565 201 A1AOJ C C13   
5298 C  C14   . A1AOJ I .   ? 0.32375 0.32075 0.30444 0.02648  0.03371  -0.03019 201 A1AOJ C C14   
5299 C  C15   . A1AOJ I .   ? 0.36816 0.36831 0.35140 0.02662  0.03666  -0.02793 201 A1AOJ C C15   
5300 C  C16   . A1AOJ I .   ? 0.31706 0.31119 0.29710 0.02354  0.02812  -0.03307 201 A1AOJ C C16   
5301 C  C17   . A1AOJ I .   ? 0.30337 0.29648 0.28467 0.02222  0.02591  -0.03447 201 A1AOJ C C17   
5302 C  C18   . A1AOJ I .   ? 0.30871 0.29973 0.29114 0.01939  0.02080  -0.03631 201 A1AOJ C C18   
5303 C  C19   . A1AOJ I .   ? 0.30549 0.29557 0.28816 0.01782  0.01793  -0.03660 201 A1AOJ C C19   
5304 C  C2    . A1AOJ I .   ? 0.27147 0.27531 0.26717 0.02333  0.03738  -0.02880 201 A1AOJ C C2    
5305 C  C20   . A1AOJ I .   ? 0.32104 0.31201 0.30200 0.01898  0.02003  -0.03557 201 A1AOJ C C20   
5306 C  C21   . A1AOJ I .   ? 0.34812 0.34100 0.32752 0.02190  0.02511  -0.03389 201 A1AOJ C C21   
5307 C  C22   . A1AOJ I .   ? 0.34908 0.33649 0.33697 0.01297  0.00899  -0.03753 201 A1AOJ C C22   
5308 C  C23   . A1AOJ I .   ? 0.44773 0.42757 0.42777 0.01618  0.00446  -0.03932 201 A1AOJ C C23   
5309 C  C24   . A1AOJ I .   ? 0.30470 0.29311 0.29141 0.01499  0.01297  -0.03817 201 A1AOJ C C24   
5310 C  C25   . A1AOJ I .   ? 0.31687 0.30365 0.30690 0.01275  0.00839  -0.03888 201 A1AOJ C C25   
5311 C  C26   . A1AOJ I .   ? 0.32057 0.31162 0.31907 0.00866  0.00766  -0.03737 201 A1AOJ C C26   
5312 C  C27   . A1AOJ I .   ? 0.34022 0.33722 0.34385 0.00648  0.01121  -0.03545 201 A1AOJ C C27   
5313 C  C28   . A1AOJ I .   ? 0.34100 0.34196 0.34953 0.00393  0.01142  -0.03302 201 A1AOJ C C28   
5314 C  C29   . A1AOJ I .   ? 0.33061 0.33215 0.34024 0.00435  0.01323  -0.03434 201 A1AOJ C C29   
5315 C  C3    . A1AOJ I .   ? 0.29011 0.29942 0.29424 0.02751  0.04571  -0.02261 201 A1AOJ C C3    
5316 C  C30   . A1AOJ I .   ? 0.33703 0.32091 0.33487 0.00889  -0.00025 -0.03916 201 A1AOJ C C30   
5317 C  C31   . A1AOJ I .   ? 0.38422 0.36295 0.37258 0.01317  -0.00020 -0.04121 201 A1AOJ C C31   
5318 C  C32   . A1AOJ I .   ? 0.30646 0.28689 0.29089 0.01527  0.00451  -0.04083 201 A1AOJ C C32   
5319 C  C33   . A1AOJ I .   ? 0.28298 0.27266 0.26733 0.01762  0.01754  -0.03762 201 A1AOJ C C33   
5320 C  C34   . A1AOJ I .   ? 0.27386 0.26385 0.25863 0.01837  0.01891  -0.03788 201 A1AOJ C C34   
5321 C  C35   . A1AOJ I .   ? 0.27021 0.26635 0.26345 0.01501  0.02170  -0.03655 201 A1AOJ C C35   
5322 C  C36   . A1AOJ I .   ? 0.26982 0.26537 0.26254 0.01629  0.02270  -0.03697 201 A1AOJ C C36   
5323 C  C37   . A1AOJ I .   ? 0.29430 0.29221 0.29322 0.01093  0.01874  -0.03664 201 A1AOJ C C37   
5324 C  C38   . A1AOJ I .   ? 0.26098 0.26161 0.25769 0.01489  0.02605  -0.03443 201 A1AOJ C C38   
5325 C  C39   . A1AOJ I .   ? 0.26174 0.26592 0.25992 0.01887  0.03347  -0.03080 201 A1AOJ C C39   
5326 C  C4    . A1AOJ I .   ? 0.27686 0.28085 0.27262 0.02796  0.04179  -0.02660 201 A1AOJ C C4    
5327 C  C5    . A1AOJ I .   ? 0.27609 0.28593 0.27638 0.03127  0.04919  -0.01938 201 A1AOJ C C5    
5328 C  C6    . A1AOJ I .   ? 0.31528 0.32402 0.31208 0.03092  0.04796  -0.02018 201 A1AOJ C C6    
5329 C  C7    . A1AOJ I .   ? 0.27024 0.28744 0.28213 0.02879  0.05251  -0.01401 201 A1AOJ C C7    
5330 C  C8    . A1AOJ I .   ? 0.28397 0.30502 0.30181 0.03107  0.05708  -0.00877 201 A1AOJ C C8    
5331 C  C9    . A1AOJ I .   ? 0.31170 0.33796 0.34363 0.02847  0.05821  -0.00506 201 A1AOJ C C9    
5332 N  N1    . A1AOJ I .   ? 0.27104 0.27978 0.27394 0.02302  0.04121  -0.02537 201 A1AOJ C N1    
5333 N  N2    . A1AOJ I .   ? 0.27931 0.28863 0.28176 0.02725  0.04542  -0.02246 201 A1AOJ C N2    
5334 N  N3    . A1AOJ I .   ? 0.28557 0.29801 0.28691 0.03274  0.05233  -0.01580 201 A1AOJ C N3    
5335 N  N4    . A1AOJ I .   ? 0.29108 0.28815 0.27106 0.02924  0.03643  -0.02912 201 A1AOJ C N4    
5336 N  N5    . A1AOJ I .   ? 0.32296 0.31147 0.30850 0.01517  0.01313  -0.03760 201 A1AOJ C N5    
5337 N  N6    . A1AOJ I .   ? 0.34406 0.33378 0.34631 0.00697  0.00368  -0.03732 201 A1AOJ C N6    
5338 O  O1    . A1AOJ I .   ? 0.27456 0.28558 0.27547 0.03531  0.05349  -0.01592 201 A1AOJ C O1    
5339 O  O2    . A1AOJ I .   ? 0.29571 0.31376 0.31202 0.02397  0.04899  -0.01637 201 A1AOJ C O2    
5340 O  O3    . A1AOJ I .   ? 0.32610 0.32290 0.33229 0.00494  0.00841  -0.03445 201 A1AOJ C O3    
5341 O  O4    . A1AOJ I .   ? 0.29614 0.29607 0.28936 0.01891  0.02956  -0.03330 201 A1AOJ C O4    
5342 O  O5    . A1AOJ I .   ? 0.26671 0.27439 0.27088 0.01592  0.03370  -0.03001 201 A1AOJ C O5    
5343 S  S1    . A1AOJ I .   ? 0.39326 0.39679 0.37911 0.03034  0.04299  -0.02377 201 A1AOJ C S1    
5344 C  C1    . A1AOJ J .   ? 0.26664 0.30985 0.25952 -0.00652 0.03181  -0.00595 201 A1AOJ D C1    
5345 C  C10   . A1AOJ J .   ? 0.40769 0.42996 0.36142 0.00395  0.03186  -0.01013 201 A1AOJ D C10   
5346 C  C11   . A1AOJ J .   ? 0.31389 0.33506 0.27188 0.00025  0.02649  -0.01220 201 A1AOJ D C11   
5347 C  C12   . A1AOJ J .   ? 0.27482 0.30908 0.25098 -0.00115 0.03494  -0.00774 201 A1AOJ D C12   
5348 C  C13   . A1AOJ J .   ? 0.27315 0.30613 0.24906 -0.00230 0.03258  -0.00922 201 A1AOJ D C13   
5349 C  C14   . A1AOJ J .   ? 0.29387 0.32753 0.27328 -0.00439 0.03014  -0.01008 201 A1AOJ D C14   
5350 C  C15   . A1AOJ J .   ? 0.30295 0.33312 0.27851 -0.00391 0.02820  -0.01102 201 A1AOJ D C15   
5351 C  C16   . A1AOJ J .   ? 0.26058 0.29631 0.24381 -0.00548 0.02983  -0.00986 201 A1AOJ D C16   
5352 C  C17   . A1AOJ J .   ? 0.23026 0.26878 0.21705 -0.00597 0.03059  -0.00913 201 A1AOJ D C17   
5353 C  C18   . A1AOJ J .   ? 0.26187 0.30151 0.25109 -0.00635 0.03001  -0.00911 201 A1AOJ D C18   
5354 C  C19   . A1AOJ J .   ? 0.27636 0.31511 0.26519 -0.00652 0.02918  -0.00943 201 A1AOJ D C19   
5355 C  C2    . A1AOJ J .   ? 0.25926 0.30063 0.24752 -0.00624 0.03199  -0.00713 201 A1AOJ D C2    
5356 C  C20   . A1AOJ J .   ? 0.28528 0.32159 0.27173 -0.00645 0.02822  -0.00994 201 A1AOJ D C20   
5357 C  C21   . A1AOJ J .   ? 0.29914 0.33358 0.28241 -0.00581 0.02830  -0.01034 201 A1AOJ D C21   
5358 C  C22   . A1AOJ J .   ? 0.33732 0.37723 0.32912 -0.00647 0.02846  -0.00903 201 A1AOJ D C22   
5359 C  C23   . A1AOJ J .   ? 0.34747 0.38612 0.33902 -0.00610 0.02901  -0.00976 201 A1AOJ D C23   
5360 C  C24   . A1AOJ J .   ? 0.25328 0.29438 0.24571 -0.00614 0.02907  -0.00902 201 A1AOJ D C24   
5361 C  C25   . A1AOJ J .   ? 0.27730 0.31876 0.27117 -0.00540 0.02824  -0.00907 201 A1AOJ D C25   
5362 C  C26   . A1AOJ J .   ? 0.29122 0.33298 0.28396 -0.00445 0.02751  -0.00869 201 A1AOJ D C26   
5363 C  C27   . A1AOJ J .   ? 0.25417 0.29676 0.24584 -0.00455 0.02779  -0.00760 201 A1AOJ D C27   
5364 C  C28   . A1AOJ J .   ? 0.32876 0.37248 0.32250 -0.00496 0.02807  -0.00521 201 A1AOJ D C28   
5365 C  C29   . A1AOJ J .   ? 0.27825 0.32119 0.26833 -0.00293 0.02732  -0.00698 201 A1AOJ D C29   
5366 C  C3    . A1AOJ J .   ? 0.27051 0.31316 0.25972 -0.00544 0.03419  -0.00484 201 A1AOJ D C3    
5367 C  C30   . A1AOJ J .   ? 0.34847 0.38872 0.34313 -0.00293 0.02575  -0.00964 201 A1AOJ D C30   
5368 C  C31   . A1AOJ J .   ? 0.34956 0.39017 0.34687 -0.00419 0.02654  -0.00955 201 A1AOJ D C31   
5369 C  C32   . A1AOJ J .   ? 0.32486 0.36608 0.32126 -0.00515 0.02810  -0.00921 201 A1AOJ D C32   
5370 C  C33   . A1AOJ J .   ? 0.23041 0.27152 0.22243 -0.00631 0.02966  -0.00882 201 A1AOJ D C33   
5371 C  C34   . A1AOJ J .   ? 0.26121 0.30317 0.25548 -0.00624 0.02943  -0.00832 201 A1AOJ D C34   
5372 C  C35   . A1AOJ J .   ? 0.22507 0.26738 0.21823 -0.00634 0.02821  -0.00837 201 A1AOJ D C35   
5373 C  C36   . A1AOJ J .   ? 0.25571 0.29828 0.25166 -0.00627 0.02730  -0.00793 201 A1AOJ D C36   
5374 C  C37   . A1AOJ J .   ? 0.25391 0.29613 0.24594 -0.00550 0.02703  -0.00856 201 A1AOJ D C37   
5375 C  C38   . A1AOJ J .   ? 0.24422 0.28639 0.23481 -0.00690 0.02879  -0.00831 201 A1AOJ D C38   
5376 C  C39   . A1AOJ J .   ? 0.25257 0.29400 0.24080 -0.00701 0.03027  -0.00798 201 A1AOJ D C39   
5377 C  C4    . A1AOJ J .   ? 0.25746 0.30129 0.25153 -0.00564 0.03392  -0.00418 201 A1AOJ D C4    
5378 C  C5    . A1AOJ J .   ? 0.25588 0.29359 0.23552 -0.00290 0.03516  -0.00640 201 A1AOJ D C5    
5379 C  C6    . A1AOJ J .   ? 0.25875 0.29316 0.23410 -0.00236 0.03365  -0.00811 201 A1AOJ D C6    
5380 C  C7    . A1AOJ J .   ? 0.28627 0.31527 0.25342 -0.00144 0.03086  -0.00992 201 A1AOJ D C7    
5381 C  C8    . A1AOJ J .   ? 0.30327 0.32781 0.26361 0.00119  0.03045  -0.01066 201 A1AOJ D C8    
5382 C  C9    . A1AOJ J .   ? 0.32983 0.35449 0.28921 0.00062  0.02997  -0.01060 201 A1AOJ D C9    
5383 N  N1    . A1AOJ J .   ? 0.23418 0.27426 0.21866 -0.00613 0.03193  -0.00751 201 A1AOJ D N1    
5384 N  N2    . A1AOJ J .   ? 0.23578 0.27598 0.22004 -0.00493 0.03385  -0.00634 201 A1AOJ D N2    
5385 N  N3    . A1AOJ J .   ? 0.25119 0.28170 0.22020 -0.00040 0.03323  -0.00891 201 A1AOJ D N3    
5386 N  N4    . A1AOJ J .   ? 0.23703 0.27207 0.21696 -0.00356 0.03233  -0.00907 201 A1AOJ D N4    
5387 N  N5    . A1AOJ J .   ? 0.28096 0.32103 0.27198 -0.00645 0.02899  -0.00918 201 A1AOJ D N5    
5388 N  N6    . A1AOJ J .   ? 0.30706 0.34818 0.29969 -0.00294 0.02654  -0.00894 201 A1AOJ D N6    
5389 O  O1    . A1AOJ J .   ? 0.25473 0.29258 0.23371 -0.00119 0.03734  -0.00493 201 A1AOJ D O1    
5390 O  O2    . A1AOJ J .   ? 0.24547 0.27649 0.21609 -0.00396 0.02925  -0.01000 201 A1AOJ D O2    
5391 O  O3    . A1AOJ J .   ? 0.33787 0.38082 0.33045 -0.00429 0.02807  -0.00677 201 A1AOJ D O3    
5392 O  O4    . A1AOJ J .   ? 0.25172 0.29373 0.24251 -0.00683 0.03006  -0.00791 201 A1AOJ D O4    
5393 O  O5    . A1AOJ J .   ? 0.23204 0.27317 0.21864 -0.00752 0.02929  -0.00828 201 A1AOJ D O5    
5394 S  S1    . A1AOJ J .   ? 0.33525 0.36355 0.30622 -0.00200 0.02934  -0.01101 201 A1AOJ D S1    
5395 O  O     . HOH   K .   ? 0.58423 0.62359 0.58282 -0.00770 0.02490  -0.00564 301 HOH   A O     
5396 O  O     . HOH   K .   ? 0.56306 0.54469 0.51676 -0.00413 -0.01858 -0.01857 302 HOH   A O     
5397 O  O     . HOH   K .   ? 0.37759 0.39963 0.39010 -0.01475 -0.00070 -0.00047 303 HOH   A O     
5398 O  O     . HOH   K .   ? 0.48264 0.52103 0.48212 -0.00387 0.02953  -0.01123 304 HOH   A O     
5399 O  O     . HOH   K .   ? 0.48126 0.55504 0.58462 -0.00490 0.02560  0.05776  305 HOH   A O     
5400 O  O     . HOH   K .   ? 0.87777 0.67719 0.57866 0.13866  -0.05411 -0.06408 306 HOH   A O     
5401 O  O     . HOH   K .   ? 0.46979 0.55057 0.72913 -0.02531 -0.01865 0.11435  307 HOH   A O     
5402 O  O     . HOH   K .   ? 0.49211 0.52706 0.48727 -0.00331 0.03107  -0.01202 308 HOH   A O     
5403 O  O     . HOH   K .   ? 0.55815 0.46023 0.54685 -0.00087 -0.10870 -0.02493 309 HOH   A O     
5404 O  O     . HOH   K .   ? 0.52865 0.52728 0.46529 0.00760  0.01452  -0.01806 310 HOH   A O     
5405 O  O     . HOH   K .   ? 0.55683 0.38038 0.47853 0.03148  -0.15432 -0.05225 311 HOH   A O     
5406 O  O     . HOH   K .   ? 0.51789 0.50629 0.67820 -0.03449 -0.08773 0.04060  312 HOH   A O     
5407 O  O     . HOH   K .   ? 0.52351 0.46731 0.60826 -0.01781 -0.09974 0.00047  313 HOH   A O     
5408 O  O     . HOH   K .   ? 0.66734 0.53459 0.69822 -0.00087 -0.15712 -0.02459 314 HOH   A O     
5409 O  O     . HOH   K .   ? 0.55490 0.49188 0.71844 -0.03363 -0.14099 0.02798  315 HOH   A O     
5410 O  O     . HOH   K .   ? 0.49286 0.49918 0.44513 0.01160  0.02545  -0.01718 316 HOH   A O     
5411 O  O     . HOH   K .   ? 0.56713 0.53419 0.56292 0.00016  -0.03580 -0.02254 317 HOH   A O     
5412 O  O     . HOH   K .   ? 0.45194 0.51252 0.58793 -0.01606 0.00182  0.05726  318 HOH   A O     
5413 O  O     . HOH   K .   ? 0.29198 0.30144 0.27543 -0.00701 0.00277  -0.01273 319 HOH   A O     
5414 O  O     . HOH   K .   ? 0.29408 0.33432 0.28363 -0.00325 0.03568  -0.00587 320 HOH   A O     
5415 O  O     . HOH   K .   ? 0.50531 0.46633 0.67360 -0.03607 -0.11917 0.03639  321 HOH   A O     
5416 O  O     . HOH   K .   ? 0.43847 0.47877 0.44068 -0.00106 0.03754  -0.00575 322 HOH   A O     
5417 O  O     . HOH   K .   ? 0.42399 0.41302 0.38666 -0.00226 -0.00994 -0.01814 323 HOH   A O     
5418 O  O     . HOH   K .   ? 0.41785 0.47352 0.64767 -0.03029 -0.03677 0.08858  324 HOH   A O     
5419 O  O     . HOH   K .   ? 0.64191 0.47543 0.49102 0.05366  -0.10946 -0.05882 325 HOH   A O     
5420 O  O     . HOH   K .   ? 0.55792 0.52585 0.54486 -0.00769 -0.04299 -0.01539 326 HOH   A O     
5421 O  O     . HOH   K .   ? 0.60643 0.64560 0.61786 -0.00298 0.02744  -0.00608 327 HOH   A O     
5422 O  O     . HOH   K .   ? 0.47115 0.50110 0.45631 -0.01054 0.01704  -0.00774 328 HOH   A O     
5423 O  O     . HOH   K .   ? 0.73385 0.51347 0.56289 0.06985  -0.15340 -0.07218 329 HOH   A O     
5424 O  O     . HOH   K .   ? 0.52632 0.61077 0.62103 0.00726  0.04139  0.06747  330 HOH   A O     
5425 O  O     . HOH   K .   ? 0.40871 0.46867 0.48096 -0.01308 0.01507  0.03823  331 HOH   A O     
5426 O  O     . HOH   K .   ? 0.39196 0.43259 0.39184 -0.00516 0.02765  -0.00681 332 HOH   A O     
5427 O  O     . HOH   K .   ? 0.32595 0.34508 0.29396 -0.00130 0.02195  -0.01402 333 HOH   A O     
5428 O  O     . HOH   K .   ? 0.40997 0.38193 0.44090 -0.00959 -0.04836 -0.01098 334 HOH   A O     
5429 O  O     . HOH   K .   ? 0.36250 0.32763 0.36566 -0.01047 -0.05213 -0.01217 335 HOH   A O     
5430 O  O     . HOH   K .   ? 0.82381 0.59833 0.58382 0.10573  -0.11820 -0.07808 336 HOH   A O     
5431 O  O     . HOH   K .   ? 0.66002 0.68731 0.62773 0.01109  0.04289  -0.00560 337 HOH   A O     
5432 O  O     . HOH   K .   ? 0.55170 0.65497 0.74700 -0.00034 0.03124  0.11239  338 HOH   A O     
5433 O  O     . HOH   K .   ? 0.54814 0.59982 0.56902 -0.00659 0.02586  0.01247  339 HOH   A O     
5434 O  O     . HOH   K .   ? 0.31605 0.35034 0.30966 -0.00820 0.02260  -0.00817 340 HOH   A O     
5435 O  O     . HOH   K .   ? 0.45065 0.48938 0.66122 -0.03603 -0.05371 0.07739  341 HOH   A O     
5436 O  O     . HOH   K .   ? 0.38132 0.34739 0.30229 0.02375  -0.00118 -0.02847 342 HOH   A O     
5437 O  O     . HOH   K .   ? 0.48546 0.45615 0.60868 -0.03031 -0.09304 0.02438  343 HOH   A O     
5438 O  O     . HOH   K .   ? 0.46192 0.45589 0.66740 -0.03636 -0.09397 0.05335  344 HOH   A O     
5439 O  O     . HOH   K .   ? 0.43216 0.45716 0.40927 -0.00063 0.02778  -0.01334 345 HOH   A O     
5440 O  O     . HOH   K .   ? 0.32890 0.33104 0.29914 -0.00418 0.00061  -0.01561 346 HOH   A O     
5441 O  O     . HOH   K .   ? 0.47203 0.39319 0.33494 0.04878  -0.01903 -0.03819 347 HOH   A O     
5442 O  O     . HOH   K .   ? 0.47686 0.52961 0.65973 -0.02445 -0.02239 0.06899  348 HOH   A O     
5443 O  O     . HOH   K .   ? 0.67019 0.54802 0.49810 0.07600  -0.03845 -0.05180 349 HOH   A O     
5444 O  O     . HOH   K .   ? 0.64869 0.55206 0.71131 -0.01057 -0.13266 -0.01197 350 HOH   A O     
5445 O  O     . HOH   K .   ? 0.57933 0.42946 0.55081 0.01605  -0.14849 -0.04051 351 HOH   A O     
5446 O  O     . HOH   K .   ? 0.36653 0.41859 0.51874 -0.02671 -0.02028 0.06296  352 HOH   A O     
5447 O  O     . HOH   K .   ? 0.54116 0.58734 0.55127 0.00058  0.04259  0.00298  353 HOH   A O     
5448 O  O     . HOH   K .   ? 0.78957 0.54390 0.50155 0.13779  -0.10858 -0.08441 354 HOH   A O     
5449 O  O     . HOH   K .   ? 0.32514 0.37050 0.38077 -0.01334 0.01035  0.02035  355 HOH   A O     
5450 O  O     . HOH   K .   ? 0.52708 0.55545 0.52685 -0.00208 0.02742  -0.01578 356 HOH   A O     
5451 O  O     . HOH   K .   ? 0.67261 0.53484 0.58734 0.03637  -0.10552 -0.05182 357 HOH   A O     
5452 O  O     . HOH   K .   ? 0.54238 0.55061 0.51486 0.00799  0.02268  -0.02042 358 HOH   A O     
5453 O  O     . HOH   K .   ? 0.41689 0.45071 0.47954 -0.01417 0.00072  0.01434  359 HOH   A O     
5454 O  O     . HOH   K .   ? 0.39544 0.41487 0.38420 -0.01068 0.00677  -0.00845 360 HOH   A O     
5455 O  O     . HOH   K .   ? 0.71725 0.63608 0.68893 -0.00020 -0.08600 -0.02526 361 HOH   A O     
5456 O  O     . HOH   K .   ? 0.57650 0.56490 0.87185 -0.04892 -0.13368 0.08504  362 HOH   A O     
5457 O  O     . HOH   K .   ? 0.47274 0.51295 0.46851 -0.00588 0.02783  -0.00808 363 HOH   A O     
5458 O  O     . HOH   K .   ? 0.57343 0.60338 0.55240 -0.01015 0.01861  -0.00877 364 HOH   A O     
5459 O  O     . HOH   K .   ? 0.58783 0.51601 0.69058 -0.02029 -0.12349 0.00367  365 HOH   A O     
5460 O  O     . HOH   K .   ? 0.56074 0.43640 0.52802 0.01693  -0.11804 -0.04003 366 HOH   A O     
5461 O  O     . HOH   K .   ? 0.44523 0.54658 0.63838 -0.00339 0.02752  0.11024  367 HOH   A O     
5462 O  O     . HOH   K .   ? 0.49432 0.48470 0.56690 -0.01752 -0.04631 0.00477  368 HOH   A O     
5463 O  O     . HOH   K .   ? 0.43739 0.53343 0.77203 -0.03111 -0.02915 0.15192  369 HOH   A O     
5464 O  O     A HOH   K .   ? 0.30396 0.35992 0.34437 -0.00627 0.02526  0.02228  370 HOH   A O     
5465 O  O     B HOH   K .   ? 0.30191 0.35458 0.35258 -0.01040 0.01830  0.02351  370 HOH   A O     
5466 O  O     . HOH   K .   ? 0.59585 0.48157 0.54738 0.02158  -0.09909 -0.04255 371 HOH   A O     
5467 O  O     . HOH   K .   ? 0.50956 0.52219 0.47473 0.01264  0.03223  -0.01621 372 HOH   A O     
5468 O  O     . HOH   K .   ? 0.33278 0.34343 0.30698 -0.00131 0.01290  -0.01633 373 HOH   A O     
5469 O  O     . HOH   K .   ? 0.61349 0.46122 0.56259 0.02380  -0.13982 -0.04604 374 HOH   A O     
5470 O  O     . HOH   K .   ? 0.39261 0.30610 0.46787 -0.01751 -0.13078 -0.00314 375 HOH   A O     
5471 O  O     . HOH   K .   ? 0.60944 0.50362 0.40170 0.09656  0.00150  -0.03715 376 HOH   A O     
5472 O  O     . HOH   K .   ? 0.60351 0.54893 0.48883 0.03620  -0.00719 -0.03176 377 HOH   A O     
5473 O  O     . HOH   K .   ? 0.57701 0.58278 0.69718 -0.03238 -0.05993 0.03552  378 HOH   A O     
5474 O  O     . HOH   K .   ? 0.58223 0.50974 0.71791 -0.02695 -0.13829 0.01505  379 HOH   A O     
5475 O  O     . HOH   K .   ? 0.53256 0.54548 0.48098 0.01747  0.03771  -0.01095 380 HOH   A O     
5476 O  O     . HOH   K .   ? 0.63499 0.63462 0.57940 0.02529  0.03345  -0.01749 381 HOH   A O     
5477 O  O     . HOH   K .   ? 0.29753 0.33441 0.29442 -0.01112 0.01911  -0.00339 382 HOH   A O     
5478 O  O     . HOH   K .   ? 0.37540 0.43294 0.47328 -0.01795 0.00397  0.04597  383 HOH   A O     
5479 O  O     . HOH   K .   ? 0.42143 0.47234 0.43640 -0.00683 0.02603  0.01010  384 HOH   A O     
5480 O  O     . HOH   K .   ? 0.59846 0.61187 0.55754 0.01292  0.03330  -0.01426 385 HOH   A O     
5481 O  O     . HOH   K .   ? 0.51733 0.43367 0.39261 0.03898  -0.03479 -0.03970 386 HOH   A O     
5482 O  O     . HOH   K .   ? 0.59302 0.53403 0.62327 -0.00588 -0.07862 -0.01700 387 HOH   A O     
5483 O  O     . HOH   K .   ? 0.52076 0.57049 0.53451 -0.00093 0.03051  0.00717  388 HOH   A O     
5484 O  O     . HOH   K .   ? 0.48906 0.53019 0.51456 -0.00610 0.02264  0.00215  389 HOH   A O     
5485 O  O     . HOH   K .   ? 0.49692 0.48460 0.66511 -0.03153 -0.08644 0.03779  390 HOH   A O     
5486 O  O     . HOH   K .   ? 0.26596 0.32475 0.45896 -0.02907 -0.02611 0.08088  391 HOH   A O     
5487 O  O     . HOH   K .   ? 0.54476 0.48906 0.42999 0.03882  -0.00599 -0.03236 392 HOH   A O     
5488 O  O     . HOH   K .   ? 0.38653 0.38990 0.61788 -0.04182 -0.09692 0.06959  393 HOH   A O     
5489 O  O     . HOH   K .   ? 0.44348 0.50889 0.51657 -0.00762 0.02323  0.04169  394 HOH   A O     
5490 O  O     . HOH   K .   ? 0.42591 0.49499 0.53859 -0.00818 0.01901  0.05579  395 HOH   A O     
5491 O  O     . HOH   K .   ? 0.34137 0.38650 0.36979 -0.00855 0.02081  0.00874  396 HOH   A O     
5492 O  O     . HOH   K .   ? 0.68096 0.58580 0.52073 0.07205  -0.01372 -0.04284 397 HOH   A O     
5493 O  O     . HOH   K .   ? 0.44725 0.50039 0.47810 -0.00956 0.02208  0.01815  398 HOH   A O     
5494 O  O     . HOH   K .   ? 0.49158 0.52913 0.49623 -0.00275 0.02851  -0.01037 399 HOH   A O     
5495 O  O     . HOH   K .   ? 0.69583 0.55950 0.54840 0.06434  -0.06831 -0.05779 400 HOH   A O     
5496 O  O     . HOH   K .   ? 0.52847 0.56141 0.51648 -0.00482 0.02802  -0.01151 401 HOH   A O     
5497 O  O     . HOH   K .   ? 0.65853 0.56291 0.50431 0.05539  -0.02893 -0.04217 402 HOH   A O     
5498 O  O     . HOH   K .   ? 0.54260 0.58343 0.55040 -0.01302 0.01656  0.00353  403 HOH   A O     
5499 O  O     . HOH   K .   ? 0.41656 0.45025 0.57607 -0.03185 -0.04240 0.05736  404 HOH   A O     
5500 O  O     . HOH   K .   ? 0.43616 0.52309 0.59932 -0.00568 0.02271  0.08722  405 HOH   A O     
5501 O  O     . HOH   K .   ? 0.62481 0.55287 0.44966 0.08428  0.02294  -0.02572 406 HOH   A O     
5502 O  O     . HOH   K .   ? 0.70335 0.58947 0.56118 0.04638  -0.05863 -0.04704 407 HOH   A O     
5503 O  O     . HOH   K .   ? 0.68257 0.54805 0.45010 0.10412  -0.01949 -0.04645 408 HOH   A O     
5504 O  O     . HOH   K .   ? 0.54383 0.45452 0.65574 -0.02438 -0.14859 0.00740  409 HOH   A O     
5505 O  O     . HOH   K .   ? 0.58167 0.62638 0.59306 -0.00196 0.03802  -0.00098 410 HOH   A O     
5506 O  O     . HOH   K .   ? 0.56759 0.58377 0.54139 0.00894  0.03136  -0.01659 411 HOH   A O     
5507 O  O     . HOH   K .   ? 0.77656 0.57376 0.57773 0.07726  -0.12168 -0.06954 412 HOH   A O     
5508 O  O     . HOH   K .   ? 0.45188 0.45196 0.38749 0.02086  0.02975  -0.01610 413 HOH   A O     
5509 O  O     . HOH   K .   ? 0.79221 0.57882 0.66270 0.05456  -0.16654 -0.06675 414 HOH   A O     
5510 O  O     . HOH   K .   ? 0.45569 0.51144 0.58172 -0.02270 -0.00793 0.05560  415 HOH   A O     
5511 O  O     . HOH   K .   ? 0.52199 0.43861 0.55454 -0.01242 -0.11296 -0.01182 416 HOH   A O     
5512 O  O     . HOH   K .   ? 0.81603 0.59948 0.59131 0.09429  -0.11936 -0.07463 417 HOH   A O     
5513 O  O     . HOH   K .   ? 0.47224 0.48465 0.42004 0.01019  0.02991  -0.01331 418 HOH   A O     
5514 O  O     . HOH   K .   ? 0.57166 0.62017 0.58291 -0.00405 0.02826  0.00538  419 HOH   A O     
5515 O  O     . HOH   K .   ? 0.57318 0.52596 0.76758 -0.03512 -0.13270 0.03729  420 HOH   A O     
5516 O  O     . HOH   K .   ? 0.46824 0.32876 0.50834 -0.00358 -0.16896 -0.02210 421 HOH   A O     
5517 O  O     . HOH   K .   ? 0.51353 0.57483 0.58962 -0.00480 0.02434  0.03678  422 HOH   A O     
5518 O  O     . HOH   K .   ? 0.70880 0.55016 0.63794 0.03238  -0.13567 -0.05176 423 HOH   A O     
5519 O  O     . HOH   K .   ? 0.59090 0.55775 0.48093 0.04441  0.02217  -0.02257 424 HOH   A O     
5520 O  O     . HOH   K .   ? 0.40201 0.30591 0.47362 -0.01501 -0.13818 -0.00666 425 HOH   A O     
5521 O  O     . HOH   K .   ? 0.62268 0.63825 0.61089 -0.01304 -0.00016 -0.00708 426 HOH   A O     
5522 O  O     . HOH   K .   ? 0.56799 0.60699 0.56594 0.00041  0.02809  -0.00969 427 HOH   A O     
5523 O  O     . HOH   K .   ? 0.61382 0.61743 0.81900 -0.03976 -0.08865 0.06162  428 HOH   A O     
5524 O  O     . HOH   K .   ? 0.54156 0.50766 0.76544 -0.04124 -0.13190 0.05372  429 HOH   A O     
5525 O  O     . HOH   K .   ? 0.60396 0.63647 0.87466 -0.03939 -0.07542 0.09108  430 HOH   A O     
5526 O  O     . HOH   K .   ? 0.60953 0.58665 0.62448 -0.00478 -0.03348 -0.01730 431 HOH   A O     
5527 O  O     . HOH   K .   ? 0.52950 0.57696 0.72013 -0.02618 -0.02998 0.06822  432 HOH   A O     
5528 O  O     . HOH   K .   ? 0.55820 0.59808 0.55657 -0.00276 0.02863  -0.00958 433 HOH   A O     
5529 O  O     . HOH   K .   ? 0.51955 0.51357 0.56990 -0.01394 -0.03347 -0.00195 434 HOH   A O     
5530 O  O     . HOH   K .   ? 0.60481 0.63378 0.58856 0.00637  0.03916  -0.00978 435 HOH   A O     
5531 O  O     . HOH   K .   ? 0.71714 0.59788 0.55556 0.07139  -0.04074 -0.05210 436 HOH   A O     
5532 O  O     . HOH   K .   ? 0.65073 0.63346 0.56137 0.03298  0.02599  -0.01926 437 HOH   A O     
5533 O  O     . HOH   K .   ? 0.57383 0.57431 0.51613 0.02068  0.02970  -0.01731 438 HOH   A O     
5534 O  O     . HOH   K .   ? 0.52770 0.50367 0.55270 -0.00804 -0.04081 -0.01296 439 HOH   A O     
5535 O  O     . HOH   K .   ? 0.55505 0.49597 0.67293 -0.02295 -0.11554 0.00963  440 HOH   A O     
5536 O  O     . HOH   K .   ? 0.69308 0.57202 0.50346 0.07353  -0.03585 -0.04761 441 HOH   A O     
5537 O  O     . HOH   K .   ? 0.49094 0.50506 0.49106 -0.01315 -0.00368 -0.00546 442 HOH   A O     
5538 O  O     . HOH   K .   ? 0.69680 0.62235 0.54459 0.05953  -0.00291 -0.03438 443 HOH   A O     
5539 O  O     . HOH   K .   ? 0.60797 0.52979 0.77544 -0.03009 -0.15485 0.02168  444 HOH   A O     
5540 O  O     . HOH   K .   ? 0.70305 0.52875 0.58340 0.04254  -0.13370 -0.05695 445 HOH   A O     
5541 O  O     . HOH   K .   ? 0.62697 0.73990 0.83677 0.00571  0.03962  0.12633  446 HOH   A O     
5542 O  O     . HOH   K .   ? 0.67365 0.63722 0.57432 0.02675  0.00136  -0.02680 447 HOH   A O     
5543 O  O     . HOH   K .   ? 0.51650 0.51740 0.50230 -0.00971 -0.01009 -0.01127 448 HOH   A O     
5544 O  O     . HOH   K .   ? 0.52368 0.52452 0.71746 -0.03364 -0.08133 0.05014  449 HOH   A O     
5545 O  O     . HOH   K .   ? 0.49375 0.58115 0.62410 0.00195  0.03449  0.07877  450 HOH   A O     
5546 O  O     . HOH   K .   ? 0.60458 0.59026 0.59029 -0.00934 -0.02561 -0.01289 451 HOH   A O     
5547 O  O     . HOH   K .   ? 0.54062 0.59971 0.59284 -0.00468 0.02649  0.02833  452 HOH   A O     
5548 O  O     . HOH   K .   ? 0.66698 0.51403 0.58680 0.03558  -0.12457 -0.05299 453 HOH   A O     
5549 O  O     . HOH   K .   ? 0.61811 0.50247 0.60231 0.01194  -0.11619 -0.03612 454 HOH   A O     
5550 O  O     . HOH   K .   ? 0.52630 0.57520 0.62076 -0.02150 -0.00517 0.04075  455 HOH   A O     
5551 O  O     . HOH   K .   ? 0.31806 0.36652 0.36371 -0.00991 0.01787  0.01766  456 HOH   A O     
5552 O  O     . HOH   K .   ? 0.60082 0.49437 0.56283 0.01834  -0.09517 -0.04041 457 HOH   A O     
5553 O  O     . HOH   K .   ? 0.51476 0.55814 0.52734 -0.00428 0.03229  -0.00436 458 HOH   A O     
5554 O  O     . HOH   K .   ? 0.43736 0.48688 0.45898 -0.00496 0.02678  0.00956  459 HOH   A O     
5555 O  O     . HOH   K .   ? 0.52424 0.51104 0.64451 -0.03341 -0.07953 0.03066  460 HOH   A O     
5556 O  O     . HOH   K .   ? 0.58651 0.54696 0.74866 -0.03055 -0.11236 0.02821  461 HOH   A O     
5557 O  O     . HOH   K .   ? 0.56287 0.61787 0.59337 -0.00356 0.02851  0.01791  462 HOH   A O     
5558 O  O     . HOH   K .   ? 0.36452 0.47886 0.71556 -0.02392 -0.01206 0.17013  463 HOH   A O     
5559 O  O     . HOH   K .   ? 0.58148 0.57441 0.78741 -0.03512 -0.09349 0.05105  464 HOH   A O     
5560 O  O     . HOH   L .   ? 0.70349 0.67098 0.57683 0.11755  0.08315  0.00423  301 HOH   B O     
5561 O  O     . HOH   L .   ? 0.74355 0.69870 0.58556 0.14005  0.09034  0.00892  302 HOH   B O     
5562 O  O     . HOH   L .   ? 0.66420 0.55345 0.65331 0.01887  -0.10357 -0.05001 303 HOH   B O     
5563 O  O     . HOH   L .   ? 0.64357 0.67648 0.63697 0.06505  0.09254  0.02889  304 HOH   B O     
5564 O  O     . HOH   L .   ? 0.69336 0.63161 0.59449 0.05828  0.00506  -0.04430 305 HOH   B O     
5565 O  O     . HOH   L .   ? 0.79310 0.65707 0.53240 0.16055  0.02414  -0.03795 306 HOH   B O     
5566 O  O     . HOH   L .   ? 0.41369 0.43188 0.42316 0.00608  0.03118  -0.02520 307 HOH   B O     
5567 O  O     . HOH   L .   ? 0.46813 0.51852 0.55265 -0.00511 0.01824  0.02670  308 HOH   B O     
5568 O  O     . HOH   L .   ? 0.50705 0.53571 0.54015 -0.00145 0.02157  -0.01241 309 HOH   B O     
5569 O  O     . HOH   L .   ? 0.46294 0.47286 0.50729 -0.01102 -0.01133 -0.00444 310 HOH   B O     
5570 O  O     . HOH   L .   ? 0.60280 0.60596 0.54299 0.08457  0.08636  0.01269  311 HOH   B O     
5571 O  O     . HOH   L .   ? 0.39799 0.42753 0.49159 -0.01230 -0.00479 0.01477  312 HOH   B O     
5572 O  O     . HOH   L .   ? 0.34940 0.37821 0.36539 0.00278  0.02766  -0.01858 313 HOH   B O     
5573 O  O     . HOH   L .   ? 0.35259 0.34724 0.32440 0.02952  0.03403  -0.02877 314 HOH   B O     
5574 O  O     . HOH   L .   ? 0.36586 0.37854 0.36114 0.02141  0.04220  -0.02051 315 HOH   B O     
5575 O  O     . HOH   L .   ? 0.75608 0.55245 0.56662 0.09433  -0.11387 -0.08052 316 HOH   B O     
5576 O  O     . HOH   L .   ? 0.69291 0.52497 0.60673 0.04974  -0.12895 -0.06870 317 HOH   B O     
5577 O  O     . HOH   L .   ? 0.53432 0.61083 0.65150 0.01044  0.03948  0.06311  318 HOH   B O     
5578 O  O     . HOH   L .   ? 0.73332 0.58932 0.53876 0.10254  -0.03806 -0.06295 319 HOH   B O     
5579 O  O     . HOH   L .   ? 0.50320 0.52727 0.51717 0.02168  0.05086  -0.01055 320 HOH   B O     
5580 O  O     . HOH   L .   ? 0.46622 0.51492 0.49248 0.01765  0.04040  0.01415  321 HOH   B O     
5581 O  O     . HOH   L .   ? 0.32190 0.32300 0.30441 0.01817  0.02859  -0.02871 322 HOH   B O     
5582 O  O     . HOH   L .   ? 0.63546 0.53175 0.60542 0.02083  -0.09058 -0.04574 323 HOH   B O     
5583 O  O     . HOH   L .   ? 0.46814 0.50377 0.53736 -0.00594 0.01262  0.00757  324 HOH   B O     
5584 O  O     . HOH   L .   ? 0.51051 0.53019 0.62094 -0.01756 -0.02407 0.01929  325 HOH   B O     
5585 O  O     . HOH   L .   ? 0.62777 0.58118 0.53918 0.06218  0.02440  -0.03820 326 HOH   B O     
5586 O  O     . HOH   L .   ? 0.49052 0.50933 0.50809 0.01027  0.03667  -0.02388 327 HOH   B O     
5587 O  O     . HOH   L .   ? 0.59059 0.57297 0.50306 0.08374  0.06905  -0.00445 328 HOH   B O     
5588 O  O     . HOH   L .   ? 0.56753 0.59222 0.59643 0.00225  0.02854  -0.02313 329 HOH   B O     
5589 O  O     . HOH   L .   ? 0.37837 0.40509 0.39902 0.00254  0.02659  -0.01990 330 HOH   B O     
5590 O  O     . HOH   L .   ? 0.56679 0.58701 0.58470 0.00678  0.03383  -0.02451 331 HOH   B O     
5591 O  O     . HOH   L .   ? 0.44345 0.47970 0.49494 0.00200  0.03397  -0.00673 332 HOH   B O     
5592 O  O     . HOH   L .   ? 0.34083 0.36875 0.35876 0.01223  0.04447  -0.01242 333 HOH   B O     
5593 O  O     . HOH   L .   ? 0.39018 0.41269 0.48519 -0.01469 -0.01428 0.01364  334 HOH   B O     
5594 O  O     . HOH   L .   ? 0.63693 0.66695 0.64912 -0.00326 0.02437  -0.01392 335 HOH   B O     
5595 O  O     . HOH   L .   ? 0.54791 0.57661 0.60344 -0.00541 0.01208  -0.00305 336 HOH   B O     
5596 O  O     . HOH   L .   ? 0.81016 0.62512 0.68674 0.06133  -0.13166 -0.06993 337 HOH   B O     
5597 O  O     . HOH   L .   ? 0.54578 0.58604 0.66084 -0.01448 -0.00472 0.03152  338 HOH   B O     
5598 O  O     . HOH   L .   ? 0.33977 0.32738 0.30755 0.03455  0.03263  -0.03281 339 HOH   B O     
5599 O  O     . HOH   L .   ? 0.41424 0.43244 0.42493 0.01138  0.03714  -0.02288 340 HOH   B O     
5600 O  O     . HOH   L .   ? 0.51395 0.54142 0.53120 0.02252  0.05381  -0.00633 341 HOH   B O     
5601 O  O     . HOH   L .   ? 0.62389 0.65288 0.63695 -0.00437 0.02176  -0.01252 342 HOH   B O     
5602 O  O     . HOH   L .   ? 0.50141 0.55792 0.57715 0.00647  0.03284  0.02983  343 HOH   B O     
5603 O  O     . HOH   L .   ? 0.50204 0.43059 0.47958 0.01387  -0.06122 -0.03801 344 HOH   B O     
5604 O  O     . HOH   L .   ? 0.51477 0.57372 0.62604 -0.00177 0.02160  0.04173  345 HOH   B O     
5605 O  O     . HOH   L .   ? 0.42097 0.35823 0.31081 0.06375  0.00943  -0.04109 346 HOH   B O     
5606 O  O     . HOH   L .   ? 0.53289 0.56759 0.56425 0.00501  0.04001  -0.00939 347 HOH   B O     
5607 O  O     . HOH   L .   ? 0.54085 0.57545 0.56511 -0.00544 0.02097  -0.00484 348 HOH   B O     
5608 O  O     . HOH   L .   ? 0.59417 0.59802 0.58202 0.00311  0.01129  -0.02283 349 HOH   B O     
5609 O  O     . HOH   L .   ? 0.63617 0.61016 0.51046 0.11256  0.08520  0.00932  350 HOH   B O     
5610 O  O     . HOH   L .   ? 0.37672 0.34127 0.32667 0.02885  0.00199  -0.04012 351 HOH   B O     
5611 O  O     . HOH   L .   ? 0.46216 0.49857 0.53997 -0.01085 0.00470  0.01554  352 HOH   B O     
5612 O  O     . HOH   L .   ? 0.75879 0.62854 0.50988 0.14446  0.01708  -0.03843 353 HOH   B O     
5613 O  O     . HOH   L .   ? 0.60617 0.64962 0.71928 0.00688  0.03984  0.01215  354 HOH   B O     
5614 O  O     . HOH   L .   ? 0.36330 0.35270 0.35101 0.01170  0.00902  -0.03528 355 HOH   B O     
5615 O  O     . HOH   L .   ? 0.51975 0.54758 0.56528 0.00107  0.02366  -0.01568 356 HOH   B O     
5616 O  O     . HOH   L .   ? 0.56739 0.60057 0.60467 0.00031  0.02912  -0.01234 357 HOH   B O     
5617 O  O     . HOH   L .   ? 0.64431 0.56743 0.44726 0.14758  0.06832  -0.00987 358 HOH   B O     
5618 O  O     . HOH   L .   ? 0.67252 0.60722 0.46571 0.16803  0.09521  0.01253  359 HOH   B O     
5619 O  O     . HOH   L .   ? 0.54185 0.55378 0.63660 -0.01442 -0.02261 0.00634  360 HOH   B O     
5620 O  O     . HOH   L .   ? 0.32972 0.34035 0.36265 -0.00526 0.00202  -0.01697 361 HOH   B O     
5621 O  O     . HOH   L .   ? 0.60326 0.57531 0.50948 0.07699  0.05463  -0.01598 362 HOH   B O     
5622 O  O     . HOH   L .   ? 0.52951 0.55265 0.54359 -0.00553 0.01503  -0.01250 363 HOH   B O     
5623 O  O     . HOH   L .   ? 0.63779 0.67069 0.64032 0.06095  0.08918  0.02522  364 HOH   B O     
5624 O  O     . HOH   L .   ? 0.55700 0.57738 0.65827 -0.01680 -0.02069 0.01705  365 HOH   B O     
5625 O  O     . HOH   L .   ? 0.57153 0.51944 0.46891 0.06994  0.02596  -0.03674 366 HOH   B O     
5626 O  O     . HOH   L .   ? 0.61054 0.64387 0.62605 -0.00185 0.02646  -0.01204 367 HOH   B O     
5627 O  O     . HOH   L .   ? 0.66552 0.58738 0.58924 0.04330  -0.02909 -0.05544 368 HOH   B O     
5628 O  O     . HOH   L .   ? 0.47758 0.51000 0.49067 0.00386  0.02879  -0.01412 369 HOH   B O     
5629 O  O     . HOH   L .   ? 0.55242 0.53637 0.51625 0.01289  0.00326  -0.02822 370 HOH   B O     
5630 O  O     . HOH   L .   ? 0.33936 0.36796 0.35445 0.00186  0.02773  -0.01963 371 HOH   B O     
5631 O  O     . HOH   L .   ? 0.50665 0.48058 0.47716 0.01933  0.00132  -0.03930 372 HOH   B O     
5632 O  O     . HOH   L .   ? 0.80806 0.67397 0.53078 0.17631  0.03985  -0.02818 373 HOH   B O     
5633 O  O     . HOH   L .   ? 0.38085 0.37791 0.41591 -0.00506 -0.01208 -0.02014 374 HOH   B O     
5634 O  O     . HOH   L .   ? 0.41984 0.45033 0.44590 0.01505  0.04870  -0.00803 375 HOH   B O     
5635 O  O     . HOH   L .   ? 0.72952 0.54852 0.47904 0.13099  -0.04862 -0.06843 376 HOH   B O     
5636 O  O     . HOH   L .   ? 0.48869 0.54356 0.55552 0.00025  0.02800  0.02585  377 HOH   B O     
5637 O  O     . HOH   L .   ? 0.42801 0.47547 0.53758 -0.00854 0.00857  0.03170  378 HOH   B O     
5638 O  O     . HOH   L .   ? 0.51533 0.51764 0.56892 -0.00792 -0.01349 -0.01460 379 HOH   B O     
5639 O  O     . HOH   L .   ? 0.49965 0.52740 0.52016 0.00173  0.02673  -0.02022 380 HOH   B O     
5640 O  O     . HOH   L .   ? 0.58982 0.55187 0.54857 0.02536  -0.00459 -0.04309 381 HOH   B O     
5641 O  O     . HOH   L .   ? 0.65281 0.48240 0.71766 0.00652  -0.20231 -0.03812 382 HOH   B O     
5642 O  O     . HOH   L .   ? 0.57062 0.60500 0.59853 0.00235  0.03627  -0.01153 383 HOH   B O     
5643 O  O     . HOH   L .   ? 0.77902 0.67685 0.53480 0.17638  0.06859  -0.01088 384 HOH   B O     
5644 O  O     . HOH   L .   ? 0.33162 0.35967 0.35053 0.00319  0.02730  -0.01857 385 HOH   B O     
5645 O  O     . HOH   L .   ? 0.58675 0.48898 0.53772 0.03058  -0.06931 -0.05575 386 HOH   B O     
5646 O  O     . HOH   L .   ? 0.48407 0.50796 0.50372 0.00156  0.02667  -0.02418 387 HOH   B O     
5647 O  O     . HOH   L .   ? 0.67852 0.63048 0.70575 0.00144  -0.05362 -0.03374 388 HOH   B O     
5648 O  O     . HOH   L .   ? 0.77662 0.58648 0.57534 0.10116  -0.09073 -0.07752 389 HOH   B O     
5649 O  O     . HOH   L .   ? 0.47337 0.42080 0.36834 0.06975  0.02530  -0.03611 390 HOH   B O     
5650 O  O     . HOH   L .   ? 0.33150 0.36467 0.34622 0.00687  0.02992  -0.01141 391 HOH   B O     
5651 O  O     . HOH   L .   ? 0.39597 0.42108 0.41599 0.00239  0.02689  -0.02320 392 HOH   B O     
5652 O  O     . HOH   L .   ? 0.50577 0.52384 0.52684 -0.00012 0.02094  -0.02572 393 HOH   B O     
5653 O  O     . HOH   L .   ? 0.54953 0.53354 0.55395 0.00501  -0.00714 -0.03464 394 HOH   B O     
5654 O  O     . HOH   L .   ? 0.34225 0.35744 0.35381 0.00599  0.02893  -0.02836 395 HOH   B O     
5655 O  O     . HOH   L .   ? 0.76425 0.54815 0.53806 0.11106  -0.10795 -0.08186 396 HOH   B O     
5656 O  O     . HOH   L .   ? 0.51874 0.58002 0.63901 -0.00463 0.01830  0.04746  397 HOH   B O     
5657 O  O     . HOH   L .   ? 0.53398 0.55380 0.52584 0.00881  0.03475  -0.01845 398 HOH   B O     
5658 O  O     . HOH   L .   ? 0.46234 0.47890 0.43601 0.06263  0.07928  0.01027  399 HOH   B O     
5659 O  O     A HOH   L .   ? 0.36416 0.38646 0.38604 0.00033  0.02390  -0.02363 400 HOH   B O     
5660 O  O     B HOH   L .   ? 0.40455 0.42677 0.42429 0.00094  0.02558  -0.02497 400 HOH   B O     
5661 O  O     . HOH   L .   ? 0.55074 0.53658 0.59823 -0.00566 -0.02613 -0.02327 401 HOH   B O     
5662 O  O     . HOH   L .   ? 0.48056 0.48401 0.51029 -0.00332 -0.00075 -0.02335 402 HOH   B O     
5663 O  O     . HOH   L .   ? 0.67252 0.64869 0.56978 0.07577  0.05755  -0.00947 403 HOH   B O     
5664 O  O     . HOH   L .   ? 0.68392 0.65630 0.56614 0.09517  0.07012  -0.00175 404 HOH   B O     
5665 O  O     . HOH   L .   ? 0.50065 0.51915 0.53376 -0.00425 0.01128  -0.01649 405 HOH   B O     
5666 O  O     . HOH   L .   ? 0.62326 0.60683 0.56419 0.05874  0.04972  -0.02114 406 HOH   B O     
5667 O  O     . HOH   L .   ? 0.54992 0.57650 0.56981 0.03779  0.06628  0.00172  407 HOH   B O     
5668 O  O     . HOH   L .   ? 0.57616 0.64047 0.64207 0.01866  0.04536  0.04001  408 HOH   B O     
5669 O  O     . HOH   L .   ? 0.53334 0.49120 0.54463 0.00503  -0.03947 -0.03685 409 HOH   B O     
5670 O  O     . HOH   L .   ? 0.54007 0.55263 0.52147 0.01128  0.03094  -0.02062 410 HOH   B O     
5671 O  O     . HOH   L .   ? 0.56783 0.50953 0.49307 0.04704  -0.00234 -0.05027 411 HOH   B O     
5672 O  O     . HOH   L .   ? 0.55059 0.58739 0.59140 -0.00854 0.01481  0.00459  412 HOH   B O     
5673 O  O     . HOH   L .   ? 0.54121 0.57079 0.55851 0.00056  0.02966  -0.01911 413 HOH   B O     
5674 O  O     . HOH   L .   ? 0.65771 0.63504 0.55793 0.09633  0.07474  -0.00135 414 HOH   B O     
5675 O  O     . HOH   L .   ? 0.68472 0.69817 0.67484 0.00323  0.02168  -0.02130 415 HOH   B O     
5676 O  O     . HOH   L .   ? 0.64319 0.48978 0.68596 0.00848  -0.17569 -0.03858 416 HOH   B O     
5677 O  O     . HOH   L .   ? 0.79681 0.72385 0.57442 0.18199  0.09916  0.01414  417 HOH   B O     
5678 O  O     . HOH   L .   ? 0.83309 0.63269 0.58632 0.12563  -0.07526 -0.07672 418 HOH   B O     
5679 O  O     . HOH   L .   ? 0.63661 0.68392 0.69296 -0.00620 0.02008  0.01683  419 HOH   B O     
5680 O  O     . HOH   L .   ? 0.45436 0.47596 0.46979 0.00838  0.03647  -0.02174 420 HOH   B O     
5681 O  O     . HOH   L .   ? 0.78182 0.64106 0.52571 0.15814  0.01660  -0.04407 421 HOH   B O     
5682 O  O     . HOH   L .   ? 0.56906 0.60012 0.61058 0.00593  0.03842  -0.01282 422 HOH   B O     
5683 O  O     . HOH   L .   ? 0.55495 0.58643 0.58043 0.00028  0.02806  -0.01590 423 HOH   B O     
5684 O  O     . HOH   L .   ? 0.59362 0.62435 0.62635 0.01084  0.04446  -0.01059 424 HOH   B O     
5685 O  O     . HOH   L .   ? 0.51550 0.52845 0.58819 -0.00995 -0.00980 -0.00505 425 HOH   B O     
5686 O  O     . HOH   L .   ? 0.42645 0.43338 0.46936 -0.00693 -0.00599 -0.01465 426 HOH   B O     
5687 O  O     . HOH   L .   ? 0.46982 0.49626 0.49367 0.00236  0.02364  -0.01977 427 HOH   B O     
5688 O  O     . HOH   L .   ? 0.55879 0.58139 0.58377 0.00302  0.02557  -0.02510 428 HOH   B O     
5689 O  O     . HOH   L .   ? 0.61198 0.63932 0.66860 0.00097  0.02193  -0.01389 429 HOH   B O     
5690 O  O     . HOH   L .   ? 0.59272 0.63147 0.59039 0.07905  0.10724  0.04405  430 HOH   B O     
5691 O  O     . HOH   L .   ? 0.56330 0.58745 0.58116 0.01314  0.04301  -0.01617 431 HOH   B O     
5692 O  O     . HOH   L .   ? 0.83948 0.60233 0.60874 0.11406  -0.12904 -0.08785 432 HOH   B O     
5693 O  O     . HOH   L .   ? 0.54733 0.57271 0.57435 0.00510  0.03493  -0.02061 433 HOH   B O     
5694 O  O     . HOH   L .   ? 0.53647 0.55645 0.59298 -0.00781 0.00221  -0.00626 434 HOH   B O     
5695 O  O     . HOH   L .   ? 0.56087 0.57648 0.60203 -0.00541 0.00561  -0.01525 435 HOH   B O     
5696 O  O     . HOH   L .   ? 0.72041 0.54901 0.49591 0.11737  -0.05263 -0.06953 436 HOH   B O     
5697 O  O     . HOH   L .   ? 0.47986 0.48446 0.51854 -0.00549 -0.00483 -0.01875 437 HOH   B O     
5698 O  O     . HOH   L .   ? 0.81539 0.67446 0.50524 0.20704  0.05879  -0.01688 438 HOH   B O     
5699 O  O     . HOH   L .   ? 0.78791 0.60298 0.53789 0.13132  -0.05296 -0.07081 439 HOH   B O     
5700 O  O     . HOH   M .   ? 0.58367 0.58926 0.61194 0.00829  0.01877  -0.03984 301 HOH   C O     
5701 O  O     . HOH   M .   ? 0.52131 0.51239 0.46274 0.08959  0.08051  0.00045  302 HOH   C O     
5702 O  O     . HOH   M .   ? 0.58992 0.60725 0.61804 0.06165  0.07886  0.00377  303 HOH   C O     
5703 O  O     . HOH   M .   ? 0.49585 0.53112 0.68416 -0.00031 0.01276  0.02106  304 HOH   C O     
5704 O  O     . HOH   M .   ? 0.30359 0.31783 0.30023 0.06475  0.07918  0.00497  305 HOH   C O     
5705 O  O     . HOH   M .   ? 0.44552 0.51083 0.69963 0.01196  0.04460  0.06325  306 HOH   C O     
5706 O  O     . HOH   M .   ? 0.34570 0.38237 0.40473 0.03851  0.07254  0.01302  307 HOH   C O     
5707 O  O     . HOH   M .   ? 0.59040 0.59987 0.53946 0.13543  0.12821  0.04518  308 HOH   C O     
5708 O  O     . HOH   M .   ? 0.43597 0.46054 0.47068 0.01585  0.04583  -0.01485 309 HOH   C O     
5709 O  O     . HOH   M .   ? 0.51597 0.56160 0.54681 0.10371  0.12936  0.06324  310 HOH   C O     
5710 O  O     . HOH   M .   ? 0.51109 0.52280 0.62386 0.00400  0.01672  -0.02189 311 HOH   C O     
5711 O  O     . HOH   M .   ? 0.45941 0.45176 0.52727 0.00661  0.00081  -0.04100 312 HOH   C O     
5712 O  O     . HOH   M .   ? 0.47111 0.50313 0.73450 -0.00096 0.00294  0.03384  313 HOH   C O     
5713 O  O     . HOH   M .   ? 0.61637 0.62102 0.62220 0.02279  0.01959  -0.03038 314 HOH   C O     
5714 O  O     . HOH   M .   ? 0.55746 0.57672 0.58112 0.00700  0.03355  -0.02605 315 HOH   C O     
5715 O  O     . HOH   M .   ? 0.48869 0.50683 0.50806 0.00472  0.02994  -0.02804 316 HOH   C O     
5716 O  O     . HOH   M .   ? 0.49553 0.46373 0.46429 0.03111  0.01163  -0.05024 317 HOH   C O     
5717 O  O     . HOH   M .   ? 0.50117 0.52832 0.66930 -0.00056 0.00849  0.00944  318 HOH   C O     
5718 O  O     . HOH   M .   ? 0.30721 0.33519 0.38858 0.00570  0.03263  -0.01114 319 HOH   C O     
5719 O  O     . HOH   M .   ? 0.58234 0.57576 0.58154 0.02399  0.03040  -0.04009 320 HOH   C O     
5720 O  O     . HOH   M .   ? 0.43315 0.45104 0.47109 0.00350  0.02372  -0.02849 321 HOH   C O     
5721 O  O     . HOH   M .   ? 0.53508 0.55028 0.55464 0.01081  0.02351  -0.02855 322 HOH   C O     
5722 O  O     . HOH   M .   ? 0.35953 0.38507 0.45637 0.00446  0.02722  -0.01073 323 HOH   C O     
5723 O  O     . HOH   M .   ? 0.58525 0.59028 0.64160 0.00483  0.01992  -0.04052 324 HOH   C O     
5724 O  O     . HOH   M .   ? 0.62187 0.62222 0.54556 0.13882  0.12435  0.04053  325 HOH   C O     
5725 O  O     . HOH   M .   ? 0.66653 0.61079 0.68307 0.03456  -0.03466 -0.05488 326 HOH   C O     
5726 O  O     . HOH   M .   ? 0.51132 0.51333 0.44605 0.14680  0.13080  0.04427  327 HOH   C O     
5727 O  O     . HOH   M .   ? 0.40315 0.41014 0.42838 0.00328  0.02013  -0.03958 328 HOH   C O     
5728 O  O     . HOH   M .   ? 0.53352 0.54025 0.56119 0.00365  0.02092  -0.04088 329 HOH   C O     
5729 O  O     . HOH   M .   ? 0.33939 0.37174 0.36831 0.07879  0.10194  0.03211  330 HOH   C O     
5730 O  O     . HOH   M .   ? 0.44150 0.46619 0.54351 0.00237  0.02093  -0.00925 331 HOH   C O     
5731 O  O     . HOH   M .   ? 0.37474 0.35911 0.33023 0.04775  0.04139  -0.02845 332 HOH   C O     
5732 O  O     . HOH   M .   ? 0.50488 0.60160 0.76936 0.04857  0.10226  0.10918  333 HOH   C O     
5733 O  O     . HOH   M .   ? 0.31376 0.32479 0.36281 0.00473  0.01529  -0.03029 334 HOH   C O     
5734 O  O     . HOH   M .   ? 0.47472 0.54472 0.63625 0.05981  0.10514  0.06991  335 HOH   C O     
5735 O  O     . HOH   M .   ? 0.47040 0.44180 0.40473 0.08195  0.05843  -0.02396 336 HOH   C O     
5736 O  O     . HOH   M .   ? 0.62078 0.55654 0.52290 0.06928  0.01362  -0.04956 337 HOH   C O     
5737 O  O     . HOH   M .   ? 0.45209 0.49724 0.71411 -0.00242 0.00666  0.04799  338 HOH   C O     
5738 O  O     . HOH   M .   ? 0.49441 0.50226 0.53098 0.00767  0.01267  -0.03191 339 HOH   C O     
5739 O  O     . HOH   M .   ? 0.38041 0.39552 0.36816 0.07633  0.08864  0.01376  340 HOH   C O     
5740 O  O     . HOH   M .   ? 0.38789 0.41799 0.59855 -0.00223 0.00238  0.02258  341 HOH   C O     
5741 O  O     . HOH   M .   ? 0.45583 0.49985 0.73733 -0.00284 0.00325  0.05131  342 HOH   C O     
5742 O  O     . HOH   M .   ? 0.32728 0.32244 0.29326 0.07435  0.07218  -0.00762 343 HOH   C O     
5743 O  O     . HOH   M .   ? 0.41605 0.37217 0.31389 0.10660  0.06417  -0.02088 344 HOH   C O     
5744 O  O     . HOH   M .   ? 0.50487 0.50210 0.51455 0.01575  0.02628  -0.04186 345 HOH   C O     
5745 O  O     . HOH   M .   ? 0.30260 0.35004 0.40247 0.04077  0.07923  0.02870  346 HOH   C O     
5746 O  O     . HOH   M .   ? 0.60463 0.58661 0.59686 0.01755  0.01191  -0.04755 347 HOH   C O     
5747 O  O     . HOH   M .   ? 0.46934 0.42867 0.40913 0.05047  0.02054  -0.04595 348 HOH   C O     
5748 O  O     . HOH   M .   ? 0.52427 0.53287 0.74728 -0.00432 -0.02102 0.01004  349 HOH   C O     
5749 O  O     . HOH   M .   ? 0.57179 0.59247 0.60297 0.00399  0.03015  -0.02673 350 HOH   C O     
5750 O  O     . HOH   M .   ? 0.55439 0.56624 0.58027 0.00837  0.02186  -0.03335 351 HOH   C O     
5751 O  O     . HOH   M .   ? 0.42767 0.51508 0.61463 0.07354  0.12511  0.10004  352 HOH   C O     
5752 O  O     . HOH   M .   ? 0.32822 0.37453 0.53241 0.01373  0.04263  0.03199  353 HOH   C O     
5753 O  O     . HOH   M .   ? 0.36222 0.34696 0.42301 0.01129  -0.01357 -0.03653 354 HOH   C O     
5754 O  O     . HOH   M .   ? 0.64218 0.63532 0.55980 0.13957  0.11923  0.03307  355 HOH   C O     
5755 O  O     . HOH   M .   ? 0.52959 0.46384 0.38867 0.12147  0.05619  -0.02675 356 HOH   C O     
5756 O  O     . HOH   M .   ? 0.52695 0.52821 0.46927 0.10337  0.09890  0.01947  357 HOH   C O     
5757 O  O     . HOH   M .   ? 0.39997 0.39674 0.41899 0.00096  0.00171  -0.03280 358 HOH   C O     
5758 O  O     . HOH   M .   ? 0.35507 0.33586 0.30004 0.07136  0.05799  -0.02057 359 HOH   C O     
5759 O  O     . HOH   M .   ? 0.55965 0.54378 0.47336 0.12126  0.09879  0.01391  360 HOH   C O     
5760 O  O     . HOH   M .   ? 0.57883 0.54074 0.57951 0.03523  -0.01698 -0.04732 361 HOH   C O     
5761 O  O     . HOH   M .   ? 0.54544 0.55464 0.64768 0.00162  0.00092  -0.01780 362 HOH   C O     
5762 O  O     . HOH   M .   ? 0.51393 0.49661 0.57782 0.01002  -0.00857 -0.04388 363 HOH   C O     
5763 O  O     . HOH   M .   ? 0.46495 0.44623 0.46142 0.01179  0.00247  -0.04458 364 HOH   C O     
5764 O  O     . HOH   M .   ? 0.63981 0.57616 0.53181 0.08210  0.02575  -0.04477 365 HOH   C O     
5765 O  O     . HOH   M .   ? 0.44622 0.46389 0.46746 0.00738  0.02393  -0.02816 366 HOH   C O     
5766 O  O     . HOH   M .   ? 0.32231 0.35821 0.53221 0.00074  0.01374  0.02538  367 HOH   C O     
5767 O  O     . HOH   M .   ? 0.40057 0.39462 0.38596 0.04764  0.05070  -0.02601 368 HOH   C O     
5768 O  O     . HOH   M .   ? 0.40948 0.38509 0.48982 0.01029  -0.02293 -0.03954 369 HOH   C O     
5769 O  O     . HOH   M .   ? 0.48214 0.50343 0.50540 0.00232  0.02489  -0.02601 370 HOH   C O     
5770 O  O     . HOH   M .   ? 0.48875 0.48557 0.62939 0.00098  -0.00934 -0.02208 371 HOH   C O     
5771 O  O     . HOH   M .   ? 0.44385 0.47531 0.69621 -0.00161 0.00181  0.03165  372 HOH   C O     
5772 O  O     . HOH   M .   ? 0.47085 0.45737 0.47644 0.00500  -0.00380 -0.03542 373 HOH   C O     
5773 O  O     . HOH   M .   ? 0.55786 0.60393 0.59042 0.12123  0.14224  0.07340  374 HOH   C O     
5774 O  O     . HOH   M .   ? 0.46066 0.53005 0.70578 0.02631  0.06626  0.06742  375 HOH   C O     
5775 O  O     . HOH   M .   ? 0.37927 0.42333 0.46321 0.03074  0.06915  0.01856  376 HOH   C O     
5776 O  O     . HOH   M .   ? 0.41468 0.48307 0.59860 0.04387  0.08871  0.06297  377 HOH   C O     
5777 O  O     . HOH   M .   ? 0.41346 0.42278 0.44929 0.01320  0.03404  -0.03396 378 HOH   C O     
5778 O  O     . HOH   M .   ? 0.61291 0.69374 0.74638 0.08038  0.12982  0.09292  379 HOH   C O     
5779 O  O     . HOH   M .   ? 0.44123 0.44073 0.49709 0.00539  0.01195  -0.04252 380 HOH   C O     
5780 O  O     . HOH   M .   ? 0.55253 0.61350 0.76366 0.02852  0.06737  0.05249  381 HOH   C O     
5781 O  O     . HOH   M .   ? 0.34144 0.34593 0.32335 0.07840  0.08240  0.00278  382 HOH   C O     
5782 O  O     . HOH   M .   ? 0.56640 0.56032 0.49549 0.12999  0.11264  0.02664  383 HOH   C O     
5783 O  O     . HOH   M .   ? 0.34342 0.36565 0.37482 0.00150  0.02228  -0.02186 384 HOH   C O     
5784 O  O     . HOH   M .   ? 0.64667 0.70796 0.71633 0.09452  0.13154  0.07593  385 HOH   C O     
5785 O  O     . HOH   M .   ? 0.49243 0.53371 0.60845 0.04216  0.07609  0.02286  386 HOH   C O     
5786 O  O     . HOH   M .   ? 0.38095 0.38791 0.43214 0.00481  0.02153  -0.03940 387 HOH   C O     
5787 O  O     . HOH   M .   ? 0.57400 0.60489 0.56809 0.13429  0.14202  0.06509  388 HOH   C O     
5788 O  O     . HOH   M .   ? 0.45214 0.43949 0.45381 0.00903  0.00526  -0.04167 389 HOH   C O     
5789 O  O     . HOH   M .   ? 0.61174 0.64048 0.60130 0.10799  0.12187  0.04847  390 HOH   C O     
5790 O  O     . HOH   M .   ? 0.51574 0.56922 0.59880 0.09736  0.12799  0.06671  391 HOH   C O     
5791 O  O     . HOH   M .   ? 0.35226 0.34383 0.34237 0.02508  0.02887  -0.03880 392 HOH   C O     
5792 O  O     . HOH   M .   ? 0.42549 0.45218 0.64921 -0.00235 -0.00104 0.02212  393 HOH   C O     
5793 O  O     . HOH   M .   ? 0.58746 0.63262 0.66274 0.03424  0.07327  0.02145  394 HOH   C O     
5794 O  O     . HOH   M .   ? 0.53960 0.56126 0.60908 0.00265  0.02224  -0.01870 395 HOH   C O     
5795 O  O     . HOH   M .   ? 0.58721 0.55714 0.49297 0.09990  0.07097  -0.01002 396 HOH   C O     
5796 O  O     . HOH   M .   ? 0.50270 0.52286 0.52700 0.00050  0.02257  -0.02537 397 HOH   C O     
5797 O  O     . HOH   M .   ? 0.51577 0.55563 0.57467 0.04151  0.07696  0.01871  398 HOH   C O     
5798 O  O     . HOH   M .   ? 0.49269 0.53505 0.71116 0.00037  0.01570  0.03404  399 HOH   C O     
5799 O  O     . HOH   M .   ? 0.33449 0.31389 0.29135 0.06199  0.04966  -0.02921 400 HOH   C O     
5800 O  O     . HOH   M .   ? 0.62997 0.62042 0.71554 0.00645  -0.01622 -0.02825 401 HOH   C O     
5801 O  O     . HOH   M .   ? 0.50315 0.53056 0.58604 0.00406  0.02891  -0.01126 402 HOH   C O     
5802 O  O     . HOH   M .   ? 0.57399 0.53774 0.66489 0.01232  -0.04130 -0.03749 403 HOH   C O     
5803 O  O     . HOH   M .   ? 0.59919 0.61811 0.74060 0.00496  0.02047  -0.00929 404 HOH   C O     
5804 O  O     . HOH   M .   ? 0.63736 0.56342 0.53014 0.07082  0.00489  -0.05275 405 HOH   C O     
5805 O  O     A HOH   M .   ? 0.46273 0.41400 0.46527 0.03750  -0.02429 -0.05260 406 HOH   C O     
5806 O  O     B HOH   M .   ? 0.47683 0.41542 0.46975 0.04476  -0.03343 -0.05558 406 HOH   C O     
5807 O  O     . HOH   M .   ? 0.52200 0.60223 0.67832 0.08372  0.13094  0.09427  407 HOH   C O     
5808 O  O     . HOH   M .   ? 0.51395 0.47101 0.59938 0.01488  -0.04531 -0.04123 408 HOH   C O     
5809 O  O     . HOH   M .   ? 0.57536 0.54857 0.65231 0.01124  -0.02319 -0.04200 409 HOH   C O     
5810 O  O     . HOH   M .   ? 0.51864 0.50098 0.50349 0.02792  0.02351  -0.04528 410 HOH   C O     
5811 O  O     . HOH   M .   ? 0.53714 0.54718 0.56591 0.00243  0.01992  -0.03730 411 HOH   C O     
5812 O  O     . HOH   M .   ? 0.47035 0.40538 0.33506 0.11767  0.05388  -0.02908 412 HOH   C O     
5813 O  O     . HOH   M .   ? 0.36203 0.39885 0.59698 -0.00142 0.00674  0.03324  413 HOH   C O     
5814 O  O     . HOH   M .   ? 0.43220 0.42563 0.49488 0.00651  0.00421  -0.04300 414 HOH   C O     
5815 O  O     . HOH   M .   ? 0.53764 0.53535 0.72310 -0.00304 -0.03098 -0.00174 415 HOH   C O     
5816 O  O     . HOH   M .   ? 0.56324 0.58338 0.58443 0.00918  0.02569  -0.02421 416 HOH   C O     
5817 O  O     . HOH   M .   ? 0.55327 0.53107 0.56031 0.00517  -0.01397 -0.03691 417 HOH   C O     
5818 O  O     . HOH   M .   ? 0.54936 0.63522 0.74033 0.07172  0.12246  0.09747  418 HOH   C O     
5819 O  O     . HOH   M .   ? 0.70200 0.71871 0.65892 0.12703  0.12762  0.04865  419 HOH   C O     
5820 O  O     . HOH   M .   ? 0.60425 0.60986 0.63268 0.00507  0.02250  -0.04184 420 HOH   C O     
5821 O  O     . HOH   M .   ? 0.54875 0.56267 0.59388 -0.00552 0.00358  -0.01600 421 HOH   C O     
5822 O  O     . HOH   M .   ? 0.55575 0.63751 0.83566 0.03029  0.07398  0.08852  422 HOH   C O     
5823 O  O     . HOH   M .   ? 0.63137 0.65372 0.68664 0.00308  0.02584  -0.02133 423 HOH   C O     
5824 O  O     . HOH   M .   ? 0.57969 0.54051 0.63654 0.01839  -0.02922 -0.04900 424 HOH   C O     
5825 O  O     . HOH   M .   ? 0.63473 0.58556 0.58309 0.03345  -0.00703 -0.04949 425 HOH   C O     
5826 O  O     . HOH   M .   ? 0.49557 0.56613 0.70294 0.03968  0.08418  0.06685  426 HOH   C O     
5827 O  O     . HOH   M .   ? 0.57306 0.49557 0.43245 0.10879  0.03491  -0.04161 427 HOH   C O     
5828 O  O     . HOH   M .   ? 0.65995 0.63850 0.55685 0.14118  0.10899  0.02066  428 HOH   C O     
5829 O  O     . HOH   M .   ? 0.61713 0.60489 0.56262 0.11117  0.09381  0.00600  429 HOH   C O     
5830 O  O     . HOH   M .   ? 0.66451 0.61725 0.59582 0.05603  0.01919  -0.04813 430 HOH   C O     
5831 O  O     . HOH   M .   ? 0.48536 0.45150 0.57822 0.01110  -0.03663 -0.03879 431 HOH   C O     
5832 O  O     . HOH   M .   ? 0.66949 0.62979 0.54472 0.13345  0.08842  0.00140  432 HOH   C O     
5833 O  O     . HOH   M .   ? 0.61615 0.61821 0.66189 0.00474  0.01754  -0.04480 433 HOH   C O     
5834 O  O     . HOH   M .   ? 0.52524 0.54278 0.52574 0.04218  0.06373  -0.00440 434 HOH   C O     
5835 O  O     . HOH   M .   ? 0.60374 0.62331 0.62037 0.01541  0.02730  -0.02115 435 HOH   C O     
5836 O  O     . HOH   M .   ? 0.67540 0.58213 0.51346 0.11612  0.02571  -0.04663 436 HOH   C O     
5837 O  O     . HOH   M .   ? 0.59872 0.57374 0.52837 0.10254  0.07722  -0.00984 437 HOH   C O     
5838 O  O     . HOH   M .   ? 0.67369 0.61059 0.50347 0.15791  0.08701  -0.00186 438 HOH   C O     
5839 O  O     . HOH   N .   ? 0.43122 0.47465 0.42413 -0.01102 0.02282  -0.00121 301 HOH   D O     
5840 O  O     . HOH   N .   ? 0.31152 0.35992 0.30680 0.01146  0.05638  0.01530  302 HOH   D O     
5841 O  O     . HOH   N .   ? 0.56403 0.59560 0.59849 -0.00409 0.00398  -0.00533 303 HOH   D O     
5842 O  O     . HOH   N .   ? 0.57611 0.56453 0.49461 0.01123  0.00985  -0.01997 304 HOH   D O     
5843 O  O     . HOH   N .   ? 0.47553 0.50533 0.55505 -0.00998 -0.01825 0.00780  305 HOH   D O     
5844 O  O     . HOH   N .   ? 0.55791 0.52721 0.42014 0.05591  0.03710  -0.01258 306 HOH   D O     
5845 O  O     . HOH   N .   ? 0.25075 0.28536 0.21629 0.00531  0.04256  -0.00135 307 HOH   D O     
5846 O  O     . HOH   N .   ? 0.62336 0.67179 0.60269 -0.01389 0.02399  -0.00324 308 HOH   D O     
5847 O  O     . HOH   N .   ? 0.53223 0.52700 0.45040 0.01525  0.02026  -0.01705 309 HOH   D O     
5848 O  O     . HOH   N .   ? 0.35281 0.35043 0.29604 0.02530  -0.02447 -0.02020 310 HOH   D O     
5849 O  O     A HOH   N .   ? 0.37615 0.41714 0.37165 -0.01074 0.02195  -0.00224 311 HOH   D O     
5850 O  O     B HOH   N .   ? 0.28078 0.32231 0.27132 -0.01014 0.02387  -0.00410 311 HOH   D O     
5851 O  O     . HOH   N .   ? 0.37345 0.42928 0.35367 -0.00183 0.02895  0.00898  312 HOH   D O     
5852 O  O     . HOH   N .   ? 0.61163 0.61382 0.54090 0.01194  0.02323  -0.01549 313 HOH   D O     
5853 O  O     . HOH   N .   ? 0.38968 0.43339 0.37405 0.02298  0.06470  0.01835  314 HOH   D O     
5854 O  O     . HOH   N .   ? 0.55866 0.54307 0.48417 0.04123  -0.02557 -0.02312 315 HOH   D O     
5855 O  O     . HOH   N .   ? 0.67647 0.67914 0.58279 0.01695  0.03044  -0.01085 316 HOH   D O     
5856 O  O     . HOH   N .   ? 0.50387 0.57962 0.66389 -0.00820 0.02700  0.05956  317 HOH   D O     
5857 O  O     . HOH   N .   ? 0.56045 0.58467 0.55159 -0.00323 -0.01565 -0.00996 318 HOH   D O     
5858 O  O     . HOH   N .   ? 0.36337 0.40025 0.31918 0.00323  0.04237  0.00163  319 HOH   D O     
5859 O  O     . HOH   N .   ? 0.47868 0.51669 0.45792 0.01195  0.05104  0.00446  320 HOH   D O     
5860 O  O     . HOH   N .   ? 0.64978 0.69663 0.61945 -0.01434 0.02314  -0.00593 321 HOH   D O     
5861 O  O     . HOH   N .   ? 0.56659 0.57883 0.46977 0.06075  0.07622  0.01983  322 HOH   D O     
5862 O  O     . HOH   N .   ? 0.55878 0.60176 0.52302 -0.00562 0.01393  -0.00739 323 HOH   D O     
5863 O  O     . HOH   N .   ? 0.49034 0.54773 0.48556 0.03889  0.08650  0.04612  324 HOH   D O     
5864 O  O     . HOH   N .   ? 0.48027 0.50412 0.43647 -0.01015 0.01642  -0.01108 325 HOH   D O     
5865 O  O     . HOH   N .   ? 0.52655 0.57481 0.49889 -0.01315 0.02274  -0.00259 326 HOH   D O     
5866 O  O     . HOH   N .   ? 0.50652 0.57911 0.59855 0.00528  0.05516  0.04592  327 HOH   D O     
5867 O  O     . HOH   N .   ? 0.32890 0.37429 0.28642 0.03152  0.03618  0.01249  328 HOH   D O     
5868 O  O     . HOH   N .   ? 0.59592 0.59072 0.50638 0.01193  0.01780  -0.01685 329 HOH   D O     
5869 O  O     . HOH   N .   ? 0.37991 0.45902 0.45135 0.00774  0.06320  0.05558  330 HOH   D O     
5870 O  O     . HOH   N .   ? 0.58979 0.60353 0.53488 0.02762  0.00257  -0.01371 331 HOH   D O     
5871 O  O     . HOH   N .   ? 0.39471 0.44619 0.48269 -0.00944 0.01485  0.02006  332 HOH   D O     
5872 O  O     . HOH   N .   ? 0.52155 0.53839 0.58048 -0.00414 -0.02553 -0.00277 333 HOH   D O     
5873 O  O     . HOH   N .   ? 0.37881 0.43932 0.35293 0.02888  0.04456  0.02792  334 HOH   D O     
5874 O  O     . HOH   N .   ? 0.47953 0.53445 0.60133 -0.01855 -0.00833 0.03544  335 HOH   D O     
5875 O  O     . HOH   N .   ? 0.51451 0.54476 0.51298 0.00147  0.01023  -0.01180 336 HOH   D O     
5876 O  O     . HOH   N .   ? 0.28501 0.32052 0.24983 0.02376  0.06051  0.01185  337 HOH   D O     
5877 O  O     . HOH   N .   ? 0.54137 0.60568 0.64208 -0.00403 0.03517  0.03474  338 HOH   D O     
5878 O  O     . HOH   N .   ? 0.35354 0.41302 0.42027 -0.01550 0.01410  0.02477  339 HOH   D O     
5879 O  O     . HOH   N .   ? 0.37431 0.41782 0.35057 -0.01125 0.02618  -0.00681 340 HOH   D O     
5880 O  O     . HOH   N .   ? 0.45723 0.46745 0.41339 0.01514  -0.01637 -0.01678 341 HOH   D O     
5881 O  O     . HOH   N .   ? 0.30379 0.35977 0.28414 0.01721  0.03804  0.01711  342 HOH   D O     
5882 O  O     . HOH   N .   ? 0.64096 0.63693 0.54956 0.03776  0.04299  -0.00832 343 HOH   D O     
5883 O  O     . HOH   N .   ? 0.50437 0.60407 0.65010 0.01037  0.06983  0.09050  344 HOH   D O     
5884 O  O     . HOH   N .   ? 0.32001 0.35014 0.29193 -0.00716 0.02408  -0.01040 345 HOH   D O     
5885 O  O     . HOH   N .   ? 0.33154 0.38100 0.32843 -0.00980 0.02459  0.00475  346 HOH   D O     
5886 O  O     . HOH   N .   ? 0.32047 0.37213 0.31757 0.00374  0.05011  0.01437  347 HOH   D O     
5887 O  O     . HOH   N .   ? 0.55718 0.53434 0.47852 0.01290  -0.00046 -0.02357 348 HOH   D O     
5888 O  O     . HOH   N .   ? 0.57418 0.60806 0.51229 0.03973  0.07378  0.02551  349 HOH   D O     
5889 O  O     . HOH   N .   ? 0.44838 0.46910 0.50322 -0.00578 -0.02318 -0.00142 350 HOH   D O     
5890 O  O     . HOH   N .   ? 0.29538 0.33347 0.27054 -0.01127 0.02381  -0.00757 351 HOH   D O     
5891 O  O     . HOH   N .   ? 0.31045 0.36214 0.29813 -0.00675 0.02705  0.00408  352 HOH   D O     
5892 O  O     . HOH   N .   ? 0.49049 0.50141 0.39875 0.05597  0.07106  0.01457  353 HOH   D O     
5893 O  O     . HOH   N .   ? 0.52700 0.58454 0.52781 -0.00468 0.04306  0.01755  354 HOH   D O     
5894 O  O     . HOH   N .   ? 0.23954 0.30755 0.30760 0.00231  0.05120  0.03671  355 HOH   D O     
5895 O  O     . HOH   N .   ? 0.45246 0.53729 0.59901 0.00439  0.05453  0.06839  356 HOH   D O     
5896 O  O     . HOH   N .   ? 0.36203 0.41981 0.36662 -0.00611 0.02817  0.01564  357 HOH   D O     
5897 O  O     . HOH   N .   ? 0.55842 0.56133 0.46740 0.04902  0.05869  0.00258  358 HOH   D O     
5898 O  O     . HOH   N .   ? 0.48911 0.48976 0.38800 0.03441  0.04486  -0.00396 359 HOH   D O     
5899 O  O     . HOH   N .   ? 0.40127 0.47346 0.45757 0.00061  0.05224  0.04193  360 HOH   D O     
5900 O  O     . HOH   N .   ? 0.56872 0.58139 0.54980 0.01146  -0.01044 -0.01624 361 HOH   D O     
5901 O  O     . HOH   N .   ? 0.38572 0.41158 0.31344 0.03928  0.01968  -0.00075 362 HOH   D O     
5902 O  O     . HOH   N .   ? 0.38668 0.42616 0.37397 0.00230  0.02485  -0.00830 363 HOH   D O     
5903 O  O     . HOH   N .   ? 0.34679 0.40641 0.34540 0.00609  0.03584  0.01856  364 HOH   D O     
5904 O  O     . HOH   N .   ? 0.56090 0.58936 0.48759 0.06164  0.08828  0.03434  365 HOH   D O     
5905 O  O     . HOH   N .   ? 0.28094 0.34427 0.33997 0.00105  0.04791  0.02897  366 HOH   D O     
5906 O  O     . HOH   N .   ? 0.36073 0.35977 0.28608 0.03829  -0.01017 -0.01754 367 HOH   D O     
5907 O  O     . HOH   N .   ? 0.52338 0.52718 0.50933 0.01267  -0.02296 -0.01778 368 HOH   D O     
5908 O  O     . HOH   N .   ? 0.41823 0.48315 0.42591 0.03113  0.08335  0.05078  369 HOH   D O     
5909 O  O     . HOH   N .   ? 0.34621 0.38590 0.33345 0.00165  0.04139  -0.00221 370 HOH   D O     
5910 O  O     . HOH   N .   ? 0.26144 0.33565 0.34864 0.00257  0.05281  0.04707  371 HOH   D O     
5911 O  O     . HOH   N .   ? 0.42096 0.47674 0.52483 -0.01201 0.01090  0.02855  372 HOH   D O     
5912 O  O     . HOH   N .   ? 0.57668 0.63712 0.59606 -0.00950 0.03566  0.01905  373 HOH   D O     
5913 O  O     . HOH   N .   ? 0.43703 0.47129 0.39623 -0.01120 0.02367  -0.00882 374 HOH   D O     
5914 O  O     . HOH   N .   ? 0.53171 0.56610 0.49913 -0.01377 0.01883  -0.00770 375 HOH   D O     
5915 O  O     . HOH   N .   ? 0.35690 0.38085 0.29594 0.03147  0.01536  -0.00594 376 HOH   D O     
5916 O  O     . HOH   N .   ? 0.38422 0.48496 0.53283 0.01609  0.07715  0.09363  377 HOH   D O     
5917 O  O     . HOH   N .   ? 0.39526 0.42020 0.43873 -0.00685 -0.01845 -0.00168 378 HOH   D O     
5918 O  O     . HOH   N .   ? 0.47429 0.49015 0.37444 0.06905  0.08582  0.02938  379 HOH   D O     
5919 O  O     . HOH   N .   ? 0.42144 0.40690 0.29626 0.05663  0.05175  -0.00228 380 HOH   D O     
5920 O  O     . HOH   N .   ? 0.41434 0.46659 0.41254 -0.01368 0.02472  0.00390  381 HOH   D O     
5921 O  O     . HOH   N .   ? 0.50624 0.51329 0.42963 0.01969  0.03573  -0.00960 382 HOH   D O     
5922 O  O     . HOH   N .   ? 0.56980 0.61174 0.56401 -0.00368 0.02823  -0.00778 383 HOH   D O     
5923 O  O     . HOH   N .   ? 0.58109 0.60894 0.53718 0.00591  -0.00082 -0.01183 384 HOH   D O     
5924 O  O     . HOH   N .   ? 0.42331 0.46037 0.39987 -0.01335 0.01968  -0.00599 385 HOH   D O     
5925 O  O     . HOH   N .   ? 0.26884 0.32509 0.27360 0.02051  0.06907  0.03138  386 HOH   D O     
5926 O  O     . HOH   N .   ? 0.50153 0.51791 0.52564 0.00131  -0.01501 -0.01075 387 HOH   D O     
5927 O  O     . HOH   N .   ? 0.54213 0.59789 0.69205 -0.01974 -0.01459 0.04353  388 HOH   D O     
5928 O  O     . HOH   N .   ? 0.43706 0.41063 0.29446 0.06099  0.04582  -0.00664 389 HOH   D O     
5929 O  O     . HOH   N .   ? 0.57491 0.58663 0.53859 0.01856  -0.00564 -0.01665 390 HOH   D O     
5930 O  O     . HOH   N .   ? 0.51498 0.58719 0.58255 -0.00685 0.04041  0.04048  391 HOH   D O     
5931 O  O     . HOH   N .   ? 0.34193 0.38475 0.31063 -0.01075 0.02936  -0.00520 392 HOH   D O     
5932 O  O     . HOH   N .   ? 0.33256 0.38562 0.32012 0.01253  0.03601  0.01193  393 HOH   D O     
5933 O  O     . HOH   N .   ? 0.47889 0.51857 0.43259 0.00670  0.01580  -0.00537 394 HOH   D O     
5934 O  O     . HOH   N .   ? 0.45234 0.50096 0.43606 0.04385  0.08583  0.03856  395 HOH   D O     
5935 O  O     . HOH   N .   ? 0.63115 0.62892 0.52339 0.06065  0.06473  0.00693  396 HOH   D O     
5936 O  O     . HOH   N .   ? 0.35434 0.44723 0.45228 0.03120  0.09359  0.08654  397 HOH   D O     
5937 O  O     . HOH   N .   ? 0.48522 0.47892 0.46777 0.01328  -0.04176 -0.01902 398 HOH   D O     
5938 O  O     . HOH   N .   ? 0.33197 0.35599 0.28246 0.00511  0.03475  -0.00798 399 HOH   D O     
5939 O  O     . HOH   N .   ? 0.29924 0.36229 0.43183 -0.01148 0.01461  0.04140  400 HOH   D O     
5940 O  O     . HOH   N .   ? 0.51910 0.55150 0.61643 -0.01031 -0.01556 0.01225  401 HOH   D O     
5941 O  O     . HOH   N .   ? 0.44949 0.48033 0.50696 -0.00922 -0.01346 0.00333  402 HOH   D O     
5942 O  O     . HOH   N .   ? 0.51886 0.58825 0.68683 -0.01858 -0.00021 0.05802  403 HOH   D O     
5943 O  O     . HOH   N .   ? 0.51795 0.51052 0.48599 0.01910  -0.03590 -0.02093 404 HOH   D O     
5944 O  O     . HOH   N .   ? 0.60187 0.60459 0.53225 0.02126  0.03287  -0.01331 405 HOH   D O     
5945 O  O     . HOH   N .   ? 0.59796 0.63657 0.66499 -0.00704 0.00715  0.00507  406 HOH   D O     
5946 O  O     . HOH   N .   ? 0.49489 0.56292 0.54376 0.02354  0.07649  0.04673  407 HOH   D O     
5947 O  O     . HOH   N .   ? 0.56976 0.58857 0.55540 0.00196  -0.01682 -0.01258 408 HOH   D O     
5948 O  O     . HOH   N .   ? 0.55581 0.58864 0.50706 -0.00689 0.02880  -0.00747 409 HOH   D O     
5949 O  O     . HOH   N .   ? 0.40017 0.42476 0.34912 -0.00664 0.02231  -0.01098 410 HOH   D O     
5950 O  O     . HOH   N .   ? 0.62246 0.67048 0.60588 -0.01438 0.02090  0.00203  411 HOH   D O     
5951 O  O     . HOH   N .   ? 0.42808 0.47717 0.38157 0.03718  0.04027  0.01927  412 HOH   D O     
5952 O  O     . HOH   N .   ? 0.39922 0.40099 0.39744 0.00750  -0.03536 -0.01558 413 HOH   D O     
5953 O  O     . HOH   N .   ? 0.62406 0.64714 0.54273 0.03315  0.06109  0.01293  414 HOH   D O     
5954 O  O     A HOH   N .   ? 0.42214 0.47006 0.49926 -0.01829 -0.01005 0.02006  415 HOH   D O     
5955 O  O     B HOH   N .   ? 0.38157 0.43188 0.46202 -0.01787 -0.00603 0.02201  415 HOH   D O     
5956 O  O     . HOH   N .   ? 0.59208 0.62863 0.57139 0.01806  0.05582  0.00676  416 HOH   D O     
5957 O  O     . HOH   N .   ? 0.49855 0.54793 0.49572 0.02712  0.07153  0.02684  417 HOH   D O     
5958 O  O     . HOH   N .   ? 0.55936 0.57639 0.49976 -0.00510 0.01810  -0.01292 418 HOH   D O     
5959 O  O     . HOH   N .   ? 0.69404 0.67476 0.59491 0.01766  0.01042  -0.02092 419 HOH   D O     
5960 O  O     . HOH   N .   ? 0.29060 0.33233 0.33084 -0.00830 0.01122  0.00207  420 HOH   D O     
5961 O  O     . HOH   N .   ? 0.43617 0.47056 0.41497 -0.01281 0.01823  -0.00636 421 HOH   D O     
5962 O  O     . HOH   N .   ? 0.49691 0.48233 0.35458 0.07384  0.06692  0.00917  422 HOH   D O     
5963 O  O     . HOH   N .   ? 0.52549 0.56220 0.49862 0.02262  0.06015  0.01103  423 HOH   D O     
5964 O  O     . HOH   N .   ? 0.54141 0.57358 0.49238 0.00908  0.00774  -0.00923 424 HOH   D O     
5965 O  O     . HOH   N .   ? 0.43089 0.47657 0.40295 -0.01256 0.02756  -0.00461 425 HOH   D O     
5966 O  O     A HOH   N .   ? 0.38386 0.43858 0.38811 -0.00019 0.03183  0.01163  426 HOH   D O     
5967 O  O     B HOH   N .   ? 0.33087 0.38754 0.34090 -0.00191 0.03109  0.01515  426 HOH   D O     
5968 O  O     . HOH   N .   ? 0.61158 0.66552 0.58838 -0.00637 0.02612  0.00509  427 HOH   D O     
5969 O  O     . HOH   N .   ? 0.52371 0.57654 0.52957 -0.00145 0.03082  0.00938  428 HOH   D O     
5970 O  O     . HOH   N .   ? 0.56109 0.61588 0.53188 -0.00094 0.02740  0.00690  429 HOH   D O     
5971 O  O     . HOH   N .   ? 0.67833 0.71631 0.66942 -0.01014 -0.00043 -0.00597 430 HOH   D O     
5972 O  O     . HOH   N .   ? 0.54478 0.61522 0.56157 0.00308  0.03670  0.03460  431 HOH   D O     
5973 O  O     . HOH   N .   ? 0.56023 0.62633 0.56963 0.04907  0.09983  0.06303  432 HOH   D O     
5974 O  O     . HOH   N .   ? 0.59290 0.64959 0.60750 -0.00913 0.02497  0.01750  433 HOH   D O     
5975 O  O     . HOH   N .   ? 0.50387 0.48322 0.46247 0.02577  -0.04875 -0.02451 434 HOH   D O     
5976 O  O     . HOH   N .   ? 0.55913 0.58339 0.51915 0.00796  0.03751  -0.00829 435 HOH   D O     
5977 O  O     . HOH   N .   ? 0.69400 0.74135 0.66127 -0.01472 0.02138  -0.00614 436 HOH   D O     
5978 O  O     . HOH   N .   ? 0.57974 0.56313 0.46094 0.03890  0.03436  -0.01185 437 HOH   D O     
5979 O  O     . HOH   N .   ? 0.41430 0.45112 0.37317 -0.00971 0.02773  -0.00735 438 HOH   D O     
5980 O  O     . HOH   N .   ? 0.65076 0.65061 0.56457 0.03962  0.04782  -0.00550 439 HOH   D O     
5981 O  O     . HOH   N .   ? 0.51818 0.55744 0.50847 -0.01413 0.01728  -0.00120 440 HOH   D O     
5982 O  O     . HOH   N .   ? 0.54848 0.56505 0.48781 0.01279  0.03665  -0.00826 441 HOH   D O     
5983 O  O     . HOH   N .   ? 0.50707 0.57326 0.52226 0.00477  0.03719  0.02915  442 HOH   D O     
5984 O  O     . HOH   N .   ? 0.50897 0.53219 0.44894 0.03294  0.01632  -0.00585 443 HOH   D O     
5985 O  O     . HOH   N .   ? 0.59602 0.64693 0.55763 0.00263  0.02513  0.00318  444 HOH   D O     
5986 O  O     . HOH   N .   ? 0.63125 0.62364 0.51093 0.06399  0.06356  0.00618  445 HOH   D O     
5987 O  O     . HOH   N .   ? 0.53468 0.57906 0.53626 -0.00337 0.02872  -0.00244 446 HOH   D O     
5988 O  O     . HOH   N .   ? 0.45614 0.51511 0.44934 -0.00584 0.02822  0.01476  447 HOH   D O     
5989 O  O     . HOH   N .   ? 0.46561 0.50744 0.47416 -0.00517 0.02728  -0.00697 448 HOH   D O     
5990 O  O     . HOH   N .   ? 0.52734 0.55056 0.52893 -0.00390 -0.01786 -0.00877 449 HOH   D O     
5991 O  O     . HOH   N .   ? 0.54843 0.52865 0.48833 0.03136  -0.04301 -0.02496 450 HOH   D O     
5992 O  O     . HOH   N .   ? 0.49581 0.54196 0.60164 -0.01104 0.00168  0.02127  451 HOH   D O     
5993 O  O     . HOH   N .   ? 0.68159 0.71995 0.67889 -0.01452 0.01494  0.00076  452 HOH   D O     
5994 O  O     . HOH   N .   ? 0.58787 0.63271 0.55534 -0.01348 0.02638  -0.00549 453 HOH   D O     
5995 O  O     . HOH   N .   ? 0.54308 0.60774 0.55861 -0.00282 0.03150  0.02648  454 HOH   D O     
5996 O  O     . HOH   N .   ? 0.61694 0.66904 0.62529 0.00179  0.03262  0.00934  455 HOH   D O     
5997 O  O     . HOH   N .   ? 0.51544 0.60718 0.68936 0.00367  0.05407  0.08114  456 HOH   D O     
5998 O  O     . HOH   N .   ? 0.57991 0.58116 0.52312 0.03100  -0.01021 -0.01860 457 HOH   D O     
5999 O  O     . HOH   N .   ? 0.58679 0.60056 0.61480 -0.00131 -0.02746 -0.00825 458 HOH   D O     
6000 O  O     . HOH   N .   ? 0.40220 0.46250 0.38304 0.02698  0.04465  0.02718  459 HOH   D O     
6001 O  O     . HOH   N .   ? 0.44939 0.52559 0.52281 -0.00194 0.04911  0.04792  460 HOH   D O     
6002 O  O     . HOH   N .   ? 0.53107 0.53665 0.55150 0.00210  -0.03639 -0.01132 461 HOH   D O     
6003 O  O     . HOH   N .   ? 0.61268 0.65622 0.58370 -0.01553 0.02057  -0.00427 462 HOH   D O     
6004 O  O     . HOH   N .   ? 0.58981 0.62664 0.56467 0.02565  0.06290  0.01282  463 HOH   D O     
6005 O  O     . HOH   N .   ? 0.60857 0.59722 0.52356 0.02586  0.02479  -0.01789 464 HOH   D O     
6006 O  O     . HOH   N .   ? 0.61864 0.60196 0.52184 0.01920  0.01424  -0.01987 465 HOH   D O     
6007 O  O     . HOH   N .   ? 0.56937 0.60393 0.52897 -0.01347 0.02071  -0.00865 466 HOH   D O     
6008 O  O     . HOH   N .   ? 0.55733 0.59235 0.64144 -0.01189 -0.01506 0.01188  467 HOH   D O     
6009 O  O     . HOH   N .   ? 0.61372 0.62817 0.58523 0.00564  -0.02110 -0.01475 468 HOH   D O     
6010 O  O     . HOH   N .   ? 0.65949 0.67104 0.56118 0.07126  0.08410  0.02507  469 HOH   D O     
6011 O  O     . HOH   N .   ? 0.40801 0.48325 0.48866 0.01573  0.07005  0.05303  470 HOH   D O     
6012 O  O     . HOH   N .   ? 0.61105 0.65580 0.59047 -0.01596 0.01888  -0.00041 471 HOH   D O     
6013 O  O     . HOH   N .   ? 0.60993 0.66065 0.58742 -0.01175 0.02349  0.00139  472 HOH   D O     
6014 O  O     . HOH   N .   ? 0.53421 0.63116 0.65021 0.01732  0.07928  0.08722  473 HOH   D O     
6015 O  O     . HOH   N .   ? 0.58797 0.64409 0.59713 -0.01296 0.02808  0.01074  474 HOH   D O     
6016 O  O     . HOH   N .   ? 0.66084 0.70093 0.62179 -0.01281 0.02558  -0.00721 475 HOH   D O     
6017 O  O     . HOH   N .   ? 0.60581 0.62759 0.64344 -0.00151 -0.00909 -0.00769 476 HOH   D O     
6018 O  O     . HOH   N .   ? 0.57824 0.59115 0.49627 0.04725  0.01200  -0.00629 477 HOH   D O     
6019 O  O     . HOH   N .   ? 0.63563 0.62224 0.54776 0.02448  0.02168  -0.01872 478 HOH   D O     
6020 O  O     . HOH   N .   ? 0.57103 0.61639 0.55286 0.04091  0.08136  0.03253  479 HOH   D O     
6021 O  O     . HOH   N .   ? 0.58664 0.58100 0.46301 0.07737  0.07609  0.01532  480 HOH   D O     
6022 O  O     . HOH   N .   ? 0.34432 0.40418 0.49016 -0.01260 0.00709  0.04200  481 HOH   D O     
6023 O  O     . HOH   N .   ? 0.57960 0.62433 0.53574 0.00343  0.01954  -0.00275 482 HOH   D O     
6024 O  O     . HOH   N .   ? 0.54394 0.59844 0.67226 -0.01173 0.00636  0.03302  483 HOH   D O     
6025 O  O     . HOH   N .   ? 0.58050 0.59557 0.62989 -0.00136 -0.02134 -0.00669 484 HOH   D O     
6026 O  O     . HOH   N .   ? 0.61657 0.68865 0.62956 0.01733  0.04616  0.04008  485 HOH   D O     
6027 O  O     . HOH   N .   ? 0.51470 0.58202 0.65786 -0.01363 0.01227  0.04860  486 HOH   D O     
6028 O  O     . HOH   N .   ? 0.52748 0.58494 0.66255 -0.01516 0.00039  0.03877  487 HOH   D O     
6029 O  O     . HOH   N .   ? 0.60655 0.64201 0.56627 0.05245  0.08488  0.03061  488 HOH   D O     
6030 O  O     . HOH   N .   ? 0.60126 0.70197 0.70813 0.03433  0.09980  0.09997  489 HOH   D O     
6031 O  O     . HOH   N .   ? 0.59079 0.63971 0.57573 0.05088  0.09184  0.04309  490 HOH   D O     
6032 O  O     . HOH   N .   ? 0.61008 0.70821 0.71173 0.02952  0.09395  0.09405  491 HOH   D O     
# 
