data_9KUE
# 
_entry.id   9KUE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9KUE         pdb_00009kue 10.2210/pdb9kue/pdb 
WWPDB D_1300054289 ?            ?                   
# 
_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       2025-04-23 
_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                        9KUE 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 v.popov@fbras.ru          Vladimir   Popov     ?  'principal investigator/group leader' 0000-0002-0133-7962 
3 kmb@inbi.ras.ru           Konstantin Boyko     ?  'principal investigator/group leader' 0000-0001-8229-189X 
4 nikolai.sluchanko@mail.ru Nikolai    Sluchanko N. 'principal investigator/group leader' 0000-0002-8608-1416 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sluchanko, N.N.'    1 ? 
'Egorkin, N.A.'      2 ? 
'Varfolomeeva, L.A.' 3 ? 
'Popov, V.O.'        4 ? 
'Boyko, K.M.'        5 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of the soluble green pigment protein from Tettigonia cantans' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sluchanko, N.N.'    1 ? 
primary 'Egorkin, N.A.'      2 ? 
primary 'Varfolomeeva, L.A.' 3 ? 
primary 'Popov, V.O.'        4 ? 
primary 'Boyko, K.M.'        5 ? 
# 
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     nat 'Dibilinoxanthinin (DBXN)' 12398.976 2   ? ? ? ? 
2 polymer     nat 'Dibilinoxanthinin (DBXN)' 7682.458  2   ? ? ? ? 
3 polymer     nat 'Dibilinoxanthinin (DBXN)' 18590.566 2   ? ? ? ? 
4 non-polymer syn "(3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL" 568.871   2   ? ? ? ? 
5 non-polymer syn 'AZIDE ION' 42.020    6   ? ? ? ? 
6 non-polymer syn 'DIUNDECYL PHOSPHATIDYL CHOLINE' 622.834   4   ? ? ? ? 
7 non-polymer syn 
;3-[5-[(~{Z})-(3-ethyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[(~{Z})-[4-(hydroxymethyl)-3-(3-hydroxy-3-oxopropyl)-5-[(~{Z})-[3-methyl-5-oxidanylidene-4-[(1~{S},4~{E},8~{Z})-5,9,13-trimethyl-1-oxidanyl-tetradeca-4,8,12-trienyl]pyrrol-2-ylidene]methyl]pyrrol-2-ylidene]methyl]-4-methyl-1~{H}-pyrrol-3-yl]propanoic acid
;
823.028   2   ? ? ? ? 
8 water       nat water 18.015    174 ? ? ? ? 
# 
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 yes 
;QGSQVEFSMKMTGGEIPGGNIVLQGVKLRIVGEWVLKGSSGESVRRTDVKVDITSTAGNQDNSFAIQLANYAHNKPNTKW
(CSD)ALLTKKYPERKPDVLAFGWGNEQVDSKASVTIG
;
;QGSQVEFSMKMTGGEIPGGNIVLQGVKLRIVGEWVLKGSSGESVRRTDVKVDITSTAGNQDNSFAIQLANYAHNKPNTKW
CALLTKKYPERKPDVLAFGWGNEQVDSKASVTIG
;
A,D ? 
2 'polypeptide(L)' no no  SVTITINQKGEITEEQKQRAQGDDWPYGQCKEDQKKSEWKDSDFLPNTQACYIGSILLTTARKTTYS 
SVTITINQKGEITEEQKQRAQGDDWPYGQCKEDQKKSEWKDSDFLPNTQACYIGSILLTTARKTTYS B,E ? 
3 'polypeptide(L)' no no  
;GASSVDDYNPAFDNTHYSRFHLLIETNGITKPCIVSTENVYTPDNATVPHKQGSDYVLVAGLAGDPNRFSAYTRSQGGSK
PLVVKLVNDGVTLELTRDGASINGKAVSVEKGVQYPQDDPNYAIRVWKSGDLVMAYSRRTAVYAYYTGTAVDVEQPVTYR
GRATGLCGNLNG
;
;GASSVDDYNPAFDNTHYSRFHLLIETNGITKPCIVSTENVYTPDNATVPHKQGSDYVLVAGLAGDPNRFSAYTRSQGGSK
PLVVKLVNDGVTLELTRDGASINGKAVSVEKGVQYPQDDPNYAIRVWKSGDLVMAYSRRTAVYAYYTGTAVDVEQPVTYR
GRATGLCGNLNG
;
C,F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "(3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL" LUT   
5 'AZIDE ION' AZI   
6 'DIUNDECYL PHOSPHATIDYL CHOLINE' PLC   
7 
;3-[5-[(~{Z})-(3-ethyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[(~{Z})-[4-(hydroxymethyl)-3-(3-hydroxy-3-oxopropyl)-5-[(~{Z})-[3-methyl-5-oxidanylidene-4-[(1~{S},4~{E},8~{Z})-5,9,13-trimethyl-1-oxidanyl-tetradeca-4,8,12-trienyl]pyrrol-2-ylidene]methyl]pyrrol-2-ylidene]methyl]-4-methyl-1~{H}-pyrrol-3-yl]propanoic acid
;
A1L6M 
8 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   GLY n 
1 3   SER n 
1 4   GLN n 
1 5   VAL n 
1 6   GLU n 
1 7   PHE n 
1 8   SER n 
1 9   MET n 
1 10  LYS n 
1 11  MET n 
1 12  THR n 
1 13  GLY n 
1 14  GLY n 
1 15  GLU n 
1 16  ILE n 
1 17  PRO n 
1 18  GLY n 
1 19  GLY n 
1 20  ASN n 
1 21  ILE n 
1 22  VAL n 
1 23  LEU n 
1 24  GLN n 
1 25  GLY n 
1 26  VAL n 
1 27  LYS n 
1 28  LEU n 
1 29  ARG n 
1 30  ILE n 
1 31  VAL n 
1 32  GLY n 
1 33  GLU n 
1 34  TRP n 
1 35  VAL n 
1 36  LEU n 
1 37  LYS n 
1 38  GLY n 
1 39  SER n 
1 40  SER n 
1 41  GLY n 
1 42  GLU n 
1 43  SER n 
1 44  VAL n 
1 45  ARG n 
1 46  ARG n 
1 47  THR n 
1 48  ASP n 
1 49  VAL n 
1 50  LYS n 
1 51  VAL n 
1 52  ASP n 
1 53  ILE n 
1 54  THR n 
1 55  SER n 
1 56  THR n 
1 57  ALA n 
1 58  GLY n 
1 59  ASN n 
1 60  GLN n 
1 61  ASP n 
1 62  ASN n 
1 63  SER n 
1 64  PHE n 
1 65  ALA n 
1 66  ILE n 
1 67  GLN n 
1 68  LEU n 
1 69  ALA n 
1 70  ASN n 
1 71  TYR n 
1 72  ALA n 
1 73  HIS n 
1 74  ASN n 
1 75  LYS n 
1 76  PRO n 
1 77  ASN n 
1 78  THR n 
1 79  LYS n 
1 80  TRP n 
1 81  CSD n 
1 82  ALA n 
1 83  LEU n 
1 84  LEU n 
1 85  THR n 
1 86  LYS n 
1 87  LYS n 
1 88  TYR n 
1 89  PRO n 
1 90  GLU n 
1 91  ARG n 
1 92  LYS n 
1 93  PRO n 
1 94  ASP n 
1 95  VAL n 
1 96  LEU n 
1 97  ALA n 
1 98  PHE n 
1 99  GLY n 
1 100 TRP n 
1 101 GLY n 
1 102 ASN n 
1 103 GLU n 
1 104 GLN n 
1 105 VAL n 
1 106 ASP n 
1 107 SER n 
1 108 LYS n 
1 109 ALA n 
1 110 SER n 
1 111 VAL n 
1 112 THR n 
1 113 ILE n 
1 114 GLY n 
2 1   SER n 
2 2   VAL n 
2 3   THR n 
2 4   ILE n 
2 5   THR n 
2 6   ILE n 
2 7   ASN n 
2 8   GLN n 
2 9   LYS n 
2 10  GLY n 
2 11  GLU n 
2 12  ILE n 
2 13  THR n 
2 14  GLU n 
2 15  GLU n 
2 16  GLN n 
2 17  LYS n 
2 18  GLN n 
2 19  ARG n 
2 20  ALA n 
2 21  GLN n 
2 22  GLY n 
2 23  ASP n 
2 24  ASP n 
2 25  TRP n 
2 26  PRO n 
2 27  TYR n 
2 28  GLY n 
2 29  GLN n 
2 30  CYS n 
2 31  LYS n 
2 32  GLU n 
2 33  ASP n 
2 34  GLN n 
2 35  LYS n 
2 36  LYS n 
2 37  SER n 
2 38  GLU n 
2 39  TRP n 
2 40  LYS n 
2 41  ASP n 
2 42  SER n 
2 43  ASP n 
2 44  PHE n 
2 45  LEU n 
2 46  PRO n 
2 47  ASN n 
2 48  THR n 
2 49  GLN n 
2 50  ALA n 
2 51  CYS n 
2 52  TYR n 
2 53  ILE n 
2 54  GLY n 
2 55  SER n 
2 56  ILE n 
2 57  LEU n 
2 58  LEU n 
2 59  THR n 
2 60  THR n 
2 61  ALA n 
2 62  ARG n 
2 63  LYS n 
2 64  THR n 
2 65  THR n 
2 66  TYR n 
2 67  SER n 
3 1   GLY n 
3 2   ALA n 
3 3   SER n 
3 4   SER n 
3 5   VAL n 
3 6   ASP n 
3 7   ASP n 
3 8   TYR n 
3 9   ASN n 
3 10  PRO n 
3 11  ALA n 
3 12  PHE n 
3 13  ASP n 
3 14  ASN n 
3 15  THR n 
3 16  HIS n 
3 17  TYR n 
3 18  SER n 
3 19  ARG n 
3 20  PHE n 
3 21  HIS n 
3 22  LEU n 
3 23  LEU n 
3 24  ILE n 
3 25  GLU n 
3 26  THR n 
3 27  ASN n 
3 28  GLY n 
3 29  ILE n 
3 30  THR n 
3 31  LYS n 
3 32  PRO n 
3 33  CYS n 
3 34  ILE n 
3 35  VAL n 
3 36  SER n 
3 37  THR n 
3 38  GLU n 
3 39  ASN n 
3 40  VAL n 
3 41  TYR n 
3 42  THR n 
3 43  PRO n 
3 44  ASP n 
3 45  ASN n 
3 46  ALA n 
3 47  THR n 
3 48  VAL n 
3 49  PRO n 
3 50  HIS n 
3 51  LYS n 
3 52  GLN n 
3 53  GLY n 
3 54  SER n 
3 55  ASP n 
3 56  TYR n 
3 57  VAL n 
3 58  LEU n 
3 59  VAL n 
3 60  ALA n 
3 61  GLY n 
3 62  LEU n 
3 63  ALA n 
3 64  GLY n 
3 65  ASP n 
3 66  PRO n 
3 67  ASN n 
3 68  ARG n 
3 69  PHE n 
3 70  SER n 
3 71  ALA n 
3 72  TYR n 
3 73  THR n 
3 74  ARG n 
3 75  SER n 
3 76  GLN n 
3 77  GLY n 
3 78  GLY n 
3 79  SER n 
3 80  LYS n 
3 81  PRO n 
3 82  LEU n 
3 83  VAL n 
3 84  VAL n 
3 85  LYS n 
3 86  LEU n 
3 87  VAL n 
3 88  ASN n 
3 89  ASP n 
3 90  GLY n 
3 91  VAL n 
3 92  THR n 
3 93  LEU n 
3 94  GLU n 
3 95  LEU n 
3 96  THR n 
3 97  ARG n 
3 98  ASP n 
3 99  GLY n 
3 100 ALA n 
3 101 SER n 
3 102 ILE n 
3 103 ASN n 
3 104 GLY n 
3 105 LYS n 
3 106 ALA n 
3 107 VAL n 
3 108 SER n 
3 109 VAL n 
3 110 GLU n 
3 111 LYS n 
3 112 GLY n 
3 113 VAL n 
3 114 GLN n 
3 115 TYR n 
3 116 PRO n 
3 117 GLN n 
3 118 ASP n 
3 119 ASP n 
3 120 PRO n 
3 121 ASN n 
3 122 TYR n 
3 123 ALA n 
3 124 ILE n 
3 125 ARG n 
3 126 VAL n 
3 127 TRP n 
3 128 LYS n 
3 129 SER n 
3 130 GLY n 
3 131 ASP n 
3 132 LEU n 
3 133 VAL n 
3 134 MET n 
3 135 ALA n 
3 136 TYR n 
3 137 SER n 
3 138 ARG n 
3 139 ARG n 
3 140 THR n 
3 141 ALA n 
3 142 VAL n 
3 143 TYR n 
3 144 ALA n 
3 145 TYR n 
3 146 TYR n 
3 147 THR n 
3 148 GLY n 
3 149 THR n 
3 150 ALA n 
3 151 VAL n 
3 152 ASP n 
3 153 VAL n 
3 154 GLU n 
3 155 GLN n 
3 156 PRO n 
3 157 VAL n 
3 158 THR n 
3 159 TYR n 
3 160 ARG n 
3 161 GLY n 
3 162 ARG n 
3 163 ALA n 
3 164 THR n 
3 165 GLY n 
3 166 LEU n 
3 167 CYS n 
3 168 GLY n 
3 169 ASN n 
3 170 LEU n 
3 171 ASN n 
3 172 GLY n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample 1 114 ? 'Tettigonia cantans' 420850 ? ? ? integuments ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 1 67  ? 'Tettigonia cantans' 420850 ? ? ? integuments ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 1 172 ? 'Tettigonia cantans' 420850 ? ? ? integuments ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1L6M non-polymer         . 
;3-[5-[(~{Z})-(3-ethyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[(~{Z})-[4-(hydroxymethyl)-3-(3-hydroxy-3-oxopropyl)-5-[(~{Z})-[3-methyl-5-oxidanylidene-4-[(1~{S},4~{E},8~{Z})-5,9,13-trimethyl-1-oxidanyl-tetradeca-4,8,12-trienyl]pyrrol-2-ylidene]methyl]pyrrol-2-ylidene]methyl]-4-methyl-1~{H}-pyrrol-3-yl]propanoic acid
;
?                                               'C48 H62 N4 O8'    823.028 
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 
AZI   non-polymer         . 'AZIDE ION' ?                                               'N3 -1'            42.020  
CSD   'L-peptide linking' n 3-SULFINOALANINE 'S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE'    'C3 H7 N O4 S'     153.157 
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  
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 
LUT   non-polymer         . "(3R,3'R,6S)-4,5-DIDEHYDRO-5,6-DIHYDRO-BETA,BETA-CAROTENE-3,3'-DIOL" 
;(3R,3'R)-BETA,BETA-CAROTENE-3,3'-DIOL; LUTEIN
;
'C40 H56 O2'       568.871 
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 
PHE   'L-peptide linking' y PHENYLALANINE ?                                               'C9 H11 N O2'      165.189 
PLC   non-polymer         . 'DIUNDECYL PHOSPHATIDYL CHOLINE' ?                                               'C32 H65 N O8 P 1' 
622.834 
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   GLN 1   0   ?   ?   ?   A . n 
A 1 2   GLY 2   1   1   GLY GLY A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   GLN 4   3   3   GLN GLN A . n 
A 1 5   VAL 5   4   4   VAL VAL A . n 
A 1 6   GLU 6   5   5   GLU GLU A . n 
A 1 7   PHE 7   6   6   PHE PHE A . n 
A 1 8   SER 8   7   7   SER SER A . n 
A 1 9   MET 9   8   8   MET MET A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  MET 11  10  10  MET MET A . n 
A 1 12  THR 12  11  11  THR THR A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  GLY 14  13  13  GLY GLY A . n 
A 1 15  GLU 15  14  14  GLU GLU A . n 
A 1 16  ILE 16  15  15  ILE ILE A . n 
A 1 17  PRO 17  16  16  PRO PRO A . n 
A 1 18  GLY 18  17  17  GLY GLY A . n 
A 1 19  GLY 19  18  18  GLY GLY A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  ILE 21  20  20  ILE ILE A . n 
A 1 22  VAL 22  21  21  VAL VAL A . n 
A 1 23  LEU 23  22  22  LEU LEU A . n 
A 1 24  GLN 24  23  23  GLN GLN A . n 
A 1 25  GLY 25  24  24  GLY GLY A . n 
A 1 26  VAL 26  25  25  VAL VAL A . n 
A 1 27  LYS 27  26  26  LYS LYS A . n 
A 1 28  LEU 28  27  27  LEU LEU A . n 
A 1 29  ARG 29  28  28  ARG ARG A . n 
A 1 30  ILE 30  29  29  ILE ILE A . n 
A 1 31  VAL 31  30  30  VAL VAL A . n 
A 1 32  GLY 32  31  31  GLY GLY A . n 
A 1 33  GLU 33  32  32  GLU GLU A . n 
A 1 34  TRP 34  33  33  TRP TRP A . n 
A 1 35  VAL 35  34  34  VAL VAL A . n 
A 1 36  LEU 36  35  35  LEU LEU A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  SER 39  38  38  SER SER A . n 
A 1 40  SER 40  39  39  SER SER A . n 
A 1 41  GLY 41  40  40  GLY GLY A . n 
A 1 42  GLU 42  41  41  GLU GLU A . n 
A 1 43  SER 43  42  42  SER SER A . n 
A 1 44  VAL 44  43  43  VAL VAL A . n 
A 1 45  ARG 45  44  44  ARG ARG A . n 
A 1 46  ARG 46  45  45  ARG ARG A . n 
A 1 47  THR 47  46  46  THR THR A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  VAL 49  48  48  VAL VAL A . n 
A 1 50  LYS 50  49  49  LYS LYS A . n 
A 1 51  VAL 51  50  50  VAL VAL A . n 
A 1 52  ASP 52  51  51  ASP ASP A . n 
A 1 53  ILE 53  52  52  ILE ILE A . n 
A 1 54  THR 54  53  53  THR THR A . n 
A 1 55  SER 55  54  54  SER SER A . n 
A 1 56  THR 56  55  55  THR THR A . n 
A 1 57  ALA 57  56  56  ALA ALA A . n 
A 1 58  GLY 58  57  57  GLY GLY A . n 
A 1 59  ASN 59  58  58  ASN ASN A . n 
A 1 60  GLN 60  59  59  GLN GLN A . n 
A 1 61  ASP 61  60  60  ASP ASP A . n 
A 1 62  ASN 62  61  61  ASN ASN A . n 
A 1 63  SER 63  62  62  SER SER A . n 
A 1 64  PHE 64  63  63  PHE PHE A . n 
A 1 65  ALA 65  64  64  ALA ALA A . n 
A 1 66  ILE 66  65  65  ILE ILE A . n 
A 1 67  GLN 67  66  66  GLN GLN A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  ALA 69  68  68  ALA ALA A . n 
A 1 70  ASN 70  69  69  ASN ASN A . n 
A 1 71  TYR 71  70  ?   ?   ?   A . n 
A 1 72  ALA 72  71  ?   ?   ?   A . n 
A 1 73  HIS 73  72  ?   ?   ?   A . n 
A 1 74  ASN 74  73  ?   ?   ?   A . n 
A 1 75  LYS 75  74  ?   ?   ?   A . n 
A 1 76  PRO 76  75  ?   ?   ?   A . n 
A 1 77  ASN 77  76  ?   ?   ?   A . n 
A 1 78  THR 78  77  77  THR THR A . n 
A 1 79  LYS 79  78  78  LYS LYS A . n 
A 1 80  TRP 80  79  79  TRP TRP A . n 
A 1 81  CSD 81  80  80  CSD CSD A . n 
A 1 82  ALA 82  81  81  ALA ALA A . n 
A 1 83  LEU 83  82  82  LEU LEU A . n 
A 1 84  LEU 84  83  83  LEU LEU A . n 
A 1 85  THR 85  84  84  THR THR A . n 
A 1 86  LYS 86  85  85  LYS LYS A . n 
A 1 87  LYS 87  86  86  LYS LYS A . n 
A 1 88  TYR 88  87  87  TYR TYR A . n 
A 1 89  PRO 89  88  88  PRO PRO A . n 
A 1 90  GLU 90  89  89  GLU GLU A . n 
A 1 91  ARG 91  90  90  ARG ARG A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  PRO 93  92  92  PRO PRO A . n 
A 1 94  ASP 94  93  93  ASP ASP A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  LEU 96  95  95  LEU LEU A . n 
A 1 97  ALA 97  96  96  ALA ALA A . n 
A 1 98  PHE 98  97  97  PHE PHE A . n 
A 1 99  GLY 99  98  98  GLY GLY A . n 
A 1 100 TRP 100 99  99  TRP TRP A . n 
A 1 101 GLY 101 100 100 GLY GLY A . n 
A 1 102 ASN 102 101 101 ASN ASN A . n 
A 1 103 GLU 103 102 102 GLU GLU A . n 
A 1 104 GLN 104 103 103 GLN GLN A . n 
A 1 105 VAL 105 104 104 VAL VAL 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 LYS 108 107 107 LYS LYS A . n 
A 1 109 ALA 109 108 108 ALA ALA A . n 
A 1 110 SER 110 109 109 SER SER A . n 
A 1 111 VAL 111 110 110 VAL VAL A . n 
A 1 112 THR 112 111 111 THR THR A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 GLY 114 113 113 GLY GLY A . n 
B 2 1   SER 1   1   1   SER SER B . n 
B 2 2   VAL 2   2   2   VAL VAL B . n 
B 2 3   THR 3   3   3   THR THR B . n 
B 2 4   ILE 4   4   4   ILE ILE B . n 
B 2 5   THR 5   5   5   THR THR B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ASN 7   7   7   ASN ASN B . n 
B 2 8   GLN 8   8   8   GLN GLN B . n 
B 2 9   LYS 9   9   9   LYS LYS B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  ILE 12  12  12  ILE ILE B . n 
B 2 13  THR 13  13  13  THR THR B . n 
B 2 14  GLU 14  14  14  GLU GLU B . n 
B 2 15  GLU 15  15  15  GLU GLU B . n 
B 2 16  GLN 16  16  16  GLN GLN B . n 
B 2 17  LYS 17  17  17  LYS LYS B . n 
B 2 18  GLN 18  18  18  GLN GLN B . n 
B 2 19  ARG 19  19  19  ARG ARG B . n 
B 2 20  ALA 20  20  20  ALA ALA B . n 
B 2 21  GLN 21  21  21  GLN GLN B . n 
B 2 22  GLY 22  22  22  GLY GLY B . n 
B 2 23  ASP 23  23  23  ASP ASP B . n 
B 2 24  ASP 24  24  24  ASP ASP B . n 
B 2 25  TRP 25  25  25  TRP TRP B . n 
B 2 26  PRO 26  26  26  PRO PRO B . n 
B 2 27  TYR 27  27  27  TYR TYR B . n 
B 2 28  GLY 28  28  28  GLY GLY B . n 
B 2 29  GLN 29  29  29  GLN GLN B . n 
B 2 30  CYS 30  30  30  CYS CYS B . n 
B 2 31  LYS 31  31  31  LYS LYS B . n 
B 2 32  GLU 32  32  32  GLU GLU B . n 
B 2 33  ASP 33  33  33  ASP ASP B . n 
B 2 34  GLN 34  34  34  GLN GLN B . n 
B 2 35  LYS 35  35  35  LYS LYS B . n 
B 2 36  LYS 36  36  36  LYS LYS B . n 
B 2 37  SER 37  37  37  SER SER B . n 
B 2 38  GLU 38  38  38  GLU GLU B . n 
B 2 39  TRP 39  39  39  TRP TRP B . n 
B 2 40  LYS 40  40  40  LYS LYS B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  SER 42  42  42  SER SER B . n 
B 2 43  ASP 43  43  43  ASP ASP B . n 
B 2 44  PHE 44  44  44  PHE PHE B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  PRO 46  46  46  PRO PRO B . n 
B 2 47  ASN 47  47  47  ASN ASN B . n 
B 2 48  THR 48  48  48  THR THR B . n 
B 2 49  GLN 49  49  49  GLN GLN B . n 
B 2 50  ALA 50  50  50  ALA ALA B . n 
B 2 51  CYS 51  51  51  CYS CYS B . n 
B 2 52  TYR 52  52  52  TYR TYR B . n 
B 2 53  ILE 53  53  53  ILE ILE B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  SER 55  55  55  SER SER B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  LEU 57  57  57  LEU LEU B . n 
B 2 58  LEU 58  58  58  LEU LEU B . n 
B 2 59  THR 59  59  59  THR THR B . n 
B 2 60  THR 60  60  60  THR THR B . n 
B 2 61  ALA 61  61  61  ALA ALA B . n 
B 2 62  ARG 62  62  62  ARG ARG B . n 
B 2 63  LYS 63  63  63  LYS LYS B . n 
B 2 64  THR 64  64  64  THR THR B . n 
B 2 65  THR 65  65  65  THR THR B . n 
B 2 66  TYR 66  66  66  TYR TYR B . n 
B 2 67  SER 67  67  67  SER SER B . n 
C 3 1   GLY 1   1   ?   ?   ?   C . n 
C 3 2   ALA 2   2   ?   ?   ?   C . n 
C 3 3   SER 3   3   ?   ?   ?   C . n 
C 3 4   SER 4   4   4   SER SER C . n 
C 3 5   VAL 5   5   5   VAL VAL C . n 
C 3 6   ASP 6   6   6   ASP ASP C . n 
C 3 7   ASP 7   7   7   ASP ASP C . n 
C 3 8   TYR 8   8   8   TYR TYR C . n 
C 3 9   ASN 9   9   9   ASN ASN C . n 
C 3 10  PRO 10  10  10  PRO PRO C . n 
C 3 11  ALA 11  11  11  ALA ALA C . n 
C 3 12  PHE 12  12  12  PHE PHE C . n 
C 3 13  ASP 13  13  13  ASP ASP C . n 
C 3 14  ASN 14  14  14  ASN ASN C . n 
C 3 15  THR 15  15  15  THR THR C . n 
C 3 16  HIS 16  16  16  HIS HIS C . n 
C 3 17  TYR 17  17  17  TYR TYR C . n 
C 3 18  SER 18  18  18  SER SER C . n 
C 3 19  ARG 19  19  19  ARG ARG C . n 
C 3 20  PHE 20  20  20  PHE PHE C . n 
C 3 21  HIS 21  21  21  HIS HIS C . n 
C 3 22  LEU 22  22  22  LEU LEU C . n 
C 3 23  LEU 23  23  23  LEU LEU C . n 
C 3 24  ILE 24  24  24  ILE ILE C . n 
C 3 25  GLU 25  25  25  GLU GLU C . n 
C 3 26  THR 26  26  26  THR THR C . n 
C 3 27  ASN 27  27  27  ASN ASN C . n 
C 3 28  GLY 28  28  28  GLY GLY C . n 
C 3 29  ILE 29  29  29  ILE ILE C . n 
C 3 30  THR 30  30  30  THR THR C . n 
C 3 31  LYS 31  31  31  LYS LYS C . n 
C 3 32  PRO 32  32  32  PRO PRO C . n 
C 3 33  CYS 33  33  33  CYS CYS C . n 
C 3 34  ILE 34  34  34  ILE ILE C . n 
C 3 35  VAL 35  35  35  VAL VAL C . n 
C 3 36  SER 36  36  36  SER SER C . n 
C 3 37  THR 37  37  37  THR THR C . n 
C 3 38  GLU 38  38  38  GLU GLU C . n 
C 3 39  ASN 39  39  39  ASN ASN C . n 
C 3 40  VAL 40  40  40  VAL VAL C . n 
C 3 41  TYR 41  41  41  TYR TYR C . n 
C 3 42  THR 42  42  42  THR THR C . n 
C 3 43  PRO 43  43  43  PRO PRO C . n 
C 3 44  ASP 44  44  44  ASP ASP C . n 
C 3 45  ASN 45  45  45  ASN ASN C . n 
C 3 46  ALA 46  46  46  ALA ALA C . n 
C 3 47  THR 47  47  47  THR THR C . n 
C 3 48  VAL 48  48  48  VAL VAL C . n 
C 3 49  PRO 49  49  49  PRO PRO C . n 
C 3 50  HIS 50  50  50  HIS HIS C . n 
C 3 51  LYS 51  51  51  LYS LYS C . n 
C 3 52  GLN 52  52  52  GLN GLN C . n 
C 3 53  GLY 53  53  53  GLY GLY C . n 
C 3 54  SER 54  54  54  SER SER C . n 
C 3 55  ASP 55  55  55  ASP ASP C . n 
C 3 56  TYR 56  56  56  TYR TYR C . n 
C 3 57  VAL 57  57  57  VAL VAL C . n 
C 3 58  LEU 58  58  58  LEU LEU C . n 
C 3 59  VAL 59  59  59  VAL VAL C . n 
C 3 60  ALA 60  60  60  ALA ALA C . n 
C 3 61  GLY 61  61  61  GLY GLY C . n 
C 3 62  LEU 62  62  62  LEU LEU C . n 
C 3 63  ALA 63  63  63  ALA ALA C . n 
C 3 64  GLY 64  64  64  GLY GLY C . n 
C 3 65  ASP 65  65  65  ASP ASP C . n 
C 3 66  PRO 66  66  66  PRO PRO C . n 
C 3 67  ASN 67  67  67  ASN ASN C . n 
C 3 68  ARG 68  68  68  ARG ARG C . n 
C 3 69  PHE 69  69  69  PHE PHE C . n 
C 3 70  SER 70  70  70  SER SER C . n 
C 3 71  ALA 71  71  71  ALA ALA C . n 
C 3 72  TYR 72  72  72  TYR TYR C . n 
C 3 73  THR 73  73  73  THR THR C . n 
C 3 74  ARG 74  74  74  ARG ARG C . n 
C 3 75  SER 75  75  75  SER SER C . n 
C 3 76  GLN 76  76  76  GLN GLN C . n 
C 3 77  GLY 77  77  77  GLY GLY C . n 
C 3 78  GLY 78  78  78  GLY GLY C . n 
C 3 79  SER 79  79  79  SER SER C . n 
C 3 80  LYS 80  80  80  LYS LYS C . n 
C 3 81  PRO 81  81  81  PRO PRO C . n 
C 3 82  LEU 82  82  82  LEU LEU C . n 
C 3 83  VAL 83  83  83  VAL VAL C . n 
C 3 84  VAL 84  84  84  VAL VAL C . n 
C 3 85  LYS 85  85  85  LYS LYS C . n 
C 3 86  LEU 86  86  86  LEU LEU C . n 
C 3 87  VAL 87  87  87  VAL VAL C . n 
C 3 88  ASN 88  88  88  ASN ASN C . n 
C 3 89  ASP 89  89  89  ASP ASP C . n 
C 3 90  GLY 90  90  90  GLY GLY C . n 
C 3 91  VAL 91  91  91  VAL VAL C . n 
C 3 92  THR 92  92  92  THR THR C . n 
C 3 93  LEU 93  93  93  LEU LEU C . n 
C 3 94  GLU 94  94  94  GLU GLU C . n 
C 3 95  LEU 95  95  95  LEU LEU C . n 
C 3 96  THR 96  96  96  THR THR C . n 
C 3 97  ARG 97  97  97  ARG ARG C . n 
C 3 98  ASP 98  98  98  ASP ASP C . n 
C 3 99  GLY 99  99  99  GLY GLY C . n 
C 3 100 ALA 100 100 100 ALA ALA C . n 
C 3 101 SER 101 101 101 SER SER C . n 
C 3 102 ILE 102 102 102 ILE ILE C . n 
C 3 103 ASN 103 103 103 ASN ASN C . n 
C 3 104 GLY 104 104 104 GLY GLY C . n 
C 3 105 LYS 105 105 105 LYS LYS C . n 
C 3 106 ALA 106 106 106 ALA ALA C . n 
C 3 107 VAL 107 107 107 VAL VAL C . n 
C 3 108 SER 108 108 108 SER SER C . n 
C 3 109 VAL 109 109 109 VAL VAL C . n 
C 3 110 GLU 110 110 110 GLU GLU C . n 
C 3 111 LYS 111 111 111 LYS LYS C . n 
C 3 112 GLY 112 112 112 GLY GLY C . n 
C 3 113 VAL 113 113 113 VAL VAL C . n 
C 3 114 GLN 114 114 114 GLN GLN C . n 
C 3 115 TYR 115 115 115 TYR TYR C . n 
C 3 116 PRO 116 116 116 PRO PRO C . n 
C 3 117 GLN 117 117 117 GLN GLN C . n 
C 3 118 ASP 118 118 118 ASP ASP C . n 
C 3 119 ASP 119 119 119 ASP ASP C . n 
C 3 120 PRO 120 120 120 PRO PRO C . n 
C 3 121 ASN 121 121 121 ASN ASN C . n 
C 3 122 TYR 122 122 122 TYR TYR C . n 
C 3 123 ALA 123 123 123 ALA ALA C . n 
C 3 124 ILE 124 124 124 ILE ILE C . n 
C 3 125 ARG 125 125 125 ARG ARG C . n 
C 3 126 VAL 126 126 126 VAL VAL C . n 
C 3 127 TRP 127 127 127 TRP TRP C . n 
C 3 128 LYS 128 128 128 LYS LYS C . n 
C 3 129 SER 129 129 129 SER SER C . n 
C 3 130 GLY 130 130 130 GLY GLY C . n 
C 3 131 ASP 131 131 131 ASP ASP C . n 
C 3 132 LEU 132 132 132 LEU LEU C . n 
C 3 133 VAL 133 133 133 VAL VAL C . n 
C 3 134 MET 134 134 134 MET MET C . n 
C 3 135 ALA 135 135 135 ALA ALA C . n 
C 3 136 TYR 136 136 136 TYR TYR C . n 
C 3 137 SER 137 137 137 SER SER C . n 
C 3 138 ARG 138 138 138 ARG ARG C . n 
C 3 139 ARG 139 139 139 ARG ARG C . n 
C 3 140 THR 140 140 140 THR THR C . n 
C 3 141 ALA 141 141 141 ALA ALA C . n 
C 3 142 VAL 142 142 142 VAL VAL C . n 
C 3 143 TYR 143 143 143 TYR TYR C . n 
C 3 144 ALA 144 144 144 ALA ALA C . n 
C 3 145 TYR 145 145 145 TYR TYR C . n 
C 3 146 TYR 146 146 146 TYR TYR C . n 
C 3 147 THR 147 147 147 THR THR C . n 
C 3 148 GLY 148 148 148 GLY GLY C . n 
C 3 149 THR 149 149 149 THR THR C . n 
C 3 150 ALA 150 150 150 ALA ALA C . n 
C 3 151 VAL 151 151 151 VAL VAL C . n 
C 3 152 ASP 152 152 152 ASP ASP C . n 
C 3 153 VAL 153 153 153 VAL VAL C . n 
C 3 154 GLU 154 154 154 GLU GLU C . n 
C 3 155 GLN 155 155 155 GLN GLN C . n 
C 3 156 PRO 156 156 156 PRO PRO C . n 
C 3 157 VAL 157 157 157 VAL VAL C . n 
C 3 158 THR 158 158 158 THR THR C . n 
C 3 159 TYR 159 159 159 TYR TYR C . n 
C 3 160 ARG 160 160 160 ARG ARG C . n 
C 3 161 GLY 161 161 161 GLY GLY C . n 
C 3 162 ARG 162 162 162 ARG ARG C . n 
C 3 163 ALA 163 163 163 ALA ALA C . n 
C 3 164 THR 164 164 164 THR THR C . n 
C 3 165 GLY 165 165 165 GLY GLY C . n 
C 3 166 LEU 166 166 166 LEU LEU C . n 
C 3 167 CYS 167 167 167 CYS CYS C . n 
C 3 168 GLY 168 168 168 GLY GLY C . n 
C 3 169 ASN 169 169 169 ASN ASN C . n 
C 3 170 LEU 170 170 170 LEU LEU C . n 
C 3 171 ASN 171 171 171 ASN ASN C . n 
C 3 172 GLY 172 172 172 GLY GLY C . n 
D 1 1   GLN 1   0   ?   ?   ?   D . n 
D 1 2   GLY 2   1   1   GLY GLY D . n 
D 1 3   SER 3   2   2   SER SER D . n 
D 1 4   GLN 4   3   3   GLN GLN D . n 
D 1 5   VAL 5   4   4   VAL VAL D . n 
D 1 6   GLU 6   5   5   GLU GLU D . n 
D 1 7   PHE 7   6   6   PHE PHE D . n 
D 1 8   SER 8   7   7   SER SER D . n 
D 1 9   MET 9   8   8   MET MET D . n 
D 1 10  LYS 10  9   9   LYS LYS D . n 
D 1 11  MET 11  10  10  MET MET D . n 
D 1 12  THR 12  11  11  THR THR D . n 
D 1 13  GLY 13  12  12  GLY GLY D . n 
D 1 14  GLY 14  13  13  GLY GLY D . n 
D 1 15  GLU 15  14  14  GLU GLU D . n 
D 1 16  ILE 16  15  15  ILE ILE D . n 
D 1 17  PRO 17  16  16  PRO PRO D . n 
D 1 18  GLY 18  17  17  GLY GLY D . n 
D 1 19  GLY 19  18  18  GLY GLY D . n 
D 1 20  ASN 20  19  19  ASN ASN D . n 
D 1 21  ILE 21  20  20  ILE ILE D . n 
D 1 22  VAL 22  21  21  VAL VAL D . n 
D 1 23  LEU 23  22  22  LEU LEU D . n 
D 1 24  GLN 24  23  23  GLN GLN D . n 
D 1 25  GLY 25  24  24  GLY GLY D . n 
D 1 26  VAL 26  25  25  VAL VAL D . n 
D 1 27  LYS 27  26  26  LYS LYS D . n 
D 1 28  LEU 28  27  27  LEU LEU D . n 
D 1 29  ARG 29  28  28  ARG ARG D . n 
D 1 30  ILE 30  29  29  ILE ILE D . n 
D 1 31  VAL 31  30  30  VAL VAL D . n 
D 1 32  GLY 32  31  31  GLY GLY D . n 
D 1 33  GLU 33  32  32  GLU GLU D . n 
D 1 34  TRP 34  33  33  TRP TRP D . n 
D 1 35  VAL 35  34  34  VAL VAL D . n 
D 1 36  LEU 36  35  35  LEU LEU D . n 
D 1 37  LYS 37  36  36  LYS LYS D . n 
D 1 38  GLY 38  37  37  GLY GLY D . n 
D 1 39  SER 39  38  38  SER SER D . n 
D 1 40  SER 40  39  39  SER SER D . n 
D 1 41  GLY 41  40  40  GLY GLY D . n 
D 1 42  GLU 42  41  41  GLU GLU D . n 
D 1 43  SER 43  42  42  SER SER D . n 
D 1 44  VAL 44  43  43  VAL VAL D . n 
D 1 45  ARG 45  44  44  ARG ARG D . n 
D 1 46  ARG 46  45  45  ARG ARG D . n 
D 1 47  THR 47  46  46  THR THR D . n 
D 1 48  ASP 48  47  47  ASP ASP D . n 
D 1 49  VAL 49  48  48  VAL VAL D . n 
D 1 50  LYS 50  49  49  LYS LYS D . n 
D 1 51  VAL 51  50  50  VAL VAL D . n 
D 1 52  ASP 52  51  51  ASP ASP D . n 
D 1 53  ILE 53  52  52  ILE ILE D . n 
D 1 54  THR 54  53  53  THR THR D . n 
D 1 55  SER 55  54  54  SER SER D . n 
D 1 56  THR 56  55  55  THR THR D . n 
D 1 57  ALA 57  56  56  ALA ALA D . n 
D 1 58  GLY 58  57  57  GLY GLY D . n 
D 1 59  ASN 59  58  58  ASN ASN D . n 
D 1 60  GLN 60  59  59  GLN GLN D . n 
D 1 61  ASP 61  60  60  ASP ASP D . n 
D 1 62  ASN 62  61  61  ASN ASN D . n 
D 1 63  SER 63  62  62  SER SER D . n 
D 1 64  PHE 64  63  63  PHE PHE D . n 
D 1 65  ALA 65  64  64  ALA ALA D . n 
D 1 66  ILE 66  65  65  ILE ILE D . n 
D 1 67  GLN 67  66  66  GLN GLN D . n 
D 1 68  LEU 68  67  67  LEU LEU D . n 
D 1 69  ALA 69  68  68  ALA ALA D . n 
D 1 70  ASN 70  69  69  ASN ASN D . n 
D 1 71  TYR 71  70  70  TYR TYR D . n 
D 1 72  ALA 72  71  ?   ?   ?   D . n 
D 1 73  HIS 73  72  ?   ?   ?   D . n 
D 1 74  ASN 74  73  ?   ?   ?   D . n 
D 1 75  LYS 75  74  ?   ?   ?   D . n 
D 1 76  PRO 76  75  ?   ?   ?   D . n 
D 1 77  ASN 77  76  ?   ?   ?   D . n 
D 1 78  THR 78  77  77  THR THR D . n 
D 1 79  LYS 79  78  78  LYS LYS D . n 
D 1 80  TRP 80  79  79  TRP TRP D . n 
D 1 81  CSD 81  80  80  CSD CSD D . n 
D 1 82  ALA 82  81  81  ALA ALA D . n 
D 1 83  LEU 83  82  82  LEU LEU D . n 
D 1 84  LEU 84  83  83  LEU LEU D . n 
D 1 85  THR 85  84  84  THR THR D . n 
D 1 86  LYS 86  85  85  LYS LYS D . n 
D 1 87  LYS 87  86  86  LYS LYS D . n 
D 1 88  TYR 88  87  87  TYR TYR D . n 
D 1 89  PRO 89  88  88  PRO PRO D . n 
D 1 90  GLU 90  89  89  GLU GLU D . n 
D 1 91  ARG 91  90  90  ARG ARG D . n 
D 1 92  LYS 92  91  91  LYS LYS D . n 
D 1 93  PRO 93  92  92  PRO PRO D . n 
D 1 94  ASP 94  93  93  ASP ASP D . n 
D 1 95  VAL 95  94  94  VAL VAL D . n 
D 1 96  LEU 96  95  95  LEU LEU D . n 
D 1 97  ALA 97  96  96  ALA ALA D . n 
D 1 98  PHE 98  97  97  PHE PHE D . n 
D 1 99  GLY 99  98  98  GLY GLY D . n 
D 1 100 TRP 100 99  99  TRP TRP D . n 
D 1 101 GLY 101 100 100 GLY GLY D . n 
D 1 102 ASN 102 101 101 ASN ASN D . n 
D 1 103 GLU 103 102 102 GLU GLU D . n 
D 1 104 GLN 104 103 103 GLN GLN D . n 
D 1 105 VAL 105 104 104 VAL VAL D . n 
D 1 106 ASP 106 105 105 ASP ASP D . n 
D 1 107 SER 107 106 106 SER SER D . n 
D 1 108 LYS 108 107 107 LYS LYS D . n 
D 1 109 ALA 109 108 108 ALA ALA D . n 
D 1 110 SER 110 109 109 SER SER D . n 
D 1 111 VAL 111 110 110 VAL VAL D . n 
D 1 112 THR 112 111 111 THR THR D . n 
D 1 113 ILE 113 112 112 ILE ILE D . n 
D 1 114 GLY 114 113 113 GLY GLY D . n 
E 2 1   SER 1   1   1   SER SER E . n 
E 2 2   VAL 2   2   2   VAL VAL E . n 
E 2 3   THR 3   3   3   THR THR E . n 
E 2 4   ILE 4   4   4   ILE ILE E . n 
E 2 5   THR 5   5   5   THR THR E . n 
E 2 6   ILE 6   6   6   ILE ILE E . n 
E 2 7   ASN 7   7   7   ASN ASN E . n 
E 2 8   GLN 8   8   8   GLN GLN E . n 
E 2 9   LYS 9   9   9   LYS LYS E . n 
E 2 10  GLY 10  10  10  GLY GLY E . n 
E 2 11  GLU 11  11  11  GLU GLU E . n 
E 2 12  ILE 12  12  12  ILE ILE E . n 
E 2 13  THR 13  13  13  THR THR E . n 
E 2 14  GLU 14  14  14  GLU GLU E . n 
E 2 15  GLU 15  15  15  GLU GLU E . n 
E 2 16  GLN 16  16  16  GLN GLN E . n 
E 2 17  LYS 17  17  17  LYS LYS E . n 
E 2 18  GLN 18  18  18  GLN GLN E . n 
E 2 19  ARG 19  19  19  ARG ARG E . n 
E 2 20  ALA 20  20  20  ALA ALA E . n 
E 2 21  GLN 21  21  21  GLN GLN E . n 
E 2 22  GLY 22  22  22  GLY GLY E . n 
E 2 23  ASP 23  23  23  ASP ASP E . n 
E 2 24  ASP 24  24  24  ASP ASP E . n 
E 2 25  TRP 25  25  25  TRP TRP E . n 
E 2 26  PRO 26  26  26  PRO PRO E . n 
E 2 27  TYR 27  27  27  TYR TYR E . n 
E 2 28  GLY 28  28  28  GLY GLY E . n 
E 2 29  GLN 29  29  29  GLN GLN E . n 
E 2 30  CYS 30  30  30  CYS CYS E . n 
E 2 31  LYS 31  31  31  LYS LYS E . n 
E 2 32  GLU 32  32  32  GLU GLU E . n 
E 2 33  ASP 33  33  33  ASP ASP E . n 
E 2 34  GLN 34  34  34  GLN GLN E . n 
E 2 35  LYS 35  35  35  LYS LYS E . n 
E 2 36  LYS 36  36  36  LYS LYS E . n 
E 2 37  SER 37  37  37  SER SER E . n 
E 2 38  GLU 38  38  38  GLU GLU E . n 
E 2 39  TRP 39  39  39  TRP TRP E . n 
E 2 40  LYS 40  40  40  LYS LYS E . n 
E 2 41  ASP 41  41  41  ASP ASP E . n 
E 2 42  SER 42  42  42  SER SER E . n 
E 2 43  ASP 43  43  43  ASP ASP E . n 
E 2 44  PHE 44  44  44  PHE PHE E . n 
E 2 45  LEU 45  45  45  LEU LEU E . n 
E 2 46  PRO 46  46  46  PRO PRO E . n 
E 2 47  ASN 47  47  47  ASN ASN E . n 
E 2 48  THR 48  48  48  THR THR E . n 
E 2 49  GLN 49  49  49  GLN GLN E . n 
E 2 50  ALA 50  50  50  ALA ALA E . n 
E 2 51  CYS 51  51  51  CYS CYS E . n 
E 2 52  TYR 52  52  52  TYR TYR E . n 
E 2 53  ILE 53  53  53  ILE ILE E . n 
E 2 54  GLY 54  54  54  GLY GLY E . n 
E 2 55  SER 55  55  55  SER SER E . n 
E 2 56  ILE 56  56  56  ILE ILE E . n 
E 2 57  LEU 57  57  57  LEU LEU E . n 
E 2 58  LEU 58  58  58  LEU LEU E . n 
E 2 59  THR 59  59  59  THR THR E . n 
E 2 60  THR 60  60  60  THR THR E . n 
E 2 61  ALA 61  61  61  ALA ALA E . n 
E 2 62  ARG 62  62  62  ARG ARG E . n 
E 2 63  LYS 63  63  63  LYS LYS E . n 
E 2 64  THR 64  64  64  THR THR E . n 
E 2 65  THR 65  65  65  THR THR E . n 
E 2 66  TYR 66  66  66  TYR TYR E . n 
E 2 67  SER 67  67  67  SER SER E . n 
F 3 1   GLY 1   1   ?   ?   ?   F . n 
F 3 2   ALA 2   2   ?   ?   ?   F . n 
F 3 3   SER 3   3   ?   ?   ?   F . n 
F 3 4   SER 4   4   4   SER SER F . n 
F 3 5   VAL 5   5   5   VAL VAL F . n 
F 3 6   ASP 6   6   6   ASP ASP F . n 
F 3 7   ASP 7   7   7   ASP ASP F . n 
F 3 8   TYR 8   8   8   TYR TYR F . n 
F 3 9   ASN 9   9   9   ASN ASN F . n 
F 3 10  PRO 10  10  10  PRO PRO F . n 
F 3 11  ALA 11  11  11  ALA ALA F . n 
F 3 12  PHE 12  12  12  PHE PHE F . n 
F 3 13  ASP 13  13  13  ASP ASP F . n 
F 3 14  ASN 14  14  14  ASN ASN F . n 
F 3 15  THR 15  15  15  THR THR F . n 
F 3 16  HIS 16  16  16  HIS HIS F . n 
F 3 17  TYR 17  17  17  TYR TYR F . n 
F 3 18  SER 18  18  18  SER SER F . n 
F 3 19  ARG 19  19  19  ARG ARG F . n 
F 3 20  PHE 20  20  20  PHE PHE F . n 
F 3 21  HIS 21  21  21  HIS HIS F . n 
F 3 22  LEU 22  22  22  LEU LEU F . n 
F 3 23  LEU 23  23  23  LEU LEU F . n 
F 3 24  ILE 24  24  24  ILE ILE F . n 
F 3 25  GLU 25  25  25  GLU GLU F . n 
F 3 26  THR 26  26  26  THR THR F . n 
F 3 27  ASN 27  27  27  ASN ASN F . n 
F 3 28  GLY 28  28  28  GLY GLY F . n 
F 3 29  ILE 29  29  29  ILE ILE F . n 
F 3 30  THR 30  30  30  THR THR F . n 
F 3 31  LYS 31  31  31  LYS LYS F . n 
F 3 32  PRO 32  32  32  PRO PRO F . n 
F 3 33  CYS 33  33  33  CYS CYS F . n 
F 3 34  ILE 34  34  34  ILE ILE F . n 
F 3 35  VAL 35  35  35  VAL VAL F . n 
F 3 36  SER 36  36  36  SER SER F . n 
F 3 37  THR 37  37  37  THR THR F . n 
F 3 38  GLU 38  38  38  GLU GLU F . n 
F 3 39  ASN 39  39  39  ASN ASN F . n 
F 3 40  VAL 40  40  40  VAL VAL F . n 
F 3 41  TYR 41  41  41  TYR TYR F . n 
F 3 42  THR 42  42  42  THR THR F . n 
F 3 43  PRO 43  43  43  PRO PRO F . n 
F 3 44  ASP 44  44  44  ASP ASP F . n 
F 3 45  ASN 45  45  45  ASN ASN F . n 
F 3 46  ALA 46  46  46  ALA ALA F . n 
F 3 47  THR 47  47  47  THR THR F . n 
F 3 48  VAL 48  48  48  VAL VAL F . n 
F 3 49  PRO 49  49  49  PRO PRO F . n 
F 3 50  HIS 50  50  50  HIS HIS F . n 
F 3 51  LYS 51  51  51  LYS LYS F . n 
F 3 52  GLN 52  52  52  GLN GLN F . n 
F 3 53  GLY 53  53  53  GLY GLY F . n 
F 3 54  SER 54  54  54  SER SER F . n 
F 3 55  ASP 55  55  55  ASP ASP F . n 
F 3 56  TYR 56  56  56  TYR TYR F . n 
F 3 57  VAL 57  57  57  VAL VAL F . n 
F 3 58  LEU 58  58  58  LEU LEU F . n 
F 3 59  VAL 59  59  59  VAL VAL F . n 
F 3 60  ALA 60  60  60  ALA ALA F . n 
F 3 61  GLY 61  61  61  GLY GLY F . n 
F 3 62  LEU 62  62  62  LEU LEU F . n 
F 3 63  ALA 63  63  63  ALA ALA F . n 
F 3 64  GLY 64  64  64  GLY GLY F . n 
F 3 65  ASP 65  65  65  ASP ASP F . n 
F 3 66  PRO 66  66  66  PRO PRO F . n 
F 3 67  ASN 67  67  67  ASN ASN F . n 
F 3 68  ARG 68  68  68  ARG ARG F . n 
F 3 69  PHE 69  69  69  PHE PHE F . n 
F 3 70  SER 70  70  70  SER SER F . n 
F 3 71  ALA 71  71  71  ALA ALA F . n 
F 3 72  TYR 72  72  72  TYR TYR F . n 
F 3 73  THR 73  73  73  THR THR F . n 
F 3 74  ARG 74  74  74  ARG ARG F . n 
F 3 75  SER 75  75  75  SER SER F . n 
F 3 76  GLN 76  76  76  GLN GLN F . n 
F 3 77  GLY 77  77  77  GLY GLY F . n 
F 3 78  GLY 78  78  78  GLY GLY F . n 
F 3 79  SER 79  79  79  SER SER F . n 
F 3 80  LYS 80  80  80  LYS LYS F . n 
F 3 81  PRO 81  81  81  PRO PRO F . n 
F 3 82  LEU 82  82  82  LEU LEU F . n 
F 3 83  VAL 83  83  83  VAL VAL F . n 
F 3 84  VAL 84  84  84  VAL VAL F . n 
F 3 85  LYS 85  85  85  LYS LYS F . n 
F 3 86  LEU 86  86  86  LEU LEU F . n 
F 3 87  VAL 87  87  87  VAL VAL F . n 
F 3 88  ASN 88  88  88  ASN ASN F . n 
F 3 89  ASP 89  89  89  ASP ASP F . n 
F 3 90  GLY 90  90  90  GLY GLY F . n 
F 3 91  VAL 91  91  91  VAL VAL F . n 
F 3 92  THR 92  92  92  THR THR F . n 
F 3 93  LEU 93  93  93  LEU LEU F . n 
F 3 94  GLU 94  94  94  GLU GLU F . n 
F 3 95  LEU 95  95  95  LEU LEU F . n 
F 3 96  THR 96  96  96  THR THR F . n 
F 3 97  ARG 97  97  97  ARG ARG F . n 
F 3 98  ASP 98  98  98  ASP ASP F . n 
F 3 99  GLY 99  99  99  GLY GLY F . n 
F 3 100 ALA 100 100 100 ALA ALA F . n 
F 3 101 SER 101 101 101 SER SER F . n 
F 3 102 ILE 102 102 102 ILE ILE F . n 
F 3 103 ASN 103 103 103 ASN ASN F . n 
F 3 104 GLY 104 104 104 GLY GLY F . n 
F 3 105 LYS 105 105 105 LYS LYS F . n 
F 3 106 ALA 106 106 106 ALA ALA F . n 
F 3 107 VAL 107 107 107 VAL VAL F . n 
F 3 108 SER 108 108 108 SER SER F . n 
F 3 109 VAL 109 109 109 VAL VAL F . n 
F 3 110 GLU 110 110 110 GLU GLU F . n 
F 3 111 LYS 111 111 111 LYS LYS F . n 
F 3 112 GLY 112 112 112 GLY GLY F . n 
F 3 113 VAL 113 113 113 VAL VAL F . n 
F 3 114 GLN 114 114 114 GLN GLN F . n 
F 3 115 TYR 115 115 115 TYR TYR F . n 
F 3 116 PRO 116 116 116 PRO PRO F . n 
F 3 117 GLN 117 117 117 GLN GLN F . n 
F 3 118 ASP 118 118 118 ASP ASP F . n 
F 3 119 ASP 119 119 119 ASP ASP F . n 
F 3 120 PRO 120 120 120 PRO PRO F . n 
F 3 121 ASN 121 121 121 ASN ASN F . n 
F 3 122 TYR 122 122 122 TYR TYR F . n 
F 3 123 ALA 123 123 123 ALA ALA F . n 
F 3 124 ILE 124 124 124 ILE ILE F . n 
F 3 125 ARG 125 125 125 ARG ARG F . n 
F 3 126 VAL 126 126 126 VAL VAL F . n 
F 3 127 TRP 127 127 127 TRP TRP F . n 
F 3 128 LYS 128 128 128 LYS LYS F . n 
F 3 129 SER 129 129 129 SER SER F . n 
F 3 130 GLY 130 130 130 GLY GLY F . n 
F 3 131 ASP 131 131 131 ASP ASP F . n 
F 3 132 LEU 132 132 132 LEU LEU F . n 
F 3 133 VAL 133 133 133 VAL VAL F . n 
F 3 134 MET 134 134 134 MET MET F . n 
F 3 135 ALA 135 135 135 ALA ALA F . n 
F 3 136 TYR 136 136 136 TYR TYR F . n 
F 3 137 SER 137 137 137 SER SER F . n 
F 3 138 ARG 138 138 138 ARG ARG F . n 
F 3 139 ARG 139 139 139 ARG ARG F . n 
F 3 140 THR 140 140 140 THR THR F . n 
F 3 141 ALA 141 141 141 ALA ALA F . n 
F 3 142 VAL 142 142 142 VAL VAL F . n 
F 3 143 TYR 143 143 143 TYR TYR F . n 
F 3 144 ALA 144 144 144 ALA ALA F . n 
F 3 145 TYR 145 145 145 TYR TYR F . n 
F 3 146 TYR 146 146 146 TYR TYR F . n 
F 3 147 THR 147 147 147 THR THR F . n 
F 3 148 GLY 148 148 148 GLY GLY F . n 
F 3 149 THR 149 149 149 THR THR F . n 
F 3 150 ALA 150 150 150 ALA ALA F . n 
F 3 151 VAL 151 151 151 VAL VAL F . n 
F 3 152 ASP 152 152 152 ASP ASP F . n 
F 3 153 VAL 153 153 153 VAL VAL F . n 
F 3 154 GLU 154 154 154 GLU GLU F . n 
F 3 155 GLN 155 155 155 GLN GLN F . n 
F 3 156 PRO 156 156 156 PRO PRO F . n 
F 3 157 VAL 157 157 157 VAL VAL F . n 
F 3 158 THR 158 158 158 THR THR F . n 
F 3 159 TYR 159 159 159 TYR TYR F . n 
F 3 160 ARG 160 160 160 ARG ARG F . n 
F 3 161 GLY 161 161 161 GLY GLY F . n 
F 3 162 ARG 162 162 162 ARG ARG F . n 
F 3 163 ALA 163 163 163 ALA ALA F . n 
F 3 164 THR 164 164 164 THR THR F . n 
F 3 165 GLY 165 165 165 GLY GLY F . n 
F 3 166 LEU 166 166 166 LEU LEU F . n 
F 3 167 CYS 167 167 167 CYS CYS F . n 
F 3 168 GLY 168 168 168 GLY GLY F . n 
F 3 169 ASN 169 169 169 ASN ASN F . n 
F 3 170 LEU 170 170 170 LEU LEU F . n 
F 3 171 ASN 171 171 171 ASN ASN F . n 
F 3 172 GLY 172 172 ?   ?   ?   F . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1L6M ? ? A1L6M ? ? 'SUBJECT OF INVESTIGATION' ? 
2 LUT   ? ? LUT   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 PLC   ? ? PLC   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 4 LUT   1  201 210 LUT   LUT A . 
H 5 AZI   1  202 2   AZI   AZI A . 
I 5 AZI   1  101 1   AZI   AZI B . 
J 6 PLC   1  201 211 PLC   PLC C . 
K 7 A1L6M 1  202 201 A1L6M BIL C . 
L 6 PLC   1  203 212 PLC   PLC C . 
M 5 AZI   1  204 3   AZI   AZI C . 
N 4 LUT   1  201 210 LUT   LUT D . 
O 6 PLC   1  202 211 PLC   PLC D . 
P 5 AZI   1  203 6   AZI   AZI D . 
Q 5 AZI   1  101 4   AZI   AZI E . 
R 5 AZI   1  102 5   AZI   AZI E . 
S 6 PLC   1  201 212 PLC   PLC F . 
T 7 A1L6M 1  202 201 A1L6M BIL F . 
U 8 HOH   1  301 119 HOH   HOH A . 
U 8 HOH   2  302 27  HOH   HOH A . 
U 8 HOH   3  303 59  HOH   HOH A . 
U 8 HOH   4  304 53  HOH   HOH A . 
U 8 HOH   5  305 83  HOH   HOH A . 
U 8 HOH   6  306 143 HOH   HOH A . 
U 8 HOH   7  307 148 HOH   HOH A . 
U 8 HOH   8  308 151 HOH   HOH A . 
U 8 HOH   9  309 127 HOH   HOH A . 
U 8 HOH   10 310 42  HOH   HOH A . 
U 8 HOH   11 311 37  HOH   HOH A . 
U 8 HOH   12 312 56  HOH   HOH A . 
U 8 HOH   13 313 17  HOH   HOH A . 
U 8 HOH   14 314 166 HOH   HOH A . 
U 8 HOH   15 315 32  HOH   HOH A . 
U 8 HOH   16 316 25  HOH   HOH A . 
U 8 HOH   17 317 120 HOH   HOH A . 
U 8 HOH   18 318 164 HOH   HOH A . 
U 8 HOH   19 319 165 HOH   HOH A . 
U 8 HOH   20 320 149 HOH   HOH A . 
U 8 HOH   21 321 125 HOH   HOH A . 
U 8 HOH   22 322 28  HOH   HOH A . 
U 8 HOH   23 323 64  HOH   HOH A . 
U 8 HOH   24 324 71  HOH   HOH A . 
U 8 HOH   25 325 57  HOH   HOH A . 
U 8 HOH   26 326 54  HOH   HOH A . 
U 8 HOH   27 327 117 HOH   HOH A . 
U 8 HOH   28 328 41  HOH   HOH A . 
U 8 HOH   29 329 106 HOH   HOH A . 
U 8 HOH   30 330 52  HOH   HOH A . 
U 8 HOH   31 331 91  HOH   HOH A . 
U 8 HOH   32 332 139 HOH   HOH A . 
V 8 HOH   1  201 118 HOH   HOH B . 
V 8 HOH   2  202 144 HOH   HOH B . 
V 8 HOH   3  203 10  HOH   HOH B . 
V 8 HOH   4  204 163 HOH   HOH B . 
V 8 HOH   5  205 167 HOH   HOH B . 
V 8 HOH   6  206 169 HOH   HOH B . 
V 8 HOH   7  207 90  HOH   HOH B . 
V 8 HOH   8  208 108 HOH   HOH B . 
V 8 HOH   9  209 82  HOH   HOH B . 
V 8 HOH   10 210 113 HOH   HOH B . 
V 8 HOH   11 211 131 HOH   HOH B . 
V 8 HOH   12 212 116 HOH   HOH B . 
V 8 HOH   13 213 137 HOH   HOH B . 
V 8 HOH   14 214 78  HOH   HOH B . 
V 8 HOH   15 215 152 HOH   HOH B . 
V 8 HOH   16 216 96  HOH   HOH B . 
V 8 HOH   17 217 134 HOH   HOH B . 
V 8 HOH   18 218 101 HOH   HOH B . 
V 8 HOH   19 219 130 HOH   HOH B . 
W 8 HOH   1  301 68  HOH   HOH C . 
W 8 HOH   2  302 73  HOH   HOH C . 
W 8 HOH   3  303 153 HOH   HOH C . 
W 8 HOH   4  304 146 HOH   HOH C . 
W 8 HOH   5  305 55  HOH   HOH C . 
W 8 HOH   6  306 100 HOH   HOH C . 
W 8 HOH   7  307 141 HOH   HOH C . 
W 8 HOH   8  308 14  HOH   HOH C . 
W 8 HOH   9  309 1   HOH   HOH C . 
W 8 HOH   10 310 50  HOH   HOH C . 
W 8 HOH   11 311 18  HOH   HOH C . 
W 8 HOH   12 312 79  HOH   HOH C . 
W 8 HOH   13 313 7   HOH   HOH C . 
W 8 HOH   14 314 24  HOH   HOH C . 
W 8 HOH   15 315 23  HOH   HOH C . 
W 8 HOH   16 316 29  HOH   HOH C . 
W 8 HOH   17 317 69  HOH   HOH C . 
W 8 HOH   18 318 26  HOH   HOH C . 
W 8 HOH   19 319 115 HOH   HOH C . 
W 8 HOH   20 320 109 HOH   HOH C . 
W 8 HOH   21 321 66  HOH   HOH C . 
W 8 HOH   22 322 171 HOH   HOH C . 
W 8 HOH   23 323 16  HOH   HOH C . 
W 8 HOH   24 324 138 HOH   HOH C . 
W 8 HOH   25 325 2   HOH   HOH C . 
W 8 HOH   26 326 93  HOH   HOH C . 
W 8 HOH   27 327 31  HOH   HOH C . 
W 8 HOH   28 328 168 HOH   HOH C . 
W 8 HOH   29 329 30  HOH   HOH C . 
W 8 HOH   30 330 40  HOH   HOH C . 
W 8 HOH   31 331 60  HOH   HOH C . 
W 8 HOH   32 332 87  HOH   HOH C . 
W 8 HOH   33 333 11  HOH   HOH C . 
W 8 HOH   34 334 4   HOH   HOH C . 
W 8 HOH   35 335 65  HOH   HOH C . 
W 8 HOH   36 336 159 HOH   HOH C . 
W 8 HOH   37 337 114 HOH   HOH C . 
W 8 HOH   38 338 44  HOH   HOH C . 
W 8 HOH   39 339 111 HOH   HOH C . 
W 8 HOH   40 340 136 HOH   HOH C . 
W 8 HOH   41 341 62  HOH   HOH C . 
W 8 HOH   42 342 86  HOH   HOH C . 
W 8 HOH   43 343 3   HOH   HOH C . 
W 8 HOH   44 344 80  HOH   HOH C . 
W 8 HOH   45 345 174 HOH   HOH C . 
W 8 HOH   46 346 5   HOH   HOH C . 
W 8 HOH   47 347 81  HOH   HOH C . 
W 8 HOH   48 348 129 HOH   HOH C . 
W 8 HOH   49 349 8   HOH   HOH C . 
W 8 HOH   50 350 110 HOH   HOH C . 
W 8 HOH   51 351 58  HOH   HOH C . 
W 8 HOH   52 352 104 HOH   HOH C . 
W 8 HOH   53 353 102 HOH   HOH C . 
W 8 HOH   54 354 92  HOH   HOH C . 
W 8 HOH   55 355 51  HOH   HOH C . 
W 8 HOH   56 356 133 HOH   HOH C . 
W 8 HOH   57 357 173 HOH   HOH C . 
X 8 HOH   1  301 63  HOH   HOH D . 
X 8 HOH   2  302 99  HOH   HOH D . 
X 8 HOH   3  303 21  HOH   HOH D . 
X 8 HOH   4  304 9   HOH   HOH D . 
X 8 HOH   5  305 128 HOH   HOH D . 
X 8 HOH   6  306 75  HOH   HOH D . 
X 8 HOH   7  307 22  HOH   HOH D . 
X 8 HOH   8  308 145 HOH   HOH D . 
X 8 HOH   9  309 12  HOH   HOH D . 
X 8 HOH   10 310 172 HOH   HOH D . 
X 8 HOH   11 311 122 HOH   HOH D . 
X 8 HOH   12 312 6   HOH   HOH D . 
X 8 HOH   13 313 156 HOH   HOH D . 
X 8 HOH   14 314 39  HOH   HOH D . 
X 8 HOH   15 315 43  HOH   HOH D . 
X 8 HOH   16 316 162 HOH   HOH D . 
X 8 HOH   17 317 88  HOH   HOH D . 
X 8 HOH   18 318 147 HOH   HOH D . 
X 8 HOH   19 319 107 HOH   HOH D . 
X 8 HOH   20 320 150 HOH   HOH D . 
X 8 HOH   21 321 61  HOH   HOH D . 
X 8 HOH   22 322 35  HOH   HOH D . 
X 8 HOH   23 323 48  HOH   HOH D . 
X 8 HOH   24 324 89  HOH   HOH D . 
X 8 HOH   25 325 154 HOH   HOH D . 
X 8 HOH   26 326 49  HOH   HOH D . 
Y 8 HOH   1  201 95  HOH   HOH E . 
Y 8 HOH   2  202 13  HOH   HOH E . 
Y 8 HOH   3  203 97  HOH   HOH E . 
Y 8 HOH   4  204 103 HOH   HOH E . 
Y 8 HOH   5  205 140 HOH   HOH E . 
Y 8 HOH   6  206 98  HOH   HOH E . 
Y 8 HOH   7  207 72  HOH   HOH E . 
Y 8 HOH   8  208 76  HOH   HOH E . 
Y 8 HOH   9  209 124 HOH   HOH E . 
Y 8 HOH   10 210 121 HOH   HOH E . 
Y 8 HOH   11 211 157 HOH   HOH E . 
Y 8 HOH   12 212 70  HOH   HOH E . 
Y 8 HOH   13 213 77  HOH   HOH E . 
Y 8 HOH   14 214 123 HOH   HOH E . 
Y 8 HOH   15 215 33  HOH   HOH E . 
Y 8 HOH   16 216 19  HOH   HOH E . 
Y 8 HOH   17 217 142 HOH   HOH E . 
Y 8 HOH   18 218 94  HOH   HOH E . 
Z 8 HOH   1  301 36  HOH   HOH F . 
Z 8 HOH   2  302 105 HOH   HOH F . 
Z 8 HOH   3  303 170 HOH   HOH F . 
Z 8 HOH   4  304 45  HOH   HOH F . 
Z 8 HOH   5  305 84  HOH   HOH F . 
Z 8 HOH   6  306 20  HOH   HOH F . 
Z 8 HOH   7  307 135 HOH   HOH F . 
Z 8 HOH   8  308 132 HOH   HOH F . 
Z 8 HOH   9  309 161 HOH   HOH F . 
Z 8 HOH   10 310 112 HOH   HOH F . 
Z 8 HOH   11 311 38  HOH   HOH F . 
Z 8 HOH   12 312 15  HOH   HOH F . 
Z 8 HOH   13 313 67  HOH   HOH F . 
Z 8 HOH   14 314 74  HOH   HOH F . 
Z 8 HOH   15 315 85  HOH   HOH F . 
Z 8 HOH   16 316 46  HOH   HOH F . 
Z 8 HOH   17 317 34  HOH   HOH F . 
Z 8 HOH   18 318 155 HOH   HOH F . 
Z 8 HOH   19 319 160 HOH   HOH F . 
Z 8 HOH   20 320 158 HOH   HOH F . 
Z 8 HOH   21 321 126 HOH   HOH F . 
Z 8 HOH   22 322 47  HOH   HOH F . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 C LYS 111 ? CD  ? C LYS 111 CD  
2  1 Y 1 C LYS 111 ? CE  ? C LYS 111 CE  
3  1 Y 1 C LYS 111 ? NZ  ? C LYS 111 NZ  
4  1 Y 1 E LYS 40  ? CG  ? E LYS 40  CG  
5  1 Y 1 E LYS 40  ? CD  ? E LYS 40  CD  
6  1 Y 1 E LYS 40  ? CE  ? E LYS 40  CE  
7  1 Y 1 E LYS 40  ? NZ  ? E LYS 40  NZ  
8  1 Y 1 F ASP 44  ? CG  ? F ASP 44  CG  
9  1 Y 1 F ASP 44  ? OD1 ? F ASP 44  OD1 
10 1 Y 1 F ASP 44  ? OD2 ? F ASP 44  OD2 
11 1 Y 1 F LYS 51  ? CG  ? F LYS 51  CG  
12 1 Y 1 F LYS 51  ? CD  ? F LYS 51  CD  
13 1 Y 1 F LYS 51  ? CE  ? F LYS 51  CE  
14 1 Y 1 F LYS 51  ? NZ  ? F LYS 51  NZ  
15 1 Y 1 F THR 164 ? OG1 ? F THR 164 OG1 
16 1 Y 1 F THR 164 ? CG2 ? F THR 164 CG2 
17 1 Y 1 F ASN 169 ? CG  ? F ASN 169 CG  
18 1 Y 1 F ASN 169 ? OD1 ? F ASN 169 OD1 
19 1 Y 1 F ASN 169 ? ND2 ? F ASN 169 ND2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0430 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KUE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.570 
_cell.length_a_esd                 ? 
_cell.length_b                     87.256 
_cell.length_b_esd                 ? 
_cell.length_c                     167.609 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KUE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KUE 
_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             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.30 
_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    '0.1 M Tris-HCl pH 8.5, 0.2 M MgCl2, 30% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            288 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 12M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-11-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9792 
_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                        'SSRF BEAMLINE BL17UM' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17UM 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KUE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.99 
_reflns.d_resolution_low                               47.57 
_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                                     48786 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                24.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.04 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.313 
_reflns.pdbx_Rpim_I_all                                0.062 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1216322 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.307 
_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                                    1.99 
_reflns_shell.d_res_low                                     2.04 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           49285 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3470 
_reflns_shell.percent_possible_obs                          99.2 
_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                               14.2 
_reflns_shell.pdbx_chi_squared                              1.08 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               1.863 
_reflns_shell.pdbx_Rpim_I_all                               0.489 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.412 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.796 
_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]                            2.13 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -1.28 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.86 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               38.229 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.939 
_refine.correlation_coeff_Fo_to_Fc_free          0.910 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9KUE 
_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                            1.99 
_refine.ls_d_res_low                             31.60 
_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                     46216 
_refine.ls_number_reflns_R_free                  2456 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.22536 
_refine.ls_R_factor_R_free                       0.26679 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.22318 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.228 
_refine.pdbx_overall_ESU_R_Free                  0.192 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             13.610 
_refine.overall_SU_ML                            0.180 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.99 
_refine_hist.d_res_low                        31.60 
_refine_hist.number_atoms_solvent             174 
_refine_hist.number_atoms_total               5823 
_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        5259 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         390 
_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' ? 0.011  0.012  5748  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.016  5392  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.107  1.826  7775  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.016  1.758  12438 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.966  5.000  676   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.732 5.000  96    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.692 10.000 883   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.106  0.200  834   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  6728  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  1270  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.386  1.495  2728  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.385  1.497  2729  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.238  2.690  3396  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.238  2.691  3397  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.850  1.680  3020  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.716  1.669  3007  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.782  3.006  4374  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.848  14.54  5897  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.826  14.40  5865  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.991 
_refine_ls_shell.d_res_low                        2.042 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             189 
_refine_ls_shell.number_reflns_R_work             3261 
_refine_ls_shell.percent_reflns_obs               99.08 
_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                  0.348 
_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   20 
_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                  0.358 
# 
_struct.entry_id                     9KUE 
_struct.title                        'Crystal structure of the soluble green pigment protein from Tettigonia cantans' 
_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        9KUE 
_struct_keywords.text            
'carotenoid binding, bilin binding, carotenoid carrier, transport protein, vitellogenin, bichromoprotein' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
J N N 6 ? 
K N N 7 ? 
L N N 6 ? 
M N N 5 ? 
N N N 4 ? 
O N N 6 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
S N N 6 ? 
T N N 7 ? 
U N N 8 ? 
V N N 8 ? 
W N N 8 ? 
X N N 8 ? 
Y N N 8 ? 
Z N N 8 ? 
# 
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 PDB 9KUE 9KUE ? 1 ? 1 
2 PDB 9KUE 9KUE ? 2 ? 1 
3 PDB 9KUE 9KUE ? 3 ? 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 9KUE A 1 ? 114 ? 9KUE 0 ? 113 ? 0 113 
2 2 9KUE B 1 ? 67  ? 9KUE 1 ? 67  ? 1 67  
3 3 9KUE C 1 ? 172 ? 9KUE 1 ? 172 ? 1 172 
4 1 9KUE D 1 ? 114 ? 9KUE 0 ? 113 ? 0 113 
5 2 9KUE E 1 ? 67  ? 9KUE 1 ? 67  ? 1 67  
6 3 9KUE F 1 ? 172 ? 9KUE 1 ? 172 ? 1 172 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 25800 ? 
1 MORE         -79   ? 
1 'SSA (A^2)'  26780 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'native gel electrophoresis' ? 
2 1 cross-linking                ? 
3 1 'gel filtration'             ? 
# 
_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 ASN A 20  ? GLN A 24  ? ASN A 19  GLN A 23  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 57  ? ASN A 59  ? ALA A 56  ASN A 58  5 ? 3  
HELX_P HELX_P3  AA3 THR B 13  ? GLY B 22  ? THR B 13  GLY B 22  1 ? 10 
HELX_P HELX_P4  AA4 PRO B 26  ? GLN B 34  ? PRO B 26  GLN B 34  1 ? 9  
HELX_P HELX_P5  AA5 LYS B 36  ? ASP B 41  ? LYS B 36  ASP B 41  1 ? 6  
HELX_P HELX_P6  AA6 THR B 48  ? THR B 59  ? THR B 48  THR B 59  1 ? 12 
HELX_P HELX_P7  AA7 SER C 4   ? TYR C 8   ? SER C 4   TYR C 8   5 ? 5  
HELX_P HELX_P8  AA8 SER C 18  ? ASN C 27  ? SER C 18  ASN C 27  1 ? 10 
HELX_P HELX_P9  AA9 SER C 108 ? GLY C 112 ? SER C 108 GLY C 112 5 ? 5  
HELX_P HELX_P10 AB1 THR C 158 ? ARG C 160 ? THR C 158 ARG C 160 5 ? 3  
HELX_P HELX_P11 AB2 ASN D 20  ? GLN D 24  ? ASN D 19  GLN D 23  5 ? 5  
HELX_P HELX_P12 AB3 ALA D 57  ? ASN D 59  ? ALA D 56  ASN D 58  5 ? 3  
HELX_P HELX_P13 AB4 THR E 13  ? GLY E 22  ? THR E 13  GLY E 22  1 ? 10 
HELX_P HELX_P14 AB5 PRO E 26  ? GLN E 34  ? PRO E 26  GLN E 34  1 ? 9  
HELX_P HELX_P15 AB6 LYS E 36  ? ASP E 41  ? LYS E 36  ASP E 41  1 ? 6  
HELX_P HELX_P16 AB7 THR E 48  ? THR E 59  ? THR E 48  THR E 59  1 ? 12 
HELX_P HELX_P17 AB8 SER F 18  ? ASN F 27  ? SER F 18  ASN F 27  1 ? 10 
HELX_P HELX_P18 AB9 THR F 158 ? ARG F 160 ? THR F 158 ARG F 160 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 
disulf1 disulf ?    ? B CYS 30 SG ? ? ? 1_555 B CYS 51  SG ? ? B CYS 30 B CYS 51  1_555 ? ? ? ? ? ? ? 2.070 ? ? 
disulf2 disulf ?    ? C CYS 33 SG ? ? ? 1_555 C CYS 167 SG ? ? C CYS 33 C CYS 167 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
disulf3 disulf ?    ? E CYS 30 SG ? ? ? 1_555 E CYS 51  SG ? ? E CYS 30 E CYS 51  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf4 disulf ?    ? F CYS 33 SG ? ? ? 1_555 F CYS 167 SG ? ? F CYS 33 F CYS 167 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
covale1 covale both ? A TRP 80 C  ? ? ? 1_555 A CSD 81  N  ? ? A TRP 79 A CSD 80  1_555 ? ? ? ? ? ? ? 1.343 ? ? 
covale2 covale both ? A CSD 81 C  ? ? ? 1_555 A ALA 82  N  ? ? A CSD 80 A ALA 81  1_555 ? ? ? ? ? ? ? 1.353 ? ? 
covale3 covale both ? D TRP 80 C  ? ? ? 1_555 D CSD 81  N  ? ? D TRP 79 D CSD 80  1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale4 covale both ? D CSD 81 C  ? ? ? 1_555 D ALA 82  N  ? ? D CSD 80 D ALA 81  1_555 ? ? ? ? ? ? ? 1.347 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CSD A 81 ? .   . .   . CSD A 80 ? 1_555 .   . .   . .     .  .  CYS 1 CSD Oxidation     'Named protein modification' 
2 CSD A 81 ? .   . .   . CSD A 80 ? 1_555 .   . .   . .     .  .  CYS 2 CSD Hydroxylation 'Named protein modification' 
3 CSD D 81 ? .   . .   . CSD D 80 ? 1_555 .   . .   . .     .  .  CYS 1 CSD Oxidation     'Named protein modification' 
4 CSD D 81 ? .   . .   . CSD D 80 ? 1_555 .   . .   . .     .  .  CYS 2 CSD Hydroxylation 'Named protein modification' 
5 CYS B 30 ? CYS B 51  ? CYS B 30 ? 1_555 CYS B 51  ? 1_555 SG SG .   . .   None          'Disulfide bridge'           
6 CYS C 33 ? CYS C 167 ? CYS C 33 ? 1_555 CYS C 167 ? 1_555 SG SG .   . .   None          'Disulfide bridge'           
7 CYS E 30 ? CYS E 51  ? CYS E 30 ? 1_555 CYS E 51  ? 1_555 SG SG .   . .   None          'Disulfide bridge'           
8 CYS F 33 ? CYS F 167 ? CYS F 33 ? 1_555 CYS F 167 ? 1_555 SG SG .   . .   None          'Disulfide bridge'           
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TRP 25  B . ? TRP 25  B PRO 26  B ? PRO 26  B 1 -2.23  
2 TYR 115 C . ? TYR 115 C PRO 116 C ? PRO 116 C 1 -22.56 
3 TRP 25  E . ? TRP 25  E PRO 26  E ? PRO 26  E 1 -5.31  
4 TYR 115 F . ? TYR 115 F PRO 116 F ? PRO 116 F 1 -22.49 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 16 ? 
AA2 ? 8  ? 
AA3 ? 7  ? 
AA4 ? 8  ? 
AA5 ? 7  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? anti-parallel 
AA1 12 13 ? anti-parallel 
AA1 13 14 ? anti-parallel 
AA1 14 15 ? anti-parallel 
AA1 15 16 ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA3 4  5  ? anti-parallel 
AA3 5  6  ? anti-parallel 
AA3 6  7  ? 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 
AA5 1  2  ? anti-parallel 
AA5 2  3  ? anti-parallel 
AA5 3  4  ? anti-parallel 
AA5 4  5  ? anti-parallel 
AA5 5  6  ? anti-parallel 
AA5 6  7  ? 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  LYS B 63  ? SER B 67  ? LYS B 63  SER B 67  
AA1 2  VAL B 2   ? GLU B 11  ? VAL B 2   GLU B 11  
AA1 3  GLN A 104 ? ILE A 113 ? GLN A 103 ILE A 112 
AA1 4  TRP A 80  ? LYS A 87  ? TRP A 79  LYS A 86  
AA1 5  ASP A 61  ? ALA A 69  ? ASP A 60  ALA A 68  
AA1 6  VAL A 44  ? SER A 55  ? VAL A 43  SER A 54  
AA1 7  VAL A 26  ? LYS A 37  ? VAL A 25  LYS A 36  
AA1 8  GLN A 4   ? GLU A 15  ? GLN A 3   GLU A 14  
AA1 9  GLN D 4   ? GLU D 15  ? GLN D 3   GLU D 14  
AA1 10 VAL D 26  ? LYS D 37  ? VAL D 25  LYS D 36  
AA1 11 VAL D 44  ? SER D 55  ? VAL D 43  SER D 54  
AA1 12 ASP D 61  ? TYR D 71  ? ASP D 60  TYR D 70  
AA1 13 LYS D 79  ? LYS D 87  ? LYS D 78  LYS D 86  
AA1 14 VAL D 105 ? GLY D 114 ? VAL D 104 GLY D 113 
AA1 15 VAL E 2   ? GLU E 11  ? VAL E 2   GLU E 11  
AA1 16 LYS E 63  ? SER E 67  ? LYS E 63  SER E 67  
AA2 1  THR C 47  ? PRO C 49  ? THR C 47  PRO C 49  
AA2 2  ASN C 39  ? TYR C 41  ? ASN C 39  TYR C 41  
AA2 3  THR C 30  ? SER C 36  ? THR C 30  SER C 36  
AA2 4  ALA C 150 ? PRO C 156 ? ALA C 150 PRO C 156 
AA2 5  TYR C 143 ? TYR C 146 ? TYR C 143 TYR C 146 
AA2 6  LEU C 132 ? TYR C 136 ? LEU C 132 TYR C 136 
AA2 7  ILE C 124 ? SER C 129 ? ILE C 124 SER C 129 
AA2 8  VAL C 113 ? TYR C 115 ? VAL C 113 TYR C 115 
AA3 1  LYS C 105 ? VAL C 107 ? LYS C 105 VAL C 107 
AA3 2  GLY C 99  ? ILE C 102 ? GLY C 99  ILE C 102 
AA3 3  VAL C 91  ? THR C 96  ? VAL C 91  THR C 96  
AA3 4  LEU C 82  ? ASN C 88  ? LEU C 82  ASN C 88  
AA3 5  PHE C 69  ? SER C 75  ? PHE C 69  SER C 75  
AA3 6  VAL C 57  ? LEU C 62  ? VAL C 57  LEU C 62  
AA3 7  ALA C 163 ? THR C 164 ? ALA C 163 THR C 164 
AA4 1  THR F 47  ? PRO F 49  ? THR F 47  PRO F 49  
AA4 2  ASN F 39  ? TYR F 41  ? ASN F 39  TYR F 41  
AA4 3  THR F 30  ? SER F 36  ? THR F 30  SER F 36  
AA4 4  ALA F 150 ? PRO F 156 ? ALA F 150 PRO F 156 
AA4 5  TYR F 143 ? TYR F 146 ? TYR F 143 TYR F 146 
AA4 6  LEU F 132 ? TYR F 136 ? LEU F 132 TYR F 136 
AA4 7  ILE F 124 ? SER F 129 ? ILE F 124 SER F 129 
AA4 8  VAL F 113 ? TYR F 115 ? VAL F 113 TYR F 115 
AA5 1  LYS F 105 ? VAL F 107 ? LYS F 105 VAL F 107 
AA5 2  GLY F 99  ? ILE F 102 ? GLY F 99  ILE F 102 
AA5 3  VAL F 91  ? THR F 96  ? VAL F 91  THR F 96  
AA5 4  LEU F 82  ? ASN F 88  ? LEU F 82  ASN F 88  
AA5 5  PHE F 69  ? SER F 75  ? PHE F 69  SER F 75  
AA5 6  VAL F 57  ? LEU F 62  ? VAL F 57  LEU F 62  
AA5 7  ALA F 163 ? THR F 164 ? ALA F 163 THR F 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  O LYS B 63  ? O LYS B 63  N GLU B 11  ? N GLU B 11  
AA1 2  3  O GLN B 8   ? O GLN B 8   N SER A 107 ? N SER A 106 
AA1 3  4  O LYS A 108 ? O LYS A 107 N THR A 85  ? N THR A 84  
AA1 4  5  O TRP A 80  ? O TRP A 79  N LEU A 68  ? N LEU A 67  
AA1 5  6  O ALA A 69  ? O ALA A 68  N ASP A 48  ? N ASP A 47  
AA1 6  7  O VAL A 49  ? O VAL A 48  N GLY A 32  ? N GLY A 31  
AA1 7  8  O ARG A 29  ? O ARG A 28  N THR A 12  ? N THR A 11  
AA1 8  9  N MET A 11  ? N MET A 10  O PHE D 7   ? O PHE D 6   
AA1 9  10 N THR D 12  ? N THR D 11  O ARG D 29  ? O ARG D 28  
AA1 10 11 N TRP D 34  ? N TRP D 33  O THR D 47  ? O THR D 46  
AA1 11 12 N LYS D 50  ? N LYS D 49  O GLN D 67  ? O GLN D 66  
AA1 12 13 N LEU D 68  ? N LEU D 67  O TRP D 80  ? O TRP D 79  
AA1 13 14 N THR D 85  ? N THR D 84  O LYS D 108 ? O LYS D 107 
AA1 14 15 N SER D 107 ? N SER D 106 O GLN E 8   ? O GLN E 8   
AA1 15 16 N GLU E 11  ? N GLU E 11  O LYS E 63  ? O LYS E 63  
AA2 1  2  O VAL C 48  ? O VAL C 48  N VAL C 40  ? N VAL C 40  
AA2 2  3  O TYR C 41  ? O TYR C 41  N ILE C 34  ? N ILE C 34  
AA2 3  4  N CYS C 33  ? N CYS C 33  O VAL C 153 ? O VAL C 153 
AA2 4  5  O GLU C 154 ? O GLU C 154 N TYR C 143 ? N TYR C 143 
AA2 5  6  O ALA C 144 ? O ALA C 144 N ALA C 135 ? N ALA C 135 
AA2 6  7  O MET C 134 ? O MET C 134 N TRP C 127 ? N TRP C 127 
AA2 7  8  O VAL C 126 ? O VAL C 126 N VAL C 113 ? N VAL C 113 
AA3 1  2  O LYS C 105 ? O LYS C 105 N ILE C 102 ? N ILE C 102 
AA3 2  3  O GLY C 99  ? O GLY C 99  N THR C 96  ? N THR C 96  
AA3 3  4  O LEU C 95  ? O LEU C 95  N VAL C 84  ? N VAL C 84  
AA3 4  5  O LYS C 85  ? O LYS C 85  N TYR C 72  ? N TYR C 72  
AA3 5  6  O ALA C 71  ? O ALA C 71  N ALA C 60  ? N ALA C 60  
AA3 6  7  N GLY C 61  ? N GLY C 61  O THR C 164 ? O THR C 164 
AA4 1  2  O VAL F 48  ? O VAL F 48  N VAL F 40  ? N VAL F 40  
AA4 2  3  O TYR F 41  ? O TYR F 41  N ILE F 34  ? N ILE F 34  
AA4 3  4  N CYS F 33  ? N CYS F 33  O VAL F 153 ? O VAL F 153 
AA4 4  5  O GLU F 154 ? O GLU F 154 N TYR F 143 ? N TYR F 143 
AA4 5  6  O ALA F 144 ? O ALA F 144 N ALA F 135 ? N ALA F 135 
AA4 6  7  O MET F 134 ? O MET F 134 N TRP F 127 ? N TRP F 127 
AA4 7  8  O ILE F 124 ? O ILE F 124 N TYR F 115 ? N TYR F 115 
AA5 1  2  O LYS F 105 ? O LYS F 105 N ILE F 102 ? N ILE F 102 
AA5 2  3  O SER F 101 ? O SER F 101 N GLU F 94  ? N GLU F 94  
AA5 3  4  O LEU F 95  ? O LEU F 95  N VAL F 84  ? N VAL F 84  
AA5 4  5  O LYS F 85  ? O LYS F 85  N TYR F 72  ? N TYR F 72  
AA5 5  6  O ALA F 71  ? O ALA F 71  N ALA F 60  ? N ALA F 60  
AA5 6  7  N GLY F 61  ? N GLY F 61  O THR F 164 ? O THR F 164 
# 
_pdbx_entry_details.entry_id                   9KUE 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE C ARG 97  ? ? CZ C ARG 97  ? ? NH2 C ARG 97  ? ? 123.52 120.30 3.22  0.50 N 
2 1 CG F MET 134 ? ? SD F MET 134 ? ? CE  F MET 134 ? ? 113.42 100.20 13.22 1.60 N 
3 1 CD F ARG 160 ? ? NE F ARG 160 ? ? CZ  F ARG 160 ? ? 133.16 123.60 9.56  1.40 N 
4 1 NE F ARG 160 ? ? CZ F ARG 160 ? ? NH1 F ARG 160 ? ? 123.84 120.30 3.54  0.50 N 
5 1 NE F ARG 162 ? ? CZ F ARG 162 ? ? NH2 F ARG 162 ? ? 124.39 120.30 4.09  0.50 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 LEU A 22  ? ? -111.61 52.58 
2 1 ASN C 45  ? ? 72.06   41.26 
3 1 ASN C 171 ? ? 92.86   46.64 
4 1 LEU D 22  ? ? -113.38 53.31 
5 1 SER D 39  ? ? -69.70  98.62 
6 1 ASN F 45  ? ? 80.84   32.29 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 SER B 1   ? ? VAL B 2   ? ? 149.46  
2 1 VAL B 2   ? ? THR B 3   ? ? -144.28 
3 1 LEU C 170 ? ? ASN C 171 ? ? 144.68  
4 1 GLU D 41  ? ? SER D 42  ? ? 136.99  
5 1 GLY F 53  ? ? SER F 54  ? ? 140.09  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 28  ? ? 0.183 'SIDE CHAIN' 
2 1 ARG B 62  ? ? 0.075 'SIDE CHAIN' 
3 1 ARG C 138 ? ? 0.100 'SIDE CHAIN' 
4 1 ARG D 28  ? ? 0.105 'SIDE CHAIN' 
5 1 ARG D 44  ? ? 0.126 'SIDE CHAIN' 
6 1 ARG F 74  ? ? 0.115 'SIDE CHAIN' 
7 1 ARG F 97  ? ? 0.078 'SIDE CHAIN' 
8 1 ARG F 160 ? ? 0.075 'SIDE CHAIN' 
9 1 ARG F 162 ? ? 0.102 'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 14.3034 -52.7548 8.0033  0.1363 ? 0.0021  ? 0.0246  ? 0.2010 ? 0.0172  ? 0.1678 ? 1.4172 ? -0.2466 
? 0.5217  ? 1.1189 ? -0.4842 ? 2.6754 ? 0.0080  ? 0.2202  ? 0.2803  ? -0.3386 ? -0.0812 ? -0.0682 ? -0.1342 ? 0.2263  ? 0.0732  ? 
2 'X-RAY DIFFRACTION' ? refined 22.4525 -59.4788 33.2724 0.0561 ? 0.0069  ? -0.0151 ? 0.3051 ? -0.0073 ? 0.1692 ? 1.7971 ? 1.4856  
? -1.2316 ? 4.2726 ? -1.7396 ? 2.9150 ? 0.1666  ? -0.2310 ? 0.0669  ? 0.4839  ? -0.0783 ? -0.1409 ? -0.1528 ? 0.4706  ? -0.0883 ? 
3 'X-RAY DIFFRACTION' ? refined 8.0181  -75.9165 25.0925 0.1560 ? 0.0174  ? 0.0301  ? 0.0850 ? 0.0072  ? 0.0955 ? 1.5998 ? 0.6348  
? -0.4732 ? 2.1710 ? -0.7407 ? 1.6718 ? -0.1117 ? -0.0243 ? -0.1187 ? -0.1179 ? 0.0050  ? 0.0177  ? 0.4990  ? 0.0261  ? 0.1067  ? 
4 'X-RAY DIFFRACTION' ? refined -3.2331 -51.6712 13.8695 0.0274 ? 0.0088  ? -0.0119 ? 0.1965 ? 0.0062  ? 0.1749 ? 0.6188 ? 0.1819  
? 0.2642  ? 1.4632 ? 0.5795  ? 3.1666 ? -0.0002 ? 0.1118  ? -0.0390 ? -0.1807 ? -0.0682 ? 0.1910  ? 0.0280  ? -0.2479 ? 0.0684  ? 
5 'X-RAY DIFFRACTION' ? refined 4.8209  -38.3264 36.0187 0.1728 ? -0.0009 ? 0.0133  ? 0.1325 ? -0.0046 ? 0.1451 ? 2.4760 ? 1.7214  
? 1.5468  ? 3.8389 ? 1.6937  ? 3.2457 ? 0.0511  ? -0.1546 ? 0.1834  ? 0.2796  ? -0.0971 ? -0.0667 ? -0.4623 ? -0.0200 ? 0.0460  ? 
6 'X-RAY DIFFRACTION' ? refined 9.7042  -25.7899 16.9235 0.5271 ? -0.1382 ? -0.0199 ? 0.1710 ? 0.0837  ? 0.2827 ? 1.9564 ? 0.4378  
? -0.1368 ? 2.7003 ? -0.5798 ? 2.6931 ? -0.0267 ? 0.1817  ? 0.4980  ? -0.0928 ? -0.1516 ? -0.2091 ? -1.1034 ? 0.4289  ? 0.1783  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 1 ? ? ? A 201 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 1 ? ? ? B 67  ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? C 4 ? ? ? C 203 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? D 1 ? ? ? D 202 ? ? ? 
5 'X-RAY DIFFRACTION' 5 ? ? E 1 ? ? ? E 67  ? ? ? 
6 'X-RAY DIFFRACTION' 6 ? ? F 4 ? ? ? F 202 ? ? ? 
# 
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 GLN 0   ? A GLN 1   
2  1 Y 1 A TYR 70  ? A TYR 71  
3  1 Y 1 A ALA 71  ? A ALA 72  
4  1 Y 1 A HIS 72  ? A HIS 73  
5  1 Y 1 A ASN 73  ? A ASN 74  
6  1 Y 1 A LYS 74  ? A LYS 75  
7  1 Y 1 A PRO 75  ? A PRO 76  
8  1 Y 1 A ASN 76  ? A ASN 77  
9  1 Y 1 C GLY 1   ? C GLY 1   
10 1 Y 1 C ALA 2   ? C ALA 2   
11 1 Y 1 C SER 3   ? C SER 3   
12 1 Y 1 D GLN 0   ? D GLN 1   
13 1 Y 1 D ALA 71  ? D ALA 72  
14 1 Y 1 D HIS 72  ? D HIS 73  
15 1 Y 1 D ASN 73  ? D ASN 74  
16 1 Y 1 D LYS 74  ? D LYS 75  
17 1 Y 1 D PRO 75  ? D PRO 76  
18 1 Y 1 D ASN 76  ? D ASN 77  
19 1 Y 1 F GLY 1   ? F GLY 1   
20 1 Y 1 F ALA 2   ? F ALA 2   
21 1 Y 1 F SER 3   ? F SER 3   
22 1 Y 1 F GLY 172 ? F GLY 172 
# 
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 
A1L6M C1     C N N 1   
A1L6M C2     C N N 2   
A1L6M C3     C N N 3   
A1L6M C4     C N N 4   
A1L6M C5     C N N 5   
A1L6M C6     C N N 6   
A1L6M O1     O N N 7   
A1L6M N1     N N N 8   
A1L6M C7     C N N 9   
A1L6M C8     C N N 10  
A1L6M C9     C Y N 11  
A1L6M C10    C Y N 12  
A1L6M C11    C N N 13  
A1L6M C12    C Y N 14  
A1L6M C13    C N N 15  
A1L6M C14    C N N 16  
A1L6M C15    C N N 17  
A1L6M O2     O N N 18  
A1L6M O3     O N N 19  
A1L6M C16    C Y N 20  
A1L6M N2     N Y N 21  
A1L6M C17    C N N 22  
A1L6M C18    C N N 23  
A1L6M N3     N N N 24  
A1L6M C19    C N N 25  
A1L6M C20    C N N 26  
A1L6M C21    C N N 27  
A1L6M N4     N N N 28  
A1L6M C22    C N N 29  
A1L6M O4     O N N 30  
A1L6M C23    C N N 31  
A1L6M C24    C N S 32  
A1L6M O5     O N N 33  
A1L6M C25    C N N 34  
A1L6M C26    C N N 35  
A1L6M C27    C N N 36  
A1L6M C28    C N N 37  
A1L6M C29    C N N 38  
A1L6M C30    C N N 39  
A1L6M C31    C N N 40  
A1L6M C32    C N N 41  
A1L6M C33    C N N 42  
A1L6M C34    C N N 43  
A1L6M C35    C N N 44  
A1L6M C36    C N N 45  
A1L6M C37    C N N 46  
A1L6M C38    C N N 47  
A1L6M C39    C N N 48  
A1L6M C40    C N N 49  
A1L6M C41    C N N 50  
A1L6M C42    C N N 51  
A1L6M C43    C N N 52  
A1L6M C44    C N N 53  
A1L6M O6     O N N 54  
A1L6M C45    C N N 55  
A1L6M C46    C N N 56  
A1L6M C47    C N N 57  
A1L6M C48    C N N 58  
A1L6M O7     O N N 59  
A1L6M O8     O N N 60  
A1L6M H1     H N N 61  
A1L6M H2     H N N 62  
A1L6M H3     H N N 63  
A1L6M H4     H N N 64  
A1L6M H5     H N N 65  
A1L6M H6     H N N 66  
A1L6M H7     H N N 67  
A1L6M H8     H N N 68  
A1L6M H9     H N N 69  
A1L6M H11    H N N 70  
A1L6M H12    H N N 71  
A1L6M H13    H N N 72  
A1L6M H14    H N N 73  
A1L6M H15    H N N 74  
A1L6M H16    H N N 75  
A1L6M H17    H N N 76  
A1L6M H18    H N N 77  
A1L6M H19    H N N 78  
A1L6M H20    H N N 79  
A1L6M H23    H N N 80  
A1L6M H25    H N N 81  
A1L6M H26    H N N 82  
A1L6M H27    H N N 83  
A1L6M H28    H N N 84  
A1L6M H29    H N N 85  
A1L6M H30    H N N 86  
A1L6M H31    H N N 87  
A1L6M H32    H N N 88  
A1L6M H33    H N N 89  
A1L6M H34    H N N 90  
A1L6M H35    H N N 91  
A1L6M H36    H N N 92  
A1L6M H37    H N N 93  
A1L6M H38    H N N 94  
A1L6M H39    H N N 95  
A1L6M H40    H N N 96  
A1L6M H41    H N N 97  
A1L6M H42    H N N 98  
A1L6M H43    H N N 99  
A1L6M H44    H N N 100 
A1L6M H45    H N N 101 
A1L6M H46    H N N 102 
A1L6M H47    H N N 103 
A1L6M H48    H N N 104 
A1L6M H49    H N N 105 
A1L6M H50    H N N 106 
A1L6M H51    H N N 107 
A1L6M H52    H N N 108 
A1L6M H53    H N N 109 
A1L6M H54    H N N 110 
A1L6M H55    H N N 111 
A1L6M H56    H N N 112 
A1L6M H57    H N N 113 
A1L6M H58    H N N 114 
A1L6M H59    H N N 115 
A1L6M H60    H N N 116 
A1L6M H61    H N N 117 
A1L6M H62    H N N 118 
A1L6M H63    H N N 119 
A1L6M H65    H N N 120 
A1L6M H10    H N N 121 
A1L6M H21    H N N 122 
ALA   N      N N N 123 
ALA   CA     C N S 124 
ALA   C      C N N 125 
ALA   O      O N N 126 
ALA   CB     C N N 127 
ALA   OXT    O N N 128 
ALA   H      H N N 129 
ALA   H2     H N N 130 
ALA   HA     H N N 131 
ALA   HB1    H N N 132 
ALA   HB2    H N N 133 
ALA   HB3    H N N 134 
ALA   HXT    H N N 135 
ARG   N      N N N 136 
ARG   CA     C N S 137 
ARG   C      C N N 138 
ARG   O      O N N 139 
ARG   CB     C N N 140 
ARG   CG     C N N 141 
ARG   CD     C N N 142 
ARG   NE     N N N 143 
ARG   CZ     C N N 144 
ARG   NH1    N N N 145 
ARG   NH2    N N N 146 
ARG   OXT    O N N 147 
ARG   H      H N N 148 
ARG   H2     H N N 149 
ARG   HA     H N N 150 
ARG   HB2    H N N 151 
ARG   HB3    H N N 152 
ARG   HG2    H N N 153 
ARG   HG3    H N N 154 
ARG   HD2    H N N 155 
ARG   HD3    H N N 156 
ARG   HE     H N N 157 
ARG   HH11   H N N 158 
ARG   HH12   H N N 159 
ARG   HH21   H N N 160 
ARG   HH22   H N N 161 
ARG   HXT    H N N 162 
ASN   N      N N N 163 
ASN   CA     C N S 164 
ASN   C      C N N 165 
ASN   O      O N N 166 
ASN   CB     C N N 167 
ASN   CG     C N N 168 
ASN   OD1    O N N 169 
ASN   ND2    N N N 170 
ASN   OXT    O N N 171 
ASN   H      H N N 172 
ASN   H2     H N N 173 
ASN   HA     H N N 174 
ASN   HB2    H N N 175 
ASN   HB3    H N N 176 
ASN   HD21   H N N 177 
ASN   HD22   H N N 178 
ASN   HXT    H N N 179 
ASP   N      N N N 180 
ASP   CA     C N S 181 
ASP   C      C N N 182 
ASP   O      O N N 183 
ASP   CB     C N N 184 
ASP   CG     C N N 185 
ASP   OD1    O N N 186 
ASP   OD2    O N N 187 
ASP   OXT    O N N 188 
ASP   H      H N N 189 
ASP   H2     H N N 190 
ASP   HA     H N N 191 
ASP   HB2    H N N 192 
ASP   HB3    H N N 193 
ASP   HD2    H N N 194 
ASP   HXT    H N N 195 
AZI   N1     N N N 196 
AZI   N2     N N N 197 
AZI   N3     N N N 198 
CSD   N      N N N 199 
CSD   CA     C N R 200 
CSD   CB     C N N 201 
CSD   SG     S N N 202 
CSD   C      C N N 203 
CSD   O      O N N 204 
CSD   OXT    O N N 205 
CSD   OD1    O N N 206 
CSD   OD2    O N N 207 
CSD   H      H N N 208 
CSD   H2     H N N 209 
CSD   HA     H N N 210 
CSD   HB2    H N N 211 
CSD   HB3    H N N 212 
CSD   HXT    H N N 213 
CSD   HD2    H N N 214 
CYS   N      N N N 215 
CYS   CA     C N R 216 
CYS   C      C N N 217 
CYS   O      O N N 218 
CYS   CB     C N N 219 
CYS   SG     S N N 220 
CYS   OXT    O N N 221 
CYS   H      H N N 222 
CYS   H2     H N N 223 
CYS   HA     H N N 224 
CYS   HB2    H N N 225 
CYS   HB3    H N N 226 
CYS   HG     H N N 227 
CYS   HXT    H N N 228 
GLN   N      N N N 229 
GLN   CA     C N S 230 
GLN   C      C N N 231 
GLN   O      O N N 232 
GLN   CB     C N N 233 
GLN   CG     C N N 234 
GLN   CD     C N N 235 
GLN   OE1    O N N 236 
GLN   NE2    N N N 237 
GLN   OXT    O N N 238 
GLN   H      H N N 239 
GLN   H2     H N N 240 
GLN   HA     H N N 241 
GLN   HB2    H N N 242 
GLN   HB3    H N N 243 
GLN   HG2    H N N 244 
GLN   HG3    H N N 245 
GLN   HE21   H N N 246 
GLN   HE22   H N N 247 
GLN   HXT    H N N 248 
GLU   N      N N N 249 
GLU   CA     C N S 250 
GLU   C      C N N 251 
GLU   O      O N N 252 
GLU   CB     C N N 253 
GLU   CG     C N N 254 
GLU   CD     C N N 255 
GLU   OE1    O N N 256 
GLU   OE2    O N N 257 
GLU   OXT    O N N 258 
GLU   H      H N N 259 
GLU   H2     H N N 260 
GLU   HA     H N N 261 
GLU   HB2    H N N 262 
GLU   HB3    H N N 263 
GLU   HG2    H N N 264 
GLU   HG3    H N N 265 
GLU   HE2    H N N 266 
GLU   HXT    H N N 267 
GLY   N      N N N 268 
GLY   CA     C N N 269 
GLY   C      C N N 270 
GLY   O      O N N 271 
GLY   OXT    O N N 272 
GLY   H      H N N 273 
GLY   H2     H N N 274 
GLY   HA2    H N N 275 
GLY   HA3    H N N 276 
GLY   HXT    H N N 277 
HIS   N      N N N 278 
HIS   CA     C N S 279 
HIS   C      C N N 280 
HIS   O      O N N 281 
HIS   CB     C N N 282 
HIS   CG     C Y N 283 
HIS   ND1    N Y N 284 
HIS   CD2    C Y N 285 
HIS   CE1    C Y N 286 
HIS   NE2    N Y N 287 
HIS   OXT    O N N 288 
HIS   H      H N N 289 
HIS   H2     H N N 290 
HIS   HA     H N N 291 
HIS   HB2    H N N 292 
HIS   HB3    H N N 293 
HIS   HD1    H N N 294 
HIS   HD2    H N N 295 
HIS   HE1    H N N 296 
HIS   HE2    H N N 297 
HIS   HXT    H N N 298 
HOH   O      O N N 299 
HOH   H1     H N N 300 
HOH   H2     H N N 301 
ILE   N      N N N 302 
ILE   CA     C N S 303 
ILE   C      C N N 304 
ILE   O      O N N 305 
ILE   CB     C N S 306 
ILE   CG1    C N N 307 
ILE   CG2    C N N 308 
ILE   CD1    C N N 309 
ILE   OXT    O N N 310 
ILE   H      H N N 311 
ILE   H2     H N N 312 
ILE   HA     H N N 313 
ILE   HB     H N N 314 
ILE   HG12   H N N 315 
ILE   HG13   H N N 316 
ILE   HG21   H N N 317 
ILE   HG22   H N N 318 
ILE   HG23   H N N 319 
ILE   HD11   H N N 320 
ILE   HD12   H N N 321 
ILE   HD13   H N N 322 
ILE   HXT    H N N 323 
LEU   N      N N N 324 
LEU   CA     C N S 325 
LEU   C      C N N 326 
LEU   O      O N N 327 
LEU   CB     C N N 328 
LEU   CG     C N N 329 
LEU   CD1    C N N 330 
LEU   CD2    C N N 331 
LEU   OXT    O N N 332 
LEU   H      H N N 333 
LEU   H2     H N N 334 
LEU   HA     H N N 335 
LEU   HB2    H N N 336 
LEU   HB3    H N N 337 
LEU   HG     H N N 338 
LEU   HD11   H N N 339 
LEU   HD12   H N N 340 
LEU   HD13   H N N 341 
LEU   HD21   H N N 342 
LEU   HD22   H N N 343 
LEU   HD23   H N N 344 
LEU   HXT    H N N 345 
LUT   C1     C N N 346 
LUT   C2     C N N 347 
LUT   C3     C N S 348 
LUT   C4     C N N 349 
LUT   C5     C N N 350 
LUT   C6     C N N 351 
LUT   C7     C N N 352 
LUT   C8     C N N 353 
LUT   C9     C N N 354 
LUT   C10    C N N 355 
LUT   C11    C N N 356 
LUT   C12    C N N 357 
LUT   C13    C N N 358 
LUT   C14    C N N 359 
LUT   C15    C N N 360 
LUT   C16    C N N 361 
LUT   C17    C N N 362 
LUT   C18    C N N 363 
LUT   C19    C N N 364 
LUT   C20    C N N 365 
LUT   O3     O N N 366 
LUT   C21    C N N 367 
LUT   C22    C N N 368 
LUT   C23    C N R 369 
LUT   C24    C N N 370 
LUT   C25    C N N 371 
LUT   C26    C N S 372 
LUT   C27    C N N 373 
LUT   C28    C N N 374 
LUT   C29    C N N 375 
LUT   C30    C N N 376 
LUT   C31    C N N 377 
LUT   C32    C N N 378 
LUT   C33    C N N 379 
LUT   C34    C N N 380 
LUT   C35    C N N 381 
LUT   C36    C N N 382 
LUT   C37    C N N 383 
LUT   C38    C N N 384 
LUT   C39    C N N 385 
LUT   C40    C N N 386 
LUT   O23    O N N 387 
LUT   H21    H N N 388 
LUT   H22    H N N 389 
LUT   H3     H N N 390 
LUT   H41    H N N 391 
LUT   H42    H N N 392 
LUT   H7     H N N 393 
LUT   H8     H N N 394 
LUT   H10    H N N 395 
LUT   H11    H N N 396 
LUT   H12    H N N 397 
LUT   H14    H N N 398 
LUT   H15    H N N 399 
LUT   H161   H N N 400 
LUT   H162   H N N 401 
LUT   H163   H N N 402 
LUT   H171   H N N 403 
LUT   H172   H N N 404 
LUT   H173   H N N 405 
LUT   H181   H N N 406 
LUT   H182   H N N 407 
LUT   H183   H N N 408 
LUT   H191   H N N 409 
LUT   H192   H N N 410 
LUT   H193   H N N 411 
LUT   H201   H N N 412 
LUT   H202   H N N 413 
LUT   H203   H N N 414 
LUT   HO3    H N N 415 
LUT   H221   H N N 416 
LUT   H222   H N N 417 
LUT   H23    H N N 418 
LUT   H24    H N N 419 
LUT   H26    H N N 420 
LUT   H27    H N N 421 
LUT   H28    H N N 422 
LUT   H30    H N N 423 
LUT   H31    H N N 424 
LUT   H32    H N N 425 
LUT   H34    H N N 426 
LUT   H35    H N N 427 
LUT   H361   H N N 428 
LUT   H362   H N N 429 
LUT   H363   H N N 430 
LUT   H371   H N N 431 
LUT   H372   H N N 432 
LUT   H373   H N N 433 
LUT   H381   H N N 434 
LUT   H382   H N N 435 
LUT   H383   H N N 436 
LUT   H391   H N N 437 
LUT   H392   H N N 438 
LUT   H393   H N N 439 
LUT   H401   H N N 440 
LUT   H402   H N N 441 
LUT   H403   H N N 442 
LUT   H1     H N N 443 
LYS   N      N N N 444 
LYS   CA     C N S 445 
LYS   C      C N N 446 
LYS   O      O N N 447 
LYS   CB     C N N 448 
LYS   CG     C N N 449 
LYS   CD     C N N 450 
LYS   CE     C N N 451 
LYS   NZ     N N N 452 
LYS   OXT    O N N 453 
LYS   H      H N N 454 
LYS   H2     H N N 455 
LYS   HA     H N N 456 
LYS   HB2    H N N 457 
LYS   HB3    H N N 458 
LYS   HG2    H N N 459 
LYS   HG3    H N N 460 
LYS   HD2    H N N 461 
LYS   HD3    H N N 462 
LYS   HE2    H N N 463 
LYS   HE3    H N N 464 
LYS   HZ1    H N N 465 
LYS   HZ2    H N N 466 
LYS   HZ3    H N N 467 
LYS   HXT    H N N 468 
MET   N      N N N 469 
MET   CA     C N S 470 
MET   C      C N N 471 
MET   O      O N N 472 
MET   CB     C N N 473 
MET   CG     C N N 474 
MET   SD     S N N 475 
MET   CE     C N N 476 
MET   OXT    O N N 477 
MET   H      H N N 478 
MET   H2     H N N 479 
MET   HA     H N N 480 
MET   HB2    H N N 481 
MET   HB3    H N N 482 
MET   HG2    H N N 483 
MET   HG3    H N N 484 
MET   HE1    H N N 485 
MET   HE2    H N N 486 
MET   HE3    H N N 487 
MET   HXT    H N N 488 
PHE   N      N N N 489 
PHE   CA     C N S 490 
PHE   C      C N N 491 
PHE   O      O N N 492 
PHE   CB     C N N 493 
PHE   CG     C Y N 494 
PHE   CD1    C Y N 495 
PHE   CD2    C Y N 496 
PHE   CE1    C Y N 497 
PHE   CE2    C Y N 498 
PHE   CZ     C Y N 499 
PHE   OXT    O N N 500 
PHE   H      H N N 501 
PHE   H2     H N N 502 
PHE   HA     H N N 503 
PHE   HB2    H N N 504 
PHE   HB3    H N N 505 
PHE   HD1    H N N 506 
PHE   HD2    H N N 507 
PHE   HE1    H N N 508 
PHE   HE2    H N N 509 
PHE   HZ     H N N 510 
PHE   HXT    H N N 511 
PLC   C1     C N N 512 
PLC   C2     C N R 513 
PLC   C3     C N N 514 
PLC   C4     C N N 515 
PLC   C5     C N N 516 
PLC   C6     C N N 517 
PLC   C7     C N N 518 
PLC   C8     C N N 519 
PLC   "C'"   C N N 520 
PLC   "C1'"  C N N 521 
PLC   "C2'"  C N N 522 
PLC   "C3'"  C N N 523 
PLC   "C4'"  C N N 524 
PLC   "C5'"  C N N 525 
PLC   "C6'"  C N N 526 
PLC   "C7'"  C N N 527 
PLC   "C8'"  C N N 528 
PLC   "C9'"  C N N 529 
PLC   "CA'"  C N N 530 
PLC   "CB'"  C N N 531 
PLC   CB     C N N 532 
PLC   C1B    C N N 533 
PLC   C2B    C N N 534 
PLC   C3B    C N N 535 
PLC   C4B    C N N 536 
PLC   C5B    C N N 537 
PLC   C6B    C N N 538 
PLC   C7B    C N N 539 
PLC   C8B    C N N 540 
PLC   C9B    C N N 541 
PLC   CAA    C N N 542 
PLC   CBA    C N N 543 
PLC   "O'"   O N N 544 
PLC   OB     O N N 545 
PLC   O2     O N N 546 
PLC   O3     O N N 547 
PLC   O1P    O N N 548 
PLC   O2P    O N N 549 
PLC   O3P    O N N 550 
PLC   O4P    O N N 551 
PLC   N      N N N 552 
PLC   P      P N R 553 
PLC   H11    H N N 554 
PLC   H12    H N N 555 
PLC   H2     H N N 556 
PLC   H31    H N N 557 
PLC   H32    H N N 558 
PLC   H41    H N N 559 
PLC   H42    H N N 560 
PLC   H51    H N N 561 
PLC   H52    H N N 562 
PLC   H61    H N N 563 
PLC   H62    H N N 564 
PLC   H63    H N N 565 
PLC   H71    H N N 566 
PLC   H72    H N N 567 
PLC   H73    H N N 568 
PLC   H81    H N N 569 
PLC   H82    H N N 570 
PLC   H83    H N N 571 
PLC   "H1'1" H N N 572 
PLC   "H1'2" H N N 573 
PLC   "H2'1" H N N 574 
PLC   "H2'2" H N N 575 
PLC   "H3'1" H N N 576 
PLC   "H3'2" H N N 577 
PLC   "H4'1" H N N 578 
PLC   "H4'2" H N N 579 
PLC   "H5'1" H N N 580 
PLC   "H5'2" H N N 581 
PLC   "H6'1" H N N 582 
PLC   "H6'2" H N N 583 
PLC   "H7'1" H N N 584 
PLC   "H7'2" H N N 585 
PLC   "H8'1" H N N 586 
PLC   "H8'2" H N N 587 
PLC   "H9'1" H N N 588 
PLC   "H9'2" H N N 589 
PLC   "HT'1" H N N 590 
PLC   "HT'2" H N N 591 
PLC   "HE'1" H N N 592 
PLC   "HE'2" H N N 593 
PLC   "HE'3" H N N 594 
PLC   H1A1   H N N 595 
PLC   H1A2   H N N 596 
PLC   H2A1   H N N 597 
PLC   H2A2   H N N 598 
PLC   H3A1   H N N 599 
PLC   H3A2   H N N 600 
PLC   H4A1   H N N 601 
PLC   H4A2   H N N 602 
PLC   H5A1   H N N 603 
PLC   H5A2   H N N 604 
PLC   H6A1   H N N 605 
PLC   H6A2   H N N 606 
PLC   H7A1   H N N 607 
PLC   H7A2   H N N 608 
PLC   H8A1   H N N 609 
PLC   H8A2   H N N 610 
PLC   H9A1   H N N 611 
PLC   H9A2   H N N 612 
PLC   HTA1   H N N 613 
PLC   HTA2   H N N 614 
PLC   HEA1   H N N 615 
PLC   HEA2   H N N 616 
PLC   HEA3   H N N 617 
PLC   HOP2   H N N 618 
PRO   N      N N N 619 
PRO   CA     C N S 620 
PRO   C      C N N 621 
PRO   O      O N N 622 
PRO   CB     C N N 623 
PRO   CG     C N N 624 
PRO   CD     C N N 625 
PRO   OXT    O N N 626 
PRO   H      H N N 627 
PRO   HA     H N N 628 
PRO   HB2    H N N 629 
PRO   HB3    H N N 630 
PRO   HG2    H N N 631 
PRO   HG3    H N N 632 
PRO   HD2    H N N 633 
PRO   HD3    H N N 634 
PRO   HXT    H N N 635 
SER   N      N N N 636 
SER   CA     C N S 637 
SER   C      C N N 638 
SER   O      O N N 639 
SER   CB     C N N 640 
SER   OG     O N N 641 
SER   OXT    O N N 642 
SER   H      H N N 643 
SER   H2     H N N 644 
SER   HA     H N N 645 
SER   HB2    H N N 646 
SER   HB3    H N N 647 
SER   HG     H N N 648 
SER   HXT    H N N 649 
THR   N      N N N 650 
THR   CA     C N S 651 
THR   C      C N N 652 
THR   O      O N N 653 
THR   CB     C N R 654 
THR   OG1    O N N 655 
THR   CG2    C N N 656 
THR   OXT    O N N 657 
THR   H      H N N 658 
THR   H2     H N N 659 
THR   HA     H N N 660 
THR   HB     H N N 661 
THR   HG1    H N N 662 
THR   HG21   H N N 663 
THR   HG22   H N N 664 
THR   HG23   H N N 665 
THR   HXT    H N N 666 
TRP   N      N N N 667 
TRP   CA     C N S 668 
TRP   C      C N N 669 
TRP   O      O N N 670 
TRP   CB     C N N 671 
TRP   CG     C Y N 672 
TRP   CD1    C Y N 673 
TRP   CD2    C Y N 674 
TRP   NE1    N Y N 675 
TRP   CE2    C Y N 676 
TRP   CE3    C Y N 677 
TRP   CZ2    C Y N 678 
TRP   CZ3    C Y N 679 
TRP   CH2    C Y N 680 
TRP   OXT    O N N 681 
TRP   H      H N N 682 
TRP   H2     H N N 683 
TRP   HA     H N N 684 
TRP   HB2    H N N 685 
TRP   HB3    H N N 686 
TRP   HD1    H N N 687 
TRP   HE1    H N N 688 
TRP   HE3    H N N 689 
TRP   HZ2    H N N 690 
TRP   HZ3    H N N 691 
TRP   HH2    H N N 692 
TRP   HXT    H N N 693 
TYR   N      N N N 694 
TYR   CA     C N S 695 
TYR   C      C N N 696 
TYR   O      O N N 697 
TYR   CB     C N N 698 
TYR   CG     C Y N 699 
TYR   CD1    C Y N 700 
TYR   CD2    C Y N 701 
TYR   CE1    C Y N 702 
TYR   CE2    C Y N 703 
TYR   CZ     C Y N 704 
TYR   OH     O N N 705 
TYR   OXT    O N N 706 
TYR   H      H N N 707 
TYR   H2     H N N 708 
TYR   HA     H N N 709 
TYR   HB2    H N N 710 
TYR   HB3    H N N 711 
TYR   HD1    H N N 712 
TYR   HD2    H N N 713 
TYR   HE1    H N N 714 
TYR   HE2    H N N 715 
TYR   HH     H N N 716 
TYR   HXT    H N N 717 
VAL   N      N N N 718 
VAL   CA     C N S 719 
VAL   C      C N N 720 
VAL   O      O N N 721 
VAL   CB     C N N 722 
VAL   CG1    C N N 723 
VAL   CG2    C N N 724 
VAL   OXT    O N N 725 
VAL   H      H N N 726 
VAL   H2     H N N 727 
VAL   HA     H N N 728 
VAL   HB     H N N 729 
VAL   HG11   H N N 730 
VAL   HG12   H N N 731 
VAL   HG13   H N N 732 
VAL   HG21   H N N 733 
VAL   HG22   H N N 734 
VAL   HG23   H N N 735 
VAL   HXT    H N N 736 
# 
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 
A1L6M C34   C33    sing N N 1   
A1L6M C36   C35    sing N N 2   
A1L6M C36   C37    sing N N 3   
A1L6M C33   C35    sing N N 4   
A1L6M C33   C32    doub N Z 5   
A1L6M C39   C38    sing N N 6   
A1L6M C37   C38    doub N N 7   
A1L6M C38   C40    sing N N 8   
A1L6M C32   C31    sing N N 9   
A1L6M C31   C30    sing N N 10  
A1L6M C30   C28    sing N N 11  
A1L6M C28   C27    doub N E 12  
A1L6M C28   C29    sing N N 13  
A1L6M C27   C26    sing N N 14  
A1L6M O4    C22    doub N N 15  
A1L6M O6    C44    sing N N 16  
A1L6M C26   C25    sing N N 17  
A1L6M C22   N4     sing N N 18  
A1L6M C22   C23    sing N N 19  
A1L6M O7    C48    sing N N 20  
A1L6M C24   C25    sing N N 21  
A1L6M C24   C23    sing N N 22  
A1L6M C24   O5     sing N N 23  
A1L6M C44   C43    sing N N 24  
A1L6M N4    C21    sing N N 25  
A1L6M C23   C41    doub N N 26  
A1L6M C48   O8     doub N N 27  
A1L6M C48   C47    sing N N 28  
A1L6M C46   C47    sing N N 29  
A1L6M C46   C45    sing N N 30  
A1L6M C43   C45    doub N N 31  
A1L6M C43   C19    sing N N 32  
A1L6M C21   C41    sing N N 33  
A1L6M C21   C20    doub N Z 34  
A1L6M C41   C42    sing N N 35  
A1L6M C45   C18    sing N N 36  
A1L6M C20   C19    sing N N 37  
A1L6M C19   N3     doub N N 38  
A1L6M C18   N3     sing N N 39  
A1L6M C18   C17    doub N Z 40  
A1L6M O3    C15    doub N N 41  
A1L6M C17   C16    sing N N 42  
A1L6M C15   O2     sing N N 43  
A1L6M C15   C14    sing N N 44  
A1L6M C14   C13    sing N N 45  
A1L6M C13   C12    sing N N 46  
A1L6M C16   C12    doub Y N 47  
A1L6M C16   N2     sing Y N 48  
A1L6M C12   C10    sing Y N 49  
A1L6M N2    C9     sing Y N 50  
A1L6M C10   C9     doub Y N 51  
A1L6M C10   C11    sing N N 52  
A1L6M C9    C8     sing N N 53  
A1L6M C8    C7     doub N Z 54  
A1L6M C7    N1     sing N N 55  
A1L6M C7    C3     sing N N 56  
A1L6M N1    C6     sing N N 57  
A1L6M C3    C2     sing N N 58  
A1L6M C3    C4     doub N N 59  
A1L6M C2    C1     sing N N 60  
A1L6M C6    O1     doub N N 61  
A1L6M C6    C4     sing N N 62  
A1L6M C4    C5     sing N N 63  
A1L6M C1    H1     sing N N 64  
A1L6M C1    H2     sing N N 65  
A1L6M C1    H3     sing N N 66  
A1L6M C2    H4     sing N N 67  
A1L6M C2    H5     sing N N 68  
A1L6M C5    H6     sing N N 69  
A1L6M C5    H7     sing N N 70  
A1L6M C5    H8     sing N N 71  
A1L6M C8    H9     sing N N 72  
A1L6M C11   H11    sing N N 73  
A1L6M C11   H12    sing N N 74  
A1L6M C11   H13    sing N N 75  
A1L6M C13   H14    sing N N 76  
A1L6M C13   H15    sing N N 77  
A1L6M C14   H16    sing N N 78  
A1L6M C14   H17    sing N N 79  
A1L6M O2    H18    sing N N 80  
A1L6M N2    H19    sing N N 81  
A1L6M C17   H20    sing N N 82  
A1L6M C20   H23    sing N N 83  
A1L6M C24   H25    sing N N 84  
A1L6M O5    H26    sing N N 85  
A1L6M C25   H27    sing N N 86  
A1L6M C25   H28    sing N N 87  
A1L6M C26   H29    sing N N 88  
A1L6M C26   H30    sing N N 89  
A1L6M C27   H31    sing N N 90  
A1L6M C29   H32    sing N N 91  
A1L6M C29   H33    sing N N 92  
A1L6M C29   H34    sing N N 93  
A1L6M C30   H35    sing N N 94  
A1L6M C30   H36    sing N N 95  
A1L6M C31   H37    sing N N 96  
A1L6M C31   H38    sing N N 97  
A1L6M C32   H39    sing N N 98  
A1L6M C34   H40    sing N N 99  
A1L6M C34   H41    sing N N 100 
A1L6M C34   H42    sing N N 101 
A1L6M C35   H43    sing N N 102 
A1L6M C35   H44    sing N N 103 
A1L6M C36   H45    sing N N 104 
A1L6M C36   H46    sing N N 105 
A1L6M C37   H47    sing N N 106 
A1L6M C39   H48    sing N N 107 
A1L6M C39   H49    sing N N 108 
A1L6M C39   H50    sing N N 109 
A1L6M C40   H51    sing N N 110 
A1L6M C40   H52    sing N N 111 
A1L6M C40   H53    sing N N 112 
A1L6M C42   H54    sing N N 113 
A1L6M C42   H55    sing N N 114 
A1L6M C42   H56    sing N N 115 
A1L6M C44   H57    sing N N 116 
A1L6M C44   H58    sing N N 117 
A1L6M O6    H59    sing N N 118 
A1L6M C46   H60    sing N N 119 
A1L6M C46   H61    sing N N 120 
A1L6M C47   H62    sing N N 121 
A1L6M C47   H63    sing N N 122 
A1L6M N1    H65    sing N N 123 
A1L6M N4    H10    sing N N 124 
A1L6M O7    H21    sing N N 125 
ALA   N     CA     sing N N 126 
ALA   N     H      sing N N 127 
ALA   N     H2     sing N N 128 
ALA   CA    C      sing N N 129 
ALA   CA    CB     sing N N 130 
ALA   CA    HA     sing N N 131 
ALA   C     O      doub N N 132 
ALA   C     OXT    sing N N 133 
ALA   CB    HB1    sing N N 134 
ALA   CB    HB2    sing N N 135 
ALA   CB    HB3    sing N N 136 
ALA   OXT   HXT    sing N N 137 
ARG   N     CA     sing N N 138 
ARG   N     H      sing N N 139 
ARG   N     H2     sing N N 140 
ARG   CA    C      sing N N 141 
ARG   CA    CB     sing N N 142 
ARG   CA    HA     sing N N 143 
ARG   C     O      doub N N 144 
ARG   C     OXT    sing N N 145 
ARG   CB    CG     sing N N 146 
ARG   CB    HB2    sing N N 147 
ARG   CB    HB3    sing N N 148 
ARG   CG    CD     sing N N 149 
ARG   CG    HG2    sing N N 150 
ARG   CG    HG3    sing N N 151 
ARG   CD    NE     sing N N 152 
ARG   CD    HD2    sing N N 153 
ARG   CD    HD3    sing N N 154 
ARG   NE    CZ     sing N N 155 
ARG   NE    HE     sing N N 156 
ARG   CZ    NH1    sing N N 157 
ARG   CZ    NH2    doub N N 158 
ARG   NH1   HH11   sing N N 159 
ARG   NH1   HH12   sing N N 160 
ARG   NH2   HH21   sing N N 161 
ARG   NH2   HH22   sing N N 162 
ARG   OXT   HXT    sing N N 163 
ASN   N     CA     sing N N 164 
ASN   N     H      sing N N 165 
ASN   N     H2     sing N N 166 
ASN   CA    C      sing N N 167 
ASN   CA    CB     sing N N 168 
ASN   CA    HA     sing N N 169 
ASN   C     O      doub N N 170 
ASN   C     OXT    sing N N 171 
ASN   CB    CG     sing N N 172 
ASN   CB    HB2    sing N N 173 
ASN   CB    HB3    sing N N 174 
ASN   CG    OD1    doub N N 175 
ASN   CG    ND2    sing N N 176 
ASN   ND2   HD21   sing N N 177 
ASN   ND2   HD22   sing N N 178 
ASN   OXT   HXT    sing N N 179 
ASP   N     CA     sing N N 180 
ASP   N     H      sing N N 181 
ASP   N     H2     sing N N 182 
ASP   CA    C      sing N N 183 
ASP   CA    CB     sing N N 184 
ASP   CA    HA     sing N N 185 
ASP   C     O      doub N N 186 
ASP   C     OXT    sing N N 187 
ASP   CB    CG     sing N N 188 
ASP   CB    HB2    sing N N 189 
ASP   CB    HB3    sing N N 190 
ASP   CG    OD1    doub N N 191 
ASP   CG    OD2    sing N N 192 
ASP   OD2   HD2    sing N N 193 
ASP   OXT   HXT    sing N N 194 
AZI   N1    N2     doub N N 195 
AZI   N2    N3     doub N N 196 
CSD   N     CA     sing N N 197 
CSD   N     H      sing N N 198 
CSD   N     H2     sing N N 199 
CSD   CA    CB     sing N N 200 
CSD   CA    C      sing N N 201 
CSD   CA    HA     sing N N 202 
CSD   CB    SG     sing N N 203 
CSD   CB    HB2    sing N N 204 
CSD   CB    HB3    sing N N 205 
CSD   SG    OD1    doub N N 206 
CSD   SG    OD2    sing N N 207 
CSD   C     O      doub N N 208 
CSD   C     OXT    sing N N 209 
CSD   OXT   HXT    sing N N 210 
CSD   OD2   HD2    sing N N 211 
CYS   N     CA     sing N N 212 
CYS   N     H      sing N N 213 
CYS   N     H2     sing N N 214 
CYS   CA    C      sing N N 215 
CYS   CA    CB     sing N N 216 
CYS   CA    HA     sing N N 217 
CYS   C     O      doub N N 218 
CYS   C     OXT    sing N N 219 
CYS   CB    SG     sing N N 220 
CYS   CB    HB2    sing N N 221 
CYS   CB    HB3    sing N N 222 
CYS   SG    HG     sing N N 223 
CYS   OXT   HXT    sing N N 224 
GLN   N     CA     sing N N 225 
GLN   N     H      sing N N 226 
GLN   N     H2     sing N N 227 
GLN   CA    C      sing N N 228 
GLN   CA    CB     sing N N 229 
GLN   CA    HA     sing N N 230 
GLN   C     O      doub N N 231 
GLN   C     OXT    sing N N 232 
GLN   CB    CG     sing N N 233 
GLN   CB    HB2    sing N N 234 
GLN   CB    HB3    sing N N 235 
GLN   CG    CD     sing N N 236 
GLN   CG    HG2    sing N N 237 
GLN   CG    HG3    sing N N 238 
GLN   CD    OE1    doub N N 239 
GLN   CD    NE2    sing N N 240 
GLN   NE2   HE21   sing N N 241 
GLN   NE2   HE22   sing N N 242 
GLN   OXT   HXT    sing N N 243 
GLU   N     CA     sing N N 244 
GLU   N     H      sing N N 245 
GLU   N     H2     sing N N 246 
GLU   CA    C      sing N N 247 
GLU   CA    CB     sing N N 248 
GLU   CA    HA     sing N N 249 
GLU   C     O      doub N N 250 
GLU   C     OXT    sing N N 251 
GLU   CB    CG     sing N N 252 
GLU   CB    HB2    sing N N 253 
GLU   CB    HB3    sing N N 254 
GLU   CG    CD     sing N N 255 
GLU   CG    HG2    sing N N 256 
GLU   CG    HG3    sing N N 257 
GLU   CD    OE1    doub N N 258 
GLU   CD    OE2    sing N N 259 
GLU   OE2   HE2    sing N N 260 
GLU   OXT   HXT    sing N N 261 
GLY   N     CA     sing N N 262 
GLY   N     H      sing N N 263 
GLY   N     H2     sing N N 264 
GLY   CA    C      sing N N 265 
GLY   CA    HA2    sing N N 266 
GLY   CA    HA3    sing N N 267 
GLY   C     O      doub N N 268 
GLY   C     OXT    sing N N 269 
GLY   OXT   HXT    sing N N 270 
HIS   N     CA     sing N N 271 
HIS   N     H      sing N N 272 
HIS   N     H2     sing N N 273 
HIS   CA    C      sing N N 274 
HIS   CA    CB     sing N N 275 
HIS   CA    HA     sing N N 276 
HIS   C     O      doub N N 277 
HIS   C     OXT    sing N N 278 
HIS   CB    CG     sing N N 279 
HIS   CB    HB2    sing N N 280 
HIS   CB    HB3    sing N N 281 
HIS   CG    ND1    sing Y N 282 
HIS   CG    CD2    doub Y N 283 
HIS   ND1   CE1    doub Y N 284 
HIS   ND1   HD1    sing N N 285 
HIS   CD2   NE2    sing Y N 286 
HIS   CD2   HD2    sing N N 287 
HIS   CE1   NE2    sing Y N 288 
HIS   CE1   HE1    sing N N 289 
HIS   NE2   HE2    sing N N 290 
HIS   OXT   HXT    sing N N 291 
HOH   O     H1     sing N N 292 
HOH   O     H2     sing N N 293 
ILE   N     CA     sing N N 294 
ILE   N     H      sing N N 295 
ILE   N     H2     sing N N 296 
ILE   CA    C      sing N N 297 
ILE   CA    CB     sing N N 298 
ILE   CA    HA     sing N N 299 
ILE   C     O      doub N N 300 
ILE   C     OXT    sing N N 301 
ILE   CB    CG1    sing N N 302 
ILE   CB    CG2    sing N N 303 
ILE   CB    HB     sing N N 304 
ILE   CG1   CD1    sing N N 305 
ILE   CG1   HG12   sing N N 306 
ILE   CG1   HG13   sing N N 307 
ILE   CG2   HG21   sing N N 308 
ILE   CG2   HG22   sing N N 309 
ILE   CG2   HG23   sing N N 310 
ILE   CD1   HD11   sing N N 311 
ILE   CD1   HD12   sing N N 312 
ILE   CD1   HD13   sing N N 313 
ILE   OXT   HXT    sing N N 314 
LEU   N     CA     sing N N 315 
LEU   N     H      sing N N 316 
LEU   N     H2     sing N N 317 
LEU   CA    C      sing N N 318 
LEU   CA    CB     sing N N 319 
LEU   CA    HA     sing N N 320 
LEU   C     O      doub N N 321 
LEU   C     OXT    sing N N 322 
LEU   CB    CG     sing N N 323 
LEU   CB    HB2    sing N N 324 
LEU   CB    HB3    sing N N 325 
LEU   CG    CD1    sing N N 326 
LEU   CG    CD2    sing N N 327 
LEU   CG    HG     sing N N 328 
LEU   CD1   HD11   sing N N 329 
LEU   CD1   HD12   sing N N 330 
LEU   CD1   HD13   sing N N 331 
LEU   CD2   HD21   sing N N 332 
LEU   CD2   HD22   sing N N 333 
LEU   CD2   HD23   sing N N 334 
LEU   OXT   HXT    sing N N 335 
LUT   C1    C2     sing N N 336 
LUT   C1    C6     sing N N 337 
LUT   C1    C16    sing N N 338 
LUT   C1    C17    sing N N 339 
LUT   C2    C3     sing N N 340 
LUT   C2    H21    sing N N 341 
LUT   C2    H22    sing N N 342 
LUT   C3    C4     sing N N 343 
LUT   C3    O3     sing N N 344 
LUT   C3    H3     sing N N 345 
LUT   C4    C5     sing N N 346 
LUT   C4    H41    sing N N 347 
LUT   C4    H42    sing N N 348 
LUT   C5    C6     doub N N 349 
LUT   C5    C18    sing N N 350 
LUT   C6    C7     sing N N 351 
LUT   C7    C8     doub N E 352 
LUT   C7    H7     sing N N 353 
LUT   C8    C9     sing N N 354 
LUT   C8    H8     sing N N 355 
LUT   C9    C10    doub N E 356 
LUT   C9    C19    sing N N 357 
LUT   C10   C11    sing N N 358 
LUT   C10   H10    sing N N 359 
LUT   C11   C12    doub N E 360 
LUT   C11   H11    sing N N 361 
LUT   C12   C13    sing N N 362 
LUT   C12   H12    sing N N 363 
LUT   C13   C14    doub N E 364 
LUT   C13   C20    sing N N 365 
LUT   C14   C15    sing N N 366 
LUT   C14   H14    sing N N 367 
LUT   C15   C35    doub N E 368 
LUT   C15   H15    sing N N 369 
LUT   C16   H161   sing N N 370 
LUT   C16   H162   sing N N 371 
LUT   C16   H163   sing N N 372 
LUT   C17   H171   sing N N 373 
LUT   C17   H172   sing N N 374 
LUT   C17   H173   sing N N 375 
LUT   C18   H181   sing N N 376 
LUT   C18   H182   sing N N 377 
LUT   C18   H183   sing N N 378 
LUT   C19   H191   sing N N 379 
LUT   C19   H192   sing N N 380 
LUT   C19   H193   sing N N 381 
LUT   C20   H201   sing N N 382 
LUT   C20   H202   sing N N 383 
LUT   C20   H203   sing N N 384 
LUT   O3    HO3    sing N N 385 
LUT   C21   C22    sing N N 386 
LUT   C21   C26    sing N N 387 
LUT   C21   C36    sing N N 388 
LUT   C21   C37    sing N N 389 
LUT   C22   C23    sing N N 390 
LUT   C22   H221   sing N N 391 
LUT   C22   H222   sing N N 392 
LUT   C23   C24    sing N N 393 
LUT   C23   O23    sing N N 394 
LUT   C23   H23    sing N N 395 
LUT   C24   C25    doub N N 396 
LUT   C24   H24    sing N N 397 
LUT   C25   C26    sing N N 398 
LUT   C25   C38    sing N N 399 
LUT   C26   C27    sing N N 400 
LUT   C26   H26    sing N N 401 
LUT   C27   C28    doub N E 402 
LUT   C27   H27    sing N N 403 
LUT   C28   C29    sing N N 404 
LUT   C28   H28    sing N N 405 
LUT   C29   C30    doub N E 406 
LUT   C29   C39    sing N N 407 
LUT   C30   C31    sing N N 408 
LUT   C30   H30    sing N N 409 
LUT   C31   C32    doub N E 410 
LUT   C31   H31    sing N N 411 
LUT   C32   C33    sing N N 412 
LUT   C32   H32    sing N N 413 
LUT   C33   C34    doub N E 414 
LUT   C33   C40    sing N N 415 
LUT   C34   C35    sing N N 416 
LUT   C34   H34    sing N N 417 
LUT   C35   H35    sing N N 418 
LUT   C36   H361   sing N N 419 
LUT   C36   H362   sing N N 420 
LUT   C36   H363   sing N N 421 
LUT   C37   H371   sing N N 422 
LUT   C37   H372   sing N N 423 
LUT   C37   H373   sing N N 424 
LUT   C38   H381   sing N N 425 
LUT   C38   H382   sing N N 426 
LUT   C38   H383   sing N N 427 
LUT   C39   H391   sing N N 428 
LUT   C39   H392   sing N N 429 
LUT   C39   H393   sing N N 430 
LUT   C40   H401   sing N N 431 
LUT   C40   H402   sing N N 432 
LUT   C40   H403   sing N N 433 
LUT   O23   H1     sing N N 434 
LYS   N     CA     sing N N 435 
LYS   N     H      sing N N 436 
LYS   N     H2     sing N N 437 
LYS   CA    C      sing N N 438 
LYS   CA    CB     sing N N 439 
LYS   CA    HA     sing N N 440 
LYS   C     O      doub N N 441 
LYS   C     OXT    sing N N 442 
LYS   CB    CG     sing N N 443 
LYS   CB    HB2    sing N N 444 
LYS   CB    HB3    sing N N 445 
LYS   CG    CD     sing N N 446 
LYS   CG    HG2    sing N N 447 
LYS   CG    HG3    sing N N 448 
LYS   CD    CE     sing N N 449 
LYS   CD    HD2    sing N N 450 
LYS   CD    HD3    sing N N 451 
LYS   CE    NZ     sing N N 452 
LYS   CE    HE2    sing N N 453 
LYS   CE    HE3    sing N N 454 
LYS   NZ    HZ1    sing N N 455 
LYS   NZ    HZ2    sing N N 456 
LYS   NZ    HZ3    sing N N 457 
LYS   OXT   HXT    sing N N 458 
MET   N     CA     sing N N 459 
MET   N     H      sing N N 460 
MET   N     H2     sing N N 461 
MET   CA    C      sing N N 462 
MET   CA    CB     sing N N 463 
MET   CA    HA     sing N N 464 
MET   C     O      doub N N 465 
MET   C     OXT    sing N N 466 
MET   CB    CG     sing N N 467 
MET   CB    HB2    sing N N 468 
MET   CB    HB3    sing N N 469 
MET   CG    SD     sing N N 470 
MET   CG    HG2    sing N N 471 
MET   CG    HG3    sing N N 472 
MET   SD    CE     sing N N 473 
MET   CE    HE1    sing N N 474 
MET   CE    HE2    sing N N 475 
MET   CE    HE3    sing N N 476 
MET   OXT   HXT    sing N N 477 
PHE   N     CA     sing N N 478 
PHE   N     H      sing N N 479 
PHE   N     H2     sing N N 480 
PHE   CA    C      sing N N 481 
PHE   CA    CB     sing N N 482 
PHE   CA    HA     sing N N 483 
PHE   C     O      doub N N 484 
PHE   C     OXT    sing N N 485 
PHE   CB    CG     sing N N 486 
PHE   CB    HB2    sing N N 487 
PHE   CB    HB3    sing N N 488 
PHE   CG    CD1    doub Y N 489 
PHE   CG    CD2    sing Y N 490 
PHE   CD1   CE1    sing Y N 491 
PHE   CD1   HD1    sing N N 492 
PHE   CD2   CE2    doub Y N 493 
PHE   CD2   HD2    sing N N 494 
PHE   CE1   CZ     doub Y N 495 
PHE   CE1   HE1    sing N N 496 
PHE   CE2   CZ     sing Y N 497 
PHE   CE2   HE2    sing N N 498 
PHE   CZ    HZ     sing N N 499 
PHE   OXT   HXT    sing N N 500 
PLC   C1    C2     sing N N 501 
PLC   C1    O3P    sing N N 502 
PLC   C1    H11    sing N N 503 
PLC   C1    H12    sing N N 504 
PLC   C2    C3     sing N N 505 
PLC   C2    O2     sing N N 506 
PLC   C2    H2     sing N N 507 
PLC   C3    O3     sing N N 508 
PLC   C3    H31    sing N N 509 
PLC   C3    H32    sing N N 510 
PLC   C4    C5     sing N N 511 
PLC   C4    O4P    sing N N 512 
PLC   C4    H41    sing N N 513 
PLC   C4    H42    sing N N 514 
PLC   C5    N      sing N N 515 
PLC   C5    H51    sing N N 516 
PLC   C5    H52    sing N N 517 
PLC   C6    N      sing N N 518 
PLC   C6    H61    sing N N 519 
PLC   C6    H62    sing N N 520 
PLC   C6    H63    sing N N 521 
PLC   C7    N      sing N N 522 
PLC   C7    H71    sing N N 523 
PLC   C7    H72    sing N N 524 
PLC   C7    H73    sing N N 525 
PLC   C8    N      sing N N 526 
PLC   C8    H81    sing N N 527 
PLC   C8    H82    sing N N 528 
PLC   C8    H83    sing N N 529 
PLC   "C'"  "C1'"  sing N N 530 
PLC   "C'"  "O'"   doub N N 531 
PLC   "C'"  O2     sing N N 532 
PLC   "C1'" "C2'"  sing N N 533 
PLC   "C1'" "H1'1" sing N N 534 
PLC   "C1'" "H1'2" sing N N 535 
PLC   "C2'" "C3'"  sing N N 536 
PLC   "C2'" "H2'1" sing N N 537 
PLC   "C2'" "H2'2" sing N N 538 
PLC   "C3'" "C4'"  sing N N 539 
PLC   "C3'" "H3'1" sing N N 540 
PLC   "C3'" "H3'2" sing N N 541 
PLC   "C4'" "C5'"  sing N N 542 
PLC   "C4'" "H4'1" sing N N 543 
PLC   "C4'" "H4'2" sing N N 544 
PLC   "C5'" "C6'"  sing N N 545 
PLC   "C5'" "H5'1" sing N N 546 
PLC   "C5'" "H5'2" sing N N 547 
PLC   "C6'" "C7'"  sing N N 548 
PLC   "C6'" "H6'1" sing N N 549 
PLC   "C6'" "H6'2" sing N N 550 
PLC   "C7'" "C8'"  sing N N 551 
PLC   "C7'" "H7'1" sing N N 552 
PLC   "C7'" "H7'2" sing N N 553 
PLC   "C8'" "C9'"  sing N N 554 
PLC   "C8'" "H8'1" sing N N 555 
PLC   "C8'" "H8'2" sing N N 556 
PLC   "C9'" "CA'"  sing N N 557 
PLC   "C9'" "H9'1" sing N N 558 
PLC   "C9'" "H9'2" sing N N 559 
PLC   "CA'" "CB'"  sing N N 560 
PLC   "CA'" "HT'1" sing N N 561 
PLC   "CA'" "HT'2" sing N N 562 
PLC   "CB'" "HE'1" sing N N 563 
PLC   "CB'" "HE'2" sing N N 564 
PLC   "CB'" "HE'3" sing N N 565 
PLC   CB    C1B    sing N N 566 
PLC   CB    OB     doub N N 567 
PLC   CB    O3     sing N N 568 
PLC   C1B   C2B    sing N N 569 
PLC   C1B   H1A1   sing N N 570 
PLC   C1B   H1A2   sing N N 571 
PLC   C2B   C3B    sing N N 572 
PLC   C2B   H2A1   sing N N 573 
PLC   C2B   H2A2   sing N N 574 
PLC   C3B   C4B    sing N N 575 
PLC   C3B   H3A1   sing N N 576 
PLC   C3B   H3A2   sing N N 577 
PLC   C4B   C5B    sing N N 578 
PLC   C4B   H4A1   sing N N 579 
PLC   C4B   H4A2   sing N N 580 
PLC   C5B   C6B    sing N N 581 
PLC   C5B   H5A1   sing N N 582 
PLC   C5B   H5A2   sing N N 583 
PLC   C6B   C7B    sing N N 584 
PLC   C6B   H6A1   sing N N 585 
PLC   C6B   H6A2   sing N N 586 
PLC   C7B   C8B    sing N N 587 
PLC   C7B   H7A1   sing N N 588 
PLC   C7B   H7A2   sing N N 589 
PLC   C8B   C9B    sing N N 590 
PLC   C8B   H8A1   sing N N 591 
PLC   C8B   H8A2   sing N N 592 
PLC   C9B   CAA    sing N N 593 
PLC   C9B   H9A1   sing N N 594 
PLC   C9B   H9A2   sing N N 595 
PLC   CAA   CBA    sing N N 596 
PLC   CAA   HTA1   sing N N 597 
PLC   CAA   HTA2   sing N N 598 
PLC   CBA   HEA1   sing N N 599 
PLC   CBA   HEA2   sing N N 600 
PLC   CBA   HEA3   sing N N 601 
PLC   O1P   P      doub N N 602 
PLC   O2P   P      sing N N 603 
PLC   O2P   HOP2   sing N N 604 
PLC   O3P   P      sing N N 605 
PLC   O4P   P      sing N N 606 
PRO   N     CA     sing N N 607 
PRO   N     CD     sing N N 608 
PRO   N     H      sing N N 609 
PRO   CA    C      sing N N 610 
PRO   CA    CB     sing N N 611 
PRO   CA    HA     sing N N 612 
PRO   C     O      doub N N 613 
PRO   C     OXT    sing N N 614 
PRO   CB    CG     sing N N 615 
PRO   CB    HB2    sing N N 616 
PRO   CB    HB3    sing N N 617 
PRO   CG    CD     sing N N 618 
PRO   CG    HG2    sing N N 619 
PRO   CG    HG3    sing N N 620 
PRO   CD    HD2    sing N N 621 
PRO   CD    HD3    sing N N 622 
PRO   OXT   HXT    sing N N 623 
SER   N     CA     sing N N 624 
SER   N     H      sing N N 625 
SER   N     H2     sing N N 626 
SER   CA    C      sing N N 627 
SER   CA    CB     sing N N 628 
SER   CA    HA     sing N N 629 
SER   C     O      doub N N 630 
SER   C     OXT    sing N N 631 
SER   CB    OG     sing N N 632 
SER   CB    HB2    sing N N 633 
SER   CB    HB3    sing N N 634 
SER   OG    HG     sing N N 635 
SER   OXT   HXT    sing N N 636 
THR   N     CA     sing N N 637 
THR   N     H      sing N N 638 
THR   N     H2     sing N N 639 
THR   CA    C      sing N N 640 
THR   CA    CB     sing N N 641 
THR   CA    HA     sing N N 642 
THR   C     O      doub N N 643 
THR   C     OXT    sing N N 644 
THR   CB    OG1    sing N N 645 
THR   CB    CG2    sing N N 646 
THR   CB    HB     sing N N 647 
THR   OG1   HG1    sing N N 648 
THR   CG2   HG21   sing N N 649 
THR   CG2   HG22   sing N N 650 
THR   CG2   HG23   sing N N 651 
THR   OXT   HXT    sing N N 652 
TRP   N     CA     sing N N 653 
TRP   N     H      sing N N 654 
TRP   N     H2     sing N N 655 
TRP   CA    C      sing N N 656 
TRP   CA    CB     sing N N 657 
TRP   CA    HA     sing N N 658 
TRP   C     O      doub N N 659 
TRP   C     OXT    sing N N 660 
TRP   CB    CG     sing N N 661 
TRP   CB    HB2    sing N N 662 
TRP   CB    HB3    sing N N 663 
TRP   CG    CD1    doub Y N 664 
TRP   CG    CD2    sing Y N 665 
TRP   CD1   NE1    sing Y N 666 
TRP   CD1   HD1    sing N N 667 
TRP   CD2   CE2    doub Y N 668 
TRP   CD2   CE3    sing Y N 669 
TRP   NE1   CE2    sing Y N 670 
TRP   NE1   HE1    sing N N 671 
TRP   CE2   CZ2    sing Y N 672 
TRP   CE3   CZ3    doub Y N 673 
TRP   CE3   HE3    sing N N 674 
TRP   CZ2   CH2    doub Y N 675 
TRP   CZ2   HZ2    sing N N 676 
TRP   CZ3   CH2    sing Y N 677 
TRP   CZ3   HZ3    sing N N 678 
TRP   CH2   HH2    sing N N 679 
TRP   OXT   HXT    sing N N 680 
TYR   N     CA     sing N N 681 
TYR   N     H      sing N N 682 
TYR   N     H2     sing N N 683 
TYR   CA    C      sing N N 684 
TYR   CA    CB     sing N N 685 
TYR   CA    HA     sing N N 686 
TYR   C     O      doub N N 687 
TYR   C     OXT    sing N N 688 
TYR   CB    CG     sing N N 689 
TYR   CB    HB2    sing N N 690 
TYR   CB    HB3    sing N N 691 
TYR   CG    CD1    doub Y N 692 
TYR   CG    CD2    sing Y N 693 
TYR   CD1   CE1    sing Y N 694 
TYR   CD1   HD1    sing N N 695 
TYR   CD2   CE2    doub Y N 696 
TYR   CD2   HD2    sing N N 697 
TYR   CE1   CZ     doub Y N 698 
TYR   CE1   HE1    sing N N 699 
TYR   CE2   CZ     sing Y N 700 
TYR   CE2   HE2    sing N N 701 
TYR   CZ    OH     sing N N 702 
TYR   OH    HH     sing N N 703 
TYR   OXT   HXT    sing N N 704 
VAL   N     CA     sing N N 705 
VAL   N     H      sing N N 706 
VAL   N     H2     sing N N 707 
VAL   CA    C      sing N N 708 
VAL   CA    CB     sing N N 709 
VAL   CA    HA     sing N N 710 
VAL   C     O      doub N N 711 
VAL   C     OXT    sing N N 712 
VAL   CB    CG1    sing N N 713 
VAL   CB    CG2    sing N N 714 
VAL   CB    HB     sing N N 715 
VAL   CG1   HG11   sing N N 716 
VAL   CG1   HG12   sing N N 717 
VAL   CG1   HG13   sing N N 718 
VAL   CG2   HG21   sing N N 719 
VAL   CG2   HG22   sing N N 720 
VAL   CG2   HG23   sing N N 721 
VAL   OXT   HXT    sing N N 722 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Higher Education of the Russian Federation' 
_pdbx_audit_support.country                'Russian Federation' 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KUE 
_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]   0.021022 
_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]   0.011461 
_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]   0.005966 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . GLY   A 1 2   ? -7.255  -32.318 5.061   1.00 53.95  ?  1   GLY   A N     1 
ATOM   2    C CA    . GLY   A 1 2   ? -6.303  -33.385 5.443   1.00 51.44  ?  1   GLY   A CA    1 
ATOM   3    C C     . GLY   A 1 2   ? -5.843  -34.224 4.244   1.00 50.27  ?  1   GLY   A C     1 
ATOM   4    O O     . GLY   A 1 2   ? -6.535  -34.248 3.220   1.00 52.67  ?  1   GLY   A O     1 
ATOM   5    N N     . SER   A 1 3   ? -4.699  -34.913 4.391   1.00 46.86  ?  2   SER   A N     1 
ATOM   6    C CA    . SER   A 1 3   ? -4.092  -35.696 3.328   1.00 45.65  ?  2   SER   A CA    1 
ATOM   7    C C     . SER   A 1 3   ? -4.627  -37.126 3.306   1.00 43.92  ?  2   SER   A C     1 
ATOM   8    O O     . SER   A 1 3   ? -4.673  -37.756 4.359   1.00 43.02  ?  2   SER   A O     1 
ATOM   9    C CB    . SER   A 1 3   ? -2.579  -35.767 3.485   1.00 45.11  ?  2   SER   A CB    1 
ATOM   10   O OG    . SER   A 1 3   ? -1.980  -34.486 3.461   1.00 46.12  ?  2   SER   A OG    1 
ATOM   11   N N     . GLN   A 1 4   ? -4.786  -37.678 2.088   1.00 44.05  ?  3   GLN   A N     1 
ATOM   12   C CA    . GLN   A 1 4   ? -5.114  -39.070 1.833   1.00 42.79  ?  3   GLN   A CA    1 
ATOM   13   C C     . GLN   A 1 4   ? -3.898  -39.825 1.304   1.00 40.25  ?  3   GLN   A C     1 
ATOM   14   O O     . GLN   A 1 4   ? -3.060  -39.188 0.691   1.00 40.18  ?  3   GLN   A O     1 
ATOM   15   C CB    . GLN   A 1 4   ? -6.249  -39.098 0.816   1.00 45.16  ?  3   GLN   A CB    1 
ATOM   16   C CG    . GLN   A 1 4   ? -7.531  -38.432 1.295   1.00 48.94  ?  3   GLN   A CG    1 
ATOM   17   C CD    . GLN   A 1 4   ? -7.963  -38.947 2.651   1.00 50.57  ?  3   GLN   A CD    1 
ATOM   18   O OE1   . GLN   A 1 4   ? -8.392  -40.105 2.780   1.00 53.89  ?  3   GLN   A OE1   1 
ATOM   19   N NE2   . GLN   A 1 4   ? -7.707  -38.162 3.693   1.00 51.48  ?  3   GLN   A NE2   1 
ATOM   20   N N     . VAL   A 1 5   ? -3.842  -41.151 1.556   1.00 37.78  ?  4   VAL   A N     1 
ATOM   21   C CA    . VAL   A 1 5   ? -2.699  -41.996 1.220   1.00 36.54  ?  4   VAL   A CA    1 
ATOM   22   C C     . VAL   A 1 5   ? -3.159  -43.230 0.423   1.00 35.51  ?  4   VAL   A C     1 
ATOM   23   O O     . VAL   A 1 5   ? -4.187  -43.817 0.736   1.00 35.02  ?  4   VAL   A O     1 
ATOM   24   C CB    . VAL   A 1 5   ? -1.832  -42.387 2.441   1.00 35.21  ?  4   VAL   A CB    1 
ATOM   25   C CG1   . VAL   A 1 5   ? -2.492  -43.386 3.396   1.00 34.35  ?  4   VAL   A CG1   1 
ATOM   26   C CG2   . VAL   A 1 5   ? -0.488  -42.941 2.014   1.00 34.61  ?  4   VAL   A CG2   1 
ATOM   27   N N     . GLU   A 1 6   ? -2.391  -43.581 -0.622  1.00 35.20  ?  5   GLU   A N     1 
ATOM   28   C CA    . GLU   A 1 6   ? -2.497  -44.828 -1.367  1.00 35.55  ?  5   GLU   A CA    1 
ATOM   29   C C     . GLU   A 1 6   ? -1.086  -45.416 -1.474  1.00 34.40  ?  5   GLU   A C     1 
ATOM   30   O O     . GLU   A 1 6   ? -0.221  -44.839 -2.142  1.00 34.83  ?  5   GLU   A O     1 
ATOM   31   C CB    . GLU   A 1 6   ? -3.058  -44.609 -2.758  1.00 37.41  ?  5   GLU   A CB    1 
ATOM   32   C CG    . GLU   A 1 6   ? -4.487  -44.076 -2.780  1.00 39.35  ?  5   GLU   A CG    1 
ATOM   33   C CD    . GLU   A 1 6   ? -4.941  -43.659 -4.170  1.00 41.88  ?  5   GLU   A CD    1 
ATOM   34   O OE1   . GLU   A 1 6   ? -4.244  -44.013 -5.137  1.00 42.35  ?  5   GLU   A OE1   1 
ATOM   35   O OE2   . GLU   A 1 6   ? -5.962  -42.933 -4.328  1.00 44.71  -1 5   GLU   A OE2   1 
ATOM   36   N N     . PHE   A 1 7   ? -0.842  -46.513 -0.742  1.00 33.40  ?  6   PHE   A N     1 
ATOM   37   C CA    . PHE   A 1 7   ? 0.454   -47.167 -0.696  1.00 32.37  ?  6   PHE   A CA    1 
ATOM   38   C C     . PHE   A 1 7   ? 0.253   -48.592 -1.186  1.00 32.97  ?  6   PHE   A C     1 
ATOM   39   O O     . PHE   A 1 7   ? -0.345  -49.383 -0.470  1.00 32.56  ?  6   PHE   A O     1 
ATOM   40   C CB    . PHE   A 1 7   ? 1.034   -47.055 0.711   1.00 31.16  ?  6   PHE   A CB    1 
ATOM   41   C CG    . PHE   A 1 7   ? 2.333   -47.829 0.931   1.00 29.43  ?  6   PHE   A CG    1 
ATOM   42   C CD1   . PHE   A 1 7   ? 3.400   -47.719 0.039   1.00 29.66  ?  6   PHE   A CD1   1 
ATOM   43   C CD2   . PHE   A 1 7   ? 2.504   -48.626 2.060   1.00 28.18  ?  6   PHE   A CD2   1 
ATOM   44   C CE1   . PHE   A 1 7   ? 4.592   -48.419 0.251   1.00 28.84  ?  6   PHE   A CE1   1 
ATOM   45   C CE2   . PHE   A 1 7   ? 3.683   -49.325 2.262   1.00 27.30  ?  6   PHE   A CE2   1 
ATOM   46   C CZ    . PHE   A 1 7   ? 4.722   -49.237 1.353   1.00 27.44  ?  6   PHE   A CZ    1 
ATOM   47   N N     . SER   A 1 8   ? 0.687   -48.864 -2.424  1.00 34.67  ?  7   SER   A N     1 
ATOM   48   C CA    . SER   A 1 8   ? 0.809   -50.219 -2.947  1.00 36.61  ?  7   SER   A CA    1 
ATOM   49   C C     . SER   A 1 8   ? 2.206   -50.736 -2.629  1.00 34.41  ?  7   SER   A C     1 
ATOM   50   O O     . SER   A 1 8   ? 3.138   -49.984 -2.833  1.00 34.32  ?  7   SER   A O     1 
ATOM   51   C CB    . SER   A 1 8   ? 0.578   -50.264 -4.416  1.00 39.09  ?  7   SER   A CB    1 
ATOM   52   O OG    . SER   A 1 8   ? -0.803  -50.093 -4.662  1.00 45.59  ?  7   SER   A OG    1 
ATOM   53   N N     . MET   A 1 9   ? 2.334   -51.979 -2.148  1.00 33.96  ?  8   MET   A N     1 
ATOM   54   C CA    . MET   A 1 9   ? 3.650   -52.592 -1.995  1.00 35.21  ?  8   MET   A CA    1 
ATOM   55   C C     . MET   A 1 9   ? 3.581   -54.098 -2.213  1.00 32.74  ?  8   MET   A C     1 
ATOM   56   O O     . MET   A 1 9   ? 2.519   -54.677 -2.035  1.00 32.15  ?  8   MET   A O     1 
ATOM   57   C CB    . MET   A 1 9   ? 4.297   -52.257 -0.648  1.00 36.92  ?  8   MET   A CB    1 
ATOM   58   C CG    . MET   A 1 9   ? 3.432   -52.568 0.546   1.00 41.48  ?  8   MET   A CG    1 
ATOM   59   S SD    . MET   A 1 9   ? 4.280   -53.033 2.063   1.00 46.47  ?  8   MET   A SD    1 
ATOM   60   C CE    . MET   A 1 9   ? 5.009   -54.596 1.546   1.00 44.48  ?  8   MET   A CE    1 
ATOM   61   N N     . LYS   A 1 10  ? 4.728   -54.683 -2.591  1.00 31.44  ?  9   LYS   A N     1 
ATOM   62   C CA    . LYS   A 1 10  ? 4.940   -56.125 -2.743  1.00 31.04  ?  9   LYS   A CA    1 
ATOM   63   C C     . LYS   A 1 10  ? 6.146   -56.491 -1.864  1.00 29.13  ?  9   LYS   A C     1 
ATOM   64   O O     . LYS   A 1 10  ? 7.201   -55.885 -2.036  1.00 28.46  ?  9   LYS   A O     1 
ATOM   65   C CB    . LYS   A 1 10  ? 5.255   -56.615 -4.168  1.00 32.23  ?  9   LYS   A CB    1 
ATOM   66   C CG    . LYS   A 1 10  ? 4.485   -56.036 -5.385  0.50 34.77  ?  9   LYS   A CG    1 
ATOM   67   C CD    . LYS   A 1 10  ? 5.196   -56.021 -6.745  0.50 36.84  ?  9   LYS   A CD    1 
ATOM   68   C CE    . LYS   A 1 10  ? 6.596   -55.449 -6.702  1.00 37.37  ?  9   LYS   A CE    1 
ATOM   69   N NZ    . LYS   A 1 10  ? 7.137   -54.801 -7.883  1.00 40.18  1  9   LYS   A NZ    1 
ATOM   70   N N     . MET   A 1 11  ? 5.974   -57.424 -0.917  1.00 28.57  ?  10  MET   A N     1 
ATOM   71   C CA    . MET   A 1 11  ? 7.049   -57.904 -0.067  1.00 29.14  ?  10  MET   A CA    1 
ATOM   72   C C     . MET   A 1 11  ? 7.432   -59.282 -0.580  1.00 30.02  ?  10  MET   A C     1 
ATOM   73   O O     . MET   A 1 11  ? 6.552   -60.123 -0.672  1.00 32.22  ?  10  MET   A O     1 
ATOM   74   C CB    . MET   A 1 11  ? 6.681   -58.022 1.409   1.00 28.81  ?  10  MET   A CB    1 
ATOM   75   C CG    . MET   A 1 11  ? 7.885   -58.380 2.287   1.00 28.93  ?  10  MET   A CG    1 
ATOM   76   S SD    . MET   A 1 11  ? 7.547   -58.099 4.034   1.00 29.89  ?  10  MET   A SD    1 
ATOM   77   C CE    . MET   A 1 11  ? 6.567   -59.590 4.231   1.00 29.67  ?  10  MET   A CE    1 
ATOM   78   N N     . THR   A 1 12  ? 8.712   -59.481 -0.921  1.00 29.49  ?  11  THR   A N     1 
ATOM   79   C CA    . THR   A 1 12  ? 9.284   -60.785 -1.220  1.00 29.90  ?  11  THR   A CA    1 
ATOM   80   C C     . THR   A 1 12  ? 10.414  -61.061 -0.234  1.00 29.87  ?  11  THR   A C     1 
ATOM   81   O O     . THR   A 1 12  ? 10.828  -60.187 0.498   1.00 28.47  ?  11  THR   A O     1 
ATOM   82   C CB    . THR   A 1 12  ? 9.732   -60.881 -2.675  1.00 30.97  ?  11  THR   A CB    1 
ATOM   83   O OG1   . THR   A 1 12  ? 10.716  -59.883 -2.877  1.00 31.82  ?  11  THR   A OG1   1 
ATOM   84   C CG2   . THR   A 1 12  ? 8.601   -60.590 -3.646  1.00 31.36  ?  11  THR   A CG2   1 
ATOM   85   N N     . GLY   A 1 13  ? 10.879  -62.310 -0.205  1.00 32.36  ?  12  GLY   A N     1 
ATOM   86   C CA    . GLY   A 1 13  ? 11.898  -62.731 0.730   1.00 31.11  ?  12  GLY   A CA    1 
ATOM   87   C C     . GLY   A 1 13  ? 11.628  -64.133 1.230   1.00 30.40  ?  12  GLY   A C     1 
ATOM   88   O O     . GLY   A 1 13  ? 10.774  -64.840 0.716   1.00 30.18  ?  12  GLY   A O     1 
ATOM   89   N N     . GLY   A 1 14  ? 12.291  -64.449 2.334   1.00 28.68  ?  13  GLY   A N     1 
ATOM   90   C CA    . GLY   A 1 14  ? 12.263  -65.797 2.849   1.00 29.27  ?  13  GLY   A CA    1 
ATOM   91   C C     . GLY   A 1 14  ? 13.310  -66.018 3.940   1.00 27.97  ?  13  GLY   A C     1 
ATOM   92   O O     . GLY   A 1 14  ? 14.057  -65.102 4.328   1.00 27.51  ?  13  GLY   A O     1 
ATOM   93   N N     . GLU   A 1 15  ? 13.320  -67.255 4.431   1.00 26.94  ?  14  GLU   A N     1 
ATOM   94   C CA    . GLU   A 1 15  ? 14.228  -67.651 5.495   1.00 27.53  ?  14  GLU   A CA    1 
ATOM   95   C C     . GLU   A 1 15  ? 15.653  -67.851 4.927   1.00 26.90  ?  14  GLU   A C     1 
ATOM   96   O O     . GLU   A 1 15  ? 15.798  -68.129 3.759   1.00 27.16  ?  14  GLU   A O     1 
ATOM   97   C CB    . GLU   A 1 15  ? 13.605  -68.826 6.237   1.00 27.74  ?  14  GLU   A CB    1 
ATOM   98   C CG    . GLU   A 1 15  ? 12.393  -68.403 7.054   1.00 26.85  ?  14  GLU   A CG    1 
ATOM   99   C CD    . GLU   A 1 15  ? 11.638  -69.515 7.760   1.00 27.81  ?  14  GLU   A CD    1 
ATOM   100  O OE1   . GLU   A 1 15  ? 11.255  -70.524 7.088   1.00 31.40  ?  14  GLU   A OE1   1 
ATOM   101  O OE2   . GLU   A 1 15  ? 11.398  -69.334 8.969   1.00 27.60  -1 14  GLU   A OE2   1 
ATOM   102  N N     . ILE   A 1 16  ? 16.682  -67.584 5.729   1.00 26.05  ?  15  ILE   A N     1 
ATOM   103  C CA    . ILE   A 1 16  ? 18.092  -67.824 5.434   1.00 27.60  ?  15  ILE   A CA    1 
ATOM   104  C C     . ILE   A 1 16  ? 18.385  -69.255 5.895   1.00 28.85  ?  15  ILE   A C     1 
ATOM   105  O O     . ILE   A 1 16  ? 17.933  -69.599 7.002   1.00 28.07  ?  15  ILE   A O     1 
ATOM   106  C CB    . ILE   A 1 16  ? 18.998  -66.832 6.204   1.00 27.86  ?  15  ILE   A CB    1 
ATOM   107  C CG1   . ILE   A 1 16  ? 18.808  -65.381 5.699   1.00 28.45  ?  15  ILE   A CG1   1 
ATOM   108  C CG2   . ILE   A 1 16  ? 20.488  -67.220 6.170   1.00 29.29  ?  15  ILE   A CG2   1 
ATOM   109  C CD1   . ILE   A 1 16  ? 19.332  -64.302 6.631   1.00 27.41  ?  15  ILE   A CD1   1 
ATOM   110  N N     . PRO   A 1 17  ? 19.172  -70.099 5.162   1.00 30.69  ?  16  PRO   A N     1 
ATOM   111  C CA    . PRO   A 1 17  ? 19.585  -71.408 5.687   1.00 32.40  ?  16  PRO   A CA    1 
ATOM   112  C C     . PRO   A 1 17  ? 20.481  -71.326 6.919   1.00 32.57  ?  16  PRO   A C     1 
ATOM   113  O O     . PRO   A 1 17  ? 21.053  -70.289 7.182   1.00 33.62  ?  16  PRO   A O     1 
ATOM   114  C CB    . PRO   A 1 17  ? 20.289  -72.111 4.504   1.00 34.18  ?  16  PRO   A CB    1 
ATOM   115  C CG    . PRO   A 1 17  ? 19.888  -71.290 3.287   1.00 33.58  ?  16  PRO   A CG    1 
ATOM   116  C CD    . PRO   A 1 17  ? 19.620  -69.904 3.765   1.00 31.65  ?  16  PRO   A CD    1 
ATOM   117  N N     . GLY   A 1 18  ? 20.517  -72.403 7.715   1.00 34.62  ?  17  GLY   A N     1 
ATOM   118  C CA    . GLY   A 1 18  ? 21.552  -72.632 8.714   1.00 33.70  ?  17  GLY   A CA    1 
ATOM   119  C C     . GLY   A 1 18  ? 21.146  -72.108 10.086  1.00 31.42  ?  17  GLY   A C     1 
ATOM   120  O O     . GLY   A 1 18  ? 20.148  -71.401 10.227  1.00 30.24  ?  17  GLY   A O     1 
ATOM   121  N N     . GLY   A 1 19  ? 21.936  -72.494 11.095  1.00 29.75  ?  18  GLY   A N     1 
ATOM   122  C CA    . GLY   A 1 19  ? 21.803  -71.992 12.436  1.00 28.07  ?  18  GLY   A CA    1 
ATOM   123  C C     . GLY   A 1 19  ? 20.497  -72.482 13.062  1.00 26.24  ?  18  GLY   A C     1 
ATOM   124  O O     . GLY   A 1 19  ? 19.914  -73.472 12.639  1.00 26.33  ?  18  GLY   A O     1 
ATOM   125  N N     . ASN   A 1 20  ? 20.006  -71.712 14.001  1.00 24.94  ?  19  ASN   A N     1 
ATOM   126  C CA    . ASN   A 1 20  ? 18.832  -72.086 14.752  1.00 24.15  ?  19  ASN   A CA    1 
ATOM   127  C C     . ASN   A 1 20  ? 17.585  -71.814 13.909  1.00 23.92  ?  19  ASN   A C     1 
ATOM   128  O O     . ASN   A 1 20  ? 17.107  -70.718 13.950  1.00 24.10  ?  19  ASN   A O     1 
ATOM   129  C CB    . ASN   A 1 20  ? 18.878  -71.418 16.120  1.00 22.64  ?  19  ASN   A CB    1 
ATOM   130  C CG    . ASN   A 1 20  ? 17.645  -71.711 16.927  1.00 21.91  ?  19  ASN   A CG    1 
ATOM   131  O OD1   . ASN   A 1 20  ? 16.805  -72.556 16.549  1.00 22.26  ?  19  ASN   A OD1   1 
ATOM   132  N ND2   . ASN   A 1 20  ? 17.540  -71.040 18.054  1.00 20.95  ?  19  ASN   A ND2   1 
ATOM   133  N N     . ILE   A 1 21  ? 17.022  -72.839 13.271  1.00 25.06  ?  20  ILE   A N     1 
ATOM   134  C CA    . ILE   A 1 21  ? 15.851  -72.715 12.411  1.00 25.50  ?  20  ILE   A CA    1 
ATOM   135  C C     . ILE   A 1 21  ? 14.566  -72.452 13.199  1.00 24.90  ?  20  ILE   A C     1 
ATOM   136  O O     . ILE   A 1 21  ? 13.573  -72.000 12.625  1.00 24.49  ?  20  ILE   A O     1 
ATOM   137  C CB    . ILE   A 1 21  ? 15.694  -73.929 11.472  1.00 27.57  ?  20  ILE   A CB    1 
ATOM   138  C CG1   . ILE   A 1 21  ? 15.492  -75.270 12.226  1.00 28.92  ?  20  ILE   A CG1   1 
ATOM   139  C CG2   . ILE   A 1 21  ? 16.890  -74.030 10.511  1.00 28.48  ?  20  ILE   A CG2   1 
ATOM   140  C CD1   . ILE   A 1 21  ? 14.768  -76.310 11.401  1.00 30.28  ?  20  ILE   A CD1   1 
ATOM   141  N N     . VAL   A 1 22  ? 14.559  -72.746 14.503  1.00 24.76  ?  21  VAL   A N     1 
ATOM   142  C CA    . VAL   A 1 22  ? 13.459  -72.353 15.366  1.00 23.96  ?  21  VAL   A CA    1 
ATOM   143  C C     . VAL   A 1 22  ? 13.374  -70.822 15.362  1.00 22.83  ?  21  VAL   A C     1 
ATOM   144  O O     . VAL   A 1 22  ? 12.262  -70.306 15.259  1.00 23.22  ?  21  VAL   A O     1 
ATOM   145  C CB    . VAL   A 1 22  ? 13.555  -73.005 16.776  1.00 24.29  ?  21  VAL   A CB    1 
ATOM   146  C CG1   . VAL   A 1 22  ? 12.447  -72.546 17.688  1.00 23.19  ?  21  VAL   A CG1   1 
ATOM   147  C CG2   . VAL   A 1 22  ? 13.603  -74.547 16.702  1.00 26.46  ?  21  VAL   A CG2   1 
ATOM   148  N N     . LEU   A 1 23  ? 14.518  -70.109 15.381  1.00 22.62  ?  22  LEU   A N     1 
ATOM   149  C CA    . LEU   A 1 23  ? 14.601  -68.654 15.197  1.00 21.78  ?  22  LEU   A CA    1 
ATOM   150  C C     . LEU   A 1 23  ? 15.286  -68.323 13.870  1.00 21.33  ?  22  LEU   A C     1 
ATOM   151  O O     . LEU   A 1 23  ? 16.168  -67.488 13.812  1.00 20.21  ?  22  LEU   A O     1 
ATOM   152  C CB    . LEU   A 1 23  ? 15.357  -68.045 16.376  1.00 21.49  ?  22  LEU   A CB    1 
ATOM   153  C CG    . LEU   A 1 23  ? 14.863  -68.442 17.771  1.00 22.28  ?  22  LEU   A CG    1 
ATOM   154  C CD1   . LEU   A 1 23  ? 15.676  -67.678 18.791  1.00 22.04  ?  22  LEU   A CD1   1 
ATOM   155  C CD2   . LEU   A 1 23  ? 13.374  -68.214 17.992  1.00 22.11  ?  22  LEU   A CD2   1 
ATOM   156  N N     . GLN   A 1 24  ? 14.785  -68.911 12.785  1.00 22.15  ?  23  GLN   A N     1 
ATOM   157  C CA    . GLN   A 1 24  ? 15.487  -68.896 11.518  1.00 22.79  ?  23  GLN   A CA    1 
ATOM   158  C C     . GLN   A 1 24  ? 15.692  -67.461 11.020  1.00 22.80  ?  23  GLN   A C     1 
ATOM   159  O O     . GLN   A 1 24  ? 14.797  -66.609 11.168  1.00 22.91  ?  23  GLN   A O     1 
ATOM   160  C CB    . GLN   A 1 24  ? 14.762  -69.701 10.442  1.00 22.94  ?  23  GLN   A CB    1 
ATOM   161  C CG    . GLN   A 1 24  ? 15.679  -70.126 9.300   1.00 23.20  ?  23  GLN   A CG    1 
ATOM   162  C CD    . GLN   A 1 24  ? 15.210  -71.337 8.527   1.00 24.34  ?  23  GLN   A CD    1 
ATOM   163  O OE1   . GLN   A 1 24  ? 14.269  -72.036 8.931   1.00 24.48  ?  23  GLN   A OE1   1 
ATOM   164  N NE2   . GLN   A 1 24  ? 15.885  -71.621 7.416   1.00 25.31  ?  23  GLN   A NE2   1 
ATOM   165  N N     . GLY   A 1 25  ? 16.876  -67.203 10.446  1.00 22.69  ?  24  GLY   A N     1 
ATOM   166  C CA    . GLY   A 1 25  ? 17.127  -65.905 9.860   1.00 22.63  ?  24  GLY   A CA    1 
ATOM   167  C C     . GLY   A 1 25  ? 16.182  -65.624 8.690   1.00 22.58  ?  24  GLY   A C     1 
ATOM   168  O O     . GLY   A 1 25  ? 15.670  -66.566 8.095   1.00 22.71  ?  24  GLY   A O     1 
ATOM   169  N N     . VAL   A 1 26  ? 15.968  -64.349 8.381   1.00 23.06  ?  25  VAL   A N     1 
ATOM   170  C CA    . VAL   A 1 26  ? 15.047  -63.907 7.331   1.00 24.25  ?  25  VAL   A CA    1 
ATOM   171  C C     . VAL   A 1 26  ? 15.732  -62.832 6.502   1.00 24.15  ?  25  VAL   A C     1 
ATOM   172  O O     . VAL   A 1 26  ? 16.552  -62.059 7.017   1.00 24.32  ?  25  VAL   A O     1 
ATOM   173  C CB    . VAL   A 1 26  ? 13.717  -63.353 7.911   1.00 24.92  ?  25  VAL   A CB    1 
ATOM   174  C CG1   . VAL   A 1 26  ? 12.990  -64.412 8.706   1.00 25.78  ?  25  VAL   A CG1   1 
ATOM   175  C CG2   . VAL   A 1 26  ? 13.888  -62.142 8.807   1.00 25.50  ?  25  VAL   A CG2   1 
ATOM   176  N N     . LYS   A 1 27  ? 15.323  -62.731 5.242   1.00 25.07  ?  26  LYS   A N     1 
ATOM   177  C CA    . LYS   A 1 27  ? 15.542  -61.549 4.443   1.00 25.27  ?  26  LYS   A CA    1 
ATOM   178  C C     . LYS   A 1 27  ? 14.234  -61.192 3.754   1.00 26.06  ?  26  LYS   A C     1 
ATOM   179  O O     . LYS   A 1 27  ? 13.487  -62.095 3.367   1.00 25.54  ?  26  LYS   A O     1 
ATOM   180  C CB    . LYS   A 1 27  ? 16.691  -61.608 3.443   1.00 26.55  ?  26  LYS   A CB    1 
ATOM   181  C CG    . LYS   A 1 27  ? 16.580  -62.545 2.264   1.00 28.32  ?  26  LYS   A CG    1 
ATOM   182  C CD    . LYS   A 1 27  ? 16.954  -63.984 2.577   1.00 29.78  ?  26  LYS   A CD    1 
ATOM   183  C CE    . LYS   A 1 27  ? 16.691  -64.828 1.370   1.00 31.17  ?  26  LYS   A CE    1 
ATOM   184  N NZ    . LYS   A 1 27  ? 17.183  -66.212 1.490   1.00 33.41  1  26  LYS   A NZ    1 
ATOM   185  N N     . LEU   A 1 28  ? 14.027  -59.872 3.599   1.00 27.32  ?  27  LEU   A N     1 
ATOM   186  C CA    . LEU   A 1 28  ? 12.793  -59.297 3.067   1.00 28.64  ?  27  LEU   A CA    1 
ATOM   187  C C     . LEU   A 1 28  ? 13.149  -58.160 2.111   1.00 28.83  ?  27  LEU   A C     1 
ATOM   188  O O     . LEU   A 1 28  ? 14.081  -57.411 2.360   1.00 27.89  ?  27  LEU   A O     1 
ATOM   189  C CB    . LEU   A 1 28  ? 11.922  -58.844 4.242   1.00 28.20  ?  27  LEU   A CB    1 
ATOM   190  C CG    . LEU   A 1 28  ? 11.431  -59.943 5.201   1.00 29.16  ?  27  LEU   A CG    1 
ATOM   191  C CD1   . LEU   A 1 28  ? 10.649  -59.358 6.356   1.00 29.71  ?  27  LEU   A CD1   1 
ATOM   192  C CD2   . LEU   A 1 28  ? 10.561  -61.002 4.569   1.00 30.77  ?  27  LEU   A CD2   1 
ATOM   193  N N     . ARG   A 1 29  ? 12.421  -58.050 1.002   1.00 30.57  ?  28  ARG   A N     1 
ATOM   194  C CA    . ARG   A 1 29  ? 12.498  -56.940 0.063   1.00 32.93  ?  28  ARG   A CA    1 
ATOM   195  C C     . ARG   A 1 29  ? 11.086  -56.377 -0.090  1.00 31.14  ?  28  ARG   A C     1 
ATOM   196  O O     . ARG   A 1 29  ? 10.198  -57.135 -0.486  1.00 29.08  ?  28  ARG   A O     1 
ATOM   197  C CB    . ARG   A 1 29  ? 13.086  -57.452 -1.253  1.00 37.30  ?  28  ARG   A CB    1 
ATOM   198  C CG    . ARG   A 1 29  ? 13.176  -56.375 -2.332  1.00 44.47  ?  28  ARG   A CG    1 
ATOM   199  C CD    . ARG   A 1 29  ? 14.465  -56.353 -3.156  1.00 52.31  ?  28  ARG   A CD    1 
ATOM   200  N NE    . ARG   A 1 29  ? 14.683  -57.203 -4.333  1.00 64.77  ?  28  ARG   A NE    1 
ATOM   201  C CZ    . ARG   A 1 29  ? 14.239  -56.952 -5.576  1.00 75.68  ?  28  ARG   A CZ    1 
ATOM   202  N NH1   . ARG   A 1 29  ? 12.998  -56.531 -5.818  1.00 72.95  1  28  ARG   A NH1   1 
ATOM   203  N NH2   . ARG   A 1 29  ? 15.044  -57.223 -6.592  1.00 81.87  ?  28  ARG   A NH2   1 
ATOM   204  N N     . ILE   A 1 30  ? 10.883  -55.091 0.264   1.00 30.22  ?  29  ILE   A N     1 
ATOM   205  C CA    . ILE   A 1 30  ? 9.645   -54.363 -0.008  1.00 30.89  ?  29  ILE   A CA    1 
ATOM   206  C C     . ILE   A 1 30  ? 9.927   -53.395 -1.156  1.00 31.81  ?  29  ILE   A C     1 
ATOM   207  O O     . ILE   A 1 30  ? 10.882  -52.624 -1.080  1.00 31.03  ?  29  ILE   A O     1 
ATOM   208  C CB    . ILE   A 1 30  ? 9.164   -53.631 1.248   1.00 30.41  ?  29  ILE   A CB    1 
ATOM   209  C CG1   . ILE   A 1 30  ? 8.766   -54.636 2.354   1.00 30.74  ?  29  ILE   A CG1   1 
ATOM   210  C CG2   . ILE   A 1 30  ? 8.063   -52.602 0.955   1.00 31.66  ?  29  ILE   A CG2   1 
ATOM   211  C CD1   . ILE   A 1 30  ? 9.860   -54.894 3.370   1.00 31.41  ?  29  ILE   A CD1   1 
ATOM   212  N N     . VAL   A 1 31  ? 9.088   -53.456 -2.192  1.00 31.74  ?  30  VAL   A N     1 
ATOM   213  C CA    . VAL   A 1 31  ? 9.031   -52.473 -3.252  1.00 32.91  ?  30  VAL   A CA    1 
ATOM   214  C C     . VAL   A 1 31  ? 7.607   -51.940 -3.260  1.00 33.08  ?  30  VAL   A C     1 
ATOM   215  O O     . VAL   A 1 31  ? 6.670   -52.735 -3.177  1.00 32.88  ?  30  VAL   A O     1 
ATOM   216  C CB    . VAL   A 1 31  ? 9.379   -53.122 -4.601  1.00 34.89  ?  30  VAL   A CB    1 
ATOM   217  C CG1   . VAL   A 1 31  ? 9.198   -52.169 -5.778  1.00 37.70  ?  30  VAL   A CG1   1 
ATOM   218  C CG2   . VAL   A 1 31  ? 10.778  -53.720 -4.611  1.00 35.59  ?  30  VAL   A CG2   1 
ATOM   219  N N     . GLY   A 1 32  ? 7.456   -50.625 -3.477  1.00 34.04  ?  31  GLY   A N     1 
ATOM   220  C CA    . GLY   A 1 32  ? 6.142   -50.032 -3.640  1.00 34.16  ?  31  GLY   A CA    1 
ATOM   221  C C     . GLY   A 1 32  ? 6.177   -48.533 -3.931  1.00 35.28  ?  31  GLY   A C     1 
ATOM   222  O O     . GLY   A 1 32  ? 7.240   -47.926 -4.017  1.00 34.70  ?  31  GLY   A O     1 
ATOM   223  N N     . GLU   A 1 33  ? 4.969   -47.954 -4.047  1.00 37.01  ?  32  GLU   A N     1 
ATOM   224  C CA    . GLU   A 1 33  ? 4.768   -46.551 -4.368  1.00 38.68  ?  32  GLU   A CA    1 
ATOM   225  C C     . GLU   A 1 33  ? 3.809   -45.968 -3.335  1.00 37.50  ?  32  GLU   A C     1 
ATOM   226  O O     . GLU   A 1 33  ? 2.720   -46.503 -3.142  1.00 36.57  ?  32  GLU   A O     1 
ATOM   227  C CB    . GLU   A 1 33  ? 4.353   -46.330 -5.820  1.00 41.83  ?  32  GLU   A CB    1 
ATOM   228  C CG    . GLU   A 1 33  ? 2.974   -46.848 -6.254  1.00 46.01  ?  32  GLU   A CG    1 
ATOM   229  C CD    . GLU   A 1 33  ? 2.486   -46.464 -7.667  1.00 51.25  ?  32  GLU   A CD    1 
ATOM   230  O OE1   . GLU   A 1 33  ? 3.231   -45.737 -8.383  1.00 52.32  ?  32  GLU   A OE1   1 
ATOM   231  O OE2   . GLU   A 1 33  ? 1.365   -46.897 -8.089  1.00 55.10  -1 32  GLU   A OE2   1 
ATOM   232  N N     . TRP   A 1 34  ? 4.253   -44.898 -2.672  1.00 36.84  ?  33  TRP   A N     1 
ATOM   233  C CA    . TRP   A 1 34  ? 3.504   -44.164 -1.664  1.00 36.46  ?  33  TRP   A CA    1 
ATOM   234  C C     . TRP   A 1 34  ? 3.010   -42.863 -2.308  1.00 37.25  ?  33  TRP   A C     1 
ATOM   235  O O     . TRP   A 1 34  ? 3.842   -42.046 -2.716  1.00 37.41  ?  33  TRP   A O     1 
ATOM   236  C CB    . TRP   A 1 34  ? 4.471   -43.905 -0.507  1.00 35.51  ?  33  TRP   A CB    1 
ATOM   237  C CG    . TRP   A 1 34  ? 3.968   -43.124 0.670   1.00 36.00  ?  33  TRP   A CG    1 
ATOM   238  C CD1   . TRP   A 1 34  ? 3.894   -41.771 0.787   1.00 37.57  ?  33  TRP   A CD1   1 
ATOM   239  C CD2   . TRP   A 1 34  ? 3.588   -43.659 1.948   1.00 35.33  ?  33  TRP   A CD2   1 
ATOM   240  N NE1   . TRP   A 1 34  ? 3.468   -41.423 2.039   1.00 37.87  ?  33  TRP   A NE1   1 
ATOM   241  C CE2   . TRP   A 1 34  ? 3.270   -42.564 2.776   1.00 36.69  ?  33  TRP   A CE2   1 
ATOM   242  C CE3   . TRP   A 1 34  ? 3.477   -44.954 2.479   1.00 34.86  ?  33  TRP   A CE3   1 
ATOM   243  C CZ2   . TRP   A 1 34  ? 2.836   -42.741 4.097   1.00 36.10  ?  33  TRP   A CZ2   1 
ATOM   244  C CZ3   . TRP   A 1 34  ? 3.063   -45.133 3.785   1.00 33.25  ?  33  TRP   A CZ3   1 
ATOM   245  C CH2   . TRP   A 1 34  ? 2.746   -44.027 4.582   1.00 34.40  ?  33  TRP   A CH2   1 
ATOM   246  N N     . VAL   A 1 35  ? 1.683   -42.690 -2.405  1.00 36.89  ?  34  VAL   A N     1 
ATOM   247  C CA    . VAL   A 1 35  ? 1.076   -41.523 -3.034  1.00 38.90  ?  34  VAL   A CA    1 
ATOM   248  C C     . VAL   A 1 35  ? 0.322   -40.765 -1.937  1.00 38.91  ?  34  VAL   A C     1 
ATOM   249  O O     . VAL   A 1 35  ? -0.545  -41.353 -1.322  1.00 37.11  ?  34  VAL   A O     1 
ATOM   250  C CB    . VAL   A 1 35  ? 0.171   -41.907 -4.214  1.00 40.02  ?  34  VAL   A CB    1 
ATOM   251  C CG1   . VAL   A 1 35  ? -0.404  -40.690 -4.931  1.00 42.29  ?  34  VAL   A CG1   1 
ATOM   252  C CG2   . VAL   A 1 35  ? 0.884   -42.826 -5.202  1.00 40.00  ?  34  VAL   A CG2   1 
ATOM   253  N N     . LEU   A 1 36  ? 0.689   -39.497 -1.663  1.00 40.19  ?  35  LEU   A N     1 
ATOM   254  C CA    . LEU   A 1 36  ? -0.133  -38.575 -0.879  1.00 41.30  ?  35  LEU   A CA    1 
ATOM   255  C C     . LEU   A 1 36  ? -0.917  -37.669 -1.832  1.00 43.28  ?  35  LEU   A C     1 
ATOM   256  O O     . LEU   A 1 36  ? -0.328  -37.143 -2.763  1.00 43.34  ?  35  LEU   A O     1 
ATOM   257  C CB    . LEU   A 1 36  ? 0.658   -37.716 0.106   1.00 41.69  ?  35  LEU   A CB    1 
ATOM   258  C CG    . LEU   A 1 36  ? 1.321   -38.446 1.275   1.00 40.47  ?  35  LEU   A CG    1 
ATOM   259  C CD1   . LEU   A 1 36  ? 2.145   -37.464 2.065   1.00 41.16  ?  35  LEU   A CD1   1 
ATOM   260  C CD2   . LEU   A 1 36  ? 0.296   -39.078 2.182   1.00 39.93  ?  35  LEU   A CD2   1 
ATOM   261  N N     . LYS   A 1 37  ? -2.208  -37.470 -1.534  1.00 44.84  ?  36  LYS   A N     1 
ATOM   262  C CA    . LYS   A 1 37  ? -3.097  -36.543 -2.215  1.00 49.57  ?  36  LYS   A CA    1 
ATOM   263  C C     . LYS   A 1 37  ? -3.604  -35.506 -1.211  1.00 51.89  ?  36  LYS   A C     1 
ATOM   264  O O     . LYS   A 1 37  ? -3.771  -35.828 -0.028  1.00 50.80  ?  36  LYS   A O     1 
ATOM   265  C CB    . LYS   A 1 37  ? -4.267  -37.342 -2.796  1.00 50.05  ?  36  LYS   A CB    1 
ATOM   266  C CG    . LYS   A 1 37  ? -3.903  -38.189 -4.012  1.00 50.30  ?  36  LYS   A CG    1 
ATOM   267  C CD    . LYS   A 1 37  ? -5.145  -38.808 -4.654  1.00 51.22  ?  36  LYS   A CD    1 
ATOM   268  C CE    . LYS   A 1 37  ? -4.918  -39.998 -5.545  1.00 50.83  ?  36  LYS   A CE    1 
ATOM   269  N NZ    . LYS   A 1 37  ? -4.752  -39.650 -6.952  1.00 51.34  1  36  LYS   A NZ    1 
ATOM   270  N N     . GLY   A 1 38  ? -3.881  -34.290 -1.697  1.00 54.48  ?  37  GLY   A N     1 
ATOM   271  C CA    . GLY   A 1 38  ? -4.615  -33.287 -0.939  1.00 58.36  ?  37  GLY   A CA    1 
ATOM   272  C C     . GLY   A 1 38  ? -6.105  -33.610 -0.845  1.00 62.14  ?  37  GLY   A C     1 
ATOM   273  O O     . GLY   A 1 38  ? -6.558  -34.625 -1.373  1.00 63.59  ?  37  GLY   A O     1 
ATOM   274  N N     . SER   A 1 39  ? -6.865  -32.679 -0.247  1.00 68.93  ?  38  SER   A N     1 
ATOM   275  C CA    . SER   A 1 39  ? -8.330  -32.683 -0.211  1.00 73.89  ?  38  SER   A CA    1 
ATOM   276  C C     . SER   A 1 39  ? -8.988  -32.758 -1.595  1.00 75.50  ?  38  SER   A C     1 
ATOM   277  O O     . SER   A 1 39  ? -9.876  -33.585 -1.768  1.00 77.42  ?  38  SER   A O     1 
ATOM   278  C CB    . SER   A 1 39  ? -8.846  -31.494 0.570   1.00 76.88  ?  38  SER   A CB    1 
ATOM   279  O OG    . SER   A 1 39  ? -8.388  -31.607 1.911   1.00 77.67  ?  38  SER   A OG    1 
ATOM   280  N N     . SER   A 1 40  ? -8.551  -31.923 -2.556  1.00 77.85  ?  39  SER   A N     1 
ATOM   281  C CA    . SER   A 1 40  ? -8.948  -32.050 -3.961  1.00 79.24  ?  39  SER   A CA    1 
ATOM   282  C C     . SER   A 1 40  ? -8.380  -33.303 -4.641  1.00 81.04  ?  39  SER   A C     1 
ATOM   283  O O     . SER   A 1 40  ? -9.009  -33.801 -5.574  1.00 79.32  ?  39  SER   A O     1 
ATOM   284  C CB    . SER   A 1 40  ? -8.570  -30.829 -4.774  1.00 80.33  ?  39  SER   A CB    1 
ATOM   285  O OG    . SER   A 1 40  ? -7.160  -30.693 -4.904  1.00 76.71  ?  39  SER   A OG    1 
ATOM   286  N N     . GLY   A 1 41  ? -7.157  -33.729 -4.257  1.00 85.49  ?  40  GLY   A N     1 
ATOM   287  C CA    . GLY   A 1 41  ? -6.398  -34.766 -4.942  1.00 85.47  ?  40  GLY   A CA    1 
ATOM   288  C C     . GLY   A 1 41  ? -5.700  -34.276 -6.215  1.00 90.43  ?  40  GLY   A C     1 
ATOM   289  O O     . GLY   A 1 41  ? -5.234  -35.116 -6.993  1.00 96.51  ?  40  GLY   A O     1 
ATOM   290  N N     . GLU   A 1 42  ? -5.567  -32.940 -6.388  1.00 86.62  ?  41  GLU   A N     1 
ATOM   291  C CA    . GLU   A 1 42  ? -4.980  -32.299 -7.559  1.00 82.39  ?  41  GLU   A CA    1 
ATOM   292  C C     . GLU   A 1 42  ? -3.504  -31.954 -7.327  1.00 78.23  ?  41  GLU   A C     1 
ATOM   293  O O     . GLU   A 1 42  ? -2.819  -31.737 -8.319  1.00 76.94  ?  41  GLU   A O     1 
ATOM   294  C CB    . GLU   A 1 42  ? -5.746  -31.023 -7.925  1.00 86.70  ?  41  GLU   A CB    1 
ATOM   295  C CG    . GLU   A 1 42  ? -7.230  -31.218 -8.260  1.00 89.13  ?  41  GLU   A CG    1 
ATOM   296  C CD    . GLU   A 1 42  ? -7.633  -31.786 -9.614  1.00 89.77  ?  41  GLU   A CD    1 
ATOM   297  O OE1   . GLU   A 1 42  ? -6.788  -31.912 -10.531 1.00 89.95  ?  41  GLU   A OE1   1 
ATOM   298  O OE2   . GLU   A 1 42  ? -8.840  -32.110 -9.737  1.00 90.68  ?  41  GLU   A OE2   1 
ATOM   299  N N     . SER   A 1 43  ? -3.065  -31.789 -6.055  1.00 73.28  ?  42  SER   A N     1 
ATOM   300  C CA    . SER   A 1 43  ? -1.669  -31.880 -5.637  1.00 69.37  ?  42  SER   A CA    1 
ATOM   301  C C     . SER   A 1 43  ? -1.350  -33.293 -5.126  1.00 64.28  ?  42  SER   A C     1 
ATOM   302  O O     . SER   A 1 43  ? -1.957  -33.752 -4.155  1.00 61.46  ?  42  SER   A O     1 
ATOM   303  C CB    . SER   A 1 43  ? -1.350  -30.879 -4.575  1.00 70.27  ?  42  SER   A CB    1 
ATOM   304  O OG    . SER   A 1 43  ? -2.169  -31.075 -3.428  1.00 69.06  ?  42  SER   A OG    1 
ATOM   305  N N     . VAL   A 1 44  ? -0.376  -33.946 -5.779  1.00 60.64  ?  43  VAL   A N     1 
ATOM   306  C CA    . VAL   A 1 44  ? -0.094  -35.365 -5.655  1.00 57.03  ?  43  VAL   A CA    1 
ATOM   307  C C     . VAL   A 1 44  ? 1.421   -35.485 -5.448  1.00 55.59  ?  43  VAL   A C     1 
ATOM   308  O O     . VAL   A 1 44  ? 2.180   -34.826 -6.148  1.00 56.49  ?  43  VAL   A O     1 
ATOM   309  C CB    . VAL   A 1 44  ? -0.615  -36.170 -6.864  1.00 56.23  ?  43  VAL   A CB    1 
ATOM   310  C CG1   . VAL   A 1 44  ? -0.373  -37.669 -6.715  1.00 53.53  ?  43  VAL   A CG1   1 
ATOM   311  C CG2   . VAL   A 1 44  ? -2.103  -35.914 -7.112  1.00 58.20  ?  43  VAL   A CG2   1 
ATOM   312  N N     . ARG   A 1 45  ? 1.844   -36.281 -4.458  1.00 52.40  ?  44  ARG   A N     1 
ATOM   313  C CA    . ARG   A 1 45  ? 3.243   -36.567 -4.170  1.00 51.88  ?  44  ARG   A CA    1 
ATOM   314  C C     . ARG   A 1 45  ? 3.419   -38.082 -4.269  1.00 48.30  ?  44  ARG   A C     1 
ATOM   315  O O     . ARG   A 1 45  ? 2.795   -38.777 -3.478  1.00 46.10  ?  44  ARG   A O     1 
ATOM   316  C CB    . ARG   A 1 45  ? 3.610   -36.011 -2.785  1.00 53.88  ?  44  ARG   A CB    1 
ATOM   317  C CG    . ARG   A 1 45  ? 4.407   -34.708 -2.797  1.00 57.87  ?  44  ARG   A CG    1 
ATOM   318  C CD    . ARG   A 1 45  ? 5.925   -34.948 -2.988  1.00 60.59  ?  44  ARG   A CD    1 
ATOM   319  N NE    . ARG   A 1 45  ? 6.842   -34.760 -1.855  1.00 62.22  ?  44  ARG   A NE    1 
ATOM   320  C CZ    . ARG   A 1 45  ? 6.776   -35.312 -0.628  1.00 65.99  ?  44  ARG   A CZ    1 
ATOM   321  N NH1   . ARG   A 1 45  ? 5.764   -36.105 -0.288  1.00 64.68  1  44  ARG   A NH1   1 
ATOM   322  N NH2   . ARG   A 1 45  ? 7.724   -35.064 0.271   1.00 67.90  ?  44  ARG   A NH2   1 
ATOM   323  N N     . ARG   A 1 46  ? 4.188   -38.564 -5.268  1.00 47.28  ?  45  ARG   A N     1 
ATOM   324  C CA    . ARG   A 1 46  ? 4.515   -39.969 -5.457  1.00 45.63  ?  45  ARG   A CA    1 
ATOM   325  C C     . ARG   A 1 46  ? 5.959   -40.203 -5.010  1.00 44.22  ?  45  ARG   A C     1 
ATOM   326  O O     . ARG   A 1 46  ? 6.859   -39.490 -5.448  1.00 45.21  ?  45  ARG   A O     1 
ATOM   327  C CB    . ARG   A 1 46  ? 4.363   -40.405 -6.909  1.00 47.72  ?  45  ARG   A CB    1 
ATOM   328  C CG    . ARG   A 1 46  ? 2.966   -40.229 -7.489  1.00 50.23  ?  45  ARG   A CG    1 
ATOM   329  C CD    . ARG   A 1 46  ? 2.856   -40.674 -8.949  1.00 52.38  ?  45  ARG   A CD    1 
ATOM   330  N NE    . ARG   A 1 46  ? 1.669   -40.089 -9.598  1.00 55.57  ?  45  ARG   A NE    1 
ATOM   331  C CZ    . ARG   A 1 46  ? 0.387   -40.506 -9.505  1.00 57.69  ?  45  ARG   A CZ    1 
ATOM   332  N NH1   . ARG   A 1 46  ? 0.074   -41.627 -8.850  1.00 57.00  ?  45  ARG   A NH1   1 
ATOM   333  N NH2   . ARG   A 1 46  ? -0.587  -39.816 -10.101 1.00 59.37  ?  45  ARG   A NH2   1 
ATOM   334  N N     . THR   A 1 47  ? 6.163   -41.194 -4.131  1.00 41.45  ?  46  THR   A N     1 
ATOM   335  C CA    . THR   A 1 47  ? 7.477   -41.600 -3.657  1.00 40.59  ?  46  THR   A CA    1 
ATOM   336  C C     . THR   A 1 47  ? 7.646   -43.105 -3.913  1.00 39.08  ?  46  THR   A C     1 
ATOM   337  O O     . THR   A 1 47  ? 6.848   -43.889 -3.426  1.00 36.92  ?  46  THR   A O     1 
ATOM   338  C CB    . THR   A 1 47  ? 7.564   -41.219 -2.182  1.00 40.50  ?  46  THR   A CB    1 
ATOM   339  O OG1   . THR   A 1 47  ? 7.200   -39.842 -2.028  1.00 42.69  ?  46  THR   A OG1   1 
ATOM   340  C CG2   . THR   A 1 47  ? 8.967   -41.422 -1.631  1.00 40.42  ?  46  THR   A CG2   1 
ATOM   341  N N     . ASP   A 1 48  ? 8.656   -43.501 -4.714  1.00 40.33  ?  47  ASP   A N     1 
ATOM   342  C CA    . ASP   A 1 48  ? 9.100   -44.887 -4.845  1.00 40.69  ?  47  ASP   A CA    1 
ATOM   343  C C     . ASP   A 1 48  ? 9.798   -45.308 -3.559  1.00 38.39  ?  47  ASP   A C     1 
ATOM   344  O O     . ASP   A 1 48  ? 10.574  -44.518 -3.036  1.00 38.76  ?  47  ASP   A O     1 
ATOM   345  C CB    . ASP   A 1 48  ? 9.982   -45.136 -6.063  1.00 42.86  ?  47  ASP   A CB    1 
ATOM   346  C CG    . ASP   A 1 48  ? 9.280   -44.940 -7.401  1.00 46.70  ?  47  ASP   A CG    1 
ATOM   347  O OD1   . ASP   A 1 48  ? 8.123   -45.385 -7.524  1.00 48.66  ?  47  ASP   A OD1   1 
ATOM   348  O OD2   . ASP   A 1 48  ? 9.874   -44.341 -8.327  1.00 51.31  -1 47  ASP   A OD2   1 
ATOM   349  N N     . VAL   A 1 49  ? 9.441   -46.509 -3.064  1.00 35.79  ?  48  VAL   A N     1 
ATOM   350  C CA    . VAL   A 1 49  ? 9.851   -47.051 -1.777  1.00 33.95  ?  48  VAL   A CA    1 
ATOM   351  C C     . VAL   A 1 49  ? 10.557  -48.364 -2.065  1.00 32.87  ?  48  VAL   A C     1 
ATOM   352  O O     . VAL   A 1 49  ? 9.931   -49.231 -2.659  1.00 31.07  ?  48  VAL   A O     1 
ATOM   353  C CB    . VAL   A 1 49  ? 8.656   -47.290 -0.837  1.00 32.23  ?  48  VAL   A CB    1 
ATOM   354  C CG1   . VAL   A 1 49  ? 9.010   -48.096 0.417   1.00 31.40  ?  48  VAL   A CG1   1 
ATOM   355  C CG2   . VAL   A 1 49  ? 8.026   -45.955 -0.466  1.00 32.95  ?  48  VAL   A CG2   1 
ATOM   356  N N     . LYS   A 1 50  ? 11.803  -48.484 -1.598  1.00 33.49  ?  49  LYS   A N     1 
ATOM   357  C CA    . LYS   A 1 50  ? 12.535  -49.738 -1.577  1.00 35.52  ?  49  LYS   A CA    1 
ATOM   358  C C     . LYS   A 1 50  ? 13.061  -49.950 -0.153  1.00 31.72  ?  49  LYS   A C     1 
ATOM   359  O O     . LYS   A 1 50  ? 13.742  -49.050 0.340   1.00 30.76  ?  49  LYS   A O     1 
ATOM   360  C CB    . LYS   A 1 50  ? 13.604  -49.643 -2.670  1.00 43.30  ?  49  LYS   A CB    1 
ATOM   361  C CG    . LYS   A 1 50  ? 14.521  -50.870 -2.828  1.00 51.46  ?  49  LYS   A CG    1 
ATOM   362  C CD    . LYS   A 1 50  ? 14.003  -52.008 -3.709  1.00 58.24  ?  49  LYS   A CD    1 
ATOM   363  C CE    . LYS   A 1 50  ? 15.095  -52.826 -4.358  1.00 62.98  ?  49  LYS   A CE    1 
ATOM   364  N NZ    . LYS   A 1 50  ? 14.574  -53.622 -5.477  1.00 66.03  1  49  LYS   A NZ    1 
ATOM   365  N N     . VAL   A 1 51  ? 12.701  -51.100 0.477   1.00 29.07  ?  50  VAL   A N     1 
ATOM   366  C CA    . VAL   A 1 51  ? 13.143  -51.486 1.814   1.00 28.02  ?  50  VAL   A CA    1 
ATOM   367  C C     . VAL   A 1 51  ? 13.786  -52.870 1.714   1.00 28.40  ?  50  VAL   A C     1 
ATOM   368  O O     . VAL   A 1 51  ? 13.176  -53.774 1.119   1.00 27.63  ?  50  VAL   A O     1 
ATOM   369  C CB    . VAL   A 1 51  ? 12.060  -51.435 2.908   1.00 26.49  ?  50  VAL   A CB    1 
ATOM   370  C CG1   . VAL   A 1 51  ? 12.581  -51.882 4.277   1.00 26.40  ?  50  VAL   A CG1   1 
ATOM   371  C CG2   . VAL   A 1 51  ? 11.499  -50.020 3.029   1.00 27.45  ?  50  VAL   A CG2   1 
ATOM   372  N N     . ASP   A 1 52  ? 15.014  -53.025 2.270   1.00 28.30  ?  51  ASP   A N     1 
ATOM   373  C CA    . ASP   A 1 52  ? 15.709  -54.311 2.351   1.00 28.25  ?  51  ASP   A CA    1 
ATOM   374  C C     . ASP   A 1 52  ? 16.030  -54.613 3.798   1.00 26.19  ?  51  ASP   A C     1 
ATOM   375  O O     . ASP   A 1 52  ? 16.695  -53.812 4.441   1.00 26.10  ?  51  ASP   A O     1 
ATOM   376  C CB    . ASP   A 1 52  ? 16.963  -54.352 1.504   1.00 31.45  ?  51  ASP   A CB    1 
ATOM   377  C CG    . ASP   A 1 52  ? 16.623  -54.137 0.033   1.00 34.99  ?  51  ASP   A CG    1 
ATOM   378  O OD1   . ASP   A 1 52  ? 15.935  -54.995 -0.535  1.00 36.65  ?  51  ASP   A OD1   1 
ATOM   379  O OD2   . ASP   A 1 52  ? 16.895  -53.027 -0.472  1.00 42.99  ?  51  ASP   A OD2   1 
ATOM   380  N N     . ILE   A 1 53  ? 15.545  -55.760 4.291   1.00 24.28  ?  52  ILE   A N     1 
ATOM   381  C CA    . ILE   A 1 53  ? 15.732  -56.168 5.680   1.00 24.03  ?  52  ILE   A CA    1 
ATOM   382  C C     . ILE   A 1 53  ? 16.442  -57.529 5.679   1.00 23.41  ?  52  ILE   A C     1 
ATOM   383  O O     . ILE   A 1 53  ? 16.087  -58.415 4.909   1.00 23.90  ?  52  ILE   A O     1 
ATOM   384  C CB    . ILE   A 1 53  ? 14.404  -56.168 6.474   1.00 22.54  ?  52  ILE   A CB    1 
ATOM   385  C CG1   . ILE   A 1 53  ? 13.794  -54.788 6.536   1.00 22.92  ?  52  ILE   A CG1   1 
ATOM   386  C CG2   . ILE   A 1 53  ? 14.606  -56.692 7.892   1.00 22.08  ?  52  ILE   A CG2   1 
ATOM   387  C CD1   . ILE   A 1 53  ? 12.368  -54.736 7.055   1.00 22.67  ?  52  ILE   A CD1   1 
ATOM   388  N N     . THR   A 1 54  ? 17.455  -57.658 6.528   1.00 22.75  ?  53  THR   A N     1 
ATOM   389  C CA    . THR   A 1 54  ? 18.010  -58.922 6.962   1.00 21.95  ?  53  THR   A CA    1 
ATOM   390  C C     . THR   A 1 54  ? 17.960  -58.953 8.484   1.00 20.35  ?  53  THR   A C     1 
ATOM   391  O O     . THR   A 1 54  ? 18.333  -57.978 9.119   1.00 19.69  ?  53  THR   A O     1 
ATOM   392  C CB    . THR   A 1 54  ? 19.444  -59.041 6.481   1.00 22.94  ?  53  THR   A CB    1 
ATOM   393  O OG1   . THR   A 1 54  ? 19.354  -59.177 5.080   1.00 24.09  ?  53  THR   A OG1   1 
ATOM   394  C CG2   . THR   A 1 54  ? 20.126  -60.269 7.021   1.00 23.43  ?  53  THR   A CG2   1 
ATOM   395  N N     . SER   A 1 55  ? 17.556  -60.102 9.038   1.00 19.98  ?  54  SER   A N     1 
ATOM   396  C CA    . SER   A 1 55  ? 17.791  -60.464 10.438  1.00 19.52  ?  54  SER   A CA    1 
ATOM   397  C C     . SER   A 1 55  ? 18.225  -61.931 10.484  1.00 19.96  ?  54  SER   A C     1 
ATOM   398  O O     . SER   A 1 55  ? 17.434  -62.793 10.142  1.00 20.45  ?  54  SER   A O     1 
ATOM   399  C CB    . SER   A 1 55  ? 16.538  -60.187 11.230  1.00 18.65  ?  54  SER   A CB    1 
ATOM   400  O OG    . SER   A 1 55  ? 16.733  -60.396 12.617  1.00 17.89  ?  54  SER   A OG    1 
ATOM   401  N N     . THR   A 1 56  ? 19.470  -62.233 10.868  1.00 20.25  ?  55  THR   A N     1 
ATOM   402  C CA    . THR   A 1 56  ? 19.977  -63.598 10.885  1.00 21.41  ?  55  THR   A CA    1 
ATOM   403  C C     . THR   A 1 56  ? 19.378  -64.379 12.059  1.00 21.38  ?  55  THR   A C     1 
ATOM   404  O O     . THR   A 1 56  ? 18.470  -63.871 12.745  1.00 20.49  ?  55  THR   A O     1 
ATOM   405  C CB    . THR   A 1 56  ? 21.504  -63.609 10.830  1.00 21.98  ?  55  THR   A CB    1 
ATOM   406  O OG1   . THR   A 1 56  ? 21.904  -63.016 12.050  1.00 21.94  ?  55  THR   A OG1   1 
ATOM   407  C CG2   . THR   A 1 56  ? 22.010  -62.967 9.545   1.00 23.03  ?  55  THR   A CG2   1 
ATOM   408  N N     . ALA   A 1 57  ? 19.747  -65.676 12.157  1.00 22.21  ?  56  ALA   A N     1 
ATOM   409  C CA    . ALA   A 1 57  ? 19.119  -66.587 13.089  1.00 22.50  ?  56  ALA   A CA    1 
ATOM   410  C C     . ALA   A 1 57  ? 19.273  -66.018 14.490  1.00 22.30  ?  56  ALA   A C     1 
ATOM   411  O O     . ALA   A 1 57  ? 20.311  -65.436 14.817  1.00 20.53  ?  56  ALA   A O     1 
ATOM   412  C CB    . ALA   A 1 57  ? 19.629  -68.032 13.018  1.00 23.72  ?  56  ALA   A CB    1 
ATOM   413  N N     . GLY   A 1 58  ? 18.161  -66.091 15.236  1.00 22.60  ?  57  GLY   A N     1 
ATOM   414  C CA    . GLY   A 1 58  ? 18.061  -65.491 16.558  1.00 23.35  ?  57  GLY   A CA    1 
ATOM   415  C C     . GLY   A 1 58  ? 18.201  -63.972 16.586  1.00 23.79  ?  57  GLY   A C     1 
ATOM   416  O O     . GLY   A 1 58  ? 18.521  -63.463 17.656  1.00 25.22  ?  57  GLY   A O     1 
ATOM   417  N N     . ASN   A 1 59  ? 17.965  -63.278 15.449  1.00 21.77  ?  58  ASN   A N     1 
ATOM   418  C CA    . ASN   A 1 59  ? 18.179  -61.837 15.300  1.00 21.60  ?  58  ASN   A CA    1 
ATOM   419  C C     . ASN   A 1 59  ? 19.589  -61.352 15.675  1.00 21.26  ?  58  ASN   A C     1 
ATOM   420  O O     . ASN   A 1 59  ? 19.758  -60.271 16.247  1.00 20.40  ?  58  ASN   A O     1 
ATOM   421  C CB    . ASN   A 1 59  ? 17.182  -61.022 16.120  1.00 20.37  ?  58  ASN   A CB    1 
ATOM   422  C CG    . ASN   A 1 59  ? 15.769  -61.490 15.972  1.00 19.91  ?  58  ASN   A CG    1 
ATOM   423  O OD1   . ASN   A 1 59  ? 15.133  -61.928 16.960  1.00 19.92  ?  58  ASN   A OD1   1 
ATOM   424  N ND2   . ASN   A 1 59  ? 15.287  -61.377 14.755  1.00 19.12  ?  58  ASN   A ND2   1 
ATOM   425  N N     . GLN   A 1 60  ? 20.589  -62.164 15.402  1.00 22.69  ?  59  GLN   A N     1 
ATOM   426  C CA    . GLN   A 1 60  ? 21.941  -61.812 15.778  1.00 25.01  ?  59  GLN   A CA    1 
ATOM   427  C C     . GLN   A 1 60  ? 22.431  -60.611 14.973  1.00 25.21  ?  59  GLN   A C     1 
ATOM   428  O O     . GLN   A 1 60  ? 22.939  -59.687 15.589  1.00 26.39  ?  59  GLN   A O     1 
ATOM   429  C CB    . GLN   A 1 60  ? 22.875  -62.997 15.624  1.00 27.10  ?  59  GLN   A CB    1 
ATOM   430  C CG    . GLN   A 1 60  ? 24.254  -62.707 16.207  1.00 30.48  ?  59  GLN   A CG    1 
ATOM   431  C CD    . GLN   A 1 60  ? 25.301  -63.581 15.588  1.00 34.74  ?  59  GLN   A CD    1 
ATOM   432  O OE1   . GLN   A 1 60  ? 25.192  -64.804 15.681  1.00 42.67  ?  59  GLN   A OE1   1 
ATOM   433  N NE2   . GLN   A 1 60  ? 26.271  -62.984 14.926  1.00 38.92  ?  59  GLN   A NE2   1 
ATOM   434  N N     . ASP   A 1 61  ? 22.328  -60.675 13.636  1.00 26.33  ?  60  ASP   A N     1 
ATOM   435  C CA    . ASP   A 1 61  ? 22.791  -59.616 12.732  1.00 28.67  ?  60  ASP   A CA    1 
ATOM   436  C C     . ASP   A 1 61  ? 21.610  -59.020 11.962  1.00 25.24  ?  60  ASP   A C     1 
ATOM   437  O O     . ASP   A 1 61  ? 20.852  -59.769 11.361  1.00 24.19  ?  60  ASP   A O     1 
ATOM   438  C CB    . ASP   A 1 61  ? 23.819  -60.132 11.740  1.00 33.41  ?  60  ASP   A CB    1 
ATOM   439  C CG    . ASP   A 1 61  ? 25.239  -60.222 12.261  1.00 39.25  ?  60  ASP   A CG    1 
ATOM   440  O OD1   . ASP   A 1 61  ? 25.638  -59.292 12.972  1.00 41.66  ?  60  ASP   A OD1   1 
ATOM   441  O OD2   . ASP   A 1 61  ? 25.952  -61.206 11.911  1.00 51.94  -1 60  ASP   A OD2   1 
ATOM   442  N N     . ASN   A 1 62  ? 21.447  -57.693 12.057  1.00 23.66  ?  61  ASN   A N     1 
ATOM   443  C CA    . ASN   A 1 62  ? 20.229  -56.987 11.646  1.00 22.12  ?  61  ASN   A CA    1 
ATOM   444  C C     . ASN   A 1 62  ? 20.648  -55.842 10.730  1.00 22.35  ?  61  ASN   A C     1 
ATOM   445  O O     . ASN   A 1 62  ? 21.643  -55.178 11.013  1.00 22.04  ?  61  ASN   A O     1 
ATOM   446  C CB    . ASN   A 1 62  ? 19.397  -56.538 12.838  1.00 20.54  ?  61  ASN   A CB    1 
ATOM   447  C CG    . ASN   A 1 62  ? 19.201  -57.656 13.834  1.00 20.12  ?  61  ASN   A CG    1 
ATOM   448  O OD1   . ASN   A 1 62  ? 20.030  -57.844 14.734  1.00 20.71  ?  61  ASN   A OD1   1 
ATOM   449  N ND2   . ASN   A 1 62  ? 18.226  -58.507 13.596  1.00 18.91  ?  61  ASN   A ND2   1 
ATOM   450  N N     . SER   A 1 63  ? 19.930  -55.695 9.614   1.00 22.93  ?  62  SER   A N     1 
ATOM   451  C CA    . SER   A 1 63  ? 20.162  -54.663 8.620   1.00 24.29  ?  62  SER   A CA    1 
ATOM   452  C C     . SER   A 1 63  ? 18.810  -54.155 8.114   1.00 23.91  ?  62  SER   A C     1 
ATOM   453  O O     . SER   A 1 63  ? 17.968  -54.981 7.789   1.00 23.79  ?  62  SER   A O     1 
ATOM   454  C CB    . SER   A 1 63  ? 21.016  -55.205 7.525   1.00 25.48  ?  62  SER   A CB    1 
ATOM   455  O OG    . SER   A 1 63  ? 21.181  -54.228 6.519   1.00 26.97  ?  62  SER   A OG    1 
ATOM   456  N N     . PHE   A 1 64  ? 18.605  -52.825 8.075   1.00 24.33  ?  63  PHE   A N     1 
ATOM   457  C CA    . PHE   A 1 64  ? 17.425  -52.164 7.528   1.00 24.62  ?  63  PHE   A CA    1 
ATOM   458  C C     . PHE   A 1 64  ? 17.907  -51.063 6.583   1.00 25.94  ?  63  PHE   A C     1 
ATOM   459  O O     . PHE   A 1 64  ? 18.582  -50.156 7.041   1.00 27.27  ?  63  PHE   A O     1 
ATOM   460  C CB    . PHE   A 1 64  ? 16.554  -51.626 8.676   1.00 24.20  ?  63  PHE   A CB    1 
ATOM   461  C CG    . PHE   A 1 64  ? 15.273  -50.910 8.261   1.00 24.40  ?  63  PHE   A CG    1 
ATOM   462  C CD1   . PHE   A 1 64  ? 15.274  -49.600 7.773   1.00 26.36  ?  63  PHE   A CD1   1 
ATOM   463  C CD2   . PHE   A 1 64  ? 14.046  -51.556 8.360   1.00 25.05  ?  63  PHE   A CD2   1 
ATOM   464  C CE1   . PHE   A 1 64  ? 14.091  -48.952 7.397   1.00 26.55  ?  63  PHE   A CE1   1 
ATOM   465  C CE2   . PHE   A 1 64  ? 12.856  -50.917 7.973   1.00 24.67  ?  63  PHE   A CE2   1 
ATOM   466  C CZ    . PHE   A 1 64  ? 12.883  -49.628 7.487   1.00 25.81  ?  63  PHE   A CZ    1 
ATOM   467  N N     . ALA   A 1 65  ? 17.573  -51.158 5.289   1.00 26.91  ?  64  ALA   A N     1 
ATOM   468  C CA    . ALA   A 1 65  ? 17.969  -50.197 4.264   1.00 29.13  ?  64  ALA   A CA    1 
ATOM   469  C C     . ALA   A 1 65  ? 16.707  -49.673 3.628   1.00 30.07  ?  64  ALA   A C     1 
ATOM   470  O O     . ALA   A 1 65  ? 15.873  -50.499 3.269   1.00 31.02  ?  64  ALA   A O     1 
ATOM   471  C CB    . ALA   A 1 65  ? 18.822  -50.831 3.201   1.00 30.00  ?  64  ALA   A CB    1 
ATOM   472  N N     . ILE   A 1 66  ? 16.547  -48.346 3.548   1.00 31.69  ?  65  ILE   A N     1 
ATOM   473  C CA    . ILE   A 1 66  ? 15.385  -47.709 2.924   1.00 31.95  ?  65  ILE   A CA    1 
ATOM   474  C C     . ILE   A 1 66  ? 15.868  -46.696 1.876   1.00 32.64  ?  65  ILE   A C     1 
ATOM   475  O O     . ILE   A 1 66  ? 16.693  -45.867 2.198   1.00 32.89  ?  65  ILE   A O     1 
ATOM   476  C CB    . ILE   A 1 66  ? 14.443  -47.116 3.988   1.00 30.94  ?  65  ILE   A CB    1 
ATOM   477  C CG1   . ILE   A 1 66  ? 13.206  -46.478 3.359   1.00 31.12  ?  65  ILE   A CG1   1 
ATOM   478  C CG2   . ILE   A 1 66  ? 15.154  -46.157 4.943   1.00 31.91  ?  65  ILE   A CG2   1 
ATOM   479  C CD1   . ILE   A 1 66  ? 12.089  -46.203 4.343   1.00 30.75  ?  65  ILE   A CD1   1 
ATOM   480  N N     . GLN   A 1 67  ? 15.391  -46.801 0.635   1.00 33.59  ?  66  GLN   A N     1 
ATOM   481  C CA    . GLN   A 1 67  ? 15.629  -45.823 -0.427  1.00 36.43  ?  66  GLN   A CA    1 
ATOM   482  C C     . GLN   A 1 67  ? 14.283  -45.223 -0.844  1.00 35.49  ?  66  GLN   A C     1 
ATOM   483  O O     . GLN   A 1 67  ? 13.366  -45.977 -1.158  1.00 33.70  ?  66  GLN   A O     1 
ATOM   484  C CB    . GLN   A 1 67  ? 16.284  -46.474 -1.638  1.00 39.37  ?  66  GLN   A CB    1 
ATOM   485  C CG    . GLN   A 1 67  ? 17.667  -47.057 -1.379  1.00 43.58  ?  66  GLN   A CG    1 
ATOM   486  C CD    . GLN   A 1 67  ? 18.073  -47.972 -2.510  1.00 50.44  ?  66  GLN   A CD    1 
ATOM   487  O OE1   . GLN   A 1 67  ? 17.566  -49.098 -2.636  1.00 56.18  ?  66  GLN   A OE1   1 
ATOM   488  N NE2   . GLN   A 1 67  ? 18.908  -47.451 -3.393  1.00 53.18  ?  66  GLN   A NE2   1 
ATOM   489  N N     . LEU   A 1 68  ? 14.163  -43.884 -0.775  1.00 37.27  ?  67  LEU   A N     1 
ATOM   490  C CA    . LEU   A 1 68  ? 12.981  -43.120 -1.164  1.00 38.92  ?  67  LEU   A CA    1 
ATOM   491  C C     . LEU   A 1 68  ? 13.345  -42.212 -2.335  1.00 41.25  ?  67  LEU   A C     1 
ATOM   492  O O     . LEU   A 1 68  ? 14.361  -41.522 -2.261  1.00 43.05  ?  67  LEU   A O     1 
ATOM   493  C CB    . LEU   A 1 68  ? 12.480  -42.298 0.024   1.00 39.12  ?  67  LEU   A CB    1 
ATOM   494  C CG    . LEU   A 1 68  ? 12.135  -43.088 1.295   1.00 38.65  ?  67  LEU   A CG    1 
ATOM   495  C CD1   . LEU   A 1 68  ? 11.824  -42.147 2.447   1.00 39.86  ?  67  LEU   A CD1   1 
ATOM   496  C CD2   . LEU   A 1 68  ? 10.974  -44.022 1.034   1.00 37.90  ?  67  LEU   A CD2   1 
ATOM   497  N N     . ALA   A 1 69  ? 12.504  -42.190 -3.387  1.00 42.29  ?  68  ALA   A N     1 
ATOM   498  C CA    . ALA   A 1 69  ? 12.703  -41.377 -4.583  1.00 44.25  ?  68  ALA   A CA    1 
ATOM   499  C C     . ALA   A 1 69  ? 11.379  -40.700 -4.954  1.00 45.07  ?  68  ALA   A C     1 
ATOM   500  O O     . ALA   A 1 69  ? 10.396  -41.415 -5.134  1.00 41.61  ?  68  ALA   A O     1 
ATOM   501  C CB    . ALA   A 1 69  ? 13.183  -42.268 -5.716  1.00 44.29  ?  68  ALA   A CB    1 
ATOM   502  N N     . ASN   A 1 70  ? 11.357  -39.350 -5.035  1.00 48.01  ?  69  ASN   A N     1 
ATOM   503  C CA    . ASN   A 1 70  ? 10.456  -38.623 -5.940  1.00 51.07  ?  69  ASN   A CA    1 
ATOM   504  C C     . ASN   A 1 70  ? 11.161  -38.545 -7.303  1.00 52.35  ?  69  ASN   A C     1 
ATOM   505  O O     . ASN   A 1 70  ? 10.434  -38.416 -8.301  1.00 57.01  ?  69  ASN   A O     1 
ATOM   506  C CB    . ASN   A 1 70  ? 10.064  -37.203 -5.508  1.00 53.25  ?  69  ASN   A CB    1 
ATOM   507  C CG    . ASN   A 1 70  ? 10.028  -36.984 -4.013  1.00 52.80  ?  69  ASN   A CG    1 
ATOM   508  O OD1   . ASN   A 1 70  ? 10.876  -36.252 -3.489  1.00 53.22  ?  69  ASN   A OD1   1 
ATOM   509  N ND2   . ASN   A 1 70  ? 9.102   -37.619 -3.309  1.00 52.30  ?  69  ASN   A ND2   1 
ATOM   510  N N     . THR   A 1 78  ? 14.323  -35.030 -4.071  1.00 63.04  ?  77  THR   A N     1 
ATOM   511  C CA    . THR   A 1 78  ? 14.722  -36.001 -5.118  1.00 64.62  ?  77  THR   A CA    1 
ATOM   512  C C     . THR   A 1 78  ? 14.936  -37.392 -4.499  1.00 64.06  ?  77  THR   A C     1 
ATOM   513  O O     . THR   A 1 78  ? 14.077  -38.250 -4.689  1.00 63.27  ?  77  THR   A O     1 
ATOM   514  C CB    . THR   A 1 78  ? 15.937  -35.486 -5.904  1.00 68.53  ?  77  THR   A CB    1 
ATOM   515  O OG1   . THR   A 1 78  ? 16.786  -34.749 -5.023  1.00 71.93  ?  77  THR   A OG1   1 
ATOM   516  C CG2   . THR   A 1 78  ? 15.561  -34.585 -7.072  1.00 70.21  ?  77  THR   A CG2   1 
ATOM   517  N N     . LYS   A 1 79  ? 16.041  -37.590 -3.741  1.00 62.49  ?  78  LYS   A N     1 
ATOM   518  C CA    . LYS   A 1 79  ? 16.508  -38.896 -3.276  1.00 60.22  ?  78  LYS   A CA    1 
ATOM   519  C C     . LYS   A 1 79  ? 16.956  -38.817 -1.812  1.00 55.73  ?  78  LYS   A C     1 
ATOM   520  O O     . LYS   A 1 79  ? 17.535  -37.829 -1.362  1.00 56.16  ?  78  LYS   A O     1 
ATOM   521  C CB    . LYS   A 1 79  ? 17.693  -39.489 -4.052  1.00 63.70  ?  78  LYS   A CB    1 
ATOM   522  C CG    . LYS   A 1 79  ? 17.457  -39.814 -5.517  1.00 67.65  ?  78  LYS   A CG    1 
ATOM   523  C CD    . LYS   A 1 79  ? 18.679  -40.352 -6.271  1.00 70.19  ?  78  LYS   A CD    1 
ATOM   524  C CE    . LYS   A 1 79  ? 19.851  -39.401 -6.493  1.00 72.07  ?  78  LYS   A CE    1 
ATOM   525  N NZ    . LYS   A 1 79  ? 19.559  -38.128 -7.162  1.00 72.02  ?  78  LYS   A NZ    1 
ATOM   526  N N     . TRP   A 1 80  ? 16.709  -39.915 -1.100  1.00 51.92  ?  79  TRP   A N     1 
ATOM   527  C CA    . TRP   A 1 80  ? 16.871  -40.043 0.341   1.00 51.73  ?  79  TRP   A CA    1 
ATOM   528  C C     . TRP   A 1 80  ? 17.109  -41.533 0.606   1.00 48.38  ?  79  TRP   A C     1 
ATOM   529  O O     . TRP   A 1 80  ? 16.294  -42.355 0.168   1.00 45.06  ?  79  TRP   A O     1 
ATOM   530  C CB    . TRP   A 1 80  ? 15.599  -39.547 1.049   1.00 53.21  ?  79  TRP   A CB    1 
ATOM   531  C CG    . TRP   A 1 80  ? 15.752  -39.284 2.521   1.00 55.83  ?  79  TRP   A CG    1 
ATOM   532  C CD1   . TRP   A 1 80  ? 16.038  -38.061 3.040   1.00 60.42  ?  79  TRP   A CD1   1 
ATOM   533  C CD2   . TRP   A 1 80  ? 15.646  -40.190 3.649   1.00 55.15  ?  79  TRP   A CD2   1 
ATOM   534  N NE1   . TRP   A 1 80  ? 16.137  -38.131 4.402   1.00 60.12  ?  79  TRP   A NE1   1 
ATOM   535  C CE2   . TRP   A 1 80  ? 15.907  -39.418 4.810   1.00 56.40  ?  79  TRP   A CE2   1 
ATOM   536  C CE3   . TRP   A 1 80  ? 15.383  -41.566 3.807   1.00 52.67  ?  79  TRP   A CE3   1 
ATOM   537  C CZ2   . TRP   A 1 80  ? 15.899  -39.971 6.099   1.00 54.36  ?  79  TRP   A CZ2   1 
ATOM   538  C CZ3   . TRP   A 1 80  ? 15.403  -42.117 5.078   1.00 52.33  ?  79  TRP   A CZ3   1 
ATOM   539  C CH2   . TRP   A 1 80  ? 15.655  -41.328 6.210   1.00 51.11  ?  79  TRP   A CH2   1 
HETATM 540  N N     . CSD   A 1 81  ? 18.244  -41.885 1.232   1.00 45.65  ?  80  CSD   A N     1 
HETATM 541  C CA    . CSD   A 1 81  ? 18.524  -43.270 1.563   1.00 44.17  ?  80  CSD   A CA    1 
HETATM 542  C CB    . CSD   A 1 81  ? 19.370  -43.915 0.465   1.00 47.96  ?  80  CSD   A CB    1 
HETATM 543  S SG    . CSD   A 1 81  ? 21.171  -43.760 0.682   1.00 53.43  ?  80  CSD   A SG    1 
HETATM 544  C C     . CSD   A 1 81  ? 19.069  -43.360 2.992   1.00 41.06  ?  80  CSD   A C     1 
HETATM 545  O O     . CSD   A 1 81  ? 19.630  -42.376 3.515   1.00 39.64  ?  80  CSD   A O     1 
HETATM 546  O OD1   . CSD   A 1 81  ? 21.612  -44.689 1.793   1.00 48.32  ?  80  CSD   A OD1   1 
HETATM 547  O OD2   . CSD   A 1 81  ? 21.824  -44.210 -0.702  1.00 59.04  ?  80  CSD   A OD2   1 
ATOM   548  N N     . ALA   A 1 82  ? 18.831  -44.538 3.614   1.00 37.46  ?  81  ALA   A N     1 
ATOM   549  C CA    . ALA   A 1 82  ? 19.284  -44.843 4.961   1.00 35.66  ?  81  ALA   A CA    1 
ATOM   550  C C     . ALA   A 1 82  ? 19.703  -46.306 5.017   1.00 34.29  ?  81  ALA   A C     1 
ATOM   551  O O     . ALA   A 1 82  ? 18.984  -47.125 4.451   1.00 32.95  ?  81  ALA   A O     1 
ATOM   552  C CB    . ALA   A 1 82  ? 18.230  -44.515 6.002   1.00 35.17  ?  81  ALA   A CB    1 
ATOM   553  N N     . LEU   A 1 83  ? 20.863  -46.587 5.644   1.00 32.53  ?  82  LEU   A N     1 
ATOM   554  C CA    . LEU   A 1 83  ? 21.285  -47.915 6.025   1.00 31.73  ?  82  LEU   A CA    1 
ATOM   555  C C     . LEU   A 1 83  ? 21.431  -47.952 7.546   1.00 29.98  ?  82  LEU   A C     1 
ATOM   556  O O     . LEU   A 1 83  ? 22.248  -47.202 8.071   1.00 30.32  ?  82  LEU   A O     1 
ATOM   557  C CB    . LEU   A 1 83  ? 22.620  -48.237 5.337   1.00 33.81  ?  82  LEU   A CB    1 
ATOM   558  C CG    . LEU   A 1 83  ? 23.206  -49.620 5.660   1.00 33.42  ?  82  LEU   A CG    1 
ATOM   559  C CD1   . LEU   A 1 83  ? 22.215  -50.755 5.392   1.00 32.68  ?  82  LEU   A CD1   1 
ATOM   560  C CD2   . LEU   A 1 83  ? 24.441  -49.833 4.874   1.00 35.94  ?  82  LEU   A CD2   1 
ATOM   561  N N     . LEU   A 1 84  ? 20.689  -48.846 8.224   1.00 27.91  ?  83  LEU   A N     1 
ATOM   562  C CA    . LEU   A 1 84  ? 20.754  -49.048 9.673   1.00 26.99  ?  83  LEU   A CA    1 
ATOM   563  C C     . LEU   A 1 84  ? 21.180  -50.498 9.926   1.00 24.94  ?  83  LEU   A C     1 
ATOM   564  O O     . LEU   A 1 84  ? 20.586  -51.372 9.339   1.00 23.97  ?  83  LEU   A O     1 
ATOM   565  C CB    . LEU   A 1 84  ? 19.412  -48.737 10.340  1.00 26.16  ?  83  LEU   A CB    1 
ATOM   566  C CG    . LEU   A 1 84  ? 18.575  -47.572 9.812   1.00 26.95  ?  83  LEU   A CG    1 
ATOM   567  C CD1   . LEU   A 1 84  ? 17.262  -47.573 10.570  1.00 25.88  ?  83  LEU   A CD1   1 
ATOM   568  C CD2   . LEU   A 1 84  ? 19.244  -46.229 9.959   1.00 28.59  ?  83  LEU   A CD2   1 
ATOM   569  N N     . THR   A 1 85  ? 22.211  -50.750 10.752  1.00 25.09  ?  84  THR   A N     1 
ATOM   570  C CA    . THR   A 1 85  ? 22.689  -52.096 11.080  1.00 24.06  ?  84  THR   A CA    1 
ATOM   571  C C     . THR   A 1 85  ? 22.826  -52.253 12.600  1.00 23.59  ?  84  THR   A C     1 
ATOM   572  O O     . THR   A 1 85  ? 23.193  -51.296 13.257  1.00 22.88  ?  84  THR   A O     1 
ATOM   573  C CB    . THR   A 1 85  ? 24.023  -52.413 10.406  1.00 24.72  ?  84  THR   A CB    1 
ATOM   574  O OG1   . THR   A 1 85  ? 24.985  -51.513 10.940  1.00 25.08  ?  84  THR   A OG1   1 
ATOM   575  C CG2   . THR   A 1 85  ? 23.942  -52.368 8.898   1.00 25.43  ?  84  THR   A CG2   1 
ATOM   576  N N     . LYS   A 1 86  ? 22.566  -53.466 13.123  1.00 24.35  ?  85  LYS   A N     1 
ATOM   577  C CA    . LYS   A 1 86  ? 22.651  -53.767 14.554  1.00 24.76  ?  85  LYS   A CA    1 
ATOM   578  C C     . LYS   A 1 86  ? 23.134  -55.209 14.738  1.00 25.20  ?  85  LYS   A C     1 
ATOM   579  O O     . LYS   A 1 86  ? 22.465  -56.153 14.290  1.00 25.25  ?  85  LYS   A O     1 
ATOM   580  C CB    . LYS   A 1 86  ? 21.316  -53.500 15.237  1.00 24.37  ?  85  LYS   A CB    1 
ATOM   581  C CG    . LYS   A 1 86  ? 21.311  -53.678 16.758  1.00 24.85  ?  85  LYS   A CG    1 
ATOM   582  C CD    . LYS   A 1 86  ? 19.994  -53.381 17.497  1.00 24.85  ?  85  LYS   A CD    1 
ATOM   583  C CE    . LYS   A 1 86  ? 19.503  -52.002 17.507  1.00 25.63  ?  85  LYS   A CE    1 
ATOM   584  N NZ    . LYS   A 1 86  ? 20.471  -50.964 17.882  1.00 27.50  1  85  LYS   A NZ    1 
ATOM   585  N N     . LYS   A 1 87  ? 24.294  -55.349 15.376  1.00 26.38  ?  86  LYS   A N     1 
ATOM   586  C CA    . LYS   A 1 87  ? 25.017  -56.605 15.487  1.00 28.60  ?  86  LYS   A CA    1 
ATOM   587  C C     . LYS   A 1 87  ? 25.146  -56.953 16.967  1.00 26.64  ?  86  LYS   A C     1 
ATOM   588  O O     . LYS   A 1 87  ? 25.680  -56.152 17.719  1.00 24.77  ?  86  LYS   A O     1 
ATOM   589  C CB    . LYS   A 1 87  ? 26.397  -56.525 14.814  1.00 32.42  ?  86  LYS   A CB    1 
ATOM   590  C CG    . LYS   A 1 87  ? 26.240  -56.171 13.334  1.00 36.37  ?  86  LYS   A CG    1 
ATOM   591  C CD    . LYS   A 1 87  ? 27.333  -56.506 12.323  1.00 38.90  ?  86  LYS   A CD    1 
ATOM   592  C CE    . LYS   A 1 87  ? 26.999  -55.829 10.995  1.00 41.81  ?  86  LYS   A CE    1 
ATOM   593  N NZ    . LYS   A 1 87  ? 27.544  -56.583 9.861   1.00 45.78  1  86  LYS   A NZ    1 
ATOM   594  N N     . TYR   A 1 88  ? 24.623  -58.129 17.339  1.00 24.69  ?  87  TYR   A N     1 
ATOM   595  C CA    . TYR   A 1 88  ? 24.623  -58.603 18.716  1.00 24.16  ?  87  TYR   A CA    1 
ATOM   596  C C     . TYR   A 1 88  ? 25.735  -59.642 18.836  1.00 24.71  ?  87  TYR   A C     1 
ATOM   597  O O     . TYR   A 1 88  ? 26.176  -60.144 17.823  1.00 23.39  ?  87  TYR   A O     1 
ATOM   598  C CB    . TYR   A 1 88  ? 23.227  -59.157 19.007  1.00 22.34  ?  87  TYR   A CB    1 
ATOM   599  C CG    . TYR   A 1 88  ? 22.151  -58.107 19.268  1.00 22.26  ?  87  TYR   A CG    1 
ATOM   600  C CD1   . TYR   A 1 88  ? 22.064  -57.455 20.501  1.00 22.59  ?  87  TYR   A CD1   1 
ATOM   601  C CD2   . TYR   A 1 88  ? 21.214  -57.767 18.310  1.00 22.22  ?  87  TYR   A CD2   1 
ATOM   602  C CE1   . TYR   A 1 88  ? 21.072  -56.524 20.766  1.00 22.27  ?  87  TYR   A CE1   1 
ATOM   603  C CE2   . TYR   A 1 88  ? 20.200  -56.855 18.570  1.00 21.41  ?  87  TYR   A CE2   1 
ATOM   604  C CZ    . TYR   A 1 88  ? 20.114  -56.235 19.812  1.00 21.38  ?  87  TYR   A CZ    1 
ATOM   605  O OH    . TYR   A 1 88  ? 19.154  -55.312 20.118  1.00 19.31  ?  87  TYR   A OH    1 
ATOM   606  N N     . PRO   A 1 89  ? 26.131  -60.077 20.049  1.00 25.41  ?  88  PRO   A N     1 
ATOM   607  C CA    . PRO   A 1 89  ? 27.110  -61.152 20.173  1.00 27.16  ?  88  PRO   A CA    1 
ATOM   608  C C     . PRO   A 1 89  ? 26.522  -62.522 19.824  1.00 28.41  ?  88  PRO   A C     1 
ATOM   609  O O     . PRO   A 1 89  ? 25.297  -62.731 19.891  1.00 24.04  ?  88  PRO   A O     1 
ATOM   610  C CB    . PRO   A 1 89  ? 27.605  -61.023 21.601  1.00 28.24  ?  88  PRO   A CB    1 
ATOM   611  C CG    . PRO   A 1 89  ? 26.446  -60.411 22.332  1.00 26.09  ?  88  PRO   A CG    1 
ATOM   612  C CD    . PRO   A 1 89  ? 25.723  -59.525 21.344  1.00 24.90  ?  88  PRO   A CD    1 
ATOM   613  N N     . GLU   A 1 90  ? 27.430  -63.445 19.440  1.00 30.47  ?  89  GLU   A N     1 
ATOM   614  C CA    . GLU   A 1 90  ? 27.084  -64.837 19.172  1.00 32.44  ?  89  GLU   A CA    1 
ATOM   615  C C     . GLU   A 1 90  ? 26.637  -65.491 20.495  1.00 29.90  ?  89  GLU   A C     1 
ATOM   616  O O     . GLU   A 1 90  ? 27.217  -65.223 21.525  1.00 28.43  ?  89  GLU   A O     1 
ATOM   617  C CB    . GLU   A 1 90  ? 28.260  -65.528 18.469  1.00 37.43  ?  89  GLU   A CB    1 
ATOM   618  C CG    . GLU   A 1 90  ? 28.460  -65.033 17.035  1.00 41.75  ?  89  GLU   A CG    1 
ATOM   619  C CD    . GLU   A 1 90  ? 29.264  -65.898 16.079  1.00 48.74  ?  89  GLU   A CD    1 
ATOM   620  O OE1   . GLU   A 1 90  ? 29.111  -67.148 16.098  1.00 52.13  ?  89  GLU   A OE1   1 
ATOM   621  O OE2   . GLU   A 1 90  ? 30.042  -65.326 15.286  1.00 54.01  ?  89  GLU   A OE2   1 
ATOM   622  N N     . ARG   A 1 91  ? 25.572  -66.298 20.467  1.00 28.87  ?  90  ARG   A N     1 
ATOM   623  C CA    . ARG   A 1 91  ? 25.000  -66.899 21.667  1.00 27.65  ?  90  ARG   A CA    1 
ATOM   624  C C     . ARG   A 1 91  ? 25.805  -68.098 22.173  1.00 30.05  ?  90  ARG   A C     1 
ATOM   625  O O     . ARG   A 1 91  ? 26.777  -68.509 21.563  1.00 30.93  ?  90  ARG   A O     1 
ATOM   626  C CB    . ARG   A 1 91  ? 23.538  -67.248 21.408  1.00 24.96  ?  90  ARG   A CB    1 
ATOM   627  C CG    . ARG   A 1 91  ? 23.216  -68.395 20.462  1.00 24.44  ?  90  ARG   A CG    1 
ATOM   628  C CD    . ARG   A 1 91  ? 21.909  -69.119 20.732  1.00 23.84  ?  90  ARG   A CD    1 
ATOM   629  N NE    . ARG   A 1 91  ? 21.704  -69.441 22.162  1.00 23.72  ?  90  ARG   A NE    1 
ATOM   630  C CZ    . ARG   A 1 91  ? 20.649  -69.210 22.931  1.00 22.19  ?  90  ARG   A CZ    1 
ATOM   631  N NH1   . ARG   A 1 91  ? 19.584  -68.618 22.428  1.00 21.91  ?  90  ARG   A NH1   1 
ATOM   632  N NH2   . ARG   A 1 91  ? 20.608  -69.644 24.176  1.00 22.32  ?  90  ARG   A NH2   1 
ATOM   633  N N     . LYS   A 1 92  ? 25.427  -68.590 23.366  1.00 31.36  ?  91  LYS   A N     1 
ATOM   634  C CA    . LYS   A 1 92  ? 25.870  -69.864 23.939  1.00 32.30  ?  91  LYS   A CA    1 
ATOM   635  C C     . LYS   A 1 92  ? 24.613  -70.602 24.422  1.00 30.82  ?  91  LYS   A C     1 
ATOM   636  O O     . LYS   A 1 92  ? 23.511  -69.994 24.457  1.00 27.93  ?  91  LYS   A O     1 
ATOM   637  C CB    . LYS   A 1 92  ? 26.911  -69.642 25.044  1.00 36.06  ?  91  LYS   A CB    1 
ATOM   638  C CG    . LYS   A 1 92  ? 28.051  -68.711 24.627  1.00 39.65  ?  91  LYS   A CG    1 
ATOM   639  C CD    . LYS   A 1 92  ? 29.421  -68.952 25.236  1.00 45.15  ?  91  LYS   A CD    1 
ATOM   640  C CE    . LYS   A 1 92  ? 29.467  -68.736 26.691  1.00 47.42  ?  91  LYS   A CE    1 
ATOM   641  N NZ    . LYS   A 1 92  ? 30.870  -68.649 27.118  1.00 51.17  ?  91  LYS   A NZ    1 
ATOM   642  N N     . PRO   A 1 93  ? 24.685  -71.922 24.731  1.00 29.99  ?  92  PRO   A N     1 
ATOM   643  C CA    . PRO   A 1 93  ? 23.492  -72.677 25.146  1.00 28.61  ?  92  PRO   A CA    1 
ATOM   644  C C     . PRO   A 1 93  ? 22.684  -72.107 26.310  1.00 26.78  ?  92  PRO   A C     1 
ATOM   645  O O     . PRO   A 1 93  ? 21.451  -72.168 26.206  1.00 26.30  ?  92  PRO   A O     1 
ATOM   646  C CB    . PRO   A 1 93  ? 23.988  -74.087 25.450  1.00 29.89  ?  92  PRO   A CB    1 
ATOM   647  C CG    . PRO   A 1 93  ? 25.267  -74.189 24.583  1.00 30.80  ?  92  PRO   A CG    1 
ATOM   648  C CD    . PRO   A 1 93  ? 25.858  -72.810 24.538  1.00 30.67  ?  92  PRO   A CD    1 
ATOM   649  N N     . ASP   A 1 94  ? 23.340  -71.524 27.335  1.00 25.81  ?  93  ASP   A N     1 
ATOM   650  C CA    . ASP   A 1 94  ? 22.653  -70.972 28.508  1.00 25.13  ?  93  ASP   A CA    1 
ATOM   651  C C     . ASP   A 1 94  ? 22.408  -69.463 28.362  1.00 23.87  ?  93  ASP   A C     1 
ATOM   652  O O     . ASP   A 1 94  ? 23.290  -68.619 28.605  1.00 23.82  ?  93  ASP   A O     1 
ATOM   653  C CB    . ASP   A 1 94  ? 23.362  -71.326 29.819  1.00 27.54  ?  93  ASP   A CB    1 
ATOM   654  C CG    . ASP   A 1 94  ? 22.569  -71.035 31.092  1.00 27.29  ?  93  ASP   A CG    1 
ATOM   655  O OD1   . ASP   A 1 94  ? 21.390  -70.621 30.999  1.00 27.15  ?  93  ASP   A OD1   1 
ATOM   656  O OD2   . ASP   A 1 94  ? 23.097  -71.207 32.186  1.00 27.59  -1 93  ASP   A OD2   1 
ATOM   657  N N     . VAL   A 1 95  ? 21.163  -69.094 28.026  1.00 22.57  ?  94  VAL   A N     1 
ATOM   658  C CA    . VAL   A 1 95  ? 20.765  -67.690 27.989  1.00 22.13  ?  94  VAL   A CA    1 
ATOM   659  C C     . VAL   A 1 95  ? 20.848  -66.982 29.346  1.00 22.58  ?  94  VAL   A C     1 
ATOM   660  O O     . VAL   A 1 95  ? 21.132  -65.778 29.352  1.00 21.42  ?  94  VAL   A O     1 
ATOM   661  C CB    . VAL   A 1 95  ? 19.370  -67.545 27.353  1.00 22.24  ?  94  VAL   A CB    1 
ATOM   662  C CG1   . VAL   A 1 95  ? 18.272  -68.037 28.303  1.00 22.62  ?  94  VAL   A CG1   1 
ATOM   663  C CG2   . VAL   A 1 95  ? 19.099  -66.134 26.863  1.00 21.94  ?  94  VAL   A CG2   1 
ATOM   664  N N     . LEU   A 1 96  ? 20.636  -67.718 30.459  1.00 23.76  ?  95  LEU   A N     1 
ATOM   665  C CA    . LEU   A 1 96  ? 20.680  -67.136 31.800  1.00 24.71  ?  95  LEU   A CA    1 
ATOM   666  C C     . LEU   A 1 96  ? 22.089  -66.759 32.258  1.00 25.76  ?  95  LEU   A C     1 
ATOM   667  O O     . LEU   A 1 96  ? 22.172  -65.966 33.181  1.00 29.80  ?  95  LEU   A O     1 
ATOM   668  C CB    . LEU   A 1 96  ? 20.026  -68.053 32.835  1.00 25.25  ?  95  LEU   A CB    1 
ATOM   669  C CG    . LEU   A 1 96  ? 18.565  -68.429 32.586  1.00 24.87  ?  95  LEU   A CG    1 
ATOM   670  C CD1   . LEU   A 1 96  ? 18.007  -69.139 33.819  1.00 24.63  ?  95  LEU   A CD1   1 
ATOM   671  C CD2   . LEU   A 1 96  ? 17.681  -67.218 32.217  1.00 24.13  ?  95  LEU   A CD2   1 
ATOM   672  N N     . ALA   A 1 97  ? 23.162  -67.291 31.651  1.00 26.05  ?  96  ALA   A N     1 
ATOM   673  C CA    . ALA   A 1 97  ? 24.521  -67.083 32.156  1.00 27.20  ?  96  ALA   A CA    1 
ATOM   674  C C     . ALA   A 1 97  ? 25.194  -65.967 31.357  1.00 27.67  ?  96  ALA   A C     1 
ATOM   675  O O     . ALA   A 1 97  ? 25.154  -66.015 30.133  1.00 27.80  ?  96  ALA   A O     1 
ATOM   676  C CB    . ALA   A 1 97  ? 25.315  -68.381 32.065  1.00 27.59  ?  96  ALA   A CB    1 
ATOM   677  N N     . PHE   A 1 98  ? 25.896  -65.062 32.039  1.00 28.04  ?  97  PHE   A N     1 
ATOM   678  C CA    . PHE   A 1 98  ? 26.672  -64.007 31.413  1.00 29.00  ?  97  PHE   A CA    1 
ATOM   679  C C     . PHE   A 1 98  ? 27.815  -64.611 30.587  1.00 29.84  ?  97  PHE   A C     1 
ATOM   680  O O     . PHE   A 1 98  ? 28.335  -65.656 30.963  1.00 30.78  ?  97  PHE   A O     1 
ATOM   681  C CB    . PHE   A 1 98  ? 27.255  -63.058 32.476  1.00 30.38  ?  97  PHE   A CB    1 
ATOM   682  C CG    . PHE   A 1 98  ? 27.783  -61.740 31.927  1.00 31.91  ?  97  PHE   A CG    1 
ATOM   683  C CD1   . PHE   A 1 98  ? 26.896  -60.819 31.356  1.00 33.19  ?  97  PHE   A CD1   1 
ATOM   684  C CD2   . PHE   A 1 98  ? 29.134  -61.415 31.961  1.00 34.39  ?  97  PHE   A CD2   1 
ATOM   685  C CE1   . PHE   A 1 98  ? 27.359  -59.625 30.805  1.00 33.53  ?  97  PHE   A CE1   1 
ATOM   686  C CE2   . PHE   A 1 98  ? 29.594  -60.212 31.411  1.00 35.16  ?  97  PHE   A CE2   1 
ATOM   687  C CZ    . PHE   A 1 98  ? 28.689  -59.314 30.851  1.00 34.39  ?  97  PHE   A CZ    1 
ATOM   688  N N     . GLY   A 1 99  ? 28.214  -63.916 29.503  1.00 29.72  ?  98  GLY   A N     1 
ATOM   689  C CA    . GLY   A 1 99  ? 29.430  -64.202 28.730  1.00 29.72  ?  98  GLY   A CA    1 
ATOM   690  C C     . GLY   A 1 99  ? 29.154  -64.654 27.295  1.00 29.37  ?  98  GLY   A C     1 
ATOM   691  O O     . GLY   A 1 99  ? 29.966  -65.382 26.761  1.00 31.95  ?  98  GLY   A O     1 
ATOM   692  N N     . TRP   A 1 100 ? 28.034  -64.230 26.664  1.00 27.21  ?  99  TRP   A N     1 
ATOM   693  C CA    . TRP   A 1 100 ? 27.783  -64.401 25.245  1.00 25.99  ?  99  TRP   A CA    1 
ATOM   694  C C     . TRP   A 1 100 ? 28.700  -63.479 24.460  1.00 25.66  ?  99  TRP   A C     1 
ATOM   695  O O     . TRP   A 1 100 ? 28.511  -62.279 24.503  1.00 24.20  ?  99  TRP   A O     1 
ATOM   696  C CB    . TRP   A 1 100 ? 26.333  -64.048 24.888  1.00 24.53  ?  99  TRP   A CB    1 
ATOM   697  C CG    . TRP   A 1 100 ? 25.335  -65.092 25.243  1.00 24.80  ?  99  TRP   A CG    1 
ATOM   698  C CD1   . TRP   A 1 100 ? 25.437  -66.115 26.126  1.00 25.67  ?  99  TRP   A CD1   1 
ATOM   699  C CD2   . TRP   A 1 100 ? 24.034  -65.170 24.647  1.00 25.38  ?  99  TRP   A CD2   1 
ATOM   700  N NE1   . TRP   A 1 100 ? 24.285  -66.849 26.098  1.00 26.57  ?  99  TRP   A NE1   1 
ATOM   701  C CE2   . TRP   A 1 100 ? 23.409  -66.299 25.206  1.00 25.24  ?  99  TRP   A CE2   1 
ATOM   702  C CE3   . TRP   A 1 100 ? 23.354  -64.404 23.683  1.00 25.20  ?  99  TRP   A CE3   1 
ATOM   703  C CZ2   . TRP   A 1 100 ? 22.121  -66.668 24.850  1.00 25.51  ?  99  TRP   A CZ2   1 
ATOM   704  C CZ3   . TRP   A 1 100 ? 22.086  -64.796 23.308  1.00 25.64  ?  99  TRP   A CZ3   1 
ATOM   705  C CH2   . TRP   A 1 100 ? 21.461  -65.890 23.917  1.00 25.80  ?  99  TRP   A CH2   1 
ATOM   706  N N     . GLY   A 1 101 ? 29.693  -64.041 23.784  1.00 27.55  ?  100 GLY   A N     1 
ATOM   707  C CA    . GLY   A 1 101 ? 30.694  -63.264 23.052  1.00 28.98  ?  100 GLY   A CA    1 
ATOM   708  C C     . GLY   A 1 101 ? 31.341  -62.166 23.902  1.00 29.49  ?  100 GLY   A C     1 
ATOM   709  O O     . GLY   A 1 101 ? 31.668  -62.419 25.060  1.00 30.60  ?  100 GLY   A O     1 
ATOM   710  N N     . ASN   A 1 102 ? 31.366  -60.928 23.365  1.00 30.48  ?  101 ASN   A N     1 
ATOM   711  C CA    . ASN   A 1 102 ? 31.875  -59.745 24.058  1.00 30.90  ?  101 ASN   A CA    1 
ATOM   712  C C     . ASN   A 1 102 ? 30.776  -58.918 24.748  1.00 29.75  ?  101 ASN   A C     1 
ATOM   713  O O     . ASN   A 1 102 ? 31.069  -57.833 25.220  1.00 30.00  ?  101 ASN   A O     1 
ATOM   714  C CB    . ASN   A 1 102 ? 32.706  -58.933 23.067  1.00 32.14  ?  101 ASN   A CB    1 
ATOM   715  C CG    . ASN   A 1 102 ? 31.884  -58.232 22.004  1.00 31.03  ?  101 ASN   A CG    1 
ATOM   716  O OD1   . ASN   A 1 102 ? 30.685  -58.505 21.843  1.00 28.95  ?  101 ASN   A OD1   1 
ATOM   717  N ND2   . ASN   A 1 102 ? 32.517  -57.352 21.251  1.00 31.92  ?  101 ASN   A ND2   1 
ATOM   718  N N     . GLU   A 1 103 ? 29.515  -59.393 24.806  1.00 27.88  ?  102 GLU   A N     1 
ATOM   719  C CA    . GLU   A 1 103 ? 28.421  -58.772 25.556  1.00 25.88  ?  102 GLU   A CA    1 
ATOM   720  C C     . GLU   A 1 103 ? 28.206  -57.308 25.142  1.00 25.85  ?  102 GLU   A C     1 
ATOM   721  O O     . GLU   A 1 103 ? 27.982  -56.449 25.989  1.00 25.66  ?  102 GLU   A O     1 
ATOM   722  C CB    . GLU   A 1 103 ? 28.623  -59.054 27.057  1.00 25.99  ?  102 GLU   A CB    1 
ATOM   723  C CG    . GLU   A 1 103 ? 28.376  -60.505 27.456  1.00 25.23  ?  102 GLU   A CG    1 
ATOM   724  C CD    . GLU   A 1 103 ? 26.914  -60.918 27.464  1.00 24.55  ?  102 GLU   A CD    1 
ATOM   725  O OE1   . GLU   A 1 103 ? 26.020  -60.103 27.040  1.00 22.97  ?  102 GLU   A OE1   1 
ATOM   726  O OE2   . GLU   A 1 103 ? 26.696  -62.095 27.857  1.00 25.04  -1 102 GLU   A OE2   1 
ATOM   727  N N     . GLN   A 1 104 ? 28.324  -57.054 23.817  1.00 26.29  ?  103 GLN   A N     1 
ATOM   728  C CA    . GLN   A 1 104 ? 28.366  -55.737 23.217  1.00 25.92  ?  103 GLN   A CA    1 
ATOM   729  C C     . GLN   A 1 104 ? 27.430  -55.706 22.022  1.00 24.79  ?  103 GLN   A C     1 
ATOM   730  O O     . GLN   A 1 104 ? 27.405  -56.669 21.272  1.00 24.64  ?  103 GLN   A O     1 
ATOM   731  C CB    . GLN   A 1 104 ? 29.761  -55.474 22.690  1.00 27.24  ?  103 GLN   A CB    1 
ATOM   732  C CG    . GLN   A 1 104 ? 30.019  -54.037 22.283  1.00 27.99  ?  103 GLN   A CG    1 
ATOM   733  C CD    . GLN   A 1 104 ? 31.498  -53.765 22.132  1.00 29.08  ?  103 GLN   A CD    1 
ATOM   734  O OE1   . GLN   A 1 104 ? 32.253  -53.843 23.108  1.00 28.97  ?  103 GLN   A OE1   1 
ATOM   735  N NE2   . GLN   A 1 104 ? 31.892  -53.440 20.907  1.00 30.20  ?  103 GLN   A NE2   1 
ATOM   736  N N     . VAL   A 1 105 ? 26.753  -54.570 21.819  1.00 24.36  ?  104 VAL   A N     1 
ATOM   737  C CA    . VAL   A 1 105 ? 25.928  -54.344 20.645  1.00 23.89  ?  104 VAL   A CA    1 
ATOM   738  C C     . VAL   A 1 105 ? 26.605  -53.262 19.806  1.00 24.65  ?  104 VAL   A C     1 
ATOM   739  O O     . VAL   A 1 105 ? 26.954  -52.223 20.362  1.00 25.27  ?  104 VAL   A O     1 
ATOM   740  C CB    . VAL   A 1 105 ? 24.478  -53.967 21.024  1.00 22.08  ?  104 VAL   A CB    1 
ATOM   741  C CG1   . VAL   A 1 105 ? 23.591  -54.005 19.802  1.00 21.11  ?  104 VAL   A CG1   1 
ATOM   742  C CG2   . VAL   A 1 105 ? 23.948  -54.913 22.096  1.00 21.79  ?  104 VAL   A CG2   1 
ATOM   743  N N     . ASP   A 1 106 ? 26.784  -53.539 18.504  1.00 25.18  ?  105 ASP   A N     1 
ATOM   744  C CA    . ASP   A 1 106 ? 27.344  -52.611 17.536  1.00 27.37  ?  105 ASP   A CA    1 
ATOM   745  C C     . ASP   A 1 106 ? 26.277  -52.127 16.562  1.00 26.52  ?  105 ASP   A C     1 
ATOM   746  O O     . ASP   A 1 106 ? 25.794  -52.894 15.742  1.00 26.66  ?  105 ASP   A O     1 
ATOM   747  C CB    . ASP   A 1 106 ? 28.474  -53.284 16.769  1.00 30.04  ?  105 ASP   A CB    1 
ATOM   748  C CG    . ASP   A 1 106 ? 29.709  -53.616 17.596  1.00 31.98  ?  105 ASP   A CG    1 
ATOM   749  O OD1   . ASP   A 1 106 ? 29.895  -52.960 18.639  1.00 33.39  ?  105 ASP   A OD1   1 
ATOM   750  O OD2   . ASP   A 1 106 ? 30.428  -54.596 17.241  1.00 34.61  -1 105 ASP   A OD2   1 
ATOM   751  N N     . SER   A 1 107 ? 26.011  -50.820 16.561  1.00 26.62  ?  106 SER   A N     1 
ATOM   752  C CA    . SER   A 1 107 ? 25.031  -50.219 15.675  1.00 25.58  ?  106 SER   A CA    1 
ATOM   753  C C     . SER   A 1 107 ? 25.679  -49.136 14.823  1.00 27.22  ?  106 SER   A C     1 
ATOM   754  O O     . SER   A 1 107 ? 26.588  -48.434 15.283  1.00 27.60  ?  106 SER   A O     1 
ATOM   755  C CB    . SER   A 1 107 ? 23.882  -49.690 16.450  1.00 24.43  ?  106 SER   A CB    1 
ATOM   756  O OG    . SER   A 1 107 ? 23.256  -50.728 17.193  1.00 22.83  ?  106 SER   A OG    1 
ATOM   757  N N     . LYS   A 1 108 ? 25.159  -49.021 13.586  1.00 27.69  ?  107 LYS   A N     1 
ATOM   758  C CA    . LYS   A 1 108 ? 25.539  -47.983 12.637  1.00 30.54  ?  107 LYS   A CA    1 
ATOM   759  C C     . LYS   A 1 108 ? 24.281  -47.486 11.916  1.00 30.35  ?  107 LYS   A C     1 
ATOM   760  O O     . LYS   A 1 108 ? 23.417  -48.319 11.575  1.00 27.98  ?  107 LYS   A O     1 
ATOM   761  C CB    . LYS   A 1 108 ? 26.550  -48.563 11.646  1.00 32.14  ?  107 LYS   A CB    1 
ATOM   762  C CG    . LYS   A 1 108 ? 27.317  -47.493 10.846  1.00 36.49  ?  107 LYS   A CG    1 
ATOM   763  C CD    . LYS   A 1 108 ? 28.340  -48.091 9.882   1.00 37.96  ?  107 LYS   A CD    1 
ATOM   764  C CE    . LYS   A 1 108 ? 28.917  -47.137 8.899   1.00 41.35  ?  107 LYS   A CE    1 
ATOM   765  N NZ    . LYS   A 1 108 ? 30.247  -47.575 8.422   1.00 43.45  1  107 LYS   A NZ    1 
ATOM   766  N N     . ALA   A 1 109 ? 24.193  -46.157 11.714  1.00 32.07  ?  108 ALA   A N     1 
ATOM   767  C CA    . ALA   A 1 109 ? 23.148  -45.514 10.914  1.00 33.09  ?  108 ALA   A CA    1 
ATOM   768  C C     . ALA   A 1 109 ? 23.800  -44.516 9.953   1.00 36.39  ?  108 ALA   A C     1 
ATOM   769  O O     . ALA   A 1 109 ? 24.586  -43.698 10.406  1.00 37.61  ?  108 ALA   A O     1 
ATOM   770  C CB    . ALA   A 1 109 ? 22.116  -44.823 11.778  1.00 32.13  ?  108 ALA   A CB    1 
ATOM   771  N N     . SER   A 1 110 ? 23.481  -44.607 8.649   1.00 37.74  ?  109 SER   A N     1 
ATOM   772  C CA    . SER   A 1 110 ? 23.947  -43.693 7.610   1.00 41.00  ?  109 SER   A CA    1 
ATOM   773  C C     . SER   A 1 110 ? 22.739  -43.157 6.845   1.00 40.14  ?  109 SER   A C     1 
ATOM   774  O O     . SER   A 1 110 ? 21.908  -43.974 6.459   1.00 37.66  ?  109 SER   A O     1 
ATOM   775  C CB    . SER   A 1 110 ? 24.877  -44.405 6.675   1.00 43.25  ?  109 SER   A CB    1 
ATOM   776  O OG    . SER   A 1 110 ? 26.012  -44.914 7.361   1.00 46.35  ?  109 SER   A OG    1 
ATOM   777  N N     . VAL   A 1 111 ? 22.638  -41.825 6.664   1.00 41.44  ?  110 VAL   A N     1 
ATOM   778  C CA    . VAL   A 1 111 ? 21.571  -41.189 5.887   1.00 42.14  ?  110 VAL   A CA    1 
ATOM   779  C C     . VAL   A 1 111 ? 22.233  -40.296 4.836   1.00 44.98  ?  110 VAL   A C     1 
ATOM   780  O O     . VAL   A 1 111 ? 23.093  -39.503 5.183   1.00 44.69  ?  110 VAL   A O     1 
ATOM   781  C CB    . VAL   A 1 111 ? 20.508  -40.435 6.706   1.00 41.23  ?  110 VAL   A CB    1 
ATOM   782  C CG1   . VAL   A 1 111 ? 21.096  -39.462 7.702   1.00 42.98  ?  110 VAL   A CG1   1 
ATOM   783  C CG2   . VAL   A 1 111 ? 19.479  -39.717 5.848   1.00 42.74  ?  110 VAL   A CG2   1 
ATOM   784  N N     . THR   A 1 112 ? 21.869  -40.489 3.554   1.00 47.58  ?  111 THR   A N     1 
ATOM   785  C CA    . THR   A 1 112 ? 22.374  -39.707 2.431   1.00 51.01  ?  111 THR   A CA    1 
ATOM   786  C C     . THR   A 1 112 ? 21.161  -39.091 1.742   1.00 52.59  ?  111 THR   A C     1 
ATOM   787  O O     . THR   A 1 112 ? 20.222  -39.812 1.383   1.00 50.19  ?  111 THR   A O     1 
ATOM   788  C CB    . THR   A 1 112 ? 23.205  -40.545 1.465   1.00 51.60  ?  111 THR   A CB    1 
ATOM   789  O OG1   . THR   A 1 112 ? 24.296  -41.032 2.236   1.00 51.95  ?  111 THR   A OG1   1 
ATOM   790  C CG2   . THR   A 1 112 ? 23.774  -39.732 0.313   1.00 54.71  ?  111 THR   A CG2   1 
ATOM   791  N N     . ILE   A 1 113 ? 21.189  -37.756 1.618   1.00 54.97  ?  112 ILE   A N     1 
ATOM   792  C CA    . ILE   A 1 113 ? 20.208  -36.962 0.896   1.00 57.77  ?  112 ILE   A CA    1 
ATOM   793  C C     . ILE   A 1 113 ? 20.869  -36.516 -0.410  1.00 59.18  ?  112 ILE   A C     1 
ATOM   794  O O     . ILE   A 1 113 ? 22.091  -36.357 -0.454  1.00 58.80  ?  112 ILE   A O     1 
ATOM   795  C CB    . ILE   A 1 113 ? 19.736  -35.799 1.790   1.00 60.45  ?  112 ILE   A CB    1 
ATOM   796  C CG1   . ILE   A 1 113 ? 19.193  -36.328 3.173   1.00 58.51  ?  112 ILE   A CG1   1 
ATOM   797  C CG2   . ILE   A 1 113 ? 18.719  -34.912 1.061   1.00 62.13  ?  112 ILE   A CG2   1 
ATOM   798  C CD1   . ILE   A 1 113 ? 20.208  -36.299 4.304   1.00 58.24  ?  112 ILE   A CD1   1 
ATOM   799  N N     . GLY   A 1 114 ? 20.061  -36.393 -1.478  1.00 59.72  ?  113 GLY   A N     1 
ATOM   800  C CA    . GLY   A 1 114 ? 20.550  -36.089 -2.812  1.00 61.68  ?  113 GLY   A CA    1 
ATOM   801  C C     . GLY   A 1 114 ? 21.237  -37.298 -3.421  1.00 61.69  ?  113 GLY   A C     1 
ATOM   802  O O     . GLY   A 1 114 ? 21.692  -37.156 -4.581  1.00 64.15  ?  113 GLY   A O     1 
ATOM   803  N N     . SER   B 2 1   ? 25.889  -35.891 -2.837  1.00 78.73  ?  1   SER   B N     1 
ATOM   804  C CA    . SER   B 2 1   ? 25.455  -36.392 -1.509  1.00 75.23  ?  1   SER   B CA    1 
ATOM   805  C C     . SER   B 2 1   ? 25.693  -35.333 -0.428  1.00 73.16  ?  1   SER   B C     1 
ATOM   806  O O     . SER   B 2 1   ? 26.634  -34.548 -0.519  1.00 71.55  ?  1   SER   B O     1 
ATOM   807  C CB    . SER   B 2 1   ? 26.155  -37.705 -1.172  1.00 74.11  ?  1   SER   B CB    1 
ATOM   808  O OG    . SER   B 2 1   ? 25.692  -38.776 -1.996  1.00 73.84  ?  1   SER   B OG    1 
ATOM   809  N N     . VAL   B 2 2   ? 24.803  -35.298 0.577   1.00 72.60  ?  2   VAL   B N     1 
ATOM   810  C CA    . VAL   B 2 2   ? 25.141  -34.884 1.938   1.00 70.29  ?  2   VAL   B CA    1 
ATOM   811  C C     . VAL   B 2 2   ? 24.704  -36.018 2.879   1.00 66.45  ?  2   VAL   B C     1 
ATOM   812  O O     . VAL   B 2 2   ? 23.540  -36.426 2.936   1.00 65.09  ?  2   VAL   B O     1 
ATOM   813  C CB    . VAL   B 2 2   ? 24.617  -33.508 2.389   1.00 72.62  ?  2   VAL   B CB    1 
ATOM   814  C CG1   . VAL   B 2 2   ? 25.396  -32.388 1.689   1.00 74.81  ?  2   VAL   B CG1   1 
ATOM   815  C CG2   . VAL   B 2 2   ? 23.103  -33.348 2.210   1.00 74.22  ?  2   VAL   B CG2   1 
ATOM   816  N N     . THR   B 2 3   ? 25.694  -36.512 3.619   1.00 62.06  ?  3   THR   B N     1 
ATOM   817  C CA    . THR   B 2 3   ? 25.828  -37.907 3.990   1.00 60.08  ?  3   THR   B CA    1 
ATOM   818  C C     . THR   B 2 3   ? 26.345  -37.844 5.424   1.00 57.58  ?  3   THR   B C     1 
ATOM   819  O O     . THR   B 2 3   ? 27.406  -37.258 5.627   1.00 58.96  ?  3   THR   B O     1 
ATOM   820  C CB    . THR   B 2 3   ? 26.713  -38.658 2.976   1.00 62.09  ?  3   THR   B CB    1 
ATOM   821  O OG1   . THR   B 2 3   ? 27.230  -39.851 3.556   1.00 60.38  ?  3   THR   B OG1   1 
ATOM   822  C CG2   . THR   B 2 3   ? 27.894  -37.866 2.418   1.00 65.98  ?  3   THR   B CG2   1 
ATOM   823  N N     . ILE   B 2 4   ? 25.513  -38.237 6.408   1.00 53.79  ?  4   ILE   B N     1 
ATOM   824  C CA    . ILE   B 2 4   ? 25.890  -38.177 7.811   1.00 51.83  ?  4   ILE   B CA    1 
ATOM   825  C C     . ILE   B 2 4   ? 25.701  -39.549 8.447   1.00 46.81  ?  4   ILE   B C     1 
ATOM   826  O O     . ILE   B 2 4   ? 24.772  -40.270 8.112   1.00 46.12  ?  4   ILE   B O     1 
ATOM   827  C CB    . ILE   B 2 4   ? 25.193  -37.026 8.560   1.00 54.06  ?  4   ILE   B CB    1 
ATOM   828  C CG1   . ILE   B 2 4   ? 23.673  -37.091 8.503   1.00 54.33  ?  4   ILE   B CG1   1 
ATOM   829  C CG2   . ILE   B 2 4   ? 25.728  -35.679 8.060   1.00 56.74  ?  4   ILE   B CG2   1 
ATOM   830  C CD1   . ILE   B 2 4   ? 23.031  -37.023 9.873   1.00 53.00  ?  4   ILE   B CD1   1 
ATOM   831  N N     . THR   B 2 5   ? 26.638  -39.892 9.344   1.00 44.35  ?  5   THR   B N     1 
ATOM   832  C CA    . THR   B 2 5   ? 26.826  -41.226 9.889   1.00 42.71  ?  5   THR   B CA    1 
ATOM   833  C C     . THR   B 2 5   ? 26.852  -41.113 11.408  1.00 41.12  ?  5   THR   B C     1 
ATOM   834  O O     . THR   B 2 5   ? 27.435  -40.161 11.919  1.00 41.13  ?  5   THR   B O     1 
ATOM   835  C CB    . THR   B 2 5   ? 28.122  -41.830 9.349   1.00 42.94  ?  5   THR   B CB    1 
ATOM   836  O OG1   . THR   B 2 5   ? 27.798  -42.040 7.983   1.00 44.62  ?  5   THR   B OG1   1 
ATOM   837  C CG2   . THR   B 2 5   ? 28.458  -43.215 9.879   1.00 41.65  ?  5   THR   B CG2   1 
ATOM   838  N N     . ILE   B 2 6   ? 26.217  -42.085 12.090  1.00 40.39  ?  6   ILE   B N     1 
ATOM   839  C CA    . ILE   B 2 6   ? 26.289  -42.271 13.537  1.00 39.76  ?  6   ILE   B CA    1 
ATOM   840  C C     . ILE   B 2 6   ? 26.650  -43.737 13.795  1.00 38.46  ?  6   ILE   B C     1 
ATOM   841  O O     . ILE   B 2 6   ? 25.966  -44.629 13.308  1.00 39.03  ?  6   ILE   B O     1 
ATOM   842  C CB    . ILE   B 2 6   ? 24.969  -41.837 14.212  1.00 41.06  ?  6   ILE   B CB    1 
ATOM   843  C CG1   . ILE   B 2 6   ? 24.657  -40.345 13.924  1.00 42.11  ?  6   ILE   B CG1   1 
ATOM   844  C CG2   . ILE   B 2 6   ? 24.988  -42.157 15.723  1.00 41.08  ?  6   ILE   B CG2   1 
ATOM   845  C CD1   . ILE   B 2 6   ? 23.297  -39.838 14.367  1.00 43.21  ?  6   ILE   B CD1   1 
ATOM   846  N N     . ASN   B 2 7   ? 27.759  -43.981 14.509  1.00 39.15  ?  7   ASN   B N     1 
ATOM   847  C CA    . ASN   B 2 7   ? 28.084  -45.267 15.118  1.00 36.88  ?  7   ASN   B CA    1 
ATOM   848  C C     . ASN   B 2 7   ? 27.590  -45.275 16.556  1.00 34.12  ?  7   ASN   B C     1 
ATOM   849  O O     . ASN   B 2 7   ? 27.591  -44.245 17.227  1.00 33.78  ?  7   ASN   B O     1 
ATOM   850  C CB    . ASN   B 2 7   ? 29.583  -45.527 15.141  1.00 39.30  ?  7   ASN   B CB    1 
ATOM   851  C CG    . ASN   B 2 7   ? 30.133  -45.608 13.740  1.00 41.66  ?  7   ASN   B CG    1 
ATOM   852  O OD1   . ASN   B 2 7   ? 29.953  -46.631 13.072  1.00 44.22  ?  7   ASN   B OD1   1 
ATOM   853  N ND2   . ASN   B 2 7   ? 30.756  -44.545 13.261  1.00 43.43  ?  7   ASN   B ND2   1 
ATOM   854  N N     . GLN   B 2 8   ? 27.218  -46.470 17.013  1.00 32.23  ?  8   GLN   B N     1 
ATOM   855  C CA    . GLN   B 2 8   ? 26.742  -46.680 18.350  1.00 30.48  ?  8   GLN   B CA    1 
ATOM   856  C C     . GLN   B 2 8   ? 27.290  -48.007 18.852  1.00 29.16  ?  8   GLN   B C     1 
ATOM   857  O O     . GLN   B 2 8   ? 27.162  -49.041 18.196  1.00 27.59  ?  8   GLN   B O     1 
ATOM   858  C CB    . GLN   B 2 8   ? 25.216  -46.542 18.305  1.00 30.05  ?  8   GLN   B CB    1 
ATOM   859  C CG    . GLN   B 2 8   ? 24.495  -46.815 19.626  1.00 28.69  ?  8   GLN   B CG    1 
ATOM   860  C CD    . GLN   B 2 8   ? 22.992  -46.935 19.456  1.00 29.16  ?  8   GLN   B CD    1 
ATOM   861  O OE1   . GLN   B 2 8   ? 22.357  -46.191 18.694  1.00 30.53  ?  8   GLN   B OE1   1 
ATOM   862  N NE2   . GLN   B 2 8   ? 22.402  -47.895 20.145  1.00 28.08  ?  8   GLN   B NE2   1 
ATOM   863  N N     . LYS   B 2 9   ? 27.755  -47.968 20.098  1.00 29.34  ?  9   LYS   B N     1 
ATOM   864  C CA    . LYS   B 2 9   ? 28.175  -49.127 20.865  1.00 28.87  ?  9   LYS   B CA    1 
ATOM   865  C C     . LYS   B 2 9   ? 27.255  -49.180 22.083  1.00 28.28  ?  9   LYS   B C     1 
ATOM   866  O O     . LYS   B 2 9   ? 27.155  -48.175 22.770  1.00 28.05  ?  9   LYS   B O     1 
ATOM   867  C CB    . LYS   B 2 9   ? 29.658  -48.920 21.197  1.00 30.16  ?  9   LYS   B CB    1 
ATOM   868  C CG    . LYS   B 2 9   ? 30.253  -49.871 22.206  1.00 31.12  ?  9   LYS   B CG    1 
ATOM   869  C CD    . LYS   B 2 9   ? 31.786  -49.925 22.240  1.00 32.87  ?  9   LYS   B CD    1 
ATOM   870  C CE    . LYS   B 2 9   ? 32.372  -48.783 22.973  1.00 35.06  ?  9   LYS   B CE    1 
ATOM   871  N NZ    . LYS   B 2 9   ? 33.817  -48.622 22.754  1.00 37.15  1  9   LYS   B NZ    1 
ATOM   872  N N     . GLY   B 2 10  ? 26.615  -50.331 22.332  1.00 27.81  ?  10  GLY   B N     1 
ATOM   873  C CA    . GLY   B 2 10  ? 25.864  -50.624 23.545  1.00 27.41  ?  10  GLY   B CA    1 
ATOM   874  C C     . GLY   B 2 10  ? 26.660  -51.607 24.401  1.00 27.19  ?  10  GLY   B C     1 
ATOM   875  O O     . GLY   B 2 10  ? 27.082  -52.649 23.878  1.00 27.08  ?  10  GLY   B O     1 
ATOM   876  N N     . GLU   B 2 11  ? 26.820  -51.290 25.700  1.00 26.96  ?  11  GLU   B N     1 
ATOM   877  C CA    . GLU   B 2 11  ? 27.513  -52.125 26.663  1.00 27.67  ?  11  GLU   B CA    1 
ATOM   878  C C     . GLU   B 2 11  ? 26.714  -52.282 27.959  1.00 27.79  ?  11  GLU   B C     1 
ATOM   879  O O     . GLU   B 2 11  ? 25.815  -51.509 28.220  1.00 27.60  ?  11  GLU   B O     1 
ATOM   880  C CB    . GLU   B 2 11  ? 28.863  -51.466 26.964  1.00 28.80  ?  11  GLU   B CB    1 
ATOM   881  C CG    . GLU   B 2 11  ? 29.763  -51.421 25.736  1.00 29.66  ?  11  GLU   B CG    1 
ATOM   882  C CD    . GLU   B 2 11  ? 31.122  -50.887 26.139  1.00 31.15  ?  11  GLU   B CD    1 
ATOM   883  O OE1   . GLU   B 2 11  ? 31.224  -49.677 26.305  1.00 32.65  ?  11  GLU   B OE1   1 
ATOM   884  O OE2   . GLU   B 2 11  ? 31.963  -51.695 26.495  1.00 31.78  -1 11  GLU   B OE2   1 
ATOM   885  N N     . ILE   B 2 12  ? 27.129  -53.264 28.779  1.00 29.60  ?  12  ILE   B N     1 
ATOM   886  C CA    . ILE   B 2 12  ? 26.645  -53.510 30.126  1.00 30.92  ?  12  ILE   B CA    1 
ATOM   887  C C     . ILE   B 2 12  ? 27.487  -52.639 31.064  1.00 32.24  ?  12  ILE   B C     1 
ATOM   888  O O     . ILE   B 2 12  ? 28.717  -52.665 30.977  1.00 33.56  ?  12  ILE   B O     1 
ATOM   889  C CB    . ILE   B 2 12  ? 26.781  -55.000 30.500  1.00 31.50  ?  12  ILE   B CB    1 
ATOM   890  C CG1   . ILE   B 2 12  ? 26.218  -55.956 29.424  1.00 31.97  ?  12  ILE   B CG1   1 
ATOM   891  C CG2   . ILE   B 2 12  ? 26.172  -55.290 31.877  1.00 31.92  ?  12  ILE   B CG2   1 
ATOM   892  C CD1   . ILE   B 2 12  ? 24.806  -55.642 28.976  1.00 31.78  ?  12  ILE   B CD1   1 
ATOM   893  N N     . THR   B 2 13  ? 26.832  -51.906 31.966  1.00 31.54  ?  13  THR   B N     1 
ATOM   894  C CA    . THR   B 2 13  ? 27.463  -51.082 33.001  1.00 33.84  ?  13  THR   B CA    1 
ATOM   895  C C     . THR   B 2 13  ? 28.148  -51.940 34.075  1.00 35.09  ?  13  THR   B C     1 
ATOM   896  O O     . THR   B 2 13  ? 27.747  -53.084 34.347  1.00 33.31  ?  13  THR   B O     1 
ATOM   897  C CB    . THR   B 2 13  ? 26.478  -50.090 33.651  1.00 34.71  ?  13  THR   B CB    1 
ATOM   898  O OG1   . THR   B 2 13  ? 25.448  -50.817 34.347  1.00 33.38  ?  13  THR   B OG1   1 
ATOM   899  C CG2   . THR   B 2 13  ? 25.886  -49.086 32.659  1.00 34.33  ?  13  THR   B CG2   1 
ATOM   900  N N     . GLU   B 2 14  ? 29.168  -51.340 34.708  1.00 37.26  ?  14  GLU   B N     1 
ATOM   901  C CA    . GLU   B 2 14  ? 29.818  -51.857 35.908  1.00 40.86  ?  14  GLU   B CA    1 
ATOM   902  C C     . GLU   B 2 14  ? 28.836  -52.099 37.049  1.00 39.86  ?  14  GLU   B C     1 
ATOM   903  O O     . GLU   B 2 14  ? 28.911  -53.164 37.642  1.00 38.25  ?  14  GLU   B O     1 
ATOM   904  C CB    . GLU   B 2 14  ? 30.942  -50.927 36.401  1.00 44.61  ?  14  GLU   B CB    1 
ATOM   905  C CG    . GLU   B 2 14  ? 32.220  -51.216 35.633  1.00 47.35  ?  14  GLU   B CG    1 
ATOM   906  C CD    . GLU   B 2 14  ? 33.391  -50.273 35.859  1.00 52.58  ?  14  GLU   B CD    1 
ATOM   907  O OE1   . GLU   B 2 14  ? 34.076  -50.095 34.836  1.00 54.50  ?  14  GLU   B OE1   1 
ATOM   908  O OE2   . GLU   B 2 14  ? 33.648  -49.744 36.970  1.00 56.50  -1 14  GLU   B OE2   1 
ATOM   909  N N     . GLU   B 2 15  ? 27.942  -51.128 37.318  1.00 41.31  ?  15  GLU   B N     1 
ATOM   910  C CA    . GLU   B 2 15  ? 26.921  -51.238 38.360  1.00 42.66  ?  15  GLU   B CA    1 
ATOM   911  C C     . GLU   B 2 15  ? 26.099  -52.526 38.187  1.00 39.39  ?  15  GLU   B C     1 
ATOM   912  O O     . GLU   B 2 15  ? 25.896  -53.251 39.155  1.00 38.62  ?  15  GLU   B O     1 
ATOM   913  C CB    . GLU   B 2 15  ? 25.866  -50.130 38.333  1.00 47.00  ?  15  GLU   B CB    1 
ATOM   914  C CG    . GLU   B 2 15  ? 26.331  -48.682 38.492  1.00 53.29  ?  15  GLU   B CG    1 
ATOM   915  C CD    . GLU   B 2 15  ? 25.275  -47.765 37.875  1.00 58.59  ?  15  GLU   B CD    1 
ATOM   916  O OE1   . GLU   B 2 15  ? 24.204  -47.546 38.497  1.00 60.09  ?  15  GLU   B OE1   1 
ATOM   917  O OE2   . GLU   B 2 15  ? 25.483  -47.353 36.704  1.00 66.85  -1 15  GLU   B OE2   1 
ATOM   918  N N     . GLN   B 2 16  ? 25.683  -52.833 36.935  1.00 36.02  ?  16  GLN   B N     1 
ATOM   919  C CA    . GLN   B 2 16  ? 24.935  -54.051 36.649  1.00 34.18  ?  16  GLN   B CA    1 
ATOM   920  C C     . GLN   B 2 16  ? 25.764  -55.293 36.994  1.00 34.03  ?  16  GLN   B C     1 
ATOM   921  O O     . GLN   B 2 16  ? 25.233  -56.203 37.664  1.00 33.32  ?  16  GLN   B O     1 
ATOM   922  C CB    . GLN   B 2 16  ? 24.426  -54.129 35.203  1.00 32.61  ?  16  GLN   B CB    1 
ATOM   923  C CG    . GLN   B 2 16  ? 23.272  -53.178 34.869  1.00 32.31  ?  16  GLN   B CG    1 
ATOM   924  C CD    . GLN   B 2 16  ? 23.086  -53.057 33.363  1.00 32.48  ?  16  GLN   B CD    1 
ATOM   925  O OE1   . GLN   B 2 16  ? 22.316  -53.816 32.765  1.00 31.67  ?  16  GLN   B OE1   1 
ATOM   926  N NE2   . GLN   B 2 16  ? 23.786  -52.147 32.710  1.00 30.51  ?  16  GLN   B NE2   1 
ATOM   927  N N     . LYS   B 2 17  ? 27.051  -55.297 36.595  1.00 33.61  ?  17  LYS   B N     1 
ATOM   928  C CA    . LYS   B 2 17  ? 27.962  -56.406 36.874  1.00 34.73  ?  17  LYS   B CA    1 
ATOM   929  C C     . LYS   B 2 17  ? 28.229  -56.578 38.375  1.00 36.63  ?  17  LYS   B C     1 
ATOM   930  O O     . LYS   B 2 17  ? 28.180  -57.707 38.860  1.00 36.54  ?  17  LYS   B O     1 
ATOM   931  C CB    . LYS   B 2 17  ? 29.294  -56.273 36.130  1.00 35.57  ?  17  LYS   B CB    1 
ATOM   932  C CG    . LYS   B 2 17  ? 29.225  -56.333 34.600  1.00 34.02  ?  17  LYS   B CG    1 
ATOM   933  C CD    . LYS   B 2 17  ? 30.649  -56.261 34.012  1.00 35.29  ?  17  LYS   B CD    1 
ATOM   934  C CE    . LYS   B 2 17  ? 30.626  -55.915 32.560  1.00 34.41  ?  17  LYS   B CE    1 
ATOM   935  N NZ    . LYS   B 2 17  ? 31.935  -55.874 31.909  1.00 36.15  1  17  LYS   B NZ    1 
ATOM   936  N N     . GLN   B 2 18  ? 28.478  -55.472 39.093  1.00 39.22  ?  18  GLN   B N     1 
ATOM   937  C CA    . GLN   B 2 18  ? 28.622  -55.491 40.549  1.00 43.32  ?  18  GLN   B CA    1 
ATOM   938  C C     . GLN   B 2 18  ? 27.387  -56.092 41.229  1.00 42.28  ?  18  GLN   B C     1 
ATOM   939  O O     . GLN   B 2 18  ? 27.541  -56.999 42.031  1.00 41.04  ?  18  GLN   B O     1 
ATOM   940  C CB    . GLN   B 2 18  ? 28.852  -54.085 41.103  1.00 46.71  ?  18  GLN   B CB    1 
ATOM   941  C CG    . GLN   B 2 18  ? 30.181  -53.455 40.692  1.00 49.70  ?  18  GLN   B CG    1 
ATOM   942  C CD    . GLN   B 2 18  ? 31.413  -54.185 41.198  1.00 54.56  ?  18  GLN   B CD    1 
ATOM   943  O OE1   . GLN   B 2 18  ? 32.409  -54.322 40.474  1.00 56.20  ?  18  GLN   B OE1   1 
ATOM   944  N NE2   . GLN   B 2 18  ? 31.393  -54.619 42.455  1.00 55.50  ?  18  GLN   B NE2   1 
ATOM   945  N N     . ARG   B 2 19  ? 26.183  -55.643 40.820  1.00 41.63  ?  19  ARG   B N     1 
ATOM   946  C CA    . ARG   B 2 19  ? 24.916  -56.141 41.349  1.00 42.43  ?  19  ARG   B CA    1 
ATOM   947  C C     . ARG   B 2 19  ? 24.770  -57.665 41.131  1.00 40.80  ?  19  ARG   B C     1 
ATOM   948  O O     . ARG   B 2 19  ? 24.438  -58.385 42.084  1.00 39.75  ?  19  ARG   B O     1 
ATOM   949  C CB    . ARG   B 2 19  ? 23.759  -55.329 40.747  1.00 42.57  ?  19  ARG   B CB    1 
ATOM   950  C CG    . ARG   B 2 19  ? 22.414  -55.609 41.410  1.00 42.71  ?  19  ARG   B CG    1 
ATOM   951  C CD    . ARG   B 2 19  ? 21.254  -54.799 40.850  1.00 41.84  ?  19  ARG   B CD    1 
ATOM   952  N NE    . ARG   B 2 19  ? 19.979  -55.395 41.271  1.00 41.50  ?  19  ARG   B NE    1 
ATOM   953  C CZ    . ARG   B 2 19  ? 18.769  -55.107 40.807  1.00 39.71  ?  19  ARG   B CZ    1 
ATOM   954  N NH1   . ARG   B 2 19  ? 18.612  -54.324 39.762  1.00 37.68  1  19  ARG   B NH1   1 
ATOM   955  N NH2   . ARG   B 2 19  ? 17.712  -55.651 41.382  1.00 40.06  ?  19  ARG   B NH2   1 
ATOM   956  N N     . ALA   B 2 20  ? 25.121  -58.157 39.917  1.00 38.44  ?  20  ALA   B N     1 
ATOM   957  C CA    . ALA   B 2 20  ? 25.050  -59.585 39.607  1.00 37.41  ?  20  ALA   B CA    1 
ATOM   958  C C     . ALA   B 2 20  ? 26.032  -60.426 40.425  1.00 40.94  ?  20  ALA   B C     1 
ATOM   959  O O     . ALA   B 2 20  ? 25.688  -61.561 40.765  1.00 40.23  ?  20  ALA   B O     1 
ATOM   960  C CB    . ALA   B 2 20  ? 25.196  -59.855 38.129  1.00 34.79  ?  20  ALA   B CB    1 
ATOM   961  N N     . GLN   B 2 21  ? 27.198  -59.871 40.794  1.00 43.38  ?  21  GLN   B N     1 
ATOM   962  C CA    . GLN   B 2 21  ? 28.135  -60.577 41.662  1.00 48.88  ?  21  GLN   B CA    1 
ATOM   963  C C     . GLN   B 2 21  ? 27.728  -60.565 43.152  1.00 51.38  ?  21  GLN   B C     1 
ATOM   964  O O     . GLN   B 2 21  ? 28.216  -61.429 43.894  1.00 52.64  ?  21  GLN   B O     1 
ATOM   965  C CB    . GLN   B 2 21  ? 29.575  -60.119 41.403  1.00 51.49  ?  21  GLN   B CB    1 
ATOM   966  C CG    . GLN   B 2 21  ? 30.625  -61.109 41.925  1.00 55.31  ?  21  GLN   B CG    1 
ATOM   967  C CD    . GLN   B 2 21  ? 31.828  -61.311 41.024  1.00 58.17  ?  21  GLN   B CD    1 
ATOM   968  O OE1   . GLN   B 2 21  ? 31.703  -61.537 39.812  1.00 56.73  ?  21  GLN   B OE1   1 
ATOM   969  N NE2   . GLN   B 2 21  ? 33.016  -61.251 41.615  1.00 62.73  ?  21  GLN   B NE2   1 
ATOM   970  N N     . GLY   B 2 22  ? 26.823  -59.655 43.591  1.00 49.51  ?  22  GLY   B N     1 
ATOM   971  C CA    . GLY   B 2 22  ? 26.338  -59.601 44.966  1.00 50.06  ?  22  GLY   B CA    1 
ATOM   972  C C     . GLY   B 2 22  ? 25.227  -60.619 45.274  1.00 48.21  ?  22  GLY   B C     1 
ATOM   973  O O     . GLY   B 2 22  ? 24.963  -61.531 44.481  1.00 44.46  ?  22  GLY   B O     1 
ATOM   974  N N     . ASP   B 2 23  ? 24.592  -60.445 46.452  1.00 49.83  ?  23  ASP   B N     1 
ATOM   975  C CA    . ASP   B 2 23  ? 23.600  -61.342 47.040  1.00 51.51  ?  23  ASP   B CA    1 
ATOM   976  C C     . ASP   B 2 23  ? 22.214  -60.704 47.227  1.00 49.48  ?  23  ASP   B C     1 
ATOM   977  O O     . ASP   B 2 23  ? 21.357  -61.334 47.845  1.00 49.43  ?  23  ASP   B O     1 
ATOM   978  C CB    . ASP   B 2 23  ? 24.091  -61.859 48.390  1.00 56.26  ?  23  ASP   B CB    1 
ATOM   979  C CG    . ASP   B 2 23  ? 25.464  -62.497 48.332  1.00 59.73  ?  23  ASP   B CG    1 
ATOM   980  O OD1   . ASP   B 2 23  ? 25.619  -63.386 47.470  1.00 60.15  ?  23  ASP   B OD1   1 
ATOM   981  O OD2   . ASP   B 2 23  ? 26.355  -62.051 49.097  1.00 65.00  -1 23  ASP   B OD2   1 
ATOM   982  N N     . ASP   B 2 24  ? 21.971  -59.477 46.730  1.00 47.55  ?  24  ASP   B N     1 
ATOM   983  C CA    . ASP   B 2 24  ? 20.666  -58.822 46.832  1.00 46.62  ?  24  ASP   B CA    1 
ATOM   984  C C     . ASP   B 2 24  ? 19.728  -59.371 45.754  1.00 42.04  ?  24  ASP   B C     1 
ATOM   985  O O     . ASP   B 2 24  ? 20.165  -60.152 44.888  1.00 40.47  ?  24  ASP   B O     1 
ATOM   986  C CB    . ASP   B 2 24  ? 20.819  -57.307 46.841  1.00 48.56  ?  24  ASP   B CB    1 
ATOM   987  C CG    . ASP   B 2 24  ? 21.433  -56.728 48.110  1.00 52.93  ?  24  ASP   B CG    1 
ATOM   988  O OD1   . ASP   B 2 24  ? 20.919  -57.046 49.197  1.00 54.00  ?  24  ASP   B OD1   1 
ATOM   989  O OD2   . ASP   B 2 24  ? 22.421  -55.961 48.002  1.00 57.32  -1 24  ASP   B OD2   1 
ATOM   990  N N     . TRP   B 2 25  ? 18.438  -58.992 45.844  1.00 40.80  ?  25  TRP   B N     1 
ATOM   991  C CA    . TRP   B 2 25  ? 17.395  -59.560 44.991  1.00 39.31  ?  25  TRP   B CA    1 
ATOM   992  C C     . TRP   B 2 25  ? 17.668  -59.147 43.531  1.00 35.19  ?  25  TRP   B C     1 
ATOM   993  O O     . TRP   B 2 25  ? 17.884  -57.961 43.305  1.00 35.01  ?  25  TRP   B O     1 
ATOM   994  C CB    . TRP   B 2 25  ? 15.965  -59.147 45.420  1.00 41.02  ?  25  TRP   B CB    1 
ATOM   995  C CG    . TRP   B 2 25  ? 14.918  -59.547 44.403  1.00 40.00  ?  25  TRP   B CG    1 
ATOM   996  C CD1   . TRP   B 2 25  ? 14.471  -58.795 43.355  1.00 39.13  ?  25  TRP   B CD1   1 
ATOM   997  C CD2   . TRP   B 2 25  ? 14.302  -60.844 44.245  1.00 40.62  ?  25  TRP   B CD2   1 
ATOM   998  N NE1   . TRP   B 2 25  ? 13.607  -59.505 42.575  1.00 38.89  ?  25  TRP   B NE1   1 
ATOM   999  C CE2   . TRP   B 2 25  ? 13.474  -60.767 43.093  1.00 39.89  ?  25  TRP   B CE2   1 
ATOM   1000 C CE3   . TRP   B 2 25  ? 14.366  -62.059 44.955  1.00 42.26  ?  25  TRP   B CE3   1 
ATOM   1001 C CZ2   . TRP   B 2 25  ? 12.710  -61.857 42.643  1.00 40.55  ?  25  TRP   B CZ2   1 
ATOM   1002 C CZ3   . TRP   B 2 25  ? 13.609  -63.132 44.519  1.00 43.28  ?  25  TRP   B CZ3   1 
ATOM   1003 C CH2   . TRP   B 2 25  ? 12.812  -63.042 43.355  1.00 42.32  ?  25  TRP   B CH2   1 
ATOM   1004 N N     . PRO   B 2 26  ? 17.601  -60.017 42.489  1.00 32.37  ?  26  PRO   B N     1 
ATOM   1005 C CA    . PRO   B 2 26  ? 17.314  -61.465 42.563  1.00 31.22  ?  26  PRO   B CA    1 
ATOM   1006 C C     . PRO   B 2 26  ? 18.508  -62.420 42.621  1.00 31.13  ?  26  PRO   B C     1 
ATOM   1007 O O     . PRO   B 2 26  ? 18.289  -63.637 42.524  1.00 30.79  ?  26  PRO   B O     1 
ATOM   1008 C CB    . PRO   B 2 26  ? 16.527  -61.660 41.268  1.00 29.22  ?  26  PRO   B CB    1 
ATOM   1009 C CG    . PRO   B 2 26  ? 17.326  -60.822 40.294  1.00 28.56  ?  26  PRO   B CG    1 
ATOM   1010 C CD    . PRO   B 2 26  ? 17.726  -59.585 41.081  1.00 30.55  ?  26  PRO   B CD    1 
ATOM   1011 N N     . TYR   B 2 27  ? 19.746  -61.890 42.792  1.00 31.89  ?  27  TYR   B N     1 
ATOM   1012 C CA    . TYR   B 2 27  ? 20.967  -62.658 42.565  1.00 31.94  ?  27  TYR   B CA    1 
ATOM   1013 C C     . TYR   B 2 27  ? 21.190  -63.621 43.735  1.00 33.56  ?  27  TYR   B C     1 
ATOM   1014 O O     . TYR   B 2 27  ? 21.629  -64.744 43.501  1.00 32.90  ?  27  TYR   B O     1 
ATOM   1015 C CB    . TYR   B 2 27  ? 22.127  -61.721 42.212  1.00 32.37  ?  27  TYR   B CB    1 
ATOM   1016 C CG    . TYR   B 2 27  ? 21.883  -60.947 40.922  1.00 30.83  ?  27  TYR   B CG    1 
ATOM   1017 C CD1   . TYR   B 2 27  ? 21.986  -61.586 39.674  1.00 29.61  ?  27  TYR   B CD1   1 
ATOM   1018 C CD2   . TYR   B 2 27  ? 21.514  -59.591 40.931  1.00 30.79  ?  27  TYR   B CD2   1 
ATOM   1019 C CE1   . TYR   B 2 27  ? 21.741  -60.902 38.481  1.00 28.09  ?  27  TYR   B CE1   1 
ATOM   1020 C CE2   . TYR   B 2 27  ? 21.253  -58.906 39.749  1.00 29.53  ?  27  TYR   B CE2   1 
ATOM   1021 C CZ    . TYR   B 2 27  ? 21.387  -59.554 38.515  1.00 28.34  ?  27  TYR   B CZ    1 
ATOM   1022 O OH    . TYR   B 2 27  ? 21.130  -58.900 37.331  1.00 26.92  ?  27  TYR   B OH    1 
ATOM   1023 N N     . GLY   B 2 28  ? 20.846  -63.221 44.969  1.00 36.18  ?  28  GLY   B N     1 
ATOM   1024 C CA    . GLY   B 2 28  ? 20.924  -64.099 46.128  1.00 38.54  ?  28  GLY   B CA    1 
ATOM   1025 C C     . GLY   B 2 28  ? 20.082  -65.363 45.965  1.00 38.41  ?  28  GLY   B C     1 
ATOM   1026 O O     . GLY   B 2 28  ? 20.633  -66.473 46.080  1.00 38.93  ?  28  GLY   B O     1 
ATOM   1027 N N     . GLN   B 2 29  ? 18.781  -65.173 45.632  1.00 36.92  ?  29  GLN   B N     1 
ATOM   1028 C CA    . GLN   B 2 29  ? 17.890  -66.304 45.404  1.00 36.75  ?  29  GLN   B CA    1 
ATOM   1029 C C     . GLN   B 2 29  ? 18.436  -67.228 44.314  1.00 35.61  ?  29  GLN   B C     1 
ATOM   1030 O O     . GLN   B 2 29  ? 18.390  -68.449 44.504  1.00 35.47  ?  29  GLN   B O     1 
ATOM   1031 C CB    . GLN   B 2 29  ? 16.462  -65.901 45.042  1.00 36.13  ?  29  GLN   B CB    1 
ATOM   1032 C CG    . GLN   B 2 29  ? 15.456  -67.053 44.925  1.00 35.58  ?  29  GLN   B CG    1 
ATOM   1033 C CD    . GLN   B 2 29  ? 15.245  -67.791 46.227  1.00 37.26  ?  29  GLN   B CD    1 
ATOM   1034 O OE1   . GLN   B 2 29  ? 14.987  -67.151 47.248  1.00 38.14  ?  29  GLN   B OE1   1 
ATOM   1035 N NE2   . GLN   B 2 29  ? 15.421  -69.114 46.226  1.00 37.71  ?  29  GLN   B NE2   1 
ATOM   1036 N N     . CYS   B 2 30  ? 18.974  -66.651 43.216  1.00 34.88  ?  30  CYS   B N     1 
ATOM   1037 C CA    . CYS   B 2 30  ? 19.534  -67.418 42.110  1.00 33.44  ?  30  CYS   B CA    1 
ATOM   1038 C C     . CYS   B 2 30  ? 20.683  -68.324 42.594  1.00 35.58  ?  30  CYS   B C     1 
ATOM   1039 O O     . CYS   B 2 30  ? 20.660  -69.536 42.351  1.00 34.34  ?  30  CYS   B O     1 
ATOM   1040 C CB    . CYS   B 2 30  ? 19.934  -66.492 40.953  1.00 31.44  ?  30  CYS   B CB    1 
ATOM   1041 S SG    . CYS   B 2 30  ? 20.582  -67.355 39.495  1.00 29.22  ?  30  CYS   B SG    1 
ATOM   1042 N N     . LYS   B 2 31  ? 21.623  -67.743 43.356  1.00 38.39  ?  31  LYS   B N     1 
ATOM   1043 C CA    . LYS   B 2 31  ? 22.717  -68.476 43.990  1.00 42.08  ?  31  LYS   B CA    1 
ATOM   1044 C C     . LYS   B 2 31  ? 22.228  -69.597 44.917  1.00 43.96  ?  31  LYS   B C     1 
ATOM   1045 O O     . LYS   B 2 31  ? 22.808  -70.684 44.873  1.00 46.74  ?  31  LYS   B O     1 
ATOM   1046 C CB    . LYS   B 2 31  ? 23.721  -67.500 44.640  1.00 43.78  ?  31  LYS   B CB    1 
ATOM   1047 C CG    . LYS   B 2 31  ? 24.466  -66.719 43.529  1.00 43.15  ?  31  LYS   B CG    1 
ATOM   1048 C CD    . LYS   B 2 31  ? 25.155  -65.424 43.925  1.00 45.48  ?  31  LYS   B CD    1 
ATOM   1049 C CE    . LYS   B 2 31  ? 25.323  -64.532 42.733  1.00 44.42  ?  31  LYS   B CE    1 
ATOM   1050 N NZ    . LYS   B 2 31  ? 26.128  -63.349 43.021  1.00 46.18  1  31  LYS   B NZ    1 
ATOM   1051 N N     . GLU   B 2 32  ? 21.158  -69.367 45.700  1.00 44.62  ?  32  GLU   B N     1 
ATOM   1052 C CA    . GLU   B 2 32  ? 20.513  -70.417 46.496  1.00 45.59  ?  32  GLU   B CA    1 
ATOM   1053 C C     . GLU   B 2 32  ? 19.913  -71.515 45.604  1.00 42.67  ?  32  GLU   B C     1 
ATOM   1054 O O     . GLU   B 2 32  ? 20.047  -72.695 45.930  1.00 41.80  ?  32  GLU   B O     1 
ATOM   1055 C CB    . GLU   B 2 32  ? 19.420  -69.891 47.438  1.00 48.89  ?  32  GLU   B CB    1 
ATOM   1056 C CG    . GLU   B 2 32  ? 19.900  -69.469 48.830  1.00 55.74  ?  32  GLU   B CG    1 
ATOM   1057 C CD    . GLU   B 2 32  ? 18.832  -69.525 49.912  1.00 58.50  ?  32  GLU   B CD    1 
ATOM   1058 O OE1   . GLU   B 2 32  ? 17.762  -68.944 49.646  1.00 57.98  ?  32  GLU   B OE1   1 
ATOM   1059 O OE2   . GLU   B 2 32  ? 19.049  -70.134 50.994  1.00 62.48  -1 32  GLU   B OE2   1 
ATOM   1060 N N     . ASP   B 2 33  ? 19.269  -71.119 44.478  1.00 39.75  ?  33  ASP   B N     1 
ATOM   1061 C CA    . ASP   B 2 33  ? 18.711  -72.059 43.514  1.00 36.35  ?  33  ASP   B CA    1 
ATOM   1062 C C     . ASP   B 2 33  ? 19.798  -72.961 42.924  1.00 36.43  ?  33  ASP   B C     1 
ATOM   1063 O O     . ASP   B 2 33  ? 19.539  -74.146 42.742  1.00 33.98  ?  33  ASP   B O     1 
ATOM   1064 C CB    . ASP   B 2 33  ? 17.839  -71.363 42.472  1.00 34.37  ?  33  ASP   B CB    1 
ATOM   1065 C CG    . ASP   B 2 33  ? 16.607  -70.609 42.971  1.00 34.89  ?  33  ASP   B CG    1 
ATOM   1066 O OD1   . ASP   B 2 33  ? 16.122  -70.943 44.105  1.00 35.20  ?  33  ASP   B OD1   1 
ATOM   1067 O OD2   . ASP   B 2 33  ? 16.185  -69.645 42.248  1.00 32.02  -1 33  ASP   B OD2   1 
ATOM   1068 N N     . GLN   B 2 34  ? 21.021  -72.423 42.698  1.00 38.11  ?  34  GLN   B N     1 
ATOM   1069 C CA    . GLN   B 2 34  ? 22.142  -73.195 42.154  1.00 40.48  ?  34  GLN   B CA    1 
ATOM   1070 C C     . GLN   B 2 34  ? 22.595  -74.375 43.027  1.00 43.17  ?  34  GLN   B C     1 
ATOM   1071 O O     . GLN   B 2 34  ? 23.207  -75.296 42.477  1.00 45.90  ?  34  GLN   B O     1 
ATOM   1072 C CB    . GLN   B 2 34  ? 23.339  -72.294 41.849  1.00 40.92  ?  34  GLN   B CB    1 
ATOM   1073 C CG    . GLN   B 2 34  ? 23.098  -71.392 40.646  1.00 40.03  ?  34  GLN   B CG    1 
ATOM   1074 C CD    . GLN   B 2 34  ? 24.083  -70.248 40.578  1.00 40.19  ?  34  GLN   B CD    1 
ATOM   1075 O OE1   . GLN   B 2 34  ? 25.304  -70.446 40.595  1.00 41.62  ?  34  GLN   B OE1   1 
ATOM   1076 N NE2   . GLN   B 2 34  ? 23.543  -69.040 40.580  1.00 39.15  ?  34  GLN   B NE2   1 
ATOM   1077 N N     . LYS   B 2 35  ? 22.331  -74.343 44.351  1.00 44.04  ?  35  LYS   B N     1 
ATOM   1078 C CA    . LYS   B 2 35  ? 22.655  -75.431 45.272  1.00 46.84  ?  35  LYS   B CA    1 
ATOM   1079 C C     . LYS   B 2 35  ? 21.509  -76.437 45.474  1.00 45.10  ?  35  LYS   B C     1 
ATOM   1080 O O     . LYS   B 2 35  ? 21.770  -77.490 46.023  1.00 44.99  ?  35  LYS   B O     1 
ATOM   1081 C CB    . LYS   B 2 35  ? 23.225  -74.841 46.572  1.00 50.14  ?  35  LYS   B CB    1 
ATOM   1082 C CG    . LYS   B 2 35  ? 24.528  -74.015 46.372  1.00 53.23  ?  35  LYS   B CG    1 
ATOM   1083 C CD    . LYS   B 2 35  ? 25.503  -73.888 47.550  1.00 56.83  ?  35  LYS   B CD    1 
ATOM   1084 C CE    . LYS   B 2 35  ? 26.896  -73.359 47.196  1.00 58.95  ?  35  LYS   B CE    1 
ATOM   1085 N NZ    . LYS   B 2 35  ? 28.004  -73.678 48.129  1.00 62.91  1  35  LYS   B NZ    1 
ATOM   1086 N N     . LYS   B 2 36  ? 20.267  -76.154 45.029  1.00 43.28  ?  36  LYS   B N     1 
ATOM   1087 C CA    . LYS   B 2 36  ? 19.172  -77.120 45.079  1.00 43.53  ?  36  LYS   B CA    1 
ATOM   1088 C C     . LYS   B 2 36  ? 19.452  -78.349 44.195  1.00 44.08  ?  36  LYS   B C     1 
ATOM   1089 O O     . LYS   B 2 36  ? 20.060  -78.228 43.112  1.00 43.35  ?  36  LYS   B O     1 
ATOM   1090 C CB    . LYS   B 2 36  ? 17.863  -76.465 44.619  1.00 42.27  ?  36  LYS   B CB    1 
ATOM   1091 C CG    . LYS   B 2 36  ? 17.320  -75.332 45.483  1.00 42.97  ?  36  LYS   B CG    1 
ATOM   1092 C CD    . LYS   B 2 36  ? 16.060  -74.733 44.884  1.00 40.77  ?  36  LYS   B CD    1 
ATOM   1093 C CE    . LYS   B 2 36  ? 15.323  -73.859 45.839  1.00 41.91  ?  36  LYS   B CE    1 
ATOM   1094 N NZ    . LYS   B 2 36  ? 14.412  -72.964 45.129  1.00 40.10  1  36  LYS   B NZ    1 
ATOM   1095 N N     . SER   B 2 37  ? 18.951  -79.516 44.646  1.00 44.58  ?  37  SER   B N     1 
ATOM   1096 C CA    . SER   B 2 37  ? 19.130  -80.803 43.973  1.00 45.55  ?  37  SER   B CA    1 
ATOM   1097 C C     . SER   B 2 37  ? 18.528  -80.824 42.563  1.00 43.35  ?  37  SER   B C     1 
ATOM   1098 O O     . SER   B 2 37  ? 19.166  -81.384 41.662  1.00 44.18  ?  37  SER   B O     1 
ATOM   1099 C CB    . SER   B 2 37  ? 18.623  -81.987 44.805  1.00 47.55  ?  37  SER   B CB    1 
ATOM   1100 O OG    . SER   B 2 37  ? 17.296  -81.798 45.286  1.00 47.06  ?  37  SER   B OG    1 
ATOM   1101 N N     . GLU   B 2 38  ? 17.367  -80.170 42.347  1.00 40.21  ?  38  GLU   B N     1 
ATOM   1102 C CA    . GLU   B 2 38  ? 16.744  -80.135 41.023  1.00 37.75  ?  38  GLU   B CA    1 
ATOM   1103 C C     . GLU   B 2 38  ? 17.580  -79.378 39.980  1.00 35.76  ?  38  GLU   B C     1 
ATOM   1104 O O     . GLU   B 2 38  ? 17.406  -79.675 38.791  1.00 35.00  ?  38  GLU   B O     1 
ATOM   1105 C CB    . GLU   B 2 38  ? 15.307  -79.605 41.058  1.00 36.45  ?  38  GLU   B CB    1 
ATOM   1106 C CG    . GLU   B 2 38  ? 15.188  -78.119 41.392  1.00 34.94  ?  38  GLU   B CG    1 
ATOM   1107 C CD    . GLU   B 2 38  ? 13.783  -77.688 41.753  1.00 33.35  ?  38  GLU   B CD    1 
ATOM   1108 O OE1   . GLU   B 2 38  ? 12.881  -77.739 40.876  1.00 30.60  ?  38  GLU   B OE1   1 
ATOM   1109 O OE2   . GLU   B 2 38  ? 13.626  -77.403 42.965  1.00 33.69  -1 38  GLU   B OE2   1 
ATOM   1110 N N     . TRP   B 2 39  ? 18.465  -78.444 40.409  1.00 34.99  ?  39  TRP   B N     1 
ATOM   1111 C CA    . TRP   B 2 39  ? 19.281  -77.635 39.513  1.00 34.43  ?  39  TRP   B CA    1 
ATOM   1112 C C     . TRP   B 2 39  ? 20.766  -77.988 39.501  1.00 36.77  ?  39  TRP   B C     1 
ATOM   1113 O O     . TRP   B 2 39  ? 21.369  -77.847 38.438  1.00 37.57  ?  39  TRP   B O     1 
ATOM   1114 C CB    . TRP   B 2 39  ? 19.097  -76.140 39.812  1.00 32.35  ?  39  TRP   B CB    1 
ATOM   1115 C CG    . TRP   B 2 39  ? 17.658  -75.672 39.841  1.00 30.31  ?  39  TRP   B CG    1 
ATOM   1116 C CD1   . TRP   B 2 39  ? 17.007  -75.179 40.927  1.00 30.07  ?  39  TRP   B CD1   1 
ATOM   1117 C CD2   . TRP   B 2 39  ? 16.683  -75.697 38.774  1.00 28.34  ?  39  TRP   B CD2   1 
ATOM   1118 N NE1   . TRP   B 2 39  ? 15.725  -74.852 40.608  1.00 29.08  ?  39  TRP   B NE1   1 
ATOM   1119 C CE2   . TRP   B 2 39  ? 15.482  -75.162 39.299  1.00 28.07  ?  39  TRP   B CE2   1 
ATOM   1120 C CE3   . TRP   B 2 39  ? 16.697  -76.100 37.429  1.00 27.69  ?  39  TRP   B CE3   1 
ATOM   1121 C CZ2   . TRP   B 2 39  ? 14.303  -75.047 38.546  1.00 26.18  ?  39  TRP   B CZ2   1 
ATOM   1122 C CZ3   . TRP   B 2 39  ? 15.544  -75.977 36.673  1.00 26.84  ?  39  TRP   B CZ3   1 
ATOM   1123 C CH2   . TRP   B 2 39  ? 14.360  -75.449 37.229  1.00 26.09  ?  39  TRP   B CH2   1 
ATOM   1124 N N     . LYS   B 2 40  ? 21.365  -78.381 40.629  1.00 39.29  ?  40  LYS   B N     1 
ATOM   1125 C CA    . LYS   B 2 40  ? 22.826  -78.312 40.796  1.00 41.98  ?  40  LYS   B CA    1 
ATOM   1126 C C     . LYS   B 2 40  ? 23.629  -79.175 39.808  1.00 43.17  ?  40  LYS   B C     1 
ATOM   1127 O O     . LYS   B 2 40  ? 24.737  -78.781 39.468  1.00 46.50  ?  40  LYS   B O     1 
ATOM   1128 C CB    . LYS   B 2 40  ? 23.276  -78.600 42.232  1.00 43.75  ?  40  LYS   B CB    1 
ATOM   1129 C CG    . LYS   B 2 40  ? 23.095  -80.005 42.776  1.00 45.94  ?  40  LYS   B CG    1 
ATOM   1130 C CD    . LYS   B 2 40  ? 23.756  -80.130 44.146  1.00 49.49  ?  40  LYS   B CD    1 
ATOM   1131 C CE    . LYS   B 2 40  ? 23.282  -81.292 44.972  1.00 51.75  ?  40  LYS   B CE    1 
ATOM   1132 N NZ    . LYS   B 2 40  ? 23.616  -82.595 44.386  1.00 53.54  1  40  LYS   B NZ    1 
ATOM   1133 N N     . ASP   B 2 41  ? 23.078  -80.305 39.311  1.00 43.40  ?  41  ASP   B N     1 
ATOM   1134 C CA    . ASP   B 2 41  ? 23.789  -81.235 38.419  1.00 44.63  ?  41  ASP   B CA    1 
ATOM   1135 C C     . ASP   B 2 41  ? 23.849  -80.784 36.951  1.00 42.34  ?  41  ASP   B C     1 
ATOM   1136 O O     . ASP   B 2 41  ? 24.503  -81.438 36.155  1.00 42.99  ?  41  ASP   B O     1 
ATOM   1137 C CB    . ASP   B 2 41  ? 23.264  -82.661 38.552  1.00 46.74  ?  41  ASP   B CB    1 
ATOM   1138 C CG    . ASP   B 2 41  ? 23.801  -83.447 39.743  1.00 50.47  ?  41  ASP   B CG    1 
ATOM   1139 O OD1   . ASP   B 2 41  ? 25.000  -83.766 39.728  1.00 56.04  ?  41  ASP   B OD1   1 
ATOM   1140 O OD2   . ASP   B 2 41  ? 23.027  -83.722 40.685  1.00 50.27  ?  41  ASP   B OD2   1 
ATOM   1141 N N     . SER   B 2 42  ? 23.187  -79.684 36.579  1.00 39.71  ?  42  SER   B N     1 
ATOM   1142 C CA    . SER   B 2 42  ? 23.154  -79.142 35.230  1.00 38.02  ?  42  SER   B CA    1 
ATOM   1143 C C     . SER   B 2 42  ? 24.318  -78.175 35.011  1.00 38.57  ?  42  SER   B C     1 
ATOM   1144 O O     . SER   B 2 42  ? 24.768  -77.521 35.942  1.00 38.91  ?  42  SER   B O     1 
ATOM   1145 C CB    . SER   B 2 42  ? 21.829  -78.452 35.035  1.00 34.78  ?  42  SER   B CB    1 
ATOM   1146 O OG    . SER   B 2 42  ? 21.590  -78.303 33.650  1.00 33.78  ?  42  SER   B OG    1 
ATOM   1147 N N     . ASP   B 2 43  ? 24.772  -78.048 33.760  1.00 40.23  ?  43  ASP   B N     1 
ATOM   1148 C CA    . ASP   B 2 43  ? 25.623  -76.934 33.327  1.00 40.63  ?  43  ASP   B CA    1 
ATOM   1149 C C     . ASP   B 2 43  ? 24.869  -75.603 33.230  1.00 37.23  ?  43  ASP   B C     1 
ATOM   1150 O O     . ASP   B 2 43  ? 25.520  -74.550 33.286  1.00 36.41  ?  43  ASP   B O     1 
ATOM   1151 C CB    . ASP   B 2 43  ? 26.304  -77.253 32.004  1.00 42.55  ?  43  ASP   B CB    1 
ATOM   1152 C CG    . ASP   B 2 43  ? 27.274  -78.424 32.042  1.00 47.05  ?  43  ASP   B CG    1 
ATOM   1153 O OD1   . ASP   B 2 43  ? 27.827  -78.721 33.118  1.00 48.36  ?  43  ASP   B OD1   1 
ATOM   1154 O OD2   . ASP   B 2 43  ? 27.475  -79.043 30.979  1.00 51.62  ?  43  ASP   B OD2   1 
ATOM   1155 N N     . PHE   B 2 44  ? 23.528  -75.643 33.099  1.00 34.53  ?  44  PHE   B N     1 
ATOM   1156 C CA    . PHE   B 2 44  ? 22.679  -74.472 32.948  1.00 31.44  ?  44  PHE   B CA    1 
ATOM   1157 C C     . PHE   B 2 44  ? 22.287  -74.008 34.349  1.00 30.93  ?  44  PHE   B C     1 
ATOM   1158 O O     . PHE   B 2 44  ? 22.071  -74.832 35.260  1.00 32.07  ?  44  PHE   B O     1 
ATOM   1159 C CB    . PHE   B 2 44  ? 21.400  -74.772 32.167  1.00 30.07  ?  44  PHE   B CB    1 
ATOM   1160 C CG    . PHE   B 2 44  ? 21.584  -75.215 30.722  1.00 30.77  ?  44  PHE   B CG    1 
ATOM   1161 C CD1   . PHE   B 2 44  ? 22.127  -76.463 30.422  1.00 32.84  ?  44  PHE   B CD1   1 
ATOM   1162 C CD2   . PHE   B 2 44  ? 21.110  -74.429 29.665  1.00 30.00  ?  44  PHE   B CD2   1 
ATOM   1163 C CE1   . PHE   B 2 44  ? 22.328  -76.868 29.104  1.00 33.97  ?  44  PHE   B CE1   1 
ATOM   1164 C CE2   . PHE   B 2 44  ? 21.276  -74.853 28.341  1.00 31.38  ?  44  PHE   B CE2   1 
ATOM   1165 C CZ    . PHE   B 2 44  ? 21.887  -76.075 28.058  1.00 32.75  ?  44  PHE   B CZ    1 
ATOM   1166 N N     . LEU   B 2 45  ? 22.140  -72.686 34.489  1.00 28.76  ?  45  LEU   B N     1 
ATOM   1167 C CA    . LEU   B 2 45  ? 21.674  -72.092 35.721  1.00 27.91  ?  45  LEU   B CA    1 
ATOM   1168 C C     . LEU   B 2 45  ? 20.194  -72.441 35.917  1.00 27.81  ?  45  LEU   B C     1 
ATOM   1169 O O     . LEU   B 2 45  ? 19.502  -72.739 34.921  1.00 26.46  ?  45  LEU   B O     1 
ATOM   1170 C CB    . LEU   B 2 45  ? 21.864  -70.586 35.681  1.00 27.09  ?  45  LEU   B CB    1 
ATOM   1171 C CG    . LEU   B 2 45  ? 23.315  -70.108 35.683  1.00 28.80  ?  45  LEU   B CG    1 
ATOM   1172 C CD1   . LEU   B 2 45  ? 23.360  -68.736 35.089  1.00 28.40  ?  45  LEU   B CD1   1 
ATOM   1173 C CD2   . LEU   B 2 45  ? 23.878  -70.119 37.071  1.00 30.43  ?  45  LEU   B CD2   1 
ATOM   1174 N N     . PRO   B 2 46  ? 19.682  -72.395 37.180  1.00 27.12  ?  46  PRO   B N     1 
ATOM   1175 C CA    . PRO   B 2 46  ? 18.287  -72.701 37.452  1.00 26.78  ?  46  PRO   B CA    1 
ATOM   1176 C C     . PRO   B 2 46  ? 17.306  -71.947 36.559  1.00 25.77  ?  46  PRO   B C     1 
ATOM   1177 O O     . PRO   B 2 46  ? 17.450  -70.739 36.403  1.00 26.57  ?  46  PRO   B O     1 
ATOM   1178 C CB    . PRO   B 2 46  ? 18.107  -72.256 38.900  1.00 27.29  ?  46  PRO   B CB    1 
ATOM   1179 C CG    . PRO   B 2 46  ? 19.511  -72.302 39.517  1.00 28.52  ?  46  PRO   B CG    1 
ATOM   1180 C CD    . PRO   B 2 46  ? 20.430  -72.024 38.405  1.00 28.11  ?  46  PRO   B CD    1 
ATOM   1181 N N     . ASN   B 2 47  ? 16.316  -72.645 35.989  1.00 24.99  ?  47  ASN   B N     1 
ATOM   1182 C CA    . ASN   B 2 47  ? 15.181  -72.024 35.314  1.00 23.98  ?  47  ASN   B CA    1 
ATOM   1183 C C     . ASN   B 2 47  ? 14.185  -71.539 36.370  1.00 23.98  ?  47  ASN   B C     1 
ATOM   1184 O O     . ASN   B 2 47  ? 13.050  -72.006 36.431  1.00 24.62  ?  47  ASN   B O     1 
ATOM   1185 C CB    . ASN   B 2 47  ? 14.588  -72.985 34.293  1.00 24.55  ?  47  ASN   B CB    1 
ATOM   1186 C CG    . ASN   B 2 47  ? 15.584  -73.391 33.227  1.00 25.39  ?  47  ASN   B CG    1 
ATOM   1187 O OD1   . ASN   B 2 47  ? 16.153  -74.474 33.363  1.00 27.41  ?  47  ASN   B OD1   1 
ATOM   1188 N ND2   . ASN   B 2 47  ? 15.838  -72.560 32.222  1.00 24.39  ?  47  ASN   B ND2   1 
ATOM   1189 N N     . THR   B 2 48  ? 14.601  -70.529 37.138  1.00 24.06  ?  48  THR   B N     1 
ATOM   1190 C CA    . THR   B 2 48  ? 13.805  -69.892 38.181  1.00 25.70  ?  48  THR   B CA    1 
ATOM   1191 C C     . THR   B 2 48  ? 13.566  -68.433 37.790  1.00 25.32  ?  48  THR   B C     1 
ATOM   1192 O O     . THR   B 2 48  ? 14.357  -67.860 37.044  1.00 24.59  ?  48  THR   B O     1 
ATOM   1193 C CB    . THR   B 2 48  ? 14.496  -70.014 39.550  1.00 26.53  ?  48  THR   B CB    1 
ATOM   1194 O OG1   . THR   B 2 48  ? 15.791  -69.391 39.512  1.00 26.64  ?  48  THR   B OG1   1 
ATOM   1195 C CG2   . THR   B 2 48  ? 14.634  -71.472 39.930  1.00 27.17  ?  48  THR   B CG2   1 
ATOM   1196 N N     . GLN   B 2 49  ? 12.515  -67.831 38.358  1.00 27.14  ?  49  GLN   B N     1 
ATOM   1197 C CA    . GLN   B 2 49  ? 12.232  -66.398 38.215  1.00 29.42  ?  49  GLN   B CA    1 
ATOM   1198 C C     . GLN   B 2 49  ? 13.439  -65.568 38.653  1.00 28.58  ?  49  GLN   B C     1 
ATOM   1199 O O     . GLN   B 2 49  ? 13.856  -64.692 37.896  1.00 28.28  ?  49  GLN   B O     1 
ATOM   1200 C CB    . GLN   B 2 49  ? 11.004  -65.899 38.979  1.00 32.50  ?  49  GLN   B CB    1 
ATOM   1201 C CG    . GLN   B 2 49  ? 9.651   -66.344 38.420  1.00 36.26  ?  49  GLN   B CG    1 
ATOM   1202 C CD    . GLN   B 2 49  ? 9.357   -65.826 37.015  1.00 40.08  ?  49  GLN   B CD    1 
ATOM   1203 O OE1   . GLN   B 2 49  ? 9.754   -64.714 36.608  1.00 43.62  ?  49  GLN   B OE1   1 
ATOM   1204 N NE2   . GLN   B 2 49  ? 8.700   -66.672 36.226  1.00 39.66  ?  49  GLN   B NE2   1 
ATOM   1205 N N     . ALA   B 2 50  ? 14.077  -65.944 39.773  1.00 28.52  ?  50  ALA   B N     1 
ATOM   1206 C CA    . ALA   B 2 50  ? 15.233  -65.241 40.304  1.00 28.06  ?  50  ALA   B CA    1 
ATOM   1207 C C     . ALA   B 2 50  ? 16.337  -65.145 39.263  1.00 26.49  ?  50  ALA   B C     1 
ATOM   1208 O O     . ALA   B 2 50  ? 16.719  -64.055 38.899  1.00 26.75  ?  50  ALA   B O     1 
ATOM   1209 C CB    . ALA   B 2 50  ? 15.725  -65.879 41.575  1.00 28.95  ?  50  ALA   B CB    1 
ATOM   1210 N N     . CYS   B 2 51  ? 16.767  -66.278 38.721  1.00 26.71  ?  51  CYS   B N     1 
ATOM   1211 C CA    . CYS   B 2 51  ? 17.873  -66.291 37.766  1.00 24.93  ?  51  CYS   B CA    1 
ATOM   1212 C C     . CYS   B 2 51  ? 17.493  -65.628 36.434  1.00 22.89  ?  51  CYS   B C     1 
ATOM   1213 O O     . CYS   B 2 51  ? 18.330  -65.029 35.781  1.00 21.65  ?  51  CYS   B O     1 
ATOM   1214 C CB    . CYS   B 2 51  ? 18.352  -67.719 37.528  1.00 25.67  ?  51  CYS   B CB    1 
ATOM   1215 S SG    . CYS   B 2 51  ? 18.975  -68.567 39.011  1.00 28.46  ?  51  CYS   B SG    1 
ATOM   1216 N N     . TYR   B 2 52  ? 16.216  -65.722 36.038  1.00 22.58  ?  52  TYR   B N     1 
ATOM   1217 C CA    . TYR   B 2 52  ? 15.738  -65.160 34.776  1.00 21.01  ?  52  TYR   B CA    1 
ATOM   1218 C C     . TYR   B 2 52  ? 15.681  -63.637 34.833  1.00 22.12  ?  52  TYR   B C     1 
ATOM   1219 O O     . TYR   B 2 52  ? 16.246  -62.998 33.955  1.00 21.68  ?  52  TYR   B O     1 
ATOM   1220 C CB    . TYR   B 2 52  ? 14.358  -65.741 34.487  1.00 20.84  ?  52  TYR   B CB    1 
ATOM   1221 C CG    . TYR   B 2 52  ? 13.713  -65.310 33.175  1.00 19.84  ?  52  TYR   B CG    1 
ATOM   1222 C CD1   . TYR   B 2 52  ? 14.453  -65.093 31.989  1.00 18.89  ?  52  TYR   B CD1   1 
ATOM   1223 C CD2   . TYR   B 2 52  ? 12.332  -65.108 33.141  1.00 19.87  ?  52  TYR   B CD2   1 
ATOM   1224 C CE1   . TYR   B 2 52  ? 13.797  -64.755 30.802  1.00 19.23  ?  52  TYR   B CE1   1 
ATOM   1225 C CE2   . TYR   B 2 52  ? 11.700  -64.722 31.981  1.00 19.72  ?  52  TYR   B CE2   1 
ATOM   1226 C CZ    . TYR   B 2 52  ? 12.412  -64.602 30.799  1.00 19.43  ?  52  TYR   B CZ    1 
ATOM   1227 O OH    . TYR   B 2 52  ? 11.771  -64.259 29.643  1.00 20.39  ?  52  TYR   B OH    1 
ATOM   1228 N N     . ILE   B 2 53  ? 15.048  -63.073 35.884  1.00 24.07  ?  53  ILE   B N     1 
ATOM   1229 C CA    . ILE   B 2 53  ? 15.040  -61.633 36.129  1.00 26.28  ?  53  ILE   B CA    1 
ATOM   1230 C C     . ILE   B 2 53  ? 16.490  -61.118 36.127  1.00 25.42  ?  53  ILE   B C     1 
ATOM   1231 O O     . ILE   B 2 53  ? 16.802  -60.129 35.446  1.00 25.51  ?  53  ILE   B O     1 
ATOM   1232 C CB    . ILE   B 2 53  ? 14.312  -61.256 37.450  1.00 30.05  ?  53  ILE   B CB    1 
ATOM   1233 C CG1   . ILE   B 2 53  ? 12.826  -61.753 37.578  1.00 32.63  ?  53  ILE   B CG1   1 
ATOM   1234 C CG2   . ILE   B 2 53  ? 14.403  -59.743 37.730  1.00 31.69  ?  53  ILE   B CG2   1 
ATOM   1235 C CD1   . ILE   B 2 53  ? 12.094  -62.111 36.291  1.00 32.80  ?  53  ILE   B CD1   1 
ATOM   1236 N N     . GLY   B 2 54  ? 17.359  -61.776 36.910  1.00 25.55  ?  54  GLY   B N     1 
ATOM   1237 C CA    . GLY   B 2 54  ? 18.745  -61.369 37.050  1.00 25.20  ?  54  GLY   B CA    1 
ATOM   1238 C C     . GLY   B 2 54  ? 19.470  -61.354 35.705  1.00 24.39  ?  54  GLY   B C     1 
ATOM   1239 O O     . GLY   B 2 54  ? 20.205  -60.411 35.434  1.00 24.86  ?  54  GLY   B O     1 
ATOM   1240 N N     . SER   B 2 55  ? 19.193  -62.372 34.870  1.00 23.84  ?  55  SER   B N     1 
ATOM   1241 C CA    . SER   B 2 55  ? 19.684  -62.438 33.510  1.00 23.18  ?  55  SER   B CA    1 
ATOM   1242 C C     . SER   B 2 55  ? 19.241  -61.220 32.689  1.00 22.61  ?  55  SER   B C     1 
ATOM   1243 O O     . SER   B 2 55  ? 20.103  -60.569 32.078  1.00 22.24  ?  55  SER   B O     1 
ATOM   1244 C CB    . SER   B 2 55  ? 19.314  -63.773 32.884  1.00 23.35  ?  55  SER   B CB    1 
ATOM   1245 O OG    . SER   B 2 55  ? 19.463  -63.764 31.474  1.00 24.98  ?  55  SER   B OG    1 
ATOM   1246 N N     . ILE   B 2 56  ? 17.932  -60.899 32.678  1.00 21.86  ?  56  ILE   B N     1 
ATOM   1247 C CA    . ILE   B 2 56  ? 17.399  -59.778 31.872  1.00 21.74  ?  56  ILE   B CA    1 
ATOM   1248 C C     . ILE   B 2 56  ? 18.041  -58.444 32.310  1.00 22.96  ?  56  ILE   B C     1 
ATOM   1249 O O     . ILE   B 2 56  ? 18.484  -57.645 31.452  1.00 22.19  ?  56  ILE   B O     1 
ATOM   1250 C CB    . ILE   B 2 56  ? 15.851  -59.695 31.940  1.00 20.34  ?  56  ILE   B CB    1 
ATOM   1251 C CG1   . ILE   B 2 56  ? 15.172  -60.946 31.350  1.00 19.71  ?  56  ILE   B CG1   1 
ATOM   1252 C CG2   . ILE   B 2 56  ? 15.332  -58.420 31.287  1.00 20.53  ?  56  ILE   B CG2   1 
ATOM   1253 C CD1   . ILE   B 2 56  ? 13.736  -61.132 31.726  1.00 20.07  ?  56  ILE   B CD1   1 
ATOM   1254 N N     . LEU   B 2 57  ? 18.059  -58.204 33.639  1.00 25.06  ?  57  LEU   B N     1 
ATOM   1255 C CA    . LEU   B 2 57  ? 18.650  -56.993 34.202  1.00 26.88  ?  57  LEU   B CA    1 
ATOM   1256 C C     . LEU   B 2 57  ? 20.116  -56.854 33.816  1.00 25.26  ?  57  LEU   B C     1 
ATOM   1257 O O     . LEU   B 2 57  ? 20.483  -55.805 33.336  1.00 25.95  ?  57  LEU   B O     1 
ATOM   1258 C CB    . LEU   B 2 57  ? 18.426  -56.862 35.711  1.00 30.89  ?  57  LEU   B CB    1 
ATOM   1259 C CG    . LEU   B 2 57  ? 16.946  -56.754 36.126  1.00 33.67  ?  57  LEU   B CG    1 
ATOM   1260 C CD1   . LEU   B 2 57  ? 16.811  -56.524 37.648  1.00 36.81  ?  57  LEU   B CD1   1 
ATOM   1261 C CD2   . LEU   B 2 57  ? 16.066  -55.729 35.353  1.00 33.14  ?  57  LEU   B CD2   1 
ATOM   1262 N N     . LEU   B 2 58  ? 20.912  -57.920 33.921  1.00 25.58  ?  58  LEU   B N     1 
ATOM   1263 C CA    . LEU   B 2 58  ? 22.341  -57.858 33.626  1.00 25.07  ?  58  LEU   B CA    1 
ATOM   1264 C C     . LEU   B 2 58  ? 22.625  -57.697 32.117  1.00 23.75  ?  58  LEU   B C     1 
ATOM   1265 O O     . LEU   B 2 58  ? 23.641  -57.120 31.770  1.00 26.19  ?  58  LEU   B O     1 
ATOM   1266 C CB    . LEU   B 2 58  ? 23.025  -59.102 34.190  1.00 26.24  ?  58  LEU   B CB    1 
ATOM   1267 C CG    . LEU   B 2 58  ? 24.534  -59.231 33.941  1.00 26.74  ?  58  LEU   B CG    1 
ATOM   1268 C CD1   . LEU   B 2 58  ? 25.295  -58.056 34.514  1.00 27.82  ?  58  LEU   B CD1   1 
ATOM   1269 C CD2   . LEU   B 2 58  ? 25.063  -60.543 34.505  1.00 27.93  ?  58  LEU   B CD2   1 
ATOM   1270 N N     . THR   B 2 59  ? 21.783  -58.225 31.209  1.00 22.80  ?  59  THR   B N     1 
ATOM   1271 C CA    . THR   B 2 59  ? 22.073  -58.231 29.771  1.00 21.00  ?  59  THR   B CA    1 
ATOM   1272 C C     . THR   B 2 59  ? 21.512  -56.999 29.052  1.00 21.89  ?  59  THR   B C     1 
ATOM   1273 O O     . THR   B 2 59  ? 21.616  -56.916 27.812  1.00 20.95  ?  59  THR   B O     1 
ATOM   1274 C CB    . THR   B 2 59  ? 21.602  -59.554 29.171  1.00 19.58  ?  59  THR   B CB    1 
ATOM   1275 O OG1   . THR   B 2 59  ? 20.211  -59.759 29.446  1.00 18.46  ?  59  THR   B OG1   1 
ATOM   1276 C CG2   . THR   B 2 59  ? 22.442  -60.717 29.650  1.00 19.13  ?  59  THR   B CG2   1 
ATOM   1277 N N     . THR   B 2 60  ? 20.885  -56.058 29.792  1.00 22.96  ?  60  THR   B N     1 
ATOM   1278 C CA    . THR   B 2 60  ? 20.366  -54.809 29.236  1.00 23.28  ?  60  THR   B CA    1 
ATOM   1279 C C     . THR   B 2 60  ? 21.540  -53.867 28.947  1.00 23.03  ?  60  THR   B C     1 
ATOM   1280 O O     . THR   B 2 60  ? 22.257  -53.530 29.883  1.00 23.53  ?  60  THR   B O     1 
ATOM   1281 C CB    . THR   B 2 60  ? 19.389  -54.171 30.220  1.00 24.35  ?  60  THR   B CB    1 
ATOM   1282 O OG1   . THR   B 2 60  ? 18.317  -55.092 30.362  1.00 25.92  ?  60  THR   B OG1   1 
ATOM   1283 C CG2   . THR   B 2 60  ? 18.843  -52.849 29.738  1.00 25.98  ?  60  THR   B CG2   1 
ATOM   1284 N N     . ALA   B 2 61  ? 21.689  -53.413 27.686  1.00 22.76  ?  61  ALA   B N     1 
ATOM   1285 C CA    . ALA   B 2 61  ? 22.855  -52.612 27.277  1.00 24.14  ?  61  ALA   B CA    1 
ATOM   1286 C C     . ALA   B 2 61  ? 22.620  -51.159 27.648  1.00 24.68  ?  61  ALA   B C     1 
ATOM   1287 O O     . ALA   B 2 61  ? 22.246  -50.355 26.797  1.00 24.67  ?  61  ALA   B O     1 
ATOM   1288 C CB    . ALA   B 2 61  ? 23.170  -52.799 25.801  1.00 23.92  ?  61  ALA   B CB    1 
ATOM   1289 N N     . ARG   B 2 62  ? 22.772  -50.838 28.944  1.00 26.77  ?  62  ARG   B N     1 
ATOM   1290 C CA    . ARG   B 2 62  ? 22.473  -49.500 29.458  1.00 28.90  ?  62  ARG   B CA    1 
ATOM   1291 C C     . ARG   B 2 62  ? 23.518  -48.449 29.095  1.00 30.73  ?  62  ARG   B C     1 
ATOM   1292 O O     . ARG   B 2 62  ? 23.170  -47.270 29.170  1.00 30.99  ?  62  ARG   B O     1 
ATOM   1293 C CB    . ARG   B 2 62  ? 22.310  -49.458 30.977  1.00 31.27  ?  62  ARG   B CB    1 
ATOM   1294 C CG    . ARG   B 2 62  ? 21.138  -50.305 31.434  1.00 32.69  ?  62  ARG   B CG    1 
ATOM   1295 C CD    . ARG   B 2 62  ? 20.745  -50.081 32.905  1.00 35.91  ?  62  ARG   B CD    1 
ATOM   1296 N NE    . ARG   B 2 62  ? 19.361  -50.539 33.118  1.00 37.41  ?  62  ARG   B NE    1 
ATOM   1297 C CZ    . ARG   B 2 62  ? 18.220  -49.927 32.770  1.00 39.74  ?  62  ARG   B CZ    1 
ATOM   1298 N NH1   . ARG   B 2 62  ? 18.187  -48.635 32.447  1.00 43.66  1  62  ARG   B NH1   1 
ATOM   1299 N NH2   . ARG   B 2 62  ? 17.098  -50.623 32.753  1.00 38.82  ?  62  ARG   B NH2   1 
ATOM   1300 N N     . LYS   B 2 63  ? 24.773  -48.858 28.796  1.00 30.86  ?  63  LYS   B N     1 
ATOM   1301 C CA    . LYS   B 2 63  ? 25.854  -47.932 28.491  1.00 33.49  ?  63  LYS   B CA    1 
ATOM   1302 C C     . LYS   B 2 63  ? 25.862  -47.709 26.980  1.00 33.43  ?  63  LYS   B C     1 
ATOM   1303 O O     . LYS   B 2 63  ? 26.205  -48.652 26.271  1.00 34.61  ?  63  LYS   B O     1 
ATOM   1304 C CB    . LYS   B 2 63  ? 27.180  -48.495 29.028  1.00 34.59  ?  63  LYS   B CB    1 
ATOM   1305 C CG    . LYS   B 2 63  ? 28.440  -47.674 28.695  1.00 37.29  ?  63  LYS   B CG    1 
ATOM   1306 C CD    . LYS   B 2 63  ? 29.671  -47.941 29.564  1.00 39.98  ?  63  LYS   B CD    1 
ATOM   1307 C CE    . LYS   B 2 63  ? 30.940  -47.356 28.985  1.00 43.27  ?  63  LYS   B CE    1 
ATOM   1308 N NZ    . LYS   B 2 63  ? 32.178  -47.760 29.672  1.00 45.16  1  63  LYS   B NZ    1 
ATOM   1309 N N     . THR   B 2 64  ? 25.486  -46.507 26.511  1.00 33.09  ?  64  THR   B N     1 
ATOM   1310 C CA    . THR   B 2 64  ? 25.489  -46.158 25.088  1.00 33.80  ?  64  THR   B CA    1 
ATOM   1311 C C     . THR   B 2 64  ? 26.558  -45.102 24.782  1.00 34.49  ?  64  THR   B C     1 
ATOM   1312 O O     . THR   B 2 64  ? 26.481  -44.053 25.385  1.00 35.54  ?  64  THR   B O     1 
ATOM   1313 C CB    . THR   B 2 64  ? 24.108  -45.647 24.672  1.00 34.12  ?  64  THR   B CB    1 
ATOM   1314 O OG1   . THR   B 2 64  ? 23.223  -46.717 24.986  1.00 31.56  ?  64  THR   B OG1   1 
ATOM   1315 C CG2   . THR   B 2 64  ? 24.019  -45.410 23.171  1.00 34.88  ?  64  THR   B CG2   1 
ATOM   1316 N N     . THR   B 2 65  ? 27.448  -45.356 23.790  1.00 34.00  ?  65  THR   B N     1 
ATOM   1317 C CA    . THR   B 2 65  ? 28.493  -44.451 23.317  1.00 35.53  ?  65  THR   B CA    1 
ATOM   1318 C C     . THR   B 2 65  ? 28.271  -44.180 21.820  1.00 35.93  ?  65  THR   B C     1 
ATOM   1319 O O     . THR   B 2 65  ? 28.206  -45.132 21.036  1.00 35.40  ?  65  THR   B O     1 
ATOM   1320 C CB    . THR   B 2 65  ? 29.863  -45.113 23.514  1.00 35.55  ?  65  THR   B CB    1 
ATOM   1321 O OG1   . THR   B 2 65  ? 29.882  -45.637 24.839  1.00 35.46  ?  65  THR   B OG1   1 
ATOM   1322 C CG2   . THR   B 2 65  ? 31.015  -44.155 23.298  1.00 37.74  ?  65  THR   B CG2   1 
ATOM   1323 N N     . TYR   B 2 66  ? 28.210  -42.894 21.421  1.00 36.68  ?  66  TYR   B N     1 
ATOM   1324 C CA    . TYR   B 2 66  ? 28.083  -42.491 20.026  1.00 36.98  ?  66  TYR   B CA    1 
ATOM   1325 C C     . TYR   B 2 66  ? 29.464  -42.123 19.484  1.00 38.46  ?  66  TYR   B C     1 
ATOM   1326 O O     . TYR   B 2 66  ? 30.258  -41.535 20.197  1.00 38.18  ?  66  TYR   B O     1 
ATOM   1327 C CB    . TYR   B 2 66  ? 27.063  -41.360 19.936  1.00 38.00  ?  66  TYR   B CB    1 
ATOM   1328 C CG    . TYR   B 2 66  ? 25.657  -41.811 20.337  1.00 37.92  ?  66  TYR   B CG    1 
ATOM   1329 C CD1   . TYR   B 2 66  ? 24.923  -42.675 19.522  1.00 37.32  ?  66  TYR   B CD1   1 
ATOM   1330 C CD2   . TYR   B 2 66  ? 25.070  -41.408 21.538  1.00 38.15  ?  66  TYR   B CD2   1 
ATOM   1331 C CE1   . TYR   B 2 66  ? 23.632  -43.080 19.862  1.00 37.17  ?  66  TYR   B CE1   1 
ATOM   1332 C CE2   . TYR   B 2 66  ? 23.799  -41.820 21.904  1.00 38.22  ?  66  TYR   B CE2   1 
ATOM   1333 C CZ    . TYR   B 2 66  ? 23.072  -42.657 21.058  1.00 37.84  ?  66  TYR   B CZ    1 
ATOM   1334 O OH    . TYR   B 2 66  ? 21.819  -43.093 21.381  1.00 38.42  ?  66  TYR   B OH    1 
ATOM   1335 N N     . SER   B 2 67  ? 29.755  -42.522 18.237  1.00 39.20  ?  67  SER   B N     1 
ATOM   1336 C CA    . SER   B 2 67  ? 30.961  -42.081 17.541  1.00 41.17  ?  67  SER   B CA    1 
ATOM   1337 C C     . SER   B 2 67  ? 30.670  -42.016 16.031  1.00 41.80  ?  67  SER   B C     1 
ATOM   1338 O O     . SER   B 2 67  ? 29.446  -41.874 15.669  1.00 38.36  ?  67  SER   B O     1 
ATOM   1339 C CB    . SER   B 2 67  ? 32.131  -42.998 17.875  1.00 40.81  ?  67  SER   B CB    1 
ATOM   1340 O OG    . SER   B 2 67  ? 31.890  -44.314 17.384  1.00 40.72  ?  67  SER   B OG    1 
ATOM   1341 O OXT   . SER   B 2 67  ? 31.654  -42.168 15.261  1.00 41.31  ?  67  SER   B OXT   1 
ATOM   1342 N N     . SER   C 3 4   ? 9.910   -59.318 38.829  1.00 61.57  ?  4   SER   C N     1 
ATOM   1343 C CA    . SER   C 3 4   ? 10.514  -58.078 38.253  1.00 54.24  ?  4   SER   C CA    1 
ATOM   1344 C C     . SER   C 3 4   ? 10.834  -58.223 36.749  1.00 53.49  ?  4   SER   C C     1 
ATOM   1345 O O     . SER   C 3 4   ? 11.617  -57.414 36.230  1.00 53.73  ?  4   SER   C O     1 
ATOM   1346 C CB    . SER   C 3 4   ? 11.750  -57.597 39.086  1.00 49.84  ?  4   SER   C CB    1 
ATOM   1347 O OG    . SER   C 3 4   ? 11.940  -58.246 40.344  1.00 45.61  ?  4   SER   C OG    1 
ATOM   1348 N N     . VAL   C 3 5   ? 10.204  -59.189 36.027  1.00 49.26  ?  5   VAL   C N     1 
ATOM   1349 C CA    . VAL   C 3 5   ? 10.347  -59.357 34.577  1.00 52.78  ?  5   VAL   C CA    1 
ATOM   1350 C C     . VAL   C 3 5   ? 9.849   -58.114 33.811  1.00 51.98  ?  5   VAL   C C     1 
ATOM   1351 O O     . VAL   C 3 5   ? 10.524  -57.687 32.879  1.00 51.59  ?  5   VAL   C O     1 
ATOM   1352 C CB    . VAL   C 3 5   ? 9.645   -60.640 34.063  1.00 53.30  ?  5   VAL   C CB    1 
ATOM   1353 C CG1   . VAL   C 3 5   ? 8.111   -60.605 34.213  1.00 57.93  ?  5   VAL   C CG1   1 
ATOM   1354 C CG2   . VAL   C 3 5   ? 10.048  -60.983 32.626  1.00 48.44  ?  5   VAL   C CG2   1 
ATOM   1355 N N     . ASP   C 3 6   ? 8.709   -57.527 34.245  1.00 51.06  ?  6   ASP   C N     1 
ATOM   1356 C CA    . ASP   C 3 6   ? 8.109   -56.330 33.667  1.00 52.12  ?  6   ASP   C CA    1 
ATOM   1357 C C     . ASP   C 3 6   ? 8.851   -55.022 34.032  1.00 49.71  ?  6   ASP   C C     1 
ATOM   1358 O O     . ASP   C 3 6   ? 8.365   -53.969 33.617  1.00 52.39  ?  6   ASP   C O     1 
ATOM   1359 C CB    . ASP   C 3 6   ? 6.596   -56.300 33.924  1.00 54.22  ?  6   ASP   C CB    1 
ATOM   1360 C CG    . ASP   C 3 6   ? 6.112   -56.156 35.369  1.00 55.70  ?  6   ASP   C CG    1 
ATOM   1361 O OD1   . ASP   C 3 6   ? 6.937   -56.345 36.296  1.00 55.31  ?  6   ASP   C OD1   1 
ATOM   1362 O OD2   . ASP   C 3 6   ? 4.913   -55.854 35.565  1.00 57.96  -1 6   ASP   C OD2   1 
ATOM   1363 N N     . ASP   C 3 7   ? 10.008  -55.057 34.767  1.00 44.95  ?  7   ASP   C N     1 
ATOM   1364 C CA    . ASP   C 3 7   ? 11.047  -54.018 34.760  1.00 36.00  ?  7   ASP   C CA    1 
ATOM   1365 C C     . ASP   C 3 7   ? 12.011  -54.124 33.572  1.00 30.77  ?  7   ASP   C C     1 
ATOM   1366 O O     . ASP   C 3 7   ? 13.053  -53.434 33.543  1.00 31.40  ?  7   ASP   C O     1 
ATOM   1367 C CB    . ASP   C 3 7   ? 11.861  -53.997 36.055  1.00 37.92  ?  7   ASP   C CB    1 
ATOM   1368 C CG    . ASP   C 3 7   ? 11.046  -53.828 37.330  1.00 44.80  ?  7   ASP   C CG    1 
ATOM   1369 O OD1   . ASP   C 3 7   ? 9.834   -53.496 37.202  1.00 48.91  ?  7   ASP   C OD1   1 
ATOM   1370 O OD2   . ASP   C 3 7   ? 11.610  -54.064 38.439  1.00 43.78  -1 7   ASP   C OD2   1 
ATOM   1371 N N     . TYR   C 3 8   ? 11.702  -54.993 32.604  1.00 25.05  ?  8   TYR   C N     1 
ATOM   1372 C CA    . TYR   C 3 8   ? 12.329  -54.937 31.292  1.00 22.11  ?  8   TYR   C CA    1 
ATOM   1373 C C     . TYR   C 3 8   ? 12.027  -53.581 30.650  1.00 20.99  ?  8   TYR   C C     1 
ATOM   1374 O O     . TYR   C 3 8   ? 10.870  -53.174 30.659  1.00 20.51  ?  8   TYR   C O     1 
ATOM   1375 C CB    . TYR   C 3 8   ? 11.839  -56.110 30.430  1.00 19.76  ?  8   TYR   C CB    1 
ATOM   1376 C CG    . TYR   C 3 8   ? 12.185  -56.016 28.950  1.00 18.47  ?  8   TYR   C CG    1 
ATOM   1377 C CD1   . TYR   C 3 8   ? 13.509  -55.903 28.513  1.00 18.14  ?  8   TYR   C CD1   1 
ATOM   1378 C CD2   . TYR   C 3 8   ? 11.188  -55.965 27.995  1.00 17.81  ?  8   TYR   C CD2   1 
ATOM   1379 C CE1   . TYR   C 3 8   ? 13.823  -55.811 27.163  1.00 17.35  ?  8   TYR   C CE1   1 
ATOM   1380 C CE2   . TYR   C 3 8   ? 11.479  -55.873 26.650  1.00 17.31  ?  8   TYR   C CE2   1 
ATOM   1381 C CZ    . TYR   C 3 8   ? 12.799  -55.828 26.228  1.00 17.43  ?  8   TYR   C CZ    1 
ATOM   1382 O OH    . TYR   C 3 8   ? 13.032  -55.710 24.876  1.00 17.49  ?  8   TYR   C OH    1 
ATOM   1383 N N     . ASN   C 3 9   ? 13.054  -52.967 30.060  1.00 20.13  ?  9   ASN   C N     1 
ATOM   1384 C CA    . ASN   C 3 9   ? 12.955  -51.734 29.320  1.00 20.55  ?  9   ASN   C CA    1 
ATOM   1385 C C     . ASN   C 3 9   ? 13.374  -52.051 27.887  1.00 19.73  ?  9   ASN   C C     1 
ATOM   1386 O O     . ASN   C 3 9   ? 14.604  -52.064 27.594  1.00 21.78  ?  9   ASN   C O     1 
ATOM   1387 C CB    . ASN   C 3 9   ? 13.768  -50.631 29.985  1.00 22.24  ?  9   ASN   C CB    1 
ATOM   1388 C CG    . ASN   C 3 9   ? 13.508  -49.269 29.372  1.00 23.07  ?  9   ASN   C CG    1 
ATOM   1389 O OD1   . ASN   C 3 9   ? 12.983  -49.156 28.254  1.00 22.15  ?  9   ASN   C OD1   1 
ATOM   1390 N ND2   . ASN   C 3 9   ? 13.824  -48.228 30.119  1.00 23.97  ?  9   ASN   C ND2   1 
ATOM   1391 N N     . PRO   C 3 10  ? 12.406  -52.210 26.946  1.00 18.16  ?  10  PRO   C N     1 
ATOM   1392 C CA    . PRO   C 3 10  ? 12.728  -52.394 25.534  1.00 17.98  ?  10  PRO   C CA    1 
ATOM   1393 C C     . PRO   C 3 10  ? 13.382  -51.202 24.822  1.00 19.49  ?  10  PRO   C C     1 
ATOM   1394 O O     . PRO   C 3 10  ? 13.861  -51.427 23.706  1.00 19.56  ?  10  PRO   C O     1 
ATOM   1395 C CB    . PRO   C 3 10  ? 11.386  -52.744 24.879  1.00 17.30  ?  10  PRO   C CB    1 
ATOM   1396 C CG    . PRO   C 3 10  ? 10.369  -52.073 25.798  1.00 17.75  ?  10  PRO   C CG    1 
ATOM   1397 C CD    . PRO   C 3 10  ? 10.938  -52.160 27.163  1.00 18.10  ?  10  PRO   C CD    1 
ATOM   1398 N N     . ALA   C 3 11  ? 13.425  -49.992 25.427  1.00 19.70  ?  11  ALA   C N     1 
ATOM   1399 C CA    . ALA   C 3 11  ? 14.215  -48.904 24.875  1.00 20.96  ?  11  ALA   C CA    1 
ATOM   1400 C C     . ALA   C 3 11  ? 15.689  -49.259 24.746  1.00 21.57  ?  11  ALA   C C     1 
ATOM   1401 O O     . ALA   C 3 11  ? 16.319  -48.693 23.868  1.00 22.06  ?  11  ALA   C O     1 
ATOM   1402 C CB    . ALA   C 3 11  ? 14.106  -47.635 25.661  1.00 21.83  ?  11  ALA   C CB    1 
ATOM   1403 N N     . PHE   C 3 12  ? 16.205  -50.130 25.630  1.00 21.43  ?  12  PHE   C N     1 
ATOM   1404 C CA    . PHE   C 3 12  ? 17.584  -50.577 25.591  1.00 21.52  ?  12  PHE   C CA    1 
ATOM   1405 C C     . PHE   C 3 12  ? 17.665  -51.889 24.826  1.00 20.79  ?  12  PHE   C C     1 
ATOM   1406 O O     . PHE   C 3 12  ? 16.821  -52.811 24.938  1.00 18.12  ?  12  PHE   C O     1 
ATOM   1407 C CB    . PHE   C 3 12  ? 18.151  -50.713 26.992  1.00 22.39  ?  12  PHE   C CB    1 
ATOM   1408 C CG    . PHE   C 3 12  ? 18.195  -49.416 27.764  1.00 23.75  ?  12  PHE   C CG    1 
ATOM   1409 C CD1   . PHE   C 3 12  ? 19.263  -48.522 27.604  1.00 25.81  ?  12  PHE   C CD1   1 
ATOM   1410 C CD2   . PHE   C 3 12  ? 17.165  -49.088 28.661  1.00 24.32  ?  12  PHE   C CD2   1 
ATOM   1411 C CE1   . PHE   C 3 12  ? 19.310  -47.337 28.334  1.00 27.49  ?  12  PHE   C CE1   1 
ATOM   1412 C CE2   . PHE   C 3 12  ? 17.215  -47.901 29.389  1.00 25.65  ?  12  PHE   C CE2   1 
ATOM   1413 C CZ    . PHE   C 3 12  ? 18.291  -47.037 29.242  1.00 27.33  ?  12  PHE   C CZ    1 
ATOM   1414 N N     . ASP   C 3 13  ? 18.697  -51.944 23.963  1.00 21.42  ?  13  ASP   C N     1 
ATOM   1415 C CA    . ASP   C 3 13  ? 19.139  -53.184 23.369  1.00 20.98  ?  13  ASP   C CA    1 
ATOM   1416 C C     . ASP   C 3 13  ? 19.558  -54.131 24.506  1.00 20.70  ?  13  ASP   C C     1 
ATOM   1417 O O     . ASP   C 3 13  ? 20.119  -53.712 25.508  1.00 23.58  ?  13  ASP   C O     1 
ATOM   1418 C CB    . ASP   C 3 13  ? 20.262  -52.902 22.363  1.00 21.66  ?  13  ASP   C CB    1 
ATOM   1419 C CG    . ASP   C 3 13  ? 19.909  -52.038 21.150  1.00 21.77  ?  13  ASP   C CG    1 
ATOM   1420 O OD1   . ASP   C 3 13  ? 18.743  -51.972 20.755  1.00 21.52  ?  13  ASP   C OD1   1 
ATOM   1421 O OD2   . ASP   C 3 13  ? 20.801  -51.430 20.568  1.00 23.70  -1 13  ASP   C OD2   1 
ATOM   1422 N N     . ASN   C 3 14  ? 19.238  -55.407 24.352  1.00 19.77  ?  14  ASN   C N     1 
ATOM   1423 C CA    . ASN   C 3 14  ? 19.596  -56.451 25.276  1.00 20.03  ?  14  ASN   C CA    1 
ATOM   1424 C C     . ASN   C 3 14  ? 20.434  -57.470 24.511  1.00 20.48  ?  14  ASN   C C     1 
ATOM   1425 O O     . ASN   C 3 14  ? 20.023  -57.886 23.418  1.00 19.99  ?  14  ASN   C O     1 
ATOM   1426 C CB    . ASN   C 3 14  ? 18.347  -57.109 25.835  1.00 18.71  ?  14  ASN   C CB    1 
ATOM   1427 C CG    . ASN   C 3 14  ? 18.690  -58.065 26.962  1.00 18.56  ?  14  ASN   C CG    1 
ATOM   1428 O OD1   . ASN   C 3 14  ? 19.153  -59.186 26.728  1.00 17.68  ?  14  ASN   C OD1   1 
ATOM   1429 N ND2   . ASN   C 3 14  ? 18.401  -57.665 28.194  1.00 19.44  ?  14  ASN   C ND2   1 
ATOM   1430 N N     . THR   C 3 15  ? 21.545  -57.925 25.122  1.00 20.68  ?  15  THR   C N     1 
ATOM   1431 C CA    . THR   C 3 15  ? 22.472  -58.820 24.449  1.00 20.21  ?  15  THR   C CA    1 
ATOM   1432 C C     . THR   C 3 15  ? 21.959  -60.249 24.346  1.00 19.99  ?  15  THR   C C     1 
ATOM   1433 O O     . THR   C 3 15  ? 22.386  -60.931 23.440  1.00 20.04  ?  15  THR   C O     1 
ATOM   1434 C CB    . THR   C 3 15  ? 23.841  -58.737 25.109  1.00 20.83  ?  15  THR   C CB    1 
ATOM   1435 O OG1   . THR   C 3 15  ? 23.709  -59.021 26.507  1.00 20.50  ?  15  THR   C OG1   1 
ATOM   1436 C CG2   . THR   C 3 15  ? 24.447  -57.369 24.878  1.00 20.90  ?  15  THR   C CG2   1 
ATOM   1437 N N     . HIS   C 3 16  ? 21.028  -60.703 25.209  1.00 19.87  ?  16  HIS   C N     1 
ATOM   1438 C CA    . HIS   C 3 16  ? 20.554  -62.090 25.221  1.00 17.88  ?  16  HIS   C CA    1 
ATOM   1439 C C     . HIS   C 3 16  ? 19.115  -62.255 24.740  1.00 17.51  ?  16  HIS   C C     1 
ATOM   1440 O O     . HIS   C 3 16  ? 18.806  -63.389 24.382  1.00 17.55  ?  16  HIS   C O     1 
ATOM   1441 C CB    . HIS   C 3 16  ? 20.657  -62.665 26.623  1.00 17.88  ?  16  HIS   C CB    1 
ATOM   1442 C CG    . HIS   C 3 16  ? 22.074  -62.920 27.067  1.00 18.61  ?  16  HIS   C CG    1 
ATOM   1443 N ND1   . HIS   C 3 16  ? 22.388  -63.990 27.865  1.00 18.62  ?  16  HIS   C ND1   1 
ATOM   1444 C CD2   . HIS   C 3 16  ? 23.242  -62.280 26.872  1.00 19.61  ?  16  HIS   C CD2   1 
ATOM   1445 C CE1   . HIS   C 3 16  ? 23.702  -63.961 28.139  1.00 19.58  ?  16  HIS   C CE1   1 
ATOM   1446 N NE2   . HIS   C 3 16  ? 24.218  -62.897 27.616  1.00 19.38  ?  16  HIS   C NE2   1 
ATOM   1447 N N     . TYR   C 3 17  ? 18.254  -61.197 24.789  1.00 17.44  ?  17  TYR   C N     1 
ATOM   1448 C CA    . TYR   C 3 17  ? 16.808  -61.329 24.603  1.00 17.92  ?  17  TYR   C CA    1 
ATOM   1449 C C     . TYR   C 3 17  ? 16.324  -60.432 23.483  1.00 17.68  ?  17  TYR   C C     1 
ATOM   1450 O O     . TYR   C 3 17  ? 16.916  -59.374 23.240  1.00 19.35  ?  17  TYR   C O     1 
ATOM   1451 C CB    . TYR   C 3 17  ? 16.077  -60.991 25.904  1.00 18.49  ?  17  TYR   C CB    1 
ATOM   1452 C CG    . TYR   C 3 17  ? 16.452  -61.949 27.016  1.00 19.68  ?  17  TYR   C CG    1 
ATOM   1453 C CD1   . TYR   C 3 17  ? 15.895  -63.242 27.050  1.00 21.11  ?  17  TYR   C CD1   1 
ATOM   1454 C CD2   . TYR   C 3 17  ? 17.373  -61.603 28.008  1.00 20.47  ?  17  TYR   C CD2   1 
ATOM   1455 C CE1   . TYR   C 3 17  ? 16.250  -64.159 28.030  1.00 20.91  ?  17  TYR   C CE1   1 
ATOM   1456 C CE2   . TYR   C 3 17  ? 17.744  -62.520 28.980  1.00 21.10  ?  17  TYR   C CE2   1 
ATOM   1457 C CZ    . TYR   C 3 17  ? 17.162  -63.786 29.004  1.00 21.69  ?  17  TYR   C CZ    1 
ATOM   1458 O OH    . TYR   C 3 17  ? 17.441  -64.719 29.949  1.00 23.49  ?  17  TYR   C OH    1 
ATOM   1459 N N     . SER   C 3 18  ? 15.238  -60.868 22.826  1.00 17.82  ?  18  SER   C N     1 
ATOM   1460 C CA    . SER   C 3 18  ? 14.547  -60.066 21.825  1.00 17.79  ?  18  SER   C CA    1 
ATOM   1461 C C     . SER   C 3 18  ? 13.445  -59.202 22.449  1.00 16.72  ?  18  SER   C C     1 
ATOM   1462 O O     . SER   C 3 18  ? 12.828  -59.623 23.434  1.00 16.47  ?  18  SER   C O     1 
ATOM   1463 C CB    . SER   C 3 18  ? 13.982  -60.941 20.740  1.00 16.57  ?  18  SER   C CB    1 
ATOM   1464 O OG    . SER   C 3 18  ? 12.864  -61.687 21.177  1.00 16.03  ?  18  SER   C OG    1 
ATOM   1465 N N     . ARG   C 3 19  ? 13.130  -58.096 21.778  1.00 16.05  ?  19  ARG   C N     1 
ATOM   1466 C CA    . ARG   C 3 19  ? 11.948  -57.300 22.079  1.00 16.54  ?  19  ARG   C CA    1 
ATOM   1467 C C     . ARG   C 3 19  ? 10.692  -58.151 21.958  1.00 16.67  ?  19  ARG   C C     1 
ATOM   1468 O O     . ARG   C 3 19  ? 9.844   -58.124 22.850  1.00 15.51  ?  19  ARG   C O     1 
ATOM   1469 C CB    . ARG   C 3 19  ? 11.779  -56.041 21.208  1.00 17.15  ?  19  ARG   C CB    1 
ATOM   1470 C CG    . ARG   C 3 19  ? 12.468  -54.755 21.624  1.00 18.28  ?  19  ARG   C CG    1 
ATOM   1471 C CD    . ARG   C 3 19  ? 13.964  -54.723 21.436  1.00 18.75  ?  19  ARG   C CD    1 
ATOM   1472 N NE    . ARG   C 3 19  ? 14.505  -53.400 21.741  1.00 20.05  ?  19  ARG   C NE    1 
ATOM   1473 C CZ    . ARG   C 3 19  ? 15.698  -52.918 21.444  1.00 18.77  ?  19  ARG   C CZ    1 
ATOM   1474 N NH1   . ARG   C 3 19  ? 16.500  -53.663 20.752  1.00 18.78  1  19  ARG   C NH1   1 
ATOM   1475 N NH2   . ARG   C 3 19  ? 16.099  -51.719 21.855  1.00 18.34  ?  19  ARG   C NH2   1 
ATOM   1476 N N     . PHE   C 3 20  ? 10.591  -58.877 20.840  1.00 18.32  ?  20  PHE   C N     1 
ATOM   1477 C CA    . PHE   C 3 20  ? 9.464   -59.755 20.547  1.00 17.75  ?  20  PHE   C CA    1 
ATOM   1478 C C     . PHE   C 3 20  ? 9.168   -60.716 21.715  1.00 16.74  ?  20  PHE   C C     1 
ATOM   1479 O O     . PHE   C 3 20  ? 8.039   -60.699 22.174  1.00 16.23  ?  20  PHE   C O     1 
ATOM   1480 C CB    . PHE   C 3 20  ? 9.709   -60.498 19.224  1.00 18.21  ?  20  PHE   C CB    1 
ATOM   1481 C CG    . PHE   C 3 20  ? 8.613   -61.498 18.912  1.00 18.27  ?  20  PHE   C CG    1 
ATOM   1482 C CD1   . PHE   C 3 20  ? 7.347   -61.051 18.471  1.00 18.87  ?  20  PHE   C CD1   1 
ATOM   1483 C CD2   . PHE   C 3 20  ? 8.822   -62.874 19.102  1.00 18.14  ?  20  PHE   C CD2   1 
ATOM   1484 C CE1   . PHE   C 3 20  ? 6.305   -61.973 18.242  1.00 18.97  ?  20  PHE   C CE1   1 
ATOM   1485 C CE2   . PHE   C 3 20  ? 7.781   -63.788 18.873  1.00 18.47  ?  20  PHE   C CE2   1 
ATOM   1486 C CZ    . PHE   C 3 20  ? 6.532   -63.341 18.454  1.00 18.39  ?  20  PHE   C CZ    1 
ATOM   1487 N N     . HIS   C 3 21  ? 10.155  -61.517 22.169  1.00 16.40  ?  21  HIS   C N     1 
ATOM   1488 C CA    . HIS   C 3 21  ? 9.990   -62.481 23.248  1.00 16.62  ?  21  HIS   C CA    1 
ATOM   1489 C C     . HIS   C 3 21  ? 9.523   -61.771 24.530  1.00 16.51  ?  21  HIS   C C     1 
ATOM   1490 O O     . HIS   C 3 21  ? 8.462   -62.083 25.041  1.00 16.19  ?  21  HIS   C O     1 
ATOM   1491 C CB    . HIS   C 3 21  ? 11.233  -63.397 23.433  1.00 16.23  ?  21  HIS   C CB    1 
ATOM   1492 C CG    . HIS   C 3 21  ? 11.289  -64.121 24.759  1.00 16.28  ?  21  HIS   C CG    1 
ATOM   1493 N ND1   . HIS   C 3 21  ? 12.480  -64.249 25.431  1.00 16.13  ?  21  HIS   C ND1   1 
ATOM   1494 C CD2   . HIS   C 3 21  ? 10.336  -64.611 25.619  1.00 15.40  ?  21  HIS   C CD2   1 
ATOM   1495 C CE1   . HIS   C 3 21  ? 12.275  -64.781 26.613  1.00 15.87  ?  21  HIS   C CE1   1 
ATOM   1496 N NE2   . HIS   C 3 21  ? 10.982  -65.012 26.739  1.00 16.56  ?  21  HIS   C NE2   1 
ATOM   1497 N N     . LEU   C 3 22  ? 10.327  -60.836 25.066  1.00 17.47  ?  22  LEU   C N     1 
ATOM   1498 C CA    . LEU   C 3 22  ? 10.007  -60.227 26.368  1.00 18.25  ?  22  LEU   C CA    1 
ATOM   1499 C C     . LEU   C 3 22  ? 8.723   -59.384 26.320  1.00 18.39  ?  22  LEU   C C     1 
ATOM   1500 O O     . LEU   C 3 22  ? 8.035   -59.349 27.315  1.00 19.21  ?  22  LEU   C O     1 
ATOM   1501 C CB    . LEU   C 3 22  ? 11.196  -59.437 26.905  1.00 19.46  ?  22  LEU   C CB    1 
ATOM   1502 C CG    . LEU   C 3 22  ? 12.495  -60.236 27.135  1.00 18.46  ?  22  LEU   C CG    1 
ATOM   1503 C CD1   . LEU   C 3 22  ? 13.591  -59.349 27.770  1.00 18.24  ?  22  LEU   C CD1   1 
ATOM   1504 C CD2   . LEU   C 3 22  ? 12.308  -61.474 27.948  1.00 18.03  ?  22  LEU   C CD2   1 
ATOM   1505 N N     . LEU   C 3 23  ? 8.382   -58.734 25.191  1.00 18.56  ?  23  LEU   C N     1 
ATOM   1506 C CA    . LEU   C 3 23  ? 7.123   -57.995 25.068  1.00 19.08  ?  23  LEU   C CA    1 
ATOM   1507 C C     . LEU   C 3 23  ? 5.906   -58.923 25.038  1.00 17.57  ?  23  LEU   C C     1 
ATOM   1508 O O     . LEU   C 3 23  ? 4.949   -58.643 25.762  1.00 17.07  ?  23  LEU   C O     1 
ATOM   1509 C CB    . LEU   C 3 23  ? 7.123   -56.977 23.923  1.00 20.21  ?  23  LEU   C CB    1 
ATOM   1510 C CG    . LEU   C 3 23  ? 8.105   -55.804 24.077  1.00 19.96  ?  23  LEU   C CG    1 
ATOM   1511 C CD1   . LEU   C 3 23  ? 8.169   -55.029 22.800  1.00 20.12  ?  23  LEU   C CD1   1 
ATOM   1512 C CD2   . LEU   C 3 23  ? 7.721   -54.933 25.216  1.00 22.01  ?  23  LEU   C CD2   1 
ATOM   1513 N N     . ILE   C 3 24  ? 5.942   -60.049 24.286  1.00 17.49  ?  24  ILE   C N     1 
ATOM   1514 C CA    . ILE   C 3 24  ? 4.839   -61.006 24.331  1.00 17.34  ?  24  ILE   C CA    1 
ATOM   1515 C C     . ILE   C 3 24  ? 4.712   -61.673 25.720  1.00 17.08  ?  24  ILE   C C     1 
ATOM   1516 O O     . ILE   C 3 24  ? 3.590   -61.920 26.178  1.00 14.84  ?  24  ILE   C O     1 
ATOM   1517 C CB    . ILE   C 3 24  ? 4.835   -62.011 23.166  1.00 17.24  ?  24  ILE   C CB    1 
ATOM   1518 C CG1   . ILE   C 3 24  ? 5.976   -63.045 23.213  1.00 16.84  ?  24  ILE   C CG1   1 
ATOM   1519 C CG2   . ILE   C 3 24  ? 4.719   -61.249 21.835  1.00 17.50  ?  24  ILE   C CG2   1 
ATOM   1520 C CD1   . ILE   C 3 24  ? 5.885   -64.090 22.115  1.00 17.18  ?  24  ILE   C CD1   1 
ATOM   1521 N N     . GLU   C 3 25  ? 5.839   -61.856 26.418  1.00 15.61  ?  25  GLU   C N     1 
ATOM   1522 C CA    . GLU   C 3 25  ? 5.867   -62.512 27.700  1.00 17.28  ?  25  GLU   C CA    1 
ATOM   1523 C C     . GLU   C 3 25  ? 5.367   -61.607 28.815  1.00 16.80  ?  25  GLU   C C     1 
ATOM   1524 O O     . GLU   C 3 25  ? 4.468   -62.016 29.542  1.00 17.83  ?  25  GLU   C O     1 
ATOM   1525 C CB    . GLU   C 3 25  ? 7.265   -63.082 27.985  1.00 18.35  ?  25  GLU   C CB    1 
ATOM   1526 C CG    . GLU   C 3 25  ? 7.202   -64.115 29.111  1.00 19.55  ?  25  GLU   C CG    1 
ATOM   1527 C CD    . GLU   C 3 25  ? 8.605   -64.618 29.323  1.00 20.64  ?  25  GLU   C CD    1 
ATOM   1528 O OE1   . GLU   C 3 25  ? 9.023   -65.509 28.537  1.00 19.56  ?  25  GLU   C OE1   1 
ATOM   1529 O OE2   . GLU   C 3 25  ? 9.258   -63.924 30.140  1.00 21.60  -1 25  GLU   C OE2   1 
ATOM   1530 N N     . THR   C 3 26  ? 5.871   -60.365 28.887  1.00 17.01  ?  26  THR   C N     1 
ATOM   1531 C CA    . THR   C 3 26  ? 5.444   -59.392 29.885  1.00 17.24  ?  26  THR   C CA    1 
ATOM   1532 C C     . THR   C 3 26  ? 4.005   -58.941 29.653  1.00 17.24  ?  26  THR   C C     1 
ATOM   1533 O O     . THR   C 3 26  ? 3.409   -58.441 30.589  1.00 17.29  ?  26  THR   C O     1 
ATOM   1534 C CB    . THR   C 3 26  ? 6.393   -58.205 29.942  1.00 19.33  ?  26  THR   C CB    1 
ATOM   1535 O OG1   . THR   C 3 26  ? 6.510   -57.631 28.635  1.00 18.22  ?  26  THR   C OG1   1 
ATOM   1536 C CG2   . THR   C 3 26  ? 7.797   -58.588 30.416  1.00 20.28  ?  26  THR   C CG2   1 
ATOM   1537 N N     . ASN   C 3 27  ? 3.464   -59.063 28.435  1.00 16.39  ?  27  ASN   C N     1 
ATOM   1538 C CA    . ASN   C 3 27  ? 2.062   -58.763 28.193  1.00 17.99  ?  27  ASN   C CA    1 
ATOM   1539 C C     . ASN   C 3 27  ? 1.146   -59.978 28.276  1.00 18.32  ?  27  ASN   C C     1 
ATOM   1540 O O     . ASN   C 3 27  ? 0.020   -59.851 27.812  1.00 19.52  ?  27  ASN   C O     1 
ATOM   1541 C CB    . ASN   C 3 27  ? 1.947   -57.977 26.886  1.00 18.59  ?  27  ASN   C CB    1 
ATOM   1542 C CG    . ASN   C 3 27  ? 2.491   -56.576 27.044  1.00 17.96  ?  27  ASN   C CG    1 
ATOM   1543 O OD1   . ASN   C 3 27  ? 1.804   -55.766 27.638  1.00 19.63  ?  27  ASN   C OD1   1 
ATOM   1544 N ND2   . ASN   C 3 27  ? 3.695   -56.291 26.588  1.00 16.91  ?  27  ASN   C ND2   1 
ATOM   1545 N N     . GLY   C 3 28  ? 1.593   -61.137 28.819  1.00 18.90  ?  28  GLY   C N     1 
ATOM   1546 C CA    . GLY   C 3 28  ? 0.790   -62.334 29.029  1.00 19.64  ?  28  GLY   C CA    1 
ATOM   1547 C C     . GLY   C 3 28  ? 0.215   -62.972 27.757  1.00 20.84  ?  28  GLY   C C     1 
ATOM   1548 O O     . GLY   C 3 28  ? -0.889  -63.517 27.805  1.00 20.19  ?  28  GLY   C O     1 
ATOM   1549 N N     . ILE   C 3 29  ? 0.899   -62.837 26.607  1.00 19.77  ?  29  ILE   C N     1 
ATOM   1550 C CA    . ILE   C 3 29  ? 0.492   -63.487 25.359  1.00 19.74  ?  29  ILE   C CA    1 
ATOM   1551 C C     . ILE   C 3 29  ? 0.996   -64.935 25.391  1.00 19.48  ?  29  ILE   C C     1 
ATOM   1552 O O     . ILE   C 3 29  ? 0.340   -65.841 24.859  1.00 20.26  ?  29  ILE   C O     1 
ATOM   1553 C CB    . ILE   C 3 29  ? 0.987   -62.652 24.146  1.00 20.09  ?  29  ILE   C CB    1 
ATOM   1554 C CG1   . ILE   C 3 29  ? 0.249   -61.295 24.100  1.00 21.26  ?  29  ILE   C CG1   1 
ATOM   1555 C CG2   . ILE   C 3 29  ? 0.872   -63.411 22.815  1.00 19.24  ?  29  ILE   C CG2   1 
ATOM   1556 C CD1   . ILE   C 3 29  ? 0.883   -60.198 23.257  1.00 22.54  ?  29  ILE   C CD1   1 
ATOM   1557 N N     . THR   C 3 30  ? 2.188   -65.148 25.988  1.00 17.55  ?  30  THR   C N     1 
ATOM   1558 C CA    . THR   C 3 30  ? 2.742   -66.451 26.266  1.00 16.44  ?  30  THR   C CA    1 
ATOM   1559 C C     . THR   C 3 30  ? 2.556   -66.779 27.748  1.00 17.41  ?  30  THR   C C     1 
ATOM   1560 O O     . THR   C 3 30  ? 2.404   -65.899 28.594  1.00 17.46  ?  30  THR   C O     1 
ATOM   1561 C CB    . THR   C 3 30  ? 4.211   -66.487 25.862  1.00 15.95  ?  30  THR   C CB    1 
ATOM   1562 O OG1   . THR   C 3 30  ? 4.824   -65.638 26.806  1.00 15.14  ?  30  THR   C OG1   1 
ATOM   1563 C CG2   . THR   C 3 30  ? 4.404   -66.015 24.446  1.00 16.09  ?  30  THR   C CG2   1 
ATOM   1564 N N     . LYS   C 3 31  ? 2.556   -68.092 28.049  1.00 18.32  ?  31  LYS   C N     1 
ATOM   1565 C CA    . LYS   C 3 31  ? 2.329   -68.614 29.395  1.00 18.69  ?  31  LYS   C CA    1 
ATOM   1566 C C     . LYS   C 3 31  ? 3.395   -69.673 29.652  1.00 17.71  ?  31  LYS   C C     1 
ATOM   1567 O O     . LYS   C 3 31  ? 3.109   -70.853 29.441  1.00 18.09  ?  31  LYS   C O     1 
ATOM   1568 C CB    . LYS   C 3 31  ? 0.868   -69.025 29.493  1.00 19.42  ?  31  LYS   C CB    1 
ATOM   1569 C CG    . LYS   C 3 31  ? -0.164  -67.919 29.451  1.00 21.46  ?  31  LYS   C CG    1 
ATOM   1570 C CD    . LYS   C 3 31  ? -0.129  -66.988 30.659  1.00 22.62  ?  31  LYS   C CD    1 
ATOM   1571 C CE    . LYS   C 3 31  ? -1.154  -65.938 30.567  1.00 23.14  ?  31  LYS   C CE    1 
ATOM   1572 N NZ    . LYS   C 3 31  ? -1.078  -64.926 31.639  1.00 24.10  1  31  LYS   C NZ    1 
ATOM   1573 N N     . PRO   C 3 32  ? 4.667   -69.299 29.980  1.00 17.35  ?  32  PRO   C N     1 
ATOM   1574 C CA    . PRO   C 3 32  ? 5.694   -70.305 30.259  1.00 17.63  ?  32  PRO   C CA    1 
ATOM   1575 C C     . PRO   C 3 32  ? 5.402   -71.169 31.493  1.00 18.94  ?  32  PRO   C C     1 
ATOM   1576 O O     . PRO   C 3 32  ? 4.943   -70.648 32.509  1.00 20.47  ?  32  PRO   C O     1 
ATOM   1577 C CB    . PRO   C 3 32  ? 6.971   -69.505 30.444  1.00 17.72  ?  32  PRO   C CB    1 
ATOM   1578 C CG    . PRO   C 3 32  ? 6.674   -68.083 29.979  1.00 16.78  ?  32  PRO   C CG    1 
ATOM   1579 C CD    . PRO   C 3 32  ? 5.179   -67.928 30.118  1.00 17.00  ?  32  PRO   C CD    1 
ATOM   1580 N N     . CYS   C 3 33  ? 5.633   -72.493 31.354  1.00 19.92  ?  33  CYS   C N     1 
ATOM   1581 C CA    . CYS   C 3 33  ? 5.648   -73.472 32.423  1.00 19.91  ?  33  CYS   C CA    1 
ATOM   1582 C C     . CYS   C 3 33  ? 7.010   -74.163 32.437  1.00 19.51  ?  33  CYS   C C     1 
ATOM   1583 O O     . CYS   C 3 33  ? 7.379   -74.667 31.392  1.00 19.35  ?  33  CYS   C O     1 
ATOM   1584 C CB    . CYS   C 3 33  ? 4.553   -74.481 32.109  1.00 20.15  ?  33  CYS   C CB    1 
ATOM   1585 S SG    . CYS   C 3 33  ? 4.305   -75.701 33.400  1.00 20.99  ?  33  CYS   C SG    1 
ATOM   1586 N N     . ILE   C 3 34  ? 7.723   -74.158 33.575  1.00 20.04  ?  34  ILE   C N     1 
ATOM   1587 C CA    . ILE   C 3 34  ? 8.984   -74.868 33.780  1.00 20.96  ?  34  ILE   C CA    1 
ATOM   1588 C C     . ILE   C 3 34  ? 8.682   -76.159 34.524  1.00 21.13  ?  34  ILE   C C     1 
ATOM   1589 O O     . ILE   C 3 34  ? 8.089   -76.129 35.597  1.00 21.58  ?  34  ILE   C O     1 
ATOM   1590 C CB    . ILE   C 3 34  ? 10.024  -74.046 34.562  1.00 22.32  ?  34  ILE   C CB    1 
ATOM   1591 C CG1   . ILE   C 3 34  ? 10.230  -72.654 33.992  1.00 23.82  ?  34  ILE   C CG1   1 
ATOM   1592 C CG2   . ILE   C 3 34  ? 11.338  -74.813 34.736  1.00 23.46  ?  34  ILE   C CG2   1 
ATOM   1593 C CD1   . ILE   C 3 34  ? 10.585  -72.555 32.526  1.00 23.60  ?  34  ILE   C CD1   1 
ATOM   1594 N N     . VAL   C 3 35  ? 9.169   -77.287 33.997  1.00 22.22  ?  35  VAL   C N     1 
ATOM   1595 C CA    . VAL   C 3 35  ? 9.101   -78.601 34.664  1.00 23.52  ?  35  VAL   C CA    1 
ATOM   1596 C C     . VAL   C 3 35  ? 10.539  -79.029 34.923  1.00 24.05  ?  35  VAL   C C     1 
ATOM   1597 O O     . VAL   C 3 35  ? 11.288  -79.148 33.975  1.00 22.48  ?  35  VAL   C O     1 
ATOM   1598 C CB    . VAL   C 3 35  ? 8.335   -79.641 33.814  1.00 24.04  ?  35  VAL   C CB    1 
ATOM   1599 C CG1   . VAL   C 3 35  ? 8.102   -80.951 34.569  1.00 25.52  ?  35  VAL   C CG1   1 
ATOM   1600 C CG2   . VAL   C 3 35  ? 6.994   -79.085 33.326  1.00 24.69  ?  35  VAL   C CG2   1 
ATOM   1601 N N     . SER   C 3 36  ? 10.912  -79.178 36.202  1.00 26.67  ?  36  SER   C N     1 
ATOM   1602 C CA    . SER   C 3 36  ? 12.122  -79.875 36.633  1.00 29.05  ?  36  SER   C CA    1 
ATOM   1603 C C     . SER   C 3 36  ? 11.793  -81.341 36.938  1.00 31.08  ?  36  SER   C C     1 
ATOM   1604 O O     . SER   C 3 36  ? 10.654  -81.786 36.819  1.00 31.26  ?  36  SER   C O     1 
ATOM   1605 C CB    . SER   C 3 36  ? 12.735  -79.158 37.830  1.00 30.14  ?  36  SER   C CB    1 
ATOM   1606 O OG    . SER   C 3 36  ? 11.948  -79.315 39.013  1.00 31.28  ?  36  SER   C OG    1 
ATOM   1607 N N     . THR   C 3 37  ? 12.818  -82.094 37.371  1.00 32.89  ?  37  THR   C N     1 
ATOM   1608 C CA    . THR   C 3 37  ? 12.670  -83.444 37.889  1.00 32.89  ?  37  THR   C CA    1 
ATOM   1609 C C     . THR   C 3 37  ? 11.853  -83.470 39.186  1.00 32.47  ?  37  THR   C C     1 
ATOM   1610 O O     . THR   C 3 37  ? 11.356  -84.533 39.492  1.00 32.60  ?  37  THR   C O     1 
ATOM   1611 C CB    . THR   C 3 37  ? 14.040  -84.115 38.082  1.00 34.41  ?  37  THR   C CB    1 
ATOM   1612 O OG1   . THR   C 3 37  ? 14.847  -83.311 38.946  1.00 33.75  ?  37  THR   C OG1   1 
ATOM   1613 C CG2   . THR   C 3 37  ? 14.713  -84.346 36.741  1.00 34.28  ?  37  THR   C CG2   1 
ATOM   1614 N N     . GLU   C 3 38  ? 11.780  -82.352 39.949  1.00 32.23  ?  38  GLU   C N     1 
ATOM   1615 C CA    . GLU   C 3 38  ? 11.161  -82.283 41.267  1.00 32.17  ?  38  GLU   C CA    1 
ATOM   1616 C C     . GLU   C 3 38  ? 9.898   -81.426 41.316  1.00 29.69  ?  38  GLU   C C     1 
ATOM   1617 O O     . GLU   C 3 38  ? 9.124   -81.630 42.242  1.00 28.66  ?  38  GLU   C O     1 
ATOM   1618 C CB    . GLU   C 3 38  ? 12.209  -81.736 42.233  1.00 34.24  ?  38  GLU   C CB    1 
ATOM   1619 C CG    . GLU   C 3 38  ? 13.415  -82.666 42.376  1.00 37.33  ?  38  GLU   C CG    1 
ATOM   1620 C CD    . GLU   C 3 38  ? 14.444  -82.249 43.420  1.00 40.62  ?  38  GLU   C CD    1 
ATOM   1621 O OE1   . GLU   C 3 38  ? 14.187  -81.342 44.282  1.00 41.69  ?  38  GLU   C OE1   1 
ATOM   1622 O OE2   . GLU   C 3 38  ? 15.572  -82.814 43.297  1.00 42.10  -1 38  GLU   C OE2   1 
ATOM   1623 N N     . ASN   C 3 39  ? 9.703   -80.437 40.407  1.00 28.54  ?  39  ASN   C N     1 
ATOM   1624 C CA    . ASN   C 3 39  ? 8.680   -79.392 40.548  1.00 26.94  ?  39  ASN   C CA    1 
ATOM   1625 C C     . ASN   C 3 39  ? 8.174   -78.917 39.184  1.00 26.01  ?  39  ASN   C C     1 
ATOM   1626 O O     . ASN   C 3 39  ? 8.979   -78.814 38.245  1.00 24.99  ?  39  ASN   C O     1 
ATOM   1627 C CB    . ASN   C 3 39  ? 9.195   -78.142 41.234  1.00 26.69  ?  39  ASN   C CB    1 
ATOM   1628 C CG    . ASN   C 3 39  ? 9.548   -78.361 42.672  1.00 28.90  ?  39  ASN   C CG    1 
ATOM   1629 O OD1   . ASN   C 3 39  ? 8.650   -78.582 43.494  1.00 30.49  ?  39  ASN   C OD1   1 
ATOM   1630 N ND2   . ASN   C 3 39  ? 10.841  -78.307 42.976  1.00 28.85  ?  39  ASN   C ND2   1 
ATOM   1631 N N     . VAL   C 3 40  ? 6.856   -78.575 39.122  1.00 24.54  ?  40  VAL   C N     1 
ATOM   1632 C CA    . VAL   C 3 40  ? 6.256   -77.834 38.021  1.00 23.01  ?  40  VAL   C CA    1 
ATOM   1633 C C     . VAL   C 3 40  ? 6.081   -76.381 38.494  1.00 22.39  ?  40  VAL   C C     1 
ATOM   1634 O O     . VAL   C 3 40  ? 5.417   -76.167 39.509  1.00 22.89  ?  40  VAL   C O     1 
ATOM   1635 C CB    . VAL   C 3 40  ? 4.916   -78.461 37.574  1.00 22.47  ?  40  VAL   C CB    1 
ATOM   1636 C CG1   . VAL   C 3 40  ? 4.310   -77.653 36.424  1.00 21.47  ?  40  VAL   C CG1   1 
ATOM   1637 C CG2   . VAL   C 3 40  ? 5.047   -79.925 37.159  1.00 23.44  ?  40  VAL   C CG2   1 
ATOM   1638 N N     . TYR   C 3 41  ? 6.675   -75.414 37.781  1.00 20.83  ?  41  TYR   C N     1 
ATOM   1639 C CA    . TYR   C 3 41  ? 6.522   -73.971 38.024  1.00 21.30  ?  41  TYR   C CA    1 
ATOM   1640 C C     . TYR   C 3 41  ? 5.454   -73.461 37.056  1.00 20.75  ?  41  TYR   C C     1 
ATOM   1641 O O     . TYR   C 3 41  ? 5.723   -73.360 35.862  1.00 20.57  ?  41  TYR   C O     1 
ATOM   1642 C CB    . TYR   C 3 41  ? 7.869   -73.237 37.887  1.00 20.70  ?  41  TYR   C CB    1 
ATOM   1643 C CG    . TYR   C 3 41  ? 8.915   -73.780 38.857  1.00 22.48  ?  41  TYR   C CG    1 
ATOM   1644 C CD1   . TYR   C 3 41  ? 9.688   -74.902 38.544  1.00 23.59  ?  41  TYR   C CD1   1 
ATOM   1645 C CD2   . TYR   C 3 41  ? 9.031   -73.252 40.139  1.00 23.62  ?  41  TYR   C CD2   1 
ATOM   1646 C CE1   . TYR   C 3 41  ? 10.608  -75.427 39.449  1.00 25.33  ?  41  TYR   C CE1   1 
ATOM   1647 C CE2   . TYR   C 3 41  ? 9.890   -73.811 41.073  1.00 25.76  ?  41  TYR   C CE2   1 
ATOM   1648 C CZ    . TYR   C 3 41  ? 10.704  -74.883 40.727  1.00 26.93  ?  41  TYR   C CZ    1 
ATOM   1649 O OH    . TYR   C 3 41  ? 11.534  -75.392 41.718  1.00 29.58  ?  41  TYR   C OH    1 
ATOM   1650 N N     . THR   C 3 42  ? 4.227   -73.250 37.548  1.00 22.55  ?  42  THR   C N     1 
ATOM   1651 C CA    . THR   C 3 42  ? 3.077   -72.969 36.680  1.00 23.36  ?  42  THR   C CA    1 
ATOM   1652 C C     . THR   C 3 42  ? 3.172   -71.538 36.146  1.00 23.62  ?  42  THR   C C     1 
ATOM   1653 O O     . THR   C 3 42  ? 3.789   -70.696 36.799  1.00 26.22  ?  42  THR   C O     1 
ATOM   1654 C CB    . THR   C 3 42  ? 1.736   -73.183 37.393  1.00 24.55  ?  42  THR   C CB    1 
ATOM   1655 O OG1   . THR   C 3 42  ? 1.559   -72.200 38.403  1.00 25.13  ?  42  THR   C OG1   1 
ATOM   1656 C CG2   . THR   C 3 42  ? 1.591   -74.595 37.927  1.00 25.48  ?  42  THR   C CG2   1 
ATOM   1657 N N     . PRO   C 3 43  ? 2.534   -71.202 34.990  1.00 24.25  ?  43  PRO   C N     1 
ATOM   1658 C CA    . PRO   C 3 43  ? 2.394   -69.816 34.545  1.00 23.43  ?  43  PRO   C CA    1 
ATOM   1659 C C     . PRO   C 3 43  ? 1.544   -68.930 35.456  1.00 24.46  ?  43  PRO   C C     1 
ATOM   1660 O O     . PRO   C 3 43  ? 1.746   -67.735 35.391  1.00 25.48  ?  43  PRO   C O     1 
ATOM   1661 C CB    . PRO   C 3 43  ? 1.797   -69.909 33.141  1.00 22.57  ?  43  PRO   C CB    1 
ATOM   1662 C CG    . PRO   C 3 43  ? 1.254   -71.293 33.022  1.00 23.13  ?  43  PRO   C CG    1 
ATOM   1663 C CD    . PRO   C 3 43  ? 1.962   -72.146 34.006  1.00 24.01  ?  43  PRO   C CD    1 
ATOM   1664 N N     . ASP   C 3 44  ? 0.660   -69.522 36.297  1.00 26.88  ?  44  ASP   C N     1 
ATOM   1665 C CA    . ASP   C 3 44  ? -0.092  -68.849 37.344  1.00 28.51  ?  44  ASP   C CA    1 
ATOM   1666 C C     . ASP   C 3 44  ? 0.711   -68.621 38.637  1.00 27.96  ?  44  ASP   C C     1 
ATOM   1667 O O     . ASP   C 3 44  ? 0.120   -68.179 39.600  1.00 30.26  ?  44  ASP   C O     1 
ATOM   1668 C CB    . ASP   C 3 44  ? -1.421  -69.586 37.555  1.00 31.94  ?  44  ASP   C CB    1 
ATOM   1669 C CG    . ASP   C 3 44  ? -2.541  -68.848 38.291  1.00 35.84  ?  44  ASP   C CG    1 
ATOM   1670 O OD1   . ASP   C 3 44  ? -2.664  -67.612 38.088  1.00 38.75  ?  44  ASP   C OD1   1 
ATOM   1671 O OD2   . ASP   C 3 44  ? -3.281  -69.500 39.079  1.00 40.81  -1 44  ASP   C OD2   1 
ATOM   1672 N N     . ASN   C 3 45  ? 2.026   -68.850 38.670  1.00 27.67  ?  45  ASN   C N     1 
ATOM   1673 C CA    . ASN   C 3 45  ? 2.960   -68.548 39.752  1.00 29.09  ?  45  ASN   C CA    1 
ATOM   1674 C C     . ASN   C 3 45  ? 2.768   -69.488 40.948  1.00 29.82  ?  45  ASN   C C     1 
ATOM   1675 O O     . ASN   C 3 45  ? 2.869   -69.049 42.084  1.00 32.99  ?  45  ASN   C O     1 
ATOM   1676 C CB    . ASN   C 3 45  ? 3.054   -67.062 40.113  1.00 31.19  ?  45  ASN   C CB    1 
ATOM   1677 C CG    . ASN   C 3 45  ? 4.323   -66.716 40.881  1.00 32.37  ?  45  ASN   C CG    1 
ATOM   1678 O OD1   . ASN   C 3 45  ? 5.389   -67.293 40.634  1.00 35.36  ?  45  ASN   C OD1   1 
ATOM   1679 N ND2   . ASN   C 3 45  ? 4.251   -65.830 41.866  1.00 35.44  ?  45  ASN   C ND2   1 
ATOM   1680 N N     . ALA   C 3 46  ? 2.548   -70.797 40.686  1.00 29.10  ?  46  ALA   C N     1 
ATOM   1681 C CA    . ALA   C 3 46  ? 2.557   -71.834 41.712  1.00 29.50  ?  46  ALA   C CA    1 
ATOM   1682 C C     . ALA   C 3 46  ? 3.700   -72.830 41.427  1.00 28.28  ?  46  ALA   C C     1 
ATOM   1683 O O     . ALA   C 3 46  ? 3.936   -73.188 40.276  1.00 25.65  ?  46  ALA   C O     1 
ATOM   1684 C CB    . ALA   C 3 46  ? 1.200   -72.502 41.789  1.00 30.35  ?  46  ALA   C CB    1 
ATOM   1685 N N     . THR   C 3 47  ? 4.409   -73.243 42.497  1.00 29.30  ?  47  THR   C N     1 
ATOM   1686 C CA    . THR   C 3 47  ? 5.356   -74.356 42.509  1.00 30.35  ?  47  THR   C CA    1 
ATOM   1687 C C     . THR   C 3 47  ? 4.592   -75.617 42.927  1.00 30.11  ?  47  THR   C C     1 
ATOM   1688 O O     . THR   C 3 47  ? 4.210   -75.670 44.078  1.00 32.95  ?  47  THR   C O     1 
ATOM   1689 C CB    . THR   C 3 47  ? 6.493   -74.021 43.489  1.00 32.04  ?  47  THR   C CB    1 
ATOM   1690 O OG1   . THR   C 3 47  ? 7.141   -72.850 43.007  1.00 30.54  ?  47  THR   C OG1   1 
ATOM   1691 C CG2   . THR   C 3 47  ? 7.553   -75.116 43.617  1.00 33.19  ?  47  THR   C CG2   1 
ATOM   1692 N N     . VAL   C 3 48  ? 4.330   -76.579 42.007  1.00 28.71  ?  48  VAL   C N     1 
ATOM   1693 C CA    . VAL   C 3 48  ? 3.663   -77.857 42.301  1.00 29.53  ?  48  VAL   C CA    1 
ATOM   1694 C C     . VAL   C 3 48  ? 4.766   -78.926 42.367  1.00 29.77  ?  48  VAL   C C     1 
ATOM   1695 O O     . VAL   C 3 48  ? 5.326   -79.247 41.313  1.00 27.46  ?  48  VAL   C O     1 
ATOM   1696 C CB    . VAL   C 3 48  ? 2.577   -78.255 41.269  1.00 28.42  ?  48  VAL   C CB    1 
ATOM   1697 C CG1   . VAL   C 3 48  ? 1.895   -79.593 41.580  1.00 29.40  ?  48  VAL   C CG1   1 
ATOM   1698 C CG2   . VAL   C 3 48  ? 1.502   -77.181 41.087  1.00 28.38  ?  48  VAL   C CG2   1 
ATOM   1699 N N     . PRO   C 3 49  ? 5.142   -79.478 43.560  1.00 30.91  ?  49  PRO   C N     1 
ATOM   1700 C CA    . PRO   C 3 49  ? 6.060   -80.622 43.639  1.00 31.68  ?  49  PRO   C CA    1 
ATOM   1701 C C     . PRO   C 3 49  ? 5.526   -81.856 42.937  1.00 31.52  ?  49  PRO   C C     1 
ATOM   1702 O O     . PRO   C 3 49  ? 4.359   -82.210 43.126  1.00 31.94  ?  49  PRO   C O     1 
ATOM   1703 C CB    . PRO   C 3 49  ? 6.226   -80.923 45.133  1.00 33.51  ?  49  PRO   C CB    1 
ATOM   1704 C CG    . PRO   C 3 49  ? 5.682   -79.707 45.825  1.00 33.38  ?  49  PRO   C CG    1 
ATOM   1705 C CD    . PRO   C 3 49  ? 4.733   -79.021 44.903  1.00 32.02  ?  49  PRO   C CD    1 
ATOM   1706 N N     . HIS   C 3 50  ? 6.353   -82.425 42.065  1.00 31.53  ?  50  HIS   C N     1 
ATOM   1707 C CA    . HIS   C 3 50  ? 6.026   -83.635 41.350  1.00 32.34  ?  50  HIS   C CA    1 
ATOM   1708 C C     . HIS   C 3 50  ? 7.355   -84.287 41.007  1.00 32.84  ?  50  HIS   C C     1 
ATOM   1709 O O     . HIS   C 3 50  ? 8.101   -83.738 40.207  1.00 31.65  ?  50  HIS   C O     1 
ATOM   1710 C CB    . HIS   C 3 50  ? 5.145   -83.383 40.107  1.00 32.20  ?  50  HIS   C CB    1 
ATOM   1711 C CG    . HIS   C 3 50  ? 4.686   -84.710 39.546  1.00 33.81  ?  50  HIS   C CG    1 
ATOM   1712 N ND1   . HIS   C 3 50  ? 5.422   -85.363 38.578  1.00 33.90  ?  50  HIS   C ND1   1 
ATOM   1713 C CD2   . HIS   C 3 50  ? 3.692   -85.554 39.884  1.00 33.83  ?  50  HIS   C CD2   1 
ATOM   1714 C CE1   . HIS   C 3 50  ? 4.869   -86.540 38.331  1.00 36.36  ?  50  HIS   C CE1   1 
ATOM   1715 N NE2   . HIS   C 3 50  ? 3.810   -86.672 39.100  1.00 36.52  ?  50  HIS   C NE2   1 
ATOM   1716 N N     . LYS   C 3 51  ? 7.637   -85.431 41.635  1.00 36.06  ?  51  LYS   C N     1 
ATOM   1717 C CA    . LYS   C 3 51  ? 8.858   -86.183 41.411  1.00 38.76  ?  51  LYS   C CA    1 
ATOM   1718 C C     . LYS   C 3 51  ? 8.689   -86.880 40.065  1.00 36.74  ?  51  LYS   C C     1 
ATOM   1719 O O     . LYS   C 3 51  ? 7.793   -87.704 39.900  1.00 38.14  ?  51  LYS   C O     1 
ATOM   1720 C CB    . LYS   C 3 51  ? 9.088   -87.106 42.616  1.00 43.00  ?  51  LYS   C CB    1 
ATOM   1721 C CG    . LYS   C 3 51  ? 10.489  -87.714 42.726  1.00 46.40  ?  51  LYS   C CG    1 
ATOM   1722 C CD    . LYS   C 3 51  ? 10.572  -88.762 43.837  1.00 50.44  ?  51  LYS   C CD    1 
ATOM   1723 C CE    . LYS   C 3 51  ? 11.943  -89.037 44.400  1.00 54.24  ?  51  LYS   C CE    1 
ATOM   1724 N NZ    . LYS   C 3 51  ? 11.857  -89.565 45.771  1.00 57.17  1  51  LYS   C NZ    1 
ATOM   1725 N N     . GLN   C 3 52  ? 9.492   -86.481 39.075  1.00 35.48  ?  52  GLN   C N     1 
ATOM   1726 C CA    . GLN   C 3 52  ? 9.478   -87.098 37.750  1.00 34.72  ?  52  GLN   C CA    1 
ATOM   1727 C C     . GLN   C 3 52  ? 9.958   -88.558 37.852  1.00 36.77  ?  52  GLN   C C     1 
ATOM   1728 O O     . GLN   C 3 52  ? 10.960  -88.835 38.524  1.00 36.12  ?  52  GLN   C O     1 
ATOM   1729 C CB    . GLN   C 3 52  ? 10.342  -86.299 36.778  1.00 32.62  ?  52  GLN   C CB    1 
ATOM   1730 C CG    . GLN   C 3 52  ? 9.793   -84.942 36.375  1.00 30.72  ?  52  GLN   C CG    1 
ATOM   1731 C CD    . GLN   C 3 52  ? 8.481   -84.984 35.633  1.00 30.30  ?  52  GLN   C CD    1 
ATOM   1732 O OE1   . GLN   C 3 52  ? 8.220   -85.898 34.837  1.00 31.60  ?  52  GLN   C OE1   1 
ATOM   1733 N NE2   . GLN   C 3 52  ? 7.624   -84.010 35.904  1.00 28.87  ?  52  GLN   C NE2   1 
ATOM   1734 N N     . GLY   C 3 53  ? 9.162   -89.468 37.259  1.00 38.12  ?  53  GLY   C N     1 
ATOM   1735 C CA    . GLY   C 3 53  ? 9.353   -90.914 37.301  1.00 39.55  ?  53  GLY   C CA    1 
ATOM   1736 C C     . GLY   C 3 53  ? 9.569   -91.420 35.878  1.00 39.75  ?  53  GLY   C C     1 
ATOM   1737 O O     . GLY   C 3 53  ? 9.757   -90.629 34.957  1.00 38.53  ?  53  GLY   C O     1 
ATOM   1738 N N     . SER   C 3 54  ? 9.532   -92.745 35.725  1.00 41.58  ?  54  SER   C N     1 
ATOM   1739 C CA    . SER   C 3 54  ? 9.791   -93.411 34.462  1.00 42.16  ?  54  SER   C CA    1 
ATOM   1740 C C     . SER   C 3 54  ? 8.570   -93.331 33.547  1.00 41.83  ?  54  SER   C C     1 
ATOM   1741 O O     . SER   C 3 54  ? 8.781   -93.417 32.340  1.00 40.22  ?  54  SER   C O     1 
ATOM   1742 C CB    . SER   C 3 54  ? 10.292  -94.828 34.687  1.00 45.21  ?  54  SER   C CB    1 
ATOM   1743 O OG    . SER   C 3 54  ? 9.288   -95.716 35.158  1.00 46.36  ?  54  SER   C OG    1 
ATOM   1744 N N     . ASP   C 3 55  ? 7.343   -93.175 34.099  1.00 41.99  ?  55  ASP   C N     1 
ATOM   1745 C CA    . ASP   C 3 55  ? 6.139   -92.956 33.314  1.00 44.05  ?  55  ASP   C CA    1 
ATOM   1746 C C     . ASP   C 3 55  ? 6.002   -91.467 32.961  1.00 42.83  ?  55  ASP   C C     1 
ATOM   1747 O O     . ASP   C 3 55  ? 6.294   -90.582 33.774  1.00 41.07  ?  55  ASP   C O     1 
ATOM   1748 C CB    . ASP   C 3 55  ? 4.884   -93.465 34.010  1.00 48.50  ?  55  ASP   C CB    1 
ATOM   1749 C CG    . ASP   C 3 55  ? 4.740   -94.981 34.141  1.00 54.42  ?  55  ASP   C CG    1 
ATOM   1750 O OD1   . ASP   C 3 55  ? 4.479   -95.652 33.093  1.00 56.28  ?  55  ASP   C OD1   1 
ATOM   1751 O OD2   . ASP   C 3 55  ? 4.882   -95.478 35.291  1.00 56.08  -1 55  ASP   C OD2   1 
ATOM   1752 N N     . TYR   C 3 56  ? 5.494   -91.215 31.744  1.00 42.63  ?  56  TYR   C N     1 
ATOM   1753 C CA    . TYR   C 3 56  ? 5.107   -89.898 31.259  1.00 40.04  ?  56  TYR   C CA    1 
ATOM   1754 C C     . TYR   C 3 56  ? 3.951   -89.321 32.097  1.00 39.42  ?  56  TYR   C C     1 
ATOM   1755 O O     . TYR   C 3 56  ? 2.963   -90.024 32.306  1.00 39.01  ?  56  TYR   C O     1 
ATOM   1756 C CB    . TYR   C 3 56  ? 4.736   -89.942 29.762  1.00 40.39  ?  56  TYR   C CB    1 
ATOM   1757 C CG    . TYR   C 3 56  ? 5.872   -89.752 28.756  1.00 40.38  ?  56  TYR   C CG    1 
ATOM   1758 C CD1   . TYR   C 3 56  ? 6.773   -88.680 28.868  1.00 38.45  ?  56  TYR   C CD1   1 
ATOM   1759 C CD2   . TYR   C 3 56  ? 6.050   -90.621 27.669  1.00 41.35  ?  56  TYR   C CD2   1 
ATOM   1760 C CE1   . TYR   C 3 56  ? 7.798   -88.478 27.947  1.00 38.57  ?  56  TYR   C CE1   1 
ATOM   1761 C CE2   . TYR   C 3 56  ? 7.069   -90.421 26.731  1.00 42.05  ?  56  TYR   C CE2   1 
ATOM   1762 C CZ    . TYR   C 3 56  ? 7.963   -89.369 26.901  1.00 40.36  ?  56  TYR   C CZ    1 
ATOM   1763 O OH    . TYR   C 3 56  ? 8.972   -89.056 26.044  1.00 44.35  ?  56  TYR   C OH    1 
ATOM   1764 N N     . VAL   C 3 57  ? 4.064   -88.027 32.501  1.00 36.23  ?  57  VAL   C N     1 
ATOM   1765 C CA    . VAL   C 3 57  ? 2.948   -87.254 33.051  1.00 34.61  ?  57  VAL   C CA    1 
ATOM   1766 C C     . VAL   C 3 57  ? 2.611   -86.092 32.106  1.00 31.23  ?  57  VAL   C C     1 
ATOM   1767 O O     . VAL   C 3 57  ? 3.514   -85.401 31.622  1.00 28.81  ?  57  VAL   C O     1 
ATOM   1768 C CB    . VAL   C 3 57  ? 3.184   -86.822 34.525  1.00 34.05  ?  57  VAL   C CB    1 
ATOM   1769 C CG1   . VAL   C 3 57  ? 4.366   -85.864 34.727  1.00 33.46  ?  57  VAL   C CG1   1 
ATOM   1770 C CG2   . VAL   C 3 57  ? 1.921   -86.267 35.149  1.00 33.38  ?  57  VAL   C CG2   1 
ATOM   1771 N N     . LEU   C 3 58  ? 1.289   -85.857 31.893  1.00 30.16  ?  58  LEU   C N     1 
ATOM   1772 C CA    . LEU   C 3 58  ? 0.752   -84.746 31.092  1.00 29.63  ?  58  LEU   C CA    1 
ATOM   1773 C C     . LEU   C 3 58  ? 1.033   -83.410 31.821  1.00 28.72  ?  58  LEU   C C     1 
ATOM   1774 O O     . LEU   C 3 58  ? 0.543   -83.212 32.944  1.00 29.05  ?  58  LEU   C O     1 
ATOM   1775 C CB    . LEU   C 3 58  ? -0.754  -84.983 30.862  1.00 29.60  ?  58  LEU   C CB    1 
ATOM   1776 C CG    . LEU   C 3 58  ? -1.512  -83.966 29.996  1.00 29.72  ?  58  LEU   C CG    1 
ATOM   1777 C CD1   . LEU   C 3 58  ? -1.188  -84.175 28.526  1.00 30.25  ?  58  LEU   C CD1   1 
ATOM   1778 C CD2   . LEU   C 3 58  ? -3.020  -83.980 30.199  1.00 30.03  ?  58  LEU   C CD2   1 
ATOM   1779 N N     . VAL   C 3 59  ? 1.863   -82.541 31.219  1.00 26.52  ?  59  VAL   C N     1 
ATOM   1780 C CA    . VAL   C 3 59  ? 2.246   -81.232 31.753  1.00 25.49  ?  59  VAL   C CA    1 
ATOM   1781 C C     . VAL   C 3 59  ? 1.424   -80.126 31.082  1.00 25.37  ?  59  VAL   C C     1 
ATOM   1782 O O     . VAL   C 3 59  ? 0.988   -79.201 31.787  1.00 25.65  ?  59  VAL   C O     1 
ATOM   1783 C CB    . VAL   C 3 59  ? 3.752   -80.933 31.746  1.00 24.23  ?  59  VAL   C CB    1 
ATOM   1784 C CG1   . VAL   C 3 59  ? 4.491   -81.947 32.634  1.00 24.70  ?  59  VAL   C CG1   1 
ATOM   1785 C CG2   . VAL   C 3 59  ? 4.394   -80.891 30.365  1.00 23.83  ?  59  VAL   C CG2   1 
ATOM   1786 N N     . ALA   C 3 60  ? 1.166   -80.248 29.766  1.00 25.70  ?  60  ALA   C N     1 
ATOM   1787 C CA    . ALA   C 3 60  ? 0.228   -79.376 29.059  1.00 25.75  ?  60  ALA   C CA    1 
ATOM   1788 C C     . ALA   C 3 60  ? -0.536  -80.142 27.982  1.00 26.46  ?  60  ALA   C C     1 
ATOM   1789 O O     . ALA   C 3 60  ? -0.079  -81.199 27.539  1.00 28.31  ?  60  ALA   C O     1 
ATOM   1790 C CB    . ALA   C 3 60  ? 0.968   -78.209 28.469  1.00 25.14  ?  60  ALA   C CB    1 
ATOM   1791 N N     . GLY   C 3 61  ? -1.703  -79.623 27.591  1.00 25.83  ?  61  GLY   C N     1 
ATOM   1792 C CA    . GLY   C 3 61  ? -2.398  -80.097 26.415  1.00 26.76  ?  61  GLY   C CA    1 
ATOM   1793 C C     . GLY   C 3 61  ? -3.815  -79.550 26.311  1.00 28.16  ?  61  GLY   C C     1 
ATOM   1794 O O     . GLY   C 3 61  ? -4.422  -79.179 27.319  1.00 30.34  ?  61  GLY   C O     1 
ATOM   1795 N N     . LEU   C 3 62  ? -4.337  -79.521 25.078  1.00 28.75  ?  62  LEU   C N     1 
ATOM   1796 C CA    . LEU   C 3 62  ? -5.685  -79.022 24.837  1.00 30.16  ?  62  LEU   C CA    1 
ATOM   1797 C C     . LEU   C 3 62  ? -6.698  -80.042 25.362  1.00 32.43  ?  62  LEU   C C     1 
ATOM   1798 O O     . LEU   C 3 62  ? -6.536  -81.264 25.122  1.00 33.91  ?  62  LEU   C O     1 
ATOM   1799 C CB    . LEU   C 3 62  ? -5.898  -78.739 23.351  1.00 31.19  ?  62  LEU   C CB    1 
ATOM   1800 C CG    . LEU   C 3 62  ? -5.259  -77.466 22.788  1.00 31.71  ?  62  LEU   C CG    1 
ATOM   1801 C CD1   . LEU   C 3 62  ? -5.247  -77.552 21.258  1.00 31.40  ?  62  LEU   C CD1   1 
ATOM   1802 C CD2   . LEU   C 3 62  ? -6.041  -76.227 23.257  1.00 32.49  ?  62  LEU   C CD2   1 
ATOM   1803 N N     . ALA   C 3 63  ? -7.743  -79.532 26.057  1.00 32.72  ?  63  ALA   C N     1 
ATOM   1804 C CA    . ALA   C 3 63  ? -8.760  -80.392 26.665  1.00 33.88  ?  63  ALA   C CA    1 
ATOM   1805 C C     . ALA   C 3 63  ? -9.477  -81.199 25.579  1.00 35.12  ?  63  ALA   C C     1 
ATOM   1806 O O     . ALA   C 3 63  ? -9.855  -80.633 24.563  1.00 33.72  ?  63  ALA   C O     1 
ATOM   1807 C CB    . ALA   C 3 63  ? -9.765  -79.574 27.448  1.00 34.26  ?  63  ALA   C CB    1 
ATOM   1808 N N     . GLY   C 3 64  ? -9.536  -82.533 25.740  1.00 36.94  ?  64  GLY   C N     1 
ATOM   1809 C CA    . GLY   C 3 64  ? -10.213 -83.413 24.801  1.00 37.93  ?  64  GLY   C CA    1 
ATOM   1810 C C     . GLY   C 3 64  ? -9.453  -83.647 23.493  1.00 39.19  ?  64  GLY   C C     1 
ATOM   1811 O O     . GLY   C 3 64  ? -9.930  -84.440 22.681  1.00 41.49  ?  64  GLY   C O     1 
ATOM   1812 N N     . ASP   C 3 65  ? -8.267  -83.036 23.288  1.00 37.78  ?  65  ASP   C N     1 
ATOM   1813 C CA    . ASP   C 3 65  ? -7.598  -83.072 21.993  1.00 37.67  ?  65  ASP   C CA    1 
ATOM   1814 C C     . ASP   C 3 65  ? -6.080  -83.125 22.189  1.00 34.41  ?  65  ASP   C C     1 
ATOM   1815 O O     . ASP   C 3 65  ? -5.398  -82.237 21.695  1.00 35.94  ?  65  ASP   C O     1 
ATOM   1816 C CB    . ASP   C 3 65  ? -8.154  -81.969 21.089  1.00 36.39  ?  65  ASP   C CB    1 
ATOM   1817 C CG    . ASP   C 3 65  ? -7.859  -82.083 19.602  1.00 35.10  ?  65  ASP   C CG    1 
ATOM   1818 O OD1   . ASP   C 3 65  ? -7.235  -83.075 19.182  1.00 34.84  ?  65  ASP   C OD1   1 
ATOM   1819 O OD2   . ASP   C 3 65  ? -8.239  -81.161 18.877  1.00 35.68  -1 65  ASP   C OD2   1 
ATOM   1820 N N     . PRO   C 3 66  ? -5.510  -84.179 22.833  1.00 32.92  ?  66  PRO   C N     1 
ATOM   1821 C CA    . PRO   C 3 66  ? -4.061  -84.300 22.988  1.00 31.74  ?  66  PRO   C CA    1 
ATOM   1822 C C     . PRO   C 3 66  ? -3.306  -84.553 21.672  1.00 32.51  ?  66  PRO   C C     1 
ATOM   1823 O O     . PRO   C 3 66  ? -2.094  -84.369 21.628  1.00 30.35  ?  66  PRO   C O     1 
ATOM   1824 C CB    . PRO   C 3 66  ? -3.908  -85.425 23.999  1.00 32.20  ?  66  PRO   C CB    1 
ATOM   1825 C CG    . PRO   C 3 66  ? -5.071  -86.346 23.654  1.00 33.83  ?  66  PRO   C CG    1 
ATOM   1826 C CD    . PRO   C 3 66  ? -6.202  -85.389 23.337  1.00 34.63  ?  66  PRO   C CD    1 
ATOM   1827 N N     . ASN   C 3 67  ? -3.996  -85.023 20.618  1.00 35.17  ?  67  ASN   C N     1 
ATOM   1828 C CA    . ASN   C 3 67  ? -3.431  -85.115 19.278  1.00 37.39  ?  67  ASN   C CA    1 
ATOM   1829 C C     . ASN   C 3 67  ? -3.102  -83.750 18.691  1.00 34.88  ?  67  ASN   C C     1 
ATOM   1830 O O     . ASN   C 3 67  ? -2.108  -83.647 17.990  1.00 36.02  ?  67  ASN   C O     1 
ATOM   1831 C CB    . ASN   C 3 67  ? -4.296  -85.917 18.305  1.00 42.03  ?  67  ASN   C CB    1 
ATOM   1832 C CG    . ASN   C 3 67  ? -3.634  -87.235 17.973  1.00 46.05  ?  67  ASN   C CG    1 
ATOM   1833 O OD1   . ASN   C 3 67  ? -3.599  -88.150 18.807  1.00 48.85  ?  67  ASN   C OD1   1 
ATOM   1834 N ND2   . ASN   C 3 67  ? -3.044  -87.320 16.792  1.00 47.59  ?  67  ASN   C ND2   1 
ATOM   1835 N N     . ARG   C 3 68  ? -3.953  -82.741 18.930  1.00 33.68  ?  68  ARG   C N     1 
ATOM   1836 C CA    . ARG   C 3 68  ? -3.700  -81.386 18.471  1.00 32.99  ?  68  ARG   C CA    1 
ATOM   1837 C C     . ARG   C 3 68  ? -2.525  -80.795 19.252  1.00 29.46  ?  68  ARG   C C     1 
ATOM   1838 O O     . ARG   C 3 68  ? -1.609  -80.266 18.632  1.00 27.59  ?  68  ARG   C O     1 
ATOM   1839 C CB    . ARG   C 3 68  ? -4.930  -80.468 18.566  1.00 34.19  ?  68  ARG   C CB    1 
ATOM   1840 C CG    . ARG   C 3 68  ? -4.769  -79.030 18.056  1.00 33.17  ?  68  ARG   C CG    1 
ATOM   1841 C CD    . ARG   C 3 68  ? -4.434  -78.911 16.578  1.00 34.00  ?  68  ARG   C CD    1 
ATOM   1842 N NE    . ARG   C 3 68  ? -4.099  -77.545 16.147  1.00 33.39  ?  68  ARG   C NE    1 
ATOM   1843 C CZ    . ARG   C 3 68  ? -3.827  -77.219 14.880  1.00 34.91  ?  68  ARG   C CZ    1 
ATOM   1844 N NH1   . ARG   C 3 68  ? -3.733  -78.136 13.941  1.00 38.77  1  68  ARG   C NH1   1 
ATOM   1845 N NH2   . ARG   C 3 68  ? -3.630  -75.979 14.519  1.00 35.22  ?  68  ARG   C NH2   1 
ATOM   1846 N N     . PHE   C 3 69  ? -2.588  -80.885 20.592  1.00 27.69  ?  69  PHE   C N     1 
ATOM   1847 C CA    . PHE   C 3 69  ? -1.495  -80.420 21.424  1.00 26.71  ?  69  PHE   C CA    1 
ATOM   1848 C C     . PHE   C 3 69  ? -1.517  -81.146 22.755  1.00 26.61  ?  69  PHE   C C     1 
ATOM   1849 O O     . PHE   C 3 69  ? -2.538  -81.082 23.452  1.00 27.57  ?  69  PHE   C O     1 
ATOM   1850 C CB    . PHE   C 3 69  ? -1.410  -78.901 21.683  1.00 25.85  ?  69  PHE   C CB    1 
ATOM   1851 C CG    . PHE   C 3 69  ? -0.280  -78.595 22.656  1.00 25.14  ?  69  PHE   C CG    1 
ATOM   1852 C CD1   . PHE   C 3 69  ? 1.048   -78.923 22.336  1.00 24.66  ?  69  PHE   C CD1   1 
ATOM   1853 C CD2   . PHE   C 3 69  ? -0.558  -78.106 23.933  1.00 24.94  ?  69  PHE   C CD2   1 
ATOM   1854 C CE1   . PHE   C 3 69  ? 2.069   -78.714 23.248  1.00 24.01  ?  69  PHE   C CE1   1 
ATOM   1855 C CE2   . PHE   C 3 69  ? 0.475   -77.893 24.848  1.00 23.80  ?  69  PHE   C CE2   1 
ATOM   1856 C CZ    . PHE   C 3 69  ? 1.772   -78.237 24.507  1.00 24.40  ?  69  PHE   C CZ    1 
ATOM   1857 N N     . SER   C 3 70  ? -0.361  -81.751 23.090  1.00 25.31  ?  70  SER   C N     1 
ATOM   1858 C CA    . SER   C 3 70  ? -0.077  -82.324 24.389  1.00 25.35  ?  70  SER   C CA    1 
ATOM   1859 C C     . SER   C 3 70  ? 1.438   -82.362 24.618  1.00 24.92  ?  70  SER   C C     1 
ATOM   1860 O O     . SER   C 3 70  ? 2.215   -82.503 23.673  1.00 24.80  ?  70  SER   C O     1 
ATOM   1861 C CB    . SER   C 3 70  ? -0.724  -83.727 24.554  1.00 27.11  ?  70  SER   C CB    1 
ATOM   1862 O OG    . SER   C 3 70  ? -0.415  -84.637 23.502  1.00 26.95  ?  70  SER   C OG    1 
ATOM   1863 N N     . ALA   C 3 71  ? 1.850   -82.247 25.885  1.00 25.80  ?  71  ALA   C N     1 
ATOM   1864 C CA    . ALA   C 3 71  ? 3.255   -82.225 26.293  1.00 26.09  ?  71  ALA   C CA    1 
ATOM   1865 C C     . ALA   C 3 71  ? 3.438   -83.089 27.538  1.00 28.60  ?  71  ALA   C C     1 
ATOM   1866 O O     . ALA   C 3 71  ? 2.677   -82.942 28.492  1.00 30.92  ?  71  ALA   C O     1 
ATOM   1867 C CB    . ALA   C 3 71  ? 3.725   -80.809 26.539  1.00 25.04  ?  71  ALA   C CB    1 
ATOM   1868 N N     . TYR   C 3 72  ? 4.430   -83.998 27.504  1.00 28.81  ?  72  TYR   C N     1 
ATOM   1869 C CA    . TYR   C 3 72  ? 4.644   -85.001 28.536  1.00 29.00  ?  72  TYR   C CA    1 
ATOM   1870 C C     . TYR   C 3 72  ? 6.106   -84.940 28.966  1.00 27.79  ?  72  TYR   C C     1 
ATOM   1871 O O     . TYR   C 3 72  ? 6.945   -84.673 28.129  1.00 25.60  ?  72  TYR   C O     1 
ATOM   1872 C CB    . TYR   C 3 72  ? 4.314   -86.452 28.139  1.00 30.63  ?  72  TYR   C CB    1 
ATOM   1873 C CG    . TYR   C 3 72  ? 2.911   -86.670 27.594  1.00 31.30  ?  72  TYR   C CG    1 
ATOM   1874 C CD1   . TYR   C 3 72  ? 2.607   -86.352 26.269  1.00 32.64  ?  72  TYR   C CD1   1 
ATOM   1875 C CD2   . TYR   C 3 72  ? 1.883   -87.187 28.386  1.00 32.04  ?  72  TYR   C CD2   1 
ATOM   1876 C CE1   . TYR   C 3 72  ? 1.320   -86.517 25.754  1.00 33.16  ?  72  TYR   C CE1   1 
ATOM   1877 C CE2   . TYR   C 3 72  ? 0.591   -87.334 27.887  1.00 32.35  ?  72  TYR   C CE2   1 
ATOM   1878 C CZ    . TYR   C 3 72  ? 0.313   -87.026 26.560  1.00 33.13  ?  72  TYR   C CZ    1 
ATOM   1879 O OH    . TYR   C 3 72  ? -0.935  -87.159 26.015  1.00 34.05  ?  72  TYR   C OH    1 
ATOM   1880 N N     . THR   C 3 73  ? 6.341   -85.230 30.263  1.00 28.32  ?  73  THR   C N     1 
ATOM   1881 C CA    . THR   C 3 73  ? 7.642   -85.286 30.915  1.00 29.70  ?  73  THR   C CA    1 
ATOM   1882 C C     . THR   C 3 73  ? 7.768   -86.632 31.633  1.00 31.58  ?  73  THR   C C     1 
ATOM   1883 O O     . THR   C 3 73  ? 6.787   -87.100 32.228  1.00 32.00  ?  73  THR   C O     1 
ATOM   1884 C CB    . THR   C 3 73  ? 7.847   -84.148 31.924  1.00 28.33  ?  73  THR   C CB    1 
ATOM   1885 O OG1   . THR   C 3 73  ? 6.813   -84.232 32.912  1.00 27.74  ?  73  THR   C OG1   1 
ATOM   1886 C CG2   . THR   C 3 73  ? 7.848   -82.796 31.243  1.00 28.16  ?  73  THR   C CG2   1 
ATOM   1887 N N     . ARG   C 3 74  ? 8.964   -87.234 31.543  1.00 31.55  ?  74  ARG   C N     1 
ATOM   1888 C CA    . ARG   C 3 74  ? 9.386   -88.334 32.402  1.00 35.54  ?  74  ARG   C CA    1 
ATOM   1889 C C     . ARG   C 3 74  ? 10.864  -88.100 32.745  1.00 36.07  ?  74  ARG   C C     1 
ATOM   1890 O O     . ARG   C 3 74  ? 11.459  -87.127 32.294  1.00 32.29  ?  74  ARG   C O     1 
ATOM   1891 C CB    . ARG   C 3 74  ? 9.025   -89.727 31.815  1.00 36.09  ?  74  ARG   C CB    1 
ATOM   1892 C CG    . ARG   C 3 74  ? 9.745   -90.009 30.500  1.00 36.75  ?  74  ARG   C CG    1 
ATOM   1893 C CD    . ARG   C 3 74  ? 9.390   -91.270 29.744  1.00 38.67  ?  74  ARG   C CD    1 
ATOM   1894 N NE    . ARG   C 3 74  ? 10.585  -91.973 29.238  1.00 40.41  ?  74  ARG   C NE    1 
ATOM   1895 C CZ    . ARG   C 3 74  ? 11.511  -92.663 29.948  1.00 41.17  ?  74  ARG   C CZ    1 
ATOM   1896 N NH1   . ARG   C 3 74  ? 11.437  -92.818 31.272  1.00 41.54  1  74  ARG   C NH1   1 
ATOM   1897 N NH2   . ARG   C 3 74  ? 12.551  -93.188 29.320  1.00 42.26  ?  74  ARG   C NH2   1 
ATOM   1898 N N     . SER   C 3 75  ? 11.399  -88.975 33.617  1.00 39.23  ?  75  SER   C N     1 
ATOM   1899 C CA    . SER   C 3 75  ? 12.805  -89.029 33.968  1.00 40.97  ?  75  SER   C CA    1 
ATOM   1900 C C     . SER   C 3 75  ? 13.300  -90.433 33.650  1.00 42.66  ?  75  SER   C C     1 
ATOM   1901 O O     . SER   C 3 75  ? 12.606  -91.392 33.978  1.00 44.43  ?  75  SER   C O     1 
ATOM   1902 C CB    . SER   C 3 75  ? 13.037  -88.712 35.404  1.00 42.98  ?  75  SER   C CB    1 
ATOM   1903 O OG    . SER   C 3 75  ? 14.430  -88.639 35.670  1.00 45.11  ?  75  SER   C OG    1 
ATOM   1904 N N     . GLN   C 3 76  ? 14.497  -90.535 33.039  1.00 42.87  ?  76  GLN   C N     1 
ATOM   1905 C CA    . GLN   C 3 76  ? 15.174  -91.807 32.811  1.00 44.47  ?  76  GLN   C CA    1 
ATOM   1906 C C     . GLN   C 3 76  ? 16.319  -92.018 33.808  1.00 45.54  ?  76  GLN   C C     1 
ATOM   1907 O O     . GLN   C 3 76  ? 17.044  -92.971 33.596  1.00 46.22  ?  76  GLN   C O     1 
ATOM   1908 C CB    . GLN   C 3 76  ? 15.563  -91.983 31.335  1.00 44.09  ?  76  GLN   C CB    1 
ATOM   1909 C CG    . GLN   C 3 76  ? 16.863  -91.316 30.885  1.00 44.68  ?  76  GLN   C CG    1 
ATOM   1910 C CD    . GLN   C 3 76  ? 17.208  -91.579 29.438  1.00 45.53  ?  76  GLN   C CD    1 
ATOM   1911 O OE1   . GLN   C 3 76  ? 17.178  -92.718 28.983  1.00 49.55  ?  76  GLN   C OE1   1 
ATOM   1912 N NE2   . GLN   C 3 76  ? 17.538  -90.537 28.688  1.00 45.04  ?  76  GLN   C NE2   1 
ATOM   1913 N N     . GLY   C 3 77  ? 16.545  -91.138 34.814  1.00 44.94  ?  77  GLY   C N     1 
ATOM   1914 C CA    . GLY   C 3 77  ? 17.653  -91.294 35.747  1.00 45.15  ?  77  GLY   C CA    1 
ATOM   1915 C C     . GLY   C 3 77  ? 18.999  -90.949 35.111  1.00 45.63  ?  77  GLY   C C     1 
ATOM   1916 O O     . GLY   C 3 77  ? 19.062  -90.638 33.923  1.00 44.64  ?  77  GLY   C O     1 
ATOM   1917 N N     . GLY   C 3 78  ? 20.055  -90.958 35.940  1.00 47.78  ?  78  GLY   C N     1 
ATOM   1918 C CA    . GLY   C 3 78  ? 21.393  -90.522 35.564  1.00 49.31  ?  78  GLY   C CA    1 
ATOM   1919 C C     . GLY   C 3 78  ? 21.506  -89.005 35.405  1.00 49.20  ?  78  GLY   C C     1 
ATOM   1920 O O     . GLY   C 3 78  ? 20.604  -88.251 35.792  1.00 50.10  ?  78  GLY   C O     1 
ATOM   1921 N N     . SER   C 3 79  ? 22.626  -88.564 34.806  1.00 51.05  ?  79  SER   C N     1 
ATOM   1922 C CA    . SER   C 3 79  ? 22.906  -87.150 34.527  1.00 50.69  ?  79  SER   C CA    1 
ATOM   1923 C C     . SER   C 3 79  ? 22.027  -86.677 33.355  1.00 50.26  ?  79  SER   C C     1 
ATOM   1924 O O     . SER   C 3 79  ? 21.822  -87.464 32.429  1.00 54.53  ?  79  SER   C O     1 
ATOM   1925 C CB    . SER   C 3 79  ? 24.437  -86.937 34.301  1.00 51.37  ?  79  SER   C CB    1 
ATOM   1926 O OG    . SER   C 3 79  ? 24.764  -85.981 33.296  1.00 50.39  ?  79  SER   C OG    1 
ATOM   1927 N N     . LYS   C 3 80  ? 21.544  -85.412 33.377  1.00 46.83  ?  80  LYS   C N     1 
ATOM   1928 C CA    . LYS   C 3 80  ? 20.635  -84.860 32.373  1.00 44.18  ?  80  LYS   C CA    1 
ATOM   1929 C C     . LYS   C 3 80  ? 19.412  -85.772 32.125  1.00 43.23  ?  80  LYS   C C     1 
ATOM   1930 O O     . LYS   C 3 80  ? 19.094  -86.124 30.971  1.00 41.68  ?  80  LYS   C O     1 
ATOM   1931 C CB    . LYS   C 3 80  ? 21.479  -84.499 31.138  1.00 45.17  ?  80  LYS   C CB    1 
ATOM   1932 C CG    . LYS   C 3 80  ? 22.491  -83.340 31.310  1.00 45.60  ?  80  LYS   C CG    1 
ATOM   1933 C CD    . LYS   C 3 80  ? 23.433  -83.101 30.131  1.00 45.26  ?  80  LYS   C CD    1 
ATOM   1934 C CE    . LYS   C 3 80  ? 24.883  -83.345 30.402  1.00 49.62  ?  80  LYS   C CE    1 
ATOM   1935 N NZ    . LYS   C 3 80  ? 25.289  -84.750 30.575  1.00 54.53  1  80  LYS   C NZ    1 
ATOM   1936 N N     . PRO   C 3 81  ? 18.647  -86.149 33.188  1.00 40.98  ?  81  PRO   C N     1 
ATOM   1937 C CA    . PRO   C 3 81  ? 17.718  -87.284 33.124  1.00 40.45  ?  81  PRO   C CA    1 
ATOM   1938 C C     . PRO   C 3 81  ? 16.345  -87.077 32.463  1.00 38.05  ?  81  PRO   C C     1 
ATOM   1939 O O     . PRO   C 3 81  ? 15.623  -88.064 32.288  1.00 39.46  ?  81  PRO   C O     1 
ATOM   1940 C CB    . PRO   C 3 81  ? 17.506  -87.584 34.604  1.00 42.41  ?  81  PRO   C CB    1 
ATOM   1941 C CG    . PRO   C 3 81  ? 17.515  -86.199 35.213  1.00 40.71  ?  81  PRO   C CG    1 
ATOM   1942 C CD    . PRO   C 3 81  ? 18.661  -85.526 34.523  1.00 40.23  ?  81  PRO   C CD    1 
ATOM   1943 N N     . LEU   C 3 82  ? 15.981  -85.844 32.085  1.00 33.78  ?  82  LEU   C N     1 
ATOM   1944 C CA    . LEU   C 3 82  ? 14.617  -85.517 31.698  1.00 32.49  ?  82  LEU   C CA    1 
ATOM   1945 C C     . LEU   C 3 82  ? 14.390  -85.968 30.250  1.00 31.71  ?  82  LEU   C C     1 
ATOM   1946 O O     . LEU   C 3 82  ? 15.264  -85.796 29.409  1.00 29.28  ?  82  LEU   C O     1 
ATOM   1947 C CB    . LEU   C 3 82  ? 14.319  -84.027 31.885  1.00 31.09  ?  82  LEU   C CB    1 
ATOM   1948 C CG    . LEU   C 3 82  ? 12.828  -83.638 31.855  1.00 31.08  ?  82  LEU   C CG    1 
ATOM   1949 C CD1   . LEU   C 3 82  ? 12.063  -84.050 33.102  1.00 31.74  ?  82  LEU   C CD1   1 
ATOM   1950 C CD2   . LEU   C 3 82  ? 12.610  -82.135 31.602  1.00 29.32  ?  82  LEU   C CD2   1 
ATOM   1951 N N     . VAL   C 3 83  ? 13.230  -86.618 30.018  1.00 31.86  ?  83  VAL   C N     1 
ATOM   1952 C CA    . VAL   C 3 83  ? 12.745  -86.964 28.691  1.00 32.16  ?  83  VAL   C CA    1 
ATOM   1953 C C     . VAL   C 3 83  ? 11.446  -86.176 28.502  1.00 31.97  ?  83  VAL   C C     1 
ATOM   1954 O O     . VAL   C 3 83  ? 10.650  -86.069 29.467  1.00 30.81  ?  83  VAL   C O     1 
ATOM   1955 C CB    . VAL   C 3 83  ? 12.594  -88.492 28.542  1.00 33.71  ?  83  VAL   C CB    1 
ATOM   1956 C CG1   . VAL   C 3 83  ? 12.011  -88.929 27.203  1.00 33.81  ?  83  VAL   C CG1   1 
ATOM   1957 C CG2   . VAL   C 3 83  ? 13.927  -89.225 28.825  1.00 35.38  ?  83  VAL   C CG2   1 
ATOM   1958 N N     . VAL   C 3 84  ? 11.269  -85.611 27.278  1.00 29.11  ?  84  VAL   C N     1 
ATOM   1959 C CA    . VAL   C 3 84  ? 10.097  -84.807 26.971  1.00 27.57  ?  84  VAL   C CA    1 
ATOM   1960 C C     . VAL   C 3 84  ? 9.470   -85.324 25.683  1.00 28.14  ?  84  VAL   C C     1 
ATOM   1961 O O     . VAL   C 3 84  ? 10.187  -85.512 24.685  1.00 28.58  ?  84  VAL   C O     1 
ATOM   1962 C CB    . VAL   C 3 84  ? 10.442  -83.304 26.869  1.00 26.39  ?  84  VAL   C CB    1 
ATOM   1963 C CG1   . VAL   C 3 84  ? 9.241   -82.450 26.419  1.00 25.49  ?  84  VAL   C CG1   1 
ATOM   1964 C CG2   . VAL   C 3 84  ? 11.012  -82.788 28.178  1.00 26.16  ?  84  VAL   C CG2   1 
ATOM   1965 N N     . LYS   C 3 85  ? 8.128   -85.419 25.702  1.00 28.09  ?  85  LYS   C N     1 
ATOM   1966 C CA    . LYS   C 3 85  ? 7.327   -85.710 24.525  1.00 30.63  ?  85  LYS   C CA    1 
ATOM   1967 C C     . LYS   C 3 85  ? 6.446   -84.496 24.238  1.00 29.73  ?  85  LYS   C C     1 
ATOM   1968 O O     . LYS   C 3 85  ? 5.714   -84.101 25.146  1.00 30.67  ?  85  LYS   C O     1 
ATOM   1969 C CB    . LYS   C 3 85  ? 6.482   -86.970 24.683  1.00 33.56  ?  85  LYS   C CB    1 
ATOM   1970 C CG    . LYS   C 3 85  ? 5.916   -87.609 23.411  1.00 36.60  ?  85  LYS   C CG    1 
ATOM   1971 C CD    . LYS   C 3 85  ? 5.310   -89.017 23.587  1.00 39.58  ?  85  LYS   C CD    1 
ATOM   1972 C CE    . LYS   C 3 85  ? 4.085   -89.064 24.484  1.00 41.66  ?  85  LYS   C CE    1 
ATOM   1973 N NZ    . LYS   C 3 85  ? 3.504   -90.390 24.679  1.00 44.54  1  85  LYS   C NZ    1 
ATOM   1974 N N     . LEU   C 3 86  ? 6.561   -83.938 23.007  1.00 27.88  ?  86  LEU   C N     1 
ATOM   1975 C CA    . LEU   C 3 86  ? 5.722   -82.884 22.478  1.00 28.14  ?  86  LEU   C CA    1 
ATOM   1976 C C     . LEU   C 3 86  ? 4.929   -83.379 21.280  1.00 29.02  ?  86  LEU   C C     1 
ATOM   1977 O O     . LEU   C 3 86  ? 5.535   -83.718 20.254  1.00 30.45  ?  86  LEU   C O     1 
ATOM   1978 C CB    . LEU   C 3 86  ? 6.584   -81.699 22.034  1.00 28.48  ?  86  LEU   C CB    1 
ATOM   1979 C CG    . LEU   C 3 86  ? 7.447   -81.017 23.096  1.00 29.16  ?  86  LEU   C CG    1 
ATOM   1980 C CD1   . LEU   C 3 86  ? 8.052   -79.799 22.469  1.00 29.41  ?  86  LEU   C CD1   1 
ATOM   1981 C CD2   . LEU   C 3 86  ? 6.684   -80.582 24.338  1.00 31.22  ?  86  LEU   C CD2   1 
ATOM   1982 N N     . VAL   C 3 87  ? 3.593   -83.341 21.391  1.00 28.87  ?  87  VAL   C N     1 
ATOM   1983 C CA    . VAL   C 3 87  ? 2.684   -83.763 20.322  1.00 30.65  ?  87  VAL   C CA    1 
ATOM   1984 C C     . VAL   C 3 87  ? 2.075   -82.467 19.763  1.00 30.26  ?  87  VAL   C C     1 
ATOM   1985 O O     . VAL   C 3 87  ? 1.472   -81.720 20.534  1.00 28.06  ?  87  VAL   C O     1 
ATOM   1986 C CB    . VAL   C 3 87  ? 1.596   -84.776 20.746  1.00 31.98  ?  87  VAL   C CB    1 
ATOM   1987 C CG1   . VAL   C 3 87  ? 0.754   -85.297 19.574  1.00 33.03  ?  87  VAL   C CG1   1 
ATOM   1988 C CG2   . VAL   C 3 87  ? 2.167   -85.931 21.558  1.00 32.78  ?  87  VAL   C CG2   1 
ATOM   1989 N N     . ASN   C 3 88  ? 2.286   -82.205 18.445  1.00 29.83  ?  88  ASN   C N     1 
ATOM   1990 C CA    . ASN   C 3 88  ? 1.749   -81.076 17.706  1.00 29.68  ?  88  ASN   C CA    1 
ATOM   1991 C C     . ASN   C 3 88  ? 1.085   -81.601 16.428  1.00 31.31  ?  88  ASN   C C     1 
ATOM   1992 O O     . ASN   C 3 88  ? 1.782   -82.071 15.527  1.00 32.29  ?  88  ASN   C O     1 
ATOM   1993 C CB    . ASN   C 3 88  ? 2.851   -80.050 17.389  1.00 28.29  ?  88  ASN   C CB    1 
ATOM   1994 C CG    . ASN   C 3 88  ? 3.500   -79.484 18.639  1.00 25.70  ?  88  ASN   C CG    1 
ATOM   1995 O OD1   . ASN   C 3 88  ? 2.905   -78.643 19.350  1.00 23.47  ?  88  ASN   C OD1   1 
ATOM   1996 N ND2   . ASN   C 3 88  ? 4.685   -79.968 18.956  1.00 25.35  ?  88  ASN   C ND2   1 
ATOM   1997 N N     . ASP   C 3 89  ? -0.256  -81.545 16.381  1.00 33.11  ?  89  ASP   C N     1 
ATOM   1998 C CA    . ASP   C 3 89  ? -1.090  -81.966 15.255  1.00 34.65  ?  89  ASP   C CA    1 
ATOM   1999 C C     . ASP   C 3 89  ? -0.716  -83.374 14.762  1.00 35.39  ?  89  ASP   C C     1 
ATOM   2000 O O     . ASP   C 3 89  ? -0.324  -83.569 13.605  1.00 34.67  ?  89  ASP   C O     1 
ATOM   2001 C CB    . ASP   C 3 89  ? -1.069  -80.880 14.183  1.00 35.83  ?  89  ASP   C CB    1 
ATOM   2002 C CG    . ASP   C 3 89  ? -2.116  -81.000 13.090  1.00 38.40  ?  89  ASP   C CG    1 
ATOM   2003 O OD1   . ASP   C 3 89  ? -3.287  -81.210 13.465  1.00 41.54  ?  89  ASP   C OD1   1 
ATOM   2004 O OD2   . ASP   C 3 89  ? -1.762  -80.849 11.895  1.00 38.08  -1 89  ASP   C OD2   1 
ATOM   2005 N N     . GLY   C 3 90  ? -0.717  -84.326 15.702  1.00 35.82  ?  90  GLY   C N     1 
ATOM   2006 C CA    . GLY   C 3 90  ? -0.465  -85.730 15.419  1.00 36.87  ?  90  GLY   C CA    1 
ATOM   2007 C C     . GLY   C 3 90  ? 1.015   -86.067 15.190  1.00 36.56  ?  90  GLY   C C     1 
ATOM   2008 O O     . GLY   C 3 90  ? 1.300   -87.240 14.978  1.00 36.98  ?  90  GLY   C O     1 
ATOM   2009 N N     . VAL   C 3 91  ? 1.958   -85.104 15.294  1.00 34.56  ?  91  VAL   C N     1 
ATOM   2010 C CA    . VAL   C 3 91  ? 3.379   -85.335 15.061  1.00 34.21  ?  91  VAL   C CA    1 
ATOM   2011 C C     . VAL   C 3 91  ? 4.080   -85.320 16.415  1.00 32.82  ?  91  VAL   C C     1 
ATOM   2012 O O     . VAL   C 3 91  ? 3.993   -84.319 17.123  1.00 31.37  ?  91  VAL   C O     1 
ATOM   2013 C CB    . VAL   C 3 91  ? 3.999   -84.299 14.119  1.00 33.82  ?  91  VAL   C CB    1 
ATOM   2014 C CG1   . VAL   C 3 91  ? 5.521   -84.467 13.973  1.00 34.20  ?  91  VAL   C CG1   1 
ATOM   2015 C CG2   . VAL   C 3 91  ? 3.287   -84.300 12.769  1.00 34.98  ?  91  VAL   C CG2   1 
ATOM   2016 N N     . THR   C 3 92  ? 4.793   -86.407 16.728  1.00 34.17  ?  92  THR   C N     1 
ATOM   2017 C CA    . THR   C 3 92  ? 5.366   -86.674 18.042  1.00 33.88  ?  92  THR   C CA    1 
ATOM   2018 C C     . THR   C 3 92  ? 6.845   -86.331 17.959  1.00 33.25  ?  92  THR   C C     1 
ATOM   2019 O O     . THR   C 3 92  ? 7.513   -86.867 17.081  1.00 35.79  ?  92  THR   C O     1 
ATOM   2020 C CB    . THR   C 3 92  ? 5.145   -88.144 18.408  1.00 35.68  ?  92  THR   C CB    1 
ATOM   2021 O OG1   . THR   C 3 92  ? 3.733   -88.243 18.350  1.00 36.99  ?  92  THR   C OG1   1 
ATOM   2022 C CG2   . THR   C 3 92  ? 5.623   -88.514 19.802  1.00 35.42  ?  92  THR   C CG2   1 
ATOM   2023 N N     . LEU   C 3 93  ? 7.316   -85.418 18.821  1.00 32.17  ?  93  LEU   C N     1 
ATOM   2024 C CA    . LEU   C 3 93  ? 8.731   -85.156 19.069  1.00 32.40  ?  93  LEU   C CA    1 
ATOM   2025 C C     . LEU   C 3 93  ? 9.058   -85.770 20.432  1.00 33.19  ?  93  LEU   C C     1 
ATOM   2026 O O     . LEU   C 3 93  ? 8.340   -85.506 21.410  1.00 32.36  ?  93  LEU   C O     1 
ATOM   2027 C CB    . LEU   C 3 93  ? 9.021   -83.649 19.036  1.00 31.81  ?  93  LEU   C CB    1 
ATOM   2028 C CG    . LEU   C 3 93  ? 10.425  -83.158 19.440  1.00 32.18  ?  93  LEU   C CG    1 
ATOM   2029 C CD1   . LEU   C 3 93  ? 11.536  -83.555 18.475  1.00 35.67  ?  93  LEU   C CD1   1 
ATOM   2030 C CD2   . LEU   C 3 93  ? 10.466  -81.629 19.613  1.00 30.83  ?  93  LEU   C CD2   1 
ATOM   2031 N N     . GLU   C 3 94  ? 10.143  -86.553 20.487  1.00 34.99  ?  94  GLU   C N     1 
ATOM   2032 C CA    . GLU   C 3 94  ? 10.728  -87.033 21.732  1.00 36.20  ?  94  GLU   C CA    1 
ATOM   2033 C C     . GLU   C 3 94  ? 12.108  -86.396 21.844  1.00 33.85  ?  94  GLU   C C     1 
ATOM   2034 O O     . GLU   C 3 94  ? 12.881  -86.501 20.906  1.00 33.11  ?  94  GLU   C O     1 
ATOM   2035 C CB    . GLU   C 3 94  ? 10.826  -88.554 21.870  1.00 39.61  ?  94  GLU   C CB    1 
ATOM   2036 C CG    . GLU   C 3 94  ? 11.255  -89.015 23.272  1.00 42.76  ?  94  GLU   C CG    1 
ATOM   2037 C CD    . GLU   C 3 94  ? 11.302  -90.508 23.558  1.00 48.19  ?  94  GLU   C CD    1 
ATOM   2038 O OE1   . GLU   C 3 94  ? 10.503  -90.914 24.441  1.00 49.53  ?  94  GLU   C OE1   1 
ATOM   2039 O OE2   . GLU   C 3 94  ? 12.116  -91.243 22.929  1.00 51.47  -1 94  GLU   C OE2   1 
ATOM   2040 N N     . LEU   C 3 95  ? 12.390  -85.795 23.011  1.00 32.66  ?  95  LEU   C N     1 
ATOM   2041 C CA    . LEU   C 3 95  ? 13.690  -85.273 23.376  1.00 31.29  ?  95  LEU   C CA    1 
ATOM   2042 C C     . LEU   C 3 95  ? 14.233  -86.071 24.550  1.00 32.44  ?  95  LEU   C C     1 
ATOM   2043 O O     . LEU   C 3 95  ? 13.497  -86.311 25.519  1.00 29.67  ?  95  LEU   C O     1 
ATOM   2044 C CB    . LEU   C 3 95  ? 13.548  -83.816 23.789  1.00 29.63  ?  95  LEU   C CB    1 
ATOM   2045 C CG    . LEU   C 3 95  ? 13.068  -82.838 22.718  1.00 29.39  ?  95  LEU   C CG    1 
ATOM   2046 C CD1   . LEU   C 3 95  ? 12.962  -81.439 23.306  1.00 27.92  ?  95  LEU   C CD1   1 
ATOM   2047 C CD2   . LEU   C 3 95  ? 13.979  -82.843 21.494  1.00 30.14  ?  95  LEU   C CD2   1 
ATOM   2048 N N     . THR   C 3 96  ? 15.528  -86.413 24.434  1.00 33.22  ?  96  THR   C N     1 
ATOM   2049 C CA    . THR   C 3 96  ? 16.365  -86.976 25.484  1.00 35.44  ?  96  THR   C CA    1 
ATOM   2050 C C     . THR   C 3 96  ? 17.710  -86.247 25.476  1.00 35.52  ?  96  THR   C C     1 
ATOM   2051 O O     . THR   C 3 96  ? 18.038  -85.502 24.550  1.00 35.56  ?  96  THR   C O     1 
ATOM   2052 C CB    . THR   C 3 96  ? 16.569  -88.479 25.240  1.00 37.87  ?  96  THR   C CB    1 
ATOM   2053 O OG1   . THR   C 3 96  ? 17.345  -88.614 24.055  1.00 39.43  ?  96  THR   C OG1   1 
ATOM   2054 C CG2   . THR   C 3 96  ? 15.296  -89.290 25.040  1.00 38.42  ?  96  THR   C CG2   1 
ATOM   2055 N N     . ARG   C 3 97  ? 18.533  -86.528 26.486  1.00 37.40  ?  97  ARG   C N     1 
ATOM   2056 C CA    . ARG   C 3 97  ? 19.894  -85.993 26.545  1.00 38.05  ?  97  ARG   C CA    1 
ATOM   2057 C C     . ARG   C 3 97  ? 20.733  -86.352 25.324  1.00 39.22  ?  97  ARG   C C     1 
ATOM   2058 O O     . ARG   C 3 97  ? 21.641  -85.597 25.027  1.00 40.96  ?  97  ARG   C O     1 
ATOM   2059 C CB    . ARG   C 3 97  ? 20.628  -86.440 27.815  1.00 38.99  ?  97  ARG   C CB    1 
ATOM   2060 C CG    . ARG   C 3 97  ? 20.821  -87.932 28.006  1.00 40.69  ?  97  ARG   C CG    1 
ATOM   2061 C CD    . ARG   C 3 97  ? 21.468  -88.265 29.338  1.00 41.23  ?  97  ARG   C CD    1 
ATOM   2062 N NE    . ARG   C 3 97  ? 21.342  -89.705 29.562  1.00 42.95  ?  97  ARG   C NE    1 
ATOM   2063 C CZ    . ARG   C 3 97  ? 20.759  -90.375 30.561  1.00 43.85  ?  97  ARG   C CZ    1 
ATOM   2064 N NH1   . ARG   C 3 97  ? 20.571  -91.670 30.405  1.00 46.30  1  97  ARG   C NH1   1 
ATOM   2065 N NH2   . ARG   C 3 97  ? 20.335  -89.802 31.675  1.00 42.31  ?  97  ARG   C NH2   1 
ATOM   2066 N N     . ASP   C 3 98  ? 20.467  -87.510 24.681  1.00 41.31  ?  98  ASP   C N     1 
ATOM   2067 C CA    . ASP   C 3 98  ? 21.172  -87.990 23.488  1.00 43.42  ?  98  ASP   C CA    1 
ATOM   2068 C C     . ASP   C 3 98  ? 20.674  -87.435 22.151  1.00 42.51  ?  98  ASP   C C     1 
ATOM   2069 O O     . ASP   C 3 98  ? 21.277  -87.778 21.142  1.00 45.83  ?  98  ASP   C O     1 
ATOM   2070 C CB    . ASP   C 3 98  ? 21.086  -89.503 23.372  1.00 46.00  ?  98  ASP   C CB    1 
ATOM   2071 C CG    . ASP   C 3 98  ? 21.628  -90.264 24.561  1.00 48.36  ?  98  ASP   C CG    1 
ATOM   2072 O OD1   . ASP   C 3 98  ? 22.665  -89.829 25.121  1.00 49.10  ?  98  ASP   C OD1   1 
ATOM   2073 O OD2   . ASP   C 3 98  ? 21.012  -91.286 24.894  1.00 49.48  -1 98  ASP   C OD2   1 
ATOM   2074 N N     . GLY   C 3 99  ? 19.599  -86.633 22.132  1.00 40.44  ?  99  GLY   C N     1 
ATOM   2075 C CA    . GLY   C 3 99  ? 19.102  -85.931 20.960  1.00 40.80  ?  99  GLY   C CA    1 
ATOM   2076 C C     . GLY   C 3 99  ? 17.596  -86.133 20.829  1.00 40.73  ?  99  GLY   C C     1 
ATOM   2077 O O     . GLY   C 3 99  ? 16.878  -86.095 21.838  1.00 40.63  ?  99  GLY   C O     1 
ATOM   2078 N N     . ALA   C 3 100 ? 17.131  -86.419 19.610  1.00 38.94  ?  100 ALA   C N     1 
ATOM   2079 C CA    . ALA   C 3 100 ? 15.736  -86.213 19.279  1.00 37.97  ?  100 ALA   C CA    1 
ATOM   2080 C C     . ALA   C 3 100 ? 15.229  -87.209 18.243  1.00 38.75  ?  100 ALA   C C     1 
ATOM   2081 O O     . ALA   C 3 100 ? 16.010  -87.660 17.409  1.00 39.37  ?  100 ALA   C O     1 
ATOM   2082 C CB    . ALA   C 3 100 ? 15.566  -84.800 18.800  1.00 36.52  ?  100 ALA   C CB    1 
ATOM   2083 N N     . SER   C 3 101 ? 13.903  -87.413 18.251  1.00 37.37  ?  101 SER   C N     1 
ATOM   2084 C CA    . SER   C 3 101 ? 13.222  -88.221 17.254  1.00 39.00  ?  101 SER   C CA    1 
ATOM   2085 C C     . SER   C 3 101 ? 11.851  -87.625 16.907  1.00 37.00  ?  101 SER   C C     1 
ATOM   2086 O O     . SER   C 3 101 ? 11.223  -87.006 17.768  1.00 33.96  ?  101 SER   C O     1 
ATOM   2087 C CB    . SER   C 3 101 ? 13.110  -89.660 17.750  1.00 40.74  ?  101 SER   C CB    1 
ATOM   2088 O OG    . SER   C 3 101 ? 12.226  -89.745 18.852  1.00 40.09  ?  101 SER   C OG    1 
ATOM   2089 N N     . ILE   C 3 102 ? 11.381  -87.908 15.679  1.00 37.97  ?  102 ILE   C N     1 
ATOM   2090 C CA    . ILE   C 3 102 ? 10.137  -87.392 15.116  1.00 37.96  ?  102 ILE   C CA    1 
ATOM   2091 C C     . ILE   C 3 102 ? 9.323   -88.594 14.655  1.00 38.99  ?  102 ILE   C C     1 
ATOM   2092 O O     . ILE   C 3 102 ? 9.732   -89.210 13.673  1.00 40.91  ?  102 ILE   C O     1 
ATOM   2093 C CB    . ILE   C 3 102 ? 10.372  -86.429 13.928  1.00 37.59  ?  102 ILE   C CB    1 
ATOM   2094 C CG1   . ILE   C 3 102 ? 11.431  -85.374 14.191  1.00 37.24  ?  102 ILE   C CG1   1 
ATOM   2095 C CG2   . ILE   C 3 102 ? 9.045   -85.836 13.446  1.00 37.19  ?  102 ILE   C CG2   1 
ATOM   2096 C CD1   . ILE   C 3 102 ? 11.077  -84.362 15.234  1.00 35.74  ?  102 ILE   C CD1   1 
ATOM   2097 N N     . ASN   C 3 103 ? 8.187   -88.891 15.308  1.00 38.91  ?  103 ASN   C N     1 
ATOM   2098 C CA    . ASN   C 3 103 ? 7.341   -90.038 14.971  1.00 42.30  ?  103 ASN   C CA    1 
ATOM   2099 C C     . ASN   C 3 103 ? 8.161   -91.350 14.934  1.00 44.36  ?  103 ASN   C C     1 
ATOM   2100 O O     . ASN   C 3 103 ? 8.271   -91.976 13.889  1.00 45.17  ?  103 ASN   C O     1 
ATOM   2101 C CB    . ASN   C 3 103 ? 6.626   -89.822 13.628  1.00 42.76  ?  103 ASN   C CB    1 
ATOM   2102 C CG    . ASN   C 3 103 ? 5.670   -88.662 13.598  1.00 40.82  ?  103 ASN   C CG    1 
ATOM   2103 O OD1   . ASN   C 3 103 ? 5.018   -88.373 14.604  1.00 39.71  ?  103 ASN   C OD1   1 
ATOM   2104 N ND2   . ASN   C 3 103 ? 5.468   -88.088 12.419  1.00 40.32  ?  103 ASN   C ND2   1 
ATOM   2105 N N     . GLY   C 3 104 ? 8.947   -91.608 15.985  1.00 44.94  ?  104 GLY   C N     1 
ATOM   2106 C CA    . GLY   C 3 104 ? 9.725   -92.834 16.129  1.00 48.66  ?  104 GLY   C CA    1 
ATOM   2107 C C     . GLY   C 3 104 ? 10.969  -93.004 15.244  1.00 50.75  ?  104 GLY   C C     1 
ATOM   2108 O O     . GLY   C 3 104 ? 11.452  -94.139 15.178  1.00 54.08  ?  104 GLY   C O     1 
ATOM   2109 N N     . LYS   C 3 105 ? 11.453  -91.961 14.529  1.00 49.30  ?  105 LYS   C N     1 
ATOM   2110 C CA    . LYS   C 3 105 ? 12.722  -92.013 13.799  1.00 51.35  ?  105 LYS   C CA    1 
ATOM   2111 C C     . LYS   C 3 105 ? 13.622  -90.914 14.364  1.00 48.87  ?  105 LYS   C C     1 
ATOM   2112 O O     . LYS   C 3 105 ? 13.163  -89.780 14.470  1.00 47.86  ?  105 LYS   C O     1 
ATOM   2113 C CB    . LYS   C 3 105 ? 12.526  -91.905 12.272  1.00 53.89  ?  105 LYS   C CB    1 
ATOM   2114 C CG    . LYS   C 3 105 ? 13.623  -92.566 11.441  1.00 59.03  ?  105 LYS   C CG    1 
ATOM   2115 C CD    . LYS   C 3 105 ? 13.457  -92.628 9.919   1.00 62.86  ?  105 LYS   C CD    1 
ATOM   2116 C CE    . LYS   C 3 105 ? 12.475  -93.638 9.384   1.00 66.48  ?  105 LYS   C CE    1 
ATOM   2117 N NZ    . LYS   C 3 105 ? 12.791  -95.056 9.634   1.00 70.18  1  105 LYS   C NZ    1 
ATOM   2118 N N     . ALA   C 3 106 ? 14.874  -91.233 14.735  1.00 49.98  ?  106 ALA   C N     1 
ATOM   2119 C CA    . ALA   C 3 106 ? 15.869  -90.259 15.180  1.00 48.48  ?  106 ALA   C CA    1 
ATOM   2120 C C     . ALA   C 3 106 ? 16.235  -89.311 14.045  1.00 48.89  ?  106 ALA   C C     1 
ATOM   2121 O O     . ALA   C 3 106 ? 16.335  -89.764 12.903  1.00 52.08  ?  106 ALA   C O     1 
ATOM   2122 C CB    . ALA   C 3 106 ? 17.139  -90.954 15.640  1.00 50.55  ?  106 ALA   C CB    1 
ATOM   2123 N N     . VAL   C 3 107 ? 16.522  -88.041 14.385  1.00 46.32  ?  107 VAL   C N     1 
ATOM   2124 C CA    . VAL   C 3 107 ? 16.787  -86.965 13.438  1.00 45.86  ?  107 VAL   C CA    1 
ATOM   2125 C C     . VAL   C 3 107 ? 18.075  -86.243 13.844  1.00 48.12  ?  107 VAL   C C     1 
ATOM   2126 O O     . VAL   C 3 107 ? 18.446  -86.274 15.025  1.00 49.36  ?  107 VAL   C O     1 
ATOM   2127 C CB    . VAL   C 3 107 ? 15.577  -86.007 13.353  1.00 44.90  ?  107 VAL   C CB    1 
ATOM   2128 C CG1   . VAL   C 3 107 ? 14.372  -86.632 12.660  1.00 46.15  ?  107 VAL   C CG1   1 
ATOM   2129 C CG2   . VAL   C 3 107 ? 15.122  -85.424 14.693  1.00 43.48  ?  107 VAL   C CG2   1 
ATOM   2130 N N     . SER   C 3 108 ? 18.750  -85.598 12.863  1.00 48.72  ?  108 SER   C N     1 
ATOM   2131 C CA    . SER   C 3 108 ? 20.003  -84.868 13.053  1.00 47.49  ?  108 SER   C CA    1 
ATOM   2132 C C     . SER   C 3 108 ? 19.679  -83.460 13.569  1.00 43.61  ?  108 SER   C C     1 
ATOM   2133 O O     . SER   C 3 108 ? 19.789  -82.474 12.852  1.00 45.11  ?  108 SER   C O     1 
ATOM   2134 C CB    . SER   C 3 108 ? 20.839  -84.862 11.780  1.00 50.13  ?  108 SER   C CB    1 
ATOM   2135 O OG    . SER   C 3 108 ? 20.163  -84.196 10.719  1.00 49.87  ?  108 SER   C OG    1 
ATOM   2136 N N     . VAL   C 3 109 ? 19.281  -83.392 14.846  1.00 43.26  ?  109 VAL   C N     1 
ATOM   2137 C CA    . VAL   C 3 109 ? 18.731  -82.204 15.502  1.00 39.62  ?  109 VAL   C CA    1 
ATOM   2138 C C     . VAL   C 3 109 ? 19.761  -81.079 15.644  1.00 39.94  ?  109 VAL   C C     1 
ATOM   2139 O O     . VAL   C 3 109 ? 19.353  -79.902 15.679  1.00 35.41  ?  109 VAL   C O     1 
ATOM   2140 C CB    . VAL   C 3 109 ? 18.085  -82.558 16.863  1.00 40.16  ?  109 VAL   C CB    1 
ATOM   2141 C CG1   . VAL   C 3 109 ? 19.060  -83.132 17.910  1.00 41.79  ?  109 VAL   C CG1   1 
ATOM   2142 C CG2   . VAL   C 3 109 ? 17.301  -81.388 17.457  1.00 36.48  ?  109 VAL   C CG2   1 
ATOM   2143 N N     . GLU   C 3 110 ? 21.071  -81.414 15.671  1.00 41.23  ?  110 GLU   C N     1 
ATOM   2144 C CA    . GLU   C 3 110 ? 22.140  -80.421 15.697  1.00 42.65  ?  110 GLU   C CA    1 
ATOM   2145 C C     . GLU   C 3 110 ? 22.236  -79.598 14.402  1.00 41.64  ?  110 GLU   C C     1 
ATOM   2146 O O     . GLU   C 3 110 ? 22.771  -78.492 14.461  1.00 38.60  ?  110 GLU   C O     1 
ATOM   2147 C CB    . GLU   C 3 110 ? 23.462  -81.096 16.073  1.00 47.73  ?  110 GLU   C CB    1 
ATOM   2148 C CG    . GLU   C 3 110 ? 23.512  -81.560 17.530  1.00 49.96  ?  110 GLU   C CG    1 
ATOM   2149 C CD    . GLU   C 3 110 ? 24.484  -82.683 17.776  1.00 55.72  ?  110 GLU   C CD    1 
ATOM   2150 O OE1   . GLU   C 3 110 ? 24.188  -83.541 18.628  1.00 61.91  ?  110 GLU   C OE1   1 
ATOM   2151 O OE2   . GLU   C 3 110 ? 25.529  -82.700 17.099  1.00 61.62  -1 110 GLU   C OE2   1 
ATOM   2152 N N     . LYS   C 3 111 ? 21.783  -80.151 13.255  1.00 42.57  ?  111 LYS   C N     1 
ATOM   2153 C CA    . LYS   C 3 111 ? 21.686  -79.398 12.005  1.00 42.98  ?  111 LYS   C CA    1 
ATOM   2154 C C     . LYS   C 3 111 ? 20.284  -78.788 11.821  1.00 38.49  ?  111 LYS   C C     1 
ATOM   2155 O O     . LYS   C 3 111 ? 20.072  -78.142 10.818  1.00 38.42  ?  111 LYS   C O     1 
ATOM   2156 C CB    . LYS   C 3 111 ? 22.387  -80.067 10.806  1.00 45.87  ?  111 LYS   C CB    1 
ATOM   2157 C CG    . LYS   C 3 111 ? 22.115  -81.513 10.413  1.00 50.07  ?  111 LYS   C CG    1 
ATOM   2158 N N     . GLY   C 3 112 ? 19.346  -78.891 12.772  1.00 34.66  ?  112 GLY   C N     1 
ATOM   2159 C CA    . GLY   C 3 112 ? 18.044  -78.249 12.687  1.00 33.34  ?  112 GLY   C CA    1 
ATOM   2160 C C     . GLY   C 3 112 ? 17.098  -79.064 11.804  1.00 33.52  ?  112 GLY   C C     1 
ATOM   2161 O O     . GLY   C 3 112 ? 17.487  -79.453 10.726  1.00 33.83  ?  112 GLY   C O     1 
ATOM   2162 N N     . VAL   C 3 113 ? 15.885  -79.388 12.272  1.00 32.33  ?  113 VAL   C N     1 
ATOM   2163 C CA    . VAL   C 3 113 ? 15.007  -80.334 11.578  1.00 35.86  ?  113 VAL   C CA    1 
ATOM   2164 C C     . VAL   C 3 113 ? 13.569  -79.798 11.598  1.00 33.71  ?  113 VAL   C C     1 
ATOM   2165 O O     . VAL   C 3 113 ? 13.100  -79.377 12.655  1.00 31.12  ?  113 VAL   C O     1 
ATOM   2166 C CB    . VAL   C 3 113 ? 15.113  -81.792 12.117  1.00 37.90  ?  113 VAL   C CB    1 
ATOM   2167 C CG1   . VAL   C 3 113 ? 14.170  -82.772 11.403  1.00 40.15  ?  113 VAL   C CG1   1 
ATOM   2168 C CG2   . VAL   C 3 113 ? 16.539  -82.314 11.935  1.00 40.07  ?  113 VAL   C CG2   1 
ATOM   2169 N N     . GLN   C 3 114 ? 12.876  -79.929 10.440  1.00 33.39  ?  114 GLN   C N     1 
ATOM   2170 C CA    . GLN   C 3 114 ? 11.494  -79.500 10.252  1.00 32.55  ?  114 GLN   C CA    1 
ATOM   2171 C C     . GLN   C 3 114 ? 10.660  -80.698 9.782   1.00 33.54  ?  114 GLN   C C     1 
ATOM   2172 O O     . GLN   C 3 114 ? 11.062  -81.342 8.826   1.00 35.11  ?  114 GLN   C O     1 
ATOM   2173 C CB    . GLN   C 3 114 ? 11.407  -78.347 9.245   1.00 31.86  ?  114 GLN   C CB    1 
ATOM   2174 C CG    . GLN   C 3 114 ? 10.024  -77.708 9.122   1.00 30.70  ?  114 GLN   C CG    1 
ATOM   2175 C CD    . GLN   C 3 114 ? 9.971   -76.615 8.079   1.00 30.17  ?  114 GLN   C CD    1 
ATOM   2176 O OE1   . GLN   C 3 114 ? 10.764  -75.680 8.144   1.00 28.46  ?  114 GLN   C OE1   1 
ATOM   2177 N NE2   . GLN   C 3 114 ? 9.038   -76.684 7.125   1.00 31.78  ?  114 GLN   C NE2   1 
ATOM   2178 N N     . TYR   C 3 115 ? 9.456   -80.874 10.367  1.00 32.14  ?  115 TYR   C N     1 
ATOM   2179 C CA    . TYR   C 3 115 ? 8.484   -81.829 9.892   1.00 34.17  ?  115 TYR   C CA    1 
ATOM   2180 C C     . TYR   C 3 115 ? 7.112   -81.176 9.703   1.00 33.47  ?  115 TYR   C C     1 
ATOM   2181 O O     . TYR   C 3 115 ? 6.630   -80.531 10.627  1.00 34.31  ?  115 TYR   C O     1 
ATOM   2182 C CB    . TYR   C 3 115 ? 8.463   -83.018 10.855  1.00 34.40  ?  115 TYR   C CB    1 
ATOM   2183 C CG    . TYR   C 3 115 ? 7.675   -84.157 10.242  1.00 36.33  ?  115 TYR   C CG    1 
ATOM   2184 C CD1   . TYR   C 3 115 ? 8.287   -85.083 9.388   1.00 38.59  ?  115 TYR   C CD1   1 
ATOM   2185 C CD2   . TYR   C 3 115 ? 6.297   -84.264 10.463  1.00 36.64  ?  115 TYR   C CD2   1 
ATOM   2186 C CE1   . TYR   C 3 115 ? 7.545   -86.112 8.799   1.00 41.67  ?  115 TYR   C CE1   1 
ATOM   2187 C CE2   . TYR   C 3 115 ? 5.549   -85.285 9.884   1.00 39.99  ?  115 TYR   C CE2   1 
ATOM   2188 C CZ    . TYR   C 3 115 ? 6.177   -86.210 9.052   1.00 41.81  ?  115 TYR   C CZ    1 
ATOM   2189 O OH    . TYR   C 3 115 ? 5.407   -87.162 8.495   1.00 44.04  ?  115 TYR   C OH    1 
ATOM   2190 N N     . PRO   C 3 116 ? 6.374   -81.398 8.586   1.00 34.81  ?  116 PRO   C N     1 
ATOM   2191 C CA    . PRO   C 3 116 ? 6.921   -81.839 7.295   1.00 36.86  ?  116 PRO   C CA    1 
ATOM   2192 C C     . PRO   C 3 116 ? 8.025   -80.917 6.781   1.00 37.35  ?  116 PRO   C C     1 
ATOM   2193 O O     . PRO   C 3 116 ? 7.906   -79.691 6.938   1.00 36.68  ?  116 PRO   C O     1 
ATOM   2194 C CB    . PRO   C 3 116 ? 5.720   -81.824 6.358   1.00 38.22  ?  116 PRO   C CB    1 
ATOM   2195 C CG    . PRO   C 3 116 ? 4.547   -82.043 7.296   1.00 37.95  ?  116 PRO   C CG    1 
ATOM   2196 C CD    . PRO   C 3 116 ? 4.907   -81.310 8.563   1.00 35.50  ?  116 PRO   C CD    1 
ATOM   2197 N N     . GLN   C 3 117 ? 9.112   -81.495 6.249   1.00 39.77  ?  117 GLN   C N     1 
ATOM   2198 C CA    . GLN   C 3 117 ? 10.270  -80.754 5.756   1.00 41.87  ?  117 GLN   C CA    1 
ATOM   2199 C C     . GLN   C 3 117 ? 9.889   -79.705 4.699   1.00 43.12  ?  117 GLN   C C     1 
ATOM   2200 O O     . GLN   C 3 117 ? 10.486  -78.636 4.714   1.00 43.53  ?  117 GLN   C O     1 
ATOM   2201 C CB    . GLN   C 3 117 ? 11.337  -81.698 5.216   1.00 46.36  ?  117 GLN   C CB    1 
ATOM   2202 C CG    . GLN   C 3 117 ? 12.731  -81.095 5.075   1.00 49.22  ?  117 GLN   C CG    1 
ATOM   2203 C CD    . GLN   C 3 117 ? 13.675  -81.912 4.214   1.00 55.36  ?  117 GLN   C CD    1 
ATOM   2204 O OE1   . GLN   C 3 117 ? 13.650  -83.149 4.205   1.00 58.65  ?  117 GLN   C OE1   1 
ATOM   2205 N NE2   . GLN   C 3 117 ? 14.516  -81.226 3.450   1.00 59.90  ?  117 GLN   C NE2   1 
ATOM   2206 N N     . ASP   C 3 118 ? 8.874   -79.989 3.859   1.00 46.98  ?  118 ASP   C N     1 
ATOM   2207 C CA    . ASP   C 3 118 ? 8.378   -79.122 2.807   1.00 50.01  ?  118 ASP   C CA    1 
ATOM   2208 C C     . ASP   C 3 118 ? 7.309   -78.110 3.247   1.00 47.12  ?  118 ASP   C C     1 
ATOM   2209 O O     . ASP   C 3 118 ? 6.957   -77.269 2.423   1.00 47.04  ?  118 ASP   C O     1 
ATOM   2210 C CB    . ASP   C 3 118 ? 7.861   -79.957 1.633   1.00 58.33  ?  118 ASP   C CB    1 
ATOM   2211 C CG    . ASP   C 3 118 ? 6.501   -80.630 1.806   1.00 65.23  ?  118 ASP   C CG    1 
ATOM   2212 O OD1   . ASP   C 3 118 ? 6.294   -81.280 2.886   1.00 64.14  ?  118 ASP   C OD1   1 
ATOM   2213 O OD2   . ASP   C 3 118 ? 5.680   -80.515 0.853   1.00 71.76  -1 118 ASP   C OD2   1 
ATOM   2214 N N     . ASP   C 3 119 ? 6.714   -78.215 4.456   1.00 44.64  ?  119 ASP   C N     1 
ATOM   2215 C CA    . ASP   C 3 119 ? 5.462   -77.523 4.766   1.00 43.54  ?  119 ASP   C CA    1 
ATOM   2216 C C     . ASP   C 3 119 ? 5.808   -76.235 5.505   1.00 39.10  ?  119 ASP   C C     1 
ATOM   2217 O O     . ASP   C 3 119 ? 6.310   -76.352 6.616   1.00 36.96  ?  119 ASP   C O     1 
ATOM   2218 C CB    . ASP   C 3 119 ? 4.444   -78.403 5.492   1.00 45.47  ?  119 ASP   C CB    1 
ATOM   2219 C CG    . ASP   C 3 119 ? 3.035   -77.833 5.678   1.00 47.03  ?  119 ASP   C CG    1 
ATOM   2220 O OD1   . ASP   C 3 119 ? 2.764   -76.683 5.252   1.00 49.22  ?  119 ASP   C OD1   1 
ATOM   2221 O OD2   . ASP   C 3 119 ? 2.187   -78.539 6.260   1.00 47.27  -1 119 ASP   C OD2   1 
ATOM   2222 N N     . PRO   C 3 120 ? 5.549   -75.003 4.974   1.00 39.37  ?  120 PRO   C N     1 
ATOM   2223 C CA    . PRO   C 3 120 ? 5.737   -73.777 5.758   1.00 36.19  ?  120 PRO   C CA    1 
ATOM   2224 C C     . PRO   C 3 120 ? 4.871   -73.704 7.016   1.00 34.96  ?  120 PRO   C C     1 
ATOM   2225 O O     . PRO   C 3 120 ? 5.319   -73.142 8.014   1.00 33.13  ?  120 PRO   C O     1 
ATOM   2226 C CB    . PRO   C 3 120 ? 5.399   -72.649 4.797   1.00 37.39  ?  120 PRO   C CB    1 
ATOM   2227 C CG    . PRO   C 3 120 ? 4.526   -73.270 3.750   1.00 39.59  ?  120 PRO   C CG    1 
ATOM   2228 C CD    . PRO   C 3 120 ? 4.967   -74.709 3.645   1.00 40.81  ?  120 PRO   C CD    1 
ATOM   2229 N N     . ASN   C 3 121 ? 3.658   -74.300 6.986   1.00 35.52  ?  121 ASN   C N     1 
ATOM   2230 C CA    . ASN   C 3 121 ? 2.858   -74.545 8.181   1.00 34.81  ?  121 ASN   C CA    1 
ATOM   2231 C C     . ASN   C 3 121 ? 3.329   -75.841 8.839   1.00 35.00  ?  121 ASN   C C     1 
ATOM   2232 O O     . ASN   C 3 121 ? 2.577   -76.796 8.950   1.00 35.52  ?  121 ASN   C O     1 
ATOM   2233 C CB    . ASN   C 3 121 ? 1.362   -74.487 7.865   1.00 36.42  ?  121 ASN   C CB    1 
ATOM   2234 C CG    . ASN   C 3 121 ? 0.502   -74.567 9.105   1.00 35.69  ?  121 ASN   C CG    1 
ATOM   2235 O OD1   . ASN   C 3 121 ? 0.818   -73.961 10.136  1.00 35.67  ?  121 ASN   C OD1   1 
ATOM   2236 N ND2   . ASN   C 3 121 ? -0.552  -75.360 9.054   1.00 38.12  ?  121 ASN   C ND2   1 
ATOM   2237 N N     . TYR   C 3 122 ? 4.560   -75.817 9.376   1.00 33.50  ?  122 TYR   C N     1 
ATOM   2238 C CA    . TYR   C 3 122 ? 5.201   -77.012 9.901   1.00 32.89  ?  122 TYR   C CA    1 
ATOM   2239 C C     . TYR   C 3 122 ? 4.584   -77.350 11.263  1.00 32.17  ?  122 TYR   C C     1 
ATOM   2240 O O     . TYR   C 3 122 ? 4.245   -76.465 12.046  1.00 30.51  ?  122 TYR   C O     1 
ATOM   2241 C CB    . TYR   C 3 122 ? 6.723   -76.895 10.014  1.00 31.05  ?  122 TYR   C CB    1 
ATOM   2242 C CG    . TYR   C 3 122 ? 7.254   -75.704 10.797  1.00 29.20  ?  122 TYR   C CG    1 
ATOM   2243 C CD1   . TYR   C 3 122 ? 7.335   -75.718 12.190  1.00 27.33  ?  122 TYR   C CD1   1 
ATOM   2244 C CD2   . TYR   C 3 122 ? 7.654   -74.543 10.131  1.00 28.36  ?  122 TYR   C CD2   1 
ATOM   2245 C CE1   . TYR   C 3 122 ? 7.785   -74.609 12.895  1.00 25.37  ?  122 TYR   C CE1   1 
ATOM   2246 C CE2   . TYR   C 3 122 ? 8.126   -73.435 10.823  1.00 26.87  ?  122 TYR   C CE2   1 
ATOM   2247 C CZ    . TYR   C 3 122 ? 8.200   -73.484 12.204  1.00 25.93  ?  122 TYR   C CZ    1 
ATOM   2248 O OH    . TYR   C 3 122 ? 8.661   -72.401 12.871  1.00 28.34  ?  122 TYR   C OH    1 
ATOM   2249 N N     . ALA   C 3 123 ? 4.494   -78.654 11.545  1.00 32.84  ?  123 ALA   C N     1 
ATOM   2250 C CA    . ALA   C 3 123 ? 4.071   -79.178 12.836  1.00 30.26  ?  123 ALA   C CA    1 
ATOM   2251 C C     . ALA   C 3 123 ? 5.167   -78.971 13.877  1.00 28.77  ?  123 ALA   C C     1 
ATOM   2252 O O     . ALA   C 3 123 ? 4.845   -78.749 15.051  1.00 26.57  ?  123 ALA   C O     1 
ATOM   2253 C CB    . ALA   C 3 123 ? 3.740   -80.640 12.729  1.00 32.18  ?  123 ALA   C CB    1 
ATOM   2254 N N     . ILE   C 3 124 ? 6.445   -79.121 13.478  1.00 28.27  ?  124 ILE   C N     1 
ATOM   2255 C CA    . ILE   C 3 124 ? 7.535   -79.027 14.429  1.00 27.88  ?  124 ILE   C CA    1 
ATOM   2256 C C     . ILE   C 3 124 ? 8.797   -78.610 13.701  1.00 27.22  ?  124 ILE   C C     1 
ATOM   2257 O O     . ILE   C 3 124 ? 9.014   -79.014 12.574  1.00 29.31  ?  124 ILE   C O     1 
ATOM   2258 C CB    . ILE   C 3 124 ? 7.707   -80.319 15.275  1.00 29.86  ?  124 ILE   C CB    1 
ATOM   2259 C CG1   . ILE   C 3 124 ? 8.700   -80.154 16.438  1.00 29.41  ?  124 ILE   C CG1   1 
ATOM   2260 C CG2   . ILE   C 3 124 ? 8.061   -81.546 14.434  1.00 31.59  ?  124 ILE   C CG2   1 
ATOM   2261 C CD1   . ILE   C 3 124 ? 8.187   -79.261 17.554  1.00 29.10  ?  124 ILE   C CD1   1 
ATOM   2262 N N     . ARG   C 3 125 ? 9.554   -77.709 14.357  1.00 26.21  ?  125 ARG   C N     1 
ATOM   2263 C CA    . ARG   C 3 125 ? 10.958  -77.443 14.126  1.00 24.95  ?  125 ARG   C CA    1 
ATOM   2264 C C     . ARG   C 3 125 ? 11.685  -77.677 15.442  1.00 24.05  ?  125 ARG   C C     1 
ATOM   2265 O O     . ARG   C 3 125 ? 11.152  -77.350 16.501  1.00 22.05  ?  125 ARG   C O     1 
ATOM   2266 C CB    . ARG   C 3 125 ? 11.201  -75.979 13.733  1.00 24.82  ?  125 ARG   C CB    1 
ATOM   2267 C CG    . ARG   C 3 125 ? 11.094  -75.766 12.242  1.00 26.30  ?  125 ARG   C CG    1 
ATOM   2268 C CD    . ARG   C 3 125 ? 11.468  -74.397 11.872  1.00 26.59  ?  125 ARG   C CD    1 
ATOM   2269 N NE    . ARG   C 3 125 ? 11.134  -74.133 10.471  1.00 27.57  ?  125 ARG   C NE    1 
ATOM   2270 C CZ    . ARG   C 3 125 ? 11.281  -72.964 9.868   1.00 26.80  ?  125 ARG   C CZ    1 
ATOM   2271 N NH1   . ARG   C 3 125 ? 11.646  -71.897 10.548  1.00 26.83  1  125 ARG   C NH1   1 
ATOM   2272 N NH2   . ARG   C 3 125 ? 10.987  -72.873 8.590   1.00 28.62  ?  125 ARG   C NH2   1 
ATOM   2273 N N     . VAL   C 3 126 ? 12.919  -78.157 15.346  1.00 25.43  ?  126 VAL   C N     1 
ATOM   2274 C CA    . VAL   C 3 126 ? 13.736  -78.510 16.501  1.00 26.52  ?  126 VAL   C CA    1 
ATOM   2275 C C     . VAL   C 3 126 ? 15.210  -78.281 16.138  1.00 27.14  ?  126 VAL   C C     1 
ATOM   2276 O O     . VAL   C 3 126 ? 15.558  -78.496 14.989  1.00 27.58  ?  126 VAL   C O     1 
ATOM   2277 C CB    . VAL   C 3 126 ? 13.415  -79.955 16.995  1.00 27.62  ?  126 VAL   C CB    1 
ATOM   2278 C CG1   . VAL   C 3 126 ? 13.722  -81.042 15.977  1.00 29.58  ?  126 VAL   C CG1   1 
ATOM   2279 C CG2   . VAL   C 3 126 ? 14.062  -80.291 18.334  1.00 27.12  ?  126 VAL   C CG2   1 
ATOM   2280 N N     . TRP   C 3 127 ? 16.022  -77.815 17.116  1.00 27.42  ?  127 TRP   C N     1 
ATOM   2281 C CA    . TRP   C 3 127 ? 17.436  -77.474 16.918  1.00 28.61  ?  127 TRP   C CA    1 
ATOM   2282 C C     . TRP   C 3 127 ? 18.195  -77.632 18.227  1.00 28.94  ?  127 TRP   C C     1 
ATOM   2283 O O     . TRP   C 3 127 ? 17.651  -77.257 19.259  1.00 30.57  ?  127 TRP   C O     1 
ATOM   2284 C CB    . TRP   C 3 127 ? 17.599  -76.024 16.425  1.00 28.90  ?  127 TRP   C CB    1 
ATOM   2285 C CG    . TRP   C 3 127 ? 19.013  -75.500 16.293  1.00 28.82  ?  127 TRP   C CG    1 
ATOM   2286 C CD1   . TRP   C 3 127 ? 19.866  -75.671 15.240  1.00 30.06  ?  127 TRP   C CD1   1 
ATOM   2287 C CD2   . TRP   C 3 127 ? 19.693  -74.625 17.221  1.00 27.54  ?  127 TRP   C CD2   1 
ATOM   2288 N NE1   . TRP   C 3 127 ? 21.034  -74.984 15.457  1.00 30.76  ?  127 TRP   C NE1   1 
ATOM   2289 C CE2   . TRP   C 3 127 ? 20.957  -74.333 16.663  1.00 28.65  ?  127 TRP   C CE2   1 
ATOM   2290 C CE3   . TRP   C 3 127 ? 19.356  -74.057 18.466  1.00 27.60  ?  127 TRP   C CE3   1 
ATOM   2291 C CZ2   . TRP   C 3 127 ? 21.873  -73.481 17.290  1.00 28.96  ?  127 TRP   C CZ2   1 
ATOM   2292 C CZ3   . TRP   C 3 127 ? 20.254  -73.186 19.078  1.00 27.51  ?  127 TRP   C CZ3   1 
ATOM   2293 C CH2   . TRP   C 3 127 ? 21.498  -72.904 18.489  1.00 27.88  ?  127 TRP   C CH2   1 
ATOM   2294 N N     . LYS   C 3 128 ? 19.461  -78.089 18.149  1.00 31.65  ?  128 LYS   C N     1 
ATOM   2295 C CA    . LYS   C 3 128 ? 20.286  -78.382 19.312  1.00 31.50  ?  128 LYS   C CA    1 
ATOM   2296 C C     . LYS   C 3 128 ? 21.672  -77.731 19.188  1.00 30.30  ?  128 LYS   C C     1 
ATOM   2297 O O     . LYS   C 3 128 ? 22.295  -77.790 18.138  1.00 30.41  ?  128 LYS   C O     1 
ATOM   2298 C CB    . LYS   C 3 128 ? 20.334  -79.899 19.521  1.00 33.44  ?  128 LYS   C CB    1 
ATOM   2299 C CG    . LYS   C 3 128 ? 21.334  -80.440 20.575  1.00 33.91  ?  128 LYS   C CG    1 
ATOM   2300 C CD    . LYS   C 3 128 ? 21.168  -81.922 20.832  1.00 35.76  ?  128 LYS   C CD    1 
ATOM   2301 C CE    . LYS   C 3 128 ? 22.103  -82.431 21.869  1.00 37.62  ?  128 LYS   C CE    1 
ATOM   2302 N NZ    . LYS   C 3 128 ? 21.669  -83.722 22.407  1.00 39.30  1  128 LYS   C NZ    1 
ATOM   2303 N N     . SER   C 3 129 ? 22.159  -77.182 20.309  1.00 29.08  ?  129 SER   C N     1 
ATOM   2304 C CA    . SER   C 3 129 ? 23.495  -76.622 20.448  1.00 30.78  ?  129 SER   C CA    1 
ATOM   2305 C C     . SER   C 3 129 ? 23.945  -76.877 21.884  1.00 32.15  ?  129 SER   C C     1 
ATOM   2306 O O     . SER   C 3 129 ? 23.193  -76.524 22.809  1.00 31.34  ?  129 SER   C O     1 
ATOM   2307 C CB    . SER   C 3 129 ? 23.495  -75.149 20.112  1.00 29.94  ?  129 SER   C CB    1 
ATOM   2308 O OG    . SER   C 3 129 ? 24.749  -74.544 20.345  1.00 32.65  ?  129 SER   C OG    1 
ATOM   2309 N N     . GLY   C 3 130 ? 25.100  -77.562 22.062  1.00 33.14  ?  130 GLY   C N     1 
ATOM   2310 C CA    . GLY   C 3 130 ? 25.474  -78.183 23.325  1.00 32.89  ?  130 GLY   C CA    1 
ATOM   2311 C C     . GLY   C 3 130 ? 24.334  -79.072 23.821  1.00 32.54  ?  130 GLY   C C     1 
ATOM   2312 O O     . GLY   C 3 130 ? 23.802  -79.851 23.030  1.00 32.08  ?  130 GLY   C O     1 
ATOM   2313 N N     . ASP   C 3 131 ? 23.862  -78.828 25.054  1.00 32.08  ?  131 ASP   C N     1 
ATOM   2314 C CA    . ASP   C 3 131 ? 22.706  -79.515 25.621  1.00 32.02  ?  131 ASP   C CA    1 
ATOM   2315 C C     . ASP   C 3 131 ? 21.390  -78.726 25.479  1.00 30.83  ?  131 ASP   C C     1 
ATOM   2316 O O     . ASP   C 3 131 ? 20.366  -79.222 25.967  1.00 31.47  ?  131 ASP   C O     1 
ATOM   2317 C CB    . ASP   C 3 131 ? 23.026  -79.935 27.049  1.00 32.76  ?  131 ASP   C CB    1 
ATOM   2318 C CG    . ASP   C 3 131 ? 24.207  -80.882 27.219  1.00 35.82  ?  131 ASP   C CG    1 
ATOM   2319 O OD1   . ASP   C 3 131 ? 24.201  -81.905 26.526  1.00 36.72  ?  131 ASP   C OD1   1 
ATOM   2320 O OD2   . ASP   C 3 131 ? 25.076  -80.625 28.096  1.00 37.81  -1 131 ASP   C OD2   1 
ATOM   2321 N N     . LEU   C 3 132 ? 21.385  -77.540 24.836  1.00 29.33  ?  132 LEU   C N     1 
ATOM   2322 C CA    . LEU   C 3 132 ? 20.166  -76.779 24.610  1.00 29.01  ?  132 LEU   C CA    1 
ATOM   2323 C C     . LEU   C 3 132 ? 19.422  -77.406 23.435  1.00 29.32  ?  132 LEU   C C     1 
ATOM   2324 O O     . LEU   C 3 132 ? 20.045  -77.561 22.386  1.00 30.97  ?  132 LEU   C O     1 
ATOM   2325 C CB    . LEU   C 3 132 ? 20.451  -75.313 24.301  1.00 27.46  ?  132 LEU   C CB    1 
ATOM   2326 C CG    . LEU   C 3 132 ? 19.240  -74.456 23.919  1.00 25.72  ?  132 LEU   C CG    1 
ATOM   2327 C CD1   . LEU   C 3 132 ? 18.298  -74.279 25.081  1.00 24.08  ?  132 LEU   C CD1   1 
ATOM   2328 C CD2   . LEU   C 3 132 ? 19.770  -73.151 23.329  1.00 25.82  ?  132 LEU   C CD2   1 
ATOM   2329 N N     . VAL   C 3 133 ? 18.111  -77.664 23.603  1.00 27.09  ?  133 VAL   C N     1 
ATOM   2330 C CA    . VAL   C 3 133 ? 17.220  -77.954 22.486  1.00 26.28  ?  133 VAL   C CA    1 
ATOM   2331 C C     . VAL   C 3 133 ? 16.102  -76.907 22.483  1.00 24.65  ?  133 VAL   C C     1 
ATOM   2332 O O     . VAL   C 3 133 ? 15.467  -76.694 23.520  1.00 23.29  ?  133 VAL   C O     1 
ATOM   2333 C CB    . VAL   C 3 133 ? 16.651  -79.386 22.467  1.00 26.96  ?  133 VAL   C CB    1 
ATOM   2334 C CG1   . VAL   C 3 133 ? 15.844  -79.635 21.191  1.00 27.51  ?  133 VAL   C CG1   1 
ATOM   2335 C CG2   . VAL   C 3 133 ? 17.742  -80.448 22.620  1.00 28.64  ?  133 VAL   C CG2   1 
ATOM   2336 N N     . MET   C 3 134 ? 15.835  -76.307 21.310  1.00 23.99  ?  134 MET   C N     1 
ATOM   2337 C CA    . MET   C 3 134 ? 14.675  -75.453 21.126  1.00 22.31  ?  134 MET   C CA    1 
ATOM   2338 C C     . MET   C 3 134 ? 13.694  -76.179 20.219  1.00 22.40  ?  134 MET   C C     1 
ATOM   2339 O O     . MET   C 3 134 ? 14.097  -76.948 19.362  1.00 23.59  ?  134 MET   C O     1 
ATOM   2340 C CB    . MET   C 3 134 ? 15.023  -74.101 20.511  1.00 22.61  ?  134 MET   C CB    1 
ATOM   2341 C CG    . MET   C 3 134 ? 15.906  -73.182 21.313  1.00 23.69  ?  134 MET   C CG    1 
ATOM   2342 S SD    . MET   C 3 134 ? 15.745  -71.440 20.788  1.00 27.68  ?  134 MET   C SD    1 
ATOM   2343 C CE    . MET   C 3 134 ? 17.037  -70.715 21.796  1.00 26.89  ?  134 MET   C CE    1 
ATOM   2344 N N     . ALA   C 3 135 ? 12.393  -75.904 20.418  1.00 21.89  ?  135 ALA   C N     1 
ATOM   2345 C CA    . ALA   C 3 135 ? 11.363  -76.453 19.570  1.00 21.41  ?  135 ALA   C CA    1 
ATOM   2346 C C     . ALA   C 3 135 ? 10.233  -75.445 19.409  1.00 20.51  ?  135 ALA   C C     1 
ATOM   2347 O O     . ALA   C 3 135 ? 9.914   -74.768 20.379  1.00 20.73  ?  135 ALA   C O     1 
ATOM   2348 C CB    . ALA   C 3 135 ? 10.873  -77.753 20.163  1.00 21.81  ?  135 ALA   C CB    1 
ATOM   2349 N N     . TYR   C 3 136 ? 9.613   -75.435 18.233  1.00 20.05  ?  136 TYR   C N     1 
ATOM   2350 C CA    . TYR   C 3 136 ? 8.455   -74.593 17.962  1.00 20.12  ?  136 TYR   C CA    1 
ATOM   2351 C C     . TYR   C 3 136 ? 7.545   -75.285 16.957  1.00 21.58  ?  136 TYR   C C     1 
ATOM   2352 O O     . TYR   C 3 136 ? 8.033   -75.962 16.061  1.00 22.99  ?  136 TYR   C O     1 
ATOM   2353 C CB    . TYR   C 3 136 ? 8.883   -73.193 17.506  1.00 18.89  ?  136 TYR   C CB    1 
ATOM   2354 C CG    . TYR   C 3 136 ? 7.732   -72.223 17.354  1.00 18.14  ?  136 TYR   C CG    1 
ATOM   2355 C CD1   . TYR   C 3 136 ? 7.111   -71.707 18.478  1.00 17.09  ?  136 TYR   C CD1   1 
ATOM   2356 C CD2   . TYR   C 3 136 ? 7.212   -71.878 16.104  1.00 18.96  ?  136 TYR   C CD2   1 
ATOM   2357 C CE1   . TYR   C 3 136 ? 6.019   -70.859 18.383  1.00 16.63  ?  136 TYR   C CE1   1 
ATOM   2358 C CE2   . TYR   C 3 136 ? 6.123   -71.019 15.992  1.00 18.51  ?  136 TYR   C CE2   1 
ATOM   2359 C CZ    . TYR   C 3 136 ? 5.523   -70.519 17.145  1.00 17.78  ?  136 TYR   C CZ    1 
ATOM   2360 O OH    . TYR   C 3 136 ? 4.488   -69.636 17.102  1.00 18.97  ?  136 TYR   C OH    1 
ATOM   2361 N N     . SER   C 3 137 ? 6.233   -75.048 17.108  1.00 22.54  ?  137 SER   C N     1 
ATOM   2362 C CA    . SER   C 3 137 ? 5.221   -75.515 16.185  1.00 23.69  ?  137 SER   C CA    1 
ATOM   2363 C C     . SER   C 3 137 ? 4.474   -74.304 15.643  1.00 24.31  ?  137 SER   C C     1 
ATOM   2364 O O     . SER   C 3 137 ? 3.826   -73.609 16.408  1.00 23.98  ?  137 SER   C O     1 
ATOM   2365 C CB    . SER   C 3 137 ? 4.299   -76.439 16.892  1.00 23.26  ?  137 SER   C CB    1 
ATOM   2366 O OG    . SER   C 3 137 ? 3.228   -76.815 16.023  1.00 24.92  ?  137 SER   C OG    1 
ATOM   2367 N N     . ARG   C 3 138 ? 4.495   -74.111 14.324  1.00 26.69  ?  138 ARG   C N     1 
ATOM   2368 C CA    . ARG   C 3 138 ? 3.605   -73.153 13.677  1.00 28.15  ?  138 ARG   C CA    1 
ATOM   2369 C C     . ARG   C 3 138 ? 2.128   -73.568 13.769  1.00 28.66  ?  138 ARG   C C     1 
ATOM   2370 O O     . ARG   C 3 138 ? 1.294   -72.685 13.797  1.00 29.47  ?  138 ARG   C O     1 
ATOM   2371 C CB    . ARG   C 3 138 ? 4.009   -72.861 12.229  1.00 30.71  ?  138 ARG   C CB    1 
ATOM   2372 C CG    . ARG   C 3 138 ? 5.030   -71.739 12.159  1.00 34.83  ?  138 ARG   C CG    1 
ATOM   2373 C CD    . ARG   C 3 138 ? 5.389   -71.288 10.759  1.00 40.47  ?  138 ARG   C CD    1 
ATOM   2374 N NE    . ARG   C 3 138 ? 4.189   -70.867 10.013  1.00 46.06  ?  138 ARG   C NE    1 
ATOM   2375 C CZ    . ARG   C 3 138 ? 3.886   -69.622 9.721   1.00 51.38  ?  138 ARG   C CZ    1 
ATOM   2376 N NH1   . ARG   C 3 138 ? 4.832   -68.697 9.678   1.00 58.09  1  138 ARG   C NH1   1 
ATOM   2377 N NH2   . ARG   C 3 138 ? 2.654   -69.307 9.412   1.00 51.47  ?  138 ARG   C NH2   1 
ATOM   2378 N N     . ARG   C 3 139 ? 1.793   -74.860 13.856  1.00 28.55  ?  139 ARG   C N     1 
ATOM   2379 C CA    . ARG   C 3 139 ? 0.394   -75.271 13.924  1.00 30.12  ?  139 ARG   C CA    1 
ATOM   2380 C C     . ARG   C 3 139 ? -0.239  -74.889 15.268  1.00 29.26  ?  139 ARG   C C     1 
ATOM   2381 O O     . ARG   C 3 139 ? -1.284  -74.263 15.258  1.00 31.88  ?  139 ARG   C O     1 
ATOM   2382 C CB    . ARG   C 3 139 ? 0.219   -76.738 13.535  1.00 30.62  ?  139 ARG   C CB    1 
ATOM   2383 C CG    . ARG   C 3 139 ? 0.598   -76.964 12.082  1.00 31.27  ?  139 ARG   C CG    1 
ATOM   2384 C CD    . ARG   C 3 139 ? 0.326   -78.404 11.658  1.00 32.45  ?  139 ARG   C CD    1 
ATOM   2385 N NE    . ARG   C 3 139 ? 1.025   -78.764 10.421  1.00 32.83  ?  139 ARG   C NE    1 
ATOM   2386 C CZ    . ARG   C 3 139 ? 1.109   -79.985 9.880   1.00 34.97  ?  139 ARG   C CZ    1 
ATOM   2387 N NH1   . ARG   C 3 139 ? 0.613   -81.038 10.497  1.00 34.76  1  139 ARG   C NH1   1 
ATOM   2388 N NH2   . ARG   C 3 139 ? 1.684   -80.134 8.689   1.00 36.54  ?  139 ARG   C NH2   1 
ATOM   2389 N N     . THR   C 3 140 ? 0.410   -75.216 16.384  1.00 27.27  ?  140 THR   C N     1 
ATOM   2390 C CA    . THR   C 3 140 ? -0.124  -74.970 17.729  1.00 25.80  ?  140 THR   C CA    1 
ATOM   2391 C C     . THR   C 3 140 ? 0.333   -73.632 18.339  1.00 24.59  ?  140 THR   C C     1 
ATOM   2392 O O     . THR   C 3 140 ? -0.243  -73.242 19.346  1.00 26.68  ?  140 THR   C O     1 
ATOM   2393 C CB    . THR   C 3 140 ? 0.313   -76.149 18.613  1.00 24.36  ?  140 THR   C CB    1 
ATOM   2394 O OG1   . THR   C 3 140 ? 1.729   -76.201 18.631  1.00 21.96  ?  140 THR   C OG1   1 
ATOM   2395 C CG2   . THR   C 3 140 ? -0.204  -77.472 18.090  1.00 25.74  ?  140 THR   C CG2   1 
ATOM   2396 N N     . ALA   C 3 141 ? 1.406   -72.997 17.819  1.00 23.87  ?  141 ALA   C N     1 
ATOM   2397 C CA    . ALA   C 3 141 ? 2.157   -71.888 18.440  1.00 22.73  ?  141 ALA   C CA    1 
ATOM   2398 C C     . ALA   C 3 141 ? 2.785   -72.220 19.801  1.00 21.92  ?  141 ALA   C C     1 
ATOM   2399 O O     . ALA   C 3 141 ? 3.181   -71.294 20.508  1.00 21.25  ?  141 ALA   C O     1 
ATOM   2400 C CB    . ALA   C 3 141 ? 1.305   -70.609 18.500  1.00 22.82  ?  141 ALA   C CB    1 
ATOM   2401 N N     . VAL   C 3 142 ? 2.996   -73.509 20.139  1.00 20.99  ?  142 VAL   C N     1 
ATOM   2402 C CA    . VAL   C 3 142 ? 3.688   -73.877 21.364  1.00 20.32  ?  142 VAL   C CA    1 
ATOM   2403 C C     . VAL   C 3 142 ? 5.189   -73.835 21.072  1.00 18.44  ?  142 VAL   C C     1 
ATOM   2404 O O     . VAL   C 3 142 ? 5.668   -74.420 20.108  1.00 18.85  ?  142 VAL   C O     1 
ATOM   2405 C CB    . VAL   C 3 142 ? 3.245   -75.234 21.919  1.00 21.00  ?  142 VAL   C CB    1 
ATOM   2406 C CG1   . VAL   C 3 142 ? 4.105   -75.687 23.094  1.00 21.10  ?  142 VAL   C CG1   1 
ATOM   2407 C CG2   . VAL   C 3 142 ? 1.754   -75.171 22.265  1.00 22.34  ?  142 VAL   C CG2   1 
ATOM   2408 N N     . TYR   C 3 143 ? 5.900   -73.109 21.914  1.00 17.66  ?  143 TYR   C N     1 
ATOM   2409 C CA    . TYR   C 3 143 ? 7.344   -73.094 21.976  1.00 17.76  ?  143 TYR   C CA    1 
ATOM   2410 C C     . TYR   C 3 143 ? 7.745   -73.881 23.206  1.00 18.76  ?  143 TYR   C C     1 
ATOM   2411 O O     . TYR   C 3 143 ? 7.100   -73.831 24.271  1.00 18.61  ?  143 TYR   C O     1 
ATOM   2412 C CB    . TYR   C 3 143 ? 7.859   -71.660 22.128  1.00 17.12  ?  143 TYR   C CB    1 
ATOM   2413 C CG    . TYR   C 3 143 ? 9.361   -71.542 22.375  1.00 15.88  ?  143 TYR   C CG    1 
ATOM   2414 C CD1   . TYR   C 3 143 ? 10.269  -71.542 21.336  1.00 16.46  ?  143 TYR   C CD1   1 
ATOM   2415 C CD2   . TYR   C 3 143 ? 9.863   -71.396 23.663  1.00 15.43  ?  143 TYR   C CD2   1 
ATOM   2416 C CE1   . TYR   C 3 143 ? 11.643  -71.417 21.557  1.00 16.15  ?  143 TYR   C CE1   1 
ATOM   2417 C CE2   . TYR   C 3 143 ? 11.224  -71.287 23.895  1.00 15.10  ?  143 TYR   C CE2   1 
ATOM   2418 C CZ    . TYR   C 3 143 ? 12.119  -71.321 22.852  1.00 15.31  ?  143 TYR   C CZ    1 
ATOM   2419 O OH    . TYR   C 3 143 ? 13.438  -71.157 23.159  1.00 16.22  ?  143 TYR   C OH    1 
ATOM   2420 N N     . ALA   C 3 144 ? 8.893   -74.526 23.087  1.00 20.79  ?  144 ALA   C N     1 
ATOM   2421 C CA    . ALA   C 3 144 ? 9.535   -75.116 24.248  1.00 20.69  ?  144 ALA   C CA    1 
ATOM   2422 C C     . ALA   C 3 144 ? 11.039  -75.023 24.105  1.00 19.82  ?  144 ALA   C C     1 
ATOM   2423 O O     . ALA   C 3 144 ? 11.548  -74.988 22.986  1.00 20.39  ?  144 ALA   C O     1 
ATOM   2424 C CB    . ALA   C 3 144 ? 9.085   -76.557 24.377  1.00 22.20  ?  144 ALA   C CB    1 
ATOM   2425 N N     . TYR   C 3 145 ? 11.730  -75.053 25.244  1.00 20.01  ?  145 TYR   C N     1 
ATOM   2426 C CA    . TYR   C 3 145 ? 13.151  -75.404 25.223  1.00 20.62  ?  145 TYR   C CA    1 
ATOM   2427 C C     . TYR   C 3 145 ? 13.520  -76.288 26.397  1.00 21.33  ?  145 TYR   C C     1 
ATOM   2428 O O     . TYR   C 3 145 ? 12.805  -76.291 27.413  1.00 21.94  ?  145 TYR   C O     1 
ATOM   2429 C CB    . TYR   C 3 145 ? 14.035  -74.164 25.128  1.00 20.63  ?  145 TYR   C CB    1 
ATOM   2430 C CG    . TYR   C 3 145 ? 14.345  -73.371 26.393  1.00 20.51  ?  145 TYR   C CG    1 
ATOM   2431 C CD1   . TYR   C 3 145 ? 13.515  -72.326 26.809  1.00 20.76  ?  145 TYR   C CD1   1 
ATOM   2432 C CD2   . TYR   C 3 145 ? 15.527  -73.579 27.112  1.00 21.69  ?  145 TYR   C CD2   1 
ATOM   2433 C CE1   . TYR   C 3 145 ? 13.808  -71.560 27.938  1.00 20.39  ?  145 TYR   C CE1   1 
ATOM   2434 C CE2   . TYR   C 3 145 ? 15.843  -72.818 28.235  1.00 20.99  ?  145 TYR   C CE2   1 
ATOM   2435 C CZ    . TYR   C 3 145 ? 15.000  -71.780 28.618  1.00 20.33  ?  145 TYR   C CZ    1 
ATOM   2436 O OH    . TYR   C 3 145 ? 15.221  -70.990 29.689  1.00 19.93  ?  145 TYR   C OH    1 
ATOM   2437 N N     . TYR   C 3 146 ? 14.664  -76.969 26.229  1.00 23.10  ?  146 TYR   C N     1 
ATOM   2438 C CA    . TYR   C 3 146 ? 15.038  -78.159 26.983  1.00 25.71  ?  146 TYR   C CA    1 
ATOM   2439 C C     . TYR   C 3 146 ? 16.554  -78.194 27.206  1.00 25.68  ?  146 TYR   C C     1 
ATOM   2440 O O     . TYR   C 3 146 ? 17.305  -77.983 26.261  1.00 25.45  ?  146 TYR   C O     1 
ATOM   2441 C CB    . TYR   C 3 146 ? 14.524  -79.411 26.250  1.00 26.53  ?  146 TYR   C CB    1 
ATOM   2442 C CG    . TYR   C 3 146 ? 15.100  -80.766 26.662  1.00 30.20  ?  146 TYR   C CG    1 
ATOM   2443 C CD1   . TYR   C 3 146 ? 14.513  -81.512 27.689  1.00 30.42  ?  146 TYR   C CD1   1 
ATOM   2444 C CD2   . TYR   C 3 146 ? 16.200  -81.320 25.994  1.00 31.73  ?  146 TYR   C CD2   1 
ATOM   2445 C CE1   . TYR   C 3 146 ? 14.987  -82.768 28.026  1.00 32.80  ?  146 TYR   C CE1   1 
ATOM   2446 C CE2   . TYR   C 3 146 ? 16.718  -82.552 26.370  1.00 33.71  ?  146 TYR   C CE2   1 
ATOM   2447 C CZ    . TYR   C 3 146 ? 16.096  -83.290 27.370  1.00 33.25  ?  146 TYR   C CZ    1 
ATOM   2448 O OH    . TYR   C 3 146 ? 16.575  -84.507 27.744  1.00 32.65  ?  146 TYR   C OH    1 
ATOM   2449 N N     . THR   C 3 147 ? 16.972  -78.509 28.448  1.00 26.91  ?  147 THR   C N     1 
ATOM   2450 C CA    . THR   C 3 147 ? 18.376  -78.564 28.873  1.00 27.90  ?  147 THR   C CA    1 
ATOM   2451 C C     . THR   C 3 147 ? 18.869  -79.979 29.222  1.00 29.24  ?  147 THR   C C     1 
ATOM   2452 O O     . THR   C 3 147 ? 20.070  -80.122 29.507  1.00 29.16  ?  147 THR   C O     1 
ATOM   2453 C CB    . THR   C 3 147 ? 18.508  -77.674 30.108  1.00 29.18  ?  147 THR   C CB    1 
ATOM   2454 O OG1   . THR   C 3 147 ? 17.744  -78.251 31.182  1.00 29.41  ?  147 THR   C OG1   1 
ATOM   2455 C CG2   . THR   C 3 147 ? 18.105  -76.238 29.818  1.00 27.69  ?  147 THR   C CG2   1 
ATOM   2456 N N     . GLY   C 3 148 ? 17.960  -80.983 29.328  1.00 29.49  ?  148 GLY   C N     1 
ATOM   2457 C CA    . GLY   C 3 148 ? 18.243  -82.238 30.016  1.00 32.81  ?  148 GLY   C CA    1 
ATOM   2458 C C     . GLY   C 3 148 ? 17.799  -82.266 31.484  1.00 34.15  ?  148 GLY   C C     1 
ATOM   2459 O O     . GLY   C 3 148 ? 17.451  -83.349 31.966  1.00 35.91  ?  148 GLY   C O     1 
ATOM   2460 N N     . THR   C 3 149 ? 17.897  -81.116 32.199  1.00 33.86  ?  149 THR   C N     1 
ATOM   2461 C CA    . THR   C 3 149 ? 17.522  -80.954 33.605  1.00 32.69  ?  149 THR   C CA    1 
ATOM   2462 C C     . THR   C 3 149 ? 16.092  -80.431 33.717  1.00 31.51  ?  149 THR   C C     1 
ATOM   2463 O O     . THR   C 3 149 ? 15.424  -80.706 34.733  1.00 31.88  ?  149 THR   C O     1 
ATOM   2464 C CB    . THR   C 3 149 ? 18.510  -79.969 34.250  1.00 32.22  ?  149 THR   C CB    1 
ATOM   2465 O OG1   . THR   C 3 149 ? 19.783  -80.520 33.948  1.00 35.24  ?  149 THR   C OG1   1 
ATOM   2466 C CG2   . THR   C 3 149 ? 18.281  -79.756 35.732  1.00 32.72  ?  149 THR   C CG2   1 
ATOM   2467 N N     . ALA   C 3 150 ? 15.696  -79.540 32.785  1.00 29.79  ?  150 ALA   C N     1 
ATOM   2468 C CA    . ALA   C 3 150 ? 14.347  -79.009 32.750  1.00 26.37  ?  150 ALA   C CA    1 
ATOM   2469 C C     . ALA   C 3 150 ? 13.891  -78.736 31.326  1.00 24.36  ?  150 ALA   C C     1 
ATOM   2470 O O     . ALA   C 3 150 ? 14.696  -78.656 30.392  1.00 23.24  ?  150 ALA   C O     1 
ATOM   2471 C CB    . ALA   C 3 150 ? 14.301  -77.768 33.586  1.00 26.24  ?  150 ALA   C CB    1 
ATOM   2472 N N     . VAL   C 3 151 ? 12.580  -78.530 31.235  1.00 22.02  ?  151 VAL   C N     1 
ATOM   2473 C CA    . VAL   C 3 151 ? 11.925  -78.075 30.029  1.00 22.24  ?  151 VAL   C CA    1 
ATOM   2474 C C     . VAL   C 3 151 ? 11.072  -76.859 30.379  1.00 21.39  ?  151 VAL   C C     1 
ATOM   2475 O O     . VAL   C 3 151 ? 10.476  -76.812 31.467  1.00 21.16  ?  151 VAL   C O     1 
ATOM   2476 C CB    . VAL   C 3 151 ? 11.105  -79.201 29.376  1.00 23.75  ?  151 VAL   C CB    1 
ATOM   2477 C CG1   . VAL   C 3 151 ? 10.005  -79.776 30.275  1.00 25.66  ?  151 VAL   C CG1   1 
ATOM   2478 C CG2   . VAL   C 3 151 ? 10.512  -78.764 28.044  1.00 24.37  ?  151 VAL   C CG2   1 
ATOM   2479 N N     . ASP   C 3 152 ? 11.050  -75.879 29.458  1.00 20.44  ?  152 ASP   C N     1 
ATOM   2480 C CA    . ASP   C 3 152 ? 10.098  -74.784 29.454  1.00 18.95  ?  152 ASP   C CA    1 
ATOM   2481 C C     . ASP   C 3 152 ? 9.088   -75.103 28.376  1.00 18.22  ?  152 ASP   C C     1 
ATOM   2482 O O     . ASP   C 3 152 ? 9.508   -75.219 27.250  1.00 17.00  ?  152 ASP   C O     1 
ATOM   2483 C CB    . ASP   C 3 152 ? 10.826  -73.486 29.201  1.00 19.44  ?  152 ASP   C CB    1 
ATOM   2484 C CG    . ASP   C 3 152 ? 9.965   -72.246 28.962  1.00 20.18  ?  152 ASP   C CG    1 
ATOM   2485 O OD1   . ASP   C 3 152 ? 8.819   -72.217 29.424  1.00 19.25  ?  152 ASP   C OD1   1 
ATOM   2486 O OD2   . ASP   C 3 152 ? 10.460  -71.342 28.249  1.00 19.29  -1 152 ASP   C OD2   1 
ATOM   2487 N N     . VAL   C 3 153 ? 7.786   -75.225 28.707  1.00 18.70  ?  153 VAL   C N     1 
ATOM   2488 C CA    . VAL   C 3 153 ? 6.722   -75.353 27.708  1.00 18.17  ?  153 VAL   C CA    1 
ATOM   2489 C C     . VAL   C 3 153 ? 5.909   -74.050 27.808  1.00 18.35  ?  153 VAL   C C     1 
ATOM   2490 O O     . VAL   C 3 153 ? 5.370   -73.708 28.882  1.00 18.23  ?  153 VAL   C O     1 
ATOM   2491 C CB    . VAL   C 3 153 ? 5.871   -76.638 27.884  1.00 18.65  ?  153 VAL   C CB    1 
ATOM   2492 C CG1   . VAL   C 3 153 ? 4.793   -76.847 26.819  1.00 19.09  ?  153 VAL   C CG1   1 
ATOM   2493 C CG2   . VAL   C 3 153 ? 6.711   -77.905 27.978  1.00 18.97  ?  153 VAL   C CG2   1 
ATOM   2494 N N     . GLU   C 3 154 ? 5.828   -73.314 26.688  1.00 18.92  ?  154 GLU   C N     1 
ATOM   2495 C CA    . GLU   C 3 154 ? 5.155   -72.037 26.620  1.00 18.33  ?  154 GLU   C CA    1 
ATOM   2496 C C     . GLU   C 3 154 ? 3.993   -72.175 25.653  1.00 20.10  ?  154 GLU   C C     1 
ATOM   2497 O O     . GLU   C 3 154 ? 4.189   -72.407 24.453  1.00 18.32  ?  154 GLU   C O     1 
ATOM   2498 C CB    . GLU   C 3 154 ? 6.103   -70.973 26.117  1.00 19.31  ?  154 GLU   C CB    1 
ATOM   2499 C CG    . GLU   C 3 154 ? 7.444   -70.873 26.872  1.00 19.19  ?  154 GLU   C CG    1 
ATOM   2500 C CD    . GLU   C 3 154 ? 8.148   -69.555 26.666  1.00 19.06  ?  154 GLU   C CD    1 
ATOM   2501 O OE1   . GLU   C 3 154 ? 7.615   -68.681 25.983  1.00 21.03  ?  154 GLU   C OE1   1 
ATOM   2502 O OE2   . GLU   C 3 154 ? 9.201   -69.310 27.252  1.00 19.86  -1 154 GLU   C OE2   1 
ATOM   2503 N N     . GLN   C 3 155 ? 2.791   -71.983 26.200  1.00 20.39  ?  155 GLN   C N     1 
ATOM   2504 C CA    . GLN   C 3 155 ? 1.557   -72.022 25.434  1.00 20.70  ?  155 GLN   C CA    1 
ATOM   2505 C C     . GLN   C 3 155 ? 1.143   -70.582 25.101  1.00 20.76  ?  155 GLN   C C     1 
ATOM   2506 O O     . GLN   C 3 155 ? 1.380   -69.656 25.902  1.00 20.35  ?  155 GLN   C O     1 
ATOM   2507 C CB    . GLN   C 3 155 ? 0.483   -72.691 26.271  1.00 20.06  ?  155 GLN   C CB    1 
ATOM   2508 C CG    . GLN   C 3 155 ? 0.763   -74.160 26.559  1.00 21.58  ?  155 GLN   C CG    1 
ATOM   2509 C CD    . GLN   C 3 155 ? -0.176  -74.720 27.595  1.00 21.86  ?  155 GLN   C CD    1 
ATOM   2510 O OE1   . GLN   C 3 155 ? 0.156   -74.820 28.789  1.00 21.71  ?  155 GLN   C OE1   1 
ATOM   2511 N NE2   . GLN   C 3 155 ? -1.389  -74.988 27.128  1.00 22.63  ?  155 GLN   C NE2   1 
ATOM   2512 N N     . PRO   C 3 156 ? 0.456   -70.359 23.953  1.00 20.10  ?  156 PRO   C N     1 
ATOM   2513 C CA    . PRO   C 3 156 ? -0.162  -69.067 23.701  1.00 20.68  ?  156 PRO   C CA    1 
ATOM   2514 C C     . PRO   C 3 156 ? -1.392  -68.875 24.595  1.00 21.36  ?  156 PRO   C C     1 
ATOM   2515 O O     . PRO   C 3 156 ? -2.092  -69.851 24.905  1.00 21.72  ?  156 PRO   C O     1 
ATOM   2516 C CB    . PRO   C 3 156 ? -0.617  -69.147 22.241  1.00 21.85  ?  156 PRO   C CB    1 
ATOM   2517 C CG    . PRO   C 3 156 ? -0.938  -70.622 22.050  1.00 22.13  ?  156 PRO   C CG    1 
ATOM   2518 C CD    . PRO   C 3 156 ? 0.138   -71.351 22.902  1.00 21.10  ?  156 PRO   C CD    1 
ATOM   2519 N N     . VAL   C 3 157 ? -1.695  -67.610 24.910  1.00 20.99  ?  157 VAL   C N     1 
ATOM   2520 C CA    . VAL   C 3 157 ? -2.815  -67.274 25.778  1.00 21.72  ?  157 VAL   C CA    1 
ATOM   2521 C C     . VAL   C 3 157 ? -4.158  -67.658 25.158  1.00 21.67  ?  157 VAL   C C     1 
ATOM   2522 O O     . VAL   C 3 157 ? -5.122  -67.809 25.911  1.00 23.10  ?  157 VAL   C O     1 
ATOM   2523 C CB    . VAL   C 3 157 ? -2.774  -65.784 26.160  1.00 21.48  ?  157 VAL   C CB    1 
ATOM   2524 C CG1   . VAL   C 3 157 ? -3.107  -64.853 24.988  1.00 21.48  ?  157 VAL   C CG1   1 
ATOM   2525 C CG2   . VAL   C 3 157 ? -3.654  -65.492 27.364  1.00 22.77  ?  157 VAL   C CG2   1 
ATOM   2526 N N     . THR   C 3 158 ? -4.215  -67.777 23.811  1.00 21.93  ?  158 THR   C N     1 
ATOM   2527 C CA    . THR   C 3 158 ? -5.359  -68.293 23.051  1.00 23.30  ?  158 THR   C CA    1 
ATOM   2528 C C     . THR   C 3 158 ? -5.847  -69.668 23.515  1.00 23.81  ?  158 THR   C C     1 
ATOM   2529 O O     . THR   C 3 158 ? -6.927  -70.025 23.112  1.00 24.31  ?  158 THR   C O     1 
ATOM   2530 C CB    . THR   C 3 158 ? -5.090  -68.282 21.537  1.00 23.91  ?  158 THR   C CB    1 
ATOM   2531 O OG1   . THR   C 3 158 ? -3.827  -68.893 21.344  1.00 22.71  ?  158 THR   C OG1   1 
ATOM   2532 C CG2   . THR   C 3 158 ? -5.040  -66.898 20.922  1.00 23.91  ?  158 THR   C CG2   1 
ATOM   2533 N N     . TYR   C 3 159 ? -5.049  -70.457 24.268  1.00 23.14  ?  159 TYR   C N     1 
ATOM   2534 C CA    . TYR   C 3 159 ? -5.465  -71.695 24.908  1.00 25.06  ?  159 TYR   C CA    1 
ATOM   2535 C C     . TYR   C 3 159 ? -6.293  -71.520 26.193  1.00 26.28  ?  159 TYR   C C     1 
ATOM   2536 O O     . TYR   C 3 159 ? -6.798  -72.543 26.688  1.00 25.89  ?  159 TYR   C O     1 
ATOM   2537 C CB    . TYR   C 3 159 ? -4.193  -72.552 25.032  1.00 24.90  ?  159 TYR   C CB    1 
ATOM   2538 C CG    . TYR   C 3 159 ? -3.631  -73.186 23.750  1.00 24.86  ?  159 TYR   C CG    1 
ATOM   2539 C CD1   . TYR   C 3 159 ? -4.166  -72.946 22.469  1.00 26.03  ?  159 TYR   C CD1   1 
ATOM   2540 C CD2   . TYR   C 3 159 ? -2.561  -74.068 23.818  1.00 25.71  ?  159 TYR   C CD2   1 
ATOM   2541 C CE1   . TYR   C 3 159 ? -3.688  -73.593 21.340  1.00 26.80  ?  159 TYR   C CE1   1 
ATOM   2542 C CE2   . TYR   C 3 159 ? -2.059  -74.721 22.689  1.00 27.03  ?  159 TYR   C CE2   1 
ATOM   2543 C CZ    . TYR   C 3 159 ? -2.631  -74.479 21.442  1.00 27.77  ?  159 TYR   C CZ    1 
ATOM   2544 O OH    . TYR   C 3 159 ? -2.235  -75.037 20.261  1.00 29.12  ?  159 TYR   C OH    1 
ATOM   2545 N N     . ARG   C 3 160 ? -6.505  -70.271 26.680  1.00 26.00  ?  160 ARG   C N     1 
ATOM   2546 C CA    . ARG   C 3 160 ? -7.207  -70.002 27.937  1.00 26.98  ?  160 ARG   C CA    1 
ATOM   2547 C C     . ARG   C 3 160 ? -8.619  -70.582 27.901  1.00 27.98  ?  160 ARG   C C     1 
ATOM   2548 O O     . ARG   C 3 160 ? -9.319  -70.357 26.920  1.00 28.98  ?  160 ARG   C O     1 
ATOM   2549 C CB    . ARG   C 3 160 ? -7.259  -68.482 28.217  1.00 26.84  ?  160 ARG   C CB    1 
ATOM   2550 C CG    . ARG   C 3 160 ? -7.973  -67.983 29.469  1.00 27.13  ?  160 ARG   C CG    1 
ATOM   2551 C CD    . ARG   C 3 160 ? -7.812  -66.495 29.584  1.00 26.68  ?  160 ARG   C CD    1 
ATOM   2552 N NE    . ARG   C 3 160 ? -6.494  -66.148 30.120  1.00 25.95  ?  160 ARG   C NE    1 
ATOM   2553 C CZ    . ARG   C 3 160 ? -6.011  -64.891 30.245  1.00 26.41  ?  160 ARG   C CZ    1 
ATOM   2554 N NH1   . ARG   C 3 160 ? -4.763  -64.672 30.621  1.00 24.08  1  160 ARG   C NH1   1 
ATOM   2555 N NH2   . ARG   C 3 160 ? -6.764  -63.862 29.936  1.00 27.91  ?  160 ARG   C NH2   1 
ATOM   2556 N N     . GLY   C 3 161 ? -8.971  -71.376 28.933  1.00 28.78  ?  161 GLY   C N     1 
ATOM   2557 C CA    . GLY   C 3 161 ? -10.240 -72.098 29.029  1.00 29.42  ?  161 GLY   C CA    1 
ATOM   2558 C C     . GLY   C 3 161 ? -10.240 -73.503 28.401  1.00 29.68  ?  161 GLY   C C     1 
ATOM   2559 O O     . GLY   C 3 161 ? -11.261 -74.166 28.532  1.00 30.79  ?  161 GLY   C O     1 
ATOM   2560 N N     . ARG   C 3 162 ? -9.145  -73.921 27.718  1.00 29.01  ?  162 ARG   C N     1 
ATOM   2561 C CA    . ARG   C 3 162 ? -8.943  -75.241 27.130  1.00 29.53  ?  162 ARG   C CA    1 
ATOM   2562 C C     . ARG   C 3 162 ? -7.655  -75.928 27.611  1.00 28.52  ?  162 ARG   C C     1 
ATOM   2563 O O     . ARG   C 3 162 ? -7.375  -77.036 27.164  1.00 29.93  ?  162 ARG   C O     1 
ATOM   2564 C CB    . ARG   C 3 162 ? -8.898  -75.036 25.605  1.00 30.39  ?  162 ARG   C CB    1 
ATOM   2565 C CG    . ARG   C 3 162 ? -10.259 -74.678 25.012  1.00 31.87  ?  162 ARG   C CG    1 
ATOM   2566 C CD    . ARG   C 3 162 ? -10.227 -74.666 23.486  1.00 32.53  ?  162 ARG   C CD    1 
ATOM   2567 N NE    . ARG   C 3 162 ? -9.356  -73.609 22.955  1.00 33.00  ?  162 ARG   C NE    1 
ATOM   2568 C CZ    . ARG   C 3 162 ? -8.564  -73.630 21.868  1.00 34.02  ?  162 ARG   C CZ    1 
ATOM   2569 N NH1   . ARG   C 3 162 ? -8.563  -74.686 21.064  1.00 34.46  1  162 ARG   C NH1   1 
ATOM   2570 N NH2   . ARG   C 3 162 ? -7.801  -72.569 21.555  1.00 33.12  ?  162 ARG   C NH2   1 
ATOM   2571 N N     . ALA   C 3 163 ? -6.937  -75.361 28.595  1.00 27.18  ?  163 ALA   C N     1 
ATOM   2572 C CA    . ALA   C 3 163 ? -5.641  -75.867 29.013  1.00 25.63  ?  163 ALA   C CA    1 
ATOM   2573 C C     . ALA   C 3 163 ? -5.840  -76.988 30.023  1.00 27.37  ?  163 ALA   C C     1 
ATOM   2574 O O     . ALA   C 3 163 ? -6.739  -76.879 30.879  1.00 28.90  ?  163 ALA   C O     1 
ATOM   2575 C CB    . ALA   C 3 163 ? -4.890  -74.751 29.655  1.00 24.73  ?  163 ALA   C CB    1 
ATOM   2576 N N     . THR   C 3 164 ? -5.012  -78.038 29.938  1.00 27.09  ?  164 THR   C N     1 
ATOM   2577 C CA    . THR   C 3 164 ? -5.026  -79.164 30.886  1.00 28.83  ?  164 THR   C CA    1 
ATOM   2578 C C     . THR   C 3 164 ? -3.570  -79.431 31.281  1.00 28.33  ?  164 THR   C C     1 
ATOM   2579 O O     . THR   C 3 164 ? -2.669  -78.689 30.854  1.00 27.50  ?  164 THR   C O     1 
ATOM   2580 C CB    . THR   C 3 164 ? -5.685  -80.424 30.290  1.00 28.76  ?  164 THR   C CB    1 
ATOM   2581 O OG1   . THR   C 3 164 ? -4.905  -80.753 29.151  1.00 27.97  ?  164 THR   C OG1   1 
ATOM   2582 C CG2   . THR   C 3 164 ? -7.101  -80.227 29.789  1.00 29.59  ?  164 THR   C CG2   1 
ATOM   2583 N N     . GLY   C 3 165 ? -3.362  -80.489 32.086  1.00 27.32  ?  165 GLY   C N     1 
ATOM   2584 C CA    . GLY   C 3 165 ? -2.025  -80.897 32.484  1.00 27.55  ?  165 GLY   C CA    1 
ATOM   2585 C C     . GLY   C 3 165 ? -1.597  -80.190 33.768  1.00 26.40  ?  165 GLY   C C     1 
ATOM   2586 O O     . GLY   C 3 165 ? -2.299  -79.284 34.262  1.00 25.03  ?  165 GLY   C O     1 
ATOM   2587 N N     . LEU   C 3 166 ? -0.441  -80.634 34.304  1.00 25.74  ?  166 LEU   C N     1 
ATOM   2588 C CA    . LEU   C 3 166 ? 0.074   -80.100 35.570  1.00 25.53  ?  166 LEU   C CA    1 
ATOM   2589 C C     . LEU   C 3 166 ? 0.405   -78.601 35.529  1.00 23.89  ?  166 LEU   C C     1 
ATOM   2590 O O     . LEU   C 3 166 ? 0.323   -77.973 36.581  1.00 23.65  ?  166 LEU   C O     1 
ATOM   2591 C CB    . LEU   C 3 166 ? 1.259   -80.931 36.061  1.00 26.28  ?  166 LEU   C CB    1 
ATOM   2592 C CG    . LEU   C 3 166 ? 0.964   -82.389 36.425  1.00 27.45  ?  166 LEU   C CG    1 
ATOM   2593 C CD1   . LEU   C 3 166 ? 2.299   -83.021 36.807  1.00 28.47  ?  166 LEU   C CD1   1 
ATOM   2594 C CD2   . LEU   C 3 166 ? -0.071  -82.576 37.532  1.00 28.52  ?  166 LEU   C CD2   1 
ATOM   2595 N N     . CYS   C 3 167 ? 0.705   -78.008 34.343  1.00 23.31  ?  167 CYS   C N     1 
ATOM   2596 C CA    . CYS   C 3 167 ? 0.935   -76.574 34.215  1.00 22.56  ?  167 CYS   C CA    1 
ATOM   2597 C C     . CYS   C 3 167 ? -0.327  -75.745 34.528  1.00 23.57  ?  167 CYS   C C     1 
ATOM   2598 O O     . CYS   C 3 167 ? -0.219  -74.601 34.923  1.00 22.12  ?  167 CYS   C O     1 
ATOM   2599 C CB    . CYS   C 3 167 ? 1.483   -76.250 32.841  1.00 22.27  ?  167 CYS   C CB    1 
ATOM   2600 S SG    . CYS   C 3 167 ? 3.094   -77.009 32.503  1.00 21.15  ?  167 CYS   C SG    1 
ATOM   2601 N N     . GLY   C 3 168 ? -1.529  -76.315 34.318  1.00 24.53  ?  168 GLY   C N     1 
ATOM   2602 C CA    . GLY   C 3 168 ? -2.770  -75.735 34.771  1.00 25.10  ?  168 GLY   C CA    1 
ATOM   2603 C C     . GLY   C 3 168 ? -3.207  -74.551 33.905  1.00 25.79  ?  168 GLY   C C     1 
ATOM   2604 O O     . GLY   C 3 168 ? -2.878  -74.477 32.715  1.00 24.87  ?  168 GLY   C O     1 
ATOM   2605 N N     . ASN   C 3 169 ? -3.938  -73.633 34.553  1.00 27.31  ?  169 ASN   C N     1 
ATOM   2606 C CA    . ASN   C 3 169 ? -4.743  -72.619 33.906  1.00 28.64  ?  169 ASN   C CA    1 
ATOM   2607 C C     . ASN   C 3 169 ? -3.797  -71.603 33.263  1.00 29.92  ?  169 ASN   C C     1 
ATOM   2608 O O     . ASN   C 3 169 ? -2.655  -71.400 33.716  1.00 27.64  ?  169 ASN   C O     1 
ATOM   2609 C CB    . ASN   C 3 169 ? -5.738  -71.993 34.901  1.00 31.02  ?  169 ASN   C CB    1 
ATOM   2610 C CG    . ASN   C 3 169 ? -5.159  -70.918 35.816  1.00 31.51  ?  169 ASN   C CG    1 
ATOM   2611 O OD1   . ASN   C 3 169 ? -5.005  -69.772 35.400  1.00 29.29  ?  169 ASN   C OD1   1 
ATOM   2612 N ND2   . ASN   C 3 169 ? -4.878  -71.216 37.079  1.00 32.89  ?  169 ASN   C ND2   1 
ATOM   2613 N N     . LEU   C 3 170 ? -4.296  -70.981 32.195  1.00 31.26  ?  170 LEU   C N     1 
ATOM   2614 C CA    . LEU   C 3 170 ? -3.621  -69.886 31.515  1.00 29.95  ?  170 LEU   C CA    1 
ATOM   2615 C C     . LEU   C 3 170 ? -4.245  -68.527 31.888  1.00 33.08  ?  170 LEU   C C     1 
ATOM   2616 O O     . LEU   C 3 170 ? -4.282  -67.611 31.069  1.00 34.00  ?  170 LEU   C O     1 
ATOM   2617 C CB    . LEU   C 3 170 ? -3.662  -70.252 30.031  1.00 28.60  ?  170 LEU   C CB    1 
ATOM   2618 C CG    . LEU   C 3 170 ? -2.977  -71.571 29.644  1.00 27.00  ?  170 LEU   C CG    1 
ATOM   2619 C CD1   . LEU   C 3 170 ? -2.879  -71.649 28.117  1.00 26.48  ?  170 LEU   C CD1   1 
ATOM   2620 C CD2   . LEU   C 3 170 ? -1.615  -71.865 30.278  1.00 25.18  ?  170 LEU   C CD2   1 
ATOM   2621 N N     . ASN   C 3 171 ? -4.664  -68.363 33.167  1.00 35.92  ?  171 ASN   C N     1 
ATOM   2622 C CA    . ASN   C 3 171 ? -4.591  -67.114 33.933  1.00 43.82  ?  171 ASN   C CA    1 
ATOM   2623 C C     . ASN   C 3 171 ? -5.916  -66.379 33.754  1.00 54.48  ?  171 ASN   C C     1 
ATOM   2624 O O     . ASN   C 3 171 ? -5.934  -65.153 33.598  1.00 70.74  ?  171 ASN   C O     1 
ATOM   2625 C CB    . ASN   C 3 171 ? -3.262  -66.362 33.744  1.00 43.27  ?  171 ASN   C CB    1 
ATOM   2626 C CG    . ASN   C 3 171 ? -2.087  -67.105 34.365  1.00 52.84  ?  171 ASN   C CG    1 
ATOM   2627 O OD1   . ASN   C 3 171 ? -1.761  -68.283 34.060  1.00 46.00  ?  171 ASN   C OD1   1 
ATOM   2628 N ND2   . ASN   C 3 171 ? -1.454  -66.413 35.303  1.00 58.48  ?  171 ASN   C ND2   1 
ATOM   2629 N N     . GLY   C 3 172 ? -7.022  -67.144 33.908  1.00 51.48  ?  172 GLY   C N     1 
ATOM   2630 C CA    . GLY   C 3 172 ? -8.290  -66.844 33.262  1.00 51.88  ?  172 GLY   C CA    1 
ATOM   2631 C C     . GLY   C 3 172 ? -8.981  -68.101 32.777  1.00 53.45  ?  172 GLY   C C     1 
ATOM   2632 O O     . GLY   C 3 172 ? -8.303  -69.146 32.743  1.00 58.50  ?  172 GLY   C O     1 
ATOM   2633 N N     . GLY   D 1 2   ? 13.793  -74.128 4.463   1.00 45.10  ?  1   GLY   D N     1 
ATOM   2634 C CA    . GLY   D 1 2   ? 13.143  -72.897 4.976   1.00 42.33  ?  1   GLY   D CA    1 
ATOM   2635 C C     . GLY   D 1 2   ? 12.172  -72.232 3.977   1.00 41.18  ?  1   GLY   D C     1 
ATOM   2636 O O     . GLY   D 1 2   ? 12.209  -72.475 2.776   1.00 42.19  ?  1   GLY   D O     1 
ATOM   2637 N N     . SER   D 1 3   ? 11.337  -71.313 4.477   1.00 39.32  ?  2   SER   D N     1 
ATOM   2638 C CA    . SER   D 1 3   ? 10.148  -70.819 3.782   1.00 39.01  ?  2   SER   D CA    1 
ATOM   2639 C C     . SER   D 1 3   ? 10.420  -69.522 3.006   1.00 38.39  ?  2   SER   D C     1 
ATOM   2640 O O     . SER   D 1 3   ? 11.275  -68.727 3.367   1.00 38.02  ?  2   SER   D O     1 
ATOM   2641 C CB    . SER   D 1 3   ? 9.024   -70.602 4.776   1.00 37.99  ?  2   SER   D CB    1 
ATOM   2642 O OG    . SER   D 1 3   ? 8.713   -71.814 5.447   1.00 39.78  ?  2   SER   D OG    1 
ATOM   2643 N N     . GLN   D 1 4   ? 9.622   -69.269 1.963   1.00 38.26  ?  3   GLN   D N     1 
ATOM   2644 C CA    . GLN   D 1 4   ? 9.598   -68.018 1.215   1.00 37.83  ?  3   GLN   D CA    1 
ATOM   2645 C C     . GLN   D 1 4   ? 8.263   -67.340 1.446   1.00 35.65  ?  3   GLN   D C     1 
ATOM   2646 O O     . GLN   D 1 4   ? 7.261   -68.030 1.681   1.00 34.84  ?  3   GLN   D O     1 
ATOM   2647 C CB    . GLN   D 1 4   ? 9.848   -68.329 -0.251  1.00 41.18  ?  3   GLN   D CB    1 
ATOM   2648 C CG    . GLN   D 1 4   ? 11.228  -68.946 -0.492  1.00 44.49  ?  3   GLN   D CG    1 
ATOM   2649 C CD    . GLN   D 1 4   ? 11.537  -69.184 -1.953  1.00 49.35  ?  3   GLN   D CD    1 
ATOM   2650 O OE1   . GLN   D 1 4   ? 12.661  -68.941 -2.426  1.00 53.56  ?  3   GLN   D OE1   1 
ATOM   2651 N NE2   . GLN   D 1 4   ? 10.554  -69.706 -2.679  1.00 51.21  ?  3   GLN   D NE2   1 
ATOM   2652 N N     . VAL   D 1 5   ? 8.275   -65.992 1.377   1.00 33.77  ?  4   VAL   D N     1 
ATOM   2653 C CA    . VAL   D 1 5   ? 7.101   -65.163 1.589   1.00 31.97  ?  4   VAL   D CA    1 
ATOM   2654 C C     . VAL   D 1 5   ? 6.886   -64.232 0.392   1.00 32.04  ?  4   VAL   D C     1 
ATOM   2655 O O     . VAL   D 1 5   ? 7.839   -63.698 -0.164  1.00 31.12  ?  4   VAL   D O     1 
ATOM   2656 C CB    . VAL   D 1 5   ? 7.162   -64.407 2.929   1.00 30.70  ?  4   VAL   D CB    1 
ATOM   2657 C CG1   . VAL   D 1 5   ? 8.256   -63.345 3.001   1.00 30.65  ?  4   VAL   D CG1   1 
ATOM   2658 C CG2   . VAL   D 1 5   ? 5.808   -63.819 3.279   1.00 29.85  ?  4   VAL   D CG2   1 
ATOM   2659 N N     . GLU   D 1 6   ? 5.604   -64.072 -0.001  1.00 33.06  ?  5   GLU   D N     1 
ATOM   2660 C CA    . GLU   D 1 6   ? 5.121   -63.004 -0.862  1.00 34.13  ?  5   GLU   D CA    1 
ATOM   2661 C C     . GLU   D 1 6   ? 3.936   -62.318 -0.193  1.00 32.59  ?  5   GLU   D C     1 
ATOM   2662 O O     . GLU   D 1 6   ? 2.976   -63.017 0.114   1.00 32.94  ?  5   GLU   D O     1 
ATOM   2663 C CB    . GLU   D 1 6   ? 4.732   -63.593 -2.209  1.00 37.38  ?  5   GLU   D CB    1 
ATOM   2664 C CG    . GLU   D 1 6   ? 5.954   -63.907 -3.070  1.00 40.94  ?  5   GLU   D CG    1 
ATOM   2665 C CD    . GLU   D 1 6   ? 5.598   -64.375 -4.461  1.00 45.31  ?  5   GLU   D CD    1 
ATOM   2666 O OE1   . GLU   D 1 6   ? 4.628   -65.168 -4.488  1.00 50.66  ?  5   GLU   D OE1   1 
ATOM   2667 O OE2   . GLU   D 1 6   ? 6.236   -64.007 -5.484  1.00 49.57  -1 5   GLU   D OE2   1 
ATOM   2668 N N     . PHE   D 1 7   ? 3.988   -60.978 -0.008  1.00 31.02  ?  6   PHE   D N     1 
ATOM   2669 C CA    . PHE   D 1 7   ? 2.919   -60.201 0.607   1.00 29.26  ?  6   PHE   D CA    1 
ATOM   2670 C C     . PHE   D 1 7   ? 2.620   -59.008 -0.306  1.00 29.87  ?  6   PHE   D C     1 
ATOM   2671 O O     . PHE   D 1 7   ? 3.466   -58.126 -0.440  1.00 30.05  ?  6   PHE   D O     1 
ATOM   2672 C CB    . PHE   D 1 7   ? 3.289   -59.768 2.023   1.00 27.42  ?  6   PHE   D CB    1 
ATOM   2673 C CG    . PHE   D 1 7   ? 2.241   -58.947 2.763   1.00 26.27  ?  6   PHE   D CG    1 
ATOM   2674 C CD1   . PHE   D 1 7   ? 0.881   -59.266 2.725   1.00 26.41  ?  6   PHE   D CD1   1 
ATOM   2675 C CD2   . PHE   D 1 7   ? 2.616   -57.858 3.517   1.00 24.99  ?  6   PHE   D CD2   1 
ATOM   2676 C CE1   . PHE   D 1 7   ? -0.075  -58.512 3.385   1.00 26.01  ?  6   PHE   D CE1   1 
ATOM   2677 C CE2   . PHE   D 1 7   ? 1.675   -57.137 4.240   1.00 25.03  ?  6   PHE   D CE2   1 
ATOM   2678 C CZ    . PHE   D 1 7   ? 0.322   -57.423 4.138   1.00 25.62  ?  6   PHE   D CZ    1 
ATOM   2679 N N     . SER   D 1 8   ? 1.498   -59.044 -1.027  1.00 30.21  ?  7   SER   D N     1 
ATOM   2680 C CA    . SER   D 1 8   ? 0.952   -57.888 -1.728  1.00 31.01  ?  7   SER   D CA    1 
ATOM   2681 C C     . SER   D 1 8   ? -0.038  -57.205 -0.814  1.00 30.33  ?  7   SER   D C     1 
ATOM   2682 O O     . SER   D 1 8   ? -0.882  -57.899 -0.279  1.00 32.15  ?  7   SER   D O     1 
ATOM   2683 C CB    . SER   D 1 8   ? 0.260   -58.274 -2.999  1.00 32.42  ?  7   SER   D CB    1 
ATOM   2684 O OG    . SER   D 1 8   ? 1.253   -58.573 -3.950  1.00 35.30  ?  7   SER   D OG    1 
ATOM   2685 N N     . MET   D 1 9   ? 0.013   -55.876 -0.707  1.00 30.22  ?  8   MET   D N     1 
ATOM   2686 C CA    . MET   D 1 9   ? -1.005  -55.134 0.028   1.00 31.18  ?  8   MET   D CA    1 
ATOM   2687 C C     . MET   D 1 9   ? -1.188  -53.748 -0.574  1.00 30.42  ?  8   MET   D C     1 
ATOM   2688 O O     . MET   D 1 9   ? -0.292  -53.274 -1.253  1.00 29.05  ?  8   MET   D O     1 
ATOM   2689 C CB    . MET   D 1 9   ? -0.682  -55.033 1.534   1.00 32.54  ?  8   MET   D CB    1 
ATOM   2690 C CG    . MET   D 1 9   ? 0.722   -54.553 1.856   1.00 33.86  ?  8   MET   D CG    1 
ATOM   2691 S SD    . MET   D 1 9   ? 0.929   -53.675 3.431   1.00 38.93  ?  8   MET   D SD    1 
ATOM   2692 C CE    . MET   D 1 9   ? 0.051   -52.180 2.956   1.00 36.89  ?  8   MET   D CE    1 
ATOM   2693 N N     . LYS   D 1 10  ? -2.368  -53.147 -0.316  1.00 30.28  ?  9   LYS   D N     1 
ATOM   2694 C CA    . LYS   D 1 10  ? -2.690  -51.748 -0.590  1.00 31.23  ?  9   LYS   D CA    1 
ATOM   2695 C C     . LYS   D 1 10  ? -3.143  -51.097 0.714   1.00 30.01  ?  9   LYS   D C     1 
ATOM   2696 O O     . LYS   D 1 10  ? -4.057  -51.633 1.345   1.00 29.78  ?  9   LYS   D O     1 
ATOM   2697 C CB    . LYS   D 1 10  ? -3.809  -51.572 -1.626  1.00 33.96  ?  9   LYS   D CB    1 
ATOM   2698 C CG    . LYS   D 1 10  ? -4.117  -50.129 -2.109  1.00 36.69  ?  9   LYS   D CG    1 
ATOM   2699 C CD    . LYS   D 1 10  ? -5.068  -50.076 -3.325  1.00 40.96  ?  9   LYS   D CD    1 
ATOM   2700 C CE    . LYS   D 1 10  ? -5.099  -48.767 -4.113  1.00 42.04  ?  9   LYS   D CE    1 
ATOM   2701 N NZ    . LYS   D 1 10  ? -4.978  -48.945 -5.571  1.00 44.35  1  9   LYS   D NZ    1 
ATOM   2702 N N     . MET   D 1 11  ? -2.523  -49.974 1.113   1.00 28.83  ?  10  MET   D N     1 
ATOM   2703 C CA    . MET   D 1 11  ? -3.026  -49.151 2.199   1.00 28.78  ?  10  MET   D CA    1 
ATOM   2704 C C     . MET   D 1 11  ? -3.760  -47.966 1.603   1.00 29.28  ?  10  MET   D C     1 
ATOM   2705 O O     . MET   D 1 11  ? -3.163  -47.235 0.810   1.00 29.40  ?  10  MET   D O     1 
ATOM   2706 C CB    . MET   D 1 11  ? -1.908  -48.637 3.104   1.00 29.01  ?  10  MET   D CB    1 
ATOM   2707 C CG    . MET   D 1 11  ? -2.410  -47.895 4.323   1.00 28.58  ?  10  MET   D CG    1 
ATOM   2708 S SD    . MET   D 1 11  ? -1.151  -47.806 5.604   1.00 28.95  ?  10  MET   D SD    1 
ATOM   2709 C CE    . MET   D 1 11  ? 0.017   -46.703 4.804   1.00 29.57  ?  10  MET   D CE    1 
ATOM   2710 N N     . THR   D 1 12  ? -5.028  -47.794 1.996   1.00 29.90  ?  11  THR   D N     1 
ATOM   2711 C CA    . THR   D 1 12  ? -5.810  -46.593 1.719   1.00 30.87  ?  11  THR   D CA    1 
ATOM   2712 C C     . THR   D 1 12  ? -6.241  -45.942 3.043   1.00 31.24  ?  11  THR   D C     1 
ATOM   2713 O O     . THR   D 1 12  ? -6.055  -46.518 4.129   1.00 29.77  ?  11  THR   D O     1 
ATOM   2714 C CB    . THR   D 1 12  ? -7.000  -46.946 0.835   1.00 31.43  ?  11  THR   D CB    1 
ATOM   2715 O OG1   . THR   D 1 12  ? -7.814  -47.853 1.558   1.00 31.06  ?  11  THR   D OG1   1 
ATOM   2716 C CG2   . THR   D 1 12  ? -6.587  -47.563 -0.481  1.00 32.56  ?  11  THR   D CG2   1 
ATOM   2717 N N     . GLY   D 1 13  ? -6.874  -44.761 2.906   1.00 30.87  ?  12  GLY   D N     1 
ATOM   2718 C CA    . GLY   D 1 13  ? -7.459  -44.015 3.994   1.00 31.02  ?  12  GLY   D CA    1 
ATOM   2719 C C     . GLY   D 1 13  ? -6.644  -42.750 4.122   1.00 31.04  ?  12  GLY   D C     1 
ATOM   2720 O O     . GLY   D 1 13  ? -6.074  -42.321 3.120   1.00 32.86  ?  12  GLY   D O     1 
ATOM   2721 N N     . GLY   D 1 14  ? -6.559  -42.178 5.317   1.00 29.51  ?  13  GLY   D N     1 
ATOM   2722 C CA    . GLY   D 1 14  ? -5.924  -40.872 5.445   1.00 31.16  ?  13  GLY   D CA    1 
ATOM   2723 C C     . GLY   D 1 14  ? -6.262  -40.146 6.737   1.00 31.08  ?  13  GLY   D C     1 
ATOM   2724 O O     . GLY   D 1 14  ? -6.885  -40.721 7.631   1.00 28.83  ?  13  GLY   D O     1 
ATOM   2725 N N     . GLU   D 1 15  ? -5.933  -38.843 6.738   1.00 32.67  ?  14  GLU   D N     1 
ATOM   2726 C CA    . GLU   D 1 15  ? -6.114  -37.987 7.898   1.00 32.32  ?  14  GLU   D CA    1 
ATOM   2727 C C     . GLU   D 1 15  ? -7.596  -37.652 8.113   1.00 35.25  ?  14  GLU   D C     1 
ATOM   2728 O O     . GLU   D 1 15  ? -8.315  -37.541 7.138   1.00 36.85  ?  14  GLU   D O     1 
ATOM   2729 C CB    . GLU   D 1 15  ? -5.205  -36.772 7.763   1.00 32.53  ?  14  GLU   D CB    1 
ATOM   2730 C CG    . GLU   D 1 15  ? -3.728  -37.120 7.849   1.00 30.93  ?  14  GLU   D CG    1 
ATOM   2731 C CD    . GLU   D 1 15  ? -2.840  -35.911 7.678   1.00 32.02  ?  14  GLU   D CD    1 
ATOM   2732 O OE1   . GLU   D 1 15  ? -3.001  -35.176 6.681   1.00 34.70  ?  14  GLU   D OE1   1 
ATOM   2733 O OE2   . GLU   D 1 15  ? -1.959  -35.711 8.523   1.00 30.72  -1 14  GLU   D OE2   1 
ATOM   2734 N N     . ILE   D 1 16  ? -8.035  -37.598 9.387   1.00 38.15  ?  15  ILE   D N     1 
ATOM   2735 C CA    . ILE   D 1 16  ? -9.405  -37.308 9.815   1.00 40.99  ?  15  ILE   D CA    1 
ATOM   2736 C C     . ILE   D 1 16  ? -9.440  -35.799 10.025  1.00 41.17  ?  15  ILE   D C     1 
ATOM   2737 O O     . ILE   D 1 16  ? -8.491  -35.303 10.640  1.00 42.77  ?  15  ILE   D O     1 
ATOM   2738 C CB    . ILE   D 1 16  ? -9.747  -38.020 11.147  1.00 42.96  ?  15  ILE   D CB    1 
ATOM   2739 C CG1   . ILE   D 1 16  ? -9.722  -39.549 11.047  1.00 42.94  ?  15  ILE   D CG1   1 
ATOM   2740 C CG2   . ILE   D 1 16  ? -11.064 -37.526 11.767  1.00 45.69  ?  15  ILE   D CG2   1 
ATOM   2741 C CD1   . ILE   D 1 16  ? -9.565  -40.232 12.403  1.00 42.08  ?  15  ILE   D CD1   1 
ATOM   2742 N N     . PRO   D 1 17  ? -10.502 -35.033 9.640   1.00 42.81  ?  16  PRO   D N     1 
ATOM   2743 C CA    . PRO   D 1 17  ? -10.576 -33.607 9.996   1.00 43.76  ?  16  PRO   D CA    1 
ATOM   2744 C C     . PRO   D 1 17  ? -10.678 -33.347 11.503  1.00 42.25  ?  16  PRO   D C     1 
ATOM   2745 O O     . PRO   D 1 17  ? -11.018 -34.249 12.267  1.00 41.04  ?  16  PRO   D O     1 
ATOM   2746 C CB    . PRO   D 1 17  ? -11.776 -33.053 9.211   1.00 45.16  ?  16  PRO   D CB    1 
ATOM   2747 C CG    . PRO   D 1 17  ? -12.090 -34.128 8.194   1.00 45.59  ?  16  PRO   D CG    1 
ATOM   2748 C CD    . PRO   D 1 17  ? -11.639 -35.441 8.786   1.00 42.90  ?  16  PRO   D CD    1 
ATOM   2749 N N     . GLY   D 1 18  ? -10.309 -32.121 11.907  1.00 43.78  ?  17  GLY   D N     1 
ATOM   2750 C CA    . GLY   D 1 18  ? -10.534 -31.595 13.247  1.00 43.95  ?  17  GLY   D CA    1 
ATOM   2751 C C     . GLY   D 1 18  ? -9.323  -31.800 14.150  1.00 41.71  ?  17  GLY   D C     1 
ATOM   2752 O O     . GLY   D 1 18  ? -8.372  -32.480 13.770  1.00 41.65  ?  17  GLY   D O     1 
ATOM   2753 N N     . GLY   D 1 19  ? -9.369  -31.157 15.326  1.00 39.84  ?  18  GLY   D N     1 
ATOM   2754 C CA    . GLY   D 1 19  ? -8.392  -31.360 16.373  1.00 37.68  ?  18  GLY   D CA    1 
ATOM   2755 C C     . GLY   D 1 19  ? -7.029  -30.814 15.957  1.00 36.85  ?  18  GLY   D C     1 
ATOM   2756 O O     . GLY   D 1 19  ? -6.928  -29.972 15.048  1.00 38.59  ?  18  GLY   D O     1 
ATOM   2757 N N     . ASN   D 1 20  ? -5.997  -31.332 16.614  1.00 33.45  ?  19  ASN   D N     1 
ATOM   2758 C CA    . ASN   D 1 20  ? -4.638  -30.850 16.434  1.00 32.96  ?  19  ASN   D CA    1 
ATOM   2759 C C     . ASN   D 1 20  ? -4.098  -31.448 15.137  1.00 32.84  ?  19  ASN   D C     1 
ATOM   2760 O O     . ASN   D 1 20  ? -3.633  -32.578 15.156  1.00 34.32  ?  19  ASN   D O     1 
ATOM   2761 C CB    . ASN   D 1 20  ? -3.793  -31.153 17.663  1.00 30.51  ?  19  ASN   D CB    1 
ATOM   2762 C CG    . ASN   D 1 20  ? -2.331  -30.836 17.494  1.00 30.79  ?  19  ASN   D CG    1 
ATOM   2763 O OD1   . ASN   D 1 20  ? -1.909  -30.190 16.521  1.00 32.77  ?  19  ASN   D OD1   1 
ATOM   2764 N ND2   . ASN   D 1 20  ? -1.525  -31.242 18.464  1.00 30.31  ?  19  ASN   D ND2   1 
ATOM   2765 N N     . ILE   D 1 21  ? -4.103  -30.681 14.051  1.00 33.65  ?  20  ILE   D N     1 
ATOM   2766 C CA    . ILE   D 1 21  ? -3.708  -31.188 12.738  1.00 32.98  ?  20  ILE   D CA    1 
ATOM   2767 C C     . ILE   D 1 21  ? -2.193  -31.385 12.640  1.00 31.68  ?  20  ILE   D C     1 
ATOM   2768 O O     . ILE   D 1 21  ? -1.743  -32.084 11.718  1.00 31.03  ?  20  ILE   D O     1 
ATOM   2769 C CB    . ILE   D 1 21  ? -4.233  -30.310 11.592  1.00 34.55  ?  20  ILE   D CB    1 
ATOM   2770 C CG1   . ILE   D 1 21  ? -3.690  -28.862 11.632  1.00 36.10  ?  20  ILE   D CG1   1 
ATOM   2771 C CG2   . ILE   D 1 21  ? -5.759  -30.354 11.551  1.00 35.34  ?  20  ILE   D CG2   1 
ATOM   2772 C CD1   . ILE   D 1 21  ? -3.784  -28.160 10.298  1.00 38.47  ?  20  ILE   D CD1   1 
ATOM   2773 N N     . VAL   D 1 22  ? -1.415  -30.750 13.540  1.00 31.26  ?  21  VAL   D N     1 
ATOM   2774 C CA    . VAL   D 1 22  ? 0.003   -31.038 13.636  1.00 31.06  ?  21  VAL   D CA    1 
ATOM   2775 C C     . VAL   D 1 22  ? 0.168   -32.531 13.945  1.00 29.14  ?  21  VAL   D C     1 
ATOM   2776 O O     . VAL   D 1 22  ? 1.018   -33.146 13.312  1.00 28.66  ?  21  VAL   D O     1 
ATOM   2777 C CB    . VAL   D 1 22  ? 0.778   -30.092 14.585  1.00 31.99  ?  21  VAL   D CB    1 
ATOM   2778 C CG1   . VAL   D 1 22  ? 2.254   -30.463 14.681  1.00 31.53  ?  21  VAL   D CG1   1 
ATOM   2779 C CG2   . VAL   D 1 22  ? 0.635   -28.626 14.142  1.00 34.30  ?  21  VAL   D CG2   1 
ATOM   2780 N N     . LEU   D 1 23  ? -0.677  -33.099 14.845  1.00 28.51  ?  22  LEU   D N     1 
ATOM   2781 C CA    . LEU   D 1 23  ? -0.728  -34.524 15.138  1.00 27.05  ?  22  LEU   D CA    1 
ATOM   2782 C C     . LEU   D 1 23  ? -2.049  -35.108 14.680  1.00 26.92  ?  22  LEU   D C     1 
ATOM   2783 O O     . LEU   D 1 23  ? -2.698  -35.830 15.437  1.00 26.03  ?  22  LEU   D O     1 
ATOM   2784 C CB    . LEU   D 1 23  ? -0.526  -34.751 16.632  1.00 26.40  ?  22  LEU   D CB    1 
ATOM   2785 C CG    . LEU   D 1 23  ? 0.698   -34.093 17.253  1.00 27.59  ?  22  LEU   D CG    1 
ATOM   2786 C CD1   . LEU   D 1 23  ? 0.773   -34.412 18.748  1.00 26.75  ?  22  LEU   D CD1   1 
ATOM   2787 C CD2   . LEU   D 1 23  ? 1.954   -34.512 16.501  1.00 27.80  ?  22  LEU   D CD2   1 
ATOM   2788 N N     . GLN   D 1 24  ? -2.383  -34.880 13.408  1.00 27.60  ?  23  GLN   D N     1 
ATOM   2789 C CA    . GLN   D 1 24  ? -3.726  -35.132 12.909  1.00 28.04  ?  23  GLN   D CA    1 
ATOM   2790 C C     . GLN   D 1 24  ? -4.103  -36.604 13.032  1.00 27.27  ?  23  GLN   D C     1 
ATOM   2791 O O     . GLN   D 1 24  ? -3.261  -37.508 12.869  1.00 26.78  ?  23  GLN   D O     1 
ATOM   2792 C CB    . GLN   D 1 24  ? -3.869  -34.703 11.458  1.00 29.42  ?  23  GLN   D CB    1 
ATOM   2793 C CG    . GLN   D 1 24  ? -5.322  -34.558 10.999  1.00 31.33  ?  23  GLN   D CG    1 
ATOM   2794 C CD    . GLN   D 1 24  ? -5.517  -33.635 9.815   1.00 33.46  ?  23  GLN   D CD    1 
ATOM   2795 O OE1   . GLN   D 1 24  ? -4.591  -32.933 9.367   1.00 34.68  ?  23  GLN   D OE1   1 
ATOM   2796 N NE2   . GLN   D 1 24  ? -6.751  -33.622 9.322   1.00 34.07  ?  23  GLN   D NE2   1 
ATOM   2797 N N     . GLY   D 1 25  ? -5.369  -36.840 13.383  1.00 28.33  ?  24  GLY   D N     1 
ATOM   2798 C CA    . GLY   D 1 25  ? -5.931  -38.172 13.405  1.00 27.48  ?  24  GLY   D CA    1 
ATOM   2799 C C     . GLY   D 1 25  ? -5.853  -38.848 12.030  1.00 28.61  ?  24  GLY   D C     1 
ATOM   2800 O O     . GLY   D 1 25  ? -5.871  -38.147 11.009  1.00 30.32  ?  24  GLY   D O     1 
ATOM   2801 N N     . VAL   D 1 26  ? -5.766  -40.191 12.011  1.00 27.97  ?  25  VAL   D N     1 
ATOM   2802 C CA    . VAL   D 1 26  ? -5.702  -40.992 10.791  1.00 28.26  ?  25  VAL   D CA    1 
ATOM   2803 C C     . VAL   D 1 26  ? -6.730  -42.118 10.907  1.00 28.20  ?  25  VAL   D C     1 
ATOM   2804 O O     . VAL   D 1 26  ? -7.000  -42.604 12.005  1.00 27.43  ?  25  VAL   D O     1 
ATOM   2805 C CB    . VAL   D 1 26  ? -4.288  -41.557 10.535  1.00 27.48  ?  25  VAL   D CB    1 
ATOM   2806 C CG1   . VAL   D 1 26  ? -3.258  -40.448 10.383  1.00 28.25  ?  25  VAL   D CG1   1 
ATOM   2807 C CG2   . VAL   D 1 26  ? -3.812  -42.522 11.622  1.00 26.81  ?  25  VAL   D CG2   1 
ATOM   2808 N N     . LYS   D 1 27  ? -7.299  -42.516 9.767   1.00 28.66  ?  26  LYS   D N     1 
ATOM   2809 C CA    . LYS   D 1 27  ? -8.024  -43.766 9.605   1.00 29.05  ?  26  LYS   D CA    1 
ATOM   2810 C C     . LYS   D 1 27  ? -7.496  -44.440 8.342   1.00 29.49  ?  26  LYS   D C     1 
ATOM   2811 O O     . LYS   D 1 27  ? -7.650  -43.861 7.256   1.00 29.57  ?  26  LYS   D O     1 
ATOM   2812 C CB    . LYS   D 1 27  ? -9.548  -43.631 9.512   1.00 31.23  ?  26  LYS   D CB    1 
ATOM   2813 C CG    . LYS   D 1 27  ? -10.350 -44.949 9.383   1.00 32.70  ?  26  LYS   D CG    1 
ATOM   2814 C CD    . LYS   D 1 27  ? -11.738 -44.884 10.036  0.50 34.82  ?  26  LYS   D CD    1 
ATOM   2815 C CE    . LYS   D 1 27  ? -12.481 -46.201 10.098  0.50 35.45  ?  26  LYS   D CE    1 
ATOM   2816 N NZ    . LYS   D 1 27  ? -13.328 -46.304 11.300  0.50 36.06  1  26  LYS   D NZ    1 
ATOM   2817 N N     . LEU   D 1 28  ? -6.966  -45.684 8.499   1.00 28.41  ?  27  LEU   D N     1 
ATOM   2818 C CA    . LEU   D 1 28  ? -6.237  -46.418 7.474   1.00 27.07  ?  27  LEU   D CA    1 
ATOM   2819 C C     . LEU   D 1 28  ? -6.883  -47.802 7.301   1.00 27.00  ?  27  LEU   D C     1 
ATOM   2820 O O     . LEU   D 1 28  ? -7.354  -48.402 8.277   1.00 24.93  ?  27  LEU   D O     1 
ATOM   2821 C CB    . LEU   D 1 28  ? -4.761  -46.495 7.862   1.00 25.14  ?  27  LEU   D CB    1 
ATOM   2822 C CG    . LEU   D 1 28  ? -4.015  -45.154 7.948   1.00 25.25  ?  27  LEU   D CG    1 
ATOM   2823 C CD1   . LEU   D 1 28  ? -2.704  -45.248 8.715   1.00 24.68  ?  27  LEU   D CD1   1 
ATOM   2824 C CD2   . LEU   D 1 28  ? -3.756  -44.614 6.588   1.00 25.98  ?  27  LEU   D CD2   1 
ATOM   2825 N N     . ARG   D 1 29  ? -6.954  -48.273 6.042   1.00 28.85  ?  28  ARG   D N     1 
ATOM   2826 C CA    . ARG   D 1 29  ? -7.313  -49.652 5.743   1.00 30.04  ?  28  ARG   D CA    1 
ATOM   2827 C C     . ARG   D 1 29  ? -6.179  -50.294 4.952   1.00 28.16  ?  28  ARG   D C     1 
ATOM   2828 O O     . ARG   D 1 29  ? -5.754  -49.717 3.955   1.00 28.29  ?  28  ARG   D O     1 
ATOM   2829 C CB    . ARG   D 1 29  ? -8.641  -49.790 4.992   1.00 33.08  ?  28  ARG   D CB    1 
ATOM   2830 C CG    . ARG   D 1 29  ? -9.102  -51.242 5.016   1.00 36.02  ?  28  ARG   D CG    1 
ATOM   2831 C CD    . ARG   D 1 29  ? -10.444 -51.582 4.442   1.00 40.85  ?  28  ARG   D CD    1 
ATOM   2832 N NE    . ARG   D 1 29  ? -11.455 -50.525 4.568   1.00 45.35  ?  28  ARG   D NE    1 
ATOM   2833 C CZ    . ARG   D 1 29  ? -12.507 -50.468 5.384   1.00 48.17  ?  28  ARG   D CZ    1 
ATOM   2834 N NH1   . ARG   D 1 29  ? -12.555 -51.091 6.552   1.00 48.67  1  28  ARG   D NH1   1 
ATOM   2835 N NH2   . ARG   D 1 29  ? -13.512 -49.688 5.044   1.00 51.20  ?  28  ARG   D NH2   1 
ATOM   2836 N N     . ILE   D 1 30  ? -5.717  -51.470 5.398   1.00 27.53  ?  29  ILE   D N     1 
ATOM   2837 C CA    . ILE   D 1 30  ? -4.771  -52.306 4.662   1.00 27.13  ?  29  ILE   D CA    1 
ATOM   2838 C C     . ILE   D 1 30  ? -5.546  -53.528 4.212   1.00 26.51  ?  29  ILE   D C     1 
ATOM   2839 O O     . ILE   D 1 30  ? -6.133  -54.206 5.050   1.00 25.68  ?  29  ILE   D O     1 
ATOM   2840 C CB    . ILE   D 1 30  ? -3.547  -52.691 5.502   1.00 27.06  ?  29  ILE   D CB    1 
ATOM   2841 C CG1   . ILE   D 1 30  ? -2.671  -51.456 5.784   1.00 27.10  ?  29  ILE   D CG1   1 
ATOM   2842 C CG2   . ILE   D 1 30  ? -2.734  -53.844 4.887   1.00 27.65  ?  29  ILE   D CG2   1 
ATOM   2843 C CD1   . ILE   D 1 30  ? -1.986  -51.473 7.142   1.00 26.86  ?  29  ILE   D CD1   1 
ATOM   2844 N N     . VAL   D 1 31  ? -5.474  -53.826 2.914   1.00 26.60  ?  30  VAL   D N     1 
ATOM   2845 C CA    . VAL   D 1 31  ? -5.993  -55.063 2.367   1.00 28.17  ?  30  VAL   D CA    1 
ATOM   2846 C C     . VAL   D 1 31  ? -4.849  -55.712 1.602   1.00 28.64  ?  30  VAL   D C     1 
ATOM   2847 O O     . VAL   D 1 31  ? -4.134  -55.010 0.871   1.00 29.21  ?  30  VAL   D O     1 
ATOM   2848 C CB    . VAL   D 1 31  ? -7.256  -54.919 1.502   1.00 30.14  ?  30  VAL   D CB    1 
ATOM   2849 C CG1   . VAL   D 1 31  ? -7.076  -54.018 0.298   1.00 31.16  ?  30  VAL   D CG1   1 
ATOM   2850 C CG2   . VAL   D 1 31  ? -7.789  -56.280 1.033   1.00 32.66  ?  30  VAL   D CG2   1 
ATOM   2851 N N     . GLY   D 1 32  ? -4.732  -57.047 1.746   1.00 27.61  ?  31  GLY   D N     1 
ATOM   2852 C CA    . GLY   D 1 32  ? -3.675  -57.773 1.064   1.00 27.75  ?  31  GLY   D CA    1 
ATOM   2853 C C     . GLY   D 1 32  ? -3.755  -59.287 1.241   1.00 27.12  ?  31  GLY   D C     1 
ATOM   2854 O O     . GLY   D 1 32  ? -4.676  -59.803 1.859   1.00 27.22  ?  31  GLY   D O     1 
ATOM   2855 N N     . GLU   D 1 33  ? -2.727  -59.957 0.721   1.00 27.10  ?  32  GLU   D N     1 
ATOM   2856 C CA    . GLU   D 1 33  ? -2.610  -61.395 0.728   1.00 27.66  ?  32  GLU   D CA    1 
ATOM   2857 C C     . GLU   D 1 33  ? -1.180  -61.764 1.091   1.00 27.05  ?  32  GLU   D C     1 
ATOM   2858 O O     . GLU   D 1 33  ? -0.251  -61.283 0.451   1.00 26.63  ?  32  GLU   D O     1 
ATOM   2859 C CB    . GLU   D 1 33  ? -2.972  -61.997 -0.622  1.00 29.32  ?  32  GLU   D CB    1 
ATOM   2860 C CG    . GLU   D 1 33  ? -3.190  -63.508 -0.511  1.00 30.76  ?  32  GLU   D CG    1 
ATOM   2861 C CD    . GLU   D 1 33  ? -3.120  -64.204 -1.843  1.00 32.77  ?  32  GLU   D CD    1 
ATOM   2862 O OE1   . GLU   D 1 33  ? -2.206  -63.913 -2.627  1.00 35.62  ?  32  GLU   D OE1   1 
ATOM   2863 O OE2   . GLU   D 1 33  ? -3.959  -65.061 -2.084  1.00 33.81  -1 32  GLU   D OE2   1 
ATOM   2864 N N     . TRP   D 1 34  ? -1.053  -62.691 2.048   1.00 27.19  ?  33  TRP   D N     1 
ATOM   2865 C CA    . TRP   D 1 34  ? 0.205   -63.152 2.600   1.00 27.95  ?  33  TRP   D CA    1 
ATOM   2866 C C     . TRP   D 1 34  ? 0.351   -64.597 2.159   1.00 28.85  ?  33  TRP   D C     1 
ATOM   2867 O O     . TRP   D 1 34  ? -0.498  -65.385 2.527   1.00 31.28  ?  33  TRP   D O     1 
ATOM   2868 C CB    . TRP   D 1 34  ? 0.140   -63.003 4.127   1.00 27.70  ?  33  TRP   D CB    1 
ATOM   2869 C CG    . TRP   D 1 34  ? 1.359   -63.451 4.899   1.00 28.40  ?  33  TRP   D CG    1 
ATOM   2870 C CD1   . TRP   D 1 34  ? 1.729   -64.710 5.261   1.00 29.99  ?  33  TRP   D CD1   1 
ATOM   2871 C CD2   . TRP   D 1 34  ? 2.357   -62.563 5.453   1.00 28.96  ?  33  TRP   D CD2   1 
ATOM   2872 N NE1   . TRP   D 1 34  ? 2.893   -64.676 5.997   1.00 30.35  ?  33  TRP   D NE1   1 
ATOM   2873 C CE2   . TRP   D 1 34  ? 3.316   -63.379 6.113   1.00 29.54  ?  33  TRP   D CE2   1 
ATOM   2874 C CE3   . TRP   D 1 34  ? 2.540   -61.166 5.434   1.00 28.10  ?  33  TRP   D CE3   1 
ATOM   2875 C CZ2   . TRP   D 1 34  ? 4.423   -62.826 6.764   1.00 29.43  ?  33  TRP   D CZ2   1 
ATOM   2876 C CZ3   . TRP   D 1 34  ? 3.629   -60.623 6.095   1.00 28.45  ?  33  TRP   D CZ3   1 
ATOM   2877 C CH2   . TRP   D 1 34  ? 4.561   -61.450 6.746   1.00 28.39  ?  33  TRP   D CH2   1 
ATOM   2878 N N     . VAL   D 1 35  ? 1.385   -64.941 1.387   1.00 29.26  ?  34  VAL   D N     1 
ATOM   2879 C CA    . VAL   D 1 35  ? 1.573   -66.276 0.830   1.00 31.21  ?  34  VAL   D CA    1 
ATOM   2880 C C     . VAL   D 1 35  ? 2.866   -66.839 1.420   1.00 32.58  ?  34  VAL   D C     1 
ATOM   2881 O O     . VAL   D 1 35  ? 3.890   -66.195 1.254   1.00 33.15  ?  34  VAL   D O     1 
ATOM   2882 C CB    . VAL   D 1 35  ? 1.626   -66.259 -0.725  1.00 31.42  ?  34  VAL   D CB    1 
ATOM   2883 C CG1   . VAL   D 1 35  ? 1.621   -67.668 -1.294  1.00 32.65  ?  34  VAL   D CG1   1 
ATOM   2884 C CG2   . VAL   D 1 35  ? 0.505   -65.402 -1.340  1.00 31.23  ?  34  VAL   D CG2   1 
ATOM   2885 N N     . LEU   D 1 36  ? 2.836   -67.996 2.108   1.00 34.44  ?  35  LEU   D N     1 
ATOM   2886 C CA    . LEU   D 1 36  ? 4.036   -68.746 2.471   1.00 35.90  ?  35  LEU   D CA    1 
ATOM   2887 C C     . LEU   D 1 36  ? 4.167   -69.931 1.519   1.00 37.84  ?  35  LEU   D C     1 
ATOM   2888 O O     . LEU   D 1 36  ? 3.188   -70.635 1.281   1.00 39.29  ?  35  LEU   D O     1 
ATOM   2889 C CB    . LEU   D 1 36  ? 4.053   -69.242 3.910   1.00 36.43  ?  35  LEU   D CB    1 
ATOM   2890 C CG    . LEU   D 1 36  ? 4.217   -68.185 4.996   1.00 35.72  ?  35  LEU   D CG    1 
ATOM   2891 C CD1   . LEU   D 1 36  ? 4.130   -68.889 6.334   1.00 35.87  ?  35  LEU   D CD1   1 
ATOM   2892 C CD2   . LEU   D 1 36  ? 5.520   -67.399 4.893   1.00 36.01  ?  35  LEU   D CD2   1 
ATOM   2893 N N     . LYS   D 1 37  ? 5.380   -70.152 1.006   1.00 39.22  ?  36  LYS   D N     1 
ATOM   2894 C CA    . LYS   D 1 37  ? 5.709   -71.278 0.146   1.00 42.82  ?  36  LYS   D CA    1 
ATOM   2895 C C     . LYS   D 1 37  ? 6.809   -72.074 0.837   1.00 43.28  ?  36  LYS   D C     1 
ATOM   2896 O O     . LYS   D 1 37  ? 7.728   -71.478 1.395   1.00 40.12  ?  36  LYS   D O     1 
ATOM   2897 C CB    . LYS   D 1 37  ? 6.194   -70.822 -1.237  1.00 44.59  ?  36  LYS   D CB    1 
ATOM   2898 C CG    . LYS   D 1 37  ? 5.159   -70.062 -2.052  1.00 45.80  ?  36  LYS   D CG    1 
ATOM   2899 C CD    . LYS   D 1 37  ? 5.445   -69.947 -3.547  1.00 47.82  ?  36  LYS   D CD    1 
ATOM   2900 C CE    . LYS   D 1 37  ? 4.350   -69.179 -4.253  1.00 48.32  ?  36  LYS   D CE    1 
ATOM   2901 N NZ    . LYS   D 1 37  ? 4.388   -69.299 -5.710  1.00 49.61  1  36  LYS   D NZ    1 
ATOM   2902 N N     . GLY   D 1 38  ? 6.703   -73.413 0.771   1.00 45.70  ?  37  GLY   D N     1 
ATOM   2903 C CA    . GLY   D 1 38  ? 7.806   -74.288 1.108   1.00 48.94  ?  37  GLY   D CA    1 
ATOM   2904 C C     . GLY   D 1 38  ? 8.962   -74.127 0.129   1.00 53.50  ?  37  GLY   D C     1 
ATOM   2905 O O     . GLY   D 1 38  ? 8.777   -73.595 -0.962  1.00 53.59  ?  37  GLY   D O     1 
ATOM   2906 N N     . SER   D 1 39  ? 10.146  -74.590 0.544   1.00 60.68  ?  38  SER   D N     1 
ATOM   2907 C CA    . SER   D 1 39  ? 11.312  -74.664 -0.323  1.00 69.05  ?  38  SER   D CA    1 
ATOM   2908 C C     . SER   D 1 39  ? 11.117  -75.806 -1.313  1.00 76.15  ?  38  SER   D C     1 
ATOM   2909 O O     . SER   D 1 39  ? 10.995  -75.557 -2.513  1.00 74.07  ?  38  SER   D O     1 
ATOM   2910 C CB    . SER   D 1 39  ? 12.607  -74.824 0.445   1.00 71.85  ?  38  SER   D CB    1 
ATOM   2911 O OG    . SER   D 1 39  ? 12.473  -75.595 1.630   1.00 73.22  ?  38  SER   D OG    1 
ATOM   2912 N N     . SER   D 1 40  ? 11.076  -77.042 -0.772  1.00 84.41  ?  39  SER   D N     1 
ATOM   2913 C CA    . SER   D 1 40  ? 11.065  -78.259 -1.570  1.00 91.09  ?  39  SER   D CA    1 
ATOM   2914 C C     . SER   D 1 40  ? 9.709   -78.351 -2.287  1.00 90.55  ?  39  SER   D C     1 
ATOM   2915 O O     . SER   D 1 40  ? 8.682   -78.658 -1.674  1.00 88.82  ?  39  SER   D O     1 
ATOM   2916 C CB    . SER   D 1 40  ? 11.449  -79.523 -0.776  1.00 93.09  ?  39  SER   D CB    1 
ATOM   2917 O OG    . SER   D 1 40  ? 10.752  -79.669 0.455   1.00 90.64  ?  39  SER   D OG    1 
ATOM   2918 N N     . GLY   D 1 41  ? 9.725   -77.929 -3.568  1.00 92.04  ?  40  GLY   D N     1 
ATOM   2919 C CA    . GLY   D 1 41  ? 8.540   -77.780 -4.393  1.00 86.45  ?  40  GLY   D CA    1 
ATOM   2920 C C     . GLY   D 1 41  ? 7.692   -76.615 -3.888  1.00 80.53  ?  40  GLY   D C     1 
ATOM   2921 O O     . GLY   D 1 41  ? 8.234   -75.553 -3.576  1.00 76.11  ?  40  GLY   D O     1 
ATOM   2922 N N     . GLU   D 1 42  ? 6.380   -76.858 -3.795  1.00 78.64  ?  41  GLU   D N     1 
ATOM   2923 C CA    . GLU   D 1 42  ? 5.396   -75.898 -3.341  1.00 75.76  ?  41  GLU   D CA    1 
ATOM   2924 C C     . GLU   D 1 42  ? 4.280   -76.686 -2.655  1.00 69.91  ?  41  GLU   D C     1 
ATOM   2925 O O     . GLU   D 1 42  ? 3.503   -77.356 -3.329  1.00 66.93  ?  41  GLU   D O     1 
ATOM   2926 C CB    . GLU   D 1 42  ? 4.922   -75.108 -4.570  1.00 80.46  ?  41  GLU   D CB    1 
ATOM   2927 C CG    . GLU   D 1 42  ? 5.843   -73.984 -5.053  1.00 87.10  ?  41  GLU   D CG    1 
ATOM   2928 C CD    . GLU   D 1 42  ? 5.340   -73.209 -6.273  1.00 91.86  ?  41  GLU   D CD    1 
ATOM   2929 O OE1   . GLU   D 1 42  ? 4.480   -72.314 -6.084  1.00 90.64  ?  41  GLU   D OE1   1 
ATOM   2930 O OE2   . GLU   D 1 42  ? 5.794   -73.502 -7.417  1.00 88.89  ?  41  GLU   D OE2   1 
ATOM   2931 N N     . SER   D 1 43  ? 4.272   -76.689 -1.311  1.00 62.86  ?  42  SER   D N     1 
ATOM   2932 C CA    . SER   D 1 43  ? 3.027   -76.522 -0.573  1.00 58.31  ?  42  SER   D CA    1 
ATOM   2933 C C     . SER   D 1 43  ? 2.918   -75.028 -0.255  1.00 53.66  ?  42  SER   D C     1 
ATOM   2934 O O     . SER   D 1 43  ? 3.912   -74.400 0.123   1.00 52.08  ?  42  SER   D O     1 
ATOM   2935 C CB    . SER   D 1 43  ? 2.905   -77.392 0.631   1.00 59.20  ?  42  SER   D CB    1 
ATOM   2936 O OG    . SER   D 1 43  ? 4.007   -77.225 1.497   1.00 62.82  ?  42  SER   D OG    1 
ATOM   2937 N N     . VAL   D 1 44  ? 1.715   -74.465 -0.473  1.00 49.44  ?  43  VAL   D N     1 
ATOM   2938 C CA    . VAL   D 1 44  ? 1.474   -73.035 -0.544  1.00 46.22  ?  43  VAL   D CA    1 
ATOM   2939 C C     . VAL   D 1 44  ? 0.334   -72.722 0.426   1.00 44.26  ?  43  VAL   D C     1 
ATOM   2940 O O     . VAL   D 1 44  ? -0.649  -73.449 0.453   1.00 43.91  ?  43  VAL   D O     1 
ATOM   2941 C CB    . VAL   D 1 44  ? 1.235   -72.554 -1.991  1.00 45.26  ?  43  VAL   D CB    1 
ATOM   2942 C CG1   . VAL   D 1 44  ? 0.977   -71.050 -2.080  1.00 44.26  ?  43  VAL   D CG1   1 
ATOM   2943 C CG2   . VAL   D 1 44  ? 2.437   -72.900 -2.857  1.00 46.53  ?  43  VAL   D CG2   1 
ATOM   2944 N N     . ARG   D 1 45  ? 0.516   -71.671 1.245   1.00 41.79  ?  44  ARG   D N     1 
ATOM   2945 C CA    . ARG   D 1 45  ? -0.456  -71.231 2.222   1.00 41.77  ?  44  ARG   D CA    1 
ATOM   2946 C C     . ARG   D 1 45  ? -0.762  -69.769 1.917   1.00 37.23  ?  44  ARG   D C     1 
ATOM   2947 O O     . ARG   D 1 45  ? 0.158   -68.980 1.951   1.00 35.95  ?  44  ARG   D O     1 
ATOM   2948 C CB    . ARG   D 1 45  ? 0.121   -71.408 3.630   1.00 45.09  ?  44  ARG   D CB    1 
ATOM   2949 C CG    . ARG   D 1 45  ? -0.979  -71.173 4.659   1.00 51.01  ?  44  ARG   D CG    1 
ATOM   2950 C CD    . ARG   D 1 45  ? -0.550  -71.413 6.097   1.00 56.57  ?  44  ARG   D CD    1 
ATOM   2951 N NE    . ARG   D 1 45  ? -0.319  -70.167 6.842   1.00 61.02  ?  44  ARG   D NE    1 
ATOM   2952 C CZ    . ARG   D 1 45  ? -0.194  -70.115 8.156   1.00 69.96  ?  44  ARG   D CZ    1 
ATOM   2953 N NH1   . ARG   D 1 45  ? 0.304   -71.153 8.815   1.00 75.86  ?  44  ARG   D NH1   1 
ATOM   2954 N NH2   . ARG   D 1 45  ? -0.471  -68.985 8.794   1.00 71.58  ?  44  ARG   D NH2   1 
ATOM   2955 N N     . ARG   D 1 46  ? -2.035  -69.426 1.717   1.00 34.70  ?  45  ARG   D N     1 
ATOM   2956 C CA    . ARG   D 1 46  ? -2.489  -68.095 1.352   1.00 33.36  ?  45  ARG   D CA    1 
ATOM   2957 C C     . ARG   D 1 46  ? -3.372  -67.594 2.486   1.00 31.84  ?  45  ARG   D C     1 
ATOM   2958 O O     . ARG   D 1 46  ? -4.263  -68.321 2.880   1.00 32.07  ?  45  ARG   D O     1 
ATOM   2959 C CB    . ARG   D 1 46  ? -3.228  -68.097 0.008   1.00 33.87  ?  45  ARG   D CB    1 
ATOM   2960 C CG    . ARG   D 1 46  ? -2.596  -68.974 -1.070  1.00 34.82  ?  45  ARG   D CG    1 
ATOM   2961 C CD    . ARG   D 1 46  ? -3.341  -68.791 -2.377  1.00 35.37  ?  45  ARG   D CD    1 
ATOM   2962 N NE    . ARG   D 1 46  ? -2.879  -67.541 -2.968  1.00 34.20  ?  45  ARG   D NE    1 
ATOM   2963 C CZ    . ARG   D 1 46  ? -1.933  -67.347 -3.887  1.00 34.17  ?  45  ARG   D CZ    1 
ATOM   2964 N NH1   . ARG   D 1 46  ? -1.647  -66.104 -4.239  1.00 33.15  ?  45  ARG   D NH1   1 
ATOM   2965 N NH2   . ARG   D 1 46  ? -1.306  -68.364 -4.469  1.00 35.16  ?  45  ARG   D NH2   1 
ATOM   2966 N N     . THR   D 1 47  ? -3.128  -66.364 2.973   1.00 30.26  ?  46  THR   D N     1 
ATOM   2967 C CA    . THR   D 1 47  ? -3.903  -65.744 4.035   1.00 29.38  ?  46  THR   D CA    1 
ATOM   2968 C C     . THR   D 1 47  ? -4.335  -64.359 3.551   1.00 28.68  ?  46  THR   D C     1 
ATOM   2969 O O     . THR   D 1 47  ? -3.478  -63.525 3.284   1.00 28.07  ?  46  THR   D O     1 
ATOM   2970 C CB    . THR   D 1 47  ? -3.037  -65.692 5.301   1.00 28.67  ?  46  THR   D CB    1 
ATOM   2971 O OG1   . THR   D 1 47  ? -2.620  -66.995 5.639   1.00 28.71  ?  46  THR   D OG1   1 
ATOM   2972 C CG2   . THR   D 1 47  ? -3.775  -65.162 6.514   1.00 28.39  ?  46  THR   D CG2   1 
ATOM   2973 N N     . ASP   D 1 48  ? -5.651  -64.112 3.457   1.00 29.31  ?  47  ASP   D N     1 
ATOM   2974 C CA    . ASP   D 1 48  ? -6.201  -62.780 3.272   1.00 29.26  ?  47  ASP   D CA    1 
ATOM   2975 C C     . ASP   D 1 48  ? -6.024  -61.969 4.550   1.00 28.08  ?  47  ASP   D C     1 
ATOM   2976 O O     . ASP   D 1 48  ? -6.208  -62.515 5.621   1.00 27.85  ?  47  ASP   D O     1 
ATOM   2977 C CB    . ASP   D 1 48  ? -7.647  -62.794 2.812   1.00 30.75  ?  47  ASP   D CB    1 
ATOM   2978 C CG    . ASP   D 1 48  ? -7.858  -63.358 1.413   1.00 32.75  ?  47  ASP   D CG    1 
ATOM   2979 O OD1   . ASP   D 1 48  ? -7.005  -63.145 0.512   1.00 32.55  ?  47  ASP   D OD1   1 
ATOM   2980 O OD2   . ASP   D 1 48  ? -8.906  -63.969 1.209   1.00 36.65  ?  47  ASP   D OD2   1 
ATOM   2981 N N     . VAL   D 1 49  ? -5.641  -60.700 4.382   1.00 27.88  ?  48  VAL   D N     1 
ATOM   2982 C CA    . VAL   D 1 49  ? -5.305  -59.765 5.437   1.00 28.31  ?  48  VAL   D CA    1 
ATOM   2983 C C     . VAL   D 1 49  ? -6.208  -58.562 5.229   1.00 29.45  ?  48  VAL   D C     1 
ATOM   2984 O O     . VAL   D 1 49  ? -6.188  -58.001 4.129   1.00 28.67  ?  48  VAL   D O     1 
ATOM   2985 C CB    . VAL   D 1 49  ? -3.832  -59.319 5.409   1.00 28.29  ?  48  VAL   D CB    1 
ATOM   2986 C CG1   . VAL   D 1 49  ? -3.529  -58.330 6.539   1.00 28.62  ?  48  VAL   D CG1   1 
ATOM   2987 C CG2   . VAL   D 1 49  ? -2.872  -60.487 5.515   1.00 28.55  ?  48  VAL   D CG2   1 
ATOM   2988 N N     . LYS   D 1 50  ? -6.996  -58.194 6.260   1.00 29.97  ?  49  LYS   D N     1 
ATOM   2989 C CA    . LYS   D 1 50  ? -7.670  -56.909 6.343   1.00 31.33  ?  49  LYS   D CA    1 
ATOM   2990 C C     . LYS   D 1 50  ? -7.302  -56.276 7.689   1.00 30.39  ?  49  LYS   D C     1 
ATOM   2991 O O     . LYS   D 1 50  ? -7.521  -56.926 8.713   1.00 29.38  ?  49  LYS   D O     1 
ATOM   2992 C CB    . LYS   D 1 50  ? -9.175  -57.094 6.095   1.00 35.49  ?  49  LYS   D CB    1 
ATOM   2993 C CG    . LYS   D 1 50  ? -10.055 -55.804 6.235   1.00 39.45  ?  49  LYS   D CG    1 
ATOM   2994 C CD    . LYS   D 1 50  ? -11.508 -55.951 5.780   1.00 44.50  ?  49  LYS   D CD    1 
ATOM   2995 C CE    . LYS   D 1 50  ? -12.554 -55.243 6.620   1.00 45.85  ?  49  LYS   D CE    1 
ATOM   2996 N NZ    . LYS   D 1 50  ? -13.864 -55.901 6.471   1.00 46.52  1  49  LYS   D NZ    1 
ATOM   2997 N N     . VAL   D 1 51  ? -6.712  -55.050 7.671   1.00 28.36  ?  50  VAL   D N     1 
ATOM   2998 C CA    . VAL   D 1 51  ? -6.335  -54.279 8.849   1.00 26.84  ?  50  VAL   D CA    1 
ATOM   2999 C C     . VAL   D 1 51  ? -7.055  -52.930 8.806   1.00 27.79  ?  50  VAL   D C     1 
ATOM   3000 O O     . VAL   D 1 51  ? -7.084  -52.299 7.763   1.00 29.33  ?  50  VAL   D O     1 
ATOM   3001 C CB    . VAL   D 1 51  ? -4.814  -54.123 8.976   1.00 25.77  ?  50  VAL   D CB    1 
ATOM   3002 C CG1   . VAL   D 1 51  ? -4.393  -53.310 10.198  1.00 25.71  ?  50  VAL   D CG1   1 
ATOM   3003 C CG2   . VAL   D 1 51  ? -4.135  -55.470 8.996   1.00 26.60  ?  50  VAL   D CG2   1 
ATOM   3004 N N     . ASP   D 1 52  ? -7.661  -52.516 9.937   1.00 28.56  ?  51  ASP   D N     1 
ATOM   3005 C CA    . ASP   D 1 52  ? -8.320  -51.229 10.121  1.00 28.65  ?  51  ASP   D CA    1 
ATOM   3006 C C     . ASP   D 1 52  ? -7.656  -50.517 11.304  1.00 27.55  ?  51  ASP   D C     1 
ATOM   3007 O O     . ASP   D 1 52  ? -7.702  -51.032 12.423  1.00 25.37  ?  51  ASP   D O     1 
ATOM   3008 C CB    . ASP   D 1 52  ? -9.798  -51.425 10.364  1.00 31.61  ?  51  ASP   D CB    1 
ATOM   3009 C CG    . ASP   D 1 52  ? -10.485 -52.074 9.179   1.00 34.84  ?  51  ASP   D CG    1 
ATOM   3010 O OD1   . ASP   D 1 52  ? -10.572 -51.383 8.155   1.00 35.69  ?  51  ASP   D OD1   1 
ATOM   3011 O OD2   . ASP   D 1 52  ? -10.803 -53.283 9.263   1.00 39.64  ?  51  ASP   D OD2   1 
ATOM   3012 N N     . ILE   D 1 53  ? -7.044  -49.345 11.043  1.00 26.47  ?  52  ILE   D N     1 
ATOM   3013 C CA    . ILE   D 1 53  ? -6.447  -48.523 12.091  1.00 26.28  ?  52  ILE   D CA    1 
ATOM   3014 C C     . ILE   D 1 53  ? -7.189  -47.186 12.169  1.00 26.08  ?  52  ILE   D C     1 
ATOM   3015 O O     . ILE   D 1 53  ? -7.381  -46.540 11.155  1.00 26.11  ?  52  ILE   D O     1 
ATOM   3016 C CB    . ILE   D 1 53  ? -4.927  -48.376 11.888  1.00 24.34  ?  52  ILE   D CB    1 
ATOM   3017 C CG1   . ILE   D 1 53  ? -4.238  -49.752 11.886  1.00 23.74  ?  52  ILE   D CG1   1 
ATOM   3018 C CG2   . ILE   D 1 53  ? -4.317  -47.461 12.953  1.00 23.91  ?  52  ILE   D CG2   1 
ATOM   3019 C CD1   . ILE   D 1 53  ? -2.892  -49.772 11.207  1.00 22.97  ?  52  ILE   D CD1   1 
ATOM   3020 N N     . THR   D 1 54  ? -7.598  -46.813 13.389  1.00 26.02  ?  53  THR   D N     1 
ATOM   3021 C CA    . THR   D 1 54  ? -7.946  -45.448 13.737  1.00 25.89  ?  53  THR   D CA    1 
ATOM   3022 C C     . THR   D 1 54  ? -7.009  -44.996 14.843  1.00 24.76  ?  53  THR   D C     1 
ATOM   3023 O O     . THR   D 1 54  ? -6.814  -45.725 15.794  1.00 23.21  ?  53  THR   D O     1 
ATOM   3024 C CB    . THR   D 1 54  ? -9.402  -45.399 14.171  1.00 26.72  ?  53  THR   D CB    1 
ATOM   3025 O OG1   . THR   D 1 54  ? -10.132 -45.565 12.962  1.00 27.64  ?  53  THR   D OG1   1 
ATOM   3026 C CG2   . THR   D 1 54  ? -9.804  -44.066 14.776  1.00 27.91  ?  53  THR   D CG2   1 
ATOM   3027 N N     . SER   D 1 55  ? -6.497  -43.770 14.722  1.00 25.29  ?  54  SER   D N     1 
ATOM   3028 C CA    . SER   D 1 55  ? -5.754  -43.079 15.769  1.00 25.26  ?  54  SER   D CA    1 
ATOM   3029 C C     . SER   D 1 55  ? -6.133  -41.597 15.673  1.00 28.45  ?  54  SER   D C     1 
ATOM   3030 O O     . SER   D 1 55  ? -5.723  -40.936 14.700  1.00 27.95  ?  54  SER   D O     1 
ATOM   3031 C CB    . SER   D 1 55  ? -4.252  -43.287 15.603  1.00 23.88  ?  54  SER   D CB    1 
ATOM   3032 O OG    . SER   D 1 55  ? -3.541  -42.753 16.707  1.00 23.40  ?  54  SER   D OG    1 
ATOM   3033 N N     . THR   D 1 56  ? -6.890  -41.069 16.666  1.00 28.57  ?  55  THR   D N     1 
ATOM   3034 C CA    . THR   D 1 56  ? -7.346  -39.688 16.651  1.00 28.46  ?  55  THR   D CA    1 
ATOM   3035 C C     . THR   D 1 56  ? -6.157  -38.745 16.888  1.00 27.87  ?  55  THR   D C     1 
ATOM   3036 O O     . THR   D 1 56  ? -5.000  -39.164 17.020  1.00 26.36  ?  55  THR   D O     1 
ATOM   3037 C CB    . THR   D 1 56  ? -8.491  -39.490 17.650  1.00 28.46  ?  55  THR   D CB    1 
ATOM   3038 O OG1   . THR   D 1 56  ? -7.977  -39.758 18.949  1.00 26.92  ?  55  THR   D OG1   1 
ATOM   3039 C CG2   . THR   D 1 56  ? -9.679  -40.384 17.351  1.00 28.90  ?  55  THR   D CG2   1 
ATOM   3040 N N     . ALA   D 1 57  ? -6.445  -37.433 16.839  1.00 28.94  ?  56  ALA   D N     1 
ATOM   3041 C CA    . ALA   D 1 57  ? -5.411  -36.436 16.925  1.00 28.03  ?  56  ALA   D CA    1 
ATOM   3042 C C     . ALA   D 1 57  ? -4.614  -36.648 18.225  1.00 25.89  ?  56  ALA   D C     1 
ATOM   3043 O O     . ALA   D 1 57  ? -5.182  -37.037 19.255  1.00 25.91  ?  56  ALA   D O     1 
ATOM   3044 C CB    . ALA   D 1 57  ? -5.984  -35.042 16.800  1.00 28.73  ?  56  ALA   D CB    1 
ATOM   3045 N N     . GLY   D 1 58  ? -3.302  -36.500 18.112  1.00 24.86  ?  57  GLY   D N     1 
ATOM   3046 C CA    . GLY   D 1 58  ? -2.361  -36.779 19.182  1.00 24.82  ?  57  GLY   D CA    1 
ATOM   3047 C C     . GLY   D 1 58  ? -2.334  -38.241 19.650  1.00 25.54  ?  57  GLY   D C     1 
ATOM   3048 O O     . GLY   D 1 58  ? -1.877  -38.449 20.770  1.00 26.00  ?  57  GLY   D O     1 
ATOM   3049 N N     . ASN   D 1 59  ? -2.861  -39.225 18.866  1.00 24.95  ?  58  ASN   D N     1 
ATOM   3050 C CA    . ASN   D 1 59  ? -3.038  -40.611 19.303  1.00 24.12  ?  58  ASN   D CA    1 
ATOM   3051 C C     . ASN   D 1 59  ? -3.857  -40.771 20.584  1.00 24.04  ?  58  ASN   D C     1 
ATOM   3052 O O     . ASN   D 1 59  ? -3.590  -41.661 21.390  1.00 25.33  ?  58  ASN   D O     1 
ATOM   3053 C CB    . ASN   D 1 59  ? -1.714  -41.360 19.500  1.00 22.62  ?  58  ASN   D CB    1 
ATOM   3054 C CG    . ASN   D 1 59  ? -0.731  -41.127 18.378  1.00 22.49  ?  58  ASN   D CG    1 
ATOM   3055 O OD1   . ASN   D 1 59  ? 0.352   -40.633 18.645  1.00 21.59  ?  58  ASN   D OD1   1 
ATOM   3056 N ND2   . ASN   D 1 59  ? -1.094  -41.441 17.146  1.00 21.82  ?  58  ASN   D ND2   1 
ATOM   3057 N N     . GLN   D 1 60  ? -4.834  -39.913 20.805  1.00 24.61  ?  59  GLN   D N     1 
ATOM   3058 C CA    . GLN   D 1 60  ? -5.604  -39.960 22.034  1.00 26.40  ?  59  GLN   D CA    1 
ATOM   3059 C C     . GLN   D 1 60  ? -6.423  -41.262 22.097  1.00 26.04  ?  59  GLN   D C     1 
ATOM   3060 O O     . GLN   D 1 60  ? -6.352  -41.959 23.106  1.00 24.86  ?  59  GLN   D O     1 
ATOM   3061 C CB    . GLN   D 1 60  ? -6.448  -38.693 22.162  1.00 28.18  ?  59  GLN   D CB    1 
ATOM   3062 C CG    . GLN   D 1 60  ? -7.305  -38.655 23.424  1.00 31.69  ?  59  GLN   D CG    1 
ATOM   3063 C CD    . GLN   D 1 60  ? -8.737  -39.128 23.230  1.00 35.38  ?  59  GLN   D CD    1 
ATOM   3064 O OE1   . GLN   D 1 60  ? -9.355  -38.884 22.184  1.00 41.56  ?  59  GLN   D OE1   1 
ATOM   3065 N NE2   . GLN   D 1 60  ? -9.271  -39.841 24.217  1.00 33.89  ?  59  GLN   D NE2   1 
ATOM   3066 N N     . ASP   D 1 61  ? -7.157  -41.583 21.009  1.00 26.40  ?  60  ASP   D N     1 
ATOM   3067 C CA    . ASP   D 1 61  ? -7.939  -42.804 20.903  1.00 26.92  ?  60  ASP   D CA    1 
ATOM   3068 C C     . ASP   D 1 61  ? -7.422  -43.649 19.746  1.00 24.18  ?  60  ASP   D C     1 
ATOM   3069 O O     . ASP   D 1 61  ? -7.313  -43.123 18.648  1.00 23.74  ?  60  ASP   D O     1 
ATOM   3070 C CB    . ASP   D 1 61  ? -9.428  -42.514 20.782  1.00 30.77  ?  60  ASP   D CB    1 
ATOM   3071 C CG    . ASP   D 1 61  ? -10.355 -43.571 21.372  1.00 35.06  ?  60  ASP   D CG    1 
ATOM   3072 O OD1   . ASP   D 1 61  ? -9.852  -44.606 21.921  1.00 36.31  ?  60  ASP   D OD1   1 
ATOM   3073 O OD2   . ASP   D 1 61  ? -11.613 -43.347 21.276  1.00 47.40  -1 60  ASP   D OD2   1 
ATOM   3074 N N     . ASN   D 1 62  ? -7.145  -44.940 20.007  1.00 22.54  ?  61  ASN   D N     1 
ATOM   3075 C CA    . ASN   D 1 62  ? -6.432  -45.836 19.102  1.00 21.87  ?  61  ASN   D CA    1 
ATOM   3076 C C     . ASN   D 1 62  ? -7.219  -47.155 18.982  1.00 22.48  ?  61  ASN   D C     1 
ATOM   3077 O O     . ASN   D 1 62  ? -7.664  -47.718 19.990  1.00 21.98  ?  61  ASN   D O     1 
ATOM   3078 C CB    . ASN   D 1 62  ? -5.003  -46.116 19.556  1.00 20.95  ?  61  ASN   D CB    1 
ATOM   3079 C CG    . ASN   D 1 62  ? -4.271  -44.845 19.903  1.00 20.73  ?  61  ASN   D CG    1 
ATOM   3080 O OD1   . ASN   D 1 62  ? -3.704  -44.223 19.009  1.00 21.03  ?  61  ASN   D OD1   1 
ATOM   3081 N ND2   . ASN   D 1 62  ? -4.295  -44.444 21.167  1.00 20.77  ?  61  ASN   D ND2   1 
ATOM   3082 N N     . SER   D 1 63  ? -7.352  -47.648 17.741  1.00 21.99  ?  62  SER   D N     1 
ATOM   3083 C CA    . SER   D 1 63  ? -8.023  -48.884 17.430  1.00 22.33  ?  62  SER   D CA    1 
ATOM   3084 C C     . SER   D 1 63  ? -7.230  -49.604 16.345  1.00 22.39  ?  62  SER   D C     1 
ATOM   3085 O O     . SER   D 1 63  ? -6.856  -48.945 15.366  1.00 23.16  ?  62  SER   D O     1 
ATOM   3086 C CB    . SER   D 1 63  ? -9.454  -48.626 17.009  1.00 23.68  ?  62  SER   D CB    1 
ATOM   3087 O OG    . SER   D 1 63  ? -10.052 -49.841 16.581  1.00 23.48  ?  62  SER   D OG    1 
ATOM   3088 N N     . PHE   D 1 64  ? -6.990  -50.920 16.537  1.00 21.93  ?  63  PHE   D N     1 
ATOM   3089 C CA    . PHE   D 1 64  ? -6.281  -51.777 15.596  1.00 22.78  ?  63  PHE   D CA    1 
ATOM   3090 C C     . PHE   D 1 64  ? -7.082  -53.069 15.468  1.00 24.59  ?  63  PHE   D C     1 
ATOM   3091 O O     . PHE   D 1 64  ? -7.128  -53.836 16.452  1.00 24.95  ?  63  PHE   D O     1 
ATOM   3092 C CB    . PHE   D 1 64  ? -4.845  -52.074 16.082  1.00 21.86  ?  63  PHE   D CB    1 
ATOM   3093 C CG    . PHE   D 1 64  ? -4.014  -52.929 15.131  1.00 22.12  ?  63  PHE   D CG    1 
ATOM   3094 C CD1   . PHE   D 1 64  ? -4.129  -54.326 15.086  1.00 23.10  ?  63  PHE   D CD1   1 
ATOM   3095 C CD2   . PHE   D 1 64  ? -3.092  -52.321 14.276  1.00 22.32  ?  63  PHE   D CD2   1 
ATOM   3096 C CE1   . PHE   D 1 64  ? -3.343  -55.088 14.195  1.00 23.56  ?  63  PHE   D CE1   1 
ATOM   3097 C CE2   . PHE   D 1 64  ? -2.295  -53.069 13.416  1.00 22.39  ?  63  PHE   D CE2   1 
ATOM   3098 C CZ    . PHE   D 1 64  ? -2.425  -54.453 13.372  1.00 23.33  ?  63  PHE   D CZ    1 
ATOM   3099 N N     . ALA   D 1 65  ? -7.669  -53.312 14.284  1.00 25.20  ?  64  ALA   D N     1 
ATOM   3100 C CA    . ALA   D 1 65  ? -8.460  -54.492 13.994  1.00 27.63  ?  64  ALA   D CA    1 
ATOM   3101 C C     . ALA   D 1 65  ? -7.802  -55.238 12.849  1.00 28.60  ?  64  ALA   D C     1 
ATOM   3102 O O     . ALA   D 1 65  ? -7.480  -54.591 11.860  1.00 31.20  ?  64  ALA   D O     1 
ATOM   3103 C CB    . ALA   D 1 65  ? -9.899  -54.128 13.653  1.00 29.28  ?  64  ALA   D CB    1 
ATOM   3104 N N     . ILE   D 1 66  ? -7.574  -56.554 13.004  1.00 28.65  ?  65  ILE   D N     1 
ATOM   3105 C CA    . ILE   D 1 66  ? -6.948  -57.385 11.975  1.00 29.11  ?  65  ILE   D CA    1 
ATOM   3106 C C     . ILE   D 1 66  ? -7.816  -58.623 11.782  1.00 28.21  ?  65  ILE   D C     1 
ATOM   3107 O O     . ILE   D 1 66  ? -8.130  -59.268 12.759  1.00 27.88  ?  65  ILE   D O     1 
ATOM   3108 C CB    . ILE   D 1 66  ? -5.466  -57.701 12.265  1.00 28.95  ?  65  ILE   D CB    1 
ATOM   3109 C CG1   . ILE   D 1 66  ? -4.820  -58.506 11.147  1.00 31.44  ?  65  ILE   D CG1   1 
ATOM   3110 C CG2   . ILE   D 1 66  ? -5.248  -58.390 13.604  1.00 30.40  ?  65  ILE   D CG2   1 
ATOM   3111 C CD1   . ILE   D 1 66  ? -3.296  -58.404 11.119  1.00 31.82  ?  65  ILE   D CD1   1 
ATOM   3112 N N     . GLN   D 1 67  ? -8.232  -58.901 10.536  1.00 28.85  ?  66  GLN   D N     1 
ATOM   3113 C CA    . GLN   D 1 67  ? -8.975  -60.095 10.150  1.00 31.16  ?  66  GLN   D CA    1 
ATOM   3114 C C     . GLN   D 1 67  ? -8.086  -60.881 9.197   1.00 29.71  ?  66  GLN   D C     1 
ATOM   3115 O O     . GLN   D 1 67  ? -7.645  -60.308 8.211   1.00 27.35  ?  66  GLN   D O     1 
ATOM   3116 C CB    . GLN   D 1 67  ? -10.307 -59.723 9.493   1.00 35.25  ?  66  GLN   D CB    1 
ATOM   3117 C CG    . GLN   D 1 67  ? -11.368 -59.191 10.463  1.00 41.21  ?  66  GLN   D CG    1 
ATOM   3118 C CD    . GLN   D 1 67  ? -11.372 -57.711 10.861  1.00 47.67  ?  66  GLN   D CD    1 
ATOM   3119 O OE1   . GLN   D 1 67  ? -10.642 -56.829 10.346  1.00 49.45  ?  66  GLN   D OE1   1 
ATOM   3120 N NE2   . GLN   D 1 67  ? -12.250 -57.420 11.824  1.00 47.55  ?  66  GLN   D NE2   1 
ATOM   3121 N N     . LEU   D 1 68  ? -7.783  -62.148 9.539   1.00 29.81  ?  67  LEU   D N     1 
ATOM   3122 C CA    . LEU   D 1 68  ? -7.079  -63.085 8.668   1.00 30.85  ?  67  LEU   D CA    1 
ATOM   3123 C C     . LEU   D 1 68  ? -8.081  -64.166 8.220   1.00 33.40  ?  67  LEU   D C     1 
ATOM   3124 O O     . LEU   D 1 68  ? -8.929  -64.593 9.022   1.00 32.57  ?  67  LEU   D O     1 
ATOM   3125 C CB    . LEU   D 1 68  ? -5.844  -63.672 9.345   1.00 29.69  ?  67  LEU   D CB    1 
ATOM   3126 C CG    . LEU   D 1 68  ? -4.863  -62.658 9.935   1.00 28.96  ?  67  LEU   D CG    1 
ATOM   3127 C CD1   . LEU   D 1 68  ? -3.800  -63.302 10.807  1.00 29.69  ?  67  LEU   D CD1   1 
ATOM   3128 C CD2   . LEU   D 1 68  ? -4.217  -61.842 8.855   1.00 29.09  ?  67  LEU   D CD2   1 
ATOM   3129 N N     . ALA   D 1 69  ? -8.024  -64.547 6.923   1.00 33.72  ?  68  ALA   D N     1 
ATOM   3130 C CA    . ALA   D 1 69  ? -8.687  -65.744 6.419   1.00 35.92  ?  68  ALA   D CA    1 
ATOM   3131 C C     . ALA   D 1 69  ? -7.637  -66.598 5.719   1.00 37.63  ?  68  ALA   D C     1 
ATOM   3132 O O     . ALA   D 1 69  ? -7.052  -66.110 4.759   1.00 35.88  ?  68  ALA   D O     1 
ATOM   3133 C CB    . ALA   D 1 69  ? -9.847  -65.376 5.504   1.00 36.77  ?  68  ALA   D CB    1 
ATOM   3134 N N     . ASN   D 1 70  ? -7.442  -67.844 6.211   1.00 41.28  ?  69  ASN   D N     1 
ATOM   3135 C CA    . ASN   D 1 70  ? -6.393  -68.772 5.810   1.00 44.81  ?  69  ASN   D CA    1 
ATOM   3136 C C     . ASN   D 1 70  ? -6.938  -69.822 4.826   1.00 47.07  ?  69  ASN   D C     1 
ATOM   3137 O O     . ASN   D 1 70  ? -8.043  -70.324 5.033   1.00 49.10  ?  69  ASN   D O     1 
ATOM   3138 C CB    . ASN   D 1 70  ? -5.858  -69.471 7.059   1.00 48.16  ?  69  ASN   D CB    1 
ATOM   3139 C CG    . ASN   D 1 70  ? -4.530  -70.157 6.872   1.00 52.45  ?  69  ASN   D CG    1 
ATOM   3140 O OD1   . ASN   D 1 70  ? -3.970  -70.203 5.765   1.00 57.11  ?  69  ASN   D OD1   1 
ATOM   3141 N ND2   . ASN   D 1 70  ? -3.991  -70.661 7.973   1.00 56.57  ?  69  ASN   D ND2   1 
ATOM   3142 N N     . TYR   D 1 71  ? -6.122  -70.196 3.812   1.00 48.40  ?  70  TYR   D N     1 
ATOM   3143 C CA    . TYR   D 1 71  ? -6.458  -71.125 2.729   1.00 51.04  ?  70  TYR   D CA    1 
ATOM   3144 C C     . TYR   D 1 71  ? -5.262  -71.205 1.712   1.00 50.55  ?  70  TYR   D C     1 
ATOM   3145 O O     . TYR   D 1 71  ? -4.182  -71.827 1.945   1.00 44.89  ?  70  TYR   D O     1 
ATOM   3146 C CB    . TYR   D 1 71  ? -7.756  -70.927 1.917   1.00 53.37  ?  70  TYR   D CB    1 
ATOM   3147 C CG    . TYR   D 1 71  ? -8.444  -69.566 1.889   1.00 53.07  ?  70  TYR   D CG    1 
ATOM   3148 C CD1   . TYR   D 1 71  ? -7.749  -68.400 1.579   1.00 52.94  ?  70  TYR   D CD1   1 
ATOM   3149 C CD2   . TYR   D 1 71  ? -9.794  -69.439 2.246   1.00 54.89  ?  70  TYR   D CD2   1 
ATOM   3150 C CE1   . TYR   D 1 71  ? -8.381  -67.159 1.598   1.00 54.88  ?  70  TYR   D CE1   1 
ATOM   3151 C CE2   . TYR   D 1 71  ? -10.434 -68.206 2.284   1.00 55.66  ?  70  TYR   D CE2   1 
ATOM   3152 C CZ    . TYR   D 1 71  ? -9.729  -67.057 1.940   1.00 57.09  ?  70  TYR   D CZ    1 
ATOM   3153 O OH    . TYR   D 1 71  ? -10.382 -65.851 1.958   1.00 56.97  ?  70  TYR   D OH    1 
ATOM   3154 N N     . THR   D 1 78  ? -9.015  -71.639 10.403  1.00 56.99  ?  77  THR   D N     1 
ATOM   3155 C CA    . THR   D 1 78  ? -9.282  -70.899 9.142   1.00 58.60  ?  77  THR   D CA    1 
ATOM   3156 C C     . THR   D 1 78  ? -9.296  -69.379 9.399   1.00 53.93  ?  77  THR   D C     1 
ATOM   3157 O O     . THR   D 1 78  ? -8.380  -68.685 8.909   1.00 48.52  ?  77  THR   D O     1 
ATOM   3158 C CB    . THR   D 1 78  ? -10.524 -71.424 8.390   1.00 66.64  ?  77  THR   D CB    1 
ATOM   3159 O OG1   . THR   D 1 78  ? -10.844 -70.490 7.358   1.00 70.50  ?  77  THR   D OG1   1 
ATOM   3160 C CG2   . THR   D 1 78  ? -11.763 -71.793 9.208   1.00 70.32  ?  77  THR   D CG2   1 
ATOM   3161 N N     . LYS   D 1 79  ? -10.335 -68.870 10.100  1.00 48.84  ?  78  LYS   D N     1 
ATOM   3162 C CA    . LYS   D 1 79  ? -10.497 -67.443 10.362  1.00 47.53  ?  78  LYS   D CA    1 
ATOM   3163 C C     . LYS   D 1 79  ? -9.839  -67.095 11.699  1.00 44.62  ?  78  LYS   D C     1 
ATOM   3164 O O     . LYS   D 1 79  ? -9.897  -67.859 12.651  1.00 45.71  ?  78  LYS   D O     1 
ATOM   3165 C CB    . LYS   D 1 79  ? -11.934 -66.908 10.369  1.00 50.92  ?  78  LYS   D CB    1 
ATOM   3166 C CG    . LYS   D 1 79  ? -12.590 -66.830 9.008   1.00 55.38  ?  78  LYS   D CG    1 
ATOM   3167 C CD    . LYS   D 1 79  ? -14.083 -66.496 9.040   1.00 60.12  ?  78  LYS   D CD    1 
ATOM   3168 C CE    . LYS   D 1 79  ? -14.419 -65.046 9.295   1.00 60.27  ?  78  LYS   D CE    1 
ATOM   3169 N NZ    . LYS   D 1 79  ? -15.860 -64.789 9.156   1.00 60.61  1  78  LYS   D NZ    1 
ATOM   3170 N N     . TRP   D 1 80  ? -9.308  -65.876 11.765  1.00 42.66  ?  79  TRP   D N     1 
ATOM   3171 C CA    . TRP   D 1 80  ? -8.588  -65.351 12.905  1.00 42.28  ?  79  TRP   D CA    1 
ATOM   3172 C C     . TRP   D 1 80  ? -8.778  -63.850 12.911  1.00 40.35  ?  79  TRP   D C     1 
ATOM   3173 O O     . TRP   D 1 80  ? -8.483  -63.242 11.899  1.00 41.63  ?  79  TRP   D O     1 
ATOM   3174 C CB    . TRP   D 1 80  ? -7.101  -65.714 12.780  1.00 42.73  ?  79  TRP   D CB    1 
ATOM   3175 C CG    . TRP   D 1 80  ? -6.362  -65.661 14.077  1.00 43.04  ?  79  TRP   D CG    1 
ATOM   3176 C CD1   . TRP   D 1 80  ? -6.193  -66.713 14.914  1.00 43.57  ?  79  TRP   D CD1   1 
ATOM   3177 C CD2   . TRP   D 1 80  ? -5.635  -64.550 14.652  1.00 43.71  ?  79  TRP   D CD2   1 
ATOM   3178 N NE1   . TRP   D 1 80  ? -5.440  -66.336 15.996  1.00 44.05  ?  79  TRP   D NE1   1 
ATOM   3179 C CE2   . TRP   D 1 80  ? -5.058  -65.030 15.858  1.00 43.72  ?  79  TRP   D CE2   1 
ATOM   3180 C CE3   . TRP   D 1 80  ? -5.375  -63.219 14.264  1.00 45.84  ?  79  TRP   D CE3   1 
ATOM   3181 C CZ2   . TRP   D 1 80  ? -4.264  -64.228 16.684  1.00 42.41  ?  79  TRP   D CZ2   1 
ATOM   3182 C CZ3   . TRP   D 1 80  ? -4.549  -62.436 15.058  1.00 41.96  ?  79  TRP   D CZ3   1 
ATOM   3183 C CH2   . TRP   D 1 80  ? -4.008  -62.937 16.257  1.00 40.99  ?  79  TRP   D CH2   1 
HETATM 3184 N N     . CSD   D 1 81  ? -9.310  -63.258 13.988  1.00 41.57  ?  80  CSD   D N     1 
HETATM 3185 C CA    . CSD   D 1 81  ? -9.279  -61.805 14.111  1.00 40.17  ?  80  CSD   D CA    1 
HETATM 3186 C CB    . CSD   D 1 81  ? -10.563 -61.156 13.600  1.00 44.23  ?  80  CSD   D CB    1 
HETATM 3187 S SG    . CSD   D 1 81  ? -11.950 -61.423 14.677  1.00 52.73  ?  80  CSD   D SG    1 
HETATM 3188 C C     . CSD   D 1 81  ? -8.904  -61.329 15.504  1.00 35.37  ?  80  CSD   D C     1 
HETATM 3189 O O     . CSD   D 1 81  ? -8.929  -62.103 16.452  1.00 33.13  ?  80  CSD   D O     1 
HETATM 3190 O OD1   . CSD   D 1 81  ? -11.859 -60.391 15.794  1.00 50.42  ?  80  CSD   D OD1   1 
HETATM 3191 O OD2   . CSD   D 1 81  ? -13.317 -61.418 13.786  1.00 57.87  ?  80  CSD   D OD2   1 
ATOM   3192 N N     . ALA   D 1 82  ? -8.532  -60.035 15.550  1.00 31.47  ?  81  ALA   D N     1 
ATOM   3193 C CA    . ALA   D 1 82  ? -8.117  -59.337 16.744  1.00 29.79  ?  81  ALA   D CA    1 
ATOM   3194 C C     . ALA   D 1 82  ? -8.619  -57.895 16.668  1.00 27.95  ?  81  ALA   D C     1 
ATOM   3195 O O     . ALA   D 1 82  ? -8.515  -57.297 15.601  1.00 29.90  ?  81  ALA   D O     1 
ATOM   3196 C CB    . ALA   D 1 82  ? -6.611  -59.406 16.916  1.00 29.74  ?  81  ALA   D CB    1 
ATOM   3197 N N     . LEU   D 1 83  ? -9.245  -57.391 17.746  1.00 25.25  ?  82  LEU   D N     1 
ATOM   3198 C CA    . LEU   D 1 83  ? -9.567  -55.987 17.949  1.00 24.30  ?  82  LEU   D CA    1 
ATOM   3199 C C     . LEU   D 1 83  ? -8.779  -55.519 19.167  1.00 22.86  ?  82  LEU   D C     1 
ATOM   3200 O O     . LEU   D 1 83  ? -9.010  -56.039 20.263  1.00 22.40  ?  82  LEU   D O     1 
ATOM   3201 C CB    . LEU   D 1 83  ? -11.075 -55.870 18.189  1.00 26.30  ?  82  LEU   D CB    1 
ATOM   3202 C CG    . LEU   D 1 83  ? -11.648 -54.476 18.483  1.00 26.42  ?  82  LEU   D CG    1 
ATOM   3203 C CD1   . LEU   D 1 83  ? -11.269 -53.455 17.395  1.00 26.78  ?  82  LEU   D CD1   1 
ATOM   3204 C CD2   . LEU   D 1 83  ? -13.143 -54.593 18.527  1.00 28.70  ?  82  LEU   D CD2   1 
ATOM   3205 N N     . LEU   D 1 84  ? -7.863  -54.562 18.958  1.00 22.82  ?  83  LEU   D N     1 
ATOM   3206 C CA    . LEU   D 1 84  ? -7.050  -53.935 20.000  1.00 22.64  ?  83  LEU   D CA    1 
ATOM   3207 C C     . LEU   D 1 84  ? -7.442  -52.461 20.117  1.00 22.39  ?  83  LEU   D C     1 
ATOM   3208 O O     . LEU   D 1 84  ? -7.442  -51.777 19.097  1.00 22.85  ?  83  LEU   D O     1 
ATOM   3209 C CB    . LEU   D 1 84  ? -5.588  -54.086 19.614  1.00 22.98  ?  83  LEU   D CB    1 
ATOM   3210 C CG    . LEU   D 1 84  ? -5.079  -55.452 19.148  1.00 23.68  ?  83  LEU   D CG    1 
ATOM   3211 C CD1   . LEU   D 1 84  ? -3.594  -55.317 18.884  1.00 23.05  ?  83  LEU   D CD1   1 
ATOM   3212 C CD2   . LEU   D 1 84  ? -5.352  -56.562 20.136  1.00 25.54  ?  83  LEU   D CD2   1 
ATOM   3213 N N     . THR   D 1 85  ? -7.784  -51.963 21.328  1.00 21.78  ?  84  THR   D N     1 
ATOM   3214 C CA    . THR   D 1 85  ? -8.183  -50.562 21.518  1.00 21.77  ?  84  THR   D CA    1 
ATOM   3215 C C     . THR   D 1 85  ? -7.418  -49.965 22.700  1.00 21.26  ?  84  THR   D C     1 
ATOM   3216 O O     . THR   D 1 85  ? -7.205  -50.677 23.658  1.00 20.80  ?  84  THR   D O     1 
ATOM   3217 C CB    . THR   D 1 85  ? -9.692  -50.356 21.703  1.00 22.47  ?  84  THR   D CB    1 
ATOM   3218 O OG1   . THR   D 1 85  ? -10.036 -51.042 22.904  1.00 22.07  ?  84  THR   D OG1   1 
ATOM   3219 C CG2   . THR   D 1 85  ? -10.489 -50.868 20.515  1.00 23.40  ?  84  THR   D CG2   1 
ATOM   3220 N N     . LYS   D 1 86  ? -7.055  -48.666 22.609  1.00 21.55  ?  85  LYS   D N     1 
ATOM   3221 C CA    . LYS   D 1 86  ? -6.270  -48.006 23.658  1.00 21.49  ?  85  LYS   D CA    1 
ATOM   3222 C C     . LYS   D 1 86  ? -6.656  -46.527 23.679  1.00 21.84  ?  85  LYS   D C     1 
ATOM   3223 O O     . LYS   D 1 86  ? -6.459  -45.804 22.679  1.00 20.92  ?  85  LYS   D O     1 
ATOM   3224 C CB    . LYS   D 1 86  ? -4.768  -48.223 23.469  1.00 19.72  ?  85  LYS   D CB    1 
ATOM   3225 C CG    . LYS   D 1 86  ? -3.868  -47.659 24.575  1.00 18.96  ?  85  LYS   D CG    1 
ATOM   3226 C CD    . LYS   D 1 86  ? -2.372  -47.915 24.427  1.00 17.93  ?  85  LYS   D CD    1 
ATOM   3227 C CE    . LYS   D 1 86  ? -1.889  -49.368 24.478  1.00 17.40  ?  85  LYS   D CE    1 
ATOM   3228 N NZ    . LYS   D 1 86  ? -2.234  -50.089 25.684  1.00 17.76  1  85  LYS   D NZ    1 
ATOM   3229 N N     . LYS   D 1 87  ? -7.142  -46.097 24.851  1.00 23.11  ?  86  LYS   D N     1 
ATOM   3230 C CA    . LYS   D 1 87  ? -7.770  -44.807 25.039  1.00 25.27  ?  86  LYS   D CA    1 
ATOM   3231 C C     . LYS   D 1 87  ? -7.000  -44.096 26.143  1.00 23.55  ?  86  LYS   D C     1 
ATOM   3232 O O     . LYS   D 1 87  ? -6.884  -44.624 27.233  1.00 22.79  ?  86  LYS   D O     1 
ATOM   3233 C CB    . LYS   D 1 87  ? -9.272  -44.957 25.314  1.00 28.57  ?  86  LYS   D CB    1 
ATOM   3234 C CG    . LYS   D 1 87  ? -10.058 -43.654 25.335  1.00 33.43  ?  86  LYS   D CG    1 
ATOM   3235 C CD    . LYS   D 1 87  ? -11.542 -43.787 25.692  1.00 37.77  ?  86  LYS   D CD    1 
ATOM   3236 C CE    . LYS   D 1 87  ? -11.773 -44.028 27.148  1.00 41.44  ?  86  LYS   D CE    1 
ATOM   3237 N NZ    . LYS   D 1 87  ? -13.184 -43.788 27.504  1.00 46.63  1  86  LYS   D NZ    1 
ATOM   3238 N N     . TYR   D 1 88  ? -6.496  -42.894 25.826  1.00 22.63  ?  87  TYR   D N     1 
ATOM   3239 C CA    . TYR   D 1 88  ? -5.731  -42.061 26.726  1.00 22.13  ?  87  TYR   D CA    1 
ATOM   3240 C C     . TYR   D 1 88  ? -6.643  -40.931 27.179  1.00 23.72  ?  87  TYR   D C     1 
ATOM   3241 O O     . TYR   D 1 88  ? -7.661  -40.674 26.524  1.00 24.14  ?  87  TYR   D O     1 
ATOM   3242 C CB    . TYR   D 1 88  ? -4.481  -41.584 25.986  1.00 21.70  ?  87  TYR   D CB    1 
ATOM   3243 C CG    . TYR   D 1 88  ? -3.402  -42.639 25.798  1.00 20.92  ?  87  TYR   D CG    1 
ATOM   3244 C CD1   . TYR   D 1 88  ? -2.530  -42.948 26.837  1.00 20.66  ?  87  TYR   D CD1   1 
ATOM   3245 C CD2   . TYR   D 1 88  ? -3.211  -43.286 24.571  1.00 20.09  ?  87  TYR   D CD2   1 
ATOM   3246 C CE1   . TYR   D 1 88  ? -1.502  -43.854 26.651  1.00 20.57  ?  87  TYR   D CE1   1 
ATOM   3247 C CE2   . TYR   D 1 88  ? -2.188  -44.192 24.377  1.00 19.68  ?  87  TYR   D CE2   1 
ATOM   3248 C CZ    . TYR   D 1 88  ? -1.332  -44.495 25.423  1.00 20.04  ?  87  TYR   D CZ    1 
ATOM   3249 O OH    . TYR   D 1 88  ? -0.279  -45.380 25.313  1.00 19.41  ?  87  TYR   D OH    1 
ATOM   3250 N N     . PRO   D 1 89  ? -6.303  -40.191 28.253  1.00 24.85  ?  88  PRO   D N     1 
ATOM   3251 C CA    . PRO   D 1 89  ? -7.105  -39.030 28.626  1.00 27.12  ?  88  PRO   D CA    1 
ATOM   3252 C C     . PRO   D 1 89  ? -6.977  -37.865 27.638  1.00 28.31  ?  88  PRO   D C     1 
ATOM   3253 O O     . PRO   D 1 89  ? -5.987  -37.745 26.917  1.00 26.09  ?  88  PRO   D O     1 
ATOM   3254 C CB    . PRO   D 1 89  ? -6.617  -38.697 30.041  1.00 27.57  ?  88  PRO   D CB    1 
ATOM   3255 C CG    . PRO   D 1 89  ? -5.279  -39.399 30.184  1.00 25.72  ?  88  PRO   D CG    1 
ATOM   3256 C CD    . PRO   D 1 89  ? -5.133  -40.406 29.123  1.00 23.81  ?  88  PRO   D CD    1 
ATOM   3257 N N     . GLU   D 1 90  ? -7.988  -36.984 27.672  1.00 32.80  ?  89  GLU   D N     1 
ATOM   3258 C CA    . GLU   D 1 90  ? -8.052  -35.723 26.944  1.00 36.05  ?  89  GLU   D CA    1 
ATOM   3259 C C     . GLU   D 1 90  ? -6.936  -34.812 27.463  1.00 33.35  ?  89  GLU   D C     1 
ATOM   3260 O O     . GLU   D 1 90  ? -6.748  -34.730 28.671  1.00 32.78  ?  89  GLU   D O     1 
ATOM   3261 C CB    . GLU   D 1 90  ? -9.385  -35.013 27.209  1.00 43.82  ?  89  GLU   D CB    1 
ATOM   3262 C CG    . GLU   D 1 90  ? -10.683 -35.759 26.875  1.00 51.61  ?  89  GLU   D CG    1 
ATOM   3263 C CD    . GLU   D 1 90  ? -11.250 -35.604 25.480  1.00 56.37  ?  89  GLU   D CD    1 
ATOM   3264 O OE1   . GLU   D 1 90  ? -10.462 -35.875 24.550  1.00 63.83  ?  89  GLU   D OE1   1 
ATOM   3265 O OE2   . GLU   D 1 90  ? -12.447 -35.270 25.326  1.00 57.24  ?  89  GLU   D OE2   1 
ATOM   3266 N N     . ARG   D 1 91  ? -6.154  -34.192 26.567  1.00 32.55  ?  90  ARG   D N     1 
ATOM   3267 C CA    . ARG   D 1 91  ? -4.988  -33.415 26.981  1.00 32.60  ?  90  ARG   D CA    1 
ATOM   3268 C C     . ARG   D 1 91  ? -5.385  -32.022 27.511  1.00 34.24  ?  90  ARG   D C     1 
ATOM   3269 O O     . ARG   D 1 91  ? -6.559  -31.623 27.490  1.00 33.29  ?  90  ARG   D O     1 
ATOM   3270 C CB    . ARG   D 1 91  ? -3.989  -33.350 25.826  1.00 32.00  ?  90  ARG   D CB    1 
ATOM   3271 C CG    . ARG   D 1 91  ? -4.332  -32.447 24.645  1.00 32.58  ?  90  ARG   D CG    1 
ATOM   3272 C CD    . ARG   D 1 91  ? -3.114  -32.079 23.868  1.00 32.64  ?  90  ARG   D CD    1 
ATOM   3273 N NE    . ARG   D 1 91  ? -2.184  -31.284 24.681  1.00 32.43  ?  90  ARG   D NE    1 
ATOM   3274 C CZ    . ARG   D 1 91  ? -0.854  -31.380 24.675  1.00 33.86  ?  90  ARG   D CZ    1 
ATOM   3275 N NH1   . ARG   D 1 91  ? -0.208  -32.185 23.830  1.00 33.04  ?  90  ARG   D NH1   1 
ATOM   3276 N NH2   . ARG   D 1 91  ? -0.107  -30.632 25.479  1.00 34.92  ?  90  ARG   D NH2   1 
ATOM   3277 N N     . LYS   D 1 92  ? -4.367  -31.298 28.007  1.00 35.32  ?  91  LYS   D N     1 
ATOM   3278 C CA    . LYS   D 1 92  ? -4.437  -29.876 28.340  1.00 38.26  ?  91  LYS   D CA    1 
ATOM   3279 C C     . LYS   D 1 92  ? -3.187  -29.205 27.774  1.00 37.75  ?  91  LYS   D C     1 
ATOM   3280 O O     . LYS   D 1 92  ? -2.271  -29.917 27.346  1.00 37.87  ?  91  LYS   D O     1 
ATOM   3281 C CB    . LYS   D 1 92  ? -4.569  -29.667 29.856  1.00 38.54  ?  91  LYS   D CB    1 
ATOM   3282 C CG    . LYS   D 1 92  ? -5.680  -30.441 30.494  1.00 39.20  ?  91  LYS   D CG    1 
ATOM   3283 C CD    . LYS   D 1 92  ? -6.095  -29.891 31.852  1.00 41.29  ?  91  LYS   D CD    1 
ATOM   3284 C CE    . LYS   D 1 92  ? -7.215  -30.681 32.402  1.00 41.52  ?  91  LYS   D CE    1 
ATOM   3285 N NZ    . LYS   D 1 92  ? -7.515  -30.261 33.766  1.00 43.07  ?  91  LYS   D NZ    1 
ATOM   3286 N N     . PRO   D 1 93  ? -3.118  -27.849 27.702  1.00 38.28  ?  92  PRO   D N     1 
ATOM   3287 C CA    . PRO   D 1 93  ? -1.974  -27.158 27.091  1.00 38.34  ?  92  PRO   D CA    1 
ATOM   3288 C C     . PRO   D 1 93  ? -0.584  -27.521 27.619  1.00 36.44  ?  92  PRO   D C     1 
ATOM   3289 O O     . PRO   D 1 93  ? 0.341   -27.656 26.795  1.00 35.23  ?  92  PRO   D O     1 
ATOM   3290 C CB    . PRO   D 1 93  ? -2.263  -25.678 27.337  1.00 40.25  ?  92  PRO   D CB    1 
ATOM   3291 C CG    . PRO   D 1 93  ? -3.781  -25.693 27.282  1.00 41.46  ?  92  PRO   D CG    1 
ATOM   3292 C CD    . PRO   D 1 93  ? -4.171  -26.882 28.073  1.00 40.15  ?  92  PRO   D CD    1 
ATOM   3293 N N     . ASP   D 1 94  ? -0.462  -27.704 28.954  1.00 33.77  ?  93  ASP   D N     1 
ATOM   3294 C CA    . ASP   D 1 94  ? 0.812   -28.001 29.592  1.00 33.04  ?  93  ASP   D CA    1 
ATOM   3295 C C     . ASP   D 1 94  ? 1.003   -29.524 29.778  1.00 30.46  ?  93  ASP   D C     1 
ATOM   3296 O O     . ASP   D 1 94  ? 0.500   -30.148 30.712  1.00 29.45  ?  93  ASP   D O     1 
ATOM   3297 C CB    . ASP   D 1 94  ? 0.994   -27.223 30.894  1.00 34.48  ?  93  ASP   D CB    1 
ATOM   3298 C CG    . ASP   D 1 94  ? 2.417   -27.237 31.448  1.00 34.14  ?  93  ASP   D CG    1 
ATOM   3299 O OD1   . ASP   D 1 94  ? 3.327   -27.737 30.764  1.00 32.92  ?  93  ASP   D OD1   1 
ATOM   3300 O OD2   . ASP   D 1 94  ? 2.612   -26.748 32.559  1.00 36.21  -1 93  ASP   D OD2   1 
ATOM   3301 N N     . VAL   D 1 95  ? 1.794   -30.121 28.888  1.00 29.46  ?  94  VAL   D N     1 
ATOM   3302 C CA    . VAL   D 1 95  ? 2.233   -31.502 28.980  1.00 27.14  ?  94  VAL   D CA    1 
ATOM   3303 C C     . VAL   D 1 95  ? 3.094   -31.759 30.211  1.00 26.66  ?  94  VAL   D C     1 
ATOM   3304 O O     . VAL   D 1 95  ? 3.048   -32.883 30.705  1.00 24.12  ?  94  VAL   D O     1 
ATOM   3305 C CB    . VAL   D 1 95  ? 2.949   -31.924 27.685  1.00 26.76  ?  94  VAL   D CB    1 
ATOM   3306 C CG1   . VAL   D 1 95  ? 4.330   -31.294 27.542  1.00 27.71  ?  94  VAL   D CG1   1 
ATOM   3307 C CG2   . VAL   D 1 95  ? 3.002   -33.446 27.513  1.00 25.16  ?  94  VAL   D CG2   1 
ATOM   3308 N N     . LEU   D 1 96  ? 3.854   -30.746 30.691  1.00 28.30  ?  95  LEU   D N     1 
ATOM   3309 C CA    . LEU   D 1 96  ? 4.697   -30.911 31.869  1.00 28.80  ?  95  LEU   D CA    1 
ATOM   3310 C C     . LEU   D 1 96  ? 3.904   -31.001 33.168  1.00 28.68  ?  95  LEU   D C     1 
ATOM   3311 O O     . LEU   D 1 96  ? 4.462   -31.437 34.163  1.00 30.84  ?  95  LEU   D O     1 
ATOM   3312 C CB    . LEU   D 1 96  ? 5.749   -29.813 31.928  1.00 30.88  ?  95  LEU   D CB    1 
ATOM   3313 C CG    . LEU   D 1 96  ? 6.660   -29.664 30.701  1.00 31.31  ?  95  LEU   D CG    1 
ATOM   3314 C CD1   . LEU   D 1 96  ? 7.726   -28.654 31.042  1.00 33.58  ?  95  LEU   D CD1   1 
ATOM   3315 C CD2   . LEU   D 1 96  ? 7.298   -30.968 30.227  1.00 29.95  ?  95  LEU   D CD2   1 
ATOM   3316 N N     . ALA   D 1 97  ? 2.638   -30.601 33.208  1.00 28.84  ?  96  ALA   D N     1 
ATOM   3317 C CA    . ALA   D 1 97  ? 1.874   -30.553 34.448  1.00 29.32  ?  96  ALA   D CA    1 
ATOM   3318 C C     . ALA   D 1 97  ? 0.967   -31.781 34.484  1.00 27.78  ?  96  ALA   D C     1 
ATOM   3319 O O     . ALA   D 1 97  ? 0.238   -32.031 33.534  1.00 26.43  ?  96  ALA   D O     1 
ATOM   3320 C CB    . ALA   D 1 97  ? 1.071   -29.275 34.525  1.00 30.98  ?  96  ALA   D CB    1 
ATOM   3321 N N     . PHE   D 1 98  ? 0.955   -32.469 35.625  1.00 27.63  ?  97  PHE   D N     1 
ATOM   3322 C CA    . PHE   D 1 98  ? 0.076   -33.587 35.890  1.00 27.91  ?  97  PHE   D CA    1 
ATOM   3323 C C     . PHE   D 1 98  ? -1.359  -33.080 35.917  1.00 29.18  ?  97  PHE   D C     1 
ATOM   3324 O O     . PHE   D 1 98  ? -1.552  -31.933 36.320  1.00 31.77  ?  97  PHE   D O     1 
ATOM   3325 C CB    . PHE   D 1 98  ? 0.465   -34.255 37.227  1.00 27.42  ?  97  PHE   D CB    1 
ATOM   3326 C CG    . PHE   D 1 98  ? -0.131  -35.640 37.413  1.00 26.98  ?  97  PHE   D CG    1 
ATOM   3327 C CD1   . PHE   D 1 98  ? 0.240   -36.688 36.551  1.00 26.97  ?  97  PHE   D CD1   1 
ATOM   3328 C CD2   . PHE   D 1 98  ? -0.950  -35.941 38.481  1.00 27.68  ?  97  PHE   D CD2   1 
ATOM   3329 C CE1   . PHE   D 1 98  ? -0.263  -37.978 36.716  1.00 27.31  ?  97  PHE   D CE1   1 
ATOM   3330 C CE2   . PHE   D 1 98  ? -1.421  -37.241 38.680  1.00 28.27  ?  97  PHE   D CE2   1 
ATOM   3331 C CZ    . PHE   D 1 98  ? -1.083  -38.266 37.791  1.00 28.22  ?  97  PHE   D CZ    1 
ATOM   3332 N N     . GLY   D 1 99  ? -2.324  -33.961 35.580  1.00 28.59  ?  98  GLY   D N     1 
ATOM   3333 C CA    . GLY   D 1 99  ? -3.758  -33.719 35.688  1.00 29.69  ?  98  GLY   D CA    1 
ATOM   3334 C C     . GLY   D 1 99  ? -4.486  -33.642 34.344  1.00 30.78  ?  98  GLY   D C     1 
ATOM   3335 O O     . GLY   D 1 99  ? -5.490  -32.958 34.257  1.00 31.47  ?  98  GLY   D O     1 
ATOM   3336 N N     . TRP   D 1 100 ? -4.030  -34.364 33.296  1.00 30.99  ?  99  TRP   D N     1 
ATOM   3337 C CA    . TRP   D 1 100 ? -4.811  -34.587 32.068  1.00 31.73  ?  99  TRP   D CA    1 
ATOM   3338 C C     . TRP   D 1 100 ? -5.929  -35.582 32.376  1.00 30.90  ?  99  TRP   D C     1 
ATOM   3339 O O     . TRP   D 1 100 ? -5.629  -36.761 32.587  1.00 30.73  ?  99  TRP   D O     1 
ATOM   3340 C CB    . TRP   D 1 100 ? -3.922  -35.148 30.946  1.00 29.51  ?  99  TRP   D CB    1 
ATOM   3341 C CG    . TRP   D 1 100 ? -2.970  -34.179 30.332  1.00 29.10  ?  99  TRP   D CG    1 
ATOM   3342 C CD1   . TRP   D 1 100 ? -2.568  -32.950 30.773  1.00 30.08  ?  99  TRP   D CD1   1 
ATOM   3343 C CD2   . TRP   D 1 100 ? -2.277  -34.412 29.104  1.00 29.13  ?  99  TRP   D CD2   1 
ATOM   3344 N NE1   . TRP   D 1 100 ? -1.675  -32.401 29.895  1.00 29.50  ?  99  TRP   D NE1   1 
ATOM   3345 C CE2   . TRP   D 1 100 ? -1.496  -33.258 28.847  1.00 29.30  ?  99  TRP   D CE2   1 
ATOM   3346 C CE3   . TRP   D 1 100 ? -2.263  -35.470 28.181  1.00 28.47  ?  99  TRP   D CE3   1 
ATOM   3347 C CZ2   . TRP   D 1 100 ? -0.698  -33.141 27.704  1.00 30.04  ?  99  TRP   D CZ2   1 
ATOM   3348 C CZ3   . TRP   D 1 100 ? -1.495  -35.342 27.034  1.00 28.58  ?  99  TRP   D CZ3   1 
ATOM   3349 C CH2   . TRP   D 1 100 ? -0.685  -34.209 26.822  1.00 30.06  ?  99  TRP   D CH2   1 
ATOM   3350 N N     . GLY   D 1 101 ? -7.180  -35.120 32.503  1.00 31.86  ?  100 GLY   D N     1 
ATOM   3351 C CA    . GLY   D 1 101 ? -8.315  -35.973 32.860  1.00 31.82  ?  100 GLY   D CA    1 
ATOM   3352 C C     . GLY   D 1 101 ? -8.067  -36.803 34.132  1.00 31.85  ?  100 GLY   D C     1 
ATOM   3353 O O     . GLY   D 1 101 ? -7.427  -36.340 35.071  1.00 34.63  ?  100 GLY   D O     1 
ATOM   3354 N N     . ASN   D 1 102 ? -8.422  -38.086 34.092  1.00 31.16  ?  101 ASN   D N     1 
ATOM   3355 C CA    . ASN   D 1 102 ? -8.260  -39.061 35.171  1.00 30.93  ?  101 ASN   D CA    1 
ATOM   3356 C C     . ASN   D 1 102 ? -6.865  -39.753 35.185  1.00 28.02  ?  101 ASN   D C     1 
ATOM   3357 O O     . ASN   D 1 102 ? -6.651  -40.648 35.988  1.00 25.36  ?  101 ASN   D O     1 
ATOM   3358 C CB    . ASN   D 1 102 ? -9.374  -40.097 35.054  1.00 33.06  ?  101 ASN   D CB    1 
ATOM   3359 C CG    . ASN   D 1 102 ? -9.239  -40.964 33.811  1.00 33.68  ?  101 ASN   D CG    1 
ATOM   3360 O OD1   . ASN   D 1 102 ? -8.296  -40.809 33.000  1.00 30.87  ?  101 ASN   D OD1   1 
ATOM   3361 N ND2   . ASN   D 1 102 ? -10.171 -41.885 33.651  1.00 34.90  ?  101 ASN   D ND2   1 
ATOM   3362 N N     . GLU   D 1 103 ? -5.936  -39.382 34.276  1.00 26.66  ?  102 GLU   D N     1 
ATOM   3363 C CA    . GLU   D 1 103 ? -4.571  -39.870 34.228  1.00 25.51  ?  102 GLU   D CA    1 
ATOM   3364 C C     . GLU   D 1 103 ? -4.521  -41.403 34.142  1.00 24.51  ?  102 GLU   D C     1 
ATOM   3365 O O     . GLU   D 1 103 ? -3.644  -42.008 34.741  1.00 24.12  ?  102 GLU   D O     1 
ATOM   3366 C CB    . GLU   D 1 103 ? -3.802  -39.179 35.360  1.00 26.33  ?  102 GLU   D CB    1 
ATOM   3367 C CG    . GLU   D 1 103 ? -3.479  -37.713 35.099  1.00 26.79  ?  102 GLU   D CG    1 
ATOM   3368 C CD    . GLU   D 1 103 ? -2.446  -37.451 34.008  1.00 26.87  ?  102 GLU   D CD    1 
ATOM   3369 O OE1   . GLU   D 1 103 ? -1.945  -38.428 33.358  1.00 26.34  ?  102 GLU   D OE1   1 
ATOM   3370 O OE2   . GLU   D 1 103 ? -2.096  -36.246 33.835  1.00 26.50  -1 102 GLU   D OE2   1 
ATOM   3371 N N     . GLN   D 1 104 ? -5.429  -41.984 33.343  1.00 25.14  ?  103 GLN   D N     1 
ATOM   3372 C CA    . GLN   D 1 104 ? -5.664  -43.416 33.224  1.00 26.73  ?  103 GLN   D CA    1 
ATOM   3373 C C     . GLN   D 1 104 ? -5.702  -43.847 31.749  1.00 24.61  ?  103 GLN   D C     1 
ATOM   3374 O O     . GLN   D 1 104 ? -6.129  -43.095 30.881  1.00 23.81  ?  103 GLN   D O     1 
ATOM   3375 C CB    . GLN   D 1 104 ? -7.020  -43.718 33.848  1.00 30.93  ?  103 GLN   D CB    1 
ATOM   3376 C CG    . GLN   D 1 104 ? -7.245  -45.203 34.101  1.00 34.45  ?  103 GLN   D CG    1 
ATOM   3377 C CD    . GLN   D 1 104 ? -8.614  -45.469 34.691  1.00 35.55  ?  103 GLN   D CD    1 
ATOM   3378 O OE1   . GLN   D 1 104 ? -8.918  -44.997 35.780  1.00 35.14  ?  103 GLN   D OE1   1 
ATOM   3379 N NE2   . GLN   D 1 104 ? -9.440  -46.218 33.969  1.00 36.57  ?  103 GLN   D NE2   1 
ATOM   3380 N N     . VAL   D 1 105 ? -5.241  -45.070 31.463  1.00 23.88  ?  104 VAL   D N     1 
ATOM   3381 C CA    . VAL   D 1 105 ? -5.265  -45.664 30.128  1.00 23.16  ?  104 VAL   D CA    1 
ATOM   3382 C C     . VAL   D 1 105 ? -6.288  -46.802 30.144  1.00 23.10  ?  104 VAL   D C     1 
ATOM   3383 O O     . VAL   D 1 105 ? -6.223  -47.628 31.045  1.00 23.54  ?  104 VAL   D O     1 
ATOM   3384 C CB    . VAL   D 1 105 ? -3.893  -46.148 29.659  1.00 21.47  ?  104 VAL   D CB    1 
ATOM   3385 C CG1   . VAL   D 1 105 ? -3.874  -46.298 28.144  1.00 21.47  ?  104 VAL   D CG1   1 
ATOM   3386 C CG2   . VAL   D 1 105 ? -2.781  -45.199 30.070  1.00 21.10  ?  104 VAL   D CG2   1 
ATOM   3387 N N     . ASP   D 1 106 ? -7.200  -46.827 29.162  1.00 23.33  ?  105 ASP   D N     1 
ATOM   3388 C CA    . ASP   D 1 106 ? -8.216  -47.860 29.009  1.00 25.65  ?  105 ASP   D CA    1 
ATOM   3389 C C     . ASP   D 1 106 ? -7.906  -48.694 27.761  1.00 22.48  ?  105 ASP   D C     1 
ATOM   3390 O O     . ASP   D 1 106 ? -8.032  -48.206 26.658  1.00 21.94  ?  105 ASP   D O     1 
ATOM   3391 C CB    . ASP   D 1 106 ? -9.615  -47.264 28.867  1.00 30.45  ?  105 ASP   D CB    1 
ATOM   3392 C CG    . ASP   D 1 106 ? -10.305 -46.810 30.138  1.00 38.95  ?  105 ASP   D CG    1 
ATOM   3393 O OD1   . ASP   D 1 106 ? -9.632  -46.659 31.185  1.00 42.54  ?  105 ASP   D OD1   1 
ATOM   3394 O OD2   . ASP   D 1 106 ? -11.559 -46.678 30.071  1.00 57.14  -1 105 ASP   D OD2   1 
ATOM   3395 N N     . SER   D 1 107 ? -7.598  -49.975 27.941  1.00 21.57  ?  106 SER   D N     1 
ATOM   3396 C CA    . SER   D 1 107 ? -7.215  -50.852 26.847  1.00 20.99  ?  106 SER   D CA    1 
ATOM   3397 C C     . SER   D 1 107 ? -8.097  -52.097 26.876  1.00 21.68  ?  106 SER   D C     1 
ATOM   3398 O O     . SER   D 1 107 ? -8.450  -52.574 27.960  1.00 21.56  ?  106 SER   D O     1 
ATOM   3399 C CB    . SER   D 1 107 ? -5.780  -51.225 26.897  1.00 19.17  ?  106 SER   D CB    1 
ATOM   3400 O OG    . SER   D 1 107 ? -4.952  -50.086 26.880  1.00 18.28  ?  106 SER   D OG    1 
ATOM   3401 N N     . LYS   D 1 108 ? -8.331  -52.642 25.665  1.00 21.49  ?  107 LYS   D N     1 
ATOM   3402 C CA    . LYS   D 1 108 ? -8.979  -53.927 25.475  1.00 22.58  ?  107 LYS   D CA    1 
ATOM   3403 C C     . LYS   D 1 108 ? -8.332  -54.653 24.301  1.00 21.84  ?  107 LYS   D C     1 
ATOM   3404 O O     . LYS   D 1 108 ? -7.957  -54.007 23.315  1.00 21.28  ?  107 LYS   D O     1 
ATOM   3405 C CB    . LYS   D 1 108 ? -10.479 -53.783 25.228  1.00 24.10  ?  107 LYS   D CB    1 
ATOM   3406 C CG    . LYS   D 1 108 ? -11.270 -55.090 25.359  1.00 25.74  ?  107 LYS   D CG    1 
ATOM   3407 C CD    . LYS   D 1 108 ? -12.773 -54.819 25.258  1.00 27.15  ?  107 LYS   D CD    1 
ATOM   3408 C CE    . LYS   D 1 108 ? -13.624 -56.019 25.511  1.00 28.79  ?  107 LYS   D CE    1 
ATOM   3409 N NZ    . LYS   D 1 108 ? -15.034 -55.658 25.378  1.00 30.15  1  107 LYS   D NZ    1 
ATOM   3410 N N     . ALA   D 1 109 ? -8.221  -55.984 24.437  1.00 22.87  ?  108 ALA   D N     1 
ATOM   3411 C CA    . ALA   D 1 109 ? -7.796  -56.889 23.372  1.00 23.61  ?  108 ALA   D CA    1 
ATOM   3412 C C     . ALA   D 1 109 ? -8.779  -58.059 23.296  1.00 24.23  ?  108 ALA   D C     1 
ATOM   3413 O O     . ALA   D 1 109 ? -9.118  -58.621 24.326  1.00 24.14  ?  108 ALA   D O     1 
ATOM   3414 C CB    . ALA   D 1 109 ? -6.387  -57.359 23.615  1.00 23.38  ?  108 ALA   D CB    1 
ATOM   3415 N N     . SER   D 1 110 ? -9.249  -58.366 22.086  1.00 24.56  ?  109 SER   D N     1 
ATOM   3416 C CA    . SER   D 1 110 ? -10.225 -59.426 21.819  1.00 27.49  ?  109 SER   D CA    1 
ATOM   3417 C C     . SER   D 1 110 ? -9.674  -60.234 20.644  1.00 27.87  ?  109 SER   D C     1 
ATOM   3418 O O     . SER   D 1 110 ? -9.331  -59.592 19.644  1.00 27.89  ?  109 SER   D O     1 
ATOM   3419 C CB    . SER   D 1 110 ? -11.611 -58.889 21.478  1.00 28.40  ?  109 SER   D CB    1 
ATOM   3420 O OG    . SER   D 1 110 ? -12.043 -57.894 22.402  1.00 29.38  ?  109 SER   D OG    1 
ATOM   3421 N N     . VAL   D 1 111 ? -9.588  -61.577 20.764  1.00 27.55  ?  110 VAL   D N     1 
ATOM   3422 C CA    . VAL   D 1 111 ? -9.150  -62.445 19.669  1.00 28.23  ?  110 VAL   D CA    1 
ATOM   3423 C C     . VAL   D 1 111 ? -10.228 -63.477 19.439  1.00 28.77  ?  110 VAL   D C     1 
ATOM   3424 O O     . VAL   D 1 111 ? -10.544 -64.138 20.399  1.00 30.05  ?  110 VAL   D O     1 
ATOM   3425 C CB    . VAL   D 1 111 ? -7.785  -63.131 19.909  1.00 28.31  ?  110 VAL   D CB    1 
ATOM   3426 C CG1   . VAL   D 1 111 ? -7.481  -64.227 18.888  1.00 29.26  ?  110 VAL   D CG1   1 
ATOM   3427 C CG2   . VAL   D 1 111 ? -6.673  -62.116 19.966  1.00 27.19  ?  110 VAL   D CG2   1 
ATOM   3428 N N     . THR   D 1 112 ? -10.684 -63.653 18.193  1.00 28.77  ?  111 THR   D N     1 
ATOM   3429 C CA    . THR   D 1 112 ? -11.666 -64.668 17.819  1.00 31.10  ?  111 THR   D CA    1 
ATOM   3430 C C     . THR   D 1 112 ? -11.031 -65.581 16.768  1.00 30.78  ?  111 THR   D C     1 
ATOM   3431 O O     . THR   D 1 112 ? -10.525 -65.078 15.766  1.00 29.14  ?  111 THR   D O     1 
ATOM   3432 C CB    . THR   D 1 112 ? -12.968 -64.033 17.328  1.00 32.05  ?  111 THR   D CB    1 
ATOM   3433 O OG1   . THR   D 1 112 ? -13.493 -63.380 18.475  1.00 33.48  ?  111 THR   D OG1   1 
ATOM   3434 C CG2   . THR   D 1 112 ? -14.024 -65.023 16.874  1.00 34.08  ?  111 THR   D CG2   1 
ATOM   3435 N N     . ILE   D 1 113 ? -11.036 -66.889 17.061  1.00 31.91  ?  112 ILE   D N     1 
ATOM   3436 C CA    . ILE   D 1 113 ? -10.521 -67.944 16.196  1.00 33.53  ?  112 ILE   D CA    1 
ATOM   3437 C C     . ILE   D 1 113 ? -11.731 -68.768 15.731  1.00 35.28  ?  112 ILE   D C     1 
ATOM   3438 O O     . ILE   D 1 113 ? -12.424 -69.328 16.571  1.00 35.75  ?  112 ILE   D O     1 
ATOM   3439 C CB    . ILE   D 1 113 ? -9.460  -68.813 16.911  1.00 33.94  ?  112 ILE   D CB    1 
ATOM   3440 C CG1   . ILE   D 1 113 ? -8.328  -67.936 17.556  1.00 32.71  ?  112 ILE   D CG1   1 
ATOM   3441 C CG2   . ILE   D 1 113 ? -8.893  -69.828 15.914  1.00 35.00  ?  112 ILE   D CG2   1 
ATOM   3442 C CD1   . ILE   D 1 113 ? -7.466  -68.632 18.601  1.00 33.51  ?  112 ILE   D CD1   1 
ATOM   3443 N N     . GLY   D 1 114 ? -11.986 -68.793 14.416  1.00 36.44  ?  113 GLY   D N     1 
ATOM   3444 C CA    . GLY   D 1 114 ? -13.022 -69.599 13.798  1.00 39.50  ?  113 GLY   D CA    1 
ATOM   3445 C C     . GLY   D 1 114 ? -12.352 -70.756 13.104  1.00 42.46  ?  113 GLY   D C     1 
ATOM   3446 O O     . GLY   D 1 114 ? -11.700 -70.471 12.056  1.00 44.78  ?  113 GLY   D O     1 
ATOM   3447 N N     . SER   E 2 1   ? -16.015 -68.206 17.614  1.00 44.83  ?  1   SER   E N     1 
ATOM   3448 C CA    . SER   E 2 1   ? -16.147 -69.649 17.966  1.00 47.19  ?  1   SER   E CA    1 
ATOM   3449 C C     . SER   E 2 1   ? -15.336 -70.026 19.216  1.00 44.53  ?  1   SER   E C     1 
ATOM   3450 O O     . SER   E 2 1   ? -15.858 -70.729 20.063  1.00 46.70  ?  1   SER   E O     1 
ATOM   3451 C CB    . SER   E 2 1   ? -15.799 -70.523 16.788  1.00 47.93  ?  1   SER   E CB    1 
ATOM   3452 O OG    . SER   E 2 1   ? -16.659 -71.641 16.780  1.00 50.63  ?  1   SER   E OG    1 
ATOM   3453 N N     . VAL   E 2 2   ? -14.058 -69.626 19.307  1.00 42.60  ?  2   VAL   E N     1 
ATOM   3454 C CA    . VAL   E 2 2   ? -13.363 -69.433 20.587  1.00 40.74  ?  2   VAL   E CA    1 
ATOM   3455 C C     . VAL   E 2 2   ? -12.756 -68.031 20.603  1.00 36.55  ?  2   VAL   E C     1 
ATOM   3456 O O     . VAL   E 2 2   ? -12.079 -67.641 19.646  1.00 35.26  ?  2   VAL   E O     1 
ATOM   3457 C CB    . VAL   E 2 2   ? -12.320 -70.508 20.956  1.00 42.46  ?  2   VAL   E CB    1 
ATOM   3458 C CG1   . VAL   E 2 2   ? -13.025 -71.823 21.341  1.00 45.16  ?  2   VAL   E CG1   1 
ATOM   3459 C CG2   . VAL   E 2 2   ? -11.276 -70.738 19.871  1.00 42.31  ?  2   VAL   E CG2   1 
ATOM   3460 N N     . THR   E 2 3   ? -13.039 -67.289 21.694  1.00 33.94  ?  3   THR   E N     1 
ATOM   3461 C CA    . THR   E 2 3   ? -12.662 -65.913 21.881  1.00 31.29  ?  3   THR   E CA    1 
ATOM   3462 C C     . THR   E 2 3   ? -11.845 -65.796 23.157  1.00 30.18  ?  3   THR   E C     1 
ATOM   3463 O O     . THR   E 2 3   ? -12.175 -66.435 24.148  1.00 30.40  ?  3   THR   E O     1 
ATOM   3464 C CB    . THR   E 2 3   ? -13.848 -64.967 21.968  1.00 32.58  ?  3   THR   E CB    1 
ATOM   3465 O OG1   . THR   E 2 3   ? -14.704 -65.213 20.865  1.00 34.47  ?  3   THR   E OG1   1 
ATOM   3466 C CG2   . THR   E 2 3   ? -13.479 -63.487 21.869  1.00 31.60  ?  3   THR   E CG2   1 
ATOM   3467 N N     . ILE   E 2 4   ? -10.819 -64.932 23.112  1.00 28.39  ?  4   ILE   E N     1 
ATOM   3468 C CA    . ILE   E 2 4   ? -10.097 -64.473 24.298  1.00 28.88  ?  4   ILE   E CA    1 
ATOM   3469 C C     . ILE   E 2 4   ? -10.265 -62.964 24.398  1.00 26.43  ?  4   ILE   E C     1 
ATOM   3470 O O     . ILE   E 2 4   ? -9.964  -62.295 23.425  1.00 25.96  ?  4   ILE   E O     1 
ATOM   3471 C CB    . ILE   E 2 4   ? -8.579  -64.790 24.293  1.00 29.38  ?  4   ILE   E CB    1 
ATOM   3472 C CG1   . ILE   E 2 4   ? -8.206  -66.004 23.529  1.00 31.33  ?  4   ILE   E CG1   1 
ATOM   3473 C CG2   . ILE   E 2 4   ? -8.030  -64.840 25.729  1.00 30.11  ?  4   ILE   E CG2   1 
ATOM   3474 C CD1   . ILE   E 2 4   ? -8.773  -67.320 24.040  1.00 33.98  ?  4   ILE   E CD1   1 
ATOM   3475 N N     . THR   E 2 5   ? -10.602 -62.458 25.582  1.00 25.98  ?  5   THR   E N     1 
ATOM   3476 C CA    . THR   E 2 5   ? -10.823 -61.036 25.806  1.00 26.07  ?  5   THR   E CA    1 
ATOM   3477 C C     . THR   E 2 5   ? -10.052 -60.665 27.058  1.00 25.83  ?  5   THR   E C     1 
ATOM   3478 O O     . THR   E 2 5   ? -10.181 -61.362 28.076  1.00 26.61  ?  5   THR   E O     1 
ATOM   3479 C CB    . THR   E 2 5   ? -12.302 -60.649 25.982  1.00 28.22  ?  5   THR   E CB    1 
ATOM   3480 O OG1   . THR   E 2 5   ? -12.980 -61.252 24.878  1.00 30.58  ?  5   THR   E OG1   1 
ATOM   3481 C CG2   . THR   E 2 5   ? -12.488 -59.142 26.004  1.00 26.67  ?  5   THR   E CG2   1 
ATOM   3482 N N     . ILE   E 2 6   ? -9.273  -59.583 26.946  1.00 24.72  ?  6   ILE   E N     1 
ATOM   3483 C CA    . ILE   E 2 6   ? -8.515  -59.026 28.053  1.00 25.26  ?  6   ILE   E CA    1 
ATOM   3484 C C     . ILE   E 2 6   ? -8.816  -57.531 28.081  1.00 24.44  ?  6   ILE   E C     1 
ATOM   3485 O O     . ILE   E 2 6   ? -8.557  -56.843 27.099  1.00 23.33  ?  6   ILE   E O     1 
ATOM   3486 C CB    . ILE   E 2 6   ? -7.002  -59.334 27.959  1.00 24.69  ?  6   ILE   E CB    1 
ATOM   3487 C CG1   . ILE   E 2 6   ? -6.745  -60.860 27.797  1.00 25.32  ?  6   ILE   E CG1   1 
ATOM   3488 C CG2   . ILE   E 2 6   ? -6.299  -58.758 29.198  1.00 24.09  ?  6   ILE   E CG2   1 
ATOM   3489 C CD1   . ILE   E 2 6   ? -5.330  -61.268 27.443  1.00 25.04  ?  6   ILE   E CD1   1 
ATOM   3490 N N     . ASN   E 2 7   ? -9.367  -57.060 29.207  1.00 25.66  ?  7   ASN   E N     1 
ATOM   3491 C CA    . ASN   E 2 7   ? -9.481  -55.655 29.551  1.00 25.86  ?  7   ASN   E CA    1 
ATOM   3492 C C     . ASN   E 2 7   ? -8.268  -55.285 30.403  1.00 24.57  ?  7   ASN   E C     1 
ATOM   3493 O O     . ASN   E 2 7   ? -7.814  -56.090 31.206  1.00 25.78  ?  7   ASN   E O     1 
ATOM   3494 C CB    . ASN   E 2 7   ? -10.738 -55.369 30.366  1.00 27.90  ?  7   ASN   E CB    1 
ATOM   3495 C CG    . ASN   E 2 7   ? -11.990 -55.716 29.588  1.00 31.19  ?  7   ASN   E CG    1 
ATOM   3496 O OD1   . ASN   E 2 7   ? -12.407 -54.952 28.714  1.00 31.52  ?  7   ASN   E OD1   1 
ATOM   3497 N ND2   . ASN   E 2 7   ? -12.571 -56.881 29.849  1.00 33.32  ?  7   ASN   E ND2   1 
ATOM   3498 N N     . GLN   E 2 8   ? -7.802  -54.057 30.249  1.00 23.64  ?  8   GLN   E N     1 
ATOM   3499 C CA    . GLN   E 2 8   ? -6.531  -53.615 30.830  1.00 24.41  ?  8   GLN   E CA    1 
ATOM   3500 C C     . GLN   E 2 8   ? -6.713  -52.143 31.174  1.00 24.22  ?  8   GLN   E C     1 
ATOM   3501 O O     . GLN   E 2 8   ? -7.100  -51.337 30.308  1.00 25.11  ?  8   GLN   E O     1 
ATOM   3502 C CB    . GLN   E 2 8   ? -5.308  -53.917 29.949  1.00 22.53  ?  8   GLN   E CB    1 
ATOM   3503 C CG    . GLN   E 2 8   ? -3.976  -53.401 30.511  1.00 23.60  ?  8   GLN   E CG    1 
ATOM   3504 C CD    . GLN   E 2 8   ? -2.833  -53.445 29.525  1.00 23.25  ?  8   GLN   E CD    1 
ATOM   3505 O OE1   . GLN   E 2 8   ? -2.605  -54.441 28.858  1.00 26.01  ?  8   GLN   E OE1   1 
ATOM   3506 N NE2   . GLN   E 2 8   ? -2.067  -52.383 29.406  1.00 23.84  ?  8   GLN   E NE2   1 
ATOM   3507 N N     . LYS   E 2 9   ? -6.451  -51.834 32.440  1.00 24.41  ?  9   LYS   E N     1 
ATOM   3508 C CA    . LYS   E 2 9   ? -6.472  -50.476 32.960  1.00 25.73  ?  9   LYS   E CA    1 
ATOM   3509 C C     . LYS   E 2 9   ? -5.031  -50.151 33.353  1.00 22.81  ?  9   LYS   E C     1 
ATOM   3510 O O     . LYS   E 2 9   ? -4.469  -50.902 34.145  1.00 22.45  ?  9   LYS   E O     1 
ATOM   3511 C CB    . LYS   E 2 9   ? -7.496  -50.452 34.100  1.00 27.36  ?  9   LYS   E CB    1 
ATOM   3512 C CG    . LYS   E 2 9   ? -7.456  -49.302 35.103  1.00 31.15  ?  9   LYS   E CG    1 
ATOM   3513 C CD    . LYS   E 2 9   ? -8.265  -49.594 36.384  1.00 35.05  ?  9   LYS   E CD    1 
ATOM   3514 C CE    . LYS   E 2 9   ? -9.732  -49.739 36.064  1.00 38.81  ?  9   LYS   E CE    1 
ATOM   3515 N NZ    . LYS   E 2 9   ? -10.607 -49.992 37.197  1.00 43.60  1  9   LYS   E NZ    1 
ATOM   3516 N N     . GLY   E 2 10  ? -4.475  -49.070 32.771  1.00 21.79  ?  10  GLY   E N     1 
ATOM   3517 C CA    . GLY   E 2 10  ? -3.195  -48.483 33.165  1.00 20.73  ?  10  GLY   E CA    1 
ATOM   3518 C C     . GLY   E 2 10  ? -3.424  -47.272 34.060  1.00 21.14  ?  10  GLY   E C     1 
ATOM   3519 O O     . GLY   E 2 10  ? -4.217  -46.391 33.698  1.00 21.69  ?  10  GLY   E O     1 
ATOM   3520 N N     . GLU   E 2 11  ? -2.750  -47.254 35.220  1.00 21.21  ?  11  GLU   E N     1 
ATOM   3521 C CA    . GLU   E 2 11  ? -2.798  -46.153 36.166  1.00 21.97  ?  11  GLU   E CA    1 
ATOM   3522 C C     . GLU   E 2 11  ? -1.389  -45.730 36.571  1.00 21.02  ?  11  GLU   E C     1 
ATOM   3523 O O     . GLU   E 2 11  ? -0.448  -46.512 36.440  1.00 18.95  ?  11  GLU   E O     1 
ATOM   3524 C CB    . GLU   E 2 11  ? -3.608  -46.628 37.368  1.00 23.70  ?  11  GLU   E CB    1 
ATOM   3525 C CG    . GLU   E 2 11  ? -5.081  -46.757 37.028  1.00 24.67  ?  11  GLU   E CG    1 
ATOM   3526 C CD    . GLU   E 2 11  ? -5.900  -47.161 38.218  1.00 26.99  ?  11  GLU   E CD    1 
ATOM   3527 O OE1   . GLU   E 2 11  ? -6.628  -46.280 38.750  1.00 29.63  ?  11  GLU   E OE1   1 
ATOM   3528 O OE2   . GLU   E 2 11  ? -5.863  -48.363 38.543  1.00 27.26  -1 11  GLU   E OE2   1 
ATOM   3529 N N     . ILE   E 2 12  ? -1.318  -44.530 37.176  1.00 21.97  ?  12  ILE   E N     1 
ATOM   3530 C CA    . ILE   E 2 12  ? -0.094  -44.010 37.811  1.00 22.85  ?  12  ILE   E CA    1 
ATOM   3531 C C     . ILE   E 2 12  ? -0.073  -44.548 39.231  1.00 23.90  ?  12  ILE   E C     1 
ATOM   3532 O O     . ILE   E 2 12  ? -1.084  -44.455 39.898  1.00 26.39  ?  12  ILE   E O     1 
ATOM   3533 C CB    . ILE   E 2 12  ? -0.080  -42.463 37.781  1.00 22.99  ?  12  ILE   E CB    1 
ATOM   3534 C CG1   . ILE   E 2 12  ? -0.392  -41.866 36.382  1.00 21.57  ?  12  ILE   E CG1   1 
ATOM   3535 C CG2   . ILE   E 2 12  ? 1.208   -41.885 38.366  1.00 23.93  ?  12  ILE   E CG2   1 
ATOM   3536 C CD1   . ILE   E 2 12  ? 0.504   -42.406 35.304  1.00 20.82  ?  12  ILE   E CD1   1 
ATOM   3537 N N     . THR   E 2 13  ? 1.072   -45.075 39.695  1.00 24.87  ?  13  THR   E N     1 
ATOM   3538 C CA    . THR   E 2 13  ? 1.232   -45.576 41.059  1.00 26.11  ?  13  THR   E CA    1 
ATOM   3539 C C     . THR   E 2 13  ? 1.260   -44.432 42.081  1.00 27.07  ?  13  THR   E C     1 
ATOM   3540 O O     . THR   E 2 13  ? 1.635   -43.306 41.750  1.00 25.40  ?  13  THR   E O     1 
ATOM   3541 C CB    . THR   E 2 13  ? 2.479   -46.453 41.200  1.00 26.76  ?  13  THR   E CB    1 
ATOM   3542 O OG1   . THR   E 2 13  ? 3.684   -45.704 40.985  1.00 26.64  ?  13  THR   E OG1   1 
ATOM   3543 C CG2   . THR   E 2 13  ? 2.400   -47.707 40.343  1.00 25.72  ?  13  THR   E CG2   1 
ATOM   3544 N N     . GLU   E 2 14  ? 0.884   -44.757 43.330  1.00 29.27  ?  14  GLU   E N     1 
ATOM   3545 C CA    . GLU   E 2 14  ? 1.007   -43.871 44.484  1.00 32.99  ?  14  GLU   E CA    1 
ATOM   3546 C C     . GLU   E 2 14  ? 2.445   -43.407 44.689  1.00 31.84  ?  14  GLU   E C     1 
ATOM   3547 O O     . GLU   E 2 14  ? 2.659   -42.220 44.862  1.00 32.73  ?  14  GLU   E O     1 
ATOM   3548 C CB    . GLU   E 2 14  ? 0.650   -44.562 45.800  1.00 37.81  ?  14  GLU   E CB    1 
ATOM   3549 C CG    . GLU   E 2 14  ? -0.837  -44.841 45.962  1.00 41.41  ?  14  GLU   E CG    1 
ATOM   3550 C CD    . GLU   E 2 14  ? -1.154  -45.821 47.085  1.00 47.50  ?  14  GLU   E CD    1 
ATOM   3551 O OE1   . GLU   E 2 14  ? -0.385  -45.773 48.089  1.00 49.41  ?  14  GLU   E OE1   1 
ATOM   3552 O OE2   . GLU   E 2 14  ? -2.192  -46.547 47.002  1.00 50.96  -1 14  GLU   E OE2   1 
ATOM   3553 N N     . GLU   E 2 15  ? 3.395   -44.347 44.625  1.00 31.40  ?  15  GLU   E N     1 
ATOM   3554 C CA    . GLU   E 2 15  ? 4.822   -44.099 44.764  1.00 32.30  ?  15  GLU   E CA    1 
ATOM   3555 C C     . GLU   E 2 15  ? 5.297   -43.031 43.768  1.00 28.71  ?  15  GLU   E C     1 
ATOM   3556 O O     . GLU   E 2 15  ? 6.006   -42.126 44.174  1.00 28.47  ?  15  GLU   E O     1 
ATOM   3557 C CB    . GLU   E 2 15  ? 5.662   -45.367 44.576  1.00 35.68  ?  15  GLU   E CB    1 
ATOM   3558 C CG    . GLU   E 2 15  ? 5.161   -46.598 45.347  1.00 42.06  ?  15  GLU   E CG    1 
ATOM   3559 C CD    . GLU   E 2 15  ? 4.380   -47.640 44.522  1.00 46.70  ?  15  GLU   E CD    1 
ATOM   3560 O OE1   . GLU   E 2 15  ? 3.112   -47.564 44.556  1.00 43.64  ?  15  GLU   E OE1   1 
ATOM   3561 O OE2   . GLU   E 2 15  ? 5.021   -48.496 43.814  1.00 50.06  -1 15  GLU   E OE2   1 
ATOM   3562 N N     . GLN   E 2 16  ? 4.849   -43.084 42.502  1.00 25.88  ?  16  GLN   E N     1 
ATOM   3563 C CA    . GLN   E 2 16  ? 5.177   -42.069 41.497  1.00 24.60  ?  16  GLN   E CA    1 
ATOM   3564 C C     . GLN   E 2 16  ? 4.664   -40.686 41.914  1.00 25.17  ?  16  GLN   E C     1 
ATOM   3565 O O     . GLN   E 2 16  ? 5.406   -39.703 41.824  1.00 24.77  ?  16  GLN   E O     1 
ATOM   3566 C CB    . GLN   E 2 16  ? 4.644   -42.384 40.095  1.00 22.94  ?  16  GLN   E CB    1 
ATOM   3567 C CG    . GLN   E 2 16  ? 5.399   -43.467 39.334  1.00 22.39  ?  16  GLN   E CG    1 
ATOM   3568 C CD    . GLN   E 2 16  ? 4.560   -44.017 38.203  1.00 21.22  ?  16  GLN   E CD    1 
ATOM   3569 O OE1   . GLN   E 2 16  ? 3.686   -44.849 38.424  1.00 21.49  ?  16  GLN   E OE1   1 
ATOM   3570 N NE2   . GLN   E 2 16  ? 4.773   -43.532 36.998  1.00 21.13  ?  16  GLN   E NE2   1 
ATOM   3571 N N     . LYS   E 2 17  ? 3.430   -40.637 42.424  1.00 25.90  ?  17  LYS   E N     1 
ATOM   3572 C CA    . LYS   E 2 17  ? 2.813   -39.395 42.869  1.00 27.34  ?  17  LYS   E CA    1 
ATOM   3573 C C     . LYS   E 2 17  ? 3.491   -38.841 44.129  1.00 28.55  ?  17  LYS   E C     1 
ATOM   3574 O O     . LYS   E 2 17  ? 3.715   -37.632 44.206  1.00 28.54  ?  17  LYS   E O     1 
ATOM   3575 C CB    . LYS   E 2 17  ? 1.309   -39.576 43.063  1.00 28.49  ?  17  LYS   E CB    1 
ATOM   3576 C CG    . LYS   E 2 17  ? 0.590   -39.918 41.742  1.00 28.42  ?  17  LYS   E CG    1 
ATOM   3577 C CD    . LYS   E 2 17  ? -0.896  -40.152 41.957  1.00 31.42  ?  17  LYS   E CD    1 
ATOM   3578 C CE    . LYS   E 2 17  ? -1.489  -41.029 40.932  1.00 32.56  ?  17  LYS   E CE    1 
ATOM   3579 N NZ    . LYS   E 2 17  ? -2.961  -41.021 40.903  1.00 36.61  1  17  LYS   E NZ    1 
ATOM   3580 N N     . GLN   E 2 18  ? 3.822   -39.715 45.099  1.00 28.96  ?  18  GLN   E N     1 
ATOM   3581 C CA    . GLN   E 2 18  ? 4.566   -39.333 46.292  1.00 29.59  ?  18  GLN   E CA    1 
ATOM   3582 C C     . GLN   E 2 18  ? 5.902   -38.699 45.902  1.00 29.13  ?  18  GLN   E C     1 
ATOM   3583 O O     . GLN   E 2 18  ? 6.205   -37.598 46.362  1.00 29.56  ?  18  GLN   E O     1 
ATOM   3584 C CB    . GLN   E 2 18  ? 4.869   -40.495 47.239  1.00 30.44  ?  18  GLN   E CB    1 
ATOM   3585 C CG    . GLN   E 2 18  ? 3.656   -41.226 47.813  1.00 31.39  ?  18  GLN   E CG    1 
ATOM   3586 C CD    . GLN   E 2 18  ? 2.719   -40.393 48.662  1.00 33.23  ?  18  GLN   E CD    1 
ATOM   3587 O OE1   . GLN   E 2 18  ? 3.051   -39.287 49.075  1.00 33.19  ?  18  GLN   E OE1   1 
ATOM   3588 N NE2   . GLN   E 2 18  ? 1.585   -40.975 49.041  1.00 34.66  ?  18  GLN   E NE2   1 
ATOM   3589 N N     . ARG   E 2 19  ? 6.621   -39.353 44.974  1.00 28.33  ?  19  ARG   E N     1 
ATOM   3590 C CA    . ARG   E 2 19  ? 7.898   -38.861 44.471  1.00 28.68  ?  19  ARG   E CA    1 
ATOM   3591 C C     . ARG   E 2 19  ? 7.766   -37.472 43.827  1.00 28.54  ?  19  ARG   E C     1 
ATOM   3592 O O     . ARG   E 2 19  ? 8.568   -36.590 44.130  1.00 28.61  ?  19  ARG   E O     1 
ATOM   3593 C CB    . ARG   E 2 19  ? 8.476   -39.901 43.500  1.00 28.71  ?  19  ARG   E CB    1 
ATOM   3594 C CG    . ARG   E 2 19  ? 9.934   -39.648 43.147  1.00 29.60  ?  19  ARG   E CG    1 
ATOM   3595 C CD    . ARG   E 2 19  ? 10.327  -40.395 41.925  1.00 29.33  ?  19  ARG   E CD    1 
ATOM   3596 N NE    . ARG   E 2 19  ? 11.714  -40.089 41.578  1.00 31.23  ?  19  ARG   E NE    1 
ATOM   3597 C CZ    . ARG   E 2 19  ? 12.334  -40.567 40.510  1.00 32.38  ?  19  ARG   E CZ    1 
ATOM   3598 N NH1   . ARG   E 2 19  ? 11.781  -41.528 39.769  1.00 30.49  1  19  ARG   E NH1   1 
ATOM   3599 N NH2   . ARG   E 2 19  ? 13.534  -40.088 40.208  1.00 33.97  ?  19  ARG   E NH2   1 
ATOM   3600 N N     . ALA   E 2 20  ? 6.723   -37.265 42.989  1.00 27.33  ?  20  ALA   E N     1 
ATOM   3601 C CA    . ALA   E 2 20  ? 6.496   -35.996 42.309  1.00 27.62  ?  20  ALA   E CA    1 
ATOM   3602 C C     . ALA   E 2 20  ? 6.155   -34.862 43.294  1.00 29.34  ?  20  ALA   E C     1 
ATOM   3603 O O     . ALA   E 2 20  ? 6.535   -33.728 43.037  1.00 28.42  ?  20  ALA   E O     1 
ATOM   3604 C CB    . ALA   E 2 20  ? 5.468   -36.124 41.192  1.00 26.01  ?  20  ALA   E CB    1 
ATOM   3605 N N     . GLN   E 2 21  ? 5.539   -35.181 44.440  1.00 32.18  ?  21  GLN   E N     1 
ATOM   3606 C CA    . GLN   E 2 21  ? 5.285   -34.179 45.474  1.00 35.65  ?  21  GLN   E CA    1 
ATOM   3607 C C     . GLN   E 2 21  ? 6.518   -33.858 46.326  1.00 37.89  ?  21  GLN   E C     1 
ATOM   3608 O O     . GLN   E 2 21  ? 6.532   -32.780 46.916  1.00 38.88  ?  21  GLN   E O     1 
ATOM   3609 C CB    . GLN   E 2 21  ? 4.030   -34.517 46.287  1.00 38.05  ?  21  GLN   E CB    1 
ATOM   3610 C CG    . GLN   E 2 21  ? 2.749   -34.642 45.452  1.00 39.06  ?  21  GLN   E CG    1 
ATOM   3611 C CD    . GLN   E 2 21  ? 2.273   -33.353 44.818  1.00 40.95  ?  21  GLN   E CD    1 
ATOM   3612 O OE1   . GLN   E 2 21  ? 2.536   -33.087 43.645  1.00 39.88  ?  21  GLN   E OE1   1 
ATOM   3613 N NE2   . GLN   E 2 21  ? 1.591   -32.527 45.594  1.00 43.84  ?  21  GLN   E NE2   1 
ATOM   3614 N N     . GLY   E 2 22  ? 7.537   -34.739 46.383  1.00 37.86  ?  22  GLY   E N     1 
ATOM   3615 C CA    . GLY   E 2 22  ? 8.758   -34.498 47.139  1.00 38.92  ?  22  GLY   E CA    1 
ATOM   3616 C C     . GLY   E 2 22  ? 9.775   -33.633 46.387  1.00 40.00  ?  22  GLY   E C     1 
ATOM   3617 O O     . GLY   E 2 22  ? 9.492   -33.078 45.317  1.00 39.49  ?  22  GLY   E O     1 
ATOM   3618 N N     . ASP   E 2 23  ? 10.992  -33.587 46.952  1.00 42.09  ?  23  ASP   E N     1 
ATOM   3619 C CA    . ASP   E 2 23  ? 12.075  -32.671 46.606  1.00 45.20  ?  23  ASP   E CA    1 
ATOM   3620 C C     . ASP   E 2 23  ? 13.293  -33.397 46.024  1.00 44.47  ?  23  ASP   E C     1 
ATOM   3621 O O     . ASP   E 2 23  ? 14.281  -32.735 45.747  1.00 48.03  ?  23  ASP   E O     1 
ATOM   3622 C CB    . ASP   E 2 23  ? 12.517  -31.906 47.862  1.00 51.56  ?  23  ASP   E CB    1 
ATOM   3623 C CG    . ASP   E 2 23  ? 11.651  -30.754 48.363  1.00 58.41  ?  23  ASP   E CG    1 
ATOM   3624 O OD1   . ASP   E 2 23  ? 10.561  -30.512 47.792  1.00 65.57  ?  23  ASP   E OD1   1 
ATOM   3625 O OD2   . ASP   E 2 23  ? 12.092  -30.066 49.314  1.00 59.70  -1 23  ASP   E OD2   1 
ATOM   3626 N N     . ASP   E 2 24  ? 13.275  -34.729 45.835  1.00 45.13  ?  24  ASP   E N     1 
ATOM   3627 C CA    . ASP   E 2 24  ? 14.413  -35.465 45.281  1.00 46.51  ?  24  ASP   E CA    1 
ATOM   3628 C C     . ASP   E 2 24  ? 14.468  -35.269 43.759  1.00 42.85  ?  24  ASP   E C     1 
ATOM   3629 O O     . ASP   E 2 24  ? 13.568  -34.659 43.176  1.00 41.05  ?  24  ASP   E O     1 
ATOM   3630 C CB    . ASP   E 2 24  ? 14.384  -36.926 45.734  1.00 47.95  ?  24  ASP   E CB    1 
ATOM   3631 C CG    . ASP   E 2 24  ? 14.676  -37.220 47.206  1.00 50.93  ?  24  ASP   E CG    1 
ATOM   3632 O OD1   . ASP   E 2 24  ? 14.917  -36.274 48.022  1.00 51.64  ?  24  ASP   E OD1   1 
ATOM   3633 O OD2   . ASP   E 2 24  ? 14.700  -38.432 47.521  1.00 52.81  -1 24  ASP   E OD2   1 
ATOM   3634 N N     . TRP   E 2 25  ? 15.542  -35.778 43.136  1.00 41.33  ?  25  TRP   E N     1 
ATOM   3635 C CA    . TRP   E 2 25  ? 15.810  -35.574 41.720  1.00 40.47  ?  25  TRP   E CA    1 
ATOM   3636 C C     . TRP   E 2 25  ? 14.710  -36.248 40.898  1.00 37.30  ?  25  TRP   E C     1 
ATOM   3637 O O     . TRP   E 2 25  ? 14.452  -37.410 41.170  1.00 37.43  ?  25  TRP   E O     1 
ATOM   3638 C CB    . TRP   E 2 25  ? 17.185  -36.149 41.298  1.00 42.05  ?  25  TRP   E CB    1 
ATOM   3639 C CG    . TRP   E 2 25  ? 17.394  -36.085 39.804  1.00 43.18  ?  25  TRP   E CG    1 
ATOM   3640 C CD1   . TRP   E 2 25  ? 17.112  -37.071 38.894  1.00 41.62  ?  25  TRP   E CD1   1 
ATOM   3641 C CD2   . TRP   E 2 25  ? 17.781  -34.928 39.035  1.00 43.38  ?  25  TRP   E CD2   1 
ATOM   3642 N NE1   . TRP   E 2 25  ? 17.313  -36.618 37.619  1.00 42.96  ?  25  TRP   E NE1   1 
ATOM   3643 C CE2   . TRP   E 2 25  ? 17.732  -35.312 37.673  1.00 44.19  ?  25  TRP   E CE2   1 
ATOM   3644 C CE3   . TRP   E 2 25  ? 18.163  -33.615 39.356  1.00 47.98  ?  25  TRP   E CE3   1 
ATOM   3645 C CZ2   . TRP   E 2 25  ? 18.077  -34.434 36.643  1.00 48.15  ?  25  TRP   E CZ2   1 
ATOM   3646 C CZ3   . TRP   E 2 25  ? 18.534  -32.752 38.338  1.00 50.29  ?  25  TRP   E CZ3   1 
ATOM   3647 C CH2   . TRP   E 2 25  ? 18.484  -33.158 36.995  1.00 50.02  ?  25  TRP   E CH2   1 
ATOM   3648 N N     . PRO   E 2 26  ? 14.101  -35.659 39.837  1.00 35.87  ?  26  PRO   E N     1 
ATOM   3649 C CA    . PRO   E 2 26  ? 14.302  -34.281 39.376  1.00 37.05  ?  26  PRO   E CA    1 
ATOM   3650 C C     . PRO   E 2 26  ? 13.305  -33.222 39.890  1.00 36.58  ?  26  PRO   E C     1 
ATOM   3651 O O     . PRO   E 2 26  ? 13.321  -32.090 39.389  1.00 34.77  ?  26  PRO   E O     1 
ATOM   3652 C CB    . PRO   E 2 26  ? 14.150  -34.479 37.861  1.00 37.13  ?  26  PRO   E CB    1 
ATOM   3653 C CG    . PRO   E 2 26  ? 12.973  -35.432 37.791  1.00 34.74  ?  26  PRO   E CG    1 
ATOM   3654 C CD    . PRO   E 2 26  ? 13.164  -36.378 38.948  1.00 35.21  ?  26  PRO   E CD    1 
ATOM   3655 N N     . TYR   E 2 27  ? 12.450  -33.573 40.879  1.00 35.30  ?  27  TYR   E N     1 
ATOM   3656 C CA    . TYR   E 2 27  ? 11.302  -32.760 41.276  1.00 35.27  ?  27  TYR   E CA    1 
ATOM   3657 C C     . TYR   E 2 27  ? 11.769  -31.535 42.071  1.00 38.44  ?  27  TYR   E C     1 
ATOM   3658 O O     . TYR   E 2 27  ? 11.199  -30.472 41.898  1.00 41.63  ?  27  TYR   E O     1 
ATOM   3659 C CB    . TYR   E 2 27  ? 10.254  -33.642 41.968  1.00 32.97  ?  27  TYR   E CB    1 
ATOM   3660 C CG    . TYR   E 2 27  ? 9.703   -34.716 41.038  1.00 29.87  ?  27  TYR   E CG    1 
ATOM   3661 C CD1   . TYR   E 2 27  ? 8.836   -34.394 39.997  1.00 27.81  ?  27  TYR   E CD1   1 
ATOM   3662 C CD2   . TYR   E 2 27  ? 10.090  -36.062 41.172  1.00 29.47  ?  27  TYR   E CD2   1 
ATOM   3663 C CE1   . TYR   E 2 27  ? 8.373   -35.359 39.105  1.00 26.38  ?  27  TYR   E CE1   1 
ATOM   3664 C CE2   . TYR   E 2 27  ? 9.626   -37.043 40.286  1.00 27.40  ?  27  TYR   E CE2   1 
ATOM   3665 C CZ    . TYR   E 2 27  ? 8.765   -36.693 39.251  1.00 26.04  ?  27  TYR   E CZ    1 
ATOM   3666 O OH    . TYR   E 2 27  ? 8.285   -37.650 38.408  1.00 24.27  ?  27  TYR   E OH    1 
ATOM   3667 N N     . GLY   E 2 28  ? 12.832  -31.659 42.877  1.00 40.24  ?  28  GLY   E N     1 
ATOM   3668 C CA    . GLY   E 2 28  ? 13.464  -30.530 43.537  1.00 41.30  ?  28  GLY   E CA    1 
ATOM   3669 C C     . GLY   E 2 28  ? 13.980  -29.478 42.566  1.00 41.73  ?  28  GLY   E C     1 
ATOM   3670 O O     . GLY   E 2 28  ? 13.634  -28.305 42.709  1.00 42.86  ?  28  GLY   E O     1 
ATOM   3671 N N     . GLN   E 2 29  ? 14.789  -29.904 41.584  1.00 41.12  ?  29  GLN   E N     1 
ATOM   3672 C CA    . GLN   E 2 29  ? 15.331  -28.990 40.587  1.00 42.45  ?  29  GLN   E CA    1 
ATOM   3673 C C     . GLN   E 2 29  ? 14.192  -28.301 39.825  1.00 42.51  ?  29  GLN   E C     1 
ATOM   3674 O O     . GLN   E 2 29  ? 14.287  -27.104 39.584  1.00 45.64  ?  29  GLN   E O     1 
ATOM   3675 C CB    . GLN   E 2 29  ? 16.329  -29.670 39.645  1.00 43.53  ?  29  GLN   E CB    1 
ATOM   3676 C CG    . GLN   E 2 29  ? 17.005  -28.758 38.615  1.00 45.73  ?  29  GLN   E CG    1 
ATOM   3677 C CD    . GLN   E 2 29  ? 17.889  -27.693 39.252  1.00 48.89  ?  29  GLN   E CD    1 
ATOM   3678 O OE1   . GLN   E 2 29  ? 18.796  -28.020 40.036  1.00 49.42  ?  29  GLN   E OE1   1 
ATOM   3679 N NE2   . GLN   E 2 29  ? 17.635  -26.419 38.965  1.00 49.16  ?  29  GLN   E NE2   1 
ATOM   3680 N N     . CYS   E 2 30  ? 13.102  -29.031 39.509  1.00 41.33  ?  30  CYS   E N     1 
ATOM   3681 C CA    . CYS   E 2 30  ? 11.925  -28.459 38.852  1.00 39.90  ?  30  CYS   E CA    1 
ATOM   3682 C C     . CYS   E 2 30  ? 11.332  -27.326 39.690  1.00 41.23  ?  30  CYS   E C     1 
ATOM   3683 O O     . CYS   E 2 30  ? 11.146  -26.229 39.178  1.00 41.62  ?  30  CYS   E O     1 
ATOM   3684 C CB    . CYS   E 2 30  ? 10.875  -29.523 38.497  1.00 36.02  ?  30  CYS   E CB    1 
ATOM   3685 S SG    . CYS   E 2 30  ? 9.450   -28.846 37.589  1.00 35.18  ?  30  CYS   E SG    1 
ATOM   3686 N N     . LYS   E 2 31  ? 11.098  -27.590 40.988  1.00 44.31  ?  31  LYS   E N     1 
ATOM   3687 C CA    . LYS   E 2 31  ? 10.629  -26.585 41.955  1.00 47.09  ?  31  LYS   E CA    1 
ATOM   3688 C C     . LYS   E 2 31  ? 11.545  -25.354 42.013  1.00 46.14  ?  31  LYS   E C     1 
ATOM   3689 O O     . LYS   E 2 31  ? 11.034  -24.257 42.067  1.00 46.35  ?  31  LYS   E O     1 
ATOM   3690 C CB    . LYS   E 2 31  ? 10.327  -27.255 43.310  1.00 49.05  ?  31  LYS   E CB    1 
ATOM   3691 C CG    . LYS   E 2 31  ? 9.074   -28.131 43.240  1.00 50.34  ?  31  LYS   E CG    1 
ATOM   3692 C CD    . LYS   E 2 31  ? 8.796   -29.199 44.304  1.00 52.61  ?  31  LYS   E CD    1 
ATOM   3693 C CE    . LYS   E 2 31  ? 7.961   -30.338 43.741  1.00 52.54  ?  31  LYS   E CE    1 
ATOM   3694 N NZ    . LYS   E 2 31  ? 7.212   -31.131 44.710  1.00 54.02  1  31  LYS   E NZ    1 
ATOM   3695 N N     . GLU   E 2 32  ? 12.869  -25.539 41.949  1.00 46.45  ?  32  GLU   E N     1 
ATOM   3696 C CA    . GLU   E 2 32  ? 13.840  -24.443 41.868  1.00 51.27  ?  32  GLU   E CA    1 
ATOM   3697 C C     . GLU   E 2 32  ? 13.688  -23.655 40.559  1.00 49.34  ?  32  GLU   E C     1 
ATOM   3698 O O     . GLU   E 2 32  ? 13.705  -22.428 40.585  1.00 51.44  ?  32  GLU   E O     1 
ATOM   3699 C CB    . GLU   E 2 32  ? 15.288  -24.944 42.004  1.00 54.06  ?  32  GLU   E CB    1 
ATOM   3700 C CG    . GLU   E 2 32  ? 16.256  -23.896 42.547  1.00 62.39  ?  32  GLU   E CG    1 
ATOM   3701 C CD    . GLU   E 2 32  ? 16.022  -23.463 43.992  1.00 64.85  ?  32  GLU   E CD    1 
ATOM   3702 O OE1   . GLU   E 2 32  ? 15.235  -24.127 44.743  1.00 66.14  ?  32  GLU   E OE1   1 
ATOM   3703 O OE2   . GLU   E 2 32  ? 16.615  -22.413 44.333  1.00 66.98  -1 32  GLU   E OE2   1 
ATOM   3704 N N     . ASP   E 2 33  ? 13.517  -24.370 39.432  1.00 46.12  ?  33  ASP   E N     1 
ATOM   3705 C CA    . ASP   E 2 33  ? 13.276  -23.763 38.133  1.00 46.71  ?  33  ASP   E CA    1 
ATOM   3706 C C     . ASP   E 2 33  ? 12.000  -22.904 38.138  1.00 48.65  ?  33  ASP   E C     1 
ATOM   3707 O O     . ASP   E 2 33  ? 12.013  -21.829 37.537  1.00 48.57  ?  33  ASP   E O     1 
ATOM   3708 C CB    . ASP   E 2 33  ? 13.330  -24.797 37.018  1.00 45.04  ?  33  ASP   E CB    1 
ATOM   3709 C CG    . ASP   E 2 33  ? 14.647  -25.552 36.821  1.00 45.77  ?  33  ASP   E CG    1 
ATOM   3710 O OD1   . ASP   E 2 33  ? 15.712  -25.106 37.303  1.00 46.09  ?  33  ASP   E OD1   1 
ATOM   3711 O OD2   . ASP   E 2 33  ? 14.605  -26.637 36.199  1.00 46.15  -1 33  ASP   E OD2   1 
ATOM   3712 N N     . GLN   E 2 34  ? 10.946  -23.320 38.872  1.00 49.17  ?  34  GLN   E N     1 
ATOM   3713 C CA    . GLN   E 2 34  ? 9.687   -22.577 38.957  1.00 51.07  ?  34  GLN   E CA    1 
ATOM   3714 C C     . GLN   E 2 34  ? 9.790   -21.209 39.634  1.00 55.65  ?  34  GLN   E C     1 
ATOM   3715 O O     . GLN   E 2 34  ? 8.868   -20.425 39.448  1.00 58.24  ?  34  GLN   E O     1 
ATOM   3716 C CB    . GLN   E 2 34  ? 8.623   -23.390 39.697  1.00 51.07  ?  34  GLN   E CB    1 
ATOM   3717 C CG    . GLN   E 2 34  ? 8.108   -24.571 38.892  1.00 49.36  ?  34  GLN   E CG    1 
ATOM   3718 C CD    . GLN   E 2 34  ? 7.321   -25.532 39.739  1.00 50.11  ?  34  GLN   E CD    1 
ATOM   3719 O OE1   . GLN   E 2 34  ? 6.257   -25.193 40.260  1.00 52.41  ?  34  GLN   E OE1   1 
ATOM   3720 N NE2   . GLN   E 2 34  ? 7.831   -26.740 39.886  1.00 50.52  ?  34  GLN   E NE2   1 
ATOM   3721 N N     . LYS   E 2 35  ? 10.834  -20.945 40.447  1.00 58.12  ?  35  LYS   E N     1 
ATOM   3722 C CA    . LYS   E 2 35  ? 11.095  -19.625 41.036  1.00 61.48  ?  35  LYS   E CA    1 
ATOM   3723 C C     . LYS   E 2 35  ? 12.008  -18.739 40.173  1.00 62.78  ?  35  LYS   E C     1 
ATOM   3724 O O     . LYS   E 2 35  ? 12.024  -17.535 40.406  1.00 67.69  ?  35  LYS   E O     1 
ATOM   3725 C CB    . LYS   E 2 35  ? 11.540  -19.704 42.505  1.00 62.97  ?  35  LYS   E CB    1 
ATOM   3726 C CG    . LYS   E 2 35  ? 12.657  -20.656 42.903  1.00 62.76  ?  35  LYS   E CG    1 
ATOM   3727 C CD    . LYS   E 2 35  ? 13.018  -20.702 44.389  1.00 63.78  ?  35  LYS   E CD    1 
ATOM   3728 C CE    . LYS   E 2 35  ? 12.502  -21.890 45.175  1.00 61.17  ?  35  LYS   E CE    1 
ATOM   3729 N NZ    . LYS   E 2 35  ? 11.114  -21.698 45.586  1.00 62.39  1  35  LYS   E NZ    1 
ATOM   3730 N N     . LYS   E 2 36  ? 12.752  -19.283 39.187  1.00 61.73  ?  36  LYS   E N     1 
ATOM   3731 C CA    . LYS   E 2 36  ? 13.602  -18.498 38.293  1.00 63.10  ?  36  LYS   E CA    1 
ATOM   3732 C C     . LYS   E 2 36  ? 12.774  -17.534 37.430  1.00 65.01  ?  36  LYS   E C     1 
ATOM   3733 O O     . LYS   E 2 36  ? 11.642  -17.860 37.056  1.00 64.33  ?  36  LYS   E O     1 
ATOM   3734 C CB    . LYS   E 2 36  ? 14.447  -19.389 37.375  1.00 60.68  ?  36  LYS   E CB    1 
ATOM   3735 C CG    . LYS   E 2 36  ? 15.497  -20.260 38.037  1.00 59.35  ?  36  LYS   E CG    1 
ATOM   3736 C CD    . LYS   E 2 36  ? 16.166  -21.179 37.026  1.00 59.01  ?  36  LYS   E CD    1 
ATOM   3737 C CE    . LYS   E 2 36  ? 17.264  -22.013 37.589  1.00 58.65  ?  36  LYS   E CE    1 
ATOM   3738 N NZ    . LYS   E 2 36  ? 17.639  -23.079 36.658  1.00 56.89  1  36  LYS   E NZ    1 
ATOM   3739 N N     . SER   E 2 37  ? 13.357  -16.347 37.147  1.00 66.00  ?  37  SER   E N     1 
ATOM   3740 C CA    . SER   E 2 37  ? 12.618  -15.209 36.613  1.00 68.14  ?  37  SER   E CA    1 
ATOM   3741 C C     . SER   E 2 37  ? 12.082  -15.476 35.203  1.00 67.27  ?  37  SER   E C     1 
ATOM   3742 O O     . SER   E 2 37  ? 10.948  -15.103 34.918  1.00 67.90  ?  37  SER   E O     1 
ATOM   3743 C CB    . SER   E 2 37  ? 13.417  -13.897 36.686  1.00 71.20  ?  37  SER   E CB    1 
ATOM   3744 O OG    . SER   E 2 37  ? 14.706  -13.974 36.090  1.00 71.07  ?  37  SER   E OG    1 
ATOM   3745 N N     . GLU   E 2 38  ? 12.858  -16.174 34.358  1.00 66.86  ?  38  GLU   E N     1 
ATOM   3746 C CA    . GLU   E 2 38  ? 12.419  -16.636 33.038  1.00 66.62  ?  38  GLU   E CA    1 
ATOM   3747 C C     . GLU   E 2 38  ? 11.167  -17.534 33.049  1.00 63.01  ?  38  GLU   E C     1 
ATOM   3748 O O     . GLU   E 2 38  ? 10.478  -17.542 32.036  1.00 65.03  ?  38  GLU   E O     1 
ATOM   3749 C CB    . GLU   E 2 38  ? 13.567  -17.320 32.280  1.00 66.36  ?  38  GLU   E CB    1 
ATOM   3750 C CG    . GLU   E 2 38  ? 14.008  -18.649 32.883  1.00 63.04  ?  38  GLU   E CG    1 
ATOM   3751 C CD    . GLU   E 2 38  ? 15.418  -19.092 32.533  1.00 64.67  ?  38  GLU   E CD    1 
ATOM   3752 O OE1   . GLU   E 2 38  ? 15.668  -19.416 31.360  1.00 65.48  ?  38  GLU   E OE1   1 
ATOM   3753 O OE2   . GLU   E 2 38  ? 16.273  -19.121 33.453  1.00 67.17  -1 38  GLU   E OE2   1 
ATOM   3754 N N     . TRP   E 2 39  ? 10.865  -18.265 34.143  1.00 59.11  ?  39  TRP   E N     1 
ATOM   3755 C CA    . TRP   E 2 39  ? 9.734   -19.204 34.218  1.00 56.29  ?  39  TRP   E CA    1 
ATOM   3756 C C     . TRP   E 2 39  ? 8.597   -18.733 35.134  1.00 57.69  ?  39  TRP   E C     1 
ATOM   3757 O O     . TRP   E 2 39  ? 7.442   -19.067 34.843  1.00 57.19  ?  39  TRP   E O     1 
ATOM   3758 C CB    . TRP   E 2 39  ? 10.194  -20.610 34.652  1.00 50.50  ?  39  TRP   E CB    1 
ATOM   3759 C CG    . TRP   E 2 39  ? 11.366  -21.168 33.889  1.00 48.02  ?  39  TRP   E CG    1 
ATOM   3760 C CD1   . TRP   E 2 39  ? 12.603  -21.441 34.392  1.00 47.40  ?  39  TRP   E CD1   1 
ATOM   3761 C CD2   . TRP   E 2 39  ? 11.434  -21.509 32.490  1.00 47.43  ?  39  TRP   E CD2   1 
ATOM   3762 N NE1   . TRP   E 2 39  ? 13.429  -21.953 33.429  1.00 46.74  ?  39  TRP   E NE1   1 
ATOM   3763 C CE2   . TRP   E 2 39  ? 12.750  -21.993 32.247  1.00 47.17  ?  39  TRP   E CE2   1 
ATOM   3764 C CE3   . TRP   E 2 39  ? 10.525  -21.465 31.418  1.00 47.55  ?  39  TRP   E CE3   1 
ATOM   3765 C CZ2   . TRP   E 2 39  ? 13.176  -22.408 30.978  1.00 47.73  ?  39  TRP   E CZ2   1 
ATOM   3766 C CZ3   . TRP   E 2 39  ? 10.946  -21.871 30.167  1.00 47.63  ?  39  TRP   E CZ3   1 
ATOM   3767 C CH2   . TRP   E 2 39  ? 12.248  -22.357 29.953  1.00 47.74  ?  39  TRP   E CH2   1 
ATOM   3768 N N     . LYS   E 2 40  ? 8.903   -17.997 36.221  1.00 59.41  ?  40  LYS   E N     1 
ATOM   3769 C CA    . LYS   E 2 40  ? 8.017   -17.897 37.379  1.00 60.14  ?  40  LYS   E CA    1 
ATOM   3770 C C     . LYS   E 2 40  ? 6.650   -17.278 37.062  1.00 63.31  ?  40  LYS   E C     1 
ATOM   3771 O O     . LYS   E 2 40  ? 5.670   -17.681 37.680  1.00 62.63  ?  40  LYS   E O     1 
ATOM   3772 C CB    . LYS   E 2 40  ? 8.676   -17.205 38.584  1.00 60.51  ?  40  LYS   E CB    1 
ATOM   3773 N N     . ASP   E 2 41  ? 6.558   -16.346 36.093  1.00 69.55  ?  41  ASP   E N     1 
ATOM   3774 C CA    . ASP   E 2 41  ? 5.317   -15.620 35.830  1.00 74.59  ?  41  ASP   E CA    1 
ATOM   3775 C C     . ASP   E 2 41  ? 4.280   -16.421 35.027  1.00 73.59  ?  41  ASP   E C     1 
ATOM   3776 O O     . ASP   E 2 41  ? 3.121   -16.001 35.003  1.00 76.23  ?  41  ASP   E O     1 
ATOM   3777 C CB    . ASP   E 2 41  ? 5.586   -14.253 35.215  1.00 80.84  ?  41  ASP   E CB    1 
ATOM   3778 C CG    . ASP   E 2 41  ? 4.462   -13.236 35.373  1.00 84.63  ?  41  ASP   E CG    1 
ATOM   3779 O OD1   . ASP   E 2 41  ? 4.271   -12.783 36.513  1.00 87.11  ?  41  ASP   E OD1   1 
ATOM   3780 O OD2   . ASP   E 2 41  ? 3.747   -12.965 34.370  1.00 85.58  ?  41  ASP   E OD2   1 
ATOM   3781 N N     . SER   E 2 42  ? 4.639   -17.575 34.419  1.00 72.51  ?  42  SER   E N     1 
ATOM   3782 C CA    . SER   E 2 42  ? 3.781   -18.243 33.441  1.00 68.97  ?  42  SER   E CA    1 
ATOM   3783 C C     . SER   E 2 42  ? 2.850   -19.266 34.095  1.00 64.64  ?  42  SER   E C     1 
ATOM   3784 O O     . SER   E 2 42  ? 3.114   -19.742 35.199  1.00 60.12  ?  42  SER   E O     1 
ATOM   3785 C CB    . SER   E 2 42  ? 4.591   -18.854 32.346  1.00 68.83  ?  42  SER   E CB    1 
ATOM   3786 O OG    . SER   E 2 42  ? 5.229   -20.061 32.721  1.00 68.09  ?  42  SER   E OG    1 
ATOM   3787 N N     . ASP   E 2 43  ? 1.768   -19.585 33.373  1.00 63.38  ?  43  ASP   E N     1 
ATOM   3788 C CA    . ASP   E 2 43  ? 0.902   -20.716 33.677  1.00 62.73  ?  43  ASP   E CA    1 
ATOM   3789 C C     . ASP   E 2 43  ? 1.574   -22.090 33.456  1.00 56.25  ?  43  ASP   E C     1 
ATOM   3790 O O     . ASP   E 2 43  ? 1.105   -23.060 34.040  1.00 52.79  ?  43  ASP   E O     1 
ATOM   3791 C CB    . ASP   E 2 43  ? -0.413  -20.637 32.900  1.00 66.66  ?  43  ASP   E CB    1 
ATOM   3792 C CG    . ASP   E 2 43  ? -1.509  -19.819 33.562  1.00 71.56  ?  43  ASP   E CG    1 
ATOM   3793 O OD1   . ASP   E 2 43  ? -1.173  -18.767 34.127  1.00 74.29  ?  43  ASP   E OD1   1 
ATOM   3794 O OD2   . ASP   E 2 43  ? -2.686  -20.256 33.501  1.00 75.03  -1 43  ASP   E OD2   1 
ATOM   3795 N N     . PHE   E 2 44  ? 2.606   -22.186 32.595  1.00 52.59  ?  44  PHE   E N     1 
ATOM   3796 C CA    . PHE   E 2 44  ? 3.243   -23.447 32.231  1.00 47.89  ?  44  PHE   E CA    1 
ATOM   3797 C C     . PHE   E 2 44  ? 4.425   -23.647 33.167  1.00 46.23  ?  44  PHE   E C     1 
ATOM   3798 O O     . PHE   E 2 44  ? 5.067   -22.671 33.520  1.00 47.69  ?  44  PHE   E O     1 
ATOM   3799 C CB    . PHE   E 2 44  ? 3.721   -23.450 30.771  1.00 46.85  ?  44  PHE   E CB    1 
ATOM   3800 C CG    . PHE   E 2 44  ? 2.597   -23.469 29.739  1.00 47.13  ?  44  PHE   E CG    1 
ATOM   3801 C CD1   . PHE   E 2 44  ? 1.705   -22.383 29.606  1.00 50.74  ?  44  PHE   E CD1   1 
ATOM   3802 C CD2   . PHE   E 2 44  ? 2.467   -24.533 28.846  1.00 44.67  ?  44  PHE   E CD2   1 
ATOM   3803 C CE1   . PHE   E 2 44  ? 0.682   -22.400 28.657  1.00 51.55  ?  44  PHE   E CE1   1 
ATOM   3804 C CE2   . PHE   E 2 44  ? 1.435   -24.562 27.913  1.00 46.12  ?  44  PHE   E CE2   1 
ATOM   3805 C CZ    . PHE   E 2 44  ? 0.556   -23.478 27.794  1.00 49.95  ?  44  PHE   E CZ    1 
ATOM   3806 N N     . LEU   E 2 45  ? 4.744   -24.908 33.494  1.00 43.50  ?  45  LEU   E N     1 
ATOM   3807 C CA    . LEU   E 2 45  ? 5.950   -25.257 34.232  1.00 42.26  ?  45  LEU   E CA    1 
ATOM   3808 C C     . LEU   E 2 45  ? 7.198   -24.960 33.389  1.00 41.72  ?  45  LEU   E C     1 
ATOM   3809 O O     . LEU   E 2 45  ? 7.100   -24.950 32.161  1.00 41.86  ?  45  LEU   E O     1 
ATOM   3810 C CB    . LEU   E 2 45  ? 5.920   -26.740 34.630  1.00 42.67  ?  45  LEU   E CB    1 
ATOM   3811 C CG    . LEU   E 2 45  ? 5.168   -27.120 35.916  1.00 44.49  ?  45  LEU   E CG    1 
ATOM   3812 C CD1   . LEU   E 2 45  ? 3.697   -26.692 36.001  1.00 47.15  ?  45  LEU   E CD1   1 
ATOM   3813 C CD2   . LEU   E 2 45  ? 5.298   -28.620 36.092  1.00 42.55  ?  45  LEU   E CD2   1 
ATOM   3814 N N     . PRO   E 2 46  ? 8.406   -24.826 33.999  1.00 40.09  ?  46  PRO   E N     1 
ATOM   3815 C CA    . PRO   E 2 46  ? 9.643   -24.609 33.253  1.00 40.58  ?  46  PRO   E CA    1 
ATOM   3816 C C     . PRO   E 2 46  ? 9.921   -25.629 32.154  1.00 39.16  ?  46  PRO   E C     1 
ATOM   3817 O O     . PRO   E 2 46  ? 9.806   -26.812 32.407  1.00 39.72  ?  46  PRO   E O     1 
ATOM   3818 C CB    . PRO   E 2 46  ? 10.750  -24.690 34.302  1.00 40.47  ?  46  PRO   E CB    1 
ATOM   3819 C CG    . PRO   E 2 46  ? 10.066  -24.371 35.617  1.00 40.84  ?  46  PRO   E CG    1 
ATOM   3820 C CD    . PRO   E 2 46  ? 8.624   -24.817 35.453  1.00 39.41  ?  46  PRO   E CD    1 
ATOM   3821 N N     . ASN   E 2 47  ? 10.281  -25.192 30.946  1.00 39.42  ?  47  ASN   E N     1 
ATOM   3822 C CA    . ASN   E 2 47  ? 10.792  -26.040 29.878  1.00 38.34  ?  47  ASN   E CA    1 
ATOM   3823 C C     . ASN   E 2 47  ? 12.268  -26.359 30.135  1.00 38.59  ?  47  ASN   E C     1 
ATOM   3824 O O     . ASN   E 2 47  ? 13.161  -25.998 29.350  1.00 39.70  ?  47  ASN   E O     1 
ATOM   3825 C CB    . ASN   E 2 47  ? 10.547  -25.404 28.521  1.00 40.52  ?  47  ASN   E CB    1 
ATOM   3826 C CG    . ASN   E 2 47  ? 9.087   -25.121 28.241  1.00 41.16  ?  47  ASN   E CG    1 
ATOM   3827 O OD1   . ASN   E 2 47  ? 8.672   -23.955 28.259  1.00 43.37  ?  47  ASN   E OD1   1 
ATOM   3828 N ND2   . ASN   E 2 47  ? 8.303   -26.151 27.955  1.00 40.14  ?  47  ASN   E ND2   1 
ATOM   3829 N N     . THR   E 2 48  ? 12.503  -27.095 31.229  1.00 36.99  ?  48  THR   E N     1 
ATOM   3830 C CA    . THR   E 2 48  ? 13.814  -27.518 31.677  1.00 37.84  ?  48  THR   E CA    1 
ATOM   3831 C C     . THR   E 2 48  ? 13.859  -29.038 31.663  1.00 36.95  ?  48  THR   E C     1 
ATOM   3832 O O     . THR   E 2 48  ? 12.826  -29.705 31.792  1.00 35.72  ?  48  THR   E O     1 
ATOM   3833 C CB    . THR   E 2 48  ? 14.088  -26.997 33.085  1.00 38.25  ?  48  THR   E CB    1 
ATOM   3834 O OG1   . THR   E 2 48  ? 13.126  -27.513 34.013  1.00 36.07  ?  48  THR   E OG1   1 
ATOM   3835 C CG2   . THR   E 2 48  ? 14.125  -25.485 33.090  1.00 40.09  ?  48  THR   E CG2   1 
ATOM   3836 N N     . GLN   E 2 49  ? 15.095  -29.561 31.648  1.00 38.46  ?  49  GLN   E N     1 
ATOM   3837 C CA    . GLN   E 2 49  ? 15.413  -30.984 31.714  1.00 36.77  ?  49  GLN   E CA    1 
ATOM   3838 C C     . GLN   E 2 49  ? 14.744  -31.581 32.968  1.00 34.82  ?  49  GLN   E C     1 
ATOM   3839 O O     . GLN   E 2 49  ? 14.024  -32.597 32.892  1.00 34.31  ?  49  GLN   E O     1 
ATOM   3840 C CB    . GLN   E 2 49  ? 16.952  -31.094 31.618  1.00 39.25  ?  49  GLN   E CB    1 
ATOM   3841 C CG    . GLN   E 2 49  ? 17.603  -30.442 30.388  0.50 41.60  ?  49  GLN   E CG    1 
ATOM   3842 C CD    . GLN   E 2 49  ? 18.325  -29.095 30.558  0.50 44.85  ?  49  GLN   E CD    1 
ATOM   3843 O OE1   . GLN   E 2 49  ? 17.797  -28.061 31.020  1.00 44.88  ?  49  GLN   E OE1   1 
ATOM   3844 N NE2   . GLN   E 2 49  ? 19.562  -29.051 30.071  0.50 46.41  ?  49  GLN   E NE2   1 
ATOM   3845 N N     . ALA   E 2 50  ? 14.900  -30.901 34.111  1.00 35.26  ?  50  ALA   E N     1 
ATOM   3846 C CA    . ALA   E 2 50  ? 14.402  -31.397 35.393  1.00 33.81  ?  50  ALA   E CA    1 
ATOM   3847 C C     . ALA   E 2 50  ? 12.893  -31.586 35.354  1.00 31.47  ?  50  ALA   E C     1 
ATOM   3848 O O     . ALA   E 2 50  ? 12.443  -32.700 35.579  1.00 31.32  ?  50  ALA   E O     1 
ATOM   3849 C CB    . ALA   E 2 50  ? 14.786  -30.508 36.520  1.00 34.89  ?  50  ALA   E CB    1 
ATOM   3850 N N     . CYS   E 2 51  ? 12.142  -30.560 34.966  1.00 31.76  ?  51  CYS   E N     1 
ATOM   3851 C CA    . CYS   E 2 51  ? 10.682  -30.679 34.922  1.00 31.68  ?  51  CYS   E CA    1 
ATOM   3852 C C     . CYS   E 2 51  ? 10.185  -31.662 33.856  1.00 30.29  ?  51  CYS   E C     1 
ATOM   3853 O O     . CYS   E 2 51  ? 9.127   -32.255 34.047  1.00 29.09  ?  51  CYS   E O     1 
ATOM   3854 C CB    . CYS   E 2 51  ? 10.015  -29.346 34.627  1.00 33.44  ?  51  CYS   E CB    1 
ATOM   3855 S SG    . CYS   E 2 51  ? 10.304  -28.107 35.903  1.00 37.00  ?  51  CYS   E SG    1 
ATOM   3856 N N     . TYR   E 2 52  ? 10.935  -31.810 32.746  1.00 30.71  ?  52  TYR   E N     1 
ATOM   3857 C CA    . TYR   E 2 52  ? 10.532  -32.663 31.638  1.00 30.49  ?  52  TYR   E CA    1 
ATOM   3858 C C     . TYR   E 2 52  ? 10.657  -34.136 32.027  1.00 28.45  ?  52  TYR   E C     1 
ATOM   3859 O O     . TYR   E 2 52  ? 9.689   -34.854 31.900  1.00 26.63  ?  52  TYR   E O     1 
ATOM   3860 C CB    . TYR   E 2 52  ? 11.404  -32.358 30.423  1.00 31.09  ?  52  TYR   E CB    1 
ATOM   3861 C CG    . TYR   E 2 52  ? 11.091  -33.128 29.149  1.00 30.58  ?  52  TYR   E CG    1 
ATOM   3862 C CD1   . TYR   E 2 52  ? 9.789   -33.526 28.774  1.00 29.25  ?  52  TYR   E CD1   1 
ATOM   3863 C CD2   . TYR   E 2 52  ? 12.136  -33.465 28.302  1.00 31.16  ?  52  TYR   E CD2   1 
ATOM   3864 C CE1   . TYR   E 2 52  ? 9.569   -34.215 27.577  1.00 28.71  ?  52  TYR   E CE1   1 
ATOM   3865 C CE2   . TYR   E 2 52  ? 11.918  -34.172 27.128  1.00 31.14  ?  52  TYR   E CE2   1 
ATOM   3866 C CZ    . TYR   E 2 52  ? 10.637  -34.517 26.742  1.00 29.79  ?  52  TYR   E CZ    1 
ATOM   3867 O OH    . TYR   E 2 52  ? 10.511  -35.106 25.523  1.00 29.72  ?  52  TYR   E OH    1 
ATOM   3868 N N     . ILE   E 2 53  ? 11.841  -34.526 32.536  1.00 29.66  ?  53  ILE   E N     1 
ATOM   3869 C CA    . ILE   E 2 53  ? 12.115  -35.862 33.044  1.00 29.39  ?  53  ILE   E CA    1 
ATOM   3870 C C     . ILE   E 2 53  ? 11.062  -36.206 34.123  1.00 26.97  ?  53  ILE   E C     1 
ATOM   3871 O O     . ILE   E 2 53  ? 10.449  -37.260 34.047  1.00 24.02  ?  53  ILE   E O     1 
ATOM   3872 C CB    . ILE   E 2 53  ? 13.590  -35.988 33.528  1.00 32.83  ?  53  ILE   E CB    1 
ATOM   3873 C CG1   . ILE   E 2 53  ? 14.612  -35.789 32.337  1.00 35.75  ?  53  ILE   E CG1   1 
ATOM   3874 C CG2   . ILE   E 2 53  ? 13.820  -37.339 34.218  1.00 33.53  ?  53  ILE   E CG2   1 
ATOM   3875 C CD1   . ILE   E 2 53  ? 16.056  -35.478 32.689  1.00 38.47  ?  53  ILE   E CD1   1 
ATOM   3876 N N     . GLY   E 2 54  ? 10.822  -35.282 35.056  1.00 26.90  ?  54  GLY   E N     1 
ATOM   3877 C CA    . GLY   E 2 54  ? 9.825   -35.445 36.108  1.00 26.84  ?  54  GLY   E CA    1 
ATOM   3878 C C     . GLY   E 2 54  ? 8.431   -35.733 35.572  1.00 25.06  ?  54  GLY   E C     1 
ATOM   3879 O O     . GLY   E 2 54  ? 7.766   -36.680 36.029  1.00 24.98  ?  54  GLY   E O     1 
ATOM   3880 N N     . SER   E 2 55  ? 8.045   -34.946 34.569  1.00 24.93  ?  55  SER   E N     1 
ATOM   3881 C CA    . SER   E 2 55  ? 6.811   -35.166 33.848  1.00 24.80  ?  55  SER   E CA    1 
ATOM   3882 C C     . SER   E 2 55  ? 6.717   -36.586 33.236  1.00 22.28  ?  55  SER   E C     1 
ATOM   3883 O O     . SER   E 2 55  ? 5.714   -37.264 33.467  1.00 21.07  ?  55  SER   E O     1 
ATOM   3884 C CB    . SER   E 2 55  ? 6.587   -34.051 32.822  1.00 26.90  ?  55  SER   E CB    1 
ATOM   3885 O OG    . SER   E 2 55  ? 5.611   -34.405 31.856  1.00 27.46  ?  55  SER   E OG    1 
ATOM   3886 N N     . ILE   E 2 56  ? 7.760   -37.045 32.513  1.00 21.40  ?  56  ILE   E N     1 
ATOM   3887 C CA    . ILE   E 2 56  ? 7.757   -38.359 31.865  1.00 20.67  ?  56  ILE   E CA    1 
ATOM   3888 C C     . ILE   E 2 56  ? 7.618   -39.494 32.913  1.00 20.50  ?  56  ILE   E C     1 
ATOM   3889 O O     . ILE   E 2 56  ? 6.819   -40.429 32.719  1.00 19.51  ?  56  ILE   E O     1 
ATOM   3890 C CB    . ILE   E 2 56  ? 9.002   -38.575 30.964  1.00 20.54  ?  56  ILE   E CB    1 
ATOM   3891 C CG1   . ILE   E 2 56  ? 9.071   -37.575 29.800  1.00 21.19  ?  56  ILE   E CG1   1 
ATOM   3892 C CG2   . ILE   E 2 56  ? 9.041   -40.009 30.424  1.00 19.59  ?  56  ILE   E CG2   1 
ATOM   3893 C CD1   . ILE   E 2 56  ? 10.462  -37.463 29.196  1.00 22.28  ?  56  ILE   E CD1   1 
ATOM   3894 N N     . LEU   E 2 57  ? 8.447   -39.433 33.967  1.00 20.39  ?  57  LEU   E N     1 
ATOM   3895 C CA    . LEU   E 2 57  ? 8.453   -40.428 35.020  1.00 20.81  ?  57  LEU   E CA    1 
ATOM   3896 C C     . LEU   E 2 57  ? 7.077   -40.569 35.671  1.00 20.32  ?  57  LEU   E C     1 
ATOM   3897 O O     . LEU   E 2 57  ? 6.592   -41.700 35.822  1.00 20.89  ?  57  LEU   E O     1 
ATOM   3898 C CB    . LEU   E 2 57  ? 9.524   -40.152 36.066  1.00 22.05  ?  57  LEU   E CB    1 
ATOM   3899 C CG    . LEU   E 2 57  ? 10.963  -40.227 35.563  1.00 23.75  ?  57  LEU   E CG    1 
ATOM   3900 C CD1   . LEU   E 2 57  ? 11.857  -39.773 36.677  1.00 24.72  ?  57  LEU   E CD1   1 
ATOM   3901 C CD2   . LEU   E 2 57  ? 11.285  -41.626 35.048  1.00 24.17  ?  57  LEU   E CD2   1 
ATOM   3902 N N     . LEU   E 2 58  ? 6.439   -39.446 35.958  1.00 20.17  ?  58  LEU   E N     1 
ATOM   3903 C CA    . LEU   E 2 58  ? 5.170   -39.417 36.652  1.00 20.60  ?  58  LEU   E CA    1 
ATOM   3904 C C     . LEU   E 2 58  ? 4.040   -39.928 35.755  1.00 20.17  ?  58  LEU   E C     1 
ATOM   3905 O O     . LEU   E 2 58  ? 3.097   -40.494 36.298  1.00 21.08  ?  58  LEU   E O     1 
ATOM   3906 C CB    . LEU   E 2 58  ? 4.896   -37.998 37.171  1.00 21.88  ?  58  LEU   E CB    1 
ATOM   3907 C CG    . LEU   E 2 58  ? 3.525   -37.757 37.821  1.00 22.59  ?  58  LEU   E CG    1 
ATOM   3908 C CD1   . LEU   E 2 58  ? 3.335   -38.666 39.055  1.00 22.60  ?  58  LEU   E CD1   1 
ATOM   3909 C CD2   . LEU   E 2 58  ? 3.371   -36.295 38.118  1.00 23.46  ?  58  LEU   E CD2   1 
ATOM   3910 N N     . THR   E 2 59  ? 4.083   -39.687 34.423  1.00 20.08  ?  59  THR   E N     1 
ATOM   3911 C CA    . THR   E 2 59  ? 2.958   -39.984 33.551  1.00 20.08  ?  59  THR   E CA    1 
ATOM   3912 C C     . THR   E 2 59  ? 3.048   -41.419 32.985  1.00 18.99  ?  59  THR   E C     1 
ATOM   3913 O O     . THR   E 2 59  ? 2.208   -41.793 32.160  1.00 19.30  ?  59  THR   E O     1 
ATOM   3914 C CB    . THR   E 2 59  ? 2.871   -38.901 32.474  1.00 20.45  ?  59  THR   E CB    1 
ATOM   3915 O OG1   . THR   E 2 59  ? 4.079   -38.808 31.727  1.00 20.96  ?  59  THR   E OG1   1 
ATOM   3916 C CG2   . THR   E 2 59  ? 2.500   -37.551 33.051  1.00 21.65  ?  59  THR   E CG2   1 
ATOM   3917 N N     . THR   E 2 60  ? 4.068   -42.206 33.381  1.00 18.28  ?  60  THR   E N     1 
ATOM   3918 C CA    . THR   E 2 60  ? 4.208   -43.608 32.983  1.00 18.52  ?  60  THR   E CA    1 
ATOM   3919 C C     . THR   E 2 60  ? 3.200   -44.494 33.730  1.00 17.66  ?  60  THR   E C     1 
ATOM   3920 O O     . THR   E 2 60  ? 3.225   -44.490 34.951  1.00 18.68  ?  60  THR   E O     1 
ATOM   3921 C CB    . THR   E 2 60  ? 5.651   -44.067 33.239  1.00 19.59  ?  60  THR   E CB    1 
ATOM   3922 O OG1   . THR   E 2 60  ? 6.362   -43.143 32.414  1.00 19.87  ?  60  THR   E OG1   1 
ATOM   3923 C CG2   . THR   E 2 60  ? 5.826   -45.525 32.857  1.00 20.17  ?  60  THR   E CG2   1 
ATOM   3924 N N     . ALA   E 2 61  ? 2.309   -45.207 33.021  1.00 16.75  ?  61  ALA   E N     1 
ATOM   3925 C CA    . ALA   E 2 61  ? 1.215   -45.956 33.643  1.00 17.99  ?  61  ALA   E CA    1 
ATOM   3926 C C     . ALA   E 2 61  ? 1.745   -47.299 34.167  1.00 18.78  ?  61  ALA   E C     1 
ATOM   3927 O O     . ALA   E 2 61  ? 1.563   -48.325 33.538  1.00 19.12  ?  61  ALA   E O     1 
ATOM   3928 C CB    . ALA   E 2 61  ? 0.080   -46.135 32.674  1.00 17.60  ?  61  ALA   E CB    1 
ATOM   3929 N N     . ARG   E 2 62  ? 2.474   -47.267 35.279  1.00 20.04  ?  62  ARG   E N     1 
ATOM   3930 C CA    . ARG   E 2 62  ? 3.158   -48.428 35.837  1.00 23.76  ?  62  ARG   E CA    1 
ATOM   3931 C C     . ARG   E 2 62  ? 2.224   -49.433 36.532  1.00 26.00  ?  62  ARG   E C     1 
ATOM   3932 O O     . ARG   E 2 62  ? 2.676   -50.546 36.782  1.00 27.49  ?  62  ARG   E O     1 
ATOM   3933 C CB    . ARG   E 2 62  ? 4.219   -48.011 36.862  1.00 25.48  ?  62  ARG   E CB    1 
ATOM   3934 C CG    . ARG   E 2 62  ? 5.383   -47.317 36.179  1.00 28.16  ?  62  ARG   E CG    1 
ATOM   3935 C CD    . ARG   E 2 62  ? 6.587   -46.991 37.035  1.00 32.02  ?  62  ARG   E CD    1 
ATOM   3936 N NE    . ARG   E 2 62  ? 7.716   -46.773 36.111  1.00 33.62  ?  62  ARG   E NE    1 
ATOM   3937 C CZ    . ARG   E 2 62  ? 8.627   -47.697 35.765  1.00 37.51  ?  62  ARG   E CZ    1 
ATOM   3938 N NH1   . ARG   E 2 62  ? 8.545   -48.957 36.187  1.00 36.88  1  62  ARG   E NH1   1 
ATOM   3939 N NH2   . ARG   E 2 62  ? 9.631   -47.380 34.964  1.00 41.24  ?  62  ARG   E NH2   1 
ATOM   3940 N N     . LYS   E 2 63  ? 1.027   -48.999 36.987  1.00 26.60  ?  63  LYS   E N     1 
ATOM   3941 C CA    . LYS   E 2 63  ? 0.053   -49.857 37.641  1.00 27.44  ?  63  LYS   E CA    1 
ATOM   3942 C C     . LYS   E 2 63  ? -0.820  -50.422 36.533  1.00 24.98  ?  63  LYS   E C     1 
ATOM   3943 O O     . LYS   E 2 63  ? -1.559  -49.642 35.930  1.00 24.07  ?  63  LYS   E O     1 
ATOM   3944 C CB    . LYS   E 2 63  ? -0.771  -49.073 38.673  1.00 29.64  ?  63  LYS   E CB    1 
ATOM   3945 C CG    . LYS   E 2 63  ? -1.770  -49.919 39.458  1.00 32.88  ?  63  LYS   E CG    1 
ATOM   3946 C CD    . LYS   E 2 63  ? -2.630  -49.201 40.506  1.00 36.20  ?  63  LYS   E CD    1 
ATOM   3947 C CE    . LYS   E 2 63  ? -3.688  -50.087 41.129  1.00 38.86  ?  63  LYS   E CE    1 
ATOM   3948 N NZ    . LYS   E 2 63  ? -4.837  -49.414 41.758  1.00 41.06  1  63  LYS   E NZ    1 
ATOM   3949 N N     . THR   E 2 64  ? -0.696  -51.735 36.254  1.00 26.45  ?  64  THR   E N     1 
ATOM   3950 C CA    . THR   E 2 64  ? -1.557  -52.469 35.332  1.00 25.28  ?  64  THR   E CA    1 
ATOM   3951 C C     . THR   E 2 64  ? -2.469  -53.429 36.078  1.00 25.74  ?  64  THR   E C     1 
ATOM   3952 O O     . THR   E 2 64  ? -1.942  -54.274 36.771  1.00 26.33  ?  64  THR   E O     1 
ATOM   3953 C CB    . THR   E 2 64  ? -0.650  -53.223 34.369  1.00 26.66  ?  64  THR   E CB    1 
ATOM   3954 O OG1   . THR   E 2 64  ? 0.135   -52.230 33.726  1.00 25.69  ?  64  THR   E OG1   1 
ATOM   3955 C CG2   . THR   E 2 64  ? -1.418  -53.971 33.285  1.00 27.68  ?  64  THR   E CG2   1 
ATOM   3956 N N     . THR   E 2 65  ? -3.794  -53.389 35.782  1.00 26.61  ?  65  THR   E N     1 
ATOM   3957 C CA    . THR   E 2 65  ? -4.827  -54.310 36.233  1.00 28.08  ?  65  THR   E CA    1 
ATOM   3958 C C     . THR   E 2 65  ? -5.501  -54.964 35.016  1.00 27.52  ?  65  THR   E C     1 
ATOM   3959 O O     . THR   E 2 65  ? -5.973  -54.243 34.141  1.00 26.33  ?  65  THR   E O     1 
ATOM   3960 C CB    . THR   E 2 65  ? -5.877  -53.516 37.014  1.00 29.27  ?  65  THR   E CB    1 
ATOM   3961 O OG1   . THR   E 2 65  ? -5.165  -52.766 37.981  1.00 30.39  ?  65  THR   E OG1   1 
ATOM   3962 C CG2   . THR   E 2 65  ? -6.888  -54.379 37.750  1.00 32.67  ?  65  THR   E CG2   1 
ATOM   3963 N N     . TYR   E 2 66  ? -5.626  -56.304 35.005  1.00 29.21  ?  66  TYR   E N     1 
ATOM   3964 C CA    . TYR   E 2 66  ? -6.320  -57.058 33.964  1.00 30.06  ?  66  TYR   E CA    1 
ATOM   3965 C C     . TYR   E 2 66  ? -7.710  -57.469 34.460  1.00 31.44  ?  66  TYR   E C     1 
ATOM   3966 O O     . TYR   E 2 66  ? -7.859  -57.777 35.632  1.00 32.12  ?  66  TYR   E O     1 
ATOM   3967 C CB    . TYR   E 2 66  ? -5.477  -58.280 33.593  1.00 31.91  ?  66  TYR   E CB    1 
ATOM   3968 C CG    . TYR   E 2 66  ? -4.116  -57.906 33.005  1.00 30.35  ?  66  TYR   E CG    1 
ATOM   3969 C CD1   . TYR   E 2 66  ? -4.025  -57.311 31.749  1.00 28.60  ?  66  TYR   E CD1   1 
ATOM   3970 C CD2   . TYR   E 2 66  ? -2.929  -58.161 33.690  1.00 31.75  ?  66  TYR   E CD2   1 
ATOM   3971 C CE1   . TYR   E 2 66  ? -2.800  -56.993 31.192  1.00 28.75  ?  66  TYR   E CE1   1 
ATOM   3972 C CE2   . TYR   E 2 66  ? -1.686  -57.843 33.137  1.00 31.23  ?  66  TYR   E CE2   1 
ATOM   3973 C CZ    . TYR   E 2 66  ? -1.624  -57.264 31.885  1.00 29.36  ?  66  TYR   E CZ    1 
ATOM   3974 O OH    . TYR   E 2 66  ? -0.434  -56.922 31.316  1.00 31.24  ?  66  TYR   E OH    1 
ATOM   3975 N N     . SER   E 2 67  ? -8.715  -57.468 33.564  1.00 31.35  ?  67  SER   E N     1 
ATOM   3976 C CA    . SER   E 2 67  ? -10.027 -58.055 33.858  1.00 34.18  ?  67  SER   E CA    1 
ATOM   3977 C C     . SER   E 2 67  ? -10.683 -58.651 32.595  1.00 34.30  ?  67  SER   E C     1 
ATOM   3978 O O     . SER   E 2 67  ? -9.981  -58.816 31.529  1.00 31.39  ?  67  SER   E O     1 
ATOM   3979 C CB    . SER   E 2 67  ? -10.909 -57.027 34.538  1.00 33.87  ?  67  SER   E CB    1 
ATOM   3980 O OG    . SER   E 2 67  ? -11.139 -55.920 33.685  1.00 31.46  ?  67  SER   E OG    1 
ATOM   3981 O OXT   . SER   E 2 67  ? -11.857 -59.044 32.753  1.00 37.22  ?  67  SER   E OXT   1 
ATOM   3982 N N     . SER   F 3 4   ? 15.062  -45.120 42.747  1.00 71.89  ?  4   SER   F N     1 
ATOM   3983 C CA    . SER   F 3 4   ? 13.906  -45.357 41.840  1.00 67.75  ?  4   SER   F CA    1 
ATOM   3984 C C     . SER   F 3 4   ? 14.293  -45.123 40.366  1.00 69.07  ?  4   SER   F C     1 
ATOM   3985 O O     . SER   F 3 4   ? 15.377  -44.624 40.054  1.00 73.34  ?  4   SER   F O     1 
ATOM   3986 C CB    . SER   F 3 4   ? 12.721  -44.512 42.278  1.00 64.53  ?  4   SER   F CB    1 
ATOM   3987 O OG    . SER   F 3 4   ? 11.521  -44.926 41.631  1.00 58.91  ?  4   SER   F OG    1 
ATOM   3988 N N     . VAL   F 3 5   ? 13.375  -45.472 39.446  1.00 68.09  ?  5   VAL   F N     1 
ATOM   3989 C CA    . VAL   F 3 5   ? 13.631  -45.497 38.004  1.00 63.98  ?  5   VAL   F CA    1 
ATOM   3990 C C     . VAL   F 3 5   ? 13.747  -44.052 37.489  1.00 57.65  ?  5   VAL   F C     1 
ATOM   3991 O O     . VAL   F 3 5   ? 12.971  -43.195 37.915  1.00 58.13  ?  5   VAL   F O     1 
ATOM   3992 C CB    . VAL   F 3 5   ? 12.532  -46.286 37.252  1.00 64.93  ?  5   VAL   F CB    1 
ATOM   3993 C CG1   . VAL   F 3 5   ? 12.861  -46.444 35.765  1.00 66.47  ?  5   VAL   F CG1   1 
ATOM   3994 C CG2   . VAL   F 3 5   ? 12.244  -47.652 37.899  1.00 65.69  ?  5   VAL   F CG2   1 
ATOM   3995 N N     . ASP   F 3 6   ? 14.743  -43.783 36.615  1.00 52.25  ?  6   ASP   F N     1 
ATOM   3996 C CA    . ASP   F 3 6   ? 14.976  -42.479 35.985  1.00 49.62  ?  6   ASP   F CA    1 
ATOM   3997 C C     . ASP   F 3 6   ? 14.909  -42.483 34.456  1.00 44.59  ?  6   ASP   F C     1 
ATOM   3998 O O     . ASP   F 3 6   ? 14.965  -41.388 33.914  1.00 44.59  ?  6   ASP   F O     1 
ATOM   3999 C CB    . ASP   F 3 6   ? 16.285  -41.845 36.455  1.00 54.08  ?  6   ASP   F CB    1 
ATOM   4000 C CG    . ASP   F 3 6   ? 16.319  -41.309 37.878  1.00 60.40  ?  6   ASP   F CG    1 
ATOM   4001 O OD1   . ASP   F 3 6   ? 15.370  -41.598 38.672  1.00 56.53  ?  6   ASP   F OD1   1 
ATOM   4002 O OD2   . ASP   F 3 6   ? 17.320  -40.601 38.184  1.00 70.01  -1 6   ASP   F OD2   1 
ATOM   4003 N N     . ASP   F 3 7   ? 14.711  -43.625 33.757  1.00 39.24  ?  7   ASP   F N     1 
ATOM   4004 C CA    . ASP   F 3 7   ? 14.666  -43.639 32.302  1.00 37.00  ?  7   ASP   F CA    1 
ATOM   4005 C C     . ASP   F 3 7   ? 13.221  -43.847 31.855  1.00 31.58  ?  7   ASP   F C     1 
ATOM   4006 O O     . ASP   F 3 7   ? 12.420  -44.445 32.564  1.00 31.32  ?  7   ASP   F O     1 
ATOM   4007 C CB    . ASP   F 3 7   ? 15.666  -44.627 31.736  1.00 40.87  ?  7   ASP   F CB    1 
ATOM   4008 C CG    . ASP   F 3 7   ? 17.120  -44.238 31.988  1.00 46.25  ?  7   ASP   F CG    1 
ATOM   4009 O OD1   . ASP   F 3 7   ? 17.648  -43.350 31.264  1.00 54.43  ?  7   ASP   F OD1   1 
ATOM   4010 O OD2   . ASP   F 3 7   ? 17.721  -44.818 32.909  1.00 48.38  -1 7   ASP   F OD2   1 
ATOM   4011 N N     . TYR   F 3 8   ? 12.900  -43.315 30.682  1.00 27.83  ?  8   TYR   F N     1 
ATOM   4012 C CA    . TYR   F 3 8   ? 11.675  -43.645 29.973  1.00 24.64  ?  8   TYR   F CA    1 
ATOM   4013 C C     . TYR   F 3 8   ? 11.676  -45.153 29.663  1.00 23.31  ?  8   TYR   F C     1 
ATOM   4014 O O     . TYR   F 3 8   ? 12.692  -45.666 29.178  1.00 22.20  ?  8   TYR   F O     1 
ATOM   4015 C CB    . TYR   F 3 8   ? 11.563  -42.809 28.701  1.00 22.67  ?  8   TYR   F CB    1 
ATOM   4016 C CG    . TYR   F 3 8   ? 10.421  -43.212 27.787  1.00 20.89  ?  8   TYR   F CG    1 
ATOM   4017 C CD1   . TYR   F 3 8   ? 9.100   -43.282 28.231  1.00 20.35  ?  8   TYR   F CD1   1 
ATOM   4018 C CD2   . TYR   F 3 8   ? 10.673  -43.600 26.483  1.00 20.59  ?  8   TYR   F CD2   1 
ATOM   4019 C CE1   . TYR   F 3 8   ? 8.071   -43.674 27.377  1.00 18.83  ?  8   TYR   F CE1   1 
ATOM   4020 C CE2   . TYR   F 3 8   ? 9.648   -43.961 25.621  1.00 19.43  ?  8   TYR   F CE2   1 
ATOM   4021 C CZ    . TYR   F 3 8   ? 8.340   -44.007 26.065  1.00 18.28  ?  8   TYR   F CZ    1 
ATOM   4022 O OH    . TYR   F 3 8   ? 7.367   -44.405 25.170  1.00 18.54  ?  8   TYR   F OH    1 
ATOM   4023 N N     . ASN   F 3 9   ? 10.521  -45.804 29.934  1.00 21.20  ?  9   ASN   F N     1 
ATOM   4024 C CA    . ASN   F 3 9   ? 10.274  -47.184 29.595  1.00 20.07  ?  9   ASN   F CA    1 
ATOM   4025 C C     . ASN   F 3 9   ? 9.104   -47.185 28.614  1.00 18.78  ?  9   ASN   F C     1 
ATOM   4026 O O     . ASN   F 3 9   ? 7.963   -47.155 29.063  1.00 18.99  ?  9   ASN   F O     1 
ATOM   4027 C CB    . ASN   F 3 9   ? 10.122  -48.039 30.854  1.00 20.17  ?  9   ASN   F CB    1 
ATOM   4028 C CG    . ASN   F 3 9   ? 10.111  -49.521 30.535  1.00 19.38  ?  9   ASN   F CG    1 
ATOM   4029 O OD1   . ASN   F 3 9   ? 9.891   -49.924 29.386  1.00 18.32  ?  9   ASN   F OD1   1 
ATOM   4030 N ND2   . ASN   F 3 9   ? 10.308  -50.351 31.523  1.00 19.75  ?  9   ASN   F ND2   1 
ATOM   4031 N N     . PRO   F 3 10  ? 9.327   -47.348 27.286  1.00 18.46  ?  10  PRO   F N     1 
ATOM   4032 C CA    . PRO   F 3 10  ? 8.230   -47.518 26.336  1.00 17.38  ?  10  PRO   F CA    1 
ATOM   4033 C C     . PRO   F 3 10  ? 7.419   -48.812 26.446  1.00 17.60  ?  10  PRO   F C     1 
ATOM   4034 O O     . PRO   F 3 10  ? 6.357   -48.857 25.798  1.00 18.59  ?  10  PRO   F O     1 
ATOM   4035 C CB    . PRO   F 3 10  ? 8.891   -47.411 24.951  1.00 17.29  ?  10  PRO   F CB    1 
ATOM   4036 C CG    . PRO   F 3 10  ? 10.317  -47.861 25.216  1.00 18.38  ?  10  PRO   F CG    1 
ATOM   4037 C CD    . PRO   F 3 10  ? 10.648  -47.458 26.621  1.00 18.89  ?  10  PRO   F CD    1 
ATOM   4038 N N     . ALA   F 3 11  ? 7.826   -49.810 27.273  1.00 17.88  ?  11  ALA   F N     1 
ATOM   4039 C CA    . ALA   F 3 11  ? 6.947   -50.924 27.594  1.00 18.59  ?  11  ALA   F CA    1 
ATOM   4040 C C     . ALA   F 3 11  ? 5.657   -50.493 28.267  1.00 19.43  ?  11  ALA   F C     1 
ATOM   4041 O O     . ALA   F 3 11  ? 4.656   -51.208 28.123  1.00 19.07  ?  11  ALA   F O     1 
ATOM   4042 C CB    . ALA   F 3 11  ? 7.603   -51.949 28.439  1.00 20.13  ?  11  ALA   F CB    1 
ATOM   4043 N N     . PHE   F 3 12  ? 5.694   -49.367 29.025  1.00 19.42  ?  12  PHE   F N     1 
ATOM   4044 C CA    . PHE   F 3 12  ? 4.535   -48.870 29.748  1.00 19.47  ?  12  PHE   F CA    1 
ATOM   4045 C C     . PHE   F 3 12  ? 3.895   -47.789 28.901  1.00 17.77  ?  12  PHE   F C     1 
ATOM   4046 O O     . PHE   F 3 12  ? 4.585   -46.967 28.291  1.00 16.87  ?  12  PHE   F O     1 
ATOM   4047 C CB    . PHE   F 3 12  ? 4.964   -48.369 31.121  1.00 21.74  ?  12  PHE   F CB    1 
ATOM   4048 C CG    . PHE   F 3 12  ? 5.452   -49.459 32.060  1.00 24.38  ?  12  PHE   F CG    1 
ATOM   4049 C CD1   . PHE   F 3 12  ? 4.546   -50.206 32.823  1.00 26.02  ?  12  PHE   F CD1   1 
ATOM   4050 C CD2   . PHE   F 3 12  ? 6.803   -49.757 32.179  1.00 26.64  ?  12  PHE   F CD2   1 
ATOM   4051 C CE1   . PHE   F 3 12  ? 4.980   -51.185 33.712  1.00 26.83  ?  12  PHE   F CE1   1 
ATOM   4052 C CE2   . PHE   F 3 12  ? 7.245   -50.750 33.069  1.00 26.55  ?  12  PHE   F CE2   1 
ATOM   4053 C CZ    . PHE   F 3 12  ? 6.330   -51.449 33.827  1.00 27.93  ?  12  PHE   F CZ    1 
ATOM   4054 N N     . ASP   F 3 13  ? 2.564   -47.805 28.849  1.00 16.35  ?  13  ASP   F N     1 
ATOM   4055 C CA    . ASP   F 3 13  ? 1.800   -46.680 28.329  1.00 16.06  ?  13  ASP   F CA    1 
ATOM   4056 C C     . ASP   F 3 13  ? 2.090   -45.422 29.157  1.00 16.41  ?  13  ASP   F C     1 
ATOM   4057 O O     . ASP   F 3 13  ? 2.281   -45.493 30.361  1.00 17.25  ?  13  ASP   F O     1 
ATOM   4058 C CB    . ASP   F 3 13  ? 0.304   -47.015 28.301  1.00 16.42  ?  13  ASP   F CB    1 
ATOM   4059 C CG    . ASP   F 3 13  ? -0.123  -48.205 27.430  1.00 16.55  ?  13  ASP   F CG    1 
ATOM   4060 O OD1   . ASP   F 3 13  ? 0.589   -48.535 26.445  1.00 15.53  ?  13  ASP   F OD1   1 
ATOM   4061 O OD2   . ASP   F 3 13  ? -1.164  -48.870 27.784  1.00 17.97  -1 13  ASP   F OD2   1 
ATOM   4062 N N     . ASN   F 3 14  ? 2.222   -44.281 28.491  1.00 16.55  ?  14  ASN   F N     1 
ATOM   4063 C CA    . ASN   F 3 14  ? 2.369   -42.995 29.128  1.00 17.23  ?  14  ASN   F CA    1 
ATOM   4064 C C     . ASN   F 3 14  ? 1.152   -42.146 28.768  1.00 16.77  ?  14  ASN   F C     1 
ATOM   4065 O O     . ASN   F 3 14  ? 0.822   -42.035 27.603  1.00 16.25  ?  14  ASN   F O     1 
ATOM   4066 C CB    . ASN   F 3 14  ? 3.663   -42.349 28.645  1.00 17.50  ?  14  ASN   F CB    1 
ATOM   4067 C CG    . ASN   F 3 14  ? 3.999   -41.103 29.420  1.00 17.94  ?  14  ASN   F CG    1 
ATOM   4068 O OD1   . ASN   F 3 14  ? 3.351   -40.062 29.233  1.00 18.12  ?  14  ASN   F OD1   1 
ATOM   4069 N ND2   . ASN   F 3 14  ? 4.968   -41.204 30.316  1.00 18.78  ?  14  ASN   F ND2   1 
ATOM   4070 N N     . THR   F 3 15  ? 0.564   -41.498 29.757  1.00 18.32  ?  15  THR   F N     1 
ATOM   4071 C CA    . THR   F 3 15  ? -0.639  -40.685 29.559  1.00 19.26  ?  15  THR   F CA    1 
ATOM   4072 C C     . THR   F 3 15  ? -0.400  -39.381 28.789  1.00 20.12  ?  15  THR   F C     1 
ATOM   4073 O O     . THR   F 3 15  ? -1.359  -38.878 28.216  1.00 20.35  ?  15  THR   F O     1 
ATOM   4074 C CB    . THR   F 3 15  ? -1.272  -40.408 30.921  1.00 20.13  ?  15  THR   F CB    1 
ATOM   4075 O OG1   . THR   F 3 15  ? -0.284  -39.791 31.755  1.00 19.93  ?  15  THR   F OG1   1 
ATOM   4076 C CG2   . THR   F 3 15  ? -1.847  -41.691 31.506  1.00 20.34  ?  15  THR   F CG2   1 
ATOM   4077 N N     . HIS   F 3 16  ? 0.840   -38.828 28.798  1.00 20.92  ?  16  HIS   F N     1 
ATOM   4078 C CA    . HIS   F 3 16  ? 1.148   -37.543 28.206  1.00 22.10  ?  16  HIS   F CA    1 
ATOM   4079 C C     . HIS   F 3 16  ? 1.960   -37.622 26.928  1.00 22.92  ?  16  HIS   F C     1 
ATOM   4080 O O     . HIS   F 3 16  ? 1.899   -36.638 26.212  1.00 24.36  ?  16  HIS   F O     1 
ATOM   4081 C CB    . HIS   F 3 16  ? 1.856   -36.639 29.219  1.00 23.02  ?  16  HIS   F CB    1 
ATOM   4082 C CG    . HIS   F 3 16  ? 0.966   -36.146 30.300  1.00 23.92  ?  16  HIS   F CG    1 
ATOM   4083 N ND1   . HIS   F 3 16  ? 1.211   -34.918 30.871  1.00 25.49  ?  16  HIS   F ND1   1 
ATOM   4084 C CD2   . HIS   F 3 16  ? -0.160  -36.601 30.867  1.00 23.42  ?  16  HIS   F CD2   1 
ATOM   4085 C CE1   . HIS   F 3 16  ? 0.306   -34.718 31.812  1.00 26.78  ?  16  HIS   F CE1   1 
ATOM   4086 N NE2   . HIS   F 3 16  ? -0.552  -35.717 31.796  1.00 25.85  ?  16  HIS   F NE2   1 
ATOM   4087 N N     . TYR   F 3 17  ? 2.764   -38.691 26.706  1.00 24.06  ?  17  TYR   F N     1 
ATOM   4088 C CA    . TYR   F 3 17  ? 3.791   -38.758 25.658  1.00 22.51  ?  17  TYR   F CA    1 
ATOM   4089 C C     . TYR   F 3 17  ? 3.559   -39.970 24.753  1.00 20.82  ?  17  TYR   F C     1 
ATOM   4090 O O     . TYR   F 3 17  ? 3.059   -41.006 25.196  1.00 21.47  ?  17  TYR   F O     1 
ATOM   4091 C CB    . TYR   F 3 17  ? 5.183   -38.802 26.310  1.00 22.78  ?  17  TYR   F CB    1 
ATOM   4092 C CG    . TYR   F 3 17  ? 5.455   -37.575 27.155  1.00 23.39  ?  17  TYR   F CG    1 
ATOM   4093 C CD1   . TYR   F 3 17  ? 5.857   -36.375 26.559  1.00 26.07  ?  17  TYR   F CD1   1 
ATOM   4094 C CD2   . TYR   F 3 17  ? 5.318   -37.584 28.532  1.00 23.44  ?  17  TYR   F CD2   1 
ATOM   4095 C CE1   . TYR   F 3 17  ? 6.047   -35.214 27.306  1.00 25.90  ?  17  TYR   F CE1   1 
ATOM   4096 C CE2   . TYR   F 3 17  ? 5.536   -36.449 29.296  1.00 24.98  ?  17  TYR   F CE2   1 
ATOM   4097 C CZ    . TYR   F 3 17  ? 5.890   -35.256 28.681  1.00 26.95  ?  17  TYR   F CZ    1 
ATOM   4098 O OH    . TYR   F 3 17  ? 6.076   -34.113 29.410  1.00 28.32  ?  17  TYR   F OH    1 
ATOM   4099 N N     . SER   F 3 18  ? 3.981   -39.835 23.488  1.00 20.14  ?  18  SER   F N     1 
ATOM   4100 C CA    . SER   F 3 18  ? 3.957   -40.916 22.518  1.00 19.61  ?  18  SER   F CA    1 
ATOM   4101 C C     . SER   F 3 18  ? 5.264   -41.695 22.561  1.00 18.89  ?  18  SER   F C     1 
ATOM   4102 O O     . SER   F 3 18  ? 6.309   -41.106 22.852  1.00 19.48  ?  18  SER   F O     1 
ATOM   4103 C CB    . SER   F 3 18  ? 3.662   -40.426 21.112  1.00 19.26  ?  18  SER   F CB    1 
ATOM   4104 O OG    . SER   F 3 18  ? 4.744   -39.720 20.524  1.00 19.00  ?  18  SER   F OG    1 
ATOM   4105 N N     . ARG   F 3 19  ? 5.188   -42.984 22.160  1.00 18.89  ?  19  ARG   F N     1 
ATOM   4106 C CA    . ARG   F 3 19  ? 6.378   -43.798 21.904  1.00 18.72  ?  19  ARG   F CA    1 
ATOM   4107 C C     . ARG   F 3 19  ? 7.217   -43.146 20.814  1.00 18.29  ?  19  ARG   F C     1 
ATOM   4108 O O     . ARG   F 3 19  ? 8.439   -43.086 20.944  1.00 18.26  ?  19  ARG   F O     1 
ATOM   4109 C CB    . ARG   F 3 19  ? 6.097   -45.256 21.472  1.00 18.79  ?  19  ARG   F CB    1 
ATOM   4110 C CG    . ARG   F 3 19  ? 5.901   -46.325 22.548  1.00 18.82  ?  19  ARG   F CG    1 
ATOM   4111 C CD    . ARG   F 3 19  ? 4.633   -46.328 23.252  1.00 17.91  ?  19  ARG   F CD    1 
ATOM   4112 N NE    . ARG   F 3 19  ? 4.482   -47.469 24.157  1.00 18.72  ?  19  ARG   F NE    1 
ATOM   4113 C CZ    . ARG   F 3 19  ? 3.378   -47.810 24.852  1.00 17.18  ?  19  ARG   F CZ    1 
ATOM   4114 N NH1   . ARG   F 3 19  ? 2.241   -47.271 24.543  1.00 16.27  1  19  ARG   F NH1   1 
ATOM   4115 N NH2   . ARG   F 3 19  ? 3.407   -48.761 25.765  1.00 16.64  ?  19  ARG   F NH2   1 
ATOM   4116 N N     . PHE   F 3 20  ? 6.559   -42.709 19.737  1.00 18.86  ?  20  PHE   F N     1 
ATOM   4117 C CA    . PHE   F 3 20  ? 7.241   -42.115 18.595  1.00 20.65  ?  20  PHE   F CA    1 
ATOM   4118 C C     . PHE   F 3 20  ? 8.097   -40.917 19.018  1.00 21.63  ?  20  PHE   F C     1 
ATOM   4119 O O     . PHE   F 3 20  ? 9.285   -40.926 18.734  1.00 22.24  ?  20  PHE   F O     1 
ATOM   4120 C CB    . PHE   F 3 20  ? 6.217   -41.704 17.535  1.00 22.42  ?  20  PHE   F CB    1 
ATOM   4121 C CG    . PHE   F 3 20  ? 6.834   -40.970 16.358  1.00 24.30  ?  20  PHE   F CG    1 
ATOM   4122 C CD1   . PHE   F 3 20  ? 7.595   -41.655 15.407  1.00 25.20  ?  20  PHE   F CD1   1 
ATOM   4123 C CD2   . PHE   F 3 20  ? 6.666   -39.578 16.221  1.00 25.77  ?  20  PHE   F CD2   1 
ATOM   4124 C CE1   . PHE   F 3 20  ? 8.173   -40.967 14.324  1.00 26.28  ?  20  PHE   F CE1   1 
ATOM   4125 C CE2   . PHE   F 3 20  ? 7.212   -38.894 15.114  1.00 25.94  ?  20  PHE   F CE2   1 
ATOM   4126 C CZ    . PHE   F 3 20  ? 7.968   -39.589 14.174  1.00 25.83  ?  20  PHE   F CZ    1 
ATOM   4127 N N     . HIS   F 3 21  ? 7.516   -39.943 19.747  1.00 20.71  ?  21  HIS   F N     1 
ATOM   4128 C CA    . HIS   F 3 21  ? 8.251   -38.753 20.172  1.00 21.35  ?  21  HIS   F CA    1 
ATOM   4129 C C     . HIS   F 3 21  ? 9.444   -39.158 21.048  1.00 20.90  ?  21  HIS   F C     1 
ATOM   4130 O O     . HIS   F 3 21  ? 10.568  -38.834 20.695  1.00 21.76  ?  21  HIS   F O     1 
ATOM   4131 C CB    . HIS   F 3 21  ? 7.308   -37.680 20.772  1.00 21.34  ?  21  HIS   F CB    1 
ATOM   4132 C CG    . HIS   F 3 21  ? 7.969   -36.695 21.688  1.00 21.90  ?  21  HIS   F CG    1 
ATOM   4133 N ND1   . HIS   F 3 21  ? 7.360   -36.279 22.853  1.00 22.43  ?  21  HIS   F ND1   1 
ATOM   4134 C CD2   . HIS   F 3 21  ? 9.172   -36.071 21.647  1.00 22.52  ?  21  HIS   F CD2   1 
ATOM   4135 C CE1   . HIS   F 3 21  ? 8.178   -35.431 23.479  1.00 22.75  ?  21  HIS   F CE1   1 
ATOM   4136 N NE2   . HIS   F 3 21  ? 9.278   -35.300 22.755  1.00 22.75  ?  21  HIS   F NE2   1 
ATOM   4137 N N     . LEU   F 3 22  ? 9.210   -39.871 22.153  1.00 19.92  ?  22  LEU   F N     1 
ATOM   4138 C CA    . LEU   F 3 22  ? 10.268  -40.129 23.122  1.00 20.61  ?  22  LEU   F CA    1 
ATOM   4139 C C     . LEU   F 3 22  ? 11.339  -41.061 22.569  1.00 21.55  ?  22  LEU   F C     1 
ATOM   4140 O O     . LEU   F 3 22  ? 12.499  -40.883 22.929  1.00 23.39  ?  22  LEU   F O     1 
ATOM   4141 C CB    . LEU   F 3 22  ? 9.722   -40.605 24.472  1.00 19.63  ?  22  LEU   F CB    1 
ATOM   4142 C CG    . LEU   F 3 22  ? 8.785   -39.649 25.215  1.00 20.23  ?  22  LEU   F CG    1 
ATOM   4143 C CD1   . LEU   F 3 22  ? 8.406   -40.132 26.592  1.00 19.91  ?  22  LEU   F CD1   1 
ATOM   4144 C CD2   . LEU   F 3 22  ? 9.335   -38.209 25.315  1.00 21.56  ?  22  LEU   F CD2   1 
ATOM   4145 N N     . LEU   F 3 23  ? 10.988  -42.019 21.708  1.00 21.45  ?  23  LEU   F N     1 
ATOM   4146 C CA    . LEU   F 3 23  ? 11.965  -42.886 21.053  1.00 23.17  ?  23  LEU   F CA    1 
ATOM   4147 C C     . LEU   F 3 23  ? 12.843  -42.116 20.062  1.00 24.39  ?  23  LEU   F C     1 
ATOM   4148 O O     . LEU   F 3 23  ? 14.059  -42.321 20.098  1.00 25.00  ?  23  LEU   F O     1 
ATOM   4149 C CB    . LEU   F 3 23  ? 11.363  -44.140 20.407  1.00 22.94  ?  23  LEU   F CB    1 
ATOM   4150 C CG    . LEU   F 3 23  ? 10.753  -45.154 21.386  1.00 24.17  ?  23  LEU   F CG    1 
ATOM   4151 C CD1   . LEU   F 3 23  ? 9.934   -46.208 20.666  1.00 22.66  ?  23  LEU   F CD1   1 
ATOM   4152 C CD2   . LEU   F 3 23  ? 11.870  -45.778 22.225  1.00 26.71  ?  23  LEU   F CD2   1 
ATOM   4153 N N     . ILE   F 3 24  ? 12.260  -41.246 19.200  1.00 24.93  ?  24  ILE   F N     1 
ATOM   4154 C CA    . ILE   F 3 24  ? 13.078  -40.467 18.271  1.00 26.76  ?  24  ILE   F CA    1 
ATOM   4155 C C     . ILE   F 3 24  ? 13.957  -39.474 19.033  1.00 29.19  ?  24  ILE   F C     1 
ATOM   4156 O O     . ILE   F 3 24  ? 15.100  -39.243 18.615  1.00 32.13  ?  24  ILE   F O     1 
ATOM   4157 C CB    . ILE   F 3 24  ? 12.284  -39.833 17.112  1.00 26.33  ?  24  ILE   F CB    1 
ATOM   4158 C CG1   . ILE   F 3 24  ? 11.323  -38.692 17.525  1.00 25.95  ?  24  ILE   F CG1   1 
ATOM   4159 C CG2   . ILE   F 3 24  ? 11.599  -40.943 16.301  1.00 25.97  ?  24  ILE   F CG2   1 
ATOM   4160 C CD1   . ILE   F 3 24  ? 10.636  -38.023 16.354  1.00 26.22  ?  24  ILE   F CD1   1 
ATOM   4161 N N     . GLU   F 3 25  ? 13.460  -38.978 20.181  1.00 28.70  ?  25  GLU   F N     1 
ATOM   4162 C CA    . GLU   F 3 25  ? 14.172  -37.999 20.974  1.00 29.55  ?  25  GLU   F CA    1 
ATOM   4163 C C     . GLU   F 3 25  ? 15.310  -38.641 21.746  1.00 29.98  ?  25  GLU   F C     1 
ATOM   4164 O O     . GLU   F 3 25  ? 16.426  -38.131 21.663  1.00 32.07  ?  25  GLU   F O     1 
ATOM   4165 C CB    . GLU   F 3 25  ? 13.191  -37.231 21.856  1.00 29.52  ?  25  GLU   F CB    1 
ATOM   4166 C CG    . GLU   F 3 25  ? 13.826  -35.982 22.454  1.00 31.76  ?  25  GLU   F CG    1 
ATOM   4167 C CD    . GLU   F 3 25  ? 12.782  -35.298 23.291  1.00 32.31  ?  25  GLU   F CD    1 
ATOM   4168 O OE1   . GLU   F 3 25  ? 11.899  -34.555 22.804  1.00 32.65  ?  25  GLU   F OE1   1 
ATOM   4169 O OE2   . GLU   F 3 25  ? 12.848  -35.617 24.459  1.00 34.38  -1 25  GLU   F OE2   1 
ATOM   4170 N N     . THR   F 3 26  ? 15.046  -39.734 22.481  1.00 28.43  ?  26  THR   F N     1 
ATOM   4171 C CA    . THR   F 3 26  ? 16.077  -40.407 23.277  1.00 29.41  ?  26  THR   F CA    1 
ATOM   4172 C C     . THR   F 3 26  ? 17.141  -41.069 22.397  1.00 30.13  ?  26  THR   F C     1 
ATOM   4173 O O     . THR   F 3 26  ? 18.236  -41.314 22.892  1.00 30.97  ?  26  THR   F O     1 
ATOM   4174 C CB    . THR   F 3 26  ? 15.452  -41.430 24.237  1.00 29.41  ?  26  THR   F CB    1 
ATOM   4175 O OG1   . THR   F 3 26  ? 14.663  -42.350 23.474  1.00 28.89  ?  26  THR   F OG1   1 
ATOM   4176 C CG2   . THR   F 3 26  ? 14.597  -40.777 25.312  1.00 28.41  ?  26  THR   F CG2   1 
ATOM   4177 N N     . ASN   F 3 27  ? 16.820  -41.391 21.133  1.00 30.09  ?  27  ASN   F N     1 
ATOM   4178 C CA    . ASN   F 3 27  ? 17.801  -41.910 20.189  1.00 32.31  ?  27  ASN   F CA    1 
ATOM   4179 C C     . ASN   F 3 27  ? 18.469  -40.819 19.352  1.00 33.90  ?  27  ASN   F C     1 
ATOM   4180 O O     . ASN   F 3 27  ? 19.118  -41.180 18.387  1.00 37.59  ?  27  ASN   F O     1 
ATOM   4181 C CB    . ASN   F 3 27  ? 17.174  -43.020 19.344  1.00 30.26  ?  27  ASN   F CB    1 
ATOM   4182 C CG    . ASN   F 3 27  ? 16.922  -44.258 20.152  1.00 28.74  ?  27  ASN   F CG    1 
ATOM   4183 O OD1   . ASN   F 3 27  ? 17.854  -45.013 20.397  1.00 30.18  ?  27  ASN   F OD1   1 
ATOM   4184 N ND2   . ASN   F 3 27  ? 15.702  -44.487 20.574  1.00 26.41  ?  27  ASN   F ND2   1 
ATOM   4185 N N     . GLY   F 3 28  ? 18.340  -39.519 19.679  1.00 35.18  ?  28  GLY   F N     1 
ATOM   4186 C CA    . GLY   F 3 28  ? 19.065  -38.456 19.002  1.00 35.89  ?  28  GLY   F CA    1 
ATOM   4187 C C     . GLY   F 3 28  ? 18.725  -38.268 17.520  1.00 36.34  ?  28  GLY   F C     1 
ATOM   4188 O O     . GLY   F 3 28  ? 19.599  -37.831 16.772  1.00 38.33  ?  28  GLY   F O     1 
ATOM   4189 N N     . ILE   F 3 29  ? 17.479  -38.550 17.104  1.00 34.26  ?  29  ILE   F N     1 
ATOM   4190 C CA    . ILE   F 3 29  ? 17.012  -38.280 15.749  1.00 35.43  ?  29  ILE   F CA    1 
ATOM   4191 C C     . ILE   F 3 29  ? 16.551  -36.820 15.675  1.00 36.48  ?  29  ILE   F C     1 
ATOM   4192 O O     . ILE   F 3 29  ? 16.739  -36.148 14.659  1.00 37.00  ?  29  ILE   F O     1 
ATOM   4193 C CB    . ILE   F 3 29  ? 15.951  -39.320 15.319  1.00 33.83  ?  29  ILE   F CB    1 
ATOM   4194 C CG1   . ILE   F 3 29  ? 16.600  -40.733 15.212  1.00 34.58  ?  29  ILE   F CG1   1 
ATOM   4195 C CG2   . ILE   F 3 29  ? 15.271  -38.917 13.999  1.00 34.43  ?  29  ILE   F CG2   1 
ATOM   4196 C CD1   . ILE   F 3 29  ? 15.634  -41.905 15.241  1.00 34.56  ?  29  ILE   F CD1   1 
ATOM   4197 N N     . THR   F 3 30  ? 15.912  -36.349 16.750  1.00 35.72  ?  30  THR   F N     1 
ATOM   4198 C CA    . THR   F 3 30  ? 15.550  -34.953 16.940  1.00 35.72  ?  30  THR   F CA    1 
ATOM   4199 C C     . THR   F 3 30  ? 16.574  -34.323 17.883  1.00 36.96  ?  30  THR   F C     1 
ATOM   4200 O O     . THR   F 3 30  ? 17.259  -35.023 18.603  1.00 34.16  ?  30  THR   F O     1 
ATOM   4201 C CB    . THR   F 3 30  ? 14.139  -34.852 17.518  1.00 34.22  ?  30  THR   F CB    1 
ATOM   4202 O OG1   . THR   F 3 30  ? 14.272  -35.395 18.825  1.00 35.20  ?  30  THR   F OG1   1 
ATOM   4203 C CG2   . THR   F 3 30  ? 13.127  -35.688 16.761  1.00 33.54  ?  30  THR   F CG2   1 
ATOM   4204 N N     . LYS   F 3 31  ? 16.667  -32.989 17.833  1.00 41.31  ?  31  LYS   F N     1 
ATOM   4205 C CA    . LYS   F 3 31  ? 17.625  -32.200 18.595  1.00 43.79  ?  31  LYS   F CA    1 
ATOM   4206 C C     . LYS   F 3 31  ? 16.856  -30.998 19.138  1.00 43.92  ?  31  LYS   F C     1 
ATOM   4207 O O     . LYS   F 3 31  ? 16.876  -29.938 18.508  1.00 44.85  ?  31  LYS   F O     1 
ATOM   4208 C CB    . LYS   F 3 31  ? 18.801  -31.900 17.654  1.00 45.59  ?  31  LYS   F CB    1 
ATOM   4209 C CG    . LYS   F 3 31  ? 19.704  -33.082 17.297  1.00 45.90  ?  31  LYS   F CG    1 
ATOM   4210 C CD    . LYS   F 3 31  ? 20.435  -33.700 18.482  1.00 46.53  ?  31  LYS   F CD    1 
ATOM   4211 C CE    . LYS   F 3 31  ? 21.634  -34.510 18.121  1.00 48.66  ?  31  LYS   F CE    1 
ATOM   4212 N NZ    . LYS   F 3 31  ? 21.977  -35.484 19.172  1.00 48.33  1  31  LYS   F NZ    1 
ATOM   4213 N N     . PRO   F 3 32  ? 16.064  -31.140 20.240  1.00 42.27  ?  32  PRO   F N     1 
ATOM   4214 C CA    . PRO   F 3 32  ? 15.337  -30.009 20.814  1.00 42.83  ?  32  PRO   F CA    1 
ATOM   4215 C C     . PRO   F 3 32  ? 16.254  -28.908 21.361  1.00 45.12  ?  32  PRO   F C     1 
ATOM   4216 O O     . PRO   F 3 32  ? 17.301  -29.207 21.957  1.00 47.34  ?  32  PRO   F O     1 
ATOM   4217 C CB    . PRO   F 3 32  ? 14.477  -30.600 21.911  1.00 41.48  ?  32  PRO   F CB    1 
ATOM   4218 C CG    . PRO   F 3 32  ? 14.507  -32.081 21.653  1.00 39.96  ?  32  PRO   F CG    1 
ATOM   4219 C CD    . PRO   F 3 32  ? 15.801  -32.377 20.985  1.00 41.39  ?  32  PRO   F CD    1 
ATOM   4220 N N     . CYS   F 3 33  ? 15.865  -27.654 21.074  1.00 44.54  ?  33  CYS   F N     1 
ATOM   4221 C CA    . CYS   F 3 33  ? 16.471  -26.456 21.618  1.00 46.06  ?  33  CYS   F CA    1 
ATOM   4222 C C     . CYS   F 3 33  ? 15.371  -25.650 22.296  1.00 45.30  ?  33  CYS   F C     1 
ATOM   4223 O O     . CYS   F 3 33  ? 14.365  -25.394 21.626  1.00 45.60  ?  33  CYS   F O     1 
ATOM   4224 C CB    . CYS   F 3 33  ? 17.091  -25.661 20.480  1.00 47.69  ?  33  CYS   F CB    1 
ATOM   4225 S SG    . CYS   F 3 33  ? 18.012  -24.216 21.063  1.00 50.49  ?  33  CYS   F SG    1 
ATOM   4226 N N     . ILE   F 3 34  ? 15.542  -25.317 23.590  1.00 45.63  ?  34  ILE   F N     1 
ATOM   4227 C CA    . ILE   F 3 34  ? 14.615  -24.462 24.327  1.00 47.97  ?  34  ILE   F CA    1 
ATOM   4228 C C     . ILE   F 3 34  ? 15.213  -23.057 24.411  1.00 53.15  ?  34  ILE   F C     1 
ATOM   4229 O O     . ILE   F 3 34  ? 16.344  -22.922 24.904  1.00 54.04  ?  34  ILE   F O     1 
ATOM   4230 C CB    . ILE   F 3 34  ? 14.347  -24.997 25.749  1.00 46.69  ?  34  ILE   F CB    1 
ATOM   4231 C CG1   . ILE   F 3 34  ? 13.847  -26.484 25.731  1.00 44.16  ?  34  ILE   F CG1   1 
ATOM   4232 C CG2   . ILE   F 3 34  ? 13.395  -24.064 26.506  1.00 47.56  ?  34  ILE   F CG2   1 
ATOM   4233 C CD1   . ILE   F 3 34  ? 12.648  -26.786 24.840  1.00 41.15  ?  34  ILE   F CD1   1 
ATOM   4234 N N     . VAL   F 3 35  ? 14.431  -22.035 24.006  1.00 55.26  ?  35  VAL   F N     1 
ATOM   4235 C CA    . VAL   F 3 35  ? 14.817  -20.643 24.176  1.00 59.19  ?  35  VAL   F CA    1 
ATOM   4236 C C     . VAL   F 3 35  ? 13.751  -19.960 25.044  1.00 59.03  ?  35  VAL   F C     1 
ATOM   4237 O O     . VAL   F 3 35  ? 12.559  -19.973 24.709  1.00 55.86  ?  35  VAL   F O     1 
ATOM   4238 C CB    . VAL   F 3 35  ? 15.147  -19.885 22.872  1.00 63.43  ?  35  VAL   F CB    1 
ATOM   4239 C CG1   . VAL   F 3 35  ? 16.383  -20.462 22.195  1.00 65.24  ?  35  VAL   F CG1   1 
ATOM   4240 C CG2   . VAL   F 3 35  ? 14.012  -19.869 21.884  1.00 60.91  ?  35  VAL   F CG2   1 
ATOM   4241 N N     . SER   F 3 36  ? 14.203  -19.453 26.211  1.00 60.69  ?  36  SER   F N     1 
ATOM   4242 C CA    . SER   F 3 36  ? 13.452  -18.569 27.087  1.00 62.62  ?  36  SER   F CA    1 
ATOM   4243 C C     . SER   F 3 36  ? 13.792  -17.115 26.743  1.00 66.91  ?  36  SER   F C     1 
ATOM   4244 O O     . SER   F 3 36  ? 14.611  -16.855 25.849  1.00 69.23  ?  36  SER   F O     1 
ATOM   4245 C CB    . SER   F 3 36  ? 13.762  -18.902 28.552  1.00 61.99  ?  36  SER   F CB    1 
ATOM   4246 O OG    . SER   F 3 36  ? 15.096  -18.547 28.910  1.00 63.51  ?  36  SER   F OG    1 
ATOM   4247 N N     . THR   F 3 37  ? 13.201  -16.173 27.512  1.00 69.08  ?  37  THR   F N     1 
ATOM   4248 C CA    . THR   F 3 37  ? 13.571  -14.757 27.473  1.00 71.90  ?  37  THR   F CA    1 
ATOM   4249 C C     . THR   F 3 37  ? 15.029  -14.518 27.891  1.00 75.15  ?  37  THR   F C     1 
ATOM   4250 O O     . THR   F 3 37  ? 15.607  -13.545 27.406  1.00 78.57  ?  37  THR   F O     1 
ATOM   4251 C CB    . THR   F 3 37  ? 12.620  -13.893 28.305  1.00 71.67  ?  37  THR   F CB    1 
ATOM   4252 O OG1   . THR   F 3 37  ? 12.603  -14.361 29.648  1.00 70.94  ?  37  THR   F OG1   1 
ATOM   4253 C CG2   . THR   F 3 37  ? 11.195  -13.908 27.785  1.00 69.34  ?  37  THR   F CG2   1 
ATOM   4254 N N     . GLU   F 3 38  ? 15.622  -15.405 28.724  1.00 74.18  ?  38  GLU   F N     1 
ATOM   4255 C CA    . GLU   F 3 38  ? 16.942  -15.215 29.315  1.00 75.32  ?  38  GLU   F CA    1 
ATOM   4256 C C     . GLU   F 3 38  ? 18.009  -16.210 28.847  1.00 74.97  ?  38  GLU   F C     1 
ATOM   4257 O O     . GLU   F 3 38  ? 19.177  -15.869 28.980  1.00 76.14  ?  38  GLU   F O     1 
ATOM   4258 C CB    . GLU   F 3 38  ? 16.790  -15.333 30.825  1.00 75.20  ?  38  GLU   F CB    1 
ATOM   4259 C CG    . GLU   F 3 38  ? 15.833  -14.309 31.431  1.00 76.73  ?  38  GLU   F CG    1 
ATOM   4260 C CD    . GLU   F 3 38  ? 15.780  -14.280 32.952  1.00 77.64  ?  38  GLU   F CD    1 
ATOM   4261 O OE1   . GLU   F 3 38  ? 16.477  -15.073 33.623  1.00 76.86  ?  38  GLU   F OE1   1 
ATOM   4262 O OE2   . GLU   F 3 38  ? 14.997  -13.460 33.469  1.00 78.40  -1 38  GLU   F OE2   1 
ATOM   4263 N N     . ASN   F 3 39  ? 17.652  -17.421 28.354  1.00 73.34  ?  39  ASN   F N     1 
ATOM   4264 C CA    . ASN   F 3 39  ? 18.607  -18.509 28.114  1.00 72.51  ?  39  ASN   F CA    1 
ATOM   4265 C C     . ASN   F 3 39  ? 18.202  -19.364 26.915  1.00 69.95  ?  39  ASN   F C     1 
ATOM   4266 O O     . ASN   F 3 39  ? 17.009  -19.559 26.691  1.00 65.30  ?  39  ASN   F O     1 
ATOM   4267 C CB    . ASN   F 3 39  ? 18.690  -19.462 29.301  1.00 72.44  ?  39  ASN   F CB    1 
ATOM   4268 C CG    . ASN   F 3 39  ? 19.394  -18.834 30.482  1.00 75.22  ?  39  ASN   F CG    1 
ATOM   4269 O OD1   . ASN   F 3 39  ? 20.598  -18.590 30.420  1.00 76.86  ?  39  ASN   F OD1   1 
ATOM   4270 N ND2   . ASN   F 3 39  ? 18.676  -18.567 31.561  1.00 75.83  ?  39  ASN   F ND2   1 
ATOM   4271 N N     . VAL   F 3 40  ? 19.216  -19.858 26.176  1.00 71.62  ?  40  VAL   F N     1 
ATOM   4272 C CA    . VAL   F 3 40  ? 19.071  -20.877 25.146  1.00 69.14  ?  40  VAL   F CA    1 
ATOM   4273 C C     . VAL   F 3 40  ? 19.651  -22.169 25.738  1.00 66.39  ?  40  VAL   F C     1 
ATOM   4274 O O     . VAL   F 3 40  ? 20.813  -22.169 26.149  1.00 67.96  ?  40  VAL   F O     1 
ATOM   4275 C CB    . VAL   F 3 40  ? 19.789  -20.487 23.829  1.00 72.10  ?  40  VAL   F CB    1 
ATOM   4276 C CG1   . VAL   F 3 40  ? 19.716  -21.592 22.777  1.00 69.23  ?  40  VAL   F CG1   1 
ATOM   4277 C CG2   . VAL   F 3 40  ? 19.398  -19.101 23.297  1.00 75.33  ?  40  VAL   F CG2   1 
ATOM   4278 N N     . TYR   F 3 41  ? 18.837  -23.246 25.797  1.00 62.59  ?  41  TYR   F N     1 
ATOM   4279 C CA    . TYR   F 3 41  ? 19.246  -24.572 26.248  1.00 59.95  ?  41  TYR   F CA    1 
ATOM   4280 C C     . TYR   F 3 41  ? 19.496  -25.411 24.995  1.00 60.81  ?  41  TYR   F C     1 
ATOM   4281 O O     . TYR   F 3 41  ? 18.532  -25.859 24.349  1.00 55.70  ?  41  TYR   F O     1 
ATOM   4282 C CB    . TYR   F 3 41  ? 18.211  -25.176 27.198  1.00 56.57  ?  41  TYR   F CB    1 
ATOM   4283 C CG    . TYR   F 3 41  ? 17.947  -24.305 28.421  1.00 56.42  ?  41  TYR   F CG    1 
ATOM   4284 C CD1   . TYR   F 3 41  ? 16.996  -23.282 28.375  1.00 56.38  ?  41  TYR   F CD1   1 
ATOM   4285 C CD2   . TYR   F 3 41  ? 18.670  -24.473 29.607  1.00 57.18  ?  41  TYR   F CD2   1 
ATOM   4286 C CE1   . TYR   F 3 41  ? 16.749  -22.469 29.473  1.00 57.38  ?  41  TYR   F CE1   1 
ATOM   4287 C CE2   . TYR   F 3 41  ? 18.437  -23.664 30.717  1.00 58.50  ?  41  TYR   F CE2   1 
ATOM   4288 C CZ    . TYR   F 3 41  ? 17.478  -22.656 30.641  1.00 58.97  ?  41  TYR   F CZ    1 
ATOM   4289 O OH    . TYR   F 3 41  ? 17.188  -21.847 31.689  1.00 61.35  ?  41  TYR   F OH    1 
ATOM   4290 N N     . THR   F 3 42  ? 20.789  -25.592 24.654  1.00 62.99  ?  42  THR   F N     1 
ATOM   4291 C CA    . THR   F 3 42  ? 21.183  -26.196 23.388  1.00 62.32  ?  42  THR   F CA    1 
ATOM   4292 C C     . THR   F 3 42  ? 20.905  -27.705 23.409  1.00 59.56  ?  42  THR   F C     1 
ATOM   4293 O O     . THR   F 3 42  ? 20.930  -28.294 24.486  1.00 57.72  ?  42  THR   F O     1 
ATOM   4294 C CB    . THR   F 3 42  ? 22.660  -25.941 23.061  1.00 63.72  ?  42  THR   F CB    1 
ATOM   4295 O OG1   . THR   F 3 42  ? 23.509  -26.607 23.985  1.00 63.91  ?  42  THR   F OG1   1 
ATOM   4296 C CG2   . THR   F 3 42  ? 23.024  -24.476 23.044  1.00 65.97  ?  42  THR   F CG2   1 
ATOM   4297 N N     . PRO   F 3 43  ? 20.706  -28.382 22.241  1.00 59.55  ?  43  PRO   F N     1 
ATOM   4298 C CA    . PRO   F 3 43  ? 20.728  -29.848 22.172  1.00 57.92  ?  43  PRO   F CA    1 
ATOM   4299 C C     . PRO   F 3 43  ? 22.080  -30.505 22.481  1.00 60.78  ?  43  PRO   F C     1 
ATOM   4300 O O     . PRO   F 3 43  ? 22.084  -31.698 22.780  1.00 60.12  ?  43  PRO   F O     1 
ATOM   4301 C CB    . PRO   F 3 43  ? 20.249  -30.174 20.759  1.00 57.00  ?  43  PRO   F CB    1 
ATOM   4302 C CG    . PRO   F 3 43  ? 20.486  -28.896 19.972  1.00 60.01  ?  43  PRO   F CG    1 
ATOM   4303 C CD    . PRO   F 3 43  ? 20.428  -27.760 20.930  1.00 60.04  ?  43  PRO   F CD    1 
ATOM   4304 N N     . ASP   F 3 44  ? 23.199  -29.750 22.408  1.00 64.52  ?  44  ASP   F N     1 
ATOM   4305 C CA    . ASP   F 3 44  ? 24.525  -30.161 22.883  1.00 68.02  ?  44  ASP   F CA    1 
ATOM   4306 C C     . ASP   F 3 44  ? 24.708  -29.981 24.405  1.00 68.17  ?  44  ASP   F C     1 
ATOM   4307 O O     . ASP   F 3 44  ? 25.847  -30.056 24.870  1.00 71.64  ?  44  ASP   F O     1 
ATOM   4308 C CB    . ASP   F 3 44  ? 25.639  -29.497 22.063  1.00 66.54  ?  44  ASP   F CB    1 
ATOM   4309 N N     . ASN   F 3 45  ? 23.635  -29.705 25.186  1.00 64.37  ?  45  ASN   F N     1 
ATOM   4310 C CA    . ASN   F 3 45  ? 23.583  -29.806 26.648  1.00 65.07  ?  45  ASN   F CA    1 
ATOM   4311 C C     . ASN   F 3 45  ? 24.203  -28.573 27.311  1.00 66.61  ?  45  ASN   F C     1 
ATOM   4312 O O     . ASN   F 3 45  ? 24.691  -28.703 28.425  1.00 67.69  ?  45  ASN   F O     1 
ATOM   4313 C CB    . ASN   F 3 45  ? 24.143  -31.146 27.166  1.00 67.61  ?  45  ASN   F CB    1 
ATOM   4314 C CG    . ASN   F 3 45  ? 23.568  -31.663 28.475  1.00 69.74  ?  45  ASN   F CG    1 
ATOM   4315 O OD1   . ASN   F 3 45  ? 24.313  -31.958 29.420  1.00 69.66  ?  45  ASN   F OD1   1 
ATOM   4316 N ND2   . ASN   F 3 45  ? 22.268  -31.922 28.523  1.00 72.66  ?  45  ASN   F ND2   1 
ATOM   4317 N N     . ALA   F 3 46  ? 24.102  -27.372 26.697  1.00 66.94  ?  46  ALA   F N     1 
ATOM   4318 C CA    . ALA   F 3 46  ? 24.694  -26.133 27.204  1.00 68.53  ?  46  ALA   F CA    1 
ATOM   4319 C C     . ALA   F 3 46  ? 23.600  -25.077 27.396  1.00 66.68  ?  46  ALA   F C     1 
ATOM   4320 O O     . ALA   F 3 46  ? 22.692  -24.984 26.565  1.00 63.42  ?  46  ALA   F O     1 
ATOM   4321 C CB    . ALA   F 3 46  ? 25.786  -25.638 26.261  1.00 70.81  ?  46  ALA   F CB    1 
ATOM   4322 N N     . THR   F 3 47  ? 23.680  -24.327 28.515  1.00 68.33  ?  47  THR   F N     1 
ATOM   4323 C CA    . THR   F 3 47  ? 22.838  -23.169 28.806  1.00 69.66  ?  47  THR   F CA    1 
ATOM   4324 C C     . THR   F 3 47  ? 23.596  -21.919 28.341  1.00 72.34  ?  47  THR   F C     1 
ATOM   4325 O O     . THR   F 3 47  ? 24.586  -21.593 28.984  1.00 75.38  ?  47  THR   F O     1 
ATOM   4326 C CB    . THR   F 3 47  ? 22.561  -23.133 30.318  1.00 69.79  ?  47  THR   F CB    1 
ATOM   4327 O OG1   . THR   F 3 47  ? 21.927  -24.340 30.718  1.00 68.23  ?  47  THR   F OG1   1 
ATOM   4328 C CG2   . THR   F 3 47  ? 21.651  -21.995 30.738  1.00 70.53  ?  47  THR   F CG2   1 
ATOM   4329 N N     . VAL   F 3 48  ? 23.183  -21.260 27.229  1.00 72.50  ?  48  VAL   F N     1 
ATOM   4330 C CA    . VAL   F 3 48  ? 23.818  -20.027 26.742  1.00 75.57  ?  48  VAL   F CA    1 
ATOM   4331 C C     . VAL   F 3 48  ? 22.880  -18.852 27.094  1.00 76.43  ?  48  VAL   F C     1 
ATOM   4332 O O     . VAL   F 3 48  ? 21.743  -18.794 26.588  1.00 71.14  ?  48  VAL   F O     1 
ATOM   4333 C CB    . VAL   F 3 48  ? 24.368  -20.006 25.292  1.00 75.39  ?  48  VAL   F CB    1 
ATOM   4334 C CG1   . VAL   F 3 48  ? 25.549  -20.964 25.132  1.00 76.02  ?  48  VAL   F CG1   1 
ATOM   4335 C CG2   . VAL   F 3 48  ? 23.343  -20.294 24.223  1.00 72.29  ?  48  VAL   F CG2   1 
ATOM   4336 N N     . PRO   F 3 49  ? 23.271  -17.946 28.052  1.00 80.79  ?  49  PRO   F N     1 
ATOM   4337 C CA    . PRO   F 3 49  ? 22.488  -16.747 28.362  1.00 83.78  ?  49  PRO   F CA    1 
ATOM   4338 C C     . PRO   F 3 49  ? 22.331  -15.789 27.185  1.00 86.41  ?  49  PRO   F C     1 
ATOM   4339 O O     . PRO   F 3 49  ? 23.322  -15.494 26.532  1.00 91.41  ?  49  PRO   F O     1 
ATOM   4340 C CB    . PRO   F 3 49  ? 23.232  -16.043 29.502  1.00 86.21  ?  49  PRO   F CB    1 
ATOM   4341 C CG    . PRO   F 3 49  ? 24.205  -17.066 30.014  1.00 85.96  ?  49  PRO   F CG    1 
ATOM   4342 C CD    . PRO   F 3 49  ? 24.449  -18.059 28.934  1.00 83.23  ?  49  PRO   F CD    1 
ATOM   4343 N N     . HIS   F 3 50  ? 21.089  -15.363 26.905  1.00 86.68  ?  50  HIS   F N     1 
ATOM   4344 C CA    . HIS   F 3 50  ? 20.802  -14.266 25.990  1.00 89.60  ?  50  HIS   F CA    1 
ATOM   4345 C C     . HIS   F 3 50  ? 19.530  -13.560 26.472  1.00 90.41  ?  50  HIS   F C     1 
ATOM   4346 O O     . HIS   F 3 50  ? 18.461  -14.160 26.412  1.00 82.52  ?  50  HIS   F O     1 
ATOM   4347 C CB    . HIS   F 3 50  ? 20.698  -14.798 24.554  1.00 89.96  ?  50  HIS   F CB    1 
ATOM   4348 C CG    . HIS   F 3 50  ? 21.010  -13.814 23.466  1.00 93.57  ?  50  HIS   F CG    1 
ATOM   4349 N ND1   . HIS   F 3 50  ? 22.273  -13.775 22.915  1.00 96.75  ?  50  HIS   F ND1   1 
ATOM   4350 C CD2   . HIS   F 3 50  ? 20.282  -12.909 22.786  1.00 95.53  ?  50  HIS   F CD2   1 
ATOM   4351 C CE1   . HIS   F 3 50  ? 22.308  -12.857 21.954  1.00 100.09 ?  50  HIS   F CE1   1 
ATOM   4352 N NE2   . HIS   F 3 50  ? 21.105  -12.325 21.853  1.00 99.28  ?  50  HIS   F NE2   1 
ATOM   4353 N N     . LYS   F 3 51  ? 19.677  -12.311 26.959  1.00 98.59  ?  51  LYS   F N     1 
ATOM   4354 C CA    . LYS   F 3 51  ? 18.576  -11.457 27.400  1.00 102.40 ?  51  LYS   F CA    1 
ATOM   4355 C C     . LYS   F 3 51  ? 18.191  -10.591 26.198  1.00 105.43 ?  51  LYS   F C     1 
ATOM   4356 O O     . LYS   F 3 51  ? 18.926  -9.667  25.835  1.00 113.48 ?  51  LYS   F O     1 
ATOM   4357 C CB    . LYS   F 3 51  ? 18.904  -10.638 28.664  1.00 102.67 ?  51  LYS   F CB    1 
ATOM   4358 N N     . GLN   F 3 52  ? 17.035  -10.896 25.589  1.00 101.94 ?  52  GLN   F N     1 
ATOM   4359 C CA    . GLN   F 3 52  ? 16.746  -10.523 24.206  1.00 103.65 ?  52  GLN   F CA    1 
ATOM   4360 C C     . GLN   F 3 52  ? 16.188  -9.096  24.165  1.00 110.53 ?  52  GLN   F C     1 
ATOM   4361 O O     . GLN   F 3 52  ? 15.514  -8.690  25.111  1.00 115.33 ?  52  GLN   F O     1 
ATOM   4362 C CB    . GLN   F 3 52  ? 15.786  -11.541 23.584  1.00 98.68  ?  52  GLN   F CB    1 
ATOM   4363 C CG    . GLN   F 3 52  ? 16.107  -12.998 23.920  1.00 92.91  ?  52  GLN   F CG    1 
ATOM   4364 C CD    . GLN   F 3 52  ? 15.704  -13.976 22.844  1.00 88.09  ?  52  GLN   F CD    1 
ATOM   4365 O OE1   . GLN   F 3 52  ? 14.666  -13.826 22.182  1.00 86.58  ?  52  GLN   F OE1   1 
ATOM   4366 N NE2   . GLN   F 3 52  ? 16.559  -14.971 22.651  1.00 84.00  ?  52  GLN   F NE2   1 
ATOM   4367 N N     . GLY   F 3 53  ? 16.419  -8.362  23.050  1.00 111.96 ?  53  GLY   F N     1 
ATOM   4368 C CA    . GLY   F 3 53  ? 15.914  -7.002  22.831  1.00 114.89 ?  53  GLY   F CA    1 
ATOM   4369 C C     . GLY   F 3 53  ? 14.437  -7.008  22.418  1.00 110.26 ?  53  GLY   F C     1 
ATOM   4370 O O     . GLY   F 3 53  ? 13.637  -7.652  23.078  1.00 111.34 ?  53  GLY   F O     1 
ATOM   4371 N N     . SER   F 3 54  ? 14.048  -6.233  21.391  1.00 104.77 ?  54  SER   F N     1 
ATOM   4372 C CA    . SER   F 3 54  ? 13.073  -6.699  20.407  1.00 96.81  ?  54  SER   F CA    1 
ATOM   4373 C C     . SER   F 3 54  ? 13.731  -6.776  19.031  1.00 96.70  ?  54  SER   F C     1 
ATOM   4374 O O     . SER   F 3 54  ? 13.030  -6.677  18.026  1.00 95.82  ?  54  SER   F O     1 
ATOM   4375 C CB    . SER   F 3 54  ? 11.781  -5.893  20.389  1.00 95.59  ?  54  SER   F CB    1 
ATOM   4376 O OG    . SER   F 3 54  ? 10.828  -6.491  19.509  1.00 90.52  ?  54  SER   F OG    1 
ATOM   4377 N N     . ASP   F 3 55  ? 15.056  -7.035  18.988  1.00 97.54  ?  55  ASP   F N     1 
ATOM   4378 C CA    . ASP   F 3 55  ? 15.739  -7.530  17.797  1.00 99.23  ?  55  ASP   F CA    1 
ATOM   4379 C C     . ASP   F 3 55  ? 15.499  -9.043  17.696  1.00 92.34  ?  55  ASP   F C     1 
ATOM   4380 O O     . ASP   F 3 55  ? 15.693  -9.734  18.694  1.00 90.55  ?  55  ASP   F O     1 
ATOM   4381 C CB    . ASP   F 3 55  ? 17.199  -7.078  17.816  1.00 105.03 ?  55  ASP   F CB    1 
ATOM   4382 C CG    . ASP   F 3 55  ? 18.057  -7.501  16.629  1.00 107.26 ?  55  ASP   F CG    1 
ATOM   4383 O OD1   . ASP   F 3 55  ? 18.466  -8.686  16.600  1.00 108.13 -1 55  ASP   F OD1   1 
ATOM   4384 O OD2   . ASP   F 3 55  ? 18.309  -6.650  15.741  1.00 109.51 ?  55  ASP   F OD2   1 
ATOM   4385 N N     . TYR   F 3 56  ? 15.038  -9.538  16.523  1.00 89.75  ?  56  TYR   F N     1 
ATOM   4386 C CA    . TYR   F 3 56  ? 14.947  -10.965 16.215  1.00 85.35  ?  56  TYR   F CA    1 
ATOM   4387 C C     . TYR   F 3 56  ? 16.360  -11.561 16.127  1.00 86.01  ?  56  TYR   F C     1 
ATOM   4388 O O     . TYR   F 3 56  ? 17.166  -11.036 15.361  1.00 85.60  ?  56  TYR   F O     1 
ATOM   4389 C CB    . TYR   F 3 56  ? 14.185  -11.220 14.898  1.00 83.88  ?  56  TYR   F CB    1 
ATOM   4390 C CG    . TYR   F 3 56  ? 12.688  -11.495 14.991  1.00 81.31  ?  56  TYR   F CG    1 
ATOM   4391 C CD1   . TYR   F 3 56  ? 12.213  -12.520 15.827  1.00 77.99  ?  56  TYR   F CD1   1 
ATOM   4392 C CD2   . TYR   F 3 56  ? 11.744  -10.798 14.217  1.00 81.00  ?  56  TYR   F CD2   1 
ATOM   4393 C CE1   . TYR   F 3 56  ? 10.856  -12.811 15.927  1.00 74.70  ?  56  TYR   F CE1   1 
ATOM   4394 C CE2   . TYR   F 3 56  ? 10.377  -11.068 14.332  1.00 80.31  ?  56  TYR   F CE2   1 
ATOM   4395 C CZ    . TYR   F 3 56  ? 9.935   -12.099 15.167  1.00 77.41  ?  56  TYR   F CZ    1 
ATOM   4396 O OH    . TYR   F 3 56  ? 8.615   -12.418 15.313  1.00 74.70  ?  56  TYR   F OH    1 
ATOM   4397 N N     . VAL   F 3 57  ? 16.638  -12.666 16.859  1.00 84.58  ?  57  VAL   F N     1 
ATOM   4398 C CA    . VAL   F 3 57  ? 17.980  -13.250 16.964  1.00 85.90  ?  57  VAL   F CA    1 
ATOM   4399 C C     . VAL   F 3 57  ? 17.928  -14.684 16.411  1.00 84.29  ?  57  VAL   F C     1 
ATOM   4400 O O     . VAL   F 3 57  ? 17.014  -15.430 16.779  1.00 80.47  ?  57  VAL   F O     1 
ATOM   4401 C CB    . VAL   F 3 57  ? 18.582  -13.224 18.392  1.00 86.69  ?  57  VAL   F CB    1 
ATOM   4402 C CG1   . VAL   F 3 57  ? 20.105  -13.332 18.352  1.00 87.90  ?  57  VAL   F CG1   1 
ATOM   4403 C CG2   . VAL   F 3 57  ? 18.175  -12.000 19.210  1.00 89.08  ?  57  VAL   F CG2   1 
ATOM   4404 N N     . LEU   F 3 58  ? 18.920  -15.064 15.568  1.00 84.19  ?  58  LEU   F N     1 
ATOM   4405 C CA    . LEU   F 3 58  ? 18.972  -16.362 14.897  1.00 83.56  ?  58  LEU   F CA    1 
ATOM   4406 C C     . LEU   F 3 58  ? 19.285  -17.446 15.942  1.00 81.75  ?  58  LEU   F C     1 
ATOM   4407 O O     . LEU   F 3 58  ? 20.377  -17.441 16.515  1.00 86.86  ?  58  LEU   F O     1 
ATOM   4408 C CB    . LEU   F 3 58  ? 20.004  -16.359 13.756  1.00 85.36  ?  58  LEU   F CB    1 
ATOM   4409 C CG    . LEU   F 3 58  ? 20.104  -17.622 12.879  1.00 83.37  ?  58  LEU   F CG    1 
ATOM   4410 C CD1   . LEU   F 3 58  ? 18.937  -17.742 11.906  1.00 82.79  ?  58  LEU   F CD1   1 
ATOM   4411 C CD2   . LEU   F 3 58  ? 21.425  -17.705 12.130  1.00 85.93  ?  58  LEU   F CD2   1 
ATOM   4412 N N     . VAL   F 3 59  ? 18.310  -18.342 16.201  1.00 78.37  ?  59  VAL   F N     1 
ATOM   4413 C CA    . VAL   F 3 59  ? 18.453  -19.449 17.143  1.00 73.63  ?  59  VAL   F CA    1 
ATOM   4414 C C     . VAL   F 3 59  ? 18.759  -20.744 16.402  1.00 67.80  ?  59  VAL   F C     1 
ATOM   4415 O O     . VAL   F 3 59  ? 19.566  -21.515 16.907  1.00 67.41  ?  59  VAL   F O     1 
ATOM   4416 C CB    . VAL   F 3 59  ? 17.279  -19.583 18.124  1.00 72.37  ?  59  VAL   F CB    1 
ATOM   4417 C CG1   . VAL   F 3 59  ? 17.345  -18.439 19.118  1.00 75.14  ?  59  VAL   F CG1   1 
ATOM   4418 C CG2   . VAL   F 3 59  ? 15.907  -19.697 17.471  1.00 71.06  ?  59  VAL   F CG2   1 
ATOM   4419 N N     . ALA   F 3 60  ? 18.149  -20.963 15.226  1.00 64.66  ?  60  ALA   F N     1 
ATOM   4420 C CA    . ALA   F 3 60  ? 18.476  -22.097 14.369  1.00 62.13  ?  60  ALA   F CA    1 
ATOM   4421 C C     . ALA   F 3 60  ? 18.370  -21.710 12.899  1.00 60.25  ?  60  ALA   F C     1 
ATOM   4422 O O     . ALA   F 3 60  ? 17.653  -20.773 12.555  1.00 58.94  ?  60  ALA   F O     1 
ATOM   4423 C CB    . ALA   F 3 60  ? 17.565  -23.288 14.700  1.00 58.94  ?  60  ALA   F CB    1 
ATOM   4424 N N     . GLY   F 3 61  ? 19.067  -22.470 12.050  1.00 59.80  ?  61  GLY   F N     1 
ATOM   4425 C CA    . GLY   F 3 61  ? 18.899  -22.346 10.610  1.00 61.47  ?  61  GLY   F CA    1 
ATOM   4426 C C     . GLY   F 3 61  ? 19.934  -23.163 9.848   1.00 62.43  ?  61  GLY   F C     1 
ATOM   4427 O O     . GLY   F 3 61  ? 20.953  -23.555 10.414  1.00 62.94  ?  61  GLY   F O     1 
ATOM   4428 N N     . LEU   F 3 62  ? 19.653  -23.425 8.565   1.00 63.54  ?  62  LEU   F N     1 
ATOM   4429 C CA    . LEU   F 3 62  ? 20.609  -24.090 7.691   1.00 65.19  ?  62  LEU   F CA    1 
ATOM   4430 C C     . LEU   F 3 62  ? 21.727  -23.094 7.337   1.00 68.42  ?  62  LEU   F C     1 
ATOM   4431 O O     . LEU   F 3 62  ? 21.469  -21.896 7.141   1.00 67.26  ?  62  LEU   F O     1 
ATOM   4432 C CB    . LEU   F 3 62  ? 19.924  -24.691 6.462   1.00 65.62  ?  62  LEU   F CB    1 
ATOM   4433 C CG    . LEU   F 3 62  ? 19.154  -25.996 6.711   1.00 62.79  ?  62  LEU   F CG    1 
ATOM   4434 C CD1   . LEU   F 3 62  ? 18.132  -26.291 5.608   1.00 63.17  ?  62  LEU   F CD1   1 
ATOM   4435 C CD2   . LEU   F 3 62  ? 20.108  -27.173 6.850   1.00 63.01  ?  62  LEU   F CD2   1 
ATOM   4436 N N     . ALA   F 3 63  ? 22.970  -23.616 7.288   1.00 70.10  ?  63  ALA   F N     1 
ATOM   4437 C CA    . ALA   F 3 63  ? 24.173  -22.859 6.953   1.00 73.04  ?  63  ALA   F CA    1 
ATOM   4438 C C     . ALA   F 3 63  ? 24.195  -22.510 5.463   1.00 74.94  ?  63  ALA   F C     1 
ATOM   4439 O O     . ALA   F 3 63  ? 24.460  -23.391 4.640   1.00 74.90  ?  63  ALA   F O     1 
ATOM   4440 C CB    . ALA   F 3 63  ? 25.406  -23.670 7.322   1.00 73.79  ?  63  ALA   F CB    1 
ATOM   4441 N N     . GLY   F 3 64  ? 23.929  -21.234 5.119   1.00 76.29  ?  64  GLY   F N     1 
ATOM   4442 C CA    . GLY   F 3 64  ? 23.818  -20.800 3.731   1.00 78.40  ?  64  GLY   F CA    1 
ATOM   4443 C C     . GLY   F 3 64  ? 22.593  -21.355 2.989   1.00 74.95  ?  64  GLY   F C     1 
ATOM   4444 O O     . GLY   F 3 64  ? 22.680  -21.545 1.779   1.00 75.94  ?  64  GLY   F O     1 
ATOM   4445 N N     . ASP   F 3 65  ? 21.486  -21.662 3.697   1.00 70.98  ?  65  ASP   F N     1 
ATOM   4446 C CA    . ASP   F 3 65  ? 20.156  -21.688 3.091   1.00 69.40  ?  65  ASP   F CA    1 
ATOM   4447 C C     . ASP   F 3 65  ? 19.128  -21.286 4.156   1.00 67.18  ?  65  ASP   F C     1 
ATOM   4448 O O     . ASP   F 3 65  ? 18.277  -22.105 4.521   1.00 64.78  ?  65  ASP   F O     1 
ATOM   4449 C CB    . ASP   F 3 65  ? 19.895  -23.006 2.366   1.00 68.61  ?  65  ASP   F CB    1 
ATOM   4450 C CG    . ASP   F 3 65  ? 18.710  -23.065 1.408   1.00 68.07  ?  65  ASP   F CG    1 
ATOM   4451 O OD1   . ASP   F 3 65  ? 17.966  -22.059 1.272   1.00 67.43  ?  65  ASP   F OD1   1 
ATOM   4452 O OD2   . ASP   F 3 65  ? 18.529  -24.147 0.801   1.00 68.02  -1 65  ASP   F OD2   1 
ATOM   4453 N N     . PRO   F 3 66  ? 19.162  -20.025 4.675   1.00 68.43  ?  66  PRO   F N     1 
ATOM   4454 C CA    . PRO   F 3 66  ? 18.206  -19.583 5.684   1.00 66.74  ?  66  PRO   F CA    1 
ATOM   4455 C C     . PRO   F 3 66  ? 16.744  -19.497 5.218   1.00 66.68  ?  66  PRO   F C     1 
ATOM   4456 O O     . PRO   F 3 66  ? 15.843  -19.521 6.055   1.00 65.20  ?  66  PRO   F O     1 
ATOM   4457 C CB    . PRO   F 3 66  ? 18.756  -18.203 6.096   1.00 69.57  ?  66  PRO   F CB    1 
ATOM   4458 C CG    . PRO   F 3 66  ? 20.129  -18.084 5.467   1.00 71.57  ?  66  PRO   F CG    1 
ATOM   4459 C CD    . PRO   F 3 66  ? 20.021  -18.904 4.242   1.00 71.37  ?  66  PRO   F CD    1 
ATOM   4460 N N     . ASN   F 3 67  ? 16.509  -19.330 3.900   1.00 69.08  ?  67  ASN   F N     1 
ATOM   4461 C CA    . ASN   F 3 67  ? 15.169  -19.423 3.321   1.00 68.67  ?  67  ASN   F CA    1 
ATOM   4462 C C     . ASN   F 3 67  ? 14.555  -20.819 3.475   1.00 64.78  ?  67  ASN   F C     1 
ATOM   4463 O O     . ASN   F 3 67  ? 13.334  -20.912 3.625   1.00 62.33  ?  67  ASN   F O     1 
ATOM   4464 C CB    . ASN   F 3 67  ? 15.104  -18.999 1.851   1.00 71.02  ?  67  ASN   F CB    1 
ATOM   4465 C CG    . ASN   F 3 67  ? 14.376  -17.688 1.675   1.00 74.61  ?  67  ASN   F CG    1 
ATOM   4466 O OD1   . ASN   F 3 67  ? 14.978  -16.613 1.834   1.00 77.38  ?  67  ASN   F OD1   1 
ATOM   4467 N ND2   . ASN   F 3 67  ? 13.094  -17.753 1.334   1.00 73.16  ?  67  ASN   F ND2   1 
ATOM   4468 N N     . ARG   F 3 68  ? 15.372  -21.886 3.343   1.00 64.69  ?  68  ARG   F N     1 
ATOM   4469 C CA    . ARG   F 3 68  ? 14.903  -23.259 3.470   1.00 62.23  ?  68  ARG   F CA    1 
ATOM   4470 C C     . ARG   F 3 68  ? 14.527  -23.509 4.924   1.00 59.40  ?  68  ARG   F C     1 
ATOM   4471 O O     . ARG   F 3 68  ? 13.428  -24.001 5.151   1.00 56.50  ?  68  ARG   F O     1 
ATOM   4472 C CB    . ARG   F 3 68  ? 15.896  -24.317 2.966   1.00 64.72  ?  68  ARG   F CB    1 
ATOM   4473 C CG    . ARG   F 3 68  ? 15.542  -25.800 3.063   1.00 63.13  ?  68  ARG   F CG    1 
ATOM   4474 C CD    . ARG   F 3 68  ? 14.305  -26.178 2.225   1.00 63.84  ?  68  ARG   F CD    1 
ATOM   4475 N NE    . ARG   F 3 68  ? 13.907  -27.587 2.354   1.00 61.34  ?  68  ARG   F NE    1 
ATOM   4476 C CZ    . ARG   F 3 68  ? 12.964  -28.205 1.615   1.00 62.00  ?  68  ARG   F CZ    1 
ATOM   4477 N NH1   . ARG   F 3 68  ? 12.184  -27.528 0.779   1.00 63.47  1  68  ARG   F NH1   1 
ATOM   4478 N NH2   . ARG   F 3 68  ? 12.789  -29.513 1.724   1.00 60.24  ?  68  ARG   F NH2   1 
ATOM   4479 N N     . PHE   F 3 69  ? 15.424  -23.172 5.874   1.00 58.81  ?  69  PHE   F N     1 
ATOM   4480 C CA    . PHE   F 3 69  ? 15.074  -23.240 7.287   1.00 56.38  ?  69  PHE   F CA    1 
ATOM   4481 C C     . PHE   F 3 69  ? 15.861  -22.209 8.094   1.00 58.15  ?  69  PHE   F C     1 
ATOM   4482 O O     . PHE   F 3 69  ? 17.093  -22.205 8.024   1.00 59.44  ?  69  PHE   F O     1 
ATOM   4483 C CB    . PHE   F 3 69  ? 15.243  -24.614 7.944   1.00 53.75  ?  69  PHE   F CB    1 
ATOM   4484 C CG    . PHE   F 3 69  ? 14.985  -24.527 9.444   1.00 51.71  ?  69  PHE   F CG    1 
ATOM   4485 C CD1   . PHE   F 3 69  ? 13.719  -24.156 9.914   1.00 49.76  ?  69  PHE   F CD1   1 
ATOM   4486 C CD2   . PHE   F 3 69  ? 16.026  -24.689 10.371  1.00 51.64  ?  69  PHE   F CD2   1 
ATOM   4487 C CE1   . PHE   F 3 69  ? 13.484  -23.997 11.273  1.00 48.36  ?  69  PHE   F CE1   1 
ATOM   4488 C CE2   . PHE   F 3 69  ? 15.780  -24.541 11.733  1.00 50.21  ?  69  PHE   F CE2   1 
ATOM   4489 C CZ    . PHE   F 3 69  ? 14.518  -24.184 12.176  1.00 49.09  ?  69  PHE   F CZ    1 
ATOM   4490 N N     . SER   F 3 70  ? 15.107  -21.397 8.874   1.00 58.53  ?  70  SER   F N     1 
ATOM   4491 C CA    . SER   F 3 70  ? 15.625  -20.506 9.903   1.00 59.96  ?  70  SER   F CA    1 
ATOM   4492 C C     . SER   F 3 70  ? 14.580  -20.265 10.999  1.00 58.13  ?  70  SER   F C     1 
ATOM   4493 O O     . SER   F 3 70  ? 13.368  -20.325 10.730  1.00 56.96  ?  70  SER   F O     1 
ATOM   4494 C CB    . SER   F 3 70  ? 16.070  -19.207 9.301   1.00 62.81  ?  70  SER   F CB    1 
ATOM   4495 O OG    . SER   F 3 70  ? 17.291  -19.416 8.642   1.00 65.70  ?  70  SER   F OG    1 
ATOM   4496 N N     . ALA   F 3 71  ? 15.066  -19.979 12.222  1.00 57.33  ?  71  ALA   F N     1 
ATOM   4497 C CA    . ALA   F 3 71  ? 14.222  -19.717 13.380  1.00 57.32  ?  71  ALA   F CA    1 
ATOM   4498 C C     . ALA   F 3 71  ? 14.779  -18.533 14.172  1.00 59.93  ?  71  ALA   F C     1 
ATOM   4499 O O     . ALA   F 3 71  ? 15.974  -18.526 14.486  1.00 60.69  ?  71  ALA   F O     1 
ATOM   4500 C CB    . ALA   F 3 71  ? 14.123  -20.954 14.241  1.00 54.11  ?  71  ALA   F CB    1 
ATOM   4501 N N     . TYR   F 3 72  ? 13.895  -17.580 14.525  1.00 61.83  ?  72  TYR   F N     1 
ATOM   4502 C CA    . TYR   F 3 72  ? 14.265  -16.348 15.207  1.00 67.78  ?  72  TYR   F CA    1 
ATOM   4503 C C     . TYR   F 3 72  ? 13.334  -16.161 16.404  1.00 67.09  ?  72  TYR   F C     1 
ATOM   4504 O O     . TYR   F 3 72  ? 12.168  -16.587 16.356  1.00 63.05  ?  72  TYR   F O     1 
ATOM   4505 C CB    . TYR   F 3 72  ? 14.231  -15.059 14.358  1.00 72.60  ?  72  TYR   F CB    1 
ATOM   4506 C CG    . TYR   F 3 72  ? 14.954  -15.152 13.017  1.00 77.06  ?  72  TYR   F CG    1 
ATOM   4507 C CD1   . TYR   F 3 72  ? 14.327  -15.752 11.918  1.00 79.60  ?  72  TYR   F CD1   1 
ATOM   4508 C CD2   . TYR   F 3 72  ? 16.267  -14.700 12.845  1.00 80.25  ?  72  TYR   F CD2   1 
ATOM   4509 C CE1   . TYR   F 3 72  ? 14.970  -15.892 10.692  1.00 81.49  ?  72  TYR   F CE1   1 
ATOM   4510 C CE2   . TYR   F 3 72  ? 16.919  -14.828 11.621  1.00 83.09  ?  72  TYR   F CE2   1 
ATOM   4511 C CZ    . TYR   F 3 72  ? 16.267  -15.418 10.536  1.00 83.54  ?  72  TYR   F CZ    1 
ATOM   4512 O OH    . TYR   F 3 72  ? 16.849  -15.583 9.306   1.00 81.39  ?  72  TYR   F OH    1 
ATOM   4513 N N     . THR   F 3 73  ? 13.869  -15.462 17.426  1.00 69.72  ?  73  THR   F N     1 
ATOM   4514 C CA    . THR   F 3 73  ? 13.187  -15.175 18.679  1.00 69.82  ?  73  THR   F CA    1 
ATOM   4515 C C     . THR   F 3 73  ? 13.396  -13.696 19.038  1.00 73.48  ?  73  THR   F C     1 
ATOM   4516 O O     . THR   F 3 73  ? 14.498  -13.146 18.889  1.00 74.15  ?  73  THR   F O     1 
ATOM   4517 C CB    . THR   F 3 73  ? 13.671  -16.119 19.778  1.00 68.64  ?  73  THR   F CB    1 
ATOM   4518 O OG1   . THR   F 3 73  ? 12.888  -15.754 20.909  1.00 70.24  ?  73  THR   F OG1   1 
ATOM   4519 C CG2   . THR   F 3 73  ? 15.176  -16.084 19.988  1.00 69.39  ?  73  THR   F CG2   1 
ATOM   4520 N N     . ARG   F 3 74  ? 12.297  -13.108 19.528  1.00 73.11  ?  74  ARG   F N     1 
ATOM   4521 C CA    . ARG   F 3 74  ? 12.173  -11.740 19.981  1.00 77.79  ?  74  ARG   F CA    1 
ATOM   4522 C C     . ARG   F 3 74  ? 11.625  -11.809 21.400  1.00 78.01  ?  74  ARG   F C     1 
ATOM   4523 O O     . ARG   F 3 74  ? 10.905  -12.755 21.728  1.00 72.23  ?  74  ARG   F O     1 
ATOM   4524 C CB    . ARG   F 3 74  ? 11.148  -10.967 19.128  1.00 78.15  ?  74  ARG   F CB    1 
ATOM   4525 C CG    . ARG   F 3 74  ? 11.730  -9.858  18.270  1.00 80.45  ?  74  ARG   F CG    1 
ATOM   4526 C CD    . ARG   F 3 74  ? 10.756  -9.149  17.313  1.00 80.61  ?  74  ARG   F CD    1 
ATOM   4527 N NE    . ARG   F 3 74  ? 9.302   -9.396  17.323  1.00 78.16  ?  74  ARG   F NE    1 
ATOM   4528 C CZ    . ARG   F 3 74  ? 8.302   -8.600  17.742  1.00 77.95  ?  74  ARG   F CZ    1 
ATOM   4529 N NH1   . ARG   F 3 74  ? 7.089   -8.744  17.221  1.00 76.55  1  74  ARG   F NH1   1 
ATOM   4530 N NH2   . ARG   F 3 74  ? 8.519   -7.616  18.598  1.00 79.86  ?  74  ARG   F NH2   1 
ATOM   4531 N N     . SER   F 3 75  ? 11.927  -10.764 22.178  1.00 80.39  ?  75  SER   F N     1 
ATOM   4532 C CA    . SER   F 3 75  ? 11.222  -10.448 23.406  1.00 81.85  ?  75  SER   F CA    1 
ATOM   4533 C C     . SER   F 3 75  ? 10.487  -9.119  23.201  1.00 85.88  ?  75  SER   F C     1 
ATOM   4534 O O     . SER   F 3 75  ? 11.002  -8.220  22.536  1.00 85.41  ?  75  SER   F O     1 
ATOM   4535 C CB    . SER   F 3 75  ? 12.189  -10.439 24.544  1.00 82.79  ?  75  SER   F CB    1 
ATOM   4536 O OG    . SER   F 3 75  ? 11.528  -10.117 25.753  1.00 85.29  ?  75  SER   F OG    1 
ATOM   4537 N N     . GLN   F 3 76  ? 9.260   -9.037  23.738  1.00 87.34  ?  76  GLN   F N     1 
ATOM   4538 C CA    . GLN   F 3 76  ? 8.337   -7.924  23.528  1.00 88.44  ?  76  GLN   F CA    1 
ATOM   4539 C C     . GLN   F 3 76  ? 8.213   -7.082  24.801  1.00 91.00  ?  76  GLN   F C     1 
ATOM   4540 O O     . GLN   F 3 76  ? 8.391   -5.874  24.741  1.00 97.29  ?  76  GLN   F O     1 
ATOM   4541 C CB    . GLN   F 3 76  ? 7.031   -8.605  23.123  1.00 85.62  ?  76  GLN   F CB    1 
ATOM   4542 C CG    . GLN   F 3 76  ? 5.976   -7.697  22.515  1.00 86.27  ?  76  GLN   F CG    1 
ATOM   4543 C CD    . GLN   F 3 76  ? 4.596   -8.227  22.813  1.00 85.10  ?  76  GLN   F CD    1 
ATOM   4544 O OE1   . GLN   F 3 76  ? 3.908   -7.722  23.700  1.00 88.95  ?  76  GLN   F OE1   1 
ATOM   4545 N NE2   . GLN   F 3 76  ? 4.245   -9.336  22.188  1.00 80.62  ?  76  GLN   F NE2   1 
ATOM   4546 N N     . GLY   F 3 77  ? 7.921   -7.728  25.941  1.00 91.80  ?  77  GLY   F N     1 
ATOM   4547 C CA    . GLY   F 3 77  ? 7.556   -7.103  27.207  1.00 95.37  ?  77  GLY   F CA    1 
ATOM   4548 C C     . GLY   F 3 77  ? 6.220   -7.653  27.715  1.00 96.22  ?  77  GLY   F C     1 
ATOM   4549 O O     . GLY   F 3 77  ? 5.474   -8.275  26.949  1.00 93.28  ?  77  GLY   F O     1 
ATOM   4550 N N     . GLY   F 3 78  ? 5.930   -7.401  29.008  1.00 100.35 ?  78  GLY   F N     1 
ATOM   4551 C CA    . GLY   F 3 78  ? 4.718   -7.867  29.672  1.00 102.23 ?  78  GLY   F CA    1 
ATOM   4552 C C     . GLY   F 3 78  ? 4.696   -9.386  29.897  1.00 98.56  ?  78  GLY   F C     1 
ATOM   4553 O O     . GLY   F 3 78  ? 5.722   -10.054 29.778  1.00 96.76  ?  78  GLY   F O     1 
ATOM   4554 N N     . SER   F 3 79  ? 3.509   -9.922  30.237  1.00 99.08  ?  79  SER   F N     1 
ATOM   4555 C CA    . SER   F 3 79  ? 3.302   -11.361 30.405  1.00 98.99  ?  79  SER   F CA    1 
ATOM   4556 C C     . SER   F 3 79  ? 3.136   -12.002 29.019  1.00 94.02  ?  79  SER   F C     1 
ATOM   4557 O O     . SER   F 3 79  ? 2.669   -11.360 28.079  1.00 96.00  ?  79  SER   F O     1 
ATOM   4558 C CB    . SER   F 3 79  ? 2.166   -11.688 31.398  1.00 102.36 ?  79  SER   F CB    1 
ATOM   4559 O OG    . SER   F 3 79  ? 0.918   -12.031 30.806  1.00 105.52 ?  79  SER   F OG    1 
ATOM   4560 N N     . LYS   F 3 80  ? 3.546   -13.273 28.888  1.00 86.02  ?  80  LYS   F N     1 
ATOM   4561 C CA    . LYS   F 3 80  ? 3.701   -13.972 27.611  1.00 80.40  ?  80  LYS   F CA    1 
ATOM   4562 C C     . LYS   F 3 80  ? 4.545   -13.157 26.608  1.00 81.14  ?  80  LYS   F C     1 
ATOM   4563 O O     . LYS   F 3 80  ? 4.121   -12.948 25.469  1.00 78.07  ?  80  LYS   F O     1 
ATOM   4564 C CB    . LYS   F 3 80  ? 2.308   -14.466 27.164  1.00 76.93  ?  80  LYS   F CB    1 
ATOM   4565 C CG    . LYS   F 3 80  ? 1.782   -15.819 27.711  1.00 72.83  ?  80  LYS   F CG    1 
ATOM   4566 C CD    . LYS   F 3 80  ? 0.861   -15.836 28.932  1.00 73.07  ?  80  LYS   F CD    1 
ATOM   4567 C CE    . LYS   F 3 80  ? -0.468  -15.133 28.830  1.00 74.67  ?  80  LYS   F CE    1 
ATOM   4568 N NZ    . LYS   F 3 80  ? -1.427  -15.659 27.855  1.00 72.38  ?  80  LYS   F NZ    1 
ATOM   4569 N N     . PRO   F 3 81  ? 5.787   -12.715 26.965  1.00 83.88  ?  81  PRO   F N     1 
ATOM   4570 C CA    . PRO   F 3 81  ? 6.548   -11.751 26.150  1.00 86.03  ?  81  PRO   F CA    1 
ATOM   4571 C C     . PRO   F 3 81  ? 7.311   -12.265 24.913  1.00 83.35  ?  81  PRO   F C     1 
ATOM   4572 O O     . PRO   F 3 81  ? 7.895   -11.450 24.188  1.00 84.98  ?  81  PRO   F O     1 
ATOM   4573 C CB    . PRO   F 3 81  ? 7.547   -11.200 27.167  1.00 88.61  ?  81  PRO   F CB    1 
ATOM   4574 C CG    . PRO   F 3 81  ? 7.866   -12.462 27.970  1.00 85.75  ?  81  PRO   F CG    1 
ATOM   4575 C CD    . PRO   F 3 81  ? 6.552   -13.139 28.159  1.00 82.78  ?  81  PRO   F CD    1 
ATOM   4576 N N     . LEU   F 3 82  ? 7.358   -13.591 24.687  1.00 80.60  ?  82  LEU   F N     1 
ATOM   4577 C CA    . LEU   F 3 82  ? 8.233   -14.206 23.687  1.00 77.25  ?  82  LEU   F CA    1 
ATOM   4578 C C     . LEU   F 3 82  ? 7.495   -14.188 22.343  1.00 74.42  ?  82  LEU   F C     1 
ATOM   4579 O O     . LEU   F 3 82  ? 6.291   -14.438 22.306  1.00 73.04  ?  82  LEU   F O     1 
ATOM   4580 C CB    . LEU   F 3 82  ? 8.594   -15.607 24.191  1.00 75.17  ?  82  LEU   F CB    1 
ATOM   4581 C CG    . LEU   F 3 82  ? 9.892   -16.307 23.762  1.00 77.03  ?  82  LEU   F CG    1 
ATOM   4582 C CD1   . LEU   F 3 82  ? 9.686   -17.120 22.490  1.00 73.82  ?  82  LEU   F CD1   1 
ATOM   4583 C CD2   . LEU   F 3 82  ? 11.127  -15.411 23.658  1.00 77.64  ?  82  LEU   F CD2   1 
ATOM   4584 N N     . VAL   F 3 83  ? 8.193   -13.768 21.275  1.00 72.95  ?  83  VAL   F N     1 
ATOM   4585 C CA    . VAL   F 3 83  ? 7.680   -13.703 19.906  1.00 70.37  ?  83  VAL   F CA    1 
ATOM   4586 C C     . VAL   F 3 83  ? 8.643   -14.530 19.047  1.00 65.97  ?  83  VAL   F C     1 
ATOM   4587 O O     . VAL   F 3 83  ? 9.861   -14.434 19.250  1.00 65.58  ?  83  VAL   F O     1 
ATOM   4588 C CB    . VAL   F 3 83  ? 7.556   -12.256 19.356  1.00 73.74  ?  83  VAL   F CB    1 
ATOM   4589 C CG1   . VAL   F 3 83  ? 6.723   -12.211 18.078  1.00 73.62  ?  83  VAL   F CG1   1 
ATOM   4590 C CG2   . VAL   F 3 83  ? 7.013   -11.249 20.360  1.00 75.49  ?  83  VAL   F CG2   1 
ATOM   4591 N N     . VAL   F 3 84  ? 8.112   -15.331 18.093  1.00 61.27  ?  84  VAL   F N     1 
ATOM   4592 C CA    . VAL   F 3 84  ? 8.912   -16.306 17.352  1.00 57.55  ?  84  VAL   F CA    1 
ATOM   4593 C C     . VAL   F 3 84  ? 8.627   -16.169 15.864  1.00 56.32  ?  84  VAL   F C     1 
ATOM   4594 O O     . VAL   F 3 84  ? 7.452   -16.092 15.484  1.00 54.65  ?  84  VAL   F O     1 
ATOM   4595 C CB    . VAL   F 3 84  ? 8.655   -17.753 17.840  1.00 54.56  ?  84  VAL   F CB    1 
ATOM   4596 C CG1   . VAL   F 3 84  ? 9.389   -18.811 17.005  1.00 52.44  ?  84  VAL   F CG1   1 
ATOM   4597 C CG2   . VAL   F 3 84  ? 8.969   -17.897 19.325  1.00 53.71  ?  84  VAL   F CG2   1 
ATOM   4598 N N     . LYS   F 3 85  ? 9.706   -16.258 15.062  1.00 56.83  ?  85  LYS   F N     1 
ATOM   4599 C CA    . LYS   F 3 85  ? 9.643   -16.299 13.606  1.00 57.67  ?  85  LYS   F CA    1 
ATOM   4600 C C     . LYS   F 3 85  ? 10.271  -17.618 13.162  1.00 55.28  ?  85  LYS   F C     1 
ATOM   4601 O O     . LYS   F 3 85  ? 11.417  -17.868 13.545  1.00 55.04  ?  85  LYS   F O     1 
ATOM   4602 C CB    . LYS   F 3 85  ? 10.353  -15.083 12.977  1.00 60.58  ?  85  LYS   F CB    1 
ATOM   4603 C CG    . LYS   F 3 85  ? 10.011  -14.810 11.507  1.00 61.57  ?  85  LYS   F CG    1 
ATOM   4604 C CD    . LYS   F 3 85  ? 10.752  -13.687 10.782  1.00 64.45  ?  85  LYS   F CD    1 
ATOM   4605 C CE    . LYS   F 3 85  ? 10.100  -12.324 10.816  1.00 67.20  ?  85  LYS   F CE    1 
ATOM   4606 N NZ    . LYS   F 3 85  ? 10.966  -11.215 10.339  1.00 70.15  1  85  LYS   F NZ    1 
ATOM   4607 N N     . LEU   F 3 86  ? 9.529   -18.425 12.374  1.00 53.92  ?  86  LEU   F N     1 
ATOM   4608 C CA    . LEU   F 3 86  ? 9.948   -19.708 11.821  1.00 52.29  ?  86  LEU   F CA    1 
ATOM   4609 C C     . LEU   F 3 86  ? 9.787   -19.661 10.309  1.00 52.47  ?  86  LEU   F C     1 
ATOM   4610 O O     . LEU   F 3 86  ? 8.648   -19.574 9.844   1.00 51.58  ?  86  LEU   F O     1 
ATOM   4611 C CB    . LEU   F 3 86  ? 9.080   -20.865 12.343  1.00 50.74  ?  86  LEU   F CB    1 
ATOM   4612 C CG    . LEU   F 3 86  ? 9.133   -21.168 13.832  1.00 50.09  ?  86  LEU   F CG    1 
ATOM   4613 C CD1   . LEU   F 3 86  ? 8.187   -22.290 14.153  1.00 47.14  ?  86  LEU   F CD1   1 
ATOM   4614 C CD2   . LEU   F 3 86  ? 10.562  -21.481 14.231  1.00 51.54  ?  86  LEU   F CD2   1 
ATOM   4615 N N     . VAL   F 3 87  ? 10.894  -19.836 9.568   1.00 53.39  ?  87  VAL   F N     1 
ATOM   4616 C CA    . VAL   F 3 87  ? 10.882  -19.799 8.103   1.00 54.49  ?  87  VAL   F CA    1 
ATOM   4617 C C     . VAL   F 3 87  ? 11.092  -21.254 7.665   1.00 51.90  ?  87  VAL   F C     1 
ATOM   4618 O O     . VAL   F 3 87  ? 12.107  -21.826 8.051   1.00 51.06  ?  87  VAL   F O     1 
ATOM   4619 C CB    . VAL   F 3 87  ? 11.796  -18.745 7.397   1.00 57.95  ?  87  VAL   F CB    1 
ATOM   4620 C CG1   . VAL   F 3 87  ? 12.737  -17.972 8.327   1.00 58.94  ?  87  VAL   F CG1   1 
ATOM   4621 C CG2   . VAL   F 3 87  ? 12.524  -19.203 6.120   1.00 58.71  ?  87  VAL   F CG2   1 
ATOM   4622 N N     . ASN   F 3 88  ? 10.130  -21.812 6.882   1.00 50.97  ?  88  ASN   F N     1 
ATOM   4623 C CA    . ASN   F 3 88  ? 10.186  -23.137 6.271   1.00 49.82  ?  88  ASN   F CA    1 
ATOM   4624 C C     . ASN   F 3 88  ? 9.891   -23.029 4.769   1.00 51.97  ?  88  ASN   F C     1 
ATOM   4625 O O     . ASN   F 3 88  ? 8.755   -22.725 4.379   1.00 51.31  ?  88  ASN   F O     1 
ATOM   4626 C CB    . ASN   F 3 88  ? 9.191   -24.107 6.911   1.00 47.66  ?  88  ASN   F CB    1 
ATOM   4627 C CG    . ASN   F 3 88  ? 9.323   -24.196 8.417   1.00 45.81  ?  88  ASN   F CG    1 
ATOM   4628 O OD1   . ASN   F 3 88  ? 8.428   -23.717 9.123   1.00 46.00  ?  88  ASN   F OD1   1 
ATOM   4629 N ND2   . ASN   F 3 88  ? 10.448  -24.689 8.912   1.00 44.83  ?  88  ASN   F ND2   1 
ATOM   4630 N N     . ASP   F 3 89  ? 10.923  -23.263 3.932   1.00 54.67  ?  89  ASP   F N     1 
ATOM   4631 C CA    . ASP   F 3 89  ? 10.860  -23.221 2.473   1.00 58.55  ?  89  ASP   F CA    1 
ATOM   4632 C C     . ASP   F 3 89  ? 10.242  -21.902 1.998   1.00 61.03  ?  89  ASP   F C     1 
ATOM   4633 O O     . ASP   F 3 89  ? 9.207   -21.910 1.324   1.00 61.11  ?  89  ASP   F O     1 
ATOM   4634 C CB    . ASP   F 3 89  ? 10.227  -24.484 1.898   1.00 57.90  ?  89  ASP   F CB    1 
ATOM   4635 C CG    . ASP   F 3 89  ? 10.399  -24.690 0.389   1.00 62.07  ?  89  ASP   F CG    1 
ATOM   4636 O OD1   . ASP   F 3 89  ? 11.529  -24.517 -0.114  1.00 66.81  ?  89  ASP   F OD1   1 
ATOM   4637 O OD2   . ASP   F 3 89  ? 9.403   -25.021 -0.295  1.00 61.49  -1 89  ASP   F OD2   1 
ATOM   4638 N N     . GLY   F 3 90  ? 10.806  -20.780 2.486   1.00 63.13  ?  90  GLY   F N     1 
ATOM   4639 C CA    . GLY   F 3 90  ? 10.359  -19.435 2.140   1.00 66.36  ?  90  GLY   F CA    1 
ATOM   4640 C C     . GLY   F 3 90  ? 8.963   -19.042 2.629   1.00 66.15  ?  90  GLY   F C     1 
ATOM   4641 O O     . GLY   F 3 90  ? 8.497   -17.998 2.203   1.00 67.68  ?  90  GLY   F O     1 
ATOM   4642 N N     . VAL   F 3 91  ? 8.339   -19.817 3.545   1.00 65.16  ?  91  VAL   F N     1 
ATOM   4643 C CA    . VAL   F 3 91  ? 7.044   -19.505 4.137   1.00 64.71  ?  91  VAL   F CA    1 
ATOM   4644 C C     . VAL   F 3 91  ? 7.332   -19.127 5.587   1.00 62.98  ?  91  VAL   F C     1 
ATOM   4645 O O     . VAL   F 3 91  ? 7.795   -19.993 6.335   1.00 62.36  ?  91  VAL   F O     1 
ATOM   4646 C CB    . VAL   F 3 91  ? 6.015   -20.648 4.044   1.00 61.82  ?  91  VAL   F CB    1 
ATOM   4647 C CG1   . VAL   F 3 91  ? 4.700   -20.257 4.724   1.00 61.51  ?  91  VAL   F CG1   1 
ATOM   4648 C CG2   . VAL   F 3 91  ? 5.789   -21.068 2.590   1.00 62.49  ?  91  VAL   F CG2   1 
ATOM   4649 N N     . THR   F 3 92  ? 6.996   -17.878 5.974   1.00 64.03  ?  92  THR   F N     1 
ATOM   4650 C CA    . THR   F 3 92  ? 7.271   -17.320 7.298   1.00 62.82  ?  92  THR   F CA    1 
ATOM   4651 C C     . THR   F 3 92  ? 6.053   -17.552 8.191   1.00 59.95  ?  92  THR   F C     1 
ATOM   4652 O O     . THR   F 3 92  ? 4.950   -17.209 7.779   1.00 59.23  ?  92  THR   F O     1 
ATOM   4653 C CB    . THR   F 3 92  ? 7.555   -15.819 7.166   1.00 66.32  ?  92  THR   F CB    1 
ATOM   4654 O OG1   . THR   F 3 92  ? 8.631   -15.694 6.249   1.00 67.85  ?  92  THR   F OG1   1 
ATOM   4655 C CG2   . THR   F 3 92  ? 7.996   -15.153 8.460   1.00 66.12  ?  92  THR   F CG2   1 
ATOM   4656 N N     . LEU   F 3 93  ? 6.256   -18.183 9.365   1.00 58.74  ?  93  LEU   F N     1 
ATOM   4657 C CA    . LEU   F 3 93  ? 5.283   -18.257 10.448  1.00 56.81  ?  93  LEU   F CA    1 
ATOM   4658 C C     . LEU   F 3 93  ? 5.741   -17.313 11.554  1.00 57.06  ?  93  LEU   F C     1 
ATOM   4659 O O     . LEU   F 3 93  ? 6.898   -17.404 11.974  1.00 57.03  ?  93  LEU   F O     1 
ATOM   4660 C CB    . LEU   F 3 93  ? 5.189   -19.692 10.959  1.00 52.52  ?  93  LEU   F CB    1 
ATOM   4661 C CG    . LEU   F 3 93  ? 4.207   -19.961 12.112  1.00 51.59  ?  93  LEU   F CG    1 
ATOM   4662 C CD1   . LEU   F 3 93  ? 2.735   -19.773 11.763  1.00 51.64  ?  93  LEU   F CD1   1 
ATOM   4663 C CD2   . LEU   F 3 93  ? 4.415   -21.371 12.682  1.00 49.02  ?  93  LEU   F CD2   1 
ATOM   4664 N N     . GLU   F 3 94  ? 4.830   -16.454 12.031  1.00 57.42  ?  94  GLU   F N     1 
ATOM   4665 C CA    . GLU   F 3 94  ? 5.101   -15.539 13.136  1.00 59.08  ?  94  GLU   F CA    1 
ATOM   4666 C C     . GLU   F 3 94  ? 4.140   -15.918 14.254  1.00 57.28  ?  94  GLU   F C     1 
ATOM   4667 O O     . GLU   F 3 94  ? 2.931   -15.988 13.983  1.00 56.97  ?  94  GLU   F O     1 
ATOM   4668 C CB    . GLU   F 3 94  ? 4.956   -14.051 12.791  1.00 62.71  ?  94  GLU   F CB    1 
ATOM   4669 C CG    . GLU   F 3 94  ? 5.442   -13.100 13.886  1.00 64.31  ?  94  GLU   F CG    1 
ATOM   4670 C CD    . GLU   F 3 94  ? 5.204   -11.623 13.557  1.00 68.67  ?  94  GLU   F CD    1 
ATOM   4671 O OE1   . GLU   F 3 94  ? 4.023   -11.249 13.354  1.00 68.97  ?  94  GLU   F OE1   1 
ATOM   4672 O OE2   . GLU   F 3 94  ? 6.178   -10.836 13.504  1.00 70.58  -1 94  GLU   F OE2   1 
ATOM   4673 N N     . LEU   F 3 95  ? 4.693   -16.150 15.462  1.00 55.96  ?  95  LEU   F N     1 
ATOM   4674 C CA    . LEU   F 3 95  ? 3.924   -16.506 16.642  1.00 56.66  ?  95  LEU   F CA    1 
ATOM   4675 C C     . LEU   F 3 95  ? 4.058   -15.412 17.691  1.00 59.51  ?  95  LEU   F C     1 
ATOM   4676 O O     . LEU   F 3 95  ? 5.188   -14.970 17.967  1.00 59.52  ?  95  LEU   F O     1 
ATOM   4677 C CB    . LEU   F 3 95  ? 4.411   -17.829 17.230  1.00 55.32  ?  95  LEU   F CB    1 
ATOM   4678 C CG    . LEU   F 3 95  ? 4.210   -19.066 16.351  1.00 53.34  ?  95  LEU   F CG    1 
ATOM   4679 C CD1   . LEU   F 3 95  ? 4.742   -20.261 17.155  1.00 51.17  ?  95  LEU   F CD1   1 
ATOM   4680 C CD2   . LEU   F 3 95  ? 2.765   -19.300 15.895  1.00 52.83  ?  95  LEU   F CD2   1 
ATOM   4681 N N     . THR   F 3 96  ? 2.893   -15.046 18.268  1.00 61.19  ?  96  THR   F N     1 
ATOM   4682 C CA    . THR   F 3 96  ? 2.760   -14.142 19.403  1.00 65.06  ?  96  THR   F CA    1 
ATOM   4683 C C     . THR   F 3 96  ? 1.696   -14.695 20.357  1.00 65.65  ?  96  THR   F C     1 
ATOM   4684 O O     . THR   F 3 96  ? 0.905   -15.547 19.995  1.00 65.17  ?  96  THR   F O     1 
ATOM   4685 C CB    . THR   F 3 96  ? 2.415   -12.716 18.927  1.00 67.76  ?  96  THR   F CB    1 
ATOM   4686 O OG1   . THR   F 3 96  ? 1.935   -12.010 20.061  1.00 70.68  ?  96  THR   F OG1   1 
ATOM   4687 C CG2   . THR   F 3 96  ? 1.311   -12.611 17.885  1.00 67.84  ?  96  THR   F CG2   1 
ATOM   4688 N N     . ARG   F 3 97  ? 1.623   -14.104 21.558  1.00 70.84  ?  97  ARG   F N     1 
ATOM   4689 C CA    . ARG   F 3 97  ? 0.567   -14.345 22.539  1.00 71.02  ?  97  ARG   F CA    1 
ATOM   4690 C C     . ARG   F 3 97  ? -0.847  -14.187 21.969  1.00 70.44  ?  97  ARG   F C     1 
ATOM   4691 O O     . ARG   F 3 97  ? -1.739  -14.848 22.472  1.00 69.64  ?  97  ARG   F O     1 
ATOM   4692 C CB    . ARG   F 3 97  ? 0.759   -13.382 23.724  1.00 75.69  ?  97  ARG   F CB    1 
ATOM   4693 C CG    . ARG   F 3 97  ? -0.289  -13.328 24.835  1.00 76.67  ?  97  ARG   F CG    1 
ATOM   4694 C CD    . ARG   F 3 97  ? -1.174  -12.096 24.784  1.00 79.12  ?  97  ARG   F CD    1 
ATOM   4695 N NE    . ARG   F 3 97  ? -0.417  -10.990 25.389  1.00 83.50  ?  97  ARG   F NE    1 
ATOM   4696 C CZ    . ARG   F 3 97  ? -0.163  -9.769  24.912  1.00 85.24  ?  97  ARG   F CZ    1 
ATOM   4697 N NH1   . ARG   F 3 97  ? 0.813   -9.052  25.443  1.00 87.35  ?  97  ARG   F NH1   1 
ATOM   4698 N NH2   . ARG   F 3 97  ? -0.826  -9.265  23.885  1.00 87.28  ?  97  ARG   F NH2   1 
ATOM   4699 N N     . ASP   F 3 98  ? -1.052  -13.310 20.970  1.00 73.67  ?  98  ASP   F N     1 
ATOM   4700 C CA    . ASP   F 3 98  ? -2.363  -13.027 20.387  1.00 75.15  ?  98  ASP   F CA    1 
ATOM   4701 C C     . ASP   F 3 98  ? -2.825  -14.037 19.338  1.00 71.76  ?  98  ASP   F C     1 
ATOM   4702 O O     . ASP   F 3 98  ? -4.009  -13.993 19.003  1.00 72.97  ?  98  ASP   F O     1 
ATOM   4703 C CB    . ASP   F 3 98  ? -2.417  -11.642 19.749  1.00 80.26  ?  98  ASP   F CB    1 
ATOM   4704 C CG    . ASP   F 3 98  ? -1.981  -10.498 20.645  1.00 82.65  ?  98  ASP   F CG    1 
ATOM   4705 O OD1   . ASP   F 3 98  ? -2.415  -10.491 21.804  1.00 84.47  ?  98  ASP   F OD1   1 
ATOM   4706 O OD2   . ASP   F 3 98  ? -1.196  -9.653  20.179  1.00 87.40  -1 98  ASP   F OD2   1 
ATOM   4707 N N     . GLY   F 3 99  ? -1.936  -14.933 18.849  1.00 68.25  ?  99  GLY   F N     1 
ATOM   4708 C CA    . GLY   F 3 99  ? -2.206  -15.808 17.723  1.00 62.72  ?  99  GLY   F CA    1 
ATOM   4709 C C     . GLY   F 3 99  ? -1.013  -15.806 16.774  1.00 61.57  ?  99  GLY   F C     1 
ATOM   4710 O O     . GLY   F 3 99  ? 0.143   -15.726 17.200  1.00 60.08  ?  99  GLY   F O     1 
ATOM   4711 N N     . ALA   F 3 100 ? -1.302  -15.865 15.473  1.00 61.68  ?  100 ALA   F N     1 
ATOM   4712 C CA    . ALA   F 3 100 ? -0.331  -16.332 14.498  1.00 59.97  ?  100 ALA   F CA    1 
ATOM   4713 C C     . ALA   F 3 100 ? -0.670  -15.810 13.107  1.00 61.53  ?  100 ALA   F C     1 
ATOM   4714 O O     . ALA   F 3 100 ? -1.839  -15.548 12.798  1.00 60.83  ?  100 ALA   F O     1 
ATOM   4715 C CB    . ALA   F 3 100 ? -0.312  -17.860 14.498  1.00 56.95  ?  100 ALA   F CB    1 
ATOM   4716 N N     . SER   F 3 101 ? 0.371   -15.768 12.261  1.00 62.30  ?  101 SER   F N     1 
ATOM   4717 C CA    . SER   F 3 101 ? 0.268   -15.331 10.878  1.00 64.10  ?  101 SER   F CA    1 
ATOM   4718 C C     . SER   F 3 101 ? 1.246   -16.113 9.996   1.00 63.05  ?  101 SER   F C     1 
ATOM   4719 O O     . SER   F 3 101 ? 2.320   -16.510 10.471  1.00 60.15  ?  101 SER   F O     1 
ATOM   4720 C CB    . SER   F 3 101 ? 0.515   -13.836 10.772  1.00 67.40  ?  101 SER   F CB    1 
ATOM   4721 O OG    . SER   F 3 101 ? 1.825   -13.504 11.221  1.00 66.91  ?  101 SER   F OG    1 
ATOM   4722 N N     . ILE   F 3 102 ? 0.881   -16.241 8.697   1.00 65.36  ?  102 ILE   F N     1 
ATOM   4723 C CA    . ILE   F 3 102 ? 1.663   -16.939 7.680   1.00 63.68  ?  102 ILE   F CA    1 
ATOM   4724 C C     . ILE   F 3 102 ? 1.953   -15.929 6.553   1.00 65.27  ?  102 ILE   F C     1 
ATOM   4725 O O     . ILE   F 3 102 ? 1.037   -15.519 5.855   1.00 64.76  ?  102 ILE   F O     1 
ATOM   4726 C CB    . ILE   F 3 102 ? 0.997   -18.260 7.202   1.00 63.15  ?  102 ILE   F CB    1 
ATOM   4727 C CG1   . ILE   F 3 102 ? -0.514  -18.137 6.904   1.00 65.29  ?  102 ILE   F CG1   1 
ATOM   4728 C CG2   . ILE   F 3 102 ? 1.211   -19.409 8.210   1.00 60.09  ?  102 ILE   F CG2   1 
ATOM   4729 C CD1   . ILE   F 3 102 ? -1.070  -19.240 6.012   1.00 63.54  ?  102 ILE   F CD1   1 
ATOM   4730 N N     . ASN   F 3 103 ? 3.234   -15.531 6.414   1.00 65.72  ?  103 ASN   F N     1 
ATOM   4731 C CA    . ASN   F 3 103 ? 3.765   -14.542 5.477   1.00 69.12  ?  103 ASN   F CA    1 
ATOM   4732 C C     . ASN   F 3 103 ? 3.394   -13.080 5.777   1.00 71.91  ?  103 ASN   F C     1 
ATOM   4733 O O     . ASN   F 3 103 ? 3.937   -12.230 5.096   1.00 73.48  ?  103 ASN   F O     1 
ATOM   4734 C CB    . ASN   F 3 103 ? 3.556   -14.929 4.002   1.00 69.83  ?  103 ASN   F CB    1 
ATOM   4735 C CG    . ASN   F 3 103 ? 4.305   -16.181 3.587   1.00 66.65  ?  103 ASN   F CG    1 
ATOM   4736 O OD1   . ASN   F 3 103 ? 5.440   -16.401 4.024   1.00 65.98  ?  103 ASN   F OD1   1 
ATOM   4737 N ND2   . ASN   F 3 103 ? 3.712   -17.004 2.729   1.00 65.20  ?  103 ASN   F ND2   1 
ATOM   4738 N N     . GLY   F 3 104 ? 2.665   -12.750 6.857   1.00 72.55  ?  104 GLY   F N     1 
ATOM   4739 C CA    . GLY   F 3 104 ? 1.968   -11.483 6.994   1.00 76.72  ?  104 GLY   F CA    1 
ATOM   4740 C C     . GLY   F 3 104 ? 0.503   -11.662 7.395   1.00 78.51  ?  104 GLY   F C     1 
ATOM   4741 O O     . GLY   F 3 104 ? 0.052   -10.956 8.300   1.00 82.57  ?  104 GLY   F O     1 
ATOM   4742 N N     . LYS   F 3 105 ? -0.238  -12.558 6.710   1.00 77.63  ?  105 LYS   F N     1 
ATOM   4743 C CA    . LYS   F 3 105 ? -1.687  -12.662 6.857   1.00 78.99  ?  105 LYS   F CA    1 
ATOM   4744 C C     . LYS   F 3 105 ? -1.995  -13.495 8.105   1.00 77.61  ?  105 LYS   F C     1 
ATOM   4745 O O     . LYS   F 3 105 ? -1.496  -14.622 8.242   1.00 72.98  ?  105 LYS   F O     1 
ATOM   4746 C CB    . LYS   F 3 105 ? -2.361  -13.187 5.581   1.00 80.81  ?  105 LYS   F CB    1 
ATOM   4747 C CG    . LYS   F 3 105 ? -1.938  -12.448 4.295   1.00 86.05  ?  105 LYS   F CG    1 
ATOM   4748 C CD    . LYS   F 3 105 ? -2.929  -12.261 3.144   1.00 88.99  ?  105 LYS   F CD    1 
ATOM   4749 C CE    . LYS   F 3 105 ? -2.279  -11.497 2.032   1.00 92.61  ?  105 LYS   F CE    1 
ATOM   4750 N NZ    . LYS   F 3 105 ? -3.101  -11.318 0.826   1.00 96.67  1  105 LYS   F NZ    1 
ATOM   4751 N N     . ALA   F 3 106 ? -2.781  -12.903 9.028   1.00 80.08  ?  106 ALA   F N     1 
ATOM   4752 C CA    . ALA   F 3 106 ? -3.213  -13.560 10.256  1.00 78.18  ?  106 ALA   F CA    1 
ATOM   4753 C C     . ALA   F 3 106 ? -4.237  -14.635 9.912   1.00 77.00  ?  106 ALA   F C     1 
ATOM   4754 O O     . ALA   F 3 106 ? -5.058  -14.433 9.020   1.00 76.41  ?  106 ALA   F O     1 
ATOM   4755 C CB    . ALA   F 3 106 ? -3.811  -12.567 11.229  1.00 80.57  ?  106 ALA   F CB    1 
ATOM   4756 N N     . VAL   F 3 107 ? -4.194  -15.740 10.675  1.00 77.82  ?  107 VAL   F N     1 
ATOM   4757 C CA    . VAL   F 3 107 ? -4.907  -16.978 10.393  1.00 75.26  ?  107 VAL   F CA    1 
ATOM   4758 C C     . VAL   F 3 107 ? -5.534  -17.489 11.691  1.00 72.15  ?  107 VAL   F C     1 
ATOM   4759 O O     . VAL   F 3 107 ? -5.037  -17.166 12.777  1.00 69.18  ?  107 VAL   F O     1 
ATOM   4760 C CB    . VAL   F 3 107 ? -3.980  -18.036 9.746   1.00 76.69  ?  107 VAL   F CB    1 
ATOM   4761 C CG1   . VAL   F 3 107 ? -3.742  -17.757 8.263   1.00 78.00  ?  107 VAL   F CG1   1 
ATOM   4762 C CG2   . VAL   F 3 107 ? -2.654  -18.231 10.498  1.00 76.45  ?  107 VAL   F CG2   1 
ATOM   4763 N N     . SER   F 3 108 ? -6.591  -18.317 11.541  1.00 67.85  ?  108 SER   F N     1 
ATOM   4764 C CA    . SER   F 3 108 ? -7.411  -18.818 12.629  1.00 65.27  ?  108 SER   F CA    1 
ATOM   4765 C C     . SER   F 3 108 ? -6.726  -20.055 13.223  1.00 64.37  ?  108 SER   F C     1 
ATOM   4766 O O     . SER   F 3 108 ? -7.141  -21.196 12.991  1.00 61.58  ?  108 SER   F O     1 
ATOM   4767 C CB    . SER   F 3 108 ? -8.813  -19.101 12.156  1.00 64.99  ?  108 SER   F CB    1 
ATOM   4768 O OG    . SER   F 3 108 ? -8.809  -20.072 11.120  1.00 62.66  ?  108 SER   F OG    1 
ATOM   4769 N N     . VAL   F 3 109 ? -5.646  -19.805 13.984  1.00 65.17  ?  109 VAL   F N     1 
ATOM   4770 C CA    . VAL   F 3 109 ? -4.745  -20.835 14.488  1.00 64.76  ?  109 VAL   F CA    1 
ATOM   4771 C C     . VAL   F 3 109 ? -5.415  -21.727 15.542  1.00 63.58  ?  109 VAL   F C     1 
ATOM   4772 O O     . VAL   F 3 109 ? -4.976  -22.866 15.705  1.00 60.66  ?  109 VAL   F O     1 
ATOM   4773 C CB    . VAL   F 3 109 ? -3.404  -20.240 14.983  1.00 65.76  ?  109 VAL   F CB    1 
ATOM   4774 C CG1   . VAL   F 3 109 ? -3.544  -19.327 16.208  1.00 66.53  ?  109 VAL   F CG1   1 
ATOM   4775 C CG2   . VAL   F 3 109 ? -2.343  -21.332 15.212  1.00 62.02  ?  109 VAL   F CG2   1 
ATOM   4776 N N     . GLU   F 3 110 ? -6.472  -21.235 16.220  1.00 64.36  ?  110 GLU   F N     1 
ATOM   4777 C CA    . GLU   F 3 110 ? -7.280  -22.040 17.138  1.00 64.67  ?  110 GLU   F CA    1 
ATOM   4778 C C     . GLU   F 3 110 ? -8.082  -23.153 16.431  1.00 60.95  ?  110 GLU   F C     1 
ATOM   4779 O O     . GLU   F 3 110 ? -8.466  -24.097 17.109  1.00 60.24  ?  110 GLU   F O     1 
ATOM   4780 C CB    . GLU   F 3 110 ? -8.065  -21.127 18.093  1.00 66.87  ?  110 GLU   F CB    1 
ATOM   4781 C CG    . GLU   F 3 110 ? -7.180  -20.362 19.090  1.00 69.16  ?  110 GLU   F CG    1 
ATOM   4782 C CD    . GLU   F 3 110 ? -7.398  -18.863 19.384  1.00 73.58  ?  110 GLU   F CD    1 
ATOM   4783 O OE1   . GLU   F 3 110 ? -8.153  -18.142 18.706  1.00 76.55  ?  110 GLU   F OE1   1 
ATOM   4784 O OE2   . GLU   F 3 110 ? -6.739  -18.355 20.320  1.00 75.24  -1 110 GLU   F OE2   1 
ATOM   4785 N N     . LYS   F 3 111 ? -8.330  -23.090 15.108  1.00 60.32  ?  111 LYS   F N     1 
ATOM   4786 C CA    . LYS   F 3 111 ? -8.651  -24.271 14.291  1.00 60.85  ?  111 LYS   F CA    1 
ATOM   4787 C C     . LYS   F 3 111 ? -7.329  -24.862 13.761  1.00 56.15  ?  111 LYS   F C     1 
ATOM   4788 O O     . LYS   F 3 111 ? -6.258  -24.471 14.203  1.00 58.26  ?  111 LYS   F O     1 
ATOM   4789 C CB    . LYS   F 3 111 ? -9.667  -23.933 13.190  1.00 65.04  ?  111 LYS   F CB    1 
ATOM   4790 C CG    . LYS   F 3 111 ? -10.950 -23.171 13.575  1.00 71.09  ?  111 LYS   F CG    1 
ATOM   4791 C CD    . LYS   F 3 111 ? -11.952 -23.876 14.496  1.00 72.95  ?  111 LYS   F CD    1 
ATOM   4792 C CE    . LYS   F 3 111 ? -13.228 -24.375 13.851  1.00 74.45  ?  111 LYS   F CE    1 
ATOM   4793 N NZ    . LYS   F 3 111 ? -14.155 -23.311 13.439  1.00 77.45  1  111 LYS   F NZ    1 
ATOM   4794 N N     . GLY   F 3 112 ? -7.345  -25.811 12.832  1.00 50.96  ?  112 GLY   F N     1 
ATOM   4795 C CA    . GLY   F 3 112 ? -6.101  -26.183 12.144  1.00 49.94  ?  112 GLY   F CA    1 
ATOM   4796 C C     . GLY   F 3 112 ? -5.738  -25.160 11.067  1.00 47.83  ?  112 GLY   F C     1 
ATOM   4797 O O     . GLY   F 3 112 ? -6.662  -24.726 10.400  1.00 46.72  ?  112 GLY   F O     1 
ATOM   4798 N N     . VAL   F 3 113 ? -4.442  -24.816 10.870  1.00 45.51  ?  113 VAL   F N     1 
ATOM   4799 C CA    . VAL   F 3 113 ? -4.039  -24.090 9.654   1.00 46.78  ?  113 VAL   F CA    1 
ATOM   4800 C C     . VAL   F 3 113 ? -2.825  -24.759 8.999   1.00 44.19  ?  113 VAL   F C     1 
ATOM   4801 O O     . VAL   F 3 113 ? -1.829  -24.984 9.673   1.00 42.64  ?  113 VAL   F O     1 
ATOM   4802 C CB    . VAL   F 3 113 ? -3.816  -22.570 9.878   1.00 49.22  ?  113 VAL   F CB    1 
ATOM   4803 C CG1   . VAL   F 3 113 ? -3.330  -21.827 8.623   1.00 51.36  ?  113 VAL   F CG1   1 
ATOM   4804 C CG2   . VAL   F 3 113 ? -5.084  -21.907 10.411  1.00 50.89  ?  113 VAL   F CG2   1 
ATOM   4805 N N     . GLN   F 3 114 ? -2.905  -24.997 7.675   1.00 45.06  ?  114 GLN   F N     1 
ATOM   4806 C CA    . GLN   F 3 114 ? -1.858  -25.570 6.839   1.00 44.23  ?  114 GLN   F CA    1 
ATOM   4807 C C     . GLN   F 3 114 ? -1.608  -24.667 5.624   1.00 46.34  ?  114 GLN   F C     1 
ATOM   4808 O O     . GLN   F 3 114 ? -2.561  -24.245 4.966   1.00 47.03  ?  114 GLN   F O     1 
ATOM   4809 C CB    . GLN   F 3 114 ? -2.332  -26.926 6.309   1.00 44.36  ?  114 GLN   F CB    1 
ATOM   4810 C CG    . GLN   F 3 114 ? -1.273  -27.745 5.571   1.00 43.44  ?  114 GLN   F CG    1 
ATOM   4811 C CD    . GLN   F 3 114 ? -1.836  -29.044 5.042   1.00 42.50  ?  114 GLN   F CD    1 
ATOM   4812 O OE1   . GLN   F 3 114 ? -2.429  -29.827 5.802   1.00 41.12  ?  114 GLN   F OE1   1 
ATOM   4813 N NE2   . GLN   F 3 114 ? -1.680  -29.290 3.747   1.00 44.05  ?  114 GLN   F NE2   1 
ATOM   4814 N N     . TYR   F 3 115 ? -0.323  -24.472 5.268   1.00 46.12  ?  115 TYR   F N     1 
ATOM   4815 C CA    . TYR   F 3 115 ? 0.070   -23.762 4.063   1.00 48.77  ?  115 TYR   F CA    1 
ATOM   4816 C C     . TYR   F 3 115 ? 1.099   -24.592 3.280   1.00 48.19  ?  115 TYR   F C     1 
ATOM   4817 O O     . TYR   F 3 115 ? 2.081   -25.034 3.862   1.00 46.33  ?  115 TYR   F O     1 
ATOM   4818 C CB    . TYR   F 3 115 ? 0.587   -22.378 4.447   1.00 50.38  ?  115 TYR   F CB    1 
ATOM   4819 C CG    . TYR   F 3 115 ? 0.816   -21.543 3.205   1.00 53.33  ?  115 TYR   F CG    1 
ATOM   4820 C CD1   . TYR   F 3 115 ? 2.054   -21.565 2.556   1.00 53.83  ?  115 TYR   F CD1   1 
ATOM   4821 C CD2   . TYR   F 3 115 ? -0.218  -20.784 2.649   1.00 55.58  ?  115 TYR   F CD2   1 
ATOM   4822 C CE1   . TYR   F 3 115 ? 2.277   -20.807 1.413   1.00 57.02  ?  115 TYR   F CE1   1 
ATOM   4823 C CE2   . TYR   F 3 115 ? -0.009  -20.030 1.505   1.00 58.81  ?  115 TYR   F CE2   1 
ATOM   4824 C CZ    . TYR   F 3 115 ? 1.237   -20.045 0.881   1.00 59.55  ?  115 TYR   F CZ    1 
ATOM   4825 O OH    . TYR   F 3 115 ? 1.428   -19.319 -0.257  1.00 62.96  ?  115 TYR   F OH    1 
ATOM   4826 N N     . PRO   F 3 116 ? 0.989   -24.774 1.933   1.00 50.44  ?  116 PRO   F N     1 
ATOM   4827 C CA    . PRO   F 3 116 ? -0.267  -24.647 1.189   1.00 52.55  ?  116 PRO   F CA    1 
ATOM   4828 C C     . PRO   F 3 116 ? -1.379  -25.542 1.739   1.00 51.42  ?  116 PRO   F C     1 
ATOM   4829 O O     . PRO   F 3 116 ? -1.108  -26.666 2.122   1.00 49.00  ?  116 PRO   F O     1 
ATOM   4830 C CB    . PRO   F 3 116 ? 0.101   -25.003 -0.252  1.00 54.04  ?  116 PRO   F CB    1 
ATOM   4831 C CG    . PRO   F 3 116 ? 1.583   -24.704 -0.322  1.00 53.88  ?  116 PRO   F CG    1 
ATOM   4832 C CD    . PRO   F 3 116 ? 2.143   -24.976 1.043   1.00 50.92  ?  116 PRO   F CD    1 
ATOM   4833 N N     . GLN   F 3 117 ? -2.604  -25.009 1.800   1.00 55.07  ?  117 GLN   F N     1 
ATOM   4834 C CA    . GLN   F 3 117 ? -3.779  -25.665 2.368   1.00 55.77  ?  117 GLN   F CA    1 
ATOM   4835 C C     . GLN   F 3 117 ? -4.087  -26.997 1.680   1.00 54.80  ?  117 GLN   F C     1 
ATOM   4836 O O     . GLN   F 3 117 ? -4.498  -27.921 2.371   1.00 52.75  ?  117 GLN   F O     1 
ATOM   4837 C CB    . GLN   F 3 117 ? -4.965  -24.692 2.320   1.00 60.57  ?  117 GLN   F CB    1 
ATOM   4838 C CG    . GLN   F 3 117 ? -6.170  -25.096 3.171   1.00 62.06  ?  117 GLN   F CG    1 
ATOM   4839 C CD    . GLN   F 3 117 ? -7.249  -25.855 2.421   1.00 64.42  ?  117 GLN   F CD    1 
ATOM   4840 O OE1   . GLN   F 3 117 ? -7.628  -25.499 1.301   1.00 66.98  ?  117 GLN   F OE1   1 
ATOM   4841 N NE2   . GLN   F 3 117 ? -7.776  -26.906 3.035   1.00 63.80  ?  117 GLN   F NE2   1 
ATOM   4842 N N     . ASP   F 3 118 ? -3.842  -27.105 0.363   1.00 55.99  ?  118 ASP   F N     1 
ATOM   4843 C CA    . ASP   F 3 118 ? -4.083  -28.316 -0.408  1.00 56.62  ?  118 ASP   F CA    1 
ATOM   4844 C C     . ASP   F 3 118 ? -2.864  -29.250 -0.486  1.00 55.53  ?  118 ASP   F C     1 
ATOM   4845 O O     . ASP   F 3 118 ? -3.046  -30.367 -0.943  1.00 57.27  ?  118 ASP   F O     1 
ATOM   4846 C CB    . ASP   F 3 118 ? -4.584  -27.941 -1.792  1.00 60.10  ?  118 ASP   F CB    1 
ATOM   4847 C CG    . ASP   F 3 118 ? -5.209  -29.039 -2.641  1.00 61.41  ?  118 ASP   F CG    1 
ATOM   4848 O OD1   . ASP   F 3 118 ? -5.906  -29.924 -2.060  1.00 60.18  ?  118 ASP   F OD1   1 
ATOM   4849 O OD2   . ASP   F 3 118 ? -4.997  -28.986 -3.880  1.00 62.05  -1 118 ASP   F OD2   1 
ATOM   4850 N N     . ASP   F 3 119 ? -1.643  -28.857 -0.055  1.00 52.73  ?  119 ASP   F N     1 
ATOM   4851 C CA    . ASP   F 3 119 ? -0.420  -29.573 -0.416  1.00 51.41  ?  119 ASP   F CA    1 
ATOM   4852 C C     . ASP   F 3 119 ? -0.087  -30.573 0.697   1.00 47.81  ?  119 ASP   F C     1 
ATOM   4853 O O     . ASP   F 3 119 ? 0.202   -30.116 1.812   1.00 45.83  ?  119 ASP   F O     1 
ATOM   4854 C CB    . ASP   F 3 119 ? 0.744   -28.639 -0.711  1.00 53.77  ?  119 ASP   F CB    1 
ATOM   4855 C CG    . ASP   F 3 119 ? 2.042   -29.231 -1.267  1.00 55.09  ?  119 ASP   F CG    1 
ATOM   4856 O OD1   . ASP   F 3 119 ? 2.112   -30.470 -1.466  1.00 55.41  ?  119 ASP   F OD1   1 
ATOM   4857 O OD2   . ASP   F 3 119 ? 2.989   -28.441 -1.516  1.00 55.01  -1 119 ASP   F OD2   1 
ATOM   4858 N N     . PRO   F 3 120 ? -0.080  -31.924 0.450   1.00 44.76  ?  120 PRO   F N     1 
ATOM   4859 C CA    . PRO   F 3 120 ? 0.367   -32.878 1.462   1.00 41.82  ?  120 PRO   F CA    1 
ATOM   4860 C C     . PRO   F 3 120 ? 1.832   -32.720 1.848   1.00 40.70  ?  120 PRO   F C     1 
ATOM   4861 O O     . PRO   F 3 120 ? 2.133   -32.952 2.988   1.00 40.58  ?  120 PRO   F O     1 
ATOM   4862 C CB    . PRO   F 3 120 ? 0.032   -34.230 0.866   1.00 41.80  ?  120 PRO   F CB    1 
ATOM   4863 C CG    . PRO   F 3 120 ? 0.065   -33.998 -0.617  1.00 44.64  ?  120 PRO   F CG    1 
ATOM   4864 C CD    . PRO   F 3 120 ? -0.434  -32.604 -0.814  1.00 46.19  ?  120 PRO   F CD    1 
ATOM   4865 N N     . ASN   F 3 121 ? 2.716   -32.269 0.940   1.00 42.96  ?  121 ASN   F N     1 
ATOM   4866 C CA    . ASN   F 3 121 ? 4.054   -31.782 1.294   1.00 42.99  ?  121 ASN   F CA    1 
ATOM   4867 C C     . ASN   F 3 121 ? 3.969   -30.313 1.739   1.00 43.90  ?  121 ASN   F C     1 
ATOM   4868 O O     . ASN   F 3 121 ? 4.535   -29.425 1.100   1.00 44.98  ?  121 ASN   F O     1 
ATOM   4869 C CB    . ASN   F 3 121 ? 5.063   -32.017 0.167   1.00 44.41  ?  121 ASN   F CB    1 
ATOM   4870 C CG    . ASN   F 3 121 ? 6.488   -31.688 0.568   1.00 44.40  ?  121 ASN   F CG    1 
ATOM   4871 O OD1   . ASN   F 3 121 ? 6.917   -31.986 1.686   1.00 45.05  ?  121 ASN   F OD1   1 
ATOM   4872 N ND2   . ASN   F 3 121 ? 7.245   -31.038 -0.292  1.00 47.02  ?  121 ASN   F ND2   1 
ATOM   4873 N N     . TYR   F 3 122 ? 3.328   -30.073 2.887   1.00 42.15  ?  122 TYR   F N     1 
ATOM   4874 C CA    . TYR   F 3 122 ? 3.059   -28.719 3.358   1.00 43.40  ?  122 TYR   F CA    1 
ATOM   4875 C C     . TYR   F 3 122 ? 4.350   -28.100 3.916   1.00 43.38  ?  122 TYR   F C     1 
ATOM   4876 O O     . TYR   F 3 122 ? 5.166   -28.777 4.546   1.00 41.62  ?  122 TYR   F O     1 
ATOM   4877 C CB    . TYR   F 3 122 ? 1.933   -28.605 4.395   1.00 42.38  ?  122 TYR   F CB    1 
ATOM   4878 C CG    . TYR   F 3 122 ? 2.072   -29.499 5.614   1.00 40.22  ?  122 TYR   F CG    1 
ATOM   4879 C CD1   . TYR   F 3 122 ? 2.860   -29.126 6.697   1.00 39.42  ?  122 TYR   F CD1   1 
ATOM   4880 C CD2   . TYR   F 3 122 ? 1.420   -30.730 5.651   1.00 38.54  ?  122 TYR   F CD2   1 
ATOM   4881 C CE1   . TYR   F 3 122 ? 2.999   -29.970 7.790   1.00 38.29  ?  122 TYR   F CE1   1 
ATOM   4882 C CE2   . TYR   F 3 122 ? 1.547   -31.575 6.737   1.00 38.47  ?  122 TYR   F CE2   1 
ATOM   4883 C CZ    . TYR   F 3 122 ? 2.326   -31.183 7.814   1.00 37.57  ?  122 TYR   F CZ    1 
ATOM   4884 O OH    . TYR   F 3 122 ? 2.451   -32.021 8.849   1.00 36.35  ?  122 TYR   F OH    1 
ATOM   4885 N N     . ALA   F 3 123 ? 4.489   -26.787 3.708   1.00 45.31  ?  123 ALA   F N     1 
ATOM   4886 C CA    . ALA   F 3 123 ? 5.553   -25.980 4.287   1.00 46.37  ?  123 ALA   F CA    1 
ATOM   4887 C C     . ALA   F 3 123 ? 5.343   -25.803 5.786   1.00 44.52  ?  123 ALA   F C     1 
ATOM   4888 O O     . ALA   F 3 123 ? 6.327   -25.776 6.508   1.00 44.13  ?  123 ALA   F O     1 
ATOM   4889 C CB    . ALA   F 3 123 ? 5.642   -24.622 3.603   1.00 49.57  ?  123 ALA   F CB    1 
ATOM   4890 N N     . ILE   F 3 124 ? 4.093   -25.615 6.230   1.00 43.64  ?  124 ILE   F N     1 
ATOM   4891 C CA    . ILE   F 3 124 ? 3.831   -25.369 7.643   1.00 42.87  ?  124 ILE   F CA    1 
ATOM   4892 C C     . ILE   F 3 124 ? 2.408   -25.814 7.972   1.00 41.96  ?  124 ILE   F C     1 
ATOM   4893 O O     . ILE   F 3 124 ? 1.520   -25.667 7.149   1.00 41.92  ?  124 ILE   F O     1 
ATOM   4894 C CB    . ILE   F 3 124 ? 4.112   -23.888 8.020   1.00 44.66  ?  124 ILE   F CB    1 
ATOM   4895 C CG1   . ILE   F 3 124 ? 4.054   -23.647 9.548   1.00 43.95  ?  124 ILE   F CG1   1 
ATOM   4896 C CG2   . ILE   F 3 124 ? 3.221   -22.886 7.278   1.00 46.52  ?  124 ILE   F CG2   1 
ATOM   4897 C CD1   . ILE   F 3 124 ? 5.187   -24.311 10.306  1.00 42.85  ?  124 ILE   F CD1   1 
ATOM   4898 N N     . ARG   F 3 125 ? 2.262   -26.432 9.151   1.00 41.43  ?  125 ARG   F N     1 
ATOM   4899 C CA    . ARG   F 3 125 ? 1.016   -26.611 9.880   1.00 41.56  ?  125 ARG   F CA    1 
ATOM   4900 C C     . ARG   F 3 125 ? 1.195   -25.984 11.257  1.00 41.04  ?  125 ARG   F C     1 
ATOM   4901 O O     . ARG   F 3 125 ? 2.290   -26.055 11.814  1.00 40.59  ?  125 ARG   F O     1 
ATOM   4902 C CB    . ARG   F 3 125 ? 0.703   -28.092 10.135  1.00 39.06  ?  125 ARG   F CB    1 
ATOM   4903 C CG    . ARG   F 3 125 ? -0.085  -28.698 8.998   1.00 39.31  ?  125 ARG   F CG    1 
ATOM   4904 C CD    . ARG   F 3 125 ? -0.547  -30.077 9.326   1.00 36.26  ?  125 ARG   F CD    1 
ATOM   4905 N NE    . ARG   F 3 125 ? -1.074  -30.747 8.139   1.00 36.01  ?  125 ARG   F NE    1 
ATOM   4906 C CZ    . ARG   F 3 125 ? -1.468  -32.012 8.083   1.00 34.31  ?  125 ARG   F CZ    1 
ATOM   4907 N NH1   . ARG   F 3 125 ? -1.276  -32.818 9.116   1.00 31.56  1  125 ARG   F NH1   1 
ATOM   4908 N NH2   . ARG   F 3 125 ? -2.024  -32.475 6.966   1.00 35.38  ?  125 ARG   F NH2   1 
ATOM   4909 N N     . VAL   F 3 126 ? 0.102   -25.447 11.808  1.00 42.62  ?  126 VAL   F N     1 
ATOM   4910 C CA    . VAL   F 3 126 ? 0.128   -24.724 13.076  1.00 42.78  ?  126 VAL   F CA    1 
ATOM   4911 C C     . VAL   F 3 126 ? -1.250  -24.874 13.725  1.00 43.09  ?  126 VAL   F C     1 
ATOM   4912 O O     . VAL   F 3 126 ? -2.268  -24.859 13.019  1.00 44.05  ?  126 VAL   F O     1 
ATOM   4913 C CB    . VAL   F 3 126 ? 0.590   -23.249 12.892  1.00 44.16  ?  126 VAL   F CB    1 
ATOM   4914 C CG1   . VAL   F 3 126 ? -0.343  -22.419 12.018  1.00 46.65  ?  126 VAL   F CG1   1 
ATOM   4915 C CG2   . VAL   F 3 126 ? 0.886   -22.544 14.211  1.00 43.82  ?  126 VAL   F CG2   1 
ATOM   4916 N N     . TRP   F 3 127 ? -1.254  -25.037 15.065  1.00 43.02  ?  127 TRP   F N     1 
ATOM   4917 C CA    . TRP   F 3 127 ? -2.459  -25.259 15.858  1.00 42.01  ?  127 TRP   F CA    1 
ATOM   4918 C C     . TRP   F 3 127 ? -2.270  -24.704 17.276  1.00 42.77  ?  127 TRP   F C     1 
ATOM   4919 O O     . TRP   F 3 127 ? -1.179  -24.820 17.823  1.00 40.81  ?  127 TRP   F O     1 
ATOM   4920 C CB    . TRP   F 3 127 ? -2.762  -26.757 15.900  1.00 39.05  ?  127 TRP   F CB    1 
ATOM   4921 C CG    . TRP   F 3 127 ? -3.943  -27.157 16.747  1.00 38.54  ?  127 TRP   F CG    1 
ATOM   4922 C CD1   . TRP   F 3 127 ? -5.262  -27.151 16.388  1.00 39.43  ?  127 TRP   F CD1   1 
ATOM   4923 C CD2   . TRP   F 3 127 ? -3.891  -27.704 18.080  1.00 37.50  ?  127 TRP   F CD2   1 
ATOM   4924 N NE1   . TRP   F 3 127 ? -6.039  -27.608 17.418  1.00 39.05  ?  127 TRP   F NE1   1 
ATOM   4925 C CE2   . TRP   F 3 127 ? -5.233  -27.966 18.464  1.00 37.91  ?  127 TRP   F CE2   1 
ATOM   4926 C CE3   . TRP   F 3 127 ? -2.851  -27.978 18.992  1.00 37.19  ?  127 TRP   F CE3   1 
ATOM   4927 C CZ2   . TRP   F 3 127 ? -5.555  -28.510 19.712  1.00 38.01  ?  127 TRP   F CZ2   1 
ATOM   4928 C CZ3   . TRP   F 3 127 ? -3.161  -28.551 20.217  1.00 37.07  ?  127 TRP   F CZ3   1 
ATOM   4929 C CH2   . TRP   F 3 127 ? -4.501  -28.830 20.563  1.00 37.98  ?  127 TRP   F CH2   1 
ATOM   4930 N N     . LYS   F 3 128 ? -3.357  -24.186 17.877  1.00 45.76  ?  128 LYS   F N     1 
ATOM   4931 C CA    . LYS   F 3 128 ? -3.333  -23.493 19.163  1.00 47.46  ?  128 LYS   F CA    1 
ATOM   4932 C C     . LYS   F 3 128 ? -4.482  -24.003 20.041  1.00 46.39  ?  128 LYS   F C     1 
ATOM   4933 O O     . LYS   F 3 128 ? -5.624  -24.148 19.569  1.00 47.55  ?  128 LYS   F O     1 
ATOM   4934 C CB    . LYS   F 3 128 ? -3.361  -21.966 18.964  1.00 51.11  ?  128 LYS   F CB    1 
ATOM   4935 C CG    . LYS   F 3 128 ? -3.514  -21.093 20.206  1.00 52.70  ?  128 LYS   F CG    1 
ATOM   4936 C CD    . LYS   F 3 128 ? -3.297  -19.597 19.964  1.00 56.35  ?  128 LYS   F CD    1 
ATOM   4937 C CE    . LYS   F 3 128 ? -3.033  -18.805 21.220  1.00 57.49  ?  128 LYS   F CE    1 
ATOM   4938 N NZ    . LYS   F 3 128 ? -2.286  -17.583 20.927  1.00 60.82  1  128 LYS   F NZ    1 
ATOM   4939 N N     . SER   F 3 129 ? -4.163  -24.222 21.323  1.00 43.42  ?  129 SER   F N     1 
ATOM   4940 C CA    . SER   F 3 129 ? -5.123  -24.581 22.357  1.00 44.12  ?  129 SER   F CA    1 
ATOM   4941 C C     . SER   F 3 129 ? -4.650  -23.925 23.653  1.00 44.81  ?  129 SER   F C     1 
ATOM   4942 O O     . SER   F 3 129 ? -3.482  -24.118 24.015  1.00 43.13  ?  129 SER   F O     1 
ATOM   4943 C CB    . SER   F 3 129 ? -5.217  -26.077 22.500  1.00 42.35  ?  129 SER   F CB    1 
ATOM   4944 O OG    . SER   F 3 129 ? -6.118  -26.441 23.530  1.00 42.03  ?  129 SER   F OG    1 
ATOM   4945 N N     . GLY   F 3 130 ? -5.513  -23.071 24.256  1.00 48.17  ?  130 GLY   F N     1 
ATOM   4946 C CA    . GLY   F 3 130 ? -5.105  -22.137 25.293  1.00 49.05  ?  130 GLY   F CA    1 
ATOM   4947 C C     . GLY   F 3 130 ? -3.906  -21.339 24.793  1.00 50.70  ?  130 GLY   F C     1 
ATOM   4948 O O     . GLY   F 3 130 ? -3.961  -20.829 23.669  1.00 51.44  ?  130 GLY   F O     1 
ATOM   4949 N N     . ASP   F 3 131 ? -2.799  -21.353 25.557  1.00 49.94  ?  131 ASP   F N     1 
ATOM   4950 C CA    . ASP   F 3 131 ? -1.567  -20.672 25.173  1.00 51.24  ?  131 ASP   F CA    1 
ATOM   4951 C C     . ASP   F 3 131 ? -0.543  -21.604 24.503  1.00 50.08  ?  131 ASP   F C     1 
ATOM   4952 O O     . ASP   F 3 131 ? 0.534   -21.115 24.151  1.00 53.38  ?  131 ASP   F O     1 
ATOM   4953 C CB    . ASP   F 3 131 ? -1.019  -19.871 26.348  1.00 54.00  ?  131 ASP   F CB    1 
ATOM   4954 C CG    . ASP   F 3 131 ? -1.978  -18.905 27.056  1.00 55.94  ?  131 ASP   F CG    1 
ATOM   4955 O OD1   . ASP   F 3 131 ? -2.623  -18.107 26.360  1.00 56.61  ?  131 ASP   F OD1   1 
ATOM   4956 O OD2   . ASP   F 3 131 ? -2.082  -18.964 28.306  1.00 56.83  -1 131 ASP   F OD2   1 
ATOM   4957 N N     . LEU   F 3 132 ? -0.838  -22.913 24.317  1.00 48.22  ?  132 LEU   F N     1 
ATOM   4958 C CA    . LEU   F 3 132 ? 0.032   -23.831 23.580  1.00 45.56  ?  132 LEU   F CA    1 
ATOM   4959 C C     . LEU   F 3 132 ? -0.137  -23.546 22.091  1.00 44.31  ?  132 LEU   F C     1 
ATOM   4960 O O     . LEU   F 3 132 ? -1.274  -23.573 21.611  1.00 42.06  ?  132 LEU   F O     1 
ATOM   4961 C CB    . LEU   F 3 132 ? -0.304  -25.306 23.847  1.00 44.54  ?  132 LEU   F CB    1 
ATOM   4962 C CG    . LEU   F 3 132 ? 0.422   -26.369 23.003  1.00 42.52  ?  132 LEU   F CG    1 
ATOM   4963 C CD1   . LEU   F 3 132 ? 1.920   -26.444 23.246  1.00 43.63  ?  132 LEU   F CD1   1 
ATOM   4964 C CD2   . LEU   F 3 132 ? -0.209  -27.694 23.253  1.00 43.36  ?  132 LEU   F CD2   1 
ATOM   4965 N N     . VAL   F 3 133 ? 0.991   -23.378 21.377  1.00 43.79  ?  133 VAL   F N     1 
ATOM   4966 C CA    . VAL   F 3 133 ? 1.016   -23.433 19.920  1.00 43.12  ?  133 VAL   F CA    1 
ATOM   4967 C C     . VAL   F 3 133 ? 1.968   -24.557 19.520  1.00 40.53  ?  133 VAL   F C     1 
ATOM   4968 O O     . VAL   F 3 133 ? 3.097   -24.577 19.999  1.00 42.20  ?  133 VAL   F O     1 
ATOM   4969 C CB    . VAL   F 3 133 ? 1.395   -22.119 19.211  1.00 43.17  ?  133 VAL   F CB    1 
ATOM   4970 C CG1   . VAL   F 3 133 ? 1.310   -22.248 17.680  1.00 42.86  ?  133 VAL   F CG1   1 
ATOM   4971 C CG2   . VAL   F 3 133 ? 0.526   -20.968 19.699  1.00 45.25  ?  133 VAL   F CG2   1 
ATOM   4972 N N     . MET   F 3 134 ? 1.529   -25.420 18.603  1.00 38.79  ?  134 MET   F N     1 
ATOM   4973 C CA    . MET   F 3 134 ? 2.386   -26.413 17.959  1.00 38.39  ?  134 MET   F CA    1 
ATOM   4974 C C     . MET   F 3 134 ? 2.564   -26.040 16.491  1.00 38.99  ?  134 MET   F C     1 
ATOM   4975 O O     . MET   F 3 134 ? 1.669   -25.455 15.884  1.00 39.47  ?  134 MET   F O     1 
ATOM   4976 C CB    . MET   F 3 134 ? 1.768   -27.811 18.066  1.00 37.08  ?  134 MET   F CB    1 
ATOM   4977 C CG    . MET   F 3 134 ? 1.722   -28.399 19.483  1.00 35.56  ?  134 MET   F CG    1 
ATOM   4978 S SD    . MET   F 3 134 ? 1.389   -30.172 19.583  1.00 35.16  ?  134 MET   F SD    1 
ATOM   4979 C CE    . MET   F 3 134 ? 2.345   -31.133 18.444  1.00 35.43  ?  134 MET   F CE    1 
ATOM   4980 N N     . ALA   F 3 135 ? 3.732   -26.372 15.932  1.00 39.49  ?  135 ALA   F N     1 
ATOM   4981 C CA    . ALA   F 3 135 ? 3.996   -26.173 14.518  1.00 40.50  ?  135 ALA   F CA    1 
ATOM   4982 C C     . ALA   F 3 135 ? 4.892   -27.279 13.984  1.00 38.68  ?  135 ALA   F C     1 
ATOM   4983 O O     . ALA   F 3 135 ? 5.801   -27.698 14.690  1.00 38.64  ?  135 ALA   F O     1 
ATOM   4984 C CB    . ALA   F 3 135 ? 4.631   -24.829 14.305  1.00 44.08  ?  135 ALA   F CB    1 
ATOM   4985 N N     . TYR   F 3 136 ? 4.629   -27.724 12.744  1.00 38.90  ?  136 TYR   F N     1 
ATOM   4986 C CA    . TYR   F 3 136 ? 5.494   -28.672 12.055  1.00 37.44  ?  136 TYR   F CA    1 
ATOM   4987 C C     . TYR   F 3 136 ? 5.542   -28.361 10.563  1.00 38.61  ?  136 TYR   F C     1 
ATOM   4988 O O     . TYR   F 3 136 ? 4.551   -27.911 9.999   1.00 38.11  ?  136 TYR   F O     1 
ATOM   4989 C CB    . TYR   F 3 136 ? 4.979   -30.096 12.309  1.00 36.28  ?  136 TYR   F CB    1 
ATOM   4990 C CG    . TYR   F 3 136 ? 5.909   -31.169 11.766  1.00 34.29  ?  136 TYR   F CG    1 
ATOM   4991 C CD1   . TYR   F 3 136 ? 7.120   -31.424 12.393  1.00 33.75  ?  136 TYR   F CD1   1 
ATOM   4992 C CD2   . TYR   F 3 136 ? 5.611   -31.865 10.587  1.00 35.29  ?  136 TYR   F CD2   1 
ATOM   4993 C CE1   . TYR   F 3 136 ? 7.997   -32.382 11.911  1.00 34.70  ?  136 TYR   F CE1   1 
ATOM   4994 C CE2   . TYR   F 3 136 ? 6.478   -32.831 10.089  1.00 34.28  ?  136 TYR   F CE2   1 
ATOM   4995 C CZ    . TYR   F 3 136 ? 7.673   -33.086 10.757  1.00 34.82  ?  136 TYR   F CZ    1 
ATOM   4996 O OH    . TYR   F 3 136 ? 8.554   -34.043 10.357  1.00 35.42  ?  136 TYR   F OH    1 
ATOM   4997 N N     . SER   F 3 137 ? 6.697   -28.647 9.946   1.00 38.06  ?  137 SER   F N     1 
ATOM   4998 C CA    . SER   F 3 137 ? 6.902   -28.528 8.512   1.00 38.54  ?  137 SER   F CA    1 
ATOM   4999 C C     . SER   F 3 137 ? 7.282   -29.903 7.969   1.00 37.21  ?  137 SER   F C     1 
ATOM   5000 O O     . SER   F 3 137 ? 8.321   -30.420 8.342   1.00 34.95  ?  137 SER   F O     1 
ATOM   5001 C CB    . SER   F 3 137 ? 7.980   -27.543 8.259   1.00 39.47  ?  137 SER   F CB    1 
ATOM   5002 O OG    . SER   F 3 137 ? 8.305   -27.522 6.877   1.00 40.47  ?  137 SER   F OG    1 
ATOM   5003 N N     . ARG   F 3 138 ? 6.480   -30.451 7.058   1.00 38.64  ?  138 ARG   F N     1 
ATOM   5004 C CA    . ARG   F 3 138 ? 6.863   -31.632 6.299   1.00 40.47  ?  138 ARG   F CA    1 
ATOM   5005 C C     . ARG   F 3 138 ? 8.056   -31.382 5.369   1.00 41.17  ?  138 ARG   F C     1 
ATOM   5006 O O     . ARG   F 3 138 ? 8.789   -32.334 5.132   1.00 39.35  ?  138 ARG   F O     1 
ATOM   5007 C CB    . ARG   F 3 138 ? 5.685   -32.217 5.509   1.00 43.96  ?  138 ARG   F CB    1 
ATOM   5008 C CG    . ARG   F 3 138 ? 4.912   -33.243 6.325   1.00 47.39  ?  138 ARG   F CG    1 
ATOM   5009 C CD    . ARG   F 3 138 ? 3.819   -33.981 5.563   1.00 53.14  ?  138 ARG   F CD    1 
ATOM   5010 N NE    . ARG   F 3 138 ? 4.300   -34.562 4.295   1.00 59.87  ?  138 ARG   F NE    1 
ATOM   5011 C CZ    . ARG   F 3 138 ? 4.648   -35.825 4.016   1.00 62.71  ?  138 ARG   F CZ    1 
ATOM   5012 N NH1   . ARG   F 3 138 ? 5.090   -36.128 2.808   1.00 67.14  1  138 ARG   F NH1   1 
ATOM   5013 N NH2   . ARG   F 3 138 ? 4.589   -36.773 4.934   1.00 63.68  ?  138 ARG   F NH2   1 
ATOM   5014 N N     . ARG   F 3 139 ? 8.280   -30.146 4.884   1.00 41.42  ?  139 ARG   F N     1 
ATOM   5015 C CA    . ARG   F 3 139 ? 9.401   -29.874 3.996   1.00 43.51  ?  139 ARG   F CA    1 
ATOM   5016 C C     . ARG   F 3 139 ? 10.735  -29.970 4.738   1.00 43.30  ?  139 ARG   F C     1 
ATOM   5017 O O     . ARG   F 3 139 ? 11.612  -30.687 4.278   1.00 45.46  ?  139 ARG   F O     1 
ATOM   5018 C CB    . ARG   F 3 139 ? 9.210   -28.558 3.234   1.00 45.58  ?  139 ARG   F CB    1 
ATOM   5019 C CG    . ARG   F 3 139 ? 8.039   -28.647 2.268   1.00 45.51  ?  139 ARG   F CG    1 
ATOM   5020 C CD    . ARG   F 3 139 ? 7.908   -27.409 1.394   1.00 47.19  ?  139 ARG   F CD    1 
ATOM   5021 N NE    . ARG   F 3 139 ? 6.580   -27.331 0.772   1.00 47.30  ?  139 ARG   F NE    1 
ATOM   5022 C CZ    . ARG   F 3 139 ? 6.073   -26.301 0.082   1.00 49.08  ?  139 ARG   F CZ    1 
ATOM   5023 N NH1   . ARG   F 3 139 ? 6.758   -25.180 -0.069  1.00 50.39  1  139 ARG   F NH1   1 
ATOM   5024 N NH2   . ARG   F 3 139 ? 4.864   -26.393 -0.445  1.00 49.39  ?  139 ARG   F NH2   1 
ATOM   5025 N N     . THR   F 3 140 ? 10.862  -29.300 5.887   1.00 42.91  ?  140 THR   F N     1 
ATOM   5026 C CA    . THR   F 3 140 ? 12.110  -29.232 6.651   1.00 43.07  ?  140 THR   F CA    1 
ATOM   5027 C C     . THR   F 3 140 ? 12.211  -30.316 7.724   1.00 41.68  ?  140 THR   F C     1 
ATOM   5028 O O     . THR   F 3 140 ? 13.324  -30.545 8.214   1.00 43.11  ?  140 THR   F O     1 
ATOM   5029 C CB    . THR   F 3 140 ? 12.220  -27.844 7.275   1.00 43.47  ?  140 THR   F CB    1 
ATOM   5030 O OG1   . THR   F 3 140 ? 11.095  -27.635 8.105   1.00 40.76  ?  140 THR   F OG1   1 
ATOM   5031 C CG2   . THR   F 3 140 ? 12.217  -26.737 6.238   1.00 45.81  ?  140 THR   F CG2   1 
ATOM   5032 N N     . ALA   F 3 141 ? 11.061  -30.900 8.145   1.00 39.34  ?  141 ALA   F N     1 
ATOM   5033 C CA    . ALA   F 3 141 ? 10.932  -31.748 9.330   1.00 39.45  ?  141 ALA   F CA    1 
ATOM   5034 C C     . ALA   F 3 141 ? 11.302  -31.045 10.649  1.00 37.92  ?  141 ALA   F C     1 
ATOM   5035 O O     . ALA   F 3 141 ? 11.528  -31.729 11.637  1.00 37.76  ?  141 ALA   F O     1 
ATOM   5036 C CB    . ALA   F 3 141 ? 11.653  -33.076 9.119   1.00 38.48  ?  141 ALA   F CB    1 
ATOM   5037 N N     . VAL   F 3 142 ? 11.221  -29.709 10.713  1.00 38.44  ?  142 VAL   F N     1 
ATOM   5038 C CA    . VAL   F 3 142 ? 11.410  -28.964 11.950  1.00 38.69  ?  142 VAL   F CA    1 
ATOM   5039 C C     . VAL   F 3 142 ? 10.049  -28.923 12.646  1.00 36.07  ?  142 VAL   F C     1 
ATOM   5040 O O     . VAL   F 3 142 ? 9.031   -28.544 12.046  1.00 36.53  ?  142 VAL   F O     1 
ATOM   5041 C CB    . VAL   F 3 142 ? 11.997  -27.560 11.744  1.00 42.10  ?  142 VAL   F CB    1 
ATOM   5042 C CG1   . VAL   F 3 142 ? 12.002  -26.749 13.042  1.00 43.58  ?  142 VAL   F CG1   1 
ATOM   5043 C CG2   . VAL   F 3 142 ? 13.393  -27.683 11.136  1.00 43.80  ?  142 VAL   F CG2   1 
ATOM   5044 N N     . TYR   F 3 143 ? 10.056  -29.376 13.895  1.00 33.67  ?  143 TYR   F N     1 
ATOM   5045 C CA    . TYR   F 3 143 ? 8.952   -29.221 14.819  1.00 32.64  ?  143 TYR   F CA    1 
ATOM   5046 C C     . TYR   F 3 143 ? 9.287   -28.083 15.778  1.00 34.04  ?  143 TYR   F C     1 
ATOM   5047 O O     . TYR   F 3 143 ? 10.445  -27.916 16.199  1.00 34.59  ?  143 TYR   F O     1 
ATOM   5048 C CB    . TYR   F 3 143 ? 8.802   -30.501 15.644  1.00 29.67  ?  143 TYR   F CB    1 
ATOM   5049 C CG    . TYR   F 3 143 ? 7.740   -30.408 16.721  1.00 28.07  ?  143 TYR   F CG    1 
ATOM   5050 C CD1   . TYR   F 3 143 ? 6.396   -30.554 16.419  1.00 27.25  ?  143 TYR   F CD1   1 
ATOM   5051 C CD2   . TYR   F 3 143 ? 8.092   -30.175 18.049  1.00 27.93  ?  143 TYR   F CD2   1 
ATOM   5052 C CE1   . TYR   F 3 143 ? 5.433   -30.438 17.397  1.00 26.64  ?  143 TYR   F CE1   1 
ATOM   5053 C CE2   . TYR   F 3 143 ? 7.138   -30.043 19.040  1.00 27.41  ?  143 TYR   F CE2   1 
ATOM   5054 C CZ    . TYR   F 3 143 ? 5.800   -30.197 18.716  1.00 27.16  ?  143 TYR   F CZ    1 
ATOM   5055 O OH    . TYR   F 3 143 ? 4.898   -30.133 19.749  1.00 28.27  ?  143 TYR   F OH    1 
ATOM   5056 N N     . ALA   F 3 144 ? 8.240   -27.389 16.207  1.00 33.93  ?  144 ALA   F N     1 
ATOM   5057 C CA    . ALA   F 3 144 ? 8.375   -26.459 17.307  1.00 35.25  ?  144 ALA   F CA    1 
ATOM   5058 C C     . ALA   F 3 144 ? 7.093   -26.422 18.113  1.00 34.40  ?  144 ALA   F C     1 
ATOM   5059 O O     . ALA   F 3 144 ? 6.030   -26.680 17.555  1.00 32.71  ?  144 ALA   F O     1 
ATOM   5060 C CB    . ALA   F 3 144 ? 8.717   -25.075 16.761  1.00 37.83  ?  144 ALA   F CB    1 
ATOM   5061 N N     . TYR   F 3 145 ? 7.209   -26.035 19.385  1.00 35.28  ?  145 TYR   F N     1 
ATOM   5062 C CA    . TYR   F 3 145 ? 6.043   -25.592 20.137  1.00 36.90  ?  145 TYR   F CA    1 
ATOM   5063 C C     . TYR   F 3 145 ? 6.391   -24.414 21.046  1.00 38.63  ?  145 TYR   F C     1 
ATOM   5064 O O     . TYR   F 3 145 ? 7.536   -24.274 21.474  1.00 39.24  ?  145 TYR   F O     1 
ATOM   5065 C CB    . TYR   F 3 145 ? 5.408   -26.759 20.904  1.00 35.30  ?  145 TYR   F CB    1 
ATOM   5066 C CG    . TYR   F 3 145 ? 5.972   -27.182 22.257  1.00 34.50  ?  145 TYR   F CG    1 
ATOM   5067 C CD1   . TYR   F 3 145 ? 5.436   -26.682 23.444  1.00 35.45  ?  145 TYR   F CD1   1 
ATOM   5068 C CD2   . TYR   F 3 145 ? 6.967   -28.156 22.357  1.00 34.08  ?  145 TYR   F CD2   1 
ATOM   5069 C CE1   . TYR   F 3 145 ? 5.897   -27.108 24.680  1.00 35.08  ?  145 TYR   F CE1   1 
ATOM   5070 C CE2   . TYR   F 3 145 ? 7.445   -28.588 23.589  1.00 33.19  ?  145 TYR   F CE2   1 
ATOM   5071 C CZ    . TYR   F 3 145 ? 6.889   -28.079 24.750  1.00 33.78  ?  145 TYR   F CZ    1 
ATOM   5072 O OH    . TYR   F 3 145 ? 7.386   -28.480 25.938  1.00 33.91  ?  145 TYR   F OH    1 
ATOM   5073 N N     . TYR   F 3 146 ? 5.333   -23.689 21.432  1.00 40.80  ?  146 TYR   F N     1 
ATOM   5074 C CA    . TYR   F 3 146 ? 5.427   -22.336 21.976  1.00 46.09  ?  146 TYR   F CA    1 
ATOM   5075 C C     . TYR   F 3 146 ? 4.377   -22.134 23.071  1.00 47.20  ?  146 TYR   F C     1 
ATOM   5076 O O     . TYR   F 3 146 ? 3.225   -22.535 22.873  1.00 46.78  ?  146 TYR   F O     1 
ATOM   5077 C CB    . TYR   F 3 146 ? 5.272   -21.339 20.821  1.00 48.18  ?  146 TYR   F CB    1 
ATOM   5078 C CG    . TYR   F 3 146 ? 4.948   -19.887 21.148  1.00 51.58  ?  146 TYR   F CG    1 
ATOM   5079 C CD1   . TYR   F 3 146 ? 5.973   -18.962 21.347  1.00 56.09  ?  146 TYR   F CD1   1 
ATOM   5080 C CD2   . TYR   F 3 146 ? 3.626   -19.424 21.203  1.00 52.11  ?  146 TYR   F CD2   1 
ATOM   5081 C CE1   . TYR   F 3 146 ? 5.699   -17.620 21.594  1.00 59.49  ?  146 TYR   F CE1   1 
ATOM   5082 C CE2   . TYR   F 3 146 ? 3.333   -18.091 21.457  1.00 56.35  ?  146 TYR   F CE2   1 
ATOM   5083 C CZ    . TYR   F 3 146 ? 4.374   -17.181 21.641  1.00 60.75  ?  146 TYR   F CZ    1 
ATOM   5084 O OH    . TYR   F 3 146 ? 4.101   -15.865 21.925  1.00 65.82  ?  146 TYR   F OH    1 
ATOM   5085 N N     . THR   F 3 147 ? 4.790   -21.471 24.174  1.00 49.25  ?  147 THR   F N     1 
ATOM   5086 C CA    . THR   F 3 147 ? 3.944   -21.184 25.335  1.00 51.83  ?  147 THR   F CA    1 
ATOM   5087 C C     . THR   F 3 147 ? 3.626   -19.692 25.524  1.00 54.65  ?  147 THR   F C     1 
ATOM   5088 O O     . THR   F 3 147 ? 2.802   -19.378 26.380  1.00 55.03  ?  147 THR   F O     1 
ATOM   5089 C CB    . THR   F 3 147 ? 4.667   -21.703 26.578  1.00 52.42  ?  147 THR   F CB    1 
ATOM   5090 O OG1   . THR   F 3 147 ? 5.856   -20.939 26.772  1.00 53.94  ?  147 THR   F OG1   1 
ATOM   5091 C CG2   . THR   F 3 147 ? 5.051   -23.167 26.464  1.00 51.37  ?  147 THR   F CG2   1 
ATOM   5092 N N     . GLY   F 3 148 ? 4.320   -18.774 24.824  1.00 56.51  ?  148 GLY   F N     1 
ATOM   5093 C CA    . GLY   F 3 148 ? 4.367   -17.363 25.192  1.00 60.72  ?  148 GLY   F CA    1 
ATOM   5094 C C     . GLY   F 3 148 ? 5.575   -16.988 26.054  1.00 61.75  ?  148 GLY   F C     1 
ATOM   5095 O O     . GLY   F 3 148 ? 6.045   -15.857 25.924  1.00 62.08  ?  148 GLY   F O     1 
ATOM   5096 N N     . THR   F 3 149 ? 6.028   -17.903 26.940  1.00 59.36  ?  149 THR   F N     1 
ATOM   5097 C CA    . THR   F 3 149 ? 7.200   -17.713 27.788  1.00 60.57  ?  149 THR   F CA    1 
ATOM   5098 C C     . THR   F 3 149 ? 8.445   -18.326 27.140  1.00 58.61  ?  149 THR   F C     1 
ATOM   5099 O O     . THR   F 3 149 ? 9.549   -17.806 27.348  1.00 63.14  ?  149 THR   F O     1 
ATOM   5100 C CB    . THR   F 3 149 ? 6.951   -18.287 29.186  1.00 59.73  ?  149 THR   F CB    1 
ATOM   5101 O OG1   . THR   F 3 149 ? 5.556   -18.267 29.466  1.00 58.34  ?  149 THR   F OG1   1 
ATOM   5102 C CG2   . THR   F 3 149 ? 7.667   -17.468 30.248  1.00 64.38  ?  149 THR   F CG2   1 
ATOM   5103 N N     . ALA   F 3 150 ? 8.279   -19.435 26.397  1.00 55.19  ?  150 ALA   F N     1 
ATOM   5104 C CA    . ALA   F 3 150 ? 9.384   -20.079 25.701  1.00 52.34  ?  150 ALA   F CA    1 
ATOM   5105 C C     . ALA   F 3 150 ? 8.903   -20.782 24.438  1.00 50.00  ?  150 ALA   F C     1 
ATOM   5106 O O     . ALA   F 3 150 ? 7.700   -20.986 24.219  1.00 47.63  ?  150 ALA   F O     1 
ATOM   5107 C CB    . ALA   F 3 150 ? 10.054  -21.058 26.629  1.00 50.61  ?  150 ALA   F CB    1 
ATOM   5108 N N     . VAL   F 3 151 ? 9.896   -21.153 23.623  1.00 49.17  ?  151 VAL   F N     1 
ATOM   5109 C CA    . VAL   F 3 151 ? 9.679   -21.958 22.438  1.00 46.76  ?  151 VAL   F CA    1 
ATOM   5110 C C     . VAL   F 3 151 ? 10.700  -23.086 22.470  1.00 44.67  ?  151 VAL   F C     1 
ATOM   5111 O O     . VAL   F 3 151 ? 11.834  -22.881 22.905  1.00 44.59  ?  151 VAL   F O     1 
ATOM   5112 C CB    . VAL   F 3 151 ? 9.713   -21.134 21.129  1.00 48.53  ?  151 VAL   F CB    1 
ATOM   5113 C CG1   . VAL   F 3 151 ? 11.014  -20.419 20.911  1.00 50.47  ?  151 VAL   F CG1   1 
ATOM   5114 C CG2   . VAL   F 3 151 ? 9.399   -21.944 19.876  1.00 47.19  ?  151 VAL   F CG2   1 
ATOM   5115 N N     . ASP   F 3 152 ? 10.231  -24.269 22.026  1.00 43.61  ?  152 ASP   F N     1 
ATOM   5116 C CA    . ASP   F 3 152 ? 11.038  -25.426 21.715  1.00 42.60  ?  152 ASP   F CA    1 
ATOM   5117 C C     . ASP   F 3 152 ? 11.168  -25.458 20.199  1.00 42.48  ?  152 ASP   F C     1 
ATOM   5118 O O     . ASP   F 3 152 ? 10.142  -25.516 19.546  1.00 42.11  ?  152 ASP   F O     1 
ATOM   5119 C CB    . ASP   F 3 152 ? 10.359  -26.685 22.248  1.00 39.91  ?  152 ASP   F CB    1 
ATOM   5120 C CG    . ASP   F 3 152 ? 10.942  -28.022 21.825  1.00 37.86  ?  152 ASP   F CG    1 
ATOM   5121 O OD1   . ASP   F 3 152 ? 12.156  -28.086 21.524  1.00 40.13  ?  152 ASP   F OD1   1 
ATOM   5122 O OD2   . ASP   F 3 152 ? 10.170  -28.972 21.777  1.00 34.92  -1 152 ASP   F OD2   1 
ATOM   5123 N N     . VAL   F 3 153 ? 12.394  -25.449 19.660  1.00 44.14  ?  153 VAL   F N     1 
ATOM   5124 C CA    . VAL   F 3 153 ? 12.646  -25.636 18.233  1.00 43.70  ?  153 VAL   F CA    1 
ATOM   5125 C C     . VAL   F 3 153 ? 13.427  -26.949 18.135  1.00 40.87  ?  153 VAL   F C     1 
ATOM   5126 O O     . VAL   F 3 153 ? 14.494  -27.078 18.738  1.00 41.61  ?  153 VAL   F O     1 
ATOM   5127 C CB    . VAL   F 3 153 ? 13.371  -24.435 17.563  1.00 47.42  ?  153 VAL   F CB    1 
ATOM   5128 C CG1   . VAL   F 3 153 ? 13.438  -24.564 16.040  1.00 47.84  ?  153 VAL   F CG1   1 
ATOM   5129 C CG2   . VAL   F 3 153 ? 12.735  -23.086 17.910  1.00 49.40  ?  153 VAL   F CG2   1 
ATOM   5130 N N     . GLU   F 3 154 ? 12.874  -27.924 17.391  1.00 38.33  ?  154 GLU   F N     1 
ATOM   5131 C CA    . GLU   F 3 154 ? 13.438  -29.252 17.282  1.00 36.83  ?  154 GLU   F CA    1 
ATOM   5132 C C     . GLU   F 3 154 ? 13.834  -29.474 15.835  1.00 36.42  ?  154 GLU   F C     1 
ATOM   5133 O O     . GLU   F 3 154 ? 12.975  -29.510 14.971  1.00 34.95  ?  154 GLU   F O     1 
ATOM   5134 C CB    . GLU   F 3 154 ? 12.479  -30.356 17.728  1.00 35.32  ?  154 GLU   F CB    1 
ATOM   5135 C CG    . GLU   F 3 154 ? 11.860  -30.137 19.099  1.00 34.83  ?  154 GLU   F CG    1 
ATOM   5136 C CD    . GLU   F 3 154 ? 11.256  -31.402 19.721  1.00 33.66  ?  154 GLU   F CD    1 
ATOM   5137 O OE1   . GLU   F 3 154 ? 11.195  -32.481 19.086  1.00 34.08  ?  154 GLU   F OE1   1 
ATOM   5138 O OE2   . GLU   F 3 154 ? 10.915  -31.357 20.906  1.00 31.95  -1 154 GLU   F OE2   1 
ATOM   5139 N N     . GLN   F 3 155 ? 15.132  -29.673 15.608  1.00 38.19  ?  155 GLN   F N     1 
ATOM   5140 C CA    . GLN   F 3 155 ? 15.691  -29.927 14.293  1.00 39.67  ?  155 GLN   F CA    1 
ATOM   5141 C C     . GLN   F 3 155 ? 15.952  -31.419 14.135  1.00 37.50  ?  155 GLN   F C     1 
ATOM   5142 O O     . GLN   F 3 155 ? 16.304  -32.082 15.114  1.00 36.75  ?  155 GLN   F O     1 
ATOM   5143 C CB    . GLN   F 3 155 ? 17.006  -29.174 14.102  1.00 41.95  ?  155 GLN   F CB    1 
ATOM   5144 C CG    . GLN   F 3 155 ? 16.865  -27.666 14.221  1.00 44.18  ?  155 GLN   F CG    1 
ATOM   5145 C CD    . GLN   F 3 155 ? 18.205  -26.980 14.177  1.00 46.71  ?  155 GLN   F CD    1 
ATOM   5146 O OE1   . GLN   F 3 155 ? 18.704  -26.555 15.216  1.00 46.98  ?  155 GLN   F OE1   1 
ATOM   5147 N NE2   . GLN   F 3 155 ? 18.822  -26.934 13.001  1.00 48.34  ?  155 GLN   F NE2   1 
ATOM   5148 N N     . PRO   F 3 156 ? 15.845  -31.978 12.900  1.00 37.64  ?  156 PRO   F N     1 
ATOM   5149 C CA    . PRO   F 3 156 ? 16.261  -33.348 12.648  1.00 36.36  ?  156 PRO   F CA    1 
ATOM   5150 C C     . PRO   F 3 156 ? 17.777  -33.466 12.633  1.00 38.39  ?  156 PRO   F C     1 
ATOM   5151 O O     . PRO   F 3 156 ? 18.446  -32.515 12.213  1.00 41.50  ?  156 PRO   F O     1 
ATOM   5152 C CB    . PRO   F 3 156 ? 15.642  -33.642 11.291  1.00 36.82  ?  156 PRO   F CB    1 
ATOM   5153 C CG    . PRO   F 3 156 ? 15.720  -32.308 10.603  1.00 38.79  ?  156 PRO   F CG    1 
ATOM   5154 C CD    . PRO   F 3 156 ? 15.364  -31.316 11.662  1.00 38.46  ?  156 PRO   F CD    1 
ATOM   5155 N N     . VAL   F 3 157 ? 18.300  -34.633 13.048  1.00 37.02  ?  157 VAL   F N     1 
ATOM   5156 C CA    . VAL   F 3 157 ? 19.736  -34.849 13.156  1.00 39.08  ?  157 VAL   F CA    1 
ATOM   5157 C C     . VAL   F 3 157 ? 20.441  -34.776 11.795  1.00 42.46  ?  157 VAL   F C     1 
ATOM   5158 O O     . VAL   F 3 157 ? 21.638  -34.537 11.771  1.00 44.25  ?  157 VAL   F O     1 
ATOM   5159 C CB    . VAL   F 3 157 ? 20.049  -36.175 13.870  1.00 38.06  ?  157 VAL   F CB    1 
ATOM   5160 C CG1   . VAL   F 3 157 ? 19.699  -37.409 13.027  1.00 37.01  ?  157 VAL   F CG1   1 
ATOM   5161 C CG2   . VAL   F 3 157 ? 21.506  -36.221 14.361  1.00 39.89  ?  157 VAL   F CG2   1 
ATOM   5162 N N     . THR   F 3 158 ? 19.705  -35.007 10.692  1.00 43.25  ?  158 THR   F N     1 
ATOM   5163 C CA    . THR   F 3 158 ? 20.114  -34.806 9.306   1.00 45.42  ?  158 THR   F CA    1 
ATOM   5164 C C     . THR   F 3 158 ? 20.660  -33.409 9.014   1.00 48.72  ?  158 THR   F C     1 
ATOM   5165 O O     . THR   F 3 158 ? 21.341  -33.306 8.009   1.00 51.22  ?  158 THR   F O     1 
ATOM   5166 C CB    . THR   F 3 158 ? 18.962  -35.138 8.334   1.00 43.90  ?  158 THR   F CB    1 
ATOM   5167 O OG1   . THR   F 3 158 ? 17.766  -34.522 8.781   1.00 42.09  ?  158 THR   F OG1   1 
ATOM   5168 C CG2   . THR   F 3 158 ? 18.672  -36.620 8.200   1.00 42.37  ?  158 THR   F CG2   1 
ATOM   5169 N N     . TYR   F 3 159 ? 20.365  -32.379 9.836   1.00 49.68  ?  159 TYR   F N     1 
ATOM   5170 C CA    . TYR   F 3 159 ? 21.017  -31.068 9.773   1.00 52.42  ?  159 TYR   F CA    1 
ATOM   5171 C C     . TYR   F 3 159 ? 22.428  -31.008 10.399  1.00 55.86  ?  159 TYR   F C     1 
ATOM   5172 O O     . TYR   F 3 159 ? 23.058  -29.957 10.254  1.00 59.16  ?  159 TYR   F O     1 
ATOM   5173 C CB    . TYR   F 3 159 ? 20.011  -30.047 10.333  1.00 50.55  ?  159 TYR   F CB    1 
ATOM   5174 C CG    . TYR   F 3 159 ? 18.756  -29.728 9.518   1.00 48.50  ?  159 TYR   F CG    1 
ATOM   5175 C CD1   . TYR   F 3 159 ? 18.420  -30.361 8.309   1.00 49.71  ?  159 TYR   F CD1   1 
ATOM   5176 C CD2   . TYR   F 3 159 ? 17.874  -28.747 9.971   1.00 47.68  ?  159 TYR   F CD2   1 
ATOM   5177 C CE1   . TYR   F 3 159 ? 17.280  -30.012 7.579   1.00 48.71  ?  159 TYR   F CE1   1 
ATOM   5178 C CE2   . TYR   F 3 159 ? 16.724  -28.399 9.261   1.00 47.72  ?  159 TYR   F CE2   1 
ATOM   5179 C CZ    . TYR   F 3 159 ? 16.424  -29.034 8.061   1.00 48.11  ?  159 TYR   F CZ    1 
ATOM   5180 O OH    . TYR   F 3 159 ? 15.321  -28.695 7.342   1.00 46.75  ?  159 TYR   F OH    1 
ATOM   5181 N N     . ARG   F 3 160 ? 22.973  -32.087 11.019  1.00 55.44  ?  160 ARG   F N     1 
ATOM   5182 C CA    . ARG   F 3 160 ? 24.335  -32.130 11.569  1.00 58.61  ?  160 ARG   F CA    1 
ATOM   5183 C C     . ARG   F 3 160 ? 25.372  -31.758 10.490  1.00 62.73  ?  160 ARG   F C     1 
ATOM   5184 O O     . ARG   F 3 160 ? 25.329  -32.313 9.389   1.00 63.23  ?  160 ARG   F O     1 
ATOM   5185 C CB    . ARG   F 3 160 ? 24.705  -33.514 12.132  1.00 57.76  ?  160 ARG   F CB    1 
ATOM   5186 C CG    . ARG   F 3 160 ? 26.035  -33.629 12.878  1.00 60.17  ?  160 ARG   F CG    1 
ATOM   5187 C CD    . ARG   F 3 160 ? 26.709  -34.998 13.079  1.00 61.32  ?  160 ARG   F CD    1 
ATOM   5188 N NE    . ARG   F 3 160 ? 26.084  -36.100 13.833  1.00 61.16  ?  160 ARG   F NE    1 
ATOM   5189 C CZ    . ARG   F 3 160 ? 25.320  -36.141 14.944  1.00 60.10  ?  160 ARG   F CZ    1 
ATOM   5190 N NH1   . ARG   F 3 160 ? 24.631  -35.106 15.405  1.00 61.48  1  160 ARG   F NH1   1 
ATOM   5191 N NH2   . ARG   F 3 160 ? 25.180  -37.289 15.590  1.00 59.41  ?  160 ARG   F NH2   1 
ATOM   5192 N N     . GLY   F 3 161 ? 26.257  -30.787 10.802  1.00 65.59  ?  161 GLY   F N     1 
ATOM   5193 C CA    . GLY   F 3 161 ? 27.234  -30.235 9.858   1.00 70.10  ?  161 GLY   F CA    1 
ATOM   5194 C C     . GLY   F 3 161 ? 26.738  -29.035 9.034   1.00 71.56  ?  161 GLY   F C     1 
ATOM   5195 O O     . GLY   F 3 161 ? 27.557  -28.433 8.335   1.00 73.02  ?  161 GLY   F O     1 
ATOM   5196 N N     . ARG   F 3 162 ? 25.425  -28.693 9.113   1.00 69.80  ?  162 ARG   F N     1 
ATOM   5197 C CA    . ARG   F 3 162 ? 24.784  -27.556 8.455   1.00 70.07  ?  162 ARG   F CA    1 
ATOM   5198 C C     . ARG   F 3 162 ? 24.049  -26.651 9.457   1.00 68.37  ?  162 ARG   F C     1 
ATOM   5199 O O     . ARG   F 3 162 ? 23.343  -25.750 9.019   1.00 69.19  ?  162 ARG   F O     1 
ATOM   5200 C CB    . ARG   F 3 162 ? 23.818  -28.133 7.405   1.00 69.00  ?  162 ARG   F CB    1 
ATOM   5201 C CG    . ARG   F 3 162 ? 24.499  -28.900 6.278   1.00 71.76  ?  162 ARG   F CG    1 
ATOM   5202 C CD    . ARG   F 3 162 ? 23.545  -29.455 5.243   1.00 71.72  ?  162 ARG   F CD    1 
ATOM   5203 N NE    . ARG   F 3 162 ? 22.537  -30.388 5.771   1.00 68.62  ?  162 ARG   F NE    1 
ATOM   5204 C CZ    . ARG   F 3 162 ? 21.255  -30.545 5.388   1.00 68.75  ?  162 ARG   F CZ    1 
ATOM   5205 N NH1   . ARG   F 3 162 ? 20.659  -31.698 5.641   1.00 68.83  1  162 ARG   F NH1   1 
ATOM   5206 N NH2   . ARG   F 3 162 ? 20.574  -29.662 4.661   1.00 70.10  ?  162 ARG   F NH2   1 
ATOM   5207 N N     . ALA   F 3 163 ? 24.255  -26.825 10.780  1.00 65.77  ?  163 ALA   F N     1 
ATOM   5208 C CA    . ALA   F 3 163 ? 23.471  -26.157 11.811  1.00 63.84  ?  163 ALA   F CA    1 
ATOM   5209 C C     . ALA   F 3 163 ? 24.055  -24.775 12.057  1.00 65.28  ?  163 ALA   F C     1 
ATOM   5210 O O     . ALA   F 3 163 ? 25.267  -24.691 12.156  1.00 69.56  ?  163 ALA   F O     1 
ATOM   5211 C CB    . ALA   F 3 163 ? 23.507  -26.972 13.092  1.00 62.35  ?  163 ALA   F CB    1 
ATOM   5212 N N     . THR   F 3 164 ? 23.210  -23.732 12.168  1.00 64.16  ?  164 THR   F N     1 
ATOM   5213 C CA    . THR   F 3 164 ? 23.614  -22.355 12.458  1.00 66.58  ?  164 THR   F CA    1 
ATOM   5214 C C     . THR   F 3 164 ? 22.776  -21.844 13.637  1.00 64.33  ?  164 THR   F C     1 
ATOM   5215 O O     . THR   F 3 164 ? 21.901  -22.564 14.098  1.00 60.17  ?  164 THR   F O     1 
ATOM   5216 C CB    . THR   F 3 164 ? 23.512  -21.492 11.186  1.00 68.59  ?  164 THR   F CB    1 
ATOM   5217 N N     . GLY   F 3 165 ? 23.100  -20.655 14.171  1.00 65.63  ?  165 GLY   F N     1 
ATOM   5218 C CA    . GLY   F 3 165 ? 22.309  -19.997 15.203  1.00 65.78  ?  165 GLY   F CA    1 
ATOM   5219 C C     . GLY   F 3 165 ? 22.767  -20.377 16.612  1.00 66.00  ?  165 GLY   F C     1 
ATOM   5220 O O     . GLY   F 3 165 ? 23.650  -21.225 16.773  1.00 66.14  ?  165 GLY   F O     1 
ATOM   5221 N N     . LEU   F 3 166 ? 22.147  -19.730 17.615  1.00 66.45  ?  166 LEU   F N     1 
ATOM   5222 C CA    . LEU   F 3 166 ? 22.476  -19.910 19.030  1.00 66.93  ?  166 LEU   F CA    1 
ATOM   5223 C C     . LEU   F 3 166 ? 22.279  -21.341 19.550  1.00 63.45  ?  166 LEU   F C     1 
ATOM   5224 O O     . LEU   F 3 166 ? 22.997  -21.718 20.463  1.00 65.31  ?  166 LEU   F O     1 
ATOM   5225 C CB    . LEU   F 3 166 ? 21.717  -18.903 19.902  1.00 67.92  ?  166 LEU   F CB    1 
ATOM   5226 C CG    . LEU   F 3 166 ? 22.082  -17.427 19.703  1.00 70.97  ?  166 LEU   F CG    1 
ATOM   5227 C CD1   . LEU   F 3 166 ? 21.196  -16.575 20.590  1.00 71.02  ?  166 LEU   F CD1   1 
ATOM   5228 C CD2   . LEU   F 3 166 ? 23.557  -17.100 19.949  1.00 74.03  ?  166 LEU   F CD2   1 
ATOM   5229 N N     . CYS   F 3 167 ? 21.373  -22.144 18.971  1.00 59.77  ?  167 CYS   F N     1 
ATOM   5230 C CA    . CYS   F 3 167 ? 21.194  -23.549 19.355  1.00 56.15  ?  167 CYS   F CA    1 
ATOM   5231 C C     . CYS   F 3 167 ? 22.423  -24.416 19.017  1.00 58.03  ?  167 CYS   F C     1 
ATOM   5232 O O     . CYS   F 3 167 ? 22.643  -25.440 19.671  1.00 54.46  ?  167 CYS   F O     1 
ATOM   5233 C CB    . CYS   F 3 167 ? 19.910  -24.118 18.774  1.00 51.93  ?  167 CYS   F CB    1 
ATOM   5234 S SG    . CYS   F 3 167 ? 18.425  -23.226 19.306  1.00 50.00  ?  167 CYS   F SG    1 
ATOM   5235 N N     . GLY   F 3 168 ? 23.238  -24.009 18.024  1.00 61.89  ?  168 GLY   F N     1 
ATOM   5236 C CA    . GLY   F 3 168 ? 24.628  -24.438 17.928  1.00 64.44  ?  168 GLY   F CA    1 
ATOM   5237 C C     . GLY   F 3 168 ? 24.754  -25.849 17.357  1.00 63.87  ?  168 GLY   F C     1 
ATOM   5238 O O     . GLY   F 3 168 ? 23.937  -26.233 16.524  1.00 60.75  ?  168 GLY   F O     1 
ATOM   5239 N N     . ASN   F 3 169 ? 25.771  -26.594 17.835  1.00 67.19  ?  169 ASN   F N     1 
ATOM   5240 C CA    . ASN   F 3 169 ? 26.121  -27.925 17.352  1.00 68.87  ?  169 ASN   F CA    1 
ATOM   5241 C C     . ASN   F 3 169 ? 24.966  -28.922 17.546  1.00 67.68  ?  169 ASN   F C     1 
ATOM   5242 O O     . ASN   F 3 169 ? 24.199  -28.814 18.507  1.00 62.93  ?  169 ASN   F O     1 
ATOM   5243 C CB    . ASN   F 3 169 ? 27.379  -28.467 18.031  1.00 71.87  ?  169 ASN   F CB    1 
ATOM   5244 N N     . LEU   F 3 170 ? 24.864  -29.871 16.603  1.00 68.93  ?  170 LEU   F N     1 
ATOM   5245 C CA    . LEU   F 3 170 ? 24.073  -31.082 16.739  1.00 69.79  ?  170 LEU   F CA    1 
ATOM   5246 C C     . LEU   F 3 170 ? 25.072  -32.225 16.977  1.00 77.32  ?  170 LEU   F C     1 
ATOM   5247 O O     . LEU   F 3 170 ? 25.848  -32.528 16.082  1.00 85.34  ?  170 LEU   F O     1 
ATOM   5248 C CB    . LEU   F 3 170 ? 23.214  -31.228 15.477  1.00 66.31  ?  170 LEU   F CB    1 
ATOM   5249 C CG    . LEU   F 3 170 ? 22.376  -30.001 15.062  1.00 65.19  ?  170 LEU   F CG    1 
ATOM   5250 C CD1   . LEU   F 3 170 ? 21.505  -30.284 13.855  1.00 63.67  ?  170 LEU   F CD1   1 
ATOM   5251 C CD2   . LEU   F 3 170 ? 21.503  -29.458 16.174  1.00 62.42  ?  170 LEU   F CD2   1 
ATOM   5252 N N     . ASN   F 3 171 ? 25.161  -32.751 18.216  1.00 83.35  ?  171 ASN   F N     1 
ATOM   5253 C CA    . ASN   F 3 171 ? 26.004  -33.889 18.589  1.00 84.79  ?  171 ASN   F CA    1 
ATOM   5254 C C     . ASN   F 3 171 ? 25.290  -34.746 19.642  1.00 79.82  ?  171 ASN   F C     1 
ATOM   5255 O O     . ASN   F 3 171 ? 25.302  -34.337 20.826  1.00 82.22  ?  171 ASN   F O     1 
ATOM   5256 C CB    . ASN   F 3 171 ? 27.374  -33.446 19.099  1.00 88.11  ?  171 ASN   F CB    1 
ATOM   5257 C CG    . ASN   F 3 171 ? 28.259  -32.942 17.988  1.00 90.06  ?  171 ASN   F CG    1 
ATOM   5258 O OD1   . ASN   F 3 171 ? 28.614  -33.714 17.089  1.00 89.15  ?  171 ASN   F OD1   1 
ATOM   5259 N ND2   . ASN   F 3 171 ? 28.576  -31.655 18.001  1.00 90.86  ?  171 ASN   F ND2   1 
HETATM 5260 C C1    . LUT   G 4 .   ? 19.273  -44.435 15.198  1.00 32.52  ?  201 LUT   A C1    1 
HETATM 5261 C C2    . LUT   G 4 .   ? 19.702  -42.993 15.512  1.00 33.71  ?  201 LUT   A C2    1 
HETATM 5262 C C3    . LUT   G 4 .   ? 21.139  -42.746 15.924  1.00 35.29  ?  201 LUT   A C3    1 
HETATM 5263 C C4    . LUT   G 4 .   ? 21.809  -43.972 16.479  1.00 34.42  ?  201 LUT   A C4    1 
HETATM 5264 C C5    . LUT   G 4 .   ? 21.666  -45.132 15.538  1.00 33.47  ?  201 LUT   A C5    1 
HETATM 5265 C C6    . LUT   G 4 .   ? 20.420  -45.457 15.072  1.00 32.73  ?  201 LUT   A C6    1 
HETATM 5266 C C7    . LUT   G 4 .   ? 20.210  -46.803 14.467  1.00 32.64  ?  201 LUT   A C7    1 
HETATM 5267 C C8    . LUT   G 4 .   ? 19.099  -47.625 14.389  1.00 31.45  ?  201 LUT   A C8    1 
HETATM 5268 C C9    . LUT   G 4 .   ? 19.097  -48.963 13.954  1.00 33.33  ?  201 LUT   A C9    1 
HETATM 5269 C C10   . LUT   G 4 .   ? 17.863  -49.585 13.604  1.00 31.98  ?  201 LUT   A C10   1 
HETATM 5270 C C11   . LUT   G 4 .   ? 17.597  -50.909 13.297  1.00 31.69  ?  201 LUT   A C11   1 
HETATM 5271 C C12   . LUT   G 4 .   ? 16.510  -51.499 12.642  1.00 31.31  ?  201 LUT   A C12   1 
HETATM 5272 C C13   . LUT   G 4 .   ? 16.359  -52.815 12.105  1.00 29.83  ?  201 LUT   A C13   1 
HETATM 5273 C C14   . LUT   G 4 .   ? 15.072  -53.313 11.846  1.00 29.40  ?  201 LUT   A C14   1 
HETATM 5274 C C15   . LUT   G 4 .   ? 14.633  -54.562 11.443  1.00 30.55  ?  201 LUT   A C15   1 
HETATM 5275 C C16   . LUT   G 4 .   ? 18.455  -44.366 13.884  1.00 31.92  ?  201 LUT   A C16   1 
HETATM 5276 C C17   . LUT   G 4 .   ? 18.328  -44.877 16.351  1.00 32.75  ?  201 LUT   A C17   1 
HETATM 5277 C C18   . LUT   G 4 .   ? 22.955  -45.901 15.308  1.00 32.92  ?  201 LUT   A C18   1 
HETATM 5278 C C19   . LUT   G 4 .   ? 20.362  -49.826 13.816  1.00 32.39  ?  201 LUT   A C19   1 
HETATM 5279 C C20   . LUT   G 4 .   ? 17.572  -53.607 11.689  1.00 28.60  ?  201 LUT   A C20   1 
HETATM 5280 O O3    . LUT   G 4 .   ? 21.144  -41.688 16.873  1.00 35.69  ?  201 LUT   A O3    1 
HETATM 5281 C C21   . LUT   G 4 .   ? 8.778   -65.244 7.561   1.00 44.24  ?  201 LUT   A C21   1 
HETATM 5282 C C22   . LUT   G 4 .   ? 8.950   -66.774 7.576   1.00 48.14  ?  201 LUT   A C22   1 
HETATM 5283 C C23   . LUT   G 4 .   ? 7.942   -67.502 8.478   1.00 50.77  ?  201 LUT   A C23   1 
HETATM 5284 C C24   . LUT   G 4 .   ? 7.613   -66.757 9.752   1.00 48.39  ?  201 LUT   A C24   1 
HETATM 5285 C C25   . LUT   G 4 .   ? 8.077   -65.541 10.061  1.00 45.48  ?  201 LUT   A C25   1 
HETATM 5286 C C26   . LUT   G 4 .   ? 8.852   -64.709 9.038   1.00 42.68  ?  201 LUT   A C26   1 
HETATM 5287 C C27   . LUT   G 4 .   ? 8.485   -63.251 9.141   1.00 38.47  ?  201 LUT   A C27   1 
HETATM 5288 C C28   . LUT   G 4 .   ? 9.277   -62.250 9.519   1.00 34.18  ?  201 LUT   A C28   1 
HETATM 5289 C C29   . LUT   G 4 .   ? 9.058   -60.870 9.563   1.00 32.51  ?  201 LUT   A C29   1 
HETATM 5290 C C30   . LUT   G 4 .   ? 10.161  -60.040 9.894   1.00 31.95  ?  201 LUT   A C30   1 
HETATM 5291 C C31   . LUT   G 4 .   ? 10.216  -58.700 10.190  1.00 32.64  ?  201 LUT   A C31   1 
HETATM 5292 C C32   . LUT   G 4 .   ? 11.365  -57.942 10.338  1.00 34.23  ?  201 LUT   A C32   1 
HETATM 5293 C C33   . LUT   G 4 .   ? 11.545  -56.539 10.565  1.00 35.61  ?  201 LUT   A C33   1 
HETATM 5294 C C34   . LUT   G 4 .   ? 12.862  -56.081 10.844  1.00 33.37  ?  201 LUT   A C34   1 
HETATM 5295 C C35   . LUT   G 4 .   ? 13.323  -54.897 11.248  1.00 31.05  ?  201 LUT   A C35   1 
HETATM 5296 C C36   . LUT   G 4 .   ? 7.454   -64.908 6.853   1.00 46.17  ?  201 LUT   A C36   1 
HETATM 5297 C C37   . LUT   G 4 .   ? 9.890   -64.587 6.725   1.00 44.90  ?  201 LUT   A C37   1 
HETATM 5298 C C38   . LUT   G 4 .   ? 7.943   -64.942 11.440  1.00 44.91  ?  201 LUT   A C38   1 
HETATM 5299 C C39   . LUT   G 4 .   ? 7.725   -60.228 9.191   1.00 31.96  ?  201 LUT   A C39   1 
HETATM 5300 C C40   . LUT   G 4 .   ? 10.394  -55.564 10.413  1.00 34.59  ?  201 LUT   A C40   1 
HETATM 5301 O O23   . LUT   G 4 .   ? 8.432   -68.828 8.816   1.00 49.98  ?  201 LUT   A O23   1 
HETATM 5302 N N1    . AZI   H 5 .   ? 34.739  -52.753 21.764  1.00 37.27  ?  202 AZI   A N1    1 
HETATM 5303 N N2    . AZI   H 5 .   ? 34.700  -52.150 22.744  1.00 46.26  ?  202 AZI   A N2    1 
HETATM 5304 N N3    . AZI   H 5 .   ? 34.636  -51.575 23.739  1.00 37.96  ?  202 AZI   A N3    1 
HETATM 5305 N N1    . AZI   I 5 .   ? 12.023  -71.134 42.230  1.00 40.81  ?  101 AZI   B N1    1 
HETATM 5306 N N2    . AZI   I 5 .   ? 12.782  -70.407 42.719  1.00 54.75  ?  101 AZI   B N2    1 
HETATM 5307 N N3    . AZI   I 5 .   ? 13.507  -69.649 43.224  1.00 36.88  ?  101 AZI   B N3    1 
HETATM 5308 C C1    . PLC   J 6 .   ? 15.758  -57.461 16.552  1.00 22.30  ?  201 PLC   C C1    1 
HETATM 5309 C C2    . PLC   J 6 .   ? 15.553  -56.473 15.412  1.00 24.80  ?  201 PLC   C C2    1 
HETATM 5310 C C3    . PLC   J 6 .   ? 16.690  -55.565 14.995  1.00 27.57  ?  201 PLC   C C3    1 
HETATM 5311 C C4    . PLC   J 6 .   ? 17.796  -59.153 19.422  1.00 19.08  ?  201 PLC   C C4    1 
HETATM 5312 C C5    . PLC   J 6 .   ? 17.841  -60.522 20.050  1.00 19.21  ?  201 PLC   C C5    1 
HETATM 5313 C C6    . PLC   J 6 .   ? 18.991  -62.461 21.030  1.00 19.40  ?  201 PLC   C C6    1 
HETATM 5314 C C7    . PLC   J 6 .   ? 19.822  -60.240 21.497  1.00 19.77  ?  201 PLC   C C7    1 
HETATM 5315 C C8    . PLC   J 6 .   ? 20.089  -61.167 19.292  1.00 19.56  ?  201 PLC   C C8    1 
HETATM 5316 C "C'"  . PLC   J 6 .   ? 13.950  -57.793 14.055  1.00 28.00  ?  201 PLC   C "C'"  1 
HETATM 5317 C "C1'" . PLC   J 6 .   ? 13.431  -58.935 13.232  1.00 28.54  ?  201 PLC   C "C1'" 1 
HETATM 5318 C "C2'" . PLC   J 6 .   ? 12.024  -59.524 13.562  0.50 28.87  ?  201 PLC   C "C2'" 1 
HETATM 5319 C "C3'" . PLC   J 6 .   ? 11.257  -59.071 14.800  0.50 29.27  ?  201 PLC   C "C3'" 1 
HETATM 5320 C "C4'" . PLC   J 6 .   ? 10.333  -57.907 14.600  0.50 29.68  ?  201 PLC   C "C4'" 1 
HETATM 5321 C "C5'" . PLC   J 6 .   ? 10.404  -56.876 15.696  0.50 28.54  ?  201 PLC   C "C5'" 1 
HETATM 5322 C "C6'" . PLC   J 6 .   ? 9.175   -56.825 16.591  0.50 27.27  ?  201 PLC   C "C6'" 1 
HETATM 5323 C "C7'" . PLC   J 6 .   ? 9.450   -56.359 17.995  0.50 25.38  ?  201 PLC   C "C7'" 1 
HETATM 5324 C "C8'" . PLC   J 6 .   ? 8.240   -56.209 18.880  0.50 24.80  ?  201 PLC   C "C8'" 1 
HETATM 5325 C "C9'" . PLC   J 6 .   ? 6.943   -56.697 18.289  0.50 24.80  ?  201 PLC   C "C9'" 1 
HETATM 5326 C "CA'" . PLC   J 6 .   ? 5.785   -56.487 19.234  0.50 24.96  ?  201 PLC   C "CA'" 1 
HETATM 5327 C "CB'" . PLC   J 6 .   ? 5.317   -57.711 19.987  0.50 24.14  ?  201 PLC   C "CB'" 1 
HETATM 5328 C CB    . PLC   J 6 .   ? 15.763  -53.458 15.816  0.50 30.83  ?  201 PLC   C CB    1 
HETATM 5329 C C1B   . PLC   J 6 .   ? 15.953  -52.719 17.078  0.50 29.68  ?  201 PLC   C C1B   1 
HETATM 5330 C C2B   . PLC   J 6 .   ? 14.889  -51.744 17.413  0.50 29.98  ?  201 PLC   C C2B   1 
HETATM 5331 C C3B   . PLC   J 6 .   ? 15.416  -50.587 18.244  0.50 29.62  ?  201 PLC   C C3B   1 
HETATM 5332 C C4B   . PLC   J 6 .   ? 16.318  -49.660 17.485  0.50 30.88  ?  201 PLC   C C4B   1 
HETATM 5333 C C5B   . PLC   J 6 .   ? 15.933  -48.205 17.546  0.50 31.66  ?  201 PLC   C C5B   1 
HETATM 5334 C C6B   . PLC   J 6 .   ? 14.562  -47.910 16.999  0.50 31.64  ?  201 PLC   C C6B   1 
HETATM 5335 C C7B   . PLC   J 6 .   ? 13.789  -46.899 17.796  0.50 31.74  ?  201 PLC   C C7B   1 
HETATM 5336 C C8B   . PLC   J 6 .   ? 13.802  -45.502 17.207  0.50 33.20  ?  201 PLC   C C8B   1 
HETATM 5337 C C9B   . PLC   J 6 .   ? 13.743  -45.484 15.702  0.50 33.94  ?  201 PLC   C C9B   1 
HETATM 5338 C CAA   . PLC   J 6 .   ? 13.771  -46.870 15.076  0.50 33.15  ?  201 PLC   C CAA   1 
HETATM 5339 C CBA   . PLC   J 6 .   ? 14.525  -46.901 13.774  0.50 33.22  ?  201 PLC   C CBA   1 
HETATM 5340 O "O'"  . PLC   J 6 .   ? 13.133  -56.993 14.269  1.00 35.95  ?  201 PLC   C "O'"  1 
HETATM 5341 O OB    . PLC   J 6 .   ? 14.909  -53.281 15.012  0.50 34.46  ?  201 PLC   C OB    1 
HETATM 5342 O O2    . PLC   J 6 .   ? 15.249  -57.472 14.343  1.00 27.35  ?  201 PLC   C O2    1 
HETATM 5343 O O3    . PLC   J 6 .   ? 16.785  -54.284 15.646  1.00 32.12  ?  201 PLC   C O3    1 
HETATM 5344 O O1P   . PLC   J 6 .   ? 14.414  -57.329 19.357  1.00 19.03  ?  201 PLC   C O1P   1 
HETATM 5345 O O2P   . PLC   J 6 .   ? 16.772  -56.385 19.984  1.00 17.45  ?  201 PLC   C O2P   1 
HETATM 5346 O O3P   . PLC   J 6 .   ? 16.484  -57.003 17.709  1.00 20.01  ?  201 PLC   C O3P   1 
HETATM 5347 O O4P   . PLC   J 6 .   ? 16.380  -58.831 19.371  1.00 18.82  ?  201 PLC   C O4P   1 
HETATM 5348 N N     . PLC   J 6 .   ? 19.197  -61.086 20.454  1.00 19.46  ?  201 PLC   C N     1 
HETATM 5349 P P     . PLC   J 6 .   ? 15.926  -57.327 19.177  1.00 18.69  ?  201 PLC   C P     1 
HETATM 5350 C C1    . A1L6M K 7 .   ? 8.897   -68.383 33.183  1.00 22.07  ?  202 A1L6M C C1    1 
HETATM 5351 C C2    . A1L6M K 7 .   ? 9.960   -67.675 32.373  1.00 21.92  ?  202 A1L6M C C2    1 
HETATM 5352 C C3    . A1L6M K 7 .   ? 11.246  -68.433 32.163  1.00 20.38  ?  202 A1L6M C C3    1 
HETATM 5353 C C4    . A1L6M K 7 .   ? 12.054  -69.008 33.105  1.00 22.68  ?  202 A1L6M C C4    1 
HETATM 5354 C C5    . A1L6M K 7 .   ? 11.920  -69.065 34.603  1.00 23.81  ?  202 A1L6M C C5    1 
HETATM 5355 C C6    . A1L6M K 7 .   ? 13.181  -69.544 32.417  1.00 24.38  ?  202 A1L6M C C6    1 
HETATM 5356 O O1    . A1L6M K 7 .   ? 14.186  -70.211 32.860  1.00 24.99  ?  202 A1L6M C O1    1 
HETATM 5357 N N1    . A1L6M K 7 .   ? 13.062  -69.300 31.088  1.00 23.15  ?  202 A1L6M C N1    1 
HETATM 5358 C C7    . A1L6M K 7 .   ? 11.890  -68.603 30.873  1.00 21.41  ?  202 A1L6M C C7    1 
HETATM 5359 C C8    . A1L6M K 7 .   ? 11.528  -68.235 29.569  1.00 18.82  ?  202 A1L6M C C8    1 
HETATM 5360 C C9    . A1L6M K 7 .   ? 12.200  -68.068 28.346  1.00 16.60  ?  202 A1L6M C C9    1 
HETATM 5361 C C10   . A1L6M K 7 .   ? 13.614  -67.845 28.052  1.00 15.97  ?  202 A1L6M C C10   1 
HETATM 5362 C C11   . A1L6M K 7 .   ? 14.749  -67.651 29.004  1.00 16.16  ?  202 A1L6M C C11   1 
HETATM 5363 C C12   . A1L6M K 7 .   ? 13.780  -67.762 26.692  1.00 16.06  ?  202 A1L6M C C12   1 
HETATM 5364 C C13   . A1L6M K 7 .   ? 15.084  -67.548 25.942  1.00 17.41  ?  202 A1L6M C C13   1 
HETATM 5365 C C14   . A1L6M K 7 .   ? 15.744  -68.893 25.680  1.00 17.86  ?  202 A1L6M C C14   1 
HETATM 5366 C C15   . A1L6M K 7 .   ? 17.099  -68.908 24.986  1.00 18.70  ?  202 A1L6M C C15   1 
HETATM 5367 O O2    . A1L6M K 7 .   ? 17.829  -69.832 25.248  1.00 18.72  ?  202 A1L6M C O2    1 
HETATM 5368 O O3    . A1L6M K 7 .   ? 17.414  -68.042 24.176  1.00 19.69  ?  202 A1L6M C O3    1 
HETATM 5369 C C16   . A1L6M K 7 .   ? 12.472  -67.983 26.101  1.00 15.39  ?  202 A1L6M C C16   1 
HETATM 5370 N N2    . A1L6M K 7 .   ? 11.556  -68.111 27.138  1.00 15.49  ?  202 A1L6M C N2    1 
HETATM 5371 C C17   . A1L6M K 7 .   ? 12.286  -67.947 24.726  1.00 14.52  ?  202 A1L6M C C17   1 
HETATM 5372 C C18   . A1L6M K 7 .   ? 11.253  -67.995 23.786  1.00 14.95  ?  202 A1L6M C C18   1 
HETATM 5373 N N3    . A1L6M K 7 .   ? 9.887   -68.073 24.072  1.00 14.39  ?  202 A1L6M C N3    1 
HETATM 5374 C C19   . A1L6M K 7 .   ? 9.236   -68.125 22.878  1.00 14.92  ?  202 A1L6M C C19   1 
HETATM 5375 C C20   . A1L6M K 7 .   ? 7.840   -68.254 22.854  1.00 15.22  ?  202 A1L6M C C20   1 
HETATM 5376 C C21   . A1L6M K 7 .   ? 6.846   -67.998 21.912  1.00 16.23  ?  202 A1L6M C C21   1 
HETATM 5377 N N4    . A1L6M K 7 .   ? 7.031   -67.300 20.748  1.00 17.00  ?  202 A1L6M C N4    1 
HETATM 5378 C C22   . A1L6M K 7 .   ? 5.831   -67.168 20.116  1.00 17.65  ?  202 A1L6M C C22   1 
HETATM 5379 O O4    . A1L6M K 7 .   ? 5.767   -66.548 19.001  1.00 17.78  ?  202 A1L6M C O4    1 
HETATM 5380 C C23   . A1L6M K 7 .   ? 4.834   -67.815 20.847  1.00 17.87  ?  202 A1L6M C C23   1 
HETATM 5381 C C24   . A1L6M K 7 .   ? 3.405   -67.809 20.358  1.00 20.12  ?  202 A1L6M C C24   1 
HETATM 5382 O O5    . A1L6M K 7 .   ? 2.544   -68.711 21.077  1.00 19.05  ?  202 A1L6M C O5    1 
HETATM 5383 C C25   . A1L6M K 7 .   ? 2.818   -66.410 20.476  1.00 21.38  ?  202 A1L6M C C25   1 
HETATM 5384 C C26   . A1L6M K 7 .   ? 1.334   -66.282 20.089  1.00 26.14  ?  202 A1L6M C C26   1 
HETATM 5385 C C27   . A1L6M K 7 .   ? 1.000   -66.714 18.683  1.00 30.43  ?  202 A1L6M C C27   1 
HETATM 5386 C C28   . A1L6M K 7 .   ? -0.125  -67.245 18.161  1.00 40.17  ?  202 A1L6M C C28   1 
HETATM 5387 C C29   . A1L6M K 7 .   ? -1.368  -67.595 18.958  1.00 39.57  ?  202 A1L6M C C29   1 
HETATM 5388 C C30   . A1L6M K 7 .   ? -0.264  -67.562 16.678  1.00 44.99  ?  202 A1L6M C C30   1 
HETATM 5389 C C31   . A1L6M K 7 .   ? 0.715   -67.080 15.597  1.00 51.01  ?  202 A1L6M C C31   1 
HETATM 5390 C C32   . A1L6M K 7 .   ? 0.219   -67.463 14.212  1.00 55.19  ?  202 A1L6M C C32   1 
HETATM 5391 C C33   . A1L6M K 7 .   ? -0.731  -66.890 13.452  1.00 61.27  ?  202 A1L6M C C33   1 
HETATM 5392 C C34   . A1L6M K 7 .   ? -1.293  -67.493 12.183  1.00 63.51  ?  202 A1L6M C C34   1 
HETATM 5393 C C35   . A1L6M K 7 .   ? -1.322  -65.548 13.829  1.00 65.39  ?  202 A1L6M C C35   1 
HETATM 5394 C C36   . A1L6M K 7 .   ? -0.329  -64.435 13.478  1.00 67.71  ?  202 A1L6M C C36   1 
HETATM 5395 C C37   . A1L6M K 7 .   ? -0.813  -63.040 13.805  1.00 70.76  ?  202 A1L6M C C37   1 
HETATM 5396 C C38   . A1L6M K 7 .   ? -0.147  -61.877 13.856  1.00 69.25  ?  202 A1L6M C C38   1 
HETATM 5397 C C39   . A1L6M K 7 .   ? 1.352   -61.730 13.679  1.00 64.66  ?  202 A1L6M C C39   1 
HETATM 5398 C C40   . A1L6M K 7 .   ? -0.840  -60.540 14.069  1.00 73.81  ?  202 A1L6M C C40   1 
HETATM 5399 C C41   . A1L6M K 7 .   ? 5.429   -68.337 21.984  1.00 16.70  ?  202 A1L6M C C41   1 
HETATM 5400 C C42   . A1L6M K 7 .   ? 4.769   -69.181 23.048  1.00 15.71  ?  202 A1L6M C C42   1 
HETATM 5401 C C43   . A1L6M K 7 .   ? 10.186  -68.023 21.864  1.00 16.70  ?  202 A1L6M C C43   1 
HETATM 5402 C C44   . A1L6M K 7 .   ? 9.945   -68.118 20.383  1.00 18.10  ?  202 A1L6M C C44   1 
HETATM 5403 O O6    . A1L6M K 7 .   ? 9.780   -66.874 19.735  1.00 17.08  ?  202 A1L6M C O6    1 
HETATM 5404 C C45   . A1L6M K 7 .   ? 11.462  -67.951 22.421  1.00 15.11  ?  202 A1L6M C C45   1 
HETATM 5405 C C46   . A1L6M K 7 .   ? 12.813  -67.865 21.762  1.00 17.18  ?  202 A1L6M C C46   1 
HETATM 5406 C C47   . A1L6M K 7 .   ? 13.651  -66.571 21.849  1.00 17.69  ?  202 A1L6M C C47   1 
HETATM 5407 C C48   . A1L6M K 7 .   ? 13.116  -65.372 21.057  1.00 18.93  ?  202 A1L6M C C48   1 
HETATM 5408 O O7    . A1L6M K 7 .   ? 12.142  -65.515 20.267  1.00 18.92  ?  202 A1L6M C O7    1 
HETATM 5409 O O8    . A1L6M K 7 .   ? 13.699  -64.290 21.161  1.00 20.11  ?  202 A1L6M C O8    1 
HETATM 5410 C C1    . PLC   L 6 .   ? 3.185   -65.907 12.697  0.50 49.26  ?  203 PLC   C C1    1 
HETATM 5411 C C2    . PLC   L 6 .   ? 3.438   -64.625 11.915  0.50 45.88  ?  203 PLC   C C2    1 
HETATM 5412 C C3    . PLC   L 6 .   ? 4.366   -63.606 12.547  0.50 43.94  ?  203 PLC   C C3    1 
HETATM 5413 C C4    . PLC   L 6 .   ? 7.452   -68.181 13.999  1.00 42.03  ?  203 PLC   C C4    1 
HETATM 5414 C C5    . PLC   L 6 .   ? 8.666   -67.472 14.548  1.00 41.89  ?  203 PLC   C C5    1 
HETATM 5415 C C6    . PLC   L 6 .   ? 7.757   -67.140 16.862  1.00 39.60  ?  203 PLC   C C6    1 
HETATM 5416 C C7    . PLC   L 6 .   ? 10.044  -66.500 16.300  1.00 42.08  ?  203 PLC   C C7    1 
HETATM 5417 C C8    . PLC   L 6 .   ? 9.418   -68.805 16.485  1.00 44.40  ?  203 PLC   C C8    1 
HETATM 5418 C "C'"  . PLC   L 6 .   ? 3.211   -65.578 9.720   0.50 47.10  ?  203 PLC   C "C'"  1 
HETATM 5419 C "C1'" . PLC   L 6 .   ? 1.825   -65.878 10.199  0.50 46.32  ?  203 PLC   C "C1'" 1 
HETATM 5420 C "C2'" . PLC   L 6 .   ? 0.765   -65.761 9.121   0.50 46.29  ?  203 PLC   C "C2'" 1 
HETATM 5421 C "C3'" . PLC   L 6 .   ? -0.047  -64.475 9.239   0.50 43.11  ?  203 PLC   C "C3'" 1 
HETATM 5422 C "C4'" . PLC   L 6 .   ? 0.317   -63.378 8.272   1.00 42.00  ?  203 PLC   C "C4'" 1 
HETATM 5423 C "C5'" . PLC   L 6 .   ? 0.565   -61.968 8.846   1.00 40.92  ?  203 PLC   C "C5'" 1 
HETATM 5424 C "C6'" . PLC   L 6 .   ? -0.114  -60.834 8.069   1.00 39.96  ?  203 PLC   C "C6'" 1 
HETATM 5425 C "C7'" . PLC   L 6 .   ? -0.227  -59.494 8.793   1.00 40.43  ?  203 PLC   C "C7'" 1 
HETATM 5426 C "C8'" . PLC   L 6 .   ? 0.546   -58.321 8.217   1.00 40.31  ?  203 PLC   C "C8'" 1 
HETATM 5427 C "C9'" . PLC   L 6 .   ? 0.324   -56.990 8.970   1.00 41.24  ?  203 PLC   C "C9'" 1 
HETATM 5428 C "CA'" . PLC   L 6 .   ? 0.709   -55.716 8.230   1.00 41.88  ?  203 PLC   C "CA'" 1 
HETATM 5429 C "CB'" . PLC   L 6 .   ? 0.357   -54.432 8.965   1.00 41.66  ?  203 PLC   C "CB'" 1 
HETATM 5430 C CB    . PLC   L 6 .   ? 5.304   -63.475 14.723  0.50 40.37  ?  203 PLC   C CB    1 
HETATM 5431 C C1B   . PLC   L 6 .   ? 6.418   -62.678 14.103  0.50 39.96  ?  203 PLC   C C1B   1 
HETATM 5432 C C2B   . PLC   L 6 .   ? 7.687   -62.776 14.916  0.50 39.28  ?  203 PLC   C C2B   1 
HETATM 5433 C C3B   . PLC   L 6 .   ? 8.948   -62.392 14.173  0.50 38.87  ?  203 PLC   C C3B   1 
HETATM 5434 C C4B   . PLC   L 6 .   ? 8.892   -61.052 13.497  0.50 37.76  ?  203 PLC   C C4B   1 
HETATM 5435 C C5B   . PLC   L 6 .   ? 8.331   -59.938 14.341  0.50 35.19  ?  203 PLC   C C5B   1 
HETATM 5436 C C6B   . PLC   L 6 .   ? 7.105   -59.305 13.743  0.50 33.52  ?  203 PLC   C C6B   1 
HETATM 5437 C C7B   . PLC   L 6 .   ? 7.219   -57.824 13.496  0.50 32.03  ?  203 PLC   C C7B   1 
HETATM 5438 C C8B   . PLC   L 6 .   ? 5.984   -57.179 12.923  0.50 30.42  ?  203 PLC   C C8B   1 
HETATM 5439 C C9B   . PLC   L 6 .   ? 6.259   -56.071 11.930  0.50 29.21  ?  203 PLC   C C9B   1 
HETATM 5440 C CAA   . PLC   L 6 .   ? 6.767   -54.795 12.526  0.50 28.21  ?  203 PLC   C CAA   1 
HETATM 5441 C CBA   . PLC   L 6 .   ? 7.518   -55.019 13.812  0.50 27.46  ?  203 PLC   C CBA   1 
HETATM 5442 O "O'"  . PLC   L 6 .   ? 3.580   -65.866 8.612   0.50 48.01  ?  203 PLC   C "O'"  1 
HETATM 5443 O OB    . PLC   L 6 .   ? 5.449   -64.013 15.760  0.50 39.96  ?  203 PLC   C OB    1 
HETATM 5444 O O2    . PLC   L 6 .   ? 4.006   -64.970 10.623  0.50 46.14  ?  203 PLC   C O2    1 
HETATM 5445 O O3    . PLC   L 6 .   ? 4.212   -63.644 13.981  0.50 42.79  ?  203 PLC   C O3    1 
HETATM 5446 O O1P   . PLC   L 6 .   ? 5.165   -68.173 12.211  1.00 43.68  ?  203 PLC   C O1P   1 
HETATM 5447 O O2P   . PLC   L 6 .   ? 4.098   -68.846 14.488  1.00 42.70  ?  203 PLC   C O2P   1 
HETATM 5448 O O3P   . PLC   L 6 .   ? 4.204   -66.353 13.679  1.00 48.85  ?  203 PLC   C O3P   1 
HETATM 5449 O O4P   . PLC   L 6 .   ? 6.184   -67.664 14.477  1.00 41.13  ?  203 PLC   C O4P   1 
HETATM 5450 N N     . PLC   L 6 .   ? 8.947   -67.494 16.045  1.00 40.96  ?  203 PLC   C N     1 
HETATM 5451 P P     . PLC   L 6 .   ? 4.827   -67.840 13.632  1.00 42.60  ?  203 PLC   C P     1 
HETATM 5452 N N1    . AZI   M 5 .   ? 19.063  -87.046 17.752  1.00 40.68  ?  204 AZI   C N1    1 
HETATM 5453 N N2    . AZI   M 5 .   ? 20.174  -86.746 17.644  1.00 45.25  ?  204 AZI   C N2    1 
HETATM 5454 N N3    . AZI   M 5 .   ? 21.273  -86.418 17.507  1.00 42.30  ?  204 AZI   C N3    1 
HETATM 5455 C C1    . LUT   N 4 .   ? -2.142  -56.981 24.654  1.00 22.21  ?  201 LUT   D C1    1 
HETATM 5456 C C2    . LUT   N 4 .   ? -2.121  -58.252 25.542  1.00 22.66  ?  201 LUT   D C2    1 
HETATM 5457 C C3    . LUT   N 4 .   ? -2.998  -58.295 26.780  1.00 24.98  ?  201 LUT   D C3    1 
HETATM 5458 C C4    . LUT   N 4 .   ? -3.647  -56.995 27.214  1.00 25.46  ?  201 LUT   D C4    1 
HETATM 5459 C C5    . LUT   N 4 .   ? -4.075  -56.100 26.081  1.00 24.27  ?  201 LUT   D C5    1 
HETATM 5460 C C6    . LUT   N 4 .   ? -3.277  -55.970 24.966  1.00 23.19  ?  201 LUT   D C6    1 
HETATM 5461 C C7    . LUT   N 4 .   ? -3.586  -54.868 24.051  1.00 22.65  ?  201 LUT   D C7    1 
HETATM 5462 C C8    . LUT   N 4 .   ? -2.878  -54.236 23.097  1.00 22.91  ?  201 LUT   D C8    1 
HETATM 5463 C C9    . LUT   N 4 .   ? -3.343  -53.066 22.442  1.00 25.16  ?  201 LUT   D C9    1 
HETATM 5464 C C10   . LUT   N 4 .   ? -2.661  -52.647 21.279  1.00 26.38  ?  201 LUT   D C10   1 
HETATM 5465 C C11   . LUT   N 4 .   ? -2.856  -51.553 20.500  1.00 26.07  ?  201 LUT   D C11   1 
HETATM 5466 C C12   . LUT   N 4 .   ? -2.432  -51.306 19.220  1.00 25.97  ?  201 LUT   D C12   1 
HETATM 5467 C C13   . LUT   N 4 .   ? -2.755  -50.219 18.365  1.00 26.41  ?  201 LUT   D C13   1 
HETATM 5468 C C14   . LUT   N 4 .   ? -1.953  -49.993 17.219  1.00 28.09  ?  201 LUT   D C14   1 
HETATM 5469 C C15   . LUT   N 4 .   ? -1.927  -48.919 16.342  1.00 30.30  ?  201 LUT   D C15   1 
HETATM 5470 C C16   . LUT   N 4 .   ? -2.272  -57.478 23.190  1.00 22.09  ?  201 LUT   D C16   1 
HETATM 5471 C C17   . LUT   N 4 .   ? -0.749  -56.313 24.779  1.00 20.81  ?  201 LUT   D C17   1 
HETATM 5472 C C18   . LUT   N 4 .   ? -5.331  -55.314 26.413  1.00 23.81  ?  201 LUT   D C18   1 
HETATM 5473 C C19   . LUT   N 4 .   ? -4.558  -52.252 22.855  1.00 26.71  ?  201 LUT   D C19   1 
HETATM 5474 C C20   . LUT   N 4 .   ? -4.036  -49.440 18.582  1.00 24.73  ?  201 LUT   D C20   1 
HETATM 5475 O O3    . LUT   N 4 .   ? -2.305  -58.835 27.885  1.00 25.94  ?  201 LUT   D O3    1 
HETATM 5476 C C21   . LUT   N 4 .   ? -0.418  -40.106 6.742   1.00 46.15  ?  201 LUT   D C21   1 
HETATM 5477 C C22   . LUT   N 4 .   ? -0.599  -38.585 6.547   1.00 50.03  ?  201 LUT   D C22   1 
HETATM 5478 C C23   . LUT   N 4 .   ? 0.716   -37.800 6.484   1.00 52.78  ?  201 LUT   D C23   1 
HETATM 5479 C C24   . LUT   N 4 .   ? 1.756   -38.313 7.446   1.00 52.88  ?  201 LUT   D C24   1 
HETATM 5480 C C25   . LUT   N 4 .   ? 1.751   -39.515 8.043   1.00 46.44  ?  201 LUT   D C25   1 
HETATM 5481 C C26   . LUT   N 4 .   ? 0.489   -40.388 8.005   1.00 43.45  ?  201 LUT   D C26   1 
HETATM 5482 C C27   . LUT   N 4 .   ? 0.748   -41.861 8.209   1.00 38.11  ?  201 LUT   D C27   1 
HETATM 5483 C C28   . LUT   N 4 .   ? 0.349   -42.623 9.259   1.00 35.75  ?  201 LUT   D C28   1 
HETATM 5484 C C29   . LUT   N 4 .   ? 0.618   -43.982 9.637   1.00 32.46  ?  201 LUT   D C29   1 
HETATM 5485 C C30   . LUT   N 4 .   ? 0.092   -44.452 10.872  1.00 30.90  ?  201 LUT   D C30   1 
HETATM 5486 C C31   . LUT   N 4 .   ? 0.175   -45.703 11.467  1.00 28.37  ?  201 LUT   D C31   1 
HETATM 5487 C C32   . LUT   N 4 .   ? -0.379  -46.143 12.632  1.00 27.62  ?  201 LUT   D C32   1 
HETATM 5488 C C33   . LUT   N 4 .   ? -0.256  -47.402 13.300  1.00 26.97  ?  201 LUT   D C33   1 
HETATM 5489 C C34   . LUT   N 4 .   ? -1.009  -47.641 14.451  1.00 27.91  ?  201 LUT   D C34   1 
HETATM 5490 C C35   . LUT   N 4 .   ? -1.125  -48.765 15.263  1.00 29.52  ?  201 LUT   D C35   1 
HETATM 5491 C C36   . LUT   N 4 .   ? 0.169   -40.714 5.459   1.00 45.93  ?  201 LUT   D C36   1 
HETATM 5492 C C37   . LUT   N 4 .   ? -1.810  -40.728 6.940   1.00 46.80  ?  201 LUT   D C37   1 
HETATM 5493 C C38   . LUT   N 4 .   ? 2.911   -39.976 8.892   1.00 42.33  ?  201 LUT   D C38   1 
HETATM 5494 C C39   . LUT   N 4 .   ? 1.371   -44.978 8.751   1.00 33.00  ?  201 LUT   D C39   1 
HETATM 5495 C C40   . LUT   N 4 .   ? 0.656   -48.499 12.762  1.00 25.21  ?  201 LUT   D C40   1 
HETATM 5496 O O23   . LUT   N 4 .   ? 0.498   -36.390 6.740   1.00 51.55  ?  201 LUT   D O23   1 
HETATM 5497 C C1    . PLC   O 6 .   ? 0.342   -44.578 19.725  1.00 21.75  ?  202 PLC   D C1    1 
HETATM 5498 C C2    . PLC   O 6 .   ? -0.681  -45.530 19.173  1.00 24.37  ?  202 PLC   D C2    1 
HETATM 5499 C C3    . PLC   O 6 .   ? -0.934  -45.369 17.698  1.00 26.31  ?  202 PLC   D C3    1 
HETATM 5500 C C4    . PLC   O 6 .   ? -0.027  -42.050 22.861  1.00 19.94  ?  202 PLC   D C4    1 
HETATM 5501 C C5    . PLC   O 6 .   ? 0.244   -40.577 22.953  1.00 20.75  ?  202 PLC   D C5    1 
HETATM 5502 C C6    . PLC   O 6 .   ? -2.076  -39.880 23.674  1.00 21.14  ?  202 PLC   D C6    1 
HETATM 5503 C C7    . PLC   O 6 .   ? -0.217  -38.337 23.825  1.00 22.67  ?  202 PLC   D C7    1 
HETATM 5504 C C8    . PLC   O 6 .   ? -0.318  -40.282 25.321  1.00 20.47  ?  202 PLC   D C8    1 
HETATM 5505 C "C'"  . PLC   O 6 .   ? -0.965  -47.675 20.324  1.00 27.03  ?  202 PLC   D "C'"  1 
HETATM 5506 C "C1'" . PLC   O 6 .   ? -0.358  -49.063 20.589  1.00 29.98  ?  202 PLC   D "C1'" 1 
HETATM 5507 C "C2'" . PLC   O 6 .   ? 0.930   -49.135 21.381  1.00 32.60  ?  202 PLC   D "C2'" 1 
HETATM 5508 C "C3'" . PLC   O 6 .   ? 1.305   -50.592 21.766  1.00 38.17  ?  202 PLC   D "C3'" 1 
HETATM 5509 C "C4'" . PLC   O 6 .   ? 2.161   -50.795 23.028  1.00 41.20  ?  202 PLC   D "C4'" 1 
HETATM 5510 C "C5'" . PLC   O 6 .   ? 2.839   -52.183 23.173  1.00 47.50  ?  202 PLC   D "C5'" 1 
HETATM 5511 C "C6'" . PLC   O 6 .   ? 4.312   -52.172 23.665  1.00 47.34  ?  202 PLC   D "C6'" 1 
HETATM 5512 C "C7'" . PLC   O 6 .   ? 5.434   -51.920 22.581  1.00 45.58  ?  202 PLC   D "C7'" 1 
HETATM 5513 C "C8'" . PLC   O 6 .   ? 6.295   -50.671 22.831  1.00 40.27  ?  202 PLC   D "C8'" 1 
HETATM 5514 C "C9'" . PLC   O 6 .   ? 7.451   -50.409 21.880  1.00 36.13  ?  202 PLC   D "C9'" 1 
HETATM 5515 C "CA'" . PLC   O 6 .   ? 8.830   -50.701 22.417  1.00 33.29  ?  202 PLC   D "CA'" 1 
HETATM 5516 C "CB'" . PLC   O 6 .   ? 9.946   -50.153 21.574  1.00 34.75  ?  202 PLC   D "CB'" 1 
HETATM 5517 C CB    . PLC   O 6 .   ? 0.393   -44.641 15.872  0.50 26.63  ?  202 PLC   D CB    1 
HETATM 5518 C C1B   . PLC   O 6 .   ? 1.820   -44.494 15.371  0.50 26.35  ?  202 PLC   D C1B   1 
HETATM 5519 C C2B   . PLC   O 6 .   ? 2.698   -45.715 15.551  0.50 26.37  ?  202 PLC   D C2B   1 
HETATM 5520 C C3B   . PLC   O 6 .   ? 4.008   -45.406 16.281  0.50 28.08  ?  202 PLC   D C3B   1 
HETATM 5521 C C4B   . PLC   O 6 .   ? 4.544   -46.516 17.183  0.50 27.81  ?  202 PLC   D C4B   1 
HETATM 5522 C C5B   . PLC   O 6 .   ? 5.983   -46.953 16.892  0.50 28.11  ?  202 PLC   D C5B   1 
HETATM 5523 C C6B   . PLC   O 6 .   ? 6.888   -45.851 16.379  0.50 29.33  ?  202 PLC   D C6B   1 
HETATM 5524 C C7B   . PLC   O 6 .   ? 8.312   -45.892 16.896  0.50 29.43  ?  202 PLC   D C7B   1 
HETATM 5525 C C8B   . PLC   O 6 .   ? 9.349   -45.565 15.856  0.50 30.45  ?  202 PLC   D C8B   1 
HETATM 5526 C C9B   . PLC   O 6 .   ? 9.407   -46.564 14.721  0.50 30.49  ?  202 PLC   D C9B   1 
HETATM 5527 C CAA   . PLC   O 6 .   ? 8.577   -46.226 13.513  0.50 29.78  ?  202 PLC   D CAA   1 
HETATM 5528 C CBA   . PLC   O 6 .   ? 9.385   -45.598 12.417  0.50 30.87  ?  202 PLC   D CBA   1 
HETATM 5529 O "O'"  . PLC   O 6 .   ? -2.062  -47.356 20.738  1.00 25.17  ?  202 PLC   D "O'"  1 
HETATM 5530 O OB    . PLC   O 6 .   ? -0.602  -44.322 15.321  1.00 29.32  ?  202 PLC   D OB    1 
HETATM 5531 O O2    . PLC   O 6 .   ? -0.257  -46.904 19.475  1.00 24.54  ?  202 PLC   D O2    1 
HETATM 5532 O O3    . PLC   O 6 .   ? 0.347   -45.149 17.081  1.00 26.88  ?  202 PLC   D O3    1 
HETATM 5533 O O1P   . PLC   O 6 .   ? 2.638   -44.106 21.339  1.00 17.60  ?  202 PLC   D O1P   1 
HETATM 5534 O O2P   . PLC   O 6 .   ? 1.260   -44.701 23.497  1.00 18.27  ?  202 PLC   D O2P   1 
HETATM 5535 O O3P   . PLC   O 6 .   ? 0.167   -44.644 21.140  1.00 19.49  ?  202 PLC   D O3P   1 
HETATM 5536 O O4P   . PLC   O 6 .   ? 0.926   -42.608 22.004  1.00 21.04  ?  202 PLC   D O4P   1 
HETATM 5537 N N     . PLC   O 6 .   ? -0.599  -39.783 23.948  1.00 21.53  ?  202 PLC   D N     1 
HETATM 5538 P P     . PLC   O 6 .   ? 1.346   -44.154 22.088  1.00 19.37  ?  202 PLC   D P     1 
HETATM 5539 N N1    . AZI   P 5 .   ? -6.410  -30.240 23.275  1.00 43.53  ?  203 AZI   D N1    1 
HETATM 5540 N N2    . AZI   P 5 .   ? -7.028  -30.928 23.972  1.00 58.98  ?  203 AZI   D N2    1 
HETATM 5541 N N3    . AZI   P 5 .   ? -7.602  -31.663 24.662  1.00 39.49  ?  203 AZI   D N3    1 
HETATM 5542 N N1    . AZI   Q 5 .   ? -1.591  -47.168 43.579  1.00 41.76  ?  101 AZI   E N1    1 
HETATM 5543 N N2    . AZI   Q 5 .   ? -0.596  -47.750 43.504  1.00 35.05  ?  101 AZI   E N2    1 
HETATM 5544 N N3    . AZI   Q 5 .   ? 0.358   -48.369 43.461  1.00 25.09  ?  101 AZI   E N3    1 
HETATM 5545 N N1    . AZI   R 5 .   ? 16.371  -27.620 28.316  1.00 46.74  ?  102 AZI   E N1    1 
HETATM 5546 N N2    . AZI   R 5 .   ? 16.861  -28.482 27.730  1.00 47.85  ?  102 AZI   E N2    1 
HETATM 5547 N N3    . AZI   R 5 .   ? 17.372  -29.342 27.174  1.00 43.37  ?  102 AZI   E N3    1 
HETATM 5548 C C1    . PLC   S 6 .   ? 7.104   -39.113 8.741   0.50 49.16  ?  201 PLC   F C1    1 
HETATM 5549 C C2    . PLC   S 6 .   ? 7.522   -40.155 7.721   0.50 48.71  ?  201 PLC   F C2    1 
HETATM 5550 C C3    . PLC   S 6 .   ? 8.985   -40.542 7.774   0.50 47.55  ?  201 PLC   F C3    1 
HETATM 5551 C C4    . PLC   S 6 .   ? 6.177   -36.414 11.135  1.00 48.85  ?  201 PLC   F C4    1 
HETATM 5552 C C5    . PLC   S 6 .   ? 5.340   -36.670 12.365  1.00 46.94  ?  201 PLC   F C5    1 
HETATM 5553 C C6    . PLC   S 6 .   ? 4.712   -34.373 13.101  1.00 48.90  ?  201 PLC   F C6    1 
HETATM 5554 C C7    . PLC   S 6 .   ? 3.450   -36.293 13.838  1.00 47.99  ?  201 PLC   F C7    1 
HETATM 5555 C C8    . PLC   S 6 .   ? 3.272   -35.561 11.540  1.00 47.56  ?  201 PLC   F C8    1 
HETATM 5556 C "C'"  . PLC   S 6 .   ? 6.315   -41.967 6.724   0.50 47.80  ?  201 PLC   F "C'"  1 
HETATM 5557 C "C1'" . PLC   S 6 .   ? 6.995   -41.406 5.488   0.50 48.98  ?  201 PLC   F "C1'" 1 
HETATM 5558 C "C2'" . PLC   S 6 .   ? 6.331   -41.802 4.199   0.50 48.84  ?  201 PLC   F "C2'" 1 
HETATM 5559 C "C3'" . PLC   S 6 .   ? 7.293   -42.303 3.118   0.50 47.69  ?  201 PLC   F "C3'" 1 
HETATM 5560 C "C4'" . PLC   S 6 .   ? 7.973   -43.636 3.390   0.50 46.45  ?  201 PLC   F "C4'" 1 
HETATM 5561 C "C5'" . PLC   S 6 .   ? 7.038   -44.811 3.591   1.00 47.02  ?  201 PLC   F "C5'" 1 
HETATM 5562 C "C6'" . PLC   S 6 .   ? 7.647   -46.237 3.459   1.00 46.03  ?  201 PLC   F "C6'" 1 
HETATM 5563 C "C7'" . PLC   S 6 .   ? 7.898   -47.005 4.741   1.00 46.07  ?  201 PLC   F "C7'" 1 
HETATM 5564 C "C8'" . PLC   S 6 .   ? 7.998   -48.528 4.599   1.00 45.85  ?  201 PLC   F "C8'" 1 
HETATM 5565 C "C9'" . PLC   S 6 .   ? 8.045   -49.271 5.930   1.00 47.21  ?  201 PLC   F "C9'" 1 
HETATM 5566 C "CA'" . PLC   S 6 .   ? 8.459   -50.732 5.882   1.00 52.10  ?  201 PLC   F "CA'" 1 
HETATM 5567 C "CB'" . PLC   S 6 .   ? 9.019   -51.311 7.183   1.00 53.58  ?  201 PLC   F "CB'" 1 
HETATM 5568 C CB    . PLC   S 6 .   ? 9.113   -40.337 10.129  0.50 42.86  ?  201 PLC   F CB    1 
HETATM 5569 C C1B   . PLC   S 6 .   ? 10.033  -40.683 11.264  0.50 41.93  ?  201 PLC   F C1B   1 
HETATM 5570 C C2B   . PLC   S 6 .   ? 11.471  -40.412 10.995  0.50 42.08  ?  201 PLC   F C2B   1 
HETATM 5571 C C3B   . PLC   S 6 .   ? 12.360  -41.490 11.583  0.50 41.00  ?  201 PLC   F C3B   1 
HETATM 5572 C C4B   . PLC   S 6 .   ? 11.608  -42.535 12.350  0.50 39.66  ?  201 PLC   F C4B   1 
HETATM 5573 C C5B   . PLC   S 6 .   ? 12.405  -43.763 12.631  0.50 39.51  ?  201 PLC   F C5B   1 
HETATM 5574 C C6B   . PLC   S 6 .   ? 11.897  -44.991 11.916  0.50 39.56  ?  201 PLC   F C6B   1 
HETATM 5575 C C7B   . PLC   S 6 .   ? 12.684  -46.246 12.227  0.50 39.19  ?  201 PLC   F C7B   1 
HETATM 5576 C C8B   . PLC   S 6 .   ? 13.073  -47.070 11.017  0.50 39.02  ?  201 PLC   F C8B   1 
HETATM 5577 C C9B   . PLC   S 6 .   ? 13.070  -48.554 11.252  0.50 36.11  ?  201 PLC   F C9B   1 
HETATM 5578 C CAA   . PLC   S 6 .   ? 13.117  -48.930 12.695  0.50 34.74  ?  201 PLC   F CAA   1 
HETATM 5579 C CBA   . PLC   S 6 .   ? 11.754  -49.247 13.253  0.50 34.05  ?  201 PLC   F CBA   1 
HETATM 5580 O "O'"  . PLC   S 6 .   ? 5.501   -42.859 6.737   0.50 44.82  ?  201 PLC   F "O'"  1 
HETATM 5581 O OB    . PLC   S 6 .   ? 8.203   -39.561 10.192  0.50 41.63  ?  201 PLC   F OB    1 
HETATM 5582 O O2    . PLC   S 6 .   ? 6.695   -41.343 7.857   0.50 49.05  ?  201 PLC   F O2    1 
HETATM 5583 O O3    . PLC   S 6 .   ? 9.365   -41.083 9.062   0.50 43.95  ?  201 PLC   F O3    1 
HETATM 5584 O O1P   . PLC   S 6 .   ? 4.877   -36.581 7.621   1.00 45.95  ?  201 PLC   F O1P   1 
HETATM 5585 O O2P   . PLC   S 6 .   ? 7.152   -35.539 8.466   1.00 47.09  ?  201 PLC   F O2P   1 
HETATM 5586 O O3P   . PLC   S 6 .   ? 7.110   -37.791 8.094   1.00 49.50  ?  201 PLC   F O3P   1 
HETATM 5587 O O4P   . PLC   S 6 .   ? 5.510   -36.930 9.948   1.00 50.40  ?  201 PLC   F O4P   1 
HETATM 5588 N N     . PLC   S 6 .   ? 4.204   -35.719 12.696  1.00 47.19  ?  201 PLC   F N     1 
HETATM 5589 P P     . PLC   S 6 .   ? 6.100   -36.605 8.490   1.00 48.63  ?  201 PLC   F P     1 
HETATM 5590 C C1    . A1L6M T 7 .   ? 14.992  -30.932 25.546  1.00 34.65  ?  202 A1L6M F C1    1 
HETATM 5591 C C2    . A1L6M T 7 .   ? 13.580  -31.532 25.404  1.00 31.94  ?  202 A1L6M F C2    1 
HETATM 5592 C C3    . A1L6M T 7 .   ? 12.424  -30.753 25.990  1.00 31.81  ?  202 A1L6M F C3    1 
HETATM 5593 C C4    . A1L6M T 7 .   ? 12.403  -29.948 27.135  1.00 33.23  ?  202 A1L6M F C4    1 
HETATM 5594 C C5    . A1L6M T 7 .   ? 13.479  -29.556 28.107  1.00 34.83  ?  202 A1L6M F C5    1 
HETATM 5595 C C6    . A1L6M T 7 .   ? 11.065  -29.506 27.281  1.00 32.38  ?  202 A1L6M F C6    1 
HETATM 5596 O O1    . A1L6M T 7 .   ? 10.567  -28.746 28.163  1.00 34.31  ?  202 A1L6M F O1    1 
HETATM 5597 N N1    . A1L6M T 7 .   ? 10.294  -30.011 26.292  1.00 30.64  ?  202 A1L6M F N1    1 
HETATM 5598 C C7    . A1L6M T 7 .   ? 11.053  -30.819 25.488  1.00 29.94  ?  202 A1L6M F C7    1 
HETATM 5599 C C8    . A1L6M T 7 .   ? 10.477  -31.514 24.415  1.00 28.51  ?  202 A1L6M F C8    1 
HETATM 5600 C C9    . A1L6M T 7 .   ? 9.210   -31.889 23.912  1.00 26.22  ?  202 A1L6M F C9    1 
HETATM 5601 C C10   . A1L6M T 7 .   ? 7.939   -31.955 24.586  1.00 25.93  ?  202 A1L6M F C10   1 
HETATM 5602 C C11   . A1L6M T 7 .   ? 7.641   -31.745 26.053  1.00 26.01  ?  202 A1L6M F C11   1 
HETATM 5603 C C12   . A1L6M T 7 .   ? 6.976   -32.297 23.668  1.00 24.87  ?  202 A1L6M F C12   1 
HETATM 5604 C C13   . A1L6M T 7 .   ? 5.517   -32.523 23.954  1.00 25.41  ?  202 A1L6M F C13   1 
HETATM 5605 C C14   . A1L6M T 7 .   ? 4.660   -31.341 23.553  1.00 27.10  ?  202 A1L6M F C14   1 
HETATM 5606 C C15   . A1L6M T 7 .   ? 3.230   -31.445 24.075  1.00 26.66  ?  202 A1L6M F C15   1 
HETATM 5607 O O2    . A1L6M T 7 .   ? 2.804   -30.492 24.720  1.00 28.48  ?  202 A1L6M F O2    1 
HETATM 5608 O O3    . A1L6M T 7 .   ? 2.572   -32.436 23.767  1.00 24.50  ?  202 A1L6M F O3    1 
HETATM 5609 C C16   . A1L6M T 7 .   ? 7.609   -32.430 22.377  1.00 24.83  ?  202 A1L6M F C16   1 
HETATM 5610 N N2    . A1L6M T 7 .   ? 8.953   -32.155 22.576  1.00 25.28  ?  202 A1L6M F N2    1 
HETATM 5611 C C17   . A1L6M T 7 .   ? 6.888   -32.881 21.258  1.00 24.11  ?  202 A1L6M F C17   1 
HETATM 5612 C C18   . A1L6M T 7 .   ? 7.098   -33.239 19.914  1.00 23.80  ?  202 A1L6M F C18   1 
HETATM 5613 N N3    . A1L6M T 7 .   ? 8.295   -33.231 19.285  1.00 25.63  ?  202 A1L6M F N3    1 
HETATM 5614 C C19   . A1L6M T 7 .   ? 8.053   -33.590 17.950  1.00 25.25  ?  202 A1L6M F C19   1 
HETATM 5615 C C20   . A1L6M T 7 .   ? 9.130   -33.625 17.082  1.00 26.10  ?  202 A1L6M F C20   1 
HETATM 5616 C C21   . A1L6M T 7 .   ? 9.426   -34.211 15.857  1.00 27.62  ?  202 A1L6M F C21   1 
HETATM 5617 N N4    . A1L6M T 7 .   ? 8.669   -35.199 15.284  1.00 27.57  ?  202 A1L6M F N4    1 
HETATM 5618 C C22   . A1L6M T 7 .   ? 9.241   -35.587 14.114  1.00 29.20  ?  202 A1L6M F C22   1 
HETATM 5619 O O4    . A1L6M T 7 .   ? 8.705   -36.495 13.396  1.00 26.59  ?  202 A1L6M F O4    1 
HETATM 5620 C C23   . A1L6M T 7 .   ? 10.411  -34.842 13.897  1.00 31.48  ?  202 A1L6M F C23   1 
HETATM 5621 C C24   . A1L6M T 7 .   ? 11.207  -35.120 12.647  1.00 35.02  ?  202 A1L6M F C24   1 
HETATM 5622 O O5    . A1L6M T 7 .   ? 12.187  -34.095 12.458  1.00 37.40  ?  202 A1L6M F O5    1 
HETATM 5623 C C25   . A1L6M T 7 .   ? 11.853  -36.511 12.720  1.00 37.48  ?  202 A1L6M F C25   1 
HETATM 5624 C C26   . A1L6M T 7 .   ? 12.878  -36.885 11.655  1.00 41.90  ?  202 A1L6M F C26   1 
HETATM 5625 C C27   . A1L6M T 7 .   ? 12.360  -37.038 10.251  1.00 47.21  ?  202 A1L6M F C27   1 
HETATM 5626 C C28   . A1L6M T 7 .   ? 13.040  -37.126 9.090   1.00 58.06  ?  202 A1L6M F C28   1 
HETATM 5627 C C29   . A1L6M T 7 .   ? 14.521  -36.847 8.921   1.00 57.63  ?  202 A1L6M F C29   1 
HETATM 5628 C C30   . A1L6M T 7 .   ? 12.345  -37.587 7.821   1.00 65.11  ?  202 A1L6M F C30   1 
HETATM 5629 C C31   . A1L6M T 7 .   ? 12.145  -36.558 6.711   1.00 69.41  ?  202 A1L6M F C31   1 
HETATM 5630 C C32   . A1L6M T 7 .   ? 11.018  -37.047 5.836   1.00 77.86  ?  202 A1L6M F C32   1 
HETATM 5631 C C33   . A1L6M T 7 .   ? 11.006  -37.956 4.848   1.00 80.20  ?  202 A1L6M F C33   1 
HETATM 5632 C C34   . A1L6M T 7 .   ? 12.236  -38.491 4.145   1.00 76.47  ?  202 A1L6M F C34   1 
HETATM 5633 C C35   . A1L6M T 7 .   ? 9.683   -38.555 4.411   1.00 81.50  ?  202 A1L6M F C35   1 
HETATM 5634 C C36   . A1L6M T 7 .   ? 8.581   -37.563 4.001   1.00 79.94  ?  202 A1L6M F C36   1 
HETATM 5635 C C37   . A1L6M T 7 .   ? 7.517   -38.245 3.177   1.00 82.10  ?  202 A1L6M F C37   1 
HETATM 5636 C C38   . A1L6M T 7 .   ? 7.534   -38.633 1.896   1.00 77.69  ?  202 A1L6M F C38   1 
HETATM 5637 C C39   . A1L6M T 7 .   ? 8.649   -38.383 0.913   1.00 73.99  ?  202 A1L6M F C39   1 
HETATM 5638 C C40   . A1L6M T 7 .   ? 6.399   -39.395 1.294   1.00 76.35  ?  202 A1L6M F C40   1 
HETATM 5639 C C41   . A1L6M T 7 .   ? 10.576  -33.991 15.007  1.00 29.99  ?  202 A1L6M F C41   1 
HETATM 5640 C C42   . A1L6M T 7 .   ? 11.640  -32.930 15.185  1.00 32.09  ?  202 A1L6M F C42   1 
HETATM 5641 C C43   . A1L6M T 7 .   ? 6.708   -33.827 17.789  1.00 23.88  ?  202 A1L6M F C43   1 
HETATM 5642 C C44   . A1L6M T 7 .   ? 5.981   -34.146 16.522  1.00 25.16  ?  202 A1L6M F C44   1 
HETATM 5643 O O6    . A1L6M T 7 .   ? 6.020   -35.505 16.121  1.00 25.22  ?  202 A1L6M F O6    1 
HETATM 5644 C C45   . A1L6M T 7 .   ? 6.130   -33.577 18.994  1.00 23.58  ?  202 A1L6M F C45   1 
HETATM 5645 C C46   . A1L6M T 7 .   ? 4.672   -33.703 19.343  1.00 23.62  ?  202 A1L6M F C46   1 
HETATM 5646 C C47   . A1L6M T 7 .   ? 4.320   -34.933 20.193  1.00 23.42  ?  202 A1L6M F C47   1 
HETATM 5647 C C48   . A1L6M T 7 .   ? 4.270   -36.306 19.536  1.00 21.87  ?  202 A1L6M F C48   1 
HETATM 5648 O O7    . A1L6M T 7 .   ? 3.877   -37.161 20.338  1.00 21.08  ?  202 A1L6M F O7    1 
HETATM 5649 O O8    . A1L6M T 7 .   ? 4.623   -36.525 18.335  1.00 22.03  ?  202 A1L6M F O8    1 
HETATM 5650 O O     . HOH   U 8 .   ? 25.349  -71.804 32.609  1.00 35.94  ?  301 HOH   A O     1 
HETATM 5651 O O     . HOH   U 8 .   ? 24.412  -50.459 19.434  1.00 24.15  ?  302 HOH   A O     1 
HETATM 5652 O O     . HOH   U 8 .   ? 19.253  -54.248 4.597   1.00 24.74  ?  303 HOH   A O     1 
HETATM 5653 O O     . HOH   U 8 .   ? 22.975  -62.121 20.910  1.00 30.15  ?  304 HOH   A O     1 
HETATM 5654 O O     . HOH   U 8 .   ? 23.059  -40.447 18.140  1.00 38.87  ?  305 HOH   A O     1 
HETATM 5655 O O     . HOH   U 8 .   ? 29.487  -55.206 27.773  1.00 28.70  ?  306 HOH   A O     1 
HETATM 5656 O O     . HOH   U 8 .   ? 29.063  -49.388 15.368  1.00 32.24  ?  307 HOH   A O     1 
HETATM 5657 O O     . HOH   U 8 .   ? 25.942  -68.425 28.601  1.00 26.43  ?  308 HOH   A O     1 
HETATM 5658 O O     . HOH   U 8 .   ? 26.431  -52.660 12.856  1.00 30.20  ?  309 HOH   A O     1 
HETATM 5659 O O     . HOH   U 8 .   ? 20.176  -48.364 17.358  1.00 27.69  ?  310 HOH   A O     1 
HETATM 5660 O O     . HOH   U 8 .   ? 31.329  -56.473 18.911  1.00 32.79  ?  311 HOH   A O     1 
HETATM 5661 O O     . HOH   U 8 .   ? 19.175  -69.023 9.301   1.00 20.51  ?  312 HOH   A O     1 
HETATM 5662 O O     . HOH   U 8 .   ? 19.222  -71.231 27.424  1.00 22.78  ?  313 HOH   A O     1 
HETATM 5663 O O     . HOH   U 8 .   ? 33.777  -51.237 19.730  1.00 38.83  ?  314 HOH   A O     1 
HETATM 5664 O O     . HOH   U 8 .   ? 12.633  -60.877 17.091  1.00 26.80  ?  315 HOH   A O     1 
HETATM 5665 O O     . HOH   U 8 .   ? 19.333  -71.993 32.127  1.00 25.77  ?  316 HOH   A O     1 
HETATM 5666 O O     . HOH   U 8 .   ? 21.861  -59.470 4.010   1.00 28.68  ?  317 HOH   A O     1 
HETATM 5667 O O     . HOH   U 8 .   ? 11.339  -69.339 12.856  1.00 30.05  ?  318 HOH   A O     1 
HETATM 5668 O O     . HOH   U 8 .   ? 11.932  -67.340 10.810  1.00 35.89  ?  319 HOH   A O     1 
HETATM 5669 O O     . HOH   U 8 .   ? 22.836  -63.640 34.544  1.00 31.52  ?  320 HOH   A O     1 
HETATM 5670 O O     . HOH   U 8 .   ? 16.784  -49.901 0.513   1.00 33.87  ?  321 HOH   A O     1 
HETATM 5671 O O     . HOH   U 8 .   ? 23.614  -66.222 17.764  1.00 27.34  ?  322 HOH   A O     1 
HETATM 5672 O O     . HOH   U 8 .   ? 22.226  -69.831 14.632  1.00 28.08  ?  323 HOH   A O     1 
HETATM 5673 O O     . HOH   U 8 .   ? 30.635  -60.932 20.087  1.00 30.09  ?  324 HOH   A O     1 
HETATM 5674 O O     . HOH   U 8 .   ? 20.625  -66.935 9.568   1.00 20.87  ?  325 HOH   A O     1 
HETATM 5675 O O     . HOH   U 8 .   ? 19.410  -66.604 20.053  1.00 24.19  ?  326 HOH   A O     1 
HETATM 5676 O O     . HOH   U 8 .   ? 26.368  -71.863 28.005  1.00 28.28  ?  327 HOH   A O     1 
HETATM 5677 O O     . HOH   U 8 .   ? 19.315  -68.311 18.101  1.00 27.63  ?  328 HOH   A O     1 
HETATM 5678 O O     . HOH   U 8 .   ? -6.498  -30.589 7.803   1.00 34.12  ?  329 HOH   A O     1 
HETATM 5679 O O     . HOH   U 8 .   ? 21.478  -64.743 19.354  1.00 25.29  ?  330 HOH   A O     1 
HETATM 5680 O O     . HOH   U 8 .   ? 12.872  -62.154 11.889  1.00 30.14  ?  331 HOH   A O     1 
HETATM 5681 O O     . HOH   U 8 .   ? 23.095  -66.411 8.409   1.00 30.61  ?  332 HOH   A O     1 
HETATM 5682 O O     . HOH   V 8 .   ? 31.928  -54.047 27.364  1.00 30.64  ?  201 HOH   B O     1 
HETATM 5683 O O     . HOH   V 8 .   ? 27.736  -40.130 16.302  1.00 36.39  ?  202 HOH   B O     1 
HETATM 5684 O O     . HOH   V 8 .   ? 15.849  -81.061 37.347  1.00 29.40  ?  203 HOH   B O     1 
HETATM 5685 O O     . HOH   V 8 .   ? 20.488  -44.471 19.682  1.00 33.87  ?  204 HOH   B O     1 
HETATM 5686 O O     . HOH   V 8 .   ? 30.336  -45.820 18.909  1.00 42.66  ?  205 HOH   B O     1 
HETATM 5687 O O     . HOH   V 8 .   ? 16.102  -70.735 48.615  1.00 39.42  ?  206 HOH   B O     1 
HETATM 5688 O O     . HOH   V 8 .   ? 34.541  -48.194 20.232  1.00 34.20  ?  207 HOH   B O     1 
HETATM 5689 O O     . HOH   V 8 .   ? 22.003  -74.922 37.917  1.00 27.76  ?  208 HOH   B O     1 
HETATM 5690 O O     . HOH   V 8 .   ? 10.582  -71.541 37.370  1.00 25.77  ?  209 HOH   B O     1 
HETATM 5691 O O     . HOH   V 8 .   ? 28.124  -40.881 23.225  1.00 32.89  ?  210 HOH   B O     1 
HETATM 5692 O O     . HOH   V 8 .   ? 23.123  -58.291 44.468  1.00 40.06  ?  211 HOH   B O     1 
HETATM 5693 O O     . HOH   V 8 .   ? 19.365  -75.695 35.363  1.00 34.79  ?  212 HOH   B O     1 
HETATM 5694 O O     . HOH   V 8 .   ? 20.086  -81.107 38.973  1.00 27.15  ?  213 HOH   B O     1 
HETATM 5695 O O     . HOH   V 8 .   ? 10.765  -69.862 39.988  1.00 25.99  ?  214 HOH   B O     1 
HETATM 5696 O O     . HOH   V 8 .   ? 25.207  -63.674 38.731  1.00 39.51  ?  215 HOH   B O     1 
HETATM 5697 O O     . HOH   V 8 .   ? 17.828  -62.576 46.912  1.00 25.89  ?  216 HOH   B O     1 
HETATM 5698 O O     . HOH   V 8 .   ? 29.956  -48.584 33.148  1.00 28.90  ?  217 HOH   B O     1 
HETATM 5699 O O     . HOH   V 8 .   ? 8.649   -70.021 36.633  1.00 27.01  ?  218 HOH   B O     1 
HETATM 5700 O O     . HOH   V 8 .   ? 22.976  -65.305 39.788  1.00 37.80  ?  219 HOH   B O     1 
HETATM 5701 O O     . HOH   W 8 .   ? 21.005  -79.938 31.891  1.00 28.49  ?  301 HOH   C O     1 
HETATM 5702 O O     . HOH   W 8 .   ? -1.047  -72.185 35.442  1.00 25.81  ?  302 HOH   C O     1 
HETATM 5703 O O     . HOH   W 8 .   ? 22.376  -91.607 27.068  1.00 39.14  ?  303 HOH   C O     1 
HETATM 5704 O O     . HOH   W 8 .   ? 9.405   -82.891 44.483  1.00 28.93  ?  304 HOH   C O     1 
HETATM 5705 O O     . HOH   W 8 .   ? 12.194  -63.982 18.168  1.00 23.28  ?  305 HOH   C O     1 
HETATM 5706 O O     . HOH   W 8 .   ? 20.337  -49.931 23.694  1.00 29.64  ?  306 HOH   C O     1 
HETATM 5707 O O     . HOH   W 8 .   ? 27.035  -75.502 21.214  1.00 50.36  ?  307 HOH   C O     1 
HETATM 5708 O O     . HOH   W 8 .   ? 12.307  -58.630 18.464  1.00 13.85  ?  308 HOH   C O     1 
HETATM 5709 O O     . HOH   W 8 .   ? 7.411   -66.111 26.533  1.00 22.63  ?  309 HOH   C O     1 
HETATM 5710 O O     . HOH   W 8 .   ? 15.748  -63.771 19.570  1.00 19.98  ?  310 HOH   C O     1 
HETATM 5711 O O     . HOH   W 8 .   ? 22.947  -50.503 21.807  1.00 20.46  ?  311 HOH   C O     1 
HETATM 5712 O O     . HOH   W 8 .   ? 19.168  -83.445 23.293  1.00 34.08  ?  312 HOH   C O     1 
HETATM 5713 O O     . HOH   W 8 .   ? 8.304   -82.228 38.019  1.00 25.05  ?  313 HOH   C O     1 
HETATM 5714 O O     . HOH   W 8 .   ? 17.088  -56.674 22.616  1.00 19.30  ?  314 HOH   C O     1 
HETATM 5715 O O     . HOH   W 8 .   ? 17.862  -71.143 30.027  1.00 19.47  ?  315 HOH   C O     1 
HETATM 5716 O O     . HOH   W 8 .   ? 5.801   -82.485 17.853  1.00 26.57  ?  316 HOH   C O     1 
HETATM 5717 O O     . HOH   W 8 .   ? 13.720  -73.957 42.296  1.00 27.23  ?  317 HOH   C O     1 
HETATM 5718 O O     . HOH   W 8 .   ? 15.631  -55.197 24.439  1.00 18.05  ?  318 HOH   C O     1 
HETATM 5719 O O     . HOH   W 8 .   ? 17.942  -76.651 33.334  1.00 31.49  ?  319 HOH   C O     1 
HETATM 5720 O O     . HOH   W 8 .   ? 6.859   -88.167 35.319  1.00 29.99  ?  320 HOH   C O     1 
HETATM 5721 O O     . HOH   W 8 .   ? -3.846  -75.487 18.137  1.00 24.03  ?  321 HOH   C O     1 
HETATM 5722 O O     . HOH   W 8 .   ? 0.167   -64.336 34.680  1.00 51.26  ?  322 HOH   C O     1 
HETATM 5723 O O     . HOH   W 8 .   ? 14.532  -63.742 23.679  1.00 17.37  ?  323 HOH   C O     1 
HETATM 5724 O O     . HOH   W 8 .   ? -4.890  -78.498 34.401  1.00 37.65  ?  324 HOH   C O     1 
HETATM 5725 O O     . HOH   W 8 .   ? -1.423  -76.058 31.057  1.00 22.80  ?  325 HOH   C O     1 
HETATM 5726 O O     . HOH   W 8 .   ? 8.791   -69.869 11.889  1.00 32.32  ?  326 HOH   C O     1 
HETATM 5727 O O     . HOH   W 8 .   ? -2.528  -63.115 29.940  1.00 20.48  ?  327 HOH   C O     1 
HETATM 5728 O O     . HOH   W 8 .   ? 5.989   -70.103 38.303  1.00 31.70  ?  328 HOH   C O     1 
HETATM 5729 O O     . HOH   W 8 .   ? 16.851  -65.241 23.849  1.00 18.57  ?  329 HOH   C O     1 
HETATM 5730 O O     . HOH   W 8 .   ? 1.540   -64.198 32.114  1.00 22.57  ?  330 HOH   C O     1 
HETATM 5731 O O     . HOH   W 8 .   ? 3.782   -64.513 30.545  1.00 26.33  ?  331 HOH   C O     1 
HETATM 5732 O O     . HOH   W 8 .   ? -2.708  -76.898 28.642  1.00 28.68  ?  332 HOH   C O     1 
HETATM 5733 O O     . HOH   W 8 .   ? 17.345  -87.651 29.312  1.00 31.99  ?  333 HOH   C O     1 
HETATM 5734 O O     . HOH   W 8 .   ? 2.595   -73.635 29.486  1.00 19.28  ?  334 HOH   C O     1 
HETATM 5735 O O     . HOH   W 8 .   ? 8.296   -54.508 30.869  1.00 24.73  ?  335 HOH   C O     1 
HETATM 5736 O O     . HOH   W 8 .   ? 4.912   -53.798 27.041  1.00 33.62  ?  336 HOH   C O     1 
HETATM 5737 O O     . HOH   W 8 .   ? 22.103  -84.018 15.419  1.00 40.23  ?  337 HOH   C O     1 
HETATM 5738 O O     . HOH   W 8 .   ? -1.181  -72.945 38.605  1.00 34.21  ?  338 HOH   C O     1 
HETATM 5739 O O     . HOH   W 8 .   ? 15.602  -54.103 30.737  1.00 26.94  ?  339 HOH   C O     1 
HETATM 5740 O O     . HOH   W 8 .   ? -2.268  -71.555 18.110  1.00 28.35  ?  340 HOH   C O     1 
HETATM 5741 O O     . HOH   W 8 .   ? 1.581   -83.406 9.069   1.00 23.84  ?  341 HOH   C O     1 
HETATM 5742 O O     . HOH   W 8 .   ? 14.439  -80.676 8.029   1.00 36.02  ?  342 HOH   C O     1 
HETATM 5743 O O     . HOH   W 8 .   ? 24.095  -71.859 21.451  1.00 12.74  ?  343 HOH   C O     1 
HETATM 5744 O O     . HOH   W 8 .   ? 16.850  -54.247 27.564  1.00 30.93  ?  344 HOH   C O     1 
HETATM 5745 O O     . HOH   W 8 .   ? 9.279   -89.400 18.050  1.00 36.81  ?  345 HOH   C O     1 
HETATM 5746 O O     . HOH   W 8 .   ? -6.969  -71.990 31.166  1.00 14.14  ?  346 HOH   C O     1 
HETATM 5747 O O     . HOH   W 8 .   ? 6.876   -89.562 9.710   1.00 32.01  ?  347 HOH   C O     1 
HETATM 5748 O O     . HOH   W 8 .   ? 19.993  -82.250 25.591  1.00 35.15  ?  348 HOH   C O     1 
HETATM 5749 O O     . HOH   W 8 .   ? -2.750  -76.242 11.576  1.00 19.26  ?  349 HOH   C O     1 
HETATM 5750 O O     . HOH   W 8 .   ? 14.522  -48.551 33.109  1.00 28.35  ?  350 HOH   C O     1 
HETATM 5751 O O     . HOH   W 8 .   ? -5.278  -61.469 31.345  1.00 25.49  ?  351 HOH   C O     1 
HETATM 5752 O O     . HOH   W 8 .   ? 0.297   -52.980 27.317  1.00 31.60  ?  352 HOH   C O     1 
HETATM 5753 O O     . HOH   W 8 .   ? 7.969   -63.732 33.067  1.00 35.41  ?  353 HOH   C O     1 
HETATM 5754 O O     . HOH   W 8 .   ? -6.584  -72.397 18.552  1.00 28.34  ?  354 HOH   C O     1 
HETATM 5755 O O     . HOH   W 8 .   ? 17.038  -65.604 20.948  1.00 19.23  ?  355 HOH   C O     1 
HETATM 5756 O O     . HOH   W 8 .   ? 4.458   -84.998 5.460   1.00 34.92  ?  356 HOH   C O     1 
HETATM 5757 O O     . HOH   W 8 .   ? 5.953   -65.262 32.436  1.00 36.55  ?  357 HOH   C O     1 
HETATM 5758 O O     . HOH   X 8 .   ? 2.553   -41.307 17.771  1.00 25.52  ?  301 HOH   D O     1 
HETATM 5759 O O     . HOH   X 8 .   ? -9.880  -49.206 25.224  1.00 23.86  ?  302 HOH   D O     1 
HETATM 5760 O O     . HOH   X 8 .   ? -3.925  -42.869 37.128  1.00 18.15  ?  303 HOH   D O     1 
HETATM 5761 O O     . HOH   X 8 .   ? 3.777   -43.523 19.114  1.00 20.41  ?  304 HOH   D O     1 
HETATM 5762 O O     . HOH   X 8 .   ? -1.611  -29.903 32.174  1.00 25.48  ?  305 HOH   D O     1 
HETATM 5763 O O     . HOH   X 8 .   ? -0.245  -67.658 4.783   1.00 38.38  ?  306 HOH   D O     1 
HETATM 5764 O O     . HOH   X 8 .   ? -4.551  -49.784 29.443  1.00 22.57  ?  307 HOH   D O     1 
HETATM 5765 O O     . HOH   X 8 .   ? -9.669  -50.188 14.018  1.00 28.43  ?  308 HOH   D O     1 
HETATM 5766 O O     . HOH   X 8 .   ? 2.799   -43.869 25.452  1.00 15.08  ?  309 HOH   D O     1 
HETATM 5767 O O     . HOH   X 8 .   ? -10.865 -55.420 22.043  1.00 32.31  ?  310 HOH   D O     1 
HETATM 5768 O O     . HOH   X 8 .   ? -2.547  -30.095 34.667  1.00 33.54  ?  311 HOH   D O     1 
HETATM 5769 O O     . HOH   X 8 .   ? -4.621  -28.916 24.741  1.00 18.14  ?  312 HOH   D O     1 
HETATM 5770 O O     . HOH   X 8 .   ? -10.411 -51.651 29.529  1.00 30.31  ?  313 HOH   D O     1 
HETATM 5771 O O     . HOH   X 8 .   ? 2.919   -28.362 26.642  1.00 29.58  ?  314 HOH   D O     1 
HETATM 5772 O O     . HOH   X 8 .   ? -3.025  -60.292 30.077  1.00 30.17  ?  315 HOH   D O     1 
HETATM 5773 O O     . HOH   X 8 .   ? -9.946  -37.251 29.561  1.00 34.98  ?  316 HOH   D O     1 
HETATM 5774 O O     . HOH   X 8 .   ? -1.849  -52.827 25.864  1.00 27.18  ?  317 HOH   D O     1 
HETATM 5775 O O     . HOH   X 8 .   ? -8.694  -30.610 28.965  1.00 37.61  ?  318 HOH   D O     1 
HETATM 5776 O O     . HOH   X 8 .   ? -3.083  -39.758 14.774  1.00 36.97  ?  319 HOH   D O     1 
HETATM 5777 O O     . HOH   X 8 .   ? -10.533 -46.812 20.153  1.00 34.08  ?  320 HOH   D O     1 
HETATM 5778 O O     . HOH   X 8 .   ? -12.502 -65.526 13.636  1.00 29.17  ?  321 HOH   D O     1 
HETATM 5779 O O     . HOH   X 8 .   ? -2.728  -33.221 20.288  1.00 21.06  ?  322 HOH   D O     1 
HETATM 5780 O O     . HOH   X 8 .   ? -1.466  -34.603 22.185  1.00 30.57  ?  323 HOH   D O     1 
HETATM 5781 O O     . HOH   X 8 .   ? -6.396  -35.073 23.466  1.00 26.10  ?  324 HOH   D O     1 
HETATM 5782 O O     . HOH   X 8 .   ? -10.140 -46.362 3.281   1.00 34.46  ?  325 HOH   D O     1 
HETATM 5783 O O     . HOH   X 8 .   ? -3.017  -36.448 23.867  1.00 34.03  ?  326 HOH   D O     1 
HETATM 5784 O O     . HOH   Y 8 .   ? -3.587  -40.674 38.514  1.00 28.67  ?  201 HOH   E O     1 
HETATM 5785 O O     . HOH   Y 8 .   ? -4.628  -50.451 37.213  1.00 30.50  ?  202 HOH   E O     1 
HETATM 5786 O O     . HOH   Y 8 .   ? 5.094   -38.418 50.219  1.00 27.06  ?  203 HOH   E O     1 
HETATM 5787 O O     . HOH   Y 8 .   ? -0.315  -55.911 29.030  1.00 31.87  ?  204 HOH   E O     1 
HETATM 5788 O O     . HOH   Y 8 .   ? 6.571   -36.907 48.785  1.00 30.90  ?  205 HOH   E O     1 
HETATM 5789 O O     . HOH   Y 8 .   ? 10.969  -36.570 45.293  1.00 30.96  ?  206 HOH   E O     1 
HETATM 5790 O O     . HOH   Y 8 .   ? -0.293  -49.827 32.280  1.00 25.42  ?  207 HOH   E O     1 
HETATM 5791 O O     . HOH   Y 8 .   ? 8.569   -44.416 31.471  1.00 22.30  ?  208 HOH   E O     1 
HETATM 5792 O O     . HOH   Y 8 .   ? 4.755   -30.718 46.571  1.00 26.58  ?  209 HOH   E O     1 
HETATM 5793 O O     . HOH   Y 8 .   ? 5.223   -32.406 40.955  1.00 34.92  ?  210 HOH   E O     1 
HETATM 5794 O O     . HOH   Y 8 .   ? 8.496   -43.739 35.564  1.00 31.65  ?  211 HOH   E O     1 
HETATM 5795 O O     . HOH   Y 8 .   ? 7.363   -40.063 39.646  1.00 24.54  ?  212 HOH   E O     1 
HETATM 5796 O O     . HOH   Y 8 .   ? -4.611  -57.792 37.265  1.00 23.32  ?  213 HOH   E O     1 
HETATM 5797 O O     . HOH   Y 8 .   ? 8.959   -42.205 39.695  1.00 27.96  ?  214 HOH   E O     1 
HETATM 5798 O O     . HOH   Y 8 .   ? 11.814  -49.090 33.879  1.00 26.67  ?  215 HOH   E O     1 
HETATM 5799 O O     . HOH   Y 8 .   ? 16.895  -32.212 42.494  1.00 24.78  ?  216 HOH   E O     1 
HETATM 5800 O O     . HOH   Y 8 .   ? 11.365  -38.522 47.313  1.00 35.91  ?  217 HOH   E O     1 
HETATM 5801 O O     . HOH   Y 8 .   ? 8.014   -30.516 40.455  1.00 28.50  ?  218 HOH   E O     1 
HETATM 5802 O O     . HOH   Z 8 .   ? 11.866  -34.695 20.013  1.00 29.25  ?  301 HOH   F O     1 
HETATM 5803 O O     . HOH   Z 8 .   ? 1.862   -34.452 8.970   1.00 35.21  ?  302 HOH   F O     1 
HETATM 5804 O O     . HOH   Z 8 .   ? 23.421  -31.868 19.870  1.00 51.41  ?  303 HOH   F O     1 
HETATM 5805 O O     . HOH   Z 8 .   ? 4.859   -36.920 22.936  1.00 26.56  ?  304 HOH   F O     1 
HETATM 5806 O O     . HOH   Z 8 .   ? 22.086  -37.617 17.536  1.00 28.63  ?  305 HOH   F O     1 
HETATM 5807 O O     . HOH   Z 8 .   ? -1.969  -49.219 30.264  1.00 17.77  ?  306 HOH   F O     1 
HETATM 5808 O O     . HOH   Z 8 .   ? 1.374   -37.817 20.869  1.00 28.47  ?  307 HOH   F O     1 
HETATM 5809 O O     . HOH   Z 8 .   ? 3.129   -38.369 17.105  1.00 29.02  ?  308 HOH   F O     1 
HETATM 5810 O O     . HOH   Z 8 .   ? 9.993   -44.835 33.654  1.00 39.76  ?  309 HOH   F O     1 
HETATM 5811 O O     . HOH   Z 8 .   ? 14.581  -44.619 27.574  1.00 24.78  ?  310 HOH   F O     1 
HETATM 5812 O O     . HOH   Z 8 .   ? 5.546   -27.807 27.831  1.00 32.03  ?  311 HOH   F O     1 
HETATM 5813 O O     . HOH   Z 8 .   ? 5.002   -44.927 26.505  1.00 16.92  ?  312 HOH   F O     1 
HETATM 5814 O O     . HOH   Z 8 .   ? -3.317  -38.310 26.366  1.00 25.68  ?  313 HOH   F O     1 
HETATM 5815 O O     . HOH   Z 8 .   ? 6.013   -44.960 29.642  1.00 33.83  ?  314 HOH   F O     1 
HETATM 5816 O O     . HOH   Z 8 .   ? 25.594  -39.200 17.611  1.00 31.20  ?  315 HOH   F O     1 
HETATM 5817 O O     . HOH   Z 8 .   ? 2.985   -35.396 23.888  1.00 26.79  ?  316 HOH   F O     1 
HETATM 5818 O O     . HOH   Z 8 .   ? 1.183   -49.977 30.172  1.00 17.70  ?  317 HOH   F O     1 
HETATM 5819 O O     . HOH   Z 8 .   ? -8.176  -18.592 15.792  1.00 49.36  ?  318 HOH   F O     1 
HETATM 5820 O O     . HOH   Z 8 .   ? -5.301  -28.959 6.158   1.00 43.69  ?  319 HOH   F O     1 
HETATM 5821 O O     . HOH   Z 8 .   ? 9.626   -44.119 37.892  1.00 34.60  ?  320 HOH   F O     1 
HETATM 5822 O O     . HOH   Z 8 .   ? 8.254   -43.756 42.022  1.00 32.29  ?  321 HOH   F O     1 
HETATM 5823 O O     . HOH   Z 8 .   ? 0.888   -35.723 22.279  1.00 32.13  ?  322 HOH   F O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . GLY   A 2   ? 0.7433 0.5665 0.7400 0.3173  -0.1410 0.0718  1   GLY   A N     
2    C CA    . GLY   A 2   ? 0.7036 0.5429 0.7080 0.2880  -0.1312 0.0653  1   GLY   A CA    
3    C C     . GLY   A 2   ? 0.6860 0.5379 0.6861 0.2650  -0.1311 0.0774  1   GLY   A C     
4    O O     . GLY   A 2   ? 0.7132 0.5780 0.7101 0.2725  -0.1388 0.0891  1   GLY   A O     
5    N N     . SER   A 3   ? 0.6439 0.4932 0.6433 0.2387  -0.1228 0.0743  2   SER   A N     
6    C CA    . SER   A 3   ? 0.6284 0.4853 0.6207 0.2171  -0.1212 0.0841  2   SER   A CA    
7    C C     . SER   A 3   ? 0.5830 0.4939 0.5919 0.2100  -0.1194 0.0801  2   SER   A C     
8    O O     . SER   A 3   ? 0.5581 0.4930 0.5833 0.2071  -0.1135 0.0678  2   SER   A O     
9    C CB    . SER   A 3   ? 0.6332 0.4636 0.6170 0.1934  -0.1129 0.0830  2   SER   A CB    
10   O OG    . SER   A 3   ? 0.6687 0.4473 0.6362 0.1951  -0.1151 0.0878  2   SER   A OG    
11   N N     . GLN   A 4   ? 0.5828 0.5069 0.5841 0.2028  -0.1238 0.0907  3   GLN   A N     
12   C CA    . GLN   A 4   ? 0.5494 0.5161 0.5604 0.1915  -0.1234 0.0885  3   GLN   A CA    
13   C C     . GLN   A 4   ? 0.5245 0.4817 0.5232 0.1675  -0.1166 0.0903  3   GLN   A C     
14   O O     . GLN   A 4   ? 0.5409 0.4641 0.5217 0.1621  -0.1151 0.0986  3   GLN   A O     
15   C CB    . GLN   A 4   ? 0.5731 0.5607 0.5822 0.2027  -0.1350 0.0984  3   GLN   A CB    
16   C CG    . GLN   A 4   ? 0.6106 0.6152 0.6338 0.2285  -0.1419 0.0973  3   GLN   A CG    
17   C CD    . GLN   A 4   ? 0.6122 0.6494 0.6598 0.2314  -0.1363 0.0837  3   GLN   A CD    
18   O OE1   . GLN   A 4   ? 0.6359 0.7141 0.6975 0.2215  -0.1362 0.0802  3   GLN   A OE1   
19   N NE2   . GLN   A 4   ? 0.6299 0.6459 0.6801 0.2419  -0.1310 0.0755  3   GLN   A NE2   
20   N N     . VAL   A 5   ? 0.4799 0.4675 0.4882 0.1544  -0.1127 0.0830  4   VAL   A N     
21   C CA    . VAL   A 5   ? 0.4693 0.4515 0.4676 0.1339  -0.1053 0.0823  4   VAL   A CA    
22   C C     . VAL   A 5   ? 0.4481 0.4580 0.4430 0.1261  -0.1100 0.0836  4   VAL   A C     
23   O O     . VAL   A 5   ? 0.4266 0.4681 0.4361 0.1299  -0.1154 0.0794  4   VAL   A O     
24   C CB    . VAL   A 5   ? 0.4490 0.4306 0.4582 0.1239  -0.0946 0.0707  4   VAL   A CB    
25   C CG1   . VAL   A 5   ? 0.4195 0.4370 0.4488 0.1232  -0.0937 0.0599  4   VAL   A CG1   
26   C CG2   . VAL   A 5   ? 0.4497 0.4190 0.4462 0.1059  -0.0865 0.0723  4   VAL   A CG2   
27   N N     . GLU   A 6   ? 0.4553 0.4523 0.4297 0.1150  -0.1081 0.0898  5   GLU   A N     
28   C CA    . GLU   A 6   ? 0.4568 0.4716 0.4222 0.1048  -0.1110 0.0889  5   GLU   A CA    
29   C C     . GLU   A 6   ? 0.4509 0.4519 0.4042 0.0901  -0.0998 0.0863  5   GLU   A C     
30   O O     . GLU   A 6   ? 0.4695 0.4475 0.4062 0.0876  -0.0953 0.0945  5   GLU   A O     
31   C CB    . GLU   A 6   ? 0.4870 0.5004 0.4340 0.1098  -0.1212 0.1001  5   GLU   A CB    
32   C CG    . GLU   A 6   ? 0.5017 0.5329 0.4603 0.1255  -0.1334 0.1040  5   GLU   A CG    
33   C CD    . GLU   A 6   ? 0.5423 0.5681 0.4810 0.1318  -0.1438 0.1169  5   GLU   A CD    
34   O OE1   . GLU   A 6   ? 0.5602 0.5733 0.4755 0.1224  -0.1420 0.1213  5   GLU   A OE1   
35   O OE2   . GLU   A 6   ? 0.5734 0.6072 0.5181 0.1475  -0.1537 0.1231  5   GLU   A OE2   
36   N N     . PHE   A 7   ? 0.4301 0.4459 0.3931 0.0811  -0.0949 0.0756  6   PHE   A N     
37   C CA    . PHE   A 7   ? 0.4228 0.4297 0.3774 0.0693  -0.0842 0.0718  6   PHE   A CA    
38   C C     . PHE   A 7   ? 0.4289 0.4498 0.3740 0.0618  -0.0875 0.0669  6   PHE   A C     
39   O O     . PHE   A 7   ? 0.4129 0.4521 0.3719 0.0591  -0.0904 0.0589  6   PHE   A O     
40   C CB    . PHE   A 7   ? 0.4015 0.4079 0.3747 0.0668  -0.0755 0.0636  6   PHE   A CB    
41   C CG    . PHE   A 7   ? 0.3823 0.3850 0.3508 0.0555  -0.0647 0.0589  6   PHE   A CG    
42   C CD1   . PHE   A 7   ? 0.3962 0.3845 0.3461 0.0505  -0.0586 0.0657  6   PHE   A CD1   
43   C CD2   . PHE   A 7   ? 0.3575 0.3728 0.3406 0.0508  -0.0603 0.0484  6   PHE   A CD2   
44   C CE1   . PHE   A 7   ? 0.3867 0.3753 0.3337 0.0422  -0.0484 0.0617  6   PHE   A CE1   
45   C CE2   . PHE   A 7   ? 0.3486 0.3613 0.3275 0.0424  -0.0510 0.0446  6   PHE   A CE2   
46   C CZ    . PHE   A 7   ? 0.3603 0.3607 0.3217 0.0387  -0.0451 0.0509  6   PHE   A CZ    
47   N N     . SER   A 8   ? 0.4619 0.4732 0.3821 0.0588  -0.0878 0.0722  7   SER   A N     
48   C CA    . SER   A 8   ? 0.4899 0.5062 0.3947 0.0514  -0.0892 0.0664  7   SER   A CA    
49   C C     . SER   A 8   ? 0.4667 0.4741 0.3666 0.0450  -0.0758 0.0617  7   SER   A C     
50   O O     . SER   A 8   ? 0.4714 0.4665 0.3662 0.0456  -0.0673 0.0681  7   SER   A O     
51   C CB    . SER   A 8   ? 0.5322 0.5429 0.4102 0.0531  -0.0963 0.0734  7   SER   A CB    
52   O OG    . SER   A 8   ? 0.6080 0.6324 0.4918 0.0579  -0.1105 0.0761  7   SER   A OG    
53   N N     . MET   A 9   ? 0.4584 0.4723 0.3598 0.0390  -0.0745 0.0515  8   MET   A N     
54   C CA    . MET   A 9   ? 0.4792 0.4858 0.3729 0.0349  -0.0626 0.0472  8   MET   A CA    
55   C C     . MET   A 9   ? 0.4526 0.4595 0.3321 0.0306  -0.0658 0.0382  8   MET   A C     
56   O O     . MET   A 9   ? 0.4406 0.4558 0.3250 0.0277  -0.0766 0.0340  8   MET   A O     
57   C CB    . MET   A 9   ? 0.4921 0.5016 0.4092 0.0333  -0.0533 0.0438  8   MET   A CB    
58   C CG    . MET   A 9   ? 0.5377 0.5607 0.4776 0.0321  -0.0582 0.0367  8   MET   A CG    
59   S SD    . MET   A 9   ? 0.5931 0.6210 0.5513 0.0278  -0.0481 0.0282  8   MET   A SD    
60   C CE    . MET   A 9   ? 0.5771 0.5991 0.5138 0.0234  -0.0449 0.0225  8   MET   A CE    
61   N N     . LYS   A 10  ? 0.4448 0.4428 0.3069 0.0303  -0.0566 0.0358  9   LYS   A N     
62   C CA    . LYS   A 10  ? 0.4473 0.4394 0.2926 0.0280  -0.0576 0.0263  9   LYS   A CA    
63   C C     . LYS   A 10  ? 0.4201 0.4123 0.2744 0.0278  -0.0445 0.0218  9   LYS   A C     
64   O O     . LYS   A 10  ? 0.4120 0.4041 0.2652 0.0307  -0.0333 0.0272  9   LYS   A O     
65   C CB    . LYS   A 10  ? 0.4783 0.4585 0.2879 0.0314  -0.0586 0.0266  9   LYS   A CB    
66   C CG    . LYS   A 10  ? 0.5166 0.4951 0.3093 0.0337  -0.0683 0.0341  9   LYS   A CG    
67   C CD    . LYS   A 10  ? 0.5573 0.5261 0.3165 0.0392  -0.0634 0.0383  9   LYS   A CD    
68   C CE    . LYS   A 10  ? 0.5630 0.5331 0.3239 0.0426  -0.0462 0.0444  9   LYS   A CE    
69   N NZ    . LYS   A 10  ? 0.6067 0.5743 0.3455 0.0471  -0.0406 0.0550  9   LYS   A NZ    
70   N N     . MET   A 11  ? 0.4091 0.4031 0.2734 0.0239  -0.0463 0.0133  10  MET   A N     
71   C CA    . MET   A 11  ? 0.4137 0.4082 0.2853 0.0244  -0.0356 0.0087  10  MET   A CA    
72   C C     . MET   A 11  ? 0.4382 0.4188 0.2835 0.0265  -0.0360 0.0010  10  MET   A C     
73   O O     . MET   A 11  ? 0.4713 0.4447 0.3080 0.0222  -0.0473 -0.0043 10  MET   A O     
74   C CB    . MET   A 11  ? 0.3972 0.4015 0.2959 0.0197  -0.0367 0.0048  10  MET   A CB    
75   C CG    . MET   A 11  ? 0.3954 0.4017 0.3021 0.0210  -0.0254 0.0014  10  MET   A CG    
76   S SD    . MET   A 11  ? 0.3918 0.4123 0.3315 0.0164  -0.0251 -0.0009 10  MET   A SD    
77   C CE    . MET   A 11  ? 0.3936 0.4086 0.3252 0.0109  -0.0359 -0.0076 10  MET   A CE    
78   N N     . THR   A 12  ? 0.4368 0.4142 0.2694 0.0332  -0.0244 0.0008  11  THR   A N     
79   C CA    . THR   A 12  ? 0.4545 0.4182 0.2633 0.0384  -0.0225 -0.0074 11  THR   A CA    
80   C C     . THR   A 12  ? 0.4472 0.4179 0.2700 0.0418  -0.0109 -0.0095 11  THR   A C     
81   O O     . THR   A 12  ? 0.4159 0.4021 0.2637 0.0395  -0.0042 -0.0042 11  THR   A O     
82   C CB    . THR   A 12  ? 0.4819 0.4368 0.2578 0.0464  -0.0196 -0.0063 11  THR   A CB    
83   O OG1   . THR   A 12  ? 0.4854 0.4547 0.2690 0.0502  -0.0065 0.0029  11  THR   A OG1   
84   C CG2   . THR   A 12  ? 0.4938 0.4427 0.2552 0.0430  -0.0321 -0.0038 11  THR   A CG2   
85   N N     . GLY   A 13  ? 0.4888 0.4465 0.2943 0.0474  -0.0098 -0.0177 12  GLY   A N     
86   C CA    . GLY   A 13  ? 0.4671 0.4309 0.2841 0.0518  -0.0004 -0.0200 12  GLY   A CA    
87   C C     . GLY   A 13  ? 0.4681 0.4129 0.2742 0.0521  -0.0072 -0.0294 12  GLY   A C     
88   O O     . GLY   A 13  ? 0.4786 0.4036 0.2645 0.0489  -0.0187 -0.0345 12  GLY   A O     
89   N N     . GLY   A 14  ? 0.4386 0.3903 0.2607 0.0539  -0.0013 -0.0306 13  GLY   A N     
90   C CA    . GLY   A 14  ? 0.4564 0.3887 0.2670 0.0559  -0.0061 -0.0382 13  GLY   A CA    
91   C C     . GLY   A 14  ? 0.4306 0.3745 0.2575 0.0616  0.0034  -0.0379 13  GLY   A C     
92   O O     . GLY   A 14  ? 0.4094 0.3781 0.2579 0.0628  0.0132  -0.0321 13  GLY   A O     
93   N N     . GLU   A 15  ? 0.4280 0.3523 0.2433 0.0643  -0.0010 -0.0440 14  GLU   A N     
94   C CA    . GLU   A 15  ? 0.4288 0.3609 0.2565 0.0705  0.0058  -0.0440 14  GLU   A CA    
95   C C     . GLU   A 15  ? 0.4233 0.3608 0.2380 0.0887  0.0182  -0.0449 14  GLU   A C     
96   O O     . GLU   A 15  ? 0.4399 0.3644 0.2278 0.0973  0.0191  -0.0481 14  GLU   A O     
97   C CB    . GLU   A 15  ? 0.4416 0.3502 0.2621 0.0654  -0.0044 -0.0483 14  GLU   A CB    
98   C CG    . GLU   A 15  ? 0.4198 0.3373 0.2630 0.0477  -0.0128 -0.0447 14  GLU   A CG    
99   C CD    . GLU   A 15  ? 0.4411 0.3376 0.2781 0.0391  -0.0235 -0.0469 14  GLU   A CD    
100  O OE1   . GLU   A 15  ? 0.5068 0.3715 0.3149 0.0390  -0.0324 -0.0521 14  GLU   A OE1   
101  O OE2   . GLU   A 15  ? 0.4253 0.3372 0.2860 0.0316  -0.0234 -0.0431 14  GLU   A OE2   
102  N N     . ILE   A 16  ? 0.3977 0.3589 0.2330 0.0940  0.0278  -0.0412 15  ILE   A N     
103  C CA    . ILE   A 16  ? 0.4154 0.3889 0.2443 0.1114  0.0400  -0.0409 15  ILE   A CA    
104  C C     . ILE   A 16  ? 0.4448 0.3948 0.2564 0.1230  0.0370  -0.0476 15  ILE   A C     
105  O O     . ILE   A 16  ? 0.4330 0.3769 0.2567 0.1148  0.0303  -0.0477 15  ILE   A O     
106  C CB    . ILE   A 16  ? 0.3946 0.4068 0.2573 0.1089  0.0498  -0.0330 15  ILE   A CB    
107  C CG1   . ILE   A 16  ? 0.3906 0.4223 0.2681 0.0980  0.0528  -0.0258 15  ILE   A CG1   
108  C CG2   . ILE   A 16  ? 0.4070 0.4374 0.2682 0.1267  0.0616  -0.0320 15  ILE   A CG2   
109  C CD1   . ILE   A 16  ? 0.3557 0.4181 0.2676 0.0891  0.0576  -0.0188 15  ILE   A CD1   
110  N N     . PRO   A 17  ? 0.4816 0.4190 0.2655 0.1430  0.0422  -0.0526 16  PRO   A N     
111  C CA    . PRO   A 17  ? 0.5159 0.4308 0.2842 0.1564  0.0400  -0.0582 16  PRO   A CA    
112  C C     . PRO   A 17  ? 0.4998 0.4421 0.2957 0.1605  0.0464  -0.0531 16  PRO   A C     
113  O O     . PRO   A 17  ? 0.4908 0.4717 0.3147 0.1565  0.0548  -0.0459 16  PRO   A O     
114  C CB    . PRO   A 17  ? 0.5554 0.4552 0.2881 0.1792  0.0458  -0.0648 16  PRO   A CB    
115  C CG    . PRO   A 17  ? 0.5484 0.4545 0.2730 0.1734  0.0474  -0.0636 16  PRO   A CG    
116  C CD    . PRO   A 17  ? 0.5001 0.4402 0.2623 0.1545  0.0495  -0.0537 16  PRO   A CD    
117  N N     . GLY   A 18  ? 0.5358 0.4561 0.3236 0.1663  0.0409  -0.0562 17  GLY   A N     
118  C CA    . GLY   A 18  ? 0.5115 0.4529 0.3162 0.1770  0.0470  -0.0526 17  GLY   A CA    
119  C C     . GLY   A 18  ? 0.4662 0.4248 0.3028 0.1591  0.0428  -0.0468 17  GLY   A C     
120  O O     . GLY   A 18  ? 0.4465 0.4069 0.2957 0.1393  0.0372  -0.0450 17  GLY   A O     
121  N N     . GLY   A 19  ? 0.4369 0.4084 0.2851 0.1677  0.0454  -0.0440 18  GLY   A N     
122  C CA    . GLY   A 19  ? 0.3986 0.3915 0.2764 0.1542  0.0431  -0.0386 18  GLY   A CA    
123  C C     . GLY   A 19  ? 0.3875 0.3502 0.2592 0.1387  0.0307  -0.0397 18  GLY   A C     
124  O O     . GLY   A 19  ? 0.4113 0.3343 0.2550 0.1409  0.0231  -0.0443 18  GLY   A O     
125  N N     . ASN   A 20  ? 0.3557 0.3385 0.2534 0.1220  0.0285  -0.0355 19  ASN   A N     
126  C CA    . ASN   A 20  ? 0.3522 0.3161 0.2492 0.1069  0.0183  -0.0348 19  ASN   A CA    
127  C C     . ASN   A 20  ? 0.3578 0.3050 0.2461 0.0934  0.0120  -0.0374 19  ASN   A C     
128  O O     . ASN   A 20  ? 0.3465 0.3148 0.2542 0.0815  0.0131  -0.0354 19  ASN   A O     
129  C CB    . ASN   A 20  ? 0.3134 0.3072 0.2396 0.0975  0.0192  -0.0298 19  ASN   A CB    
130  C CG    . ASN   A 20  ? 0.3080 0.2886 0.2356 0.0816  0.0101  -0.0280 19  ASN   A CG    
131  O OD1   . ASN   A 20  ? 0.3304 0.2782 0.2373 0.0770  0.0022  -0.0295 19  ASN   A OD1   
132  N ND2   . ASN   A 20  ? 0.2795 0.2859 0.2305 0.0730  0.0109  -0.0245 19  ASN   A ND2   
133  N N     . ILE   A 21  ? 0.3948 0.3032 0.2541 0.0946  0.0043  -0.0415 20  ILE   A N     
134  C CA    . ILE   A 21  ? 0.4097 0.3010 0.2580 0.0821  -0.0032 -0.0440 20  ILE   A CA    
135  C C     . ILE   A 21  ? 0.3950 0.2915 0.2596 0.0610  -0.0113 -0.0400 20  ILE   A C     
136  O O     . ILE   A 21  ? 0.3896 0.2856 0.2552 0.0492  -0.0164 -0.0404 20  ILE   A O     
137  C CB    . ILE   A 21  ? 0.4637 0.3102 0.2735 0.0896  -0.0102 -0.0505 20  ILE   A CB    
138  C CG1   . ILE   A 21  ? 0.4974 0.3105 0.2910 0.0890  -0.0189 -0.0502 20  ILE   A CG1   
139  C CG2   . ILE   A 21  ? 0.4810 0.3269 0.2740 0.1121  -0.0009 -0.0551 20  ILE   A CG2   
140  C CD1   . ILE   A 21  ? 0.5425 0.3073 0.3006 0.0856  -0.0310 -0.0560 20  ILE   A CD1   
141  N N     . VAL   A 22  ? 0.3868 0.2900 0.2638 0.0568  -0.0124 -0.0356 21  VAL   A N     
142  C CA    . VAL   A 22  ? 0.3657 0.2829 0.2619 0.0386  -0.0173 -0.0310 21  VAL   A CA    
143  C C     . VAL   A 22  ? 0.3305 0.2838 0.2531 0.0345  -0.0111 -0.0301 21  VAL   A C     
144  O O     . VAL   A 22  ? 0.3303 0.2904 0.2616 0.0217  -0.0157 -0.0289 21  VAL   A O     
145  C CB    . VAL   A 22  ? 0.3679 0.2855 0.2695 0.0364  -0.0190 -0.0259 21  VAL   A CB    
146  C CG1   . VAL   A 22  ? 0.3407 0.2778 0.2625 0.0189  -0.0225 -0.0208 21  VAL   A CG1   
147  C CG2   . VAL   A 22  ? 0.4194 0.2946 0.2915 0.0403  -0.0265 -0.0262 21  VAL   A CG2   
148  N N     . LEU   A 23  ? 0.3168 0.2917 0.2508 0.0452  -0.0014 -0.0305 22  LEU   A N     
149  C CA    . LEU   A 23  ? 0.2899 0.2929 0.2446 0.0423  0.0043  -0.0299 22  LEU   A CA    
150  C C     . LEU   A 23  ? 0.2884 0.2895 0.2326 0.0519  0.0098  -0.0320 22  LEU   A C     
151  O O     . LEU   A 23  ? 0.2625 0.2856 0.2196 0.0566  0.0178  -0.0306 22  LEU   A O     
152  C CB    . LEU   A 23  ? 0.2694 0.3003 0.2466 0.0438  0.0101  -0.0275 22  LEU   A CB    
153  C CG    . LEU   A 23  ? 0.2755 0.3102 0.2609 0.0368  0.0060  -0.0250 22  LEU   A CG    
154  C CD1   . LEU   A 23  ? 0.2560 0.3193 0.2622 0.0387  0.0116  -0.0239 22  LEU   A CD1   
155  C CD2   . LEU   A 23  ? 0.2716 0.3060 0.2625 0.0224  -0.0005 -0.0238 22  LEU   A CD2   
156  N N     . GLN   A 24  ? 0.3152 0.2906 0.2358 0.0528  0.0049  -0.0350 23  GLN   A N     
157  C CA    . GLN   A 24  ? 0.3309 0.3003 0.2347 0.0645  0.0101  -0.0375 23  GLN   A CA    
158  C C     . GLN   A 24  ? 0.3171 0.3119 0.2372 0.0619  0.0165  -0.0345 23  GLN   A C     
159  O O     . GLN   A 24  ? 0.3108 0.3144 0.2453 0.0499  0.0128  -0.0325 23  GLN   A O     
160  C CB    . GLN   A 24  ? 0.3538 0.2900 0.2278 0.0642  0.0020  -0.0421 23  GLN   A CB    
161  C CG    . GLN   A 24  ? 0.3694 0.2935 0.2184 0.0813  0.0076  -0.0462 23  GLN   A CG    
162  C CD    . GLN   A 24  ? 0.4095 0.2925 0.2228 0.0847  -0.0013 -0.0528 23  GLN   A CD    
163  O OE1   . GLN   A 24  ? 0.4208 0.2817 0.2275 0.0736  -0.0126 -0.0537 23  GLN   A OE1   
164  N NE2   . GLN   A 24  ? 0.4336 0.3057 0.2223 0.1001  0.0035  -0.0573 23  GLN   A NE2   
165  N N     . GLY   A 25  ? 0.3124 0.3194 0.2303 0.0736  0.0262  -0.0335 24  GLY   A N     
166  C CA    . GLY   A 25  ? 0.3008 0.3284 0.2308 0.0704  0.0321  -0.0294 24  GLY   A CA    
167  C C     . GLY   A 25  ? 0.3100 0.3227 0.2250 0.0656  0.0270  -0.0302 24  GLY   A C     
168  O O     . GLY   A 25  ? 0.3285 0.3154 0.2190 0.0685  0.0208  -0.0349 24  GLY   A O     
169  N N     . VAL   A 26  ? 0.3067 0.3342 0.2353 0.0584  0.0288  -0.0256 25  VAL   A N     
170  C CA    . VAL   A 26  ? 0.3289 0.3460 0.2463 0.0535  0.0236  -0.0248 25  VAL   A CA    
171  C C     . VAL   A 26  ? 0.3217 0.3539 0.2418 0.0555  0.0319  -0.0187 25  VAL   A C     
172  O O     . VAL   A 26  ? 0.3101 0.3636 0.2502 0.0541  0.0391  -0.0141 25  VAL   A O     
173  C CB    . VAL   A 26  ? 0.3322 0.3499 0.2649 0.0406  0.0145  -0.0241 25  VAL   A CB    
174  C CG1   . VAL   A 26  ? 0.3481 0.3532 0.2784 0.0366  0.0064  -0.0283 25  VAL   A CG1   
175  C CG2   . VAL   A 26  ? 0.3228 0.3622 0.2838 0.0347  0.0180  -0.0200 25  VAL   A CG2   
176  N N     . LYS   A 27  ? 0.3436 0.3648 0.2440 0.0571  0.0299  -0.0181 26  LYS   A N     
177  C CA    . LYS   A 27  ? 0.3415 0.3740 0.2447 0.0550  0.0346  -0.0106 26  LYS   A CA    
178  C C     . LYS   A 27  ? 0.3590 0.3780 0.2532 0.0488  0.0247  -0.0101 26  LYS   A C     
179  O O     . LYS   A 27  ? 0.3650 0.3653 0.2400 0.0499  0.0164  -0.0159 26  LYS   A O     
180  C CB    . LYS   A 27  ? 0.3601 0.4005 0.2480 0.0654  0.0456  -0.0072 26  LYS   A CB    
181  C CG    . LYS   A 27  ? 0.4005 0.4219 0.2535 0.0759  0.0443  -0.0123 26  LYS   A CG    
182  C CD    . LYS   A 27  ? 0.4284 0.4364 0.2664 0.0870  0.0442  -0.0212 26  LYS   A CD    
183  C CE    . LYS   A 27  ? 0.4666 0.4506 0.2670 0.0964  0.0408  -0.0275 26  LYS   A CE    
184  N NZ    . LYS   A 27  ? 0.5076 0.4742 0.2876 0.1101  0.0414  -0.0363 26  LYS   A NZ    
185  N N     . LEU   A 28  ? 0.3673 0.3958 0.2749 0.0424  0.0252  -0.0027 27  LEU   A N     
186  C CA    . LEU   A 28  ? 0.3879 0.4082 0.2922 0.0370  0.0158  -0.0005 27  LEU   A CA    
187  C C     . LEU   A 28  ? 0.3898 0.4152 0.2904 0.0369  0.0207  0.0090  27  LEU   A C     
188  O O     . LEU   A 28  ? 0.3691 0.4076 0.2829 0.0354  0.0293  0.0150  27  LEU   A O     
189  C CB    . LEU   A 28  ? 0.3727 0.3976 0.3013 0.0292  0.0091  -0.0017 27  LEU   A CB    
190  C CG    . LEU   A 28  ? 0.3849 0.4058 0.3173 0.0274  0.0036  -0.0093 27  LEU   A CG    
191  C CD1   . LEU   A 28  ? 0.3805 0.4109 0.3375 0.0207  -0.0009 -0.0093 27  LEU   A CD1   
192  C CD2   . LEU   A 28  ? 0.4180 0.4222 0.3290 0.0271  -0.0059 -0.0140 27  LEU   A CD2   
193  N N     . ARG   A 29  ? 0.4216 0.4366 0.3032 0.0379  0.0146  0.0111  28  ARG   A N     
194  C CA    . ARG   A 29  ? 0.4527 0.4696 0.3290 0.0370  0.0169  0.0213  28  ARG   A CA    
195  C C     . ARG   A 29  ? 0.4316 0.4411 0.3106 0.0328  0.0045  0.0229  28  ARG   A C     
196  O O     . ARG   A 29  ? 0.4134 0.4136 0.2780 0.0338  -0.0049 0.0175  28  ARG   A O     
197  C CB    . ARG   A 29  ? 0.5192 0.5326 0.3653 0.0450  0.0223  0.0226  28  ARG   A CB    
198  C CG    . ARG   A 29  ? 0.6124 0.6278 0.4493 0.0441  0.0249  0.0346  28  ARG   A CG    
199  C CD    . ARG   A 29  ? 0.7129 0.7392 0.5353 0.0498  0.0386  0.0411  28  ARG   A CD    
200  N NE    . ARG   A 29  ? 0.8840 0.9047 0.6721 0.0602  0.0412  0.0379  28  ARG   A NE    
201  C CZ    . ARG   A 29  ? 1.0332 1.0462 0.7963 0.0625  0.0377  0.0427  28  ARG   A CZ    
202  N NH1   . ARG   A 29  ? 1.0032 1.0041 0.7644 0.0576  0.0246  0.0439  28  ARG   A NH1   
203  N NH2   . ARG   A 29  ? 1.1178 1.1367 0.8560 0.0714  0.0475  0.0456  28  ARG   A NH2   
204  N N     . ILE   A 30  ? 0.4125 0.4259 0.3099 0.0284  0.0038  0.0300  29  ILE   A N     
205  C CA    . ILE   A 30  ? 0.4221 0.4301 0.3215 0.0271  -0.0068 0.0337  29  ILE   A CA    
206  C C     . ILE   A 30  ? 0.4397 0.4433 0.3257 0.0282  -0.0042 0.0455  29  ILE   A C     
207  O O     . ILE   A 30  ? 0.4264 0.4334 0.3193 0.0255  0.0046  0.0527  29  ILE   A O     
208  C CB    . ILE   A 30  ? 0.4052 0.4178 0.3323 0.0237  -0.0098 0.0325  29  ILE   A CB    
209  C CG1   . ILE   A 30  ? 0.4036 0.4219 0.3423 0.0223  -0.0128 0.0219  29  ILE   A CG1   
210  C CG2   . ILE   A 30  ? 0.4214 0.4295 0.3521 0.0250  -0.0188 0.0382  29  ILE   A CG2   
211  C CD1   . ILE   A 30  ? 0.4055 0.4308 0.3570 0.0206  -0.0036 0.0182  29  ILE   A CD1   
212  N N     . VAL   A 31  ? 0.4474 0.4442 0.3145 0.0311  -0.0126 0.0478  30  VAL   A N     
213  C CA    . VAL   A 31  ? 0.4683 0.4596 0.3227 0.0323  -0.0132 0.0599  30  VAL   A CA    
214  C C     . VAL   A 31  ? 0.4696 0.4573 0.3300 0.0335  -0.0268 0.0614  30  VAL   A C     
215  O O     . VAL   A 31  ? 0.4670 0.4568 0.3256 0.0342  -0.0363 0.0536  30  VAL   A O     
216  C CB    . VAL   A 31  ? 0.5051 0.4935 0.3270 0.0368  -0.0109 0.0614  30  VAL   A CB    
217  C CG1   . VAL   A 31  ? 0.5480 0.5309 0.3534 0.0383  -0.0128 0.0747  30  VAL   A CG1   
218  C CG2   . VAL   A 31  ? 0.5138 0.5091 0.3295 0.0384  0.0032  0.0594  30  VAL   A CG2   
219  N N     . GLY   A 32  ? 0.4823 0.4642 0.3470 0.0339  -0.0281 0.0723  31  GLY   A N     
220  C CA    . GLY   A 32  ? 0.4836 0.4627 0.3517 0.0378  -0.0408 0.0754  31  GLY   A CA    
221  C C     . GLY   A 32  ? 0.5011 0.4688 0.3707 0.0394  -0.0411 0.0886  31  GLY   A C     
222  O O     . GLY   A 32  ? 0.4962 0.4578 0.3644 0.0352  -0.0316 0.0961  31  GLY   A O     
223  N N     . GLU   A 33  ? 0.5226 0.4880 0.3957 0.0454  -0.0527 0.0917  32  GLU   A N     
224  C CA    . GLU   A 33  ? 0.5488 0.4998 0.4210 0.0493  -0.0559 0.1041  32  GLU   A CA    
225  C C     . GLU   A 33  ? 0.5259 0.4778 0.4212 0.0555  -0.0632 0.0997  32  GLU   A C     
226  O O     . GLU   A 33  ? 0.5071 0.4732 0.4093 0.0601  -0.0720 0.0932  32  GLU   A O     
227  C CB    . GLU   A 33  ? 0.5989 0.5447 0.4456 0.0536  -0.0624 0.1151  32  GLU   A CB    
228  C CG    . GLU   A 33  ? 0.6497 0.6065 0.4919 0.0601  -0.0765 0.1116  32  GLU   A CG    
229  C CD    . GLU   A 33  ? 0.7264 0.6776 0.5433 0.0654  -0.0848 0.1236  32  GLU   A CD    
230  O OE1   . GLU   A 33  ? 0.7500 0.6871 0.5510 0.0643  -0.0789 0.1362  32  GLU   A OE1   
231  O OE2   . GLU   A 33  ? 0.7730 0.7352 0.5855 0.0699  -0.0975 0.1213  32  GLU   A OE2   
232  N N     . TRP   A 34  ? 0.5187 0.4561 0.4250 0.0550  -0.0594 0.1030  33  TRP   A N     
233  C CA    . TRP   A 34  ? 0.5086 0.4425 0.4342 0.0626  -0.0649 0.0989  33  TRP   A CA    
234  C C     . TRP   A 34  ? 0.5285 0.4420 0.4448 0.0712  -0.0722 0.1116  33  TRP   A C     
235  O O     . TRP   A 34  ? 0.5412 0.4332 0.4470 0.0662  -0.0679 0.1221  33  TRP   A O     
236  C CB    . TRP   A 34  ? 0.4938 0.4214 0.4339 0.0555  -0.0559 0.0930  33  TRP   A CB    
237  C CG    . TRP   A 34  ? 0.4965 0.4172 0.4543 0.0625  -0.0593 0.0870  33  TRP   A CG    
238  C CD1   . TRP   A 34  ? 0.5251 0.4206 0.4818 0.0678  -0.0628 0.0930  33  TRP   A CD1   
239  C CD2   . TRP   A 34  ? 0.4758 0.4133 0.4532 0.0646  -0.0586 0.0732  33  TRP   A CD2   
240  N NE1   . TRP   A 34  ? 0.5235 0.4185 0.4967 0.0745  -0.0645 0.0828  33  TRP   A NE1   
241  C CE2   . TRP   A 34  ? 0.4949 0.4176 0.4816 0.0726  -0.0615 0.0709  33  TRP   A CE2   
242  C CE3   . TRP   A 34  ? 0.4586 0.4207 0.4451 0.0607  -0.0560 0.0630  33  TRP   A CE3   
243  C CZ2   . TRP   A 34  ? 0.4773 0.4124 0.4819 0.0774  -0.0612 0.0585  33  TRP   A CZ2   
244  C CZ3   . TRP   A 34  ? 0.4279 0.4023 0.4331 0.0640  -0.0558 0.0522  33  TRP   A CZ3   
245  C CH2   . TRP   A 34  ? 0.4434 0.4059 0.4576 0.0725  -0.0580 0.0499  33  TRP   A CH2   
246  N N     . VAL   A 35  ? 0.5201 0.4412 0.4403 0.0838  -0.0833 0.1114  34  VAL   A N     
247  C CA    . VAL   A 35  ? 0.5547 0.4577 0.4656 0.0949  -0.0918 0.1235  34  VAL   A CA    
248  C C     . VAL   A 35  ? 0.5498 0.4489 0.4796 0.1076  -0.0964 0.1174  34  VAL   A C     
249  O O     . VAL   A 35  ? 0.5132 0.4376 0.4590 0.1135  -0.0999 0.1077  34  VAL   A O     
250  C CB    . VAL   A 35  ? 0.5691 0.4855 0.4661 0.1010  -0.1017 0.1299  34  VAL   A CB    
251  C CG1   . VAL   A 35  ? 0.6081 0.5051 0.4936 0.1134  -0.1107 0.1440  34  VAL   A CG1   
252  C CG2   . VAL   A 35  ? 0.5735 0.4957 0.4505 0.0896  -0.0968 0.1325  34  VAL   A CG2   
253  N N     . LEU   A 36  ? 0.5775 0.4448 0.5047 0.1110  -0.0960 0.1228  35  LEU   A N     
254  C CA    . LEU   A 36  ? 0.5914 0.4484 0.5294 0.1276  -0.1023 0.1192  35  LEU   A CA    
255  C C     . LEU   A 36  ? 0.6263 0.4678 0.5504 0.1422  -0.1130 0.1328  35  LEU   A C     
256  O O     . LEU   A 36  ? 0.6416 0.4590 0.5461 0.1364  -0.1129 0.1464  35  LEU   A O     
257  C CB    . LEU   A 36  ? 0.6047 0.4324 0.5469 0.1241  -0.0972 0.1149  35  LEU   A CB    
258  C CG    . LEU   A 36  ? 0.5790 0.4215 0.5372 0.1131  -0.0881 0.1004  35  LEU   A CG    
259  C CD1   . LEU   A 36  ? 0.5988 0.4082 0.5569 0.1085  -0.0851 0.0983  35  LEU   A CD1   
260  C CD2   . LEU   A 36  ? 0.5552 0.4292 0.5327 0.1240  -0.0901 0.0872  35  LEU   A CD2   
261  N N     . LYS   A 37  ? 0.6375 0.4938 0.5725 0.1614  -0.1216 0.1293  36  LYS   A N     
262  C CA    . LYS   A 37  ? 0.7049 0.5483 0.6303 0.1799  -0.1328 0.1406  36  LYS   A CA    
263  C C     . LYS   A 37  ? 0.7371 0.5625 0.6720 0.1988  -0.1359 0.1347  36  LYS   A C     
264  O O     . LYS   A 37  ? 0.7115 0.5535 0.6652 0.2012  -0.1316 0.1202  36  LYS   A O     
265  C CB    . LYS   A 37  ? 0.6953 0.5799 0.6266 0.1875  -0.1412 0.1414  36  LYS   A CB    
266  C CG    . LYS   A 37  ? 0.7003 0.5958 0.6151 0.1728  -0.1413 0.1488  36  LYS   A CG    
267  C CD    . LYS   A 37  ? 0.6988 0.6304 0.6167 0.1810  -0.1527 0.1507  36  LYS   A CD    
268  C CE    . LYS   A 37  ? 0.6917 0.6421 0.5976 0.1656  -0.1528 0.1513  36  LYS   A CE    
269  N NZ    . LYS   A 37  ? 0.7126 0.6471 0.5909 0.1654  -0.1580 0.1664  36  LYS   A NZ    
270  N N     . GLY   A 38  ? 0.7862 0.5776 0.7064 0.2131  -0.1437 0.1461  37  GLY   A N     
271  C CA    . GLY   A 38  ? 0.8390 0.6137 0.7646 0.2370  -0.1492 0.1415  37  GLY   A CA    
272  C C     . GLY   A 38  ? 0.8670 0.6847 0.8092 0.2588  -0.1567 0.1380  37  GLY   A C     
273  O O     . GLY   A 38  ? 0.8693 0.7282 0.8186 0.2529  -0.1585 0.1393  37  GLY   A O     
274  N N     . SER   A 39  ? 0.9558 0.7614 0.9019 0.2846  -0.1620 0.1346  38  SER   A N     
275  C CA    . SER   A 39  ? 1.0014 0.8442 0.9620 0.3103  -0.1702 0.1341  38  SER   A CA    
276  C C     . SER   A 39  ? 1.0199 0.8774 0.9715 0.3156  -0.1810 0.1503  38  SER   A C     
277  O O     . SER   A 39  ? 1.0215 0.9308 0.9893 0.3185  -0.1850 0.1492  38  SER   A O     
278  C CB    . SER   A 39  ? 1.0480 0.8648 1.0083 0.3387  -0.1736 0.1290  38  SER   A CB    
279  O OG    . SER   A 39  ? 1.0555 0.8693 1.0263 0.3342  -0.1640 0.1120  38  SER   A OG    
280  N N     . SER   A 40  ? 1.0729 0.8862 0.9986 0.3156  -0.1861 0.1655  39  SER   A N     
281  C CA    . SER   A 40  ? 1.0916 0.9151 1.0040 0.3161  -0.1954 0.1819  39  SER   A CA    
282  C C     . SER   A 40  ? 1.1069 0.9559 1.0164 0.2883  -0.1909 0.1831  39  SER   A C     
283  O O     . SER   A 40  ? 1.0765 0.9543 0.9830 0.2893  -0.1990 0.1909  39  SER   A O     
284  C CB    . SER   A 40  ? 1.1336 0.9013 1.0173 0.3223  -0.2013 0.1988  39  SER   A CB    
285  O OG    . SER   A 40  ? 1.1064 0.8348 0.9735 0.2976  -0.1925 0.2021  39  SER   A OG    
286  N N     . GLY   A 41  ? 1.1688 1.0034 1.0759 0.2645  -0.1787 0.1764  40  GLY   A N     
287  C CA    . GLY   A 41  ? 1.1670 1.0147 1.0658 0.2392  -0.1731 0.1783  40  GLY   A CA    
288  C C     . GLY   A 41  ? 1.2509 1.0655 1.1196 0.2308  -0.1747 0.1962  40  GLY   A C     
289  O O     . GLY   A 41  ? 1.3266 1.1553 1.1849 0.2140  -0.1717 0.1994  40  GLY   A O     
290  N N     . GLU   A 42  ? 1.2227 0.9920 1.0764 0.2417  -0.1786 0.2075  41  GLU   A N     
291  C CA    . GLU   A 42  ? 1.1904 0.9252 1.0149 0.2355  -0.1808 0.2270  41  GLU   A CA    
292  C C     . GLU   A 42  ? 1.1533 0.8510 0.9680 0.2141  -0.1693 0.2292  41  GLU   A C     
293  O O     . GLU   A 42  ? 1.1508 0.8298 0.9428 0.2022  -0.1677 0.2448  41  GLU   A O     
294  C CB    . GLU   A 42  ? 1.2589 0.9640 1.0715 0.2600  -0.1933 0.2401  41  GLU   A CB    
295  C CG    . GLU   A 42  ? 1.2741 1.0165 1.0958 0.2833  -0.2062 0.2411  41  GLU   A CG    
296  C CD    . GLU   A 42  ? 1.2782 1.0468 1.0859 0.2806  -0.2139 0.2532  41  GLU   A CD    
297  O OE1   . GLU   A 42  ? 1.2933 1.0466 1.0779 0.2630  -0.2101 0.2643  41  GLU   A OE1   
298  O OE2   . GLU   A 42  ? 1.2727 1.0799 1.0930 0.2966  -0.2242 0.2513  41  GLU   A OE2   
299  N N     . SER   A 43  ? 1.0893 0.7754 0.9195 0.2106  -0.1624 0.2153  42  SER   A N     
300  C CA    . SER   A 43  ? 1.0459 0.7148 0.8752 0.1866  -0.1502 0.2123  42  SER   A CA    
301  C C     . SER   A 43  ? 0.9607 0.6731 0.8084 0.1726  -0.1405 0.1966  42  SER   A C     
302  O O     . SER   A 43  ? 0.9096 0.6466 0.7788 0.1811  -0.1405 0.1807  42  SER   A O     
303  C CB    . SER   A 43  ? 1.0691 0.6984 0.9023 0.1901  -0.1498 0.2063  42  SER   A CB    
304  O OG    . SER   A 43  ? 1.0400 0.6890 0.8951 0.2065  -0.1514 0.1882  42  SER   A OG    
305  N N     . VAL   A 44  ? 0.9153 0.6357 0.7531 0.1519  -0.1321 0.2020  43  VAL   A N     
306  C CA    . VAL   A 44  ? 0.8529 0.6129 0.7011 0.1397  -0.1243 0.1906  43  VAL   A CA    
307  C C     . VAL   A 44  ? 0.8393 0.5878 0.6850 0.1174  -0.1114 0.1910  43  VAL   A C     
308  O O     . VAL   A 44  ? 0.8653 0.5881 0.6930 0.1083  -0.1090 0.2064  43  VAL   A O     
309  C CB    . VAL   A 44  ? 0.8379 0.6252 0.6735 0.1410  -0.1290 0.1967  43  VAL   A CB    
310  C CG1   . VAL   A 44  ? 0.7885 0.6124 0.6328 0.1294  -0.1222 0.1838  43  VAL   A CG1   
311  C CG2   . VAL   A 44  ? 0.8579 0.6569 0.6965 0.1629  -0.1432 0.1987  43  VAL   A CG2   
312  N N     . ARG   A 45  ? 0.7862 0.5544 0.6505 0.1090  -0.1033 0.1751  44  ARG   A N     
313  C CA    . ARG   A 45  ? 0.7797 0.5458 0.6456 0.0889  -0.0910 0.1737  44  ARG   A CA    
314  C C     . ARG   A 45  ? 0.7197 0.5245 0.5909 0.0819  -0.0845 0.1641  44  ARG   A C     
315  O O     . ARG   A 45  ? 0.6788 0.5057 0.5671 0.0877  -0.0859 0.1494  44  ARG   A O     
316  C CB    . ARG   A 45  ? 0.8053 0.5544 0.6875 0.0867  -0.0887 0.1632  44  ARG   A CB    
317  C CG    . ARG   A 45  ? 0.8737 0.5795 0.7456 0.0784  -0.0888 0.1749  44  ARG   A CG    
318  C CD    . ARG   A 45  ? 0.9083 0.6162 0.7774 0.0545  -0.0772 0.1810  44  ARG   A CD    
319  N NE    . ARG   A 45  ? 0.9271 0.6270 0.8100 0.0415  -0.0716 0.1724  44  ARG   A NE    
320  C CZ    . ARG   A 45  ? 0.9627 0.6793 0.8653 0.0434  -0.0693 0.1538  44  ARG   A CZ    
321  N NH1   . ARG   A 45  ? 0.9340 0.6769 0.8467 0.0579  -0.0718 0.1412  44  ARG   A NH1   
322  N NH2   . ARG   A 45  ? 0.9867 0.6944 0.8987 0.0298  -0.0648 0.1484  44  ARG   A NH2   
323  N N     . ARG   A 46  ? 0.7100 0.5217 0.5647 0.0709  -0.0780 0.1729  45  ARG   A N     
324  C CA    . ARG   A 46  ? 0.6791 0.5211 0.5337 0.0643  -0.0713 0.1644  45  ARG   A CA    
325  C C     . ARG   A 46  ? 0.6588 0.5024 0.5188 0.0484  -0.0578 0.1626  45  ARG   A C     
326  O O     . ARG   A 46  ? 0.6802 0.5074 0.5303 0.0390  -0.0526 0.1759  45  ARG   A O     
327  C CB    . ARG   A 46  ? 0.7109 0.5613 0.5409 0.0654  -0.0733 0.1743  45  ARG   A CB    
328  C CG    . ARG   A 46  ? 0.7442 0.5968 0.5674 0.0803  -0.0875 0.1775  45  ARG   A CG    
329  C CD    . ARG   A 46  ? 0.7780 0.6383 0.5740 0.0807  -0.0902 0.1869  45  ARG   A CD    
330  N NE    . ARG   A 46  ? 0.8230 0.6784 0.6101 0.0945  -0.1045 0.1956  45  ARG   A NE    
331  C CZ    . ARG   A 46  ? 0.8406 0.7149 0.6363 0.1055  -0.1164 0.1882  45  ARG   A CZ    
332  N NH1   . ARG   A 46  ? 0.8182 0.7177 0.6298 0.1029  -0.1161 0.1717  45  ARG   A NH1   
333  N NH2   . ARG   A 46  ? 0.8663 0.7354 0.6543 0.1187  -0.1290 0.1983  45  ARG   A NH2   
334  N N     . THR   A 47  ? 0.6114 0.4759 0.4876 0.0453  -0.0527 0.1470  46  THR   A N     
335  C CA    . THR   A 47  ? 0.5955 0.4679 0.4787 0.0321  -0.0405 0.1436  46  THR   A CA    
336  C C     . THR   A 47  ? 0.5686 0.4681 0.4480 0.0312  -0.0353 0.1346  46  THR   A C     
337  O O     . THR   A 47  ? 0.5338 0.4468 0.4220 0.0374  -0.0401 0.1221  46  THR   A O     
338  C CB    . THR   A 47  ? 0.5889 0.4550 0.4950 0.0305  -0.0405 0.1331  46  THR   A CB    
339  O OG1   . THR   A 47  ? 0.6267 0.4632 0.5321 0.0346  -0.0477 0.1402  46  THR   A OG1   
340  C CG2   . THR   A 47  ? 0.5828 0.4553 0.4976 0.0162  -0.0292 0.1314  46  THR   A CG2   
341  N N     . ASP   A 48  ? 0.5869 0.4939 0.4517 0.0240  -0.0257 0.1416  47  ASP   A N     
342  C CA    . ASP   A 48  ? 0.5856 0.5144 0.4460 0.0231  -0.0188 0.1323  47  ASP   A CA    
343  C C     . ASP   A 48  ? 0.5457 0.4845 0.4283 0.0173  -0.0119 0.1211  47  ASP   A C     
344  O O     . ASP   A 48  ? 0.5491 0.4810 0.4427 0.0092  -0.0071 0.1261  47  ASP   A O     
345  C CB    . ASP   A 48  ? 0.6187 0.5537 0.4560 0.0197  -0.0099 0.1429  47  ASP   A CB    
346  C CG    . ASP   A 48  ? 0.6783 0.6063 0.4896 0.0263  -0.0169 0.1527  47  ASP   A CG    
347  O OD1   . ASP   A 48  ? 0.7039 0.6331 0.5118 0.0345  -0.0279 0.1454  47  ASP   A OD1   
348  O OD2   . ASP   A 48  ? 0.7440 0.6669 0.5385 0.0226  -0.0118 0.1683  47  ASP   A OD2   
349  N N     . VAL   A 49  ? 0.5061 0.4593 0.3944 0.0211  -0.0129 0.1067  48  VAL   A N     
350  C CA    . VAL   A 49  ? 0.4726 0.4360 0.3814 0.0178  -0.0086 0.0946  48  VAL   A CA    
351  C C     . VAL   A 49  ? 0.4569 0.4358 0.3563 0.0177  -0.0007 0.0889  48  VAL   A C     
352  O O     . VAL   A 49  ? 0.4380 0.4197 0.3229 0.0233  -0.0053 0.0842  48  VAL   A O     
353  C CB    . VAL   A 49  ? 0.4452 0.4103 0.3691 0.0235  -0.0180 0.0831  48  VAL   A CB    
354  C CG1   . VAL   A 49  ? 0.4247 0.4024 0.3661 0.0208  -0.0138 0.0704  48  VAL   A CG1   
355  C CG2   . VAL   A 49  ? 0.4565 0.4058 0.3896 0.0263  -0.0250 0.0877  48  VAL   A CG2   
356  N N     . LYS   A 50  ? 0.4587 0.4470 0.3668 0.0116  0.0100  0.0889  49  LYS   A N     
357  C CA    . LYS   A 50  ? 0.4808 0.4844 0.3843 0.0134  0.0179  0.0817  49  LYS   A CA    
358  C C     . LYS   A 50  ? 0.4218 0.4342 0.3493 0.0094  0.0213  0.0733  49  LYS   A C     
359  O O     . LYS   A 50  ? 0.4049 0.4175 0.3463 0.0017  0.0250  0.0790  49  LYS   A O     
360  C CB    . LYS   A 50  ? 0.5826 0.5934 0.4693 0.0120  0.0284  0.0930  49  LYS   A CB    
361  C CG    . LYS   A 50  ? 0.6832 0.7106 0.5616 0.0166  0.0384  0.0871  49  LYS   A CG    
362  C CD    . LYS   A 50  ? 0.7790 0.8029 0.6308 0.0267  0.0353  0.0800  49  LYS   A CD    
363  C CE    . LYS   A 50  ? 0.8402 0.8776 0.6750 0.0329  0.0474  0.0799  49  LYS   A CE    
364  N NZ    . LYS   A 50  ? 0.8924 0.9212 0.6952 0.0421  0.0435  0.0757  49  LYS   A NZ    
365  N N     . VAL   A 51  ? 0.3851 0.4031 0.3161 0.0137  0.0190  0.0605  50  VAL   A N     
366  C CA    . VAL   A 51  ? 0.3621 0.3894 0.3131 0.0112  0.0218  0.0520  50  VAL   A CA    
367  C C     . VAL   A 51  ? 0.3665 0.4042 0.3083 0.0161  0.0280  0.0456  50  VAL   A C     
368  O O     . VAL   A 51  ? 0.3645 0.3966 0.2888 0.0221  0.0238  0.0407  50  VAL   A O     
369  C CB    . VAL   A 51  ? 0.3390 0.3621 0.3054 0.0117  0.0127  0.0434  50  VAL   A CB    
370  C CG1   . VAL   A 51  ? 0.3283 0.3619 0.3129 0.0093  0.0160  0.0352  50  VAL   A CG1   
371  C CG2   . VAL   A 51  ? 0.3525 0.3638 0.3268 0.0095  0.0071  0.0492  50  VAL   A CG2   
372  N N     . ASP   A 52  ? 0.3568 0.4089 0.3094 0.0139  0.0372  0.0458  51  ASP   A N     
373  C CA    . ASP   A 52  ? 0.3550 0.4172 0.3011 0.0205  0.0434  0.0394  51  ASP   A CA    
374  C C     . ASP   A 52  ? 0.3189 0.3898 0.2863 0.0182  0.0437  0.0324  51  ASP   A C     
375  O O     . ASP   A 52  ? 0.3087 0.3890 0.2941 0.0111  0.0470  0.0364  51  ASP   A O     
376  C CB    . ASP   A 52  ? 0.3942 0.4704 0.3304 0.0232  0.0552  0.0472  51  ASP   A CB    
377  C CG    . ASP   A 52  ? 0.4500 0.5178 0.3615 0.0264  0.0550  0.0540  51  ASP   A CG    
378  O OD1   . ASP   A 52  ? 0.4817 0.5380 0.3728 0.0340  0.0500  0.0473  51  ASP   A OD1   
379  O OD2   . ASP   A 52  ? 0.5502 0.6199 0.4633 0.0199  0.0577  0.0661  51  ASP   A OD2   
380  N N     . ILE   A 53  ? 0.2974 0.3639 0.2612 0.0234  0.0396  0.0223  52  ILE   A N     
381  C CA    . ILE   A 53  ? 0.2860 0.3597 0.2674 0.0220  0.0391  0.0156  52  ILE   A CA    
382  C C     . ILE   A 53  ? 0.2801 0.3583 0.2511 0.0308  0.0442  0.0106  52  ILE   A C     
383  O O     . ILE   A 53  ? 0.2974 0.3638 0.2466 0.0377  0.0422  0.0071  52  ILE   A O     
384  C CB    . ILE   A 53  ? 0.2676 0.3319 0.2570 0.0191  0.0288  0.0095  52  ILE   A CB    
385  C CG1   . ILE   A 53  ? 0.2704 0.3304 0.2700 0.0133  0.0244  0.0140  52  ILE   A CG1   
386  C CG2   . ILE   A 53  ? 0.2540 0.3263 0.2586 0.0182  0.0287  0.0030  52  ILE   A CG2   
387  C CD1   . ILE   A 53  ? 0.2676 0.3211 0.2727 0.0129  0.0146  0.0092  52  ILE   A CD1   
388  N N     . THR   A 54  ? 0.2614 0.3559 0.2470 0.0310  0.0501  0.0103  53  THR   A N     
389  C CA    . THR   A 54  ? 0.2516 0.3497 0.2326 0.0397  0.0529  0.0045  53  THR   A CA    
390  C C     . THR   A 54  ? 0.2224 0.3269 0.2239 0.0351  0.0496  0.0004  53  THR   A C     
391  O O     . THR   A 54  ? 0.2034 0.3204 0.2243 0.0272  0.0507  0.0037  53  THR   A O     
392  C CB    . THR   A 54  ? 0.2583 0.3759 0.2374 0.0465  0.0644  0.0095  53  THR   A CB    
393  O OG1   . THR   A 54  ? 0.2833 0.3929 0.2391 0.0525  0.0671  0.0120  53  THR   A OG1   
394  C CG2   . THR   A 54  ? 0.2636 0.3867 0.2399 0.0574  0.0676  0.0041  53  THR   A CG2   
395  N N     . SER   A 55  ? 0.2230 0.3180 0.2183 0.0398  0.0453  -0.0066 54  SER   A N     
396  C CA    . SER   A 55  ? 0.2094 0.3126 0.2196 0.0387  0.0441  -0.0100 54  SER   A CA    
397  C C     . SER   A 55  ? 0.2220 0.3189 0.2175 0.0501  0.0456  -0.0140 54  SER   A C     
398  O O     . SER   A 55  ? 0.2411 0.3168 0.2189 0.0527  0.0400  -0.0182 54  SER   A O     
399  C CB    . SER   A 55  ? 0.1982 0.2934 0.2169 0.0307  0.0355  -0.0133 54  SER   A CB    
400  O OG    . SER   A 55  ? 0.1808 0.2854 0.2136 0.0289  0.0345  -0.0159 54  SER   A OG    
401  N N     . THR   A 56  ? 0.2177 0.3320 0.2196 0.0570  0.0525  -0.0126 55  THR   A N     
402  C CA    . THR   A 56  ? 0.2398 0.3471 0.2266 0.0706  0.0542  -0.0161 55  THR   A CA    
403  C C     . THR   A 56  ? 0.2427 0.3383 0.2313 0.0686  0.0468  -0.0204 55  THR   A C     
404  O O     . THR   A 56  ? 0.2281 0.3220 0.2283 0.0570  0.0407  -0.0211 55  THR   A O     
405  C CB    . THR   A 56  ? 0.2359 0.3695 0.2298 0.0802  0.0643  -0.0120 55  THR   A CB    
406  O OG1   . THR   A 56  ? 0.2198 0.3745 0.2392 0.0722  0.0638  -0.0098 55  THR   A OG1   
407  C CG2   . THR   A 56  ? 0.2475 0.3917 0.2358 0.0821  0.0721  -0.0067 55  THR   A CG2   
408  N N     . ALA   A 57  ? 0.2624 0.3460 0.2355 0.0807  0.0467  -0.0235 56  ALA   A N     
409  C CA    . ALA   A 57  ? 0.2730 0.3398 0.2421 0.0790  0.0391  -0.0265 56  ALA   A CA    
410  C C     . ALA   A 57  ? 0.2547 0.3433 0.2492 0.0712  0.0386  -0.0243 56  ALA   A C     
411  O O     . ALA   A 57  ? 0.2183 0.3330 0.2289 0.0734  0.0447  -0.0213 56  ALA   A O     
412  C CB    . ALA   A 57  ? 0.3018 0.3501 0.2494 0.0943  0.0391  -0.0294 56  ALA   A CB    
413  N N     . GLY   A 58  ? 0.2605 0.3395 0.2585 0.0609  0.0310  -0.0255 57  GLY   A N     
414  C CA    . GLY   A 58  ? 0.2569 0.3541 0.2761 0.0528  0.0297  -0.0244 57  GLY   A CA    
415  C C     . GLY   A 58  ? 0.2492 0.3669 0.2879 0.0449  0.0325  -0.0231 57  GLY   A C     
416  O O     . GLY   A 58  ? 0.2560 0.3910 0.3111 0.0409  0.0326  -0.0228 57  GLY   A O     
417  N N     . ASN   A 59  ? 0.2261 0.3399 0.2613 0.0426  0.0341  -0.0222 58  ASN   A N     
418  C CA    . ASN   A 59  ? 0.2140 0.3423 0.2642 0.0356  0.0366  -0.0199 58  ASN   A CA    
419  C C     . ASN   A 59  ? 0.1967 0.3495 0.2614 0.0368  0.0426  -0.0168 58  ASN   A C     
420  O O     . ASN   A 59  ? 0.1763 0.3416 0.2573 0.0283  0.0420  -0.0161 58  ASN   A O     
421  C CB    . ASN   A 59  ? 0.1942 0.3232 0.2567 0.0257  0.0311  -0.0219 58  ASN   A CB    
422  C CG    . ASN   A 59  ? 0.1971 0.3093 0.2502 0.0232  0.0248  -0.0240 58  ASN   A CG    
423  O OD1   . ASN   A 59  ? 0.1961 0.3084 0.2524 0.0206  0.0207  -0.0259 58  ASN   A OD1   
424  N ND2   . ASN   A 59  ? 0.1949 0.2950 0.2368 0.0235  0.0238  -0.0229 58  ASN   A ND2   
425  N N     . GLN   A 60  ? 0.2146 0.3743 0.2731 0.0475  0.0477  -0.0153 59  GLN   A N     
426  C CA    . GLN   A 60  ? 0.2297 0.4173 0.3033 0.0489  0.0530  -0.0116 59  GLN   A CA    
427  C C     . GLN   A 60  ? 0.2250 0.4256 0.3071 0.0419  0.0577  -0.0062 59  GLN   A C     
428  O O     . GLN   A 60  ? 0.2281 0.4463 0.3284 0.0326  0.0573  -0.0041 59  GLN   A O     
429  C CB    . GLN   A 60  ? 0.2570 0.4508 0.3217 0.0645  0.0577  -0.0107 59  GLN   A CB    
430  C CG    . GLN   A 60  ? 0.2823 0.5102 0.3657 0.0661  0.0622  -0.0064 59  GLN   A CG    
431  C CD    . GLN   A 60  ? 0.3351 0.5746 0.4102 0.0833  0.0696  -0.0038 59  GLN   A CD    
432  O OE1   . GLN   A 60  ? 0.4463 0.6695 0.5053 0.0966  0.0683  -0.0071 59  GLN   A OE1   
433  N NE2   . GLN   A 60  ? 0.3760 0.6420 0.4605 0.0836  0.0773  0.0022  59  GLN   A NE2   
434  N N     . ASP   A 61  ? 0.2471 0.4386 0.3147 0.0463  0.0617  -0.0039 60  ASP   A N     
435  C CA    . ASP   A 61  ? 0.2715 0.4741 0.3439 0.0401  0.0668  0.0029  60  ASP   A CA    
436  C C     . ASP   A 61  ? 0.2393 0.4185 0.3013 0.0339  0.0627  0.0025  60  ASP   A C     
437  O O     . ASP   A 61  ? 0.2391 0.3980 0.2820 0.0406  0.0605  -0.0010 60  ASP   A O     
438  C CB    . ASP   A 61  ? 0.3295 0.5468 0.3930 0.0518  0.0765  0.0076  60  ASP   A CB    
439  C CG    . ASP   A 61  ? 0.3864 0.6382 0.4665 0.0554  0.0824  0.0120  60  ASP   A CG    
440  O OD1   . ASP   A 61  ? 0.4042 0.6733 0.5055 0.0424  0.0805  0.0152  60  ASP   A OD1   
441  O OD2   . ASP   A 61  ? 0.5470 0.8085 0.6180 0.0716  0.0886  0.0122  60  ASP   A OD2   
442  N N     . ASN   A 62  ? 0.2146 0.3955 0.2889 0.0211  0.0606  0.0060  61  ASN   A N     
443  C CA    . ASN   A 62  ? 0.2043 0.3635 0.2728 0.0151  0.0548  0.0053  61  ASN   A CA    
444  C C     . ASN   A 62  ? 0.2053 0.3684 0.2754 0.0079  0.0585  0.0142  61  ASN   A C     
445  O O     . ASN   A 62  ? 0.1904 0.3719 0.2751 0.0006  0.0619  0.0195  61  ASN   A O     
446  C CB    . ASN   A 62  ? 0.1831 0.3348 0.2625 0.0085  0.0468  -0.0005 61  ASN   A CB    
447  C CG    . ASN   A 62  ? 0.1775 0.3302 0.2567 0.0143  0.0443  -0.0071 61  ASN   A CG    
448  O OD1   . ASN   A 62  ? 0.1758 0.3449 0.2661 0.0144  0.0459  -0.0078 61  ASN   A OD1   
449  N ND2   . ASN   A 62  ? 0.1721 0.3087 0.2377 0.0194  0.0407  -0.0108 61  ASN   A ND2   
450  N N     . SER   A 63  ? 0.2232 0.3703 0.2777 0.0096  0.0576  0.0166  62  SER   A N     
451  C CA    . SER   A 63  ? 0.2415 0.3882 0.2934 0.0034  0.0606  0.0261  62  SER   A CA    
452  C C     . SER   A 63  ? 0.2483 0.3704 0.2900 0.0020  0.0532  0.0254  62  SER   A C     
453  O O     . SER   A 63  ? 0.2554 0.3655 0.2830 0.0095  0.0497  0.0201  62  SER   A O     
454  C CB    . SER   A 63  ? 0.2563 0.4160 0.2958 0.0109  0.0701  0.0319  62  SER   A CB    
455  O OG    . SER   A 63  ? 0.2767 0.4360 0.3119 0.0044  0.0732  0.0425  62  SER   A OG    
456  N N     . PHE   A 64  ? 0.2539 0.3681 0.3024 -0.0076 0.0500  0.0308  63  PHE   A N     
457  C CA    . PHE   A 64  ? 0.2676 0.3604 0.3074 -0.0081 0.0432  0.0321  63  PHE   A CA    
458  C C     . PHE   A 64  ? 0.2864 0.3765 0.3226 -0.0152 0.0462  0.0446  63  PHE   A C     
459  O O     . PHE   A 64  ? 0.2976 0.3915 0.3469 -0.0254 0.0470  0.0493  63  PHE   A O     
460  C CB    . PHE   A 64  ? 0.2618 0.3441 0.3136 -0.0108 0.0347  0.0250  63  PHE   A CB    
461  C CG    . PHE   A 64  ? 0.2731 0.3356 0.3185 -0.0092 0.0270  0.0258  63  PHE   A CG    
462  C CD1   . PHE   A 64  ? 0.3025 0.3520 0.3469 -0.0148 0.0251  0.0340  63  PHE   A CD1   
463  C CD2   . PHE   A 64  ? 0.2846 0.3419 0.3251 -0.0022 0.0211  0.0191  63  PHE   A CD2   
464  C CE1   . PHE   A 64  ? 0.3130 0.3446 0.3512 -0.0111 0.0177  0.0350  63  PHE   A CE1   
465  C CE2   . PHE   A 64  ? 0.2860 0.3294 0.3221 0.0005  0.0138  0.0204  63  PHE   A CE2   
466  C CZ    . PHE   A 64  ? 0.3052 0.3358 0.3398 -0.0028 0.0122  0.0281  63  PHE   A CZ    
467  N N     . ALA   A 65  ? 0.3072 0.3904 0.3248 -0.0107 0.0475  0.0503  64  ALA   A N     
468  C CA    . ALA   A 65  ? 0.3387 0.4189 0.3493 -0.0168 0.0508  0.0638  64  ALA   A CA    
469  C C     . ALA   A 65  ? 0.3623 0.4195 0.3605 -0.0141 0.0425  0.0655  64  ALA   A C     
470  O O     . ALA   A 65  ? 0.3802 0.4325 0.3659 -0.0049 0.0390  0.0593  64  ALA   A O     
471  C CB    . ALA   A 65  ? 0.3487 0.4455 0.3458 -0.0122 0.0611  0.0703  64  ALA   A CB    
472  N N     . ILE   A 66  ? 0.3867 0.4291 0.3882 -0.0218 0.0385  0.0735  65  ILE   A N     
473  C CA    . ILE   A 66  ? 0.4012 0.4216 0.3913 -0.0182 0.0302  0.0769  65  ILE   A CA    
474  C C     . ILE   A 66  ? 0.4157 0.4285 0.3958 -0.0253 0.0331  0.0933  65  ILE   A C     
475  O O     . ILE   A 66  ? 0.4156 0.4281 0.4059 -0.0368 0.0356  0.1003  65  ILE   A O     
476  C CB    . ILE   A 66  ? 0.3894 0.3946 0.3917 -0.0172 0.0205  0.0688  65  ILE   A CB    
477  C CG1   . ILE   A 66  ? 0.4018 0.3870 0.3934 -0.0110 0.0117  0.0723  65  ILE   A CG1   
478  C CG2   . ILE   A 66  ? 0.3979 0.3984 0.4161 -0.0279 0.0204  0.0697  65  ILE   A CG2   
479  C CD1   . ILE   A 66  ? 0.3968 0.3728 0.3987 -0.0050 0.0028  0.0625  65  ILE   A CD1   
480  N N     . GLN   A 67  ? 0.4364 0.4439 0.3961 -0.0195 0.0325  0.0998  66  GLN   A N     
481  C CA    . GLN   A 67  ? 0.4800 0.4773 0.4270 -0.0250 0.0338  0.1164  66  GLN   A CA    
482  C C     . GLN   A 67  ? 0.4796 0.4527 0.4162 -0.0184 0.0224  0.1181  66  GLN   A C     
483  O O     . GLN   A 67  ? 0.4597 0.4339 0.3868 -0.0078 0.0176  0.1108  66  GLN   A O     
484  C CB    . GLN   A 67  ? 0.5175 0.5320 0.4461 -0.0223 0.0436  0.1240  66  GLN   A CB    
485  C CG    . GLN   A 67  ? 0.5586 0.6009 0.4964 -0.0265 0.0559  0.1242  66  GLN   A CG    
486  C CD    . GLN   A 67  ? 0.6470 0.7060 0.5636 -0.0178 0.0649  0.1268  66  GLN   A CD    
487  O OE1   . GLN   A 67  ? 0.7230 0.7830 0.6284 -0.0057 0.0633  0.1149  66  GLN   A OE1   
488  N NE2   . GLN   A 67  ? 0.6807 0.7505 0.5892 -0.0239 0.0737  0.1428  66  GLN   A NE2   
489  N N     . LEU   A 68  ? 0.5086 0.4598 0.4476 -0.0247 0.0172  0.1272  67  LEU   A N     
490  C CA    . LEU   A 68  ? 0.5408 0.4676 0.4705 -0.0177 0.0064  0.1309  67  LEU   A CA    
491  C C     . LEU   A 68  ? 0.5802 0.4940 0.4929 -0.0237 0.0079  0.1505  67  LEU   A C     
492  O O     . LEU   A 68  ? 0.6023 0.5134 0.5198 -0.0373 0.0131  0.1606  67  LEU   A O     
493  C CB    . LEU   A 68  ? 0.5444 0.4521 0.4899 -0.0176 -0.0018 0.1239  67  LEU   A CB    
494  C CG    . LEU   A 68  ? 0.5283 0.4491 0.4911 -0.0125 -0.0031 0.1056  67  LEU   A CG    
495  C CD1   . LEU   A 68  ? 0.5456 0.4472 0.5216 -0.0130 -0.0098 0.0996  67  LEU   A CD1   
496  C CD2   . LEU   A 68  ? 0.5174 0.4479 0.4748 0.0005  -0.0079 0.0974  67  LEU   A CD2   
497  N N     . ALA   A 69  ? 0.6024 0.5088 0.4957 -0.0146 0.0026  0.1565  68  ALA   A N     
498  C CA    . ALA   A 69  ? 0.6380 0.5315 0.5118 -0.0185 0.0032  0.1760  68  ALA   A CA    
499  C C     . ALA   A 69  ? 0.6598 0.5292 0.5235 -0.0076 -0.0101 0.1793  68  ALA   A C     
500  O O     . ALA   A 69  ? 0.6148 0.4921 0.4740 0.0048  -0.0160 0.1702  68  ALA   A O     
501  C CB    . ALA   A 69  ? 0.6372 0.5533 0.4923 -0.0167 0.0122  0.1809  68  ALA   A CB    
502  N N     . ASN   A 70  ? 0.7078 0.5480 0.5684 -0.0121 -0.0152 0.1921  69  ASN   A N     
503  C CA    . ASN   A 70  ? 0.7600 0.5785 0.6019 -0.0033 -0.0248 0.2039  69  ASN   A CA    
504  C C     . ASN   A 70  ? 0.7820 0.6058 0.6013 -0.0105 -0.0175 0.2229  69  ASN   A C     
505  O O     . ASN   A 70  ? 0.8498 0.6671 0.6490 -0.0014 -0.0236 0.2312  69  ASN   A O     
506  C CB    . ASN   A 70  ? 0.7995 0.5799 0.6439 -0.0028 -0.0345 0.2102  69  ASN   A CB    
507  C CG    . ASN   A 70  ? 0.7889 0.5612 0.6562 -0.0034 -0.0372 0.1950  69  ASN   A CG    
508  O OD1   . ASN   A 70  ? 0.7975 0.5534 0.6713 -0.0171 -0.0349 0.1993  69  ASN   A OD1   
509  N ND2   . ASN   A 70  ? 0.7744 0.5591 0.6535 0.0100  -0.0419 0.1777  69  ASN   A ND2   
510  N N     . THR   A 78  ? 0.9235 0.6759 0.7959 -0.0725 -0.0149 0.2369  77  THR   A N     
511  C CA    . THR   A 78  ? 0.9346 0.7235 0.7972 -0.0715 -0.0036 0.2434  77  THR   A CA    
512  C C     . THR   A 78  ? 0.9095 0.7369 0.7876 -0.0661 0.0039  0.2242  77  THR   A C     
513  O O     . THR   A 78  ? 0.8971 0.7363 0.7704 -0.0498 0.0018  0.2132  77  THR   A O     
514  C CB    . THR   A 78  ? 0.9849 0.7790 0.8399 -0.0915 0.0054  0.2663  77  THR   A CB    
515  O OG1   . THR   A 78  ? 1.0267 0.8085 0.8979 -0.1107 0.0048  0.2685  77  THR   A OG1   
516  C CG2   . THR   A 78  ? 1.0236 0.7906 0.8535 -0.0914 0.0005  0.2877  77  THR   A CG2   
517  N N     . LYS   A 79  ? 0.8774 0.7228 0.7740 -0.0800 0.0115  0.2207  78  LYS   A N     
518  C CA    . LYS   A 79  ? 0.8317 0.7153 0.7412 -0.0767 0.0205  0.2065  78  LYS   A CA    
519  C C     . LYS   A 79  ? 0.7662 0.6509 0.7002 -0.0847 0.0189  0.1938  78  LYS   A C     
520  O O     . LYS   A 79  ? 0.7750 0.6424 0.7165 -0.1003 0.0161  0.2009  78  LYS   A O     
521  C CB    . LYS   A 79  ? 0.8653 0.7842 0.7710 -0.0846 0.0352  0.2172  78  LYS   A CB    
522  C CG    . LYS   A 79  ? 0.9213 0.8478 0.8012 -0.0764 0.0396  0.2282  78  LYS   A CG    
523  C CD    . LYS   A 79  ? 0.9429 0.9060 0.8180 -0.0828 0.0555  0.2390  78  LYS   A CD    
524  C CE    . LYS   A 79  ? 0.9635 0.9311 0.8438 -0.1045 0.0621  0.2603  78  LYS   A CE    
525  N NZ    . LYS   A 79  ? 0.9788 0.9136 0.8442 -0.1132 0.0555  0.2798  78  LYS   A NZ    
526  N N     . TRP   A 80  ? 0.7076 0.6128 0.6524 -0.0744 0.0205  0.1754  79  TRP   A N     
527  C CA    . TRP   A 80  ? 0.6972 0.6050 0.6631 -0.0769 0.0179  0.1601  79  TRP   A CA    
528  C C     . TRP   A 80  ? 0.6406 0.5842 0.6136 -0.0689 0.0259  0.1476  79  TRP   A C     
529  O O     . TRP   A 80  ? 0.6000 0.5490 0.5629 -0.0543 0.0250  0.1411  79  TRP   A O     
530  C CB    . TRP   A 80  ? 0.7257 0.6036 0.6924 -0.0658 0.0052  0.1487  79  TRP   A CB    
531  C CG    . TRP   A 80  ? 0.7552 0.6264 0.7397 -0.0701 0.0009  0.1356  79  TRP   A CG    
532  C CD1   . TRP   A 80  ? 0.8222 0.6642 0.8094 -0.0815 -0.0056 0.1392  79  TRP   A CD1   
533  C CD2   . TRP   A 80  ? 0.7349 0.6259 0.7346 -0.0640 0.0019  0.1174  79  TRP   A CD2   
534  N NE1   . TRP   A 80  ? 0.8130 0.6561 0.8153 -0.0826 -0.0087 0.1239  79  TRP   A NE1   
535  C CE2   . TRP   A 80  ? 0.7528 0.6267 0.7635 -0.0720 -0.0038 0.1109  79  TRP   A CE2   
536  C CE3   . TRP   A 80  ? 0.6928 0.6121 0.6965 -0.0534 0.0066  0.1063  79  TRP   A CE3   
537  C CZ2   . TRP   A 80  ? 0.7178 0.6047 0.7431 -0.0689 -0.0044 0.0943  79  TRP   A CZ2   
538  C CZ3   . TRP   A 80  ? 0.6793 0.6105 0.6983 -0.0513 0.0062  0.0911  79  TRP   A CZ3   
539  C CH2   . TRP   A 80  ? 0.6653 0.5819 0.6950 -0.0586 0.0011  0.0853  79  TRP   A CH2   
540  N N     . CSD   A 81  ? 0.5926 0.5602 0.5815 -0.0787 0.0331  0.1456  80  CSD   A N     
541  C CA    . CSD   A 81  ? 0.5614 0.5600 0.5567 -0.0704 0.0401  0.1339  80  CSD   A CA    
542  C CB    . CSD   A 81  ? 0.6035 0.6298 0.5889 -0.0701 0.0525  0.1442  80  CSD   A CB    
543  S SG    . CSD   A 81  ? 0.6560 0.7153 0.6587 -0.0875 0.0638  0.1550  80  CSD   A SG    
544  C C     . CSD   A 81  ? 0.5116 0.5195 0.5291 -0.0769 0.0391  0.1232  80  CSD   A C     
545  O O     . CSD   A 81  ? 0.4934 0.4915 0.5211 -0.0918 0.0360  0.1283  80  CSD   A O     
546  O OD1   . CSD   A 81  ? 0.5778 0.6600 0.5983 -0.0836 0.0662  0.1405  80  CSD   A OD1   
547  O OD2   . CSD   A 81  ? 0.7240 0.8083 0.7112 -0.0845 0.0765  0.1685  80  CSD   A OD2   
548  N N     . ALA   A 82  ? 0.4586 0.4828 0.4817 -0.0658 0.0405  0.1084  81  ALA   A N     
549  C CA    . ALA   A 82  ? 0.4255 0.4618 0.4676 -0.0691 0.0399  0.0973  81  ALA   A CA    
550  C C     . ALA   A 82  ? 0.3976 0.4639 0.4415 -0.0597 0.0479  0.0905  81  ALA   A C     
551  O O     . ALA   A 82  ? 0.3856 0.4505 0.4159 -0.0468 0.0483  0.0861  81  ALA   A O     
552  C CB    . ALA   A 82  ? 0.4252 0.4390 0.4720 -0.0640 0.0292  0.0843  81  ALA   A CB    
553  N N     . LEU   A 83  ? 0.3617 0.4533 0.4209 -0.0665 0.0535  0.0903  82  LEU   A N     
554  C CA    . LEU   A 83  ? 0.3416 0.4587 0.4052 -0.0570 0.0594  0.0820  82  LEU   A CA    
555  C C     . LEU   A 83  ? 0.3122 0.4330 0.3940 -0.0606 0.0544  0.0712  82  LEU   A C     
556  O O     . LEU   A 83  ? 0.3095 0.4372 0.4053 -0.0745 0.0535  0.0757  82  LEU   A O     
557  C CB    . LEU   A 83  ? 0.3567 0.5059 0.4221 -0.0598 0.0715  0.0930  82  LEU   A CB    
558  C CG    . LEU   A 83  ? 0.3415 0.5180 0.4103 -0.0479 0.0784  0.0855  82  LEU   A CG    
559  C CD1   . LEU   A 83  ? 0.3423 0.5058 0.3934 -0.0304 0.0767  0.0745  82  LEU   A CD1   
560  C CD2   . LEU   A 83  ? 0.3626 0.5712 0.4317 -0.0485 0.0907  0.0972  82  LEU   A CD2   
561  N N     . LEU   A 84  ? 0.2873 0.4050 0.3680 -0.0490 0.0510  0.0578  83  LEU   A N     
562  C CA    . LEU   A 84  ? 0.2692 0.3920 0.3644 -0.0501 0.0467  0.0471  83  LEU   A CA    
563  C C     . LEU   A 84  ? 0.2353 0.3809 0.3314 -0.0395 0.0525  0.0415  83  LEU   A C     
564  O O     . LEU   A 84  ? 0.2292 0.3701 0.3114 -0.0280 0.0540  0.0387  83  LEU   A O     
565  C CB    . LEU   A 84  ? 0.2677 0.3656 0.3607 -0.0459 0.0371  0.0371  83  LEU   A CB    
566  C CG    . LEU   A 84  ? 0.2898 0.3595 0.3747 -0.0486 0.0309  0.0413  83  LEU   A CG    
567  C CD1   . LEU   A 84  ? 0.2818 0.3356 0.3659 -0.0403 0.0230  0.0299  83  LEU   A CD1   
568  C CD2   . LEU   A 84  ? 0.3116 0.3715 0.4030 -0.0636 0.0283  0.0485  83  LEU   A CD2   
569  N N     . THR   A 85  ? 0.2244 0.3934 0.3355 -0.0433 0.0550  0.0405  84  THR   A N     
570  C CA    . THR   A 85  ? 0.2042 0.3937 0.3162 -0.0322 0.0599  0.0357  84  THR   A CA    
571  C C     . THR   A 85  ? 0.1913 0.3877 0.3174 -0.0343 0.0547  0.0270  84  THR   A C     
572  O O     . THR   A 85  ? 0.1776 0.3754 0.3162 -0.0468 0.0505  0.0279  84  THR   A O     
573  C CB    . THR   A 85  ? 0.2015 0.4210 0.3167 -0.0313 0.0703  0.0453  84  THR   A CB    
574  O OG1   . THR   A 85  ? 0.1939 0.4307 0.3282 -0.0466 0.0697  0.0514  84  THR   A OG1   
575  C CG2   . THR   A 85  ? 0.2173 0.4328 0.3161 -0.0276 0.0765  0.0537  84  THR   A CG2   
576  N N     . LYS   A 86  ? 0.2010 0.4006 0.3234 -0.0224 0.0548  0.0192  85  LYS   A N     
577  C CA    . LYS   A 86  ? 0.2003 0.4071 0.3334 -0.0226 0.0502  0.0114  85  LYS   A CA    
578  C C     . LYS   A 86  ? 0.2016 0.4241 0.3317 -0.0097 0.0548  0.0093  85  LYS   A C     
579  O O     . LYS   A 86  ? 0.2117 0.4211 0.3265 0.0013  0.0556  0.0061  85  LYS   A O     
580  C CB    . LYS   A 86  ? 0.2044 0.3876 0.3338 -0.0228 0.0421  0.0028  85  LYS   A CB    
581  C CG    . LYS   A 86  ? 0.2053 0.3949 0.3439 -0.0236 0.0372  -0.0052 85  LYS   A CG    
582  C CD    . LYS   A 86  ? 0.2127 0.3833 0.3482 -0.0227 0.0302  -0.0136 85  LYS   A CD    
583  C CE    . LYS   A 86  ? 0.2279 0.3813 0.3646 -0.0304 0.0251  -0.0146 85  LYS   A CE    
584  N NZ    . LYS   A 86  ? 0.2464 0.4049 0.3934 -0.0426 0.0230  -0.0125 85  LYS   A NZ    
585  N N     . LYS   A 87  ? 0.2031 0.4523 0.3469 -0.0112 0.0569  0.0114  86  LYS   A N     
586  C CA    . LYS   A 87  ? 0.2255 0.4933 0.3680 0.0020  0.0620  0.0114  86  LYS   A CA    
587  C C     . LYS   A 87  ? 0.1947 0.4706 0.3467 0.0022  0.0564  0.0054  86  LYS   A C     
588  O O     . LYS   A 87  ? 0.1612 0.4510 0.3287 -0.0092 0.0528  0.0061  86  LYS   A O     
589  C CB    . LYS   A 87  ? 0.2606 0.5598 0.4115 0.0025  0.0706  0.0212  86  LYS   A CB    
590  C CG    . LYS   A 87  ? 0.3172 0.6085 0.4563 0.0025  0.0765  0.0277  86  LYS   A CG    
591  C CD    . LYS   A 87  ? 0.3405 0.6590 0.4785 0.0101  0.0877  0.0368  86  LYS   A CD    
592  C CE    . LYS   A 87  ? 0.3851 0.6919 0.5116 0.0053  0.0916  0.0436  86  LYS   A CE    
593  N NZ    . LYS   A 87  ? 0.4354 0.7558 0.5483 0.0202  0.1023  0.0481  86  LYS   A NZ    
594  N N     . TYR   A 88  ? 0.1773 0.4426 0.3183 0.0142  0.0551  0.0000  87  TYR   A N     
595  C CA    . TYR   A 88  ? 0.1671 0.4376 0.3134 0.0159  0.0500  -0.0051 87  TYR   A CA    
596  C C     . TYR   A 88  ? 0.1658 0.4589 0.3140 0.0286  0.0546  -0.0018 87  TYR   A C     
597  O O     . TYR   A 88  ? 0.1503 0.4474 0.2909 0.0382  0.0615  0.0021  87  TYR   A O     
598  C CB    . TYR   A 88  ? 0.1579 0.4006 0.2905 0.0194  0.0453  -0.0115 87  TYR   A CB    
599  C CG    . TYR   A 88  ? 0.1618 0.3881 0.2960 0.0085  0.0397  -0.0156 87  TYR   A CG    
600  C CD1   . TYR   A 88  ? 0.1608 0.3922 0.3052 0.0009  0.0342  -0.0200 87  TYR   A CD1   
601  C CD2   . TYR   A 88  ? 0.1712 0.3772 0.2959 0.0072  0.0396  -0.0154 87  TYR   A CD2   
602  C CE1   . TYR   A 88  ? 0.1621 0.3779 0.3063 -0.0060 0.0294  -0.0245 87  TYR   A CE1   
603  C CE2   . TYR   A 88  ? 0.1652 0.3570 0.2912 0.0001  0.0345  -0.0191 87  TYR   A CE2   
604  C CZ    . TYR   A 88  ? 0.1602 0.3564 0.2958 -0.0058 0.0296  -0.0240 87  TYR   A CZ    
605  O OH    . TYR   A 88  ? 0.1383 0.3210 0.2743 -0.0104 0.0249  -0.0284 87  TYR   A OH    
606  N N     . PRO   A 89  ? 0.1679 0.4743 0.3233 0.0311  0.0508  -0.0038 88  PRO   A N     
607  C CA    . PRO   A 89  ? 0.1836 0.5093 0.3390 0.0459  0.0546  -0.0006 88  PRO   A CA    
608  C C     . PRO   A 89  ? 0.2152 0.5157 0.3485 0.0618  0.0558  -0.0032 88  PRO   A C     
609  O O     . PRO   A 89  ? 0.1739 0.4449 0.2946 0.0592  0.0515  -0.0079 88  PRO   A O     
610  C CB    . PRO   A 89  ? 0.1860 0.5315 0.3554 0.0415  0.0486  -0.0017 88  PRO   A CB    
611  C CG    . PRO   A 89  ? 0.1669 0.4906 0.3338 0.0297  0.0414  -0.0084 88  PRO   A CG    
612  C CD    . PRO   A 89  ? 0.1594 0.4644 0.3224 0.0209  0.0429  -0.0089 88  PRO   A CD    
613  N N     . GLU   A 90  ? 0.2386 0.5518 0.3673 0.0784  0.0613  0.0001  89  GLU   A N     
614  C CA    . GLU   A 90  ? 0.2794 0.5676 0.3855 0.0953  0.0617  -0.0024 89  GLU   A CA    
615  C C     . GLU   A 90  ? 0.2518 0.5290 0.3551 0.0959  0.0540  -0.0051 89  GLU   A C     
616  O O     . GLU   A 90  ? 0.2201 0.5210 0.3390 0.0925  0.0512  -0.0034 89  GLU   A O     
617  C CB    . GLU   A 90  ? 0.3377 0.6444 0.4401 0.1143  0.0698  0.0016  89  GLU   A CB    
618  C CG    . GLU   A 90  ? 0.3921 0.7034 0.4908 0.1147  0.0779  0.0041  89  GLU   A CG    
619  C CD    . GLU   A 90  ? 0.4829 0.8011 0.5680 0.1369  0.0867  0.0060  89  GLU   A CD    
620  O OE1   . GLU   A 90  ? 0.5406 0.8352 0.6050 0.1541  0.0853  0.0019  89  GLU   A OE1   
621  O OE2   . GLU   A 90  ? 0.5372 0.8836 0.6312 0.1374  0.0951  0.0116  89  GLU   A OE2   
622  N N     . ARG   A 91  ? 0.2572 0.4991 0.3407 0.0984  0.0500  -0.0087 90  ARG   A N     
623  C CA    . ARG   A 91  ? 0.2472 0.4768 0.3265 0.0967  0.0429  -0.0099 90  ARG   A CA    
624  C C     . ARG   A 91  ? 0.2791 0.5115 0.3512 0.1141  0.0426  -0.0071 90  ARG   A C     
625  O O     . ARG   A 91  ? 0.2873 0.5307 0.3571 0.1291  0.0481  -0.0049 90  ARG   A O     
626  C CB    . ARG   A 91  ? 0.2308 0.4243 0.2933 0.0903  0.0385  -0.0134 90  ARG   A CB    
627  C CG    . ARG   A 91  ? 0.2433 0.4047 0.2804 0.1016  0.0387  -0.0145 90  ARG   A CG    
628  C CD    . ARG   A 91  ? 0.2521 0.3803 0.2733 0.0954  0.0315  -0.0161 90  ARG   A CD    
629  N NE    . ARG   A 91  ? 0.2476 0.3797 0.2737 0.0914  0.0265  -0.0137 90  ARG   A NE    
630  C CZ    . ARG   A 91  ? 0.2283 0.3566 0.2582 0.0779  0.0216  -0.0137 90  ARG   A CZ    
631  N NH1   . ARG   A 91  ? 0.2273 0.3473 0.2580 0.0663  0.0203  -0.0163 90  ARG   A NH1   
632  N NH2   . ARG   A 91  ? 0.2282 0.3604 0.2594 0.0769  0.0180  -0.0107 90  ARG   A NH2   
633  N N     . LYS   A 92  ? 0.2988 0.5243 0.3685 0.1122  0.0363  -0.0064 91  LYS   A N     
634  C CA    . LYS   A 92  ? 0.3174 0.5348 0.3751 0.1277  0.0338  -0.0032 91  LYS   A CA    
635  C C     . LYS   A 92  ? 0.3163 0.4980 0.3565 0.1216  0.0272  -0.0038 91  LYS   A C     
636  O O     . LYS   A 92  ? 0.2819 0.4550 0.3244 0.1053  0.0249  -0.0064 91  LYS   A O     
637  C CB    . LYS   A 92  ? 0.3469 0.6007 0.4225 0.1307  0.0325  0.0006  91  LYS   A CB    
638  C CG    . LYS   A 92  ? 0.3718 0.6657 0.4691 0.1308  0.0382  0.0019  91  LYS   A CG    
639  C CD    . LYS   A 92  ? 0.4251 0.7551 0.5353 0.1430  0.0385  0.0071  91  LYS   A CD    
640  C CE    . LYS   A 92  ? 0.4453 0.7908 0.5654 0.1351  0.0312  0.0082  91  LYS   A CE    
641  N NZ    . LYS   A 92  ? 0.4725 0.8613 0.6105 0.1434  0.0315  0.0132  91  LYS   A NZ    
642  N N     . PRO   A 93  ? 0.3198 0.4785 0.3412 0.1341  0.0238  -0.0007 92  PRO   A N     
643  C CA    . PRO   A 93  ? 0.3196 0.4437 0.3238 0.1264  0.0171  0.0005  92  PRO   A CA    
644  C C     . PRO   A 93  ? 0.2889 0.4242 0.3043 0.1089  0.0131  0.0018  92  PRO   A C     
645  O O     . PRO   A 93  ? 0.2922 0.4069 0.3003 0.0964  0.0101  0.0010  92  PRO   A O     
646  C CB    . PRO   A 93  ? 0.3496 0.4520 0.3341 0.1437  0.0139  0.0049  92  PRO   A CB    
647  C CG    . PRO   A 93  ? 0.3566 0.4723 0.3415 0.1642  0.0205  0.0034  92  PRO   A CG    
648  C CD    . PRO   A 93  ? 0.3304 0.4915 0.3437 0.1571  0.0261  0.0020  92  PRO   A CD    
649  N N     . ASP   A 94  ? 0.2597 0.4284 0.2924 0.1079  0.0131  0.0034  93  ASP   A N     
650  C CA    . ASP   A 94  ? 0.2442 0.4251 0.2856 0.0936  0.0097  0.0038  93  ASP   A CA    
651  C C     . ASP   A 94  ? 0.2146 0.4172 0.2749 0.0806  0.0122  -0.0022 93  ASP   A C     
652  O O     . ASP   A 94  ? 0.1988 0.4307 0.2757 0.0805  0.0138  -0.0039 93  ASP   A O     
653  C CB    . ASP   A 94  ? 0.2678 0.4668 0.3118 0.0997  0.0064  0.0089  93  ASP   A CB    
654  C CG    . ASP   A 94  ? 0.2614 0.4679 0.3075 0.0870  0.0027  0.0102  93  ASP   A CG    
655  O OD1   . ASP   A 94  ? 0.2627 0.4602 0.3085 0.0739  0.0028  0.0075  93  ASP   A OD1   
656  O OD2   . ASP   A 94  ? 0.2590 0.4822 0.3069 0.0907  -0.0003 0.0139  93  ASP   A OD2   
657  N N     . VAL   A 95  ? 0.2039 0.3920 0.2618 0.0687  0.0118  -0.0051 94  VAL   A N     
658  C CA    . VAL   A 95  ? 0.1880 0.3917 0.2611 0.0571  0.0132  -0.0106 94  VAL   A CA    
659  C C     . VAL   A 95  ? 0.1820 0.4097 0.2661 0.0510  0.0109  -0.0122 94  VAL   A C     
660  O O     . VAL   A 95  ? 0.1571 0.4018 0.2550 0.0454  0.0118  -0.0171 94  VAL   A O     
661  C CB    . VAL   A 95  ? 0.1980 0.3818 0.2652 0.0478  0.0128  -0.0126 94  VAL   A CB    
662  C CG1   . VAL   A 95  ? 0.2072 0.3845 0.2679 0.0408  0.0090  -0.0096 94  VAL   A CG1   
663  C CG2   . VAL   A 95  ? 0.1865 0.3804 0.2668 0.0400  0.0149  -0.0183 94  VAL   A CG2   
664  N N     . LEU   A 96  ? 0.1996 0.4270 0.2761 0.0522  0.0075  -0.0079 95  LEU   A N     
665  C CA    . LEU   A 96  ? 0.2020 0.4515 0.2854 0.0475  0.0050  -0.0096 95  LEU   A CA    
666  C C     . LEU   A 96  ? 0.2031 0.4783 0.2972 0.0527  0.0038  -0.0103 95  LEU   A C     
667  O O     . LEU   A 96  ? 0.2459 0.5395 0.3469 0.0470  0.0013  -0.0143 95  LEU   A O     
668  C CB    . LEU   A 96  ? 0.2152 0.4582 0.2860 0.0469  0.0021  -0.0035 95  LEU   A CB    
669  C CG    . LEU   A 96  ? 0.2200 0.4431 0.2819 0.0390  0.0025  -0.0013 95  LEU   A CG    
670  C CD1   . LEU   A 96  ? 0.2197 0.4443 0.2718 0.0362  -0.0001 0.0057  95  LEU   A CD1   
671  C CD2   . LEU   A 96  ? 0.2055 0.4340 0.2773 0.0298  0.0046  -0.0088 95  LEU   A CD2   
672  N N     . ALA   A 97  ? 0.2056 0.4833 0.3007 0.0634  0.0052  -0.0068 96  ALA   A N     
673  C CA    . ALA   A 97  ? 0.2068 0.5134 0.3131 0.0690  0.0034  -0.0055 96  ALA   A CA    
674  C C     . ALA   A 97  ? 0.2017 0.5248 0.3247 0.0642  0.0062  -0.0098 96  ALA   A C     
675  O O     . ALA   A 97  ? 0.2076 0.5189 0.3296 0.0667  0.0110  -0.0097 96  ALA   A O     
676  C CB    . ALA   A 97  ? 0.2157 0.5191 0.3136 0.0855  0.0034  0.0020  96  ALA   A CB    
677  N N     . PHE   A 98  ? 0.1927 0.5431 0.3297 0.0578  0.0028  -0.0126 97  PHE   A N     
678  C CA    . PHE   A 98  ? 0.1931 0.5618 0.3469 0.0512  0.0042  -0.0149 97  PHE   A CA    
679  C C     . PHE   A 98  ? 0.1972 0.5800 0.3567 0.0635  0.0085  -0.0083 97  PHE   A C     
680  O O     . PHE   A 98  ? 0.2090 0.5974 0.3632 0.0771  0.0076  -0.0030 97  PHE   A O     
681  C CB    . PHE   A 98  ? 0.1980 0.5926 0.3637 0.0414  -0.0025 -0.0187 97  PHE   A CB    
682  C CG    . PHE   A 98  ? 0.2079 0.6151 0.3895 0.0288  -0.0027 -0.0220 97  PHE   A CG    
683  C CD1   . PHE   A 98  ? 0.2316 0.6178 0.4115 0.0186  -0.0010 -0.0277 97  PHE   A CD1   
684  C CD2   . PHE   A 98  ? 0.2228 0.6627 0.4211 0.0268  -0.0049 -0.0185 97  PHE   A CD2   
685  C CE1   . PHE   A 98  ? 0.2294 0.6228 0.4219 0.0066  -0.0015 -0.0295 97  PHE   A CE1   
686  C CE2   . PHE   A 98  ? 0.2245 0.6743 0.4370 0.0129  -0.0053 -0.0200 97  PHE   A CE2   
687  C CZ    . PHE   A 98  ? 0.2246 0.6488 0.4331 0.0026  -0.0038 -0.0255 97  PHE   A CZ    
688  N N     . GLY   A 99  ? 0.1899 0.5795 0.3598 0.0592  0.0131  -0.0084 98  GLY   A N     
689  C CA    . GLY   A 99  ? 0.1791 0.5915 0.3585 0.0691  0.0181  -0.0024 98  GLY   A CA    
690  C C     . GLY   A 99  ? 0.1848 0.5770 0.3542 0.0776  0.0261  -0.0009 98  GLY   A C     
691  O O     . GLY   A 99  ? 0.2139 0.6173 0.3827 0.0928  0.0307  0.0040  98  GLY   A O     
692  N N     . TRP   A 100 ? 0.1698 0.5334 0.3306 0.0690  0.0277  -0.0053 99  TRP   A N     
693  C CA    . TRP   A 100 ? 0.1629 0.5097 0.3151 0.0738  0.0345  -0.0045 99  TRP   A CA    
694  C C     . TRP   A 100 ? 0.1443 0.5175 0.3130 0.0684  0.0393  -0.0013 99  TRP   A C     
695  O O     . TRP   A 100 ? 0.1212 0.4980 0.3003 0.0520  0.0372  -0.0034 99  TRP   A O     
696  C CB    . TRP   A 100 ? 0.1590 0.4729 0.3002 0.0642  0.0333  -0.0096 99  TRP   A CB    
697  C CG    . TRP   A 100 ? 0.1781 0.4633 0.3008 0.0696  0.0304  -0.0110 99  TRP   A CG    
698  C CD1   . TRP   A 100 ? 0.1925 0.4752 0.3075 0.0783  0.0271  -0.0088 99  TRP   A CD1   
699  C CD2   . TRP   A 100 ? 0.2000 0.4546 0.3096 0.0650  0.0301  -0.0139 99  TRP   A CD2   
700  N NE1   . TRP   A 100 ? 0.2203 0.4715 0.3179 0.0784  0.0249  -0.0098 99  TRP   A NE1   
701  C CE2   . TRP   A 100 ? 0.2098 0.4448 0.3045 0.0702  0.0265  -0.0131 99  TRP   A CE2   
702  C CE3   . TRP   A 100 ? 0.2019 0.4446 0.3110 0.0570  0.0320  -0.0164 99  TRP   A CE3   
703  C CZ2   . TRP   A 100 ? 0.2274 0.4336 0.3083 0.0659  0.0246  -0.0146 99  TRP   A CZ2   
704  C CZ3   . TRP   A 100 ? 0.2215 0.4362 0.3165 0.0548  0.0301  -0.0184 99  TRP   A CZ3   
705  C CH2   . TRP   A 100 ? 0.2333 0.4314 0.3155 0.0581  0.0263  -0.0176 99  TRP   A CH2   
706  N N     . GLY   A 101 ? 0.1616 0.5531 0.3322 0.0823  0.0456  0.0040  100 GLY   A N     
707  C CA    . GLY   A 101 ? 0.1634 0.5866 0.3509 0.0777  0.0512  0.0093  100 GLY   A CA    
708  C C     . GLY   A 101 ? 0.1517 0.6061 0.3626 0.0606  0.0456  0.0107  100 GLY   A C     
709  O O     . GLY   A 101 ? 0.1593 0.6274 0.3757 0.0618  0.0393  0.0101  100 GLY   A O     
710  N N     . ASN   A 102 ? 0.1593 0.6184 0.3805 0.0433  0.0465  0.0119  101 ASN   A N     
711  C CA    . ASN   A 102 ? 0.1507 0.6319 0.3914 0.0236  0.0399  0.0124  101 ASN   A CA    
712  C C     . ASN   A 102 ? 0.1481 0.5994 0.3828 0.0086  0.0317  0.0037  101 ASN   A C     
713  O O     . ASN   A 102 ? 0.1440 0.6051 0.3909 -0.0087 0.0256  0.0026  101 ASN   A O     
714  C CB    . ASN   A 102 ? 0.1531 0.6591 0.4088 0.0140  0.0457  0.0205  101 ASN   A CB    
715  C CG    . ASN   A 102 ? 0.1521 0.6288 0.3982 0.0055  0.0494  0.0199  101 ASN   A CG    
716  O OD1   . ASN   A 102 ? 0.1445 0.5833 0.3721 0.0100  0.0488  0.0134  101 ASN   A OD1   
717  N ND2   . ASN   A 102 ? 0.1530 0.6482 0.4116 -0.0068 0.0530  0.0275  101 ASN   A ND2   
718  N N     . GLU   A 103 ? 0.1426 0.5579 0.3586 0.0147  0.0312  -0.0025 102 GLU   A N     
719  C CA    . GLU   A 103 ? 0.1279 0.5181 0.3372 0.0046  0.0243  -0.0109 102 GLU   A CA    
720  C C     . GLU   A 103 ? 0.1286 0.5098 0.3439 -0.0130 0.0223  -0.0125 102 GLU   A C     
721  O O     . GLU   A 103 ? 0.1268 0.5033 0.3449 -0.0246 0.0147  -0.0184 102 GLU   A O     
722  C CB    . GLU   A 103 ? 0.1245 0.5269 0.3360 0.0053  0.0168  -0.0144 102 GLU   A CB    
723  C CG    . GLU   A 103 ? 0.1209 0.5177 0.3199 0.0225  0.0180  -0.0135 102 GLU   A CG    
724  C CD    . GLU   A 103 ? 0.1301 0.4916 0.3110 0.0255  0.0182  -0.0182 102 GLU   A CD    
725  O OE1   . GLU   A 103 ? 0.1178 0.4592 0.2956 0.0164  0.0182  -0.0224 102 GLU   A OE1   
726  O OE2   . GLU   A 103 ? 0.1423 0.4970 0.3122 0.0373  0.0181  -0.0166 102 GLU   A OE2   
727  N N     . GLN   A 104 ? 0.1350 0.5133 0.3505 -0.0139 0.0290  -0.0068 103 GLN   A N     
728  C CA    . GLN   A 104 ? 0.1301 0.5030 0.3518 -0.0299 0.0283  -0.0048 103 GLN   A CA    
729  C C     . GLN   A 104 ? 0.1295 0.4745 0.3377 -0.0261 0.0336  -0.0041 103 GLN   A C     
730  O O     . GLN   A 104 ? 0.1306 0.4753 0.3303 -0.0126 0.0405  -0.0010 103 GLN   A O     
731  C CB    . GLN   A 104 ? 0.1294 0.5375 0.3680 -0.0355 0.0322  0.0053  103 GLN   A CB    
732  C CG    . GLN   A 104 ? 0.1365 0.5428 0.3840 -0.0561 0.0295  0.0090  103 GLN   A CG    
733  C CD    . GLN   A 104 ? 0.1293 0.5781 0.3975 -0.0651 0.0312  0.0193  103 GLN   A CD    
734  O OE1   . GLN   A 104 ? 0.1150 0.5899 0.3957 -0.0686 0.0255  0.0186  103 GLN   A OE1   
735  N NE2   . GLN   A 104 ? 0.1394 0.5968 0.4111 -0.0690 0.0390  0.0293  103 GLN   A NE2   
736  N N     . VAL   A 105 ? 0.1325 0.4548 0.3382 -0.0379 0.0299  -0.0067 104 VAL   A N     
737  C CA    . VAL   A 105 ? 0.1386 0.4365 0.3328 -0.0363 0.0338  -0.0048 104 VAL   A CA    
738  C C     . VAL   A 105 ? 0.1432 0.4475 0.3457 -0.0498 0.0357  0.0036  104 VAL   A C     
739  O O     . VAL   A 105 ? 0.1475 0.4531 0.3594 -0.0648 0.0292  0.0029  104 VAL   A O     
740  C CB    . VAL   A 105 ? 0.1300 0.3956 0.3132 -0.0364 0.0282  -0.0136 104 VAL   A CB    
741  C CG1   . VAL   A 105 ? 0.1292 0.3730 0.2999 -0.0316 0.0321  -0.0113 104 VAL   A CG1   
742  C CG2   . VAL   A 105 ? 0.1283 0.3932 0.3064 -0.0269 0.0256  -0.0208 104 VAL   A CG2   
743  N N     . ASP   A 106 ? 0.1505 0.4580 0.3480 -0.0447 0.0441  0.0115  105 ASP   A N     
744  C CA    . ASP   A 106 ? 0.1747 0.4879 0.3775 -0.0566 0.0474  0.0217  105 ASP   A CA    
745  C C     . ASP   A 106 ? 0.1798 0.4604 0.3674 -0.0566 0.0480  0.0223  105 ASP   A C     
746  O O     . ASP   A 106 ? 0.1886 0.4617 0.3628 -0.0437 0.0535  0.0227  105 ASP   A O     
747  C CB    . ASP   A 106 ? 0.1951 0.5427 0.4036 -0.0498 0.0576  0.0315  105 ASP   A CB    
748  C CG    . ASP   A 106 ? 0.2005 0.5872 0.4274 -0.0509 0.0573  0.0338  105 ASP   A CG    
749  O OD1   . ASP   A 106 ? 0.2139 0.6029 0.4517 -0.0638 0.0484  0.0302  105 ASP   A OD1   
750  O OD2   . ASP   A 106 ? 0.2244 0.6377 0.4529 -0.0368 0.0653  0.0381  105 ASP   A OD2   
751  N N     . SER   A 107 ? 0.1867 0.4487 0.3760 -0.0713 0.0421  0.0234  106 SER   A N     
752  C CA    . SER   A 107 ? 0.1883 0.4195 0.3640 -0.0717 0.0414  0.0250  106 SER   A CA    
753  C C     . SER   A 107 ? 0.2072 0.4400 0.3870 -0.0870 0.0431  0.0375  106 SER   A C     
754  O O     . SER   A 107 ? 0.2029 0.4493 0.3966 -0.1025 0.0400  0.0417  106 SER   A O     
755  C CB    . SER   A 107 ? 0.1858 0.3869 0.3557 -0.0719 0.0323  0.0144  106 SER   A CB    
756  O OG    . SER   A 107 ? 0.1666 0.3684 0.3325 -0.0588 0.0315  0.0046  106 SER   A OG    
757  N N     . LYS   A 108 ? 0.2224 0.4405 0.3890 -0.0830 0.0474  0.0437  107 LYS   A N     
758  C CA    . LYS   A 108 ? 0.2604 0.4738 0.4262 -0.0965 0.0491  0.0568  107 LYS   A CA    
759  C C     . LYS   A 108 ? 0.2761 0.4525 0.4244 -0.0923 0.0459  0.0564  107 LYS   A C     
760  O O     . LYS   A 108 ? 0.2530 0.4214 0.3888 -0.0766 0.0478  0.0507  107 LYS   A O     
761  C CB    . LYS   A 108 ? 0.2685 0.5158 0.4367 -0.0938 0.0612  0.0688  107 LYS   A CB    
762  C CG    . LYS   A 108 ? 0.3196 0.5741 0.4927 -0.1118 0.0639  0.0852  107 LYS   A CG    
763  C CD    . LYS   A 108 ? 0.3242 0.6179 0.5000 -0.1077 0.0772  0.0974  107 LYS   A CD    
764  C CE    . LYS   A 108 ? 0.3646 0.6649 0.5415 -0.1237 0.0815  0.1152  107 LYS   A CE    
765  N NZ    . LYS   A 108 ? 0.3705 0.7211 0.5593 -0.1242 0.0935  0.1272  107 LYS   A NZ    
766  N N     . ALA   A 109 ? 0.3059 0.4597 0.4530 -0.1065 0.0402  0.0625  108 ALA   A N     
767  C CA    . ALA   A 109 ? 0.3354 0.4554 0.4664 -0.1037 0.0370  0.0653  108 ALA   A CA    
768  C C     . ALA   A 109 ? 0.3787 0.4958 0.5083 -0.1193 0.0392  0.0823  108 ALA   A C     
769  O O     . ALA   A 109 ? 0.3898 0.5087 0.5306 -0.1371 0.0354  0.0871  108 ALA   A O     
770  C CB    . ALA   A 109 ? 0.3357 0.4220 0.4632 -0.1024 0.0258  0.0540  108 ALA   A CB    
771  N N     . SER   A 110 ? 0.4019 0.5147 0.5172 -0.1135 0.0448  0.0917  109 SER   A N     
772  C CA    . SER   A 110 ? 0.4465 0.5544 0.5569 -0.1269 0.0474  0.1093  109 SER   A CA    
773  C C     . SER   A 110 ? 0.4545 0.5254 0.5453 -0.1199 0.0425  0.1114  109 SER   A C     
774  O O     . SER   A 110 ? 0.4273 0.4968 0.5069 -0.1026 0.0443  0.1048  109 SER   A O     
775  C CB    . SER   A 110 ? 0.4622 0.6079 0.5731 -0.1251 0.0607  0.1206  109 SER   A CB    
776  O OG    . SER   A 110 ? 0.4825 0.6658 0.6126 -0.1297 0.0653  0.1195  109 SER   A OG    
777  N N     . VAL   A 111 ? 0.4823 0.5233 0.5689 -0.1333 0.0355  0.1201  110 VAL   A N     
778  C CA    . VAL   A 111 ? 0.5091 0.5148 0.5770 -0.1271 0.0303  0.1244  110 VAL   A CA    
779  C C     . VAL   A 111 ? 0.5488 0.5499 0.6103 -0.1430 0.0333  0.1458  110 VAL   A C     
780  O O     . VAL   A 111 ? 0.5422 0.5420 0.6137 -0.1630 0.0310  0.1535  110 VAL   A O     
781  C CB    . VAL   A 111 ? 0.5122 0.4779 0.5765 -0.1226 0.0173  0.1129  110 VAL   A CB    
782  C CG1   . VAL   A 111 ? 0.5360 0.4863 0.6107 -0.1397 0.0096  0.1111  110 VAL   A CG1   
783  C CG2   . VAL   A 111 ? 0.5490 0.4802 0.5948 -0.1156 0.0119  0.1194  110 VAL   A CG2   
784  N N     . THR   A 112 ? 0.5873 0.5886 0.6320 -0.1350 0.0386  0.1557  111 THR   A N     
785  C CA    . THR   A 112 ? 0.6353 0.6325 0.6704 -0.1480 0.0423  0.1774  111 THR   A CA    
786  C C     . THR   A 112 ? 0.6755 0.6331 0.6895 -0.1388 0.0346  0.1808  111 THR   A C     
787  O O     . THR   A 112 ? 0.6489 0.6061 0.6519 -0.1195 0.0346  0.1725  111 THR   A O     
788  C CB    . THR   A 112 ? 0.6292 0.6691 0.6622 -0.1462 0.0572  0.1879  111 THR   A CB    
789  O OG1   . THR   A 112 ? 0.6147 0.6902 0.6692 -0.1538 0.0628  0.1842  111 THR   A OG1   
790  C CG2   . THR   A 112 ? 0.6719 0.7116 0.6950 -0.1608 0.0621  0.2119  111 THR   A CG2   
791  N N     . ILE   A 113 ? 0.7187 0.6424 0.7275 -0.1531 0.0270  0.1927  112 ILE   A N     
792  C CA    . ILE   A 113 ? 0.7742 0.6583 0.7625 -0.1469 0.0193  0.2001  112 ILE   A CA    
793  C C     . ILE   A 113 ? 0.7940 0.6843 0.7704 -0.1594 0.0264  0.2249  112 ILE   A C     
794  O O     . ILE   A 113 ? 0.7779 0.6910 0.7651 -0.1787 0.0333  0.2366  112 ILE   A O     
795  C CB    . ILE   A 113 ? 0.8233 0.6609 0.8125 -0.1518 0.0049  0.1944  112 ILE   A CB    
796  C CG1   . ILE   A 113 ? 0.7940 0.6330 0.7961 -0.1395 -0.0002 0.1694  112 ILE   A CG1   
797  C CG2   . ILE   A 113 ? 0.8662 0.6606 0.8339 -0.1436 -0.0038 0.2028  112 ILE   A CG2   
798  C CD1   . ILE   A 113 ? 0.7794 0.6322 0.8012 -0.1555 -0.0002 0.1629  112 ILE   A CD1   
799  N N     . GLY   A 114 ? 0.8134 0.6878 0.7680 -0.1478 0.0251  0.2329  113 GLY   A N     
800  C CA    . GLY   A 114 ? 0.8407 0.7227 0.7801 -0.1562 0.0325  0.2562  113 GLY   A CA    
801  C C     . GLY   A 114 ? 0.8234 0.7569 0.7638 -0.1513 0.0481  0.2575  113 GLY   A C     
802  O O     . GLY   A 114 ? 0.8549 0.8010 0.7815 -0.1567 0.0562  0.2767  113 GLY   A O     
803  N N     . SER   B 1   ? 1.1742 1.0155 0.8017 -0.3183 0.0915  0.3251  1   SER   B N     
804  C CA    . SER   B 1   ? 1.0970 0.9744 0.7872 -0.2944 0.0836  0.3108  1   SER   B CA    
805  C C     . SER   B 1   ? 1.0462 0.9329 0.8007 -0.2762 0.0990  0.3064  1   SER   B C     
806  O O     . SER   B 1   ? 1.0310 0.9035 0.7842 -0.2829 0.1242  0.2983  1   SER   B O     
807  C CB    . SER   B 1   ? 1.0801 0.9736 0.7621 -0.2941 0.0970  0.2743  1   SER   B CB    
808  O OG    . SER   B 1   ? 1.0995 0.9816 0.7242 -0.3089 0.0799  0.2782  1   SER   B OG    
809  N N     . VAL   B 2   ? 1.0145 0.9217 0.8222 -0.2551 0.0845  0.3126  2   VAL   B N     
810  C CA    . VAL   B 2   ? 0.9617 0.8828 0.8260 -0.2376 0.1015  0.2924  2   VAL   B CA    
811  C C     . VAL   B 2   ? 0.8933 0.8461 0.7853 -0.2230 0.0899  0.2754  2   VAL   B C     
812  O O     . VAL   B 2   ? 0.8688 0.8322 0.7719 -0.2145 0.0654  0.2941  2   VAL   B O     
813  C CB    . VAL   B 2   ? 0.9842 0.8889 0.8861 -0.2253 0.1054  0.3139  2   VAL   B CB    
814  C CG1   . VAL   B 2   ? 1.0308 0.9034 0.9084 -0.2404 0.1251  0.3208  2   VAL   B CG1   
815  C CG2   . VAL   B 2   ? 0.9980 0.9042 0.9178 -0.2132 0.0782  0.3525  2   VAL   B CG2   
816  N N     . THR   B 3   ? 0.8279 0.7971 0.7330 -0.2212 0.1080  0.2411  3   THR   B N     
817  C CA    . THR   B 3   ? 0.7952 0.7888 0.6988 -0.2174 0.1032  0.2191  3   THR   B CA    
818  C C     . THR   B 3   ? 0.7410 0.7547 0.6921 -0.2043 0.1162  0.1945  3   THR   B C     
819  O O     . THR   B 3   ? 0.7568 0.7681 0.7152 -0.2112 0.1371  0.1805  3   THR   B O     
820  C CB    . THR   B 3   ? 0.8400 0.8262 0.6930 -0.2350 0.1142  0.2066  3   THR   B CB    
821  O OG1   . THR   B 3   ? 0.8075 0.8167 0.6698 -0.2288 0.1206  0.1794  3   THR   B OG1   
822  C CG2   . THR   B 3   ? 0.9000 0.8699 0.7370 -0.2493 0.1406  0.2013  3   THR   B CG2   
823  N N     . ILE   B 4   ? 0.6768 0.7065 0.6603 -0.1875 0.1032  0.1936  4   ILE   B N     
824  C CA    . ILE   B 4   ? 0.6343 0.6788 0.6562 -0.1769 0.1132  0.1720  4   ILE   B CA    
825  C C     . ILE   B 4   ? 0.5589 0.6299 0.5897 -0.1673 0.1030  0.1564  4   ILE   B C     
826  O O     . ILE   B 4   ? 0.5520 0.6270 0.5732 -0.1633 0.0847  0.1685  4   ILE   B O     
827  C CB    . ILE   B 4   ? 0.6578 0.6860 0.7102 -0.1661 0.1160  0.1845  4   ILE   B CB    
828  C CG1   . ILE   B 4   ? 0.6570 0.6840 0.7232 -0.1522 0.0971  0.2115  4   ILE   B CG1   
829  C CG2   . ILE   B 4   ? 0.7045 0.7042 0.7474 -0.1775 0.1323  0.1931  4   ILE   B CG2   
830  C CD1   . ILE   B 4   ? 0.6256 0.6573 0.7307 -0.1340 0.0996  0.2062  4   ILE   B CD1   
831  N N     . THR   B 5   ? 0.5157 0.6049 0.5643 -0.1658 0.1143  0.1307  5   THR   B N     
832  C CA    . THR   B 5   ? 0.4845 0.5990 0.5393 -0.1587 0.1093  0.1132  5   THR   B CA    
833  C C     . THR   B 5   ? 0.4486 0.5755 0.5382 -0.1486 0.1104  0.0996  5   THR   B C     
834  O O     . THR   B 5   ? 0.4466 0.5671 0.5488 -0.1544 0.1221  0.0936  5   THR   B O     
835  C CB    . THR   B 5   ? 0.4887 0.6141 0.5287 -0.1684 0.1237  0.0977  5   THR   B CB    
836  O OG1   . THR   B 5   ? 0.5302 0.6363 0.5288 -0.1776 0.1206  0.1114  5   THR   B OG1   
837  C CG2   . THR   B 5   ? 0.4615 0.6112 0.5099 -0.1599 0.1222  0.0805  5   THR   B CG2   
838  N N     . ILE   B 6   ? 0.4311 0.5725 0.5311 -0.1361 0.0984  0.0952  6   ILE   B N     
839  C CA    . ILE   B 6   ? 0.4104 0.5644 0.5357 -0.1276 0.0986  0.0803  6   ILE   B CA    
840  C C     . ILE   B 6   ? 0.3856 0.5647 0.5111 -0.1223 0.0930  0.0666  6   ILE   B C     
841  O O     . ILE   B 6   ? 0.3969 0.5768 0.5092 -0.1174 0.0826  0.0730  6   ILE   B O     
842  C CB    . ILE   B 6   ? 0.4266 0.5668 0.5668 -0.1154 0.0925  0.0924  6   ILE   B CB    
843  C CG1   . ILE   B 6   ? 0.4488 0.5602 0.5909 -0.1188 0.1020  0.1078  6   ILE   B CG1   
844  C CG2   . ILE   B 6   ? 0.4180 0.5670 0.5758 -0.1078 0.0933  0.0761  6   ILE   B CG2   
845  C CD1   . ILE   B 6   ? 0.4620 0.5572 0.6226 -0.1045 0.1003  0.1256  6   ILE   B CD1   
846  N N     . ASN   B 7   ? 0.3829 0.5818 0.5230 -0.1248 0.0997  0.0494  7   ASN   B N     
847  C CA    . ASN   B 7   ? 0.3429 0.5660 0.4924 -0.1164 0.0949  0.0373  7   ASN   B CA    
848  C C     . ASN   B 7   ? 0.3016 0.5276 0.4673 -0.1086 0.0872  0.0317  7   ASN   B C     
849  O O     . ASN   B 7   ? 0.2990 0.5133 0.4712 -0.1139 0.0910  0.0302  7   ASN   B O     
850  C CB    . ASN   B 7   ? 0.3610 0.6083 0.5237 -0.1228 0.1054  0.0259  7   ASN   B CB    
851  C CG    . ASN   B 7   ? 0.3987 0.6408 0.5434 -0.1301 0.1181  0.0299  7   ASN   B CG    
852  O OD1   . ASN   B 7   ? 0.4382 0.6773 0.5647 -0.1248 0.1190  0.0303  7   ASN   B OD1   
853  N ND2   . ASN   B 7   ? 0.4233 0.6590 0.5676 -0.1435 0.1294  0.0328  7   ASN   B ND2   
854  N N     . GLN   B 8   ? 0.2728 0.5108 0.4409 -0.0974 0.0783  0.0279  8   GLN   B N     
855  C CA    . GLN   B 8   ? 0.2463 0.4866 0.4253 -0.0898 0.0715  0.0225  8   GLN   B CA    
856  C C     . GLN   B 8   ? 0.2190 0.4837 0.4052 -0.0829 0.0664  0.0130  8   GLN   B C     
857  O O     . GLN   B 8   ? 0.2005 0.4694 0.3784 -0.0767 0.0647  0.0147  8   GLN   B O     
858  C CB    . GLN   B 8   ? 0.2486 0.4696 0.4236 -0.0813 0.0660  0.0354  8   GLN   B CB    
859  C CG    . GLN   B 8   ? 0.2291 0.4477 0.4130 -0.0718 0.0621  0.0317  8   GLN   B CG    
860  C CD    . GLN   B 8   ? 0.2376 0.4452 0.4250 -0.0619 0.0568  0.0473  8   GLN   B CD    
861  O OE1   . GLN   B 8   ? 0.2588 0.4534 0.4476 -0.0627 0.0581  0.0633  8   GLN   B OE1   
862  N NE2   . GLN   B 8   ? 0.2201 0.4349 0.4117 -0.0527 0.0501  0.0451  8   GLN   B NE2   
863  N N     . LYS   B 9   ? 0.2136 0.4893 0.4118 -0.0843 0.0634  0.0041  9   LYS   B N     
864  C CA    . LYS   B 9   ? 0.1970 0.4950 0.4051 -0.0768 0.0562  -0.0023 9   LYS   B CA    
865  C C     . LYS   B 9   ? 0.1952 0.4807 0.3984 -0.0715 0.0490  -0.0042 9   LYS   B C     
866  O O     . LYS   B 9   ? 0.1988 0.4692 0.3979 -0.0800 0.0516  -0.0070 9   LYS   B O     
867  C CB    . LYS   B 9   ? 0.1981 0.5228 0.4251 -0.0870 0.0578  -0.0077 9   LYS   B CB    
868  C CG    . LYS   B 9   ? 0.1961 0.5473 0.4389 -0.0818 0.0481  -0.0112 9   LYS   B CG    
869  C CD    . LYS   B 9   ? 0.1964 0.5842 0.4681 -0.0894 0.0490  -0.0108 9   LYS   B CD    
870  C CE    . LYS   B 9   ? 0.2216 0.6133 0.4972 -0.1101 0.0438  -0.0138 9   LYS   B CE    
871  N NZ    . LYS   B 9   ? 0.2251 0.6537 0.5326 -0.1210 0.0458  -0.0102 9   LYS   B NZ    
872  N N     . GLY   B 10  ? 0.1893 0.4772 0.3901 -0.0588 0.0425  -0.0031 10  GLY   B N     
873  C CA    . GLY   B 10  ? 0.1883 0.4677 0.3852 -0.0530 0.0370  -0.0053 10  GLY   B CA    
874  C C     . GLY   B 10  ? 0.1759 0.4777 0.3795 -0.0501 0.0289  -0.0111 10  GLY   B C     
875  O O     . GLY   B 10  ? 0.1668 0.4848 0.3774 -0.0422 0.0276  -0.0098 10  GLY   B O     
876  N N     . GLU   B 11  ? 0.1755 0.4745 0.3742 -0.0565 0.0242  -0.0166 11  GLU   B N     
877  C CA    . GLU   B 11  ? 0.1761 0.4955 0.3796 -0.0555 0.0132  -0.0191 11  GLU   B CA    
878  C C     . GLU   B 11  ? 0.1906 0.4905 0.3748 -0.0545 0.0093  -0.0221 11  GLU   B C     
879  O O     . GLU   B 11  ? 0.2028 0.4735 0.3722 -0.0571 0.0179  -0.0239 11  GLU   B O     
880  C CB    . GLU   B 11  ? 0.1800 0.5200 0.3941 -0.0722 0.0085  -0.0215 11  GLU   B CB    
881  C CG    . GLU   B 11  ? 0.1759 0.5385 0.4127 -0.0725 0.0149  -0.0178 11  GLU   B CG    
882  C CD    . GLU   B 11  ? 0.1797 0.5696 0.4342 -0.0897 0.0084  -0.0177 11  GLU   B CD    
883  O OE1   . GLU   B 11  ? 0.2073 0.5825 0.4506 -0.1075 0.0107  -0.0220 11  GLU   B OE1   
884  O OE2   . GLU   B 11  ? 0.1691 0.5921 0.4464 -0.0859 -0.0006 -0.0126 11  GLU   B OE2   
885  N N     . ILE   B 12  ? 0.2076 0.5237 0.3933 -0.0507 -0.0021 -0.0215 12  ILE   B N     
886  C CA    . ILE   B 12  ? 0.2368 0.5371 0.4009 -0.0525 -0.0075 -0.0242 12  ILE   B CA    
887  C C     . ILE   B 12  ? 0.2583 0.5580 0.4085 -0.0744 -0.0148 -0.0295 12  ILE   B C     
888  O O     . ILE   B 12  ? 0.2584 0.5897 0.4271 -0.0827 -0.0256 -0.0264 12  ILE   B O     
889  C CB    . ILE   B 12  ? 0.2361 0.5539 0.4070 -0.0392 -0.0177 -0.0189 12  ILE   B CB    
890  C CG1   . ILE   B 12  ? 0.2371 0.5570 0.4205 -0.0213 -0.0114 -0.0143 12  ILE   B CG1   
891  C CG2   . ILE   B 12  ? 0.2570 0.5547 0.4010 -0.0412 -0.0220 -0.0209 12  ILE   B CG2   
892  C CD1   . ILE   B 12  ? 0.2471 0.5401 0.4204 -0.0173 -0.0009 -0.0142 12  ILE   B CD1   
893  N N     . THR   B 13  ? 0.2725 0.5356 0.3902 -0.0848 -0.0083 -0.0365 13  THR   B N     
894  C CA    . THR   B 13  ? 0.3153 0.5652 0.4053 -0.1100 -0.0145 -0.0436 13  THR   B CA    
895  C C     . THR   B 13  ? 0.3272 0.5973 0.4089 -0.1167 -0.0363 -0.0398 13  THR   B C     
896  O O     . THR   B 13  ? 0.3012 0.5783 0.3862 -0.1005 -0.0409 -0.0343 13  THR   B O     
897  C CB    . THR   B 13  ? 0.3575 0.5526 0.4088 -0.1183 0.0044  -0.0532 13  THR   B CB    
898  O OG1   . THR   B 13  ? 0.3526 0.5282 0.3876 -0.1055 0.0099  -0.0526 13  THR   B OG1   
899  C CG2   . THR   B 13  ? 0.3559 0.5308 0.4177 -0.1133 0.0251  -0.0537 13  THR   B CG2   
900  N N     . GLU   B 14  ? 0.3563 0.6340 0.4254 -0.1429 -0.0505 -0.0416 14  GLU   B N     
901  C CA    . GLU   B 14  ? 0.4033 0.6940 0.4550 -0.1574 -0.0740 -0.0369 14  GLU   B CA    
902  C C     . GLU   B 14  ? 0.4218 0.6686 0.4242 -0.1583 -0.0688 -0.0430 14  GLU   B C     
903  O O     . GLU   B 14  ? 0.3964 0.6584 0.3983 -0.1510 -0.0832 -0.0345 14  GLU   B O     
904  C CB    . GLU   B 14  ? 0.4527 0.7512 0.4912 -0.1923 -0.0900 -0.0386 14  GLU   B CB    
905  C CG    . GLU   B 14  ? 0.4472 0.8083 0.5437 -0.1908 -0.1050 -0.0251 14  GLU   B CG    
906  C CD    . GLU   B 14  ? 0.5072 0.8859 0.6046 -0.2253 -0.1205 -0.0240 14  GLU   B CD    
907  O OE1   . GLU   B 14  ? 0.5041 0.9182 0.6482 -0.2209 -0.1172 -0.0182 14  GLU   B OE1   
908  O OE2   . GLU   B 14  ? 0.5786 0.9367 0.6314 -0.2571 -0.1353 -0.0283 14  GLU   B OE2   
909  N N     . GLU   B 15  ? 0.4713 0.6635 0.4349 -0.1661 -0.0460 -0.0564 15  GLU   B N     
910  C CA    . GLU   B 15  ? 0.5204 0.6644 0.4362 -0.1666 -0.0334 -0.0632 15  GLU   B CA    
911  C C     . GLU   B 15  ? 0.4677 0.6240 0.4051 -0.1367 -0.0302 -0.0548 15  GLU   B C     
912  O O     . GLU   B 15  ? 0.4699 0.6167 0.3809 -0.1377 -0.0376 -0.0526 15  GLU   B O     
913  C CB    . GLU   B 15  ? 0.6032 0.6900 0.4926 -0.1674 0.0000  -0.0754 15  GLU   B CB    
914  C CG    . GLU   B 15  ? 0.7041 0.7579 0.5626 -0.1958 0.0080  -0.0871 15  GLU   B CG    
915  C CD    . GLU   B 15  ? 0.7829 0.7971 0.6461 -0.1825 0.0433  -0.0922 15  GLU   B CD    
916  O OE1   . GLU   B 15  ? 0.8287 0.7932 0.6613 -0.1772 0.0690  -0.0980 15  GLU   B OE1   
917  O OE2   . GLU   B 15  ? 0.8670 0.9032 0.7699 -0.1745 0.0458  -0.0877 15  GLU   B OE2   
918  N N     . GLN   B 16  ? 0.4028 0.5801 0.3858 -0.1124 -0.0210 -0.0495 16  GLN   B N     
919  C CA    . GLN   B 16  ? 0.3689 0.5574 0.3724 -0.0871 -0.0190 -0.0416 16  GLN   B CA    
920  C C     . GLN   B 16  ? 0.3510 0.5757 0.3662 -0.0831 -0.0434 -0.0315 16  GLN   B C     
921  O O     . GLN   B 16  ? 0.3501 0.5653 0.3507 -0.0748 -0.0450 -0.0278 16  GLN   B O     
922  C CB    . GLN   B 16  ? 0.3307 0.5336 0.3748 -0.0675 -0.0079 -0.0373 16  GLN   B CB    
923  C CG    . GLN   B 16  ? 0.3398 0.5082 0.3797 -0.0640 0.0171  -0.0412 16  GLN   B CG    
924  C CD    . GLN   B 16  ? 0.3229 0.5104 0.4005 -0.0517 0.0214  -0.0350 16  GLN   B CD    
925  O OE1   . GLN   B 16  ? 0.3038 0.4992 0.4003 -0.0354 0.0235  -0.0276 16  GLN   B OE1   
926  N NE2   . GLN   B 16  ? 0.2929 0.4871 0.3792 -0.0613 0.0217  -0.0373 16  GLN   B NE2   
927  N N     . LYS   B 17  ? 0.3234 0.5879 0.3655 -0.0892 -0.0608 -0.0256 17  LYS   B N     
928  C CA    . LYS   B 17  ? 0.3179 0.6211 0.3804 -0.0840 -0.0831 -0.0122 17  LYS   B CA    
929  C C     . LYS   B 17  ? 0.3590 0.6513 0.3814 -0.1019 -0.1009 -0.0094 17  LYS   B C     
930  O O     . LYS   B 17  ? 0.3549 0.6556 0.3778 -0.0906 -0.1107 0.0007  17  LYS   B O     
931  C CB    . LYS   B 17  ? 0.2984 0.6487 0.4045 -0.0868 -0.0947 -0.0044 17  LYS   B CB    
932  C CG    . LYS   B 17  ? 0.2610 0.6257 0.4059 -0.0687 -0.0790 -0.0046 17  LYS   B CG    
933  C CD    . LYS   B 17  ? 0.2469 0.6589 0.4350 -0.0723 -0.0888 0.0046  17  LYS   B CD    
934  C CE    . LYS   B 17  ? 0.2259 0.6425 0.4389 -0.0631 -0.0708 0.0009  17  LYS   B CE    
935  N NZ    . LYS   B 17  ? 0.2190 0.6790 0.4754 -0.0646 -0.0745 0.0097  17  LYS   B NZ    
936  N N     . GLN   B 18  ? 0.4125 0.6817 0.3960 -0.1310 -0.1044 -0.0180 18  GLN   B N     
937  C CA    . GLN   B 18  ? 0.4892 0.7367 0.4200 -0.1538 -0.1198 -0.0176 18  GLN   B CA    
938  C C     . GLN   B 18  ? 0.5018 0.7082 0.3964 -0.1424 -0.1048 -0.0215 18  GLN   B C     
939  O O     . GLN   B 18  ? 0.4890 0.7011 0.3691 -0.1421 -0.1212 -0.0112 18  GLN   B O     
940  C CB    . GLN   B 18  ? 0.5592 0.7726 0.4430 -0.1887 -0.1179 -0.0310 18  GLN   B CB    
941  C CG    . GLN   B 18  ? 0.5744 0.8277 0.4864 -0.2083 -0.1373 -0.0259 18  GLN   B CG    
942  C CD    . GLN   B 18  ? 0.6113 0.9172 0.5446 -0.2182 -0.1748 -0.0056 18  GLN   B CD    
943  O OE1   . GLN   B 18  ? 0.5942 0.9554 0.5858 -0.2137 -0.1877 0.0071  18  GLN   B OE1   
944  N NE2   . GLN   B 18  ? 0.6441 0.9336 0.5311 -0.2331 -0.1924 -0.0004 18  GLN   B NE2   
945  N N     . ARG   B 19  ? 0.5080 0.6779 0.3958 -0.1310 -0.0737 -0.0334 19  ARG   B N     
946  C CA    . ARG   B 19  ? 0.5391 0.6721 0.4011 -0.1190 -0.0548 -0.0363 19  ARG   B CA    
947  C C     . ARG   B 19  ? 0.4985 0.6604 0.3914 -0.0944 -0.0642 -0.0225 19  ARG   B C     
948  O O     . ARG   B 19  ? 0.5011 0.6458 0.3633 -0.0950 -0.0678 -0.0185 19  ARG   B O     
949  C CB    . ARG   B 19  ? 0.5500 0.6508 0.4167 -0.1095 -0.0212 -0.0467 19  ARG   B CB    
950  C CG    . ARG   B 19  ? 0.5748 0.6338 0.4141 -0.1010 0.0028  -0.0497 19  ARG   B CG    
951  C CD    . ARG   B 19  ? 0.5686 0.6002 0.4209 -0.0902 0.0362  -0.0555 19  ARG   B CD    
952  N NE    . ARG   B 19  ? 0.5736 0.5824 0.4207 -0.0759 0.0564  -0.0525 19  ARG   B NE    
953  C CZ    . ARG   B 19  ? 0.5473 0.5425 0.4188 -0.0604 0.0836  -0.0505 19  ARG   B CZ    
954  N NH1   . ARG   B 19  ? 0.5067 0.5114 0.4137 -0.0537 0.0923  -0.0494 19  ARG   B NH1   
955  N NH2   . ARG   B 19  ? 0.5613 0.5360 0.4248 -0.0514 0.1012  -0.0471 19  ARG   B NH2   
956  N N     . ALA   B 20  ? 0.4364 0.6390 0.3851 -0.0752 -0.0684 -0.0152 20  ALA   B N     
957  C CA    . ALA   B 20  ? 0.4066 0.6317 0.3833 -0.0526 -0.0747 -0.0033 20  ALA   B CA    
958  C C     . ALA   B 20  ? 0.4449 0.6930 0.4177 -0.0566 -0.1014 0.0109  20  ALA   B C     
959  O O     . ALA   B 20  ? 0.4378 0.6827 0.4082 -0.0430 -0.1036 0.0194  20  ALA   B O     
960  C CB    . ALA   B 20  ? 0.3468 0.6007 0.3744 -0.0342 -0.0695 -0.0006 20  ALA   B CB    
961  N N     . GLN   B 21  ? 0.4692 0.7389 0.4402 -0.0764 -0.1222 0.0150  21  GLN   B N     
962  C CA    . GLN   B 21  ? 0.5317 0.8259 0.4997 -0.0832 -0.1511 0.0324  21  GLN   B CA    
963  C C     . GLN   B 21  ? 0.5989 0.8536 0.4996 -0.1031 -0.1580 0.0310  21  GLN   B C     
964  O O     . GLN   B 21  ? 0.6119 0.8811 0.5070 -0.1036 -0.1803 0.0480  21  GLN   B O     
965  C CB    . GLN   B 21  ? 0.5376 0.8791 0.5398 -0.0962 -0.1733 0.0422  21  GLN   B CB    
966  C CG    . GLN   B 21  ? 0.5633 0.9473 0.5909 -0.0927 -0.2031 0.0678  21  GLN   B CG    
967  C CD    . GLN   B 21  ? 0.5557 0.9994 0.6552 -0.0813 -0.2122 0.0831  21  GLN   B CD    
968  O OE1   . GLN   B 21  ? 0.5206 0.9744 0.6607 -0.0582 -0.1916 0.0790  21  GLN   B OE1   
969  N NE2   . GLN   B 21  ? 0.5946 1.0785 0.7103 -0.0983 -0.2430 0.1024  21  GLN   B NE2   
970  N N     . GLY   B 22  ? 0.6094 0.8125 0.4592 -0.1181 -0.1373 0.0124  22  GLY   B N     
971  C CA    . GLY   B 22  ? 0.6558 0.8119 0.4345 -0.1374 -0.1368 0.0084  22  GLY   B CA    
972  C C     . GLY   B 22  ? 0.6446 0.7758 0.4115 -0.1173 -0.1205 0.0106  22  GLY   B C     
973  O O     . GLY   B 22  ? 0.5733 0.7281 0.3879 -0.0894 -0.1157 0.0180  22  GLY   B O     
974  N N     . ASP   B 23  ? 0.7049 0.7848 0.4038 -0.1341 -0.1109 0.0037  23  ASP   B N     
975  C CA    . ASP   B 23  ? 0.7440 0.7944 0.4187 -0.1223 -0.0967 0.0066  23  ASP   B CA    
976  C C     . ASP   B 23  ? 0.7468 0.7427 0.3907 -0.1222 -0.0559 -0.0109 23  ASP   B C     
977  O O     . ASP   B 23  ? 0.7645 0.7312 0.3824 -0.1165 -0.0412 -0.0092 23  ASP   B O     
978  C CB    . ASP   B 23  ? 0.8273 0.8642 0.4460 -0.1421 -0.1211 0.0181  23  ASP   B CB    
979  C CG    . ASP   B 23  ? 0.8413 0.9341 0.4939 -0.1422 -0.1624 0.0404  23  ASP   B CG    
980  O OD1   . ASP   B 23  ? 0.8123 0.9447 0.5284 -0.1133 -0.1655 0.0520  23  ASP   B OD1   
981  O OD2   . ASP   B 23  ? 0.9193 1.0147 0.5359 -0.1718 -0.1894 0.0460  23  ASP   B OD2   
982  N N     . ASP   B 24  ? 0.7259 0.7069 0.3739 -0.1278 -0.0357 -0.0258 24  ASP   B N     
983  C CA    . ASP   B 24  ? 0.7364 0.6690 0.3660 -0.1243 0.0059  -0.0392 24  ASP   B CA    
984  C C     . ASP   B 24  ? 0.6491 0.6047 0.3434 -0.0928 0.0227  -0.0339 24  ASP   B C     
985  O O     . ASP   B 24  ? 0.5962 0.5995 0.3418 -0.0765 0.0030  -0.0233 24  ASP   B O     
986  C CB    . ASP   B 24  ? 0.7797 0.6819 0.3833 -0.1440 0.0208  -0.0550 24  ASP   B CB    
987  C CG    . ASP   B 24  ? 0.8767 0.7369 0.3975 -0.1808 0.0117  -0.0631 24  ASP   B CG    
988  O OD1   . ASP   B 24  ? 0.9242 0.7406 0.3868 -0.1901 0.0230  -0.0651 24  ASP   B OD1   
989  O OD2   . ASP   B 24  ? 0.9320 0.8018 0.4442 -0.2021 -0.0067 -0.0672 24  ASP   B OD2   
990  N N     . TRP   B 25  ? 0.6467 0.5668 0.3368 -0.0854 0.0596  -0.0402 25  TRP   B N     
991  C CA    . TRP   B 25  ? 0.6031 0.5417 0.3488 -0.0597 0.0749  -0.0327 25  TRP   B CA    
992  C C     . TRP   B 25  ? 0.5175 0.4960 0.3234 -0.0484 0.0678  -0.0311 25  TRP   B C     
993  O O     . TRP   B 25  ? 0.5203 0.4876 0.3224 -0.0570 0.0766  -0.0398 25  TRP   B O     
994  C CB    . TRP   B 25  ? 0.6424 0.5384 0.3778 -0.0550 0.1168  -0.0365 25  TRP   B CB    
995  C CG    . TRP   B 25  ? 0.5989 0.5210 0.4000 -0.0318 0.1294  -0.0264 25  TRP   B CG    
996  C CD1   . TRP   B 25  ? 0.5668 0.5038 0.4163 -0.0216 0.1415  -0.0248 25  TRP   B CD1   
997  C CD2   . TRP   B 25  ? 0.5920 0.5328 0.4187 -0.0184 0.1251  -0.0144 25  TRP   B CD2   
998  N NE1   . TRP   B 25  ? 0.5371 0.5015 0.4389 -0.0047 0.1435  -0.0123 25  TRP   B NE1   
999  C CE2   . TRP   B 25  ? 0.5535 0.5198 0.4422 -0.0030 0.1343  -0.0066 25  TRP   B CE2   
1000 C CE3   . TRP   B 25  ? 0.6223 0.5593 0.4242 -0.0192 0.1137  -0.0086 25  TRP   B CE3   
1001 C CZ2   . TRP   B 25  ? 0.5433 0.5303 0.4672 0.0088  0.1321  0.0055  25  TRP   B CZ2   
1002 C CZ3   . TRP   B 25  ? 0.6173 0.5723 0.4548 -0.0054 0.1144  0.0026  25  TRP   B CZ3   
1003 C CH2   . TRP   B 25  ? 0.5768 0.5571 0.4742 0.0073  0.1225  0.0090  25  TRP   B CH2   
1004 N N     . PRO   B 26  ? 0.4509 0.4700 0.3089 -0.0303 0.0555  -0.0211 26  PRO   B N     
1005 C CA    . PRO   B 26  ? 0.4289 0.4607 0.2968 -0.0187 0.0464  -0.0106 26  PRO   B CA    
1006 C C     . PRO   B 26  ? 0.4189 0.4780 0.2857 -0.0183 0.0148  -0.0034 26  PRO   B C     
1007 O O     . PRO   B 26  ? 0.4074 0.4759 0.2866 -0.0066 0.0088  0.0057  26  PRO   B O     
1008 C CB    . PRO   B 26  ? 0.3776 0.4320 0.3007 -0.0023 0.0543  -0.0050 26  PRO   B CB    
1009 C CG    . PRO   B 26  ? 0.3537 0.4312 0.3002 -0.0042 0.0445  -0.0090 26  PRO   B CG    
1010 C CD    . PRO   B 26  ? 0.4008 0.4508 0.3092 -0.0211 0.0525  -0.0198 26  PRO   B CD    
1011 N N     . TYR   B 27  ? 0.4287 0.5000 0.2829 -0.0313 -0.0045 -0.0059 27  TYR   B N     
1012 C CA    . TYR   B 27  ? 0.4109 0.5192 0.2833 -0.0276 -0.0337 0.0042  27  TYR   B CA    
1013 C C     . TYR   B 27  ? 0.4467 0.5443 0.2842 -0.0313 -0.0474 0.0140  27  TYR   B C     
1014 O O     . TYR   B 27  ? 0.4228 0.5439 0.2833 -0.0179 -0.0620 0.0265  27  TYR   B O     
1015 C CB    . TYR   B 27  ? 0.4055 0.5366 0.2878 -0.0397 -0.0481 0.0008  27  TYR   B CB    
1016 C CG    . TYR   B 27  ? 0.3695 0.5123 0.2896 -0.0329 -0.0347 -0.0062 27  TYR   B CG    
1017 C CD1   . TYR   B 27  ? 0.3280 0.5014 0.2958 -0.0146 -0.0374 -0.0004 27  TYR   B CD1   
1018 C CD2   . TYR   B 27  ? 0.3821 0.5007 0.2872 -0.0449 -0.0176 -0.0180 27  TYR   B CD2   
1019 C CE1   . TYR   B 27  ? 0.2959 0.4780 0.2933 -0.0102 -0.0266 -0.0053 27  TYR   B CE1   
1020 C CE2   . TYR   B 27  ? 0.3511 0.4798 0.2911 -0.0379 -0.0061 -0.0215 27  TYR   B CE2   
1021 C CZ    . TYR   B 27  ? 0.3097 0.4718 0.2953 -0.0214 -0.0123 -0.0147 27  TYR   B CZ    
1022 O OH    . TYR   B 27  ? 0.2790 0.4496 0.2942 -0.0164 -0.0028 -0.0167 27  TYR   B OH    
1023 N N     . GLY   B 28  ? 0.5120 0.5703 0.2924 -0.0489 -0.0403 0.0090  28  GLY   B N     
1024 C CA    . GLY   B 28  ? 0.5610 0.6028 0.3006 -0.0543 -0.0514 0.0188  28  GLY   B CA    
1025 C C     . GLY   B 28  ? 0.5545 0.5932 0.3116 -0.0340 -0.0415 0.0270  28  GLY   B C     
1026 O O     . GLY   B 28  ? 0.5520 0.6086 0.3184 -0.0251 -0.0610 0.0417  28  GLY   B O     
1027 N N     . GLN   B 29  ? 0.5393 0.5577 0.3060 -0.0266 -0.0116 0.0191  29  GLN   B N     
1028 C CA    . GLN   B 29  ? 0.5317 0.5474 0.3171 -0.0106 -0.0013 0.0265  29  GLN   B CA    
1029 C C     . GLN   B 29  ? 0.4884 0.5417 0.3228 0.0069  -0.0178 0.0354  29  GLN   B C     
1030 O O     . GLN   B 29  ? 0.4874 0.5390 0.3214 0.0160  -0.0237 0.0460  29  GLN   B O     
1031 C CB    . GLN   B 29  ? 0.5241 0.5230 0.3258 -0.0058 0.0306  0.0199  29  GLN   B CB    
1032 C CG    . GLN   B 29  ? 0.5134 0.5075 0.3310 0.0058  0.0412  0.0283  29  GLN   B CG    
1033 C CD    . GLN   B 29  ? 0.5612 0.5240 0.3305 -0.0002 0.0439  0.0341  29  GLN   B CD    
1034 O OE1   . GLN   B 29  ? 0.5989 0.5280 0.3223 -0.0136 0.0584  0.0281  29  GLN   B OE1   
1035 N NE2   . GLN   B 29  ? 0.5631 0.5325 0.3370 0.0085  0.0305  0.0455  29  GLN   B NE2   
1036 N N     . CYS   B 30  ? 0.4570 0.5394 0.3290 0.0108  -0.0233 0.0310  30  CYS   B N     
1037 C CA    . CYS   B 30  ? 0.4142 0.5273 0.3289 0.0262  -0.0343 0.0374  30  CYS   B CA    
1038 C C     . CYS   B 30  ? 0.4378 0.5653 0.3488 0.0309  -0.0573 0.0512  30  CYS   B C     
1039 O O     . CYS   B 30  ? 0.4175 0.5459 0.3415 0.0451  -0.0588 0.0605  30  CYS   B O     
1040 C CB    . CYS   B 30  ? 0.3699 0.5071 0.3177 0.0265  -0.0341 0.0299  30  CYS   B CB    
1041 S SG    . CYS   B 30  ? 0.3163 0.4837 0.3103 0.0440  -0.0412 0.0354  30  CYS   B SG    
1042 N N     . LYS   B 31  ? 0.4773 0.6130 0.3682 0.0175  -0.0745 0.0540  31  LYS   B N     
1043 C CA    . LYS   B 31  ? 0.5196 0.6721 0.4073 0.0191  -0.0995 0.0714  31  LYS   B CA    
1044 C C     . LYS   B 31  ? 0.5623 0.6886 0.4195 0.0231  -0.0996 0.0824  31  LYS   B C     
1045 O O     . LYS   B 31  ? 0.5866 0.7267 0.4627 0.0377  -0.1115 0.0988  31  LYS   B O     
1046 C CB    . LYS   B 31  ? 0.5426 0.7091 0.4118 -0.0020 -0.1200 0.0726  31  LYS   B CB    
1047 C CG    . LYS   B 31  ? 0.5079 0.7099 0.4217 -0.0005 -0.1227 0.0672  31  LYS   B CG    
1048 C CD    . LYS   B 31  ? 0.5410 0.7503 0.4367 -0.0255 -0.1350 0.0613  31  LYS   B CD    
1049 C CE    . LYS   B 31  ? 0.5094 0.7372 0.4413 -0.0237 -0.1248 0.0498  31  LYS   B CE    
1050 N NZ    . LYS   B 31  ? 0.5324 0.7702 0.4522 -0.0479 -0.1379 0.0456  31  LYS   B NZ    
1051 N N     . GLU   B 32  ? 0.5984 0.6855 0.4114 0.0119  -0.0835 0.0743  32  GLU   B N     
1052 C CA    . GLU   B 32  ? 0.6301 0.6881 0.4138 0.0153  -0.0784 0.0833  32  GLU   B CA    
1053 C C     . GLU   B 32  ? 0.5811 0.6399 0.4003 0.0362  -0.0658 0.0863  32  GLU   B C     
1054 O O     . GLU   B 32  ? 0.5738 0.6256 0.3889 0.0460  -0.0721 0.1005  32  GLU   B O     
1055 C CB    . GLU   B 32  ? 0.7038 0.7181 0.4356 -0.0007 -0.0576 0.0730  32  GLU   B CB    
1056 C CG    . GLU   B 32  ? 0.8188 0.8113 0.4876 -0.0235 -0.0710 0.0762  32  GLU   B CG    
1057 C CD    . GLU   B 32  ? 0.8901 0.8315 0.5010 -0.0350 -0.0488 0.0719  32  GLU   B CD    
1058 O OE1   . GLU   B 32  ? 0.8885 0.8108 0.5036 -0.0347 -0.0180 0.0576  32  GLU   B OE1   
1059 O OE2   . GLU   B 32  ? 0.9630 0.8840 0.5270 -0.0437 -0.0609 0.0842  32  GLU   B OE2   
1060 N N     . ASP   B 33  ? 0.5312 0.5966 0.3826 0.0413  -0.0490 0.0738  33  ASP   B N     
1061 C CA    . ASP   B 33  ? 0.4783 0.5431 0.3595 0.0558  -0.0387 0.0750  33  ASP   B CA    
1062 C C     . ASP   B 33  ? 0.4632 0.5486 0.3722 0.0720  -0.0527 0.0862  33  ASP   B C     
1063 O O     . ASP   B 33  ? 0.4359 0.5070 0.3482 0.0829  -0.0479 0.0933  33  ASP   B O     
1064 C CB    . ASP   B 33  ? 0.4435 0.5126 0.3499 0.0541  -0.0220 0.0620  33  ASP   B CB    
1065 C CG    . ASP   B 33  ? 0.4628 0.5108 0.3521 0.0427  -0.0022 0.0544  33  ASP   B CG    
1066 O OD1   . ASP   B 33  ? 0.4874 0.5085 0.3414 0.0371  0.0046  0.0583  33  ASP   B OD1   
1067 O OD2   . ASP   B 33  ? 0.4159 0.4737 0.3271 0.0398  0.0074  0.0457  33  ASP   B OD2   
1068 N N     . GLN   B 34  ? 0.4678 0.5843 0.3959 0.0730  -0.0684 0.0889  34  GLN   B N     
1069 C CA    . GLN   B 34  ? 0.4792 0.6184 0.4405 0.0902  -0.0786 0.1016  34  GLN   B CA    
1070 C C     . GLN   B 34  ? 0.5198 0.6507 0.4700 0.0998  -0.0898 0.1223  34  GLN   B C     
1071 O O     . GLN   B 34  ? 0.5421 0.6805 0.5212 0.1187  -0.0893 0.1332  34  GLN   B O     
1072 C CB    . GLN   B 34  ? 0.4633 0.6411 0.4505 0.0872  -0.0927 0.1025  34  GLN   B CB    
1073 C CG    . GLN   B 34  ? 0.4414 0.6294 0.4503 0.0842  -0.0803 0.0853  34  GLN   B CG    
1074 C CD    . GLN   B 34  ? 0.4277 0.6479 0.4515 0.0745  -0.0931 0.0837  34  GLN   B CD    
1075 O OE1   . GLN   B 34  ? 0.4271 0.6776 0.4767 0.0807  -0.1078 0.0973  34  GLN   B OE1   
1076 N NE2   . GLN   B 34  ? 0.4221 0.6352 0.4302 0.0584  -0.0870 0.0689  34  GLN   B NE2   
1077 N N     . LYS   B 35  ? 0.5508 0.6640 0.4587 0.0873  -0.0983 0.1286  35  LYS   B N     
1078 C CA    . LYS   B 35  ? 0.5957 0.6973 0.4867 0.0944  -0.1099 0.1501  35  LYS   B CA    
1079 C C     . LYS   B 35  ? 0.5953 0.6553 0.4628 0.0987  -0.0919 0.1495  35  LYS   B C     
1080 O O     . LYS   B 35  ? 0.6008 0.6487 0.4600 0.1085  -0.0983 0.1679  35  LYS   B O     
1081 C CB    . LYS   B 35  ? 0.6470 0.7551 0.5028 0.0759  -0.1337 0.1602  35  LYS   B CB    
1082 C CG    . LYS   B 35  ? 0.6611 0.8151 0.5462 0.0710  -0.1559 0.1658  35  LYS   B CG    
1083 C CD    . LYS   B 35  ? 0.7082 0.8789 0.5722 0.0570  -0.1887 0.1873  35  LYS   B CD    
1084 C CE    . LYS   B 35  ? 0.7018 0.9264 0.6116 0.0563  -0.2117 0.1990  35  LYS   B CE    
1085 N NZ    . LYS   B 35  ? 0.7424 0.9945 0.6535 0.0508  -0.2471 0.2303  35  LYS   B NZ    
1086 N N     . LYS   B 36  ? 0.5814 0.6212 0.4416 0.0917  -0.0700 0.1311  36  LYS   B N     
1087 C CA    . LYS   B 36  ? 0.6012 0.6059 0.4466 0.0943  -0.0527 0.1311  36  LYS   B CA    
1088 C C     . LYS   B 36  ? 0.6008 0.6004 0.4736 0.1137  -0.0476 0.1381  36  LYS   B C     
1089 O O     . LYS   B 36  ? 0.5728 0.5934 0.4808 0.1233  -0.0473 0.1337  36  LYS   B O     
1090 C CB    . LYS   B 36  ? 0.5887 0.5834 0.4338 0.0826  -0.0324 0.1126  36  LYS   B CB    
1091 C CG    . LYS   B 36  ? 0.6101 0.5974 0.4253 0.0648  -0.0272 0.1043  36  LYS   B CG    
1092 C CD    . LYS   B 36  ? 0.5791 0.5619 0.4082 0.0578  -0.0055 0.0902  36  LYS   B CD    
1093 C CE    . LYS   B 36  ? 0.6101 0.5744 0.4079 0.0431  0.0083  0.0841  36  LYS   B CE    
1094 N NZ    . LYS   B 36  ? 0.5758 0.5477 0.4000 0.0391  0.0261  0.0726  36  LYS   B NZ    
1095 N N     . SER   B 37  ? 0.6250 0.5913 0.4777 0.1180  -0.0405 0.1477  37  SER   B N     
1096 C CA    . SER   B 37  ? 0.6380 0.5865 0.5061 0.1349  -0.0322 0.1548  37  SER   B CA    
1097 C C     . SER   B 37  ? 0.6054 0.5485 0.4932 0.1333  -0.0155 0.1374  37  SER   B C     
1098 O O     . SER   B 37  ? 0.6090 0.5512 0.5185 0.1475  -0.0109 0.1386  37  SER   B O     
1099 C CB    . SER   B 37  ? 0.6866 0.5958 0.5242 0.1368  -0.0269 0.1682  37  SER   B CB    
1100 O OG    . SER   B 37  ? 0.6973 0.5846 0.5061 0.1186  -0.0152 0.1592  37  SER   B OG    
1101 N N     . GLU   B 38  ? 0.5686 0.5093 0.4499 0.1159  -0.0066 0.1225  38  GLU   B N     
1102 C CA    . GLU   B 38  ? 0.5328 0.4709 0.4307 0.1103  0.0049  0.1086  38  GLU   B CA    
1103 C C     . GLU   B 38  ? 0.4879 0.4562 0.4146 0.1156  0.0003  0.1004  38  GLU   B C     
1104 O O     . GLU   B 38  ? 0.4781 0.4378 0.4142 0.1150  0.0089  0.0922  38  GLU   B O     
1105 C CB    . GLU   B 38  ? 0.5194 0.4539 0.4117 0.0912  0.0138  0.0997  38  GLU   B CB    
1106 C CG    . GLU   B 38  ? 0.4889 0.4511 0.3874 0.0827  0.0102  0.0929  38  GLU   B CG    
1107 C CD    . GLU   B 38  ? 0.4726 0.4279 0.3665 0.0675  0.0228  0.0896  38  GLU   B CD    
1108 O OE1   . GLU   B 38  ? 0.4315 0.3878 0.3433 0.0592  0.0301  0.0851  38  GLU   B OE1   
1109 O OE2   . GLU   B 38  ? 0.4876 0.4346 0.3579 0.0638  0.0253  0.0935  38  GLU   B OE2   
1110 N N     . TRP   B 39  ? 0.4642 0.4643 0.4010 0.1185  -0.0127 0.1028  39  TRP   B N     
1111 C CA    . TRP   B 39  ? 0.4376 0.4683 0.4022 0.1221  -0.0168 0.0959  39  TRP   B CA    
1112 C C     . TRP   B 39  ? 0.4543 0.5027 0.4399 0.1404  -0.0251 0.1085  39  TRP   B C     
1113 O O     . TRP   B 39  ? 0.4521 0.5133 0.4621 0.1474  -0.0200 0.1035  39  TRP   B O     
1114 C CB    . TRP   B 39  ? 0.4028 0.4580 0.3682 0.1083  -0.0232 0.0875  39  TRP   B CB    
1115 C CG    . TRP   B 39  ? 0.3850 0.4277 0.3390 0.0928  -0.0127 0.0782  39  TRP   B CG    
1116 C CD1   . TRP   B 39  ? 0.3917 0.4267 0.3241 0.0824  -0.0108 0.0786  39  TRP   B CD1   
1117 C CD2   . TRP   B 39  ? 0.3587 0.3947 0.3233 0.0855  -0.0021 0.0697  39  TRP   B CD2   
1118 N NE1   . TRP   B 39  ? 0.3801 0.4081 0.3166 0.0721  0.0023  0.0719  39  TRP   B NE1   
1119 C CE2   . TRP   B 39  ? 0.3593 0.3902 0.3168 0.0728  0.0054  0.0676  39  TRP   B CE2   
1120 C CE3   . TRP   B 39  ? 0.3472 0.3799 0.3248 0.0869  0.0021  0.0645  39  TRP   B CE3   
1121 C CZ2   . TRP   B 39  ? 0.3317 0.3609 0.3022 0.0623  0.0139  0.0638  39  TRP   B CZ2   
1122 C CZ3   . TRP   B 39  ? 0.3369 0.3642 0.3188 0.0734  0.0084  0.0590  39  TRP   B CZ3   
1123 C CH2   . TRP   B 39  ? 0.3266 0.3557 0.3090 0.0616  0.0127  0.0602  39  TRP   B CH2   
1124 N N     . LYS   B 40  ? 0.4877 0.5391 0.4661 0.1473  -0.0375 0.1259  40  LYS   B N     
1125 C CA    . LYS   B 40  ? 0.5015 0.5853 0.5080 0.1608  -0.0516 0.1413  40  LYS   B CA    
1126 C C     . LYS   B 40  ? 0.5063 0.5887 0.5454 0.1831  -0.0392 0.1476  40  LYS   B C     
1127 O O     . LYS   B 40  ? 0.5252 0.6421 0.5993 0.1921  -0.0449 0.1540  40  LYS   B O     
1128 C CB    . LYS   B 40  ? 0.5279 0.6158 0.5187 0.1615  -0.0708 0.1626  40  LYS   B CB    
1129 C CG    . LYS   B 40  ? 0.5718 0.6263 0.5472 0.1740  -0.0664 0.1789  40  LYS   B CG    
1130 C CD    . LYS   B 40  ? 0.6167 0.6836 0.5800 0.1737  -0.0906 0.2034  40  LYS   B CD    
1131 C CE    . LYS   B 40  ? 0.6685 0.6968 0.6010 0.1786  -0.0880 0.2181  40  LYS   B CE    
1132 N NZ    . LYS   B 40  ? 0.6897 0.6986 0.6458 0.2037  -0.0735 0.2300  40  LYS   B NZ    
1133 N N     . ASP   B 41  ? 0.5270 0.5679 0.5541 0.1908  -0.0201 0.1451  41  ASP   B N     
1134 C CA    . ASP   B 41  ? 0.5398 0.5665 0.5895 0.2123  -0.0025 0.1504  41  ASP   B CA    
1135 C C     . ASP   B 41  ? 0.5060 0.5345 0.5681 0.2095  0.0131  0.1315  41  ASP   B C     
1136 O O     . ASP   B 41  ? 0.5132 0.5283 0.5918 0.2263  0.0312  0.1339  41  ASP   B O     
1137 C CB    . ASP   B 41  ? 0.5919 0.5665 0.6176 0.2204  0.0125  0.1562  41  ASP   B CB    
1138 C CG    . ASP   B 41  ? 0.6389 0.6116 0.6671 0.2359  0.0020  0.1835  41  ASP   B CG    
1139 O OD1   . ASP   B 41  ? 0.6907 0.6831 0.7556 0.2582  0.0011  0.2025  41  ASP   B OD1   
1140 O OD2   . ASP   B 41  ? 0.6539 0.6068 0.6492 0.2255  -0.0051 0.1874  41  ASP   B OD2   
1141 N N     . SER   B 42  ? 0.4713 0.5132 0.5244 0.1888  0.0083  0.1137  42  SER   B N     
1142 C CA    . SER   B 42  ? 0.4469 0.4911 0.5067 0.1824  0.0198  0.0967  42  SER   B CA    
1143 C C     . SER   B 42  ? 0.4259 0.5172 0.5224 0.1882  0.0124  0.0999  42  SER   B C     
1144 O O     . SER   B 42  ? 0.4145 0.5402 0.5238 0.1862  -0.0071 0.1096  42  SER   B O     
1145 C CB    . SER   B 42  ? 0.4162 0.4535 0.4519 0.1581  0.0165  0.0808  42  SER   B CB    
1146 O OG    . SER   B 42  ? 0.4088 0.4339 0.4407 0.1506  0.0290  0.0663  42  SER   B OG    
1147 N N     . ASP   B 43  ? 0.4427 0.5334 0.5525 0.1921  0.0281  0.0910  43  ASP   B N     
1148 C CA    . ASP   B 43  ? 0.4233 0.5565 0.5638 0.1910  0.0233  0.0891  43  ASP   B CA    
1149 C C     . ASP   B 43  ? 0.3794 0.5280 0.5071 0.1675  0.0115  0.0746  43  ASP   B C     
1150 O O     . ASP   B 43  ? 0.3489 0.5354 0.4990 0.1636  0.0014  0.0753  43  ASP   B O     
1151 C CB    . ASP   B 43  ? 0.4467 0.5689 0.6012 0.2023  0.0477  0.0841  43  ASP   B CB    
1152 C CG    . ASP   B 43  ? 0.4991 0.6108 0.6776 0.2298  0.0642  0.1008  43  ASP   B CG    
1153 O OD1   . ASP   B 43  ? 0.5004 0.6348 0.7022 0.2425  0.0504  0.1216  43  ASP   B OD1   
1154 O OD2   . ASP   B 43  ? 0.5701 0.6486 0.7424 0.2382  0.0920  0.0938  43  ASP   B OD2   
1155 N N     . PHE   B 44  ? 0.3655 0.4858 0.4606 0.1521  0.0131  0.0634  44  PHE   B N     
1156 C CA    . PHE   B 44  ? 0.3260 0.4567 0.4120 0.1321  0.0055  0.0521  44  PHE   B CA    
1157 C C     . PHE   B 44  ? 0.3181 0.4605 0.3968 0.1254  -0.0099 0.0576  44  PHE   B C     
1158 O O     . PHE   B 44  ? 0.3421 0.4687 0.4076 0.1304  -0.0126 0.0666  44  PHE   B O     
1159 C CB    . PHE   B 44  ? 0.3280 0.4264 0.3882 0.1183  0.0138  0.0416  44  PHE   B CB    
1160 C CG    . PHE   B 44  ? 0.3468 0.4230 0.3992 0.1181  0.0294  0.0336  44  PHE   B CG    
1161 C CD1   . PHE   B 44  ? 0.3852 0.4318 0.4308 0.1323  0.0451  0.0364  44  PHE   B CD1   
1162 C CD2   . PHE   B 44  ? 0.3385 0.4168 0.3847 0.1022  0.0299  0.0235  44  PHE   B CD2   
1163 C CE1   . PHE   B 44  ? 0.4139 0.4324 0.4446 0.1307  0.0632  0.0274  44  PHE   B CE1   
1164 C CE2   . PHE   B 44  ? 0.3701 0.4223 0.3998 0.0989  0.0444  0.0157  44  PHE   B CE2   
1165 C CZ    . PHE   B 44  ? 0.4017 0.4217 0.4209 0.1124  0.0623  0.0164  44  PHE   B CZ    
1166 N N     . LEU   B 45  ? 0.2819 0.4462 0.3646 0.1129  -0.0178 0.0517  45  LEU   B N     
1167 C CA    . LEU   B 45  ? 0.2747 0.4426 0.3431 0.1033  -0.0277 0.0535  45  LEU   B CA    
1168 C C     . LEU   B 45  ? 0.2903 0.4298 0.3366 0.0950  -0.0204 0.0500  45  LEU   B C     
1169 O O     . LEU   B 45  ? 0.2778 0.4036 0.3240 0.0915  -0.0116 0.0444  45  LEU   B O     
1170 C CB    . LEU   B 45  ? 0.2541 0.4450 0.3302 0.0918  -0.0329 0.0465  45  LEU   B CB    
1171 C CG    . LEU   B 45  ? 0.2574 0.4806 0.3563 0.0957  -0.0427 0.0514  45  LEU   B CG    
1172 C CD1   . LEU   B 45  ? 0.2443 0.4827 0.3519 0.0842  -0.0416 0.0413  45  LEU   B CD1   
1173 C CD2   . LEU   B 45  ? 0.2779 0.5108 0.3676 0.0935  -0.0587 0.0622  45  LEU   B CD2   
1174 N N     . PRO   B 46  ? 0.2911 0.4215 0.3177 0.0897  -0.0239 0.0540  46  PRO   B N     
1175 C CA    . PRO   B 46  ? 0.3000 0.4067 0.3107 0.0819  -0.0150 0.0527  46  PRO   B CA    
1176 C C     . PRO   B 46  ? 0.2822 0.3922 0.3047 0.0715  -0.0074 0.0448  46  PRO   B C     
1177 O O     . PRO   B 46  ? 0.2834 0.4105 0.3158 0.0665  -0.0085 0.0396  46  PRO   B O     
1178 C CB    . PRO   B 46  ? 0.3155 0.4173 0.3042 0.0757  -0.0180 0.0559  46  PRO   B CB    
1179 C CG    . PRO   B 46  ? 0.3265 0.4438 0.3134 0.0821  -0.0333 0.0636  46  PRO   B CG    
1180 C CD    . PRO   B 46  ? 0.3031 0.4450 0.3199 0.0886  -0.0365 0.0608  46  PRO   B CD    
1181 N N     . ASN   B 47  ? 0.2780 0.3718 0.2997 0.0670  -0.0008 0.0453  47  ASN   B N     
1182 C CA    . ASN   B 47  ? 0.2593 0.3578 0.2942 0.0552  0.0039  0.0432  47  ASN   B CA    
1183 C C     . ASN   B 47  ? 0.2613 0.3561 0.2939 0.0495  0.0116  0.0468  47  ASN   B C     
1184 O O     . ASN   B 47  ? 0.2718 0.3566 0.3069 0.0429  0.0180  0.0520  47  ASN   B O     
1185 C CB    . ASN   B 47  ? 0.2721 0.3556 0.3052 0.0491  0.0051  0.0442  47  ASN   B CB    
1186 C CG    . ASN   B 47  ? 0.2847 0.3651 0.3148 0.0545  0.0030  0.0390  47  ASN   B CG    
1187 O OD1   . ASN   B 47  ? 0.3212 0.3824 0.3377 0.0634  0.0056  0.0402  47  ASN   B OD1   
1188 N ND2   . ASN   B 47  ? 0.2629 0.3590 0.3048 0.0503  0.0007  0.0341  47  ASN   B ND2   
1189 N N     . THR   B 48  ? 0.2611 0.3635 0.2894 0.0504  0.0125  0.0439  48  THR   B N     
1190 C CA    . THR   B 48  ? 0.2874 0.3808 0.3080 0.0454  0.0246  0.0451  48  THR   B CA    
1191 C C     . THR   B 48  ? 0.2717 0.3789 0.3114 0.0414  0.0308  0.0410  48  THR   B C     
1192 O O     . THR   B 48  ? 0.2539 0.3770 0.3035 0.0426  0.0225  0.0362  48  THR   B O     
1193 C CB    . THR   B 48  ? 0.3138 0.3934 0.3008 0.0469  0.0221  0.0449  48  THR   B CB    
1194 O OG1   . THR   B 48  ? 0.3112 0.4057 0.2953 0.0484  0.0097  0.0403  48  THR   B OG1   
1195 C CG2   . THR   B 48  ? 0.3323 0.3967 0.3031 0.0521  0.0171  0.0520  48  THR   B CG2   
1196 N N     . GLN   B 49  ? 0.2960 0.3947 0.3404 0.0376  0.0479  0.0437  49  GLN   B N     
1197 C CA    . GLN   B 49  ? 0.3177 0.4222 0.3779 0.0356  0.0590  0.0413  49  GLN   B CA    
1198 C C     . GLN   B 49  ? 0.3158 0.4174 0.3524 0.0341  0.0538  0.0310  49  GLN   B C     
1199 O O     . GLN   B 49  ? 0.3021 0.4180 0.3546 0.0336  0.0502  0.0274  49  GLN   B O     
1200 C CB    . GLN   B 49  ? 0.3596 0.4494 0.4257 0.0342  0.0839  0.0463  49  GLN   B CB    
1201 C CG    . GLN   B 49  ? 0.3906 0.4921 0.4950 0.0336  0.0907  0.0600  49  GLN   B CG    
1202 C CD    . GLN   B 49  ? 0.4161 0.5451 0.5617 0.0327  0.0821  0.0667  49  GLN   B CD    
1203 O OE1   . GLN   B 49  ? 0.4556 0.5917 0.6100 0.0345  0.0829  0.0630  49  GLN   B OE1   
1204 N NE2   . GLN   B 49  ? 0.3990 0.5418 0.5663 0.0278  0.0720  0.0770  49  GLN   B NE2   
1205 N N     . ALA   B 50  ? 0.3330 0.4185 0.3321 0.0320  0.0497  0.0278  50  ALA   B N     
1206 C CA    . ALA   B 50  ? 0.3363 0.4197 0.3099 0.0263  0.0411  0.0202  50  ALA   B CA    
1207 C C     . ALA   B 50  ? 0.3000 0.4120 0.2944 0.0293  0.0226  0.0184  50  ALA   B C     
1208 O O     . ALA   B 50  ? 0.2984 0.4178 0.3000 0.0249  0.0234  0.0126  50  ALA   B O     
1209 C CB    . ALA   B 50  ? 0.3676 0.4332 0.2992 0.0221  0.0340  0.0216  50  ALA   B CB    
1210 N N     . CYS   B 51  ? 0.2948 0.4198 0.3002 0.0372  0.0097  0.0236  51  CYS   B N     
1211 C CA    . CYS   B 51  ? 0.2577 0.4073 0.2822 0.0415  -0.0040 0.0226  51  CYS   B CA    
1212 C C     . CYS   B 51  ? 0.2183 0.3803 0.2712 0.0412  0.0013  0.0198  51  CYS   B C     
1213 O O     . CYS   B 51  ? 0.1931 0.3718 0.2577 0.0403  -0.0046 0.0162  51  CYS   B O     
1214 C CB    . CYS   B 51  ? 0.2649 0.4180 0.2925 0.0516  -0.0132 0.0292  51  CYS   B CB    
1215 S SG    . CYS   B 51  ? 0.3137 0.4562 0.3114 0.0535  -0.0237 0.0373  51  CYS   B SG    
1216 N N     . TYR   B 52  ? 0.2127 0.3676 0.2776 0.0406  0.0116  0.0234  52  TYR   B N     
1217 C CA    . TYR   B 52  ? 0.1802 0.3470 0.2712 0.0387  0.0138  0.0247  52  TYR   B CA    
1218 C C     . TYR   B 52  ? 0.1912 0.3599 0.2892 0.0344  0.0221  0.0213  52  TYR   B C     
1219 O O     . TYR   B 52  ? 0.1773 0.3593 0.2870 0.0330  0.0175  0.0188  52  TYR   B O     
1220 C CB    . TYR   B 52  ? 0.1755 0.3371 0.2792 0.0372  0.0196  0.0333  52  TYR   B CB    
1221 C CG    . TYR   B 52  ? 0.1494 0.3245 0.2798 0.0326  0.0179  0.0393  52  TYR   B CG    
1222 C CD1   . TYR   B 52  ? 0.1323 0.3188 0.2667 0.0311  0.0085  0.0360  52  TYR   B CD1   
1223 C CD2   . TYR   B 52  ? 0.1418 0.3187 0.2943 0.0291  0.0259  0.0504  52  TYR   B CD2   
1224 C CE1   . TYR   B 52  ? 0.1272 0.3234 0.2802 0.0244  0.0049  0.0435  52  TYR   B CE1   
1225 C CE2   . TYR   B 52  ? 0.1263 0.3182 0.3048 0.0235  0.0210  0.0599  52  TYR   B CE2   
1226 C CZ    . TYR   B 52  ? 0.1210 0.3210 0.2961 0.0200  0.0090  0.0564  52  TYR   B CZ    
1227 O OH    . TYR   B 52  ? 0.1222 0.3350 0.3174 0.0118  0.0017  0.0674  52  TYR   B OH    
1228 N N     . ILE   B 53  ? 0.2254 0.3764 0.3127 0.0321  0.0367  0.0209  53  ILE   B N     
1229 C CA    . ILE   B 53  ? 0.2566 0.3992 0.3428 0.0279  0.0489  0.0162  53  ILE   B CA    
1230 C C     . ILE   B 53  ? 0.2482 0.3980 0.3196 0.0225  0.0368  0.0070  53  ILE   B C     
1231 O O     . ILE   B 53  ? 0.2427 0.3998 0.3267 0.0197  0.0379  0.0045  53  ILE   B O     
1232 C CB    . ILE   B 53  ? 0.3212 0.4343 0.3863 0.0255  0.0699  0.0148  53  ILE   B CB    
1233 C CG1   . ILE   B 53  ? 0.3489 0.4568 0.4340 0.0307  0.0853  0.0260  53  ILE   B CG1   
1234 C CG2   . ILE   B 53  ? 0.3506 0.4462 0.4074 0.0201  0.0858  0.0079  53  ILE   B CG2   
1235 C CD1   . ILE   B 53  ? 0.3282 0.4616 0.4564 0.0345  0.0785  0.0384  53  ILE   B CD1   
1236 N N     . GLY   B 54  ? 0.2585 0.4073 0.3050 0.0204  0.0248  0.0041  54  GLY   B N     
1237 C CA    . GLY   B 54  ? 0.2538 0.4139 0.2898 0.0136  0.0111  -0.0012 54  GLY   B CA    
1238 C C     . GLY   B 54  ? 0.2244 0.4126 0.2898 0.0178  0.0015  -0.0002 54  GLY   B C     
1239 O O     . GLY   B 54  ? 0.2263 0.4230 0.2951 0.0107  -0.0010 -0.0049 54  GLY   B O     
1240 N N     . SER   B 55  ? 0.2084 0.4062 0.2911 0.0275  -0.0016 0.0053  55  SER   B N     
1241 C CA    . SER   B 55  ? 0.1865 0.4029 0.2911 0.0309  -0.0060 0.0059  55  SER   B CA    
1242 C C     . SER   B 55  ? 0.1746 0.3918 0.2928 0.0258  0.0019  0.0046  55  SER   B C     
1243 O O     . SER   B 55  ? 0.1629 0.3931 0.2891 0.0224  -0.0012 0.0014  55  SER   B O     
1244 C CB    . SER   B 55  ? 0.1875 0.4027 0.2970 0.0389  -0.0078 0.0108  55  SER   B CB    
1245 O OG    . SER   B 55  ? 0.2007 0.4244 0.3238 0.0392  -0.0079 0.0107  55  SER   B OG    
1246 N N     . ILE   B 56  ? 0.1673 0.3721 0.2913 0.0256  0.0124  0.0091  56  ILE   B N     
1247 C CA    . ILE   B 56  ? 0.1595 0.3654 0.3011 0.0227  0.0199  0.0123  56  ILE   B CA    
1248 C C     . ILE   B 56  ? 0.1798 0.3791 0.3133 0.0161  0.0260  0.0049  56  ILE   B C     
1249 O O     . ILE   B 56  ? 0.1638 0.3713 0.3078 0.0126  0.0252  0.0043  56  ILE   B O     
1250 C CB    . ILE   B 56  ? 0.1397 0.3368 0.2963 0.0252  0.0309  0.0226  56  ILE   B CB    
1251 C CG1   . ILE   B 56  ? 0.1266 0.3307 0.2916 0.0270  0.0228  0.0310  56  ILE   B CG1   
1252 C CG2   . ILE   B 56  ? 0.1348 0.3326 0.3127 0.0239  0.0397  0.0292  56  ILE   B CG2   
1253 C CD1   . ILE   B 56  ? 0.1277 0.3266 0.3081 0.0284  0.0320  0.0422  56  ILE   B CD1   
1254 N N     . LEU   B 57  ? 0.2204 0.4011 0.3308 0.0122  0.0326  -0.0008 57  LEU   B N     
1255 C CA    . LEU   B 57  ? 0.2539 0.4206 0.3468 0.0017  0.0387  -0.0094 57  LEU   B CA    
1256 C C     . LEU   B 57  ? 0.2263 0.4141 0.3192 -0.0053 0.0231  -0.0143 57  LEU   B C     
1257 O O     . LEU   B 57  ? 0.2335 0.4210 0.3315 -0.0119 0.0269  -0.0173 57  LEU   B O     
1258 C CB    . LEU   B 57  ? 0.3262 0.4633 0.3843 -0.0048 0.0484  -0.0154 57  LEU   B CB    
1259 C CG    . LEU   B 57  ? 0.3683 0.4813 0.4296 0.0021  0.0712  -0.0103 57  LEU   B CG    
1260 C CD1   . LEU   B 57  ? 0.4351 0.5108 0.4526 -0.0066 0.0850  -0.0185 57  LEU   B CD1   
1261 C CD2   . LEU   B 57  ? 0.3533 0.4613 0.4447 0.0077  0.0892  -0.0034 57  LEU   B CD2   
1262 N N     . LEU   B 58  ? 0.2239 0.4314 0.3166 -0.0024 0.0072  -0.0129 58  LEU   B N     
1263 C CA    . LEU   B 58  ? 0.2066 0.4389 0.3068 -0.0077 -0.0064 -0.0145 58  LEU   B CA    
1264 C C     . LEU   B 58  ? 0.1747 0.4255 0.3020 -0.0032 -0.0055 -0.0123 58  LEU   B C     
1265 O O     . LEU   B 58  ? 0.1978 0.4641 0.3333 -0.0104 -0.0096 -0.0145 58  LEU   B O     
1266 C CB    . LEU   B 58  ? 0.2170 0.4649 0.3150 -0.0026 -0.0211 -0.0099 58  LEU   B CB    
1267 C CG    . LEU   B 58  ? 0.2066 0.4869 0.3223 -0.0050 -0.0352 -0.0068 58  LEU   B CG    
1268 C CD1   . LEU   B 58  ? 0.2235 0.5057 0.3277 -0.0245 -0.0410 -0.0116 58  LEU   B CD1   
1269 C CD2   . LEU   B 58  ? 0.2160 0.5103 0.3347 0.0040  -0.0478 0.0019  58  LEU   B CD2   
1270 N N     . THR   B 59  ? 0.1595 0.4086 0.2984 0.0063  -0.0007 -0.0073 59  THR   B N     
1271 C CA    . THR   B 59  ? 0.1268 0.3889 0.2822 0.0085  -0.0006 -0.0050 59  THR   B CA    
1272 C C     . THR   B 59  ? 0.1389 0.3925 0.3003 0.0030  0.0079  -0.0034 59  THR   B C     
1273 O O     . THR   B 59  ? 0.1218 0.3821 0.2920 0.0027  0.0081  -0.0002 59  THR   B O     
1274 C CB    . THR   B 59  ? 0.1083 0.3702 0.2654 0.0177  -0.0026 -0.0003 59  THR   B CB    
1275 O OG1   . THR   B 59  ? 0.1006 0.3468 0.2540 0.0194  0.0010  0.0044  59  THR   B OG1   
1276 C CG2   . THR   B 59  ? 0.1000 0.3714 0.2556 0.0250  -0.0091 -0.0005 59  THR   B CG2   
1277 N N     . THR   B 60  ? 0.1608 0.3959 0.3156 -0.0012 0.0166  -0.0045 60  THR   B N     
1278 C CA    . THR   B 60  ? 0.1659 0.3899 0.3287 -0.0047 0.0271  -0.0010 60  THR   B CA    
1279 C C     . THR   B 60  ? 0.1614 0.3910 0.3226 -0.0151 0.0266  -0.0073 60  THR   B C     
1280 O O     . THR   B 60  ? 0.1737 0.3995 0.3207 -0.0239 0.0252  -0.0155 60  THR   B O     
1281 C CB    . THR   B 60  ? 0.1904 0.3882 0.3465 -0.0041 0.0416  -0.0005 60  THR   B CB    
1282 O OG1   . THR   B 60  ? 0.2080 0.4056 0.3714 0.0051  0.0419  0.0074  60  THR   B OG1   
1283 C CG2   . THR   B 60  ? 0.2122 0.3953 0.3796 -0.0051 0.0555  0.0052  60  THR   B CG2   
1284 N N     . ALA   B 61  ? 0.1516 0.3884 0.3248 -0.0165 0.0274  -0.0026 61  ALA   B N     
1285 C CA    . ALA   B 61  ? 0.1660 0.4109 0.3403 -0.0269 0.0275  -0.0076 61  ALA   B CA    
1286 C C     . ALA   B 61  ? 0.1832 0.4038 0.3508 -0.0353 0.0396  -0.0096 61  ALA   B C     
1287 O O     . ALA   B 61  ? 0.1831 0.3954 0.3587 -0.0356 0.0469  -0.0028 61  ALA   B O     
1288 C CB    . ALA   B 61  ? 0.1553 0.4141 0.3395 -0.0258 0.0255  -0.0023 61  ALA   B CB    
1289 N N     . ARG   B 62  ? 0.2211 0.4257 0.3704 -0.0425 0.0427  -0.0183 62  ARG   B N     
1290 C CA    . ARG   B 62  ? 0.2641 0.4347 0.3991 -0.0512 0.0586  -0.0224 62  ARG   B CA    
1291 C C     . ARG   B 62  ? 0.2888 0.4587 0.4202 -0.0673 0.0596  -0.0277 62  ARG   B C     
1292 O O     . ARG   B 62  ? 0.3056 0.4438 0.4281 -0.0728 0.0757  -0.0288 62  ARG   B O     
1293 C CB    . ARG   B 62  ? 0.3124 0.4574 0.4182 -0.0578 0.0639  -0.0317 62  ARG   B CB    
1294 C CG    . ARG   B 62  ? 0.3317 0.4704 0.4399 -0.0428 0.0685  -0.0262 62  ARG   B CG    
1295 C CD    . ARG   B 62  ? 0.3959 0.4981 0.4703 -0.0490 0.0813  -0.0347 62  ARG   B CD    
1296 N NE    . ARG   B 62  ? 0.4149 0.5061 0.5002 -0.0328 0.0945  -0.0262 62  ARG   B NE    
1297 C CZ    . ARG   B 62  ? 0.4432 0.5176 0.5490 -0.0216 0.1151  -0.0162 62  ARG   B CZ    
1298 N NH1   . ARG   B 62  ? 0.4998 0.5516 0.6075 -0.0250 0.1312  -0.0158 62  ARG   B NH1   
1299 N NH2   . ARG   B 62  ? 0.4223 0.5033 0.5493 -0.0071 0.1196  -0.0047 62  ARG   B NH2   
1300 N N     . LYS   B 63  ? 0.2772 0.4793 0.4161 -0.0750 0.0448  -0.0304 63  LYS   B N     
1301 C CA    . LYS   B 63  ? 0.3090 0.5155 0.4478 -0.0924 0.0447  -0.0346 63  LYS   B CA    
1302 C C     . LYS   B 63  ? 0.2976 0.5153 0.4571 -0.0863 0.0490  -0.0261 63  LYS   B C     
1303 O O     . LYS   B 63  ? 0.2975 0.5443 0.4731 -0.0780 0.0409  -0.0216 63  LYS   B O     
1304 C CB    . LYS   B 63  ? 0.3110 0.5501 0.4531 -0.1039 0.0270  -0.0387 63  LYS   B CB    
1305 C CG    . LYS   B 63  ? 0.3378 0.5916 0.4875 -0.1239 0.0241  -0.0410 63  LYS   B CG    
1306 C CD    . LYS   B 63  ? 0.3621 0.6438 0.5133 -0.1412 0.0057  -0.0431 63  LYS   B CD    
1307 C CE    . LYS   B 63  ? 0.3874 0.6964 0.5601 -0.1578 0.0021  -0.0411 63  LYS   B CE    
1308 N NZ    . LYS   B 63  ? 0.3931 0.7419 0.5808 -0.1725 -0.0187 -0.0375 63  LYS   B NZ    
1309 N N     . THR   B 64  ? 0.3034 0.4946 0.4593 -0.0906 0.0629  -0.0234 64  THR   B N     
1310 C CA    . THR   B 64  ? 0.3058 0.5029 0.4755 -0.0877 0.0668  -0.0139 64  THR   B CA    
1311 C C     . THR   B 64  ? 0.3160 0.5110 0.4833 -0.1066 0.0715  -0.0183 64  THR   B C     
1312 O O     . THR   B 64  ? 0.3450 0.5088 0.4967 -0.1176 0.0815  -0.0235 64  THR   B O     
1313 C CB    . THR   B 64  ? 0.3178 0.4883 0.4904 -0.0759 0.0779  -0.0018 64  THR   B CB    
1314 O OG1   . THR   B 64  ? 0.2811 0.4593 0.4588 -0.0613 0.0719  0.0024  64  THR   B OG1   
1315 C CG2   . THR   B 64  ? 0.3217 0.4988 0.5046 -0.0737 0.0780  0.0111  64  THR   B CG2   
1316 N N     . THR   B 65  ? 0.2959 0.5190 0.4770 -0.1098 0.0673  -0.0154 65  THR   B N     
1317 C CA    . THR   B 65  ? 0.3131 0.5397 0.4971 -0.1275 0.0724  -0.0174 65  THR   B CA    
1318 C C     . THR   B 65  ? 0.3180 0.5411 0.5061 -0.1226 0.0801  -0.0064 65  THR   B C     
1319 O O     . THR   B 65  ? 0.3029 0.5449 0.4974 -0.1118 0.0759  -0.0011 65  THR   B O     
1320 C CB    . THR   B 65  ? 0.2938 0.5621 0.4946 -0.1358 0.0619  -0.0220 65  THR   B CB    
1321 O OG1   . THR   B 65  ? 0.2928 0.5664 0.4881 -0.1370 0.0506  -0.0284 65  THR   B OG1   
1322 C CG2   . THR   B 65  ? 0.3171 0.5926 0.5241 -0.1581 0.0658  -0.0243 65  THR   B CG2   
1323 N N     . TYR   B 66  ? 0.3389 0.5351 0.5194 -0.1324 0.0916  -0.0029 66  TYR   B N     
1324 C CA    . TYR   B 66  ? 0.3450 0.5349 0.5251 -0.1314 0.0983  0.0090  66  TYR   B CA    
1325 C C     . TYR   B 66  ? 0.3561 0.5633 0.5420 -0.1484 0.1029  0.0052  66  TYR   B C     
1326 O O     . TYR   B 66  ? 0.3515 0.5598 0.5391 -0.1650 0.1042  -0.0038 66  TYR   B O     
1327 C CB    . TYR   B 66  ? 0.3744 0.5235 0.5461 -0.1286 0.1089  0.0188  66  TYR   B CB    
1328 C CG    . TYR   B 66  ? 0.3758 0.5143 0.5505 -0.1097 0.1059  0.0265  66  TYR   B CG    
1329 C CD1   . TYR   B 66  ? 0.3617 0.5145 0.5418 -0.0966 0.0962  0.0393  66  TYR   B CD1   
1330 C CD2   . TYR   B 66  ? 0.3886 0.5018 0.5591 -0.1068 0.1135  0.0211  66  TYR   B CD2   
1331 C CE1   . TYR   B 66  ? 0.3590 0.5063 0.5470 -0.0812 0.0926  0.0487  66  TYR   B CE1   
1332 C CE2   . TYR   B 66  ? 0.3894 0.4953 0.5674 -0.0893 0.1135  0.0295  66  TYR   B CE2   
1333 C CZ    . TYR   B 66  ? 0.3738 0.4998 0.5641 -0.0763 0.1021  0.0444  66  TYR   B CZ    
1334 O OH    . TYR   B 66  ? 0.3778 0.5015 0.5805 -0.0608 0.1006  0.0548  66  TYR   B OH    
1335 N N     . SER   B 67  ? 0.3604 0.5810 0.5479 -0.1460 0.1054  0.0123  67  SER   B N     
1336 C CA    . SER   B 67  ? 0.3790 0.6124 0.5727 -0.1612 0.1146  0.0115  67  SER   B CA    
1337 C C     . SER   B 67  ? 0.3961 0.6170 0.5749 -0.1586 0.1221  0.0236  67  SER   B C     
1338 O O     . SER   B 67  ? 0.3659 0.5619 0.5298 -0.1491 0.1185  0.0347  67  SER   B O     
1339 C CB    . SER   B 67  ? 0.3524 0.6288 0.5693 -0.1632 0.1108  0.0038  67  SER   B CB    
1340 O OG    . SER   B 67  ? 0.3464 0.6372 0.5637 -0.1463 0.1083  0.0060  67  SER   B OG    
1341 O OXT   . SER   B 67  ? 0.3831 0.6205 0.5661 -0.1662 0.1311  0.0231  67  SER   B OXT   
1342 N N     . SER   C 4   ? 0.7821 0.8035 0.7539 -0.0369 0.0345  -0.0779 4   SER   C N     
1343 C CA    . SER   C 4   ? 0.6835 0.7054 0.6719 -0.0396 0.0308  -0.0818 4   SER   C CA    
1344 C C     . SER   C 4   ? 0.6601 0.6952 0.6770 -0.0312 0.0241  -0.0708 4   SER   C C     
1345 O O     . SER   C 4   ? 0.6578 0.6969 0.6869 -0.0337 0.0181  -0.0706 4   SER   C O     
1346 C CB    . SER   C 4   ? 0.6343 0.6568 0.6026 -0.0514 0.0203  -0.0866 4   SER   C CB    
1347 O OG    . SER   C 4   ? 0.5924 0.6125 0.5280 -0.0581 0.0175  -0.0881 4   SER   C OG    
1348 N N     . VAL   C 5   ? 0.6017 0.6418 0.6282 -0.0224 0.0259  -0.0621 5   VAL   C N     
1349 C CA    . VAL   C 5   ? 0.6355 0.6852 0.6848 -0.0152 0.0213  -0.0527 5   VAL   C CA    
1350 C C     . VAL   C 5   ? 0.6187 0.6645 0.6917 -0.0143 0.0265  -0.0556 5   VAL   C C     
1351 O O     . VAL   C 5   ? 0.6069 0.6594 0.6940 -0.0131 0.0203  -0.0506 5   VAL   C O     
1352 C CB    . VAL   C 5   ? 0.6409 0.6929 0.6911 -0.0084 0.0229  -0.0448 5   VAL   C CB    
1353 C CG1   . VAL   C 5   ? 0.7000 0.7444 0.7565 -0.0073 0.0347  -0.0484 5   VAL   C CG1   
1354 C CG2   . VAL   C 5   ? 0.5715 0.6322 0.6368 -0.0025 0.0167  -0.0353 5   VAL   C CG2   
1355 N N     . ASP   C 6   ? 0.6092 0.6440 0.6868 -0.0147 0.0385  -0.0630 6   ASP   C N     
1356 C CA    . ASP   C 6   ? 0.6166 0.6458 0.7179 -0.0128 0.0452  -0.0652 6   ASP   C CA    
1357 C C     . ASP   C 6   ? 0.5895 0.6096 0.6897 -0.0196 0.0452  -0.0737 6   ASP   C C     
1358 O O     . ASP   C 6   ? 0.6194 0.6319 0.7392 -0.0178 0.0518  -0.0756 6   ASP   C O     
1359 C CB    . ASP   C 6   ? 0.6421 0.6650 0.7532 -0.0090 0.0587  -0.0678 6   ASP   C CB    
1360 C CG    . ASP   C 6   ? 0.6714 0.6812 0.7637 -0.0134 0.0711  -0.0798 6   ASP   C CG    
1361 O OD1   . ASP   C 6   ? 0.6770 0.6828 0.7418 -0.0205 0.0672  -0.0857 6   ASP   C OD1   
1362 O OD2   . ASP   C 6   ? 0.6976 0.7019 0.8028 -0.0099 0.0847  -0.0827 6   ASP   C OD2   
1363 N N     . ASP   C 7   ? 0.5360 0.5568 0.6151 -0.0278 0.0374  -0.0778 7   ASP   C N     
1364 C CA    . ASP   C 7   ? 0.4230 0.4413 0.5037 -0.0355 0.0316  -0.0817 7   ASP   C CA    
1365 C C     . ASP   C 7   ? 0.3459 0.3804 0.4427 -0.0330 0.0201  -0.0699 7   ASP   C C     
1366 O O     . ASP   C 7   ? 0.3526 0.3894 0.4512 -0.0402 0.0133  -0.0709 7   ASP   C O     
1367 C CB    . ASP   C 7   ? 0.4581 0.4725 0.5101 -0.0471 0.0267  -0.0904 7   ASP   C CB    
1368 C CG    . ASP   C 7   ? 0.5588 0.5550 0.5886 -0.0517 0.0390  -0.1036 7   ASP   C CG    
1369 O OD1   . ASP   C 7   ? 0.6104 0.5957 0.6522 -0.0455 0.0534  -0.1072 7   ASP   C OD1   
1370 O OD2   . ASP   C 7   ? 0.5564 0.5502 0.5570 -0.0614 0.0342  -0.1094 7   ASP   C OD2   
1371 N N     . TYR   C 8   ? 0.2664 0.3117 0.3737 -0.0238 0.0181  -0.0589 8   TYR   C N     
1372 C CA    . TYR   C 8   ? 0.2196 0.2765 0.3441 -0.0203 0.0115  -0.0483 8   TYR   C CA    
1373 C C     . TYR   C 8   ? 0.2013 0.2498 0.3464 -0.0211 0.0159  -0.0492 8   TYR   C C     
1374 O O     . TYR   C 8   ? 0.1958 0.2340 0.3497 -0.0177 0.0249  -0.0520 8   TYR   C O     
1375 C CB    . TYR   C 8   ? 0.1862 0.2510 0.3135 -0.0114 0.0106  -0.0386 8   TYR   C CB    
1376 C CG    . TYR   C 8   ? 0.1618 0.2350 0.3050 -0.0073 0.0066  -0.0282 8   TYR   C CG    
1377 C CD1   . TYR   C 8   ? 0.1533 0.2368 0.2992 -0.0093 0.0000  -0.0233 8   TYR   C CD1   
1378 C CD2   . TYR   C 8   ? 0.1497 0.2210 0.3058 -0.0025 0.0097  -0.0230 8   TYR   C CD2   
1379 C CE1   . TYR   C 8   ? 0.1371 0.2271 0.2951 -0.0060 -0.0019 -0.0140 8   TYR   C CE1   
1380 C CE2   . TYR   C 8   ? 0.1378 0.2154 0.3043 0.0000  0.0061  -0.0134 8   TYR   C CE2   
1381 C CZ    . TYR   C 8   ? 0.1368 0.2229 0.3027 -0.0015 0.0011  -0.0093 8   TYR   C CZ    
1382 O OH    . TYR   C 8   ? 0.1331 0.2241 0.3073 0.0007  -0.0008 0.0000  8   TYR   C OH    
1383 N N     . ASN   C 9   ? 0.1855 0.2397 0.3398 -0.0248 0.0099  -0.0450 9   ASN   C N     
1384 C CA    . ASN   C 9   ? 0.1865 0.2337 0.3606 -0.0257 0.0128  -0.0431 9   ASN   C CA    
1385 C C     . ASN   C 9   ? 0.1675 0.2284 0.3538 -0.0208 0.0073  -0.0292 9   ASN   C C     
1386 O O     . ASN   C 9   ? 0.1896 0.2616 0.3764 -0.0246 0.0008  -0.0249 9   ASN   C O     
1387 C CB    . ASN   C 9   ? 0.2116 0.2500 0.3834 -0.0369 0.0118  -0.0516 9   ASN   C CB    
1388 C CG    . ASN   C 9   ? 0.2199 0.2452 0.4116 -0.0380 0.0171  -0.0509 9   ASN   C CG    
1389 O OD1   . ASN   C 9   ? 0.2016 0.2294 0.4107 -0.0305 0.0186  -0.0406 9   ASN   C OD1   
1390 N ND2   . ASN   C 9   ? 0.2377 0.2472 0.4257 -0.0478 0.0200  -0.0616 9   ASN   C ND2   
1391 N N     . PRO   C 10  ? 0.1440 0.2047 0.3412 -0.0132 0.0100  -0.0218 10  PRO   C N     
1392 C CA    . PRO   C 10  ? 0.1357 0.2063 0.3413 -0.0098 0.0057  -0.0092 10  PRO   C CA    
1393 C C     . PRO   C 10  ? 0.1503 0.2195 0.3708 -0.0140 0.0047  -0.0040 10  PRO   C C     
1394 O O     . PRO   C 10  ? 0.1470 0.2257 0.3705 -0.0122 0.0013  0.0063  10  PRO   C O     
1395 C CB    . PRO   C 10  ? 0.1254 0.1945 0.3374 -0.0032 0.0080  -0.0036 10  PRO   C CB    
1396 C CG    . PRO   C 10  ? 0.1331 0.1892 0.3522 -0.0030 0.0158  -0.0120 10  PRO   C CG    
1397 C CD    . PRO   C 10  ? 0.1444 0.1959 0.3474 -0.0084 0.0174  -0.0243 10  PRO   C CD    
1398 N N     . ALA   C 11  ? 0.1546 0.2110 0.3827 -0.0197 0.0083  -0.0111 11  ALA   C N     
1399 C CA    . ALA   C 11  ? 0.1671 0.2214 0.4078 -0.0255 0.0070  -0.0066 11  ALA   C CA    
1400 C C     . ALA   C 11  ? 0.1713 0.2414 0.4069 -0.0309 0.0005  -0.0035 11  ALA   C C     
1401 O O     . ALA   C 11  ? 0.1724 0.2466 0.4191 -0.0335 -0.0008 0.0050  11  ALA   C O     
1402 C CB    . ALA   C 11  ? 0.1826 0.2178 0.4290 -0.0322 0.0123  -0.0165 11  ALA   C CB    
1403 N N     . PHE   C 12  ? 0.1716 0.2504 0.3923 -0.0325 -0.0031 -0.0094 12  PHE   C N     
1404 C CA    . PHE   C 12  ? 0.1673 0.2642 0.3862 -0.0362 -0.0095 -0.0051 12  PHE   C CA    
1405 C C     . PHE   C 12  ? 0.1553 0.2658 0.3688 -0.0266 -0.0103 0.0037  12  PHE   C C     
1406 O O     . PHE   C 12  ? 0.1260 0.2336 0.3287 -0.0196 -0.0086 0.0023  12  PHE   C O     
1407 C CB    . PHE   C 12  ? 0.1816 0.2804 0.3885 -0.0440 -0.0140 -0.0149 12  PHE   C CB    
1408 C CG    . PHE   C 12  ? 0.2037 0.2866 0.4119 -0.0557 -0.0130 -0.0253 12  PHE   C CG    
1409 C CD1   . PHE   C 12  ? 0.2247 0.3118 0.4441 -0.0664 -0.0171 -0.0233 12  PHE   C CD1   
1410 C CD2   . PHE   C 12  ? 0.2212 0.2837 0.4190 -0.0565 -0.0069 -0.0375 12  PHE   C CD2   
1411 C CE1   . PHE   C 12  ? 0.2524 0.3216 0.4706 -0.0787 -0.0159 -0.0340 12  PHE   C CE1   
1412 C CE2   . PHE   C 12  ? 0.2449 0.2888 0.4409 -0.0676 -0.0042 -0.0486 12  PHE   C CE2   
1413 C CZ    . PHE   C 12  ? 0.2624 0.3087 0.4674 -0.0792 -0.0092 -0.0474 12  PHE   C CZ    
1414 N N     . ASP   C 13  ? 0.1558 0.2804 0.3775 -0.0268 -0.0118 0.0133  13  ASP   C N     
1415 C CA    . ASP   C 13  ? 0.1477 0.2857 0.3635 -0.0190 -0.0116 0.0205  13  ASP   C CA    
1416 C C     . ASP   C 13  ? 0.1451 0.2911 0.3503 -0.0180 -0.0156 0.0159  13  ASP   C C     
1417 O O     . ASP   C 13  ? 0.1799 0.3296 0.3863 -0.0258 -0.0206 0.0108  13  ASP   C O     
1418 C CB    . ASP   C 13  ? 0.1477 0.2993 0.3760 -0.0204 -0.0105 0.0308  13  ASP   C CB    
1419 C CG    . ASP   C 13  ? 0.1489 0.2930 0.3853 -0.0214 -0.0067 0.0377  13  ASP   C CG    
1420 O OD1   . ASP   C 13  ? 0.1517 0.2828 0.3832 -0.0179 -0.0050 0.0376  13  ASP   C OD1   
1421 O OD2   . ASP   C 13  ? 0.1666 0.3190 0.4150 -0.0260 -0.0057 0.0446  13  ASP   C OD2   
1422 N N     . ASN   C 14  ? 0.1369 0.2840 0.3302 -0.0090 -0.0139 0.0178  14  ASN   C N     
1423 C CA    . ASN   C 14  ? 0.1414 0.2953 0.3245 -0.0061 -0.0171 0.0162  14  ASN   C CA    
1424 C C     . ASN   C 14  ? 0.1422 0.3089 0.3271 0.0024  -0.0147 0.0257  14  ASN   C C     
1425 O O     . ASN   C 14  ? 0.1393 0.3001 0.3201 0.0084  -0.0089 0.0295  14  ASN   C O     
1426 C CB    . ASN   C 14  ? 0.1348 0.2745 0.3017 -0.0025 -0.0153 0.0098  14  ASN   C CB    
1427 C CG    . ASN   C 14  ? 0.1351 0.2799 0.2900 -0.0010 -0.0192 0.0082  14  ASN   C CG    
1428 O OD1   . ASN   C 14  ? 0.1230 0.2747 0.2741 0.0066  -0.0187 0.0145  14  ASN   C OD1   
1429 N ND2   . ASN   C 14  ? 0.1508 0.2899 0.2978 -0.0080 -0.0222 -0.0001 14  ASN   C ND2   
1430 N N     . THR   C 15  ? 0.1377 0.3208 0.3274 0.0029  -0.0190 0.0296  15  THR   C N     
1431 C CA    . THR   C 15  ? 0.1251 0.3217 0.3209 0.0119  -0.0151 0.0393  15  THR   C CA    
1432 C C     . THR   C 15  ? 0.1310 0.3181 0.3105 0.0228  -0.0104 0.0397  15  THR   C C     
1433 O O     . THR   C 15  ? 0.1304 0.3200 0.3109 0.0311  -0.0032 0.0459  15  THR   C O     
1434 C CB    . THR   C 15  ? 0.1199 0.3398 0.3316 0.0089  -0.0217 0.0452  15  THR   C CB    
1435 O OG1   . THR   C 15  ? 0.1191 0.3390 0.3210 0.0054  -0.0303 0.0407  15  THR   C OG1   
1436 C CG2   . THR   C 15  ? 0.1118 0.3409 0.3414 -0.0022 -0.0244 0.0462  15  THR   C CG2   
1437 N N     . HIS   C 16  ? 0.1391 0.3135 0.3025 0.0226  -0.0130 0.0331  16  HIS   C N     
1438 C CA    . HIS   C 16  ? 0.1225 0.2867 0.2702 0.0316  -0.0090 0.0337  16  HIS   C CA    
1439 C C     . HIS   C 16  ? 0.1293 0.2733 0.2627 0.0314  -0.0049 0.0278  16  HIS   C C     
1440 O O     . HIS   C 16  ? 0.1370 0.2716 0.2582 0.0383  -0.0002 0.0291  16  HIS   C O     
1441 C CB    . HIS   C 16  ? 0.1240 0.2909 0.2643 0.0315  -0.0152 0.0329  16  HIS   C CB    
1442 C CG    . HIS   C 16  ? 0.1217 0.3101 0.2754 0.0342  -0.0201 0.0418  16  HIS   C CG    
1443 N ND1   . HIS   C 16  ? 0.1228 0.3144 0.2704 0.0402  -0.0230 0.0468  16  HIS   C ND1   
1444 C CD2   . HIS   C 16  ? 0.1206 0.3295 0.2950 0.0314  -0.0232 0.0478  16  HIS   C CD2   
1445 C CE1   . HIS   C 16  ? 0.1212 0.3361 0.2867 0.0414  -0.0285 0.0562  16  HIS   C CE1   
1446 N NE2   . HIS   C 16  ? 0.1094 0.3356 0.2913 0.0351  -0.0292 0.0563  16  HIS   C NE2   
1447 N N     . TYR   C 17  ? 0.1299 0.2673 0.2655 0.0238  -0.0066 0.0219  17  TYR   C N     
1448 C CA    . TYR   C 17  ? 0.1446 0.2662 0.2702 0.0229  -0.0043 0.0171  17  TYR   C CA    
1449 C C     . TYR   C 17  ? 0.1400 0.2583 0.2735 0.0200  -0.0027 0.0186  17  TYR   C C     
1450 O O     . TYR   C 17  ? 0.1542 0.2797 0.3012 0.0161  -0.0040 0.0205  17  TYR   C O     
1451 C CB    . TYR   C 17  ? 0.1549 0.2712 0.2765 0.0178  -0.0069 0.0095  17  TYR   C CB    
1452 C CG    . TYR   C 17  ? 0.1731 0.2914 0.2834 0.0201  -0.0092 0.0093  17  TYR   C CG    
1453 C CD1   . TYR   C 17  ? 0.1990 0.3081 0.2951 0.0256  -0.0061 0.0103  17  TYR   C CD1   
1454 C CD2   . TYR   C 17  ? 0.1786 0.3077 0.2915 0.0163  -0.0149 0.0091  17  TYR   C CD2   
1455 C CE1   . TYR   C 17  ? 0.1996 0.3095 0.2853 0.0283  -0.0081 0.0120  17  TYR   C CE1   
1456 C CE2   . TYR   C 17  ? 0.1892 0.3212 0.2913 0.0186  -0.0182 0.0113  17  TYR   C CE2   
1457 C CZ    . TYR   C 17  ? 0.2044 0.3264 0.2931 0.0251  -0.0144 0.0130  17  TYR   C CZ    
1458 O OH    . TYR   C 17  ? 0.2308 0.3535 0.3082 0.0278  -0.0171 0.0164  17  TYR   C OH    
1459 N N     . SER   C 18  ? 0.1482 0.2557 0.2732 0.0211  -0.0007 0.0184  18  SER   C N     
1460 C CA    . SER   C 18  ? 0.1469 0.2509 0.2783 0.0179  -0.0009 0.0211  18  SER   C CA    
1461 C C     . SER   C 18  ? 0.1317 0.2310 0.2725 0.0137  -0.0025 0.0165  18  SER   C C     
1462 O O     . SER   C 18  ? 0.1317 0.2267 0.2673 0.0137  -0.0020 0.0109  18  SER   C O     
1463 C CB    . SER   C 18  ? 0.1386 0.2348 0.2563 0.0197  0.0007  0.0243  18  SER   C CB    
1464 O OG    . SER   C 18  ? 0.1376 0.2253 0.2463 0.0194  0.0001  0.0204  18  SER   C OG    
1465 N N     . ARG   C 19  ? 0.1190 0.2181 0.2728 0.0108  -0.0033 0.0201  19  ARG   C N     
1466 C CA    . ARG   C 19  ? 0.1231 0.2167 0.2886 0.0087  -0.0032 0.0180  19  ARG   C CA    
1467 C C     . ARG   C 19  ? 0.1284 0.2177 0.2873 0.0100  -0.0035 0.0182  19  ARG   C C     
1468 O O     . ARG   C 19  ? 0.1135 0.1994 0.2763 0.0098  -0.0013 0.0129  19  ARG   C O     
1469 C CB    . ARG   C 19  ? 0.1255 0.2189 0.3072 0.0066  -0.0043 0.0246  19  ARG   C CB    
1470 C CG    . ARG   C 19  ? 0.1354 0.2284 0.3308 0.0032  -0.0031 0.0226  19  ARG   C CG    
1471 C CD    . ARG   C 19  ? 0.1394 0.2405 0.3325 0.0014  -0.0038 0.0245  19  ARG   C CD    
1472 N NE    . ARG   C 19  ? 0.1516 0.2511 0.3591 -0.0040 -0.0035 0.0232  19  ARG   C NE    
1473 C CZ    . ARG   C 19  ? 0.1311 0.2378 0.3444 -0.0078 -0.0042 0.0268  19  ARG   C CZ    
1474 N NH1   . ARG   C 19  ? 0.1300 0.2469 0.3367 -0.0053 -0.0041 0.0327  19  ARG   C NH1   
1475 N NH2   . ARG   C 19  ? 0.1228 0.2257 0.3484 -0.0143 -0.0040 0.0242  19  ARG   C NH2   
1476 N N     . PHE   C 20  ? 0.1529 0.2419 0.3013 0.0104  -0.0057 0.0241  20  PHE   C N     
1477 C CA    . PHE   C 20  ? 0.1496 0.2346 0.2902 0.0095  -0.0074 0.0251  20  PHE   C CA    
1478 C C     . PHE   C 20  ? 0.1412 0.2224 0.2726 0.0108  -0.0045 0.0178  20  PHE   C C     
1479 O O     . PHE   C 20  ? 0.1326 0.2128 0.2713 0.0093  -0.0040 0.0163  20  PHE   C O     
1480 C CB    . PHE   C 20  ? 0.1619 0.2443 0.2856 0.0085  -0.0095 0.0305  20  PHE   C CB    
1481 C CG    . PHE   C 20  ? 0.1682 0.2451 0.2807 0.0053  -0.0123 0.0309  20  PHE   C CG    
1482 C CD1   . PHE   C 20  ? 0.1707 0.2509 0.2954 0.0011  -0.0178 0.0363  20  PHE   C CD1   
1483 C CD2   . PHE   C 20  ? 0.1763 0.2448 0.2680 0.0063  -0.0096 0.0264  20  PHE   C CD2   
1484 C CE1   . PHE   C 20  ? 0.1757 0.2528 0.2922 -0.0036 -0.0215 0.0369  20  PHE   C CE1   
1485 C CE2   . PHE   C 20  ? 0.1861 0.2482 0.2676 0.0016  -0.0122 0.0262  20  PHE   C CE2   
1486 C CZ    . PHE   C 20  ? 0.1792 0.2464 0.2730 -0.0040 -0.0186 0.0312  20  PHE   C CZ    
1487 N N     . HIS   C 21  ? 0.1421 0.2218 0.2593 0.0136  -0.0023 0.0147  21  HIS   C N     
1488 C CA    . HIS   C 21  ? 0.1499 0.2252 0.2563 0.0149  0.0001  0.0096  21  HIS   C CA    
1489 C C     . HIS   C 21  ? 0.1447 0.2213 0.2611 0.0133  0.0022  0.0038  21  HIS   C C     
1490 O O     . HIS   C 21  ? 0.1419 0.2150 0.2584 0.0118  0.0044  0.0015  21  HIS   C O     
1491 C CB    . HIS   C 21  ? 0.1499 0.2245 0.2422 0.0195  0.0015  0.0097  21  HIS   C CB    
1492 C CG    . HIS   C 21  ? 0.1544 0.2263 0.2380 0.0210  0.0031  0.0058  21  HIS   C CG    
1493 N ND1   . HIS   C 21  ? 0.1514 0.2289 0.2327 0.0242  0.0026  0.0062  21  HIS   C ND1   
1494 C CD2   . HIS   C 21  ? 0.1470 0.2130 0.2251 0.0190  0.0048  0.0023  21  HIS   C CD2   
1495 C CE1   . HIS   C 21  ? 0.1519 0.2262 0.2247 0.0240  0.0031  0.0034  21  HIS   C CE1   
1496 N NE2   . HIS   C 21  ? 0.1641 0.2307 0.2342 0.0209  0.0053  0.0007  21  HIS   C NE2   
1497 N N     . LEU   C 22  ? 0.1532 0.2340 0.2767 0.0129  0.0023  0.0012  22  LEU   C N     
1498 C CA    . LEU   C 22  ? 0.1626 0.2412 0.2895 0.0105  0.0054  -0.0062 22  LEU   C CA    
1499 C C     . LEU   C 22  ? 0.1599 0.2356 0.3032 0.0091  0.0091  -0.0074 22  LEU   C C     
1500 O O     . LEU   C 22  ? 0.1719 0.2434 0.3145 0.0081  0.0143  -0.0132 22  LEU   C O     
1501 C CB    . LEU   C 22  ? 0.1761 0.2585 0.3047 0.0083  0.0037  -0.0092 22  LEU   C CB    
1502 C CG    . LEU   C 22  ? 0.1652 0.2540 0.2820 0.0101  0.0000  -0.0068 22  LEU   C CG    
1503 C CD1   . LEU   C 22  ? 0.1589 0.2540 0.2800 0.0057  -0.0033 -0.0095 22  LEU   C CD1   
1504 C CD2   . LEU   C 22  ? 0.1666 0.2519 0.2666 0.0121  0.0007  -0.0080 22  LEU   C CD2   
1505 N N     . LEU   C 23  ? 0.1563 0.2344 0.3145 0.0095  0.0069  -0.0010 23  LEU   C N     
1506 C CA    . LEU   C 23  ? 0.1566 0.2339 0.3344 0.0096  0.0098  0.0006  23  LEU   C CA    
1507 C C     . LEU   C 23  ? 0.1373 0.2159 0.3145 0.0095  0.0105  0.0027  23  LEU   C C     
1508 O O     . LEU   C 23  ? 0.1277 0.2051 0.3159 0.0099  0.0167  -0.0005 23  LEU   C O     
1509 C CB    . LEU   C 23  ? 0.1642 0.2443 0.3592 0.0099  0.0063  0.0087  23  LEU   C CB    
1510 C CG    . LEU   C 23  ? 0.1599 0.2374 0.3612 0.0088  0.0074  0.0064  23  LEU   C CG    
1511 C CD1   . LEU   C 23  ? 0.1566 0.2367 0.3713 0.0089  0.0033  0.0166  23  LEU   C CD1   
1512 C CD2   . LEU   C 23  ? 0.1854 0.2549 0.3958 0.0083  0.0150  -0.0024 23  LEU   C CD2   
1513 N N     . ILE   C 24  ? 0.1404 0.2200 0.3040 0.0085  0.0053  0.0074  24  ILE   C N     
1514 C CA    . ILE   C 24  ? 0.1393 0.2190 0.3005 0.0065  0.0055  0.0087  24  ILE   C CA    
1515 C C     . ILE   C 24  ? 0.1414 0.2162 0.2914 0.0065  0.0122  0.0011  24  ILE   C C     
1516 O O     . ILE   C 24  ? 0.1102 0.1861 0.2677 0.0049  0.0163  0.0006  24  ILE   C O     
1517 C CB    . ILE   C 24  ? 0.1430 0.2217 0.2904 0.0037  -0.0014 0.0145  24  ILE   C CB    
1518 C CG1   . ILE   C 24  ? 0.1489 0.2201 0.2707 0.0052  -0.0011 0.0114  24  ILE   C CG1   
1519 C CG2   . ILE   C 24  ? 0.1407 0.2248 0.2993 0.0024  -0.0080 0.0231  24  ILE   C CG2   
1520 C CD1   . ILE   C 24  ? 0.1606 0.2261 0.2659 0.0021  -0.0054 0.0152  24  ILE   C CD1   
1521 N N     . GLU   C 25  ? 0.1294 0.2001 0.2635 0.0079  0.0134  -0.0041 25  GLU   C N     
1522 C CA    . GLU   C 25  ? 0.1571 0.2229 0.2767 0.0074  0.0183  -0.0099 25  GLU   C CA    
1523 C C     . GLU   C 25  ? 0.1486 0.2130 0.2767 0.0065  0.0262  -0.0167 25  GLU   C C     
1524 O O     . GLU   C 25  ? 0.1629 0.2250 0.2896 0.0051  0.0326  -0.0191 25  GLU   C O     
1525 C CB    . GLU   C 25  ? 0.1776 0.2414 0.2781 0.0093  0.0151  -0.0106 25  GLU   C CB    
1526 C CG    . GLU   C 25  ? 0.2008 0.2589 0.2831 0.0088  0.0183  -0.0132 25  GLU   C CG    
1527 C CD    . GLU   C 25  ? 0.2192 0.2778 0.2873 0.0117  0.0141  -0.0115 25  GLU   C CD    
1528 O OE1   . GLU   C 25  ? 0.2084 0.2648 0.2699 0.0148  0.0115  -0.0064 25  GLU   C OE1   
1529 O OE2   . GLU   C 25  ? 0.2308 0.2925 0.2975 0.0104  0.0135  -0.0154 25  GLU   C OE2   
1530 N N     . THR   C 26  ? 0.1481 0.2126 0.2855 0.0069  0.0268  -0.0199 26  THR   C N     
1531 C CA    . THR   C 26  ? 0.1505 0.2099 0.2947 0.0058  0.0358  -0.0278 26  THR   C CA    
1532 C C     . THR   C 26  ? 0.1418 0.2031 0.3099 0.0076  0.0426  -0.0255 26  THR   C C     
1533 O O     . THR   C 26  ? 0.1430 0.1989 0.3152 0.0075  0.0533  -0.0324 26  THR   C O     
1534 C CB    . THR   C 26  ? 0.1768 0.2334 0.3241 0.0045  0.0343  -0.0318 26  THR   C CB    
1535 O OG1   . THR   C 26  ? 0.1552 0.2169 0.3203 0.0066  0.0289  -0.0241 26  THR   C OG1   
1536 C CG2   . THR   C 26  ? 0.1956 0.2530 0.3218 0.0018  0.0280  -0.0342 26  THR   C CG2   
1537 N N     . ASN   C 27  ? 0.1231 0.1923 0.3073 0.0091  0.0368  -0.0158 27  ASN   C N     
1538 C CA    . ASN   C 27  ? 0.1329 0.2079 0.3428 0.0107  0.0414  -0.0110 27  ASN   C CA    
1539 C C     . ASN   C 27  ? 0.1364 0.2163 0.3433 0.0082  0.0418  -0.0077 27  ASN   C C     
1540 O O     . ASN   C 27  ? 0.1407 0.2297 0.3714 0.0086  0.0423  -0.0008 27  ASN   C O     
1541 C CB    . ASN   C 27  ? 0.1310 0.2126 0.3626 0.0126  0.0342  -0.0013 27  ASN   C CB    
1542 C CG    . ASN   C 27  ? 0.1220 0.1968 0.3635 0.0151  0.0381  -0.0050 27  ASN   C CG    
1543 O OD1   . ASN   C 27  ? 0.1386 0.2096 0.3975 0.0180  0.0485  -0.0084 27  ASN   C OD1   
1544 N ND2   . ASN   C 27  ? 0.1132 0.1854 0.3441 0.0138  0.0315  -0.0048 27  ASN   C ND2   
1545 N N     . GLY   C 28  ? 0.1544 0.2291 0.3346 0.0054  0.0411  -0.0113 28  GLY   C N     
1546 C CA    . GLY   C 28  ? 0.1651 0.2414 0.3398 0.0020  0.0426  -0.0089 28  GLY   C CA    
1547 C C     . GLY   C 28  ? 0.1753 0.2588 0.3578 -0.0013 0.0329  0.0008  28  GLY   C C     
1548 O O     . GLY   C 28  ? 0.1618 0.2508 0.3544 -0.0049 0.0349  0.0045  28  GLY   C O     
1549 N N     . ILE   C 29  ? 0.1626 0.2468 0.3418 -0.0009 0.0227  0.0052  29  ILE   C N     
1550 C CA    . ILE   C 29  ? 0.1610 0.2491 0.3400 -0.0057 0.0127  0.0134  29  ILE   C CA    
1551 C C     . ILE   C 29  ? 0.1713 0.2484 0.3205 -0.0089 0.0107  0.0109  29  ILE   C C     
1552 O O     . ILE   C 29  ? 0.1830 0.2592 0.3277 -0.0152 0.0063  0.0147  29  ILE   C O     
1553 C CB    . ILE   C 29  ? 0.1618 0.2538 0.3479 -0.0042 0.0044  0.0191  29  ILE   C CB    
1554 C CG1   . ILE   C 29  ? 0.1621 0.2642 0.3815 -0.0010 0.0066  0.0237  29  ILE   C CG1   
1555 C CG2   . ILE   C 29  ? 0.1547 0.2467 0.3296 -0.0103 -0.0065 0.0259  29  ILE   C CG2   
1556 C CD1   . ILE   C 29  ? 0.1751 0.2787 0.4026 0.0020  0.0016  0.0283  29  ILE   C CD1   
1557 N N     . THR   C 30  ? 0.1565 0.2246 0.2857 -0.0049 0.0136  0.0051  30  THR   C N     
1558 C CA    . THR   C 30  ? 0.1551 0.2115 0.2582 -0.0055 0.0140  0.0031  30  THR   C CA    
1559 C C     . THR   C 30  ? 0.1707 0.2234 0.2674 -0.0051 0.0225  -0.0016 30  THR   C C     
1560 O O     . THR   C 30  ? 0.1665 0.2236 0.2733 -0.0033 0.0284  -0.0055 30  THR   C O     
1561 C CB    . THR   C 30  ? 0.1555 0.2070 0.2435 -0.0007 0.0108  0.0023  30  THR   C CB    
1562 O OG1   . THR   C 30  ? 0.1427 0.1977 0.2349 0.0032  0.0146  -0.0019 30  THR   C OG1   
1563 C CG2   . THR   C 30  ? 0.1542 0.2094 0.2477 -0.0014 0.0042  0.0069  30  THR   C CG2   
1564 N N     . LYS   C 31  ? 0.1920 0.2344 0.2696 -0.0074 0.0236  -0.0012 31  LYS   C N     
1565 C CA    . LYS   C 31  ? 0.2017 0.2390 0.2693 -0.0082 0.0312  -0.0039 31  LYS   C CA    
1566 C C     . LYS   C 31  ? 0.2021 0.2268 0.2440 -0.0051 0.0298  -0.0032 31  LYS   C C     
1567 O O     . LYS   C 31  ? 0.2143 0.2285 0.2445 -0.0082 0.0297  -0.0005 31  LYS   C O     
1568 C CB    . LYS   C 31  ? 0.2062 0.2464 0.2851 -0.0150 0.0351  -0.0016 31  LYS   C CB    
1569 C CG    . LYS   C 31  ? 0.2174 0.2721 0.3260 -0.0160 0.0385  -0.0011 31  LYS   C CG    
1570 C CD    . LYS   C 31  ? 0.2297 0.2868 0.3431 -0.0122 0.0485  -0.0071 31  LYS   C CD    
1571 C CE    . LYS   C 31  ? 0.2218 0.2913 0.3664 -0.0116 0.0537  -0.0062 31  LYS   C CE    
1572 N NZ    . LYS   C 31  ? 0.2331 0.3013 0.3810 -0.0078 0.0648  -0.0136 31  LYS   C NZ    
1573 N N     . PRO   C 32  ? 0.1998 0.2253 0.2340 0.0008  0.0279  -0.0047 32  PRO   C N     
1574 C CA    . PRO   C 32  ? 0.2133 0.2292 0.2272 0.0051  0.0266  -0.0020 32  PRO   C CA    
1575 C C     . PRO   C 32  ? 0.2379 0.2454 0.2364 0.0033  0.0316  -0.0009 32  PRO   C C     
1576 O O     . PRO   C 32  ? 0.2554 0.2671 0.2552 0.0004  0.0363  -0.0041 32  PRO   C O     
1577 C CB    . PRO   C 32  ? 0.2113 0.2352 0.2267 0.0104  0.0230  -0.0029 32  PRO   C CB    
1578 C CG    . PRO   C 32  ? 0.1891 0.2240 0.2245 0.0088  0.0220  -0.0064 32  PRO   C CG    
1579 C CD    . PRO   C 32  ? 0.1881 0.2237 0.2340 0.0033  0.0269  -0.0081 32  PRO   C CD    
1580 N N     . CYS   C 33  ? 0.2599 0.2536 0.2432 0.0047  0.0316  0.0036  33  CYS   C N     
1581 C CA    . CYS   C 33  ? 0.2691 0.2524 0.2350 0.0044  0.0353  0.0071  33  CYS   C CA    
1582 C C     . CYS   C 33  ? 0.2704 0.2472 0.2239 0.0130  0.0319  0.0126  33  CYS   C C     
1583 O O     . CYS   C 33  ? 0.2709 0.2402 0.2241 0.0166  0.0306  0.0141  33  CYS   C O     
1584 C CB    . CYS   C 33  ? 0.2776 0.2483 0.2399 -0.0021 0.0391  0.0088  33  CYS   C CB    
1585 S SG    . CYS   C 33  ? 0.2999 0.2559 0.2417 -0.0044 0.0452  0.0141  33  CYS   C SG    
1586 N N     . ILE   C 34  ? 0.2792 0.2592 0.2230 0.0160  0.0305  0.0158  34  ILE   C N     
1587 C CA    . ILE   C 34  ? 0.2951 0.2715 0.2298 0.0247  0.0269  0.0237  34  ILE   C CA    
1588 C C     . ILE   C 34  ? 0.3085 0.2683 0.2258 0.0243  0.0308  0.0304  34  ILE   C C     
1589 O O     . ILE   C 34  ? 0.3175 0.2771 0.2255 0.0183  0.0334  0.0304  34  ILE   C O     
1590 C CB    . ILE   C 34  ? 0.3065 0.2991 0.2424 0.0272  0.0206  0.0250  34  ILE   C CB    
1591 C CG1   . ILE   C 34  ? 0.3147 0.3226 0.2675 0.0257  0.0175  0.0179  34  ILE   C CG1   
1592 C CG2   . ILE   C 34  ? 0.3225 0.3149 0.2539 0.0368  0.0160  0.0355  34  ILE   C CG2   
1593 C CD1   . ILE   C 34  ? 0.3072 0.3163 0.2733 0.0304  0.0168  0.0174  34  ILE   C CD1   
1594 N N     . VAL   C 35  ? 0.3293 0.2741 0.2410 0.0311  0.0319  0.0367  35  VAL   C N     
1595 C CA    . VAL   C 35  ? 0.3573 0.2837 0.2527 0.0327  0.0354  0.0453  35  VAL   C CA    
1596 C C     . VAL   C 35  ? 0.3638 0.2922 0.2578 0.0449  0.0311  0.0556  35  VAL   C C     
1597 O O     . VAL   C 35  ? 0.3412 0.2688 0.2441 0.0531  0.0310  0.0563  35  VAL   C O     
1598 C CB    . VAL   C 35  ? 0.3734 0.2763 0.2637 0.0295  0.0418  0.0439  35  VAL   C CB    
1599 C CG1   . VAL   C 35  ? 0.4049 0.2866 0.2783 0.0293  0.0464  0.0526  35  VAL   C CG1   
1600 C CG2   . VAL   C 35  ? 0.3777 0.2845 0.2759 0.0176  0.0439  0.0346  35  VAL   C CG2   
1601 N N     . SER   C 36  ? 0.3988 0.3318 0.2827 0.0456  0.0273  0.0638  36  SER   C N     
1602 C CA    . SER   C 36  ? 0.4299 0.3627 0.3114 0.0568  0.0230  0.0776  36  SER   C CA    
1603 C C     . SER   C 36  ? 0.4692 0.3757 0.3360 0.0593  0.0291  0.0868  36  SER   C C     
1604 O O     . SER   C 36  ? 0.4800 0.3694 0.3382 0.0511  0.0362  0.0819  36  SER   C O     
1605 C CB    . SER   C 36  ? 0.4378 0.3916 0.3155 0.0547  0.0134  0.0823  36  SER   C CB    
1606 O OG    . SER   C 36  ? 0.4610 0.4089 0.3186 0.0453  0.0148  0.0835  36  SER   C OG    
1607 N N     . THR   C 37  ? 0.4934 0.3974 0.3588 0.0706  0.0259  0.1016  37  THR   C N     
1608 C CA    . THR   C 37  ? 0.5062 0.3862 0.3573 0.0740  0.0304  0.1135  37  THR   C CA    
1609 C C     . THR   C 37  ? 0.5080 0.3865 0.3392 0.0624  0.0296  0.1162  37  THR   C C     
1610 O O     . THR   C 37  ? 0.5219 0.3770 0.3399 0.0613  0.0357  0.1230  37  THR   C O     
1611 C CB    . THR   C 37  ? 0.5225 0.4042 0.3810 0.0902  0.0263  0.1306  37  THR   C CB    
1612 O OG1   . THR   C 37  ? 0.5028 0.4140 0.3654 0.0905  0.0135  0.1371  37  THR   C OG1   
1613 C CG2   . THR   C 37  ? 0.5169 0.3929 0.3928 0.1023  0.0320  0.1279  37  THR   C CG2   
1614 N N     . GLU   C 38  ? 0.4985 0.3996 0.3264 0.0542  0.0230  0.1114  38  GLU   C N     
1615 C CA    . GLU   C 38  ? 0.5048 0.4061 0.3112 0.0436  0.0227  0.1141  38  GLU   C CA    
1616 C C     . GLU   C 38  ? 0.4731 0.3781 0.2770 0.0297  0.0293  0.0982  38  GLU   C C     
1617 O O     . GLU   C 38  ? 0.4684 0.3665 0.2542 0.0207  0.0341  0.0997  38  GLU   C O     
1618 C CB    . GLU   C 38  ? 0.5256 0.4485 0.3269 0.0452  0.0098  0.1226  38  GLU   C CB    
1619 C CG    . GLU   C 38  ? 0.5639 0.4853 0.3691 0.0592  0.0028  0.1421  38  GLU   C CG    
1620 C CD    . GLU   C 38  ? 0.6000 0.5440 0.3993 0.0595  -0.0122 0.1537  38  GLU   C CD    
1621 O OE1   . GLU   C 38  ? 0.6145 0.5714 0.3981 0.0468  -0.0172 0.1472  38  GLU   C OE1   
1622 O OE2   . GLU   C 38  ? 0.6125 0.5621 0.4250 0.0729  -0.0190 0.1694  38  GLU   C OE2   
1623 N N     . ASN   C 39  ? 0.4485 0.3653 0.2705 0.0280  0.0298  0.0843  39  ASN   C N     
1624 C CA    . ASN   C 39  ? 0.4248 0.3503 0.2486 0.0166  0.0346  0.0704  39  ASN   C CA    
1625 C C     . ASN   C 39  ? 0.4052 0.3327 0.2505 0.0162  0.0380  0.0590  39  ASN   C C     
1626 O O     . ASN   C 39  ? 0.3863 0.3180 0.2452 0.0245  0.0333  0.0590  39  ASN   C O     
1627 C CB    . ASN   C 39  ? 0.4156 0.3616 0.2370 0.0134  0.0278  0.0655  39  ASN   C CB    
1628 C CG    . ASN   C 39  ? 0.4516 0.3983 0.2480 0.0099  0.0236  0.0745  39  ASN   C CG    
1629 O OD1   . ASN   C 39  ? 0.4808 0.4185 0.2593 0.0014  0.0315  0.0740  39  ASN   C OD1   
1630 N ND2   . ASN   C 39  ? 0.4477 0.4058 0.2428 0.0158  0.0112  0.0836  39  ASN   C ND2   
1631 N N     . VAL   C 40  ? 0.3858 0.3121 0.2347 0.0065  0.0461  0.0502  40  VAL   C N     
1632 C CA    . VAL   C 40  ? 0.3570 0.2905 0.2267 0.0039  0.0478  0.0395  40  VAL   C CA    
1633 C C     . VAL   C 40  ? 0.3410 0.2926 0.2169 -0.0004 0.0478  0.0304  40  VAL   C C     
1634 O O     . VAL   C 40  ? 0.3507 0.3027 0.2163 -0.0073 0.0541  0.0285  40  VAL   C O     
1635 C CB    . VAL   C 40  ? 0.3529 0.2744 0.2264 -0.0039 0.0559  0.0376  40  VAL   C CB    
1636 C CG1   . VAL   C 40  ? 0.3295 0.2611 0.2254 -0.0068 0.0556  0.0284  40  VAL   C CG1   
1637 C CG2   . VAL   C 40  ? 0.3759 0.2748 0.2401 -0.0013 0.0570  0.0455  40  VAL   C CG2   
1638 N N     . TYR   C 41  ? 0.3118 0.2764 0.2032 0.0034  0.0420  0.0250  41  TYR   C N     
1639 C CA    . TYR   C 41  ? 0.3100 0.2890 0.2101 -0.0003 0.0425  0.0154  41  TYR   C CA    
1640 C C     . TYR   C 41  ? 0.2949 0.2770 0.2165 -0.0035 0.0474  0.0085  41  TYR   C C     
1641 O O     . TYR   C 41  ? 0.2871 0.2717 0.2228 0.0003  0.0429  0.0082  41  TYR   C O     
1642 C CB    . TYR   C 41  ? 0.2971 0.2881 0.2012 0.0050  0.0326  0.0153  41  TYR   C CB    
1643 C CG    . TYR   C 41  ? 0.3260 0.3168 0.2111 0.0076  0.0258  0.0243  41  TYR   C CG    
1644 C CD1   . TYR   C 41  ? 0.3429 0.3277 0.2256 0.0160  0.0214  0.0356  41  TYR   C CD1   
1645 C CD2   . TYR   C 41  ? 0.3449 0.3399 0.2128 0.0013  0.0248  0.0222  41  TYR   C CD2   
1646 C CE1   . TYR   C 41  ? 0.3694 0.3556 0.2374 0.0190  0.0145  0.0464  41  TYR   C CE1   
1647 C CE2   . TYR   C 41  ? 0.3782 0.3735 0.2269 0.0023  0.0174  0.0323  41  TYR   C CE2   
1648 C CZ    . TYR   C 41  ? 0.3934 0.3859 0.2440 0.0117  0.0114  0.0454  41  TYR   C CZ    
1649 O OH    . TYR   C 41  ? 0.4319 0.4268 0.2654 0.0128  0.0031  0.0572  41  TYR   C OH    
1650 N N     . THR   C 42  ? 0.3169 0.2989 0.2411 -0.0105 0.0570  0.0045  42  THR   C N     
1651 C CA    . THR   C 42  ? 0.3183 0.3044 0.2650 -0.0139 0.0613  0.0010  42  THR   C CA    
1652 C C     . THR   C 42  ? 0.3104 0.3098 0.2772 -0.0120 0.0592  -0.0060 42  THR   C C     
1653 O O     . THR   C 42  ? 0.3437 0.3475 0.3049 -0.0109 0.0586  -0.0104 42  THR   C O     
1654 C CB    . THR   C 42  ? 0.3336 0.3181 0.2812 -0.0215 0.0731  0.0004  42  THR   C CB    
1655 O OG1   . THR   C 42  ? 0.3399 0.3302 0.2846 -0.0232 0.0806  -0.0062 42  THR   C OG1   
1656 C CG2   . THR   C 42  ? 0.3568 0.3268 0.2846 -0.0244 0.0758  0.0081  42  THR   C CG2   
1657 N N     . PRO   C 43  ? 0.3086 0.3142 0.2984 -0.0126 0.0579  -0.0068 43  PRO   C N     
1658 C CA    . PRO   C 43  ? 0.2872 0.3045 0.2983 -0.0113 0.0576  -0.0121 43  PRO   C CA    
1659 C C     . PRO   C 43  ? 0.2960 0.3181 0.3154 -0.0141 0.0690  -0.0181 43  PRO   C C     
1660 O O     . PRO   C 43  ? 0.3033 0.3311 0.3339 -0.0119 0.0694  -0.0234 43  PRO   C O     
1661 C CB    . PRO   C 43  ? 0.2683 0.2901 0.2992 -0.0123 0.0530  -0.0089 43  PRO   C CB    
1662 C CG    . PRO   C 43  ? 0.2818 0.2940 0.3032 -0.0169 0.0537  -0.0038 43  PRO   C CG    
1663 C CD    . PRO   C 43  ? 0.3057 0.3060 0.3007 -0.0153 0.0554  -0.0020 43  PRO   C CD    
1664 N N     . ASP   C 44  ? 0.3302 0.3483 0.3430 -0.0188 0.0789  -0.0173 44  ASP   C N     
1665 C CA    . ASP   C 44  ? 0.3494 0.3693 0.3645 -0.0214 0.0929  -0.0232 44  ASP   C CA    
1666 C C     . ASP   C 44  ? 0.3550 0.3668 0.3405 -0.0222 0.0957  -0.0284 44  ASP   C C     
1667 O O     . ASP   C 44  ? 0.3865 0.3962 0.3671 -0.0253 0.1088  -0.0341 44  ASP   C O     
1668 C CB    . ASP   C 44  ? 0.3897 0.4107 0.4132 -0.0268 0.1027  -0.0189 44  ASP   C CB    
1669 C CG    . ASP   C 44  ? 0.4322 0.4591 0.4706 -0.0286 0.1198  -0.0237 44  ASP   C CG    
1670 O OD1   . ASP   C 44  ? 0.4604 0.4938 0.5181 -0.0247 0.1231  -0.0293 44  ASP   C OD1   
1671 O OD2   . ASP   C 44  ? 0.4985 0.5225 0.5295 -0.0336 0.1309  -0.0217 44  ASP   C OD2   
1672 N N     . ASN   C 45  ? 0.3588 0.3669 0.3256 -0.0199 0.0842  -0.0266 45  ASN   C N     
1673 C CA    . ASN   C 45  ? 0.3873 0.3907 0.3273 -0.0216 0.0823  -0.0304 45  ASN   C CA    
1674 C C     . ASN   C 45  ? 0.4090 0.4033 0.3205 -0.0263 0.0880  -0.0267 45  ASN   C C     
1675 O O     . ASN   C 45  ? 0.4578 0.4476 0.3482 -0.0309 0.0938  -0.0324 45  ASN   C O     
1676 C CB    . ASN   C 45  ? 0.4119 0.4171 0.3562 -0.0229 0.0870  -0.0416 45  ASN   C CB    
1677 C CG    . ASN   C 45  ? 0.4362 0.4387 0.3551 -0.0255 0.0789  -0.0447 45  ASN   C CG    
1678 O OD1   . ASN   C 45  ? 0.4757 0.4811 0.3868 -0.0231 0.0654  -0.0374 45  ASN   C OD1   
1679 N ND2   . ASN   C 45  ? 0.4820 0.4785 0.3862 -0.0310 0.0868  -0.0550 45  ASN   C ND2   
1680 N N     . ALA   C 46  ? 0.4026 0.3922 0.3108 -0.0259 0.0861  -0.0170 46  ALA   C N     
1681 C CA    . ALA   C 46  ? 0.4204 0.3999 0.3006 -0.0296 0.0890  -0.0105 46  ALA   C CA    
1682 C C     . ALA   C 46  ? 0.4102 0.3854 0.2787 -0.0245 0.0753  -0.0001 46  ALA   C C     
1683 O O     . ALA   C 46  ? 0.3712 0.3475 0.2560 -0.0194 0.0686  0.0034  46  ALA   C O     
1684 C CB    . ALA   C 46  ? 0.4300 0.4059 0.3172 -0.0341 0.1015  -0.0077 46  ALA   C CB    
1685 N N     . THR   C 47  ? 0.4345 0.4045 0.2743 -0.0260 0.0716  0.0052  47  THR   C N     
1686 C CA    . THR   C 47  ? 0.4540 0.4182 0.2809 -0.0210 0.0613  0.0178  47  THR   C CA    
1687 C C     . THR   C 47  ? 0.4598 0.4100 0.2742 -0.0242 0.0691  0.0263  47  THR   C C     
1688 O O     . THR   C 47  ? 0.5045 0.4503 0.2972 -0.0308 0.0761  0.0268  47  THR   C O     
1689 C CB    . THR   C 47  ? 0.4814 0.4501 0.2858 -0.0220 0.0519  0.0203  47  THR   C CB    
1690 O OG1   . THR   C 47  ? 0.4534 0.4345 0.2723 -0.0202 0.0451  0.0122  47  THR   C OG1   
1691 C CG2   . THR   C 47  ? 0.5008 0.4662 0.2941 -0.0157 0.0406  0.0356  47  THR   C CG2   
1692 N N     . VAL   C 48  ? 0.4407 0.3828 0.2672 -0.0209 0.0689  0.0321  48  VAL   C N     
1693 C CA    . VAL   C 48  ? 0.4600 0.3864 0.2757 -0.0245 0.0756  0.0408  48  VAL   C CA    
1694 C C     . VAL   C 48  ? 0.4712 0.3868 0.2730 -0.0169 0.0664  0.0539  48  VAL   C C     
1695 O O     . VAL   C 48  ? 0.4383 0.3515 0.2535 -0.0093 0.0603  0.0556  48  VAL   C O     
1696 C CB    . VAL   C 48  ? 0.4402 0.3624 0.2772 -0.0278 0.0816  0.0383  48  VAL   C CB    
1697 C CG1   . VAL   C 48  ? 0.4622 0.3667 0.2880 -0.0332 0.0885  0.0472  48  VAL   C CG1   
1698 C CG2   . VAL   C 48  ? 0.4283 0.3642 0.2857 -0.0335 0.0898  0.0274  48  VAL   C CG2   
1699 N N     . PRO   C 49  ? 0.4967 0.4055 0.2720 -0.0181 0.0654  0.0640  49  PRO   C N     
1700 C CA    . PRO   C 49  ? 0.5138 0.4109 0.2788 -0.0102 0.0580  0.0792  49  PRO   C CA    
1701 C C     . PRO   C 49  ? 0.5168 0.3936 0.2874 -0.0091 0.0638  0.0845  49  PRO   C C     
1702 O O     . PRO   C 49  ? 0.5260 0.3939 0.2937 -0.0183 0.0743  0.0830  49  PRO   C O     
1703 C CB    . PRO   C 49  ? 0.5484 0.4420 0.2828 -0.0148 0.0576  0.0890  49  PRO   C CB    
1704 C CG    . PRO   C 49  ? 0.5451 0.4511 0.2721 -0.0244 0.0631  0.0765  49  PRO   C CG    
1705 C CD    . PRO   C 49  ? 0.5173 0.4289 0.2704 -0.0270 0.0715  0.0620  49  PRO   C CD    
1706 N N     . HIS   C 50  ? 0.5160 0.3859 0.2961 0.0015  0.0577  0.0896  50  HIS   C N     
1707 C CA    . HIS   C 50  ? 0.5333 0.3798 0.3157 0.0031  0.0627  0.0942  50  HIS   C CA    
1708 C C     . HIS   C 50  ? 0.5416 0.3808 0.3251 0.0176  0.0556  0.1047  50  HIS   C C     
1709 O O     . HIS   C 50  ? 0.5176 0.3683 0.3166 0.0254  0.0500  0.0999  50  HIS   C O     
1710 C CB    . HIS   C 50  ? 0.5254 0.3711 0.3268 -0.0023 0.0673  0.0814  50  HIS   C CB    
1711 C CG    . HIS   C 50  ? 0.5562 0.3742 0.3541 -0.0043 0.0730  0.0858  50  HIS   C CG    
1712 N ND1   . HIS   C 50  ? 0.5612 0.3641 0.3627 0.0051  0.0708  0.0878  50  HIS   C ND1   
1713 C CD2   . HIS   C 50  ? 0.5652 0.3659 0.3541 -0.0143 0.0812  0.0895  50  HIS   C CD2   
1714 C CE1   . HIS   C 50  ? 0.6041 0.3795 0.3978 0.0005  0.0773  0.0914  50  HIS   C CE1   
1715 N NE2   . HIS   C 50  ? 0.6088 0.3832 0.3957 -0.0118 0.0831  0.0928  50  HIS   C NE2   
1716 N N     . LYS   C 51  ? 0.5937 0.4144 0.3620 0.0214  0.0567  0.1198  51  LYS   C N     
1717 C CA    . LYS   C 51  ? 0.6299 0.4418 0.4008 0.0366  0.0517  0.1325  51  LYS   C CA    
1718 C C     . LYS   C 51  ? 0.6082 0.3982 0.3897 0.0405  0.0585  0.1271  51  LYS   C C     
1719 O O     . LYS   C 51  ? 0.6364 0.4023 0.4102 0.0331  0.0670  0.1265  51  LYS   C O     
1720 C CB    . LYS   C 51  ? 0.6946 0.4940 0.4451 0.0382  0.0508  0.1513  51  LYS   C CB    
1721 C CG    . LYS   C 51  ? 0.7369 0.5348 0.4913 0.0551  0.0432  0.1685  51  LYS   C CG    
1722 C CD    . LYS   C 51  ? 0.8003 0.5816 0.5345 0.0563  0.0431  0.1888  51  LYS   C CD    
1723 C CE    . LYS   C 51  ? 0.8444 0.6358 0.5808 0.0704  0.0315  0.2087  51  LYS   C CE    
1724 N NZ    . LYS   C 51  ? 0.8915 0.6775 0.6031 0.0659  0.0280  0.2264  51  LYS   C NZ    
1725 N N     . GLN   C 52  ? 0.5838 0.3824 0.3820 0.0503  0.0551  0.1219  52  GLN   C N     
1726 C CA    . GLN   C 52  ? 0.5789 0.3561 0.3841 0.0545  0.0618  0.1161  52  GLN   C CA    
1727 C C     . GLN   C 52  ? 0.6182 0.3643 0.4148 0.0647  0.0672  0.1302  52  GLN   C C     
1728 O O     . GLN   C 52  ? 0.6080 0.3591 0.4052 0.0768  0.0625  0.1453  52  GLN   C O     
1729 C CB    . GLN   C 52  ? 0.5404 0.3353 0.3637 0.0634  0.0576  0.1090  52  GLN   C CB    
1730 C CG    . GLN   C 52  ? 0.5049 0.3241 0.3382 0.0536  0.0541  0.0940  52  GLN   C CG    
1731 C CD    . GLN   C 52  ? 0.5041 0.3114 0.3359 0.0403  0.0600  0.0818  52  GLN   C CD    
1732 O OE1   . GLN   C 52  ? 0.5310 0.3119 0.3577 0.0398  0.0663  0.0800  52  GLN   C OE1   
1733 N NE2   . GLN   C 52  ? 0.4781 0.3041 0.3145 0.0290  0.0581  0.0737  52  GLN   C NE2   
1734 N N     . GLY   C 53  ? 0.6486 0.3629 0.4369 0.0582  0.0768  0.1257  53  GLY   C N     
1735 C CA    . GLY   C 53  ? 0.6825 0.3599 0.4603 0.0648  0.0845  0.1369  53  GLY   C CA    
1736 C C     . GLY   C 53  ? 0.6920 0.3449 0.4733 0.0700  0.0924  0.1276  53  GLY   C C     
1737 O O     . GLY   C 53  ? 0.6679 0.3361 0.4600 0.0706  0.0904  0.1154  53  GLY   C O     
1738 N N     . SER   C 54  ? 0.7323 0.3451 0.5024 0.0732  0.1020  0.1335  54  SER   C N     
1739 C CA    . SER   C 54  ? 0.7508 0.3324 0.5188 0.0786  0.1118  0.1254  54  SER   C CA    
1740 C C     . SER   C 54  ? 0.7537 0.3229 0.5129 0.0586  0.1146  0.1072  54  SER   C C     
1741 O O     . SER   C 54  ? 0.7385 0.2934 0.4964 0.0604  0.1196  0.0959  54  SER   C O     
1742 C CB    . SER   C 54  ? 0.8053 0.3473 0.5651 0.0907  0.1216  0.1391  54  SER   C CB    
1743 O OG    . SER   C 54  ? 0.8356 0.3480 0.5780 0.0770  0.1265  0.1423  54  SER   C OG    
1744 N N     . ASP   C 55  ? 0.7555 0.3308 0.5091 0.0399  0.1116  0.1050  55  ASP   C N     
1745 C CA    . ASP   C 55  ? 0.7837 0.3560 0.5341 0.0198  0.1115  0.0896  55  ASP   C CA    
1746 C C     . ASP   C 55  ? 0.7490 0.3632 0.5152 0.0162  0.1023  0.0795  55  ASP   C C     
1747 O O     . ASP   C 55  ? 0.7122 0.3594 0.4889 0.0210  0.0957  0.0845  55  ASP   C O     
1748 C CB    . ASP   C 55  ? 0.8464 0.4082 0.5881 0.0017  0.1135  0.0927  55  ASP   C CB    
1749 C CG    . ASP   C 55  ? 0.9430 0.4573 0.6673 -0.0002 0.1234  0.0999  55  ASP   C CG    
1750 O OD1   . ASP   C 55  ? 0.9808 0.4625 0.6950 -0.0070 0.1291  0.0901  55  ASP   C OD1   
1751 O OD2   . ASP   C 55  ? 0.9675 0.4764 0.6868 0.0044  0.1253  0.1155  55  ASP   C OD2   
1752 N N     . TYR   C 56  ? 0.7476 0.3583 0.5138 0.0061  0.1017  0.0652  56  TYR   C N     
1753 C CA    . TYR   C 56  ? 0.6986 0.3439 0.4790 -0.0007 0.0935  0.0553  56  TYR   C CA    
1754 C C     . TYR   C 56  ? 0.6800 0.3492 0.4687 -0.0150 0.0893  0.0563  56  TYR   C C     
1755 O O     . TYR   C 56  ? 0.6827 0.3352 0.4642 -0.0290 0.0927  0.0572  56  TYR   C O     
1756 C CB    . TYR   C 56  ? 0.7095 0.3411 0.4842 -0.0101 0.0937  0.0417  56  TYR   C CB    
1757 C CG    . TYR   C 56  ? 0.7111 0.3385 0.4847 0.0038  0.0959  0.0368  56  TYR   C CG    
1758 C CD1   . TYR   C 56  ? 0.6703 0.3303 0.4603 0.0172  0.0910  0.0388  56  TYR   C CD1   
1759 C CD2   . TYR   C 56  ? 0.7418 0.3321 0.4973 0.0028  0.1036  0.0294  56  TYR   C CD2   
1760 C CE1   . TYR   C 56  ? 0.6721 0.3305 0.4630 0.0293  0.0940  0.0350  56  TYR   C CE1   
1761 C CE2   . TYR   C 56  ? 0.7524 0.3392 0.5063 0.0153  0.1076  0.0245  56  TYR   C CE2   
1762 C CZ    . TYR   C 56  ? 0.7128 0.3347 0.4858 0.0292  0.1031  0.0283  56  TYR   C CZ    
1763 O OH    . TYR   C 56  ? 0.7619 0.3860 0.5370 0.0414  0.1071  0.0247  56  TYR   C OH    
1764 N N     . VAL   C 57  ? 0.6217 0.3287 0.4261 -0.0119 0.0828  0.0553  57  VAL   C N     
1765 C CA    . VAL   C 57  ? 0.5890 0.3212 0.4047 -0.0248 0.0801  0.0532  57  VAL   C CA    
1766 C C     . VAL   C 57  ? 0.5326 0.2892 0.3647 -0.0295 0.0737  0.0425  57  VAL   C C     
1767 O O     . VAL   C 57  ? 0.4960 0.2647 0.3339 -0.0187 0.0698  0.0396  57  VAL   C O     
1768 C CB    . VAL   C 57  ? 0.5755 0.3261 0.3920 -0.0195 0.0802  0.0617  57  VAL   C CB    
1769 C CG1   . VAL   C 57  ? 0.5580 0.3316 0.3818 -0.0050 0.0743  0.0625  57  VAL   C CG1   
1770 C CG2   . VAL   C 57  ? 0.5580 0.3272 0.3832 -0.0334 0.0817  0.0597  57  VAL   C CG2   
1771 N N     . LEU   C 58  ? 0.5129 0.2785 0.3545 -0.0458 0.0726  0.0382  58  LEU   C N     
1772 C CA    . LEU   C 58  ? 0.4917 0.2823 0.3516 -0.0518 0.0660  0.0305  58  LEU   C CA    
1773 C C     . LEU   C 58  ? 0.4642 0.2873 0.3398 -0.0439 0.0640  0.0308  58  LEU   C C     
1774 O O     . LEU   C 58  ? 0.4636 0.2973 0.3430 -0.0466 0.0681  0.0346  58  LEU   C O     
1775 C CB    . LEU   C 58  ? 0.4881 0.2804 0.3563 -0.0711 0.0657  0.0290  58  LEU   C CB    
1776 C CG    . LEU   C 58  ? 0.4738 0.2918 0.3635 -0.0795 0.0580  0.0235  58  LEU   C CG    
1777 C CD1   . LEU   C 58  ? 0.4886 0.2925 0.3684 -0.0818 0.0518  0.0173  58  LEU   C CD1   
1778 C CD2   . LEU   C 58  ? 0.4680 0.2986 0.3744 -0.0964 0.0583  0.0254  58  LEU   C CD2   
1779 N N     . VAL   C 59  ? 0.4296 0.2659 0.3120 -0.0344 0.0588  0.0269  59  VAL   C N     
1780 C CA    . VAL   C 59  ? 0.4027 0.2667 0.2988 -0.0273 0.0563  0.0259  59  VAL   C CA    
1781 C C     . VAL   C 59  ? 0.3867 0.2730 0.3043 -0.0345 0.0520  0.0201  59  VAL   C C     
1782 O O     . VAL   C 59  ? 0.3787 0.2856 0.3103 -0.0354 0.0534  0.0194  59  VAL   C O     
1783 C CB    . VAL   C 59  ? 0.3875 0.2539 0.2794 -0.0122 0.0536  0.0273  59  VAL   C CB    
1784 C CG1   . VAL   C 59  ? 0.4049 0.2539 0.2797 -0.0045 0.0574  0.0359  59  VAL   C CG1   
1785 C CG2   . VAL   C 59  ? 0.3842 0.2451 0.2762 -0.0076 0.0503  0.0232  59  VAL   C CG2   
1786 N N     . ALA   C 60  ? 0.3920 0.2731 0.3114 -0.0400 0.0472  0.0165  60  ALA   C N     
1787 C CA    . ALA   C 60  ? 0.3793 0.2800 0.3192 -0.0486 0.0419  0.0136  60  ALA   C CA    
1788 C C     . ALA   C 60  ? 0.3945 0.2816 0.3291 -0.0620 0.0379  0.0122  60  ALA   C C     
1789 O O     . ALA   C 60  ? 0.4344 0.2944 0.3469 -0.0624 0.0393  0.0112  60  ALA   C O     
1790 C CB    . ALA   C 60  ? 0.3629 0.2796 0.3126 -0.0401 0.0367  0.0107  60  ALA   C CB    
1791 N N     . GLY   C 61  ? 0.3738 0.2790 0.3287 -0.0733 0.0331  0.0126  61  GLY   C N     
1792 C CA    . GLY   C 61  ? 0.3891 0.2869 0.3408 -0.0874 0.0258  0.0114  61  GLY   C CA    
1793 C C     . GLY   C 61  ? 0.3888 0.3120 0.3691 -0.0998 0.0209  0.0150  61  GLY   C C     
1794 O O     . GLY   C 61  ? 0.4045 0.3443 0.4040 -0.0993 0.0269  0.0183  61  GLY   C O     
1795 N N     . LEU   C 62  ? 0.3945 0.3206 0.3772 -0.1113 0.0101  0.0148  62  LEU   C N     
1796 C CA    . LEU   C 62  ? 0.3935 0.3461 0.4063 -0.1237 0.0033  0.0202  62  LEU   C CA    
1797 C C     . LEU   C 62  ? 0.4237 0.3698 0.4385 -0.1382 0.0068  0.0233  62  LEU   C C     
1798 O O     . LEU   C 62  ? 0.4618 0.3778 0.4489 -0.1464 0.0074  0.0202  62  LEU   C O     
1799 C CB    . LEU   C 62  ? 0.4053 0.3626 0.4172 -0.1329 -0.0111 0.0204  62  LEU   C CB    
1800 C CG    . LEU   C 62  ? 0.4034 0.3768 0.4246 -0.1212 -0.0159 0.0205  62  LEU   C CG    
1801 C CD1   . LEU   C 62  ? 0.4068 0.3737 0.4124 -0.1315 -0.0291 0.0197  62  LEU   C CD1   
1802 C CD2   . LEU   C 62  ? 0.3875 0.3964 0.4505 -0.1174 -0.0161 0.0272  62  LEU   C CD2   
1803 N N     . ALA   C 63  ? 0.4072 0.3806 0.4553 -0.1416 0.0102  0.0293  63  ALA   C N     
1804 C CA    . ALA   C 63  ? 0.4200 0.3919 0.4752 -0.1553 0.0152  0.0336  63  ALA   C CA    
1805 C C     . ALA   C 63  ? 0.4404 0.4043 0.4897 -0.1764 0.0027  0.0347  63  ALA   C C     
1806 O O     . ALA   C 63  ? 0.4126 0.3935 0.4752 -0.1827 -0.0104 0.0369  63  ALA   C O     
1807 C CB    . ALA   C 63  ? 0.4001 0.4060 0.4956 -0.1545 0.0215  0.0401  63  ALA   C CB    
1808 N N     . GLY   C 64  ? 0.4816 0.4158 0.5063 -0.1872 0.0062  0.0329  64  GLY   C N     
1809 C CA    . GLY   C 64  ? 0.5016 0.4232 0.5163 -0.2097 -0.0047 0.0327  64  GLY   C CA    
1810 C C     . GLY   C 64  ? 0.5364 0.4340 0.5186 -0.2119 -0.0148 0.0249  64  GLY   C C     
1811 O O     . GLY   C 64  ? 0.5761 0.4576 0.5428 -0.2317 -0.0238 0.0229  64  GLY   C O     
1812 N N     . ASP   C 65  ? 0.5246 0.4172 0.4937 -0.1931 -0.0126 0.0201  65  ASP   C N     
1813 C CA    . ASP   C 65  ? 0.5380 0.4132 0.4800 -0.1946 -0.0213 0.0136  65  ASP   C CA    
1814 C C     . ASP   C 65  ? 0.5130 0.3649 0.4296 -0.1737 -0.0108 0.0071  65  ASP   C C     
1815 O O     . ASP   C 65  ? 0.5283 0.3909 0.4462 -0.1623 -0.0138 0.0058  65  ASP   C O     
1816 C CB    . ASP   C 65  ? 0.5029 0.4114 0.4683 -0.1999 -0.0363 0.0184  65  ASP   C CB    
1817 C CG    . ASP   C 65  ? 0.5009 0.3944 0.4385 -0.2095 -0.0485 0.0134  65  ASP   C CG    
1818 O OD1   . ASP   C 65  ? 0.5238 0.3781 0.4217 -0.2131 -0.0445 0.0045  65  ASP   C OD1   
1819 O OD2   . ASP   C 65  ? 0.4934 0.4137 0.4487 -0.2129 -0.0611 0.0187  65  ASP   C OD2   
1820 N N     . PRO   C 66  ? 0.5127 0.3322 0.4061 -0.1688 0.0011  0.0040  66  PRO   C N     
1821 C CA    . PRO   C 66  ? 0.5118 0.3105 0.3837 -0.1490 0.0104  -0.0004 66  PRO   C CA    
1822 C C     . PRO   C 66  ? 0.5395 0.3140 0.3816 -0.1493 0.0075  -0.0084 66  PRO   C C     
1823 O O     . PRO   C 66  ? 0.5187 0.2846 0.3499 -0.1319 0.0140  -0.0111 66  PRO   C O     
1824 C CB    . PRO   C 66  ? 0.5307 0.3030 0.3896 -0.1468 0.0223  0.0010  66  PRO   C CB    
1825 C CG    . PRO   C 66  ? 0.5579 0.3163 0.4111 -0.1711 0.0178  0.0007  66  PRO   C CG    
1826 C CD    . PRO   C 66  ? 0.5439 0.3427 0.4293 -0.1830 0.0057  0.0053  66  PRO   C CD    
1827 N N     . ASN   C 67  ? 0.5823 0.3445 0.4096 -0.1698 -0.0017 -0.0122 67  ASN   C N     
1828 C CA    . ASN   C 67  ? 0.6267 0.3690 0.4248 -0.1729 -0.0054 -0.0201 67  ASN   C CA    
1829 C C     . ASN   C 67  ? 0.5797 0.3529 0.3928 -0.1645 -0.0131 -0.0178 67  ASN   C C     
1830 O O     . ASN   C 67  ? 0.6059 0.3648 0.3980 -0.1555 -0.0095 -0.0232 67  ASN   C O     
1831 C CB    . ASN   C 67  ? 0.6998 0.4215 0.4756 -0.1994 -0.0147 -0.0249 67  ASN   C CB    
1832 C CG    . ASN   C 67  ? 0.7826 0.4512 0.5158 -0.2008 -0.0035 -0.0350 67  ASN   C CG    
1833 O OD1   . ASN   C 67  ? 0.8271 0.4732 0.5557 -0.1986 0.0070  -0.0346 67  ASN   C OD1   
1834 N ND2   . ASN   C 67  ? 0.8199 0.4668 0.5217 -0.2026 -0.0039 -0.0437 67  ASN   C ND2   
1835 N N     . ARG   C 68  ? 0.5390 0.3526 0.3880 -0.1680 -0.0228 -0.0096 68  ARG   C N     
1836 C CA    . ARG   C 68  ? 0.5145 0.3578 0.3814 -0.1595 -0.0297 -0.0059 68  ARG   C CA    
1837 C C     . ARG   C 68  ? 0.4651 0.3140 0.3400 -0.1349 -0.0182 -0.0059 68  ARG   C C     
1838 O O     . ARG   C 68  ? 0.4449 0.2929 0.3104 -0.1251 -0.0175 -0.0082 68  ARG   C O     
1839 C CB    . ARG   C 68  ? 0.5029 0.3868 0.4092 -0.1682 -0.0416 0.0038  68  ARG   C CB    
1840 C CG    . ARG   C 68  ? 0.4731 0.3871 0.4001 -0.1602 -0.0494 0.0091  68  ARG   C CG    
1841 C CD    . ARG   C 68  ? 0.4956 0.3997 0.3965 -0.1677 -0.0590 0.0064  68  ARG   C CD    
1842 N NE    . ARG   C 68  ? 0.4735 0.4029 0.3920 -0.1577 -0.0643 0.0120  68  ARG   C NE    
1843 C CZ    . ARG   C 68  ? 0.5003 0.4265 0.3996 -0.1632 -0.0731 0.0119  68  ARG   C CZ    
1844 N NH1   . ARG   C 68  ? 0.5723 0.4694 0.4314 -0.1771 -0.0761 0.0048  68  ARG   C NH1   
1845 N NH2   . ARG   C 68  ? 0.4903 0.4400 0.4079 -0.1555 -0.0784 0.0186  68  ARG   C NH2   
1846 N N     . PHE   C 69  ? 0.4350 0.2904 0.3266 -0.1266 -0.0097 -0.0027 69  PHE   C N     
1847 C CA    . PHE   C 69  ? 0.4194 0.2791 0.3164 -0.1056 -0.0001 -0.0025 69  PHE   C CA    
1848 C C     . PHE   C 69  ? 0.4212 0.2712 0.3187 -0.1013 0.0100  -0.0007 69  PHE   C C     
1849 O O     . PHE   C 69  ? 0.4217 0.2868 0.3388 -0.1090 0.0093  0.0037  69  PHE   C O     
1850 C CB    . PHE   C 69  ? 0.3867 0.2816 0.3138 -0.0956 -0.0033 0.0019  69  PHE   C CB    
1851 C CG    . PHE   C 69  ? 0.3767 0.2727 0.3057 -0.0766 0.0064  0.0016  69  PHE   C CG    
1852 C CD1   . PHE   C 69  ? 0.3841 0.2613 0.2917 -0.0653 0.0118  -0.0020 69  PHE   C CD1   
1853 C CD2   . PHE   C 69  ? 0.3612 0.2750 0.3114 -0.0711 0.0108  0.0051  69  PHE   C CD2   
1854 C CE1   . PHE   C 69  ? 0.3738 0.2538 0.2845 -0.0493 0.0191  -0.0008 69  PHE   C CE1   
1855 C CE2   . PHE   C 69  ? 0.3474 0.2612 0.2958 -0.0560 0.0181  0.0049  69  PHE   C CE2   
1856 C CZ    . PHE   C 69  ? 0.3667 0.2643 0.2961 -0.0456 0.0213  0.0026  69  PHE   C CZ    
1857 N N     . SER   C 70  ? 0.4189 0.2460 0.2967 -0.0882 0.0195  -0.0030 70  SER   C N     
1858 C CA    . SER   C 70  ? 0.4227 0.2412 0.2993 -0.0801 0.0290  0.0003  70  SER   C CA    
1859 C C     . SER   C 70  ? 0.4240 0.2328 0.2899 -0.0608 0.0359  0.0000  70  SER   C C     
1860 O O     . SER   C 70  ? 0.4322 0.2270 0.2830 -0.0561 0.0368  -0.0041 70  SER   C O     
1861 C CB    . SER   C 70  ? 0.4603 0.2499 0.3200 -0.0928 0.0328  0.0001  70  SER   C CB    
1862 O OG    . SER   C 70  ? 0.4788 0.2350 0.3102 -0.0983 0.0337  -0.0061 70  SER   C OG    
1863 N N     . ALA   C 71  ? 0.4300 0.2468 0.3036 -0.0500 0.0410  0.0050  71  ALA   C N     
1864 C CA    . ALA   C 71  ? 0.4363 0.2499 0.3049 -0.0320 0.0460  0.0073  71  ALA   C CA    
1865 C C     . ALA   C 71  ? 0.4751 0.2753 0.3363 -0.0271 0.0528  0.0135  71  ALA   C C     
1866 O O     . ALA   C 71  ? 0.4978 0.3094 0.3677 -0.0328 0.0530  0.0169  71  ALA   C O     
1867 C CB    . ALA   C 71  ? 0.4058 0.2512 0.2944 -0.0235 0.0418  0.0080  71  ALA   C CB    
1868 N N     . TYR   C 72  ? 0.4912 0.2668 0.3364 -0.0164 0.0591  0.0158  72  TYR   C N     
1869 C CA    . TYR   C 72  ? 0.5030 0.2603 0.3383 -0.0116 0.0655  0.0233  72  TYR   C CA    
1870 C C     . TYR   C 72  ? 0.4861 0.2469 0.3228 0.0077  0.0677  0.0296  72  TYR   C C     
1871 O O     . TYR   C 72  ? 0.4577 0.2193 0.2955 0.0162  0.0682  0.0265  72  TYR   C O     
1872 C CB    . TYR   C 72  ? 0.5440 0.2613 0.3584 -0.0184 0.0720  0.0223  72  TYR   C CB    
1873 C CG    . TYR   C 72  ? 0.5555 0.2667 0.3672 -0.0395 0.0689  0.0165  72  TYR   C CG    
1874 C CD1   . TYR   C 72  ? 0.5734 0.2845 0.3823 -0.0484 0.0639  0.0077  72  TYR   C CD1   
1875 C CD2   . TYR   C 72  ? 0.5660 0.2730 0.3782 -0.0516 0.0704  0.0206  72  TYR   C CD2   
1876 C CE1   . TYR   C 72  ? 0.5809 0.2899 0.3892 -0.0690 0.0587  0.0036  72  TYR   C CE1   
1877 C CE2   . TYR   C 72  ? 0.5696 0.2757 0.3837 -0.0718 0.0664  0.0164  72  TYR   C CE2   
1878 C CZ    . TYR   C 72  ? 0.5799 0.2868 0.3921 -0.0808 0.0599  0.0081  72  TYR   C CZ    
1879 O OH    . TYR   C 72  ? 0.5902 0.2985 0.4052 -0.1017 0.0538  0.0050  72  TYR   C OH    
1880 N N     . THR   C 73  ? 0.4924 0.2552 0.3285 0.0133  0.0692  0.0390  73  THR   C N     
1881 C CA    . THR   C 73  ? 0.5074 0.2753 0.3457 0.0302  0.0696  0.0482  73  THR   C CA    
1882 C C     . THR   C 73  ? 0.5453 0.2852 0.3694 0.0342  0.0759  0.0583  73  THR   C C     
1883 O O     . THR   C 73  ? 0.5564 0.2866 0.3728 0.0229  0.0777  0.0601  73  THR   C O     
1884 C CB    . THR   C 73  ? 0.4745 0.2763 0.3254 0.0322  0.0626  0.0515  73  THR   C CB    
1885 O OG1   . THR   C 73  ? 0.4680 0.2714 0.3145 0.0212  0.0631  0.0535  73  THR   C OG1   
1886 C CG2   . THR   C 73  ? 0.4587 0.2864 0.3249 0.0300  0.0569  0.0428  73  THR   C CG2   
1887 N N     . ARG   C 74  ? 0.5496 0.2770 0.3721 0.0505  0.0799  0.0655  74  ARG   C N     
1888 C CA    . ARG   C 74  ? 0.6097 0.3170 0.4236 0.0590  0.0844  0.0790  74  ARG   C CA    
1889 C C     . ARG   C 74  ? 0.6067 0.3308 0.4331 0.0782  0.0816  0.0897  74  ARG   C C     
1890 O O     . ARG   C 74  ? 0.5457 0.2950 0.3861 0.0828  0.0770  0.0853  74  ARG   C O     
1891 C CB    . ARG   C 74  ? 0.6373 0.2994 0.4344 0.0563  0.0951  0.0775  74  ARG   C CB    
1892 C CG    . ARG   C 74  ? 0.6521 0.2965 0.4478 0.0655  0.1022  0.0705  74  ARG   C CG    
1893 C CD    . ARG   C 74  ? 0.6987 0.2959 0.4748 0.0612  0.1136  0.0653  74  ARG   C CD    
1894 N NE    . ARG   C 74  ? 0.7286 0.3030 0.5037 0.0803  0.1244  0.0690  74  ARG   C NE    
1895 C CZ    . ARG   C 74  ? 0.7394 0.3049 0.5201 0.0984  0.1293  0.0846  74  ARG   C CZ    
1896 N NH1   . ARG   C 74  ? 0.7396 0.3151 0.5237 0.0998  0.1235  0.0992  74  ARG   C NH1   
1897 N NH2   . ARG   C 74  ? 0.7584 0.3056 0.5416 0.1159  0.1404  0.0865  74  ARG   C NH2   
1898 N N     . SER   C 75  ? 0.6522 0.3640 0.4744 0.0881  0.0834  0.1051  75  SER   C N     
1899 C CA    . SER   C 75  ? 0.6658 0.3900 0.5008 0.1070  0.0810  0.1188  75  SER   C CA    
1900 C C     . SER   C 75  ? 0.7015 0.3882 0.5313 0.1200  0.0927  0.1271  75  SER   C C     
1901 O O     . SER   C 75  ? 0.7392 0.3958 0.5530 0.1140  0.0983  0.1302  75  SER   C O     
1902 C CB    . SER   C 75  ? 0.6832 0.4305 0.5193 0.1074  0.0707  0.1321  75  SER   C CB    
1903 O OG    . SER   C 75  ? 0.6989 0.4640 0.5510 0.1246  0.0659  0.1456  75  SER   C OG    
1904 N N     . GLN   C 76  ? 0.6986 0.3872 0.5431 0.1378  0.0973  0.1310  76  GLN   C N     
1905 C CA    . GLN   C 76  ? 0.7300 0.3855 0.5742 0.1543  0.1096  0.1410  76  GLN   C CA    
1906 C C     . GLN   C 76  ? 0.7319 0.4053 0.5931 0.1720  0.1038  0.1640  76  GLN   C C     
1907 O O     . GLN   C 76  ? 0.7460 0.3968 0.6132 0.1891  0.1142  0.1741  76  GLN   C O     
1908 C CB    . GLN   C 76  ? 0.7309 0.3676 0.5765 0.1611  0.1228  0.1286  76  GLN   C CB    
1909 C CG    . GLN   C 76  ? 0.7203 0.3862 0.5911 0.1774  0.1226  0.1321  76  GLN   C CG    
1910 C CD    . GLN   C 76  ? 0.7396 0.3828 0.6077 0.1838  0.1383  0.1198  76  GLN   C CD    
1911 O OE1   . GLN   C 76  ? 0.8091 0.4093 0.6642 0.1896  0.1534  0.1185  76  GLN   C OE1   
1912 N NE2   . GLN   C 76  ? 0.7210 0.3906 0.5996 0.1825  0.1359  0.1105  76  GLN   C NE2   
1913 N N     . GLY   C 77  ? 0.7083 0.4215 0.5779 0.1688  0.0879  0.1721  77  GLY   C N     
1914 C CA    . GLY   C 77  ? 0.6988 0.4323 0.5844 0.1840  0.0798  0.1949  77  GLY   C CA    
1915 C C     . GLY   C 77  ? 0.6879 0.4434 0.6025 0.2018  0.0810  0.1994  77  GLY   C C     
1916 O O     . GLY   C 77  ? 0.6750 0.4265 0.5945 0.2027  0.0900  0.1845  77  GLY   C O     
1917 N N     . GLY   C 78  ? 0.7001 0.4814 0.6339 0.2147  0.0711  0.2209  78  GLY   C N     
1918 C CA    . GLY   C 78  ? 0.6986 0.5102 0.6647 0.2306  0.0692  0.2289  78  GLY   C CA    
1919 C C     . GLY   C 78  ? 0.6805 0.5329 0.6558 0.2192  0.0574  0.2172  78  GLY   C C     
1920 O O     . GLY   C 78  ? 0.6953 0.5557 0.6526 0.2000  0.0487  0.2054  78  GLY   C O     
1921 N N     . SER   C 79  ? 0.6859 0.5633 0.6905 0.2317  0.0585  0.2207  79  SER   C N     
1922 C CA    . SER   C 79  ? 0.6645 0.5797 0.6819 0.2229  0.0490  0.2108  79  SER   C CA    
1923 C C     . SER   C 79  ? 0.6697 0.5677 0.6723 0.2114  0.0595  0.1854  79  SER   C C     
1924 O O     . SER   C 79  ? 0.7375 0.6016 0.7328 0.2179  0.0766  0.1786  79  SER   C O     
1925 C CB    . SER   C 79  ? 0.6492 0.5970 0.7055 0.2404  0.0475  0.2256  79  SER   C CB    
1926 O OG    . SER   C 79  ? 0.6260 0.5921 0.6964 0.2382  0.0513  0.2125  79  SER   C OG    
1927 N N     . LYS   C 80  ? 0.6204 0.5406 0.6184 0.1946  0.0494  0.1721  80  LYS   C N     
1928 C CA    . LYS   C 80  ? 0.5955 0.5033 0.5799 0.1820  0.0561  0.1501  80  LYS   C CA    
1929 C C     . LYS   C 80  ? 0.6071 0.4722 0.5634 0.1750  0.0662  0.1409  80  LYS   C C     
1930 O O     . LYS   C 80  ? 0.5985 0.4383 0.5467 0.1753  0.0795  0.1291  80  LYS   C O     
1931 C CB    . LYS   C 80  ? 0.5983 0.5154 0.6026 0.1917  0.0652  0.1458  80  LYS   C CB    
1932 C CG    . LYS   C 80  ? 0.5795 0.5419 0.6112 0.1931  0.0539  0.1515  80  LYS   C CG    
1933 C CD    . LYS   C 80  ? 0.5646 0.5366 0.6184 0.2043  0.0648  0.1502  80  LYS   C CD    
1934 C CE    . LYS   C 80  ? 0.6006 0.5974 0.6874 0.2223  0.0642  0.1700  80  LYS   C CE    
1935 N NZ    . LYS   C 80  ? 0.6690 0.6432 0.7597 0.2405  0.0747  0.1841  80  LYS   C NZ    
1936 N N     . PRO   C 81  ? 0.5875 0.4432 0.5264 0.1663  0.0602  0.1453  81  PRO   C N     
1937 C CA    . PRO   C 81  ? 0.6021 0.4164 0.5184 0.1627  0.0702  0.1425  81  PRO   C CA    
1938 C C     . PRO   C 81  ? 0.5843 0.3803 0.4811 0.1448  0.0745  0.1229  81  PRO   C C     
1939 O O     . PRO   C 81  ? 0.6198 0.3805 0.4989 0.1411  0.0833  0.1203  81  PRO   C O     
1940 C CB    . PRO   C 81  ? 0.6284 0.4470 0.5360 0.1592  0.0605  0.1565  81  PRO   C CB    
1941 C CG    . PRO   C 81  ? 0.5920 0.4497 0.5051 0.1486  0.0456  0.1531  81  PRO   C CG    
1942 C CD    . PRO   C 81  ? 0.5689 0.4521 0.5076 0.1590  0.0440  0.1535  81  PRO   C CD    
1943 N N     . LEU   C 82  ? 0.5212 0.3402 0.4221 0.1337  0.0683  0.1103  82  LEU   C N     
1944 C CA    . LEU   C 82  ? 0.5129 0.3224 0.3991 0.1158  0.0688  0.0949  82  LEU   C CA    
1945 C C     . LEU   C 82  ? 0.5144 0.2973 0.3930 0.1155  0.0804  0.0834  82  LEU   C C     
1946 O O     . LEU   C 82  ? 0.4789 0.2660 0.3677 0.1257  0.0853  0.0822  82  LEU   C O     
1947 C CB    . LEU   C 82  ? 0.4812 0.3243 0.3760 0.1052  0.0581  0.0873  82  LEU   C CB    
1948 C CG    . LEU   C 82  ? 0.4861 0.3250 0.3696 0.0868  0.0569  0.0753  82  LEU   C CG    
1949 C CD1   . LEU   C 82  ? 0.5007 0.3337 0.3717 0.0791  0.0548  0.0808  82  LEU   C CD1   
1950 C CD2   . LEU   C 82  ? 0.4502 0.3180 0.3456 0.0789  0.0497  0.0658  82  LEU   C CD2   
1951 N N     . VAL   C 83  ? 0.5323 0.2866 0.3916 0.1032  0.0851  0.0760  83  VAL   C N     
1952 C CA    . VAL   C 83  ? 0.5490 0.2776 0.3954 0.0969  0.0935  0.0629  83  VAL   C CA    
1953 C C     . VAL   C 83  ? 0.5442 0.2841 0.3866 0.0769  0.0859  0.0517  83  VAL   C C     
1954 O O     . VAL   C 83  ? 0.5273 0.2747 0.3685 0.0675  0.0803  0.0545  83  VAL   C O     
1955 C CB    . VAL   C 83  ? 0.5896 0.2731 0.4179 0.0997  0.1055  0.0650  83  VAL   C CB    
1956 C CG1   . VAL   C 83  ? 0.6076 0.2600 0.4169 0.0900  0.1138  0.0503  83  VAL   C CG1   
1957 C CG2   . VAL   C 83  ? 0.6106 0.2856 0.4479 0.1220  0.1132  0.0787  83  VAL   C CG2   
1958 N N     . VAL   C 84  ? 0.5075 0.2498 0.3488 0.0711  0.0863  0.0402  84  VAL   C N     
1959 C CA    . VAL   C 84  ? 0.4836 0.2390 0.3250 0.0536  0.0786  0.0311  84  VAL   C CA    
1960 C C     . VAL   C 84  ? 0.5059 0.2341 0.3291 0.0430  0.0833  0.0203  84  VAL   C C     
1961 O O     . VAL   C 84  ? 0.5181 0.2334 0.3345 0.0500  0.0903  0.0162  84  VAL   C O     
1962 C CB    . VAL   C 84  ? 0.4496 0.2428 0.3103 0.0549  0.0703  0.0294  84  VAL   C CB    
1963 C CG1   . VAL   C 84  ? 0.4331 0.2391 0.2964 0.0383  0.0631  0.0209  84  VAL   C CG1   
1964 C CG2   . VAL   C 84  ? 0.4335 0.2519 0.3087 0.0625  0.0647  0.0389  84  VAL   C CG2   
1965 N N     . LYS   C 85  ? 0.5091 0.2324 0.3257 0.0252  0.0788  0.0157  85  LYS   C N     
1966 C CA    . LYS   C 85  ? 0.5531 0.2570 0.3536 0.0103  0.0790  0.0054  85  LYS   C CA    
1967 C C     . LYS   C 85  ? 0.5269 0.2616 0.3410 -0.0025 0.0674  0.0016  85  LYS   C C     
1968 O O     . LYS   C 85  ? 0.5282 0.2816 0.3556 -0.0084 0.0620  0.0053  85  LYS   C O     
1969 C CB    . LYS   C 85  ? 0.6076 0.2778 0.3898 -0.0013 0.0832  0.0043  85  LYS   C CB    
1970 C CG    . LYS   C 85  ? 0.6643 0.3037 0.4226 -0.0157 0.0855  -0.0065 85  LYS   C CG    
1971 C CD    . LYS   C 85  ? 0.7223 0.3214 0.4603 -0.0256 0.0919  -0.0075 85  LYS   C CD    
1972 C CE    . LYS   C 85  ? 0.7417 0.3520 0.4892 -0.0402 0.0852  -0.0029 85  LYS   C CE    
1973 N NZ    . LYS   C 85  ? 0.7969 0.3691 0.5261 -0.0508 0.0912  -0.0029 85  LYS   C NZ    
1974 N N     . LEU   C 86  ? 0.5035 0.2420 0.3139 -0.0058 0.0649  -0.0051 86  LEU   C N     
1975 C CA    . LEU   C 86  ? 0.4951 0.2580 0.3163 -0.0182 0.0541  -0.0082 86  LEU   C CA    
1976 C C     . LEU   C 86  ? 0.5202 0.2620 0.3206 -0.0352 0.0516  -0.0158 86  LEU   C C     
1977 O O     . LEU   C 86  ? 0.5518 0.2732 0.3321 -0.0331 0.0570  -0.0214 86  LEU   C O     
1978 C CB    . LEU   C 86  ? 0.4868 0.2743 0.3211 -0.0083 0.0517  -0.0078 86  LEU   C CB    
1979 C CG    . LEU   C 86  ? 0.4803 0.2920 0.3355 0.0067  0.0521  -0.0009 86  LEU   C CG    
1980 C CD1   . LEU   C 86  ? 0.4716 0.3065 0.3393 0.0114  0.0484  -0.0015 86  LEU   C CD1   
1981 C CD2   . LEU   C 86  ? 0.4944 0.3256 0.3660 0.0023  0.0467  0.0032  86  LEU   C CD2   
1982 N N     . VAL   C 87  ? 0.5140 0.2631 0.3200 -0.0524 0.0432  -0.0157 87  VAL   C N     
1983 C CA    . VAL   C 87  ? 0.5476 0.2811 0.3360 -0.0721 0.0374  -0.0218 87  VAL   C CA    
1984 C C     . VAL   C 87  ? 0.5249 0.2926 0.3321 -0.0798 0.0244  -0.0202 87  VAL   C C     
1985 O O     . VAL   C 87  ? 0.4780 0.2751 0.3130 -0.0802 0.0190  -0.0143 87  VAL   C O     
1986 C CB    . VAL   C 87  ? 0.5726 0.2883 0.3543 -0.0879 0.0368  -0.0217 87  VAL   C CB    
1987 C CG1   . VAL   C 87  ? 0.5995 0.2961 0.3593 -0.1100 0.0300  -0.0286 87  VAL   C CG1   
1988 C CG2   . VAL   C 87  ? 0.5967 0.2827 0.3659 -0.0783 0.0495  -0.0202 87  VAL   C CG2   
1989 N N     . ASN   C 88  ? 0.5267 0.2890 0.3177 -0.0848 0.0207  -0.0249 88  ASN   C N     
1990 C CA    . ASN   C 88  ? 0.5112 0.3011 0.3153 -0.0929 0.0079  -0.0225 88  ASN   C CA    
1991 C C     . ASN   C 88  ? 0.5474 0.3182 0.3241 -0.1133 0.0004  -0.0279 88  ASN   C C     
1992 O O     . ASN   C 88  ? 0.5793 0.3232 0.3245 -0.1128 0.0065  -0.0350 88  ASN   C O     
1993 C CB    . ASN   C 88  ? 0.4859 0.2917 0.2974 -0.0774 0.0103  -0.0211 88  ASN   C CB    
1994 C CG    . ASN   C 88  ? 0.4378 0.2632 0.2753 -0.0597 0.0158  -0.0160 88  ASN   C CG    
1995 O OD1   . ASN   C 88  ? 0.3908 0.2444 0.2565 -0.0600 0.0097  -0.0107 88  ASN   C OD1   
1996 N ND2   . ASN   C 88  ? 0.4415 0.2519 0.2697 -0.0447 0.0274  -0.0173 88  ASN   C ND2   
1997 N N     . ASP   C 89  ? 0.5617 0.3461 0.3500 -0.1316 -0.0123 -0.0244 89  ASP   C N     
1998 C CA    . ASP   C 89  ? 0.5927 0.3650 0.3589 -0.1548 -0.0235 -0.0277 89  ASP   C CA    
1999 C C     . ASP   C 89  ? 0.6331 0.3562 0.3552 -0.1616 -0.0141 -0.0388 89  ASP   C C     
2000 O O     . ASP   C 89  ? 0.6422 0.3439 0.3311 -0.1675 -0.0138 -0.0460 89  ASP   C O     
2001 C CB    . ASP   C 89  ? 0.6001 0.3932 0.3680 -0.1579 -0.0348 -0.0245 89  ASP   C CB    
2002 C CG    . ASP   C 89  ? 0.6374 0.4307 0.3910 -0.1834 -0.0516 -0.0240 89  ASP   C CG    
2003 O OD1   . ASP   C 89  ? 0.6667 0.4729 0.4387 -0.1975 -0.0611 -0.0191 89  ASP   C OD1   
2004 O OD2   . ASP   C 89  ? 0.6463 0.4289 0.3716 -0.1892 -0.0554 -0.0276 89  ASP   C OD2   
2005 N N     . GLY   C 90  ? 0.6455 0.3490 0.3666 -0.1583 -0.0041 -0.0402 90  GLY   C N     
2006 C CA    . GLY   C 90  ? 0.6877 0.3422 0.3709 -0.1644 0.0063  -0.0499 90  GLY   C CA    
2007 C C     . GLY   C 90  ? 0.7005 0.3272 0.3613 -0.1445 0.0237  -0.0562 90  GLY   C C     
2008 O O     . GLY   C 90  ? 0.7306 0.3139 0.3606 -0.1470 0.0348  -0.0643 90  GLY   C O     
2009 N N     . VAL   C 91  ? 0.6617 0.3121 0.3395 -0.1245 0.0274  -0.0521 91  VAL   C N     
2010 C CA    . VAL   C 91  ? 0.6692 0.2991 0.3314 -0.1050 0.0438  -0.0563 91  VAL   C CA    
2011 C C     . VAL   C 91  ? 0.6390 0.2804 0.3278 -0.0832 0.0527  -0.0488 91  VAL   C C     
2012 O O     . VAL   C 91  ? 0.5969 0.2766 0.3184 -0.0765 0.0457  -0.0406 91  VAL   C O     
2013 C CB    . VAL   C 91  ? 0.6590 0.3066 0.3195 -0.0998 0.0415  -0.0566 91  VAL   C CB    
2014 C CG1   . VAL   C 91  ? 0.6720 0.3042 0.3234 -0.0779 0.0599  -0.0593 91  VAL   C CG1   
2015 C CG2   . VAL   C 91  ? 0.6870 0.3238 0.3183 -0.1227 0.0311  -0.0629 91  VAL   C CG2   
2016 N N     . THR   C 92  ? 0.6726 0.2797 0.3459 -0.0725 0.0682  -0.0515 92  THR   C N     
2017 C CA    . THR   C 92  ? 0.6609 0.2723 0.3542 -0.0545 0.0760  -0.0434 92  THR   C CA    
2018 C C     . THR   C 92  ? 0.6491 0.2657 0.3483 -0.0313 0.0869  -0.0413 92  THR   C C     
2019 O O     . THR   C 92  ? 0.6991 0.2867 0.3740 -0.0272 0.0987  -0.0484 92  THR   C O     
2020 C CB    . THR   C 92  ? 0.7043 0.2735 0.3779 -0.0583 0.0855  -0.0459 92  THR   C CB    
2021 O OG1   . THR   C 92  ? 0.7207 0.2926 0.3923 -0.0823 0.0731  -0.0475 92  THR   C OG1   
2022 C CG2   . THR   C 92  ? 0.6940 0.2660 0.3860 -0.0418 0.0921  -0.0358 92  THR   C CG2   
2023 N N     . LEU   C 93  ? 0.6126 0.2661 0.3434 -0.0178 0.0831  -0.0321 93  LEU   C N     
2024 C CA    . LEU   C 93  ? 0.6081 0.2711 0.3517 0.0048  0.0923  -0.0270 93  LEU   C CA    
2025 C C     . LEU   C 93  ? 0.6147 0.2752 0.3711 0.0169  0.0968  -0.0180 93  LEU   C C     
2026 O O     . LEU   C 93  ? 0.5932 0.2718 0.3644 0.0112  0.0877  -0.0128 93  LEU   C O     
2027 C CB    . LEU   C 93  ? 0.5781 0.2841 0.3464 0.0088  0.0832  -0.0230 93  LEU   C CB    
2028 C CG    . LEU   C 93  ? 0.5696 0.2950 0.3581 0.0300  0.0893  -0.0159 93  LEU   C CG    
2029 C CD1   . LEU   C 93  ? 0.6250 0.3308 0.3993 0.0412  0.1041  -0.0195 93  LEU   C CD1   
2030 C CD2   . LEU   C 93  ? 0.5298 0.2976 0.3441 0.0300  0.0780  -0.0119 93  LEU   C CD2   
2031 N N     . GLU   C 94  ? 0.6464 0.2853 0.3976 0.0339  0.1110  -0.0156 94  GLU   C N     
2032 C CA    . GLU   C 94  ? 0.6563 0.2968 0.4222 0.0490  0.1149  -0.0042 94  GLU   C CA    
2033 C C     . GLU   C 94  ? 0.6110 0.2766 0.3984 0.0690  0.1183  0.0029  94  GLU   C C     
2034 O O     . GLU   C 94  ? 0.6078 0.2622 0.3880 0.0771  0.1290  -0.0012 94  GLU   C O     
2035 C CB    . GLU   C 94  ? 0.7209 0.3162 0.4678 0.0533  0.1279  -0.0039 94  GLU   C CB    
2036 C CG    . GLU   C 94  ? 0.7541 0.3538 0.5169 0.0667  0.1289  0.0104  94  GLU   C CG    
2037 C CD    . GLU   C 94  ? 0.8429 0.3983 0.5897 0.0714  0.1412  0.0135  94  GLU   C CD    
2038 O OE1   . GLU   C 94  ? 0.8622 0.4126 0.6072 0.0624  0.1360  0.0183  94  GLU   C OE1   
2039 O OE2   . GLU   C 94  ? 0.8977 0.4233 0.6345 0.0839  0.1566  0.0114  94  GLU   C OE2   
2040 N N     . LEU   C 95  ? 0.5769 0.2749 0.3891 0.0760  0.1099  0.0136  95  LEU   C N     
2041 C CA    . LEU   C 95  ? 0.5432 0.2671 0.3786 0.0939  0.1111  0.0229  95  LEU   C CA    
2042 C C     . LEU   C 95  ? 0.5567 0.2755 0.4003 0.1071  0.1138  0.0359  95  LEU   C C     
2043 O O     . LEU   C 95  ? 0.5227 0.2407 0.3639 0.0998  0.1072  0.0398  95  LEU   C O     
2044 C CB    . LEU   C 95  ? 0.5011 0.2678 0.3569 0.0885  0.0968  0.0244  95  LEU   C CB    
2045 C CG    . LEU   C 95  ? 0.4952 0.2733 0.3482 0.0767  0.0921  0.0146  95  LEU   C CG    
2046 C CD1   . LEU   C 95  ? 0.4559 0.2737 0.3312 0.0732  0.0791  0.0175  95  LEU   C CD1   
2047 C CD2   . LEU   C 95  ? 0.5092 0.2791 0.3568 0.0849  0.1029  0.0109  95  LEU   C CD2   
2048 N N     . THR   C 96  ? 0.5632 0.2810 0.4180 0.1264  0.1236  0.0433  96  THR   C N     
2049 C CA    . THR   C 96  ? 0.5848 0.3068 0.4549 0.1428  0.1250  0.0592  96  THR   C CA    
2050 C C     . THR   C 96  ? 0.5651 0.3213 0.4633 0.1580  0.1243  0.0678  96  THR   C C     
2051 O O     . THR   C 96  ? 0.5598 0.3287 0.4626 0.1572  0.1266  0.0608  96  THR   C O     
2052 C CB    . THR   C 96  ? 0.6356 0.3124 0.4909 0.1526  0.1414  0.0611  96  THR   C CB    
2053 O OG1   . THR   C 96  ? 0.6598 0.3243 0.5139 0.1627  0.1563  0.0554  96  THR   C OG1   
2054 C CG2   . THR   C 96  ? 0.6654 0.3033 0.4911 0.1363  0.1442  0.0512  96  THR   C CG2   
2055 N N     . ARG   C 97  ? 0.5779 0.3481 0.4950 0.1719  0.1215  0.0843  97  ARG   C N     
2056 C CA    . ARG   C 97  ? 0.5653 0.3682 0.5122 0.1871  0.1208  0.0951  97  ARG   C CA    
2057 C C     . ARG   C 97  ? 0.5834 0.3722 0.5344 0.2006  0.1393  0.0920  97  ARG   C C     
2058 O O     . ARG   C 97  ? 0.5880 0.4067 0.5617 0.2076  0.1390  0.0957  97  ARG   C O     
2059 C CB    . ARG   C 97  ? 0.5664 0.3833 0.5317 0.2001  0.1147  0.1153  97  ARG   C CB    
2060 C CG    . ARG   C 97  ? 0.6021 0.3830 0.5611 0.2136  0.1272  0.1245  97  ARG   C CG    
2061 C CD    . ARG   C 97  ? 0.5970 0.3957 0.5740 0.2246  0.1177  0.1464  97  ARG   C CD    
2062 N NE    . ARG   C 97  ? 0.6360 0.3943 0.6015 0.2339  0.1290  0.1540  97  ARG   C NE    
2063 C CZ    . ARG   C 97  ? 0.6571 0.3998 0.6092 0.2298  0.1235  0.1624  97  ARG   C CZ    
2064 N NH1   . ARG   C 97  ? 0.7073 0.4058 0.6462 0.2370  0.1377  0.1649  97  ARG   C NH1   
2065 N NH2   . ARG   C 97  ? 0.6303 0.3975 0.5797 0.2180  0.1055  0.1677  97  ARG   C NH2   
2066 N N     . ASP   C 98  ? 0.6323 0.3755 0.5616 0.2042  0.1560  0.0858  98  ASP   C N     
2067 C CA    . ASP   C 98  ? 0.6673 0.3886 0.5940 0.2165  0.1773  0.0807  98  ASP   C CA    
2068 C C     . ASP   C 98  ? 0.6661 0.3779 0.5711 0.2029  0.1823  0.0619  98  ASP   C C     
2069 O O     . ASP   C 98  ? 0.7158 0.4096 0.6159 0.2123  0.2009  0.0569  98  ASP   C O     
2070 C CB    . ASP   C 98  ? 0.7225 0.3936 0.6315 0.2254  0.1943  0.0810  98  ASP   C CB    
2071 C CG    . ASP   C 98  ? 0.7454 0.4182 0.6737 0.2413  0.1926  0.1011  98  ASP   C CG    
2072 O OD1   . ASP   C 98  ? 0.7307 0.4419 0.6932 0.2551  0.1868  0.1172  98  ASP   C OD1   
2073 O OD2   . ASP   C 98  ? 0.7784 0.4141 0.6873 0.2390  0.1968  0.1012  98  ASP   C OD2   
2074 N N     . GLY   C 99  ? 0.6407 0.3630 0.5327 0.1817  0.1672  0.0522  99  GLY   C N     
2075 C CA    . GLY   C 99  ? 0.6515 0.3724 0.5263 0.1676  0.1676  0.0372  99  GLY   C CA    
2076 C C     . GLY   C 99  ? 0.6684 0.3660 0.5133 0.1460  0.1600  0.0253  99  GLY   C C     
2077 O O     . GLY   C 99  ? 0.6633 0.3691 0.5114 0.1382  0.1469  0.0295  99  GLY   C O     
2078 N N     . ALA   C 100 ? 0.6655 0.3331 0.4810 0.1362  0.1689  0.0113  100 ALA   C N     
2079 C CA    . ALA   C 100 ? 0.6640 0.3223 0.4565 0.1129  0.1579  0.0002  100 ALA   C CA    
2080 C C     . ALA   C 100 ? 0.7030 0.3121 0.4571 0.1038  0.1703  -0.0132 100 ALA   C C     
2081 O O     . ALA   C 100 ? 0.7219 0.3091 0.4647 0.1139  0.1881  -0.0175 100 ALA   C O     
2082 C CB    . ALA   C 100 ? 0.6310 0.3240 0.4325 0.1035  0.1463  -0.0026 100 ALA   C CB    
2083 N N     . SER   C 101 ? 0.6966 0.2919 0.4315 0.0831  0.1601  -0.0202 101 SER   C N     
2084 C CA    . SER   C 101 ? 0.7449 0.2961 0.4408 0.0684  0.1672  -0.0342 101 SER   C CA    
2085 C C     . SER   C 101 ? 0.7198 0.2815 0.4043 0.0426  0.1493  -0.0410 101 SER   C C     
2086 O O     . SER   C 101 ? 0.6640 0.2563 0.3699 0.0367  0.1337  -0.0343 101 SER   C O     
2087 C CB    . SER   C 101 ? 0.7853 0.2945 0.4679 0.0721  0.1780  -0.0336 101 SER   C CB    
2088 O OG    . SER   C 101 ? 0.7703 0.2897 0.4633 0.0632  0.1643  -0.0272 101 SER   C OG    
2089 N N     . ILE   C 102 ? 0.7531 0.2867 0.4030 0.0272  0.1524  -0.0540 102 ILE   C N     
2090 C CA    . ILE   C 102 ? 0.7546 0.2963 0.3914 0.0021  0.1357  -0.0602 102 ILE   C CA    
2091 C C     . ILE   C 102 ? 0.7959 0.2899 0.3955 -0.0154 0.1394  -0.0711 102 ILE   C C     
2092 O O     . ILE   C 102 ? 0.8434 0.3004 0.4105 -0.0160 0.1537  -0.0816 102 ILE   C O     
2093 C CB    . ILE   C 102 ? 0.7478 0.3048 0.3758 -0.0026 0.1332  -0.0648 102 ILE   C CB    
2094 C CG1   . ILE   C 102 ? 0.7197 0.3154 0.3798 0.0162  0.1345  -0.0555 102 ILE   C CG1   
2095 C CG2   . ILE   C 102 ? 0.7408 0.3114 0.3607 -0.0279 0.1132  -0.0678 102 ILE   C CG2   
2096 C CD1   . ILE   C 102 ? 0.6731 0.3141 0.3708 0.0169  0.1177  -0.0448 102 ILE   C CD1   
2097 N N     . ASN   C 103 ? 0.7935 0.2880 0.3969 -0.0305 0.1273  -0.0691 103 ASN   C N     
2098 C CA    . ASN   C 103 ? 0.8620 0.3125 0.4328 -0.0495 0.1291  -0.0786 103 ASN   C CA    
2099 C C     . ASN   C 103 ? 0.9122 0.3117 0.4616 -0.0362 0.1522  -0.0834 103 ASN   C C     
2100 O O     . ASN   C 103 ? 0.9486 0.3074 0.4604 -0.0434 0.1631  -0.0964 103 ASN   C O     
2101 C CB    . ASN   C 103 ? 0.8814 0.3224 0.4207 -0.0736 0.1205  -0.0901 103 ASN   C CB    
2102 C CG    . ASN   C 103 ? 0.8349 0.3215 0.3944 -0.0887 0.0974  -0.0846 103 ASN   C CG    
2103 O OD1   . ASN   C 103 ? 0.8020 0.3158 0.3912 -0.0907 0.0866  -0.0755 103 ASN   C OD1   
2104 N ND2   . ASN   C 103 ? 0.8333 0.3247 0.3738 -0.1015 0.0902  -0.0904 103 ASN   C ND2   
2105 N N     . GLY   C 104 ? 0.9092 0.3143 0.4838 -0.0133 0.1610  -0.0724 104 GLY   C N     
2106 C CA    . GLY   C 104 ? 0.9754 0.3358 0.5377 0.0024  0.1825  -0.0732 104 GLY   C CA    
2107 C C     . GLY   C 104 ? 1.0132 0.3529 0.5622 0.0200  0.2035  -0.0791 104 GLY   C C     
2108 O O     . GLY   C 104 ? 1.0760 0.3700 0.6089 0.0299  0.2230  -0.0825 104 GLY   C O     
2109 N N     . LYS   C 105 ? 0.9835 0.3523 0.5376 0.0233  0.2014  -0.0808 105 LYS   C N     
2110 C CA    . LYS   C 105 ? 1.0154 0.3720 0.5636 0.0423  0.2224  -0.0840 105 LYS   C CA    
2111 C C     . LYS   C 105 ? 0.9511 0.3622 0.5435 0.0621  0.2177  -0.0696 105 LYS   C C     
2112 O O     . LYS   C 105 ? 0.9190 0.3722 0.5273 0.0525  0.1987  -0.0659 105 LYS   C O     
2113 C CB    . LYS   C 105 ? 1.0693 0.4027 0.5755 0.0262  0.2273  -0.1007 105 LYS   C CB    
2114 C CG    . LYS   C 105 ? 1.1550 0.4491 0.6388 0.0419  0.2564  -0.1091 105 LYS   C CG    
2115 C CD    . LYS   C 105 ? 1.2309 0.4930 0.6646 0.0253  0.2647  -0.1273 105 LYS   C CD    
2116 C CE    . LYS   C 105 ? 1.3110 0.5189 0.6959 0.0004  0.2652  -0.1433 105 LYS   C CE    
2117 N NZ    . LYS   C 105 ? 1.3816 0.5335 0.7513 0.0105  0.2875  -0.1484 105 LYS   C NZ    
2118 N N     . ALA   C 106 ? 0.9582 0.3690 0.5716 0.0888  0.2345  -0.0609 106 ALA   C N     
2119 C CA    . ALA   C 106 ? 0.9093 0.3694 0.5634 0.1075  0.2319  -0.0475 106 ALA   C CA    
2120 C C     . ALA   C 106 ? 0.9111 0.3883 0.5581 0.1041  0.2340  -0.0540 106 ALA   C C     
2121 O O     . ALA   C 106 ? 0.9752 0.4164 0.5873 0.0997  0.2495  -0.0671 106 ALA   C O     
2122 C CB    . ALA   C 106 ? 0.9314 0.3825 0.6066 0.1359  0.2513  -0.0372 106 ALA   C CB    
2123 N N     . VAL   C 107 ? 0.8503 0.3799 0.5296 0.1073  0.2203  -0.0445 107 VAL   C N     
2124 C CA    . VAL   C 107 ? 0.8376 0.3901 0.5148 0.1026  0.2186  -0.0479 107 VAL   C CA    
2125 C C     . VAL   C 107 ? 0.8390 0.4317 0.5576 0.1240  0.2228  -0.0346 107 VAL   C C     
2126 O O     . VAL   C 107 ? 0.8367 0.4506 0.5881 0.1365  0.2174  -0.0218 107 VAL   C O     
2127 C CB    . VAL   C 107 ? 0.8190 0.3951 0.4920 0.0790  0.1940  -0.0504 107 VAL   C CB    
2128 C CG1   . VAL   C 107 ? 0.8614 0.4002 0.4918 0.0557  0.1901  -0.0640 107 VAL   C CG1   
2129 C CG2   . VAL   C 107 ? 0.7771 0.3903 0.4846 0.0783  0.1740  -0.0391 107 VAL   C CG2   
2130 N N     . SER   C 108 ? 0.8440 0.4471 0.5600 0.1269  0.2320  -0.0371 108 SER   C N     
2131 C CA    . SER   C 108 ? 0.8031 0.4442 0.5570 0.1449  0.2372  -0.0252 108 SER   C CA    
2132 C C     . SER   C 108 ? 0.7287 0.4190 0.5091 0.1358  0.2130  -0.0178 108 SER   C C     
2133 O O     . SER   C 108 ? 0.7414 0.4510 0.5215 0.1292  0.2100  -0.0191 108 SER   C O     
2134 C CB    . SER   C 108 ? 0.8461 0.4740 0.5845 0.1515  0.2598  -0.0313 108 SER   C CB    
2135 O OG    . SER   C 108 ? 0.8542 0.4789 0.5617 0.1311  0.2532  -0.0415 108 SER   C OG    
2136 N N     . VAL   C 109 ? 0.7111 0.4193 0.5134 0.1356  0.1968  -0.0098 109 VAL   C N     
2137 C CA    . VAL   C 109 ? 0.6451 0.3922 0.4681 0.1250  0.1737  -0.0047 109 VAL   C CA    
2138 C C     . VAL   C 109 ? 0.6232 0.4132 0.4811 0.1344  0.1714  0.0053  109 VAL   C C     
2139 O O     . VAL   C 109 ? 0.5535 0.3709 0.4209 0.1233  0.1560  0.0061  109 VAL   C O     
2140 C CB    . VAL   C 109 ? 0.6472 0.3977 0.4809 0.1231  0.1604  0.0007  109 VAL   C CB    
2141 C CG1   . VAL   C 109 ? 0.6565 0.4146 0.5167 0.1432  0.1661  0.0133  109 VAL   C CG1   
2142 C CG2   . VAL   C 109 ? 0.5847 0.3682 0.4330 0.1097  0.1384  0.0028  109 VAL   C CG2   
2143 N N     . GLU   C 110 ? 0.6312 0.4267 0.5086 0.1540  0.1869  0.0129  110 GLU   C N     
2144 C CA    . GLU   C 110 ? 0.6247 0.4601 0.5356 0.1624  0.1866  0.0226  110 GLU   C CA    
2145 C C     . GLU   C 110 ? 0.6148 0.4542 0.5130 0.1543  0.1920  0.0164  110 GLU   C C     
2146 O O     . GLU   C 110 ? 0.5559 0.4309 0.4798 0.1543  0.1856  0.0233  110 GLU   C O     
2147 C CB    . GLU   C 110 ? 0.6786 0.5191 0.6159 0.1856  0.2019  0.0337  110 GLU   C CB    
2148 C CG    . GLU   C 110 ? 0.6964 0.5467 0.6551 0.1932  0.1912  0.0447  110 GLU   C CG    
2149 C CD    . GLU   C 110 ? 0.7686 0.6069 0.7417 0.2154  0.2085  0.0539  110 GLU   C CD    
2150 O OE1   . GLU   C 110 ? 0.8529 0.6756 0.8240 0.2197  0.2053  0.0582  110 GLU   C OE1   
2151 O OE2   . GLU   C 110 ? 0.8369 0.6808 0.8236 0.2286  0.2260  0.0574  110 GLU   C OE2   
2152 N N     . LYS   C 111 ? 0.6523 0.4547 0.5105 0.1472  0.2041  0.0041  111 LYS   C N     
2153 C CA    . LYS   C 111 ? 0.6637 0.4666 0.5026 0.1362  0.2071  -0.0020 111 LYS   C CA    
2154 C C     . LYS   C 111 ? 0.6141 0.4160 0.4325 0.1136  0.1864  -0.0084 111 LYS   C C     
2155 O O     . LYS   C 111 ? 0.6188 0.4212 0.4198 0.1028  0.1857  -0.0122 111 LYS   C O     
2156 C CB    . LYS   C 111 ? 0.7183 0.4921 0.5325 0.1440  0.2343  -0.0086 111 LYS   C CB    
2157 C CG    . LYS   C 111 ? 0.8007 0.5232 0.5785 0.1461  0.2510  -0.0197 111 LYS   C CG    
2158 N N     . GLY   C 112 ? 0.5632 0.3673 0.3863 0.1063  0.1692  -0.0080 112 GLY   C N     
2159 C CA    . GLY   C 112 ? 0.5488 0.3574 0.3606 0.0865  0.1497  -0.0118 112 GLY   C CA    
2160 C C     . GLY   C 112 ? 0.5792 0.3482 0.3463 0.0724  0.1524  -0.0239 112 GLY   C C     
2161 O O     . GLY   C 112 ? 0.5998 0.3457 0.3399 0.0727  0.1678  -0.0303 112 GLY   C O     
2162 N N     . VAL   C 113 ? 0.5702 0.3299 0.3285 0.0598  0.1388  -0.0272 113 VAL   C N     
2163 C CA    . VAL   C 113 ? 0.6417 0.3620 0.3587 0.0458  0.1409  -0.0384 113 VAL   C CA    
2164 C C     . VAL   C 113 ? 0.6123 0.3429 0.3257 0.0251  0.1189  -0.0392 113 VAL   C C     
2165 O O     . VAL   C 113 ? 0.5623 0.3165 0.3035 0.0250  0.1057  -0.0329 113 VAL   C O     
2166 C CB    . VAL   C 113 ? 0.6822 0.3688 0.3889 0.0539  0.1531  -0.0422 113 VAL   C CB    
2167 C CG1   . VAL   C 113 ? 0.7400 0.3833 0.4023 0.0369  0.1548  -0.0548 113 VAL   C CG1   
2168 C CG2   . VAL   C 113 ? 0.7119 0.3876 0.4228 0.0751  0.1766  -0.0407 113 VAL   C CG2   
2169 N N     . GLN   C 114 ? 0.6271 0.3373 0.3043 0.0077  0.1160  -0.0471 114 GLN   C N     
2170 C CA    . GLN   C 114 ? 0.6155 0.3341 0.2871 -0.0132 0.0954  -0.0472 114 GLN   C CA    
2171 C C     . GLN   C 114 ? 0.6545 0.3331 0.2868 -0.0289 0.0961  -0.0579 114 GLN   C C     
2172 O O     . GLN   C 114 ? 0.6974 0.3435 0.2932 -0.0311 0.1098  -0.0669 114 GLN   C O     
2173 C CB    . GLN   C 114 ? 0.6021 0.3394 0.2692 -0.0221 0.0871  -0.0440 114 GLN   C CB    
2174 C CG    . GLN   C 114 ? 0.5803 0.3346 0.2515 -0.0413 0.0641  -0.0403 114 GLN   C CG    
2175 C CD    . GLN   C 114 ? 0.5702 0.3407 0.2355 -0.0495 0.0562  -0.0355 114 GLN   C CD    
2176 O OE1   . GLN   C 114 ? 0.5332 0.3269 0.2210 -0.0381 0.0595  -0.0286 114 GLN   C OE1   
2177 N NE2   . GLN   C 114 ? 0.6038 0.3638 0.2398 -0.0699 0.0446  -0.0378 114 GLN   C NE2   
2178 N N     . TYR   C 115 ? 0.6330 0.3157 0.2725 -0.0419 0.0807  -0.0568 115 TYR   C N     
2179 C CA    . TYR   C 115 ? 0.6809 0.3314 0.2861 -0.0615 0.0766  -0.0657 115 TYR   C CA    
2180 C C     . TYR   C 115 ? 0.6623 0.3351 0.2741 -0.0825 0.0529  -0.0613 115 TYR   C C     
2181 O O     . TYR   C 115 ? 0.6497 0.3547 0.2991 -0.0800 0.0416  -0.0524 115 TYR   C O     
2182 C CB    . TYR   C 115 ? 0.6911 0.3178 0.2980 -0.0553 0.0854  -0.0685 115 TYR   C CB    
2183 C CG    . TYR   C 115 ? 0.7434 0.3282 0.3090 -0.0750 0.0857  -0.0797 115 TYR   C CG    
2184 C CD1   . TYR   C 115 ? 0.8008 0.3406 0.3249 -0.0743 0.1040  -0.0916 115 TYR   C CD1   
2185 C CD2   . TYR   C 115 ? 0.7447 0.3351 0.3125 -0.0956 0.0676  -0.0787 115 TYR   C CD2   
2186 C CE1   . TYR   C 115 ? 0.8673 0.3656 0.3502 -0.0948 0.1039  -0.1032 115 TYR   C CE1   
2187 C CE2   . TYR   C 115 ? 0.8122 0.3650 0.3422 -0.1164 0.0662  -0.0889 115 TYR   C CE2   
2188 C CZ    . TYR   C 115 ? 0.8658 0.3712 0.3517 -0.1165 0.0840  -0.1017 115 TYR   C CZ    
2189 O OH    . TYR   C 115 ? 0.9194 0.3872 0.3669 -0.1390 0.0815  -0.1123 115 TYR   C OH    
2190 N N     . PRO   C 116 ? 0.6968 0.3526 0.2733 -0.1045 0.0444  -0.0671 116 PRO   C N     
2191 C CA    . PRO   C 116 ? 0.7498 0.3720 0.2786 -0.1099 0.0560  -0.0774 116 PRO   C CA    
2192 C C     . PRO   C 116 ? 0.7488 0.3874 0.2829 -0.0956 0.0649  -0.0733 116 PRO   C C     
2193 O O     . PRO   C 116 ? 0.7167 0.3949 0.2822 -0.0932 0.0525  -0.0621 116 PRO   C O     
2194 C CB    . PRO   C 116 ? 0.7780 0.3953 0.2788 -0.1386 0.0370  -0.0796 116 PRO   C CB    
2195 C CG    . PRO   C 116 ? 0.7611 0.3924 0.2884 -0.1481 0.0217  -0.0748 116 PRO   C CG    
2196 C CD    . PRO   C 116 ? 0.7004 0.3678 0.2806 -0.1268 0.0228  -0.0640 116 PRO   C CD    
2197 N N     . GLN   C 117 ? 0.7982 0.4071 0.3057 -0.0850 0.0876  -0.0816 117 GLN   C N     
2198 C CA    . GLN   C 117 ? 0.8190 0.4407 0.3310 -0.0706 0.0999  -0.0781 117 GLN   C CA    
2199 C C     . GLN   C 117 ? 0.8332 0.4730 0.3322 -0.0855 0.0859  -0.0734 117 GLN   C C     
2200 O O     . GLN   C 117 ? 0.8197 0.4899 0.3445 -0.0749 0.0858  -0.0639 117 GLN   C O     
2201 C CB    . GLN   C 117 ? 0.9000 0.4816 0.3797 -0.0599 0.1278  -0.0892 117 GLN   C CB    
2202 C CG    . GLN   C 117 ? 0.9251 0.5227 0.4223 -0.0387 0.1452  -0.0840 117 GLN   C CG    
2203 C CD    . GLN   C 117 ? 1.0288 0.5865 0.4881 -0.0316 0.1733  -0.0952 117 GLN   C CD    
2204 O OE1   . GLN   C 117 ? 1.0932 0.6091 0.5261 -0.0317 0.1866  -0.1064 117 GLN   C OE1   
2205 N NE2   . GLN   C 117 ? 1.0843 0.6525 0.5393 -0.0255 0.1841  -0.0926 117 GLN   C NE2   
2206 N N     . ASP   C 118 ? 0.9002 0.5228 0.3620 -0.1103 0.0728  -0.0785 118 ASP   C N     
2207 C CA    . ASP   C 118 ? 0.9396 0.5763 0.3842 -0.1274 0.0570  -0.0732 118 ASP   C CA    
2208 C C     . ASP   C 118 ? 0.8759 0.5553 0.3593 -0.1358 0.0296  -0.0589 118 ASP   C C     
2209 O O     . ASP   C 118 ? 0.8722 0.5675 0.3476 -0.1474 0.0160  -0.0513 118 ASP   C O     
2210 C CB    . ASP   C 118 ? 1.0793 0.6756 0.4614 -0.1512 0.0560  -0.0855 118 ASP   C CB    
2211 C CG    . ASP   C 118 ? 1.1734 0.7595 0.5456 -0.1734 0.0372  -0.0889 118 ASP   C CG    
2212 O OD1   . ASP   C 118 ? 1.1531 0.7352 0.5489 -0.1663 0.0399  -0.0909 118 ASP   C OD1   
2213 O OD2   . ASP   C 118 ? 1.2680 0.8503 0.6083 -0.1982 0.0200  -0.0889 118 ASP   C OD2   
2214 N N     . ASP   C 119 ? 0.8262 0.5220 0.3479 -0.1318 0.0213  -0.0549 119 ASP   C N     
2215 C CA    . ASP   C 119 ? 0.7918 0.5200 0.3426 -0.1440 -0.0039 -0.0438 119 ASP   C CA    
2216 C C     . ASP   C 119 ? 0.7045 0.4740 0.3069 -0.1268 -0.0068 -0.0309 119 ASP   C C     
2217 O O     . ASP   C 119 ? 0.6659 0.4415 0.2969 -0.1096 0.0031  -0.0312 119 ASP   C O     
2218 C CB    . ASP   C 119 ? 0.8170 0.5368 0.3738 -0.1542 -0.0118 -0.0473 119 ASP   C CB    
2219 C CG    . ASP   C 119 ? 0.8173 0.5684 0.4012 -0.1696 -0.0372 -0.0363 119 ASP   C CG    
2220 O OD1   . ASP   C 119 ? 0.8296 0.6104 0.4300 -0.1723 -0.0507 -0.0245 119 ASP   C OD1   
2221 O OD2   . ASP   C 119 ? 0.8198 0.5659 0.4102 -0.1788 -0.0432 -0.0384 119 ASP   C OD2   
2222 N N     . PRO   C 120 ? 0.6942 0.4918 0.3100 -0.1312 -0.0204 -0.0190 120 PRO   C N     
2223 C CA    . PRO   C 120 ? 0.6245 0.4594 0.2910 -0.1166 -0.0241 -0.0073 120 PRO   C CA    
2224 C C     . PRO   C 120 ? 0.5886 0.4437 0.2961 -0.1146 -0.0335 -0.0031 120 PRO   C C     
2225 O O     . PRO   C 120 ? 0.5471 0.4209 0.2909 -0.0983 -0.0281 0.0006  120 PRO   C O     
2226 C CB    . PRO   C 120 ? 0.6333 0.4878 0.2995 -0.1260 -0.0385 0.0045  120 PRO   C CB    
2227 C CG    . PRO   C 120 ? 0.6811 0.5174 0.3058 -0.1498 -0.0509 0.0017  120 PRO   C CG    
2228 C CD    . PRO   C 120 ? 0.7237 0.5190 0.3079 -0.1515 -0.0346 -0.0153 120 PRO   C CD    
2229 N N     . ASN   C 121 ? 0.5993 0.4499 0.3001 -0.1316 -0.0465 -0.0039 121 ASN   C N     
2230 C CA    . ASN   C 121 ? 0.5757 0.4384 0.3086 -0.1307 -0.0513 -0.0024 121 ASN   C CA    
2231 C C     . ASN   C 121 ? 0.5932 0.4263 0.3102 -0.1245 -0.0354 -0.0145 121 ASN   C C     
2232 O O     . ASN   C 121 ? 0.6096 0.4265 0.3134 -0.1372 -0.0390 -0.0195 121 ASN   C O     
2233 C CB    . ASN   C 121 ? 0.5893 0.4657 0.3288 -0.1512 -0.0725 0.0046  121 ASN   C CB    
2234 C CG    . ASN   C 121 ? 0.5612 0.4553 0.3395 -0.1495 -0.0765 0.0081  121 ASN   C CG    
2235 O OD1   . ASN   C 121 ? 0.5433 0.4554 0.3566 -0.1329 -0.0699 0.0114  121 ASN   C OD1   
2236 N ND2   . ASN   C 121 ? 0.5968 0.4843 0.3674 -0.1672 -0.0861 0.0067  121 ASN   C ND2   
2237 N N     . TYR   C 122 ? 0.5734 0.4024 0.2971 -0.1044 -0.0184 -0.0175 122 TYR   C N     
2238 C CA    . TYR   C 122 ? 0.5805 0.3806 0.2886 -0.0959 -0.0018 -0.0273 122 TYR   C CA    
2239 C C     . TYR   C 122 ? 0.5592 0.3679 0.2953 -0.0931 -0.0041 -0.0255 122 TYR   C C     
2240 O O     . TYR   C 122 ? 0.5152 0.3549 0.2889 -0.0879 -0.0112 -0.0174 122 TYR   C O     
2241 C CB    . TYR   C 122 ? 0.5584 0.3542 0.2673 -0.0753 0.0163  -0.0292 122 TYR   C CB    
2242 C CG    . TYR   C 122 ? 0.5094 0.3397 0.2601 -0.0600 0.0156  -0.0201 122 TYR   C CG    
2243 C CD1   . TYR   C 122 ? 0.4715 0.3143 0.2524 -0.0487 0.0177  -0.0178 122 TYR   C CD1   
2244 C CD2   . TYR   C 122 ? 0.4901 0.3394 0.2480 -0.0582 0.0123  -0.0139 122 TYR   C CD2   
2245 C CE1   . TYR   C 122 ? 0.4253 0.2976 0.2410 -0.0371 0.0162  -0.0107 122 TYR   C CE1   
2246 C CE2   . TYR   C 122 ? 0.4492 0.3277 0.2439 -0.0460 0.0115  -0.0063 122 TYR   C CE2   
2247 C CZ    . TYR   C 122 ? 0.4244 0.3136 0.2471 -0.0357 0.0135  -0.0055 122 TYR   C CZ    
2248 O OH    . TYR   C 122 ? 0.4354 0.3506 0.2906 -0.0256 0.0124  0.0007  122 TYR   C OH    
2249 N N     . ALA   C 123 ? 0.5845 0.3630 0.3003 -0.0962 0.0036  -0.0334 123 ALA   C N     
2250 C CA    . ALA   C 123 ? 0.5446 0.3247 0.2806 -0.0928 0.0050  -0.0323 123 ALA   C CA    
2251 C C     . ALA   C 123 ? 0.5155 0.3043 0.2733 -0.0698 0.0173  -0.0297 123 ALA   C C     
2252 O O     . ALA   C 123 ? 0.4723 0.2791 0.2583 -0.0648 0.0148  -0.0248 123 ALA   C O     
2253 C CB    . ALA   C 123 ? 0.5920 0.3337 0.2969 -0.1031 0.0105  -0.0410 123 ALA   C CB    
2254 N N     . ILE   C 124 ? 0.5184 0.2936 0.2620 -0.0567 0.0310  -0.0331 124 ILE   C N     
2255 C CA    . ILE   C 124 ? 0.5040 0.2874 0.2679 -0.0358 0.0417  -0.0298 124 ILE   C CA    
2256 C C     . ILE   C 124 ? 0.4975 0.2814 0.2553 -0.0243 0.0518  -0.0301 124 ILE   C C     
2257 O O     . ILE   C 124 ? 0.5419 0.3030 0.2687 -0.0295 0.0579  -0.0363 124 ILE   C O     
2258 C CB    . ILE   C 124 ? 0.5399 0.2980 0.2967 -0.0296 0.0520  -0.0325 124 ILE   C CB    
2259 C CG1   . ILE   C 124 ? 0.5208 0.2935 0.3030 -0.0094 0.0592  -0.0262 124 ILE   C CG1   
2260 C CG2   . ILE   C 124 ? 0.5891 0.3041 0.3072 -0.0318 0.0649  -0.0417 124 ILE   C CG2   
2261 C CD1   . ILE   C 124 ? 0.4948 0.3010 0.3099 -0.0090 0.0483  -0.0192 124 ILE   C CD1   
2262 N N     . ARG   C 125 ? 0.4653 0.2772 0.2535 -0.0102 0.0525  -0.0232 125 ARG   C N     
2263 C CA    . ARG   C 125 ? 0.4464 0.2625 0.2390 0.0052  0.0645  -0.0215 125 ARG   C CA    
2264 C C     . ARG   C 125 ? 0.4242 0.2491 0.2404 0.0213  0.0700  -0.0167 125 ARG   C C     
2265 O O     . ARG   C 125 ? 0.3862 0.2283 0.2233 0.0201  0.0609  -0.0128 125 ARG   C O     
2266 C CB    . ARG   C 125 ? 0.4285 0.2749 0.2396 0.0052  0.0575  -0.0157 125 ARG   C CB    
2267 C CG    . ARG   C 125 ? 0.4595 0.2957 0.2440 -0.0051 0.0576  -0.0187 125 ARG   C CG    
2268 C CD    . ARG   C 125 ? 0.4481 0.3115 0.2506 -0.0035 0.0528  -0.0118 125 ARG   C CD    
2269 N NE    . ARG   C 125 ? 0.4723 0.3274 0.2480 -0.0162 0.0495  -0.0131 125 ARG   C NE    
2270 C CZ    . ARG   C 125 ? 0.4532 0.3277 0.2374 -0.0186 0.0441  -0.0065 125 ARG   C CZ    
2271 N NH1   . ARG   C 125 ? 0.4321 0.3351 0.2521 -0.0105 0.0404  0.0009  125 ARG   C NH1   
2272 N NH2   . ARG   C 125 ? 0.4895 0.3533 0.2444 -0.0307 0.0415  -0.0073 125 ARG   C NH2   
2273 N N     . VAL   C 126 ? 0.4455 0.2611 0.2595 0.0361  0.0847  -0.0162 126 VAL   C N     
2274 C CA    . VAL   C 126 ? 0.4502 0.2728 0.2848 0.0520  0.0902  -0.0102 126 VAL   C CA    
2275 C C     . VAL   C 126 ? 0.4516 0.2830 0.2965 0.0675  0.1025  -0.0063 126 VAL   C C     
2276 O O     . VAL   C 126 ? 0.4694 0.2843 0.2942 0.0672  0.1131  -0.0111 126 VAL   C O     
2277 C CB    . VAL   C 126 ? 0.4799 0.2710 0.2983 0.0533  0.0966  -0.0130 126 VAL   C CB    
2278 C CG1   . VAL   C 126 ? 0.5283 0.2807 0.3150 0.0546  0.1124  -0.0207 126 VAL   C CG1   
2279 C CG2   . VAL   C 126 ? 0.4631 0.2637 0.3034 0.0678  0.0986  -0.0045 126 VAL   C CG2   
2280 N N     . TRP   C 127 ? 0.4359 0.2941 0.3117 0.0793  0.1005  0.0026  127 TRP   C N     
2281 C CA    . TRP   C 127 ? 0.4397 0.3140 0.3334 0.0935  0.1099  0.0086  127 TRP   C CA    
2282 C C     . TRP   C 127 ? 0.4289 0.3208 0.3498 0.1066  0.1083  0.0184  127 TRP   C C     
2283 O O     . TRP   C 127 ? 0.4411 0.3472 0.3731 0.1015  0.0951  0.0209  127 TRP   C O     
2284 C CB    . TRP   C 127 ? 0.4294 0.3316 0.3369 0.0878  0.1029  0.0106  127 TRP   C CB    
2285 C CG    . TRP   C 127 ? 0.4133 0.3377 0.3440 0.1001  0.1107  0.0180  127 TRP   C CG    
2286 C CD1   . TRP   C 127 ? 0.4338 0.3510 0.3573 0.1068  0.1266  0.0175  127 TRP   C CD1   
2287 C CD2   . TRP   C 127 ? 0.3741 0.3331 0.3391 0.1050  0.1024  0.0268  127 TRP   C CD2   
2288 N NE1   . TRP   C 127 ? 0.4226 0.3695 0.3768 0.1161  0.1290  0.0265  127 TRP   C NE1   
2289 C CE2   . TRP   C 127 ? 0.3788 0.3515 0.3584 0.1145  0.1134  0.0322  127 TRP   C CE2   
2290 C CE3   . TRP   C 127 ? 0.3622 0.3410 0.3454 0.1013  0.0874  0.0302  127 TRP   C CE3   
2291 C CZ2   . TRP   C 127 ? 0.3600 0.3669 0.3733 0.1192  0.1080  0.0414  127 TRP   C CZ2   
2292 C CZ3   . TRP   C 127 ? 0.3408 0.3510 0.3536 0.1054  0.0821  0.0380  127 TRP   C CZ3   
2293 C CH2   . TRP   C 127 ? 0.3355 0.3601 0.3639 0.1138  0.0915  0.0437  127 TRP   C CH2   
2294 N N     . LYS   C 128 ? 0.4589 0.3522 0.3914 0.1230  0.1215  0.0244  128 LYS   C N     
2295 C CA    . LYS   C 128 ? 0.4431 0.3525 0.4011 0.1364  0.1203  0.0357  128 LYS   C CA    
2296 C C     . LYS   C 128 ? 0.4081 0.3477 0.3957 0.1476  0.1248  0.0448  128 LYS   C C     
2297 O O     . LYS   C 128 ? 0.4124 0.3464 0.3968 0.1532  0.1392  0.0432  128 LYS   C O     
2298 C CB    . LYS   C 128 ? 0.4829 0.3601 0.4274 0.1464  0.1319  0.0364  128 LYS   C CB    
2299 C CG    . LYS   C 128 ? 0.4762 0.3659 0.4463 0.1636  0.1336  0.0505  128 LYS   C CG    
2300 C CD    . LYS   C 128 ? 0.5167 0.3708 0.4714 0.1716  0.1438  0.0513  128 LYS   C CD    
2301 C CE    . LYS   C 128 ? 0.5271 0.3945 0.5076 0.1884  0.1438  0.0672  128 LYS   C CE    
2302 N NZ    . LYS   C 128 ? 0.5643 0.3991 0.5296 0.1925  0.1482  0.0692  128 LYS   C NZ    
2303 N N     . SER   C 129 ? 0.3728 0.3437 0.3883 0.1504  0.1127  0.0546  129 SER   C N     
2304 C CA    . SER   C 129 ? 0.3725 0.3761 0.4209 0.1602  0.1139  0.0654  129 SER   C CA    
2305 C C     . SER   C 129 ? 0.3769 0.3986 0.4461 0.1669  0.1035  0.0772  129 SER   C C     
2306 O O     . SER   C 129 ? 0.3666 0.3931 0.4311 0.1565  0.0883  0.0755  129 SER   C O     
2307 C CB    . SER   C 129 ? 0.3501 0.3787 0.4089 0.1488  0.1051  0.0633  129 SER   C CB    
2308 O OG    . SER   C 129 ? 0.3621 0.4244 0.4542 0.1556  0.1042  0.0741  129 SER   C OG    
2309 N N     . GLY   C 130 ? 0.3799 0.4092 0.4700 0.1842  0.1125  0.0893  130 GLY   C N     
2310 C CA    . GLY   C 130 ? 0.3692 0.4072 0.4734 0.1928  0.1050  0.1020  130 GLY   C CA    
2311 C C     . GLY   C 130 ? 0.3854 0.3904 0.4606 0.1883  0.1029  0.0963  130 GLY   C C     
2312 O O     . GLY   C 130 ? 0.3994 0.3692 0.4504 0.1894  0.1163  0.0875  130 GLY   C O     
2313 N N     . ASP   C 131 ? 0.3761 0.3920 0.4507 0.1802  0.0859  0.0996  131 ASP   C N     
2314 C CA    . ASP   C 131 ? 0.3931 0.3818 0.4415 0.1734  0.0825  0.0946  131 ASP   C CA    
2315 C C     . ASP   C 131 ? 0.3865 0.3697 0.4150 0.1540  0.0744  0.0802  131 ASP   C C     
2316 O O     . ASP   C 131 ? 0.4078 0.3712 0.4166 0.1468  0.0715  0.0761  131 ASP   C O     
2317 C CB    . ASP   C 131 ? 0.3955 0.3958 0.4534 0.1784  0.0719  0.1086  131 ASP   C CB    
2318 C CG    . ASP   C 131 ? 0.4268 0.4295 0.5048 0.1988  0.0799  0.1249  131 ASP   C CG    
2319 O OD1   . ASP   C 131 ? 0.4516 0.4235 0.5199 0.2089  0.0967  0.1231  131 ASP   C OD1   
2320 O OD2   . ASP   C 131 ? 0.4335 0.4674 0.5357 0.2038  0.0688  0.1397  131 ASP   C OD2   
2321 N N     . LEU   C 132 ? 0.3598 0.3599 0.3947 0.1458  0.0714  0.0736  132 LEU   C N     
2322 C CA    . LEU   C 132 ? 0.3622 0.3578 0.3821 0.1291  0.0647  0.0616  132 LEU   C CA    
2323 C C     . LEU   C 132 ? 0.3851 0.3484 0.3806 0.1260  0.0759  0.0515  132 LEU   C C     
2324 O O     . LEU   C 132 ? 0.4078 0.3654 0.4033 0.1327  0.0875  0.0506  132 LEU   C O     
2325 C CB    . LEU   C 132 ? 0.3283 0.3510 0.3640 0.1221  0.0579  0.0595  132 LEU   C CB    
2326 C CG    . LEU   C 132 ? 0.3115 0.3301 0.3354 0.1067  0.0523  0.0484  132 LEU   C CG    
2327 C CD1   . LEU   C 132 ? 0.2924 0.3117 0.3106 0.0976  0.0417  0.0461  132 LEU   C CD1   
2328 C CD2   . LEU   C 132 ? 0.2997 0.3410 0.3402 0.1031  0.0497  0.0480  132 LEU   C CD2   
2329 N N     . VAL   C 133 ? 0.3697 0.3145 0.3451 0.1146  0.0719  0.0441  133 VAL   C N     
2330 C CA    . VAL   C 133 ? 0.3756 0.2951 0.3279 0.1060  0.0777  0.0335  133 VAL   C CA    
2331 C C     . VAL   C 133 ? 0.3516 0.2822 0.3029 0.0901  0.0661  0.0271  133 VAL   C C     
2332 O O     . VAL   C 133 ? 0.3307 0.2687 0.2855 0.0843  0.0573  0.0279  133 VAL   C O     
2333 C CB    . VAL   C 133 ? 0.4039 0.2873 0.3332 0.1065  0.0855  0.0308  133 VAL   C CB    
2334 C CG1   . VAL   C 133 ? 0.4276 0.2858 0.3317 0.0959  0.0907  0.0196  133 VAL   C CG1   
2335 C CG2   . VAL   C 133 ? 0.4279 0.2992 0.3611 0.1242  0.0976  0.0388  133 VAL   C CG2   
2336 N N     . MET   C 134 ? 0.3454 0.2753 0.2908 0.0832  0.0671  0.0212  134 MET   C N     
2337 C CA    . MET   C 134 ? 0.3225 0.2589 0.2662 0.0687  0.0573  0.0159  134 MET   C CA    
2338 C C     . MET   C 134 ? 0.3413 0.2505 0.2594 0.0592  0.0602  0.0088  134 MET   C C     
2339 O O     . MET   C 134 ? 0.3692 0.2572 0.2701 0.0630  0.0705  0.0061  134 MET   C O     
2340 C CB    . MET   C 134 ? 0.3142 0.2727 0.2720 0.0661  0.0534  0.0164  134 MET   C CB    
2341 C CG    . MET   C 134 ? 0.3101 0.2967 0.2934 0.0716  0.0487  0.0224  134 MET   C CG    
2342 S SD    . MET   C 134 ? 0.3481 0.3569 0.3467 0.0629  0.0410  0.0215  134 MET   C SD    
2343 C CE    . MET   C 134 ? 0.3201 0.3565 0.3452 0.0700  0.0375  0.0283  134 MET   C CE    
2344 N N     . ALA   C 135 ? 0.3352 0.2453 0.2512 0.0463  0.0511  0.0056  135 ALA   C N     
2345 C CA    . ALA   C 135 ? 0.3435 0.2324 0.2377 0.0343  0.0506  -0.0003 135 ALA   C CA    
2346 C C     . ALA   C 135 ? 0.3233 0.2287 0.2270 0.0213  0.0387  -0.0010 135 ALA   C C     
2347 O O     . ALA   C 135 ? 0.3132 0.2377 0.2367 0.0212  0.0327  0.0017  135 ALA   C O     
2348 C CB    . ALA   C 135 ? 0.3611 0.2263 0.2413 0.0329  0.0542  -0.0017 135 ALA   C CB    
2349 N N     . TYR   C 136 ? 0.3258 0.2219 0.2142 0.0105  0.0359  -0.0045 136 TYR   C N     
2350 C CA    . TYR   C 136 ? 0.3186 0.2294 0.2166 -0.0020 0.0241  -0.0034 136 TYR   C CA    
2351 C C     . TYR   C 136 ? 0.3518 0.2428 0.2253 -0.0164 0.0208  -0.0074 136 TYR   C C     
2352 O O     . TYR   C 136 ? 0.3856 0.2546 0.2333 -0.0167 0.0277  -0.0117 136 TYR   C O     
2353 C CB    . TYR   C 136 ? 0.2898 0.2235 0.2044 0.0003  0.0201  0.0005  136 TYR   C CB    
2354 C CG    . TYR   C 136 ? 0.2693 0.2202 0.1996 -0.0100 0.0083  0.0036  136 TYR   C CG    
2355 C CD1   . TYR   C 136 ? 0.2428 0.2096 0.1968 -0.0098 0.0042  0.0055  136 TYR   C CD1   
2356 C CD2   . TYR   C 136 ? 0.2830 0.2334 0.2039 -0.0202 0.0016  0.0051  136 TYR   C CD2   
2357 C CE1   . TYR   C 136 ? 0.2259 0.2083 0.1978 -0.0177 -0.0048 0.0091  136 TYR   C CE1   
2358 C CE2   . TYR   C 136 ? 0.2655 0.2332 0.2045 -0.0287 -0.0097 0.0101  136 TYR   C CE2   
2359 C CZ    . TYR   C 136 ? 0.2418 0.2255 0.2081 -0.0267 -0.0122 0.0121  136 TYR   C CZ    
2360 O OH    . TYR   C 136 ? 0.2435 0.2450 0.2321 -0.0327 -0.0212 0.0176  136 TYR   C OH    
2361 N N     . SER   C 137 ? 0.3577 0.2580 0.2407 -0.0286 0.0104  -0.0058 137 SER   C N     
2362 C CA    . SER   C 137 ? 0.3824 0.2705 0.2471 -0.0452 0.0032  -0.0079 137 SER   C CA    
2363 C C     . SER   C 137 ? 0.3761 0.2891 0.2586 -0.0532 -0.0097 -0.0018 137 SER   C C     
2364 O O     . SER   C 137 ? 0.3549 0.2898 0.2663 -0.0529 -0.0150 0.0029  137 SER   C O     
2365 C CB    . SER   C 137 ? 0.3809 0.2588 0.2440 -0.0530 0.0022  -0.0095 137 SER   C CB    
2366 O OG    . SER   C 137 ? 0.4095 0.2793 0.2581 -0.0715 -0.0071 -0.0107 137 SER   C OG    
2367 N N     . ARG   C 138 ? 0.4141 0.3221 0.2781 -0.0610 -0.0143 -0.0016 138 ARG   C N     
2368 C CA    . ARG   C 138 ? 0.4212 0.3498 0.2986 -0.0714 -0.0286 0.0058  138 ARG   C CA    
2369 C C     . ARG   C 138 ? 0.4245 0.3567 0.3077 -0.0870 -0.0398 0.0080  138 ARG   C C     
2370 O O     . ARG   C 138 ? 0.4174 0.3744 0.3277 -0.0912 -0.0504 0.0163  138 ARG   C O     
2371 C CB    . ARG   C 138 ? 0.4639 0.3859 0.3170 -0.0769 -0.0313 0.0066  138 ARG   C CB    
2372 C CG    . ARG   C 138 ? 0.5062 0.4431 0.3739 -0.0638 -0.0266 0.0109  138 ARG   C CG    
2373 C CD    . ARG   C 138 ? 0.5858 0.5196 0.4323 -0.0693 -0.0293 0.0138  138 ARG   C CD    
2374 N NE    . ARG   C 138 ? 0.6526 0.5972 0.5001 -0.0852 -0.0465 0.0214  138 ARG   C NE    
2375 C CZ    . ARG   C 138 ? 0.7047 0.6727 0.5749 -0.0856 -0.0563 0.0324  138 ARG   C CZ    
2376 N NH1   . ARG   C 138 ? 0.7829 0.7599 0.6643 -0.0743 -0.0500 0.0359  138 ARG   C NH1   
2377 N NH2   . ARG   C 138 ? 0.6972 0.6793 0.5792 -0.0978 -0.0723 0.0407  138 ARG   C NH2   
2378 N N     . ARG   C 139 ? 0.4383 0.3470 0.2994 -0.0953 -0.0371 0.0014  139 ARG   C N     
2379 C CA    . ARG   C 139 ? 0.4543 0.3677 0.3223 -0.1119 -0.0480 0.0040  139 ARG   C CA    
2380 C C     . ARG   C 139 ? 0.4230 0.3590 0.3299 -0.1062 -0.0474 0.0089  139 ARG   C C     
2381 O O     . ARG   C 139 ? 0.4393 0.3994 0.3725 -0.1136 -0.0581 0.0170  139 ARG   C O     
2382 C CB    . ARG   C 139 ? 0.4843 0.3637 0.3153 -0.1245 -0.0455 -0.0046 139 ARG   C CB    
2383 C CG    . ARG   C 139 ? 0.5123 0.3715 0.3043 -0.1337 -0.0480 -0.0092 139 ARG   C CG    
2384 C CD    . ARG   C 139 ? 0.5525 0.3747 0.3056 -0.1486 -0.0457 -0.0190 139 ARG   C CD    
2385 N NE    . ARG   C 139 ? 0.5814 0.3757 0.2903 -0.1531 -0.0411 -0.0268 139 ARG   C NE    
2386 C CZ    . ARG   C 139 ? 0.6360 0.3903 0.3025 -0.1636 -0.0348 -0.0380 139 ARG   C CZ    
2387 N NH1   . ARG   C 139 ? 0.6408 0.3764 0.3033 -0.1702 -0.0319 -0.0426 139 ARG   C NH1   
2388 N NH2   . ARG   C 139 ? 0.6767 0.4084 0.3033 -0.1683 -0.0307 -0.0447 139 ARG   C NH2   
2389 N N     . THR   C 140 ? 0.3988 0.3278 0.3094 -0.0930 -0.0346 0.0050  140 THR   C N     
2390 C CA    . THR   C 140 ? 0.3645 0.3103 0.3054 -0.0881 -0.0317 0.0081  140 THR   C CA    
2391 C C     . THR   C 140 ? 0.3318 0.3015 0.3011 -0.0737 -0.0291 0.0120  140 THR   C C     
2392 O O     . THR   C 140 ? 0.3444 0.3299 0.3395 -0.0711 -0.0272 0.0147  140 THR   C O     
2393 C CB    . THR   C 140 ? 0.3595 0.2820 0.2842 -0.0833 -0.0200 0.0022  140 THR   C CB    
2394 O OG1   . THR   C 140 ? 0.3382 0.2482 0.2482 -0.0688 -0.0106 -0.0016 140 THR   C OG1   
2395 C CG2   . THR   C 140 ? 0.3948 0.2909 0.2923 -0.0984 -0.0215 -0.0020 140 THR   C CG2   
2396 N N     . ALA   C 141 ? 0.3246 0.2945 0.2878 -0.0646 -0.0272 0.0114  141 ALA   C N     
2397 C CA    . ALA   C 141 ? 0.2981 0.2838 0.2817 -0.0505 -0.0227 0.0130  141 ALA   C CA    
2398 C C     . ALA   C 141 ? 0.2886 0.2699 0.2742 -0.0397 -0.0121 0.0092  141 ALA   C C     
2399 O O     . ALA   C 141 ? 0.2692 0.2649 0.2735 -0.0308 -0.0095 0.0102  141 ALA   C O     
2400 C CB    . ALA   C 141 ? 0.2793 0.2915 0.2963 -0.0521 -0.0299 0.0203  141 ALA   C CB    
2401 N N     . VAL   C 142 ? 0.2910 0.2510 0.2556 -0.0400 -0.0061 0.0050  142 VAL   C N     
2402 C CA    . VAL   C 142 ? 0.2843 0.2395 0.2482 -0.0296 0.0027  0.0032  142 VAL   C CA    
2403 C C     . VAL   C 142 ? 0.2662 0.2151 0.2192 -0.0179 0.0079  0.0019  142 VAL   C C     
2404 O O     . VAL   C 142 ? 0.2838 0.2161 0.2161 -0.0185 0.0100  -0.0003 142 VAL   C O     
2405 C CB    . VAL   C 142 ? 0.3043 0.2401 0.2534 -0.0344 0.0071  0.0014  142 VAL   C CB    
2406 C CG1   . VAL   C 142 ? 0.3093 0.2384 0.2541 -0.0229 0.0155  0.0013  142 VAL   C CG1   
2407 C CG2   . VAL   C 142 ? 0.3124 0.2590 0.2774 -0.0461 0.0025  0.0039  142 VAL   C CG2   
2408 N N     . TYR   C 143 ? 0.2469 0.2097 0.2144 -0.0080 0.0104  0.0032  143 TYR   C N     
2409 C CA    . TYR   C 143 ? 0.2502 0.2114 0.2132 0.0038  0.0155  0.0034  143 TYR   C CA    
2410 C C     . TYR   C 143 ? 0.2667 0.2207 0.2252 0.0103  0.0209  0.0040  143 TYR   C C     
2411 O O     . TYR   C 143 ? 0.2605 0.2201 0.2264 0.0077  0.0203  0.0044  143 TYR   C O     
2412 C CB    . TYR   C 143 ? 0.2278 0.2112 0.2115 0.0084  0.0127  0.0053  143 TYR   C CB    
2413 C CG    . TYR   C 143 ? 0.2105 0.1977 0.1951 0.0197  0.0169  0.0067  143 TYR   C CG    
2414 C CD1   . TYR   C 143 ? 0.2211 0.2051 0.1990 0.0239  0.0199  0.0076  143 TYR   C CD1   
2415 C CD2   . TYR   C 143 ? 0.1994 0.1949 0.1920 0.0254  0.0178  0.0078  143 TYR   C CD2   
2416 C CE1   . TYR   C 143 ? 0.2131 0.2040 0.1964 0.0342  0.0240  0.0103  143 TYR   C CE1   
2417 C CE2   . TYR   C 143 ? 0.1918 0.1939 0.1880 0.0346  0.0199  0.0105  143 TYR   C CE2   
2418 C CZ    . TYR   C 143 ? 0.1959 0.1965 0.1893 0.0394  0.0232  0.0122  143 TYR   C CZ    
2419 O OH    . TYR   C 143 ? 0.2010 0.2122 0.2030 0.0483  0.0251  0.0161  143 TYR   C OH    
2420 N N     . ALA   C 144 ? 0.2995 0.2430 0.2473 0.0197  0.0266  0.0050  144 ALA   C N     
2421 C CA    . ALA   C 144 ? 0.2996 0.2404 0.2462 0.0281  0.0305  0.0082  144 ALA   C CA    
2422 C C     . ALA   C 144 ? 0.2856 0.2317 0.2358 0.0405  0.0339  0.0116  144 ALA   C C     
2423 O O     . ALA   C 144 ? 0.2956 0.2375 0.2415 0.0428  0.0371  0.0105  144 ALA   C O     
2424 C CB    . ALA   C 144 ? 0.3334 0.2486 0.2613 0.0259  0.0353  0.0078  144 ALA   C CB    
2425 N N     . TYR   C 145 ? 0.2828 0.2377 0.2399 0.0478  0.0335  0.0164  145 TYR   C N     
2426 C CA    . TYR   C 145 ? 0.2889 0.2456 0.2490 0.0606  0.0378  0.0220  145 TYR   C CA    
2427 C C     . TYR   C 145 ? 0.3009 0.2523 0.2574 0.0673  0.0389  0.0285  145 TYR   C C     
2428 O O     . TYR   C 145 ? 0.3091 0.2617 0.2629 0.0614  0.0350  0.0286  145 TYR   C O     
2429 C CB    . TYR   C 145 ? 0.2743 0.2564 0.2533 0.0636  0.0338  0.0238  145 TYR   C CB    
2430 C CG    . TYR   C 145 ? 0.2613 0.2645 0.2535 0.0631  0.0263  0.0267  145 TYR   C CG    
2431 C CD1   . TYR   C 145 ? 0.2590 0.2724 0.2572 0.0535  0.0206  0.0217  145 TYR   C CD1   
2432 C CD2   . TYR   C 145 ? 0.2701 0.2842 0.2699 0.0720  0.0250  0.0345  145 TYR   C CD2   
2433 C CE1   . TYR   C 145 ? 0.2462 0.2757 0.2527 0.0517  0.0149  0.0226  145 TYR   C CE1   
2434 C CE2   . TYR   C 145 ? 0.2519 0.2849 0.2606 0.0693  0.0169  0.0366  145 TYR   C CE2   
2435 C CZ    . TYR   C 145 ? 0.2409 0.2803 0.2514 0.0587  0.0123  0.0296  145 TYR   C CZ    
2436 O OH    . TYR   C 145 ? 0.2293 0.2832 0.2446 0.0543  0.0056  0.0293  145 TYR   C OH    
2437 N N     . TYR   C 146 ? 0.3244 0.2712 0.2821 0.0798  0.0447  0.0348  146 TYR   C N     
2438 C CA    . TYR   C 146 ? 0.3640 0.2974 0.3153 0.0883  0.0484  0.0425  146 TYR   C CA    
2439 C C     . TYR   C 146 ? 0.3532 0.3019 0.3207 0.1027  0.0493  0.0527  146 TYR   C C     
2440 O O     . TYR   C 146 ? 0.3460 0.2991 0.3218 0.1090  0.0548  0.0524  146 TYR   C O     
2441 C CB    . TYR   C 146 ? 0.3926 0.2916 0.3239 0.0882  0.0583  0.0388  146 TYR   C CB    
2442 C CG    . TYR   C 146 ? 0.4480 0.3266 0.3730 0.1001  0.0660  0.0472  146 TYR   C CG    
2443 C CD1   . TYR   C 146 ? 0.4582 0.3243 0.3734 0.0973  0.0644  0.0515  146 TYR   C CD1   
2444 C CD2   . TYR   C 146 ? 0.4688 0.3391 0.3976 0.1143  0.0762  0.0511  146 TYR   C CD2   
2445 C CE1   . TYR   C 146 ? 0.4974 0.3423 0.4067 0.1081  0.0716  0.0601  146 TYR   C CE1   
2446 C CE2   . TYR   C 146 ? 0.5016 0.3522 0.4271 0.1266  0.0841  0.0597  146 TYR   C CE2   
2447 C CZ    . TYR   C 146 ? 0.5038 0.3406 0.4190 0.1233  0.0814  0.0644  146 TYR   C CZ    
2448 O OH    . TYR   C 146 ? 0.5043 0.3199 0.4162 0.1354  0.0891  0.0741  146 TYR   C OH    
2449 N N     . THR   C 147 ? 0.3646 0.3214 0.3363 0.1075  0.0441  0.0626  147 THR   C N     
2450 C CA    . THR   C 147 ? 0.3648 0.3403 0.3548 0.1203  0.0421  0.0751  147 THR   C CA    
2451 C C     . THR   C 147 ? 0.3888 0.3466 0.3756 0.1336  0.0486  0.0865  147 THR   C C     
2452 O O     . THR   C 147 ? 0.3762 0.3502 0.3814 0.1460  0.0475  0.0989  147 THR   C O     
2453 C CB    . THR   C 147 ? 0.3697 0.3719 0.3673 0.1137  0.0281  0.0789  147 THR   C CB    
2454 O OG1   . THR   C 147 ? 0.3823 0.3722 0.3630 0.1086  0.0249  0.0810  147 THR   C OG1   
2455 C CG2   . THR   C 147 ? 0.3435 0.3619 0.3465 0.1018  0.0225  0.0684  147 THR   C CG2   
2456 N N     . GLY   C 148 ? 0.4093 0.3361 0.3749 0.1307  0.0543  0.0839  148 GLY   C N     
2457 C CA    . GLY   C 148 ? 0.4586 0.3685 0.4194 0.1407  0.0578  0.0960  148 GLY   C CA    
2458 C C     . GLY   C 148 ? 0.4760 0.3925 0.4292 0.1339  0.0470  0.1029  148 GLY   C C     
2459 O O     . GLY   C 148 ? 0.5106 0.4036 0.4504 0.1362  0.0510  0.1089  148 GLY   C O     
2460 N N     . THR   C 149 ? 0.4596 0.4064 0.4204 0.1261  0.0344  0.1026  149 THR   C N     
2461 C CA    . THR   C 149 ? 0.4453 0.4006 0.3962 0.1181  0.0242  0.1076  149 THR   C CA    
2462 C C     . THR   C 149 ? 0.4379 0.3860 0.3731 0.1014  0.0242  0.0937  149 THR   C C     
2463 O O     . THR   C 149 ? 0.4499 0.3916 0.3698 0.0943  0.0217  0.0961  149 THR   C O     
2464 C CB    . THR   C 149 ? 0.4220 0.4130 0.3891 0.1184  0.0112  0.1141  149 THR   C CB    
2465 O OG1   . THR   C 149 ? 0.4516 0.4497 0.4378 0.1348  0.0131  0.1274  149 THR   C OG1   
2466 C CG2   . THR   C 149 ? 0.4294 0.4301 0.3836 0.1096  0.0001  0.1195  149 THR   C CG2   
2467 N N     . ALA   C 150 ? 0.4123 0.3660 0.3535 0.0950  0.0258  0.0806  150 ALA   C N     
2468 C CA    . ALA   C 150 ? 0.3738 0.3227 0.3056 0.0806  0.0265  0.0683  150 ALA   C CA    
2469 C C     . ALA   C 150 ? 0.3496 0.2911 0.2850 0.0777  0.0321  0.0575  150 ALA   C C     
2470 O O     . ALA   C 150 ? 0.3311 0.2756 0.2764 0.0856  0.0349  0.0578  150 ALA   C O     
2471 C CB    . ALA   C 150 ? 0.3627 0.3356 0.2986 0.0724  0.0175  0.0653  150 ALA   C CB    
2472 N N     . VAL   C 151 ? 0.3250 0.2590 0.2528 0.0656  0.0334  0.0487  151 VAL   C N     
2473 C CA    . VAL   C 151 ? 0.3277 0.2588 0.2584 0.0592  0.0357  0.0388  151 VAL   C CA    
2474 C C     . VAL   C 151 ? 0.3090 0.2569 0.2469 0.0483  0.0308  0.0320  151 VAL   C C     
2475 O O     . VAL   C 151 ? 0.3070 0.2570 0.2399 0.0427  0.0297  0.0326  151 VAL   C O     
2476 C CB    . VAL   C 151 ? 0.3615 0.2637 0.2773 0.0551  0.0427  0.0359  151 VAL   C CB    
2477 C CG1   . VAL   C 151 ? 0.3930 0.2841 0.2979 0.0463  0.0437  0.0368  151 VAL   C CG1   
2478 C CG2   . VAL   C 151 ? 0.3697 0.2695 0.2867 0.0479  0.0433  0.0269  151 VAL   C CG2   
2479 N N     . ASP   C 152 ? 0.2893 0.2485 0.2387 0.0459  0.0288  0.0261  152 ASP   C N     
2480 C CA    . ASP   C 152 ? 0.2636 0.2345 0.2219 0.0362  0.0260  0.0194  152 ASP   C CA    
2481 C C     . ASP   C 152 ? 0.2595 0.2182 0.2147 0.0293  0.0283  0.0150  152 ASP   C C     
2482 O O     . ASP   C 152 ? 0.2460 0.1996 0.2001 0.0321  0.0292  0.0142  152 ASP   C O     
2483 C CB    . ASP   C 152 ? 0.2579 0.2491 0.2316 0.0383  0.0215  0.0178  152 ASP   C CB    
2484 C CG    . ASP   C 152 ? 0.2595 0.2617 0.2456 0.0303  0.0194  0.0114  152 ASP   C CG    
2485 O OD1   . ASP   C 152 ? 0.2488 0.2484 0.2341 0.0233  0.0211  0.0086  152 ASP   C OD1   
2486 O OD2   . ASP   C 152 ? 0.2407 0.2536 0.2385 0.0316  0.0169  0.0103  152 ASP   C OD2   
2487 N N     . VAL   C 153 ? 0.2672 0.2221 0.2212 0.0198  0.0293  0.0126  153 VAL   C N     
2488 C CA    . VAL   C 153 ? 0.2623 0.2108 0.2171 0.0108  0.0288  0.0092  153 VAL   C CA    
2489 C C     . VAL   C 153 ? 0.2516 0.2200 0.2256 0.0048  0.0257  0.0063  153 VAL   C C     
2490 O O     . VAL   C 153 ? 0.2457 0.2215 0.2253 0.0023  0.0277  0.0058  153 VAL   C O     
2491 C CB    . VAL   C 153 ? 0.2797 0.2080 0.2207 0.0040  0.0326  0.0101  153 VAL   C CB    
2492 C CG1   . VAL   C 153 ? 0.2875 0.2095 0.2282 -0.0074 0.0304  0.0070  153 VAL   C CG1   
2493 C CG2   . VAL   C 153 ? 0.2972 0.2036 0.2201 0.0115  0.0373  0.0137  153 VAL   C CG2   
2494 N N     . GLU   C 154 ? 0.2530 0.2290 0.2367 0.0030  0.0216  0.0047  154 GLU   C N     
2495 C CA    . GLU   C 154 ? 0.2327 0.2265 0.2370 -0.0009 0.0186  0.0033  154 GLU   C CA    
2496 C C     . GLU   C 154 ? 0.2540 0.2468 0.2631 -0.0104 0.0151  0.0040  154 GLU   C C     
2497 O O     . GLU   C 154 ? 0.2362 0.2225 0.2374 -0.0123 0.0114  0.0044  154 GLU   C O     
2498 C CB    . GLU   C 154 ? 0.2385 0.2434 0.2517 0.0049  0.0156  0.0031  154 GLU   C CB    
2499 C CG    . GLU   C 154 ? 0.2376 0.2452 0.2464 0.0135  0.0170  0.0036  154 GLU   C CG    
2500 C CD    . GLU   C 154 ? 0.2262 0.2485 0.2493 0.0164  0.0141  0.0030  154 GLU   C CD    
2501 O OE1   . GLU   C 154 ? 0.2445 0.2739 0.2806 0.0129  0.0117  0.0025  154 GLU   C OE1   
2502 O OE2   . GLU   C 154 ? 0.2346 0.2625 0.2574 0.0216  0.0136  0.0037  154 GLU   C OE2   
2503 N N     . GLN   C 155 ? 0.2506 0.2511 0.2730 -0.0168 0.0162  0.0044  155 GLN   C N     
2504 C CA    . GLN   C 155 ? 0.2495 0.2545 0.2825 -0.0269 0.0117  0.0067  155 GLN   C CA    
2505 C C     . GLN   C 155 ? 0.2347 0.2600 0.2942 -0.0262 0.0081  0.0086  155 GLN   C C     
2506 O O     . GLN   C 155 ? 0.2222 0.2568 0.2939 -0.0201 0.0124  0.0068  155 GLN   C O     
2507 C CB    . GLN   C 155 ? 0.2410 0.2443 0.2769 -0.0338 0.0163  0.0076  155 GLN   C CB    
2508 C CG    . GLN   C 155 ? 0.2761 0.2571 0.2866 -0.0355 0.0198  0.0070  155 GLN   C CG    
2509 C CD    . GLN   C 155 ? 0.2790 0.2590 0.2925 -0.0415 0.0260  0.0084  155 GLN   C CD    
2510 O OE1   . GLN   C 155 ? 0.2799 0.2576 0.2874 -0.0363 0.0330  0.0080  155 GLN   C OE1   
2511 N NE2   . GLN   C 155 ? 0.2837 0.2680 0.3081 -0.0531 0.0230  0.0109  155 GLN   C NE2   
2512 N N     . PRO   C 156 ? 0.2211 0.2529 0.2897 -0.0332 0.0000  0.0127  156 PRO   C N     
2513 C CA    . PRO   C 156 ? 0.2122 0.2637 0.3099 -0.0329 -0.0032 0.0169  156 PRO   C CA    
2514 C C     . PRO   C 156 ? 0.2090 0.2724 0.3303 -0.0357 0.0021  0.0186  156 PRO   C C     
2515 O O     . PRO   C 156 ? 0.2166 0.2756 0.3332 -0.0429 0.0038  0.0191  156 PRO   C O     
2516 C CB    . PRO   C 156 ? 0.2263 0.2802 0.3235 -0.0413 -0.0146 0.0225  156 PRO   C CB    
2517 C CG    . PRO   C 156 ? 0.2426 0.2807 0.3174 -0.0507 -0.0158 0.0208  156 PRO   C CG    
2518 C CD    . PRO   C 156 ? 0.2432 0.2634 0.2951 -0.0429 -0.0064 0.0141  156 PRO   C CD    
2519 N N     . VAL   C 157 ? 0.1906 0.2686 0.3384 -0.0305 0.0051  0.0200  157 VAL   C N     
2520 C CA    . VAL   C 157 ? 0.1875 0.2775 0.3605 -0.0311 0.0130  0.0214  157 VAL   C CA    
2521 C C     . VAL   C 157 ? 0.1762 0.2786 0.3684 -0.0410 0.0068  0.0297  157 VAL   C C     
2522 O O     . VAL   C 157 ? 0.1859 0.2965 0.3951 -0.0435 0.0143  0.0311  157 VAL   C O     
2523 C CB    . VAL   C 157 ? 0.1733 0.2729 0.3698 -0.0225 0.0188  0.0205  157 VAL   C CB    
2524 C CG1   . VAL   C 157 ? 0.1612 0.2738 0.3813 -0.0222 0.0094  0.0290  157 VAL   C CG1   
2525 C CG2   . VAL   C 157 ? 0.1813 0.2874 0.3965 -0.0209 0.0323  0.0183  157 VAL   C CG2   
2526 N N     . THR   C 158 ? 0.1796 0.2844 0.3691 -0.0471 -0.0068 0.0356  158 THR   C N     
2527 C CA    . THR   C 158 ? 0.1895 0.3047 0.3909 -0.0595 -0.0168 0.0439  158 THR   C CA    
2528 C C     . THR   C 158 ? 0.2039 0.3097 0.3911 -0.0693 -0.0139 0.0415  158 THR   C C     
2529 O O     . THR   C 158 ? 0.2012 0.3186 0.4037 -0.0804 -0.0207 0.0485  158 THR   C O     
2530 C CB    . THR   C 158 ? 0.2018 0.3156 0.3911 -0.0656 -0.0321 0.0487  158 THR   C CB    
2531 O OG1   . THR   C 158 ? 0.2071 0.2977 0.3582 -0.0632 -0.0308 0.0405  158 THR   C OG1   
2532 C CG2   . THR   C 158 ? 0.1892 0.3178 0.4013 -0.0592 -0.0374 0.0558  158 THR   C CG2   
2533 N N     . TYR   C 159 ? 0.2120 0.2969 0.3701 -0.0662 -0.0054 0.0330  159 TYR   C N     
2534 C CA    . TYR   C 159 ? 0.2443 0.3182 0.3896 -0.0738 -0.0002 0.0312  159 TYR   C CA    
2535 C C     . TYR   C 159 ? 0.2484 0.3340 0.4160 -0.0724 0.0126  0.0321  159 TYR   C C     
2536 O O     . TYR   C 159 ? 0.2483 0.3268 0.4084 -0.0804 0.0169  0.0323  159 TYR   C O     
2537 C CB    . TYR   C 159 ? 0.2645 0.3112 0.3704 -0.0698 0.0025  0.0238  159 TYR   C CB    
2538 C CG    . TYR   C 159 ? 0.2781 0.3086 0.3579 -0.0752 -0.0075 0.0226  159 TYR   C CG    
2539 C CD1   . TYR   C 159 ? 0.2876 0.3269 0.3743 -0.0844 -0.0203 0.0276  159 TYR   C CD1   
2540 C CD2   . TYR   C 159 ? 0.3082 0.3134 0.3551 -0.0713 -0.0036 0.0168  159 TYR   C CD2   
2541 C CE1   . TYR   C 159 ? 0.3130 0.3344 0.3708 -0.0908 -0.0278 0.0252  159 TYR   C CE1   
2542 C CE2   . TYR   C 159 ? 0.3397 0.3267 0.3607 -0.0759 -0.0096 0.0145  159 TYR   C CE2   
2543 C CZ    . TYR   C 159 ? 0.3455 0.3397 0.3700 -0.0863 -0.0214 0.0180  159 TYR   C CZ    
2544 O OH    . TYR   C 159 ? 0.3777 0.3540 0.3748 -0.0927 -0.0273 0.0153  159 TYR   C OH    
2545 N N     . ARG   C 160 ? 0.2303 0.3324 0.4251 -0.0633 0.0193  0.0329  160 ARG   C N     
2546 C CA    . ARG   C 160 ? 0.2335 0.3445 0.4470 -0.0605 0.0344  0.0322  160 ARG   C CA    
2547 C C     . ARG   C 160 ? 0.2335 0.3591 0.4704 -0.0722 0.0343  0.0401  160 ARG   C C     
2548 O O     . ARG   C 160 ? 0.2329 0.3751 0.4931 -0.0783 0.0229  0.0485  160 ARG   C O     
2549 C CB    . ARG   C 160 ? 0.2180 0.3429 0.4587 -0.0493 0.0410  0.0319  160 ARG   C CB    
2550 C CG    . ARG   C 160 ? 0.2121 0.3455 0.4733 -0.0449 0.0590  0.0300  160 ARG   C CG    
2551 C CD    . ARG   C 160 ? 0.1972 0.3375 0.4791 -0.0336 0.0647  0.0281  160 ARG   C CD    
2552 N NE    . ARG   C 160 ? 0.2040 0.3260 0.4560 -0.0265 0.0681  0.0176  160 ARG   C NE    
2553 C CZ    . ARG   C 160 ? 0.2075 0.3286 0.4674 -0.0176 0.0720  0.0133  160 ARG   C CZ    
2554 N NH1   . ARG   C 160 ? 0.1924 0.2982 0.4244 -0.0135 0.0721  0.0048  160 ARG   C NH1   
2555 N NH2   . ARG   C 160 ? 0.2092 0.3450 0.5062 -0.0130 0.0750  0.0185  160 ARG   C NH2   
2556 N N     . GLY   C 161 ? 0.2486 0.3676 0.4773 -0.0762 0.0459  0.0382  161 GLY   C N     
2557 C CA    . GLY   C 161 ? 0.2465 0.3771 0.4943 -0.0888 0.0475  0.0454  161 GLY   C CA    
2558 C C     . GLY   C 161 ? 0.2633 0.3780 0.4863 -0.1032 0.0366  0.0466  161 GLY   C C     
2559 O O     . GLY   C 161 ? 0.2700 0.3929 0.5071 -0.1153 0.0379  0.0523  161 GLY   C O     
2560 N N     . ARG   C 162 ? 0.2737 0.3663 0.4621 -0.1021 0.0271  0.0414  162 ARG   C N     
2561 C CA    . ARG   C 162 ? 0.2977 0.3681 0.4563 -0.1139 0.0190  0.0402  162 ARG   C CA    
2562 C C     . ARG   C 162 ? 0.3088 0.3485 0.4264 -0.1064 0.0247  0.0324  162 ARG   C C     
2563 O O     . ARG   C 162 ? 0.3431 0.3601 0.4340 -0.1140 0.0203  0.0306  162 ARG   C O     
2564 C CB    . ARG   C 162 ? 0.3075 0.3816 0.4658 -0.1199 0.0014  0.0427  162 ARG   C CB    
2565 C CG    . ARG   C 162 ? 0.3036 0.4070 0.5002 -0.1313 -0.0079 0.0530  162 ARG   C CG    
2566 C CD    . ARG   C 162 ? 0.3143 0.4182 0.5033 -0.1406 -0.0271 0.0560  162 ARG   C CD    
2567 N NE    . ARG   C 162 ? 0.3206 0.4265 0.5069 -0.1275 -0.0308 0.0544  162 ARG   C NE    
2568 C CZ    . ARG   C 162 ? 0.3469 0.4390 0.5066 -0.1284 -0.0412 0.0515  162 ARG   C CZ    
2569 N NH1   . ARG   C 162 ? 0.3684 0.4417 0.4991 -0.1429 -0.0503 0.0492  162 ARG   C NH1   
2570 N NH2   . ARG   C 162 ? 0.3334 0.4298 0.4953 -0.1155 -0.0420 0.0510  162 ARG   C NH2   
2571 N N     . ALA   C 163 ? 0.2940 0.3321 0.4067 -0.0926 0.0352  0.0282  163 ALA   C N     
2572 C CA    . ALA   C 163 ? 0.2940 0.3077 0.3721 -0.0842 0.0386  0.0228  163 ALA   C CA    
2573 C C     . ALA   C 163 ? 0.3267 0.3247 0.3884 -0.0889 0.0482  0.0238  163 ALA   C C     
2574 O O     . ALA   C 163 ? 0.3365 0.3465 0.4150 -0.0926 0.0575  0.0267  163 ALA   C O     
2575 C CB    . ALA   C 163 ? 0.2789 0.3003 0.3605 -0.0701 0.0441  0.0190  163 ALA   C CB    
2576 N N     . THR   C 164 ? 0.3428 0.3136 0.3728 -0.0882 0.0471  0.0221  164 THR   C N     
2577 C CA    . THR   C 164 ? 0.3778 0.3293 0.3883 -0.0912 0.0557  0.0242  164 THR   C CA    
2578 C C     . THR   C 164 ? 0.3870 0.3195 0.3697 -0.0782 0.0574  0.0221  164 THR   C C     
2579 O O     . THR   C 164 ? 0.3750 0.3125 0.3572 -0.0680 0.0525  0.0187  164 THR   C O     
2580 C CB    . THR   C 164 ? 0.3853 0.3198 0.3874 -0.1066 0.0523  0.0266  164 THR   C CB    
2581 O OG1   . THR   C 164 ? 0.3873 0.3044 0.3710 -0.1051 0.0434  0.0228  164 THR   C OG1   
2582 C CG2   . THR   C 164 ? 0.3792 0.3345 0.4103 -0.1213 0.0479  0.0302  164 THR   C CG2   
2583 N N     . GLY   C 165 ? 0.3881 0.3001 0.3499 -0.0788 0.0640  0.0253  165 GLY   C N     
2584 C CA    . GLY   C 165 ? 0.4050 0.2993 0.3424 -0.0667 0.0650  0.0259  165 GLY   C CA    
2585 C C     . GLY   C 165 ? 0.3869 0.2932 0.3231 -0.0581 0.0707  0.0268  165 GLY   C C     
2586 O O     . GLY   C 165 ? 0.3567 0.2836 0.3106 -0.0604 0.0749  0.0250  165 GLY   C O     
2587 N N     . LEU   C 166 ? 0.3902 0.2826 0.3051 -0.0483 0.0709  0.0297  166 LEU   C N     
2588 C CA    . LEU   C 166 ? 0.3872 0.2881 0.2949 -0.0416 0.0745  0.0313  166 LEU   C CA    
2589 C C     . LEU   C 166 ? 0.3539 0.2777 0.2763 -0.0360 0.0715  0.0248  166 LEU   C C     
2590 O O     . LEU   C 166 ? 0.3482 0.2817 0.2688 -0.0355 0.0766  0.0237  166 LEU   C O     
2591 C CB    . LEU   C 166 ? 0.4105 0.2934 0.2945 -0.0327 0.0731  0.0379  166 LEU   C CB    
2592 C CG    . LEU   C 166 ? 0.4393 0.2972 0.3064 -0.0375 0.0782  0.0458  166 LEU   C CG    
2593 C CD1   . LEU   C 166 ? 0.4632 0.3068 0.3118 -0.0254 0.0754  0.0534  166 LEU   C CD1   
2594 C CD2   . LEU   C 166 ? 0.4534 0.3130 0.3172 -0.0474 0.0875  0.0493  166 LEU   C CD2   
2595 N N     . CYS   C 167 ? 0.3396 0.2708 0.2754 -0.0328 0.0641  0.0205  167 CYS   C N     
2596 C CA    . CYS   C 167 ? 0.3180 0.2694 0.2698 -0.0285 0.0614  0.0149  167 CYS   C CA    
2597 C C     . CYS   C 167 ? 0.3183 0.2861 0.2911 -0.0351 0.0679  0.0117  167 CYS   C C     
2598 O O     . CYS   C 167 ? 0.2925 0.2735 0.2743 -0.0317 0.0699  0.0073  167 CYS   C O     
2599 C CB    . CYS   C 167 ? 0.3109 0.2645 0.2708 -0.0245 0.0528  0.0126  167 CYS   C CB    
2600 S SG    . CYS   C 167 ? 0.3087 0.2463 0.2485 -0.0139 0.0480  0.0158  167 CYS   C SG    
2601 N N     . GLY   C 168 ? 0.3276 0.2946 0.3098 -0.0448 0.0715  0.0143  168 GLY   C N     
2602 C CA    . GLY   C 168 ? 0.3226 0.3051 0.3260 -0.0508 0.0801  0.0135  168 GLY   C CA    
2603 C C     . GLY   C 168 ? 0.3149 0.3170 0.3481 -0.0497 0.0760  0.0106  168 GLY   C C     
2604 O O     . GLY   C 168 ? 0.3015 0.3040 0.3394 -0.0487 0.0654  0.0107  168 GLY   C O     
2605 N N     . ASN   C 169 ? 0.3227 0.3398 0.3749 -0.0495 0.0856  0.0084  169 ASN   C N     
2606 C CA    . ASN   C 169 ? 0.3215 0.3585 0.4082 -0.0497 0.0851  0.0083  169 ASN   C CA    
2607 C C     . ASN   C 169 ? 0.3358 0.3760 0.4250 -0.0411 0.0767  0.0043  169 ASN   C C     
2608 O O     . ASN   C 169 ? 0.3168 0.3482 0.3852 -0.0347 0.0758  0.0000  169 ASN   C O     
2609 C CB    . ASN   C 169 ? 0.3415 0.3906 0.4467 -0.0505 0.1010  0.0070  169 ASN   C CB    
2610 C CG    . ASN   C 169 ? 0.3505 0.3987 0.4482 -0.0424 0.1095  -0.0009 169 ASN   C CG    
2611 O OD1   . ASN   C 169 ? 0.3137 0.3705 0.4287 -0.0365 0.1076  -0.0042 169 ASN   C OD1   
2612 N ND2   . ASN   C 169 ? 0.3803 0.4174 0.4520 -0.0428 0.1194  -0.0040 169 ASN   C ND2   
2613 N N     . LEU   C 170 ? 0.3392 0.3933 0.4552 -0.0418 0.0700  0.0069  170 LEU   C N     
2614 C CA    . LEU   C 170 ? 0.3180 0.3776 0.4424 -0.0346 0.0632  0.0046  170 LEU   C CA    
2615 C C     . LEU   C 170 ? 0.3430 0.4174 0.4963 -0.0302 0.0720  0.0028  170 LEU   C C     
2616 O O     . LEU   C 170 ? 0.3445 0.4288 0.5185 -0.0268 0.0662  0.0047  170 LEU   C O     
2617 C CB    . LEU   C 170 ? 0.2990 0.3602 0.4276 -0.0389 0.0491  0.0098  170 LEU   C CB    
2618 C CG    . LEU   C 170 ? 0.2952 0.3375 0.3933 -0.0423 0.0428  0.0101  170 LEU   C CG    
2619 C CD1   . LEU   C 170 ? 0.2879 0.3307 0.3875 -0.0458 0.0298  0.0131  170 LEU   C CD1   
2620 C CD2   . LEU   C 170 ? 0.2867 0.3136 0.3562 -0.0349 0.0447  0.0058  170 LEU   C CD2   
2621 N N     . ASN   C 171 ? 0.3796 0.4532 0.5320 -0.0296 0.0871  -0.0012 171 ASN   C N     
2622 C CA    . ASN   C 171 ? 0.4765 0.5519 0.6366 -0.0231 0.0983  -0.0082 171 ASN   C CA    
2623 C C     . ASN   C 171 ? 0.5919 0.6849 0.7932 -0.0222 0.1067  -0.0043 171 ASN   C C     
2624 O O     . ASN   C 171 ? 0.7895 0.8876 1.0107 -0.0156 0.1098  -0.0065 171 ASN   C O     
2625 C CB    . ASN   C 171 ? 0.4766 0.5446 0.6226 -0.0171 0.0912  -0.0139 171 ASN   C CB    
2626 C CG    . ASN   C 171 ? 0.6157 0.6687 0.7232 -0.0177 0.0876  -0.0174 171 ASN   C CG    
2627 O OD1   . ASN   C 171 ? 0.5369 0.5834 0.6275 -0.0206 0.0801  -0.0128 171 ASN   C OD1   
2628 N ND2   . ASN   C 171 ? 0.6941 0.7407 0.7871 -0.0151 0.0936  -0.0253 171 ASN   C ND2   
2629 N N     . GLY   C 172 ? 0.5468 0.6481 0.7610 -0.0287 0.1120  0.0017  172 GLY   C N     
2630 C CA    . GLY   C 172 ? 0.5303 0.6532 0.7877 -0.0303 0.1122  0.0108  172 GLY   C CA    
2631 C C     . GLY   C 172 ? 0.5472 0.6761 0.8076 -0.0415 0.1045  0.0194  172 GLY   C C     
2632 O O     . GLY   C 172 ? 0.6277 0.7406 0.8545 -0.0466 0.0972  0.0178  172 GLY   C O     
2633 N N     . GLY   D 2   ? 0.6890 0.5369 0.4875 0.2838  0.0124  -0.1341 1   GLY   D N     
2634 C CA    . GLY   D 2   ? 0.6331 0.5121 0.4632 0.2560  0.0133  -0.1212 1   GLY   D CA    
2635 C C     . GLY   D 2   ? 0.6165 0.5006 0.4477 0.2287  0.0176  -0.1181 1   GLY   D C     
2636 O O     . GLY   D 2   ? 0.6365 0.5148 0.4516 0.2309  0.0224  -0.1261 1   GLY   D O     
2637 N N     . SER   D 3   ? 0.5815 0.4797 0.4328 0.2040  0.0160  -0.1066 2   SER   D N     
2638 C CA    . SER   D 3   ? 0.5802 0.4733 0.4287 0.1777  0.0158  -0.1022 2   SER   D CA    
2639 C C     . SER   D 3   ? 0.5478 0.4895 0.4212 0.1692  0.0246  -0.1008 2   SER   D C     
2640 O O     . SER   D 3   ? 0.5202 0.5036 0.4208 0.1747  0.0301  -0.0989 2   SER   D O     
2641 C CB    . SER   D 3   ? 0.5700 0.4493 0.4241 0.1571  0.0086  -0.0915 2   SER   D CB    
2642 O OG    . SER   D 3   ? 0.6185 0.4484 0.4446 0.1616  0.0010  -0.0925 2   SER   D OG    
2643 N N     . GLN   D 4   ? 0.5521 0.4869 0.4147 0.1533  0.0250  -0.1009 3   GLN   D N     
2644 C CA    . GLN   D 4   ? 0.5291 0.4997 0.4084 0.1408  0.0313  -0.0976 3   GLN   D CA    
2645 C C     . GLN   D 4   ? 0.5002 0.4672 0.3869 0.1171  0.0246  -0.0878 3   GLN   D C     
2646 O O     . GLN   D 4   ? 0.5062 0.4400 0.3777 0.1085  0.0164  -0.0869 3   GLN   D O     
2647 C CB    . GLN   D 4   ? 0.5811 0.5456 0.4379 0.1454  0.0368  -0.1070 3   GLN   D CB    
2648 C CG    . GLN   D 4   ? 0.6214 0.5957 0.4734 0.1711  0.0448  -0.1181 3   GLN   D CG    
2649 C CD    . GLN   D 4   ? 0.6911 0.6628 0.5211 0.1758  0.0521  -0.1280 3   GLN   D CD    
2650 O OE1   . GLN   D 4   ? 0.7310 0.7352 0.5689 0.1882  0.0632  -0.1348 3   GLN   D OE1   
2651 N NE2   . GLN   D 4   ? 0.7370 0.6706 0.5383 0.1656  0.0462  -0.1298 3   GLN   D NE2   
2652 N N     . VAL   D 5   ? 0.4575 0.4590 0.3666 0.1067  0.0283  -0.0811 4   VAL   D N     
2653 C CA    . VAL   D 5   ? 0.4303 0.4348 0.3496 0.0872  0.0224  -0.0722 4   VAL   D CA    
2654 C C     . VAL   D 5   ? 0.4277 0.4461 0.3436 0.0775  0.0252  -0.0711 4   VAL   D C     
2655 O O     . VAL   D 5   ? 0.4078 0.4482 0.3265 0.0826  0.0341  -0.0732 4   VAL   D O     
2656 C CB    . VAL   D 5   ? 0.3982 0.4230 0.3450 0.0840  0.0217  -0.0636 4   VAL   D CB    
2657 C CG1   . VAL   D 5   ? 0.3784 0.4409 0.3453 0.0878  0.0302  -0.0615 4   VAL   D CG1   
2658 C CG2   . VAL   D 5   ? 0.3858 0.4078 0.3404 0.0664  0.0144  -0.0560 4   VAL   D CG2   
2659 N N     . GLU   D 6   ? 0.4476 0.4526 0.3560 0.0632  0.0171  -0.0682 5   GLU   D N     
2660 C CA    . GLU   D 6   ? 0.4576 0.4742 0.3649 0.0524  0.0160  -0.0643 5   GLU   D CA    
2661 C C     . GLU   D 6   ? 0.4312 0.4525 0.3544 0.0399  0.0073  -0.0561 5   GLU   D C     
2662 O O     . GLU   D 6   ? 0.4426 0.4469 0.3621 0.0341  -0.0006 -0.0571 5   GLU   D O     
2663 C CB    . GLU   D 6   ? 0.5153 0.5110 0.3938 0.0503  0.0134  -0.0711 5   GLU   D CB    
2664 C CG    . GLU   D 6   ? 0.5647 0.5630 0.4279 0.0622  0.0243  -0.0789 5   GLU   D CG    
2665 C CD    . GLU   D 6   ? 0.6373 0.6148 0.4695 0.0597  0.0224  -0.0857 5   GLU   D CD    
2666 O OE1   . GLU   D 6   ? 0.7179 0.6695 0.5376 0.0542  0.0126  -0.0880 5   GLU   D OE1   
2667 O OE2   . GLU   D 6   ? 0.6929 0.6785 0.5121 0.0618  0.0303  -0.0888 5   GLU   D OE2   
2668 N N     . PHE   D 7   ? 0.3990 0.4420 0.3376 0.0354  0.0088  -0.0487 6   PHE   D N     
2669 C CA    . PHE   D 7   ? 0.3694 0.4192 0.3233 0.0263  0.0011  -0.0416 6   PHE   D CA    
2670 C C     . PHE   D 7   ? 0.3771 0.4337 0.3243 0.0208  -0.0010 -0.0375 6   PHE   D C     
2671 O O     . PHE   D 7   ? 0.3747 0.4435 0.3235 0.0220  0.0061  -0.0343 6   PHE   D O     
2672 C CB    . PHE   D 7   ? 0.3333 0.3975 0.3109 0.0283  0.0041  -0.0362 6   PHE   D CB    
2673 C CG    . PHE   D 7   ? 0.3106 0.3829 0.3046 0.0206  -0.0026 -0.0296 6   PHE   D CG    
2674 C CD1   . PHE   D 7   ? 0.3149 0.3801 0.3083 0.0132  -0.0120 -0.0304 6   PHE   D CD1   
2675 C CD2   . PHE   D 7   ? 0.2838 0.3721 0.2937 0.0207  0.0006  -0.0234 6   PHE   D CD2   
2676 C CE1   . PHE   D 7   ? 0.3006 0.3772 0.3103 0.0079  -0.0175 -0.0256 6   PHE   D CE1   
2677 C CE2   . PHE   D 7   ? 0.2774 0.3722 0.3013 0.0157  -0.0051 -0.0183 6   PHE   D CE2   
2678 C CZ    . PHE   D 7   ? 0.2862 0.3767 0.3105 0.0101  -0.0140 -0.0195 6   PHE   D CZ    
2679 N N     . SER   D 8   ? 0.3881 0.4354 0.3244 0.0147  -0.0108 -0.0384 7   SER   D N     
2680 C CA    . SER   D 8   ? 0.3991 0.4501 0.3291 0.0104  -0.0165 -0.0337 7   SER   D CA    
2681 C C     . SER   D 8   ? 0.3798 0.4416 0.3308 0.0073  -0.0243 -0.0281 7   SER   D C     
2682 O O     . SER   D 8   ? 0.3998 0.4613 0.3606 0.0041  -0.0302 -0.0306 7   SER   D O     
2683 C CB    . SER   D 8   ? 0.4293 0.4664 0.3362 0.0070  -0.0243 -0.0381 7   SER   D CB    
2684 O OG    . SER   D 8   ? 0.4758 0.5045 0.3610 0.0104  -0.0157 -0.0424 7   SER   D OG    
2685 N N     . MET   D 9   ? 0.3746 0.4441 0.3296 0.0075  -0.0245 -0.0213 8   MET   D N     
2686 C CA    . MET   D 9   ? 0.3780 0.4569 0.3499 0.0066  -0.0328 -0.0169 8   MET   D CA    
2687 C C     . MET   D 9   ? 0.3732 0.4493 0.3333 0.0077  -0.0374 -0.0112 8   MET   D C     
2688 O O     . MET   D 9   ? 0.3645 0.4329 0.3066 0.0073  -0.0310 -0.0092 8   MET   D O     
2689 C CB    . MET   D 9   ? 0.3835 0.4734 0.3793 0.0078  -0.0270 -0.0141 8   MET   D CB    
2690 C CG    . MET   D 9   ? 0.3992 0.4921 0.3953 0.0100  -0.0156 -0.0110 8   MET   D CG    
2691 S SD    . MET   D 9   ? 0.4517 0.5568 0.4707 0.0106  -0.0124 -0.0050 8   MET   D SD    
2692 C CE    . MET   D 9   ? 0.4300 0.5311 0.4406 0.0103  -0.0213 0.0005  8   MET   D CE    
2693 N N     . LYS   D 10  ? 0.3663 0.4485 0.3355 0.0093  -0.0484 -0.0091 9   LYS   D N     
2694 C CA    . LYS   D 10  ? 0.3829 0.4606 0.3430 0.0131  -0.0547 -0.0032 9   LYS   D CA    
2695 C C     . LYS   D 10  ? 0.3556 0.4454 0.3392 0.0165  -0.0560 -0.0001 9   LYS   D C     
2696 O O     . LYS   D 10  ? 0.3409 0.4454 0.3451 0.0166  -0.0609 -0.0037 9   LYS   D O     
2697 C CB    . LYS   D 10  ? 0.4236 0.4970 0.3697 0.0156  -0.0695 -0.0048 9   LYS   D CB    
2698 C CG    . LYS   D 10  ? 0.4682 0.5297 0.3963 0.0217  -0.0779 0.0014  9   LYS   D CG    
2699 C CD    . LYS   D 10  ? 0.5307 0.5858 0.4397 0.0251  -0.0932 -0.0007 9   LYS   D CD    
2700 C CE    . LYS   D 10  ? 0.5620 0.5950 0.4404 0.0309  -0.1007 0.0058  9   LYS   D CE    
2701 N NZ    . LYS   D 10  ? 0.6088 0.6232 0.4531 0.0282  -0.1049 0.0051  9   LYS   D NZ    
2702 N N     . MET   D 11  ? 0.3441 0.4277 0.3234 0.0182  -0.0514 0.0061  10  MET   D N     
2703 C CA    . MET   D 11  ? 0.3358 0.4263 0.3313 0.0229  -0.0541 0.0091  10  MET   D CA    
2704 C C     . MET   D 11  ? 0.3516 0.4305 0.3304 0.0302  -0.0657 0.0125  10  MET   D C     
2705 O O     . MET   D 11  ? 0.3692 0.4274 0.3204 0.0290  -0.0648 0.0170  10  MET   D O     
2706 C CB    . MET   D 11  ? 0.3381 0.4265 0.3377 0.0199  -0.0427 0.0133  10  MET   D CB    
2707 C CG    . MET   D 11  ? 0.3252 0.4198 0.3410 0.0246  -0.0447 0.0155  10  MET   D CG    
2708 S SD    . MET   D 11  ? 0.3246 0.4232 0.3523 0.0192  -0.0314 0.0180  10  MET   D SD    
2709 C CE    . MET   D 11  ? 0.3492 0.4272 0.3471 0.0137  -0.0263 0.0237  10  MET   D CE    
2710 N N     . THR   D 12  ? 0.3497 0.4422 0.3442 0.0378  -0.0762 0.0101  11  THR   D N     
2711 C CA    . THR   D 12  ? 0.3687 0.4525 0.3516 0.0490  -0.0884 0.0128  11  THR   D CA    
2712 C C     . THR   D 12  ? 0.3631 0.4575 0.3664 0.0559  -0.0880 0.0133  11  THR   D C     
2713 O O     . THR   D 12  ? 0.3311 0.4417 0.3585 0.0509  -0.0792 0.0113  11  THR   D O     
2714 C CB    . THR   D 12  ? 0.3728 0.4665 0.3549 0.0544  -0.1031 0.0079  11  THR   D CB    
2715 O OG1   . THR   D 12  ? 0.3471 0.4714 0.3618 0.0524  -0.1039 0.0012  11  THR   D OG1   
2716 C CG2   . THR   D 12  ? 0.3993 0.4799 0.3578 0.0476  -0.1037 0.0071  11  THR   D CG2   
2717 N N     . GLY   D 13  ? 0.3660 0.4496 0.3573 0.0685  -0.0985 0.0156  12  GLY   D N     
2718 C CA    . GLY   D 13  ? 0.3602 0.4517 0.3665 0.0787  -0.1005 0.0151  12  GLY   D CA    
2719 C C     . GLY   D 13  ? 0.3808 0.4386 0.3598 0.0803  -0.0972 0.0226  12  GLY   D C     
2720 O O     . GLY   D 13  ? 0.4239 0.4541 0.3706 0.0772  -0.0988 0.0274  12  GLY   D O     
2721 N N     . GLY   D 14  ? 0.3579 0.4161 0.3472 0.0833  -0.0922 0.0233  13  GLY   D N     
2722 C CA    . GLY   D 14  ? 0.4002 0.4233 0.3605 0.0850  -0.0910 0.0299  13  GLY   D CA    
2723 C C     . GLY   D 14  ? 0.3949 0.4194 0.3664 0.0937  -0.0900 0.0289  13  GLY   D C     
2724 O O     . GLY   D 14  ? 0.3452 0.4010 0.3493 0.0968  -0.0880 0.0232  13  GLY   D O     
2725 N N     . GLU   D 15  ? 0.4379 0.4255 0.3779 0.0981  -0.0925 0.0342  14  GLU   D N     
2726 C CA    . GLU   D 15  ? 0.4355 0.4151 0.3773 0.1062  -0.0915 0.0337  14  GLU   D CA    
2727 C C     . GLU   D 15  ? 0.4635 0.4579 0.4178 0.1293  -0.1039 0.0275  14  GLU   D C     
2728 O O     . GLU   D 15  ? 0.4879 0.4801 0.4321 0.1406  -0.1165 0.0265  14  GLU   D O     
2729 C CB    . GLU   D 15  ? 0.4679 0.3998 0.3682 0.1007  -0.0898 0.0412  14  GLU   D CB    
2730 C CG    . GLU   D 15  ? 0.4500 0.3783 0.3467 0.0771  -0.0754 0.0453  14  GLU   D CG    
2731 C CD    . GLU   D 15  ? 0.4930 0.3757 0.3478 0.0682  -0.0734 0.0524  14  GLU   D CD    
2732 O OE1   . GLU   D 15  ? 0.5507 0.3993 0.3685 0.0725  -0.0819 0.0566  14  GLU   D OE1   
2733 O OE2   . GLU   D 15  ? 0.4767 0.3568 0.3337 0.0556  -0.0634 0.0538  14  GLU   D OE2   
2734 N N     . ILE   D 16  ? 0.4857 0.4995 0.4643 0.1355  -0.0998 0.0227  15  ILE   D N     
2735 C CA    . ILE   D 16  ? 0.5085 0.5441 0.5048 0.1571  -0.1087 0.0152  15  ILE   D CA    
2736 C C     . ILE   D 16  ? 0.5358 0.5297 0.4987 0.1726  -0.1150 0.0178  15  ILE   D C     
2737 O O     . ILE   D 16  ? 0.5706 0.5375 0.5171 0.1621  -0.1061 0.0225  15  ILE   D O     
2738 C CB    . ILE   D 16  ? 0.5069 0.5824 0.5431 0.1535  -0.0985 0.0088  15  ILE   D CB    
2739 C CG1   . ILE   D 16  ? 0.4844 0.5965 0.5505 0.1374  -0.0920 0.0061  15  ILE   D CG1   
2740 C CG2   . ILE   D 16  ? 0.5285 0.6259 0.5814 0.1758  -0.1052 0.0004  15  ILE   D CG2   
2741 C CD1   . ILE   D 16  ? 0.4565 0.5925 0.5500 0.1270  -0.0788 0.0032  15  ILE   D CD1   
2742 N N     . PRO   D 17  ? 0.5622 0.5498 0.5144 0.1977  -0.1301 0.0143  16  PRO   D N     
2743 C CA    . PRO   D 17  ? 0.5995 0.5446 0.5187 0.2145  -0.1358 0.0158  16  PRO   D CA    
2744 C C     . PRO   D 17  ? 0.5710 0.5266 0.5075 0.2182  -0.1266 0.0110  16  PRO   D C     
2745 O O     . PRO   D 17  ? 0.5261 0.5289 0.5042 0.2130  -0.1181 0.0049  16  PRO   D O     
2746 C CB    . PRO   D 17  ? 0.6213 0.5647 0.5300 0.2430  -0.1552 0.0118  16  PRO   D CB    
2747 C CG    . PRO   D 17  ? 0.6093 0.5857 0.5371 0.2361  -0.1599 0.0106  16  PRO   D CG    
2748 C CD    . PRO   D 17  ? 0.5488 0.5656 0.5156 0.2121  -0.1437 0.0088  16  PRO   D CD    
2749 N N     . GLY   D 18  ? 0.6185 0.5260 0.5190 0.2249  -0.1277 0.0141  17  GLY   D N     
2750 C CA    . GLY   D 18  ? 0.6184 0.5261 0.5255 0.2340  -0.1221 0.0089  17  GLY   D CA    
2751 C C     . GLY   D 18  ? 0.5928 0.4917 0.5004 0.2084  -0.1060 0.0132  17  GLY   D C     
2752 O O     . GLY   D 18  ? 0.5904 0.4919 0.5003 0.1845  -0.0988 0.0191  17  GLY   D O     
2753 N N     . GLY   D 19  ? 0.5743 0.4617 0.4777 0.2150  -0.1014 0.0097  18  GLY   D N     
2754 C CA    . GLY   D 19  ? 0.5459 0.4316 0.4542 0.1938  -0.0873 0.0118  18  GLY   D CA    
2755 C C     . GLY   D 19  ? 0.5647 0.4018 0.4337 0.1730  -0.0849 0.0217  18  GLY   D C     
2756 O O     . GLY   D 19  ? 0.6145 0.4079 0.4437 0.1781  -0.0943 0.0266  18  GLY   D O     
2757 N N     . ASN   D 20  ? 0.5146 0.3613 0.3949 0.1492  -0.0726 0.0243  19  ASN   D N     
2758 C CA    . ASN   D 20  ? 0.5315 0.3407 0.3801 0.1267  -0.0682 0.0322  19  ASN   D CA    
2759 C C     . ASN   D 20  ? 0.5289 0.3433 0.3756 0.1131  -0.0687 0.0380  19  ASN   D C     
2760 O O     . ASN   D 20  ? 0.5254 0.3765 0.4022 0.0989  -0.0608 0.0380  19  ASN   D O     
2761 C CB    . ASN   D 20  ? 0.4916 0.3130 0.3546 0.1090  -0.0562 0.0317  19  ASN   D CB    
2762 C CG    . ASN   D 20  ? 0.5121 0.3072 0.3506 0.0829  -0.0508 0.0388  19  ASN   D CG    
2763 O OD1   . ASN   D 20  ? 0.5608 0.3200 0.3643 0.0767  -0.0551 0.0445  19  ASN   D OD1   
2764 N ND2   . ASN   D 20  ? 0.4950 0.3070 0.3495 0.0667  -0.0414 0.0383  19  ASN   D ND2   
2765 N N     . ILE   D 21  ? 0.5652 0.3398 0.3733 0.1169  -0.0776 0.0428  20  ILE   D N     
2766 C CA    . ILE   D 21  ? 0.5577 0.3351 0.3602 0.1061  -0.0787 0.0478  20  ILE   D CA    
2767 C C     . ILE   D 21  ? 0.5458 0.3178 0.3400 0.0759  -0.0672 0.0535  20  ILE   D C     
2768 O O     . ILE   D 21  ? 0.5310 0.3176 0.3305 0.0645  -0.0644 0.0562  20  ILE   D O     
2769 C CB    . ILE   D 21  ? 0.6057 0.3407 0.3665 0.1203  -0.0924 0.0513  20  ILE   D CB    
2770 C CG1   . ILE   D 21  ? 0.6660 0.3348 0.3709 0.1158  -0.0951 0.0569  20  ILE   D CG1   
2771 C CG2   . ILE   D 21  ? 0.6035 0.3577 0.3813 0.1513  -0.1045 0.0443  20  ILE   D CG2   
2772 C CD1   . ILE   D 21  ? 0.7276 0.3496 0.3844 0.1199  -0.1060 0.0631  20  ILE   D CD1   
2773 N N     . VAL   D 22  ? 0.5520 0.3036 0.3323 0.0633  -0.0609 0.0549  21  VAL   D N     
2774 C CA    . VAL   D 22  ? 0.5467 0.3052 0.3283 0.0350  -0.0496 0.0584  21  VAL   D CA    
2775 C C     . VAL   D 22  ? 0.4862 0.3029 0.3182 0.0306  -0.0419 0.0546  21  VAL   D C     
2776 O O     . VAL   D 22  ? 0.4731 0.3052 0.3108 0.0145  -0.0357 0.0570  21  VAL   D O     
2777 C CB    . VAL   D 22  ? 0.5763 0.3046 0.3346 0.0216  -0.0453 0.0597  21  VAL   D CB    
2778 C CG1   . VAL   D 22  ? 0.5627 0.3074 0.3278 -0.0078 -0.0340 0.0622  21  VAL   D CG1   
2779 C CG2   . VAL   D 22  ? 0.6463 0.3092 0.3476 0.0248  -0.0535 0.0640  21  VAL   D CG2   
2780 N N     . LEU   D 23  ? 0.4570 0.3038 0.3224 0.0453  -0.0423 0.0486  22  LEU   D N     
2781 C CA    . LEU   D 23  ? 0.4075 0.3038 0.3165 0.0435  -0.0366 0.0449  22  LEU   D CA    
2782 C C     . LEU   D 23  ? 0.3922 0.3102 0.3205 0.0624  -0.0436 0.0407  22  LEU   D C     
2783 O O     . LEU   D 23  ? 0.3598 0.3097 0.3196 0.0696  -0.0416 0.0354  22  LEU   D O     
2784 C CB    . LEU   D 23  ? 0.3869 0.2999 0.3163 0.0406  -0.0301 0.0415  22  LEU   D CB    
2785 C CG    . LEU   D 23  ? 0.4146 0.3077 0.3258 0.0226  -0.0246 0.0445  22  LEU   D CG    
2786 C CD1   . LEU   D 23  ? 0.3908 0.3024 0.3231 0.0219  -0.0195 0.0407  22  LEU   D CD1   
2787 C CD2   . LEU   D 23  ? 0.4152 0.3163 0.3246 0.0023  -0.0189 0.0485  22  LEU   D CD2   
2788 N N     . GLN   D 24  ? 0.4120 0.3150 0.3215 0.0680  -0.0513 0.0431  23  GLN   D N     
2789 C CA    . GLN   D 24  ? 0.4089 0.3265 0.3299 0.0879  -0.0610 0.0389  23  GLN   D CA    
2790 C C     . GLN   D 24  ? 0.3689 0.3352 0.3319 0.0863  -0.0571 0.0342  23  GLN   D C     
2791 O O     . GLN   D 24  ? 0.3536 0.3356 0.3285 0.0705  -0.0493 0.0357  23  GLN   D O     
2792 C CB    . GLN   D 24  ? 0.4450 0.3368 0.3359 0.0919  -0.0703 0.0430  23  GLN   D CB    
2793 C CG    . GLN   D 24  ? 0.4660 0.3642 0.3603 0.1164  -0.0838 0.0386  23  GLN   D CG    
2794 C CD    . GLN   D 24  ? 0.5211 0.3775 0.3726 0.1251  -0.0958 0.0432  23  GLN   D CD    
2795 O OE1   . GLN   D 24  ? 0.5630 0.3784 0.3762 0.1123  -0.0938 0.0503  23  GLN   D OE1   
2796 N NE2   . GLN   D 24  ? 0.5236 0.3906 0.3804 0.1469  -0.1089 0.0390  23  GLN   D NE2   
2797 N N     . GLY   D 25  ? 0.3670 0.3573 0.3522 0.1027  -0.0622 0.0278  24  GLY   D N     
2798 C CA    . GLY   D 25  ? 0.3299 0.3632 0.3508 0.1013  -0.0601 0.0228  24  GLY   D CA    
2799 C C     . GLY   D 25  ? 0.3438 0.3816 0.3615 0.0964  -0.0642 0.0245  24  GLY   D C     
2800 O O     . GLY   D 25  ? 0.3836 0.3951 0.3732 0.1016  -0.0725 0.0279  24  GLY   D O     
2801 N N     . VAL   D 26  ? 0.3174 0.3849 0.3603 0.0865  -0.0588 0.0221  25  VAL   D N     
2802 C CA    . VAL   D 26  ? 0.3194 0.3934 0.3611 0.0811  -0.0618 0.0225  25  VAL   D CA    
2803 C C     . VAL   D 26  ? 0.2957 0.4071 0.3686 0.0833  -0.0637 0.0155  25  VAL   D C     
2804 O O     . VAL   D 26  ? 0.2712 0.4036 0.3674 0.0811  -0.0575 0.0119  25  VAL   D O     
2805 C CB    . VAL   D 26  ? 0.3140 0.3811 0.3490 0.0636  -0.0520 0.0266  25  VAL   D CB    
2806 C CG1   . VAL   D 26  ? 0.3452 0.3785 0.3495 0.0580  -0.0494 0.0330  25  VAL   D CG1   
2807 C CG2   . VAL   D 26  ? 0.2901 0.3785 0.3500 0.0542  -0.0415 0.0246  25  VAL   D CG2   
2808 N N     . LYS   D 27  ? 0.3000 0.4181 0.3709 0.0862  -0.0722 0.0136  26  LYS   D N     
2809 C CA    . LYS   D 27  ? 0.2861 0.4361 0.3815 0.0822  -0.0734 0.0077  26  LYS   D CA    
2810 C C     . LYS   D 27  ? 0.2994 0.4404 0.3808 0.0736  -0.0748 0.0095  26  LYS   D C     
2811 O O     . LYS   D 27  ? 0.3130 0.4378 0.3727 0.0802  -0.0841 0.0115  26  LYS   D O     
2812 C CB    . LYS   D 27  ? 0.2999 0.4754 0.4113 0.0957  -0.0843 0.0008  26  LYS   D CB    
2813 C CG    . LYS   D 27  ? 0.2981 0.5088 0.4354 0.0880  -0.0853 -0.0061 26  LYS   D CG    
2814 C CD    . LYS   D 27  ? 0.3038 0.5509 0.4683 0.0971  -0.0895 -0.0142 26  LYS   D CD    
2815 C CE    . LYS   D 27  ? 0.2915 0.5739 0.4816 0.0850  -0.0882 -0.0211 26  LYS   D CE    
2816 N NZ    . LYS   D 27  ? 0.2790 0.5942 0.4967 0.0856  -0.0829 -0.0275 26  LYS   D NZ    
2817 N N     . LEU   D 28  ? 0.2784 0.4296 0.3713 0.0602  -0.0663 0.0082  27  LEU   D N     
2818 C CA    . LEU   D 28  ? 0.2692 0.4106 0.3486 0.0513  -0.0644 0.0094  27  LEU   D CA    
2819 C C     . LEU   D 28  ? 0.2555 0.4185 0.3520 0.0450  -0.0657 0.0032  27  LEU   D C     
2820 O O     . LEU   D 28  ? 0.2153 0.3976 0.3341 0.0415  -0.0620 -0.0004 27  LEU   D O     
2821 C CB    . LEU   D 28  ? 0.2519 0.3794 0.3237 0.0424  -0.0523 0.0139  27  LEU   D CB    
2822 C CG    . LEU   D 28  ? 0.2679 0.3721 0.3194 0.0444  -0.0504 0.0200  27  LEU   D CG    
2823 C CD1   . LEU   D 28  ? 0.2612 0.3620 0.3144 0.0351  -0.0384 0.0228  27  LEU   D CD1   
2824 C CD2   . LEU   D 28  ? 0.2940 0.3767 0.3164 0.0449  -0.0555 0.0233  27  LEU   D CD2   
2825 N N     . ARG   D 29  ? 0.2848 0.4429 0.3683 0.0428  -0.0714 0.0018  28  ARG   D N     
2826 C CA    . ARG   D 29  ? 0.2927 0.4635 0.3853 0.0341  -0.0717 -0.0038 28  ARG   D CA    
2827 C C     . ARG   D 29  ? 0.2815 0.4335 0.3549 0.0271  -0.0658 -0.0023 28  ARG   D C     
2828 O O     . ARG   D 29  ? 0.2963 0.4315 0.3471 0.0300  -0.0686 0.0008  28  ARG   D O     
2829 C CB    . ARG   D 29  ? 0.3242 0.5114 0.4214 0.0375  -0.0852 -0.0093 28  ARG   D CB    
2830 C CG    . ARG   D 29  ? 0.3522 0.5543 0.4620 0.0253  -0.0842 -0.0157 28  ARG   D CG    
2831 C CD    . ARG   D 29  ? 0.4027 0.6276 0.5220 0.0245  -0.0966 -0.0226 28  ARG   D CD    
2832 N NE    . ARG   D 29  ? 0.4491 0.6937 0.5801 0.0378  -0.1066 -0.0240 28  ARG   D NE    
2833 C CZ    . ARG   D 29  ? 0.4652 0.7420 0.6232 0.0394  -0.1086 -0.0292 28  ARG   D CZ    
2834 N NH1   . ARG   D 29  ? 0.4608 0.7507 0.6377 0.0294  -0.0980 -0.0311 28  ARG   D NH1   
2835 N NH2   . ARG   D 29  ? 0.4948 0.7908 0.6598 0.0528  -0.1214 -0.0324 28  ARG   D NH2   
2836 N N     . ILE   D 30  ? 0.2705 0.4243 0.3512 0.0186  -0.0578 -0.0048 29  ILE   D N     
2837 C CA    . ILE   D 30  ? 0.2755 0.4150 0.3403 0.0136  -0.0525 -0.0056 29  ILE   D CA    
2838 C C     . ILE   D 30  ? 0.2653 0.4099 0.3320 0.0072  -0.0576 -0.0123 29  ILE   D C     
2839 O O     . ILE   D 30  ? 0.2454 0.4015 0.3287 0.0018  -0.0568 -0.0154 29  ILE   D O     
2840 C CB    . ILE   D 30  ? 0.2752 0.4095 0.3434 0.0112  -0.0403 -0.0037 29  ILE   D CB    
2841 C CG1   . ILE   D 30  ? 0.2793 0.4078 0.3423 0.0150  -0.0354 0.0025  29  ILE   D CG1   
2842 C CG2   . ILE   D 30  ? 0.2904 0.4139 0.3462 0.0077  -0.0351 -0.0070 29  ILE   D CG2   
2843 C CD1   . ILE   D 30  ? 0.2703 0.4032 0.3469 0.0140  -0.0269 0.0045  29  ILE   D CD1   
2844 N N     . VAL   D 31  ? 0.2766 0.4104 0.3236 0.0064  -0.0620 -0.0144 30  VAL   D N     
2845 C CA    . VAL   D 31  ? 0.2982 0.4311 0.3411 -0.0011 -0.0661 -0.0210 30  VAL   D CA    
2846 C C     . VAL   D 31  ? 0.3185 0.4304 0.3391 -0.0020 -0.0593 -0.0221 30  VAL   D C     
2847 O O     . VAL   D 31  ? 0.3344 0.4367 0.3386 0.0027  -0.0572 -0.0188 30  VAL   D O     
2848 C CB    . VAL   D 31  ? 0.3202 0.4634 0.3614 -0.0016 -0.0804 -0.0248 30  VAL   D CB    
2849 C CG1   . VAL   D 31  ? 0.3444 0.4762 0.3633 0.0058  -0.0868 -0.0218 30  VAL   D CG1   
2850 C CG2   . VAL   D 31  ? 0.3542 0.4959 0.3907 -0.0124 -0.0843 -0.0323 30  VAL   D CG2   
2851 N N     . GLY   D 32  ? 0.3089 0.4131 0.3272 -0.0082 -0.0560 -0.0272 31  GLY   D N     
2852 C CA    . GLY   D 32  ? 0.3241 0.4089 0.3214 -0.0070 -0.0494 -0.0297 31  GLY   D CA    
2853 C C     . GLY   D 32  ? 0.3223 0.3942 0.3140 -0.0131 -0.0481 -0.0360 31  GLY   D C     
2854 O O     . GLY   D 32  ? 0.3179 0.3954 0.3208 -0.0212 -0.0523 -0.0382 31  GLY   D O     
2855 N N     . GLU   D 33  ? 0.3341 0.3882 0.3072 -0.0091 -0.0414 -0.0390 32  GLU   D N     
2856 C CA    . GLU   D 33  ? 0.3525 0.3862 0.3122 -0.0122 -0.0400 -0.0453 32  GLU   D CA    
2857 C C     . GLU   D 33  ? 0.3495 0.3737 0.3044 -0.0020 -0.0289 -0.0455 32  GLU   D C     
2858 O O     . GLU   D 33  ? 0.3460 0.3727 0.2933 0.0056  -0.0232 -0.0450 32  GLU   D O     
2859 C CB    . GLU   D 33  ? 0.3868 0.4052 0.3218 -0.0162 -0.0461 -0.0518 32  GLU   D CB    
2860 C CG    . GLU   D 33  ? 0.4181 0.4124 0.3383 -0.0227 -0.0471 -0.0588 32  GLU   D CG    
2861 C CD    . GLU   D 33  ? 0.4607 0.4335 0.3508 -0.0235 -0.0501 -0.0660 32  GLU   D CD    
2862 O OE1   . GLU   D 33  ? 0.5025 0.4715 0.3793 -0.0137 -0.0445 -0.0667 32  GLU   D OE1   
2863 O OE2   . GLU   D 33  ? 0.4821 0.4416 0.3608 -0.0348 -0.0573 -0.0715 32  GLU   D OE2   
2864 N N     . TRP   D 34  ? 0.3545 0.3672 0.3114 -0.0024 -0.0265 -0.0469 33  TRP   D N     
2865 C CA    . TRP   D 34  ? 0.3677 0.3722 0.3220 0.0088  -0.0180 -0.0475 33  TRP   D CA    
2866 C C     . TRP   D 34  ? 0.3982 0.3716 0.3264 0.0104  -0.0186 -0.0553 33  TRP   D C     
2867 O O     . TRP   D 34  ? 0.4364 0.3937 0.3585 0.0004  -0.0239 -0.0571 33  TRP   D O     
2868 C CB    . TRP   D 34  ? 0.3553 0.3676 0.3295 0.0077  -0.0164 -0.0422 33  TRP   D CB    
2869 C CG    . TRP   D 34  ? 0.3664 0.3724 0.3404 0.0197  -0.0097 -0.0422 33  TRP   D CG    
2870 C CD1   . TRP   D 34  ? 0.4006 0.3804 0.3584 0.0249  -0.0091 -0.0464 33  TRP   D CD1   
2871 C CD2   . TRP   D 34  ? 0.3609 0.3881 0.3515 0.0283  -0.0035 -0.0378 33  TRP   D CD2   
2872 N NE1   . TRP   D 34  ? 0.4009 0.3863 0.3657 0.0381  -0.0037 -0.0449 33  TRP   D NE1   
2873 C CE2   . TRP   D 34  ? 0.3735 0.3897 0.3593 0.0396  0.0001  -0.0400 33  TRP   D CE2   
2874 C CE3   . TRP   D 34  ? 0.3361 0.3886 0.3430 0.0274  -0.0012 -0.0324 33  TRP   D CE3   
2875 C CZ2   . TRP   D 34  ? 0.3610 0.3961 0.3613 0.0491  0.0055  -0.0373 33  TRP   D CZ2   
2876 C CZ3   . TRP   D 34  ? 0.3312 0.3992 0.3505 0.0348  0.0049  -0.0295 33  TRP   D CZ3   
2877 C CH2   . TRP   D 34  ? 0.3331 0.3948 0.3507 0.0453  0.0081  -0.0322 33  TRP   D CH2   
2878 N N     . VAL   D 35  ? 0.4119 0.3764 0.3236 0.0221  -0.0131 -0.0603 34  VAL   D N     
2879 C CA    . VAL   D 35  ? 0.4570 0.3889 0.3398 0.0260  -0.0138 -0.0688 34  VAL   D CA    
2880 C C     . VAL   D 35  ? 0.4778 0.4023 0.3578 0.0434  -0.0065 -0.0711 34  VAL   D C     
2881 O O     . VAL   D 35  ? 0.4743 0.4208 0.3644 0.0543  0.0009  -0.0705 34  VAL   D O     
2882 C CB    . VAL   D 35  ? 0.4683 0.3952 0.3304 0.0266  -0.0140 -0.0746 34  VAL   D CB    
2883 C CG1   . VAL   D 35  ? 0.5074 0.3966 0.3367 0.0287  -0.0160 -0.0840 34  VAL   D CG1   
2884 C CG2   . VAL   D 35  ? 0.4589 0.4006 0.3270 0.0128  -0.0217 -0.0711 34  VAL   D CG2   
2885 N N     . LEU   D 36  ? 0.5161 0.4105 0.3819 0.0459  -0.0089 -0.0738 35  LEU   D N     
2886 C CA    . LEU   D 36  ? 0.5427 0.4231 0.3982 0.0656  -0.0041 -0.0781 35  LEU   D CA    
2887 C C     . LEU   D 36  ? 0.5915 0.4352 0.4109 0.0720  -0.0053 -0.0883 35  LEU   D C     
2888 O O     . LEU   D 36  ? 0.6266 0.4406 0.4255 0.0585  -0.0120 -0.0906 35  LEU   D O     
2889 C CB    . LEU   D 36  ? 0.5531 0.4193 0.4117 0.0675  -0.0064 -0.0742 35  LEU   D CB    
2890 C CG    . LEU   D 36  ? 0.5219 0.4216 0.4135 0.0660  -0.0042 -0.0653 35  LEU   D CG    
2891 C CD1   . LEU   D 36  ? 0.5333 0.4102 0.4194 0.0667  -0.0075 -0.0623 35  LEU   D CD1   
2892 C CD2   . LEU   D 36  ? 0.5083 0.4417 0.4182 0.0815  0.0033  -0.0653 35  LEU   D CD2   
2893 N N     . LYS   D 37  ? 0.6105 0.4574 0.4223 0.0923  0.0015  -0.0949 36  LYS   D N     
2894 C CA    . LYS   D 37  ? 0.6794 0.4915 0.4560 0.1034  0.0018  -0.1058 36  LYS   D CA    
2895 C C     . LYS   D 37  ? 0.6925 0.4904 0.4614 0.1275  0.0042  -0.1102 36  LYS   D C     
2896 O O     . LYS   D 37  ? 0.6329 0.4644 0.4272 0.1399  0.0096  -0.1076 36  LYS   D O     
2897 C CB    . LYS   D 37  ? 0.6971 0.5278 0.4691 0.1082  0.0086  -0.1116 36  LYS   D CB    
2898 C CG    . LYS   D 37  ? 0.7080 0.5496 0.4826 0.0871  0.0049  -0.1080 36  LYS   D CG    
2899 C CD    . LYS   D 37  ? 0.7393 0.5826 0.4951 0.0898  0.0095  -0.1151 36  LYS   D CD    
2900 C CE    . LYS   D 37  ? 0.7421 0.5942 0.4995 0.0695  0.0033  -0.1105 36  LYS   D CE    
2901 N NZ    . LYS   D 37  ? 0.7707 0.6130 0.5012 0.0693  0.0049  -0.1177 36  LYS   D NZ    
2902 N N     . GLY   D 38  ? 0.7524 0.4994 0.4845 0.1340  -0.0005 -0.1172 37  GLY   D N     
2903 C CA    . GLY   D 38  ? 0.8053 0.5328 0.5216 0.1617  0.0010  -0.1241 37  GLY   D CA    
2904 C C     . GLY   D 38  ? 0.8539 0.6068 0.5721 0.1829  0.0106  -0.1336 37  GLY   D C     
2905 O O     . GLY   D 38  ? 0.8487 0.6192 0.5682 0.1740  0.0151  -0.1358 37  GLY   D O     
2906 N N     . SER   D 39  ? 0.9441 0.6997 0.6619 0.2111  0.0133  -0.1394 38  SER   D N     
2907 C CA    . SER   D 39  ? 1.0433 0.8206 0.7596 0.2346  0.0227  -0.1508 38  SER   D CA    
2908 C C     . SER   D 39  ? 1.1656 0.8923 0.8356 0.2418  0.0211  -0.1624 38  SER   D C     
2909 O O     . SER   D 39  ? 1.1391 0.8739 0.8012 0.2352  0.0267  -0.1674 38  SER   D O     
2910 C CB    . SER   D 39  ? 1.0662 0.8658 0.7981 0.2636  0.0252  -0.1545 38  SER   D CB    
2911 O OG    . SER   D 39  ? 1.1004 0.8624 0.8191 0.2713  0.0150  -0.1510 38  SER   D OG    
2912 N N     . SER   D 40  ? 1.2996 0.9712 0.9366 0.2547  0.0129  -0.1661 39  SER   D N     
2913 C CA    . SER   D 40  ? 1.4187 1.0354 1.0069 0.2667  0.0108  -0.1784 39  SER   D CA    
2914 C C     . SER   D 40  ? 1.4296 1.0154 0.9955 0.2353  0.0059  -0.1762 39  SER   D C     
2915 O O     . SER   D 40  ? 1.4226 0.9750 0.9771 0.2142  -0.0034 -0.1689 39  SER   D O     
2916 C CB    . SER   D 40  ? 1.4729 1.0356 1.0286 0.2903  0.0028  -0.1829 39  SER   D CB    
2917 O OG    . SER   D 40  ? 1.4505 0.9879 1.0054 0.2753  -0.0067 -0.1714 39  SER   D OG    
2918 N N     . GLY   D 41  ? 1.4421 1.0481 1.0068 0.2306  0.0129  -0.1818 40  GLY   D N     
2919 C CA    . GLY   D 41  ? 1.3812 0.9722 0.9314 0.2018  0.0088  -0.1801 40  GLY   D CA    
2920 C C     . GLY   D 41  ? 1.2807 0.9096 0.8693 0.1741  0.0061  -0.1657 40  GLY   D C     
2921 O O     . GLY   D 41  ? 1.1939 0.8762 0.8218 0.1773  0.0128  -0.1598 40  GLY   D O     
2922 N N     . GLU   D 42  ? 1.2708 0.8710 0.8461 0.1476  -0.0037 -0.1611 41  GLU   D N     
2923 C CA    . GLU   D 42  ? 1.2140 0.8439 0.8207 0.1212  -0.0078 -0.1490 41  GLU   D CA    
2924 C C     . GLU   D 42  ? 1.1608 0.7472 0.7481 0.1014  -0.0186 -0.1458 41  GLU   D C     
2925 O O     . GLU   D 42  ? 1.1457 0.6960 0.7012 0.0870  -0.0247 -0.1512 41  GLU   D O     
2926 C CB    . GLU   D 42  ? 1.2636 0.9184 0.8749 0.1071  -0.0065 -0.1495 41  GLU   D CB    
2927 C CG    . GLU   D 42  ? 1.3213 1.0283 0.9597 0.1184  0.0045  -0.1485 41  GLU   D CG    
2928 C CD    . GLU   D 42  ? 1.3759 1.1013 1.0129 0.1038  0.0049  -0.1483 41  GLU   D CD    
2929 O OE1   . GLU   D 42  ? 1.3453 1.0936 1.0048 0.0845  -0.0003 -0.1387 41  GLU   D OE1   
2930 O OE2   . GLU   D 42  ? 1.3500 1.0657 0.9618 0.1125  0.0100  -0.1578 41  GLU   D OE2   
2931 N N     . SER   D 43  ? 1.0662 0.6532 0.6691 0.1011  -0.0205 -0.1380 42  SER   D N     
2932 C CA    . SER   D 43  ? 1.0056 0.5911 0.6189 0.0730  -0.0275 -0.1293 42  SER   D CA    
2933 C C     . SER   D 43  ? 0.9090 0.5575 0.5723 0.0663  -0.0238 -0.1196 42  SER   D C     
2934 O O     . SER   D 43  ? 0.8702 0.5506 0.5580 0.0843  -0.0171 -0.1169 42  SER   D O     
2935 C CB    . SER   D 43  ? 1.0361 0.5814 0.6319 0.0719  -0.0318 -0.1264 42  SER   D CB    
2936 O OG    . SER   D 43  ? 1.0722 0.6312 0.6836 0.0961  -0.0274 -0.1235 42  SER   D OG    
2937 N N     . VAL   D 44  ? 0.8454 0.5112 0.5220 0.0408  -0.0287 -0.1152 43  VAL   D N     
2938 C CA    . VAL   D 44  ? 0.7733 0.4934 0.4896 0.0341  -0.0267 -0.1079 43  VAL   D CA    
2939 C C     . VAL   D 44  ? 0.7380 0.4692 0.4744 0.0122  -0.0321 -0.0998 43  VAL   D C     
2940 O O     . VAL   D 44  ? 0.7486 0.4531 0.4666 -0.0065 -0.0388 -0.1020 43  VAL   D O     
2941 C CB    . VAL   D 44  ? 0.7581 0.4922 0.4693 0.0297  -0.0273 -0.1121 43  VAL   D CB    
2942 C CG1   . VAL   D 44  ? 0.7165 0.5012 0.4640 0.0236  -0.0261 -0.1041 43  VAL   D CG1   
2943 C CG2   . VAL   D 44  ? 0.7843 0.5083 0.4752 0.0521  -0.0199 -0.1206 43  VAL   D CG2   
2944 N N     . ARG   D 45  ? 0.6817 0.4519 0.4544 0.0146  -0.0285 -0.0912 44  ARG   D N     
2945 C CA    . ARG   D 45  ? 0.6682 0.4552 0.4637 -0.0031 -0.0318 -0.0837 44  ARG   D CA    
2946 C C     . ARG   D 45  ? 0.5834 0.4190 0.4121 -0.0066 -0.0313 -0.0784 44  ARG   D C     
2947 O O     . ARG   D 45  ? 0.5540 0.4130 0.3990 0.0080  -0.0252 -0.0755 44  ARG   D O     
2948 C CB    . ARG   D 45  ? 0.7097 0.4909 0.5125 0.0055  -0.0283 -0.0786 44  ARG   D CB    
2949 C CG    . ARG   D 45  ? 0.7758 0.5672 0.5952 -0.0150 -0.0313 -0.0722 44  ARG   D CG    
2950 C CD    . ARG   D 45  ? 0.8489 0.6297 0.6708 -0.0096 -0.0286 -0.0668 44  ARG   D CD    
2951 N NE    . ARG   D 45  ? 0.8786 0.7022 0.7376 -0.0053 -0.0247 -0.0592 44  ARG   D NE    
2952 C CZ    . ARG   D 45  ? 0.9892 0.8126 0.8565 -0.0050 -0.0229 -0.0534 44  ARG   D CZ    
2953 N NH1   . ARG   D 45  ? 1.0856 0.8699 0.9271 0.0021  -0.0235 -0.0541 44  ARG   D NH1   
2954 N NH2   . ARG   D 45  ? 0.9865 0.8474 0.8858 -0.0094 -0.0208 -0.0470 44  ARG   D NH2   
2955 N N     . ARG   D 46  ? 0.5434 0.3933 0.3817 -0.0258 -0.0380 -0.0773 45  ARG   D N     
2956 C CA    . ARG   D 46  ? 0.5040 0.3946 0.3689 -0.0290 -0.0399 -0.0729 45  ARG   D CA    
2957 C C     . ARG   D 46  ? 0.4683 0.3814 0.3602 -0.0411 -0.0419 -0.0669 45  ARG   D C     
2958 O O     . ARG   D 46  ? 0.4774 0.3780 0.3630 -0.0572 -0.0460 -0.0689 45  ARG   D O     
2959 C CB    . ARG   D 46  ? 0.5150 0.4053 0.3667 -0.0380 -0.0475 -0.0782 45  ARG   D CB    
2960 C CG    . ARG   D 46  ? 0.5496 0.4073 0.3660 -0.0306 -0.0464 -0.0864 45  ARG   D CG    
2961 C CD    . ARG   D 46  ? 0.5590 0.4205 0.3642 -0.0397 -0.0545 -0.0907 45  ARG   D CD    
2962 N NE    . ARG   D 46  ? 0.5305 0.4200 0.3487 -0.0295 -0.0517 -0.0866 45  ARG   D NE    
2963 C CZ    . ARG   D 46  ? 0.5367 0.4220 0.3396 -0.0168 -0.0458 -0.0891 45  ARG   D CZ    
2964 N NH1   . ARG   D 46  ? 0.5105 0.4222 0.3268 -0.0115 -0.0435 -0.0837 45  ARG   D NH1   
2965 N NH2   . ARG   D 46  ? 0.5698 0.4238 0.3423 -0.0099 -0.0423 -0.0972 45  ARG   D NH2   
2966 N N     . THR   D 47  ? 0.4281 0.3736 0.3480 -0.0341 -0.0385 -0.0600 46  THR   D N     
2967 C CA    . THR   D 47  ? 0.4000 0.3698 0.3465 -0.0428 -0.0394 -0.0546 46  THR   D CA    
2968 C C     . THR   D 47  ? 0.3727 0.3770 0.3401 -0.0412 -0.0428 -0.0514 46  THR   D C     
2969 O O     . THR   D 47  ? 0.3603 0.3740 0.3322 -0.0285 -0.0387 -0.0480 46  THR   D O     
2970 C CB    . THR   D 47  ? 0.3890 0.3563 0.3440 -0.0336 -0.0319 -0.0495 46  THR   D CB    
2971 O OG1   . THR   D 47  ? 0.4098 0.3406 0.3405 -0.0328 -0.0303 -0.0527 46  THR   D OG1   
2972 C CG2   . THR   D 47  ? 0.3706 0.3587 0.3495 -0.0424 -0.0316 -0.0444 46  THR   D CG2   
2973 N N     . ASP   D 48  ? 0.3705 0.3934 0.3498 -0.0540 -0.0505 -0.0526 47  ASP   D N     
2974 C CA    . ASP   D 48  ? 0.3518 0.4073 0.3525 -0.0511 -0.0549 -0.0491 47  ASP   D CA    
2975 C C     . ASP   D 48  ? 0.3231 0.3964 0.3475 -0.0462 -0.0491 -0.0426 47  ASP   D C     
2976 O O     . ASP   D 48  ? 0.3196 0.3892 0.3494 -0.0531 -0.0455 -0.0421 47  ASP   D O     
2977 C CB    . ASP   D 48  ? 0.3625 0.4359 0.3701 -0.0639 -0.0656 -0.0535 47  ASP   D CB    
2978 C CG    . ASP   D 48  ? 0.4005 0.4593 0.3845 -0.0680 -0.0730 -0.0598 47  ASP   D CG    
2979 O OD1   . ASP   D 48  ? 0.4082 0.4534 0.3750 -0.0572 -0.0715 -0.0594 47  ASP   D OD1   
2980 O OD2   . ASP   D 48  ? 0.4489 0.5118 0.4318 -0.0831 -0.0805 -0.0654 47  ASP   D OD2   
2981 N N     . VAL   D 49  ? 0.3121 0.4007 0.3463 -0.0352 -0.0484 -0.0378 48  VAL   D N     
2982 C CA    . VAL   D 49  ? 0.3067 0.4095 0.3595 -0.0287 -0.0431 -0.0316 48  VAL   D CA    
2983 C C     . VAL   D 49  ? 0.3077 0.4354 0.3757 -0.0267 -0.0502 -0.0299 48  VAL   D C     
2984 O O     . VAL   D 49  ? 0.3012 0.4287 0.3595 -0.0217 -0.0554 -0.0299 48  VAL   D O     
2985 C CB    . VAL   D 49  ? 0.3115 0.4055 0.3578 -0.0168 -0.0354 -0.0275 48  VAL   D CB    
2986 C CG1   . VAL   D 49  ? 0.3051 0.4129 0.3695 -0.0120 -0.0307 -0.0214 48  VAL   D CG1   
2987 C CG2   . VAL   D 49  ? 0.3277 0.3986 0.3584 -0.0146 -0.0294 -0.0302 48  VAL   D CG2   
2988 N N     . LYS   D 50  ? 0.3006 0.4482 0.3900 -0.0300 -0.0504 -0.0290 49  LYS   D N     
2989 C CA    . LYS   D 50  ? 0.3049 0.4756 0.4100 -0.0235 -0.0555 -0.0269 49  LYS   D CA    
2990 C C     . LYS   D 50  ? 0.2862 0.4628 0.4055 -0.0192 -0.0478 -0.0221 49  LYS   D C     
2991 O O     . LYS   D 50  ? 0.2700 0.4489 0.3975 -0.0270 -0.0429 -0.0231 49  LYS   D O     
2992 C CB    . LYS   D 50  ? 0.3457 0.5398 0.4631 -0.0312 -0.0650 -0.0329 49  LYS   D CB    
2993 C CG    . LYS   D 50  ? 0.3804 0.6022 0.5163 -0.0220 -0.0717 -0.0323 49  LYS   D CG    
2994 C CD    . LYS   D 50  ? 0.4307 0.6807 0.5794 -0.0273 -0.0829 -0.0395 49  LYS   D CD    
2995 C CE    . LYS   D 50  ? 0.4270 0.7120 0.6031 -0.0236 -0.0850 -0.0417 49  LYS   D CE    
2996 N NZ    . LYS   D 50  ? 0.4203 0.7355 0.6118 -0.0359 -0.0918 -0.0503 49  LYS   D NZ    
2997 N N     . VAL   D 51  ? 0.2612 0.4368 0.3796 -0.0081 -0.0468 -0.0169 50  VAL   D N     
2998 C CA    . VAL   D 51  ? 0.2370 0.4166 0.3660 -0.0034 -0.0406 -0.0124 50  VAL   D CA    
2999 C C     . VAL   D 51  ? 0.2417 0.4355 0.3787 0.0054  -0.0468 -0.0112 50  VAL   D C     
3000 O O     . VAL   D 51  ? 0.2666 0.4555 0.3922 0.0116  -0.0535 -0.0102 50  VAL   D O     
3001 C CB    . VAL   D 51  ? 0.2331 0.3951 0.3508 0.0005  -0.0328 -0.0077 50  VAL   D CB    
3002 C CG1   . VAL   D 51  ? 0.2281 0.3934 0.3552 0.0042  -0.0272 -0.0033 50  VAL   D CG1   
3003 C CG2   . VAL   D 51  ? 0.2513 0.3993 0.3602 -0.0046 -0.0279 -0.0098 50  VAL   D CG2   
3004 N N     . ASP   D 52  ? 0.2402 0.4499 0.3948 0.0066  -0.0449 -0.0115 51  ASP   D N     
3005 C CA    . ASP   D 52  ? 0.2347 0.4567 0.3971 0.0174  -0.0499 -0.0110 51  ASP   D CA    
3006 C C     . ASP   D 52  ? 0.2223 0.4376 0.3869 0.0210  -0.0420 -0.0065 51  ASP   D C     
3007 O O     . ASP   D 52  ? 0.1889 0.4107 0.3644 0.0149  -0.0350 -0.0074 51  ASP   D O     
3008 C CB    . ASP   D 52  ? 0.2555 0.5075 0.4381 0.0157  -0.0552 -0.0177 51  ASP   D CB    
3009 C CG    . ASP   D 52  ? 0.2945 0.5547 0.4747 0.0113  -0.0644 -0.0226 51  ASP   D CG    
3010 O OD1   . ASP   D 52  ? 0.3105 0.5657 0.4797 0.0208  -0.0736 -0.0217 51  ASP   D OD1   
3011 O OD2   . ASP   D 52  ? 0.3517 0.6179 0.5365 -0.0026 -0.0624 -0.0268 51  ASP   D OD2   
3012 N N     . ILE   D 53  ? 0.2181 0.4182 0.3696 0.0299  -0.0433 -0.0017 52  ILE   D N     
3013 C CA    . ILE   D 53  ? 0.2183 0.4107 0.3694 0.0332  -0.0371 0.0022  52  ILE   D CA    
3014 C C     . ILE   D 53  ? 0.2152 0.4099 0.3659 0.0459  -0.0436 0.0020  52  ILE   D C     
3015 O O     . ILE   D 53  ? 0.2229 0.4089 0.3603 0.0532  -0.0518 0.0030  52  ILE   D O     
3016 C CB    . ILE   D 53  ? 0.2066 0.3772 0.3410 0.0299  -0.0315 0.0077  52  ILE   D CB    
3017 C CG1   . ILE   D 53  ? 0.1989 0.3685 0.3345 0.0207  -0.0257 0.0067  52  ILE   D CG1   
3018 C CG2   . ILE   D 53  ? 0.2043 0.3669 0.3372 0.0318  -0.0263 0.0114  52  ILE   D CG2   
3019 C CD1   . ILE   D 53  ? 0.1994 0.3541 0.3193 0.0188  -0.0220 0.0098  52  ILE   D CD1   
3020 N N     . THR   D 54  ? 0.2069 0.4117 0.3702 0.0489  -0.0398 0.0004  53  THR   D N     
3021 C CA    . THR   D 54  ? 0.2087 0.4079 0.3671 0.0620  -0.0433 0.0009  53  THR   D CA    
3022 C C     . THR   D 54  ? 0.2014 0.3854 0.3541 0.0589  -0.0346 0.0049  53  THR   D C     
3023 O O     . THR   D 54  ? 0.1749 0.3678 0.3391 0.0506  -0.0268 0.0040  53  THR   D O     
3024 C CB    . THR   D 54  ? 0.2022 0.4312 0.3816 0.0698  -0.0469 -0.0064 53  THR   D CB    
3025 O OG1   . THR   D 54  ? 0.2103 0.4496 0.3903 0.0742  -0.0575 -0.0094 53  THR   D OG1   
3026 C CG2   . THR   D 54  ? 0.2200 0.4445 0.3960 0.0851  -0.0491 -0.0073 53  THR   D CG2   
3027 N N     . SER   D 55  ? 0.2228 0.3825 0.3556 0.0653  -0.0367 0.0090  54  SER   D N     
3028 C CA    . SER   D 55  ? 0.2301 0.3744 0.3551 0.0637  -0.0305 0.0120  54  SER   D CA    
3029 C C     . SER   D 55  ? 0.2829 0.4078 0.3904 0.0774  -0.0371 0.0126  54  SER   D C     
3030 O O     . SER   D 55  ? 0.2922 0.3933 0.3765 0.0792  -0.0424 0.0167  54  SER   D O     
3031 C CB    . SER   D 55  ? 0.2222 0.3503 0.3349 0.0515  -0.0249 0.0176  54  SER   D CB    
3032 O OG    . SER   D 55  ? 0.2212 0.3388 0.3291 0.0480  -0.0192 0.0197  54  SER   D OG    
3033 N N     . THR   D 56  ? 0.2793 0.4117 0.3947 0.0872  -0.0365 0.0084  55  THR   D N     
3034 C CA    . THR   D 56  ? 0.2904 0.4028 0.3881 0.1032  -0.0432 0.0078  55  THR   D CA    
3035 C C     . THR   D 56  ? 0.3052 0.3794 0.3743 0.0973  -0.0405 0.0141  55  THR   D C     
3036 O O     . THR   D 56  ? 0.2890 0.3575 0.3552 0.0813  -0.0338 0.0184  55  THR   D O     
3037 C CB    . THR   D 56  ? 0.2769 0.4117 0.3927 0.1157  -0.0423 0.0002  55  THR   D CB    
3038 O OG1   . THR   D 56  ? 0.2542 0.3916 0.3768 0.1058  -0.0315 0.0003  55  THR   D OG1   
3039 C CG2   . THR   D 56  ? 0.2593 0.4351 0.4035 0.1191  -0.0450 -0.0066 55  THR   D CG2   
3040 N N     . ALA   D 57  ? 0.3359 0.3824 0.3814 0.1107  -0.0470 0.0143  56  ALA   D N     
3041 C CA    . ALA   D 57  ? 0.3486 0.3545 0.3620 0.1041  -0.0458 0.0201  56  ALA   D CA    
3042 C C     . ALA   D 57  ? 0.3177 0.3272 0.3388 0.0912  -0.0352 0.0205  56  ALA   D C     
3043 O O     . ALA   D 57  ? 0.3032 0.3355 0.3456 0.0952  -0.0308 0.0153  56  ALA   D O     
3044 C CB    . ALA   D 57  ? 0.3778 0.3508 0.3629 0.1221  -0.0547 0.0194  56  ALA   D CB    
3045 N N     . GLY   D 58  ? 0.3162 0.3070 0.3213 0.0746  -0.0311 0.0263  57  GLY   D N     
3046 C CA    . GLY   D 58  ? 0.3120 0.3075 0.3235 0.0605  -0.0225 0.0272  57  GLY   D CA    
3047 C C     . GLY   D 58  ? 0.2977 0.3308 0.3421 0.0542  -0.0163 0.0249  57  GLY   D C     
3048 O O     . GLY   D 58  ? 0.2994 0.3378 0.3504 0.0476  -0.0105 0.0243  57  GLY   D O     
3049 N N     . ASN   D 59  ? 0.2768 0.3327 0.3386 0.0564  -0.0180 0.0235  58  ASN   D N     
3050 C CA    . ASN   D 59  ? 0.2469 0.3336 0.3360 0.0517  -0.0130 0.0208  58  ASN   D CA    
3051 C C     . ASN   D 59  ? 0.2357 0.3376 0.3400 0.0569  -0.0094 0.0159  58  ASN   D C     
3052 O O     . ASN   D 59  ? 0.2430 0.3590 0.3605 0.0490  -0.0032 0.0153  58  ASN   D O     
3053 C CB    . ASN   D 59  ? 0.2258 0.3159 0.3178 0.0368  -0.0070 0.0241  58  ASN   D CB    
3054 C CG    . ASN   D 59  ? 0.2336 0.3107 0.3101 0.0296  -0.0083 0.0285  58  ASN   D CG    
3055 O OD1   . ASN   D 59  ? 0.2302 0.2953 0.2949 0.0205  -0.0054 0.0314  58  ASN   D OD1   
3056 N ND2   . ASN   D 59  ? 0.2246 0.3045 0.3000 0.0325  -0.0123 0.0285  58  ASN   D ND2   
3057 N N     . GLN   D 60  ? 0.2454 0.3438 0.3460 0.0708  -0.0129 0.0121  59  GLN   D N     
3058 C CA    . GLN   D 60  ? 0.2587 0.3722 0.3722 0.0760  -0.0082 0.0066  59  GLN   D CA    
3059 C C     . GLN   D 60  ? 0.2332 0.3822 0.3741 0.0731  -0.0051 0.0024  59  GLN   D C     
3060 O O     . GLN   D 60  ? 0.2111 0.3716 0.3620 0.0650  0.0023  0.0013  59  GLN   D O     
3061 C CB    . GLN   D 60  ? 0.2890 0.3905 0.3910 0.0940  -0.0130 0.0025  59  GLN   D CB    
3062 C CG    . GLN   D 60  ? 0.3233 0.4425 0.4382 0.1010  -0.0072 -0.0044 59  GLN   D CG    
3063 C CD    . GLN   D 60  ? 0.3494 0.5055 0.4893 0.1114  -0.0084 -0.0120 59  GLN   D CD    
3064 O OE1   . GLN   D 60  ? 0.4257 0.5865 0.5667 0.1226  -0.0172 -0.0136 59  GLN   D OE1   
3065 N NE2   . GLN   D 60  ? 0.3148 0.4985 0.4743 0.1066  0.0002  -0.0168 59  GLN   D NE2   
3066 N N     . ASP   D 61  ? 0.2299 0.3935 0.3797 0.0783  -0.0112 0.0003  60  ASP   D N     
3067 C CA    . ASP   D 61  ? 0.2180 0.4135 0.3912 0.0733  -0.0094 -0.0038 60  ASP   D CA    
3068 C C     . ASP   D 61  ? 0.1843 0.3781 0.3565 0.0645  -0.0126 -0.0002 60  ASP   D C     
3069 O O     . ASP   D 61  ? 0.1867 0.3681 0.3470 0.0704  -0.0201 0.0019  60  ASP   D O     
3070 C CB    . ASP   D 61  ? 0.2532 0.4745 0.4414 0.0868  -0.0135 -0.0117 60  ASP   D CB    
3071 C CG    . ASP   D 61  ? 0.2869 0.5448 0.5005 0.0795  -0.0073 -0.0179 60  ASP   D CG    
3072 O OD1   . ASP   D 61  ? 0.3013 0.5600 0.5182 0.0633  0.0003  -0.0155 60  ASP   D OD1   
3073 O OD2   . ASP   D 61  ? 0.4285 0.7145 0.6579 0.0902  -0.0104 -0.0256 60  ASP   D OD2   
3074 N N     . ASN   D 62  ? 0.1568 0.3608 0.3388 0.0512  -0.0071 0.0002  61  ASN   D N     
3075 C CA    . ASN   D 62  ? 0.1513 0.3498 0.3297 0.0423  -0.0084 0.0035  61  ASN   D CA    
3076 C C     . ASN   D 62  ? 0.1464 0.3670 0.3407 0.0345  -0.0073 -0.0008 61  ASN   D C     
3077 O O     . ASN   D 62  ? 0.1325 0.3656 0.3370 0.0285  -0.0011 -0.0034 61  ASN   D O     
3078 C CB    . ASN   D 62  ? 0.1488 0.3300 0.3171 0.0337  -0.0031 0.0088  61  ASN   D CB    
3079 C CG    . ASN   D 62  ? 0.1576 0.3191 0.3109 0.0377  -0.0031 0.0123  61  ASN   D CG    
3080 O OD1   . ASN   D 62  ? 0.1710 0.3176 0.3104 0.0393  -0.0070 0.0154  61  ASN   D OD1   
3081 N ND2   . ASN   D 62  ? 0.1586 0.3184 0.3121 0.0383  0.0013  0.0115  61  ASN   D ND2   
3082 N N     . SER   D 63  ? 0.1397 0.3626 0.3331 0.0332  -0.0130 -0.0013 62  SER   D N     
3083 C CA    . SER   D 63  ? 0.1350 0.3744 0.3393 0.0243  -0.0133 -0.0053 62  SER   D CA    
3084 C C     . SER   D 63  ? 0.1445 0.3692 0.3372 0.0192  -0.0158 -0.0026 62  SER   D C     
3085 O O     . SER   D 63  ? 0.1615 0.3754 0.3431 0.0259  -0.0213 -0.0003 62  SER   D O     
3086 C CB    . SER   D 63  ? 0.1384 0.4042 0.3571 0.0303  -0.0195 -0.0118 62  SER   D CB    
3087 O OG    . SER   D 63  ? 0.1280 0.4088 0.3553 0.0190  -0.0205 -0.0158 62  SER   D OG    
3088 N N     . PHE   D 64  ? 0.1394 0.3617 0.3321 0.0078  -0.0117 -0.0032 63  PHE   D N     
3089 C CA    . PHE   D 64  ? 0.1585 0.3669 0.3399 0.0034  -0.0132 -0.0020 63  PHE   D CA    
3090 C C     . PHE   D 64  ? 0.1771 0.3939 0.3634 -0.0076 -0.0136 -0.0067 63  PHE   D C     
3091 O O     . PHE   D 64  ? 0.1817 0.3966 0.3695 -0.0162 -0.0077 -0.0071 63  PHE   D O     
3092 C CB    . PHE   D 64  ? 0.1569 0.3461 0.3277 0.0021  -0.0074 0.0026  63  PHE   D CB    
3093 C CG    . PHE   D 64  ? 0.1686 0.3445 0.3274 0.0002  -0.0082 0.0029  63  PHE   D CG    
3094 C CD1   . PHE   D 64  ? 0.1843 0.3541 0.3393 -0.0073 -0.0073 0.0003  63  PHE   D CD1   
3095 C CD2   . PHE   D 64  ? 0.1772 0.3448 0.3260 0.0057  -0.0094 0.0056  63  PHE   D CD2   
3096 C CE1   . PHE   D 64  ? 0.1991 0.3548 0.3411 -0.0068 -0.0080 -0.0003 63  PHE   D CE1   
3097 C CE2   . PHE   D 64  ? 0.1851 0.3427 0.3231 0.0050  -0.0089 0.0050  63  PHE   D CE2   
3098 C CZ    . PHE   D 64  ? 0.1999 0.3517 0.3348 0.0000  -0.0084 0.0018  63  PHE   D CZ    
3099 N N     . ALA   D 65  ? 0.1828 0.4061 0.3687 -0.0083 -0.0207 -0.0102 64  ALA   D N     
3100 C CA    . ALA   D 65  ? 0.2104 0.4408 0.3988 -0.0204 -0.0223 -0.0153 64  ALA   D CA    
3101 C C     . ALA   D 65  ? 0.2348 0.4456 0.4061 -0.0223 -0.0254 -0.0152 64  ALA   D C     
3102 O O     . ALA   D 65  ? 0.2713 0.4783 0.4359 -0.0137 -0.0304 -0.0138 64  ALA   D O     
3103 C CB    . ALA   D 65  ? 0.2155 0.4763 0.4205 -0.0203 -0.0289 -0.0212 64  ALA   D CB    
3104 N N     . ILE   D 66  ? 0.2438 0.4395 0.4054 -0.0329 -0.0222 -0.0165 65  ILE   D N     
3105 C CA    . ILE   D 66  ? 0.2628 0.4374 0.4060 -0.0340 -0.0245 -0.0175 65  ILE   D CA    
3106 C C     . ILE   D 66  ? 0.2532 0.4262 0.3922 -0.0491 -0.0267 -0.0231 65  ILE   D C     
3107 O O     . ILE   D 66  ? 0.2495 0.4201 0.3897 -0.0594 -0.0219 -0.0236 65  ILE   D O     
3108 C CB    . ILE   D 66  ? 0.2734 0.4239 0.4027 -0.0281 -0.0186 -0.0134 65  ILE   D CB    
3109 C CG1   . ILE   D 66  ? 0.3178 0.4487 0.4282 -0.0269 -0.0205 -0.0156 65  ILE   D CG1   
3110 C CG2   . ILE   D 66  ? 0.2957 0.4359 0.4234 -0.0337 -0.0124 -0.0118 65  ILE   D CG2   
3111 C CD1   . ILE   D 66  ? 0.3302 0.4475 0.4313 -0.0164 -0.0158 -0.0124 65  ILE   D CD1   
3112 N N     . GLN   D 67  ? 0.2631 0.4370 0.3958 -0.0515 -0.0340 -0.0272 66  GLN   D N     
3113 C CA    . GLN   D 67  ? 0.2968 0.4657 0.4214 -0.0671 -0.0372 -0.0331 66  GLN   D CA    
3114 C C     . GLN   D 67  ? 0.2974 0.4350 0.3964 -0.0647 -0.0384 -0.0340 66  GLN   D C     
3115 O O     . GLN   D 67  ? 0.2694 0.4064 0.3635 -0.0541 -0.0420 -0.0332 66  GLN   D O     
3116 C CB    . GLN   D 67  ? 0.3332 0.5333 0.4729 -0.0719 -0.0461 -0.0385 66  GLN   D CB    
3117 C CG    . GLN   D 67  ? 0.3884 0.6232 0.5543 -0.0763 -0.0446 -0.0403 66  GLN   D CG    
3118 C CD    . GLN   D 67  ? 0.4576 0.7128 0.6408 -0.0598 -0.0445 -0.0369 66  GLN   D CD    
3119 O OE1   . GLN   D 67  ? 0.4852 0.7312 0.6623 -0.0444 -0.0468 -0.0325 66  GLN   D OE1   
3120 N NE2   . GLN   D 67  ? 0.4398 0.7230 0.6438 -0.0640 -0.0413 -0.0393 66  GLN   D NE2   
3121 N N     . LEU   D 68  ? 0.3139 0.4238 0.3948 -0.0734 -0.0348 -0.0353 67  LEU   D N     
3122 C CA    . LEU   D 68  ? 0.3467 0.4247 0.4009 -0.0718 -0.0360 -0.0380 67  LEU   D CA    
3123 C C     . LEU   D 68  ? 0.3857 0.4552 0.4279 -0.0906 -0.0412 -0.0447 67  LEU   D C     
3124 O O     . LEU   D 68  ? 0.3711 0.4471 0.4193 -0.1065 -0.0398 -0.0460 67  LEU   D O     
3125 C CB    . LEU   D 68  ? 0.3469 0.3956 0.3857 -0.0639 -0.0291 -0.0348 67  LEU   D CB    
3126 C CG    . LEU   D 68  ? 0.3298 0.3891 0.3814 -0.0483 -0.0240 -0.0286 67  LEU   D CG    
3127 C CD1   . LEU   D 68  ? 0.3513 0.3862 0.3905 -0.0418 -0.0185 -0.0261 67  LEU   D CD1   
3128 C CD2   . LEU   D 68  ? 0.3285 0.3960 0.3807 -0.0358 -0.0254 -0.0281 67  LEU   D CD2   
3129 N N     . ALA   D 69  ? 0.3995 0.4568 0.4248 -0.0901 -0.0470 -0.0492 68  ALA   D N     
3130 C CA    . ALA   D 69  ? 0.4403 0.4787 0.4459 -0.1074 -0.0517 -0.0559 68  ALA   D CA    
3131 C C     . ALA   D 69  ? 0.4867 0.4836 0.4596 -0.0992 -0.0506 -0.0581 68  ALA   D C     
3132 O O     . ALA   D 69  ? 0.4653 0.4638 0.4343 -0.0857 -0.0522 -0.0583 68  ALA   D O     
3133 C CB    . ALA   D 69  ? 0.4376 0.5049 0.4546 -0.1161 -0.0616 -0.0610 68  ALA   D CB    
3134 N N     . ASN   D 70  ? 0.5536 0.5130 0.5019 -0.1073 -0.0478 -0.0598 69  ASN   D N     
3135 C CA    . ASN   D 70  ? 0.6238 0.5395 0.5392 -0.0972 -0.0459 -0.0622 69  ASN   D CA    
3136 C C     . ASN   D 70  ? 0.6711 0.5596 0.5576 -0.1110 -0.0524 -0.0703 69  ASN   D C     
3137 O O     . ASN   D 70  ? 0.6973 0.5864 0.5819 -0.1338 -0.0561 -0.0733 69  ASN   D O     
3138 C CB    . ASN   D 70  ? 0.6799 0.5669 0.5829 -0.0961 -0.0400 -0.0588 69  ASN   D CB    
3139 C CG    . ASN   D 70  ? 0.7560 0.6050 0.6318 -0.0773 -0.0373 -0.0600 69  ASN   D CG    
3140 O OD1   . ASN   D 70  ? 0.8211 0.6634 0.6854 -0.0658 -0.0386 -0.0642 69  ASN   D OD1   
3141 N ND2   . ASN   D 70  ? 0.8195 0.6449 0.6849 -0.0727 -0.0334 -0.0565 69  ASN   D ND2   
3142 N N     . TYR   D 71  ? 0.7041 0.5680 0.5667 -0.0979 -0.0531 -0.0744 70  TYR   D N     
3143 C CA    . TYR   D 71  ? 0.7577 0.5926 0.5890 -0.1073 -0.0593 -0.0827 70  TYR   D CA    
3144 C C     . TYR   D 71  ? 0.7646 0.5806 0.5756 -0.0852 -0.0569 -0.0860 70  TYR   D C     
3145 O O     . TYR   D 71  ? 0.7101 0.4944 0.5009 -0.0697 -0.0515 -0.0868 70  TYR   D O     
3146 C CB    . TYR   D 71  ? 0.7768 0.6353 0.6157 -0.1263 -0.0687 -0.0873 70  TYR   D CB    
3147 C CG    . TYR   D 71  ? 0.7413 0.6551 0.6198 -0.1265 -0.0721 -0.0835 70  TYR   D CG    
3148 C CD1   . TYR   D 71  ? 0.7264 0.6632 0.6217 -0.1060 -0.0696 -0.0788 70  TYR   D CD1   
3149 C CD2   . TYR   D 71  ? 0.7478 0.6912 0.6465 -0.1473 -0.0774 -0.0850 70  TYR   D CD2   
3150 C CE1   . TYR   D 71  ? 0.7255 0.7069 0.6527 -0.1049 -0.0733 -0.0752 70  TYR   D CE1   
3151 C CE2   . TYR   D 71  ? 0.7290 0.7223 0.6633 -0.1446 -0.0809 -0.0822 70  TYR   D CE2   
3152 C CZ    . TYR   D 71  ? 0.7375 0.7472 0.6844 -0.1226 -0.0795 -0.0771 70  TYR   D CZ    
3153 O OH    . TYR   D 71  ? 0.7113 0.7645 0.6887 -0.1189 -0.0840 -0.0746 70  TYR   D OH    
3154 N N     . THR   D 78  ? 0.8083 0.6653 0.6919 -0.1792 -0.0345 -0.0575 77  THR   D N     
3155 C CA    . THR   D 78  ? 0.8103 0.7020 0.7143 -0.1727 -0.0406 -0.0616 77  THR   D CA    
3156 C C     . THR   D 78  ? 0.7192 0.6641 0.6659 -0.1589 -0.0387 -0.0571 77  THR   D C     
3157 O O     . THR   D 78  ? 0.6465 0.5972 0.5998 -0.1359 -0.0388 -0.0548 77  THR   D O     
3158 C CB    . THR   D 78  ? 0.9115 0.8101 0.8104 -0.1985 -0.0472 -0.0694 77  THR   D CB    
3159 O OG1   . THR   D 78  ? 0.9384 0.8779 0.8622 -0.1905 -0.0535 -0.0722 77  THR   D OG1   
3160 C CG2   . THR   D 78  ? 0.9513 0.8640 0.8565 -0.2290 -0.0450 -0.0711 77  THR   D CG2   
3161 N N     . LYS   D 79  ? 0.6330 0.6159 0.6066 -0.1732 -0.0368 -0.0567 78  LYS   D N     
3162 C CA    . LYS   D 79  ? 0.5876 0.6189 0.5993 -0.1610 -0.0357 -0.0534 78  LYS   D CA    
3163 C C     . LYS   D 79  ? 0.5505 0.5773 0.5675 -0.1518 -0.0271 -0.0462 78  LYS   D C     
3164 O O     . LYS   D 79  ? 0.5774 0.5807 0.5786 -0.1641 -0.0221 -0.0445 78  LYS   D O     
3165 C CB    . LYS   D 79  ? 0.6041 0.6850 0.6456 -0.1761 -0.0386 -0.0577 78  LYS   D CB    
3166 C CG    . LYS   D 79  ? 0.6533 0.7522 0.6988 -0.1797 -0.0491 -0.0644 78  LYS   D CG    
3167 C CD    . LYS   D 79  ? 0.6871 0.8363 0.7610 -0.1963 -0.0531 -0.0703 78  LYS   D CD    
3168 C CE    . LYS   D 79  ? 0.6604 0.8583 0.7714 -0.1806 -0.0538 -0.0684 78  LYS   D CE    
3169 N NZ    . LYS   D 79  ? 0.6387 0.8872 0.7768 -0.1940 -0.0594 -0.0759 78  LYS   D NZ    
3170 N N     . TRP   D 80  ? 0.5103 0.5613 0.5493 -0.1319 -0.0261 -0.0419 79  TRP   D N     
3171 C CA    . TRP   D 80  ? 0.5033 0.5537 0.5493 -0.1205 -0.0193 -0.0353 79  TRP   D CA    
3172 C C     . TRP   D 80  ? 0.4542 0.5467 0.5321 -0.1087 -0.0197 -0.0334 79  TRP   D C     
3173 O O     . TRP   D 80  ? 0.4660 0.5672 0.5484 -0.0966 -0.0245 -0.0340 79  TRP   D O     
3174 C CB    . TRP   D 80  ? 0.5282 0.5430 0.5524 -0.1030 -0.0182 -0.0321 79  TRP   D CB    
3175 C CG    . TRP   D 80  ? 0.5371 0.5397 0.5586 -0.0960 -0.0122 -0.0261 79  TRP   D CG    
3176 C CD1   . TRP   D 80  ? 0.5637 0.5311 0.5606 -0.1037 -0.0095 -0.0247 79  TRP   D CD1   
3177 C CD2   . TRP   D 80  ? 0.5332 0.5545 0.5731 -0.0800 -0.0090 -0.0209 79  TRP   D CD2   
3178 N NE1   . TRP   D 80  ? 0.5696 0.5344 0.5695 -0.0930 -0.0054 -0.0189 79  TRP   D NE1   
3179 C CE2   . TRP   D 80  ? 0.5456 0.5434 0.5720 -0.0787 -0.0049 -0.0167 79  TRP   D CE2   
3180 C CE3   . TRP   D 80  ? 0.5424 0.5939 0.6052 -0.0670 -0.0097 -0.0192 79  TRP   D CE3   
3181 C CZ2   . TRP   D 80  ? 0.5221 0.5295 0.5597 -0.0656 -0.0018 -0.0115 79  TRP   D CZ2   
3182 C CZ3   . TRP   D 80  ? 0.4881 0.5462 0.5601 -0.0548 -0.0060 -0.0140 79  TRP   D CZ3   
3183 C CH2   . TRP   D 80  ? 0.4862 0.5242 0.5470 -0.0543 -0.0022 -0.0105 79  TRP   D CH2   
3184 N N     . CSD   D 81  ? 0.4553 0.5716 0.5524 -0.1125 -0.0149 -0.0315 80  CSD   D N     
3185 C CA    . CSD   D 81  ? 0.4189 0.5665 0.5410 -0.0978 -0.0149 -0.0290 80  CSD   D CA    
3186 C CB    . CSD   D 81  ? 0.4490 0.6371 0.5945 -0.1020 -0.0202 -0.0342 80  CSD   D CB    
3187 S SG    . CSD   D 81  ? 0.5416 0.7582 0.7036 -0.1225 -0.0149 -0.0386 80  CSD   D SG    
3188 C C     . CSD   D 81  ? 0.3555 0.5044 0.4839 -0.0935 -0.0073 -0.0239 80  CSD   D C     
3189 O O     . CSD   D 81  ? 0.3368 0.4686 0.4535 -0.1046 -0.0019 -0.0227 80  CSD   D O     
3190 O OD1   . CSD   D 81  ? 0.5010 0.7351 0.6797 -0.1124 -0.0086 -0.0349 80  CSD   D OD1   
3191 O OD2   . CSD   D 81  ? 0.5889 0.8421 0.7678 -0.1327 -0.0229 -0.0471 80  CSD   D OD2   
3192 N N     . ALA   D 82  ? 0.2953 0.4614 0.4390 -0.0775 -0.0076 -0.0209 81  ALA   D N     
3193 C CA    . ALA   D 82  ? 0.2706 0.4400 0.4211 -0.0709 -0.0016 -0.0163 81  ALA   D CA    
3194 C C     . ALA   D 82  ? 0.2293 0.4305 0.4022 -0.0609 -0.0035 -0.0169 81  ALA   D C     
3195 O O     . ALA   D 82  ? 0.2512 0.4582 0.4267 -0.0514 -0.0098 -0.0174 81  ALA   D O     
3196 C CB    . ALA   D 82  ? 0.2841 0.4264 0.4196 -0.0593 0.0000  -0.0109 81  ALA   D CB    
3197 N N     . LEU   D 83  ? 0.1842 0.4044 0.3708 -0.0633 0.0015  -0.0174 82  LEU   D N     
3198 C CA    . LEU   D 83  ? 0.1586 0.4024 0.3624 -0.0510 0.0008  -0.0176 82  LEU   D CA    
3199 C C     . LEU   D 83  ? 0.1458 0.3775 0.3453 -0.0458 0.0075  -0.0124 82  LEU   D C     
3200 O O     . LEU   D 83  ? 0.1415 0.3710 0.3387 -0.0558 0.0143  -0.0124 82  LEU   D O     
3201 C CB    . LEU   D 83  ? 0.1651 0.4449 0.3891 -0.0585 0.0013  -0.0244 82  LEU   D CB    
3202 C CG    . LEU   D 83  ? 0.1514 0.4585 0.3939 -0.0447 0.0005  -0.0265 82  LEU   D CG    
3203 C CD1   . LEU   D 83  ? 0.1577 0.4614 0.3986 -0.0270 -0.0088 -0.0247 82  LEU   D CD1   
3204 C CD2   . LEU   D 83  ? 0.1601 0.5067 0.4236 -0.0525 0.0002  -0.0350 82  LEU   D CD2   
3205 N N     . LEU   D 84  ? 0.1492 0.3722 0.3455 -0.0316 0.0053  -0.0083 83  LEU   D N     
3206 C CA    . LEU   D 84  ? 0.1516 0.3645 0.3440 -0.0257 0.0100  -0.0037 83  LEU   D CA    
3207 C C     . LEU   D 84  ? 0.1396 0.3683 0.3428 -0.0144 0.0086  -0.0045 83  LEU   D C     
3208 O O     . LEU   D 84  ? 0.1443 0.3756 0.3483 -0.0057 0.0023  -0.0047 83  LEU   D O     
3209 C CB    . LEU   D 84  ? 0.1685 0.3579 0.3466 -0.0204 0.0085  0.0011  83  LEU   D CB    
3210 C CG    . LEU   D 84  ? 0.1880 0.3589 0.3527 -0.0263 0.0078  0.0012  83  LEU   D CG    
3211 C CD1   . LEU   D 84  ? 0.1886 0.3439 0.3434 -0.0175 0.0070  0.0050  83  LEU   D CD1   
3212 C CD2   . LEU   D 84  ? 0.2177 0.3779 0.3747 -0.0378 0.0123  0.0009  83  LEU   D CD2   
3213 N N     . THR   D 85  ? 0.1275 0.3639 0.3359 -0.0140 0.0142  -0.0052 84  THR   D N     
3214 C CA    . THR   D 85  ? 0.1211 0.3690 0.3369 -0.0018 0.0130  -0.0067 84  THR   D CA    
3215 C C     . THR   D 85  ? 0.1224 0.3558 0.3297 0.0010  0.0181  -0.0030 84  THR   D C     
3216 O O     . THR   D 85  ? 0.1201 0.3473 0.3228 -0.0080 0.0241  -0.0018 84  THR   D O     
3217 C CB    . THR   D 85  ? 0.1134 0.3930 0.3473 -0.0012 0.0138  -0.0141 84  THR   D CB    
3218 O OG1   . THR   D 85  ? 0.1057 0.3911 0.3417 -0.0133 0.0230  -0.0157 84  THR   D OG1   
3219 C CG2   . THR   D 85  ? 0.1163 0.4134 0.3596 -0.0040 0.0071  -0.0185 84  THR   D CG2   
3220 N N     . LYS   D 86  ? 0.1298 0.3563 0.3328 0.0127  0.0152  -0.0014 85  LYS   D N     
3221 C CA    . LYS   D 86  ? 0.1374 0.3486 0.3304 0.0147  0.0190  0.0018  85  LYS   D CA    
3222 C C     . LYS   D 86  ? 0.1422 0.3537 0.3339 0.0276  0.0164  -0.0001 85  LYS   D C     
3223 O O     . LYS   D 86  ? 0.1351 0.3387 0.3211 0.0353  0.0097  0.0012  85  LYS   D O     
3224 C CB    . LYS   D 86  ? 0.1265 0.3164 0.3064 0.0117  0.0177  0.0079  85  LYS   D CB    
3225 C CG    . LYS   D 86  ? 0.1249 0.3008 0.2947 0.0116  0.0207  0.0110  85  LYS   D CG    
3226 C CD    . LYS   D 86  ? 0.1197 0.2814 0.2800 0.0085  0.0191  0.0159  85  LYS   D CD    
3227 C CE    . LYS   D 86  ? 0.1142 0.2734 0.2735 0.0021  0.0201  0.0172  85  LYS   D CE    
3228 N NZ    . LYS   D 86  ? 0.1199 0.2776 0.2773 -0.0035 0.0246  0.0168  85  LYS   D NZ    
3229 N N     . LYS   D 87  ? 0.1558 0.3728 0.3494 0.0297  0.0219  -0.0032 86  LYS   D N     
3230 C CA    . LYS   D 87  ? 0.1825 0.4020 0.3756 0.0434  0.0204  -0.0071 86  LYS   D CA    
3231 C C     . LYS   D 87  ? 0.1729 0.3713 0.3506 0.0437  0.0242  -0.0046 86  LYS   D C     
3232 O O     . LYS   D 87  ? 0.1630 0.3628 0.3403 0.0356  0.0311  -0.0046 86  LYS   D O     
3233 C CB    . LYS   D 87  ? 0.2073 0.4590 0.4192 0.0472  0.0235  -0.0154 86  LYS   D CB    
3234 C CG    . LYS   D 87  ? 0.2665 0.5241 0.4795 0.0657  0.0204  -0.0209 86  LYS   D CG    
3235 C CD    . LYS   D 87  ? 0.3013 0.5978 0.5361 0.0705  0.0243  -0.0307 86  LYS   D CD    
3236 C CE    . LYS   D 87  ? 0.3441 0.6492 0.5810 0.0633  0.0362  -0.0338 86  LYS   D CE    
3237 N NZ    . LYS   D 87  ? 0.3907 0.7339 0.6472 0.0720  0.0403  -0.0445 86  LYS   D NZ    
3238 N N     . TYR   D 88  ? 0.1733 0.3504 0.3360 0.0523  0.0191  -0.0025 87  TYR   D N     
3239 C CA    . TYR   D 88  ? 0.1805 0.3347 0.3258 0.0522  0.0211  -0.0004 87  TYR   D CA    
3240 C C     . TYR   D 88  ? 0.2023 0.3555 0.3435 0.0669  0.0213  -0.0064 87  TYR   D C     
3241 O O     . TYR   D 88  ? 0.1996 0.3674 0.3502 0.0787  0.0175  -0.0110 87  TYR   D O     
3242 C CB    . TYR   D 88  ? 0.1884 0.3184 0.3176 0.0487  0.0156  0.0060  87  TYR   D CB    
3243 C CG    . TYR   D 88  ? 0.1773 0.3084 0.3092 0.0356  0.0166  0.0110  87  TYR   D CG    
3244 C CD1   . TYR   D 88  ? 0.1778 0.3027 0.3045 0.0270  0.0203  0.0133  87  TYR   D CD1   
3245 C CD2   . TYR   D 88  ? 0.1628 0.3000 0.3005 0.0332  0.0131  0.0130  87  TYR   D CD2   
3246 C CE1   . TYR   D 88  ? 0.1757 0.3018 0.3041 0.0182  0.0200  0.0172  87  TYR   D CE1   
3247 C CE2   . TYR   D 88  ? 0.1572 0.2945 0.2959 0.0239  0.0138  0.0166  87  TYR   D CE2   
3248 C CZ    . TYR   D 88  ? 0.1647 0.2973 0.2995 0.0171  0.0171  0.0186  87  TYR   D CZ    
3249 O OH    . TYR   D 88  ? 0.1561 0.2898 0.2918 0.0105  0.0171  0.0215  87  TYR   D OH    
3250 N N     . PRO   D 89  ? 0.2275 0.3630 0.3536 0.0680  0.0246  -0.0070 88  PRO   D N     
3251 C CA    . PRO   D 89  ? 0.2608 0.3905 0.3791 0.0842  0.0243  -0.0133 88  PRO   D CA    
3252 C C     . PRO   D 89  ? 0.2902 0.3946 0.3909 0.0960  0.0147  -0.0118 88  PRO   D C     
3253 O O     . PRO   D 89  ? 0.2729 0.3572 0.3611 0.0881  0.0100  -0.0050 88  PRO   D O     
3254 C CB    . PRO   D 89  ? 0.2765 0.3907 0.3804 0.0792  0.0305  -0.0137 88  PRO   D CB    
3255 C CG    . PRO   D 89  ? 0.2579 0.3623 0.3571 0.0613  0.0308  -0.0060 88  PRO   D CG    
3256 C CD    . PRO   D 89  ? 0.2235 0.3433 0.3380 0.0550  0.0279  -0.0024 88  PRO   D CD    
3257 N N     . GLU   D 90  ? 0.3480 0.4527 0.4457 0.1152  0.0123  -0.0186 89  GLU   D N     
3258 C CA    . GLU   D 90  ? 0.4067 0.4814 0.4816 0.1303  0.0030  -0.0184 89  GLU   D CA    
3259 C C     . GLU   D 90  ? 0.3980 0.4288 0.4404 0.1234  0.0028  -0.0139 89  GLU   D C     
3260 O O     . GLU   D 90  ? 0.3934 0.4206 0.4314 0.1192  0.0096  -0.0162 89  GLU   D O     
3261 C CB    . GLU   D 90  ? 0.5005 0.5859 0.5787 0.1545  0.0017  -0.0283 89  GLU   D CB    
3262 C CG    . GLU   D 90  ? 0.5713 0.7061 0.6834 0.1632  0.0023  -0.0354 89  GLU   D CG    
3263 C CD    . GLU   D 90  ? 0.6281 0.7693 0.7444 0.1760  -0.0094 -0.0357 89  GLU   D CD    
3264 O OE1   . GLU   D 90  ? 0.7307 0.8558 0.8387 0.1648  -0.0145 -0.0275 89  GLU   D OE1   
3265 O OE2   . GLU   D 90  ? 0.6273 0.7916 0.7558 0.1967  -0.0133 -0.0444 89  GLU   D OE2   
3266 N N     . ARG   D 91  ? 0.4064 0.4048 0.4256 0.1196  -0.0045 -0.0076 90  ARG   D N     
3267 C CA    . ARG   D 91  ? 0.4301 0.3892 0.4191 0.1080  -0.0045 -0.0030 90  ARG   D CA    
3268 C C     . ARG   D 91  ? 0.4729 0.3961 0.4320 0.1235  -0.0073 -0.0077 90  ARG   D C     
3269 O O     . ARG   D 91  ? 0.4579 0.3870 0.4198 0.1458  -0.0098 -0.0147 90  ARG   D O     
3270 C CB    . ARG   D 91  ? 0.4330 0.3741 0.4088 0.0950  -0.0096 0.0052  90  ARG   D CB    
3271 C CG    . ARG   D 91  ? 0.4573 0.3704 0.4101 0.1072  -0.0192 0.0068  90  ARG   D CG    
3272 C CD    . ARG   D 91  ? 0.4758 0.3600 0.4045 0.0900  -0.0218 0.0148  90  ARG   D CD    
3273 N NE    . ARG   D 91  ? 0.4927 0.3447 0.3949 0.0774  -0.0195 0.0164  90  ARG   D NE    
3274 C CZ    . ARG   D 91  ? 0.5153 0.3611 0.4102 0.0541  -0.0166 0.0218  90  ARG   D CZ    
3275 N NH1   . ARG   D 91  ? 0.4930 0.3596 0.4028 0.0414  -0.0153 0.0264  90  ARG   D NH1   
3276 N NH2   . ARG   D 91  ? 0.5456 0.3642 0.4170 0.0428  -0.0152 0.0221  90  ARG   D NH2   
3277 N N     . LYS   D 92  ? 0.5086 0.3950 0.4385 0.1112  -0.0071 -0.0044 91  LYS   D N     
3278 C CA    . LYS   D 92  ? 0.5745 0.4135 0.4658 0.1214  -0.0112 -0.0071 91  LYS   D CA    
3279 C C     . LYS   D 92  ? 0.5927 0.3903 0.4512 0.1031  -0.0157 0.0008  91  LYS   D C     
3280 O O     . LYS   D 92  ? 0.5847 0.3983 0.4558 0.0831  -0.0139 0.0071  91  LYS   D O     
3281 C CB    . LYS   D 92  ? 0.5800 0.4171 0.4673 0.1232  -0.0043 -0.0134 91  LYS   D CB    
3282 C CG    . LYS   D 92  ? 0.5623 0.4443 0.4829 0.1358  0.0026  -0.0210 91  LYS   D CG    
3283 C CD    . LYS   D 92  ? 0.5962 0.4682 0.5044 0.1450  0.0084  -0.0291 91  LYS   D CD    
3284 C CE    . LYS   D 92  ? 0.5720 0.4918 0.5136 0.1556  0.0164  -0.0367 91  LYS   D CE    
3285 N NZ    . LYS   D 92  ? 0.5979 0.5106 0.5278 0.1615  0.0238  -0.0444 91  LYS   D NZ    
3286 N N     . PRO   D 93  ? 0.6317 0.3758 0.4469 0.1091  -0.0216 0.0005  92  PRO   D N     
3287 C CA    . PRO   D 93  ? 0.6579 0.3605 0.4384 0.0894  -0.0256 0.0080  92  PRO   D CA    
3288 C C     . PRO   D 93  ? 0.6304 0.3402 0.4141 0.0593  -0.0201 0.0123  92  PRO   D C     
3289 O O     . PRO   D 93  ? 0.6170 0.3249 0.3967 0.0402  -0.0209 0.0190  92  PRO   D O     
3290 C CB    . PRO   D 93  ? 0.7183 0.3608 0.4503 0.1019  -0.0314 0.0050  92  PRO   D CB    
3291 C CG    . PRO   D 93  ? 0.7233 0.3820 0.4699 0.1356  -0.0343 -0.0026 92  PRO   D CG    
3292 C CD    . PRO   D 93  ? 0.6711 0.3892 0.4653 0.1360  -0.0253 -0.0072 92  PRO   D CD    
3293 N N     . ASP   D 94  ? 0.5904 0.3109 0.3819 0.0558  -0.0147 0.0080  93  ASP   D N     
3294 C CA    . ASP   D 94  ? 0.5780 0.3059 0.3716 0.0297  -0.0110 0.0109  93  ASP   D CA    
3295 C C     . ASP   D 94  ? 0.5110 0.2959 0.3506 0.0236  -0.0054 0.0120  93  ASP   D C     
3296 O O     . ASP   D 94  ? 0.4830 0.2928 0.3429 0.0309  -0.0008 0.0077  93  ASP   D O     
3297 C CB    . ASP   D 94  ? 0.6145 0.3133 0.3821 0.0270  -0.0100 0.0062  93  ASP   D CB    
3298 C CG    . ASP   D 94  ? 0.6130 0.3103 0.3737 -0.0017 -0.0089 0.0093  93  ASP   D CG    
3299 O OD1   . ASP   D 94  ? 0.5867 0.3034 0.3605 -0.0196 -0.0089 0.0150  93  ASP   D OD1   
3300 O OD2   . ASP   D 94  ? 0.6515 0.3301 0.3941 -0.0057 -0.0081 0.0054  93  ASP   D OD2   
3301 N N     . VAL   D 95  ? 0.4876 0.2909 0.3406 0.0091  -0.0057 0.0179  94  VAL   D N     
3302 C CA    . VAL   D 95  ? 0.4305 0.2803 0.3203 0.0010  -0.0016 0.0196  94  VAL   D CA    
3303 C C     . VAL   D 95  ? 0.4205 0.2793 0.3133 -0.0132 0.0010  0.0187  94  VAL   D C     
3304 O O     . VAL   D 95  ? 0.3677 0.2606 0.2882 -0.0122 0.0044  0.0180  94  VAL   D O     
3305 C CB    . VAL   D 95  ? 0.4188 0.2811 0.3167 -0.0104 -0.0028 0.0252  94  VAL   D CB    
3306 C CG1   . VAL   D 95  ? 0.4438 0.2885 0.3204 -0.0339 -0.0037 0.0288  94  VAL   D CG1   
3307 C CG2   . VAL   D 95  ? 0.3700 0.2791 0.3068 -0.0103 0.0006  0.0260  94  VAL   D CG2   
3308 N N     . LEU   D 96  ? 0.4619 0.2889 0.3245 -0.0265 -0.0012 0.0187  95  LEU   D N     
3309 C CA    . LEU   D 96  ? 0.4655 0.3001 0.3285 -0.0403 -0.0003 0.0175  95  LEU   D CA    
3310 C C     . LEU   D 96  ? 0.4642 0.2980 0.3275 -0.0277 0.0026  0.0120  95  LEU   D C     
3311 O O     . LEU   D 96  ? 0.4852 0.3323 0.3544 -0.0363 0.0035  0.0111  95  LEU   D O     
3312 C CB    . LEU   D 96  ? 0.5135 0.3159 0.3440 -0.0607 -0.0038 0.0187  95  LEU   D CB    
3313 C CG    . LEU   D 96  ? 0.5196 0.3233 0.3469 -0.0776 -0.0052 0.0238  95  LEU   D CG    
3314 C CD1   . LEU   D 96  ? 0.5678 0.3440 0.3642 -0.1012 -0.0077 0.0239  95  LEU   D CD1   
3315 C CD2   . LEU   D 96  ? 0.4728 0.3268 0.3382 -0.0833 -0.0030 0.0265  95  LEU   D CD2   
3316 N N     . ALA   D 97  ? 0.4732 0.2930 0.3297 -0.0073 0.0039  0.0078  96  ALA   D N     
3317 C CA    . ALA   D 97  ? 0.4810 0.2986 0.3344 0.0043  0.0079  0.0015  96  ALA   D CA    
3318 C C     . ALA   D 97  ? 0.4360 0.2947 0.3248 0.0167  0.0133  0.0001  96  ALA   D C     
3319 O O     . ALA   D 97  ? 0.4100 0.2810 0.3133 0.0281  0.0131  0.0005  96  ALA   D O     
3320 C CB    . ALA   D 97  ? 0.5262 0.3029 0.3481 0.0196  0.0064  -0.0036 96  ALA   D CB    
3321 N N     . PHE   D 98  ? 0.4250 0.3012 0.3236 0.0141  0.0179  -0.0019 97  PHE   D N     
3322 C CA    . PHE   D 98  ? 0.4080 0.3183 0.3342 0.0229  0.0241  -0.0038 97  PHE   D CA    
3323 C C     . PHE   D 98  ? 0.4258 0.3328 0.3502 0.0438  0.0279  -0.0109 97  PHE   D C     
3324 O O     . PHE   D 98  ? 0.4780 0.3535 0.3754 0.0508  0.0269  -0.0153 97  PHE   D O     
3325 C CB    . PHE   D 98  ? 0.3980 0.3183 0.3255 0.0139  0.0278  -0.0043 97  PHE   D CB    
3326 C CG    . PHE   D 98  ? 0.3718 0.3266 0.3265 0.0164  0.0337  -0.0039 97  PHE   D CG    
3327 C CD1   . PHE   D 98  ? 0.3562 0.3345 0.3339 0.0110  0.0316  0.0015  97  PHE   D CD1   
3328 C CD2   . PHE   D 98  ? 0.3784 0.3404 0.3328 0.0217  0.0414  -0.0088 97  PHE   D CD2   
3329 C CE1   . PHE   D 98  ? 0.3450 0.3496 0.3432 0.0114  0.0364  0.0020  97  PHE   D CE1   
3330 C CE2   . PHE   D 98  ? 0.3695 0.3598 0.3448 0.0201  0.0469  -0.0079 97  PHE   D CE2   
3331 C CZ    . PHE   D 98  ? 0.3553 0.3652 0.3517 0.0149  0.0441  -0.0024 97  PHE   D CZ    
3332 N N     . GLY   D 99  ? 0.3979 0.3382 0.3503 0.0529  0.0323  -0.0126 98  GLY   D N     
3333 C CA    . GLY   D 99  ? 0.4062 0.3569 0.3651 0.0726  0.0369  -0.0205 98  GLY   D CA    
3334 C C     . GLY   D 99  ? 0.4119 0.3732 0.3843 0.0857  0.0326  -0.0208 98  GLY   D C     
3335 O O     . GLY   D 99  ? 0.4230 0.3812 0.3915 0.1048  0.0326  -0.0276 98  GLY   D O     
3336 N N     . TRP   D 100 ? 0.4045 0.3799 0.3930 0.0770  0.0286  -0.0142 99  TRP   D N     
3337 C CA    . TRP   D 100 ? 0.4022 0.3954 0.4081 0.0880  0.0251  -0.0147 99  TRP   D CA    
3338 C C     . TRP   D 100 ? 0.3678 0.4028 0.4035 0.0932  0.0323  -0.0199 99  TRP   D C     
3339 O O     . TRP   D 100 ? 0.3531 0.4092 0.4052 0.0796  0.0364  -0.0167 99  TRP   D O     
3340 C CB    . TRP   D 100 ? 0.3709 0.3667 0.3835 0.0752  0.0200  -0.0065 99  TRP   D CB    
3341 C CG    . TRP   D 100 ? 0.3867 0.3463 0.3725 0.0696  0.0131  -0.0016 99  TRP   D CG    
3342 C CD1   . TRP   D 100 ? 0.4228 0.3438 0.3764 0.0697  0.0107  -0.0023 99  TRP   D CD1   
3343 C CD2   . TRP   D 100 ? 0.3869 0.3455 0.3743 0.0609  0.0083  0.0049  99  TRP   D CD2   
3344 N NE1   . TRP   D 100 ? 0.4299 0.3260 0.3648 0.0600  0.0048  0.0035  99  TRP   D NE1   
3345 C CE2   . TRP   D 100 ? 0.4129 0.3323 0.3682 0.0551  0.0035  0.0079  99  TRP   D CE2   
3346 C CE3   . TRP   D 100 ? 0.3619 0.3474 0.3725 0.0570  0.0078  0.0080  99  TRP   D CE3   
3347 C CZ2   . TRP   D 100 ? 0.4284 0.3375 0.3755 0.0448  -0.0007 0.0140  99  TRP   D CZ2   
3348 C CZ3   . TRP   D 100 ? 0.3694 0.3444 0.3720 0.0491  0.0032  0.0136  99  TRP   D CZ3   
3349 C CH2   . TRP   D 100 ? 0.4106 0.3493 0.3824 0.0421  -0.0004 0.0168  99  TRP   D CH2   
3350 N N     . GLY   D 101 ? 0.3745 0.4209 0.4152 0.1120  0.0343  -0.0285 100 GLY   D N     
3351 C CA    . GLY   D 101 ? 0.3503 0.4396 0.4190 0.1157  0.0422  -0.0349 100 GLY   D CA    
3352 C C     . GLY   D 101 ? 0.3461 0.4461 0.4181 0.1003  0.0525  -0.0347 100 GLY   D C     
3353 O O     . GLY   D 101 ? 0.3968 0.4718 0.4471 0.0956  0.0546  -0.0340 100 GLY   D O     
3354 N N     . ASN   D 102 ? 0.3186 0.4511 0.4143 0.0900  0.0576  -0.0340 101 ASN   D N     
3355 C CA    . ASN   D 102 ? 0.3115 0.4540 0.4095 0.0744  0.0668  -0.0328 101 ASN   D CA    
3356 C C     . ASN   D 102 ? 0.2837 0.4081 0.3728 0.0567  0.0630  -0.0227 101 ASN   D C     
3357 O O     . ASN   D 102 ? 0.2486 0.3777 0.3372 0.0441  0.0687  -0.0207 101 ASN   D O     
3358 C CB    . ASN   D 102 ? 0.3159 0.4996 0.4408 0.0713  0.0738  -0.0373 101 ASN   D CB    
3359 C CG    . ASN   D 102 ? 0.3140 0.5101 0.4556 0.0646  0.0675  -0.0321 101 ASN   D CG    
3360 O OD1   . ASN   D 102 ? 0.2879 0.4631 0.4218 0.0631  0.0584  -0.0252 101 ASN   D OD1   
3361 N ND2   . ASN   D 102 ? 0.3109 0.5410 0.4742 0.0595  0.0727  -0.0359 101 ASN   D ND2   
3362 N N     . GLU   D 103 ? 0.2752 0.3804 0.3574 0.0559  0.0534  -0.0167 102 GLU   D N     
3363 C CA    . GLU   D 103 ? 0.2678 0.3589 0.3426 0.0419  0.0491  -0.0085 102 GLU   D CA    
3364 C C     . GLU   D 103 ? 0.2433 0.3541 0.3339 0.0307  0.0517  -0.0051 102 GLU   D C     
3365 O O     . GLU   D 103 ? 0.2434 0.3463 0.3266 0.0201  0.0516  -0.0006 102 GLU   D O     
3366 C CB    . GLU   D 103 ? 0.2946 0.3603 0.3454 0.0378  0.0495  -0.0081 102 GLU   D CB    
3367 C CG    . GLU   D 103 ? 0.3166 0.3542 0.3472 0.0452  0.0439  -0.0092 102 GLU   D CG    
3368 C CD    . GLU   D 103 ? 0.3235 0.3478 0.3497 0.0394  0.0352  -0.0028 102 GLU   D CD    
3369 O OE1   . GLU   D 103 ? 0.3066 0.3461 0.3479 0.0314  0.0333  0.0022  102 GLU   D OE1   
3370 O OE2   . GLU   D 103 ? 0.3351 0.3317 0.3400 0.0422  0.0307  -0.0030 102 GLU   D OE2   
3371 N N     . GLN   D 104 ? 0.2368 0.3712 0.3473 0.0337  0.0527  -0.0074 103 GLN   D N     
3372 C CA    . GLN   D 104 ? 0.2464 0.3987 0.3704 0.0236  0.0559  -0.0057 103 GLN   D CA    
3373 C C     . GLN   D 104 ? 0.2117 0.3738 0.3496 0.0247  0.0497  -0.0037 103 GLN   D C     
3374 O O     . GLN   D 104 ? 0.1988 0.3643 0.3415 0.0353  0.0452  -0.0061 103 GLN   D O     
3375 C CB    . GLN   D 104 ? 0.2882 0.4642 0.4227 0.0241  0.0654  -0.0128 103 GLN   D CB    
3376 C CG    . GLN   D 104 ? 0.3268 0.5147 0.4675 0.0094  0.0707  -0.0111 103 GLN   D CG    
3377 C CD    . GLN   D 104 ? 0.3282 0.5429 0.4796 0.0071  0.0812  -0.0187 103 GLN   D CD    
3378 O OE1   . GLN   D 104 ? 0.3262 0.5400 0.4689 0.0087  0.0886  -0.0227 103 GLN   D OE1   
3379 N NE2   . GLN   D 104 ? 0.3265 0.5663 0.4965 0.0026  0.0823  -0.0214 103 GLN   D NE2   
3380 N N     . VAL   D 105 ? 0.2005 0.3646 0.3423 0.0143  0.0489  0.0006  104 VAL   D N     
3381 C CA    . VAL   D 105 ? 0.1848 0.3574 0.3379 0.0137  0.0438  0.0022  104 VAL   D CA    
3382 C C     . VAL   D 105 ? 0.1728 0.3661 0.3387 0.0064  0.0489  -0.0011 104 VAL   D C     
3383 O O     . VAL   D 105 ? 0.1815 0.3714 0.3413 -0.0037 0.0544  0.0001  104 VAL   D O     
3384 C CB    . VAL   D 105 ? 0.1708 0.3283 0.3167 0.0086  0.0384  0.0087  104 VAL   D CB    
3385 C CG1   . VAL   D 105 ? 0.1663 0.3291 0.3204 0.0114  0.0327  0.0095  104 VAL   D CG1   
3386 C CG2   . VAL   D 105 ? 0.1772 0.3158 0.3086 0.0102  0.0355  0.0117  104 VAL   D CG2   
3387 N N     . ASP   D 106 ? 0.1639 0.3771 0.3453 0.0106  0.0467  -0.0051 105 ASP   D N     
3388 C CA    . ASP   D 106 ? 0.1813 0.4171 0.3761 0.0019  0.0506  -0.0089 105 ASP   D CA    
3389 C C     . ASP   D 106 ? 0.1408 0.3745 0.3389 -0.0024 0.0442  -0.0061 105 ASP   D C     
3390 O O     . ASP   D 106 ? 0.1302 0.3690 0.3346 0.0060  0.0374  -0.0070 105 ASP   D O     
3391 C CB    . ASP   D 106 ? 0.2262 0.4923 0.4384 0.0101  0.0525  -0.0175 105 ASP   D CB    
3392 C CG    . ASP   D 106 ? 0.3297 0.6076 0.5428 0.0117  0.0619  -0.0230 105 ASP   D CG    
3393 O OD1   . ASP   D 106 ? 0.3873 0.6449 0.5840 0.0086  0.0662  -0.0198 105 ASP   D OD1   
3394 O OD2   . ASP   D 106 ? 0.5432 0.8537 0.7741 0.0154  0.0652  -0.0312 105 ASP   D OD2   
3395 N N     . SER   D 107 ? 0.1341 0.3594 0.3261 -0.0154 0.0464  -0.0032 106 SER   D N     
3396 C CA    . SER   D 107 ? 0.1292 0.3481 0.3203 -0.0194 0.0408  -0.0008 106 SER   D CA    
3397 C C     . SER   D 107 ? 0.1332 0.3625 0.3281 -0.0338 0.0449  -0.0039 106 SER   D C     
3398 O O     . SER   D 107 ? 0.1336 0.3625 0.3231 -0.0439 0.0526  -0.0045 106 SER   D O     
3399 C CB    . SER   D 107 ? 0.1199 0.3126 0.2957 -0.0196 0.0379  0.0057  106 SER   D CB    
3400 O OG    . SER   D 107 ? 0.1127 0.2972 0.2845 -0.0096 0.0346  0.0082  106 SER   D OG    
3401 N N     . LYS   D 108 ? 0.1271 0.3617 0.3276 -0.0359 0.0395  -0.0052 107 LYS   D N     
3402 C CA    . LYS   D 108 ? 0.1399 0.3781 0.3398 -0.0513 0.0416  -0.0076 107 LYS   D CA    
3403 C C     . LYS   D 108 ? 0.1389 0.3603 0.3308 -0.0515 0.0344  -0.0052 107 LYS   D C     
3404 O O     . LYS   D 108 ? 0.1298 0.3528 0.3261 -0.0400 0.0277  -0.0046 107 LYS   D O     
3405 C CB    . LYS   D 108 ? 0.1401 0.4151 0.3606 -0.0557 0.0434  -0.0156 107 LYS   D CB    
3406 C CG    . LYS   D 108 ? 0.1594 0.4404 0.3782 -0.0768 0.0481  -0.0187 107 LYS   D CG    
3407 C CD    . LYS   D 108 ? 0.1543 0.4799 0.3975 -0.0812 0.0507  -0.0279 107 LYS   D CD    
3408 C CE    . LYS   D 108 ? 0.1721 0.5075 0.4141 -0.1054 0.0570  -0.0318 107 LYS   D CE    
3409 N NZ    . LYS   D 108 ? 0.1634 0.5490 0.4330 -0.1082 0.0591  -0.0416 107 LYS   D NZ    
3410 N N     . ALA   D 109 ? 0.1627 0.3659 0.3402 -0.0647 0.0361  -0.0039 108 ALA   D N     
3411 C CA    . ALA   D 109 ? 0.1810 0.3674 0.3486 -0.0668 0.0303  -0.0032 108 ALA   D CA    
3412 C C     . ALA   D 109 ? 0.1896 0.3777 0.3532 -0.0859 0.0327  -0.0072 108 ALA   D C     
3413 O O     . ALA   D 109 ? 0.1938 0.3751 0.3482 -0.0987 0.0395  -0.0068 108 ALA   D O     
3414 C CB    . ALA   D 109 ? 0.1957 0.3493 0.3433 -0.0613 0.0287  0.0026  108 ALA   D CB    
3415 N N     . SER   D 110 ? 0.1889 0.3861 0.3582 -0.0885 0.0271  -0.0112 109 SER   D N     
3416 C CA    . SER   D 110 ? 0.2257 0.4268 0.3920 -0.1081 0.0280  -0.0159 109 SER   D CA    
3417 C C     . SER   D 110 ? 0.2437 0.4205 0.3947 -0.1075 0.0207  -0.0156 109 SER   D C     
3418 O O     . SER   D 110 ? 0.2388 0.4230 0.3978 -0.0936 0.0143  -0.0159 109 SER   D O     
3419 C CB    . SER   D 110 ? 0.2133 0.4595 0.4063 -0.1127 0.0276  -0.0234 109 SER   D CB    
3420 O OG    . SER   D 110 ? 0.2116 0.4835 0.4213 -0.1070 0.0334  -0.0246 109 SER   D OG    
3421 N N     . VAL   D 111 ? 0.2580 0.4040 0.3847 -0.1219 0.0219  -0.0152 110 VAL   D N     
3422 C CA    . VAL   D 111 ? 0.2811 0.4014 0.3901 -0.1220 0.0155  -0.0162 110 VAL   D CA    
3423 C C     . VAL   D 111 ? 0.2909 0.4101 0.3921 -0.1458 0.0159  -0.0215 110 VAL   D C     
3424 O O     . VAL   D 111 ? 0.3162 0.4217 0.4037 -0.1617 0.0221  -0.0205 110 VAL   D O     
3425 C CB    . VAL   D 111 ? 0.3063 0.3819 0.3874 -0.1129 0.0147  -0.0109 110 VAL   D CB    
3426 C CG1   . VAL   D 111 ? 0.3358 0.3815 0.3944 -0.1152 0.0093  -0.0132 110 VAL   D CG1   
3427 C CG2   . VAL   D 111 ? 0.2873 0.3681 0.3778 -0.0908 0.0135  -0.0066 110 VAL   D CG2   
3428 N N     . THR   D 112 ? 0.2859 0.4153 0.3918 -0.1488 0.0091  -0.0267 111 THR   D N     
3429 C CA    . THR   D 112 ? 0.3190 0.4467 0.4160 -0.1728 0.0080  -0.0325 111 THR   D CA    
3430 C C     . THR   D 112 ? 0.3368 0.4259 0.4068 -0.1709 0.0013  -0.0332 111 THR   D C     
3431 O O     . THR   D 112 ? 0.3124 0.4062 0.3884 -0.1539 -0.0049 -0.0336 111 THR   D O     
3432 C CB    . THR   D 112 ? 0.3027 0.4835 0.4315 -0.1796 0.0054  -0.0397 111 THR   D CB    
3433 O OG1   . THR   D 112 ? 0.3047 0.5146 0.4529 -0.1820 0.0134  -0.0394 111 THR   D OG1   
3434 C CG2   . THR   D 112 ? 0.3287 0.5145 0.4516 -0.2062 0.0034  -0.0468 111 THR   D CG2   
3435 N N     . ILE   D 113 ? 0.3752 0.4241 0.4132 -0.1880 0.0031  -0.0334 112 ILE   D N     
3436 C CA    . ILE   D 113 ? 0.4207 0.4263 0.4269 -0.1886 -0.0025 -0.0350 112 ILE   D CA    
3437 C C     . ILE   D 113 ? 0.4444 0.4529 0.4433 -0.2172 -0.0046 -0.0421 112 ILE   D C     
3438 O O     . ILE   D 113 ? 0.4547 0.4586 0.4449 -0.2404 0.0013  -0.0426 112 ILE   D O     
3439 C CB    . ILE   D 113 ? 0.4567 0.4064 0.4263 -0.1830 -0.0001 -0.0295 112 ILE   D CB    
3440 C CG1   . ILE   D 113 ? 0.4359 0.3902 0.4166 -0.1572 0.0022  -0.0228 112 ILE   D CG1   
3441 C CG2   . ILE   D 113 ? 0.4957 0.4014 0.4328 -0.1793 -0.0064 -0.0324 112 ILE   D CG2   
3442 C CD1   . ILE   D 113 ? 0.4712 0.3806 0.4216 -0.1527 0.0049  -0.0171 112 ILE   D CD1   
3443 N N     . GLY   D 114 ? 0.4547 0.4726 0.4571 -0.2163 -0.0127 -0.0477 113 GLY   D N     
3444 C CA    . GLY   D 114 ? 0.4962 0.5150 0.4896 -0.2425 -0.0166 -0.0552 113 GLY   D CA    
3445 C C     . GLY   D 114 ? 0.5674 0.5276 0.5182 -0.2428 -0.0212 -0.0564 113 GLY   D C     
3446 O O     . GLY   D 114 ? 0.5982 0.5547 0.5485 -0.2227 -0.0274 -0.0573 113 GLY   D O     
3447 N N     . SER   E 1   ? 0.4479 0.5966 0.6589 -0.1318 -0.1259 -0.0615 1   SER   E N     
3448 C CA    . SER   E 1   ? 0.4921 0.6068 0.6943 -0.1545 -0.1358 -0.0601 1   SER   E CA    
3449 C C     . SER   E 1   ? 0.4751 0.5551 0.6618 -0.1600 -0.1322 -0.0484 1   SER   E C     
3450 O O     . SER   E 1   ? 0.5080 0.5762 0.6902 -0.1863 -0.1339 -0.0396 1   SER   E O     
3451 C CB    . SER   E 1   ? 0.5155 0.6002 0.7052 -0.1500 -0.1516 -0.0733 1   SER   E CB    
3452 O OG    . SER   E 1   ? 0.5528 0.6262 0.7445 -0.1759 -0.1634 -0.0744 1   SER   E OG    
3453 N N     . VAL   E 2   ? 0.4603 0.5215 0.6369 -0.1377 -0.1294 -0.0484 2   VAL   E N     
3454 C CA    . VAL   E 2   ? 0.4457 0.4897 0.6125 -0.1383 -0.1234 -0.0357 2   VAL   E CA    
3455 C C     . VAL   E 2   ? 0.3820 0.4522 0.5544 -0.1149 -0.1088 -0.0357 2   VAL   E C     
3456 O O     . VAL   E 2   ? 0.3650 0.4369 0.5378 -0.0939 -0.1091 -0.0462 2   VAL   E O     
3457 C CB    . VAL   E 2   ? 0.4926 0.4785 0.6423 -0.1377 -0.1396 -0.0343 2   VAL   E CB    
3458 C CG1   . VAL   E 2   ? 0.5416 0.4949 0.6794 -0.1679 -0.1543 -0.0280 2   VAL   E CG1   
3459 C CG2   . VAL   E 2   ? 0.4954 0.4643 0.6480 -0.1125 -0.1476 -0.0520 2   VAL   E CG2   
3460 N N     . THR   E 3   ? 0.3417 0.4316 0.5162 -0.1214 -0.0955 -0.0249 3   THR   E N     
3461 C CA    . THR   E 3   ? 0.2980 0.4130 0.4779 -0.1033 -0.0817 -0.0236 3   THR   E CA    
3462 C C     . THR   E 3   ? 0.2961 0.3892 0.4613 -0.1051 -0.0777 -0.0127 3   THR   E C     
3463 O O     . THR   E 3   ? 0.3083 0.3853 0.4615 -0.1278 -0.0793 -0.0031 3   THR   E O     
3464 C CB    . THR   E 3   ? 0.2913 0.4552 0.4915 -0.1068 -0.0700 -0.0247 3   THR   E CB    
3465 O OG1   . THR   E 3   ? 0.3046 0.4864 0.5187 -0.1084 -0.0784 -0.0339 3   THR   E OG1   
3466 C CG2   . THR   E 3   ? 0.2696 0.4553 0.4758 -0.0844 -0.0601 -0.0258 3   THR   E CG2   
3467 N N     . ILE   E 4   ? 0.2738 0.3670 0.4378 -0.0835 -0.0726 -0.0139 4   ILE   E N     
3468 C CA    . ILE   E 4   ? 0.2876 0.3693 0.4405 -0.0825 -0.0673 -0.0043 4   ILE   E CA    
3469 C C     . ILE   E 4   ? 0.2416 0.3591 0.4035 -0.0707 -0.0509 -0.0050 4   ILE   E C     
3470 O O     . ILE   E 4   ? 0.2289 0.3590 0.3983 -0.0527 -0.0494 -0.0124 4   ILE   E O     
3471 C CB    . ILE   E 4   ? 0.3075 0.3549 0.4539 -0.0672 -0.0781 -0.0064 4   ILE   E CB    
3472 C CG1   . ILE   E 4   ? 0.3410 0.3600 0.4893 -0.0646 -0.0950 -0.0156 4   ILE   E CG1   
3473 C CG2   . ILE   E 4   ? 0.3307 0.3533 0.4602 -0.0755 -0.0815 0.0066  4   ILE   E CG2   
3474 C CD1   . ILE   E 4   ? 0.3895 0.3758 0.5255 -0.0877 -0.1101 -0.0082 4   ILE   E CD1   
3475 N N     . THR   E 5   ? 0.2341 0.3619 0.3910 -0.0813 -0.0400 0.0024  5   THR   E N     
3476 C CA    . THR   E 5   ? 0.2215 0.3807 0.3882 -0.0705 -0.0255 0.0002  5   THR   E CA    
3477 C C     . THR   E 5   ? 0.2301 0.3728 0.3786 -0.0731 -0.0203 0.0085  5   THR   E C     
3478 O O     . THR   E 5   ? 0.2520 0.3767 0.3824 -0.0945 -0.0215 0.0166  5   THR   E O     
3479 C CB    . THR   E 5   ? 0.2285 0.4288 0.4147 -0.0811 -0.0146 -0.0051 5   THR   E CB    
3480 O OG1   . THR   E 5   ? 0.2507 0.4601 0.4511 -0.0824 -0.0240 -0.0114 5   THR   E OG1   
3481 C CG2   . THR   E 5   ? 0.1943 0.4236 0.3953 -0.0638 -0.0042 -0.0108 5   THR   E CG2   
3482 N N     . ILE   E 6   ? 0.2144 0.3605 0.3642 -0.0537 -0.0161 0.0068  6   ILE   E N     
3483 C CA    . ILE   E 6   ? 0.2305 0.3642 0.3649 -0.0537 -0.0115 0.0130  6   ILE   E CA    
3484 C C     . ILE   E 6   ? 0.2072 0.3693 0.3521 -0.0414 0.0020  0.0077  6   ILE   E C     
3485 O O     . ILE   E 6   ? 0.1873 0.3570 0.3422 -0.0236 0.0006  0.0028  6   ILE   E O     
3486 C CB    . ILE   E 6   ? 0.2366 0.3385 0.3628 -0.0427 -0.0240 0.0155  6   ILE   E CB    
3487 C CG1   . ILE   E 6   ? 0.2567 0.3277 0.3778 -0.0510 -0.0416 0.0175  6   ILE   E CG1   
3488 C CG2   . ILE   E 6   ? 0.2388 0.3282 0.3484 -0.0449 -0.0215 0.0224  6   ILE   E CG2   
3489 C CD1   . ILE   E 6   ? 0.2598 0.3062 0.3853 -0.0361 -0.0558 0.0132  6   ILE   E CD1   
3490 N N     . ASN   E 7   ? 0.2200 0.3950 0.3599 -0.0525 0.0144  0.0081  7   ASN   E N     
3491 C CA    . ASN   E 7   ? 0.2141 0.4081 0.3605 -0.0413 0.0260  0.0023  7   ASN   E CA    
3492 C C     . ASN   E 7   ? 0.2141 0.3820 0.3373 -0.0399 0.0251  0.0093  7   ASN   E C     
3493 O O     . ASN   E 7   ? 0.2450 0.3883 0.3462 -0.0551 0.0198  0.0179  7   ASN   E O     
3494 C CB    . ASN   E 7   ? 0.2261 0.4518 0.3821 -0.0549 0.0419  -0.0059 7   ASN   E CB    
3495 C CG    . ASN   E 7   ? 0.2477 0.5046 0.4329 -0.0570 0.0418  -0.0149 7   ASN   E CG    
3496 O OD1   . ASN   E 7   ? 0.2370 0.5136 0.4471 -0.0379 0.0384  -0.0232 7   ASN   E OD1   
3497 N ND2   . ASN   E 7   ? 0.2757 0.5338 0.4565 -0.0808 0.0425  -0.0124 7   ASN   E ND2   
3498 N N     . GLN   E 8   ? 0.1998 0.3714 0.3269 -0.0231 0.0284  0.0058  8   GLN   E N     
3499 C CA    . GLN   E 8   ? 0.2232 0.3716 0.3327 -0.0192 0.0254  0.0112  8   GLN   E CA    
3500 C C     . GLN   E 8   ? 0.2155 0.3768 0.3280 -0.0097 0.0360  0.0046  8   GLN   E C     
3501 O O     . GLN   E 8   ? 0.2166 0.3916 0.3459 0.0052  0.0365  -0.0016 8   GLN   E O     
3502 C CB    . GLN   E 8   ? 0.2046 0.3350 0.3163 -0.0081 0.0130  0.0139  8   GLN   E CB    
3503 C CG    . GLN   E 8   ? 0.2279 0.3403 0.3285 -0.0039 0.0095  0.0170  8   GLN   E CG    
3504 C CD    . GLN   E 8   ? 0.2222 0.3284 0.3328 0.0077  0.0022  0.0141  8   GLN   E CD    
3505 O OE1   . GLN   E 8   ? 0.2559 0.3575 0.3748 0.0085  -0.0059 0.0120  8   GLN   E OE1   
3506 N NE2   . GLN   E 8   ? 0.2297 0.3363 0.3397 0.0155  0.0056  0.0122  8   GLN   E NE2   
3507 N N     . LYS   E 9   ? 0.2270 0.3800 0.3205 -0.0191 0.0420  0.0060  9   LYS   E N     
3508 C CA    . LYS   E 9   ? 0.2421 0.4011 0.3342 -0.0114 0.0512  -0.0014 9   LYS   E CA    
3509 C C     . LYS   E 9   ? 0.2206 0.3522 0.2939 -0.0092 0.0434  0.0060  9   LYS   E C     
3510 O O     . LYS   E 9   ? 0.2291 0.3418 0.2820 -0.0228 0.0374  0.0139  9   LYS   E O     
3511 C CB    . LYS   E 9   ? 0.2586 0.4358 0.3450 -0.0273 0.0669  -0.0096 9   LYS   E CB    
3512 C CG    . LYS   E 9   ? 0.3098 0.4885 0.3854 -0.0265 0.0781  -0.0187 9   LYS   E CG    
3513 C CD    . LYS   E 9   ? 0.3597 0.5528 0.4191 -0.0505 0.0954  -0.0264 9   LYS   E CD    
3514 C CE    . LYS   E 9   ? 0.3829 0.6174 0.4743 -0.0524 0.1080  -0.0413 9   LYS   E CE    
3515 N NZ    . LYS   E 9   ? 0.4398 0.6965 0.5201 -0.0781 0.1289  -0.0527 9   LYS   E NZ    
3516 N N     . GLY   E 10  ? 0.2067 0.3349 0.2865 0.0065  0.0416  0.0035  10  GLY   E N     
3517 C CA    . GLY   E 10  ? 0.2044 0.3126 0.2707 0.0083  0.0366  0.0072  10  GLY   E CA    
3518 C C     . GLY   E 10  ? 0.2131 0.3208 0.2693 0.0092  0.0456  0.0001  10  GLY   E C     
3519 O O     . GLY   E 10  ? 0.2116 0.3317 0.2808 0.0199  0.0516  -0.0089 10  GLY   E O     
3520 N N     . GLU   E 11  ? 0.2268 0.3186 0.2603 -0.0016 0.0443  0.0032  11  GLU   E N     
3521 C CA    . GLU   E 11  ? 0.2428 0.3301 0.2618 -0.0027 0.0522  -0.0046 11  GLU   E CA    
3522 C C     . GLU   E 11  ? 0.2436 0.3075 0.2475 -0.0042 0.0420  0.0011  11  GLU   E C     
3523 O O     . GLU   E 11  ? 0.2211 0.2744 0.2244 -0.0079 0.0292  0.0104  11  GLU   E O     
3524 C CB    . GLU   E 11  ? 0.2687 0.3628 0.2688 -0.0206 0.0631  -0.0088 11  GLU   E CB    
3525 C CG    . GLU   E 11  ? 0.2634 0.3886 0.2853 -0.0188 0.0765  -0.0199 11  GLU   E CG    
3526 C CD    . GLU   E 11  ? 0.2953 0.4321 0.2982 -0.0407 0.0917  -0.0270 11  GLU   E CD    
3527 O OE1   . GLU   E 11  ? 0.3208 0.4759 0.3290 -0.0387 0.1076  -0.0453 11  GLU   E OE1   
3528 O OE2   . GLU   E 11  ? 0.3078 0.4358 0.2921 -0.0600 0.0877  -0.0157 11  GLU   E OE2   
3529 N N     . ILE   E 12  ? 0.2615 0.3185 0.2547 -0.0020 0.0474  -0.0068 12  ILE   E N     
3530 C CA    . ILE   E 12  ? 0.2856 0.3210 0.2614 -0.0065 0.0388  -0.0036 12  ILE   E CA    
3531 C C     . ILE   E 12  ? 0.3130 0.3378 0.2574 -0.0250 0.0382  -0.0015 12  ILE   E C     
3532 O O     . ILE   E 12  ? 0.3456 0.3795 0.2778 -0.0322 0.0523  -0.0103 12  ILE   E O     
3533 C CB    . ILE   E 12  ? 0.2899 0.3182 0.2655 0.0030  0.0434  -0.0132 12  ILE   E CB    
3534 C CG1   . ILE   E 12  ? 0.2623 0.2960 0.2613 0.0191  0.0431  -0.0146 12  ILE   E CG1   
3535 C CG2   . ILE   E 12  ? 0.3143 0.3212 0.2737 -0.0030 0.0340  -0.0104 12  ILE   E CG2   
3536 C CD1   . ILE   E 12  ? 0.2489 0.2824 0.2597 0.0196  0.0340  -0.0040 12  ILE   E CD1   
3537 N N     . THR   E 13  ? 0.3360 0.3418 0.2672 -0.0334 0.0214  0.0086  13  THR   E N     
3538 C CA    . THR   E 13  ? 0.3706 0.3573 0.2639 -0.0531 0.0149  0.0135  13  THR   E CA    
3539 C C     . THR   E 13  ? 0.3951 0.3719 0.2615 -0.0594 0.0225  0.0038  13  THR   E C     
3540 O O     . THR   E 13  ? 0.3697 0.3466 0.2486 -0.0476 0.0246  -0.0033 13  THR   E O     
3541 C CB    . THR   E 13  ? 0.3861 0.3529 0.2776 -0.0573 -0.0113 0.0264  13  THR   E CB    
3542 O OG1   . THR   E 13  ? 0.3811 0.3437 0.2874 -0.0486 -0.0216 0.0245  13  THR   E OG1   
3543 C CG2   . THR   E 13  ? 0.3633 0.3362 0.2777 -0.0526 -0.0196 0.0336  13  THR   E CG2   
3544 N N     . GLU   E 14  ? 0.4405 0.4057 0.2657 -0.0804 0.0260  0.0038  14  GLU   E N     
3545 C CA    . GLU   E 14  ? 0.5040 0.4551 0.2942 -0.0913 0.0311  -0.0054 14  GLU   E CA    
3546 C C     . GLU   E 14  ? 0.4985 0.4268 0.2846 -0.0887 0.0094  0.0006  14  GLU   E C     
3547 O O     . GLU   E 14  ? 0.5111 0.4362 0.2961 -0.0832 0.0147  -0.0104 14  GLU   E O     
3548 C CB    . GLU   E 14  ? 0.5882 0.5233 0.3251 -0.1204 0.0325  -0.0017 14  GLU   E CB    
3549 C CG    . GLU   E 14  ? 0.6271 0.5873 0.3590 -0.1311 0.0596  -0.0128 14  GLU   E CG    
3550 C CD    . GLU   E 14  ? 0.7288 0.6710 0.4050 -0.1657 0.0593  -0.0042 14  GLU   E CD    
3551 O OE1   . GLU   E 14  ? 0.7796 0.6884 0.4094 -0.1822 0.0442  0.0029  14  GLU   E OE1   
3552 O OE2   . GLU   E 14  ? 0.7667 0.7271 0.4424 -0.1782 0.0746  -0.0056 14  GLU   E OE2   
3553 N N     . GLU   E 15  ? 0.4970 0.4108 0.2854 -0.0919 -0.0158 0.0161  15  GLU   E N     
3554 C CA    . GLU   E 15  ? 0.5119 0.4097 0.3056 -0.0895 -0.0396 0.0210  15  GLU   E CA    
3555 C C     . GLU   E 15  ? 0.4480 0.3618 0.2812 -0.0710 -0.0335 0.0127  15  GLU   E C     
3556 O O     . GLU   E 15  ? 0.4510 0.3540 0.2766 -0.0730 -0.0390 0.0081  15  GLU   E O     
3557 C CB    . GLU   E 15  ? 0.5537 0.4413 0.3605 -0.0895 -0.0678 0.0351  15  GLU   E CB    
3558 C CG    . GLU   E 15  ? 0.6547 0.5206 0.4229 -0.1083 -0.0779 0.0471  15  GLU   E CG    
3559 C CD    . GLU   E 15  ? 0.7022 0.5816 0.4904 -0.1039 -0.0712 0.0518  15  GLU   E CD    
3560 O OE1   . GLU   E 15  ? 0.6632 0.5565 0.4383 -0.1110 -0.0455 0.0464  15  GLU   E OE1   
3561 O OE2   . GLU   E 15  ? 0.7341 0.6130 0.5548 -0.0927 -0.0909 0.0580  15  GLU   E OE2   
3562 N N     . GLN   E 16  ? 0.3926 0.3289 0.2618 -0.0559 -0.0220 0.0108  16  GLN   E N     
3563 C CA    . GLN   E 16  ? 0.3632 0.3100 0.2613 -0.0424 -0.0155 0.0046  16  GLN   E CA    
3564 C C     . GLN   E 16  ? 0.3790 0.3177 0.2597 -0.0414 -0.0017 -0.0074 16  GLN   E C     
3565 O O     . GLN   E 16  ? 0.3761 0.3053 0.2596 -0.0400 -0.0059 -0.0108 16  GLN   E O     
3566 C CB    . GLN   E 16  ? 0.3244 0.2924 0.2549 -0.0291 -0.0062 0.0052  16  GLN   E CB    
3567 C CG    . GLN   E 16  ? 0.3049 0.2829 0.2631 -0.0258 -0.0190 0.0123  16  GLN   E CG    
3568 C CD    . GLN   E 16  ? 0.2774 0.2733 0.2556 -0.0166 -0.0089 0.0128  16  GLN   E CD    
3569 O OE1   . GLN   E 16  ? 0.2825 0.2809 0.2530 -0.0194 -0.0058 0.0156  16  GLN   E OE1   
3570 N NE2   . GLN   E 16  ? 0.2651 0.2722 0.2654 -0.0081 -0.0034 0.0101  16  GLN   E NE2   
3571 N N     . LYS   E 17  ? 0.3927 0.3354 0.2561 -0.0434 0.0142  -0.0154 17  LYS   E N     
3572 C CA    . LYS   E 17  ? 0.4169 0.3541 0.2678 -0.0401 0.0278  -0.0315 17  LYS   E CA    
3573 C C     . LYS   E 17  ? 0.4521 0.3656 0.2672 -0.0541 0.0209  -0.0356 17  LYS   E C     
3574 O O     . LYS   E 17  ? 0.4570 0.3578 0.2696 -0.0493 0.0221  -0.0455 17  LYS   E O     
3575 C CB    . LYS   E 17  ? 0.4256 0.3815 0.2755 -0.0385 0.0479  -0.0432 17  LYS   E CB    
3576 C CG    . LYS   E 17  ? 0.4046 0.3830 0.2922 -0.0228 0.0529  -0.0411 17  LYS   E CG    
3577 C CD    . LYS   E 17  ? 0.4328 0.4352 0.3257 -0.0222 0.0719  -0.0546 17  LYS   E CD    
3578 C CE    . LYS   E 17  ? 0.4307 0.4546 0.3517 -0.0155 0.0727  -0.0476 17  LYS   E CE    
3579 N NZ    . LYS   E 17  ? 0.4668 0.5191 0.4052 -0.0108 0.0903  -0.0638 17  LYS   E NZ    
3580 N N     . GLN   E 18  ? 0.4707 0.3742 0.2553 -0.0721 0.0112  -0.0276 18  GLN   E N     
3581 C CA    . GLN   E 18  ? 0.4998 0.3781 0.2465 -0.0876 -0.0002 -0.0289 18  GLN   E CA    
3582 C C     . GLN   E 18  ? 0.4909 0.3593 0.2566 -0.0824 -0.0183 -0.0250 18  GLN   E C     
3583 O O     . GLN   E 18  ? 0.5063 0.3593 0.2575 -0.0848 -0.0180 -0.0349 18  GLN   E O     
3584 C CB    . GLN   E 18  ? 0.5276 0.3907 0.2382 -0.1082 -0.0159 -0.0160 18  GLN   E CB    
3585 C CG    . GLN   E 18  ? 0.5477 0.4164 0.2285 -0.1225 0.0009  -0.0180 18  GLN   E CG    
3586 C CD    . GLN   E 18  ? 0.5805 0.4517 0.2303 -0.1316 0.0262  -0.0393 18  GLN   E CD    
3587 O OE1   . GLN   E 18  ? 0.5873 0.4470 0.2268 -0.1297 0.0275  -0.0517 18  GLN   E OE1   
3588 N NE2   . GLN   E 18  ? 0.6002 0.4852 0.2314 -0.1448 0.0460  -0.0447 18  GLN   E NE2   
3589 N N     . ARG   E 19  ? 0.4650 0.3451 0.2663 -0.0752 -0.0312 -0.0132 19  ARG   E N     
3590 C CA    . ARG   E 19  ? 0.4612 0.3407 0.2878 -0.0724 -0.0454 -0.0112 19  ARG   E CA    
3591 C C     . ARG   E 19  ? 0.4565 0.3340 0.2940 -0.0640 -0.0326 -0.0209 19  ARG   E C     
3592 O O     . ARG   E 19  ? 0.4642 0.3273 0.2956 -0.0702 -0.0405 -0.0248 19  ARG   E O     
3593 C CB    . ARG   E 19  ? 0.4417 0.3411 0.3082 -0.0654 -0.0557 -0.0016 19  ARG   E CB    
3594 C CG    . ARG   E 19  ? 0.4413 0.3466 0.3369 -0.0667 -0.0720 -0.0016 19  ARG   E CG    
3595 C CD    . ARG   E 19  ? 0.4141 0.3455 0.3547 -0.0574 -0.0730 0.0010  19  ARG   E CD    
3596 N NE    . ARG   E 19  ? 0.4234 0.3673 0.3960 -0.0606 -0.0847 -0.0032 19  ARG   E NE    
3597 C CZ    . ARG   E 19  ? 0.4142 0.3855 0.4305 -0.0552 -0.0846 -0.0060 19  ARG   E CZ    
3598 N NH1   . ARG   E 19  ? 0.3805 0.3656 0.4124 -0.0454 -0.0785 -0.0034 19  ARG   E NH1   
3599 N NH2   . ARG   E 19  ? 0.4199 0.4063 0.4647 -0.0614 -0.0902 -0.0132 19  ARG   E NH2   
3600 N N     . ALA   E 20  ? 0.4331 0.3213 0.2841 -0.0511 -0.0151 -0.0246 20  ALA   E N     
3601 C CA    . ALA   E 20  ? 0.4370 0.3166 0.2959 -0.0422 -0.0072 -0.0320 20  ALA   E CA    
3602 C C     . ALA   E 20  ? 0.4766 0.3325 0.3058 -0.0448 -0.0028 -0.0466 20  ALA   E C     
3603 O O     . ALA   E 20  ? 0.4712 0.3084 0.3001 -0.0435 -0.0059 -0.0511 20  ALA   E O     
3604 C CB    . ALA   E 20  ? 0.4046 0.2989 0.2848 -0.0271 0.0048  -0.0319 20  ALA   E CB    
3605 N N     . GLN   E 21  ? 0.5223 0.3769 0.3237 -0.0512 0.0036  -0.0543 21  GLN   E N     
3606 C CA    . GLN   E 21  ? 0.5834 0.4169 0.3542 -0.0557 0.0087  -0.0714 21  GLN   E CA    
3607 C C     . GLN   E 21  ? 0.6273 0.4388 0.3735 -0.0722 -0.0084 -0.0689 21  GLN   E C     
3608 O O     . GLN   E 21  ? 0.6541 0.4435 0.3798 -0.0745 -0.0070 -0.0831 21  GLN   E O     
3609 C CB    . GLN   E 21  ? 0.6168 0.4613 0.3675 -0.0579 0.0271  -0.0853 21  GLN   E CB    
3610 C CG    . GLN   E 21  ? 0.6114 0.4801 0.3926 -0.0402 0.0435  -0.0922 21  GLN   E CG    
3611 C CD    . GLN   E 21  ? 0.6317 0.4906 0.4335 -0.0204 0.0469  -0.1067 21  GLN   E CD    
3612 O OE1   . GLN   E 21  ? 0.6111 0.4660 0.4380 -0.0092 0.0382  -0.0965 21  GLN   E OE1   
3613 N NE2   . GLN   E 21  ? 0.6750 0.5270 0.4639 -0.0170 0.0582  -0.1313 21  GLN   E NE2   
3614 N N     . GLY   E 22  ? 0.6238 0.4402 0.3744 -0.0823 -0.0262 -0.0532 22  GLY   E N     
3615 C CA    . GLY   E 22  ? 0.6487 0.4475 0.3826 -0.0972 -0.0466 -0.0508 22  GLY   E CA    
3616 C C     . GLY   E 22  ? 0.6548 0.4497 0.4154 -0.0960 -0.0555 -0.0496 22  GLY   E C     
3617 O O     . GLY   E 22  ? 0.6392 0.4382 0.4231 -0.0850 -0.0454 -0.0506 22  GLY   E O     
3618 N N     . ASP   E 23  ? 0.6854 0.4722 0.4414 -0.1097 -0.0764 -0.0466 23  ASP   E N     
3619 C CA    . ASP   E 23  ? 0.7215 0.5019 0.4940 -0.1164 -0.0863 -0.0484 23  ASP   E CA    
3620 C C     . ASP   E 23  ? 0.6894 0.4963 0.5040 -0.1203 -0.1025 -0.0389 23  ASP   E C     
3621 O O     . ASP   E 23  ? 0.7282 0.5363 0.5605 -0.1293 -0.1103 -0.0413 23  ASP   E O     
3622 C CB    . ASP   E 23  ? 0.8245 0.5756 0.5588 -0.1310 -0.0981 -0.0575 23  ASP   E CB    
3623 C CG    . ASP   E 23  ? 0.9327 0.6547 0.6318 -0.1288 -0.0837 -0.0735 23  ASP   E CG    
3624 O OD1   . ASP   E 23  ? 1.0209 0.7450 0.7256 -0.1138 -0.0642 -0.0789 23  ASP   E OD1   
3625 O OD2   . ASP   E 23  ? 0.9677 0.6646 0.6362 -0.1416 -0.0936 -0.0824 23  ASP   E OD2   
3626 N N     . ASP   E 24  ? 0.6841 0.5131 0.5176 -0.1144 -0.1080 -0.0303 24  ASP   E N     
3627 C CA    . ASP   E 24  ? 0.6766 0.5338 0.5569 -0.1151 -0.1238 -0.0260 24  ASP   E CA    
3628 C C     . ASP   E 24  ? 0.6090 0.4908 0.5285 -0.1086 -0.1067 -0.0264 24  ASP   E C     
3629 O O     . ASP   E 24  ? 0.5934 0.4657 0.5004 -0.1026 -0.0867 -0.0269 24  ASP   E O     
3630 C CB    . ASP   E 24  ? 0.6919 0.5557 0.5741 -0.1111 -0.1401 -0.0181 24  ASP   E CB    
3631 C CG    . ASP   E 24  ? 0.7512 0.5891 0.5948 -0.1227 -0.1652 -0.0153 24  ASP   E CG    
3632 O OD1   . ASP   E 24  ? 0.7783 0.5934 0.5903 -0.1346 -0.1699 -0.0213 24  ASP   E OD1   
3633 O OD2   . ASP   E 24  ? 0.7753 0.6128 0.6186 -0.1207 -0.1824 -0.0069 24  ASP   E OD2   
3634 N N     . TRP   E 25  ? 0.5635 0.4765 0.5302 -0.1106 -0.1158 -0.0276 25  TRP   E N     
3635 C CA    . TRP   E 25  ? 0.5327 0.4709 0.5340 -0.1106 -0.0998 -0.0299 25  TRP   E CA    
3636 C C     . TRP   E 25  ? 0.4900 0.4355 0.4918 -0.0957 -0.0830 -0.0243 25  TRP   E C     
3637 O O     . TRP   E 25  ? 0.4867 0.4404 0.4951 -0.0865 -0.0910 -0.0208 25  TRP   E O     
3638 C CB    . TRP   E 25  ? 0.5209 0.4990 0.5779 -0.1157 -0.1117 -0.0372 25  TRP   E CB    
3639 C CG    . TRP   E 25  ? 0.5147 0.5222 0.6036 -0.1182 -0.0913 -0.0411 25  TRP   E CG    
3640 C CD1   . TRP   E 25  ? 0.4778 0.5109 0.5926 -0.1067 -0.0822 -0.0414 25  TRP   E CD1   
3641 C CD2   . TRP   E 25  ? 0.5179 0.5251 0.6053 -0.1354 -0.0763 -0.0442 25  TRP   E CD2   
3642 N NE1   . TRP   E 25  ? 0.4844 0.5351 0.6127 -0.1161 -0.0617 -0.0452 25  TRP   E NE1   
3643 C CE2   . TRP   E 25  ? 0.5112 0.5457 0.6220 -0.1349 -0.0580 -0.0460 25  TRP   E CE2   
3644 C CE3   . TRP   E 25  ? 0.5915 0.5749 0.6566 -0.1532 -0.0772 -0.0454 25  TRP   E CE3   
3645 C CZ2   . TRP   E 25  ? 0.5608 0.5990 0.6698 -0.1539 -0.0407 -0.0479 25  TRP   E CZ2   
3646 C CZ3   . TRP   E 25  ? 0.6192 0.6056 0.6860 -0.1715 -0.0615 -0.0469 25  TRP   E CZ3   
3647 C CH2   . TRP   E 25  ? 0.6005 0.6133 0.6868 -0.1729 -0.0432 -0.0474 25  TRP   E CH2   
3648 N N     . PRO   E 26  ? 0.4744 0.4170 0.4716 -0.0938 -0.0629 -0.0228 26  PRO   E N     
3649 C CA    . PRO   E 26  ? 0.4995 0.4247 0.4836 -0.1057 -0.0546 -0.0245 26  PRO   E CA    
3650 C C     . PRO   E 26  ? 0.5222 0.4053 0.4623 -0.1020 -0.0502 -0.0240 26  PRO   E C     
3651 O O     . PRO   E 26  ? 0.5110 0.3724 0.4377 -0.1097 -0.0450 -0.0242 26  PRO   E O     
3652 C CB    . PRO   E 26  ? 0.4880 0.4322 0.4906 -0.1047 -0.0389 -0.0219 26  PRO   E CB    
3653 C CG    . PRO   E 26  ? 0.4581 0.4054 0.4565 -0.0854 -0.0343 -0.0172 26  PRO   E CG    
3654 C CD    . PRO   E 26  ? 0.4601 0.4141 0.4635 -0.0804 -0.0497 -0.0182 26  PRO   E CD    
3655 N N     . TYR   E 27  ? 0.5177 0.3885 0.4350 -0.0916 -0.0524 -0.0249 27  TYR   E N     
3656 C CA    . TYR   E 27  ? 0.5388 0.3788 0.4226 -0.0837 -0.0445 -0.0292 27  TYR   E CA    
3657 C C     . TYR   E 27  ? 0.5976 0.4062 0.4566 -0.0951 -0.0521 -0.0366 27  TYR   E C     
3658 O O     . TYR   E 27  ? 0.6535 0.4336 0.4946 -0.0914 -0.0469 -0.0413 27  TYR   E O     
3659 C CB    . TYR   E 27  ? 0.5119 0.3574 0.3833 -0.0724 -0.0401 -0.0301 27  TYR   E CB    
3660 C CG    . TYR   E 27  ? 0.4560 0.3279 0.3511 -0.0615 -0.0323 -0.0231 27  TYR   E CG    
3661 C CD1   . TYR   E 27  ? 0.4282 0.2994 0.3290 -0.0505 -0.0202 -0.0223 27  TYR   E CD1   
3662 C CD2   . TYR   E 27  ? 0.4377 0.3324 0.3496 -0.0622 -0.0401 -0.0174 27  TYR   E CD2   
3663 C CE1   . TYR   E 27  ? 0.3953 0.2901 0.3168 -0.0420 -0.0141 -0.0164 27  TYR   E CE1   
3664 C CE2   . TYR   E 27  ? 0.3967 0.3137 0.3305 -0.0528 -0.0337 -0.0122 27  TYR   E CE2   
3665 C CZ    . TYR   E 27  ? 0.3776 0.2959 0.3157 -0.0433 -0.0197 -0.0118 27  TYR   E CZ    
3666 O OH    . TYR   E 27  ? 0.3421 0.2810 0.2990 -0.0351 -0.0142 -0.0074 27  TYR   E OH    
3667 N N     . GLY   E 28  ? 0.6190 0.4309 0.4789 -0.1086 -0.0669 -0.0382 28  GLY   E N     
3668 C CA    . GLY   E 28  ? 0.6483 0.4328 0.4882 -0.1225 -0.0761 -0.0451 28  GLY   E CA    
3669 C C     . GLY   E 28  ? 0.6549 0.4279 0.5029 -0.1330 -0.0731 -0.0439 28  GLY   E C     
3670 O O     . GLY   E 28  ? 0.6906 0.4258 0.5121 -0.1346 -0.0722 -0.0492 28  GLY   E O     
3671 N N     . GLN   E 29  ? 0.6253 0.4291 0.5081 -0.1414 -0.0715 -0.0383 29  GLN   E N     
3672 C CA    . GLN   E 29  ? 0.6437 0.4386 0.5304 -0.1574 -0.0667 -0.0360 29  GLN   E CA    
3673 C C     . GLN   E 29  ? 0.6636 0.4255 0.5260 -0.1470 -0.0566 -0.0316 29  GLN   E C     
3674 O O     . GLN   E 29  ? 0.7230 0.4477 0.5636 -0.1580 -0.0591 -0.0313 29  GLN   E O     
3675 C CB    . GLN   E 29  ? 0.6280 0.4686 0.5572 -0.1692 -0.0626 -0.0340 29  GLN   E CB    
3676 C CG    . GLN   E 29  ? 0.6577 0.4924 0.5875 -0.1934 -0.0553 -0.0321 29  GLN   E CG    
3677 C CD    . GLN   E 29  ? 0.7086 0.5219 0.6270 -0.2159 -0.0663 -0.0374 29  GLN   E CD    
3678 O OE1   . GLN   E 29  ? 0.6996 0.5369 0.6412 -0.2229 -0.0784 -0.0451 29  GLN   E OE1   
3679 N NE2   . GLN   E 29  ? 0.7402 0.5051 0.6225 -0.2272 -0.0655 -0.0337 29  GLN   E NE2   
3680 N N     . CYS   E 30  ? 0.6442 0.4164 0.5096 -0.1258 -0.0482 -0.0286 30  CYS   E N     
3681 C CA    . CYS   E 30  ? 0.6418 0.3851 0.4891 -0.1121 -0.0424 -0.0261 30  CYS   E CA    
3682 C C     . CYS   E 30  ? 0.6842 0.3817 0.5008 -0.1056 -0.0486 -0.0359 30  CYS   E C     
3683 O O     . CYS   E 30  ? 0.7084 0.3660 0.5068 -0.1085 -0.0530 -0.0345 30  CYS   E O     
3684 C CB    . CYS   E 30  ? 0.5800 0.3480 0.4406 -0.0910 -0.0335 -0.0236 30  CYS   E CB    
3685 S SG    . CYS   E 30  ? 0.5847 0.3212 0.4306 -0.0729 -0.0307 -0.0215 30  CYS   E SG    
3686 N N     . LYS   E 31  ? 0.7248 0.4255 0.5332 -0.0990 -0.0502 -0.0463 31  LYS   E N     
3687 C CA    . LYS   E 31  ? 0.7824 0.4445 0.5623 -0.0943 -0.0545 -0.0606 31  LYS   E CA    
3688 C C     . LYS   E 31  ? 0.7882 0.4133 0.5515 -0.1138 -0.0660 -0.0618 31  LYS   E C     
3689 O O     . LYS   E 31  ? 0.8122 0.3938 0.5551 -0.1079 -0.0703 -0.0697 31  LYS   E O     
3690 C CB    . LYS   E 31  ? 0.8054 0.4829 0.5754 -0.0897 -0.0520 -0.0709 31  LYS   E CB    
3691 C CG    . LYS   E 31  ? 0.8109 0.5121 0.5897 -0.0700 -0.0389 -0.0730 31  LYS   E CG    
3692 C CD    . LYS   E 31  ? 0.8344 0.5596 0.6048 -0.0705 -0.0343 -0.0767 31  LYS   E CD    
3693 C CE    . LYS   E 31  ? 0.8160 0.5736 0.6067 -0.0579 -0.0235 -0.0702 31  LYS   E CE    
3694 N NZ    . LYS   E 31  ? 0.8350 0.6070 0.6106 -0.0566 -0.0149 -0.0770 31  LYS   E NZ    
3695 N N     . GLU   E 32  ? 0.7823 0.4251 0.5575 -0.1366 -0.0718 -0.0551 32  GLU   E N     
3696 C CA    . GLU   E 32  ? 0.8570 0.4705 0.6204 -0.1602 -0.0816 -0.0549 32  GLU   E CA    
3697 C C     . GLU   E 32  ? 0.8451 0.4291 0.6005 -0.1664 -0.0804 -0.0450 32  GLU   E C     
3698 O O     . GLU   E 32  ? 0.8974 0.4306 0.6265 -0.1743 -0.0896 -0.0476 32  GLU   E O     
3699 C CB    . GLU   E 32  ? 0.8719 0.5222 0.6598 -0.1834 -0.0870 -0.0518 32  GLU   E CB    
3700 C CG    . GLU   E 32  ? 0.9915 0.6144 0.7646 -0.2076 -0.0997 -0.0575 32  GLU   E CG    
3701 C CD    . GLU   E 32  ? 1.0418 0.6363 0.7859 -0.2028 -0.1098 -0.0711 32  GLU   E CD    
3702 O OE1   . GLU   E 32  ? 1.0576 0.6613 0.7941 -0.1834 -0.1064 -0.0769 32  GLU   E OE1   
3703 O OE2   . GLU   E 32  ? 1.0860 0.6469 0.8119 -0.2209 -0.1203 -0.0764 32  GLU   E OE2   
3704 N N     . ASP   E 33  ? 0.7886 0.4006 0.5630 -0.1634 -0.0708 -0.0337 33  ASP   E N     
3705 C CA    . ASP   E 33  ? 0.8101 0.3937 0.5709 -0.1699 -0.0703 -0.0223 33  ASP   E CA    
3706 C C     . ASP   E 33  ? 0.8612 0.3911 0.5962 -0.1475 -0.0785 -0.0262 33  ASP   E C     
3707 O O     . ASP   E 33  ? 0.8860 0.3645 0.5950 -0.1582 -0.0888 -0.0200 33  ASP   E O     
3708 C CB    . ASP   E 33  ? 0.7665 0.3937 0.5510 -0.1710 -0.0579 -0.0119 33  ASP   E CB    
3709 C CG    . ASP   E 33  ? 0.7476 0.4278 0.5634 -0.1934 -0.0504 -0.0114 33  ASP   E CG    
3710 O OD1   . ASP   E 33  ? 0.7505 0.4317 0.5692 -0.2155 -0.0557 -0.0160 33  ASP   E OD1   
3711 O OD2   . ASP   E 33  ? 0.7294 0.4529 0.5710 -0.1874 -0.0400 -0.0085 33  ASP   E OD2   
3712 N N     . GLN   E 34  ? 0.8622 0.4018 0.6042 -0.1184 -0.0753 -0.0381 34  GLN   E N     
3713 C CA    . GLN   E 34  ? 0.9045 0.4027 0.6330 -0.0934 -0.0823 -0.0479 34  GLN   E CA    
3714 C C     . GLN   E 34  ? 0.9908 0.4313 0.6923 -0.0969 -0.0964 -0.0599 34  GLN   E C     
3715 O O     . GLN   E 34  ? 1.0411 0.4389 0.7327 -0.0779 -0.1065 -0.0671 34  GLN   E O     
3716 C CB    . GLN   E 34  ? 0.8877 0.4193 0.6335 -0.0660 -0.0716 -0.0620 34  GLN   E CB    
3717 C CG    . GLN   E 34  ? 0.8435 0.4185 0.6135 -0.0556 -0.0610 -0.0519 34  GLN   E CG    
3718 C CD    . GLN   E 34  ? 0.8347 0.4489 0.6203 -0.0379 -0.0487 -0.0640 34  GLN   E CD    
3719 O OE1   . GLN   E 34  ? 0.8674 0.4715 0.6525 -0.0176 -0.0470 -0.0811 34  GLN   E OE1   
3720 N NE2   . GLN   E 34  ? 0.8201 0.4792 0.6202 -0.0464 -0.0403 -0.0567 34  GLN   E NE2   
3721 N N     . LYS   E 35  ? 1.0257 0.4646 0.7179 -0.1184 -0.0989 -0.0642 35  LYS   E N     
3722 C CA    . LYS   E 35  ? 1.0968 0.4782 0.7610 -0.1267 -0.1134 -0.0748 35  LYS   E CA    
3723 C C     . LYS   E 35  ? 1.1334 0.4742 0.7778 -0.1573 -0.1253 -0.0589 35  LYS   E C     
3724 O O     . LYS   E 35  ? 1.2246 0.5049 0.8424 -0.1620 -0.1407 -0.0652 35  LYS   E O     
3725 C CB    . LYS   E 35  ? 1.1131 0.5072 0.7722 -0.1318 -0.1119 -0.0915 35  LYS   E CB    
3726 C CG    . LYS   E 35  ? 1.0879 0.5340 0.7627 -0.1524 -0.1064 -0.0847 35  LYS   E CG    
3727 C CD    . LYS   E 35  ? 1.1033 0.5541 0.7659 -0.1572 -0.1096 -0.1004 35  LYS   E CD    
3728 C CE    . LYS   E 35  ? 1.0527 0.5473 0.7240 -0.1424 -0.0989 -0.1067 35  LYS   E CE    
3729 N NZ    . LYS   E 35  ? 1.0766 0.5569 0.7371 -0.1161 -0.0904 -0.1240 35  LYS   E NZ    
3730 N N     . LYS   E 36  ? 1.1064 0.4774 0.7615 -0.1796 -0.1181 -0.0400 36  LYS   E N     
3731 C CA    . LYS   E 36  ? 1.1424 0.4792 0.7758 -0.2140 -0.1256 -0.0248 36  LYS   E CA    
3732 C C     . LYS   E 36  ? 1.2006 0.4671 0.8024 -0.2064 -0.1414 -0.0164 36  LYS   E C     
3733 O O     . LYS   E 36  ? 1.1893 0.4561 0.7986 -0.1764 -0.1419 -0.0167 36  LYS   E O     
3734 C CB    . LYS   E 36  ? 1.0864 0.4783 0.7409 -0.2378 -0.1103 -0.0105 36  LYS   E CB    
3735 C CG    . LYS   E 36  ? 1.0363 0.4937 0.7252 -0.2505 -0.0999 -0.0173 36  LYS   E CG    
3736 C CD    . LYS   E 36  ? 1.0040 0.5179 0.7202 -0.2679 -0.0842 -0.0076 36  LYS   E CD    
3737 C CE    . LYS   E 36  ? 0.9647 0.5425 0.7211 -0.2795 -0.0779 -0.0159 36  LYS   E CE    
3738 N NZ    . LYS   E 36  ? 0.9117 0.5484 0.7014 -0.2853 -0.0618 -0.0115 36  LYS   E NZ    
3739 N N     . SER   E 37  ? 1.2456 0.4501 0.8121 -0.2345 -0.1568 -0.0091 37  SER   E N     
3740 C CA    . SER   E 37  ? 1.3130 0.4330 0.8431 -0.2268 -0.1804 -0.0038 37  SER   E CA    
3741 C C     . SER   E 37  ? 1.3082 0.4196 0.8282 -0.2256 -0.1824 0.0164  37  SER   E C     
3742 O O     . SER   E 37  ? 1.3331 0.4019 0.8448 -0.1962 -0.1995 0.0150  37  SER   E O     
3743 C CB    . SER   E 37  ? 1.3880 0.4388 0.8785 -0.2607 -0.1983 0.0003  37  SER   E CB    
3744 O OG    . SER   E 37  ? 1.3824 0.4533 0.8645 -0.3092 -0.1880 0.0162  37  SER   E OG    
3745 N N     . GLU   E 38  ? 1.2868 0.4428 0.8109 -0.2554 -0.1651 0.0323  38  GLU   E N     
3746 C CA    . GLU   E 38  ? 1.2852 0.4455 0.8004 -0.2567 -0.1625 0.0501  38  GLU   E CA    
3747 C C     . GLU   E 38  ? 1.2172 0.4126 0.7642 -0.2111 -0.1584 0.0427  38  GLU   E C     
3748 O O     . GLU   E 38  ? 1.2562 0.4277 0.7871 -0.2042 -0.1678 0.0557  38  GLU   E O     
3749 C CB    . GLU   E 38  ? 1.2622 0.4765 0.7828 -0.2973 -0.1393 0.0617  38  GLU   E CB    
3750 C CG    . GLU   E 38  ? 1.1699 0.4794 0.7458 -0.2879 -0.1140 0.0483  38  GLU   E CG    
3751 C CD    . GLU   E 38  ? 1.1676 0.5306 0.7588 -0.3292 -0.0938 0.0504  38  GLU   E CD    
3752 O OE1   . GLU   E 38  ? 1.1763 0.5541 0.7576 -0.3515 -0.0823 0.0622  38  GLU   E OE1   
3753 O OE2   . GLU   E 38  ? 1.1818 0.5738 0.7965 -0.3393 -0.0897 0.0381  38  GLU   E OE2   
3754 N N     . TRP   E 39  ? 1.1366 0.3851 0.7242 -0.1831 -0.1458 0.0231  39  TRP   E N     
3755 C CA    . TRP   E 39  ? 1.0766 0.3659 0.6964 -0.1446 -0.1384 0.0150  39  TRP   E CA    
3756 C C     . TRP   E 39  ? 1.0994 0.3636 0.7287 -0.1057 -0.1503 -0.0064 39  TRP   E C     
3757 O O     . TRP   E 39  ? 1.0854 0.3567 0.7310 -0.0752 -0.1534 -0.0106 39  TRP   E O     
3758 C CB    . TRP   E 39  ? 0.9615 0.3369 0.6203 -0.1448 -0.1127 0.0097  39  TRP   E CB    
3759 C CG    . TRP   E 39  ? 0.9168 0.3292 0.5784 -0.1800 -0.0983 0.0233  39  TRP   E CG    
3760 C CD1   . TRP   E 39  ? 0.8916 0.3410 0.5683 -0.2044 -0.0874 0.0192  39  TRP   E CD1   
3761 C CD2   . TRP   E 39  ? 0.9110 0.3293 0.5618 -0.1958 -0.0931 0.0402  39  TRP   E CD2   
3762 N NE1   . TRP   E 39  ? 0.8699 0.3533 0.5525 -0.2323 -0.0740 0.0294  39  TRP   E NE1   
3763 C CE2   . TRP   E 39  ? 0.8882 0.3524 0.5517 -0.2294 -0.0758 0.0425  39  TRP   E CE2   
3764 C CE3   . TRP   E 39  ? 0.9279 0.3186 0.5600 -0.1854 -0.1020 0.0521  39  TRP   E CE3   
3765 C CZ2   . TRP   E 39  ? 0.8911 0.3749 0.5473 -0.2541 -0.0638 0.0545  39  TRP   E CZ2   
3766 C CZ3   . TRP   E 39  ? 0.9286 0.3336 0.5474 -0.2109 -0.0925 0.0670  39  TRP   E CZ3   
3767 C CH2   . TRP   E 39  ? 0.9101 0.3631 0.5408 -0.2450 -0.0716 0.0671  39  TRP   E CH2   
3768 N N     . LYS   E 40  ? 1.1321 0.3713 0.7538 -0.1070 -0.1558 -0.0221 40  LYS   E N     
3769 C CA    . LYS   E 40  ? 1.1341 0.3772 0.7738 -0.0733 -0.1556 -0.0493 40  LYS   E CA    
3770 C C     . LYS   E 40  ? 1.1877 0.3876 0.8302 -0.0383 -0.1746 -0.0594 40  LYS   E C     
3771 O O     . LYS   E 40  ? 1.1589 0.3899 0.8307 -0.0067 -0.1664 -0.0808 40  LYS   E O     
3772 C CB    . LYS   E 40  ? 1.1501 0.3726 0.7764 -0.0846 -0.1580 -0.0652 40  LYS   E CB    
3773 N N     . ASP   E 41  ? 1.2996 0.4299 0.9131 -0.0444 -0.2006 -0.0446 41  ASP   E N     
3774 C CA    . ASP   E 41  ? 1.3790 0.4589 0.9964 -0.0097 -0.2261 -0.0557 41  ASP   E CA    
3775 C C     . ASP   E 41  ? 1.3461 0.4596 0.9903 0.0149  -0.2252 -0.0510 41  ASP   E C     
3776 O O     . ASP   E 41  ? 1.3814 0.4711 1.0440 0.0504  -0.2436 -0.0672 41  ASP   E O     
3777 C CB    . ASP   E 41  ? 1.5057 0.4879 1.0780 -0.0246 -0.2603 -0.0425 41  ASP   E CB    
3778 C CG    . ASP   E 41  ? 1.5729 0.4914 1.1512 0.0136  -0.2920 -0.0631 41  ASP   E CG    
3779 O OD1   . ASP   E 41  ? 1.6011 0.5153 1.1935 0.0307  -0.2901 -0.0930 41  ASP   E OD1   
3780 O OD2   . ASP   E 41  ? 1.6007 0.4784 1.1725 0.0276  -0.3184 -0.0514 41  ASP   E OD2   
3781 N N     . SER   E 42  ? 1.3110 0.4817 0.9623 -0.0012 -0.2047 -0.0325 42  SER   E N     
3782 C CA    . SER   E 42  ? 1.2541 0.4452 0.9210 0.0153  -0.2080 -0.0231 42  SER   E CA    
3783 C C     . SER   E 42  ? 1.1582 0.4219 0.8758 0.0465  -0.1874 -0.0449 42  SER   E C     
3784 O O     . SER   E 42  ? 1.0804 0.3890 0.8150 0.0460  -0.1645 -0.0606 42  SER   E O     
3785 C CB    . SER   E 42  ? 1.2548 0.4614 0.8991 -0.0187 -0.1990 0.0063  42  SER   E CB    
3786 O OG    . SER   E 42  ? 1.2120 0.4960 0.8789 -0.0315 -0.1666 0.0058  42  SER   E OG    
3787 N N     . ASP   E 43  ? 1.1331 0.4043 0.8709 0.0708  -0.1975 -0.0445 43  ASP   E N     
3788 C CA    . ASP   E 43  ? 1.0855 0.4291 0.8688 0.0936  -0.1774 -0.0590 43  ASP   E CA    
3789 C C     . ASP   E 43  ? 0.9809 0.3883 0.7678 0.0709  -0.1494 -0.0429 43  ASP   E C     
3790 O O     . ASP   E 43  ? 0.9060 0.3741 0.7256 0.0831  -0.1284 -0.0560 43  ASP   E O     
3791 C CB    . ASP   E 43  ? 1.1313 0.4642 0.9371 0.1244  -0.1992 -0.0630 43  ASP   E CB    
3792 C CG    . ASP   E 43  ? 1.1897 0.5028 1.0265 0.1622  -0.2152 -0.0959 43  ASP   E CG    
3793 O OD1   . ASP   E 43  ? 1.2466 0.5100 1.0659 0.1616  -0.2269 -0.1062 43  ASP   E OD1   
3794 O OD2   . ASP   E 43  ? 1.2067 0.5566 1.0875 0.1916  -0.2153 -0.1128 43  ASP   E OD2   
3795 N N     . PHE   E 44  ? 0.9498 0.3438 0.7047 0.0385  -0.1495 -0.0165 44  PHE   E N     
3796 C CA    . PHE   E 44  ? 0.8691 0.3201 0.6305 0.0190  -0.1263 -0.0033 44  PHE   E CA    
3797 C C     . PHE   E 44  ? 0.8407 0.3158 0.6001 -0.0029 -0.1080 -0.0068 44  PHE   E C     
3798 O O     . PHE   E 44  ? 0.8810 0.3141 0.6167 -0.0168 -0.1169 -0.0073 44  PHE   E O     
3799 C CB    . PHE   E 44  ? 0.8739 0.3022 0.6040 -0.0053 -0.1343 0.0229  44  PHE   E CB    
3800 C CG    . PHE   E 44  ? 0.8836 0.2934 0.6137 0.0137  -0.1535 0.0294  44  PHE   E CG    
3801 C CD1   . PHE   E 44  ? 0.9519 0.3014 0.6746 0.0361  -0.1850 0.0243  44  PHE   E CD1   
3802 C CD2   . PHE   E 44  ? 0.8376 0.2857 0.5738 0.0087  -0.1437 0.0406  44  PHE   E CD2   
3803 C CE1   . PHE   E 44  ? 0.9673 0.2990 0.6921 0.0543  -0.2072 0.0301  44  PHE   E CE1   
3804 C CE2   . PHE   E 44  ? 0.8619 0.2930 0.5974 0.0254  -0.1635 0.0464  44  PHE   E CE2   
3805 C CZ    . PHE   E 44  ? 0.9324 0.3042 0.6613 0.0476  -0.1966 0.0423  44  PHE   E CZ    
3806 N N     . LEU   E 45  ? 0.7773 0.3157 0.5599 -0.0073 -0.0856 -0.0078 45  LEU   E N     
3807 C CA    . LEU   E 45  ? 0.7525 0.3172 0.5358 -0.0292 -0.0717 -0.0085 45  LEU   E CA    
3808 C C     . LEU   E 45  ? 0.7584 0.3079 0.5188 -0.0635 -0.0730 0.0089  45  LEU   E C     
3809 O O     . LEU   E 45  ? 0.7692 0.3054 0.5157 -0.0715 -0.0775 0.0233  45  LEU   E O     
3810 C CB    . LEU   E 45  ? 0.7258 0.3563 0.5391 -0.0241 -0.0528 -0.0120 45  LEU   E CB    
3811 C CG    . LEU   E 45  ? 0.7354 0.3893 0.5659 -0.0039 -0.0450 -0.0311 45  LEU   E CG    
3812 C CD1   . LEU   E 45  ? 0.7705 0.4105 0.6104 0.0251  -0.0508 -0.0454 45  LEU   E CD1   
3813 C CD2   . LEU   E 45  ? 0.6847 0.3949 0.5370 -0.0058 -0.0299 -0.0283 45  LEU   E CD2   
3814 N N     . PRO   E 46  ? 0.7360 0.2936 0.4936 -0.0865 -0.0674 0.0073  46  PRO   E N     
3815 C CA    . PRO   E 46  ? 0.7484 0.3026 0.4910 -0.1221 -0.0646 0.0200  46  PRO   E CA    
3816 C C     . PRO   E 46  ? 0.7123 0.3084 0.4671 -0.1328 -0.0512 0.0300  46  PRO   E C     
3817 O O     . PRO   E 46  ? 0.6914 0.3398 0.4781 -0.1203 -0.0394 0.0245  46  PRO   E O     
3818 C CB    . PRO   E 46  ? 0.7348 0.3129 0.4900 -0.1373 -0.0587 0.0112  46  PRO   E CB    
3819 C CG    . PRO   E 46  ? 0.7440 0.3074 0.5003 -0.1135 -0.0651 -0.0045 46  PRO   E CG    
3820 C CD    . PRO   E 46  ? 0.7203 0.2897 0.4875 -0.0811 -0.0644 -0.0084 46  PRO   E CD    
3821 N N     . ASN   E 47  ? 0.7330 0.3047 0.4600 -0.1573 -0.0531 0.0439  47  ASN   E N     
3822 C CA    . ASN   E 47  ? 0.7039 0.3150 0.4378 -0.1757 -0.0376 0.0506  47  ASN   E CA    
3823 C C     . ASN   E 47  ? 0.6854 0.3400 0.4407 -0.2036 -0.0223 0.0440  47  ASN   E C     
3824 O O     . ASN   E 47  ? 0.7063 0.3580 0.4442 -0.2391 -0.0152 0.0497  47  ASN   E O     
3825 C CB    . ASN   E 47  ? 0.7620 0.3264 0.4509 -0.1936 -0.0459 0.0673  47  ASN   E CB    
3826 C CG    . ASN   E 47  ? 0.7888 0.3121 0.4630 -0.1635 -0.0655 0.0725  47  ASN   E CG    
3827 O OD1   . ASN   E 47  ? 0.8493 0.3068 0.4918 -0.1611 -0.0875 0.0779  47  ASN   E OD1   
3828 N ND2   . ASN   E 47  ? 0.7558 0.3154 0.4540 -0.1406 -0.0599 0.0701  47  ASN   E ND2   
3829 N N     . THR   E 48  ? 0.6379 0.3352 0.4321 -0.1882 -0.0177 0.0311  48  THR   E N     
3830 C CA    . THR   E 48  ? 0.6232 0.3661 0.4484 -0.2067 -0.0084 0.0216  48  THR   E CA    
3831 C C     . THR   E 48  ? 0.5766 0.3821 0.4454 -0.1917 0.0025  0.0141  48  THR   E C     
3832 O O     . THR   E 48  ? 0.5573 0.3675 0.4322 -0.1638 0.0009  0.0148  48  THR   E O     
3833 C CB    . THR   E 48  ? 0.6321 0.3610 0.4602 -0.2022 -0.0195 0.0133  48  THR   E CB    
3834 O OG1   . THR   E 48  ? 0.6001 0.3324 0.4380 -0.1687 -0.0246 0.0077  48  THR   E OG1   
3835 C CG2   . THR   E 48  ? 0.6909 0.3556 0.4769 -0.2183 -0.0315 0.0190  48  THR   E CG2   
3836 N N     . GLN   E 49  ? 0.5685 0.4219 0.4711 -0.2097 0.0117  0.0047  49  GLN   E N     
3837 C CA    . GLN   E 49  ? 0.5113 0.4242 0.4615 -0.1977 0.0187  -0.0055 49  GLN   E CA    
3838 C C     . GLN   E 49  ? 0.4828 0.3958 0.4444 -0.1671 0.0067  -0.0079 49  GLN   E C     
3839 O O     . GLN   E 49  ? 0.4662 0.3965 0.4408 -0.1456 0.0085  -0.0075 49  GLN   E O     
3840 C CB    . GLN   E 49  ? 0.5164 0.4733 0.5018 -0.2243 0.0262  -0.0183 49  GLN   E CB    
3841 C CG    . GLN   E 49  ? 0.5518 0.5089 0.5200 -0.2610 0.0417  -0.0170 49  GLN   E CG    
3842 C CD    . GLN   E 49  ? 0.6116 0.5379 0.5544 -0.2932 0.0385  -0.0143 49  GLN   E CD    
3843 O OE1   . GLN   E 49  ? 0.6456 0.5125 0.5473 -0.2915 0.0247  -0.0033 49  GLN   E OE1   
3844 N NE2   . GLN   E 49  ? 0.6100 0.5765 0.5767 -0.3262 0.0527  -0.0259 49  GLN   E NE2   
3845 N N     . ALA   E 50  ? 0.5000 0.3891 0.4506 -0.1672 -0.0053 -0.0099 50  ALA   E N     
3846 C CA    . ALA   E 50  ? 0.4806 0.3688 0.4353 -0.1452 -0.0158 -0.0134 50  ALA   E CA    
3847 C C     . ALA   E 50  ? 0.4642 0.3321 0.3995 -0.1209 -0.0142 -0.0080 50  ALA   E C     
3848 O O     . ALA   E 50  ? 0.4485 0.3407 0.4009 -0.1047 -0.0131 -0.0090 50  ALA   E O     
3849 C CB    . ALA   E 50  ? 0.5086 0.3700 0.4469 -0.1526 -0.0276 -0.0173 50  ALA   E CB    
3850 N N     . CYS   E 51  ? 0.4926 0.3182 0.3958 -0.1192 -0.0149 -0.0027 51  CYS   E N     
3851 C CA    . CYS   E 51  ? 0.5007 0.3107 0.3922 -0.0949 -0.0147 -0.0008 51  CYS   E CA    
3852 C C     . CYS   E 51  ? 0.4694 0.3059 0.3758 -0.0868 -0.0063 0.0045  51  CYS   E C     
3853 O O     . CYS   E 51  ? 0.4503 0.2935 0.3614 -0.0663 -0.0051 0.0034  51  CYS   E O     
3854 C CB    . CYS   E 51  ? 0.5514 0.3087 0.4105 -0.0928 -0.0217 0.0023  51  CYS   E CB    
3855 S SG    . CYS   E 51  ? 0.6171 0.3344 0.4545 -0.0976 -0.0326 -0.0067 51  CYS   E SG    
3856 N N     . TYR   E 52  ? 0.4674 0.3194 0.3799 -0.1049 0.0006  0.0086  52  TYR   E N     
3857 C CA    . TYR   E 52  ? 0.4542 0.3282 0.3761 -0.1003 0.0088  0.0124  52  TYR   E CA    
3858 C C     . TYR   E 52  ? 0.4010 0.3208 0.3592 -0.0887 0.0126  0.0058  52  TYR   E C     
3859 O O     . TYR   E 52  ? 0.3742 0.3010 0.3368 -0.0710 0.0136  0.0073  52  TYR   E O     
3860 C CB    . TYR   E 52  ? 0.4630 0.3411 0.3772 -0.1275 0.0172  0.0156  52  TYR   E CB    
3861 C CG    . TYR   E 52  ? 0.4491 0.3468 0.3659 -0.1279 0.0269  0.0184  52  TYR   E CG    
3862 C CD1   . TYR   E 52  ? 0.4380 0.3263 0.3470 -0.1066 0.0232  0.0239  52  TYR   E CD1   
3863 C CD2   . TYR   E 52  ? 0.4421 0.3712 0.3708 -0.1515 0.0405  0.0131  52  TYR   E CD2   
3864 C CE1   . TYR   E 52  ? 0.4258 0.3306 0.3343 -0.1097 0.0311  0.0259  52  TYR   E CE1   
3865 C CE2   . TYR   E 52  ? 0.4356 0.3834 0.3641 -0.1543 0.0508  0.0130  52  TYR   E CE2   
3866 C CZ    . TYR   E 52  ? 0.4282 0.3606 0.3433 -0.1340 0.0452  0.0207  52  TYR   E CZ    
3867 O OH    . TYR   E 52  ? 0.4244 0.3714 0.3335 -0.1412 0.0547  0.0206  52  TYR   E OH    
3868 N N     . ILE   E 53  ? 0.3984 0.3459 0.3825 -0.0988 0.0120  -0.0019 53  ILE   E N     
3869 C CA    . ILE   E 53  ? 0.3715 0.3551 0.3898 -0.0883 0.0093  -0.0084 53  ILE   E CA    
3870 C C     . ILE   E 53  ? 0.3496 0.3185 0.3565 -0.0686 0.0016  -0.0057 53  ILE   E C     
3871 O O     . ILE   E 53  ? 0.3036 0.2876 0.3216 -0.0555 0.0026  -0.0049 53  ILE   E O     
3872 C CB    . ILE   E 53  ? 0.3967 0.4060 0.4448 -0.1020 0.0041  -0.0182 53  ILE   E CB    
3873 C CG1   . ILE   E 53  ? 0.4193 0.4544 0.4847 -0.1242 0.0170  -0.0249 53  ILE   E CG1   
3874 C CG2   . ILE   E 53  ? 0.3855 0.4220 0.4662 -0.0882 -0.0063 -0.0238 53  ILE   E CG2   
3875 C CD1   . ILE   E 53  ? 0.4370 0.4951 0.5296 -0.1432 0.0140  -0.0361 53  ILE   E CD1   
3876 N N     . GLY   E 54  ? 0.3668 0.3058 0.3495 -0.0687 -0.0044 -0.0056 54  GLY   E N     
3877 C CA    . GLY   E 54  ? 0.3755 0.3012 0.3430 -0.0544 -0.0079 -0.0063 54  GLY   E CA    
3878 C C     . GLY   E 54  ? 0.3554 0.2791 0.3176 -0.0387 -0.0007 -0.0035 54  GLY   E C     
3879 O O     . GLY   E 54  ? 0.3483 0.2852 0.3158 -0.0289 0.0002  -0.0040 54  GLY   E O     
3880 N N     . SER   E 55  ? 0.3630 0.2697 0.3145 -0.0386 0.0027  -0.0001 55  SER   E N     
3881 C CA    . SER   E 55  ? 0.3620 0.2678 0.3124 -0.0244 0.0064  0.0026  55  SER   E CA    
3882 C C     . SER   E 55  ? 0.3114 0.2511 0.2842 -0.0207 0.0113  0.0049  55  SER   E C     
3883 O O     . SER   E 55  ? 0.2910 0.2404 0.2692 -0.0080 0.0132  0.0038  55  SER   E O     
3884 C CB    . SER   E 55  ? 0.4051 0.2805 0.3365 -0.0276 0.0035  0.0078  55  SER   E CB    
3885 O OG    . SER   E 55  ? 0.4105 0.2890 0.3438 -0.0167 0.0042  0.0118  55  SER   E OG    
3886 N N     . ILE   E 56  ? 0.2888 0.2479 0.2764 -0.0327 0.0140  0.0058  56  ILE   E N     
3887 C CA    . ILE   E 56  ? 0.2620 0.2513 0.2721 -0.0291 0.0180  0.0051  56  ILE   E CA    
3888 C C     . ILE   E 56  ? 0.2497 0.2542 0.2749 -0.0205 0.0129  0.0026  56  ILE   E C     
3889 O O     . ILE   E 56  ? 0.2314 0.2465 0.2635 -0.0109 0.0143  0.0039  56  ILE   E O     
3890 C CB    . ILE   E 56  ? 0.2477 0.2583 0.2744 -0.0443 0.0235  0.0011  56  ILE   E CB    
3891 C CG1   . ILE   E 56  ? 0.2696 0.2627 0.2727 -0.0581 0.0297  0.0057  56  ILE   E CG1   
3892 C CG2   . ILE   E 56  ? 0.2162 0.2583 0.2700 -0.0382 0.0266  -0.0037 56  ILE   E CG2   
3893 C CD1   . ILE   E 56  ? 0.2727 0.2859 0.2877 -0.0803 0.0378  -0.0009 56  ILE   E CD1   
3894 N N     . LEU   E 57  ? 0.2478 0.2511 0.2760 -0.0263 0.0051  -0.0003 57  LEU   E N     
3895 C CA    . LEU   E 57  ? 0.2490 0.2583 0.2833 -0.0222 -0.0042 -0.0006 57  LEU   E CA    
3896 C C     . LEU   E 57  ? 0.2537 0.2511 0.2672 -0.0141 -0.0012 0.0021  57  LEU   E C     
3897 O O     . LEU   E 57  ? 0.2561 0.2627 0.2751 -0.0099 -0.0031 0.0044  57  LEU   E O     
3898 C CB    . LEU   E 57  ? 0.2664 0.2703 0.3009 -0.0311 -0.0162 -0.0034 57  LEU   E CB    
3899 C CG    . LEU   E 57  ? 0.2705 0.2957 0.3362 -0.0396 -0.0204 -0.0098 57  LEU   E CG    
3900 C CD1   . LEU   E 57  ? 0.2865 0.3031 0.3494 -0.0481 -0.0341 -0.0125 57  LEU   E CD1   
3901 C CD2   . LEU   E 57  ? 0.2556 0.3076 0.3554 -0.0329 -0.0246 -0.0138 57  LEU   E CD2   
3902 N N     . LEU   E 58  ? 0.2652 0.2436 0.2574 -0.0124 0.0040  0.0003  58  LEU   E N     
3903 C CA    . LEU   E 58  ? 0.2779 0.2501 0.2545 -0.0058 0.0093  -0.0025 58  LEU   E CA    
3904 C C     . LEU   E 58  ? 0.2644 0.2499 0.2521 0.0045  0.0167  -0.0014 58  LEU   E C     
3905 O O     . LEU   E 58  ? 0.2746 0.2673 0.2590 0.0072  0.0211  -0.0036 58  LEU   E O     
3906 C CB    . LEU   E 58  ? 0.3086 0.2575 0.2654 -0.0049 0.0116  -0.0093 58  LEU   E CB    
3907 C CG    . LEU   E 58  ? 0.3218 0.2686 0.2678 0.0034  0.0203  -0.0184 58  LEU   E CG    
3908 C CD1   . LEU   E 58  ? 0.3239 0.2782 0.2565 -0.0051 0.0219  -0.0196 58  LEU   E CD1   
3909 C CD2   . LEU   E 58  ? 0.3456 0.2678 0.2780 0.0071  0.0204  -0.0278 58  LEU   E CD2   
3910 N N     . THR   E 59  ? 0.2591 0.2470 0.2568 0.0080  0.0180  0.0015  59  THR   E N     
3911 C CA    . THR   E 59  ? 0.2536 0.2502 0.2591 0.0180  0.0221  0.0021  59  THR   E CA    
3912 C C     . THR   E 59  ? 0.2269 0.2454 0.2493 0.0171  0.0221  0.0057  59  THR   E C     
3913 O O     . THR   E 59  ? 0.2255 0.2528 0.2551 0.0237  0.0244  0.0065  59  THR   E O     
3914 C CB    . THR   E 59  ? 0.2662 0.2458 0.2648 0.0206  0.0203  0.0040  59  THR   E CB    
3915 O OG1   . THR   E 59  ? 0.2732 0.2518 0.2712 0.0086  0.0193  0.0085  59  THR   E OG1   
3916 C CG2   . THR   E 59  ? 0.2949 0.2489 0.2786 0.0254  0.0176  -0.0013 59  THR   E CG2   
3917 N N     . THR   E 60  ? 0.2127 0.2385 0.2432 0.0099  0.0171  0.0068  60  THR   E N     
3918 C CA    . THR   E 60  ? 0.2044 0.2467 0.2526 0.0105  0.0141  0.0080  60  THR   E CA    
3919 C C     . THR   E 60  ? 0.1946 0.2388 0.2376 0.0119  0.0136  0.0099  60  THR   E C     
3920 O O     . THR   E 60  ? 0.2156 0.2502 0.2438 0.0062  0.0104  0.0107  60  THR   E O     
3921 C CB    . THR   E 60  ? 0.2114 0.2588 0.2741 0.0045  0.0050  0.0060  60  THR   E CB    
3922 O OG1   . THR   E 60  ? 0.2133 0.2625 0.2791 0.0001  0.0103  0.0030  60  THR   E OG1   
3923 C CG2   . THR   E 60  ? 0.2071 0.2681 0.2911 0.0076  -0.0011 0.0046  60  THR   E CG2   
3924 N N     . ALA   E 61  ? 0.1765 0.2320 0.2281 0.0165  0.0170  0.0105  61  ALA   E N     
3925 C CA    . ALA   E 61  ? 0.1927 0.2520 0.2388 0.0144  0.0192  0.0116  61  ALA   E CA    
3926 C C     . ALA   E 61  ? 0.2040 0.2588 0.2509 0.0072  0.0080  0.0164  61  ALA   E C     
3927 O O     . ALA   E 61  ? 0.2019 0.2632 0.2614 0.0087  0.0044  0.0175  61  ALA   E O     
3928 C CB    . ALA   E 61  ? 0.1797 0.2526 0.2366 0.0213  0.0251  0.0097  61  ALA   E CB    
3929 N N     . ARG   E 62  ? 0.2294 0.2696 0.2624 -0.0002 -0.0006 0.0189  62  ARG   E N     
3930 C CA    . ARG   E 62  ? 0.2809 0.3089 0.3129 -0.0062 -0.0181 0.0243  62  ARG   E CA    
3931 C C     . ARG   E 62  ? 0.3191 0.3376 0.3310 -0.0172 -0.0203 0.0309  62  ARG   E C     
3932 O O     . ARG   E 62  ? 0.3431 0.3468 0.3545 -0.0213 -0.0381 0.0367  62  ARG   E O     
3933 C CB    . ARG   E 62  ? 0.3120 0.3241 0.3320 -0.0119 -0.0305 0.0257  62  ARG   E CB    
3934 C CG    . ARG   E 62  ? 0.3343 0.3568 0.3790 -0.0047 -0.0320 0.0191  62  ARG   E CG    
3935 C CD    . ARG   E 62  ? 0.3875 0.3990 0.4301 -0.0095 -0.0473 0.0186  62  ARG   E CD    
3936 N NE    . ARG   E 62  ? 0.3897 0.4199 0.4679 -0.0035 -0.0487 0.0100  62  ARG   E NE    
3937 C CZ    . ARG   E 62  ? 0.4247 0.4649 0.5357 0.0016  -0.0633 0.0044  62  ARG   E CZ    
3938 N NH1   . ARG   E 62  ? 0.4206 0.4480 0.5327 0.0035  -0.0814 0.0087  62  ARG   E NH1   
3939 N NH2   . ARG   E 62  ? 0.4533 0.5163 0.5972 0.0042  -0.0600 -0.0072 62  ARG   E NH2   
3940 N N     . LYS   E 63  ? 0.3309 0.3552 0.3246 -0.0239 -0.0042 0.0291  63  LYS   E N     
3941 C CA    . LYS   E 63  ? 0.3499 0.3698 0.3229 -0.0392 -0.0014 0.0336  63  LYS   E CA    
3942 C C     . LYS   E 63  ? 0.3044 0.3439 0.3008 -0.0330 0.0055  0.0311  63  LYS   E C     
3943 O O     . LYS   E 63  ? 0.2806 0.3419 0.2919 -0.0238 0.0203  0.0228  63  LYS   E O     
3944 C CB    . LYS   E 63  ? 0.3852 0.4090 0.3320 -0.0506 0.0155  0.0278  63  LYS   E CB    
3945 C CG    . LYS   E 63  ? 0.4357 0.4574 0.3561 -0.0729 0.0221  0.0309  63  LYS   E CG    
3946 C CD    . LYS   E 63  ? 0.4829 0.5145 0.3782 -0.0871 0.0430  0.0205  63  LYS   E CD    
3947 C CE    . LYS   E 63  ? 0.5228 0.5589 0.3946 -0.1130 0.0536  0.0218  63  LYS   E CE    
3948 N NZ    . LYS   E 63  ? 0.5436 0.6074 0.4090 -0.1235 0.0815  0.0040  63  LYS   E NZ    
3949 N N     . THR   E 64  ? 0.3253 0.3544 0.3254 -0.0370 -0.0080 0.0378  64  THR   E N     
3950 C CA    . THR   E 64  ? 0.2999 0.3434 0.3172 -0.0352 -0.0038 0.0363  64  THR   E CA    
3951 C C     . THR   E 64  ? 0.3164 0.3511 0.3104 -0.0570 -0.0032 0.0426  64  THR   E C     
3952 O O     . THR   E 64  ? 0.3413 0.3457 0.3134 -0.0691 -0.0206 0.0527  64  THR   E O     
3953 C CB    . THR   E 64  ? 0.3119 0.3489 0.3522 -0.0235 -0.0196 0.0363  64  THR   E CB    
3954 O OG1   . THR   E 64  ? 0.2899 0.3384 0.3477 -0.0087 -0.0158 0.0295  64  THR   E OG1   
3955 C CG2   . THR   E 64  ? 0.3147 0.3646 0.3726 -0.0205 -0.0170 0.0333  64  THR   E CG2   
3956 N N     . THR   E 65  ? 0.3161 0.3767 0.3183 -0.0617 0.0138  0.0365  65  THR   E N     
3957 C CA    . THR   E 65  ? 0.3396 0.4008 0.3265 -0.0844 0.0185  0.0398  65  THR   E CA    
3958 C C     . THR   E 65  ? 0.3172 0.3956 0.3328 -0.0780 0.0181  0.0365  65  THR   E C     
3959 O O     . THR   E 65  ? 0.2831 0.3904 0.3269 -0.0617 0.0279  0.0263  65  THR   E O     
3960 C CB    . THR   E 65  ? 0.3490 0.4360 0.3271 -0.0963 0.0426  0.0298  65  THR   E CB    
3961 O OG1   . THR   E 65  ? 0.3768 0.4480 0.3300 -0.0985 0.0426  0.0307  65  THR   E OG1   
3962 C CG2   . THR   E 65  ? 0.3990 0.4883 0.3540 -0.1275 0.0516  0.0320  65  THR   E CG2   
3963 N N     . TYR   E 66  ? 0.3487 0.4070 0.3540 -0.0925 0.0056  0.0450  66  TYR   E N     
3964 C CA    . TYR   E 66  ? 0.3479 0.4188 0.3754 -0.0909 0.0041  0.0419  66  TYR   E CA    
3965 C C     . TYR   E 66  ? 0.3625 0.4509 0.3812 -0.1168 0.0184  0.0404  66  TYR   E C     
3966 O O     . TYR   E 66  ? 0.3881 0.4602 0.3722 -0.1423 0.0210  0.0475  66  TYR   E O     
3967 C CB    . TYR   E 66  ? 0.3844 0.4190 0.4088 -0.0891 -0.0209 0.0499  66  TYR   E CB    
3968 C CG    . TYR   E 66  ? 0.3616 0.3883 0.4033 -0.0639 -0.0323 0.0464  66  TYR   E CG    
3969 C CD1   . TYR   E 66  ? 0.3210 0.3733 0.3923 -0.0431 -0.0251 0.0356  66  TYR   E CD1   
3970 C CD2   . TYR   E 66  ? 0.3948 0.3889 0.4229 -0.0631 -0.0509 0.0530  66  TYR   E CD2   
3971 C CE1   . TYR   E 66  ? 0.3191 0.3680 0.4052 -0.0249 -0.0322 0.0305  66  TYR   E CE1   
3972 C CE2   . TYR   E 66  ? 0.3807 0.3746 0.4312 -0.0415 -0.0598 0.0464  66  TYR   E CE2   
3973 C CZ    . TYR   E 66  ? 0.3378 0.3607 0.4171 -0.0239 -0.0483 0.0346  66  TYR   E CZ    
3974 O OH    . TYR   E 66  ? 0.3533 0.3804 0.4533 -0.0071 -0.0529 0.0262  66  TYR   E OH    
3975 N N     . SER   E 67  ? 0.3399 0.4622 0.3890 -0.1121 0.0273  0.0306  67  SER   E N     
3976 C CA    . SER   E 67  ? 0.3690 0.5118 0.4177 -0.1379 0.0390  0.0274  67  SER   E CA    
3977 C C     . SER   E 67  ? 0.3547 0.5143 0.4340 -0.1316 0.0334  0.0222  67  SER   E C     
3978 O O     . SER   E 67  ? 0.3183 0.4640 0.4104 -0.1098 0.0181  0.0234  67  SER   E O     
3979 C CB    . SER   E 67  ? 0.3487 0.5322 0.4057 -0.1436 0.0643  0.0135  67  SER   E CB    
3980 O OG    . SER   E 67  ? 0.2945 0.5102 0.3904 -0.1142 0.0693  -0.0001 67  SER   E OG    
3981 O OXT   . SER   E 67  ? 0.3811 0.5656 0.4676 -0.1524 0.0444  0.0169  67  SER   E OXT   
3982 N N     . SER   F 4   ? 0.9024 1.0447 0.7844 -0.1606 -0.1828 0.1541  4   SER   F N     
3983 C CA    . SER   F 4   ? 0.8526 0.9764 0.7451 -0.1405 -0.1547 0.1403  4   SER   F CA    
3984 C C     . SER   F 4   ? 0.8487 0.9883 0.7874 -0.1336 -0.1465 0.1369  4   SER   F C     
3985 O O     . SER   F 4   ? 0.8887 1.0502 0.8478 -0.1456 -0.1601 0.1428  4   SER   F O     
3986 C CB    . SER   F 4   ? 0.8447 0.9245 0.6828 -0.1446 -0.1422 0.1184  4   SER   F CB    
3987 O OG    . SER   F 4   ? 0.7747 0.8409 0.6226 -0.1250 -0.1172 0.1085  4   SER   F OG    
3988 N N     . VAL   F 5   ? 0.8347 0.9635 0.7887 -0.1152 -0.1239 0.1272  5   VAL   F N     
3989 C CA    . VAL   F 5   ? 0.7638 0.9071 0.7602 -0.1054 -0.1136 0.1251  5   VAL   F CA    
3990 C C     . VAL   F 5   ? 0.6940 0.8216 0.6748 -0.1191 -0.1146 0.1112  5   VAL   F C     
3991 O O     . VAL   F 5   ? 0.7259 0.8192 0.6637 -0.1256 -0.1114 0.0960  5   VAL   F O     
3992 C CB    . VAL   F 5   ? 0.7747 0.9076 0.7849 -0.0839 -0.0913 0.1181  5   VAL   F CB    
3993 C CG1   . VAL   F 5   ? 0.7752 0.9237 0.8267 -0.0736 -0.0812 0.1169  5   VAL   F CG1   
3994 C CG2   . VAL   F 5   ? 0.7800 0.9188 0.7970 -0.0726 -0.0894 0.1305  5   VAL   F CG2   
3995 N N     . ASP   F 6   ? 0.6060 0.7581 0.6211 -0.1236 -0.1186 0.1171  6   ASP   F N     
3996 C CA    . ASP   F 6   ? 0.5802 0.7194 0.5860 -0.1372 -0.1192 0.1070  6   ASP   F CA    
3997 C C     . ASP   F 6   ? 0.5040 0.6494 0.5406 -0.1254 -0.1029 0.1033  6   ASP   F C     
3998 O O     . ASP   F 6   ? 0.5132 0.6427 0.5381 -0.1357 -0.1018 0.0950  6   ASP   F O     
3999 C CB    . ASP   F 6   ? 0.6287 0.7881 0.6379 -0.1612 -0.1412 0.1170  6   ASP   F CB    
4000 C CG    . ASP   F 6   ? 0.7305 0.8714 0.6932 -0.1804 -0.1594 0.1147  6   ASP   F CG    
4001 O OD1   . ASP   F 6   ? 0.7012 0.8172 0.6293 -0.1735 -0.1545 0.1079  6   ASP   F OD1   
4002 O OD2   . ASP   F 6   ? 0.8489 1.0013 0.8100 -0.2036 -0.1783 0.1200  6   ASP   F OD2   
4003 N N     . ASP   F 7   ? 0.4197 0.5818 0.4893 -0.1048 -0.0898 0.1079  7   ASP   F N     
4004 C CA    . ASP   F 7   ? 0.3819 0.5484 0.4755 -0.0946 -0.0746 0.1038  7   ASP   F CA    
4005 C C     . ASP   F 7   ? 0.3284 0.4659 0.4054 -0.0790 -0.0584 0.0894  7   ASP   F C     
4006 O O     . ASP   F 7   ? 0.3334 0.4597 0.3970 -0.0714 -0.0562 0.0872  7   ASP   F O     
4007 C CB    . ASP   F 7   ? 0.4010 0.6080 0.5438 -0.0854 -0.0721 0.1185  7   ASP   F CB    
4008 C CG    . ASP   F 7   ? 0.4504 0.6911 0.6156 -0.1020 -0.0875 0.1329  7   ASP   F CG    
4009 O OD1   . ASP   F 7   ? 0.5506 0.7960 0.7214 -0.1137 -0.0864 0.1313  7   ASP   F OD1   
4010 O OD2   . ASP   F 7   ? 0.4658 0.7290 0.6434 -0.1039 -0.1011 0.1466  7   ASP   F OD2   
4011 N N     . TYR   F 8   ? 0.2844 0.4109 0.3622 -0.0756 -0.0479 0.0806  8   TYR   F N     
4012 C CA    . TYR   F 8   ? 0.2517 0.3598 0.3245 -0.0597 -0.0332 0.0694  8   TYR   F CA    
4013 C C     . TYR   F 8   ? 0.2182 0.3460 0.3216 -0.0435 -0.0251 0.0755  8   TYR   F C     
4014 O O     . TYR   F 8   ? 0.1849 0.3394 0.3191 -0.0413 -0.0243 0.0854  8   TYR   F O     
4015 C CB    . TYR   F 8   ? 0.2314 0.3285 0.3013 -0.0604 -0.0261 0.0623  8   TYR   F CB    
4016 C CG    . TYR   F 8   ? 0.2133 0.2975 0.2830 -0.0443 -0.0129 0.0526  8   TYR   F CG    
4017 C CD1   . TYR   F 8   ? 0.2197 0.2829 0.2707 -0.0366 -0.0094 0.0430  8   TYR   F CD1   
4018 C CD2   . TYR   F 8   ? 0.1991 0.2946 0.2883 -0.0370 -0.0036 0.0533  8   TYR   F CD2   
4019 C CE1   . TYR   F 8   ? 0.2019 0.2574 0.2561 -0.0234 0.0006  0.0351  8   TYR   F CE1   
4020 C CE2   . TYR   F 8   ? 0.1893 0.2731 0.2759 -0.0243 0.0062  0.0442  8   TYR   F CE2   
4021 C CZ    . TYR   F 8   ? 0.1863 0.2513 0.2571 -0.0179 0.0072  0.0355  8   TYR   F CZ    
4022 O OH    . TYR   F 8   ? 0.1916 0.2493 0.2636 -0.0068 0.0149  0.0276  8   TYR   F OH    
4023 N N     . ASN   F 9   ? 0.1993 0.3124 0.2937 -0.0327 -0.0183 0.0692  9   ASN   F N     
4024 C CA    . ASN   F 9   ? 0.1744 0.2963 0.2918 -0.0181 -0.0095 0.0721  9   ASN   F CA    
4025 C C     . ASN   F 9   ? 0.1660 0.2703 0.2773 -0.0091 0.0022  0.0584  9   ASN   F C     
4026 O O     . ASN   F 9   ? 0.1799 0.2675 0.2741 -0.0069 0.0047  0.0511  9   ASN   F O     
4027 C CB    . ASN   F 9   ? 0.1757 0.2996 0.2910 -0.0165 -0.0143 0.0803  9   ASN   F CB    
4028 C CG    . ASN   F 9   ? 0.1538 0.2863 0.2960 -0.0024 -0.0065 0.0861  9   ASN   F CG    
4029 O OD1   . ASN   F 9   ? 0.1362 0.2673 0.2926 0.0068  0.0043  0.0796  9   ASN   F OD1   
4030 N ND2   . ASN   F 9   ? 0.1552 0.2933 0.3017 -0.0007 -0.0116 0.0979  9   ASN   F ND2   
4031 N N     . PRO   F 10  ? 0.1552 0.2648 0.2814 -0.0032 0.0102  0.0554  10  PRO   F N     
4032 C CA    . PRO   F 10  ? 0.1481 0.2431 0.2692 0.0052  0.0193  0.0435  10  PRO   F CA    
4033 C C     . PRO   F 10  ? 0.1490 0.2404 0.2794 0.0151  0.0255  0.0412  10  PRO   F C     
4034 O O     . PRO   F 10  ? 0.1676 0.2470 0.2918 0.0195  0.0305  0.0309  10  PRO   F O     
4035 C CB    . PRO   F 10  ? 0.1408 0.2436 0.2726 0.0071  0.0254  0.0426  10  PRO   F CB    
4036 C CG    . PRO   F 10  ? 0.1382 0.2658 0.2942 0.0058  0.0239  0.0555  10  PRO   F CG    
4037 C CD    . PRO   F 10  ? 0.1455 0.2772 0.2950 -0.0040 0.0114  0.0636  10  PRO   F CD    
4038 N N     . ALA   F 11  ? 0.1449 0.2453 0.2891 0.0177  0.0241  0.0510  11  ALA   F N     
4039 C CA    . ALA   F 11  ? 0.1553 0.2473 0.3035 0.0241  0.0291  0.0497  11  ALA   F CA    
4040 C C     . ALA   F 11  ? 0.1773 0.2557 0.3051 0.0205  0.0287  0.0430  11  ALA   F C     
4041 O O     . ALA   F 11  ? 0.1741 0.2450 0.3055 0.0247  0.0348  0.0379  11  ALA   F O     
4042 C CB    . ALA   F 11  ? 0.1669 0.2678 0.3300 0.0270  0.0268  0.0633  11  ALA   F CB    
4043 N N     . PHE   F 12  ? 0.1851 0.2602 0.2924 0.0125  0.0221  0.0431  12  PHE   F N     
4044 C CA    . PHE   F 12  ? 0.1968 0.2591 0.2838 0.0103  0.0237  0.0365  12  PHE   F CA    
4045 C C     . PHE   F 12  ? 0.1819 0.2344 0.2589 0.0115  0.0254  0.0247  12  PHE   F C     
4046 O O     . PHE   F 12  ? 0.1718 0.2240 0.2451 0.0082  0.0214  0.0240  12  PHE   F O     
4047 C CB    . PHE   F 12  ? 0.2327 0.2934 0.2998 0.0017  0.0163  0.0429  12  PHE   F CB    
4048 C CG    . PHE   F 12  ? 0.2608 0.3303 0.3350 0.0010  0.0134  0.0565  12  PHE   F CG    
4049 C CD1   . PHE   F 12  ? 0.2853 0.3488 0.3544 0.0028  0.0194  0.0582  12  PHE   F CD1   
4050 C CD2   . PHE   F 12  ? 0.2800 0.3647 0.3675 -0.0012 0.0048  0.0690  12  PHE   F CD2   
4051 C CE1   . PHE   F 12  ? 0.2927 0.3613 0.3653 0.0020  0.0161  0.0725  12  PHE   F CE1   
4052 C CE2   . PHE   F 12  ? 0.2741 0.3663 0.3682 -0.0005 0.0005  0.0834  12  PHE   F CE2   
4053 C CZ    . PHE   F 12  ? 0.2981 0.3802 0.3828 0.0010  0.0060  0.0852  12  PHE   F CZ    
4054 N N     . ASP   F 13  ? 0.1671 0.2127 0.2415 0.0161  0.0312  0.0166  13  ASP   F N     
4055 C CA    . ASP   F 13  ? 0.1707 0.2059 0.2336 0.0185  0.0318  0.0069  13  ASP   F CA    
4056 C C     . ASP   F 13  ? 0.1877 0.2104 0.2253 0.0125  0.0276  0.0060  13  ASP   F C     
4057 O O     . ASP   F 13  ? 0.2030 0.2240 0.2285 0.0075  0.0266  0.0098  13  ASP   F O     
4058 C CB    . ASP   F 13  ? 0.1730 0.2083 0.2425 0.0249  0.0386  0.0003  13  ASP   F CB    
4059 C CG    . ASP   F 13  ? 0.1642 0.2084 0.2561 0.0285  0.0416  -0.0009 13  ASP   F CG    
4060 O OD1   . ASP   F 13  ? 0.1480 0.1945 0.2475 0.0290  0.0394  -0.0002 13  ASP   F OD1   
4061 O OD2   . ASP   F 13  ? 0.1777 0.2260 0.2791 0.0299  0.0470  -0.0025 13  ASP   F OD2   
4062 N N     . ASN   F 14  ? 0.1967 0.2084 0.2239 0.0119  0.0244  0.0015  14  ASN   F N     
4063 C CA    . ASN   F 14  ? 0.2201 0.2133 0.2211 0.0064  0.0209  -0.0018 14  ASN   F CA    
4064 C C     . ASN   F 14  ? 0.2220 0.1999 0.2151 0.0156  0.0255  -0.0114 14  ASN   F C     
4065 O O     . ASN   F 14  ? 0.2116 0.1909 0.2150 0.0215  0.0253  -0.0132 14  ASN   F O     
4066 C CB    . ASN   F 14  ? 0.2256 0.2170 0.2223 -0.0033 0.0129  0.0030  14  ASN   F CB    
4067 C CG    . ASN   F 14  ? 0.2479 0.2180 0.2159 -0.0129 0.0075  0.0003  14  ASN   F CG    
4068 O OD1   . ASN   F 14  ? 0.2632 0.2107 0.2146 -0.0094 0.0093  -0.0075 14  ASN   F OD1   
4069 N ND2   . ASN   F 14  ? 0.2589 0.2346 0.2201 -0.0249 0.0003  0.0066  14  ASN   F ND2   
4070 N N     . THR   F 15  ? 0.2534 0.2159 0.2266 0.0168  0.0292  -0.0171 15  THR   F N     
4071 C CA    . THR   F 15  ? 0.2716 0.2204 0.2397 0.0281  0.0350  -0.0257 15  THR   F CA    
4072 C C     . THR   F 15  ? 0.2944 0.2210 0.2490 0.0287  0.0296  -0.0283 15  THR   F C     
4073 O O     . THR   F 15  ? 0.2980 0.2182 0.2570 0.0406  0.0324  -0.0327 15  THR   F O     
4074 C CB    . THR   F 15  ? 0.2925 0.2303 0.2418 0.0299  0.0432  -0.0315 15  THR   F CB    
4075 O OG1   . THR   F 15  ? 0.3059 0.2257 0.2257 0.0173  0.0375  -0.0314 15  THR   F OG1   
4076 C CG2   . THR   F 15  ? 0.2825 0.2424 0.2481 0.0318  0.0508  -0.0284 15  THR   F CG2   
4077 N N     . HIS   F 16  ? 0.3134 0.2289 0.2527 0.0156  0.0217  -0.0246 16  HIS   F N     
4078 C CA    . HIS   F 16  ? 0.3423 0.2325 0.2650 0.0130  0.0168  -0.0260 16  HIS   F CA    
4079 C C     . HIS   F 16  ? 0.3456 0.2453 0.2801 0.0077  0.0110  -0.0184 16  HIS   F C     
4080 O O     . HIS   F 16  ? 0.3741 0.2536 0.2978 0.0090  0.0085  -0.0188 16  HIS   F O     
4081 C CB    . HIS   F 16  ? 0.3726 0.2376 0.2644 -0.0001 0.0128  -0.0288 16  HIS   F CB    
4082 C CG    . HIS   F 16  ? 0.3982 0.2420 0.2686 0.0067  0.0203  -0.0391 16  HIS   F CG    
4083 N ND1   . HIS   F 16  ? 0.4417 0.2486 0.2783 -0.0001 0.0183  -0.0458 16  HIS   F ND1   
4084 C CD2   . HIS   F 16  ? 0.3876 0.2386 0.2635 0.0194  0.0310  -0.0444 16  HIS   F CD2   
4085 C CE1   . HIS   F 16  ? 0.4679 0.2609 0.2888 0.0090  0.0283  -0.0555 16  HIS   F CE1   
4086 N NE2   . HIS   F 16  ? 0.4382 0.2596 0.2844 0.0212  0.0366  -0.0542 16  HIS   F NE2   
4087 N N     . TYR   F 17  ? 0.3446 0.2714 0.2982 0.0017  0.0094  -0.0113 17  TYR   F N     
4088 C CA    . TYR   F 17  ? 0.3186 0.2555 0.2812 -0.0056 0.0059  -0.0038 17  TYR   F CA    
4089 C C     . TYR   F 17  ? 0.2808 0.2420 0.2681 0.0026  0.0101  -0.0019 17  TYR   F C     
4090 O O     . TYR   F 17  ? 0.2797 0.2552 0.2808 0.0085  0.0138  -0.0035 17  TYR   F O     
4091 C CB    . TYR   F 17  ? 0.3193 0.2651 0.2811 -0.0217 0.0003  0.0031  17  TYR   F CB    
4092 C CG    . TYR   F 17  ? 0.3455 0.2641 0.2791 -0.0328 -0.0054 0.0001  17  TYR   F CG    
4093 C CD1   . TYR   F 17  ? 0.3920 0.2882 0.3102 -0.0409 -0.0091 0.0010  17  TYR   F CD1   
4094 C CD2   . TYR   F 17  ? 0.3533 0.2651 0.2721 -0.0365 -0.0069 -0.0038 17  TYR   F CD2   
4095 C CE1   . TYR   F 17  ? 0.4099 0.2749 0.2994 -0.0518 -0.0142 -0.0033 17  TYR   F CE1   
4096 C CE2   . TYR   F 17  ? 0.3928 0.2752 0.2810 -0.0474 -0.0120 -0.0087 17  TYR   F CE2   
4097 C CZ    . TYR   F 17  ? 0.4309 0.2885 0.3047 -0.0551 -0.0157 -0.0091 17  TYR   F CZ    
4098 O OH    . TYR   F 17  ? 0.4706 0.2937 0.3118 -0.0665 -0.0206 -0.0152 17  TYR   F OH    
4099 N N     . SER   F 18  ? 0.2705 0.2341 0.2608 0.0016  0.0097  0.0015  18  SER   F N     
4100 C CA    . SER   F 18  ? 0.2514 0.2341 0.2597 0.0072  0.0138  0.0023  18  SER   F CA    
4101 C C     . SER   F 18  ? 0.2301 0.2337 0.2538 0.0000  0.0159  0.0093  18  SER   F C     
4102 O O     . SER   F 18  ? 0.2388 0.2428 0.2586 -0.0111 0.0128  0.0153  18  SER   F O     
4103 C CB    . SER   F 18  ? 0.2526 0.2266 0.2526 0.0107  0.0133  0.0020  18  SER   F CB    
4104 O OG    . SER   F 18  ? 0.2539 0.2233 0.2447 0.0005  0.0126  0.0086  18  SER   F OG    
4105 N N     . ARG   F 19  ? 0.2186 0.2387 0.2605 0.0066  0.0212  0.0085  19  ARG   F N     
4106 C CA    . ARG   F 19  ? 0.2039 0.2439 0.2636 0.0040  0.0256  0.0148  19  ARG   F CA    
4107 C C     . ARG   F 19  ? 0.2000 0.2407 0.2542 -0.0018 0.0278  0.0187  19  ARG   F C     
4108 O O     . ARG   F 19  ? 0.1914 0.2464 0.2559 -0.0095 0.0288  0.0267  19  ARG   F O     
4109 C CB    . ARG   F 19  ? 0.1956 0.2462 0.2722 0.0132  0.0324  0.0116  19  ARG   F CB    
4110 C CG    . ARG   F 19  ? 0.1885 0.2468 0.2798 0.0168  0.0328  0.0130  19  ARG   F CG    
4111 C CD    . ARG   F 19  ? 0.1823 0.2310 0.2671 0.0197  0.0305  0.0077  19  ARG   F CD    
4112 N NE    . ARG   F 19  ? 0.1858 0.2413 0.2840 0.0222  0.0326  0.0105  19  ARG   F NE    
4113 C CZ    . ARG   F 19  ? 0.1681 0.2191 0.2655 0.0246  0.0333  0.0071  19  ARG   F CZ    
4114 N NH1   . ARG   F 19  ? 0.1619 0.2049 0.2513 0.0273  0.0329  -0.0005 19  ARG   F NH1   
4115 N NH2   . ARG   F 19  ? 0.1565 0.2125 0.2633 0.0249  0.0350  0.0123  19  ARG   F NH2   
4116 N N     . PHE   F 20  ? 0.2166 0.2440 0.2559 0.0017  0.0287  0.0142  20  PHE   F N     
4117 C CA    . PHE   F 20  ? 0.2430 0.2687 0.2729 -0.0037 0.0322  0.0183  20  PHE   F CA    
4118 C C     . PHE   F 20  ? 0.2598 0.2801 0.2820 -0.0172 0.0277  0.0261  20  PHE   F C     
4119 O O     . PHE   F 20  ? 0.2589 0.2950 0.2912 -0.0252 0.0323  0.0335  20  PHE   F O     
4120 C CB    . PHE   F 20  ? 0.2779 0.2861 0.2878 0.0019  0.0303  0.0132  20  PHE   F CB    
4121 C CG    . PHE   F 20  ? 0.3091 0.3113 0.3029 -0.0045 0.0335  0.0187  20  PHE   F CG    
4122 C CD1   . PHE   F 20  ? 0.3142 0.3307 0.3126 -0.0049 0.0441  0.0199  20  PHE   F CD1   
4123 C CD2   . PHE   F 20  ? 0.3422 0.3222 0.3147 -0.0102 0.0271  0.0230  20  PHE   F CD2   
4124 C CE1   . PHE   F 20  ? 0.3352 0.3467 0.3165 -0.0118 0.0489  0.0258  20  PHE   F CE1   
4125 C CE2   . PHE   F 20  ? 0.3526 0.3251 0.3079 -0.0172 0.0304  0.0297  20  PHE   F CE2   
4126 C CZ    . PHE   F 20  ? 0.3442 0.3337 0.3036 -0.0186 0.0415  0.0314  20  PHE   F CZ    
4127 N N     . HIS   F 21  ? 0.2606 0.2596 0.2668 -0.0200 0.0195  0.0242  21  HIS   F N     
4128 C CA    . HIS   F 21  ? 0.2763 0.2637 0.2710 -0.0346 0.0142  0.0300  21  HIS   F CA    
4129 C C     . HIS   F 21  ? 0.2562 0.2674 0.2703 -0.0448 0.0128  0.0365  21  HIS   F C     
4130 O O     . HIS   F 21  ? 0.2609 0.2839 0.2818 -0.0566 0.0142  0.0449  21  HIS   F O     
4131 C CB    . HIS   F 21  ? 0.2949 0.2498 0.2662 -0.0333 0.0070  0.0246  21  HIS   F CB    
4132 C CG    . HIS   F 21  ? 0.3108 0.2514 0.2701 -0.0485 0.0004  0.0273  21  HIS   F CG    
4133 N ND1   . HIS   F 21  ? 0.3284 0.2499 0.2741 -0.0473 -0.0045 0.0205  21  HIS   F ND1   
4134 C CD2   . HIS   F 21  ? 0.3182 0.2610 0.2764 -0.0663 -0.0022 0.0354  21  HIS   F CD2   
4135 C CE1   . HIS   F 21  ? 0.3404 0.2499 0.2740 -0.0644 -0.0107 0.0235  21  HIS   F CE1   
4136 N NE2   . HIS   F 21  ? 0.3327 0.2561 0.2755 -0.0767 -0.0102 0.0330  21  HIS   F NE2   
4137 N N     . LEU   F 22  ? 0.2377 0.2575 0.2616 -0.0406 0.0099  0.0340  22  LEU   F N     
4138 C CA    . LEU   F 22  ? 0.2347 0.2747 0.2736 -0.0507 0.0049  0.0414  22  LEU   F CA    
4139 C C     . LEU   F 22  ? 0.2251 0.2991 0.2944 -0.0495 0.0118  0.0497  22  LEU   F C     
4140 O O     . LEU   F 22  ? 0.2374 0.3307 0.3207 -0.0616 0.0077  0.0591  22  LEU   F O     
4141 C CB    . LEU   F 22  ? 0.2237 0.2616 0.2604 -0.0469 -0.0003 0.0379  22  LEU   F CB    
4142 C CG    . LEU   F 22  ? 0.2521 0.2578 0.2589 -0.0484 -0.0054 0.0294  22  LEU   F CG    
4143 C CD1   . LEU   F 22  ? 0.2492 0.2554 0.2520 -0.0467 -0.0089 0.0272  22  LEU   F CD1   
4144 C CD2   . LEU   F 22  ? 0.2828 0.2677 0.2686 -0.0647 -0.0124 0.0308  22  LEU   F CD2   
4145 N N     . LEU   F 23  ? 0.2179 0.2993 0.2978 -0.0357 0.0220  0.0463  23  LEU   F N     
4146 C CA    . LEU   F 23  ? 0.2213 0.3310 0.3279 -0.0321 0.0317  0.0524  23  LEU   F CA    
4147 C C     . LEU   F 23  ? 0.2350 0.3511 0.3407 -0.0422 0.0373  0.0584  23  LEU   F C     
4148 O O     . LEU   F 23  ? 0.2248 0.3696 0.3556 -0.0478 0.0404  0.0682  23  LEU   F O     
4149 C CB    . LEU   F 23  ? 0.2154 0.3265 0.3296 -0.0154 0.0418  0.0454  23  LEU   F CB    
4150 C CG    . LEU   F 23  ? 0.2280 0.3393 0.3512 -0.0064 0.0386  0.0427  23  LEU   F CG    
4151 C CD1   . LEU   F 23  ? 0.2109 0.3150 0.3350 0.0070  0.0472  0.0336  23  LEU   F CD1   
4152 C CD2   . LEU   F 23  ? 0.2420 0.3799 0.3930 -0.0077 0.0365  0.0540  23  LEU   F CD2   
4153 N N     . ILE   F 24  ? 0.2590 0.3505 0.3377 -0.0446 0.0387  0.0541  24  ILE   F N     
4154 C CA    . ILE   F 24  ? 0.2824 0.3776 0.3569 -0.0559 0.0445  0.0613  24  ILE   F CA    
4155 C C     . ILE   F 24  ? 0.3107 0.4100 0.3883 -0.0755 0.0351  0.0705  24  ILE   F C     
4156 O O     . ILE   F 24  ? 0.3355 0.4567 0.4287 -0.0866 0.0406  0.0803  24  ILE   F O     
4157 C CB    . ILE   F 24  ? 0.2965 0.3640 0.3401 -0.0535 0.0477  0.0567  24  ILE   F CB    
4158 C CG1   . ILE   F 24  ? 0.3132 0.3448 0.3281 -0.0569 0.0354  0.0529  24  ILE   F CG1   
4159 C CG2   . ILE   F 24  ? 0.2915 0.3605 0.3346 -0.0366 0.0565  0.0480  24  ILE   F CG2   
4160 C CD1   . ILE   F 24  ? 0.3345 0.3408 0.3211 -0.0543 0.0370  0.0516  24  ILE   F CD1   
4161 N N     . GLU   F 25  ? 0.3151 0.3958 0.3796 -0.0801 0.0217  0.0670  25  GLU   F N     
4162 C CA    . GLU   F 25  ? 0.3280 0.4058 0.3888 -0.1003 0.0106  0.0732  25  GLU   F CA    
4163 C C     . GLU   F 25  ? 0.3092 0.4262 0.4037 -0.1067 0.0066  0.0824  25  GLU   F C     
4164 O O     . GLU   F 25  ? 0.3250 0.4606 0.4331 -0.1238 0.0048  0.0926  25  GLU   F O     
4165 C CB    . GLU   F 25  ? 0.3505 0.3905 0.3806 -0.1017 -0.0005 0.0643  25  GLU   F CB    
4166 C CG    . GLU   F 25  ? 0.3888 0.4135 0.4045 -0.1247 -0.0115 0.0684  25  GLU   F CG    
4167 C CD    . GLU   F 25  ? 0.4202 0.4041 0.4032 -0.1226 -0.0194 0.0575  25  GLU   F CD    
4168 O OE1   . GLU   F 25  ? 0.4448 0.3933 0.4023 -0.1167 -0.0174 0.0515  25  GLU   F OE1   
4169 O OE2   . GLU   F 25  ? 0.4437 0.4340 0.4285 -0.1250 -0.0271 0.0554  25  GLU   F OE2   
4170 N N     . THR   F 26  ? 0.2803 0.4108 0.3892 -0.0939 0.0048  0.0802  26  THR   F N     
4171 C CA    . THR   F 26  ? 0.2694 0.4371 0.4109 -0.0976 -0.0008 0.0906  26  THR   F CA    
4172 C C     . THR   F 26  ? 0.2530 0.4598 0.4319 -0.0935 0.0120  0.1002  26  THR   F C     
4173 O O     . THR   F 26  ? 0.2416 0.4836 0.4514 -0.1006 0.0069  0.1121  26  THR   F O     
4174 C CB    . THR   F 26  ? 0.2684 0.4363 0.4128 -0.0838 -0.0051 0.0870  26  THR   F CB    
4175 O OG1   . THR   F 26  ? 0.2630 0.4252 0.4096 -0.0636 0.0082  0.0795  26  THR   F OG1   
4176 C CG2   . THR   F 26  ? 0.2777 0.4134 0.3883 -0.0898 -0.0172 0.0791  26  THR   F CG2   
4177 N N     . ASN   F 27  ? 0.2550 0.4569 0.4312 -0.0815 0.0284  0.0953  27  ASN   F N     
4178 C CA    . ASN   F 27  ? 0.2621 0.4971 0.4683 -0.0774 0.0441  0.1027  27  ASN   F CA    
4179 C C     . ASN   F 27  ? 0.2833 0.5208 0.4840 -0.0948 0.0495  0.1090  27  ASN   F C     
4180 O O     . ASN   F 27  ? 0.3164 0.5765 0.5353 -0.0904 0.0662  0.1133  27  ASN   F O     
4181 C CB    . ASN   F 27  ? 0.2384 0.4675 0.4440 -0.0550 0.0597  0.0935  27  ASN   F CB    
4182 C CG    . ASN   F 27  ? 0.2106 0.4475 0.4340 -0.0397 0.0567  0.0920  27  ASN   F CG    
4183 O OD1   . ASN   F 27  ? 0.2055 0.4757 0.4653 -0.0342 0.0603  0.1013  27  ASN   F OD1   
4184 N ND2   . ASN   F 27  ? 0.1982 0.4064 0.3987 -0.0325 0.0506  0.0818  27  ASN   F ND2   
4185 N N     . GLY   F 28  ? 0.3158 0.5295 0.4913 -0.1142 0.0373  0.1098  28  GLY   F N     
4186 C CA    . GLY   F 28  ? 0.3254 0.5411 0.4972 -0.1339 0.0411  0.1181  28  GLY   F CA    
4187 C C     . GLY   F 28  ? 0.3432 0.5430 0.4946 -0.1282 0.0581  0.1151  28  GLY   F C     
4188 O O     . GLY   F 28  ? 0.3594 0.5764 0.5204 -0.1404 0.0683  0.1248  28  GLY   F O     
4189 N N     . ILE   F 29  ? 0.3368 0.5051 0.4599 -0.1116 0.0605  0.1028  29  ILE   F N     
4190 C CA    . ILE   F 29  ? 0.3675 0.5152 0.4635 -0.1073 0.0725  0.0997  29  ILE   F CA    
4191 C C     . ILE   F 29  ? 0.4060 0.5139 0.4659 -0.1221 0.0625  0.1011  29  ILE   F C     
4192 O O     . ILE   F 29  ? 0.4223 0.5193 0.4644 -0.1303 0.0704  0.1067  29  ILE   F O     
4193 C CB    . ILE   F 29  ? 0.3545 0.4908 0.4402 -0.0839 0.0782  0.0868  29  ILE   F CB    
4194 C CG1   . ILE   F 29  ? 0.3399 0.5131 0.4611 -0.0703 0.0916  0.0868  29  ILE   F CG1   
4195 C CG2   . ILE   F 29  ? 0.3830 0.4922 0.4329 -0.0807 0.0853  0.0830  29  ILE   F CG2   
4196 C CD1   . ILE   F 29  ? 0.3438 0.5072 0.4620 -0.0495 0.0930  0.0741  29  ILE   F CD1   
4197 N N     . THR   F 30  ? 0.4088 0.4924 0.4558 -0.1245 0.0459  0.0958  30  THR   F N     
4198 C CA    . THR   F 30  ? 0.4327 0.4763 0.4483 -0.1383 0.0351  0.0965  30  THR   F CA    
4199 C C     . THR   F 30  ? 0.4400 0.4947 0.4694 -0.1616 0.0251  0.1044  30  THR   F C     
4200 O O     . THR   F 30  ? 0.3823 0.4726 0.4432 -0.1630 0.0226  0.1072  30  THR   F O     
4201 C CB    . THR   F 30  ? 0.4335 0.4418 0.4250 -0.1244 0.0251  0.0840  30  THR   F CB    
4202 O OG1   . THR   F 30  ? 0.4346 0.4587 0.4443 -0.1237 0.0169  0.0805  30  THR   F OG1   
4203 C CG2   . THR   F 30  ? 0.4278 0.4334 0.4132 -0.1019 0.0324  0.0759  30  THR   F CG2   
4204 N N     . LYS   F 31  ? 0.5140 0.5366 0.5188 -0.1803 0.0187  0.1084  31  LYS   F N     
4205 C CA    . LYS   F 31  ? 0.5419 0.5682 0.5536 -0.2071 0.0081  0.1158  31  LYS   F CA    
4206 C C     . LYS   F 31  ? 0.5764 0.5451 0.5474 -0.2142 -0.0047 0.1087  31  LYS   F C     
4207 O O     . LYS   F 31  ? 0.6066 0.5436 0.5540 -0.2264 -0.0035 0.1138  31  LYS   F O     
4208 C CB    . LYS   F 31  ? 0.5502 0.6027 0.5794 -0.2247 0.0193  0.1308  31  LYS   F CB    
4209 C CG    . LYS   F 31  ? 0.5188 0.6318 0.5934 -0.2178 0.0326  0.1377  31  LYS   F CG    
4210 C CD    . LYS   F 31  ? 0.5011 0.6539 0.6129 -0.2222 0.0223  0.1403  31  LYS   F CD    
4211 C CE    . LYS   F 31  ? 0.4914 0.7051 0.6525 -0.2222 0.0346  0.1519  31  LYS   F CE    
4212 N NZ    . LYS   F 31  ? 0.4638 0.7132 0.6592 -0.2140 0.0257  0.1523  31  LYS   F NZ    
4213 N N     . PRO   F 32  ? 0.5656 0.5158 0.5246 -0.2044 -0.0151 0.0965  32  PRO   F N     
4214 C CA    . PRO   F 32  ? 0.6042 0.4985 0.5245 -0.2093 -0.0252 0.0882  32  PRO   F CA    
4215 C C     . PRO   F 32  ? 0.6416 0.5200 0.5526 -0.2411 -0.0361 0.0935  32  PRO   F C     
4216 O O     . PRO   F 32  ? 0.6491 0.5640 0.5857 -0.2581 -0.0425 0.0995  32  PRO   F O     
4217 C CB    . PRO   F 32  ? 0.5901 0.4798 0.5061 -0.1927 -0.0310 0.0750  32  PRO   F CB    
4218 C CG    . PRO   F 32  ? 0.5440 0.4813 0.4932 -0.1749 -0.0226 0.0764  32  PRO   F CG    
4219 C CD    . PRO   F 32  ? 0.5379 0.5169 0.5178 -0.1877 -0.0163 0.0901  32  PRO   F CD    
4220 N N     . CYS   F 33  ? 0.6642 0.4886 0.5397 -0.2490 -0.0383 0.0924  33  CYS   F N     
4221 C CA    . CYS   F 33  ? 0.7006 0.4929 0.5566 -0.2785 -0.0495 0.0941  33  CYS   F CA    
4222 C C     . CYS   F 33  ? 0.7263 0.4551 0.5399 -0.2700 -0.0560 0.0793  33  CYS   F C     
4223 O O     . CYS   F 33  ? 0.7466 0.4443 0.5416 -0.2496 -0.0491 0.0765  33  CYS   F O     
4224 C CB    . CYS   F 33  ? 0.7256 0.5081 0.5781 -0.2963 -0.0431 0.1085  33  CYS   F CB    
4225 S SG    . CYS   F 33  ? 0.7798 0.5260 0.6126 -0.3384 -0.0569 0.1129  33  CYS   F SG    
4226 N N     . ILE   F 34  ? 0.7407 0.4530 0.5401 -0.2839 -0.0686 0.0701  34  ILE   F N     
4227 C CA    . ILE   F 34  ? 0.8057 0.4546 0.5623 -0.2784 -0.0734 0.0548  34  ILE   F CA    
4228 C C     . ILE   F 34  ? 0.8970 0.4972 0.6253 -0.3091 -0.0817 0.0570  34  ILE   F C     
4229 O O     . ILE   F 34  ? 0.8985 0.5179 0.6367 -0.3394 -0.0921 0.0621  34  ILE   F O     
4230 C CB    . ILE   F 34  ? 0.7888 0.4448 0.5402 -0.2738 -0.0809 0.0412  34  ILE   F CB    
4231 C CG1   . ILE   F 34  ? 0.7296 0.4363 0.5118 -0.2462 -0.0732 0.0404  34  ILE   F CG1   
4232 C CG2   . ILE   F 34  ? 0.8381 0.4262 0.5427 -0.2675 -0.0830 0.0241  34  ILE   F CG2   
4233 C CD1   . ILE   F 34  ? 0.6940 0.3926 0.4767 -0.2145 -0.0602 0.0381  34  ILE   F CD1   
4234 N N     . VAL   F 35  ? 0.9563 0.4933 0.6499 -0.3011 -0.0781 0.0531  35  VAL   F N     
4235 C CA    . VAL   F 35  ? 1.0372 0.5147 0.6970 -0.3278 -0.0856 0.0526  35  VAL   F CA    
4236 C C     . VAL   F 35  ? 1.0715 0.4829 0.6884 -0.3134 -0.0874 0.0330  35  VAL   F C     
4237 O O     . VAL   F 35  ? 1.0418 0.4313 0.6494 -0.2812 -0.0783 0.0276  35  VAL   F O     
4238 C CB    . VAL   F 35  ? 1.0987 0.5563 0.7551 -0.3385 -0.0801 0.0693  35  VAL   F CB    
4239 C CG1   . VAL   F 35  ? 1.0865 0.6090 0.7835 -0.3585 -0.0778 0.0876  35  VAL   F CG1   
4240 C CG2   . VAL   F 35  ? 1.0763 0.5137 0.7244 -0.3056 -0.0690 0.0717  35  VAL   F CG2   
4241 N N     . SER   F 36  ? 1.1093 0.4945 0.7022 -0.3373 -0.0991 0.0218  36  SER   F N     
4242 C CA    . SER   F 36  ? 1.1738 0.4868 0.7188 -0.3324 -0.1010 0.0025  36  SER   F CA    
4243 C C     . SER   F 36  ? 1.2621 0.5060 0.7741 -0.3559 -0.1050 0.0054  36  SER   F C     
4244 O O     . SER   F 36  ? 1.2817 0.5390 0.8098 -0.3767 -0.1064 0.0234  36  SER   F O     
4245 C CB    . SER   F 36  ? 1.1664 0.4893 0.6997 -0.3459 -0.1115 -0.0119 36  SER   F CB    
4246 O OG    . SER   F 36  ? 1.1826 0.5141 0.7163 -0.3887 -0.1272 -0.0061 36  SER   F OG    
4247 N N     . THR   F 37  ? 1.3305 0.4994 0.7949 -0.3540 -0.1063 -0.0127 37  THR   F N     
4248 C CA    . THR   F 37  ? 1.4041 0.4978 0.8300 -0.3802 -0.1122 -0.0138 37  THR   F CA    
4249 C C     . THR   F 37  ? 1.4396 0.5481 0.8676 -0.4298 -0.1285 -0.0086 37  THR   F C     
4250 O O     . THR   F 37  ? 1.5009 0.5696 0.9149 -0.4567 -0.1328 0.0003  37  THR   F O     
4251 C CB    . THR   F 37  ? 1.4462 0.4567 0.8202 -0.3655 -0.1088 -0.0369 37  THR   F CB    
4252 O OG1   . THR   F 37  ? 1.4374 0.4598 0.7981 -0.3687 -0.1139 -0.0556 37  THR   F OG1   
4253 C CG2   . THR   F 37  ? 1.4237 0.4137 0.7971 -0.3181 -0.0930 -0.0396 37  THR   F CG2   
4254 N N     . GLU   F 38  ? 1.4011 0.5683 0.8491 -0.4421 -0.1380 -0.0120 38  GLU   F N     
4255 C CA    . GLU   F 38  ? 1.4091 0.5933 0.8593 -0.4884 -0.1564 -0.0089 38  GLU   F CA    
4256 C C     . GLU   F 38  ? 1.3531 0.6324 0.8632 -0.5024 -0.1607 0.0122  38  GLU   F C     
4257 O O     . GLU   F 38  ? 1.3602 0.6536 0.8792 -0.5428 -0.1746 0.0208  38  GLU   F O     
4258 C CB    . GLU   F 38  ? 1.4235 0.5922 0.8416 -0.4933 -0.1668 -0.0309 38  GLU   F CB    
4259 C CG    . GLU   F 38  ? 1.4960 0.5681 0.8514 -0.4823 -0.1619 -0.0544 38  GLU   F CG    
4260 C CD    . GLU   F 38  ? 1.5292 0.5774 0.8434 -0.4929 -0.1721 -0.0775 38  GLU   F CD    
4261 O OE1   . GLU   F 38  ? 1.4935 0.6007 0.8262 -0.5095 -0.1855 -0.0750 38  GLU   F OE1   
4262 O OE2   . GLU   F 38  ? 1.5830 0.5514 0.8446 -0.4825 -0.1659 -0.0982 38  GLU   F OE2   
4263 N N     . ASN   F 39  ? 1.2972 0.6410 0.8483 -0.4709 -0.1495 0.0201  39  ASN   F N     
4264 C CA    . ASN   F 39  ? 1.2376 0.6724 0.8449 -0.4794 -0.1527 0.0368  39  ASN   F CA    
4265 C C     . ASN   F 39  ? 1.1776 0.6575 0.8226 -0.4475 -0.1348 0.0497  39  ASN   F C     
4266 O O     . ASN   F 39  ? 1.1304 0.5883 0.7625 -0.4121 -0.1231 0.0414  39  ASN   F O     
4267 C CB    . ASN   F 39  ? 1.2198 0.6965 0.8360 -0.4756 -0.1626 0.0280  39  ASN   F CB    
4268 C CG    . ASN   F 39  ? 1.2728 0.7252 0.8600 -0.5134 -0.1840 0.0188  39  ASN   F CG    
4269 O OD1   . ASN   F 39  ? 1.2778 0.7572 0.8855 -0.5500 -0.1970 0.0313  39  ASN   F OD1   
4270 N ND2   . ASN   F 39  ? 1.3129 0.7159 0.8525 -0.5063 -0.1879 -0.0030 39  ASN   F ND2   
4271 N N     . VAL   F 40  ? 1.1622 0.7053 0.8536 -0.4615 -0.1331 0.0695  40  VAL   F N     
4272 C CA    . VAL   F 40  ? 1.0990 0.6975 0.8304 -0.4354 -0.1175 0.0815  40  VAL   F CA    
4273 C C     . VAL   F 40  ? 1.0245 0.6994 0.7984 -0.4328 -0.1226 0.0845  40  VAL   F C     
4274 O O     . VAL   F 40  ? 1.0253 0.7354 0.8214 -0.4632 -0.1350 0.0928  40  VAL   F O     
4275 C CB    . VAL   F 40  ? 1.1257 0.7374 0.8762 -0.4512 -0.1085 0.1017  40  VAL   F CB    
4276 C CG1   . VAL   F 40  ? 1.0570 0.7272 0.8464 -0.4257 -0.0917 0.1129  40  VAL   F CG1   
4277 C CG2   . VAL   F 40  ? 1.2073 0.7403 0.9145 -0.4602 -0.1062 0.1020  40  VAL   F CG2   
4278 N N     . TYR   F 41  ? 0.9645 0.6637 0.7500 -0.3973 -0.1141 0.0783  41  TYR   F N     
4279 C CA    . TYR   F 41  ? 0.8946 0.6628 0.7203 -0.3888 -0.1165 0.0821  41  TYR   F CA    
4280 C C     . TYR   F 41  ? 0.8739 0.6941 0.7424 -0.3731 -0.1002 0.0966  41  TYR   F C     
4281 O O     . TYR   F 41  ? 0.8129 0.6257 0.6776 -0.3423 -0.0864 0.0926  41  TYR   F O     
4282 C CB    . TYR   F 41  ? 0.8622 0.6182 0.6692 -0.3631 -0.1178 0.0658  41  TYR   F CB    
4283 C CG    . TYR   F 41  ? 0.8947 0.5951 0.6538 -0.3783 -0.1316 0.0499  41  TYR   F CG    
4284 C CD1   . TYR   F 41  ? 0.9345 0.5610 0.6469 -0.3708 -0.1267 0.0367  41  TYR   F CD1   
4285 C CD2   . TYR   F 41  ? 0.8981 0.6178 0.6568 -0.4003 -0.1497 0.0482  41  TYR   F CD2   
4286 C CE1   . TYR   F 41  ? 0.9812 0.5524 0.6466 -0.3837 -0.1371 0.0205  41  TYR   F CE1   
4287 C CE2   . TYR   F 41  ? 0.9494 0.6149 0.6585 -0.4155 -0.1620 0.0321  41  TYR   F CE2   
4288 C CZ    . TYR   F 41  ? 0.9965 0.5862 0.6581 -0.4070 -0.1545 0.0174  41  TYR   F CZ    
4289 O OH    . TYR   F 41  ? 1.0636 0.5943 0.6732 -0.4193 -0.1635 -0.0004 41  TYR   F OH    
4290 N N     . THR   F 42  ? 0.8711 0.7432 0.7792 -0.3950 -0.1016 0.1131  42  THR   F N     
4291 C CA    . THR   F 42  ? 0.8353 0.7523 0.7804 -0.3851 -0.0840 0.1272  42  THR   F CA    
4292 C C     . THR   F 42  ? 0.7734 0.7395 0.7501 -0.3541 -0.0761 0.1259  42  THR   F C     
4293 O O     . THR   F 42  ? 0.7416 0.7256 0.7260 -0.3509 -0.0875 0.1207  42  THR   F O     
4294 C CB    . THR   F 42  ? 0.8263 0.7871 0.8075 -0.4174 -0.0860 0.1454  42  THR   F CB    
4295 O OG1   . THR   F 42  ? 0.7987 0.8136 0.8159 -0.4277 -0.0994 0.1498  42  THR   F OG1   
4296 C CG2   . THR   F 42  ? 0.8803 0.7937 0.8325 -0.4520 -0.0944 0.1480  42  THR   F CG2   
4297 N N     . PRO   F 43  ? 0.7594 0.7485 0.7546 -0.3324 -0.0569 0.1312  43  PRO   F N     
4298 C CA    . PRO   F 43  ? 0.7091 0.7504 0.7411 -0.3079 -0.0486 0.1324  43  PRO   F CA    
4299 C C     . PRO   F 43  ? 0.7054 0.8144 0.7894 -0.3207 -0.0521 0.1460  43  PRO   F C     
4300 O O     . PRO   F 43  ? 0.6755 0.8218 0.7871 -0.3011 -0.0500 0.1457  43  PRO   F O     
4301 C CB    . PRO   F 43  ? 0.6982 0.7384 0.7292 -0.2873 -0.0277 0.1341  43  PRO   F CB    
4302 C CG    . PRO   F 43  ? 0.7551 0.7621 0.7630 -0.3085 -0.0245 0.1414  43  PRO   F CG    
4303 C CD    . PRO   F 43  ? 0.7806 0.7425 0.7581 -0.3308 -0.0427 0.1360  43  PRO   F CD    
4304 N N     . ASP   F 44  ? 0.7424 0.8675 0.8415 -0.3528 -0.0576 0.1584  44  ASP   F N     
4305 C CA    . ASP   F 44  ? 0.7488 0.9375 0.8979 -0.3700 -0.0659 0.1722  44  ASP   F CA    
4306 C C     . ASP   F 44  ? 0.7548 0.9396 0.8958 -0.3865 -0.0926 0.1678  44  ASP   F C     
4307 O O     . ASP   F 44  ? 0.7705 1.0030 0.9485 -0.4077 -0.1047 0.1802  44  ASP   F O     
4308 C CB    . ASP   F 44  ? 0.7136 0.9275 0.8870 -0.3973 -0.0585 0.1886  44  ASP   F CB    
4309 N N     . ASN   F 45  ? 0.7410 0.8709 0.8338 -0.3786 -0.1023 0.1509  45  ASN   F N     
4310 C CA    . ASN   F 45  ? 0.7562 0.8809 0.8352 -0.3857 -0.1243 0.1440  45  ASN   F CA    
4311 C C     . ASN   F 45  ? 0.7911 0.8915 0.8484 -0.4260 -0.1447 0.1442  45  ASN   F C     
4312 O O     . ASN   F 45  ? 0.7974 0.9158 0.8587 -0.4410 -0.1654 0.1452  45  ASN   F O     
4313 C CB    . ASN   F 45  ? 0.7509 0.9409 0.8770 -0.3729 -0.1289 0.1533  45  ASN   F CB    
4314 C CG    . ASN   F 45  ? 0.7889 0.9672 0.8935 -0.3629 -0.1436 0.1436  45  ASN   F CG    
4315 O OD1   . ASN   F 45  ? 0.7704 0.9828 0.8933 -0.3766 -0.1627 0.1514  45  ASN   F OD1   
4316 N ND2   . ASN   F 45  ? 0.8507 0.9883 0.9216 -0.3371 -0.1342 0.1287  45  ASN   F ND2   
4317 N N     . ALA   F 46  ? 0.8204 0.8741 0.8491 -0.4432 -0.1403 0.1422  46  ALA   F N     
4318 C CA    . ALA   F 46  ? 0.8578 0.8819 0.8639 -0.4837 -0.1583 0.1421  46  ALA   F CA    
4319 C C     . ALA   F 46  ? 0.8866 0.8212 0.8257 -0.4828 -0.1586 0.1236  46  ALA   F C     
4320 O O     . ALA   F 46  ? 0.8622 0.7642 0.7835 -0.4588 -0.1408 0.1187  46  ALA   F O     
4321 C CB    . ALA   F 46  ? 0.8654 0.9197 0.9053 -0.5096 -0.1523 0.1604  46  ALA   F CB    
4322 N N     . THR   F 47  ? 0.9324 0.8288 0.8349 -0.5076 -0.1794 0.1132  47  THR   F N     
4323 C CA    . THR   F 47  ? 0.9998 0.8085 0.8385 -0.5126 -0.1814 0.0956  47  THR   F CA    
4324 C C     . THR   F 47  ? 1.0456 0.8271 0.8760 -0.5510 -0.1864 0.1034  47  THR   F C     
4325 O O     . THR   F 47  ? 1.0754 0.8745 0.9141 -0.5870 -0.2061 0.1081  47  THR   F O     
4326 C CB    . THR   F 47  ? 1.0221 0.8056 0.8239 -0.5188 -0.2002 0.0793  47  THR   F CB    
4327 O OG1   . THR   F 47  ? 0.9888 0.8018 0.8018 -0.4851 -0.1947 0.0750  47  THR   F OG1   
4328 C CG2   . THR   F 47  ? 1.0849 0.7759 0.8188 -0.5208 -0.2008 0.0585  47  THR   F CG2   
4329 N N     . VAL   F 48  ? 1.0652 0.8078 0.8816 -0.5449 -0.1699 0.1063  48  VAL   F N     
4330 C CA    . VAL   F 48  ? 1.1195 0.8283 0.9236 -0.5810 -0.1730 0.1144  48  VAL   F CA    
4331 C C     . VAL   F 48  ? 1.1867 0.7949 0.9224 -0.5815 -0.1755 0.0958  48  VAL   F C     
4332 O O     . VAL   F 48  ? 1.1410 0.7091 0.8530 -0.5484 -0.1603 0.0885  48  VAL   F O     
4333 C CB    . VAL   F 48  ? 1.0946 0.8356 0.9342 -0.5848 -0.1555 0.1357  48  VAL   F CB    
4334 C CG1   . VAL   F 48  ? 1.0476 0.8859 0.9550 -0.5937 -0.1558 0.1538  48  VAL   F CG1   
4335 C CG2   . VAL   F 48  ? 1.0640 0.7877 0.8950 -0.5458 -0.1327 0.1353  48  VAL   F CG2   
4336 N N     . PRO   F 49  ? 1.2678 0.8324 0.9693 -0.6166 -0.1954 0.0861  49  PRO   F N     
4337 C CA    . PRO   F 49  ? 1.3610 0.8255 0.9970 -0.6195 -0.1968 0.0685  49  PRO   F CA    
4338 C C     . PRO   F 49  ? 1.4153 0.8307 1.0371 -0.6234 -0.1838 0.0779  49  PRO   F C     
4339 O O     . PRO   F 49  ? 1.4608 0.9025 1.1099 -0.6531 -0.1846 0.0966  49  PRO   F O     
4340 C CB    . PRO   F 49  ? 1.4088 0.8481 1.0186 -0.6636 -0.2218 0.0596  49  PRO   F CB    
4341 C CG    . PRO   F 49  ? 1.3582 0.8894 1.0186 -0.6763 -0.2355 0.0702  49  PRO   F CG    
4342 C CD    . PRO   F 49  ? 1.2772 0.8855 0.9996 -0.6541 -0.2185 0.0906  49  PRO   F CD    
4343 N N     . HIS   F 50  ? 1.4539 0.8030 1.0365 -0.5924 -0.1713 0.0666  50  HIS   F N     
4344 C CA    . HIS   F 50  ? 1.5220 0.8051 1.0774 -0.5960 -0.1622 0.0729  50  HIS   F CA    
4345 C C     . HIS   F 50  ? 1.5816 0.7744 1.0790 -0.5720 -0.1592 0.0510  50  HIS   F C     
4346 O O     . HIS   F 50  ? 1.4803 0.6775 0.9774 -0.5294 -0.1480 0.0431  50  HIS   F O     
4347 C CB    . HIS   F 50  ? 1.5005 0.8262 1.0914 -0.5741 -0.1435 0.0930  50  HIS   F CB    
4348 C CG    . HIS   F 50  ? 1.5624 0.8501 1.1427 -0.5930 -0.1367 0.1100  50  HIS   F CG    
4349 N ND1   . HIS   F 50  ? 1.5753 0.9100 1.1906 -0.6282 -0.1375 0.1308  50  HIS   F ND1   
4350 C CD2   . HIS   F 50  ? 1.6240 0.8385 1.1672 -0.5816 -0.1284 0.1118  50  HIS   F CD2   
4351 C CE1   . HIS   F 50  ? 1.6393 0.9279 1.2358 -0.6397 -0.1295 0.1445  50  HIS   F CE1   
4352 N NE2   . HIS   F 50  ? 1.6686 0.8830 1.2208 -0.6112 -0.1246 0.1337  50  HIS   F NE2   
4353 N N     . LYS   F 51  ? 1.7274 0.8406 1.1780 -0.6001 -0.1691 0.0413  51  LYS   F N     
4354 C CA    . LYS   F 51  ? 1.8266 0.8447 1.2194 -0.5808 -0.1654 0.0207  51  LYS   F CA    
4355 C C     . LYS   F 51  ? 1.8877 0.8515 1.2667 -0.5727 -0.1535 0.0340  51  LYS   F C     
4356 O O     . LYS   F 51  ? 2.0056 0.9336 1.3726 -0.6090 -0.1591 0.0446  51  LYS   F O     
4357 C CB    . LYS   F 51  ? 1.8660 0.8238 1.2114 -0.6137 -0.1823 0.0002  51  LYS   F CB    
4358 N N     . GLN   F 52  ? 1.8449 0.8029 1.2253 -0.5260 -0.1381 0.0343  52  GLN   F N     
4359 C CA    . GLN   F 52  ? 1.8707 0.8120 1.2557 -0.5130 -0.1264 0.0542  52  GLN   F CA    
4360 C C     . GLN   F 52  ? 2.0126 0.8434 1.3436 -0.5130 -0.1256 0.0482  52  GLN   F C     
4361 O O     . GLN   F 52  ? 2.1046 0.8787 1.3989 -0.5007 -0.1274 0.0249  52  GLN   F O     
4362 C CB    . GLN   F 52  ? 1.7827 0.7718 1.1949 -0.4647 -0.1129 0.0578  52  GLN   F CB    
4363 C CG    . GLN   F 52  ? 1.6621 0.7480 1.1201 -0.4579 -0.1135 0.0568  52  GLN   F CG    
4364 C CD    . GLN   F 52  ? 1.5688 0.7146 1.0636 -0.4271 -0.1007 0.0707  52  GLN   F CD    
4365 O OE1   . GLN   F 52  ? 1.5628 0.6804 1.0462 -0.3944 -0.0915 0.0723  52  GLN   F OE1   
4366 N NE2   . GLN   F 52  ? 1.4745 0.7031 1.0139 -0.4385 -0.1007 0.0812  52  GLN   F NE2   
4367 N N     . GLY   F 53  ? 2.0431 0.8424 1.3685 -0.5241 -0.1214 0.0693  53  GLY   F N     
4368 C CA    . GLY   F 53  ? 2.1319 0.8248 1.4084 -0.5228 -0.1200 0.0684  53  GLY   F CA    
4369 C C     . GLY   F 53  ? 2.0873 0.7495 1.3527 -0.4678 -0.1082 0.0650  53  GLY   F C     
4370 O O     . GLY   F 53  ? 2.0927 0.7746 1.3630 -0.4357 -0.1049 0.0468  53  GLY   F O     
4371 N N     . SER   F 54  ? 2.0409 0.6507 1.2892 -0.4575 -0.1026 0.0822  54  SER   F N     
4372 C CA    . SER   F 54  ? 1.9266 0.5600 1.1917 -0.4129 -0.0925 0.0946  54  SER   F CA    
4373 C C     . SER   F 54  ? 1.9075 0.5751 1.1915 -0.4293 -0.0893 0.1258  54  SER   F C     
4374 O O     . SER   F 54  ? 1.9010 0.5572 1.1824 -0.4016 -0.0832 0.1411  54  SER   F O     
4375 C CB    . SER   F 54  ? 1.9503 0.5005 1.1813 -0.3744 -0.0880 0.0875  54  SER   F CB    
4376 O OG    . SER   F 54  ? 1.8667 0.4528 1.1197 -0.3313 -0.0807 0.0989  54  SER   F OG    
4377 N N     . ASP   F 55  ? 1.8945 0.6111 1.2003 -0.4727 -0.0929 0.1353  55  ASP   F N     
4378 C CA    . ASP   F 55  ? 1.8849 0.6643 1.2211 -0.4852 -0.0865 0.1618  55  ASP   F CA    
4379 C C     . ASP   F 55  ? 1.7506 0.6271 1.1309 -0.4579 -0.0807 0.1582  55  ASP   F C     
4380 O O     . ASP   F 55  ? 1.7078 0.6257 1.1071 -0.4600 -0.0853 0.1405  55  ASP   F O     
4381 C CB    . ASP   F 55  ? 1.9543 0.7404 1.2958 -0.5416 -0.0915 0.1734  55  ASP   F CB    
4382 C CG    . ASP   F 55  ? 1.9509 0.8010 1.3235 -0.5600 -0.0825 0.2012  55  ASP   F CG    
4383 O OD1   . ASP   F 55  ? 1.9165 0.8586 1.3331 -0.5565 -0.0785 0.2014  55  ASP   F OD1   
4384 O OD2   . ASP   F 55  ? 2.0009 0.8073 1.3528 -0.5772 -0.0787 0.2226  55  ASP   F OD2   
4385 N N     . TYR   F 56  ? 1.7030 0.6109 1.0961 -0.4322 -0.0714 0.1744  56  TYR   F N     
4386 C CA    . TYR   F 56  ? 1.6031 0.6024 1.0374 -0.4114 -0.0648 0.1744  56  TYR   F CA    
4387 C C     . TYR   F 56  ? 1.5753 0.6470 1.0455 -0.4476 -0.0626 0.1840  56  TYR   F C     
4388 O O     . TYR   F 56  ? 1.5732 0.6392 1.0402 -0.4766 -0.0588 0.2045  56  TYR   F O     
4389 C CB    . TYR   F 56  ? 1.5825 0.5898 1.0149 -0.3805 -0.0566 0.1905  56  TYR   F CB    
4390 C CG    . TYR   F 56  ? 1.5571 0.5493 0.9830 -0.3318 -0.0572 0.1785  56  TYR   F CG    
4391 C CD1   . TYR   F 56  ? 1.4910 0.5302 0.9420 -0.3099 -0.0576 0.1578  56  TYR   F CD1   
4392 C CD2   . TYR   F 56  ? 1.5810 0.5177 0.9791 -0.3072 -0.0573 0.1894  56  TYR   F CD2   
4393 C CE1   . TYR   F 56  ? 1.4523 0.4839 0.9020 -0.2671 -0.0573 0.1473  56  TYR   F CE1   
4394 C CE2   . TYR   F 56  ? 1.5746 0.5040 0.9727 -0.2629 -0.0585 0.1789  56  TYR   F CE2   
4395 C CZ    . TYR   F 56  ? 1.5120 0.4916 0.9375 -0.2433 -0.0578 0.1579  56  TYR   F CZ    
4396 O OH    . TYR   F 56  ? 1.4763 0.4554 0.9064 -0.2017 -0.0580 0.1477  56  TYR   F OH    
4397 N N     . VAL   F 57  ? 1.5224 0.6633 1.0280 -0.4444 -0.0641 0.1709  57  VAL   F N     
4398 C CA    . VAL   F 57  ? 1.5025 0.7144 1.0469 -0.4768 -0.0636 0.1783  57  VAL   F CA    
4399 C C     . VAL   F 57  ? 1.4404 0.7372 1.0251 -0.4526 -0.0528 0.1817  57  VAL   F C     
4400 O O     . VAL   F 57  ? 1.3855 0.6965 0.9753 -0.4181 -0.0529 0.1669  57  VAL   F O     
4401 C CB    . VAL   F 57  ? 1.5084 0.7260 1.0594 -0.5013 -0.0773 0.1619  57  VAL   F CB    
4402 C CG1   . VAL   F 57  ? 1.4946 0.7660 1.0792 -0.5448 -0.0792 0.1758  57  VAL   F CG1   
4403 C CG2   . VAL   F 57  ? 1.5855 0.7103 1.0888 -0.5108 -0.0884 0.1479  57  VAL   F CG2   
4404 N N     . LEU   F 58  ? 1.4111 0.7632 1.0243 -0.4716 -0.0428 0.2004  58  LEU   F N     
4405 C CA    . LEU   F 58  ? 1.3662 0.7940 1.0145 -0.4510 -0.0301 0.2050  58  LEU   F CA    
4406 C C     . LEU   F 58  ? 1.3100 0.7992 0.9968 -0.4468 -0.0353 0.1904  58  LEU   F C     
4407 O O     . LEU   F 58  ? 1.3562 0.8768 1.0674 -0.4776 -0.0408 0.1930  58  LEU   F O     
4408 C CB    . LEU   F 58  ? 1.3713 0.8357 1.0363 -0.4743 -0.0161 0.2286  58  LEU   F CB    
4409 C CG    . LEU   F 58  ? 1.3120 0.8481 1.0074 -0.4539 0.0004  0.2343  58  LEU   F CG    
4410 C CD1   . LEU   F 58  ? 1.3234 0.8327 0.9894 -0.4198 0.0068  0.2358  58  LEU   F CD1   
4411 C CD2   . LEU   F 58  ? 1.3188 0.9046 1.0415 -0.4833 0.0146  0.2544  58  LEU   F CD2   
4412 N N     . VAL   F 59  ? 1.2604 0.7651 0.9520 -0.4095 -0.0346 0.1759  59  VAL   F N     
4413 C CA    . VAL   F 59  ? 1.1711 0.7306 0.8960 -0.4006 -0.0388 0.1629  59  VAL   F CA    
4414 C C     . VAL   F 59  ? 1.0595 0.6932 0.8232 -0.3858 -0.0249 0.1699  59  VAL   F C     
4415 O O     . VAL   F 59  ? 1.0225 0.7143 0.8244 -0.3947 -0.0258 0.1696  59  VAL   F O     
4416 C CB    . VAL   F 59  ? 1.1719 0.6998 0.8778 -0.3739 -0.0475 0.1415  59  VAL   F CB    
4417 C CG1   . VAL   F 59  ? 1.2379 0.7046 0.9124 -0.3955 -0.0612 0.1325  59  VAL   F CG1   
4418 C CG2   . VAL   F 59  ? 1.1712 0.6718 0.8570 -0.3363 -0.0412 0.1377  59  VAL   F CG2   
4419 N N     . ALA   F 60  ? 1.0245 0.6547 0.7774 -0.3643 -0.0129 0.1762  60  ALA   F N     
4420 C CA    . ALA   F 60  ? 0.9616 0.6545 0.7445 -0.3523 0.0024  0.1830  60  ALA   F CA    
4421 C C     . ALA   F 60  ? 0.9508 0.6270 0.7115 -0.3512 0.0151  0.1984  60  ALA   F C     
4422 O O     . ALA   F 60  ? 0.9678 0.5828 0.6890 -0.3476 0.0106  0.2013  60  ALA   F O     
4423 C CB    . ALA   F 60  ? 0.9091 0.6263 0.7042 -0.3170 0.0024  0.1673  60  ALA   F CB    
4424 N N     . GLY   F 61  ? 0.9185 0.6493 0.7041 -0.3527 0.0315  0.2082  61  GLY   F N     
4425 C CA    . GLY   F 61  ? 0.9502 0.6722 0.7130 -0.3475 0.0454  0.2213  61  GLY   F CA    
4426 C C     . GLY   F 61  ? 0.9300 0.7173 0.7246 -0.3547 0.0656  0.2312  61  GLY   F C     
4427 O O     . GLY   F 61  ? 0.9066 0.7423 0.7426 -0.3701 0.0681  0.2323  61  GLY   F O     
4428 N N     . LEU   F 62  ? 0.9503 0.7390 0.7250 -0.3424 0.0800  0.2383  62  LEU   F N     
4429 C CA    . LEU   F 62  ? 0.9455 0.7890 0.7426 -0.3490 0.1029  0.2483  62  LEU   F CA    
4430 C C     . LEU   F 62  ? 0.9869 0.8281 0.7844 -0.3865 0.1108  0.2690  62  LEU   F C     
4431 O O     . LEU   F 62  ? 1.0037 0.7875 0.7642 -0.4011 0.1030  0.2787  62  LEU   F O     
4432 C CB    . LEU   F 62  ? 0.9605 0.8027 0.7303 -0.3249 0.1153  0.2475  62  LEU   F CB    
4433 C CG    . LEU   F 62  ? 0.9122 0.7781 0.6955 -0.2918 0.1134  0.2279  62  LEU   F CG    
4434 C CD1   . LEU   F 62  ? 0.9378 0.7815 0.6811 -0.2691 0.1167  0.2256  62  LEU   F CD1   
4435 C CD2   . LEU   F 62  ? 0.8756 0.8105 0.7079 -0.2901 0.1293  0.2242  62  LEU   F CD2   
4436 N N     . ALA   F 63  ? 0.9720 0.8770 0.8144 -0.4016 0.1264  0.2760  63  ALA   F N     
4437 C CA    . ALA   F 63  ? 1.0005 0.9196 0.8550 -0.4384 0.1370  0.2964  63  ALA   F CA    
4438 C C     . ALA   F 63  ? 1.0420 0.9453 0.8599 -0.4425 0.1572  0.3125  63  ALA   F C     
4439 O O     . ALA   F 63  ? 1.0242 0.9699 0.8517 -0.4295 0.1793  0.3134  63  ALA   F O     
4440 C CB    . ALA   F 63  ? 0.9619 0.9614 0.8805 -0.4477 0.1485  0.2985  63  ALA   F CB    
4441 N N     . GLY   F 64  ? 1.0948 0.9353 0.8686 -0.4604 0.1502  0.3254  64  GLY   F N     
4442 C CA    . GLY   F 64  ? 1.1444 0.9598 0.8745 -0.4640 0.1662  0.3421  64  GLY   F CA    
4443 C C     . GLY   F 64  ? 1.1218 0.9142 0.8118 -0.4278 0.1661  0.3329  64  GLY   F C     
4444 O O     . GLY   F 64  ? 1.1402 0.9396 0.8056 -0.4253 0.1852  0.3431  64  GLY   F O     
4445 N N     . ASP   F 65  ? 1.0812 0.8502 0.7655 -0.4006 0.1456  0.3138  65  ASP   F N     
4446 C CA    . ASP   F 65  ? 1.0911 0.8170 0.7289 -0.3729 0.1373  0.3092  65  ASP   F CA    
4447 C C     . ASP   F 65  ? 1.0801 0.7609 0.7114 -0.3585 0.1104  0.2954  65  ASP   F C     
4448 O O     . ASP   F 65  ? 1.0440 0.7345 0.6828 -0.3296 0.1023  0.2773  65  ASP   F O     
4449 C CB    . ASP   F 65  ? 1.0665 0.8338 0.7067 -0.3473 0.1516  0.2993  65  ASP   F CB    
4450 C CG    . ASP   F 65  ? 1.0887 0.8199 0.6777 -0.3240 0.1468  0.2989  65  ASP   F CG    
4451 O OD1   . ASP   F 65  ? 1.1133 0.7848 0.6637 -0.3238 0.1309  0.3075  65  ASP   F OD1   
4452 O OD2   . ASP   F 65  ? 1.0777 0.8408 0.6659 -0.3057 0.1584  0.2898  65  ASP   F OD2   
4453 N N     . PRO   F 66  ? 1.1182 0.7473 0.7346 -0.3782 0.0971  0.3031  66  PRO   F N     
4454 C CA    . PRO   F 66  ? 1.1152 0.6980 0.7228 -0.3643 0.0742  0.2894  66  PRO   F CA    
4455 C C     . PRO   F 66  ? 1.1414 0.6810 0.7109 -0.3324 0.0634  0.2857  66  PRO   F C     
4456 O O     . PRO   F 66  ? 1.1290 0.6476 0.7007 -0.3124 0.0478  0.2701  66  PRO   F O     
4457 C CB    . PRO   F 66  ? 1.1710 0.7062 0.7661 -0.3970 0.0670  0.3015  66  PRO   F CB    
4458 C CG    . PRO   F 66  ? 1.1797 0.7504 0.7894 -0.4303 0.0859  0.3203  66  PRO   F CG    
4459 C CD    . PRO   F 66  ? 1.1688 0.7733 0.7697 -0.4138 0.1038  0.3256  66  PRO   F CD    
4460 N N     . ASN   F 67  ? 1.1886 0.7138 0.7225 -0.3288 0.0711  0.3012  67  ASN   F N     
4461 C CA    . ASN   F 67  ? 1.2037 0.7002 0.7052 -0.2980 0.0609  0.2991  67  ASN   F CA    
4462 C C     . ASN   F 67  ? 1.1312 0.6744 0.6559 -0.2692 0.0607  0.2786  67  ASN   F C     
4463 O O     . ASN   F 67  ? 1.1107 0.6326 0.6249 -0.2426 0.0459  0.2695  67  ASN   F O     
4464 C CB    . ASN   F 67  ? 1.2561 0.7302 0.7120 -0.3019 0.0682  0.3211  67  ASN   F CB    
4465 C CG    . ASN   F 67  ? 1.3406 0.7389 0.7553 -0.3000 0.0524  0.3352  67  ASN   F CG    
4466 O OD1   . ASN   F 67  ? 1.3917 0.7525 0.7958 -0.3259 0.0528  0.3491  67  ASN   F OD1   
4467 N ND2   . ASN   F 67  ? 1.3376 0.7125 0.7298 -0.2699 0.0383  0.3327  67  ASN   F ND2   
4468 N N     . ARG   F 68  ? 1.0994 0.7044 0.6541 -0.2740 0.0778  0.2728  68  ARG   F N     
4469 C CA    . ARG   F 68  ? 1.0465 0.6947 0.6235 -0.2491 0.0794  0.2538  68  ARG   F CA    
4470 C C     . ARG   F 68  ? 0.9980 0.6506 0.6081 -0.2389 0.0657  0.2352  68  ARG   F C     
4471 O O     . ARG   F 68  ? 0.9629 0.6115 0.5722 -0.2130 0.0548  0.2220  68  ARG   F O     
4472 C CB    . ARG   F 68  ? 1.0499 0.7588 0.6501 -0.2554 0.1026  0.2525  68  ARG   F CB    
4473 C CG    . ARG   F 68  ? 1.0075 0.7600 0.6311 -0.2317 0.1067  0.2329  68  ARG   F CG    
4474 C CD    . ARG   F 68  ? 1.0346 0.7686 0.6225 -0.2075 0.0992  0.2281  68  ARG   F CD    
4475 N NE    . ARG   F 68  ? 0.9836 0.7544 0.5928 -0.1864 0.1018  0.2085  68  ARG   F NE    
4476 C CZ    . ARG   F 68  ? 1.0013 0.7683 0.5860 -0.1671 0.0974  0.2014  68  ARG   F CZ    
4477 N NH1   . ARG   F 68  ? 1.0479 0.7763 0.5873 -0.1631 0.0868  0.2120  68  ARG   F NH1   
4478 N NH2   . ARG   F 68  ? 0.9609 0.7618 0.5663 -0.1521 0.1026  0.1839  68  ARG   F NH2   
4479 N N     . PHE   F 69  ? 0.9785 0.6401 0.6159 -0.2601 0.0660  0.2349  69  PHE   F N     
4480 C CA    . PHE   F 69  ? 0.9412 0.5990 0.6019 -0.2532 0.0519  0.2187  69  PHE   F CA    
4481 C C     . PHE   F 69  ? 0.9694 0.6046 0.6352 -0.2819 0.0466  0.2246  69  PHE   F C     
4482 O O     . PHE   F 69  ? 0.9686 0.6349 0.6547 -0.3073 0.0573  0.2337  69  PHE   F O     
4483 C CB    . PHE   F 69  ? 0.8749 0.5898 0.5777 -0.2410 0.0560  0.2022  69  PHE   F CB    
4484 C CG    . PHE   F 69  ? 0.8456 0.5522 0.5670 -0.2387 0.0415  0.1881  69  PHE   F CG    
4485 C CD1   . PHE   F 69  ? 0.8412 0.5058 0.5435 -0.2190 0.0269  0.1786  69  PHE   F CD1   
4486 C CD2   . PHE   F 69  ? 0.8230 0.5607 0.5783 -0.2578 0.0422  0.1861  69  PHE   F CD2   
4487 C CE1   . PHE   F 69  ? 0.8237 0.4765 0.5373 -0.2178 0.0155  0.1657  69  PHE   F CE1   
4488 C CE2   . PHE   F 69  ? 0.8057 0.5313 0.5707 -0.2573 0.0282  0.1736  69  PHE   F CE2   
4489 C CZ    . PHE   F 69  ? 0.8139 0.4954 0.5560 -0.2376 0.0160  0.1630  69  PHE   F CZ    
4490 N N     . SER   F 70  ? 0.9974 0.5803 0.6461 -0.2766 0.0301  0.2181  70  SER   F N     
4491 C CA    . SER   F 70  ? 1.0239 0.5792 0.6752 -0.2999 0.0212  0.2170  70  SER   F CA    
4492 C C     . SER   F 70  ? 1.0156 0.5339 0.6592 -0.2809 0.0057  0.1995  70  SER   F C     
4493 O O     . SER   F 70  ? 1.0142 0.5097 0.6405 -0.2523 0.0009  0.1946  70  SER   F O     
4494 C CB    . SER   F 70  ? 1.0860 0.5936 0.7067 -0.3250 0.0222  0.2363  70  SER   F CB    
4495 O OG    . SER   F 70  ? 1.1032 0.6528 0.7403 -0.3495 0.0375  0.2508  70  SER   F OG    
4496 N N     . ALA   F 71  ? 1.0030 0.5164 0.6590 -0.2977 -0.0019 0.1906  71  ALA   F N     
4497 C CA    . ALA   F 71  ? 1.0174 0.4960 0.6647 -0.2834 -0.0144 0.1729  71  ALA   F CA    
4498 C C     . ALA   F 71  ? 1.0717 0.5028 0.7025 -0.3122 -0.0231 0.1729  71  ALA   F C     
4499 O O     . ALA   F 71  ? 1.0660 0.5242 0.7157 -0.3428 -0.0225 0.1776  71  ALA   F O     
4500 C CB    . ALA   F 71  ? 0.9480 0.4790 0.6288 -0.2696 -0.0151 0.1565  71  ALA   F CB    
4501 N N     . TYR   F 72  ? 1.1300 0.4920 0.7274 -0.3016 -0.0314 0.1668  72  TYR   F N     
4502 C CA    . TYR   F 72  ? 1.2335 0.5358 0.8063 -0.3267 -0.0397 0.1653  72  TYR   F CA    
4503 C C     . TYR   F 72  ? 1.2415 0.5069 0.8008 -0.3073 -0.0481 0.1432  72  TYR   F C     
4504 O O     . TYR   F 72  ? 1.1904 0.4557 0.7493 -0.2715 -0.0468 0.1350  72  TYR   F O     
4505 C CB    . TYR   F 72  ? 1.3287 0.5648 0.8648 -0.3377 -0.0396 0.1825  72  TYR   F CB    
4506 C CG    . TYR   F 72  ? 1.3742 0.6384 0.9152 -0.3530 -0.0291 0.2062  72  TYR   F CG    
4507 C CD1   . TYR   F 72  ? 1.3988 0.6859 0.9396 -0.3267 -0.0218 0.2143  72  TYR   F CD1   
4508 C CD2   . TYR   F 72  ? 1.4100 0.6823 0.9568 -0.3941 -0.0259 0.2201  72  TYR   F CD2   
4509 C CE1   . TYR   F 72  ? 1.4138 0.7273 0.9553 -0.3397 -0.0105 0.2347  72  TYR   F CE1   
4510 C CE2   . TYR   F 72  ? 1.4347 0.7361 0.9864 -0.4071 -0.0134 0.2415  72  TYR   F CE2   
4511 C CZ    . TYR   F 72  ? 1.4357 0.7560 0.9824 -0.3795 -0.0050 0.2485  72  TYR   F CZ    
4512 O OH    . TYR   F 72  ? 1.3995 0.7472 0.9459 -0.3904 0.0087  0.2685  72  TYR   F OH    
4513 N N     . THR   F 73  ? 1.2903 0.5222 0.8365 -0.3328 -0.0562 0.1345  73  THR   F N     
4514 C CA    . THR   F 73  ? 1.3107 0.5033 0.8389 -0.3212 -0.0631 0.1125  73  THR   F CA    
4515 C C     . THR   F 73  ? 1.3986 0.5072 0.8862 -0.3442 -0.0698 0.1113  73  THR   F C     
4516 O O     . THR   F 73  ? 1.4103 0.5119 0.8951 -0.3824 -0.0731 0.1223  73  THR   F O     
4517 C CB    . THR   F 73  ? 1.2685 0.5161 0.8233 -0.3290 -0.0671 0.0986  73  THR   F CB    
4518 O OG1   . THR   F 73  ? 1.3124 0.5142 0.8422 -0.3156 -0.0718 0.0775  73  THR   F OG1   
4519 C CG2   . THR   F 73  ? 1.2621 0.5407 0.8336 -0.3720 -0.0723 0.1069  73  THR   F CG2   
4520 N N     . ARG   F 74  ? 1.4241 0.4713 0.8825 -0.3193 -0.0709 0.0972  74  ARG   F N     
4521 C CA    . ARG   F 74  ? 1.5278 0.4845 0.9431 -0.3304 -0.0758 0.0909  74  ARG   F CA    
4522 C C     . ARG   F 74  ? 1.5415 0.4786 0.9437 -0.3185 -0.0785 0.0636  74  ARG   F C     
4523 O O     . ARG   F 74  ? 1.4473 0.4273 0.8696 -0.2890 -0.0743 0.0532  74  ARG   F O     
4524 C CB    . ARG   F 74  ? 1.5603 0.4572 0.9516 -0.3020 -0.0716 0.1003  74  ARG   F CB    
4525 C CG    . ARG   F 74  ? 1.6153 0.4592 0.9822 -0.3276 -0.0731 0.1211  74  ARG   F CG    
4526 C CD    . ARG   F 74  ? 1.6430 0.4320 0.9876 -0.2986 -0.0702 0.1348  74  ARG   F CD    
4527 N NE    . ARG   F 74  ? 1.6135 0.3961 0.9602 -0.2490 -0.0674 0.1263  74  ARG   F NE    
4528 C CZ    . ARG   F 74  ? 1.6428 0.3552 0.9639 -0.2224 -0.0673 0.1158  74  ARG   F CZ    
4529 N NH1   . ARG   F 74  ? 1.6227 0.3355 0.9505 -0.1797 -0.0650 0.1200  74  ARG   F NH1   
4530 N NH2   . ARG   F 74  ? 1.7022 0.3419 0.9903 -0.2387 -0.0698 0.1027  74  ARG   F NH2   
4531 N N     . SER   F 75  ? 1.6071 0.4750 0.9724 -0.3414 -0.0849 0.0524  75  SER   F N     
4532 C CA    . SER   F 75  ? 1.6508 0.4715 0.9875 -0.3270 -0.0852 0.0262  75  SER   F CA    
4533 C C     . SER   F 75  ? 1.7491 0.4703 1.0438 -0.3130 -0.0821 0.0243  75  SER   F C     
4534 O O     . SER   F 75  ? 1.7639 0.4399 1.0412 -0.3353 -0.0852 0.0396  75  SER   F O     
4535 C CB    . SER   F 75  ? 1.6644 0.4896 0.9915 -0.3649 -0.0956 0.0128  75  SER   F CB    
4536 O OG    . SER   F 75  ? 1.7237 0.4999 1.0170 -0.3524 -0.0949 -0.0138 75  SER   F OG    
4537 N N     . GLN   F 76  ? 1.7826 0.4724 1.0637 -0.2743 -0.0748 0.0069  76  GLN   F N     
4538 C CA    . GLN   F 76  ? 1.8365 0.4388 1.0850 -0.2491 -0.0694 0.0049  76  GLN   F CA    
4539 C C     . GLN   F 76  ? 1.9103 0.4346 1.1129 -0.2562 -0.0692 -0.0219 76  GLN   F C     
4540 O O     . GLN   F 76  ? 2.0308 0.4702 1.1955 -0.2705 -0.0715 -0.0214 76  GLN   F O     
4541 C CB    . GLN   F 76  ? 1.7795 0.4183 1.0552 -0.1979 -0.0601 0.0064  76  GLN   F CB    
4542 C CG    . GLN   F 76  ? 1.8156 0.3879 1.0744 -0.1635 -0.0549 0.0132  76  GLN   F CG    
4543 C CD    . GLN   F 76  ? 1.7872 0.3814 1.0646 -0.1142 -0.0453 0.0015  76  GLN   F CD    
4544 O OE1   . GLN   F 76  ? 1.8606 0.4037 1.1154 -0.0950 -0.0380 -0.0192 76  GLN   F OE1   
4545 N NE2   . GLN   F 76  ? 1.6894 0.3647 1.0089 -0.0963 -0.0445 0.0122  76  GLN   F NE2   
4546 N N     . GLY   F 77  ? 1.9109 0.4622 1.1147 -0.2472 -0.0662 -0.0450 77  GLY   F N     
4547 C CA    . GLY   F 77  ? 1.9933 0.4771 1.1530 -0.2444 -0.0624 -0.0738 77  GLY   F CA    
4548 C C     . GLY   F 77  ? 1.9950 0.4961 1.1650 -0.1956 -0.0480 -0.0895 77  GLY   F C     
4549 O O     . GLY   F 77  ? 1.9288 0.4784 1.1369 -0.1622 -0.0419 -0.0763 77  GLY   F O     
4550 N N     . GLY   F 78  ? 2.0725 0.5332 1.2070 -0.1933 -0.0425 -0.1179 78  GLY   F N     
4551 C CA    . GLY   F 78  ? 2.0903 0.5638 1.2300 -0.1508 -0.0268 -0.1355 78  GLY   F CA    
4552 C C     . GLY   F 78  ? 1.9946 0.5726 1.1776 -0.1453 -0.0266 -0.1335 78  GLY   F C     
4553 O O     . GLY   F 78  ? 1.9463 0.5814 1.1488 -0.1774 -0.0392 -0.1230 78  GLY   F O     
4554 N N     . SER   F 79  ? 1.9878 0.5898 1.1869 -0.1040 -0.0115 -0.1434 79  SER   F N     
4555 C CA    . SER   F 79  ? 1.9412 0.6375 1.1823 -0.0937 -0.0092 -0.1410 79  SER   F CA    
4556 C C     . SER   F 79  ? 1.8404 0.5982 1.1337 -0.0795 -0.0126 -0.1141 79  SER   F C     
4557 O O     . SER   F 79  ? 1.8746 0.6010 1.1720 -0.0613 -0.0111 -0.1015 79  SER   F O     
4558 C CB    . SER   F 79  ? 1.9853 0.6832 1.2209 -0.0602 0.0086  -0.1625 79  SER   F CB    
4559 O OG    . SER   F 79  ? 2.0034 0.7295 1.2764 -0.0152 0.0210  -0.1554 79  SER   F OG    
4560 N N     . LYS   F 80  ? 1.6979 0.5416 1.0288 -0.0885 -0.0177 -0.1052 80  LYS   F N     
4561 C CA    . LYS   F 80  ? 1.5916 0.4965 0.9670 -0.0854 -0.0230 -0.0808 80  LYS   F CA    
4562 C C     . LYS   F 80  ? 1.6150 0.4874 0.9806 -0.1099 -0.0333 -0.0623 80  LYS   F C     
4563 O O     . LYS   F 80  ? 1.5720 0.4423 0.9521 -0.0926 -0.0327 -0.0453 80  LYS   F O     
4564 C CB    . LYS   F 80  ? 1.5274 0.4613 0.9342 -0.0397 -0.0119 -0.0781 80  LYS   F CB    
4565 C CG    . LYS   F 80  ? 1.4407 0.4470 0.8795 -0.0240 -0.0051 -0.0852 80  LYS   F CG    
4566 C CD    . LYS   F 80  ? 1.4540 0.4441 0.8784 -0.0019 0.0093  -0.1080 80  LYS   F CD    
4567 C CE    . LYS   F 80  ? 1.4887 0.4377 0.9106 0.0380  0.0224  -0.1136 80  LYS   F CE    
4568 N NZ    . LYS   F 80  ? 1.4295 0.4238 0.8967 0.0699  0.0249  -0.0990 80  LYS   F NZ    
4569 N N     . PRO   F 81  ? 1.6649 0.5154 1.0069 -0.1525 -0.0437 -0.0633 81  PRO   F N     
4570 C CA    . PRO   F 81  ? 1.7122 0.5186 1.0380 -0.1779 -0.0517 -0.0476 81  PRO   F CA    
4571 C C     . PRO   F 81  ? 1.6481 0.5109 1.0080 -0.1939 -0.0579 -0.0212 81  PRO   F C     
4572 O O     . PRO   F 81  ? 1.6854 0.5116 1.0317 -0.2144 -0.0629 -0.0066 81  PRO   F O     
4573 C CB    . PRO   F 81  ? 1.7693 0.5380 1.0594 -0.2187 -0.0605 -0.0614 81  PRO   F CB    
4574 C CG    . PRO   F 81  ? 1.7000 0.5446 1.0135 -0.2254 -0.0629 -0.0695 81  PRO   F CG    
4575 C CD    . PRO   F 81  ? 1.6483 0.5181 0.9789 -0.1805 -0.0495 -0.0780 81  PRO   F CD    
4576 N N     . LEU   F 82  ? 1.5707 0.5194 0.9724 -0.1866 -0.0569 -0.0153 82  LEU   F N     
4577 C CA    . LEU   F 82  ? 1.4981 0.5058 0.9311 -0.2050 -0.0612 0.0062  82  LEU   F CA    
4578 C C     . LEU   F 82  ? 1.4568 0.4678 0.9030 -0.1777 -0.0565 0.0235  82  LEU   F C     
4579 O O     . LEU   F 82  ? 1.4360 0.4491 0.8899 -0.1406 -0.0503 0.0180  82  LEU   F O     
4580 C CB    . LEU   F 82  ? 1.4331 0.5229 0.9002 -0.2084 -0.0619 0.0019  82  LEU   F CB    
4581 C CG    . LEU   F 82  ? 1.4256 0.5788 0.9224 -0.2384 -0.0675 0.0169  82  LEU   F CG    
4582 C CD1   . LEU   F 82  ? 1.3557 0.5625 0.8867 -0.2209 -0.0616 0.0339  82  LEU   F CD1   
4583 C CD2   . LEU   F 82  ? 1.4487 0.5725 0.9288 -0.2808 -0.0760 0.0256  82  LEU   F CD2   
4584 N N     . VAL   F 83  ? 1.4407 0.4455 0.8856 -0.1973 -0.0597 0.0444  83  VAL   F N     
4585 C CA    . VAL   F 83  ? 1.4048 0.4119 0.8570 -0.1778 -0.0572 0.0639  83  VAL   F CA    
4586 C C     . VAL   F 83  ? 1.3170 0.3922 0.7974 -0.1981 -0.0573 0.0810  83  VAL   F C     
4587 O O     . VAL   F 83  ? 1.3084 0.3938 0.7896 -0.2347 -0.0605 0.0846  83  VAL   F O     
4588 C CB    . VAL   F 83  ? 1.4875 0.4107 0.9034 -0.1809 -0.0593 0.0748  83  VAL   F CB    
4589 C CG1   . VAL   F 83  ? 1.4846 0.4073 0.9054 -0.1520 -0.0578 0.0930  83  VAL   F CG1   
4590 C CG2   . VAL   F 83  ? 1.5475 0.3919 0.9290 -0.1727 -0.0589 0.0563  83  VAL   F CG2   
4591 N N     . VAL   F 84  ? 1.2345 0.3557 0.7378 -0.1751 -0.0536 0.0911  84  VAL   F N     
4592 C CA    . VAL   F 84  ? 1.1547 0.3455 0.6863 -0.1889 -0.0508 0.1034  84  VAL   F CA    
4593 C C     . VAL   F 84  ? 1.1414 0.3304 0.6681 -0.1786 -0.0489 0.1241  84  VAL   F C     
4594 O O     . VAL   F 84  ? 1.1272 0.3002 0.6490 -0.1467 -0.0498 0.1245  84  VAL   F O     
4595 C CB    . VAL   F 84  ? 1.0819 0.3428 0.6484 -0.1735 -0.0478 0.0912  84  VAL   F CB    
4596 C CG1   . VAL   F 84  ? 1.0222 0.3523 0.6179 -0.1828 -0.0432 0.1031  84  VAL   F CG1   
4597 C CG2   . VAL   F 84  ? 1.0700 0.3327 0.6379 -0.1849 -0.0505 0.0724  84  VAL   F CG2   
4598 N N     . LYS   F 85  ? 1.1381 0.3517 0.6693 -0.2053 -0.0458 0.1407  85  LYS   F N     
4599 C CA    . LYS   F 85  ? 1.1475 0.3701 0.6735 -0.2006 -0.0424 0.1611  85  LYS   F CA    
4600 C C     . LYS   F 85  ? 1.0799 0.3823 0.6381 -0.2062 -0.0349 0.1635  85  LYS   F C     
4601 O O     . LYS   F 85  ? 1.0614 0.3937 0.6360 -0.2337 -0.0318 0.1632  85  LYS   F O     
4602 C CB    . LYS   F 85  ? 1.2115 0.3826 0.7077 -0.2279 -0.0428 0.1803  85  LYS   F CB    
4603 C CG    . LYS   F 85  ? 1.2347 0.3926 0.7120 -0.2184 -0.0411 0.2024  85  LYS   F CG    
4604 C CD    . LYS   F 85  ? 1.2968 0.4074 0.7444 -0.2468 -0.0399 0.2246  85  LYS   F CD    
4605 C CE    . LYS   F 85  ? 1.3736 0.3956 0.7842 -0.2389 -0.0476 0.2303  85  LYS   F CE    
4606 N NZ    . LYS   F 85  ? 1.4368 0.4092 0.8194 -0.2727 -0.0464 0.2500  85  LYS   F NZ    
4607 N N     . LEU   F 86  ? 1.0490 0.3836 0.6161 -0.1805 -0.0326 0.1657  86  LEU   F N     
4608 C CA    . LEU   F 86  ? 0.9965 0.4004 0.5898 -0.1805 -0.0245 0.1670  86  LEU   F CA    
4609 C C     . LEU   F 86  ? 1.0051 0.4084 0.5802 -0.1758 -0.0211 0.1852  86  LEU   F C     
4610 O O     . LEU   F 86  ? 1.0044 0.3891 0.5664 -0.1498 -0.0273 0.1865  86  LEU   F O     
4611 C CB    . LEU   F 86  ? 0.9554 0.3985 0.5740 -0.1529 -0.0257 0.1495  86  LEU   F CB    
4612 C CG    . LEU   F 86  ? 0.9377 0.3905 0.5749 -0.1539 -0.0281 0.1308  86  LEU   F CG    
4613 C CD1   . LEU   F 86  ? 0.8809 0.3698 0.5402 -0.1262 -0.0281 0.1171  86  LEU   F CD1   
4614 C CD2   . LEU   F 86  ? 0.9386 0.4255 0.5943 -0.1843 -0.0237 0.1323  86  LEU   F CD2   
4615 N N     . VAL   F 87  ? 1.0072 0.4371 0.5842 -0.1994 -0.0109 0.1982  87  VAL   F N     
4616 C CA    . VAL   F 87  ? 1.0284 0.4585 0.5834 -0.1987 -0.0055 0.2162  87  VAL   F CA    
4617 C C     . VAL   F 87  ? 0.9648 0.4627 0.5444 -0.1913 0.0046  0.2099  87  VAL   F C     
4618 O O     . VAL   F 87  ? 0.9312 0.4707 0.5383 -0.2079 0.0140  0.2059  87  VAL   F O     
4619 C CB    . VAL   F 87  ? 1.0917 0.4896 0.6205 -0.2284 -0.0001 0.2384  87  VAL   F CB    
4620 C CG1   . VAL   F 87  ? 1.1090 0.4862 0.6442 -0.2583 -0.0008 0.2379  87  VAL   F CG1   
4621 C CG2   . VAL   F 87  ? 1.0915 0.5247 0.6146 -0.2408 0.0146  0.2537  87  VAL   F CG2   
4622 N N     . ASN   F 88  ? 0.9536 0.4600 0.5231 -0.1667 0.0017  0.2092  88  ASN   F N     
4623 C CA    . ASN   F 88  ? 0.9163 0.4767 0.4998 -0.1583 0.0107  0.2036  88  ASN   F CA    
4624 C C     . ASN   F 88  ? 0.9589 0.5090 0.5067 -0.1543 0.0124  0.2188  88  ASN   F C     
4625 O O     . ASN   F 88  ? 0.9667 0.4894 0.4936 -0.1347 -0.0007 0.2218  88  ASN   F O     
4626 C CB    . ASN   F 88  ? 0.8731 0.4573 0.4804 -0.1320 0.0035  0.1839  88  ASN   F CB    
4627 C CG    . ASN   F 88  ? 0.8379 0.4279 0.4746 -0.1335 0.0005  0.1690  88  ASN   F CG    
4628 O OD1   . ASN   F 88  ? 0.8513 0.4111 0.4853 -0.1192 -0.0107 0.1621  88  ASN   F OD1   
4629 N ND2   . ASN   F 88  ? 0.8053 0.4304 0.4675 -0.1512 0.0102  0.1656  88  ASN   F ND2   
4630 N N     . ASP   F 89  ? 0.9877 0.5610 0.5286 -0.1732 0.0288  0.2292  89  ASP   F N     
4631 C CA    . ASP   F 89  ? 1.0514 0.6187 0.5546 -0.1740 0.0340  0.2441  89  ASP   F CA    
4632 C C     . ASP   F 89  ? 1.1168 0.6227 0.5795 -0.1728 0.0206  0.2623  89  ASP   F C     
4633 O O     . ASP   F 89  ? 1.1311 0.6214 0.5692 -0.1534 0.0088  0.2659  89  ASP   F O     
4634 C CB    . ASP   F 89  ? 1.0312 0.6334 0.5353 -0.1538 0.0349  0.2321  89  ASP   F CB    
4635 C CG    . ASP   F 89  ? 1.0956 0.7018 0.5610 -0.1581 0.0445  0.2443  89  ASP   F CG    
4636 O OD1   . ASP   F 89  ? 1.1549 0.7708 0.6125 -0.1800 0.0630  0.2556  89  ASP   F OD1   
4637 O OD2   . ASP   F 89  ? 1.0978 0.6986 0.5401 -0.1404 0.0337  0.2426  89  ASP   F OD2   
4638 N N     . GLY   F 90  ? 1.1566 0.6264 0.6157 -0.1920 0.0201  0.2724  90  GLY   F N     
4639 C CA    . GLY   F 90  ? 1.2315 0.6365 0.6534 -0.1931 0.0087  0.2907  90  GLY   F CA    
4640 C C     . GLY   F 90  ? 1.2418 0.6109 0.6607 -0.1643 -0.0119 0.2843  90  GLY   F C     
4641 O O     . GLY   F 90  ? 1.2896 0.6054 0.6765 -0.1608 -0.0218 0.3008  90  GLY   F O     
4642 N N     . VAL   F 91  ? 1.2087 0.6052 0.6616 -0.1446 -0.0175 0.2618  91  VAL   F N     
4643 C CA    . VAL   F 91  ? 1.2107 0.5801 0.6680 -0.1169 -0.0342 0.2538  91  VAL   F CA    
4644 C C     . VAL   F 91  ? 1.1857 0.5408 0.6664 -0.1235 -0.0338 0.2399  91  VAL   F C     
4645 O O     . VAL   F 91  ? 1.1527 0.5511 0.6655 -0.1287 -0.0266 0.2235  91  VAL   F O     
4646 C CB    . VAL   F 91  ? 1.1544 0.5644 0.6301 -0.0898 -0.0408 0.2397  91  VAL   F CB    
4647 C CG1   . VAL   F 91  ? 1.1558 0.5403 0.6411 -0.0618 -0.0564 0.2324  91  VAL   F CG1   
4648 C CG2   . VAL   F 91  ? 1.1673 0.5916 0.6156 -0.0863 -0.0419 0.2520  91  VAL   F CG2   
4649 N N     . THR   F 92  ? 1.2255 0.5188 0.6885 -0.1215 -0.0422 0.2461  92  THR   F N     
4650 C CA    . THR   F 92  ? 1.2151 0.4821 0.6897 -0.1300 -0.0426 0.2338  92  THR   F CA    
4651 C C     . THR   F 92  ? 1.1731 0.4383 0.6663 -0.0987 -0.0512 0.2154  92  THR   F C     
4652 O O     . THR   F 92  ? 1.1758 0.4171 0.6577 -0.0731 -0.0609 0.2213  92  THR   F O     
4653 C CB    . THR   F 92  ? 1.2946 0.4895 0.7356 -0.1450 -0.0458 0.2502  92  THR   F CB    
4654 O OG1   . THR   F 92  ? 1.3166 0.5194 0.7419 -0.1737 -0.0365 0.2687  92  THR   F OG1   
4655 C CG2   . THR   F 92  ? 1.3017 0.4630 0.7474 -0.1600 -0.0459 0.2380  92  THR   F CG2   
4656 N N     . LEU   F 93  ? 1.1382 0.4329 0.6606 -0.1006 -0.0472 0.1946  93  LEU   F N     
4657 C CA    . LEU   F 93  ? 1.1109 0.3983 0.6491 -0.0767 -0.0522 0.1761  93  LEU   F CA    
4658 C C     . LEU   F 93  ? 1.1332 0.3733 0.6616 -0.0918 -0.0518 0.1685  93  LEU   F C     
4659 O O     . LEU   F 93  ? 1.1267 0.3801 0.6601 -0.1209 -0.0463 0.1661  93  LEU   F O     
4660 C CB    . LEU   F 93  ? 1.0228 0.3761 0.5966 -0.0693 -0.0479 0.1589  93  LEU   F CB    
4661 C CG    . LEU   F 93  ? 1.0036 0.3595 0.5970 -0.0458 -0.0506 0.1392  93  LEU   F CG    
4662 C CD1   . LEU   F 93  ? 1.0090 0.3510 0.6021 -0.0120 -0.0587 0.1411  93  LEU   F CD1   
4663 C CD2   . LEU   F 93  ? 0.9389 0.3580 0.5655 -0.0466 -0.0449 0.1242  93  LEU   F CD2   
4664 N N     . GLU   F 94  ? 1.1596 0.3469 0.6751 -0.0718 -0.0574 0.1642  94  GLU   F N     
4665 C CA    . GLU   F 94  ? 1.2027 0.3378 0.7042 -0.0827 -0.0571 0.1538  94  GLU   F CA    
4666 C C     . GLU   F 94  ? 1.1712 0.3144 0.6907 -0.0566 -0.0565 0.1316  94  GLU   F C     
4667 O O     . GLU   F 94  ? 1.1651 0.3080 0.6916 -0.0238 -0.0598 0.1320  94  GLU   F O     
4668 C CB    . GLU   F 94  ? 1.2878 0.3418 0.7530 -0.0837 -0.0616 0.1673  94  GLU   F CB    
4669 C CG    . GLU   F 94  ? 1.3338 0.3301 0.7797 -0.1021 -0.0607 0.1559  94  GLU   F CG    
4670 C CD    . GLU   F 94  ? 1.4305 0.3394 0.8392 -0.1002 -0.0648 0.1686  94  GLU   F CD    
4671 O OE1   . GLU   F 94  ? 1.4454 0.3255 0.8497 -0.0653 -0.0684 0.1709  94  GLU   F OE1   
4672 O OE2   . GLU   F 94  ? 1.4757 0.3447 0.8611 -0.1331 -0.0648 0.1770  94  GLU   F OE2   
4673 N N     . LEU   F 95  ? 1.1493 0.3010 0.6758 -0.0721 -0.0527 0.1139  95  LEU   F N     
4674 C CA    . LEU   F 95  ? 1.1515 0.3100 0.6912 -0.0520 -0.0501 0.0922  95  LEU   F CA    
4675 C C     . LEU   F 95  ? 1.2190 0.3109 0.7310 -0.0605 -0.0496 0.0802  95  LEU   F C     
4676 O O     . LEU   F 95  ? 1.2310 0.3034 0.7271 -0.0942 -0.0509 0.0812  95  LEU   F O     
4677 C CB    . LEU   F 95  ? 1.1020 0.3291 0.6709 -0.0618 -0.0464 0.0808  95  LEU   F CB    
4678 C CG    . LEU   F 95  ? 1.0452 0.3390 0.6425 -0.0517 -0.0455 0.0879  95  LEU   F CG    
4679 C CD1   . LEU   F 95  ? 0.9900 0.3406 0.6136 -0.0619 -0.0414 0.0752  95  LEU   F CD1   
4680 C CD2   . LEU   F 95  ? 1.0327 0.3337 0.6409 -0.0151 -0.0477 0.0885  95  LEU   F CD2   
4681 N N     . THR   F 96  ? 1.2517 0.3129 0.7602 -0.0296 -0.0471 0.0683  96  THR   F N     
4682 C CA    . THR   F 96  ? 1.3302 0.3291 0.8126 -0.0297 -0.0440 0.0515  96  THR   F CA    
4683 C C     . THR   F 96  ? 1.3252 0.3445 0.8247 0.0000  -0.0366 0.0316  96  THR   F C     
4684 O O     . THR   F 96  ? 1.2919 0.3621 0.8222 0.0240  -0.0353 0.0339  96  THR   F O     
4685 C CB    . THR   F 96  ? 1.4022 0.3193 0.8531 -0.0210 -0.0464 0.0616  96  THR   F CB    
4686 O OG1   . THR   F 96  ? 1.4647 0.3261 0.8949 -0.0096 -0.0407 0.0415  96  THR   F OG1   
4687 C CG2   . THR   F 96  ? 1.3992 0.3169 0.8615 0.0142  -0.0491 0.0772  96  THR   F CG2   
4688 N N     . ARG   F 97  ? 1.4141 0.3871 0.8903 -0.0012 -0.0314 0.0121  97  ARG   F N     
4689 C CA    . ARG   F 97  ? 1.4129 0.3888 0.8968 0.0278  -0.0215 -0.0075 97  ARG   F CA    
4690 C C     . ARG   F 97  ? 1.4002 0.3737 0.9024 0.0711  -0.0181 -0.0014 97  ARG   F C     
4691 O O     . ARG   F 97  ? 1.3700 0.3795 0.8964 0.0954  -0.0105 -0.0121 97  ARG   F O     
4692 C CB    . ARG   F 97  ? 1.5092 0.4143 0.9525 0.0184  -0.0163 -0.0272 97  ARG   F CB    
4693 C CG    . ARG   F 97  ? 1.5284 0.4171 0.9676 0.0473  -0.0029 -0.0496 97  ARG   F CG    
4694 C CD    . ARG   F 97  ? 1.5915 0.4049 1.0100 0.0762  0.0036  -0.0523 97  ARG   F CD    
4695 N NE    . ARG   F 97  ? 1.6905 0.4234 1.0588 0.0506  0.0026  -0.0630 97  ARG   F NE    
4696 C CZ    . ARG   F 97  ? 1.7477 0.4052 1.0857 0.0442  -0.0019 -0.0548 97  ARG   F CZ    
4697 N NH1   . ARG   F 97  ? 1.8069 0.4085 1.1033 0.0089  -0.0061 -0.0634 97  ARG   F NH1   
4698 N NH2   . ARG   F 97  ? 1.7770 0.4144 1.1250 0.0701  -0.0038 -0.0366 97  ARG   F NH2   
4699 N N     . ASP   F 98  ? 1.4587 0.3904 0.9500 0.0802  -0.0241 0.0163  98  ASP   F N     
4700 C CA    . ASP   F 98  ? 1.4741 0.3991 0.9820 0.1213  -0.0235 0.0248  98  ASP   F CA    
4701 C C     . ASP   F 98  ? 1.3941 0.3920 0.9404 0.1340  -0.0307 0.0407  98  ASP   F C     
4702 O O     . ASP   F 98  ? 1.3998 0.4057 0.9672 0.1691  -0.0309 0.0456  98  ASP   F O     
4703 C CB    . ASP   F 98  ? 1.5749 0.4213 1.0533 0.1271  -0.0284 0.0389  98  ASP   F CB    
4704 C CG    . ASP   F 98  ? 1.6477 0.4096 1.0831 0.1142  -0.0225 0.0244  98  ASP   F CG    
4705 O OD1   . ASP   F 98  ? 1.6759 0.4259 1.1075 0.1262  -0.0110 0.0013  98  ASP   F OD1   
4706 O OD2   . ASP   F 98  ? 1.7357 0.4448 1.1403 0.0907  -0.0291 0.0361  98  ASP   F OD2   
4707 N N     . GLY   F 99  ? 1.3291 0.3790 0.8849 0.1067  -0.0362 0.0481  99  GLY   F N     
4708 C CA    . GLY   F 99  ? 1.2301 0.3398 0.8132 0.1134  -0.0438 0.0638  99  GLY   F CA    
4709 C C     . GLY   F 99  ? 1.2199 0.3324 0.7870 0.0813  -0.0509 0.0808  99  GLY   F C     
4710 O O     . GLY   F 99  ? 1.2095 0.3126 0.7607 0.0492  -0.0487 0.0763  99  GLY   F O     
4711 N N     . ALA   F 100 ? 1.2156 0.3416 0.7866 0.0897  -0.0596 0.1010  100 ALA   F N     
4712 C CA    . ALA   F 100 ? 1.1858 0.3409 0.7519 0.0632  -0.0638 0.1156  100 ALA   F CA    
4713 C C     . ALA   F 100 ? 1.2165 0.3527 0.7685 0.0727  -0.0737 0.1401  100 ALA   F C     
4714 O O     . ALA   F 100 ? 1.2077 0.3356 0.7679 0.1044  -0.0798 0.1455  100 ALA   F O     
4715 C CB    . ALA   F 100 ? 1.1103 0.3446 0.7090 0.0615  -0.0616 0.1080  100 ALA   F CB    
4716 N N     . SER   F 101 ? 1.2322 0.3692 0.7656 0.0447  -0.0752 0.1552  101 SER   F N     
4717 C CA    . SER   F 101 ? 1.2671 0.3879 0.7806 0.0470  -0.0840 0.1802  101 SER   F CA    
4718 C C     . SER   F 101 ? 1.2397 0.4054 0.7506 0.0205  -0.0818 0.1897  101 SER   F C     
4719 O O     . SER   F 101 ? 1.1947 0.3806 0.7102 -0.0067 -0.0731 0.1812  101 SER   F O     
4720 C CB    . SER   F 101 ? 1.3479 0.3872 0.8256 0.0408  -0.0861 0.1930  101 SER   F CB    
4721 O OG    . SER   F 101 ? 1.3542 0.3730 0.8153 0.0040  -0.0788 0.1896  101 SER   F OG    
4722 N N     . ILE   F 102 ? 1.2684 0.4456 0.7693 0.0286  -0.0899 0.2084  102 ILE   F N     
4723 C CA    . ILE   F 102 ? 1.2368 0.4527 0.7300 0.0078  -0.0871 0.2188  102 ILE   F CA    
4724 C C     . ILE   F 102 ? 1.2863 0.4546 0.7391 -0.0018 -0.0922 0.2459  102 ILE   F C     
4725 O O     . ILE   F 102 ? 1.2904 0.4389 0.7312 0.0204  -0.1043 0.2601  102 ILE   F O     
4726 C CB    . ILE   F 102 ? 1.2005 0.4815 0.7173 0.0235  -0.0910 0.2130  102 ILE   F CB    
4727 C CG1   . ILE   F 102 ? 1.2259 0.5037 0.7509 0.0590  -0.1055 0.2172  102 ILE   F CG1   
4728 C CG2   . ILE   F 102 ? 1.1328 0.4653 0.6852 0.0201  -0.0818 0.1888  102 ILE   F CG2   
4729 C CD1   . ILE   F 102 ? 1.1821 0.5145 0.7174 0.0682  -0.1130 0.2190  102 ILE   F CD1   
4730 N N     . ASN   F 103 ? 1.3041 0.4555 0.7375 -0.0353 -0.0830 0.2538  103 ASN   F N     
4731 C CA    . ASN   F 103 ? 1.3761 0.4801 0.7699 -0.0524 -0.0841 0.2795  103 ASN   F CA    
4732 C C     . ASN   F 103 ? 1.4464 0.4689 0.8171 -0.0449 -0.0908 0.2887  103 ASN   F C     
4733 O O     . ASN   F 103 ? 1.4919 0.4710 0.8292 -0.0628 -0.0907 0.3101  103 ASN   F O     
4734 C CB    . ASN   F 103 ? 1.3843 0.5107 0.7584 -0.0487 -0.0890 0.2987  103 ASN   F CB    
4735 C CG    . ASN   F 103 ? 1.3176 0.5112 0.7037 -0.0657 -0.0777 0.2923  103 ASN   F CG    
4736 O OD1   . ASN   F 103 ? 1.3000 0.5109 0.6962 -0.0923 -0.0640 0.2854  103 ASN   F OD1   
4737 N ND2   . ASN   F 103 ? 1.2870 0.5186 0.6719 -0.0512 -0.0834 0.2946  103 ASN   F ND2   
4738 N N     . GLY   F 104 ? 1.4574 0.4555 0.8437 -0.0236 -0.0938 0.2723  104 GLY   F N     
4739 C CA    . GLY   F 104 ? 1.5416 0.4650 0.9083 -0.0047 -0.1015 0.2809  104 GLY   F CA    
4740 C C     . GLY   F 104 ? 1.5532 0.4849 0.9447 0.0386  -0.1094 0.2706  104 GLY   F C     
4741 O O     . GLY   F 104 ? 1.6193 0.5054 1.0126 0.0536  -0.1083 0.2599  104 GLY   F O     
4742 N N     . LYS   F 105 ? 1.5176 0.5049 0.9271 0.0581  -0.1171 0.2742  105 LYS   F N     
4743 C CA    . LYS   F 105 ? 1.5233 0.5208 0.9572 0.0992  -0.1270 0.2704  105 LYS   F CA    
4744 C C     . LYS   F 105 ? 1.4785 0.5187 0.9517 0.1082  -0.1183 0.2405  105 LYS   F C     
4745 O O     . LYS   F 105 ? 1.3944 0.4934 0.8850 0.0922  -0.1120 0.2282  105 LYS   F O     
4746 C CB    . LYS   F 105 ? 1.5338 0.5688 0.9677 0.1139  -0.1414 0.2883  105 LYS   F CB    
4747 C CG    . LYS   F 105 ? 1.6281 0.6239 1.0173 0.1008  -0.1490 0.3191  105 LYS   F CG    
4748 C CD    . LYS   F 105 ? 1.6694 0.6640 1.0478 0.1257  -0.1688 0.3432  105 LYS   F CD    
4749 C CE    . LYS   F 105 ? 1.7465 0.6969 1.0752 0.1063  -0.1726 0.3726  105 LYS   F CE    
4750 N NZ    . LYS   F 105 ? 1.8047 0.7530 1.1154 0.1259  -0.1929 0.3988  105 LYS   F NZ    
4751 N N     . ALA   F 106 ? 1.5169 0.5238 1.0021 0.1334  -0.1168 0.2293  106 ALA   F N     
4752 C CA    . ALA   F 106 ? 1.4702 0.5106 0.9897 0.1453  -0.1079 0.2022  106 ALA   F CA    
4753 C C     . ALA   F 106 ? 1.4201 0.5295 0.9762 0.1690  -0.1150 0.2002  106 ALA   F C     
4754 O O     . ALA   F 106 ? 1.4117 0.5220 0.9694 0.1906  -0.1286 0.2179  106 ALA   F O     
4755 C CB    . ALA   F 106 ? 1.5204 0.5025 1.0382 0.1673  -0.1029 0.1921  106 ALA   F CB    
4756 N N     . VAL   F 107 ? 1.4025 0.5669 0.9876 0.1644  -0.1065 0.1788  107 VAL   F N     
4757 C CA    . VAL   F 107 ? 1.3347 0.5709 0.9541 0.1769  -0.1115 0.1743  107 VAL   F CA    
4758 C C     . VAL   F 107 ? 1.2750 0.5371 0.9292 0.1923  -0.1014 0.1505  107 VAL   F C     
4759 O O     . VAL   F 107 ? 1.2488 0.4840 0.8957 0.1828  -0.0890 0.1353  107 VAL   F O     
4760 C CB    . VAL   F 107 ? 1.3386 0.6218 0.9534 0.1480  -0.1106 0.1756  107 VAL   F CB    
4761 C CG1   . VAL   F 107 ? 1.3683 0.6412 0.9540 0.1404  -0.1222 0.2004  107 VAL   F CG1   
4762 C CG2   . VAL   F 107 ? 1.3395 0.6201 0.9453 0.1163  -0.0965 0.1627  107 VAL   F CG2   
4763 N N     . SER   F 108 ? 1.1906 0.5065 0.8808 0.2136  -0.1071 0.1480  108 SER   F N     
4764 C CA    . SER   F 108 ? 1.1359 0.4814 0.8627 0.2322  -0.0983 0.1289  108 SER   F CA    
4765 C C     . SER   F 108 ? 1.1049 0.4974 0.8435 0.2089  -0.0884 0.1118  108 SER   F C     
4766 O O     . SER   F 108 ? 1.0410 0.4920 0.8069 0.2108  -0.0917 0.1084  108 SER   F O     
4767 C CB    . SER   F 108 ? 1.1087 0.4907 0.8700 0.2630  -0.1096 0.1362  108 SER   F CB    
4768 O OG    . SER   F 108 ? 1.0604 0.4924 0.8281 0.2529  -0.1219 0.1447  108 SER   F OG    
4769 N N     . VAL   F 109 ? 1.1315 0.4963 0.8486 0.1859  -0.0772 0.1018  109 VAL   F N     
4770 C CA    . VAL   F 109 ? 1.1122 0.5136 0.8346 0.1605  -0.0691 0.0891  109 VAL   F CA    
4771 C C     . VAL   F 109 ? 1.0723 0.5150 0.8284 0.1722  -0.0603 0.0706  109 VAL   F C     
4772 O O     . VAL   F 109 ? 1.0158 0.5034 0.7855 0.1572  -0.0570 0.0634  109 VAL   F O     
4773 C CB    . VAL   F 109 ? 1.1489 0.5097 0.8399 0.1320  -0.0622 0.0858  109 VAL   F CB    
4774 C CG1   . VAL   F 109 ? 1.1793 0.4902 0.8584 0.1388  -0.0535 0.0727  109 VAL   F CG1   
4775 C CG2   . VAL   F 109 ? 1.0850 0.4888 0.7826 0.1044  -0.0568 0.0785  109 VAL   F CG2   
4776 N N     . GLU   F 110 ? 1.0824 0.5106 0.8525 0.1992  -0.0558 0.0638  110 GLU   F N     
4777 C CA    . GLU   F 110 ? 1.0613 0.5304 0.8653 0.2131  -0.0467 0.0485  110 GLU   F CA    
4778 C C     . GLU   F 110 ? 0.9811 0.5137 0.8210 0.2225  -0.0552 0.0537  110 GLU   F C     
4779 O O     . GLU   F 110 ? 0.9492 0.5235 0.8161 0.2244  -0.0477 0.0418  110 GLU   F O     
4780 C CB    . GLU   F 110 ? 1.1012 0.5331 0.9063 0.2377  -0.0363 0.0392  110 GLU   F CB    
4781 C CG    . GLU   F 110 ? 1.1606 0.5375 0.9297 0.2221  -0.0255 0.0271  110 GLU   F CG    
4782 C CD    . GLU   F 110 ? 1.2499 0.5531 0.9928 0.2370  -0.0216 0.0266  110 GLU   F CD    
4783 O OE1   . GLU   F 110 ? 1.2930 0.5750 1.0407 0.2612  -0.0282 0.0392  110 GLU   F OE1   
4784 O OE2   . GLU   F 110 ? 1.2947 0.5559 1.0084 0.2229  -0.0124 0.0134  110 GLU   F OE2   
4785 N N     . LYS   F 111 ? 0.9709 0.5111 0.8099 0.2267  -0.0709 0.0709  111 LYS   F N     
4786 C CA    . LYS   F 111 ? 0.9513 0.5485 0.8121 0.2232  -0.0808 0.0752  111 LYS   F CA    
4787 C C     . LYS   F 111 ? 0.8976 0.5012 0.7346 0.1920  -0.0812 0.0769  111 LYS   F C     
4788 O O     . LYS   F 111 ? 0.9426 0.5160 0.7550 0.1740  -0.0730 0.0734  111 LYS   F O     
4789 C CB    . LYS   F 111 ? 0.9984 0.6028 0.8699 0.2442  -0.0982 0.0920  111 LYS   F CB    
4790 C CG    . LYS   F 111 ? 1.0699 0.6648 0.9663 0.2782  -0.0988 0.0942  111 LYS   F CG    
4791 C CD    . LYS   F 111 ? 1.0632 0.7032 1.0053 0.2939  -0.0894 0.0805  111 LYS   F CD    
4792 C CE    . LYS   F 111 ? 1.0516 0.7424 1.0346 0.3126  -0.1036 0.0890  111 LYS   F CE    
4793 N NZ    . LYS   F 111 ? 1.0927 0.7640 1.0862 0.3428  -0.1136 0.1037  111 LYS   F NZ    
4794 N N     . GLY   F 112 ? 0.8166 0.4593 0.6602 0.1843  -0.0900 0.0816  112 GLY   F N     
4795 C CA    . GLY   F 112 ? 0.8124 0.4550 0.6299 0.1579  -0.0897 0.0858  112 GLY   F CA    
4796 C C     . GLY   F 112 ? 0.8106 0.4137 0.5930 0.1548  -0.0990 0.1044  112 GLY   F C     
4797 O O     . GLY   F 112 ? 0.7971 0.3959 0.5819 0.1732  -0.1121 0.1159  112 GLY   F O     
4798 N N     . VAL   F 113 ? 0.7997 0.3775 0.5520 0.1316  -0.0930 0.1088  113 VAL   F N     
4799 C CA    . VAL   F 113 ? 0.8370 0.3856 0.5548 0.1245  -0.1013 0.1281  113 VAL   F CA    
4800 C C     . VAL   F 113 ? 0.8041 0.3703 0.5045 0.0976  -0.0954 0.1300  113 VAL   F C     
4801 O O     . VAL   F 113 ? 0.7834 0.3519 0.4849 0.0797  -0.0829 0.1214  113 VAL   F O     
4802 C CB    . VAL   F 113 ? 0.8972 0.3827 0.5901 0.1266  -0.1009 0.1376  113 VAL   F CB    
4803 C CG1   . VAL   F 113 ? 0.9477 0.4012 0.6026 0.1166  -0.1085 0.1595  113 VAL   F CG1   
4804 C CG2   . VAL   F 113 ? 0.9185 0.3861 0.6290 0.1572  -0.1058 0.1364  113 VAL   F CG2   
4805 N N     . GLN   F 114 ? 0.8178 0.3941 0.5003 0.0953  -0.1046 0.1424  114 GLN   F N     
4806 C CA    . GLN   F 114 ? 0.8093 0.4001 0.4710 0.0728  -0.0984 0.1460  114 GLN   F CA    
4807 C C     . GLN   F 114 ? 0.8612 0.4178 0.4818 0.0672  -0.1056 0.1681  114 GLN   F C     
4808 O O     . GLN   F 114 ? 0.8764 0.4221 0.4883 0.0838  -0.1213 0.1798  114 GLN   F O     
4809 C CB    . GLN   F 114 ? 0.7902 0.4294 0.4660 0.0759  -0.1025 0.1379  114 GLN   F CB    
4810 C CG    . GLN   F 114 ? 0.7775 0.4368 0.4363 0.0548  -0.0925 0.1367  114 GLN   F CG    
4811 C CD    . GLN   F 114 ? 0.7486 0.4484 0.4177 0.0588  -0.0974 0.1274  114 GLN   F CD    
4812 O OE1   . GLN   F 114 ? 0.7107 0.4378 0.4139 0.0675  -0.0975 0.1129  114 GLN   F OE1   
4813 N NE2   . GLN   F 114 ? 0.7777 0.4801 0.4157 0.0516  -0.1015 0.1353  114 GLN   F NE2   
4814 N N     . TYR   F 115 ? 0.8703 0.4151 0.4667 0.0431  -0.0941 0.1745  115 TYR   F N     
4815 C CA    . TYR   F 115 ? 0.9274 0.4438 0.4820 0.0333  -0.0976 0.1957  115 TYR   F CA    
4816 C C     . TYR   F 115 ? 0.9158 0.4601 0.4551 0.0118  -0.0852 0.1954  115 TYR   F C     
4817 O O     . TYR   F 115 ? 0.8815 0.4431 0.4356 -0.0038 -0.0695 0.1854  115 TYR   F O     
4818 C CB    . TYR   F 115 ? 0.9713 0.4340 0.5090 0.0254  -0.0947 0.2070  115 TYR   F CB    
4819 C CG    . TYR   F 115 ? 1.0349 0.4630 0.5284 0.0178  -0.1001 0.2317  115 TYR   F CG    
4820 C CD1   . TYR   F 115 ? 1.0495 0.4780 0.5179 -0.0091 -0.0871 0.2404  115 TYR   F CD1   
4821 C CD2   . TYR   F 115 ? 1.0788 0.4768 0.5563 0.0380  -0.1180 0.2474  115 TYR   F CD2   
4822 C CE1   . TYR   F 115 ? 1.1151 0.5114 0.5401 -0.0176 -0.0907 0.2642  115 TYR   F CE1   
4823 C CE2   . TYR   F 115 ? 1.1453 0.5100 0.5793 0.0307  -0.1238 0.2719  115 TYR   F CE2   
4824 C CZ    . TYR   F 115 ? 1.1645 0.5276 0.5705 0.0022  -0.1097 0.2803  115 TYR   F CZ    
4825 O OH    . TYR   F 115 ? 1.2337 0.5640 0.5943 -0.0058 -0.1144 0.3054  115 TYR   F OH    
4826 N N     . PRO   F 116 ? 0.9538 0.5015 0.4610 0.0095  -0.0909 0.2073  116 PRO   F N     
4827 C CA    . PRO   F 116 ? 0.9861 0.5294 0.4811 0.0289  -0.1121 0.2163  116 PRO   F CA    
4828 C C     . PRO   F 116 ? 0.9468 0.5262 0.4806 0.0484  -0.1218 0.1991  116 PRO   F C     
4829 O O     . PRO   F 116 ? 0.8965 0.5127 0.4525 0.0430  -0.1119 0.1812  116 PRO   F O     
4830 C CB    . PRO   F 116 ? 1.0166 0.5667 0.4698 0.0165  -0.1118 0.2268  116 PRO   F CB    
4831 C CG    . PRO   F 116 ? 1.0244 0.5625 0.4603 -0.0088 -0.0901 0.2321  116 PRO   F CG    
4832 C CD    . PRO   F 116 ? 0.9682 0.5208 0.4458 -0.0134 -0.0765 0.2148  116 PRO   F CD    
4833 N N     . GLN   F 117 ? 0.9936 0.5618 0.5371 0.0709  -0.1404 0.2057  117 GLN   F N     
4834 C CA    . GLN   F 117 ? 0.9781 0.5788 0.5620 0.0907  -0.1505 0.1924  117 GLN   F CA    
4835 C C     . GLN   F 117 ? 0.9508 0.5953 0.5360 0.0871  -0.1557 0.1829  117 GLN   F C     
4836 O O     . GLN   F 117 ? 0.9013 0.5799 0.5229 0.0921  -0.1532 0.1651  117 GLN   F O     
4837 C CB    . GLN   F 117 ? 1.0446 0.6228 0.6340 0.1155  -0.1698 0.2064  117 GLN   F CB    
4838 C CG    . GLN   F 117 ? 1.0374 0.6447 0.6759 0.1379  -0.1768 0.1938  117 GLN   F CG    
4839 C CD    . GLN   F 117 ? 1.0509 0.6969 0.7000 0.1479  -0.1965 0.1948  117 GLN   F CD    
4840 O OE1   . GLN   F 117 ? 1.0954 0.7325 0.7171 0.1513  -0.2145 0.2127  117 GLN   F OE1   
4841 N NE2   . GLN   F 117 ? 1.0155 0.7046 0.7039 0.1518  -0.1946 0.1765  117 GLN   F NE2   
4842 N N     . ASP   F 118 ? 0.9809 0.6222 0.5244 0.0768  -0.1614 0.1941  118 ASP   F N     
4843 C CA    . ASP   F 118 ? 0.9800 0.6558 0.5154 0.0713  -0.1666 0.1848  118 ASP   F CA    
4844 C C     . ASP   F 118 ? 0.9644 0.6556 0.4901 0.0504  -0.1435 0.1710  118 ASP   F C     
4845 O O     . ASP   F 118 ? 0.9779 0.6967 0.5014 0.0464  -0.1449 0.1590  118 ASP   F O     
4846 C CB    . ASP   F 118 ? 1.0425 0.7059 0.5351 0.0730  -0.1869 0.2037  118 ASP   F CB    
4847 C CG    . ASP   F 118 ? 1.0518 0.7473 0.5343 0.0709  -0.2007 0.1958  118 ASP   F CG    
4848 O OD1   . ASP   F 118 ? 1.0114 0.7410 0.5342 0.0781  -0.2051 0.1788  118 ASP   F OD1   
4849 O OD2   . ASP   F 118 ? 1.0804 0.7649 0.5124 0.0611  -0.2070 0.2071  118 ASP   F OD2   
4850 N N     . ASP   F 119 ? 0.9355 0.6107 0.4572 0.0370  -0.1227 0.1721  119 ASP   F N     
4851 C CA    . ASP   F 119 ? 0.9199 0.6076 0.4259 0.0176  -0.1013 0.1649  119 ASP   F CA    
4852 C C     . ASP   F 119 ? 0.8495 0.5676 0.3995 0.0166  -0.0871 0.1431  119 ASP   F C     
4853 O O     . ASP   F 119 ? 0.8177 0.5289 0.3947 0.0178  -0.0806 0.1410  119 ASP   F O     
4854 C CB    . ASP   F 119 ? 0.9691 0.6276 0.4463 0.0017  -0.0874 0.1806  119 ASP   F CB    
4855 C CG    . ASP   F 119 ? 0.9881 0.6593 0.4459 -0.0183 -0.0641 0.1773  119 ASP   F CG    
4856 O OD1   . ASP   F 119 ? 0.9799 0.6815 0.4439 -0.0194 -0.0571 0.1610  119 ASP   F OD1   
4857 O OD2   . ASP   F 119 ? 1.0011 0.6511 0.4379 -0.0327 -0.0522 0.1915  119 ASP   F OD2   
4858 N N     . PRO   F 120 ? 0.7986 0.5475 0.3545 0.0139  -0.0819 0.1267  120 PRO   F N     
4859 C CA    . PRO   F 120 ? 0.7399 0.5146 0.3346 0.0121  -0.0670 0.1084  120 PRO   F CA    
4860 C C     . PRO   F 120 ? 0.7254 0.4981 0.3230 -0.0023 -0.0442 0.1096  120 PRO   F C     
4861 O O     . PRO   F 120 ? 0.7083 0.4925 0.3411 -0.0016 -0.0366 0.1009  120 PRO   F O     
4862 C CB    . PRO   F 120 ? 0.7328 0.5319 0.3235 0.0118  -0.0679 0.0938  120 PRO   F CB    
4863 C CG    . PRO   F 120 ? 0.7911 0.5758 0.3293 0.0052  -0.0732 0.1045  120 PRO   F CG    
4864 C CD    . PRO   F 120 ? 0.8252 0.5821 0.3476 0.0112  -0.0893 0.1251  120 PRO   F CD    
4865 N N     . ASN   F 121 ? 0.7704 0.5294 0.3322 -0.0156 -0.0341 0.1217  121 ASN   F N     
4866 C CA    . ASN   F 121 ? 0.7712 0.5255 0.3367 -0.0304 -0.0152 0.1282  121 ASN   F CA    
4867 C C     . ASN   F 121 ? 0.7953 0.5157 0.3571 -0.0311 -0.0238 0.1437  121 ASN   F C     
4868 O O     . ASN   F 121 ? 0.8271 0.5237 0.3584 -0.0427 -0.0199 0.1605  121 ASN   F O     
4869 C CB    . ASN   F 121 ? 0.7989 0.5571 0.3315 -0.0450 0.0024  0.1336  121 ASN   F CB    
4870 C CG    . ASN   F 121 ? 0.7928 0.5562 0.3382 -0.0611 0.0233  0.1392  121 ASN   F CG    
4871 O OD1   . ASN   F 121 ? 0.7818 0.5625 0.3676 -0.0615 0.0295  0.1305  121 ASN   F OD1   
4872 N ND2   . ASN   F 121 ? 0.8414 0.5910 0.3539 -0.0754 0.0338  0.1548  121 ASN   F ND2   
4873 N N     . TYR   F 122 ? 0.7639 0.4809 0.3569 -0.0198 -0.0334 0.1375  122 TYR   F N     
4874 C CA    . TYR   F 122 ? 0.7932 0.4736 0.3821 -0.0169 -0.0427 0.1494  122 TYR   F CA    
4875 C C     . TYR   F 122 ? 0.7955 0.4646 0.3880 -0.0358 -0.0281 0.1545  122 TYR   F C     
4876 O O     . TYR   F 122 ? 0.7558 0.4518 0.3737 -0.0445 -0.0147 0.1442  122 TYR   F O     
4877 C CB    . TYR   F 122 ? 0.7712 0.4493 0.3896 0.0022  -0.0557 0.1406  122 TYR   F CB    
4878 C CG    . TYR   F 122 ? 0.7205 0.4281 0.3794 0.0039  -0.0476 0.1219  122 TYR   F CG    
4879 C CD1   . TYR   F 122 ? 0.7072 0.4083 0.3822 -0.0057 -0.0384 0.1189  122 TYR   F CD1   
4880 C CD2   . TYR   F 122 ? 0.6815 0.4223 0.3604 0.0135  -0.0501 0.1080  122 TYR   F CD2   
4881 C CE1   . TYR   F 122 ? 0.6725 0.4007 0.3815 -0.0045 -0.0320 0.1034  122 TYR   F CE1   
4882 C CE2   . TYR   F 122 ? 0.6606 0.4266 0.3745 0.0147  -0.0427 0.0926  122 TYR   F CE2   
4883 C CZ    . TYR   F 122 ? 0.6465 0.4062 0.3748 0.0064  -0.0339 0.0909  122 TYR   F CZ    
4884 O OH    . TYR   F 122 ? 0.6125 0.3966 0.3719 0.0075  -0.0277 0.0776  122 TYR   F OH    
4885 N N     . ALA   F 123 ? 0.8417 0.4700 0.4100 -0.0418 -0.0324 0.1713  123 ALA   F N     
4886 C CA    . ALA   F 123 ? 0.8605 0.4704 0.4308 -0.0607 -0.0228 0.1776  123 ALA   F CA    
4887 C C     . ALA   F 123 ? 0.8282 0.4335 0.4298 -0.0551 -0.0263 0.1651  123 ALA   F C     
4888 O O     . ALA   F 123 ? 0.8156 0.4285 0.4328 -0.0713 -0.0164 0.1616  123 ALA   F O     
4889 C CB    . ALA   F 123 ? 0.9297 0.4915 0.4620 -0.0684 -0.0278 0.1994  123 ALA   F CB    
4890 N N     . ILE   F 124 ? 0.8190 0.4110 0.4282 -0.0332 -0.0401 0.1596  124 ILE   F N     
4891 C CA    . ILE   F 124 ? 0.8041 0.3873 0.4375 -0.0270 -0.0420 0.1476  124 ILE   F CA    
4892 C C     . ILE   F 124 ? 0.7827 0.3770 0.4344 -0.0004 -0.0527 0.1374  124 ILE   F C     
4893 O O     . ILE   F 124 ? 0.7889 0.3763 0.4277 0.0137  -0.0638 0.1452  124 ILE   F O     
4894 C CB    . ILE   F 124 ? 0.8510 0.3805 0.4653 -0.0353 -0.0445 0.1576  124 ILE   F CB    
4895 C CG1   . ILE   F 124 ? 0.8388 0.3577 0.4734 -0.0334 -0.0439 0.1432  124 ILE   F CG1   
4896 C CG2   . ILE   F 124 ? 0.8980 0.3846 0.4848 -0.0210 -0.0571 0.1726  124 ILE   F CG2   
4897 C CD1   . ILE   F 124 ? 0.8072 0.3581 0.4627 -0.0531 -0.0330 0.1336  124 ILE   F CD1   
4898 N N     . ARG   F 125 ? 0.7586 0.3745 0.4411 0.0044  -0.0491 0.1207  125 ARG   F N     
4899 C CA    . ARG   F 125 ? 0.7515 0.3721 0.4555 0.0270  -0.0562 0.1100  125 ARG   F CA    
4900 C C     . ARG   F 125 ? 0.7501 0.3475 0.4617 0.0252  -0.0522 0.1018  125 ARG   F C     
4901 O O     . ARG   F 125 ? 0.7427 0.3435 0.4560 0.0058  -0.0437 0.0984  125 ARG   F O     
4902 C CB    . ARG   F 125 ? 0.6935 0.3637 0.4267 0.0325  -0.0531 0.0958  125 ARG   F CB    
4903 C CG    . ARG   F 125 ? 0.6914 0.3812 0.4209 0.0429  -0.0619 0.0993  125 ARG   F CG    
4904 C CD    . ARG   F 125 ? 0.6291 0.3613 0.3875 0.0489  -0.0602 0.0848  125 ARG   F CD    
4905 N NE    . ARG   F 125 ? 0.6223 0.3733 0.3725 0.0529  -0.0681 0.0872  125 ARG   F NE    
4906 C CZ    . ARG   F 125 ? 0.5831 0.3687 0.3518 0.0556  -0.0681 0.0760  125 ARG   F CZ    
4907 N NH1   . ARG   F 125 ? 0.5319 0.3387 0.3286 0.0540  -0.0588 0.0628  125 ARG   F NH1   
4908 N NH2   . ARG   F 125 ? 0.5971 0.3939 0.3533 0.0584  -0.0778 0.0784  125 ARG   F NH2   
4909 N N     . VAL   F 126 ? 0.7749 0.3521 0.4925 0.0459  -0.0581 0.0979  126 VAL   F N     
4910 C CA    . VAL   F 126 ? 0.7868 0.3338 0.5048 0.0466  -0.0542 0.0893  126 VAL   F CA    
4911 C C     . VAL   F 126 ? 0.7811 0.3352 0.5210 0.0736  -0.0567 0.0793  126 VAL   F C     
4912 O O     . VAL   F 126 ? 0.7896 0.3492 0.5350 0.0928  -0.0653 0.0858  126 VAL   F O     
4913 C CB    . VAL   F 126 ? 0.8347 0.3227 0.5204 0.0378  -0.0563 0.1009  126 VAL   F CB    
4914 C CG1   . VAL   F 126 ? 0.8816 0.3386 0.5524 0.0572  -0.0667 0.1148  126 VAL   F CG1   
4915 C CG2   . VAL   F 126 ? 0.8436 0.2976 0.5238 0.0318  -0.0513 0.0901  126 VAL   F CG2   
4916 N N     . TRP   F 127 ? 0.7754 0.3315 0.5276 0.0740  -0.0491 0.0642  127 TRP   F N     
4917 C CA    . TRP   F 127 ? 0.7514 0.3183 0.5263 0.0972  -0.0472 0.0530  127 TRP   F CA    
4918 C C     . TRP   F 127 ? 0.7732 0.3111 0.5406 0.0948  -0.0386 0.0402  127 TRP   F C     
4919 O O     . TRP   F 127 ? 0.7522 0.2882 0.5099 0.0724  -0.0342 0.0358  127 TRP   F O     
4920 C CB    . TRP   F 127 ? 0.6846 0.3096 0.4896 0.0990  -0.0454 0.0458  127 TRP   F CB    
4921 C CG    . TRP   F 127 ? 0.6627 0.3069 0.4948 0.1194  -0.0417 0.0346  127 TRP   F CG    
4922 C CD1   . TRP   F 127 ? 0.6634 0.3200 0.5147 0.1431  -0.0474 0.0372  127 TRP   F CD1   
4923 C CD2   . TRP   F 127 ? 0.6407 0.2990 0.4853 0.1167  -0.0311 0.0200  127 TRP   F CD2   
4924 N NE1   . TRP   F 127 ? 0.6435 0.3205 0.5199 0.1554  -0.0394 0.0250  127 TRP   F NE1   
4925 C CE2   . TRP   F 127 ? 0.6309 0.3081 0.5015 0.1396  -0.0290 0.0144  127 TRP   F CE2   
4926 C CE3   . TRP   F 127 ? 0.6397 0.2974 0.4760 0.0971  -0.0239 0.0124  127 TRP   F CE3   
4927 C CZ2   . TRP   F 127 ? 0.6214 0.3154 0.5073 0.1426  -0.0181 0.0012  127 TRP   F CZ2   
4928 C CZ3   . TRP   F 127 ? 0.6280 0.3023 0.4781 0.1003  -0.0152 -0.0003 127 TRP   F CZ3   
4929 C CH2   . TRP   F 127 ? 0.6260 0.3177 0.4994 0.1225  -0.0115 -0.0059 127 TRP   F CH2   
4930 N N     . LYS   F 128 ? 0.8151 0.3349 0.5887 0.1184  -0.0361 0.0337  128 LYS   F N     
4931 C CA    . LYS   F 128 ? 0.8534 0.3366 0.6133 0.1196  -0.0272 0.0207  128 LYS   F CA    
4932 C C     . LYS   F 128 ? 0.8230 0.3307 0.6091 0.1418  -0.0190 0.0079  128 LYS   F C     
4933 O O     . LYS   F 128 ? 0.8233 0.3504 0.6331 0.1656  -0.0218 0.0122  128 LYS   F O     
4934 C CB    . LYS   F 128 ? 0.9315 0.3484 0.6619 0.1251  -0.0298 0.0269  128 LYS   F CB    
4935 C CG    . LYS   F 128 ? 0.9740 0.3427 0.6856 0.1305  -0.0205 0.0124  128 LYS   F CG    
4936 C CD    . LYS   F 128 ? 1.0557 0.3522 0.7331 0.1301  -0.0234 0.0187  128 LYS   F CD    
4937 C CE    . LYS   F 128 ? 1.0967 0.3414 0.7462 0.1243  -0.0145 0.0023  128 LYS   F CE    
4938 N NZ    . LYS   F 128 ? 1.1730 0.3524 0.7853 0.1082  -0.0193 0.0094  128 LYS   F NZ    
4939 N N     . SER   F 129 ? 0.7876 0.2938 0.5683 0.1332  -0.0090 -0.0068 129 SER   F N     
4940 C CA    . SER   F 129 ? 0.7854 0.3074 0.5836 0.1511  0.0023  -0.0202 129 SER   F CA    
4941 C C     . SER   F 129 ? 0.8185 0.2983 0.5859 0.1420  0.0116  -0.0344 129 SER   F C     
4942 O O     . SER   F 129 ? 0.8040 0.2811 0.5538 0.1151  0.0094  -0.0365 129 SER   F O     
4943 C CB    . SER   F 129 ? 0.7326 0.3161 0.5605 0.1462  0.0041  -0.0226 129 SER   F CB    
4944 O OG    . SER   F 129 ? 0.7177 0.3173 0.5618 0.1613  0.0163  -0.0345 129 SER   F OG    
4945 N N     . GLY   F 130 ? 0.8756 0.3197 0.6351 0.1641  0.0210  -0.0432 130 GLY   F N     
4946 C CA    . GLY   F 130 ? 0.9184 0.3059 0.6393 0.1570  0.0286  -0.0565 130 GLY   F CA    
4947 C C     . GLY   F 130 ? 0.9644 0.3092 0.6529 0.1323  0.0177  -0.0489 130 GLY   F C     
4948 O O     . GLY   F 130 ? 0.9780 0.3086 0.6679 0.1375  0.0088  -0.0343 130 GLY   F O     
4949 N N     . ASP   F 131 ? 0.9676 0.2994 0.6304 0.1035  0.0169  -0.0566 131 ASP   F N     
4950 C CA    . ASP   F 131 ? 1.0048 0.3020 0.6399 0.0754  0.0068  -0.0494 131 ASP   F CA    
4951 C C     . ASP   F 131 ? 0.9679 0.3147 0.6202 0.0512  -0.0027 -0.0369 131 ASP   F C     
4952 O O     . ASP   F 131 ? 1.0227 0.3487 0.6569 0.0261  -0.0104 -0.0295 131 ASP   F O     
4953 C CB    . ASP   F 131 ? 1.0715 0.3151 0.6652 0.0591  0.0104  -0.0650 131 ASP   F CB    
4954 C CG    . ASP   F 131 ? 1.1220 0.3097 0.6937 0.0834  0.0224  -0.0797 131 ASP   F CG    
4955 O OD1   . ASP   F 131 ? 1.1413 0.2963 0.7133 0.1044  0.0227  -0.0729 131 ASP   F OD1   
4956 O OD2   . ASP   F 131 ? 1.1429 0.3200 0.6964 0.0820  0.0319  -0.0978 131 ASP   F OD2   
4957 N N     . LEU   F 132 ? 0.9115 0.3219 0.5986 0.0576  -0.0016 -0.0344 132 LEU   F N     
4958 C CA    . LEU   F 132 ? 0.8563 0.3130 0.5617 0.0393  -0.0087 -0.0227 132 LEU   F CA    
4959 C C     . LEU   F 132 ? 0.8389 0.2940 0.5504 0.0463  -0.0153 -0.0065 132 LEU   F C     
4960 O O     . LEU   F 132 ? 0.8033 0.2649 0.5299 0.0720  -0.0145 -0.0040 132 LEU   F O     
4961 C CB    . LEU   F 132 ? 0.8120 0.3302 0.5499 0.0454  -0.0048 -0.0259 132 LEU   F CB    
4962 C CG    . LEU   F 132 ? 0.7628 0.3298 0.5229 0.0324  -0.0101 -0.0149 132 LEU   F CG    
4963 C CD1   . LEU   F 132 ? 0.7790 0.3497 0.5291 0.0021  -0.0142 -0.0118 132 LEU   F CD1   
4964 C CD2   . LEU   F 132 ? 0.7467 0.3636 0.5371 0.0439  -0.0055 -0.0191 132 LEU   F CD2   
4965 N N     . VAL   F 133 ? 0.8363 0.2890 0.5384 0.0228  -0.0216 0.0051  133 VAL   F N     
4966 C CA    . VAL   F 133 ? 0.8218 0.2863 0.5303 0.0248  -0.0272 0.0216  133 VAL   F CA    
4967 C C     . VAL   F 133 ? 0.7658 0.2820 0.4921 0.0062  -0.0277 0.0269  133 VAL   F C     
4968 O O     . VAL   F 133 ? 0.7882 0.3065 0.5086 -0.0180 -0.0275 0.0259  133 VAL   F O     
4969 C CB    . VAL   F 133 ? 0.8499 0.2608 0.5294 0.0166  -0.0322 0.0335  133 VAL   F CB    
4970 C CG1   . VAL   F 133 ? 0.8398 0.2653 0.5235 0.0206  -0.0376 0.0512  133 VAL   F CG1   
4971 C CG2   . VAL   F 133 ? 0.9016 0.2553 0.5622 0.0356  -0.0307 0.0273  133 VAL   F CG2   
4972 N N     . MET   F 134 ? 0.7241 0.2789 0.4709 0.0173  -0.0287 0.0329  134 MET   F N     
4973 C CA    . MET   F 134 ? 0.6999 0.2981 0.4607 0.0026  -0.0280 0.0392  134 MET   F CA    
4974 C C     . MET   F 134 ? 0.7143 0.3043 0.4630 0.0000  -0.0319 0.0548  134 MET   F C     
4975 O O     . MET   F 134 ? 0.7309 0.2983 0.4705 0.0169  -0.0368 0.0603  134 MET   F O     
4976 C CB    . MET   F 134 ? 0.6569 0.3045 0.4474 0.0156  -0.0252 0.0323  134 MET   F CB    
4977 C CG    . MET   F 134 ? 0.6283 0.2912 0.4314 0.0153  -0.0203 0.0188  134 MET   F CG    
4978 S SD    . MET   F 134 ? 0.5924 0.3140 0.4297 0.0224  -0.0164 0.0135  134 MET   F SD    
4979 C CE    . MET   F 134 ? 0.5801 0.3374 0.4285 0.0099  -0.0159 0.0224  134 MET   F CE    
4980 N N     . ALA   F 135 ? 0.7142 0.3234 0.4627 -0.0208 -0.0293 0.0627  135 ALA   F N     
4981 C CA    . ALA   F 135 ? 0.7322 0.3390 0.4676 -0.0252 -0.0306 0.0774  135 ALA   F CA    
4982 C C     . ALA   F 135 ? 0.6887 0.3419 0.4391 -0.0377 -0.0239 0.0799  135 ALA   F C     
4983 O O     . ALA   F 135 ? 0.6767 0.3503 0.4411 -0.0524 -0.0191 0.0756  135 ALA   F O     
4984 C CB    . ALA   F 135 ? 0.8024 0.3624 0.5098 -0.0412 -0.0324 0.0883  135 ALA   F CB    
4985 N N     . TYR   F 136 ? 0.6877 0.3562 0.4341 -0.0314 -0.0239 0.0868  136 TYR   F N     
4986 C CA    . TYR   F 136 ? 0.6537 0.3599 0.4088 -0.0423 -0.0155 0.0896  136 TYR   F CA    
4987 C C     . TYR   F 136 ? 0.6802 0.3767 0.4101 -0.0445 -0.0155 0.1032  136 TYR   F C     
4988 O O     . TYR   F 136 ? 0.6864 0.3614 0.4001 -0.0303 -0.0246 0.1077  136 TYR   F O     
4989 C CB    . TYR   F 136 ? 0.6168 0.3633 0.3982 -0.0292 -0.0134 0.0771  136 TYR   F CB    
4990 C CG    . TYR   F 136 ? 0.5751 0.3594 0.3683 -0.0386 -0.0028 0.0774  136 TYR   F CG    
4991 C CD1   . TYR   F 136 ? 0.5565 0.3596 0.3663 -0.0542 0.0051  0.0772  136 TYR   F CD1   
4992 C CD2   . TYR   F 136 ? 0.5853 0.3846 0.3712 -0.0321 -0.0008 0.0784  136 TYR   F CD2   
4993 C CE1   . TYR   F 136 ? 0.5523 0.3903 0.3759 -0.0606 0.0164  0.0780  136 TYR   F CE1   
4994 C CE2   . TYR   F 136 ? 0.5591 0.3894 0.3539 -0.0393 0.0113  0.0773  136 TYR   F CE2   
4995 C CZ    . TYR   F 136 ? 0.5525 0.4025 0.3679 -0.0524 0.0207  0.0774  136 TYR   F CZ    
4996 O OH    . TYR   F 136 ? 0.5449 0.4268 0.3740 -0.0571 0.0339  0.0765  136 TYR   F OH    
4997 N N     . SER   F 137 ? 0.6678 0.3828 0.3955 -0.0618 -0.0049 0.1101  137 SER   F N     
4998 C CA    . SER   F 137 ? 0.6834 0.3951 0.3857 -0.0663 -0.0013 0.1225  137 SER   F CA    
4999 C C     . SER   F 137 ? 0.6477 0.4032 0.3630 -0.0655 0.0095  0.1161  137 SER   F C     
5000 O O     . SER   F 137 ? 0.6031 0.3856 0.3392 -0.0771 0.0210  0.1136  137 SER   F O     
5001 C CB    . SER   F 137 ? 0.7074 0.3988 0.3933 -0.0888 0.0045  0.1369  137 SER   F CB    
5002 O OG    . SER   F 137 ? 0.7282 0.4204 0.3888 -0.0951 0.0111  0.1492  137 SER   F OG    
5003 N N     . ARG   F 138 ? 0.6684 0.4293 0.3704 -0.0526 0.0057  0.1141  138 ARG   F N     
5004 C CA    . ARG   F 138 ? 0.6803 0.4734 0.3840 -0.0532 0.0171  0.1089  138 ARG   F CA    
5005 C C     . ARG   F 138 ? 0.6947 0.4904 0.3792 -0.0709 0.0322  0.1210  138 ARG   F C     
5006 O O     . ARG   F 138 ? 0.6572 0.4838 0.3541 -0.0745 0.0472  0.1155  138 ARG   F O     
5007 C CB    . ARG   F 138 ? 0.7289 0.5234 0.4181 -0.0376 0.0074  0.1035  138 ARG   F CB    
5008 C CG    . ARG   F 138 ? 0.7546 0.5710 0.4751 -0.0236 0.0024  0.0868  138 ARG   F CG    
5009 C CD    . ARG   F 138 ? 0.8284 0.6519 0.5390 -0.0113 -0.0070 0.0801  138 ARG   F CD    
5010 N NE    . ARG   F 138 ? 0.9196 0.7510 0.6041 -0.0178 0.0023  0.0808  138 ARG   F NE    
5011 C CZ    . ARG   F 138 ? 0.9455 0.8006 0.6366 -0.0184 0.0137  0.0688  138 ARG   F CZ    
5012 N NH1   . ARG   F 138 ? 1.0119 0.8673 0.6720 -0.0245 0.0230  0.0705  138 ARG   F NH1   
5013 N NH2   . ARG   F 138 ? 0.9390 0.8151 0.6653 -0.0130 0.0171  0.0556  138 ARG   F NH2   
5014 N N     . ARG   F 139 ? 0.7179 0.4818 0.3742 -0.0816 0.0299  0.1374  139 ARG   F N     
5015 C CA    . ARG   F 139 ? 0.7494 0.5165 0.3872 -0.0999 0.0456  0.1504  139 ARG   F CA    
5016 C C     . ARG   F 139 ? 0.7277 0.5198 0.3977 -0.1164 0.0598  0.1506  139 ARG   F C     
5017 O O     . ARG   F 139 ? 0.7416 0.5653 0.4205 -0.1227 0.0776  0.1500  139 ARG   F O     
5018 C CB    . ARG   F 139 ? 0.8036 0.5280 0.4004 -0.1071 0.0387  0.1694  139 ARG   F CB    
5019 C CG    . ARG   F 139 ? 0.8188 0.5276 0.3829 -0.0915 0.0261  0.1710  139 ARG   F CG    
5020 C CD    . ARG   F 139 ? 0.8685 0.5355 0.3890 -0.0982 0.0196  0.1924  139 ARG   F CD    
5021 N NE    . ARG   F 139 ? 0.8841 0.5331 0.3800 -0.0800 0.0005  0.1946  139 ARG   F NE    
5022 C CZ    . ARG   F 139 ? 0.9319 0.5418 0.3912 -0.0783 -0.0120 0.2128  139 ARG   F CZ    
5023 N NH1   . ARG   F 139 ? 0.9655 0.5438 0.4054 -0.0945 -0.0071 0.2308  139 ARG   F NH1   
5024 N NH2   . ARG   F 139 ? 0.9435 0.5460 0.3869 -0.0606 -0.0305 0.2139  139 ARG   F NH2   
5025 N N     . THR   F 140 ? 0.7209 0.5003 0.4090 -0.1225 0.0517  0.1508  140 THR   F N     
5026 C CA    . THR   F 140 ? 0.7059 0.5069 0.4236 -0.1408 0.0608  0.1529  140 THR   F CA    
5027 C C     . THR   F 140 ? 0.6625 0.4995 0.4216 -0.1322 0.0613  0.1374  140 THR   F C     
5028 O O     . THR   F 140 ? 0.6614 0.5275 0.4490 -0.1455 0.0702  0.1393  140 THR   F O     
5029 C CB    . THR   F 140 ? 0.7270 0.4893 0.4352 -0.1550 0.0504  0.1618  140 THR   F CB    
5030 O OG1   . THR   F 140 ? 0.7010 0.4386 0.4090 -0.1388 0.0339  0.1516  140 THR   F OG1   
5031 C CG2   . THR   F 140 ? 0.7830 0.5070 0.4505 -0.1652 0.0504  0.1796  140 THR   F CG2   
5032 N N     . ALA   F 141 ? 0.6324 0.4665 0.3958 -0.1113 0.0507  0.1239  141 ALA   F N     
5033 C CA    . ALA   F 141 ? 0.6145 0.4722 0.4122 -0.1027 0.0476  0.1102  141 ALA   F CA    
5034 C C     . ALA   F 141 ? 0.5935 0.4413 0.4057 -0.1140 0.0396  0.1106  141 ALA   F C     
5035 O O     . ALA   F 141 ? 0.5739 0.4459 0.4149 -0.1118 0.0390  0.1023  141 ALA   F O     
5036 C CB    . ALA   F 141 ? 0.5787 0.4812 0.4021 -0.1004 0.0626  0.1050  141 ALA   F CB    
5037 N N     . VAL   F 142 ? 0.6211 0.4291 0.4102 -0.1242 0.0319  0.1189  142 VAL   F N     
5038 C CA    . VAL   F 142 ? 0.6286 0.4180 0.4233 -0.1345 0.0228  0.1169  142 VAL   F CA    
5039 C C     . VAL   F 142 ? 0.6051 0.3712 0.3940 -0.1140 0.0110  0.1048  142 VAL   F C     
5040 O O     . VAL   F 142 ? 0.6272 0.3666 0.3942 -0.0999 0.0057  0.1059  142 VAL   F O     
5041 C CB    . VAL   F 142 ? 0.6910 0.4451 0.4635 -0.1564 0.0208  0.1303  142 VAL   F CB    
5042 C CG1   . VAL   F 142 ? 0.7197 0.4452 0.4908 -0.1656 0.0096  0.1252  142 VAL   F CG1   
5043 C CG2   . VAL   F 142 ? 0.6982 0.4832 0.4828 -0.1779 0.0343  0.1425  142 VAL   F CG2   
5044 N N     . TYR   F 143 ? 0.5628 0.3432 0.3732 -0.1120 0.0076  0.0941  143 TYR   F N     
5045 C CA    . TYR   F 143 ? 0.5582 0.3170 0.3650 -0.0968 -0.0015 0.0827  143 TYR   F CA    
5046 C C     . TYR   F 143 ? 0.5916 0.3159 0.3857 -0.1117 -0.0082 0.0824  143 TYR   F C     
5047 O O     . TYR   F 143 ? 0.5922 0.3275 0.3947 -0.1338 -0.0074 0.0867  143 TYR   F O     
5048 C CB    . TYR   F 143 ? 0.4986 0.2945 0.3341 -0.0870 0.0002  0.0712  143 TYR   F CB    
5049 C CG    . TYR   F 143 ? 0.4847 0.2632 0.3186 -0.0730 -0.0068 0.0593  143 TYR   F CG    
5050 C CD1   . TYR   F 143 ? 0.4791 0.2482 0.3083 -0.0511 -0.0093 0.0540  143 TYR   F CD1   
5051 C CD2   . TYR   F 143 ? 0.4838 0.2567 0.3206 -0.0823 -0.0106 0.0536  143 TYR   F CD2   
5052 C CE1   . TYR   F 143 ? 0.4757 0.2311 0.3054 -0.0381 -0.0132 0.0437  143 TYR   F CE1   
5053 C CE2   . TYR   F 143 ? 0.4850 0.2400 0.3166 -0.0698 -0.0145 0.0424  143 TYR   F CE2   
5054 C CZ    . TYR   F 143 ? 0.4848 0.2326 0.3147 -0.0470 -0.0146 0.0374  143 TYR   F CZ    
5055 O OH    . TYR   F 143 ? 0.5034 0.2388 0.3319 -0.0346 -0.0159 0.0264  143 TYR   F OH    
5056 N N     . ALA   F 144 ? 0.6093 0.2944 0.3855 -0.0987 -0.0150 0.0761  144 ALA   F N     
5057 C CA    . ALA   F 144 ? 0.6424 0.2922 0.4048 -0.1091 -0.0209 0.0709  144 ALA   F CA    
5058 C C     . ALA   F 144 ? 0.6395 0.2700 0.3975 -0.0868 -0.0241 0.0575  144 ALA   F C     
5059 O O     . ALA   F 144 ? 0.6172 0.2488 0.3768 -0.0645 -0.0237 0.0565  144 ALA   F O     
5060 C CB    . ALA   F 144 ? 0.7003 0.3029 0.4341 -0.1237 -0.0235 0.0820  144 ALA   F CB    
5061 N N     . TYR   F 145 ? 0.6592 0.2711 0.4100 -0.0939 -0.0272 0.0478  145 TYR   F N     
5062 C CA    . TYR   F 145 ? 0.6951 0.2741 0.4328 -0.0750 -0.0284 0.0357  145 TYR   F CA    
5063 C C     . TYR   F 145 ? 0.7430 0.2720 0.4526 -0.0901 -0.0324 0.0301  145 TYR   F C     
5064 O O     . TYR   F 145 ? 0.7501 0.2832 0.4574 -0.1164 -0.0358 0.0320  145 TYR   F O     
5065 C CB    . TYR   F 145 ? 0.6553 0.2707 0.4152 -0.0593 -0.0251 0.0244  145 TYR   F CB    
5066 C CG    . TYR   F 145 ? 0.6391 0.2686 0.4030 -0.0718 -0.0259 0.0154  145 TYR   F CG    
5067 C CD1   . TYR   F 145 ? 0.6677 0.2663 0.4130 -0.0672 -0.0260 0.0024  145 TYR   F CD1   
5068 C CD2   . TYR   F 145 ? 0.6109 0.2864 0.3976 -0.0858 -0.0261 0.0199  145 TYR   F CD2   
5069 C CE1   . TYR   F 145 ? 0.6587 0.2704 0.4039 -0.0785 -0.0276 -0.0053 145 TYR   F CE1   
5070 C CE2   . TYR   F 145 ? 0.5933 0.2836 0.3840 -0.0960 -0.0288 0.0136  145 TYR   F CE2   
5071 C CZ    . TYR   F 145 ? 0.6189 0.2774 0.3873 -0.0928 -0.0301 0.0011  145 TYR   F CZ    
5072 O OH    . TYR   F 145 ? 0.6163 0.2881 0.3839 -0.1044 -0.0338 -0.0042 145 TYR   F OH    
5073 N N     . TYR   F 146 ? 0.7911 0.2772 0.4821 -0.0717 -0.0317 0.0215  146 TYR   F N     
5074 C CA    . TYR   F 146 ? 0.8905 0.3131 0.5474 -0.0809 -0.0345 0.0167  146 TYR   F CA    
5075 C C     . TYR   F 146 ? 0.9167 0.3141 0.5627 -0.0606 -0.0302 -0.0008 146 TYR   F C     
5076 O O     . TYR   F 146 ? 0.9020 0.3128 0.5627 -0.0322 -0.0253 -0.0034 146 TYR   F O     
5077 C CB    . TYR   F 146 ? 0.9358 0.3187 0.5760 -0.0782 -0.0364 0.0300  146 TYR   F CB    
5078 C CG    . TYR   F 146 ? 1.0158 0.3236 0.6205 -0.0769 -0.0379 0.0259  146 TYR   F CG    
5079 C CD1   . TYR   F 146 ? 1.0945 0.3626 0.6740 -0.1072 -0.0425 0.0287  146 TYR   F CD1   
5080 C CD2   . TYR   F 146 ? 1.0355 0.3112 0.6331 -0.0454 -0.0346 0.0201  146 TYR   F CD2   
5081 C CE1   . TYR   F 146 ? 1.1741 0.3674 0.7186 -0.1068 -0.0437 0.0249  146 TYR   F CE1   
5082 C CE2   . TYR   F 146 ? 1.1243 0.3275 0.6893 -0.0419 -0.0348 0.0166  146 TYR   F CE2   
5083 C CZ    . TYR   F 146 ? 1.2042 0.3632 0.7407 -0.0729 -0.0393 0.0187  146 TYR   F CZ    
5084 O OH    . TYR   F 146 ? 1.3058 0.3875 0.8075 -0.0704 -0.0392 0.0140  146 TYR   F OH    
5085 N N     . THR   F 147 ? 0.9640 0.3241 0.5830 -0.0764 -0.0318 -0.0122 147 THR   F N     
5086 C CA    . THR   F 147 ? 1.0126 0.3429 0.6138 -0.0609 -0.0259 -0.0306 147 THR   F CA    
5087 C C     . THR   F 147 ? 1.0873 0.3389 0.6502 -0.0580 -0.0249 -0.0369 147 THR   F C     
5088 O O     . THR   F 147 ? 1.1071 0.3297 0.6543 -0.0406 -0.0173 -0.0525 147 THR   F O     
5089 C CB    . THR   F 147 ? 1.0155 0.3647 0.6113 -0.0815 -0.0284 -0.0409 147 THR   F CB    
5090 O OG1   . THR   F 147 ? 1.0525 0.3723 0.6247 -0.1148 -0.0377 -0.0388 147 THR   F OG1   
5091 C CG2   . THR   F 147 ? 0.9654 0.3881 0.5984 -0.0844 -0.0294 -0.0342 147 THR   F CG2   
5092 N N     . GLY   F 148 ? 1.1289 0.3437 0.6746 -0.0764 -0.0315 -0.0258 148 GLY   F N     
5093 C CA    . GLY   F 148 ? 1.2226 0.3578 0.7266 -0.0839 -0.0324 -0.0327 148 GLY   F CA    
5094 C C     . GLY   F 148 ? 1.2510 0.3658 0.7294 -0.1225 -0.0401 -0.0399 148 GLY   F C     
5095 O O     . GLY   F 148 ? 1.2846 0.3407 0.7332 -0.1406 -0.0447 -0.0379 148 GLY   F O     
5096 N N     . THR   F 149 ? 1.2019 0.3624 0.6910 -0.1347 -0.0421 -0.0479 149 THR   F N     
5097 C CA    . THR   F 149 ? 1.2261 0.3794 0.6958 -0.1722 -0.0522 -0.0535 149 THR   F CA    
5098 C C     . THR   F 149 ? 1.1723 0.3822 0.6726 -0.1993 -0.0612 -0.0352 149 THR   F C     
5099 O O     . THR   F 149 ? 1.2389 0.4343 0.7258 -0.2344 -0.0715 -0.0323 149 THR   F O     
5100 C CB    . THR   F 149 ? 1.2145 0.3809 0.6741 -0.1691 -0.0500 -0.0721 149 THR   F CB    
5101 O OG1   . THR   F 149 ? 1.2050 0.3526 0.6591 -0.1321 -0.0361 -0.0842 149 THR   F OG1   
5102 C CG2   . THR   F 149 ? 1.3048 0.4213 0.7201 -0.1999 -0.0587 -0.0857 149 THR   F CG2   
5103 N N     . ALA   F 150 ? 1.0936 0.3679 0.6352 -0.1837 -0.0571 -0.0237 150 ALA   F N     
5104 C CA    . ALA   F 150 ? 1.0285 0.3584 0.6017 -0.2043 -0.0623 -0.0065 150 ALA   F CA    
5105 C C     . ALA   F 150 ? 0.9754 0.3445 0.5800 -0.1814 -0.0549 0.0067  150 ALA   F C     
5106 O O     . ALA   F 150 ? 0.9457 0.3107 0.5534 -0.1496 -0.0476 0.0022  150 ALA   F O     
5107 C CB    . ALA   F 150 ? 0.9837 0.3650 0.5743 -0.2180 -0.0678 -0.0106 150 ALA   F CB    
5108 N N     . VAL   F 151 ? 0.9438 0.3526 0.5717 -0.1995 -0.0568 0.0229  151 VAL   F N     
5109 C CA    . VAL   F 151 ? 0.8892 0.3417 0.5458 -0.1833 -0.0503 0.0351  151 VAL   F CA    
5110 C C     . VAL   F 151 ? 0.8284 0.3489 0.5200 -0.1977 -0.0510 0.0416  151 VAL   F C     
5111 O O     . VAL   F 151 ? 0.8238 0.3527 0.5176 -0.2269 -0.0576 0.0451  151 VAL   F O     
5112 C CB    . VAL   F 151 ? 0.9254 0.3484 0.5700 -0.1856 -0.0485 0.0503  151 VAL   F CB    
5113 C CG1   . VAL   F 151 ? 0.9564 0.3677 0.5934 -0.2221 -0.0531 0.0615  151 VAL   F CG1   
5114 C CG2   . VAL   F 151 ? 0.8872 0.3512 0.5548 -0.1681 -0.0419 0.0616  151 VAL   F CG2   
5115 N N     . ASP   F 152 ? 0.7901 0.3575 0.5093 -0.1758 -0.0444 0.0429  152 ASP   F N     
5116 C CA    . ASP   F 152 ? 0.7442 0.3753 0.4992 -0.1818 -0.0417 0.0510  152 ASP   F CA    
5117 C C     . ASP   F 152 ? 0.7366 0.3787 0.4989 -0.1788 -0.0346 0.0650  152 ASP   F C     
5118 O O     . ASP   F 152 ? 0.7380 0.3682 0.4937 -0.1557 -0.0307 0.0640  152 ASP   F O     
5119 C CB    . ASP   F 152 ? 0.6914 0.3583 0.4667 -0.1595 -0.0385 0.0417  152 ASP   F CB    
5120 C CG    . ASP   F 152 ? 0.6322 0.3615 0.4449 -0.1576 -0.0336 0.0488  152 ASP   F CG    
5121 O OD1   . ASP   F 152 ? 0.6470 0.4023 0.4755 -0.1780 -0.0340 0.0596  152 ASP   F OD1   
5122 O OD2   . ASP   F 152 ? 0.5833 0.3339 0.4097 -0.1357 -0.0287 0.0437  152 ASP   F OD2   
5123 N N     . VAL   F 153 ? 0.7446 0.4116 0.5207 -0.2016 -0.0329 0.0781  153 VAL   F N     
5124 C CA    . VAL   F 153 ? 0.7306 0.4156 0.5142 -0.2002 -0.0237 0.0916  153 VAL   F CA    
5125 C C     . VAL   F 153 ? 0.6596 0.4110 0.4824 -0.2013 -0.0173 0.0950  153 VAL   F C     
5126 O O     . VAL   F 153 ? 0.6537 0.4316 0.4957 -0.2216 -0.0205 0.0983  153 VAL   F O     
5127 C CB    . VAL   F 153 ? 0.7944 0.4485 0.5590 -0.2250 -0.0238 0.1055  153 VAL   F CB    
5128 C CG1   . VAL   F 153 ? 0.7962 0.4617 0.5600 -0.2206 -0.0132 0.1192  153 VAL   F CG1   
5129 C CG2   . VAL   F 153 ? 0.8561 0.4389 0.5819 -0.2265 -0.0316 0.1012  153 VAL   F CG2   
5130 N N     . GLU   F 154 ? 0.6149 0.3920 0.4495 -0.1790 -0.0088 0.0940  154 GLU   F N     
5131 C CA    . GLU   F 154 ? 0.5651 0.3993 0.4349 -0.1746 -0.0013 0.0950  154 GLU   F CA    
5132 C C     . GLU   F 154 ? 0.5530 0.4049 0.4258 -0.1749 0.0114  0.1059  154 GLU   F C     
5133 O O     . GLU   F 154 ? 0.5456 0.3814 0.4007 -0.1588 0.0147  0.1049  154 GLU   F O     
5134 C CB    . GLU   F 154 ? 0.5373 0.3867 0.4180 -0.1492 -0.0013 0.0826  154 GLU   F CB    
5135 C CG    . GLU   F 154 ? 0.5413 0.3692 0.4131 -0.1453 -0.0115 0.0709  154 GLU   F CG    
5136 C CD    . GLU   F 154 ? 0.5110 0.3660 0.4020 -0.1262 -0.0104 0.0612  154 GLU   F CD    
5137 O OE1   . GLU   F 154 ? 0.4991 0.3859 0.4098 -0.1140 -0.0024 0.0621  154 GLU   F OE1   
5138 O OE2   . GLU   F 154 ? 0.4945 0.3391 0.3804 -0.1251 -0.0170 0.0528  154 GLU   F OE2   
5139 N N     . GLN   F 155 ? 0.5557 0.4436 0.4520 -0.1927 0.0184  0.1161  155 GLN   F N     
5140 C CA    . GLN   F 155 ? 0.5655 0.4753 0.4665 -0.1951 0.0337  0.1267  155 GLN   F CA    
5141 C C     . GLN   F 155 ? 0.5103 0.4705 0.4439 -0.1801 0.0444  0.1227  155 GLN   F C     
5142 O O     . GLN   F 155 ? 0.4819 0.4701 0.4441 -0.1790 0.0402  0.1185  155 GLN   F O     
5143 C CB    . GLN   F 155 ? 0.5883 0.5081 0.4976 -0.2249 0.0373  0.1415  155 GLN   F CB    
5144 C CG    . GLN   F 155 ? 0.6455 0.5115 0.5215 -0.2430 0.0273  0.1465  155 GLN   F CG    
5145 C CD    . GLN   F 155 ? 0.6692 0.5481 0.5575 -0.2758 0.0296  0.1609  155 GLN   F CD    
5146 O OE1   . GLN   F 155 ? 0.6702 0.5472 0.5676 -0.2942 0.0176  0.1597  155 GLN   F OE1   
5147 N NE2   . GLN   F 155 ? 0.6836 0.5794 0.5739 -0.2841 0.0451  0.1743  155 GLN   F NE2   
5148 N N     . PRO   F 156 ? 0.5098 0.4816 0.4385 -0.1691 0.0588  0.1245  156 PRO   F N     
5149 C CA    . PRO   F 156 ? 0.4686 0.4856 0.4273 -0.1568 0.0718  0.1213  156 PRO   F CA    
5150 C C     . PRO   F 156 ? 0.4685 0.5287 0.4615 -0.1738 0.0825  0.1330  156 PRO   F C     
5151 O O     . PRO   F 156 ? 0.5123 0.5668 0.4976 -0.1948 0.0858  0.1452  156 PRO   F O     
5152 C CB    . PRO   F 156 ? 0.4870 0.4925 0.4195 -0.1434 0.0825  0.1193  156 PRO   F CB    
5153 C CG    . PRO   F 156 ? 0.5336 0.5064 0.4337 -0.1597 0.0817  0.1310  156 PRO   F CG    
5154 C CD    . PRO   F 156 ? 0.5432 0.4833 0.4347 -0.1684 0.0634  0.1301  156 PRO   F CD    
5155 N N     . VAL   F 157 ? 0.4238 0.5273 0.4556 -0.1643 0.0884  0.1302  157 VAL   F N     
5156 C CA    . VAL   F 157 ? 0.4201 0.5717 0.4931 -0.1775 0.0976  0.1416  157 VAL   F CA    
5157 C C     . VAL   F 157 ? 0.4577 0.6260 0.5295 -0.1831 0.1202  0.1512  157 VAL   F C     
5158 O O     . VAL   F 157 ? 0.4593 0.6618 0.5602 -0.2003 0.1277  0.1639  157 VAL   F O     
5159 C CB    . VAL   F 157 ? 0.3800 0.5717 0.4943 -0.1619 0.0988  0.1371  157 VAL   F CB    
5160 C CG1   . VAL   F 157 ? 0.3629 0.5646 0.4787 -0.1370 0.1163  0.1286  157 VAL   F CG1   
5161 C CG2   . VAL   F 157 ? 0.3705 0.6125 0.5326 -0.1775 0.1006  0.1506  157 VAL   F CG2   
5162 N N     . THR   F 158 ? 0.4862 0.6323 0.5250 -0.1692 0.1307  0.1452  158 THR   F N     
5163 C CA    . THR   F 158 ? 0.5184 0.6674 0.5398 -0.1742 0.1513  0.1528  158 THR   F CA    
5164 C C     . THR   F 158 ? 0.5702 0.7044 0.5764 -0.2020 0.1504  0.1686  158 THR   F C     
5165 O O     . THR   F 158 ? 0.5976 0.7474 0.6011 -0.2100 0.1704  0.1781  158 THR   F O     
5166 C CB    . THR   F 158 ? 0.5246 0.6408 0.5025 -0.1560 0.1549  0.1423  158 THR   F CB    
5167 O OG1   . THR   F 158 ? 0.5266 0.5980 0.4747 -0.1528 0.1332  0.1365  158 THR   F OG1   
5168 C CG2   . THR   F 158 ? 0.4944 0.6295 0.4859 -0.1315 0.1642  0.1283  158 THR   F CG2   
5169 N N     . TYR   F 159 ? 0.5968 0.6997 0.5912 -0.2164 0.1294  0.1709  159 TYR   F N     
5170 C CA    . TYR   F 159 ? 0.6388 0.7281 0.6250 -0.2461 0.1266  0.1861  159 TYR   F CA    
5171 C C     . TYR   F 159 ? 0.6498 0.7874 0.6852 -0.2680 0.1288  0.1971  159 TYR   F C     
5172 O O     . TYR   F 159 ? 0.6957 0.8256 0.7266 -0.2954 0.1285  0.2107  159 TYR   F O     
5173 C CB    . TYR   F 159 ? 0.6473 0.6769 0.5962 -0.2495 0.1042  0.1816  159 TYR   F CB    
5174 C CG    . TYR   F 159 ? 0.6545 0.6348 0.5535 -0.2344 0.1018  0.1773  159 TYR   F CG    
5175 C CD1   . TYR   F 159 ? 0.6740 0.6595 0.5554 -0.2187 0.1169  0.1759  159 TYR   F CD1   
5176 C CD2   . TYR   F 159 ? 0.6725 0.5989 0.5401 -0.2357 0.0833  0.1748  159 TYR   F CD2   
5177 C CE1   . TYR   F 159 ? 0.6910 0.6329 0.5269 -0.2067 0.1114  0.1737  159 TYR   F CE1   
5178 C CE2   . TYR   F 159 ? 0.7013 0.5846 0.5270 -0.2213 0.0791  0.1728  159 TYR   F CE2   
5179 C CZ    . TYR   F 159 ? 0.7084 0.6009 0.5187 -0.2073 0.0920  0.1729  159 TYR   F CZ    
5180 O OH    . TYR   F 159 ? 0.7175 0.5711 0.4876 -0.1943 0.0857  0.1726  159 TYR   F OH    
5181 N N     . ARG   F 160 ? 0.6119 0.7997 0.6947 -0.2576 0.1314  0.1934  160 ARG   F N     
5182 C CA    . ARG   F 160 ? 0.6167 0.8582 0.7520 -0.2762 0.1330  0.2054  160 ARG   F CA    
5183 C C     . ARG   F 160 ? 0.6559 0.9251 0.8024 -0.2939 0.1563  0.2218  160 ARG   F C     
5184 O O     . ARG   F 160 ? 0.6624 0.9403 0.7999 -0.2791 0.1794  0.2208  160 ARG   F O     
5185 C CB    . ARG   F 160 ? 0.5729 0.8652 0.7564 -0.2557 0.1365  0.2002  160 ARG   F CB    
5186 C CG    . ARG   F 160 ? 0.5643 0.9152 0.8068 -0.2720 0.1331  0.2128  160 ARG   F CG    
5187 C CD    . ARG   F 160 ? 0.5402 0.9517 0.8380 -0.2518 0.1443  0.2136  160 ARG   F CD    
5188 N NE    . ARG   F 160 ? 0.5356 0.9467 0.8414 -0.2249 0.1349  0.2009  160 ARG   F NE    
5189 C CZ    . ARG   F 160 ? 0.5361 0.9201 0.8272 -0.2205 0.1108  0.1915  160 ARG   F CZ    
5190 N NH1   . ARG   F 160 ? 0.5834 0.9186 0.8339 -0.2355 0.0918  0.1870  160 ARG   F NH1   
5191 N NH2   . ARG   F 160 ? 0.5130 0.9162 0.8282 -0.1985 0.1071  0.1858  160 ARG   F NH2   
5192 N N     . GLY   F 161 ? 0.6832 0.9631 0.8457 -0.3268 0.1502  0.2365  161 GLY   F N     
5193 C CA    . GLY   F 161 ? 0.7297 1.0324 0.9013 -0.3493 0.1708  0.2542  161 GLY   F CA    
5194 C C     . GLY   F 161 ? 0.7873 1.0308 0.9010 -0.3651 0.1722  0.2604  161 GLY   F C     
5195 O O     . GLY   F 161 ? 0.7993 1.0572 0.9177 -0.3885 0.1875  0.2770  161 GLY   F O     
5196 N N     . ARG   F 162 ? 0.8037 0.9828 0.8655 -0.3522 0.1568  0.2486  162 ARG   F N     
5197 C CA    . ARG   F 162 ? 0.8472 0.9631 0.8520 -0.3627 0.1536  0.2539  162 ARG   F CA    
5198 C C     . ARG   F 162 ? 0.8532 0.9127 0.8318 -0.3704 0.1248  0.2472  162 ARG   F C     
5199 O O     . ARG   F 162 ? 0.8993 0.9001 0.8297 -0.3737 0.1194  0.2497  162 ARG   F O     
5200 C CB    . ARG   F 162 ? 0.8536 0.9480 0.8199 -0.3339 0.1656  0.2456  162 ARG   F CB    
5201 C CG    . ARG   F 162 ? 0.8690 1.0084 0.8491 -0.3276 0.1965  0.2514  162 ARG   F CG    
5202 C CD    . ARG   F 162 ? 0.8909 1.0061 0.8279 -0.3017 0.2064  0.2422  162 ARG   F CD    
5203 N NE    . ARG   F 162 ? 0.8544 0.9618 0.7908 -0.2717 0.1938  0.2218  162 ARG   F NE    
5204 C CZ    . ARG   F 162 ? 0.8842 0.9503 0.7777 -0.2514 0.1854  0.2108  162 ARG   F CZ    
5205 N NH1   . ARG   F 162 ? 0.8779 0.9556 0.7817 -0.2252 0.1835  0.1938  162 ARG   F NH1   
5206 N NH2   . ARG   F 162 ? 0.9351 0.9517 0.7768 -0.2558 0.1803  0.2171  162 ARG   F NH2   
5207 N N     . ALA   F 163 ? 0.8051 0.8804 0.8136 -0.3745 0.1068  0.2399  163 ALA   F N     
5208 C CA    . ALA   F 163 ? 0.8067 0.8297 0.7891 -0.3764 0.0814  0.2294  163 ALA   F CA    
5209 C C     . ALA   F 163 ? 0.8386 0.8322 0.8094 -0.4141 0.0717  0.2412  163 ALA   F C     
5210 O O     . ALA   F 163 ? 0.8657 0.9034 0.8738 -0.4395 0.0761  0.2535  163 ALA   F O     
5211 C CB    . ALA   F 163 ? 0.7664 0.8203 0.7824 -0.3663 0.0677  0.2173  163 ALA   F CB    
5212 N N     . THR   F 164 ? 0.8651 0.7859 0.7869 -0.4174 0.0587  0.2376  164 THR   F N     
5213 C CA    . THR   F 164 ? 0.9161 0.7947 0.8190 -0.4523 0.0477  0.2465  164 THR   F CA    
5214 C C     . THR   F 164 ? 0.9148 0.7387 0.7908 -0.4480 0.0242  0.2301  164 THR   F C     
5215 O O     . THR   F 164 ? 0.8631 0.6863 0.7367 -0.4180 0.0192  0.2142  164 THR   F O     
5216 C CB    . THR   F 164 ? 0.9672 0.8061 0.8327 -0.4619 0.0601  0.2620  164 THR   F CB    
5217 N N     . GLY   F 165 ? 0.9515 0.7326 0.8096 -0.4790 0.0108  0.2334  165 GLY   F N     
5218 C CA    . GLY   F 165 ? 0.9854 0.7042 0.8099 -0.4767 -0.0090 0.2177  165 GLY   F CA    
5219 C C     . GLY   F 165 ? 0.9695 0.7178 0.8206 -0.4869 -0.0252 0.2064  165 GLY   F C     
5220 O O     . GLY   F 165 ? 0.9314 0.7513 0.8304 -0.4925 -0.0219 0.2116  165 GLY   F O     
5221 N N     . LEU   F 166 ? 1.0054 0.6961 0.8231 -0.4883 -0.0423 0.1914  166 LEU   F N     
5222 C CA    . LEU   F 166 ? 1.0029 0.7074 0.8327 -0.5003 -0.0603 0.1795  166 LEU   F CA    
5223 C C     . LEU   F 166 ? 0.9282 0.6915 0.7911 -0.4726 -0.0598 0.1704  166 LEU   F C     
5224 O O     . LEU   F 166 ? 0.9296 0.7322 0.8195 -0.4874 -0.0716 0.1690  166 LEU   F O     
5225 C CB    . LEU   F 166 ? 1.0597 0.6822 0.8386 -0.5038 -0.0753 0.1634  166 LEU   F CB    
5226 C CG    . LEU   F 166 ? 1.1301 0.6899 0.8766 -0.5383 -0.0805 0.1708  166 LEU   F CG    
5227 C CD1   . LEU   F 166 ? 1.1755 0.6525 0.8705 -0.5340 -0.0930 0.1516  166 LEU   F CD1   
5228 C CD2   . LEU   F 166 ? 1.1477 0.7426 0.9226 -0.5851 -0.0887 0.1835  166 LEU   F CD2   
5229 N N     . CYS   F 167 ? 0.8793 0.6504 0.7413 -0.4347 -0.0472 0.1657  167 CYS   F N     
5230 C CA    . CYS   F 167 ? 0.8047 0.6301 0.6985 -0.4087 -0.0448 0.1585  167 CYS   F CA    
5231 C C     . CYS   F 167 ? 0.7830 0.6894 0.7326 -0.4178 -0.0364 0.1728  167 CYS   F C     
5232 O O     . CYS   F 167 ? 0.7112 0.6651 0.6927 -0.4070 -0.0402 0.1690  167 CYS   F O     
5233 C CB    . CYS   F 167 ? 0.7620 0.5715 0.6394 -0.3693 -0.0342 0.1500  167 CYS   F CB    
5234 S SG    . CYS   F 167 ? 0.7850 0.5087 0.6061 -0.3536 -0.0436 0.1330  167 CYS   F SG    
5235 N N     . GLY   F 168 ? 0.8223 0.7448 0.7845 -0.4373 -0.0245 0.1899  168 GLY   F N     
5236 C CA    . GLY   F 168 ? 0.8130 0.8070 0.8283 -0.4573 -0.0199 0.2049  168 GLY   F CA    
5237 C C     . GLY   F 168 ? 0.7719 0.8285 0.8265 -0.4290 -0.0022 0.2073  168 GLY   F C     
5238 O O     . GLY   F 168 ? 0.7439 0.7848 0.7796 -0.4020 0.0120  0.2029  168 GLY   F O     
5239 N N     . ASN   F 169 ? 0.7732 0.8984 0.8813 -0.4357 -0.0042 0.2143  169 ASN   F N     
5240 C CA    . ASN   F 169 ? 0.7585 0.9474 0.9107 -0.4118 0.0132  0.2183  169 ASN   F CA    
5241 C C     . ASN   F 169 ? 0.7528 0.9284 0.8905 -0.3725 0.0145  0.2018  169 ASN   F C     
5242 O O     . ASN   F 169 ? 0.7127 0.8531 0.8252 -0.3664 -0.0028 0.1887  169 ASN   F O     
5243 C CB    . ASN   F 169 ? 0.7522 1.0133 0.9650 -0.4257 0.0064  0.2289  169 ASN   F CB    
5244 N N     . LEU   F 170 ? 0.7544 0.9575 0.9072 -0.3474 0.0362  0.2026  170 LEU   F N     
5245 C CA    . LEU   F 170 ? 0.7624 0.9717 0.9176 -0.3121 0.0398  0.1899  170 LEU   F CA    
5246 C C     . LEU   F 170 ? 0.8135 1.0952 1.0289 -0.3051 0.0463  0.1975  170 LEU   F C     
5247 O O     . LEU   F 170 ? 0.8925 1.2136 1.1363 -0.3056 0.0664  0.2080  170 LEU   F O     
5248 C CB    . LEU   F 170 ? 0.7386 0.9193 0.8616 -0.2914 0.0580  0.1848  170 LEU   F CB    
5249 C CG    . LEU   F 170 ? 0.7652 0.8786 0.8331 -0.2995 0.0531  0.1823  170 LEU   F CG    
5250 C CD1   . LEU   F 170 ? 0.7633 0.8542 0.8016 -0.2771 0.0683  0.1778  170 LEU   F CD1   
5251 C CD2   . LEU   F 170 ? 0.7559 0.8215 0.7944 -0.2995 0.0309  0.1701  170 LEU   F CD2   
5252 N N     . ASN   F 171 ? 0.8770 1.1772 1.1128 -0.3017 0.0287  0.1941  171 ASN   F N     
5253 C CA    . ASN   F 171 ? 0.8545 1.2199 1.1472 -0.2914 0.0313  0.2015  171 ASN   F CA    
5254 C C     . ASN   F 171 ? 0.7954 1.1531 1.0844 -0.2702 0.0173  0.1903  171 ASN   F C     
5255 O O     . ASN   F 171 ? 0.8317 1.1793 1.1130 -0.2852 -0.0063 0.1890  171 ASN   F O     
5256 C CB    . ASN   F 171 ? 0.8666 1.2793 1.2018 -0.3217 0.0206  0.2181  171 ASN   F CB    
5257 C CG    . ASN   F 171 ? 0.8763 1.3147 1.2308 -0.3388 0.0401  0.2321  171 ASN   F CG    
5258 O OD1   . ASN   F 171 ? 0.8437 1.3180 1.2257 -0.3210 0.0648  0.2366  171 ASN   F OD1   
5259 N ND2   . ASN   F 171 ? 0.8996 1.3163 1.2365 -0.3728 0.0311  0.2384  171 ASN   F ND2   
5260 C C1    . LUT   G .   ? 0.3592 0.3933 0.4829 -0.0791 0.0022  0.0090  201 LUT   A C1    
5261 C C2    . LUT   G .   ? 0.3827 0.3920 0.5061 -0.0938 -0.0058 0.0105  201 LUT   A C2    
5262 C C3    . LUT   G .   ? 0.3931 0.4192 0.5286 -0.1122 -0.0062 0.0148  201 LUT   A C3    
5263 C C4    . LUT   G .   ? 0.3651 0.4303 0.5125 -0.1092 -0.0004 0.0116  201 LUT   A C4    
5264 C C5    . LUT   G .   ? 0.3469 0.4326 0.4923 -0.0975 0.0097  0.0174  201 LUT   A C5    
5265 C C6    . LUT   G .   ? 0.3464 0.4171 0.4801 -0.0828 0.0104  0.0142  201 LUT   A C6    
5266 C C7    . LUT   G .   ? 0.3399 0.4299 0.4703 -0.0703 0.0183  0.0156  201 LUT   A C7    
5267 C C8    . LUT   G .   ? 0.3287 0.4151 0.4511 -0.0556 0.0188  0.0094  201 LUT   A C8    
5268 C C9    . LUT   G .   ? 0.3479 0.4518 0.4668 -0.0461 0.0252  0.0099  201 LUT   A C9    
5269 C C10   . LUT   G .   ? 0.3374 0.4318 0.4460 -0.0344 0.0240  0.0061  201 LUT   A C10   
5270 C C11   . LUT   G .   ? 0.3325 0.4366 0.4348 -0.0250 0.0276  0.0043  201 LUT   A C11   
5271 C C12   . LUT   G .   ? 0.3347 0.4298 0.4252 -0.0164 0.0261  0.0031  201 LUT   A C12   
5272 C C13   . LUT   G .   ? 0.3176 0.4180 0.3979 -0.0087 0.0291  0.0025  201 LUT   A C13   
5273 C C14   . LUT   G .   ? 0.3183 0.4088 0.3899 -0.0028 0.0244  -0.0010 201 LUT   A C14   
5274 C C15   . LUT   G .   ? 0.3369 0.4268 0.3971 0.0034  0.0242  -0.0032 201 LUT   A C15   
5275 C C16   . LUT   G .   ? 0.3604 0.3804 0.4719 -0.0714 0.0042  0.0168  201 LUT   A C16   
5276 C C17   . LUT   G .   ? 0.3627 0.3956 0.4860 -0.0665 -0.0014 -0.0060 201 LUT   A C17   
5277 C C18   . LUT   G .   ? 0.3234 0.4472 0.4803 -0.1022 0.0177  0.0252  201 LUT   A C18   
5278 C C19   . LUT   G .   ? 0.3244 0.4570 0.4493 -0.0471 0.0329  0.0146  201 LUT   A C19   
5279 C C20   . LUT   G .   ? 0.2975 0.4137 0.3753 -0.0069 0.0369  0.0063  201 LUT   A C20   
5280 O O3    . LUT   G .   ? 0.4072 0.4079 0.5409 -0.1205 -0.0168 0.0068  201 LUT   A O3    
5281 C C21   . LUT   G .   ? 0.5997 0.5727 0.5085 0.0094  -0.0295 -0.0307 201 LUT   A C21   
5282 C C22   . LUT   G .   ? 0.6653 0.6123 0.5514 0.0102  -0.0341 -0.0357 201 LUT   A C22   
5283 C C23   . LUT   G .   ? 0.6971 0.6413 0.5904 -0.0026 -0.0436 -0.0348 201 LUT   A C23   
5284 C C24   . LUT   G .   ? 0.6470 0.6195 0.5722 -0.0079 -0.0402 -0.0303 201 LUT   A C24   
5285 C C25   . LUT   G .   ? 0.5963 0.5907 0.5409 -0.0028 -0.0314 -0.0281 201 LUT   A C25   
5286 C C26   . LUT   G .   ? 0.5627 0.5578 0.5009 0.0063  -0.0247 -0.0280 201 LUT   A C26   
5287 C C27   . LUT   G .   ? 0.4955 0.5116 0.4546 0.0048  -0.0225 -0.0241 201 LUT   A C27   
5288 C C28   . LUT   G .   ? 0.4317 0.4614 0.4055 0.0092  -0.0138 -0.0222 201 LUT   A C28   
5289 C C29   . LUT   G .   ? 0.4009 0.4439 0.3905 0.0087  -0.0120 -0.0189 201 LUT   A C29   
5290 C C30   . LUT   G .   ? 0.3876 0.4390 0.3873 0.0123  -0.0030 -0.0174 201 LUT   A C30   
5291 C C31   . LUT   G .   ? 0.3878 0.4490 0.4032 0.0116  -0.0005 -0.0148 201 LUT   A C31   
5292 C C32   . LUT   G .   ? 0.4039 0.4706 0.4262 0.0129  0.0071  -0.0127 201 LUT   A C32   
5293 C C33   . LUT   G .   ? 0.4155 0.4869 0.4507 0.0110  0.0089  -0.0098 201 LUT   A C33   
5294 C C34   . LUT   G .   ? 0.3826 0.4607 0.4245 0.0100  0.0161  -0.0079 201 LUT   A C34   
5295 C C35   . LUT   G .   ? 0.3481 0.4295 0.4021 0.0063  0.0180  -0.0059 201 LUT   A C35   
5296 C C36   . LUT   G .   ? 0.6244 0.5985 0.5314 0.0013  -0.0401 -0.0288 201 LUT   A C36   
5297 C C37   . LUT   G .   ? 0.6097 0.5853 0.5111 0.0203  -0.0195 -0.0297 201 LUT   A C37   
5298 C C38   . LUT   G .   ? 0.5723 0.5903 0.5440 -0.0059 -0.0276 -0.0256 201 LUT   A C38   
5299 C C39   . LUT   G .   ? 0.3907 0.4382 0.3853 0.0050  -0.0200 -0.0165 201 LUT   A C39   
5300 C C40   . LUT   G .   ? 0.4019 0.4703 0.4422 0.0104  0.0027  -0.0083 201 LUT   A C40   
5301 O O23   . LUT   G .   ? 0.7011 0.6210 0.5769 -0.0001 -0.0451 -0.0383 201 LUT   A O23   
5308 C C1    . PLC   J .   ? 0.2084 0.3401 0.2986 0.0069  0.0247  -0.0232 201 PLC   C C1    
5309 C C2    . PLC   J .   ? 0.2441 0.3668 0.3312 0.0045  0.0248  -0.0193 201 PLC   C C2    
5310 C C3    . PLC   J .   ? 0.2754 0.4041 0.3679 0.0003  0.0291  -0.0144 201 PLC   C C3    
5311 C C4    . PLC   J .   ? 0.1513 0.3180 0.2557 0.0120  0.0276  -0.0271 201 PLC   C C4    
5312 C C5    . PLC   J .   ? 0.1550 0.3220 0.2529 0.0179  0.0270  -0.0274 201 PLC   C C5    
5313 C C6    . PLC   J .   ? 0.1568 0.3322 0.2480 0.0300  0.0283  -0.0252 201 PLC   C C6    
5314 C C7    . PLC   J .   ? 0.1446 0.3455 0.2610 0.0181  0.0291  -0.0268 201 PLC   C C7    
5315 C C8    . PLC   J .   ? 0.1537 0.3385 0.2510 0.0288  0.0358  -0.0215 201 PLC   C C8    
5316 C "C'"  . PLC   J .   ? 0.2992 0.4020 0.3628 0.0102  0.0198  -0.0191 201 PLC   C "C'"  
5317 C "C1'" . PLC   J .   ? 0.3156 0.4069 0.3620 0.0136  0.0174  -0.0193 201 PLC   C "C1'" 
5318 C "C2'" . PLC   J .   ? 0.3221 0.4082 0.3665 0.0112  0.0098  -0.0218 201 PLC   C "C2'" 
5319 C "C3'" . PLC   J .   ? 0.3184 0.4152 0.3785 0.0077  0.0068  -0.0240 201 PLC   C "C3'" 
5320 C "C4'" . PLC   J .   ? 0.3208 0.4190 0.3880 0.0066  0.0034  -0.0234 201 PLC   C "C4'" 
5321 C "C5'" . PLC   J .   ? 0.2981 0.4059 0.3805 0.0063  0.0047  -0.0261 201 PLC   C "C5'" 
5322 C "C6'" . PLC   J .   ? 0.2758 0.3935 0.3668 0.0063  0.0007  -0.0287 201 PLC   C "C6'" 
5323 C "C7'" . PLC   J .   ? 0.2447 0.3728 0.3466 0.0069  0.0027  -0.0332 201 PLC   C "C7'" 
5324 C "C8'" . PLC   J .   ? 0.2305 0.3713 0.3404 0.0086  0.0001  -0.0357 201 PLC   C "C8'" 
5325 C "C9'" . PLC   J .   ? 0.2298 0.3744 0.3381 0.0080  -0.0045 -0.0323 201 PLC   C "C9'" 
5326 C "CA'" . PLC   J .   ? 0.2223 0.3855 0.3408 0.0104  -0.0060 -0.0340 201 PLC   C "CA'" 
5327 C "CB'" . PLC   J .   ? 0.2068 0.3837 0.3267 0.0050  -0.0064 -0.0320 201 PLC   C "CB'" 
5328 C CB    . PLC   J .   ? 0.3167 0.4333 0.4216 -0.0078 0.0213  -0.0182 201 PLC   C CB    
5329 C C1B   . PLC   J .   ? 0.2974 0.4173 0.4131 -0.0120 0.0184  -0.0235 201 PLC   C C1B   
5330 C C2B   . PLC   J .   ? 0.3055 0.4119 0.4217 -0.0110 0.0129  -0.0278 201 PLC   C C2B   
5331 C C3B   . PLC   J .   ? 0.3001 0.4023 0.4231 -0.0172 0.0099  -0.0315 201 PLC   C C3B   
5332 C C4B   . PLC   J .   ? 0.3185 0.4127 0.4420 -0.0260 0.0106  -0.0244 201 PLC   C C4B   
5333 C C5B   . PLC   J .   ? 0.3366 0.4081 0.4583 -0.0291 0.0048  -0.0260 201 PLC   C C5B   
5334 C C6B   . PLC   J .   ? 0.3441 0.4000 0.4581 -0.0200 0.0019  -0.0263 201 PLC   C C6B   
5335 C C7B   . PLC   J .   ? 0.3513 0.3906 0.4641 -0.0155 -0.0043 -0.0344 201 PLC   C C7B   
5336 C C8B   . PLC   J .   ? 0.3810 0.3925 0.4879 -0.0190 -0.0088 -0.0303 201 PLC   C C8B   
5337 C C9B   . PLC   J .   ? 0.3945 0.3999 0.4953 -0.0200 -0.0067 -0.0185 201 PLC   C C9B   
5338 C CAA   . PLC   J .   ? 0.3770 0.4046 0.4779 -0.0174 -0.0005 -0.0144 201 PLC   C CAA   
5339 C CBA   . PLC   J .   ? 0.3795 0.4071 0.4754 -0.0239 0.0038  -0.0024 201 PLC   C CBA   
5340 O "O'"  . PLC   J .   ? 0.3982 0.4995 0.4681 0.0076  0.0160  -0.0199 201 PLC   C "O'"  
5341 O OB    . PLC   J .   ? 0.3690 0.4741 0.4664 -0.0054 0.0193  -0.0162 201 PLC   C OB    
5342 O O2    . PLC   J .   ? 0.2848 0.3984 0.3557 0.0097  0.0254  -0.0175 201 PLC   C O2    
5343 O O3    . PLC   J .   ? 0.3292 0.4580 0.4333 -0.0067 0.0265  -0.0155 201 PLC   C O3    
5344 O O1P   . PLC   J .   ? 0.1579 0.3014 0.2639 0.0039  0.0172  -0.0334 201 PLC   C O1P   
5345 O O2P   . PLC   J .   ? 0.1272 0.2886 0.2473 -0.0011 0.0215  -0.0327 201 PLC   C O2P   
5346 O O3P   . PLC   J .   ? 0.1708 0.3158 0.2739 0.0037  0.0252  -0.0253 201 PLC   C O3P   
5347 O O4P   . PLC   J .   ? 0.1530 0.3075 0.2545 0.0091  0.0234  -0.0295 201 PLC   C O4P   
5348 N N     . PLC   J .   ? 0.1521 0.3342 0.2532 0.0236  0.0302  -0.0253 201 PLC   C N     
5349 P P     . PLC   J .   ? 0.1504 0.3011 0.2588 0.0036  0.0215  -0.0308 201 PLC   C P     
5350 C C1    . A1L6M K .   ? 0.2682 0.3041 0.2664 0.0117  0.0195  -0.0068 202 A1L6M C C1    
5351 C C2    . A1L6M K .   ? 0.2589 0.3045 0.2693 0.0151  0.0134  -0.0058 202 A1L6M C C2    
5352 C C3    . A1L6M K .   ? 0.2402 0.2884 0.2456 0.0217  0.0082  0.0019  202 A1L6M C C3    
5353 C C4    . A1L6M K .   ? 0.2728 0.3228 0.2661 0.0238  0.0045  0.0069  202 A1L6M C C4    
5354 C C5    . A1L6M K .   ? 0.2931 0.3417 0.2698 0.0187  0.0038  0.0059  202 A1L6M C C5    
5355 C C6    . A1L6M K .   ? 0.2911 0.3456 0.2897 0.0320  0.0012  0.0146  202 A1L6M C C6    
5356 O O1    . A1L6M K .   ? 0.2988 0.3575 0.2932 0.0375  -0.0029 0.0230  202 A1L6M C O1    
5357 N N1    . A1L6M K .   ? 0.2718 0.3257 0.2820 0.0340  0.0036  0.0132  202 A1L6M C N1    
5358 C C7    . A1L6M K .   ? 0.2494 0.3001 0.2641 0.0275  0.0067  0.0059  202 A1L6M C C7    
5359 C C8    . A1L6M K .   ? 0.2132 0.2632 0.2386 0.0275  0.0081  0.0046  202 A1L6M C C8    
5360 C C9    . A1L6M K .   ? 0.1812 0.2350 0.2147 0.0313  0.0072  0.0074  202 A1L6M C C9    
5361 C C10   . A1L6M K .   ? 0.1671 0.2318 0.2078 0.0366  0.0047  0.0119  202 A1L6M C C10   
5362 C C11   . A1L6M K .   ? 0.1645 0.2417 0.2079 0.0383  -0.0002 0.0152  202 A1L6M C C11   
5363 C C12   . A1L6M K .   ? 0.1670 0.2306 0.2126 0.0387  0.0068  0.0134  202 A1L6M C C12   
5364 C C13   . A1L6M K .   ? 0.1777 0.2513 0.2324 0.0442  0.0072  0.0183  202 A1L6M C C13   
5365 C C14   . A1L6M K .   ? 0.1889 0.2549 0.2346 0.0533  0.0121  0.0236  202 A1L6M C C14   
5366 C C15   . A1L6M K .   ? 0.1930 0.2689 0.2487 0.0610  0.0153  0.0297  202 A1L6M C C15   
5367 O O2    . A1L6M K .   ? 0.1941 0.2690 0.2483 0.0695  0.0182  0.0353  202 A1L6M C O2    
5368 O O3    . A1L6M K .   ? 0.1994 0.2836 0.2650 0.0589  0.0157  0.0297  202 A1L6M C O3    
5369 C C16   . A1L6M K .   ? 0.1643 0.2161 0.2043 0.0342  0.0090  0.0101  202 A1L6M C C16   
5370 N N2    . A1L6M K .   ? 0.1683 0.2162 0.2040 0.0300  0.0091  0.0068  202 A1L6M C N2    
5371 C C17   . A1L6M K .   ? 0.1547 0.2024 0.1946 0.0336  0.0104  0.0109  202 A1L6M C C17   
5372 C C18   . A1L6M K .   ? 0.1639 0.2039 0.2004 0.0283  0.0102  0.0097  202 A1L6M C C18   
5373 N N3    . A1L6M K .   ? 0.1581 0.1938 0.1947 0.0219  0.0090  0.0072  202 A1L6M C N3    
5374 C C19   . A1L6M K .   ? 0.1675 0.1984 0.2011 0.0172  0.0073  0.0083  202 A1L6M C C19   
5375 C C20   . A1L6M K .   ? 0.1714 0.1997 0.2072 0.0099  0.0050  0.0076  202 A1L6M C C20   
5376 C C21   . A1L6M K .   ? 0.1824 0.2119 0.2225 0.0026  0.0003  0.0098  202 A1L6M C C21   
5377 N N4    . A1L6M K .   ? 0.1895 0.2237 0.2329 0.0011  -0.0035 0.0133  202 A1L6M C N4    
5378 C C22   . A1L6M K .   ? 0.1951 0.2318 0.2438 -0.0070 -0.0095 0.0164  202 A1L6M C C22   
5379 O O4    . A1L6M K .   ? 0.1944 0.2355 0.2455 -0.0102 -0.0148 0.0212  202 A1L6M C O4    
5380 C C23   . A1L6M K .   ? 0.1981 0.2323 0.2485 -0.0111 -0.0089 0.0147  202 A1L6M C C23   
5381 C C24   . A1L6M K .   ? 0.2215 0.2611 0.2816 -0.0208 -0.0157 0.0189  202 A1L6M C C24   
5382 O O5    . A1L6M K .   ? 0.2101 0.2451 0.2684 -0.0256 -0.0136 0.0169  202 A1L6M C O5    
5383 C C25   . A1L6M K .   ? 0.2213 0.2790 0.3119 -0.0197 -0.0184 0.0236  202 A1L6M C C25   
5384 C C26   . A1L6M K .   ? 0.2720 0.3405 0.3806 -0.0281 -0.0254 0.0302  202 A1L6M C C26   
5385 C C27   . A1L6M K .   ? 0.3320 0.3975 0.4268 -0.0377 -0.0358 0.0354  202 A1L6M C C27   
5386 C C28   . A1L6M K .   ? 0.4538 0.5225 0.5498 -0.0490 -0.0440 0.0400  202 A1L6M C C28   
5387 C C29   . A1L6M K .   ? 0.4367 0.5144 0.5524 -0.0538 -0.0432 0.0414  202 A1L6M C C29   
5388 C C30   . A1L6M K .   ? 0.5229 0.5871 0.5994 -0.0597 -0.0554 0.0447  202 A1L6M C C30   
5389 C C31   . A1L6M K .   ? 0.6069 0.6656 0.6659 -0.0577 -0.0578 0.0464  202 A1L6M C C31   
5390 C C32   . A1L6M K .   ? 0.6675 0.7226 0.7067 -0.0718 -0.0702 0.0517  202 A1L6M C C32   
5391 C C33   . A1L6M K .   ? 0.7342 0.8054 0.7882 -0.0805 -0.0840 0.0633  202 A1L6M C C33   
5392 C C34   . A1L6M K .   ? 0.7727 0.8386 0.8017 -0.0976 -0.0977 0.0674  202 A1L6M C C34   
5393 C C35   . A1L6M K .   ? 0.7635 0.8593 0.8616 -0.0738 -0.0869 0.0738  202 A1L6M C C35   
5394 C C36   . A1L6M K .   ? 0.7918 0.8886 0.8924 -0.0641 -0.0837 0.0767  202 A1L6M C C36   
5395 C C37   . A1L6M K .   ? 0.8097 0.9264 0.9524 -0.0567 -0.0851 0.0867  202 A1L6M C C37   
5396 C C38   . A1L6M K .   ? 0.7851 0.9046 0.9415 -0.0470 -0.0806 0.0896  202 A1L6M C C38   
5397 C C39   . A1L6M K .   ? 0.7391 0.8450 0.8726 -0.0413 -0.0725 0.0830  202 A1L6M C C39   
5398 C C40   . A1L6M K .   ? 0.8227 0.9599 1.0220 -0.0410 -0.0827 0.1009  202 A1L6M C C40   
5399 C C41   . A1L6M K .   ? 0.1873 0.2160 0.2313 -0.0053 -0.0022 0.0103  202 A1L6M C C41   
5400 C C42   . A1L6M K .   ? 0.1778 0.2008 0.2183 -0.0073 0.0016  0.0078  202 A1L6M C C42   
5401 C C43   . A1L6M K .   ? 0.1914 0.2222 0.2208 0.0206  0.0083  0.0106  202 A1L6M C C43   
5402 C C44   . A1L6M K .   ? 0.2146 0.2389 0.2343 0.0164  0.0072  0.0123  202 A1L6M C C44   
5403 O O6    . A1L6M K .   ? 0.1933 0.2289 0.2267 0.0131  0.0027  0.0155  202 A1L6M C O6    
5404 C C45   . A1L6M K .   ? 0.1681 0.2052 0.2010 0.0281  0.0109  0.0117  202 A1L6M C C45   
5405 C C46   . A1L6M K .   ? 0.1927 0.2340 0.2260 0.0343  0.0143  0.0150  202 A1L6M C C46   
5406 C C47   . A1L6M K .   ? 0.1870 0.2461 0.2392 0.0352  0.0120  0.0173  202 A1L6M C C47   
5407 C C48   . A1L6M K .   ? 0.1975 0.2619 0.2597 0.0290  0.0085  0.0182  202 A1L6M C C48   
5408 O O7    . A1L6M K .   ? 0.2026 0.2590 0.2573 0.0241  0.0068  0.0183  202 A1L6M C O7    
5409 O O8    . A1L6M K .   ? 0.2035 0.2798 0.2809 0.0286  0.0068  0.0199  202 A1L6M C O8    
5410 C C1    . PLC   L .   ? 0.6483 0.5960 0.6275 0.0399  -0.0066 -0.0253 203 PLC   C C1    
5411 C C2    . PLC   L .   ? 0.5853 0.5704 0.5874 0.0413  -0.0034 -0.0248 203 PLC   C C2    
5412 C C3    . PLC   L .   ? 0.5443 0.5578 0.5674 0.0494  -0.0001 -0.0209 203 PLC   C C3    
5413 C C4    . PLC   L .   ? 0.5829 0.4899 0.5244 0.1127  -0.0118 -0.0343 203 PLC   C C4    
5414 C C5    . PLC   L .   ? 0.5613 0.5042 0.5260 0.1274  -0.0106 -0.0335 203 PLC   C C5    
5415 C C6    . PLC   L .   ? 0.5371 0.4649 0.5027 0.1093  -0.0152 -0.0202 203 PLC   C C6    
5416 C C7    . PLC   L .   ? 0.5402 0.5242 0.5345 0.1407  -0.0130 -0.0278 203 PLC   C C7    
5417 C C8    . PLC   L .   ? 0.6182 0.5156 0.5530 0.1487  -0.0218 -0.0307 203 PLC   C C8    
5418 C "C'"  . PLC   L .   ? 0.6171 0.5806 0.5918 0.0422  -0.0050 -0.0353 203 PLC   C "C'"  
5419 C "C1'" . PLC   L .   ? 0.6127 0.5632 0.5839 0.0237  -0.0089 -0.0331 203 PLC   C "C1'" 
5420 C "C2'" . PLC   L .   ? 0.6119 0.5660 0.5811 0.0106  -0.0120 -0.0360 203 PLC   C "C2'" 
5421 C "C3'" . PLC   L .   ? 0.5519 0.5391 0.5470 0.0008  -0.0124 -0.0314 203 PLC   C "C3'" 
5422 C "C4'" . PLC   L .   ? 0.5260 0.5377 0.5320 0.0067  -0.0112 -0.0310 203 PLC   C "C4'" 
5423 C "C5'" . PLC   L .   ? 0.4948 0.5353 0.5247 0.0092  -0.0084 -0.0248 203 PLC   C "C5'" 
5424 C "C6'" . PLC   L .   ? 0.4726 0.5332 0.5123 0.0044  -0.0112 -0.0232 203 PLC   C "C6'" 
5425 C "C7'" . PLC   L .   ? 0.4645 0.5472 0.5245 0.0042  -0.0100 -0.0172 203 PLC   C "C7'" 
5426 C "C8'" . PLC   L .   ? 0.4576 0.5534 0.5206 0.0104  -0.0072 -0.0144 203 PLC   C "C8'" 
5427 C "C9'" . PLC   L .   ? 0.4586 0.5706 0.5378 0.0093  -0.0070 -0.0087 203 PLC   C "C9'" 
5428 C "CA'" . PLC   L .   ? 0.4647 0.5847 0.5417 0.0115  -0.0064 -0.0057 203 PLC   C "CA'" 
5429 C "CB'" . PLC   L .   ? 0.4548 0.5848 0.5434 0.0107  -0.0074 -0.0006 203 PLC   C "CB'" 
5430 C CB    . PLC   L .   ? 0.4950 0.5117 0.5271 0.0586  -0.0008 -0.0146 203 PLC   C CB    
5431 C C1B   . PLC   L .   ? 0.4747 0.5218 0.5219 0.0683  0.0029  -0.0165 203 PLC   C C1B   
5432 C C2B   . PLC   L .   ? 0.4615 0.5176 0.5133 0.0829  0.0023  -0.0167 203 PLC   C C2B   
5433 C C3B   . PLC   L .   ? 0.4434 0.5277 0.5058 0.0944  0.0063  -0.0214 203 PLC   C C3B   
5434 C C4B   . PLC   L .   ? 0.4142 0.5272 0.4931 0.0838  0.0114  -0.0195 203 PLC   C C4B   
5435 C C5B   . PLC   L .   ? 0.3740 0.4968 0.4662 0.0710  0.0111  -0.0123 203 PLC   C C5B   
5436 C C6B   . PLC   L .   ? 0.3540 0.4733 0.4462 0.0570  0.0115  -0.0096 203 PLC   C C6B   
5437 C C7B   . PLC   L .   ? 0.3234 0.4653 0.4283 0.0493  0.0147  -0.0063 203 PLC   C C7B   
5438 C C8B   . PLC   L .   ? 0.3049 0.4423 0.4085 0.0384  0.0134  -0.0038 203 PLC   C C8B   
5439 C C9B   . PLC   L .   ? 0.2846 0.4358 0.3894 0.0343  0.0166  -0.0030 203 PLC   C C9B   
5440 C CAA   . PLC   L .   ? 0.2636 0.4301 0.3783 0.0298  0.0189  0.0013  203 PLC   C CAA   
5441 C CBA   . PLC   L .   ? 0.2488 0.4223 0.3724 0.0343  0.0189  0.0019  203 PLC   C CBA   
5442 O "O'"  . PLC   L .   ? 0.6339 0.5929 0.5972 0.0484  -0.0041 -0.0409 203 PLC   C "O'"  
5443 O OB    . PLC   L .   ? 0.4981 0.4985 0.5217 0.0616  -0.0032 -0.0125 203 PLC   C OB    
5444 O O2    . PLC   L .   ? 0.5933 0.5752 0.5845 0.0503  -0.0023 -0.0311 203 PLC   C O2    
5445 O O3    . PLC   L .   ? 0.5306 0.5384 0.5566 0.0466  -0.0014 -0.0160 203 PLC   C O3    
5446 O O1P   . PLC   L .   ? 0.6119 0.5047 0.5431 0.0768  -0.0098 -0.0366 203 PLC   C O1P   
5447 O O2P   . PLC   L .   ? 0.6184 0.4715 0.5326 0.0588  -0.0147 -0.0268 203 PLC   C O2P   
5448 O O3P   . PLC   L .   ? 0.6489 0.5855 0.6217 0.0545  -0.0073 -0.0240 203 PLC   C O3P   
5449 O O4P   . PLC   L .   ? 0.5688 0.4765 0.5175 0.0890  -0.0112 -0.0278 203 PLC   C O4P   
5450 N N     . PLC   L .   ? 0.5513 0.4886 0.5162 0.1313  -0.0151 -0.0279 203 PLC   C N     
5451 P P     . PLC   L .   ? 0.5944 0.4895 0.5347 0.0688  -0.0108 -0.0291 203 PLC   C P     
5455 C C1    . LUT   N .   ? 0.2080 0.3103 0.3255 -0.0298 0.0222  0.0165  201 LUT   D C1    
5456 C C2    . LUT   N .   ? 0.2295 0.3057 0.3256 -0.0373 0.0236  0.0183  201 LUT   D C2    
5457 C C3    . LUT   N .   ? 0.2606 0.3364 0.3521 -0.0491 0.0300  0.0188  201 LUT   D C3    
5458 C C4    . LUT   N .   ? 0.2517 0.3541 0.3615 -0.0489 0.0343  0.0171  201 LUT   D C4    
5459 C C5    . LUT   N .   ? 0.2213 0.3487 0.3522 -0.0432 0.0322  0.0136  201 LUT   D C5    
5460 C C6    . LUT   N .   ? 0.2074 0.3330 0.3407 -0.0339 0.0263  0.0142  201 LUT   D C6    
5461 C C7    . LUT   N .   ? 0.1883 0.3345 0.3379 -0.0273 0.0240  0.0120  201 LUT   D C7    
5462 C C8    . LUT   N .   ? 0.1896 0.3383 0.3427 -0.0182 0.0196  0.0128  201 LUT   D C8    
5463 C C9    . LUT   N .   ? 0.2091 0.3736 0.3734 -0.0128 0.0177  0.0112  201 LUT   D C9    
5464 C C10   . LUT   N .   ? 0.2254 0.3884 0.3886 -0.0062 0.0133  0.0122  201 LUT   D C10   
5465 C C11   . LUT   N .   ? 0.2176 0.3881 0.3850 -0.0003 0.0102  0.0118  201 LUT   D C11   
5466 C C12   . LUT   N .   ? 0.2182 0.3867 0.3820 0.0035  0.0063  0.0122  201 LUT   D C12   
5467 C C13   . LUT   N .   ? 0.2225 0.3946 0.3863 0.0091  0.0022  0.0121  201 LUT   D C13   
5468 C C14   . LUT   N .   ? 0.2492 0.4142 0.4039 0.0113  -0.0001 0.0138  201 LUT   D C14   
5469 C C15   . LUT   N .   ? 0.2810 0.4420 0.4284 0.0158  -0.0038 0.0152  201 LUT   D C15   
5470 C C16   . LUT   N .   ? 0.2058 0.3087 0.3249 -0.0291 0.0185  0.0136  201 LUT   D C16   
5471 C C17   . LUT   N .   ? 0.1904 0.2920 0.3083 -0.0177 0.0192  0.0195  201 LUT   D C17   
5472 C C18   . LUT   N .   ? 0.2017 0.3546 0.3482 -0.0472 0.0372  0.0096  201 LUT   D C18   
5473 C C19   . LUT   N .   ? 0.2189 0.4011 0.3947 -0.0127 0.0197  0.0081  201 LUT   D C19   
5474 C C20   . LUT   N .   ? 0.1946 0.3785 0.3667 0.0132  0.0002  0.0094  201 LUT   D C20   
5475 O O3    . LUT   N .   ? 0.2879 0.3389 0.3587 -0.0486 0.0297  0.0229  201 LUT   D O3    
5476 C C21   . LUT   N .   ? 0.6171 0.5956 0.5408 0.0243  -0.0413 0.0463  201 LUT   D C21   
5477 C C22   . LUT   N .   ? 0.6917 0.6301 0.5790 0.0281  -0.0481 0.0516  201 LUT   D C22   
5478 C C23   . LUT   N .   ? 0.7435 0.6581 0.6038 0.0103  -0.0391 0.0570  201 LUT   D C23   
5479 C C24   . LUT   N .   ? 0.7281 0.6677 0.6132 -0.0024 -0.0266 0.0551  201 LUT   D C24   
5480 C C25   . LUT   N .   ? 0.6221 0.5982 0.5444 -0.0004 -0.0223 0.0501  201 LUT   D C25   
5481 C C26   . LUT   N .   ? 0.5699 0.5655 0.5153 0.0148  -0.0300 0.0453  201 LUT   D C26   
5482 C C27   . LUT   N .   ? 0.4812 0.5100 0.4568 0.0121  -0.0238 0.0405  201 LUT   D C27   
5483 C C28   . LUT   N .   ? 0.4338 0.4854 0.4392 0.0165  -0.0226 0.0365  201 LUT   D C28   
5484 C C29   . LUT   N .   ? 0.3754 0.4522 0.4055 0.0140  -0.0171 0.0325  201 LUT   D C29   
5485 C C30   . LUT   N .   ? 0.3427 0.4349 0.3965 0.0181  -0.0167 0.0297  201 LUT   D C30   
5486 C C31   . LUT   N .   ? 0.2972 0.4084 0.3722 0.0166  -0.0127 0.0262  201 LUT   D C31   
5487 C C32   . LUT   N .   ? 0.2777 0.4006 0.3712 0.0192  -0.0121 0.0239  201 LUT   D C32   
5488 C C33   . LUT   N .   ? 0.2595 0.3959 0.3693 0.0167  -0.0081 0.0210  201 LUT   D C33   
5489 C C34   . LUT   N .   ? 0.2639 0.4087 0.3879 0.0184  -0.0079 0.0192  201 LUT   D C34   
5490 C C35   . LUT   N .   ? 0.2772 0.4308 0.4136 0.0156  -0.0047 0.0169  201 LUT   D C35   
5491 C C36   . LUT   N .   ? 0.6181 0.5974 0.5294 0.0155  -0.0377 0.0467  201 LUT   D C36   
5492 C C37   . LUT   N .   ? 0.6101 0.6098 0.5583 0.0396  -0.0503 0.0409  201 LUT   D C37   
5493 C C38   . LUT   N .   ? 0.5563 0.5541 0.4980 -0.0124 -0.0110 0.0487  201 LUT   D C38   
5494 C C39   . LUT   N .   ? 0.3796 0.4652 0.4090 0.0080  -0.0120 0.0306  201 LUT   D C39   
5495 C C40   . LUT   N .   ? 0.2363 0.3761 0.3454 0.0128  -0.0040 0.0196  201 LUT   D C40   
5496 O O23   . LUT   N .   ? 0.7513 0.6268 0.5806 0.0140  -0.0451 0.0612  201 LUT   D O23   
5497 C C1    . PLC   O .   ? 0.1933 0.3187 0.3143 0.0150  0.0038  0.0256  202 PLC   D C1    
5498 C C2    . PLC   O .   ? 0.2185 0.3563 0.3510 0.0187  0.0020  0.0226  202 PLC   D C2    
5499 C C3    . PLC   O .   ? 0.2464 0.3810 0.3722 0.0214  -0.0026 0.0227  202 PLC   D C3    
5500 C C4    . PLC   O .   ? 0.1855 0.2836 0.2885 0.0192  0.0066  0.0247  202 PLC   D C4    
5501 C C5    . PLC   O .   ? 0.2109 0.2848 0.2926 0.0197  0.0045  0.0260  202 PLC   D C5    
5502 C C6    . PLC   O .   ? 0.2138 0.2893 0.3000 0.0416  0.0029  0.0183  202 PLC   D C6    
5503 C C7    . PLC   O .   ? 0.2594 0.2931 0.3088 0.0279  0.0016  0.0244  202 PLC   D C7    
5504 C C8    . PLC   O .   ? 0.2074 0.2799 0.2904 0.0231  0.0096  0.0216  202 PLC   D C8    
5505 C "C'"  . PLC   O .   ? 0.2405 0.3950 0.3915 0.0132  0.0072  0.0195  202 PLC   D "C'"  
5506 C "C1'" . PLC   O .   ? 0.2766 0.4324 0.4299 0.0087  0.0096  0.0196  202 PLC   D "C1'" 
5507 C "C2'" . PLC   O .   ? 0.3127 0.4639 0.4619 0.0067  0.0117  0.0221  202 PLC   D "C2'" 
5508 C "C3'" . PLC   O .   ? 0.3836 0.5334 0.5331 0.0052  0.0127  0.0216  202 PLC   D "C3'" 
5509 C "C4'" . PLC   O .   ? 0.4244 0.5703 0.5706 0.0046  0.0138  0.0235  202 PLC   D "C4'" 
5510 C "C5'" . PLC   O .   ? 0.5073 0.6480 0.6495 0.0064  0.0129  0.0233  202 PLC   D "C5'" 
5511 C "C6'" . PLC   O .   ? 0.5050 0.6482 0.6453 0.0097  0.0113  0.0245  202 PLC   D "C6'" 
5512 C "C7'" . PLC   O .   ? 0.4777 0.6324 0.6215 0.0127  0.0106  0.0234  202 PLC   D "C7'" 
5513 C "C8'" . PLC   O .   ? 0.4065 0.5710 0.5526 0.0093  0.0109  0.0247  202 PLC   D "C8'" 
5514 C "C9'" . PLC   O .   ? 0.3481 0.5271 0.4975 0.0094  0.0117  0.0233  202 PLC   D "C9'" 
5515 C "CA'" . PLC   O .   ? 0.3060 0.4992 0.4598 0.0123  0.0100  0.0221  202 PLC   D "CA'" 
5516 C "CB'" . PLC   O .   ? 0.3162 0.5291 0.4749 0.0090  0.0123  0.0202  202 PLC   D "CB'" 
5517 C CB    . PLC   O .   ? 0.2645 0.3816 0.3656 0.0163  -0.0041 0.0274  202 PLC   D CB    
5518 C C1B   . PLC   O .   ? 0.2658 0.3787 0.3565 0.0077  -0.0001 0.0301  202 PLC   D C1B   
5519 C C2B   . PLC   O .   ? 0.2568 0.3853 0.3596 0.0039  0.0048  0.0284  202 PLC   D C2B   
5520 C C3B   . PLC   O .   ? 0.2775 0.4095 0.3801 -0.0032 0.0094  0.0298  202 PLC   D C3B   
5521 C C4B   . PLC   O .   ? 0.2642 0.4107 0.3818 -0.0023 0.0119  0.0278  202 PLC   D C4B   
5522 C C5B   . PLC   O .   ? 0.2627 0.4226 0.3827 -0.0062 0.0159  0.0268  202 PLC   D C5B   
5523 C C6B   . PLC   O .   ? 0.2823 0.4411 0.3911 -0.0155 0.0186  0.0287  202 PLC   D C6B   
5524 C C7B   . PLC   O .   ? 0.2754 0.4520 0.3909 -0.0214 0.0222  0.0275  202 PLC   D C7B   
5525 C C8B   . PLC   O .   ? 0.2869 0.4738 0.3963 -0.0299 0.0272  0.0268  202 PLC   D C8B   
5526 C C9B   . PLC   O .   ? 0.2839 0.4792 0.3955 -0.0240 0.0295  0.0236  202 PLC   D C9B   
5527 C CAA   . PLC   O .   ? 0.2863 0.4635 0.3819 -0.0243 0.0284  0.0254  202 PLC   D CAA   
5528 C CBA   . PLC   O .   ? 0.3039 0.4835 0.3855 -0.0350 0.0340  0.0258  202 PLC   D CBA   
5529 O "O'"  . PLC   O .   ? 0.2133 0.3733 0.3697 0.0163  0.0070  0.0171  202 PLC   D "O'"  
5530 O OB    . PLC   O .   ? 0.3006 0.4147 0.3987 0.0230  -0.0096 0.0263  202 PLC   D OB    
5531 O O2    . PLC   O .   ? 0.2147 0.3615 0.3561 0.0139  0.0052  0.0219  202 PLC   D O2    
5532 O O3    . PLC   O .   ? 0.2603 0.3867 0.3745 0.0156  -0.0010 0.0259  202 PLC   D O3    
5533 O O1P   . PLC   O .   ? 0.1450 0.2652 0.2586 0.0019  0.0093  0.0293  202 PLC   D O1P   
5534 O O2P   . PLC   O .   ? 0.1476 0.2732 0.2733 0.0075  0.0121  0.0257  202 PLC   D O2P   
5535 O O3P   . PLC   O .   ? 0.1619 0.2899 0.2885 0.0148  0.0067  0.0246  202 PLC   D O3P   
5536 O O4P   . PLC   O .   ? 0.1976 0.3001 0.3015 0.0123  0.0066  0.0273  202 PLC   D O4P   
5537 N N     . PLC   O .   ? 0.2259 0.2903 0.3018 0.0281  0.0048  0.0227  202 PLC   D N     
5538 P P     . PLC   O .   ? 0.1654 0.2860 0.2847 0.0085  0.0091  0.0269  202 PLC   D P     
5548 C C1    . PLC   S .   ? 0.6701 0.5064 0.6913 0.0464  -0.0484 0.0347  201 PLC   F C1    
5549 C C2    . PLC   S .   ? 0.6573 0.5167 0.6766 0.0375  -0.0425 0.0433  201 PLC   F C2    
5550 C C3    . PLC   S .   ? 0.6394 0.5059 0.6614 0.0190  -0.0348 0.0459  201 PLC   F C3    
5551 C C4    . PLC   S .   ? 0.6916 0.4585 0.7059 0.0726  -0.0638 0.0112  201 PLC   F C4    
5552 C C5    . PLC   S .   ? 0.6586 0.4432 0.6817 0.0887  -0.0637 -0.0049 201 PLC   F C5    
5553 C C6    . PLC   S .   ? 0.7142 0.4280 0.7158 0.1118  -0.0771 -0.0142 201 PLC   F C6    
5554 C C7    . PLC   S .   ? 0.6664 0.4624 0.6946 0.1262  -0.0675 -0.0251 201 PLC   F C7    
5555 C C8    . PLC   S .   ? 0.6765 0.4419 0.6888 0.1255  -0.0746 0.0007  201 PLC   F C8    
5556 C "C'"  . PLC   S .   ? 0.6307 0.5345 0.6508 0.0469  -0.0416 0.0443  201 PLC   F "C'"  
5557 C "C1'" . PLC   S .   ? 0.6569 0.5420 0.6619 0.0392  -0.0409 0.0590  201 PLC   F "C1'" 
5558 C "C2'" . PLC   S .   ? 0.6566 0.5493 0.6500 0.0446  -0.0438 0.0676  201 PLC   F "C2'" 
5559 C "C3'" . PLC   S .   ? 0.6443 0.5419 0.6256 0.0332  -0.0373 0.0774  201 PLC   F "C3'" 
5560 C "C4'" . PLC   S .   ? 0.6185 0.5413 0.6052 0.0258  -0.0292 0.0704  201 PLC   F "C4'" 
5561 C "C5'" . PLC   S .   ? 0.6166 0.5619 0.6081 0.0328  -0.0319 0.0611  201 PLC   F "C5'" 
5562 C "C6'" . PLC   S .   ? 0.5982 0.5634 0.5874 0.0268  -0.0252 0.0567  201 PLC   F "C6'" 
5563 C "C7'" . PLC   S .   ? 0.5886 0.5686 0.5933 0.0242  -0.0214 0.0447  201 PLC   F "C7'" 
5564 C "C8'" . PLC   S .   ? 0.5813 0.5786 0.5821 0.0226  -0.0185 0.0393  201 PLC   F "C8'" 
5565 C "C9'" . PLC   S .   ? 0.5890 0.5998 0.6050 0.0213  -0.0165 0.0283  201 PLC   F "C9'" 
5566 C "CA'" . PLC   S .   ? 0.6488 0.6712 0.6597 0.0186  -0.0125 0.0237  201 PLC   F "CA'" 
5567 C "CB'" . PLC   S .   ? 0.6595 0.6924 0.6838 0.0155  -0.0079 0.0156  201 PLC   F "CB'" 
5568 C CB    . PLC   S .   ? 0.5744 0.4411 0.6131 0.0206  -0.0359 0.0237  201 PLC   F CB    
5569 C C1B   . PLC   S .   ? 0.5555 0.4332 0.6044 0.0105  -0.0320 0.0147  201 PLC   F C1B   
5570 C C2B   . PLC   S .   ? 0.5596 0.4314 0.6079 -0.0084 -0.0287 0.0227  201 PLC   F C2B   
5571 C C3B   . PLC   S .   ? 0.5318 0.4343 0.5916 -0.0171 -0.0216 0.0179  201 PLC   F C3B   
5572 C C4B   . PLC   S .   ? 0.5042 0.4308 0.5716 -0.0060 -0.0200 0.0063  201 PLC   F C4B   
5573 C C5B   . PLC   S .   ? 0.4898 0.4459 0.5654 -0.0127 -0.0128 0.0045  201 PLC   F C5B   
5574 C C6B   . PLC   S .   ? 0.4843 0.4608 0.5579 -0.0064 -0.0090 0.0069  201 PLC   F C6B   
5575 C C7B   . PLC   S .   ? 0.4691 0.4712 0.5488 -0.0111 -0.0023 0.0045  201 PLC   F C7B   
5576 C C8B   . PLC   S .   ? 0.4660 0.4786 0.5381 -0.0125 0.0032  0.0130  201 PLC   F C8B   
5577 C C9B   . PLC   S .   ? 0.4215 0.4553 0.4953 -0.0089 0.0070  0.0079  201 PLC   F C9B   
5578 C CAA   . PLC   S .   ? 0.3968 0.4412 0.4818 -0.0085 0.0066  -0.0021 201 PLC   F CAA   
5579 C CBA   . PLC   S .   ? 0.3869 0.4333 0.4736 0.0003  0.0019  -0.0093 201 PLC   F CBA   
5580 O "O'"  . PLC   S .   ? 0.5836 0.5108 0.6087 0.0531  -0.0427 0.0398  201 PLC   F "O'"  
5581 O OB    . PLC   S .   ? 0.5665 0.4148 0.6004 0.0334  -0.0425 0.0220  201 PLC   F OB    
5582 O O2    . PLC   S .   ? 0.6483 0.5400 0.6755 0.0454  -0.0413 0.0366  201 PLC   F O2    
5583 O O3    . PLC   S .   ? 0.5841 0.4664 0.6193 0.0157  -0.0314 0.0330  201 PLC   F O3    
5584 O O1P   . PLC   S .   ? 0.6590 0.4318 0.6550 0.0837  -0.0689 0.0471  201 PLC   F O1P   
5585 O O2P   . PLC   S .   ? 0.6900 0.4183 0.6807 0.0523  -0.0662 0.0466  201 PLC   F O2P   
5586 O O3P   . PLC   S .   ? 0.6920 0.4896 0.6991 0.0478  -0.0546 0.0449  201 PLC   F O3P   
5587 O O4P   . PLC   S .   ? 0.7057 0.4904 0.7191 0.0783  -0.0634 0.0221  201 PLC   F O4P   
5588 N N     . PLC   S .   ? 0.6707 0.4352 0.6872 0.1128  -0.0706 -0.0108 201 PLC   F N     
5589 P P     . PLC   S .   ? 0.6932 0.4607 0.6940 0.0666  -0.0640 0.0405  201 PLC   F P     
5590 C C1    . A1L6M T .   ? 0.5029 0.4011 0.4125 -0.2142 -0.0620 0.0615  202 A1L6M F C1    
5591 C C2    . A1L6M T .   ? 0.4753 0.3611 0.3770 -0.1835 -0.0523 0.0511  202 A1L6M F C2    
5592 C C3    . A1L6M T .   ? 0.5045 0.3374 0.3667 -0.1756 -0.0537 0.0368  202 A1L6M F C3    
5593 C C4    . A1L6M T .   ? 0.5446 0.3428 0.3752 -0.1891 -0.0636 0.0280  202 A1L6M F C4    
5594 C C5    . A1L6M T .   ? 0.5664 0.3673 0.3897 -0.2178 -0.0784 0.0301  202 A1L6M F C5    
5595 C C6    . A1L6M T .   ? 0.5571 0.3131 0.3599 -0.1703 -0.0575 0.0151  202 A1L6M F C6    
5596 O O1    . A1L6M T .   ? 0.6075 0.3207 0.3754 -0.1723 -0.0606 0.0029  202 A1L6M F O1    
5597 N N1    . A1L6M T .   ? 0.5265 0.2930 0.3447 -0.1474 -0.0467 0.0167  202 A1L6M F N1    
5598 C C7    . A1L6M T .   ? 0.4913 0.3029 0.3434 -0.1497 -0.0440 0.0289  202 A1L6M F C7    
5599 C C8    . A1L6M T .   ? 0.4614 0.2907 0.3312 -0.1297 -0.0339 0.0315  202 A1L6M F C8    
5600 C C9    . A1L6M T .   ? 0.4345 0.2577 0.3040 -0.1049 -0.0262 0.0256  202 A1L6M F C9    
5601 C C10   . A1L6M T .   ? 0.4410 0.2459 0.2984 -0.0872 -0.0242 0.0138  202 A1L6M F C10   
5602 C C11   . A1L6M T .   ? 0.4540 0.2413 0.2929 -0.0894 -0.0277 0.0037  202 A1L6M F C11   
5603 C C12   . A1L6M T .   ? 0.4241 0.2319 0.2891 -0.0673 -0.0178 0.0130  202 A1L6M F C12   
5604 C C13   . A1L6M T .   ? 0.4345 0.2336 0.2975 -0.0451 -0.0135 0.0033  202 A1L6M F C13   
5605 C C14   . A1L6M T .   ? 0.4771 0.2346 0.3181 -0.0354 -0.0135 0.0002  202 A1L6M F C14   
5606 C C15   . A1L6M T .   ? 0.4742 0.2238 0.3150 -0.0138 -0.0087 -0.0099 202 A1L6M F C15   
5607 O O2    . A1L6M T .   ? 0.5169 0.2301 0.3353 -0.0109 -0.0082 -0.0170 202 A1L6M F O2    
5608 O O3    . A1L6M T .   ? 0.4297 0.2085 0.2927 -0.0007 -0.0051 -0.0104 202 A1L6M F O3    
5609 C C16   . A1L6M T .   ? 0.4143 0.2382 0.2909 -0.0719 -0.0155 0.0234  202 A1L6M F C16   
5610 N N2    . A1L6M T .   ? 0.4162 0.2488 0.2957 -0.0944 -0.0195 0.0308  202 A1L6M F N2    
5611 C C17   . A1L6M T .   ? 0.3999 0.2322 0.2842 -0.0558 -0.0104 0.0246  202 A1L6M F C17   
5612 C C18   . A1L6M T .   ? 0.3881 0.2359 0.2803 -0.0536 -0.0061 0.0317  202 A1L6M F C18   
5613 N N3    . A1L6M T .   ? 0.4042 0.2672 0.3024 -0.0686 -0.0034 0.0414  202 A1L6M F N3    
5614 C C19   . A1L6M T .   ? 0.3964 0.2677 0.2953 -0.0604 0.0021  0.0450  202 A1L6M F C19   
5615 C C20   . A1L6M T .   ? 0.4004 0.2874 0.3037 -0.0725 0.0083  0.0547  202 A1L6M F C20   
5616 C C21   . A1L6M T .   ? 0.4119 0.3179 0.3195 -0.0700 0.0171  0.0592  202 A1L6M F C21   
5617 N N4    . A1L6M T .   ? 0.4057 0.3240 0.3180 -0.0536 0.0207  0.0529  202 A1L6M F N4    
5618 C C22   . A1L6M T .   ? 0.4216 0.3548 0.3330 -0.0560 0.0304  0.0580  202 A1L6M F C22   
5619 O O4    . A1L6M T .   ? 0.3851 0.3283 0.2969 -0.0438 0.0347  0.0523  202 A1L6M F O4    
5620 C C23   . A1L6M T .   ? 0.4511 0.3850 0.3599 -0.0742 0.0346  0.0691  202 A1L6M F C23   
5621 C C24   . A1L6M T .   ? 0.4910 0.4418 0.3979 -0.0795 0.0482  0.0763  202 A1L6M F C24   
5622 O O5    . A1L6M T .   ? 0.5253 0.4701 0.4257 -0.0995 0.0507  0.0888  202 A1L6M F O5    
5623 C C25   . A1L6M T .   ? 0.4984 0.4893 0.4363 -0.0739 0.0595  0.0723  202 A1L6M F C25   
5624 C C26   . A1L6M T .   ? 0.5450 0.5591 0.4878 -0.0791 0.0770  0.0787  202 A1L6M F C26   
5625 C C27   . A1L6M T .   ? 0.6263 0.6279 0.5397 -0.0721 0.0841  0.0767  202 A1L6M F C27   
5626 C C28   . A1L6M T .   ? 0.7641 0.7752 0.6668 -0.0768 0.1000  0.0822  202 A1L6M F C28   
5627 C C29   . A1L6M T .   ? 0.7442 0.7807 0.6646 -0.0925 0.1146  0.0944  202 A1L6M F C29   
5628 C C30   . A1L6M T .   ? 0.8678 0.8668 0.7393 -0.0667 0.1052  0.0759  202 A1L6M F C30   
5629 C C31   . A1L6M T .   ? 0.9453 0.9174 0.7744 -0.0749 0.1045  0.0856  202 A1L6M F C31   
5630 C C32   . A1L6M T .   ? 1.0678 1.0237 0.8667 -0.0620 0.0995  0.0765  202 A1L6M F C32   
5631 C C33   . A1L6M T .   ? 1.1001 1.0634 0.8838 -0.0557 0.1113  0.0689  202 A1L6M F C33   
5632 C C34   . A1L6M T .   ? 1.0439 1.0305 0.8310 -0.0605 0.1369  0.0705  202 A1L6M F C34   
5633 C C35   . A1L6M T .   ? 1.1284 1.0770 0.8912 -0.0428 0.0992  0.0567  202 A1L6M F C35   
5634 C C36   . A1L6M T .   ? 1.1299 1.0476 0.8596 -0.0423 0.0793  0.0631  202 A1L6M F C36   
5635 C C37   . A1L6M T .   ? 1.1686 1.0781 0.8729 -0.0329 0.0710  0.0528  202 A1L6M F C37   
5636 C C38   . A1L6M T .   ? 1.1264 1.0311 0.7945 -0.0343 0.0782  0.0501  202 A1L6M F C38   
5637 C C39   . A1L6M T .   ? 1.0878 0.9937 0.7298 -0.0452 0.0991  0.0586  202 A1L6M F C39   
5638 C C40   . A1L6M T .   ? 1.1184 1.0163 0.7662 -0.0261 0.0661  0.0376  202 A1L6M F C40   
5639 C C41   . A1L6M T .   ? 0.4379 0.3557 0.3459 -0.0845 0.0254  0.0702  202 A1L6M F C41   
5640 C C42   . A1L6M T .   ? 0.4688 0.3780 0.3723 -0.1073 0.0241  0.0807  202 A1L6M F C42   
5641 C C43   . A1L6M T .   ? 0.3834 0.2458 0.2781 -0.0414 0.0005  0.0378  202 A1L6M F C43   
5642 C C44   . A1L6M T .   ? 0.4006 0.2649 0.2905 -0.0291 0.0020  0.0386  202 A1L6M F C44   
5643 O O6    . A1L6M T .   ? 0.3844 0.2809 0.2930 -0.0231 0.0080  0.0353  202 A1L6M F O6    
5644 C C45   . A1L6M T .   ? 0.3848 0.2336 0.2773 -0.0371 -0.0039 0.0301  202 A1L6M F C45   
5645 C C46   . A1L6M T .   ? 0.3885 0.2283 0.2806 -0.0179 -0.0056 0.0212  202 A1L6M F C46   
5646 C C47   . A1L6M T .   ? 0.3696 0.2368 0.2835 -0.0107 -0.0026 0.0138  202 A1L6M F C47   
5647 C C48   . A1L6M T .   ? 0.3320 0.2321 0.2670 -0.0047 0.0019  0.0136  202 A1L6M F C48   
5648 O O7    . A1L6M T .   ? 0.3119 0.2272 0.2618 0.0009  0.0037  0.0081  202 A1L6M F O7    
5649 O O8    . A1L6M T .   ? 0.3315 0.2395 0.2661 -0.0062 0.0042  0.0185  202 A1L6M F O8    
# 
