data_9CZ7
# 
_entry.id   9CZ7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9CZ7         pdb_00009cz7 10.2210/pdb9cz7/pdb 
WWPDB D_1000286496 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-13 
2 'Structure model' 1 1 2024-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CZ7 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9CZA unspecified 
PDB . 9CZD unspecified 
PDB . 9CZF unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              albert.lin@morphictx.com 
_pdbx_contact_author.name_first         Fu-Yang 
_pdbx_contact_author.name_last          Lin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2638-1281 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Monroy, M.F.' 1 0000-0003-0475-1402 
'Qiao, Q.'     2 0009-0005-3960-1668 
'Lin, F.Y.'    3 0000-0002-2638-1281 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                18656 
_citation.page_last                 18681 
_citation.title                     
'The Discovery of MORF-627, a Highly Selective Conformationally-Biased Zwitterionic Integrin alpha v beta 6 Inhibitor for Fibrosis.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01851 
_citation.pdbx_database_id_PubMed   39446989 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Harrison, B.A.'  1  ? 
primary 'Dowling, J.E.'   2  ? 
primary 'Bursavich, M.G.' 3  ? 
primary 'Troast, D.M.'    4  ? 
primary 'Chong, K.M.'     5  ? 
primary 'Hahn, K.N.'      6  ? 
primary 'Zhong, C.'       7  ? 
primary 'Mulvihill, K.M.' 8  ? 
primary 'Nguyen, H.'      9  ? 
primary 'Monroy, M.F.'    10 ? 
primary 'Qiao, Q.'        11 ? 
primary 'Sosa, B.'        12 ? 
primary 'Mostafavi, S.'   13 ? 
primary 'Smukste, I.'     14 ? 
primary 'Lee, D.'         15 ? 
primary 'Cappellucci, L.' 16 ? 
primary 'Konopka, E.H.'   17 ? 
primary 'Nowakowski, P.'  18 ? 
primary 'Stawski, L.'     19 ? 
primary 'Senices, M.'     20 ? 
primary 'Nguyen, M.H.'    21 ? 
primary 'Kapoor, P.S.'    22 ? 
primary 'Luus, L.'        23 ? 
primary 'Sullivan, A.'    24 ? 
primary 'Bortolato, A.'   25 ? 
primary 'Svensson, M.'    26 ? 
primary 'Hickey, E.R.'    27 ? 
primary 'Konze, K.D.'     28 ? 
primary 'Day, T.'         29 ? 
primary 'Kim, B.'         30 ? 
primary 'Negri, A.'       31 ? 
primary 'Gerasyuto, A.I.' 32 ? 
primary 'Moy, T.I.'       33 ? 
primary 'Lu, M.'          34 ? 
primary 'Ray, A.S.'       35 ? 
primary 'Wang, L.'        36 ? 
primary 'Cui, D.'         37 ? 
primary 'Lin, F.Y.'       38 ? 
primary 'Lippa, B.'       39 ? 
primary 'Rogers, B.N.'    40 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Integrin alpha-V heavy chain' 66456.484 1  ? ? ? ? 
2  polymer     man 'Integrin beta-6' 52714.875 1  ? ? ? ? 
3  polymer     man '17E6 Fab light chain' 23722.037 1  ? ? ? ? 
4  polymer     man '17E6 Fab heavy chain' 23209.912 1  ? ? ? ? 
5  branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   2  
? ? ? ? 
6  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
1072.964  1  ? ? ? ? 
7  branched    man 
;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
;
910.823   1  ? ? ? ? 
8  non-polymer syn 'CALCIUM ION' 40.078    6  ? ? ? ? 
9  non-polymer syn GLYCEROL 92.094    8  ? ? ? ? 
10 non-polymer syn 'MAGNESIUM ION' 24.305    1  ? ? ? ? 
11 non-polymer syn '(2S)-phenyl{(3S)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid' 409.521   
1  ? ? ? ? 
12 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2  ? ? ? ? 
13 non-polymer syn 'ACETATE ION' 59.044    2  ? ? ? ? 
14 water       nat water 18.015    57 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY
AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS
IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV
SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ
RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSC
PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK
ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME
YRLDYRTAADTTGLQPILNQFTPANISRQAHILLDGGSLEVLFQG
;
;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY
AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS
IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV
SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ
RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSC
PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK
ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME
YRLDYRTAADTTGLQPILNQFTPANISRQAHILLDGGSLEVLFQG
;
A ? 
2 'polypeptide(L)' no no 
;GCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDI
VQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKP
VSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRND
SLHLLVFVSDADSHFGMDSKLAGIVCPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENY
AKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTV
NIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCESGHSLEVLFQ
G
;
;GCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDI
VQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKP
VSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRND
SLHLLVFVSDADSHFGMDSKLAGIVCPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENY
AKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTV
NIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCESGHSLEVLFQ
G
;
B ? 
3 'polypeptide(L)' no no 
;DIQMTQTTSSLSASLGDRVIISCRASQDISNYLSWYQQKPDGTVKLLIFYTSKLHSGVPSRFSGSGSGTDYSLTISNLDQ
EDIATYFCQQGNTFPYTFGGGTKVEMRRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVL
NSWTDQDSKDSTYSFSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
;
;DIQMTQTTSSLSASLGDRVIISCRASQDISNYLSWYQQKPDGTVKLLIFYTSKLHSGVPSRFSGSGSGTDYSLTISNLDQ
EDIATYFCQQGNTFPYTFGGGTKVEMRRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVL
NSWTDQDSKDSTYSFSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
;
C ? 
4 'polypeptide(L)' no no 
;QVQLQQSGAELAEPGASVKMSCKASGYTFSSFWMHWVKQRPGQGLEWIGYINPNSGYTECNEIFRDKATMTADTSSSTAY
MQLSGLTSEDSAVYYCASFLGRGAMDYWGQGTSVTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWN
SGSLSAGVHTFPAVLQSSLYTLSSSVTVVASTWPSQSITCNVAHPASSTKVDKKIEPR
;
;QVQLQQSGAELAEPGASVKMSCKASGYTFSSFWMHWVKQRPGQGLEWIGYINPNSGYTECNEIFRDKATMTADTSSSTAY
MQLSGLTSEDSAVYYCASFLGRGAMDYWGQGTSVTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWN
SGSLSAGVHTFPAVLQSSLYTLSSSVTVVASTWPSQSITCNVAHPASSTKVDKKIEPR
;
D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
8  'CALCIUM ION'                                                                                        CA    
9  GLYCEROL                                                                                             GOL   
10 'MAGNESIUM ION'                                                                                      MG    
11 '(2S)-phenyl{(3S)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid' A1A6A 
12 2-acetamido-2-deoxy-beta-D-glucopyranose                                                             NAG   
13 'ACETATE ION'                                                                                        ACT   
14 water                                                                                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   ASN n 
1 3   LEU n 
1 4   ASP n 
1 5   VAL n 
1 6   ASP n 
1 7   SER n 
1 8   PRO n 
1 9   ALA n 
1 10  GLU n 
1 11  TYR n 
1 12  SER n 
1 13  GLY n 
1 14  PRO n 
1 15  GLU n 
1 16  GLY n 
1 17  SER n 
1 18  TYR n 
1 19  PHE n 
1 20  GLY n 
1 21  PHE n 
1 22  ALA n 
1 23  VAL n 
1 24  ASP n 
1 25  PHE n 
1 26  PHE n 
1 27  VAL n 
1 28  PRO n 
1 29  SER n 
1 30  ALA n 
1 31  SER n 
1 32  SER n 
1 33  ARG n 
1 34  MET n 
1 35  PHE n 
1 36  LEU n 
1 37  LEU n 
1 38  VAL n 
1 39  GLY n 
1 40  ALA n 
1 41  PRO n 
1 42  LYS n 
1 43  ALA n 
1 44  ASN n 
1 45  THR n 
1 46  THR n 
1 47  GLN n 
1 48  PRO n 
1 49  GLY n 
1 50  ILE n 
1 51  VAL n 
1 52  GLU n 
1 53  GLY n 
1 54  GLY n 
1 55  GLN n 
1 56  VAL n 
1 57  LEU n 
1 58  LYS n 
1 59  CYS n 
1 60  ASP n 
1 61  TRP n 
1 62  SER n 
1 63  SER n 
1 64  THR n 
1 65  ARG n 
1 66  ARG n 
1 67  CYS n 
1 68  GLN n 
1 69  PRO n 
1 70  ILE n 
1 71  GLU n 
1 72  PHE n 
1 73  ASP n 
1 74  ALA n 
1 75  THR n 
1 76  GLY n 
1 77  ASN n 
1 78  ARG n 
1 79  ASP n 
1 80  TYR n 
1 81  ALA n 
1 82  LYS n 
1 83  ASP n 
1 84  ASP n 
1 85  PRO n 
1 86  LEU n 
1 87  GLU n 
1 88  PHE n 
1 89  LYS n 
1 90  SER n 
1 91  HIS n 
1 92  GLN n 
1 93  TRP n 
1 94  PHE n 
1 95  GLY n 
1 96  ALA n 
1 97  SER n 
1 98  VAL n 
1 99  ARG n 
1 100 SER n 
1 101 LYS n 
1 102 GLN n 
1 103 ASP n 
1 104 LYS n 
1 105 ILE n 
1 106 LEU n 
1 107 ALA n 
1 108 CYS n 
1 109 ALA n 
1 110 PRO n 
1 111 LEU n 
1 112 TYR n 
1 113 HIS n 
1 114 TRP n 
1 115 ARG n 
1 116 THR n 
1 117 GLU n 
1 118 MET n 
1 119 LYS n 
1 120 GLN n 
1 121 GLU n 
1 122 ARG n 
1 123 GLU n 
1 124 PRO n 
1 125 VAL n 
1 126 GLY n 
1 127 THR n 
1 128 CYS n 
1 129 PHE n 
1 130 LEU n 
1 131 GLN n 
1 132 ASP n 
1 133 GLY n 
1 134 THR n 
1 135 LYS n 
1 136 THR n 
1 137 VAL n 
1 138 GLU n 
1 139 TYR n 
1 140 ALA n 
1 141 PRO n 
1 142 CYS n 
1 143 ARG n 
1 144 SER n 
1 145 GLN n 
1 146 ASP n 
1 147 ILE n 
1 148 ASP n 
1 149 ALA n 
1 150 ASP n 
1 151 GLY n 
1 152 GLN n 
1 153 GLY n 
1 154 PHE n 
1 155 CYS n 
1 156 GLN n 
1 157 GLY n 
1 158 GLY n 
1 159 PHE n 
1 160 SER n 
1 161 ILE n 
1 162 ASP n 
1 163 PHE n 
1 164 THR n 
1 165 LYS n 
1 166 ALA n 
1 167 ASP n 
1 168 ARG n 
1 169 VAL n 
1 170 LEU n 
1 171 LEU n 
1 172 GLY n 
1 173 GLY n 
1 174 PRO n 
1 175 GLY n 
1 176 SER n 
1 177 PHE n 
1 178 TYR n 
1 179 TRP n 
1 180 GLN n 
1 181 GLY n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 SER n 
1 186 ASP n 
1 187 GLN n 
1 188 VAL n 
1 189 ALA n 
1 190 GLU n 
1 191 ILE n 
1 192 VAL n 
1 193 SER n 
1 194 LYS n 
1 195 TYR n 
1 196 ASP n 
1 197 PRO n 
1 198 ASN n 
1 199 VAL n 
1 200 TYR n 
1 201 SER n 
1 202 ILE n 
1 203 LYS n 
1 204 TYR n 
1 205 ASN n 
1 206 ASN n 
1 207 GLN n 
1 208 LEU n 
1 209 ALA n 
1 210 THR n 
1 211 ARG n 
1 212 THR n 
1 213 ALA n 
1 214 GLN n 
1 215 ALA n 
1 216 ILE n 
1 217 PHE n 
1 218 ASP n 
1 219 ASP n 
1 220 SER n 
1 221 TYR n 
1 222 LEU n 
1 223 GLY n 
1 224 TYR n 
1 225 SER n 
1 226 VAL n 
1 227 ALA n 
1 228 VAL n 
1 229 GLY n 
1 230 ASP n 
1 231 PHE n 
1 232 ASN n 
1 233 GLY n 
1 234 ASP n 
1 235 GLY n 
1 236 ILE n 
1 237 ASP n 
1 238 ASP n 
1 239 PHE n 
1 240 VAL n 
1 241 SER n 
1 242 GLY n 
1 243 VAL n 
1 244 PRO n 
1 245 ARG n 
1 246 ALA n 
1 247 ALA n 
1 248 ARG n 
1 249 THR n 
1 250 LEU n 
1 251 GLY n 
1 252 MET n 
1 253 VAL n 
1 254 TYR n 
1 255 ILE n 
1 256 TYR n 
1 257 ASP n 
1 258 GLY n 
1 259 LYS n 
1 260 ASN n 
1 261 MET n 
1 262 SER n 
1 263 SER n 
1 264 LEU n 
1 265 TYR n 
1 266 ASN n 
1 267 PHE n 
1 268 THR n 
1 269 GLY n 
1 270 GLU n 
1 271 GLN n 
1 272 MET n 
1 273 ALA n 
1 274 ALA n 
1 275 TYR n 
1 276 PHE n 
1 277 GLY n 
1 278 PHE n 
1 279 SER n 
1 280 VAL n 
1 281 ALA n 
1 282 ALA n 
1 283 THR n 
1 284 ASP n 
1 285 ILE n 
1 286 ASN n 
1 287 GLY n 
1 288 ASP n 
1 289 ASP n 
1 290 TYR n 
1 291 ALA n 
1 292 ASP n 
1 293 VAL n 
1 294 PHE n 
1 295 ILE n 
1 296 GLY n 
1 297 ALA n 
1 298 PRO n 
1 299 LEU n 
1 300 PHE n 
1 301 MET n 
1 302 ASP n 
1 303 ARG n 
1 304 GLY n 
1 305 SER n 
1 306 ASP n 
1 307 GLY n 
1 308 LYS n 
1 309 LEU n 
1 310 GLN n 
1 311 GLU n 
1 312 VAL n 
1 313 GLY n 
1 314 GLN n 
1 315 VAL n 
1 316 SER n 
1 317 VAL n 
1 318 SER n 
1 319 LEU n 
1 320 GLN n 
1 321 ARG n 
1 322 ALA n 
1 323 SER n 
1 324 GLY n 
1 325 ASP n 
1 326 PHE n 
1 327 GLN n 
1 328 THR n 
1 329 THR n 
1 330 LYS n 
1 331 LEU n 
1 332 ASN n 
1 333 GLY n 
1 334 PHE n 
1 335 GLU n 
1 336 VAL n 
1 337 PHE n 
1 338 ALA n 
1 339 ARG n 
1 340 PHE n 
1 341 GLY n 
1 342 SER n 
1 343 ALA n 
1 344 ILE n 
1 345 ALA n 
1 346 PRO n 
1 347 LEU n 
1 348 GLY n 
1 349 ASP n 
1 350 LEU n 
1 351 ASP n 
1 352 GLN n 
1 353 ASP n 
1 354 GLY n 
1 355 PHE n 
1 356 ASN n 
1 357 ASP n 
1 358 ILE n 
1 359 ALA n 
1 360 ILE n 
1 361 ALA n 
1 362 ALA n 
1 363 PRO n 
1 364 TYR n 
1 365 GLY n 
1 366 GLY n 
1 367 GLU n 
1 368 ASP n 
1 369 LYS n 
1 370 LYS n 
1 371 GLY n 
1 372 ILE n 
1 373 VAL n 
1 374 TYR n 
1 375 ILE n 
1 376 PHE n 
1 377 ASN n 
1 378 GLY n 
1 379 ARG n 
1 380 SER n 
1 381 THR n 
1 382 GLY n 
1 383 LEU n 
1 384 ASN n 
1 385 ALA n 
1 386 VAL n 
1 387 PRO n 
1 388 SER n 
1 389 GLN n 
1 390 ILE n 
1 391 LEU n 
1 392 GLU n 
1 393 GLY n 
1 394 GLN n 
1 395 TRP n 
1 396 ALA n 
1 397 ALA n 
1 398 ARG n 
1 399 SER n 
1 400 CYS n 
1 401 PRO n 
1 402 PRO n 
1 403 SER n 
1 404 PHE n 
1 405 GLY n 
1 406 TYR n 
1 407 SER n 
1 408 MET n 
1 409 LYS n 
1 410 GLY n 
1 411 ALA n 
1 412 THR n 
1 413 ASP n 
1 414 ILE n 
1 415 ASP n 
1 416 LYS n 
1 417 ASN n 
1 418 GLY n 
1 419 TYR n 
1 420 PRO n 
1 421 ASP n 
1 422 LEU n 
1 423 ILE n 
1 424 VAL n 
1 425 GLY n 
1 426 ALA n 
1 427 PHE n 
1 428 GLY n 
1 429 VAL n 
1 430 ASP n 
1 431 ARG n 
1 432 ALA n 
1 433 ILE n 
1 434 LEU n 
1 435 TYR n 
1 436 ARG n 
1 437 ALA n 
1 438 ARG n 
1 439 PRO n 
1 440 VAL n 
1 441 ILE n 
1 442 THR n 
1 443 VAL n 
1 444 ASN n 
1 445 ALA n 
1 446 GLY n 
1 447 LEU n 
1 448 GLU n 
1 449 VAL n 
1 450 TYR n 
1 451 PRO n 
1 452 SER n 
1 453 ILE n 
1 454 LEU n 
1 455 ASN n 
1 456 GLN n 
1 457 ASP n 
1 458 ASN n 
1 459 LYS n 
1 460 THR n 
1 461 CYS n 
1 462 SER n 
1 463 LEU n 
1 464 PRO n 
1 465 GLY n 
1 466 THR n 
1 467 ALA n 
1 468 LEU n 
1 469 LYS n 
1 470 VAL n 
1 471 SER n 
1 472 CYS n 
1 473 PHE n 
1 474 ASN n 
1 475 VAL n 
1 476 ARG n 
1 477 PHE n 
1 478 CYS n 
1 479 LEU n 
1 480 LYS n 
1 481 ALA n 
1 482 ASP n 
1 483 GLY n 
1 484 LYS n 
1 485 GLY n 
1 486 VAL n 
1 487 LEU n 
1 488 PRO n 
1 489 ARG n 
1 490 LYS n 
1 491 LEU n 
1 492 ASN n 
1 493 PHE n 
1 494 GLN n 
1 495 VAL n 
1 496 GLU n 
1 497 LEU n 
1 498 LEU n 
1 499 LEU n 
1 500 ASP n 
1 501 LYS n 
1 502 LEU n 
1 503 LYS n 
1 504 GLN n 
1 505 LYS n 
1 506 GLY n 
1 507 ALA n 
1 508 ILE n 
1 509 ARG n 
1 510 ARG n 
1 511 ALA n 
1 512 LEU n 
1 513 PHE n 
1 514 LEU n 
1 515 TYR n 
1 516 SER n 
1 517 ARG n 
1 518 SER n 
1 519 PRO n 
1 520 SER n 
1 521 HIS n 
1 522 SER n 
1 523 LYS n 
1 524 ASN n 
1 525 MET n 
1 526 THR n 
1 527 ILE n 
1 528 SER n 
1 529 ARG n 
1 530 GLY n 
1 531 GLY n 
1 532 LEU n 
1 533 MET n 
1 534 GLN n 
1 535 CYS n 
1 536 GLU n 
1 537 GLU n 
1 538 LEU n 
1 539 ILE n 
1 540 ALA n 
1 541 TYR n 
1 542 LEU n 
1 543 ARG n 
1 544 ASP n 
1 545 GLU n 
1 546 SER n 
1 547 GLU n 
1 548 PHE n 
1 549 ARG n 
1 550 ASP n 
1 551 LYS n 
1 552 LEU n 
1 553 THR n 
1 554 PRO n 
1 555 ILE n 
1 556 THR n 
1 557 ILE n 
1 558 PHE n 
1 559 MET n 
1 560 GLU n 
1 561 TYR n 
1 562 ARG n 
1 563 LEU n 
1 564 ASP n 
1 565 TYR n 
1 566 ARG n 
1 567 THR n 
1 568 ALA n 
1 569 ALA n 
1 570 ASP n 
1 571 THR n 
1 572 THR n 
1 573 GLY n 
1 574 LEU n 
1 575 GLN n 
1 576 PRO n 
1 577 ILE n 
1 578 LEU n 
1 579 ASN n 
1 580 GLN n 
1 581 PHE n 
1 582 THR n 
1 583 PRO n 
1 584 ALA n 
1 585 ASN n 
1 586 ILE n 
1 587 SER n 
1 588 ARG n 
1 589 GLN n 
1 590 ALA n 
1 591 HIS n 
1 592 ILE n 
1 593 LEU n 
1 594 LEU n 
1 595 ASP n 
1 596 GLY n 
1 597 GLY n 
1 598 SER n 
1 599 LEU n 
1 600 GLU n 
1 601 VAL n 
1 602 LEU n 
1 603 PHE n 
1 604 GLN n 
1 605 GLY n 
2 1   GLY n 
2 2   CYS n 
2 3   ALA n 
2 4   LEU n 
2 5   GLY n 
2 6   GLY n 
2 7   ALA n 
2 8   GLU n 
2 9   THR n 
2 10  CYS n 
2 11  GLU n 
2 12  ASP n 
2 13  CYS n 
2 14  LEU n 
2 15  LEU n 
2 16  ILE n 
2 17  GLY n 
2 18  PRO n 
2 19  GLN n 
2 20  CYS n 
2 21  ALA n 
2 22  TRP n 
2 23  CYS n 
2 24  ALA n 
2 25  GLN n 
2 26  GLU n 
2 27  ASN n 
2 28  PHE n 
2 29  THR n 
2 30  HIS n 
2 31  PRO n 
2 32  SER n 
2 33  GLY n 
2 34  VAL n 
2 35  GLY n 
2 36  GLU n 
2 37  ARG n 
2 38  CYS n 
2 39  ASP n 
2 40  THR n 
2 41  PRO n 
2 42  ALA n 
2 43  ASN n 
2 44  LEU n 
2 45  LEU n 
2 46  ALA n 
2 47  LYS n 
2 48  GLY n 
2 49  CYS n 
2 50  GLN n 
2 51  LEU n 
2 52  ASN n 
2 53  PHE n 
2 54  ILE n 
2 55  GLU n 
2 56  ASN n 
2 57  PRO n 
2 58  VAL n 
2 59  SER n 
2 60  GLN n 
2 61  VAL n 
2 62  GLU n 
2 63  ILE n 
2 64  LEU n 
2 65  LYS n 
2 66  ASN n 
2 67  LYS n 
2 68  PRO n 
2 69  LEU n 
2 70  SER n 
2 71  VAL n 
2 72  GLY n 
2 73  ARG n 
2 74  GLN n 
2 75  LYS n 
2 76  ASN n 
2 77  SER n 
2 78  SER n 
2 79  ASP n 
2 80  ILE n 
2 81  VAL n 
2 82  GLN n 
2 83  ILE n 
2 84  ALA n 
2 85  PRO n 
2 86  GLN n 
2 87  SER n 
2 88  LEU n 
2 89  ILE n 
2 90  LEU n 
2 91  LYS n 
2 92  LEU n 
2 93  ARG n 
2 94  PRO n 
2 95  GLY n 
2 96  GLY n 
2 97  ALA n 
2 98  GLN n 
2 99  THR n 
2 100 LEU n 
2 101 GLN n 
2 102 VAL n 
2 103 HIS n 
2 104 VAL n 
2 105 ARG n 
2 106 GLN n 
2 107 THR n 
2 108 GLU n 
2 109 ASP n 
2 110 TYR n 
2 111 PRO n 
2 112 VAL n 
2 113 ASP n 
2 114 LEU n 
2 115 TYR n 
2 116 TYR n 
2 117 LEU n 
2 118 MET n 
2 119 ASP n 
2 120 LEU n 
2 121 SER n 
2 122 ALA n 
2 123 SER n 
2 124 MET n 
2 125 ASP n 
2 126 ASP n 
2 127 ASP n 
2 128 LEU n 
2 129 ASN n 
2 130 THR n 
2 131 ILE n 
2 132 LYS n 
2 133 GLU n 
2 134 LEU n 
2 135 GLY n 
2 136 SER n 
2 137 ARG n 
2 138 LEU n 
2 139 SER n 
2 140 LYS n 
2 141 GLU n 
2 142 MET n 
2 143 SER n 
2 144 LYS n 
2 145 LEU n 
2 146 THR n 
2 147 SER n 
2 148 ASN n 
2 149 PHE n 
2 150 ARG n 
2 151 LEU n 
2 152 GLY n 
2 153 PHE n 
2 154 GLY n 
2 155 SER n 
2 156 PHE n 
2 157 VAL n 
2 158 GLU n 
2 159 LYS n 
2 160 PRO n 
2 161 VAL n 
2 162 SER n 
2 163 PRO n 
2 164 PHE n 
2 165 VAL n 
2 166 LYS n 
2 167 THR n 
2 168 THR n 
2 169 PRO n 
2 170 GLU n 
2 171 GLU n 
2 172 ILE n 
2 173 ALA n 
2 174 ASN n 
2 175 PRO n 
2 176 CYS n 
2 177 SER n 
2 178 SER n 
2 179 ILE n 
2 180 PRO n 
2 181 TYR n 
2 182 PHE n 
2 183 CYS n 
2 184 LEU n 
2 185 PRO n 
2 186 THR n 
2 187 PHE n 
2 188 GLY n 
2 189 PHE n 
2 190 LYS n 
2 191 HIS n 
2 192 ILE n 
2 193 LEU n 
2 194 PRO n 
2 195 LEU n 
2 196 THR n 
2 197 ASN n 
2 198 ASP n 
2 199 ALA n 
2 200 GLU n 
2 201 ARG n 
2 202 PHE n 
2 203 ASN n 
2 204 GLU n 
2 205 ILE n 
2 206 VAL n 
2 207 LYS n 
2 208 ASN n 
2 209 GLN n 
2 210 LYS n 
2 211 ILE n 
2 212 SER n 
2 213 ALA n 
2 214 ASN n 
2 215 ILE n 
2 216 ASP n 
2 217 THR n 
2 218 PRO n 
2 219 GLU n 
2 220 GLY n 
2 221 GLY n 
2 222 PHE n 
2 223 ASP n 
2 224 ALA n 
2 225 ILE n 
2 226 MET n 
2 227 GLN n 
2 228 ALA n 
2 229 ALA n 
2 230 VAL n 
2 231 CYS n 
2 232 LYS n 
2 233 GLU n 
2 234 LYS n 
2 235 ILE n 
2 236 GLY n 
2 237 TRP n 
2 238 ARG n 
2 239 ASN n 
2 240 ASP n 
2 241 SER n 
2 242 LEU n 
2 243 HIS n 
2 244 LEU n 
2 245 LEU n 
2 246 VAL n 
2 247 PHE n 
2 248 VAL n 
2 249 SER n 
2 250 ASP n 
2 251 ALA n 
2 252 ASP n 
2 253 SER n 
2 254 HIS n 
2 255 PHE n 
2 256 GLY n 
2 257 MET n 
2 258 ASP n 
2 259 SER n 
2 260 LYS n 
2 261 LEU n 
2 262 ALA n 
2 263 GLY n 
2 264 ILE n 
2 265 VAL n 
2 266 CYS n 
2 267 PRO n 
2 268 ASN n 
2 269 ASP n 
2 270 GLY n 
2 271 LEU n 
2 272 CYS n 
2 273 HIS n 
2 274 LEU n 
2 275 ASP n 
2 276 SER n 
2 277 LYS n 
2 278 ASN n 
2 279 GLU n 
2 280 TYR n 
2 281 SER n 
2 282 MET n 
2 283 SER n 
2 284 THR n 
2 285 VAL n 
2 286 LEU n 
2 287 GLU n 
2 288 TYR n 
2 289 PRO n 
2 290 THR n 
2 291 ILE n 
2 292 GLY n 
2 293 GLN n 
2 294 LEU n 
2 295 ILE n 
2 296 ASP n 
2 297 LYS n 
2 298 LEU n 
2 299 VAL n 
2 300 GLN n 
2 301 ASN n 
2 302 ASN n 
2 303 VAL n 
2 304 LEU n 
2 305 LEU n 
2 306 ILE n 
2 307 PHE n 
2 308 ALA n 
2 309 VAL n 
2 310 THR n 
2 311 GLN n 
2 312 GLU n 
2 313 GLN n 
2 314 VAL n 
2 315 HIS n 
2 316 LEU n 
2 317 TYR n 
2 318 GLU n 
2 319 ASN n 
2 320 TYR n 
2 321 ALA n 
2 322 LYS n 
2 323 LEU n 
2 324 ILE n 
2 325 PRO n 
2 326 GLY n 
2 327 ALA n 
2 328 THR n 
2 329 VAL n 
2 330 GLY n 
2 331 LEU n 
2 332 LEU n 
2 333 GLN n 
2 334 LYS n 
2 335 ASP n 
2 336 SER n 
2 337 GLY n 
2 338 ASN n 
2 339 ILE n 
2 340 LEU n 
2 341 GLN n 
2 342 LEU n 
2 343 ILE n 
2 344 ILE n 
2 345 SER n 
2 346 ALA n 
2 347 TYR n 
2 348 GLU n 
2 349 GLU n 
2 350 LEU n 
2 351 ARG n 
2 352 SER n 
2 353 GLU n 
2 354 VAL n 
2 355 GLU n 
2 356 LEU n 
2 357 GLU n 
2 358 VAL n 
2 359 LEU n 
2 360 GLY n 
2 361 ASP n 
2 362 THR n 
2 363 GLU n 
2 364 GLY n 
2 365 LEU n 
2 366 ASN n 
2 367 LEU n 
2 368 SER n 
2 369 PHE n 
2 370 THR n 
2 371 ALA n 
2 372 ILE n 
2 373 CYS n 
2 374 ASN n 
2 375 ASN n 
2 376 GLY n 
2 377 THR n 
2 378 LEU n 
2 379 PHE n 
2 380 GLN n 
2 381 HIS n 
2 382 GLN n 
2 383 LYS n 
2 384 LYS n 
2 385 CYS n 
2 386 SER n 
2 387 HIS n 
2 388 MET n 
2 389 LYS n 
2 390 VAL n 
2 391 GLY n 
2 392 ASP n 
2 393 THR n 
2 394 ALA n 
2 395 SER n 
2 396 PHE n 
2 397 SER n 
2 398 VAL n 
2 399 THR n 
2 400 VAL n 
2 401 ASN n 
2 402 ILE n 
2 403 PRO n 
2 404 HIS n 
2 405 CYS n 
2 406 GLU n 
2 407 ARG n 
2 408 ARG n 
2 409 SER n 
2 410 ARG n 
2 411 HIS n 
2 412 ILE n 
2 413 ILE n 
2 414 ILE n 
2 415 LYS n 
2 416 PRO n 
2 417 VAL n 
2 418 GLY n 
2 419 LEU n 
2 420 GLY n 
2 421 ASP n 
2 422 ALA n 
2 423 LEU n 
2 424 GLU n 
2 425 LEU n 
2 426 LEU n 
2 427 VAL n 
2 428 SER n 
2 429 PRO n 
2 430 GLU n 
2 431 CYS n 
2 432 ASN n 
2 433 CYS n 
2 434 ASP n 
2 435 CYS n 
2 436 GLN n 
2 437 LYS n 
2 438 GLU n 
2 439 VAL n 
2 440 GLU n 
2 441 VAL n 
2 442 ASN n 
2 443 SER n 
2 444 SER n 
2 445 LYS n 
2 446 CYS n 
2 447 HIS n 
2 448 HIS n 
2 449 GLY n 
2 450 ASN n 
2 451 GLY n 
2 452 SER n 
2 453 PHE n 
2 454 GLN n 
2 455 CYS n 
2 456 GLY n 
2 457 VAL n 
2 458 CYS n 
2 459 ALA n 
2 460 CYS n 
2 461 HIS n 
2 462 PRO n 
2 463 GLY n 
2 464 HIS n 
2 465 MET n 
2 466 GLY n 
2 467 PRO n 
2 468 ARG n 
2 469 CYS n 
2 470 GLU n 
2 471 SER n 
2 472 GLY n 
2 473 HIS n 
2 474 SER n 
2 475 LEU n 
2 476 GLU n 
2 477 VAL n 
2 478 LEU n 
2 479 PHE n 
2 480 GLN n 
2 481 GLY n 
3 1   ASP n 
3 2   ILE n 
3 3   GLN n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   THR n 
3 8   THR n 
3 9   SER n 
3 10  SER n 
3 11  LEU n 
3 12  SER n 
3 13  ALA n 
3 14  SER n 
3 15  LEU n 
3 16  GLY n 
3 17  ASP n 
3 18  ARG n 
3 19  VAL n 
3 20  ILE n 
3 21  ILE n 
3 22  SER n 
3 23  CYS n 
3 24  ARG n 
3 25  ALA n 
3 26  SER n 
3 27  GLN n 
3 28  ASP n 
3 29  ILE n 
3 30  SER n 
3 31  ASN n 
3 32  TYR n 
3 33  LEU n 
3 34  SER n 
3 35  TRP n 
3 36  TYR n 
3 37  GLN n 
3 38  GLN n 
3 39  LYS n 
3 40  PRO n 
3 41  ASP n 
3 42  GLY n 
3 43  THR n 
3 44  VAL n 
3 45  LYS n 
3 46  LEU n 
3 47  LEU n 
3 48  ILE n 
3 49  PHE n 
3 50  TYR n 
3 51  THR n 
3 52  SER n 
3 53  LYS n 
3 54  LEU n 
3 55  HIS n 
3 56  SER n 
3 57  GLY n 
3 58  VAL n 
3 59  PRO n 
3 60  SER n 
3 61  ARG n 
3 62  PHE n 
3 63  SER n 
3 64  GLY n 
3 65  SER n 
3 66  GLY n 
3 67  SER n 
3 68  GLY n 
3 69  THR n 
3 70  ASP n 
3 71  TYR n 
3 72  SER n 
3 73  LEU n 
3 74  THR n 
3 75  ILE n 
3 76  SER n 
3 77  ASN n 
3 78  LEU n 
3 79  ASP n 
3 80  GLN n 
3 81  GLU n 
3 82  ASP n 
3 83  ILE n 
3 84  ALA n 
3 85  THR n 
3 86  TYR n 
3 87  PHE n 
3 88  CYS n 
3 89  GLN n 
3 90  GLN n 
3 91  GLY n 
3 92  ASN n 
3 93  THR n 
3 94  PHE n 
3 95  PRO n 
3 96  TYR n 
3 97  THR n 
3 98  PHE n 
3 99  GLY n 
3 100 GLY n 
3 101 GLY n 
3 102 THR n 
3 103 LYS n 
3 104 VAL n 
3 105 GLU n 
3 106 MET n 
3 107 ARG n 
3 108 ARG n 
3 109 ALA n 
3 110 ASP n 
3 111 ALA n 
3 112 ALA n 
3 113 PRO n 
3 114 THR n 
3 115 VAL n 
3 116 SER n 
3 117 ILE n 
3 118 PHE n 
3 119 PRO n 
3 120 PRO n 
3 121 SER n 
3 122 SER n 
3 123 GLU n 
3 124 GLN n 
3 125 LEU n 
3 126 THR n 
3 127 SER n 
3 128 GLY n 
3 129 GLY n 
3 130 ALA n 
3 131 SER n 
3 132 VAL n 
3 133 VAL n 
3 134 CYS n 
3 135 PHE n 
3 136 LEU n 
3 137 ASN n 
3 138 ASN n 
3 139 PHE n 
3 140 TYR n 
3 141 PRO n 
3 142 LYS n 
3 143 ASP n 
3 144 ILE n 
3 145 ASN n 
3 146 VAL n 
3 147 LYS n 
3 148 TRP n 
3 149 LYS n 
3 150 ILE n 
3 151 ASP n 
3 152 GLY n 
3 153 SER n 
3 154 GLU n 
3 155 ARG n 
3 156 GLN n 
3 157 ASN n 
3 158 GLY n 
3 159 VAL n 
3 160 LEU n 
3 161 ASN n 
3 162 SER n 
3 163 TRP n 
3 164 THR n 
3 165 ASP n 
3 166 GLN n 
3 167 ASP n 
3 168 SER n 
3 169 LYS n 
3 170 ASP n 
3 171 SER n 
3 172 THR n 
3 173 TYR n 
3 174 SER n 
3 175 PHE n 
3 176 SER n 
3 177 SER n 
3 178 THR n 
3 179 LEU n 
3 180 THR n 
3 181 LEU n 
3 182 THR n 
3 183 LYS n 
3 184 ASP n 
3 185 GLU n 
3 186 TYR n 
3 187 GLU n 
3 188 ARG n 
3 189 HIS n 
3 190 ASN n 
3 191 SER n 
3 192 TYR n 
3 193 THR n 
3 194 CYS n 
3 195 GLU n 
3 196 ALA n 
3 197 THR n 
3 198 HIS n 
3 199 LYS n 
3 200 THR n 
3 201 SER n 
3 202 THR n 
3 203 SER n 
3 204 PRO n 
3 205 ILE n 
3 206 VAL n 
3 207 LYS n 
3 208 SER n 
3 209 PHE n 
3 210 ASN n 
3 211 ARG n 
3 212 ASN n 
3 213 GLU n 
3 214 CYS n 
4 1   GLN n 
4 2   VAL n 
4 3   GLN n 
4 4   LEU n 
4 5   GLN n 
4 6   GLN n 
4 7   SER n 
4 8   GLY n 
4 9   ALA n 
4 10  GLU n 
4 11  LEU n 
4 12  ALA n 
4 13  GLU n 
4 14  PRO n 
4 15  GLY n 
4 16  ALA n 
4 17  SER n 
4 18  VAL n 
4 19  LYS n 
4 20  MET n 
4 21  SER n 
4 22  CYS n 
4 23  LYS n 
4 24  ALA n 
4 25  SER n 
4 26  GLY n 
4 27  TYR n 
4 28  THR n 
4 29  PHE n 
4 30  SER n 
4 31  SER n 
4 32  PHE n 
4 33  TRP n 
4 34  MET n 
4 35  HIS n 
4 36  TRP n 
4 37  VAL n 
4 38  LYS n 
4 39  GLN n 
4 40  ARG n 
4 41  PRO n 
4 42  GLY n 
4 43  GLN n 
4 44  GLY n 
4 45  LEU n 
4 46  GLU n 
4 47  TRP n 
4 48  ILE n 
4 49  GLY n 
4 50  TYR n 
4 51  ILE n 
4 52  ASN n 
4 53  PRO n 
4 54  ASN n 
4 55  SER n 
4 56  GLY n 
4 57  TYR n 
4 58  THR n 
4 59  GLU n 
4 60  CYS n 
4 61  ASN n 
4 62  GLU n 
4 63  ILE n 
4 64  PHE n 
4 65  ARG n 
4 66  ASP n 
4 67  LYS n 
4 68  ALA n 
4 69  THR n 
4 70  MET n 
4 71  THR n 
4 72  ALA n 
4 73  ASP n 
4 74  THR n 
4 75  SER n 
4 76  SER n 
4 77  SER n 
4 78  THR n 
4 79  ALA n 
4 80  TYR n 
4 81  MET n 
4 82  GLN n 
4 83  LEU n 
4 84  SER n 
4 85  GLY n 
4 86  LEU n 
4 87  THR n 
4 88  SER n 
4 89  GLU n 
4 90  ASP n 
4 91  SER n 
4 92  ALA n 
4 93  VAL n 
4 94  TYR n 
4 95  TYR n 
4 96  CYS n 
4 97  ALA n 
4 98  SER n 
4 99  PHE n 
4 100 LEU n 
4 101 GLY n 
4 102 ARG n 
4 103 GLY n 
4 104 ALA n 
4 105 MET n 
4 106 ASP n 
4 107 TYR n 
4 108 TRP n 
4 109 GLY n 
4 110 GLN n 
4 111 GLY n 
4 112 THR n 
4 113 SER n 
4 114 VAL n 
4 115 THR n 
4 116 VAL n 
4 117 SER n 
4 118 SER n 
4 119 ALA n 
4 120 LYS n 
4 121 THR n 
4 122 THR n 
4 123 ALA n 
4 124 PRO n 
4 125 SER n 
4 126 VAL n 
4 127 TYR n 
4 128 PRO n 
4 129 LEU n 
4 130 ALA n 
4 131 PRO n 
4 132 VAL n 
4 133 CYS n 
4 134 GLY n 
4 135 ASP n 
4 136 THR n 
4 137 THR n 
4 138 GLY n 
4 139 SER n 
4 140 SER n 
4 141 VAL n 
4 142 THR n 
4 143 LEU n 
4 144 GLY n 
4 145 CYS n 
4 146 LEU n 
4 147 VAL n 
4 148 LYS n 
4 149 GLY n 
4 150 TYR n 
4 151 PHE n 
4 152 PRO n 
4 153 GLU n 
4 154 PRO n 
4 155 VAL n 
4 156 THR n 
4 157 LEU n 
4 158 THR n 
4 159 TRP n 
4 160 ASN n 
4 161 SER n 
4 162 GLY n 
4 163 SER n 
4 164 LEU n 
4 165 SER n 
4 166 ALA n 
4 167 GLY n 
4 168 VAL n 
4 169 HIS n 
4 170 THR n 
4 171 PHE n 
4 172 PRO n 
4 173 ALA n 
4 174 VAL n 
4 175 LEU n 
4 176 GLN n 
4 177 SER n 
4 178 SER n 
4 179 LEU n 
4 180 TYR n 
4 181 THR n 
4 182 LEU n 
4 183 SER n 
4 184 SER n 
4 185 SER n 
4 186 VAL n 
4 187 THR n 
4 188 VAL n 
4 189 VAL n 
4 190 ALA n 
4 191 SER n 
4 192 THR n 
4 193 TRP n 
4 194 PRO n 
4 195 SER n 
4 196 GLN n 
4 197 SER n 
4 198 ILE n 
4 199 THR n 
4 200 CYS n 
4 201 ASN n 
4 202 VAL n 
4 203 ALA n 
4 204 HIS n 
4 205 PRO n 
4 206 ALA n 
4 207 SER n 
4 208 SER n 
4 209 THR n 
4 210 LYS n 
4 211 VAL n 
4 212 ASP n 
4 213 LYS n 
4 214 LYS n 
4 215 ILE n 
4 216 GLU n 
4 217 PRO n 
4 218 ARG n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 605 human ? 'ITGAV, MSK8, VNRA, VTNR' ? ? ? ? ? ? 'Homo sapiens' 9606  ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 481 human ? ITGB6                     ? ? ? ? ? ? 'Homo sapiens' 9606  ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 214 ?     ? ?                         ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 218 ?     ? ?                         ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
5 oligosaccharide 
6 oligosaccharide 
7 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 5 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                                         
'Glycam Condensed Sequence' GMML       1.0   
2 5 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1'                                                
WURCS                       PDB2Glycan 1.1.0 
3 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'                                                          
LINUCS                      PDB-CARE   ?     
4 6 'DManpa1-3[DManpa1-6]DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH'                                                          
'Glycam Condensed Sequence' GMML       1.0   
5 6 'WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c6-d1_d3-e1_d6-f1'         
WURCS                       PDB2Glycan 1.1.0 
6 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}' 
LINUCS                      PDB-CARE   ?     
7 7 'DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH'                                                                   
'Glycam Condensed Sequence' GMML       1.0   
8 7 'WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1'                 
WURCS                       PDB2Glycan 1.1.0 
9 7 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}'                    
LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1  5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2  5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3  6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
4  6 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
5  6 4 MAN C1 O1 3 BMA O6 HO6 sing ? 
6  6 5 MAN C1 O1 4 MAN O3 HO3 sing ? 
7  6 6 MAN C1 O1 4 MAN O6 HO6 sing ? 
8  7 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
9  7 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
10 7 4 MAN C1 O1 3 BMA O3 HO3 sing ? 
11 7 5 MAN C1 O1 3 BMA O6 HO6 sing ? 
# 
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 
A1A6A non-polymer                   . 
'(2S)-phenyl{(3S)-3-[4-(5,6,7,8-tetrahydro-1,8-naphthyridin-2-yl)butoxy]pyrrolidin-1-yl}acetic acid' ? 'C24 H31 N3 O3'  409.521 
ACT   non-polymer                   . 'ACETATE ION' ? 'C2 H3 O2 -1'    59.044  
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 
BMA   'D-saccharide, beta linking'  . beta-D-mannopyranose 'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
CA    non-polymer                   . 'CALCIUM ION' ? 'Ca 2'           40.078  
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  
GOL   non-polymer                   . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS   'L-peptide linking'           y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer                   . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking'           y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking'           y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking'           y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MAN   'D-saccharide, alpha linking' . alpha-D-mannopyranose 'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6'      180.156 
MET   'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
MG    non-polymer                   . 'MAGNESIUM ION' ? 'Mg 2'           24.305  
NAG   'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE   'L-peptide linking'           y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking'           y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking'           y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking'           y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking'           y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking'           y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking'           y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   PHE 1   1   1   PHE PHE A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  TYR 11  11  11  TYR TYR A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  PHE 19  19  19  PHE PHE A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  CYS 59  59  59  CYS CYS A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  TRP 61  61  61  TRP TRP A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  CYS 67  67  67  CYS CYS A . n 
A 1 68  GLN 68  68  68  GLN GLN A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  TRP 93  93  93  TRP TRP A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 ALA 107 107 107 ALA ALA A . n 
A 1 108 CYS 108 108 108 CYS CYS A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 TYR 112 112 112 TYR TYR A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 TRP 114 114 114 TRP TRP A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 CYS 142 142 142 CYS CYS A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 GLN 145 145 145 GLN GLN A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 ILE 147 147 147 ILE ILE A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 CYS 155 155 155 CYS CYS A . n 
A 1 156 GLN 156 156 156 GLN GLN A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 PHE 163 163 163 PHE PHE A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 TRP 179 179 179 TRP TRP A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 TYR 195 195 195 TYR TYR A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 ASN 198 198 198 ASN ASN A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 TYR 200 200 200 TYR TYR A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 GLN 207 207 207 GLN GLN A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 THR 212 212 212 THR THR A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 GLN 214 214 214 GLN GLN A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 ASP 237 237 237 ASP ASP A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 PRO 244 244 244 PRO PRO A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 MET 261 261 261 MET MET A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 TYR 265 265 265 TYR TYR A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 MET 272 272 272 MET MET A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 ALA 274 274 274 ALA ALA A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 PHE 278 278 278 PHE PHE A . n 
A 1 279 SER 279 279 279 SER SER A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 THR 283 283 283 THR THR A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ASN 286 286 286 ASN ASN A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 MET 301 301 301 MET MET A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 SER 305 305 305 SER SER A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 GLN 314 314 314 GLN GLN A . n 
A 1 315 VAL 315 315 315 VAL VAL A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 SER 318 318 318 SER SER A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 ARG 321 321 321 ARG ARG A . n 
A 1 322 ALA 322 322 322 ALA ALA A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 GLN 327 327 327 GLN GLN A . n 
A 1 328 THR 328 328 328 THR THR A . n 
A 1 329 THR 329 329 329 THR THR A . n 
A 1 330 LYS 330 330 330 LYS LYS A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 GLY 333 333 333 GLY GLY A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 GLU 335 335 335 GLU GLU A . n 
A 1 336 VAL 336 336 336 VAL VAL A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 ARG 339 339 339 ARG ARG A . n 
A 1 340 PHE 340 340 340 PHE PHE A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 PRO 346 346 346 PRO PRO A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 GLN 352 352 352 GLN GLN A . n 
A 1 353 ASP 353 353 353 ASP ASP A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 ASP 357 357 357 ASP ASP A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 ILE 360 360 360 ILE ILE A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 ALA 362 362 362 ALA ALA A . n 
A 1 363 PRO 363 363 363 PRO PRO A . n 
A 1 364 TYR 364 364 364 TYR TYR A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 ASP 368 368 368 ASP ASP A . n 
A 1 369 LYS 369 369 369 LYS LYS A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 GLY 371 371 371 GLY GLY A . n 
A 1 372 ILE 372 372 372 ILE ILE A . n 
A 1 373 VAL 373 373 373 VAL VAL A . n 
A 1 374 TYR 374 374 374 TYR TYR A . n 
A 1 375 ILE 375 375 375 ILE ILE A . n 
A 1 376 PHE 376 376 376 PHE PHE A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 GLY 378 378 378 GLY GLY A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 SER 380 380 380 SER SER A . n 
A 1 381 THR 381 381 381 THR THR A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 LEU 383 383 383 LEU LEU A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 PRO 387 387 387 PRO PRO A . n 
A 1 388 SER 388 388 388 SER SER A . n 
A 1 389 GLN 389 389 389 GLN GLN A . n 
A 1 390 ILE 390 390 390 ILE ILE A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 GLN 394 394 394 GLN GLN A . n 
A 1 395 TRP 395 395 395 TRP TRP A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 ARG 398 398 398 ARG ARG A . n 
A 1 399 SER 399 399 399 SER SER A . n 
A 1 400 CYS 400 400 400 CYS CYS A . n 
A 1 401 PRO 401 401 401 PRO PRO A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 PHE 404 404 404 PHE PHE A . n 
A 1 405 GLY 405 405 405 GLY GLY A . n 
A 1 406 TYR 406 406 406 TYR TYR A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 MET 408 408 408 MET MET A . n 
A 1 409 LYS 409 409 409 LYS LYS A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 ALA 411 411 411 ALA ALA A . n 
A 1 412 THR 412 412 412 THR THR A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 ILE 414 414 414 ILE ILE A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 LYS 416 416 416 LYS LYS A . n 
A 1 417 ASN 417 417 417 ASN ASN A . n 
A 1 418 GLY 418 418 418 GLY GLY A . n 
A 1 419 TYR 419 419 419 TYR TYR A . n 
A 1 420 PRO 420 420 420 PRO PRO A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 ILE 423 423 423 ILE ILE A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 ALA 426 426 426 ALA ALA A . n 
A 1 427 PHE 427 427 427 PHE PHE A . n 
A 1 428 GLY 428 428 428 GLY GLY A . n 
A 1 429 VAL 429 429 429 VAL VAL A . n 
A 1 430 ASP 430 430 430 ASP ASP A . n 
A 1 431 ARG 431 431 431 ARG ARG A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 LEU 434 434 434 LEU LEU A . n 
A 1 435 TYR 435 435 435 TYR TYR A . n 
A 1 436 ARG 436 436 436 ARG ARG A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 PRO 439 439 439 PRO PRO A . n 
A 1 440 VAL 440 440 440 VAL VAL A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 THR 442 442 442 THR THR A . n 
A 1 443 VAL 443 443 443 VAL VAL A . n 
A 1 444 ASN 444 444 444 ASN ASN A . n 
A 1 445 ALA 445 445 445 ALA ALA A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 VAL 449 449 449 VAL VAL A . n 
A 1 450 TYR 450 450 450 TYR TYR A . n 
A 1 451 PRO 451 451 451 PRO PRO A . n 
A 1 452 SER 452 452 452 SER SER A . n 
A 1 453 ILE 453 453 453 ILE ILE A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 GLN 456 456 456 GLN GLN A . n 
A 1 457 ASP 457 457 457 ASP ASP A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 THR 460 460 460 THR THR A . n 
A 1 461 CYS 461 461 461 CYS CYS A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 PRO 464 464 464 PRO PRO A . n 
A 1 465 GLY 465 465 465 GLY GLY A . n 
A 1 466 THR 466 466 466 THR THR A . n 
A 1 467 ALA 467 467 467 ALA ALA A . n 
A 1 468 LEU 468 468 468 LEU LEU A . n 
A 1 469 LYS 469 469 469 LYS LYS A . n 
A 1 470 VAL 470 470 470 VAL VAL A . n 
A 1 471 SER 471 471 471 SER SER A . n 
A 1 472 CYS 472 472 472 CYS CYS A . n 
A 1 473 PHE 473 473 473 PHE PHE A . n 
A 1 474 ASN 474 474 474 ASN ASN A . n 
A 1 475 VAL 475 475 475 VAL VAL A . n 
A 1 476 ARG 476 476 476 ARG ARG A . n 
A 1 477 PHE 477 477 477 PHE PHE A . n 
A 1 478 CYS 478 478 478 CYS CYS A . n 
A 1 479 LEU 479 479 479 LEU LEU A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 ASP 482 482 482 ASP ASP A . n 
A 1 483 GLY 483 483 483 GLY GLY A . n 
A 1 484 LYS 484 484 484 LYS LYS A . n 
A 1 485 GLY 485 485 485 GLY GLY A . n 
A 1 486 VAL 486 486 486 VAL VAL A . n 
A 1 487 LEU 487 487 487 LEU LEU A . n 
A 1 488 PRO 488 488 488 PRO PRO A . n 
A 1 489 ARG 489 489 489 ARG ARG A . n 
A 1 490 LYS 490 490 490 LYS LYS A . n 
A 1 491 LEU 491 491 491 LEU LEU A . n 
A 1 492 ASN 492 492 492 ASN ASN A . n 
A 1 493 PHE 493 493 493 PHE PHE A . n 
A 1 494 GLN 494 494 494 GLN GLN A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 GLU 496 496 496 GLU GLU A . n 
A 1 497 LEU 497 497 497 LEU LEU A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 LEU 499 499 499 LEU LEU A . n 
A 1 500 ASP 500 500 500 ASP ASP A . n 
A 1 501 LYS 501 501 501 LYS LYS A . n 
A 1 502 LEU 502 502 502 LEU LEU A . n 
A 1 503 LYS 503 503 503 LYS LYS A . n 
A 1 504 GLN 504 504 504 GLN GLN A . n 
A 1 505 LYS 505 505 505 LYS LYS A . n 
A 1 506 GLY 506 506 506 GLY GLY A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 ILE 508 508 508 ILE ILE A . n 
A 1 509 ARG 509 509 509 ARG ARG A . n 
A 1 510 ARG 510 510 510 ARG ARG A . n 
A 1 511 ALA 511 511 511 ALA ALA A . n 
A 1 512 LEU 512 512 512 LEU LEU A . n 
A 1 513 PHE 513 513 513 PHE PHE A . n 
A 1 514 LEU 514 514 514 LEU LEU A . n 
A 1 515 TYR 515 515 515 TYR TYR A . n 
A 1 516 SER 516 516 516 SER SER A . n 
A 1 517 ARG 517 517 517 ARG ARG A . n 
A 1 518 SER 518 518 518 SER SER A . n 
A 1 519 PRO 519 519 519 PRO PRO A . n 
A 1 520 SER 520 520 520 SER SER A . n 
A 1 521 HIS 521 521 521 HIS HIS A . n 
A 1 522 SER 522 522 522 SER SER A . n 
A 1 523 LYS 523 523 523 LYS LYS A . n 
A 1 524 ASN 524 524 524 ASN ASN A . n 
A 1 525 MET 525 525 525 MET MET A . n 
A 1 526 THR 526 526 526 THR THR A . n 
A 1 527 ILE 527 527 527 ILE ILE A . n 
A 1 528 SER 528 528 528 SER SER A . n 
A 1 529 ARG 529 529 529 ARG ARG A . n 
A 1 530 GLY 530 530 530 GLY GLY A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 LEU 532 532 532 LEU LEU A . n 
A 1 533 MET 533 533 533 MET MET A . n 
A 1 534 GLN 534 534 534 GLN GLN A . n 
A 1 535 CYS 535 535 535 CYS CYS A . n 
A 1 536 GLU 536 536 536 GLU GLU A . n 
A 1 537 GLU 537 537 537 GLU GLU A . n 
A 1 538 LEU 538 538 538 LEU LEU A . n 
A 1 539 ILE 539 539 539 ILE ILE A . n 
A 1 540 ALA 540 540 540 ALA ALA A . n 
A 1 541 TYR 541 541 541 TYR TYR A . n 
A 1 542 LEU 542 542 542 LEU LEU A . n 
A 1 543 ARG 543 543 543 ARG ARG A . n 
A 1 544 ASP 544 544 544 ASP ASP A . n 
A 1 545 GLU 545 545 545 GLU GLU A . n 
A 1 546 SER 546 546 546 SER SER A . n 
A 1 547 GLU 547 547 547 GLU GLU A . n 
A 1 548 PHE 548 548 548 PHE PHE A . n 
A 1 549 ARG 549 549 549 ARG ARG A . n 
A 1 550 ASP 550 550 550 ASP ASP A . n 
A 1 551 LYS 551 551 551 LYS LYS A . n 
A 1 552 LEU 552 552 552 LEU LEU A . n 
A 1 553 THR 553 553 553 THR THR A . n 
A 1 554 PRO 554 554 554 PRO PRO A . n 
A 1 555 ILE 555 555 555 ILE ILE A . n 
A 1 556 THR 556 556 556 THR THR A . n 
A 1 557 ILE 557 557 557 ILE ILE A . n 
A 1 558 PHE 558 558 558 PHE PHE A . n 
A 1 559 MET 559 559 559 MET MET A . n 
A 1 560 GLU 560 560 560 GLU GLU A . n 
A 1 561 TYR 561 561 561 TYR TYR A . n 
A 1 562 ARG 562 562 562 ARG ARG A . n 
A 1 563 LEU 563 563 563 LEU LEU A . n 
A 1 564 ASP 564 564 564 ASP ASP A . n 
A 1 565 TYR 565 565 565 TYR TYR A . n 
A 1 566 ARG 566 566 566 ARG ARG A . n 
A 1 567 THR 567 567 567 THR THR A . n 
A 1 568 ALA 568 568 568 ALA ALA A . n 
A 1 569 ALA 569 569 569 ALA ALA A . n 
A 1 570 ASP 570 570 570 ASP ASP A . n 
A 1 571 THR 571 571 571 THR THR A . n 
A 1 572 THR 572 572 572 THR THR A . n 
A 1 573 GLY 573 573 573 GLY GLY A . n 
A 1 574 LEU 574 574 574 LEU LEU A . n 
A 1 575 GLN 575 575 575 GLN GLN A . n 
A 1 576 PRO 576 576 576 PRO PRO A . n 
A 1 577 ILE 577 577 577 ILE ILE A . n 
A 1 578 LEU 578 578 578 LEU LEU A . n 
A 1 579 ASN 579 579 579 ASN ASN A . n 
A 1 580 GLN 580 580 580 GLN GLN A . n 
A 1 581 PHE 581 581 581 PHE PHE A . n 
A 1 582 THR 582 582 582 THR THR A . n 
A 1 583 PRO 583 583 583 PRO PRO A . n 
A 1 584 ALA 584 584 584 ALA ALA A . n 
A 1 585 ASN 585 585 585 ASN ASN A . n 
A 1 586 ILE 586 586 586 ILE ILE A . n 
A 1 587 SER 587 587 587 SER SER A . n 
A 1 588 ARG 588 588 588 ARG ARG A . n 
A 1 589 GLN 589 589 589 GLN GLN A . n 
A 1 590 ALA 590 590 590 ALA ALA A . n 
A 1 591 HIS 591 591 591 HIS HIS A . n 
A 1 592 ILE 592 592 592 ILE ILE A . n 
A 1 593 LEU 593 593 593 LEU LEU A . n 
A 1 594 LEU 594 594 594 LEU LEU A . n 
A 1 595 ASP 595 595 595 ASP ASP A . n 
A 1 596 GLY 596 596 ?   ?   ?   A . n 
A 1 597 GLY 597 597 ?   ?   ?   A . n 
A 1 598 SER 598 598 ?   ?   ?   A . n 
A 1 599 LEU 599 599 ?   ?   ?   A . n 
A 1 600 GLU 600 600 ?   ?   ?   A . n 
A 1 601 VAL 601 601 ?   ?   ?   A . n 
A 1 602 LEU 602 602 ?   ?   ?   A . n 
A 1 603 PHE 603 603 ?   ?   ?   A . n 
A 1 604 GLN 604 604 ?   ?   ?   A . n 
A 1 605 GLY 605 605 ?   ?   ?   A . n 
B 2 1   GLY 1   5   5   GLY GLY B . n 
B 2 2   CYS 2   6   6   CYS CYS B . n 
B 2 3   ALA 3   7   7   ALA ALA B . n 
B 2 4   LEU 4   8   8   LEU LEU B . n 
B 2 5   GLY 5   9   9   GLY GLY B . n 
B 2 6   GLY 6   10  10  GLY GLY B . n 
B 2 7   ALA 7   11  11  ALA ALA B . n 
B 2 8   GLU 8   12  12  GLU GLU B . n 
B 2 9   THR 9   13  13  THR THR B . n 
B 2 10  CYS 10  14  14  CYS CYS B . n 
B 2 11  GLU 11  15  15  GLU GLU B . n 
B 2 12  ASP 12  16  16  ASP ASP B . n 
B 2 13  CYS 13  17  17  CYS CYS B . n 
B 2 14  LEU 14  18  18  LEU LEU B . n 
B 2 15  LEU 15  19  19  LEU LEU B . n 
B 2 16  ILE 16  20  20  ILE ILE B . n 
B 2 17  GLY 17  21  21  GLY GLY B . n 
B 2 18  PRO 18  22  22  PRO PRO B . n 
B 2 19  GLN 19  23  23  GLN GLN B . n 
B 2 20  CYS 20  24  24  CYS CYS B . n 
B 2 21  ALA 21  25  25  ALA ALA B . n 
B 2 22  TRP 22  26  26  TRP TRP B . n 
B 2 23  CYS 23  27  27  CYS CYS B . n 
B 2 24  ALA 24  28  28  ALA ALA B . n 
B 2 25  GLN 25  29  29  GLN GLN B . n 
B 2 26  GLU 26  30  30  GLU GLU B . n 
B 2 27  ASN 27  31  31  ASN ASN B . n 
B 2 28  PHE 28  32  ?   ?   ?   B . n 
B 2 29  THR 29  33  ?   ?   ?   B . n 
B 2 30  HIS 30  34  ?   ?   ?   B . n 
B 2 31  PRO 31  35  ?   ?   ?   B . n 
B 2 32  SER 32  36  ?   ?   ?   B . n 
B 2 33  GLY 33  37  ?   ?   ?   B . n 
B 2 34  VAL 34  38  ?   ?   ?   B . n 
B 2 35  GLY 35  39  39  GLY GLY B . n 
B 2 36  GLU 36  40  40  GLU GLU B . n 
B 2 37  ARG 37  41  41  ARG ARG B . n 
B 2 38  CYS 38  42  42  CYS CYS B . n 
B 2 39  ASP 39  43  43  ASP ASP B . n 
B 2 40  THR 40  44  44  THR THR B . n 
B 2 41  PRO 41  45  45  PRO PRO B . n 
B 2 42  ALA 42  46  46  ALA ALA B . n 
B 2 43  ASN 43  47  47  ASN ASN B . n 
B 2 44  LEU 44  48  48  LEU LEU B . n 
B 2 45  LEU 45  49  49  LEU LEU B . n 
B 2 46  ALA 46  50  50  ALA ALA B . n 
B 2 47  LYS 47  51  51  LYS LYS B . n 
B 2 48  GLY 48  52  52  GLY GLY B . n 
B 2 49  CYS 49  53  53  CYS CYS B . n 
B 2 50  GLN 50  54  54  GLN GLN B . n 
B 2 51  LEU 51  55  55  LEU LEU B . n 
B 2 52  ASN 52  56  56  ASN ASN B . n 
B 2 53  PHE 53  57  57  PHE PHE B . n 
B 2 54  ILE 54  58  58  ILE ILE B . n 
B 2 55  GLU 55  59  59  GLU GLU B . n 
B 2 56  ASN 56  60  60  ASN ASN B . n 
B 2 57  PRO 57  61  61  PRO PRO B . n 
B 2 58  VAL 58  62  62  VAL VAL B . n 
B 2 59  SER 59  63  63  SER SER B . n 
B 2 60  GLN 60  64  64  GLN GLN B . n 
B 2 61  VAL 61  65  65  VAL VAL B . n 
B 2 62  GLU 62  66  66  GLU GLU B . n 
B 2 63  ILE 63  67  67  ILE ILE B . n 
B 2 64  LEU 64  68  68  LEU LEU B . n 
B 2 65  LYS 65  69  69  LYS LYS B . n 
B 2 66  ASN 66  70  70  ASN ASN B . n 
B 2 67  LYS 67  71  71  LYS LYS B . n 
B 2 68  PRO 68  72  72  PRO PRO B . n 
B 2 69  LEU 69  73  73  LEU LEU B . n 
B 2 70  SER 70  74  74  SER SER B . n 
B 2 71  VAL 71  75  75  VAL VAL B . n 
B 2 72  GLY 72  76  76  GLY GLY B . n 
B 2 73  ARG 73  77  77  ARG ARG B . n 
B 2 74  GLN 74  78  78  GLN GLN B . n 
B 2 75  LYS 75  79  79  LYS LYS B . n 
B 2 76  ASN 76  80  80  ASN ASN B . n 
B 2 77  SER 77  81  81  SER SER B . n 
B 2 78  SER 78  82  82  SER SER B . n 
B 2 79  ASP 79  83  83  ASP ASP B . n 
B 2 80  ILE 80  84  84  ILE ILE B . n 
B 2 81  VAL 81  85  85  VAL VAL B . n 
B 2 82  GLN 82  86  86  GLN GLN B . n 
B 2 83  ILE 83  87  87  ILE ILE B . n 
B 2 84  ALA 84  88  88  ALA ALA B . n 
B 2 85  PRO 85  89  89  PRO PRO B . n 
B 2 86  GLN 86  90  90  GLN GLN B . n 
B 2 87  SER 87  91  91  SER SER B . n 
B 2 88  LEU 88  92  92  LEU LEU B . n 
B 2 89  ILE 89  93  93  ILE ILE B . n 
B 2 90  LEU 90  94  94  LEU LEU B . n 
B 2 91  LYS 91  95  95  LYS LYS B . n 
B 2 92  LEU 92  96  96  LEU LEU B . n 
B 2 93  ARG 93  97  97  ARG ARG B . n 
B 2 94  PRO 94  98  98  PRO PRO B . n 
B 2 95  GLY 95  99  99  GLY GLY B . n 
B 2 96  GLY 96  100 100 GLY GLY B . n 
B 2 97  ALA 97  101 101 ALA ALA B . n 
B 2 98  GLN 98  102 102 GLN GLN B . n 
B 2 99  THR 99  103 103 THR THR B . n 
B 2 100 LEU 100 104 104 LEU LEU B . n 
B 2 101 GLN 101 105 105 GLN GLN B . n 
B 2 102 VAL 102 106 106 VAL VAL B . n 
B 2 103 HIS 103 107 107 HIS HIS B . n 
B 2 104 VAL 104 108 108 VAL VAL B . n 
B 2 105 ARG 105 109 109 ARG ARG B . n 
B 2 106 GLN 106 110 110 GLN GLN B . n 
B 2 107 THR 107 111 111 THR THR B . n 
B 2 108 GLU 108 112 112 GLU GLU B . n 
B 2 109 ASP 109 113 113 ASP ASP B . n 
B 2 110 TYR 110 114 114 TYR TYR B . n 
B 2 111 PRO 111 115 115 PRO PRO B . n 
B 2 112 VAL 112 116 116 VAL VAL B . n 
B 2 113 ASP 113 117 117 ASP ASP B . n 
B 2 114 LEU 114 118 118 LEU LEU B . n 
B 2 115 TYR 115 119 119 TYR TYR B . n 
B 2 116 TYR 116 120 120 TYR TYR B . n 
B 2 117 LEU 117 121 121 LEU LEU B . n 
B 2 118 MET 118 122 122 MET MET B . n 
B 2 119 ASP 119 123 123 ASP ASP B . n 
B 2 120 LEU 120 124 124 LEU LEU B . n 
B 2 121 SER 121 125 125 SER SER B . n 
B 2 122 ALA 122 126 126 ALA ALA B . n 
B 2 123 SER 123 127 127 SER SER B . n 
B 2 124 MET 124 128 128 MET MET B . n 
B 2 125 ASP 125 129 129 ASP ASP B . n 
B 2 126 ASP 126 130 130 ASP ASP B . n 
B 2 127 ASP 127 131 131 ASP ASP B . n 
B 2 128 LEU 128 132 132 LEU LEU B . n 
B 2 129 ASN 129 133 133 ASN ASN B . n 
B 2 130 THR 130 134 134 THR THR B . n 
B 2 131 ILE 131 135 135 ILE ILE B . n 
B 2 132 LYS 132 136 136 LYS LYS B . n 
B 2 133 GLU 133 137 137 GLU GLU B . n 
B 2 134 LEU 134 138 138 LEU LEU B . n 
B 2 135 GLY 135 139 139 GLY GLY B . n 
B 2 136 SER 136 140 140 SER SER B . n 
B 2 137 ARG 137 141 141 ARG ARG B . n 
B 2 138 LEU 138 142 142 LEU LEU B . n 
B 2 139 SER 139 143 143 SER SER B . n 
B 2 140 LYS 140 144 144 LYS LYS B . n 
B 2 141 GLU 141 145 145 GLU GLU B . n 
B 2 142 MET 142 146 146 MET MET B . n 
B 2 143 SER 143 147 147 SER SER B . n 
B 2 144 LYS 144 148 148 LYS LYS B . n 
B 2 145 LEU 145 149 149 LEU LEU B . n 
B 2 146 THR 146 150 150 THR THR B . n 
B 2 147 SER 147 151 151 SER SER B . n 
B 2 148 ASN 148 152 152 ASN ASN B . n 
B 2 149 PHE 149 153 153 PHE PHE B . n 
B 2 150 ARG 150 154 154 ARG ARG B . n 
B 2 151 LEU 151 155 155 LEU LEU B . n 
B 2 152 GLY 152 156 156 GLY GLY B . n 
B 2 153 PHE 153 157 157 PHE PHE B . n 
B 2 154 GLY 154 158 158 GLY GLY B . n 
B 2 155 SER 155 159 159 SER SER B . n 
B 2 156 PHE 156 160 160 PHE PHE B . n 
B 2 157 VAL 157 161 161 VAL VAL B . n 
B 2 158 GLU 158 162 162 GLU GLU B . n 
B 2 159 LYS 159 163 163 LYS LYS B . n 
B 2 160 PRO 160 164 164 PRO PRO B . n 
B 2 161 VAL 161 165 165 VAL VAL B . n 
B 2 162 SER 162 166 166 SER SER B . n 
B 2 163 PRO 163 167 167 PRO PRO B . n 
B 2 164 PHE 164 168 168 PHE PHE B . n 
B 2 165 VAL 165 169 169 VAL VAL B . n 
B 2 166 LYS 166 170 170 LYS LYS B . n 
B 2 167 THR 167 171 171 THR THR B . n 
B 2 168 THR 168 172 172 THR THR B . n 
B 2 169 PRO 169 173 173 PRO PRO B . n 
B 2 170 GLU 170 174 174 GLU GLU B . n 
B 2 171 GLU 171 175 175 GLU GLU B . n 
B 2 172 ILE 172 176 176 ILE ILE B . n 
B 2 173 ALA 173 177 177 ALA ALA B . n 
B 2 174 ASN 174 178 178 ASN ASN B . n 
B 2 175 PRO 175 179 179 PRO PRO B . n 
B 2 176 CYS 176 180 180 CYS CYS B . n 
B 2 177 SER 177 181 181 SER SER B . n 
B 2 178 SER 178 182 182 SER SER B . n 
B 2 179 ILE 179 183 183 ILE ILE B . n 
B 2 180 PRO 180 184 184 PRO PRO B . n 
B 2 181 TYR 181 185 185 TYR TYR B . n 
B 2 182 PHE 182 186 186 PHE PHE B . n 
B 2 183 CYS 183 187 187 CYS CYS B . n 
B 2 184 LEU 184 188 188 LEU LEU B . n 
B 2 185 PRO 185 189 189 PRO PRO B . n 
B 2 186 THR 186 190 190 THR THR B . n 
B 2 187 PHE 187 191 191 PHE PHE B . n 
B 2 188 GLY 188 192 192 GLY GLY B . n 
B 2 189 PHE 189 193 193 PHE PHE B . n 
B 2 190 LYS 190 194 194 LYS LYS B . n 
B 2 191 HIS 191 195 195 HIS HIS B . n 
B 2 192 ILE 192 196 196 ILE ILE B . n 
B 2 193 LEU 193 197 197 LEU LEU B . n 
B 2 194 PRO 194 198 198 PRO PRO B . n 
B 2 195 LEU 195 199 199 LEU LEU B . n 
B 2 196 THR 196 200 200 THR THR B . n 
B 2 197 ASN 197 201 201 ASN ASN B . n 
B 2 198 ASP 198 202 202 ASP ASP B . n 
B 2 199 ALA 199 203 203 ALA ALA B . n 
B 2 200 GLU 200 204 204 GLU GLU B . n 
B 2 201 ARG 201 205 205 ARG ARG B . n 
B 2 202 PHE 202 206 206 PHE PHE B . n 
B 2 203 ASN 203 207 207 ASN ASN B . n 
B 2 204 GLU 204 208 208 GLU GLU B . n 
B 2 205 ILE 205 209 209 ILE ILE B . n 
B 2 206 VAL 206 210 210 VAL VAL B . n 
B 2 207 LYS 207 211 211 LYS LYS B . n 
B 2 208 ASN 208 212 212 ASN ASN B . n 
B 2 209 GLN 209 213 213 GLN GLN B . n 
B 2 210 LYS 210 214 214 LYS LYS B . n 
B 2 211 ILE 211 215 215 ILE ILE B . n 
B 2 212 SER 212 216 216 SER SER B . n 
B 2 213 ALA 213 217 217 ALA ALA B . n 
B 2 214 ASN 214 218 218 ASN ASN B . n 
B 2 215 ILE 215 219 219 ILE ILE B . n 
B 2 216 ASP 216 220 220 ASP ASP B . n 
B 2 217 THR 217 221 221 THR THR B . n 
B 2 218 PRO 218 222 222 PRO PRO B . n 
B 2 219 GLU 219 223 223 GLU GLU B . n 
B 2 220 GLY 220 224 224 GLY GLY B . n 
B 2 221 GLY 221 225 225 GLY GLY B . n 
B 2 222 PHE 222 226 226 PHE PHE B . n 
B 2 223 ASP 223 227 227 ASP ASP B . n 
B 2 224 ALA 224 228 228 ALA ALA B . n 
B 2 225 ILE 225 229 229 ILE ILE B . n 
B 2 226 MET 226 230 230 MET MET B . n 
B 2 227 GLN 227 231 231 GLN GLN B . n 
B 2 228 ALA 228 232 232 ALA ALA B . n 
B 2 229 ALA 229 233 233 ALA ALA B . n 
B 2 230 VAL 230 234 234 VAL VAL B . n 
B 2 231 CYS 231 235 235 CYS CYS B . n 
B 2 232 LYS 232 236 236 LYS LYS B . n 
B 2 233 GLU 233 237 237 GLU GLU B . n 
B 2 234 LYS 234 238 238 LYS LYS B . n 
B 2 235 ILE 235 239 239 ILE ILE B . n 
B 2 236 GLY 236 240 240 GLY GLY B . n 
B 2 237 TRP 237 241 241 TRP TRP B . n 
B 2 238 ARG 238 242 242 ARG ARG B . n 
B 2 239 ASN 239 243 243 ASN ASN B . n 
B 2 240 ASP 240 244 244 ASP ASP B . n 
B 2 241 SER 241 245 245 SER SER B . n 
B 2 242 LEU 242 246 246 LEU LEU B . n 
B 2 243 HIS 243 247 247 HIS HIS B . n 
B 2 244 LEU 244 248 248 LEU LEU B . n 
B 2 245 LEU 245 249 249 LEU LEU B . n 
B 2 246 VAL 246 250 250 VAL VAL B . n 
B 2 247 PHE 247 251 251 PHE PHE B . n 
B 2 248 VAL 248 252 252 VAL VAL B . n 
B 2 249 SER 249 253 253 SER SER B . n 
B 2 250 ASP 250 254 254 ASP ASP B . n 
B 2 251 ALA 251 255 255 ALA ALA B . n 
B 2 252 ASP 252 256 256 ASP ASP B . n 
B 2 253 SER 253 257 257 SER SER B . n 
B 2 254 HIS 254 258 258 HIS HIS B . n 
B 2 255 PHE 255 259 259 PHE PHE B . n 
B 2 256 GLY 256 260 260 GLY GLY B . n 
B 2 257 MET 257 261 261 MET MET B . n 
B 2 258 ASP 258 262 262 ASP ASP B . n 
B 2 259 SER 259 263 263 SER SER B . n 
B 2 260 LYS 260 264 264 LYS LYS B . n 
B 2 261 LEU 261 265 265 LEU LEU B . n 
B 2 262 ALA 262 266 266 ALA ALA B . n 
B 2 263 GLY 263 267 267 GLY GLY B . n 
B 2 264 ILE 264 268 268 ILE ILE B . n 
B 2 265 VAL 265 269 269 VAL VAL B . n 
B 2 266 CYS 266 270 270 CYS CYS B . n 
B 2 267 PRO 267 271 271 PRO PRO B . n 
B 2 268 ASN 268 272 272 ASN ASN B . n 
B 2 269 ASP 269 273 273 ASP ASP B . n 
B 2 270 GLY 270 274 274 GLY GLY B . n 
B 2 271 LEU 271 275 275 LEU LEU B . n 
B 2 272 CYS 272 276 276 CYS CYS B . n 
B 2 273 HIS 273 277 277 HIS HIS B . n 
B 2 274 LEU 274 278 278 LEU LEU B . n 
B 2 275 ASP 275 279 279 ASP ASP B . n 
B 2 276 SER 276 280 280 SER SER B . n 
B 2 277 LYS 277 281 281 LYS LYS B . n 
B 2 278 ASN 278 282 282 ASN ASN B . n 
B 2 279 GLU 279 283 283 GLU GLU B . n 
B 2 280 TYR 280 284 284 TYR TYR B . n 
B 2 281 SER 281 285 285 SER SER B . n 
B 2 282 MET 282 286 286 MET MET B . n 
B 2 283 SER 283 287 287 SER SER B . n 
B 2 284 THR 284 288 288 THR THR B . n 
B 2 285 VAL 285 289 289 VAL VAL B . n 
B 2 286 LEU 286 290 290 LEU LEU B . n 
B 2 287 GLU 287 291 291 GLU GLU B . n 
B 2 288 TYR 288 292 292 TYR TYR B . n 
B 2 289 PRO 289 293 293 PRO PRO B . n 
B 2 290 THR 290 294 294 THR THR B . n 
B 2 291 ILE 291 295 295 ILE ILE B . n 
B 2 292 GLY 292 296 296 GLY GLY B . n 
B 2 293 GLN 293 297 297 GLN GLN B . n 
B 2 294 LEU 294 298 298 LEU LEU B . n 
B 2 295 ILE 295 299 299 ILE ILE B . n 
B 2 296 ASP 296 300 300 ASP ASP B . n 
B 2 297 LYS 297 301 301 LYS LYS B . n 
B 2 298 LEU 298 302 302 LEU LEU B . n 
B 2 299 VAL 299 303 303 VAL VAL B . n 
B 2 300 GLN 300 304 304 GLN GLN B . n 
B 2 301 ASN 301 305 305 ASN ASN B . n 
B 2 302 ASN 302 306 306 ASN ASN B . n 
B 2 303 VAL 303 307 307 VAL VAL B . n 
B 2 304 LEU 304 308 308 LEU LEU B . n 
B 2 305 LEU 305 309 309 LEU LEU B . n 
B 2 306 ILE 306 310 310 ILE ILE B . n 
B 2 307 PHE 307 311 311 PHE PHE B . n 
B 2 308 ALA 308 312 312 ALA ALA B . n 
B 2 309 VAL 309 313 313 VAL VAL B . n 
B 2 310 THR 310 314 314 THR THR B . n 
B 2 311 GLN 311 315 315 GLN GLN B . n 
B 2 312 GLU 312 316 316 GLU GLU B . n 
B 2 313 GLN 313 317 317 GLN GLN B . n 
B 2 314 VAL 314 318 318 VAL VAL B . n 
B 2 315 HIS 315 319 319 HIS HIS B . n 
B 2 316 LEU 316 320 320 LEU LEU B . n 
B 2 317 TYR 317 321 321 TYR TYR B . n 
B 2 318 GLU 318 322 322 GLU GLU B . n 
B 2 319 ASN 319 323 323 ASN ASN B . n 
B 2 320 TYR 320 324 324 TYR TYR B . n 
B 2 321 ALA 321 325 325 ALA ALA B . n 
B 2 322 LYS 322 326 326 LYS LYS B . n 
B 2 323 LEU 323 327 327 LEU LEU B . n 
B 2 324 ILE 324 328 328 ILE ILE B . n 
B 2 325 PRO 325 329 329 PRO PRO B . n 
B 2 326 GLY 326 330 330 GLY GLY B . n 
B 2 327 ALA 327 331 331 ALA ALA B . n 
B 2 328 THR 328 332 332 THR THR B . n 
B 2 329 VAL 329 333 333 VAL VAL B . n 
B 2 330 GLY 330 334 334 GLY GLY B . n 
B 2 331 LEU 331 335 335 LEU LEU B . n 
B 2 332 LEU 332 336 336 LEU LEU B . n 
B 2 333 GLN 333 337 337 GLN GLN B . n 
B 2 334 LYS 334 338 338 LYS LYS B . n 
B 2 335 ASP 335 339 339 ASP ASP B . n 
B 2 336 SER 336 340 340 SER SER B . n 
B 2 337 GLY 337 341 341 GLY GLY B . n 
B 2 338 ASN 338 342 342 ASN ASN B . n 
B 2 339 ILE 339 343 343 ILE ILE B . n 
B 2 340 LEU 340 344 344 LEU LEU B . n 
B 2 341 GLN 341 345 345 GLN GLN B . n 
B 2 342 LEU 342 346 346 LEU LEU B . n 
B 2 343 ILE 343 347 347 ILE ILE B . n 
B 2 344 ILE 344 348 348 ILE ILE B . n 
B 2 345 SER 345 349 349 SER SER B . n 
B 2 346 ALA 346 350 350 ALA ALA B . n 
B 2 347 TYR 347 351 351 TYR TYR B . n 
B 2 348 GLU 348 352 352 GLU GLU B . n 
B 2 349 GLU 349 353 353 GLU GLU B . n 
B 2 350 LEU 350 354 354 LEU LEU B . n 
B 2 351 ARG 351 355 355 ARG ARG B . n 
B 2 352 SER 352 356 356 SER SER B . n 
B 2 353 GLU 353 357 357 GLU GLU B . n 
B 2 354 VAL 354 358 358 VAL VAL B . n 
B 2 355 GLU 355 359 359 GLU GLU B . n 
B 2 356 LEU 356 360 360 LEU LEU B . n 
B 2 357 GLU 357 361 361 GLU GLU B . n 
B 2 358 VAL 358 362 362 VAL VAL B . n 
B 2 359 LEU 359 363 363 LEU LEU B . n 
B 2 360 GLY 360 364 364 GLY GLY B . n 
B 2 361 ASP 361 365 365 ASP ASP B . n 
B 2 362 THR 362 366 366 THR THR B . n 
B 2 363 GLU 363 367 367 GLU GLU B . n 
B 2 364 GLY 364 368 368 GLY GLY B . n 
B 2 365 LEU 365 369 369 LEU LEU B . n 
B 2 366 ASN 366 370 370 ASN ASN B . n 
B 2 367 LEU 367 371 371 LEU LEU B . n 
B 2 368 SER 368 372 372 SER SER B . n 
B 2 369 PHE 369 373 373 PHE PHE B . n 
B 2 370 THR 370 374 374 THR THR B . n 
B 2 371 ALA 371 375 375 ALA ALA B . n 
B 2 372 ILE 372 376 376 ILE ILE B . n 
B 2 373 CYS 373 377 377 CYS CYS B . n 
B 2 374 ASN 374 378 378 ASN ASN B . n 
B 2 375 ASN 375 379 379 ASN ASN B . n 
B 2 376 GLY 376 380 380 GLY GLY B . n 
B 2 377 THR 377 381 381 THR THR B . n 
B 2 378 LEU 378 382 382 LEU LEU B . n 
B 2 379 PHE 379 383 383 PHE PHE B . n 
B 2 380 GLN 380 384 384 GLN GLN B . n 
B 2 381 HIS 381 385 385 HIS HIS B . n 
B 2 382 GLN 382 386 386 GLN GLN B . n 
B 2 383 LYS 383 387 387 LYS LYS B . n 
B 2 384 LYS 384 388 388 LYS LYS B . n 
B 2 385 CYS 385 389 389 CYS CYS B . n 
B 2 386 SER 386 390 390 SER SER B . n 
B 2 387 HIS 387 391 391 HIS HIS B . n 
B 2 388 MET 388 392 392 MET MET B . n 
B 2 389 LYS 389 393 393 LYS LYS B . n 
B 2 390 VAL 390 394 394 VAL VAL B . n 
B 2 391 GLY 391 395 395 GLY GLY B . n 
B 2 392 ASP 392 396 396 ASP ASP B . n 
B 2 393 THR 393 397 397 THR THR B . n 
B 2 394 ALA 394 398 398 ALA ALA B . n 
B 2 395 SER 395 399 399 SER SER B . n 
B 2 396 PHE 396 400 400 PHE PHE B . n 
B 2 397 SER 397 401 401 SER SER B . n 
B 2 398 VAL 398 402 402 VAL VAL B . n 
B 2 399 THR 399 403 403 THR THR B . n 
B 2 400 VAL 400 404 404 VAL VAL B . n 
B 2 401 ASN 401 405 405 ASN ASN B . n 
B 2 402 ILE 402 406 406 ILE ILE B . n 
B 2 403 PRO 403 407 407 PRO PRO B . n 
B 2 404 HIS 404 408 408 HIS HIS B . n 
B 2 405 CYS 405 409 409 CYS CYS B . n 
B 2 406 GLU 406 410 410 GLU GLU B . n 
B 2 407 ARG 407 411 411 ARG ARG B . n 
B 2 408 ARG 408 412 412 ARG ARG B . n 
B 2 409 SER 409 413 413 SER SER B . n 
B 2 410 ARG 410 414 414 ARG ARG B . n 
B 2 411 HIS 411 415 415 HIS HIS B . n 
B 2 412 ILE 412 416 416 ILE ILE B . n 
B 2 413 ILE 413 417 417 ILE ILE B . n 
B 2 414 ILE 414 418 418 ILE ILE B . n 
B 2 415 LYS 415 419 419 LYS LYS B . n 
B 2 416 PRO 416 420 420 PRO PRO B . n 
B 2 417 VAL 417 421 421 VAL VAL B . n 
B 2 418 GLY 418 422 422 GLY GLY B . n 
B 2 419 LEU 419 423 423 LEU LEU B . n 
B 2 420 GLY 420 424 424 GLY GLY B . n 
B 2 421 ASP 421 425 425 ASP ASP B . n 
B 2 422 ALA 422 426 426 ALA ALA B . n 
B 2 423 LEU 423 427 427 LEU LEU B . n 
B 2 424 GLU 424 428 428 GLU GLU B . n 
B 2 425 LEU 425 429 429 LEU LEU B . n 
B 2 426 LEU 426 430 430 LEU LEU B . n 
B 2 427 VAL 427 431 431 VAL VAL B . n 
B 2 428 SER 428 432 432 SER SER B . n 
B 2 429 PRO 429 433 433 PRO PRO B . n 
B 2 430 GLU 430 434 434 GLU GLU B . n 
B 2 431 CYS 431 435 435 CYS CYS B . n 
B 2 432 ASN 432 436 436 ASN ASN B . n 
B 2 433 CYS 433 437 437 CYS CYS B . n 
B 2 434 ASP 434 438 438 ASP ASP B . n 
B 2 435 CYS 435 439 439 CYS CYS B . n 
B 2 436 GLN 436 440 440 GLN GLN B . n 
B 2 437 LYS 437 441 441 LYS LYS B . n 
B 2 438 GLU 438 442 442 GLU GLU B . n 
B 2 439 VAL 439 443 443 VAL VAL B . n 
B 2 440 GLU 440 444 444 GLU GLU B . n 
B 2 441 VAL 441 445 445 VAL VAL B . n 
B 2 442 ASN 442 446 446 ASN ASN B . n 
B 2 443 SER 443 447 447 SER SER B . n 
B 2 444 SER 444 448 448 SER SER B . n 
B 2 445 LYS 445 449 449 LYS LYS B . n 
B 2 446 CYS 446 450 450 CYS CYS B . n 
B 2 447 HIS 447 451 451 HIS HIS B . n 
B 2 448 HIS 448 452 452 HIS HIS B . n 
B 2 449 GLY 449 453 453 GLY GLY B . n 
B 2 450 ASN 450 454 454 ASN ASN B . n 
B 2 451 GLY 451 455 455 GLY GLY B . n 
B 2 452 SER 452 456 456 SER SER B . n 
B 2 453 PHE 453 457 457 PHE PHE B . n 
B 2 454 GLN 454 458 458 GLN GLN B . n 
B 2 455 CYS 455 459 459 CYS CYS B . n 
B 2 456 GLY 456 460 460 GLY GLY B . n 
B 2 457 VAL 457 461 461 VAL VAL B . n 
B 2 458 CYS 458 462 462 CYS CYS B . n 
B 2 459 ALA 459 463 463 ALA ALA B . n 
B 2 460 CYS 460 464 464 CYS CYS B . n 
B 2 461 HIS 461 465 465 HIS HIS B . n 
B 2 462 PRO 462 466 466 PRO PRO B . n 
B 2 463 GLY 463 467 467 GLY GLY B . n 
B 2 464 HIS 464 468 468 HIS HIS B . n 
B 2 465 MET 465 469 469 MET MET B . n 
B 2 466 GLY 466 470 470 GLY GLY B . n 
B 2 467 PRO 467 471 471 PRO PRO B . n 
B 2 468 ARG 468 472 472 ARG ARG B . n 
B 2 469 CYS 469 473 473 CYS CYS B . n 
B 2 470 GLU 470 474 474 GLU GLU B . n 
B 2 471 SER 471 475 475 SER SER B . n 
B 2 472 GLY 472 476 476 GLY GLY B . n 
B 2 473 HIS 473 477 477 HIS HIS B . n 
B 2 474 SER 474 478 ?   ?   ?   B . n 
B 2 475 LEU 475 479 ?   ?   ?   B . n 
B 2 476 GLU 476 480 ?   ?   ?   B . n 
B 2 477 VAL 477 481 ?   ?   ?   B . n 
B 2 478 LEU 478 482 ?   ?   ?   B . n 
B 2 479 PHE 479 483 ?   ?   ?   B . n 
B 2 480 GLN 480 484 ?   ?   ?   B . n 
B 2 481 GLY 481 485 ?   ?   ?   B . n 
C 3 1   ASP 1   1   1   ASP ASP C . n 
C 3 2   ILE 2   2   2   ILE ILE C . n 
C 3 3   GLN 3   3   3   GLN GLN C . n 
C 3 4   MET 4   4   4   MET MET C . n 
C 3 5   THR 5   5   5   THR THR C . n 
C 3 6   GLN 6   6   6   GLN GLN C . n 
C 3 7   THR 7   7   7   THR THR C . n 
C 3 8   THR 8   8   8   THR THR C . n 
C 3 9   SER 9   9   9   SER SER C . n 
C 3 10  SER 10  10  10  SER SER C . n 
C 3 11  LEU 11  11  11  LEU LEU C . n 
C 3 12  SER 12  12  12  SER SER C . n 
C 3 13  ALA 13  13  13  ALA ALA C . n 
C 3 14  SER 14  14  14  SER SER C . n 
C 3 15  LEU 15  15  15  LEU LEU C . n 
C 3 16  GLY 16  16  16  GLY GLY C . n 
C 3 17  ASP 17  17  17  ASP ASP C . n 
C 3 18  ARG 18  18  18  ARG ARG C . n 
C 3 19  VAL 19  19  19  VAL VAL C . n 
C 3 20  ILE 20  20  20  ILE ILE C . n 
C 3 21  ILE 21  21  21  ILE ILE C . n 
C 3 22  SER 22  22  22  SER SER C . n 
C 3 23  CYS 23  23  23  CYS CYS C . n 
C 3 24  ARG 24  24  24  ARG ARG C . n 
C 3 25  ALA 25  25  25  ALA ALA C . n 
C 3 26  SER 26  26  26  SER SER C . n 
C 3 27  GLN 27  27  27  GLN GLN C . n 
C 3 28  ASP 28  28  28  ASP ASP C . n 
C 3 29  ILE 29  29  29  ILE ILE C . n 
C 3 30  SER 30  30  30  SER SER C . n 
C 3 31  ASN 31  31  31  ASN ASN C . n 
C 3 32  TYR 32  32  32  TYR TYR C . n 
C 3 33  LEU 33  33  33  LEU LEU C . n 
C 3 34  SER 34  34  34  SER SER C . n 
C 3 35  TRP 35  35  35  TRP TRP C . n 
C 3 36  TYR 36  36  36  TYR TYR C . n 
C 3 37  GLN 37  37  37  GLN GLN C . n 
C 3 38  GLN 38  38  38  GLN GLN C . n 
C 3 39  LYS 39  39  39  LYS LYS C . n 
C 3 40  PRO 40  40  40  PRO PRO C . n 
C 3 41  ASP 41  41  41  ASP ASP C . n 
C 3 42  GLY 42  42  42  GLY GLY C . n 
C 3 43  THR 43  43  43  THR THR C . n 
C 3 44  VAL 44  44  44  VAL VAL C . n 
C 3 45  LYS 45  45  45  LYS LYS C . n 
C 3 46  LEU 46  46  46  LEU LEU C . n 
C 3 47  LEU 47  47  47  LEU LEU C . n 
C 3 48  ILE 48  48  48  ILE ILE C . n 
C 3 49  PHE 49  49  49  PHE PHE C . n 
C 3 50  TYR 50  50  50  TYR TYR C . n 
C 3 51  THR 51  51  51  THR THR C . n 
C 3 52  SER 52  52  52  SER SER C . n 
C 3 53  LYS 53  53  53  LYS LYS C . n 
C 3 54  LEU 54  54  54  LEU LEU C . n 
C 3 55  HIS 55  55  55  HIS HIS C . n 
C 3 56  SER 56  56  56  SER SER C . n 
C 3 57  GLY 57  57  57  GLY GLY C . n 
C 3 58  VAL 58  58  58  VAL VAL C . n 
C 3 59  PRO 59  59  59  PRO PRO C . n 
C 3 60  SER 60  60  60  SER SER C . n 
C 3 61  ARG 61  61  61  ARG ARG C . n 
C 3 62  PHE 62  62  62  PHE PHE C . n 
C 3 63  SER 63  63  63  SER SER C . n 
C 3 64  GLY 64  64  64  GLY GLY C . n 
C 3 65  SER 65  65  65  SER SER C . n 
C 3 66  GLY 66  66  66  GLY GLY C . n 
C 3 67  SER 67  67  67  SER SER C . n 
C 3 68  GLY 68  68  68  GLY GLY C . n 
C 3 69  THR 69  69  69  THR THR C . n 
C 3 70  ASP 70  70  70  ASP ASP C . n 
C 3 71  TYR 71  71  71  TYR TYR C . n 
C 3 72  SER 72  72  72  SER SER C . n 
C 3 73  LEU 73  73  73  LEU LEU C . n 
C 3 74  THR 74  74  74  THR THR C . n 
C 3 75  ILE 75  75  75  ILE ILE C . n 
C 3 76  SER 76  76  76  SER SER C . n 
C 3 77  ASN 77  77  77  ASN ASN C . n 
C 3 78  LEU 78  78  78  LEU LEU C . n 
C 3 79  ASP 79  79  79  ASP ASP C . n 
C 3 80  GLN 80  80  80  GLN GLN C . n 
C 3 81  GLU 81  81  81  GLU GLU C . n 
C 3 82  ASP 82  82  82  ASP ASP C . n 
C 3 83  ILE 83  83  83  ILE ILE C . n 
C 3 84  ALA 84  84  84  ALA ALA C . n 
C 3 85  THR 85  85  85  THR THR C . n 
C 3 86  TYR 86  86  86  TYR TYR C . n 
C 3 87  PHE 87  87  87  PHE PHE C . n 
C 3 88  CYS 88  88  88  CYS CYS C . n 
C 3 89  GLN 89  89  89  GLN GLN C . n 
C 3 90  GLN 90  90  90  GLN GLN C . n 
C 3 91  GLY 91  91  91  GLY GLY C . n 
C 3 92  ASN 92  92  92  ASN ASN C . n 
C 3 93  THR 93  93  93  THR THR C . n 
C 3 94  PHE 94  94  94  PHE PHE C . n 
C 3 95  PRO 95  95  95  PRO PRO C . n 
C 3 96  TYR 96  96  96  TYR TYR C . n 
C 3 97  THR 97  97  97  THR THR C . n 
C 3 98  PHE 98  98  98  PHE PHE C . n 
C 3 99  GLY 99  99  99  GLY GLY C . n 
C 3 100 GLY 100 100 100 GLY GLY C . n 
C 3 101 GLY 101 101 101 GLY GLY C . n 
C 3 102 THR 102 102 102 THR THR C . n 
C 3 103 LYS 103 103 103 LYS LYS C . n 
C 3 104 VAL 104 104 104 VAL VAL C . n 
C 3 105 GLU 105 105 105 GLU GLU C . n 
C 3 106 MET 106 106 106 MET MET C . n 
C 3 107 ARG 107 107 107 ARG ARG C . n 
C 3 108 ARG 108 108 108 ARG ARG C . n 
C 3 109 ALA 109 109 109 ALA ALA C . n 
C 3 110 ASP 110 110 110 ASP ASP C . n 
C 3 111 ALA 111 111 111 ALA ALA C . n 
C 3 112 ALA 112 112 112 ALA ALA C . n 
C 3 113 PRO 113 113 113 PRO PRO C . n 
C 3 114 THR 114 114 114 THR THR C . n 
C 3 115 VAL 115 115 115 VAL VAL C . n 
C 3 116 SER 116 116 116 SER SER C . n 
C 3 117 ILE 117 117 117 ILE ILE C . n 
C 3 118 PHE 118 118 118 PHE PHE C . n 
C 3 119 PRO 119 119 119 PRO PRO C . n 
C 3 120 PRO 120 120 120 PRO PRO C . n 
C 3 121 SER 121 121 121 SER SER C . n 
C 3 122 SER 122 122 122 SER SER C . n 
C 3 123 GLU 123 123 123 GLU GLU C . n 
C 3 124 GLN 124 124 124 GLN GLN C . n 
C 3 125 LEU 125 125 125 LEU LEU C . n 
C 3 126 THR 126 126 126 THR THR C . n 
C 3 127 SER 127 127 127 SER SER C . n 
C 3 128 GLY 128 128 128 GLY GLY C . n 
C 3 129 GLY 129 129 129 GLY GLY C . n 
C 3 130 ALA 130 130 130 ALA ALA C . n 
C 3 131 SER 131 131 131 SER SER C . n 
C 3 132 VAL 132 132 132 VAL VAL C . n 
C 3 133 VAL 133 133 133 VAL VAL C . n 
C 3 134 CYS 134 134 134 CYS CYS C . n 
C 3 135 PHE 135 135 135 PHE PHE C . n 
C 3 136 LEU 136 136 136 LEU LEU C . n 
C 3 137 ASN 137 137 137 ASN ASN C . n 
C 3 138 ASN 138 138 138 ASN ASN C . n 
C 3 139 PHE 139 139 139 PHE PHE C . n 
C 3 140 TYR 140 140 140 TYR TYR C . n 
C 3 141 PRO 141 141 141 PRO PRO C . n 
C 3 142 LYS 142 142 142 LYS LYS C . n 
C 3 143 ASP 143 143 143 ASP ASP C . n 
C 3 144 ILE 144 144 144 ILE ILE C . n 
C 3 145 ASN 145 145 145 ASN ASN C . n 
C 3 146 VAL 146 146 146 VAL VAL C . n 
C 3 147 LYS 147 147 147 LYS LYS C . n 
C 3 148 TRP 148 148 148 TRP TRP C . n 
C 3 149 LYS 149 149 149 LYS LYS C . n 
C 3 150 ILE 150 150 150 ILE ILE C . n 
C 3 151 ASP 151 151 151 ASP ASP C . n 
C 3 152 GLY 152 152 152 GLY GLY C . n 
C 3 153 SER 153 153 153 SER SER C . n 
C 3 154 GLU 154 154 154 GLU GLU C . n 
C 3 155 ARG 155 155 155 ARG ARG C . n 
C 3 156 GLN 156 156 156 GLN GLN C . n 
C 3 157 ASN 157 157 157 ASN ASN C . n 
C 3 158 GLY 158 158 158 GLY GLY C . n 
C 3 159 VAL 159 159 159 VAL VAL C . n 
C 3 160 LEU 160 160 160 LEU LEU C . n 
C 3 161 ASN 161 161 161 ASN ASN C . n 
C 3 162 SER 162 162 162 SER SER C . n 
C 3 163 TRP 163 163 163 TRP TRP C . n 
C 3 164 THR 164 164 164 THR THR C . n 
C 3 165 ASP 165 165 165 ASP ASP C . n 
C 3 166 GLN 166 166 166 GLN GLN C . n 
C 3 167 ASP 167 167 167 ASP ASP C . n 
C 3 168 SER 168 168 168 SER SER C . n 
C 3 169 LYS 169 169 169 LYS LYS C . n 
C 3 170 ASP 170 170 170 ASP ASP C . n 
C 3 171 SER 171 171 171 SER SER C . n 
C 3 172 THR 172 172 172 THR THR C . n 
C 3 173 TYR 173 173 173 TYR TYR C . n 
C 3 174 SER 174 174 174 SER SER C . n 
C 3 175 PHE 175 175 175 PHE PHE C . n 
C 3 176 SER 176 176 176 SER SER C . n 
C 3 177 SER 177 177 177 SER SER C . n 
C 3 178 THR 178 178 178 THR THR C . n 
C 3 179 LEU 179 179 179 LEU LEU C . n 
C 3 180 THR 180 180 180 THR THR C . n 
C 3 181 LEU 181 181 181 LEU LEU C . n 
C 3 182 THR 182 182 182 THR THR C . n 
C 3 183 LYS 183 183 183 LYS LYS C . n 
C 3 184 ASP 184 184 184 ASP ASP C . n 
C 3 185 GLU 185 185 185 GLU GLU C . n 
C 3 186 TYR 186 186 186 TYR TYR C . n 
C 3 187 GLU 187 187 187 GLU GLU C . n 
C 3 188 ARG 188 188 188 ARG ARG C . n 
C 3 189 HIS 189 189 189 HIS HIS C . n 
C 3 190 ASN 190 190 190 ASN ASN C . n 
C 3 191 SER 191 191 191 SER SER C . n 
C 3 192 TYR 192 192 192 TYR TYR C . n 
C 3 193 THR 193 193 193 THR THR C . n 
C 3 194 CYS 194 194 194 CYS CYS C . n 
C 3 195 GLU 195 195 195 GLU GLU C . n 
C 3 196 ALA 196 196 196 ALA ALA C . n 
C 3 197 THR 197 197 197 THR THR C . n 
C 3 198 HIS 198 198 198 HIS HIS C . n 
C 3 199 LYS 199 199 199 LYS LYS C . n 
C 3 200 THR 200 200 200 THR THR C . n 
C 3 201 SER 201 201 201 SER SER C . n 
C 3 202 THR 202 202 202 THR THR C . n 
C 3 203 SER 203 203 203 SER SER C . n 
C 3 204 PRO 204 204 204 PRO PRO C . n 
C 3 205 ILE 205 205 205 ILE ILE C . n 
C 3 206 VAL 206 206 206 VAL VAL C . n 
C 3 207 LYS 207 207 207 LYS LYS C . n 
C 3 208 SER 208 208 208 SER SER C . n 
C 3 209 PHE 209 209 209 PHE PHE C . n 
C 3 210 ASN 210 210 210 ASN ASN C . n 
C 3 211 ARG 211 211 211 ARG ARG C . n 
C 3 212 ASN 212 212 212 ASN ASN C . n 
C 3 213 GLU 213 213 213 GLU GLU C . n 
C 3 214 CYS 214 214 214 CYS CYS C . n 
D 4 1   GLN 1   1   1   GLN GLN D . n 
D 4 2   VAL 2   2   2   VAL VAL D . n 
D 4 3   GLN 3   3   3   GLN GLN D . n 
D 4 4   LEU 4   4   4   LEU LEU D . n 
D 4 5   GLN 5   5   5   GLN GLN D . n 
D 4 6   GLN 6   6   6   GLN GLN D . n 
D 4 7   SER 7   7   7   SER SER D . n 
D 4 8   GLY 8   8   8   GLY GLY D . n 
D 4 9   ALA 9   9   9   ALA ALA D . n 
D 4 10  GLU 10  10  10  GLU GLU D . n 
D 4 11  LEU 11  11  11  LEU LEU D . n 
D 4 12  ALA 12  12  12  ALA ALA D . n 
D 4 13  GLU 13  13  13  GLU GLU D . n 
D 4 14  PRO 14  14  14  PRO PRO D . n 
D 4 15  GLY 15  15  15  GLY GLY D . n 
D 4 16  ALA 16  16  16  ALA ALA D . n 
D 4 17  SER 17  17  17  SER SER D . n 
D 4 18  VAL 18  18  18  VAL VAL D . n 
D 4 19  LYS 19  19  19  LYS LYS D . n 
D 4 20  MET 20  20  20  MET MET D . n 
D 4 21  SER 21  21  21  SER SER D . n 
D 4 22  CYS 22  22  22  CYS CYS D . n 
D 4 23  LYS 23  23  23  LYS LYS D . n 
D 4 24  ALA 24  24  24  ALA ALA D . n 
D 4 25  SER 25  25  25  SER SER D . n 
D 4 26  GLY 26  26  26  GLY GLY D . n 
D 4 27  TYR 27  27  27  TYR TYR D . n 
D 4 28  THR 28  28  28  THR THR D . n 
D 4 29  PHE 29  29  29  PHE PHE D . n 
D 4 30  SER 30  30  30  SER SER D . n 
D 4 31  SER 31  31  31  SER SER D . n 
D 4 32  PHE 32  32  32  PHE PHE D . n 
D 4 33  TRP 33  33  33  TRP TRP D . n 
D 4 34  MET 34  34  34  MET MET D . n 
D 4 35  HIS 35  35  35  HIS HIS D . n 
D 4 36  TRP 36  36  36  TRP TRP D . n 
D 4 37  VAL 37  37  37  VAL VAL D . n 
D 4 38  LYS 38  38  38  LYS LYS D . n 
D 4 39  GLN 39  39  39  GLN GLN D . n 
D 4 40  ARG 40  40  40  ARG ARG D . n 
D 4 41  PRO 41  41  41  PRO PRO D . n 
D 4 42  GLY 42  42  42  GLY GLY D . n 
D 4 43  GLN 43  43  43  GLN GLN D . n 
D 4 44  GLY 44  44  44  GLY GLY D . n 
D 4 45  LEU 45  45  45  LEU LEU D . n 
D 4 46  GLU 46  46  46  GLU GLU D . n 
D 4 47  TRP 47  47  47  TRP TRP D . n 
D 4 48  ILE 48  48  48  ILE ILE D . n 
D 4 49  GLY 49  49  49  GLY GLY D . n 
D 4 50  TYR 50  50  50  TYR TYR D . n 
D 4 51  ILE 51  51  51  ILE ILE D . n 
D 4 52  ASN 52  52  52  ASN ASN D . n 
D 4 53  PRO 53  53  53  PRO PRO D . n 
D 4 54  ASN 54  54  54  ASN ASN D . n 
D 4 55  SER 55  55  55  SER SER D . n 
D 4 56  GLY 56  56  56  GLY GLY D . n 
D 4 57  TYR 57  57  57  TYR TYR D . n 
D 4 58  THR 58  58  58  THR THR D . n 
D 4 59  GLU 59  59  59  GLU GLU D . n 
D 4 60  CYS 60  60  60  CYS CYS D . n 
D 4 61  ASN 61  61  61  ASN ASN D . n 
D 4 62  GLU 62  62  62  GLU GLU D . n 
D 4 63  ILE 63  63  63  ILE ILE D . n 
D 4 64  PHE 64  64  64  PHE PHE D . n 
D 4 65  ARG 65  65  65  ARG ARG D . n 
D 4 66  ASP 66  66  66  ASP ASP D . n 
D 4 67  LYS 67  67  67  LYS LYS D . n 
D 4 68  ALA 68  68  68  ALA ALA D . n 
D 4 69  THR 69  69  69  THR THR D . n 
D 4 70  MET 70  70  70  MET MET D . n 
D 4 71  THR 71  71  71  THR THR D . n 
D 4 72  ALA 72  72  72  ALA ALA D . n 
D 4 73  ASP 73  73  73  ASP ASP D . n 
D 4 74  THR 74  74  74  THR THR D . n 
D 4 75  SER 75  75  75  SER SER D . n 
D 4 76  SER 76  76  76  SER SER D . n 
D 4 77  SER 77  77  77  SER SER D . n 
D 4 78  THR 78  78  78  THR THR D . n 
D 4 79  ALA 79  79  79  ALA ALA D . n 
D 4 80  TYR 80  80  80  TYR TYR D . n 
D 4 81  MET 81  81  81  MET MET D . n 
D 4 82  GLN 82  82  82  GLN GLN D . n 
D 4 83  LEU 83  83  83  LEU LEU D . n 
D 4 84  SER 84  84  84  SER SER D . n 
D 4 85  GLY 85  85  85  GLY GLY D . n 
D 4 86  LEU 86  86  86  LEU LEU D . n 
D 4 87  THR 87  87  87  THR THR D . n 
D 4 88  SER 88  88  88  SER SER D . n 
D 4 89  GLU 89  89  89  GLU GLU D . n 
D 4 90  ASP 90  90  90  ASP ASP D . n 
D 4 91  SER 91  91  91  SER SER D . n 
D 4 92  ALA 92  92  92  ALA ALA D . n 
D 4 93  VAL 93  93  93  VAL VAL D . n 
D 4 94  TYR 94  94  94  TYR TYR D . n 
D 4 95  TYR 95  95  95  TYR TYR D . n 
D 4 96  CYS 96  96  96  CYS CYS D . n 
D 4 97  ALA 97  97  97  ALA ALA D . n 
D 4 98  SER 98  98  98  SER SER D . n 
D 4 99  PHE 99  99  99  PHE PHE D . n 
D 4 100 LEU 100 100 100 LEU LEU D . n 
D 4 101 GLY 101 101 101 GLY GLY D . n 
D 4 102 ARG 102 102 102 ARG ARG D . n 
D 4 103 GLY 103 103 103 GLY GLY D . n 
D 4 104 ALA 104 104 104 ALA ALA D . n 
D 4 105 MET 105 105 105 MET MET D . n 
D 4 106 ASP 106 106 106 ASP ASP D . n 
D 4 107 TYR 107 107 107 TYR TYR D . n 
D 4 108 TRP 108 108 108 TRP TRP D . n 
D 4 109 GLY 109 109 109 GLY GLY D . n 
D 4 110 GLN 110 110 110 GLN GLN D . n 
D 4 111 GLY 111 111 111 GLY GLY D . n 
D 4 112 THR 112 112 112 THR THR D . n 
D 4 113 SER 113 113 113 SER SER D . n 
D 4 114 VAL 114 114 114 VAL VAL D . n 
D 4 115 THR 115 115 115 THR THR D . n 
D 4 116 VAL 116 116 116 VAL VAL D . n 
D 4 117 SER 117 117 117 SER SER D . n 
D 4 118 SER 118 118 118 SER SER D . n 
D 4 119 ALA 119 119 119 ALA ALA D . n 
D 4 120 LYS 120 120 120 LYS LYS D . n 
D 4 121 THR 121 121 121 THR THR D . n 
D 4 122 THR 122 122 122 THR THR D . n 
D 4 123 ALA 123 123 123 ALA ALA D . n 
D 4 124 PRO 124 124 124 PRO PRO D . n 
D 4 125 SER 125 125 125 SER SER D . n 
D 4 126 VAL 126 126 126 VAL VAL D . n 
D 4 127 TYR 127 127 127 TYR TYR D . n 
D 4 128 PRO 128 128 128 PRO PRO D . n 
D 4 129 LEU 129 129 129 LEU LEU D . n 
D 4 130 ALA 130 130 130 ALA ALA D . n 
D 4 131 PRO 131 131 131 PRO PRO D . n 
D 4 132 VAL 132 132 132 VAL VAL D . n 
D 4 133 CYS 133 133 133 CYS CYS D . n 
D 4 134 GLY 134 134 ?   ?   ?   D . n 
D 4 135 ASP 135 135 ?   ?   ?   D . n 
D 4 136 THR 136 136 ?   ?   ?   D . n 
D 4 137 THR 137 137 ?   ?   ?   D . n 
D 4 138 GLY 138 138 138 GLY GLY D . n 
D 4 139 SER 139 139 139 SER SER D . n 
D 4 140 SER 140 140 140 SER SER D . n 
D 4 141 VAL 141 141 141 VAL VAL D . n 
D 4 142 THR 142 142 142 THR THR D . n 
D 4 143 LEU 143 143 143 LEU LEU D . n 
D 4 144 GLY 144 144 144 GLY GLY D . n 
D 4 145 CYS 145 145 145 CYS CYS D . n 
D 4 146 LEU 146 146 146 LEU LEU D . n 
D 4 147 VAL 147 147 147 VAL VAL D . n 
D 4 148 LYS 148 148 148 LYS LYS D . n 
D 4 149 GLY 149 149 149 GLY GLY D . n 
D 4 150 TYR 150 150 150 TYR TYR D . n 
D 4 151 PHE 151 151 151 PHE PHE D . n 
D 4 152 PRO 152 152 152 PRO PRO D . n 
D 4 153 GLU 153 153 153 GLU GLU D . n 
D 4 154 PRO 154 154 154 PRO PRO D . n 
D 4 155 VAL 155 155 155 VAL VAL D . n 
D 4 156 THR 156 156 156 THR THR D . n 
D 4 157 LEU 157 157 157 LEU LEU D . n 
D 4 158 THR 158 158 158 THR THR D . n 
D 4 159 TRP 159 159 159 TRP TRP D . n 
D 4 160 ASN 160 160 160 ASN ASN D . n 
D 4 161 SER 161 161 161 SER SER D . n 
D 4 162 GLY 162 162 162 GLY GLY D . n 
D 4 163 SER 163 163 163 SER SER D . n 
D 4 164 LEU 164 164 164 LEU LEU D . n 
D 4 165 SER 165 165 165 SER SER D . n 
D 4 166 ALA 166 166 166 ALA ALA D . n 
D 4 167 GLY 167 167 167 GLY GLY D . n 
D 4 168 VAL 168 168 168 VAL VAL D . n 
D 4 169 HIS 169 169 169 HIS HIS D . n 
D 4 170 THR 170 170 170 THR THR D . n 
D 4 171 PHE 171 171 171 PHE PHE D . n 
D 4 172 PRO 172 172 172 PRO PRO D . n 
D 4 173 ALA 173 173 173 ALA ALA D . n 
D 4 174 VAL 174 174 174 VAL VAL D . n 
D 4 175 LEU 175 175 175 LEU LEU D . n 
D 4 176 GLN 176 176 176 GLN GLN D . n 
D 4 177 SER 177 177 177 SER SER D . n 
D 4 178 SER 178 178 178 SER SER D . n 
D 4 179 LEU 179 179 179 LEU LEU D . n 
D 4 180 TYR 180 180 180 TYR TYR D . n 
D 4 181 THR 181 181 181 THR THR D . n 
D 4 182 LEU 182 182 182 LEU LEU D . n 
D 4 183 SER 183 183 183 SER SER D . n 
D 4 184 SER 184 184 184 SER SER D . n 
D 4 185 SER 185 185 185 SER SER D . n 
D 4 186 VAL 186 186 186 VAL VAL D . n 
D 4 187 THR 187 187 187 THR THR D . n 
D 4 188 VAL 188 188 188 VAL VAL D . n 
D 4 189 VAL 189 189 189 VAL VAL D . n 
D 4 190 ALA 190 190 190 ALA ALA D . n 
D 4 191 SER 191 191 191 SER SER D . n 
D 4 192 THR 192 192 192 THR THR D . n 
D 4 193 TRP 193 193 193 TRP TRP D . n 
D 4 194 PRO 194 194 194 PRO PRO D . n 
D 4 195 SER 195 195 195 SER SER D . n 
D 4 196 GLN 196 196 196 GLN GLN D . n 
D 4 197 SER 197 197 197 SER SER D . n 
D 4 198 ILE 198 198 198 ILE ILE D . n 
D 4 199 THR 199 199 199 THR THR D . n 
D 4 200 CYS 200 200 200 CYS CYS D . n 
D 4 201 ASN 201 201 201 ASN ASN D . n 
D 4 202 VAL 202 202 202 VAL VAL D . n 
D 4 203 ALA 203 203 203 ALA ALA D . n 
D 4 204 HIS 204 204 204 HIS HIS D . n 
D 4 205 PRO 205 205 205 PRO PRO D . n 
D 4 206 ALA 206 206 206 ALA ALA D . n 
D 4 207 SER 207 207 207 SER SER D . n 
D 4 208 SER 208 208 208 SER SER D . n 
D 4 209 THR 209 209 209 THR THR D . n 
D 4 210 LYS 210 210 210 LYS LYS D . n 
D 4 211 VAL 211 211 211 VAL VAL D . n 
D 4 212 ASP 212 212 212 ASP ASP D . n 
D 4 213 LYS 213 213 213 LYS LYS D . n 
D 4 214 LYS 214 214 214 LYS LYS D . n 
D 4 215 ILE 215 215 215 ILE ILE D . n 
D 4 216 GLU 216 216 216 GLU GLU D . n 
D 4 217 PRO 217 217 217 PRO PRO D . n 
D 4 218 ARG 218 218 ?   ?   ?   D . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
E 5 NAG 1 E NAG 1 E NAG 1 n 
E 5 NAG 2 E NAG 2 E NAG 2 n 
E 5 BMA 3 E BMA 3 E BMA 3 n 
F 5 NAG 1 I NAG 1 I NAG 1 n 
F 5 NAG 2 I NAG 2 I NAG 2 n 
F 5 BMA 3 I BMA 3 I BMA 3 n 
G 6 NAG 1 F NAG 1 F NAG 1 n 
G 6 NAG 2 F NAG 2 F NAG 2 n 
G 6 BMA 3 F BMA 3 F BMA 3 n 
G 6 MAN 4 F MAN 4 F MAN 4 n 
G 6 MAN 5 F MAN 5 F MAN 5 n 
G 6 MAN 6 F MAN 6 F MAN 6 n 
H 7 NAG 1 G NAG 1 G NAG 1 n 
H 7 NAG 2 G NAG 2 G NAG 2 n 
H 7 BMA 3 G BMA 3 G BMA 3 n 
H 7 MAN 4 G MAN 4 G MAN 4 n 
H 7 MAN 5 G MAN 5 G MAN 5 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A6A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A6A 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I  8  CA    1  2001 2001 CA    CA  A . 
J  8  CA    1  2002 2002 CA    CA  A . 
K  8  CA    1  2003 2003 CA    CA  A . 
L  8  CA    1  2004 2004 CA    CA  A . 
M  9  GOL   1  2005 3    GOL   GOL A . 
N  9  GOL   1  2006 4    GOL   GOL A . 
O  9  GOL   1  2007 5    GOL   GOL A . 
P  9  GOL   1  2008 9    GOL   GOL A . 
Q  10 MG    1  2001 2001 MG    MG  B . 
R  8  CA    1  2002 2002 CA    CA  B . 
S  8  CA    1  2003 2003 CA    CA  B . 
T  11 A1A6A 1  2004 1    A1A6A 771 B . 
U  12 NAG   1  2005 8001 NAG   NAG B . 
V  9  GOL   1  2006 6    GOL   GOL B . 
W  9  GOL   1  2007 8    GOL   GOL B . 
X  13 ACT   1  2008 3    ACT   ACT B . 
Y  12 NAG   1  2009 2    NAG   NAG B . 
Z  9  GOL   1  301  1    GOL   GOL C . 
AA 9  GOL   1  301  7    GOL   GOL D . 
BA 13 ACT   1  302  2    ACT   ACT D . 
CA 14 HOH   1  2101 33   HOH   HOH A . 
CA 14 HOH   2  2102 30   HOH   HOH A . 
CA 14 HOH   3  2103 31   HOH   HOH A . 
CA 14 HOH   4  2104 11   HOH   HOH A . 
CA 14 HOH   5  2105 9    HOH   HOH A . 
CA 14 HOH   6  2106 49   HOH   HOH A . 
CA 14 HOH   7  2107 15   HOH   HOH A . 
CA 14 HOH   8  2108 57   HOH   HOH A . 
CA 14 HOH   9  2109 46   HOH   HOH A . 
CA 14 HOH   10 2110 13   HOH   HOH A . 
CA 14 HOH   11 2111 41   HOH   HOH A . 
CA 14 HOH   12 2112 64   HOH   HOH A . 
CA 14 HOH   13 2113 28   HOH   HOH A . 
CA 14 HOH   14 2114 19   HOH   HOH A . 
CA 14 HOH   15 2115 56   HOH   HOH A . 
CA 14 HOH   16 2116 40   HOH   HOH A . 
CA 14 HOH   17 2117 52   HOH   HOH A . 
CA 14 HOH   18 2118 60   HOH   HOH A . 
CA 14 HOH   19 2119 32   HOH   HOH A . 
CA 14 HOH   20 2120 26   HOH   HOH A . 
CA 14 HOH   21 2121 39   HOH   HOH A . 
CA 14 HOH   22 2122 14   HOH   HOH A . 
CA 14 HOH   23 2123 29   HOH   HOH A . 
CA 14 HOH   24 2124 8    HOH   HOH A . 
CA 14 HOH   25 2125 27   HOH   HOH A . 
CA 14 HOH   26 2126 62   HOH   HOH A . 
CA 14 HOH   27 2127 20   HOH   HOH A . 
CA 14 HOH   28 2128 10   HOH   HOH A . 
CA 14 HOH   29 2129 38   HOH   HOH A . 
CA 14 HOH   30 2130 23   HOH   HOH A . 
CA 14 HOH   31 2131 44   HOH   HOH A . 
CA 14 HOH   32 2132 63   HOH   HOH A . 
CA 14 HOH   33 2133 48   HOH   HOH A . 
DA 14 HOH   1  2101 36   HOH   HOH B . 
DA 14 HOH   2  2102 4    HOH   HOH B . 
DA 14 HOH   3  2103 3    HOH   HOH B . 
DA 14 HOH   4  2104 18   HOH   HOH B . 
DA 14 HOH   5  2105 6    HOH   HOH B . 
DA 14 HOH   6  2106 42   HOH   HOH B . 
DA 14 HOH   7  2107 2    HOH   HOH B . 
DA 14 HOH   8  2108 7    HOH   HOH B . 
DA 14 HOH   9  2109 53   HOH   HOH B . 
DA 14 HOH   10 2110 45   HOH   HOH B . 
DA 14 HOH   11 2111 16   HOH   HOH B . 
DA 14 HOH   12 2112 25   HOH   HOH B . 
DA 14 HOH   13 2113 24   HOH   HOH B . 
DA 14 HOH   14 2114 17   HOH   HOH B . 
DA 14 HOH   15 2115 1    HOH   HOH B . 
DA 14 HOH   16 2116 35   HOH   HOH B . 
DA 14 HOH   17 2117 5    HOH   HOH B . 
EA 14 HOH   1  401  22   HOH   HOH D . 
EA 14 HOH   2  402  66   HOH   HOH D . 
EA 14 HOH   3  403  58   HOH   HOH D . 
EA 14 HOH   4  404  21   HOH   HOH D . 
EA 14 HOH   5  405  50   HOH   HOH D . 
EA 14 HOH   6  406  65   HOH   HOH D . 
EA 14 HOH   7  407  51   HOH   HOH D . 
# 
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 N 1 E NAG 1    ? O1 ? E NAG 1 O1 
2 1 N 1 B NAG 2005 ? O1 ? U NAG 1 O1 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.17.1_3660 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? 3.13.0      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.9       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                     9CZ7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     96.494 
_cell.length_a_esd                 ? 
_cell.length_b                     132.501 
_cell.length_b_esd                 ? 
_cell.length_c                     168.366 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CZ7 
_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                   9CZ7 
_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             3.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.72 
_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, HANGING 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    '13% PEG 3350, 100 mM HEPES pH 7.1, 200 mM ammonium citrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-05-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.920105 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.920105 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          62.27 
_reflns.entry_id                                       9CZ7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.57 
_reflns.d_resolution_low                               52.06 
_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                                     69516 
_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                           99.88 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.36 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.57 
_reflns_shell.d_res_low                                     2.662 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5073 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.369 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CZ7 
_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                            2.57 
_refine.ls_d_res_low                             52.06 
_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                     69369 
_refine.ls_number_reflns_R_free                  3422 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2170 
_refine.ls_R_factor_R_free                       0.2342 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2161 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.52 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.36 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.57 
_refine_hist.d_res_low                        52.06 
_refine_hist.number_atoms_solvent             57 
_refine_hist.number_atoms_total               11823 
_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        11434 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         332 
_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' ? 0.003  ? 12022 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.650  ? 16287 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.569 ? 4435  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 1846  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 2094  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.57 2.61  . . 135 2663 97.00  . . . . 0.3524 . . . . . . . . . . . 0.3524 
'X-RAY DIFFRACTION' 2.61 2.64  . . 143 2695 100.00 . . . . 0.3483 . . . . . . . . . . . 0.3923 
'X-RAY DIFFRACTION' 2.64 2.69  . . 138 2731 100.00 . . . . 0.3248 . . . . . . . . . . . 0.3843 
'X-RAY DIFFRACTION' 2.69 2.73  . . 140 2716 100.00 . . . . 0.3263 . . . . . . . . . . . 0.3266 
'X-RAY DIFFRACTION' 2.73 2.78  . . 139 2729 100.00 . . . . 0.3089 . . . . . . . . . . . 0.3089 
'X-RAY DIFFRACTION' 2.78 2.83  . . 157 2708 100.00 . . . . 0.3061 . . . . . . . . . . . 0.3239 
'X-RAY DIFFRACTION' 2.83 2.88  . . 127 2721 100.00 . . . . 0.2917 . . . . . . . . . . . 0.3284 
'X-RAY DIFFRACTION' 2.88 2.94  . . 142 2734 100.00 . . . . 0.2912 . . . . . . . . . . . 0.2912 
'X-RAY DIFFRACTION' 2.94 3.00  . . 135 2722 100.00 . . . . 0.3010 . . . . . . . . . . . 0.3294 
'X-RAY DIFFRACTION' 3.00 3.07  . . 144 2711 100.00 . . . . 0.2898 . . . . . . . . . . . 0.2946 
'X-RAY DIFFRACTION' 3.07 3.15  . . 157 2732 100.00 . . . . 0.2682 . . . . . . . . . . . 0.2682 
'X-RAY DIFFRACTION' 3.15 3.24  . . 125 2745 100.00 . . . . 0.2676 . . . . . . . . . . . 0.2843 
'X-RAY DIFFRACTION' 3.24 3.33  . . 141 2731 100.00 . . . . 0.2590 . . . . . . . . . . . 0.2661 
'X-RAY DIFFRACTION' 3.33 3.44  . . 132 2743 100.00 . . . . 0.2459 . . . . . . . . . . . 0.2632 
'X-RAY DIFFRACTION' 3.44 3.56  . . 153 2754 100.00 . . . . 0.2423 . . . . . . . . . . . 0.2680 
'X-RAY DIFFRACTION' 3.56 3.70  . . 143 2727 100.00 . . . . 0.2242 . . . . . . . . . . . 0.2669 
'X-RAY DIFFRACTION' 3.70 3.87  . . 142 2751 100.00 . . . . 0.2035 . . . . . . . . . . . 0.2418 
'X-RAY DIFFRACTION' 3.87 4.08  . . 157 2732 100.00 . . . . 0.1857 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 4.08 4.33  . . 146 2774 100.00 . . . . 0.1743 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 4.33 4.67  . . 139 2772 100.00 . . . . 0.1556 . . . . . . . . . . . 0.1563 
'X-RAY DIFFRACTION' 4.67 5.14  . . 148 2794 100.00 . . . . 0.1558 . . . . . . . . . . . 0.1785 
'X-RAY DIFFRACTION' 5.14 5.88  . . 141 2794 100.00 . . . . 0.1803 . . . . . . . . . . . 0.1848 
'X-RAY DIFFRACTION' 5.88 7.40  . . 141 2844 100.00 . . . . 0.2020 . . . . . . . . . . . 0.2283 
'X-RAY DIFFRACTION' 7.40 52.06 . . 157 2924 99.00  . . . . 0.1854 . . . . . . . . . . . 0.2013 
# 
_struct.entry_id                     9CZ7 
_struct.title                        'Crystal structure of integrin avb6 headpiece in complex with compound 12' 
_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        9CZ7 
_struct_keywords.text            
;avb6 integrin, fibrosis, idiopathic pulmonary fibrosis, free energy perturbation, CELL ADHESION, CELL ADHESION-IMMUNE SYSTEM complex
;
_struct_keywords.pdbx_keywords   'CELL ADHESION/IMMUNE SYSTEM' 
# 
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 4  ? 
E  N N 5  ? 
F  N N 5  ? 
G  N N 6  ? 
H  N N 7  ? 
I  N N 8  ? 
J  N N 8  ? 
K  N N 8  ? 
L  N N 8  ? 
M  N N 9  ? 
N  N N 9  ? 
O  N N 9  ? 
P  N N 9  ? 
Q  N N 10 ? 
R  N N 8  ? 
S  N N 8  ? 
T  N N 11 ? 
U  N N 12 ? 
V  N N 9  ? 
W  N N 9  ? 
X  N N 13 ? 
Y  N N 12 ? 
Z  N N 9  ? 
AA N N 9  ? 
BA N N 13 ? 
CA N N 14 ? 
DA N N 14 ? 
EA N N 14 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ITAV_HUMAN P06756 ? 1 
;FNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDY
AKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFS
IDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFV
SGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQ
RASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSM
PPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLK
ADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFME
YRLDYRTAADTTGLQPILNQFTPANISRQAHILLD
;
31 
2 UNP ITB6_HUMAN P18564 ? 2 
;GCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDI
VQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKP
VSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRND
SLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENY
AKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTV
NIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCE
;
22 
3 PDB 9CZ7       9CZ7   ? 3 ? 1  
4 PDB 9CZ7       9CZ7   ? 4 ? 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 9CZ7 A 1 ? 595 ? P06756 31 ? 625 ? 1 595 
2 2 9CZ7 B 1 ? 470 ? P18564 22 ? 491 ? 5 474 
3 3 9CZ7 C 1 ? 214 ? 9CZ7   1  ? 214 ? 1 214 
4 4 9CZ7 D 1 ? 218 ? 9CZ7   1  ? 218 ? 1 218 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CZ7 CYS A 400 ? UNP P06756 MET 430 conflict         400 1  
1 9CZ7 GLY A 596 ? UNP P06756 ?   ?   'expression tag' 596 2  
1 9CZ7 GLY A 597 ? UNP P06756 ?   ?   'expression tag' 597 3  
1 9CZ7 SER A 598 ? UNP P06756 ?   ?   'expression tag' 598 4  
1 9CZ7 LEU A 599 ? UNP P06756 ?   ?   'expression tag' 599 5  
1 9CZ7 GLU A 600 ? UNP P06756 ?   ?   'expression tag' 600 6  
1 9CZ7 VAL A 601 ? UNP P06756 ?   ?   'expression tag' 601 7  
1 9CZ7 LEU A 602 ? UNP P06756 ?   ?   'expression tag' 602 8  
1 9CZ7 PHE A 603 ? UNP P06756 ?   ?   'expression tag' 603 9  
1 9CZ7 GLN A 604 ? UNP P06756 ?   ?   'expression tag' 604 10 
1 9CZ7 GLY A 605 ? UNP P06756 ?   ?   'expression tag' 605 11 
2 9CZ7 CYS B 266 ? UNP P18564 ILE 287 conflict         270 12 
2 9CZ7 SER B 471 ? UNP P18564 ?   ?   'expression tag' 475 13 
2 9CZ7 GLY B 472 ? UNP P18564 ?   ?   'expression tag' 476 14 
2 9CZ7 HIS B 473 ? UNP P18564 ?   ?   'expression tag' 477 15 
2 9CZ7 SER B 474 ? UNP P18564 ?   ?   'expression tag' 478 16 
2 9CZ7 LEU B 475 ? UNP P18564 ?   ?   'expression tag' 479 17 
2 9CZ7 GLU B 476 ? UNP P18564 ?   ?   'expression tag' 480 18 
2 9CZ7 VAL B 477 ? UNP P18564 ?   ?   'expression tag' 481 19 
2 9CZ7 LEU B 478 ? UNP P18564 ?   ?   'expression tag' 482 20 
2 9CZ7 PHE B 479 ? UNP P18564 ?   ?   'expression tag' 483 21 
2 9CZ7 GLN B 480 ? UNP P18564 ?   ?   'expression tag' 484 22 
2 9CZ7 GLY B 481 ? UNP P18564 ?   ?   'expression tag' 485 23 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 175 ? GLN A 180 ? GLY A 175 GLN A 180 1 ? 6  
HELX_P HELX_P2  AA2 VAL A 188 ? LYS A 194 ? VAL A 188 LYS A 194 1 ? 7  
HELX_P HELX_P3  AA3 GLN A 214 ? ASP A 218 ? GLN A 214 ASP A 218 5 ? 5  
HELX_P HELX_P4  AA4 ARG A 245 ? LEU A 250 ? ARG A 245 LEU A 250 1 ? 6  
HELX_P HELX_P5  AA5 GLY A 366 ? LYS A 370 ? GLY A 366 LYS A 370 5 ? 5  
HELX_P HELX_P6  AA6 PHE A 427 ? VAL A 429 ? PHE A 427 VAL A 429 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 544 ? PHE A 548 ? ASP A 544 PHE A 548 5 ? 5  
HELX_P HELX_P8  AA8 TYR A 565 ? ALA A 569 ? TYR A 565 ALA A 569 5 ? 5  
HELX_P HELX_P9  AA9 THR B 9   ? GLY B 17  ? THR B 13  GLY B 21  1 ? 9  
HELX_P HELX_P10 AB1 THR B 40  ? LYS B 47  ? THR B 44  LYS B 51  1 ? 8  
HELX_P HELX_P11 AB2 ASN B 76  ? ILE B 80  ? ASN B 80  ILE B 84  5 ? 5  
HELX_P HELX_P12 AB3 SER B 121 ? SER B 123 ? SER B 125 SER B 127 5 ? 3  
HELX_P HELX_P13 AB4 MET B 124 ? ILE B 131 ? MET B 128 ILE B 135 1 ? 8  
HELX_P HELX_P14 AB5 GLU B 133 ? LYS B 144 ? GLU B 137 LYS B 148 1 ? 12 
HELX_P HELX_P15 AB6 THR B 168 ? ASN B 174 ? THR B 172 ASN B 178 1 ? 7  
HELX_P HELX_P16 AB7 ASP B 198 ? ASN B 208 ? ASP B 202 ASN B 212 1 ? 11 
HELX_P HELX_P17 AB8 GLY B 220 ? CYS B 231 ? GLY B 224 CYS B 235 1 ? 12 
HELX_P HELX_P18 AB9 CYS B 231 ? GLY B 236 ? CYS B 235 GLY B 240 1 ? 6  
HELX_P HELX_P19 AC1 PHE B 255 ? GLY B 263 ? PHE B 259 GLY B 267 5 ? 9  
HELX_P HELX_P20 AC2 TYR B 280 ? VAL B 285 ? TYR B 284 VAL B 289 5 ? 6  
HELX_P HELX_P21 AC3 THR B 290 ? ASN B 301 ? THR B 294 ASN B 305 1 ? 12 
HELX_P HELX_P22 AC4 GLN B 313 ? ILE B 324 ? GLN B 317 ILE B 328 1 ? 12 
HELX_P HELX_P23 AC5 ASN B 338 ? SER B 352 ? ASN B 342 SER B 356 1 ? 15 
HELX_P HELX_P24 AC6 CYS B 433 ? LYS B 437 ? CYS B 437 LYS B 441 5 ? 5  
HELX_P HELX_P25 AC7 ASP C 79  ? ILE C 83  ? ASP C 79  ILE C 83  5 ? 5  
HELX_P HELX_P26 AC8 SER C 121 ? SER C 127 ? SER C 121 SER C 127 1 ? 7  
HELX_P HELX_P27 AC9 THR C 182 ? HIS C 189 ? THR C 182 HIS C 189 1 ? 8  
HELX_P HELX_P28 AD1 THR D 28  ? PHE D 32  ? THR D 28  PHE D 32  5 ? 5  
HELX_P HELX_P29 AD2 THR D 74  ? SER D 76  ? THR D 74  SER D 76  5 ? 3  
HELX_P HELX_P30 AD3 SER D 161 ? SER D 163 ? SER D 161 SER D 163 5 ? 3  
HELX_P HELX_P31 AD4 SER D 191 ? TRP D 193 ? SER D 191 TRP D 193 5 ? 3  
HELX_P HELX_P32 AD5 PRO D 205 ? SER D 208 ? PRO D 205 SER D 208 5 ? 4  
# 
_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 ?    ? A CYS 59  SG  ? ? ? 1_555 A  CYS   67  SG  ? ? A CYS 59   A CYS   67   1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf2  disulf ?    ? A CYS 108 SG  ? ? ? 1_555 A  CYS   128 SG  ? ? A CYS 108  A CYS   128  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf3  disulf ?    ? A CYS 142 SG  ? ? ? 1_555 A  CYS   155 SG  ? ? A CYS 142  A CYS   155  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf4  disulf ?    ? A CYS 400 SG  ? ? ? 1_555 B  CYS   266 SG  ? ? A CYS 400  B CYS   270  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf5  disulf ?    ? A CYS 461 SG  ? ? ? 1_555 A  CYS   472 SG  ? ? A CYS 461  A CYS   472  1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf6  disulf ?    ? A CYS 478 SG  ? ? ? 1_555 A  CYS   535 SG  ? ? A CYS 478  A CYS   535  1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf7  disulf ?    ? B CYS 2   SG  ? ? ? 1_555 B  CYS   20  SG  ? ? B CYS 6    B CYS   24   1_555 ? ? ? ? ? ? ? 2.018 ? ? 
disulf8  disulf ?    ? B CYS 10  SG  ? ? ? 1_555 B  CYS   433 SG  ? ? B CYS 14   B CYS   437  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf9  disulf ?    ? B CYS 13  SG  ? ? ? 1_555 B  CYS   38  SG  ? ? B CYS 17   B CYS   42   1_555 ? ? ? ? ? ? ? 2.024 ? ? 
disulf10 disulf ?    ? B CYS 23  SG  ? ? ? 1_555 B  CYS   49  SG  ? ? B CYS 27   B CYS   53   1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf11 disulf ?    ? B CYS 176 SG  ? ? ? 1_555 B  CYS   183 SG  ? ? B CYS 180  B CYS   187  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf12 disulf ?    ? B CYS 231 SG  ? ? ? 1_555 B  CYS   272 SG  ? ? B CYS 235  B CYS   276  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf13 disulf ?    ? B CYS 373 SG  ? ? ? 1_555 B  CYS   385 SG  ? ? B CYS 377  B CYS   389  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf14 disulf ?    ? B CYS 405 SG  ? ? ? 1_555 B  CYS   431 SG  ? ? B CYS 409  B CYS   435  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf15 disulf ?    ? B CYS 435 SG  ? ? ? 1_555 B  CYS   455 SG  ? ? B CYS 439  B CYS   459  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf16 disulf ?    ? B CYS 446 SG  ? ? ? 1_555 B  CYS   458 SG  ? ? B CYS 450  B CYS   462  1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf17 disulf ?    ? B CYS 460 SG  ? ? ? 1_555 B  CYS   469 SG  ? ? B CYS 464  B CYS   473  1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf18 disulf ?    ? C CYS 23  SG  ? ? ? 1_555 C  CYS   88  SG  ? ? C CYS 23   C CYS   88   1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf19 disulf ?    ? C CYS 134 SG  ? ? ? 1_555 C  CYS   194 SG  ? ? C CYS 134  C CYS   194  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf20 disulf ?    ? C CYS 214 SG  ? ? ? 1_555 D  CYS   133 SG  ? ? C CYS 214  D CYS   133  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf21 disulf ?    ? D CYS 22  SG  ? ? ? 1_555 D  CYS   96  SG  ? ? D CYS 22   D CYS   96   1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf22 disulf ?    ? D CYS 145 SG  ? ? ? 1_555 D  CYS   200 SG  ? ? D CYS 145  D CYS   200  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
covale1  covale one  ? A ASN 44  ND2 ? ? ? 1_555 F  NAG   .   C1  ? ? A ASN 44   I NAG   1    1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale2  covale one  ? A ASN 260 ND2 ? ? ? 1_555 G  NAG   .   C1  ? ? A ASN 260  F NAG   1    1_555 ? ? ? ? ? ? ? 1.439 ? 
N-Glycosylation 
covale3  covale one  ? A ASN 266 ND2 ? ? ? 1_555 H  NAG   .   C1  ? ? A ASN 266  G NAG   1    1_555 ? ? ? ? ? ? ? 1.437 ? 
N-Glycosylation 
covale4  covale one  ? B ASN 239 ND2 ? ? ? 1_555 Y  NAG   .   C1  ? ? B ASN 243  B NAG   2009 1_555 ? ? ? ? ? ? ? 1.446 ? 
N-Glycosylation 
covale5  covale both ? E NAG .   O4  ? ? ? 1_555 E  NAG   .   C1  ? ? E NAG 1    E NAG   2    1_555 ? ? ? ? ? ? ? 1.413 ? ? 
covale6  covale both ? E NAG .   O4  ? ? ? 1_555 E  BMA   .   C1  ? ? E NAG 2    E BMA   3    1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale7  covale both ? F NAG .   O4  ? ? ? 1_555 F  NAG   .   C1  ? ? I NAG 1    I NAG   2    1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale8  covale both ? F NAG .   O4  ? ? ? 1_555 F  BMA   .   C1  ? ? I NAG 2    I BMA   3    1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale9  covale both ? G NAG .   O4  ? ? ? 1_555 G  NAG   .   C1  ? ? F NAG 1    F NAG   2    1_555 ? ? ? ? ? ? ? 1.448 ? ? 
covale10 covale both ? G NAG .   O4  ? ? ? 1_555 G  BMA   .   C1  ? ? F NAG 2    F BMA   3    1_555 ? ? ? ? ? ? ? 1.447 ? ? 
covale11 covale both ? G BMA .   O6  ? ? ? 1_555 G  MAN   .   C1  ? ? F BMA 3    F MAN   4    1_555 ? ? ? ? ? ? ? 1.452 ? ? 
covale12 covale both ? G MAN .   O3  ? ? ? 1_555 G  MAN   .   C1  ? ? F MAN 4    F MAN   5    1_555 ? ? ? ? ? ? ? 1.437 ? ? 
covale13 covale both ? G MAN .   O6  ? ? ? 1_555 G  MAN   .   C1  ? ? F MAN 4    F MAN   6    1_555 ? ? ? ? ? ? ? 1.450 ? ? 
covale14 covale both ? H NAG .   O4  ? ? ? 1_555 H  NAG   .   C1  ? ? G NAG 1    G NAG   2    1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale15 covale both ? H NAG .   O4  ? ? ? 1_555 H  BMA   .   C1  ? ? G NAG 2    G BMA   3    1_555 ? ? ? ? ? ? ? 1.442 ? ? 
covale16 covale both ? H BMA .   O3  ? ? ? 1_555 H  MAN   .   C1  ? ? G BMA 3    G MAN   4    1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale17 covale both ? H BMA .   O6  ? ? ? 1_555 H  MAN   .   C1  ? ? G BMA 3    G MAN   5    1_555 ? ? ? ? ? ? ? 1.441 ? ? 
metalc1  metalc ?    ? A ASP 230 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 230  A CA    2001 1_555 ? ? ? ? ? ? ? 2.389 ? ? 
metalc2  metalc ?    ? A ASN 232 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASN 232  A CA    2001 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc3  metalc ?    ? A ASP 234 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 234  A CA    2001 1_555 ? ? ? ? ? ? ? 2.443 ? ? 
metalc4  metalc ?    ? A ILE 236 O   ? ? ? 1_555 I  CA    .   CA  ? ? A ILE 236  A CA    2001 1_555 ? ? ? ? ? ? ? 2.217 ? ? 
metalc5  metalc ?    ? A ASP 238 OD1 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 238  A CA    2001 1_555 ? ? ? ? ? ? ? 2.393 ? ? 
metalc6  metalc ?    ? A ASP 238 OD2 ? ? ? 1_555 I  CA    .   CA  ? ? A ASP 238  A CA    2001 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc7  metalc ?    ? A ASP 284 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 284  A CA    2004 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc8  metalc ?    ? A ASN 286 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASN 286  A CA    2004 1_555 ? ? ? ? ? ? ? 2.351 ? ? 
metalc9  metalc ?    ? A ASP 288 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 288  A CA    2004 1_555 ? ? ? ? ? ? ? 2.445 ? ? 
metalc10 metalc ?    ? A TYR 290 O   ? ? ? 1_555 L  CA    .   CA  ? ? A TYR 290  A CA    2004 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
metalc11 metalc ?    ? A ASP 292 OD1 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 292  A CA    2004 1_555 ? ? ? ? ? ? ? 2.380 ? ? 
metalc12 metalc ?    ? A ASP 292 OD2 ? ? ? 1_555 L  CA    .   CA  ? ? A ASP 292  A CA    2004 1_555 ? ? ? ? ? ? ? 2.430 ? ? 
metalc13 metalc ?    ? A ASP 349 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 349  A CA    2002 1_555 ? ? ? ? ? ? ? 2.411 ? ? 
metalc14 metalc ?    ? A ASP 351 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 351  A CA    2002 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc15 metalc ?    ? A ASP 353 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 353  A CA    2002 1_555 ? ? ? ? ? ? ? 2.419 ? ? 
metalc16 metalc ?    ? A PHE 355 O   ? ? ? 1_555 J  CA    .   CA  ? ? A PHE 355  A CA    2002 1_555 ? ? ? ? ? ? ? 2.251 ? ? 
metalc17 metalc ?    ? A ASP 357 OD1 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 357  A CA    2002 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc18 metalc ?    ? A ASP 357 OD2 ? ? ? 1_555 J  CA    .   CA  ? ? A ASP 357  A CA    2002 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc19 metalc ?    ? A ASP 413 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 413  A CA    2003 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc20 metalc ?    ? A ASP 415 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 415  A CA    2003 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc21 metalc ?    ? A ASN 417 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASN 417  A CA    2003 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc22 metalc ?    ? A TYR 419 O   ? ? ? 1_555 K  CA    .   CA  ? ? A TYR 419  A CA    2003 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc23 metalc ?    ? A ASP 421 OD1 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 421  A CA    2003 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc24 metalc ?    ? A ASP 421 OD2 ? ? ? 1_555 K  CA    .   CA  ? ? A ASP 421  A CA    2003 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc25 metalc ?    ? I CA  .   CA  ? ? ? 1_555 CA HOH   .   O   ? ? A CA  2001 A HOH   2104 1_555 ? ? ? ? ? ? ? 2.400 ? ? 
metalc26 metalc ?    ? J CA  .   CA  ? ? ? 1_555 CA HOH   .   O   ? ? A CA  2002 A HOH   2103 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
metalc27 metalc ?    ? K CA  .   CA  ? ? ? 1_555 CA HOH   .   O   ? ? A CA  2003 A HOH   2119 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc28 metalc ?    ? L CA  .   CA  ? ? ? 1_555 CA HOH   .   O   ? ? A CA  2004 A HOH   2101 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc29 metalc ?    ? B SER 121 OG  ? ? ? 1_555 Q  MG    .   MG  ? ? B SER 125  B MG    2001 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc30 metalc ?    ? B SER 123 O   ? ? ? 1_555 S  CA    .   CA  ? ? B SER 127  B CA    2003 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc31 metalc ?    ? B ASP 126 OD1 ? ? ? 1_555 S  CA    .   CA  ? ? B ASP 130  B CA    2003 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc32 metalc ?    ? B ASP 126 OD2 ? ? ? 1_555 S  CA    .   CA  ? ? B ASP 130  B CA    2003 1_555 ? ? ? ? ? ? ? 2.459 ? ? 
metalc33 metalc ?    ? B ASP 127 OD1 ? ? ? 1_555 S  CA    .   CA  ? ? B ASP 131  B CA    2003 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc34 metalc ?    ? B GLU 158 OE2 ? ? ? 1_555 R  CA    .   CA  ? ? B GLU 162  B CA    2002 1_555 ? ? ? ? ? ? ? 2.401 ? ? 
metalc35 metalc ?    ? B ASN 214 OD1 ? ? ? 1_555 R  CA    .   CA  ? ? B ASN 218  B CA    2002 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc36 metalc ?    ? B ASP 216 O   ? ? ? 1_555 R  CA    .   CA  ? ? B ASP 220  B CA    2002 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc37 metalc ?    ? B ASP 216 OD1 ? ? ? 1_555 R  CA    .   CA  ? ? B ASP 220  B CA    2002 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc38 metalc ?    ? B PRO 218 O   ? ? ? 1_555 R  CA    .   CA  ? ? B PRO 222  B CA    2002 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc39 metalc ?    ? B GLU 219 OE2 ? ? ? 1_555 Q  MG    .   MG  ? ? B GLU 223  B MG    2001 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc40 metalc ?    ? B GLU 219 OE1 ? ? ? 1_555 R  CA    .   CA  ? ? B GLU 223  B CA    2002 1_555 ? ? ? ? ? ? ? 2.369 ? ? 
metalc41 metalc ?    ? B LYS 334 O   ? ? ? 1_555 S  CA    .   CA  ? ? B LYS 338  B CA    2003 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc42 metalc ?    ? Q MG  .   MG  ? ? ? 1_555 T  A1A6A .   O01 ? ? B MG  2001 B A1A6A 2004 1_555 ? ? ? ? ? ? ? 2.149 ? ? 
metalc43 metalc ?    ? Q MG  .   MG  ? ? ? 1_555 DA HOH   .   O   ? ? B MG  2001 B HOH   2103 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
metalc44 metalc ?    ? Q MG  .   MG  ? ? ? 1_555 DA HOH   .   O   ? ? B MG  2001 B HOH   2107 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc45 metalc ?    ? Q MG  .   MG  ? ? ? 1_555 DA HOH   .   O   ? ? B MG  2001 B HOH   2115 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc46 metalc ?    ? S CA  .   CA  ? ? ? 1_555 DA HOH   .   O   ? ? B CA  2003 B HOH   2102 1_555 ? ? ? ? ? ? ? 2.490 ? ? 
metalc47 metalc ?    ? S CA  .   CA  ? ? ? 1_555 DA HOH   .   O   ? ? B CA  2003 B HOH   2117 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OD1 ? A  ASP   230 ? A ASP   230  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD1 ? A  ASN   232 ? A ASN   232  ? 1_555 84.5  ? 
2   OD1 ? A  ASP   230 ? A ASP   230  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP   234 ? A ASP   234  ? 1_555 80.3  ? 
3   OD1 ? A  ASN   232 ? A ASN   232  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP   234 ? A ASP   234  ? 1_555 77.9  ? 
4   OD1 ? A  ASP   230 ? A ASP   230  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? A  ILE   236 ? A ILE   236  ? 1_555 80.7  ? 
5   OD1 ? A  ASN   232 ? A ASN   232  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? A  ILE   236 ? A ILE   236  ? 1_555 163.5 ? 
6   OD1 ? A  ASP   234 ? A ASP   234  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? A  ILE   236 ? A ILE   236  ? 1_555 92.4  ? 
7   OD1 ? A  ASP   230 ? A ASP   230  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP   238 ? A ASP   238  ? 1_555 135.3 ? 
8   OD1 ? A  ASN   232 ? A ASN   232  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP   238 ? A ASP   238  ? 1_555 104.6 ? 
9   OD1 ? A  ASP   234 ? A ASP   234  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP   238 ? A ASP   238  ? 1_555 144.3 ? 
10  O   ? A  ILE   236 ? A ILE   236  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD1 ? A  ASP   238 ? A ASP   238  ? 1_555 91.1  ? 
11  OD1 ? A  ASP   230 ? A ASP   230  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP   238 ? A ASP   238  ? 1_555 85.2  ? 
12  OD1 ? A  ASN   232 ? A ASN   232  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP   238 ? A ASP   238  ? 1_555 82.1  ? 
13  OD1 ? A  ASP   234 ? A ASP   234  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP   238 ? A ASP   238  ? 1_555 156.3 ? 
14  O   ? A  ILE   236 ? A ILE   236  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP   238 ? A ASP   238  ? 1_555 103.8 ? 
15  OD1 ? A  ASP   238 ? A ASP   238  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 OD2 ? A  ASP   238 ? A ASP   238  ? 1_555 54.0  ? 
16  OD1 ? A  ASP   230 ? A ASP   230  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? CA HOH   .   ? A HOH   2104 ? 1_555 150.7 ? 
17  OD1 ? A  ASN   232 ? A ASN   232  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? CA HOH   .   ? A HOH   2104 ? 1_555 85.7  ? 
18  OD1 ? A  ASP   234 ? A ASP   234  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? CA HOH   .   ? A HOH   2104 ? 1_555 70.6  ? 
19  O   ? A  ILE   236 ? A ILE   236  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? CA HOH   .   ? A HOH   2104 ? 1_555 103.8 ? 
20  OD1 ? A  ASP   238 ? A ASP   238  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? CA HOH   .   ? A HOH   2104 ? 1_555 74.0  ? 
21  OD2 ? A  ASP   238 ? A ASP   238  ? 1_555 CA ? I CA . ? A CA 2001 ? 1_555 O   ? CA HOH   .   ? A HOH   2104 ? 1_555 120.6 ? 
22  OD1 ? A  ASP   284 ? A ASP   284  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD1 ? A  ASN   286 ? A ASN   286  ? 1_555 77.5  ? 
23  OD1 ? A  ASP   284 ? A ASP   284  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP   288 ? A ASP   288  ? 1_555 72.1  ? 
24  OD1 ? A  ASN   286 ? A ASN   286  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP   288 ? A ASP   288  ? 1_555 79.9  ? 
25  OD1 ? A  ASP   284 ? A ASP   284  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? A  TYR   290 ? A TYR   290  ? 1_555 88.1  ? 
26  OD1 ? A  ASN   286 ? A ASN   286  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? A  TYR   290 ? A TYR   290  ? 1_555 165.5 ? 
27  OD1 ? A  ASP   288 ? A ASP   288  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? A  TYR   290 ? A TYR   290  ? 1_555 94.4  ? 
28  OD1 ? A  ASP   284 ? A ASP   284  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP   292 ? A ASP   292  ? 1_555 138.9 ? 
29  OD1 ? A  ASN   286 ? A ASN   286  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP   292 ? A ASP   292  ? 1_555 115.4 ? 
30  OD1 ? A  ASP   288 ? A ASP   288  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP   292 ? A ASP   292  ? 1_555 145.9 ? 
31  O   ? A  TYR   290 ? A TYR   290  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD1 ? A  ASP   292 ? A ASP   292  ? 1_555 76.6  ? 
32  OD1 ? A  ASP   284 ? A ASP   284  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP   292 ? A ASP   292  ? 1_555 95.8  ? 
33  OD1 ? A  ASN   286 ? A ASN   286  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP   292 ? A ASP   292  ? 1_555 77.2  ? 
34  OD1 ? A  ASP   288 ? A ASP   288  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP   292 ? A ASP   292  ? 1_555 156.0 ? 
35  O   ? A  TYR   290 ? A TYR   290  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP   292 ? A ASP   292  ? 1_555 106.1 ? 
36  OD1 ? A  ASP   292 ? A ASP   292  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 OD2 ? A  ASP   292 ? A ASP   292  ? 1_555 54.2  ? 
37  OD1 ? A  ASP   284 ? A ASP   284  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? CA HOH   .   ? A HOH   2101 ? 1_555 144.6 ? 
38  OD1 ? A  ASN   286 ? A ASN   286  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? CA HOH   .   ? A HOH   2101 ? 1_555 90.3  ? 
39  OD1 ? A  ASP   288 ? A ASP   288  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? CA HOH   .   ? A HOH   2101 ? 1_555 73.1  ? 
40  O   ? A  TYR   290 ? A TYR   290  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? CA HOH   .   ? A HOH   2101 ? 1_555 100.9 ? 
41  OD1 ? A  ASP   292 ? A ASP   292  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? CA HOH   .   ? A HOH   2101 ? 1_555 76.3  ? 
42  OD2 ? A  ASP   292 ? A ASP   292  ? 1_555 CA ? L CA . ? A CA 2004 ? 1_555 O   ? CA HOH   .   ? A HOH   2101 ? 1_555 113.9 ? 
43  OD1 ? A  ASP   349 ? A ASP   349  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP   351 ? A ASP   351  ? 1_555 86.9  ? 
44  OD1 ? A  ASP   349 ? A ASP   349  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP   353 ? A ASP   353  ? 1_555 72.8  ? 
45  OD1 ? A  ASP   351 ? A ASP   351  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP   353 ? A ASP   353  ? 1_555 91.0  ? 
46  OD1 ? A  ASP   349 ? A ASP   349  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? A  PHE   355 ? A PHE   355  ? 1_555 68.5  ? 
47  OD1 ? A  ASP   351 ? A ASP   351  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? A  PHE   355 ? A PHE   355  ? 1_555 154.8 ? 
48  OD1 ? A  ASP   353 ? A ASP   353  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? A  PHE   355 ? A PHE   355  ? 1_555 87.0  ? 
49  OD1 ? A  ASP   349 ? A ASP   349  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP   357 ? A ASP   357  ? 1_555 132.5 ? 
50  OD1 ? A  ASP   351 ? A ASP   351  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP   357 ? A ASP   357  ? 1_555 105.2 ? 
51  OD1 ? A  ASP   353 ? A ASP   353  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP   357 ? A ASP   357  ? 1_555 149.6 ? 
52  O   ? A  PHE   355 ? A PHE   355  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD1 ? A  ASP   357 ? A ASP   357  ? 1_555 88.6  ? 
53  OD1 ? A  ASP   349 ? A ASP   349  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP   357 ? A ASP   357  ? 1_555 88.1  ? 
54  OD1 ? A  ASP   351 ? A ASP   351  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP   357 ? A ASP   357  ? 1_555 73.9  ? 
55  OD1 ? A  ASP   353 ? A ASP   353  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP   357 ? A ASP   357  ? 1_555 156.4 ? 
56  O   ? A  PHE   355 ? A PHE   355  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP   357 ? A ASP   357  ? 1_555 99.0  ? 
57  OD1 ? A  ASP   357 ? A ASP   357  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 OD2 ? A  ASP   357 ? A ASP   357  ? 1_555 53.9  ? 
58  OD1 ? A  ASP   349 ? A ASP   349  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? CA HOH   .   ? A HOH   2103 ? 1_555 147.6 ? 
59  OD1 ? A  ASP   351 ? A ASP   351  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? CA HOH   .   ? A HOH   2103 ? 1_555 101.7 ? 
60  OD1 ? A  ASP   353 ? A ASP   353  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? CA HOH   .   ? A HOH   2103 ? 1_555 75.9  ? 
61  O   ? A  PHE   355 ? A PHE   355  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? CA HOH   .   ? A HOH   2103 ? 1_555 102.2 ? 
62  OD1 ? A  ASP   357 ? A ASP   357  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? CA HOH   .   ? A HOH   2103 ? 1_555 75.7  ? 
63  OD2 ? A  ASP   357 ? A ASP   357  ? 1_555 CA ? J CA . ? A CA 2002 ? 1_555 O   ? CA HOH   .   ? A HOH   2103 ? 1_555 124.2 ? 
64  OD1 ? A  ASP   413 ? A ASP   413  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP   415 ? A ASP   415  ? 1_555 76.3  ? 
65  OD1 ? A  ASP   413 ? A ASP   413  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD1 ? A  ASN   417 ? A ASN   417  ? 1_555 76.2  ? 
66  OD1 ? A  ASP   415 ? A ASP   415  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD1 ? A  ASN   417 ? A ASN   417  ? 1_555 76.2  ? 
67  OD1 ? A  ASP   413 ? A ASP   413  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? A  TYR   419 ? A TYR   419  ? 1_555 73.2  ? 
68  OD1 ? A  ASP   415 ? A ASP   415  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? A  TYR   419 ? A TYR   419  ? 1_555 147.2 ? 
69  OD1 ? A  ASN   417 ? A ASN   417  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? A  TYR   419 ? A TYR   419  ? 1_555 85.0  ? 
70  OD1 ? A  ASP   413 ? A ASP   413  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP   421 ? A ASP   421  ? 1_555 142.2 ? 
71  OD1 ? A  ASP   415 ? A ASP   415  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP   421 ? A ASP   421  ? 1_555 119.9 ? 
72  OD1 ? A  ASN   417 ? A ASN   417  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP   421 ? A ASP   421  ? 1_555 138.3 ? 
73  O   ? A  TYR   419 ? A TYR   419  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD1 ? A  ASP   421 ? A ASP   421  ? 1_555 92.0  ? 
74  OD1 ? A  ASP   413 ? A ASP   413  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP   421 ? A ASP   421  ? 1_555 96.5  ? 
75  OD1 ? A  ASP   415 ? A ASP   415  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP   421 ? A ASP   421  ? 1_555 85.6  ? 
76  OD1 ? A  ASN   417 ? A ASN   417  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP   421 ? A ASP   421  ? 1_555 161.5 ? 
77  O   ? A  TYR   419 ? A TYR   419  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP   421 ? A ASP   421  ? 1_555 109.4 ? 
78  OD1 ? A  ASP   421 ? A ASP   421  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 OD2 ? A  ASP   421 ? A ASP   421  ? 1_555 55.1  ? 
79  OD1 ? A  ASP   413 ? A ASP   413  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? CA HOH   .   ? A HOH   2119 ? 1_555 141.7 ? 
80  OD1 ? A  ASP   415 ? A ASP   415  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? CA HOH   .   ? A HOH   2119 ? 1_555 72.4  ? 
81  OD1 ? A  ASN   417 ? A ASN   417  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? CA HOH   .   ? A HOH   2119 ? 1_555 75.5  ? 
82  O   ? A  TYR   419 ? A TYR   419  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? CA HOH   .   ? A HOH   2119 ? 1_555 128.6 ? 
83  OD1 ? A  ASP   421 ? A ASP   421  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? CA HOH   .   ? A HOH   2119 ? 1_555 74.3  ? 
84  OD2 ? A  ASP   421 ? A ASP   421  ? 1_555 CA ? K CA . ? A CA 2003 ? 1_555 O   ? CA HOH   .   ? A HOH   2119 ? 1_555 102.4 ? 
85  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 98.9  ? 
86  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O01 ? T  A1A6A .   ? B A1A6A 2004 ? 1_555 101.3 ? 
87  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O01 ? T  A1A6A .   ? B A1A6A 2004 ? 1_555 94.4  ? 
88  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2103 ? 1_555 79.0  ? 
89  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2103 ? 1_555 101.6 ? 
90  O01 ? T  A1A6A .   ? B A1A6A 2004 ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2103 ? 1_555 163.8 ? 
91  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2107 ? 1_555 108.6 ? 
92  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2107 ? 1_555 152.1 ? 
93  O01 ? T  A1A6A .   ? B A1A6A 2004 ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2107 ? 1_555 84.5  ? 
94  O   ? DA HOH   .   ? B HOH   2103 ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2107 ? 1_555 80.2  ? 
95  OG  ? B  SER   121 ? B SER   125  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2115 ? 1_555 166.3 ? 
96  OE2 ? B  GLU   219 ? B GLU   223  ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2115 ? 1_555 84.9  ? 
97  O01 ? T  A1A6A .   ? B A1A6A 2004 ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2115 ? 1_555 91.5  ? 
98  O   ? DA HOH   .   ? B HOH   2103 ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2115 ? 1_555 87.4  ? 
99  O   ? DA HOH   .   ? B HOH   2107 ? 1_555 MG ? Q MG . ? B MG 2001 ? 1_555 O   ? DA HOH   .   ? B HOH   2115 ? 1_555 67.3  ? 
100 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 79.4  ? 
101 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 132.1 ? 
102 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 54.3  ? 
103 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 92.5  ? 
104 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 75.1  ? 
105 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 87.2  ? 
106 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 156.1 ? 
107 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 120.4 ? 
108 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 70.9  ? 
109 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? B  LYS   334 ? B LYS   338  ? 1_555 81.3  ? 
110 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2102 ? 1_555 96.9  ? 
111 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2102 ? 1_555 164.3 ? 
112 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2102 ? 1_555 130.9 ? 
113 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2102 ? 1_555 89.9  ? 
114 O   ? B  LYS   334 ? B LYS   338  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2102 ? 1_555 60.2  ? 
115 O   ? B  SER   123 ? B SER   127  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2117 ? 1_555 85.0  ? 
116 OD1 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2117 ? 1_555 92.3  ? 
117 OD2 ? B  ASP   126 ? B ASP   130  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2117 ? 1_555 85.4  ? 
118 OD1 ? B  ASP   127 ? B ASP   131  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2117 ? 1_555 167.4 ? 
119 O   ? B  LYS   334 ? B LYS   338  ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2117 ? 1_555 105.8 ? 
120 O   ? DA HOH   .   ? B HOH   2102 ? 1_555 CA ? S CA . ? B CA 2003 ? 1_555 O   ? DA HOH   .   ? B HOH   2117 ? 1_555 102.6 ? 
121 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 101.6 ? 
122 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 O   ? B  ASP   216 ? B ASP   220  ? 1_555 151.9 ? 
123 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 O   ? B  ASP   216 ? B ASP   220  ? 1_555 85.5  ? 
124 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 88.7  ? 
125 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 79.6  ? 
126 O   ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 65.7  ? 
127 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 76.7  ? 
128 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 177.9 ? 
129 O   ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 96.5  ? 
130 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 O   ? B  PRO   218 ? B PRO   222  ? 1_555 101.6 ? 
131 OE2 ? B  GLU   158 ? B GLU   162  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 104.9 ? 
132 OD1 ? B  ASN   214 ? B ASN   218  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 84.7  ? 
133 O   ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 102.8 ? 
134 OD1 ? B  ASP   216 ? B ASP   220  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 161.0 ? 
135 O   ? B  PRO   218 ? B PRO   222  ? 1_555 CA ? R CA . ? B CA 2002 ? 1_555 OE1 ? B  GLU   219 ? B GLU   223  ? 1_555 94.5  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG F .   ? ASN A 44  ? NAG I 1    ? 1_555 ASN A 44  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG G .   ? ASN A 260 ? NAG F 1    ? 1_555 ASN A 260 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG H .   ? ASN A 266 ? NAG G 1    ? 1_555 ASN A 266 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG Y .   ? ASN B 239 ? NAG B 2009 ? 1_555 ASN B 243 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  CYS A 59  ? CYS A 67  ? CYS A 59   ? 1_555 CYS A 67  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
6  CYS A 108 ? CYS A 128 ? CYS A 108  ? 1_555 CYS A 128 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
7  CYS A 142 ? CYS A 155 ? CYS A 142  ? 1_555 CYS A 155 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS A 400 ? CYS B 266 ? CYS A 400  ? 1_555 CYS B 270 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS A 461 ? CYS A 472 ? CYS A 461  ? 1_555 CYS A 472 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS A 478 ? CYS A 535 ? CYS A 478  ? 1_555 CYS A 535 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS B 2   ? CYS B 20  ? CYS B 6    ? 1_555 CYS B 24  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS B 10  ? CYS B 433 ? CYS B 14   ? 1_555 CYS B 437 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS B 13  ? CYS B 38  ? CYS B 17   ? 1_555 CYS B 42  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS B 23  ? CYS B 49  ? CYS B 27   ? 1_555 CYS B 53  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS B 176 ? CYS B 183 ? CYS B 180  ? 1_555 CYS B 187 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS B 231 ? CYS B 272 ? CYS B 235  ? 1_555 CYS B 276 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS B 373 ? CYS B 385 ? CYS B 377  ? 1_555 CYS B 389 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 CYS B 405 ? CYS B 431 ? CYS B 409  ? 1_555 CYS B 435 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
19 CYS B 435 ? CYS B 455 ? CYS B 439  ? 1_555 CYS B 459 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
20 CYS B 446 ? CYS B 458 ? CYS B 450  ? 1_555 CYS B 462 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
21 CYS B 460 ? CYS B 469 ? CYS B 464  ? 1_555 CYS B 473 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
22 CYS C 23  ? CYS C 88  ? CYS C 23   ? 1_555 CYS C 88  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
23 CYS C 134 ? CYS C 194 ? CYS C 134  ? 1_555 CYS C 194 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
24 CYS C 214 ? CYS D 133 ? CYS C 214  ? 1_555 CYS D 133 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
25 CYS D 22  ? CYS D 96  ? CYS D 22   ? 1_555 CYS D 96  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
26 CYS D 145 ? CYS D 200 ? CYS D 145  ? 1_555 CYS D 200 ? 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 TYR 450 A . ? TYR 450 A PRO 451 A ? PRO 451 A 1 -2.68  
2 ALA 84  B . ? ALA 88  B PRO 85  B ? PRO 89  B 1 1.49   
3 SER 162 B . ? SER 166 B PRO 163 B ? PRO 167 B 1 4.59   
4 ILE 179 B . ? ILE 183 B PRO 180 B ? PRO 184 B 1 -10.00 
5 PHE 94  C . ? PHE 94  C PRO 95  C ? PRO 95  C 1 -1.59  
6 TYR 140 C . ? TYR 140 C PRO 141 C ? PRO 141 C 1 -2.57  
7 PHE 151 D . ? PHE 151 D PRO 152 D ? PRO 152 D 1 -3.52  
8 GLU 153 D . ? GLU 153 D PRO 154 D ? PRO 154 D 1 1.47   
9 TRP 193 D . ? TRP 193 D PRO 194 D ? PRO 194 D 1 3.25   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 5 ? 
AB4 ? 5 ? 
AB5 ? 6 ? 
AB6 ? 5 ? 
AB7 ? 6 ? 
AB8 ? 2 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 6 ? 
AC3 ? 4 ? 
AC4 ? 4 ? 
AC5 ? 3 ? 
AC6 ? 4 ? 
AC7 ? 6 ? 
AC8 ? 4 ? 
AC9 ? 4 ? 
AD1 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB3 4 5 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? parallel      
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? parallel      
AB7 3 4 ? parallel      
AB7 4 5 ? parallel      
AB7 5 6 ? parallel      
AB8 1 2 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? parallel      
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC2 4 5 ? anti-parallel 
AC2 5 6 ? anti-parallel 
AC3 1 2 ? parallel      
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC7 1 2 ? parallel      
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC7 4 5 ? anti-parallel 
AC7 5 6 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AD1 1 2 ? anti-parallel 
AD1 2 3 ? 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 ALA A 9   ? SER A 12  ? ALA A 9   SER A 12  
AA1 2 ARG A 431 ? TYR A 435 ? ARG A 431 TYR A 435 
AA1 3 ASP A 421 ? ALA A 426 ? ASP A 421 ALA A 426 
AA1 4 MET A 408 ? THR A 412 ? MET A 408 THR A 412 
AA2 1 VAL A 23  ? PHE A 26  ? VAL A 23  PHE A 26  
AA2 2 PHE A 35  ? ALA A 40  ? PHE A 35  ALA A 40  
AA2 3 GLN A 55  ? ASP A 60  ? GLN A 55  ASP A 60  
AA2 4 CYS A 67  ? PRO A 69  ? CYS A 67  PRO A 69  
AA3 1 ASP A 79  ? ALA A 81  ? ASP A 79  ALA A 81  
AA3 2 ASP A 84  ? PRO A 85  ? ASP A 84  PRO A 85  
AA4 1 GLU A 87  ? PHE A 88  ? GLU A 87  PHE A 88  
AA4 2 HIS A 113 ? TRP A 114 ? HIS A 113 TRP A 114 
AA5 1 VAL A 98  ? LYS A 101 ? VAL A 98  LYS A 101 
AA5 2 LYS A 104 ? ALA A 109 ? LYS A 104 ALA A 109 
AA5 3 THR A 127 ? GLN A 131 ? THR A 127 GLN A 131 
AA5 4 THR A 136 ? TYR A 139 ? THR A 136 TYR A 139 
AA6 1 SER A 160 ? PHE A 163 ? SER A 160 PHE A 163 
AA6 2 ARG A 168 ? GLY A 173 ? ARG A 168 GLY A 173 
AA6 3 GLN A 182 ? GLN A 187 ? GLN A 182 GLN A 187 
AA6 4 LEU A 208 ? ALA A 209 ? LEU A 208 ALA A 209 
AA7 1 VAL A 226 ? GLY A 229 ? VAL A 226 GLY A 229 
AA7 2 ASP A 238 ? VAL A 243 ? ASP A 238 VAL A 243 
AA7 3 MET A 252 ? TYR A 256 ? MET A 252 TYR A 256 
AA7 4 SER A 263 ? THR A 268 ? SER A 263 THR A 268 
AA8 1 VAL A 280 ? THR A 283 ? VAL A 280 THR A 283 
AA8 2 ASP A 292 ? ALA A 297 ? ASP A 292 ALA A 297 
AA8 3 GLN A 314 ? GLN A 320 ? GLN A 314 GLN A 320 
AA8 4 PHE A 326 ? ASN A 332 ? PHE A 326 ASN A 332 
AA9 1 MET A 301 ? ARG A 303 ? MET A 301 ARG A 303 
AA9 2 LEU A 309 ? GLU A 311 ? LEU A 309 GLU A 311 
AB1 1 ILE A 344 ? GLY A 348 ? ILE A 344 GLY A 348 
AB1 2 ASP A 357 ? ALA A 362 ? ASP A 357 ALA A 362 
AB1 3 ILE A 372 ? ARG A 379 ? ILE A 372 ARG A 379 
AB1 4 GLY A 382 ? LEU A 383 ? GLY A 382 LEU A 383 
AB2 1 ILE A 344 ? GLY A 348 ? ILE A 344 GLY A 348 
AB2 2 ASP A 357 ? ALA A 362 ? ASP A 357 ALA A 362 
AB2 3 ILE A 372 ? ARG A 379 ? ILE A 372 ARG A 379 
AB2 4 GLN A 389 ? GLU A 392 ? GLN A 389 GLU A 392 
AB3 1 ALA A 511 ? PHE A 513 ? ALA A 511 PHE A 513 
AB3 2 GLN A 534 ? LEU A 542 ? GLN A 534 LEU A 542 
AB3 3 CYS A 472 ? GLY A 483 ? CYS A 472 GLY A 483 
AB3 4 VAL A 440 ? TYR A 450 ? VAL A 440 TYR A 450 
AB3 5 ILE A 577 ? LEU A 578 ? ILE A 577 LEU A 578 
AB4 1 ILE A 453 ? LEU A 454 ? ILE A 453 LEU A 454 
AB4 2 ASN A 585 ? ILE A 592 ? ASN A 585 ILE A 592 
AB4 3 ILE A 555 ? LEU A 563 ? ILE A 555 LEU A 563 
AB4 4 LEU A 491 ? LEU A 499 ? LEU A 491 LEU A 499 
AB4 5 SER A 520 ? ILE A 527 ? SER A 520 ILE A 527 
AB5 1 GLN B 60  ? LYS B 65  ? GLN B 64  LYS B 69  
AB5 2 SER B 87  ? LEU B 92  ? SER B 91  LEU B 96  
AB5 3 LEU B 423 ? PRO B 429 ? LEU B 427 PRO B 433 
AB5 4 ARG B 410 ? PRO B 416 ? ARG B 414 PRO B 420 
AB5 5 VAL B 354 ? GLY B 360 ? VAL B 358 GLY B 364 
AB5 6 LYS B 384 ? CYS B 385 ? LYS B 388 CYS B 389 
AB6 1 ILE B 83  ? ALA B 84  ? ILE B 87  ALA B 88  
AB6 2 ALA B 97  ? ARG B 105 ? ALA B 101 ARG B 109 
AB6 3 THR B 393 ? ASN B 401 ? THR B 397 ASN B 405 
AB6 4 ASN B 366 ? CYS B 373 ? ASN B 370 CYS B 377 
AB6 5 LEU B 378 ? GLN B 380 ? LEU B 382 GLN B 384 
AB7 1 PHE B 189 ? THR B 196 ? PHE B 193 THR B 200 
AB7 2 PHE B 149 ? PHE B 156 ? PHE B 153 PHE B 160 
AB7 3 VAL B 112 ? ASP B 119 ? VAL B 116 ASP B 123 
AB7 4 LEU B 242 ? SER B 249 ? LEU B 246 SER B 253 
AB7 5 LEU B 304 ? VAL B 309 ? LEU B 308 VAL B 313 
AB7 6 THR B 328 ? LEU B 331 ? THR B 332 LEU B 335 
AB8 1 GLY B 451 ? PHE B 453 ? GLY B 455 PHE B 457 
AB8 2 CYS B 458 ? CYS B 460 ? CYS B 462 CYS B 464 
AB9 1 HIS B 464 ? MET B 465 ? HIS B 468 MET B 469 
AB9 2 SER B 471 ? GLY B 472 ? SER B 475 GLY B 476 
AC1 1 MET C 4   ? THR C 5   ? MET C 4   THR C 5   
AC1 2 VAL C 19  ? ALA C 25  ? VAL C 19  ALA C 25  
AC1 3 ASP C 70  ? ILE C 75  ? ASP C 70  ILE C 75  
AC1 4 PHE C 62  ? SER C 67  ? PHE C 62  SER C 67  
AC2 1 SER C 10  ? ALA C 13  ? SER C 10  ALA C 13  
AC2 2 THR C 102 ? MET C 106 ? THR C 102 MET C 106 
AC2 3 THR C 85  ? GLN C 90  ? THR C 85  GLN C 90  
AC2 4 LEU C 33  ? GLN C 38  ? LEU C 33  GLN C 38  
AC2 5 VAL C 44  ? PHE C 49  ? VAL C 44  PHE C 49  
AC2 6 LYS C 53  ? LEU C 54  ? LYS C 53  LEU C 54  
AC3 1 SER C 10  ? ALA C 13  ? SER C 10  ALA C 13  
AC3 2 THR C 102 ? MET C 106 ? THR C 102 MET C 106 
AC3 3 THR C 85  ? GLN C 90  ? THR C 85  GLN C 90  
AC3 4 THR C 97  ? PHE C 98  ? THR C 97  PHE C 98  
AC4 1 THR C 114 ? PHE C 118 ? THR C 114 PHE C 118 
AC4 2 ALA C 130 ? PHE C 139 ? ALA C 130 PHE C 139 
AC4 3 TYR C 173 ? LEU C 181 ? TYR C 173 LEU C 181 
AC4 4 VAL C 159 ? TRP C 163 ? VAL C 159 TRP C 163 
AC5 1 ASN C 145 ? LYS C 149 ? ASN C 145 LYS C 149 
AC5 2 SER C 191 ? HIS C 198 ? SER C 191 HIS C 198 
AC5 3 SER C 201 ? ASN C 210 ? SER C 201 ASN C 210 
AC6 1 GLN D 3   ? GLN D 6   ? GLN D 3   GLN D 6   
AC6 2 SER D 17  ? SER D 25  ? SER D 17  SER D 25  
AC6 3 THR D 78  ? SER D 84  ? THR D 78  SER D 84  
AC6 4 ALA D 68  ? ASP D 73  ? ALA D 68  ASP D 73  
AC7 1 GLU D 10  ? ALA D 12  ? GLU D 10  ALA D 12  
AC7 2 THR D 112 ? VAL D 116 ? THR D 112 VAL D 116 
AC7 3 ALA D 92  ? SER D 98  ? ALA D 92  SER D 98  
AC7 4 MET D 34  ? GLN D 39  ? MET D 34  GLN D 39  
AC7 5 GLU D 46  ? ILE D 51  ? GLU D 46  ILE D 51  
AC7 6 THR D 58  ? CYS D 60  ? THR D 58  CYS D 60  
AC8 1 SER D 125 ? LEU D 129 ? SER D 125 LEU D 129 
AC8 2 SER D 140 ? TYR D 150 ? SER D 140 TYR D 150 
AC8 3 TYR D 180 ? VAL D 189 ? TYR D 180 VAL D 189 
AC8 4 VAL D 168 ? THR D 170 ? VAL D 168 THR D 170 
AC9 1 SER D 125 ? LEU D 129 ? SER D 125 LEU D 129 
AC9 2 SER D 140 ? TYR D 150 ? SER D 140 TYR D 150 
AC9 3 TYR D 180 ? VAL D 189 ? TYR D 180 VAL D 189 
AC9 4 VAL D 174 ? LEU D 175 ? VAL D 174 LEU D 175 
AD1 1 THR D 156 ? TRP D 159 ? THR D 156 TRP D 159 
AD1 2 ILE D 198 ? HIS D 204 ? ILE D 198 HIS D 204 
AD1 3 THR D 209 ? ILE D 215 ? THR D 209 ILE D 215 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 11  ? N TYR A 11  O ALA A 432 ? O ALA A 432 
AA1 2 3 O ILE A 433 ? O ILE A 433 N VAL A 424 ? N VAL A 424 
AA1 3 4 O ILE A 423 ? O ILE A 423 N LYS A 409 ? N LYS A 409 
AA2 1 2 N ASP A 24  ? N ASP A 24  O LEU A 37  ? O LEU A 37  
AA2 2 3 N ALA A 40  ? N ALA A 40  O GLN A 55  ? O GLN A 55  
AA2 3 4 N LYS A 58  ? N LYS A 58  O GLN A 68  ? O GLN A 68  
AA3 1 2 N TYR A 80  ? N TYR A 80  O ASP A 84  ? O ASP A 84  
AA4 1 2 N PHE A 88  ? N PHE A 88  O HIS A 113 ? O HIS A 113 
AA5 1 2 N ARG A 99  ? N ARG A 99  O LEU A 106 ? O LEU A 106 
AA5 2 3 N ALA A 109 ? N ALA A 109 O THR A 127 ? O THR A 127 
AA5 3 4 N CYS A 128 ? N CYS A 128 O TYR A 139 ? O TYR A 139 
AA6 1 2 N SER A 160 ? N SER A 160 O GLY A 172 ? O GLY A 172 
AA6 2 3 N VAL A 169 ? N VAL A 169 O ASP A 186 ? O ASP A 186 
AA6 3 4 N SER A 185 ? N SER A 185 O LEU A 208 ? O LEU A 208 
AA7 1 2 N ALA A 227 ? N ALA A 227 O VAL A 240 ? O VAL A 240 
AA7 2 3 N VAL A 243 ? N VAL A 243 O MET A 252 ? O MET A 252 
AA7 3 4 N ILE A 255 ? N ILE A 255 O LEU A 264 ? O LEU A 264 
AA8 1 2 N ALA A 281 ? N ALA A 281 O PHE A 294 ? O PHE A 294 
AA8 2 3 N VAL A 293 ? N VAL A 293 O SER A 318 ? O SER A 318 
AA8 3 4 N VAL A 317 ? N VAL A 317 O THR A 329 ? O THR A 329 
AA9 1 2 N ASP A 302 ? N ASP A 302 O GLN A 310 ? O GLN A 310 
AB1 1 2 N GLY A 348 ? N GLY A 348 O ASP A 357 ? O ASP A 357 
AB1 2 3 N ILE A 358 ? N ILE A 358 O PHE A 376 ? O PHE A 376 
AB1 3 4 N ARG A 379 ? N ARG A 379 O GLY A 382 ? O GLY A 382 
AB2 1 2 N GLY A 348 ? N GLY A 348 O ASP A 357 ? O ASP A 357 
AB2 2 3 N ILE A 358 ? N ILE A 358 O PHE A 376 ? O PHE A 376 
AB2 3 4 N VAL A 373 ? N VAL A 373 O LEU A 391 ? O LEU A 391 
AB3 1 2 N LEU A 512 ? N LEU A 512 O TYR A 541 ? O TYR A 541 
AB3 2 3 O GLU A 536 ? O GLU A 536 N PHE A 477 ? N PHE A 477 
AB3 3 4 O CYS A 478 ? O CYS A 478 N GLY A 446 ? N GLY A 446 
AB3 4 5 N ILE A 441 ? N ILE A 441 O ILE A 577 ? O ILE A 577 
AB4 1 2 N LEU A 454 ? N LEU A 454 O HIS A 591 ? O HIS A 591 
AB4 2 3 O ARG A 588 ? O ARG A 588 N ILE A 557 ? N ILE A 557 
AB4 3 4 O GLU A 560 ? O GLU A 560 N GLU A 496 ? N GLU A 496 
AB4 4 5 N PHE A 493 ? N PHE A 493 O MET A 525 ? O MET A 525 
AB5 1 2 N GLU B 62  ? N GLU B 66  O ILE B 89  ? O ILE B 93  
AB5 2 3 N LEU B 90  ? N LEU B 94  O SER B 428 ? O SER B 432 
AB5 3 4 O LEU B 425 ? O LEU B 429 N ILE B 412 ? N ILE B 416 
AB5 4 5 O ILE B 413 ? O ILE B 417 N LEU B 359 ? N LEU B 363 
AB5 5 6 N VAL B 354 ? N VAL B 358 O CYS B 385 ? O CYS B 389 
AB6 1 2 N ALA B 84  ? N ALA B 88  O HIS B 103 ? O HIS B 107 
AB6 2 3 N LEU B 100 ? N LEU B 104 O VAL B 398 ? O VAL B 402 
AB6 3 4 O SER B 395 ? O SER B 399 N ILE B 372 ? N ILE B 376 
AB6 4 5 N ALA B 371 ? N ALA B 375 O GLN B 380 ? O GLN B 384 
AB7 1 2 O LYS B 190 ? O LYS B 194 N SER B 155 ? N SER B 159 
AB7 2 3 O GLY B 152 ? O GLY B 156 N TYR B 116 ? N TYR B 120 
AB7 3 4 N ASP B 119 ? N ASP B 123 O VAL B 248 ? O VAL B 252 
AB7 4 5 N HIS B 243 ? N HIS B 247 O LEU B 304 ? O LEU B 308 
AB7 5 6 N PHE B 307 ? N PHE B 311 O GLY B 330 ? O GLY B 334 
AB8 1 2 N SER B 452 ? N SER B 456 O ALA B 459 ? O ALA B 463 
AB9 1 2 N MET B 465 ? N MET B 469 O SER B 471 ? O SER B 475 
AC1 1 2 N THR C 5   ? N THR C 5   O ARG C 24  ? O ARG C 24  
AC1 2 3 N VAL C 19  ? N VAL C 19  O ILE C 75  ? O ILE C 75  
AC1 3 4 O THR C 74  ? O THR C 74  N SER C 63  ? N SER C 63  
AC2 1 2 N LEU C 11  ? N LEU C 11  O LYS C 103 ? O LYS C 103 
AC2 2 3 O THR C 102 ? O THR C 102 N TYR C 86  ? N TYR C 86  
AC2 3 4 O THR C 85  ? O THR C 85  N GLN C 38  ? N GLN C 38  
AC2 4 5 N TRP C 35  ? N TRP C 35  O LEU C 47  ? O LEU C 47  
AC2 5 6 N PHE C 49  ? N PHE C 49  O LYS C 53  ? O LYS C 53  
AC3 1 2 N LEU C 11  ? N LEU C 11  O LYS C 103 ? O LYS C 103 
AC3 2 3 O THR C 102 ? O THR C 102 N TYR C 86  ? N TYR C 86  
AC3 3 4 N GLN C 90  ? N GLN C 90  O THR C 97  ? O THR C 97  
AC4 1 2 N PHE C 118 ? N PHE C 118 O VAL C 133 ? O VAL C 133 
AC4 2 3 N LEU C 136 ? N LEU C 136 O PHE C 175 ? O PHE C 175 
AC4 3 4 O THR C 178 ? O THR C 178 N LEU C 160 ? N LEU C 160 
AC5 1 2 N ASN C 145 ? N ASN C 145 O THR C 197 ? O THR C 197 
AC5 2 3 N ALA C 196 ? N ALA C 196 O ILE C 205 ? O ILE C 205 
AC6 1 2 N GLN D 5   ? N GLN D 5   O LYS D 23  ? O LYS D 23  
AC6 2 3 N MET D 20  ? N MET D 20  O MET D 81  ? O MET D 81  
AC6 3 4 O THR D 78  ? O THR D 78  N ASP D 73  ? N ASP D 73  
AC7 1 2 N GLU D 10  ? N GLU D 10  O SER D 113 ? O SER D 113 
AC7 2 3 O VAL D 114 ? O VAL D 114 N ALA D 92  ? N ALA D 92  
AC7 3 4 O ALA D 97  ? O ALA D 97  N HIS D 35  ? N HIS D 35  
AC7 4 5 N LYS D 38  ? N LYS D 38  O GLU D 46  ? O GLU D 46  
AC7 5 6 N TYR D 50  ? N TYR D 50  O GLU D 59  ? O GLU D 59  
AC8 1 2 N TYR D 127 ? N TYR D 127 O LEU D 146 ? O LEU D 146 
AC8 2 3 N VAL D 147 ? N VAL D 147 O LEU D 182 ? O LEU D 182 
AC8 3 4 O SER D 185 ? O SER D 185 N HIS D 169 ? N HIS D 169 
AC9 1 2 N TYR D 127 ? N TYR D 127 O LEU D 146 ? O LEU D 146 
AC9 2 3 N VAL D 147 ? N VAL D 147 O LEU D 182 ? O LEU D 182 
AC9 3 4 O THR D 181 ? O THR D 181 N VAL D 174 ? N VAL D 174 
AD1 1 2 N THR D 158 ? N THR D 158 O ASN D 201 ? O ASN D 201 
AD1 2 3 N VAL D 202 ? N VAL D 202 O VAL D 211 ? O VAL D 211 
# 
_pdbx_entry_details.entry_id                   9CZ7 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HG  C CYS 214 ? ? SG  D CYS 133  ? ? 1.10 
2 1 HG  A CYS 142 ? ? SG  A CYS 155  ? ? 1.29 
3 1 OD1 A ASN 377 ? ? HG  A SER 388  ? ? 1.51 
4 1 O   A ARG 115 ? ? HG1 A THR 116  ? ? 1.55 
5 1 OD1 B ASP 256 ? ? O   B HOH 2101 ? ? 2.15 
# 
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 SER A 62  ? ? 70.48   -33.52  
2  1 THR A 64  ? ? -152.28 -26.31  
3  1 GLN A 102 ? ? 57.05   -117.68 
4  1 THR A 116 ? ? 73.77   157.79  
5  1 MET A 118 ? ? -96.42  -79.07  
6  1 ARG A 122 ? ? -151.21 79.14   
7  1 ASP A 132 ? ? -94.78  -81.91  
8  1 SER A 144 ? ? -103.32 -165.29 
9  1 ASP A 148 ? ? 75.72   -179.77 
10 1 TYR A 221 ? ? 73.79   41.02   
11 1 ALA A 362 ? ? -116.41 79.86   
12 1 SER A 399 ? ? -127.70 -65.06  
13 1 LYS A 469 ? ? -150.68 85.05   
14 1 ARG A 489 ? ? -101.03 41.37   
15 1 LYS A 490 ? ? -170.93 136.86  
16 1 LYS A 523 ? ? -171.05 124.37  
17 1 LEU A 552 ? ? -94.69  -62.39  
18 1 GLU B 30  ? ? 32.93   51.94   
19 1 ASN B 60  ? ? -175.23 95.28   
20 1 ASN B 70  ? ? -143.74 56.96   
21 1 PRO B 89  ? ? -68.45  -178.21 
22 1 VAL B 161 ? ? -137.28 -74.74  
23 1 SER B 216 ? ? -118.70 -166.01 
24 1 ASN B 243 ? ? -54.69  175.80  
25 1 VAL B 269 ? ? -142.39 28.32   
26 1 HIS B 277 ? ? -144.22 55.59   
27 1 SER B 340 ? ? 59.79   17.50   
28 1 ASN B 379 ? ? 59.52   -130.62 
29 1 HIS B 385 ? ? -93.34  59.71   
30 1 HIS B 451 ? ? 47.39   78.95   
31 1 GLN B 458 ? ? -102.31 -60.43  
32 1 CYS B 459 ? ? -141.77 43.65   
33 1 THR C 51  ? ? 73.63   -44.39  
34 1 SER C 52  ? ? -145.66 15.88   
35 1 ASN C 138 ? ? 52.06   76.12   
36 1 ILE C 150 ? ? -98.21  -112.78 
37 1 ASN C 157 ? ? -122.16 -51.74  
38 1 CYS D 22  ? ? -166.75 96.80   
39 1 PRO D 131 ? ? -65.47  -179.70 
40 1 SER D 165 ? ? -120.29 -60.16  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 11.3160 -6.3423  -30.6992 0.7790 ? 0.1053  ? -0.2108 ? 0.4876 ? 0.1156  ? 0.7325 ? 6.2729 ? 
3.0549  ? 0.0072  ? 2.9701 ? 0.1743  ? 1.9414 ? -0.1431 ? 0.5824  ? 0.7971  ? -0.2190 ? -0.0455 ? 0.3537  ? -0.7960 ? -0.0398 ? 
0.1655  ? 
2  'X-RAY DIFFRACTION' ? refined 5.3537  -25.6875 -37.1898 0.4316 ? 0.0425  ? -0.0887 ? 0.4435 ? 0.0250  ? 0.4205 ? 3.4248 ? 
1.0743  ? 0.0558  ? 3.0994 ? 0.4129  ? 2.8174 ? -0.2528 ? 0.3514  ? 0.1646  ? -0.3190 ? 0.1361  ? 0.1784  ? -0.3028 ? -0.3087 ? 
0.1063  ? 
3  'X-RAY DIFFRACTION' ? refined 23.8004 -29.5572 -29.9903 0.3915 ? 0.0202  ? -0.0476 ? 0.4137 ? 0.0855  ? 0.4313 ? 2.1280 ? 
0.3151  ? 0.6870  ? 1.1590 ? 0.4334  ? 1.9215 ? -0.1077 ? 0.2330  ? 0.0827  ? -0.0815 ? -0.0619 ? -0.1436 ? -0.0173 ? 0.3714  ? 
0.1685  ? 
4  'X-RAY DIFFRACTION' ? refined 31.6628 -20.6727 -12.6477 0.4798 ? -0.0879 ? -0.1661 ? 0.5207 ? 0.0988  ? 0.5106 ? 3.1100 ? 
0.3229  ? -3.1216 ? 1.6304 ? -0.9757 ? 8.6576 ? -0.2740 ? -0.6528 ? -0.2119 ? 0.2997  ? -0.1514 ? -0.1725 ? -0.0985 ? 1.1771  ? 
0.3712  ? 
5  'X-RAY DIFFRACTION' ? refined 25.0798 -8.5465  -17.5724 0.6439 ? -0.0668 ? -0.1806 ? 0.4306 ? 0.1039  ? 0.5330 ? 7.6489 ? 
1.1590  ? -2.7818 ? 3.1811 ? -0.3582 ? 4.6952 ? 0.0188  ? -0.1689 ? 0.6462  ? 0.2135  ? -0.1529 ? -0.0960 ? -0.7467 ? 0.3138  ? 
0.1244  ? 
6  'X-RAY DIFFRACTION' ? refined 35.8334 5.1167   -20.0838 0.7450 ? -0.0251 ? -0.1458 ? 0.4131 ? 0.0661  ? 0.8159 ? 4.3494 ? 
1.0328  ? 0.7927  ? 1.2680 ? 0.4894  ? 0.7891 ? -0.2371 ? 0.0640  ? 0.8627  ? -0.1082 ? 0.1379  ? 0.0215  ? -0.1665 ? 0.1965  ? 
0.2084  ? 
7  'X-RAY DIFFRACTION' ? refined 48.1938 20.7470  -11.2039 0.7492 ? -0.0185 ? -0.1136 ? 0.6171 ? -0.0374 ? 1.0885 ? 4.6269 ? 
0.7421  ? 2.6030  ? 4.1494 ? 2.4423  ? 8.8850 ? -0.4223 ? -0.1827 ? 1.2372  ? -0.1764 ? 0.4263  ? -0.0556 ? -0.7727 ? 0.0001  ? 
0.0297  ? 
8  'X-RAY DIFFRACTION' ? refined 47.8746 14.9942  -8.9617  0.7988 ? 0.0407  ? -0.0153 ? 0.8390 ? -0.1245 ? 0.9391 ? 3.7291 ? 
1.8189  ? 4.4532  ? 2.9315 ? 0.5808  ? 6.1691 ? -0.4453 ? -0.9860 ? 0.7794  ? -0.3218 ? 0.2560  ? 0.0867  ? -0.4541 ? -0.7433 ? 
0.3012  ? 
9  'X-RAY DIFFRACTION' ? refined 39.6489 -6.5584  24.9956  0.9472 ? 0.0644  ? -0.2894 ? 0.7023 ? 0.0028  ? 0.8933 ? 3.8430 ? 
2.9783  ? -0.4484 ? 6.6101 ? -1.3185 ? 2.2591 ? 0.1228  ? -0.4175 ? 0.5079  ? 0.9199  ? -0.4536 ? -0.9795 ? -0.8288 ? 0.1334  ? 
0.2628  ? 
10 'X-RAY DIFFRACTION' ? refined 6.0720  -39.0827 2.9842   0.3849 ? 0.0396  ? 0.0873  ? 0.4470 ? 0.0401  ? 0.4568 ? 1.9673 ? 
0.5091  ? 0.9829  ? 1.1095 ? 0.2802  ? 2.0603 ? 0.0664  ? -0.4520 ? -0.1638 ? 0.1441  ? -0.0636 ? 0.1596  ? 0.3190  ? -0.5214 ? 
-0.0119 ? 
11 'X-RAY DIFFRACTION' ? refined 11.4209 -34.8589 -0.9701  0.3095 ? -0.0053 ? -0.0032 ? 0.3873 ? 0.0311  ? 0.4033 ? 1.7251 ? 
-0.3769 ? 0.3914  ? 2.4378 ? -1.3331 ? 4.4184 ? 0.0258  ? -0.2681 ? -0.0409 ? 0.0803  ? -0.0357 ? 0.0789  ? -0.0549 ? -0.0935 ? 
0.0156  ? 
12 'X-RAY DIFFRACTION' ? refined 28.9474 -27.1801 14.6820  0.4463 ? 0.0747  ? -0.0177 ? 0.6104 ? -0.1423 ? 0.4561 ? 6.4433 ? 
4.4286  ? -2.3375 ? 8.8788 ? -2.3411 ? 5.8733 ? -0.1682 ? 0.0784  ? -0.4552 ? -0.0358 ? 0.3139  ? -0.5264 ? 0.0043  ? -0.0812 ? 
-0.1551 ? 
13 'X-RAY DIFFRACTION' ? refined 28.4286 -20.9036 17.9892  0.5778 ? 0.1603  ? 0.0358  ? 0.7245 ? -0.0257 ? 0.4392 ? 5.6790 ? 
4.3949  ? 0.1580  ? 6.7473 ? 0.1010  ? 2.1906 ? -0.0456 ? 0.1217  ? 0.2400  ? -0.1251 ? 0.0160  ? -0.0701 ? -0.3167 ? -0.1551 ? 
0.0712  ? 
14 'X-RAY DIFFRACTION' ? refined 42.4467 19.3607  19.4730  1.0602 ? 0.0579  ? -0.2004 ? 0.9894 ? -0.2344 ? 1.2665 ? 5.8573 ? 
-1.4317 ? -1.9931 ? 6.6780 ? -2.4976 ? 5.0714 ? 0.4557  ? -0.1001 ? -0.0445 ? 0.3470  ? 0.0657  ? -0.0778 ? -0.7192 ? 0.4992  ? 
-0.5322 ? 
15 'X-RAY DIFFRACTION' ? refined -7.0112 -45.7720 -63.1112 0.8276 ? -0.0237 ? -0.1534 ? 0.8867 ? -0.1955 ? 0.7547 ? 2.2283 ? 
-0.6543 ? -2.8988 ? 0.7492 ? 0.5662  ? 8.0669 ? -0.1469 ? 0.7381  ? -0.3075 ? -0.4906 ? -0.3914 ? 0.4466  ? 0.3720  ? -1.6402 ? 
0.5437  ? 
16 'X-RAY DIFFRACTION' ? refined 1.1147  -40.0921 -61.1421 0.6150 ? 0.0810  ? -0.1431 ? 0.5714 ? -0.0364 ? 0.4460 ? 4.4646 ? 
-1.4360 ? -0.2429 ? 5.2670 ? 1.2634  ? 7.3904 ? -0.0457 ? 0.8132  ? 0.1552  ? -0.7271 ? -0.2969 ? 0.4061  ? -0.4319 ? -0.3369 ? 
0.3637  ? 
17 'X-RAY DIFFRACTION' ? refined 0.7500  -45.7758 -61.4867 0.5772 ? 0.0635  ? -0.0927 ? 0.6046 ? -0.0411 ? 0.6013 ? 2.5300 ? 
-0.9746 ? 0.9741  ? 3.5511 ? -0.2938 ? 7.1903 ? 0.2120  ? 0.3789  ? 0.2657  ? -0.4267 ? -0.5891 ? 0.0732  ? 0.1819  ? 0.0983  ? 
0.3157  ? 
18 'X-RAY DIFFRACTION' ? refined 1.3815  -49.8572 -81.8912 1.1841 ? 0.2439  ? -0.2646 ? 0.7845 ? -0.0847 ? 0.6839 ? 0.1126 ? 
-0.8064 ? -1.0389 ? 3.4961 ? 4.9406  ? 6.9530 ? 0.8199  ? 0.5918  ? -0.5900 ? -1.2277 ? -0.4038 ? 0.2083  ? 0.5616  ? -0.6380 ? 
-0.3733 ? 
19 'X-RAY DIFFRACTION' ? refined 14.6899 -72.0574 -86.3811 0.8362 ? 0.0608  ? -0.0655 ? 0.9429 ? -0.1999 ? 0.7176 ? 3.9743 ? 
-4.0392 ? -2.8067 ? 7.3928 ? 3.2555  ? 2.1258 ? 0.2397  ? 0.8909  ? -0.5335 ? -0.3406 ? -0.7158 ? 0.5180  ? -0.1706 ? -0.8030 ? 
0.3938  ? 
20 'X-RAY DIFFRACTION' ? refined 0.9828  -71.4992 -84.3997 0.6307 ? 0.0379  ? -0.0881 ? 1.0967 ? -0.4550 ? 1.5204 ? 4.5593 ? 
-0.8188 ? -0.2572 ? 2.7281 ? -2.5881 ? 2.6833 ? -0.2999 ? 0.8384  ? -0.8863 ? 0.0633  ? 0.1257  ? 2.4589  ? 0.3669  ? -0.9598 ? 
0.3165  ? 
21 'X-RAY DIFFRACTION' ? refined 8.7292  -61.7479 -80.5101 0.6375 ? 0.0629  ? -0.0178 ? 0.8358 ? -0.1031 ? 0.5800 ? 6.7308 ? 
-2.5359 ? 0.4051  ? 9.5658 ? 2.8544  ? 5.8245 ? -0.4948 ? 0.6483  ? -0.6076 ? 0.6773  ? 0.5787  ? 0.6322  ? -0.6035 ? 0.1387  ? 
-0.1020 ? 
22 'X-RAY DIFFRACTION' ? refined 8.4794  -81.9616 -88.1701 0.9587 ? 0.1996  ? -0.1789 ? 1.1038 ? -0.5533 ? 1.4159 ? 9.4202 ? 
-7.1064 ? 7.1980  ? 7.4747 ? -7.6465 ? 7.7793 ? -0.1029 ? 0.2002  ? -1.5323 ? -0.1815 ? 0.0257  ? 1.8431  ? 0.0380  ? -0.8936 ? 
0.2309  ? 
23 'X-RAY DIFFRACTION' ? refined 4.7965  -70.8784 -94.3216 1.2756 ? 0.1446  ? -0.3050 ? 1.3109 ? -0.5624 ? 1.2688 ? 4.3649 ? 
-0.4506 ? 3.7858  ? 7.3623 ? -2.2391 ? 6.1348 ? 1.5016  ? 1.0375  ? -1.5717 ? -2.9496 ? -1.4534 ? 1.8241  ? 0.3720  ? -0.6113 ? 
0.1220  ? 
24 'X-RAY DIFFRACTION' ? refined 18.7776 -57.4935 -54.2969 0.6705 ? 0.1952  ? -0.0891 ? 0.7005 ? -0.0217 ? 0.5272 ? 4.6465 ? 
1.5096  ? -0.7309 ? 2.0162 ? -0.3873 ? 5.6838 ? 0.1758  ? -0.1732 ? -0.6987 ? -0.3107 ? -0.2707 ? -0.9224 ? 0.8495  ? 0.8191  ? 
0.0710  ? 
25 'X-RAY DIFFRACTION' ? refined 12.7360 -51.8792 -50.2197 0.6658 ? 0.1045  ? -0.0594 ? 0.4784 ? -0.0198 ? 0.4213 ? 4.5734 ? 
-0.6304 ? -1.2700 ? 2.3980 ? 0.8368  ? 4.1772 ? 0.1869  ? 0.3632  ? -0.5286 ? -0.0927 ? -0.1908 ? -0.1724 ? 0.9506  ? 0.1916  ? 
0.0238  ? 
26 'X-RAY DIFFRACTION' ? refined 5.3154  -55.7732 -43.8020 0.7498 ? -0.0218 ? 0.0789  ? 0.5537 ? -0.0032 ? 0.6728 ? 3.1875 ? 
-0.8420 ? 5.2019  ? 6.7256 ? 1.2161  ? 9.7050 ? 0.2230  ? -0.5068 ? -0.9352 ? 0.9735  ? 0.2154  ? 0.7303  ? 1.3368  ? -0.5569 ? 
-0.3171 ? 
27 'X-RAY DIFFRACTION' ? refined 16.9775 -55.7167 -43.7706 0.8261 ? 0.2300  ? -0.1534 ? 0.5691 ? -0.1195 ? 0.5181 ? 6.7062 ? 
0.8795  ? -2.9648 ? 8.9619 ? -2.8151 ? 4.9045 ? -0.2258 ? 0.1382  ? -0.1714 ? -0.2670 ? 0.2389  ? -0.2375 ? 0.9639  ? 0.3633  ? 
-0.0963 ? 
28 'X-RAY DIFFRACTION' ? refined 9.0906  -52.7113 -53.5418 0.6190 ? 0.0135  ? -0.0588 ? 0.5600 ? -0.0971 ? 0.5137 ? 2.5020 ? 
-3.1920 ? 0.6440  ? 6.0294 ? -1.6123 ? 3.1896 ? 0.2204  ? 0.0474  ? -0.2804 ? -0.6997 ? -0.3672 ? 0.5107  ? 0.6607  ? 0.0115  ? 
0.1878  ? 
29 'X-RAY DIFFRACTION' ? refined 19.1980 -70.9505 -61.5189 0.9617 ? 0.1348  ? -0.1265 ? 0.6739 ? -0.0293 ? 0.7935 ? 4.6679 ? 
-3.0500 ? -4.3890 ? 7.2724 ? 7.1466  ? 7.5788 ? 0.1830  ? 0.2116  ? -0.1430 ? 0.4837  ? -0.0374 ? -0.7794 ? 0.1376  ? -0.6139 ? 
-0.1475 ? 
30 'X-RAY DIFFRACTION' ? refined 21.6120 -67.4409 -81.9171 0.5596 ? 0.1597  ? -0.0406 ? 0.7050 ? -0.0582 ? 0.5980 ? 6.5376 ? 
-1.0937 ? -0.4629 ? 8.3381 ? -2.8808 ? 8.0316 ? -0.0435 ? 0.6875  ? 0.0014  ? -0.0272 ? -0.1477 ? -0.1796 ? 0.3629  ? 0.6529  ? 
0.1047  ? 
31 'X-RAY DIFFRACTION' ? refined 16.6036 -63.6541 -77.9675 1.1174 ? 0.0747  ? -0.0614 ? 0.7945 ? -0.0166 ? 0.8885 ? 5.5303 ? 
0.2950  ? -4.6833 ? 2.0743 ? -0.9753 ? 6.6249 ? -0.8604 ? 0.0069  ? -0.9117 ? 0.0071  ? -0.2704 ? -1.0300 ? 0.5582  ? -0.0153 ? 
0.9420  ? 
32 'X-RAY DIFFRACTION' ? refined 19.3119 -64.1916 -84.4416 0.8216 ? 0.0058  ? 0.0164  ? 0.8036 ? -0.1425 ? 0.7090 ? 5.9321 ? 
-2.2405 ? 3.1605  ? 5.0780 ? -2.3723 ? 2.2345 ? 0.0071  ? 1.0336  ? -0.0107 ? -0.1921 ? 0.1487  ? -0.5195 ? -0.2335 ? -0.4113 ? 
-0.0650 ? 
33 'X-RAY DIFFRACTION' ? refined 28.8421 -67.1302 -83.2270 0.7449 ? 0.0701  ? 0.1419  ? 0.7782 ? 0.0406  ? 0.9069 ? 7.0185 ? 
-1.6087 ? 0.9230  ? 7.3526 ? 0.3769  ? 7.2068 ? 0.0809  ? 0.8775  ? 0.2098  ? -0.3575 ? -0.0510 ? -0.9982 ? -0.4626 ? 0.4601  ? 
0.0977  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 66 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 67 through 149 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 150 through 303 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 304 through 342 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 343 through 407 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 408 through 460 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 461 through 533 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 534 through 595 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 5 through 80 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 81 through 224 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 225 through 356 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 357 through 380 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 381 through 441 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 442 through 477 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 1 through 32 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 33 through 75 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 76 through 101 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 102 through 113 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 114 through 139 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 140 through 158 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 159 through 181 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 182 through 197 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 198 through 214 )
;
24 'X-RAY DIFFRACTION' 24 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 16 )
;
25 'X-RAY DIFFRACTION' 25 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 17 through 44 )
;
26 'X-RAY DIFFRACTION' 26 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 45 through 67 )
;
27 'X-RAY DIFFRACTION' 27 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 68 through 84 )
;
28 'X-RAY DIFFRACTION' 28 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 85 through 111 )
;
29 'X-RAY DIFFRACTION' 29 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 112 through 124 )
;
30 'X-RAY DIFFRACTION' 30 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 125 through 162 )
;
31 'X-RAY DIFFRACTION' 31 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 163 through 178 )
;
32 'X-RAY DIFFRACTION' 32 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 179 through 192 )
;
33 'X-RAY DIFFRACTION' 33 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 193 through 217 )
;
# 
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 GLY 596 ? A GLY 596 
2  1 Y 1 A GLY 597 ? A GLY 597 
3  1 Y 1 A SER 598 ? A SER 598 
4  1 Y 1 A LEU 599 ? A LEU 599 
5  1 Y 1 A GLU 600 ? A GLU 600 
6  1 Y 1 A VAL 601 ? A VAL 601 
7  1 Y 1 A LEU 602 ? A LEU 602 
8  1 Y 1 A PHE 603 ? A PHE 603 
9  1 Y 1 A GLN 604 ? A GLN 604 
10 1 Y 1 A GLY 605 ? A GLY 605 
11 1 Y 1 B PHE 32  ? B PHE 28  
12 1 Y 1 B THR 33  ? B THR 29  
13 1 Y 1 B HIS 34  ? B HIS 30  
14 1 Y 1 B PRO 35  ? B PRO 31  
15 1 Y 1 B SER 36  ? B SER 32  
16 1 Y 1 B GLY 37  ? B GLY 33  
17 1 Y 1 B VAL 38  ? B VAL 34  
18 1 Y 1 B SER 478 ? B SER 474 
19 1 Y 1 B LEU 479 ? B LEU 475 
20 1 Y 1 B GLU 480 ? B GLU 476 
21 1 Y 1 B VAL 481 ? B VAL 477 
22 1 Y 1 B LEU 482 ? B LEU 478 
23 1 Y 1 B PHE 483 ? B PHE 479 
24 1 Y 1 B GLN 484 ? B GLN 480 
25 1 Y 1 B GLY 485 ? B GLY 481 
26 1 Y 1 D GLY 134 ? D GLY 134 
27 1 Y 1 D ASP 135 ? D ASP 135 
28 1 Y 1 D THR 136 ? D THR 136 
29 1 Y 1 D THR 137 ? D THR 137 
30 1 Y 1 D ARG 218 ? D ARG 218 
# 
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 
A1A6A C15  C  Y N 1   
A1A6A C17  C  Y N 2   
A1A6A C18  C  Y N 3   
A1A6A C19  C  N N 4   
A1A6A C21  C  N N 5   
A1A6A C20  C  N N 6   
A1A6A C13  C  N N 7   
A1A6A C14  C  N N 8   
A1A6A C12  C  N N 9   
A1A6A C11  C  N N 10  
A1A6A C23  C  Y N 11  
A1A6A C02  C  N N 12  
A1A6A C04  C  N S 13  
A1A6A C06  C  N N 14  
A1A6A C07  C  N N 15  
A1A6A C08  C  N R 16  
A1A6A C09  C  N N 17  
A1A6A C24  C  Y N 18  
A1A6A C25  C  Y N 19  
A1A6A C26  C  Y N 20  
A1A6A C27  C  Y N 21  
A1A6A C28  C  Y N 22  
A1A6A C29  C  Y N 23  
A1A6A C30  C  Y N 24  
A1A6A N05  N  N N 25  
A1A6A N16  N  Y N 26  
A1A6A N22  N  N N 27  
A1A6A O01  O  N N 28  
A1A6A O03  O  N N 29  
A1A6A O10  O  N N 30  
A1A6A H192 H  N N 31  
A1A6A H191 H  N N 32  
A1A6A H211 H  N N 33  
A1A6A H212 H  N N 34  
A1A6A H201 H  N N 35  
A1A6A H202 H  N N 36  
A1A6A H131 H  N N 37  
A1A6A H132 H  N N 38  
A1A6A H142 H  N N 39  
A1A6A H141 H  N N 40  
A1A6A H122 H  N N 41  
A1A6A H121 H  N N 42  
A1A6A H111 H  N N 43  
A1A6A H112 H  N N 44  
A1A6A H231 H  N N 45  
A1A6A H041 H  N N 46  
A1A6A H061 H  N N 47  
A1A6A H062 H  N N 48  
A1A6A H072 H  N N 49  
A1A6A H071 H  N N 50  
A1A6A H081 H  N N 51  
A1A6A H092 H  N N 52  
A1A6A H091 H  N N 53  
A1A6A H241 H  N N 54  
A1A6A H261 H  N N 55  
A1A6A H271 H  N N 56  
A1A6A H281 H  N N 57  
A1A6A H291 H  N N 58  
A1A6A H301 H  N N 59  
A1A6A H221 H  N N 60  
A1A6A H1   H  N N 61  
ACT   C    C  N N 62  
ACT   O    O  N N 63  
ACT   OXT  O  N N 64  
ACT   CH3  C  N N 65  
ACT   H1   H  N N 66  
ACT   H2   H  N N 67  
ACT   H3   H  N N 68  
ALA   N    N  N N 69  
ALA   CA   C  N S 70  
ALA   C    C  N N 71  
ALA   O    O  N N 72  
ALA   CB   C  N N 73  
ALA   OXT  O  N N 74  
ALA   H    H  N N 75  
ALA   H2   H  N N 76  
ALA   HA   H  N N 77  
ALA   HB1  H  N N 78  
ALA   HB2  H  N N 79  
ALA   HB3  H  N N 80  
ALA   HXT  H  N N 81  
ARG   N    N  N N 82  
ARG   CA   C  N S 83  
ARG   C    C  N N 84  
ARG   O    O  N N 85  
ARG   CB   C  N N 86  
ARG   CG   C  N N 87  
ARG   CD   C  N N 88  
ARG   NE   N  N N 89  
ARG   CZ   C  N N 90  
ARG   NH1  N  N N 91  
ARG   NH2  N  N N 92  
ARG   OXT  O  N N 93  
ARG   H    H  N N 94  
ARG   H2   H  N N 95  
ARG   HA   H  N N 96  
ARG   HB2  H  N N 97  
ARG   HB3  H  N N 98  
ARG   HG2  H  N N 99  
ARG   HG3  H  N N 100 
ARG   HD2  H  N N 101 
ARG   HD3  H  N N 102 
ARG   HE   H  N N 103 
ARG   HH11 H  N N 104 
ARG   HH12 H  N N 105 
ARG   HH21 H  N N 106 
ARG   HH22 H  N N 107 
ARG   HXT  H  N N 108 
ASN   N    N  N N 109 
ASN   CA   C  N S 110 
ASN   C    C  N N 111 
ASN   O    O  N N 112 
ASN   CB   C  N N 113 
ASN   CG   C  N N 114 
ASN   OD1  O  N N 115 
ASN   ND2  N  N N 116 
ASN   OXT  O  N N 117 
ASN   H    H  N N 118 
ASN   H2   H  N N 119 
ASN   HA   H  N N 120 
ASN   HB2  H  N N 121 
ASN   HB3  H  N N 122 
ASN   HD21 H  N N 123 
ASN   HD22 H  N N 124 
ASN   HXT  H  N N 125 
ASP   N    N  N N 126 
ASP   CA   C  N S 127 
ASP   C    C  N N 128 
ASP   O    O  N N 129 
ASP   CB   C  N N 130 
ASP   CG   C  N N 131 
ASP   OD1  O  N N 132 
ASP   OD2  O  N N 133 
ASP   OXT  O  N N 134 
ASP   H    H  N N 135 
ASP   H2   H  N N 136 
ASP   HA   H  N N 137 
ASP   HB2  H  N N 138 
ASP   HB3  H  N N 139 
ASP   HD2  H  N N 140 
ASP   HXT  H  N N 141 
BMA   C1   C  N R 142 
BMA   C2   C  N S 143 
BMA   C3   C  N S 144 
BMA   C4   C  N S 145 
BMA   C5   C  N R 146 
BMA   C6   C  N N 147 
BMA   O1   O  N N 148 
BMA   O2   O  N N 149 
BMA   O3   O  N N 150 
BMA   O4   O  N N 151 
BMA   O5   O  N N 152 
BMA   O6   O  N N 153 
BMA   H1   H  N N 154 
BMA   H2   H  N N 155 
BMA   H3   H  N N 156 
BMA   H4   H  N N 157 
BMA   H5   H  N N 158 
BMA   H61  H  N N 159 
BMA   H62  H  N N 160 
BMA   HO1  H  N N 161 
BMA   HO2  H  N N 162 
BMA   HO3  H  N N 163 
BMA   HO4  H  N N 164 
BMA   HO6  H  N N 165 
CA    CA   CA N N 166 
CYS   N    N  N N 167 
CYS   CA   C  N R 168 
CYS   C    C  N N 169 
CYS   O    O  N N 170 
CYS   CB   C  N N 171 
CYS   SG   S  N N 172 
CYS   OXT  O  N N 173 
CYS   H    H  N N 174 
CYS   H2   H  N N 175 
CYS   HA   H  N N 176 
CYS   HB2  H  N N 177 
CYS   HB3  H  N N 178 
CYS   HG   H  N N 179 
CYS   HXT  H  N N 180 
GLN   N    N  N N 181 
GLN   CA   C  N S 182 
GLN   C    C  N N 183 
GLN   O    O  N N 184 
GLN   CB   C  N N 185 
GLN   CG   C  N N 186 
GLN   CD   C  N N 187 
GLN   OE1  O  N N 188 
GLN   NE2  N  N N 189 
GLN   OXT  O  N N 190 
GLN   H    H  N N 191 
GLN   H2   H  N N 192 
GLN   HA   H  N N 193 
GLN   HB2  H  N N 194 
GLN   HB3  H  N N 195 
GLN   HG2  H  N N 196 
GLN   HG3  H  N N 197 
GLN   HE21 H  N N 198 
GLN   HE22 H  N N 199 
GLN   HXT  H  N N 200 
GLU   N    N  N N 201 
GLU   CA   C  N S 202 
GLU   C    C  N N 203 
GLU   O    O  N N 204 
GLU   CB   C  N N 205 
GLU   CG   C  N N 206 
GLU   CD   C  N N 207 
GLU   OE1  O  N N 208 
GLU   OE2  O  N N 209 
GLU   OXT  O  N N 210 
GLU   H    H  N N 211 
GLU   H2   H  N N 212 
GLU   HA   H  N N 213 
GLU   HB2  H  N N 214 
GLU   HB3  H  N N 215 
GLU   HG2  H  N N 216 
GLU   HG3  H  N N 217 
GLU   HE2  H  N N 218 
GLU   HXT  H  N N 219 
GLY   N    N  N N 220 
GLY   CA   C  N N 221 
GLY   C    C  N N 222 
GLY   O    O  N N 223 
GLY   OXT  O  N N 224 
GLY   H    H  N N 225 
GLY   H2   H  N N 226 
GLY   HA2  H  N N 227 
GLY   HA3  H  N N 228 
GLY   HXT  H  N N 229 
GOL   C1   C  N N 230 
GOL   O1   O  N N 231 
GOL   C2   C  N N 232 
GOL   O2   O  N N 233 
GOL   C3   C  N N 234 
GOL   O3   O  N N 235 
GOL   H11  H  N N 236 
GOL   H12  H  N N 237 
GOL   HO1  H  N N 238 
GOL   H2   H  N N 239 
GOL   HO2  H  N N 240 
GOL   H31  H  N N 241 
GOL   H32  H  N N 242 
GOL   HO3  H  N N 243 
HIS   N    N  N N 244 
HIS   CA   C  N S 245 
HIS   C    C  N N 246 
HIS   O    O  N N 247 
HIS   CB   C  N N 248 
HIS   CG   C  Y N 249 
HIS   ND1  N  Y N 250 
HIS   CD2  C  Y N 251 
HIS   CE1  C  Y N 252 
HIS   NE2  N  Y N 253 
HIS   OXT  O  N N 254 
HIS   H    H  N N 255 
HIS   H2   H  N N 256 
HIS   HA   H  N N 257 
HIS   HB2  H  N N 258 
HIS   HB3  H  N N 259 
HIS   HD1  H  N N 260 
HIS   HD2  H  N N 261 
HIS   HE1  H  N N 262 
HIS   HE2  H  N N 263 
HIS   HXT  H  N N 264 
HOH   O    O  N N 265 
HOH   H1   H  N N 266 
HOH   H2   H  N N 267 
ILE   N    N  N N 268 
ILE   CA   C  N S 269 
ILE   C    C  N N 270 
ILE   O    O  N N 271 
ILE   CB   C  N S 272 
ILE   CG1  C  N N 273 
ILE   CG2  C  N N 274 
ILE   CD1  C  N N 275 
ILE   OXT  O  N N 276 
ILE   H    H  N N 277 
ILE   H2   H  N N 278 
ILE   HA   H  N N 279 
ILE   HB   H  N N 280 
ILE   HG12 H  N N 281 
ILE   HG13 H  N N 282 
ILE   HG21 H  N N 283 
ILE   HG22 H  N N 284 
ILE   HG23 H  N N 285 
ILE   HD11 H  N N 286 
ILE   HD12 H  N N 287 
ILE   HD13 H  N N 288 
ILE   HXT  H  N N 289 
LEU   N    N  N N 290 
LEU   CA   C  N S 291 
LEU   C    C  N N 292 
LEU   O    O  N N 293 
LEU   CB   C  N N 294 
LEU   CG   C  N N 295 
LEU   CD1  C  N N 296 
LEU   CD2  C  N N 297 
LEU   OXT  O  N N 298 
LEU   H    H  N N 299 
LEU   H2   H  N N 300 
LEU   HA   H  N N 301 
LEU   HB2  H  N N 302 
LEU   HB3  H  N N 303 
LEU   HG   H  N N 304 
LEU   HD11 H  N N 305 
LEU   HD12 H  N N 306 
LEU   HD13 H  N N 307 
LEU   HD21 H  N N 308 
LEU   HD22 H  N N 309 
LEU   HD23 H  N N 310 
LEU   HXT  H  N N 311 
LYS   N    N  N N 312 
LYS   CA   C  N S 313 
LYS   C    C  N N 314 
LYS   O    O  N N 315 
LYS   CB   C  N N 316 
LYS   CG   C  N N 317 
LYS   CD   C  N N 318 
LYS   CE   C  N N 319 
LYS   NZ   N  N N 320 
LYS   OXT  O  N N 321 
LYS   H    H  N N 322 
LYS   H2   H  N N 323 
LYS   HA   H  N N 324 
LYS   HB2  H  N N 325 
LYS   HB3  H  N N 326 
LYS   HG2  H  N N 327 
LYS   HG3  H  N N 328 
LYS   HD2  H  N N 329 
LYS   HD3  H  N N 330 
LYS   HE2  H  N N 331 
LYS   HE3  H  N N 332 
LYS   HZ1  H  N N 333 
LYS   HZ2  H  N N 334 
LYS   HZ3  H  N N 335 
LYS   HXT  H  N N 336 
MAN   C1   C  N S 337 
MAN   C2   C  N S 338 
MAN   C3   C  N S 339 
MAN   C4   C  N S 340 
MAN   C5   C  N R 341 
MAN   C6   C  N N 342 
MAN   O1   O  N N 343 
MAN   O2   O  N N 344 
MAN   O3   O  N N 345 
MAN   O4   O  N N 346 
MAN   O5   O  N N 347 
MAN   O6   O  N N 348 
MAN   H1   H  N N 349 
MAN   H2   H  N N 350 
MAN   H3   H  N N 351 
MAN   H4   H  N N 352 
MAN   H5   H  N N 353 
MAN   H61  H  N N 354 
MAN   H62  H  N N 355 
MAN   HO1  H  N N 356 
MAN   HO2  H  N N 357 
MAN   HO3  H  N N 358 
MAN   HO4  H  N N 359 
MAN   HO6  H  N N 360 
MET   N    N  N N 361 
MET   CA   C  N S 362 
MET   C    C  N N 363 
MET   O    O  N N 364 
MET   CB   C  N N 365 
MET   CG   C  N N 366 
MET   SD   S  N N 367 
MET   CE   C  N N 368 
MET   OXT  O  N N 369 
MET   H    H  N N 370 
MET   H2   H  N N 371 
MET   HA   H  N N 372 
MET   HB2  H  N N 373 
MET   HB3  H  N N 374 
MET   HG2  H  N N 375 
MET   HG3  H  N N 376 
MET   HE1  H  N N 377 
MET   HE2  H  N N 378 
MET   HE3  H  N N 379 
MET   HXT  H  N N 380 
MG    MG   MG N N 381 
NAG   C1   C  N R 382 
NAG   C2   C  N R 383 
NAG   C3   C  N R 384 
NAG   C4   C  N S 385 
NAG   C5   C  N R 386 
NAG   C6   C  N N 387 
NAG   C7   C  N N 388 
NAG   C8   C  N N 389 
NAG   N2   N  N N 390 
NAG   O1   O  N N 391 
NAG   O3   O  N N 392 
NAG   O4   O  N N 393 
NAG   O5   O  N N 394 
NAG   O6   O  N N 395 
NAG   O7   O  N N 396 
NAG   H1   H  N N 397 
NAG   H2   H  N N 398 
NAG   H3   H  N N 399 
NAG   H4   H  N N 400 
NAG   H5   H  N N 401 
NAG   H61  H  N N 402 
NAG   H62  H  N N 403 
NAG   H81  H  N N 404 
NAG   H82  H  N N 405 
NAG   H83  H  N N 406 
NAG   HN2  H  N N 407 
NAG   HO1  H  N N 408 
NAG   HO3  H  N N 409 
NAG   HO4  H  N N 410 
NAG   HO6  H  N N 411 
PHE   N    N  N N 412 
PHE   CA   C  N S 413 
PHE   C    C  N N 414 
PHE   O    O  N N 415 
PHE   CB   C  N N 416 
PHE   CG   C  Y N 417 
PHE   CD1  C  Y N 418 
PHE   CD2  C  Y N 419 
PHE   CE1  C  Y N 420 
PHE   CE2  C  Y N 421 
PHE   CZ   C  Y N 422 
PHE   OXT  O  N N 423 
PHE   H    H  N N 424 
PHE   H2   H  N N 425 
PHE   HA   H  N N 426 
PHE   HB2  H  N N 427 
PHE   HB3  H  N N 428 
PHE   HD1  H  N N 429 
PHE   HD2  H  N N 430 
PHE   HE1  H  N N 431 
PHE   HE2  H  N N 432 
PHE   HZ   H  N N 433 
PHE   HXT  H  N N 434 
PRO   N    N  N N 435 
PRO   CA   C  N S 436 
PRO   C    C  N N 437 
PRO   O    O  N N 438 
PRO   CB   C  N N 439 
PRO   CG   C  N N 440 
PRO   CD   C  N N 441 
PRO   OXT  O  N N 442 
PRO   H    H  N N 443 
PRO   HA   H  N N 444 
PRO   HB2  H  N N 445 
PRO   HB3  H  N N 446 
PRO   HG2  H  N N 447 
PRO   HG3  H  N N 448 
PRO   HD2  H  N N 449 
PRO   HD3  H  N N 450 
PRO   HXT  H  N N 451 
SER   N    N  N N 452 
SER   CA   C  N S 453 
SER   C    C  N N 454 
SER   O    O  N N 455 
SER   CB   C  N N 456 
SER   OG   O  N N 457 
SER   OXT  O  N N 458 
SER   H    H  N N 459 
SER   H2   H  N N 460 
SER   HA   H  N N 461 
SER   HB2  H  N N 462 
SER   HB3  H  N N 463 
SER   HG   H  N N 464 
SER   HXT  H  N N 465 
THR   N    N  N N 466 
THR   CA   C  N S 467 
THR   C    C  N N 468 
THR   O    O  N N 469 
THR   CB   C  N R 470 
THR   OG1  O  N N 471 
THR   CG2  C  N N 472 
THR   OXT  O  N N 473 
THR   H    H  N N 474 
THR   H2   H  N N 475 
THR   HA   H  N N 476 
THR   HB   H  N N 477 
THR   HG1  H  N N 478 
THR   HG21 H  N N 479 
THR   HG22 H  N N 480 
THR   HG23 H  N N 481 
THR   HXT  H  N N 482 
TRP   N    N  N N 483 
TRP   CA   C  N S 484 
TRP   C    C  N N 485 
TRP   O    O  N N 486 
TRP   CB   C  N N 487 
TRP   CG   C  Y N 488 
TRP   CD1  C  Y N 489 
TRP   CD2  C  Y N 490 
TRP   NE1  N  Y N 491 
TRP   CE2  C  Y N 492 
TRP   CE3  C  Y N 493 
TRP   CZ2  C  Y N 494 
TRP   CZ3  C  Y N 495 
TRP   CH2  C  Y N 496 
TRP   OXT  O  N N 497 
TRP   H    H  N N 498 
TRP   H2   H  N N 499 
TRP   HA   H  N N 500 
TRP   HB2  H  N N 501 
TRP   HB3  H  N N 502 
TRP   HD1  H  N N 503 
TRP   HE1  H  N N 504 
TRP   HE3  H  N N 505 
TRP   HZ2  H  N N 506 
TRP   HZ3  H  N N 507 
TRP   HH2  H  N N 508 
TRP   HXT  H  N N 509 
TYR   N    N  N N 510 
TYR   CA   C  N S 511 
TYR   C    C  N N 512 
TYR   O    O  N N 513 
TYR   CB   C  N N 514 
TYR   CG   C  Y N 515 
TYR   CD1  C  Y N 516 
TYR   CD2  C  Y N 517 
TYR   CE1  C  Y N 518 
TYR   CE2  C  Y N 519 
TYR   CZ   C  Y N 520 
TYR   OH   O  N N 521 
TYR   OXT  O  N N 522 
TYR   H    H  N N 523 
TYR   H2   H  N N 524 
TYR   HA   H  N N 525 
TYR   HB2  H  N N 526 
TYR   HB3  H  N N 527 
TYR   HD1  H  N N 528 
TYR   HD2  H  N N 529 
TYR   HE1  H  N N 530 
TYR   HE2  H  N N 531 
TYR   HH   H  N N 532 
TYR   HXT  H  N N 533 
VAL   N    N  N N 534 
VAL   CA   C  N S 535 
VAL   C    C  N N 536 
VAL   O    O  N N 537 
VAL   CB   C  N N 538 
VAL   CG1  C  N N 539 
VAL   CG2  C  N N 540 
VAL   OXT  O  N N 541 
VAL   H    H  N N 542 
VAL   H2   H  N N 543 
VAL   HA   H  N N 544 
VAL   HB   H  N N 545 
VAL   HG11 H  N N 546 
VAL   HG12 H  N N 547 
VAL   HG13 H  N N 548 
VAL   HG21 H  N N 549 
VAL   HG22 H  N N 550 
VAL   HG23 H  N N 551 
VAL   HXT  H  N N 552 
# 
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 
A1A6A C02 O01  sing N N 1   
A1A6A O03 C02  doub N N 2   
A1A6A C04 C02  sing N N 3   
A1A6A C06 N05  sing N N 4   
A1A6A C07 C06  sing N N 5   
A1A6A C08 C07  sing N N 6   
A1A6A C09 C08  sing N N 7   
A1A6A O10 C08  sing N N 8   
A1A6A C11 O10  sing N N 9   
A1A6A C12 C11  sing N N 10  
A1A6A C13 C12  sing N N 11  
A1A6A C14 C13  sing N N 12  
A1A6A C15 C14  sing N N 13  
A1A6A N16 C15  doub Y N 14  
A1A6A C17 N16  sing Y N 15  
A1A6A C18 C17  doub Y N 16  
A1A6A C20 C19  sing N N 17  
A1A6A C21 C20  sing N N 18  
A1A6A N22 C21  sing N N 19  
A1A6A C19 C18  sing N N 20  
A1A6A C23 C18  sing Y N 21  
A1A6A C24 C23  doub Y N 22  
A1A6A N05 C04  sing N N 23  
A1A6A C25 C04  sing N N 24  
A1A6A C26 C25  doub Y N 25  
A1A6A C27 C26  sing Y N 26  
A1A6A C28 C27  doub Y N 27  
A1A6A C29 C28  sing Y N 28  
A1A6A C30 C29  doub Y N 29  
A1A6A N05 C09  sing N N 30  
A1A6A C15 C24  sing Y N 31  
A1A6A C17 N22  sing N N 32  
A1A6A C25 C30  sing Y N 33  
A1A6A C19 H192 sing N N 34  
A1A6A C19 H191 sing N N 35  
A1A6A C21 H211 sing N N 36  
A1A6A C21 H212 sing N N 37  
A1A6A C20 H201 sing N N 38  
A1A6A C20 H202 sing N N 39  
A1A6A C13 H131 sing N N 40  
A1A6A C13 H132 sing N N 41  
A1A6A C14 H142 sing N N 42  
A1A6A C14 H141 sing N N 43  
A1A6A C12 H122 sing N N 44  
A1A6A C12 H121 sing N N 45  
A1A6A C11 H111 sing N N 46  
A1A6A C11 H112 sing N N 47  
A1A6A C23 H231 sing N N 48  
A1A6A C04 H041 sing N N 49  
A1A6A C06 H061 sing N N 50  
A1A6A C06 H062 sing N N 51  
A1A6A C07 H072 sing N N 52  
A1A6A C07 H071 sing N N 53  
A1A6A C08 H081 sing N N 54  
A1A6A C09 H092 sing N N 55  
A1A6A C09 H091 sing N N 56  
A1A6A C24 H241 sing N N 57  
A1A6A C26 H261 sing N N 58  
A1A6A C27 H271 sing N N 59  
A1A6A C28 H281 sing N N 60  
A1A6A C29 H291 sing N N 61  
A1A6A C30 H301 sing N N 62  
A1A6A N22 H221 sing N N 63  
A1A6A O01 H1   sing N N 64  
ACT   C   O    doub N N 65  
ACT   C   OXT  sing N N 66  
ACT   C   CH3  sing N N 67  
ACT   CH3 H1   sing N N 68  
ACT   CH3 H2   sing N N 69  
ACT   CH3 H3   sing N N 70  
ALA   N   CA   sing N N 71  
ALA   N   H    sing N N 72  
ALA   N   H2   sing N N 73  
ALA   CA  C    sing N N 74  
ALA   CA  CB   sing N N 75  
ALA   CA  HA   sing N N 76  
ALA   C   O    doub N N 77  
ALA   C   OXT  sing N N 78  
ALA   CB  HB1  sing N N 79  
ALA   CB  HB2  sing N N 80  
ALA   CB  HB3  sing N N 81  
ALA   OXT HXT  sing N N 82  
ARG   N   CA   sing N N 83  
ARG   N   H    sing N N 84  
ARG   N   H2   sing N N 85  
ARG   CA  C    sing N N 86  
ARG   CA  CB   sing N N 87  
ARG   CA  HA   sing N N 88  
ARG   C   O    doub N N 89  
ARG   C   OXT  sing N N 90  
ARG   CB  CG   sing N N 91  
ARG   CB  HB2  sing N N 92  
ARG   CB  HB3  sing N N 93  
ARG   CG  CD   sing N N 94  
ARG   CG  HG2  sing N N 95  
ARG   CG  HG3  sing N N 96  
ARG   CD  NE   sing N N 97  
ARG   CD  HD2  sing N N 98  
ARG   CD  HD3  sing N N 99  
ARG   NE  CZ   sing N N 100 
ARG   NE  HE   sing N N 101 
ARG   CZ  NH1  sing N N 102 
ARG   CZ  NH2  doub N N 103 
ARG   NH1 HH11 sing N N 104 
ARG   NH1 HH12 sing N N 105 
ARG   NH2 HH21 sing N N 106 
ARG   NH2 HH22 sing N N 107 
ARG   OXT HXT  sing N N 108 
ASN   N   CA   sing N N 109 
ASN   N   H    sing N N 110 
ASN   N   H2   sing N N 111 
ASN   CA  C    sing N N 112 
ASN   CA  CB   sing N N 113 
ASN   CA  HA   sing N N 114 
ASN   C   O    doub N N 115 
ASN   C   OXT  sing N N 116 
ASN   CB  CG   sing N N 117 
ASN   CB  HB2  sing N N 118 
ASN   CB  HB3  sing N N 119 
ASN   CG  OD1  doub N N 120 
ASN   CG  ND2  sing N N 121 
ASN   ND2 HD21 sing N N 122 
ASN   ND2 HD22 sing N N 123 
ASN   OXT HXT  sing N N 124 
ASP   N   CA   sing N N 125 
ASP   N   H    sing N N 126 
ASP   N   H2   sing N N 127 
ASP   CA  C    sing N N 128 
ASP   CA  CB   sing N N 129 
ASP   CA  HA   sing N N 130 
ASP   C   O    doub N N 131 
ASP   C   OXT  sing N N 132 
ASP   CB  CG   sing N N 133 
ASP   CB  HB2  sing N N 134 
ASP   CB  HB3  sing N N 135 
ASP   CG  OD1  doub N N 136 
ASP   CG  OD2  sing N N 137 
ASP   OD2 HD2  sing N N 138 
ASP   OXT HXT  sing N N 139 
BMA   C1  C2   sing N N 140 
BMA   C1  O1   sing N N 141 
BMA   C1  O5   sing N N 142 
BMA   C1  H1   sing N N 143 
BMA   C2  C3   sing N N 144 
BMA   C2  O2   sing N N 145 
BMA   C2  H2   sing N N 146 
BMA   C3  C4   sing N N 147 
BMA   C3  O3   sing N N 148 
BMA   C3  H3   sing N N 149 
BMA   C4  C5   sing N N 150 
BMA   C4  O4   sing N N 151 
BMA   C4  H4   sing N N 152 
BMA   C5  C6   sing N N 153 
BMA   C5  O5   sing N N 154 
BMA   C5  H5   sing N N 155 
BMA   C6  O6   sing N N 156 
BMA   C6  H61  sing N N 157 
BMA   C6  H62  sing N N 158 
BMA   O1  HO1  sing N N 159 
BMA   O2  HO2  sing N N 160 
BMA   O3  HO3  sing N N 161 
BMA   O4  HO4  sing N N 162 
BMA   O6  HO6  sing N N 163 
CYS   N   CA   sing N N 164 
CYS   N   H    sing N N 165 
CYS   N   H2   sing N N 166 
CYS   CA  C    sing N N 167 
CYS   CA  CB   sing N N 168 
CYS   CA  HA   sing N N 169 
CYS   C   O    doub N N 170 
CYS   C   OXT  sing N N 171 
CYS   CB  SG   sing N N 172 
CYS   CB  HB2  sing N N 173 
CYS   CB  HB3  sing N N 174 
CYS   SG  HG   sing N N 175 
CYS   OXT HXT  sing N N 176 
GLN   N   CA   sing N N 177 
GLN   N   H    sing N N 178 
GLN   N   H2   sing N N 179 
GLN   CA  C    sing N N 180 
GLN   CA  CB   sing N N 181 
GLN   CA  HA   sing N N 182 
GLN   C   O    doub N N 183 
GLN   C   OXT  sing N N 184 
GLN   CB  CG   sing N N 185 
GLN   CB  HB2  sing N N 186 
GLN   CB  HB3  sing N N 187 
GLN   CG  CD   sing N N 188 
GLN   CG  HG2  sing N N 189 
GLN   CG  HG3  sing N N 190 
GLN   CD  OE1  doub N N 191 
GLN   CD  NE2  sing N N 192 
GLN   NE2 HE21 sing N N 193 
GLN   NE2 HE22 sing N N 194 
GLN   OXT HXT  sing N N 195 
GLU   N   CA   sing N N 196 
GLU   N   H    sing N N 197 
GLU   N   H2   sing N N 198 
GLU   CA  C    sing N N 199 
GLU   CA  CB   sing N N 200 
GLU   CA  HA   sing N N 201 
GLU   C   O    doub N N 202 
GLU   C   OXT  sing N N 203 
GLU   CB  CG   sing N N 204 
GLU   CB  HB2  sing N N 205 
GLU   CB  HB3  sing N N 206 
GLU   CG  CD   sing N N 207 
GLU   CG  HG2  sing N N 208 
GLU   CG  HG3  sing N N 209 
GLU   CD  OE1  doub N N 210 
GLU   CD  OE2  sing N N 211 
GLU   OE2 HE2  sing N N 212 
GLU   OXT HXT  sing N N 213 
GLY   N   CA   sing N N 214 
GLY   N   H    sing N N 215 
GLY   N   H2   sing N N 216 
GLY   CA  C    sing N N 217 
GLY   CA  HA2  sing N N 218 
GLY   CA  HA3  sing N N 219 
GLY   C   O    doub N N 220 
GLY   C   OXT  sing N N 221 
GLY   OXT HXT  sing N N 222 
GOL   C1  O1   sing N N 223 
GOL   C1  C2   sing N N 224 
GOL   C1  H11  sing N N 225 
GOL   C1  H12  sing N N 226 
GOL   O1  HO1  sing N N 227 
GOL   C2  O2   sing N N 228 
GOL   C2  C3   sing N N 229 
GOL   C2  H2   sing N N 230 
GOL   O2  HO2  sing N N 231 
GOL   C3  O3   sing N N 232 
GOL   C3  H31  sing N N 233 
GOL   C3  H32  sing N N 234 
GOL   O3  HO3  sing N N 235 
HIS   N   CA   sing N N 236 
HIS   N   H    sing N N 237 
HIS   N   H2   sing N N 238 
HIS   CA  C    sing N N 239 
HIS   CA  CB   sing N N 240 
HIS   CA  HA   sing N N 241 
HIS   C   O    doub N N 242 
HIS   C   OXT  sing N N 243 
HIS   CB  CG   sing N N 244 
HIS   CB  HB2  sing N N 245 
HIS   CB  HB3  sing N N 246 
HIS   CG  ND1  sing Y N 247 
HIS   CG  CD2  doub Y N 248 
HIS   ND1 CE1  doub Y N 249 
HIS   ND1 HD1  sing N N 250 
HIS   CD2 NE2  sing Y N 251 
HIS   CD2 HD2  sing N N 252 
HIS   CE1 NE2  sing Y N 253 
HIS   CE1 HE1  sing N N 254 
HIS   NE2 HE2  sing N N 255 
HIS   OXT HXT  sing N N 256 
HOH   O   H1   sing N N 257 
HOH   O   H2   sing N N 258 
ILE   N   CA   sing N N 259 
ILE   N   H    sing N N 260 
ILE   N   H2   sing N N 261 
ILE   CA  C    sing N N 262 
ILE   CA  CB   sing N N 263 
ILE   CA  HA   sing N N 264 
ILE   C   O    doub N N 265 
ILE   C   OXT  sing N N 266 
ILE   CB  CG1  sing N N 267 
ILE   CB  CG2  sing N N 268 
ILE   CB  HB   sing N N 269 
ILE   CG1 CD1  sing N N 270 
ILE   CG1 HG12 sing N N 271 
ILE   CG1 HG13 sing N N 272 
ILE   CG2 HG21 sing N N 273 
ILE   CG2 HG22 sing N N 274 
ILE   CG2 HG23 sing N N 275 
ILE   CD1 HD11 sing N N 276 
ILE   CD1 HD12 sing N N 277 
ILE   CD1 HD13 sing N N 278 
ILE   OXT HXT  sing N N 279 
LEU   N   CA   sing N N 280 
LEU   N   H    sing N N 281 
LEU   N   H2   sing N N 282 
LEU   CA  C    sing N N 283 
LEU   CA  CB   sing N N 284 
LEU   CA  HA   sing N N 285 
LEU   C   O    doub N N 286 
LEU   C   OXT  sing N N 287 
LEU   CB  CG   sing N N 288 
LEU   CB  HB2  sing N N 289 
LEU   CB  HB3  sing N N 290 
LEU   CG  CD1  sing N N 291 
LEU   CG  CD2  sing N N 292 
LEU   CG  HG   sing N N 293 
LEU   CD1 HD11 sing N N 294 
LEU   CD1 HD12 sing N N 295 
LEU   CD1 HD13 sing N N 296 
LEU   CD2 HD21 sing N N 297 
LEU   CD2 HD22 sing N N 298 
LEU   CD2 HD23 sing N N 299 
LEU   OXT HXT  sing N N 300 
LYS   N   CA   sing N N 301 
LYS   N   H    sing N N 302 
LYS   N   H2   sing N N 303 
LYS   CA  C    sing N N 304 
LYS   CA  CB   sing N N 305 
LYS   CA  HA   sing N N 306 
LYS   C   O    doub N N 307 
LYS   C   OXT  sing N N 308 
LYS   CB  CG   sing N N 309 
LYS   CB  HB2  sing N N 310 
LYS   CB  HB3  sing N N 311 
LYS   CG  CD   sing N N 312 
LYS   CG  HG2  sing N N 313 
LYS   CG  HG3  sing N N 314 
LYS   CD  CE   sing N N 315 
LYS   CD  HD2  sing N N 316 
LYS   CD  HD3  sing N N 317 
LYS   CE  NZ   sing N N 318 
LYS   CE  HE2  sing N N 319 
LYS   CE  HE3  sing N N 320 
LYS   NZ  HZ1  sing N N 321 
LYS   NZ  HZ2  sing N N 322 
LYS   NZ  HZ3  sing N N 323 
LYS   OXT HXT  sing N N 324 
MAN   C1  C2   sing N N 325 
MAN   C1  O1   sing N N 326 
MAN   C1  O5   sing N N 327 
MAN   C1  H1   sing N N 328 
MAN   C2  C3   sing N N 329 
MAN   C2  O2   sing N N 330 
MAN   C2  H2   sing N N 331 
MAN   C3  C4   sing N N 332 
MAN   C3  O3   sing N N 333 
MAN   C3  H3   sing N N 334 
MAN   C4  C5   sing N N 335 
MAN   C4  O4   sing N N 336 
MAN   C4  H4   sing N N 337 
MAN   C5  C6   sing N N 338 
MAN   C5  O5   sing N N 339 
MAN   C5  H5   sing N N 340 
MAN   C6  O6   sing N N 341 
MAN   C6  H61  sing N N 342 
MAN   C6  H62  sing N N 343 
MAN   O1  HO1  sing N N 344 
MAN   O2  HO2  sing N N 345 
MAN   O3  HO3  sing N N 346 
MAN   O4  HO4  sing N N 347 
MAN   O6  HO6  sing N N 348 
MET   N   CA   sing N N 349 
MET   N   H    sing N N 350 
MET   N   H2   sing N N 351 
MET   CA  C    sing N N 352 
MET   CA  CB   sing N N 353 
MET   CA  HA   sing N N 354 
MET   C   O    doub N N 355 
MET   C   OXT  sing N N 356 
MET   CB  CG   sing N N 357 
MET   CB  HB2  sing N N 358 
MET   CB  HB3  sing N N 359 
MET   CG  SD   sing N N 360 
MET   CG  HG2  sing N N 361 
MET   CG  HG3  sing N N 362 
MET   SD  CE   sing N N 363 
MET   CE  HE1  sing N N 364 
MET   CE  HE2  sing N N 365 
MET   CE  HE3  sing N N 366 
MET   OXT HXT  sing N N 367 
NAG   C1  C2   sing N N 368 
NAG   C1  O1   sing N N 369 
NAG   C1  O5   sing N N 370 
NAG   C1  H1   sing N N 371 
NAG   C2  C3   sing N N 372 
NAG   C2  N2   sing N N 373 
NAG   C2  H2   sing N N 374 
NAG   C3  C4   sing N N 375 
NAG   C3  O3   sing N N 376 
NAG   C3  H3   sing N N 377 
NAG   C4  C5   sing N N 378 
NAG   C4  O4   sing N N 379 
NAG   C4  H4   sing N N 380 
NAG   C5  C6   sing N N 381 
NAG   C5  O5   sing N N 382 
NAG   C5  H5   sing N N 383 
NAG   C6  O6   sing N N 384 
NAG   C6  H61  sing N N 385 
NAG   C6  H62  sing N N 386 
NAG   C7  C8   sing N N 387 
NAG   C7  N2   sing N N 388 
NAG   C7  O7   doub N N 389 
NAG   C8  H81  sing N N 390 
NAG   C8  H82  sing N N 391 
NAG   C8  H83  sing N N 392 
NAG   N2  HN2  sing N N 393 
NAG   O1  HO1  sing N N 394 
NAG   O3  HO3  sing N N 395 
NAG   O4  HO4  sing N N 396 
NAG   O6  HO6  sing N N 397 
PHE   N   CA   sing N N 398 
PHE   N   H    sing N N 399 
PHE   N   H2   sing N N 400 
PHE   CA  C    sing N N 401 
PHE   CA  CB   sing N N 402 
PHE   CA  HA   sing N N 403 
PHE   C   O    doub N N 404 
PHE   C   OXT  sing N N 405 
PHE   CB  CG   sing N N 406 
PHE   CB  HB2  sing N N 407 
PHE   CB  HB3  sing N N 408 
PHE   CG  CD1  doub Y N 409 
PHE   CG  CD2  sing Y N 410 
PHE   CD1 CE1  sing Y N 411 
PHE   CD1 HD1  sing N N 412 
PHE   CD2 CE2  doub Y N 413 
PHE   CD2 HD2  sing N N 414 
PHE   CE1 CZ   doub Y N 415 
PHE   CE1 HE1  sing N N 416 
PHE   CE2 CZ   sing Y N 417 
PHE   CE2 HE2  sing N N 418 
PHE   CZ  HZ   sing N N 419 
PHE   OXT HXT  sing N N 420 
PRO   N   CA   sing N N 421 
PRO   N   CD   sing N N 422 
PRO   N   H    sing N N 423 
PRO   CA  C    sing N N 424 
PRO   CA  CB   sing N N 425 
PRO   CA  HA   sing N N 426 
PRO   C   O    doub N N 427 
PRO   C   OXT  sing N N 428 
PRO   CB  CG   sing N N 429 
PRO   CB  HB2  sing N N 430 
PRO   CB  HB3  sing N N 431 
PRO   CG  CD   sing N N 432 
PRO   CG  HG2  sing N N 433 
PRO   CG  HG3  sing N N 434 
PRO   CD  HD2  sing N N 435 
PRO   CD  HD3  sing N N 436 
PRO   OXT HXT  sing N N 437 
SER   N   CA   sing N N 438 
SER   N   H    sing N N 439 
SER   N   H2   sing N N 440 
SER   CA  C    sing N N 441 
SER   CA  CB   sing N N 442 
SER   CA  HA   sing N N 443 
SER   C   O    doub N N 444 
SER   C   OXT  sing N N 445 
SER   CB  OG   sing N N 446 
SER   CB  HB2  sing N N 447 
SER   CB  HB3  sing N N 448 
SER   OG  HG   sing N N 449 
SER   OXT HXT  sing N N 450 
THR   N   CA   sing N N 451 
THR   N   H    sing N N 452 
THR   N   H2   sing N N 453 
THR   CA  C    sing N N 454 
THR   CA  CB   sing N N 455 
THR   CA  HA   sing N N 456 
THR   C   O    doub N N 457 
THR   C   OXT  sing N N 458 
THR   CB  OG1  sing N N 459 
THR   CB  CG2  sing N N 460 
THR   CB  HB   sing N N 461 
THR   OG1 HG1  sing N N 462 
THR   CG2 HG21 sing N N 463 
THR   CG2 HG22 sing N N 464 
THR   CG2 HG23 sing N N 465 
THR   OXT HXT  sing N N 466 
TRP   N   CA   sing N N 467 
TRP   N   H    sing N N 468 
TRP   N   H2   sing N N 469 
TRP   CA  C    sing N N 470 
TRP   CA  CB   sing N N 471 
TRP   CA  HA   sing N N 472 
TRP   C   O    doub N N 473 
TRP   C   OXT  sing N N 474 
TRP   CB  CG   sing N N 475 
TRP   CB  HB2  sing N N 476 
TRP   CB  HB3  sing N N 477 
TRP   CG  CD1  doub Y N 478 
TRP   CG  CD2  sing Y N 479 
TRP   CD1 NE1  sing Y N 480 
TRP   CD1 HD1  sing N N 481 
TRP   CD2 CE2  doub Y N 482 
TRP   CD2 CE3  sing Y N 483 
TRP   NE1 CE2  sing Y N 484 
TRP   NE1 HE1  sing N N 485 
TRP   CE2 CZ2  sing Y N 486 
TRP   CE3 CZ3  doub Y N 487 
TRP   CE3 HE3  sing N N 488 
TRP   CZ2 CH2  doub Y N 489 
TRP   CZ2 HZ2  sing N N 490 
TRP   CZ3 CH2  sing Y N 491 
TRP   CZ3 HZ3  sing N N 492 
TRP   CH2 HH2  sing N N 493 
TRP   OXT HXT  sing N N 494 
TYR   N   CA   sing N N 495 
TYR   N   H    sing N N 496 
TYR   N   H2   sing N N 497 
TYR   CA  C    sing N N 498 
TYR   CA  CB   sing N N 499 
TYR   CA  HA   sing N N 500 
TYR   C   O    doub N N 501 
TYR   C   OXT  sing N N 502 
TYR   CB  CG   sing N N 503 
TYR   CB  HB2  sing N N 504 
TYR   CB  HB3  sing N N 505 
TYR   CG  CD1  doub Y N 506 
TYR   CG  CD2  sing Y N 507 
TYR   CD1 CE1  sing Y N 508 
TYR   CD1 HD1  sing N N 509 
TYR   CD2 CE2  doub Y N 510 
TYR   CD2 HD2  sing N N 511 
TYR   CE1 CZ   doub Y N 512 
TYR   CE1 HE1  sing N N 513 
TYR   CE2 CZ   sing Y N 514 
TYR   CE2 HE2  sing N N 515 
TYR   CZ  OH   sing N N 516 
TYR   OH  HH   sing N N 517 
TYR   OXT HXT  sing N N 518 
VAL   N   CA   sing N N 519 
VAL   N   H    sing N N 520 
VAL   N   H2   sing N N 521 
VAL   CA  C    sing N N 522 
VAL   CA  CB   sing N N 523 
VAL   CA  HA   sing N N 524 
VAL   C   O    doub N N 525 
VAL   C   OXT  sing N N 526 
VAL   CB  CG1  sing N N 527 
VAL   CB  CG2  sing N N 528 
VAL   CB  HB   sing N N 529 
VAL   CG1 HG11 sing N N 530 
VAL   CG1 HG12 sing N N 531 
VAL   CG1 HG13 sing N N 532 
VAL   CG2 HG21 sing N N 533 
VAL   CG2 HG22 sing N N 534 
VAL   CG2 HG23 sing N N 535 
VAL   OXT HXT  sing N N 536 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
6 NAG 1 n 
6 NAG 2 n 
6 BMA 3 n 
6 MAN 4 n 
6 MAN 5 n 
6 MAN 6 n 
7 NAG 1 n 
7 NAG 2 n 
7 BMA 3 n 
7 MAN 4 n 
7 MAN 5 n 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 4UM9 ? 
2 ? 'experimental model' PDB 4O02 ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CZ7 
_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]   0.010363 
_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]   0.007547 
_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]   0.005939 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CA  ? ? 16.26893 3.65395 ? ? 3.58509  77.28589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H   ? ? ?        ?       ? ? ?        ?        ? ? ?   ? ? 
MG  ? ? 9.41153  2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N    . PHE   A  1  1   ? 32.294  -1.413  -19.624  1.00 76.98  ? 1    PHE   A N    1 
ATOM   2     C  CA   . PHE   A  1  1   ? 32.121  -0.165  -18.825  1.00 80.52  ? 1    PHE   A CA   1 
ATOM   3     C  C    . PHE   A  1  1   ? 31.463  0.994   -19.581  1.00 80.38  ? 1    PHE   A C    1 
ATOM   4     O  O    . PHE   A  1  1   ? 31.048  1.969   -18.957  1.00 84.64  ? 1    PHE   A O    1 
ATOM   5     C  CB   . PHE   A  1  1   ? 33.483  0.307   -18.291  1.00 71.39  ? 1    PHE   A CB   1 
ATOM   6     C  CG   . PHE   A  1  1   ? 34.495  0.607   -19.369  1.00 86.18  ? 1    PHE   A CG   1 
ATOM   7     C  CD1  . PHE   A  1  1   ? 34.563  1.865   -19.949  1.00 92.60  ? 1    PHE   A CD1  1 
ATOM   8     C  CD2  . PHE   A  1  1   ? 35.389  -0.365  -19.789  1.00 87.30  ? 1    PHE   A CD2  1 
ATOM   9     C  CE1  . PHE   A  1  1   ? 35.498  2.142   -20.933  1.00 91.91  ? 1    PHE   A CE1  1 
ATOM   10    C  CE2  . PHE   A  1  1   ? 36.325  -0.092  -20.772  1.00 85.69  ? 1    PHE   A CE2  1 
ATOM   11    C  CZ   . PHE   A  1  1   ? 36.379  1.163   -21.343  1.00 87.88  ? 1    PHE   A CZ   1 
ATOM   12    H  H1   . PHE   A  1  1   ? 32.563  -2.072  -19.091  1.00 92.41  ? 1    PHE   A H1   1 
ATOM   13    H  H2   . PHE   A  1  1   ? 31.518  -1.633  -20.001  1.00 92.41  ? 1    PHE   A H2   1 
ATOM   14    H  H3   . PHE   A  1  1   ? 32.903  -1.277  -20.259  1.00 92.41  ? 1    PHE   A H3   1 
ATOM   15    H  HA   . PHE   A  1  1   ? 31.522  -0.388  -18.096  1.00 96.66  ? 1    PHE   A HA   1 
ATOM   16    H  HB2  . PHE   A  1  1   ? 33.351  1.118   -17.777  1.00 85.48  ? 1    PHE   A HB2  1 
ATOM   17    H  HB3  . PHE   A  1  1   ? 33.852  -0.389  -17.725  1.00 85.48  ? 1    PHE   A HB3  1 
ATOM   18    H  HD1  . PHE   A  1  1   ? 33.974  2.530   -19.675  1.00 111.15 ? 1    PHE   A HD1  1 
ATOM   19    H  HD2  . PHE   A  1  1   ? 35.360  -1.212  -19.405  1.00 104.79 ? 1    PHE   A HD2  1 
ATOM   20    H  HE1  . PHE   A  1  1   ? 35.531  2.989   -21.317  1.00 110.33 ? 1    PHE   A HE1  1 
ATOM   21    H  HE2  . PHE   A  1  1   ? 36.917  -0.754  -21.047  1.00 102.86 ? 1    PHE   A HE2  1 
ATOM   22    H  HZ   . PHE   A  1  1   ? 37.008  1.348   -22.003  1.00 105.49 ? 1    PHE   A HZ   1 
ATOM   23    N  N    . ASN   A  1  2   ? 31.352  0.904   -20.907  1.00 76.51  ? 2    ASN   A N    1 
ATOM   24    C  CA   . ASN   A  1  2   ? 30.917  2.042   -21.709  1.00 73.09  ? 2    ASN   A CA   1 
ATOM   25    C  C    . ASN   A  1  2   ? 29.473  1.942   -22.192  1.00 71.41  ? 2    ASN   A C    1 
ATOM   26    O  O    . ASN   A  1  2   ? 29.056  2.759   -23.019  1.00 72.72  ? 2    ASN   A O    1 
ATOM   27    C  CB   . ASN   A  1  2   ? 31.847  2.233   -22.913  1.00 71.38  ? 2    ASN   A CB   1 
ATOM   28    C  CG   . ASN   A  1  2   ? 32.029  0.967   -23.720  1.00 70.10  ? 2    ASN   A CG   1 
ATOM   29    O  OD1  . ASN   A  1  2   ? 32.099  -0.129  -23.167  1.00 70.11  ? 2    ASN   A OD1  1 
ATOM   30    N  ND2  . ASN   A  1  2   ? 32.111  1.111   -25.039  1.00 71.21  ? 2    ASN   A ND2  1 
ATOM   31    H  H    . ASN   A  1  2   ? 31.523  0.194   -21.361  1.00 91.85  ? 2    ASN   A H    1 
ATOM   32    H  HA   . ASN   A  1  2   ? 30.978  2.829   -21.145  1.00 87.75  ? 2    ASN   A HA   1 
ATOM   33    H  HB2  . ASN   A  1  2   ? 31.472  2.910   -23.497  1.00 85.69  ? 2    ASN   A HB2  1 
ATOM   34    H  HB3  . ASN   A  1  2   ? 32.720  2.514   -22.596  1.00 85.69  ? 2    ASN   A HB3  1 
ATOM   35    H  HD21 . ASN   A  1  2   ? 32.214  0.421   -25.542  1.00 85.49  ? 2    ASN   A HD21 1 
ATOM   36    H  HD22 . ASN   A  1  2   ? 32.060  1.895   -25.390  1.00 85.49  ? 2    ASN   A HD22 1 
ATOM   37    N  N    . LEU   A  1  3   ? 28.694  0.986   -21.696  1.00 68.30  ? 3    LEU   A N    1 
ATOM   38    C  CA   . LEU   A  1  3   ? 27.286  0.929   -22.067  1.00 70.74  ? 3    LEU   A CA   1 
ATOM   39    C  C    . LEU   A  1  3   ? 26.532  2.109   -21.463  1.00 77.24  ? 3    LEU   A C    1 
ATOM   40    O  O    . LEU   A  1  3   ? 26.748  2.479   -20.306  1.00 81.53  ? 3    LEU   A O    1 
ATOM   41    C  CB   . LEU   A  1  3   ? 26.660  -0.388  -21.611  1.00 68.23  ? 3    LEU   A CB   1 
ATOM   42    C  CG   . LEU   A  1  3   ? 26.933  -1.591  -22.518  1.00 63.28  ? 3    LEU   A CG   1 
ATOM   43    C  CD1  . LEU   A  1  3   ? 26.459  -2.881  -21.869  1.00 59.29  ? 3    LEU   A CD1  1 
ATOM   44    C  CD2  . LEU   A  1  3   ? 26.268  -1.406  -23.880  1.00 62.92  ? 3    LEU   A CD2  1 
ATOM   45    H  H    . LEU   A  1  3   ? 28.952  0.370   -21.154  1.00 82.00  ? 3    LEU   A H    1 
ATOM   46    H  HA   . LEU   A  1  3   ? 27.205  0.975   -23.033  1.00 84.92  ? 3    LEU   A HA   1 
ATOM   47    H  HB2  . LEU   A  1  3   ? 27.008  -0.603  -20.731  1.00 81.92  ? 3    LEU   A HB2  1 
ATOM   48    H  HB3  . LEU   A  1  3   ? 25.698  -0.270  -21.567  1.00 81.92  ? 3    LEU   A HB3  1 
ATOM   49    H  HG   . LEU   A  1  3   ? 27.891  -1.659  -22.657  1.00 75.97  ? 3    LEU   A HG   1 
ATOM   50    H  HD11 . LEU   A  1  3   ? 26.757  -3.633  -22.406  1.00 71.19  ? 3    LEU   A HD11 1 
ATOM   51    H  HD12 . LEU   A  1  3   ? 26.834  -2.942  -20.977  1.00 71.19  ? 3    LEU   A HD12 1 
ATOM   52    H  HD13 . LEU   A  1  3   ? 25.490  -2.873  -21.821  1.00 71.19  ? 3    LEU   A HD13 1 
ATOM   53    H  HD21 . LEU   A  1  3   ? 26.418  -2.201  -24.415  1.00 75.55  ? 3    LEU   A HD21 1 
ATOM   54    H  HD22 . LEU   A  1  3   ? 25.317  -1.269  -23.750  1.00 75.55  ? 3    LEU   A HD22 1 
ATOM   55    H  HD23 . LEU   A  1  3   ? 26.658  -0.634  -24.319  1.00 75.55  ? 3    LEU   A HD23 1 
ATOM   56    N  N    . ASP   A  1  4   ? 25.646  2.707   -22.261  1.00 79.61  ? 4    ASP   A N    1 
ATOM   57    C  CA   . ASP   A  1  4   ? 24.850  3.848   -21.818  1.00 81.60  ? 4    ASP   A CA   1 
ATOM   58    C  C    . ASP   A  1  4   ? 23.620  3.329   -21.087  1.00 84.37  ? 4    ASP   A C    1 
ATOM   59    O  O    . ASP   A  1  4   ? 22.695  2.794   -21.710  1.00 86.98  ? 4    ASP   A O    1 
ATOM   60    C  CB   . ASP   A  1  4   ? 24.448  4.727   -22.999  1.00 79.67  ? 4    ASP   A CB   1 
ATOM   61    C  CG   . ASP   A  1  4   ? 23.504  5.849   -22.595  1.00 82.50  ? 4    ASP   A CG   1 
ATOM   62    O  OD1  . ASP   A  1  4   ? 23.371  6.111   -21.381  1.00 84.83  ? 4    ASP   A OD1  1 
ATOM   63    O  OD2  . ASP   A  1  4   ? 22.890  6.465   -23.491  1.00 85.25  ? 4    ASP   A OD2  1 
ATOM   64    H  H    . ASP   A  1  4   ? 25.487  2.466   -23.071  1.00 95.57  ? 4    ASP   A H    1 
ATOM   65    H  HA   . ASP   A  1  4   ? 25.380  4.386   -21.209  1.00 97.95  ? 4    ASP   A HA   1 
ATOM   66    H  HB2  . ASP   A  1  4   ? 25.244  5.127   -23.382  1.00 95.64  ? 4    ASP   A HB2  1 
ATOM   67    H  HB3  . ASP   A  1  4   ? 23.999  4.181   -23.663  1.00 95.64  ? 4    ASP   A HB3  1 
ATOM   68    N  N    . VAL   A  1  5   ? 23.604  3.493   -19.763  1.00 84.15  ? 5    VAL   A N    1 
ATOM   69    C  CA   . VAL   A  1  5   ? 22.472  3.066   -18.949  1.00 83.59  ? 5    VAL   A CA   1 
ATOM   70    C  C    . VAL   A  1  5   ? 21.548  4.220   -18.584  1.00 88.96  ? 5    VAL   A C    1 
ATOM   71    O  O    . VAL   A  1  5   ? 20.441  3.974   -18.079  1.00 90.21  ? 5    VAL   A O    1 
ATOM   72    C  CB   . VAL   A  1  5   ? 22.954  2.359   -17.663  1.00 79.37  ? 5    VAL   A CB   1 
ATOM   73    C  CG1  . VAL   A  1  5   ? 23.833  1.167   -18.016  1.00 76.48  ? 5    VAL   A CG1  1 
ATOM   74    C  CG2  . VAL   A  1  5   ? 23.703  3.332   -16.759  1.00 78.64  ? 5    VAL   A CG2  1 
ATOM   75    H  H    . VAL   A  1  5   ? 24.243  3.851   -19.312  1.00 101.01 ? 5    VAL   A H    1 
ATOM   76    H  HA   . VAL   A  1  5   ? 21.953  2.430   -19.464  1.00 100.34 ? 5    VAL   A HA   1 
ATOM   77    H  HB   . VAL   A  1  5   ? 22.181  2.035   -17.174  1.00 95.28  ? 5    VAL   A HB   1 
ATOM   78    H  HG11 . VAL   A  1  5   ? 24.112  0.727   -17.198  1.00 91.81  ? 5    VAL   A HG11 1 
ATOM   79    H  HG12 . VAL   A  1  5   ? 23.324  0.551   -18.566  1.00 91.81  ? 5    VAL   A HG12 1 
ATOM   80    H  HG13 . VAL   A  1  5   ? 24.610  1.481   -18.504  1.00 91.81  ? 5    VAL   A HG13 1 
ATOM   81    H  HG21 . VAL   A  1  5   ? 24.026  2.854   -15.980  1.00 94.41  ? 5    VAL   A HG21 1 
ATOM   82    H  HG22 . VAL   A  1  5   ? 24.451  3.707   -17.250  1.00 94.41  ? 5    VAL   A HG22 1 
ATOM   83    H  HG23 . VAL   A  1  5   ? 23.098  4.039   -16.486  1.00 94.41  ? 5    VAL   A HG23 1 
ATOM   84    N  N    . ASP   A  1  6   ? 21.959  5.467   -18.828  1.00 91.95  ? 6    ASP   A N    1 
ATOM   85    C  CA   . ASP   A  1  6   ? 21.130  6.604   -18.446  1.00 98.78  ? 6    ASP   A CA   1 
ATOM   86    C  C    . ASP   A  1  6   ? 19.886  6.719   -19.318  1.00 101.48 ? 6    ASP   A C    1 
ATOM   87    O  O    . ASP   A  1  6   ? 18.827  7.127   -18.828  1.00 106.97 ? 6    ASP   A O    1 
ATOM   88    C  CB   . ASP   A  1  6   ? 21.946  7.895   -18.521  1.00 102.86 ? 6    ASP   A CB   1 
ATOM   89    C  CG   . ASP   A  1  6   ? 23.147  7.881   -17.597  1.00 107.22 ? 6    ASP   A CG   1 
ATOM   90    O  OD1  . ASP   A  1  6   ? 23.030  7.341   -16.476  1.00 108.03 ? 6    ASP   A OD1  1 
ATOM   91    O  OD2  . ASP   A  1  6   ? 24.208  8.408   -17.992  1.00 109.39 ? 6    ASP   A OD2  1 
ATOM   92    H  H    . ASP   A  1  6   ? 22.701  5.676   -19.208  1.00 110.37 ? 6    ASP   A H    1 
ATOM   93    H  HA   . ASP   A  1  6   ? 20.841  6.480   -17.528  1.00 118.58 ? 6    ASP   A HA   1 
ATOM   94    H  HB2  . ASP   A  1  6   ? 22.267  8.014   -19.429  1.00 123.47 ? 6    ASP   A HB2  1 
ATOM   95    H  HB3  . ASP   A  1  6   ? 21.381  8.642   -18.269  1.00 123.47 ? 6    ASP   A HB3  1 
ATOM   96    N  N    . SER   A  1  7   ? 19.986  6.364   -20.598  1.00 98.16  ? 7    SER   A N    1 
ATOM   97    C  CA   . SER   A  1  7   ? 18.877  6.527   -21.540  1.00 94.32  ? 7    SER   A CA   1 
ATOM   98    C  C    . SER   A  1  7   ? 18.914  5.409   -22.569  1.00 89.36  ? 7    SER   A C    1 
ATOM   99    O  O    . SER   A  1  7   ? 19.371  5.594   -23.704  1.00 90.80  ? 7    SER   A O    1 
ATOM   100   C  CB   . SER   A  1  7   ? 18.934  7.895   -22.222  1.00 95.30  ? 7    SER   A CB   1 
ATOM   101   O  OG   . SER   A  1  7   ? 20.245  8.186   -22.676  1.00 93.70  ? 7    SER   A OG   1 
ATOM   102   H  H    . SER   A  1  7   ? 20.693  6.024   -20.949  1.00 117.83 ? 7    SER   A H    1 
ATOM   103   H  HA   . SER   A  1  7   ? 18.040  6.454   -21.055  1.00 113.22 ? 7    SER   A HA   1 
ATOM   104   H  HB2  . SER   A  1  7   ? 18.331  7.893   -22.982  1.00 114.40 ? 7    SER   A HB2  1 
ATOM   105   H  HB3  . SER   A  1  7   ? 18.663  8.576   -21.586  1.00 114.40 ? 7    SER   A HB3  1 
ATOM   106   H  HG   . SER   A  1  7   ? 20.517  7.571   -23.179  1.00 112.48 ? 7    SER   A HG   1 
ATOM   107   N  N    . PRO   A  1  8   ? 18.438  4.222   -22.205  1.00 84.08  ? 8    PRO   A N    1 
ATOM   108   C  CA   . PRO   A  1  8   ? 18.312  3.132   -23.174  1.00 78.62  ? 8    PRO   A CA   1 
ATOM   109   C  C    . PRO   A  1  8   ? 16.965  3.154   -23.884  1.00 78.26  ? 8    PRO   A C    1 
ATOM   110   O  O    . PRO   A  1  8   ? 16.012  3.808   -23.457  1.00 81.03  ? 8    PRO   A O    1 
ATOM   111   C  CB   . PRO   A  1  8   ? 18.446  1.881   -22.295  1.00 76.11  ? 8    PRO   A CB   1 
ATOM   112   C  CG   . PRO   A  1  8   ? 17.837  2.297   -20.994  1.00 78.27  ? 8    PRO   A CG   1 
ATOM   113   C  CD   . PRO   A  1  8   ? 18.126  3.777   -20.833  1.00 82.38  ? 8    PRO   A CD   1 
ATOM   114   H  HA   . PRO   A  1  8   ? 19.028  3.154   -23.829  1.00 94.38  ? 8    PRO   A HA   1 
ATOM   115   H  HB2  . PRO   A  1  8   ? 17.961  1.140   -22.690  1.00 91.37  ? 8    PRO   A HB2  1 
ATOM   116   H  HB3  . PRO   A  1  8   ? 19.381  1.645   -22.187  1.00 91.37  ? 8    PRO   A HB3  1 
ATOM   117   H  HG2  . PRO   A  1  8   ? 16.881  2.137   -21.018  1.00 93.97  ? 8    PRO   A HG2  1 
ATOM   118   H  HG3  . PRO   A  1  8   ? 18.240  1.791   -20.271  1.00 93.97  ? 8    PRO   A HG3  1 
ATOM   119   H  HD2  . PRO   A  1  8   ? 17.349  4.243   -20.488  1.00 98.89  ? 8    PRO   A HD2  1 
ATOM   120   H  HD3  . PRO   A  1  8   ? 18.885  3.917   -20.246  1.00 98.89  ? 8    PRO   A HD3  1 
ATOM   121   N  N    . ALA   A  1  9   ? 16.904  2.416   -24.990  1.00 74.50  ? 9    ALA   A N    1 
ATOM   122   C  CA   . ALA   A  1  9   ? 15.685  2.312   -25.782  1.00 72.45  ? 9    ALA   A CA   1 
ATOM   123   C  C    . ALA   A  1  9   ? 14.817  1.201   -25.206  1.00 72.17  ? 9    ALA   A C    1 
ATOM   124   O  O    . ALA   A  1  9   ? 15.250  0.047   -25.116  1.00 71.47  ? 9    ALA   A O    1 
ATOM   125   C  CB   . ALA   A  1  9   ? 16.005  2.047   -27.252  1.00 70.20  ? 9    ALA   A CB   1 
ATOM   126   H  H    . ALA   A  1  9   ? 17.564  1.961   -25.304  1.00 89.44  ? 9    ALA   A H    1 
ATOM   127   H  HA   . ALA   A  1  9   ? 15.196  3.148   -25.734  1.00 86.97  ? 9    ALA   A HA   1 
ATOM   128   H  HB1  . ALA   A  1  9   ? 15.174  1.987   -27.749  1.00 84.27  ? 9    ALA   A HB1  1 
ATOM   129   H  HB2  . ALA   A  1  9   ? 16.543  2.778   -27.595  1.00 84.27  ? 9    ALA   A HB2  1 
ATOM   130   H  HB3  . ALA   A  1  9   ? 16.495  1.213   -27.323  1.00 84.27  ? 9    ALA   A HB3  1 
ATOM   131   N  N    . GLU   A  1  10  ? 13.593  1.553   -24.828  1.00 74.05  ? 10   GLU   A N    1 
ATOM   132   C  CA   . GLU   A  1  10  ? 12.692  0.675   -24.094  1.00 72.70  ? 10   GLU   A CA   1 
ATOM   133   C  C    . GLU   A  1  10  ? 11.519  0.305   -24.991  1.00 76.51  ? 10   GLU   A C    1 
ATOM   134   O  O    . GLU   A  1  10  ? 10.733  1.175   -25.383  1.00 81.11  ? 10   GLU   A O    1 
ATOM   135   C  CB   . GLU   A  1  10  ? 12.213  1.369   -22.818  1.00 71.49  ? 10   GLU   A CB   1 
ATOM   136   C  CG   . GLU   A  1  10  ? 11.295  0.551   -21.935  1.00 73.54  ? 10   GLU   A CG   1 
ATOM   137   C  CD   . GLU   A  1  10  ? 10.915  1.300   -20.674  1.00 81.81  ? 10   GLU   A CD   1 
ATOM   138   O  OE1  . GLU   A  1  10  ? 11.695  2.182   -20.254  1.00 81.46  ? 10   GLU   A OE1  1 
ATOM   139   O  OE2  . GLU   A  1  10  ? 9.842   1.012   -20.103  1.00 83.86  ? 10   GLU   A OE2  1 
ATOM   140   H  H    . GLU   A  1  10  ? 13.251  2.325   -24.991  1.00 88.89  ? 10   GLU   A H    1 
ATOM   141   H  HA   . GLU   A  1  10  ? 13.147  -0.146  -23.852  1.00 87.28  ? 10   GLU   A HA   1 
ATOM   142   H  HB2  . GLU   A  1  10  ? 12.991  1.602   -22.288  1.00 85.83  ? 10   GLU   A HB2  1 
ATOM   143   H  HB3  . GLU   A  1  10  ? 11.731  2.172   -23.071  1.00 85.83  ? 10   GLU   A HB3  1 
ATOM   144   H  HG2  . GLU   A  1  10  ? 10.482  0.345   -22.423  1.00 88.28  ? 10   GLU   A HG2  1 
ATOM   145   H  HG3  . GLU   A  1  10  ? 11.745  -0.269  -21.679  1.00 88.28  ? 10   GLU   A HG3  1 
ATOM   146   N  N    . TYR   A  1  11  ? 11.410  -0.979  -25.318  1.00 75.54  ? 11   TYR   A N    1 
ATOM   147   C  CA   . TYR   A  1  11  ? 10.328  -1.508  -26.132  1.00 78.09  ? 11   TYR   A CA   1 
ATOM   148   C  C    . TYR   A  1  11  ? 9.428   -2.387  -25.275  1.00 78.19  ? 11   TYR   A C    1 
ATOM   149   O  O    . TYR   A  1  11  ? 9.885   -3.036  -24.330  1.00 81.43  ? 11   TYR   A O    1 
ATOM   150   C  CB   . TYR   A  1  11  ? 10.871  -2.316  -27.313  1.00 74.83  ? 11   TYR   A CB   1 
ATOM   151   C  CG   . TYR   A  1  11  ? 11.773  -1.525  -28.233  1.00 76.97  ? 11   TYR   A CG   1 
ATOM   152   C  CD1  . TYR   A  1  11  ? 13.111  -1.324  -27.921  1.00 76.03  ? 11   TYR   A CD1  1 
ATOM   153   C  CD2  . TYR   A  1  11  ? 11.288  -0.983  -29.415  1.00 81.49  ? 11   TYR   A CD2  1 
ATOM   154   C  CE1  . TYR   A  1  11  ? 13.939  -0.602  -28.758  1.00 79.16  ? 11   TYR   A CE1  1 
ATOM   155   C  CE2  . TYR   A  1  11  ? 12.108  -0.261  -30.259  1.00 83.39  ? 11   TYR   A CE2  1 
ATOM   156   C  CZ   . TYR   A  1  11  ? 13.433  -0.074  -29.926  1.00 82.83  ? 11   TYR   A CZ   1 
ATOM   157   O  OH   . TYR   A  1  11  ? 14.254  0.645   -30.763  1.00 85.98  ? 11   TYR   A OH   1 
ATOM   158   H  H    . TYR   A  1  11  ? 11.971  -1.581  -25.069  1.00 90.69  ? 11   TYR   A H    1 
ATOM   159   H  HA   . TYR   A  1  11  ? 9.798   -0.777  -26.489  1.00 93.74  ? 11   TYR   A HA   1 
ATOM   160   H  HB2  . TYR   A  1  11  ? 11.383  -3.065  -26.969  1.00 89.83  ? 11   TYR   A HB2  1 
ATOM   161   H  HB3  . TYR   A  1  11  ? 10.123  -2.640  -27.839  1.00 89.83  ? 11   TYR   A HB3  1 
ATOM   162   H  HD1  . TYR   A  1  11  ? 13.455  -1.682  -27.135  1.00 91.27  ? 11   TYR   A HD1  1 
ATOM   163   H  HD2  . TYR   A  1  11  ? 10.395  -1.108  -29.643  1.00 97.83  ? 11   TYR   A HD2  1 
ATOM   164   H  HE1  . TYR   A  1  11  ? 14.832  -0.473  -28.535  1.00 95.03  ? 11   TYR   A HE1  1 
ATOM   165   H  HE2  . TYR   A  1  11  ? 11.769  0.098   -31.047  1.00 100.11 ? 11   TYR   A HE2  1 
ATOM   166   H  HH   . TYR   A  1  11  ? 13.891  0.734   -31.515  1.00 103.21 ? 11   TYR   A HH   1 
ATOM   167   N  N    . SER   A  1  12  ? 8.141   -2.405  -25.612  1.00 72.50  ? 12   SER   A N    1 
ATOM   168   C  CA   . SER   A  1  12  ? 7.153   -3.159  -24.859  1.00 69.16  ? 12   SER   A CA   1 
ATOM   169   C  C    . SER   A  1  12  ? 6.279   -3.967  -25.805  1.00 67.98  ? 12   SER   A C    1 
ATOM   170   O  O    . SER   A  1  12  ? 6.080   -3.596  -26.965  1.00 71.37  ? 12   SER   A O    1 
ATOM   171   C  CB   . SER   A  1  12  ? 6.272   -2.234  -24.009  1.00 71.40  ? 12   SER   A CB   1 
ATOM   172   O  OG   . SER   A  1  12  ? 5.617   -1.272  -24.816  1.00 78.84  ? 12   SER   A OG   1 
ATOM   173   H  H    . SER   A  1  12  ? 7.815   -1.980  -26.285  1.00 87.04  ? 12   SER   A H    1 
ATOM   174   H  HA   . SER   A  1  12  ? 7.608   -3.779  -24.269  1.00 83.03  ? 12   SER   A HA   1 
ATOM   175   H  HB2  . SER   A  1  12  ? 5.605   -2.769  -23.551  1.00 85.71  ? 12   SER   A HB2  1 
ATOM   176   H  HB3  . SER   A  1  12  ? 6.830   -1.775  -23.362  1.00 85.71  ? 12   SER   A HB3  1 
ATOM   177   H  HG   . SER   A  1  12  ? 5.182   -0.740  -24.334  1.00 94.64  ? 12   SER   A HG   1 
ATOM   178   N  N    . GLY   A  1  13  ? 5.764   -5.081  -25.292  1.00 64.09  ? 13   GLY   A N    1 
ATOM   179   C  CA   . GLY   A  1  13  ? 4.838   -5.908  -26.024  1.00 63.11  ? 13   GLY   A CA   1 
ATOM   180   C  C    . GLY   A  1  13  ? 3.550   -6.112  -25.252  1.00 63.24  ? 13   GLY   A C    1 
ATOM   181   O  O    . GLY   A  1  13  ? 3.360   -5.567  -24.160  1.00 63.26  ? 13   GLY   A O    1 
ATOM   182   H  H    . GLY   A  1  13  ? 5.946   -5.378  -24.506  1.00 76.95  ? 13   GLY   A H    1 
ATOM   183   H  HA2  . GLY   A  1  13  ? 4.627   -5.487  -26.872  1.00 75.77  ? 13   GLY   A HA2  1 
ATOM   184   H  HA3  . GLY   A  1  13  ? 5.239   -6.775  -26.192  1.00 75.77  ? 13   GLY   A HA3  1 
ATOM   185   N  N    . PRO   A  1  14  ? 2.637   -6.904  -25.809  1.00 60.45  ? 14   PRO   A N    1 
ATOM   186   C  CA   . PRO   A  1  14  ? 1.366   -7.154  -25.120  1.00 58.61  ? 14   PRO   A CA   1 
ATOM   187   C  C    . PRO   A  1  14  ? 1.594   -7.801  -23.762  1.00 59.72  ? 14   PRO   A C    1 
ATOM   188   O  O    . PRO   A  1  14  ? 2.496   -8.623  -23.588  1.00 59.88  ? 14   PRO   A O    1 
ATOM   189   C  CB   . PRO   A  1  14  ? 0.620   -8.095  -26.074  1.00 55.98  ? 14   PRO   A CB   1 
ATOM   190   C  CG   . PRO   A  1  14  ? 1.289   -7.927  -27.401  1.00 55.66  ? 14   PRO   A CG   1 
ATOM   191   C  CD   . PRO   A  1  14  ? 2.716   -7.594  -27.108  1.00 54.78  ? 14   PRO   A CD   1 
ATOM   192   H  HA   . PRO   A  1  14  ? 0.864   -6.331  -25.012  1.00 70.37  ? 14   PRO   A HA   1 
ATOM   193   H  HB2  . PRO   A  1  14  ? 0.697   -9.010  -25.761  1.00 67.21  ? 14   PRO   A HB2  1 
ATOM   194   H  HB3  . PRO   A  1  14  ? -0.315  -7.839  -26.124  1.00 67.21  ? 14   PRO   A HB3  1 
ATOM   195   H  HG2  . PRO   A  1  14  ? 1.227   -8.754  -27.904  1.00 66.61  ? 14   PRO   A HG2  1 
ATOM   196   H  HG3  . PRO   A  1  14  ? 0.863   -7.207  -27.892  1.00 66.61  ? 14   PRO   A HG3  1 
ATOM   197   H  HD2  . PRO   A  1  14  ? 3.252   -8.400  -27.039  1.00 65.77  ? 14   PRO   A HD2  1 
ATOM   198   H  HD3  . PRO   A  1  14  ? 3.082   -7.009  -27.789  1.00 65.77  ? 14   PRO   A HD3  1 
ATOM   199   N  N    . GLU   A  1  15  ? 0.765   -7.421  -22.793  1.00 65.12  ? 15   GLU   A N    1 
ATOM   200   C  CA   . GLU   A  1  15  ? 0.881   -7.992  -21.458  1.00 70.52  ? 15   GLU   A CA   1 
ATOM   201   C  C    . GLU   A  1  15  ? 0.597   -9.488  -21.501  1.00 70.74  ? 15   GLU   A C    1 
ATOM   202   O  O    . GLU   A  1  15  ? -0.416  -9.926  -22.054  1.00 73.24  ? 15   GLU   A O    1 
ATOM   203   C  CB   . GLU   A  1  15  ? -0.082  -7.303  -20.491  1.00 78.05  ? 15   GLU   A CB   1 
ATOM   204   C  CG   . GLU   A  1  15  ? 0.082   -7.765  -19.049  1.00 84.68  ? 15   GLU   A CG   1 
ATOM   205   C  CD   . GLU   A  1  15  ? -1.001  -7.235  -18.132  1.00 96.40  ? 15   GLU   A CD   1 
ATOM   206   O  OE1  . GLU   A  1  15  ? -0.732  -7.077  -16.922  1.00 101.29 ? 15   GLU   A OE1  1 
ATOM   207   O  OE2  . GLU   A  1  15  ? -2.121  -6.976  -18.620  1.00 99.16  ? 15   GLU   A OE2  1 
ATOM   208   H  H    . GLU   A  1  15  ? 0.135   -6.842  -22.883  1.00 78.18  ? 15   GLU   A H    1 
ATOM   209   H  HA   . GLU   A  1  15  ? 1.783   -7.852  -21.132  1.00 84.66  ? 15   GLU   A HA   1 
ATOM   210   H  HB2  . GLU   A  1  15  ? 0.078   -6.346  -20.518  1.00 93.70  ? 15   GLU   A HB2  1 
ATOM   211   H  HB3  . GLU   A  1  15  ? -0.992  -7.495  -20.765  1.00 93.70  ? 15   GLU   A HB3  1 
ATOM   212   H  HG2  . GLU   A  1  15  ? 0.048   -8.734  -19.023  1.00 101.65 ? 15   GLU   A HG2  1 
ATOM   213   H  HG3  . GLU   A  1  15  ? 0.937   -7.454  -18.713  1.00 101.65 ? 15   GLU   A HG3  1 
ATOM   214   N  N    . GLY   A  1  16  ? 1.496   -10.270 -20.909  1.00 66.34  ? 16   GLY   A N    1 
ATOM   215   C  CA   . GLY   A  1  16  ? 1.342   -11.706 -20.842  1.00 63.33  ? 16   GLY   A CA   1 
ATOM   216   C  C    . GLY   A  1  16  ? 1.856   -12.462 -22.045  1.00 60.93  ? 16   GLY   A C    1 
ATOM   217   O  O    . GLY   A  1  16  ? 1.707   -13.691 -22.093  1.00 62.24  ? 16   GLY   A O    1 
ATOM   218   H  H    . GLY   A  1  16  ? 2.215   -9.981  -20.534  1.00 79.64  ? 16   GLY   A H    1 
ATOM   219   H  HA2  . GLY   A  1  16  ? 1.819   -12.033 -20.063  1.00 76.03  ? 16   GLY   A HA2  1 
ATOM   220   H  HA3  . GLY   A  1  16  ? 0.399   -11.912 -20.744  1.00 76.03  ? 16   GLY   A HA3  1 
ATOM   221   N  N    . SER   A  1  17  ? 2.457   -11.776 -23.013  1.00 60.73  ? 17   SER   A N    1 
ATOM   222   C  CA   . SER   A  1  17  ? 2.957   -12.407 -24.226  1.00 61.25  ? 17   SER   A CA   1 
ATOM   223   C  C    . SER   A  1  17  ? 4.398   -12.881 -24.100  1.00 58.87  ? 17   SER   A C    1 
ATOM   224   O  O    . SER   A  1  17  ? 4.934   -13.445 -25.060  1.00 56.76  ? 17   SER   A O    1 
ATOM   225   C  CB   . SER   A  1  17  ? 2.850   -11.432 -25.402  1.00 62.83  ? 17   SER   A CB   1 
ATOM   226   O  OG   . SER   A  1  17  ? 3.702   -10.314 -25.218  1.00 63.81  ? 17   SER   A OG   1 
ATOM   227   H  H    . SER   A  1  17  ? 2.589   -10.927 -22.988  1.00 72.91  ? 17   SER   A H    1 
ATOM   228   H  HA   . SER   A  1  17  ? 2.405   -13.181 -24.419  1.00 73.54  ? 17   SER   A HA   1 
ATOM   229   H  HB2  . SER   A  1  17  ? 3.107   -11.892 -26.216  1.00 75.43  ? 17   SER   A HB2  1 
ATOM   230   H  HB3  . SER   A  1  17  ? 1.934   -11.121 -25.471  1.00 75.43  ? 17   SER   A HB3  1 
ATOM   231   H  HG   . SER   A  1  17  ? 3.385   -9.805  -24.629  1.00 76.60  ? 17   SER   A HG   1 
ATOM   232   N  N    . TYR   A  1  18  ? 5.035   -12.671 -22.949  1.00 58.79  ? 18   TYR   A N    1 
ATOM   233   C  CA   . TYR   A  1  18  ? 6.455   -12.979 -22.781  1.00 55.58  ? 18   TYR   A CA   1 
ATOM   234   C  C    . TYR   A  1  18  ? 7.292   -12.286 -23.853  1.00 55.34  ? 18   TYR   A C    1 
ATOM   235   O  O    . TYR   A  1  18  ? 8.321   -12.803 -24.296  1.00 53.68  ? 18   TYR   A O    1 
ATOM   236   C  CB   . TYR   A  1  18  ? 6.702   -14.490 -22.788  1.00 54.92  ? 18   TYR   A CB   1 
ATOM   237   C  CG   . TYR   A  1  18  ? 6.281   -15.200 -21.513  1.00 53.47  ? 18   TYR   A CG   1 
ATOM   238   C  CD1  . TYR   A  1  18  ? 5.570   -14.536 -20.518  1.00 55.47  ? 18   TYR   A CD1  1 
ATOM   239   C  CD2  . TYR   A  1  18  ? 6.607   -16.533 -21.302  1.00 52.04  ? 18   TYR   A CD2  1 
ATOM   240   C  CE1  . TYR   A  1  18  ? 5.192   -15.183 -19.355  1.00 57.67  ? 18   TYR   A CE1  1 
ATOM   241   C  CE2  . TYR   A  1  18  ? 6.233   -17.187 -20.142  1.00 53.20  ? 18   TYR   A CE2  1 
ATOM   242   C  CZ   . TYR   A  1  18  ? 5.527   -16.508 -19.173  1.00 56.48  ? 18   TYR   A CZ   1 
ATOM   243   O  OH   . TYR   A  1  18  ? 5.153   -17.155 -18.017  1.00 59.07  ? 18   TYR   A OH   1 
ATOM   244   H  H    . TYR   A  1  18  ? 4.664   -12.347 -22.244  1.00 70.59  ? 18   TYR   A H    1 
ATOM   245   H  HA   . TYR   A  1  18  ? 6.743   -12.642 -21.918  1.00 66.73  ? 18   TYR   A HA   1 
ATOM   246   H  HB2  . TYR   A  1  18  ? 6.201   -14.882 -23.521  1.00 65.94  ? 18   TYR   A HB2  1 
ATOM   247   H  HB3  . TYR   A  1  18  ? 7.651   -14.648 -22.912  1.00 65.94  ? 18   TYR   A HB3  1 
ATOM   248   H  HD1  . TYR   A  1  18  ? 5.346   -13.641 -20.636  1.00 66.60  ? 18   TYR   A HD1  1 
ATOM   249   H  HD2  . TYR   A  1  18  ? 7.086   -16.994 -21.952  1.00 62.49  ? 18   TYR   A HD2  1 
ATOM   250   H  HE1  . TYR   A  1  18  ? 4.714   -14.727 -18.700  1.00 69.24  ? 18   TYR   A HE1  1 
ATOM   251   H  HE2  . TYR   A  1  18  ? 6.457   -18.081 -20.017  1.00 63.88  ? 18   TYR   A HE2  1 
ATOM   252   H  HH   . TYR   A  1  18  ? 5.441   -17.944 -18.023  1.00 70.92  ? 18   TYR   A HH   1 
ATOM   253   N  N    . PHE   A  1  19  ? 6.840   -11.110 -24.280  1.00 58.65  ? 19   PHE   A N    1 
ATOM   254   C  CA   . PHE   A  1  19  ? 7.628   -10.250 -25.153  1.00 57.10  ? 19   PHE   A CA   1 
ATOM   255   C  C    . PHE   A  1  19  ? 9.013   -10.037 -24.561  1.00 57.40  ? 19   PHE   A C    1 
ATOM   256   O  O    . PHE   A  1  19  ? 9.151   -9.491  -23.463  1.00 57.26  ? 19   PHE   A O    1 
ATOM   257   C  CB   . PHE   A  1  19  ? 6.902   -8.915  -25.333  1.00 61.93  ? 19   PHE   A CB   1 
ATOM   258   C  CG   . PHE   A  1  19  ? 7.662   -7.901  -26.141  1.00 66.09  ? 19   PHE   A CG   1 
ATOM   259   C  CD1  . PHE   A  1  19  ? 8.572   -7.051  -25.533  1.00 67.14  ? 19   PHE   A CD1  1 
ATOM   260   C  CD2  . PHE   A  1  19  ? 7.445   -7.777  -27.503  1.00 69.03  ? 19   PHE   A CD2  1 
ATOM   261   C  CE1  . PHE   A  1  19  ? 9.264   -6.111  -26.271  1.00 71.60  ? 19   PHE   A CE1  1 
ATOM   262   C  CE2  . PHE   A  1  19  ? 8.132   -6.837  -28.247  1.00 72.66  ? 19   PHE   A CE2  1 
ATOM   263   C  CZ   . PHE   A  1  19  ? 9.042   -6.002  -27.629  1.00 73.93  ? 19   PHE   A CZ   1 
ATOM   264   H  H    . PHE   A  1  19  ? 6.071   -10.784 -24.076  1.00 70.42  ? 19   PHE   A H    1 
ATOM   265   H  HA   . PHE   A  1  19  ? 7.729   -10.660 -26.027  1.00 68.55  ? 19   PHE   A HA   1 
ATOM   266   H  HB2  . PHE   A  1  19  ? 6.059   -9.079  -25.785  1.00 74.36  ? 19   PHE   A HB2  1 
ATOM   267   H  HB3  . PHE   A  1  19  ? 6.739   -8.530  -24.457  1.00 74.36  ? 19   PHE   A HB3  1 
ATOM   268   H  HD1  . PHE   A  1  19  ? 8.719   -7.115  -24.617  1.00 80.60  ? 19   PHE   A HD1  1 
ATOM   269   H  HD2  . PHE   A  1  19  ? 6.829   -8.334  -27.922  1.00 82.87  ? 19   PHE   A HD2  1 
ATOM   270   H  HE1  . PHE   A  1  19  ? 9.879   -5.552  -25.854  1.00 85.96  ? 19   PHE   A HE1  1 
ATOM   271   H  HE2  . PHE   A  1  19  ? 7.983   -6.768  -29.162  1.00 87.23  ? 19   PHE   A HE2  1 
ATOM   272   H  HZ   . PHE   A  1  19  ? 9.504   -5.367  -28.128  1.00 88.75  ? 19   PHE   A HZ   1 
ATOM   273   N  N    . GLY   A  1  20  ? 10.039  -10.475 -25.287  1.00 55.22  ? 20   GLY   A N    1 
ATOM   274   C  CA   . GLY   A  1  20  ? 11.406  -10.412 -24.811  1.00 55.55  ? 20   GLY   A CA   1 
ATOM   275   C  C    . GLY   A  1  20  ? 11.990  -11.745 -24.397  1.00 52.85  ? 20   GLY   A C    1 
ATOM   276   O  O    . GLY   A  1  20  ? 13.131  -11.780 -23.921  1.00 48.10  ? 20   GLY   A O    1 
ATOM   277   H  H    . GLY   A  1  20  ? 9.961   -10.818 -26.072  1.00 66.30  ? 20   GLY   A H    1 
ATOM   278   H  HA2  . GLY   A  1  20  ? 11.966  -10.048 -25.515  1.00 66.70  ? 20   GLY   A HA2  1 
ATOM   279   H  HA3  . GLY   A  1  20  ? 11.442  -9.820  -24.042  1.00 66.70  ? 20   GLY   A HA3  1 
ATOM   280   N  N    . PHE   A  1  21  ? 11.244  -12.841 -24.551  1.00 53.02  ? 21   PHE   A N    1 
ATOM   281   C  CA   . PHE   A  1  21  ? 11.779  -14.166 -24.260  1.00 49.82  ? 21   PHE   A CA   1 
ATOM   282   C  C    . PHE   A  1  21  ? 12.963  -14.506 -25.155  1.00 50.75  ? 21   PHE   A C    1 
ATOM   283   O  O    . PHE   A  1  21  ? 13.789  -15.348 -24.784  1.00 52.29  ? 21   PHE   A O    1 
ATOM   284   C  CB   . PHE   A  1  21  ? 10.668  -15.205 -24.426  1.00 50.74  ? 21   PHE   A CB   1 
ATOM   285   C  CG   . PHE   A  1  21  ? 11.024  -16.572 -23.917  1.00 49.97  ? 21   PHE   A CG   1 
ATOM   286   C  CD1  . PHE   A  1  21  ? 10.916  -16.874 -22.570  1.00 51.39  ? 21   PHE   A CD1  1 
ATOM   287   C  CD2  . PHE   A  1  21  ? 11.445  -17.561 -24.790  1.00 46.14  ? 21   PHE   A CD2  1 
ATOM   288   C  CE1  . PHE   A  1  21  ? 11.234  -18.135 -22.101  1.00 50.78  ? 21   PHE   A CE1  1 
ATOM   289   C  CE2  . PHE   A  1  21  ? 11.765  -18.823 -24.327  1.00 45.82  ? 21   PHE   A CE2  1 
ATOM   290   C  CZ   . PHE   A  1  21  ? 11.659  -19.111 -22.981  1.00 48.43  ? 21   PHE   A CZ   1 
ATOM   291   H  H    . PHE   A  1  21  ? 10.428  -12.842 -24.821  1.00 63.66  ? 21   PHE   A H    1 
ATOM   292   H  HA   . PHE   A  1  21  ? 12.089  -14.199 -23.341  1.00 59.82  ? 21   PHE   A HA   1 
ATOM   293   H  HB2  . PHE   A  1  21  ? 9.886   -14.903 -23.937  1.00 60.92  ? 21   PHE   A HB2  1 
ATOM   294   H  HB3  . PHE   A  1  21  ? 10.458  -15.287 -25.369  1.00 60.92  ? 21   PHE   A HB3  1 
ATOM   295   H  HD1  . PHE   A  1  21  ? 10.626  -16.222 -21.974  1.00 61.71  ? 21   PHE   A HD1  1 
ATOM   296   H  HD2  . PHE   A  1  21  ? 11.514  -17.374 -25.698  1.00 55.40  ? 21   PHE   A HD2  1 
ATOM   297   H  HE1  . PHE   A  1  21  ? 11.162  -18.326 -21.194  1.00 60.97  ? 21   PHE   A HE1  1 
ATOM   298   H  HE2  . PHE   A  1  21  ? 12.051  -19.479 -24.922  1.00 55.03  ? 21   PHE   A HE2  1 
ATOM   299   H  HZ   . PHE   A  1  21  ? 11.873  -19.960 -22.668  1.00 58.15  ? 21   PHE   A HZ   1 
ATOM   300   N  N    . ALA   A  1  22  ? 13.062  -13.866 -26.318  1.00 51.06  ? 22   ALA   A N    1 
ATOM   301   C  CA   . ALA   A  1  22  ? 14.156  -14.078 -27.254  1.00 53.20  ? 22   ALA   A CA   1 
ATOM   302   C  C    . ALA   A  1  22  ? 14.398  -12.769 -27.989  1.00 54.79  ? 22   ALA   A C    1 
ATOM   303   O  O    . ALA   A  1  22  ? 13.450  -12.031 -28.272  1.00 55.26  ? 22   ALA   A O    1 
ATOM   304   C  CB   . ALA   A  1  22  ? 13.837  -15.202 -28.244  1.00 54.72  ? 22   ALA   A CB   1 
ATOM   305   H  H    . ALA   A  1  22  ? 12.489  -13.287 -26.594  1.00 61.31  ? 22   ALA   A H    1 
ATOM   306   H  HA   . ALA   A  1  22  ? 14.965  -14.327 -26.780  1.00 63.87  ? 22   ALA   A HA   1 
ATOM   307   H  HB1  . ALA   A  1  22  ? 14.590  -15.317 -28.845  1.00 65.70  ? 22   ALA   A HB1  1 
ATOM   308   H  HB2  . ALA   A  1  22  ? 13.679  -16.022 -27.751  1.00 65.70  ? 22   ALA   A HB2  1 
ATOM   309   H  HB3  . ALA   A  1  22  ? 13.044  -14.962 -28.750  1.00 65.70  ? 22   ALA   A HB3  1 
ATOM   310   N  N    . VAL   A  1  23  ? 15.661  -12.480 -28.292  1.00 51.88  ? 23   VAL   A N    1 
ATOM   311   C  CA   . VAL   A  1  23  ? 16.036  -11.218 -28.918  1.00 51.72  ? 23   VAL   A CA   1 
ATOM   312   C  C    . VAL   A  1  23  ? 17.188  -11.449 -29.883  1.00 55.22  ? 23   VAL   A C    1 
ATOM   313   O  O    . VAL   A  1  23  ? 18.070  -12.277 -29.632  1.00 59.21  ? 23   VAL   A O    1 
ATOM   314   C  CB   . VAL   A  1  23  ? 16.425  -10.154 -27.871  1.00 51.59  ? 23   VAL   A CB   1 
ATOM   315   C  CG1  . VAL   A  1  23  ? 15.185  -9.595  -27.195  1.00 53.48  ? 23   VAL   A CG1  1 
ATOM   316   C  CG2  . VAL   A  1  23  ? 17.382  -10.743 -26.844  1.00 54.00  ? 23   VAL   A CG2  1 
ATOM   317   H  H    . VAL   A  1  23  ? 16.325  -13.005 -28.142  1.00 62.29  ? 23   VAL   A H    1 
ATOM   318   H  HA   . VAL   A  1  23  ? 15.276  -10.895 -29.429  1.00 62.10  ? 23   VAL   A HA   1 
ATOM   319   H  HB   . VAL   A  1  23  ? 16.878  -9.422  -28.318  1.00 61.94  ? 23   VAL   A HB   1 
ATOM   320   H  HG11 . VAL   A  1  23  ? 15.432  -8.809  -26.682  1.00 64.22  ? 23   VAL   A HG11 1 
ATOM   321   H  HG12 . VAL   A  1  23  ? 14.535  -9.356  -27.874  1.00 64.22  ? 23   VAL   A HG12 1 
ATOM   322   H  HG13 . VAL   A  1  23  ? 14.815  -10.271 -26.606  1.00 64.22  ? 23   VAL   A HG13 1 
ATOM   323   H  HG21 . VAL   A  1  23  ? 17.595  -10.064 -26.185  1.00 64.84  ? 23   VAL   A HG21 1 
ATOM   324   H  HG22 . VAL   A  1  23  ? 16.957  -11.500 -26.413  1.00 64.84  ? 23   VAL   A HG22 1 
ATOM   325   H  HG23 . VAL   A  1  23  ? 18.191  -11.030 -27.295  1.00 64.84  ? 23   VAL   A HG23 1 
ATOM   326   N  N    . ASP   A  1  24  ? 17.181  -10.704 -30.987  1.00 54.51  ? 24   ASP   A N    1 
ATOM   327   C  CA   . ASP   A  1  24  ? 18.277  -10.744 -31.941  1.00 55.76  ? 24   ASP   A CA   1 
ATOM   328   C  C    . ASP   A  1  24  ? 18.265  -9.465  -32.762  1.00 60.19  ? 24   ASP   A C    1 
ATOM   329   O  O    . ASP   A  1  24  ? 17.240  -8.788  -32.880  1.00 65.13  ? 24   ASP   A O    1 
ATOM   330   C  CB   . ASP   A  1  24  ? 18.183  -11.963 -32.861  1.00 58.27  ? 24   ASP   A CB   1 
ATOM   331   C  CG   . ASP   A  1  24  ? 19.511  -12.310 -33.497  1.00 62.89  ? 24   ASP   A CG   1 
ATOM   332   O  OD1  . ASP   A  1  24  ? 20.387  -11.424 -33.580  1.00 63.78  ? 24   ASP   A OD1  1 
ATOM   333   O  OD2  . ASP   A  1  24  ? 19.682  -13.469 -33.916  1.00 67.22  ? 24   ASP   A OD2  1 
ATOM   334   H  H    . ASP   A  1  24  ? 16.547  -10.165 -31.204  1.00 65.45  ? 24   ASP   A H    1 
ATOM   335   H  HA   . ASP   A  1  24  ? 19.115  -10.790 -31.454  1.00 66.95  ? 24   ASP   A HA   1 
ATOM   336   H  HB2  . ASP   A  1  24  ? 17.888  -12.729 -32.344  1.00 69.96  ? 24   ASP   A HB2  1 
ATOM   337   H  HB3  . ASP   A  1  24  ? 17.549  -11.777 -33.571  1.00 69.96  ? 24   ASP   A HB3  1 
ATOM   338   N  N    . PHE   A  1  25  ? 19.425  -9.144  -33.325  1.00 61.11  ? 25   PHE   A N    1 
ATOM   339   C  CA   . PHE   A  1  25  ? 19.547  -8.034  -34.256  1.00 61.22  ? 25   PHE   A CA   1 
ATOM   340   C  C    . PHE   A  1  25  ? 19.170  -8.484  -35.663  1.00 62.51  ? 25   PHE   A C    1 
ATOM   341   O  O    . PHE   A  1  25  ? 19.396  -9.634  -36.050  1.00 61.41  ? 25   PHE   A O    1 
ATOM   342   C  CB   . PHE   A  1  25  ? 20.975  -7.489  -34.262  1.00 59.96  ? 25   PHE   A CB   1 
ATOM   343   C  CG   . PHE   A  1  25  ? 21.305  -6.615  -33.085  1.00 58.21  ? 25   PHE   A CG   1 
ATOM   344   C  CD1  . PHE   A  1  25  ? 20.849  -5.309  -33.031  1.00 60.98  ? 25   PHE   A CD1  1 
ATOM   345   C  CD2  . PHE   A  1  25  ? 22.087  -7.092  -32.045  1.00 57.61  ? 25   PHE   A CD2  1 
ATOM   346   C  CE1  . PHE   A  1  25  ? 21.157  -4.495  -31.958  1.00 63.50  ? 25   PHE   A CE1  1 
ATOM   347   C  CE2  . PHE   A  1  25  ? 22.404  -6.278  -30.969  1.00 59.23  ? 25   PHE   A CE2  1 
ATOM   348   C  CZ   . PHE   A  1  25  ? 21.938  -4.978  -30.929  1.00 61.69  ? 25   PHE   A CZ   1 
ATOM   349   H  H    . PHE   A  1  25  ? 20.165  -9.560  -33.181  1.00 73.36  ? 25   PHE   A H    1 
ATOM   350   H  HA   . PHE   A  1  25  ? 18.950  -7.319  -33.985  1.00 73.50  ? 25   PHE   A HA   1 
ATOM   351   H  HB2  . PHE   A  1  25  ? 21.592  -8.237  -34.255  1.00 71.99  ? 25   PHE   A HB2  1 
ATOM   352   H  HB3  . PHE   A  1  25  ? 21.102  -6.961  -35.066  1.00 71.99  ? 25   PHE   A HB3  1 
ATOM   353   H  HD1  . PHE   A  1  25  ? 20.328  -4.975  -33.725  1.00 73.21  ? 25   PHE   A HD1  1 
ATOM   354   H  HD2  . PHE   A  1  25  ? 22.402  -7.966  -32.068  1.00 69.17  ? 25   PHE   A HD2  1 
ATOM   355   H  HE1  . PHE   A  1  25  ? 20.838  -3.622  -31.930  1.00 76.24  ? 25   PHE   A HE1  1 
ATOM   356   H  HE2  . PHE   A  1  25  ? 22.930  -6.606  -30.276  1.00 71.12  ? 25   PHE   A HE2  1 
ATOM   357   H  HZ   . PHE   A  1  25  ? 22.151  -4.430  -30.208  1.00 74.06  ? 25   PHE   A HZ   1 
ATOM   358   N  N    . PHE   A  1  26  ? 18.593  -7.563  -36.432  1.00 64.24  ? 26   PHE   A N    1 
ATOM   359   C  CA   . PHE   A  1  26  ? 18.239  -7.814  -37.825  1.00 59.47  ? 26   PHE   A CA   1 
ATOM   360   C  C    . PHE   A  1  26  ? 18.970  -6.814  -38.708  1.00 73.11  ? 26   PHE   A C    1 
ATOM   361   O  O    . PHE   A  1  26  ? 18.772  -5.602  -38.573  1.00 73.10  ? 26   PHE   A O    1 
ATOM   362   C  CB   . PHE   A  1  26  ? 16.727  -7.718  -38.043  1.00 71.16  ? 26   PHE   A CB   1 
ATOM   363   C  CG   . PHE   A  1  26  ? 16.296  -8.046  -39.446  1.00 74.26  ? 26   PHE   A CG   1 
ATOM   364   C  CD1  . PHE   A  1  26  ? 16.836  -9.133  -40.113  1.00 62.43  ? 26   PHE   A CD1  1 
ATOM   365   C  CD2  . PHE   A  1  26  ? 15.343  -7.276  -40.093  1.00 77.72  ? 26   PHE   A CD2  1 
ATOM   366   C  CE1  . PHE   A  1  26  ? 16.444  -9.442  -41.400  1.00 76.90  ? 26   PHE   A CE1  1 
ATOM   367   C  CE2  . PHE   A  1  26  ? 14.944  -7.582  -41.381  1.00 66.62  ? 26   PHE   A CE2  1 
ATOM   368   C  CZ   . PHE   A  1  26  ? 15.496  -8.667  -42.035  1.00 67.02  ? 26   PHE   A CZ   1 
ATOM   369   H  H    . PHE   A  1  26  ? 18.393  -6.771  -36.163  1.00 77.12  ? 26   PHE   A H    1 
ATOM   370   H  HA   . PHE   A  1  26  ? 18.526  -8.708  -38.070  1.00 71.19  ? 26   PHE   A HA   1 
ATOM   371   H  HB2  . PHE   A  1  26  ? 16.285  -8.339  -37.444  1.00 85.43  ? 26   PHE   A HB2  1 
ATOM   372   H  HB3  . PHE   A  1  26  ? 16.442  -6.811  -37.850  1.00 85.43  ? 26   PHE   A HB3  1 
ATOM   373   H  HD1  . PHE   A  1  26  ? 17.472  -9.663  -39.688  1.00 74.74  ? 26   PHE   A HD1  1 
ATOM   374   H  HD2  . PHE   A  1  26  ? 14.968  -6.546  -39.656  1.00 93.30  ? 26   PHE   A HD2  1 
ATOM   375   H  HE1  . PHE   A  1  26  ? 16.818  -10.172 -41.838  1.00 92.32  ? 26   PHE   A HE1  1 
ATOM   376   H  HE2  . PHE   A  1  26  ? 14.306  -7.057  -41.807  1.00 79.76  ? 26   PHE   A HE2  1 
ATOM   377   H  HZ   . PHE   A  1  26  ? 15.229  -8.874  -42.901  1.00 80.24  ? 26   PHE   A HZ   1 
ATOM   378   N  N    . VAL   A  1  27  ? 19.808  -7.322  -39.607  1.00 75.90  ? 27   VAL   A N    1 
ATOM   379   C  CA   . VAL   A  1  27  ? 20.545  -6.481  -40.547  1.00 78.12  ? 27   VAL   A CA   1 
ATOM   380   C  C    . VAL   A  1  27  ? 20.252  -6.951  -41.969  1.00 82.76  ? 27   VAL   A C    1 
ATOM   381   O  O    . VAL   A  1  27  ? 20.711  -8.028  -42.374  1.00 81.25  ? 27   VAL   A O    1 
ATOM   382   C  CB   . VAL   A  1  27  ? 22.056  -6.497  -40.250  1.00 76.95  ? 27   VAL   A CB   1 
ATOM   383   C  CG1  . VAL   A  1  27  ? 22.333  -5.898  -38.878  1.00 71.25  ? 27   VAL   A CG1  1 
ATOM   384   C  CG2  . VAL   A  1  27  ? 22.628  -7.911  -40.335  1.00 79.50  ? 27   VAL   A CG2  1 
ATOM   385   H  H    . VAL   A  1  27  ? 19.970  -8.163  -39.694  1.00 91.12  ? 27   VAL   A H    1 
ATOM   386   H  HA   . VAL   A  1  27  ? 20.232  -5.567  -40.462  1.00 93.78  ? 27   VAL   A HA   1 
ATOM   387   H  HB   . VAL   A  1  27  ? 22.501  -5.958  -40.923  1.00 92.37  ? 27   VAL   A HB   1 
ATOM   388   H  HG11 . VAL   A  1  27  ? 23.291  -5.888  -38.726  1.00 85.54  ? 27   VAL   A HG11 1 
ATOM   389   H  HG12 . VAL   A  1  27  ? 21.984  -4.994  -38.852  1.00 85.54  ? 27   VAL   A HG12 1 
ATOM   390   H  HG13 . VAL   A  1  27  ? 21.896  -6.441  -38.203  1.00 85.54  ? 27   VAL   A HG13 1 
ATOM   391   H  HG21 . VAL   A  1  27  ? 23.542  -7.901  -40.011  1.00 95.43  ? 27   VAL   A HG21 1 
ATOM   392   H  HG22 . VAL   A  1  27  ? 22.089  -8.503  -39.788  1.00 95.43  ? 27   VAL   A HG22 1 
ATOM   393   H  HG23 . VAL   A  1  27  ? 22.608  -8.205  -41.259  1.00 95.43  ? 27   VAL   A HG23 1 
ATOM   394   N  N    . PRO   A  1  28  ? 19.476  -6.204  -42.754  1.00 93.03  ? 28   PRO   A N    1 
ATOM   395   C  CA   . PRO   A  1  28  ? 19.286  -6.583  -44.158  1.00 102.52 ? 28   PRO   A CA   1 
ATOM   396   C  C    . PRO   A  1  28  ? 20.586  -6.495  -44.943  1.00 114.49 ? 28   PRO   A C    1 
ATOM   397   O  O    . PRO   A  1  28  ? 21.495  -5.733  -44.608  1.00 120.13 ? 28   PRO   A O    1 
ATOM   398   C  CB   . PRO   A  1  28  ? 18.252  -5.571  -44.664  1.00 103.53 ? 28   PRO   A CB   1 
ATOM   399   C  CG   . PRO   A  1  28  ? 17.511  -5.155  -43.443  1.00 98.77  ? 28   PRO   A CG   1 
ATOM   400   C  CD   . PRO   A  1  28  ? 18.531  -5.151  -42.340  1.00 94.42  ? 28   PRO   A CD   1 
ATOM   401   H  HA   . PRO   A  1  28  ? 18.927  -7.481  -44.226  1.00 123.06 ? 28   PRO   A HA   1 
ATOM   402   H  HB2  . PRO   A  1  28  ? 18.701  -4.815  -45.074  1.00 124.27 ? 28   PRO   A HB2  1 
ATOM   403   H  HB3  . PRO   A  1  28  ? 17.660  -5.993  -45.305  1.00 124.27 ? 28   PRO   A HB3  1 
ATOM   404   H  HG2  . PRO   A  1  28  ? 17.137  -4.270  -43.571  1.00 118.56 ? 28   PRO   A HG2  1 
ATOM   405   H  HG3  . PRO   A  1  28  ? 16.802  -5.791  -43.256  1.00 118.56 ? 28   PRO   A HG3  1 
ATOM   406   H  HD2  . PRO   A  1  28  ? 18.975  -4.291  -42.284  1.00 113.35 ? 28   PRO   A HD2  1 
ATOM   407   H  HD3  . PRO   A  1  28  ? 18.121  -5.370  -41.489  1.00 113.35 ? 28   PRO   A HD3  1 
ATOM   408   N  N    . SER   A  1  29  ? 20.658  -7.293  -46.011  1.00 124.88 ? 29   SER   A N    1 
ATOM   409   C  CA   . SER   A  1  29  ? 21.876  -7.381  -46.806  1.00 138.24 ? 29   SER   A CA   1 
ATOM   410   C  C    . SER   A  1  29  ? 22.139  -6.125  -47.628  1.00 151.54 ? 29   SER   A C    1 
ATOM   411   O  O    . SER   A  1  29  ? 23.276  -5.916  -48.063  1.00 159.04 ? 29   SER   A O    1 
ATOM   412   C  CB   . SER   A  1  29  ? 21.796  -8.596  -47.732  1.00 141.79 ? 29   SER   A CB   1 
ATOM   413   O  OG   . SER   A  1  29  ? 23.012  -8.791  -48.431  1.00 146.18 ? 29   SER   A OG   1 
ATOM   414   H  H    . SER   A  1  29  ? 20.016  -7.790  -46.293  1.00 149.90 ? 29   SER   A H    1 
ATOM   415   H  HA   . SER   A  1  29  ? 22.629  -7.498  -46.206  1.00 165.92 ? 29   SER   A HA   1 
ATOM   416   H  HB2  . SER   A  1  29  ? 21.610  -9.385  -47.199  1.00 170.19 ? 29   SER   A HB2  1 
ATOM   417   H  HB3  . SER   A  1  29  ? 21.084  -8.455  -48.375  1.00 170.19 ? 29   SER   A HB3  1 
ATOM   418   H  HG   . SER   A  1  29  ? 23.067  -9.586  -48.697  1.00 175.45 ? 29   SER   A HG   1 
ATOM   419   N  N    . ALA   A  1  30  ? 21.125  -5.285  -47.850  1.00 153.53 ? 30   ALA   A N    1 
ATOM   420   C  CA   . ALA   A  1  30  ? 21.272  -4.090  -48.673  1.00 161.85 ? 30   ALA   A CA   1 
ATOM   421   C  C    . ALA   A  1  30  ? 21.687  -2.864  -47.865  1.00 159.71 ? 30   ALA   A C    1 
ATOM   422   O  O    . ALA   A  1  30  ? 21.403  -1.731  -48.277  1.00 168.45 ? 30   ALA   A O    1 
ATOM   423   C  CB   . ALA   A  1  30  ? 19.973  -3.812  -49.430  1.00 168.06 ? 30   ALA   A CB   1 
ATOM   424   H  H    . ALA   A  1  30  ? 20.334  -5.391  -47.530  1.00 184.28 ? 30   ALA   A H    1 
ATOM   425   H  HA   . ALA   A  1  30  ? 21.970  -4.258  -49.326  1.00 194.26 ? 30   ALA   A HA   1 
ATOM   426   H  HB1  . ALA   A  1  30  ? 20.106  -3.053  -50.018  1.00 201.70 ? 30   ALA   A HB1  1 
ATOM   427   H  HB2  . ALA   A  1  30  ? 19.737  -4.596  -49.950  1.00 201.70 ? 30   ALA   A HB2  1 
ATOM   428   H  HB3  . ALA   A  1  30  ? 19.270  -3.616  -48.790  1.00 201.70 ? 30   ALA   A HB3  1 
ATOM   429   N  N    . SER   A  1  31  ? 22.354  -3.062  -46.727  1.00 149.22 ? 31   SER   A N    1 
ATOM   430   C  CA   . SER   A  1  31  ? 22.839  -1.959  -45.896  1.00 143.75 ? 31   SER   A CA   1 
ATOM   431   C  C    . SER   A  1  31  ? 21.729  -0.948  -45.619  1.00 137.29 ? 31   SER   A C    1 
ATOM   432   O  O    . SER   A  1  31  ? 21.951  0.265   -45.602  1.00 139.77 ? 31   SER   A O    1 
ATOM   433   C  CB   . SER   A  1  31  ? 24.044  -1.274  -46.545  1.00 150.08 ? 31   SER   A CB   1 
ATOM   434   O  OG   . SER   A  1  31  ? 23.647  -0.470  -47.642  1.00 157.98 ? 31   SER   A OG   1 
ATOM   435   H  H    . SER   A  1  31  ? 22.542  -3.839  -46.410  1.00 179.10 ? 31   SER   A H    1 
ATOM   436   H  HA   . SER   A  1  31  ? 23.122  -2.325  -45.044  1.00 172.53 ? 31   SER   A HA   1 
ATOM   437   H  HB2  . SER   A  1  31  ? 24.479  -0.712  -45.884  1.00 180.14 ? 31   SER   A HB2  1 
ATOM   438   H  HB3  . SER   A  1  31  ? 24.660  -1.954  -46.860  1.00 180.14 ? 31   SER   A HB3  1 
ATOM   439   H  HG   . SER   A  1  31  ? 23.237  0.210   -47.367  1.00 189.62 ? 31   SER   A HG   1 
ATOM   440   N  N    . SER   A  1  32  ? 20.521  -1.455  -45.403  1.00 130.73 ? 32   SER   A N    1 
ATOM   441   C  CA   . SER   A  1  32  ? 19.377  -0.615  -45.091  1.00 131.04 ? 32   SER   A CA   1 
ATOM   442   C  C    . SER   A  1  32  ? 19.341  -0.361  -43.585  1.00 127.17 ? 32   SER   A C    1 
ATOM   443   O  O    . SER   A  1  32  ? 20.293  -0.661  -42.859  1.00 123.81 ? 32   SER   A O    1 
ATOM   444   C  CB   . SER   A  1  32  ? 18.091  -1.269  -45.591  1.00 132.43 ? 32   SER   A CB   1 
ATOM   445   O  OG   . SER   A  1  32  ? 18.109  -1.408  -47.000  1.00 138.72 ? 32   SER   A OG   1 
ATOM   446   H  H    . SER   A  1  32  ? 20.337  -2.295  -45.433  1.00 156.92 ? 32   SER   A H    1 
ATOM   447   H  HA   . SER   A  1  32  ? 19.482  0.234   -45.548  1.00 157.29 ? 32   SER   A HA   1 
ATOM   448   H  HB2  . SER   A  1  32  ? 18.007  -2.147  -45.188  1.00 158.96 ? 32   SER   A HB2  1 
ATOM   449   H  HB3  . SER   A  1  32  ? 17.337  -0.714  -45.338  1.00 158.96 ? 32   SER   A HB3  1 
ATOM   450   H  HG   . SER   A  1  32  ? 18.243  -0.662  -47.361  1.00 166.50 ? 32   SER   A HG   1 
ATOM   451   N  N    . ARG   A  1  33  ? 18.239  0.203   -43.098  1.00 124.51 ? 33   ARG   A N    1 
ATOM   452   C  CA   . ARG   A  1  33  ? 18.086  0.391   -41.665  1.00 119.21 ? 33   ARG   A CA   1 
ATOM   453   C  C    . ARG   A  1  33  ? 18.197  -0.946  -40.945  1.00 111.42 ? 33   ARG   A C    1 
ATOM   454   O  O    . ARG   A  1  33  ? 17.895  -2.006  -41.501  1.00 113.38 ? 33   ARG   A O    1 
ATOM   455   C  CB   . ARG   A  1  33  ? 16.739  1.038   -41.344  1.00 121.64 ? 33   ARG   A CB   1 
ATOM   456   C  CG   . ARG   A  1  33  ? 16.607  2.468   -41.823  1.00 128.17 ? 33   ARG   A CG   1 
ATOM   457   C  CD   . ARG   A  1  33  ? 15.267  3.053   -41.418  1.00 130.90 ? 33   ARG   A CD   1 
ATOM   458   N  NE   . ARG   A  1  33  ? 15.082  4.408   -41.928  1.00 143.12 ? 33   ARG   A NE   1 
ATOM   459   C  CZ   . ARG   A  1  33  ? 13.963  5.111   -41.796  1.00 151.16 ? 33   ARG   A CZ   1 
ATOM   460   N  NH1  . ARG   A  1  33  ? 13.887  6.337   -42.294  1.00 154.07 ? 33   ARG   A NH1  1 
ATOM   461   N  NH2  . ARG   A  1  33  ? 12.916  4.590   -41.168  1.00 154.46 ? 33   ARG   A NH2  1 
ATOM   462   H  H    . ARG   A  1  33  ? 17.577  0.481   -43.571  1.00 149.45 ? 33   ARG   A H    1 
ATOM   463   H  HA   . ARG   A  1  33  ? 18.785  0.982   -41.343  1.00 143.08 ? 33   ARG   A HA   1 
ATOM   464   H  HB2  . ARG   A  1  33  ? 16.038  0.519   -41.769  1.00 146.00 ? 33   ARG   A HB2  1 
ATOM   465   H  HB3  . ARG   A  1  33  ? 16.616  1.037   -40.382  1.00 146.00 ? 33   ARG   A HB3  1 
ATOM   466   H  HG2  . ARG   A  1  33  ? 17.309  3.007   -41.428  1.00 153.84 ? 33   ARG   A HG2  1 
ATOM   467   H  HG3  . ARG   A  1  33  ? 16.673  2.493   -42.790  1.00 153.84 ? 33   ARG   A HG3  1 
ATOM   468   H  HD2  . ARG   A  1  33  ? 14.556  2.497   -41.772  1.00 157.12 ? 33   ARG   A HD2  1 
ATOM   469   H  HD3  . ARG   A  1  33  ? 15.212  3.085   -40.450  1.00 157.12 ? 33   ARG   A HD3  1 
ATOM   470   H  HE   . ARG   A  1  33  ? 15.741  4.775   -42.342  1.00 171.78 ? 33   ARG   A HE   1 
ATOM   471   H  HH11 . ARG   A  1  33  ? 14.563  6.677   -42.703  1.00 184.93 ? 33   ARG   A HH11 1 
ATOM   472   H  HH12 . ARG   A  1  33  ? 13.163  6.793   -42.208  1.00 184.93 ? 33   ARG   A HH12 1 
ATOM   473   H  HH21 . ARG   A  1  33  ? 12.961  3.794   -40.845  1.00 185.39 ? 33   ARG   A HH21 1 
ATOM   474   H  HH22 . ARG   A  1  33  ? 12.193  5.048   -41.084  1.00 185.39 ? 33   ARG   A HH22 1 
ATOM   475   N  N    . MET   A  1  34  ? 18.643  -0.887  -39.699  1.00 101.60 ? 34   MET   A N    1 
ATOM   476   C  CA   . MET   A  1  34  ? 18.720  -2.055  -38.838  1.00 91.50  ? 34   MET   A CA   1 
ATOM   477   C  C    . MET   A  1  34  ? 17.525  -2.063  -37.895  1.00 88.55  ? 34   MET   A C    1 
ATOM   478   O  O    . MET   A  1  34  ? 16.978  -1.013  -37.548  1.00 88.24  ? 34   MET   A O    1 
ATOM   479   C  CB   . MET   A  1  34  ? 20.029  -2.054  -38.049  1.00 84.70  ? 34   MET   A CB   1 
ATOM   480   C  CG   . MET   A  1  34  ? 21.264  -2.085  -38.940  1.00 82.70  ? 34   MET   A CG   1 
ATOM   481   S  SD   . MET   A  1  34  ? 22.804  -1.750  -38.065  1.00 86.21  ? 34   MET   A SD   1 
ATOM   482   C  CE   . MET   A  1  34  ? 23.994  -2.475  -39.192  1.00 89.95  ? 34   MET   A CE   1 
ATOM   483   H  H    . MET   A  1  34  ? 18.912  -0.163  -39.321  1.00 121.96 ? 34   MET   A H    1 
ATOM   484   H  HA   . MET   A  1  34  ? 18.708  -2.865  -39.371  1.00 109.83 ? 34   MET   A HA   1 
ATOM   485   H  HB2  . MET   A  1  34  ? 20.071  -1.249  -37.509  1.00 101.68 ? 34   MET   A HB2  1 
ATOM   486   H  HB3  . MET   A  1  34  ? 20.053  -2.838  -37.479  1.00 101.68 ? 34   MET   A HB3  1 
ATOM   487   H  HG2  . MET   A  1  34  ? 21.338  -2.966  -39.340  1.00 99.27  ? 34   MET   A HG2  1 
ATOM   488   H  HG3  . MET   A  1  34  ? 21.166  -1.413  -39.633  1.00 99.27  ? 34   MET   A HG3  1 
ATOM   489   H  HE1  . MET   A  1  34  ? 24.882  -2.389  -38.811  1.00 107.98 ? 34   MET   A HE1  1 
ATOM   490   H  HE2  . MET   A  1  34  ? 23.777  -3.412  -39.320  1.00 107.98 ? 34   MET   A HE2  1 
ATOM   491   H  HE3  . MET   A  1  34  ? 23.951  -2.007  -40.040  1.00 107.98 ? 34   MET   A HE3  1 
ATOM   492   N  N    . PHE   A  1  35  ? 17.111  -3.263  -37.497  1.00 85.77  ? 35   PHE   A N    1 
ATOM   493   C  CA   . PHE   A  1  35  ? 15.951  -3.438  -36.639  1.00 82.86  ? 35   PHE   A CA   1 
ATOM   494   C  C    . PHE   A  1  35  ? 16.281  -4.410  -35.519  1.00 74.97  ? 35   PHE   A C    1 
ATOM   495   O  O    . PHE   A  1  35  ? 17.348  -5.030  -35.488  1.00 74.49  ? 35   PHE   A O    1 
ATOM   496   C  CB   . PHE   A  1  35  ? 14.741  -3.953  -37.427  1.00 63.67  ? 35   PHE   A CB   1 
ATOM   497   C  CG   . PHE   A  1  35  ? 14.409  -3.124  -38.624  1.00 76.81  ? 35   PHE   A CG   1 
ATOM   498   C  CD1  . PHE   A  1  35  ? 14.975  -3.410  -39.853  1.00 75.77  ? 35   PHE   A CD1  1 
ATOM   499   C  CD2  . PHE   A  1  35  ? 13.539  -2.054  -38.521  1.00 80.46  ? 35   PHE   A CD2  1 
ATOM   500   C  CE1  . PHE   A  1  35  ? 14.676  -2.647  -40.960  1.00 78.22  ? 35   PHE   A CE1  1 
ATOM   501   C  CE2  . PHE   A  1  35  ? 13.235  -1.286  -39.624  1.00 83.69  ? 35   PHE   A CE2  1 
ATOM   502   C  CZ   . PHE   A  1  35  ? 13.804  -1.582  -40.847  1.00 80.92  ? 35   PHE   A CZ   1 
ATOM   503   H  H    . PHE   A  1  35  ? 17.495  -4.001  -37.716  1.00 102.96 ? 35   PHE   A H    1 
ATOM   504   H  HA   . PHE   A  1  35  ? 15.726  -2.581  -36.245  1.00 99.47  ? 35   PHE   A HA   1 
ATOM   505   H  HB2  . PHE   A  1  35  ? 14.927  -4.854  -37.732  1.00 76.22  ? 35   PHE   A HB2  1 
ATOM   506   H  HB3  . PHE   A  1  35  ? 13.966  -3.953  -36.843  1.00 76.22  ? 35   PHE   A HB3  1 
ATOM   507   H  HD1  . PHE   A  1  35  ? 15.563  -4.125  -39.933  1.00 90.96  ? 35   PHE   A HD1  1 
ATOM   508   H  HD2  . PHE   A  1  35  ? 13.155  -1.851  -37.699  1.00 96.58  ? 35   PHE   A HD2  1 
ATOM   509   H  HE1  . PHE   A  1  35  ? 15.060  -2.849  -41.783  1.00 93.91  ? 35   PHE   A HE1  1 
ATOM   510   H  HE2  . PHE   A  1  35  ? 12.648  -0.569  -39.545  1.00 100.47 ? 35   PHE   A HE2  1 
ATOM   511   H  HZ   . PHE   A  1  35  ? 13.601  -1.065  -41.593  1.00 97.14  ? 35   PHE   A HZ   1 
ATOM   512   N  N    . LEU   A  1  36  ? 15.339  -4.531  -34.592  1.00 72.94  ? 36   LEU   A N    1 
ATOM   513   C  CA   . LEU   A  1  36  ? 15.413  -5.490  -33.502  1.00 69.38  ? 36   LEU   A CA   1 
ATOM   514   C  C    . LEU   A  1  36  ? 14.343  -6.554  -33.702  1.00 71.71  ? 36   LEU   A C    1 
ATOM   515   O  O    . LEU   A  1  36  ? 13.193  -6.234  -34.027  1.00 78.58  ? 36   LEU   A O    1 
ATOM   516   C  CB   . LEU   A  1  36  ? 15.226  -4.807  -32.145  1.00 66.55  ? 36   LEU   A CB   1 
ATOM   517   C  CG   . LEU   A  1  36  ? 16.327  -3.870  -31.641  1.00 69.65  ? 36   LEU   A CG   1 
ATOM   518   C  CD1  . LEU   A  1  36  ? 16.480  -2.636  -32.519  1.00 76.45  ? 36   LEU   A CD1  1 
ATOM   519   C  CD2  . LEU   A  1  36  ? 16.035  -3.459  -30.206  1.00 70.17  ? 36   LEU   A CD2  1 
ATOM   520   H  H    . LEU   A  1  36  ? 14.625  -4.051  -34.574  1.00 87.57  ? 36   LEU   A H    1 
ATOM   521   H  HA   . LEU   A  1  36  ? 16.285  -5.916  -33.507  1.00 83.29  ? 36   LEU   A HA   1 
ATOM   522   H  HB2  . LEU   A  1  36  ? 14.414  -4.278  -32.194  1.00 79.90  ? 36   LEU   A HB2  1 
ATOM   523   H  HB3  . LEU   A  1  36  ? 15.129  -5.504  -31.478  1.00 79.90  ? 36   LEU   A HB3  1 
ATOM   524   H  HG   . LEU   A  1  36  ? 17.171  -4.347  -31.676  1.00 83.62  ? 36   LEU   A HG   1 
ATOM   525   H  HD11 . LEU   A  1  36  ? 17.150  -2.053  -32.130  1.00 91.78  ? 36   LEU   A HD11 1 
ATOM   526   H  HD12 . LEU   A  1  36  ? 16.758  -2.912  -33.406  1.00 91.78  ? 36   LEU   A HD12 1 
ATOM   527   H  HD13 . LEU   A  1  36  ? 15.628  -2.175  -32.567  1.00 91.78  ? 36   LEU   A HD13 1 
ATOM   528   H  HD21 . LEU   A  1  36  ? 16.740  -2.869  -29.896  1.00 84.25  ? 36   LEU   A HD21 1 
ATOM   529   H  HD22 . LEU   A  1  36  ? 15.182  -2.999  -30.176  1.00 84.25  ? 36   LEU   A HD22 1 
ATOM   530   H  HD23 . LEU   A  1  36  ? 16.002  -4.254  -29.650  1.00 84.25  ? 36   LEU   A HD23 1 
ATOM   531   N  N    . LEU   A  1  37  ? 14.726  -7.812  -33.522  1.00 64.69  ? 37   LEU   A N    1 
ATOM   532   C  CA   . LEU   A  1  37  ? 13.791  -8.927  -33.519  1.00 62.31  ? 37   LEU   A CA   1 
ATOM   533   C  C    . LEU   A  1  37  ? 13.518  -9.322  -32.075  1.00 57.57  ? 37   LEU   A C    1 
ATOM   534   O  O    . LEU   A  1  37  ? 14.454  -9.472  -31.283  1.00 54.26  ? 37   LEU   A O    1 
ATOM   535   C  CB   . LEU   A  1  37  ? 14.344  -10.119 -34.300  1.00 62.63  ? 37   LEU   A CB   1 
ATOM   536   C  CG   . LEU   A  1  37  ? 14.715  -9.854  -35.760  1.00 64.76  ? 37   LEU   A CG   1 
ATOM   537   C  CD1  . LEU   A  1  37  ? 15.182  -11.133 -36.446  1.00 66.24  ? 37   LEU   A CD1  1 
ATOM   538   C  CD2  . LEU   A  1  37  ? 13.549  -9.236  -36.519  1.00 64.72  ? 37   LEU   A CD2  1 
ATOM   539   H  H    . LEU   A  1  37  ? 15.543  -8.050  -33.397  1.00 77.66  ? 37   LEU   A H    1 
ATOM   540   H  HA   . LEU   A  1  37  ? 12.959  -8.662  -33.941  1.00 74.81  ? 37   LEU   A HA   1 
ATOM   541   H  HB2  . LEU   A  1  37  ? 15.147  -10.427 -33.851  1.00 75.19  ? 37   LEU   A HB2  1 
ATOM   542   H  HB3  . LEU   A  1  37  ? 13.673  -10.820 -34.297  1.00 75.19  ? 37   LEU   A HB3  1 
ATOM   543   H  HG   . LEU   A  1  37  ? 15.449  -9.220  -35.776  1.00 77.74  ? 37   LEU   A HG   1 
ATOM   544   H  HD11 . LEU   A  1  37  ? 15.422  -10.930 -37.363  1.00 79.53  ? 37   LEU   A HD11 1 
ATOM   545   H  HD12 . LEU   A  1  37  ? 15.953  -11.482 -35.972  1.00 79.53  ? 37   LEU   A HD12 1 
ATOM   546   H  HD13 . LEU   A  1  37  ? 14.461  -11.782 -36.429  1.00 79.53  ? 37   LEU   A HD13 1 
ATOM   547   H  HD21 . LEU   A  1  37  ? 13.803  -9.120  -37.448  1.00 77.70  ? 37   LEU   A HD21 1 
ATOM   548   H  HD22 . LEU   A  1  37  ? 12.782  -9.827  -36.457  1.00 77.70  ? 37   LEU   A HD22 1 
ATOM   549   H  HD23 . LEU   A  1  37  ? 13.335  -8.376  -36.125  1.00 77.70  ? 37   LEU   A HD23 1 
ATOM   550   N  N    . VAL   A  1  38  ? 12.242  -9.482  -31.733  1.00 58.45  ? 38   VAL   A N    1 
ATOM   551   C  CA   . VAL   A  1  38  ? 11.842  -9.813  -30.371  1.00 58.65  ? 38   VAL   A CA   1 
ATOM   552   C  C    . VAL   A  1  38  ? 10.795  -10.911 -30.419  1.00 57.47  ? 38   VAL   A C    1 
ATOM   553   O  O    . VAL   A  1  38  ? 9.765   -10.770 -31.088  1.00 59.45  ? 38   VAL   A O    1 
ATOM   554   C  CB   . VAL   A  1  38  ? 11.295  -8.587  -29.615  1.00 63.23  ? 38   VAL   A CB   1 
ATOM   555   C  CG1  . VAL   A  1  38  ? 10.893  -8.979  -28.199  1.00 66.34  ? 38   VAL   A CG1  1 
ATOM   556   C  CG2  . VAL   A  1  38  ? 12.331  -7.477  -29.591  1.00 64.15  ? 38   VAL   A CG2  1 
ATOM   557   H  H    . VAL   A  1  38  ? 11.583  -9.403  -32.280  1.00 70.18  ? 38   VAL   A H    1 
ATOM   558   H  HA   . VAL   A  1  38  ? 12.615  -10.150 -29.892  1.00 70.42  ? 38   VAL   A HA   1 
ATOM   559   H  HB   . VAL   A  1  38  ? 10.508  -8.254  -30.073  1.00 75.91  ? 38   VAL   A HB   1 
ATOM   560   H  HG11 . VAL   A  1  38  ? 10.649  -8.179  -27.707  1.00 79.65  ? 38   VAL   A HG11 1 
ATOM   561   H  HG12 . VAL   A  1  38  ? 10.135  -9.583  -28.243  1.00 79.65  ? 38   VAL   A HG12 1 
ATOM   562   H  HG13 . VAL   A  1  38  ? 11.642  -9.417  -27.768  1.00 79.65  ? 38   VAL   A HG13 1 
ATOM   563   H  HG21 . VAL   A  1  38  ? 11.990  -6.737  -29.064  1.00 77.02  ? 38   VAL   A HG21 1 
ATOM   564   H  HG22 . VAL   A  1  38  ? 13.149  -7.816  -29.194  1.00 77.02  ? 38   VAL   A HG22 1 
ATOM   565   H  HG23 . VAL   A  1  38  ? 12.502  -7.185  -30.500  1.00 77.02  ? 38   VAL   A HG23 1 
ATOM   566   N  N    . GLY   A  1  39  ? 11.047  -12.001 -29.703  1.00 58.23  ? 39   GLY   A N    1 
ATOM   567   C  CA   . GLY   A  1  39  ? 10.078  -13.069 -29.591  1.00 57.14  ? 39   GLY   A CA   1 
ATOM   568   C  C    . GLY   A  1  39  ? 9.068   -12.795 -28.486  1.00 53.72  ? 39   GLY   A C    1 
ATOM   569   O  O    . GLY   A  1  39  ? 9.423   -12.352 -27.394  1.00 53.79  ? 39   GLY   A O    1 
ATOM   570   H  H    . GLY   A  1  39  ? 11.777  -12.142 -29.272  1.00 69.91  ? 39   GLY   A H    1 
ATOM   571   H  HA2  . GLY   A  1  39  ? 9.600   -13.163 -30.430  1.00 68.60  ? 39   GLY   A HA2  1 
ATOM   572   H  HA3  . GLY   A  1  39  ? 10.534  -13.902 -29.393  1.00 68.60  ? 39   GLY   A HA3  1 
ATOM   573   N  N    . ALA   A  1  40  ? 7.803   -13.058 -28.793  1.00 50.63  ? 40   ALA   A N    1 
ATOM   574   C  CA   . ALA   A  1  40  ? 6.705   -12.975 -27.831  1.00 50.13  ? 40   ALA   A CA   1 
ATOM   575   C  C    . ALA   A  1  40  ? 5.939   -14.290 -27.901  1.00 49.75  ? 40   ALA   A C    1 
ATOM   576   O  O    . ALA   A  1  40  ? 4.828   -14.353 -28.441  1.00 50.73  ? 40   ALA   A O    1 
ATOM   577   C  CB   . ALA   A  1  40  ? 5.801   -11.778 -28.124  1.00 52.40  ? 40   ALA   A CB   1 
ATOM   578   H  H    . ALA   A  1  40  ? 7.546   -13.294 -29.579  1.00 60.80  ? 40   ALA   A H    1 
ATOM   579   H  HA   . ALA   A  1  40  ? 7.053   -12.858 -26.933  1.00 60.19  ? 40   ALA   A HA   1 
ATOM   580   H  HB1  . ALA   A  1  40  ? 5.086   -11.754 -27.468  1.00 62.92  ? 40   ALA   A HB1  1 
ATOM   581   H  HB2  . ALA   A  1  40  ? 6.326   -10.965 -28.071  1.00 62.92  ? 40   ALA   A HB2  1 
ATOM   582   H  HB3  . ALA   A  1  40  ? 5.429   -11.875 -29.015  1.00 62.92  ? 40   ALA   A HB3  1 
ATOM   583   N  N    . PRO   A  1  41  ? 6.515   -15.369 -27.363  1.00 47.60  ? 41   PRO   A N    1 
ATOM   584   C  CA   . PRO   A  1  41  ? 5.980   -16.712 -27.647  1.00 48.31  ? 41   PRO   A CA   1 
ATOM   585   C  C    . PRO   A  1  41  ? 4.575   -16.969 -27.122  1.00 48.51  ? 41   PRO   A C    1 
ATOM   586   O  O    . PRO   A  1  41  ? 3.966   -17.964 -27.536  1.00 49.27  ? 41   PRO   A O    1 
ATOM   587   C  CB   . PRO   A  1  41  ? 7.001   -17.646 -26.979  1.00 46.27  ? 41   PRO   A CB   1 
ATOM   588   C  CG   . PRO   A  1  41  ? 7.714   -16.797 -25.978  1.00 46.02  ? 41   PRO   A CG   1 
ATOM   589   C  CD   . PRO   A  1  41  ? 7.755   -15.425 -26.570  1.00 47.82  ? 41   PRO   A CD   1 
ATOM   590   H  HA   . PRO   A  1  41  ? 5.980   -16.858 -28.606  1.00 58.01  ? 41   PRO   A HA   1 
ATOM   591   H  HB2  . PRO   A  1  41  ? 6.539   -18.380 -26.544  1.00 55.56  ? 41   PRO   A HB2  1 
ATOM   592   H  HB3  . PRO   A  1  41  ? 7.617   -17.990 -27.644  1.00 55.56  ? 41   PRO   A HB3  1 
ATOM   593   H  HG2  . PRO   A  1  41  ? 7.226   -16.797 -25.140  1.00 55.26  ? 41   PRO   A HG2  1 
ATOM   594   H  HG3  . PRO   A  1  41  ? 8.612   -17.139 -25.839  1.00 55.26  ? 41   PRO   A HG3  1 
ATOM   595   H  HD2  . PRO   A  1  41  ? 7.752   -14.747 -25.876  1.00 57.42  ? 41   PRO   A HD2  1 
ATOM   596   H  HD3  . PRO   A  1  41  ? 8.534   -15.315 -27.138  1.00 57.42  ? 41   PRO   A HD3  1 
ATOM   597   N  N    . LYS   A  1  42  ? 4.037   -16.128 -26.240  1.00 48.84  ? 42   LYS   A N    1 
ATOM   598   C  CA   . LYS   A  1  42  ? 2.675   -16.301 -25.749  1.00 55.19  ? 42   LYS   A CA   1 
ATOM   599   C  C    . LYS   A  1  42  ? 1.713   -15.268 -26.321  1.00 59.89  ? 42   LYS   A C    1 
ATOM   600   O  O    . LYS   A  1  42  ? 0.566   -15.185 -25.868  1.00 61.73  ? 42   LYS   A O    1 
ATOM   601   C  CB   . LYS   A  1  42  ? 2.648   -16.253 -24.220  1.00 59.20  ? 42   LYS   A CB   1 
ATOM   602   C  CG   . LYS   A  1  42  ? 3.043   -17.568 -23.570  1.00 59.28  ? 42   LYS   A CG   1 
ATOM   603   C  CD   . LYS   A  1  42  ? 2.797   -17.564 -22.071  1.00 62.28  ? 42   LYS   A CD   1 
ATOM   604   C  CE   . LYS   A  1  42  ? 2.923   -18.970 -21.506  1.00 66.84  ? 42   LYS   A CE   1 
ATOM   605   N  NZ   . LYS   A  1  42  ? 2.960   -18.997 -20.019  1.00 69.32  ? 42   LYS   A NZ   1 
ATOM   606   H  H    . LYS   A  1  42  ? 4.445   -15.446 -25.911  1.00 58.64  ? 42   LYS   A H    1 
ATOM   607   H  HA   . LYS   A  1  42  ? 2.363   -17.178 -26.023  1.00 66.27  ? 42   LYS   A HA   1 
ATOM   608   H  HB2  . LYS   A  1  42  ? 3.269   -15.572 -23.917  1.00 71.07  ? 42   LYS   A HB2  1 
ATOM   609   H  HB3  . LYS   A  1  42  ? 1.749   -16.035 -23.929  1.00 71.07  ? 42   LYS   A HB3  1 
ATOM   610   H  HG2  . LYS   A  1  42  ? 2.520   -18.286 -23.960  1.00 71.17  ? 42   LYS   A HG2  1 
ATOM   611   H  HG3  . LYS   A  1  42  ? 3.988   -17.726 -23.720  1.00 71.17  ? 42   LYS   A HG3  1 
ATOM   612   H  HD2  . LYS   A  1  42  ? 3.453   -16.997 -21.635  1.00 74.77  ? 42   LYS   A HD2  1 
ATOM   613   H  HD3  . LYS   A  1  42  ? 1.902   -17.237 -21.889  1.00 74.77  ? 42   LYS   A HD3  1 
ATOM   614   H  HE2  . LYS   A  1  42  ? 2.161   -19.495 -21.795  1.00 80.24  ? 42   LYS   A HE2  1 
ATOM   615   H  HE3  . LYS   A  1  42  ? 3.744   -19.369 -21.833  1.00 80.24  ? 42   LYS   A HE3  1 
ATOM   616   H  HZ1  . LYS   A  1  42  ? 3.056   -19.834 -19.732  1.00 83.22  ? 42   LYS   A HZ1  1 
ATOM   617   H  HZ2  . LYS   A  1  42  ? 3.644   -18.510 -19.723  1.00 83.22  ? 42   LYS   A HZ2  1 
ATOM   618   H  HZ3  . LYS   A  1  42  ? 2.204   -18.663 -19.690  1.00 83.22  ? 42   LYS   A HZ3  1 
ATOM   619   N  N    . ALA   A  1  43  ? 2.143   -14.491 -27.310  1.00 62.12  ? 43   ALA   A N    1 
ATOM   620   C  CA   . ALA   A  1  43  ? 1.284   -13.466 -27.881  1.00 61.18  ? 43   ALA   A CA   1 
ATOM   621   C  C    . ALA   A  1  43  ? 0.142   -14.090 -28.669  1.00 64.11  ? 43   ALA   A C    1 
ATOM   622   O  O    . ALA   A  1  43  ? 0.325   -15.073 -29.393  1.00 62.50  ? 43   ALA   A O    1 
ATOM   623   C  CB   . ALA   A  1  43  ? 2.092   -12.543 -28.790  1.00 56.39  ? 43   ALA   A CB   1 
ATOM   624   H  H    . ALA   A  1  43  ? 2.924   -14.540 -27.666  1.00 74.58  ? 43   ALA   A H    1 
ATOM   625   H  HA   . ALA   A  1  43  ? 0.904   -12.937 -27.161  1.00 73.45  ? 43   ALA   A HA   1 
ATOM   626   H  HB1  . ALA   A  1  43  ? 1.490   -11.910 -29.212  1.00 67.71  ? 43   ALA   A HB1  1 
ATOM   627   H  HB2  . ALA   A  1  43  ? 2.748   -12.069 -28.255  1.00 67.71  ? 43   ALA   A HB2  1 
ATOM   628   H  HB3  . ALA   A  1  43  ? 2.538   -13.077 -29.465  1.00 67.71  ? 43   ALA   A HB3  1 
ATOM   629   N  N    . ASN   A  1  44  ? -1.045  -13.510 -28.523  1.00 66.48  ? 44   ASN   A N    1 
ATOM   630   C  CA   . ASN   A  1  44  ? -2.177  -13.896 -29.350  1.00 70.65  ? 44   ASN   A CA   1 
ATOM   631   C  C    . ASN   A  1  44  ? -1.986  -13.378 -30.771  1.00 68.94  ? 44   ASN   A C    1 
ATOM   632   O  O    . ASN   A  1  44  ? -1.335  -12.355 -31.002  1.00 72.69  ? 44   ASN   A O    1 
ATOM   633   C  CB   . ASN   A  1  44  ? -3.474  -13.358 -28.750  1.00 78.12  ? 44   ASN   A CB   1 
ATOM   634   C  CG   . ASN   A  1  44  ? -4.034  -14.270 -27.677  1.00 83.25  ? 44   ASN   A CG   1 
ATOM   635   O  OD1  . ASN   A  1  44  ? -4.118  -15.481 -27.871  1.00 79.48  ? 44   ASN   A OD1  1 
ATOM   636   N  ND2  . ASN   A  1  44  ? -4.414  -13.701 -26.539  1.00 97.64  ? 44   ASN   A ND2  1 
ATOM   637   H  H    . ASN   A  1  44  ? -1.219  -12.892 -27.951  1.00 79.81  ? 44   ASN   A H    1 
ATOM   638   H  HA   . ASN   A  1  44  ? -2.249  -14.862 -29.389  1.00 84.82  ? 44   ASN   A HA   1 
ATOM   639   H  HB2  . ASN   A  1  44  ? -3.304  -12.491 -28.350  1.00 93.78  ? 44   ASN   A HB2  1 
ATOM   640   H  HB3  . ASN   A  1  44  ? -4.139  -13.275 -29.452  1.00 93.78  ? 44   ASN   A HB3  1 
ATOM   641   H  HD21 . ASN   A  1  44  ? -4.344  -12.853 -26.416  1.00 117.21 ? 44   ASN   A HD21 1 
ATOM   642   N  N    . THR   A  1  45  ? -2.553  -14.103 -31.732  1.00 64.52  ? 45   THR   A N    1 
ATOM   643   C  CA   . THR   A  1  45  ? -2.388  -13.789 -33.143  1.00 61.89  ? 45   THR   A CA   1 
ATOM   644   C  C    . THR   A  1  45  ? -3.744  -13.800 -33.832  1.00 60.87  ? 45   THR   A C    1 
ATOM   645   O  O    . THR   A  1  45  ? -4.759  -14.208 -33.260  1.00 60.78  ? 45   THR   A O    1 
ATOM   646   C  CB   . THR   A  1  45  ? -1.442  -14.783 -33.835  1.00 59.79  ? 45   THR   A CB   1 
ATOM   647   O  OG1  . THR   A  1  45  ? -2.068  -16.070 -33.916  1.00 57.73  ? 45   THR   A OG1  1 
ATOM   648   C  CG2  . THR   A  1  45  ? -0.133  -14.907 -33.067  1.00 54.08  ? 45   THR   A CG2  1 
ATOM   649   H  H    . THR   A  1  45  ? -3.046  -14.793 -31.586  1.00 77.46  ? 45   THR   A H    1 
ATOM   650   H  HA   . THR   A  1  45  ? -2.012  -12.899 -33.222  1.00 74.31  ? 45   THR   A HA   1 
ATOM   651   H  HB   . THR   A  1  45  ? -1.241  -14.463 -34.729  1.00 71.79  ? 45   THR   A HB   1 
ATOM   652   H  HG1  . THR   A  1  45  ? -1.571  -16.605 -34.331  1.00 69.32  ? 45   THR   A HG1  1 
ATOM   653   H  HG21 . THR   A  1  45  ? 0.464   -15.520 -33.524  1.00 64.94  ? 45   THR   A HG21 1 
ATOM   654   H  HG22 . THR   A  1  45  ? 0.297   -14.040 -33.001  1.00 64.94  ? 45   THR   A HG22 1 
ATOM   655   H  HG23 . THR   A  1  45  ? -0.304  -15.243 -32.173  1.00 64.94  ? 45   THR   A HG23 1 
ATOM   656   N  N    . THR   A  1  46  ? -3.749  -13.338 -35.081  1.00 64.10  ? 46   THR   A N    1 
ATOM   657   C  CA   . THR   A  1  46  ? -4.950  -13.347 -35.905  1.00 74.96  ? 46   THR   A CA   1 
ATOM   658   C  C    . THR   A  1  46  ? -5.202  -14.697 -36.560  1.00 78.86  ? 46   THR   A C    1 
ATOM   659   O  O    . THR   A  1  46  ? -6.218  -14.855 -37.244  1.00 85.19  ? 46   THR   A O    1 
ATOM   660   C  CB   . THR   A  1  46  ? -4.853  -12.271 -36.990  1.00 79.64  ? 46   THR   A CB   1 
ATOM   661   O  OG1  . THR   A  1  46  ? -3.700  -12.513 -37.806  1.00 77.16  ? 46   THR   A OG1  1 
ATOM   662   C  CG2  . THR   A  1  46  ? -4.749  -10.890 -36.365  1.00 83.41  ? 46   THR   A CG2  1 
ATOM   663   H  H    . THR   A  1  46  ? -3.059  -13.012 -35.477  1.00 76.96  ? 46   THR   A H    1 
ATOM   664   H  HA   . THR   A  1  46  ? -5.711  -13.136 -35.342  1.00 89.99  ? 46   THR   A HA   1 
ATOM   665   H  HB   . THR   A  1  46  ? -5.650  -12.296 -37.543  1.00 95.61  ? 46   THR   A HB   1 
ATOM   666   H  HG1  . THR   A  1  46  ? -3.637  -11.920 -38.398  1.00 92.63  ? 46   THR   A HG1  1 
ATOM   667   H  HG21 . THR   A  1  46  ? -4.700  -10.214 -37.059  1.00 100.13 ? 46   THR   A HG21 1 
ATOM   668   H  HG22 . THR   A  1  46  ? -5.526  -10.717 -35.811  1.00 100.13 ? 46   THR   A HG22 1 
ATOM   669   H  HG23 . THR   A  1  46  ? -3.952  -10.835 -35.814  1.00 100.13 ? 46   THR   A HG23 1 
ATOM   670   N  N    . GLN   A  1  47  ? -4.306  -15.657 -36.376  1.00 77.32  ? 47   GLN   A N    1 
ATOM   671   C  CA   . GLN   A  1  47  ? -4.485  -16.972 -36.973  1.00 72.86  ? 47   GLN   A CA   1 
ATOM   672   C  C    . GLN   A  1  47  ? -5.831  -17.552 -36.547  1.00 70.46  ? 47   GLN   A C    1 
ATOM   673   O  O    . GLN   A  1  47  ? -6.124  -17.605 -35.345  1.00 68.74  ? 47   GLN   A O    1 
ATOM   674   C  CB   . GLN   A  1  47  ? -3.344  -17.895 -36.551  1.00 65.56  ? 47   GLN   A CB   1 
ATOM   675   C  CG   . GLN   A  1  47  ? -1.993  -17.460 -37.088  1.00 57.10  ? 47   GLN   A CG   1 
ATOM   676   C  CD   . GLN   A  1  47  ? -0.844  -18.226 -36.469  1.00 54.18  ? 47   GLN   A CD   1 
ATOM   677   O  OE1  . GLN   A  1  47  ? -0.374  -17.892 -35.381  1.00 52.41  ? 47   GLN   A OE1  1 
ATOM   678   N  NE2  . GLN   A  1  47  ? -0.385  -19.261 -37.159  1.00 55.12  ? 47   GLN   A NE2  1 
ATOM   679   H  H    . GLN   A  1  47  ? -3.588  -15.574 -35.910  1.00 92.82  ? 47   GLN   A H    1 
ATOM   680   H  HA   . GLN   A  1  47  ? -4.478  -16.901 -37.940  1.00 87.47  ? 47   GLN   A HA   1 
ATOM   681   H  HB2  . GLN   A  1  47  ? -3.291  -17.906 -35.582  1.00 78.71  ? 47   GLN   A HB2  1 
ATOM   682   H  HB3  . GLN   A  1  47  ? -3.524  -18.788 -36.884  1.00 78.71  ? 47   GLN   A HB3  1 
ATOM   683   H  HG2  . GLN   A  1  47  ? -1.971  -17.608 -38.046  1.00 68.56  ? 47   GLN   A HG2  1 
ATOM   684   H  HG3  . GLN   A  1  47  ? -1.865  -16.518 -36.894  1.00 68.56  ? 47   GLN   A HG3  1 
ATOM   685   H  HE21 . GLN   A  1  47  ? -0.739  -19.465 -37.916  1.00 66.18  ? 47   GLN   A HE21 1 
ATOM   686   H  HE22 . GLN   A  1  47  ? 0.268   -19.729 -36.850  1.00 66.18  ? 47   GLN   A HE22 1 
ATOM   687   N  N    . PRO   A  1  48  ? -6.673  -17.987 -37.485  1.00 72.25  ? 48   PRO   A N    1 
ATOM   688   C  CA   . PRO   A  1  48  ? -8.010  -18.473 -37.106  1.00 75.00  ? 48   PRO   A CA   1 
ATOM   689   C  C    . PRO   A  1  48  ? -7.936  -19.645 -36.138  1.00 74.18  ? 48   PRO   A C    1 
ATOM   690   O  O    . PRO   A  1  48  ? -7.314  -20.672 -36.421  1.00 74.96  ? 48   PRO   A O    1 
ATOM   691   C  CB   . PRO   A  1  48  ? -8.629  -18.885 -38.449  1.00 65.11  ? 48   PRO   A CB   1 
ATOM   692   C  CG   . PRO   A  1  48  ? -7.873  -18.120 -39.476  1.00 67.60  ? 48   PRO   A CG   1 
ATOM   693   C  CD   . PRO   A  1  48  ? -6.482  -17.990 -38.948  1.00 71.11  ? 48   PRO   A CD   1 
ATOM   694   H  HA   . PRO   A  1  48  ? -8.526  -17.757 -36.705  1.00 90.04  ? 48   PRO   A HA   1 
ATOM   695   H  HB2  . PRO   A  1  48  ? -8.525  -19.840 -38.581  1.00 77.94  ? 48   PRO   A HB2  1 
ATOM   696   H  HB3  . PRO   A  1  48  ? -9.570  -18.648 -38.463  1.00 77.94  ? 48   PRO   A HB3  1 
ATOM   697   H  HG2  . PRO   A  1  48  ? -7.878  -18.607 -40.315  1.00 81.15  ? 48   PRO   A HG2  1 
ATOM   698   H  HG3  . PRO   A  1  48  ? -8.278  -17.247 -39.597  1.00 81.15  ? 48   PRO   A HG3  1 
ATOM   699   H  HD2  . PRO   A  1  48  ? -5.937  -18.743 -39.223  1.00 85.36  ? 48   PRO   A HD2  1 
ATOM   700   H  HD3  . PRO   A  1  48  ? -6.076  -17.161 -39.245  1.00 85.36  ? 48   PRO   A HD3  1 
ATOM   701   N  N    . GLY   A  1  49  ? -8.577  -19.479 -34.983  1.00 59.08  ? 49   GLY   A N    1 
ATOM   702   C  CA   . GLY   A  1  49  ? -8.727  -20.547 -34.019  1.00 57.35  ? 49   GLY   A CA   1 
ATOM   703   C  C    . GLY   A  1  49  ? -7.510  -20.846 -33.173  1.00 62.56  ? 49   GLY   A C    1 
ATOM   704   O  O    . GLY   A  1  49  ? -7.550  -21.798 -32.382  1.00 62.73  ? 49   GLY   A O    1 
ATOM   705   H  H    . GLY   A  1  49  ? -8.939  -18.739 -34.736  1.00 70.71  ? 49   GLY   A H    1 
ATOM   706   H  HA2  . GLY   A  1  49  ? -9.452  -20.317 -33.417  1.00 68.64  ? 49   GLY   A HA2  1 
ATOM   707   H  HA3  . GLY   A  1  49  ? -8.958  -21.360 -34.495  1.00 68.64  ? 49   GLY   A HA3  1 
ATOM   708   N  N    . ILE   A  1  50  ? -6.436  -20.073 -33.300  1.00 61.86  ? 50   ILE   A N    1 
ATOM   709   C  CA   . ILE   A  1  50  ? -5.197  -20.326 -32.575  1.00 55.38  ? 50   ILE   A CA   1 
ATOM   710   C  C    . ILE   A  1  50  ? -5.130  -19.383 -31.383  1.00 54.56  ? 50   ILE   A C    1 
ATOM   711   O  O    . ILE   A  1  50  ? -5.219  -18.159 -31.540  1.00 54.73  ? 50   ILE   A O    1 
ATOM   712   C  CB   . ILE   A  1  50  ? -3.970  -20.153 -33.485  1.00 57.87  ? 50   ILE   A CB   1 
ATOM   713   C  CG1  . ILE   A  1  50  ? -4.075  -21.076 -34.703  1.00 61.84  ? 50   ILE   A CG1  1 
ATOM   714   C  CG2  . ILE   A  1  50  ? -2.685  -20.423 -32.710  1.00 59.07  ? 50   ILE   A CG2  1 
ATOM   715   C  CD1  . ILE   A  1  50  ? -4.485  -22.504 -34.374  1.00 63.06  ? 50   ILE   A CD1  1 
ATOM   716   H  H    . ILE   A  1  50  ? -6.401  -19.382 -33.810  1.00 74.26  ? 50   ILE   A H    1 
ATOM   717   H  HA   . ILE   A  1  50  ? -5.207  -21.236 -32.240  1.00 66.49  ? 50   ILE   A HA   1 
ATOM   718   H  HB   . ILE   A  1  50  ? -3.947  -19.235 -33.798  1.00 69.48  ? 50   ILE   A HB   1 
ATOM   719   H  HG12 . ILE   A  1  50  ? -4.739  -20.713 -35.310  1.00 74.24  ? 50   ILE   A HG12 1 
ATOM   720   H  HG13 . ILE   A  1  50  ? -3.210  -21.113 -35.140  1.00 74.24  ? 50   ILE   A HG13 1 
ATOM   721   H  HG21 . ILE   A  1  50  ? -1.929  -20.335 -33.311  1.00 70.92  ? 50   ILE   A HG21 1 
ATOM   722   H  HG22 . ILE   A  1  50  ? -2.611  -19.779 -31.988  1.00 70.92  ? 50   ILE   A HG22 1 
ATOM   723   H  HG23 . ILE   A  1  50  ? -2.718  -21.322 -32.348  1.00 70.92  ? 50   ILE   A HG23 1 
ATOM   724   H  HD11 . ILE   A  1  50  ? -4.441  -23.039 -35.182  1.00 75.71  ? 50   ILE   A HD11 1 
ATOM   725   H  HD12 . ILE   A  1  50  ? -3.878  -22.861 -33.707  1.00 75.71  ? 50   ILE   A HD12 1 
ATOM   726   H  HD13 . ILE   A  1  50  ? -5.391  -22.501 -34.029  1.00 75.71  ? 50   ILE   A HD13 1 
ATOM   727   N  N    . VAL   A  1  51  ? -4.970  -19.954 -30.192  1.00 55.95  ? 51   VAL   A N    1 
ATOM   728   C  CA   . VAL   A  1  51  ? -4.782  -19.191 -28.966  1.00 58.48  ? 51   VAL   A CA   1 
ATOM   729   C  C    . VAL   A  1  51  ? -3.301  -19.195 -28.621  1.00 57.08  ? 51   VAL   A C    1 
ATOM   730   O  O    . VAL   A  1  51  ? -2.662  -20.255 -28.596  1.00 55.00  ? 51   VAL   A O    1 
ATOM   731   C  CB   . VAL   A  1  51  ? -5.614  -19.773 -27.810  1.00 60.76  ? 51   VAL   A CB   1 
ATOM   732   C  CG1  . VAL   A  1  51  ? -5.416  -18.946 -26.546  1.00 62.12  ? 51   VAL   A CG1  1 
ATOM   733   C  CG2  . VAL   A  1  51  ? -7.082  -19.830 -28.192  1.00 51.40  ? 51   VAL   A CG2  1 
ATOM   734   H  H    . VAL   A  1  51  ? -4.966  -20.805 -30.068  1.00 67.18  ? 51   VAL   A H    1 
ATOM   735   H  HA   . VAL   A  1  51  ? -5.065  -18.275 -29.113  1.00 70.21  ? 51   VAL   A HA   1 
ATOM   736   H  HB   . VAL   A  1  51  ? -5.315  -20.678 -27.629  1.00 72.95  ? 51   VAL   A HB   1 
ATOM   737   H  HG11 . VAL   A  1  51  ? -5.959  -19.320 -25.835  1.00 74.58  ? 51   VAL   A HG11 1 
ATOM   738   H  HG12 . VAL   A  1  51  ? -4.479  -18.973 -26.295  1.00 74.58  ? 51   VAL   A HG12 1 
ATOM   739   H  HG13 . VAL   A  1  51  ? -5.685  -18.031 -26.722  1.00 74.58  ? 51   VAL   A HG13 1 
ATOM   740   H  HG21 . VAL   A  1  51  ? -7.589  -20.184 -27.444  1.00 61.50  ? 51   VAL   A HG21 1 
ATOM   741   H  HG22 . VAL   A  1  51  ? -7.388  -18.935 -28.405  1.00 61.50  ? 51   VAL   A HG22 1 
ATOM   742   H  HG23 . VAL   A  1  51  ? -7.186  -20.407 -28.964  1.00 61.50  ? 51   VAL   A HG23 1 
ATOM   743   N  N    . GLU   A  1  52  ? -2.757  -18.009 -28.354  1.00 55.65  ? 52   GLU   A N    1 
ATOM   744   C  CA   . GLU   A  1  52  ? -1.367  -17.849 -27.937  1.00 56.80  ? 52   GLU   A CA   1 
ATOM   745   C  C    . GLU   A  1  52  ? -0.424  -18.651 -28.829  1.00 59.22  ? 52   GLU   A C    1 
ATOM   746   O  O    . GLU   A  1  52  ? 0.426   -19.412 -28.360  1.00 60.69  ? 52   GLU   A O    1 
ATOM   747   C  CB   . GLU   A  1  52  ? -1.194  -18.236 -26.468  1.00 57.40  ? 52   GLU   A CB   1 
ATOM   748   C  CG   . GLU   A  1  52  ? -1.925  -17.311 -25.511  1.00 63.33  ? 52   GLU   A CG   1 
ATOM   749   C  CD   . GLU   A  1  52  ? -1.461  -17.461 -24.076  1.00 65.77  ? 52   GLU   A CD   1 
ATOM   750   O  OE1  . GLU   A  1  52  ? -0.663  -18.381 -23.798  1.00 67.78  ? 52   GLU   A OE1  1 
ATOM   751   O  OE2  . GLU   A  1  52  ? -1.894  -16.654 -23.227  1.00 66.17  ? 52   GLU   A OE2  1 
ATOM   752   H  H    . GLU   A  1  52  ? -3.184  -17.265 -28.409  1.00 66.82  ? 52   GLU   A H    1 
ATOM   753   H  HA   . GLU   A  1  52  ? -1.129  -16.914 -28.033  1.00 68.20  ? 52   GLU   A HA   1 
ATOM   754   H  HB2  . GLU   A  1  52  ? -1.539  -19.133 -26.337  1.00 68.91  ? 52   GLU   A HB2  1 
ATOM   755   H  HB3  . GLU   A  1  52  ? -0.250  -18.208 -26.246  1.00 68.91  ? 52   GLU   A HB3  1 
ATOM   756   H  HG2  . GLU   A  1  52  ? -1.771  -16.392 -25.781  1.00 76.03  ? 52   GLU   A HG2  1 
ATOM   757   H  HG3  . GLU   A  1  52  ? -2.874  -17.512 -25.542  1.00 76.03  ? 52   GLU   A HG3  1 
ATOM   758   N  N    . GLY   A  1  53  ? -0.586  -18.478 -30.141  1.00 55.62  ? 53   GLY   A N    1 
ATOM   759   C  CA   . GLY   A  1  53  ? 0.379   -19.026 -31.073  1.00 55.51  ? 53   GLY   A CA   1 
ATOM   760   C  C    . GLY   A  1  53  ? 1.737   -18.364 -30.991  1.00 54.83  ? 53   GLY   A C    1 
ATOM   761   O  O    . GLY   A  1  53  ? 2.724   -18.936 -31.463  1.00 45.92  ? 53   GLY   A O    1 
ATOM   762   H  H    . GLY   A  1  53  ? -1.239  -18.053 -30.505  1.00 66.78  ? 53   GLY   A H    1 
ATOM   763   H  HA2  . GLY   A  1  53  ? 0.493   -19.972 -30.891  1.00 66.65  ? 53   GLY   A HA2  1 
ATOM   764   H  HA3  . GLY   A  1  53  ? 0.044   -18.916 -31.977  1.00 66.65  ? 53   GLY   A HA3  1 
ATOM   765   N  N    . GLY   A  1  54  ? 1.809   -17.178 -30.391  1.00 54.58  ? 54   GLY   A N    1 
ATOM   766   C  CA   . GLY   A  1  54  ? 3.048   -16.439 -30.316  1.00 54.19  ? 54   GLY   A CA   1 
ATOM   767   C  C    . GLY   A  1  54  ? 3.414   -15.798 -31.637  1.00 55.38  ? 54   GLY   A C    1 
ATOM   768   O  O    . GLY   A  1  54  ? 2.833   -16.097 -32.690  1.00 52.90  ? 54   GLY   A O    1 
ATOM   769   H  H    . GLY   A  1  54  ? 1.142   -16.783 -30.018  1.00 65.54  ? 54   GLY   A H    1 
ATOM   770   H  HA2  . GLY   A  1  54  ? 2.965   -15.740 -29.649  1.00 65.07  ? 54   GLY   A HA2  1 
ATOM   771   H  HA3  . GLY   A  1  54  ? 3.764   -17.039 -30.057  1.00 65.07  ? 54   GLY   A HA3  1 
ATOM   772   N  N    . GLN   A  1  55  ? 4.390   -14.902 -31.592  1.00 58.90  ? 55   GLN   A N    1 
ATOM   773   C  CA   . GLN   A  1  55  ? 4.820   -14.211 -32.796  1.00 61.16  ? 55   GLN   A CA   1 
ATOM   774   C  C    . GLN   A  1  55  ? 6.190   -13.595 -32.568  1.00 58.07  ? 55   GLN   A C    1 
ATOM   775   O  O    . GLN   A  1  55  ? 6.654   -13.456 -31.434  1.00 57.14  ? 55   GLN   A O    1 
ATOM   776   C  CB   . GLN   A  1  55  ? 3.810   -13.134 -33.213  1.00 63.18  ? 55   GLN   A CB   1 
ATOM   777   C  CG   . GLN   A  1  55  ? 3.484   -12.137 -32.116  1.00 64.48  ? 55   GLN   A CG   1 
ATOM   778   C  CD   . GLN   A  1  55  ? 2.289   -11.263 -32.447  1.00 68.54  ? 55   GLN   A CD   1 
ATOM   779   O  OE1  . GLN   A  1  55  ? 1.568   -11.512 -33.414  1.00 70.21  ? 55   GLN   A OE1  1 
ATOM   780   N  NE2  . GLN   A  1  55  ? 2.070   -10.232 -31.638  1.00 67.43  ? 55   GLN   A NE2  1 
ATOM   781   H  H    . GLN   A  1  55  ? 4.816   -14.678 -30.880  1.00 70.72  ? 55   GLN   A H    1 
ATOM   782   H  HA   . GLN   A  1  55  ? 4.902   -14.858 -33.515  1.00 73.43  ? 55   GLN   A HA   1 
ATOM   783   H  HB2  . GLN   A  1  55  ? 4.175   -12.639 -33.963  1.00 75.85  ? 55   GLN   A HB2  1 
ATOM   784   H  HB3  . GLN   A  1  55  ? 2.982   -13.568 -33.474  1.00 75.85  ? 55   GLN   A HB3  1 
ATOM   785   H  HG2  . GLN   A  1  55  ? 3.283   -12.621 -31.299  1.00 77.41  ? 55   GLN   A HG2  1 
ATOM   786   H  HG3  . GLN   A  1  55  ? 4.249   -11.557 -31.979  1.00 77.41  ? 55   GLN   A HG3  1 
ATOM   787   H  HE21 . GLN   A  1  55  ? 2.593   -10.091 -30.970  1.00 80.95  ? 55   GLN   A HE21 1 
ATOM   788   H  HE22 . GLN   A  1  55  ? 1.405   -9.705  -31.782  1.00 80.95  ? 55   GLN   A HE22 1 
ATOM   789   N  N    . VAL   A  1  56  ? 6.834   -13.240 -33.677  1.00 60.44  ? 56   VAL   A N    1 
ATOM   790   C  CA   . VAL   A  1  56  ? 8.099   -12.516 -33.683  1.00 56.85  ? 56   VAL   A CA   1 
ATOM   791   C  C    . VAL   A  1  56  ? 7.829   -11.115 -34.214  1.00 58.32  ? 56   VAL   A C    1 
ATOM   792   O  O    . VAL   A  1  56  ? 7.094   -10.947 -35.194  1.00 60.34  ? 56   VAL   A O    1 
ATOM   793   C  CB   . VAL   A  1  56  ? 9.157   -13.237 -34.540  1.00 54.32  ? 56   VAL   A CB   1 
ATOM   794   C  CG1  . VAL   A  1  56  ? 10.440  -12.418 -34.623  1.00 54.55  ? 56   VAL   A CG1  1 
ATOM   795   C  CG2  . VAL   A  1  56  ? 9.441   -14.624 -33.980  1.00 51.26  ? 56   VAL   A CG2  1 
ATOM   796   H  H    . VAL   A  1  56  ? 6.546   -13.415 -34.468  1.00 72.56  ? 56   VAL   A H    1 
ATOM   797   H  HA   . VAL   A  1  56  ? 8.444   -12.448 -32.779  1.00 68.26  ? 56   VAL   A HA   1 
ATOM   798   H  HB   . VAL   A  1  56  ? 8.811   -13.338 -35.441  1.00 65.23  ? 56   VAL   A HB   1 
ATOM   799   H  HG11 . VAL   A  1  56  ? 11.096  -12.910 -35.140  1.00 65.50  ? 56   VAL   A HG11 1 
ATOM   800   H  HG12 . VAL   A  1  56  ? 10.246  -11.571 -35.054  1.00 65.50  ? 56   VAL   A HG12 1 
ATOM   801   H  HG13 . VAL   A  1  56  ? 10.774  -12.263 -33.725  1.00 65.50  ? 56   VAL   A HG13 1 
ATOM   802   H  HG21 . VAL   A  1  56  ? 10.118  -15.052 -34.527  1.00 61.54  ? 56   VAL   A HG21 1 
ATOM   803   H  HG22 . VAL   A  1  56  ? 9.758   -14.537 -33.068  1.00 61.54  ? 56   VAL   A HG22 1 
ATOM   804   H  HG23 . VAL   A  1  56  ? 8.623   -15.145 -33.999  1.00 61.54  ? 56   VAL   A HG23 1 
ATOM   805   N  N    . LEU   A  1  57  ? 8.419   -10.112 -33.568  1.00 57.34  ? 57   LEU   A N    1 
ATOM   806   C  CA   . LEU   A  1  57  ? 8.198   -8.719  -33.929  1.00 59.83  ? 57   LEU   A CA   1 
ATOM   807   C  C    . LEU   A  1  57  ? 9.490   -8.076  -34.413  1.00 57.96  ? 57   LEU   A C    1 
ATOM   808   O  O    . LEU   A  1  57  ? 10.565  -8.314  -33.852  1.00 56.30  ? 57   LEU   A O    1 
ATOM   809   C  CB   . LEU   A  1  57  ? 7.651   -7.908  -32.747  1.00 61.80  ? 57   LEU   A CB   1 
ATOM   810   C  CG   . LEU   A  1  57  ? 6.266   -8.267  -32.210  1.00 61.03  ? 57   LEU   A CG   1 
ATOM   811   C  CD1  . LEU   A  1  57  ? 6.378   -9.210  -31.026  1.00 59.50  ? 57   LEU   A CD1  1 
ATOM   812   C  CD2  . LEU   A  1  57  ? 5.507   -7.005  -31.826  1.00 61.93  ? 57   LEU   A CD2  1 
ATOM   813   H  H    . LEU   A  1  57  ? 8.960   -10.217 -32.908  1.00 68.85  ? 57   LEU   A H    1 
ATOM   814   H  HA   . LEU   A  1  57  ? 7.554   -8.693  -34.654  1.00 71.84  ? 57   LEU   A HA   1 
ATOM   815   H  HB2  . LEU   A  1  57  ? 8.272   -8.010  -32.008  1.00 74.20  ? 57   LEU   A HB2  1 
ATOM   816   H  HB3  . LEU   A  1  57  ? 7.612   -6.979  -33.021  1.00 74.20  ? 57   LEU   A HB3  1 
ATOM   817   H  HG   . LEU   A  1  57  ? 5.763   -8.722  -32.904  1.00 73.27  ? 57   LEU   A HG   1 
ATOM   818   H  HD11 . LEU   A  1  57  ? 5.487   -9.427  -30.709  1.00 71.43  ? 57   LEU   A HD11 1 
ATOM   819   H  HD12 . LEU   A  1  57  ? 6.834   -10.019 -31.308  1.00 71.43  ? 57   LEU   A HD12 1 
ATOM   820   H  HD13 . LEU   A  1  57  ? 6.883   -8.774  -30.321  1.00 71.43  ? 57   LEU   A HD13 1 
ATOM   821   H  HD21 . LEU   A  1  57  ? 4.643   -7.254  -31.462  1.00 74.35  ? 57   LEU   A HD21 1 
ATOM   822   H  HD22 . LEU   A  1  57  ? 6.019   -6.519  -31.160  1.00 74.35  ? 57   LEU   A HD22 1 
ATOM   823   H  HD23 . LEU   A  1  57  ? 5.387   -6.455  -32.616  1.00 74.35  ? 57   LEU   A HD23 1 
ATOM   824   N  N    . LYS   A  1  58  ? 9.370   -7.261  -35.456  1.00 58.99  ? 58   LYS   A N    1 
ATOM   825   C  CA   . LYS   A  1  58  ? 10.446  -6.397  -35.925  1.00 63.26  ? 58   LYS   A CA   1 
ATOM   826   C  C    . LYS   A  1  58  ? 10.227  -5.007  -35.342  1.00 67.18  ? 58   LYS   A C    1 
ATOM   827   O  O    . LYS   A  1  58  ? 9.110   -4.482  -35.388  1.00 68.81  ? 58   LYS   A O    1 
ATOM   828   C  CB   . LYS   A  1  58  ? 10.471  -6.345  -37.454  1.00 67.36  ? 58   LYS   A CB   1 
ATOM   829   C  CG   . LYS   A  1  58  ? 11.609  -5.523  -38.043  1.00 74.91  ? 58   LYS   A CG   1 
ATOM   830   C  CD   . LYS   A  1  58  ? 11.928  -5.955  -39.472  1.00 81.69  ? 58   LYS   A CD   1 
ATOM   831   C  CE   . LYS   A  1  58  ? 10.897  -5.451  -40.471  1.00 87.80  ? 58   LYS   A CE   1 
ATOM   832   N  NZ   . LYS   A  1  58  ? 10.884  -6.274  -41.715  1.00 90.64  ? 58   LYS   A NZ   1 
ATOM   833   H  H    . LYS   A  1  58  ? 8.652   -7.189  -35.923  1.00 70.83  ? 58   LYS   A H    1 
ATOM   834   H  HA   . LYS   A  1  58  ? 11.307  -6.731  -35.628  1.00 75.95  ? 58   LYS   A HA   1 
ATOM   835   H  HB2  . LYS   A  1  58  ? 10.560  -7.251  -37.791  1.00 80.87  ? 58   LYS   A HB2  1 
ATOM   836   H  HB3  . LYS   A  1  58  ? 9.638   -5.956  -37.763  1.00 80.87  ? 58   LYS   A HB3  1 
ATOM   837   H  HG2  . LYS   A  1  58  ? 11.355  -4.587  -38.056  1.00 89.93  ? 58   LYS   A HG2  1 
ATOM   838   H  HG3  . LYS   A  1  58  ? 12.406  -5.643  -37.502  1.00 89.93  ? 58   LYS   A HG3  1 
ATOM   839   H  HD2  . LYS   A  1  58  ? 12.794  -5.599  -39.726  1.00 98.06  ? 58   LYS   A HD2  1 
ATOM   840   H  HD3  . LYS   A  1  58  ? 11.942  -6.924  -39.516  1.00 98.06  ? 58   LYS   A HD3  1 
ATOM   841   H  HE2  . LYS   A  1  58  ? 10.015  -5.492  -40.070  1.00 105.40 ? 58   LYS   A HE2  1 
ATOM   842   H  HE3  . LYS   A  1  58  ? 11.109  -4.536  -40.715  1.00 105.40 ? 58   LYS   A HE3  1 
ATOM   843   H  HZ1  . LYS   A  1  58  ? 10.288  -5.948  -42.290  1.00 108.81 ? 58   LYS   A HZ1  1 
ATOM   844   H  HZ2  . LYS   A  1  58  ? 11.688  -6.263  -42.096  1.00 108.81 ? 58   LYS   A HZ2  1 
ATOM   845   H  HZ3  . LYS   A  1  58  ? 10.669  -7.115  -41.521  1.00 108.81 ? 58   LYS   A HZ3  1 
ATOM   846   N  N    . CYS   A  1  59  ? 11.284  -4.416  -34.787  1.00 69.49  ? 59   CYS   A N    1 
ATOM   847   C  CA   . CYS   A  1  59  ? 11.185  -3.146  -34.080  1.00 76.92  ? 59   CYS   A CA   1 
ATOM   848   C  C    . CYS   A  1  59  ? 12.112  -2.117  -34.712  1.00 83.49  ? 59   CYS   A C    1 
ATOM   849   O  O    . CYS   A  1  59  ? 13.314  -2.363  -34.859  1.00 84.33  ? 59   CYS   A O    1 
ATOM   850   C  CB   . CYS   A  1  59  ? 11.528  -3.317  -32.596  1.00 75.44  ? 59   CYS   A CB   1 
ATOM   851   S  SG   . CYS   A  1  59  ? 10.467  -4.473  -31.687  1.00 75.71  ? 59   CYS   A SG   1 
ATOM   852   H  H    . CYS   A  1  59  ? 12.081  -4.739  -34.809  1.00 83.42  ? 59   CYS   A H    1 
ATOM   853   H  HA   . CYS   A  1  59  ? 10.277  -2.814  -34.157  1.00 92.34  ? 59   CYS   A HA   1 
ATOM   854   H  HB2  . CYS   A  1  59  ? 12.439  -3.644  -32.529  1.00 90.56  ? 59   CYS   A HB2  1 
ATOM   855   H  HB3  . CYS   A  1  59  ? 11.454  -2.452  -32.163  1.00 90.56  ? 59   CYS   A HB3  1 
ATOM   856   N  N    . ASP   A  1  60  ? 11.550  -0.965  -35.077  1.00 88.20  ? 60   ASP   A N    1 
ATOM   857   C  CA   . ASP   A  1  60  ? 12.358  0.140   -35.572  1.00 92.78  ? 60   ASP   A CA   1 
ATOM   858   C  C    . ASP   A  1  60  ? 13.341  0.593   -34.500  1.00 94.74  ? 60   ASP   A C    1 
ATOM   859   O  O    . ASP   A  1  60  ? 13.056  0.527   -33.301  1.00 88.77  ? 60   ASP   A O    1 
ATOM   860   C  CB   . ASP   A  1  60  ? 11.472  1.321   -35.972  1.00 95.03  ? 60   ASP   A CB   1 
ATOM   861   C  CG   . ASP   A  1  60  ? 10.492  0.976   -37.072  1.00 98.85  ? 60   ASP   A CG   1 
ATOM   862   O  OD1  . ASP   A  1  60  ? 10.403  -0.211  -37.449  1.00 98.49  ? 60   ASP   A OD1  1 
ATOM   863   O  OD2  . ASP   A  1  60  ? 9.809   1.900   -37.562  1.00 104.65 ? 60   ASP   A OD2  1 
ATOM   864   H  H    . ASP   A  1  60  ? 10.707  -0.801  -35.046  1.00 105.87 ? 60   ASP   A H    1 
ATOM   865   H  HA   . ASP   A  1  60  ? 12.851  -0.153  -36.355  1.00 111.37 ? 60   ASP   A HA   1 
ATOM   866   H  HB2  . ASP   A  1  60  ? 10.963  1.609   -35.198  1.00 114.08 ? 60   ASP   A HB2  1 
ATOM   867   H  HB3  . ASP   A  1  60  ? 12.034  2.045   -36.288  1.00 114.08 ? 60   ASP   A HB3  1 
ATOM   868   N  N    . TRP   A  1  61  ? 14.505  1.072   -34.935  1.00 104.30 ? 61   TRP   A N    1 
ATOM   869   C  CA   . TRP   A  1  61  ? 15.460  1.695   -34.027  1.00 112.25 ? 61   TRP   A CA   1 
ATOM   870   C  C    . TRP   A  1  61  ? 15.269  3.207   -34.077  1.00 127.84 ? 61   TRP   A C    1 
ATOM   871   O  O    . TRP   A  1  61  ? 15.602  3.851   -35.079  1.00 143.77 ? 61   TRP   A O    1 
ATOM   872   C  CB   . TRP   A  1  61  ? 16.907  1.342   -34.358  1.00 104.92 ? 61   TRP   A CB   1 
ATOM   873   C  CG   . TRP   A  1  61  ? 17.841  2.147   -33.501  1.00 96.48  ? 61   TRP   A CG   1 
ATOM   874   C  CD1  . TRP   A  1  61  ? 17.932  2.109   -32.140  1.00 92.07  ? 61   TRP   A CD1  1 
ATOM   875   C  CD2  . TRP   A  1  61  ? 18.788  3.129   -33.938  1.00 92.65  ? 61   TRP   A CD2  1 
ATOM   876   N  NE1  . TRP   A  1  61  ? 18.881  2.999   -31.703  1.00 91.84  ? 61   TRP   A NE1  1 
ATOM   877   C  CE2  . TRP   A  1  61  ? 19.423  3.637   -32.787  1.00 91.77  ? 61   TRP   A CE2  1 
ATOM   878   C  CE3  . TRP   A  1  61  ? 19.166  3.624   -35.189  1.00 91.05  ? 61   TRP   A CE3  1 
ATOM   879   C  CZ2  . TRP   A  1  61  ? 20.412  4.614   -32.849  1.00 92.47  ? 61   TRP   A CZ2  1 
ATOM   880   C  CZ3  . TRP   A  1  61  ? 20.151  4.593   -35.249  1.00 92.32  ? 61   TRP   A CZ3  1 
ATOM   881   C  CH2  . TRP   A  1  61  ? 20.762  5.078   -34.086  1.00 93.36  ? 61   TRP   A CH2  1 
ATOM   882   H  H    . TRP   A  1  61  ? 14.763  1.046   -35.755  1.00 125.20 ? 61   TRP   A H    1 
ATOM   883   H  HA   . TRP   A  1  61  ? 15.269  1.368   -33.134  1.00 134.74 ? 61   TRP   A HA   1 
ATOM   884   H  HB2  . TRP   A  1  61  ? 17.061  0.400   -34.186  1.00 125.94 ? 61   TRP   A HB2  1 
ATOM   885   H  HB3  . TRP   A  1  61  ? 17.088  1.543   -35.290  1.00 125.94 ? 61   TRP   A HB3  1 
ATOM   886   H  HD1  . TRP   A  1  61  ? 17.425  1.559   -31.588  1.00 110.52 ? 61   TRP   A HD1  1 
ATOM   887   H  HE1  . TRP   A  1  61  ? 19.099  3.134   -30.882  1.00 110.24 ? 61   TRP   A HE1  1 
ATOM   888   H  HE3  . TRP   A  1  61  ? 18.763  3.309   -35.966  1.00 109.30 ? 61   TRP   A HE3  1 
ATOM   889   H  HZ2  . TRP   A  1  61  ? 20.820  4.938   -32.079  1.00 111.00 ? 61   TRP   A HZ2  1 
ATOM   890   H  HZ3  . TRP   A  1  61  ? 20.412  4.929   -36.076  1.00 110.82 ? 61   TRP   A HZ3  1 
ATOM   891   H  HH2  . TRP   A  1  61  ? 21.421  5.730   -34.157  1.00 112.07 ? 61   TRP   A HH2  1 
ATOM   892   N  N    . SER   A  1  62  ? 14.711  3.763   -33.005  1.00 125.45 ? 62   SER   A N    1 
ATOM   893   C  CA   . SER   A  1  62  ? 14.729  5.198   -32.757  1.00 139.23 ? 62   SER   A CA   1 
ATOM   894   C  C    . SER   A  1  62  ? 13.840  5.991   -33.706  1.00 146.04 ? 62   SER   A C    1 
ATOM   895   O  O    . SER   A  1  62  ? 13.289  7.022   -33.306  1.00 149.97 ? 62   SER   A O    1 
ATOM   896   C  CB   . SER   A  1  62  ? 16.162  5.730   -32.842  1.00 147.50 ? 62   SER   A CB   1 
ATOM   897   O  OG   . SER   A  1  62  ? 16.225  7.075   -32.399  1.00 155.39 ? 62   SER   A OG   1 
ATOM   898   H  H    . SER   A  1  62  ? 14.305  3.318   -32.391  1.00 150.57 ? 62   SER   A H    1 
ATOM   899   H  HA   . SER   A  1  62  ? 14.377  5.335   -31.864  1.00 167.11 ? 62   SER   A HA   1 
ATOM   900   H  HB2  . SER   A  1  62  ? 16.736  5.185   -32.281  1.00 177.03 ? 62   SER   A HB2  1 
ATOM   901   H  HB3  . SER   A  1  62  ? 16.461  5.687   -33.764  1.00 177.03 ? 62   SER   A HB3  1 
ATOM   902   H  HG   . SER   A  1  62  ? 17.018  7.351   -32.430  1.00 186.50 ? 62   SER   A HG   1 
ATOM   903   N  N    . SER   A  1  63  ? 13.706  5.555   -34.958  1.00 143.61 ? 63   SER   A N    1 
ATOM   904   C  CA   . SER   A  1  63  ? 12.774  6.214   -35.864  1.00 146.79 ? 63   SER   A CA   1 
ATOM   905   C  C    . SER   A  1  63  ? 11.449  6.483   -35.158  1.00 143.74 ? 63   SER   A C    1 
ATOM   906   O  O    . SER   A  1  63  ? 10.856  7.554   -35.314  1.00 148.54 ? 63   SER   A O    1 
ATOM   907   C  CB   . SER   A  1  63  ? 12.540  5.363   -37.111  1.00 145.21 ? 63   SER   A CB   1 
ATOM   908   O  OG   . SER   A  1  63  ? 13.658  5.393   -37.979  1.00 142.06 ? 63   SER   A OG   1 
ATOM   909   H  H    . SER   A  1  63  ? 14.136  4.892   -35.298  1.00 172.37 ? 63   SER   A H    1 
ATOM   910   H  HA   . SER   A  1  63  ? 13.153  7.061   -36.147  1.00 176.18 ? 63   SER   A HA   1 
ATOM   911   H  HB2  . SER   A  1  63  ? 12.380  4.446   -36.839  1.00 174.28 ? 63   SER   A HB2  1 
ATOM   912   H  HB3  . SER   A  1  63  ? 11.767  5.707   -37.585  1.00 174.28 ? 63   SER   A HB3  1 
ATOM   913   H  HG   . SER   A  1  63  ? 13.466  5.024   -38.709  1.00 170.51 ? 63   SER   A HG   1 
ATOM   914   N  N    . THR   A  1  64  ? 10.985  5.507   -34.377  1.00 133.00 ? 64   THR   A N    1 
ATOM   915   C  CA   . THR   A  1  64  ? 9.695   5.596   -33.708  1.00 136.22 ? 64   THR   A CA   1 
ATOM   916   C  C    . THR   A  1  64  ? 9.678   4.774   -32.423  1.00 124.05 ? 64   THR   A C    1 
ATOM   917   O  O    . THR   A  1  64  ? 8.915   5.077   -31.501  1.00 121.24 ? 64   THR   A O    1 
ATOM   918   C  CB   . THR   A  1  64  ? 8.574   5.104   -34.630  1.00 140.26 ? 64   THR   A CB   1 
ATOM   919   O  OG1  . THR   A  1  64  ? 8.537   3.672   -34.604  1.00 126.59 ? 64   THR   A OG1  1 
ATOM   920   C  CG2  . THR   A  1  64  ? 8.794   5.558   -36.072  1.00 153.68 ? 64   THR   A CG2  1 
ATOM   921   H  H    . THR   A  1  64  ? 11.407  4.774   -34.219  1.00 159.63 ? 64   THR   A H    1 
ATOM   922   H  HA   . THR   A  1  64  ? 9.535   6.526   -33.485  1.00 163.50 ? 64   THR   A HA   1 
ATOM   923   H  HB   . THR   A  1  64  ? 7.732   5.472   -34.323  1.00 168.35 ? 64   THR   A HB   1 
ATOM   924   H  HG1  . THR   A  1  64  ? 9.185   3.359   -35.037  1.00 151.95 ? 64   THR   A HG1  1 
ATOM   925   H  HG21 . THR   A  1  64  ? 8.086   5.215   -36.639  1.00 184.45 ? 64   THR   A HG21 1 
ATOM   926   H  HG22 . THR   A  1  64  ? 8.793   6.527   -36.118  1.00 184.45 ? 64   THR   A HG22 1 
ATOM   927   H  HG23 . THR   A  1  64  ? 9.646   5.228   -36.398  1.00 184.45 ? 64   THR   A HG23 1 
ATOM   928   N  N    . ARG   A  1  65  ? 10.514  3.731   -32.359  1.00 120.19 ? 65   ARG   A N    1 
ATOM   929   C  CA   . ARG   A  1  65  ? 10.482  2.719   -31.301  1.00 117.08 ? 65   ARG   A CA   1 
ATOM   930   C  C    . ARG   A  1  65  ? 9.241   1.833   -31.399  1.00 113.92 ? 65   ARG   A C    1 
ATOM   931   O  O    . ARG   A  1  65  ? 8.769   1.300   -30.391  1.00 110.81 ? 65   ARG   A O    1 
ATOM   932   C  CB   . ARG   A  1  65  ? 10.570  3.340   -29.900  1.00 120.11 ? 65   ARG   A CB   1 
ATOM   933   C  CG   . ARG   A  1  65  ? 11.936  3.903   -29.540  1.00 120.41 ? 65   ARG   A CG   1 
ATOM   934   C  CD   . ARG   A  1  65  ? 12.237  3.754   -28.050  1.00 118.20 ? 65   ARG   A CD   1 
ATOM   935   N  NE   . ARG   A  1  65  ? 11.095  4.094   -27.202  1.00 122.51 ? 65   ARG   A NE   1 
ATOM   936   C  CZ   . ARG   A  1  65  ? 11.179  4.377   -25.905  1.00 129.08 ? 65   ARG   A CZ   1 
ATOM   937   N  NH1  . ARG   A  1  65  ? 12.356  4.381   -25.293  1.00 127.19 ? 65   ARG   A NH1  1 
ATOM   938   N  NH2  . ARG   A  1  65  ? 10.084  4.669   -25.218  1.00 136.55 ? 65   ARG   A NH2  1 
ATOM   939   H  H    . ARG   A  1  65  ? 11.130  3.584   -32.941  1.00 144.26 ? 65   ARG   A H    1 
ATOM   940   H  HA   . ARG   A  1  65  ? 11.263  2.155   -31.417  1.00 140.54 ? 65   ARG   A HA   1 
ATOM   941   H  HB2  . ARG   A  1  65  ? 9.930   4.068   -29.845  1.00 144.17 ? 65   ARG   A HB2  1 
ATOM   942   H  HB3  . ARG   A  1  65  ? 10.353  2.658   -29.246  1.00 144.17 ? 65   ARG   A HB3  1 
ATOM   943   H  HG2  . ARG   A  1  65  ? 12.620  3.426   -30.037  1.00 144.53 ? 65   ARG   A HG2  1 
ATOM   944   H  HG3  . ARG   A  1  65  ? 11.963  4.846   -29.763  1.00 144.53 ? 65   ARG   A HG3  1 
ATOM   945   H  HD2  . ARG   A  1  65  ? 12.482  2.834   -27.867  1.00 141.87 ? 65   ARG   A HD2  1 
ATOM   946   H  HD3  . ARG   A  1  65  ? 12.970  4.345   -27.816  1.00 141.87 ? 65   ARG   A HD3  1 
ATOM   947   H  HE   . ARG   A  1  65  ? 10.317  4.113   -27.567  1.00 147.05 ? 65   ARG   A HE   1 
ATOM   948   H  HH11 . ARG   A  1  65  ? 13.071  4.200   -25.736  1.00 152.67 ? 65   ARG   A HH11 1 
ATOM   949   H  HH12 . ARG   A  1  65  ? 12.404  4.564   -24.455  1.00 152.67 ? 65   ARG   A HH12 1 
ATOM   950   H  HH21 . ARG   A  1  65  ? 9.319   4.676   -25.611  1.00 163.90 ? 65   ARG   A HH21 1 
ATOM   951   H  HH22 . ARG   A  1  65  ? 10.138  4.852   -24.379  1.00 163.90 ? 65   ARG   A HH22 1 
ATOM   952   N  N    . ARG   A  1  66  ? 8.710   1.656   -32.606  1.00 114.46 ? 66   ARG   A N    1 
ATOM   953   C  CA   . ARG   A  1  66  ? 7.524   0.844   -32.829  1.00 111.65 ? 66   ARG   A CA   1 
ATOM   954   C  C    . ARG   A  1  66  ? 7.915   -0.575  -33.227  1.00 99.59  ? 66   ARG   A C    1 
ATOM   955   O  O    . ARG   A  1  66  ? 8.937   -0.798  -33.880  1.00 99.77  ? 66   ARG   A O    1 
ATOM   956   C  CB   . ARG   A  1  66  ? 6.632   1.455   -33.915  1.00 121.30 ? 66   ARG   A CB   1 
ATOM   957   C  CG   . ARG   A  1  66  ? 5.949   2.756   -33.504  1.00 130.91 ? 66   ARG   A CG   1 
ATOM   958   C  CD   . ARG   A  1  66  ? 4.818   3.146   -34.457  1.00 139.41 ? 66   ARG   A CD   1 
ATOM   959   N  NE   . ARG   A  1  66  ? 5.254   3.381   -35.834  1.00 151.12 ? 66   ARG   A NE   1 
ATOM   960   C  CZ   . ARG   A  1  66  ? 5.592   4.570   -36.332  1.00 162.95 ? 66   ARG   A CZ   1 
ATOM   961   N  NH1  . ARG   A  1  66  ? 5.569   5.656   -35.570  1.00 169.20 ? 66   ARG   A NH1  1 
ATOM   962   N  NH2  . ARG   A  1  66  ? 5.962   4.671   -37.602  1.00 166.62 ? 66   ARG   A NH2  1 
ATOM   963   H  H    . ARG   A  1  66  ? 9.028   2.006   -33.325  1.00 137.39 ? 66   ARG   A H    1 
ATOM   964   H  HA   . ARG   A  1  66  ? 7.012   0.799   -32.006  1.00 134.02 ? 66   ARG   A HA   1 
ATOM   965   H  HB2  . ARG   A  1  66  ? 7.178   1.644   -34.694  1.00 145.59 ? 66   ARG   A HB2  1 
ATOM   966   H  HB3  . ARG   A  1  66  ? 5.938   0.817   -34.142  1.00 145.59 ? 66   ARG   A HB3  1 
ATOM   967   H  HG2  . ARG   A  1  66  ? 5.571   2.650   -32.617  1.00 157.13 ? 66   ARG   A HG2  1 
ATOM   968   H  HG3  . ARG   A  1  66  ? 6.602   3.472   -33.503  1.00 157.13 ? 66   ARG   A HG3  1 
ATOM   969   H  HD2  . ARG   A  1  66  ? 4.164   2.430   -34.473  1.00 167.33 ? 66   ARG   A HD2  1 
ATOM   970   H  HD3  . ARG   A  1  66  ? 4.408   3.964   -34.134  1.00 167.33 ? 66   ARG   A HD3  1 
ATOM   971   H  HE   . ARG   A  1  66  ? 5.294   2.703   -36.361  1.00 181.38 ? 66   ARG   A HE   1 
ATOM   972   H  HH11 . ARG   A  1  66  ? 5.334   5.598   -34.745  1.00 203.08 ? 66   ARG   A HH11 1 
ATOM   973   H  HH12 . ARG   A  1  66  ? 5.790   6.419   -35.902  1.00 203.08 ? 66   ARG   A HH12 1 
ATOM   974   H  HH21 . ARG   A  1  66  ? 5.983   3.971   -38.102  1.00 199.98 ? 66   ARG   A HH21 1 
ATOM   975   H  HH22 . ARG   A  1  66  ? 6.181   5.437   -37.927  1.00 199.98 ? 66   ARG   A HH22 1 
ATOM   976   N  N    . CYS   A  1  67  ? 7.085   -1.533  -32.823  1.00 91.96  ? 67   CYS   A N    1 
ATOM   977   C  CA   . CYS   A  1  67  ? 7.269   -2.939  -33.153  1.00 84.86  ? 67   CYS   A CA   1 
ATOM   978   C  C    . CYS   A  1  67  ? 6.041   -3.447  -33.895  1.00 84.41  ? 67   CYS   A C    1 
ATOM   979   O  O    . CYS   A  1  67  ? 4.905   -3.161  -33.501  1.00 84.95  ? 67   CYS   A O    1 
ATOM   980   C  CB   . CYS   A  1  67  ? 7.504   -3.781  -31.894  1.00 81.16  ? 67   CYS   A CB   1 
ATOM   981   S  SG   . CYS   A  1  67  ? 8.968   -3.325  -30.930  1.00 84.48  ? 67   CYS   A SG   1 
ATOM   982   H  H    . CYS   A  1  67  ? 6.387   -1.387  -32.341  1.00 110.39 ? 67   CYS   A H    1 
ATOM   983   H  HA   . CYS   A  1  67  ? 8.043   -3.039  -33.731  1.00 101.87 ? 67   CYS   A HA   1 
ATOM   984   H  HB2  . CYS   A  1  67  ? 6.732   -3.687  -31.314  1.00 97.42  ? 67   CYS   A HB2  1 
ATOM   985   H  HB3  . CYS   A  1  67  ? 7.608   -4.708  -32.160  1.00 97.42  ? 67   CYS   A HB3  1 
ATOM   986   N  N    . GLN   A  1  68  ? 6.272   -4.199  -34.970  1.00 84.92  ? 68   GLN   A N    1 
ATOM   987   C  CA   . GLN   A  1  68  ? 5.197   -4.782  -35.758  1.00 87.48  ? 68   GLN   A CA   1 
ATOM   988   C  C    . GLN   A  1  68  ? 5.465   -6.263  -35.984  1.00 80.62  ? 68   GLN   A C    1 
ATOM   989   O  O    . GLN   A  1  68  ? 6.600   -6.647  -36.289  1.00 82.51  ? 68   GLN   A O    1 
ATOM   990   C  CB   . GLN   A  1  68  ? 5.051   -4.063  -37.108  1.00 92.88  ? 68   GLN   A CB   1 
ATOM   991   C  CG   . GLN   A  1  68  ? 4.130   -2.854  -37.056  1.00 98.94  ? 68   GLN   A CG   1 
ATOM   992   C  CD   . GLN   A  1  68  ? 4.154   -2.038  -38.333  1.00 106.22 ? 68   GLN   A CD   1 
ATOM   993   O  OE1  . GLN   A  1  68  ? 4.612   -2.505  -39.375  1.00 109.06 ? 68   GLN   A OE1  1 
ATOM   994   N  NE2  . GLN   A  1  68  ? 3.663   -0.806  -38.255  1.00 112.63 ? 68   GLN   A NE2  1 
ATOM   995   H  H    . GLN   A  1  68  ? 7.058   -4.387  -35.265  1.00 101.94 ? 68   GLN   A H    1 
ATOM   996   H  HA   . GLN   A  1  68  ? 4.359   -4.694  -35.278  1.00 105.02 ? 68   GLN   A HA   1 
ATOM   997   H  HB2  . GLN   A  1  68  ? 5.926   -3.758  -37.397  1.00 111.49 ? 68   GLN   A HB2  1 
ATOM   998   H  HB3  . GLN   A  1  68  ? 4.687   -4.686  -37.757  1.00 111.49 ? 68   GLN   A HB3  1 
ATOM   999   H  HG2  . GLN   A  1  68  ? 3.220   -3.156  -36.911  1.00 118.76 ? 68   GLN   A HG2  1 
ATOM   1000  H  HG3  . GLN   A  1  68  ? 4.407   -2.277  -36.327  1.00 118.76 ? 68   GLN   A HG3  1 
ATOM   1001  H  HE21 . GLN   A  1  68  ? 3.354   -0.512  -37.508  1.00 135.20 ? 68   GLN   A HE21 1 
ATOM   1002  H  HE22 . GLN   A  1  68  ? 3.654   -0.302  -38.952  1.00 135.20 ? 68   GLN   A HE22 1 
ATOM   1003  N  N    . PRO   A  1  69  ? 4.452   -7.121  -35.841  1.00 72.28  ? 69   PRO   A N    1 
ATOM   1004  C  CA   . PRO   A  1  69  ? 4.692   -8.562  -35.989  1.00 65.63  ? 69   PRO   A CA   1 
ATOM   1005  C  C    . PRO   A  1  69  ? 5.119   -8.927  -37.402  1.00 64.12  ? 69   PRO   A C    1 
ATOM   1006  O  O    . PRO   A  1  69  ? 4.632   -8.366  -38.386  1.00 68.38  ? 69   PRO   A O    1 
ATOM   1007  C  CB   . PRO   A  1  69  ? 3.337   -9.190  -35.635  1.00 65.23  ? 69   PRO   A CB   1 
ATOM   1008  C  CG   . PRO   A  1  69  ? 2.593   -8.138  -34.894  1.00 68.48  ? 69   PRO   A CG   1 
ATOM   1009  C  CD   . PRO   A  1  69  ? 3.056   -6.839  -35.459  1.00 71.20  ? 69   PRO   A CD   1 
ATOM   1010  H  HA   . PRO   A  1  69  ? 5.370   -8.854  -35.359  1.00 78.79  ? 69   PRO   A HA   1 
ATOM   1011  H  HB2  . PRO   A  1  69  ? 2.868   -9.437  -36.448  1.00 78.31  ? 69   PRO   A HB2  1 
ATOM   1012  H  HB3  . PRO   A  1  69  ? 3.473   -9.973  -35.080  1.00 78.31  ? 69   PRO   A HB3  1 
ATOM   1013  H  HG2  . PRO   A  1  69  ? 1.639   -8.253  -35.032  1.00 82.21  ? 69   PRO   A HG2  1 
ATOM   1014  H  HG3  . PRO   A  1  69  ? 2.800   -8.196  -33.948  1.00 82.21  ? 69   PRO   A HG3  1 
ATOM   1015  H  HD2  . PRO   A  1  69  ? 2.529   -6.590  -36.234  1.00 85.47  ? 69   PRO   A HD2  1 
ATOM   1016  H  HD3  . PRO   A  1  69  ? 3.016   -6.136  -34.791  1.00 85.47  ? 69   PRO   A HD3  1 
ATOM   1017  N  N    . ILE   A  1  70  ? 6.039   -9.879  -37.496  1.00 61.75  ? 70   ILE   A N    1 
ATOM   1018  C  CA   . ILE   A  1  70  ? 6.437   -10.449 -38.776  1.00 64.54  ? 70   ILE   A CA   1 
ATOM   1019  C  C    . ILE   A  1  70  ? 5.461   -11.564 -39.130  1.00 72.27  ? 70   ILE   A C    1 
ATOM   1020  O  O    . ILE   A  1  70  ? 5.209   -12.463 -38.318  1.00 73.07  ? 70   ILE   A O    1 
ATOM   1021  C  CB   . ILE   A  1  70  ? 7.881   -10.972 -38.722  1.00 56.72  ? 70   ILE   A CB   1 
ATOM   1022  C  CG1  . ILE   A  1  70  ? 8.851   -9.827  -38.420  1.00 52.53  ? 70   ILE   A CG1  1 
ATOM   1023  C  CG2  . ILE   A  1  70  ? 8.256   -11.656 -40.037  1.00 53.86  ? 70   ILE   A CG2  1 
ATOM   1024  C  CD1  . ILE   A  1  70  ? 10.284  -10.275 -38.207  1.00 51.03  ? 70   ILE   A CD1  1 
ATOM   1025  H  H    . ILE   A  1  70  ? 6.452   -10.218 -36.822  1.00 74.14  ? 70   ILE   A H    1 
ATOM   1026  H  HA   . ILE   A  1  70  ? 6.390   -9.766  -39.463  1.00 77.48  ? 70   ILE   A HA   1 
ATOM   1027  H  HB   . ILE   A  1  70  ? 7.941   -11.627 -38.009  1.00 68.10  ? 70   ILE   A HB   1 
ATOM   1028  H  HG12 . ILE   A  1  70  ? 8.843   -9.207  -39.166  1.00 62.85  ? 70   ILE   A HG12 1 
ATOM   1029  H  HG13 . ILE   A  1  70  ? 8.559   -9.377  -37.612  1.00 62.85  ? 70   ILE   A HG13 1 
ATOM   1030  H  HG21 . ILE   A  1  70  ? 9.161   -11.997 -39.968  1.00 64.67  ? 70   ILE   A HG21 1 
ATOM   1031  H  HG22 . ILE   A  1  70  ? 7.639   -12.386 -40.200  1.00 64.67  ? 70   ILE   A HG22 1 
ATOM   1032  H  HG23 . ILE   A  1  70  ? 8.200   -11.008 -40.757  1.00 64.67  ? 70   ILE   A HG23 1 
ATOM   1033  H  HD11 . ILE   A  1  70  ? 10.825  -9.505  -37.976  1.00 61.20  ? 70   ILE   A HD11 1 
ATOM   1034  H  HD12 . ILE   A  1  70  ? 10.308  -10.925 -37.487  1.00 61.20  ? 70   ILE   A HD12 1 
ATOM   1035  H  HD13 . ILE   A  1  70  ? 10.614  -10.677 -39.026  1.00 61.20  ? 70   ILE   A HD13 1 
ATOM   1036  N  N    . GLU   A  1  71  ? 4.912   -11.511 -40.341  1.00 80.90  ? 71   GLU   A N    1 
ATOM   1037  C  CA   . GLU   A  1  71  ? 3.973   -12.533 -40.801  1.00 85.57  ? 71   GLU   A CA   1 
ATOM   1038  C  C    . GLU   A  1  71  ? 4.770   -13.707 -41.356  1.00 83.78  ? 71   GLU   A C    1 
ATOM   1039  O  O    . GLU   A  1  71  ? 5.089   -13.766 -42.545  1.00 85.72  ? 71   GLU   A O    1 
ATOM   1040  C  CB   . GLU   A  1  71  ? 3.019   -11.967 -41.846  1.00 92.13  ? 71   GLU   A CB   1 
ATOM   1041  C  CG   . GLU   A  1  71  ? 1.965   -12.966 -42.314  1.00 97.86  ? 71   GLU   A CG   1 
ATOM   1042  C  CD   . GLU   A  1  71  ? 1.120   -12.441 -43.458  1.00 107.59 ? 71   GLU   A CD   1 
ATOM   1043  O  OE1  . GLU   A  1  71  ? 0.730   -11.255 -43.417  1.00 116.11 ? 71   GLU   A OE1  1 
ATOM   1044  O  OE2  . GLU   A  1  71  ? 0.851   -13.214 -44.401  1.00 111.86 ? 71   GLU   A OE2  1 
ATOM   1045  H  H    . GLU   A  1  71  ? 5.067   -10.891 -40.916  1.00 97.11  ? 71   GLU   A H    1 
ATOM   1046  H  HA   . GLU   A  1  71  ? 3.451   -12.843 -40.044  1.00 102.72 ? 71   GLU   A HA   1 
ATOM   1047  H  HB2  . GLU   A  1  71  ? 2.556   -11.204 -41.466  1.00 110.59 ? 71   GLU   A HB2  1 
ATOM   1048  H  HB3  . GLU   A  1  71  ? 3.532   -11.692 -42.621  1.00 110.59 ? 71   GLU   A HB3  1 
ATOM   1049  H  HG2  . GLU   A  1  71  ? 2.409   -13.774 -42.617  1.00 117.47 ? 71   GLU   A HG2  1 
ATOM   1050  H  HG3  . GLU   A  1  71  ? 1.373   -13.171 -41.574  1.00 117.47 ? 71   GLU   A HG3  1 
ATOM   1051  N  N    . PHE   A  1  72  ? 5.105   -14.655 -40.478  1.00 79.24  ? 72   PHE   A N    1 
ATOM   1052  C  CA   . PHE   A  1  72  ? 5.685   -15.913 -40.934  1.00 72.45  ? 72   PHE   A CA   1 
ATOM   1053  C  C    . PHE   A  1  72  ? 4.607   -16.855 -41.452  1.00 70.91  ? 72   PHE   A C    1 
ATOM   1054  O  O    . PHE   A  1  72  ? 4.796   -17.523 -42.475  1.00 73.19  ? 72   PHE   A O    1 
ATOM   1055  C  CB   . PHE   A  1  72  ? 6.453   -16.593 -39.800  1.00 65.09  ? 72   PHE   A CB   1 
ATOM   1056  C  CG   . PHE   A  1  72  ? 7.781   -15.966 -39.496  1.00 61.93  ? 72   PHE   A CG   1 
ATOM   1057  C  CD1  . PHE   A  1  72  ? 8.923   -16.376 -40.162  1.00 61.68  ? 72   PHE   A CD1  1 
ATOM   1058  C  CD2  . PHE   A  1  72  ? 7.890   -14.982 -38.528  1.00 61.49  ? 72   PHE   A CD2  1 
ATOM   1059  C  CE1  . PHE   A  1  72  ? 10.149  -15.808 -39.877  1.00 62.59  ? 72   PHE   A CE1  1 
ATOM   1060  C  CE2  . PHE   A  1  72  ? 9.112   -14.411 -38.239  1.00 62.69  ? 72   PHE   A CE2  1 
ATOM   1061  C  CZ   . PHE   A  1  72  ? 10.243  -14.824 -38.914  1.00 62.22  ? 72   PHE   A CZ   1 
ATOM   1062  H  H    . PHE   A  1  72  ? 5.007   -14.593 -39.626  1.00 95.12  ? 72   PHE   A H    1 
ATOM   1063  H  HA   . PHE   A  1  72  ? 6.311   -15.719 -41.650  1.00 86.98  ? 72   PHE   A HA   1 
ATOM   1064  H  HB2  . PHE   A  1  72  ? 5.916   -16.552 -38.994  1.00 78.14  ? 72   PHE   A HB2  1 
ATOM   1065  H  HB3  . PHE   A  1  72  ? 6.613   -17.518 -40.045  1.00 78.14  ? 72   PHE   A HB3  1 
ATOM   1066  H  HD1  . PHE   A  1  72  ? 8.865   -17.041 -40.809  1.00 74.05  ? 72   PHE   A HD1  1 
ATOM   1067  H  HD2  . PHE   A  1  72  ? 7.132   -14.703 -38.068  1.00 73.82  ? 72   PHE   A HD2  1 
ATOM   1068  H  HE1  . PHE   A  1  72  ? 10.909  -16.087 -40.334  1.00 75.14  ? 72   PHE   A HE1  1 
ATOM   1069  H  HE2  . PHE   A  1  72  ? 9.174   -13.748 -37.590  1.00 75.27  ? 72   PHE   A HE2  1 
ATOM   1070  H  HZ   . PHE   A  1  72  ? 11.067  -14.440 -38.720  1.00 74.70  ? 72   PHE   A HZ   1 
ATOM   1071  N  N    . ASP   A  1  73  ? 3.476   -16.918 -40.754  1.00 66.70  ? 73   ASP   A N    1 
ATOM   1072  C  CA   . ASP   A  1  73  ? 2.394   -17.837 -41.087  1.00 62.56  ? 73   ASP   A CA   1 
ATOM   1073  C  C    . ASP   A  1  73  ? 1.096   -17.237 -40.574  1.00 64.19  ? 73   ASP   A C    1 
ATOM   1074  O  O    . ASP   A  1  73  ? 0.960   -16.993 -39.372  1.00 67.13  ? 73   ASP   A O    1 
ATOM   1075  C  CB   . ASP   A  1  73  ? 2.639   -19.216 -40.471  1.00 62.22  ? 73   ASP   A CB   1 
ATOM   1076  C  CG   . ASP   A  1  73  ? 1.363   -20.016 -40.304  1.00 66.25  ? 73   ASP   A CG   1 
ATOM   1077  O  OD1  . ASP   A  1  73  ? 0.539   -20.030 -41.242  1.00 69.47  ? 73   ASP   A OD1  1 
ATOM   1078  O  OD2  . ASP   A  1  73  ? 1.190   -20.640 -39.236  1.00 65.88  ? 73   ASP   A OD2  1 
ATOM   1079  H  H    . ASP   A  1  73  ? 3.309   -16.427 -40.068  1.00 80.08  ? 73   ASP   A H    1 
ATOM   1080  H  HA   . ASP   A  1  73  ? 2.331   -17.942 -42.049  1.00 75.11  ? 73   ASP   A HA   1 
ATOM   1081  H  HB2  . ASP   A  1  73  ? 3.235   -19.719 -41.048  1.00 74.70  ? 73   ASP   A HB2  1 
ATOM   1082  H  HB3  . ASP   A  1  73  ? 3.041   -19.105 -39.596  1.00 74.70  ? 73   ASP   A HB3  1 
ATOM   1083  N  N    . ALA   A  1  74  ? 0.152   -16.998 -41.481  1.00 66.21  ? 74   ALA   A N    1 
ATOM   1084  C  CA   . ALA   A  1  74  ? -1.112  -16.359 -41.143  1.00 67.59  ? 74   ALA   A CA   1 
ATOM   1085  C  C    . ALA   A  1  74  ? -2.247  -17.351 -40.928  1.00 66.94  ? 74   ALA   A C    1 
ATOM   1086  O  O    . ALA   A  1  74  ? -3.360  -16.931 -40.594  1.00 68.80  ? 74   ALA   A O    1 
ATOM   1087  C  CB   . ALA   A  1  74  ? -1.507  -15.369 -42.245  1.00 68.48  ? 74   ALA   A CB   1 
ATOM   1088  H  H    . ALA   A  1  74  ? 0.223   -17.202 -42.313  1.00 79.49  ? 74   ALA   A H    1 
ATOM   1089  H  HA   . ALA   A  1  74  ? -0.991  -15.865 -40.317  1.00 81.15  ? 74   ALA   A HA   1 
ATOM   1090  H  HB1  . ALA   A  1  74  ? -2.360  -14.968 -42.017  1.00 82.21  ? 74   ALA   A HB1  1 
ATOM   1091  H  HB2  . ALA   A  1  74  ? -0.825  -14.682 -42.311  1.00 82.21  ? 74   ALA   A HB2  1 
ATOM   1092  H  HB3  . ALA   A  1  74  ? -1.579  -15.845 -43.086  1.00 82.21  ? 74   ALA   A HB3  1 
ATOM   1093  N  N    . THR   A  1  75  ? -1.997  -18.645 -41.095  1.00 62.40  ? 75   THR   A N    1 
ATOM   1094  C  CA   . THR   A  1  75  ? -3.051  -19.647 -41.116  1.00 61.45  ? 75   THR   A CA   1 
ATOM   1095  C  C    . THR   A  1  75  ? -3.210  -20.320 -39.759  1.00 60.67  ? 75   THR   A C    1 
ATOM   1096  O  O    . THR   A  1  75  ? -2.337  -20.250 -38.889  1.00 62.15  ? 75   THR   A O    1 
ATOM   1097  C  CB   . THR   A  1  75  ? -2.763  -20.718 -42.172  1.00 61.81  ? 75   THR   A CB   1 
ATOM   1098  O  OG1  . THR   A  1  75  ? -1.733  -21.598 -41.699  1.00 61.17  ? 75   THR   A OG1  1 
ATOM   1099  C  CG2  . THR   A  1  75  ? -2.313  -20.083 -43.474  1.00 61.79  ? 75   THR   A CG2  1 
ATOM   1100  H  H    . THR   A  1  75  ? -1.208  -18.971 -41.201  1.00 74.92  ? 75   THR   A H    1 
ATOM   1101  H  HA   . THR   A  1  75  ? -3.885  -19.201 -41.333  1.00 73.77  ? 75   THR   A HA   1 
ATOM   1102  H  HB   . THR   A  1  75  ? -3.573  -21.224 -42.342  1.00 74.21  ? 75   THR   A HB   1 
ATOM   1103  H  HG1  . THR   A  1  75  ? -1.037  -21.161 -41.530  1.00 73.44  ? 75   THR   A HG1  1 
ATOM   1104  H  HG21 . THR   A  1  75  ? -2.165  -20.769 -44.144  1.00 74.19  ? 75   THR   A HG21 1 
ATOM   1105  H  HG22 . THR   A  1  75  ? -2.991  -19.469 -43.796  1.00 74.19  ? 75   THR   A HG22 1 
ATOM   1106  H  HG23 . THR   A  1  75  ? -1.486  -19.595 -43.336  1.00 74.19  ? 75   THR   A HG23 1 
ATOM   1107  N  N    . GLY   A  1  76  ? -4.347  -20.983 -39.596  1.00 58.00  ? 76   GLY   A N    1 
ATOM   1108  C  CA   . GLY   A  1  76  ? -4.610  -21.829 -38.451  1.00 57.42  ? 76   GLY   A CA   1 
ATOM   1109  C  C    . GLY   A  1  76  ? -4.124  -23.244 -38.673  1.00 56.24  ? 76   GLY   A C    1 
ATOM   1110  O  O    . GLY   A  1  76  ? -3.140  -23.486 -39.379  1.00 57.44  ? 76   GLY   A O    1 
ATOM   1111  H  H    . GLY   A  1  76  ? -5.000  -20.954 -40.155  1.00 69.63  ? 76   GLY   A H    1 
ATOM   1112  H  HA2  . GLY   A  1  76  ? -4.160  -21.468 -37.671  1.00 68.94  ? 76   GLY   A HA2  1 
ATOM   1113  H  HA3  . GLY   A  1  76  ? -5.565  -21.855 -38.281  1.00 68.94  ? 76   GLY   A HA3  1 
ATOM   1114  N  N    . ASN   A  1  77  ? -4.833  -24.197 -38.073  1.00 54.71  ? 77   ASN   A N    1 
ATOM   1115  C  CA   . ASN   A  1  77  ? -4.429  -25.595 -38.135  1.00 54.37  ? 77   ASN   A CA   1 
ATOM   1116  C  C    . ASN   A  1  77  ? -4.932  -26.248 -39.415  1.00 63.46  ? 77   ASN   A C    1 
ATOM   1117  O  O    . ASN   A  1  77  ? -6.121  -26.167 -39.741  1.00 68.13  ? 77   ASN   A O    1 
ATOM   1118  C  CB   . ASN   A  1  77  ? -4.966  -26.360 -36.926  1.00 50.90  ? 77   ASN   A CB   1 
ATOM   1119  C  CG   . ASN   A  1  77  ? -4.305  -25.945 -35.630  1.00 54.44  ? 77   ASN   A CG   1 
ATOM   1120  O  OD1  . ASN   A  1  77  ? -3.190  -25.426 -35.625  1.00 54.42  ? 77   ASN   A OD1  1 
ATOM   1121  N  ND2  . ASN   A  1  77  ? -4.990  -26.180 -34.518  1.00 57.45  ? 77   ASN   A ND2  1 
ATOM   1122  H  H    . ASN   A  1  77  ? -5.553  -24.058 -37.624  1.00 65.69  ? 77   ASN   A H    1 
ATOM   1123  H  HA   . ASN   A  1  77  ? -3.460  -25.636 -38.130  1.00 65.28  ? 77   ASN   A HA   1 
ATOM   1124  H  HB2  . ASN   A  1  77  ? -5.918  -26.194 -36.844  1.00 61.12  ? 77   ASN   A HB2  1 
ATOM   1125  H  HB3  . ASN   A  1  77  ? -4.804  -27.308 -37.055  1.00 61.12  ? 77   ASN   A HB3  1 
ATOM   1126  H  HD21 . ASN   A  1  77  ? -4.659  -25.962 -33.755  1.00 68.98  ? 77   ASN   A HD21 1 
ATOM   1127  H  HD22 . ASN   A  1  77  ? -5.766  -26.550 -34.561  1.00 68.98  ? 77   ASN   A HD22 1 
ATOM   1128  N  N    . ARG   A  1  78  ? -4.024  -26.899 -40.138  1.00 64.71  ? 78   ARG   A N    1 
ATOM   1129  C  CA   . ARG   A  1  78  ? -4.430  -27.760 -41.239  1.00 61.67  ? 78   ARG   A CA   1 
ATOM   1130  C  C    . ARG   A  1  78  ? -5.260  -28.924 -40.711  1.00 60.61  ? 78   ARG   A C    1 
ATOM   1131  O  O    . ARG   A  1  78  ? -5.139  -29.329 -39.552  1.00 60.88  ? 78   ARG   A O    1 
ATOM   1132  C  CB   . ARG   A  1  78  ? -3.205  -28.289 -41.984  1.00 59.26  ? 78   ARG   A CB   1 
ATOM   1133  C  CG   . ARG   A  1  78  ? -2.568  -27.283 -42.921  1.00 59.82  ? 78   ARG   A CG   1 
ATOM   1134  C  CD   . ARG   A  1  78  ? -1.283  -27.825 -43.514  1.00 56.85  ? 78   ARG   A CD   1 
ATOM   1135  N  NE   . ARG   A  1  78  ? -0.190  -27.814 -42.547  1.00 55.14  ? 78   ARG   A NE   1 
ATOM   1136  C  CZ   . ARG   A  1  78  ? 1.083   -28.030 -42.858  1.00 54.29  ? 78   ARG   A CZ   1 
ATOM   1137  N  NH1  . ARG   A  1  78  ? 1.430   -28.275 -44.115  1.00 53.17  ? 78   ARG   A NH1  1 
ATOM   1138  N  NH2  . ARG   A  1  78  ? 2.012   -27.998 -41.911  1.00 54.02  ? 78   ARG   A NH2  1 
ATOM   1139  H  H    . ARG   A  1  78  ? -3.174  -26.859 -40.011  1.00 77.69  ? 78   ARG   A H    1 
ATOM   1140  H  HA   . ARG   A  1  78  ? -4.966  -27.253 -41.868  1.00 74.04  ? 78   ARG   A HA   1 
ATOM   1141  H  HB2  . ARG   A  1  78  ? -2.536  -28.551 -41.333  1.00 71.15  ? 78   ARG   A HB2  1 
ATOM   1142  H  HB3  . ARG   A  1  78  ? -3.472  -29.056 -42.513  1.00 71.15  ? 78   ARG   A HB3  1 
ATOM   1143  H  HG2  . ARG   A  1  78  ? -3.180  -27.085 -43.646  1.00 71.83  ? 78   ARG   A HG2  1 
ATOM   1144  H  HG3  . ARG   A  1  78  ? -2.360  -26.472 -42.431  1.00 71.83  ? 78   ARG   A HG3  1 
ATOM   1145  H  HD2  . ARG   A  1  78  ? -1.425  -28.741 -43.802  1.00 68.26  ? 78   ARG   A HD2  1 
ATOM   1146  H  HD3  . ARG   A  1  78  ? -1.025  -27.276 -44.271  1.00 68.26  ? 78   ARG   A HD3  1 
ATOM   1147  H  HE   . ARG   A  1  78  ? -0.383  -27.657 -41.724  1.00 66.21  ? 78   ARG   A HE   1 
ATOM   1148  H  HH11 . ARG   A  1  78  ? 0.830   -28.293 -44.730  1.00 63.84  ? 78   ARG   A HH11 1 
ATOM   1149  H  HH12 . ARG   A  1  78  ? 2.255   -28.415 -44.313  1.00 63.84  ? 78   ARG   A HH12 1 
ATOM   1150  H  HH21 . ARG   A  1  78  ? 1.790   -27.836 -41.096  1.00 64.86  ? 78   ARG   A HH21 1 
ATOM   1151  H  HH22 . ARG   A  1  78  ? 2.836   -28.138 -42.113  1.00 64.86  ? 78   ARG   A HH22 1 
ATOM   1152  N  N    . ASP   A  1  79  ? -6.110  -29.466 -41.578  1.00 62.54  ? 79   ASP   A N    1 
ATOM   1153  C  CA   . ASP   A  1  79  ? -6.963  -30.598 -41.245  1.00 61.93  ? 79   ASP   A CA   1 
ATOM   1154  C  C    . ASP   A  1  79  ? -6.444  -31.853 -41.932  1.00 61.10  ? 79   ASP   A C    1 
ATOM   1155  O  O    . ASP   A  1  79  ? -6.121  -31.824 -43.124  1.00 63.13  ? 79   ASP   A O    1 
ATOM   1156  C  CB   . ASP   A  1  79  ? -8.412  -30.342 -41.671  1.00 61.37  ? 79   ASP   A CB   1 
ATOM   1157  C  CG   . ASP   A  1  79  ? -9.187  -29.521 -40.660  1.00 64.55  ? 79   ASP   A CG   1 
ATOM   1158  O  OD1  . ASP   A  1  79  ? -8.650  -29.243 -39.568  1.00 64.50  ? 79   ASP   A OD1  1 
ATOM   1159  O  OD2  . ASP   A  1  79  ? -10.343 -29.154 -40.960  1.00 69.86  ? 79   ASP   A OD2  1 
ATOM   1160  H  H    . ASP   A  1  79  ? -6.211  -29.187 -42.385  1.00 75.08  ? 79   ASP   A H    1 
ATOM   1161  H  HA   . ASP   A  1  79  ? -6.939  -30.737 -40.285  1.00 74.35  ? 79   ASP   A HA   1 
ATOM   1162  H  HB2  . ASP   A  1  79  ? -8.413  -29.860 -42.513  1.00 73.68  ? 79   ASP   A HB2  1 
ATOM   1163  H  HB3  . ASP   A  1  79  ? -8.865  -31.194 -41.776  1.00 73.68  ? 79   ASP   A HB3  1 
ATOM   1164  N  N    . TYR   A  1  80  ? -6.357  -32.948 -41.176  1.00 60.76  ? 80   TYR   A N    1 
ATOM   1165  C  CA   . TYR   A  1  80  ? -6.196  -34.258 -41.795  1.00 65.48  ? 80   TYR   A CA   1 
ATOM   1166  C  C    . TYR   A  1  80  ? -7.523  -34.767 -42.337  1.00 67.99  ? 80   TYR   A C    1 
ATOM   1167  O  O    . TYR   A  1  80  ? -7.553  -35.461 -43.360  1.00 69.00  ? 80   TYR   A O    1 
ATOM   1168  C  CB   . TYR   A  1  80  ? -5.626  -35.258 -40.789  1.00 66.68  ? 80   TYR   A CB   1 
ATOM   1169  C  CG   . TYR   A  1  80  ? -5.633  -36.683 -41.294  1.00 65.99  ? 80   TYR   A CG   1 
ATOM   1170  C  CD1  . TYR   A  1  80  ? -4.579  -37.177 -42.050  1.00 64.34  ? 80   TYR   A CD1  1 
ATOM   1171  C  CD2  . TYR   A  1  80  ? -6.698  -37.533 -41.021  1.00 67.49  ? 80   TYR   A CD2  1 
ATOM   1172  C  CE1  . TYR   A  1  80  ? -4.583  -38.477 -42.518  1.00 64.84  ? 80   TYR   A CE1  1 
ATOM   1173  C  CE2  . TYR   A  1  80  ? -6.712  -38.833 -41.484  1.00 67.60  ? 80   TYR   A CE2  1 
ATOM   1174  C  CZ   . TYR   A  1  80  ? -5.652  -39.301 -42.232  1.00 66.92  ? 80   TYR   A CZ   1 
ATOM   1175  O  OH   . TYR   A  1  80  ? -5.661  -40.596 -42.695  1.00 70.39  ? 80   TYR   A OH   1 
ATOM   1176  H  H    . TYR   A  1  80  ? -6.388  -32.957 -40.316  1.00 72.94  ? 80   TYR   A H    1 
ATOM   1177  H  HA   . TYR   A  1  80  ? -5.562  -34.189 -42.526  1.00 78.61  ? 80   TYR   A HA   1 
ATOM   1178  H  HB2  . TYR   A  1  80  ? -4.708  -35.016 -40.592  1.00 80.06  ? 80   TYR   A HB2  1 
ATOM   1179  H  HB3  . TYR   A  1  80  ? -6.159  -35.226 -39.979  1.00 80.06  ? 80   TYR   A HB3  1 
ATOM   1180  H  HD1  . TYR   A  1  80  ? -3.858  -36.623 -42.245  1.00 77.24  ? 80   TYR   A HD1  1 
ATOM   1181  H  HD2  . TYR   A  1  80  ? -7.415  -37.220 -40.517  1.00 81.03  ? 80   TYR   A HD2  1 
ATOM   1182  H  HE1  . TYR   A  1  80  ? -3.870  -38.794 -43.023  1.00 77.84  ? 80   TYR   A HE1  1 
ATOM   1183  H  HE2  . TYR   A  1  80  ? -7.432  -39.391 -41.293  1.00 81.16  ? 80   TYR   A HE2  1 
ATOM   1184  H  HH   . TYR   A  1  80  ? -4.984  -40.735 -43.173  1.00 84.50  ? 80   TYR   A HH   1 
ATOM   1185  N  N    . ALA   A  1  81  ? -8.615  -34.431 -41.658  1.00 67.92  ? 81   ALA   A N    1 
ATOM   1186  C  CA   . ALA   A  1  81  ? -9.970  -34.746 -42.086  1.00 70.89  ? 81   ALA   A CA   1 
ATOM   1187  C  C    . ALA   A  1  81  ? -10.889 -33.769 -41.366  1.00 72.79  ? 81   ALA   A C    1 
ATOM   1188  O  O    . ALA   A  1  81  ? -10.451 -33.010 -40.497  1.00 74.62  ? 81   ALA   A O    1 
ATOM   1189  C  CB   . ALA   A  1  81  ? -10.335 -36.201 -41.779  1.00 74.84  ? 81   ALA   A CB   1 
ATOM   1190  H  H    . ALA   A  1  81  ? -8.596  -34.001 -40.914  1.00 81.54  ? 81   ALA   A H    1 
ATOM   1191  H  HA   . ALA   A  1  81  ? -10.064 -34.628 -43.044  1.00 85.11  ? 81   ALA   A HA   1 
ATOM   1192  H  HB1  . ALA   A  1  81  ? -11.243 -36.369 -42.078  1.00 89.84  ? 81   ALA   A HB1  1 
ATOM   1193  H  HB2  . ALA   A  1  81  ? -9.719  -36.786 -42.247  1.00 89.84  ? 81   ALA   A HB2  1 
ATOM   1194  H  HB3  . ALA   A  1  81  ? -10.269 -36.348 -40.823  1.00 89.84  ? 81   ALA   A HB3  1 
ATOM   1195  N  N    . LYS   A  1  82  ? -12.167 -33.782 -41.734  1.00 75.54  ? 82   LYS   A N    1 
ATOM   1196  C  CA   . LYS   A  1  82  ? -13.109 -32.876 -41.090  1.00 80.36  ? 82   LYS   A CA   1 
ATOM   1197  C  C    . LYS   A  1  82  ? -13.133 -33.148 -39.591  1.00 79.95  ? 82   LYS   A C    1 
ATOM   1198  O  O    . LYS   A  1  82  ? -13.303 -34.291 -39.158  1.00 81.07  ? 82   LYS   A O    1 
ATOM   1199  C  CB   . LYS   A  1  82  ? -14.509 -33.034 -41.679  1.00 89.23  ? 82   LYS   A CB   1 
ATOM   1200  C  CG   . LYS   A  1  82  ? -15.373 -31.783 -41.536  1.00 94.36  ? 82   LYS   A CG   1 
ATOM   1201  C  CD   . LYS   A  1  82  ? -16.852 -32.086 -41.733  1.00 100.70 ? 82   LYS   A CD   1 
ATOM   1202  C  CE   . LYS   A  1  82  ? -17.651 -30.829 -42.052  1.00 104.77 ? 82   LYS   A CE   1 
ATOM   1203  N  NZ   . LYS   A  1  82  ? -17.341 -30.295 -43.409  1.00 107.36 ? 82   LYS   A NZ   1 
ATOM   1204  H  H    . LYS   A  1  82  ? -12.504 -34.293 -42.338  1.00 90.68  ? 82   LYS   A H    1 
ATOM   1205  H  HA   . LYS   A  1  82  ? -12.831 -31.960 -41.245  1.00 96.47  ? 82   LYS   A HA   1 
ATOM   1206  H  HB2  . LYS   A  1  82  ? -14.430 -33.234 -42.625  1.00 107.11 ? 82   LYS   A HB2  1 
ATOM   1207  H  HB3  . LYS   A  1  82  ? -14.961 -33.761 -41.223  1.00 107.11 ? 82   LYS   A HB3  1 
ATOM   1208  H  HG2  . LYS   A  1  82  ? -15.255 -31.413 -40.647  1.00 113.27 ? 82   LYS   A HG2  1 
ATOM   1209  H  HG3  . LYS   A  1  82  ? -15.106 -31.132 -42.204  1.00 113.27 ? 82   LYS   A HG3  1 
ATOM   1210  H  HD2  . LYS   A  1  82  ? -16.955 -32.707 -42.471  1.00 120.88 ? 82   LYS   A HD2  1 
ATOM   1211  H  HD3  . LYS   A  1  82  ? -17.209 -32.475 -40.919  1.00 120.88 ? 82   LYS   A HD3  1 
ATOM   1212  H  HE2  . LYS   A  1  82  ? -18.598 -31.036 -42.018  1.00 125.77 ? 82   LYS   A HE2  1 
ATOM   1213  H  HE3  . LYS   A  1  82  ? -17.439 -30.142 -41.401  1.00 125.77 ? 82   LYS   A HE3  1 
ATOM   1214  H  HZ1  . LYS   A  1  82  ? -17.963 -29.708 -43.654  1.00 128.87 ? 82   LYS   A HZ1  1 
ATOM   1215  H  HZ2  . LYS   A  1  82  ? -16.548 -29.891 -43.403  1.00 128.87 ? 82   LYS   A HZ2  1 
ATOM   1216  H  HZ3  . LYS   A  1  82  ? -17.321 -30.960 -44.000  1.00 128.87 ? 82   LYS   A HZ3  1 
ATOM   1217  N  N    . ASP   A  1  83  ? -12.949 -32.092 -38.798  1.00 83.00  ? 83   ASP   A N    1 
ATOM   1218  C  CA   . ASP   A  1  83  ? -12.909 -32.209 -37.341  1.00 86.38  ? 83   ASP   A CA   1 
ATOM   1219  C  C    . ASP   A  1  83  ? -11.777 -33.126 -36.888  1.00 86.39  ? 83   ASP   A C    1 
ATOM   1220  O  O    . ASP   A  1  83  ? -11.868 -33.778 -35.844  1.00 86.12  ? 83   ASP   A O    1 
ATOM   1221  C  CB   . ASP   A  1  83  ? -14.251 -32.705 -36.795  1.00 89.84  ? 83   ASP   A CB   1 
ATOM   1222  C  CG   . ASP   A  1  83  ? -15.401 -31.784 -37.153  1.00 102.43 ? 83   ASP   A CG   1 
ATOM   1223  O  OD1  . ASP   A  1  83  ? -15.339 -30.587 -36.801  1.00 106.74 ? 83   ASP   A OD1  1 
ATOM   1224  O  OD2  . ASP   A  1  83  ? -16.361 -32.254 -37.799  1.00 107.48 ? 83   ASP   A OD2  1 
ATOM   1225  H  H    . ASP   A  1  83  ? -12.842 -31.288 -39.084  1.00 99.64  ? 83   ASP   A H    1 
ATOM   1226  H  HA   . ASP   A  1  83  ? -12.740 -31.331 -36.966  1.00 103.70 ? 83   ASP   A HA   1 
ATOM   1227  H  HB2  . ASP   A  1  83  ? -14.440 -33.581 -37.167  1.00 107.85 ? 83   ASP   A HB2  1 
ATOM   1228  H  HB3  . ASP   A  1  83  ? -14.199 -32.760 -35.828  1.00 107.85 ? 83   ASP   A HB3  1 
ATOM   1229  N  N    . ASP   A  1  84  ? -10.702 -33.182 -37.672  1.00 80.66  ? 84   ASP   A N    1 
ATOM   1230  C  CA   . ASP   A  1  84  ? -9.536  -34.012 -37.367  1.00 70.47  ? 84   ASP   A CA   1 
ATOM   1231  C  C    . ASP   A  1  84  ? -8.294  -33.220 -37.748  1.00 65.74  ? 84   ASP   A C    1 
ATOM   1232  O  O    . ASP   A  1  84  ? -7.724  -33.404 -38.830  1.00 64.30  ? 84   ASP   A O    1 
ATOM   1233  C  CB   . ASP   A  1  84  ? -9.599  -35.346 -38.114  1.00 70.23  ? 84   ASP   A CB   1 
ATOM   1234  C  CG   . ASP   A  1  84  ? -8.702  -36.403 -37.500  1.00 68.39  ? 84   ASP   A CG   1 
ATOM   1235  O  OD1  . ASP   A  1  84  ? -7.714  -36.033 -36.832  1.00 63.95  ? 84   ASP   A OD1  1 
ATOM   1236  O  OD2  . ASP   A  1  84  ? -8.986  -37.605 -37.686  1.00 66.83  ? 84   ASP   A OD2  1 
ATOM   1237  H  H    . ASP   A  1  84  ? -10.622 -32.738 -38.404  1.00 96.83  ? 84   ASP   A H    1 
ATOM   1238  H  HA   . ASP   A  1  84  ? -9.505  -34.205 -36.417  1.00 84.60  ? 84   ASP   A HA   1 
ATOM   1239  H  HB2  . ASP   A  1  84  ? -10.510 -35.677 -38.094  1.00 84.32  ? 84   ASP   A HB2  1 
ATOM   1240  H  HB3  . ASP   A  1  84  ? -9.316  -35.208 -39.032  1.00 84.32  ? 84   ASP   A HB3  1 
ATOM   1241  N  N    . PRO   A  1  85  ? -7.845  -32.317 -36.877  1.00 60.83  ? 85   PRO   A N    1 
ATOM   1242  C  CA   . PRO   A  1  85  ? -6.726  -31.443 -37.245  1.00 58.80  ? 85   PRO   A CA   1 
ATOM   1243  C  C    . PRO   A  1  85  ? -5.437  -32.220 -37.453  1.00 54.58  ? 85   PRO   A C    1 
ATOM   1244  O  O    . PRO   A  1  85  ? -5.159  -33.209 -36.769  1.00 52.33  ? 85   PRO   A O    1 
ATOM   1245  C  CB   . PRO   A  1  85  ? -6.606  -30.487 -36.050  1.00 59.60  ? 85   PRO   A CB   1 
ATOM   1246  C  CG   . PRO   A  1  85  ? -7.895  -30.609 -35.310  1.00 59.53  ? 85   PRO   A CG   1 
ATOM   1247  C  CD   . PRO   A  1  85  ? -8.353  -32.014 -35.529  1.00 58.58  ? 85   PRO   A CD   1 
ATOM   1248  H  HA   . PRO   A  1  85  ? -6.940  -30.948 -38.051  1.00 70.60  ? 85   PRO   A HA   1 
ATOM   1249  H  HB2  . PRO   A  1  85  ? -5.860  -30.753 -35.491  1.00 71.56  ? 85   PRO   A HB2  1 
ATOM   1250  H  HB3  . PRO   A  1  85  ? -6.475  -29.580 -36.369  1.00 71.56  ? 85   PRO   A HB3  1 
ATOM   1251  H  HG2  . PRO   A  1  85  ? -7.749  -30.437 -34.367  1.00 71.47  ? 85   PRO   A HG2  1 
ATOM   1252  H  HG3  . PRO   A  1  85  ? -8.539  -29.977 -35.667  1.00 71.47  ? 85   PRO   A HG3  1 
ATOM   1253  H  HD2  . PRO   A  1  85  ? -7.966  -32.612 -34.870  1.00 70.34  ? 85   PRO   A HD2  1 
ATOM   1254  H  HD3  . PRO   A  1  85  ? -9.321  -32.072 -35.502  1.00 70.34  ? 85   PRO   A HD3  1 
ATOM   1255  N  N    . LEU   A  1  86  ? -4.645  -31.751 -38.414  1.00 54.16  ? 86   LEU   A N    1 
ATOM   1256  C  CA   . LEU   A  1  86  ? -3.333  -32.331 -38.660  1.00 53.15  ? 86   LEU   A CA   1 
ATOM   1257  C  C    . LEU   A  1  86  ? -2.301  -31.831 -37.660  1.00 52.01  ? 86   LEU   A C    1 
ATOM   1258  O  O    . LEU   A  1  86  ? -1.358  -32.558 -37.329  1.00 51.22  ? 86   LEU   A O    1 
ATOM   1259  C  CB   . LEU   A  1  86  ? -2.883  -32.001 -40.084  1.00 55.31  ? 86   LEU   A CB   1 
ATOM   1260  C  CG   . LEU   A  1  86  ? -1.536  -32.554 -40.547  1.00 55.30  ? 86   LEU   A CG   1 
ATOM   1261  C  CD1  . LEU   A  1  86  ? -1.586  -34.068 -40.660  1.00 56.02  ? 86   LEU   A CD1  1 
ATOM   1262  C  CD2  . LEU   A  1  86  ? -1.150  -31.922 -41.873  1.00 56.65  ? 86   LEU   A CD2  1 
ATOM   1263  H  H    . LEU   A  1  86  ? -4.845  -31.097 -38.937  1.00 65.03  ? 86   LEU   A H    1 
ATOM   1264  H  HA   . LEU   A  1  86  ? -3.390  -33.296 -38.577  1.00 63.81  ? 86   LEU   A HA   1 
ATOM   1265  H  HB2  . LEU   A  1  86  ? -3.552  -32.348 -40.694  1.00 66.41  ? 86   LEU   A HB2  1 
ATOM   1266  H  HB3  . LEU   A  1  86  ? -2.831  -31.036 -40.161  1.00 66.41  ? 86   LEU   A HB3  1 
ATOM   1267  H  HG   . LEU   A  1  86  ? -0.853  -32.336 -39.893  1.00 66.40  ? 86   LEU   A HG   1 
ATOM   1268  H  HD11 . LEU   A  1  86  ? -0.725  -34.391 -40.967  1.00 67.26  ? 86   LEU   A HD11 1 
ATOM   1269  H  HD12 . LEU   A  1  86  ? -1.788  -34.443 -39.788  1.00 67.26  ? 86   LEU   A HD12 1 
ATOM   1270  H  HD13 . LEU   A  1  86  ? -2.277  -34.315 -41.294  1.00 67.26  ? 86   LEU   A HD13 1 
ATOM   1271  H  HD21 . LEU   A  1  86  ? -0.300  -32.289 -42.163  1.00 68.02  ? 86   LEU   A HD21 1 
ATOM   1272  H  HD22 . LEU   A  1  86  ? -1.837  -32.120 -42.529  1.00 68.02  ? 86   LEU   A HD22 1 
ATOM   1273  H  HD23 . LEU   A  1  86  ? -1.072  -30.962 -41.755  1.00 68.02  ? 86   LEU   A HD23 1 
ATOM   1274  N  N    . GLU   A  1  87  ? -2.473  -30.607 -37.165  1.00 53.42  ? 87   GLU   A N    1 
ATOM   1275  C  CA   . GLU   A  1  87  ? -1.491  -29.952 -36.315  1.00 51.41  ? 87   GLU   A CA   1 
ATOM   1276  C  C    . GLU   A  1  87  ? -2.219  -29.147 -35.248  1.00 52.63  ? 87   GLU   A C    1 
ATOM   1277  O  O    . GLU   A  1  87  ? -3.436  -28.958 -35.305  1.00 55.47  ? 87   GLU   A O    1 
ATOM   1278  C  CB   . GLU   A  1  87  ? -0.565  -29.055 -37.146  1.00 51.98  ? 87   GLU   A CB   1 
ATOM   1279  C  CG   . GLU   A  1  87  ? -1.307  -28.118 -38.090  1.00 55.22  ? 87   GLU   A CG   1 
ATOM   1280  C  CD   . GLU   A  1  87  ? -0.401  -27.497 -39.133  1.00 55.67  ? 87   GLU   A CD   1 
ATOM   1281  O  OE1  . GLU   A  1  87  ? 0.771   -27.916 -39.234  1.00 54.54  ? 87   GLU   A OE1  1 
ATOM   1282  O  OE2  . GLU   A  1  87  ? -0.864  -26.590 -39.858  1.00 58.20  ? 87   GLU   A OE2  1 
ATOM   1283  H  H    . GLU   A  1  87  ? -3.170  -30.126 -37.312  1.00 64.14  ? 87   GLU   A H    1 
ATOM   1284  H  HA   . GLU   A  1  87  ? -0.948  -30.617 -35.864  1.00 61.72  ? 87   GLU   A HA   1 
ATOM   1285  H  HB2  . GLU   A  1  87  ? -0.035  -28.511 -36.544  1.00 62.41  ? 87   GLU   A HB2  1 
ATOM   1286  H  HB3  . GLU   A  1  87  ? 0.015   -29.618 -37.683  1.00 62.41  ? 87   GLU   A HB3  1 
ATOM   1287  H  HG2  . GLU   A  1  87  ? -1.998  -28.618 -38.552  1.00 66.30  ? 87   GLU   A HG2  1 
ATOM   1288  H  HG3  . GLU   A  1  87  ? -1.706  -27.401 -37.573  1.00 66.30  ? 87   GLU   A HG3  1 
ATOM   1289  N  N    . PHE   A  1  88  ? -1.458  -28.671 -34.262  1.00 53.85  ? 88   PHE   A N    1 
ATOM   1290  C  CA   . PHE   A  1  88  ? -2.014  -27.904 -33.145  1.00 53.56  ? 88   PHE   A CA   1 
ATOM   1291  C  C    . PHE   A  1  88  ? -1.074  -26.737 -32.862  1.00 54.19  ? 88   PHE   A C    1 
ATOM   1292  O  O    . PHE   A  1  88  ? -0.027  -26.914 -32.229  1.00 52.03  ? 88   PHE   A O    1 
ATOM   1293  C  CB   . PHE   A  1  88  ? -2.197  -28.780 -31.913  1.00 50.60  ? 88   PHE   A CB   1 
ATOM   1294  C  CG   . PHE   A  1  88  ? -2.960  -30.043 -32.179  1.00 48.25  ? 88   PHE   A CG   1 
ATOM   1295  C  CD1  . PHE   A  1  88  ? -2.297  -31.203 -32.540  1.00 49.35  ? 88   PHE   A CD1  1 
ATOM   1296  C  CD2  . PHE   A  1  88  ? -4.340  -30.069 -32.073  1.00 47.90  ? 88   PHE   A CD2  1 
ATOM   1297  C  CE1  . PHE   A  1  88  ? -2.995  -32.368 -32.787  1.00 49.85  ? 88   PHE   A CE1  1 
ATOM   1298  C  CE2  . PHE   A  1  88  ? -5.044  -31.231 -32.319  1.00 47.26  ? 88   PHE   A CE2  1 
ATOM   1299  C  CZ   . PHE   A  1  88  ? -4.371  -32.382 -32.677  1.00 47.39  ? 88   PHE   A CZ   1 
ATOM   1300  H  H    . PHE   A  1  88  ? -0.606  -28.781 -34.216  1.00 64.66  ? 88   PHE   A H    1 
ATOM   1301  H  HA   . PHE   A  1  88  ? -2.878  -27.545 -33.402  1.00 64.30  ? 88   PHE   A HA   1 
ATOM   1302  H  HB2  . PHE   A  1  88  ? -1.322  -29.028 -31.574  1.00 60.76  ? 88   PHE   A HB2  1 
ATOM   1303  H  HB3  . PHE   A  1  88  ? -2.682  -28.276 -31.241  1.00 60.76  ? 88   PHE   A HB3  1 
ATOM   1304  H  HD1  . PHE   A  1  88  ? -1.370  -31.197 -32.617  1.00 59.26  ? 88   PHE   A HD1  1 
ATOM   1305  H  HD2  . PHE   A  1  88  ? -4.797  -29.296 -31.834  1.00 57.51  ? 88   PHE   A HD2  1 
ATOM   1306  H  HE1  . PHE   A  1  88  ? -2.539  -33.142 -33.027  1.00 59.85  ? 88   PHE   A HE1  1 
ATOM   1307  H  HE2  . PHE   A  1  88  ? -5.971  -31.238 -32.245  1.00 56.74  ? 88   PHE   A HE2  1 
ATOM   1308  H  HZ   . PHE   A  1  88  ? -4.843  -33.166 -32.843  1.00 56.91  ? 88   PHE   A HZ   1 
ATOM   1309  N  N    . LYS   A  1  89  ? -1.459  -25.546 -33.318  1.00 52.33  ? 89   LYS   A N    1 
ATOM   1310  C  CA   . LYS   A  1  89  ? -0.605  -24.372 -33.211  1.00 50.27  ? 89   LYS   A CA   1 
ATOM   1311  C  C    . LYS   A  1  89  ? -0.861  -23.548 -31.957  1.00 52.93  ? 89   LYS   A C    1 
ATOM   1312  O  O    . LYS   A  1  89  ? -0.030  -22.699 -31.615  1.00 52.28  ? 89   LYS   A O    1 
ATOM   1313  C  CB   . LYS   A  1  89  ? -0.791  -23.479 -34.440  1.00 49.66  ? 89   LYS   A CB   1 
ATOM   1314  C  CG   . LYS   A  1  89  ? -0.370  -24.133 -35.745  1.00 50.01  ? 89   LYS   A CG   1 
ATOM   1315  C  CD   . LYS   A  1  89  ? -0.606  -23.208 -36.926  1.00 54.22  ? 89   LYS   A CD   1 
ATOM   1316  C  CE   . LYS   A  1  89  ? -0.316  -23.903 -38.245  1.00 54.51  ? 89   LYS   A CE   1 
ATOM   1317  N  NZ   . LYS   A  1  89  ? -0.574  -23.014 -39.412  1.00 55.24  ? 89   LYS   A NZ   1 
ATOM   1318  H  H    . LYS   A  1  89  ? -2.216  -25.394 -33.696  1.00 62.84  ? 89   LYS   A H    1 
ATOM   1319  H  HA   . LYS   A  1  89  ? 0.318   -24.667 -33.183  1.00 60.36  ? 89   LYS   A HA   1 
ATOM   1320  H  HB2  . LYS   A  1  89  ? -1.729  -23.244 -34.517  1.00 59.62  ? 89   LYS   A HB2  1 
ATOM   1321  H  HB3  . LYS   A  1  89  ? -0.256  -22.677 -34.326  1.00 59.62  ? 89   LYS   A HB3  1 
ATOM   1322  H  HG2  . LYS   A  1  89  ? 0.575   -24.347 -35.708  1.00 60.04  ? 89   LYS   A HG2  1 
ATOM   1323  H  HG3  . LYS   A  1  89  ? -0.888  -24.942 -35.881  1.00 60.04  ? 89   LYS   A HG3  1 
ATOM   1324  H  HD2  . LYS   A  1  89  ? -1.532  -22.922 -36.929  1.00 65.11  ? 89   LYS   A HD2  1 
ATOM   1325  H  HD3  . LYS   A  1  89  ? -0.020  -22.438 -36.853  1.00 65.11  ? 89   LYS   A HD3  1 
ATOM   1326  H  HE2  . LYS   A  1  89  ? 0.616   -24.171 -38.268  1.00 65.44  ? 89   LYS   A HE2  1 
ATOM   1327  H  HE3  . LYS   A  1  89  ? -0.887  -24.683 -38.327  1.00 65.44  ? 89   LYS   A HE3  1 
ATOM   1328  H  HZ1  . LYS   A  1  89  ? -0.252  -23.386 -40.154  1.00 66.33  ? 89   LYS   A HZ1  1 
ATOM   1329  H  HZ2  . LYS   A  1  89  ? -1.449  -22.886 -39.510  1.00 66.33  ? 89   LYS   A HZ2  1 
ATOM   1330  H  HZ3  . LYS   A  1  89  ? -0.178  -22.227 -39.288  1.00 66.33  ? 89   LYS   A HZ3  1 
ATOM   1331  N  N    . SER   A  1  90  ? -1.978  -23.763 -31.268  1.00 55.08  ? 90   SER   A N    1 
ATOM   1332  C  CA   . SER   A  1  90  ? -2.247  -23.011 -30.050  1.00 54.68  ? 90   SER   A CA   1 
ATOM   1333  C  C    . SER   A  1  90  ? -1.195  -23.327 -28.995  1.00 51.71  ? 90   SER   A C    1 
ATOM   1334  O  O    . SER   A  1  90  ? -0.844  -24.490 -28.777  1.00 49.83  ? 90   SER   A O    1 
ATOM   1335  C  CB   . SER   A  1  90  ? -3.644  -23.336 -29.522  1.00 55.27  ? 90   SER   A CB   1 
ATOM   1336  O  OG   . SER   A  1  90  ? -4.643  -22.929 -30.440  1.00 57.32  ? 90   SER   A OG   1 
ATOM   1337  H  H    . SER   A  1  90  ? -2.587  -24.331 -31.483  1.00 66.14  ? 90   SER   A H    1 
ATOM   1338  H  HA   . SER   A  1  90  ? -2.215  -22.061 -30.245  1.00 65.65  ? 90   SER   A HA   1 
ATOM   1339  H  HB2  . SER   A  1  90  ? -3.713  -24.294 -29.385  1.00 66.36  ? 90   SER   A HB2  1 
ATOM   1340  H  HB3  . SER   A  1  90  ? -3.779  -22.870 -28.682  1.00 66.36  ? 90   SER   A HB3  1 
ATOM   1341  H  HG   . SER   A  1  90  ? -5.404  -23.116 -30.137  1.00 68.82  ? 90   SER   A HG   1 
ATOM   1342  N  N    . HIS   A  1  91  ? -0.685  -22.281 -28.344  1.00 53.01  ? 91   HIS   A N    1 
ATOM   1343  C  CA   . HIS   A  1  91  ? 0.324   -22.424 -27.296  1.00 52.81  ? 91   HIS   A CA   1 
ATOM   1344  C  C    . HIS   A  1  91  ? 1.582   -23.110 -27.815  1.00 52.31  ? 91   HIS   A C    1 
ATOM   1345  O  O    . HIS   A  1  91  ? 2.315   -23.747 -27.056  1.00 53.92  ? 91   HIS   A O    1 
ATOM   1346  C  CB   . HIS   A  1  91  ? -0.236  -23.191 -26.096  1.00 49.43  ? 91   HIS   A CB   1 
ATOM   1347  C  CG   . HIS   A  1  91  ? -1.519  -22.632 -25.572  1.00 51.57  ? 91   HIS   A CG   1 
ATOM   1348  N  ND1  . HIS   A  1  91  ? -1.566  -21.557 -24.710  1.00 54.90  ? 91   HIS   A ND1  1 
ATOM   1349  C  CD2  . HIS   A  1  91  ? -2.805  -22.995 -25.790  1.00 52.31  ? 91   HIS   A CD2  1 
ATOM   1350  C  CE1  . HIS   A  1  91  ? -2.825  -21.283 -24.419  1.00 55.13  ? 91   HIS   A CE1  1 
ATOM   1351  N  NE2  . HIS   A  1  91  ? -3.597  -22.141 -25.061  1.00 53.80  ? 91   HIS   A NE2  1 
ATOM   1352  H  H    . HIS   A  1  91  ? -0.912  -21.465 -28.495  1.00 63.65  ? 91   HIS   A H    1 
ATOM   1353  H  HA   . HIS   A  1  91  ? 0.577   -21.537 -26.998  1.00 63.41  ? 91   HIS   A HA   1 
ATOM   1354  H  HB2  . HIS   A  1  91  ? -0.399  -24.110 -26.362  1.00 59.35  ? 91   HIS   A HB2  1 
ATOM   1355  H  HB3  . HIS   A  1  91  ? 0.415   -23.164 -25.378  1.00 59.35  ? 91   HIS   A HB3  1 
ATOM   1356  H  HD2  . HIS   A  1  91  ? -3.098  -23.692 -26.332  1.00 62.81  ? 91   HIS   A HD2  1 
ATOM   1357  H  HE1  . HIS   A  1  91  ? -3.118  -20.602 -23.858  1.00 66.19  ? 91   HIS   A HE1  1 
ATOM   1358  H  HE2  . HIS   A  1  91  ? -4.456  -22.162 -25.028  1.00 64.60  ? 91   HIS   A HE2  1 
ATOM   1359  N  N    . GLN   A  1  92  ? 1.841   -22.989 -29.117  1.00 50.77  ? 92   GLN   A N    1 
ATOM   1360  C  CA   . GLN   A  1  92  ? 3.029   -23.592 -29.702  1.00 50.01  ? 92   GLN   A CA   1 
ATOM   1361  C  C    . GLN   A  1  92  ? 4.303   -22.839 -29.351  1.00 48.52  ? 92   GLN   A C    1 
ATOM   1362  O  O    . GLN   A  1  92  ? 5.395   -23.336 -29.647  1.00 43.38  ? 92   GLN   A O    1 
ATOM   1363  C  CB   . GLN   A  1  92  ? 2.885   -23.657 -31.219  1.00 49.46  ? 92   GLN   A CB   1 
ATOM   1364  C  CG   . GLN   A  1  92  ? 2.846   -22.291 -31.871  1.00 49.19  ? 92   GLN   A CG   1 
ATOM   1365  C  CD   . GLN   A  1  92  ? 2.606   -22.367 -33.360  1.00 46.57  ? 92   GLN   A CD   1 
ATOM   1366  O  OE1  . GLN   A  1  92  ? 2.762   -23.423 -33.974  1.00 43.23  ? 92   GLN   A OE1  1 
ATOM   1367  N  NE2  . GLN   A  1  92  ? 2.221   -21.245 -33.951  1.00 48.89  ? 92   GLN   A NE2  1 
ATOM   1368  H  H    . GLN   A  1  92  ? 1.346   -22.564 -29.677  1.00 60.97  ? 92   GLN   A H    1 
ATOM   1369  H  HA   . GLN   A  1  92  ? 3.112   -24.498 -29.364  1.00 60.04  ? 92   GLN   A HA   1 
ATOM   1370  H  HB2  . GLN   A  1  92  ? 3.641   -24.142 -31.586  1.00 59.39  ? 92   GLN   A HB2  1 
ATOM   1371  H  HB3  . GLN   A  1  92  ? 2.059   -24.116 -31.437  1.00 59.39  ? 92   GLN   A HB3  1 
ATOM   1372  H  HG2  . GLN   A  1  92  ? 2.128   -21.772 -31.477  1.00 59.07  ? 92   GLN   A HG2  1 
ATOM   1373  H  HG3  . GLN   A  1  92  ? 3.696   -21.846 -31.726  1.00 59.07  ? 92   GLN   A HG3  1 
ATOM   1374  H  HE21 . GLN   A  1  92  ? 2.121   -20.527 -33.488  1.00 58.70  ? 92   GLN   A HE21 1 
ATOM   1375  H  HE22 . GLN   A  1  92  ? 2.071   -21.234 -34.798  1.00 58.70  ? 92   GLN   A HE22 1 
ATOM   1376  N  N    . TRP   A  1  93  ? 4.193   -21.655 -28.749  1.00 49.68  ? 93   TRP   A N    1 
ATOM   1377  C  CA   . TRP   A  1  93  ? 5.358   -20.870 -28.346  1.00 45.82  ? 93   TRP   A CA   1 
ATOM   1378  C  C    . TRP   A  1  93  ? 6.193   -20.455 -29.558  1.00 45.66  ? 93   TRP   A C    1 
ATOM   1379  O  O    . TRP   A  1  93  ? 7.419   -20.586 -29.567  1.00 47.94  ? 93   TRP   A O    1 
ATOM   1380  C  CB   . TRP   A  1  93  ? 6.218   -21.647 -27.344  1.00 45.41  ? 93   TRP   A CB   1 
ATOM   1381  C  CG   . TRP   A  1  93  ? 5.765   -21.562 -25.923  1.00 45.24  ? 93   TRP   A CG   1 
ATOM   1382  C  CD1  . TRP   A  1  93  ? 4.616   -22.071 -25.393  1.00 45.12  ? 93   TRP   A CD1  1 
ATOM   1383  C  CD2  . TRP   A  1  93  ? 6.472   -20.950 -24.838  1.00 44.83  ? 93   TRP   A CD2  1 
ATOM   1384  N  NE1  . TRP   A  1  93  ? 4.559   -21.805 -24.046  1.00 47.37  ? 93   TRP   A NE1  1 
ATOM   1385  C  CE2  . TRP   A  1  93  ? 5.687   -21.118 -23.681  1.00 46.26  ? 93   TRP   A CE2  1 
ATOM   1386  C  CE3  . TRP   A  1  93  ? 7.691   -20.272 -24.734  1.00 43.58  ? 93   TRP   A CE3  1 
ATOM   1387  C  CZ2  . TRP   A  1  93  ? 6.080   -20.632 -22.436  1.00 48.68  ? 93   TRP   A CZ2  1 
ATOM   1388  C  CZ3  . TRP   A  1  93  ? 8.079   -19.789 -23.498  1.00 46.40  ? 93   TRP   A CZ3  1 
ATOM   1389  C  CH2  . TRP   A  1  93  ? 7.276   -19.971 -22.365  1.00 49.46  ? 93   TRP   A CH2  1 
ATOM   1390  H  H    . TRP   A  1  93  ? 3.443   -21.279 -28.561  1.00 59.65  ? 93   TRP   A H    1 
ATOM   1391  H  HA   . TRP   A  1  93  ? 5.041   -20.060 -27.917  1.00 55.02  ? 93   TRP   A HA   1 
ATOM   1392  H  HB2  . TRP   A  1  93  ? 6.211   -22.584 -27.596  1.00 54.53  ? 93   TRP   A HB2  1 
ATOM   1393  H  HB3  . TRP   A  1  93  ? 7.123   -21.300 -27.382  1.00 54.53  ? 93   TRP   A HB3  1 
ATOM   1394  H  HD1  . TRP   A  1  93  ? 3.966   -22.531 -25.874  1.00 54.18  ? 93   TRP   A HD1  1 
ATOM   1395  H  HE1  . TRP   A  1  93  ? 3.919   -22.033 -23.518  1.00 56.88  ? 93   TRP   A HE1  1 
ATOM   1396  H  HE3  . TRP   A  1  93  ? 8.230   -20.149 -25.482  1.00 52.33  ? 93   TRP   A HE3  1 
ATOM   1397  H  HZ2  . TRP   A  1  93  ? 5.550   -20.752 -21.681  1.00 58.46  ? 93   TRP   A HZ2  1 
ATOM   1398  H  HZ3  . TRP   A  1  93  ? 8.887   -19.336 -23.417  1.00 55.72  ? 93   TRP   A HZ3  1 
ATOM   1399  H  HH2  . TRP   A  1  93  ? 7.562   -19.635 -21.547  1.00 59.39  ? 93   TRP   A HH2  1 
ATOM   1400  N  N    . PHE   A  1  94  ? 5.529   -19.946 -30.593  1.00 50.27  ? 94   PHE   A N    1 
ATOM   1401  C  CA   . PHE   A  1  94  ? 6.274   -19.448 -31.741  1.00 48.78  ? 94   PHE   A CA   1 
ATOM   1402  C  C    . PHE   A  1  94  ? 7.023   -18.182 -31.352  1.00 48.04  ? 94   PHE   A C    1 
ATOM   1403  O  O    . PHE   A  1  94  ? 6.440   -17.249 -30.791  1.00 46.51  ? 94   PHE   A O    1 
ATOM   1404  C  CB   . PHE   A  1  94  ? 5.368   -19.158 -32.931  1.00 47.78  ? 94   PHE   A CB   1 
ATOM   1405  C  CG   . PHE   A  1  94  ? 6.115   -18.616 -34.117  1.00 50.47  ? 94   PHE   A CG   1 
ATOM   1406  C  CD1  . PHE   A  1  94  ? 6.916   -19.448 -34.880  1.00 50.76  ? 94   PHE   A CD1  1 
ATOM   1407  C  CD2  . PHE   A  1  94  ? 6.045   -17.274 -34.449  1.00 51.39  ? 94   PHE   A CD2  1 
ATOM   1408  C  CE1  . PHE   A  1  94  ? 7.620   -18.956 -35.961  1.00 51.04  ? 94   PHE   A CE1  1 
ATOM   1409  C  CE2  . PHE   A  1  94  ? 6.747   -16.775 -35.532  1.00 51.49  ? 94   PHE   A CE2  1 
ATOM   1410  C  CZ   . PHE   A  1  94  ? 7.535   -17.618 -36.288  1.00 51.64  ? 94   PHE   A CZ   1 
ATOM   1411  H  H    . PHE   A  1  94  ? 4.673   -19.880 -30.651  1.00 60.37  ? 94   PHE   A H    1 
ATOM   1412  H  HA   . PHE   A  1  94  ? 6.901   -20.134 -32.018  1.00 58.57  ? 94   PHE   A HA   1 
ATOM   1413  H  HB2  . PHE   A  1  94  ? 4.931   -19.981 -33.203  1.00 57.38  ? 94   PHE   A HB2  1 
ATOM   1414  H  HB3  . PHE   A  1  94  ? 4.704   -18.501 -32.670  1.00 57.38  ? 94   PHE   A HB3  1 
ATOM   1415  H  HD1  . PHE   A  1  94  ? 6.982   -20.350 -34.661  1.00 60.95  ? 94   PHE   A HD1  1 
ATOM   1416  H  HD2  . PHE   A  1  94  ? 5.521   -16.701 -33.938  1.00 61.70  ? 94   PHE   A HD2  1 
ATOM   1417  H  HE1  . PHE   A  1  94  ? 8.151   -19.526 -36.469  1.00 61.29  ? 94   PHE   A HE1  1 
ATOM   1418  H  HE2  . PHE   A  1  94  ? 6.688   -15.873 -35.750  1.00 61.83  ? 94   PHE   A HE2  1 
ATOM   1419  H  HZ   . PHE   A  1  94  ? 8.008   -17.285 -37.017  1.00 62.01  ? 94   PHE   A HZ   1 
ATOM   1420  N  N    . GLY   A  1  95  ? 8.311   -18.143 -31.667  1.00 49.90  ? 95   GLY   A N    1 
ATOM   1421  C  CA   . GLY   A  1  95  ? 9.163   -17.069 -31.214  1.00 51.24  ? 95   GLY   A CA   1 
ATOM   1422  C  C    . GLY   A  1  95  ? 9.884   -17.351 -29.919  1.00 50.12  ? 95   GLY   A C    1 
ATOM   1423  O  O    . GLY   A  1  95  ? 10.508  -16.438 -29.365  1.00 52.41  ? 95   GLY   A O    1 
ATOM   1424  H  H    . GLY   A  1  95  ? 8.713   -18.734 -32.145  1.00 59.91  ? 95   GLY   A H    1 
ATOM   1425  H  HA2  . GLY   A  1  95  ? 9.831   -16.892 -31.895  1.00 61.53  ? 95   GLY   A HA2  1 
ATOM   1426  H  HA3  . GLY   A  1  95  ? 8.623   -16.274 -31.088  1.00 61.53  ? 95   GLY   A HA3  1 
ATOM   1427  N  N    . ALA   A  1  96  ? 9.804   -18.581 -29.406  1.00 48.61  ? 96   ALA   A N    1 
ATOM   1428  C  CA   . ALA   A  1  96  ? 10.637  -18.958 -28.271  1.00 49.31  ? 96   ALA   A CA   1 
ATOM   1429  C  C    . ALA   A  1  96  ? 12.113  -18.842 -28.617  1.00 47.60  ? 96   ALA   A C    1 
ATOM   1430  O  O    . ALA   A  1  96  ? 12.943  -18.588 -27.737  1.00 43.73  ? 96   ALA   A O    1 
ATOM   1431  C  CB   . ALA   A  1  96  ? 10.307  -20.382 -27.826  1.00 49.09  ? 96   ALA   A CB   1 
ATOM   1432  H  H    . ALA   A  1  96  ? 9.285   -19.203 -29.693  1.00 58.37  ? 96   ALA   A H    1 
ATOM   1433  H  HA   . ALA   A  1  96  ? 10.448  -18.364 -27.527  1.00 59.21  ? 96   ALA   A HA   1 
ATOM   1434  H  HB1  . ALA   A  1  96  ? 10.866  -20.614 -27.068  1.00 58.95  ? 96   ALA   A HB1  1 
ATOM   1435  H  HB2  . ALA   A  1  96  ? 9.371   -20.426 -27.573  1.00 58.95  ? 96   ALA   A HB2  1 
ATOM   1436  H  HB3  . ALA   A  1  96  ? 10.479  -20.991 -28.562  1.00 58.95  ? 96   ALA   A HB3  1 
ATOM   1437  N  N    . SER   A  1  97  ? 12.455  -19.021 -29.891  1.00 47.99  ? 97   SER   A N    1 
ATOM   1438  C  CA   . SER   A  1  97  ? 13.823  -18.892 -30.369  1.00 50.54  ? 97   SER   A CA   1 
ATOM   1439  C  C    . SER   A  1  97  ? 13.798  -18.158 -31.699  1.00 50.83  ? 97   SER   A C    1 
ATOM   1440  O  O    . SER   A  1  97  ? 13.002  -18.496 -32.581  1.00 51.26  ? 97   SER   A O    1 
ATOM   1441  C  CB   . SER   A  1  97  ? 14.487  -20.262 -30.529  1.00 53.06  ? 97   SER   A CB   1 
ATOM   1442  O  OG   . SER   A  1  97  ? 13.771  -21.067 -31.448  1.00 59.13  ? 97   SER   A OG   1 
ATOM   1443  H  H    . SER   A  1  97  ? 11.895  -19.224 -30.512  1.00 57.62  ? 97   SER   A H    1 
ATOM   1444  H  HA   . SER   A  1  97  ? 14.348  -18.376 -29.738  1.00 60.69  ? 97   SER   A HA   1 
ATOM   1445  H  HB2  . SER   A  1  97  ? 15.392  -20.138 -30.856  1.00 63.71  ? 97   SER   A HB2  1 
ATOM   1446  H  HB3  . SER   A  1  97  ? 14.504  -20.707 -29.667  1.00 63.71  ? 97   SER   A HB3  1 
ATOM   1447  H  HG   . SER   A  1  97  ? 13.901  -21.880 -31.280  1.00 70.99  ? 97   SER   A HG   1 
ATOM   1448  N  N    . VAL   A  1  98  ? 14.663  -17.157 -31.838  1.00 53.38  ? 98   VAL   A N    1 
ATOM   1449  C  CA   . VAL   A  1  98  ? 14.735  -16.346 -33.047  1.00 56.53  ? 98   VAL   A CA   1 
ATOM   1450  C  C    . VAL   A  1  98  ? 16.199  -16.067 -33.351  1.00 53.91  ? 98   VAL   A C    1 
ATOM   1451  O  O    . VAL   A  1  98  ? 16.951  -15.638 -32.469  1.00 54.96  ? 98   VAL   A O    1 
ATOM   1452  C  CB   . VAL   A  1  98  ? 13.959  -15.021 -32.903  1.00 60.75  ? 98   VAL   A CB   1 
ATOM   1453  C  CG1  . VAL   A  1  98  ? 13.893  -14.295 -34.241  1.00 64.14  ? 98   VAL   A CG1  1 
ATOM   1454  C  CG2  . VAL   A  1  98  ? 12.560  -15.274 -32.356  1.00 63.01  ? 98   VAL   A CG2  1 
ATOM   1455  H  H    . VAL   A  1  98  ? 15.228  -16.925 -31.234  1.00 64.09  ? 98   VAL   A H    1 
ATOM   1456  H  HA   . VAL   A  1  98  ? 14.355  -16.844 -33.787  1.00 67.88  ? 98   VAL   A HA   1 
ATOM   1457  H  HB   . VAL   A  1  98  ? 14.426  -14.451 -32.272  1.00 72.94  ? 98   VAL   A HB   1 
ATOM   1458  H  HG11 . VAL   A  1  98  ? 13.392  -13.472 -34.129  1.00 77.01  ? 98   VAL   A HG11 1 
ATOM   1459  H  HG12 . VAL   A  1  98  ? 14.795  -14.095 -34.537  1.00 77.01  ? 98   VAL   A HG12 1 
ATOM   1460  H  HG13 . VAL   A  1  98  ? 13.451  -14.866 -34.888  1.00 77.01  ? 98   VAL   A HG13 1 
ATOM   1461  H  HG21 . VAL   A  1  98  ? 12.090  -14.428 -32.289  1.00 75.65  ? 98   VAL   A HG21 1 
ATOM   1462  H  HG22 . VAL   A  1  98  ? 12.088  -15.867 -32.960  1.00 75.65  ? 98   VAL   A HG22 1 
ATOM   1463  H  HG23 . VAL   A  1  98  ? 12.633  -15.683 -31.480  1.00 75.65  ? 98   VAL   A HG23 1 
ATOM   1464  N  N    . ARG   A  1  99  ? 16.603  -16.317 -34.593  1.00 56.72  ? 99   ARG   A N    1 
ATOM   1465  C  CA   A ARG   A  1  99  ? 17.954  -16.054 -35.067  0.45 58.69  ? 99   ARG   A CA   1 
ATOM   1466  C  CA   B ARG   A  1  99  ? 17.950  -15.998 -35.036  0.55 58.60  ? 99   ARG   A CA   1 
ATOM   1467  C  C    . ARG   A  1  99  ? 17.884  -15.342 -36.407  1.00 58.14  ? 99   ARG   A C    1 
ATOM   1468  O  O    . ARG   A  1  99  ? 16.948  -15.555 -37.183  1.00 58.03  ? 99   ARG   A O    1 
ATOM   1469  C  CB   A ARG   A  1  99  ? 18.764  -17.339 -35.239  0.45 59.14  ? 99   ARG   A CB   1 
ATOM   1470  C  CB   B ARG   A  1  99  ? 18.851  -17.245 -35.070  0.55 59.20  ? 99   ARG   A CB   1 
ATOM   1471  C  CG   A ARG   A  1  99  ? 19.556  -17.741 -34.028  0.45 60.72  ? 99   ARG   A CG   1 
ATOM   1472  C  CG   B ARG   A  1  99  ? 19.607  -17.499 -33.762  0.55 60.74  ? 99   ARG   A CG   1 
ATOM   1473  C  CD   A ARG   A  1  99  ? 20.732  -16.817 -33.771  0.45 63.87  ? 99   ARG   A CD   1 
ATOM   1474  C  CD   B ARG   A  1  99  ? 20.706  -16.464 -33.534  0.55 64.27  ? 99   ARG   A CD   1 
ATOM   1475  N  NE   A ARG   A  1  99  ? 21.451  -17.275 -32.591  0.45 63.93  ? 99   ARG   A NE   1 
ATOM   1476  N  NE   B ARG   A  1  99  ? 21.901  -16.725 -34.334  0.55 65.72  ? 99   ARG   A NE   1 
ATOM   1477  C  CZ   A ARG   A  1  99  ? 21.019  -17.098 -31.347  0.45 64.11  ? 99   ARG   A CZ   1 
ATOM   1478  C  CZ   B ARG   A  1  99  ? 22.765  -15.790 -34.725  0.55 70.33  ? 99   ARG   A CZ   1 
ATOM   1479  N  NH1  A ARG   A  1  99  ? 19.878  -16.459 -31.123  0.45 63.28  ? 99   ARG   A NH1  1 
ATOM   1480  N  NH1  B ARG   A  1  99  ? 23.824  -16.131 -35.446  0.55 72.88  ? 99   ARG   A NH1  1 
ATOM   1481  N  NH2  A ARG   A  1  99  ? 21.728  -17.559 -30.328  0.45 65.95  ? 99   ARG   A NH2  1 
ATOM   1482  N  NH2  B ARG   A  1  99  ? 22.569  -14.515 -34.414  0.55 71.64  ? 99   ARG   A NH2  1 
ATOM   1483  H  H    A ARG   A  1  99  ? 16.093  -16.651 -35.200  0.45 68.11  ? 99   ARG   A H    1 
ATOM   1484  H  H    B ARG   A  1  99  ? 16.109  -16.674 -35.200  0.55 68.11  ? 99   ARG   A H    1 
ATOM   1485  H  HA   A ARG   A  1  99  ? 18.409  -15.488 -34.423  0.45 70.47  ? 99   ARG   A HA   1 
ATOM   1486  H  HA   B ARG   A  1  99  ? 18.354  -15.364 -34.425  0.55 70.36  ? 99   ARG   A HA   1 
ATOM   1487  H  HB2  A ARG   A  1  99  ? 18.153  -18.064 -35.444  0.45 71.00  ? 99   ARG   A HB2  1 
ATOM   1488  H  HB2  B ARG   A  1  99  ? 18.300  -18.023 -35.248  0.55 71.08  ? 99   ARG   A HB2  1 
ATOM   1489  H  HB3  A ARG   A  1  99  ? 19.389  -17.215 -35.971  0.45 71.00  ? 99   ARG   A HB3  1 
ATOM   1490  H  HB3  B ARG   A  1  99  ? 19.508  -17.135 -35.774  0.55 71.08  ? 99   ARG   A HB3  1 
ATOM   1491  H  HG2  A ARG   A  1  99  ? 18.979  -17.717 -33.249  0.45 72.90  ? 99   ARG   A HG2  1 
ATOM   1492  H  HG2  B ARG   A  1  99  ? 18.986  -17.451 -33.018  0.55 72.93  ? 99   ARG   A HG2  1 
ATOM   1493  H  HG3  A ARG   A  1  99  ? 19.902  -18.638 -34.158  0.45 72.90  ? 99   ARG   A HG3  1 
ATOM   1494  H  HG3  B ARG   A  1  99  ? 20.019  -18.376 -33.795  0.55 72.93  ? 99   ARG   A HG3  1 
ATOM   1495  H  HD2  A ARG   A  1  99  ? 21.334  -16.830 -34.532  0.45 76.69  ? 99   ARG   A HD2  1 
ATOM   1496  H  HD2  B ARG   A  1  99  ? 20.369  -15.587 -33.774  0.55 77.16  ? 99   ARG   A HD2  1 
ATOM   1497  H  HD3  A ARG   A  1  99  ? 20.414  -15.914 -33.616  0.45 76.69  ? 99   ARG   A HD3  1 
ATOM   1498  H  HD3  B ARG   A  1  99  ? 20.962  -16.476 -32.598  0.55 77.16  ? 99   ARG   A HD3  1 
ATOM   1499  H  HE   A ARG   A  1  99  ? 22.199  -17.684 -32.706  0.45 76.75  ? 99   ARG   A HE   1 
ATOM   1500  H  HE   B ARG   A  1  99  ? 22.056  -17.537 -34.569  0.55 78.90  ? 99   ARG   A HE   1 
ATOM   1501  H  HH11 A ARG   A  1  99  ? 19.416  -16.158 -31.783  0.45 75.97  ? 99   ARG   A HH11 1 
ATOM   1502  H  HH11 B ARG   A  1  99  ? 23.951  -16.954 -35.661  0.55 87.50  ? 99   ARG   A HH11 1 
ATOM   1503  H  HH12 A ARG   A  1  99  ? 19.600  -16.345 -30.317  0.45 75.97  ? 99   ARG   A HH12 1 
ATOM   1504  H  HH12 B ARG   A  1  99  ? 24.384  -15.529 -35.699  0.55 87.50  ? 99   ARG   A HH12 1 
ATOM   1505  H  HH21 A ARG   A  1  99  ? 22.468  -17.973 -30.471  0.45 79.18  ? 99   ARG   A HH21 1 
ATOM   1506  H  HH21 B ARG   A  1  99  ? 21.878  -14.285 -33.957  0.55 86.00  ? 99   ARG   A HH21 1 
ATOM   1507  H  HH22 A ARG   A  1  99  ? 21.449  -17.444 -29.523  0.45 79.18  ? 99   ARG   A HH22 1 
ATOM   1508  H  HH22 B ARG   A  1  99  ? 23.133  -13.918 -34.671  0.55 86.00  ? 99   ARG   A HH22 1 
ATOM   1509  N  N    . SER   A  1  100 ? 18.890  -14.521 -36.685  1.00 61.19  ? 100  SER   A N    1 
ATOM   1510  C  CA   . SER   A  1  100 ? 18.946  -13.775 -37.929  1.00 65.41  ? 100  SER   A CA   1 
ATOM   1511  C  C    . SER   A  1  100 ? 20.352  -13.839 -38.498  1.00 67.33  ? 100  SER   A C    1 
ATOM   1512  O  O    . SER   A  1  100 ? 21.337  -13.835 -37.754  1.00 69.68  ? 100  SER   A O    1 
ATOM   1513  C  CB   . SER   A  1  100 ? 18.531  -12.315 -37.719  1.00 69.92  ? 100  SER   A CB   1 
ATOM   1514  O  OG   . SER   A  1  100 ? 18.446  -11.634 -38.958  1.00 76.68  ? 100  SER   A OG   1 
ATOM   1515  H  H    . SER   A  1  100 ? 19.557  -14.379 -36.161  1.00 73.46  ? 100  SER   A H    1 
ATOM   1516  H  HA   . SER   A  1  100 ? 18.343  -14.175 -38.575  1.00 78.53  ? 100  SER   A HA   1 
ATOM   1517  H  HB2  . SER   A  1  100 ? 17.663  -12.292 -37.287  1.00 83.94  ? 100  SER   A HB2  1 
ATOM   1518  H  HB3  . SER   A  1  100 ? 19.191  -11.876 -37.161  1.00 83.94  ? 100  SER   A HB3  1 
ATOM   1519  H  HG   . SER   A  1  100 ? 18.135  -12.146 -39.546  1.00 92.06  ? 100  SER   A HG   1 
ATOM   1520  N  N    . LYS   A  1  101 ? 20.432  -13.907 -39.823  1.00 67.05  ? 101  LYS   A N    1 
ATOM   1521  C  CA   . LYS   A  1  101 ? 21.707  -13.860 -40.528  1.00 71.66  ? 101  LYS   A CA   1 
ATOM   1522  C  C    . LYS   A  1  101 ? 21.459  -13.128 -41.837  1.00 73.82  ? 101  LYS   A C    1 
ATOM   1523  O  O    . LYS   A  1  101 ? 20.865  -13.695 -42.758  1.00 70.50  ? 101  LYS   A O    1 
ATOM   1524  C  CB   . LYS   A  1  101 ? 22.261  -15.258 -40.777  1.00 71.70  ? 101  LYS   A CB   1 
ATOM   1525  C  CG   . LYS   A  1  101 ? 23.585  -15.261 -41.520  1.00 71.19  ? 101  LYS   A CG   1 
ATOM   1526  C  CD   . LYS   A  1  101 ? 23.984  -16.658 -41.947  1.00 72.04  ? 101  LYS   A CD   1 
ATOM   1527  C  CE   . LYS   A  1  101 ? 25.149  -16.614 -42.917  1.00 76.20  ? 101  LYS   A CE   1 
ATOM   1528  N  NZ   . LYS   A  1  101 ? 26.307  -15.865 -42.366  1.00 83.65  ? 101  LYS   A NZ   1 
ATOM   1529  H  H    . LYS   A  1  101 ? 19.751  -13.981 -40.343  1.00 80.50  ? 101  LYS   A H    1 
ATOM   1530  H  HA   . LYS   A  1  101 ? 22.359  -13.372 -40.001  1.00 86.02  ? 101  LYS   A HA   1 
ATOM   1531  H  HB2  . LYS   A  1  101 ? 22.398  -15.698 -39.923  1.00 86.08  ? 101  LYS   A HB2  1 
ATOM   1532  H  HB3  . LYS   A  1  101 ? 21.621  -15.758 -41.308  1.00 86.08  ? 101  LYS   A HB3  1 
ATOM   1533  H  HG2  . LYS   A  1  101 ? 23.507  -14.711 -42.315  1.00 85.47  ? 101  LYS   A HG2  1 
ATOM   1534  H  HG3  . LYS   A  1  101 ? 24.278  -14.910 -40.940  1.00 85.47  ? 101  LYS   A HG3  1 
ATOM   1535  H  HD2  . LYS   A  1  101 ? 24.251  -17.170 -41.168  1.00 86.49  ? 101  LYS   A HD2  1 
ATOM   1536  H  HD3  . LYS   A  1  101 ? 23.234  -17.089 -42.386  1.00 86.49  ? 101  LYS   A HD3  1 
ATOM   1537  H  HE2  . LYS   A  1  101 ? 25.439  -17.520 -43.108  1.00 91.47  ? 101  LYS   A HE2  1 
ATOM   1538  H  HE3  . LYS   A  1  101 ? 24.867  -16.176 -43.735  1.00 91.47  ? 101  LYS   A HE3  1 
ATOM   1539  H  HZ1  . LYS   A  1  101 ? 27.041  -16.054 -42.833  1.00 100.42 ? 101  LYS   A HZ1  1 
ATOM   1540  H  HZ2  . LYS   A  1  101 ? 26.153  -14.990 -42.412  1.00 100.42 ? 101  LYS   A HZ2  1 
ATOM   1541  H  HZ3  . LYS   A  1  101 ? 26.439  -16.091 -41.516  1.00 100.42 ? 101  LYS   A HZ3  1 
ATOM   1542  N  N    . GLN   A  1  102 ? 21.902  -11.876 -41.919  1.00 77.82  ? 102  GLN   A N    1 
ATOM   1543  C  CA   . GLN   A  1  102 ? 21.709  -11.053 -43.114  1.00 80.82  ? 102  GLN   A CA   1 
ATOM   1544  C  C    . GLN   A  1  102 ? 20.212  -10.988 -43.393  1.00 78.10  ? 102  GLN   A C    1 
ATOM   1545  O  O    . GLN   A  1  102 ? 19.467  -10.482 -42.537  1.00 76.36  ? 102  GLN   A O    1 
ATOM   1546  C  CB   . GLN   A  1  102 ? 22.578  -11.623 -44.235  1.00 85.32  ? 102  GLN   A CB   1 
ATOM   1547  C  CG   . GLN   A  1  102 ? 24.065  -11.489 -43.973  1.00 91.19  ? 102  GLN   A CG   1 
ATOM   1548  C  CD   . GLN   A  1  102 ? 24.908  -12.185 -45.019  1.00 96.76  ? 102  GLN   A CD   1 
ATOM   1549  O  OE1  . GLN   A  1  102 ? 24.546  -13.250 -45.521  1.00 93.12  ? 102  GLN   A OE1  1 
ATOM   1550  N  NE2  . GLN   A  1  102 ? 26.040  -11.582 -45.359  1.00 104.60 ? 102  GLN   A NE2  1 
ATOM   1551  H  H    . GLN   A  1  102 ? 22.324  -11.475 -41.286  1.00 93.42  ? 102  GLN   A H    1 
ATOM   1552  H  HA   . GLN   A  1  102 ? 22.002  -10.146 -42.930  1.00 97.02  ? 102  GLN   A HA   1 
ATOM   1553  H  HB2  . GLN   A  1  102 ? 22.378  -12.567 -44.336  1.00 102.41 ? 102  GLN   A HB2  1 
ATOM   1554  H  HB3  . GLN   A  1  102 ? 22.378  -11.151 -45.058  1.00 102.41 ? 102  GLN   A HB3  1 
ATOM   1555  H  HG2  . GLN   A  1  102 ? 24.302  -10.549 -43.972  1.00 109.47 ? 102  GLN   A HG2  1 
ATOM   1556  H  HG3  . GLN   A  1  102 ? 24.271  -11.884 -43.111  1.00 109.47 ? 102  GLN   A HG3  1 
ATOM   1557  H  HE21 . GLN   A  1  102 ? 26.259  -10.838 -44.988  1.00 125.56 ? 102  GLN   A HE21 1 
ATOM   1558  H  HE22 . GLN   A  1  102 ? 26.555  -11.936 -45.949  1.00 125.56 ? 102  GLN   A HE22 1 
ATOM   1559  N  N    . ASP   A  1  103 ? 19.724  -11.485 -44.530  1.00 78.84  ? 103  ASP   A N    1 
ATOM   1560  C  CA   . ASP   A  1  103 ? 18.313  -11.354 -44.867  1.00 79.61  ? 103  ASP   A CA   1 
ATOM   1561  C  C    . ASP   A  1  103 ? 17.434  -12.383 -44.172  1.00 77.62  ? 103  ASP   A C    1 
ATOM   1562  O  O    . ASP   A  1  103 ? 16.218  -12.181 -44.084  1.00 79.43  ? 103  ASP   A O    1 
ATOM   1563  C  CB   . ASP   A  1  103 ? 18.118  -11.483 -46.379  1.00 85.42  ? 103  ASP   A CB   1 
ATOM   1564  C  CG   . ASP   A  1  103 ? 18.644  -10.284 -47.140  1.00 95.52  ? 103  ASP   A CG   1 
ATOM   1565  O  OD1  . ASP   A  1  103 ? 18.718  -9.188  -46.546  1.00 100.54 ? 103  ASP   A OD1  1 
ATOM   1566  O  OD2  . ASP   A  1  103 ? 18.979  -10.437 -48.333  1.00 102.50 ? 103  ASP   A OD2  1 
ATOM   1567  H  H    . ASP   A  1  103 ? 20.190  -11.901 -45.121  1.00 94.65  ? 103  ASP   A H    1 
ATOM   1568  H  HA   . ASP   A  1  103 ? 18.019  -10.472 -44.589  1.00 95.57  ? 103  ASP   A HA   1 
ATOM   1569  H  HB2  . ASP   A  1  103 ? 18.592  -12.269 -46.693  1.00 102.54 ? 103  ASP   A HB2  1 
ATOM   1570  H  HB3  . ASP   A  1  103 ? 17.171  -11.568 -46.571  1.00 102.54 ? 103  ASP   A HB3  1 
ATOM   1571  N  N    . LYS   A  1  104 ? 18.014  -13.470 -43.679  1.00 72.55  ? 104  LYS   A N    1 
ATOM   1572  C  CA   . LYS   A  1  104 ? 17.242  -14.607 -43.204  1.00 66.04  ? 104  LYS   A CA   1 
ATOM   1573  C  C    . LYS   A  1  104 ? 16.845  -14.424 -41.747  1.00 57.84  ? 104  LYS   A C    1 
ATOM   1574  O  O    . LYS   A  1  104 ? 17.628  -13.928 -40.931  1.00 52.97  ? 104  LYS   A O    1 
ATOM   1575  C  CB   . LYS   A  1  104 ? 18.052  -15.894 -43.370  1.00 67.13  ? 104  LYS   A CB   1 
ATOM   1576  C  CG   . LYS   A  1  104 ? 18.602  -16.092 -44.779  1.00 69.78  ? 104  LYS   A CG   1 
ATOM   1577  C  CD   . LYS   A  1  104 ? 19.761  -17.070 -44.792  1.00 71.57  ? 104  LYS   A CD   1 
ATOM   1578  C  CE   . LYS   A  1  104 ? 21.062  -16.393 -44.395  1.00 74.24  ? 104  LYS   A CE   1 
ATOM   1579  N  NZ   . LYS   A  1  104 ? 21.632  -15.560 -45.497  1.00 78.88  ? 104  LYS   A NZ   1 
ATOM   1580  H  H    . LYS   A  1  104 ? 18.865  -13.574 -43.609  1.00 87.10  ? 104  LYS   A H    1 
ATOM   1581  H  HA   . LYS   A  1  104 ? 16.425  -14.682 -43.722  1.00 79.28  ? 104  LYS   A HA   1 
ATOM   1582  H  HB2  . LYS   A  1  104 ? 18.805  -15.870 -42.759  1.00 80.59  ? 104  LYS   A HB2  1 
ATOM   1583  H  HB3  . LYS   A  1  104 ? 17.482  -16.651 -43.166  1.00 80.59  ? 104  LYS   A HB3  1 
ATOM   1584  H  HG2  . LYS   A  1  104 ? 17.902  -16.442 -45.351  1.00 83.78  ? 104  LYS   A HG2  1 
ATOM   1585  H  HG3  . LYS   A  1  104 ? 18.917  -15.241 -45.123  1.00 83.78  ? 104  LYS   A HG3  1 
ATOM   1586  H  HD2  . LYS   A  1  104 ? 19.585  -17.786 -44.162  1.00 85.91  ? 104  LYS   A HD2  1 
ATOM   1587  H  HD3  . LYS   A  1  104 ? 19.866  -17.432 -45.686  1.00 85.91  ? 104  LYS   A HD3  1 
ATOM   1588  H  HE2  . LYS   A  1  104 ? 20.899  -15.814 -43.634  1.00 89.13  ? 104  LYS   A HE2  1 
ATOM   1589  H  HE3  . LYS   A  1  104 ? 21.715  -17.071 -44.162  1.00 89.13  ? 104  LYS   A HE3  1 
ATOM   1590  H  HZ1  . LYS   A  1  104 ? 22.403  -15.200 -45.238  1.00 94.69  ? 104  LYS   A HZ1  1 
ATOM   1591  H  HZ2  . LYS   A  1  104 ? 21.775  -16.064 -46.216  1.00 94.69  ? 104  LYS   A HZ2  1 
ATOM   1592  H  HZ3  . LYS   A  1  104 ? 21.065  -14.908 -45.709  1.00 94.69  ? 104  LYS   A HZ3  1 
ATOM   1593  N  N    . ILE   A  1  105 ? 15.613  -14.817 -41.430  1.00 55.40  ? 105  ILE   A N    1 
ATOM   1594  C  CA   . ILE   A  1  105 ? 15.116  -14.861 -40.061  1.00 51.98  ? 105  ILE   A CA   1 
ATOM   1595  C  C    . ILE   A  1  105 ? 14.602  -16.269 -39.808  1.00 52.03  ? 105  ILE   A C    1 
ATOM   1596  O  O    . ILE   A  1  105 ? 13.725  -16.752 -40.536  1.00 54.21  ? 105  ILE   A O    1 
ATOM   1597  C  CB   . ILE   A  1  105 ? 14.003  -13.831 -39.803  1.00 54.02  ? 105  ILE   A CB   1 
ATOM   1598  C  CG1  . ILE   A  1  105 ? 14.511  -12.413 -40.072  1.00 59.15  ? 105  ILE   A CG1  1 
ATOM   1599  C  CG2  . ILE   A  1  105 ? 13.490  -13.958 -38.367  1.00 52.39  ? 105  ILE   A CG2  1 
ATOM   1600  C  CD1  . ILE   A  1  105 ? 13.449  -11.338 -39.924  1.00 61.45  ? 105  ILE   A CD1  1 
ATOM   1601  H  H    . ILE   A  1  105 ? 15.031  -15.070 -42.011  1.00 66.52  ? 105  ILE   A H    1 
ATOM   1602  H  HA   . ILE   A  1  105 ? 15.846  -14.674 -39.450  1.00 62.42  ? 105  ILE   A HA   1 
ATOM   1603  H  HB   . ILE   A  1  105 ? 13.270  -14.011 -40.412  1.00 64.86  ? 105  ILE   A HB   1 
ATOM   1604  H  HG12 . ILE   A  1  105 ? 15.222  -12.213 -39.443  1.00 71.02  ? 105  ILE   A HG12 1 
ATOM   1605  H  HG13 . ILE   A  1  105 ? 14.850  -12.371 -40.979  1.00 71.02  ? 105  ILE   A HG13 1 
ATOM   1606  H  HG21 . ILE   A  1  105 ? 12.780  -13.312 -38.227  1.00 62.90  ? 105  ILE   A HG21 1 
ATOM   1607  H  HG22 . ILE   A  1  105 ? 13.152  -14.857 -38.231  1.00 62.90  ? 105  ILE   A HG22 1 
ATOM   1608  H  HG23 . ILE   A  1  105 ? 14.221  -13.783 -37.754  1.00 62.90  ? 105  ILE   A HG23 1 
ATOM   1609  H  HD11 . ILE   A  1  105 ? 13.835  -10.478 -40.153  1.00 73.77  ? 105  ILE   A HD11 1 
ATOM   1610  H  HD12 . ILE   A  1  105 ? 12.711  -11.539 -40.522  1.00 73.77  ? 105  ILE   A HD12 1 
ATOM   1611  H  HD13 . ILE   A  1  105 ? 13.136  -11.327 -39.006  1.00 73.77  ? 105  ILE   A HD13 1 
ATOM   1612  N  N    . LEU   A  1  106 ? 15.141  -16.925 -38.786  1.00 49.96  ? 106  LEU   A N    1 
ATOM   1613  C  CA   . LEU   A  1  106 ? 14.672  -18.233 -38.351  1.00 49.06  ? 106  LEU   A CA   1 
ATOM   1614  C  C    . LEU   A  1  106 ? 13.980  -18.072 -37.004  1.00 50.36  ? 106  LEU   A C    1 
ATOM   1615  O  O    . LEU   A  1  106 ? 14.591  -17.595 -36.042  1.00 52.53  ? 106  LEU   A O    1 
ATOM   1616  C  CB   . LEU   A  1  106 ? 15.824  -19.232 -38.254  1.00 49.50  ? 106  LEU   A CB   1 
ATOM   1617  C  CG   . LEU   A  1  106 ? 15.448  -20.665 -37.864  1.00 45.95  ? 106  LEU   A CG   1 
ATOM   1618  C  CD1  . LEU   A  1  106 ? 14.452  -21.267 -38.846  1.00 46.86  ? 106  LEU   A CD1  1 
ATOM   1619  C  CD2  . LEU   A  1  106 ? 16.693  -21.530 -37.780  1.00 44.53  ? 106  LEU   A CD2  1 
ATOM   1620  H  H    . LEU   A  1  106 ? 15.797  -16.623 -38.318  1.00 59.99  ? 106  LEU   A H    1 
ATOM   1621  H  HA   . LEU   A  1  106 ? 14.030  -18.579 -38.991  1.00 58.91  ? 106  LEU   A HA   1 
ATOM   1622  H  HB2  . LEU   A  1  106 ? 16.258  -19.276 -39.120  1.00 59.44  ? 106  LEU   A HB2  1 
ATOM   1623  H  HB3  . LEU   A  1  106 ? 16.448  -18.908 -37.586  1.00 59.44  ? 106  LEU   A HB3  1 
ATOM   1624  H  HG   . LEU   A  1  106 ? 15.022  -20.644 -36.993  1.00 55.17  ? 106  LEU   A HG   1 
ATOM   1625  H  HD11 . LEU   A  1  106 ? 14.264  -22.182 -38.584  1.00 56.27  ? 106  LEU   A HD11 1 
ATOM   1626  H  HD12 . LEU   A  1  106 ? 13.635  -20.743 -38.828  1.00 56.27  ? 106  LEU   A HD12 1 
ATOM   1627  H  HD13 . LEU   A  1  106 ? 14.836  -21.250 -39.737  1.00 56.27  ? 106  LEU   A HD13 1 
ATOM   1628  H  HD21 . LEU   A  1  106 ? 16.438  -22.426 -37.509  1.00 53.47  ? 106  LEU   A HD21 1 
ATOM   1629  H  HD22 . LEU   A  1  106 ? 17.120  -21.556 -38.651  1.00 53.47  ? 106  LEU   A HD22 1 
ATOM   1630  H  HD23 . LEU   A  1  106 ? 17.300  -21.148 -37.126  1.00 53.47  ? 106  LEU   A HD23 1 
ATOM   1631  N  N    . ALA   A  1  107 ? 12.708  -18.455 -36.947  1.00 53.20  ? 107  ALA   A N    1 
ATOM   1632  C  CA   . ALA   A  1  107 ? 11.916  -18.430 -35.726  1.00 53.43  ? 107  ALA   A CA   1 
ATOM   1633  C  C    . ALA   A  1  107 ? 11.220  -19.775 -35.579  1.00 51.85  ? 107  ALA   A C    1 
ATOM   1634  O  O    . ALA   A  1  107 ? 10.758  -20.349 -36.569  1.00 50.62  ? 107  ALA   A O    1 
ATOM   1635  C  CB   . ALA   A  1  107 ? 10.890  -17.293 -35.752  1.00 53.55  ? 107  ALA   A CB   1 
ATOM   1636  H  H    . ALA   A  1  107 ? 12.268  -18.744 -37.628  1.00 63.88  ? 107  ALA   A H    1 
ATOM   1637  H  HA   . ALA   A  1  107 ? 12.485  -18.290 -34.953  1.00 64.15  ? 107  ALA   A HA   1 
ATOM   1638  H  HB1  . ALA   A  1  107 ? 10.366  -17.322 -34.936  1.00 64.30  ? 107  ALA   A HB1  1 
ATOM   1639  H  HB2  . ALA   A  1  107 ? 11.359  -16.446 -35.813  1.00 64.30  ? 107  ALA   A HB2  1 
ATOM   1640  H  HB3  . ALA   A  1  107 ? 10.311  -17.407 -36.521  1.00 64.30  ? 107  ALA   A HB3  1 
ATOM   1641  N  N    . CYS   A  1  108 ? 11.147  -20.278 -34.348  1.00 52.54  ? 108  CYS   A N    1 
ATOM   1642  C  CA   . CYS   A  1  108 ? 10.695  -21.640 -34.106  1.00 49.94  ? 108  CYS   A CA   1 
ATOM   1643  C  C    . CYS   A  1  108 ? 9.628   -21.685 -33.020  1.00 45.33  ? 108  CYS   A C    1 
ATOM   1644  O  O    . CYS   A  1  108 ? 9.558   -20.813 -32.150  1.00 43.83  ? 108  CYS   A O    1 
ATOM   1645  C  CB   . CYS   A  1  108 ? 11.866  -22.547 -33.705  1.00 51.16  ? 108  CYS   A CB   1 
ATOM   1646  S  SG   . CYS   A  1  108 ? 13.157  -22.716 -34.958  1.00 57.35  ? 108  CYS   A SG   1 
ATOM   1647  H  H    . CYS   A  1  108 ? 11.356  -19.845 -33.635  1.00 63.08  ? 108  CYS   A H    1 
ATOM   1648  H  HA   . CYS   A  1  108 ? 10.288  -21.978 -34.919  1.00 59.97  ? 108  CYS   A HA   1 
ATOM   1649  H  HB2  . CYS   A  1  108 ? 12.280  -22.181 -32.907  1.00 61.43  ? 108  CYS   A HB2  1 
ATOM   1650  H  HB3  . CYS   A  1  108 ? 11.520  -23.434 -33.521  1.00 61.43  ? 108  CYS   A HB3  1 
ATOM   1651  N  N    . ALA   A  1  109 ? 8.801   -22.732 -33.086  1.00 42.94  ? 109  ALA   A N    1 
ATOM   1652  C  CA   . ALA   A  1  109 ? 7.725   -22.993 -32.131  1.00 43.12  ? 109  ALA   A CA   1 
ATOM   1653  C  C    . ALA   A  1  109 ? 7.983   -24.353 -31.496  1.00 42.46  ? 109  ALA   A C    1 
ATOM   1654  O  O    . ALA   A  1  109 ? 7.516   -25.384 -32.006  1.00 41.34  ? 109  ALA   A O    1 
ATOM   1655  C  CB   . ALA   A  1  109 ? 6.361   -22.959 -32.818  1.00 45.38  ? 109  ALA   A CB   1 
ATOM   1656  H  H    . ALA   A  1  109 ? 8.847   -23.329 -33.703  1.00 51.57  ? 109  ALA   A H    1 
ATOM   1657  H  HA   . ALA   A  1  109 ? 7.733   -22.317 -31.436  1.00 51.78  ? 109  ALA   A HA   1 
ATOM   1658  H  HB1  . ALA   A  1  109 ? 5.671   -23.136 -32.160  1.00 54.50  ? 109  ALA   A HB1  1 
ATOM   1659  H  HB2  . ALA   A  1  109 ? 6.227   -22.082 -33.211  1.00 54.50  ? 109  ALA   A HB2  1 
ATOM   1660  H  HB3  . ALA   A  1  109 ? 6.340   -23.638 -33.510  1.00 54.50  ? 109  ALA   A HB3  1 
ATOM   1661  N  N    . PRO   A  1  110 ? 8.720   -24.411 -30.381  1.00 45.08  ? 110  PRO   A N    1 
ATOM   1662  C  CA   . PRO   A  1  110 ? 9.130   -25.718 -29.841  1.00 45.41  ? 110  PRO   A CA   1 
ATOM   1663  C  C    . PRO   A  1  110 ? 8.001   -26.529 -29.219  1.00 45.90  ? 110  PRO   A C    1 
ATOM   1664  O  O    . PRO   A  1  110 ? 8.241   -27.684 -28.846  1.00 45.80  ? 110  PRO   A O    1 
ATOM   1665  C  CB   . PRO   A  1  110 ? 10.186  -25.350 -28.785  1.00 47.03  ? 110  PRO   A CB   1 
ATOM   1666  C  CG   . PRO   A  1  110 ? 10.567  -23.926 -29.078  1.00 48.79  ? 110  PRO   A CG   1 
ATOM   1667  C  CD   . PRO   A  1  110 ? 9.338   -23.299 -29.641  1.00 49.30  ? 110  PRO   A CD   1 
ATOM   1668  H  HA   . PRO   A  1  110 ? 9.543   -26.243 -30.544  1.00 54.53  ? 110  PRO   A HA   1 
ATOM   1669  H  HB2  . PRO   A  1  110 ? 9.803   -25.429 -27.897  1.00 56.48  ? 110  PRO   A HB2  1 
ATOM   1670  H  HB3  . PRO   A  1  110 ? 10.953  -25.937 -28.869  1.00 56.48  ? 110  PRO   A HB3  1 
ATOM   1671  H  HG2  . PRO   A  1  110 ? 10.838  -23.482 -28.259  1.00 58.58  ? 110  PRO   A HG2  1 
ATOM   1672  H  HG3  . PRO   A  1  110 ? 11.292  -23.905 -29.722  1.00 58.58  ? 110  PRO   A HG3  1 
ATOM   1673  H  HD2  . PRO   A  1  110 ? 8.753   -22.984 -28.935  1.00 59.20  ? 110  PRO   A HD2  1 
ATOM   1674  H  HD3  . PRO   A  1  110 ? 9.563   -22.567 -30.237  1.00 59.20  ? 110  PRO   A HD3  1 
ATOM   1675  N  N    . LEU   A  1  111 ? 6.791   -25.978 -29.088  1.00 42.91  ? 111  LEU   A N    1 
ATOM   1676  C  CA   . LEU   A  1  111 ? 5.659   -26.723 -28.545  1.00 41.95  ? 111  LEU   A CA   1 
ATOM   1677  C  C    . LEU   A  1  111 ? 4.551   -26.911 -29.575  1.00 46.61  ? 111  LEU   A C    1 
ATOM   1678  O  O    . LEU   A  1  111 ? 3.412   -27.224 -29.214  1.00 45.62  ? 111  LEU   A O    1 
ATOM   1679  C  CB   . LEU   A  1  111 ? 5.119   -26.039 -27.290  1.00 41.06  ? 111  LEU   A CB   1 
ATOM   1680  C  CG   . LEU   A  1  111 ? 5.893   -26.455 -26.038  1.00 42.95  ? 111  LEU   A CG   1 
ATOM   1681  C  CD1  . LEU   A  1  111 ? 5.589   -25.531 -24.877  1.00 43.42  ? 111  LEU   A CD1  1 
ATOM   1682  C  CD2  . LEU   A  1  111 ? 5.577   -27.903 -25.672  1.00 39.75  ? 111  LEU   A CD2  1 
ATOM   1683  H  H    . LEU   A  1  111 ? 6.603   -25.168 -29.309  1.00 51.52  ? 111  LEU   A H    1 
ATOM   1684  H  HA   . LEU   A  1  111 ? 5.968   -27.606 -28.289  1.00 50.37  ? 111  LEU   A HA   1 
ATOM   1685  H  HB2  . LEU   A  1  111 ? 5.198   -25.078 -27.393  1.00 49.31  ? 111  LEU   A HB2  1 
ATOM   1686  H  HB3  . LEU   A  1  111 ? 4.189   -26.285 -27.169  1.00 49.31  ? 111  LEU   A HB3  1 
ATOM   1687  H  HG   . LEU   A  1  111 ? 6.843   -26.388 -26.224  1.00 51.58  ? 111  LEU   A HG   1 
ATOM   1688  H  HD11 . LEU   A  1  111 ? 6.081   -25.831 -24.097  1.00 52.14  ? 111  LEU   A HD11 1 
ATOM   1689  H  HD12 . LEU   A  1  111 ? 5.859   -24.629 -25.111  1.00 52.14  ? 111  LEU   A HD12 1 
ATOM   1690  H  HD13 . LEU   A  1  111 ? 4.636   -25.554 -24.696  1.00 52.14  ? 111  LEU   A HD13 1 
ATOM   1691  H  HD21 . LEU   A  1  111 ? 6.038   -28.128 -24.849  1.00 47.74  ? 111  LEU   A HD21 1 
ATOM   1692  H  HD22 . LEU   A  1  111 ? 4.619   -27.996 -25.551  1.00 47.74  ? 111  LEU   A HD22 1 
ATOM   1693  H  HD23 . LEU   A  1  111 ? 5.878   -28.483 -26.389  1.00 47.74  ? 111  LEU   A HD23 1 
ATOM   1694  N  N    . TYR   A  1  112 ? 4.868   -26.724 -30.848  1.00 48.32  ? 112  TYR   A N    1 
ATOM   1695  C  CA   . TYR   A  1  112 ? 3.975   -27.122 -31.924  1.00 48.61  ? 112  TYR   A CA   1 
ATOM   1696  C  C    . TYR   A  1  112 ? 3.791   -28.637 -31.917  1.00 52.18  ? 112  TYR   A C    1 
ATOM   1697  O  O    . TYR   A  1  112 ? 4.762   -29.388 -32.047  1.00 54.06  ? 112  TYR   A O    1 
ATOM   1698  C  CB   . TYR   A  1  112 ? 4.562   -26.643 -33.252  1.00 48.08  ? 112  TYR   A CB   1 
ATOM   1699  C  CG   . TYR   A  1  112 ? 4.028   -27.334 -34.479  1.00 45.79  ? 112  TYR   A CG   1 
ATOM   1700  C  CD1  . TYR   A  1  112 ? 2.933   -26.827 -35.160  1.00 44.95  ? 112  TYR   A CD1  1 
ATOM   1701  C  CD2  . TYR   A  1  112 ? 4.635   -28.482 -34.970  1.00 41.18  ? 112  TYR   A CD2  1 
ATOM   1702  C  CE1  . TYR   A  1  112 ? 2.448   -27.449 -36.288  1.00 41.73  ? 112  TYR   A CE1  1 
ATOM   1703  C  CE2  . TYR   A  1  112 ? 4.155   -29.114 -36.097  1.00 41.20  ? 112  TYR   A CE2  1 
ATOM   1704  C  CZ   . TYR   A  1  112 ? 3.061   -28.593 -36.753  1.00 40.92  ? 112  TYR   A CZ   1 
ATOM   1705  O  OH   . TYR   A  1  112 ? 2.577   -29.214 -37.879  1.00 44.17  ? 112  TYR   A OH   1 
ATOM   1706  H  H    . TYR   A  1  112 ? 5.602   -26.366 -31.119  1.00 58.02  ? 112  TYR   A H    1 
ATOM   1707  H  HA   . TYR   A  1  112 ? 3.100   -26.718 -31.809  1.00 58.37  ? 112  TYR   A HA   1 
ATOM   1708  H  HB2  . TYR   A  1  112 ? 4.372   -25.696 -33.346  1.00 57.73  ? 112  TYR   A HB2  1 
ATOM   1709  H  HB3  . TYR   A  1  112 ? 5.521   -26.788 -33.232  1.00 57.73  ? 112  TYR   A HB3  1 
ATOM   1710  H  HD1  . TYR   A  1  112 ? 2.519   -26.054 -34.850  1.00 53.98  ? 112  TYR   A HD1  1 
ATOM   1711  H  HD2  . TYR   A  1  112 ? 5.377   -28.831 -34.532  1.00 49.45  ? 112  TYR   A HD2  1 
ATOM   1712  H  HE1  . TYR   A  1  112 ? 1.711   -27.099 -36.735  1.00 50.11  ? 112  TYR   A HE1  1 
ATOM   1713  H  HE2  . TYR   A  1  112 ? 4.566   -29.886 -36.412  1.00 49.48  ? 112  TYR   A HE2  1 
ATOM   1714  H  HH   . TYR   A  1  112 ? 2.006   -28.725 -38.254  1.00 53.04  ? 112  TYR   A HH   1 
ATOM   1715  N  N    . HIS   A  1  113 ? 2.549   -29.085 -31.741  1.00 50.74  ? 113  HIS   A N    1 
ATOM   1716  C  CA   . HIS   A  1  113 ? 2.205   -30.498 -31.811  1.00 48.13  ? 113  HIS   A CA   1 
ATOM   1717  C  C    . HIS   A  1  113 ? 1.636   -30.836 -33.183  1.00 49.75  ? 113  HIS   A C    1 
ATOM   1718  O  O    . HIS   A  1  113 ? 1.162   -29.964 -33.916  1.00 55.31  ? 113  HIS   A O    1 
ATOM   1719  C  CB   . HIS   A  1  113 ? 1.174   -30.880 -30.746  1.00 48.59  ? 113  HIS   A CB   1 
ATOM   1720  C  CG   . HIS   A  1  113 ? 1.657   -30.719 -29.341  1.00 46.94  ? 113  HIS   A CG   1 
ATOM   1721  N  ND1  . HIS   A  1  113 ? 1.879   -29.487 -28.766  1.00 47.93  ? 113  HIS   A ND1  1 
ATOM   1722  C  CD2  . HIS   A  1  113 ? 1.938   -31.637 -28.386  1.00 47.83  ? 113  HIS   A CD2  1 
ATOM   1723  C  CE1  . HIS   A  1  113 ? 2.286   -29.653 -27.520  1.00 48.97  ? 113  HIS   A CE1  1 
ATOM   1724  N  NE2  . HIS   A  1  113 ? 2.329   -30.947 -27.266  1.00 48.31  ? 113  HIS   A NE2  1 
ATOM   1725  H  H    . HIS   A  1  113 ? 1.875   -28.576 -31.577  1.00 60.93  ? 113  HIS   A H    1 
ATOM   1726  H  HA   . HIS   A  1  113 ? 3.011   -31.016 -31.657  1.00 57.79  ? 113  HIS   A HA   1 
ATOM   1727  H  HB2  . HIS   A  1  113 ? 0.392   -30.317 -30.855  1.00 58.34  ? 113  HIS   A HB2  1 
ATOM   1728  H  HB3  . HIS   A  1  113 ? 0.932   -31.811 -30.869  1.00 58.34  ? 113  HIS   A HB3  1 
ATOM   1729  H  HD1  . HIS   A  1  113 ? 1.770   -28.729 -29.157  1.00 57.55  ? 113  HIS   A HD1  1 
ATOM   1730  H  HD2  . HIS   A  1  113 ? 1.878   -32.561 -28.474  1.00 57.43  ? 113  HIS   A HD2  1 
ATOM   1731  H  HE1  . HIS   A  1  113 ? 2.506   -28.973 -26.925  1.00 58.80  ? 113  HIS   A HE1  1 
ATOM   1732  N  N    . TRP   A  1  114 ? 1.665   -32.123 -33.516  1.00 46.53  ? 114  TRP   A N    1 
ATOM   1733  C  CA   . TRP   A  1  114 ? 1.042   -32.578 -34.750  1.00 50.67  ? 114  TRP   A CA   1 
ATOM   1734  C  C    . TRP   A  1  114 ? 0.525   -33.998 -34.567  1.00 50.23  ? 114  TRP   A C    1 
ATOM   1735  O  O    . TRP   A  1  114 ? 0.860   -34.694 -33.606  1.00 48.84  ? 114  TRP   A O    1 
ATOM   1736  C  CB   . TRP   A  1  114 ? 2.012   -32.446 -35.931  1.00 53.67  ? 114  TRP   A CB   1 
ATOM   1737  C  CG   . TRP   A  1  114 ? 2.741   -33.683 -36.343  1.00 53.29  ? 114  TRP   A CG   1 
ATOM   1738  C  CD1  . TRP   A  1  114 ? 3.602   -34.428 -35.590  1.00 56.45  ? 114  TRP   A CD1  1 
ATOM   1739  C  CD2  . TRP   A  1  114 ? 2.706   -34.296 -37.637  1.00 54.43  ? 114  TRP   A CD2  1 
ATOM   1740  N  NE1  . TRP   A  1  114 ? 4.093   -35.477 -36.333  1.00 58.87  ? 114  TRP   A NE1  1 
ATOM   1741  C  CE2  . TRP   A  1  114 ? 3.556   -35.417 -37.593  1.00 56.69  ? 114  TRP   A CE2  1 
ATOM   1742  C  CE3  . TRP   A  1  114 ? 2.029   -34.008 -38.827  1.00 61.55  ? 114  TRP   A CE3  1 
ATOM   1743  C  CZ2  . TRP   A  1  114 ? 3.751   -36.250 -38.694  1.00 62.30  ? 114  TRP   A CZ2  1 
ATOM   1744  C  CZ3  . TRP   A  1  114 ? 2.218   -34.837 -39.917  1.00 66.50  ? 114  TRP   A CZ3  1 
ATOM   1745  C  CH2  . TRP   A  1  114 ? 3.071   -35.945 -39.843  1.00 67.46  ? 114  TRP   A CH2  1 
ATOM   1746  H  H    . TRP   A  1  114 ? 2.036   -32.743 -33.049  1.00 55.88  ? 114  TRP   A H    1 
ATOM   1747  H  HA   . TRP   A  1  114 ? 0.265   -32.031 -34.945  1.00 60.84  ? 114  TRP   A HA   1 
ATOM   1748  H  HB2  . TRP   A  1  114 ? 1.506   -32.145 -36.702  1.00 64.44  ? 114  TRP   A HB2  1 
ATOM   1749  H  HB3  . TRP   A  1  114 ? 2.683   -31.786 -35.696  1.00 64.44  ? 114  TRP   A HB3  1 
ATOM   1750  H  HD1  . TRP   A  1  114 ? 3.825   -34.251 -34.704  1.00 67.78  ? 114  TRP   A HD1  1 
ATOM   1751  H  HE1  . TRP   A  1  114 ? 4.645   -36.073 -36.052  1.00 70.68  ? 114  TRP   A HE1  1 
ATOM   1752  H  HE3  . TRP   A  1  114 ? 1.463   -33.272 -38.884  1.00 73.89  ? 114  TRP   A HE3  1 
ATOM   1753  H  HZ2  . TRP   A  1  114 ? 4.320   -36.984 -38.650  1.00 74.79  ? 114  TRP   A HZ2  1 
ATOM   1754  H  HZ3  . TRP   A  1  114 ? 1.772   -34.656 -40.712  1.00 79.84  ? 114  TRP   A HZ3  1 
ATOM   1755  H  HH2  . TRP   A  1  114 ? 3.178   -36.487 -40.592  1.00 80.99  ? 114  TRP   A HH2  1 
ATOM   1756  N  N    . ARG   A  1  115 ? -0.315  -34.410 -35.517  1.00 49.60  ? 115  ARG   A N    1 
ATOM   1757  C  CA   . ARG   A  1  115 ? -1.159  -35.591 -35.383  1.00 50.68  ? 115  ARG   A CA   1 
ATOM   1758  C  C    . ARG   A  1  115 ? -0.505  -36.867 -35.887  1.00 51.88  ? 115  ARG   A C    1 
ATOM   1759  O  O    . ARG   A  1  115 ? -0.816  -37.949 -35.376  1.00 57.19  ? 115  ARG   A O    1 
ATOM   1760  C  CB   . ARG   A  1  115 ? -2.468  -35.361 -36.153  1.00 52.00  ? 115  ARG   A CB   1 
ATOM   1761  C  CG   . ARG   A  1  115 ? -3.401  -36.566 -36.276  1.00 51.50  ? 115  ARG   A CG   1 
ATOM   1762  C  CD   . ARG   A  1  115 ? -4.369  -36.358 -37.433  1.00 54.06  ? 115  ARG   A CD   1 
ATOM   1763  N  NE   . ARG   A  1  115 ? -5.449  -37.342 -37.465  1.00 56.01  ? 115  ARG   A NE   1 
ATOM   1764  C  CZ   . ARG   A  1  115 ? -5.345  -38.560 -37.989  1.00 57.35  ? 115  ARG   A CZ   1 
ATOM   1765  N  NH1  . ARG   A  1  115 ? -4.200  -38.969 -38.520  1.00 58.75  ? 115  ARG   A NH1  1 
ATOM   1766  N  NH2  . ARG   A  1  115 ? -6.391  -39.375 -37.974  1.00 56.26  ? 115  ARG   A NH2  1 
ATOM   1767  H  H    . ARG   A  1  115 ? -0.416  -34.009 -36.271  1.00 59.56  ? 115  ARG   A H    1 
ATOM   1768  H  HA   . ARG   A  1  115 ? -1.360  -35.724 -34.444  1.00 60.85  ? 115  ARG   A HA   1 
ATOM   1769  H  HB2  . ARG   A  1  115 ? -2.965  -34.661 -35.701  1.00 62.44  ? 115  ARG   A HB2  1 
ATOM   1770  H  HB3  . ARG   A  1  115 ? -2.243  -35.081 -37.054  1.00 62.44  ? 115  ARG   A HB3  1 
ATOM   1771  H  HG2  . ARG   A  1  115 ? -2.880  -37.367 -36.445  1.00 61.84  ? 115  ARG   A HG2  1 
ATOM   1772  H  HG3  . ARG   A  1  115 ? -3.911  -36.669 -35.457  1.00 61.84  ? 115  ARG   A HG3  1 
ATOM   1773  H  HD2  . ARG   A  1  115 ? -4.770  -35.479 -37.353  1.00 64.91  ? 115  ARG   A HD2  1 
ATOM   1774  H  HD3  . ARG   A  1  115 ? -3.880  -36.426 -38.268  1.00 64.91  ? 115  ARG   A HD3  1 
ATOM   1775  H  HE   . ARG   A  1  115 ? -6.204  -37.117 -37.122  1.00 67.25  ? 115  ARG   A HE   1 
ATOM   1776  H  HH11 . ARG   A  1  115 ? -3.518  -38.446 -38.528  1.00 70.53  ? 115  ARG   A HH11 1 
ATOM   1777  H  HH12 . ARG   A  1  115 ? -4.141  -39.758 -38.857  1.00 70.53  ? 115  ARG   A HH12 1 
ATOM   1778  H  HH21 . ARG   A  1  115 ? -7.133  -39.116 -37.626  1.00 67.55  ? 115  ARG   A HH21 1 
ATOM   1779  H  HH22 . ARG   A  1  115 ? -6.326  -40.163 -38.312  1.00 67.55  ? 115  ARG   A HH22 1 
ATOM   1780  N  N    . THR   A  1  116 ? 0.392   -36.767 -36.867  1.00 50.73  ? 116  THR   A N    1 
ATOM   1781  C  CA   . THR   A  1  116 ? 0.853   -37.917 -37.637  1.00 52.66  ? 116  THR   A CA   1 
ATOM   1782  C  C    . THR   A  1  116 ? -0.258  -38.337 -38.592  1.00 58.43  ? 116  THR   A C    1 
ATOM   1783  O  O    . THR   A  1  116 ? -1.432  -38.025 -38.361  1.00 55.78  ? 116  THR   A O    1 
ATOM   1784  C  CB   . THR   A  1  116 ? 1.258   -39.100 -36.749  1.00 51.49  ? 116  THR   A CB   1 
ATOM   1785  O  OG1  . THR   A  1  116 ? 0.088   -39.783 -36.278  1.00 52.26  ? 116  THR   A OG1  1 
ATOM   1786  C  CG2  . THR   A  1  116 ? 2.104   -38.639 -35.562  1.00 45.89  ? 116  THR   A CG2  1 
ATOM   1787  H  H    . THR   A  1  116 ? 0.755   -36.026 -37.110  1.00 60.91  ? 116  THR   A H    1 
ATOM   1788  H  HA   . THR   A  1  116 ? 1.651   -37.668 -38.129  1.00 63.22  ? 116  THR   A HA   1 
ATOM   1789  H  HB   . THR   A  1  116 ? 1.796   -39.715 -37.271  1.00 61.82  ? 116  THR   A HB   1 
ATOM   1790  H  HG1  . THR   A  1  116 ? -0.248  -39.365 -35.632  1.00 62.75  ? 116  THR   A HG1  1 
ATOM   1791  H  HG21 . THR   A  1  116 ? 2.366   -39.403 -35.025  1.00 55.11  ? 116  THR   A HG21 1 
ATOM   1792  H  HG22 . THR   A  1  116 ? 2.902   -38.188 -35.878  1.00 55.11  ? 116  THR   A HG22 1 
ATOM   1793  H  HG23 . THR   A  1  116 ? 1.594   -38.027 -35.009  1.00 55.11  ? 116  THR   A HG23 1 
ATOM   1794  N  N    . GLU   A  1  117 ? 0.098   -39.039 -39.664  1.00 65.29  ? 117  GLU   A N    1 
ATOM   1795  C  CA   . GLU   A  1  117 ? -0.868  -39.408 -40.689  1.00 68.80  ? 117  GLU   A CA   1 
ATOM   1796  C  C    . GLU   A  1  117 ? -1.561  -40.736 -40.421  1.00 70.30  ? 117  GLU   A C    1 
ATOM   1797  O  O    . GLU   A  1  117 ? -2.535  -41.054 -41.111  1.00 75.51  ? 117  GLU   A O    1 
ATOM   1798  C  CB   . GLU   A  1  117 ? -0.185  -39.474 -42.056  1.00 74.33  ? 117  GLU   A CB   1 
ATOM   1799  C  CG   . GLU   A  1  117 ? -0.229  -38.173 -42.825  1.00 80.00  ? 117  GLU   A CG   1 
ATOM   1800  C  CD   . GLU   A  1  117 ? 0.192   -38.347 -44.268  1.00 87.10  ? 117  GLU   A CD   1 
ATOM   1801  O  OE1  . GLU   A  1  117 ? 1.244   -38.976 -44.508  1.00 87.84  ? 117  GLU   A OE1  1 
ATOM   1802  O  OE2  . GLU   A  1  117 ? -0.538  -37.869 -45.161  1.00 89.30  ? 117  GLU   A OE2  1 
ATOM   1803  H  H    . GLU   A  1  117 ? 0.897   -39.314 -39.820  1.00 78.39  ? 117  GLU   A H    1 
ATOM   1804  H  HA   . GLU   A  1  117 ? -1.551  -38.720 -40.720  1.00 82.59  ? 117  GLU   A HA   1 
ATOM   1805  H  HB2  . GLU   A  1  117 ? 0.747   -39.710 -41.927  1.00 89.23  ? 117  GLU   A HB2  1 
ATOM   1806  H  HB3  . GLU   A  1  117 ? -0.627  -40.150 -42.593  1.00 89.23  ? 117  GLU   A HB3  1 
ATOM   1807  H  HG2  . GLU   A  1  117 ? -1.136  -37.828 -42.815  1.00 96.04  ? 117  GLU   A HG2  1 
ATOM   1808  H  HG3  . GLU   A  1  117 ? 0.373   -37.537 -42.409  1.00 96.04  ? 117  GLU   A HG3  1 
ATOM   1809  N  N    . MET   A  1  118 ? -1.092  -41.514 -39.449  1.00 70.52  ? 118  MET   A N    1 
ATOM   1810  C  CA   . MET   A  1  118 ? -1.673  -42.826 -39.191  1.00 76.80  ? 118  MET   A CA   1 
ATOM   1811  C  C    . MET   A  1  118 ? -2.699  -42.742 -38.066  1.00 80.29  ? 118  MET   A C    1 
ATOM   1812  O  O    . MET   A  1  118 ? -3.905  -42.698 -38.328  1.00 84.51  ? 118  MET   A O    1 
ATOM   1813  C  CB   . MET   A  1  118 ? -0.564  -43.831 -38.875  1.00 80.50  ? 118  MET   A CB   1 
ATOM   1814  C  CG   . MET   A  1  118 ? 0.475   -43.950 -39.994  1.00 82.17  ? 118  MET   A CG   1 
ATOM   1815  S  SD   . MET   A  1  118 ? -0.241  -44.500 -41.560  1.00 85.35  ? 118  MET   A SD   1 
ATOM   1816  C  CE   . MET   A  1  118 ? 0.979   -43.928 -42.744  1.00 86.34  ? 118  MET   A CE   1 
ATOM   1817  H  H    . MET   A  1  118 ? -0.441  -41.305 -38.928  1.00 84.66  ? 118  MET   A H    1 
ATOM   1818  H  HA   . MET   A  1  118 ? -2.131  -43.145 -39.985  1.00 92.19  ? 118  MET   A HA   1 
ATOM   1819  H  HB2  . MET   A  1  118 ? -0.104  -43.549 -38.069  1.00 96.64  ? 118  MET   A HB2  1 
ATOM   1820  H  HB3  . MET   A  1  118 ? -0.961  -44.706 -38.742  1.00 96.64  ? 118  MET   A HB3  1 
ATOM   1821  H  HG2  . MET   A  1  118 ? 0.883   -43.082 -40.140  1.00 98.65  ? 118  MET   A HG2  1 
ATOM   1822  H  HG3  . MET   A  1  118 ? 1.151   -44.594 -39.731  1.00 98.65  ? 118  MET   A HG3  1 
ATOM   1823  H  HE1  . MET   A  1  118 ? 0.716   -44.215 -43.632  1.00 103.65 ? 118  MET   A HE1  1 
ATOM   1824  H  HE2  . MET   A  1  118 ? 1.024   -42.960 -42.708  1.00 103.65 ? 118  MET   A HE2  1 
ATOM   1825  H  HE3  . MET   A  1  118 ? 1.842   -44.308 -42.516  1.00 103.65 ? 118  MET   A HE3  1 
ATOM   1826  N  N    . LYS   A  1  119 ? -2.242  -42.705 -36.818  1.00 81.42  ? 119  LYS   A N    1 
ATOM   1827  C  CA   . LYS   A  1  119 ? -3.139  -42.615 -35.675  1.00 83.12  ? 119  LYS   A CA   1 
ATOM   1828  C  C    . LYS   A  1  119 ? -3.391  -41.158 -35.294  1.00 80.41  ? 119  LYS   A C    1 
ATOM   1829  O  O    . LYS   A  1  119 ? -2.679  -40.245 -35.719  1.00 79.22  ? 119  LYS   A O    1 
ATOM   1830  C  CB   . LYS   A  1  119 ? -2.559  -43.370 -34.476  1.00 88.13  ? 119  LYS   A CB   1 
ATOM   1831  C  CG   . LYS   A  1  119 ? -2.451  -44.874 -34.675  1.00 97.49  ? 119  LYS   A CG   1 
ATOM   1832  C  CD   . LYS   A  1  119 ? -1.822  -45.557 -33.467  1.00 105.26 ? 119  LYS   A CD   1 
ATOM   1833  C  CE   . LYS   A  1  119 ? -1.774  -47.067 -33.648  1.00 114.76 ? 119  LYS   A CE   1 
ATOM   1834  N  NZ   . LYS   A  1  119 ? -1.163  -47.768 -32.484  1.00 119.26 ? 119  LYS   A NZ   1 
ATOM   1835  H  H    . LYS   A  1  119 ? -1.409  -42.730 -36.608  1.00 97.74  ? 119  LYS   A H    1 
ATOM   1836  H  HA   . LYS   A  1  119 ? -3.989  -43.019 -35.909  1.00 99.78  ? 119  LYS   A HA   1 
ATOM   1837  H  HB2  . LYS   A  1  119 ? -1.667  -43.032 -34.300  1.00 105.79 ? 119  LYS   A HB2  1 
ATOM   1838  H  HB3  . LYS   A  1  119 ? -3.130  -43.215 -33.708  1.00 105.79 ? 119  LYS   A HB3  1 
ATOM   1839  H  HG2  . LYS   A  1  119 ? -3.338  -45.244 -34.807  1.00 117.03 ? 119  LYS   A HG2  1 
ATOM   1840  H  HG3  . LYS   A  1  119 ? -1.897  -45.056 -35.450  1.00 117.03 ? 119  LYS   A HG3  1 
ATOM   1841  H  HD2  . LYS   A  1  119 ? -0.915  -45.234 -33.350  1.00 126.35 ? 119  LYS   A HD2  1 
ATOM   1842  H  HD3  . LYS   A  1  119 ? -2.349  -45.360 -32.676  1.00 126.35 ? 119  LYS   A HD3  1 
ATOM   1843  H  HE2  . LYS   A  1  119 ? -2.678  -47.401 -33.758  1.00 137.74 ? 119  LYS   A HE2  1 
ATOM   1844  H  HE3  . LYS   A  1  119 ? -1.245  -47.274 -34.434  1.00 137.74 ? 119  LYS   A HE3  1 
ATOM   1845  H  HZ1  . LYS   A  1  119 ? -1.137  -48.645 -32.636  1.00 143.15 ? 119  LYS   A HZ1  1 
ATOM   1846  H  HZ2  . LYS   A  1  119 ? -0.333  -47.473 -32.352  1.00 143.15 ? 119  LYS   A HZ2  1 
ATOM   1847  H  HZ3  . LYS   A  1  119 ? -1.643  -47.616 -31.750  1.00 143.15 ? 119  LYS   A HZ3  1 
ATOM   1848  N  N    . GLN   A  1  120 ? -4.426  -40.951 -34.481  1.00 79.79  ? 120  GLN   A N    1 
ATOM   1849  C  CA   . GLN   A  1  120 ? -4.721  -39.634 -33.916  1.00 76.75  ? 120  GLN   A CA   1 
ATOM   1850  C  C    . GLN   A  1  120 ? -3.803  -39.413 -32.723  1.00 72.26  ? 120  GLN   A C    1 
ATOM   1851  O  O    . GLN   A  1  120 ? -4.067  -39.902 -31.622  1.00 75.65  ? 120  GLN   A O    1 
ATOM   1852  C  CB   . GLN   A  1  120 ? -6.181  -39.530 -33.492  1.00 81.47  ? 120  GLN   A CB   1 
ATOM   1853  C  CG   . GLN   A  1  120 ? -7.189  -39.476 -34.623  1.00 87.76  ? 120  GLN   A CG   1 
ATOM   1854  C  CD   . GLN   A  1  120 ? -8.612  -39.376 -34.106  1.00 94.09  ? 120  GLN   A CD   1 
ATOM   1855  O  OE1  . GLN   A  1  120 ? -8.873  -39.626 -32.930  1.00 94.28  ? 120  GLN   A OE1  1 
ATOM   1856  N  NE2  . GLN   A  1  120 ? -9.537  -39.002 -34.981  1.00 103.55 ? 120  GLN   A NE2  1 
ATOM   1857  H  H    . GLN   A  1  120 ? -4.979  -41.563 -34.238  1.00 95.79  ? 120  GLN   A H    1 
ATOM   1858  H  HA   . GLN   A  1  120 ? -4.548  -38.958 -34.590  1.00 92.13  ? 120  GLN   A HA   1 
ATOM   1859  H  HB2  . GLN   A  1  120 ? -6.397  -40.304 -32.949  1.00 97.80  ? 120  GLN   A HB2  1 
ATOM   1860  H  HB3  . GLN   A  1  120 ? -6.289  -38.719 -32.970  1.00 97.80  ? 120  GLN   A HB3  1 
ATOM   1861  H  HG2  . GLN   A  1  120 ? -7.010  -38.698 -35.174  1.00 105.34 ? 120  GLN   A HG2  1 
ATOM   1862  H  HG3  . GLN   A  1  120 ? -7.115  -40.283 -35.156  1.00 105.34 ? 120  GLN   A HG3  1 
ATOM   1863  H  HE21 . GLN   A  1  120 ? -9.316  -38.831 -35.794  1.00 124.30 ? 120  GLN   A HE21 1 
ATOM   1864  H  HE22 . GLN   A  1  120 ? -10.358 -38.931 -34.734  1.00 124.30 ? 120  GLN   A HE22 1 
ATOM   1865  N  N    . GLU   A  1  121 ? -2.724  -38.671 -32.933  1.00 67.10  ? 121  GLU   A N    1 
ATOM   1866  C  CA   . GLU   A  1  121 ? -1.756  -38.376 -31.888  1.00 57.93  ? 121  GLU   A CA   1 
ATOM   1867  C  C    . GLU   A  1  121 ? -1.661  -36.866 -31.692  1.00 51.36  ? 121  GLU   A C    1 
ATOM   1868  O  O    . GLU   A  1  121 ? -2.362  -36.084 -32.338  1.00 51.56  ? 121  GLU   A O    1 
ATOM   1869  C  CB   . GLU   A  1  121 ? -0.387  -38.971 -32.233  1.00 53.74  ? 121  GLU   A CB   1 
ATOM   1870  C  CG   . GLU   A  1  121 ? -0.398  -40.481 -32.411  1.00 57.59  ? 121  GLU   A CG   1 
ATOM   1871  C  CD   . GLU   A  1  121 ? -0.635  -41.223 -31.110  1.00 68.50  ? 121  GLU   A CD   1 
ATOM   1872  O  OE1  . GLU   A  1  121 ? -0.438  -40.619 -30.034  1.00 72.58  ? 121  GLU   A OE1  1 
ATOM   1873  O  OE2  . GLU   A  1  121 ? -1.019  -42.410 -31.162  1.00 74.76  ? 121  GLU   A OE2  1 
ATOM   1874  H  H    . GLU   A  1  121 ? -2.528  -38.318 -33.692  1.00 80.56  ? 121  GLU   A H    1 
ATOM   1875  H  HA   . GLU   A  1  121 ? -2.058  -38.772 -31.056  1.00 69.56  ? 121  GLU   A HA   1 
ATOM   1876  H  HB2  . GLU   A  1  121 ? -0.077  -38.578 -33.063  1.00 64.52  ? 121  GLU   A HB2  1 
ATOM   1877  H  HB3  . GLU   A  1  121 ? 0.232   -38.763 -31.516  1.00 64.52  ? 121  GLU   A HB3  1 
ATOM   1878  H  HG2  . GLU   A  1  121 ? -1.107  -40.722 -33.027  1.00 69.14  ? 121  GLU   A HG2  1 
ATOM   1879  H  HG3  . GLU   A  1  121 ? 0.460   -40.764 -32.765  1.00 69.14  ? 121  GLU   A HG3  1 
ATOM   1880  N  N    . ARG   A  1  122 ? -0.780  -36.464 -30.773  1.00 49.43  ? 122  ARG   A N    1 
ATOM   1881  C  CA   . ARG   A  1  122 ? -0.512  -35.053 -30.500  1.00 48.56  ? 122  ARG   A CA   1 
ATOM   1882  C  C    . ARG   A  1  122 ? 0.937   -34.980 -30.010  1.00 45.04  ? 122  ARG   A C    1 
ATOM   1883  O  O    . ARG   A  1  122 ? 1.222   -34.878 -28.814  1.00 46.28  ? 122  ARG   A O    1 
ATOM   1884  C  CB   . ARG   A  1  122 ? -1.487  -34.465 -29.481  1.00 56.21  ? 122  ARG   A CB   1 
ATOM   1885  C  CG   . ARG   A  1  122 ? -1.441  -32.953 -29.420  1.00 63.87  ? 122  ARG   A CG   1 
ATOM   1886  C  CD   . ARG   A  1  122 ? -2.425  -32.375 -28.419  1.00 68.23  ? 122  ARG   A CD   1 
ATOM   1887  N  NE   . ARG   A  1  122 ? -2.361  -30.916 -28.417  1.00 69.26  ? 122  ARG   A NE   1 
ATOM   1888  C  CZ   . ARG   A  1  122 ? -1.616  -30.189 -27.588  1.00 67.89  ? 122  ARG   A CZ   1 
ATOM   1889  N  NH1  . ARG   A  1  122 ? -0.863  -30.773 -26.664  1.00 67.06  ? 122  ARG   A NH1  1 
ATOM   1890  N  NH2  . ARG   A  1  122 ? -1.628  -28.867 -27.682  1.00 67.30  ? 122  ARG   A NH2  1 
ATOM   1891  H  H    . ARG   A  1  122 ? -0.316  -37.000 -30.286  1.00 59.36  ? 122  ARG   A H    1 
ATOM   1892  H  HA   . ARG   A  1  122 ? -0.596  -34.535 -31.316  1.00 58.31  ? 122  ARG   A HA   1 
ATOM   1893  H  HB2  . ARG   A  1  122 ? -2.389  -34.727 -29.722  1.00 67.49  ? 122  ARG   A HB2  1 
ATOM   1894  H  HB3  . ARG   A  1  122 ? -1.266  -34.807 -28.601  1.00 67.49  ? 122  ARG   A HB3  1 
ATOM   1895  H  HG2  . ARG   A  1  122 ? -0.549  -32.674 -29.158  1.00 76.68  ? 122  ARG   A HG2  1 
ATOM   1896  H  HG3  . ARG   A  1  122 ? -1.658  -32.594 -30.294  1.00 76.68  ? 122  ARG   A HG3  1 
ATOM   1897  H  HD2  . ARG   A  1  122 ? -3.326  -32.645 -28.657  1.00 81.91  ? 122  ARG   A HD2  1 
ATOM   1898  H  HD3  . ARG   A  1  122 ? -2.208  -32.695 -27.529  1.00 81.91  ? 122  ARG   A HD3  1 
ATOM   1899  H  HE   . ARG   A  1  122 ? -2.841  -30.495 -28.995  1.00 83.15  ? 122  ARG   A HE   1 
ATOM   1900  H  HH11 . ARG   A  1  122 ? -0.854  -31.630 -26.595  1.00 80.51  ? 122  ARG   A HH11 1 
ATOM   1901  H  HH12 . ARG   A  1  122 ? -0.385  -30.294 -26.133  1.00 80.51  ? 122  ARG   A HH12 1 
ATOM   1902  H  HH21 . ARG   A  1  122 ? -2.116  -28.482 -28.277  1.00 80.80  ? 122  ARG   A HH21 1 
ATOM   1903  H  HH22 . ARG   A  1  122 ? -1.147  -28.394 -27.149  1.00 80.80  ? 122  ARG   A HH22 1 
ATOM   1904  N  N    . GLU   A  1  123 ? 1.867   -35.032 -30.961  1.00 41.32  ? 123  GLU   A N    1 
ATOM   1905  C  CA   . GLU   A  1  123 ? 3.278   -35.214 -30.652  1.00 42.71  ? 123  GLU   A CA   1 
ATOM   1906  C  C    . GLU   A  1  123 ? 4.033   -33.910 -30.849  1.00 43.60  ? 123  GLU   A C    1 
ATOM   1907  O  O    . GLU   A  1  123 ? 4.044   -33.372 -31.966  1.00 43.88  ? 123  GLU   A O    1 
ATOM   1908  C  CB   . GLU   A  1  123 ? 3.868   -36.318 -31.530  1.00 46.64  ? 123  GLU   A CB   1 
ATOM   1909  C  CG   . GLU   A  1  123 ? 3.186   -37.664 -31.330  1.00 51.56  ? 123  GLU   A CG   1 
ATOM   1910  C  CD   . GLU   A  1  123 ? 3.938   -38.811 -31.975  1.00 54.51  ? 123  GLU   A CD   1 
ATOM   1911  O  OE1  . GLU   A  1  123 ? 4.833   -38.547 -32.806  1.00 54.80  ? 123  GLU   A OE1  1 
ATOM   1912  O  OE2  . GLU   A  1  123 ? 3.634   -39.978 -31.648  1.00 53.62  ? 123  GLU   A OE2  1 
ATOM   1913  H  H    . GLU   A  1  123 ? 1.701   -34.964 -31.803  1.00 49.63  ? 123  GLU   A H    1 
ATOM   1914  H  HA   . GLU   A  1  123 ? 3.371   -35.470 -29.721  1.00 51.29  ? 123  GLU   A HA   1 
ATOM   1915  H  HB2  . GLU   A  1  123 ? 3.767   -36.066 -32.461  1.00 56.00  ? 123  GLU   A HB2  1 
ATOM   1916  H  HB3  . GLU   A  1  123 ? 4.808   -36.423 -31.314  1.00 56.00  ? 123  GLU   A HB3  1 
ATOM   1917  H  HG2  . GLU   A  1  123 ? 3.122   -37.846 -30.379  1.00 61.91  ? 123  GLU   A HG2  1 
ATOM   1918  H  HG3  . GLU   A  1  123 ? 2.300   -37.630 -31.722  1.00 61.91  ? 123  GLU   A HG3  1 
ATOM   1919  N  N    . PRO   A  1  124 ? 4.682   -33.366 -29.810  1.00 44.11  ? 124  PRO   A N    1 
ATOM   1920  C  CA   . PRO   A  1  124 ? 5.369   -32.064 -29.941  1.00 40.77  ? 124  PRO   A CA   1 
ATOM   1921  C  C    . PRO   A  1  124 ? 6.692   -32.175 -30.689  1.00 39.29  ? 124  PRO   A C    1 
ATOM   1922  O  O    . PRO   A  1  124 ? 7.789   -32.109 -30.123  1.00 40.91  ? 124  PRO   A O    1 
ATOM   1923  C  CB   . PRO   A  1  124 ? 5.549   -31.644 -28.478  1.00 44.09  ? 124  PRO   A CB   1 
ATOM   1924  C  CG   . PRO   A  1  124 ? 5.718   -32.934 -27.751  1.00 42.83  ? 124  PRO   A CG   1 
ATOM   1925  C  CD   . PRO   A  1  124 ? 4.825   -33.925 -28.452  1.00 43.19  ? 124  PRO   A CD   1 
ATOM   1926  H  HA   . PRO   A  1  124 ? 4.795   -31.427 -30.395  1.00 48.96  ? 124  PRO   A HA   1 
ATOM   1927  H  HB2  . PRO   A  1  124 ? 6.336   -31.084 -28.385  1.00 52.95  ? 124  PRO   A HB2  1 
ATOM   1928  H  HB3  . PRO   A  1  124 ? 4.764   -31.167 -28.168  1.00 52.95  ? 124  PRO   A HB3  1 
ATOM   1929  H  HG2  . PRO   A  1  124 ? 6.645   -33.215 -27.796  1.00 51.43  ? 124  PRO   A HG2  1 
ATOM   1930  H  HG3  . PRO   A  1  124 ? 5.449   -32.824 -26.826  1.00 51.43  ? 124  PRO   A HG3  1 
ATOM   1931  H  HD2  . PRO   A  1  124 ? 5.241   -34.801 -28.482  1.00 51.86  ? 124  PRO   A HD2  1 
ATOM   1932  H  HD3  . PRO   A  1  124 ? 3.962   -33.982 -28.011  1.00 51.86  ? 124  PRO   A HD3  1 
ATOM   1933  N  N    . VAL   A  1  125 ? 6.599   -32.348 -32.010  1.00 37.81  ? 125  VAL   A N    1 
ATOM   1934  C  CA   . VAL   A  1  125 ? 7.799   -32.420 -32.831  1.00 37.89  ? 125  VAL   A CA   1 
ATOM   1935  C  C    . VAL   A  1  125 ? 8.447   -31.053 -32.997  1.00 40.05  ? 125  VAL   A C    1 
ATOM   1936  O  O    . VAL   A  1  125 ? 9.639   -30.971 -33.315  1.00 43.21  ? 125  VAL   A O    1 
ATOM   1937  C  CB   . VAL   A  1  125 ? 7.484   -33.021 -34.214  1.00 41.49  ? 125  VAL   A CB   1 
ATOM   1938  C  CG1  . VAL   A  1  125 ? 6.974   -34.445 -34.071  1.00 45.98  ? 125  VAL   A CG1  1 
ATOM   1939  C  CG2  . VAL   A  1  125 ? 6.475   -32.155 -34.961  1.00 39.78  ? 125  VAL   A CG2  1 
ATOM   1940  H  H    . VAL   A  1  125 ? 5.861   -32.426 -32.445  1.00 45.41  ? 125  VAL   A H    1 
ATOM   1941  H  HA   . VAL   A  1  125 ? 8.427   -33.006 -32.380  1.00 45.51  ? 125  VAL   A HA   1 
ATOM   1942  H  HB   . VAL   A  1  125 ? 8.299   -33.046 -34.738  1.00 49.83  ? 125  VAL   A HB   1 
ATOM   1943  H  HG11 . VAL   A  1  125 ? 6.811   -34.813 -34.953  1.00 55.21  ? 125  VAL   A HG11 1 
ATOM   1944  H  HG12 . VAL   A  1  125 ? 7.643   -34.975 -33.610  1.00 55.21  ? 125  VAL   A HG12 1 
ATOM   1945  H  HG13 . VAL   A  1  125 ? 6.150   -34.436 -33.559  1.00 55.21  ? 125  VAL   A HG13 1 
ATOM   1946  H  HG21 . VAL   A  1  125 ? 6.310   -32.544 -35.834  1.00 47.77  ? 125  VAL   A HG21 1 
ATOM   1947  H  HG22 . VAL   A  1  125 ? 5.649   -32.121 -34.452  1.00 47.77  ? 125  VAL   A HG22 1 
ATOM   1948  H  HG23 . VAL   A  1  125 ? 6.838   -31.261 -35.060  1.00 47.77  ? 125  VAL   A HG23 1 
ATOM   1949  N  N    . GLY   A  1  126 ? 7.693   -29.977 -32.794  1.00 43.66  ? 126  GLY   A N    1 
ATOM   1950  C  CA   . GLY   A  1  126 ? 8.213   -28.641 -32.999  1.00 47.23  ? 126  GLY   A CA   1 
ATOM   1951  C  C    . GLY   A  1  126 ? 8.304   -28.281 -34.467  1.00 50.57  ? 126  GLY   A C    1 
ATOM   1952  O  O    . GLY   A  1  126 ? 8.416   -29.163 -35.324  1.00 51.01  ? 126  GLY   A O    1 
ATOM   1953  H  H    . GLY   A  1  126 ? 6.873   -30.000 -32.536  1.00 52.43  ? 126  GLY   A H    1 
ATOM   1954  H  HA2  . GLY   A  1  126 ? 7.632   -28.000 -32.562  1.00 56.71  ? 126  GLY   A HA2  1 
ATOM   1955  H  HA3  . GLY   A  1  126 ? 9.100   -28.579 -32.612  1.00 56.71  ? 126  GLY   A HA3  1 
ATOM   1956  N  N    . THR   A  1  127 ? 8.250   -26.987 -34.770  1.00 46.82  ? 127  THR   A N    1 
ATOM   1957  C  CA   . THR   A  1  127 ? 8.391   -26.521 -36.140  1.00 43.83  ? 127  THR   A CA   1 
ATOM   1958  C  C    . THR   A  1  127 ? 9.125   -25.190 -36.131  1.00 42.39  ? 127  THR   A C    1 
ATOM   1959  O  O    . THR   A  1  127 ? 9.188   -24.497 -35.111  1.00 39.79  ? 127  THR   A O    1 
ATOM   1960  C  CB   . THR   A  1  127 ? 7.032   -26.372 -36.840  1.00 49.00  ? 127  THR   A CB   1 
ATOM   1961  O  OG1  . THR   A  1  127 ? 7.233   -26.220 -38.251  1.00 47.20  ? 127  THR   A OG1  1 
ATOM   1962  C  CG2  . THR   A  1  127 ? 6.270   -25.157 -36.309  1.00 49.12  ? 127  THR   A CG2  1 
ATOM   1963  H  H    . THR   A  1  127 ? 8.132   -26.358 -34.196  1.00 56.22  ? 127  THR   A H    1 
ATOM   1964  H  HA   . THR   A  1  127 ? 8.918   -27.164 -36.640  1.00 52.63  ? 127  THR   A HA   1 
ATOM   1965  H  HB   . THR   A  1  127 ? 6.498   -27.163 -36.667  1.00 58.84  ? 127  THR   A HB   1 
ATOM   1966  H  HG1  . THR   A  1  127 ? 6.494   -26.235 -38.650  1.00 56.67  ? 127  THR   A HG1  1 
ATOM   1967  H  HG21 . THR   A  1  127 ? 5.392   -25.111 -36.719  1.00 58.98  ? 127  THR   A HG21 1 
ATOM   1968  H  HG22 . THR   A  1  127 ? 6.165   -25.226 -35.348  1.00 58.98  ? 127  THR   A HG22 1 
ATOM   1969  H  HG23 . THR   A  1  127 ? 6.757   -24.344 -36.516  1.00 58.98  ? 127  THR   A HG23 1 
ATOM   1970  N  N    . CYS   A  1  128 ? 9.682   -24.842 -37.286  1.00 50.55  ? 128  CYS   A N    1 
ATOM   1971  C  CA   . CYS   A  1  128 ? 10.321  -23.555 -37.491  1.00 50.46  ? 128  CYS   A CA   1 
ATOM   1972  C  C    . CYS   A  1  128 ? 9.831   -22.957 -38.800  1.00 51.15  ? 128  CYS   A C    1 
ATOM   1973  O  O    . CYS   A  1  128 ? 9.311   -23.656 -39.674  1.00 51.47  ? 128  CYS   A O    1 
ATOM   1974  C  CB   . CYS   A  1  128 ? 11.851  -23.669 -37.525  1.00 51.83  ? 128  CYS   A CB   1 
ATOM   1975  S  SG   . CYS   A  1  128 ? 12.607  -24.349 -36.033  1.00 56.86  ? 128  CYS   A SG   1 
ATOM   1976  H  H    . CYS   A  1  128 ? 9.701   -25.350 -37.981  1.00 60.70  ? 128  CYS   A H    1 
ATOM   1977  H  HA   . CYS   A  1  128 ? 10.079  -22.962 -36.762  1.00 60.58  ? 128  CYS   A HA   1 
ATOM   1978  H  HB2  . CYS   A  1  128 ? 12.098  -24.247 -38.264  1.00 62.24  ? 128  CYS   A HB2  1 
ATOM   1979  H  HB3  . CYS   A  1  128 ? 12.221  -22.783 -37.659  1.00 62.24  ? 128  CYS   A HB3  1 
ATOM   1980  N  N    . PHE   A  1  129 ? 9.997   -21.645 -38.918  1.00 46.36  ? 129  PHE   A N    1 
ATOM   1981  C  CA   . PHE   A  1  129 ? 9.747   -20.935 -40.161  1.00 49.42  ? 129  PHE   A CA   1 
ATOM   1982  C  C    . PHE   A  1  129 ? 10.988  -20.142 -40.530  1.00 52.40  ? 129  PHE   A C    1 
ATOM   1983  O  O    . PHE   A  1  129 ? 11.587  -19.479 -39.675  1.00 50.97  ? 129  PHE   A O    1 
ATOM   1984  C  CB   . PHE   A  1  129 ? 8.534   -20.012 -40.050  1.00 52.23  ? 129  PHE   A CB   1 
ATOM   1985  C  CG   . PHE   A  1  129 ? 7.227   -20.743 -40.022  1.00 52.06  ? 129  PHE   A CG   1 
ATOM   1986  C  CD1  . PHE   A  1  129 ? 6.567   -21.052 -41.199  1.00 53.27  ? 129  PHE   A CD1  1 
ATOM   1987  C  CD2  . PHE   A  1  129 ? 6.664   -21.135 -38.819  1.00 50.04  ? 129  PHE   A CD2  1 
ATOM   1988  C  CE1  . PHE   A  1  129 ? 5.365   -21.731 -41.178  1.00 52.30  ? 129  PHE   A CE1  1 
ATOM   1989  C  CE2  . PHE   A  1  129 ? 5.463   -21.815 -38.791  1.00 47.00  ? 129  PHE   A CE2  1 
ATOM   1990  C  CZ   . PHE   A  1  129 ? 4.812   -22.114 -39.972  1.00 48.90  ? 129  PHE   A CZ   1 
ATOM   1991  H  H    . PHE   A  1  129 ? 10.260  -21.135 -38.277  1.00 55.67  ? 129  PHE   A H    1 
ATOM   1992  H  HA   . PHE   A  1  129 ? 9.567   -21.574 -40.869  1.00 59.34  ? 129  PHE   A HA   1 
ATOM   1993  H  HB2  . PHE   A  1  129 ? 8.606   -19.499 -39.230  1.00 62.72  ? 129  PHE   A HB2  1 
ATOM   1994  H  HB3  . PHE   A  1  129 ? 8.524   -19.415 -40.815  1.00 62.72  ? 129  PHE   A HB3  1 
ATOM   1995  H  HD1  . PHE   A  1  129 ? 6.937   -20.798 -42.013  1.00 63.96  ? 129  PHE   A HD1  1 
ATOM   1996  H  HD2  . PHE   A  1  129 ? 7.100   -20.939 -38.022  1.00 60.09  ? 129  PHE   A HD2  1 
ATOM   1997  H  HE1  . PHE   A  1  129 ? 4.929   -21.931 -41.974  1.00 62.80  ? 129  PHE   A HE1  1 
ATOM   1998  H  HE2  . PHE   A  1  129 ? 5.092   -22.071 -37.977  1.00 56.44  ? 129  PHE   A HE2  1 
ATOM   1999  H  HZ   . PHE   A  1  129 ? 4.004   -22.573 -39.955  1.00 58.71  ? 129  PHE   A HZ   1 
ATOM   2000  N  N    . LEU   A  1  130 ? 11.374  -20.228 -41.796  1.00 56.38  ? 130  LEU   A N    1 
ATOM   2001  C  CA   . LEU   A  1  130 ? 12.532  -19.520 -42.322  1.00 61.02  ? 130  LEU   A CA   1 
ATOM   2002  C  C    . LEU   A  1  130 ? 12.047  -18.530 -43.367  1.00 68.17  ? 130  LEU   A C    1 
ATOM   2003  O  O    . LEU   A  1  130 ? 11.423  -18.925 -44.357  1.00 63.83  ? 130  LEU   A O    1 
ATOM   2004  C  CB   . LEU   A  1  130 ? 13.545  -20.492 -42.928  1.00 56.72  ? 130  LEU   A CB   1 
ATOM   2005  C  CG   . LEU   A  1  130 ? 14.794  -19.845 -43.527  1.00 55.61  ? 130  LEU   A CG   1 
ATOM   2006  C  CD1  . LEU   A  1  130 ? 15.605  -19.144 -42.449  1.00 55.60  ? 130  LEU   A CD1  1 
ATOM   2007  C  CD2  . LEU   A  1  130 ? 15.639  -20.881 -44.248  1.00 56.94  ? 130  LEU   A CD2  1 
ATOM   2008  H  H    . LEU   A  1  130 ? 10.969  -20.703 -42.387  1.00 67.69  ? 130  LEU   A H    1 
ATOM   2009  H  HA   . LEU   A  1  130 ? 12.973  -19.033 -41.608  1.00 73.26  ? 130  LEU   A HA   1 
ATOM   2010  H  HB2  . LEU   A  1  130 ? 13.838  -21.100 -42.232  1.00 68.10  ? 130  LEU   A HB2  1 
ATOM   2011  H  HB3  . LEU   A  1  130 ? 13.106  -20.987 -43.637  1.00 68.10  ? 130  LEU   A HB3  1 
ATOM   2012  H  HG   . LEU   A  1  130 ? 14.523  -19.178 -44.177  1.00 66.77  ? 130  LEU   A HG   1 
ATOM   2013  H  HD11 . LEU   A  1  130 ? 16.407  -18.772 -42.848  1.00 66.76  ? 130  LEU   A HD11 1 
ATOM   2014  H  HD12 . LEU   A  1  130 ? 15.068  -18.434 -42.062  1.00 66.76  ? 130  LEU   A HD12 1 
ATOM   2015  H  HD13 . LEU   A  1  130 ? 15.844  -19.788 -41.765  1.00 66.76  ? 130  LEU   A HD13 1 
ATOM   2016  H  HD21 . LEU   A  1  130 ? 16.419  -20.445 -44.625  1.00 68.37  ? 130  LEU   A HD21 1 
ATOM   2017  H  HD22 . LEU   A  1  130 ? 15.914  -21.561 -43.614  1.00 68.37  ? 130  LEU   A HD22 1 
ATOM   2018  H  HD23 . LEU   A  1  130 ? 15.110  -21.283 -44.956  1.00 68.37  ? 130  LEU   A HD23 1 
ATOM   2019  N  N    . GLN   A  1  131 ? 12.331  -17.251 -43.144  1.00 76.96  ? 131  GLN   A N    1 
ATOM   2020  C  CA   . GLN   A  1  131 ? 11.944  -16.182 -44.054  1.00 86.19  ? 131  GLN   A CA   1 
ATOM   2021  C  C    . GLN   A  1  131 ? 13.204  -15.530 -44.598  1.00 92.85  ? 131  GLN   A C    1 
ATOM   2022  O  O    . GLN   A  1  131 ? 14.045  -15.059 -43.825  1.00 94.03  ? 131  GLN   A O    1 
ATOM   2023  C  CB   . GLN   A  1  131 ? 11.069  -15.149 -43.346  1.00 87.73  ? 131  GLN   A CB   1 
ATOM   2024  C  CG   . GLN   A  1  131 ? 10.784  -13.911 -44.176  1.00 90.74  ? 131  GLN   A CG   1 
ATOM   2025  C  CD   . GLN   A  1  131 ? 9.789   -12.988 -43.509  1.00 92.34  ? 131  GLN   A CD   1 
ATOM   2026  O  OE1  . GLN   A  1  131 ? 10.087  -11.826 -43.231  1.00 93.18  ? 131  GLN   A OE1  1 
ATOM   2027  N  NE2  . GLN   A  1  131 ? 8.593   -13.501 -43.248  1.00 91.58  ? 131  GLN   A NE2  1 
ATOM   2028  H  H    . GLN   A  1  131 ? 12.759  -16.971 -42.452  1.00 92.38  ? 131  GLN   A H    1 
ATOM   2029  H  HA   . GLN   A  1  131 ? 11.441  -16.552 -44.796  1.00 103.46 ? 131  GLN   A HA   1 
ATOM   2030  H  HB2  . GLN   A  1  131 ? 10.218  -15.559 -43.126  1.00 105.31 ? 131  GLN   A HB2  1 
ATOM   2031  H  HB3  . GLN   A  1  131 ? 11.518  -14.863 -42.535  1.00 105.31 ? 131  GLN   A HB3  1 
ATOM   2032  H  HG2  . GLN   A  1  131 ? 11.610  -13.420 -44.307  1.00 108.93 ? 131  GLN   A HG2  1 
ATOM   2033  H  HG3  . GLN   A  1  131 ? 10.418  -14.181 -45.033  1.00 108.93 ? 131  GLN   A HG3  1 
ATOM   2034  H  HE21 . GLN   A  1  131 ? 8.421   -14.318 -43.458  1.00 109.93 ? 131  GLN   A HE21 1 
ATOM   2035  H  HE22 . GLN   A  1  131 ? 7.991   -13.018 -42.870  1.00 109.93 ? 131  GLN   A HE22 1 
ATOM   2036  N  N    . ASP   A  1  132 ? 13.334  -15.503 -45.922  1.00 97.28  ? 132  ASP   A N    1 
ATOM   2037  C  CA   . ASP   A  1  132 ? 14.469  -14.839 -46.551  1.00 102.62 ? 132  ASP   A CA   1 
ATOM   2038  C  C    . ASP   A  1  132 ? 14.072  -13.415 -46.923  1.00 106.18 ? 132  ASP   A C    1 
ATOM   2039  O  O    . ASP   A  1  132 ? 14.367  -12.471 -46.184  1.00 100.87 ? 132  ASP   A O    1 
ATOM   2040  C  CB   . ASP   A  1  132 ? 14.945  -15.626 -47.774  1.00 104.29 ? 132  ASP   A CB   1 
ATOM   2041  C  CG   . ASP   A  1  132 ? 16.342  -15.231 -48.209  1.00 110.15 ? 132  ASP   A CG   1 
ATOM   2042  O  OD1  . ASP   A  1  132 ? 16.654  -14.022 -48.177  1.00 117.12 ? 132  ASP   A OD1  1 
ATOM   2043  O  OD2  . ASP   A  1  132 ? 17.131  -16.129 -48.571  1.00 114.98 ? 132  ASP   A OD2  1 
ATOM   2044  H  H    . ASP   A  1  132 ? 12.780  -15.860 -46.475  1.00 116.78 ? 132  ASP   A H    1 
ATOM   2045  H  HA   . ASP   A  1  132 ? 15.219  -14.799 -45.938  1.00 123.18 ? 132  ASP   A HA   1 
ATOM   2046  H  HB2  . ASP   A  1  132 ? 14.953  -16.572 -47.558  1.00 125.18 ? 132  ASP   A HB2  1 
ATOM   2047  H  HB3  . ASP   A  1  132 ? 14.341  -15.460 -48.514  1.00 125.18 ? 132  ASP   A HB3  1 
ATOM   2048  N  N    . GLY   A  1  133 ? 13.399  -13.252 -48.060  1.00 111.62 ? 133  GLY   A N    1 
ATOM   2049  C  CA   . GLY   A  1  133 ? 12.830  -11.974 -48.435  1.00 116.86 ? 133  GLY   A CA   1 
ATOM   2050  C  C    . GLY   A  1  133 ? 11.323  -12.087 -48.498  1.00 116.62 ? 133  GLY   A C    1 
ATOM   2051  O  O    . GLY   A  1  133 ? 10.642  -11.996 -47.472  1.00 120.34 ? 133  GLY   A O    1 
ATOM   2052  H  H    . GLY   A  1  133 ? 13.260  -13.877 -48.634  1.00 133.99 ? 133  GLY   A H    1 
ATOM   2053  H  HA2  . GLY   A  1  133 ? 13.071  -11.299 -47.782  1.00 140.27 ? 133  GLY   A HA2  1 
ATOM   2054  H  HA3  . GLY   A  1  133 ? 13.165  -11.705 -49.305  1.00 140.27 ? 133  GLY   A HA3  1 
ATOM   2055  N  N    . THR   A  1  134 ? 10.790  -12.292 -49.702  1.00 113.44 ? 134  THR   A N    1 
ATOM   2056  C  CA   . THR   A  1  134 ? 9.390   -12.678 -49.826  1.00 115.44 ? 134  THR   A CA   1 
ATOM   2057  C  C    . THR   A  1  134 ? 9.189   -14.123 -49.392  1.00 105.47 ? 134  THR   A C    1 
ATOM   2058  O  O    . THR   A  1  134 ? 8.176   -14.458 -48.767  1.00 104.40 ? 134  THR   A O    1 
ATOM   2059  C  CB   . THR   A  1  134 ? 8.919   -12.499 -51.268  1.00 123.64 ? 134  THR   A CB   1 
ATOM   2060  O  OG1  . THR   A  1  134 ? 9.738   -13.289 -52.140  1.00 126.63 ? 134  THR   A OG1  1 
ATOM   2061  C  CG2  . THR   A  1  134 ? 8.999   -11.040 -51.685  1.00 125.87 ? 134  THR   A CG2  1 
ATOM   2062  H  H    . THR   A  1  134 ? 11.211  -12.217 -50.448  1.00 136.17 ? 134  THR   A H    1 
ATOM   2063  H  HA   . THR   A  1  134 ? 8.856   -12.101 -49.258  1.00 138.57 ? 134  THR   A HA   1 
ATOM   2064  H  HB   . THR   A  1  134 ? 7.994   -12.783 -51.344  1.00 148.40 ? 134  THR   A HB   1 
ATOM   2065  H  HG1  . THR   A  1  134 ? 9.437   -13.259 -52.923  1.00 152.00 ? 134  THR   A HG1  1 
ATOM   2066  H  HG21 . THR   A  1  134 ? 8.671   -10.936 -52.592  1.00 151.08 ? 134  THR   A HG21 1 
ATOM   2067  H  HG22 . THR   A  1  134 ? 8.459   -10.496 -51.091  1.00 151.08 ? 134  THR   A HG22 1 
ATOM   2068  H  HG23 . THR   A  1  134 ? 9.918   -10.734 -51.645  1.00 151.08 ? 134  THR   A HG23 1 
ATOM   2069  N  N    . LYS   A  1  135 ? 10.154  -14.984 -49.701  1.00 99.16  ? 135  LYS   A N    1 
ATOM   2070  C  CA   . LYS   A  1  135 ? 9.984   -16.417 -49.513  1.00 93.44  ? 135  LYS   A CA   1 
ATOM   2071  C  C    . LYS   A  1  135 ? 10.033  -16.784 -48.035  1.00 85.41  ? 135  LYS   A C    1 
ATOM   2072  O  O    . LYS   A  1  135 ? 10.953  -16.393 -47.311  1.00 85.32  ? 135  LYS   A O    1 
ATOM   2073  C  CB   . LYS   A  1  135 ? 11.068  -17.173 -50.281  1.00 93.32  ? 135  LYS   A CB   1 
ATOM   2074  C  CG   . LYS   A  1  135 ? 10.913  -18.686 -50.267  1.00 91.38  ? 135  LYS   A CG   1 
ATOM   2075  C  CD   . LYS   A  1  135 ? 9.682   -19.129 -51.045  1.00 93.75  ? 135  LYS   A CD   1 
ATOM   2076  C  CE   . LYS   A  1  135 ? 9.492   -20.635 -50.983  1.00 97.58  ? 135  LYS   A CE   1 
ATOM   2077  N  NZ   . LYS   A  1  135 ? 10.626  -21.387 -51.592  1.00 100.96 ? 135  LYS   A NZ   1 
ATOM   2078  H  H    . LYS   A  1  135 ? 10.920  -14.762 -50.024  1.00 119.03 ? 135  LYS   A H    1 
ATOM   2079  H  HA   . LYS   A  1  135 ? 9.115   -16.681 -49.854  1.00 112.16 ? 135  LYS   A HA   1 
ATOM   2080  H  HB2  . LYS   A  1  135 ? 11.048  -16.885 -51.207  1.00 112.02 ? 135  LYS   A HB2  1 
ATOM   2081  H  HB3  . LYS   A  1  135 ? 11.929  -16.963 -49.887  1.00 112.02 ? 135  LYS   A HB3  1 
ATOM   2082  H  HG2  . LYS   A  1  135 ? 11.694  -19.093 -50.675  1.00 109.69 ? 135  LYS   A HG2  1 
ATOM   2083  H  HG3  . LYS   A  1  135 ? 10.820  -18.991 -49.351  1.00 109.69 ? 135  LYS   A HG3  1 
ATOM   2084  H  HD2  . LYS   A  1  135 ? 8.895   -18.708 -50.666  1.00 112.54 ? 135  LYS   A HD2  1 
ATOM   2085  H  HD3  . LYS   A  1  135 ? 9.781   -18.873 -51.975  1.00 112.54 ? 135  LYS   A HD3  1 
ATOM   2086  H  HE2  . LYS   A  1  135 ? 9.418   -20.907 -50.054  1.00 117.13 ? 135  LYS   A HE2  1 
ATOM   2087  H  HE3  . LYS   A  1  135 ? 8.684   -20.872 -51.463  1.00 117.13 ? 135  LYS   A HE3  1 
ATOM   2088  H  HZ1  . LYS   A  1  135 ? 10.512  -22.261 -51.471  1.00 121.19 ? 135  LYS   A HZ1  1 
ATOM   2089  H  HZ2  . LYS   A  1  135 ? 10.669  -21.219 -52.465  1.00 121.19 ? 135  LYS   A HZ2  1 
ATOM   2090  H  HZ3  . LYS   A  1  135 ? 11.393  -21.141 -51.212  1.00 121.19 ? 135  LYS   A HZ3  1 
ATOM   2091  N  N    . THR   A  1  136 ? 9.032   -17.543 -47.596  1.00 76.64  ? 136  THR   A N    1 
ATOM   2092  C  CA   . THR   A  1  136 ? 8.988   -18.133 -46.265  1.00 68.24  ? 136  THR   A CA   1 
ATOM   2093  C  C    . THR   A  1  136 ? 8.706   -19.619 -46.426  1.00 61.68  ? 136  THR   A C    1 
ATOM   2094  O  O    . THR   A  1  136 ? 7.826   -20.001 -47.204  1.00 59.56  ? 136  THR   A O    1 
ATOM   2095  C  CB   . THR   A  1  136 ? 7.909   -17.471 -45.397  1.00 67.06  ? 136  THR   A CB   1 
ATOM   2096  O  OG1  . THR   A  1  136 ? 8.211   -16.079 -45.231  1.00 70.22  ? 136  THR   A OG1  1 
ATOM   2097  C  CG2  . THR   A  1  136 ? 7.823   -18.139 -44.027  1.00 64.00  ? 136  THR   A CG2  1 
ATOM   2098  H  H    . THR   A  1  136 ? 8.341   -17.736 -48.070  1.00 92.00  ? 136  THR   A H    1 
ATOM   2099  H  HA   . THR   A  1  136 ? 9.839   -18.017 -45.815  1.00 81.92  ? 136  THR   A HA   1 
ATOM   2100  H  HB   . THR   A  1  136 ? 7.048   -17.567 -45.832  1.00 80.51  ? 136  THR   A HB   1 
ATOM   2101  H  HG1  . THR   A  1  136 ? 7.542   -15.676 -44.921  1.00 84.30  ? 136  THR   A HG1  1 
ATOM   2102  H  HG21 . THR   A  1  136 ? 7.157   -17.692 -43.482  1.00 76.84  ? 136  THR   A HG21 1 
ATOM   2103  H  HG22 . THR   A  1  136 ? 7.574   -19.071 -44.128  1.00 76.84  ? 136  THR   A HG22 1 
ATOM   2104  H  HG23 . THR   A  1  136 ? 8.682   -18.089 -43.579  1.00 76.84  ? 136  THR   A HG23 1 
ATOM   2105  N  N    . VAL   A  1  137 ? 9.454   -20.455 -45.706  1.00 57.74  ? 137  VAL   A N    1 
ATOM   2106  C  CA   . VAL   A  1  137 ? 9.261   -21.898 -45.750  1.00 57.66  ? 137  VAL   A CA   1 
ATOM   2107  C  C    . VAL   A  1  137 ? 9.205   -22.440 -44.331  1.00 55.91  ? 137  VAL   A C    1 
ATOM   2108  O  O    . VAL   A  1  137 ? 9.841   -21.907 -43.415  1.00 58.01  ? 137  VAL   A O    1 
ATOM   2109  C  CB   . VAL   A  1  137 ? 10.374  -22.624 -46.544  1.00 58.64  ? 137  VAL   A CB   1 
ATOM   2110  C  CG1  . VAL   A  1  137 ? 10.426  -22.122 -47.972  1.00 60.92  ? 137  VAL   A CG1  1 
ATOM   2111  C  CG2  . VAL   A  1  137 ? 11.726  -22.462 -45.858  1.00 58.00  ? 137  VAL   A CG2  1 
ATOM   2112  H  H    . VAL   A  1  137 ? 10.086  -20.205 -45.179  1.00 69.33  ? 137  VAL   A H    1 
ATOM   2113  H  HA   . VAL   A  1  137 ? 8.412   -22.074 -46.185  1.00 69.23  ? 137  VAL   A HA   1 
ATOM   2114  H  HB   . VAL   A  1  137 ? 10.168  -23.571 -46.568  1.00 70.40  ? 137  VAL   A HB   1 
ATOM   2115  H  HG11 . VAL   A  1  137 ? 11.123  -22.599 -48.449  1.00 73.14  ? 137  VAL   A HG11 1 
ATOM   2116  H  HG12 . VAL   A  1  137 ? 9.568   -22.281 -48.394  1.00 73.14  ? 137  VAL   A HG12 1 
ATOM   2117  H  HG13 . VAL   A  1  137 ? 10.621  -21.172 -47.965  1.00 73.14  ? 137  VAL   A HG13 1 
ATOM   2118  H  HG21 . VAL   A  1  137 ? 12.408  -22.892 -46.398  1.00 69.64  ? 137  VAL   A HG21 1 
ATOM   2119  H  HG22 . VAL   A  1  137 ? 11.924  -21.516 -45.768  1.00 69.64  ? 137  VAL   A HG22 1 
ATOM   2120  H  HG23 . VAL   A  1  137 ? 11.688  -22.876 -44.982  1.00 69.64  ? 137  VAL   A HG23 1 
ATOM   2121  N  N    . GLU   A  1  138 ? 8.444   -23.514 -44.155  1.00 54.42  ? 138  GLU   A N    1 
ATOM   2122  C  CA   . GLU   A  1  138 ? 8.418   -24.217 -42.883  1.00 55.31  ? 138  GLU   A CA   1 
ATOM   2123  C  C    . GLU   A  1  138 ? 9.586   -25.191 -42.813  1.00 56.56  ? 138  GLU   A C    1 
ATOM   2124  O  O    . GLU   A  1  138 ? 9.935   -25.837 -43.806  1.00 59.72  ? 138  GLU   A O    1 
ATOM   2125  C  CB   . GLU   A  1  138 ? 7.101   -24.970 -42.699  1.00 53.10  ? 138  GLU   A CB   1 
ATOM   2126  C  CG   . GLU   A  1  138 ? 6.860   -25.415 -41.265  1.00 52.07  ? 138  GLU   A CG   1 
ATOM   2127  C  CD   . GLU   A  1  138 ? 5.590   -26.225 -41.103  1.00 50.65  ? 138  GLU   A CD   1 
ATOM   2128  O  OE1  . GLU   A  1  138 ? 5.036   -26.680 -42.125  1.00 52.26  ? 138  GLU   A OE1  1 
ATOM   2129  O  OE2  . GLU   A  1  138 ? 5.145   -26.406 -39.950  1.00 50.12  ? 138  GLU   A OE2  1 
ATOM   2130  H  H    . GLU   A  1  138 ? 7.933   -23.855 -44.758  1.00 65.34  ? 138  GLU   A H    1 
ATOM   2131  H  HA   . GLU   A  1  138 ? 8.494   -23.578 -42.157  1.00 66.41  ? 138  GLU   A HA   1 
ATOM   2132  H  HB2  . GLU   A  1  138 ? 6.369   -24.388 -42.958  1.00 63.76  ? 138  GLU   A HB2  1 
ATOM   2133  H  HB3  . GLU   A  1  138 ? 7.111   -25.761 -43.260  1.00 63.76  ? 138  GLU   A HB3  1 
ATOM   2134  H  HG2  . GLU   A  1  138 ? 7.605   -25.967 -40.977  1.00 62.52  ? 138  GLU   A HG2  1 
ATOM   2135  H  HG3  . GLU   A  1  138 ? 6.790   -24.631 -40.699  1.00 62.52  ? 138  GLU   A HG3  1 
ATOM   2136  N  N    . TYR   A  1  139 ? 10.191  -25.290 -41.633  1.00 50.77  ? 139  TYR   A N    1 
ATOM   2137  C  CA   . TYR   A  1  139 ? 11.332  -26.173 -41.402  1.00 49.44  ? 139  TYR   A CA   1 
ATOM   2138  C  C    . TYR   A  1  139 ? 11.069  -26.949 -40.116  1.00 47.26  ? 139  TYR   A C    1 
ATOM   2139  O  O    . TYR   A  1  139 ? 11.342  -26.458 -39.017  1.00 50.85  ? 139  TYR   A O    1 
ATOM   2140  C  CB   . TYR   A  1  139 ? 12.633  -25.381 -41.325  1.00 48.74  ? 139  TYR   A CB   1 
ATOM   2141  C  CG   . TYR   A  1  139 ? 13.843  -26.218 -40.983  1.00 49.19  ? 139  TYR   A CG   1 
ATOM   2142  C  CD1  . TYR   A  1  139 ? 14.217  -27.293 -41.780  1.00 51.72  ? 139  TYR   A CD1  1 
ATOM   2143  C  CD2  . TYR   A  1  139 ? 14.619  -25.927 -39.870  1.00 48.17  ? 139  TYR   A CD2  1 
ATOM   2144  C  CE1  . TYR   A  1  139 ? 15.325  -28.060 -41.471  1.00 50.76  ? 139  TYR   A CE1  1 
ATOM   2145  C  CE2  . TYR   A  1  139 ? 15.729  -26.686 -39.554  1.00 47.41  ? 139  TYR   A CE2  1 
ATOM   2146  C  CZ   . TYR   A  1  139 ? 16.078  -27.751 -40.358  1.00 47.90  ? 139  TYR   A CZ   1 
ATOM   2147  O  OH   . TYR   A  1  139 ? 17.182  -28.509 -40.045  1.00 49.22  ? 139  TYR   A OH   1 
ATOM   2148  H  H    . TYR   A  1  139 ? 9.954   -24.847 -40.935  1.00 60.96  ? 139  TYR   A H    1 
ATOM   2149  H  HA   . TYR   A  1  139 ? 11.406  -26.807 -42.132  1.00 59.36  ? 139  TYR   A HA   1 
ATOM   2150  H  HB2  . TYR   A  1  139 ? 12.796  -24.965 -42.186  1.00 58.53  ? 139  TYR   A HB2  1 
ATOM   2151  H  HB3  . TYR   A  1  139 ? 12.542  -24.700 -40.640  1.00 58.53  ? 139  TYR   A HB3  1 
ATOM   2152  H  HD1  . TYR   A  1  139 ? 13.713  -27.501 -42.533  1.00 62.10  ? 139  TYR   A HD1  1 
ATOM   2153  H  HD2  . TYR   A  1  139 ? 14.388  -25.209 -39.327  1.00 57.84  ? 139  TYR   A HD2  1 
ATOM   2154  H  HE1  . TYR   A  1  139 ? 15.562  -28.779 -42.011  1.00 60.95  ? 139  TYR   A HE1  1 
ATOM   2155  H  HE2  . TYR   A  1  139 ? 16.238  -26.480 -38.804  1.00 56.93  ? 139  TYR   A HE2  1 
ATOM   2156  H  HH   . TYR   A  1  139 ? 17.307  -29.092 -40.636  1.00 59.11  ? 139  TYR   A HH   1 
ATOM   2157  N  N    . ALA   A  1  140 ? 10.533  -28.161 -40.262  1.00 42.24  ? 140  ALA   A N    1 
ATOM   2158  C  CA   . ALA   A  1  140 ? 10.235  -29.056 -39.147  1.00 43.15  ? 140  ALA   A CA   1 
ATOM   2159  C  C    . ALA   A  1  140 ? 11.041  -30.334 -39.360  1.00 43.01  ? 140  ALA   A C    1 
ATOM   2160  O  O    . ALA   A  1  140 ? 10.491  -31.366 -39.776  1.00 42.22  ? 140  ALA   A O    1 
ATOM   2161  C  CB   . ALA   A  1  140 ? 8.738   -29.345 -39.049  1.00 45.35  ? 140  ALA   A CB   1 
ATOM   2162  H  H    . ALA   A  1  140 ? 10.325  -28.497 -41.026  1.00 50.73  ? 140  ALA   A H    1 
ATOM   2163  H  HA   . ALA   A  1  140 ? 10.514  -28.650 -38.311  1.00 51.82  ? 140  ALA   A HA   1 
ATOM   2164  H  HB1  . ALA   A  1  140 ? 8.578   -29.930 -38.292  1.00 54.46  ? 140  ALA   A HB1  1 
ATOM   2165  H  HB2  . ALA   A  1  140 ? 8.262   -28.509 -38.927  1.00 54.46  ? 140  ALA   A HB2  1 
ATOM   2166  H  HB3  . ALA   A  1  140 ? 8.446   -29.776 -39.867  1.00 54.46  ? 140  ALA   A HB3  1 
ATOM   2167  N  N    . PRO   A  1  141 ? 12.349  -30.301 -39.093  1.00 44.82  ? 141  PRO   A N    1 
ATOM   2168  C  CA   . PRO   A  1  141 ? 13.175  -31.493 -39.346  1.00 46.86  ? 141  PRO   A CA   1 
ATOM   2169  C  C    . PRO   A  1  141 ? 12.812  -32.680 -38.478  1.00 49.29  ? 141  PRO   A C    1 
ATOM   2170  O  O    . PRO   A  1  141 ? 13.105  -33.818 -38.863  1.00 50.87  ? 141  PRO   A O    1 
ATOM   2171  C  CB   . PRO   A  1  141 ? 14.599  -31.001 -39.053  1.00 47.71  ? 141  PRO   A CB   1 
ATOM   2172  C  CG   . PRO   A  1  141 ? 14.416  -29.866 -38.103  1.00 47.53  ? 141  PRO   A CG   1 
ATOM   2173  C  CD   . PRO   A  1  141 ? 13.135  -29.197 -38.514  1.00 47.10  ? 141  PRO   A CD   1 
ATOM   2174  H  HA   . PRO   A  1  141 ? 13.109  -31.748 -40.280  1.00 56.27  ? 141  PRO   A HA   1 
ATOM   2175  H  HB2  . PRO   A  1  141 ? 15.119  -31.714 -38.649  1.00 57.29  ? 141  PRO   A HB2  1 
ATOM   2176  H  HB3  . PRO   A  1  141 ? 15.023  -30.705 -39.874  1.00 57.29  ? 141  PRO   A HB3  1 
ATOM   2177  H  HG2  . PRO   A  1  141 ? 14.353  -30.204 -37.196  1.00 57.07  ? 141  PRO   A HG2  1 
ATOM   2178  H  HG3  . PRO   A  1  141 ? 15.164  -29.252 -38.177  1.00 57.07  ? 141  PRO   A HG3  1 
ATOM   2179  H  HD2  . PRO   A  1  141 ? 12.682  -28.817 -37.745  1.00 56.56  ? 141  PRO   A HD2  1 
ATOM   2180  H  HD3  . PRO   A  1  141 ? 13.302  -28.508 -39.176  1.00 56.56  ? 141  PRO   A HD3  1 
ATOM   2181  N  N    . CYS   A  1  142 ? 12.191  -32.457 -37.322  1.00 46.41  ? 142  CYS   A N    1 
ATOM   2182  C  CA   . CYS   A  1  142 ? 11.789  -33.546 -36.444  1.00 47.53  ? 142  CYS   A CA   1 
ATOM   2183  C  C    . CYS   A  1  142 ? 10.396  -34.077 -36.751  1.00 49.36  ? 142  CYS   A C    1 
ATOM   2184  O  O    . CYS   A  1  142 ? 10.010  -35.112 -36.197  1.00 50.64  ? 142  CYS   A O    1 
ATOM   2185  C  CB   . CYS   A  1  142 ? 11.866  -33.088 -34.986  1.00 50.35  ? 142  CYS   A CB   1 
ATOM   2186  S  SG   . CYS   A  1  142 ? 13.483  -33.404 -34.250  1.00 56.45  ? 142  CYS   A SG   1 
ATOM   2187  H  H    . CYS   A  1  142 ? 11.991  -31.676 -37.023  1.00 55.73  ? 142  CYS   A H    1 
ATOM   2188  H  HA   . CYS   A  1  142 ? 12.407  -34.285 -36.554  1.00 57.08  ? 142  CYS   A HA   1 
ATOM   2189  H  HB2  . CYS   A  1  142 ? 11.696  -32.134 -34.944  1.00 60.46  ? 142  CYS   A HB2  1 
ATOM   2190  H  HB3  . CYS   A  1  142 ? 11.199  -33.567 -34.469  1.00 60.46  ? 142  CYS   A HB3  1 
ATOM   2191  H  HG   . CYS   A  1  142 ? 13.750  -32.511 -33.494  1.00 67.78  ? 142  CYS   A HG   1 
ATOM   2192  N  N    . ARG   A  1  143 ? 9.638   -33.407 -37.619  1.00 49.56  ? 143  ARG   A N    1 
ATOM   2193  C  CA   . ARG   A  1  143 ? 8.355   -33.928 -38.089  1.00 48.35  ? 143  ARG   A CA   1 
ATOM   2194  C  C    . ARG   A  1  143 ? 8.626   -34.980 -39.166  1.00 49.86  ? 143  ARG   A C    1 
ATOM   2195  O  O    . ARG   A  1  143 ? 8.328   -34.813 -40.350  1.00 51.86  ? 143  ARG   A O    1 
ATOM   2196  C  CB   . ARG   A  1  143 ? 7.472   -32.806 -38.612  1.00 48.14  ? 143  ARG   A CB   1 
ATOM   2197  C  CG   . ARG   A  1  143 ? 6.056   -33.245 -38.948  1.00 49.50  ? 143  ARG   A CG   1 
ATOM   2198  C  CD   . ARG   A  1  143 ? 5.180   -32.047 -39.258  1.00 48.93  ? 143  ARG   A CD   1 
ATOM   2199  N  NE   . ARG   A  1  143 ? 5.624   -31.343 -40.458  1.00 47.90  ? 143  ARG   A NE   1 
ATOM   2200  C  CZ   . ARG   A  1  143 ? 5.426   -30.049 -40.689  1.00 51.21  ? 143  ARG   A CZ   1 
ATOM   2201  N  NH1  . ARG   A  1  143 ? 4.799   -29.293 -39.796  1.00 50.44  ? 143  ARG   A NH1  1 
ATOM   2202  N  NH2  . ARG   A  1  143 ? 5.867   -29.504 -41.815  1.00 54.81  ? 143  ARG   A NH2  1 
ATOM   2203  H  H    . ARG   A  1  143 ? 9.846   -32.642 -37.953  1.00 59.51  ? 143  ARG   A H    1 
ATOM   2204  H  HA   . ARG   A  1  143 ? 7.890   -34.348 -37.348  1.00 58.06  ? 143  ARG   A HA   1 
ATOM   2205  H  HB2  . ARG   A  1  143 ? 7.415   -32.114 -37.936  1.00 57.81  ? 143  ARG   A HB2  1 
ATOM   2206  H  HB3  . ARG   A  1  143 ? 7.871   -32.448 -39.421  1.00 57.81  ? 143  ARG   A HB3  1 
ATOM   2207  H  HG2  . ARG   A  1  143 ? 6.071   -33.824 -39.726  1.00 59.44  ? 143  ARG   A HG2  1 
ATOM   2208  H  HG3  . ARG   A  1  143 ? 5.675   -33.717 -38.191  1.00 59.44  ? 143  ARG   A HG3  1 
ATOM   2209  H  HD2  . ARG   A  1  143 ? 4.269   -32.346 -39.401  1.00 58.75  ? 143  ARG   A HD2  1 
ATOM   2210  H  HD3  . ARG   A  1  143 ? 5.212   -31.426 -38.513  1.00 58.75  ? 143  ARG   A HD3  1 
ATOM   2211  H  HE   . ARG   A  1  143 ? 6.043   -31.798 -41.057  1.00 57.51  ? 143  ARG   A HE   1 
ATOM   2212  H  HH11 . ARG   A  1  143 ? 4.518   -29.640 -39.061  1.00 60.56  ? 143  ARG   A HH11 1 
ATOM   2213  H  HH12 . ARG   A  1  143 ? 4.674   -28.456 -39.953  1.00 60.56  ? 143  ARG   A HH12 1 
ATOM   2214  H  HH21 . ARG   A  1  143 ? 6.281   -29.988 -42.393  1.00 65.81  ? 143  ARG   A HH21 1 
ATOM   2215  H  HH22 . ARG   A  1  143 ? 5.740   -28.667 -41.966  1.00 65.81  ? 143  ARG   A HH22 1 
ATOM   2216  N  N    . SER   A  1  144 ? 9.218   -36.081 -38.725  1.00 51.75  ? 144  SER   A N    1 
ATOM   2217  C  CA   . SER   A  1  144 ? 9.610   -37.170 -39.599  1.00 49.80  ? 144  SER   A CA   1 
ATOM   2218  C  C    . SER   A  1  144 ? 8.611   -38.317 -39.457  1.00 51.58  ? 144  SER   A C    1 
ATOM   2219  O  O    . SER   A  1  144 ? 7.516   -38.154 -38.912  1.00 51.57  ? 144  SER   A O    1 
ATOM   2220  C  CB   . SER   A  1  144 ? 11.040  -37.596 -39.263  1.00 49.05  ? 144  SER   A CB   1 
ATOM   2221  O  OG   . SER   A  1  144 ? 11.114  -38.135 -37.953  1.00 46.95  ? 144  SER   A OG   1 
ATOM   2222  H  H    . SER   A  1  144 ? 9.407   -36.223 -37.899  1.00 62.14  ? 144  SER   A H    1 
ATOM   2223  H  HA   . SER   A  1  144 ? 9.592   -36.869 -40.521  1.00 59.80  ? 144  SER   A HA   1 
ATOM   2224  H  HB2  . SER   A  1  144 ? 11.325  -38.271 -39.898  1.00 58.90  ? 144  SER   A HB2  1 
ATOM   2225  H  HB3  . SER   A  1  144 ? 11.621  -36.821 -39.318  1.00 58.90  ? 144  SER   A HB3  1 
ATOM   2226  H  HG   . SER   A  1  144 ? 11.901  -38.377 -37.786  1.00 56.38  ? 144  SER   A HG   1 
ATOM   2227  N  N    . GLN   A  1  145 ? 8.990   -39.493 -39.955  1.00 50.65  ? 145  GLN   A N    1 
ATOM   2228  C  CA   . GLN   A  1  145 ? 8.197   -40.706 -39.814  1.00 51.75  ? 145  GLN   A CA   1 
ATOM   2229  C  C    . GLN   A  1  145 ? 8.689   -41.576 -38.665  1.00 53.30  ? 145  GLN   A C    1 
ATOM   2230  O  O    . GLN   A  1  145 ? 8.170   -42.679 -38.466  1.00 54.35  ? 145  GLN   A O    1 
ATOM   2231  C  CB   . GLN   A  1  145 ? 8.213   -41.476 -41.139  1.00 59.78  ? 145  GLN   A CB   1 
ATOM   2232  C  CG   . GLN   A  1  145 ? 7.576   -40.671 -42.277  1.00 62.46  ? 145  GLN   A CG   1 
ATOM   2233  C  CD   . GLN   A  1  145 ? 7.966   -41.153 -43.659  1.00 61.32  ? 145  GLN   A CD   1 
ATOM   2234  O  OE1  . GLN   A  1  145 ? 8.713   -42.118 -43.805  1.00 64.25  ? 145  GLN   A OE1  1 
ATOM   2235  N  NE2  . GLN   A  1  145 ? 7.461   -40.474 -44.685  1.00 58.62  ? 145  GLN   A NE2  1 
ATOM   2236  H  H    . GLN   A  1  145 ? 9.722   -39.614 -40.390  1.00 60.82  ? 145  GLN   A H    1 
ATOM   2237  H  HA   . GLN   A  1  145 ? 7.272   -40.485 -39.625  1.00 62.14  ? 145  GLN   A HA   1 
ATOM   2238  H  HB2  . GLN   A  1  145 ? 9.131   -41.672 -41.382  1.00 71.77  ? 145  GLN   A HB2  1 
ATOM   2239  H  HB3  . GLN   A  1  145 ? 7.714   -42.301 -41.034  1.00 71.77  ? 145  GLN   A HB3  1 
ATOM   2240  H  HG2  . GLN   A  1  145 ? 6.611   -40.735 -42.203  1.00 74.98  ? 145  GLN   A HG2  1 
ATOM   2241  H  HG3  . GLN   A  1  145 ? 7.854   -39.745 -42.198  1.00 74.98  ? 145  GLN   A HG3  1 
ATOM   2242  H  HE21 . GLN   A  1  145 ? 6.944   -39.802 -44.544  1.00 70.38  ? 145  GLN   A HE21 1 
ATOM   2243  H  HE22 . GLN   A  1  145 ? 7.652   -40.708 -45.491  1.00 70.38  ? 145  GLN   A HE22 1 
ATOM   2244  N  N    . ASP   A  1  146 ? 9.672   -41.091 -37.904  1.00 54.93  ? 146  ASP   A N    1 
ATOM   2245  C  CA   . ASP   A  1  146 ? 10.182  -41.746 -36.699  1.00 53.20  ? 146  ASP   A CA   1 
ATOM   2246  C  C    . ASP   A  1  146 ? 9.398   -41.173 -35.524  1.00 52.59  ? 146  ASP   A C    1 
ATOM   2247  O  O    . ASP   A  1  146 ? 9.745   -40.132 -34.964  1.00 56.39  ? 146  ASP   A O    1 
ATOM   2248  C  CB   . ASP   A  1  146 ? 11.681  -41.504 -36.565  1.00 55.08  ? 146  ASP   A CB   1 
ATOM   2249  C  CG   . ASP   A  1  146 ? 12.347  -42.448 -35.585  1.00 60.45  ? 146  ASP   A CG   1 
ATOM   2250  O  OD1  . ASP   A  1  146 ? 11.691  -43.413 -35.141  1.00 63.27  ? 146  ASP   A OD1  1 
ATOM   2251  O  OD2  . ASP   A  1  146 ? 13.533  -42.224 -35.260  1.00 64.21  ? 146  ASP   A OD2  1 
ATOM   2252  H  H    . ASP   A  1  146 ? 10.077  -40.351 -38.073  1.00 65.96  ? 146  ASP   A H    1 
ATOM   2253  H  HA   . ASP   A  1  146 ? 10.035  -42.704 -36.737  1.00 63.88  ? 146  ASP   A HA   1 
ATOM   2254  H  HB2  . ASP   A  1  146 ? 12.098  -41.628 -37.432  1.00 66.13  ? 146  ASP   A HB2  1 
ATOM   2255  H  HB3  . ASP   A  1  146 ? 11.827  -40.597 -36.254  1.00 66.13  ? 146  ASP   A HB3  1 
ATOM   2256  N  N    . ILE   A  1  147 ? 8.333   -41.870 -35.138  1.00 50.18  ? 147  ILE   A N    1 
ATOM   2257  C  CA   . ILE   A  1  147 ? 7.272   -41.284 -34.331  1.00 54.16  ? 147  ILE   A CA   1 
ATOM   2258  C  C    . ILE   A  1  147 ? 7.371   -41.734 -32.879  1.00 55.10  ? 147  ILE   A C    1 
ATOM   2259  O  O    . ILE   A  1  147 ? 8.060   -42.699 -32.534  1.00 58.97  ? 147  ILE   A O    1 
ATOM   2260  C  CB   . ILE   A  1  147 ? 5.869   -41.613 -34.913  1.00 61.27  ? 147  ILE   A CB   1 
ATOM   2261  C  CG1  . ILE   A  1  147 ? 5.713   -43.108 -35.234  1.00 66.59  ? 147  ILE   A CG1  1 
ATOM   2262  C  CG2  . ILE   A  1  147 ? 5.607   -40.778 -36.158  1.00 64.43  ? 147  ILE   A CG2  1 
ATOM   2263  C  CD1  . ILE   A  1  147 ? 5.074   -43.913 -34.132  1.00 71.26  ? 147  ILE   A CD1  1 
ATOM   2264  H  H    . ILE   A  1  147 ? 8.201   -42.697 -35.334  1.00 60.25  ? 147  ILE   A H    1 
ATOM   2265  H  HA   . ILE   A  1  147 ? 7.403   -40.323 -34.330  1.00 65.03  ? 147  ILE   A HA   1 
ATOM   2266  H  HB   . ILE   A  1  147 ? 5.216   -41.392 -34.231  1.00 73.56  ? 147  ILE   A HB   1 
ATOM   2267  H  HG12 . ILE   A  1  147 ? 5.159   -43.199 -36.025  1.00 79.94  ? 147  ILE   A HG12 1 
ATOM   2268  H  HG13 . ILE   A  1  147 ? 6.592   -43.482 -35.400  1.00 79.94  ? 147  ILE   A HG13 1 
ATOM   2269  H  HG21 . ILE   A  1  147 ? 4.713   -40.968 -36.484  1.00 77.35  ? 147  ILE   A HG21 1 
ATOM   2270  H  HG22 . ILE   A  1  147 ? 5.684   -39.838 -35.930  1.00 77.35  ? 147  ILE   A HG22 1 
ATOM   2271  H  HG23 . ILE   A  1  147 ? 6.262   -41.008 -36.836  1.00 77.35  ? 147  ILE   A HG23 1 
ATOM   2272  H  HD11 . ILE   A  1  147 ? 5.024   -44.841 -34.407  1.00 85.55  ? 147  ILE   A HD11 1 
ATOM   2273  H  HD12 . ILE   A  1  147 ? 5.613   -43.834 -33.329  1.00 85.55  ? 147  ILE   A HD12 1 
ATOM   2274  H  HD13 . ILE   A  1  147 ? 4.182   -43.569 -33.966  1.00 85.55  ? 147  ILE   A HD13 1 
ATOM   2275  N  N    . ASP   A  1  148 ? 6.667   -41.000 -32.011  1.00 53.21  ? 148  ASP   A N    1 
ATOM   2276  C  CA   . ASP   A  1  148 ? 6.560   -41.284 -30.582  1.00 58.42  ? 148  ASP   A CA   1 
ATOM   2277  C  C    . ASP   A  1  148 ? 7.832   -40.892 -29.840  1.00 58.70  ? 148  ASP   A C    1 
ATOM   2278  O  O    . ASP   A  1  148 ? 8.781   -40.385 -30.445  1.00 55.58  ? 148  ASP   A O    1 
ATOM   2279  C  CB   . ASP   A  1  148 ? 6.246   -42.763 -30.343  1.00 60.11  ? 148  ASP   A CB   1 
ATOM   2280  C  CG   . ASP   A  1  148 ? 5.188   -42.967 -29.275  1.00 58.57  ? 148  ASP   A CG   1 
ATOM   2281  O  OD1  . ASP   A  1  148 ? 5.094   -42.127 -28.354  1.00 53.64  ? 148  ASP   A OD1  1 
ATOM   2282  O  OD2  . ASP   A  1  148 ? 4.446   -43.969 -29.360  1.00 58.50  ? 148  ASP   A OD2  1 
ATOM   2283  H  H    . ASP   A  1  148 ? 6.223   -40.299 -32.238  1.00 63.89  ? 148  ASP   A H    1 
ATOM   2284  H  HA   . ASP   A  1  148 ? 5.830   -40.757 -30.223  1.00 70.14  ? 148  ASP   A HA   1 
ATOM   2285  H  HB2  . ASP   A  1  148 ? 5.920   -43.156 -31.168  1.00 72.17  ? 148  ASP   A HB2  1 
ATOM   2286  H  HB3  . ASP   A  1  148 ? 7.054   -43.216 -30.056  1.00 72.17  ? 148  ASP   A HB3  1 
ATOM   2287  N  N    . ALA   A  1  149 ? 7.850   -41.112 -28.521  1.00 59.37  ? 149  ALA   A N    1 
ATOM   2288  C  CA   . ALA   A  1  149 ? 9.041   -40.806 -27.737  1.00 61.44  ? 149  ALA   A CA   1 
ATOM   2289  C  C    . ALA   A  1  149 ? 10.236  -41.624 -28.211  1.00 60.19  ? 149  ALA   A C    1 
ATOM   2290  O  O    . ALA   A  1  149 ? 11.371  -41.135 -28.210  1.00 56.40  ? 149  ALA   A O    1 
ATOM   2291  C  CB   . ALA   A  1  149 ? 8.774   -41.062 -26.253  1.00 65.21  ? 149  ALA   A CB   1 
ATOM   2292  H  H    . ALA   A  1  149 ? 7.194   -41.432 -28.066  1.00 71.29  ? 149  ALA   A H    1 
ATOM   2293  H  HA   . ALA   A  1  149 ? 9.255   -39.866 -27.846  1.00 73.77  ? 149  ALA   A HA   1 
ATOM   2294  H  HB1  . ALA   A  1  149 ? 9.577   -40.859 -25.748  1.00 78.29  ? 149  ALA   A HB1  1 
ATOM   2295  H  HB2  . ALA   A  1  149 ? 8.046   -40.492 -25.961  1.00 78.29  ? 149  ALA   A HB2  1 
ATOM   2296  H  HB3  . ALA   A  1  149 ? 8.534   -41.994 -26.132  1.00 78.29  ? 149  ALA   A HB3  1 
ATOM   2297  N  N    . ASP   A  1  150 ? 9.999   -42.877 -28.609  1.00 58.79  ? 150  ASP   A N    1 
ATOM   2298  C  CA   . ASP   A  1  150 ? 11.064  -43.694 -29.182  1.00 60.31  ? 150  ASP   A CA   1 
ATOM   2299  C  C    . ASP   A  1  150 ? 11.830  -42.921 -30.248  1.00 54.09  ? 150  ASP   A C    1 
ATOM   2300  O  O    . ASP   A  1  150 ? 13.065  -42.939 -30.283  1.00 52.05  ? 150  ASP   A O    1 
ATOM   2301  C  CB   . ASP   A  1  150 ? 10.480  -44.976 -29.782  1.00 71.57  ? 150  ASP   A CB   1 
ATOM   2302  C  CG   . ASP   A  1  150 ? 10.016  -45.960 -28.729  1.00 89.26  ? 150  ASP   A CG   1 
ATOM   2303  O  OD1  . ASP   A  1  150 ? 10.609  -45.984 -27.633  1.00 97.31  ? 150  ASP   A OD1  1 
ATOM   2304  O  OD2  . ASP   A  1  150 ? 9.065   -46.722 -29.003  1.00 96.14  ? 150  ASP   A OD2  1 
ATOM   2305  H  H    . ASP   A  1  150 ? 9.237   -43.272 -28.557  1.00 70.58  ? 150  ASP   A H    1 
ATOM   2306  H  HA   . ASP   A  1  150 ? 11.680  -43.941 -28.475  1.00 72.41  ? 150  ASP   A HA   1 
ATOM   2307  H  HB2  . ASP   A  1  150 ? 9.716   -44.746 -30.335  1.00 85.92  ? 150  ASP   A HB2  1 
ATOM   2308  H  HB3  . ASP   A  1  150 ? 11.159  -45.411 -30.321  1.00 85.92  ? 150  ASP   A HB3  1 
ATOM   2309  N  N    . GLY   A  1  151 ? 11.106  -42.231 -31.126  1.00 52.08  ? 151  GLY   A N    1 
ATOM   2310  C  CA   . GLY   A  1  151 ? 11.722  -41.512 -32.220  1.00 48.65  ? 151  GLY   A CA   1 
ATOM   2311  C  C    . GLY   A  1  151 ? 11.825  -40.024 -31.969  1.00 47.16  ? 151  GLY   A C    1 
ATOM   2312  O  O    . GLY   A  1  151 ? 12.331  -39.596 -30.927  1.00 49.61  ? 151  GLY   A O    1 
ATOM   2313  H  H    . GLY   A  1  151 ? 10.248  -42.168 -31.104  1.00 62.53  ? 151  GLY   A H    1 
ATOM   2314  H  HA2  . GLY   A  1  151 ? 12.617  -41.858 -32.364  1.00 58.42  ? 151  GLY   A HA2  1 
ATOM   2315  H  HA3  . GLY   A  1  151 ? 11.198  -41.648 -33.025  1.00 58.42  ? 151  GLY   A HA3  1 
ATOM   2316  N  N    . GLN   A  1  152 ? 11.342  -39.223 -32.919  1.00 44.75  ? 152  GLN   A N    1 
ATOM   2317  C  CA   . GLN   A  1  152 ? 11.417  -37.770 -32.840  1.00 43.64  ? 152  GLN   A CA   1 
ATOM   2318  C  C    . GLN   A  1  152 ? 10.051  -37.135 -32.600  1.00 42.99  ? 152  GLN   A C    1 
ATOM   2319  O  O    . GLN   A  1  152 ? 9.873   -35.939 -32.855  1.00 44.23  ? 152  GLN   A O    1 
ATOM   2320  C  CB   . GLN   A  1  152 ? 12.044  -37.209 -34.118  1.00 43.00  ? 152  GLN   A CB   1 
ATOM   2321  C  CG   . GLN   A  1  152 ? 13.349  -37.883 -34.518  1.00 45.22  ? 152  GLN   A CG   1 
ATOM   2322  C  CD   . GLN   A  1  152 ? 13.808  -37.481 -35.904  1.00 49.14  ? 152  GLN   A CD   1 
ATOM   2323  O  OE1  . GLN   A  1  152 ? 13.361  -38.042 -36.905  1.00 51.58  ? 152  GLN   A OE1  1 
ATOM   2324  N  NE2  . GLN   A  1  152 ? 14.704  -36.504 -35.971  1.00 49.78  ? 152  GLN   A NE2  1 
ATOM   2325  H  H    . GLN   A  1  152 ? 10.959  -39.507 -33.634  1.00 53.73  ? 152  GLN   A H    1 
ATOM   2326  H  HA   . GLN   A  1  152 ? 11.987  -37.530 -32.092  1.00 52.40  ? 152  GLN   A HA   1 
ATOM   2327  H  HB2  . GLN   A  1  152 ? 11.416  -37.326 -34.848  1.00 51.63  ? 152  GLN   A HB2  1 
ATOM   2328  H  HB3  . GLN   A  1  152 ? 12.227  -36.266 -33.985  1.00 51.63  ? 152  GLN   A HB3  1 
ATOM   2329  H  HG2  . GLN   A  1  152 ? 14.041  -37.631 -33.887  1.00 54.30  ? 152  GLN   A HG2  1 
ATOM   2330  H  HG3  . GLN   A  1  152 ? 13.225  -38.845 -34.508  1.00 54.30  ? 152  GLN   A HG3  1 
ATOM   2331  H  HE21 . GLN   A  1  152 ? 14.992  -36.134 -35.250  1.00 59.77  ? 152  GLN   A HE21 1 
ATOM   2332  H  HE22 . GLN   A  1  152 ? 14.996  -36.240 -36.736  1.00 59.77  ? 152  GLN   A HE22 1 
ATOM   2333  N  N    . GLY   A  1  153 ? 9.082   -37.912 -32.112  1.00 43.42  ? 153  GLY   A N    1 
ATOM   2334  C  CA   . GLY   A  1  153 ? 7.749   -37.374 -31.901  1.00 45.99  ? 153  GLY   A CA   1 
ATOM   2335  C  C    . GLY   A  1  153 ? 7.696   -36.300 -30.834  1.00 44.35  ? 153  GLY   A C    1 
ATOM   2336  O  O    . GLY   A  1  153 ? 6.858   -35.396 -30.902  1.00 42.11  ? 153  GLY   A O    1 
ATOM   2337  H  H    . GLY   A  1  153 ? 9.174   -38.740 -31.900  1.00 52.14  ? 153  GLY   A H    1 
ATOM   2338  H  HA2  . GLY   A  1  153 ? 7.427   -36.991 -32.731  1.00 55.22  ? 153  GLY   A HA2  1 
ATOM   2339  H  HA3  . GLY   A  1  153 ? 7.156   -38.094 -31.634  1.00 55.22  ? 153  GLY   A HA3  1 
ATOM   2340  N  N    . PHE   A  1  154 ? 8.581   -36.377 -29.841  1.00 46.12  ? 154  PHE   A N    1 
ATOM   2341  C  CA   . PHE   A  1  154 ? 8.634   -35.414 -28.749  1.00 49.29  ? 154  PHE   A CA   1 
ATOM   2342  C  C    . PHE   A  1  154 ? 9.910   -34.583 -28.802  1.00 49.54  ? 154  PHE   A C    1 
ATOM   2343  O  O    . PHE   A  1  154 ? 10.383  -34.083 -27.780  1.00 49.26  ? 154  PHE   A O    1 
ATOM   2344  C  CB   . PHE   A  1  154 ? 8.509   -36.137 -27.411  1.00 47.87  ? 154  PHE   A CB   1 
ATOM   2345  C  CG   . PHE   A  1  154 ? 7.147   -36.713 -27.174  1.00 46.86  ? 154  PHE   A CG   1 
ATOM   2346  C  CD1  . PHE   A  1  154 ? 6.709   -37.807 -27.902  1.00 48.60  ? 154  PHE   A CD1  1 
ATOM   2347  C  CD2  . PHE   A  1  154 ? 6.298   -36.152 -26.239  1.00 50.07  ? 154  PHE   A CD2  1 
ATOM   2348  C  CE1  . PHE   A  1  154 ? 5.452   -38.334 -27.696  1.00 50.16  ? 154  PHE   A CE1  1 
ATOM   2349  C  CE2  . PHE   A  1  154 ? 5.040   -36.675 -26.027  1.00 51.21  ? 154  PHE   A CE2  1 
ATOM   2350  C  CZ   . PHE   A  1  154 ? 4.616   -37.768 -26.756  1.00 50.34  ? 154  PHE   A CZ   1 
ATOM   2351  H  H    . PHE   A  1  154 ? 9.175   -36.996 -29.780  1.00 55.38  ? 154  PHE   A H    1 
ATOM   2352  H  HA   . PHE   A  1  154 ? 7.887   -34.800 -28.825  1.00 59.19  ? 154  PHE   A HA   1 
ATOM   2353  H  HB2  . PHE   A  1  154 ? 9.149   -36.866 -27.387  1.00 57.48  ? 154  PHE   A HB2  1 
ATOM   2354  H  HB3  . PHE   A  1  154 ? 8.695   -35.509 -26.696  1.00 57.48  ? 154  PHE   A HB3  1 
ATOM   2355  H  HD1  . PHE   A  1  154 ? 7.270   -38.191 -28.537  1.00 58.36  ? 154  PHE   A HD1  1 
ATOM   2356  H  HD2  . PHE   A  1  154 ? 6.579   -35.414 -25.747  1.00 60.12  ? 154  PHE   A HD2  1 
ATOM   2357  H  HE1  . PHE   A  1  154 ? 5.168   -39.069 -28.189  1.00 60.23  ? 154  PHE   A HE1  1 
ATOM   2358  H  HE2  . PHE   A  1  154 ? 4.477   -36.291 -25.394  1.00 61.49  ? 154  PHE   A HE2  1 
ATOM   2359  H  HZ   . PHE   A  1  154 ? 3.769   -38.123 -26.614  1.00 60.44  ? 154  PHE   A HZ   1 
ATOM   2360  N  N    . CYS   A  1  155 ? 10.449  -34.404 -30.008  1.00 49.91  ? 155  CYS   A N    1 
ATOM   2361  C  CA   . CYS   A  1  155 ? 11.772  -33.816 -30.174  1.00 48.33  ? 155  CYS   A CA   1 
ATOM   2362  C  C    . CYS   A  1  155 ? 11.791  -32.328 -29.851  1.00 48.08  ? 155  CYS   A C    1 
ATOM   2363  O  O    . CYS   A  1  155 ? 12.829  -31.804 -29.430  1.00 49.86  ? 155  CYS   A O    1 
ATOM   2364  C  CB   . CYS   A  1  155 ? 12.243  -34.067 -31.605  1.00 50.54  ? 155  CYS   A CB   1 
ATOM   2365  S  SG   . CYS   A  1  155 ? 13.285  -32.791 -32.326  1.00 55.54  ? 155  CYS   A SG   1 
ATOM   2366  H  H    . CYS   A  1  155 ? 10.066  -34.617 -30.748  1.00 59.93  ? 155  CYS   A H    1 
ATOM   2367  H  HA   . CYS   A  1  155 ? 12.391  -34.241 -29.560  1.00 58.04  ? 155  CYS   A HA   1 
ATOM   2368  H  HB2  . CYS   A  1  155 ? 12.752  -34.893 -31.617  1.00 60.68  ? 155  CYS   A HB2  1 
ATOM   2369  H  HB3  . CYS   A  1  155 ? 11.460  -34.152 -32.172  1.00 60.68  ? 155  CYS   A HB3  1 
ATOM   2370  H  HG   . CYS   A  1  155 ? 14.427  -33.157 -32.297  1.00 66.68  ? 155  CYS   A HG   1 
ATOM   2371  N  N    . GLN   A  1  156 ? 10.671  -31.633 -30.037  1.00 44.43  ? 156  GLN   A N    1 
ATOM   2372  C  CA   . GLN   A  1  156 ? 10.603  -30.191 -29.805  1.00 44.49  ? 156  GLN   A CA   1 
ATOM   2373  C  C    . GLN   A  1  156 ? 11.704  -29.466 -30.576  1.00 41.88  ? 156  GLN   A C    1 
ATOM   2374  O  O    . GLN   A  1  156 ? 12.417  -28.613 -30.044  1.00 43.53  ? 156  GLN   A O    1 
ATOM   2375  C  CB   . GLN   A  1  156 ? 10.688  -29.872 -28.312  1.00 43.25  ? 156  GLN   A CB   1 
ATOM   2376  C  CG   . GLN   A  1  156 ? 9.584   -30.483 -27.475  1.00 45.78  ? 156  GLN   A CG   1 
ATOM   2377  C  CD   . GLN   A  1  156 ? 9.555   -29.916 -26.073  1.00 49.09  ? 156  GLN   A CD   1 
ATOM   2378  O  OE1  . GLN   A  1  156 ? 9.853   -30.612 -25.105  1.00 51.66  ? 156  GLN   A OE1  1 
ATOM   2379  N  NE2  . GLN   A  1  156 ? 9.205   -28.640 -25.957  1.00 48.95  ? 156  GLN   A NE2  1 
ATOM   2380  H  H    . GLN   A  1  156 ? 9.929   -31.977 -30.301  1.00 53.35  ? 156  GLN   A H    1 
ATOM   2381  H  HA   . GLN   A  1  156 ? 9.747   -29.870 -30.131  1.00 53.42  ? 156  GLN   A HA   1 
ATOM   2382  H  HB2  . GLN   A  1  156 ? 11.532  -30.206 -27.973  1.00 51.94  ? 156  GLN   A HB2  1 
ATOM   2383  H  HB3  . GLN   A  1  156 ? 10.642  -28.910 -28.199  1.00 51.94  ? 156  GLN   A HB3  1 
ATOM   2384  H  HG2  . GLN   A  1  156 ? 8.728   -30.301 -27.893  1.00 54.97  ? 156  GLN   A HG2  1 
ATOM   2385  H  HG3  . GLN   A  1  156 ? 9.725   -31.441 -27.411  1.00 54.97  ? 156  GLN   A HG3  1 
ATOM   2386  H  HE21 . GLN   A  1  156 ? 9.009   -28.182 -26.659  1.00 58.77  ? 156  GLN   A HE21 1 
ATOM   2387  H  HE22 . GLN   A  1  156 ? 9.173   -28.271 -25.181  1.00 58.77  ? 156  GLN   A HE22 1 
ATOM   2388  N  N    . GLY   A  1  157 ? 11.843  -29.823 -31.851  1.00 41.13  ? 157  GLY   A N    1 
ATOM   2389  C  CA   . GLY   A  1  157 ? 12.848  -29.218 -32.702  1.00 41.16  ? 157  GLY   A CA   1 
ATOM   2390  C  C    . GLY   A  1  157 ? 12.688  -27.717 -32.816  1.00 46.61  ? 157  GLY   A C    1 
ATOM   2391  O  O    . GLY   A  1  157 ? 11.597  -27.223 -33.118  1.00 48.36  ? 157  GLY   A O    1 
ATOM   2392  H  H    . GLY   A  1  157 ? 11.361  -30.418 -32.244  1.00 49.39  ? 157  GLY   A H    1 
ATOM   2393  H  HA2  . GLY   A  1  157 ? 13.729  -29.404 -32.339  1.00 49.43  ? 157  GLY   A HA2  1 
ATOM   2394  H  HA3  . GLY   A  1  157 ? 12.786  -29.600 -33.591  1.00 49.43  ? 157  GLY   A HA3  1 
ATOM   2395  N  N    . GLY   A  1  158 ? 13.773  -26.980 -32.586  1.00 46.64  ? 158  GLY   A N    1 
ATOM   2396  C  CA   . GLY   A  1  158 ? 13.743  -25.532 -32.529  1.00 41.18  ? 158  GLY   A CA   1 
ATOM   2397  C  C    . GLY   A  1  158 ? 13.869  -24.977 -31.130  1.00 36.56  ? 158  GLY   A C    1 
ATOM   2398  O  O    . GLY   A  1  158 ? 13.956  -23.753 -30.969  1.00 39.13  ? 158  GLY   A O    1 
ATOM   2399  H  H    . GLY   A  1  158 ? 14.556  -27.311 -32.457  1.00 56.00  ? 158  GLY   A H    1 
ATOM   2400  H  HA2  . GLY   A  1  158 ? 14.475  -25.181 -33.059  1.00 49.46  ? 158  GLY   A HA2  1 
ATOM   2401  H  HA3  . GLY   A  1  158 ? 12.904  -25.220 -32.902  1.00 49.46  ? 158  GLY   A HA3  1 
ATOM   2402  N  N    . PHE   A  1  159 ? 13.870  -25.843 -30.113  1.00 36.96  ? 159  PHE   A N    1 
ATOM   2403  C  CA   . PHE   A  1  159 ? 14.139  -25.416 -28.742  1.00 39.02  ? 159  PHE   A CA   1 
ATOM   2404  C  C    . PHE   A  1  159 ? 15.359  -24.503 -28.668  1.00 41.55  ? 159  PHE   A C    1 
ATOM   2405  O  O    . PHE   A  1  159 ? 15.438  -23.644 -27.783  1.00 46.82  ? 159  PHE   A O    1 
ATOM   2406  C  CB   . PHE   A  1  159 ? 14.326  -26.665 -27.874  1.00 42.18  ? 159  PHE   A CB   1 
ATOM   2407  C  CG   . PHE   A  1  159 ? 14.329  -26.400 -26.395  1.00 46.52  ? 159  PHE   A CG   1 
ATOM   2408  C  CD1  . PHE   A  1  159 ? 13.146  -26.391 -25.675  1.00 48.74  ? 159  PHE   A CD1  1 
ATOM   2409  C  CD2  . PHE   A  1  159 ? 15.519  -26.196 -25.720  1.00 46.18  ? 159  PHE   A CD2  1 
ATOM   2410  C  CE1  . PHE   A  1  159 ? 13.151  -26.164 -24.312  1.00 49.31  ? 159  PHE   A CE1  1 
ATOM   2411  C  CE2  . PHE   A  1  159 ? 15.529  -25.968 -24.358  1.00 45.15  ? 159  PHE   A CE2  1 
ATOM   2412  C  CZ   . PHE   A  1  159 ? 14.344  -25.952 -23.653  1.00 46.75  ? 159  PHE   A CZ   1 
ATOM   2413  H  H    . PHE   A  1  159 ? 13.717  -26.685 -30.191  1.00 44.39  ? 159  PHE   A H    1 
ATOM   2414  H  HA   . PHE   A  1  159 ? 13.388  -24.911 -28.394  1.00 46.86  ? 159  PHE   A HA   1 
ATOM   2415  H  HB2  . PHE   A  1  159 ? 13.601  -27.282 -28.059  1.00 50.65  ? 159  PHE   A HB2  1 
ATOM   2416  H  HB3  . PHE   A  1  159 ? 15.176  -27.074 -28.099  1.00 50.65  ? 159  PHE   A HB3  1 
ATOM   2417  H  HD1  . PHE   A  1  159 ? 12.339  -26.540 -26.113  1.00 58.53  ? 159  PHE   A HD1  1 
ATOM   2418  H  HD2  . PHE   A  1  159 ? 16.322  -26.213 -26.188  1.00 55.45  ? 159  PHE   A HD2  1 
ATOM   2419  H  HE1  . PHE   A  1  159 ? 12.350  -26.153 -23.840  1.00 59.21  ? 159  PHE   A HE1  1 
ATOM   2420  H  HE2  . PHE   A  1  159 ? 16.335  -25.825 -23.916  1.00 54.22  ? 159  PHE   A HE2  1 
ATOM   2421  H  HZ   . PHE   A  1  159 ? 14.349  -25.799 -22.736  1.00 56.14  ? 159  PHE   A HZ   1 
ATOM   2422  N  N    . SER   A  1  160 ? 16.309  -24.666 -29.587  1.00 41.81  ? 160  SER   A N    1 
ATOM   2423  C  CA   . SER   A  1  160 ? 17.483  -23.805 -29.670  1.00 43.65  ? 160  SER   A CA   1 
ATOM   2424  C  C    . SER   A  1  160 ? 18.013  -23.855 -31.096  1.00 46.60  ? 160  SER   A C    1 
ATOM   2425  O  O    . SER   A  1  160 ? 17.931  -24.891 -31.761  1.00 46.81  ? 160  SER   A O    1 
ATOM   2426  C  CB   . SER   A  1  160 ? 18.570  -24.239 -28.681  1.00 40.47  ? 160  SER   A CB   1 
ATOM   2427  O  OG   . SER   A  1  160 ? 19.109  -25.498 -29.042  1.00 39.07  ? 160  SER   A OG   1 
ATOM   2428  H  H    . SER   A  1  160 ? 16.296  -25.282 -30.187  1.00 50.21  ? 160  SER   A H    1 
ATOM   2429  H  HA   . SER   A  1  160 ? 17.233  -22.891 -29.461  1.00 52.42  ? 160  SER   A HA   1 
ATOM   2430  H  HB2  . SER   A  1  160 ? 19.280  -23.579 -28.685  1.00 48.60  ? 160  SER   A HB2  1 
ATOM   2431  H  HB3  . SER   A  1  160 ? 18.182  -24.304 -27.795  1.00 48.60  ? 160  SER   A HB3  1 
ATOM   2432  H  HG   . SER   A  1  160 ? 18.888  -26.078 -28.476  1.00 46.92  ? 160  SER   A HG   1 
ATOM   2433  N  N    . ILE   A  1  161 ? 18.560  -22.728 -31.563  1.00 48.53  ? 161  ILE   A N    1 
ATOM   2434  C  CA   . ILE   A  1  161 ? 19.000  -22.602 -32.949  1.00 48.39  ? 161  ILE   A CA   1 
ATOM   2435  C  C    . ILE   A  1  161 ? 20.173  -21.637 -33.044  1.00 49.34  ? 161  ILE   A C    1 
ATOM   2436  O  O    . ILE   A  1  161 ? 20.428  -20.839 -32.139  1.00 52.66  ? 161  ILE   A O    1 
ATOM   2437  C  CB   . ILE   A  1  161 ? 17.854  -22.124 -33.878  1.00 47.61  ? 161  ILE   A CB   1 
ATOM   2438  C  CG1  . ILE   A  1  161 ? 17.226  -20.839 -33.327  1.00 48.88  ? 161  ILE   A CG1  1 
ATOM   2439  C  CG2  . ILE   A  1  161 ? 16.811  -23.219 -34.043  1.00 46.05  ? 161  ILE   A CG2  1 
ATOM   2440  C  CD1  . ILE   A  1  161 ? 16.153  -20.243 -34.220  1.00 52.80  ? 161  ILE   A CD1  1 
ATOM   2441  H  H    . ILE   A  1  161 ? 18.685  -22.020 -31.090  1.00 58.28  ? 161  ILE   A H    1 
ATOM   2442  H  HA   . ILE   A  1  161 ? 19.312  -23.473 -33.241  1.00 58.10  ? 161  ILE   A HA   1 
ATOM   2443  H  HB   . ILE   A  1  161 ? 18.225  -21.927 -34.752  1.00 57.17  ? 161  ILE   A HB   1 
ATOM   2444  H  HG12 . ILE   A  1  161 ? 16.819  -21.036 -32.469  1.00 58.70  ? 161  ILE   A HG12 1 
ATOM   2445  H  HG13 . ILE   A  1  161 ? 17.923  -20.174 -33.219  1.00 58.70  ? 161  ILE   A HG13 1 
ATOM   2446  H  HG21 . ILE   A  1  161 ? 16.141  -22.923 -34.679  1.00 55.30  ? 161  ILE   A HG21 1 
ATOM   2447  H  HG22 . ILE   A  1  161 ? 17.246  -24.022 -34.371  1.00 55.30  ? 161  ILE   A HG22 1 
ATOM   2448  H  HG23 . ILE   A  1  161 ? 16.398  -23.394 -33.184  1.00 55.30  ? 161  ILE   A HG23 1 
ATOM   2449  H  HD11 . ILE   A  1  161 ? 15.834  -19.418 -33.822  1.00 63.39  ? 161  ILE   A HD11 1 
ATOM   2450  H  HD12 . ILE   A  1  161 ? 16.534  -20.063 -35.094  1.00 63.39  ? 161  ILE   A HD12 1 
ATOM   2451  H  HD13 . ILE   A  1  161 ? 15.422  -20.875 -34.302  1.00 63.39  ? 161  ILE   A HD13 1 
ATOM   2452  N  N    . ASP   A  1  162 ? 20.889  -21.719 -34.165  1.00 50.06  ? 162  ASP   A N    1 
ATOM   2453  C  CA   . ASP   A  1  162 ? 21.955  -20.786 -34.509  1.00 52.12  ? 162  ASP   A CA   1 
ATOM   2454  C  C    . ASP   A  1  162 ? 22.309  -20.993 -35.976  1.00 53.91  ? 162  ASP   A C    1 
ATOM   2455  O  O    . ASP   A  1  162 ? 22.028  -22.046 -36.555  1.00 50.41  ? 162  ASP   A O    1 
ATOM   2456  C  CB   . ASP   A  1  162 ? 23.193  -20.978 -33.624  1.00 53.31  ? 162  ASP   A CB   1 
ATOM   2457  C  CG   . ASP   A  1  162 ? 24.062  -19.735 -33.557  1.00 56.14  ? 162  ASP   A CG   1 
ATOM   2458  O  OD1  . ASP   A  1  162 ? 23.806  -18.785 -34.326  1.00 58.81  ? 162  ASP   A OD1  1 
ATOM   2459  O  OD2  . ASP   A  1  162 ? 24.996  -19.705 -32.728  1.00 59.63  ? 162  ASP   A OD2  1 
ATOM   2460  H  H    . ASP   A  1  162 ? 20.772  -22.327 -34.761  1.00 60.10  ? 162  ASP   A H    1 
ATOM   2461  H  HA   . ASP   A  1  162 ? 21.640  -19.876 -34.390  1.00 62.58  ? 162  ASP   A HA   1 
ATOM   2462  H  HB2  . ASP   A  1  162 ? 22.907  -21.194 -32.723  1.00 64.01  ? 162  ASP   A HB2  1 
ATOM   2463  H  HB3  . ASP   A  1  162 ? 23.730  -21.702 -33.984  1.00 64.01  ? 162  ASP   A HB3  1 
ATOM   2464  N  N    . PHE   A  1  163 ? 22.918  -19.969 -36.571  1.00 59.11  ? 163  PHE   A N    1 
ATOM   2465  C  CA   . PHE   A  1  163 ? 23.432  -20.039 -37.932  1.00 59.18  ? 163  PHE   A CA   1 
ATOM   2466  C  C    . PHE   A  1  163 ? 24.941  -20.254 -37.901  1.00 60.34  ? 163  PHE   A C    1 
ATOM   2467  O  O    . PHE   A  1  163 ? 25.634  -19.720 -37.030  1.00 62.53  ? 163  PHE   A O    1 
ATOM   2468  C  CB   . PHE   A  1  163 ? 23.132  -18.756 -38.714  1.00 59.13  ? 163  PHE   A CB   1 
ATOM   2469  C  CG   . PHE   A  1  163 ? 21.703  -18.624 -39.166  1.00 58.59  ? 163  PHE   A CG   1 
ATOM   2470  C  CD1  . PHE   A  1  163 ? 21.258  -19.273 -40.306  1.00 59.56  ? 163  PHE   A CD1  1 
ATOM   2471  C  CD2  . PHE   A  1  163 ? 20.815  -17.822 -38.468  1.00 58.05  ? 163  PHE   A CD2  1 
ATOM   2472  C  CE1  . PHE   A  1  163 ? 19.947  -19.140 -40.730  1.00 59.73  ? 163  PHE   A CE1  1 
ATOM   2473  C  CE2  . PHE   A  1  163 ? 19.505  -17.685 -38.888  1.00 59.84  ? 163  PHE   A CE2  1 
ATOM   2474  C  CZ   . PHE   A  1  163 ? 19.072  -18.344 -40.020  1.00 59.09  ? 163  PHE   A CZ   1 
ATOM   2475  H  H    . PHE   A  1  163 ? 23.048  -19.206 -36.196  1.00 70.97  ? 163  PHE   A H    1 
ATOM   2476  H  HA   . PHE   A  1  163 ? 23.008  -20.783 -38.388  1.00 71.05  ? 163  PHE   A HA   1 
ATOM   2477  H  HB2  . PHE   A  1  163 ? 23.332  -17.995 -38.148  1.00 71.00  ? 163  PHE   A HB2  1 
ATOM   2478  H  HB3  . PHE   A  1  163 ? 23.692  -18.738 -39.505  1.00 71.00  ? 163  PHE   A HB3  1 
ATOM   2479  H  HD1  . PHE   A  1  163 ? 21.846  -19.805 -40.792  1.00 71.51  ? 163  PHE   A HD1  1 
ATOM   2480  H  HD2  . PHE   A  1  163 ? 21.104  -17.370 -37.708  1.00 69.70  ? 163  PHE   A HD2  1 
ATOM   2481  H  HE1  . PHE   A  1  163 ? 19.657  -19.586 -41.493  1.00 71.71  ? 163  PHE   A HE1  1 
ATOM   2482  H  HE2  . PHE   A  1  163 ? 18.917  -17.149 -38.407  1.00 71.84  ? 163  PHE   A HE2  1 
ATOM   2483  H  HZ   . PHE   A  1  163 ? 18.191  -18.252 -40.304  1.00 70.95  ? 163  PHE   A HZ   1 
ATOM   2484  N  N    . THR   A  1  164 ? 25.446  -21.031 -38.853  1.00 59.27  ? 164  THR   A N    1 
ATOM   2485  C  CA   . THR   A  1  164 ? 26.880  -21.097 -39.085  1.00 58.82  ? 164  THR   A CA   1 
ATOM   2486  C  C    . THR   A  1  164 ? 27.273  -20.024 -40.095  1.00 63.12  ? 164  THR   A C    1 
ATOM   2487  O  O    . THR   A  1  164 ? 26.440  -19.512 -40.848  1.00 63.00  ? 164  THR   A O    1 
ATOM   2488  C  CB   . THR   A  1  164 ? 27.309  -22.473 -39.600  1.00 55.88  ? 164  THR   A CB   1 
ATOM   2489  O  OG1  . THR   A  1  164 ? 27.025  -22.576 -41.000  1.00 53.27  ? 164  THR   A OG1  1 
ATOM   2490  C  CG2  . THR   A  1  164 ? 26.586  -23.586 -38.852  1.00 55.57  ? 164  THR   A CG2  1 
ATOM   2491  H  H    . THR   A  1  164 ? 24.977  -21.527 -39.376  1.00 71.16  ? 164  THR   A H    1 
ATOM   2492  H  HA   . THR   A  1  164 ? 27.348  -20.949 -38.249  1.00 70.62  ? 164  THR   A HA   1 
ATOM   2493  H  HB   . THR   A  1  164 ? 28.262  -22.583 -39.454  1.00 67.09  ? 164  THR   A HB   1 
ATOM   2494  H  HG1  . THR   A  1  164 ? 27.479  -23.195 -41.340  1.00 63.96  ? 164  THR   A HG1  1 
ATOM   2495  H  HG21 . THR   A  1  164 ? 26.902  -24.451 -39.158  1.00 66.72  ? 164  THR   A HG21 1 
ATOM   2496  H  HG22 . THR   A  1  164 ? 26.753  -23.509 -37.900  1.00 66.72  ? 164  THR   A HG22 1 
ATOM   2497  H  HG23 . THR   A  1  164 ? 25.631  -23.526 -39.010  1.00 66.72  ? 164  THR   A HG23 1 
ATOM   2498  N  N    . LYS   A  1  165 ? 28.563  -19.684 -40.108  1.00 70.25  ? 165  LYS   A N    1 
ATOM   2499  C  CA   . LYS   A  1  165 ? 29.018  -18.622 -40.997  1.00 80.64  ? 165  LYS   A CA   1 
ATOM   2500  C  C    . LYS   A  1  165 ? 28.824  -18.981 -42.464  1.00 79.26  ? 165  LYS   A C    1 
ATOM   2501  O  O    . LYS   A  1  165 ? 28.842  -18.087 -43.317  1.00 77.56  ? 165  LYS   A O    1 
ATOM   2502  C  CB   . LYS   A  1  165 ? 30.487  -18.290 -40.726  1.00 88.99  ? 165  LYS   A CB   1 
ATOM   2503  C  CG   . LYS   A  1  165 ? 31.499  -19.283 -41.276  1.00 95.88  ? 165  LYS   A CG   1 
ATOM   2504  C  CD   . LYS   A  1  165 ? 32.899  -18.701 -41.181  1.00 103.74 ? 165  LYS   A CD   1 
ATOM   2505  C  CE   . LYS   A  1  165 ? 33.934  -19.616 -41.795  1.00 111.17 ? 165  LYS   A CE   1 
ATOM   2506  N  NZ   . LYS   A  1  165 ? 35.300  -19.022 -41.752  1.00 117.64 ? 165  LYS   A NZ   1 
ATOM   2507  H  H    . LYS   A  1  165 ? 29.176  -20.045 -39.625  1.00 84.34  ? 165  LYS   A H    1 
ATOM   2508  H  HA   . LYS   A  1  165 ? 28.499  -17.823 -40.813  1.00 96.81  ? 165  LYS   A HA   1 
ATOM   2509  H  HB2  . LYS   A  1  165 ? 30.683  -17.428 -41.127  1.00 106.82 ? 165  LYS   A HB2  1 
ATOM   2510  H  HB3  . LYS   A  1  165 ? 30.618  -18.247 -39.766  1.00 106.82 ? 165  LYS   A HB3  1 
ATOM   2511  H  HG2  . LYS   A  1  165 ? 31.467  -20.103 -40.760  1.00 115.09 ? 165  LYS   A HG2  1 
ATOM   2512  H  HG3  . LYS   A  1  165 ? 31.302  -19.470 -42.208  1.00 115.09 ? 165  LYS   A HG3  1 
ATOM   2513  H  HD2  . LYS   A  1  165 ? 32.925  -17.854 -41.653  1.00 124.52 ? 165  LYS   A HD2  1 
ATOM   2514  H  HD3  . LYS   A  1  165 ? 33.127  -18.568 -40.248  1.00 124.52 ? 165  LYS   A HD3  1 
ATOM   2515  H  HE2  . LYS   A  1  165 ? 33.952  -20.453 -41.305  1.00 133.44 ? 165  LYS   A HE2  1 
ATOM   2516  H  HE3  . LYS   A  1  165 ? 33.704  -19.781 -42.723  1.00 133.44 ? 165  LYS   A HE3  1 
ATOM   2517  H  HZ1  . LYS   A  1  165 ? 35.892  -19.594 -42.090  1.00 141.20 ? 165  LYS   A HZ1  1 
ATOM   2518  H  HZ2  . LYS   A  1  165 ? 35.320  -18.270 -42.228  1.00 141.20 ? 165  LYS   A HZ2  1 
ATOM   2519  H  HZ3  . LYS   A  1  165 ? 35.525  -18.837 -40.911  1.00 141.20 ? 165  LYS   A HZ3  1 
ATOM   2520  N  N    . ALA   A  1  166 ? 28.636  -20.265 -42.777  1.00 74.88  ? 166  ALA   A N    1 
ATOM   2521  C  CA   . ALA   A  1  166 ? 28.464  -20.730 -44.148  1.00 71.72  ? 166  ALA   A CA   1 
ATOM   2522  C  C    . ALA   A  1  166 ? 27.010  -21.056 -44.473  1.00 76.50  ? 166  ALA   A C    1 
ATOM   2523  O  O    . ALA   A  1  166 ? 26.740  -21.911 -45.323  1.00 77.14  ? 166  ALA   A O    1 
ATOM   2524  C  CB   . ALA   A  1  166 ? 29.346  -21.952 -44.403  1.00 64.82  ? 166  ALA   A CB   1 
ATOM   2525  H  H    . ALA   A  1  166 ? 28.604  -20.898 -42.196  1.00 89.90  ? 166  ALA   A H    1 
ATOM   2526  H  HA   . ALA   A  1  166 ? 28.746  -20.021 -44.746  1.00 86.10  ? 166  ALA   A HA   1 
ATOM   2527  H  HB1  . ALA   A  1  166 ? 29.226  -22.241 -45.321  1.00 77.82  ? 166  ALA   A HB1  1 
ATOM   2528  H  HB2  . ALA   A  1  166 ? 30.273  -21.709 -44.251  1.00 77.82  ? 166  ALA   A HB2  1 
ATOM   2529  H  HB3  . ALA   A  1  166 ? 29.085  -22.662 -43.796  1.00 77.82  ? 166  ALA   A HB3  1 
ATOM   2530  N  N    . ASP   A  1  167 ? 26.066  -20.393 -43.808  1.00 82.43  ? 167  ASP   A N    1 
ATOM   2531  C  CA   . ASP   A  1  167 ? 24.643  -20.553 -44.100  1.00 91.84  ? 167  ASP   A CA   1 
ATOM   2532  C  C    . ASP   A  1  167 ? 24.201  -22.007 -43.936  1.00 87.23  ? 167  ASP   A C    1 
ATOM   2533  O  O    . ASP   A  1  167 ? 23.550  -22.590 -44.805  1.00 89.98  ? 167  ASP   A O    1 
ATOM   2534  C  CB   . ASP   A  1  167 ? 24.319  -20.033 -45.501  1.00 104.87 ? 167  ASP   A CB   1 
ATOM   2535  C  CG   . ASP   A  1  167 ? 24.430  -18.528 -45.597  1.00 118.97 ? 167  ASP   A CG   1 
ATOM   2536  O  OD1  . ASP   A  1  167 ? 23.649  -17.837 -44.918  1.00 122.08 ? 167  ASP   A OD1  1 
ATOM   2537  O  OD2  . ASP   A  1  167 ? 25.308  -18.037 -46.336  1.00 124.14 ? 167  ASP   A OD2  1 
ATOM   2538  H  H    . ASP   A  1  167 ? 26.227  -19.837 -43.172  1.00 98.95  ? 167  ASP   A H    1 
ATOM   2539  H  HA   . ASP   A  1  167 ? 24.137  -20.030 -43.458  1.00 110.25 ? 167  ASP   A HA   1 
ATOM   2540  H  HB2  . ASP   A  1  167 ? 24.940  -20.422 -46.136  1.00 125.88 ? 167  ASP   A HB2  1 
ATOM   2541  H  HB3  . ASP   A  1  167 ? 23.410  -20.282 -45.730  1.00 125.88 ? 167  ASP   A HB3  1 
ATOM   2542  N  N    . ARG   A  1  168 ? 24.583  -22.597 -42.809  1.00 76.12  ? 168  ARG   A N    1 
ATOM   2543  C  CA   . ARG   A  1  168 ? 23.964  -23.806 -42.295  1.00 65.82  ? 168  ARG   A CA   1 
ATOM   2544  C  C    . ARG   A  1  168 ? 23.161  -23.445 -41.054  1.00 63.75  ? 168  ARG   A C    1 
ATOM   2545  O  O    . ARG   A  1  168 ? 23.528  -22.538 -40.301  1.00 65.41  ? 168  ARG   A O    1 
ATOM   2546  C  CB   . ARG   A  1  168 ? 24.998  -24.879 -41.940  1.00 61.38  ? 168  ARG   A CB   1 
ATOM   2547  C  CG   . ARG   A  1  168 ? 25.093  -26.022 -42.938  1.00 60.03  ? 168  ARG   A CG   1 
ATOM   2548  C  CD   . ARG   A  1  168 ? 25.971  -27.149 -42.413  1.00 60.28  ? 168  ARG   A CD   1 
ATOM   2549  N  NE   . ARG   A  1  168 ? 26.165  -28.200 -43.410  1.00 65.42  ? 168  ARG   A NE   1 
ATOM   2550  C  CZ   . ARG   A  1  168 ? 25.331  -29.217 -43.607  1.00 67.90  ? 168  ARG   A CZ   1 
ATOM   2551  N  NH1  . ARG   A  1  168 ? 24.228  -29.338 -42.880  1.00 66.00  ? 168  ARG   A NH1  1 
ATOM   2552  N  NH2  . ARG   A  1  168 ? 25.601  -30.119 -44.541  1.00 73.41  ? 168  ARG   A NH2  1 
ATOM   2553  H  H    . ARG   A  1  168 ? 25.220  -22.304 -42.310  1.00 91.39  ? 168  ARG   A H    1 
ATOM   2554  H  HA   . ARG   A  1  168 ? 23.379  -24.187 -42.970  1.00 79.02  ? 168  ARG   A HA   1 
ATOM   2555  H  HB2  . ARG   A  1  168 ? 25.872  -24.461 -41.890  1.00 73.69  ? 168  ARG   A HB2  1 
ATOM   2556  H  HB3  . ARG   A  1  168 ? 24.764  -25.261 -41.079  1.00 73.69  ? 168  ARG   A HB3  1 
ATOM   2557  H  HG2  . ARG   A  1  168 ? 24.206  -26.378 -43.104  1.00 72.08  ? 168  ARG   A HG2  1 
ATOM   2558  H  HG3  . ARG   A  1  168 ? 25.479  -25.695 -43.766  1.00 72.08  ? 168  ARG   A HG3  1 
ATOM   2559  H  HD2  . ARG   A  1  168 ? 26.841  -26.792 -42.176  1.00 72.37  ? 168  ARG   A HD2  1 
ATOM   2560  H  HD3  . ARG   A  1  168 ? 25.551  -27.545 -41.634  1.00 72.37  ? 168  ARG   A HD3  1 
ATOM   2561  H  HE   . ARG   A  1  168 ? 26.868  -28.158 -43.903  1.00 78.54  ? 168  ARG   A HE   1 
ATOM   2562  H  HH11 . ARG   A  1  168 ? 24.047  -28.755 -42.273  1.00 79.23  ? 168  ARG   A HH11 1 
ATOM   2563  H  HH12 . ARG   A  1  168 ? 23.694  -29.998 -43.014  1.00 79.23  ? 168  ARG   A HH12 1 
ATOM   2564  H  HH21 . ARG   A  1  168 ? 26.314  -30.045 -45.017  1.00 88.13  ? 168  ARG   A HH21 1 
ATOM   2565  H  HH22 . ARG   A  1  168 ? 25.064  -30.777 -44.672  1.00 88.13  ? 168  ARG   A HH22 1 
ATOM   2566  N  N    . VAL   A  1  169 ? 22.064  -24.142 -40.855  1.00 57.69  ? 169  VAL   A N    1 
ATOM   2567  C  CA   . VAL   A  1  169 ? 21.287  -24.010 -39.631  1.00 53.27  ? 169  VAL   A CA   1 
ATOM   2568  C  C    . VAL   A  1  169 ? 21.761  -25.073 -38.656  1.00 50.49  ? 169  VAL   A C    1 
ATOM   2569  O  O    . VAL   A  1  169 ? 22.018  -26.217 -39.044  1.00 49.03  ? 169  VAL   A O    1 
ATOM   2570  C  CB   . VAL   A  1  169 ? 19.779  -24.141 -39.914  1.00 53.00  ? 169  VAL   A CB   1 
ATOM   2571  C  CG1  . VAL   A  1  169 ? 19.001  -24.355 -38.617  1.00 50.25  ? 169  VAL   A CG1  1 
ATOM   2572  C  CG2  . VAL   A  1  169 ? 19.272  -22.906 -40.637  1.00 58.91  ? 169  VAL   A CG2  1 
ATOM   2573  H  H    . VAL   A  1  169 ? 21.741  -24.706 -41.417  1.00 69.27  ? 169  VAL   A H    1 
ATOM   2574  H  HA   . VAL   A  1  169 ? 21.438  -23.134 -39.243  1.00 63.96  ? 169  VAL   A HA   1 
ATOM   2575  H  HB   . VAL   A  1  169 ? 19.633  -24.914 -40.481  1.00 63.64  ? 169  VAL   A HB   1 
ATOM   2576  H  HG11 . VAL   A  1  169 ? 18.051  -24.342 -38.813  1.00 60.33  ? 169  VAL   A HG11 1 
ATOM   2577  H  HG12 . VAL   A  1  169 ? 19.249  -25.212 -38.238  1.00 60.33  ? 169  VAL   A HG12 1 
ATOM   2578  H  HG13 . VAL   A  1  169 ? 19.220  -23.642 -37.996  1.00 60.33  ? 169  VAL   A HG13 1 
ATOM   2579  H  HG21 . VAL   A  1  169 ? 18.322  -23.006 -40.806  1.00 70.72  ? 169  VAL   A HG21 1 
ATOM   2580  H  HG22 . VAL   A  1  169 ? 19.429  -22.127 -40.081  1.00 70.72  ? 169  VAL   A HG22 1 
ATOM   2581  H  HG23 . VAL   A  1  169 ? 19.749  -22.814 -41.477  1.00 70.72  ? 169  VAL   A HG23 1 
ATOM   2582  N  N    . LEU   A  1  170 ? 21.905  -24.691 -37.394  1.00 50.18  ? 170  LEU   A N    1 
ATOM   2583  C  CA   . LEU   A  1  170 ? 22.097  -25.638 -36.304  1.00 50.04  ? 170  LEU   A CA   1 
ATOM   2584  C  C    . LEU   A  1  170 ? 20.857  -25.577 -35.426  1.00 51.80  ? 170  LEU   A C    1 
ATOM   2585  O  O    . LEU   A  1  170 ? 20.497  -24.503 -34.931  1.00 55.79  ? 170  LEU   A O    1 
ATOM   2586  C  CB   . LEU   A  1  170 ? 23.353  -25.328 -35.493  1.00 48.34  ? 170  LEU   A CB   1 
ATOM   2587  C  CG   . LEU   A  1  170 ? 23.568  -26.261 -34.297  1.00 48.51  ? 170  LEU   A CG   1 
ATOM   2588  C  CD1  . LEU   A  1  170 ? 23.696  -27.715 -34.747  1.00 46.52  ? 170  LEU   A CD1  1 
ATOM   2589  C  CD2  . LEU   A  1  170 ? 24.788  -25.837 -33.500  1.00 51.45  ? 170  LEU   A CD2  1 
ATOM   2590  H  H    . LEU   A  1  170 ? 21.895  -23.870 -37.138  1.00 60.25  ? 170  LEU   A H    1 
ATOM   2591  H  HA   . LEU   A  1  170 ? 22.202  -26.534 -36.660  1.00 60.09  ? 170  LEU   A HA   1 
ATOM   2592  H  HB2  . LEU   A  1  170 ? 24.126  -25.409 -36.074  1.00 58.04  ? 170  LEU   A HB2  1 
ATOM   2593  H  HB3  . LEU   A  1  170 ? 23.287  -24.422 -35.153  1.00 58.04  ? 170  LEU   A HB3  1 
ATOM   2594  H  HG   . LEU   A  1  170 ? 22.792  -26.202 -33.718  1.00 58.25  ? 170  LEU   A HG   1 
ATOM   2595  H  HD11 . LEU   A  1  170 ? 23.841  -28.275 -33.968  1.00 55.86  ? 170  LEU   A HD11 1 
ATOM   2596  H  HD12 . LEU   A  1  170 ? 22.878  -27.980 -35.197  1.00 55.86  ? 170  LEU   A HD12 1 
ATOM   2597  H  HD13 . LEU   A  1  170 ? 24.448  -27.793 -35.354  1.00 55.86  ? 170  LEU   A HD13 1 
ATOM   2598  H  HD21 . LEU   A  1  170 ? 24.906  -26.447 -32.756  1.00 61.78  ? 170  LEU   A HD21 1 
ATOM   2599  H  HD22 . LEU   A  1  170 ? 25.567  -25.863 -34.077  1.00 61.78  ? 170  LEU   A HD22 1 
ATOM   2600  H  HD23 . LEU   A  1  170 ? 24.651  -24.935 -33.170  1.00 61.78  ? 170  LEU   A HD23 1 
ATOM   2601  N  N    . LEU   A  1  171 ? 20.207  -26.719 -35.243  1.00 51.09  ? 171  LEU   A N    1 
ATOM   2602  C  CA   . LEU   A  1  171 ? 18.938  -26.793 -34.537  1.00 46.31  ? 171  LEU   A CA   1 
ATOM   2603  C  C    . LEU   A  1  171 ? 19.022  -27.851 -33.450  1.00 45.58  ? 171  LEU   A C    1 
ATOM   2604  O  O    . LEU   A  1  171 ? 19.547  -28.945 -33.674  1.00 48.24  ? 171  LEU   A O    1 
ATOM   2605  C  CB   . LEU   A  1  171 ? 17.799  -27.111 -35.510  1.00 46.35  ? 171  LEU   A CB   1 
ATOM   2606  C  CG   . LEU   A  1  171 ? 16.396  -27.225 -34.918  1.00 45.26  ? 171  LEU   A CG   1 
ATOM   2607  C  CD1  . LEU   A  1  171 ? 15.371  -26.716 -35.914  1.00 47.15  ? 171  LEU   A CD1  1 
ATOM   2608  C  CD2  . LEU   A  1  171 ? 16.095  -28.664 -34.537  1.00 41.75  ? 171  LEU   A CD2  1 
ATOM   2609  H  H    . LEU   A  1  171 ? 20.489  -27.481 -35.526  1.00 61.35  ? 171  LEU   A H    1 
ATOM   2610  H  HA   . LEU   A  1  171 ? 18.744  -25.946 -34.107  1.00 55.61  ? 171  LEU   A HA   1 
ATOM   2611  H  HB2  . LEU   A  1  171 ? 17.769  -26.407 -36.176  1.00 55.65  ? 171  LEU   A HB2  1 
ATOM   2612  H  HB3  . LEU   A  1  171 ? 17.996  -27.961 -35.935  1.00 55.65  ? 171  LEU   A HB3  1 
ATOM   2613  H  HG   . LEU   A  1  171 ? 16.342  -26.684 -34.114  1.00 54.35  ? 171  LEU   A HG   1 
ATOM   2614  H  HD11 . LEU   A  1  171 ? 14.485  -26.808 -35.530  1.00 56.61  ? 171  LEU   A HD11 1 
ATOM   2615  H  HD12 . LEU   A  1  171 ? 15.553  -25.782 -36.106  1.00 56.61  ? 171  LEU   A HD12 1 
ATOM   2616  H  HD13 . LEU   A  1  171 ? 15.434  -27.239 -36.728  1.00 56.61  ? 171  LEU   A HD13 1 
ATOM   2617  H  HD21 . LEU   A  1  171 ? 15.186  -28.718 -34.203  1.00 50.13  ? 171  LEU   A HD21 1 
ATOM   2618  H  HD22 . LEU   A  1  171 ? 16.193  -29.225 -35.322  1.00 50.13  ? 171  LEU   A HD22 1 
ATOM   2619  H  HD23 . LEU   A  1  171 ? 16.718  -28.945 -33.849  1.00 50.13  ? 171  LEU   A HD23 1 
ATOM   2620  N  N    . GLY   A  1  172 ? 18.499  -27.518 -32.276  1.00 44.70  ? 172  GLY   A N    1 
ATOM   2621  C  CA   . GLY   A  1  172 ? 18.488  -28.420 -31.134  1.00 43.40  ? 172  GLY   A CA   1 
ATOM   2622  C  C    . GLY   A  1  172 ? 17.071  -28.854 -30.800  1.00 45.60  ? 172  GLY   A C    1 
ATOM   2623  O  O    . GLY   A  1  172 ? 16.134  -28.054 -30.874  1.00 42.98  ? 172  GLY   A O    1 
ATOM   2624  H  H    . GLY   A  1  172 ? 18.136  -26.756 -32.113  1.00 53.68  ? 172  GLY   A H    1 
ATOM   2625  H  HA2  . GLY   A  1  172 ? 19.016  -29.209 -31.334  1.00 52.12  ? 172  GLY   A HA2  1 
ATOM   2626  H  HA3  . GLY   A  1  172 ? 18.868  -27.974 -30.361  1.00 52.12  ? 172  GLY   A HA3  1 
ATOM   2627  N  N    . GLY   A  1  173 ? 16.927  -30.126 -30.439  1.00 44.46  ? 173  GLY   A N    1 
ATOM   2628  C  CA   . GLY   A  1  173 ? 15.659  -30.672 -30.019  1.00 47.17  ? 173  GLY   A CA   1 
ATOM   2629  C  C    . GLY   A  1  173 ? 15.851  -31.636 -28.865  1.00 47.06  ? 173  GLY   A C    1 
ATOM   2630  O  O    . GLY   A  1  173 ? 16.233  -32.794 -29.055  1.00 45.58  ? 173  GLY   A O    1 
ATOM   2631  H  H    . GLY   A  1  173 ? 17.568  -30.699 -30.432  1.00 53.39  ? 173  GLY   A H    1 
ATOM   2632  H  HA2  . GLY   A  1  173 ? 15.071  -29.955 -29.735  1.00 56.64  ? 173  GLY   A HA2  1 
ATOM   2633  H  HA3  . GLY   A  1  173 ? 15.245  -31.146 -30.758  1.00 56.64  ? 173  GLY   A HA3  1 
ATOM   2634  N  N    . PRO   A  1  174 ? 15.590  -31.178 -27.635  1.00 44.42  ? 174  PRO   A N    1 
ATOM   2635  C  CA   . PRO   A  1  174 ? 16.000  -31.954 -26.456  1.00 42.77  ? 174  PRO   A CA   1 
ATOM   2636  C  C    . PRO   A  1  174 ? 15.198  -33.221 -26.205  1.00 42.25  ? 174  PRO   A C    1 
ATOM   2637  O  O    . PRO   A  1  174 ? 15.516  -33.944 -25.254  1.00 41.54  ? 174  PRO   A O    1 
ATOM   2638  C  CB   . PRO   A  1  174 ? 15.807  -30.956 -25.303  1.00 48.11  ? 174  PRO   A CB   1 
ATOM   2639  C  CG   . PRO   A  1  174 ? 14.743  -30.033 -25.782  1.00 50.53  ? 174  PRO   A CG   1 
ATOM   2640  C  CD   . PRO   A  1  174 ? 14.956  -29.899 -27.260  1.00 47.30  ? 174  PRO   A CD   1 
ATOM   2641  H  HA   . PRO   A  1  174 ? 16.938  -32.190 -26.536  1.00 51.36  ? 174  PRO   A HA   1 
ATOM   2642  H  HB2  . PRO   A  1  174 ? 15.527  -31.424 -24.501  1.00 57.77  ? 174  PRO   A HB2  1 
ATOM   2643  H  HB3  . PRO   A  1  174 ? 16.635  -30.478 -25.136  1.00 57.77  ? 174  PRO   A HB3  1 
ATOM   2644  H  HG2  . PRO   A  1  174 ? 13.871  -30.412 -25.593  1.00 60.67  ? 174  PRO   A HG2  1 
ATOM   2645  H  HG3  . PRO   A  1  174 ? 14.833  -29.173 -25.343  1.00 60.67  ? 174  PRO   A HG3  1 
ATOM   2646  H  HD2  . PRO   A  1  174 ? 14.109  -29.787 -27.721  1.00 56.80  ? 174  PRO   A HD2  1 
ATOM   2647  H  HD3  . PRO   A  1  174 ? 15.543  -29.153 -27.458  1.00 56.80  ? 174  PRO   A HD3  1 
ATOM   2648  N  N    . GLY   A  1  175 ? 14.189  -33.535 -27.014  1.00 43.03  ? 175  GLY   A N    1 
ATOM   2649  C  CA   . GLY   A  1  175 ? 13.295  -34.627 -26.680  1.00 40.91  ? 175  GLY   A CA   1 
ATOM   2650  C  C    . GLY   A  1  175 ? 13.485  -35.913 -27.459  1.00 40.88  ? 175  GLY   A C    1 
ATOM   2651  O  O    . GLY   A  1  175 ? 12.898  -36.940 -27.106  1.00 41.30  ? 175  GLY   A O    1 
ATOM   2652  H  H    . GLY   A  1  175 ? 14.008  -33.133 -27.753  1.00 51.67  ? 175  GLY   A H    1 
ATOM   2653  H  HA2  . GLY   A  1  175 ? 13.410  -34.839 -25.740  1.00 49.13  ? 175  GLY   A HA2  1 
ATOM   2654  H  HA3  . GLY   A  1  175 ? 12.383  -34.332 -26.828  1.00 49.13  ? 175  GLY   A HA3  1 
ATOM   2655  N  N    . SER   A  1  176 ? 14.303  -35.883 -28.508  1.00 41.74  ? 176  SER   A N    1 
ATOM   2656  C  CA   . SER   A  1  176 ? 14.429  -37.043 -29.380  1.00 44.07  ? 176  SER   A CA   1 
ATOM   2657  C  C    . SER   A  1  176 ? 14.932  -38.261 -28.614  1.00 44.22  ? 176  SER   A C    1 
ATOM   2658  O  O    . SER   A  1  176 ? 15.769  -38.152 -27.714  1.00 42.98  ? 176  SER   A O    1 
ATOM   2659  C  CB   . SER   A  1  176 ? 15.382  -36.737 -30.537  1.00 47.45  ? 176  SER   A CB   1 
ATOM   2660  O  OG   . SER   A  1  176 ? 14.831  -35.782 -31.424  1.00 47.02  ? 176  SER   A OG   1 
ATOM   2661  H  H    . SER   A  1  176 ? 14.789  -35.211 -28.734  1.00 50.13  ? 176  SER   A H    1 
ATOM   2662  H  HA   . SER   A  1  176 ? 13.554  -37.254 -29.743  1.00 52.92  ? 176  SER   A HA   1 
ATOM   2663  H  HB2  . SER   A  1  176 ? 16.212  -36.387 -30.176  1.00 56.97  ? 176  SER   A HB2  1 
ATOM   2664  H  HB3  . SER   A  1  176 ? 15.554  -37.557 -31.027  1.00 56.97  ? 176  SER   A HB3  1 
ATOM   2665  H  HG   . SER   A  1  176 ? 14.749  -35.042 -31.034  1.00 56.46  ? 176  SER   A HG   1 
ATOM   2666  N  N    . PHE   A  1  177 ? 14.406  -39.431 -28.980  1.00 45.54  ? 177  PHE   A N    1 
ATOM   2667  C  CA   . PHE   A  1  177 ? 14.922  -40.717 -28.517  1.00 49.29  ? 177  PHE   A CA   1 
ATOM   2668  C  C    . PHE   A  1  177 ? 14.862  -40.815 -26.991  1.00 53.36  ? 177  PHE   A C    1 
ATOM   2669  O  O    . PHE   A  1  177 ? 15.872  -40.984 -26.306  1.00 50.71  ? 177  PHE   A O    1 
ATOM   2670  C  CB   . PHE   A  1  177 ? 16.347  -40.926 -29.039  1.00 50.17  ? 177  PHE   A CB   1 
ATOM   2671  C  CG   . PHE   A  1  177 ? 16.532  -40.492 -30.467  1.00 52.51  ? 177  PHE   A CG   1 
ATOM   2672  C  CD1  . PHE   A  1  177 ? 15.592  -40.817 -31.432  1.00 53.59  ? 177  PHE   A CD1  1 
ATOM   2673  C  CD2  . PHE   A  1  177 ? 17.638  -39.746 -30.842  1.00 53.62  ? 177  PHE   A CD2  1 
ATOM   2674  C  CE1  . PHE   A  1  177 ? 15.757  -40.417 -32.746  1.00 54.09  ? 177  PHE   A CE1  1 
ATOM   2675  C  CE2  . PHE   A  1  177 ? 17.807  -39.340 -32.154  1.00 53.39  ? 177  PHE   A CE2  1 
ATOM   2676  C  CZ   . PHE   A  1  177 ? 16.865  -39.676 -33.106  1.00 52.74  ? 177  PHE   A CZ   1 
ATOM   2677  H  H    . PHE   A  1  177 ? 13.732  -39.506 -29.510  1.00 54.69  ? 177  PHE   A H    1 
ATOM   2678  H  HA   . PHE   A  1  177 ? 14.360  -41.427 -28.865  1.00 59.19  ? 177  PHE   A HA   1 
ATOM   2679  H  HB2  . PHE   A  1  177 ? 16.959  -40.412 -28.490  1.00 60.24  ? 177  PHE   A HB2  1 
ATOM   2680  H  HB3  . PHE   A  1  177 ? 16.564  -41.870 -28.984  1.00 60.24  ? 177  PHE   A HB3  1 
ATOM   2681  H  HD1  . PHE   A  1  177 ? 14.840  -41.310 -31.194  1.00 64.35  ? 177  PHE   A HD1  1 
ATOM   2682  H  HD2  . PHE   A  1  177 ? 18.274  -39.514 -30.204  1.00 64.38  ? 177  PHE   A HD2  1 
ATOM   2683  H  HE1  . PHE   A  1  177 ? 15.123  -40.647 -33.386  1.00 64.94  ? 177  PHE   A HE1  1 
ATOM   2684  H  HE2  . PHE   A  1  177 ? 18.555  -38.842 -32.395  1.00 64.10  ? 177  PHE   A HE2  1 
ATOM   2685  H  HZ   . PHE   A  1  177 ? 16.977  -39.403 -33.989  1.00 63.33  ? 177  PHE   A HZ   1 
ATOM   2686  N  N    . TYR   A  1  178 ? 13.640  -40.721 -26.471  1.00 49.28  ? 178  TYR   A N    1 
ATOM   2687  C  CA   . TYR   A  1  178 ? 13.392  -40.700 -25.031  1.00 46.05  ? 178  TYR   A CA   1 
ATOM   2688  C  C    . TYR   A  1  178 ? 14.285  -39.668 -24.344  1.00 41.94  ? 178  TYR   A C    1 
ATOM   2689  O  O    . TYR   A  1  178 ? 15.019  -39.959 -23.396  1.00 41.66  ? 178  TYR   A O    1 
ATOM   2690  C  CB   . TYR   A  1  178 ? 13.562  -42.093 -24.423  1.00 48.60  ? 178  TYR   A CB   1 
ATOM   2691  C  CG   . TYR   A  1  178 ? 12.247  -42.832 -24.311  1.00 53.62  ? 178  TYR   A CG   1 
ATOM   2692  C  CD1  . TYR   A  1  178 ? 11.321  -42.487 -23.335  1.00 55.53  ? 178  TYR   A CD1  1 
ATOM   2693  C  CD2  . TYR   A  1  178 ? 11.921  -43.857 -25.187  1.00 56.81  ? 178  TYR   A CD2  1 
ATOM   2694  C  CE1  . TYR   A  1  178 ? 10.112  -43.147 -23.229  1.00 58.35  ? 178  TYR   A CE1  1 
ATOM   2695  C  CE2  . TYR   A  1  178 ? 10.712  -44.524 -25.087  1.00 59.83  ? 178  TYR   A CE2  1 
ATOM   2696  C  CZ   . TYR   A  1  178 ? 9.813   -44.164 -24.108  1.00 62.33  ? 178  TYR   A CZ   1 
ATOM   2697  O  OH   . TYR   A  1  178 ? 8.610   -44.825 -24.007  1.00 66.98  ? 178  TYR   A OH   1 
ATOM   2698  H  H    . TYR   A  1  178 ? 12.922  -40.667 -26.942  1.00 59.18  ? 178  TYR   A H    1 
ATOM   2699  H  HA   . TYR   A  1  178 ? 12.472  -40.432 -24.878  1.00 55.30  ? 178  TYR   A HA   1 
ATOM   2700  H  HB2  . TYR   A  1  178 ? 14.156  -42.615 -24.984  1.00 58.36  ? 178  TYR   A HB2  1 
ATOM   2701  H  HB3  . TYR   A  1  178 ? 13.938  -42.008 -23.532  1.00 58.36  ? 178  TYR   A HB3  1 
ATOM   2702  H  HD1  . TYR   A  1  178 ? 11.519  -41.799 -22.741  1.00 66.67  ? 178  TYR   A HD1  1 
ATOM   2703  H  HD2  . TYR   A  1  178 ? 12.524  -44.100 -25.852  1.00 68.20  ? 178  TYR   A HD2  1 
ATOM   2704  H  HE1  . TYR   A  1  178 ? 9.504   -42.905 -22.568  1.00 70.06  ? 178  TYR   A HE1  1 
ATOM   2705  H  HE2  . TYR   A  1  178 ? 10.508  -45.211 -25.679  1.00 71.83  ? 178  TYR   A HE2  1 
ATOM   2706  H  HH   . TYR   A  1  178 ? 8.539   -45.387 -24.628  1.00 80.41  ? 178  TYR   A HH   1 
ATOM   2707  N  N    . TRP   A  1  179 ? 14.212  -38.439 -24.851  1.00 42.17  ? 179  TRP   A N    1 
ATOM   2708  C  CA   . TRP   A  1  179 ? 14.864  -37.270 -24.268  1.00 39.79  ? 179  TRP   A CA   1 
ATOM   2709  C  C    . TRP   A  1  179 ? 16.376  -37.421 -24.182  1.00 40.16  ? 179  TRP   A C    1 
ATOM   2710  O  O    . TRP   A  1  179 ? 17.027  -36.751 -23.372  1.00 40.10  ? 179  TRP   A O    1 
ATOM   2711  C  CB   . TRP   A  1  179 ? 14.257  -36.946 -22.899  1.00 38.70  ? 179  TRP   A CB   1 
ATOM   2712  C  CG   . TRP   A  1  179 ? 12.868  -36.431 -23.067  1.00 37.21  ? 179  TRP   A CG   1 
ATOM   2713  C  CD1  . TRP   A  1  179 ? 12.498  -35.137 -23.283  1.00 38.81  ? 179  TRP   A CD1  1 
ATOM   2714  C  CD2  . TRP   A  1  179 ? 11.661  -37.202 -23.082  1.00 39.92  ? 179  TRP   A CD2  1 
ATOM   2715  N  NE1  . TRP   A  1  179 ? 11.135  -35.051 -23.423  1.00 41.39  ? 179  TRP   A NE1  1 
ATOM   2716  C  CE2  . TRP   A  1  179 ? 10.597  -36.305 -23.300  1.00 41.02  ? 179  TRP   A CE2  1 
ATOM   2717  C  CE3  . TRP   A  1  179 ? 11.376  -38.562 -22.925  1.00 42.69  ? 179  TRP   A CE3  1 
ATOM   2718  C  CZ2  . TRP   A  1  179 ? 9.270   -36.722 -23.362  1.00 40.92  ? 179  TRP   A CZ2  1 
ATOM   2719  C  CZ3  . TRP   A  1  179 ? 10.057  -38.974 -22.986  1.00 44.48  ? 179  TRP   A CZ3  1 
ATOM   2720  C  CH2  . TRP   A  1  179 ? 9.021   -38.058 -23.203  1.00 44.07  ? 179  TRP   A CH2  1 
ATOM   2721  H  H    . TRP   A  1  179 ? 13.771  -38.250 -25.565  1.00 50.64  ? 179  TRP   A H    1 
ATOM   2722  H  HA   . TRP   A  1  179 ? 14.708  -36.509 -24.849  1.00 47.78  ? 179  TRP   A HA   1 
ATOM   2723  H  HB2  . TRP   A  1  179 ? 14.229  -37.749 -22.355  1.00 46.47  ? 179  TRP   A HB2  1 
ATOM   2724  H  HB3  . TRP   A  1  179 ? 14.791  -36.266 -22.459  1.00 46.47  ? 179  TRP   A HB3  1 
ATOM   2725  H  HD1  . TRP   A  1  179 ? 13.084  -34.417 -23.330  1.00 46.61  ? 179  TRP   A HD1  1 
ATOM   2726  H  HE1  . TRP   A  1  179 ? 10.691  -34.328 -23.564  1.00 49.70  ? 179  TRP   A HE1  1 
ATOM   2727  H  HE3  . TRP   A  1  179 ? 12.060  -39.177 -22.783  1.00 51.27  ? 179  TRP   A HE3  1 
ATOM   2728  H  HZ2  . TRP   A  1  179 ? 8.580   -36.116 -23.505  1.00 49.14  ? 179  TRP   A HZ2  1 
ATOM   2729  H  HZ3  . TRP   A  1  179 ? 9.855   -39.876 -22.880  1.00 53.42  ? 179  TRP   A HZ3  1 
ATOM   2730  H  HH2  . TRP   A  1  179 ? 8.144   -38.364 -23.241  1.00 52.92  ? 179  TRP   A HH2  1 
ATOM   2731  N  N    . GLN   A  1  180 ? 16.953  -38.288 -25.016  1.00 40.75  ? 180  GLN   A N    1 
ATOM   2732  C  CA   . GLN   A  1  180 ? 18.386  -38.208 -25.269  1.00 41.13  ? 180  GLN   A CA   1 
ATOM   2733  C  C    . GLN   A  1  180 ? 18.749  -36.851 -25.856  1.00 39.88  ? 180  GLN   A C    1 
ATOM   2734  O  O    . GLN   A  1  180 ? 19.799  -36.283 -25.534  1.00 45.32  ? 180  GLN   A O    1 
ATOM   2735  C  CB   . GLN   A  1  180 ? 18.822  -39.324 -26.220  1.00 41.73  ? 180  GLN   A CB   1 
ATOM   2736  C  CG   . GLN   A  1  180 ? 18.823  -40.719 -25.613  1.00 39.97  ? 180  GLN   A CG   1 
ATOM   2737  C  CD   . GLN   A  1  180 ? 19.314  -41.775 -26.587  1.00 43.55  ? 180  GLN   A CD   1 
ATOM   2738  O  OE1  . GLN   A  1  180 ? 19.854  -41.454 -27.647  1.00 45.70  ? 180  GLN   A OE1  1 
ATOM   2739  N  NE2  . GLN   A  1  180 ? 19.129  -43.042 -26.233  1.00 44.86  ? 180  GLN   A NE2  1 
ATOM   2740  H  H    . GLN   A  1  180 ? 16.545  -38.916 -25.438  1.00 48.93  ? 180  GLN   A H    1 
ATOM   2741  H  HA   . GLN   A  1  180 ? 18.860  -38.327 -24.432  1.00 49.39  ? 180  GLN   A HA   1 
ATOM   2742  H  HB2  . GLN   A  1  180 ? 18.215  -39.337 -26.978  1.00 50.11  ? 180  GLN   A HB2  1 
ATOM   2743  H  HB3  . GLN   A  1  180 ? 19.724  -39.137 -26.521  1.00 50.11  ? 180  GLN   A HB3  1 
ATOM   2744  H  HG2  . GLN   A  1  180 ? 19.407  -40.728 -24.839  1.00 48.00  ? 180  GLN   A HG2  1 
ATOM   2745  H  HG3  . GLN   A  1  180 ? 17.919  -40.951 -25.349  1.00 48.00  ? 180  GLN   A HG3  1 
ATOM   2746  H  HE21 . GLN   A  1  180 ? 18.747  -43.228 -25.486  1.00 53.87  ? 180  GLN   A HE21 1 
ATOM   2747  H  HE22 . GLN   A  1  180 ? 19.390  -43.676 -26.752  1.00 53.87  ? 180  GLN   A HE22 1 
ATOM   2748  N  N    . GLY   A  1  181 ? 17.883  -36.310 -26.710  1.00 42.17  ? 181  GLY   A N    1 
ATOM   2749  C  CA   . GLY   A  1  181 ? 18.164  -35.085 -27.424  1.00 46.47  ? 181  GLY   A CA   1 
ATOM   2750  C  C    . GLY   A  1  181 ? 18.807  -35.351 -28.772  1.00 47.35  ? 181  GLY   A C    1 
ATOM   2751  O  O    . GLY   A  1  181 ? 19.162  -36.479 -29.124  1.00 48.77  ? 181  GLY   A O    1 
ATOM   2752  H  H    . GLY   A  1  181 ? 17.113  -36.646 -26.892  1.00 50.65  ? 181  GLY   A H    1 
ATOM   2753  H  HA2  . GLY   A  1  181 ? 17.337  -34.598 -27.568  1.00 55.80  ? 181  GLY   A HA2  1 
ATOM   2754  H  HA3  . GLY   A  1  181 ? 18.767  -34.535 -26.899  1.00 55.80  ? 181  GLY   A HA3  1 
ATOM   2755  N  N    . GLN   A  1  182 ? 18.965  -34.280 -29.544  1.00 47.43  ? 182  GLN   A N    1 
ATOM   2756  C  CA   . GLN   A  1  182 ? 19.446  -34.433 -30.909  1.00 46.09  ? 182  GLN   A CA   1 
ATOM   2757  C  C    . GLN   A  1  182 ? 19.843  -33.077 -31.467  1.00 45.25  ? 182  GLN   A C    1 
ATOM   2758  O  O    . GLN   A  1  182 ? 19.209  -32.064 -31.162  1.00 44.60  ? 182  GLN   A O    1 
ATOM   2759  C  CB   . GLN   A  1  182 ? 18.366  -35.077 -31.790  1.00 46.73  ? 182  GLN   A CB   1 
ATOM   2760  C  CG   . GLN   A  1  182 ? 18.766  -35.300 -33.239  1.00 49.77  ? 182  GLN   A CG   1 
ATOM   2761  C  CD   . GLN   A  1  182 ? 17.690  -36.023 -34.026  1.00 50.92  ? 182  GLN   A CD   1 
ATOM   2762  O  OE1  . GLN   A  1  182 ? 16.499  -35.873 -33.752  1.00 51.08  ? 182  GLN   A OE1  1 
ATOM   2763  N  NE2  . GLN   A  1  182 ? 18.104  -36.821 -35.004  1.00 53.28  ? 182  GLN   A NE2  1 
ATOM   2764  H  H    . GLN   A  1  182 ? 18.802  -33.470 -29.304  1.00 56.96  ? 182  GLN   A H    1 
ATOM   2765  H  HA   . GLN   A  1  182 ? 20.237  -34.994 -30.914  1.00 55.35  ? 182  GLN   A HA   1 
ATOM   2766  H  HB2  . GLN   A  1  182 ? 18.139  -35.942 -31.415  1.00 56.12  ? 182  GLN   A HB2  1 
ATOM   2767  H  HB3  . GLN   A  1  182 ? 17.586  -34.500 -31.790  1.00 56.12  ? 182  GLN   A HB3  1 
ATOM   2768  H  HG2  . GLN   A  1  182 ? 18.925  -34.442 -33.661  1.00 59.76  ? 182  GLN   A HG2  1 
ATOM   2769  H  HG3  . GLN   A  1  182 ? 19.573  -35.838 -33.266  1.00 59.76  ? 182  GLN   A HG3  1 
ATOM   2770  H  HE21 . GLN   A  1  182 ? 18.945  -36.906 -35.162  1.00 63.97  ? 182  GLN   A HE21 1 
ATOM   2771  H  HE22 . GLN   A  1  182 ? 17.531  -37.252 -35.479  1.00 63.97  ? 182  GLN   A HE22 1 
ATOM   2772  N  N    . LEU   A  1  183 ? 20.901  -33.070 -32.273  1.00 45.62  ? 183  LEU   A N    1 
ATOM   2773  C  CA   . LEU   A  1  183 ? 21.295  -31.917 -33.067  1.00 43.47  ? 183  LEU   A CA   1 
ATOM   2774  C  C    . LEU   A  1  183 ? 21.074  -32.238 -34.539  1.00 43.99  ? 183  LEU   A C    1 
ATOM   2775  O  O    . LEU   A  1  183 ? 21.398  -33.338 -34.996  1.00 48.46  ? 183  LEU   A O    1 
ATOM   2776  C  CB   . LEU   A  1  183 ? 22.761  -31.549 -32.832  1.00 45.38  ? 183  LEU   A CB   1 
ATOM   2777  C  CG   . LEU   A  1  183 ? 23.166  -31.231 -31.392  1.00 44.75  ? 183  LEU   A CG   1 
ATOM   2778  C  CD1  . LEU   A  1  183 ? 24.635  -30.834 -31.335  1.00 46.21  ? 183  LEU   A CD1  1 
ATOM   2779  C  CD2  . LEU   A  1  183 ? 22.284  -30.137 -30.809  1.00 41.25  ? 183  LEU   A CD2  1 
ATOM   2780  H  H    . LEU   A  1  183 ? 21.422  -33.747 -32.379  1.00 54.78  ? 183  LEU   A H    1 
ATOM   2781  H  HA   . LEU   A  1  183 ? 20.756  -31.149 -32.822  1.00 52.20  ? 183  LEU   A HA   1 
ATOM   2782  H  HB2  . LEU   A  1  183 ? 23.308  -32.295 -33.123  1.00 54.49  ? 183  LEU   A HB2  1 
ATOM   2783  H  HB3  . LEU   A  1  183 ? 22.962  -30.763 -33.364  1.00 54.49  ? 183  LEU   A HB3  1 
ATOM   2784  H  HG   . LEU   A  1  183 ? 23.046  -32.024 -30.847  1.00 53.74  ? 183  LEU   A HG   1 
ATOM   2785  H  HD11 . LEU   A  1  183 ? 24.874  -30.638 -30.416  1.00 55.49  ? 183  LEU   A HD11 1 
ATOM   2786  H  HD12 . LEU   A  1  183 ? 25.174  -31.568 -31.668  1.00 55.49  ? 183  LEU   A HD12 1 
ATOM   2787  H  HD13 . LEU   A  1  183 ? 24.771  -30.047 -31.886  1.00 55.49  ? 183  LEU   A HD13 1 
ATOM   2788  H  HD21 . LEU   A  1  183 ? 22.598  -29.921 -29.917  1.00 49.54  ? 183  LEU   A HD21 1 
ATOM   2789  H  HD22 . LEU   A  1  183 ? 22.337  -29.353 -31.377  1.00 49.54  ? 183  LEU   A HD22 1 
ATOM   2790  H  HD23 . LEU   A  1  183 ? 21.369  -30.457 -30.770  1.00 49.54  ? 183  LEU   A HD23 1 
ATOM   2791  N  N    . ILE   A  1  184 ? 20.515  -31.282 -35.273  1.00 44.27  ? 184  ILE   A N    1 
ATOM   2792  C  CA   . ILE   A  1  184 ? 20.287  -31.419 -36.706  1.00 43.97  ? 184  ILE   A CA   1 
ATOM   2793  C  C    . ILE   A  1  184 ? 20.784  -30.151 -37.382  1.00 44.42  ? 184  ILE   A C    1 
ATOM   2794  O  O    . ILE   A  1  184 ? 20.465  -29.042 -36.939  1.00 47.34  ? 184  ILE   A O    1 
ATOM   2795  C  CB   . ILE   A  1  184 ? 18.802  -31.658 -37.041  1.00 44.33  ? 184  ILE   A CB   1 
ATOM   2796  C  CG1  . ILE   A  1  184 ? 18.279  -32.899 -36.317  1.00 45.76  ? 184  ILE   A CG1  1 
ATOM   2797  C  CG2  . ILE   A  1  184 ? 18.619  -31.827 -38.546  1.00 47.76  ? 184  ILE   A CG2  1 
ATOM   2798  C  CD1  . ILE   A  1  184 ? 16.787  -33.117 -36.484  1.00 43.75  ? 184  ILE   A CD1  1 
ATOM   2799  H  H    . ILE   A  1  184 ? 20.252  -30.527 -34.955  1.00 53.16  ? 184  ILE   A H    1 
ATOM   2800  H  HA   . ILE   A  1  184 ? 20.795  -32.174 -37.040  1.00 52.81  ? 184  ILE   A HA   1 
ATOM   2801  H  HB   . ILE   A  1  184 ? 18.300  -30.884 -36.741  1.00 53.23  ? 184  ILE   A HB   1 
ATOM   2802  H  HG12 . ILE   A  1  184 ? 18.734  -33.681 -36.668  1.00 54.95  ? 184  ILE   A HG12 1 
ATOM   2803  H  HG13 . ILE   A  1  184 ? 18.461  -32.808 -35.369  1.00 54.95  ? 184  ILE   A HG13 1 
ATOM   2804  H  HG21 . ILE   A  1  184 ? 17.672  -31.900 -38.742  1.00 57.35  ? 184  ILE   A HG21 1 
ATOM   2805  H  HG22 . ILE   A  1  184 ? 18.991  -31.053 -38.998  1.00 57.35  ? 184  ILE   A HG22 1 
ATOM   2806  H  HG23 . ILE   A  1  184 ? 19.079  -32.631 -38.832  1.00 57.35  ? 184  ILE   A HG23 1 
ATOM   2807  H  HD11 . ILE   A  1  184 ? 16.520  -33.891 -35.963  1.00 52.54  ? 184  ILE   A HD11 1 
ATOM   2808  H  HD12 . ILE   A  1  184 ? 16.315  -32.330 -36.171  1.00 52.54  ? 184  ILE   A HD12 1 
ATOM   2809  H  HD13 . ILE   A  1  184 ? 16.592  -33.268 -37.423  1.00 52.54  ? 184  ILE   A HD13 1 
ATOM   2810  N  N    . SER   A  1  185 ? 21.557  -30.314 -38.452  1.00 44.64  ? 185  SER   A N    1 
ATOM   2811  C  CA   . SER   A  1  185 ? 22.064  -29.187 -39.221  1.00 49.69  ? 185  SER   A CA   1 
ATOM   2812  C  C    . SER   A  1  185 ? 21.701  -29.375 -40.684  1.00 51.98  ? 185  SER   A C    1 
ATOM   2813  O  O    . SER   A  1  185 ? 21.983  -30.425 -41.270  1.00 54.76  ? 185  SER   A O    1 
ATOM   2814  C  CB   . SER   A  1  185 ? 23.580  -29.042 -39.069  1.00 53.92  ? 185  SER   A CB   1 
ATOM   2815  O  OG   . SER   A  1  185 ? 24.071  -28.023 -39.922  1.00 56.65  ? 185  SER   A OG   1 
ATOM   2816  H  H    . SER   A  1  185 ? 21.803  -31.080 -38.755  1.00 53.60  ? 185  SER   A H    1 
ATOM   2817  H  HA   . SER   A  1  185 ? 21.647  -28.371 -38.904  1.00 59.66  ? 185  SER   A HA   1 
ATOM   2818  H  HB2  . SER   A  1  185 ? 23.785  -28.811 -38.149  1.00 64.74  ? 185  SER   A HB2  1 
ATOM   2819  H  HB3  . SER   A  1  185 ? 24.004  -29.882 -39.303  1.00 64.74  ? 185  SER   A HB3  1 
ATOM   2820  H  HG   . SER   A  1  185 ? 23.579  -27.344 -39.871  1.00 68.02  ? 185  SER   A HG   1 
ATOM   2821  N  N    . ASP   A  1  186 ? 21.083  -28.353 -41.269  1.00 52.38  ? 186  ASP   A N    1 
ATOM   2822  C  CA   . ASP   A  1  186 ? 20.666  -28.380 -42.660  1.00 53.59  ? 186  ASP   A CA   1 
ATOM   2823  C  C    . ASP   A  1  186 ? 21.117  -27.109 -43.361  1.00 55.87  ? 186  ASP   A C    1 
ATOM   2824  O  O    . ASP   A  1  186 ? 21.160  -26.028 -42.767  1.00 58.10  ? 186  ASP   A O    1 
ATOM   2825  C  CB   . ASP   A  1  186 ? 19.145  -28.527 -42.787  1.00 57.99  ? 186  ASP   A CB   1 
ATOM   2826  C  CG   . ASP   A  1  186 ? 18.701  -29.976 -42.809  1.00 60.76  ? 186  ASP   A CG   1 
ATOM   2827  O  OD1  . ASP   A  1  186 ? 19.238  -30.751 -43.629  1.00 65.14  ? 186  ASP   A OD1  1 
ATOM   2828  O  OD2  . ASP   A  1  186 ? 17.822  -30.344 -42.002  1.00 58.80  ? 186  ASP   A OD2  1 
ATOM   2829  H  H    . ASP   A  1  186 ? 20.890  -27.617 -40.868  1.00 62.90  ? 186  ASP   A H    1 
ATOM   2830  H  HA   . ASP   A  1  186 ? 21.085  -29.133 -43.105  1.00 64.34  ? 186  ASP   A HA   1 
ATOM   2831  H  HB2  . ASP   A  1  186 ? 18.720  -28.094 -42.031  1.00 69.62  ? 186  ASP   A HB2  1 
ATOM   2832  H  HB3  . ASP   A  1  186 ? 18.855  -28.111 -43.614  1.00 69.62  ? 186  ASP   A HB3  1 
ATOM   2833  N  N    . GLN   A  1  187 ? 21.455  -27.258 -44.636  1.00 60.28  ? 187  GLN   A N    1 
ATOM   2834  C  CA   . GLN   A  1  187 ? 21.812  -26.115 -45.460  1.00 62.06  ? 187  GLN   A CA   1 
ATOM   2835  C  C    . GLN   A  1  187 ? 20.561  -25.305 -45.767  1.00 64.05  ? 187  GLN   A C    1 
ATOM   2836  O  O    . GLN   A  1  187 ? 19.538  -25.861 -46.178  1.00 68.24  ? 187  GLN   A O    1 
ATOM   2837  C  CB   . GLN   A  1  187 ? 22.477  -26.593 -46.749  1.00 64.67  ? 187  GLN   A CB   1 
ATOM   2838  C  CG   . GLN   A  1  187 ? 23.680  -27.495 -46.504  1.00 68.46  ? 187  GLN   A CG   1 
ATOM   2839  C  CD   . GLN   A  1  187 ? 24.105  -28.268 -47.736  1.00 73.50  ? 187  GLN   A CD   1 
ATOM   2840  O  OE1  . GLN   A  1  187 ? 23.273  -28.684 -48.543  1.00 71.23  ? 187  GLN   A OE1  1 
ATOM   2841  N  NE2  . GLN   A  1  187 ? 25.409  -28.469 -47.884  1.00 80.83  ? 187  GLN   A NE2  1 
ATOM   2842  H  H    . GLN   A  1  187 ? 21.486  -28.013 -45.047  1.00 72.37  ? 187  GLN   A H    1 
ATOM   2843  H  HA   . GLN   A  1  187 ? 22.442  -25.544 -44.993  1.00 74.51  ? 187  GLN   A HA   1 
ATOM   2844  H  HB2  . GLN   A  1  187 ? 21.830  -27.093 -47.269  1.00 77.64  ? 187  GLN   A HB2  1 
ATOM   2845  H  HB3  . GLN   A  1  187 ? 22.781  -25.820 -47.250  1.00 77.64  ? 187  GLN   A HB3  1 
ATOM   2846  H  HG2  . GLN   A  1  187 ? 24.430  -26.950 -46.221  1.00 82.19  ? 187  GLN   A HG2  1 
ATOM   2847  H  HG3  . GLN   A  1  187 ? 23.456  -28.137 -45.812  1.00 82.19  ? 187  GLN   A HG3  1 
ATOM   2848  H  HE21 . GLN   A  1  187 ? 25.960  -28.167 -47.297  1.00 97.04  ? 187  GLN   A HE21 1 
ATOM   2849  H  HE22 . GLN   A  1  187 ? 25.702  -28.902 -48.566  1.00 97.04  ? 187  GLN   A HE22 1 
ATOM   2850  N  N    . VAL   A  1  188 ? 20.631  -23.988 -45.551  1.00 62.76  ? 188  VAL   A N    1 
ATOM   2851  C  CA   . VAL   A  1  188 ? 19.474  -23.147 -45.839  1.00 64.30  ? 188  VAL   A CA   1 
ATOM   2852  C  C    . VAL   A  1  188 ? 19.030  -23.342 -47.281  1.00 64.89  ? 188  VAL   A C    1 
ATOM   2853  O  O    . VAL   A  1  188 ? 17.836  -23.260 -47.590  1.00 67.22  ? 188  VAL   A O    1 
ATOM   2854  C  CB   . VAL   A  1  188 ? 19.781  -21.665 -45.545  1.00 65.53  ? 188  VAL   A CB   1 
ATOM   2855  C  CG1  . VAL   A  1  188 ? 20.184  -21.477 -44.088  1.00 63.25  ? 188  VAL   A CG1  1 
ATOM   2856  C  CG2  . VAL   A  1  188 ? 20.861  -21.140 -46.481  1.00 71.65  ? 188  VAL   A CG2  1 
ATOM   2857  H  H    . VAL   A  1  188 ? 21.319  -23.571 -45.246  1.00 75.35  ? 188  VAL   A H    1 
ATOM   2858  H  HA   . VAL   A  1  188 ? 18.750  -23.415 -45.252  1.00 77.20  ? 188  VAL   A HA   1 
ATOM   2859  H  HB   . VAL   A  1  188 ? 18.977  -21.144 -45.701  1.00 78.67  ? 188  VAL   A HB   1 
ATOM   2860  H  HG11 . VAL   A  1  188 ? 20.348  -20.535 -43.925  1.00 75.94  ? 188  VAL   A HG11 1 
ATOM   2861  H  HG12 . VAL   A  1  188 ? 19.464  -21.791 -43.519  1.00 75.94  ? 188  VAL   A HG12 1 
ATOM   2862  H  HG13 . VAL   A  1  188 ? 20.990  -21.989 -43.915  1.00 75.94  ? 188  VAL   A HG13 1 
ATOM   2863  H  HG21 . VAL   A  1  188 ? 21.045  -20.213 -46.263  1.00 86.02  ? 188  VAL   A HG21 1 
ATOM   2864  H  HG22 . VAL   A  1  188 ? 21.663  -21.673 -46.368  1.00 86.02  ? 188  VAL   A HG22 1 
ATOM   2865  H  HG23 . VAL   A  1  188 ? 20.546  -21.208 -47.396  1.00 86.02  ? 188  VAL   A HG23 1 
ATOM   2866  N  N    . ALA   A  1  189 ? 19.976  -23.612 -48.183  1.00 64.19  ? 189  ALA   A N    1 
ATOM   2867  C  CA   . ALA   A  1  189 ? 19.620  -23.844 -49.578  1.00 64.11  ? 189  ALA   A CA   1 
ATOM   2868  C  C    . ALA   A  1  189 ? 18.714  -25.060 -49.715  1.00 64.70  ? 189  ALA   A C    1 
ATOM   2869  O  O    . ALA   A  1  189 ? 17.735  -25.033 -50.470  1.00 68.18  ? 189  ALA   A O    1 
ATOM   2870  C  CB   . ALA   A  1  189 ? 20.884  -24.016 -50.419  1.00 62.30  ? 189  ALA   A CB   1 
ATOM   2871  H  H    . ALA   A  1  189 ? 20.818  -23.665 -48.014  1.00 77.06  ? 189  ALA   A H    1 
ATOM   2872  H  HA   . ALA   A  1  189 ? 19.140  -23.071 -49.915  1.00 76.97  ? 189  ALA   A HA   1 
ATOM   2873  H  HB1  . ALA   A  1  189 ? 20.631  -24.144 -51.347  1.00 74.79  ? 189  ALA   A HB1  1 
ATOM   2874  H  HB2  . ALA   A  1  189 ? 21.432  -23.220 -50.333  1.00 74.79  ? 189  ALA   A HB2  1 
ATOM   2875  H  HB3  . ALA   A  1  189 ? 21.373  -24.790 -50.100  1.00 74.79  ? 189  ALA   A HB3  1 
ATOM   2876  N  N    . GLU   A  1  190 ? 19.024  -26.139 -48.992  1.00 63.32  ? 190  GLU   A N    1 
ATOM   2877  C  CA   . GLU   A  1  190 ? 18.145  -27.303 -48.996  1.00 63.99  ? 190  GLU   A CA   1 
ATOM   2878  C  C    . GLU   A  1  190 ? 16.794  -26.969 -48.380  1.00 62.49  ? 190  GLU   A C    1 
ATOM   2879  O  O    . GLU   A  1  190 ? 15.746  -27.358 -48.909  1.00 62.22  ? 190  GLU   A O    1 
ATOM   2880  C  CB   . GLU   A  1  190 ? 18.796  -28.457 -48.235  1.00 62.69  ? 190  GLU   A CB   1 
ATOM   2881  C  CG   . GLU   A  1  190 ? 19.859  -29.202 -49.013  1.00 65.49  ? 190  GLU   A CG   1 
ATOM   2882  C  CD   . GLU   A  1  190 ? 19.284  -29.977 -50.175  1.00 70.81  ? 190  GLU   A CD   1 
ATOM   2883  O  OE1  . GLU   A  1  190 ? 19.356  -29.473 -51.315  1.00 76.28  ? 190  GLU   A OE1  1 
ATOM   2884  O  OE2  . GLU   A  1  190 ? 18.750  -31.083 -49.946  1.00 70.97  ? 190  GLU   A OE2  1 
ATOM   2885  H  H    . GLU   A  1  190 ? 19.726  -26.219 -48.501  1.00 76.02  ? 190  GLU   A H    1 
ATOM   2886  H  HA   . GLU   A  1  190 ? 18.005  -27.583 -49.914  1.00 76.82  ? 190  GLU   A HA   1 
ATOM   2887  H  HB2  . GLU   A  1  190 ? 19.213  -28.103 -47.434  1.00 75.26  ? 190  GLU   A HB2  1 
ATOM   2888  H  HB3  . GLU   A  1  190 ? 18.107  -29.096 -47.995  1.00 75.26  ? 190  GLU   A HB3  1 
ATOM   2889  H  HG2  . GLU   A  1  190 ? 20.501  -28.565 -49.363  1.00 78.62  ? 190  GLU   A HG2  1 
ATOM   2890  H  HG3  . GLU   A  1  190 ? 20.303  -29.830 -48.422  1.00 78.62  ? 190  GLU   A HG3  1 
ATOM   2891  N  N    . ILE   A  1  191 ? 16.801  -26.243 -47.260  1.00 61.44  ? 191  ILE   A N    1 
ATOM   2892  C  CA   . ILE   A  1  191 ? 15.566  -25.991 -46.524  1.00 58.80  ? 191  ILE   A CA   1 
ATOM   2893  C  C    . ILE   A  1  191 ? 14.534  -25.314 -47.418  1.00 58.59  ? 191  ILE   A C    1 
ATOM   2894  O  O    . ILE   A  1  191 ? 13.342  -25.642 -47.370  1.00 59.33  ? 191  ILE   A O    1 
ATOM   2895  C  CB   . ILE   A  1  191 ? 15.863  -25.157 -45.263  1.00 54.87  ? 191  ILE   A CB   1 
ATOM   2896  C  CG1  . ILE   A  1  191 ? 16.751  -25.960 -44.307  1.00 54.11  ? 191  ILE   A CG1  1 
ATOM   2897  C  CG2  . ILE   A  1  191 ? 14.566  -24.745 -44.578  1.00 54.04  ? 191  ILE   A CG2  1 
ATOM   2898  C  CD1  . ILE   A  1  191 ? 17.267  -25.170 -43.121  1.00 54.80  ? 191  ILE   A CD1  1 
ATOM   2899  H  H    . ILE   A  1  191 ? 17.501  -25.889 -46.910  1.00 73.77  ? 191  ILE   A H    1 
ATOM   2900  H  HA   . ILE   A  1  191 ? 15.195  -26.842 -46.243  1.00 70.60  ? 191  ILE   A HA   1 
ATOM   2901  H  HB   . ILE   A  1  191 ? 16.336  -24.352 -45.525  1.00 65.88  ? 191  ILE   A HB   1 
ATOM   2902  H  HG12 . ILE   A  1  191 ? 16.237  -26.706 -43.961  1.00 64.97  ? 191  ILE   A HG12 1 
ATOM   2903  H  HG13 . ILE   A  1  191 ? 17.520  -26.287 -44.799  1.00 64.97  ? 191  ILE   A HG13 1 
ATOM   2904  H  HG21 . ILE   A  1  191 ? 14.778  -24.277 -43.756  1.00 64.89  ? 191  ILE   A HG21 1 
ATOM   2905  H  HG22 . ILE   A  1  191 ? 14.067  -24.162 -45.172  1.00 64.89  ? 191  ILE   A HG22 1 
ATOM   2906  H  HG23 . ILE   A  1  191 ? 14.046  -25.540 -44.382  1.00 64.89  ? 191  ILE   A HG23 1 
ATOM   2907  H  HD11 . ILE   A  1  191 ? 17.843  -25.741 -42.588  1.00 65.80  ? 191  ILE   A HD11 1 
ATOM   2908  H  HD12 . ILE   A  1  191 ? 17.768  -24.406 -43.444  1.00 65.80  ? 191  ILE   A HD12 1 
ATOM   2909  H  HD13 . ILE   A  1  191 ? 16.514  -24.871 -42.588  1.00 65.80  ? 191  ILE   A HD13 1 
ATOM   2910  N  N    . VAL   A  1  192 ? 14.968  -24.368 -48.245  1.00 57.87  ? 192  VAL   A N    1 
ATOM   2911  C  CA   . VAL   A  1  192 ? 14.033  -23.623 -49.082  1.00 63.72  ? 192  VAL   A CA   1 
ATOM   2912  C  C    . VAL   A  1  192 ? 13.768  -24.345 -50.398  1.00 63.43  ? 192  VAL   A C    1 
ATOM   2913  O  O    . VAL   A  1  192 ? 12.632  -24.372 -50.878  1.00 61.24  ? 192  VAL   A O    1 
ATOM   2914  C  CB   . VAL   A  1  192 ? 14.558  -22.190 -49.324  1.00 70.62  ? 192  VAL   A CB   1 
ATOM   2915  C  CG1  . VAL   A  1  192 ? 15.046  -21.567 -48.021  1.00 71.16  ? 192  VAL   A CG1  1 
ATOM   2916  C  CG2  . VAL   A  1  192 ? 15.662  -22.177 -50.380  1.00 74.41  ? 192  VAL   A CG2  1 
ATOM   2917  H  H    . VAL   A  1  192 ? 15.792  -24.141 -48.340  1.00 69.48  ? 192  VAL   A H    1 
ATOM   2918  H  HA   . VAL   A  1  192 ? 13.190  -23.553 -48.607  1.00 76.50  ? 192  VAL   A HA   1 
ATOM   2919  H  HB   . VAL   A  1  192 ? 13.826  -21.650 -49.661  1.00 84.78  ? 192  VAL   A HB   1 
ATOM   2920  H  HG11 . VAL   A  1  192 ? 15.342  -20.660 -48.196  1.00 85.43  ? 192  VAL   A HG11 1 
ATOM   2921  H  HG12 . VAL   A  1  192 ? 14.316  -21.559 -47.382  1.00 85.43  ? 192  VAL   A HG12 1 
ATOM   2922  H  HG13 . VAL   A  1  192 ? 15.783  -22.095 -47.675  1.00 85.43  ? 192  VAL   A HG13 1 
ATOM   2923  H  HG21 . VAL   A  1  192 ? 16.012  -21.276 -50.460  1.00 89.33  ? 192  VAL   A HG21 1 
ATOM   2924  H  HG22 . VAL   A  1  192 ? 16.368  -22.783 -50.106  1.00 89.33  ? 192  VAL   A HG22 1 
ATOM   2925  H  HG23 . VAL   A  1  192 ? 15.290  -22.464 -51.229  1.00 89.33  ? 192  VAL   A HG23 1 
ATOM   2926  N  N    . SER   A  1  193 ? 14.801  -24.944 -50.996  1.00 63.41  ? 193  SER   A N    1 
ATOM   2927  C  CA   . SER   A  1  193 ? 14.638  -25.541 -52.317  1.00 65.95  ? 193  SER   A CA   1 
ATOM   2928  C  C    . SER   A  1  193 ? 13.765  -26.786 -52.255  1.00 65.97  ? 193  SER   A C    1 
ATOM   2929  O  O    . SER   A  1  193 ? 12.927  -27.008 -53.136  1.00 69.32  ? 193  SER   A O    1 
ATOM   2930  C  CB   . SER   A  1  193 ? 16.004  -25.881 -52.911  1.00 70.08  ? 193  SER   A CB   1 
ATOM   2931  O  OG   . SER   A  1  193 ? 16.474  -27.127 -52.425  1.00 74.07  ? 193  SER   A OG   1 
ATOM   2932  H  H    . SER   A  1  193 ? 15.590  -25.015 -50.663  1.00 76.13  ? 193  SER   A H    1 
ATOM   2933  H  HA   . SER   A  1  193 ? 14.207  -24.895 -52.898  1.00 79.17  ? 193  SER   A HA   1 
ATOM   2934  H  HB2  . SER   A  1  193 ? 15.925  -25.930 -53.877  1.00 84.13  ? 193  SER   A HB2  1 
ATOM   2935  H  HB3  . SER   A  1  193 ? 16.637  -25.188 -52.665  1.00 84.13  ? 193  SER   A HB3  1 
ATOM   2936  H  HG   . SER   A  1  193 ? 17.218  -27.307 -52.769  1.00 88.92  ? 193  SER   A HG   1 
ATOM   2937  N  N    . LYS   A  1  194 ? 13.946  -27.609 -51.225  1.00 67.62  ? 194  LYS   A N    1 
ATOM   2938  C  CA   . LYS   A  1  194 ? 13.179  -28.838 -51.093  1.00 71.66  ? 194  LYS   A CA   1 
ATOM   2939  C  C    . LYS   A  1  194 ? 11.804  -28.615 -50.479  1.00 68.40  ? 194  LYS   A C    1 
ATOM   2940  O  O    . LYS   A  1  194 ? 11.023  -29.569 -50.398  1.00 68.31  ? 194  LYS   A O    1 
ATOM   2941  C  CB   . LYS   A  1  194 ? 13.946  -29.852 -50.240  1.00 76.36  ? 194  LYS   A CB   1 
ATOM   2942  C  CG   . LYS   A  1  194 ? 15.387  -30.090 -50.671  1.00 82.44  ? 194  LYS   A CG   1 
ATOM   2943  C  CD   . LYS   A  1  194 ? 15.489  -30.911 -51.950  1.00 87.58  ? 194  LYS   A CD   1 
ATOM   2944  C  CE   . LYS   A  1  194 ? 16.935  -31.305 -52.210  1.00 91.22  ? 194  LYS   A CE   1 
ATOM   2945  N  NZ   . LYS   A  1  194 ? 17.172  -31.898 -53.552  1.00 100.88 ? 194  LYS   A NZ   1 
ATOM   2946  H  H    . LYS   A  1  194 ? 14.509  -27.476 -50.589  1.00 81.19  ? 194  LYS   A H    1 
ATOM   2947  H  HA   . LYS   A  1  194 ? 13.058  -29.217 -51.978  1.00 86.03  ? 194  LYS   A HA   1 
ATOM   2948  H  HB2  . LYS   A  1  194 ? 13.965  -29.533 -49.324  1.00 91.67  ? 194  LYS   A HB2  1 
ATOM   2949  H  HB3  . LYS   A  1  194 ? 13.485  -30.704 -50.285  1.00 91.67  ? 194  LYS   A HB3  1 
ATOM   2950  H  HG2  . LYS   A  1  194 ? 15.816  -29.234 -50.830  1.00 98.97  ? 194  LYS   A HG2  1 
ATOM   2951  H  HG3  . LYS   A  1  194 ? 15.854  -30.569 -49.969  1.00 98.97  ? 194  LYS   A HG3  1 
ATOM   2952  H  HD2  . LYS   A  1  194 ? 14.959  -31.718 -51.861  1.00 105.13 ? 194  LYS   A HD2  1 
ATOM   2953  H  HD3  . LYS   A  1  194 ? 15.171  -30.386 -52.700  1.00 105.13 ? 194  LYS   A HD3  1 
ATOM   2954  H  HE2  . LYS   A  1  194 ? 17.490  -30.513 -52.136  1.00 109.50 ? 194  LYS   A HE2  1 
ATOM   2955  H  HE3  . LYS   A  1  194 ? 17.202  -31.961 -51.548  1.00 109.50 ? 194  LYS   A HE3  1 
ATOM   2956  H  HZ1  . LYS   A  1  194 ? 18.032  -32.109 -53.644  1.00 121.09 ? 194  LYS   A HZ1  1 
ATOM   2957  H  HZ2  . LYS   A  1  194 ? 16.681  -32.634 -53.651  1.00 121.09 ? 194  LYS   A HZ2  1 
ATOM   2958  H  HZ3  . LYS   A  1  194 ? 16.949  -31.315 -54.186  1.00 121.09 ? 194  LYS   A HZ3  1 
ATOM   2959  N  N    . TYR   A  1  195 ? 11.487  -27.396 -50.046  1.00 65.81  ? 195  TYR   A N    1 
ATOM   2960  C  CA   . TYR   A  1  195 ? 10.202  -27.164 -49.404  1.00 63.46  ? 195  TYR   A CA   1 
ATOM   2961  C  C    . TYR   A  1  195 ? 9.060   -27.476 -50.363  1.00 67.14  ? 195  TYR   A C    1 
ATOM   2962  O  O    . TYR   A  1  195 ? 9.067   -27.059 -51.526  1.00 69.68  ? 195  TYR   A O    1 
ATOM   2963  C  CB   . TYR   A  1  195 ? 10.086  -25.724 -48.905  1.00 60.06  ? 195  TYR   A CB   1 
ATOM   2964  C  CG   . TYR   A  1  195 ? 8.753   -25.465 -48.241  1.00 57.92  ? 195  TYR   A CG   1 
ATOM   2965  C  CD1  . TYR   A  1  195 ? 8.387   -26.158 -47.094  1.00 56.97  ? 195  TYR   A CD1  1 
ATOM   2966  C  CD2  . TYR   A  1  195 ? 7.852   -24.549 -48.767  1.00 59.65  ? 195  TYR   A CD2  1 
ATOM   2967  C  CE1  . TYR   A  1  195 ? 7.168   -25.941 -46.485  1.00 58.15  ? 195  TYR   A CE1  1 
ATOM   2968  C  CE2  . TYR   A  1  195 ? 6.628   -24.324 -48.162  1.00 61.55  ? 195  TYR   A CE2  1 
ATOM   2969  C  CZ   . TYR   A  1  195 ? 6.292   -25.024 -47.022  1.00 59.95  ? 195  TYR   A CZ   1 
ATOM   2970  O  OH   . TYR   A  1  195 ? 5.077   -24.807 -46.413  1.00 58.20  ? 195  TYR   A OH   1 
ATOM   2971  H  H    . TYR   A  1  195 ? 11.991  -26.702 -50.111  1.00 79.00  ? 195  TYR   A H    1 
ATOM   2972  H  HA   . TYR   A  1  195 ? 10.134  -27.750 -48.634  1.00 76.19  ? 195  TYR   A HA   1 
ATOM   2973  H  HB2  . TYR   A  1  195 ? 10.787  -25.552 -48.258  1.00 72.11  ? 195  TYR   A HB2  1 
ATOM   2974  H  HB3  . TYR   A  1  195 ? 10.174  -25.117 -49.657  1.00 72.11  ? 195  TYR   A HB3  1 
ATOM   2975  H  HD1  . TYR   A  1  195 ? 8.975   -26.779 -46.729  1.00 68.40  ? 195  TYR   A HD1  1 
ATOM   2976  H  HD2  . TYR   A  1  195 ? 8.075   -24.080 -49.538  1.00 71.62  ? 195  TYR   A HD2  1 
ATOM   2977  H  HE1  . TYR   A  1  195 ? 6.939   -26.412 -45.716  1.00 69.82  ? 195  TYR   A HE1  1 
ATOM   2978  H  HE2  . TYR   A  1  195 ? 6.035   -23.705 -48.523  1.00 73.90  ? 195  TYR   A HE2  1 
ATOM   2979  H  HH   . TYR   A  1  195 ? 4.654   -24.207 -46.821  1.00 69.87  ? 195  TYR   A HH   1 
ATOM   2980  N  N    . ASP   A  1  196 ? 8.080   -28.220 -49.860  1.00 63.48  ? 196  ASP   A N    1 
ATOM   2981  C  CA   . ASP   A  1  196 ? 6.868   -28.597 -50.574  1.00 63.96  ? 196  ASP   A CA   1 
ATOM   2982  C  C    . ASP   A  1  196 ? 5.760   -28.722 -49.534  1.00 59.44  ? 196  ASP   A C    1 
ATOM   2983  O  O    . ASP   A  1  196 ? 5.803   -29.636 -48.701  1.00 57.04  ? 196  ASP   A O    1 
ATOM   2984  C  CB   . ASP   A  1  196 ? 7.065   -29.910 -51.334  1.00 66.21  ? 196  ASP   A CB   1 
ATOM   2985  C  CG   . ASP   A  1  196 ? 5.857   -30.293 -52.175  1.00 69.26  ? 196  ASP   A CG   1 
ATOM   2986  O  OD1  . ASP   A  1  196 ? 4.739   -29.824 -51.876  1.00 70.88  ? 196  ASP   A OD1  1 
ATOM   2987  O  OD2  . ASP   A  1  196 ? 6.027   -31.074 -53.135  1.00 69.48  ? 196  ASP   A OD2  1 
ATOM   2988  H  H    . ASP   A  1  196 ? 8.095   -28.537 -49.061  1.00 76.21  ? 196  ASP   A H    1 
ATOM   2989  H  HA   . ASP   A  1  196 ? 6.626   -27.930 -51.236  1.00 76.79  ? 196  ASP   A HA   1 
ATOM   2990  H  HB2  . ASP   A  1  196 ? 7.827   -29.820 -51.928  1.00 79.49  ? 196  ASP   A HB2  1 
ATOM   2991  H  HB3  . ASP   A  1  196 ? 7.225   -30.623 -50.697  1.00 79.49  ? 196  ASP   A HB3  1 
ATOM   2992  N  N    . PRO   A  1  197 ? 4.760   -27.833 -49.529  1.00 61.44  ? 197  PRO   A N    1 
ATOM   2993  C  CA   . PRO   A  1  197 ? 3.746   -27.885 -48.464  1.00 60.35  ? 197  PRO   A CA   1 
ATOM   2994  C  C    . PRO   A  1  197 ? 2.867   -29.122 -48.511  1.00 60.67  ? 197  PRO   A C    1 
ATOM   2995  O  O    . PRO   A  1  197 ? 2.147   -29.381 -47.537  1.00 60.83  ? 197  PRO   A O    1 
ATOM   2996  C  CB   . PRO   A  1  197 ? 2.925   -26.610 -48.698  1.00 61.39  ? 197  PRO   A CB   1 
ATOM   2997  C  CG   . PRO   A  1  197 ? 3.085   -26.324 -50.147  1.00 63.34  ? 197  PRO   A CG   1 
ATOM   2998  C  CD   . PRO   A  1  197 ? 4.480   -26.761 -50.502  1.00 62.97  ? 197  PRO   A CD   1 
ATOM   2999  H  HA   . PRO   A  1  197 ? 4.173   -27.832 -47.595  1.00 72.46  ? 197  PRO   A HA   1 
ATOM   3000  H  HB2  . PRO   A  1  197 ? 1.995   -26.769 -48.475  1.00 73.70  ? 197  PRO   A HB2  1 
ATOM   3001  H  HB3  . PRO   A  1  197 ? 3.277   -25.885 -48.158  1.00 73.70  ? 197  PRO   A HB3  1 
ATOM   3002  H  HG2  . PRO   A  1  197 ? 2.429   -26.826 -50.654  1.00 76.04  ? 197  PRO   A HG2  1 
ATOM   3003  H  HG3  . PRO   A  1  197 ? 2.972   -25.374 -50.306  1.00 76.04  ? 197  PRO   A HG3  1 
ATOM   3004  H  HD2  . PRO   A  1  197 ? 4.513   -27.101 -51.410  1.00 75.60  ? 197  PRO   A HD2  1 
ATOM   3005  H  HD3  . PRO   A  1  197 ? 5.107   -26.029 -50.399  1.00 75.60  ? 197  PRO   A HD3  1 
ATOM   3006  N  N    . ASN   A  1  198 ? 2.896   -29.888 -49.601  1.00 62.35  ? 198  ASN   A N    1 
ATOM   3007  C  CA   . ASN   A  1  198 ? 2.143   -31.133 -49.680  1.00 59.15  ? 198  ASN   A CA   1 
ATOM   3008  C  C    . ASN   A  1  198 ? 2.867   -32.299 -49.022  1.00 57.91  ? 198  ASN   A C    1 
ATOM   3009  O  O    . ASN   A  1  198 ? 2.262   -33.363 -48.849  1.00 55.11  ? 198  ASN   A O    1 
ATOM   3010  C  CB   . ASN   A  1  198 ? 1.851   -31.471 -51.142  1.00 58.20  ? 198  ASN   A CB   1 
ATOM   3011  C  CG   . ASN   A  1  198 ? 0.900   -30.485 -51.787  1.00 59.63  ? 198  ASN   A CG   1 
ATOM   3012  O  OD1  . ASN   A  1  198 ? -0.176  -30.207 -51.257  1.00 60.59  ? 198  ASN   A OD1  1 
ATOM   3013  N  ND2  . ASN   A  1  198 ? 1.297   -29.939 -52.929  1.00 61.33  ? 198  ASN   A ND2  1 
ATOM   3014  H  H    . ASN   A  1  198 ? 3.347   -29.706 -50.310  1.00 74.86  ? 198  ASN   A H    1 
ATOM   3015  H  HA   . ASN   A  1  198 ? 1.295   -31.016 -49.225  1.00 71.02  ? 198  ASN   A HA   1 
ATOM   3016  H  HB2  . ASN   A  1  198 ? 2.682   -31.459 -51.643  1.00 69.88  ? 198  ASN   A HB2  1 
ATOM   3017  H  HB3  . ASN   A  1  198 ? 1.448   -32.353 -51.190  1.00 69.88  ? 198  ASN   A HB3  1 
ATOM   3018  H  HD21 . ASN   A  1  198 ? 0.792   -29.372 -53.334  1.00 73.63  ? 198  ASN   A HD21 1 
ATOM   3019  H  HD22 . ASN   A  1  198 ? 2.060   -30.151 -53.265  1.00 73.63  ? 198  ASN   A HD22 1 
ATOM   3020  N  N    . VAL   A  1  199 ? 4.133   -32.125 -48.654  1.00 56.51  ? 199  VAL   A N    1 
ATOM   3021  C  CA   . VAL   A  1  199 ? 4.932   -33.165 -48.018  1.00 54.47  ? 199  VAL   A CA   1 
ATOM   3022  C  C    . VAL   A  1  199 ? 5.282   -32.681 -46.620  1.00 54.66  ? 199  VAL   A C    1 
ATOM   3023  O  O    . VAL   A  1  199 ? 5.914   -31.629 -46.459  1.00 57.64  ? 199  VAL   A O    1 
ATOM   3024  C  CB   . VAL   A  1  199 ? 6.197   -33.486 -48.827  1.00 50.71  ? 199  VAL   A CB   1 
ATOM   3025  C  CG1  . VAL   A  1  199 ? 6.984   -34.609 -48.167  1.00 48.39  ? 199  VAL   A CG1  1 
ATOM   3026  C  CG2  . VAL   A  1  199 ? 5.825   -33.852 -50.257  1.00 46.89  ? 199  VAL   A CG2  1 
ATOM   3027  H  H    . VAL   A  1  199 ? 4.563   -31.389 -48.767  1.00 67.85  ? 199  VAL   A H    1 
ATOM   3028  H  HA   . VAL   A  1  199 ? 4.409   -33.978 -47.940  1.00 65.40  ? 199  VAL   A HA   1 
ATOM   3029  H  HB   . VAL   A  1  199 ? 6.766   -32.701 -48.853  1.00 60.89  ? 199  VAL   A HB   1 
ATOM   3030  H  HG11 . VAL   A  1  199 ? 7.767   -34.805 -48.706  1.00 58.11  ? 199  VAL   A HG11 1 
ATOM   3031  H  HG12 . VAL   A  1  199 ? 7.255   -34.326 -47.280  1.00 58.11  ? 199  VAL   A HG12 1 
ATOM   3032  H  HG13 . VAL   A  1  199 ? 6.419   -35.396 -48.106  1.00 58.11  ? 199  VAL   A HG13 1 
ATOM   3033  H  HG21 . VAL   A  1  199 ? 6.634   -34.065 -50.749  1.00 56.31  ? 199  VAL   A HG21 1 
ATOM   3034  H  HG22 . VAL   A  1  199 ? 5.235   -34.621 -50.243  1.00 56.31  ? 199  VAL   A HG22 1 
ATOM   3035  H  HG23 . VAL   A  1  199 ? 5.376   -33.098 -50.670  1.00 56.31  ? 199  VAL   A HG23 1 
ATOM   3036  N  N    . TYR   A  1  200 ? 4.874   -33.449 -45.612  1.00 53.95  ? 200  TYR   A N    1 
ATOM   3037  C  CA   . TYR   A  1  200 ? 5.053   -33.050 -44.222  1.00 51.66  ? 200  TYR   A CA   1 
ATOM   3038  C  C    . TYR   A  1  200 ? 6.411   -33.449 -43.661  1.00 47.64  ? 200  TYR   A C    1 
ATOM   3039  O  O    . TYR   A  1  200 ? 6.890   -32.809 -42.718  1.00 47.74  ? 200  TYR   A O    1 
ATOM   3040  C  CB   . TYR   A  1  200 ? 3.942   -33.660 -43.361  1.00 48.41  ? 200  TYR   A CB   1 
ATOM   3041  C  CG   . TYR   A  1  200 ? 2.545   -33.441 -43.911  1.00 51.14  ? 200  TYR   A CG   1 
ATOM   3042  C  CD1  . TYR   A  1  200 ? 2.193   -32.244 -44.524  1.00 50.68  ? 200  TYR   A CD1  1 
ATOM   3043  C  CD2  . TYR   A  1  200 ? 1.580   -34.437 -43.824  1.00 51.19  ? 200  TYR   A CD2  1 
ATOM   3044  C  CE1  . TYR   A  1  200 ? 0.917   -32.045 -45.028  1.00 48.95  ? 200  TYR   A CE1  1 
ATOM   3045  C  CE2  . TYR   A  1  200 ? 0.304   -34.246 -44.325  1.00 49.19  ? 200  TYR   A CE2  1 
ATOM   3046  C  CZ   . TYR   A  1  200 ? -0.021  -33.050 -44.926  1.00 49.16  ? 200  TYR   A CZ   1 
ATOM   3047  O  OH   . TYR   A  1  200 ? -1.290  -32.857 -45.426  1.00 51.04  ? 200  TYR   A OH   1 
ATOM   3048  H  H    . TYR   A  1  200 ? 4.487   -34.211 -45.709  1.00 64.78  ? 200  TYR   A H    1 
ATOM   3049  H  HA   . TYR   A  1  200 ? 4.986   -32.084 -44.161  1.00 62.03  ? 200  TYR   A HA   1 
ATOM   3050  H  HB2  . TYR   A  1  200 ? 4.087   -34.617 -43.298  1.00 58.13  ? 200  TYR   A HB2  1 
ATOM   3051  H  HB3  . TYR   A  1  200 ? 3.978   -33.260 -42.479  1.00 58.13  ? 200  TYR   A HB3  1 
ATOM   3052  H  HD1  . TYR   A  1  200 ? 2.824   -31.565 -44.597  1.00 60.86  ? 200  TYR   A HD1  1 
ATOM   3053  H  HD2  . TYR   A  1  200 ? 1.795   -35.247 -43.420  1.00 61.46  ? 200  TYR   A HD2  1 
ATOM   3054  H  HE1  . TYR   A  1  200 ? 0.695   -31.237 -45.433  1.00 58.78  ? 200  TYR   A HE1  1 
ATOM   3055  H  HE2  . TYR   A  1  200 ? -0.330  -34.923 -44.257  1.00 59.06  ? 200  TYR   A HE2  1 
ATOM   3056  H  HH   . TYR   A  1  200 ? -1.758  -33.541 -45.292  1.00 61.29  ? 200  TYR   A HH   1 
ATOM   3057  N  N    . SER   A  1  201 ? 7.042   -34.483 -44.216  1.00 47.16  ? 201  SER   A N    1 
ATOM   3058  C  CA   . SER   A  1  201 ? 8.370   -34.936 -43.799  1.00 48.00  ? 201  SER   A CA   1 
ATOM   3059  C  C    . SER   A  1  201 ? 9.288   -34.823 -45.012  1.00 49.93  ? 201  SER   A C    1 
ATOM   3060  O  O    . SER   A  1  201 ? 9.304   -35.709 -45.873  1.00 52.08  ? 201  SER   A O    1 
ATOM   3061  C  CB   . SER   A  1  201 ? 8.321   -36.364 -43.264  1.00 52.42  ? 201  SER   A CB   1 
ATOM   3062  O  OG   . SER   A  1  201 ? 7.342   -36.492 -42.248  1.00 53.70  ? 201  SER   A OG   1 
ATOM   3063  H  H    . SER   A  1  201 ? 6.711   -34.953 -44.856  1.00 56.63  ? 201  SER   A H    1 
ATOM   3064  H  HA   . SER   A  1  201 ? 8.707   -34.362 -43.094  1.00 57.63  ? 201  SER   A HA   1 
ATOM   3065  H  HB2  . SER   A  1  201 ? 8.100   -36.966 -43.992  1.00 62.94  ? 201  SER   A HB2  1 
ATOM   3066  H  HB3  . SER   A  1  201 ? 9.189   -36.592 -42.897  1.00 62.94  ? 201  SER   A HB3  1 
ATOM   3067  H  HG   . SER   A  1  201 ? 7.507   -35.958 -41.621  1.00 64.48  ? 201  SER   A HG   1 
ATOM   3068  N  N    . ILE   A  1  202 ? 10.052  -33.740 -45.077  1.00 52.05  ? 202  ILE   A N    1 
ATOM   3069  C  CA   . ILE   A  1  202 ? 10.850  -33.414 -46.252  1.00 52.63  ? 202  ILE   A CA   1 
ATOM   3070  C  C    . ILE   A  1  202 ? 12.194  -34.122 -46.174  1.00 53.51  ? 202  ILE   A C    1 
ATOM   3071  O  O    . ILE   A  1  202 ? 12.853  -34.131 -45.128  1.00 54.43  ? 202  ILE   A O    1 
ATOM   3072  C  CB   . ILE   A  1  202 ? 11.029  -31.888 -46.376  1.00 51.58  ? 202  ILE   A CB   1 
ATOM   3073  C  CG1  . ILE   A  1  202 ? 9.688   -31.236 -46.721  1.00 57.37  ? 202  ILE   A CG1  1 
ATOM   3074  C  CG2  . ILE   A  1  202 ? 12.081  -31.551 -47.430  1.00 50.41  ? 202  ILE   A CG2  1 
ATOM   3075  C  CD1  . ILE   A  1  202 ? 9.666   -29.739 -46.533  1.00 63.75  ? 202  ILE   A CD1  1 
ATOM   3076  H  H    . ILE   A  1  202 ? 10.127  -33.168 -44.440  1.00 62.50  ? 202  ILE   A H    1 
ATOM   3077  H  HA   . ILE   A  1  202 ? 10.391  -33.738 -47.043  1.00 63.19  ? 202  ILE   A HA   1 
ATOM   3078  H  HB   . ILE   A  1  202 ? 11.337  -31.541 -45.524  1.00 61.93  ? 202  ILE   A HB   1 
ATOM   3079  H  HG12 . ILE   A  1  202 ? 9.484   -31.420 -47.651  1.00 68.88  ? 202  ILE   A HG12 1 
ATOM   3080  H  HG13 . ILE   A  1  202 ? 9.002   -31.616 -46.149  1.00 68.88  ? 202  ILE   A HG13 1 
ATOM   3081  H  HG21 . ILE   A  1  202 ? 12.105  -30.589 -47.556  1.00 60.53  ? 202  ILE   A HG21 1 
ATOM   3082  H  HG22 . ILE   A  1  202 ? 12.946  -31.866 -47.124  1.00 60.53  ? 202  ILE   A HG22 1 
ATOM   3083  H  HG23 . ILE   A  1  202 ? 11.845  -31.988 -48.263  1.00 60.53  ? 202  ILE   A HG23 1 
ATOM   3084  H  HD11 . ILE   A  1  202 ? 8.781   -29.407 -46.746  1.00 76.54  ? 202  ILE   A HD11 1 
ATOM   3085  H  HD12 . ILE   A  1  202 ? 9.883   -29.534 -45.610  1.00 76.54  ? 202  ILE   A HD12 1 
ATOM   3086  H  HD13 . ILE   A  1  202 ? 10.322  -29.337 -47.124  1.00 76.54  ? 202  ILE   A HD13 1 
ATOM   3087  N  N    . LYS   A  1  203 ? 12.603  -34.713 -47.295  1.00 56.77  ? 203  LYS   A N    1 
ATOM   3088  C  CA   . LYS   A  1  203 ? 13.906  -35.362 -47.416  1.00 55.91  ? 203  LYS   A CA   1 
ATOM   3089  C  C    . LYS   A  1  203 ? 14.926  -34.301 -47.812  1.00 54.51  ? 203  LYS   A C    1 
ATOM   3090  O  O    . LYS   A  1  203 ? 15.013  -33.913 -48.979  1.00 59.30  ? 203  LYS   A O    1 
ATOM   3091  C  CB   . LYS   A  1  203 ? 13.857  -36.491 -48.440  1.00 57.26  ? 203  LYS   A CB   1 
ATOM   3092  C  CG   . LYS   A  1  203 ? 13.079  -37.719 -47.989  1.00 56.65  ? 203  LYS   A CG   1 
ATOM   3093  C  CD   . LYS   A  1  203 ? 13.166  -38.842 -49.014  1.00 55.93  ? 203  LYS   A CD   1 
ATOM   3094  C  CE   . LYS   A  1  203 ? 12.487  -40.112 -48.518  1.00 59.36  ? 203  LYS   A CE   1 
ATOM   3095  N  NZ   . LYS   A  1  203 ? 11.019  -39.944 -48.331  1.00 58.90  ? 203  LYS   A NZ   1 
ATOM   3096  H  H    . LYS   A  1  203 ? 12.133  -34.752 -48.014  1.00 68.16  ? 203  LYS   A H    1 
ATOM   3097  H  HA   . LYS   A  1  203 ? 14.159  -35.736 -46.558  1.00 67.13  ? 203  LYS   A HA   1 
ATOM   3098  H  HB2  . LYS   A  1  203 ? 13.435  -36.157 -49.247  1.00 68.75  ? 203  LYS   A HB2  1 
ATOM   3099  H  HB3  . LYS   A  1  203 ? 14.764  -36.773 -48.632  1.00 68.75  ? 203  LYS   A HB3  1 
ATOM   3100  H  HG2  . LYS   A  1  203 ? 13.445  -38.041 -47.151  1.00 68.01  ? 203  LYS   A HG2  1 
ATOM   3101  H  HG3  . LYS   A  1  203 ? 12.145  -37.483 -47.873  1.00 68.01  ? 203  LYS   A HG3  1 
ATOM   3102  H  HD2  . LYS   A  1  203 ? 12.727  -38.563 -49.833  1.00 67.15  ? 203  LYS   A HD2  1 
ATOM   3103  H  HD3  . LYS   A  1  203 ? 14.098  -39.044 -49.189  1.00 67.15  ? 203  LYS   A HD3  1 
ATOM   3104  H  HE2  . LYS   A  1  203 ? 12.628  -40.820 -49.166  1.00 71.26  ? 203  LYS   A HE2  1 
ATOM   3105  H  HE3  . LYS   A  1  203 ? 12.871  -40.364 -47.663  1.00 71.26  ? 203  LYS   A HE3  1 
ATOM   3106  H  HZ1  . LYS   A  1  203 ? 10.663  -40.696 -48.015  1.00 70.71  ? 203  LYS   A HZ1  1 
ATOM   3107  H  HZ2  . LYS   A  1  203 ? 10.859  -39.285 -47.755  1.00 70.71  ? 203  LYS   A HZ2  1 
ATOM   3108  H  HZ3  . LYS   A  1  203 ? 10.633  -39.747 -49.109  1.00 70.71  ? 203  LYS   A HZ3  1 
ATOM   3109  N  N    . TYR   A  1  204 ? 15.697  -33.825 -46.838  1.00 53.87  ? 204  TYR   A N    1 
ATOM   3110  C  CA   . TYR   A  1  204 ? 16.764  -32.867 -47.096  1.00 58.04  ? 204  TYR   A CA   1 
ATOM   3111  C  C    . TYR   A  1  204 ? 18.068  -33.624 -47.315  1.00 61.19  ? 204  TYR   A C    1 
ATOM   3112  O  O    . TYR   A  1  204 ? 18.532  -34.341 -46.422  1.00 61.75  ? 204  TYR   A O    1 
ATOM   3113  C  CB   . TYR   A  1  204 ? 16.925  -31.885 -45.937  1.00 57.71  ? 204  TYR   A CB   1 
ATOM   3114  C  CG   . TYR   A  1  204 ? 15.688  -31.086 -45.611  1.00 57.12  ? 204  TYR   A CG   1 
ATOM   3115  C  CD1  . TYR   A  1  204 ? 15.267  -30.052 -46.435  1.00 57.11  ? 204  TYR   A CD1  1 
ATOM   3116  C  CD2  . TYR   A  1  204 ? 14.949  -31.356 -44.469  1.00 58.12  ? 204  TYR   A CD2  1 
ATOM   3117  C  CE1  . TYR   A  1  204 ? 14.138  -29.316 -46.135  1.00 57.57  ? 204  TYR   A CE1  1 
ATOM   3118  C  CE2  . TYR   A  1  204 ? 13.820  -30.627 -44.160  1.00 57.20  ? 204  TYR   A CE2  1 
ATOM   3119  C  CZ   . TYR   A  1  204 ? 13.419  -29.607 -44.995  1.00 57.04  ? 204  TYR   A CZ   1 
ATOM   3120  O  OH   . TYR   A  1  204 ? 12.294  -28.877 -44.689  1.00 57.60  ? 204  TYR   A OH   1 
ATOM   3121  H  H    . TYR   A  1  204 ? 15.619  -34.044 -46.010  1.00 64.68  ? 204  TYR   A H    1 
ATOM   3122  H  HA   . TYR   A  1  204 ? 16.544  -32.363 -47.894  1.00 69.69  ? 204  TYR   A HA   1 
ATOM   3123  H  HB2  . TYR   A  1  204 ? 17.168  -32.384 -45.141  1.00 69.29  ? 204  TYR   A HB2  1 
ATOM   3124  H  HB3  . TYR   A  1  204 ? 17.628  -31.256 -46.161  1.00 69.29  ? 204  TYR   A HB3  1 
ATOM   3125  H  HD1  . TYR   A  1  204 ? 15.754  -29.850 -47.201  1.00 68.57  ? 204  TYR   A HD1  1 
ATOM   3126  H  HD2  . TYR   A  1  204 ? 15.219  -32.042 -43.901  1.00 69.79  ? 204  TYR   A HD2  1 
ATOM   3127  H  HE1  . TYR   A  1  204 ? 13.863  -28.629 -46.698  1.00 69.12  ? 204  TYR   A HE1  1 
ATOM   3128  H  HE2  . TYR   A  1  204 ? 13.332  -30.822 -43.392  1.00 68.67  ? 204  TYR   A HE2  1 
ATOM   3129  H  HH   . TYR   A  1  204 ? 11.963  -29.150 -43.967  1.00 69.16  ? 204  TYR   A HH   1 
ATOM   3130  N  N    . ASN   A  1  205 ? 18.653  -33.467 -48.497  1.00 63.84  ? 205  ASN   A N    1 
ATOM   3131  C  CA   . ASN   A  1  205 ? 19.977  -34.015 -48.732  1.00 67.24  ? 205  ASN   A CA   1 
ATOM   3132  C  C    . ASN   A  1  205 ? 21.004  -33.273 -47.880  1.00 64.90  ? 205  ASN   A C    1 
ATOM   3133  O  O    . ASN   A  1  205 ? 20.778  -32.148 -47.424  1.00 65.72  ? 205  ASN   A O    1 
ATOM   3134  C  CB   . ASN   A  1  205 ? 20.343  -33.918 -50.214  1.00 75.92  ? 205  ASN   A CB   1 
ATOM   3135  C  CG   . ASN   A  1  205 ? 21.594  -34.703 -50.559  1.00 86.93  ? 205  ASN   A CG   1 
ATOM   3136  O  OD1  . ASN   A  1  205 ? 22.052  -35.538 -49.780  1.00 89.08  ? 205  ASN   A OD1  1 
ATOM   3137  N  ND2  . ASN   A  1  205 ? 22.149  -34.444 -51.737  1.00 97.17  ? 205  ASN   A ND2  1 
ATOM   3138  H  H    . ASN   A  1  205 ? 18.309  -33.053 -49.167  1.00 76.65  ? 205  ASN   A H    1 
ATOM   3139  H  HA   . ASN   A  1  205 ? 19.996  -34.954 -48.488  1.00 80.72  ? 205  ASN   A HA   1 
ATOM   3140  H  HB2  . ASN   A  1  205 ? 19.611  -34.271 -50.744  1.00 91.15  ? 205  ASN   A HB2  1 
ATOM   3141  H  HB3  . ASN   A  1  205 ? 20.499  -32.988 -50.441  1.00 91.15  ? 205  ASN   A HB3  1 
ATOM   3142  H  HD21 . ASN   A  1  205 ? 22.860  -34.863 -51.979  1.00 116.64 ? 205  ASN   A HD21 1 
ATOM   3143  H  HD22 . ASN   A  1  205 ? 21.798  -33.856 -52.258  1.00 116.64 ? 205  ASN   A HD22 1 
ATOM   3144  N  N    . ASN   A  1  206 ? 22.142  -33.927 -47.654  1.00 59.27  ? 206  ASN   A N    1 
ATOM   3145  C  CA   . ASN   A  1  206 ? 23.258  -33.332 -46.921  1.00 60.09  ? 206  ASN   A CA   1 
ATOM   3146  C  C    . ASN   A  1  206 ? 22.854  -32.893 -45.516  1.00 55.06  ? 206  ASN   A C    1 
ATOM   3147  O  O    . ASN   A  1  206 ? 23.447  -31.972 -44.949  1.00 50.67  ? 206  ASN   A O    1 
ATOM   3148  C  CB   . ASN   A  1  206 ? 23.852  -32.150 -47.691  1.00 64.44  ? 206  ASN   A CB   1 
ATOM   3149  C  CG   . ASN   A  1  206 ? 24.376  -32.549 -49.053  1.00 69.62  ? 206  ASN   A CG   1 
ATOM   3150  O  OD1  . ASN   A  1  206 ? 24.947  -33.626 -49.220  1.00 71.66  ? 206  ASN   A OD1  1 
ATOM   3151  N  ND2  . ASN   A  1  206 ? 24.177  -31.683 -50.039  1.00 73.32  ? 206  ASN   A ND2  1 
ATOM   3152  H  H    . ASN   A  1  206 ? 22.294  -34.730 -47.921  1.00 71.16  ? 206  ASN   A H    1 
ATOM   3153  H  HA   . ASN   A  1  206 ? 23.944  -34.011 -46.822  1.00 72.14  ? 206  ASN   A HA   1 
ATOM   3154  H  HB2  . ASN   A  1  206 ? 23.165  -31.477 -47.817  1.00 77.37  ? 206  ASN   A HB2  1 
ATOM   3155  H  HB3  . ASN   A  1  206 ? 24.590  -31.779 -47.182  1.00 77.37  ? 206  ASN   A HB3  1 
ATOM   3156  H  HD21 . ASN   A  1  206 ? 24.456  -31.864 -50.832  1.00 88.02  ? 206  ASN   A HD21 1 
ATOM   3157  H  HD22 . ASN   A  1  206 ? 23.769  -30.942 -49.885  1.00 88.02  ? 206  ASN   A HD22 1 
ATOM   3158  N  N    . GLN   A  1  207 ? 21.842  -33.537 -44.942  1.00 56.18  ? 207  GLN   A N    1 
ATOM   3159  C  CA   . GLN   A  1  207 ? 21.482  -33.279 -43.557  1.00 52.87  ? 207  GLN   A CA   1 
ATOM   3160  C  C    . GLN   A  1  207 ? 22.472  -33.968 -42.625  1.00 55.20  ? 207  GLN   A C    1 
ATOM   3161  O  O    . GLN   A  1  207 ? 22.942  -35.075 -42.902  1.00 58.63  ? 207  GLN   A O    1 
ATOM   3162  C  CB   . GLN   A  1  207 ? 20.064  -33.769 -43.263  1.00 49.85  ? 207  GLN   A CB   1 
ATOM   3163  C  CG   . GLN   A  1  207 ? 19.612  -33.514 -41.829  1.00 46.43  ? 207  GLN   A CG   1 
ATOM   3164  C  CD   . GLN   A  1  207 ? 18.193  -33.981 -41.568  1.00 46.92  ? 207  GLN   A CD   1 
ATOM   3165  O  OE1  . GLN   A  1  207 ? 17.940  -35.174 -41.406  1.00 48.26  ? 207  GLN   A OE1  1 
ATOM   3166  N  NE2  . GLN   A  1  207 ? 17.259  -33.038 -41.522  1.00 50.26  ? 207  GLN   A NE2  1 
ATOM   3167  H  H    . GLN   A  1  207 ? 21.353  -34.126 -45.334  1.00 67.46  ? 207  GLN   A H    1 
ATOM   3168  H  HA   . GLN   A  1  207 ? 21.507  -32.324 -43.389  1.00 63.48  ? 207  GLN   A HA   1 
ATOM   3169  H  HB2  . GLN   A  1  207 ? 19.447  -33.310 -43.854  1.00 59.86  ? 207  GLN   A HB2  1 
ATOM   3170  H  HB3  . GLN   A  1  207 ? 20.026  -34.725 -43.420  1.00 59.86  ? 207  GLN   A HB3  1 
ATOM   3171  H  HG2  . GLN   A  1  207 ? 20.201  -33.990 -41.223  1.00 55.75  ? 207  GLN   A HG2  1 
ATOM   3172  H  HG3  . GLN   A  1  207 ? 19.651  -32.561 -41.650  1.00 55.75  ? 207  GLN   A HG3  1 
ATOM   3173  H  HE21 . GLN   A  1  207 ? 17.474  -32.214 -41.639  1.00 60.34  ? 207  GLN   A HE21 1 
ATOM   3174  H  HE22 . GLN   A  1  207 ? 16.439  -33.252 -41.377  1.00 60.34  ? 207  GLN   A HE22 1 
ATOM   3175  N  N    . LEU   A  1  208 ? 22.794  -33.298 -41.524  1.00 52.57  ? 208  LEU   A N    1 
ATOM   3176  C  CA   . LEU   A  1  208 ? 23.621  -33.854 -40.464  1.00 51.43  ? 208  LEU   A CA   1 
ATOM   3177  C  C    . LEU   A  1  208 ? 22.770  -34.010 -39.212  1.00 50.26  ? 208  LEU   A C    1 
ATOM   3178  O  O    . LEU   A  1  208 ? 21.968  -33.129 -38.888  1.00 52.43  ? 208  LEU   A O    1 
ATOM   3179  C  CB   . LEU   A  1  208 ? 24.825  -32.956 -40.174  1.00 53.94  ? 208  LEU   A CB   1 
ATOM   3180  C  CG   . LEU   A  1  208 ? 25.760  -32.678 -41.352  1.00 58.29  ? 208  LEU   A CG   1 
ATOM   3181  C  CD1  . LEU   A  1  208 ? 26.832  -31.677 -40.951  1.00 60.77  ? 208  LEU   A CD1  1 
ATOM   3182  C  CD2  . LEU   A  1  208 ? 26.391  -33.965 -41.860  1.00 55.92  ? 208  LEU   A CD2  1 
ATOM   3183  H  H    . LEU   A  1  208 ? 22.536  -32.493 -41.365  1.00 63.12  ? 208  LEU   A H    1 
ATOM   3184  H  HA   . LEU   A  1  208 ? 23.961  -34.725 -40.725  1.00 61.75  ? 208  LEU   A HA   1 
ATOM   3185  H  HB2  . LEU   A  1  208 ? 24.493  -32.099 -39.863  1.00 64.77  ? 208  LEU   A HB2  1 
ATOM   3186  H  HB3  . LEU   A  1  208 ? 25.355  -33.378 -39.480  1.00 64.77  ? 208  LEU   A HB3  1 
ATOM   3187  H  HG   . LEU   A  1  208 ? 25.244  -32.296 -42.080  1.00 69.98  ? 208  LEU   A HG   1 
ATOM   3188  H  HD11 . LEU   A  1  208 ? 27.421  -31.525 -41.707  1.00 72.97  ? 208  LEU   A HD11 1 
ATOM   3189  H  HD12 . LEU   A  1  208 ? 26.406  -30.845 -40.691  1.00 72.97  ? 208  LEU   A HD12 1 
ATOM   3190  H  HD13 . LEU   A  1  208 ? 27.337  -32.037 -40.205  1.00 72.97  ? 208  LEU   A HD13 1 
ATOM   3191  H  HD21 . LEU   A  1  208 ? 27.004  -33.753 -42.581  1.00 67.14  ? 208  LEU   A HD21 1 
ATOM   3192  H  HD22 . LEU   A  1  208 ? 26.871  -34.389 -41.131  1.00 67.14  ? 208  LEU   A HD22 1 
ATOM   3193  H  HD23 . LEU   A  1  208 ? 25.691  -34.554 -42.182  1.00 67.14  ? 208  LEU   A HD23 1 
ATOM   3194  N  N    . ALA   A  1  209 ? 22.934  -35.130 -38.511  1.00 48.81  ? 209  ALA   A N    1 
ATOM   3195  C  CA   . ALA   A  1  209 ? 22.092  -35.394 -37.352  1.00 47.85  ? 209  ALA   A CA   1 
ATOM   3196  C  C    . ALA   A  1  209 ? 22.763  -36.401 -36.432  1.00 49.83  ? 209  ALA   A C    1 
ATOM   3197  O  O    . ALA   A  1  209 ? 23.254  -37.435 -36.894  1.00 50.74  ? 209  ALA   A O    1 
ATOM   3198  C  CB   . ALA   A  1  209 ? 20.718  -35.915 -37.788  1.00 47.74  ? 209  ALA   A CB   1 
ATOM   3199  H  H    . ALA   A  1  209 ? 23.516  -35.739 -38.685  1.00 58.61  ? 209  ALA   A H    1 
ATOM   3200  H  HA   . ALA   A  1  209 ? 21.983  -34.569 -36.853  1.00 57.46  ? 209  ALA   A HA   1 
ATOM   3201  H  HB1  . ALA   A  1  209 ? 20.179  -36.083 -36.999  1.00 57.33  ? 209  ALA   A HB1  1 
ATOM   3202  H  HB2  . ALA   A  1  209 ? 20.289  -35.247 -38.345  1.00 57.33  ? 209  ALA   A HB2  1 
ATOM   3203  H  HB3  . ALA   A  1  209 ? 20.836  -36.737 -38.289  1.00 57.33  ? 209  ALA   A HB3  1 
ATOM   3204  N  N    . THR   A  1  210 ? 22.775  -36.096 -35.136  1.00 50.98  ? 210  THR   A N    1 
ATOM   3205  C  CA   . THR   A  1  210 ? 23.185  -37.081 -34.146  1.00 50.09  ? 210  THR   A CA   1 
ATOM   3206  C  C    . THR   A  1  210 ? 22.241  -38.276 -34.194  1.00 52.76  ? 210  THR   A C    1 
ATOM   3207  O  O    . THR   A  1  210 ? 21.071  -38.158 -34.568  1.00 52.82  ? 210  THR   A O    1 
ATOM   3208  C  CB   . THR   A  1  210 ? 23.191  -36.472 -32.742  1.00 43.11  ? 210  THR   A CB   1 
ATOM   3209  O  OG1  . THR   A  1  210 ? 21.898  -35.935 -32.439  1.00 42.84  ? 210  THR   A OG1  1 
ATOM   3210  C  CG2  . THR   A  1  210 ? 24.237  -35.372 -32.638  1.00 42.97  ? 210  THR   A CG2  1 
ATOM   3211  H  H    . THR   A  1  210 ? 22.552  -35.332 -34.809  1.00 61.22  ? 210  THR   A H    1 
ATOM   3212  H  HA   . THR   A  1  210 ? 24.087  -37.381 -34.337  1.00 60.14  ? 210  THR   A HA   1 
ATOM   3213  H  HB   . THR   A  1  210 ? 23.411  -37.161 -32.096  1.00 51.76  ? 210  THR   A HB   1 
ATOM   3214  H  HG1  . THR   A  1  210 ? 21.369  -36.555 -32.238  1.00 51.44  ? 210  THR   A HG1  1 
ATOM   3215  H  HG21 . THR   A  1  210 ? 24.240  -35.001 -31.742  1.00 51.60  ? 210  THR   A HG21 1 
ATOM   3216  H  HG22 . THR   A  1  210 ? 25.116  -35.730 -32.835  1.00 51.60  ? 210  THR   A HG22 1 
ATOM   3217  H  HG23 . THR   A  1  210 ? 24.037  -34.663 -33.270  1.00 51.60  ? 210  THR   A HG23 1 
ATOM   3218  N  N    . ARG   A  1  211 ? 22.757  -39.436 -33.808  1.00 55.79  ? 211  ARG   A N    1 
ATOM   3219  C  CA   . ARG   A  1  211 ? 22.038  -40.692 -33.941  1.00 60.47  ? 211  ARG   A CA   1 
ATOM   3220  C  C    . ARG   A  1  211 ? 21.562  -41.189 -32.583  1.00 60.01  ? 211  ARG   A C    1 
ATOM   3221  O  O    . ARG   A  1  211 ? 22.062  -40.781 -31.530  1.00 62.53  ? 211  ARG   A O    1 
ATOM   3222  C  CB   . ARG   A  1  211 ? 22.920  -41.754 -34.608  1.00 68.21  ? 211  ARG   A CB   1 
ATOM   3223  C  CG   . ARG   A  1  211 ? 23.255  -41.461 -36.068  1.00 72.81  ? 211  ARG   A CG   1 
ATOM   3224  C  CD   . ARG   A  1  211 ? 24.312  -42.421 -36.603  1.00 80.64  ? 211  ARG   A CD   1 
ATOM   3225  N  NE   . ARG   A  1  211 ? 23.843  -43.202 -37.748  1.00 89.72  ? 211  ARG   A NE   1 
ATOM   3226  C  CZ   . ARG   A  1  211 ? 24.094  -42.910 -39.024  1.00 100.44 ? 211  ARG   A CZ   1 
ATOM   3227  N  NH1  . ARG   A  1  211 ? 24.817  -41.845 -39.348  1.00 109.17 ? 211  ARG   A NH1  1 
ATOM   3228  N  NH2  . ARG   A  1  211 ? 23.620  -43.692 -39.983  1.00 102.95 ? 211  ARG   A NH2  1 
ATOM   3229  H  H    . ARG   A  1  211 ? 23.539  -39.521 -33.459  1.00 66.98  ? 211  ARG   A H    1 
ATOM   3230  H  HA   . ARG   A  1  211 ? 21.254  -40.551 -34.494  1.00 72.60  ? 211  ARG   A HA   1 
ATOM   3231  H  HB2  . ARG   A  1  211 ? 23.756  -41.814 -34.120  1.00 81.88  ? 211  ARG   A HB2  1 
ATOM   3232  H  HB3  . ARG   A  1  211 ? 22.457  -42.606 -34.578  1.00 81.88  ? 211  ARG   A HB3  1 
ATOM   3233  H  HG2  . ARG   A  1  211 ? 22.455  -41.558 -36.607  1.00 87.41  ? 211  ARG   A HG2  1 
ATOM   3234  H  HG3  . ARG   A  1  211 ? 23.598  -40.557 -36.144  1.00 87.41  ? 211  ARG   A HG3  1 
ATOM   3235  H  HD2  . ARG   A  1  211 ? 25.088  -41.912 -36.885  1.00 96.81  ? 211  ARG   A HD2  1 
ATOM   3236  H  HD3  . ARG   A  1  211 ? 24.560  -43.041 -35.899  1.00 96.81  ? 211  ARG   A HD3  1 
ATOM   3237  H  HE   . ARG   A  1  211 ? 23.370  -43.901 -37.586  1.00 107.70 ? 211  ARG   A HE   1 
ATOM   3238  H  HH11 . ARG   A  1  211 ? 25.129  -41.333 -38.731  1.00 131.04 ? 211  ARG   A HH11 1 
ATOM   3239  H  HH12 . ARG   A  1  211 ? 24.972  -41.666 -40.175  1.00 131.04 ? 211  ARG   A HH12 1 
ATOM   3240  H  HH21 . ARG   A  1  211 ? 23.152  -44.385 -39.782  1.00 123.58 ? 211  ARG   A HH21 1 
ATOM   3241  H  HH22 . ARG   A  1  211 ? 23.780  -43.506 -40.808  1.00 123.58 ? 211  ARG   A HH22 1 
ATOM   3242  N  N    . THR   A  1  212 ? 20.572  -42.078 -32.626  1.00 56.35  ? 212  THR   A N    1 
ATOM   3243  C  CA   . THR   A  1  212 ? 20.073  -42.705 -31.411  1.00 51.97  ? 212  THR   A CA   1 
ATOM   3244  C  C    . THR   A  1  212 ? 21.165  -43.554 -30.774  1.00 55.30  ? 212  THR   A C    1 
ATOM   3245  O  O    . THR   A  1  212 ? 21.898  -44.269 -31.462  1.00 59.46  ? 212  THR   A O    1 
ATOM   3246  C  CB   . THR   A  1  212 ? 18.858  -43.577 -31.723  1.00 48.81  ? 212  THR   A CB   1 
ATOM   3247  O  OG1  . THR   A  1  212 ? 17.891  -42.816 -32.456  1.00 55.72  ? 212  THR   A OG1  1 
ATOM   3248  C  CG2  . THR   A  1  212 ? 18.224  -44.092 -30.439  1.00 47.52  ? 212  THR   A CG2  1 
ATOM   3249  H  H    . THR   A  1  212 ? 20.176  -42.334 -33.344  1.00 67.66  ? 212  THR   A H    1 
ATOM   3250  H  HA   . THR   A  1  212 ? 19.800  -42.018 -30.782  1.00 62.40  ? 212  THR   A HA   1 
ATOM   3251  H  HB   . THR   A  1  212 ? 19.137  -44.339 -32.254  1.00 58.61  ? 212  THR   A HB   1 
ATOM   3252  H  HG1  . THR   A  1  212 ? 17.586  -42.199 -31.974  1.00 66.90  ? 212  THR   A HG1  1 
ATOM   3253  H  HG21 . THR   A  1  212 ? 17.429  -44.608 -30.646  1.00 57.07  ? 212  THR   A HG21 1 
ATOM   3254  H  HG22 . THR   A  1  212 ? 18.852  -44.658 -29.963  1.00 57.07  ? 212  THR   A HG22 1 
ATOM   3255  H  HG23 . THR   A  1  212 ? 17.977  -43.347 -29.869  1.00 57.07  ? 212  THR   A HG23 1 
ATOM   3256  N  N    . ALA   A  1  213 ? 21.263  -43.481 -29.454  1.00 54.66  ? 213  ALA   A N    1 
ATOM   3257  C  CA   . ALA   A  1  213 ? 22.284  -44.192 -28.703  1.00 54.54  ? 213  ALA   A CA   1 
ATOM   3258  C  C    . ALA   A  1  213 ? 21.627  -45.088 -27.658  1.00 52.93  ? 213  ALA   A C    1 
ATOM   3259  O  O    . ALA   A  1  213 ? 20.404  -45.105 -27.495  1.00 52.03  ? 213  ALA   A O    1 
ATOM   3260  C  CB   . ALA   A  1  213 ? 23.260  -43.210 -28.047  1.00 52.61  ? 213  ALA   A CB   1 
ATOM   3261  H  H    . ALA   A  1  213 ? 20.736  -43.013 -28.961  1.00 65.63  ? 213  ALA   A H    1 
ATOM   3262  H  HA   . ALA   A  1  213 ? 22.785  -44.758 -29.311  1.00 65.48  ? 213  ALA   A HA   1 
ATOM   3263  H  HB1  . ALA   A  1  213 ? 23.935  -43.712 -27.564  1.00 63.17  ? 213  ALA   A HB1  1 
ATOM   3264  H  HB2  . ALA   A  1  213 ? 23.678  -42.672 -28.738  1.00 63.17  ? 213  ALA   A HB2  1 
ATOM   3265  H  HB3  . ALA   A  1  213 ? 22.770  -42.640 -27.434  1.00 63.17  ? 213  ALA   A HB3  1 
ATOM   3266  N  N    . GLN   A  1  214 ? 22.468  -45.838 -26.949  1.00 54.34  ? 214  GLN   A N    1 
ATOM   3267  C  CA   . GLN   A  1  214 ? 22.008  -46.787 -25.944  1.00 54.83  ? 214  GLN   A CA   1 
ATOM   3268  C  C    . GLN   A  1  214 ? 21.106  -46.091 -24.933  1.00 53.60  ? 214  GLN   A C    1 
ATOM   3269  O  O    . GLN   A  1  214 ? 21.198  -44.873 -24.745  1.00 52.30  ? 214  GLN   A O    1 
ATOM   3270  C  CB   . GLN   A  1  214 ? 23.203  -47.445 -25.250  1.00 51.35  ? 214  GLN   A CB   1 
ATOM   3271  C  CG   . GLN   A  1  214 ? 24.119  -48.234 -26.190  1.00 55.39  ? 214  GLN   A CG   1 
ATOM   3272  C  CD   . GLN   A  1  214 ? 25.135  -47.360 -26.907  1.00 61.53  ? 214  GLN   A CD   1 
ATOM   3273  O  OE1  . GLN   A  1  214 ? 25.026  -46.134 -26.906  1.00 61.81  ? 214  GLN   A OE1  1 
ATOM   3274  N  NE2  . GLN   A  1  214 ? 26.129  -47.990 -27.522  1.00 67.97  ? 214  GLN   A NE2  1 
ATOM   3275  H  H    . GLN   A  1  214 ? 23.324  -45.814 -27.033  1.00 65.24  ? 214  GLN   A H    1 
ATOM   3276  H  HA   . GLN   A  1  214 ? 21.492  -47.489 -26.371  1.00 65.83  ? 214  GLN   A HA   1 
ATOM   3277  H  HB2  . GLN   A  1  214 ? 23.738  -46.753 -24.831  1.00 61.66  ? 214  GLN   A HB2  1 
ATOM   3278  H  HB3  . GLN   A  1  214 ? 22.871  -48.061 -24.578  1.00 61.66  ? 214  GLN   A HB3  1 
ATOM   3279  H  HG2  . GLN   A  1  214 ? 24.606  -48.895 -25.673  1.00 66.51  ? 214  GLN   A HG2  1 
ATOM   3280  H  HG3  . GLN   A  1  214 ? 23.576  -48.674 -26.863  1.00 66.51  ? 214  GLN   A HG3  1 
ATOM   3281  H  HE21 . GLN   A  1  214 ? 26.173  -48.849 -27.501  1.00 81.60  ? 214  GLN   A HE21 1 
ATOM   3282  H  HE22 . GLN   A  1  214 ? 26.730  -47.540 -27.942  1.00 81.60  ? 214  GLN   A HE22 1 
ATOM   3283  N  N    . ALA   A  1  215 ? 20.230  -46.856 -24.277  1.00 54.00  ? 215  ALA   A N    1 
ATOM   3284  C  CA   . ALA   A  1  215 ? 19.232  -46.260 -23.396  1.00 52.47  ? 215  ALA   A CA   1 
ATOM   3285  C  C    . ALA   A  1  215 ? 19.848  -45.571 -22.186  1.00 54.00  ? 215  ALA   A C    1 
ATOM   3286  O  O    . ALA   A  1  215 ? 19.191  -44.717 -21.580  1.00 50.74  ? 215  ALA   A O    1 
ATOM   3287  C  CB   . ALA   A  1  215 ? 18.240  -47.324 -22.928  1.00 51.50  ? 215  ALA   A CB   1 
ATOM   3288  H  H    . ALA   A  1  215 ? 20.194  -47.714 -24.325  1.00 64.83  ? 215  ALA   A H    1 
ATOM   3289  H  HA   . ALA   A  1  215 ? 18.745  -45.590 -23.902  1.00 63.00  ? 215  ALA   A HA   1 
ATOM   3290  H  HB1  . ALA   A  1  215 ? 17.595  -46.914 -22.331  1.00 61.84  ? 215  ALA   A HB1  1 
ATOM   3291  H  HB2  . ALA   A  1  215 ? 17.786  -47.695 -23.701  1.00 61.84  ? 215  ALA   A HB2  1 
ATOM   3292  H  HB3  . ALA   A  1  215 ? 18.724  -48.024 -22.462  1.00 61.84  ? 215  ALA   A HB3  1 
ATOM   3293  N  N    . ILE   A  1  216 ? 21.085  -45.914 -21.817  1.00 61.48  ? 216  ILE   A N    1 
ATOM   3294  C  CA   . ILE   A  1  216 ? 21.721  -45.257 -20.682  1.00 65.25  ? 216  ILE   A CA   1 
ATOM   3295  C  C    . ILE   A  1  216 ? 21.765  -43.748 -20.871  1.00 59.72  ? 216  ILE   A C    1 
ATOM   3296  O  O    . ILE   A  1  216 ? 21.837  -43.002 -19.889  1.00 59.77  ? 216  ILE   A O    1 
ATOM   3297  C  CB   . ILE   A  1  216 ? 23.143  -45.812 -20.448  1.00 73.87  ? 216  ILE   A CB   1 
ATOM   3298  C  CG1  . ILE   A  1  216 ? 23.762  -45.162 -19.205  1.00 81.79  ? 216  ILE   A CG1  1 
ATOM   3299  C  CG2  . ILE   A  1  216 ? 24.021  -45.571 -21.670  1.00 77.17  ? 216  ILE   A CG2  1 
ATOM   3300  C  CD1  . ILE   A  1  216 ? 25.115  -45.718 -18.811  1.00 89.39  ? 216  ILE   A CD1  1 
ATOM   3301  H  H    . ILE   A  1  216 ? 21.566  -46.513 -22.203  1.00 73.81  ? 216  ILE   A H    1 
ATOM   3302  H  HA   . ILE   A  1  216 ? 21.194  -45.455 -19.892  1.00 78.34  ? 216  ILE   A HA   1 
ATOM   3303  H  HB   . ILE   A  1  216 ? 23.081  -46.770 -20.303  1.00 88.68  ? 216  ILE   A HB   1 
ATOM   3304  H  HG12 . ILE   A  1  216 ? 23.873  -44.214 -19.376  1.00 98.18  ? 216  ILE   A HG12 1 
ATOM   3305  H  HG13 . ILE   A  1  216 ? 23.161  -45.296 -18.456  1.00 98.18  ? 216  ILE   A HG13 1 
ATOM   3306  H  HG21 . ILE   A  1  216 ? 24.890  -45.973 -21.519  1.00 92.64  ? 216  ILE   A HG21 1 
ATOM   3307  H  HG22 . ILE   A  1  216 ? 23.600  -45.974 -22.446  1.00 92.64  ? 216  ILE   A HG22 1 
ATOM   3308  H  HG23 . ILE   A  1  216 ? 24.118  -44.615 -21.806  1.00 92.64  ? 216  ILE   A HG23 1 
ATOM   3309  H  HD11 . ILE   A  1  216 ? 25.419  -45.269 -18.006  1.00 107.31 ? 216  ILE   A HD11 1 
ATOM   3310  H  HD12 . ILE   A  1  216 ? 25.030  -46.670 -18.646  1.00 107.31 ? 216  ILE   A HD12 1 
ATOM   3311  H  HD13 . ILE   A  1  216 ? 25.743  -45.562 -19.533  1.00 107.31 ? 216  ILE   A HD13 1 
ATOM   3312  N  N    . PHE   A  1  217 ? 21.720  -43.277 -22.114  1.00 53.91  ? 217  PHE   A N    1 
ATOM   3313  C  CA   . PHE   A  1  217 ? 21.792  -41.854 -22.412  1.00 50.38  ? 217  PHE   A CA   1 
ATOM   3314  C  C    . PHE   A  1  217 ? 20.429  -41.176 -22.423  1.00 45.90  ? 217  PHE   A C    1 
ATOM   3315  O  O    . PHE   A  1  217 ? 20.357  -39.972 -22.688  1.00 44.34  ? 217  PHE   A O    1 
ATOM   3316  C  CB   . PHE   A  1  217 ? 22.488  -41.644 -23.760  1.00 46.97  ? 217  PHE   A CB   1 
ATOM   3317  C  CG   . PHE   A  1  217 ? 23.868  -42.229 -23.818  1.00 46.10  ? 217  PHE   A CG   1 
ATOM   3318  C  CD1  . PHE   A  1  217 ? 24.947  -41.540 -23.289  1.00 43.20  ? 217  PHE   A CD1  1 
ATOM   3319  C  CD2  . PHE   A  1  217 ? 24.088  -43.472 -24.389  1.00 45.68  ? 217  PHE   A CD2  1 
ATOM   3320  C  CE1  . PHE   A  1  217 ? 26.219  -42.075 -23.334  1.00 42.59  ? 217  PHE   A CE1  1 
ATOM   3321  C  CE2  . PHE   A  1  217 ? 25.359  -44.013 -24.438  1.00 45.10  ? 217  PHE   A CE2  1 
ATOM   3322  C  CZ   . PHE   A  1  217 ? 26.426  -43.313 -23.908  1.00 42.61  ? 217  PHE   A CZ   1 
ATOM   3323  H  H    . PHE   A  1  217 ? 21.646  -43.772 -22.813  1.00 64.73  ? 217  PHE   A H    1 
ATOM   3324  H  HA   . PHE   A  1  217 ? 22.324  -41.419 -21.728  1.00 60.49  ? 217  PHE   A HA   1 
ATOM   3325  H  HB2  . PHE   A  1  217 ? 21.957  -42.065 -24.454  1.00 56.41  ? 217  PHE   A HB2  1 
ATOM   3326  H  HB3  . PHE   A  1  217 ? 22.561  -40.692 -23.929  1.00 56.41  ? 217  PHE   A HB3  1 
ATOM   3327  H  HD1  . PHE   A  1  217 ? 24.813  -40.706 -22.900  1.00 51.87  ? 217  PHE   A HD1  1 
ATOM   3328  H  HD2  . PHE   A  1  217 ? 23.372  -43.948 -24.744  1.00 54.85  ? 217  PHE   A HD2  1 
ATOM   3329  H  HE1  . PHE   A  1  217 ? 26.936  -41.602 -22.978  1.00 51.14  ? 217  PHE   A HE1  1 
ATOM   3330  H  HE2  . PHE   A  1  217 ? 25.496  -44.846 -24.827  1.00 54.16  ? 217  PHE   A HE2  1 
ATOM   3331  H  HZ   . PHE   A  1  217 ? 27.282  -43.676 -23.938  1.00 51.17  ? 217  PHE   A HZ   1 
ATOM   3332  N  N    . ASP   A  1  218 ? 19.354  -41.910 -22.146  1.00 44.14  ? 218  ASP   A N    1 
ATOM   3333  C  CA   . ASP   A  1  218 ? 18.032  -41.302 -22.094  1.00 48.54  ? 218  ASP   A CA   1 
ATOM   3334  C  C    . ASP   A  1  218 ? 18.018  -40.134 -21.114  1.00 48.47  ? 218  ASP   A C    1 
ATOM   3335  O  O    . ASP   A  1  218 ? 18.775  -40.100 -20.140  1.00 48.93  ? 218  ASP   A O    1 
ATOM   3336  C  CB   . ASP   A  1  218 ? 16.982  -42.334 -21.677  1.00 54.23  ? 218  ASP   A CB   1 
ATOM   3337  C  CG   . ASP   A  1  218 ? 16.764  -43.407 -22.726  1.00 57.45  ? 218  ASP   A CG   1 
ATOM   3338  O  OD1  . ASP   A  1  218 ? 17.317  -43.279 -23.838  1.00 57.93  ? 218  ASP   A OD1  1 
ATOM   3339  O  OD2  . ASP   A  1  218 ? 16.038  -44.379 -22.433  1.00 60.78  ? 218  ASP   A OD2  1 
ATOM   3340  H  H    . ASP   A  1  218 ? 19.364  -42.755 -21.985  1.00 53.00  ? 218  ASP   A H    1 
ATOM   3341  H  HA   . ASP   A  1  218 ? 17.800  -40.971 -22.976  1.00 58.29  ? 218  ASP   A HA   1 
ATOM   3342  H  HB2  . ASP   A  1  218 ? 17.273  -42.769 -20.860  1.00 65.11  ? 218  ASP   A HB2  1 
ATOM   3343  H  HB3  . ASP   A  1  218 ? 16.136  -41.883 -21.530  1.00 65.11  ? 218  ASP   A HB3  1 
ATOM   3344  N  N    . ASP   A  1  219 ? 17.148  -39.163 -21.389  1.00 49.19  ? 219  ASP   A N    1 
ATOM   3345  C  CA   . ASP   A  1  219 ? 16.902  -38.052 -20.470  1.00 50.14  ? 219  ASP   A CA   1 
ATOM   3346  C  C    . ASP   A  1  219 ? 18.163  -37.218 -20.247  1.00 52.03  ? 219  ASP   A C    1 
ATOM   3347  O  O    . ASP   A  1  219 ? 18.467  -36.806 -19.126  1.00 53.73  ? 219  ASP   A O    1 
ATOM   3348  C  CB   . ASP   A  1  219 ? 16.348  -38.571 -19.141  1.00 50.47  ? 219  ASP   A CB   1 
ATOM   3349  C  CG   . ASP   A  1  219 ? 15.075  -39.378 -19.318  1.00 56.56  ? 219  ASP   A CG   1 
ATOM   3350  O  OD1  . ASP   A  1  219 ? 14.096  -38.836 -19.873  1.00 56.94  ? 219  ASP   A OD1  1 
ATOM   3351  O  OD2  . ASP   A  1  219 ? 15.058  -40.560 -18.916  1.00 58.20  ? 219  ASP   A OD2  1 
ATOM   3352  H  H    . ASP   A  1  219 ? 16.681  -39.125 -22.110  1.00 59.06  ? 219  ASP   A H    1 
ATOM   3353  H  HA   . ASP   A  1  219 ? 16.243  -37.462 -20.868  1.00 60.21  ? 219  ASP   A HA   1 
ATOM   3354  H  HB2  . ASP   A  1  219 ? 17.011  -39.142 -18.722  1.00 60.60  ? 219  ASP   A HB2  1 
ATOM   3355  H  HB3  . ASP   A  1  219 ? 16.148  -37.817 -18.565  1.00 60.60  ? 219  ASP   A HB3  1 
ATOM   3356  N  N    . SER   A  1  220 ? 18.901  -36.960 -21.328  1.00 50.88  ? 220  SER   A N    1 
ATOM   3357  C  CA   . SER   A  1  220 ? 20.104  -36.137 -21.274  1.00 47.24  ? 220  SER   A CA   1 
ATOM   3358  C  C    . SER   A  1  220 ? 19.876  -34.706 -21.738  1.00 46.73  ? 220  SER   A C    1 
ATOM   3359  O  O    . SER   A  1  220 ? 20.549  -33.794 -21.245  1.00 46.91  ? 220  SER   A O    1 
ATOM   3360  C  CB   . SER   A  1  220 ? 21.212  -36.759 -22.130  1.00 47.64  ? 220  SER   A CB   1 
ATOM   3361  O  OG   . SER   A  1  220 ? 21.630  -38.005 -21.600  1.00 51.84  ? 220  SER   A OG   1 
ATOM   3362  H  H    . SER   A  1  220 ? 18.722  -37.256 -22.115  1.00 61.09  ? 220  SER   A H    1 
ATOM   3363  H  HA   . SER   A  1  220 ? 20.415  -36.107 -20.355  1.00 56.73  ? 220  SER   A HA   1 
ATOM   3364  H  HB2  . SER   A  1  220 ? 20.875  -36.897 -23.029  1.00 57.21  ? 220  SER   A HB2  1 
ATOM   3365  H  HB3  . SER   A  1  220 ? 21.971  -36.156 -22.149  1.00 57.21  ? 220  SER   A HB3  1 
ATOM   3366  H  HG   . SER   A  1  220 ? 21.406  -38.627 -22.119  1.00 62.25  ? 220  SER   A HG   1 
ATOM   3367  N  N    . TYR   A  1  221 ? 18.957  -34.494 -22.684  1.00 45.74  ? 221  TYR   A N    1 
ATOM   3368  C  CA   . TYR   A  1  221 ? 18.583  -33.164 -23.172  1.00 45.55  ? 221  TYR   A CA   1 
ATOM   3369  C  C    . TYR   A  1  221 ? 19.663  -32.555 -24.072  1.00 43.21  ? 221  TYR   A C    1 
ATOM   3370  O  O    . TYR   A  1  221 ? 19.951  -31.361 -23.985  1.00 41.53  ? 221  TYR   A O    1 
ATOM   3371  C  CB   . TYR   A  1  221 ? 18.256  -32.203 -22.023  1.00 50.90  ? 221  TYR   A CB   1 
ATOM   3372  C  CG   . TYR   A  1  221 ? 16.946  -32.454 -21.301  1.00 53.11  ? 221  TYR   A CG   1 
ATOM   3373  C  CD1  . TYR   A  1  221 ? 16.128  -33.529 -21.631  1.00 51.41  ? 221  TYR   A CD1  1 
ATOM   3374  C  CD2  . TYR   A  1  221 ? 16.525  -31.600 -20.290  1.00 51.13  ? 221  TYR   A CD2  1 
ATOM   3375  C  CE1  . TYR   A  1  221 ? 14.932  -33.746 -20.966  1.00 48.06  ? 221  TYR   A CE1  1 
ATOM   3376  C  CE2  . TYR   A  1  221 ? 15.336  -31.808 -19.623  1.00 48.89  ? 221  TYR   A CE2  1 
ATOM   3377  C  CZ   . TYR   A  1  221 ? 14.543  -32.881 -19.963  1.00 49.06  ? 221  TYR   A CZ   1 
ATOM   3378  O  OH   . TYR   A  1  221 ? 13.357  -33.085 -19.296  1.00 55.11  ? 221  TYR   A OH   1 
ATOM   3379  H  H    . TYR   A  1  221 ? 18.522  -35.127 -23.071  1.00 54.93  ? 221  TYR   A H    1 
ATOM   3380  H  HA   . TYR   A  1  221 ? 17.784  -33.275 -23.712  1.00 54.69  ? 221  TYR   A HA   1 
ATOM   3381  H  HB2  . TYR   A  1  221 ? 18.964  -32.267 -21.363  1.00 61.11  ? 221  TYR   A HB2  1 
ATOM   3382  H  HB3  . TYR   A  1  221 ? 18.218  -31.302 -22.381  1.00 61.11  ? 221  TYR   A HB3  1 
ATOM   3383  H  HD1  . TYR   A  1  221 ? 16.388  -34.111 -22.308  1.00 61.73  ? 221  TYR   A HD1  1 
ATOM   3384  H  HD2  . TYR   A  1  221 ? 17.056  -30.872 -20.058  1.00 61.39  ? 221  TYR   A HD2  1 
ATOM   3385  H  HE1  . TYR   A  1  221 ? 14.395  -34.471 -21.193  1.00 57.71  ? 221  TYR   A HE1  1 
ATOM   3386  H  HE2  . TYR   A  1  221 ? 15.071  -31.227 -18.948  1.00 58.71  ? 221  TYR   A HE2  1 
ATOM   3387  H  HH   . TYR   A  1  221 ? 13.255  -32.497 -18.705  1.00 66.17  ? 221  TYR   A HH   1 
ATOM   3388  N  N    . LEU   A  1  222 ? 20.260  -33.365 -24.945  1.00 40.07  ? 222  LEU   A N    1 
ATOM   3389  C  CA   . LEU   A  1  222 ? 21.097  -32.800 -25.997  1.00 40.80  ? 222  LEU   A CA   1 
ATOM   3390  C  C    . LEU   A  1  222 ? 20.275  -31.820 -26.827  1.00 41.43  ? 222  LEU   A C    1 
ATOM   3391  O  O    . LEU   A  1  222 ? 19.119  -32.086 -27.163  1.00 39.62  ? 222  LEU   A O    1 
ATOM   3392  C  CB   . LEU   A  1  222 ? 21.665  -33.901 -26.895  1.00 42.18  ? 222  LEU   A CB   1 
ATOM   3393  C  CG   . LEU   A  1  222 ? 22.440  -33.419 -28.130  1.00 42.73  ? 222  LEU   A CG   1 
ATOM   3394  C  CD1  . LEU   A  1  222 ? 23.658  -32.591 -27.733  1.00 43.91  ? 222  LEU   A CD1  1 
ATOM   3395  C  CD2  . LEU   A  1  222 ? 22.855  -34.592 -29.007  1.00 40.15  ? 222  LEU   A CD2  1 
ATOM   3396  H  H    . LEU   A  1  222 ? 20.197  -34.222 -24.950  1.00 48.12  ? 222  LEU   A H    1 
ATOM   3397  H  HA   . LEU   A  1  222 ? 21.849  -32.334 -25.600  1.00 49.00  ? 222  LEU   A HA   1 
ATOM   3398  H  HB2  . LEU   A  1  222 ? 22.273  -34.441 -26.366  1.00 50.65  ? 222  LEU   A HB2  1 
ATOM   3399  H  HB3  . LEU   A  1  222 ? 20.928  -34.445 -27.212  1.00 50.65  ? 222  LEU   A HB3  1 
ATOM   3400  H  HG   . LEU   A  1  222 ? 21.853  -32.848 -28.650  1.00 51.31  ? 222  LEU   A HG   1 
ATOM   3401  H  HD11 . LEU   A  1  222 ? 24.117  -32.300 -28.536  1.00 52.73  ? 222  LEU   A HD11 1 
ATOM   3402  H  HD12 . LEU   A  1  222 ? 23.363  -31.821 -27.222  1.00 52.73  ? 222  LEU   A HD12 1 
ATOM   3403  H  HD13 . LEU   A  1  222 ? 24.250  -33.139 -27.193  1.00 52.73  ? 222  LEU   A HD13 1 
ATOM   3404  H  HD21 . LEU   A  1  222 ? 23.328  -34.254 -29.784  1.00 48.22  ? 222  LEU   A HD21 1 
ATOM   3405  H  HD22 . LEU   A  1  222 ? 23.435  -35.179 -28.497  1.00 48.22  ? 222  LEU   A HD22 1 
ATOM   3406  H  HD23 . LEU   A  1  222 ? 22.061  -35.074 -29.287  1.00 48.22  ? 222  LEU   A HD23 1 
ATOM   3407  N  N    . GLY   A  1  223 ? 20.873  -30.681 -27.160  1.00 43.83  ? 223  GLY   A N    1 
ATOM   3408  C  CA   . GLY   A  1  223 ? 20.160  -29.656 -27.891  1.00 42.21  ? 223  GLY   A CA   1 
ATOM   3409  C  C    . GLY   A  1  223 ? 19.358  -28.706 -27.033  1.00 44.49  ? 223  GLY   A C    1 
ATOM   3410  O  O    . GLY   A  1  223 ? 18.598  -27.894 -27.577  1.00 41.80  ? 223  GLY   A O    1 
ATOM   3411  H  H    . GLY   A  1  223 ? 21.688  -30.484 -26.972  1.00 52.63  ? 223  GLY   A H    1 
ATOM   3412  H  HA2  . GLY   A  1  223 ? 20.801  -29.131 -28.395  1.00 50.69  ? 223  GLY   A HA2  1 
ATOM   3413  H  HA3  . GLY   A  1  223 ? 19.547  -30.085 -28.510  1.00 50.69  ? 223  GLY   A HA3  1 
ATOM   3414  N  N    . TYR   A  1  224 ? 19.485  -28.794 -25.708  1.00 45.68  ? 224  TYR   A N    1 
ATOM   3415  C  CA   . TYR   A  1  224 ? 18.905  -27.782 -24.831  1.00 43.93  ? 224  TYR   A CA   1 
ATOM   3416  C  C    . TYR   A  1  224 ? 19.412  -26.391 -25.190  1.00 45.08  ? 224  TYR   A C    1 
ATOM   3417  O  O    . TYR   A  1  224 ? 18.676  -25.406 -25.062  1.00 43.25  ? 224  TYR   A O    1 
ATOM   3418  C  CB   . TYR   A  1  224 ? 19.246  -28.126 -23.379  1.00 42.34  ? 224  TYR   A CB   1 
ATOM   3419  C  CG   . TYR   A  1  224 ? 18.377  -27.479 -22.325  1.00 40.97  ? 224  TYR   A CG   1 
ATOM   3420  C  CD1  . TYR   A  1  224 ? 18.647  -26.199 -21.862  1.00 39.68  ? 224  TYR   A CD1  1 
ATOM   3421  C  CD2  . TYR   A  1  224 ? 17.303  -28.164 -21.767  1.00 43.75  ? 224  TYR   A CD2  1 
ATOM   3422  C  CE1  . TYR   A  1  224 ? 17.862  -25.610 -20.888  1.00 45.00  ? 224  TYR   A CE1  1 
ATOM   3423  C  CE2  . TYR   A  1  224 ? 16.514  -27.583 -20.791  1.00 45.87  ? 224  TYR   A CE2  1 
ATOM   3424  C  CZ   . TYR   A  1  224 ? 16.799  -26.307 -20.355  1.00 46.92  ? 224  TYR   A CZ   1 
ATOM   3425  O  OH   . TYR   A  1  224 ? 16.018  -25.725 -19.384  1.00 47.64  ? 224  TYR   A OH   1 
ATOM   3426  H  H    . TYR   A  1  224 ? 19.899  -29.425 -25.296  1.00 54.86  ? 224  TYR   A H    1 
ATOM   3427  H  HA   . TYR   A  1  224 ? 17.940  -27.778 -24.924  1.00 52.75  ? 224  TYR   A HA   1 
ATOM   3428  H  HB2  . TYR   A  1  224 ? 19.166  -29.087 -23.268  1.00 50.84  ? 224  TYR   A HB2  1 
ATOM   3429  H  HB3  . TYR   A  1  224 ? 20.160  -27.848 -23.208  1.00 50.84  ? 224  TYR   A HB3  1 
ATOM   3430  H  HD1  . TYR   A  1  224 ? 19.368  -25.729 -22.214  1.00 47.65  ? 224  TYR   A HD1  1 
ATOM   3431  H  HD2  . TYR   A  1  224 ? 17.113  -29.027 -22.054  1.00 52.54  ? 224  TYR   A HD2  1 
ATOM   3432  H  HE1  . TYR   A  1  224 ? 18.051  -24.749 -20.594  1.00 54.03  ? 224  TYR   A HE1  1 
ATOM   3433  H  HE2  . TYR   A  1  224 ? 15.795  -28.051 -20.432  1.00 55.09  ? 224  TYR   A HE2  1 
ATOM   3434  H  HH   . TYR   A  1  224 ? 15.465  -26.283 -19.087  1.00 57.21  ? 224  TYR   A HH   1 
ATOM   3435  N  N    . SER   A  1  225 ? 20.658  -26.296 -25.652  1.00 45.78  ? 225  SER   A N    1 
ATOM   3436  C  CA   . SER   A  1  225 ? 21.281  -25.033 -26.019  1.00 43.69  ? 225  SER   A CA   1 
ATOM   3437  C  C    . SER   A  1  225 ? 22.355  -25.322 -27.056  1.00 41.67  ? 225  SER   A C    1 
ATOM   3438  O  O    . SER   A  1  225 ? 22.942  -26.406 -27.063  1.00 41.59  ? 225  SER   A O    1 
ATOM   3439  C  CB   . SER   A  1  225 ? 21.894  -24.336 -24.802  1.00 46.05  ? 225  SER   A CB   1 
ATOM   3440  O  OG   . SER   A  1  225 ? 22.945  -25.116 -24.255  1.00 51.37  ? 225  SER   A OG   1 
ATOM   3441  H  H    . SER   A  1  225 ? 21.177  -26.973 -25.765  1.00 54.97  ? 225  SER   A H    1 
ATOM   3442  H  HA   . SER   A  1  225 ? 20.622  -24.435 -26.406  1.00 52.47  ? 225  SER   A HA   1 
ATOM   3443  H  HB2  . SER   A  1  225 ? 22.248  -23.475 -25.075  1.00 55.30  ? 225  SER   A HB2  1 
ATOM   3444  H  HB3  . SER   A  1  225 ? 21.207  -24.214 -24.128  1.00 55.30  ? 225  SER   A HB3  1 
ATOM   3445  H  HG   . SER   A  1  225 ? 22.789  -25.282 -23.446  1.00 61.69  ? 225  SER   A HG   1 
ATOM   3446  N  N    . VAL   A  1  226 ? 22.612  -24.351 -27.934  1.00 44.90  ? 226  VAL   A N    1 
ATOM   3447  C  CA   . VAL   A  1  226 ? 23.592  -24.529 -28.998  1.00 46.44  ? 226  VAL   A CA   1 
ATOM   3448  C  C    . VAL   A  1  226 ? 24.343  -23.230 -29.258  1.00 47.86  ? 226  VAL   A C    1 
ATOM   3449  O  O    . VAL   A  1  226 ? 23.801  -22.130 -29.112  1.00 51.52  ? 226  VAL   A O    1 
ATOM   3450  C  CB   . VAL   A  1  226 ? 22.944  -25.022 -30.315  1.00 43.45  ? 226  VAL   A CB   1 
ATOM   3451  C  CG1  . VAL   A  1  226 ? 22.242  -26.354 -30.104  1.00 45.05  ? 226  VAL   A CG1  1 
ATOM   3452  C  CG2  . VAL   A  1  226 ? 21.982  -23.976 -30.869  1.00 39.73  ? 226  VAL   A CG2  1 
ATOM   3453  H  H    . VAL   A  1  226 ? 22.229  -23.581 -27.931  1.00 53.92  ? 226  VAL   A H    1 
ATOM   3454  H  HA   . VAL   A  1  226 ? 24.234  -25.187 -28.689  1.00 55.76  ? 226  VAL   A HA   1 
ATOM   3455  H  HB   . VAL   A  1  226 ? 23.643  -25.157 -30.974  1.00 52.18  ? 226  VAL   A HB   1 
ATOM   3456  H  HG11 . VAL   A  1  226 ? 21.873  -26.654 -30.949  1.00 54.10  ? 226  VAL   A HG11 1 
ATOM   3457  H  HG12 . VAL   A  1  226 ? 22.885  -27.001 -29.775  1.00 54.10  ? 226  VAL   A HG12 1 
ATOM   3458  H  HG13 . VAL   A  1  226 ? 21.530  -26.236 -29.456  1.00 54.10  ? 226  VAL   A HG13 1 
ATOM   3459  H  HG21 . VAL   A  1  226 ? 21.581  -24.316 -31.684  1.00 47.71  ? 226  VAL   A HG21 1 
ATOM   3460  H  HG22 . VAL   A  1  226 ? 21.293  -23.800 -30.210  1.00 47.71  ? 226  VAL   A HG22 1 
ATOM   3461  H  HG23 . VAL   A  1  226 ? 22.475  -23.162 -31.058  1.00 47.71  ? 226  VAL   A HG23 1 
ATOM   3462  N  N    . ALA   A  1  227 ? 25.605  -23.379 -29.653  1.00 48.20  ? 227  ALA   A N    1 
ATOM   3463  C  CA   . ALA   A  1  227 ? 26.418  -22.300 -30.193  1.00 50.05  ? 227  ALA   A CA   1 
ATOM   3464  C  C    . ALA   A  1  227 ? 27.301  -22.894 -31.281  1.00 50.94  ? 227  ALA   A C    1 
ATOM   3465  O  O    . ALA   A  1  227 ? 27.391  -24.116 -31.433  1.00 49.94  ? 227  ALA   A O    1 
ATOM   3466  C  CB   . ALA   A  1  227 ? 27.264  -21.621 -29.110  1.00 49.94  ? 227  ALA   A CB   1 
ATOM   3467  H  H    . ALA   A  1  227 ? 26.028  -24.127 -29.616  1.00 57.88  ? 227  ALA   A H    1 
ATOM   3468  H  HA   . ALA   A  1  227 ? 25.850  -21.616 -30.580  1.00 60.10  ? 227  ALA   A HA   1 
ATOM   3469  H  HB1  . ALA   A  1  227 ? 27.791  -20.915 -29.516  1.00 59.97  ? 227  ALA   A HB1  1 
ATOM   3470  H  HB2  . ALA   A  1  227 ? 26.674  -21.247 -28.437  1.00 59.97  ? 227  ALA   A HB2  1 
ATOM   3471  H  HB3  . ALA   A  1  227 ? 27.849  -22.280 -28.706  1.00 59.97  ? 227  ALA   A HB3  1 
ATOM   3472  N  N    . VAL   A  1  228 ? 27.958  -22.027 -32.048  1.00 50.26  ? 228  VAL   A N    1 
ATOM   3473  C  CA   . VAL   A  1  228 ? 28.772  -22.471 -33.170  1.00 51.30  ? 228  VAL   A CA   1 
ATOM   3474  C  C    . VAL   A  1  228 ? 30.141  -21.812 -33.112  1.00 57.77  ? 228  VAL   A C    1 
ATOM   3475  O  O    . VAL   A  1  228 ? 30.290  -20.663 -32.683  1.00 59.12  ? 228  VAL   A O    1 
ATOM   3476  C  CB   . VAL   A  1  228 ? 28.092  -22.183 -34.528  1.00 49.71  ? 228  VAL   A CB   1 
ATOM   3477  C  CG1  . VAL   A  1  228 ? 26.877  -23.080 -34.708  1.00 50.96  ? 228  VAL   A CG1  1 
ATOM   3478  C  CG2  . VAL   A  1  228 ? 27.703  -20.719 -34.632  1.00 50.22  ? 228  VAL   A CG2  1 
ATOM   3479  H  H    . VAL   A  1  228 ? 27.945  -21.175 -31.936  1.00 60.34  ? 228  VAL   A H    1 
ATOM   3480  H  HA   . VAL   A  1  228 ? 28.906  -23.428 -33.086  1.00 61.60  ? 228  VAL   A HA   1 
ATOM   3481  H  HB   . VAL   A  1  228 ? 28.720  -22.374 -35.242  1.00 59.69  ? 228  VAL   A HB   1 
ATOM   3482  H  HG11 . VAL   A  1  228 ? 26.467  -22.888 -35.566  1.00 61.19  ? 228  VAL   A HG11 1 
ATOM   3483  H  HG12 . VAL   A  1  228 ? 27.161  -24.007 -34.677  1.00 61.19  ? 228  VAL   A HG12 1 
ATOM   3484  H  HG13 . VAL   A  1  228 ? 26.245  -22.904 -33.993  1.00 61.19  ? 228  VAL   A HG13 1 
ATOM   3485  H  HG21 . VAL   A  1  228 ? 27.298  -20.561 -35.499  1.00 60.30  ? 228  VAL   A HG21 1 
ATOM   3486  H  HG22 . VAL   A  1  228 ? 27.070  -20.509 -33.928  1.00 60.30  ? 228  VAL   A HG22 1 
ATOM   3487  H  HG23 . VAL   A  1  228 ? 28.499  -20.173 -34.534  1.00 60.30  ? 228  VAL   A HG23 1 
ATOM   3488  N  N    . GLY   A  1  229 ? 31.143  -22.561 -33.551  1.00 58.92  ? 229  GLY   A N    1 
ATOM   3489  C  CA   . GLY   A  1  229 ? 32.500  -22.060 -33.608  1.00 59.51  ? 229  GLY   A CA   1 
ATOM   3490  C  C    . GLY   A  1  229 ? 33.409  -23.149 -34.133  1.00 58.16  ? 229  GLY   A C    1 
ATOM   3491  O  O    . GLY   A  1  229 ? 33.104  -24.343 -34.041  1.00 55.12  ? 229  GLY   A O    1 
ATOM   3492  H  H    . GLY   A  1  229 ? 31.059  -23.372 -33.823  1.00 70.75  ? 229  GLY   A H    1 
ATOM   3493  H  HA2  . GLY   A  1  229 ? 32.548  -21.293 -34.199  1.00 71.45  ? 229  GLY   A HA2  1 
ATOM   3494  H  HA3  . GLY   A  1  229 ? 32.796  -21.797 -32.723  1.00 71.45  ? 229  GLY   A HA3  1 
ATOM   3495  N  N    . ASP   A  1  230 ? 34.530  -22.713 -34.700  1.00 60.00  ? 230  ASP   A N    1 
ATOM   3496  C  CA   . ASP   A  1  230 ? 35.509  -23.645 -35.242  1.00 60.46  ? 230  ASP   A CA   1 
ATOM   3497  C  C    . ASP   A  1  230 ? 36.419  -24.140 -34.124  1.00 59.15  ? 230  ASP   A C    1 
ATOM   3498  O  O    . ASP   A  1  230 ? 36.959  -23.340 -33.355  1.00 58.64  ? 230  ASP   A O    1 
ATOM   3499  C  CB   . ASP   A  1  230 ? 36.333  -22.976 -36.340  1.00 60.74  ? 230  ASP   A CB   1 
ATOM   3500  C  CG   . ASP   A  1  230 ? 37.144  -23.970 -37.150  1.00 60.43  ? 230  ASP   A CG   1 
ATOM   3501  O  OD1  . ASP   A  1  230 ? 36.804  -25.173 -37.134  1.00 58.09  ? 230  ASP   A OD1  1 
ATOM   3502  O  OD2  . ASP   A  1  230 ? 38.124  -23.548 -37.799  1.00 59.97  ? 230  ASP   A OD2  1 
ATOM   3503  H  H    . ASP   A  1  230 ? 34.745  -21.885 -34.783  1.00 72.03  ? 230  ASP   A H    1 
ATOM   3504  H  HA   . ASP   A  1  230 ? 35.053  -24.408 -35.632  1.00 72.58  ? 230  ASP   A HA   1 
ATOM   3505  H  HB2  . ASP   A  1  230 ? 35.735  -22.512 -36.947  1.00 72.92  ? 230  ASP   A HB2  1 
ATOM   3506  H  HB3  . ASP   A  1  230 ? 36.949  -22.345 -35.935  1.00 72.92  ? 230  ASP   A HB3  1 
ATOM   3507  N  N    . PHE   A  1  231 ? 36.587  -25.466 -34.034  1.00 58.74  ? 231  PHE   A N    1 
ATOM   3508  C  CA   . PHE   A  1  231 ? 37.409  -26.052 -32.982  1.00 59.58  ? 231  PHE   A CA   1 
ATOM   3509  C  C    . PHE   A  1  231 ? 38.348  -27.142 -33.489  1.00 60.30  ? 231  PHE   A C    1 
ATOM   3510  O  O    . PHE   A  1  231 ? 39.008  -27.797 -32.671  1.00 61.94  ? 231  PHE   A O    1 
ATOM   3511  C  CB   . PHE   A  1  231 ? 36.520  -26.607 -31.864  1.00 58.97  ? 231  PHE   A CB   1 
ATOM   3512  C  CG   . PHE   A  1  231 ? 35.734  -25.549 -31.147  1.00 55.54  ? 231  PHE   A CG   1 
ATOM   3513  C  CD1  . PHE   A  1  231 ? 36.304  -24.828 -30.110  1.00 55.64  ? 231  PHE   A CD1  1 
ATOM   3514  C  CD2  . PHE   A  1  231 ? 34.432  -25.266 -31.517  1.00 53.36  ? 231  PHE   A CD2  1 
ATOM   3515  C  CE1  . PHE   A  1  231 ? 35.585  -23.849 -29.453  1.00 54.91  ? 231  PHE   A CE1  1 
ATOM   3516  C  CE2  . PHE   A  1  231 ? 33.708  -24.288 -30.864  1.00 51.28  ? 231  PHE   A CE2  1 
ATOM   3517  C  CZ   . PHE   A  1  231 ? 34.285  -23.579 -29.830  1.00 52.68  ? 231  PHE   A CZ   1 
ATOM   3518  H  H    . PHE   A  1  231 ? 36.236  -26.039 -34.570  1.00 70.52  ? 231  PHE   A H    1 
ATOM   3519  H  HA   . PHE   A  1  231 ? 37.969  -25.356 -32.604  1.00 71.54  ? 231  PHE   A HA   1 
ATOM   3520  H  HB2  . PHE   A  1  231 ? 35.890  -27.236 -32.248  1.00 70.80  ? 231  PHE   A HB2  1 
ATOM   3521  H  HB3  . PHE   A  1  231 ? 37.080  -27.055 -31.211  1.00 70.80  ? 231  PHE   A HB3  1 
ATOM   3522  H  HD1  . PHE   A  1  231 ? 37.180  -25.005 -29.854  1.00 66.81  ? 231  PHE   A HD1  1 
ATOM   3523  H  HD2  . PHE   A  1  231 ? 34.039  -25.739 -32.215  1.00 64.07  ? 231  PHE   A HD2  1 
ATOM   3524  H  HE1  . PHE   A  1  231 ? 35.976  -23.372 -28.756  1.00 65.93  ? 231  PHE   A HE1  1 
ATOM   3525  H  HE2  . PHE   A  1  231 ? 32.832  -24.109 -31.120  1.00 61.57  ? 231  PHE   A HE2  1 
ATOM   3526  H  HZ   . PHE   A  1  231 ? 33.799  -22.920 -29.389  1.00 63.25  ? 231  PHE   A HZ   1 
ATOM   3527  N  N    . ASN   A  1  232 ? 38.430  -27.364 -34.803  1.00 61.86  ? 232  ASN   A N    1 
ATOM   3528  C  CA   . ASN   A  1  232 ? 39.515  -28.146 -35.383  1.00 63.85  ? 232  ASN   A CA   1 
ATOM   3529  C  C    . ASN   A  1  232 ? 40.210  -27.374 -36.502  1.00 68.66  ? 232  ASN   A C    1 
ATOM   3530  O  O    . ASN   A  1  232 ? 40.877  -27.979 -37.348  1.00 72.48  ? 232  ASN   A O    1 
ATOM   3531  C  CB   . ASN   A  1  232 ? 39.024  -29.506 -35.887  1.00 63.30  ? 232  ASN   A CB   1 
ATOM   3532  C  CG   . ASN   A  1  232 ? 37.807  -29.401 -36.776  1.00 66.40  ? 232  ASN   A CG   1 
ATOM   3533  O  OD1  . ASN   A  1  232 ? 37.366  -28.307 -37.122  1.00 68.15  ? 232  ASN   A OD1  1 
ATOM   3534  N  ND2  . ASN   A  1  232 ? 37.257  -30.549 -37.160  1.00 69.34  ? 232  ASN   A ND2  1 
ATOM   3535  H  H    . ASN   A  1  232 ? 37.864  -27.069 -35.380  1.00 74.27  ? 232  ASN   A H    1 
ATOM   3536  H  HA   . ASN   A  1  232 ? 40.171  -28.327 -34.692  1.00 76.66  ? 232  ASN   A HA   1 
ATOM   3537  H  HB2  . ASN   A  1  232 ? 39.732  -29.928 -36.399  1.00 76.00  ? 232  ASN   A HB2  1 
ATOM   3538  H  HB3  . ASN   A  1  232 ? 38.790  -30.059 -35.125  1.00 76.00  ? 232  ASN   A HB3  1 
ATOM   3539  H  HD21 . ASN   A  1  232 ? 36.563  -30.545 -37.666  1.00 83.24  ? 232  ASN   A HD21 1 
ATOM   3540  H  HD22 . ASN   A  1  232 ? 37.597  -31.296 -36.901  1.00 83.24  ? 232  ASN   A HD22 1 
ATOM   3541  N  N    . GLY   A  1  233 ? 40.052  -26.052 -36.524  1.00 70.55  ? 233  GLY   A N    1 
ATOM   3542  C  CA   . GLY   A  1  233 ? 40.865  -25.194 -37.364  1.00 70.95  ? 233  GLY   A CA   1 
ATOM   3543  C  C    . GLY   A  1  233 ? 40.714  -25.395 -38.853  1.00 73.56  ? 233  GLY   A C    1 
ATOM   3544  O  O    . GLY   A  1  233 ? 41.610  -25.009 -39.608  1.00 76.82  ? 233  GLY   A O    1 
ATOM   3545  H  H    . GLY   A  1  233 ? 39.472  -25.625 -36.054  1.00 84.70  ? 233  GLY   A H    1 
ATOM   3546  H  HA2  . GLY   A  1  233 ? 40.639  -24.271 -37.170  1.00 85.17  ? 233  GLY   A HA2  1 
ATOM   3547  H  HA3  . GLY   A  1  233 ? 41.798  -25.344 -37.143  1.00 85.17  ? 233  GLY   A HA3  1 
ATOM   3548  N  N    . ASP   A  1  234 ? 39.606  -25.978 -39.310  1.00 73.26  ? 234  ASP   A N    1 
ATOM   3549  C  CA   . ASP   A  1  234 ? 39.368  -26.155 -40.736  1.00 74.55  ? 234  ASP   A CA   1 
ATOM   3550  C  C    . ASP   A  1  234 ? 38.436  -25.090 -41.305  1.00 74.22  ? 234  ASP   A C    1 
ATOM   3551  O  O    . ASP   A  1  234 ? 37.896  -25.269 -42.402  1.00 72.06  ? 234  ASP   A O    1 
ATOM   3552  C  CB   . ASP   A  1  234 ? 38.808  -27.552 -41.017  1.00 73.33  ? 234  ASP   A CB   1 
ATOM   3553  C  CG   . ASP   A  1  234 ? 37.386  -27.733 -40.514  1.00 70.63  ? 234  ASP   A CG   1 
ATOM   3554  O  OD1  . ASP   A  1  234 ? 36.899  -26.884 -39.735  1.00 72.03  ? 234  ASP   A OD1  1 
ATOM   3555  O  OD2  . ASP   A  1  234 ? 36.750  -28.735 -40.904  1.00 71.43  ? 234  ASP   A OD2  1 
ATOM   3556  H  H    . ASP   A  1  234 ? 38.977  -26.280 -38.808  1.00 87.95  ? 234  ASP   A H    1 
ATOM   3557  H  HA   . ASP   A  1  234 ? 40.219  -26.081 -41.195  1.00 89.49  ? 234  ASP   A HA   1 
ATOM   3558  H  HB2  . ASP   A  1  234 ? 38.808  -27.704 -41.975  1.00 88.03  ? 234  ASP   A HB2  1 
ATOM   3559  H  HB3  . ASP   A  1  234 ? 39.368  -28.210 -40.576  1.00 88.03  ? 234  ASP   A HB3  1 
ATOM   3560  N  N    . GLY   A  1  235 ? 38.237  -23.988 -40.583  1.00 76.41  ? 235  GLY   A N    1 
ATOM   3561  C  CA   . GLY   A  1  235 ? 37.366  -22.925 -41.029  1.00 75.34  ? 235  GLY   A CA   1 
ATOM   3562  C  C    . GLY   A  1  235 ? 35.890  -23.245 -41.011  1.00 77.29  ? 235  GLY   A C    1 
ATOM   3563  O  O    . GLY   A  1  235 ? 35.078  -22.330 -41.174  1.00 81.50  ? 235  GLY   A O    1 
ATOM   3564  H  H    . GLY   A  1  235 ? 38.605  -23.839 -39.820  1.00 91.73  ? 235  GLY   A H    1 
ATOM   3565  H  HA2  . GLY   A  1  235 ? 37.505  -22.153 -40.459  1.00 90.44  ? 235  GLY   A HA2  1 
ATOM   3566  H  HA3  . GLY   A  1  235 ? 37.605  -22.693 -41.940  1.00 90.44  ? 235  GLY   A HA3  1 
ATOM   3567  N  N    . ILE   A  1  236 ? 35.507  -24.503 -40.823  1.00 72.63  ? 236  ILE   A N    1 
ATOM   3568  C  CA   . ILE   A  1  236 ? 34.102  -24.891 -40.788  1.00 70.63  ? 236  ILE   A CA   1 
ATOM   3569  C  C    . ILE   A  1  236 ? 33.612  -24.778 -39.352  1.00 68.40  ? 236  ILE   A C    1 
ATOM   3570  O  O    . ILE   A  1  236 ? 34.141  -25.441 -38.453  1.00 66.21  ? 236  ILE   A O    1 
ATOM   3571  C  CB   . ILE   A  1  236 ? 33.904  -26.316 -41.328  1.00 70.73  ? 236  ILE   A CB   1 
ATOM   3572  C  CG1  . ILE   A  1  236 ? 34.355  -26.395 -42.788  1.00 73.58  ? 236  ILE   A CG1  1 
ATOM   3573  C  CG2  . ILE   A  1  236 ? 32.444  -26.737 -41.197  1.00 66.43  ? 236  ILE   A CG2  1 
ATOM   3574  C  CD1  . ILE   A  1  236 ? 34.493  -27.807 -43.306  1.00 76.06  ? 236  ILE   A CD1  1 
ATOM   3575  H  H    . ILE   A  1  236 ? 36.051  -25.160 -40.711  1.00 87.19  ? 236  ILE   A H    1 
ATOM   3576  H  HA   . ILE   A  1  236 ? 33.587  -24.282 -41.340  1.00 84.79  ? 236  ILE   A HA   1 
ATOM   3577  H  HB   . ILE   A  1  236 ? 34.449  -26.922 -40.801  1.00 84.91  ? 236  ILE   A HB   1 
ATOM   3578  H  HG12 . ILE   A  1  236 ? 33.701  -25.940 -43.341  1.00 88.33  ? 236  ILE   A HG12 1 
ATOM   3579  H  HG13 . ILE   A  1  236 ? 35.219  -25.963 -42.872  1.00 88.33  ? 236  ILE   A HG13 1 
ATOM   3580  H  HG21 . ILE   A  1  236 ? 32.336  -27.624 -41.576  1.00 79.75  ? 236  ILE   A HG21 1 
ATOM   3581  H  HG22 . ILE   A  1  236 ? 32.201  -26.747 -40.258  1.00 79.75  ? 236  ILE   A HG22 1 
ATOM   3582  H  HG23 . ILE   A  1  236 ? 31.888  -26.103 -41.676  1.00 79.75  ? 236  ILE   A HG23 1 
ATOM   3583  H  HD11 . ILE   A  1  236 ? 34.800  -27.777 -44.226  1.00 91.31  ? 236  ILE   A HD11 1 
ATOM   3584  H  HD12 . ILE   A  1  236 ? 35.136  -28.283 -42.758  1.00 91.31  ? 236  ILE   A HD12 1 
ATOM   3585  H  HD13 . ILE   A  1  236 ? 33.630  -28.247 -43.260  1.00 91.31  ? 236  ILE   A HD13 1 
ATOM   3586  N  N    . ASP   A  1  237 ? 32.605  -23.936 -39.133  1.00 68.11  ? 237  ASP   A N    1 
ATOM   3587  C  CA   . ASP   A  1  237 ? 32.009  -23.823 -37.810  1.00 65.02  ? 237  ASP   A CA   1 
ATOM   3588  C  C    . ASP   A  1  237 ? 31.538  -25.188 -37.328  1.00 61.92  ? 237  ASP   A C    1 
ATOM   3589  O  O    . ASP   A  1  237 ? 30.868  -25.923 -38.059  1.00 61.74  ? 237  ASP   A O    1 
ATOM   3590  C  CB   . ASP   A  1  237 ? 30.839  -22.840 -37.836  1.00 66.03  ? 237  ASP   A CB   1 
ATOM   3591  C  CG   . ASP   A  1  237 ? 31.290  -21.392 -37.795  1.00 71.20  ? 237  ASP   A CG   1 
ATOM   3592  O  OD1  . ASP   A  1  237 ? 32.511  -21.147 -37.703  1.00 74.40  ? 237  ASP   A OD1  1 
ATOM   3593  O  OD2  . ASP   A  1  237 ? 30.420  -20.497 -37.851  1.00 71.13  ? 237  ASP   A OD2  1 
ATOM   3594  H  H    . ASP   A  1  237 ? 32.254  -23.426 -39.729  1.00 81.77  ? 237  ASP   A H    1 
ATOM   3595  H  HA   . ASP   A  1  237 ? 32.672  -23.485 -37.188  1.00 78.06  ? 237  ASP   A HA   1 
ATOM   3596  H  HB2  . ASP   A  1  237 ? 30.332  -22.973 -38.652  1.00 79.27  ? 237  ASP   A HB2  1 
ATOM   3597  H  HB3  . ASP   A  1  237 ? 30.274  -23.000 -37.064  1.00 79.27  ? 237  ASP   A HB3  1 
ATOM   3598  N  N    . ASP   A  1  238 ? 31.898  -25.526 -36.096  1.00 60.17  ? 238  ASP   A N    1 
ATOM   3599  C  CA   . ASP   A  1  238 ? 31.487  -26.766 -35.457  1.00 56.53  ? 238  ASP   A CA   1 
ATOM   3600  C  C    . ASP   A  1  238 ? 30.350  -26.488 -34.477  1.00 54.61  ? 238  ASP   A C    1 
ATOM   3601  O  O    . ASP   A  1  238 ? 30.053  -25.339 -34.140  1.00 56.81  ? 238  ASP   A O    1 
ATOM   3602  C  CB   . ASP   A  1  238 ? 32.684  -27.415 -34.758  1.00 53.86  ? 238  ASP   A CB   1 
ATOM   3603  C  CG   . ASP   A  1  238 ? 33.852  -27.652 -35.705  1.00 56.59  ? 238  ASP   A CG   1 
ATOM   3604  O  OD1  . ASP   A  1  238 ? 33.633  -28.237 -36.787  1.00 57.10  ? 238  ASP   A OD1  1 
ATOM   3605  O  OD2  . ASP   A  1  238 ? 34.986  -27.240 -35.381  1.00 56.91  ? 238  ASP   A OD2  1 
ATOM   3606  H  H    . ASP   A  1  238 ? 32.397  -25.036 -35.595  1.00 72.24  ? 238  ASP   A H    1 
ATOM   3607  H  HA   . ASP   A  1  238 ? 31.161  -27.394 -36.120  1.00 67.87  ? 238  ASP   A HA   1 
ATOM   3608  H  HB2  . ASP   A  1  238 ? 32.989  -26.833 -34.044  1.00 64.67  ? 238  ASP   A HB2  1 
ATOM   3609  H  HB3  . ASP   A  1  238 ? 32.413  -28.272 -34.394  1.00 64.67  ? 238  ASP   A HB3  1 
ATOM   3610  N  N    . PHE   A  1  239 ? 29.706  -27.560 -34.019  1.00 49.94  ? 239  PHE   A N    1 
ATOM   3611  C  CA   . PHE   A  1  239 ? 28.478  -27.458 -33.239  1.00 50.51  ? 239  PHE   A CA   1 
ATOM   3612  C  C    . PHE   A  1  239 ? 28.769  -27.701 -31.763  1.00 49.49  ? 239  PHE   A C    1 
ATOM   3613  O  O    . PHE   A  1  239 ? 29.292  -28.758 -31.394  1.00 51.48  ? 239  PHE   A O    1 
ATOM   3614  C  CB   . PHE   A  1  239 ? 27.434  -28.459 -33.735  1.00 49.54  ? 239  PHE   A CB   1 
ATOM   3615  C  CG   . PHE   A  1  239 ? 27.227  -28.438 -35.221  1.00 49.92  ? 239  PHE   A CG   1 
ATOM   3616  C  CD1  . PHE   A  1  239 ? 27.295  -27.252 -35.934  1.00 53.03  ? 239  PHE   A CD1  1 
ATOM   3617  C  CD2  . PHE   A  1  239 ? 26.965  -29.611 -35.906  1.00 51.70  ? 239  PHE   A CD2  1 
ATOM   3618  C  CE1  . PHE   A  1  239 ? 27.102  -27.239 -37.304  1.00 56.51  ? 239  PHE   A CE1  1 
ATOM   3619  C  CE2  . PHE   A  1  239 ? 26.772  -29.606 -37.272  1.00 54.79  ? 239  PHE   A CE2  1 
ATOM   3620  C  CZ   . PHE   A  1  239 ? 26.841  -28.419 -37.973  1.00 57.25  ? 239  PHE   A CZ   1 
ATOM   3621  H  H    . PHE   A  1  239 ? 29.966  -28.369 -34.151  1.00 59.96  ? 239  PHE   A H    1 
ATOM   3622  H  HA   . PHE   A  1  239 ? 28.129  -26.558 -33.333  1.00 60.65  ? 239  PHE   A HA   1 
ATOM   3623  H  HB2  . PHE   A  1  239 ? 27.720  -29.353 -33.490  1.00 59.49  ? 239  PHE   A HB2  1 
ATOM   3624  H  HB3  . PHE   A  1  239 ? 26.584  -28.255 -33.315  1.00 59.49  ? 239  PHE   A HB3  1 
ATOM   3625  H  HD1  . PHE   A  1  239 ? 27.471  -26.455 -35.487  1.00 63.67  ? 239  PHE   A HD1  1 
ATOM   3626  H  HD2  . PHE   A  1  239 ? 26.918  -30.414 -35.439  1.00 62.08  ? 239  PHE   A HD2  1 
ATOM   3627  H  HE1  . PHE   A  1  239 ? 27.149  -26.438 -37.774  1.00 67.85  ? 239  PHE   A HE1  1 
ATOM   3628  H  HE2  . PHE   A  1  239 ? 26.595  -30.402 -37.721  1.00 65.78  ? 239  PHE   A HE2  1 
ATOM   3629  H  HZ   . PHE   A  1  239 ? 26.711  -28.414 -38.894  1.00 68.73  ? 239  PHE   A HZ   1 
ATOM   3630  N  N    . VAL   A  1  240 ? 28.415  -26.729 -30.926  1.00 48.94  ? 240  VAL   A N    1 
ATOM   3631  C  CA   . VAL   A  1  240 ? 28.489  -26.845 -29.474  1.00 47.02  ? 240  VAL   A CA   1 
ATOM   3632  C  C    . VAL   A  1  240 ? 27.065  -26.931 -28.945  1.00 45.41  ? 240  VAL   A C    1 
ATOM   3633  O  O    . VAL   A  1  240 ? 26.176  -26.219 -29.427  1.00 48.68  ? 240  VAL   A O    1 
ATOM   3634  C  CB   . VAL   A  1  240 ? 29.232  -25.647 -28.850  1.00 47.45  ? 240  VAL   A CB   1 
ATOM   3635  C  CG1  . VAL   A  1  240 ? 29.394  -25.837 -27.346  1.00 45.07  ? 240  VAL   A CG1  1 
ATOM   3636  C  CG2  . VAL   A  1  240 ? 30.581  -25.445 -29.526  1.00 51.49  ? 240  VAL   A CG2  1 
ATOM   3637  H  H    . VAL   A  1  240 ? 28.118  -25.965 -31.186  1.00 58.77  ? 240  VAL   A H    1 
ATOM   3638  H  HA   . VAL   A  1  240 ? 28.967  -27.654 -29.233  1.00 56.46  ? 240  VAL   A HA   1 
ATOM   3639  H  HB   . VAL   A  1  240 ? 28.706  -24.845 -28.989  1.00 56.97  ? 240  VAL   A HB   1 
ATOM   3640  H  HG11 . VAL   A  1  240 ? 29.871  -25.075 -26.981  1.00 54.13  ? 240  VAL   A HG11 1 
ATOM   3641  H  HG12 . VAL   A  1  240 ? 28.516  -25.904 -26.940  1.00 54.13  ? 240  VAL   A HG12 1 
ATOM   3642  H  HG13 . VAL   A  1  240 ? 29.897  -26.650 -27.183  1.00 54.13  ? 240  VAL   A HG13 1 
ATOM   3643  H  HG21 . VAL   A  1  240 ? 31.034  -24.695 -29.109  1.00 61.82  ? 240  VAL   A HG21 1 
ATOM   3644  H  HG22 . VAL   A  1  240 ? 31.111  -26.251 -29.421  1.00 61.82  ? 240  VAL   A HG22 1 
ATOM   3645  H  HG23 . VAL   A  1  240 ? 30.438  -25.263 -30.468  1.00 61.82  ? 240  VAL   A HG23 1 
ATOM   3646  N  N    . SER   A  1  241 ? 26.842  -27.797 -27.957  1.00 37.75  ? 241  SER   A N    1 
ATOM   3647  C  CA   . SER   A  1  241 ? 25.496  -27.978 -27.433  1.00 43.19  ? 241  SER   A CA   1 
ATOM   3648  C  C    . SER   A  1  241 ? 25.535  -28.395 -25.971  1.00 49.57  ? 241  SER   A C    1 
ATOM   3649  O  O    . SER   A  1  241 ? 26.379  -29.199 -25.565  1.00 47.27  ? 241  SER   A O    1 
ATOM   3650  C  CB   . SER   A  1  241 ? 24.719  -29.019 -28.247  1.00 45.86  ? 241  SER   A CB   1 
ATOM   3651  O  OG   . SER   A  1  241 ? 23.390  -29.140 -27.771  1.00 47.32  ? 241  SER   A OG   1 
ATOM   3652  H  H    . SER   A  1  241 ? 27.445  -28.283 -27.583  1.00 45.33  ? 241  SER   A H    1 
ATOM   3653  H  HA   . SER   A  1  241 ? 25.035  -27.125 -27.477  1.00 51.87  ? 241  SER   A HA   1 
ATOM   3654  H  HB2  . SER   A  1  241 ? 24.698  -28.743 -29.177  1.00 55.07  ? 241  SER   A HB2  1 
ATOM   3655  H  HB3  . SER   A  1  241 ? 25.163  -29.878 -28.167  1.00 55.07  ? 241  SER   A HB3  1 
ATOM   3656  H  HG   . SER   A  1  241 ? 23.107  -28.391 -27.517  1.00 56.83  ? 241  SER   A HG   1 
ATOM   3657  N  N    . GLY   A  1  242 ? 24.601  -27.850 -25.194  1.00 51.55  ? 242  GLY   A N    1 
ATOM   3658  C  CA   . GLY   A  1  242 ? 24.484  -28.188 -23.787  1.00 50.93  ? 242  GLY   A CA   1 
ATOM   3659  C  C    . GLY   A  1  242 ? 23.628  -29.427 -23.576  1.00 49.48  ? 242  GLY   A C    1 
ATOM   3660  O  O    . GLY   A  1  242 ? 22.627  -29.635 -24.258  1.00 47.45  ? 242  GLY   A O    1 
ATOM   3661  H  H    . GLY   A  1  242 ? 24.019  -27.277 -25.465  1.00 61.90  ? 242  GLY   A H    1 
ATOM   3662  H  HA2  . GLY   A  1  242 ? 25.365  -28.355 -23.419  1.00 61.16  ? 242  GLY   A HA2  1 
ATOM   3663  H  HA3  . GLY   A  1  242 ? 24.078  -27.448 -23.309  1.00 61.16  ? 242  GLY   A HA3  1 
ATOM   3664  N  N    . VAL   A  1  243 ? 24.038  -30.242 -22.610  1.00 45.54  ? 243  VAL   A N    1 
ATOM   3665  C  CA   . VAL   A  1  243 ? 23.389  -31.516 -22.309  1.00 43.89  ? 243  VAL   A CA   1 
ATOM   3666  C  C    . VAL   A  1  243 ? 23.217  -31.584 -20.795  1.00 43.96  ? 243  VAL   A C    1 
ATOM   3667  O  O    . VAL   A  1  243 ? 23.921  -32.351 -20.124  1.00 44.84  ? 243  VAL   A O    1 
ATOM   3668  C  CB   . VAL   A  1  243 ? 24.212  -32.696 -22.846  1.00 45.47  ? 243  VAL   A CB   1 
ATOM   3669  C  CG1  . VAL   A  1  243 ? 23.374  -33.958 -22.874  1.00 46.29  ? 243  VAL   A CG1  1 
ATOM   3670  C  CG2  . VAL   A  1  243 ? 24.760  -32.379 -24.236  1.00 51.26  ? 243  VAL   A CG2  1 
ATOM   3671  H  H    . VAL   A  1  243 ? 24.710  -30.076 -22.099  1.00 54.68  ? 243  VAL   A H    1 
ATOM   3672  H  HA   . VAL   A  1  243 ? 22.515  -31.560 -22.729  1.00 52.71  ? 243  VAL   A HA   1 
ATOM   3673  H  HB   . VAL   A  1  243 ? 24.965  -32.848 -22.254  1.00 54.60  ? 243  VAL   A HB   1 
ATOM   3674  H  HG11 . VAL   A  1  243 ? 23.922  -34.694 -23.191  1.00 55.59  ? 243  VAL   A HG11 1 
ATOM   3675  H  HG12 . VAL   A  1  243 ? 23.056  -34.146 -21.977  1.00 55.59  ? 243  VAL   A HG12 1 
ATOM   3676  H  HG13 . VAL   A  1  243 ? 22.622  -33.825 -23.471  1.00 55.59  ? 243  VAL   A HG13 1 
ATOM   3677  H  HG21 . VAL   A  1  243 ? 25.244  -33.152 -24.568  1.00 61.55  ? 243  VAL   A HG21 1 
ATOM   3678  H  HG22 . VAL   A  1  243 ? 24.019  -32.174 -24.827  1.00 61.55  ? 243  VAL   A HG22 1 
ATOM   3679  H  HG23 . VAL   A  1  243 ? 25.356  -31.617 -24.174  1.00 61.55  ? 243  VAL   A HG23 1 
ATOM   3680  N  N    . PRO   A  1  244 ? 22.286  -30.815 -20.221  1.00 41.62  ? 244  PRO   A N    1 
ATOM   3681  C  CA   . PRO   A  1  244 ? 22.345  -30.527 -18.777  1.00 42.77  ? 244  PRO   A CA   1 
ATOM   3682  C  C    . PRO   A  1  244 ? 21.949  -31.674 -17.858  1.00 45.27  ? 244  PRO   A C    1 
ATOM   3683  O  O    . PRO   A  1  244 ? 22.234  -31.585 -16.655  1.00 50.35  ? 244  PRO   A O    1 
ATOM   3684  C  CB   . PRO   A  1  244 ? 21.376  -29.348 -18.622  1.00 45.79  ? 244  PRO   A CB   1 
ATOM   3685  C  CG   . PRO   A  1  244 ? 20.430  -29.477 -19.769  1.00 42.96  ? 244  PRO   A CG   1 
ATOM   3686  C  CD   . PRO   A  1  244 ? 21.231  -30.044 -20.902  1.00 41.40  ? 244  PRO   A CD   1 
ATOM   3687  H  HA   . PRO   A  1  244 ? 23.247  -30.254 -18.549  1.00 51.36  ? 244  PRO   A HA   1 
ATOM   3688  H  HB2  . PRO   A  1  244 ? 20.907  -29.414 -17.775  1.00 54.98  ? 244  PRO   A HB2  1 
ATOM   3689  H  HB3  . PRO   A  1  244 ? 21.864  -28.511 -18.666  1.00 54.98  ? 244  PRO   A HB3  1 
ATOM   3690  H  HG2  . PRO   A  1  244 ? 19.704  -30.074 -19.528  1.00 51.59  ? 244  PRO   A HG2  1 
ATOM   3691  H  HG3  . PRO   A  1  244 ? 20.077  -28.604 -20.001  1.00 51.59  ? 244  PRO   A HG3  1 
ATOM   3692  H  HD2  . PRO   A  1  244 ? 20.684  -30.622 -21.455  1.00 49.72  ? 244  PRO   A HD2  1 
ATOM   3693  H  HD3  . PRO   A  1  244 ? 21.616  -29.335 -21.441  1.00 49.72  ? 244  PRO   A HD3  1 
ATOM   3694  N  N    . ARG   A  1  245 ? 21.308  -32.730 -18.350  1.00 46.31  ? 245  ARG   A N    1 
ATOM   3695  C  CA   . ARG   A  1  245 ? 20.948  -33.863 -17.507  1.00 46.20  ? 245  ARG   A CA   1 
ATOM   3696  C  C    . ARG   A  1  245 ? 21.891  -35.048 -17.672  1.00 44.29  ? 245  ARG   A C    1 
ATOM   3697  O  O    . ARG   A  1  245 ? 21.736  -36.049 -16.965  1.00 49.69  ? 245  ARG   A O    1 
ATOM   3698  C  CB   . ARG   A  1  245 ? 19.508  -34.305 -17.795  1.00 45.87  ? 245  ARG   A CB   1 
ATOM   3699  C  CG   . ARG   A  1  245 ? 18.450  -33.398 -17.177  1.00 45.63  ? 245  ARG   A CG   1 
ATOM   3700  C  CD   . ARG   A  1  245 ? 17.064  -34.028 -17.228  1.00 44.49  ? 245  ARG   A CD   1 
ATOM   3701  N  NE   . ARG   A  1  245 ? 17.005  -35.290 -16.492  1.00 42.34  ? 245  ARG   A NE   1 
ATOM   3702  C  CZ   . ARG   A  1  245 ? 16.743  -35.394 -15.192  1.00 48.04  ? 245  ARG   A CZ   1 
ATOM   3703  N  NH1  . ARG   A  1  245 ? 16.512  -34.311 -14.464  1.00 53.14  ? 245  ARG   A NH1  1 
ATOM   3704  N  NH2  . ARG   A  1  245 ? 16.714  -36.588 -14.616  1.00 50.26  ? 245  ARG   A NH2  1 
ATOM   3705  H  H    . ARG   A  1  245 ? 21.069  -32.812 -19.173  1.00 55.61  ? 245  ARG   A H    1 
ATOM   3706  H  HA   . ARG   A  1  245 ? 20.990  -33.580 -16.580  1.00 55.48  ? 245  ARG   A HA   1 
ATOM   3707  H  HB2  . ARG   A  1  245 ? 19.370  -34.309 -18.755  1.00 55.08  ? 245  ARG   A HB2  1 
ATOM   3708  H  HB3  . ARG   A  1  245 ? 19.378  -35.197 -17.437  1.00 55.08  ? 245  ARG   A HB3  1 
ATOM   3709  H  HG2  . ARG   A  1  245 ? 18.674  -33.231 -16.248  1.00 54.79  ? 245  ARG   A HG2  1 
ATOM   3710  H  HG3  . ARG   A  1  245 ? 18.421  -32.561 -17.666  1.00 54.79  ? 245  ARG   A HG3  1 
ATOM   3711  H  HD2  . ARG   A  1  245 ? 16.422  -33.418 -16.834  1.00 53.43  ? 245  ARG   A HD2  1 
ATOM   3712  H  HD3  . ARG   A  1  245 ? 16.829  -34.206 -18.152  1.00 53.43  ? 245  ARG   A HD3  1 
ATOM   3713  H  HE   . ARG   A  1  245 ? 17.149  -36.016 -16.931  1.00 50.85  ? 245  ARG   A HE   1 
ATOM   3714  H  HH11 . ARG   A  1  245 ? 16.530  -33.534 -14.831  1.00 63.81  ? 245  ARG   A HH11 1 
ATOM   3715  H  HH12 . ARG   A  1  245 ? 16.343  -34.386 -13.624  1.00 63.81  ? 245  ARG   A HH12 1 
ATOM   3716  H  HH21 . ARG   A  1  245 ? 16.864  -37.295 -15.083  1.00 60.35  ? 245  ARG   A HH21 1 
ATOM   3717  H  HH22 . ARG   A  1  245 ? 16.545  -36.656 -13.776  1.00 60.35  ? 245  ARG   A HH22 1 
ATOM   3718  N  N    . ALA   A  1  246 ? 22.867  -34.957 -18.572  1.00 42.08  ? 246  ALA   A N    1 
ATOM   3719  C  CA   . ALA   A  1  246 ? 23.791  -36.055 -18.804  1.00 44.06  ? 246  ALA   A CA   1 
ATOM   3720  C  C    . ALA   A  1  246 ? 24.701  -36.264 -17.594  1.00 48.89  ? 246  ALA   A C    1 
ATOM   3721  O  O    . ALA   A  1  246 ? 24.765  -35.445 -16.672  1.00 52.20  ? 246  ALA   A O    1 
ATOM   3722  C  CB   . ALA   A  1  246 ? 24.632  -35.788 -20.052  1.00 42.33  ? 246  ALA   A CB   1 
ATOM   3723  H  H    . ALA   A  1  246 ? 23.013  -34.265 -19.062  1.00 50.53  ? 246  ALA   A H    1 
ATOM   3724  H  HA   . ALA   A  1  246 ? 23.283  -36.869 -18.944  1.00 52.91  ? 246  ALA   A HA   1 
ATOM   3725  H  HB1  . ALA   A  1  246 ? 25.246  -36.527 -20.182  1.00 50.84  ? 246  ALA   A HB1  1 
ATOM   3726  H  HB2  . ALA   A  1  246 ? 24.043  -35.708 -20.818  1.00 50.84  ? 246  ALA   A HB2  1 
ATOM   3727  H  HB3  . ALA   A  1  246 ? 25.128  -34.964 -19.928  1.00 50.84  ? 246  ALA   A HB3  1 
ATOM   3728  N  N    . ALA   A  1  247 ? 25.419  -37.387 -17.613  1.00 55.11  ? 247  ALA   A N    1 
ATOM   3729  C  CA   . ALA   A  1  247 ? 26.337  -37.752 -16.534  1.00 57.27  ? 247  ALA   A CA   1 
ATOM   3730  C  C    . ALA   A  1  247 ? 25.622  -37.754 -15.187  1.00 58.16  ? 247  ALA   A C    1 
ATOM   3731  O  O    . ALA   A  1  247 ? 26.131  -37.246 -14.185  1.00 58.50  ? 247  ALA   A O    1 
ATOM   3732  C  CB   . ALA   A  1  247 ? 27.548  -36.818 -16.506  1.00 59.29  ? 247  ALA   A CB   1 
ATOM   3733  H  H    . ALA   A  1  247 ? 25.391  -37.964 -18.250  1.00 66.17  ? 247  ALA   A H    1 
ATOM   3734  H  HA   . ALA   A  1  247 ? 26.659  -38.652 -16.698  1.00 68.76  ? 247  ALA   A HA   1 
ATOM   3735  H  HB1  . ALA   A  1  247 ? 28.149  -37.100 -15.799  1.00 71.19  ? 247  ALA   A HB1  1 
ATOM   3736  H  HB2  . ALA   A  1  247 ? 28.001  -36.862 -17.363  1.00 71.19  ? 247  ALA   A HB2  1 
ATOM   3737  H  HB3  . ALA   A  1  247 ? 27.244  -35.912 -16.339  1.00 71.19  ? 247  ALA   A HB3  1 
ATOM   3738  N  N    . ARG   A  1  248 ? 24.426  -38.339 -15.167  1.00 58.97  ? 248  ARG   A N    1 
ATOM   3739  C  CA   . ARG   A  1  248 ? 23.591  -38.395 -13.971  1.00 59.35  ? 248  ARG   A CA   1 
ATOM   3740  C  C    . ARG   A  1  248 ? 23.489  -37.019 -13.315  1.00 57.44  ? 248  ARG   A C    1 
ATOM   3741  O  O    . ARG   A  1  248 ? 23.722  -36.845 -12.117  1.00 58.28  ? 248  ARG   A O    1 
ATOM   3742  C  CB   . ARG   A  1  248 ? 24.108  -39.449 -12.990  1.00 64.49  ? 248  ARG   A CB   1 
ATOM   3743  C  CG   . ARG   A  1  248 ? 24.077  -40.883 -13.537  1.00 75.20  ? 248  ARG   A CG   1 
ATOM   3744  C  CD   . ARG   A  1  248 ? 22.682  -41.315 -14.013  1.00 84.15  ? 248  ARG   A CD   1 
ATOM   3745  N  NE   . ARG   A  1  248 ? 21.889  -41.960 -12.969  1.00 89.13  ? 248  ARG   A NE   1 
ATOM   3746  C  CZ   . ARG   A  1  248 ? 20.575  -42.157 -13.043  1.00 88.56  ? 248  ARG   A CZ   1 
ATOM   3747  N  NH1  . ARG   A  1  248 ? 19.894  -41.749 -14.107  1.00 87.40  ? 248  ARG   A NH1  1 
ATOM   3748  N  NH2  . ARG   A  1  248 ? 19.937  -42.755 -12.048  1.00 89.14  ? 248  ARG   A NH2  1 
ATOM   3749  H  H    . ARG   A  1  248 ? 24.069  -38.719 -15.851  1.00 70.80  ? 248  ARG   A H    1 
ATOM   3750  H  HA   . ARG   A  1  248 ? 22.694  -38.657 -14.231  1.00 71.25  ? 248  ARG   A HA   1 
ATOM   3751  H  HB2  . ARG   A  1  248 ? 25.028  -39.239 -12.765  1.00 77.42  ? 248  ARG   A HB2  1 
ATOM   3752  H  HB3  . ARG   A  1  248 ? 23.558  -39.426 -12.191  1.00 77.42  ? 248  ARG   A HB3  1 
ATOM   3753  H  HG2  . ARG   A  1  248 ? 24.683  -40.945 -14.292  1.00 90.27  ? 248  ARG   A HG2  1 
ATOM   3754  H  HG3  . ARG   A  1  248 ? 24.356  -41.494 -12.837  1.00 90.27  ? 248  ARG   A HG3  1 
ATOM   3755  H  HD2  . ARG   A  1  248 ? 22.196  -40.531 -14.314  1.00 101.02 ? 248  ARG   A HD2  1 
ATOM   3756  H  HD3  . ARG   A  1  248 ? 22.780  -41.945 -14.744  1.00 101.02 ? 248  ARG   A HD3  1 
ATOM   3757  H  HE   . ARG   A  1  248 ? 22.298  -42.229 -12.262  1.00 107.00 ? 248  ARG   A HE   1 
ATOM   3758  H  HH11 . ARG   A  1  248 ? 20.301  -41.355 -14.754  1.00 104.91 ? 248  ARG   A HH11 1 
ATOM   3759  H  HH12 . ARG   A  1  248 ? 19.045  -41.879 -14.150  1.00 104.91 ? 248  ARG   A HH12 1 
ATOM   3760  H  HH21 . ARG   A  1  248 ? 20.372  -43.016 -11.354  1.00 107.00 ? 248  ARG   A HH21 1 
ATOM   3761  H  HH22 . ARG   A  1  248 ? 19.088  -42.882 -12.096  1.00 107.00 ? 248  ARG   A HH22 1 
ATOM   3762  N  N    . THR   A  1  249 ? 23.127  -36.033 -14.133  1.00 53.66  ? 249  THR   A N    1 
ATOM   3763  C  CA   . THR   A  1  249 ? 22.786  -34.668 -13.744  1.00 55.39  ? 249  THR   A CA   1 
ATOM   3764  C  C    . THR   A  1  249 ? 24.002  -33.826 -13.384  1.00 52.64  ? 249  THR   A C    1 
ATOM   3765  O  O    . THR   A  1  249 ? 23.829  -32.698 -12.898  1.00 53.16  ? 249  THR   A O    1 
ATOM   3766  C  CB   . THR   A  1  249 ? 21.803  -34.620 -12.567  1.00 59.91  ? 249  THR   A CB   1 
ATOM   3767  O  OG1  . THR   A  1  249 ? 22.462  -35.032 -11.362  1.00 61.11  ? 249  THR   A OG1  1 
ATOM   3768  C  CG2  . THR   A  1  249 ? 20.606  -35.522 -12.836  1.00 64.93  ? 249  THR   A CG2  1 
ATOM   3769  H  H    . THR   A  1  249 ? 23.069  -36.142 -14.984  1.00 64.43  ? 249  THR   A H    1 
ATOM   3770  H  HA   . THR   A  1  249 ? 22.366  -34.254 -14.514  1.00 66.51  ? 249  THR   A HA   1 
ATOM   3771  H  HB   . THR   A  1  249 ? 21.479  -33.712 -12.453  1.00 71.93  ? 249  THR   A HB   1 
ATOM   3772  H  HG1  . THR   A  1  249 ? 22.570  -35.865 -11.365  1.00 73.37  ? 249  THR   A HG1  1 
ATOM   3773  H  HG21 . THR   A  1  249 ? 19.967  -35.452 -12.109  1.00 77.95  ? 249  THR   A HG21 1 
ATOM   3774  H  HG22 . THR   A  1  249 ? 20.172  -35.261 -13.663  1.00 77.95  ? 249  THR   A HG22 1 
ATOM   3775  H  HG23 . THR   A  1  249 ? 20.896  -36.445 -12.911  1.00 77.95  ? 249  THR   A HG23 1 
ATOM   3776  N  N    . LEU   A  1  250 ? 25.222  -34.321 -13.595  1.00 52.99  ? 250  LEU   A N    1 
ATOM   3777  C  CA   . LEU   A  1  250 ? 26.373  -33.430 -13.531  1.00 51.55  ? 250  LEU   A CA   1 
ATOM   3778  C  C    . LEU   A  1  250 ? 26.341  -32.424 -14.670  1.00 50.65  ? 250  LEU   A C    1 
ATOM   3779  O  O    . LEU   A  1  250 ? 26.861  -31.310 -14.532  1.00 52.30  ? 250  LEU   A O    1 
ATOM   3780  C  CB   . LEU   A  1  250 ? 27.676  -34.224 -13.581  1.00 49.87  ? 250  LEU   A CB   1 
ATOM   3781  C  CG   . LEU   A  1  250 ? 28.123  -34.898 -12.286  1.00 49.30  ? 250  LEU   A CG   1 
ATOM   3782  C  CD1  . LEU   A  1  250 ? 29.321  -35.785 -12.561  1.00 44.94  ? 250  LEU   A CD1  1 
ATOM   3783  C  CD2  . LEU   A  1  250 ? 28.456  -33.862 -11.225  1.00 52.99  ? 250  LEU   A CD2  1 
ATOM   3784  H  H    . LEU   A  1  250 ? 25.402  -35.143 -13.771  1.00 63.62  ? 250  LEU   A H    1 
ATOM   3785  H  HA   . LEU   A  1  250 ? 26.350  -32.954 -12.685  1.00 61.90  ? 250  LEU   A HA   1 
ATOM   3786  H  HB2  . LEU   A  1  250 ? 27.574  -34.924 -14.244  1.00 59.89  ? 250  LEU   A HB2  1 
ATOM   3787  H  HB3  . LEU   A  1  250 ? 28.386  -33.617 -13.844  1.00 59.89  ? 250  LEU   A HB3  1 
ATOM   3788  H  HG   . LEU   A  1  250 ? 27.402  -35.448 -11.942  1.00 59.19  ? 250  LEU   A HG   1 
ATOM   3789  H  HD11 . LEU   A  1  250 ? 29.607  -36.197 -11.730  1.00 53.96  ? 250  LEU   A HD11 1 
ATOM   3790  H  HD12 . LEU   A  1  250 ? 29.067  -36.471 -13.199  1.00 53.96  ? 250  LEU   A HD12 1 
ATOM   3791  H  HD13 . LEU   A  1  250 ? 30.039  -35.244 -12.926  1.00 53.96  ? 250  LEU   A HD13 1 
ATOM   3792  H  HD21 . LEU   A  1  250 ? 28.755  -34.316 -10.422  1.00 63.62  ? 250  LEU   A HD21 1 
ATOM   3793  H  HD22 . LEU   A  1  250 ? 29.159  -33.282 -11.558  1.00 63.62  ? 250  LEU   A HD22 1 
ATOM   3794  H  HD23 . LEU   A  1  250 ? 27.660  -33.340 -11.033  1.00 63.62  ? 250  LEU   A HD23 1 
ATOM   3795  N  N    . GLY   A  1  251 ? 25.730  -32.792 -15.784  1.00 47.66  ? 251  GLY   A N    1 
ATOM   3796  C  CA   . GLY   A  1  251 ? 25.718  -31.949 -16.965  1.00 48.14  ? 251  GLY   A CA   1 
ATOM   3797  C  C    . GLY   A  1  251 ? 26.926  -32.185 -17.846  1.00 46.70  ? 251  GLY   A C    1 
ATOM   3798  O  O    . GLY   A  1  251 ? 28.019  -32.521 -17.387  1.00 46.08  ? 251  GLY   A O    1 
ATOM   3799  H  H    . GLY   A  1  251 ? 25.309  -33.536 -15.884  1.00 57.23  ? 251  GLY   A H    1 
ATOM   3800  H  HA2  . GLY   A  1  251 ? 24.919  -32.134 -17.484  1.00 57.80  ? 251  GLY   A HA2  1 
ATOM   3801  H  HA3  . GLY   A  1  251 ? 25.711  -31.018 -16.695  1.00 57.80  ? 251  GLY   A HA3  1 
ATOM   3802  N  N    . MET   A  1  252 ? 26.716  -32.016 -19.148  1.00 40.80  ? 252  MET   A N    1 
ATOM   3803  C  CA   . MET   A  1  252 ? 27.793  -32.120 -20.117  1.00 42.36  ? 252  MET   A CA   1 
ATOM   3804  C  C    . MET   A  1  252 ? 27.544  -31.121 -21.233  1.00 40.25  ? 252  MET   A C    1 
ATOM   3805  O  O    . MET   A  1  252 ? 26.434  -30.608 -21.402  1.00 38.12  ? 252  MET   A O    1 
ATOM   3806  C  CB   . MET   A  1  252 ? 27.910  -33.535 -20.700  1.00 44.65  ? 252  MET   A CB   1 
ATOM   3807  C  CG   . MET   A  1  252 ? 28.395  -34.585 -19.714  1.00 49.01  ? 252  MET   A CG   1 
ATOM   3808  S  SD   . MET   A  1  252 ? 28.702  -36.188 -20.486  1.00 51.03  ? 252  MET   A SD   1 
ATOM   3809  C  CE   . MET   A  1  252 ? 30.209  -35.856 -21.399  1.00 52.06  ? 252  MET   A CE   1 
ATOM   3810  H  H    . MET   A  1  252 ? 25.950  -31.839 -19.496  1.00 49.00  ? 252  MET   A H    1 
ATOM   3811  H  HA   . MET   A  1  252 ? 28.629  -31.911 -19.672  1.00 50.86  ? 252  MET   A HA   1 
ATOM   3812  H  HB2  . MET   A  1  252 ? 27.036  -33.812 -21.016  1.00 53.62  ? 252  MET   A HB2  1 
ATOM   3813  H  HB3  . MET   A  1  252 ? 28.539  -33.514 -21.438  1.00 53.62  ? 252  MET   A HB3  1 
ATOM   3814  H  HG2  . MET   A  1  252 ? 29.226  -34.282 -19.315  1.00 58.85  ? 252  MET   A HG2  1 
ATOM   3815  H  HG3  . MET   A  1  252 ? 27.722  -34.707 -19.028  1.00 58.85  ? 252  MET   A HG3  1 
ATOM   3816  H  HE1  . MET   A  1  252 ? 30.487  -36.665 -21.854  1.00 62.51  ? 252  MET   A HE1  1 
ATOM   3817  H  HE2  . MET   A  1  252 ? 30.037  -35.154 -22.047  1.00 62.51  ? 252  MET   A HE2  1 
ATOM   3818  H  HE3  . MET   A  1  252 ? 30.898  -35.571 -20.778  1.00 62.51  ? 252  MET   A HE3  1 
ATOM   3819  N  N    . VAL   A  1  253 ? 28.601  -30.845 -21.989  1.00 40.76  ? 253  VAL   A N    1 
ATOM   3820  C  CA   . VAL   A  1  253 ? 28.521  -30.077 -23.223  1.00 39.87  ? 253  VAL   A CA   1 
ATOM   3821  C  C    . VAL   A  1  253 ? 29.237  -30.876 -24.301  1.00 44.64  ? 253  VAL   A C    1 
ATOM   3822  O  O    . VAL   A  1  253 ? 30.399  -31.260 -24.125  1.00 44.67  ? 253  VAL   A O    1 
ATOM   3823  C  CB   . VAL   A  1  253 ? 29.144  -28.675 -23.077  1.00 42.99  ? 253  VAL   A CB   1 
ATOM   3824  C  CG1  . VAL   A  1  253 ? 29.306  -28.009 -24.443  1.00 45.51  ? 253  VAL   A CG1  1 
ATOM   3825  C  CG2  . VAL   A  1  253 ? 28.288  -27.810 -22.162  1.00 36.50  ? 253  VAL   A CG2  1 
ATOM   3826  H  H    . VAL   A  1  253 ? 29.400  -31.100 -21.800  1.00 48.95  ? 253  VAL   A H    1 
ATOM   3827  H  HA   . VAL   A  1  253 ? 27.593  -29.960 -23.479  1.00 47.88  ? 253  VAL   A HA   1 
ATOM   3828  H  HB   . VAL   A  1  253 ? 30.025  -28.765 -22.681  1.00 51.63  ? 253  VAL   A HB   1 
ATOM   3829  H  HG11 . VAL   A  1  253 ? 29.638  -27.106 -24.317  1.00 54.64  ? 253  VAL   A HG11 1 
ATOM   3830  H  HG12 . VAL   A  1  253 ? 29.936  -28.522 -24.972  1.00 54.64  ? 253  VAL   A HG12 1 
ATOM   3831  H  HG13 . VAL   A  1  253 ? 28.444  -27.984 -24.887  1.00 54.64  ? 253  VAL   A HG13 1 
ATOM   3832  H  HG21 . VAL   A  1  253 ? 28.673  -26.921 -22.117  1.00 43.84  ? 253  VAL   A HG21 1 
ATOM   3833  H  HG22 . VAL   A  1  253 ? 27.389  -27.763 -22.522  1.00 43.84  ? 253  VAL   A HG22 1 
ATOM   3834  H  HG23 . VAL   A  1  253 ? 28.270  -28.208 -21.278  1.00 43.84  ? 253  VAL   A HG23 1 
ATOM   3835  N  N    . TYR   A  1  254 ? 28.544  -31.136 -25.403  1.00 52.12  ? 254  TYR   A N    1 
ATOM   3836  C  CA   . TYR   A  1  254 ? 29.109  -31.871 -26.523  1.00 49.23  ? 254  TYR   A CA   1 
ATOM   3837  C  C    . TYR   A  1  254 ? 29.543  -30.900 -27.611  1.00 48.63  ? 254  TYR   A C    1 
ATOM   3838  O  O    . TYR   A  1  254 ? 28.857  -29.910 -27.883  1.00 48.39  ? 254  TYR   A O    1 
ATOM   3839  C  CB   . TYR   A  1  254 ? 28.099  -32.858 -27.110  1.00 50.41  ? 254  TYR   A CB   1 
ATOM   3840  C  CG   . TYR   A  1  254 ? 27.673  -33.989 -26.198  1.00 50.87  ? 254  TYR   A CG   1 
ATOM   3841  C  CD1  . TYR   A  1  254 ? 28.374  -34.291 -25.036  1.00 51.32  ? 254  TYR   A CD1  1 
ATOM   3842  C  CD2  . TYR   A  1  254 ? 26.566  -34.763 -26.512  1.00 50.48  ? 254  TYR   A CD2  1 
ATOM   3843  C  CE1  . TYR   A  1  254 ? 27.975  -35.333 -24.213  1.00 53.22  ? 254  TYR   A CE1  1 
ATOM   3844  C  CE2  . TYR   A  1  254 ? 26.162  -35.801 -25.702  1.00 51.65  ? 254  TYR   A CE2  1 
ATOM   3845  C  CZ   . TYR   A  1  254 ? 26.867  -36.083 -24.555  1.00 54.50  ? 254  TYR   A CZ   1 
ATOM   3846  O  OH   . TYR   A  1  254 ? 26.456  -37.121 -23.750  1.00 59.37  ? 254  TYR   A OH   1 
ATOM   3847  H  H    . TYR   A  1  254 ? 27.729  -30.891 -25.527  1.00 62.58  ? 254  TYR   A H    1 
ATOM   3848  H  HA   . TYR   A  1  254 ? 29.880  -32.370 -26.213  1.00 59.11  ? 254  TYR   A HA   1 
ATOM   3849  H  HB2  . TYR   A  1  254 ? 27.298  -32.367 -27.351  1.00 60.53  ? 254  TYR   A HB2  1 
ATOM   3850  H  HB3  . TYR   A  1  254 ? 28.491  -33.260 -27.901  1.00 60.53  ? 254  TYR   A HB3  1 
ATOM   3851  H  HD1  . TYR   A  1  254 ? 29.121  -33.787 -24.807  1.00 61.62  ? 254  TYR   A HD1  1 
ATOM   3852  H  HD2  . TYR   A  1  254 ? 26.087  -34.578 -27.287  1.00 60.61  ? 254  TYR   A HD2  1 
ATOM   3853  H  HE1  . TYR   A  1  254 ? 28.450  -35.525 -23.437  1.00 63.90  ? 254  TYR   A HE1  1 
ATOM   3854  H  HE2  . TYR   A  1  254 ? 25.417  -36.309 -25.930  1.00 62.01  ? 254  TYR   A HE2  1 
ATOM   3855  H  HH   . TYR   A  1  254 ? 25.749  -37.457 -24.054  1.00 71.28  ? 254  TYR   A HH   1 
ATOM   3856  N  N    . ILE   A  1  255 ? 30.684  -31.188 -28.230  1.00 50.53  ? 255  ILE   A N    1 
ATOM   3857  C  CA   . ILE   A  1  255 ? 31.113  -30.513 -29.448  1.00 49.80  ? 255  ILE   A CA   1 
ATOM   3858  C  C    . ILE   A  1  255 ? 31.212  -31.561 -30.548  1.00 51.35  ? 255  ILE   A C    1 
ATOM   3859  O  O    . ILE   A  1  255 ? 31.885  -32.585 -30.379  1.00 52.61  ? 255  ILE   A O    1 
ATOM   3860  C  CB   . ILE   A  1  255 ? 32.452  -29.775 -29.265  1.00 52.87  ? 255  ILE   A CB   1 
ATOM   3861  C  CG1  . ILE   A  1  255 ? 32.328  -28.727 -28.154  1.00 52.66  ? 255  ILE   A CG1  1 
ATOM   3862  C  CG2  . ILE   A  1  255 ? 32.877  -29.116 -30.578  1.00 55.39  ? 255  ILE   A CG2  1 
ATOM   3863  C  CD1  . ILE   A  1  255 ? 33.559  -27.853 -27.972  1.00 54.27  ? 255  ILE   A CD1  1 
ATOM   3864  H  H    . ILE   A  1  255 ? 31.238  -31.785 -27.956  1.00 60.67  ? 255  ILE   A H    1 
ATOM   3865  H  HA   . ILE   A  1  255 ? 30.448  -29.854 -29.703  1.00 59.80  ? 255  ILE   A HA   1 
ATOM   3866  H  HB   . ILE   A  1  255 ? 33.130  -30.420 -29.008  1.00 63.48  ? 255  ILE   A HB   1 
ATOM   3867  H  HG12 . ILE   A  1  255 ? 31.582  -28.142 -28.363  1.00 63.22  ? 255  ILE   A HG12 1 
ATOM   3868  H  HG13 . ILE   A  1  255 ? 32.166  -29.184 -27.314  1.00 63.22  ? 255  ILE   A HG13 1 
ATOM   3869  H  HG21 . ILE   A  1  255 ? 33.751  -28.712 -30.461  1.00 66.50  ? 255  ILE   A HG21 1 
ATOM   3870  H  HG22 . ILE   A  1  255 ? 32.915  -29.792 -31.273  1.00 66.50  ? 255  ILE   A HG22 1 
ATOM   3871  H  HG23 . ILE   A  1  255 ? 32.227  -28.436 -30.814  1.00 66.50  ? 255  ILE   A HG23 1 
ATOM   3872  H  HD11 . ILE   A  1  255 ? 33.412  -27.252 -27.224  1.00 65.16  ? 255  ILE   A HD11 1 
ATOM   3873  H  HD12 . ILE   A  1  255 ? 34.325  -28.420 -27.795  1.00 65.16  ? 255  ILE   A HD12 1 
ATOM   3874  H  HD13 . ILE   A  1  255 ? 33.706  -27.341 -28.783  1.00 65.16  ? 255  ILE   A HD13 1 
ATOM   3875  N  N    . TYR   A  1  256 ? 30.533  -31.308 -31.665  1.00 45.57  ? 256  TYR   A N    1 
ATOM   3876  C  CA   . TYR   A  1  256 ? 30.558  -32.180 -32.828  1.00 47.00  ? 256  TYR   A CA   1 
ATOM   3877  C  C    . TYR   A  1  256 ? 31.169  -31.435 -34.009  1.00 51.25  ? 256  TYR   A C    1 
ATOM   3878  O  O    . TYR   A  1  256 ? 31.097  -30.205 -34.090  1.00 51.39  ? 256  TYR   A O    1 
ATOM   3879  C  CB   . TYR   A  1  256 ? 29.149  -32.655 -33.222  1.00 46.01  ? 256  TYR   A CB   1 
ATOM   3880  C  CG   . TYR   A  1  256 ? 28.432  -33.552 -32.231  1.00 45.96  ? 256  TYR   A CG   1 
ATOM   3881  C  CD1  . TYR   A  1  256 ? 27.634  -33.017 -31.226  1.00 45.19  ? 256  TYR   A CD1  1 
ATOM   3882  C  CD2  . TYR   A  1  256 ? 28.517  -34.936 -32.329  1.00 46.61  ? 256  TYR   A CD2  1 
ATOM   3883  C  CE1  . TYR   A  1  256 ? 26.960  -33.836 -30.333  1.00 44.83  ? 256  TYR   A CE1  1 
ATOM   3884  C  CE2  . TYR   A  1  256 ? 27.848  -35.760 -31.442  1.00 46.82  ? 256  TYR   A CE2  1 
ATOM   3885  C  CZ   . TYR   A  1  256 ? 27.070  -35.207 -30.450  1.00 47.03  ? 256  TYR   A CZ   1 
ATOM   3886  O  OH   . TYR   A  1  256 ? 26.411  -36.040 -29.574  1.00 47.07  ? 256  TYR   A OH   1 
ATOM   3887  H  H    . TYR   A  1  256 ? 30.036  -30.615 -31.772  1.00 54.72  ? 256  TYR   A H    1 
ATOM   3888  H  HA   . TYR   A  1  256 ? 31.097  -32.960 -32.623  1.00 56.43  ? 256  TYR   A HA   1 
ATOM   3889  H  HB2  . TYR   A  1  256 ? 28.593  -31.872 -33.351  1.00 55.25  ? 256  TYR   A HB2  1 
ATOM   3890  H  HB3  . TYR   A  1  256 ? 29.221  -33.151 -34.053  1.00 55.25  ? 256  TYR   A HB3  1 
ATOM   3891  H  HD1  . TYR   A  1  256 ? 27.550  -32.093 -31.152  1.00 54.27  ? 256  TYR   A HD1  1 
ATOM   3892  H  HD2  . TYR   A  1  256 ? 29.033  -35.315 -33.003  1.00 55.97  ? 256  TYR   A HD2  1 
ATOM   3893  H  HE1  . TYR   A  1  256 ? 26.438  -33.464 -29.659  1.00 53.83  ? 256  TYR   A HE1  1 
ATOM   3894  H  HE2  . TYR   A  1  256 ? 27.923  -36.684 -31.516  1.00 56.22  ? 256  TYR   A HE2  1 
ATOM   3895  H  HH   . TYR   A  1  256 ? 26.421  -35.711 -28.802  1.00 56.52  ? 256  TYR   A HH   1 
ATOM   3896  N  N    . ASP   A  1  257 ? 31.757  -32.190 -34.934  1.00 54.17  ? 257  ASP   A N    1 
ATOM   3897  C  CA   . ASP   A  1  257 ? 32.312  -31.599 -36.144  1.00 57.30  ? 257  ASP   A CA   1 
ATOM   3898  C  C    . ASP   A  1  257 ? 31.190  -31.064 -37.027  1.00 58.56  ? 257  ASP   A C    1 
ATOM   3899  O  O    . ASP   A  1  257 ? 30.210  -31.764 -37.296  1.00 60.69  ? 257  ASP   A O    1 
ATOM   3900  C  CB   . ASP   A  1  257 ? 33.140  -32.636 -36.903  1.00 61.31  ? 257  ASP   A CB   1 
ATOM   3901  C  CG   . ASP   A  1  257 ? 33.996  -32.020 -37.996  1.00 71.92  ? 257  ASP   A CG   1 
ATOM   3902  O  OD1  . ASP   A  1  257 ? 33.513  -31.108 -38.699  1.00 75.68  ? 257  ASP   A OD1  1 
ATOM   3903  O  OD2  . ASP   A  1  257 ? 35.158  -32.452 -38.151  1.00 77.15  ? 257  ASP   A OD2  1 
ATOM   3904  H  H    . ASP   A  1  257 ? 31.845  -33.044 -34.883  1.00 65.04  ? 257  ASP   A H    1 
ATOM   3905  H  HA   . ASP   A  1  257 ? 32.895  -30.860 -35.908  1.00 68.79  ? 257  ASP   A HA   1 
ATOM   3906  H  HB2  . ASP   A  1  257 ? 33.729  -33.087 -36.279  1.00 73.61  ? 257  ASP   A HB2  1 
ATOM   3907  H  HB3  . ASP   A  1  257 ? 32.540  -33.276 -37.316  1.00 73.61  ? 257  ASP   A HB3  1 
ATOM   3908  N  N    . GLY   A  1  258 ? 31.336  -29.818 -37.479  1.00 56.28  ? 258  GLY   A N    1 
ATOM   3909  C  CA   . GLY   A  1  258 ? 30.337  -29.196 -38.326  1.00 55.47  ? 258  GLY   A CA   1 
ATOM   3910  C  C    . GLY   A  1  258 ? 30.289  -29.710 -39.747  1.00 56.61  ? 258  GLY   A C    1 
ATOM   3911  O  O    . GLY   A  1  258 ? 29.470  -29.228 -40.536  1.00 53.54  ? 258  GLY   A O    1 
ATOM   3912  H  H    . GLY   A  1  258 ? 32.011  -29.315 -37.305  1.00 67.57  ? 258  GLY   A H    1 
ATOM   3913  H  HA2  . GLY   A  1  258 ? 29.463  -29.340 -37.931  1.00 66.59  ? 258  GLY   A HA2  1 
ATOM   3914  H  HA3  . GLY   A  1  258 ? 30.513  -28.243 -38.364  1.00 66.59  ? 258  GLY   A HA3  1 
ATOM   3915  N  N    . LYS   A  1  259 ? 31.143  -30.670 -40.097  1.00 60.04  ? 259  LYS   A N    1 
ATOM   3916  C  CA   . LYS   A  1  259 ? 31.177  -31.255 -41.432  1.00 64.76  ? 259  LYS   A CA   1 
ATOM   3917  C  C    . LYS   A  1  259 ? 30.552  -32.644 -41.486  1.00 64.24  ? 259  LYS   A C    1 
ATOM   3918  O  O    . LYS   A  1  259 ? 29.906  -32.983 -42.482  1.00 65.08  ? 259  LYS   A O    1 
ATOM   3919  C  CB   . LYS   A  1  259 ? 32.626  -31.317 -41.936  1.00 74.06  ? 259  LYS   A CB   1 
ATOM   3920  C  CG   . LYS   A  1  259 ? 32.840  -32.203 -43.159  1.00 79.81  ? 259  LYS   A CG   1 
ATOM   3921  C  CD   . LYS   A  1  259 ? 34.204  -31.962 -43.808  1.00 84.51  ? 259  LYS   A CD   1 
ATOM   3922  C  CE   . LYS   A  1  259 ? 34.121  -30.934 -44.931  1.00 87.54  ? 259  LYS   A CE   1 
ATOM   3923  N  NZ   . LYS   A  1  259 ? 35.429  -30.712 -45.615  1.00 89.27  ? 259  LYS   A NZ   1 
ATOM   3924  H  H    . LYS   A  1  259 ? 31.727  -31.007 -39.564  1.00 72.08  ? 259  LYS   A H    1 
ATOM   3925  H  HA   . LYS   A  1  259 ? 30.676  -30.689 -42.040  1.00 77.75  ? 259  LYS   A HA   1 
ATOM   3926  H  HB2  . LYS   A  1  259 ? 32.908  -30.420 -42.172  1.00 88.91  ? 259  LYS   A HB2  1 
ATOM   3927  H  HB3  . LYS   A  1  259 ? 33.185  -31.664 -41.223  1.00 88.91  ? 259  LYS   A HB3  1 
ATOM   3928  H  HG2  . LYS   A  1  259 ? 32.793  -33.134 -42.891  1.00 95.81  ? 259  LYS   A HG2  1 
ATOM   3929  H  HG3  . LYS   A  1  259 ? 32.154  -32.010 -43.817  1.00 95.81  ? 259  LYS   A HG3  1 
ATOM   3930  H  HD2  . LYS   A  1  259 ? 34.824  -31.632 -43.139  1.00 101.45 ? 259  LYS   A HD2  1 
ATOM   3931  H  HD3  . LYS   A  1  259 ? 34.532  -32.795 -44.182  1.00 101.45 ? 259  LYS   A HD3  1 
ATOM   3932  H  HE2  . LYS   A  1  259 ? 33.485  -31.243 -45.595  1.00 105.09 ? 259  LYS   A HE2  1 
ATOM   3933  H  HE3  . LYS   A  1  259 ? 33.829  -30.086 -44.561  1.00 105.09 ? 259  LYS   A HE3  1 
ATOM   3934  H  HZ1  . LYS   A  1  259 ? 35.342  -30.088 -46.244  1.00 107.16 ? 259  LYS   A HZ1  1 
ATOM   3935  H  HZ2  . LYS   A  1  259 ? 36.040  -30.445 -45.026  1.00 107.16 ? 259  LYS   A HZ2  1 
ATOM   3936  H  HZ3  . LYS   A  1  259 ? 35.706  -31.468 -45.995  1.00 107.16 ? 259  LYS   A HZ3  1 
ATOM   3937  N  N    . ASN   A  1  260 ? 30.714  -33.455 -40.434  1.00 69.07  ? 260  ASN   A N    1 
ATOM   3938  C  CA   . ASN   A  1  260 ? 30.157  -34.803 -40.429  1.00 72.08  ? 260  ASN   A CA   1 
ATOM   3939  C  C    . ASN   A  1  260 ? 29.494  -35.182 -39.108  1.00 65.37  ? 260  ASN   A C    1 
ATOM   3940  O  O    . ASN   A  1  260 ? 29.180  -36.363 -38.911  1.00 63.92  ? 260  ASN   A O    1 
ATOM   3941  C  CB   . ASN   A  1  260 ? 31.248  -35.831 -40.766  1.00 83.79  ? 260  ASN   A CB   1 
ATOM   3942  C  CG   . ASN   A  1  260 ? 32.564  -35.534 -40.075  1.00 93.19  ? 260  ASN   A CG   1 
ATOM   3943  O  OD1  . ASN   A  1  260 ? 32.607  -34.818 -39.076  1.00 92.37  ? 260  ASN   A OD1  1 
ATOM   3944  N  ND2  . ASN   A  1  260 ? 33.648  -36.088 -40.608  1.00 103.55 ? 260  ASN   A ND2  1 
ATOM   3945  H  H    . ASN   A  1  260 ? 31.141  -33.246 -39.717  1.00 82.92  ? 260  ASN   A H    1 
ATOM   3946  H  HA   . ASN   A  1  260 ? 29.470  -34.846 -41.112  1.00 86.54  ? 260  ASN   A HA   1 
ATOM   3947  H  HB2  . ASN   A  1  260 ? 30.952  -36.710 -40.484  1.00 100.59 ? 260  ASN   A HB2  1 
ATOM   3948  H  HB3  . ASN   A  1  260 ? 31.404  -35.824 -41.724  1.00 100.59 ? 260  ASN   A HB3  1 
ATOM   3949  H  HD21 . ASN   A  1  260 ? 33.570  -36.585 -41.305  1.00 124.30 ? 260  ASN   A HD21 1 
ATOM   3950  N  N    . MET   A  1  261 ? 29.260  -34.231 -38.203  1.00 61.97  ? 261  MET   A N    1 
ATOM   3951  C  CA   . MET   A  1  261 ? 28.611  -34.509 -36.921  1.00 56.40  ? 261  MET   A CA   1 
ATOM   3952  C  C    . MET   A  1  261 ? 29.355  -35.587 -36.135  1.00 58.85  ? 261  MET   A C    1 
ATOM   3953  O  O    . MET   A  1  261 ? 28.765  -36.304 -35.325  1.00 60.51  ? 261  MET   A O    1 
ATOM   3954  C  CB   . MET   A  1  261 ? 27.145  -34.912 -37.118  1.00 52.90  ? 261  MET   A CB   1 
ATOM   3955  C  CG   . MET   A  1  261 ? 26.293  -34.816 -35.855  1.00 53.20  ? 261  MET   A CG   1 
ATOM   3956  S  SD   . MET   A  1  261 ? 26.081  -33.123 -35.266  1.00 56.42  ? 261  MET   A SD   1 
ATOM   3957  C  CE   . MET   A  1  261 ? 24.844  -32.516 -36.408  1.00 54.19  ? 261  MET   A CE   1 
ATOM   3958  H  H    . MET   A  1  261 ? 29.471  -33.405 -38.310  1.00 74.41  ? 261  MET   A H    1 
ATOM   3959  H  HA   . MET   A  1  261 ? 28.625  -33.694 -36.396  1.00 67.72  ? 261  MET   A HA   1 
ATOM   3960  H  HB2  . MET   A  1  261 ? 26.750  -34.328 -37.784  1.00 63.51  ? 261  MET   A HB2  1 
ATOM   3961  H  HB3  . MET   A  1  261 ? 27.115  -35.832 -37.424  1.00 63.51  ? 261  MET   A HB3  1 
ATOM   3962  H  HG2  . MET   A  1  261 ? 25.413  -35.179 -36.041  1.00 63.87  ? 261  MET   A HG2  1 
ATOM   3963  H  HG3  . MET   A  1  261 ? 26.720  -35.326 -35.148  1.00 63.87  ? 261  MET   A HG3  1 
ATOM   3964  H  HE1  . MET   A  1  261 ? 24.649  -31.589 -36.199  1.00 65.06  ? 261  MET   A HE1  1 
ATOM   3965  H  HE2  . MET   A  1  261 ? 25.188  -32.586 -37.313  1.00 65.06  ? 261  MET   A HE2  1 
ATOM   3966  H  HE3  . MET   A  1  261 ? 24.040  -33.052 -36.318  1.00 65.06  ? 261  MET   A HE3  1 
ATOM   3967  N  N    . SER   A  1  262 ? 30.656  -35.716 -36.375  1.00 62.05  ? 262  SER   A N    1 
ATOM   3968  C  CA   . SER   A  1  262 ? 31.488  -36.613 -35.587  1.00 61.40  ? 262  SER   A CA   1 
ATOM   3969  C  C    . SER   A  1  262 ? 31.842  -35.949 -34.262  1.00 60.69  ? 262  SER   A C    1 
ATOM   3970  O  O    . SER   A  1  262 ? 32.039  -34.733 -34.196  1.00 63.61  ? 262  SER   A O    1 
ATOM   3971  C  CB   . SER   A  1  262 ? 32.757  -36.974 -36.358  1.00 62.38  ? 262  SER   A CB   1 
ATOM   3972  O  OG   . SER   A  1  262 ? 33.631  -37.767 -35.575  1.00 68.86  ? 262  SER   A OG   1 
ATOM   3973  H  H    . SER   A  1  262 ? 31.082  -35.292 -36.990  1.00 74.50  ? 262  SER   A H    1 
ATOM   3974  H  HA   . SER   A  1  262 ? 31.012  -37.438 -35.402  1.00 73.71  ? 262  SER   A HA   1 
ATOM   3975  H  HB2  . SER   A  1  262 ? 32.510  -37.472 -37.153  1.00 74.90  ? 262  SER   A HB2  1 
ATOM   3976  H  HB3  . SER   A  1  262 ? 33.215  -36.156 -36.608  1.00 74.90  ? 262  SER   A HB3  1 
ATOM   3977  H  HG   . SER   A  1  262 ? 34.334  -37.931 -36.006  1.00 82.66  ? 262  SER   A HG   1 
ATOM   3978  N  N    . SER   A  1  263 ? 31.916  -36.751 -33.202  1.00 57.05  ? 263  SER   A N    1 
ATOM   3979  C  CA   . SER   A  1  263 ? 32.181  -36.204 -31.878  1.00 52.54  ? 263  SER   A CA   1 
ATOM   3980  C  C    . SER   A  1  263 ? 33.624  -35.722 -31.786  1.00 57.71  ? 263  SER   A C    1 
ATOM   3981  O  O    . SER   A  1  263 ? 34.557  -36.450 -32.141  1.00 61.69  ? 263  SER   A O    1 
ATOM   3982  C  CB   . SER   A  1  263 ? 31.903  -37.249 -30.800  1.00 48.14  ? 263  SER   A CB   1 
ATOM   3983  O  OG   . SER   A  1  263 ? 32.131  -36.709 -29.509  1.00 48.18  ? 263  SER   A OG   1 
ATOM   3984  H  H    . SER   A  1  263 ? 31.818  -37.605 -33.224  1.00 68.49  ? 263  SER   A H    1 
ATOM   3985  H  HA   . SER   A  1  263 ? 31.594  -35.448 -31.723  1.00 63.08  ? 263  SER   A HA   1 
ATOM   3986  H  HB2  . SER   A  1  263 ? 30.978  -37.533 -30.866  1.00 57.80  ? 263  SER   A HB2  1 
ATOM   3987  H  HB3  . SER   A  1  263 ? 32.493  -38.007 -30.935  1.00 57.80  ? 263  SER   A HB3  1 
ATOM   3988  H  HG   . SER   A  1  263 ? 31.599  -37.052 -28.957  1.00 57.86  ? 263  SER   A HG   1 
ATOM   3989  N  N    . LEU   A  1  264 ? 33.806  -34.493 -31.299  1.00 57.56  ? 264  LEU   A N    1 
ATOM   3990  C  CA   . LEU   A  1  264 ? 35.122  -33.872 -31.217  1.00 59.16  ? 264  LEU   A CA   1 
ATOM   3991  C  C    . LEU   A  1  264 ? 35.605  -33.711 -29.780  1.00 56.01  ? 264  LEU   A C    1 
ATOM   3992  O  O    . LEU   A  1  264 ? 36.673  -34.218 -29.429  1.00 57.00  ? 264  LEU   A O    1 
ATOM   3993  C  CB   . LEU   A  1  264 ? 35.107  -32.504 -31.916  1.00 62.63  ? 264  LEU   A CB   1 
ATOM   3994  C  CG   . LEU   A  1  264 ? 35.239  -32.447 -33.439  1.00 63.42  ? 264  LEU   A CG   1 
ATOM   3995  C  CD1  . LEU   A  1  264 ? 35.317  -30.991 -33.866  1.00 63.58  ? 264  LEU   A CD1  1 
ATOM   3996  C  CD2  . LEU   A  1  264 ? 36.454  -33.219 -33.941  1.00 65.88  ? 264  LEU   A CD2  1 
ATOM   3997  H  H    . LEU   A  1  264 ? 33.170  -33.994 -31.007  1.00 69.11  ? 264  LEU   A H    1 
ATOM   3998  H  HA   . LEU   A  1  264 ? 35.751  -34.449 -31.677  1.00 71.03  ? 264  LEU   A HA   1 
ATOM   3999  H  HB2  . LEU   A  1  264 ? 34.265  -32.076 -31.697  1.00 75.19  ? 264  LEU   A HB2  1 
ATOM   4000  H  HB3  . LEU   A  1  264 ? 35.846  -31.987 -31.557  1.00 75.19  ? 264  LEU   A HB3  1 
ATOM   4001  H  HG   . LEU   A  1  264 ? 34.464  -32.869 -33.841  1.00 76.14  ? 264  LEU   A HG   1 
ATOM   4002  H  HD11 . LEU   A  1  264 ? 35.440  -30.950 -34.828  1.00 76.33  ? 264  LEU   A HD11 1 
ATOM   4003  H  HD12 . LEU   A  1  264 ? 34.492  -30.545 -33.619  1.00 76.33  ? 264  LEU   A HD12 1 
ATOM   4004  H  HD13 . LEU   A  1  264 ? 36.067  -30.570 -33.419  1.00 76.33  ? 264  LEU   A HD13 1 
ATOM   4005  H  HD21 . LEU   A  1  264 ? 36.527  -33.101 -34.901  1.00 79.09  ? 264  LEU   A HD21 1 
ATOM   4006  H  HD22 . LEU   A  1  264 ? 37.249  -32.876 -33.504  1.00 79.09  ? 264  LEU   A HD22 1 
ATOM   4007  H  HD23 . LEU   A  1  264 ? 36.340  -34.159 -33.731  1.00 79.09  ? 264  LEU   A HD23 1 
ATOM   4008  N  N    A TYR   A  1  265 ? 34.847  -33.020 -28.931  0.50 55.48  ? 265  TYR   A N    1 
ATOM   4009  N  N    B TYR   A  1  265 ? 34.849  -32.999 -28.943  0.50 55.50  ? 265  TYR   A N    1 
ATOM   4010  C  CA   A TYR   A  1  265 ? 35.296  -32.778 -27.568  0.50 49.85  ? 265  TYR   A CA   1 
ATOM   4011  C  CA   B TYR   A  1  265 ? 35.264  -32.697 -27.581  0.50 49.79  ? 265  TYR   A CA   1 
ATOM   4012  C  C    A TYR   A  1  265 ? 34.100  -32.760 -26.630  0.50 56.11  ? 265  TYR   A C    1 
ATOM   4013  C  C    B TYR   A  1  265 ? 34.075  -32.836 -26.640  0.50 55.95  ? 265  TYR   A C    1 
ATOM   4014  O  O    A TYR   A  1  265 ? 32.962  -32.514 -27.039  0.50 54.22  ? 265  TYR   A O    1 
ATOM   4015  O  O    B TYR   A  1  265 ? 32.915  -32.765 -27.055  0.50 54.69  ? 265  TYR   A O    1 
ATOM   4016  C  CB   A TYR   A  1  265 ? 36.082  -31.465 -27.463  0.50 56.26  ? 265  TYR   A CB   1 
ATOM   4017  C  CB   B TYR   A  1  265 ? 35.841  -31.277 -27.461  0.50 56.18  ? 265  TYR   A CB   1 
ATOM   4018  C  CG   A TYR   A  1  265 ? 36.742  -31.255 -26.119  0.50 52.11  ? 265  TYR   A CG   1 
ATOM   4019  C  CG   B TYR   A  1  265 ? 37.112  -31.038 -28.244  0.50 54.39  ? 265  TYR   A CG   1 
ATOM   4020  C  CD1  A TYR   A  1  265 ? 37.957  -31.854 -25.815  0.50 55.81  ? 265  TYR   A CD1  1 
ATOM   4021  C  CD1  B TYR   A  1  265 ? 38.327  -31.551 -27.808  0.50 56.18  ? 265  TYR   A CD1  1 
ATOM   4022  C  CD2  A TYR   A  1  265 ? 36.150  -30.456 -25.153  0.50 52.81  ? 265  TYR   A CD2  1 
ATOM   4023  C  CD2  B TYR   A  1  265 ? 37.102  -30.280 -29.408  0.50 54.31  ? 265  TYR   A CD2  1 
ATOM   4024  C  CE1  A TYR   A  1  265 ? 38.562  -31.662 -24.585  0.50 53.90  ? 265  TYR   A CE1  1 
ATOM   4025  C  CE1  B TYR   A  1  265 ? 39.493  -31.327 -28.516  0.50 55.61  ? 265  TYR   A CE1  1 
ATOM   4026  C  CE2  A TYR   A  1  265 ? 36.747  -30.258 -23.924  0.50 50.75  ? 265  TYR   A CE2  1 
ATOM   4027  C  CE2  B TYR   A  1  265 ? 38.263  -30.050 -30.122  0.50 53.23  ? 265  TYR   A CE2  1 
ATOM   4028  C  CZ   A TYR   A  1  265 ? 37.951  -30.862 -23.644  0.50 49.90  ? 265  TYR   A CZ   1 
ATOM   4029  C  CZ   B TYR   A  1  265 ? 39.455  -30.576 -29.671  0.50 55.71  ? 265  TYR   A CZ   1 
ATOM   4030  O  OH   A TYR   A  1  265 ? 38.541  -30.661 -22.417  0.50 46.78  ? 265  TYR   A OH   1 
ATOM   4031  O  OH   B TYR   A  1  265 ? 40.613  -30.348 -30.379  0.50 59.78  ? 265  TYR   A OH   1 
ATOM   4032  H  H    A TYR   A  1  265 ? 34.078  -32.685 -29.120  0.50 66.61  ? 265  TYR   A H    1 
ATOM   4033  H  H    B TYR   A  1  265 ? 34.078  -32.677 -29.147  0.50 66.63  ? 265  TYR   A H    1 
ATOM   4034  H  HA   A TYR   A  1  265 ? 35.874  -33.507 -27.293  0.50 59.86  ? 265  TYR   A HA   1 
ATOM   4035  H  HA   B TYR   A  1  265 ? 35.944  -33.335 -27.317  0.50 59.78  ? 265  TYR   A HA   1 
ATOM   4036  H  HB2  A TYR   A  1  265 ? 36.779  -31.464 -28.138  0.50 67.54  ? 265  TYR   A HB2  1 
ATOM   4037  H  HB2  B TYR   A  1  265 ? 35.177  -30.647 -27.783  0.50 67.46  ? 265  TYR   A HB2  1 
ATOM   4038  H  HB3  A TYR   A  1  265 ? 35.473  -30.725 -27.613  0.50 67.54  ? 265  TYR   A HB3  1 
ATOM   4039  H  HB3  B TYR   A  1  265 ? 36.037  -31.103 -26.527  0.50 67.46  ? 265  TYR   A HB3  1 
ATOM   4040  H  HD1  A TYR   A  1  265 ? 38.371  -32.394 -26.449  0.50 67.00  ? 265  TYR   A HD1  1 
ATOM   4041  H  HD1  B TYR   A  1  265 ? 38.356  -32.054 -27.026  0.50 67.45  ? 265  TYR   A HD1  1 
ATOM   4042  H  HD2  A TYR   A  1  265 ? 35.336  -30.045 -25.337  0.50 63.41  ? 265  TYR   A HD2  1 
ATOM   4043  H  HD2  B TYR   A  1  265 ? 36.300  -29.920 -29.712  0.50 65.21  ? 265  TYR   A HD2  1 
ATOM   4044  H  HE1  A TYR   A  1  265 ? 39.376  -32.070 -24.395  0.50 64.71  ? 265  TYR   A HE1  1 
ATOM   4045  H  HE1  B TYR   A  1  265 ? 40.298  -31.682 -28.214  0.50 66.76  ? 265  TYR   A HE1  1 
ATOM   4046  H  HE2  A TYR   A  1  265 ? 36.337  -29.718 -23.288  0.50 60.93  ? 265  TYR   A HE2  1 
ATOM   4047  H  HE2  B TYR   A  1  265 ? 38.240  -29.544 -30.901  0.50 63.92  ? 265  TYR   A HE2  1 
ATOM   4048  H  HH   A TYR   A  1  265 ? 38.058  -30.163 -21.945  0.50 56.18  ? 265  TYR   A HH   1 
ATOM   4049  H  HH   B TYR   A  1  265 ? 40.444  -29.903 -31.071  0.50 71.77  ? 265  TYR   A HH   1 
ATOM   4050  N  N    . ASN   A  1  266 ? 34.383  -33.026 -25.356  1.00 56.41  ? 266  ASN   A N    1 
ATOM   4051  C  CA   . ASN   A  1  266 ? 33.378  -33.106 -24.309  1.00 56.67  ? 266  ASN   A CA   1 
ATOM   4052  C  C    . ASN   A  1  266 ? 33.807  -32.273 -23.109  1.00 55.16  ? 266  ASN   A C    1 
ATOM   4053  O  O    . ASN   A  1  266 ? 34.991  -32.233 -22.762  1.00 59.77  ? 266  ASN   A O    1 
ATOM   4054  C  CB   . ASN   A  1  266 ? 33.167  -34.550 -23.842  1.00 58.26  ? 266  ASN   A CB   1 
ATOM   4055  C  CG   . ASN   A  1  266 ? 32.291  -35.351 -24.774  1.00 61.17  ? 266  ASN   A CG   1 
ATOM   4056  O  OD1  . ASN   A  1  266 ? 31.419  -34.812 -25.454  1.00 61.66  ? 266  ASN   A OD1  1 
ATOM   4057  N  ND2  . ASN   A  1  266 ? 32.516  -36.659 -24.803  1.00 70.37  ? 266  ASN   A ND2  1 
ATOM   4058  H  H    A ASN   A  1  266 ? 35.180  -33.168 -25.068  0.50 67.73  ? 266  ASN   A H    1 
ATOM   4059  H  H    B ASN   A  1  266 ? 35.187  -33.113 -25.065  0.50 67.73  ? 266  ASN   A H    1 
ATOM   4060  H  HA   . ASN   A  1  266 ? 32.543  -32.754 -24.655  1.00 68.04  ? 266  ASN   A HA   1 
ATOM   4061  H  HB2  . ASN   A  1  266 ? 34.029  -34.992 -23.788  1.00 69.95  ? 266  ASN   A HB2  1 
ATOM   4062  H  HB3  . ASN   A  1  266 ? 32.744  -34.540 -22.969  1.00 69.95  ? 266  ASN   A HB3  1 
ATOM   4063  H  HD21 . ASN   A  1  266 ? 33.142  -36.997 -24.320  1.00 84.48  ? 266  ASN   A HD21 1 
ATOM   4064  N  N    . PHE   A  1  267 ? 32.836  -31.619 -22.478  1.00 49.26  ? 267  PHE   A N    1 
ATOM   4065  C  CA   . PHE   A  1  267 ? 33.004  -31.006 -21.169  1.00 51.26  ? 267  PHE   A CA   1 
ATOM   4066  C  C    . PHE   A  1  267 ? 32.013  -31.653 -20.210  1.00 53.73  ? 267  PHE   A C    1 
ATOM   4067  O  O    . PHE   A  1  267 ? 30.944  -32.112 -20.623  1.00 54.75  ? 267  PHE   A O    1 
ATOM   4068  C  CB   . PHE   A  1  267 ? 32.767  -29.490 -21.207  1.00 55.82  ? 267  PHE   A CB   1 
ATOM   4069  C  CG   . PHE   A  1  267 ? 33.654  -28.752 -22.172  1.00 59.19  ? 267  PHE   A CG   1 
ATOM   4070  C  CD1  . PHE   A  1  267 ? 33.333  -28.689 -23.518  1.00 60.62  ? 267  PHE   A CD1  1 
ATOM   4071  C  CD2  . PHE   A  1  267 ? 34.795  -28.103 -21.729  1.00 59.40  ? 267  PHE   A CD2  1 
ATOM   4072  C  CE1  . PHE   A  1  267 ? 34.140  -28.003 -24.406  1.00 60.27  ? 267  PHE   A CE1  1 
ATOM   4073  C  CE2  . PHE   A  1  267 ? 35.606  -27.414 -22.613  1.00 59.76  ? 267  PHE   A CE2  1 
ATOM   4074  C  CZ   . PHE   A  1  267 ? 35.278  -27.366 -23.954  1.00 58.77  ? 267  PHE   A CZ   1 
ATOM   4075  H  H    . PHE   A  1  267 ? 32.045  -31.515 -22.801  1.00 59.15  ? 267  PHE   A H    1 
ATOM   4076  H  HA   . PHE   A  1  267 ? 33.909  -31.148 -20.852  1.00 61.54  ? 267  PHE   A HA   1 
ATOM   4077  H  HB2  . PHE   A  1  267 ? 31.848  -29.326 -21.468  1.00 67.02  ? 267  PHE   A HB2  1 
ATOM   4078  H  HB3  . PHE   A  1  267 ? 32.930  -29.129 -20.322  1.00 67.02  ? 267  PHE   A HB3  1 
ATOM   4079  H  HD1  . PHE   A  1  267 ? 32.566  -29.114 -23.828  1.00 72.78  ? 267  PHE   A HD1  1 
ATOM   4080  H  HD2  . PHE   A  1  267 ? 35.019  -28.131 -20.827  1.00 71.31  ? 267  PHE   A HD2  1 
ATOM   4081  H  HE1  . PHE   A  1  267 ? 33.916  -27.971 -25.308  1.00 72.37  ? 267  PHE   A HE1  1 
ATOM   4082  H  HE2  . PHE   A  1  267 ? 36.371  -26.983 -22.305  1.00 71.75  ? 267  PHE   A HE2  1 
ATOM   4083  H  HZ   . PHE   A  1  267 ? 35.823  -26.905 -24.550  1.00 70.56  ? 267  PHE   A HZ   1 
ATOM   4084  N  N    . THR   A  1  268 ? 32.365  -31.692 -18.926  1.00 55.00  ? 268  THR   A N    1 
ATOM   4085  C  CA   . THR   A  1  268 ? 31.487  -32.284 -17.926  1.00 52.26  ? 268  THR   A CA   1 
ATOM   4086  C  C    . THR   A  1  268 ? 31.428  -31.401 -16.689  1.00 54.12  ? 268  THR   A C    1 
ATOM   4087  O  O    . THR   A  1  268 ? 32.441  -30.841 -16.263  1.00 55.02  ? 268  THR   A O    1 
ATOM   4088  C  CB   . THR   A  1  268 ? 31.946  -33.692 -17.525  1.00 56.40  ? 268  THR   A CB   1 
ATOM   4089  O  OG1  . THR   A  1  268 ? 32.004  -34.529 -18.687  1.00 60.01  ? 268  THR   A OG1  1 
ATOM   4090  C  CG2  . THR   A  1  268 ? 30.976  -34.300 -16.516  1.00 57.04  ? 268  THR   A CG2  1 
ATOM   4091  H  H    . THR   A  1  268 ? 33.104  -31.384 -18.613  1.00 66.03  ? 268  THR   A H    1 
ATOM   4092  H  HA   . THR   A  1  268 ? 30.593  -32.342 -18.298  1.00 62.75  ? 268  THR   A HA   1 
ATOM   4093  H  HB   . THR   A  1  268 ? 32.825  -33.643 -17.118  1.00 67.72  ? 268  THR   A HB   1 
ATOM   4094  H  HG1  . THR   A  1  268 ? 32.243  -35.304 -18.471  1.00 72.05  ? 268  THR   A HG1  1 
ATOM   4095  H  HG21 . THR   A  1  268 ? 31.233  -35.215 -16.318  1.00 68.49  ? 268  THR   A HG21 1 
ATOM   4096  H  HG22 . THR   A  1  268 ? 30.987  -33.786 -15.694  1.00 68.49  ? 268  THR   A HG22 1 
ATOM   4097  H  HG23 . THR   A  1  268 ? 30.076  -34.297 -16.877  1.00 68.49  ? 268  THR   A HG23 1 
ATOM   4098  N  N    . GLY   A  1  269 ? 30.233  -31.296 -16.115  1.00 52.33  ? 269  GLY   A N    1 
ATOM   4099  C  CA   . GLY   A  1  269 ? 30.044  -30.517 -14.912  1.00 52.90  ? 269  GLY   A CA   1 
ATOM   4100  C  C    . GLY   A  1  269 ? 30.690  -31.160 -13.700  1.00 56.39  ? 269  GLY   A C    1 
ATOM   4101  O  O    . GLY   A  1  269 ? 31.094  -32.323 -13.702  1.00 57.44  ? 269  GLY   A O    1 
ATOM   4102  H  H    . GLY   A  1  269 ? 29.516  -31.670 -16.408  1.00 62.83  ? 269  GLY   A H    1 
ATOM   4103  H  HA2  . GLY   A  1  269 ? 30.433  -29.637 -15.035  1.00 63.52  ? 269  GLY   A HA2  1 
ATOM   4104  H  HA3  . GLY   A  1  269 ? 29.094  -30.421 -14.738  1.00 63.52  ? 269  GLY   A HA3  1 
ATOM   4105  N  N    . GLU   A  1  270 ? 30.779  -30.367 -12.633  1.00 64.25  ? 270  GLU   A N    1 
ATOM   4106  C  CA   . GLU   A  1  270 ? 31.415  -30.790 -11.395  1.00 70.92  ? 270  GLU   A CA   1 
ATOM   4107  C  C    . GLU   A  1  270 ? 30.432  -31.066 -10.268  1.00 69.92  ? 270  GLU   A C    1 
ATOM   4108  O  O    . GLU   A  1  270 ? 30.825  -31.676 -9.267   1.00 75.76  ? 270  GLU   A O    1 
ATOM   4109  C  CB   . GLU   A  1  270 ? 32.412  -29.721 -10.920  1.00 80.38  ? 270  GLU   A CB   1 
ATOM   4110  C  CG   . GLU   A  1  270 ? 33.571  -29.461 -11.867  1.00 95.90  ? 270  GLU   A CG   1 
ATOM   4111  C  CD   . GLU   A  1  270 ? 34.681  -30.484 -11.728  1.00 106.61 ? 270  GLU   A CD   1 
ATOM   4112  O  OE1  . GLU   A  1  270 ? 34.481  -31.644 -12.145  1.00 109.49 ? 270  GLU   A OE1  1 
ATOM   4113  O  OE2  . GLU   A  1  270 ? 35.751  -30.129 -11.190  1.00 111.42 ? 270  GLU   A OE2  1 
ATOM   4114  H  H    . GLU   A  1  270 ? 30.471  -29.565 -12.604  1.00 77.14  ? 270  GLU   A H    1 
ATOM   4115  H  HA   . GLU   A  1  270 ? 31.904  -31.609 -11.572  1.00 85.14  ? 270  GLU   A HA   1 
ATOM   4116  H  HB2  . GLU   A  1  270 ? 31.934  -28.884 -10.808  1.00 96.49  ? 270  GLU   A HB2  1 
ATOM   4117  H  HB3  . GLU   A  1  270 ? 32.786  -30.006 -10.072  1.00 96.49  ? 270  GLU   A HB3  1 
ATOM   4118  H  HG2  . GLU   A  1  270 ? 33.247  -29.491 -12.780  1.00 115.11 ? 270  GLU   A HG2  1 
ATOM   4119  H  HG3  . GLU   A  1  270 ? 33.945  -28.586 -11.676  1.00 115.11 ? 270  GLU   A HG3  1 
ATOM   4120  N  N    . GLN   A  1  271 ? 29.177  -30.639 -10.394  1.00 64.67  ? 271  GLN   A N    1 
ATOM   4121  C  CA   . GLN   A  1  271 ? 28.235  -30.690 -9.286   1.00 60.13  ? 271  GLN   A CA   1 
ATOM   4122  C  C    . GLN   A  1  271 ? 26.887  -31.210 -9.759   1.00 62.44  ? 271  GLN   A C    1 
ATOM   4123  O  O    . GLN   A  1  271 ? 26.442  -30.898 -10.867  1.00 64.82  ? 271  GLN   A O    1 
ATOM   4124  C  CB   . GLN   A  1  271 ? 28.062  -29.308 -8.649   1.00 56.44  ? 271  GLN   A CB   1 
ATOM   4125  C  CG   . GLN   A  1  271 ? 27.136  -29.293 -7.448   1.00 58.44  ? 271  GLN   A CG   1 
ATOM   4126  C  CD   . GLN   A  1  271 ? 26.951  -27.904 -6.879   1.00 61.91  ? 271  GLN   A CD   1 
ATOM   4127  O  OE1  . GLN   A  1  271 ? 25.915  -27.270 -7.081   1.00 63.39  ? 271  GLN   A OE1  1 
ATOM   4128  N  NE2  . GLN   A  1  271 ? 27.958  -27.420 -6.163   1.00 62.25  ? 271  GLN   A NE2  1 
ATOM   4129  H  H    . GLN   A  1  271 ? 28.847  -30.313 -11.118  1.00 77.64  ? 271  GLN   A H    1 
ATOM   4130  H  HA   . GLN   A  1  271 ? 28.566  -31.309 -8.617   1.00 72.19  ? 271  GLN   A HA   1 
ATOM   4131  H  HB2  . GLN   A  1  271 ? 28.930  -28.990 -8.356   1.00 67.76  ? 271  GLN   A HB2  1 
ATOM   4132  H  HB3  . GLN   A  1  271 ? 27.694  -28.703 -9.313   1.00 67.76  ? 271  GLN   A HB3  1 
ATOM   4133  H  HG2  . GLN   A  1  271 ? 26.266  -29.628 -7.715   1.00 70.16  ? 271  GLN   A HG2  1 
ATOM   4134  H  HG3  . GLN   A  1  271 ? 27.510  -29.857 -6.753   1.00 70.16  ? 271  GLN   A HG3  1 
ATOM   4135  H  HE21 . GLN   A  1  271 ? 28.667  -27.891 -6.045   1.00 74.74  ? 271  GLN   A HE21 1 
ATOM   4136  H  HE22 . GLN   A  1  271 ? 27.902  -26.634 -5.818   1.00 74.74  ? 271  GLN   A HE22 1 
ATOM   4137  N  N    . MET   A  1  272 ? 26.243  -31.999 -8.902   1.00 63.61  ? 272  MET   A N    1 
ATOM   4138  C  CA   . MET   A  1  272 ? 24.953  -32.587 -9.232   1.00 63.20  ? 272  MET   A CA   1 
ATOM   4139  C  C    . MET   A  1  272 ? 23.880  -31.513 -9.343   1.00 62.22  ? 272  MET   A C    1 
ATOM   4140  O  O    . MET   A  1  272 ? 23.717  -30.683 -8.443   1.00 63.31  ? 272  MET   A O    1 
ATOM   4141  C  CB   . MET   A  1  272 ? 24.560  -33.610 -8.168   1.00 68.59  ? 272  MET   A CB   1 
ATOM   4142  C  CG   . MET   A  1  272 ? 25.426  -34.853 -8.165   1.00 74.32  ? 272  MET   A CG   1 
ATOM   4143  S  SD   . MET   A  1  272 ? 24.618  -36.252 -8.963   1.00 78.66  ? 272  MET   A SD   1 
ATOM   4144  C  CE   . MET   A  1  272 ? 26.037  -37.202 -9.497   1.00 84.33  ? 272  MET   A CE   1 
ATOM   4145  H  H    . MET   A  1  272 ? 26.534  -32.208 -8.120   1.00 76.37  ? 272  MET   A H    1 
ATOM   4146  H  HA   . MET   A  1  272 ? 25.028  -33.043 -10.085  1.00 75.87  ? 272  MET   A HA   1 
ATOM   4147  H  HB2  . MET   A  1  272 ? 24.635  -33.195 -7.294   1.00 82.34  ? 272  MET   A HB2  1 
ATOM   4148  H  HB3  . MET   A  1  272 ? 23.644  -33.887 -8.326   1.00 82.34  ? 272  MET   A HB3  1 
ATOM   4149  H  HG2  . MET   A  1  272 ? 26.250  -34.668 -8.642   1.00 89.22  ? 272  MET   A HG2  1 
ATOM   4150  H  HG3  . MET   A  1  272 ? 25.623  -35.101 -7.248   1.00 89.22  ? 272  MET   A HG3  1 
ATOM   4151  H  HE1  . MET   A  1  272 ? 25.730  -37.987 -9.977   1.00 101.23 ? 272  MET   A HE1  1 
ATOM   4152  H  HE2  . MET   A  1  272 ? 26.584  -36.651 -10.080  1.00 101.23 ? 272  MET   A HE2  1 
ATOM   4153  H  HE3  . MET   A  1  272 ? 26.550  -37.470 -8.718   1.00 101.23 ? 272  MET   A HE3  1 
ATOM   4154  N  N    . ALA   A  1  273 ? 23.146  -31.533 -10.455  1.00 58.94  ? 273  ALA   A N    1 
ATOM   4155  C  CA   . ALA   A  1  273 ? 21.969  -30.688 -10.643  1.00 59.53  ? 273  ALA   A CA   1 
ATOM   4156  C  C    . ALA   A  1  273 ? 22.318  -29.202 -10.644  1.00 56.50  ? 273  ALA   A C    1 
ATOM   4157  O  O    . ALA   A  1  273 ? 21.502  -28.364 -10.254  1.00 55.90  ? 273  ALA   A O    1 
ATOM   4158  C  CB   . ALA   A  1  273 ? 20.908  -30.982 -9.579   1.00 62.29  ? 273  ALA   A CB   1 
ATOM   4159  H  H    . ALA   A  1  273 ? 23.315  -32.039 -11.129  1.00 70.76  ? 273  ALA   A H    1 
ATOM   4160  H  HA   . ALA   A  1  273 ? 21.595  -30.891 -11.514  1.00 71.47  ? 273  ALA   A HA   1 
ATOM   4161  H  HB1  . ALA   A  1  273 ? 20.136  -30.417 -9.739   1.00 74.79  ? 273  ALA   A HB1  1 
ATOM   4162  H  HB2  . ALA   A  1  273 ? 20.652  -31.915 -9.637   1.00 74.79  ? 273  ALA   A HB2  1 
ATOM   4163  H  HB3  . ALA   A  1  273 ? 21.279  -30.794 -8.702   1.00 74.79  ? 273  ALA   A HB3  1 
ATOM   4164  N  N    . ALA   A  1  274 ? 23.530  -28.860 -11.078  1.00 54.06  ? 274  ALA   A N    1 
ATOM   4165  C  CA   . ALA   A  1  274 ? 23.871  -27.465 -11.325  1.00 52.76  ? 274  ALA   A CA   1 
ATOM   4166  C  C    . ALA   A  1  274 ? 23.294  -26.957 -12.640  1.00 49.28  ? 274  ALA   A C    1 
ATOM   4167  O  O    . ALA   A  1  274 ? 23.392  -25.758 -12.922  1.00 44.92  ? 274  ALA   A O    1 
ATOM   4168  C  CB   . ALA   A  1  274 ? 25.390  -27.287 -11.327  1.00 52.47  ? 274  ALA   A CB   1 
ATOM   4169  H  H    . ALA   A  1  274 ? 24.168  -29.416 -11.236  1.00 64.91  ? 274  ALA   A H    1 
ATOM   4170  H  HA   . ALA   A  1  274 ? 23.514  -26.921 -10.606  1.00 63.34  ? 274  ALA   A HA   1 
ATOM   4171  H  HB1  . ALA   A  1  274 ? 25.598  -26.350 -11.470  1.00 63.00  ? 274  ALA   A HB1  1 
ATOM   4172  H  HB2  . ALA   A  1  274 ? 25.744  -27.578 -10.472  1.00 63.00  ? 274  ALA   A HB2  1 
ATOM   4173  H  HB3  . ALA   A  1  274 ? 25.770  -27.822 -12.042  1.00 63.00  ? 274  ALA   A HB3  1 
ATOM   4174  N  N    . TYR   A  1  275 ? 22.686  -27.840 -13.432  1.00 49.61  ? 275  TYR   A N    1 
ATOM   4175  C  CA   . TYR   A  1  275 ? 22.191  -27.516 -14.770  1.00 47.63  ? 275  TYR   A CA   1 
ATOM   4176  C  C    . TYR   A  1  275 ? 23.315  -26.991 -15.661  1.00 47.08  ? 275  TYR   A C    1 
ATOM   4177  O  O    . TYR   A  1  275 ? 23.124  -26.093 -16.483  1.00 45.47  ? 275  TYR   A O    1 
ATOM   4178  C  CB   . TYR   A  1  275 ? 21.018  -26.538 -14.714  1.00 47.91  ? 275  TYR   A CB   1 
ATOM   4179  C  CG   . TYR   A  1  275 ? 19.827  -27.080 -15.466  1.00 52.17  ? 275  TYR   A CG   1 
ATOM   4180  C  CD1  . TYR   A  1  275 ? 19.727  -26.927 -16.841  1.00 55.01  ? 275  TYR   A CD1  1 
ATOM   4181  C  CD2  . TYR   A  1  275 ? 18.825  -27.782 -14.809  1.00 53.60  ? 275  TYR   A CD2  1 
ATOM   4182  C  CE1  . TYR   A  1  275 ? 18.651  -27.436 -17.539  1.00 55.12  ? 275  TYR   A CE1  1 
ATOM   4183  C  CE2  . TYR   A  1  275 ? 17.743  -28.296 -15.500  1.00 53.80  ? 275  TYR   A CE2  1 
ATOM   4184  C  CZ   . TYR   A  1  275 ? 17.664  -28.122 -16.866  1.00 53.24  ? 275  TYR   A CZ   1 
ATOM   4185  O  OH   . TYR   A  1  275 ? 16.593  -28.629 -17.566  1.00 53.88  ? 275  TYR   A OH   1 
ATOM   4186  H  H    . TYR   A  1  275 ? 22.545  -28.659 -13.211  1.00 59.57  ? 275  TYR   A H    1 
ATOM   4187  H  HA   . TYR   A  1  275 ? 21.861  -28.332 -15.177  1.00 57.19  ? 275  TYR   A HA   1 
ATOM   4188  H  HB2  . TYR   A  1  275 ? 20.761  -26.395 -13.790  1.00 57.53  ? 275  TYR   A HB2  1 
ATOM   4189  H  HB3  . TYR   A  1  275 ? 21.281  -25.697 -15.119  1.00 57.53  ? 275  TYR   A HB3  1 
ATOM   4190  H  HD1  . TYR   A  1  275 ? 20.396  -26.473 -17.300  1.00 66.05  ? 275  TYR   A HD1  1 
ATOM   4191  H  HD2  . TYR   A  1  275 ? 18.882  -27.908 -13.889  1.00 64.36  ? 275  TYR   A HD2  1 
ATOM   4192  H  HE1  . TYR   A  1  275 ? 18.593  -27.316 -18.460  1.00 66.18  ? 275  TYR   A HE1  1 
ATOM   4193  H  HE2  . TYR   A  1  275 ? 17.074  -28.756 -15.047  1.00 64.59  ? 275  TYR   A HE2  1 
ATOM   4194  H  HH   . TYR   A  1  275 ? 16.258  -29.277 -17.149  1.00 64.69  ? 275  TYR   A HH   1 
ATOM   4195  N  N    . PHE   A  1  276 ? 24.496  -27.575 -15.493  1.00 52.07  ? 276  PHE   A N    1 
ATOM   4196  C  CA   . PHE   A  1  276 ? 25.631  -27.333 -16.373  1.00 49.74  ? 276  PHE   A CA   1 
ATOM   4197  C  C    . PHE   A  1  276 ? 25.250  -27.601 -17.822  1.00 49.05  ? 276  PHE   A C    1 
ATOM   4198  O  O    . PHE   A  1  276 ? 24.941  -28.736 -18.193  1.00 51.00  ? 276  PHE   A O    1 
ATOM   4199  C  CB   . PHE   A  1  276 ? 26.781  -28.244 -15.933  1.00 45.98  ? 276  PHE   A CB   1 
ATOM   4200  C  CG   . PHE   A  1  276 ? 28.026  -28.120 -16.759  1.00 48.08  ? 276  PHE   A CG   1 
ATOM   4201  C  CD1  . PHE   A  1  276 ? 29.010  -27.211 -16.414  1.00 49.36  ? 276  PHE   A CD1  1 
ATOM   4202  C  CD2  . PHE   A  1  276 ? 28.232  -28.941 -17.856  1.00 52.06  ? 276  PHE   A CD2  1 
ATOM   4203  C  CE1  . PHE   A  1  276 ? 30.168  -27.105 -17.160  1.00 49.56  ? 276  PHE   A CE1  1 
ATOM   4204  C  CE2  . PHE   A  1  276 ? 29.388  -28.840 -18.607  1.00 52.96  ? 276  PHE   A CE2  1 
ATOM   4205  C  CZ   . PHE   A  1  276 ? 30.359  -27.923 -18.256  1.00 51.21  ? 276  PHE   A CZ   1 
ATOM   4206  H  H    . PHE   A  1  276 ? 24.671  -28.130 -14.859  1.00 62.52  ? 276  PHE   A H    1 
ATOM   4207  H  HA   . PHE   A  1  276 ? 25.920  -26.409 -16.312  1.00 59.72  ? 276  PHE   A HA   1 
ATOM   4208  H  HB2  . PHE   A  1  276 ? 27.014  -28.025 -15.017  1.00 55.21  ? 276  PHE   A HB2  1 
ATOM   4209  H  HB3  . PHE   A  1  276 ? 26.483  -29.165 -15.988  1.00 55.21  ? 276  PHE   A HB3  1 
ATOM   4210  H  HD1  . PHE   A  1  276 ? 28.891  -26.664 -15.672  1.00 59.27  ? 276  PHE   A HD1  1 
ATOM   4211  H  HD2  . PHE   A  1  276 ? 27.585  -29.567 -18.090  1.00 62.51  ? 276  PHE   A HD2  1 
ATOM   4212  H  HE1  . PHE   A  1  276 ? 30.819  -26.484 -16.923  1.00 59.50  ? 276  PHE   A HE1  1 
ATOM   4213  H  HE2  . PHE   A  1  276 ? 29.512  -29.390 -19.347  1.00 63.59  ? 276  PHE   A HE2  1 
ATOM   4214  H  HZ   . PHE   A  1  276 ? 31.140  -27.856 -18.756  1.00 61.49  ? 276  PHE   A HZ   1 
ATOM   4215  N  N    . GLY   A  1  277 ? 25.271  -26.551 -18.642  1.00 43.51  ? 277  GLY   A N    1 
ATOM   4216  C  CA   . GLY   A  1  277 ? 24.860  -26.641 -20.029  1.00 41.57  ? 277  GLY   A CA   1 
ATOM   4217  C  C    . GLY   A  1  277 ? 23.556  -25.941 -20.343  1.00 43.46  ? 277  GLY   A C    1 
ATOM   4218  O  O    . GLY   A  1  277 ? 23.116  -25.977 -21.499  1.00 40.65  ? 277  GLY   A O    1 
ATOM   4219  H  H    . GLY   A  1  277 ? 25.525  -25.763 -18.408  1.00 52.25  ? 277  GLY   A H    1 
ATOM   4220  H  HA2  . GLY   A  1  277 ? 25.550  -26.248 -20.586  1.00 49.92  ? 277  GLY   A HA2  1 
ATOM   4221  H  HA3  . GLY   A  1  277 ? 24.759  -27.577 -20.265  1.00 49.92  ? 277  GLY   A HA3  1 
ATOM   4222  N  N    . PHE   A  1  278 ? 22.915  -25.318 -19.351  1.00 44.10  ? 278  PHE   A N    1 
ATOM   4223  C  CA   . PHE   A  1  278 ? 21.720  -24.525 -19.614  1.00 43.61  ? 278  PHE   A CA   1 
ATOM   4224  C  C    . PHE   A  1  278 ? 21.972  -23.514 -20.723  1.00 46.50  ? 278  PHE   A C    1 
ATOM   4225  O  O    . PHE   A  1  278 ? 21.083  -23.230 -21.535  1.00 44.45  ? 278  PHE   A O    1 
ATOM   4226  C  CB   . PHE   A  1  278 ? 21.284  -23.816 -18.329  1.00 43.92  ? 278  PHE   A CB   1 
ATOM   4227  C  CG   . PHE   A  1  278 ? 20.015  -23.024 -18.465  1.00 41.79  ? 278  PHE   A CG   1 
ATOM   4228  C  CD1  . PHE   A  1  278 ? 18.783  -23.633 -18.303  1.00 42.00  ? 278  PHE   A CD1  1 
ATOM   4229  C  CD2  . PHE   A  1  278 ? 20.055  -21.666 -18.739  1.00 43.38  ? 278  PHE   A CD2  1 
ATOM   4230  C  CE1  . PHE   A  1  278 ? 17.614  -22.907 -18.421  1.00 44.50  ? 278  PHE   A CE1  1 
ATOM   4231  C  CE2  . PHE   A  1  278 ? 18.888  -20.934 -18.857  1.00 46.94  ? 278  PHE   A CE2  1 
ATOM   4232  C  CZ   . PHE   A  1  278 ? 17.666  -21.556 -18.698  1.00 45.50  ? 278  PHE   A CZ   1 
ATOM   4233  H  H    . PHE   A  1  278 ? 23.151  -25.341 -18.524  1.00 52.96  ? 278  PHE   A H    1 
ATOM   4234  H  HA   . PHE   A  1  278 ? 20.999  -25.109 -19.898  1.00 52.37  ? 278  PHE   A HA   1 
ATOM   4235  H  HB2  . PHE   A  1  278 ? 21.142  -24.484 -17.640  1.00 52.74  ? 278  PHE   A HB2  1 
ATOM   4236  H  HB3  . PHE   A  1  278 ? 21.986  -23.204 -18.058  1.00 52.74  ? 278  PHE   A HB3  1 
ATOM   4237  H  HD1  . PHE   A  1  278 ? 18.742  -24.543 -18.113  1.00 50.44  ? 278  PHE   A HD1  1 
ATOM   4238  H  HD2  . PHE   A  1  278 ? 20.876  -21.242 -18.844  1.00 52.09  ? 278  PHE   A HD2  1 
ATOM   4239  H  HE1  . PHE   A  1  278 ? 16.792  -23.328 -18.314  1.00 53.43  ? 278  PHE   A HE1  1 
ATOM   4240  H  HE2  . PHE   A  1  278 ? 18.926  -20.024 -19.044  1.00 56.37  ? 278  PHE   A HE2  1 
ATOM   4241  H  HZ   . PHE   A  1  278 ? 16.880  -21.066 -18.777  1.00 54.64  ? 278  PHE   A HZ   1 
ATOM   4242  N  N    . SER   A  1  279 ? 23.185  -22.968 -20.777  1.00 49.29  ? 279  SER   A N    1 
ATOM   4243  C  CA   . SER   A  1  279 ? 23.567  -21.985 -21.777  1.00 50.36  ? 279  SER   A CA   1 
ATOM   4244  C  C    . SER   A  1  279 ? 24.983  -22.277 -22.246  1.00 48.59  ? 279  SER   A C    1 
ATOM   4245  O  O    . SER   A  1  279 ? 25.792  -22.846 -21.510  1.00 51.42  ? 279  SER   A O    1 
ATOM   4246  C  CB   . SER   A  1  279 ? 23.480  -20.560 -21.218  1.00 52.48  ? 279  SER   A CB   1 
ATOM   4247  O  OG   . SER   A  1  279 ? 24.198  -20.453 -20.001  1.00 58.66  ? 279  SER   A OG   1 
ATOM   4248  H  H    . SER   A  1  279 ? 23.819  -23.158 -20.227  1.00 59.19  ? 279  SER   A H    1 
ATOM   4249  H  HA   . SER   A  1  279 ? 22.977  -22.048 -22.545  1.00 60.47  ? 279  SER   A HA   1 
ATOM   4250  H  HB2  . SER   A  1  279 ? 23.859  -19.943 -21.864  1.00 63.02  ? 279  SER   A HB2  1 
ATOM   4251  H  HB3  . SER   A  1  279 ? 22.549  -20.340 -21.056  1.00 63.02  ? 279  SER   A HB3  1 
ATOM   4252  H  HG   . SER   A  1  279 ? 23.833  -19.884 -19.502  1.00 70.43  ? 279  SER   A HG   1 
ATOM   4253  N  N    . VAL   A  1  280 ? 25.274  -21.889 -23.488  1.00 50.68  ? 280  VAL   A N    1 
ATOM   4254  C  CA   . VAL   A  1  280 ? 26.605  -22.048 -24.060  1.00 50.47  ? 280  VAL   A CA   1 
ATOM   4255  C  C    . VAL   A  1  280 ? 26.836  -20.917 -25.052  1.00 47.49  ? 280  VAL   A C    1 
ATOM   4256  O  O    . VAL   A  1  280 ? 25.899  -20.419 -25.682  1.00 49.25  ? 280  VAL   A O    1 
ATOM   4257  C  CB   . VAL   A  1  280 ? 26.786  -23.426 -24.743  1.00 50.71  ? 280  VAL   A CB   1 
ATOM   4258  C  CG1  . VAL   A  1  280 ? 26.633  -24.556 -23.731  1.00 54.63  ? 280  VAL   A CG1  1 
ATOM   4259  C  CG2  . VAL   A  1  280 ? 25.798  -23.590 -25.890  1.00 50.91  ? 280  VAL   A CG2  1 
ATOM   4260  H  H    . VAL   A  1  280 ? 24.708  -21.526 -24.024  1.00 60.85  ? 280  VAL   A H    1 
ATOM   4261  H  HA   . VAL   A  1  280 ? 27.262  -21.977 -23.350  1.00 60.61  ? 280  VAL   A HA   1 
ATOM   4262  H  HB   . VAL   A  1  280 ? 27.682  -23.475 -25.110  1.00 60.89  ? 280  VAL   A HB   1 
ATOM   4263  H  HG11 . VAL   A  1  280 ? 26.807  -25.402 -24.173  1.00 65.60  ? 280  VAL   A HG11 1 
ATOM   4264  H  HG12 . VAL   A  1  280 ? 27.268  -24.422 -23.010  1.00 65.60  ? 280  VAL   A HG12 1 
ATOM   4265  H  HG13 . VAL   A  1  280 ? 25.728  -24.546 -23.381  1.00 65.60  ? 280  VAL   A HG13 1 
ATOM   4266  H  HG21 . VAL   A  1  280 ? 25.919  -24.466 -26.289  1.00 61.12  ? 280  VAL   A HG21 1 
ATOM   4267  H  HG22 . VAL   A  1  280 ? 24.895  -23.506 -25.544  1.00 61.12  ? 280  VAL   A HG22 1 
ATOM   4268  H  HG23 . VAL   A  1  280 ? 25.964  -22.900 -26.551  1.00 61.12  ? 280  VAL   A HG23 1 
ATOM   4269  N  N    . ALA   A  1  281 ? 28.097  -20.514 -25.191  1.00 45.10  ? 281  ALA   A N    1 
ATOM   4270  C  CA   . ALA   A  1  281 ? 28.469  -19.458 -26.121  1.00 45.40  ? 281  ALA   A CA   1 
ATOM   4271  C  C    . ALA   A  1  281 ? 29.878  -19.721 -26.631  1.00 49.61  ? 281  ALA   A C    1 
ATOM   4272  O  O    . ALA   A  1  281 ? 30.698  -20.331 -25.942  1.00 52.57  ? 281  ALA   A O    1 
ATOM   4273  C  CB   . ALA   A  1  281 ? 28.392  -18.075 -25.466  1.00 44.76  ? 281  ALA   A CB   1 
ATOM   4274  H  H    . ALA   A  1  281 ? 28.761  -20.841 -24.752  1.00 54.16  ? 281  ALA   A H    1 
ATOM   4275  H  HA   . ALA   A  1  281 ? 27.864  -19.469 -26.879  1.00 54.51  ? 281  ALA   A HA   1 
ATOM   4276  H  HB1  . ALA   A  1  281 ? 28.658  -17.404 -26.114  1.00 53.75  ? 281  ALA   A HB1  1 
ATOM   4277  H  HB2  . ALA   A  1  281 ? 27.481  -17.913 -25.176  1.00 53.75  ? 281  ALA   A HB2  1 
ATOM   4278  H  HB3  . ALA   A  1  281 ? 28.991  -18.053 -24.703  1.00 53.75  ? 281  ALA   A HB3  1 
ATOM   4279  N  N    . ALA   A  1  282 ? 30.150  -19.250 -27.848  1.00 51.67  ? 282  ALA   A N    1 
ATOM   4280  C  CA   . ALA   A  1  282 ? 31.455  -19.414 -28.479  1.00 50.31  ? 282  ALA   A CA   1 
ATOM   4281  C  C    . ALA   A  1  282 ? 31.906  -18.077 -29.045  1.00 54.98  ? 282  ALA   A C    1 
ATOM   4282  O  O    . ALA   A  1  282 ? 31.227  -17.499 -29.900  1.00 56.93  ? 282  ALA   A O    1 
ATOM   4283  C  CB   . ALA   A  1  282 ? 31.409  -20.474 -29.583  1.00 47.82  ? 282  ALA   A CB   1 
ATOM   4284  H  H    . ALA   A  1  282 ? 29.583  -18.825 -28.335  1.00 62.04  ? 282  ALA   A H    1 
ATOM   4285  H  HA   . ALA   A  1  282 ? 32.098  -19.693 -27.809  1.00 60.40  ? 282  ALA   A HA   1 
ATOM   4286  H  HB1  . ALA   A  1  282 ? 32.293  -20.564 -29.972  1.00 57.42  ? 282  ALA   A HB1  1 
ATOM   4287  H  HB2  . ALA   A  1  282 ? 31.130  -21.320 -29.198  1.00 57.42  ? 282  ALA   A HB2  1 
ATOM   4288  H  HB3  . ALA   A  1  282 ? 30.776  -20.195 -30.263  1.00 57.42  ? 282  ALA   A HB3  1 
ATOM   4289  N  N    . THR   A  1  283 ? 33.052  -17.594 -28.571  1.00 56.26  ? 283  THR   A N    1 
ATOM   4290  C  CA   . THR   A  1  283 ? 33.630  -16.347 -29.048  1.00 58.34  ? 283  THR   A CA   1 
ATOM   4291  C  C    . THR   A  1  283 ? 35.091  -16.308 -28.623  1.00 60.86  ? 283  THR   A C    1 
ATOM   4292  O  O    . THR   A  1  283 ? 35.455  -16.832 -27.568  1.00 61.20  ? 283  THR   A O    1 
ATOM   4293  C  CB   . THR   A  1  283 ? 32.875  -15.128 -28.501  1.00 60.66  ? 283  THR   A CB   1 
ATOM   4294  O  OG1  . THR   A  1  283 ? 33.472  -13.923 -28.997  1.00 65.85  ? 283  THR   A OG1  1 
ATOM   4295  C  CG2  . THR   A  1  283 ? 32.898  -15.113 -26.975  1.00 59.45  ? 283  THR   A CG2  1 
ATOM   4296  H  H    . THR   A  1  283 ? 33.521  -17.980 -27.962  1.00 67.54  ? 283  THR   A H    1 
ATOM   4297  H  HA   . THR   A  1  283 ? 33.588  -16.312 -30.016  1.00 70.05  ? 283  THR   A HA   1 
ATOM   4298  H  HB   . THR   A  1  283 ? 31.950  -15.172 -28.789  1.00 72.83  ? 283  THR   A HB   1 
ATOM   4299  H  HG1  . THR   A  1  283 ? 33.071  -13.254 -28.686  1.00 79.06  ? 283  THR   A HG1  1 
ATOM   4300  H  HG21 . THR   A  1  283 ? 32.413  -14.341 -26.644  1.00 71.38  ? 283  THR   A HG21 1 
ATOM   4301  H  HG22 . THR   A  1  283 ? 32.481  -15.918 -26.630  1.00 71.38  ? 283  THR   A HG22 1 
ATOM   4302  H  HG23 . THR   A  1  283 ? 33.813  -15.070 -26.657  1.00 71.38  ? 283  THR   A HG23 1 
ATOM   4303  N  N    . ASP   A  1  284 ? 35.924  -15.691 -29.459  1.00 61.84  ? 284  ASP   A N    1 
ATOM   4304  C  CA   . ASP   A  1  284 ? 37.341  -15.535 -29.147  1.00 62.38  ? 284  ASP   A CA   1 
ATOM   4305  C  C    . ASP   A  1  284 ? 37.495  -14.371 -28.177  1.00 66.31  ? 284  ASP   A C    1 
ATOM   4306  O  O    . ASP   A  1  284 ? 37.381  -13.207 -28.572  1.00 69.43  ? 284  ASP   A O    1 
ATOM   4307  C  CB   . ASP   A  1  284 ? 38.157  -15.298 -30.413  1.00 61.62  ? 284  ASP   A CB   1 
ATOM   4308  C  CG   . ASP   A  1  284 ? 39.635  -15.119 -30.126  1.00 64.76  ? 284  ASP   A CG   1 
ATOM   4309  O  OD1  . ASP   A  1  284 ? 40.088  -15.548 -29.043  1.00 66.04  ? 284  ASP   A OD1  1 
ATOM   4310  O  OD2  . ASP   A  1  284 ? 40.344  -14.539 -30.977  1.00 68.21  ? 284  ASP   A OD2  1 
ATOM   4311  H  H    . ASP   A  1  284 ? 35.691  -15.353 -30.215  1.00 74.25  ? 284  ASP   A H    1 
ATOM   4312  H  HA   . ASP   A  1  284 ? 37.669  -16.346 -28.728  1.00 74.89  ? 284  ASP   A HA   1 
ATOM   4313  H  HB2  . ASP   A  1  284 ? 38.055  -16.061 -31.003  1.00 73.98  ? 284  ASP   A HB2  1 
ATOM   4314  H  HB3  . ASP   A  1  284 ? 37.835  -14.495 -30.852  1.00 73.98  ? 284  ASP   A HB3  1 
ATOM   4315  N  N    . ILE   A  1  285 ? 37.763  -14.682 -26.910  1.00 68.06  ? 285  ILE   A N    1 
ATOM   4316  C  CA   . ILE   A  1  285 ? 37.784  -13.654 -25.878  1.00 72.69  ? 285  ILE   A CA   1 
ATOM   4317  C  C    . ILE   A  1  285 ? 39.167  -13.048 -25.664  1.00 75.39  ? 285  ILE   A C    1 
ATOM   4318  O  O    . ILE   A  1  285 ? 39.273  -11.983 -25.038  1.00 76.83  ? 285  ILE   A O    1 
ATOM   4319  C  CB   . ILE   A  1  285 ? 37.254  -14.230 -24.550  1.00 75.01  ? 285  ILE   A CB   1 
ATOM   4320  C  CG1  . ILE   A  1  285 ? 36.681  -13.116 -23.672  1.00 79.27  ? 285  ILE   A CG1  1 
ATOM   4321  C  CG2  . ILE   A  1  285 ? 38.354  -14.985 -23.804  1.00 76.34  ? 285  ILE   A CG2  1 
ATOM   4322  C  CD1  . ILE   A  1  285 ? 35.358  -12.567 -24.171  1.00 81.07  ? 285  ILE   A CD1  1 
ATOM   4323  H  H    . ILE   A  1  285 ? 37.933  -15.476 -26.625  1.00 81.71  ? 285  ILE   A H    1 
ATOM   4324  H  HA   . ILE   A  1  285 ? 37.202  -12.930 -26.158  1.00 87.26  ? 285  ILE   A HA   1 
ATOM   4325  H  HB   . ILE   A  1  285 ? 36.543  -14.855 -24.760  1.00 90.05  ? 285  ILE   A HB   1 
ATOM   4326  H  HG12 . ILE   A  1  285 ? 36.539  -13.466 -22.779  1.00 95.16  ? 285  ILE   A HG12 1 
ATOM   4327  H  HG13 . ILE   A  1  285 ? 37.315  -12.383 -23.645  1.00 95.16  ? 285  ILE   A HG13 1 
ATOM   4328  H  HG21 . ILE   A  1  285 ? 37.963  -15.440 -23.042  1.00 91.64  ? 285  ILE   A HG21 1 
ATOM   4329  H  HG22 . ILE   A  1  285 ? 38.756  -15.632 -24.405  1.00 91.64  ? 285  ILE   A HG22 1 
ATOM   4330  H  HG23 . ILE   A  1  285 ? 39.024  -14.352 -23.504  1.00 91.64  ? 285  ILE   A HG23 1 
ATOM   4331  H  HD11 . ILE   A  1  285 ? 35.046  -11.886 -23.554  1.00 97.32  ? 285  ILE   A HD11 1 
ATOM   4332  H  HD12 . ILE   A  1  285 ? 35.488  -12.181 -25.051  1.00 97.32  ? 285  ILE   A HD12 1 
ATOM   4333  H  HD13 . ILE   A  1  285 ? 34.713  -13.290 -24.219  1.00 97.32  ? 285  ILE   A HD13 1 
ATOM   4334  N  N    . ASN   A  1  286 ? 40.227  -13.687 -26.164  1.00 76.09  ? 286  ASN   A N    1 
ATOM   4335  C  CA   . ASN   A  1  286 ? 41.592  -13.254 -25.885  1.00 75.09  ? 286  ASN   A CA   1 
ATOM   4336  C  C    . ASN   A  1  286 ? 42.400  -12.963 -27.144  1.00 75.52  ? 286  ASN   A C    1 
ATOM   4337  O  O    . ASN   A  1  286 ? 43.623  -12.794 -27.056  1.00 78.80  ? 286  ASN   A O    1 
ATOM   4338  C  CB   . ASN   A  1  286 ? 42.310  -14.306 -25.033  1.00 73.87  ? 286  ASN   A CB   1 
ATOM   4339  C  CG   . ASN   A  1  286 ? 42.373  -15.656 -25.709  1.00 73.11  ? 286  ASN   A CG   1 
ATOM   4340  O  OD1  . ASN   A  1  286 ? 41.486  -16.017 -26.482  1.00 73.04  ? 286  ASN   A OD1  1 
ATOM   4341  N  ND2  . ASN   A  1  286 ? 43.425  -16.413 -25.422  1.00 71.77  ? 286  ASN   A ND2  1 
ATOM   4342  H  H    . ASN   A  1  286 ? 40.178  -14.379 -26.672  1.00 91.34  ? 286  ASN   A H    1 
ATOM   4343  H  HA   . ASN   A  1  286 ? 41.549  -12.428 -25.379  1.00 90.15  ? 286  ASN   A HA   1 
ATOM   4344  H  HB2  . ASN   A  1  286 ? 43.219  -14.011 -24.865  1.00 88.68  ? 286  ASN   A HB2  1 
ATOM   4345  H  HB3  . ASN   A  1  286 ? 41.835  -14.412 -24.193  1.00 88.68  ? 286  ASN   A HB3  1 
ATOM   4346  H  HD21 . ASN   A  1  286 ? 43.507  -17.190 -25.782  1.00 86.16  ? 286  ASN   A HD21 1 
ATOM   4347  H  HD22 . ASN   A  1  286 ? 44.025  -16.126 -24.877  1.00 86.16  ? 286  ASN   A HD22 1 
ATOM   4348  N  N    . GLY   A  1  287 ? 41.762  -12.912 -28.311  1.00 74.28  ? 287  GLY   A N    1 
ATOM   4349  C  CA   . GLY   A  1  287 ? 42.390  -12.358 -29.493  1.00 77.66  ? 287  GLY   A CA   1 
ATOM   4350  C  C    . GLY   A  1  287 ? 43.349  -13.259 -30.239  1.00 80.27  ? 287  GLY   A C    1 
ATOM   4351  O  O    . GLY   A  1  287 ? 44.094  -12.759 -31.091  1.00 82.73  ? 287  GLY   A O    1 
ATOM   4352  H  H    . GLY   A  1  287 ? 40.960  -13.195 -28.439  1.00 89.17  ? 287  GLY   A H    1 
ATOM   4353  H  HA2  . GLY   A  1  287 ? 41.692  -12.103 -30.116  1.00 93.22  ? 287  GLY   A HA2  1 
ATOM   4354  H  HA3  . GLY   A  1  287 ? 42.884  -11.566 -29.231  1.00 93.22  ? 287  GLY   A HA3  1 
ATOM   4355  N  N    . ASP   A  1  288 ? 43.366  -14.561 -29.964  1.00 79.51  ? 288  ASP   A N    1 
ATOM   4356  C  CA   . ASP   A  1  288 ? 44.220  -15.478 -30.710  1.00 79.91  ? 288  ASP   A CA   1 
ATOM   4357  C  C    . ASP   A  1  288 ? 43.501  -16.126 -31.889  1.00 80.46  ? 288  ASP   A C    1 
ATOM   4358  O  O    . ASP   A  1  288 ? 44.036  -17.068 -32.483  1.00 82.40  ? 288  ASP   A O    1 
ATOM   4359  C  CB   . ASP   A  1  288 ? 44.787  -16.561 -29.784  1.00 80.00  ? 288  ASP   A CB   1 
ATOM   4360  C  CG   . ASP   A  1  288 ? 43.708  -17.339 -29.053  1.00 81.14  ? 288  ASP   A CG   1 
ATOM   4361  O  OD1  . ASP   A  1  288 ? 42.511  -17.011 -29.211  1.00 80.42  ? 288  ASP   A OD1  1 
ATOM   4362  O  OD2  . ASP   A  1  288 ? 44.061  -18.284 -28.315  1.00 81.56  ? 288  ASP   A OD2  1 
ATOM   4363  H  H    . ASP   A  1  288 ? 42.892  -14.935 -29.352  1.00 95.44  ? 288  ASP   A H    1 
ATOM   4364  H  HA   . ASP   A  1  288 ? 44.971  -14.974 -31.060  1.00 95.93  ? 288  ASP   A HA   1 
ATOM   4365  H  HB2  . ASP   A  1  288 ? 45.303  -17.190 -30.312  1.00 96.04  ? 288  ASP   A HB2  1 
ATOM   4366  H  HB3  . ASP   A  1  288 ? 45.355  -16.142 -29.119  1.00 96.04  ? 288  ASP   A HB3  1 
ATOM   4367  N  N    . ASP   A  1  289 ? 42.314  -15.637 -32.245  1.00 78.50  ? 289  ASP   A N    1 
ATOM   4368  C  CA   . ASP   A  1  289 ? 41.508  -16.148 -33.351  1.00 78.55  ? 289  ASP   A CA   1 
ATOM   4369  C  C    . ASP   A  1  289 ? 41.042  -17.582 -33.130  1.00 75.73  ? 289  ASP   A C    1 
ATOM   4370  O  O    . ASP   A  1  289 ? 40.525  -18.210 -34.062  1.00 76.60  ? 289  ASP   A O    1 
ATOM   4371  C  CB   . ASP   A  1  289 ? 42.262  -16.050 -34.684  1.00 85.47  ? 289  ASP   A CB   1 
ATOM   4372  C  CG   . ASP   A  1  289 ? 42.509  -14.615 -35.111  1.00 93.45  ? 289  ASP   A CG   1 
ATOM   4373  O  OD1  . ASP   A  1  289 ? 41.606  -13.771 -34.922  1.00 94.15  ? 289  ASP   A OD1  1 
ATOM   4374  O  OD2  . ASP   A  1  289 ? 43.607  -14.332 -35.634  1.00 96.44  ? 289  ASP   A OD2  1 
ATOM   4375  H  H    . ASP   A  1  289 ? 41.939  -14.978 -31.840  1.00 94.24  ? 289  ASP   A H    1 
ATOM   4376  H  HA   . ASP   A  1  289 ? 40.713  -15.596 -33.414  1.00 94.30  ? 289  ASP   A HA   1 
ATOM   4377  H  HB2  . ASP   A  1  289 ? 43.123  -16.488 -34.594  1.00 102.60 ? 289  ASP   A HB2  1 
ATOM   4378  H  HB3  . ASP   A  1  289 ? 41.739  -16.484 -35.376  1.00 102.60 ? 289  ASP   A HB3  1 
ATOM   4379  N  N    . TYR   A  1  290 ? 41.207  -18.117 -31.924  1.00 75.10  ? 290  TYR   A N    1 
ATOM   4380  C  CA   . TYR   A  1  290 ? 40.702  -19.438 -31.570  1.00 73.53  ? 290  TYR   A CA   1 
ATOM   4381  C  C    . TYR   A  1  290 ? 39.452  -19.267 -30.716  1.00 71.90  ? 290  TYR   A C    1 
ATOM   4382  O  O    . TYR   A  1  290 ? 39.507  -18.655 -29.644  1.00 74.35  ? 290  TYR   A O    1 
ATOM   4383  C  CB   . TYR   A  1  290 ? 41.756  -20.251 -30.822  1.00 75.57  ? 290  TYR   A CB   1 
ATOM   4384  C  CG   . TYR   A  1  290 ? 42.788  -20.897 -31.718  1.00 75.50  ? 290  TYR   A CG   1 
ATOM   4385  C  CD1  . TYR   A  1  290 ? 42.491  -22.053 -32.428  1.00 71.26  ? 290  TYR   A CD1  1 
ATOM   4386  C  CD2  . TYR   A  1  290 ? 44.060  -20.358 -31.847  1.00 76.58  ? 290  TYR   A CD2  1 
ATOM   4387  C  CE1  . TYR   A  1  290 ? 43.429  -22.650 -33.246  1.00 73.92  ? 290  TYR   A CE1  1 
ATOM   4388  C  CE2  . TYR   A  1  290 ? 45.007  -20.949 -32.662  1.00 78.09  ? 290  TYR   A CE2  1 
ATOM   4389  C  CZ   . TYR   A  1  290 ? 44.686  -22.095 -33.359  1.00 79.56  ? 290  TYR   A CZ   1 
ATOM   4390  O  OH   . TYR   A  1  290 ? 45.625  -22.686 -34.172  1.00 84.41  ? 290  TYR   A OH   1 
ATOM   4391  H  H    . TYR   A  1  290 ? 41.619  -17.725 -31.279  1.00 90.16  ? 290  TYR   A H    1 
ATOM   4392  H  HA   . TYR   A  1  290 ? 40.467  -19.922 -32.378  1.00 88.27  ? 290  TYR   A HA   1 
ATOM   4393  H  HB2  . TYR   A  1  290 ? 42.225  -19.663 -30.209  1.00 90.72  ? 290  TYR   A HB2  1 
ATOM   4394  H  HB3  . TYR   A  1  290 ? 41.311  -20.957 -30.328  1.00 90.72  ? 290  TYR   A HB3  1 
ATOM   4395  H  HD1  . TYR   A  1  290 ? 41.645  -22.431 -32.351  1.00 85.55  ? 290  TYR   A HD1  1 
ATOM   4396  H  HD2  . TYR   A  1  290 ? 44.280  -19.587 -31.377  1.00 91.93  ? 290  TYR   A HD2  1 
ATOM   4397  H  HE1  . TYR   A  1  290 ? 43.215  -23.422 -33.718  1.00 88.74  ? 290  TYR   A HE1  1 
ATOM   4398  H  HE2  . TYR   A  1  290 ? 45.855  -20.576 -32.740  1.00 93.75  ? 290  TYR   A HE2  1 
ATOM   4399  H  HH   . TYR   A  1  290 ? 46.347  -22.258 -34.136  1.00 101.33 ? 290  TYR   A HH   1 
ATOM   4400  N  N    . ALA   A  1  291 ? 38.332  -19.804 -31.193  1.00 68.40  ? 291  ALA   A N    1 
ATOM   4401  C  CA   . ALA   A  1  291 ? 37.074  -19.658 -30.474  1.00 63.10  ? 291  ALA   A CA   1 
ATOM   4402  C  C    . ALA   A  1  291 ? 37.171  -20.292 -29.093  1.00 58.92  ? 291  ALA   A C    1 
ATOM   4403  O  O    . ALA   A  1  291 ? 37.775  -21.353 -28.917  1.00 56.33  ? 291  ALA   A O    1 
ATOM   4404  C  CB   . ALA   A  1  291 ? 35.934  -20.295 -31.267  1.00 60.81  ? 291  ALA   A CB   1 
ATOM   4405  H  H    . ALA   A  1  291 ? 38.275  -20.253 -31.924  1.00 82.11  ? 291  ALA   A H    1 
ATOM   4406  H  HA   . ALA   A  1  291 ? 36.876  -18.715 -30.364  1.00 75.75  ? 291  ALA   A HA   1 
ATOM   4407  H  HB1  . ALA   A  1  291 ? 35.108  -20.197 -30.767  1.00 73.01  ? 291  ALA   A HB1  1 
ATOM   4408  H  HB2  . ALA   A  1  291 ? 35.856  -19.847 -32.124  1.00 73.01  ? 291  ALA   A HB2  1 
ATOM   4409  H  HB3  . ALA   A  1  291 ? 36.129  -21.235 -31.402  1.00 73.01  ? 291  ALA   A HB3  1 
ATOM   4410  N  N    . ASP   A  1  292 ? 36.565  -19.633 -28.111  1.00 60.31  ? 292  ASP   A N    1 
ATOM   4411  C  CA   . ASP   A  1  292 ? 36.568  -20.084 -26.728  1.00 60.56  ? 292  ASP   A CA   1 
ATOM   4412  C  C    . ASP   A  1  292 ? 35.144  -20.420 -26.306  1.00 60.86  ? 292  ASP   A C    1 
ATOM   4413  O  O    . ASP   A  1  292 ? 34.172  -19.914 -26.871  1.00 62.47  ? 292  ASP   A O    1 
ATOM   4414  C  CB   . ASP   A  1  292 ? 37.180  -19.015 -25.817  1.00 61.88  ? 292  ASP   A CB   1 
ATOM   4415  C  CG   . ASP   A  1  292 ? 38.526  -18.519 -26.330  1.00 64.17  ? 292  ASP   A CG   1 
ATOM   4416  O  OD1  . ASP   A  1  292 ? 39.300  -19.343 -26.860  1.00 64.80  ? 292  ASP   A OD1  1 
ATOM   4417  O  OD2  . ASP   A  1  292 ? 38.808  -17.307 -26.221  1.00 66.76  ? 292  ASP   A OD2  1 
ATOM   4418  H  H    . ASP   A  1  292 ? 36.133  -18.899 -28.227  1.00 72.40  ? 292  ASP   A H    1 
ATOM   4419  H  HA   . ASP   A  1  292 ? 37.098  -20.891 -26.631  1.00 72.71  ? 292  ASP   A HA   1 
ATOM   4420  H  HB2  . ASP   A  1  292 ? 36.577  -18.256 -25.768  1.00 74.29  ? 292  ASP   A HB2  1 
ATOM   4421  H  HB3  . ASP   A  1  292 ? 37.314  -19.390 -24.932  1.00 74.29  ? 292  ASP   A HB3  1 
ATOM   4422  N  N    . VAL   A  1  293 ? 35.026  -21.283 -25.300  1.00 59.89  ? 293  VAL   A N    1 
ATOM   4423  C  CA   . VAL   A  1  293 ? 33.759  -21.915 -24.945  1.00 57.14  ? 293  VAL   A CA   1 
ATOM   4424  C  C    . VAL   A  1  293 ? 33.343  -21.448 -23.559  1.00 54.26  ? 293  VAL   A C    1 
ATOM   4425  O  O    . VAL   A  1  293 ? 34.101  -21.595 -22.591  1.00 55.50  ? 293  VAL   A O    1 
ATOM   4426  C  CB   . VAL   A  1  293 ? 33.861  -23.449 -24.997  1.00 56.26  ? 293  VAL   A CB   1 
ATOM   4427  C  CG1  . VAL   A  1  293 ? 32.570  -24.090 -24.504  1.00 53.29  ? 293  VAL   A CG1  1 
ATOM   4428  C  CG2  . VAL   A  1  293 ? 34.184  -23.905 -26.412  1.00 57.52  ? 293  VAL   A CG2  1 
ATOM   4429  H  H    . VAL   A  1  293 ? 35.682  -21.524 -24.798  1.00 71.91  ? 293  VAL   A H    1 
ATOM   4430  H  HA   . VAL   A  1  293 ? 33.078  -21.621 -25.570  1.00 68.60  ? 293  VAL   A HA   1 
ATOM   4431  H  HB   . VAL   A  1  293 ? 34.578  -23.738 -24.411  1.00 67.54  ? 293  VAL   A HB   1 
ATOM   4432  H  HG11 . VAL   A  1  293 ? 32.634  -25.052 -24.612  1.00 63.99  ? 293  VAL   A HG11 1 
ATOM   4433  H  HG12 . VAL   A  1  293 ? 32.445  -23.869 -23.568  1.00 63.99  ? 293  VAL   A HG12 1 
ATOM   4434  H  HG13 . VAL   A  1  293 ? 31.828  -23.747 -25.026  1.00 63.99  ? 293  VAL   A HG13 1 
ATOM   4435  H  HG21 . VAL   A  1  293 ? 34.225  -24.874 -26.430  1.00 69.06  ? 293  VAL   A HG21 1 
ATOM   4436  H  HG22 . VAL   A  1  293 ? 33.488  -23.592 -27.011  1.00 69.06  ? 293  VAL   A HG22 1 
ATOM   4437  H  HG23 . VAL   A  1  293 ? 35.040  -23.532 -26.676  1.00 69.06  ? 293  VAL   A HG23 1 
ATOM   4438  N  N    . PHE   A  1  294 ? 32.133  -20.905 -23.464  1.00 50.79  ? 294  PHE   A N    1 
ATOM   4439  C  CA   . PHE   A  1  294 ? 31.536  -20.479 -22.206  1.00 50.58  ? 294  PHE   A CA   1 
ATOM   4440  C  C    . PHE   A  1  294 ? 30.337  -21.372 -21.909  1.00 50.74  ? 294  PHE   A C    1 
ATOM   4441  O  O    . PHE   A  1  294 ? 29.495  -21.593 -22.785  1.00 44.53  ? 294  PHE   A O    1 
ATOM   4442  C  CB   . PHE   A  1  294 ? 31.112  -19.010 -22.277  1.00 53.92  ? 294  PHE   A CB   1 
ATOM   4443  C  CG   . PHE   A  1  294 ? 32.248  -18.063 -22.564  1.00 56.84  ? 294  PHE   A CG   1 
ATOM   4444  C  CD1  . PHE   A  1  294 ? 32.808  -17.992 -23.831  1.00 56.07  ? 294  PHE   A CD1  1 
ATOM   4445  C  CD2  . PHE   A  1  294 ? 32.755  -17.245 -21.568  1.00 58.72  ? 294  PHE   A CD2  1 
ATOM   4446  C  CE1  . PHE   A  1  294 ? 33.853  -17.126 -24.097  1.00 55.28  ? 294  PHE   A CE1  1 
ATOM   4447  C  CE2  . PHE   A  1  294 ? 33.799  -16.375 -21.828  1.00 58.53  ? 294  PHE   A CE2  1 
ATOM   4448  C  CZ   . PHE   A  1  294 ? 34.348  -16.316 -23.095  1.00 57.91  ? 294  PHE   A CZ   1 
ATOM   4449  H  H    . PHE   A  1  294 ? 31.621  -20.768 -24.141  1.00 60.99  ? 294  PHE   A H    1 
ATOM   4450  H  HA   . PHE   A  1  294 ? 32.174  -20.571 -21.481  1.00 60.74  ? 294  PHE   A HA   1 
ATOM   4451  H  HB2  . PHE   A  1  294 ? 30.456  -18.908 -22.985  1.00 64.74  ? 294  PHE   A HB2  1 
ATOM   4452  H  HB3  . PHE   A  1  294 ? 30.722  -18.756 -21.426  1.00 64.74  ? 294  PHE   A HB3  1 
ATOM   4453  H  HD1  . PHE   A  1  294 ? 32.476  -18.533 -24.511  1.00 67.33  ? 294  PHE   A HD1  1 
ATOM   4454  H  HD2  . PHE   A  1  294 ? 32.389  -17.280 -20.714  1.00 70.51  ? 294  PHE   A HD2  1 
ATOM   4455  H  HE1  . PHE   A  1  294 ? 34.222  -17.089 -24.950  1.00 66.38  ? 294  PHE   A HE1  1 
ATOM   4456  H  HE2  . PHE   A  1  294 ? 34.131  -15.831 -21.152  1.00 70.27  ? 294  PHE   A HE2  1 
ATOM   4457  H  HZ   . PHE   A  1  294 ? 35.050  -15.732 -23.271  1.00 69.53  ? 294  PHE   A HZ   1 
ATOM   4458  N  N    . ILE   A  1  295 ? 30.267  -21.889 -20.682  1.00 54.00  ? 295  ILE   A N    1 
ATOM   4459  C  CA   . ILE   A  1  295 ? 29.219  -22.818 -20.272  1.00 50.74  ? 295  ILE   A CA   1 
ATOM   4460  C  C    . ILE   A  1  295 ? 28.638  -22.338 -18.950  1.00 49.68  ? 295  ILE   A C    1 
ATOM   4461  O  O    . ILE   A  1  295 ? 29.384  -22.064 -18.003  1.00 53.08  ? 295  ILE   A O    1 
ATOM   4462  C  CB   . ILE   A  1  295 ? 29.751  -24.258 -20.130  1.00 49.94  ? 295  ILE   A CB   1 
ATOM   4463  C  CG1  . ILE   A  1  295 ? 30.428  -24.709 -21.426  1.00 50.39  ? 295  ILE   A CG1  1 
ATOM   4464  C  CG2  . ILE   A  1  295 ? 28.614  -25.208 -19.766  1.00 46.95  ? 295  ILE   A CG2  1 
ATOM   4465  C  CD1  . ILE   A  1  295 ? 31.187  -26.014 -21.296  1.00 50.97  ? 295  ILE   A CD1  1 
ATOM   4466  H  H    . ILE   A  1  295 ? 30.830  -21.711 -20.057  1.00 64.84  ? 295  ILE   A H    1 
ATOM   4467  H  HA   . ILE   A  1  295 ? 28.514  -22.814 -20.938  1.00 60.93  ? 295  ILE   A HA   1 
ATOM   4468  H  HB   . ILE   A  1  295 ? 30.410  -24.271 -19.418  1.00 59.97  ? 295  ILE   A HB   1 
ATOM   4469  H  HG12 . ILE   A  1  295 ? 29.747  -24.830 -22.107  1.00 60.50  ? 295  ILE   A HG12 1 
ATOM   4470  H  HG13 . ILE   A  1  295 ? 31.058  -24.026 -21.704  1.00 60.50  ? 295  ILE   A HG13 1 
ATOM   4471  H  HG21 . ILE   A  1  295 ? 28.969  -26.106 -19.680  1.00 56.38  ? 295  ILE   A HG21 1 
ATOM   4472  H  HG22 . ILE   A  1  295 ? 28.223  -24.924 -18.925  1.00 56.38  ? 295  ILE   A HG22 1 
ATOM   4473  H  HG23 . ILE   A  1  295 ? 27.945  -25.182 -20.468  1.00 56.38  ? 295  ILE   A HG23 1 
ATOM   4474  H  HD11 . ILE   A  1  295 ? 31.603  -26.223 -22.147  1.00 61.20  ? 295  ILE   A HD11 1 
ATOM   4475  H  HD12 . ILE   A  1  295 ? 31.867  -25.916 -20.611  1.00 61.20  ? 295  ILE   A HD12 1 
ATOM   4476  H  HD13 . ILE   A  1  295 ? 30.567  -26.717 -21.049  1.00 61.20  ? 295  ILE   A HD13 1 
ATOM   4477  N  N    . GLY   A  1  296 ? 27.313  -22.256 -18.880  1.00 43.76  ? 296  GLY   A N    1 
ATOM   4478  C  CA   . GLY   A  1  296 ? 26.624  -21.762 -17.699  1.00 45.90  ? 296  GLY   A CA   1 
ATOM   4479  C  C    . GLY   A  1  296 ? 25.982  -22.882 -16.899  1.00 48.66  ? 296  GLY   A C    1 
ATOM   4480  O  O    . GLY   A  1  296 ? 25.359  -23.784 -17.460  1.00 47.47  ? 296  GLY   A O    1 
ATOM   4481  H  H    . GLY   A  1  296 ? 26.783  -22.485 -19.518  1.00 52.55  ? 296  GLY   A H    1 
ATOM   4482  H  HA2  . GLY   A  1  296 ? 27.257  -21.301 -17.126  1.00 55.11  ? 296  GLY   A HA2  1 
ATOM   4483  H  HA3  . GLY   A  1  296 ? 25.930  -21.140 -17.967  1.00 55.11  ? 296  GLY   A HA3  1 
ATOM   4484  N  N    . ALA   A  1  297 ? 26.141  -22.806 -15.578  1.00 49.13  ? 297  ALA   A N    1 
ATOM   4485  C  CA   . ALA   A  1  297 ? 25.539  -23.745 -14.632  1.00 48.31  ? 297  ALA   A CA   1 
ATOM   4486  C  C    . ALA   A  1  297 ? 24.825  -22.916 -13.571  1.00 51.01  ? 297  ALA   A C    1 
ATOM   4487  O  O    . ALA   A  1  297 ? 25.334  -22.740 -12.456  1.00 50.64  ? 297  ALA   A O    1 
ATOM   4488  C  CB   . ALA   A  1  297 ? 26.592  -24.665 -14.014  1.00 47.11  ? 297  ALA   A CB   1 
ATOM   4489  H  H    . ALA   A  1  297 ? 26.611  -22.197 -15.193  1.00 58.99  ? 297  ALA   A H    1 
ATOM   4490  H  HA   . ALA   A  1  297 ? 24.889  -24.307 -15.084  1.00 58.01  ? 297  ALA   A HA   1 
ATOM   4491  H  HB1  . ALA   A  1  297 ? 26.155  -25.283 -13.407  1.00 56.57  ? 297  ALA   A HB1  1 
ATOM   4492  H  HB2  . ALA   A  1  297 ? 27.036  -25.157 -14.723  1.00 56.57  ? 297  ALA   A HB2  1 
ATOM   4493  H  HB3  . ALA   A  1  297 ? 27.237  -24.126 -13.530  1.00 56.57  ? 297  ALA   A HB3  1 
ATOM   4494  N  N    . PRO   A  1  298 ? 23.634  -22.393 -13.884  1.00 51.99  ? 298  PRO   A N    1 
ATOM   4495  C  CA   . PRO   A  1  298 ? 23.036  -21.354 -13.028  1.00 50.98  ? 298  PRO   A CA   1 
ATOM   4496  C  C    . PRO   A  1  298 ? 22.635  -21.826 -11.639  1.00 48.93  ? 298  PRO   A C    1 
ATOM   4497  O  O    . PRO   A  1  298 ? 22.346  -20.976 -10.786  1.00 50.95  ? 298  PRO   A O    1 
ATOM   4498  C  CB   . PRO   A  1  298 ? 21.802  -20.904 -13.829  1.00 53.35  ? 298  PRO   A CB   1 
ATOM   4499  C  CG   . PRO   A  1  298 ? 22.007  -21.431 -15.219  1.00 50.25  ? 298  PRO   A CG   1 
ATOM   4500  C  CD   . PRO   A  1  298 ? 22.800  -22.682 -15.063  1.00 49.32  ? 298  PRO   A CD   1 
ATOM   4501  H  HA   . PRO   A  1  298 ? 23.657  -20.614 -12.940  1.00 61.21  ? 298  PRO   A HA   1 
ATOM   4502  H  HB2  . PRO   A  1  298 ? 21.000  -21.279 -13.433  1.00 64.06  ? 298  PRO   A HB2  1 
ATOM   4503  H  HB3  . PRO   A  1  298 ? 21.749  -19.935 -13.832  1.00 64.06  ? 298  PRO   A HB3  1 
ATOM   4504  H  HG2  . PRO   A  1  298 ? 21.148  -21.617 -15.629  1.00 60.34  ? 298  PRO   A HG2  1 
ATOM   4505  H  HG3  . PRO   A  1  298 ? 22.493  -20.779 -15.749  1.00 60.34  ? 298  PRO   A HG3  1 
ATOM   4506  H  HD2  . PRO   A  1  298 ? 22.221  -23.443 -14.900  1.00 59.23  ? 298  PRO   A HD2  1 
ATOM   4507  H  HD3  . PRO   A  1  298 ? 23.350  -22.845 -15.845  1.00 59.23  ? 298  PRO   A HD3  1 
ATOM   4508  N  N    . LEU   A  1  299 ? 22.600  -23.132 -11.377  1.00 49.80  ? 299  LEU   A N    1 
ATOM   4509  C  CA   . LEU   A  1  299 ? 22.210  -23.652 -10.072  1.00 52.71  ? 299  LEU   A CA   1 
ATOM   4510  C  C    . LEU   A  1  299 ? 23.401  -24.177 -9.279   1.00 53.67  ? 299  LEU   A C    1 
ATOM   4511  O  O    . LEU   A  1  299 ? 23.212  -24.788 -8.222   1.00 54.00  ? 299  LEU   A O    1 
ATOM   4512  C  CB   . LEU   A  1  299 ? 21.162  -24.753 -10.236  1.00 54.44  ? 299  LEU   A CB   1 
ATOM   4513  C  CG   . LEU   A  1  299 ? 20.028  -24.448 -11.218  1.00 57.32  ? 299  LEU   A CG   1 
ATOM   4514  C  CD1  . LEU   A  1  299 ? 19.044  -25.607 -11.259  1.00 59.21  ? 299  LEU   A CD1  1 
ATOM   4515  C  CD2  . LEU   A  1  299 ? 19.318  -23.148 -10.862  1.00 57.89  ? 299  LEU   A CD2  1 
ATOM   4516  H  H    . LEU   A  1  299 ? 22.800  -23.743 -11.948  1.00 59.79  ? 299  LEU   A H    1 
ATOM   4517  H  HA   . LEU   A  1  299 ? 21.808  -22.932 -9.560   1.00 63.29  ? 299  LEU   A HA   1 
ATOM   4518  H  HB2  . LEU   A  1  299 ? 21.609  -25.554 -10.551  1.00 65.36  ? 299  LEU   A HB2  1 
ATOM   4519  H  HB3  . LEU   A  1  299 ? 20.757  -24.918 -9.370   1.00 65.36  ? 299  LEU   A HB3  1 
ATOM   4520  H  HG   . LEU   A  1  299 ? 20.406  -24.335 -12.104  1.00 68.82  ? 299  LEU   A HG   1 
ATOM   4521  H  HD11 . LEU   A  1  299 ? 18.341  -25.402 -11.896  1.00 71.09  ? 299  LEU   A HD11 1 
ATOM   4522  H  HD12 . LEU   A  1  299 ? 19.513  -26.411 -11.533  1.00 71.09  ? 299  LEU   A HD12 1 
ATOM   4523  H  HD13 . LEU   A  1  299 ? 18.664  -25.731 -10.375  1.00 71.09  ? 299  LEU   A HD13 1 
ATOM   4524  H  HD21 . LEU   A  1  299 ? 18.599  -22.997 -11.496  1.00 69.50  ? 299  LEU   A HD21 1 
ATOM   4525  H  HD22 . LEU   A  1  299 ? 18.958  -23.219 -9.964   1.00 69.50  ? 299  LEU   A HD22 1 
ATOM   4526  H  HD23 . LEU   A  1  299 ? 19.955  -22.418 -10.906  1.00 69.50  ? 299  LEU   A HD23 1 
ATOM   4527  N  N    . PHE   A  1  300 ? 24.618  -23.956 -9.768   1.00 52.24  ? 300  PHE   A N    1 
ATOM   4528  C  CA   . PHE   A  1  300 ? 25.811  -24.375 -9.046   1.00 54.21  ? 300  PHE   A CA   1 
ATOM   4529  C  C    . PHE   A  1  300 ? 25.853  -23.728 -7.667   1.00 57.22  ? 300  PHE   A C    1 
ATOM   4530  O  O    . PHE   A  1  300 ? 25.507  -22.555 -7.502   1.00 58.04  ? 300  PHE   A O    1 
ATOM   4531  C  CB   . PHE   A  1  300 ? 27.054  -24.000 -9.854   1.00 54.97  ? 300  PHE   A CB   1 
ATOM   4532  C  CG   . PHE   A  1  300 ? 28.347  -24.301 -9.159   1.00 53.09  ? 300  PHE   A CG   1 
ATOM   4533  C  CD1  . PHE   A  1  300 ? 28.891  -23.398 -8.262   1.00 53.65  ? 300  PHE   A CD1  1 
ATOM   4534  C  CD2  . PHE   A  1  300 ? 29.025  -25.480 -9.411   1.00 55.11  ? 300  PHE   A CD2  1 
ATOM   4535  C  CE1  . PHE   A  1  300 ? 30.081  -23.669 -7.622   1.00 53.63  ? 300  PHE   A CE1  1 
ATOM   4536  C  CE2  . PHE   A  1  300 ? 30.218  -25.757 -8.776   1.00 56.65  ? 300  PHE   A CE2  1 
ATOM   4537  C  CZ   . PHE   A  1  300 ? 30.747  -24.849 -7.879   1.00 54.03  ? 300  PHE   A CZ   1 
ATOM   4538  H  H    . PHE   A  1  300 ? 24.780  -23.565 -10.517  1.00 62.73  ? 300  PHE   A H    1 
ATOM   4539  H  HA   . PHE   A  1  300 ? 25.805  -25.337 -8.923   1.00 65.08  ? 300  PHE   A HA   1 
ATOM   4540  H  HB2  . PHE   A  1  300 ? 27.045  -24.497 -10.687  1.00 66.00  ? 300  PHE   A HB2  1 
ATOM   4541  H  HB3  . PHE   A  1  300 ? 27.031  -23.048 -10.036  1.00 66.00  ? 300  PHE   A HB3  1 
ATOM   4542  H  HD1  . PHE   A  1  300 ? 28.448  -22.598 -8.089   1.00 64.41  ? 300  PHE   A HD1  1 
ATOM   4543  H  HD2  . PHE   A  1  300 ? 28.672  -26.093 -10.016  1.00 66.17  ? 300  PHE   A HD2  1 
ATOM   4544  H  HE1  . PHE   A  1  300 ? 30.435  -23.057 -7.017   1.00 64.39  ? 300  PHE   A HE1  1 
ATOM   4545  H  HE2  . PHE   A  1  300 ? 30.665  -26.553 -8.951   1.00 68.02  ? 300  PHE   A HE2  1 
ATOM   4546  H  HZ   . PHE   A  1  300 ? 31.551  -25.034 -7.449   1.00 64.87  ? 300  PHE   A HZ   1 
ATOM   4547  N  N    . MET   A  1  301 ? 26.288  -24.499 -6.673   1.00 60.91  ? 301  MET   A N    1 
ATOM   4548  C  CA   . MET   A  1  301 ? 26.306  -24.062 -5.282   1.00 64.48  ? 301  MET   A CA   1 
ATOM   4549  C  C    . MET   A  1  301 ? 27.746  -23.909 -4.810   1.00 64.30  ? 301  MET   A C    1 
ATOM   4550  O  O    . MET   A  1  301 ? 28.526  -24.867 -4.855   1.00 60.52  ? 301  MET   A O    1 
ATOM   4551  C  CB   . MET   A  1  301 ? 25.553  -25.051 -4.391   1.00 67.05  ? 301  MET   A CB   1 
ATOM   4552  C  CG   . MET   A  1  301 ? 24.047  -25.051 -4.604   1.00 65.45  ? 301  MET   A CG   1 
ATOM   4553  S  SD   . MET   A  1  301 ? 23.180  -26.169 -3.487   1.00 63.67  ? 301  MET   A SD   1 
ATOM   4554  C  CE   . MET   A  1  301 ? 23.677  -27.759 -4.144   1.00 64.54  ? 301  MET   A CE   1 
ATOM   4555  H  H    . MET   A  1  301 ? 26.586  -25.299 -6.784   1.00 73.13  ? 301  MET   A H    1 
ATOM   4556  H  HA   . MET   A  1  301 ? 25.867  -23.199 -5.224   1.00 77.41  ? 301  MET   A HA   1 
ATOM   4557  H  HB2  . MET   A  1  301 ? 25.878  -25.947 -4.576   1.00 80.50  ? 301  MET   A HB2  1 
ATOM   4558  H  HB3  . MET   A  1  301 ? 25.720  -24.824 -3.463   1.00 80.50  ? 301  MET   A HB3  1 
ATOM   4559  H  HG2  . MET   A  1  301 ? 23.708  -24.155 -4.454   1.00 78.58  ? 301  MET   A HG2  1 
ATOM   4560  H  HG3  . MET   A  1  301 ? 23.857  -25.330 -5.513   1.00 78.58  ? 301  MET   A HG3  1 
ATOM   4561  H  HE1  . MET   A  1  301 ? 23.286  -28.462 -3.602   1.00 77.48  ? 301  MET   A HE1  1 
ATOM   4562  H  HE2  . MET   A  1  301 ? 23.364  -27.834 -5.059   1.00 77.48  ? 301  MET   A HE2  1 
ATOM   4563  H  HE3  . MET   A  1  301 ? 24.645  -27.822 -4.119   1.00 77.48  ? 301  MET   A HE3  1 
ATOM   4564  N  N    . ASP   A  1  302 ? 28.086  -22.708 -4.355   1.00 70.50  ? 302  ASP   A N    1 
ATOM   4565  C  CA   . ASP   A  1  302 ? 29.393  -22.404 -3.796   1.00 77.91  ? 302  ASP   A CA   1 
ATOM   4566  C  C    . ASP   A  1  302 ? 29.375  -22.607 -2.284   1.00 79.36  ? 302  ASP   A C    1 
ATOM   4567  O  O    . ASP   A  1  302 ? 28.317  -22.691 -1.656   1.00 81.01  ? 302  ASP   A O    1 
ATOM   4568  C  CB   . ASP   A  1  302 ? 29.790  -20.964 -4.127   1.00 87.22  ? 302  ASP   A CB   1 
ATOM   4569  C  CG   . ASP   A  1  302 ? 31.239  -20.660 -3.794   1.00 97.93  ? 302  ASP   A CG   1 
ATOM   4570  O  OD1  . ASP   A  1  302 ? 32.053  -21.606 -3.741   1.00 102.15 ? 302  ASP   A OD1  1 
ATOM   4571  O  OD2  . ASP   A  1  302 ? 31.561  -19.472 -3.579   1.00 102.57 ? 302  ASP   A OD2  1 
ATOM   4572  H  H    . ASP   A  1  302 ? 27.557  -22.029 -4.361   1.00 84.64  ? 302  ASP   A H    1 
ATOM   4573  H  HA   . ASP   A  1  302 ? 30.059  -22.997 -4.177   1.00 93.53  ? 302  ASP   A HA   1 
ATOM   4574  H  HB2  . ASP   A  1  302 ? 29.662  -20.811 -5.076   1.00 104.70 ? 302  ASP   A HB2  1 
ATOM   4575  H  HB3  . ASP   A  1  302 ? 29.232  -20.357 -3.616   1.00 104.70 ? 302  ASP   A HB3  1 
ATOM   4576  N  N    . ARG   A  1  303 ? 30.567  -22.687 -1.704   1.00 81.03  ? 303  ARG   A N    1 
ATOM   4577  C  CA   . ARG   A  1  303 ? 30.735  -22.784 -0.261   1.00 79.20  ? 303  ARG   A CA   1 
ATOM   4578  C  C    . ARG   A  1  303 ? 31.134  -21.419 0.287    1.00 79.09  ? 303  ARG   A C    1 
ATOM   4579  O  O    . ARG   A  1  303 ? 31.969  -20.725 -0.299   1.00 80.29  ? 303  ARG   A O    1 
ATOM   4580  C  CB   . ARG   A  1  303 ? 31.791  -23.831 0.094    1.00 80.48  ? 303  ARG   A CB   1 
ATOM   4581  C  CG   . ARG   A  1  303 ? 31.738  -24.315 1.533    1.00 88.45  ? 303  ARG   A CG   1 
ATOM   4582  C  CD   . ARG   A  1  303 ? 30.565  -25.257 1.777    1.00 91.51  ? 303  ARG   A CD   1 
ATOM   4583  N  NE   . ARG   A  1  303 ? 30.683  -26.510 1.035    1.00 90.82  ? 303  ARG   A NE   1 
ATOM   4584  C  CZ   . ARG   A  1  303 ? 29.981  -27.608 1.304    1.00 92.08  ? 303  ARG   A CZ   1 
ATOM   4585  N  NH1  . ARG   A  1  303 ? 29.110  -27.620 2.305    1.00 93.44  ? 303  ARG   A NH1  1 
ATOM   4586  N  NH2  . ARG   A  1  303 ? 30.156  -28.702 0.574    1.00 90.26  ? 303  ARG   A NH2  1 
ATOM   4587  H  H    . ARG   A  1  303 ? 31.311  -22.687 -2.136   1.00 97.27  ? 303  ARG   A H    1 
ATOM   4588  H  HA   . ARG   A  1  303 ? 29.901  -23.053 0.157    1.00 95.08  ? 303  ARG   A HA   1 
ATOM   4589  H  HB2  . ARG   A  1  303 ? 31.666  -24.603 -0.480   1.00 96.62  ? 303  ARG   A HB2  1 
ATOM   4590  H  HB3  . ARG   A  1  303 ? 32.669  -23.447 -0.054   1.00 96.62  ? 303  ARG   A HB3  1 
ATOM   4591  H  HG2  . ARG   A  1  303 ? 32.557  -24.792 1.740    1.00 106.17 ? 303  ARG   A HG2  1 
ATOM   4592  H  HG3  . ARG   A  1  303 ? 31.640  -23.552 2.123    1.00 106.17 ? 303  ARG   A HG3  1 
ATOM   4593  H  HD2  . ARG   A  1  303 ? 30.523  -25.471 2.722    1.00 109.85 ? 303  ARG   A HD2  1 
ATOM   4594  H  HD3  . ARG   A  1  303 ? 29.745  -24.820 1.499    1.00 109.85 ? 303  ARG   A HD3  1 
ATOM   4595  H  HE   . ARG   A  1  303 ? 31.242  -26.539 0.382    1.00 109.02 ? 303  ARG   A HE   1 
ATOM   4596  H  HH11 . ARG   A  1  303 ? 28.997  -26.915 2.785    1.00 112.16 ? 303  ARG   A HH11 1 
ATOM   4597  H  HH12 . ARG   A  1  303 ? 28.660  -28.333 2.475    1.00 112.16 ? 303  ARG   A HH12 1 
ATOM   4598  H  HH21 . ARG   A  1  303 ? 30.722  -28.701 -0.073   1.00 108.35 ? 303  ARG   A HH21 1 
ATOM   4599  H  HH22 . ARG   A  1  303 ? 29.702  -29.411 0.748    1.00 108.35 ? 303  ARG   A HH22 1 
ATOM   4600  N  N    . GLY   A  1  304 ? 30.528  -21.035 1.413    1.00 83.19  ? 304  GLY   A N    1 
ATOM   4601  C  CA   . GLY   A  1  304 ? 30.724  -19.722 1.983    1.00 85.42  ? 304  GLY   A CA   1 
ATOM   4602  C  C    . GLY   A  1  304 ? 31.713  -19.714 3.141    1.00 87.28  ? 304  GLY   A C    1 
ATOM   4603  O  O    . GLY   A  1  304 ? 32.217  -20.741 3.588    1.00 86.91  ? 304  GLY   A O    1 
ATOM   4604  H  H    . GLY   A  1  304 ? 29.991  -21.533 1.864    1.00 99.86  ? 304  GLY   A H    1 
ATOM   4605  H  HA2  . GLY   A  1  304 ? 31.058  -19.124 1.296    1.00 102.54 ? 304  GLY   A HA2  1 
ATOM   4606  H  HA3  . GLY   A  1  304 ? 29.874  -19.387 2.308    1.00 102.54 ? 304  GLY   A HA3  1 
ATOM   4607  N  N    . SER   A  1  305 ? 31.987  -18.499 3.625    1.00 88.29  ? 305  SER   A N    1 
ATOM   4608  C  CA   . SER   A  1  305 ? 32.874  -18.338 4.772    1.00 88.89  ? 305  SER   A CA   1 
ATOM   4609  C  C    . SER   A  1  305 ? 32.399  -19.169 5.955    1.00 89.78  ? 305  SER   A C    1 
ATOM   4610  O  O    . SER   A  1  305 ? 33.211  -19.714 6.712    1.00 93.49  ? 305  SER   A O    1 
ATOM   4611  C  CB   . SER   A  1  305 ? 32.962  -16.860 5.158    1.00 90.10  ? 305  SER   A CB   1 
ATOM   4612  O  OG   . SER   A  1  305 ? 33.576  -16.697 6.423    1.00 97.15  ? 305  SER   A OG   1 
ATOM   4613  H  H    . SER   A  1  305 ? 31.674  -17.762 3.309    1.00 105.99 ? 305  SER   A H    1 
ATOM   4614  H  HA   . SER   A  1  305 ? 33.764  -18.639 4.528    1.00 106.71 ? 305  SER   A HA   1 
ATOM   4615  H  HB2  . SER   A  1  305 ? 33.487  -16.392 4.490    1.00 108.15 ? 305  SER   A HB2  1 
ATOM   4616  H  HB3  . SER   A  1  305 ? 32.065  -16.491 5.194    1.00 108.15 ? 305  SER   A HB3  1 
ATOM   4617  H  HG   . SER   A  1  305 ? 33.053  -16.947 7.031    1.00 116.61 ? 305  SER   A HG   1 
ATOM   4618  N  N    . ASP   A  1  306 ? 31.083  -19.274 6.130    1.00 89.45  ? 306  ASP   A N    1 
ATOM   4619  C  CA   . ASP   A  1  306 ? 30.495  -20.085 7.186    1.00 90.28  ? 306  ASP   A CA   1 
ATOM   4620  C  C    . ASP   A  1  306 ? 30.416  -21.562 6.824    1.00 87.89  ? 306  ASP   A C    1 
ATOM   4621  O  O    . ASP   A  1  306 ? 29.897  -22.351 7.621    1.00 87.98  ? 306  ASP   A O    1 
ATOM   4622  C  CB   . ASP   A  1  306 ? 29.093  -19.566 7.517    1.00 90.00  ? 306  ASP   A CB   1 
ATOM   4623  C  CG   . ASP   A  1  306 ? 28.228  -19.399 6.282    1.00 88.32  ? 306  ASP   A CG   1 
ATOM   4624  O  OD1  . ASP   A  1  306 ? 28.724  -19.673 5.170    1.00 89.23  ? 306  ASP   A OD1  1 
ATOM   4625  O  OD2  . ASP   A  1  306 ? 27.057  -18.989 6.422    1.00 89.44  ? 306  ASP   A OD2  1 
ATOM   4626  H  H    . ASP   A  1  306 ? 30.501  -18.875 5.639    1.00 107.38 ? 306  ASP   A H    1 
ATOM   4627  H  HA   . ASP   A  1  306 ? 31.043  -20.005 7.982    1.00 108.38 ? 306  ASP   A HA   1 
ATOM   4628  H  HB2  . ASP   A  1  306 ? 28.653  -20.195 8.110    1.00 108.03 ? 306  ASP   A HB2  1 
ATOM   4629  H  HB3  . ASP   A  1  306 ? 29.170  -18.701 7.950    1.00 108.03 ? 306  ASP   A HB3  1 
ATOM   4630  N  N    . GLY   A  1  307 ? 30.914  -21.955 5.654    1.00 89.98  ? 307  GLY   A N    1 
ATOM   4631  C  CA   . GLY   A  1  307 ? 30.850  -23.337 5.232    1.00 90.29  ? 307  GLY   A CA   1 
ATOM   4632  C  C    . GLY   A  1  307 ? 29.493  -23.792 4.754    1.00 90.73  ? 307  GLY   A C    1 
ATOM   4633  O  O    . GLY   A  1  307 ? 29.290  -24.998 4.570    1.00 88.18  ? 307  GLY   A O    1 
ATOM   4634  H  H    . GLY   A  1  307 ? 31.294  -21.431 5.087    1.00 108.01 ? 307  GLY   A H    1 
ATOM   4635  H  HA2  . GLY   A  1  307 ? 31.480  -23.470 4.506    1.00 108.38 ? 307  GLY   A HA2  1 
ATOM   4636  H  HA3  . GLY   A  1  307 ? 31.106  -23.902 5.979    1.00 108.38 ? 307  GLY   A HA3  1 
ATOM   4637  N  N    . LYS   A  1  308 ? 28.554  -22.873 4.555    1.00 90.53  ? 308  LYS   A N    1 
ATOM   4638  C  CA   . LYS   A  1  308 ? 27.228  -23.213 4.063    1.00 93.70  ? 308  LYS   A CA   1 
ATOM   4639  C  C    . LYS   A  1  308 ? 27.207  -23.149 2.542    1.00 88.48  ? 308  LYS   A C    1 
ATOM   4640  O  O    . LYS   A  1  308 ? 27.839  -22.278 1.936    1.00 88.21  ? 308  LYS   A O    1 
ATOM   4641  C  CB   . LYS   A  1  308 ? 26.182  -22.260 4.645    1.00 102.75 ? 308  LYS   A CB   1 
ATOM   4642  C  CG   . LYS   A  1  308 ? 24.752  -22.569 4.227    1.00 109.47 ? 308  LYS   A CG   1 
ATOM   4643  C  CD   . LYS   A  1  308 ? 23.762  -21.574 4.817    1.00 115.55 ? 308  LYS   A CD   1 
ATOM   4644  C  CE   . LYS   A  1  308 ? 22.344  -21.874 4.355    1.00 124.21 ? 308  LYS   A CE   1 
ATOM   4645  N  NZ   . LYS   A  1  308 ? 21.336  -20.934 4.923    1.00 129.01 ? 308  LYS   A NZ   1 
ATOM   4646  H  H    . LYS   A  1  308 ? 28.664  -22.033 4.701    1.00 108.67 ? 308  LYS   A H    1 
ATOM   4647  H  HA   . LYS   A  1  308 ? 26.999  -24.116 4.334    1.00 112.47 ? 308  LYS   A HA   1 
ATOM   4648  H  HB2  . LYS   A  1  308 ? 26.222  -22.310 5.613    1.00 123.34 ? 308  LYS   A HB2  1 
ATOM   4649  H  HB3  . LYS   A  1  308 ? 26.385  -21.359 4.349    1.00 123.34 ? 308  LYS   A HB3  1 
ATOM   4650  H  HG2  . LYS   A  1  308 ? 24.685  -22.528 3.260    1.00 131.40 ? 308  LYS   A HG2  1 
ATOM   4651  H  HG3  . LYS   A  1  308 ? 24.512  -23.456 4.538    1.00 131.40 ? 308  LYS   A HG3  1 
ATOM   4652  H  HD2  . LYS   A  1  308 ? 23.787  -21.628 5.785    1.00 138.70 ? 308  LYS   A HD2  1 
ATOM   4653  H  HD3  . LYS   A  1  308 ? 23.995  -20.677 4.529    1.00 138.70 ? 308  LYS   A HD3  1 
ATOM   4654  H  HE2  . LYS   A  1  308 ? 22.305  -21.804 3.388    1.00 149.09 ? 308  LYS   A HE2  1 
ATOM   4655  H  HE3  . LYS   A  1  308 ? 22.105  -22.772 4.632    1.00 149.09 ? 308  LYS   A HE3  1 
ATOM   4656  H  HZ1  . LYS   A  1  308 ? 20.525  -21.298 4.884    1.00 154.85 ? 308  LYS   A HZ1  1 
ATOM   4657  H  HZ2  . LYS   A  1  308 ? 21.532  -20.756 5.773    1.00 154.85 ? 308  LYS   A HZ2  1 
ATOM   4658  H  HZ3  . LYS   A  1  308 ? 21.335  -20.174 4.461    1.00 154.85 ? 308  LYS   A HZ3  1 
ATOM   4659  N  N    . LEU   A  1  309 ? 26.487  -24.084 1.928    1.00 81.33  ? 309  LEU   A N    1 
ATOM   4660  C  CA   . LEU   A  1  309 ? 26.281  -24.033 0.488    1.00 69.92  ? 309  LEU   A CA   1 
ATOM   4661  C  C    . LEU   A  1  309 ? 25.318  -22.907 0.139    1.00 64.95  ? 309  LEU   A C    1 
ATOM   4662  O  O    . LEU   A  1  309 ? 24.374  -22.622 0.880    1.00 61.47  ? 309  LEU   A O    1 
ATOM   4663  C  CB   . LEU   A  1  309 ? 25.729  -25.361 -0.028   1.00 65.26  ? 309  LEU   A CB   1 
ATOM   4664  C  CG   . LEU   A  1  309 ? 26.699  -26.525 -0.232   1.00 64.40  ? 309  LEU   A CG   1 
ATOM   4665  C  CD1  . LEU   A  1  309 ? 25.909  -27.786 -0.539   1.00 60.58  ? 309  LEU   A CD1  1 
ATOM   4666  C  CD2  . LEU   A  1  309 ? 27.692  -26.234 -1.349   1.00 64.35  ? 309  LEU   A CD2  1 
ATOM   4667  H  H    . LEU   A  1  309 ? 26.112  -24.751 2.320    1.00 97.64  ? 309  LEU   A H    1 
ATOM   4668  H  HA   . LEU   A  1  309 ? 27.131  -23.872 0.048    1.00 83.94  ? 309  LEU   A HA   1 
ATOM   4669  H  HB2  . LEU   A  1  309 ? 25.061  -25.666 0.606    1.00 78.35  ? 309  LEU   A HB2  1 
ATOM   4670  H  HB3  . LEU   A  1  309 ? 25.316  -25.191 -0.889   1.00 78.35  ? 309  LEU   A HB3  1 
ATOM   4671  H  HG   . LEU   A  1  309 ? 27.214  -26.658 0.579    1.00 77.31  ? 309  LEU   A HG   1 
ATOM   4672  H  HD11 . LEU   A  1  309 ? 26.528  -28.517 -0.695   1.00 72.73  ? 309  LEU   A HD11 1 
ATOM   4673  H  HD12 . LEU   A  1  309 ? 25.337  -27.992 0.217    1.00 72.73  ? 309  LEU   A HD12 1 
ATOM   4674  H  HD13 . LEU   A  1  309 ? 25.369  -27.636 -1.331   1.00 72.73  ? 309  LEU   A HD13 1 
ATOM   4675  H  HD21 . LEU   A  1  309 ? 28.273  -27.003 -1.463   1.00 77.26  ? 309  LEU   A HD21 1 
ATOM   4676  H  HD22 . LEU   A  1  309 ? 27.204  -26.064 -2.170   1.00 77.26  ? 309  LEU   A HD22 1 
ATOM   4677  H  HD23 . LEU   A  1  309 ? 28.217  -25.455 -1.109   1.00 77.26  ? 309  LEU   A HD23 1 
ATOM   4678  N  N    . GLN   A  1  310 ? 25.560  -22.265 -1.001   1.00 68.82  ? 310  GLN   A N    1 
ATOM   4679  C  CA   . GLN   A  1  310 ? 24.685  -21.198 -1.474   1.00 72.11  ? 310  GLN   A CA   1 
ATOM   4680  C  C    . GLN   A  1  310 ? 24.632  -21.252 -2.991   1.00 68.57  ? 310  GLN   A C    1 
ATOM   4681  O  O    . GLN   A  1  310 ? 25.662  -21.111 -3.656   1.00 68.97  ? 310  GLN   A O    1 
ATOM   4682  C  CB   . GLN   A  1  310 ? 25.165  -19.826 -0.990   1.00 78.96  ? 310  GLN   A CB   1 
ATOM   4683  C  CG   . GLN   A  1  310 ? 26.677  -19.655 -0.928   1.00 88.16  ? 310  GLN   A CG   1 
ATOM   4684  C  CD   . GLN   A  1  310 ? 27.081  -18.396 -0.184   1.00 98.93  ? 310  GLN   A CD   1 
ATOM   4685  O  OE1  . GLN   A  1  310 ? 26.336  -17.894 0.658    1.00 104.20 ? 310  GLN   A OE1  1 
ATOM   4686  N  NE2  . GLN   A  1  310 ? 28.264  -17.880 -0.491   1.00 104.84 ? 310  GLN   A NE2  1 
ATOM   4687  H  H    . GLN   A  1  310 ? 26.226  -22.430 -1.519   1.00 82.62  ? 310  GLN   A H    1 
ATOM   4688  H  HA   . GLN   A  1  310 ? 23.789  -21.342 -1.132   1.00 86.57  ? 310  GLN   A HA   1 
ATOM   4689  H  HB2  . GLN   A  1  310 ? 24.821  -19.150 -1.595   1.00 94.79  ? 310  GLN   A HB2  1 
ATOM   4690  H  HB3  . GLN   A  1  310 ? 24.820  -19.678 -0.096   1.00 94.79  ? 310  GLN   A HB3  1 
ATOM   4691  H  HG2  . GLN   A  1  310 ? 27.065  -20.416 -0.469   1.00 105.82 ? 310  GLN   A HG2  1 
ATOM   4692  H  HG3  . GLN   A  1  310 ? 27.028  -19.598 -1.831   1.00 105.82 ? 310  GLN   A HG3  1 
ATOM   4693  H  HE21 . GLN   A  1  310 ? 28.758  -18.259 -1.086   1.00 125.85 ? 310  GLN   A HE21 1 
ATOM   4694  H  HE22 . GLN   A  1  310 ? 28.538  -17.167 -0.096   1.00 125.85 ? 310  GLN   A HE22 1 
ATOM   4695  N  N    . GLU   A  1  311 ? 23.434  -21.468 -3.528   1.00 63.83  ? 311  GLU   A N    1 
ATOM   4696  C  CA   . GLU   A  1  311 ? 23.237  -21.492 -4.971   1.00 59.76  ? 311  GLU   A CA   1 
ATOM   4697  C  C    . GLU   A  1  311 ? 23.471  -20.100 -5.541   1.00 56.93  ? 311  GLU   A C    1 
ATOM   4698  O  O    . GLU   A  1  311 ? 22.735  -19.162 -5.219   1.00 54.89  ? 311  GLU   A O    1 
ATOM   4699  C  CB   . GLU   A  1  311 ? 21.827  -21.979 -5.292   1.00 57.99  ? 311  GLU   A CB   1 
ATOM   4700  C  CG   . GLU   A  1  311 ? 21.506  -22.071 -6.773   1.00 57.00  ? 311  GLU   A CG   1 
ATOM   4701  C  CD   . GLU   A  1  311 ? 20.125  -22.644 -7.026   1.00 59.45  ? 311  GLU   A CD   1 
ATOM   4702  O  OE1  . GLU   A  1  311 ? 19.904  -23.829 -6.696   1.00 60.50  ? 311  GLU   A OE1  1 
ATOM   4703  O  OE2  . GLU   A  1  311 ? 19.259  -21.906 -7.540   1.00 58.98  ? 311  GLU   A OE2  1 
ATOM   4704  H  H    . GLU   A  1  311 ? 22.716  -21.604 -3.075   1.00 76.63  ? 311  GLU   A H    1 
ATOM   4705  H  HA   . GLU   A  1  311 ? 23.870  -22.102 -5.381   1.00 71.75  ? 311  GLU   A HA   1 
ATOM   4706  H  HB2  . GLU   A  1  311 ? 21.714  -22.865 -4.914   1.00 69.63  ? 311  GLU   A HB2  1 
ATOM   4707  H  HB3  . GLU   A  1  311 ? 21.191  -21.365 -4.894   1.00 69.63  ? 311  GLU   A HB3  1 
ATOM   4708  H  HG2  . GLU   A  1  311 ? 21.541  -21.183 -7.161   1.00 68.44  ? 311  GLU   A HG2  1 
ATOM   4709  H  HG3  . GLU   A  1  311 ? 22.156  -22.648 -7.204   1.00 68.44  ? 311  GLU   A HG3  1 
ATOM   4710  N  N    . VAL   A  1  312 ? 24.495  -19.962 -6.382   1.00 54.09  ? 312  VAL   A N    1 
ATOM   4711  C  CA   . VAL   A  1  312 ? 24.838  -18.668 -6.962   1.00 53.66  ? 312  VAL   A CA   1 
ATOM   4712  C  C    . VAL   A  1  312 ? 25.086  -18.803 -8.458   1.00 50.81  ? 312  VAL   A C    1 
ATOM   4713  O  O    . VAL   A  1  312 ? 25.177  -17.799 -9.172   1.00 51.89  ? 312  VAL   A O    1 
ATOM   4714  C  CB   . VAL   A  1  312 ? 26.069  -18.057 -6.265   1.00 58.87  ? 312  VAL   A CB   1 
ATOM   4715  C  CG1  . VAL   A  1  312 ? 25.753  -17.745 -4.812   1.00 58.60  ? 312  VAL   A CG1  1 
ATOM   4716  C  CG2  . VAL   A  1  312 ? 27.269  -18.994 -6.371   1.00 59.99  ? 312  VAL   A CG2  1 
ATOM   4717  H  H    . VAL   A  1  312 ? 25.007  -20.606 -6.633   1.00 64.95  ? 312  VAL   A H    1 
ATOM   4718  H  HA   . VAL   A  1  312 ? 24.079  -18.077 -6.841   1.00 64.42  ? 312  VAL   A HA   1 
ATOM   4719  H  HB   . VAL   A  1  312 ? 26.302  -17.226 -6.708   1.00 70.68  ? 312  VAL   A HB   1 
ATOM   4720  H  HG11 . VAL   A  1  312 ? 26.531  -17.337 -4.401   1.00 70.35  ? 312  VAL   A HG11 1 
ATOM   4721  H  HG12 . VAL   A  1  312 ? 25.001  -17.134 -4.777   1.00 70.35  ? 312  VAL   A HG12 1 
ATOM   4722  H  HG13 . VAL   A  1  312 ? 25.531  -18.570 -4.353   1.00 70.35  ? 312  VAL   A HG13 1 
ATOM   4723  H  HG21 . VAL   A  1  312 ? 28.030  -18.584 -5.932   1.00 72.03  ? 312  VAL   A HG21 1 
ATOM   4724  H  HG22 . VAL   A  1  312 ? 27.052  -19.835 -5.939   1.00 72.03  ? 312  VAL   A HG22 1 
ATOM   4725  H  HG23 . VAL   A  1  312 ? 27.469  -19.146 -7.308   1.00 72.03  ? 312  VAL   A HG23 1 
ATOM   4726  N  N    . GLY   A  1  313 ? 25.194  -20.034 -8.946   1.00 51.37  ? 313  GLY   A N    1 
ATOM   4727  C  CA   . GLY   A  1  313 ? 25.526  -20.270 -10.333  1.00 50.88  ? 313  GLY   A CA   1 
ATOM   4728  C  C    . GLY   A  1  313 ? 27.013  -20.119 -10.596  1.00 50.87  ? 313  GLY   A C    1 
ATOM   4729  O  O    . GLY   A  1  313 ? 27.786  -19.630 -9.771   1.00 49.95  ? 313  GLY   A O    1 
ATOM   4730  H  H    . GLY   A  1  313 ? 25.077  -20.751 -8.485   1.00 61.68  ? 313  GLY   A H    1 
ATOM   4731  H  HA2  . GLY   A  1  313 ? 25.260  -21.170 -10.580  1.00 61.09  ? 313  GLY   A HA2  1 
ATOM   4732  H  HA3  . GLY   A  1  313 ? 25.049  -19.636 -10.892  1.00 61.09  ? 313  GLY   A HA3  1 
ATOM   4733  N  N    . GLN   A  1  314 ? 27.417  -20.551 -11.788  1.00 52.16  ? 314  GLN   A N    1 
ATOM   4734  C  CA   . GLN   A  1  314 ? 28.825  -20.574 -12.150  1.00 53.89  ? 314  GLN   A CA   1 
ATOM   4735  C  C    . GLN   A  1  314 ? 28.946  -20.686 -13.662  1.00 56.97  ? 314  GLN   A C    1 
ATOM   4736  O  O    . GLN   A  1  314 ? 28.177  -21.410 -14.299  1.00 59.20  ? 314  GLN   A O    1 
ATOM   4737  C  CB   . GLN   A  1  314 ? 29.546  -21.741 -11.466  1.00 54.75  ? 314  GLN   A CB   1 
ATOM   4738  C  CG   . GLN   A  1  314 ? 30.971  -21.971 -11.937  1.00 55.48  ? 314  GLN   A CG   1 
ATOM   4739  C  CD   . GLN   A  1  314 ? 31.642  -23.112 -11.199  1.00 57.87  ? 314  GLN   A CD   1 
ATOM   4740  O  OE1  . GLN   A  1  314 ? 31.537  -24.271 -11.598  1.00 59.54  ? 314  GLN   A OE1  1 
ATOM   4741  N  NE2  . GLN   A  1  314 ? 32.330  -22.788 -10.111  1.00 57.87  ? 314  GLN   A NE2  1 
ATOM   4742  H  H    . GLN   A  1  314 ? 26.890  -20.838 -12.404  1.00 62.63  ? 314  GLN   A H    1 
ATOM   4743  H  HA   . GLN   A  1  314 ? 29.248  -19.745 -11.877  1.00 64.70  ? 314  GLN   A HA   1 
ATOM   4744  H  HB2  . GLN   A  1  314 ? 29.578  -21.568 -10.512  1.00 65.74  ? 314  GLN   A HB2  1 
ATOM   4745  H  HB3  . GLN   A  1  314 ? 29.047  -22.555 -11.639  1.00 65.74  ? 314  GLN   A HB3  1 
ATOM   4746  H  HG2  . GLN   A  1  314 ? 30.963  -22.186 -12.882  1.00 66.62  ? 314  GLN   A HG2  1 
ATOM   4747  H  HG3  . GLN   A  1  314 ? 31.490  -21.166 -11.784  1.00 66.62  ? 314  GLN   A HG3  1 
ATOM   4748  H  HE21 . GLN   A  1  314 ? 32.376  -21.967 -9.861   1.00 69.48  ? 314  GLN   A HE21 1 
ATOM   4749  H  HE22 . GLN   A  1  314 ? 32.729  -23.400 -9.657   1.00 69.48  ? 314  GLN   A HE22 1 
ATOM   4750  N  N    . VAL   A  1  315 ? 29.915  -19.968 -14.224  1.00 57.90  ? 315  VAL   A N    1 
ATOM   4751  C  CA   . VAL   A  1  315 ? 30.228  -20.023 -15.646  1.00 54.67  ? 315  VAL   A CA   1 
ATOM   4752  C  C    . VAL   A  1  315 ? 31.658  -20.519 -15.802  1.00 57.56  ? 315  VAL   A C    1 
ATOM   4753  O  O    . VAL   A  1  315 ? 32.550  -20.114 -15.047  1.00 58.45  ? 315  VAL   A O    1 
ATOM   4754  C  CB   . VAL   A  1  315 ? 30.050  -18.650 -16.327  1.00 57.31  ? 315  VAL   A CB   1 
ATOM   4755  C  CG1  . VAL   A  1  315 ? 30.601  -18.680 -17.748  1.00 56.94  ? 315  VAL   A CG1  1 
ATOM   4756  C  CG2  . VAL   A  1  315 ? 28.584  -18.245 -16.330  1.00 60.92  ? 315  VAL   A CG2  1 
ATOM   4757  H  H    . VAL   A  1  315 ? 30.419  -19.425 -13.787  1.00 69.52  ? 315  VAL   A H    1 
ATOM   4758  H  HA   . VAL   A  1  315 ? 29.631  -20.653 -16.080  1.00 65.64  ? 315  VAL   A HA   1 
ATOM   4759  H  HB   . VAL   A  1  315 ? 30.548  -17.986 -15.825  1.00 68.81  ? 315  VAL   A HB   1 
ATOM   4760  H  HG11 . VAL   A  1  315 ? 30.398  -17.837 -18.183  1.00 68.37  ? 315  VAL   A HG11 1 
ATOM   4761  H  HG12 . VAL   A  1  315 ? 31.562  -18.809 -17.712  1.00 68.37  ? 315  VAL   A HG12 1 
ATOM   4762  H  HG13 . VAL   A  1  315 ? 30.187  -19.411 -18.232  1.00 68.37  ? 315  VAL   A HG13 1 
ATOM   4763  H  HG21 . VAL   A  1  315 ? 28.495  -17.384 -16.767  1.00 73.15  ? 315  VAL   A HG21 1 
ATOM   4764  H  HG22 . VAL   A  1  315 ? 28.073  -18.915 -16.812  1.00 73.15  ? 315  VAL   A HG22 1 
ATOM   4765  H  HG23 . VAL   A  1  315 ? 28.270  -18.186 -15.414  1.00 73.15  ? 315  VAL   A HG23 1 
ATOM   4766  N  N    . SER   A  1  316 ? 31.874  -21.390 -16.783  1.00 56.11  ? 316  SER   A N    1 
ATOM   4767  C  CA   . SER   A  1  316 ? 33.194  -21.926 -17.081  1.00 54.63  ? 316  SER   A CA   1 
ATOM   4768  C  C    . SER   A  1  316 ? 33.689  -21.356 -18.403  1.00 52.26  ? 316  SER   A C    1 
ATOM   4769  O  O    . SER   A  1  316 ? 32.943  -21.299 -19.385  1.00 53.43  ? 316  SER   A O    1 
ATOM   4770  C  CB   . SER   A  1  316 ? 33.170  -23.455 -17.146  1.00 58.32  ? 316  SER   A CB   1 
ATOM   4771  O  OG   . SER   A  1  316 ? 32.609  -23.907 -18.366  1.00 65.35  ? 316  SER   A OG   1 
ATOM   4772  H  H    . SER   A  1  316 ? 31.256  -21.691 -17.300  1.00 67.37  ? 316  SER   A H    1 
ATOM   4773  H  HA   . SER   A  1  316 ? 33.815  -21.667 -16.383  1.00 65.60  ? 316  SER   A HA   1 
ATOM   4774  H  HB2  . SER   A  1  316 ? 34.078  -23.787 -17.076  1.00 70.02  ? 316  SER   A HB2  1 
ATOM   4775  H  HB3  . SER   A  1  316 ? 32.635  -23.792 -16.411  1.00 70.02  ? 316  SER   A HB3  1 
ATOM   4776  H  HG   . SER   A  1  316 ? 32.425  -24.724 -18.312  1.00 78.46  ? 316  SER   A HG   1 
ATOM   4777  N  N    . VAL   A  1  317 ? 34.951  -20.938 -18.418  1.00 52.97  ? 317  VAL   A N    1 
ATOM   4778  C  CA   . VAL   A  1  317 ? 35.571  -20.288 -19.566  1.00 49.56  ? 317  VAL   A CA   1 
ATOM   4779  C  C    . VAL   A  1  317 ? 36.713  -21.180 -20.029  1.00 52.44  ? 317  VAL   A C    1 
ATOM   4780  O  O    . VAL   A  1  317 ? 37.693  -21.366 -19.297  1.00 57.31  ? 317  VAL   A O    1 
ATOM   4781  C  CB   . VAL   A  1  317 ? 36.078  -18.879 -19.214  1.00 48.74  ? 317  VAL   A CB   1 
ATOM   4782  C  CG1  . VAL   A  1  317 ? 36.637  -18.185 -20.446  1.00 51.95  ? 317  VAL   A CG1  1 
ATOM   4783  C  CG2  . VAL   A  1  317 ? 34.962  -18.054 -18.583  1.00 46.02  ? 317  VAL   A CG2  1 
ATOM   4784  H  H    . VAL   A  1  317 ? 35.486  -21.024 -17.750  1.00 63.61  ? 317  VAL   A H    1 
ATOM   4785  H  HA   . VAL   A  1  317 ? 34.928  -20.208 -20.288  1.00 59.51  ? 317  VAL   A HA   1 
ATOM   4786  H  HB   . VAL   A  1  317 ? 36.797  -18.957 -18.567  1.00 58.53  ? 317  VAL   A HB   1 
ATOM   4787  H  HG11 . VAL   A  1  317 ? 36.945  -17.299 -20.197  1.00 62.37  ? 317  VAL   A HG11 1 
ATOM   4788  H  HG12 . VAL   A  1  317 ? 37.377  -18.706 -20.794  1.00 62.37  ? 317  VAL   A HG12 1 
ATOM   4789  H  HG13 . VAL   A  1  317 ? 35.938  -18.116 -21.114  1.00 62.37  ? 317  VAL   A HG13 1 
ATOM   4790  H  HG21 . VAL   A  1  317 ? 35.304  -17.172 -18.369  1.00 55.27  ? 317  VAL   A HG21 1 
ATOM   4791  H  HG22 . VAL   A  1  317 ? 34.229  -17.980 -19.213  1.00 55.27  ? 317  VAL   A HG22 1 
ATOM   4792  H  HG23 . VAL   A  1  317 ? 34.661  -18.496 -17.774  1.00 55.27  ? 317  VAL   A HG23 1 
ATOM   4793  N  N    . SER   A  1  318 ? 36.593  -21.725 -21.237  1.00 54.41  ? 318  SER   A N    1 
ATOM   4794  C  CA   . SER   A  1  318 ? 37.555  -22.690 -21.768  1.00 60.66  ? 318  SER   A CA   1 
ATOM   4795  C  C    . SER   A  1  318 ? 38.213  -22.100 -23.012  1.00 60.02  ? 318  SER   A C    1 
ATOM   4796  O  O    . SER   A  1  318 ? 37.636  -22.130 -24.104  1.00 57.06  ? 318  SER   A O    1 
ATOM   4797  C  CB   . SER   A  1  318 ? 36.872  -24.017 -22.083  1.00 63.37  ? 318  SER   A CB   1 
ATOM   4798  O  OG   . SER   A  1  318 ? 36.039  -24.422 -21.011  1.00 68.69  ? 318  SER   A OG   1 
ATOM   4799  H  H    . SER   A  1  318 ? 35.950  -21.548 -21.780  1.00 65.33  ? 318  SER   A H    1 
ATOM   4800  H  HA   . SER   A  1  318 ? 38.249  -22.839 -21.106  1.00 72.83  ? 318  SER   A HA   1 
ATOM   4801  H  HB2  . SER   A  1  318 ? 36.330  -23.912 -22.881  1.00 76.08  ? 318  SER   A HB2  1 
ATOM   4802  H  HB3  . SER   A  1  318 ? 37.550  -24.695 -22.229  1.00 76.08  ? 318  SER   A HB3  1 
ATOM   4803  H  HG   . SER   A  1  318 ? 35.803  -25.221 -21.117  1.00 82.47  ? 318  SER   A HG   1 
ATOM   4804  N  N    . LEU   A  1  319 ? 39.423  -21.573 -22.845  1.00 63.42  ? 319  LEU   A N    1 
ATOM   4805  C  CA   . LEU   A  1  319 ? 40.172  -21.019 -23.966  1.00 64.20  ? 319  LEU   A CA   1 
ATOM   4806  C  C    . LEU   A  1  319 ? 40.687  -22.144 -24.854  1.00 65.95  ? 319  LEU   A C    1 
ATOM   4807  O  O    . LEU   A  1  319 ? 41.388  -23.046 -24.382  1.00 68.84  ? 319  LEU   A O    1 
ATOM   4808  C  CB   . LEU   A  1  319 ? 41.333  -20.173 -23.454  1.00 64.08  ? 319  LEU   A CB   1 
ATOM   4809  C  CG   . LEU   A  1  319 ? 41.032  -18.728 -23.054  1.00 61.58  ? 319  LEU   A CG   1 
ATOM   4810  C  CD1  . LEU   A  1  319 ? 39.716  -18.604 -22.302  1.00 62.51  ? 319  LEU   A CD1  1 
ATOM   4811  C  CD2  . LEU   A  1  319 ? 42.182  -18.208 -22.212  1.00 60.70  ? 319  LEU   A CD2  1 
ATOM   4812  H  H    . LEU   A  1  319 ? 39.832  -21.524 -22.091  1.00 76.14  ? 319  LEU   A H    1 
ATOM   4813  H  HA   . LEU   A  1  319 ? 39.586  -20.452 -24.492  1.00 77.08  ? 319  LEU   A HA   1 
ATOM   4814  H  HB2  . LEU   A  1  319 ? 41.696  -20.611 -22.668  1.00 76.93  ? 319  LEU   A HB2  1 
ATOM   4815  H  HB3  . LEU   A  1  319 ? 42.004  -20.136 -24.153  1.00 76.93  ? 319  LEU   A HB3  1 
ATOM   4816  H  HG   . LEU   A  1  319 ? 40.939  -18.188 -23.855  1.00 73.93  ? 319  LEU   A HG   1 
ATOM   4817  H  HD11 . LEU   A  1  319 ? 39.580  -17.676 -22.054  1.00 75.05  ? 319  LEU   A HD11 1 
ATOM   4818  H  HD12 . LEU   A  1  319 ? 38.994  -18.902 -22.877  1.00 75.05  ? 319  LEU   A HD12 1 
ATOM   4819  H  HD13 . LEU   A  1  319 ? 39.754  -19.157 -21.506  1.00 75.05  ? 319  LEU   A HD13 1 
ATOM   4820  H  HD21 . LEU   A  1  319 ? 41.982  -17.302 -21.930  1.00 72.88  ? 319  LEU   A HD21 1 
ATOM   4821  H  HD22 . LEU   A  1  319 ? 42.289  -18.780 -21.436  1.00 72.88  ? 319  LEU   A HD22 1 
ATOM   4822  H  HD23 . LEU   A  1  319 ? 42.993  -18.218 -22.744  1.00 72.88  ? 319  LEU   A HD23 1 
ATOM   4823  N  N    . GLN   A  1  320 ? 40.344  -22.089 -26.137  1.00 61.73  ? 320  GLN   A N    1 
ATOM   4824  C  CA   . GLN   A  1  320 ? 40.852  -23.071 -27.083  1.00 61.71  ? 320  GLN   A CA   1 
ATOM   4825  C  C    . GLN   A  1  320 ? 42.324  -22.810 -27.372  1.00 67.78  ? 320  GLN   A C    1 
ATOM   4826  O  O    . GLN   A  1  320 ? 42.758  -21.661 -27.490  1.00 68.46  ? 320  GLN   A O    1 
ATOM   4827  C  CB   . GLN   A  1  320 ? 40.049  -23.026 -28.381  1.00 54.94  ? 320  GLN   A CB   1 
ATOM   4828  C  CG   . GLN   A  1  320 ? 40.588  -23.936 -29.477  1.00 55.48  ? 320  GLN   A CG   1 
ATOM   4829  C  CD   . GLN   A  1  320 ? 39.768  -23.899 -30.759  1.00 54.10  ? 320  GLN   A CD   1 
ATOM   4830  O  OE1  . GLN   A  1  320 ? 39.996  -24.699 -31.665  1.00 57.56  ? 320  GLN   A OE1  1 
ATOM   4831  N  NE2  . GLN   A  1  320 ? 38.818  -22.970 -30.845  1.00 50.96  ? 320  GLN   A NE2  1 
ATOM   4832  H  H    . GLN   A  1  320 ? 39.823  -21.498 -26.481  1.00 74.11  ? 320  GLN   A H    1 
ATOM   4833  H  HA   . GLN   A  1  320 ? 40.763  -23.960 -26.705  1.00 74.08  ? 320  GLN   A HA   1 
ATOM   4834  H  HB2  . GLN   A  1  320 ? 39.138  -23.300 -28.192  1.00 65.97  ? 320  GLN   A HB2  1 
ATOM   4835  H  HB3  . GLN   A  1  320 ? 40.059  -22.117 -28.721  1.00 65.97  ? 320  GLN   A HB3  1 
ATOM   4836  H  HG2  . GLN   A  1  320 ? 41.492  -23.661 -29.696  1.00 66.61  ? 320  GLN   A HG2  1 
ATOM   4837  H  HG3  . GLN   A  1  320 ? 40.589  -24.850 -29.153  1.00 66.61  ? 320  GLN   A HG3  1 
ATOM   4838  H  HE21 . GLN   A  1  320 ? 38.690  -22.424 -30.192  1.00 61.19  ? 320  GLN   A HE21 1 
ATOM   4839  H  HE22 . GLN   A  1  320 ? 38.332  -22.915 -31.552  1.00 61.19  ? 320  GLN   A HE22 1 
ATOM   4840  N  N    . ARG   A  1  321 ? 43.092  -23.888 -27.490  1.00 73.68  ? 321  ARG   A N    1 
ATOM   4841  C  CA   . ARG   A  1  321 ? 44.506  -23.814 -27.818  1.00 81.22  ? 321  ARG   A CA   1 
ATOM   4842  C  C    . ARG   A  1  321 ? 44.776  -24.623 -29.080  1.00 81.45  ? 321  ARG   A C    1 
ATOM   4843  O  O    . ARG   A  1  321 ? 44.074  -25.595 -29.376  1.00 82.38  ? 321  ARG   A O    1 
ATOM   4844  C  CB   . ARG   A  1  321 ? 45.371  -24.322 -26.657  1.00 87.67  ? 321  ARG   A CB   1 
ATOM   4845  C  CG   . ARG   A  1  321 ? 45.041  -23.661 -25.323  1.00 93.63  ? 321  ARG   A CG   1 
ATOM   4846  C  CD   . ARG   A  1  321 ? 46.210  -23.723 -24.355  1.00 100.15 ? 321  ARG   A CD   1 
ATOM   4847  N  NE   . ARG   A  1  321 ? 46.707  -25.083 -24.180  1.00 102.80 ? 321  ARG   A NE   1 
ATOM   4848  C  CZ   . ARG   A  1  321 ? 47.778  -25.401 -23.460  1.00 104.92 ? 321  ARG   A CZ   1 
ATOM   4849  N  NH1  . ARG   A  1  321 ? 48.153  -26.667 -23.361  1.00 106.03 ? 321  ARG   A NH1  1 
ATOM   4850  N  NH2  . ARG   A  1  321 ? 48.476  -24.458 -22.842  1.00 107.66 ? 321  ARG   A NH2  1 
ATOM   4851  H  H    . ARG   A  1  321 ? 42.807  -24.693 -27.380  1.00 88.46  ? 321  ARG   A H    1 
ATOM   4852  H  HA   . ARG   A  1  321 ? 44.762  -22.894 -27.993  1.00 97.50  ? 321  ARG   A HA   1 
ATOM   4853  H  HB2  . ARG   A  1  321 ? 45.232  -25.277 -26.558  1.00 105.25 ? 321  ARG   A HB2  1 
ATOM   4854  H  HB3  . ARG   A  1  321 ? 46.302  -24.141 -26.857  1.00 105.25 ? 321  ARG   A HB3  1 
ATOM   4855  H  HG2  . ARG   A  1  321 ? 44.823  -22.728 -25.475  1.00 112.39 ? 321  ARG   A HG2  1 
ATOM   4856  H  HG3  . ARG   A  1  321 ? 44.287  -24.117 -24.918  1.00 112.39 ? 321  ARG   A HG3  1 
ATOM   4857  H  HD2  . ARG   A  1  321 ? 46.935  -23.177 -24.696  1.00 120.22 ? 321  ARG   A HD2  1 
ATOM   4858  H  HD3  . ARG   A  1  321 ? 45.924  -23.392 -23.489  1.00 120.22 ? 321  ARG   A HD3  1 
ATOM   4859  H  HE   . ARG   A  1  321 ? 46.279  -25.720 -24.567  1.00 123.40 ? 321  ARG   A HE   1 
ATOM   4860  H  HH11 . ARG   A  1  321 ? 47.703  -27.282 -23.761  1.00 127.28 ? 321  ARG   A HH11 1 
ATOM   4861  H  HH12 . ARG   A  1  321 ? 48.845  -26.876 -22.895  1.00 127.28 ? 321  ARG   A HH12 1 
ATOM   4862  H  HH21 . ARG   A  1  321 ? 48.237  -23.634 -22.905  1.00 129.23 ? 321  ARG   A HH21 1 
ATOM   4863  H  HH22 . ARG   A  1  321 ? 49.168  -24.670 -22.377  1.00 129.23 ? 321  ARG   A HH22 1 
ATOM   4864  N  N    . ALA   A  1  322 ? 45.799  -24.203 -29.829  1.00 84.20  ? 322  ALA   A N    1 
ATOM   4865  C  CA   . ALA   A  1  322 ? 46.106  -24.856 -31.097  1.00 88.08  ? 322  ALA   A CA   1 
ATOM   4866  C  C    . ALA   A  1  322 ? 46.331  -26.349 -30.919  1.00 98.76  ? 322  ALA   A C    1 
ATOM   4867  O  O    . ALA   A  1  322 ? 45.968  -27.142 -31.796  1.00 97.58  ? 322  ALA   A O    1 
ATOM   4868  C  CB   . ALA   A  1  322 ? 47.336  -24.212 -31.735  1.00 85.70  ? 322  ALA   A CB   1 
ATOM   4869  H  H    . ALA   A  1  322 ? 46.323  -23.551 -29.626  1.00 101.07 ? 322  ALA   A H    1 
ATOM   4870  H  HA   . ALA   A  1  322 ? 45.354  -24.734 -31.697  1.00 105.74 ? 322  ALA   A HA   1 
ATOM   4871  H  HB1  . ALA   A  1  322 ? 47.523  -24.656 -32.577  1.00 102.88 ? 322  ALA   A HB1  1 
ATOM   4872  H  HB2  . ALA   A  1  322 ? 47.156  -23.272 -31.889  1.00 102.88 ? 322  ALA   A HB2  1 
ATOM   4873  H  HB3  . ALA   A  1  322 ? 48.091  -24.310 -31.134  1.00 102.88 ? 322  ALA   A HB3  1 
ATOM   4874  N  N    . SER   A  1  323 ? 46.913  -26.751 -29.791  1.00 108.99 ? 323  SER   A N    1 
ATOM   4875  C  CA   . SER   A  1  323 ? 47.155  -28.155 -29.503  1.00 115.93 ? 323  SER   A CA   1 
ATOM   4876  C  C    . SER   A  1  323 ? 45.873  -28.964 -29.347  1.00 124.27 ? 323  SER   A C    1 
ATOM   4877  O  O    . SER   A  1  323 ? 45.943  -30.174 -29.128  1.00 140.49 ? 323  SER   A O    1 
ATOM   4878  C  CB   . SER   A  1  323 ? 47.997  -28.280 -28.229  1.00 111.94 ? 323  SER   A CB   1 
ATOM   4879  O  OG   . SER   A  1  323 ? 47.382  -27.592 -27.152  1.00 102.06 ? 323  SER   A OG   1 
ATOM   4880  H  H    . SER   A  1  323 ? 47.181  -26.219 -29.170  1.00 130.82 ? 323  SER   A H    1 
ATOM   4881  H  HA   . SER   A  1  323 ? 47.633  -28.534 -30.257  1.00 139.15 ? 323  SER   A HA   1 
ATOM   4882  H  HB2  . SER   A  1  323 ? 48.083  -29.218 -27.998  1.00 134.37 ? 323  SER   A HB2  1 
ATOM   4883  H  HB3  . SER   A  1  323 ? 48.873  -27.896 -28.391  1.00 134.37 ? 323  SER   A HB3  1 
ATOM   4884  H  HG   . SER   A  1  323 ? 47.901  -27.568 -26.493  1.00 122.51 ? 323  SER   A HG   1 
ATOM   4885  N  N    . GLY   A  1  324 ? 44.706  -28.319 -29.451  1.00 119.70 ? 324  GLY   A N    1 
ATOM   4886  C  CA   . GLY   A  1  324 ? 43.435  -28.997 -29.338  1.00 122.72 ? 324  GLY   A CA   1 
ATOM   4887  C  C    . GLY   A  1  324 ? 42.885  -29.084 -27.932  1.00 123.64 ? 324  GLY   A C    1 
ATOM   4888  O  O    . GLY   A  1  324 ? 41.688  -29.340 -27.764  1.00 126.43 ? 324  GLY   A O    1 
ATOM   4889  H  H    . GLY   A  1  324 ? 44.635  -27.473 -29.589  1.00 143.67 ? 324  GLY   A H    1 
ATOM   4890  H  HA2  . GLY   A  1  324 ? 42.783  -28.528 -29.882  1.00 147.30 ? 324  GLY   A HA2  1 
ATOM   4891  H  HA3  . GLY   A  1  324 ? 43.534  -29.901 -29.674  1.00 147.30 ? 324  GLY   A HA3  1 
ATOM   4892  N  N    . ASP   A  1  325 ? 43.719  -28.875 -26.920  1.00 118.78 ? 325  ASP   A N    1 
ATOM   4893  C  CA   . ASP   A  1  325 ? 43.270  -28.929 -25.537  1.00 117.98 ? 325  ASP   A CA   1 
ATOM   4894  C  C    . ASP   A  1  325 ? 42.400  -27.710 -25.236  1.00 103.93 ? 325  ASP   A C    1 
ATOM   4895  O  O    . ASP   A  1  325 ? 42.067  -26.908 -26.113  1.00 99.41  ? 325  ASP   A O    1 
ATOM   4896  C  CB   . ASP   A  1  325 ? 44.466  -29.003 -24.592  1.00 129.15 ? 325  ASP   A CB   1 
ATOM   4897  C  CG   . ASP   A  1  325 ? 45.239  -30.299 -24.726  1.00 134.83 ? 325  ASP   A CG   1 
ATOM   4898  O  OD1  . ASP   A  1  325 ? 44.750  -31.218 -25.415  1.00 139.85 ? 325  ASP   A OD1  1 
ATOM   4899  O  OD2  . ASP   A  1  325 ? 46.338  -30.397 -24.141  1.00 141.79 ? 325  ASP   A OD2  1 
ATOM   4900  H  H    . ASP   A  1  325 ? 44.556  -28.700 -27.009  1.00 142.58 ? 325  ASP   A H    1 
ATOM   4901  H  HA   . ASP   A  1  325 ? 42.736  -29.731 -25.427  1.00 141.62 ? 325  ASP   A HA   1 
ATOM   4902  H  HB2  . ASP   A  1  325 ? 45.071  -28.271 -24.790  1.00 155.02 ? 325  ASP   A HB2  1 
ATOM   4903  H  HB3  . ASP   A  1  325 ? 44.151  -28.935 -23.677  1.00 155.02 ? 325  ASP   A HB3  1 
ATOM   4904  N  N    . PHE   A  1  326 ? 42.020  -27.571 -23.970  1.00 93.28  ? 326  PHE   A N    1 
ATOM   4905  C  CA   . PHE   A  1  326 ? 41.322  -26.393 -23.485  1.00 82.10  ? 326  PHE   A CA   1 
ATOM   4906  C  C    . PHE   A  1  326 ? 41.928  -25.984 -22.152  1.00 80.38  ? 326  PHE   A C    1 
ATOM   4907  O  O    . PHE   A  1  326 ? 42.441  -26.817 -21.400  1.00 58.63  ? 326  PHE   A O    1 
ATOM   4908  C  CB   . PHE   A  1  326 ? 39.815  -26.641 -23.335  1.00 73.65  ? 326  PHE   A CB   1 
ATOM   4909  C  CG   . PHE   A  1  326 ? 39.069  -26.656 -24.641  1.00 64.78  ? 326  PHE   A CG   1 
ATOM   4910  C  CD1  . PHE   A  1  326 ? 38.948  -27.826 -25.373  1.00 63.14  ? 326  PHE   A CD1  1 
ATOM   4911  C  CD2  . PHE   A  1  326 ? 38.489  -25.500 -25.136  1.00 57.71  ? 326  PHE   A CD2  1 
ATOM   4912  C  CE1  . PHE   A  1  326 ? 38.262  -27.842 -26.574  1.00 61.15  ? 326  PHE   A CE1  1 
ATOM   4913  C  CE2  . PHE   A  1  326 ? 37.802  -25.510 -26.337  1.00 53.15  ? 326  PHE   A CE2  1 
ATOM   4914  C  CZ   . PHE   A  1  326 ? 37.689  -26.683 -27.056  1.00 55.79  ? 326  PHE   A CZ   1 
ATOM   4915  H  H    . PHE   A  1  326 ? 42.159  -28.162 -23.360  1.00 111.97 ? 326  PHE   A H    1 
ATOM   4916  H  HA   . PHE   A  1  326 ? 41.435  -25.661 -24.112  1.00 98.55  ? 326  PHE   A HA   1 
ATOM   4917  H  HB2  . PHE   A  1  326 ? 39.682  -27.502 -22.908  1.00 88.41  ? 326  PHE   A HB2  1 
ATOM   4918  H  HB3  . PHE   A  1  326 ? 39.436  -25.937 -22.786  1.00 88.41  ? 326  PHE   A HB3  1 
ATOM   4919  H  HD1  . PHE   A  1  326 ? 39.332  -28.610 -25.053  1.00 75.80  ? 326  PHE   A HD1  1 
ATOM   4920  H  HD2  . PHE   A  1  326 ? 38.562  -24.707 -24.656  1.00 69.28  ? 326  PHE   A HD2  1 
ATOM   4921  H  HE1  . PHE   A  1  326 ? 38.188  -28.633 -27.057  1.00 73.42  ? 326  PHE   A HE1  1 
ATOM   4922  H  HE2  . PHE   A  1  326 ? 37.417  -24.728 -26.659  1.00 63.81  ? 326  PHE   A HE2  1 
ATOM   4923  H  HZ   . PHE   A  1  326 ? 37.228  -26.692 -27.863  1.00 66.99  ? 326  PHE   A HZ   1 
ATOM   4924  N  N    . GLN   A  1  327 ? 41.874  -24.685 -21.878  1.00 77.56  ? 327  GLN   A N    1 
ATOM   4925  C  CA   . GLN   A  1  327 ? 42.396  -24.093 -20.650  1.00 74.45  ? 327  GLN   A CA   1 
ATOM   4926  C  C    . GLN   A  1  327 ? 41.216  -23.459 -19.926  1.00 69.44  ? 327  GLN   A C    1 
ATOM   4927  O  O    . GLN   A  1  327 ? 40.723  -22.403 -20.340  1.00 63.84  ? 327  GLN   A O    1 
ATOM   4928  C  CB   . GLN   A  1  327 ? 43.485  -23.073 -20.972  1.00 78.83  ? 327  GLN   A CB   1 
ATOM   4929  C  CG   . GLN   A  1  327 ? 44.069  -22.350 -19.779  1.00 85.47  ? 327  GLN   A CG   1 
ATOM   4930  C  CD   . GLN   A  1  327 ? 45.398  -21.699 -20.108  1.00 92.06  ? 327  GLN   A CD   1 
ATOM   4931  O  OE1  . GLN   A  1  327 ? 46.460  -22.246 -19.810  1.00 96.99  ? 327  GLN   A OE1  1 
ATOM   4932  N  NE2  . GLN   A  1  327 ? 45.346  -20.532 -20.739  1.00 95.39  ? 327  GLN   A NE2  1 
ATOM   4933  H  H    . GLN   A  1  327 ? 41.527  -24.104 -22.408  1.00 93.11  ? 327  GLN   A H    1 
ATOM   4934  H  HA   . GLN   A  1  327 ? 42.785  -24.769 -20.073  1.00 89.38  ? 327  GLN   A HA   1 
ATOM   4935  H  HB2  . GLN   A  1  327 ? 44.214  -23.535 -21.416  1.00 94.64  ? 327  GLN   A HB2  1 
ATOM   4936  H  HB3  . GLN   A  1  327 ? 43.110  -22.401 -21.563  1.00 94.64  ? 327  GLN   A HB3  1 
ATOM   4937  H  HG2  . GLN   A  1  327 ? 43.454  -21.657 -19.493  1.00 102.60 ? 327  GLN   A HG2  1 
ATOM   4938  H  HG3  . GLN   A  1  327 ? 44.211  -22.984 -19.059  1.00 102.60 ? 327  GLN   A HG3  1 
ATOM   4939  H  HE21 . GLN   A  1  327 ? 44.585  -20.184 -20.938  1.00 114.50 ? 327  GLN   A HE21 1 
ATOM   4940  H  HE22 . GLN   A  1  327 ? 46.073  -20.123 -20.947  1.00 114.50 ? 327  GLN   A HE22 1 
ATOM   4941  N  N    . THR   A  1  328 ? 40.758  -24.102 -18.855  1.00 68.87  ? 328  THR   A N    1 
ATOM   4942  C  CA   . THR   A  1  328 ? 39.461  -23.806 -18.265  1.00 64.31  ? 328  THR   A CA   1 
ATOM   4943  C  C    . THR   A  1  328 ? 39.601  -23.045 -16.953  1.00 65.48  ? 328  THR   A C    1 
ATOM   4944  O  O    . THR   A  1  328 ? 40.531  -23.280 -16.175  1.00 66.86  ? 328  THR   A O    1 
ATOM   4945  C  CB   . THR   A  1  328 ? 38.667  -25.096 -18.024  1.00 61.89  ? 328  THR   A CB   1 
ATOM   4946  O  OG1  . THR   A  1  328 ? 38.529  -25.811 -19.258  1.00 61.97  ? 328  THR   A OG1  1 
ATOM   4947  C  CG2  . THR   A  1  328 ? 37.283  -24.779 -17.473  1.00 56.49  ? 328  THR   A CG2  1 
ATOM   4948  H  H    . THR   A  1  328 ? 41.190  -24.724 -18.448  1.00 82.68  ? 328  THR   A H    1 
ATOM   4949  H  HA   . THR   A  1  328 ? 38.970  -23.236 -18.876  1.00 77.20  ? 328  THR   A HA   1 
ATOM   4950  H  HB   . THR   A  1  328 ? 39.137  -25.647 -17.379  1.00 74.30  ? 328  THR   A HB   1 
ATOM   4951  H  HG1  . THR   A  1  328 ? 37.983  -25.416 -19.760  1.00 74.40  ? 328  THR   A HG1  1 
ATOM   4952  H  HG21 . THR   A  1  328 ? 36.757  -25.592 -17.410  1.00 67.82  ? 328  THR   A HG21 1 
ATOM   4953  H  HG22 . THR   A  1  328 ? 37.359  -24.385 -16.590  1.00 67.82  ? 328  THR   A HG22 1 
ATOM   4954  H  HG23 . THR   A  1  328 ? 36.827  -24.154 -18.058  1.00 67.82  ? 328  THR   A HG23 1 
ATOM   4955  N  N    . THR   A  1  329 ? 38.657  -22.133 -16.724  1.00 65.38  ? 329  THR   A N    1 
ATOM   4956  C  CA   . THR   A  1  329 ? 38.539  -21.386 -15.482  1.00 73.24  ? 329  THR   A CA   1 
ATOM   4957  C  C    . THR   A  1  329 ? 37.057  -21.223 -15.172  1.00 69.80  ? 329  THR   A C    1 
ATOM   4958  O  O    . THR   A  1  329 ? 36.210  -21.268 -16.067  1.00 66.44  ? 329  THR   A O    1 
ATOM   4959  C  CB   . THR   A  1  329 ? 39.213  -20.009 -15.572  1.00 83.09  ? 329  THR   A CB   1 
ATOM   4960  O  OG1  . THR   A  1  329 ? 40.585  -20.165 -15.953  1.00 93.08  ? 329  THR   A OG1  1 
ATOM   4961  C  CG2  . THR   A  1  329 ? 39.139  -19.278 -14.234  1.00 91.25  ? 329  THR   A CG2  1 
ATOM   4962  H  H    . THR   A  1  329 ? 38.052  -21.924 -17.297  1.00 78.49  ? 329  THR   A H    1 
ATOM   4963  H  HA   . THR   A  1  329 ? 38.965  -21.875 -14.761  1.00 87.92  ? 329  THR   A HA   1 
ATOM   4964  H  HB   . THR   A  1  329 ? 38.752  -19.472 -16.235  1.00 99.75  ? 329  THR   A HB   1 
ATOM   4965  H  HG1  . THR   A  1  329 ? 40.968  -19.418 -15.962  1.00 111.73 ? 329  THR   A HG1  1 
ATOM   4966  H  HG21 . THR   A  1  329 ? 39.666  -18.464 -14.271  1.00 109.54 ? 329  THR   A HG21 1 
ATOM   4967  H  HG22 . THR   A  1  329 ? 38.218  -19.048 -14.032  1.00 109.54 ? 329  THR   A HG22 1 
ATOM   4968  H  HG23 . THR   A  1  329 ? 39.484  -19.844 -13.527  1.00 109.54 ? 329  THR   A HG23 1 
ATOM   4969  N  N    . LYS   A  1  330 ? 36.750  -21.033 -13.895  1.00 72.15  ? 330  LYS   A N    1 
ATOM   4970  C  CA   . LYS   A  1  330 ? 35.378  -20.887 -13.437  1.00 71.25  ? 330  LYS   A CA   1 
ATOM   4971  C  C    . LYS   A  1  330 ? 35.133  -19.457 -12.972  1.00 71.30  ? 330  LYS   A C    1 
ATOM   4972  O  O    . LYS   A  1  330 ? 36.065  -18.696 -12.698  1.00 76.37  ? 330  LYS   A O    1 
ATOM   4973  C  CB   . LYS   A  1  330 ? 35.071  -21.876 -12.306  1.00 71.96  ? 330  LYS   A CB   1 
ATOM   4974  C  CG   . LYS   A  1  330 ? 35.559  -23.301 -12.570  1.00 73.82  ? 330  LYS   A CG   1 
ATOM   4975  C  CD   . LYS   A  1  330 ? 34.585  -24.103 -13.421  1.00 74.55  ? 330  LYS   A CD   1 
ATOM   4976  C  CE   . LYS   A  1  330 ? 35.156  -25.473 -13.770  1.00 81.42  ? 330  LYS   A CE   1 
ATOM   4977  N  NZ   . LYS   A  1  330 ? 35.552  -26.257 -12.564  1.00 89.45  ? 330  LYS   A NZ   1 
ATOM   4978  H  H    . LYS   A  1  330 ? 37.332  -20.984 -13.264  1.00 86.62  ? 330  LYS   A H    1 
ATOM   4979  H  HA   . LYS   A  1  330 ? 34.769  -21.074 -14.168  1.00 85.53  ? 330  LYS   A HA   1 
ATOM   4980  H  HB2  . LYS   A  1  330 ? 35.501  -21.563 -11.495  1.00 86.39  ? 330  LYS   A HB2  1 
ATOM   4981  H  HB3  . LYS   A  1  330 ? 34.110  -21.913 -12.179  1.00 86.39  ? 330  LYS   A HB3  1 
ATOM   4982  H  HG2  . LYS   A  1  330 ? 36.408  -23.264 -13.039  1.00 88.62  ? 330  LYS   A HG2  1 
ATOM   4983  H  HG3  . LYS   A  1  330 ? 35.668  -23.761 -11.723  1.00 88.62  ? 330  LYS   A HG3  1 
ATOM   4984  H  HD2  . LYS   A  1  330 ? 33.759  -24.232 -12.930  1.00 89.50  ? 330  LYS   A HD2  1 
ATOM   4985  H  HD3  . LYS   A  1  330 ? 34.409  -23.625 -14.247  1.00 89.50  ? 330  LYS   A HD3  1 
ATOM   4986  H  HE2  . LYS   A  1  330 ? 34.485  -25.982 -14.251  1.00 97.75  ? 330  LYS   A HE2  1 
ATOM   4987  H  HE3  . LYS   A  1  330 ? 35.944  -25.356 -14.323  1.00 97.75  ? 330  LYS   A HE3  1 
ATOM   4988  H  HZ1  . LYS   A  1  330 ? 35.743  -27.095 -12.794  1.00 107.37 ? 330  LYS   A HZ1  1 
ATOM   4989  H  HZ2  . LYS   A  1  330 ? 36.270  -25.891 -12.185  1.00 107.37 ? 330  LYS   A HZ2  1 
ATOM   4990  H  HZ3  . LYS   A  1  330 ? 34.886  -26.265 -11.973  1.00 107.37 ? 330  LYS   A HZ3  1 
ATOM   4991  N  N    . LEU   A  1  331 ? 33.853  -19.103 -12.887  1.00 68.73  ? 331  LEU   A N    1 
ATOM   4992  C  CA   . LEU   A  1  331 ? 33.441  -17.736 -12.577  1.00 64.11  ? 331  LEU   A CA   1 
ATOM   4993  C  C    . LEU   A  1  331 ? 32.109  -17.830 -11.847  1.00 61.72  ? 331  LEU   A C    1 
ATOM   4994  O  O    . LEU   A  1  331 ? 31.093  -18.171 -12.459  1.00 61.98  ? 331  LEU   A O    1 
ATOM   4995  C  CB   . LEU   A  1  331 ? 33.317  -16.907 -13.850  1.00 62.71  ? 331  LEU   A CB   1 
ATOM   4996  C  CG   . LEU   A  1  331 ? 33.562  -15.402 -13.773  1.00 63.71  ? 331  LEU   A CG   1 
ATOM   4997  C  CD1  . LEU   A  1  331 ? 35.016  -15.105 -13.438  1.00 68.81  ? 331  LEU   A CD1  1 
ATOM   4998  C  CD2  . LEU   A  1  331 ? 33.167  -14.773 -15.098  1.00 58.68  ? 331  LEU   A CD2  1 
ATOM   4999  H  H    . LEU   A  1  331 ? 33.195  -19.643 -13.006  1.00 82.51  ? 331  LEU   A H    1 
ATOM   5000  H  HA   . LEU   A  1  331 ? 34.090  -17.308 -11.997  1.00 76.97  ? 331  LEU   A HA   1 
ATOM   5001  H  HB2  . LEU   A  1  331 ? 33.956  -17.258 -14.490  1.00 75.29  ? 331  LEU   A HB2  1 
ATOM   5002  H  HB3  . LEU   A  1  331 ? 32.414  -17.022 -14.187  1.00 75.29  ? 331  LEU   A HB3  1 
ATOM   5003  H  HG   . LEU   A  1  331 ? 33.025  -15.013 -13.065  1.00 76.49  ? 331  LEU   A HG   1 
ATOM   5004  H  HD11 . LEU   A  1  331 ? 35.151  -14.145 -13.444  1.00 82.61  ? 331  LEU   A HD11 1 
ATOM   5005  H  HD12 . LEU   A  1  331 ? 35.216  -15.462 -12.558  1.00 82.61  ? 331  LEU   A HD12 1 
ATOM   5006  H  HD13 . LEU   A  1  331 ? 35.585  -15.524 -14.102  1.00 82.61  ? 331  LEU   A HD13 1 
ATOM   5007  H  HD21 . LEU   A  1  331 ? 33.389  -13.829 -15.077  1.00 70.45  ? 331  LEU   A HD21 1 
ATOM   5008  H  HD22 . LEU   A  1  331 ? 33.654  -15.211 -15.813  1.00 70.45  ? 331  LEU   A HD22 1 
ATOM   5009  H  HD23 . LEU   A  1  331 ? 32.213  -14.886 -15.229  1.00 70.45  ? 331  LEU   A HD23 1 
ATOM   5010  N  N    . ASN   A  1  332 ? 32.110  -17.532 -10.554  1.00 61.02  ? 332  ASN   A N    1 
ATOM   5011  C  CA   . ASN   A  1  332 ? 30.948  -17.789 -9.719   1.00 62.17  ? 332  ASN   A CA   1 
ATOM   5012  C  C    . ASN   A  1  332 ? 30.016  -16.587 -9.672   1.00 63.96  ? 332  ASN   A C    1 
ATOM   5013  O  O    . ASN   A  1  332 ? 30.432  -15.439 -9.851   1.00 68.86  ? 332  ASN   A O    1 
ATOM   5014  C  CB   . ASN   A  1  332 ? 31.378  -18.161 -8.301   1.00 65.74  ? 332  ASN   A CB   1 
ATOM   5015  C  CG   . ASN   A  1  332 ? 31.986  -19.544 -8.225   1.00 68.25  ? 332  ASN   A CG   1 
ATOM   5016  O  OD1  . ASN   A  1  332 ? 32.398  -20.109 -9.238   1.00 68.68  ? 332  ASN   A OD1  1 
ATOM   5017  N  ND2  . ASN   A  1  332 ? 32.040  -20.100 -7.023   1.00 75.76  ? 332  ASN   A ND2  1 
ATOM   5018  H  H    . ASN   A  1  332 ? 32.774  -17.179 -10.137  1.00 73.27  ? 332  ASN   A H    1 
ATOM   5019  H  HA   . ASN   A  1  332 ? 30.451  -18.530 -10.100  1.00 74.64  ? 332  ASN   A HA   1 
ATOM   5020  H  HB2  . ASN   A  1  332 ? 32.041  -17.523 -7.993   1.00 78.92  ? 332  ASN   A HB2  1 
ATOM   5021  H  HB3  . ASN   A  1  332 ? 30.603  -18.140 -7.719   1.00 78.92  ? 332  ASN   A HB3  1 
ATOM   5022  H  HD21 . ASN   A  1  332 ? 32.376  -20.885 -6.927   1.00 90.95  ? 332  ASN   A HD21 1 
ATOM   5023  H  HD22 . ASN   A  1  332 ? 31.738  -19.675 -6.338   1.00 90.95  ? 332  ASN   A HD22 1 
ATOM   5024  N  N    . GLY   A  1  333 ? 28.741  -16.869 -9.431   1.00 62.43  ? 333  GLY   A N    1 
ATOM   5025  C  CA   . GLY   A  1  333 ? 27.768  -15.818 -9.249   1.00 61.36  ? 333  GLY   A CA   1 
ATOM   5026  C  C    . GLY   A  1  333 ? 28.041  -15.017 -7.993   1.00 63.18  ? 333  GLY   A C    1 
ATOM   5027  O  O    . GLY   A  1  333 ? 28.914  -15.334 -7.184   1.00 62.91  ? 333  GLY   A O    1 
ATOM   5028  H  H    . GLY   A  1  333 ? 28.420  -17.665 -9.368   1.00 74.96  ? 333  GLY   A H    1 
ATOM   5029  H  HA2  . GLY   A  1  333 ? 27.794  -15.217 -10.010  1.00 73.66  ? 333  GLY   A HA2  1 
ATOM   5030  H  HA3  . GLY   A  1  333 ? 26.881  -16.205 -9.183   1.00 73.66  ? 333  GLY   A HA3  1 
ATOM   5031  N  N    . PHE   A  1  334 ? 27.265  -13.948 -7.831   1.00 63.07  ? 334  PHE   A N    1 
ATOM   5032  C  CA   . PHE   A  1  334 ? 27.435  -13.035 -6.711   1.00 66.11  ? 334  PHE   A CA   1 
ATOM   5033  C  C    . PHE   A  1  334 ? 26.272  -13.044 -5.734   1.00 67.84  ? 334  PHE   A C    1 
ATOM   5034  O  O    . PHE   A  1  334 ? 26.483  -12.797 -4.545   1.00 71.49  ? 334  PHE   A O    1 
ATOM   5035  C  CB   . PHE   A  1  334 ? 27.637  -11.605 -7.224   1.00 68.40  ? 334  PHE   A CB   1 
ATOM   5036  C  CG   . PHE   A  1  334 ? 28.701  -11.486 -8.276   1.00 67.69  ? 334  PHE   A CG   1 
ATOM   5037  C  CD1  . PHE   A  1  334 ? 30.037  -11.404 -7.923   1.00 69.02  ? 334  PHE   A CD1  1 
ATOM   5038  C  CD2  . PHE   A  1  334 ? 28.365  -11.459 -9.619   1.00 62.40  ? 334  PHE   A CD2  1 
ATOM   5039  C  CE1  . PHE   A  1  334 ? 31.018  -11.296 -8.890   1.00 71.01  ? 334  PHE   A CE1  1 
ATOM   5040  C  CE2  . PHE   A  1  334 ? 29.341  -11.350 -10.590  1.00 63.21  ? 334  PHE   A CE2  1 
ATOM   5041  C  CZ   . PHE   A  1  334 ? 30.669  -11.268 -10.225  1.00 67.83  ? 334  PHE   A CZ   1 
ATOM   5042  H  H    . PHE   A  1  334 ? 26.626  -13.731 -8.364   1.00 75.72  ? 334  PHE   A H    1 
ATOM   5043  H  HA   . PHE   A  1  334 ? 28.232  -13.291 -6.219   1.00 79.37  ? 334  PHE   A HA   1 
ATOM   5044  H  HB2  . PHE   A  1  334 ? 26.804  -11.291 -7.609   1.00 82.11  ? 334  PHE   A HB2  1 
ATOM   5045  H  HB3  . PHE   A  1  334 ? 27.893  -11.039 -6.479   1.00 82.11  ? 334  PHE   A HB3  1 
ATOM   5046  H  HD1  . PHE   A  1  334 ? 30.277  -11.421 -7.025   1.00 82.86  ? 334  PHE   A HD1  1 
ATOM   5047  H  HD2  . PHE   A  1  334 ? 27.471  -11.514 -9.870   1.00 74.92  ? 334  PHE   A HD2  1 
ATOM   5048  H  HE1  . PHE   A  1  334 ? 31.913  -11.241 -8.641   1.00 85.24  ? 334  PHE   A HE1  1 
ATOM   5049  H  HE2  . PHE   A  1  334 ? 29.103  -11.332 -11.489  1.00 75.89  ? 334  PHE   A HE2  1 
ATOM   5050  H  HZ   . PHE   A  1  334 ? 31.328  -11.195 -10.877  1.00 81.44  ? 334  PHE   A HZ   1 
ATOM   5051  N  N    . GLU   A  1  335 ? 25.058  -13.324 -6.200   1.00 65.44  ? 335  GLU   A N    1 
ATOM   5052  C  CA   . GLU   A  1  335 ? 23.875  -13.341 -5.356   1.00 61.81  ? 335  GLU   A CA   1 
ATOM   5053  C  C    . GLU   A  1  335 ? 23.270  -14.736 -5.332   1.00 61.12  ? 335  GLU   A C    1 
ATOM   5054  O  O    . GLU   A  1  335 ? 23.311  -15.470 -6.325   1.00 62.05  ? 335  GLU   A O    1 
ATOM   5055  C  CB   . GLU   A  1  335 ? 22.821  -12.347 -5.846   1.00 60.67  ? 335  GLU   A CB   1 
ATOM   5056  C  CG   . GLU   A  1  335 ? 23.188  -10.890 -5.667   1.00 64.90  ? 335  GLU   A CG   1 
ATOM   5057  C  CD   . GLU   A  1  335 ? 22.210  -9.972  -6.369   1.00 73.16  ? 335  GLU   A CD   1 
ATOM   5058  O  OE1  . GLU   A  1  335 ? 22.127  -10.039 -7.613   1.00 76.10  ? 335  GLU   A OE1  1 
ATOM   5059  O  OE2  . GLU   A  1  335 ? 21.511  -9.202  -5.679   1.00 79.20  ? 335  GLU   A OE2  1 
ATOM   5060  H  H    . GLU   A  1  335 ? 24.894  -13.512 -7.023   1.00 78.57  ? 335  GLU   A H    1 
ATOM   5061  H  HA   . GLU   A  1  335 ? 24.131  -13.098 -4.452   1.00 74.21  ? 335  GLU   A HA   1 
ATOM   5062  H  HB2  . GLU   A  1  335 ? 22.674  -12.497 -6.794   1.00 72.84  ? 335  GLU   A HB2  1 
ATOM   5063  H  HB3  . GLU   A  1  335 ? 21.999  -12.503 -5.355   1.00 72.84  ? 335  GLU   A HB3  1 
ATOM   5064  H  HG2  . GLU   A  1  335 ? 23.184  -10.673 -4.722   1.00 77.92  ? 335  GLU   A HG2  1 
ATOM   5065  H  HG3  . GLU   A  1  335 ? 24.071  -10.735 -6.039   1.00 77.92  ? 335  GLU   A HG3  1 
ATOM   5066  N  N    . VAL   A  1  336 ? 22.690  -15.089 -4.185   1.00 59.22  ? 336  VAL   A N    1 
ATOM   5067  C  CA   . VAL   A  1  336 ? 22.090  -16.405 -4.025   1.00 57.05  ? 336  VAL   A CA   1 
ATOM   5068  C  C    . VAL   A  1  336 ? 20.774  -16.463 -4.789   1.00 54.19  ? 336  VAL   A C    1 
ATOM   5069  O  O    . VAL   A  1  336 ? 19.974  -15.519 -4.762   1.00 56.39  ? 336  VAL   A O    1 
ATOM   5070  C  CB   . VAL   A  1  336 ? 21.881  -16.723 -2.535   1.00 60.28  ? 336  VAL   A CB   1 
ATOM   5071  C  CG1  . VAL   A  1  336 ? 21.381  -18.148 -2.362   1.00 60.89  ? 336  VAL   A CG1  1 
ATOM   5072  C  CG2  . VAL   A  1  336 ? 23.171  -16.509 -1.756   1.00 64.30  ? 336  VAL   A CG2  1 
ATOM   5073  H  H    . VAL   A  1  336 ? 22.633  -14.586 -3.490   1.00 71.10  ? 336  VAL   A H    1 
ATOM   5074  H  HA   . VAL   A  1  336 ? 22.690  -17.072 -4.396   1.00 68.50  ? 336  VAL   A HA   1 
ATOM   5075  H  HB   . VAL   A  1  336 ? 21.210  -16.120 -2.177   1.00 72.38  ? 336  VAL   A HB   1 
ATOM   5076  H  HG11 . VAL   A  1  336 ? 21.232  -18.318 -1.419   1.00 73.11  ? 336  VAL   A HG11 1 
ATOM   5077  H  HG12 . VAL   A  1  336 ? 20.551  -18.253 -2.853   1.00 73.11  ? 336  VAL   A HG12 1 
ATOM   5078  H  HG13 . VAL   A  1  336 ? 22.049  -18.761 -2.708   1.00 73.11  ? 336  VAL   A HG13 1 
ATOM   5079  H  HG21 . VAL   A  1  336 ? 23.015  -16.721 -0.823   1.00 77.19  ? 336  VAL   A HG21 1 
ATOM   5080  H  HG22 . VAL   A  1  336 ? 23.858  -17.091 -2.118   1.00 77.19  ? 336  VAL   A HG22 1 
ATOM   5081  H  HG23 . VAL   A  1  336 ? 23.443  -15.582 -1.844   1.00 77.19  ? 336  VAL   A HG23 1 
ATOM   5082  N  N    . PHE   A  1  337 ? 20.547  -17.577 -5.482   1.00 52.19  ? 337  PHE   A N    1 
ATOM   5083  C  CA   . PHE   A  1  337 ? 19.328  -17.841 -6.240   1.00 52.04  ? 337  PHE   A CA   1 
ATOM   5084  C  C    . PHE   A  1  337 ? 19.138  -16.886 -7.412   1.00 54.99  ? 337  PHE   A C    1 
ATOM   5085  O  O    . PHE   A  1  337 ? 18.091  -16.922 -8.070   1.00 56.25  ? 337  PHE   A O    1 
ATOM   5086  C  CB   . PHE   A  1  337 ? 18.091  -17.795 -5.332   1.00 49.88  ? 337  PHE   A CB   1 
ATOM   5087  C  CG   . PHE   A  1  337 ? 18.066  -18.875 -4.289   1.00 49.06  ? 337  PHE   A CG   1 
ATOM   5088  C  CD1  . PHE   A  1  337 ? 18.223  -20.205 -4.645   1.00 47.61  ? 337  PHE   A CD1  1 
ATOM   5089  C  CD2  . PHE   A  1  337 ? 17.894  -18.561 -2.952   1.00 50.62  ? 337  PHE   A CD2  1 
ATOM   5090  C  CE1  . PHE   A  1  337 ? 18.204  -21.199 -3.688   1.00 47.27  ? 337  PHE   A CE1  1 
ATOM   5091  C  CE2  . PHE   A  1  337 ? 17.878  -19.551 -1.990   1.00 50.36  ? 337  PHE   A CE2  1 
ATOM   5092  C  CZ   . PHE   A  1  337 ? 18.032  -20.873 -2.359   1.00 49.41  ? 337  PHE   A CZ   1 
ATOM   5093  H  H    . PHE   A  1  337 ? 21.113  -18.224 -5.529   1.00 62.67  ? 337  PHE   A H    1 
ATOM   5094  H  HA   . PHE   A  1  337 ? 19.399  -18.734 -6.612   1.00 62.49  ? 337  PHE   A HA   1 
ATOM   5095  H  HB2  . PHE   A  1  337 ? 18.071  -16.941 -4.874   1.00 59.89  ? 337  PHE   A HB2  1 
ATOM   5096  H  HB3  . PHE   A  1  337 ? 17.297  -17.895 -5.881   1.00 59.89  ? 337  PHE   A HB3  1 
ATOM   5097  H  HD1  . PHE   A  1  337 ? 18.343  -20.430 -5.539   1.00 57.16  ? 337  PHE   A HD1  1 
ATOM   5098  H  HD2  . PHE   A  1  337 ? 17.789  -17.672 -2.699   1.00 60.78  ? 337  PHE   A HD2  1 
ATOM   5099  H  HE1  . PHE   A  1  337 ? 18.306  -22.089 -3.939   1.00 56.76  ? 337  PHE   A HE1  1 
ATOM   5100  H  HE2  . PHE   A  1  337 ? 17.762  -19.329 -1.094   1.00 60.47  ? 337  PHE   A HE2  1 
ATOM   5101  H  HZ   . PHE   A  1  337 ? 18.020  -21.541 -1.712   1.00 59.33  ? 337  PHE   A HZ   1 
ATOM   5102  N  N    . ALA   A  1  338 ? 20.121  -16.031 -7.695   1.00 54.52  ? 338  ALA   A N    1 
ATOM   5103  C  CA   . ALA   A  1  338 ? 20.046  -15.147 -8.850   1.00 53.53  ? 338  ALA   A CA   1 
ATOM   5104  C  C    . ALA   A  1  338 ? 20.297  -15.877 -10.163  1.00 47.42  ? 338  ALA   A C    1 
ATOM   5105  O  O    . ALA   A  1  338 ? 20.044  -15.305 -11.229  1.00 46.81  ? 338  ALA   A O    1 
ATOM   5106  C  CB   . ALA   A  1  338 ? 21.047  -14.000 -8.695   1.00 56.23  ? 338  ALA   A CB   1 
ATOM   5107  H  H    . ALA   A  1  338 ? 20.840  -15.946 -7.232   1.00 65.46  ? 338  ALA   A H    1 
ATOM   5108  H  HA   . ALA   A  1  338 ? 19.158  -14.759 -8.893   1.00 64.27  ? 338  ALA   A HA   1 
ATOM   5109  H  HB1  . ALA   A  1  338 ? 20.960  -13.401 -9.453   1.00 67.52  ? 338  ALA   A HB1  1 
ATOM   5110  H  HB2  . ALA   A  1  338 ? 20.856  -13.523 -7.873   1.00 67.52  ? 338  ALA   A HB2  1 
ATOM   5111  H  HB3  . ALA   A  1  338 ? 21.944  -14.367 -8.665   1.00 67.52  ? 338  ALA   A HB3  1 
ATOM   5112  N  N    . ARG   A  1  339 ? 20.787  -17.115 -10.109  1.00 46.88  ? 339  ARG   A N    1 
ATOM   5113  C  CA   . ARG   A  1  339 ? 20.988  -17.940 -11.300  1.00 46.42  ? 339  ARG   A CA   1 
ATOM   5114  C  C    . ARG   A  1  339 ? 21.932  -17.270 -12.293  1.00 48.06  ? 339  ARG   A C    1 
ATOM   5115  O  O    . ARG   A  1  339 ? 21.723  -17.316 -13.507  1.00 48.06  ? 339  ARG   A O    1 
ATOM   5116  C  CB   . ARG   A  1  339 ? 19.653  -18.282 -11.961  1.00 41.33  ? 339  ARG   A CB   1 
ATOM   5117  C  CG   . ARG   A  1  339 ? 18.747  -19.087 -11.057  1.00 42.19  ? 339  ARG   A CG   1 
ATOM   5118  C  CD   . ARG   A  1  339 ? 17.654  -19.801 -11.818  1.00 46.28  ? 339  ARG   A CD   1 
ATOM   5119  N  NE   . ARG   A  1  339 ? 16.848  -20.612 -10.912  1.00 50.22  ? 339  ARG   A NE   1 
ATOM   5120  C  CZ   . ARG   A  1  339 ? 15.660  -21.125 -11.212  1.00 53.76  ? 339  ARG   A CZ   1 
ATOM   5121  N  NH1  . ARG   A  1  339 ? 15.117  -20.914 -12.403  1.00 57.21  ? 339  ARG   A NH1  1 
ATOM   5122  N  NH2  . ARG   A  1  339 ? 15.011  -21.847 -10.309  1.00 56.37  ? 339  ARG   A NH2  1 
ATOM   5123  H  H    . ARG   A  1  339 ? 21.015  -17.508 -9.379   1.00 56.29  ? 339  ARG   A H    1 
ATOM   5124  H  HA   . ARG   A  1  339 ? 21.408  -18.771 -11.026  1.00 55.74  ? 339  ARG   A HA   1 
ATOM   5125  H  HB2  . ARG   A  1  339 ? 19.194  -17.458 -12.191  1.00 49.63  ? 339  ARG   A HB2  1 
ATOM   5126  H  HB3  . ARG   A  1  339 ? 19.820  -18.803 -12.762  1.00 49.63  ? 339  ARG   A HB3  1 
ATOM   5127  H  HG2  . ARG   A  1  339 ? 19.275  -19.755 -10.593  1.00 50.67  ? 339  ARG   A HG2  1 
ATOM   5128  H  HG3  . ARG   A  1  339 ? 18.328  -18.492 -10.416  1.00 50.67  ? 339  ARG   A HG3  1 
ATOM   5129  H  HD2  . ARG   A  1  339 ? 17.077  -19.149 -12.247  1.00 55.57  ? 339  ARG   A HD2  1 
ATOM   5130  H  HD3  . ARG   A  1  339 ? 18.049  -20.383 -12.486  1.00 55.57  ? 339  ARG   A HD3  1 
ATOM   5131  H  HE   . ARG   A  1  339 ? 17.164  -20.768 -10.128  1.00 60.30  ? 339  ARG   A HE   1 
ATOM   5132  H  HH11 . ARG   A  1  339 ? 15.535  -20.442 -12.989  1.00 68.68  ? 339  ARG   A HH11 1 
ATOM   5133  H  HH12 . ARG   A  1  339 ? 14.348  -21.250 -12.591  1.00 68.68  ? 339  ARG   A HH12 1 
ATOM   5134  H  HH21 . ARG   A  1  339 ? 15.359  -21.982 -9.535   1.00 67.68  ? 339  ARG   A HH21 1 
ATOM   5135  H  HH22 . ARG   A  1  339 ? 14.242  -22.182 -10.499  1.00 67.68  ? 339  ARG   A HH22 1 
ATOM   5136  N  N    . PHE   A  1  340 ? 22.973  -16.631 -11.765  1.00 50.55  ? 340  PHE   A N    1 
ATOM   5137  C  CA   . PHE   A  1  340 ? 24.084  -16.154 -12.576  1.00 52.11  ? 340  PHE   A CA   1 
ATOM   5138  C  C    . PHE   A  1  340 ? 24.469  -17.199 -13.614  1.00 50.41  ? 340  PHE   A C    1 
ATOM   5139  O  O    . PHE   A  1  340 ? 24.637  -18.378 -13.293  1.00 47.63  ? 340  PHE   A O    1 
ATOM   5140  C  CB   . PHE   A  1  340 ? 25.272  -15.843 -11.662  1.00 55.52  ? 340  PHE   A CB   1 
ATOM   5141  C  CG   . PHE   A  1  340 ? 26.514  -15.411 -12.385  1.00 57.21  ? 340  PHE   A CG   1 
ATOM   5142  C  CD1  . PHE   A  1  340 ? 26.711  -14.082 -12.720  1.00 57.41  ? 340  PHE   A CD1  1 
ATOM   5143  C  CD2  . PHE   A  1  340 ? 27.504  -16.330 -12.698  1.00 56.74  ? 340  PHE   A CD2  1 
ATOM   5144  C  CE1  . PHE   A  1  340 ? 27.861  -13.680 -13.372  1.00 56.59  ? 340  PHE   A CE1  1 
ATOM   5145  C  CE2  . PHE   A  1  340 ? 28.656  -15.934 -13.350  1.00 54.42  ? 340  PHE   A CE2  1 
ATOM   5146  C  CZ   . PHE   A  1  340 ? 28.836  -14.607 -13.685  1.00 53.31  ? 340  PHE   A CZ   1 
ATOM   5147  H  H    . PHE   A  1  340 ? 23.059  -16.460 -10.927  1.00 60.69  ? 340  PHE   A H    1 
ATOM   5148  H  HA   . PHE   A  1  340 ? 23.836  -15.341 -13.043  1.00 62.57  ? 340  PHE   A HA   1 
ATOM   5149  H  HB2  . PHE   A  1  340 ? 25.019  -15.126 -11.059  1.00 66.66  ? 340  PHE   A HB2  1 
ATOM   5150  H  HB3  . PHE   A  1  340 ? 25.490  -16.641 -11.155  1.00 66.66  ? 340  PHE   A HB3  1 
ATOM   5151  H  HD1  . PHE   A  1  340 ? 26.061  -13.453 -12.503  1.00 68.93  ? 340  PHE   A HD1  1 
ATOM   5152  H  HD2  . PHE   A  1  340 ? 27.390  -17.224 -12.467  1.00 68.12  ? 340  PHE   A HD2  1 
ATOM   5153  H  HE1  . PHE   A  1  340 ? 27.979  -12.786 -13.599  1.00 67.94  ? 340  PHE   A HE1  1 
ATOM   5154  H  HE2  . PHE   A  1  340 ? 29.310  -16.560 -13.561  1.00 65.35  ? 340  PHE   A HE2  1 
ATOM   5155  H  HZ   . PHE   A  1  340 ? 29.612  -14.337 -14.122  1.00 64.01  ? 340  PHE   A HZ   1 
ATOM   5156  N  N    . GLY   A  1  341 ? 24.587  -16.765 -14.864  1.00 49.40  ? 341  GLY   A N    1 
ATOM   5157  C  CA   . GLY   A  1  341 ? 24.936  -17.659 -15.946  1.00 45.67  ? 341  GLY   A CA   1 
ATOM   5158  C  C    . GLY   A  1  341 ? 23.769  -18.262 -16.692  1.00 49.40  ? 341  GLY   A C    1 
ATOM   5159  O  O    . GLY   A  1  341 ? 23.979  -19.167 -17.508  1.00 48.24  ? 341  GLY   A O    1 
ATOM   5160  H  H    . GLY   A  1  341 ? 24.467  -15.948 -15.108  1.00 59.31  ? 341  GLY   A H    1 
ATOM   5161  H  HA2  . GLY   A  1  341 ? 25.475  -17.171 -16.588  1.00 54.84  ? 341  GLY   A HA2  1 
ATOM   5162  H  HA3  . GLY   A  1  341 ? 25.462  -18.390 -15.584  1.00 54.84  ? 341  GLY   A HA3  1 
ATOM   5163  N  N    . SER   A  1  342 ? 22.541  -17.799 -16.438  1.00 49.59  ? 342  SER   A N    1 
ATOM   5164  C  CA   . SER   A  1  342 ? 21.401  -18.297 -17.198  1.00 46.47  ? 342  SER   A CA   1 
ATOM   5165  C  C    . SER   A  1  342 ? 21.513  -17.926 -18.671  1.00 49.24  ? 342  SER   A C    1 
ATOM   5166  O  O    . SER   A  1  342 ? 21.029  -18.664 -19.536  1.00 54.30  ? 342  SER   A O    1 
ATOM   5167  C  CB   . SER   A  1  342 ? 20.097  -17.752 -16.615  1.00 46.74  ? 342  SER   A CB   1 
ATOM   5168  O  OG   . SER   A  1  342 ? 19.875  -18.244 -15.305  1.00 50.60  ? 342  SER   A OG   1 
ATOM   5169  H  H    . SER   A  1  342 ? 22.349  -17.209 -15.843  1.00 59.55  ? 342  SER   A H    1 
ATOM   5170  H  HA   . SER   A  1  342 ? 21.378  -19.265 -17.128  1.00 55.80  ? 342  SER   A HA   1 
ATOM   5171  H  HB2  . SER   A  1  342 ? 20.149  -16.784 -16.582  1.00 56.13  ? 342  SER   A HB2  1 
ATOM   5172  H  HB3  . SER   A  1  342 ? 19.360  -18.026 -17.183  1.00 56.13  ? 342  SER   A HB3  1 
ATOM   5173  H  HG   . SER   A  1  342 ? 20.450  -17.931 -14.779  1.00 60.75  ? 342  SER   A HG   1 
ATOM   5174  N  N    . ALA   A  1  343 ? 22.147  -16.795 -18.973  1.00 50.00  ? 343  ALA   A N    1 
ATOM   5175  C  CA   . ALA   A  1  343 ? 22.321  -16.334 -20.342  1.00 49.08  ? 343  ALA   A CA   1 
ATOM   5176  C  C    . ALA   A  1  343 ? 23.717  -15.751 -20.495  1.00 47.82  ? 343  ALA   A C    1 
ATOM   5177  O  O    . ALA   A  1  343 ? 24.213  -15.064 -19.598  1.00 47.99  ? 343  ALA   A O    1 
ATOM   5178  C  CB   . ALA   A  1  343 ? 21.267  -15.287 -20.720  1.00 46.13  ? 343  ALA   A CB   1 
ATOM   5179  H  H    . ALA   A  1  343 ? 22.492  -16.268 -18.387  1.00 60.04  ? 343  ALA   A H    1 
ATOM   5180  H  HA   . ALA   A  1  343 ? 22.234  -17.082 -20.953  1.00 58.93  ? 343  ALA   A HA   1 
ATOM   5181  H  HB1  . ALA   A  1  343 ? 21.400  -15.024 -21.644  1.00 55.39  ? 343  ALA   A HB1  1 
ATOM   5182  H  HB2  . ALA   A  1  343 ? 20.384  -15.674 -20.611  1.00 55.39  ? 343  ALA   A HB2  1 
ATOM   5183  H  HB3  . ALA   A  1  343 ? 21.364  -14.516 -20.139  1.00 55.39  ? 343  ALA   A HB3  1 
ATOM   5184  N  N    . ILE   A  1  344 ? 24.343  -16.032 -21.635  1.00 47.96  ? 344  ILE   A N    1 
ATOM   5185  C  CA   . ILE   A  1  344 ? 25.711  -15.611 -21.915  1.00 50.07  ? 344  ILE   A CA   1 
ATOM   5186  C  C    . ILE   A  1  344 ? 25.742  -15.069 -23.336  1.00 55.88  ? 344  ILE   A C    1 
ATOM   5187  O  O    . ILE   A  1  344 ? 25.517  -15.820 -24.292  1.00 61.36  ? 344  ILE   A O    1 
ATOM   5188  C  CB   . ILE   A  1  344 ? 26.716  -16.766 -21.759  1.00 52.73  ? 344  ILE   A CB   1 
ATOM   5189  C  CG1  . ILE   A  1  344 ? 26.589  -17.400 -20.370  1.00 51.63  ? 344  ILE   A CG1  1 
ATOM   5190  C  CG2  . ILE   A  1  344 ? 28.136  -16.268 -21.992  1.00 53.93  ? 344  ILE   A CG2  1 
ATOM   5191  C  CD1  . ILE   A  1  344 ? 27.269  -18.743 -20.248  1.00 55.62  ? 344  ILE   A CD1  1 
ATOM   5192  H  H    . ILE   A  1  344 ? 23.985  -16.476 -22.279  1.00 57.59  ? 344  ILE   A H    1 
ATOM   5193  H  HA   . ILE   A  1  344 ? 25.967  -14.900 -21.306  1.00 60.13  ? 344  ILE   A HA   1 
ATOM   5194  H  HB   . ILE   A  1  344 ? 26.512  -17.441 -22.424  1.00 63.31  ? 344  ILE   A HB   1 
ATOM   5195  H  HG12 . ILE   A  1  344 ? 26.991  -16.805 -19.718  1.00 61.99  ? 344  ILE   A HG12 1 
ATOM   5196  H  HG13 . ILE   A  1  344 ? 25.648  -17.525 -20.169  1.00 61.99  ? 344  ILE   A HG13 1 
ATOM   5197  H  HG21 . ILE   A  1  344 ? 28.751  -17.011 -21.889  1.00 64.76  ? 344  ILE   A HG21 1 
ATOM   5198  H  HG22 . ILE   A  1  344 ? 28.200  -15.906 -22.889  1.00 64.76  ? 344  ILE   A HG22 1 
ATOM   5199  H  HG23 . ILE   A  1  344 ? 28.339  -15.578 -21.341  1.00 64.76  ? 344  ILE   A HG23 1 
ATOM   5200  H  HD11 . ILE   A  1  344 ? 27.126  -19.089 -19.353  1.00 66.78  ? 344  ILE   A HD11 1 
ATOM   5201  H  HD12 . ILE   A  1  344 ? 26.888  -19.350 -20.902  1.00 66.78  ? 344  ILE   A HD12 1 
ATOM   5202  H  HD13 . ILE   A  1  344 ? 28.218  -18.632 -20.413  1.00 66.78  ? 344  ILE   A HD13 1 
ATOM   5203  N  N    . ALA   A  1  345 ? 26.026  -13.780 -23.481  1.00 54.09  ? 345  ALA   A N    1 
ATOM   5204  C  CA   . ALA   A  1  345 ? 25.944  -13.115 -24.780  1.00 51.59  ? 345  ALA   A CA   1 
ATOM   5205  C  C    . ALA   A  1  345 ? 27.298  -12.578 -25.213  1.00 52.00  ? 345  ALA   A C    1 
ATOM   5206  O  O    . ALA   A  1  345 ? 27.796  -11.606 -24.612  1.00 52.81  ? 345  ALA   A O    1 
ATOM   5207  C  CB   . ALA   A  1  345 ? 24.925  -11.974 -24.726  1.00 50.93  ? 345  ALA   A CB   1 
ATOM   5208  H  H    . ALA   A  1  345 ? 26.270  -13.264 -22.838  1.00 64.95  ? 345  ALA   A H    1 
ATOM   5209  H  HA   . ALA   A  1  345 ? 25.667  -13.770 -25.439  1.00 61.94  ? 345  ALA   A HA   1 
ATOM   5210  H  HB1  . ALA   A  1  345 ? 24.869  -11.559 -25.601  1.00 61.16  ? 345  ALA   A HB1  1 
ATOM   5211  H  HB2  . ALA   A  1  345 ? 24.060  -12.335 -24.476  1.00 61.16  ? 345  ALA   A HB2  1 
ATOM   5212  H  HB3  . ALA   A  1  345 ? 25.215  -11.323 -24.068  1.00 61.16  ? 345  ALA   A HB3  1 
ATOM   5213  N  N    . PRO   A  1  346 ? 27.936  -13.159 -26.227  1.00 51.94  ? 346  PRO   A N    1 
ATOM   5214  C  CA   . PRO   A  1  346 ? 29.076  -12.483 -26.853  1.00 53.77  ? 346  PRO   A CA   1 
ATOM   5215  C  C    . PRO   A  1  346 ? 28.690  -11.067 -27.255  1.00 60.42  ? 346  PRO   A C    1 
ATOM   5216  O  O    . PRO   A  1  346 ? 27.610  -10.828 -27.799  1.00 62.14  ? 346  PRO   A O    1 
ATOM   5217  C  CB   . PRO   A  1  346 ? 29.385  -13.361 -28.070  1.00 53.86  ? 346  PRO   A CB   1 
ATOM   5218  C  CG   . PRO   A  1  346 ? 28.894  -14.715 -27.685  1.00 53.43  ? 346  PRO   A CG   1 
ATOM   5219  C  CD   . PRO   A  1  346 ? 27.682  -14.482 -26.827  1.00 51.06  ? 346  PRO   A CD   1 
ATOM   5220  H  HA   . PRO   A  1  346 ? 29.849  -12.468 -26.267  1.00 64.56  ? 346  PRO   A HA   1 
ATOM   5221  H  HB2  . PRO   A  1  346 ? 28.913  -13.027 -28.849  1.00 64.67  ? 346  PRO   A HB2  1 
ATOM   5222  H  HB3  . PRO   A  1  346 ? 30.340  -13.371 -28.239  1.00 64.67  ? 346  PRO   A HB3  1 
ATOM   5223  H  HG2  . PRO   A  1  346 ? 28.661  -15.217 -28.482  1.00 64.16  ? 346  PRO   A HG2  1 
ATOM   5224  H  HG3  . PRO   A  1  346 ? 29.583  -15.183 -27.188  1.00 64.16  ? 346  PRO   A HG3  1 
ATOM   5225  H  HD2  . PRO   A  1  346 ? 26.876  -14.467 -27.366  1.00 61.30  ? 346  PRO   A HD2  1 
ATOM   5226  H  HD3  . PRO   A  1  346 ? 27.609  -15.163 -26.141  1.00 61.30  ? 346  PRO   A HD3  1 
ATOM   5227  N  N    . LEU   A  1  347 ? 29.582  -10.121 -26.972  1.00 62.33  ? 347  LEU   A N    1 
ATOM   5228  C  CA   . LEU   A  1  347 ? 29.309  -8.708  -27.177  1.00 63.44  ? 347  LEU   A CA   1 
ATOM   5229  C  C    . LEU   A  1  347 ? 30.132  -8.095  -28.298  1.00 65.24  ? 347  LEU   A C    1 
ATOM   5230  O  O    . LEU   A  1  347 ? 29.970  -6.904  -28.586  1.00 64.14  ? 347  LEU   A O    1 
ATOM   5231  C  CB   . LEU   A  1  347 ? 29.579  -7.930  -25.883  1.00 62.86  ? 347  LEU   A CB   1 
ATOM   5232  C  CG   . LEU   A  1  347 ? 28.708  -8.263  -24.674  1.00 62.84  ? 347  LEU   A CG   1 
ATOM   5233  C  CD1  . LEU   A  1  347 ? 29.199  -7.497  -23.455  1.00 59.58  ? 347  LEU   A CD1  1 
ATOM   5234  C  CD2  . LEU   A  1  347 ? 27.256  -7.943  -24.967  1.00 64.46  ? 347  LEU   A CD2  1 
ATOM   5235  H  H    . LEU   A  1  347 ? 30.366  -10.279 -26.655  1.00 74.83  ? 347  LEU   A H    1 
ATOM   5236  H  HA   . LEU   A  1  347 ? 28.372  -8.611  -27.406  1.00 76.16  ? 347  LEU   A HA   1 
ATOM   5237  H  HB2  . LEU   A  1  347 ? 30.498  -8.096  -25.622  1.00 75.47  ? 347  LEU   A HB2  1 
ATOM   5238  H  HB3  . LEU   A  1  347 ? 29.452  -6.987  -26.071  1.00 75.47  ? 347  LEU   A HB3  1 
ATOM   5239  H  HG   . LEU   A  1  347 ? 28.769  -9.211  -24.479  1.00 75.45  ? 347  LEU   A HG   1 
ATOM   5240  H  HD11 . LEU   A  1  347 ? 28.623  -7.701  -22.701  1.00 71.53  ? 347  LEU   A HD11 1 
ATOM   5241  H  HD12 . LEU   A  1  347 ? 30.110  -7.766  -23.258  1.00 71.53  ? 347  LEU   A HD12 1 
ATOM   5242  H  HD13 . LEU   A  1  347 ? 29.168  -6.546  -23.646  1.00 71.53  ? 347  LEU   A HD13 1 
ATOM   5243  H  HD21 . LEU   A  1  347 ? 26.729  -8.111  -24.170  1.00 77.39  ? 347  LEU   A HD21 1 
ATOM   5244  H  HD22 . LEU   A  1  347 ? 27.183  -7.010  -25.222  1.00 77.39  ? 347  LEU   A HD22 1 
ATOM   5245  H  HD23 . LEU   A  1  347 ? 26.948  -8.509  -25.692  1.00 77.39  ? 347  LEU   A HD23 1 
ATOM   5246  N  N    . GLY   A  1  348 ? 30.998  -8.870  -28.944  1.00 65.29  ? 348  GLY   A N    1 
ATOM   5247  C  CA   . GLY   A  1  348 ? 32.009  -8.245  -29.767  1.00 64.60  ? 348  GLY   A CA   1 
ATOM   5248  C  C    . GLY   A  1  348 ? 33.015  -7.538  -28.875  1.00 63.21  ? 348  GLY   A C    1 
ATOM   5249  O  O    . GLY   A  1  348 ? 33.215  -7.896  -27.710  1.00 62.87  ? 348  GLY   A O    1 
ATOM   5250  H  H    . GLY   A  1  348 ? 31.017  -9.730  -28.920  1.00 78.38  ? 348  GLY   A H    1 
ATOM   5251  H  HA2  . GLY   A  1  348 ? 32.469  -8.915  -30.297  1.00 77.56  ? 348  GLY   A HA2  1 
ATOM   5252  H  HA3  . GLY   A  1  348 ? 31.600  -7.597  -30.362  1.00 77.56  ? 348  GLY   A HA3  1 
ATOM   5253  N  N    . ASP   A  1  349 ? 33.650  -6.508  -29.424  1.00 66.02  ? 349  ASP   A N    1 
ATOM   5254  C  CA   . ASP   A  1  349 ? 34.581  -5.673  -28.665  1.00 64.39  ? 349  ASP   A CA   1 
ATOM   5255  C  C    . ASP   A  1  349 ? 33.802  -4.441  -28.212  1.00 62.20  ? 349  ASP   A C    1 
ATOM   5256  O  O    . ASP   A  1  349 ? 33.706  -3.443  -28.926  1.00 66.42  ? 349  ASP   A O    1 
ATOM   5257  C  CB   . ASP   A  1  349 ? 35.800  -5.309  -29.500  1.00 71.10  ? 349  ASP   A CB   1 
ATOM   5258  C  CG   . ASP   A  1  349 ? 36.942  -4.767  -28.659  1.00 75.78  ? 349  ASP   A CG   1 
ATOM   5259  O  OD1  . ASP   A  1  349 ? 36.798  -4.712  -27.419  1.00 76.03  ? 349  ASP   A OD1  1 
ATOM   5260  O  OD2  . ASP   A  1  349 ? 37.985  -4.399  -29.240  1.00 79.66  ? 349  ASP   A OD2  1 
ATOM   5261  H  H    . ASP   A  1  349 ? 33.558  -6.268  -30.245  1.00 79.26  ? 349  ASP   A H    1 
ATOM   5262  H  HA   . ASP   A  1  349 ? 34.893  -6.154  -27.883  1.00 77.31  ? 349  ASP   A HA   1 
ATOM   5263  H  HB2  . ASP   A  1  349 ? 36.116  -6.102  -29.962  1.00 85.36  ? 349  ASP   A HB2  1 
ATOM   5264  H  HB3  . ASP   A  1  349 ? 35.551  -4.627  -30.144  1.00 85.36  ? 349  ASP   A HB3  1 
ATOM   5265  N  N    . LEU   A  1  350 ? 33.238  -4.524  -27.005  1.00 57.14  ? 350  LEU   A N    1 
ATOM   5266  C  CA   . LEU   A  1  350 ? 32.385  -3.451  -26.504  1.00 60.40  ? 350  LEU   A CA   1 
ATOM   5267  C  C    . LEU   A  1  350 ? 33.162  -2.147  -26.363  1.00 68.00  ? 350  LEU   A C    1 
ATOM   5268  O  O    . LEU   A  1  350 ? 32.697  -1.085  -26.796  1.00 71.30  ? 350  LEU   A O    1 
ATOM   5269  C  CB   . LEU   A  1  350 ? 31.769  -3.865  -25.167  1.00 59.16  ? 350  LEU   A CB   1 
ATOM   5270  C  CG   . LEU   A  1  350 ? 30.892  -2.837  -24.449  1.00 64.55  ? 350  LEU   A CG   1 
ATOM   5271  C  CD1  . LEU   A  1  350 ? 29.666  -2.474  -25.274  1.00 69.52  ? 350  LEU   A CD1  1 
ATOM   5272  C  CD2  . LEU   A  1  350 ? 30.485  -3.371  -23.086  1.00 61.24  ? 350  LEU   A CD2  1 
ATOM   5273  H  H    . LEU   A  1  350 ? 33.333  -5.185  -26.463  1.00 68.60  ? 350  LEU   A H    1 
ATOM   5274  H  HA   . LEU   A  1  350 ? 31.666  -3.298  -27.137  1.00 72.51  ? 350  LEU   A HA   1 
ATOM   5275  H  HB2  . LEU   A  1  350 ? 31.217  -4.646  -25.323  1.00 71.03  ? 350  LEU   A HB2  1 
ATOM   5276  H  HB3  . LEU   A  1  350 ? 32.495  -4.087  -24.562  1.00 71.03  ? 350  LEU   A HB3  1 
ATOM   5277  H  HG   . LEU   A  1  350 ? 31.403  -2.021  -24.327  1.00 77.49  ? 350  LEU   A HG   1 
ATOM   5278  H  HD11 . LEU   A  1  350 ? 29.144  -1.815  -24.790  1.00 83.47  ? 350  LEU   A HD11 1 
ATOM   5279  H  HD12 . LEU   A  1  350 ? 29.955  -2.108  -26.124  1.00 83.47  ? 350  LEU   A HD12 1 
ATOM   5280  H  HD13 . LEU   A  1  350 ? 29.136  -3.273  -25.420  1.00 83.47  ? 350  LEU   A HD13 1 
ATOM   5281  H  HD21 . LEU   A  1  350 ? 29.949  -2.702  -22.632  1.00 73.52  ? 350  LEU   A HD21 1 
ATOM   5282  H  HD22 . LEU   A  1  350 ? 29.968  -4.183  -23.206  1.00 73.52  ? 350  LEU   A HD22 1 
ATOM   5283  H  HD23 . LEU   A  1  350 ? 31.284  -3.561  -22.570  1.00 73.52  ? 350  LEU   A HD23 1 
ATOM   5284  N  N    . ASP   A  1  351 ? 34.350  -2.203  -25.762  1.00 67.13  ? 351  ASP   A N    1 
ATOM   5285  C  CA   . ASP   A  1  351 ? 35.153  -1.011  -25.522  1.00 71.97  ? 351  ASP   A CA   1 
ATOM   5286  C  C    . ASP   A  1  351 ? 36.202  -0.774  -26.604  1.00 75.37  ? 351  ASP   A C    1 
ATOM   5287  O  O    . ASP   A  1  351 ? 37.026  0.135   -26.462  1.00 79.31  ? 351  ASP   A O    1 
ATOM   5288  C  CB   . ASP   A  1  351 ? 35.825  -1.093  -24.147  1.00 73.13  ? 351  ASP   A CB   1 
ATOM   5289  C  CG   . ASP   A  1  351 ? 36.689  -2.324  -23.990  1.00 73.22  ? 351  ASP   A CG   1 
ATOM   5290  O  OD1  . ASP   A  1  351 ? 36.301  -3.390  -24.507  1.00 70.12  ? 351  ASP   A OD1  1 
ATOM   5291  O  OD2  . ASP   A  1  351 ? 37.755  -2.224  -23.346  1.00 76.39  ? 351  ASP   A OD2  1 
ATOM   5292  H  H    . ASP   A  1  351 ? 34.714  -2.930  -25.482  1.00 80.60  ? 351  ASP   A H    1 
ATOM   5293  H  HA   . ASP   A  1  351 ? 34.560  -0.243  -25.518  1.00 86.41  ? 351  ASP   A HA   1 
ATOM   5294  H  HB2  . ASP   A  1  351 ? 36.389  -0.313  -24.025  1.00 87.80  ? 351  ASP   A HB2  1 
ATOM   5295  H  HB3  . ASP   A  1  351 ? 35.139  -1.118  -23.462  1.00 87.80  ? 351  ASP   A HB3  1 
ATOM   5296  N  N    . GLN   A  1  352 ? 36.185  -1.560  -27.681  1.00 75.34  ? 352  GLN   A N    1 
ATOM   5297  C  CA   . GLN   A  1  352 ? 37.092  -1.370  -28.814  1.00 77.51  ? 352  GLN   A CA   1 
ATOM   5298  C  C    . GLN   A  1  352 ? 38.542  -1.256  -28.348  1.00 81.56  ? 352  GLN   A C    1 
ATOM   5299  O  O    . GLN   A  1  352 ? 39.283  -0.353  -28.744  1.00 86.77  ? 352  GLN   A O    1 
ATOM   5300  C  CB   . GLN   A  1  352 ? 36.687  -0.144  -29.635  1.00 79.09  ? 352  GLN   A CB   1 
ATOM   5301  C  CG   . GLN   A  1  352 ? 35.427  -0.335  -30.465  1.00 78.17  ? 352  GLN   A CG   1 
ATOM   5302  C  CD   . GLN   A  1  352 ? 35.597  -1.378  -31.552  1.00 76.45  ? 352  GLN   A CD   1 
ATOM   5303  O  OE1  . GLN   A  1  352 ? 36.284  -1.148  -32.548  1.00 79.65  ? 352  GLN   A OE1  1 
ATOM   5304  N  NE2  . GLN   A  1  352 ? 34.974  -2.534  -31.365  1.00 67.49  ? 352  GLN   A NE2  1 
ATOM   5305  H  H    . GLN   A  1  352 ? 35.646  -2.223  -27.781  1.00 90.44  ? 352  GLN   A H    1 
ATOM   5306  H  HA   . GLN   A  1  352 ? 37.029  -2.153  -29.384  1.00 93.05  ? 352  GLN   A HA   1 
ATOM   5307  H  HB2  . GLN   A  1  352 ? 36.531  0.597   -29.029  1.00 94.95  ? 352  GLN   A HB2  1 
ATOM   5308  H  HB3  . GLN   A  1  352 ? 37.410  0.073   -30.245  1.00 94.95  ? 352  GLN   A HB3  1 
ATOM   5309  H  HG2  . GLN   A  1  352 ? 34.706  -0.623  -29.883  1.00 93.84  ? 352  GLN   A HG2  1 
ATOM   5310  H  HG3  . GLN   A  1  352 ? 35.196  0.506   -30.889  1.00 93.84  ? 352  GLN   A HG3  1 
ATOM   5311  H  HE21 . GLN   A  1  352 ? 34.505  -2.660  -30.655  1.00 80.80  ? 352  GLN   A HE21 1 
ATOM   5312  H  HE22 . GLN   A  1  352 ? 35.040  -3.158  -31.953  1.00 80.80  ? 352  GLN   A HE22 1 
ATOM   5313  N  N    . ASP   A  1  353 ? 38.951  -2.193  -27.496  1.00 80.93  ? 353  ASP   A N    1 
ATOM   5314  C  CA   . ASP   A  1  353 ? 40.316  -2.242  -26.993  1.00 82.13  ? 353  ASP   A CA   1 
ATOM   5315  C  C    . ASP   A  1  353 ? 41.143  -3.346  -27.636  1.00 78.30  ? 353  ASP   A C    1 
ATOM   5316  O  O    . ASP   A  1  353 ? 42.327  -3.483  -27.313  1.00 80.91  ? 353  ASP   A O    1 
ATOM   5317  C  CB   . ASP   A  1  353 ? 40.313  -2.419  -25.469  1.00 86.94  ? 353  ASP   A CB   1 
ATOM   5318  C  CG   . ASP   A  1  353 ? 39.836  -3.794  -25.038  1.00 87.21  ? 353  ASP   A CG   1 
ATOM   5319  O  OD1  . ASP   A  1  353 ? 39.183  -4.487  -25.848  1.00 85.77  ? 353  ASP   A OD1  1 
ATOM   5320  O  OD2  . ASP   A  1  353 ? 40.109  -4.178  -23.881  1.00 87.35  ? 353  ASP   A OD2  1 
ATOM   5321  H  H    . ASP   A  1  353 ? 38.446  -2.820  -27.191  1.00 97.16  ? 353  ASP   A H    1 
ATOM   5322  H  HA   . ASP   A  1  353 ? 40.748  -1.396  -27.190  1.00 98.59  ? 353  ASP   A HA   1 
ATOM   5323  H  HB2  . ASP   A  1  353 ? 41.215  -2.296  -25.135  1.00 104.37 ? 353  ASP   A HB2  1 
ATOM   5324  H  HB3  . ASP   A  1  353 ? 39.720  -1.759  -25.076  1.00 104.37 ? 353  ASP   A HB3  1 
ATOM   5325  N  N    . GLY   A  1  354 ? 40.555  -4.130  -28.540  1.00 76.00  ? 354  GLY   A N    1 
ATOM   5326  C  CA   . GLY   A  1  354 ? 41.255  -5.207  -29.210  1.00 78.67  ? 354  GLY   A CA   1 
ATOM   5327  C  C    . GLY   A  1  354 ? 40.899  -6.596  -28.726  1.00 78.15  ? 354  GLY   A C    1 
ATOM   5328  O  O    . GLY   A  1  354 ? 41.421  -7.573  -29.277  1.00 78.19  ? 354  GLY   A O    1 
ATOM   5329  H  H    . GLY   A  1  354 ? 39.733  -4.050  -28.781  1.00 91.23  ? 354  GLY   A H    1 
ATOM   5330  H  HA2  . GLY   A  1  354 ? 41.055  -5.164  -30.158  1.00 94.45  ? 354  GLY   A HA2  1 
ATOM   5331  H  HA3  . GLY   A  1  354 ? 42.209  -5.085  -29.082  1.00 94.45  ? 354  GLY   A HA3  1 
ATOM   5332  N  N    . PHE   A  1  355 ? 40.038  -6.724  -27.719  1.00 75.82  ? 355  PHE   A N    1 
ATOM   5333  C  CA   . PHE   A  1  355 ? 39.625  -8.020  -27.204  1.00 72.16  ? 355  PHE   A CA   1 
ATOM   5334  C  C    . PHE   A  1  355 ? 38.112  -8.066  -27.081  1.00 67.73  ? 355  PHE   A C    1 
ATOM   5335  O  O    . PHE   A  1  355 ? 37.488  -7.113  -26.606  1.00 67.93  ? 355  PHE   A O    1 
ATOM   5336  C  CB   . PHE   A  1  355 ? 40.252  -8.312  -25.841  1.00 72.53  ? 355  PHE   A CB   1 
ATOM   5337  C  CG   . PHE   A  1  355 ? 41.745  -8.343  -25.865  1.00 73.81  ? 355  PHE   A CG   1 
ATOM   5338  C  CD1  . PHE   A  1  355 ? 42.417  -9.444  -26.364  1.00 76.01  ? 355  PHE   A CD1  1 
ATOM   5339  C  CD2  . PHE   A  1  355 ? 42.478  -7.272  -25.391  1.00 74.06  ? 355  PHE   A CD2  1 
ATOM   5340  C  CE1  . PHE   A  1  355 ? 43.795  -9.476  -26.390  1.00 79.09  ? 355  PHE   A CE1  1 
ATOM   5341  C  CE2  . PHE   A  1  355 ? 43.856  -7.296  -25.411  1.00 77.67  ? 355  PHE   A CE2  1 
ATOM   5342  C  CZ   . PHE   A  1  355 ? 44.517  -8.400  -25.912  1.00 78.60  ? 355  PHE   A CZ   1 
ATOM   5343  H  H    . PHE   A  1  355 ? 39.674  -6.059  -27.312  1.00 91.02  ? 355  PHE   A H    1 
ATOM   5344  H  HA   . PHE   A  1  355 ? 39.906  -8.710  -27.825  1.00 86.62  ? 355  PHE   A HA   1 
ATOM   5345  H  HB2  . PHE   A  1  355 ? 39.980  -7.621  -25.217  1.00 87.07  ? 355  PHE   A HB2  1 
ATOM   5346  H  HB3  . PHE   A  1  355 ? 39.942  -9.178  -25.534  1.00 87.07  ? 355  PHE   A HB3  1 
ATOM   5347  H  HD1  . PHE   A  1  355 ? 41.935  -10.171 -26.686  1.00 91.25  ? 355  PHE   A HD1  1 
ATOM   5348  H  HD2  . PHE   A  1  355 ? 42.037  -6.526  -25.054  1.00 88.91  ? 355  PHE   A HD2  1 
ATOM   5349  H  HE1  . PHE   A  1  355 ? 44.238  -10.220 -26.728  1.00 94.95  ? 355  PHE   A HE1  1 
ATOM   5350  H  HE2  . PHE   A  1  355 ? 44.340  -6.570  -25.089  1.00 93.24  ? 355  PHE   A HE2  1 
ATOM   5351  H  HZ   . PHE   A  1  355 ? 45.446  -8.419  -25.928  1.00 94.36  ? 355  PHE   A HZ   1 
ATOM   5352  N  N    . ASN   A  1  356 ? 37.531  -9.181  -27.507  1.00 64.28  ? 356  ASN   A N    1 
ATOM   5353  C  CA   . ASN   A  1  356 ? 36.096  -9.353  -27.382  1.00 62.35  ? 356  ASN   A CA   1 
ATOM   5354  C  C    . ASN   A  1  356 ? 35.699  -9.412  -25.911  1.00 64.18  ? 356  ASN   A C    1 
ATOM   5355  O  O    . ASN   A  1  356 ? 36.511  -9.691  -25.024  1.00 65.75  ? 356  ASN   A O    1 
ATOM   5356  C  CB   . ASN   A  1  356 ? 35.641  -10.615 -28.110  1.00 57.73  ? 356  ASN   A CB   1 
ATOM   5357  C  CG   . ASN   A  1  356 ? 35.770  -10.490 -29.616  1.00 60.42  ? 356  ASN   A CG   1 
ATOM   5358  O  OD1  . ASN   A  1  356 ? 35.644  -9.399  -30.171  1.00 61.17  ? 356  ASN   A OD1  1 
ATOM   5359  N  ND2  . ASN   A  1  356 ? 36.025  -11.608 -30.285  1.00 62.34  ? 356  ASN   A ND2  1 
ATOM   5360  H  H    . ASN   A  1  356 ? 37.943  -9.844  -27.868  1.00 77.17  ? 356  ASN   A H    1 
ATOM   5361  H  HA   . ASN   A  1  356 ? 35.638  -8.600  -27.787  1.00 74.86  ? 356  ASN   A HA   1 
ATOM   5362  H  HB2  . ASN   A  1  356 ? 36.188  -11.362 -27.822  1.00 69.31  ? 356  ASN   A HB2  1 
ATOM   5363  H  HB3  . ASN   A  1  356 ? 34.710  -10.785 -27.901  1.00 69.31  ? 356  ASN   A HB3  1 
ATOM   5364  H  HD21 . ASN   A  1  356 ? 36.107  -11.588 -31.141  1.00 74.84  ? 356  ASN   A HD21 1 
ATOM   5365  H  HD22 . ASN   A  1  356 ? 36.109  -12.352 -29.862  1.00 74.84  ? 356  ASN   A HD22 1 
ATOM   5366  N  N    . ASP   A  1  357 ? 34.425  -9.136  -25.664  1.00 64.64  ? 357  ASP   A N    1 
ATOM   5367  C  CA   . ASP   A  1  357 ? 33.866  -9.040  -24.326  1.00 64.59  ? 357  ASP   A CA   1 
ATOM   5368  C  C    . ASP   A  1  357 ? 32.618  -9.911  -24.277  1.00 64.90  ? 357  ASP   A C    1 
ATOM   5369  O  O    . ASP   A  1  357 ? 32.281  -10.599 -25.246  1.00 67.88  ? 357  ASP   A O    1 
ATOM   5370  C  CB   . ASP   A  1  357 ? 33.586  -7.574  -23.979  1.00 67.14  ? 357  ASP   A CB   1 
ATOM   5371  C  CG   . ASP   A  1  357 ? 34.782  -6.674  -24.275  1.00 73.74  ? 357  ASP   A CG   1 
ATOM   5372  O  OD1  . ASP   A  1  357 ? 35.895  -6.997  -23.810  1.00 76.11  ? 357  ASP   A OD1  1 
ATOM   5373  O  OD2  . ASP   A  1  357 ? 34.623  -5.664  -24.993  1.00 77.09  ? 357  ASP   A OD2  1 
ATOM   5374  H  H    . ASP   A  1  357 ? 33.843  -8.995  -26.282  1.00 77.60  ? 357  ASP   A H    1 
ATOM   5375  H  HA   . ASP   A  1  357 ? 34.482  -9.382  -23.659  1.00 77.54  ? 357  ASP   A HA   1 
ATOM   5376  H  HB2  . ASP   A  1  357 ? 32.834  -7.260  -24.505  1.00 80.61  ? 357  ASP   A HB2  1 
ATOM   5377  H  HB3  . ASP   A  1  357 ? 33.382  -7.504  -23.033  1.00 80.61  ? 357  ASP   A HB3  1 
ATOM   5378  N  N    . ILE   A  1  358 ? 31.923  -9.903  -23.141  1.00 63.48  ? 358  ILE   A N    1 
ATOM   5379  C  CA   . ILE   A  1  358 ? 30.827  -10.841 -22.941  1.00 60.02  ? 358  ILE   A CA   1 
ATOM   5380  C  C    . ILE   A  1  358 ? 29.969  -10.360 -21.785  1.00 55.50  ? 358  ILE   A C    1 
ATOM   5381  O  O    . ILE   A  1  358 ? 30.470  -9.783  -20.817  1.00 54.29  ? 358  ILE   A O    1 
ATOM   5382  C  CB   . ILE   A  1  358 ? 31.379  -12.271 -22.703  1.00 60.22  ? 358  ILE   A CB   1 
ATOM   5383  C  CG1  . ILE   A  1  358 ? 30.321  -13.325 -23.023  1.00 62.71  ? 358  ILE   A CG1  1 
ATOM   5384  C  CG2  . ILE   A  1  358 ? 31.880  -12.429 -21.270  1.00 61.21  ? 358  ILE   A CG2  1 
ATOM   5385  C  CD1  . ILE   A  1  358 ? 30.919  -14.664 -23.400  1.00 66.39  ? 358  ILE   A CD1  1 
ATOM   5386  H  H    . ILE   A  1  358 ? 32.067  -9.370  -22.482  1.00 76.22  ? 358  ILE   A H    1 
ATOM   5387  H  HA   . ILE   A  1  358 ? 30.263  -10.847 -23.731  1.00 72.06  ? 358  ILE   A HA   1 
ATOM   5388  H  HB   . ILE   A  1  358 ? 32.128  -12.402 -23.305  1.00 72.30  ? 358  ILE   A HB   1 
ATOM   5389  H  HG12 . ILE   A  1  358 ? 29.760  -13.457 -22.242  1.00 75.29  ? 358  ILE   A HG12 1 
ATOM   5390  H  HG13 . ILE   A  1  358 ? 29.783  -13.016 -23.769  1.00 75.29  ? 358  ILE   A HG13 1 
ATOM   5391  H  HG21 . ILE   A  1  358 ? 32.293  -13.301 -21.174  1.00 73.49  ? 358  ILE   A HG21 1 
ATOM   5392  H  HG22 . ILE   A  1  358 ? 32.529  -11.733 -21.084  1.00 73.49  ? 358  ILE   A HG22 1 
ATOM   5393  H  HG23 . ILE   A  1  358 ? 31.128  -12.351 -20.662  1.00 73.49  ? 358  ILE   A HG23 1 
ATOM   5394  H  HD11 . ILE   A  1  358 ? 30.201  -15.283 -23.609  1.00 79.70  ? 358  ILE   A HD11 1 
ATOM   5395  H  HD12 . ILE   A  1  358 ? 31.491  -14.548 -24.174  1.00 79.70  ? 358  ILE   A HD12 1 
ATOM   5396  H  HD13 . ILE   A  1  358 ? 31.438  -15.000 -22.652  1.00 79.70  ? 358  ILE   A HD13 1 
ATOM   5397  N  N    . ALA   A  1  359 ? 28.665  -10.603 -21.891  1.00 53.09  ? 359  ALA   A N    1 
ATOM   5398  C  CA   . ALA   A  1  359 ? 27.708  -10.304 -20.836  1.00 54.01  ? 359  ALA   A CA   1 
ATOM   5399  C  C    . ALA   A  1  359 ? 27.143  -11.602 -20.277  1.00 52.73  ? 359  ALA   A C    1 
ATOM   5400  O  O    . ALA   A  1  359 ? 26.844  -12.536 -21.028  1.00 54.89  ? 359  ALA   A O    1 
ATOM   5401  C  CB   . ALA   A  1  359 ? 26.568  -9.423  -21.354  1.00 55.09  ? 359  ALA   A CB   1 
ATOM   5402  H  H    . ALA   A  1  359 ? 28.301  -10.952 -22.588  1.00 63.74  ? 359  ALA   A H    1 
ATOM   5403  H  HA   . ALA   A  1  359 ? 28.156  -9.827  -20.120  1.00 64.85  ? 359  ALA   A HA   1 
ATOM   5404  H  HB1  . ALA   A  1  359 ? 25.940  -9.263  -20.632  1.00 66.14  ? 359  ALA   A HB1  1 
ATOM   5405  H  HB2  . ALA   A  1  359 ? 26.935  -8.582  -21.666  1.00 66.14  ? 359  ALA   A HB2  1 
ATOM   5406  H  HB3  . ALA   A  1  359 ? 26.122  -9.881  -22.084  1.00 66.14  ? 359  ALA   A HB3  1 
ATOM   5407  N  N    . ILE   A  1  360 ? 26.999  -11.654 -18.955  1.00 49.93  ? 360  ILE   A N    1 
ATOM   5408  C  CA   . ILE   A  1  360 ? 26.446  -12.809 -18.259  1.00 49.84  ? 360  ILE   A CA   1 
ATOM   5409  C  C    . ILE   A  1  360 ? 25.288  -12.326 -17.400  1.00 51.04  ? 360  ILE   A C    1 
ATOM   5410  O  O    . ILE   A  1  360 ? 25.451  -11.403 -16.593  1.00 53.39  ? 360  ILE   A O    1 
ATOM   5411  C  CB   . ILE   A  1  360 ? 27.507  -13.520 -17.397  1.00 51.27  ? 360  ILE   A CB   1 
ATOM   5412  C  CG1  . ILE   A  1  360 ? 28.612  -14.082 -18.294  1.00 49.10  ? 360  ILE   A CG1  1 
ATOM   5413  C  CG2  . ILE   A  1  360 ? 26.868  -14.629 -16.569  1.00 51.99  ? 360  ILE   A CG2  1 
ATOM   5414  C  CD1  . ILE   A  1  360 ? 29.848  -14.519 -17.546  1.00 49.78  ? 360  ILE   A CD1  1 
ATOM   5415  H  H    . ILE   A  1  360 ? 27.222  -11.013 -18.427  1.00 59.95  ? 360  ILE   A H    1 
ATOM   5416  H  HA   . ILE   A  1  360 ? 26.105  -13.448 -18.904  1.00 59.84  ? 360  ILE   A HA   1 
ATOM   5417  H  HB   . ILE   A  1  360 ? 27.897  -12.874 -16.788  1.00 61.56  ? 360  ILE   A HB   1 
ATOM   5418  H  HG12 . ILE   A  1  360 ? 28.265  -14.855 -18.767  1.00 58.96  ? 360  ILE   A HG12 1 
ATOM   5419  H  HG13 . ILE   A  1  360 ? 28.877  -13.397 -18.928  1.00 58.96  ? 360  ILE   A HG13 1 
ATOM   5420  H  HG21 . ILE   A  1  360 ? 27.562  -15.098 -16.079  1.00 62.42  ? 360  ILE   A HG21 1 
ATOM   5421  H  HG22 . ILE   A  1  360 ? 26.234  -14.236 -15.949  1.00 62.42  ? 360  ILE   A HG22 1 
ATOM   5422  H  HG23 . ILE   A  1  360 ? 26.410  -15.244 -17.163  1.00 62.42  ? 360  ILE   A HG23 1 
ATOM   5423  H  HD11 . ILE   A  1  360 ? 30.507  -14.837 -18.183  1.00 59.77  ? 360  ILE   A HD11 1 
ATOM   5424  H  HD12 . ILE   A  1  360 ? 30.203  -13.762 -17.054  1.00 59.77  ? 360  ILE   A HD12 1 
ATOM   5425  H  HD13 . ILE   A  1  360 ? 29.611  -15.231 -16.932  1.00 59.77  ? 360  ILE   A HD13 1 
ATOM   5426  N  N    . ALA   A  1  361 ? 24.127  -12.948 -17.566  1.00 49.96  ? 361  ALA   A N    1 
ATOM   5427  C  CA   . ALA   A  1  361 ? 22.915  -12.512 -16.894  1.00 50.46  ? 361  ALA   A CA   1 
ATOM   5428  C  C    . ALA   A  1  361 ? 22.686  -13.294 -15.607  1.00 53.21  ? 361  ALA   A C    1 
ATOM   5429  O  O    . ALA   A  1  361 ? 22.931  -14.502 -15.543  1.00 51.84  ? 361  ALA   A O    1 
ATOM   5430  C  CB   . ALA   A  1  361 ? 21.704  -12.669 -17.815  1.00 50.34  ? 361  ALA   A CB   1 
ATOM   5431  H  H    . ALA   A  1  361 ? 24.017  -13.635 -18.072  1.00 59.99  ? 361  ALA   A H    1 
ATOM   5432  H  HA   . ALA   A  1  361 ? 23.011  -11.577 -16.654  1.00 60.59  ? 361  ALA   A HA   1 
ATOM   5433  H  HB1  . ALA   A  1  361 ? 20.910  -12.369 -17.345  1.00 60.44  ? 361  ALA   A HB1  1 
ATOM   5434  H  HB2  . ALA   A  1  361 ? 21.840  -12.132 -18.610  1.00 60.44  ? 361  ALA   A HB2  1 
ATOM   5435  H  HB3  . ALA   A  1  361 ? 21.611  -13.603 -18.058  1.00 60.44  ? 361  ALA   A HB3  1 
ATOM   5436  N  N    . ALA   A  1  362 ? 22.223  -12.582 -14.577  1.00 57.88  ? 362  ALA   A N    1 
ATOM   5437  C  CA   . ALA   A  1  362 ? 21.695  -13.167 -13.346  1.00 55.63  ? 362  ALA   A CA   1 
ATOM   5438  C  C    . ALA   A  1  362 ? 20.228  -12.755 -13.290  1.00 52.75  ? 362  ALA   A C    1 
ATOM   5439  O  O    . ALA   A  1  362 ? 19.866  -11.803 -12.582  1.00 54.83  ? 362  ALA   A O    1 
ATOM   5440  C  CB   . ALA   A  1  362 ? 22.469  -12.697 -12.117  1.00 54.95  ? 362  ALA   A CB   1 
ATOM   5441  H  H    . ALA   A  1  362 ? 22.205  -11.722 -14.570  1.00 69.49  ? 362  ALA   A H    1 
ATOM   5442  H  HA   . ALA   A  1  362 ? 21.763  -14.134 -13.363  1.00 66.79  ? 362  ALA   A HA   1 
ATOM   5443  H  HB1  . ALA   A  1  362 ? 22.084  -13.106 -11.326  1.00 65.98  ? 362  ALA   A HB1  1 
ATOM   5444  H  HB2  . ALA   A  1  362 ? 23.398  -12.961 -12.209  1.00 65.98  ? 362  ALA   A HB2  1 
ATOM   5445  H  HB3  . ALA   A  1  362 ? 22.405  -11.731 -12.054  1.00 65.98  ? 362  ALA   A HB3  1 
ATOM   5446  N  N    . PRO   A  1  363 ? 19.354  -13.445 -14.029  1.00 53.32  ? 363  PRO   A N    1 
ATOM   5447  C  CA   . PRO   A  1  363 ? 18.021  -12.880 -14.304  1.00 52.08  ? 363  PRO   A CA   1 
ATOM   5448  C  C    . PRO   A  1  363 ? 17.150  -12.678 -13.077  1.00 56.37  ? 363  PRO   A C    1 
ATOM   5449  O  O    . PRO   A  1  363 ? 16.167  -11.932 -13.162  1.00 58.16  ? 363  PRO   A O    1 
ATOM   5450  C  CB   . PRO   A  1  363 ? 17.394  -13.906 -15.262  1.00 50.59  ? 363  PRO   A CB   1 
ATOM   5451  C  CG   . PRO   A  1  363 ? 18.537  -14.696 -15.804  1.00 52.14  ? 363  PRO   A CG   1 
ATOM   5452  C  CD   . PRO   A  1  363 ? 19.558  -14.733 -14.714  1.00 53.31  ? 363  PRO   A CD   1 
ATOM   5453  H  HA   . PRO   A  1  363 ? 18.125  -12.028 -14.755  1.00 62.53  ? 363  PRO   A HA   1 
ATOM   5454  H  HB2  . PRO   A  1  363 ? 16.780  -14.478 -14.775  1.00 60.74  ? 363  PRO   A HB2  1 
ATOM   5455  H  HB3  . PRO   A  1  363 ? 16.925  -13.445 -15.975  1.00 60.74  ? 363  PRO   A HB3  1 
ATOM   5456  H  HG2  . PRO   A  1  363 ? 18.240  -15.592 -16.027  1.00 62.61  ? 363  PRO   A HG2  1 
ATOM   5457  H  HG3  . PRO   A  1  363 ? 18.893  -14.258 -16.593  1.00 62.61  ? 363  PRO   A HG3  1 
ATOM   5458  H  HD2  . PRO   A  1  363 ? 19.395  -15.475 -14.112  1.00 64.00  ? 363  PRO   A HD2  1 
ATOM   5459  H  HD3  . PRO   A  1  363 ? 20.454  -14.793 -15.080  1.00 64.00  ? 363  PRO   A HD3  1 
ATOM   5460  N  N    . TYR   A  1  364 ? 17.462  -13.312 -11.946  1.00 59.08  ? 364  TYR   A N    1 
ATOM   5461  C  CA   . TYR   A  1  364 ? 16.639  -13.196 -10.747  1.00 60.62  ? 364  TYR   A CA   1 
ATOM   5462  C  C    . TYR   A  1  364 ? 17.385  -12.523 -9.603   1.00 60.70  ? 364  TYR   A C    1 
ATOM   5463  O  O    . TYR   A  1  364 ? 17.027  -12.709 -8.436   1.00 62.10  ? 364  TYR   A O    1 
ATOM   5464  C  CB   . TYR   A  1  364 ? 16.130  -14.576 -10.331  1.00 62.46  ? 364  TYR   A CB   1 
ATOM   5465  C  CG   . TYR   A  1  364 ? 15.479  -15.316 -11.476  1.00 62.55  ? 364  TYR   A CG   1 
ATOM   5466  C  CD1  . TYR   A  1  364 ? 14.236  -14.929 -11.956  1.00 61.29  ? 364  TYR   A CD1  1 
ATOM   5467  C  CD2  . TYR   A  1  364 ? 16.114  -16.388 -12.088  1.00 63.97  ? 364  TYR   A CD2  1 
ATOM   5468  C  CE1  . TYR   A  1  364 ? 13.638  -15.594 -13.008  1.00 61.83  ? 364  TYR   A CE1  1 
ATOM   5469  C  CE2  . TYR   A  1  364 ? 15.522  -17.060 -13.142  1.00 65.26  ? 364  TYR   A CE2  1 
ATOM   5470  C  CZ   . TYR   A  1  364 ? 14.285  -16.659 -13.598  1.00 64.32  ? 364  TYR   A CZ   1 
ATOM   5471  O  OH   . TYR   A  1  364 ? 13.689  -17.322 -14.646  1.00 65.98  ? 364  TYR   A OH   1 
ATOM   5472  H  H    . TYR   A  1  364 ? 18.152  -13.817 -11.850  1.00 70.94  ? 364  TYR   A H    1 
ATOM   5473  H  HA   . TYR   A  1  364 ? 15.868  -12.641 -10.946  1.00 72.78  ? 364  TYR   A HA   1 
ATOM   5474  H  HB2  . TYR   A  1  364 ? 16.877  -15.107 -10.013  1.00 74.99  ? 364  TYR   A HB2  1 
ATOM   5475  H  HB3  . TYR   A  1  364 ? 15.473  -14.473 -9.625   1.00 74.99  ? 364  TYR   A HB3  1 
ATOM   5476  H  HD1  . TYR   A  1  364 ? 13.797  -14.210 -11.562  1.00 73.59  ? 364  TYR   A HD1  1 
ATOM   5477  H  HD2  . TYR   A  1  364 ? 16.950  -16.658 -11.785  1.00 76.81  ? 364  TYR   A HD2  1 
ATOM   5478  H  HE1  . TYR   A  1  364 ? 12.804  -15.324 -13.318  1.00 74.24  ? 364  TYR   A HE1  1 
ATOM   5479  H  HE2  . TYR   A  1  364 ? 15.957  -17.779 -13.540  1.00 78.35  ? 364  TYR   A HE2  1 
ATOM   5480  H  HH   . TYR   A  1  364 ? 14.173  -17.963 -14.892  1.00 79.21  ? 364  TYR   A HH   1 
ATOM   5481  N  N    . GLY   A  1  365 ? 18.412  -11.736 -9.917   1.00 62.09  ? 365  GLY   A N    1 
ATOM   5482  C  CA   . GLY   A  1  365 ? 19.149  -10.991 -8.920   1.00 61.96  ? 365  GLY   A CA   1 
ATOM   5483  C  C    . GLY   A  1  365 ? 18.609  -9.585  -8.748   1.00 65.75  ? 365  GLY   A C    1 
ATOM   5484  O  O    . GLY   A  1  365 ? 17.578  -9.203  -9.306   1.00 66.99  ? 365  GLY   A O    1 
ATOM   5485  H  H    . GLY   A  1  365 ? 18.702  -11.620 -10.719  1.00 74.55  ? 365  GLY   A H    1 
ATOM   5486  H  HA2  . GLY   A  1  365 ? 19.090  -11.449 -8.067   1.00 74.39  ? 365  GLY   A HA2  1 
ATOM   5487  H  HA3  . GLY   A  1  365 ? 20.080  -10.933 -9.185   1.00 74.39  ? 365  GLY   A HA3  1 
ATOM   5488  N  N    . GLY   A  1  366 ? 19.330  -8.803  -7.953   1.00 70.21  ? 366  GLY   A N    1 
ATOM   5489  C  CA   . GLY   A  1  366 ? 18.951  -7.428  -7.719   1.00 76.55  ? 366  GLY   A CA   1 
ATOM   5490  C  C    . GLY   A  1  366 ? 17.752  -7.299  -6.793   1.00 86.49  ? 366  GLY   A C    1 
ATOM   5491  O  O    . GLY   A  1  366 ? 17.249  -8.264  -6.215   1.00 87.38  ? 366  GLY   A O    1 
ATOM   5492  H  H    . GLY   A  1  366 ? 20.043  -9.051  -7.539   1.00 84.29  ? 366  GLY   A H    1 
ATOM   5493  H  HA2  . GLY   A  1  366 ? 19.697  -6.955  -7.319   1.00 91.90  ? 366  GLY   A HA2  1 
ATOM   5494  H  HA3  . GLY   A  1  366 ? 18.729  -7.010  -8.565   1.00 91.90  ? 366  GLY   A HA3  1 
ATOM   5495  N  N    . GLU   A  1  367 ? 17.293  -6.056  -6.666   1.00 96.74  ? 367  GLU   A N    1 
ATOM   5496  C  CA   . GLU   A  1  367 ? 16.189  -5.747  -5.770   1.00 102.71 ? 367  GLU   A CA   1 
ATOM   5497  C  C    . GLU   A  1  367 ? 14.870  -6.218  -6.371   1.00 101.62 ? 367  GLU   A C    1 
ATOM   5498  O  O    . GLU   A  1  367 ? 14.586  -5.963  -7.545   1.00 97.84  ? 367  GLU   A O    1 
ATOM   5499  C  CB   . GLU   A  1  367 ? 16.139  -4.244  -5.500   1.00 109.89 ? 367  GLU   A CB   1 
ATOM   5500  C  CG   . GLU   A  1  367 ? 17.480  -3.638  -5.117   1.00 117.03 ? 367  GLU   A CG   1 
ATOM   5501  C  CD   . GLU   A  1  367 ? 17.381  -2.159  -4.800   1.00 128.09 ? 367  GLU   A CD   1 
ATOM   5502  O  OE1  . GLU   A  1  367 ? 16.674  -1.438  -5.534   1.00 133.01 ? 367  GLU   A OE1  1 
ATOM   5503  O  OE2  . GLU   A  1  367 ? 18.006  -1.720  -3.811   1.00 135.62 ? 367  GLU   A OE2  1 
ATOM   5504  H  H    . GLU   A  1  367 ? 17.606  -5.376  -7.089   1.00 116.13 ? 367  GLU   A H    1 
ATOM   5505  H  HA   . GLU   A  1  367 ? 16.320  -6.207  -4.926   1.00 123.29 ? 367  GLU   A HA   1 
ATOM   5506  H  HB2  . GLU   A  1  367 ? 15.831  -3.795  -6.303   1.00 131.91 ? 367  GLU   A HB2  1 
ATOM   5507  H  HB3  . GLU   A  1  367 ? 15.522  -4.080  -4.770   1.00 131.91 ? 367  GLU   A HB3  1 
ATOM   5508  H  HG2  . GLU   A  1  367 ? 17.820  -4.092  -4.330   1.00 140.47 ? 367  GLU   A HG2  1 
ATOM   5509  H  HG3  . GLU   A  1  367 ? 18.100  -3.746  -5.856   1.00 140.47 ? 367  GLU   A HG3  1 
ATOM   5510  N  N    . ASP   A  1  368 ? 14.063  -6.903  -5.561   1.00 103.55 ? 368  ASP   A N    1 
ATOM   5511  C  CA   . ASP   A  1  368 ? 12.754  -7.395  -5.991   1.00 105.91 ? 368  ASP   A CA   1 
ATOM   5512  C  C    . ASP   A  1  368 ? 12.867  -8.222  -7.270   1.00 98.09  ? 368  ASP   A C    1 
ATOM   5513  O  O    . ASP   A  1  368 ? 12.022  -8.146  -8.165   1.00 98.61  ? 368  ASP   A O    1 
ATOM   5514  C  CB   . ASP   A  1  368 ? 11.771  -6.237  -6.175   1.00 113.98 ? 368  ASP   A CB   1 
ATOM   5515  C  CG   . ASP   A  1  368 ? 11.411  -5.565  -4.863   1.00 122.24 ? 368  ASP   A CG   1 
ATOM   5516  O  OD1  . ASP   A  1  368 ? 12.328  -5.073  -4.172   1.00 124.76 ? 368  ASP   A OD1  1 
ATOM   5517  O  OD2  . ASP   A  1  368 ? 10.209  -5.527  -4.524   1.00 125.39 ? 368  ASP   A OD2  1 
ATOM   5518  H  H    . ASP   A  1  368 ? 14.254  -7.099  -4.746   1.00 124.30 ? 368  ASP   A H    1 
ATOM   5519  H  HA   . ASP   A  1  368 ? 12.405  -7.979  -5.300   1.00 127.13 ? 368  ASP   A HA   1 
ATOM   5520  H  HB2  . ASP   A  1  368 ? 12.173  -5.570  -6.754   1.00 136.81 ? 368  ASP   A HB2  1 
ATOM   5521  H  HB3  . ASP   A  1  368 ? 10.954  -6.574  -6.574   1.00 136.81 ? 368  ASP   A HB3  1 
ATOM   5522  N  N    . LYS   A  1  369 ? 13.928  -9.025  -7.353   1.00 92.70  ? 369  LYS   A N    1 
ATOM   5523  C  CA   . LYS   A  1  369 ? 14.147  -9.931  -8.480   1.00 86.59  ? 369  LYS   A CA   1 
ATOM   5524  C  C    . LYS   A  1  369 ? 14.006  -9.207  -9.818   1.00 81.50  ? 369  LYS   A C    1 
ATOM   5525  O  O    . LYS   A  1  369 ? 13.415  -9.724  -10.768  1.00 81.68  ? 369  LYS   A O    1 
ATOM   5526  C  CB   . LYS   A  1  369 ? 13.188  -11.125 -8.422   1.00 92.41  ? 369  LYS   A CB   1 
ATOM   5527  C  CG   . LYS   A  1  369 ? 13.300  -11.990 -7.172   1.00 97.36  ? 369  LYS   A CG   1 
ATOM   5528  C  CD   . LYS   A  1  369 ? 12.598  -13.332 -7.371   1.00 95.69  ? 369  LYS   A CD   1 
ATOM   5529  C  CE   . LYS   A  1  369 ? 11.794  -13.745 -6.147   1.00 100.60 ? 369  LYS   A CE   1 
ATOM   5530  N  NZ   . LYS   A  1  369 ? 10.558  -12.929 -5.991   1.00 104.29 ? 369  LYS   A NZ   1 
ATOM   5531  H  H    . LYS   A  1  369 ? 14.548  -9.064  -6.757   1.00 111.28 ? 369  LYS   A H    1 
ATOM   5532  H  HA   . LYS   A  1  369 ? 15.056  -10.263 -8.419   1.00 103.95 ? 369  LYS   A HA   1 
ATOM   5533  H  HB2  . LYS   A  1  369 ? 12.279  -10.789 -8.461   1.00 110.93 ? 369  LYS   A HB2  1 
ATOM   5534  H  HB3  . LYS   A  1  369 ? 13.365  -11.697 -9.185   1.00 110.93 ? 369  LYS   A HB3  1 
ATOM   5535  H  HG2  . LYS   A  1  369 ? 14.235  -12.158 -6.977   1.00 116.86 ? 369  LYS   A HG2  1 
ATOM   5536  H  HG3  . LYS   A  1  369 ? 12.882  -11.533 -6.425   1.00 116.86 ? 369  LYS   A HG3  1 
ATOM   5537  H  HD2  . LYS   A  1  369 ? 11.990  -13.266 -8.124   1.00 114.87 ? 369  LYS   A HD2  1 
ATOM   5538  H  HD3  . LYS   A  1  369 ? 13.264  -14.017 -7.541   1.00 114.87 ? 369  LYS   A HD3  1 
ATOM   5539  H  HE2  . LYS   A  1  369 ? 11.534  -14.675 -6.236   1.00 120.76 ? 369  LYS   A HE2  1 
ATOM   5540  H  HE3  . LYS   A  1  369 ? 12.338  -13.627 -5.353   1.00 120.76 ? 369  LYS   A HE3  1 
ATOM   5541  H  HZ1  . LYS   A  1  369 ? 10.118  -13.180 -5.260   1.00 125.19 ? 369  LYS   A HZ1  1 
ATOM   5542  H  HZ2  . LYS   A  1  369 ? 10.769  -12.067 -5.918   1.00 125.19 ? 369  LYS   A HZ2  1 
ATOM   5543  H  HZ3  . LYS   A  1  369 ? 10.029  -13.038 -6.698   1.00 125.19 ? 369  LYS   A HZ3  1 
ATOM   5544  N  N    . LYS   A  1  370 ? 14.557  -7.995  -9.899   1.00 77.80  ? 370  LYS   A N    1 
ATOM   5545  C  CA   . LYS   A  1  370 ? 14.470  -7.225  -11.134  1.00 78.79  ? 370  LYS   A CA   1 
ATOM   5546  C  C    . LYS   A  1  370 ? 15.523  -7.619  -12.161  1.00 76.58  ? 370  LYS   A C    1 
ATOM   5547  O  O    . LYS   A  1  370 ? 15.469  -7.125  -13.291  1.00 77.32  ? 370  LYS   A O    1 
ATOM   5548  C  CB   . LYS   A  1  370 ? 14.586  -5.727  -10.841  1.00 82.07  ? 370  LYS   A CB   1 
ATOM   5549  C  CG   . LYS   A  1  370 ? 13.337  -5.120  -10.224  1.00 81.62  ? 370  LYS   A CG   1 
ATOM   5550  C  CD   . LYS   A  1  370 ? 13.441  -3.606  -10.144  1.00 80.99  ? 370  LYS   A CD   1 
ATOM   5551  C  CE   . LYS   A  1  370 ? 12.340  -3.018  -9.278   1.00 83.83  ? 370  LYS   A CE   1 
ATOM   5552  N  NZ   . LYS   A  1  370 ? 12.465  -1.540  -9.146   1.00 89.50  ? 370  LYS   A NZ   1 
ATOM   5553  H  H    . LYS   A  1  370 ? 14.980  -7.604  -9.260   1.00 93.39  ? 370  LYS   A H    1 
ATOM   5554  H  HA   . LYS   A  1  370 ? 13.597  -7.384  -11.526  1.00 94.58  ? 370  LYS   A HA   1 
ATOM   5555  H  HB2  . LYS   A  1  370 ? 15.319  -5.588  -10.221  1.00 98.52  ? 370  LYS   A HB2  1 
ATOM   5556  H  HB3  . LYS   A  1  370 ? 14.762  -5.260  -11.673  1.00 98.52  ? 370  LYS   A HB3  1 
ATOM   5557  H  HG2  . LYS   A  1  370 ? 12.567  -5.345  -10.769  1.00 97.98  ? 370  LYS   A HG2  1 
ATOM   5558  H  HG3  . LYS   A  1  370 ? 13.220  -5.466  -9.326   1.00 97.98  ? 370  LYS   A HG3  1 
ATOM   5559  H  HD2  . LYS   A  1  370 ? 14.296  -3.363  -9.757   1.00 97.23  ? 370  LYS   A HD2  1 
ATOM   5560  H  HD3  . LYS   A  1  370 ? 13.361  -3.231  -11.035  1.00 97.23  ? 370  LYS   A HD3  1 
ATOM   5561  H  HE2  . LYS   A  1  370 ? 11.478  -3.214  -9.679   1.00 100.63 ? 370  LYS   A HE2  1 
ATOM   5562  H  HE3  . LYS   A  1  370 ? 12.389  -3.406  -8.391   1.00 100.63 ? 370  LYS   A HE3  1 
ATOM   5563  H  HZ1  . LYS   A  1  370 ? 11.826  -1.226  -8.612   1.00 107.44 ? 370  LYS   A HZ1  1 
ATOM   5564  H  HZ2  . LYS   A  1  370 ? 13.259  -1.331  -8.801   1.00 107.44 ? 370  LYS   A HZ2  1 
ATOM   5565  H  HZ3  . LYS   A  1  370 ? 12.388  -1.155  -9.945   1.00 107.44 ? 370  LYS   A HZ3  1 
ATOM   5566  N  N    . GLY   A  1  371 ? 16.469  -8.478  -11.804  1.00 72.32  ? 371  GLY   A N    1 
ATOM   5567  C  CA   . GLY   A  1  371 ? 17.439  -8.982  -12.767  1.00 65.54  ? 371  GLY   A CA   1 
ATOM   5568  C  C    . GLY   A  1  371 ? 18.687  -8.127  -12.846  1.00 63.82  ? 371  GLY   A C    1 
ATOM   5569  O  O    . GLY   A  1  371 ? 18.680  -6.928  -12.568  1.00 65.90  ? 371  GLY   A O    1 
ATOM   5570  H  H    . GLY   A  1  371 ? 16.571  -8.786  -11.008  1.00 86.82  ? 371  GLY   A H    1 
ATOM   5571  H  HA2  . GLY   A  1  371 ? 17.702  -9.881  -12.515  1.00 78.69  ? 371  GLY   A HA2  1 
ATOM   5572  H  HA3  . GLY   A  1  371 ? 17.032  -9.007  -13.647  1.00 78.69  ? 371  GLY   A HA3  1 
ATOM   5573  N  N    . ILE   A  1  372 ? 19.789  -8.767  -13.238  1.00 63.09  ? 372  ILE   A N    1 
ATOM   5574  C  CA   . ILE   A  1  372 ? 21.081  -8.101  -13.359  1.00 64.92  ? 372  ILE   A CA   1 
ATOM   5575  C  C    . ILE   A  1  372 ? 21.841  -8.720  -14.524  1.00 62.74  ? 372  ILE   A C    1 
ATOM   5576  O  O    . ILE   A  1  372 ? 21.720  -9.915  -14.804  1.00 60.85  ? 372  ILE   A O    1 
ATOM   5577  C  CB   . ILE   A  1  372 ? 21.897  -8.199  -12.047  1.00 65.65  ? 372  ILE   A CB   1 
ATOM   5578  C  CG1  . ILE   A  1  372 ? 21.287  -7.291  -10.976  1.00 66.44  ? 372  ILE   A CG1  1 
ATOM   5579  C  CG2  . ILE   A  1  372 ? 23.360  -7.835  -12.290  1.00 67.36  ? 372  ILE   A CG2  1 
ATOM   5580  C  CD1  . ILE   A  1  372 ? 21.899  -7.454  -9.602   1.00 71.04  ? 372  ILE   A CD1  1 
ATOM   5581  H  H    . ILE   A  1  372 ? 19.812  -9.602  -13.443  1.00 75.74  ? 372  ILE   A H    1 
ATOM   5582  H  HA   . ILE   A  1  372 ? 20.934  -7.163  -13.559  1.00 77.95  ? 372  ILE   A HA   1 
ATOM   5583  H  HB   . ILE   A  1  372 ? 21.861  -9.117  -11.734  1.00 78.81  ? 372  ILE   A HB   1 
ATOM   5584  H  HG12 . ILE   A  1  372 ? 21.412  -6.367  -11.245  1.00 79.77  ? 372  ILE   A HG12 1 
ATOM   5585  H  HG13 . ILE   A  1  372 ? 20.341  -7.490  -10.902  1.00 79.77  ? 372  ILE   A HG13 1 
ATOM   5586  H  HG21 . ILE   A  1  372 ? 23.829  -7.828  -11.441  1.00 80.87  ? 372  ILE   A HG21 1 
ATOM   5587  H  HG22 . ILE   A  1  372 ? 23.756  -8.495  -12.880  1.00 80.87  ? 372  ILE   A HG22 1 
ATOM   5588  H  HG23 . ILE   A  1  372 ? 23.403  -6.957  -12.699  1.00 80.87  ? 372  ILE   A HG23 1 
ATOM   5589  H  HD11 . ILE   A  1  372 ? 21.423  -6.888  -8.975   1.00 85.29  ? 372  ILE   A HD11 1 
ATOM   5590  H  HD12 . ILE   A  1  372 ? 21.824  -8.383  -9.332   1.00 85.29  ? 372  ILE   A HD12 1 
ATOM   5591  H  HD13 . ILE   A  1  372 ? 22.833  -7.195  -9.639   1.00 85.29  ? 372  ILE   A HD13 1 
ATOM   5592  N  N    . VAL   A  1  373 ? 22.632  -7.890  -15.203  1.00 61.66  ? 373  VAL   A N    1 
ATOM   5593  C  CA   . VAL   A  1  373 ? 23.517  -8.327  -16.277  1.00 61.81  ? 373  VAL   A CA   1 
ATOM   5594  C  C    . VAL   A  1  373 ? 24.917  -7.821  -15.968  1.00 60.88  ? 373  VAL   A C    1 
ATOM   5595  O  O    . VAL   A  1  373 ? 25.096  -6.658  -15.589  1.00 57.56  ? 373  VAL   A O    1 
ATOM   5596  C  CB   . VAL   A  1  373 ? 23.046  -7.814  -17.654  1.00 64.23  ? 373  VAL   A CB   1 
ATOM   5597  C  CG1  . VAL   A  1  373 ? 24.106  -8.077  -18.721  1.00 66.19  ? 373  VAL   A CG1  1 
ATOM   5598  C  CG2  . VAL   A  1  373 ? 21.731  -8.470  -18.039  1.00 61.09  ? 373  VAL   A CG2  1 
ATOM   5599  H  H    . VAL   A  1  373 ? 22.673  -7.044  -15.054  1.00 74.03  ? 373  VAL   A H    1 
ATOM   5600  H  HA   . VAL   A  1  373 ? 23.534  -9.296  -16.308  1.00 74.21  ? 373  VAL   A HA   1 
ATOM   5601  H  HB   . VAL   A  1  373 ? 22.907  -6.856  -17.600  1.00 77.12  ? 373  VAL   A HB   1 
ATOM   5602  H  HG11 . VAL   A  1  373 ? 23.754  -7.816  -19.586  1.00 79.46  ? 373  VAL   A HG11 1 
ATOM   5603  H  HG12 . VAL   A  1  373 ? 24.897  -7.555  -18.514  1.00 79.46  ? 373  VAL   A HG12 1 
ATOM   5604  H  HG13 . VAL   A  1  373 ? 24.324  -9.022  -18.723  1.00 79.46  ? 373  VAL   A HG13 1 
ATOM   5605  H  HG21 . VAL   A  1  373 ? 21.449  -8.129  -18.902  1.00 73.35  ? 373  VAL   A HG21 1 
ATOM   5606  H  HG22 . VAL   A  1  373 ? 21.860  -9.430  -18.088  1.00 73.35  ? 373  VAL   A HG22 1 
ATOM   5607  H  HG23 . VAL   A  1  373 ? 21.065  -8.259  -17.366  1.00 73.35  ? 373  VAL   A HG23 1 
ATOM   5608  N  N    . TYR   A  1  374 ? 25.911  -8.691  -16.134  1.00 62.26  ? 374  TYR   A N    1 
ATOM   5609  C  CA   . TYR   A  1  374 ? 27.302  -8.377  -15.841  1.00 62.57  ? 374  TYR   A CA   1 
ATOM   5610  C  C    . TYR   A  1  374 ? 28.101  -8.339  -17.135  1.00 62.23  ? 374  TYR   A C    1 
ATOM   5611  O  O    . TYR   A  1  374 ? 27.992  -9.251  -17.960  1.00 59.19  ? 374  TYR   A O    1 
ATOM   5612  C  CB   . TYR   A  1  374 ? 27.907  -9.408  -14.887  1.00 63.22  ? 374  TYR   A CB   1 
ATOM   5613  C  CG   . TYR   A  1  374 ? 27.240  -9.456  -13.534  1.00 59.95  ? 374  TYR   A CG   1 
ATOM   5614  C  CD1  . TYR   A  1  374 ? 27.611  -8.578  -12.527  1.00 58.67  ? 374  TYR   A CD1  1 
ATOM   5615  C  CD2  . TYR   A  1  374 ? 26.242  -10.382 -13.262  1.00 58.05  ? 374  TYR   A CD2  1 
ATOM   5616  C  CE1  . TYR   A  1  374 ? 27.006  -8.616  -11.287  1.00 62.62  ? 374  TYR   A CE1  1 
ATOM   5617  C  CE2  . TYR   A  1  374 ? 25.631  -10.429 -12.025  1.00 59.17  ? 374  TYR   A CE2  1 
ATOM   5618  C  CZ   . TYR   A  1  374 ? 26.017  -9.544  -11.041  1.00 62.54  ? 374  TYR   A CZ   1 
ATOM   5619  O  OH   . TYR   A  1  374 ? 25.413  -9.586  -9.805   1.00 64.65  ? 374  TYR   A OH   1 
ATOM   5620  H  H    . TYR   A  1  374 ? 25.797  -9.493  -16.424  1.00 74.75  ? 374  TYR   A H    1 
ATOM   5621  H  HA   . TYR   A  1  374 ? 27.351  -7.502  -15.424  1.00 75.12  ? 374  TYR   A HA   1 
ATOM   5622  H  HB2  . TYR   A  1  374 ? 27.826  -10.288 -15.288  1.00 75.90  ? 374  TYR   A HB2  1 
ATOM   5623  H  HB3  . TYR   A  1  374 ? 28.842  -9.192  -14.748  1.00 75.90  ? 374  TYR   A HB3  1 
ATOM   5624  H  HD1  . TYR   A  1  374 ? 28.279  -7.952  -12.689  1.00 70.45  ? 374  TYR   A HD1  1 
ATOM   5625  H  HD2  . TYR   A  1  374 ? 25.981  -10.980 -13.925  1.00 69.70  ? 374  TYR   A HD2  1 
ATOM   5626  H  HE1  . TYR   A  1  374 ? 27.263  -8.020  -10.622  1.00 75.18  ? 374  TYR   A HE1  1 
ATOM   5627  H  HE2  . TYR   A  1  374 ? 24.963  -11.055 -11.856  1.00 71.04  ? 374  TYR   A HE2  1 
ATOM   5628  H  HH   . TYR   A  1  374 ? 24.830  -10.190 -9.790   1.00 77.62  ? 374  TYR   A HH   1 
ATOM   5629  N  N    . ILE   A  1  375 ? 28.905  -7.293  -17.301  1.00 64.55  ? 375  ILE   A N    1 
ATOM   5630  C  CA   . ILE   A  1  375 ? 29.766  -7.129  -18.467  1.00 61.01  ? 375  ILE   A CA   1 
ATOM   5631  C  C    . ILE   A  1  375 ? 31.181  -7.527  -18.077  1.00 61.57  ? 375  ILE   A C    1 
ATOM   5632  O  O    . ILE   A  1  375 ? 31.740  -6.994  -17.110  1.00 66.55  ? 375  ILE   A O    1 
ATOM   5633  C  CB   . ILE   A  1  375 ? 29.730  -5.682  -18.990  1.00 63.82  ? 375  ILE   A CB   1 
ATOM   5634  C  CG1  . ILE   A  1  375 ? 28.289  -5.246  -19.275  1.00 62.75  ? 375  ILE   A CG1  1 
ATOM   5635  C  CG2  . ILE   A  1  375 ? 30.595  -5.543  -20.240  1.00 67.33  ? 375  ILE   A CG2  1 
ATOM   5636  C  CD1  . ILE   A  1  375 ? 27.582  -6.073  -20.332  1.00 60.81  ? 375  ILE   A CD1  1 
ATOM   5637  H  H    . ILE   A  1  375 ? 28.971  -6.648  -16.736  1.00 77.50  ? 375  ILE   A H    1 
ATOM   5638  H  HA   . ILE   A  1  375 ? 29.461  -7.717  -19.176  1.00 73.25  ? 375  ILE   A HA   1 
ATOM   5639  H  HB   . ILE   A  1  375 ? 30.091  -5.102  -18.302  1.00 76.62  ? 375  ILE   A HB   1 
ATOM   5640  H  HG12 . ILE   A  1  375 ? 27.776  -5.318  -18.455  1.00 75.33  ? 375  ILE   A HG12 1 
ATOM   5641  H  HG13 . ILE   A  1  375 ? 28.299  -4.326  -19.581  1.00 75.33  ? 375  ILE   A HG13 1 
ATOM   5642  H  HG21 . ILE   A  1  375 ? 30.535  -4.632  -20.566  1.00 80.83  ? 375  ILE   A HG21 1 
ATOM   5643  H  HG22 . ILE   A  1  375 ? 31.515  -5.753  -20.012  1.00 80.83  ? 375  ILE   A HG22 1 
ATOM   5644  H  HG23 . ILE   A  1  375 ? 30.274  -6.159  -20.917  1.00 80.83  ? 375  ILE   A HG23 1 
ATOM   5645  H  HD11 . ILE   A  1  375 ? 26.677  -5.741  -20.439  1.00 73.01  ? 375  ILE   A HD11 1 
ATOM   5646  H  HD12 . ILE   A  1  375 ? 28.065  -5.995  -21.169  1.00 73.01  ? 375  ILE   A HD12 1 
ATOM   5647  H  HD13 . ILE   A  1  375 ? 27.563  -7.000  -20.046  1.00 73.01  ? 375  ILE   A HD13 1 
ATOM   5648  N  N    . PHE   A  1  376 ? 31.762  -8.458  -18.828  1.00 58.48  ? 376  PHE   A N    1 
ATOM   5649  C  CA   . PHE   A  1  376 ? 33.129  -8.913  -18.610  1.00 58.74  ? 376  PHE   A CA   1 
ATOM   5650  C  C    . PHE   A  1  376 ? 33.951  -8.584  -19.846  1.00 60.05  ? 376  PHE   A C    1 
ATOM   5651  O  O    . PHE   A  1  376 ? 33.602  -9.003  -20.955  1.00 60.70  ? 376  PHE   A O    1 
ATOM   5652  C  CB   . PHE   A  1  376 ? 33.171  -10.414 -18.318  1.00 58.80  ? 376  PHE   A CB   1 
ATOM   5653  C  CG   . PHE   A  1  376 ? 32.556  -10.790 -17.005  1.00 61.05  ? 376  PHE   A CG   1 
ATOM   5654  C  CD1  . PHE   A  1  376 ? 31.195  -11.030 -16.905  1.00 62.18  ? 376  PHE   A CD1  1 
ATOM   5655  C  CD2  . PHE   A  1  376 ? 33.337  -10.902 -15.868  1.00 61.06  ? 376  PHE   A CD2  1 
ATOM   5656  C  CE1  . PHE   A  1  376 ? 30.626  -11.375 -15.695  1.00 61.37  ? 376  PHE   A CE1  1 
ATOM   5657  C  CE2  . PHE   A  1  376 ? 32.774  -11.246 -14.656  1.00 60.88  ? 376  PHE   A CE2  1 
ATOM   5658  C  CZ   . PHE   A  1  376 ? 31.417  -11.485 -14.569  1.00 61.21  ? 376  PHE   A CZ   1 
ATOM   5659  H  H    . PHE   A  1  376 ? 31.372  -8.851  -19.486  1.00 70.21  ? 376  PHE   A H    1 
ATOM   5660  H  HA   . PHE   A  1  376 ? 33.511  -8.445  -17.850  1.00 70.53  ? 376  PHE   A HA   1 
ATOM   5661  H  HB2  . PHE   A  1  376 ? 32.687  -10.881 -19.017  1.00 70.59  ? 376  PHE   A HB2  1 
ATOM   5662  H  HB3  . PHE   A  1  376 ? 34.097  -10.703 -18.305  1.00 70.59  ? 376  PHE   A HB3  1 
ATOM   5663  H  HD1  . PHE   A  1  376 ? 30.659  -10.957 -17.662  1.00 74.65  ? 376  PHE   A HD1  1 
ATOM   5664  H  HD2  . PHE   A  1  376 ? 34.251  -10.745 -15.922  1.00 73.31  ? 376  PHE   A HD2  1 
ATOM   5665  H  HE1  . PHE   A  1  376 ? 29.712  -11.534 -15.639  1.00 73.69  ? 376  PHE   A HE1  1 
ATOM   5666  H  HE2  . PHE   A  1  376 ? 33.309  -11.316 -13.898  1.00 73.09  ? 376  PHE   A HE2  1 
ATOM   5667  H  HZ   . PHE   A  1  376 ? 31.037  -11.719 -13.754  1.00 73.49  ? 376  PHE   A HZ   1 
ATOM   5668  N  N    . ASN   A  1  377 ? 35.032  -7.835  -19.656  1.00 59.55  ? 377  ASN   A N    1 
ATOM   5669  C  CA   . ASN   A  1  377 ? 35.914  -7.479  -20.756  1.00 64.65  ? 377  ASN   A CA   1 
ATOM   5670  C  C    . ASN   A  1  377 ? 36.998  -8.535  -20.911  1.00 67.17  ? 377  ASN   A C    1 
ATOM   5671  O  O    . ASN   A  1  377 ? 37.471  -9.109  -19.926  1.00 69.73  ? 377  ASN   A O    1 
ATOM   5672  C  CB   . ASN   A  1  377 ? 36.553  -6.110  -20.530  1.00 68.85  ? 377  ASN   A CB   1 
ATOM   5673  C  CG   . ASN   A  1  377 ? 35.530  -5.006  -20.402  1.00 68.74  ? 377  ASN   A CG   1 
ATOM   5674  O  OD1  . ASN   A  1  377 ? 35.102  -4.677  -19.301  1.00 67.48  ? 377  ASN   A OD1  1 
ATOM   5675  N  ND2  . ASN   A  1  377 ? 35.130  -4.429  -21.529  1.00 66.92  ? 377  ASN   A ND2  1 
ATOM   5676  H  H    . ASN   A  1  377 ? 35.276  -7.520  -18.894  1.00 71.50  ? 377  ASN   A H    1 
ATOM   5677  H  HA   . ASN   A  1  377 ? 35.399  -7.434  -21.577  1.00 77.62  ? 377  ASN   A HA   1 
ATOM   5678  H  HB2  . ASN   A  1  377 ? 37.074  -6.134  -19.712  1.00 82.65  ? 377  ASN   A HB2  1 
ATOM   5679  H  HB3  . ASN   A  1  377 ? 37.128  -5.901  -21.283  1.00 82.65  ? 377  ASN   A HB3  1 
ATOM   5680  H  HD21 . ASN   A  1  377 ? 34.549  -3.796  -21.505  1.00 80.34  ? 377  ASN   A HD21 1 
ATOM   5681  H  HD22 . ASN   A  1  377 ? 35.453  -4.688  -22.283  1.00 80.34  ? 377  ASN   A HD22 1 
ATOM   5682  N  N    . GLY   A  1  378 ? 37.384  -8.787  -22.158  1.00 66.82  ? 378  GLY   A N    1 
ATOM   5683  C  CA   . GLY   A  1  378 ? 38.422  -9.751  -22.438  1.00 67.72  ? 378  GLY   A CA   1 
ATOM   5684  C  C    . GLY   A  1  378 ? 39.807  -9.136  -22.408  1.00 72.72  ? 378  GLY   A C    1 
ATOM   5685  O  O    . GLY   A  1  378 ? 39.983  -7.919  -22.413  1.00 71.09  ? 378  GLY   A O    1 
ATOM   5686  H  H    . GLY   A  1  378 ? 37.055  -8.409  -22.857  1.00 80.22  ? 378  GLY   A H    1 
ATOM   5687  H  HA2  . GLY   A  1  378 ? 38.389  -10.460 -21.776  1.00 81.30  ? 378  GLY   A HA2  1 
ATOM   5688  H  HA3  . GLY   A  1  378 ? 38.276  -10.133 -23.317  1.00 81.30  ? 378  GLY   A HA3  1 
ATOM   5689  N  N    . ARG   A  1  379 ? 40.803  -10.013 -22.370  1.00 76.98  ? 379  ARG   A N    1 
ATOM   5690  C  CA   . ARG   A  1  379 ? 42.198  -9.600  -22.419  1.00 82.93  ? 379  ARG   A CA   1 
ATOM   5691  C  C    . ARG   A  1  379 ? 43.024  -10.806 -22.845  1.00 80.65  ? 379  ARG   A C    1 
ATOM   5692  O  O    . ARG   A  1  379 ? 42.528  -11.934 -22.905  1.00 78.29  ? 379  ARG   A O    1 
ATOM   5693  C  CB   . ARG   A  1  379 ? 42.664  -9.028  -21.075  1.00 89.66  ? 379  ARG   A CB   1 
ATOM   5694  C  CG   . ARG   A  1  379 ? 42.297  -9.859  -19.856  1.00 92.49  ? 379  ARG   A CG   1 
ATOM   5695  C  CD   . ARG   A  1  379 ? 42.722  -9.150  -18.577  1.00 98.95  ? 379  ARG   A CD   1 
ATOM   5696  N  NE   . ARG   A  1  379 ? 42.611  -10.005 -17.399  1.00 106.29 ? 379  ARG   A NE   1 
ATOM   5697  C  CZ   . ARG   A  1  379 ? 43.027  -9.663  -16.183  1.00 112.52 ? 379  ARG   A CZ   1 
ATOM   5698  N  NH1  . ARG   A  1  379 ? 43.588  -8.478  -15.976  1.00 116.87 ? 379  ARG   A NH1  1 
ATOM   5699  N  NH2  . ARG   A  1  379 ? 42.886  -10.507 -15.171  1.00 114.23 ? 379  ARG   A NH2  1 
ATOM   5700  H  H    . ARG   A  1  379 ? 40.695  -10.864 -22.316  1.00 92.41  ? 379  ARG   A H    1 
ATOM   5701  H  HA   . ARG   A  1  379 ? 42.315  -8.904  -23.084  1.00 99.55  ? 379  ARG   A HA   1 
ATOM   5702  H  HB2  . ARG   A  1  379 ? 43.631  -8.951  -21.093  1.00 107.63 ? 379  ARG   A HB2  1 
ATOM   5703  H  HB3  . ARG   A  1  379 ? 42.263  -8.152  -20.960  1.00 107.63 ? 379  ARG   A HB3  1 
ATOM   5704  H  HG2  . ARG   A  1  379 ? 41.336  -9.992  -19.831  1.00 111.03 ? 379  ARG   A HG2  1 
ATOM   5705  H  HG3  . ARG   A  1  379 ? 42.749  -10.716 -19.900  1.00 111.03 ? 379  ARG   A HG3  1 
ATOM   5706  H  HD2  . ARG   A  1  379 ? 43.648  -8.873  -18.661  1.00 118.78 ? 379  ARG   A HD2  1 
ATOM   5707  H  HD3  . ARG   A  1  379 ? 42.155  -8.375  -18.440  1.00 118.78 ? 379  ARG   A HD3  1 
ATOM   5708  H  HE   . ARG   A  1  379 ? 42.253  -10.781 -17.497  1.00 127.59 ? 379  ARG   A HE   1 
ATOM   5709  H  HH11 . ARG   A  1  379 ? 43.683  -7.927  -16.629  1.00 140.29 ? 379  ARG   A HH11 1 
ATOM   5710  H  HH12 . ARG   A  1  379 ? 43.855  -8.260  -15.188  1.00 140.29 ? 379  ARG   A HH12 1 
ATOM   5711  H  HH21 . ARG   A  1  379 ? 42.525  -11.277 -15.301  1.00 137.11 ? 379  ARG   A HH21 1 
ATOM   5712  H  HH22 . ARG   A  1  379 ? 43.155  -10.286 -14.385  1.00 137.11 ? 379  ARG   A HH22 1 
ATOM   5713  N  N    . SER   A  1  380 ? 44.298  -10.549 -23.146  1.00 81.34  ? 380  SER   A N    1 
ATOM   5714  C  CA   . SER   A  1  380 ? 45.131  -11.571 -23.771  1.00 79.73  ? 380  SER   A CA   1 
ATOM   5715  C  C    . SER   A  1  380 ? 45.197  -12.847 -22.940  1.00 83.89  ? 380  SER   A C    1 
ATOM   5716  O  O    . SER   A  1  380 ? 45.294  -13.945 -23.501  1.00 86.73  ? 380  SER   A O    1 
ATOM   5717  C  CB   . SER   A  1  380 ? 46.538  -11.022 -24.003  1.00 77.47  ? 380  SER   A CB   1 
ATOM   5718  O  OG   . SER   A  1  380 ? 47.103  -10.549 -22.793  1.00 77.66  ? 380  SER   A OG   1 
ATOM   5719  H  H    . SER   A  1  380 ? 44.697  -9.801  -23.001  1.00 97.64  ? 380  SER   A H    1 
ATOM   5720  H  HA   . SER   A  1  380 ? 44.744  -11.800 -24.630  1.00 95.71  ? 380  SER   A HA   1 
ATOM   5721  H  HB2  . SER   A  1  380 ? 47.099  -11.730 -24.357  1.00 93.00  ? 380  SER   A HB2  1 
ATOM   5722  H  HB3  . SER   A  1  380 ? 46.490  -10.288 -24.636  1.00 93.00  ? 380  SER   A HB3  1 
ATOM   5723  H  HG   . SER   A  1  380 ? 47.862  -10.221 -22.939  1.00 93.23  ? 380  SER   A HG   1 
ATOM   5724  N  N    . THR   A  1  381 ? 45.145  -12.731 -21.612  1.00 85.36  ? 381  THR   A N    1 
ATOM   5725  C  CA   . THR   A  1  381 ? 45.260  -13.920 -20.773  1.00 88.63  ? 381  THR   A CA   1 
ATOM   5726  C  C    . THR   A  1  381 ? 43.986  -14.752 -20.804  1.00 85.59  ? 381  THR   A C    1 
ATOM   5727  O  O    . THR   A  1  381 ? 44.048  -15.985 -20.734  1.00 88.91  ? 381  THR   A O    1 
ATOM   5728  C  CB   . THR   A  1  381 ? 45.588  -13.524 -19.333  1.00 91.30  ? 381  THR   A CB   1 
ATOM   5729  O  OG1  . THR   A  1  381 ? 44.469  -12.839 -18.754  1.00 91.81  ? 381  THR   A OG1  1 
ATOM   5730  C  CG2  . THR   A  1  381 ? 46.809  -12.616 -19.290  1.00 91.87  ? 381  THR   A CG2  1 
ATOM   5731  H  H    . THR   A  1  381 ? 45.046  -11.993 -21.182  1.00 102.46 ? 381  THR   A H    1 
ATOM   5732  H  HA   . THR   A  1  381 ? 45.989  -14.463 -21.109  1.00 106.40 ? 381  THR   A HA   1 
ATOM   5733  H  HB   . THR   A  1  381 ? 45.782  -14.322 -18.816  1.00 109.59 ? 381  THR   A HB   1 
ATOM   5734  H  HG1  . THR   A  1  381 ? 44.662  -12.578 -17.979  1.00 110.21 ? 381  THR   A HG1  1 
ATOM   5735  H  HG21 . THR   A  1  381 ? 47.017  -12.382 -18.371  1.00 110.29 ? 381  THR   A HG21 1 
ATOM   5736  H  HG22 . THR   A  1  381 ? 47.573  -13.070 -19.679  1.00 110.29 ? 381  THR   A HG22 1 
ATOM   5737  H  HG23 . THR   A  1  381 ? 46.637  -11.804 -19.790  1.00 110.29 ? 381  THR   A HG23 1 
ATOM   5738  N  N    . GLY   A  1  382 ? 42.832  -14.102 -20.909  1.00 80.69  ? 382  GLY   A N    1 
ATOM   5739  C  CA   . GLY   A  1  382 ? 41.560  -14.793 -20.944  1.00 74.96  ? 382  GLY   A CA   1 
ATOM   5740  C  C    . GLY   A  1  382 ? 40.416  -13.816 -20.796  1.00 70.83  ? 382  GLY   A C    1 
ATOM   5741  O  O    . GLY   A  1  382 ? 40.300  -12.865 -21.575  1.00 74.29  ? 382  GLY   A O    1 
ATOM   5742  H  H    . GLY   A  1  382 ? 42.762  -13.247 -20.962  1.00 96.87  ? 382  GLY   A H    1 
ATOM   5743  H  HA2  . GLY   A  1  382 ? 41.465  -15.261 -21.788  1.00 89.99  ? 382  GLY   A HA2  1 
ATOM   5744  H  HA3  . GLY   A  1  382 ? 41.517  -15.437 -20.220  1.00 89.99  ? 382  GLY   A HA3  1 
ATOM   5745  N  N    . LEU   A  1  383 ? 39.565  -14.038 -19.802  1.00 67.58  ? 383  LEU   A N    1 
ATOM   5746  C  CA   . LEU   A  1  383 ? 38.504  -13.106 -19.451  1.00 71.02  ? 383  LEU   A CA   1 
ATOM   5747  C  C    . LEU   A  1  383 ? 38.871  -12.420 -18.144  1.00 78.06  ? 383  LEU   A C    1 
ATOM   5748  O  O    . LEU   A  1  383 ? 39.290  -13.082 -17.188  1.00 79.46  ? 383  LEU   A O    1 
ATOM   5749  C  CB   . LEU   A  1  383 ? 37.161  -13.823 -19.311  1.00 69.14  ? 383  LEU   A CB   1 
ATOM   5750  C  CG   . LEU   A  1  383 ? 35.956  -12.911 -19.070  1.00 68.75  ? 383  LEU   A CG   1 
ATOM   5751  C  CD1  . LEU   A  1  383 ? 35.677  -12.055 -20.297  1.00 68.91  ? 383  LEU   A CD1  1 
ATOM   5752  C  CD2  . LEU   A  1  383 ? 34.736  -13.733 -18.694  1.00 69.43  ? 383  LEU   A CD2  1 
ATOM   5753  H  H    . LEU   A  1  383 ? 39.584  -14.739 -19.304  1.00 81.13  ? 383  LEU   A H    1 
ATOM   5754  H  HA   . LEU   A  1  383 ? 38.414  -12.435 -20.145  1.00 85.26  ? 383  LEU   A HA   1 
ATOM   5755  H  HB2  . LEU   A  1  383 ? 36.992  -14.317 -20.128  1.00 83.00  ? 383  LEU   A HB2  1 
ATOM   5756  H  HB3  . LEU   A  1  383 ? 37.217  -14.433 -18.559  1.00 83.00  ? 383  LEU   A HB3  1 
ATOM   5757  H  HG   . LEU   A  1  383 ? 36.153  -12.314 -18.331  1.00 82.53  ? 383  LEU   A HG   1 
ATOM   5758  H  HD11 . LEU   A  1  383 ? 34.882  -11.522 -20.137  1.00 82.73  ? 383  LEU   A HD11 1 
ATOM   5759  H  HD12 . LEU   A  1  383 ? 36.438  -11.475 -20.457  1.00 82.73  ? 383  LEU   A HD12 1 
ATOM   5760  H  HD13 . LEU   A  1  383 ? 35.538  -12.635 -21.062  1.00 82.73  ? 383  LEU   A HD13 1 
ATOM   5761  H  HD21 . LEU   A  1  383 ? 33.981  -13.138 -18.569  1.00 83.35  ? 383  LEU   A HD21 1 
ATOM   5762  H  HD22 . LEU   A  1  383 ? 34.547  -14.362 -19.408  1.00 83.35  ? 383  LEU   A HD22 1 
ATOM   5763  H  HD23 . LEU   A  1  383 ? 34.920  -14.213 -17.871  1.00 83.35  ? 383  LEU   A HD23 1 
ATOM   5764  N  N    . ASN   A  1  384 ? 38.730  -11.099 -18.108  1.00 82.78  ? 384  ASN   A N    1 
ATOM   5765  C  CA   . ASN   A  1  384 ? 38.900  -10.377 -16.855  1.00 87.77  ? 384  ASN   A CA   1 
ATOM   5766  C  C    . ASN   A  1  384 ? 37.838  -10.843 -15.867  1.00 90.50  ? 384  ASN   A C    1 
ATOM   5767  O  O    . ASN   A  1  384 ? 36.637  -10.711 -16.124  1.00 95.69  ? 384  ASN   A O    1 
ATOM   5768  C  CB   . ASN   A  1  384 ? 38.806  -8.872  -17.091  1.00 86.41  ? 384  ASN   A CB   1 
ATOM   5769  C  CG   . ASN   A  1  384 ? 39.120  -8.068  -15.844  1.00 87.24  ? 384  ASN   A CG   1 
ATOM   5770  O  OD1  . ASN   A  1  384 ? 39.401  -8.629  -14.786  1.00 87.88  ? 384  ASN   A OD1  1 
ATOM   5771  N  ND2  . ASN   A  1  384 ? 39.087  -6.747  -15.968  1.00 86.91  ? 384  ASN   A ND2  1 
ATOM   5772  H  H    . ASN   A  1  384 ? 38.539  -10.605 -18.785  1.00 99.38  ? 384  ASN   A H    1 
ATOM   5773  H  HA   . ASN   A  1  384 ? 39.779  -10.555 -16.485  1.00 105.36 ? 384  ASN   A HA   1 
ATOM   5774  H  HB2  . ASN   A  1  384 ? 39.440  -8.619  -17.780  1.00 103.73 ? 384  ASN   A HB2  1 
ATOM   5775  H  HB3  . ASN   A  1  384 ? 37.905  -8.651  -17.372  1.00 103.73 ? 384  ASN   A HB3  1 
ATOM   5776  H  HD21 . ASN   A  1  384 ? 39.258  -6.247  -15.289  1.00 104.33 ? 384  ASN   A HD21 1 
ATOM   5777  H  HD22 . ASN   A  1  384 ? 38.895  -6.390  -16.726  1.00 104.33 ? 384  ASN   A HD22 1 
ATOM   5778  N  N    . ALA   A  1  385 ? 38.283  -11.398 -14.739  1.00 89.46  ? 385  ALA   A N    1 
ATOM   5779  C  CA   . ALA   A  1  385 ? 37.370  -12.059 -13.816  1.00 86.15  ? 385  ALA   A CA   1 
ATOM   5780  C  C    . ALA   A  1  385 ? 36.483  -11.091 -13.046  1.00 83.21  ? 385  ALA   A C    1 
ATOM   5781  O  O    . ALA   A  1  385 ? 35.583  -11.546 -12.333  1.00 82.47  ? 385  ALA   A O    1 
ATOM   5782  C  CB   . ALA   A  1  385 ? 38.162  -12.917 -12.827  1.00 90.76  ? 385  ALA   A CB   1 
ATOM   5783  H  H    . ALA   A  1  385 ? 39.106  -11.404 -14.489  1.00 107.38 ? 385  ALA   A H    1 
ATOM   5784  H  HA   . ALA   A  1  385 ? 36.789  -12.641 -14.331  1.00 103.42 ? 385  ALA   A HA   1 
ATOM   5785  H  HB1  . ALA   A  1  385 ? 37.542  -13.358 -12.225  1.00 108.95 ? 385  ALA   A HB1  1 
ATOM   5786  H  HB2  . ALA   A  1  385 ? 38.670  -13.580 -13.321  1.00 108.95 ? 385  ALA   A HB2  1 
ATOM   5787  H  HB3  . ALA   A  1  385 ? 38.763  -12.346 -12.324  1.00 108.95 ? 385  ALA   A HB3  1 
ATOM   5788  N  N    . VAL   A  1  386 ? 36.702  -9.791  -13.165  1.00 82.75  ? 386  VAL   A N    1 
ATOM   5789  C  CA   . VAL   A  1  386 ? 35.914  -8.779  -12.464  1.00 82.63  ? 386  VAL   A CA   1 
ATOM   5790  C  C    . VAL   A  1  386 ? 35.025  -8.081  -13.483  1.00 78.32  ? 386  VAL   A C    1 
ATOM   5791  O  O    . VAL   A  1  386 ? 35.534  -7.597  -14.500  1.00 77.94  ? 386  VAL   A O    1 
ATOM   5792  C  CB   . VAL   A  1  386 ? 36.809  -7.756  -11.738  1.00 88.55  ? 386  VAL   A CB   1 
ATOM   5793  C  CG1  . VAL   A  1  386 ? 35.957  -6.807  -10.905  1.00 89.94  ? 386  VAL   A CG1  1 
ATOM   5794  C  CG2  . VAL   A  1  386 ? 37.834  -8.466  -10.869  1.00 92.83  ? 386  VAL   A CG2  1 
ATOM   5795  H  H    . VAL   A  1  386 ? 37.321  -9.457  -13.661  1.00 99.34  ? 386  VAL   A H    1 
ATOM   5796  H  HA   . VAL   A  1  386 ? 35.348  -9.212  -11.806  1.00 99.19  ? 386  VAL   A HA   1 
ATOM   5797  H  HB   . VAL   A  1  386 ? 37.289  -7.231  -12.398  1.00 106.29 ? 386  VAL   A HB   1 
ATOM   5798  H  HG11 . VAL   A  1  386 ? 36.539  -6.189  -10.437  1.00 107.96 ? 386  VAL   A HG11 1 
ATOM   5799  H  HG12 . VAL   A  1  386 ? 35.361  -6.319  -11.494  1.00 107.96 ? 386  VAL   A HG12 1 
ATOM   5800  H  HG13 . VAL   A  1  386 ? 35.441  -7.324  -10.267  1.00 107.96 ? 386  VAL   A HG13 1 
ATOM   5801  H  HG21 . VAL   A  1  386 ? 38.362  -7.803  -10.398  1.00 111.44 ? 386  VAL   A HG21 1 
ATOM   5802  H  HG22 . VAL   A  1  386 ? 37.370  -9.032  -10.232  1.00 111.44 ? 386  VAL   A HG22 1 
ATOM   5803  H  HG23 . VAL   A  1  386 ? 38.408  -9.006  -11.435  1.00 111.44 ? 386  VAL   A HG23 1 
ATOM   5804  N  N    . PRO   A  1  387 ? 33.713  -7.998  -13.258  1.00 75.49  ? 387  PRO   A N    1 
ATOM   5805  C  CA   . PRO   A  1  387 ? 32.851  -7.299  -14.221  1.00 72.89  ? 387  PRO   A CA   1 
ATOM   5806  C  C    . PRO   A  1  387 ? 33.145  -5.807  -14.228  1.00 73.84  ? 387  PRO   A C    1 
ATOM   5807  O  O    . PRO   A  1  387 ? 33.268  -5.177  -13.175  1.00 74.57  ? 387  PRO   A O    1 
ATOM   5808  C  CB   . PRO   A  1  387 ? 31.435  -7.597  -13.714  1.00 72.62  ? 387  PRO   A CB   1 
ATOM   5809  C  CG   . PRO   A  1  387 ? 31.607  -7.848  -12.257  1.00 76.49  ? 387  PRO   A CG   1 
ATOM   5810  C  CD   . PRO   A  1  387 ? 32.945  -8.516  -12.111  1.00 76.09  ? 387  PRO   A CD   1 
ATOM   5811  H  HA   . PRO   A  1  387 ? 32.963  -7.661  -15.114  1.00 87.51  ? 387  PRO   A HA   1 
ATOM   5812  H  HB2  . PRO   A  1  387 ? 30.859  -6.833  -13.871  1.00 87.19  ? 387  PRO   A HB2  1 
ATOM   5813  H  HB3  . PRO   A  1  387 ? 31.079  -8.380  -14.163  1.00 87.19  ? 387  PRO   A HB3  1 
ATOM   5814  H  HG2  . PRO   A  1  387 ? 31.588  -7.006  -11.775  1.00 91.82  ? 387  PRO   A HG2  1 
ATOM   5815  H  HG3  . PRO   A  1  387 ? 30.897  -8.428  -11.939  1.00 91.82  ? 387  PRO   A HG3  1 
ATOM   5816  H  HD2  . PRO   A  1  387 ? 33.366  -8.266  -11.273  1.00 91.35  ? 387  PRO   A HD2  1 
ATOM   5817  H  HD3  . PRO   A  1  387 ? 32.856  -9.481  -12.162  1.00 91.35  ? 387  PRO   A HD3  1 
ATOM   5818  N  N    . SER   A  1  388 ? 33.262  -5.245  -15.429  1.00 72.35  ? 388  SER   A N    1 
ATOM   5819  C  CA   . SER   A  1  388 ? 33.496  -3.817  -15.588  1.00 73.54  ? 388  SER   A CA   1 
ATOM   5820  C  C    . SER   A  1  388 ? 32.213  -3.002  -15.547  1.00 69.72  ? 388  SER   A C    1 
ATOM   5821  O  O    . SER   A  1  388 ? 32.281  -1.769  -15.591  1.00 67.88  ? 388  SER   A O    1 
ATOM   5822  C  CB   . SER   A  1  388 ? 34.218  -3.550  -16.909  1.00 77.99  ? 388  SER   A CB   1 
ATOM   5823  O  OG   . SER   A  1  388 ? 33.384  -3.887  -18.003  1.00 78.01  ? 388  SER   A OG   1 
ATOM   5824  H  H    . SER   A  1  388 ? 33.208  -5.676  -16.172  1.00 86.85  ? 388  SER   A H    1 
ATOM   5825  H  HA   . SER   A  1  388 ? 34.068  -3.517  -14.865  1.00 88.29  ? 388  SER   A HA   1 
ATOM   5826  H  HB2  . SER   A  1  388 ? 34.446  -2.609  -16.961  1.00 93.62  ? 388  SER   A HB2  1 
ATOM   5827  H  HB3  . SER   A  1  388 ? 35.023  -4.089  -16.946  1.00 93.62  ? 388  SER   A HB3  1 
ATOM   5828  H  HG   . SER   A  1  388 ? 33.852  -4.111  -18.663  1.00 93.65  ? 388  SER   A HG   1 
ATOM   5829  N  N    . GLN   A  1  389 ? 31.054  -3.649  -15.472  1.00 68.41  ? 389  GLN   A N    1 
ATOM   5830  C  CA   . GLN   A  1  389 ? 29.791  -2.927  -15.463  1.00 67.19  ? 389  GLN   A CA   1 
ATOM   5831  C  C    . GLN   A  1  389 ? 28.691  -3.868  -15.002  1.00 68.27  ? 389  GLN   A C    1 
ATOM   5832  O  O    . GLN   A  1  389 ? 28.795  -5.089  -15.143  1.00 67.08  ? 389  GLN   A O    1 
ATOM   5833  C  CB   . GLN   A  1  389 ? 29.464  -2.357  -16.845  1.00 64.13  ? 389  GLN   A CB   1 
ATOM   5834  C  CG   . GLN   A  1  389 ? 28.372  -1.306  -16.829  1.00 65.65  ? 389  GLN   A CG   1 
ATOM   5835  C  CD   . GLN   A  1  389 ? 28.263  -0.560  -18.143  1.00 67.19  ? 389  GLN   A CD   1 
ATOM   5836  O  OE1  . GLN   A  1  389 ? 28.871  -0.946  -19.142  1.00 70.38  ? 389  GLN   A OE1  1 
ATOM   5837  N  NE2  . GLN   A  1  389 ? 27.492  0.519   -18.147  1.00 67.25  ? 389  GLN   A NE2  1 
ATOM   5838  H  H    . GLN   A  1  389 ? 30.975  -4.504  -15.424  1.00 82.13  ? 389  GLN   A H    1 
ATOM   5839  H  HA   . GLN   A  1  389 ? 29.845  -2.194  -14.830  1.00 80.66  ? 389  GLN   A HA   1 
ATOM   5840  H  HB2  . GLN   A  1  389 ? 30.263  -1.949  -17.211  1.00 76.99  ? 389  GLN   A HB2  1 
ATOM   5841  H  HB3  . GLN   A  1  389 ? 29.169  -3.081  -17.419  1.00 76.99  ? 389  GLN   A HB3  1 
ATOM   5842  H  HG2  . GLN   A  1  389 ? 27.520  -1.736  -16.656  1.00 78.82  ? 389  GLN   A HG2  1 
ATOM   5843  H  HG3  . GLN   A  1  389 ? 28.565  -0.659  -16.132  1.00 78.82  ? 389  GLN   A HG3  1 
ATOM   5844  H  HE21 . GLN   A  1  389 ? 27.086  0.761   -17.428  1.00 80.74  ? 389  GLN   A HE21 1 
ATOM   5845  H  HE22 . GLN   A  1  389 ? 27.397  0.978   -18.868  1.00 80.74  ? 389  GLN   A HE22 1 
ATOM   5846  N  N    . ILE   A  1  390 ? 27.631  -3.275  -14.453  1.00 71.23  ? 390  ILE   A N    1 
ATOM   5847  C  CA   . ILE   A  1  390 ? 26.488  -4.013  -13.928  1.00 66.49  ? 390  ILE   A CA   1 
ATOM   5848  C  C    . ILE   A  1  390 ? 25.226  -3.303  -14.392  1.00 63.07  ? 390  ILE   A C    1 
ATOM   5849  O  O    . ILE   A  1  390 ? 24.996  -2.143  -14.031  1.00 63.72  ? 390  ILE   A O    1 
ATOM   5850  C  CB   . ILE   A  1  390 ? 26.510  -4.108  -12.393  1.00 67.78  ? 390  ILE   A CB   1 
ATOM   5851  C  CG1  . ILE   A  1  390 ? 27.703  -4.948  -11.934  1.00 66.54  ? 390  ILE   A CG1  1 
ATOM   5852  C  CG2  . ILE   A  1  390 ? 25.203  -4.698  -11.871  1.00 68.06  ? 390  ILE   A CG2  1 
ATOM   5853  C  CD1  . ILE   A  1  390 ? 27.990  -4.840  -10.455  1.00 68.83  ? 390  ILE   A CD1  1 
ATOM   5854  H  H    . ILE   A  1  390 ? 27.551  -2.423  -14.371  1.00 85.51  ? 390  ILE   A H    1 
ATOM   5855  H  HA   . ILE   A  1  390 ? 26.489  -4.913  -14.290  1.00 79.82  ? 390  ILE   A HA   1 
ATOM   5856  H  HB   . ILE   A  1  390 ? 26.605  -3.213  -12.031  1.00 81.38  ? 390  ILE   A HB   1 
ATOM   5857  H  HG12 . ILE   A  1  390 ? 27.522  -5.880  -12.133  1.00 79.89  ? 390  ILE   A HG12 1 
ATOM   5858  H  HG13 . ILE   A  1  390 ? 28.494  -4.654  -12.412  1.00 79.89  ? 390  ILE   A HG13 1 
ATOM   5859  H  HG21 . ILE   A  1  390 ? 25.258  -4.786  -10.907  1.00 81.71  ? 390  ILE   A HG21 1 
ATOM   5860  H  HG22 . ILE   A  1  390 ? 24.472  -4.106  -12.109  1.00 81.71  ? 390  ILE   A HG22 1 
ATOM   5861  H  HG23 . ILE   A  1  390 ? 25.067  -5.570  -12.275  1.00 81.71  ? 390  ILE   A HG23 1 
ATOM   5862  H  HD11 . ILE   A  1  390 ? 28.762  -5.386  -10.242  1.00 82.63  ? 390  ILE   A HD11 1 
ATOM   5863  H  HD12 . ILE   A  1  390 ? 28.171  -3.912  -10.236  1.00 82.63  ? 390  ILE   A HD12 1 
ATOM   5864  H  HD13 . ILE   A  1  390 ? 27.217  -5.152  -9.959   1.00 82.63  ? 390  ILE   A HD13 1 
ATOM   5865  N  N    . LEU   A  1  391 ? 24.413  -3.990  -15.184  1.00 60.88  ? 391  LEU   A N    1 
ATOM   5866  C  CA   . LEU   A  1  391 ? 23.139  -3.463  -15.647  1.00 61.75  ? 391  LEU   A CA   1 
ATOM   5867  C  C    . LEU   A  1  391 ? 22.036  -4.021  -14.759  1.00 64.87  ? 391  LEU   A C    1 
ATOM   5868  O  O    . LEU   A  1  391 ? 22.002  -5.226  -14.487  1.00 64.35  ? 391  LEU   A O    1 
ATOM   5869  C  CB   . LEU   A  1  391 ? 22.896  -3.827  -17.112  1.00 61.93  ? 391  LEU   A CB   1 
ATOM   5870  C  CG   . LEU   A  1  391 ? 23.797  -3.136  -18.143  1.00 68.16  ? 391  LEU   A CG   1 
ATOM   5871  C  CD1  . LEU   A  1  391 ? 25.274  -3.456  -17.936  1.00 72.80  ? 391  LEU   A CD1  1 
ATOM   5872  C  CD2  . LEU   A  1  391 ? 23.373  -3.524  -19.547  1.00 70.12  ? 391  LEU   A CD2  1 
ATOM   5873  H  H    . LEU   A  1  391 ? 24.582  -4.782  -15.472  1.00 73.09  ? 391  LEU   A H    1 
ATOM   5874  H  HA   . LEU   A  1  391 ? 23.130  -2.495  -15.584  1.00 74.14  ? 391  LEU   A HA   1 
ATOM   5875  H  HB2  . LEU   A  1  391 ? 23.030  -4.783  -17.211  1.00 74.35  ? 391  LEU   A HB2  1 
ATOM   5876  H  HB3  . LEU   A  1  391 ? 21.980  -3.596  -17.332  1.00 74.35  ? 391  LEU   A HB3  1 
ATOM   5877  H  HG   . LEU   A  1  391 ? 23.698  -2.178  -18.027  1.00 81.83  ? 391  LEU   A HG   1 
ATOM   5878  H  HD11 . LEU   A  1  391 ? 25.787  -3.065  -18.661  1.00 87.40  ? 391  LEU   A HD11 1 
ATOM   5879  H  HD12 . LEU   A  1  391 ? 25.563  -3.082  -17.089  1.00 87.40  ? 391  LEU   A HD12 1 
ATOM   5880  H  HD13 . LEU   A  1  391 ? 25.391  -4.418  -17.930  1.00 87.40  ? 391  LEU   A HD13 1 
ATOM   5881  H  HD21 . LEU   A  1  391 ? 23.963  -3.093  -20.186  1.00 84.18  ? 391  LEU   A HD21 1 
ATOM   5882  H  HD22 . LEU   A  1  391 ? 23.432  -4.488  -19.640  1.00 84.18  ? 391  LEU   A HD22 1 
ATOM   5883  H  HD23 . LEU   A  1  391 ? 22.459  -3.234  -19.693  1.00 84.18  ? 391  LEU   A HD23 1 
ATOM   5884  N  N    . GLU   A  1  392 ? 21.149  -3.144  -14.297  1.00 64.49  ? 392  GLU   A N    1 
ATOM   5885  C  CA   . GLU   A  1  392 ? 20.102  -3.504  -13.352  1.00 63.53  ? 392  GLU   A CA   1 
ATOM   5886  C  C    . GLU   A  1  392 ? 18.739  -3.297  -13.995  1.00 62.53  ? 392  GLU   A C    1 
ATOM   5887  O  O    . GLU   A  1  392 ? 18.445  -2.207  -14.498  1.00 63.83  ? 392  GLU   A O    1 
ATOM   5888  C  CB   . GLU   A  1  392 ? 20.211  -2.670  -12.072  1.00 70.65  ? 392  GLU   A CB   1 
ATOM   5889  C  CG   . GLU   A  1  392 ? 21.442  -2.971  -11.231  1.00 76.13  ? 392  GLU   A CG   1 
ATOM   5890  C  CD   . GLU   A  1  392 ? 21.670  -1.940  -10.143  1.00 83.18  ? 392  GLU   A CD   1 
ATOM   5891  O  OE1  . GLU   A  1  392 ? 21.509  -0.733  -10.422  1.00 86.23  ? 392  GLU   A OE1  1 
ATOM   5892  O  OE2  . GLU   A  1  392 ? 22.006  -2.336  -9.007   1.00 84.93  ? 392  GLU   A OE2  1 
ATOM   5893  H  H    . GLU   A  1  392 ? 21.135  -2.315  -14.524  1.00 77.43  ? 392  GLU   A H    1 
ATOM   5894  H  HA   . GLU   A  1  392 ? 20.187  -4.442  -13.120  1.00 76.27  ? 392  GLU   A HA   1 
ATOM   5895  H  HB2  . GLU   A  1  392 ? 20.244  -1.732  -12.315  1.00 84.81  ? 392  GLU   A HB2  1 
ATOM   5896  H  HB3  . GLU   A  1  392 ? 19.430  -2.843  -11.522  1.00 84.81  ? 392  GLU   A HB3  1 
ATOM   5897  H  HG2  . GLU   A  1  392 ? 21.332  -3.837  -10.807  1.00 91.39  ? 392  GLU   A HG2  1 
ATOM   5898  H  HG3  . GLU   A  1  392 ? 22.223  -2.980  -11.806  1.00 91.39  ? 392  GLU   A HG3  1 
ATOM   5899  N  N    . GLY   A  1  393 ? 17.915  -4.342  -13.980  1.00 61.47  ? 393  GLY   A N    1 
ATOM   5900  C  CA   . GLY   A  1  393 ? 16.544  -4.189  -14.423  1.00 63.52  ? 393  GLY   A CA   1 
ATOM   5901  C  C    . GLY   A  1  393 ? 15.798  -3.181  -13.570  1.00 70.71  ? 393  GLY   A C    1 
ATOM   5902  O  O    . GLY   A  1  393 ? 16.040  -3.049  -12.369  1.00 70.83  ? 393  GLY   A O    1 
ATOM   5903  H  H    . GLY   A  1  393 ? 18.125  -5.135  -13.721  1.00 73.81  ? 393  GLY   A H    1 
ATOM   5904  H  HA2  . GLY   A  1  393 ? 16.532  -3.885  -15.344  1.00 76.26  ? 393  GLY   A HA2  1 
ATOM   5905  H  HA3  . GLY   A  1  393 ? 16.086  -5.042  -14.366  1.00 76.26  ? 393  GLY   A HA3  1 
ATOM   5906  N  N    . GLN   A  1  394 ? 14.877  -2.457  -14.207  1.00 77.59  ? 394  GLN   A N    1 
ATOM   5907  C  CA   . GLN   A  1  394 ? 14.179  -1.362  -13.553  1.00 86.07  ? 394  GLN   A CA   1 
ATOM   5908  C  C    . GLN   A  1  394 ? 12.698  -1.623  -13.320  1.00 85.62  ? 394  GLN   A C    1 
ATOM   5909  O  O    . GLN   A  1  394 ? 12.044  -0.803  -12.666  1.00 89.22  ? 394  GLN   A O    1 
ATOM   5910  C  CB   . GLN   A  1  394 ? 14.332  -0.075  -14.380  1.00 95.77  ? 394  GLN   A CB   1 
ATOM   5911  C  CG   . GLN   A  1  394 ? 15.774  0.373   -14.562  1.00 103.18 ? 394  GLN   A CG   1 
ATOM   5912  C  CD   . GLN   A  1  394 ? 16.433  0.761   -13.254  1.00 112.65 ? 394  GLN   A CD   1 
ATOM   5913  O  OE1  . GLN   A  1  394 ? 15.758  1.027   -12.259  1.00 120.98 ? 394  GLN   A OE1  1 
ATOM   5914  N  NE2  . GLN   A  1  394 ? 17.761  0.793   -13.246  1.00 115.14 ? 394  GLN   A NE2  1 
ATOM   5915  H  H    . GLN   A  1  394 ? 14.641  -2.586  -15.023  1.00 93.14  ? 394  GLN   A H    1 
ATOM   5916  H  HA   . GLN   A  1  394 ? 14.586  -1.218  -12.684  1.00 103.32 ? 394  GLN   A HA   1 
ATOM   5917  H  HB2  . GLN   A  1  394 ? 13.956  -0.224  -15.261  1.00 114.97 ? 394  GLN   A HB2  1 
ATOM   5918  H  HB3  . GLN   A  1  394 ? 13.855  0.641   -13.932  1.00 114.97 ? 394  GLN   A HB3  1 
ATOM   5919  H  HG2  . GLN   A  1  394 ? 16.284  -0.354  -14.952  1.00 123.85 ? 394  GLN   A HG2  1 
ATOM   5920  H  HG3  . GLN   A  1  394 ? 15.794  1.145   -15.149  1.00 123.85 ? 394  GLN   A HG3  1 
ATOM   5921  H  HE21 . GLN   A  1  394 ? 18.200  0.599   -13.960  1.00 138.21 ? 394  GLN   A HE21 1 
ATOM   5922  H  HE22 . GLN   A  1  394 ? 18.182  1.007   -12.528  1.00 138.21 ? 394  GLN   A HE22 1 
ATOM   5923  N  N    . TRP   A  1  395 ? 12.151  -2.728  -13.819  1.00 81.29  ? 395  TRP   A N    1 
ATOM   5924  C  CA   . TRP   A  1  395 ? 10.720  -2.980  -13.749  1.00 81.55  ? 395  TRP   A CA   1 
ATOM   5925  C  C    . TRP   A  1  395 ? 10.405  -4.164  -12.849  1.00 80.03  ? 395  TRP   A C    1 
ATOM   5926  O  O    . TRP   A  1  395 ? 11.169  -5.128  -12.755  1.00 78.15  ? 395  TRP   A O    1 
ATOM   5927  C  CB   . TRP   A  1  395 ? 10.146  -3.222  -15.145  1.00 81.94  ? 395  TRP   A CB   1 
ATOM   5928  C  CG   . TRP   A  1  395 ? 10.432  -2.078  -16.028  1.00 87.61  ? 395  TRP   A CG   1 
ATOM   5929  C  CD1  . TRP   A  1  395 ? 9.649   -0.983  -16.232  1.00 91.58  ? 395  TRP   A CD1  1 
ATOM   5930  C  CD2  . TRP   A  1  395 ? 11.612  -1.883  -16.809  1.00 87.56  ? 395  TRP   A CD2  1 
ATOM   5931  N  NE1  . TRP   A  1  395 ? 10.264  -0.119  -17.104  1.00 97.23  ? 395  TRP   A NE1  1 
ATOM   5932  C  CE2  . TRP   A  1  395 ? 11.472  -0.651  -17.473  1.00 91.73  ? 395  TRP   A CE2  1 
ATOM   5933  C  CE3  . TRP   A  1  395 ? 12.772  -2.635  -17.015  1.00 83.30  ? 395  TRP   A CE3  1 
ATOM   5934  C  CZ2  . TRP   A  1  395 ? 12.448  -0.154  -18.331  1.00 89.15  ? 395  TRP   A CZ2  1 
ATOM   5935  C  CZ3  . TRP   A  1  395 ? 13.737  -2.142  -17.868  1.00 85.11  ? 395  TRP   A CZ3  1 
ATOM   5936  C  CH2  . TRP   A  1  395 ? 13.570  -0.913  -18.516  1.00 88.91  ? 395  TRP   A CH2  1 
ATOM   5937  H  H    . TRP   A  1  395 ? 12.597  -3.353  -14.207  1.00 97.59  ? 395  TRP   A H    1 
ATOM   5938  H  HA   . TRP   A  1  395 ? 10.286  -2.205  -13.360  1.00 97.90  ? 395  TRP   A HA   1 
ATOM   5939  H  HB2  . TRP   A  1  395 ? 10.549  -4.017  -15.528  1.00 98.36  ? 395  TRP   A HB2  1 
ATOM   5940  H  HB3  . TRP   A  1  395 ? 9.184   -3.333  -15.085  1.00 98.36  ? 395  TRP   A HB3  1 
ATOM   5941  H  HD1  . TRP   A  1  395 ? 8.819   -0.841  -15.837  1.00 109.93 ? 395  TRP   A HD1  1 
ATOM   5942  H  HE1  . TRP   A  1  395 ? 9.944   0.632   -17.374  1.00 116.71 ? 395  TRP   A HE1  1 
ATOM   5943  H  HE3  . TRP   A  1  395 ? 12.890  -3.452  -16.586  1.00 100.00 ? 395  TRP   A HE3  1 
ATOM   5944  H  HZ2  . TRP   A  1  395 ? 12.341  0.663   -18.762  1.00 107.02 ? 395  TRP   A HZ2  1 
ATOM   5945  H  HZ3  . TRP   A  1  395 ? 14.513  -2.634  -18.015  1.00 102.17 ? 395  TRP   A HZ3  1 
ATOM   5946  H  HH2  . TRP   A  1  395 ? 14.238  -0.605  -19.085  1.00 106.73 ? 395  TRP   A HH2  1 
ATOM   5947  N  N    . ALA   A  1  396 ? 9.257   -4.066  -12.187  1.00 82.16  ? 396  ALA   A N    1 
ATOM   5948  C  CA   . ALA   A  1  396 ? 8.727   -5.098  -11.315  1.00 81.72  ? 396  ALA   A CA   1 
ATOM   5949  C  C    . ALA   A  1  396 ? 7.405   -5.596  -11.885  1.00 85.23  ? 396  ALA   A C    1 
ATOM   5950  O  O    . ALA   A  1  396 ? 6.720   -4.885  -12.626  1.00 88.21  ? 396  ALA   A O    1 
ATOM   5951  C  CB   . ALA   A  1  396 ? 8.536   -4.563  -9.891   1.00 83.82  ? 396  ALA   A CB   1 
ATOM   5952  H  H    . ALA   A  1  396 ? 8.746   -3.376  -12.231  1.00 98.62  ? 396  ALA   A H    1 
ATOM   5953  H  HA   . ALA   A  1  396 ? 9.337   -5.850  -11.267  1.00 98.10  ? 396  ALA   A HA   1 
ATOM   5954  H  HB1  . ALA   A  1  396 ? 7.796   -5.032  -9.474   1.00 100.63 ? 396  ALA   A HB1  1 
ATOM   5955  H  HB2  . ALA   A  1  396 ? 9.350   -4.714  -9.385   1.00 100.63 ? 396  ALA   A HB2  1 
ATOM   5956  H  HB3  . ALA   A  1  396 ? 8.344   -3.614  -9.933   1.00 100.63 ? 396  ALA   A HB3  1 
ATOM   5957  N  N    . ALA   A  1  397 ? 7.050   -6.831  -11.537  1.00 89.02  ? 397  ALA   A N    1 
ATOM   5958  C  CA   . ALA   A  1  397 ? 5.856   -7.476  -12.067  1.00 95.55  ? 397  ALA   A CA   1 
ATOM   5959  C  C    . ALA   A  1  397 ? 5.057   -8.092  -10.925  1.00 102.43 ? 397  ALA   A C    1 
ATOM   5960  O  O    . ALA   A  1  397 ? 5.477   -8.079  -9.764   1.00 101.10 ? 397  ALA   A O    1 
ATOM   5961  C  CB   . ALA   A  1  397 ? 6.219   -8.541  -13.111  1.00 92.63  ? 397  ALA   A CB   1 
ATOM   5962  H  H    . ALA   A  1  397 ? 7.494   -7.321  -10.987  1.00 106.87 ? 397  ALA   A H    1 
ATOM   5963  H  HA   . ALA   A  1  397 ? 5.303   -6.803  -12.493  1.00 114.70 ? 397  ALA   A HA   1 
ATOM   5964  H  HB1  . ALA   A  1  397 ? 5.668   -8.412  -13.898  1.00 111.19 ? 397  ALA   A HB1  1 
ATOM   5965  H  HB2  . ALA   A  1  397 ? 7.156   -8.448  -13.344  1.00 111.19 ? 397  ALA   A HB2  1 
ATOM   5966  H  HB3  . ALA   A  1  397 ? 6.057   -9.420  -12.734  1.00 111.19 ? 397  ALA   A HB3  1 
ATOM   5967  N  N    . ARG   A  1  398 ? 3.889   -8.646  -11.268  1.00 111.03 ? 398  ARG   A N    1 
ATOM   5968  C  CA   . ARG   A  1  398 ? 2.967   -9.183  -10.276  1.00 118.77 ? 398  ARG   A CA   1 
ATOM   5969  C  C    . ARG   A  1  398 ? 2.562   -10.632 -10.538  1.00 123.45 ? 398  ARG   A C    1 
ATOM   5970  O  O    . ARG   A  1  398 ? 1.705   -11.155 -9.816   1.00 132.15 ? 398  ARG   A O    1 
ATOM   5971  C  CB   . ARG   A  1  398 ? 1.704   -8.313  -10.203  1.00 125.18 ? 398  ARG   A CB   1 
ATOM   5972  C  CG   . ARG   A  1  398 ? 1.964   -6.834  -9.938   1.00 131.78 ? 398  ARG   A CG   1 
ATOM   5973  C  CD   . ARG   A  1  398 ? 0.657   -6.063  -9.790   1.00 138.93 ? 398  ARG   A CD   1 
ATOM   5974  N  NE   . ARG   A  1  398 ? 0.802   -4.885  -8.937   1.00 142.29 ? 398  ARG   A NE   1 
ATOM   5975  C  CZ   . ARG   A  1  398 ? -0.197  -4.309  -8.272   1.00 148.72 ? 398  ARG   A CZ   1 
ATOM   5976  N  NH1  . ARG   A  1  398 ? 0.037   -3.241  -7.521   1.00 152.04 ? 398  ARG   A NH1  1 
ATOM   5977  N  NH2  . ARG   A  1  398 ? -1.427  -4.801  -8.345   1.00 152.09 ? 398  ARG   A NH2  1 
ATOM   5978  H  H    . ARG   A  1  398 ? 3.610   -8.722  -12.078  1.00 133.28 ? 398  ARG   A H    1 
ATOM   5979  H  HA   . ARG   A  1  398 ? 3.414   -9.163  -9.415   1.00 142.57 ? 398  ARG   A HA   1 
ATOM   5980  H  HB2  . ARG   A  1  398 ? 1.234   -8.380  -11.049  1.00 150.25 ? 398  ARG   A HB2  1 
ATOM   5981  H  HB3  . ARG   A  1  398 ? 1.143   -8.644  -9.484   1.00 150.25 ? 398  ARG   A HB3  1 
ATOM   5982  H  HG2  . ARG   A  1  398 ? 2.471   -6.738  -9.117   1.00 158.17 ? 398  ARG   A HG2  1 
ATOM   5983  H  HG3  . ARG   A  1  398 ? 2.460   -6.456  -10.681  1.00 158.17 ? 398  ARG   A HG3  1 
ATOM   5984  H  HD2  . ARG   A  1  398 ? 0.361   -5.767  -10.665  1.00 166.75 ? 398  ARG   A HD2  1 
ATOM   5985  H  HD3  . ARG   A  1  398 ? -0.011  -6.643  -9.393   1.00 166.75 ? 398  ARG   A HD3  1 
ATOM   5986  H  HE   . ARG   A  1  398 ? 1.587   -4.541  -8.859   1.00 170.78 ? 398  ARG   A HE   1 
ATOM   5987  H  HH11 . ARG   A  1  398 ? 0.833   -2.921  -7.464   1.00 182.48 ? 398  ARG   A HH11 1 
ATOM   5988  H  HH12 . ARG   A  1  398 ? -0.608  -2.868  -7.092   1.00 182.48 ? 398  ARG   A HH12 1 
ATOM   5989  H  HH21 . ARG   A  1  398 ? -1.583  -5.498  -8.824   1.00 182.55 ? 398  ARG   A HH21 1 
ATOM   5990  H  HH22 . ARG   A  1  398 ? -2.067  -4.424  -7.913   1.00 182.55 ? 398  ARG   A HH22 1 
ATOM   5991  N  N    . SER   A  1  399 ? 3.142   -11.296 -11.540  1.00 121.82 ? 399  SER   A N    1 
ATOM   5992  C  CA   . SER   A  1  399 ? 2.757   -12.670 -11.851  1.00 121.25 ? 399  SER   A CA   1 
ATOM   5993  C  C    . SER   A  1  399 ? 3.963   -13.601 -11.915  1.00 112.72 ? 399  SER   A C    1 
ATOM   5994  O  O    . SER   A  1  399 ? 4.089   -14.524 -11.104  1.00 111.31 ? 399  SER   A O    1 
ATOM   5995  C  CB   . SER   A  1  399 ? 1.983   -12.712 -13.173  1.00 129.46 ? 399  SER   A CB   1 
ATOM   5996  O  OG   . SER   A  1  399 ? 2.504   -11.776 -14.101  1.00 133.67 ? 399  SER   A OG   1 
ATOM   5997  H  H    . SER   A  1  399 ? 3.755   -10.974 -12.049  1.00 146.23 ? 399  SER   A H    1 
ATOM   5998  H  HA   . SER   A  1  399 ? 2.182   -12.995 -11.140  1.00 145.54 ? 399  SER   A HA   1 
ATOM   5999  H  HB2  . SER   A  1  399 ? 2.055   -13.602 -13.551  1.00 155.39 ? 399  SER   A HB2  1 
ATOM   6000  H  HB3  . SER   A  1  399 ? 1.053   -12.499 -13.000  1.00 155.39 ? 399  SER   A HB3  1 
ATOM   6001  H  HG   . SER   A  1  399 ? 2.775   -12.174 -14.789  1.00 160.44 ? 399  SER   A HG   1 
ATOM   6002  N  N    . CYS   A  1  400 ? 4.846   -13.373 -12.887  1.00 95.96  ? 400  CYS   A N    1 
ATOM   6003  C  CA   . CYS   A  1  400 ? 6.077   -14.120 -13.083  1.00 83.69  ? 400  CYS   A CA   1 
ATOM   6004  C  C    . CYS   A  1  400 ? 7.258   -13.157 -13.024  1.00 76.58  ? 400  CYS   A C    1 
ATOM   6005  O  O    . CYS   A  1  400 ? 7.131   -12.007 -13.459  1.00 77.82  ? 400  CYS   A O    1 
ATOM   6006  C  CB   . CYS   A  1  400 ? 6.049   -14.847 -14.437  1.00 84.22  ? 400  CYS   A CB   1 
ATOM   6007  S  SG   . CYS   A  1  400 ? 7.426   -15.973 -14.793  1.00 82.56  ? 400  CYS   A SG   1 
ATOM   6008  H  H    . CYS   A  1  400 ? 4.744   -12.755 -13.476  1.00 115.19 ? 400  CYS   A H    1 
ATOM   6009  H  HA   . CYS   A  1  400 ? 6.192   -14.791 -12.392  1.00 100.46 ? 400  CYS   A HA   1 
ATOM   6010  H  HB2  . CYS   A  1  400 ? 5.235   -15.374 -14.477  1.00 101.10 ? 400  CYS   A HB2  1 
ATOM   6011  H  HB3  . CYS   A  1  400 ? 6.044   -14.176 -15.137  1.00 101.10 ? 400  CYS   A HB3  1 
ATOM   6012  N  N    . PRO   A  1  401 ? 8.403   -13.570 -12.481  1.00 68.80  ? 401  PRO   A N    1 
ATOM   6013  C  CA   . PRO   A  1  401 ? 9.480   -12.610 -12.253  1.00 63.97  ? 401  PRO   A CA   1 
ATOM   6014  C  C    . PRO   A  1  401 ? 9.863   -11.901 -13.538  1.00 59.50  ? 401  PRO   A C    1 
ATOM   6015  O  O    . PRO   A  1  401 ? 9.810   -12.490 -14.632  1.00 58.37  ? 401  PRO   A O    1 
ATOM   6016  C  CB   . PRO   A  1  401 ? 10.626  -13.485 -11.727  1.00 62.03  ? 401  PRO   A CB   1 
ATOM   6017  C  CG   . PRO   A  1  401 ? 9.943   -14.607 -11.061  1.00 64.97  ? 401  PRO   A CG   1 
ATOM   6018  C  CD   . PRO   A  1  401 ? 8.738   -14.893 -11.920  1.00 66.48  ? 401  PRO   A CD   1 
ATOM   6019  H  HA   . PRO   A  1  401 ? 9.223   -11.957 -11.584  1.00 76.80  ? 401  PRO   A HA   1 
ATOM   6020  H  HB2  . PRO   A  1  401 ? 11.174  -13.797 -12.464  1.00 74.47  ? 401  PRO   A HB2  1 
ATOM   6021  H  HB3  . PRO   A  1  401 ? 11.169  -12.983 -11.099  1.00 74.47  ? 401  PRO   A HB3  1 
ATOM   6022  H  HG2  . PRO   A  1  401 ? 10.532  -15.377 -11.022  1.00 78.00  ? 401  PRO   A HG2  1 
ATOM   6023  H  HG3  . PRO   A  1  401 ? 9.676   -14.348 -10.165  1.00 78.00  ? 401  PRO   A HG3  1 
ATOM   6024  H  HD2  . PRO   A  1  401 ? 8.957   -15.522 -12.626  1.00 79.81  ? 401  PRO   A HD2  1 
ATOM   6025  H  HD3  . PRO   A  1  401 ? 8.006   -15.238 -11.385  1.00 79.81  ? 401  PRO   A HD3  1 
ATOM   6026  N  N    . PRO   A  1  402 ? 10.259  -10.625 -13.448  1.00 59.93  ? 402  PRO   A N    1 
ATOM   6027  C  CA   . PRO   A  1  402 ? 10.657  -9.887  -14.661  1.00 60.70  ? 402  PRO   A CA   1 
ATOM   6028  C  C    . PRO   A  1  402 ? 11.664  -10.620 -15.536  1.00 58.78  ? 402  PRO   A C    1 
ATOM   6029  O  O    . PRO   A  1  402 ? 11.597  -10.516 -16.767  1.00 60.37  ? 402  PRO   A O    1 
ATOM   6030  C  CB   . PRO   A  1  402 ? 11.251  -8.587  -14.096  1.00 60.19  ? 402  PRO   A CB   1 
ATOM   6031  C  CG   . PRO   A  1  402 ? 10.628  -8.414  -12.756  1.00 60.84  ? 402  PRO   A CG   1 
ATOM   6032  C  CD   . PRO   A  1  402 ? 10.208  -9.762  -12.253  1.00 60.75  ? 402  PRO   A CD   1 
ATOM   6033  H  HA   . PRO   A  1  402 ? 9.865   -9.690  -15.185  1.00 72.88  ? 402  PRO   A HA   1 
ATOM   6034  H  HB2  . PRO   A  1  402 ? 12.214  -8.673  -14.020  1.00 72.27  ? 402  PRO   A HB2  1 
ATOM   6035  H  HB3  . PRO   A  1  402 ? 11.028  -7.845  -14.679  1.00 72.27  ? 402  PRO   A HB3  1 
ATOM   6036  H  HG2  . PRO   A  1  402 ? 11.278  -8.020  -12.153  1.00 73.04  ? 402  PRO   A HG2  1 
ATOM   6037  H  HG3  . PRO   A  1  402 ? 9.856   -7.833  -12.838  1.00 73.04  ? 402  PRO   A HG3  1 
ATOM   6038  H  HD2  . PRO   A  1  402 ? 10.823  -10.081 -11.574  1.00 72.94  ? 402  PRO   A HD2  1 
ATOM   6039  H  HD3  . PRO   A  1  402 ? 9.307   -9.728  -11.894  1.00 72.94  ? 402  PRO   A HD3  1 
ATOM   6040  N  N    . SER   A  1  403 ? 12.606  -11.346 -14.934  1.00 54.42  ? 403  SER   A N    1 
ATOM   6041  C  CA   . SER   A  1  403 ? 13.594  -12.128 -15.678  1.00 53.86  ? 403  SER   A CA   1 
ATOM   6042  C  C    . SER   A  1  403 ? 14.414  -11.248 -16.622  1.00 54.78  ? 403  SER   A C    1 
ATOM   6043  O  O    . SER   A  1  403 ? 14.719  -11.635 -17.752  1.00 54.15  ? 403  SER   A O    1 
ATOM   6044  C  CB   . SER   A  1  403 ? 12.922  -13.264 -16.453  1.00 55.86  ? 403  SER   A CB   1 
ATOM   6045  O  OG   . SER   A  1  403 ? 11.907  -13.880 -15.681  1.00 58.96  ? 403  SER   A OG   1 
ATOM   6046  H  H    . SER   A  1  403 ? 12.695  -11.403 -14.080  1.00 65.34  ? 403  SER   A H    1 
ATOM   6047  H  HA   . SER   A  1  403 ? 14.211  -12.517 -15.039  1.00 64.67  ? 403  SER   A HA   1 
ATOM   6048  H  HB2  . SER   A  1  403 ? 12.527  -12.902 -17.262  1.00 67.07  ? 403  SER   A HB2  1 
ATOM   6049  H  HB3  . SER   A  1  403 ? 13.591  -13.929 -16.680  1.00 67.07  ? 403  SER   A HB3  1 
ATOM   6050  H  HG   . SER   A  1  403 ? 11.192  -13.442 -15.745  1.00 70.79  ? 403  SER   A HG   1 
ATOM   6051  N  N    . PHE   A  1  404 ? 14.773  -10.054 -16.158  1.00 57.13  ? 404  PHE   A N    1 
ATOM   6052  C  CA   . PHE   A  1  404 ? 15.650  -9.176  -16.926  1.00 54.29  ? 404  PHE   A CA   1 
ATOM   6053  C  C    . PHE   A  1  404 ? 16.989  -9.859  -17.166  1.00 53.18  ? 404  PHE   A C    1 
ATOM   6054  O  O    . PHE   A  1  404 ? 17.681  -10.239 -16.217  1.00 53.33  ? 404  PHE   A O    1 
ATOM   6055  C  CB   . PHE   A  1  404 ? 15.838  -7.858  -16.173  1.00 53.47  ? 404  PHE   A CB   1 
ATOM   6056  C  CG   . PHE   A  1  404 ? 16.913  -6.967  -16.738  1.00 51.04  ? 404  PHE   A CG   1 
ATOM   6057  C  CD1  . PHE   A  1  404 ? 18.226  -7.079  -16.304  1.00 49.99  ? 404  PHE   A CD1  1 
ATOM   6058  C  CD2  . PHE   A  1  404 ? 16.605  -5.998  -17.678  1.00 54.27  ? 404  PHE   A CD2  1 
ATOM   6059  C  CE1  . PHE   A  1  404 ? 19.213  -6.253  -16.811  1.00 53.48  ? 404  PHE   A CE1  1 
ATOM   6060  C  CE2  . PHE   A  1  404 ? 17.588  -5.168  -18.187  1.00 56.21  ? 404  PHE   A CE2  1 
ATOM   6061  C  CZ   . PHE   A  1  404 ? 18.893  -5.296  -17.752  1.00 55.64  ? 404  PHE   A CZ   1 
ATOM   6062  H  H    . PHE   A  1  404 ? 14.523  -9.730  -15.402  1.00 68.59  ? 404  PHE   A H    1 
ATOM   6063  H  HA   . PHE   A  1  404 ? 15.250  -8.980  -17.787  1.00 65.19  ? 404  PHE   A HA   1 
ATOM   6064  H  HB2  . PHE   A  1  404 ? 15.003  -7.364  -16.200  1.00 64.20  ? 404  PHE   A HB2  1 
ATOM   6065  H  HB3  . PHE   A  1  404 ? 16.075  -8.058  -15.254  1.00 64.20  ? 404  PHE   A HB3  1 
ATOM   6066  H  HD1  . PHE   A  1  404 ? 18.445  -7.717  -15.664  1.00 60.03  ? 404  PHE   A HD1  1 
ATOM   6067  H  HD2  . PHE   A  1  404 ? 15.727  -5.903  -17.970  1.00 65.16  ? 404  PHE   A HD2  1 
ATOM   6068  H  HE1  . PHE   A  1  404 ? 20.091  -6.343  -16.519  1.00 64.22  ? 404  PHE   A HE1  1 
ATOM   6069  H  HE2  . PHE   A  1  404 ? 17.370  -4.525  -18.823  1.00 67.49  ? 404  PHE   A HE2  1 
ATOM   6070  H  HZ   . PHE   A  1  404 ? 19.554  -4.738  -18.093  1.00 66.80  ? 404  PHE   A HZ   1 
ATOM   6071  N  N    . GLY   A  1  405 ? 17.354  -10.016 -18.438  1.00 53.41  ? 405  GLY   A N    1 
ATOM   6072  C  CA   . GLY   A  1  405 ? 18.572  -10.703 -18.810  1.00 52.08  ? 405  GLY   A CA   1 
ATOM   6073  C  C    . GLY   A  1  405 ? 18.391  -12.154 -19.193  1.00 53.70  ? 405  GLY   A C    1 
ATOM   6074  O  O    . GLY   A  1  405 ? 19.367  -12.793 -19.607  1.00 51.83  ? 405  GLY   A O    1 
ATOM   6075  H  H    . GLY   A  1  405 ? 16.901  -9.726  -19.108  1.00 64.13  ? 405  GLY   A H    1 
ATOM   6076  H  HA2  . GLY   A  1  405 ? 18.968  -10.244 -19.568  1.00 62.53  ? 405  GLY   A HA2  1 
ATOM   6077  H  HA3  . GLY   A  1  405 ? 19.189  -10.669 -18.062  1.00 62.53  ? 405  GLY   A HA3  1 
ATOM   6078  N  N    . TYR   A  1  406 ? 17.177  -12.696 -19.069  1.00 54.20  ? 406  TYR   A N    1 
ATOM   6079  C  CA   . TYR   A  1  406 ? 16.935  -14.081 -19.458  1.00 52.37  ? 406  TYR   A CA   1 
ATOM   6080  C  C    . TYR   A  1  406 ? 17.366  -14.339 -20.894  1.00 54.81  ? 406  TYR   A C    1 
ATOM   6081  O  O    . TYR   A  1  406 ? 17.791  -15.452 -21.227  1.00 56.03  ? 406  TYR   A O    1 
ATOM   6082  C  CB   . TYR   A  1  406 ? 15.455  -14.417 -19.279  1.00 52.30  ? 406  TYR   A CB   1 
ATOM   6083  C  CG   . TYR   A  1  406 ? 15.133  -15.883 -19.442  1.00 49.16  ? 406  TYR   A CG   1 
ATOM   6084  C  CD1  . TYR   A  1  406 ? 14.838  -16.415 -20.690  1.00 47.29  ? 406  TYR   A CD1  1 
ATOM   6085  C  CD2  . TYR   A  1  406 ? 15.120  -16.735 -18.347  1.00 48.00  ? 406  TYR   A CD2  1 
ATOM   6086  C  CE1  . TYR   A  1  406 ? 14.542  -17.754 -20.843  1.00 46.39  ? 406  TYR   A CE1  1 
ATOM   6087  C  CE2  . TYR   A  1  406 ? 14.825  -18.076 -18.489  1.00 47.03  ? 406  TYR   A CE2  1 
ATOM   6088  C  CZ   . TYR   A  1  406 ? 14.537  -18.580 -19.739  1.00 48.89  ? 406  TYR   A CZ   1 
ATOM   6089  O  OH   . TYR   A  1  406 ? 14.242  -19.916 -19.885  1.00 54.44  ? 406  TYR   A OH   1 
ATOM   6090  H  H    . TYR   A  1  406 ? 16.485  -12.286 -18.764  1.00 65.08  ? 406  TYR   A H    1 
ATOM   6091  H  HA   . TYR   A  1  406 ? 17.448  -14.668 -18.881  1.00 62.88  ? 406  TYR   A HA   1 
ATOM   6092  H  HB2  . TYR   A  1  406 ? 15.182  -14.153 -18.387  1.00 62.80  ? 406  TYR   A HB2  1 
ATOM   6093  H  HB3  . TYR   A  1  406 ? 14.942  -13.927 -19.941  1.00 62.80  ? 406  TYR   A HB3  1 
ATOM   6094  H  HD1  . TYR   A  1  406 ? 14.840  -15.859 -21.436  1.00 56.78  ? 406  TYR   A HD1  1 
ATOM   6095  H  HD2  . TYR   A  1  406 ? 15.314  -16.397 -17.502  1.00 57.63  ? 406  TYR   A HD2  1 
ATOM   6096  H  HE1  . TYR   A  1  406 ? 14.348  -18.098 -21.685  1.00 55.71  ? 406  TYR   A HE1  1 
ATOM   6097  H  HE2  . TYR   A  1  406 ? 14.820  -18.635 -17.746  1.00 56.47  ? 406  TYR   A HE2  1 
ATOM   6098  H  HH   . TYR   A  1  406 ? 14.238  -20.293 -19.134  1.00 65.36  ? 406  TYR   A HH   1 
ATOM   6099  N  N    . SER   A  1  407 ? 17.259  -13.333 -21.757  1.00 56.68  ? 407  SER   A N    1 
ATOM   6100  C  CA   . SER   A  1  407 ? 17.782  -13.398 -23.112  1.00 57.54  ? 407  SER   A CA   1 
ATOM   6101  C  C    . SER   A  1  407 ? 18.578  -12.133 -23.392  1.00 54.42  ? 407  SER   A C    1 
ATOM   6102  O  O    . SER   A  1  407 ? 18.268  -11.056 -22.875  1.00 52.62  ? 407  SER   A O    1 
ATOM   6103  C  CB   . SER   A  1  407 ? 16.665  -13.550 -24.152  1.00 63.14  ? 407  SER   A CB   1 
ATOM   6104  O  OG   . SER   A  1  407 ? 15.883  -12.372 -24.236  1.00 65.60  ? 407  SER   A OG   1 
ATOM   6105  H  H    . SER   A  1  407 ? 16.876  -12.585 -21.574  1.00 68.06  ? 407  SER   A H    1 
ATOM   6106  H  HA   . SER   A  1  407 ? 18.370  -14.165 -23.198  1.00 69.09  ? 407  SER   A HA   1 
ATOM   6107  H  HB2  . SER   A  1  407 ? 17.064  -13.724 -25.019  1.00 75.81  ? 407  SER   A HB2  1 
ATOM   6108  H  HB3  . SER   A  1  407 ? 16.094  -14.290 -23.895  1.00 75.81  ? 407  SER   A HB3  1 
ATOM   6109  H  HG   . SER   A  1  407 ? 15.071  -12.558 -24.129  1.00 78.75  ? 407  SER   A HG   1 
ATOM   6110  N  N    . MET   A  1  408 ? 19.615  -12.277 -24.212  1.00 59.07  ? 408  MET   A N    1 
ATOM   6111  C  CA   . MET   A  1  408 ? 20.444  -11.148 -24.601  1.00 55.95  ? 408  MET   A CA   1 
ATOM   6112  C  C    . MET   A  1  408 ? 20.998  -11.405 -25.993  1.00 54.98  ? 408  MET   A C    1 
ATOM   6113  O  O    . MET   A  1  408 ? 21.097  -12.549 -26.443  1.00 56.09  ? 408  MET   A O    1 
ATOM   6114  C  CB   . MET   A  1  408 ? 21.602  -10.917 -23.621  1.00 53.41  ? 408  MET   A CB   1 
ATOM   6115  C  CG   . MET   A  1  408 ? 21.190  -10.673 -22.181  1.00 54.01  ? 408  MET   A CG   1 
ATOM   6116  S  SD   . MET   A  1  408 ? 22.608  -10.346 -21.113  1.00 53.97  ? 408  MET   A SD   1 
ATOM   6117  C  CE   . MET   A  1  408 ? 23.416  -11.946 -21.101  1.00 52.78  ? 408  MET   A CE   1 
ATOM   6118  H  H    . MET   A  1  408 ? 19.860  -13.025 -24.557  1.00 70.92  ? 408  MET   A H    1 
ATOM   6119  H  HA   . MET   A  1  408 ? 19.891  -10.351 -24.609  1.00 67.17  ? 408  MET   A HA   1 
ATOM   6120  H  HB2  . MET   A  1  408 ? 22.173  -11.701 -23.631  1.00 64.13  ? 408  MET   A HB2  1 
ATOM   6121  H  HB3  . MET   A  1  408 ? 22.102  -10.140 -23.916  1.00 64.13  ? 408  MET   A HB3  1 
ATOM   6122  H  HG2  . MET   A  1  408 ? 20.600  -9.904  -22.145  1.00 64.85  ? 408  MET   A HG2  1 
ATOM   6123  H  HG3  . MET   A  1  408 ? 20.732  -11.459 -21.844  1.00 64.85  ? 408  MET   A HG3  1 
ATOM   6124  H  HE1  . MET   A  1  408 ? 24.213  -11.893 -20.550  1.00 63.38  ? 408  MET   A HE1  1 
ATOM   6125  H  HE2  . MET   A  1  408 ? 22.806  -12.606 -20.736  1.00 63.38  ? 408  MET   A HE2  1 
ATOM   6126  H  HE3  . MET   A  1  408 ? 23.658  -12.186 -22.009  1.00 63.38  ? 408  MET   A HE3  1 
ATOM   6127  N  N    . LYS   A  1  409 ? 21.358  -10.318 -26.670  1.00 54.57  ? 409  LYS   A N    1 
ATOM   6128  C  CA   . LYS   A  1  409 ? 22.081  -10.406 -27.930  1.00 56.74  ? 409  LYS   A CA   1 
ATOM   6129  C  C    . LYS   A  1  409 ? 22.893  -9.134  -28.099  1.00 57.78  ? 409  LYS   A C    1 
ATOM   6130  O  O    . LYS   A  1  409 ? 22.373  -8.031  -27.899  1.00 57.89  ? 409  LYS   A O    1 
ATOM   6131  C  CB   . LYS   A  1  409 ? 21.135  -10.596 -29.119  1.00 57.40  ? 409  LYS   A CB   1 
ATOM   6132  C  CG   . LYS   A  1  409 ? 21.853  -10.913 -30.427  1.00 57.46  ? 409  LYS   A CG   1 
ATOM   6133  C  CD   . LYS   A  1  409 ? 22.217  -12.388 -30.528  1.00 54.72  ? 409  LYS   A CD   1 
ATOM   6134  C  CE   . LYS   A  1  409 ? 23.073  -12.668 -31.754  1.00 60.90  ? 409  LYS   A CE   1 
ATOM   6135  N  NZ   . LYS   A  1  409 ? 23.544  -14.081 -31.804  1.00 71.68  ? 409  LYS   A NZ   1 
ATOM   6136  H  H    . LYS   A  1  409 ? 21.193  -9.513  -26.416  1.00 65.52  ? 409  LYS   A H    1 
ATOM   6137  H  HA   . LYS   A  1  409 ? 22.681  -11.168 -27.908  1.00 68.13  ? 409  LYS   A HA   1 
ATOM   6138  H  HB2  . LYS   A  1  409 ? 20.533  -11.331 -28.926  1.00 68.92  ? 409  LYS   A HB2  1 
ATOM   6139  H  HB3  . LYS   A  1  409 ? 20.628  -9.779  -29.249  1.00 68.92  ? 409  LYS   A HB3  1 
ATOM   6140  H  HG2  . LYS   A  1  409 ? 21.274  -10.691 -31.173  1.00 68.99  ? 409  LYS   A HG2  1 
ATOM   6141  H  HG3  . LYS   A  1  409 ? 22.672  -10.394 -30.477  1.00 68.99  ? 409  LYS   A HG3  1 
ATOM   6142  H  HD2  . LYS   A  1  409 ? 22.718  -12.650 -29.740  1.00 65.70  ? 409  LYS   A HD2  1 
ATOM   6143  H  HD3  . LYS   A  1  409 ? 21.406  -12.915 -30.596  1.00 65.70  ? 409  LYS   A HD3  1 
ATOM   6144  H  HE2  . LYS   A  1  409 ? 22.551  -12.496 -32.553  1.00 73.12  ? 409  LYS   A HE2  1 
ATOM   6145  H  HE3  . LYS   A  1  409 ? 23.853  -12.091 -31.736  1.00 73.12  ? 409  LYS   A HE3  1 
ATOM   6146  H  HZ1  . LYS   A  1  409 ? 24.064  -14.204 -32.516  1.00 86.05  ? 409  LYS   A HZ1  1 
ATOM   6147  H  HZ2  . LYS   A  1  409 ? 24.009  -14.274 -31.070  1.00 86.05  ? 409  LYS   A HZ2  1 
ATOM   6148  H  HZ3  . LYS   A  1  409 ? 22.847  -14.633 -31.857  1.00 86.05  ? 409  LYS   A HZ3  1 
ATOM   6149  N  N    . GLY   A  1  410 ? 24.165  -9.286  -28.459  1.00 59.01  ? 410  GLY   A N    1 
ATOM   6150  C  CA   . GLY   A  1  410 ? 25.034  -8.152  -28.671  1.00 57.21  ? 410  GLY   A CA   1 
ATOM   6151  C  C    . GLY   A  1  410 ? 25.793  -8.266  -29.984  1.00 57.38  ? 410  GLY   A C    1 
ATOM   6152  O  O    . GLY   A  1  410 ? 25.356  -8.921  -30.922  1.00 60.43  ? 410  GLY   A O    1 
ATOM   6153  H  H    . GLY   A  1  410 ? 24.543  -10.048 -28.585  1.00 70.85  ? 410  GLY   A H    1 
ATOM   6154  H  HA2  . GLY   A  1  410 ? 24.508  -7.338  -28.690  1.00 68.68  ? 410  GLY   A HA2  1 
ATOM   6155  H  HA3  . GLY   A  1  410 ? 25.677  -8.096  -27.947  1.00 68.68  ? 410  GLY   A HA3  1 
ATOM   6156  N  N    . ALA   A  1  411 ? 26.954  -7.598  -30.033  1.00 54.82  ? 411  ALA   A N    1 
ATOM   6157  C  CA   . ALA   A  1  411 ? 27.871  -7.685  -31.171  1.00 53.88  ? 411  ALA   A CA   1 
ATOM   6158  C  C    . ALA   A  1  411 ? 27.283  -7.089  -32.447  1.00 56.69  ? 411  ALA   A C    1 
ATOM   6159  O  O    . ALA   A  1  411 ? 27.595  -7.543  -33.550  1.00 61.08  ? 411  ALA   A O    1 
ATOM   6160  C  CB   . ALA   A  1  411 ? 28.302  -9.134  -31.426  1.00 51.73  ? 411  ALA   A CB   1 
ATOM   6161  H  H    . ALA   A  1  411 ? 27.234  -7.080  -29.407  1.00 65.82  ? 411  ALA   A H    1 
ATOM   6162  H  HA   . ALA   A  1  411 ? 28.659  -7.164  -30.951  1.00 64.70  ? 411  ALA   A HA   1 
ATOM   6163  H  HB1  . ALA   A  1  411 ? 28.936  -9.150  -32.160  1.00 62.12  ? 411  ALA   A HB1  1 
ATOM   6164  H  HB2  . ALA   A  1  411 ? 28.717  -9.486  -30.623  1.00 62.12  ? 411  ALA   A HB2  1 
ATOM   6165  H  HB3  . ALA   A  1  411 ? 27.520  -9.661  -31.652  1.00 62.12  ? 411  ALA   A HB3  1 
ATOM   6166  N  N    . THR   A  1  412 ? 26.436  -6.070  -32.322  1.00 58.06  ? 412  THR   A N    1 
ATOM   6167  C  CA   . THR   A  1  412 ? 25.936  -5.338  -33.479  1.00 60.63  ? 412  THR   A CA   1 
ATOM   6168  C  C    . THR   A  1  412 ? 25.950  -3.852  -33.167  1.00 58.83  ? 412  THR   A C    1 
ATOM   6169  O  O    . THR   A  1  412 ? 25.421  -3.425  -32.136  1.00 56.65  ? 412  THR   A O    1 
ATOM   6170  C  CB   . THR   A  1  412 ? 24.517  -5.777  -33.860  1.00 65.28  ? 412  THR   A CB   1 
ATOM   6171  O  OG1  . THR   A  1  412 ? 24.557  -7.082  -34.451  1.00 71.40  ? 412  THR   A OG1  1 
ATOM   6172  C  CG2  . THR   A  1  412 ? 23.876  -4.788  -34.837  1.00 65.31  ? 412  THR   A CG2  1 
ATOM   6173  H  H    . THR   A  1  412 ? 26.134  -5.783  -31.570  1.00 69.71  ? 412  THR   A H    1 
ATOM   6174  H  HA   . THR   A  1  412 ? 26.519  -5.505  -34.236  1.00 72.79  ? 412  THR   A HA   1 
ATOM   6175  H  HB   . THR   A  1  412 ? 23.967  -5.801  -33.061  1.00 78.38  ? 412  THR   A HB   1 
ATOM   6176  H  HG1  . THR   A  1  412 ? 23.958  -7.567  -34.117  1.00 85.72  ? 412  THR   A HG1  1 
ATOM   6177  H  HG21 . THR   A  1  412 ? 22.999  -5.107  -35.104  1.00 78.41  ? 412  THR   A HG21 1 
ATOM   6178  H  HG22 . THR   A  1  412 ? 23.780  -3.920  -34.416  1.00 78.41  ? 412  THR   A HG22 1 
ATOM   6179  H  HG23 . THR   A  1  412 ? 24.431  -4.695  -35.627  1.00 78.41  ? 412  THR   A HG23 1 
ATOM   6180  N  N    . ASP   A  1  413 ? 26.541  -3.071  -34.067  1.00 62.26  ? 413  ASP   A N    1 
ATOM   6181  C  CA   . ASP   A  1  413 ? 26.583  -1.616  -33.938  1.00 64.31  ? 413  ASP   A CA   1 
ATOM   6182  C  C    . ASP   A  1  413 ? 25.347  -1.064  -34.635  1.00 67.23  ? 413  ASP   A C    1 
ATOM   6183  O  O    . ASP   A  1  413 ? 25.356  -0.785  -35.835  1.00 69.82  ? 413  ASP   A O    1 
ATOM   6184  C  CB   . ASP   A  1  413 ? 27.868  -1.062  -34.537  1.00 65.66  ? 413  ASP   A CB   1 
ATOM   6185  C  CG   . ASP   A  1  413 ? 28.109  0.385   -34.160  1.00 68.92  ? 413  ASP   A CG   1 
ATOM   6186  O  OD1  . ASP   A  1  413 ? 27.419  0.882   -33.248  1.00 68.97  ? 413  ASP   A OD1  1 
ATOM   6187  O  OD2  . ASP   A  1  413 ? 28.985  1.028   -34.777  1.00 71.87  ? 413  ASP   A OD2  1 
ATOM   6188  H  H    . ASP   A  1  413 ? 26.933  -3.365  -34.774  1.00 74.75  ? 413  ASP   A H    1 
ATOM   6189  H  HA   . ASP   A  1  413 ? 26.555  -1.365  -33.001  1.00 77.21  ? 413  ASP   A HA   1 
ATOM   6190  H  HB2  . ASP   A  1  413 ? 28.619  -1.585  -34.217  1.00 78.83  ? 413  ASP   A HB2  1 
ATOM   6191  H  HB3  . ASP   A  1  413 ? 27.815  -1.115  -35.505  1.00 78.83  ? 413  ASP   A HB3  1 
ATOM   6192  N  N    . ILE   A  1  414 ? 24.263  -0.904  -33.874  1.00 68.16  ? 414  ILE   A N    1 
ATOM   6193  C  CA   . ILE   A  1  414 ? 23.001  -0.522  -34.497  1.00 72.73  ? 414  ILE   A CA   1 
ATOM   6194  C  C    . ILE   A  1  414 ? 22.960  0.971   -34.800  1.00 76.61  ? 414  ILE   A C    1 
ATOM   6195  O  O    . ILE   A  1  414 ? 22.268  1.395   -35.732  1.00 78.60  ? 414  ILE   A O    1 
ATOM   6196  C  CB   . ILE   A  1  414 ? 21.811  -0.940  -33.618  1.00 70.74  ? 414  ILE   A CB   1 
ATOM   6197  C  CG1  . ILE   A  1  414 ? 20.510  -0.790  -34.406  1.00 70.23  ? 414  ILE   A CG1  1 
ATOM   6198  C  CG2  . ILE   A  1  414 ? 21.753  -0.097  -32.353  1.00 69.81  ? 414  ILE   A CG2  1 
ATOM   6199  C  CD1  . ILE   A  1  414 ? 19.315  -1.426  -33.743  1.00 67.53  ? 414  ILE   A CD1  1 
ATOM   6200  H  H    . ILE   A  1  414 ? 24.234  -1.007  -33.021  1.00 81.83  ? 414  ILE   A H    1 
ATOM   6201  H  HA   . ILE   A  1  414 ? 22.932  -0.998  -35.340  1.00 87.31  ? 414  ILE   A HA   1 
ATOM   6202  H  HB   . ILE   A  1  414 ? 21.929  -1.868  -33.362  1.00 84.93  ? 414  ILE   A HB   1 
ATOM   6203  H  HG12 . ILE   A  1  414 ? 20.319  0.155   -34.514  1.00 84.32  ? 414  ILE   A HG12 1 
ATOM   6204  H  HG13 . ILE   A  1  414 ? 20.623  -1.207  -35.275  1.00 84.32  ? 414  ILE   A HG13 1 
ATOM   6205  H  HG21 . ILE   A  1  414 ? 21.038  -0.427  -31.786  1.00 83.80  ? 414  ILE   A HG21 1 
ATOM   6206  H  HG22 . ILE   A  1  414 ? 22.602  -0.167  -31.888  1.00 83.80  ? 414  ILE   A HG22 1 
ATOM   6207  H  HG23 . ILE   A  1  414 ? 21.584  0.826   -32.596  1.00 83.80  ? 414  ILE   A HG23 1 
ATOM   6208  H  HD11 . ILE   A  1  414 ? 18.542  -1.322  -34.318  1.00 81.07  ? 414  ILE   A HD11 1 
ATOM   6209  H  HD12 . ILE   A  1  414 ? 19.498  -2.369  -33.602  1.00 81.07  ? 414  ILE   A HD12 1 
ATOM   6210  H  HD13 . ILE   A  1  414 ? 19.156  -0.989  -32.892  1.00 81.07  ? 414  ILE   A HD13 1 
ATOM   6211  N  N    . ASP   A  1  415 ? 23.677  1.790   -34.033  1.00 77.69  ? 415  ASP   A N    1 
ATOM   6212  C  CA   . ASP   A  1  415 ? 23.729  3.224   -34.278  1.00 81.98  ? 415  ASP   A CA   1 
ATOM   6213  C  C    . ASP   A  1  415 ? 24.978  3.636   -35.047  1.00 88.05  ? 415  ASP   A C    1 
ATOM   6214  O  O    . ASP   A  1  415 ? 25.266  4.833   -35.143  1.00 87.34  ? 415  ASP   A O    1 
ATOM   6215  C  CB   . ASP   A  1  415 ? 23.641  3.995   -32.958  1.00 79.35  ? 415  ASP   A CB   1 
ATOM   6216  C  CG   . ASP   A  1  415 ? 24.903  3.889   -32.129  1.00 76.61  ? 415  ASP   A CG   1 
ATOM   6217  O  OD1  . ASP   A  1  415 ? 25.638  2.893   -32.285  1.00 75.45  ? 415  ASP   A OD1  1 
ATOM   6218  O  OD2  . ASP   A  1  415 ? 25.158  4.805   -31.318  1.00 76.67  ? 415  ASP   A OD2  1 
ATOM   6219  H  H    . ASP   A  1  415 ? 24.145  1.533   -33.358  1.00 93.27  ? 415  ASP   A H    1 
ATOM   6220  H  HA   . ASP   A  1  415 ? 22.958  3.472   -34.811  1.00 98.41  ? 415  ASP   A HA   1 
ATOM   6221  H  HB2  . ASP   A  1  415 ? 23.486  4.933   -33.150  1.00 95.25  ? 415  ASP   A HB2  1 
ATOM   6222  H  HB3  . ASP   A  1  415 ? 22.907  3.639   -32.432  1.00 95.25  ? 415  ASP   A HB3  1 
ATOM   6223  N  N    . LYS   A  1  416 ? 25.723  2.673   -35.592  1.00 92.54  ? 416  LYS   A N    1 
ATOM   6224  C  CA   . LYS   A  1  416 ? 26.856  2.958   -36.471  1.00 97.40  ? 416  LYS   A CA   1 
ATOM   6225  C  C    . LYS   A  1  416 ? 27.795  3.991   -35.851  1.00 93.20  ? 416  LYS   A C    1 
ATOM   6226  O  O    . LYS   A  1  416 ? 28.300  4.889   -36.527  1.00 97.14  ? 416  LYS   A O    1 
ATOM   6227  C  CB   . LYS   A  1  416 ? 26.369  3.425   -37.845  1.00 106.07 ? 416  LYS   A CB   1 
ATOM   6228  C  CG   . LYS   A  1  416 ? 25.768  2.327   -38.715  1.00 111.51 ? 416  LYS   A CG   1 
ATOM   6229  C  CD   . LYS   A  1  416 ? 26.848  1.461   -39.349  1.00 118.84 ? 416  LYS   A CD   1 
ATOM   6230  C  CE   . LYS   A  1  416 ? 26.278  0.544   -40.421  1.00 126.79 ? 416  LYS   A CE   1 
ATOM   6231  N  NZ   . LYS   A  1  416 ? 27.311  -0.372  -40.982  1.00 135.74 ? 416  LYS   A NZ   1 
ATOM   6232  H  H    . LYS   A  1  416 ? 25.589  1.833   -35.467  1.00 111.09 ? 416  LYS   A H    1 
ATOM   6233  H  HA   . LYS   A  1  416 ? 27.364  2.140   -36.588  1.00 116.92 ? 416  LYS   A HA   1 
ATOM   6234  H  HB2  . LYS   A  1  416 ? 25.686  4.102   -37.717  1.00 127.32 ? 416  LYS   A HB2  1 
ATOM   6235  H  HB3  . LYS   A  1  416 ? 27.122  3.801   -38.328  1.00 127.32 ? 416  LYS   A HB3  1 
ATOM   6236  H  HG2  . LYS   A  1  416 ? 25.203  1.758   -38.169  1.00 133.85 ? 416  LYS   A HG2  1 
ATOM   6237  H  HG3  . LYS   A  1  416 ? 25.245  2.730   -39.426  1.00 133.85 ? 416  LYS   A HG3  1 
ATOM   6238  H  HD2  . LYS   A  1  416 ? 27.516  2.032   -39.760  1.00 142.65 ? 416  LYS   A HD2  1 
ATOM   6239  H  HD3  . LYS   A  1  416 ? 27.259  0.910   -38.664  1.00 142.65 ? 416  LYS   A HD3  1 
ATOM   6240  H  HE2  . LYS   A  1  416 ? 25.571  0.003   -40.035  1.00 152.18 ? 416  LYS   A HE2  1 
ATOM   6241  H  HE3  . LYS   A  1  416 ? 25.925  1.083   -41.147  1.00 152.18 ? 416  LYS   A HE3  1 
ATOM   6242  H  HZ1  . LYS   A  1  416 ? 26.949  -0.893  -41.607  1.00 162.92 ? 416  LYS   A HZ1  1 
ATOM   6243  H  HZ2  . LYS   A  1  416 ? 27.971  0.101   -41.347  1.00 162.92 ? 416  LYS   A HZ2  1 
ATOM   6244  H  HZ3  . LYS   A  1  416 ? 27.646  -0.885  -40.337  1.00 162.92 ? 416  LYS   A HZ3  1 
ATOM   6245  N  N    . ASN   A  1  417 ? 28.029  3.864   -34.546  1.00 84.67  ? 417  ASN   A N    1 
ATOM   6246  C  CA   . ASN   A  1  417 ? 28.928  4.756   -33.828  1.00 78.09  ? 417  ASN   A CA   1 
ATOM   6247  C  C    . ASN   A  1  417 ? 30.290  4.124   -33.567  1.00 74.16  ? 417  ASN   A C    1 
ATOM   6248  O  O    . ASN   A  1  417 ? 31.113  4.717   -32.863  1.00 72.33  ? 417  ASN   A O    1 
ATOM   6249  C  CB   . ASN   A  1  417 ? 28.295  5.197   -32.506  1.00 74.67  ? 417  ASN   A CB   1 
ATOM   6250  C  CG   . ASN   A  1  417 ? 28.559  4.223   -31.376  1.00 77.73  ? 417  ASN   A CG   1 
ATOM   6251  O  OD1  . ASN   A  1  417 ? 28.478  3.006   -31.553  1.00 78.80  ? 417  ASN   A OD1  1 
ATOM   6252  N  ND2  . ASN   A  1  417 ? 28.884  4.756   -30.203  1.00 77.95  ? 417  ASN   A ND2  1 
ATOM   6253  H  H    . ASN   A  1  417 ? 27.672  3.259   -34.050  1.00 101.64 ? 417  ASN   A H    1 
ATOM   6254  H  HA   . ASN   A  1  417 ? 29.067  5.551   -34.367  1.00 93.74  ? 417  ASN   A HA   1 
ATOM   6255  H  HB2  . ASN   A  1  417 ? 28.661  6.058   -32.251  1.00 89.64  ? 417  ASN   A HB2  1 
ATOM   6256  H  HB3  . ASN   A  1  417 ? 27.334  5.267   -32.623  1.00 89.64  ? 417  ASN   A HB3  1 
ATOM   6257  H  HD21 . ASN   A  1  417 ? 29.045  4.246   -29.529  1.00 93.58  ? 417  ASN   A HD21 1 
ATOM   6258  H  HD22 . ASN   A  1  417 ? 28.935  5.610   -30.118  1.00 93.58  ? 417  ASN   A HD22 1 
ATOM   6259  N  N    . GLY   A  1  418 ? 30.545  2.938   -34.118  1.00 73.75  ? 418  GLY   A N    1 
ATOM   6260  C  CA   . GLY   A  1  418 ? 31.825  2.281   -33.978  1.00 75.24  ? 418  GLY   A CA   1 
ATOM   6261  C  C    . GLY   A  1  418 ? 31.944  1.327   -32.810  1.00 73.97  ? 418  GLY   A C    1 
ATOM   6262  O  O    . GLY   A  1  418 ? 33.018  0.740   -32.621  1.00 75.99  ? 418  GLY   A O    1 
ATOM   6263  H  H    . GLY   A  1  418 ? 29.976  2.492   -34.584  1.00 88.54  ? 418  GLY   A H    1 
ATOM   6264  H  HA2  . GLY   A  1  418 ? 32.002  1.776   -34.788  1.00 90.33  ? 418  GLY   A HA2  1 
ATOM   6265  H  HA3  . GLY   A  1  418 ? 32.510  2.959   -33.873  1.00 90.33  ? 418  GLY   A HA3  1 
ATOM   6266  N  N    . TYR   A  1  419 ? 30.884  1.145   -32.022  1.00 73.50  ? 419  TYR   A N    1 
ATOM   6267  C  CA   . TYR   A  1  419 ? 30.932  0.293   -30.841  1.00 72.34  ? 419  TYR   A CA   1 
ATOM   6268  C  C    . TYR   A  1  419 ? 29.698  -0.602  -30.815  1.00 71.28  ? 419  TYR   A C    1 
ATOM   6269  O  O    . TYR   A  1  419 ? 28.574  -0.108  -31.004  1.00 71.41  ? 419  TYR   A O    1 
ATOM   6270  C  CB   . TYR   A  1  419 ? 31.012  1.149   -29.568  1.00 70.88  ? 419  TYR   A CB   1 
ATOM   6271  C  CG   . TYR   A  1  419 ? 32.280  1.969   -29.472  1.00 73.29  ? 419  TYR   A CG   1 
ATOM   6272  C  CD1  . TYR   A  1  419 ? 32.431  3.143   -30.201  1.00 78.01  ? 419  TYR   A CD1  1 
ATOM   6273  C  CD2  . TYR   A  1  419 ? 33.329  1.569   -28.655  1.00 74.47  ? 419  TYR   A CD2  1 
ATOM   6274  C  CE1  . TYR   A  1  419 ? 33.592  3.891   -30.122  1.00 79.60  ? 419  TYR   A CE1  1 
ATOM   6275  C  CE2  . TYR   A  1  419 ? 34.490  2.314   -28.564  1.00 77.12  ? 419  TYR   A CE2  1 
ATOM   6276  C  CZ   . TYR   A  1  419 ? 34.618  3.471   -29.301  1.00 78.69  ? 419  TYR   A CZ   1 
ATOM   6277  O  OH   . TYR   A  1  419 ? 35.774  4.213   -29.208  1.00 82.38  ? 419  TYR   A OH   1 
ATOM   6278  H  H    . TYR   A  1  419 ? 30.118  1.511   -32.155  1.00 88.23  ? 419  TYR   A H    1 
ATOM   6279  H  HA   . TYR   A  1  419 ? 31.714  -0.278  -30.883  1.00 86.85  ? 419  TYR   A HA   1 
ATOM   6280  H  HB2  . TYR   A  1  419 ? 30.259  1.761   -29.555  1.00 85.09  ? 419  TYR   A HB2  1 
ATOM   6281  H  HB3  . TYR   A  1  419 ? 30.977  0.564   -28.795  1.00 85.09  ? 419  TYR   A HB3  1 
ATOM   6282  H  HD1  . TYR   A  1  419 ? 31.739  3.430   -30.752  1.00 93.65  ? 419  TYR   A HD1  1 
ATOM   6283  H  HD2  . TYR   A  1  419 ? 33.248  0.786   -28.160  1.00 89.41  ? 419  TYR   A HD2  1 
ATOM   6284  H  HE1  . TYR   A  1  419 ? 33.680  4.673   -30.619  1.00 95.56  ? 419  TYR   A HE1  1 
ATOM   6285  H  HE2  . TYR   A  1  419 ? 35.181  2.035   -28.008  1.00 92.58  ? 419  TYR   A HE2  1 
ATOM   6286  H  HH   . TYR   A  1  419 ? 35.712  4.902   -29.684  1.00 98.89  ? 419  TYR   A HH   1 
ATOM   6287  N  N    . PRO   A  1  420 ? 29.850  -1.907  -30.586  1.00 69.95  ? 420  PRO   A N    1 
ATOM   6288  C  CA   . PRO   A  1  420 ? 28.680  -2.793  -30.593  1.00 66.48  ? 420  PRO   A CA   1 
ATOM   6289  C  C    . PRO   A  1  420 ? 27.722  -2.465  -29.459  1.00 66.58  ? 420  PRO   A C    1 
ATOM   6290  O  O    . PRO   A  1  420 ? 28.098  -1.915  -28.423  1.00 66.60  ? 420  PRO   A O    1 
ATOM   6291  C  CB   . PRO   A  1  420 ? 29.281  -4.195  -30.421  1.00 66.69  ? 420  PRO   A CB   1 
ATOM   6292  C  CG   . PRO   A  1  420 ? 30.743  -4.045  -30.686  1.00 69.58  ? 420  PRO   A CG   1 
ATOM   6293  C  CD   . PRO   A  1  420 ? 31.088  -2.650  -30.289  1.00 70.22  ? 420  PRO   A CD   1 
ATOM   6294  H  HA   . PRO   A  1  420 ? 28.216  -2.739  -31.443  1.00 79.81  ? 420  PRO   A HA   1 
ATOM   6295  H  HB2  . PRO   A  1  420 ? 29.125  -4.509  -29.517  1.00 80.07  ? 420  PRO   A HB2  1 
ATOM   6296  H  HB3  . PRO   A  1  420 ? 28.876  -4.804  -31.058  1.00 80.07  ? 420  PRO   A HB3  1 
ATOM   6297  H  HG2  . PRO   A  1  420 ? 31.239  -4.686  -30.155  1.00 83.53  ? 420  PRO   A HG2  1 
ATOM   6298  H  HG3  . PRO   A  1  420 ? 30.921  -4.187  -31.629  1.00 83.53  ? 420  PRO   A HG3  1 
ATOM   6299  H  HD2  . PRO   A  1  420 ? 31.303  -2.602  -29.344  1.00 84.31  ? 420  PRO   A HD2  1 
ATOM   6300  H  HD3  . PRO   A  1  420 ? 31.829  -2.313  -30.816  1.00 84.31  ? 420  PRO   A HD3  1 
ATOM   6301  N  N    . ASP   A  1  421 ? 26.460  -2.826  -29.670  1.00 65.50  ? 421  ASP   A N    1 
ATOM   6302  C  CA   . ASP   A  1  421 ? 25.385  -2.529  -28.736  1.00 64.00  ? 421  ASP   A CA   1 
ATOM   6303  C  C    . ASP   A  1  421 ? 24.712  -3.822  -28.293  1.00 63.87  ? 421  ASP   A C    1 
ATOM   6304  O  O    . ASP   A  1  421 ? 24.877  -4.877  -28.911  1.00 66.66  ? 421  ASP   A O    1 
ATOM   6305  C  CB   . ASP   A  1  421 ? 24.374  -1.570  -29.373  1.00 65.57  ? 421  ASP   A CB   1 
ATOM   6306  C  CG   . ASP   A  1  421 ? 25.039  -0.322  -29.934  1.00 65.90  ? 421  ASP   A CG   1 
ATOM   6307  O  OD1  . ASP   A  1  421 ? 25.844  0.298   -29.207  1.00 64.13  ? 421  ASP   A OD1  1 
ATOM   6308  O  OD2  . ASP   A  1  421 ? 24.778  0.029   -31.104  1.00 68.42  ? 421  ASP   A OD2  1 
ATOM   6309  H  H    . ASP   A  1  421 ? 26.196  -3.255  -30.368  1.00 78.63  ? 421  ASP   A H    1 
ATOM   6310  H  HA   . ASP   A  1  421 ? 25.738  -2.105  -27.938  1.00 76.83  ? 421  ASP   A HA   1 
ATOM   6311  H  HB2  . ASP   A  1  421 ? 23.921  -2.023  -30.101  1.00 78.72  ? 421  ASP   A HB2  1 
ATOM   6312  H  HB3  . ASP   A  1  421 ? 23.731  -1.294  -28.702  1.00 78.72  ? 421  ASP   A HB3  1 
ATOM   6313  N  N    . LEU   A  1  422 ? 23.947  -3.730  -27.205  1.00 62.53  ? 422  LEU   A N    1 
ATOM   6314  C  CA   . LEU   A  1  422 ? 23.416  -4.895  -26.509  1.00 62.80  ? 422  LEU   A CA   1 
ATOM   6315  C  C    . LEU   A  1  422 ? 21.901  -4.814  -26.387  1.00 63.23  ? 422  LEU   A C    1 
ATOM   6316  O  O    . LEU   A  1  422 ? 21.351  -3.766  -26.036  1.00 62.23  ? 422  LEU   A O    1 
ATOM   6317  C  CB   . LEU   A  1  422 ? 24.036  -5.013  -25.108  1.00 61.12  ? 422  LEU   A CB   1 
ATOM   6318  C  CG   . LEU   A  1  422 ? 23.446  -6.066  -24.167  1.00 59.08  ? 422  LEU   A CG   1 
ATOM   6319  C  CD1  . LEU   A  1  422 ? 23.675  -7.464  -24.716  1.00 58.49  ? 422  LEU   A CD1  1 
ATOM   6320  C  CD2  . LEU   A  1  422 ? 24.037  -5.927  -22.770  1.00 58.84  ? 422  LEU   A CD2  1 
ATOM   6321  H  H    . LEU   A  1  422 ? 23.719  -2.984  -26.845  1.00 75.08  ? 422  LEU   A H    1 
ATOM   6322  H  HA   . LEU   A  1  422 ? 23.623  -5.690  -27.023  1.00 75.40  ? 422  LEU   A HA   1 
ATOM   6323  H  HB2  . LEU   A  1  422 ? 24.976  -5.227  -25.217  1.00 73.38  ? 422  LEU   A HB2  1 
ATOM   6324  H  HB3  . LEU   A  1  422 ? 23.940  -4.155  -24.667  1.00 73.38  ? 422  LEU   A HB3  1 
ATOM   6325  H  HG   . LEU   A  1  422 ? 22.489  -5.928  -24.099  1.00 70.93  ? 422  LEU   A HG   1 
ATOM   6326  H  HD11 . LEU   A  1  422 ? 23.321  -8.112  -24.087  1.00 70.23  ? 422  LEU   A HD11 1 
ATOM   6327  H  HD12 . LEU   A  1  422 ? 23.219  -7.547  -25.568  1.00 70.23  ? 422  LEU   A HD12 1 
ATOM   6328  H  HD13 . LEU   A  1  422 ? 24.627  -7.604  -24.835  1.00 70.23  ? 422  LEU   A HD13 1 
ATOM   6329  H  HD21 . LEU   A  1  422 ? 23.652  -6.607  -22.195  1.00 70.64  ? 422  LEU   A HD21 1 
ATOM   6330  H  HD22 . LEU   A  1  422 ? 24.999  -6.043  -22.821  1.00 70.64  ? 422  LEU   A HD22 1 
ATOM   6331  H  HD23 . LEU   A  1  422 ? 23.828  -5.045  -22.425  1.00 70.64  ? 422  LEU   A HD23 1 
ATOM   6332  N  N    . ILE   A  1  423 ? 21.232  -5.936  -26.665  1.00 60.29  ? 423  ILE   A N    1 
ATOM   6333  C  CA   . ILE   A  1  423 ? 19.803  -6.094  -26.415  1.00 59.32  ? 423  ILE   A CA   1 
ATOM   6334  C  C    . ILE   A  1  423 ? 19.631  -6.974  -25.186  1.00 59.70  ? 423  ILE   A C    1 
ATOM   6335  O  O    . ILE   A  1  423 ? 20.304  -8.004  -25.046  1.00 59.72  ? 423  ILE   A O    1 
ATOM   6336  C  CB   . ILE   A  1  423 ? 19.072  -6.711  -27.623  1.00 65.00  ? 423  ILE   A CB   1 
ATOM   6337  C  CG1  . ILE   A  1  423 ? 19.337  -5.905  -28.895  1.00 67.22  ? 423  ILE   A CG1  1 
ATOM   6338  C  CG2  . ILE   A  1  423 ? 17.571  -6.779  -27.349  1.00 65.86  ? 423  ILE   A CG2  1 
ATOM   6339  C  CD1  . ILE   A  1  423 ? 18.869  -6.599  -30.164  1.00 67.57  ? 423  ILE   A CD1  1 
ATOM   6340  H  H    . ILE   A  1  423 ? 21.597  -6.635  -27.008  1.00 72.38  ? 423  ILE   A H    1 
ATOM   6341  H  HA   . ILE   A  1  423 ? 19.417  -5.221  -26.247  1.00 71.22  ? 423  ILE   A HA   1 
ATOM   6342  H  HB   . ILE   A  1  423 ? 19.415  -7.608  -27.756  1.00 78.04  ? 423  ILE   A HB   1 
ATOM   6343  H  HG12 . ILE   A  1  423 ? 18.870  -5.057  -28.831  1.00 80.71  ? 423  ILE   A HG12 1 
ATOM   6344  H  HG13 . ILE   A  1  423 ? 20.292  -5.752  -28.975  1.00 80.71  ? 423  ILE   A HG13 1 
ATOM   6345  H  HG21 . ILE   A  1  423 ? 17.125  -7.159  -28.122  1.00 79.07  ? 423  ILE   A HG21 1 
ATOM   6346  H  HG22 . ILE   A  1  423 ? 17.417  -7.338  -26.571  1.00 79.07  ? 423  ILE   A HG22 1 
ATOM   6347  H  HG23 . ILE   A  1  423 ? 17.239  -5.883  -27.183  1.00 79.07  ? 423  ILE   A HG23 1 
ATOM   6348  H  HD11 . ILE   A  1  423 ? 19.089  -6.044  -30.928  1.00 81.12  ? 423  ILE   A HD11 1 
ATOM   6349  H  HD12 . ILE   A  1  423 ? 19.318  -7.456  -30.238  1.00 81.12  ? 423  ILE   A HD12 1 
ATOM   6350  H  HD13 . ILE   A  1  423 ? 17.910  -6.731  -30.116  1.00 81.12  ? 423  ILE   A HD13 1 
ATOM   6351  N  N    . VAL   A  1  424 ? 18.726  -6.575  -24.296  1.00 61.49  ? 424  VAL   A N    1 
ATOM   6352  C  CA   . VAL   A  1  424 ? 18.386  -7.354  -23.112  1.00 60.52  ? 424  VAL   A CA   1 
ATOM   6353  C  C    . VAL   A  1  424 ? 16.877  -7.536  -23.079  1.00 58.86  ? 424  VAL   A C    1 
ATOM   6354  O  O    . VAL   A  1  424 ? 16.128  -6.554  -23.154  1.00 60.76  ? 424  VAL   A O    1 
ATOM   6355  C  CB   . VAL   A  1  424 ? 18.873  -6.680  -21.814  1.00 60.61  ? 424  VAL   A CB   1 
ATOM   6356  C  CG1  . VAL   A  1  424 ? 18.450  -7.501  -20.602  1.00 60.13  ? 424  VAL   A CG1  1 
ATOM   6357  C  CG2  . VAL   A  1  424 ? 20.382  -6.502  -21.840  1.00 62.45  ? 424  VAL   A CG2  1 
ATOM   6358  H  H    . VAL   A  1  424 ? 18.287  -5.838  -24.359  1.00 73.83  ? 424  VAL   A H    1 
ATOM   6359  H  HA   . VAL   A  1  424 ? 18.804  -8.227  -23.176  1.00 72.66  ? 424  VAL   A HA   1 
ATOM   6360  H  HB   . VAL   A  1  424 ? 18.467  -5.802  -21.743  1.00 72.77  ? 424  VAL   A HB   1 
ATOM   6361  H  HG11 . VAL   A  1  424 ? 18.837  -7.108  -19.804  1.00 72.19  ? 424  VAL   A HG11 1 
ATOM   6362  H  HG12 . VAL   A  1  424 ? 17.482  -7.493  -20.538  1.00 72.19  ? 424  VAL   A HG12 1 
ATOM   6363  H  HG13 . VAL   A  1  424 ? 18.767  -8.411  -20.710  1.00 72.19  ? 424  VAL   A HG13 1 
ATOM   6364  H  HG21 . VAL   A  1  424 ? 20.666  -6.092  -21.008  1.00 74.98  ? 424  VAL   A HG21 1 
ATOM   6365  H  HG22 . VAL   A  1  424 ? 20.801  -7.371  -21.940  1.00 74.98  ? 424  VAL   A HG22 1 
ATOM   6366  H  HG23 . VAL   A  1  424 ? 20.620  -5.932  -22.588  1.00 74.98  ? 424  VAL   A HG23 1 
ATOM   6367  N  N    . GLY   A  1  425 ? 16.429  -8.784  -22.964  1.00 56.53  ? 425  GLY   A N    1 
ATOM   6368  C  CA   . GLY   A  1  425 ? 15.023  -9.074  -22.815  1.00 54.46  ? 425  GLY   A CA   1 
ATOM   6369  C  C    . GLY   A  1  425 ? 14.614  -9.236  -21.360  1.00 51.81  ? 425  GLY   A C    1 
ATOM   6370  O  O    . GLY   A  1  425 ? 15.429  -9.538  -20.491  1.00 50.46  ? 425  GLY   A O    1 
ATOM   6371  H  H    . GLY   A  1  425 ? 16.932  -9.481  -22.970  1.00 67.87  ? 425  GLY   A H    1 
ATOM   6372  H  HA2  . GLY   A  1  425 ? 14.504  -8.351  -23.200  1.00 65.38  ? 425  GLY   A HA2  1 
ATOM   6373  H  HA3  . GLY   A  1  425 ? 14.815  -9.897  -23.284  1.00 65.38  ? 425  GLY   A HA3  1 
ATOM   6374  N  N    . ALA   A  1  426 ? 13.319  -9.026  -21.105  1.00 52.06  ? 426  ALA   A N    1 
ATOM   6375  C  CA   . ALA   A  1  426 ? 12.734  -9.143  -19.772  1.00 51.88  ? 426  ALA   A CA   1 
ATOM   6376  C  C    . ALA   A  1  426 ? 11.295  -9.637  -19.949  1.00 55.31  ? 426  ALA   A C    1 
ATOM   6377  O  O    . ALA   A  1  426 ? 10.320  -8.901  -19.799  1.00 58.80  ? 426  ALA   A O    1 
ATOM   6378  C  CB   . ALA   A  1  426 ? 12.789  -7.815  -19.014  1.00 49.78  ? 426  ALA   A CB   1 
ATOM   6379  H  H    . ALA   A  1  426 ? 12.746  -8.809  -21.708  1.00 62.51  ? 426  ALA   A H    1 
ATOM   6380  H  HA   . ALA   A  1  426 ? 13.224  -9.802  -19.256  1.00 62.29  ? 426  ALA   A HA   1 
ATOM   6381  H  HB1  . ALA   A  1  426 ? 12.421  -7.944  -18.125  1.00 59.77  ? 426  ALA   A HB1  1 
ATOM   6382  H  HB2  . ALA   A  1  426 ? 13.712  -7.526  -18.951  1.00 59.77  ? 426  ALA   A HB2  1 
ATOM   6383  H  HB3  . ALA   A  1  426 ? 12.267  -7.155  -19.495  1.00 59.77  ? 426  ALA   A HB3  1 
ATOM   6384  N  N    . PHE   A  1  427 ? 11.153  -10.927 -20.267  1.00 55.94  ? 427  PHE   A N    1 
ATOM   6385  C  CA   . PHE   A  1  427 ? 9.858   -11.437 -20.707  1.00 59.05  ? 427  PHE   A CA   1 
ATOM   6386  C  C    . PHE   A  1  427 ? 8.812   -11.389 -19.599  1.00 61.53  ? 427  PHE   A C    1 
ATOM   6387  O  O    . PHE   A  1  427 ? 7.612   -11.326 -19.890  1.00 64.99  ? 427  PHE   A O    1 
ATOM   6388  C  CB   . PHE   A  1  427 ? 10.007  -12.865 -21.248  1.00 58.10  ? 427  PHE   A CB   1 
ATOM   6389  C  CG   . PHE   A  1  427 ? 10.191  -13.918 -20.185  1.00 57.05  ? 427  PHE   A CG   1 
ATOM   6390  C  CD1  . PHE   A  1  427 ? 9.095   -14.494 -19.561  1.00 54.94  ? 427  PHE   A CD1  1 
ATOM   6391  C  CD2  . PHE   A  1  427 ? 11.459  -14.356 -19.834  1.00 57.12  ? 427  PHE   A CD2  1 
ATOM   6392  C  CE1  . PHE   A  1  427 ? 9.260   -15.470 -18.594  1.00 55.51  ? 427  PHE   A CE1  1 
ATOM   6393  C  CE2  . PHE   A  1  427 ? 11.629  -15.334 -18.869  1.00 57.08  ? 427  PHE   A CE2  1 
ATOM   6394  C  CZ   . PHE   A  1  427 ? 10.528  -15.891 -18.250  1.00 56.48  ? 427  PHE   A CZ   1 
ATOM   6395  H  H    . PHE   A  1  427 ? 11.780  -11.515 -20.237  1.00 67.16  ? 427  PHE   A H    1 
ATOM   6396  H  HA   . PHE   A  1  427 ? 9.539   -10.875 -21.431  1.00 70.89  ? 427  PHE   A HA   1 
ATOM   6397  H  HB2  . PHE   A  1  427 ? 9.207   -13.091 -21.749  1.00 69.76  ? 427  PHE   A HB2  1 
ATOM   6398  H  HB3  . PHE   A  1  427 ? 10.782  -12.896 -21.829  1.00 69.76  ? 427  PHE   A HB3  1 
ATOM   6399  H  HD1  . PHE   A  1  427 ? 8.238   -14.221 -19.795  1.00 65.97  ? 427  PHE   A HD1  1 
ATOM   6400  H  HD2  . PHE   A  1  427 ? 12.204  -13.989 -20.253  1.00 68.58  ? 427  PHE   A HD2  1 
ATOM   6401  H  HE1  . PHE   A  1  427 ? 8.517   -15.841 -18.177  1.00 66.65  ? 427  PHE   A HE1  1 
ATOM   6402  H  HE2  . PHE   A  1  427 ? 12.484  -15.616 -18.637  1.00 68.53  ? 427  PHE   A HE2  1 
ATOM   6403  H  HZ   . PHE   A  1  427 ? 10.640  -16.549 -17.602  1.00 67.81  ? 427  PHE   A HZ   1 
ATOM   6404  N  N    . GLY   A  1  428 ? 9.234   -11.414 -18.334  1.00 59.28  ? 428  GLY   A N    1 
ATOM   6405  C  CA   . GLY   A  1  428 ? 8.278   -11.379 -17.240  1.00 58.68  ? 428  GLY   A CA   1 
ATOM   6406  C  C    . GLY   A  1  428 ? 7.548   -10.060 -17.103  1.00 59.56  ? 428  GLY   A C    1 
ATOM   6407  O  O    . GLY   A  1  428 ? 6.493   -10.011 -16.462  1.00 61.04  ? 428  GLY   A O    1 
ATOM   6408  H  H    . GLY   A  1  428 ? 10.058  -11.451 -18.090  1.00 71.17  ? 428  GLY   A H    1 
ATOM   6409  H  HA2  . GLY   A  1  428 ? 7.616   -12.074 -17.379  1.00 70.45  ? 428  GLY   A HA2  1 
ATOM   6410  H  HA3  . GLY   A  1  428 ? 8.746   -11.549 -16.408  1.00 70.45  ? 428  GLY   A HA3  1 
ATOM   6411  N  N    . VAL   A  1  429 ? 8.093   -8.989  -17.679  1.00 62.37  ? 429  VAL   A N    1 
ATOM   6412  C  CA   . VAL   A  1  429 ? 7.428   -7.697  -17.750  1.00 63.99  ? 429  VAL   A CA   1 
ATOM   6413  C  C    . VAL   A  1  429 ? 7.162   -7.280  -19.190  1.00 66.49  ? 429  VAL   A C    1 
ATOM   6414  O  O    . VAL   A  1  429 ? 6.810   -6.127  -19.443  1.00 66.90  ? 429  VAL   A O    1 
ATOM   6415  C  CB   . VAL   A  1  429 ? 8.233   -6.611  -17.008  1.00 58.25  ? 429  VAL   A CB   1 
ATOM   6416  C  CG1  . VAL   A  1  429 ? 8.265   -6.902  -15.515  1.00 58.15  ? 429  VAL   A CG1  1 
ATOM   6417  C  CG2  . VAL   A  1  429 ? 9.644   -6.513  -17.571  1.00 53.95  ? 429  VAL   A CG2  1 
ATOM   6418  H  H    . VAL   A  1  429 ? 8.871   -8.990  -18.044  1.00 74.89  ? 429  VAL   A H    1 
ATOM   6419  H  HA   . VAL   A  1  429 ? 6.568   -7.777  -17.308  1.00 76.83  ? 429  VAL   A HA   1 
ATOM   6420  H  HB   . VAL   A  1  429 ? 7.800   -5.753  -17.139  1.00 69.93  ? 429  VAL   A HB   1 
ATOM   6421  H  HG11 . VAL   A  1  429 ? 8.776   -6.208  -15.069  1.00 69.82  ? 429  VAL   A HG11 1 
ATOM   6422  H  HG12 . VAL   A  1  429 ? 7.356   -6.914  -15.176  1.00 69.82  ? 429  VAL   A HG12 1 
ATOM   6423  H  HG13 . VAL   A  1  429 ? 8.684   -7.765  -15.370  1.00 69.82  ? 429  VAL   A HG13 1 
ATOM   6424  H  HG21 . VAL   A  1  429 ? 10.126  -5.819  -17.095  1.00 64.78  ? 429  VAL   A HG21 1 
ATOM   6425  H  HG22 . VAL   A  1  429 ? 10.091  -7.366  -17.453  1.00 64.78  ? 429  VAL   A HG22 1 
ATOM   6426  H  HG23 . VAL   A  1  429 ? 9.593   -6.294  -18.514  1.00 64.78  ? 429  VAL   A HG23 1 
ATOM   6427  N  N    . ASP   A  1  430 ? 7.331   -8.197  -20.140  1.00 69.16  ? 430  ASP   A N    1 
ATOM   6428  C  CA   . ASP   A  1  430 ? 7.033   -7.945  -21.546  1.00 73.44  ? 430  ASP   A CA   1 
ATOM   6429  C  C    . ASP   A  1  430 ? 7.775   -6.703  -22.034  1.00 76.35  ? 430  ASP   A C    1 
ATOM   6430  O  O    . ASP   A  1  430 ? 7.193   -5.748  -22.551  1.00 78.42  ? 430  ASP   A O    1 
ATOM   6431  C  CB   . ASP   A  1  430 ? 5.522   -7.816  -21.748  1.00 74.84  ? 430  ASP   A CB   1 
ATOM   6432  C  CG   . ASP   A  1  430 ? 4.760   -8.991  -21.164  1.00 78.68  ? 430  ASP   A CG   1 
ATOM   6433  O  OD1  . ASP   A  1  430 ? 5.004   -10.136 -21.601  1.00 78.87  ? 430  ASP   A OD1  1 
ATOM   6434  O  OD2  . ASP   A  1  430 ? 3.932   -8.773  -20.254  1.00 80.64  ? 430  ASP   A OD2  1 
ATOM   6435  H  H    . ASP   A  1  430 ? 7.624   -8.991  -19.990  1.00 83.03  ? 430  ASP   A H    1 
ATOM   6436  H  HA   . ASP   A  1  430 ? 7.344   -8.694  -22.078  1.00 88.17  ? 430  ASP   A HA   1 
ATOM   6437  H  HB2  . ASP   A  1  430 ? 5.211   -7.008  -21.311  1.00 89.84  ? 430  ASP   A HB2  1 
ATOM   6438  H  HB3  . ASP   A  1  430 ? 5.331   -7.775  -22.698  1.00 89.84  ? 430  ASP   A HB3  1 
ATOM   6439  N  N    . ARG   A  1  431 ? 9.094   -6.738  -21.855  1.00 76.93  ? 431  ARG   A N    1 
ATOM   6440  C  CA   . ARG   A  1  431 ? 9.952   -5.602  -22.142  1.00 75.64  ? 431  ARG   A CA   1 
ATOM   6441  C  C    . ARG   A  1  431 ? 11.245  -6.088  -22.778  1.00 67.64  ? 431  ARG   A C    1 
ATOM   6442  O  O    . ARG   A  1  431 ? 11.742  -7.174  -22.467  1.00 63.96  ? 431  ARG   A O    1 
ATOM   6443  C  CB   . ARG   A  1  431 ? 10.276  -4.812  -20.867  1.00 83.29  ? 431  ARG   A CB   1 
ATOM   6444  C  CG   . ARG   A  1  431 ? 10.516  -3.329  -21.087  1.00 92.56  ? 431  ARG   A CG   1 
ATOM   6445  C  CD   . ARG   A  1  431 ? 9.223   -2.549  -20.936  1.00 100.35 ? 431  ARG   A CD   1 
ATOM   6446  N  NE   . ARG   A  1  431 ? 8.666   -2.692  -19.593  1.00 108.27 ? 431  ARG   A NE   1 
ATOM   6447  C  CZ   . ARG   A  1  431 ? 7.421   -2.369  -19.257  1.00 118.34 ? 431  ARG   A CZ   1 
ATOM   6448  N  NH1  . ARG   A  1  431 ? 6.588   -1.885  -20.167  1.00 121.82 ? 431  ARG   A NH1  1 
ATOM   6449  N  NH2  . ARG   A  1  431 ? 7.008   -2.538  -18.008  1.00 124.41 ? 431  ARG   A NH2  1 
ATOM   6450  H  H    . ARG   A  1  431 ? 9.520   -7.426  -21.563  1.00 92.36  ? 431  ARG   A H    1 
ATOM   6451  H  HA   . ARG   A  1  431 ? 9.507   -5.013  -22.771  1.00 90.80  ? 431  ARG   A HA   1 
ATOM   6452  H  HB2  . ARG   A  1  431 ? 9.532   -4.901  -20.252  1.00 99.98  ? 431  ARG   A HB2  1 
ATOM   6453  H  HB3  . ARG   A  1  431 ? 11.080  -5.183  -20.471  1.00 99.98  ? 431  ARG   A HB3  1 
ATOM   6454  H  HG2  . ARG   A  1  431 ? 11.152  -3.002  -20.431  1.00 111.10 ? 431  ARG   A HG2  1 
ATOM   6455  H  HG3  . ARG   A  1  431 ? 10.859  -3.185  -21.983  1.00 111.10 ? 431  ARG   A HG3  1 
ATOM   6456  H  HD2  . ARG   A  1  431 ? 9.395   -1.608  -21.096  1.00 120.45 ? 431  ARG   A HD2  1 
ATOM   6457  H  HD3  . ARG   A  1  431 ? 8.572   -2.880  -21.573  1.00 120.45 ? 431  ARG   A HD3  1 
ATOM   6458  H  HE   . ARG   A  1  431 ? 9.179   -3.006  -18.978  1.00 129.96 ? 431  ARG   A HE   1 
ATOM   6459  H  HH11 . ARG   A  1  431 ? 6.852   -1.777  -20.978  1.00 146.22 ? 431  ARG   A HH11 1 
ATOM   6460  H  HH12 . ARG   A  1  431 ? 5.783   -1.677  -19.946  1.00 146.22 ? 431  ARG   A HH12 1 
ATOM   6461  H  HH21 . ARG   A  1  431 ? 7.545   -2.856  -17.417  1.00 149.32 ? 431  ARG   A HH21 1 
ATOM   6462  H  HH22 . ARG   A  1  431 ? 6.203   -2.330  -17.790  1.00 149.32 ? 431  ARG   A HH22 1 
ATOM   6463  N  N    . ALA   A  1  432 ? 11.783  -5.266  -23.675  1.00 65.58  ? 432  ALA   A N    1 
ATOM   6464  C  CA   . ALA   A  1  432 ? 13.101  -5.483  -24.255  1.00 66.76  ? 432  ALA   A CA   1 
ATOM   6465  C  C    . ALA   A  1  432 ? 13.799  -4.136  -24.339  1.00 68.61  ? 432  ALA   A C    1 
ATOM   6466  O  O    . ALA   A  1  432 ? 13.194  -3.146  -24.765  1.00 71.38  ? 432  ALA   A O    1 
ATOM   6467  C  CB   . ALA   A  1  432 ? 13.018  -6.133  -25.639  1.00 68.06  ? 432  ALA   A CB   1 
ATOM   6468  H  H    . ALA   A  1  432 ? 11.393  -4.558  -23.970  1.00 78.73  ? 432  ALA   A H    1 
ATOM   6469  H  HA   . ALA   A  1  432 ? 13.619  -6.077  -23.689  1.00 80.15  ? 432  ALA   A HA   1 
ATOM   6470  H  HB1  . ALA   A  1  432 ? 13.916  -6.256  -25.985  1.00 81.71  ? 432  ALA   A HB1  1 
ATOM   6471  H  HB2  . ALA   A  1  432 ? 12.575  -6.992  -25.558  1.00 81.71  ? 432  ALA   A HB2  1 
ATOM   6472  H  HB3  . ALA   A  1  432 ? 12.513  -5.554  -26.230  1.00 81.71  ? 432  ALA   A HB3  1 
ATOM   6473  N  N    . ILE   A  1  433 ? 15.062  -4.100  -23.932  1.00 69.48  ? 433  ILE   A N    1 
ATOM   6474  C  CA   . ILE   A  1  433 ? 15.804  -2.857  -23.772  1.00 69.02  ? 433  ILE   A CA   1 
ATOM   6475  C  C    . ILE   A  1  433 ? 17.066  -2.918  -24.618  1.00 65.29  ? 433  ILE   A C    1 
ATOM   6476  O  O    . ILE   A  1  433 ? 17.728  -3.959  -24.689  1.00 65.73  ? 433  ILE   A O    1 
ATOM   6477  C  CB   . ILE   A  1  433 ? 16.149  -2.604  -22.289  1.00 71.34  ? 433  ILE   A CB   1 
ATOM   6478  C  CG1  . ILE   A  1  433 ? 14.878  -2.637  -21.435  1.00 75.77  ? 433  ILE   A CG1  1 
ATOM   6479  C  CG2  . ILE   A  1  433 ? 16.855  -1.271  -22.122  1.00 74.10  ? 433  ILE   A CG2  1 
ATOM   6480  C  CD1  . ILE   A  1  433 ? 14.693  -3.925  -20.663  1.00 81.84  ? 433  ILE   A CD1  1 
ATOM   6481  H  H    . ILE   A  1  433 ? 15.521  -4.801  -23.739  1.00 83.41  ? 433  ILE   A H    1 
ATOM   6482  H  HA   . ILE   A  1  433 ? 15.265  -2.119  -24.096  1.00 82.87  ? 433  ILE   A HA   1 
ATOM   6483  H  HB   . ILE   A  1  433 ? 16.745  -3.310  -21.993  1.00 85.65  ? 433  ILE   A HB   1 
ATOM   6484  H  HG12 . ILE   A  1  433 ? 14.915  -1.910  -20.794  1.00 90.96  ? 433  ILE   A HG12 1 
ATOM   6485  H  HG13 . ILE   A  1  433 ? 14.110  -2.527  -22.017  1.00 90.96  ? 433  ILE   A HG13 1 
ATOM   6486  H  HG21 . ILE   A  1  433 ? 17.032  -1.123  -21.180  1.00 88.96  ? 433  ILE   A HG21 1 
ATOM   6487  H  HG22 . ILE   A  1  433 ? 17.690  -1.293  -22.616  1.00 88.96  ? 433  ILE   A HG22 1 
ATOM   6488  H  HG23 . ILE   A  1  433 ? 16.285  -0.566  -22.467  1.00 88.96  ? 433  ILE   A HG23 1 
ATOM   6489  H  HD11 . ILE   A  1  433 ? 13.856  -3.882  -20.174  1.00 98.24  ? 433  ILE   A HD11 1 
ATOM   6490  H  HD12 . ILE   A  1  433 ? 14.675  -4.667  -21.287  1.00 98.24  ? 433  ILE   A HD12 1 
ATOM   6491  H  HD13 . ILE   A  1  433 ? 15.432  -4.031  -20.044  1.00 98.24  ? 433  ILE   A HD13 1 
ATOM   6492  N  N    . LEU   A  1  434 ? 17.395  -1.800  -25.260  1.00 63.98  ? 434  LEU   A N    1 
ATOM   6493  C  CA   . LEU   A  1  434 ? 18.622  -1.662  -26.034  1.00 66.00  ? 434  LEU   A CA   1 
ATOM   6494  C  C    . LEU   A  1  434 ? 19.564  -0.707  -25.316  1.00 65.74  ? 434  LEU   A C    1 
ATOM   6495  O  O    . LEU   A  1  434 ? 19.176  0.415   -24.971  1.00 70.15  ? 434  LEU   A O    1 
ATOM   6496  C  CB   . LEU   A  1  434 ? 18.338  -1.151  -27.449  1.00 69.09  ? 434  LEU   A CB   1 
ATOM   6497  C  CG   . LEU   A  1  434 ? 19.572  -0.793  -28.286  1.00 71.68  ? 434  LEU   A CG   1 
ATOM   6498  C  CD1  . LEU   A  1  434 ? 20.329  -2.044  -28.700  1.00 69.10  ? 434  LEU   A CD1  1 
ATOM   6499  C  CD2  . LEU   A  1  434 ? 19.190  0.032   -29.504  1.00 79.48  ? 434  LEU   A CD2  1 
ATOM   6500  H  H    . LEU   A  1  434 ? 16.909  -1.090  -25.261  1.00 76.81  ? 434  LEU   A H    1 
ATOM   6501  H  HA   . LEU   A  1  434 ? 19.050  -2.530  -26.107  1.00 79.24  ? 434  LEU   A HA   1 
ATOM   6502  H  HB2  . LEU   A  1  434 ? 17.854  -1.841  -27.930  1.00 82.94  ? 434  LEU   A HB2  1 
ATOM   6503  H  HB3  . LEU   A  1  434 ? 17.794  -0.351  -27.380  1.00 82.94  ? 434  LEU   A HB3  1 
ATOM   6504  H  HG   . LEU   A  1  434 ? 20.165  -0.252  -27.741  1.00 86.06  ? 434  LEU   A HG   1 
ATOM   6505  H  HD11 . LEU   A  1  434 ? 21.121  -1.785  -29.196  1.00 82.96  ? 434  LEU   A HD11 1 
ATOM   6506  H  HD12 . LEU   A  1  434 ? 20.584  -2.537  -27.904  1.00 82.96  ? 434  LEU   A HD12 1 
ATOM   6507  H  HD13 . LEU   A  1  434 ? 19.754  -2.592  -29.257  1.00 82.96  ? 434  LEU   A HD13 1 
ATOM   6508  H  HD21 . LEU   A  1  434 ? 19.996  0.277   -29.985  1.00 95.41  ? 434  LEU   A HD21 1 
ATOM   6509  H  HD22 . LEU   A  1  434 ? 18.611  -0.497  -30.075  1.00 95.41  ? 434  LEU   A HD22 1 
ATOM   6510  H  HD23 . LEU   A  1  434 ? 18.724  0.831   -29.211  1.00 95.41  ? 434  LEU   A HD23 1 
ATOM   6511  N  N    . TYR   A  1  435 ? 20.795  -1.155  -25.100  1.00 62.84  ? 435  TYR   A N    1 
ATOM   6512  C  CA   . TYR   A  1  435 ? 21.855  -0.340  -24.527  1.00 60.65  ? 435  TYR   A CA   1 
ATOM   6513  C  C    . TYR   A  1  435 ? 22.887  -0.052  -25.606  1.00 58.92  ? 435  TYR   A C    1 
ATOM   6514  O  O    . TYR   A  1  435 ? 23.406  -0.980  -26.236  1.00 56.35  ? 435  TYR   A O    1 
ATOM   6515  C  CB   . TYR   A  1  435 ? 22.520  -1.048  -23.347  1.00 61.92  ? 435  TYR   A CB   1 
ATOM   6516  C  CG   . TYR   A  1  435 ? 21.604  -1.299  -22.174  1.00 64.06  ? 435  TYR   A CG   1 
ATOM   6517  C  CD1  . TYR   A  1  435 ? 21.449  -0.348  -21.176  1.00 67.25  ? 435  TYR   A CD1  1 
ATOM   6518  C  CD2  . TYR   A  1  435 ? 20.901  -2.491  -22.060  1.00 63.43  ? 435  TYR   A CD2  1 
ATOM   6519  C  CE1  . TYR   A  1  435 ? 20.616  -0.573  -20.099  1.00 68.18  ? 435  TYR   A CE1  1 
ATOM   6520  C  CE2  . TYR   A  1  435 ? 20.065  -2.726  -20.986  1.00 65.84  ? 435  TYR   A CE2  1 
ATOM   6521  C  CZ   . TYR   A  1  435 ? 19.928  -1.764  -20.007  1.00 67.07  ? 435  TYR   A CZ   1 
ATOM   6522  O  OH   . TYR   A  1  435 ? 19.099  -1.989  -18.932  1.00 68.04  ? 435  TYR   A OH   1 
ATOM   6523  H  H    . TYR   A  1  435 ? 21.047  -1.957  -25.283  1.00 75.45  ? 435  TYR   A H    1 
ATOM   6524  H  HA   . TYR   A  1  435 ? 21.485  0.499   -24.208  1.00 72.82  ? 435  TYR   A HA   1 
ATOM   6525  H  HB2  . TYR   A  1  435 ? 22.853  -1.907  -23.649  1.00 74.34  ? 435  TYR   A HB2  1 
ATOM   6526  H  HB3  . TYR   A  1  435 ? 23.256  -0.499  -23.032  1.00 74.34  ? 435  TYR   A HB3  1 
ATOM   6527  H  HD1  . TYR   A  1  435 ? 21.914  0.455   -21.234  1.00 80.73  ? 435  TYR   A HD1  1 
ATOM   6528  H  HD2  . TYR   A  1  435 ? 20.994  -3.142  -22.718  1.00 76.15  ? 435  TYR   A HD2  1 
ATOM   6529  H  HE1  . TYR   A  1  435 ? 20.520  0.075   -19.439  1.00 81.86  ? 435  TYR   A HE1  1 
ATOM   6530  H  HE2  . TYR   A  1  435 ? 19.598  -3.528  -20.923  1.00 79.04  ? 435  TYR   A HE2  1 
ATOM   6531  H  HH   . TYR   A  1  435 ? 19.020  -2.814  -18.799  1.00 81.68  ? 435  TYR   A HH   1 
ATOM   6532  N  N    . ARG   A  1  436 ? 23.182  1.224   -25.818  1.00 64.01  ? 436  ARG   A N    1 
ATOM   6533  C  CA   . ARG   A  1  436 ? 24.149  1.640   -26.822  1.00 70.37  ? 436  ARG   A CA   1 
ATOM   6534  C  C    . ARG   A  1  436 ? 25.500  1.899   -26.170  1.00 68.01  ? 436  ARG   A C    1 
ATOM   6535  O  O    . ARG   A  1  436 ? 25.576  2.428   -25.057  1.00 67.84  ? 436  ARG   A O    1 
ATOM   6536  C  CB   . ARG   A  1  436 ? 23.663  2.890   -27.552  1.00 79.66  ? 436  ARG   A CB   1 
ATOM   6537  C  CG   . ARG   A  1  436 ? 22.314  2.699   -28.216  1.00 86.13  ? 436  ARG   A CG   1 
ATOM   6538  C  CD   . ARG   A  1  436 ? 22.046  3.797   -29.210  1.00 89.58  ? 436  ARG   A CD   1 
ATOM   6539  N  NE   . ARG   A  1  436 ? 21.853  5.087   -28.557  1.00 92.67  ? 436  ARG   A NE   1 
ATOM   6540  C  CZ   . ARG   A  1  436 ? 22.051  6.258   -29.152  1.00 100.31 ? 436  ARG   A CZ   1 
ATOM   6541  N  NH1  . ARG   A  1  436 ? 22.464  6.300   -30.411  1.00 106.34 ? 436  ARG   A NH1  1 
ATOM   6542  N  NH2  . ARG   A  1  436 ? 21.848  7.387   -28.485  1.00 103.99 ? 436  ARG   A NH2  1 
ATOM   6543  H  H    . ARG   A  1  436 ? 22.828  1.878   -25.385  1.00 76.85  ? 436  ARG   A H    1 
ATOM   6544  H  HA   . ARG   A  1  436 ? 24.265  0.935   -27.477  1.00 84.48  ? 436  ARG   A HA   1 
ATOM   6545  H  HB2  . ARG   A  1  436 ? 23.583  3.616   -26.915  1.00 95.63  ? 436  ARG   A HB2  1 
ATOM   6546  H  HB3  . ARG   A  1  436 ? 24.305  3.122   -28.241  1.00 95.63  ? 436  ARG   A HB3  1 
ATOM   6547  H  HG2  . ARG   A  1  436 ? 22.300  1.850   -28.684  1.00 103.39 ? 436  ARG   A HG2  1 
ATOM   6548  H  HG3  . ARG   A  1  436 ? 21.616  2.718   -27.542  1.00 103.39 ? 436  ARG   A HG3  1 
ATOM   6549  H  HD2  . ARG   A  1  436 ? 22.801  3.873   -29.814  1.00 107.54 ? 436  ARG   A HD2  1 
ATOM   6550  H  HD3  . ARG   A  1  436 ? 21.241  3.587   -29.709  1.00 107.54 ? 436  ARG   A HD3  1 
ATOM   6551  H  HE   . ARG   A  1  436 ? 21.594  5.090   -27.737  1.00 111.25 ? 436  ARG   A HE   1 
ATOM   6552  H  HH11 . ARG   A  1  436 ? 22.603  5.569   -30.843  1.00 127.65 ? 436  ARG   A HH11 1 
ATOM   6553  H  HH12 . ARG   A  1  436 ? 22.593  7.058   -30.797  1.00 127.65 ? 436  ARG   A HH12 1 
ATOM   6554  H  HH21 . ARG   A  1  436 ? 21.587  7.361   -27.666  1.00 124.83 ? 436  ARG   A HH21 1 
ATOM   6555  H  HH22 . ARG   A  1  436 ? 21.977  8.144   -28.872  1.00 124.83 ? 436  ARG   A HH22 1 
ATOM   6556  N  N    . ALA   A  1  437 ? 26.564  1.518   -26.871  1.00 65.86  ? 437  ALA   A N    1 
ATOM   6557  C  CA   . ALA   A  1  437 ? 27.916  1.607   -26.339  1.00 66.68  ? 437  ALA   A CA   1 
ATOM   6558  C  C    . ALA   A  1  437 ? 28.490  2.996   -26.579  1.00 68.77  ? 437  ALA   A C    1 
ATOM   6559  O  O    . ALA   A  1  437 ? 28.523  3.476   -27.718  1.00 69.54  ? 437  ALA   A O    1 
ATOM   6560  C  CB   . ALA   A  1  437 ? 28.815  0.550   -26.978  1.00 65.67  ? 437  ALA   A CB   1 
ATOM   6561  H  H    . ALA   A  1  437 ? 26.527  1.201   -27.670  1.00 79.07  ? 437  ALA   A H    1 
ATOM   6562  H  HA   . ALA   A  1  437 ? 27.889  1.454   -25.381  1.00 80.05  ? 437  ALA   A HA   1 
ATOM   6563  H  HB1  . ALA   A  1  437 ? 29.713  0.641   -26.622  1.00 78.84  ? 437  ALA   A HB1  1 
ATOM   6564  H  HB2  . ALA   A  1  437 ? 28.465  -0.331  -26.769  1.00 78.84  ? 437  ALA   A HB2  1 
ATOM   6565  H  HB3  . ALA   A  1  437 ? 28.825  0.682   -27.939  1.00 78.84  ? 437  ALA   A HB3  1 
ATOM   6566  N  N    . ARG   A  1  438 ? 28.942  3.635   -25.505  1.00 68.47  ? 438  ARG   A N    1 
ATOM   6567  C  CA   . ARG   A  1  438 ? 29.578  4.937   -25.603  1.00 70.94  ? 438  ARG   A CA   1 
ATOM   6568  C  C    . ARG   A  1  438 ? 31.005  4.791   -26.126  1.00 72.55  ? 438  ARG   A C    1 
ATOM   6569  O  O    . ARG   A  1  438 ? 31.682  3.801   -25.837  1.00 73.35  ? 438  ARG   A O    1 
ATOM   6570  C  CB   . ARG   A  1  438 ? 29.601  5.620   -24.239  1.00 70.83  ? 438  ARG   A CB   1 
ATOM   6571  C  CG   . ARG   A  1  438 ? 28.223  5.916   -23.668  1.00 71.07  ? 438  ARG   A CG   1 
ATOM   6572  C  CD   . ARG   A  1  438 ? 28.264  6.151   -22.161  1.00 71.06  ? 438  ARG   A CD   1 
ATOM   6573  N  NE   . ARG   A  1  438 ? 28.954  7.386   -21.792  1.00 73.67  ? 438  ARG   A NE   1 
ATOM   6574  C  CZ   . ARG   A  1  438 ? 29.072  7.832   -20.544  1.00 75.22  ? 438  ARG   A CZ   1 
ATOM   6575  N  NH1  . ARG   A  1  438 ? 28.547  7.147   -19.537  1.00 73.07  ? 438  ARG   A NH1  1 
ATOM   6576  N  NH2  . ARG   A  1  438 ? 29.716  8.966   -20.301  1.00 79.79  ? 438  ARG   A NH2  1 
ATOM   6577  H  H    . ARG   A  1  438 ? 28.892  3.330   -24.702  1.00 82.20  ? 438  ARG   A H    1 
ATOM   6578  H  HA   . ARG   A  1  438 ? 29.079  5.499   -26.216  1.00 85.17  ? 438  ARG   A HA   1 
ATOM   6579  H  HB2  . ARG   A  1  438 ? 30.063  5.042   -23.610  1.00 85.04  ? 438  ARG   A HB2  1 
ATOM   6580  H  HB3  . ARG   A  1  438 ? 30.073  6.463   -24.322  1.00 85.04  ? 438  ARG   A HB3  1 
ATOM   6581  H  HG2  . ARG   A  1  438 ? 27.868  6.715   -24.089  1.00 85.33  ? 438  ARG   A HG2  1 
ATOM   6582  H  HG3  . ARG   A  1  438 ? 27.637  5.162   -23.840  1.00 85.33  ? 438  ARG   A HG3  1 
ATOM   6583  H  HD2  . ARG   A  1  438 ? 27.356  6.205   -21.825  1.00 85.31  ? 438  ARG   A HD2  1 
ATOM   6584  H  HD3  . ARG   A  1  438 ? 28.730  5.412   -21.739  1.00 85.31  ? 438  ARG   A HD3  1 
ATOM   6585  H  HE   . ARG   A  1  438 ? 29.306  7.853   -22.422  1.00 88.44  ? 438  ARG   A HE   1 
ATOM   6586  H  HH11 . ARG   A  1  438 ? 28.128  6.412   -19.688  1.00 87.72  ? 438  ARG   A HH11 1 
ATOM   6587  H  HH12 . ARG   A  1  438 ? 28.626  7.439   -18.731  1.00 87.72  ? 438  ARG   A HH12 1 
ATOM   6588  H  HH21 . ARG   A  1  438 ? 30.058  9.414   -20.951  1.00 95.79  ? 438  ARG   A HH21 1 
ATOM   6589  H  HH22 . ARG   A  1  438 ? 29.792  9.253   -19.494  1.00 95.79  ? 438  ARG   A HH22 1 
ATOM   6590  N  N    . PRO   A  1  439 ? 31.488  5.761   -26.897  1.00 72.57  ? 439  PRO   A N    1 
ATOM   6591  C  CA   . PRO   A  1  439 ? 32.884  5.706   -27.342  1.00 73.36  ? 439  PRO   A CA   1 
ATOM   6592  C  C    . PRO   A  1  439 ? 33.835  5.937   -26.180  1.00 74.82  ? 439  PRO   A C    1 
ATOM   6593  O  O    . PRO   A  1  439 ? 33.497  6.584   -25.186  1.00 75.84  ? 439  PRO   A O    1 
ATOM   6594  C  CB   . PRO   A  1  439 ? 32.973  6.829   -28.381  1.00 73.18  ? 439  PRO   A CB   1 
ATOM   6595  C  CG   . PRO   A  1  439 ? 31.890  7.775   -28.000  1.00 72.80  ? 439  PRO   A CG   1 
ATOM   6596  C  CD   . PRO   A  1  439 ? 30.788  6.949   -27.416  1.00 71.85  ? 439  PRO   A CD   1 
ATOM   6597  H  HA   . PRO   A  1  439 ? 33.087  4.860   -27.770  1.00 88.07  ? 439  PRO   A HA   1 
ATOM   6598  H  HB2  . PRO   A  1  439 ? 33.842  7.256   -28.334  1.00 87.85  ? 439  PRO   A HB2  1 
ATOM   6599  H  HB3  . PRO   A  1  439 ? 32.826  6.470   -29.270  1.00 87.85  ? 439  PRO   A HB3  1 
ATOM   6600  H  HG2  . PRO   A  1  439 ? 32.227  8.407   -27.345  1.00 87.40  ? 439  PRO   A HG2  1 
ATOM   6601  H  HG3  . PRO   A  1  439 ? 31.581  8.248   -28.788  1.00 87.40  ? 439  PRO   A HG3  1 
ATOM   6602  H  HD2  . PRO   A  1  439 ? 30.342  7.427   -26.699  1.00 86.25  ? 439  PRO   A HD2  1 
ATOM   6603  H  HD3  . PRO   A  1  439 ? 30.145  6.700   -28.098  1.00 86.25  ? 439  PRO   A HD3  1 
ATOM   6604  N  N    . VAL   A  1  440 ? 35.042  5.394   -26.315  1.00 76.05  ? 440  VAL   A N    1 
ATOM   6605  C  CA   . VAL   A  1  440 ? 36.000  5.315   -25.219  1.00 75.57  ? 440  VAL   A CA   1 
ATOM   6606  C  C    . VAL   A  1  440 ? 37.179  6.227   -25.519  1.00 78.51  ? 440  VAL   A C    1 
ATOM   6607  O  O    . VAL   A  1  440 ? 37.817  6.109   -26.572  1.00 80.20  ? 440  VAL   A O    1 
ATOM   6608  C  CB   . VAL   A  1  440 ? 36.467  3.866   -24.991  1.00 73.98  ? 440  VAL   A CB   1 
ATOM   6609  C  CG1  . VAL   A  1  440 ? 37.488  3.805   -23.861  1.00 73.24  ? 440  VAL   A CG1  1 
ATOM   6610  C  CG2  . VAL   A  1  440 ? 35.273  2.973   -24.687  1.00 72.02  ? 440  VAL   A CG2  1 
ATOM   6611  H  H    . VAL   A  1  440 ? 35.334  5.057   -27.051  1.00 91.29  ? 440  VAL   A H    1 
ATOM   6612  H  HA   . VAL   A  1  440 ? 35.576  5.637   -24.409  1.00 90.72  ? 440  VAL   A HA   1 
ATOM   6613  H  HB   . VAL   A  1  440 ? 36.896  3.540   -25.797  1.00 88.81  ? 440  VAL   A HB   1 
ATOM   6614  H  HG11 . VAL   A  1  440 ? 37.726  2.879   -23.700  1.00 87.93  ? 440  VAL   A HG11 1 
ATOM   6615  H  HG12 . VAL   A  1  440 ? 38.275  4.310   -24.119  1.00 87.93  ? 440  VAL   A HG12 1 
ATOM   6616  H  HG13 . VAL   A  1  440 ? 37.097  4.190   -23.061  1.00 87.93  ? 440  VAL   A HG13 1 
ATOM   6617  H  HG21 . VAL   A  1  440 ? 35.587  2.069   -24.528  1.00 86.46  ? 440  VAL   A HG21 1 
ATOM   6618  H  HG22 . VAL   A  1  440 ? 34.820  3.309   -23.897  1.00 86.46  ? 440  VAL   A HG22 1 
ATOM   6619  H  HG23 . VAL   A  1  440 ? 34.668  2.985   -25.445  1.00 86.46  ? 440  VAL   A HG23 1 
ATOM   6620  N  N    . ILE   A  1  441 ? 37.470  7.128   -24.584  1.00 80.20  ? 441  ILE   A N    1 
ATOM   6621  C  CA   . ILE   A  1  441 ? 38.619  8.020   -24.661  1.00 83.68  ? 441  ILE   A CA   1 
ATOM   6622  C  C    . ILE   A  1  441 ? 39.740  7.414   -23.828  1.00 84.19  ? 441  ILE   A C    1 
ATOM   6623  O  O    . ILE   A  1  441 ? 39.575  7.190   -22.622  1.00 79.79  ? 441  ILE   A O    1 
ATOM   6624  C  CB   . ILE   A  1  441 ? 38.274  9.429   -24.153  1.00 86.01  ? 441  ILE   A CB   1 
ATOM   6625  C  CG1  . ILE   A  1  441 ? 37.134  10.043  -24.967  1.00 86.14  ? 441  ILE   A CG1  1 
ATOM   6626  C  CG2  . ILE   A  1  441 ? 39.502  10.332  -24.206  1.00 90.37  ? 441  ILE   A CG2  1 
ATOM   6627  C  CD1  . ILE   A  1  441 ? 36.443  11.182  -24.249  1.00 86.35  ? 441  ILE   A CD1  1 
ATOM   6628  H  H    . ILE   A  1  441 ? 36.999  7.244   -23.874  1.00 96.27  ? 441  ILE   A H    1 
ATOM   6629  H  HA   . ILE   A  1  441 ? 38.911  8.086   -25.584  1.00 100.45 ? 441  ILE   A HA   1 
ATOM   6630  H  HB   . ILE   A  1  441 ? 37.980  9.347   -23.232  1.00 103.25 ? 441  ILE   A HB   1 
ATOM   6631  H  HG12 . ILE   A  1  441 ? 37.492  10.387  -25.800  1.00 103.41 ? 441  ILE   A HG12 1 
ATOM   6632  H  HG13 . ILE   A  1  441 ? 36.472  9.357   -25.148  1.00 103.41 ? 441  ILE   A HG13 1 
ATOM   6633  H  HG21 . ILE   A  1  441 ? 39.250  11.224  -23.920  1.00 108.48 ? 441  ILE   A HG21 1 
ATOM   6634  H  HG22 . ILE   A  1  441 ? 40.182  9.975   -23.614  1.00 108.48 ? 441  ILE   A HG22 1 
ATOM   6635  H  HG23 . ILE   A  1  441 ? 39.836  10.359  -25.116  1.00 108.48 ? 441  ILE   A HG23 1 
ATOM   6636  H  HD11 . ILE   A  1  441 ? 35.774  11.566  -24.837  1.00 103.66 ? 441  ILE   A HD11 1 
ATOM   6637  H  HD12 . ILE   A  1  441 ? 36.021  10.839  -23.446  1.00 103.66 ? 441  ILE   A HD12 1 
ATOM   6638  H  HD13 . ILE   A  1  441 ? 37.103  11.854  -24.016  1.00 103.66 ? 441  ILE   A HD13 1 
ATOM   6639  N  N    . THR   A  1  442 ? 40.876  7.150   -24.461  1.00 85.87  ? 442  THR   A N    1 
ATOM   6640  C  CA   . THR   A  1  442 ? 42.086  6.754   -23.754  1.00 89.44  ? 442  THR   A CA   1 
ATOM   6641  C  C    . THR   A  1  442 ? 42.955  7.986   -23.537  1.00 93.84  ? 442  THR   A C    1 
ATOM   6642  O  O    . THR   A  1  442 ? 43.048  8.854   -24.410  1.00 100.55 ? 442  THR   A O    1 
ATOM   6643  C  CB   . THR   A  1  442 ? 42.858  5.686   -24.529  1.00 91.66  ? 442  THR   A CB   1 
ATOM   6644  O  OG1  . THR   A  1  442 ? 42.081  4.481   -24.583  1.00 89.55  ? 442  THR   A OG1  1 
ATOM   6645  C  CG2  . THR   A  1  442 ? 44.198  5.394   -23.859  1.00 92.10  ? 442  THR   A CG2  1 
ATOM   6646  H  H    . THR   A  1  442 ? 40.973  7.194   -25.314  1.00 103.08 ? 442  THR   A H    1 
ATOM   6647  H  HA   . THR   A  1  442 ? 41.858  6.374   -22.891  1.00 107.36 ? 442  THR   A HA   1 
ATOM   6648  H  HB   . THR   A  1  442 ? 43.032  6.002   -25.429  1.00 110.03 ? 442  THR   A HB   1 
ATOM   6649  H  HG1  . THR   A  1  442 ? 42.505  3.884   -24.995  1.00 107.49 ? 442  THR   A HG1  1 
ATOM   6650  H  HG21 . THR   A  1  442 ? 44.651  4.673   -24.324  1.00 110.56 ? 442  THR   A HG21 1 
ATOM   6651  H  HG22 . THR   A  1  442 ? 44.759  6.185   -23.881  1.00 110.56 ? 442  THR   A HG22 1 
ATOM   6652  H  HG23 . THR   A  1  442 ? 44.057  5.133   -22.935  1.00 110.56 ? 442  THR   A HG23 1 
ATOM   6653  N  N    . VAL   A  1  443 ? 43.590  8.058   -22.369  1.00 90.67  ? 443  VAL   A N    1 
ATOM   6654  C  CA   . VAL   A  1  443 ? 44.306  9.252   -21.935  1.00 93.00  ? 443  VAL   A CA   1 
ATOM   6655  C  C    . VAL   A  1  443 ? 45.689  8.852   -21.439  1.00 93.31  ? 443  VAL   A C    1 
ATOM   6656  O  O    . VAL   A  1  443 ? 45.825  7.907   -20.654  1.00 94.70  ? 443  VAL   A O    1 
ATOM   6657  C  CB   . VAL   A  1  443 ? 43.527  10.001  -20.836  1.00 93.83  ? 443  VAL   A CB   1 
ATOM   6658  C  CG1  . VAL   A  1  443 ? 44.273  11.254  -20.399  1.00 96.61  ? 443  VAL   A CG1  1 
ATOM   6659  C  CG2  . VAL   A  1  443 ? 42.125  10.356  -21.326  1.00 94.67  ? 443  VAL   A CG2  1 
ATOM   6660  H  H    . VAL   A  1  443 ? 43.620  7.413   -21.800  1.00 108.84 ? 443  VAL   A H    1 
ATOM   6661  H  HA   . VAL   A  1  443 ? 44.428  9.844   -22.693  1.00 111.63 ? 443  VAL   A HA   1 
ATOM   6662  H  HB   . VAL   A  1  443 ? 43.443  9.420   -20.063  1.00 112.63 ? 443  VAL   A HB   1 
ATOM   6663  H  HG11 . VAL   A  1  443 ? 43.744  11.721  -19.734  1.00 115.96 ? 443  VAL   A HG11 1 
ATOM   6664  H  HG12 . VAL   A  1  443 ? 45.128  10.996  -20.021  1.00 115.96 ? 443  VAL   A HG12 1 
ATOM   6665  H  HG13 . VAL   A  1  443 ? 44.411  11.824  -21.172  1.00 115.96 ? 443  VAL   A HG13 1 
ATOM   6666  H  HG21 . VAL   A  1  443 ? 41.655  10.830  -20.622  1.00 113.64 ? 443  VAL   A HG21 1 
ATOM   6667  H  HG22 . VAL   A  1  443 ? 42.199  10.919  -22.112  1.00 113.64 ? 443  VAL   A HG22 1 
ATOM   6668  H  HG23 . VAL   A  1  443 ? 41.652  9.539   -21.548  1.00 113.64 ? 443  VAL   A HG23 1 
ATOM   6669  N  N    . ASN   A  1  444 ? 46.713  9.574   -21.900  1.00 93.25  ? 444  ASN   A N    1 
ATOM   6670  C  CA   . ASN   A  1  444 ? 48.087  9.422   -21.430  1.00 93.23  ? 444  ASN   A CA   1 
ATOM   6671  C  C    . ASN   A  1  444 ? 48.429  10.656  -20.603  1.00 92.43  ? 444  ASN   A C    1 
ATOM   6672  O  O    . ASN   A  1  444 ? 48.542  11.758  -21.150  1.00 93.91  ? 444  ASN   A O    1 
ATOM   6673  C  CB   . ASN   A  1  444 ? 49.067  9.278   -22.593  1.00 97.84  ? 444  ASN   A CB   1 
ATOM   6674  C  CG   . ASN   A  1  444 ? 48.883  7.990   -23.367  1.00 101.65 ? 444  ASN   A CG   1 
ATOM   6675  O  OD1  . ASN   A  1  444 ? 47.762  7.533   -23.589  1.00 103.21 ? 444  ASN   A OD1  1 
ATOM   6676  N  ND2  . ASN   A  1  444 ? 49.995  7.398   -23.791  1.00 101.90 ? 444  ASN   A ND2  1 
ATOM   6677  H  H    . ASN   A  1  444 ? 46.630  10.178  -22.506  1.00 111.93 ? 444  ASN   A H    1 
ATOM   6678  H  HA   . ASN   A  1  444 ? 48.149  8.627   -20.878  1.00 111.91 ? 444  ASN   A HA   1 
ATOM   6679  H  HB2  . ASN   A  1  444 ? 48.936  10.017  -23.208  1.00 117.44 ? 444  ASN   A HB2  1 
ATOM   6680  H  HB3  . ASN   A  1  444 ? 49.972  9.291   -22.246  1.00 117.44 ? 444  ASN   A HB3  1 
ATOM   6681  H  HD21 . ASN   A  1  444 ? 49.949  6.664   -24.235  1.00 122.31 ? 444  ASN   A HD21 1 
ATOM   6682  H  HD22 . ASN   A  1  444 ? 50.761  7.749   -23.620  1.00 122.31 ? 444  ASN   A HD22 1 
ATOM   6683  N  N    . ALA   A  1  445 ? 48.605  10.477  -19.297  1.00 90.01  ? 445  ALA   A N    1 
ATOM   6684  C  CA   . ALA   A  1  445 ? 48.872  11.583  -18.389  1.00 87.96  ? 445  ALA   A CA   1 
ATOM   6685  C  C    . ALA   A  1  445 ? 50.280  11.477  -17.819  1.00 88.42  ? 445  ALA   A C    1 
ATOM   6686  O  O    . ALA   A  1  445 ? 50.740  10.385  -17.471  1.00 89.09  ? 445  ALA   A O    1 
ATOM   6687  C  CB   . ALA   A  1  445 ? 47.851  11.613  -17.248  1.00 85.30  ? 445  ALA   A CB   1 
ATOM   6688  H  H    . ALA   A  1  445 ? 48.573  9.710   -18.909  1.00 108.05 ? 445  ALA   A H    1 
ATOM   6689  H  HA   . ALA   A  1  445 ? 48.811  12.418  -18.879  1.00 105.59 ? 445  ALA   A HA   1 
ATOM   6690  H  HB1  . ALA   A  1  445 ? 48.036  12.376  -16.679  1.00 102.40 ? 445  ALA   A HB1  1 
ATOM   6691  H  HB2  . ALA   A  1  445 ? 46.960  11.688  -17.624  1.00 102.40 ? 445  ALA   A HB2  1 
ATOM   6692  H  HB3  . ALA   A  1  445 ? 47.925  10.792  -16.736  1.00 102.40 ? 445  ALA   A HB3  1 
ATOM   6693  N  N    . GLY   A  1  446 ? 50.954  12.618  -17.721  1.00 88.47  ? 446  GLY   A N    1 
ATOM   6694  C  CA   . GLY   A  1  446 ? 52.300  12.662  -17.187  1.00 87.05  ? 446  GLY   A CA   1 
ATOM   6695  C  C    . GLY   A  1  446 ? 52.427  13.703  -16.095  1.00 87.72  ? 446  GLY   A C    1 
ATOM   6696  O  O    . GLY   A  1  446 ? 51.752  14.732  -16.103  1.00 89.39  ? 446  GLY   A O    1 
ATOM   6697  H  H    . GLY   A  1  446 ? 50.647  13.384  -17.961  1.00 106.20 ? 446  GLY   A H    1 
ATOM   6698  H  HA2  . GLY   A  1  446 ? 52.532  11.796  -16.818  1.00 104.49 ? 446  GLY   A HA2  1 
ATOM   6699  H  HA3  . GLY   A  1  446 ? 52.924  12.881  -17.897  1.00 104.49 ? 446  GLY   A HA3  1 
ATOM   6700  N  N    . LEU   A  1  447 ? 53.315  13.416  -15.144  1.00 86.07  ? 447  LEU   A N    1 
ATOM   6701  C  CA   . LEU   A  1  447 ? 53.578  14.304  -14.016  1.00 89.65  ? 447  LEU   A CA   1 
ATOM   6702  C  C    . LEU   A  1  447 ? 55.065  14.241  -13.700  1.00 98.33  ? 447  LEU   A C    1 
ATOM   6703  O  O    . LEU   A  1  447 ? 55.591  13.163  -13.408  1.00 99.78  ? 447  LEU   A O    1 
ATOM   6704  C  CB   . LEU   A  1  447 ? 52.744  13.906  -12.793  1.00 86.78  ? 447  LEU   A CB   1 
ATOM   6705  C  CG   . LEU   A  1  447 ? 52.886  14.779  -11.542  1.00 86.78  ? 447  LEU   A CG   1 
ATOM   6706  C  CD1  . LEU   A  1  447 ? 52.328  16.173  -11.784  1.00 88.10  ? 447  LEU   A CD1  1 
ATOM   6707  C  CD2  . LEU   A  1  447 ? 52.200  14.129  -10.347  1.00 85.53  ? 447  LEU   A CD2  1 
ATOM   6708  H  H    . LEU   A  1  447 ? 53.787  12.697  -15.131  1.00 103.32 ? 447  LEU   A H    1 
ATOM   6709  H  HA   . LEU   A  1  447 ? 53.351  15.216  -14.254  1.00 107.62 ? 447  LEU   A HA   1 
ATOM   6710  H  HB2  . LEU   A  1  447 ? 51.809  13.929  -13.049  1.00 104.17 ? 447  LEU   A HB2  1 
ATOM   6711  H  HB3  . LEU   A  1  447 ? 52.997  13.005  -12.539  1.00 104.17 ? 447  LEU   A HB3  1 
ATOM   6712  H  HG   . LEU   A  1  447 ? 53.830  14.868  -11.335  1.00 104.17 ? 447  LEU   A HG   1 
ATOM   6713  H  HD11 . LEU   A  1  447 ? 52.396  16.687  -10.964  1.00 105.75 ? 447  LEU   A HD11 1 
ATOM   6714  H  HD12 . LEU   A  1  447 ? 52.842  16.601  -12.486  1.00 105.75 ? 447  LEU   A HD12 1 
ATOM   6715  H  HD13 . LEU   A  1  447 ? 51.399  16.099  -12.052  1.00 105.75 ? 447  LEU   A HD13 1 
ATOM   6716  H  HD21 . LEU   A  1  447 ? 52.308  14.701  -9.572   1.00 102.67 ? 447  LEU   A HD21 1 
ATOM   6717  H  HD22 . LEU   A  1  447 ? 51.258  14.017  -10.547  1.00 102.67 ? 447  LEU   A HD22 1 
ATOM   6718  H  HD23 . LEU   A  1  447 ? 52.608  13.265  -10.180  1.00 102.67 ? 447  LEU   A HD23 1 
ATOM   6719  N  N    . GLU   A  1  448 ? 55.738  15.388  -13.767  1.00 103.92 ? 448  GLU   A N    1 
ATOM   6720  C  CA   . GLU   A  1  448 ? 57.171  15.486  -13.516  1.00 109.01 ? 448  GLU   A CA   1 
ATOM   6721  C  C    . GLU   A  1  448 ? 57.414  16.493  -12.400  1.00 106.98 ? 448  GLU   A C    1 
ATOM   6722  O  O    . GLU   A  1  448 ? 56.877  17.606  -12.437  1.00 108.29 ? 448  GLU   A O    1 
ATOM   6723  C  CB   . GLU   A  1  448 ? 57.926  15.908  -14.782  1.00 117.35 ? 448  GLU   A CB   1 
ATOM   6724  C  CG   . GLU   A  1  448 ? 57.690  15.008  -15.988  1.00 122.10 ? 448  GLU   A CG   1 
ATOM   6725  C  CD   . GLU   A  1  448 ? 58.354  15.536  -17.247  1.00 135.53 ? 448  GLU   A CD   1 
ATOM   6726  O  OE1  . GLU   A  1  448 ? 59.069  16.556  -17.159  1.00 140.73 ? 448  GLU   A OE1  1 
ATOM   6727  O  OE2  . GLU   A  1  448 ? 58.158  14.933  -18.323  1.00 138.66 ? 448  GLU   A OE2  1 
ATOM   6728  H  H    . GLU   A  1  448 ? 55.375  16.143  -13.963  1.00 124.74 ? 448  GLU   A H    1 
ATOM   6729  H  HA   . GLU   A  1  448 ? 57.510  14.623  -13.231  1.00 130.85 ? 448  GLU   A HA   1 
ATOM   6730  H  HB2  . GLU   A  1  448 ? 57.645  16.804  -15.025  1.00 140.85 ? 448  GLU   A HB2  1 
ATOM   6731  H  HB3  . GLU   A  1  448 ? 58.877  15.898  -14.591  1.00 140.85 ? 448  GLU   A HB3  1 
ATOM   6732  H  HG2  . GLU   A  1  448 ? 58.053  14.127  -15.803  1.00 146.55 ? 448  GLU   A HG2  1 
ATOM   6733  H  HG3  . GLU   A  1  448 ? 56.736  14.945  -16.155  1.00 146.55 ? 448  GLU   A HG3  1 
ATOM   6734  N  N    . VAL   A  1  449 ? 58.222  16.105  -11.417  1.00 101.10 ? 449  VAL   A N    1 
ATOM   6735  C  CA   . VAL   A  1  449 ? 58.550  16.947  -10.270  1.00 97.12  ? 449  VAL   A CA   1 
ATOM   6736  C  C    . VAL   A  1  449 ? 60.063  17.126  -10.263  1.00 95.88  ? 449  VAL   A C    1 
ATOM   6737  O  O    . VAL   A  1  449 ? 60.801  16.203  -9.896   1.00 96.17  ? 449  VAL   A O    1 
ATOM   6738  C  CB   . VAL   A  1  449 ? 58.059  16.338  -8.947   1.00 92.23  ? 449  VAL   A CB   1 
ATOM   6739  C  CG1  . VAL   A  1  449 ? 58.503  17.191  -7.761   1.00 92.06  ? 449  VAL   A CG1  1 
ATOM   6740  C  CG2  . VAL   A  1  449 ? 56.544  16.183  -8.960   1.00 89.35  ? 449  VAL   A CG2  1 
ATOM   6741  H  H    . VAL   A  1  449 ? 58.603  15.334  -11.391  1.00 121.36 ? 449  VAL   A H    1 
ATOM   6742  H  HA   . VAL   A  1  449 ? 58.135  17.817  -10.377  1.00 116.59 ? 449  VAL   A HA   1 
ATOM   6743  H  HB   . VAL   A  1  449 ? 58.452  15.457  -8.846   1.00 110.71 ? 449  VAL   A HB   1 
ATOM   6744  H  HG11 . VAL   A  1  449 ? 58.148  16.806  -6.945   1.00 110.51 ? 449  VAL   A HG11 1 
ATOM   6745  H  HG12 . VAL   A  1  449 ? 59.473  17.203  -7.726   1.00 110.51 ? 449  VAL   A HG12 1 
ATOM   6746  H  HG13 . VAL   A  1  449 ? 58.165  18.093  -7.877   1.00 110.51 ? 449  VAL   A HG13 1 
ATOM   6747  H  HG21 . VAL   A  1  449 ? 56.258  15.801  -8.115   1.00 107.26 ? 449  VAL   A HG21 1 
ATOM   6748  H  HG22 . VAL   A  1  449 ? 56.138  17.056  -9.082   1.00 107.26 ? 449  VAL   A HG22 1 
ATOM   6749  H  HG23 . VAL   A  1  449 ? 56.292  15.596  -9.690   1.00 107.26 ? 449  VAL   A HG23 1 
ATOM   6750  N  N    . TYR   A  1  450 ? 60.531  18.309  -10.663  1.00 96.25  ? 450  TYR   A N    1 
ATOM   6751  C  CA   . TYR   A  1  450 ? 61.959  18.604  -10.675  1.00 96.27  ? 450  TYR   A CA   1 
ATOM   6752  C  C    . TYR   A  1  450 ? 62.215  19.924  -9.957   1.00 97.07  ? 450  TYR   A C    1 
ATOM   6753  O  O    . TYR   A  1  450 ? 61.535  20.925  -10.243  1.00 97.13  ? 450  TYR   A O    1 
ATOM   6754  C  CB   . TYR   A  1  450 ? 62.509  18.659  -12.112  1.00 97.52  ? 450  TYR   A CB   1 
ATOM   6755  C  CG   . TYR   A  1  450 ? 61.745  19.548  -13.074  1.00 103.71 ? 450  TYR   A CG   1 
ATOM   6756  C  CD1  . TYR   A  1  450 ? 60.516  19.155  -13.587  1.00 103.62 ? 450  TYR   A CD1  1 
ATOM   6757  C  CD2  . TYR   A  1  450 ? 62.269  20.765  -13.493  1.00 110.05 ? 450  TYR   A CD2  1 
ATOM   6758  C  CE1  . TYR   A  1  450 ? 59.821  19.956  -14.474  1.00 106.64 ? 450  TYR   A CE1  1 
ATOM   6759  C  CE2  . TYR   A  1  450 ? 61.580  21.572  -14.383  1.00 111.81 ? 450  TYR   A CE2  1 
ATOM   6760  C  CZ   . TYR   A  1  450 ? 60.356  21.162  -14.867  1.00 110.74 ? 450  TYR   A CZ   1 
ATOM   6761  O  OH   . TYR   A  1  450 ? 59.663  21.956  -15.752  1.00 111.87 ? 450  TYR   A OH   1 
ATOM   6762  H  H    . TYR   A  1  450 ? 60.036  18.959  -10.933  1.00 115.54 ? 450  TYR   A H    1 
ATOM   6763  H  HA   . TYR   A  1  450 ? 62.425  17.901  -10.196  1.00 115.56 ? 450  TYR   A HA   1 
ATOM   6764  H  HB2  . TYR   A  1  450 ? 63.421  18.989  -12.077  1.00 117.07 ? 450  TYR   A HB2  1 
ATOM   6765  H  HB3  . TYR   A  1  450 ? 62.496  17.761  -12.478  1.00 117.07 ? 450  TYR   A HB3  1 
ATOM   6766  H  HD1  . TYR   A  1  450 ? 60.153  18.338  -13.329  1.00 124.39 ? 450  TYR   A HD1  1 
ATOM   6767  H  HD2  . TYR   A  1  450 ? 63.096  21.042  -13.171  1.00 132.09 ? 450  TYR   A HD2  1 
ATOM   6768  H  HE1  . TYR   A  1  450 ? 58.996  19.681  -14.803  1.00 128.00 ? 450  TYR   A HE1  1 
ATOM   6769  H  HE2  . TYR   A  1  450 ? 61.942  22.385  -14.653  1.00 134.21 ? 450  TYR   A HE2  1 
ATOM   6770  H  HH   . TYR   A  1  450 ? 59.572  22.728  -15.435  1.00 134.29 ? 450  TYR   A HH   1 
ATOM   6771  N  N    . PRO   A  1  451 ? 63.177  19.978  -9.014   1.00 99.78  ? 451  PRO   A N    1 
ATOM   6772  C  CA   . PRO   A  1  451 ? 63.999  18.852  -8.548   1.00 100.64 ? 451  PRO   A CA   1 
ATOM   6773  C  C    . PRO   A  1  451 ? 63.223  17.855  -7.688   1.00 97.93  ? 451  PRO   A C    1 
ATOM   6774  O  O    . PRO   A  1  451 ? 62.206  18.209  -7.091   1.00 100.37 ? 451  PRO   A O    1 
ATOM   6775  C  CB   . PRO   A  1  451 ? 65.099  19.536  -7.730   1.00 105.40 ? 451  PRO   A CB   1 
ATOM   6776  C  CG   . PRO   A  1  451 ? 64.487  20.804  -7.265   1.00 106.83 ? 451  PRO   A CG   1 
ATOM   6777  C  CD   . PRO   A  1  451 ? 63.593  21.247  -8.389   1.00 105.26 ? 451  PRO   A CD   1 
ATOM   6778  H  HA   . PRO   A  1  451 ? 64.391  18.383  -9.301   1.00 120.81 ? 451  PRO   A HA   1 
ATOM   6779  H  HB2  . PRO   A  1  451 ? 65.352  18.976  -6.980   1.00 126.52 ? 451  PRO   A HB2  1 
ATOM   6780  H  HB3  . PRO   A  1  451 ? 65.872  19.708  -8.291   1.00 126.52 ? 451  PRO   A HB3  1 
ATOM   6781  H  HG2  . PRO   A  1  451 ? 63.975  20.645  -6.458   1.00 128.24 ? 451  PRO   A HG2  1 
ATOM   6782  H  HG3  . PRO   A  1  451 ? 65.180  21.461  -7.095   1.00 128.24 ? 451  PRO   A HG3  1 
ATOM   6783  H  HD2  . PRO   A  1  451 ? 62.825  21.732  -8.048   1.00 126.35 ? 451  PRO   A HD2  1 
ATOM   6784  H  HD3  . PRO   A  1  451 ? 64.081  21.799  -9.020   1.00 126.35 ? 451  PRO   A HD3  1 
ATOM   6785  N  N    . SER   A  1  452 ? 63.711  16.614  -7.631   1.00 97.90  ? 452  SER   A N    1 
ATOM   6786  C  CA   . SER   A  1  452 ? 63.031  15.573  -6.868   1.00 94.20  ? 452  SER   A CA   1 
ATOM   6787  C  C    . SER   A  1  452 ? 63.423  15.618  -5.395   1.00 96.17  ? 452  SER   A C    1 
ATOM   6788  O  O    . SER   A  1  452 ? 62.558  15.587  -4.514   1.00 96.91  ? 452  SER   A O    1 
ATOM   6789  C  CB   . SER   A  1  452 ? 63.348  14.201  -7.466   1.00 93.68  ? 452  SER   A CB   1 
ATOM   6790  O  OG   . SER   A  1  452 ? 62.732  13.164  -6.724   1.00 93.72  ? 452  SER   A OG   1 
ATOM   6791  H  H    . SER   A  1  452 ? 64.430  16.353  -8.024   1.00 117.51 ? 452  SER   A H    1 
ATOM   6792  H  HA   . SER   A  1  452 ? 62.074  15.714  -6.926   1.00 113.08 ? 452  SER   A HA   1 
ATOM   6793  H  HB2  . SER   A  1  452 ? 63.020  14.172  -8.379   1.00 112.45 ? 452  SER   A HB2  1 
ATOM   6794  H  HB3  . SER   A  1  452 ? 64.309  14.067  -7.455   1.00 112.45 ? 452  SER   A HB3  1 
ATOM   6795  H  HG   . SER   A  1  452 ? 62.900  12.420  -7.075   1.00 112.51 ? 452  SER   A HG   1 
ATOM   6796  N  N    . ILE   A  1  453 ? 64.721  15.684  -5.112   1.00 97.50  ? 453  ILE   A N    1 
ATOM   6797  C  CA   . ILE   A  1  453 ? 65.203  15.817  -3.742   1.00 98.56  ? 453  ILE   A CA   1 
ATOM   6798  C  C    . ILE   A  1  453 ? 65.151  17.287  -3.349   1.00 101.39 ? 453  ILE   A C    1 
ATOM   6799  O  O    . ILE   A  1  453 ? 65.521  18.168  -4.135   1.00 100.06 ? 453  ILE   A O    1 
ATOM   6800  C  CB   . ILE   A  1  453 ? 66.626  15.245  -3.610   1.00 98.76  ? 453  ILE   A CB   1 
ATOM   6801  C  CG1  . ILE   A  1  453 ? 66.628  13.732  -3.853   1.00 98.58  ? 453  ILE   A CG1  1 
ATOM   6802  C  CG2  . ILE   A  1  453 ? 67.205  15.546  -2.232   1.00 100.30 ? 453  ILE   A CG2  1 
ATOM   6803  C  CD1  . ILE   A  1  453 ? 66.772  13.329  -5.309   1.00 98.62  ? 453  ILE   A CD1  1 
ATOM   6804  H  H    . ILE   A  1  453 ? 65.347  15.653  -5.700   1.00 117.04 ? 453  ILE   A H    1 
ATOM   6805  H  HA   . ILE   A  1  453 ? 64.626  15.315  -3.145   1.00 118.31 ? 453  ILE   A HA   1 
ATOM   6806  H  HB   . ILE   A  1  453 ? 67.178  15.674  -4.283   1.00 118.55 ? 453  ILE   A HB   1 
ATOM   6807  H  HG12 . ILE   A  1  453 ? 67.371  13.342  -3.366   1.00 118.33 ? 453  ILE   A HG12 1 
ATOM   6808  H  HG13 . ILE   A  1  453 ? 65.790  13.366  -3.529   1.00 118.33 ? 453  ILE   A HG13 1 
ATOM   6809  H  HG21 . ILE   A  1  453 ? 68.085  15.143  -2.165   1.00 120.40 ? 453  ILE   A HG21 1 
ATOM   6810  H  HG22 . ILE   A  1  453 ? 67.271  16.507  -2.119   1.00 120.40 ? 453  ILE   A HG22 1 
ATOM   6811  H  HG23 . ILE   A  1  453 ? 66.619  15.173  -1.555   1.00 120.40 ? 453  ILE   A HG23 1 
ATOM   6812  H  HD11 . ILE   A  1  453 ? 66.702  12.364  -5.378   1.00 118.38 ? 453  ILE   A HD11 1 
ATOM   6813  H  HD12 . ILE   A  1  453 ? 66.066  13.751  -5.824   1.00 118.38 ? 453  ILE   A HD12 1 
ATOM   6814  H  HD13 . ILE   A  1  453 ? 67.638  13.622  -5.633   1.00 118.38 ? 453  ILE   A HD13 1 
ATOM   6815  N  N    . LEU   A  1  454 ? 64.692  17.561  -2.130   1.00 102.29 ? 454  LEU   A N    1 
ATOM   6816  C  CA   . LEU   A  1  454 ? 64.480  18.924  -1.658   1.00 104.67 ? 454  LEU   A CA   1 
ATOM   6817  C  C    . LEU   A  1  454 ? 65.287  19.172  -0.391   1.00 107.98 ? 454  LEU   A C    1 
ATOM   6818  O  O    . LEU   A  1  454 ? 65.223  18.382  0.558    1.00 110.70 ? 454  LEU   A O    1 
ATOM   6819  C  CB   . LEU   A  1  454 ? 62.992  19.184  -1.398   1.00 102.10 ? 454  LEU   A CB   1 
ATOM   6820  C  CG   . LEU   A  1  454 ? 62.067  19.047  -2.611   1.00 96.07  ? 454  LEU   A CG   1 
ATOM   6821  C  CD1  . LEU   A  1  454 ? 60.620  19.288  -2.206   1.00 90.13  ? 454  LEU   A CD1  1 
ATOM   6822  C  CD2  . LEU   A  1  454 ? 62.476  20.003  -3.724   1.00 97.68  ? 454  LEU   A CD2  1 
ATOM   6823  H  H    . LEU   A  1  454 ? 64.492  16.960  -1.548   1.00 122.78 ? 454  LEU   A H    1 
ATOM   6824  H  HA   . LEU   A  1  454 ? 64.794  19.546  -2.332   1.00 125.64 ? 454  LEU   A HA   1 
ATOM   6825  H  HB2  . LEU   A  1  454 ? 62.686  18.551  -0.730   1.00 122.56 ? 454  LEU   A HB2  1 
ATOM   6826  H  HB3  . LEU   A  1  454 ? 62.897  20.090  -1.065   1.00 122.56 ? 454  LEU   A HB3  1 
ATOM   6827  H  HG   . LEU   A  1  454 ? 62.141  18.144  -2.956   1.00 115.32 ? 454  LEU   A HG   1 
ATOM   6828  H  HD11 . LEU   A  1  454 ? 60.043  19.085  -2.959   1.00 108.19 ? 454  LEU   A HD11 1 
ATOM   6829  H  HD12 . LEU   A  1  454 ? 60.402  18.711  -1.457   1.00 108.19 ? 454  LEU   A HD12 1 
ATOM   6830  H  HD13 . LEU   A  1  454 ? 60.514  20.217  -1.949   1.00 108.19 ? 454  LEU   A HD13 1 
ATOM   6831  H  HD21 . LEU   A  1  454 ? 61.887  19.873  -4.484   1.00 117.26 ? 454  LEU   A HD21 1 
ATOM   6832  H  HD22 . LEU   A  1  454 ? 62.404  20.914  -3.401   1.00 117.26 ? 454  LEU   A HD22 1 
ATOM   6833  H  HD23 . LEU   A  1  454 ? 63.393  19.815  -3.980   1.00 117.26 ? 454  LEU   A HD23 1 
ATOM   6834  N  N    . ASN   A  1  455 ? 66.034  20.274  -0.378   1.00 106.69 ? 455  ASN   A N    1 
ATOM   6835  C  CA   . ASN   A  1  455 ? 66.843  20.683  0.763    1.00 109.87 ? 455  ASN   A CA   1 
ATOM   6836  C  C    . ASN   A  1  455 ? 66.248  21.940  1.380    1.00 113.95 ? 455  ASN   A C    1 
ATOM   6837  O  O    . ASN   A  1  455 ? 66.046  22.943  0.688    1.00 111.90 ? 455  ASN   A O    1 
ATOM   6838  C  CB   . ASN   A  1  455 ? 68.293  20.935  0.345    1.00 109.61 ? 455  ASN   A CB   1 
ATOM   6839  C  CG   . ASN   A  1  455 ? 69.134  21.528  1.467    1.00 111.27 ? 455  ASN   A CG   1 
ATOM   6840  O  OD1  . ASN   A  1  455 ? 68.667  21.694  2.594    1.00 112.67 ? 455  ASN   A OD1  1 
ATOM   6841  N  ND2  . ASN   A  1  455 ? 70.389  21.835  1.163    1.00 112.59 ? 455  ASN   A ND2  1 
ATOM   6842  H  H    . ASN   A  1  455 ? 66.089  20.818  -1.043   1.00 128.07 ? 455  ASN   A H    1 
ATOM   6843  H  HA   . ASN   A  1  455 ? 66.836  19.980  1.431    1.00 131.88 ? 455  ASN   A HA   1 
ATOM   6844  H  HB2  . ASN   A  1  455 ? 68.697  20.094  0.080    1.00 131.56 ? 455  ASN   A HB2  1 
ATOM   6845  H  HB3  . ASN   A  1  455 ? 68.304  21.558  -0.399   1.00 131.56 ? 455  ASN   A HB3  1 
ATOM   6846  H  HD21 . ASN   A  1  455 ? 70.907  22.172  1.761    1.00 135.14 ? 455  ASN   A HD21 1 
ATOM   6847  H  HD22 . ASN   A  1  455 ? 70.685  21.695  0.367    1.00 135.14 ? 455  ASN   A HD22 1 
ATOM   6848  N  N    . GLN   A  1  456 ? 65.995  21.887  2.689    1.00 120.87 ? 456  GLN   A N    1 
ATOM   6849  C  CA   . GLN   A  1  456 ? 65.331  22.996  3.366    1.00 127.69 ? 456  GLN   A CA   1 
ATOM   6850  C  C    . GLN   A  1  456 ? 66.185  24.258  3.356    1.00 131.75 ? 456  GLN   A C    1 
ATOM   6851  O  O    . GLN   A  1  456 ? 65.673  25.356  3.104    1.00 135.94 ? 456  GLN   A O    1 
ATOM   6852  C  CB   . GLN   A  1  456 ? 64.991  22.590  4.800    1.00 130.80 ? 456  GLN   A CB   1 
ATOM   6853  C  CG   . GLN   A  1  456 ? 63.816  21.628  4.891    1.00 127.21 ? 456  GLN   A CG   1 
ATOM   6854  C  CD   . GLN   A  1  456 ? 63.788  20.840  6.185    1.00 127.10 ? 456  GLN   A CD   1 
ATOM   6855  O  OE1  . GLN   A  1  456 ? 62.744  20.721  6.824    1.00 125.70 ? 456  GLN   A OE1  1 
ATOM   6856  N  NE2  . GLN   A  1  456 ? 64.932  20.280  6.569    1.00 127.12 ? 456  GLN   A NE2  1 
ATOM   6857  H  H    . GLN   A  1  456 ? 66.196  21.227  3.202    1.00 145.08 ? 456  GLN   A H    1 
ATOM   6858  H  HA   . GLN   A  1  456 ? 64.506  23.198  2.897    1.00 153.27 ? 456  GLN   A HA   1 
ATOM   6859  H  HB2  . GLN   A  1  456 ? 65.764  22.156  5.194    1.00 156.99 ? 456  GLN   A HB2  1 
ATOM   6860  H  HB3  . GLN   A  1  456 ? 64.764  23.387  5.305    1.00 156.99 ? 456  GLN   A HB3  1 
ATOM   6861  H  HG2  . GLN   A  1  456 ? 62.990  22.133  4.832    1.00 152.69 ? 456  GLN   A HG2  1 
ATOM   6862  H  HG3  . GLN   A  1  456 ? 63.871  20.995  4.158    1.00 152.69 ? 456  GLN   A HG3  1 
ATOM   6863  H  HE21 . GLN   A  1  456 ? 65.639  20.376  6.090    1.00 152.58 ? 456  GLN   A HE21 1 
ATOM   6864  H  HE22 . GLN   A  1  456 ? 64.964  19.824  7.297    1.00 152.58 ? 456  GLN   A HE22 1 
ATOM   6865  N  N    . ASP   A  1  457 ? 67.486  24.128  3.628    1.00 133.55 ? 457  ASP   A N    1 
ATOM   6866  C  CA   . ASP   A  1  457 ? 68.330  25.312  3.765    1.00 136.46 ? 457  ASP   A CA   1 
ATOM   6867  C  C    . ASP   A  1  457 ? 68.333  26.154  2.500    1.00 141.66 ? 457  ASP   A C    1 
ATOM   6868  O  O    . ASP   A  1  457 ? 68.517  27.376  2.564    1.00 148.30 ? 457  ASP   A O    1 
ATOM   6869  C  CB   . ASP   A  1  457 ? 69.761  24.901  4.110    1.00 134.71 ? 457  ASP   A CB   1 
ATOM   6870  C  CG   . ASP   A  1  457 ? 69.913  24.484  5.553    1.00 139.90 ? 457  ASP   A CG   1 
ATOM   6871  O  OD1  . ASP   A  1  457 ? 68.944  24.658  6.321    1.00 142.16 ? 457  ASP   A OD1  1 
ATOM   6872  O  OD2  . ASP   A  1  457 ? 70.996  23.984  5.922    1.00 142.64 ? 457  ASP   A OD2  1 
ATOM   6873  H  H    . ASP   A  1  457 ? 67.895  23.380  3.736    1.00 160.30 ? 457  ASP   A H    1 
ATOM   6874  H  HA   . ASP   A  1  457 ? 67.980  25.852  4.491    1.00 163.79 ? 457  ASP   A HA   1 
ATOM   6875  H  HB2  . ASP   A  1  457 ? 70.019  24.151  3.552    1.00 161.69 ? 457  ASP   A HB2  1 
ATOM   6876  H  HB3  . ASP   A  1  457 ? 70.354  25.652  3.950    1.00 161.69 ? 457  ASP   A HB3  1 
ATOM   6877  N  N    . ASN   A  1  458 ? 68.130  25.521  1.351    1.00 142.62 ? 458  ASN   A N    1 
ATOM   6878  C  CA   . ASN   A  1  458 ? 68.281  26.167  0.053    1.00 141.04 ? 458  ASN   A CA   1 
ATOM   6879  C  C    . ASN   A  1  458 ? 67.036  26.990  -0.278   1.00 141.93 ? 458  ASN   A C    1 
ATOM   6880  O  O    . ASN   A  1  458 ? 65.961  26.428  -0.519   1.00 139.49 ? 458  ASN   A O    1 
ATOM   6881  C  CB   . ASN   A  1  458 ? 68.546  25.101  -1.005   1.00 136.98 ? 458  ASN   A CB   1 
ATOM   6882  C  CG   . ASN   A  1  458 ? 68.709  25.692  -2.374   1.00 139.98 ? 458  ASN   A CG   1 
ATOM   6883  O  OD1  . ASN   A  1  458 ? 67.737  25.801  -3.112   1.00 139.47 ? 458  ASN   A OD1  1 
ATOM   6884  N  ND2  . ASN   A  1  458 ? 69.934  26.125  -2.706   1.00 144.36 ? 458  ASN   A ND2  1 
ATOM   6885  H  H    . ASN   A  1  458 ? 67.897  24.695  1.294    1.00 171.18 ? 458  ASN   A H    1 
ATOM   6886  H  HA   . ASN   A  1  458 ? 69.027  26.786  0.082    1.00 169.28 ? 458  ASN   A HA   1 
ATOM   6887  H  HB2  . ASN   A  1  458 ? 69.361  24.626  -0.781   1.00 164.41 ? 458  ASN   A HB2  1 
ATOM   6888  H  HB3  . ASN   A  1  458 ? 67.798  24.484  -1.029   1.00 164.41 ? 458  ASN   A HB3  1 
ATOM   6889  H  HD21 . ASN   A  1  458 ? 70.119  26.486  -3.470   1.00 173.27 ? 458  ASN   A HD21 1 
ATOM   6890  N  N    . LYS   A  1  459 ? 67.180  28.328  -0.312   1.00 147.12 ? 459  LYS   A N    1 
ATOM   6891  C  CA   . LYS   A  1  459 ? 66.049  29.247  -0.524   1.00 152.04 ? 459  LYS   A CA   1 
ATOM   6892  C  C    . LYS   A  1  459 ? 66.466  30.356  -1.497   1.00 158.79 ? 459  LYS   A C    1 
ATOM   6893  O  O    . LYS   A  1  459 ? 66.863  31.450  -1.081   1.00 163.60 ? 459  LYS   A O    1 
ATOM   6894  C  CB   . LYS   A  1  459 ? 65.560  29.839  0.798    1.00 153.17 ? 459  LYS   A CB   1 
ATOM   6895  C  CG   . LYS   A  1  459 ? 65.480  28.874  1.972    1.00 147.91 ? 459  LYS   A CG   1 
ATOM   6896  C  CD   . LYS   A  1  459 ? 65.241  29.647  3.266    1.00 147.18 ? 459  LYS   A CD   1 
ATOM   6897  C  CE   . LYS   A  1  459 ? 64.552  28.809  4.331    1.00 145.07 ? 459  LYS   A CE   1 
ATOM   6898  N  NZ   . LYS   A  1  459 ? 63.615  29.637  5.145    1.00 148.23 ? 459  LYS   A NZ   1 
ATOM   6899  H  H    . LYS   A  1  459 ? 67.934  28.730  -0.213   1.00 176.58 ? 459  LYS   A H    1 
ATOM   6900  H  HA   . LYS   A  1  459 ? 65.334  28.740  -0.941   1.00 182.49 ? 459  LYS   A HA   1 
ATOM   6901  H  HB2  . LYS   A  1  459 ? 66.167  30.551  1.053    1.00 183.85 ? 459  LYS   A HB2  1 
ATOM   6902  H  HB3  . LYS   A  1  459 ? 64.669  30.196  0.659    1.00 183.85 ? 459  LYS   A HB3  1 
ATOM   6903  H  HG2  . LYS   A  1  459 ? 64.743  28.256  1.838    1.00 177.53 ? 459  LYS   A HG2  1 
ATOM   6904  H  HG3  . LYS   A  1  459 ? 66.313  28.384  2.051    1.00 177.53 ? 459  LYS   A HG3  1 
ATOM   6905  H  HD2  . LYS   A  1  459 ? 66.095  29.941  3.621    1.00 176.65 ? 459  LYS   A HD2  1 
ATOM   6906  H  HD3  . LYS   A  1  459 ? 64.679  30.415  3.078    1.00 176.65 ? 459  LYS   A HD3  1 
ATOM   6907  H  HE2  . LYS   A  1  459 ? 64.045  28.101  3.905    1.00 174.12 ? 459  LYS   A HE2  1 
ATOM   6908  H  HE3  . LYS   A  1  459 ? 65.219  28.429  4.924    1.00 174.12 ? 459  LYS   A HE3  1 
ATOM   6909  H  HZ1  . LYS   A  1  459 ? 63.356  29.183  5.866    1.00 177.92 ? 459  LYS   A HZ1  1 
ATOM   6910  H  HZ2  . LYS   A  1  459 ? 64.018  30.387  5.404    1.00 177.92 ? 459  LYS   A HZ2  1 
ATOM   6911  H  HZ3  . LYS   A  1  459 ? 62.897  29.846  4.662    1.00 177.92 ? 459  LYS   A HZ3  1 
ATOM   6912  N  N    . THR   A  1  460 ? 66.355  30.083  -2.796   1.00 162.61 ? 460  THR   A N    1 
ATOM   6913  C  CA   . THR   A  1  460 ? 66.608  31.082  -3.830   1.00 169.07 ? 460  THR   A CA   1 
ATOM   6914  C  C    . THR   A  1  460 ? 65.324  31.563  -4.495   1.00 171.44 ? 460  THR   A C    1 
ATOM   6915  O  O    . THR   A  1  460 ? 65.383  32.272  -5.505   1.00 177.27 ? 460  THR   A O    1 
ATOM   6916  C  CB   . THR   A  1  460 ? 67.564  30.524  -4.888   1.00 168.51 ? 460  THR   A CB   1 
ATOM   6917  O  OG1  . THR   A  1  460 ? 67.078  29.262  -5.364   1.00 167.03 ? 460  THR   A OG1  1 
ATOM   6918  C  CG2  . THR   A  1  460 ? 68.956  30.347  -4.305   1.00 167.66 ? 460  THR   A CG2  1 
ATOM   6919  H  H    . THR   A  1  460 ? 66.131  29.313  -3.107   1.00 195.17 ? 460  THR   A H    1 
ATOM   6920  H  HA   . THR   A  1  460 ? 67.038  31.847  -3.416   1.00 202.92 ? 460  THR   A HA   1 
ATOM   6921  H  HB   . THR   A  1  460 ? 67.620  31.144  -5.632   1.00 202.25 ? 460  THR   A HB   1 
ATOM   6922  H  HG1  . THR   A  1  460 ? 66.591  29.378  -6.039   1.00 200.47 ? 460  THR   A HG1  1 
ATOM   6923  H  HG21 . THR   A  1  460 ? 69.565  30.030  -4.990   1.00 201.22 ? 460  THR   A HG21 1 
ATOM   6924  H  HG22 . THR   A  1  460 ? 69.282  31.194  -3.962   1.00 201.22 ? 460  THR   A HG22 1 
ATOM   6925  H  HG23 . THR   A  1  460 ? 68.933  29.703  -3.581   1.00 201.22 ? 460  THR   A HG23 1 
ATOM   6926  N  N    . CYS   A  1  461 ? 64.172  31.204  -3.941   1.00 177.61 ? 461  CYS   A N    1 
ATOM   6927  C  CA   . CYS   A  1  461 ? 62.867  31.513  -4.502   1.00 176.95 ? 461  CYS   A CA   1 
ATOM   6928  C  C    . CYS   A  1  461 ? 62.126  32.444  -3.555   1.00 176.17 ? 461  CYS   A C    1 
ATOM   6929  O  O    . CYS   A  1  461 ? 62.372  32.443  -2.345   1.00 176.46 ? 461  CYS   A O    1 
ATOM   6930  C  CB   . CYS   A  1  461 ? 62.086  30.221  -4.723   1.00 177.28 ? 461  CYS   A CB   1 
ATOM   6931  S  SG   . CYS   A  1  461 ? 63.172  28.778  -4.624   1.00 182.50 ? 461  CYS   A SG   1 
ATOM   6932  H  H    . CYS   A  1  461 ? 64.121  30.760  -3.206   1.00 213.17 ? 461  CYS   A H    1 
ATOM   6933  H  HA   . CYS   A  1  461 ? 62.944  31.969  -5.354   1.00 212.38 ? 461  CYS   A HA   1 
ATOM   6934  H  HB2  . CYS   A  1  461 ? 61.402  30.138  -4.041   1.00 212.77 ? 461  CYS   A HB2  1 
ATOM   6935  H  HB3  . CYS   A  1  461 ? 61.678  30.239  -5.602   1.00 212.77 ? 461  CYS   A HB3  1 
ATOM   6936  H  HG   . CYS   A  1  461 ? 64.107  28.942  -5.358   1.00 219.04 ? 461  CYS   A HG   1 
ATOM   6937  N  N    . SER   A  1  462 ? 61.218  33.247  -4.105   1.00 170.99 ? 462  SER   A N    1 
ATOM   6938  C  CA   . SER   A  1  462 ? 60.573  34.311  -3.348   1.00 174.87 ? 462  SER   A CA   1 
ATOM   6939  C  C    . SER   A  1  462 ? 59.064  34.121  -3.335   1.00 166.85 ? 462  SER   A C    1 
ATOM   6940  O  O    . SER   A  1  462 ? 58.453  33.855  -4.375   1.00 152.61 ? 462  SER   A O    1 
ATOM   6941  C  CB   . SER   A  1  462 ? 60.923  35.686  -3.925   1.00 180.10 ? 462  SER   A CB   1 
ATOM   6942  O  OG   . SER   A  1  462 ? 60.426  35.832  -5.243   1.00 176.41 ? 462  SER   A OG   1 
ATOM   6943  H  H    . SER   A  1  462 ? 60.960  33.193  -4.923   1.00 205.23 ? 462  SER   A H    1 
ATOM   6944  H  HA   . SER   A  1  462 ? 60.881  34.267  -2.429   1.00 209.88 ? 462  SER   A HA   1 
ATOM   6945  H  HB2  . SER   A  1  462 ? 60.529  36.371  -3.363   1.00 216.16 ? 462  SER   A HB2  1 
ATOM   6946  H  HB3  . SER   A  1  462 ? 61.887  35.783  -3.941   1.00 216.16 ? 462  SER   A HB3  1 
ATOM   6947  H  HG   . SER   A  1  462 ? 60.007  36.557  -5.313   1.00 211.73 ? 462  SER   A HG   1 
ATOM   6948  N  N    . LEU   A  1  463 ? 58.478  34.265  -2.153   1.00 166.86 ? 463  LEU   A N    1 
ATOM   6949  C  CA   . LEU   A  1  463 ? 57.043  34.199  -1.939   1.00 161.45 ? 463  LEU   A CA   1 
ATOM   6950  C  C    . LEU   A  1  463 ? 56.386  35.493  -2.419   1.00 167.07 ? 463  LEU   A C    1 
ATOM   6951  O  O    . LEU   A  1  463 ? 57.028  36.547  -2.447   1.00 180.07 ? 463  LEU   A O    1 
ATOM   6952  C  CB   . LEU   A  1  463 ? 56.755  33.985  -0.454   1.00 156.12 ? 463  LEU   A CB   1 
ATOM   6953  C  CG   . LEU   A  1  463 ? 55.487  33.269  0.018    1.00 144.02 ? 463  LEU   A CG   1 
ATOM   6954  C  CD1  . LEU   A  1  463 ? 55.310  31.909  -0.644   1.00 136.21 ? 463  LEU   A CD1  1 
ATOM   6955  C  CD2  . LEU   A  1  463 ? 55.539  33.109  1.536    1.00 139.51 ? 463  LEU   A CD2  1 
ATOM   6956  H  H    . LEU   A  1  463 ? 58.911  34.409  -1.424   1.00 200.27 ? 463  LEU   A H    1 
ATOM   6957  H  HA   . LEU   A  1  463 ? 56.657  33.461  -2.436   1.00 193.78 ? 463  LEU   A HA   1 
ATOM   6958  H  HB2  . LEU   A  1  463 ? 57.497  33.473  -0.096   1.00 187.38 ? 463  LEU   A HB2  1 
ATOM   6959  H  HB3  . LEU   A  1  463 ? 56.729  34.864  -0.044   1.00 187.38 ? 463  LEU   A HB3  1 
ATOM   6960  H  HG   . LEU   A  1  463 ? 54.718  33.804  -0.233   1.00 172.86 ? 463  LEU   A HG   1 
ATOM   6961  H  HD11 . LEU   A  1  463 ? 54.380  31.643  -0.575   1.00 163.49 ? 463  LEU   A HD11 1 
ATOM   6962  H  HD12 . LEU   A  1  463 ? 55.566  31.977  -1.577   1.00 163.49 ? 463  LEU   A HD12 1 
ATOM   6963  H  HD13 . LEU   A  1  463 ? 55.874  31.262  -0.193   1.00 163.49 ? 463  LEU   A HD13 1 
ATOM   6964  H  HD21 . LEU   A  1  463 ? 55.017  33.815  1.947    1.00 167.45 ? 463  LEU   A HD21 1 
ATOM   6965  H  HD22 . LEU   A  1  463 ? 55.172  32.243  1.776    1.00 167.45 ? 463  LEU   A HD22 1 
ATOM   6966  H  HD23 . LEU   A  1  463 ? 56.462  33.168  1.829    1.00 167.45 ? 463  LEU   A HD23 1 
ATOM   6967  N  N    . PRO   A  1  464 ? 55.114  35.447  -2.816   1.00 161.59 ? 464  PRO   A N    1 
ATOM   6968  C  CA   . PRO   A  1  464 ? 54.409  36.699  -3.119   1.00 167.70 ? 464  PRO   A CA   1 
ATOM   6969  C  C    . PRO   A  1  464 ? 54.443  37.625  -1.913   1.00 172.82 ? 464  PRO   A C    1 
ATOM   6970  O  O    . PRO   A  1  464 ? 54.165  37.214  -0.784   1.00 175.63 ? 464  PRO   A O    1 
ATOM   6971  C  CB   . PRO   A  1  464 ? 52.985  36.242  -3.454   1.00 165.90 ? 464  PRO   A CB   1 
ATOM   6972  C  CG   . PRO   A  1  464 ? 53.124  34.826  -3.872   1.00 159.32 ? 464  PRO   A CG   1 
ATOM   6973  C  CD   . PRO   A  1  464 ? 54.278  34.264  -3.089   1.00 157.14 ? 464  PRO   A CD   1 
ATOM   6974  H  HA   . PRO   A  1  464 ? 54.790  37.141  -3.894   1.00 201.28 ? 464  PRO   A HA   1 
ATOM   6975  H  HB2  . PRO   A  1  464 ? 52.421  36.317  -2.668   1.00 199.12 ? 464  PRO   A HB2  1 
ATOM   6976  H  HB3  . PRO   A  1  464 ? 52.626  36.783  -4.174   1.00 199.12 ? 464  PRO   A HB3  1 
ATOM   6977  H  HG2  . PRO   A  1  464 ? 52.307  34.345  -3.668   1.00 191.22 ? 464  PRO   A HG2  1 
ATOM   6978  H  HG3  . PRO   A  1  464 ? 53.305  34.784  -4.824   1.00 191.22 ? 464  PRO   A HG3  1 
ATOM   6979  H  HD2  . PRO   A  1  464 ? 53.970  33.860  -2.263   1.00 188.60 ? 464  PRO   A HD2  1 
ATOM   6980  H  HD3  . PRO   A  1  464 ? 54.766  33.611  -3.615   1.00 188.60 ? 464  PRO   A HD3  1 
ATOM   6981  N  N    . GLY   A  1  465 ? 54.791  38.880  -2.159   1.00 206.65 ? 465  GLY   A N    1 
ATOM   6982  C  CA   . GLY   A  1  465 ? 55.095  39.808  -1.094   1.00 227.42 ? 465  GLY   A CA   1 
ATOM   6983  C  C    . GLY   A  1  465 ? 56.590  39.940  -0.888   1.00 212.23 ? 465  GLY   A C    1 
ATOM   6984  O  O    . GLY   A  1  465 ? 57.400  39.642  -1.769   1.00 222.09 ? 465  GLY   A O    1 
ATOM   6985  H  H    . GLY   A  1  465 ? 54.857  39.218  -2.947   1.00 248.01 ? 465  GLY   A H    1 
ATOM   6986  H  HA2  . GLY   A  1  465 ? 54.734  40.681  -1.311   1.00 272.94 ? 465  GLY   A HA2  1 
ATOM   6987  H  HA3  . GLY   A  1  465 ? 54.695  39.497  -0.267   1.00 272.94 ? 465  GLY   A HA3  1 
ATOM   6988  N  N    . THR   A  1  466 ? 56.961  40.383  0.313    1.00 178.67 ? 466  THR   A N    1 
ATOM   6989  C  CA   . THR   A  1  466 ? 58.356  40.653  0.631    1.00 188.42 ? 466  THR   A CA   1 
ATOM   6990  C  C    . THR   A  1  466 ? 59.007  39.564  1.483    1.00 187.85 ? 466  THR   A C    1 
ATOM   6991  O  O    . THR   A  1  466 ? 60.098  39.786  2.016    1.00 195.48 ? 466  THR   A O    1 
ATOM   6992  C  CB   . THR   A  1  466 ? 58.486  42.003  1.345    1.00 196.20 ? 466  THR   A CB   1 
ATOM   6993  O  OG1  . THR   A  1  466 ? 57.692  41.998  2.539    1.00 193.98 ? 466  THR   A OG1  1 
ATOM   6994  C  CG2  . THR   A  1  466 ? 58.035  43.145  0.437    1.00 203.87 ? 466  THR   A CG2  1 
ATOM   6995  H  H    . THR   A  1  466 ? 56.417  40.534  0.961    1.00 214.44 ? 466  THR   A H    1 
ATOM   6996  H  HA   . THR   A  1  466 ? 58.844  40.700  -0.206   1.00 226.14 ? 466  THR   A HA   1 
ATOM   6997  H  HB   . THR   A  1  466 ? 59.415  42.154  1.578    1.00 235.48 ? 466  THR   A HB   1 
ATOM   6998  H  HG1  . THR   A  1  466 ? 56.958  42.382  2.398    1.00 232.81 ? 466  THR   A HG1  1 
ATOM   6999  H  HG21 . THR   A  1  466 ? 58.397  43.986  0.756    1.00 244.68 ? 466  THR   A HG21 1 
ATOM   7000  H  HG22 . THR   A  1  466 ? 58.347  42.992  -0.469   1.00 244.68 ? 466  THR   A HG22 1 
ATOM   7001  H  HG23 . THR   A  1  466 ? 57.067  43.201  0.430    1.00 244.68 ? 466  THR   A HG23 1 
ATOM   7002  N  N    . ALA   A  1  467 ? 58.377  38.394  1.617    1.00 196.31 ? 467  ALA   A N    1 
ATOM   7003  C  CA   . ALA   A  1  467 ? 58.958  37.337  2.443    1.00 207.28 ? 467  ALA   A CA   1 
ATOM   7004  C  C    . ALA   A  1  467 ? 60.281  36.850  1.859    1.00 210.22 ? 467  ALA   A C    1 
ATOM   7005  O  O    . ALA   A  1  467 ? 61.291  36.758  2.568    1.00 227.20 ? 467  ALA   A O    1 
ATOM   7006  C  CB   . ALA   A  1  467 ? 57.969  36.179  2.590    1.00 208.17 ? 467  ALA   A CB   1 
ATOM   7007  H  H    . ALA   A  1  467 ? 57.627  38.191  1.247    1.00 235.61 ? 467  ALA   A H    1 
ATOM   7008  H  HA   . ALA   A  1  467 ? 59.133  37.693  3.328    1.00 248.77 ? 467  ALA   A HA   1 
ATOM   7009  H  HB1  . ALA   A  1  467 ? 58.360  35.380  2.204    1.00 249.84 ? 467  ALA   A HB1  1 
ATOM   7010  H  HB2  . ALA   A  1  467 ? 57.787  36.037  3.532    1.00 249.84 ? 467  ALA   A HB2  1 
ATOM   7011  H  HB3  . ALA   A  1  467 ? 57.148  36.404  2.124    1.00 249.84 ? 467  ALA   A HB3  1 
ATOM   7012  N  N    . LEU   A  1  468 ? 60.288  36.516  0.568    1.00 196.74 ? 468  LEU   A N    1 
ATOM   7013  C  CA   . LEU   A  1  468 ? 61.512  36.214  -0.181   1.00 198.28 ? 468  LEU   A CA   1 
ATOM   7014  C  C    . LEU   A  1  468 ? 62.387  35.154  0.496    1.00 191.83 ? 468  LEU   A C    1 
ATOM   7015  O  O    . LEU   A  1  468 ? 63.617  35.219  0.416    1.00 199.02 ? 468  LEU   A O    1 
ATOM   7016  C  CB   . LEU   A  1  468 ? 62.338  37.488  -0.409   1.00 206.27 ? 468  LEU   A CB   1 
ATOM   7017  C  CG   . LEU   A  1  468 ? 61.632  38.732  -0.958   1.00 210.62 ? 468  LEU   A CG   1 
ATOM   7018  C  CD1  . LEU   A  1  468 ? 62.281  39.995  -0.402   1.00 217.95 ? 468  LEU   A CD1  1 
ATOM   7019  C  CD2  . LEU   A  1  468 ? 61.642  38.762  -2.483   1.00 210.27 ? 468  LEU   A CD2  1 
ATOM   7020  H  H    . LEU   A  1  468 ? 59.576  36.455  0.088    1.00 236.12 ? 468  LEU   A H    1 
ATOM   7021  H  HA   . LEU   A  1  468 ? 61.234  35.848  -1.035   1.00 237.97 ? 468  LEU   A HA   1 
ATOM   7022  H  HB2  . LEU   A  1  468 ? 62.722  37.743  0.445    1.00 247.56 ? 468  LEU   A HB2  1 
ATOM   7023  H  HB3  . LEU   A  1  468 ? 63.043  37.270  -1.038   1.00 247.56 ? 468  LEU   A HB3  1 
ATOM   7024  H  HG   . LEU   A  1  468 ? 60.705  38.702  -0.676   1.00 252.78 ? 468  LEU   A HG   1 
ATOM   7025  H  HD11 . LEU   A  1  468 ? 61.848  40.770  -0.793   1.00 261.57 ? 468  LEU   A HD11 1 
ATOM   7026  H  HD12 . LEU   A  1  468 ? 62.174  40.007  0.562    1.00 261.57 ? 468  LEU   A HD12 1 
ATOM   7027  H  HD13 . LEU   A  1  468 ? 63.223  39.993  -0.631   1.00 261.57 ? 468  LEU   A HD13 1 
ATOM   7028  H  HD21 . LEU   A  1  468 ? 62.358  38.193  -2.806   1.00 252.36 ? 468  LEU   A HD21 1 
ATOM   7029  H  HD22 . LEU   A  1  468 ? 60.788  38.438  -2.810   1.00 252.36 ? 468  LEU   A HD22 1 
ATOM   7030  H  HD23 . LEU   A  1  468 ? 61.785  39.675  -2.779   1.00 252.36 ? 468  LEU   A HD23 1 
ATOM   7031  N  N    . LYS   A  1  469 ? 61.791  34.153  1.161    1.00 186.63 ? 469  LYS   A N    1 
ATOM   7032  C  CA   . LYS   A  1  469 ? 62.609  33.139  1.852    1.00 185.65 ? 469  LYS   A CA   1 
ATOM   7033  C  C    . LYS   A  1  469 ? 61.858  31.797  1.891    1.00 171.64 ? 469  LYS   A C    1 
ATOM   7034  O  O    . LYS   A  1  469 ? 61.215  31.465  2.890    1.00 182.38 ? 469  LYS   A O    1 
ATOM   7035  C  CB   . LYS   A  1  469 ? 62.984  33.581  3.263    1.00 182.03 ? 469  LYS   A CB   1 
ATOM   7036  C  CG   . LYS   A  1  469 ? 63.948  34.760  3.393    1.00 168.07 ? 469  LYS   A CG   1 
ATOM   7037  C  CD   . LYS   A  1  469 ? 64.205  35.077  4.874    1.00 153.91 ? 469  LYS   A CD   1 
ATOM   7038  C  CE   . LYS   A  1  469 ? 65.179  36.235  5.066    1.00 152.91 ? 469  LYS   A CE   1 
ATOM   7039  N  NZ   . LYS   A  1  469 ? 65.414  36.561  6.507    1.00 156.41 ? 469  LYS   A NZ   1 
ATOM   7040  H  H    . LYS   A  1  469 ? 60.940  34.041  1.225    1.00 223.99 ? 469  LYS   A H    1 
ATOM   7041  H  HA   . LYS   A  1  469 ? 63.411  33.013  1.320    1.00 222.82 ? 469  LYS   A HA   1 
ATOM   7042  H  HB2  . LYS   A  1  469 ? 62.168  33.833  3.723    1.00 218.47 ? 469  LYS   A HB2  1 
ATOM   7043  H  HB3  . LYS   A  1  469 ? 63.398  32.828  3.712    1.00 218.47 ? 469  LYS   A HB3  1 
ATOM   7044  H  HG2  . LYS   A  1  469 ? 64.793  34.538  2.972    1.00 201.72 ? 469  LYS   A HG2  1 
ATOM   7045  H  HG3  . LYS   A  1  469 ? 63.563  35.544  2.970    1.00 201.72 ? 469  LYS   A HG3  1 
ATOM   7046  H  HD2  . LYS   A  1  469 ? 63.365  35.318  5.297    1.00 184.72 ? 469  LYS   A HD2  1 
ATOM   7047  H  HD3  . LYS   A  1  469 ? 64.581  34.294  5.305    1.00 184.72 ? 469  LYS   A HD3  1 
ATOM   7048  H  HE2  . LYS   A  1  469 ? 66.032  35.999  4.668    1.00 183.53 ? 469  LYS   A HE2  1 
ATOM   7049  H  HE3  . LYS   A  1  469 ? 64.819  37.026  4.635    1.00 183.53 ? 469  LYS   A HE3  1 
ATOM   7050  H  HZ1  . LYS   A  1  469 ? 65.631  37.420  6.593    1.00 187.73 ? 469  LYS   A HZ1  1 
ATOM   7051  H  HZ2  . LYS   A  1  469 ? 64.678  36.400  6.980    1.00 187.73 ? 469  LYS   A HZ2  1 
ATOM   7052  H  HZ3  . LYS   A  1  469 ? 66.079  36.063  6.827    1.00 187.73 ? 469  LYS   A HZ3  1 
ATOM   7053  N  N    . VAL   A  1  470 ? 61.980  31.011  0.823    1.00 151.41 ? 470  VAL   A N    1 
ATOM   7054  C  CA   . VAL   A  1  470 ? 61.353  29.690  0.792    1.00 135.67 ? 470  VAL   A CA   1 
ATOM   7055  C  C    . VAL   A  1  470 ? 62.162  28.741  -0.085   1.00 138.04 ? 470  VAL   A C    1 
ATOM   7056  O  O    . VAL   A  1  470 ? 62.783  29.149  -1.070   1.00 144.64 ? 470  VAL   A O    1 
ATOM   7057  C  CB   . VAL   A  1  470 ? 59.887  29.758  0.297    1.00 132.44 ? 470  VAL   A CB   1 
ATOM   7058  C  CG1  . VAL   A  1  470 ? 58.980  30.315  1.386    1.00 132.54 ? 470  VAL   A CG1  1 
ATOM   7059  C  CG2  . VAL   A  1  470 ? 59.789  30.592  -0.972   1.00 135.50 ? 470  VAL   A CG2  1 
ATOM   7060  H  H    . VAL   A  1  470 ? 62.416  31.218  0.111    1.00 181.73 ? 470  VAL   A H    1 
ATOM   7061  H  HA   . VAL   A  1  470 ? 61.370  29.341  1.697    1.00 162.84 ? 470  VAL   A HA   1 
ATOM   7062  H  HB   . VAL   A  1  470 ? 59.584  28.861  0.088    1.00 158.96 ? 470  VAL   A HB   1 
ATOM   7063  H  HG11 . VAL   A  1  470 ? 58.063  30.302  1.070    1.00 159.08 ? 470  VAL   A HG11 1 
ATOM   7064  H  HG12 . VAL   A  1  470 ? 59.064  29.763  2.180    1.00 159.08 ? 470  VAL   A HG12 1 
ATOM   7065  H  HG13 . VAL   A  1  470 ? 59.248  31.225  1.586    1.00 159.08 ? 470  VAL   A HG13 1 
ATOM   7066  H  HG21 . VAL   A  1  470 ? 58.893  30.510  -1.335   1.00 162.64 ? 470  VAL   A HG21 1 
ATOM   7067  H  HG22 . VAL   A  1  470 ? 59.974  31.519  -0.755   1.00 162.64 ? 470  VAL   A HG22 1 
ATOM   7068  H  HG23 . VAL   A  1  470 ? 60.438  30.266  -1.614   1.00 162.64 ? 470  VAL   A HG23 1 
ATOM   7069  N  N    . SER   A  1  471 ? 62.134  27.458  0.283    1.00 129.86 ? 471  SER   A N    1 
ATOM   7070  C  CA   . SER   A  1  471 ? 62.749  26.384  -0.493   1.00 129.45 ? 471  SER   A CA   1 
ATOM   7071  C  C    . SER   A  1  471 ? 61.727  25.840  -1.486   1.00 127.47 ? 471  SER   A C    1 
ATOM   7072  O  O    . SER   A  1  471 ? 60.596  25.528  -1.101   1.00 113.67 ? 471  SER   A O    1 
ATOM   7073  C  CB   . SER   A  1  471 ? 63.230  25.270  0.438    1.00 130.46 ? 471  SER   A CB   1 
ATOM   7074  O  OG   . SER   A  1  471 ? 64.167  24.426  -0.206   1.00 131.03 ? 471  SER   A OG   1 
ATOM   7075  H  H    . SER   A  1  471 ? 61.754  27.177  1.002    1.00 155.87 ? 471  SER   A H    1 
ATOM   7076  H  HA   . SER   A  1  471 ? 63.513  26.721  -0.985   1.00 155.38 ? 471  SER   A HA   1 
ATOM   7077  H  HB2  . SER   A  1  471 ? 63.651  25.671  1.215    1.00 156.58 ? 471  SER   A HB2  1 
ATOM   7078  H  HB3  . SER   A  1  471 ? 62.466  24.739  0.712    1.00 156.58 ? 471  SER   A HB3  1 
ATOM   7079  H  HG   . SER   A  1  471 ? 64.643  24.037  0.366    1.00 157.28 ? 471  SER   A HG   1 
ATOM   7080  N  N    . CYS   A  1  472 ? 62.125  25.707  -2.755   1.00 144.72 ? 472  CYS   A N    1 
ATOM   7081  C  CA   . CYS   A  1  472 ? 61.147  25.543  -3.821   1.00 157.29 ? 472  CYS   A CA   1 
ATOM   7082  C  C    . CYS   A  1  472 ? 61.580  24.518  -4.862   1.00 133.00 ? 472  CYS   A C    1 
ATOM   7083  O  O    . CYS   A  1  472 ? 62.728  24.066  -4.904   1.00 129.63 ? 472  CYS   A O    1 
ATOM   7084  C  CB   . CYS   A  1  472 ? 60.875  26.871  -4.536   1.00 182.51 ? 472  CYS   A CB   1 
ATOM   7085  S  SG   . CYS   A  1  472 ? 62.182  27.351  -5.666   1.00 182.51 ? 472  CYS   A SG   1 
ATOM   7086  H  H    . CYS   A  1  472 ? 62.945  25.710  -3.015   1.00 173.70 ? 472  CYS   A H    1 
ATOM   7087  H  HA   . CYS   A  1  472 ? 60.343  25.201  -3.398   1.00 188.79 ? 472  CYS   A HA   1 
ATOM   7088  H  HB2  . CYS   A  1  472 ? 60.054  26.789  -5.047   1.00 219.05 ? 472  CYS   A HB2  1 
ATOM   7089  H  HB3  . CYS   A  1  472 ? 60.783  27.571  -3.871   1.00 219.05 ? 472  CYS   A HB3  1 
ATOM   7090  H  HG   . CYS   A  1  472 ? 61.748  28.152  -6.448   1.00 219.05 ? 472  CYS   A HG   1 
ATOM   7091  N  N    . PHE   A  1  473 ? 60.616  24.189  -5.719   1.00 116.76 ? 473  PHE   A N    1 
ATOM   7092  C  CA   . PHE   A  1  473 ? 60.725  23.254  -6.835   1.00 111.76 ? 473  PHE   A CA   1 
ATOM   7093  C  C    . PHE   A  1  473 ? 59.492  23.497  -7.703   1.00 111.59 ? 473  PHE   A C    1 
ATOM   7094  O  O    . PHE   A  1  473 ? 58.687  24.388  -7.414   1.00 109.61 ? 473  PHE   A O    1 
ATOM   7095  C  CB   . PHE   A  1  473 ? 60.802  21.810  -6.350   1.00 108.42 ? 473  PHE   A CB   1 
ATOM   7096  C  CG   . PHE   A  1  473 ? 59.577  21.363  -5.619   1.00 104.67 ? 473  PHE   A CG   1 
ATOM   7097  C  CD1  . PHE   A  1  473 ? 59.341  21.785  -4.323   1.00 106.35 ? 473  PHE   A CD1  1 
ATOM   7098  C  CD2  . PHE   A  1  473 ? 58.652  20.537  -6.231   1.00 100.66 ? 473  PHE   A CD2  1 
ATOM   7099  C  CE1  . PHE   A  1  473 ? 58.209  21.386  -3.648   1.00 104.96 ? 473  PHE   A CE1  1 
ATOM   7100  C  CE2  . PHE   A  1  473 ? 57.517  20.132  -5.561   1.00 99.30  ? 473  PHE   A CE2  1 
ATOM   7101  C  CZ   . PHE   A  1  473 ? 57.295  20.558  -4.266   1.00 101.48 ? 473  PHE   A CZ   1 
ATOM   7102  H  H    . PHE   A  1  473 ? 59.824  24.521  -5.670   1.00 140.15 ? 473  PHE   A H    1 
ATOM   7103  H  HA   . PHE   A  1  473 ? 61.527  23.431  -7.351   1.00 134.15 ? 473  PHE   A HA   1 
ATOM   7104  H  HB2  . PHE   A  1  473 ? 60.920  21.227  -7.117   1.00 130.14 ? 473  PHE   A HB2  1 
ATOM   7105  H  HB3  . PHE   A  1  473 ? 61.557  21.721  -5.747   1.00 130.14 ? 473  PHE   A HB3  1 
ATOM   7106  H  HD1  . PHE   A  1  473 ? 59.953  22.344  -3.903   1.00 127.66 ? 473  PHE   A HD1  1 
ATOM   7107  H  HD2  . PHE   A  1  473 ? 58.797  20.252  -7.105   1.00 120.83 ? 473  PHE   A HD2  1 
ATOM   7108  H  HE1  . PHE   A  1  473 ? 58.060  21.674  -2.776   1.00 125.99 ? 473  PHE   A HE1  1 
ATOM   7109  H  HE2  . PHE   A  1  473 ? 56.903  19.574  -5.980   1.00 119.19 ? 473  PHE   A HE2  1 
ATOM   7110  H  HZ   . PHE   A  1  473 ? 56.530  20.286  -3.812   1.00 121.82 ? 473  PHE   A HZ   1 
ATOM   7111  N  N    . ASN   A  1  474 ? 59.329  22.697  -8.758   1.00 114.01 ? 474  ASN   A N    1 
ATOM   7112  C  CA   . ASN   A  1  474 ? 58.201  22.899  -9.659   1.00 111.68 ? 474  ASN   A CA   1 
ATOM   7113  C  C    . ASN   A  1  474 ? 57.571  21.573  -10.063  1.00 105.03 ? 474  ASN   A C    1 
ATOM   7114  O  O    . ASN   A  1  474 ? 58.215  20.521  -10.050  1.00 103.84 ? 474  ASN   A O    1 
ATOM   7115  C  CB   . ASN   A  1  474 ? 58.614  23.693  -10.913  1.00 117.40 ? 474  ASN   A CB   1 
ATOM   7116  C  CG   . ASN   A  1  474 ? 59.682  22.995  -11.733  1.00 124.68 ? 474  ASN   A CG   1 
ATOM   7117  O  OD1  . ASN   A  1  474 ? 59.654  21.778  -11.917  1.00 125.28 ? 474  ASN   A OD1  1 
ATOM   7118  N  ND2  . ASN   A  1  474 ? 60.632  23.774  -12.239  1.00 132.00 ? 474  ASN   A ND2  1 
ATOM   7119  H  H    . ASN   A  1  474 ? 59.849  22.045  -8.966   1.00 136.85 ? 474  ASN   A H    1 
ATOM   7120  H  HA   . ASN   A  1  474 ? 57.517  23.396  -9.184   1.00 134.06 ? 474  ASN   A HA   1 
ATOM   7121  H  HB2  . ASN   A  1  474 ? 57.835  23.815  -11.479  1.00 140.92 ? 474  ASN   A HB2  1 
ATOM   7122  H  HB3  . ASN   A  1  474 ? 58.964  24.555  -10.639  1.00 140.92 ? 474  ASN   A HB3  1 
ATOM   7123  H  HD21 . ASN   A  1  474 ? 61.263  23.431  -12.712  1.00 158.44 ? 474  ASN   A HD21 1 
ATOM   7124  H  HD22 . ASN   A  1  474 ? 60.617  24.621  -12.092  1.00 158.44 ? 474  ASN   A HD22 1 
ATOM   7125  N  N    . VAL   A  1  475 ? 56.290  21.654  -10.423  1.00 101.33 ? 475  VAL   A N    1 
ATOM   7126  C  CA   . VAL   A  1  475 ? 55.476  20.521  -10.847  1.00 98.41  ? 475  VAL   A CA   1 
ATOM   7127  C  C    . VAL   A  1  475 ? 55.011  20.789  -12.271  1.00 98.66  ? 475  VAL   A C    1 
ATOM   7128  O  O    . VAL   A  1  475 ? 54.543  21.892  -12.579  1.00 96.69  ? 475  VAL   A O    1 
ATOM   7129  C  CB   . VAL   A  1  475 ? 54.269  20.314  -9.910   1.00 95.58  ? 475  VAL   A CB   1 
ATOM   7130  C  CG1  . VAL   A  1  475 ? 53.322  19.251  -10.458  1.00 93.75  ? 475  VAL   A CG1  1 
ATOM   7131  C  CG2  . VAL   A  1  475 ? 54.732  19.950  -8.504   1.00 93.95  ? 475  VAL   A CG2  1 
ATOM   7132  H  H    . VAL   A  1  475 ? 55.851  22.394  -10.430  1.00 121.63 ? 475  VAL   A H    1 
ATOM   7133  H  HA   . VAL   A  1  475 ? 56.012  19.712  -10.840  1.00 118.12 ? 475  VAL   A HA   1 
ATOM   7134  H  HB   . VAL   A  1  475 ? 53.778  21.149  -9.860   1.00 114.74 ? 475  VAL   A HB   1 
ATOM   7135  H  HG11 . VAL   A  1  475 ? 52.604  19.109  -9.821   1.00 112.54 ? 475  VAL   A HG11 1 
ATOM   7136  H  HG12 . VAL   A  1  475 ? 52.958  19.557  -11.303  1.00 112.54 ? 475  VAL   A HG12 1 
ATOM   7137  H  HG13 . VAL   A  1  475 ? 53.815  18.426  -10.589  1.00 112.54 ? 475  VAL   A HG13 1 
ATOM   7138  H  HG21 . VAL   A  1  475 ? 53.954  19.784  -7.949   1.00 112.78 ? 475  VAL   A HG21 1 
ATOM   7139  H  HG22 . VAL   A  1  475 ? 55.283  19.153  -8.549   1.00 112.78 ? 475  VAL   A HG22 1 
ATOM   7140  H  HG23 . VAL   A  1  475 ? 55.247  20.688  -8.140   1.00 112.78 ? 475  VAL   A HG23 1 
ATOM   7141  N  N    . ARG   A  1  476 ? 55.136  19.780  -13.132  1.00 100.36 ? 476  ARG   A N    1 
ATOM   7142  C  CA   . ARG   A  1  476 ? 54.728  19.853  -14.531  1.00 104.65 ? 476  ARG   A CA   1 
ATOM   7143  C  C    . ARG   A  1  476 ? 53.690  18.770  -14.788  1.00 101.81 ? 476  ARG   A C    1 
ATOM   7144  O  O    . ARG   A  1  476 ? 53.983  17.580  -14.627  1.00 96.51  ? 476  ARG   A O    1 
ATOM   7145  C  CB   . ARG   A  1  476 ? 55.932  19.671  -15.458  1.00 111.91 ? 476  ARG   A CB   1 
ATOM   7146  C  CG   . ARG   A  1  476 ? 55.642  19.913  -16.928  1.00 116.86 ? 476  ARG   A CG   1 
ATOM   7147  C  CD   . ARG   A  1  476 ? 56.936  19.866  -17.725  1.00 121.99 ? 476  ARG   A CD   1 
ATOM   7148  N  NE   . ARG   A  1  476 ? 56.734  20.167  -19.141  1.00 127.24 ? 476  ARG   A NE   1 
ATOM   7149  C  CZ   . ARG   A  1  476 ? 56.863  19.288  -20.135  1.00 132.76 ? 476  ARG   A CZ   1 
ATOM   7150  N  NH1  . ARG   A  1  476 ? 57.207  18.030  -19.891  1.00 132.71 ? 476  ARG   A NH1  1 
ATOM   7151  N  NH2  . ARG   A  1  476 ? 56.658  19.673  -21.388  1.00 139.42 ? 476  ARG   A NH2  1 
ATOM   7152  H  H    . ARG   A  1  476 ? 55.466  19.015  -12.919  1.00 120.47 ? 476  ARG   A H    1 
ATOM   7153  H  HA   . ARG   A  1  476 ? 54.327  20.717  -14.712  1.00 125.62 ? 476  ARG   A HA   1 
ATOM   7154  H  HB2  . ARG   A  1  476 ? 56.624  20.296  -15.191  1.00 134.33 ? 476  ARG   A HB2  1 
ATOM   7155  H  HB3  . ARG   A  1  476 ? 56.254  18.761  -15.370  1.00 134.33 ? 476  ARG   A HB3  1 
ATOM   7156  H  HG2  . ARG   A  1  476 ? 55.045  19.224  -17.261  1.00 140.27 ? 476  ARG   A HG2  1 
ATOM   7157  H  HG3  . ARG   A  1  476 ? 55.236  20.786  -17.042  1.00 140.27 ? 476  ARG   A HG3  1 
ATOM   7158  H  HD2  . ARG   A  1  476 ? 57.554  20.520  -17.363  1.00 146.43 ? 476  ARG   A HD2  1 
ATOM   7159  H  HD3  . ARG   A  1  476 ? 57.317  18.976  -17.658  1.00 146.43 ? 476  ARG   A HD3  1 
ATOM   7160  H  HE   . ARG   A  1  476 ? 56.516  20.973  -19.349  1.00 152.72 ? 476  ARG   A HE   1 
ATOM   7161  H  HH11 . ARG   A  1  476 ? 57.349  17.772  -19.083  1.00 159.28 ? 476  ARG   A HH11 1 
ATOM   7162  H  HH12 . ARG   A  1  476 ? 57.287  17.472  -20.541  1.00 159.28 ? 476  ARG   A HH12 1 
ATOM   7163  H  HH21 . ARG   A  1  476 ? 56.442  20.488  -21.557  1.00 167.34 ? 476  ARG   A HH21 1 
ATOM   7164  H  HH22 . ARG   A  1  476 ? 56.740  19.108  -22.031  1.00 167.34 ? 476  ARG   A HH22 1 
ATOM   7165  N  N    . PHE   A  1  477 ? 52.485  19.172  -15.192  1.00 105.66 ? 477  PHE   A N    1 
ATOM   7166  C  CA   . PHE   A  1  477 ? 51.374  18.243  -15.378  1.00 106.09 ? 477  PHE   A CA   1 
ATOM   7167  C  C    . PHE   A  1  477 ? 50.911  18.270  -16.833  1.00 106.52 ? 477  PHE   A C    1 
ATOM   7168  O  O    . PHE   A  1  477 ? 50.706  19.347  -17.402  1.00 109.32 ? 477  PHE   A O    1 
ATOM   7169  C  CB   . PHE   A  1  477 ? 50.228  18.576  -14.394  1.00 106.28 ? 477  PHE   A CB   1 
ATOM   7170  C  CG   . PHE   A  1  477 ? 49.337  19.709  -14.829  1.00 107.56 ? 477  PHE   A CG   1 
ATOM   7171  C  CD1  . PHE   A  1  477 ? 49.426  20.961  -14.240  1.00 108.67 ? 477  PHE   A CD1  1 
ATOM   7172  C  CD2  . PHE   A  1  477 ? 48.388  19.509  -15.806  1.00 109.38 ? 477  PHE   A CD2  1 
ATOM   7173  C  CE1  . PHE   A  1  477 ? 48.594  21.991  -14.648  1.00 113.60 ? 477  PHE   A CE1  1 
ATOM   7174  C  CE2  . PHE   A  1  477 ? 47.576  20.524  -16.213  1.00 114.35 ? 477  PHE   A CE2  1 
ATOM   7175  C  CZ   . PHE   A  1  477 ? 47.669  21.765  -15.636  1.00 116.50 ? 477  PHE   A CZ   1 
ATOM   7176  H  H    . PHE   A  1  477 ? 52.286  19.991  -15.366  1.00 126.83 ? 477  PHE   A H    1 
ATOM   7177  H  HA   . PHE   A  1  477 ? 51.661  17.334  -15.202  1.00 127.35 ? 477  PHE   A HA   1 
ATOM   7178  H  HB2  . PHE   A  1  477 ? 49.670  17.789  -14.292  1.00 127.57 ? 477  PHE   A HB2  1 
ATOM   7179  H  HB3  . PHE   A  1  477 ? 50.616  18.821  -13.540  1.00 127.57 ? 477  PHE   A HB3  1 
ATOM   7180  H  HD1  . PHE   A  1  477 ? 50.049  21.111  -13.566  1.00 130.44 ? 477  PHE   A HD1  1 
ATOM   7181  H  HD2  . PHE   A  1  477 ? 48.301  18.669  -16.195  1.00 131.29 ? 477  PHE   A HD2  1 
ATOM   7182  H  HE1  . PHE   A  1  477 ? 48.662  22.831  -14.255  1.00 136.36 ? 477  PHE   A HE1  1 
ATOM   7183  H  HE2  . PHE   A  1  477 ? 46.953  20.374  -16.887  1.00 137.26 ? 477  PHE   A HE2  1 
ATOM   7184  H  HZ   . PHE   A  1  477 ? 47.107  22.451  -15.915  1.00 139.84 ? 477  PHE   A HZ   1 
ATOM   7185  N  N    . CYS   A  1  478 ? 50.752  17.083  -17.437  1.00 105.07 ? 478  CYS   A N    1 
ATOM   7186  C  CA   . CYS   A  1  478 ? 50.348  16.985  -18.836  1.00 105.72 ? 478  CYS   A CA   1 
ATOM   7187  C  C    . CYS   A  1  478 ? 49.301  15.898  -19.053  1.00 104.25 ? 478  CYS   A C    1 
ATOM   7188  O  O    . CYS   A  1  478 ? 49.308  14.857  -18.389  1.00 103.66 ? 478  CYS   A O    1 
ATOM   7189  C  CB   . CYS   A  1  478 ? 51.527  16.667  -19.762  1.00 107.05 ? 478  CYS   A CB   1 
ATOM   7190  S  SG   . CYS   A  1  478 ? 53.090  17.426  -19.329  1.00 116.92 ? 478  CYS   A SG   1 
ATOM   7191  H  H    . CYS   A  1  478 ? 50.873  16.324  -17.052  1.00 126.12 ? 478  CYS   A H    1 
ATOM   7192  H  HA   . CYS   A  1  478 ? 49.956  17.842  -19.065  1.00 126.90 ? 478  CYS   A HA   1 
ATOM   7193  H  HB2  . CYS   A  1  478 ? 51.664  15.707  -19.759  1.00 128.50 ? 478  CYS   A HB2  1 
ATOM   7194  H  HB3  . CYS   A  1  478 ? 51.301  16.967  -20.656  1.00 128.50 ? 478  CYS   A HB3  1 
ATOM   7195  N  N    . LEU   A  1  479 ? 48.426  16.144  -20.037  1.00 101.87 ? 479  LEU   A N    1 
ATOM   7196  C  CA   . LEU   A  1  479 ? 47.421  15.192  -20.497  1.00 98.89  ? 479  LEU   A CA   1 
ATOM   7197  C  C    . LEU   A  1  479 ? 47.439  15.103  -22.021  1.00 96.99  ? 479  LEU   A C    1 
ATOM   7198  O  O    . LEU   A  1  479 ? 47.702  16.089  -22.716  1.00 98.07  ? 479  LEU   A O    1 
ATOM   7199  C  CB   . LEU   A  1  479 ? 46.002  15.591  -20.039  1.00 99.99  ? 479  LEU   A CB   1 
ATOM   7200  C  CG   . LEU   A  1  479 ? 45.317  14.812  -18.913  1.00 99.05  ? 479  LEU   A CG   1 
ATOM   7201  C  CD1  . LEU   A  1  479 ? 46.237  14.640  -17.738  1.00 98.72  ? 479  LEU   A CD1  1 
ATOM   7202  C  CD2  . LEU   A  1  479 ? 44.061  15.544  -18.480  1.00 97.81  ? 479  LEU   A CD2  1 
ATOM   7203  H  H    . LEU   A  1  479 ? 48.398  16.888  -20.468  1.00 122.28 ? 479  LEU   A H    1 
ATOM   7204  H  HA   . LEU   A  1  479 ? 47.634  14.318  -20.134  1.00 118.71 ? 479  LEU   A HA   1 
ATOM   7205  H  HB2  . LEU   A  1  479 ? 46.045  16.514  -19.742  1.00 120.02 ? 479  LEU   A HB2  1 
ATOM   7206  H  HB3  . LEU   A  1  479 ? 45.420  15.518  -20.811  1.00 120.02 ? 479  LEU   A HB3  1 
ATOM   7207  H  HG   . LEU   A  1  479 ? 45.080  13.929  -19.238  1.00 118.90 ? 479  LEU   A HG   1 
ATOM   7208  H  HD11 . LEU   A  1  479 ? 45.710  14.424  -16.953  1.00 118.50 ? 479  LEU   A HD11 1 
ATOM   7209  H  HD12 . LEU   A  1  479 ? 46.859  13.920  -17.927  1.00 118.50 ? 479  LEU   A HD12 1 
ATOM   7210  H  HD13 . LEU   A  1  479 ? 46.723  15.467  -17.594  1.00 118.50 ? 479  LEU   A HD13 1 
ATOM   7211  H  HD21 . LEU   A  1  479 ? 43.368  14.893  -18.286  1.00 117.41 ? 479  LEU   A HD21 1 
ATOM   7212  H  HD22 . LEU   A  1  479 ? 44.258  16.064  -17.685  1.00 117.41 ? 479  LEU   A HD22 1 
ATOM   7213  H  HD23 . LEU   A  1  479 ? 43.774  16.130  -19.197  1.00 117.41 ? 479  LEU   A HD23 1 
ATOM   7214  N  N    . LYS   A  1  480 ? 47.143  13.906  -22.534  1.00 95.06  ? 480  LYS   A N    1 
ATOM   7215  C  CA   . LYS   A  1  480 ? 47.019  13.641  -23.964  1.00 91.99  ? 480  LYS   A CA   1 
ATOM   7216  C  C    . LYS   A  1  480 ? 45.872  12.659  -24.158  1.00 90.20  ? 480  LYS   A C    1 
ATOM   7217  O  O    . LYS   A  1  480 ? 45.706  11.741  -23.352  1.00 90.26  ? 480  LYS   A O    1 
ATOM   7218  C  CB   . LYS   A  1  480 ? 48.320  13.063  -24.539  1.00 90.60  ? 480  LYS   A CB   1 
ATOM   7219  C  CG   . LYS   A  1  480 ? 48.332  12.865  -26.047  1.00 94.31  ? 480  LYS   A CG   1 
ATOM   7220  C  CD   . LYS   A  1  480 ? 49.531  12.022  -26.465  1.00 97.13  ? 480  LYS   A CD   1 
ATOM   7221  C  CE   . LYS   A  1  480 ? 49.486  11.652  -27.939  1.00 100.65 ? 480  LYS   A CE   1 
ATOM   7222  N  NZ   . LYS   A  1  480 ? 50.628  10.775  -28.328  1.00 104.03 ? 480  LYS   A NZ   1 
ATOM   7223  H  H    . LYS   A  1  480 ? 47.005  13.207  -22.053  1.00 114.11 ? 480  LYS   A H    1 
ATOM   7224  H  HA   . LYS   A  1  480 ? 46.821  14.457  -24.450  1.00 110.42 ? 480  LYS   A HA   1 
ATOM   7225  H  HB2  . LYS   A  1  480 ? 49.046  13.667  -24.320  1.00 108.75 ? 480  LYS   A HB2  1 
ATOM   7226  H  HB3  . LYS   A  1  480 ? 48.475  12.196  -24.131  1.00 108.75 ? 480  LYS   A HB3  1 
ATOM   7227  H  HG2  . LYS   A  1  480 ? 47.522  12.408  -26.322  1.00 113.21 ? 480  LYS   A HG2  1 
ATOM   7228  H  HG3  . LYS   A  1  480 ? 48.392  13.727  -26.488  1.00 113.21 ? 480  LYS   A HG3  1 
ATOM   7229  H  HD2  . LYS   A  1  480 ? 50.345  12.524  -26.305  1.00 116.59 ? 480  LYS   A HD2  1 
ATOM   7230  H  HD3  . LYS   A  1  480 ? 49.540  11.201  -25.948  1.00 116.59 ? 480  LYS   A HD3  1 
ATOM   7231  H  HE2  . LYS   A  1  480 ? 48.661  11.176  -28.124  1.00 120.82 ? 480  LYS   A HE2  1 
ATOM   7232  H  HE3  . LYS   A  1  480 ? 49.528  12.461  -28.473  1.00 120.82 ? 480  LYS   A HE3  1 
ATOM   7233  H  HZ1  . LYS   A  1  480 ? 50.588  10.591  -29.198  1.00 124.87 ? 480  LYS   A HZ1  1 
ATOM   7234  H  HZ2  . LYS   A  1  480 ? 51.399  11.185  -28.155  1.00 124.87 ? 480  LYS   A HZ2  1 
ATOM   7235  H  HZ3  . LYS   A  1  480 ? 50.597  10.013  -27.870  1.00 124.87 ? 480  LYS   A HZ3  1 
ATOM   7236  N  N    . ALA   A  1  481 ? 45.080  12.841  -25.216  1.00 90.99  ? 481  ALA   A N    1 
ATOM   7237  C  CA   . ALA   A  1  481 ? 43.895  12.009  -25.384  1.00 91.63  ? 481  ALA   A CA   1 
ATOM   7238  C  C    . ALA   A  1  481 ? 43.627  11.723  -26.854  1.00 96.48  ? 481  ALA   A C    1 
ATOM   7239  O  O    . ALA   A  1  481 ? 44.027  12.476  -27.746  1.00 100.16 ? 481  ALA   A O    1 
ATOM   7240  C  CB   . ALA   A  1  481 ? 42.661  12.664  -24.748  1.00 90.09  ? 481  ALA   A CB   1 
ATOM   7241  H  H    . ALA   A  1  481 ? 45.207  13.426  -25.834  1.00 109.22 ? 481  ALA   A H    1 
ATOM   7242  H  HA   . ALA   A  1  481 ? 44.070  11.157  -24.956  1.00 110.00 ? 481  ALA   A HA   1 
ATOM   7243  H  HB1  . ALA   A  1  481 ? 41.905  12.063  -24.835  1.00 108.14 ? 481  ALA   A HB1  1 
ATOM   7244  H  HB2  . ALA   A  1  481 ? 42.842  12.834  -23.810  1.00 108.14 ? 481  ALA   A HB2  1 
ATOM   7245  H  HB3  . ALA   A  1  481 ? 42.476  13.499  -25.205  1.00 108.14 ? 481  ALA   A HB3  1 
ATOM   7246  N  N    . ASP   A  1  482 ? 42.923  10.615  -27.084  1.00 96.70  ? 482  ASP   A N    1 
ATOM   7247  C  CA   . ASP   A  1  482 ? 42.536  10.162  -28.414  1.00 101.67 ? 482  ASP   A CA   1 
ATOM   7248  C  C    . ASP   A  1  482 ? 41.370  9.191   -28.245  1.00 100.99 ? 482  ASP   A C    1 
ATOM   7249  O  O    . ASP   A  1  482 ? 40.920  8.924   -27.127  1.00 98.30  ? 482  ASP   A O    1 
ATOM   7250  C  CB   . ASP   A  1  482 ? 43.718  9.510   -29.139  1.00 104.71 ? 482  ASP   A CB   1 
ATOM   7251  C  CG   . ASP   A  1  482 ? 43.506  9.415   -30.638  1.00 109.27 ? 482  ASP   A CG   1 
ATOM   7252  O  OD1  . ASP   A  1  482 ? 42.522  9.996   -31.142  1.00 110.73 ? 482  ASP   A OD1  1 
ATOM   7253  O  OD2  . ASP   A  1  482 ? 44.324  8.753   -31.312  1.00 111.66 ? 482  ASP   A OD2  1 
ATOM   7254  H  H    . ASP   A  1  482 ? 42.649  10.090  -26.460  1.00 116.08 ? 482  ASP   A H    1 
ATOM   7255  H  HA   . ASP   A  1  482 ? 42.239  10.917  -28.944  1.00 122.04 ? 482  ASP   A HA   1 
ATOM   7256  H  HB2  . ASP   A  1  482 ? 44.515  10.039  -28.982  1.00 125.69 ? 482  ASP   A HB2  1 
ATOM   7257  H  HB3  . ASP   A  1  482 ? 43.842  8.611   -28.796  1.00 125.69 ? 482  ASP   A HB3  1 
ATOM   7258  N  N    . GLY   A  1  483 ? 40.884  8.662   -29.360  1.00 103.32 ? 483  GLY   A N    1 
ATOM   7259  C  CA   . GLY   A  1  483 ? 39.806  7.698   -29.299  1.00 104.67 ? 483  GLY   A CA   1 
ATOM   7260  C  C    . GLY   A  1  483 ? 39.580  7.038   -30.640  1.00 111.02 ? 483  GLY   A C    1 
ATOM   7261  O  O    . GLY   A  1  483 ? 40.345  7.228   -31.587  1.00 115.05 ? 483  GLY   A O    1 
ATOM   7262  H  H    . GLY   A  1  483 ? 41.160  8.845   -30.154  1.00 124.02 ? 483  GLY   A H    1 
ATOM   7263  H  HA2  . GLY   A  1  483 ? 40.021  7.011   -28.649  1.00 125.64 ? 483  GLY   A HA2  1 
ATOM   7264  H  HA3  . GLY   A  1  483 ? 38.987  8.142   -29.031  1.00 125.64 ? 483  GLY   A HA3  1 
ATOM   7265  N  N    . LYS   A  1  484 ? 38.509  6.248   -30.701  1.00 114.71 ? 484  LYS   A N    1 
ATOM   7266  C  CA   . LYS   A  1  484 ? 38.090  5.562   -31.914  1.00 122.23 ? 484  LYS   A CA   1 
ATOM   7267  C  C    . LYS   A  1  484 ? 36.593  5.760   -32.103  1.00 124.59 ? 484  LYS   A C    1 
ATOM   7268  O  O    . LYS   A  1  484 ? 35.826  5.705   -31.138  1.00 124.56 ? 484  LYS   A O    1 
ATOM   7269  C  CB   . LYS   A  1  484 ? 38.408  4.059   -31.852  1.00 125.47 ? 484  LYS   A CB   1 
ATOM   7270  C  CG   . LYS   A  1  484 ? 39.892  3.726   -31.789  1.00 131.57 ? 484  LYS   A CG   1 
ATOM   7271  C  CD   . LYS   A  1  484 ? 40.114  2.222   -31.696  1.00 134.23 ? 484  LYS   A CD   1 
ATOM   7272  C  CE   . LYS   A  1  484 ? 41.592  1.868   -31.699  1.00 136.17 ? 484  LYS   A CE   1 
ATOM   7273  N  NZ   . LYS   A  1  484 ? 41.810  0.398   -31.595  1.00 139.36 ? 484  LYS   A NZ   1 
ATOM   7274  H  H    . LYS   A  1  484 ? 37.995  6.092   -30.030  1.00 137.69 ? 484  LYS   A H    1 
ATOM   7275  H  HA   . LYS   A  1  484 ? 38.555  5.936   -32.679  1.00 146.72 ? 484  LYS   A HA   1 
ATOM   7276  H  HB2  . LYS   A  1  484 ? 37.992  3.689   -31.058  1.00 150.60 ? 484  LYS   A HB2  1 
ATOM   7277  H  HB3  . LYS   A  1  484 ? 38.047  3.634   -32.645  1.00 150.60 ? 484  LYS   A HB3  1 
ATOM   7278  H  HG2  . LYS   A  1  484 ? 40.330  4.051   -32.592  1.00 157.92 ? 484  LYS   A HG2  1 
ATOM   7279  H  HG3  . LYS   A  1  484 ? 40.284  4.143   -31.006  1.00 157.92 ? 484  LYS   A HG3  1 
ATOM   7280  H  HD2  . LYS   A  1  484 ? 39.724  1.892   -30.871  1.00 161.12 ? 484  LYS   A HD2  1 
ATOM   7281  H  HD3  . LYS   A  1  484 ? 39.696  1.789   -32.456  1.00 161.12 ? 484  LYS   A HD3  1 
ATOM   7282  H  HE2  . LYS   A  1  484 ? 41.993  2.176   -32.527  1.00 163.44 ? 484  LYS   A HE2  1 
ATOM   7283  H  HE3  . LYS   A  1  484 ? 42.025  2.293   -30.942  1.00 163.44 ? 484  LYS   A HE3  1 
ATOM   7284  H  HZ1  . LYS   A  1  484 ? 42.318  0.215   -30.887  1.00 167.26 ? 484  LYS   A HZ1  1 
ATOM   7285  H  HZ2  . LYS   A  1  484 ? 41.030  -0.020  -31.506  1.00 167.26 ? 484  LYS   A HZ2  1 
ATOM   7286  H  HZ3  . LYS   A  1  484 ? 42.217  0.098   -32.327  1.00 167.26 ? 484  LYS   A HZ3  1 
ATOM   7287  N  N    . GLY   A  1  485 ? 36.186  5.996   -33.346  1.00 129.45 ? 485  GLY   A N    1 
ATOM   7288  C  CA   . GLY   A  1  485 ? 34.783  6.117   -33.676  1.00 133.90 ? 485  GLY   A CA   1 
ATOM   7289  C  C    . GLY   A  1  485 ? 34.306  7.548   -33.798  1.00 133.55 ? 485  GLY   A C    1 
ATOM   7290  O  O    . GLY   A  1  485 ? 35.077  8.476   -34.080  1.00 132.57 ? 485  GLY   A O    1 
ATOM   7291  H  H    . GLY   A  1  485 ? 36.712  6.091   -34.020  1.00 155.38 ? 485  GLY   A H    1 
ATOM   7292  H  HA2  . GLY   A  1  485 ? 34.619  5.673   -34.523  1.00 160.72 ? 485  GLY   A HA2  1 
ATOM   7293  H  HA3  . GLY   A  1  485 ? 34.258  5.684   -32.985  1.00 160.72 ? 485  GLY   A HA3  1 
ATOM   7294  N  N    . VAL   A  1  486 ? 33.009  7.727   -33.578  1.00 134.82 ? 486  VAL   A N    1 
ATOM   7295  C  CA   . VAL   A  1  486 ? 32.360  9.027   -33.708  1.00 140.31 ? 486  VAL   A CA   1 
ATOM   7296  C  C    . VAL   A  1  486 ? 32.678  9.847   -32.462  1.00 137.41 ? 486  VAL   A C    1 
ATOM   7297  O  O    . VAL   A  1  486 ? 32.180  9.551   -31.374  1.00 139.01 ? 486  VAL   A O    1 
ATOM   7298  C  CB   . VAL   A  1  486 ? 30.846  8.875   -33.900  1.00 144.82 ? 486  VAL   A CB   1 
ATOM   7299  C  CG1  . VAL   A  1  486 ? 30.132  10.199  -33.651  1.00 146.19 ? 486  VAL   A CG1  1 
ATOM   7300  C  CG2  . VAL   A  1  486 ? 30.534  8.355   -35.297  1.00 149.95 ? 486  VAL   A CG2  1 
ATOM   7301  H  H    . VAL   A  1  486 ? 32.471  7.098   -33.347  1.00 161.82 ? 486  VAL   A H    1 
ATOM   7302  H  HA   . VAL   A  1  486 ? 32.726  9.492   -34.478  1.00 168.41 ? 486  VAL   A HA   1 
ATOM   7303  H  HB   . VAL   A  1  486 ? 30.516  8.230   -33.255  1.00 173.82 ? 486  VAL   A HB   1 
ATOM   7304  H  HG11 . VAL   A  1  486 ? 29.205  10.114  -33.923  1.00 175.47 ? 486  VAL   A HG11 1 
ATOM   7305  H  HG12 . VAL   A  1  486 ? 30.181  10.411  -32.705  1.00 175.47 ? 486  VAL   A HG12 1 
ATOM   7306  H  HG13 . VAL   A  1  486 ? 30.567  10.894  -34.169  1.00 175.47 ? 486  VAL   A HG13 1 
ATOM   7307  H  HG21 . VAL   A  1  486 ? 29.577  8.218   -35.377  1.00 179.98 ? 486  VAL   A HG21 1 
ATOM   7308  H  HG22 . VAL   A  1  486 ? 30.830  9.008   -35.951  1.00 179.98 ? 486  VAL   A HG22 1 
ATOM   7309  H  HG23 . VAL   A  1  486 ? 31.001  7.516   -35.434  1.00 179.98 ? 486  VAL   A HG23 1 
ATOM   7310  N  N    . LEU   A  1  487 ? 33.494  10.887  -32.619  1.00 136.65 ? 487  LEU   A N    1 
ATOM   7311  C  CA   . LEU   A  1  487 ? 33.863  11.748  -31.503  1.00 133.05 ? 487  LEU   A CA   1 
ATOM   7312  C  C    . LEU   A  1  487 ? 34.189  13.141  -32.016  1.00 135.56 ? 487  LEU   A C    1 
ATOM   7313  O  O    . LEU   A  1  487 ? 34.600  13.292  -33.173  1.00 140.44 ? 487  LEU   A O    1 
ATOM   7314  C  CB   . LEU   A  1  487 ? 35.074  11.194  -30.739  1.00 126.80 ? 487  LEU   A CB   1 
ATOM   7315  C  CG   . LEU   A  1  487 ? 34.890  9.888   -29.970  1.00 127.57 ? 487  LEU   A CG   1 
ATOM   7316  C  CD1  . LEU   A  1  487 ? 36.222  9.439   -29.393  1.00 124.44 ? 487  LEU   A CD1  1 
ATOM   7317  C  CD2  . LEU   A  1  487 ? 33.857  10.066  -28.874  1.00 130.81 ? 487  LEU   A CD2  1 
ATOM   7318  H  H    . LEU   A  1  487 ? 33.849  11.115  -33.369  1.00 164.02 ? 487  LEU   A H    1 
ATOM   7319  H  HA   . LEU   A  1  487 ? 33.106  11.815  -30.901  1.00 159.70 ? 487  LEU   A HA   1 
ATOM   7320  H  HB2  . LEU   A  1  487 ? 35.785  11.043  -31.381  1.00 152.19 ? 487  LEU   A HB2  1 
ATOM   7321  H  HB3  . LEU   A  1  487 ? 35.347  11.863  -30.092  1.00 152.19 ? 487  LEU   A HB3  1 
ATOM   7322  H  HG   . LEU   A  1  487 ? 34.570  9.196   -30.569  1.00 153.12 ? 487  LEU   A HG   1 
ATOM   7323  H  HD11 . LEU   A  1  487 ? 36.061  8.758   -28.721  1.00 149.37 ? 487  LEU   A HD11 1 
ATOM   7324  H  HD12 . LEU   A  1  487 ? 36.769  9.076   -30.108  1.00 149.37 ? 487  LEU   A HD12 1 
ATOM   7325  H  HD13 . LEU   A  1  487 ? 36.666  10.202  -28.991  1.00 149.37 ? 487  LEU   A HD13 1 
ATOM   7326  H  HD21 . LEU   A  1  487 ? 34.060  9.458   -28.146  1.00 157.01 ? 487  LEU   A HD21 1 
ATOM   7327  H  HD22 . LEU   A  1  487 ? 33.888  10.983  -28.557  1.00 157.01 ? 487  LEU   A HD22 1 
ATOM   7328  H  HD23 . LEU   A  1  487 ? 32.978  9.870   -29.233  1.00 157.01 ? 487  LEU   A HD23 1 
ATOM   7329  N  N    . PRO   A  1  488 ? 34.032  14.168  -31.186  1.00 133.52 ? 488  PRO   A N    1 
ATOM   7330  C  CA   . PRO   A  1  488 ? 34.495  15.508  -31.557  1.00 133.56 ? 488  PRO   A CA   1 
ATOM   7331  C  C    . PRO   A  1  488 ? 36.004  15.628  -31.378  1.00 129.62 ? 488  PRO   A C    1 
ATOM   7332  O  O    . PRO   A  1  488 ? 36.654  14.790  -30.751  1.00 127.53 ? 488  PRO   A O    1 
ATOM   7333  C  CB   . PRO   A  1  488 ? 33.740  16.418  -30.584  1.00 137.14 ? 488  PRO   A CB   1 
ATOM   7334  C  CG   . PRO   A  1  488 ? 33.577  15.577  -29.362  1.00 134.86 ? 488  PRO   A CG   1 
ATOM   7335  C  CD   . PRO   A  1  488 ? 33.411  14.154  -29.847  1.00 133.00 ? 488  PRO   A CD   1 
ATOM   7336  H  HA   . PRO   A  1  488 ? 34.252  15.733  -32.468  1.00 160.31 ? 488  PRO   A HA   1 
ATOM   7337  H  HB2  . PRO   A  1  488 ? 34.262  17.213  -30.396  1.00 164.61 ? 488  PRO   A HB2  1 
ATOM   7338  H  HB3  . PRO   A  1  488 ? 32.880  16.667  -30.957  1.00 164.61 ? 488  PRO   A HB3  1 
ATOM   7339  H  HG2  . PRO   A  1  488 ? 34.365  15.658  -28.803  1.00 161.87 ? 488  PRO   A HG2  1 
ATOM   7340  H  HG3  . PRO   A  1  488 ? 32.791  15.865  -28.871  1.00 161.87 ? 488  PRO   A HG3  1 
ATOM   7341  H  HD2  . PRO   A  1  488 ? 33.872  13.535  -29.261  1.00 159.64 ? 488  PRO   A HD2  1 
ATOM   7342  H  HD3  . PRO   A  1  488 ? 32.471  13.919  -29.906  1.00 159.64 ? 488  PRO   A HD3  1 
ATOM   7343  N  N    . ARG   A  1  489 ? 36.558  16.699  -31.944  1.00 132.00 ? 489  ARG   A N    1 
ATOM   7344  C  CA   . ARG   A  1  489 ? 37.998  16.960  -31.901  1.00 130.36 ? 489  ARG   A CA   1 
ATOM   7345  C  C    . ARG   A  1  489 ? 38.361  17.998  -30.845  1.00 128.40 ? 489  ARG   A C    1 
ATOM   7346  O  O    . ARG   A  1  489 ? 39.204  18.869  -31.078  1.00 126.34 ? 489  ARG   A O    1 
ATOM   7347  C  CB   . ARG   A  1  489 ? 38.497  17.410  -33.269  1.00 134.80 ? 489  ARG   A CB   1 
ATOM   7348  C  CG   . ARG   A  1  489 ? 38.438  16.355  -34.362  1.00 137.94 ? 489  ARG   A CG   1 
ATOM   7349  C  CD   . ARG   A  1  489 ? 39.031  16.916  -35.645  1.00 144.07 ? 489  ARG   A CD   1 
ATOM   7350  N  NE   . ARG   A  1  489 ? 38.941  15.995  -36.773  1.00 146.97 ? 489  ARG   A NE   1 
ATOM   7351  C  CZ   . ARG   A  1  489 ? 39.300  16.305  -38.016  1.00 153.62 ? 489  ARG   A CZ   1 
ATOM   7352  N  NH1  . ARG   A  1  489 ? 39.770  17.514  -38.293  1.00 159.27 ? 489  ARG   A NH1  1 
ATOM   7353  N  NH2  . ARG   A  1  489 ? 39.185  15.407  -38.985  1.00 154.53 ? 489  ARG   A NH2  1 
ATOM   7354  H  H    . ARG   A  1  489 ? 36.113  17.301  -32.367  1.00 158.43 ? 489  ARG   A H    1 
ATOM   7355  H  HA   . ARG   A  1  489 ? 38.447  16.132  -31.671  1.00 156.47 ? 489  ARG   A HA   1 
ATOM   7356  H  HB2  . ARG   A  1  489 ? 37.955  18.159  -33.561  1.00 161.80 ? 489  ARG   A HB2  1 
ATOM   7357  H  HB3  . ARG   A  1  489 ? 39.423  17.684  -33.182  1.00 161.80 ? 489  ARG   A HB3  1 
ATOM   7358  H  HG2  . ARG   A  1  489 ? 38.950  15.576  -34.094  1.00 165.57 ? 489  ARG   A HG2  1 
ATOM   7359  H  HG3  . ARG   A  1  489 ? 37.515  16.105  -34.527  1.00 165.57 ? 489  ARG   A HG3  1 
ATOM   7360  H  HD2  . ARG   A  1  489 ? 38.554  17.726  -35.883  1.00 172.93 ? 489  ARG   A HD2  1 
ATOM   7361  H  HD3  . ARG   A  1  489 ? 39.969  17.114  -35.497  1.00 172.93 ? 489  ARG   A HD3  1 
ATOM   7362  H  HE   . ARG   A  1  489 ? 38.638  15.204  -36.626  1.00 176.40 ? 489  ARG   A HE   1 
ATOM   7363  H  HH11 . ARG   A  1  489 ? 39.845  18.101  -37.668  1.00 191.16 ? 489  ARG   A HH11 1 
ATOM   7364  H  HH12 . ARG   A  1  489 ? 40.002  17.712  -39.098  1.00 191.16 ? 489  ARG   A HH12 1 
ATOM   7365  H  HH21 . ARG   A  1  489 ? 38.879  14.623  -38.811  1.00 185.48 ? 489  ARG   A HH21 1 
ATOM   7366  H  HH22 . ARG   A  1  489 ? 39.418  15.609  -39.788  1.00 185.48 ? 489  ARG   A HH22 1 
ATOM   7367  N  N    . LYS   A  1  490 ? 37.741  17.923  -29.673  1.00 126.87 ? 490  LYS   A N    1 
ATOM   7368  C  CA   . LYS   A  1  490 ? 37.981  18.872  -28.596  1.00 126.60 ? 490  LYS   A CA   1 
ATOM   7369  C  C    . LYS   A  1  490 ? 37.280  18.343  -27.359  1.00 124.41 ? 490  LYS   A C    1 
ATOM   7370  O  O    . LYS   A  1  490 ? 36.146  17.866  -27.444  1.00 127.49 ? 490  LYS   A O    1 
ATOM   7371  C  CB   . LYS   A  1  490 ? 37.465  20.272  -28.959  1.00 131.77 ? 490  LYS   A CB   1 
ATOM   7372  C  CG   . LYS   A  1  490 ? 37.572  21.319  -27.852  1.00 130.63 ? 490  LYS   A CG   1 
ATOM   7373  C  CD   . LYS   A  1  490 ? 37.093  22.683  -28.350  1.00 133.89 ? 490  LYS   A CD   1 
ATOM   7374  C  CE   . LYS   A  1  490 ? 36.826  23.658  -27.213  1.00 135.82 ? 490  LYS   A CE   1 
ATOM   7375  N  NZ   . LYS   A  1  490 ? 35.646  23.260  -26.401  1.00 136.54 ? 490  LYS   A NZ   1 
ATOM   7376  H  H    . LYS   A  1  490 ? 37.163  17.318  -29.473  1.00 152.29 ? 490  LYS   A H    1 
ATOM   7377  H  HA   . LYS   A  1  490 ? 38.930  18.950  -28.413  1.00 151.96 ? 490  LYS   A HA   1 
ATOM   7378  H  HB2  . LYS   A  1  490 ? 37.977  20.599  -29.716  1.00 158.17 ? 490  LYS   A HB2  1 
ATOM   7379  H  HB3  . LYS   A  1  490 ? 36.528  20.200  -29.199  1.00 158.17 ? 490  LYS   A HB3  1 
ATOM   7380  H  HG2  . LYS   A  1  490 ? 37.019  21.054  -27.100  1.00 156.79 ? 490  LYS   A HG2  1 
ATOM   7381  H  HG3  . LYS   A  1  490 ? 38.497  21.401  -27.571  1.00 156.79 ? 490  LYS   A HG3  1 
ATOM   7382  H  HD2  . LYS   A  1  490 ? 37.774  23.068  -28.923  1.00 160.70 ? 490  LYS   A HD2  1 
ATOM   7383  H  HD3  . LYS   A  1  490 ? 36.268  22.567  -28.848  1.00 160.70 ? 490  LYS   A HD3  1 
ATOM   7384  H  HE2  . LYS   A  1  490 ? 37.599  23.686  -26.628  1.00 163.02 ? 490  LYS   A HE2  1 
ATOM   7385  H  HE3  . LYS   A  1  490 ? 36.656  24.539  -27.581  1.00 163.02 ? 490  LYS   A HE3  1 
ATOM   7386  H  HZ1  . LYS   A  1  490 ? 35.224  23.984  -26.103  1.00 163.89 ? 490  LYS   A HZ1  1 
ATOM   7387  H  HZ2  . LYS   A  1  490 ? 35.083  22.781  -26.897  1.00 163.89 ? 490  LYS   A HZ2  1 
ATOM   7388  H  HZ3  . LYS   A  1  490 ? 35.906  22.770  -25.705  1.00 163.89 ? 490  LYS   A HZ3  1 
ATOM   7389  N  N    . LEU   A  1  491 ? 37.960  18.421  -26.220  1.00 120.08 ? 491  LEU   A N    1 
ATOM   7390  C  CA   . LEU   A  1  491 ? 37.441  17.897  -24.967  1.00 114.28 ? 491  LEU   A CA   1 
ATOM   7391  C  C    . LEU   A  1  491 ? 37.850  18.822  -23.833  1.00 114.05 ? 491  LEU   A C    1 
ATOM   7392  O  O    . LEU   A  1  491 ? 38.967  19.350  -23.828  1.00 113.42 ? 491  LEU   A O    1 
ATOM   7393  C  CB   . LEU   A  1  491 ? 37.958  16.479  -24.693  1.00 107.60 ? 491  LEU   A CB   1 
ATOM   7394  C  CG   . LEU   A  1  491 ? 37.392  15.342  -25.543  1.00 108.42 ? 491  LEU   A CG   1 
ATOM   7395  C  CD1  . LEU   A  1  491 ? 38.512  14.402  -25.955  1.00 104.20 ? 491  LEU   A CD1  1 
ATOM   7396  C  CD2  . LEU   A  1  491 ? 36.324  14.592  -24.768  1.00 110.43 ? 491  LEU   A CD2  1 
ATOM   7397  H  H    . LEU   A  1  491 ? 38.739  18.779  -26.149  1.00 144.14 ? 491  LEU   A H    1 
ATOM   7398  H  HA   . LEU   A  1  491 ? 36.472  17.865  -25.004  1.00 137.17 ? 491  LEU   A HA   1 
ATOM   7399  H  HB2  . LEU   A  1  491 ? 38.918  16.482  -24.832  1.00 129.15 ? 491  LEU   A HB2  1 
ATOM   7400  H  HB3  . LEU   A  1  491 ? 37.757  16.264  -23.769  1.00 129.15 ? 491  LEU   A HB3  1 
ATOM   7401  H  HG   . LEU   A  1  491 ? 36.984  15.703  -26.345  1.00 130.14 ? 491  LEU   A HG   1 
ATOM   7402  H  HD11 . LEU   A  1  491 ? 38.136  13.671  -26.470  1.00 125.08 ? 491  LEU   A HD11 1 
ATOM   7403  H  HD12 . LEU   A  1  491 ? 39.152  14.892  -26.495  1.00 125.08 ? 491  LEU   A HD12 1 
ATOM   7404  H  HD13 . LEU   A  1  491 ? 38.945  14.058  -25.159  1.00 125.08 ? 491  LEU   A HD13 1 
ATOM   7405  H  HD21 . LEU   A  1  491 ? 35.962  13.888  -25.329  1.00 132.55 ? 491  LEU   A HD21 1 
ATOM   7406  H  HD22 . LEU   A  1  491 ? 36.722  14.208  -23.971  1.00 132.55 ? 491  LEU   A HD22 1 
ATOM   7407  H  HD23 . LEU   A  1  491 ? 35.620  15.212  -24.520  1.00 132.55 ? 491  LEU   A HD23 1 
ATOM   7408  N  N    . ASN   A  1  492 ? 36.947  19.011  -22.874  1.00 114.38 ? 492  ASN   A N    1 
ATOM   7409  C  CA   . ASN   A  1  492 ? 37.206  19.846  -21.708  1.00 115.13 ? 492  ASN   A CA   1 
ATOM   7410  C  C    . ASN   A  1  492 ? 37.558  18.948  -20.530  1.00 111.29 ? 492  ASN   A C    1 
ATOM   7411  O  O    . ASN   A  1  492 ? 36.736  18.132  -20.099  1.00 109.19 ? 492  ASN   A O    1 
ATOM   7412  C  CB   . ASN   A  1  492 ? 36.003  20.722  -21.357  1.00 120.47 ? 492  ASN   A CB   1 
ATOM   7413  C  CG   . ASN   A  1  492 ? 35.460  21.481  -22.549  1.00 126.55 ? 492  ASN   A CG   1 
ATOM   7414  O  OD1  . ASN   A  1  492 ? 34.249  21.685  -22.677  1.00 129.75 ? 492  ASN   A OD1  1 
ATOM   7415  N  ND2  . ASN   A  1  492 ? 36.353  21.890  -23.439  1.00 128.88 ? 492  ASN   A ND2  1 
ATOM   7416  H  H    . ASN   A  1  492 ? 36.162  18.658  -22.879  1.00 137.29 ? 492  ASN   A H    1 
ATOM   7417  H  HA   . ASN   A  1  492 ? 37.955  20.430  -21.903  1.00 138.20 ? 492  ASN   A HA   1 
ATOM   7418  H  HB2  . ASN   A  1  492 ? 35.292  20.158  -21.013  1.00 144.60 ? 492  ASN   A HB2  1 
ATOM   7419  H  HB3  . ASN   A  1  492 ? 36.268  21.369  -20.685  1.00 144.60 ? 492  ASN   A HB3  1 
ATOM   7420  H  HD21 . ASN   A  1  492 ? 36.097  22.326  -24.135  1.00 154.70 ? 492  ASN   A HD21 1 
ATOM   7421  H  HD22 . ASN   A  1  492 ? 37.187  21.720  -23.321  1.00 154.70 ? 492  ASN   A HD22 1 
ATOM   7422  N  N    . PHE   A  1  493 ? 38.769  19.109  -20.011  1.00 108.29 ? 493  PHE   A N    1 
ATOM   7423  C  CA   . PHE   A  1  493 ? 39.261  18.323  -18.892  1.00 104.61 ? 493  PHE   A CA   1 
ATOM   7424  C  C    . PHE   A  1  493 ? 39.359  19.188  -17.642  1.00 104.17 ? 493  PHE   A C    1 
ATOM   7425  O  O    . PHE   A  1  493 ? 39.634  20.390  -17.715  1.00 102.44 ? 493  PHE   A O    1 
ATOM   7426  C  CB   . PHE   A  1  493 ? 40.635  17.714  -19.196  1.00 101.13 ? 493  PHE   A CB   1 
ATOM   7427  C  CG   . PHE   A  1  493 ? 40.577  16.414  -19.946  1.00 96.39  ? 493  PHE   A CG   1 
ATOM   7428  C  CD1  . PHE   A  1  493 ? 40.554  16.398  -21.331  1.00 95.21  ? 493  PHE   A CD1  1 
ATOM   7429  C  CD2  . PHE   A  1  493 ? 40.563  15.208  -19.266  1.00 92.61  ? 493  PHE   A CD2  1 
ATOM   7430  C  CE1  . PHE   A  1  493 ? 40.508  15.202  -22.023  1.00 92.69  ? 493  PHE   A CE1  1 
ATOM   7431  C  CE2  . PHE   A  1  493 ? 40.520  14.009  -19.952  1.00 89.40  ? 493  PHE   A CE2  1 
ATOM   7432  C  CZ   . PHE   A  1  493 ? 40.491  14.006  -21.332  1.00 90.08  ? 493  PHE   A CZ   1 
ATOM   7433  H  H    . PHE   A  1  493 ? 39.339  19.684  -20.299  1.00 129.98 ? 493  PHE   A H    1 
ATOM   7434  H  HA   . PHE   A  1  493 ? 38.638  17.599  -18.719  1.00 125.57 ? 493  PHE   A HA   1 
ATOM   7435  H  HB2  . PHE   A  1  493 ? 41.141  18.343  -19.734  1.00 121.40 ? 493  PHE   A HB2  1 
ATOM   7436  H  HB3  . PHE   A  1  493 ? 41.095  17.550  -18.357  1.00 121.40 ? 493  PHE   A HB3  1 
ATOM   7437  H  HD1  . PHE   A  1  493 ? 40.570  17.201  -21.800  1.00 114.29 ? 493  PHE   A HD1  1 
ATOM   7438  H  HD2  . PHE   A  1  493 ? 40.584  15.204  -18.336  1.00 111.17 ? 493  PHE   A HD2  1 
ATOM   7439  H  HE1  . PHE   A  1  493 ? 40.490  15.203  -22.953  1.00 111.27 ? 493  PHE   A HE1  1 
ATOM   7440  H  HE2  . PHE   A  1  493 ? 40.511  13.206  -19.484  1.00 107.32 ? 493  PHE   A HE2  1 
ATOM   7441  H  HZ   . PHE   A  1  493 ? 40.459  13.201  -21.796  1.00 108.13 ? 493  PHE   A HZ   1 
ATOM   7442  N  N    . GLN   A  1  494 ? 39.133  18.560  -16.491  1.00 105.71 ? 494  GLN   A N    1 
ATOM   7443  C  CA   . GLN   A  1  494 ? 39.283  19.205  -15.191  1.00 108.39 ? 494  GLN   A CA   1 
ATOM   7444  C  C    . GLN   A  1  494 ? 40.381  18.474  -14.427  1.00 98.92  ? 494  GLN   A C    1 
ATOM   7445  O  O    . GLN   A  1  494 ? 40.190  17.329  -14.000  1.00 94.31  ? 494  GLN   A O    1 
ATOM   7446  C  CB   . GLN   A  1  494 ? 37.968  19.201  -14.411  1.00 117.60 ? 494  GLN   A CB   1 
ATOM   7447  C  CG   . GLN   A  1  494 ? 37.107  20.449  -14.615  1.00 127.36 ? 494  GLN   A CG   1 
ATOM   7448  C  CD   . GLN   A  1  494 ? 36.347  20.445  -15.929  1.00 131.70 ? 494  GLN   A CD   1 
ATOM   7449  O  OE1  . GLN   A  1  494 ? 35.537  19.555  -16.189  1.00 132.15 ? 494  GLN   A OE1  1 
ATOM   7450  N  NE2  . GLN   A  1  494 ? 36.600  21.449  -16.763  1.00 131.41 ? 494  GLN   A NE2  1 
ATOM   7451  H  H    . GLN   A  1  494 ? 38.884  17.738  -16.438  1.00 126.89 ? 494  GLN   A H    1 
ATOM   7452  H  HA   . GLN   A  1  494 ? 39.554  20.128  -15.316  1.00 130.11 ? 494  GLN   A HA   1 
ATOM   7453  H  HB2  . GLN   A  1  494 ? 37.444  18.434  -14.693  1.00 141.15 ? 494  GLN   A HB2  1 
ATOM   7454  H  HB3  . GLN   A  1  494 ? 38.169  19.135  -13.465  1.00 141.15 ? 494  GLN   A HB3  1 
ATOM   7455  H  HG2  . GLN   A  1  494 ? 36.458  20.503  -13.896  1.00 152.87 ? 494  GLN   A HG2  1 
ATOM   7456  H  HG3  . GLN   A  1  494 ? 37.680  21.231  -14.604  1.00 152.87 ? 494  GLN   A HG3  1 
ATOM   7457  H  HE21 . GLN   A  1  494 ? 37.169  22.056  -16.545  1.00 157.73 ? 494  GLN   A HE21 1 
ATOM   7458  H  HE22 . GLN   A  1  494 ? 36.195  21.492  -17.520  1.00 157.73 ? 494  GLN   A HE22 1 
ATOM   7459  N  N    . VAL   A  1  495 ? 41.526  19.133  -14.258  1.00 96.76  ? 495  VAL   A N    1 
ATOM   7460  C  CA   . VAL   A  1  495 ? 42.686  18.559  -13.586  1.00 92.74  ? 495  VAL   A CA   1 
ATOM   7461  C  C    . VAL   A  1  495 ? 42.818  19.190  -12.207  1.00 94.79  ? 495  VAL   A C    1 
ATOM   7462  O  O    . VAL   A  1  495 ? 42.602  20.396  -12.039  1.00 98.34  ? 495  VAL   A O    1 
ATOM   7463  C  CB   . VAL   A  1  495 ? 43.974  18.766  -14.407  1.00 88.42  ? 495  VAL   A CB   1 
ATOM   7464  C  CG1  . VAL   A  1  495 ? 45.195  18.288  -13.626  1.00 84.73  ? 495  VAL   A CG1  1 
ATOM   7465  C  CG2  . VAL   A  1  495 ? 43.878  18.039  -15.743  1.00 87.75  ? 495  VAL   A CG2  1 
ATOM   7466  H  H    . VAL   A  1  495 ? 41.656  19.938  -14.532  1.00 116.15 ? 495  VAL   A H    1 
ATOM   7467  H  HA   . VAL   A  1  495 ? 42.545  17.606  -13.473  1.00 111.32 ? 495  VAL   A HA   1 
ATOM   7468  H  HB   . VAL   A  1  495 ? 44.082  19.714  -14.583  1.00 106.14 ? 495  VAL   A HB   1 
ATOM   7469  H  HG11 . VAL   A  1  495 ? 45.985  18.392  -14.180  1.00 101.72 ? 495  VAL   A HG11 1 
ATOM   7470  H  HG12 . VAL   A  1  495 ? 45.284  18.822  -12.821  1.00 101.72 ? 495  VAL   A HG12 1 
ATOM   7471  H  HG13 . VAL   A  1  495 ? 45.075  17.355  -13.392  1.00 101.72 ? 495  VAL   A HG13 1 
ATOM   7472  H  HG21 . VAL   A  1  495 ? 44.698  18.182  -16.240  1.00 105.34 ? 495  VAL   A HG21 1 
ATOM   7473  H  HG22 . VAL   A  1  495 ? 43.752  17.091  -15.578  1.00 105.34 ? 495  VAL   A HG22 1 
ATOM   7474  H  HG23 . VAL   A  1  495 ? 43.124  18.391  -16.240  1.00 105.34 ? 495  VAL   A HG23 1 
ATOM   7475  N  N    . GLU   A  1  496 ? 43.182  18.370  -11.221  1.00 94.95  ? 496  GLU   A N    1 
ATOM   7476  C  CA   . GLU   A  1  496 ? 43.401  18.816  -9.852   1.00 98.94  ? 496  GLU   A CA   1 
ATOM   7477  C  C    . GLU   A  1  496 ? 44.715  18.248  -9.336   1.00 97.06  ? 496  GLU   A C    1 
ATOM   7478  O  O    . GLU   A  1  496 ? 45.011  17.066  -9.533   1.00 96.65  ? 496  GLU   A O    1 
ATOM   7479  C  CB   . GLU   A  1  496 ? 42.249  18.385  -8.928   1.00 104.17 ? 496  GLU   A CB   1 
ATOM   7480  C  CG   . GLU   A  1  496 ? 41.242  19.488  -8.627   1.00 108.68 ? 496  GLU   A CG   1 
ATOM   7481  C  CD   . GLU   A  1  496 ? 40.113  19.022  -7.726   1.00 114.20 ? 496  GLU   A CD   1 
ATOM   7482  O  OE1  . GLU   A  1  496 ? 40.278  17.986  -7.049   1.00 115.45 ? 496  GLU   A OE1  1 
ATOM   7483  O  OE2  . GLU   A  1  496 ? 39.060  19.693  -7.698   1.00 118.81 ? 496  GLU   A OE2  1 
ATOM   7484  H  H    . GLU   A  1  496 ? 43.311  17.526  -11.327  1.00 113.98 ? 496  GLU   A H    1 
ATOM   7485  H  HA   . GLU   A  1  496 ? 43.457  19.784  -9.835   1.00 118.76 ? 496  GLU   A HA   1 
ATOM   7486  H  HB2  . GLU   A  1  496 ? 41.769  17.656  -9.351   1.00 125.05 ? 496  GLU   A HB2  1 
ATOM   7487  H  HB3  . GLU   A  1  496 ? 42.624  18.091  -8.084   1.00 125.05 ? 496  GLU   A HB3  1 
ATOM   7488  H  HG2  . GLU   A  1  496 ? 41.698  20.220  -8.183   1.00 130.45 ? 496  GLU   A HG2  1 
ATOM   7489  H  HG3  . GLU   A  1  496 ? 40.852  19.797  -9.460   1.00 130.45 ? 496  GLU   A HG3  1 
ATOM   7490  N  N    . LEU   A  1  497 ? 45.502  19.099  -8.680   1.00 92.95  ? 497  LEU   A N    1 
ATOM   7491  C  CA   . LEU   A  1  497 ? 46.766  18.708  -8.071   1.00 92.84  ? 497  LEU   A CA   1 
ATOM   7492  C  C    . LEU   A  1  497 ? 46.694  18.917  -6.565   1.00 94.30  ? 497  LEU   A C    1 
ATOM   7493  O  O    . LEU   A  1  497 ? 46.086  19.882  -6.092   1.00 97.93  ? 497  LEU   A O    1 
ATOM   7494  C  CB   . LEU   A  1  497 ? 47.932  19.515  -8.646   1.00 94.89  ? 497  LEU   A CB   1 
ATOM   7495  C  CG   . LEU   A  1  497 ? 48.299  19.267  -10.107  1.00 96.81  ? 497  LEU   A CG   1 
ATOM   7496  C  CD1  . LEU   A  1  497 ? 49.238  20.356  -10.574  1.00 98.45  ? 497  LEU   A CD1  1 
ATOM   7497  C  CD2  . LEU   A  1  497 ? 48.940  17.905  -10.283  1.00 97.22  ? 497  LEU   A CD2  1 
ATOM   7498  H  H    . LEU   A  1  497 ? 45.317  19.932  -8.572   1.00 111.57 ? 497  LEU   A H    1 
ATOM   7499  H  HA   . LEU   A  1  497 ? 46.930  17.768  -8.246   1.00 111.45 ? 497  LEU   A HA   1 
ATOM   7500  H  HB2  . LEU   A  1  497 ? 47.711  20.456  -8.567   1.00 113.91 ? 497  LEU   A HB2  1 
ATOM   7501  H  HB3  . LEU   A  1  497 ? 48.721  19.314  -8.119   1.00 113.91 ? 497  LEU   A HB3  1 
ATOM   7502  H  HG   . LEU   A  1  497 ? 47.496  19.281  -10.651  1.00 116.21 ? 497  LEU   A HG   1 
ATOM   7503  H  HD11 . LEU   A  1  497 ? 49.524  20.159  -11.480  1.00 118.18 ? 497  LEU   A HD11 1 
ATOM   7504  H  HD12 . LEU   A  1  497 ? 48.771  21.206  -10.551  1.00 118.18 ? 497  LEU   A HD12 1 
ATOM   7505  H  HD13 . LEU   A  1  497 ? 50.007  20.384  -9.983   1.00 118.18 ? 497  LEU   A HD13 1 
ATOM   7506  H  HD21 . LEU   A  1  497 ? 49.142  17.770  -11.222  1.00 116.70 ? 497  LEU   A HD21 1 
ATOM   7507  H  HD22 . LEU   A  1  497 ? 49.757  17.870  -9.761   1.00 116.70 ? 497  LEU   A HD22 1 
ATOM   7508  H  HD23 . LEU   A  1  497 ? 48.322  17.223  -9.976   1.00 116.70 ? 497  LEU   A HD23 1 
ATOM   7509  N  N    . LEU   A  1  498 ? 47.323  18.014  -5.815   1.00 91.52  ? 498  LEU   A N    1 
ATOM   7510  C  CA   . LEU   A  1  498 ? 47.329  18.083  -4.357   1.00 91.51  ? 498  LEU   A CA   1 
ATOM   7511  C  C    . LEU   A  1  498 ? 48.708  17.701  -3.845   1.00 89.40  ? 498  LEU   A C    1 
ATOM   7512  O  O    . LEU   A  1  498 ? 49.142  16.559  -4.022   1.00 87.55  ? 498  LEU   A O    1 
ATOM   7513  C  CB   . LEU   A  1  498 ? 46.261  17.162  -3.756   1.00 92.67  ? 498  LEU   A CB   1 
ATOM   7514  C  CG   . LEU   A  1  498 ? 46.323  16.977  -2.237   1.00 95.55  ? 498  LEU   A CG   1 
ATOM   7515  C  CD1  . LEU   A  1  498 ? 46.192  18.313  -1.516   1.00 99.79  ? 498  LEU   A CD1  1 
ATOM   7516  C  CD2  . LEU   A  1  498 ? 45.248  16.008  -1.773   1.00 94.09  ? 498  LEU   A CD2  1 
ATOM   7517  H  H    . LEU   A  1  498 ? 47.760  17.345  -6.132   1.00 109.87 ? 498  LEU   A H    1 
ATOM   7518  H  HA   . LEU   A  1  498 ? 47.144  18.995  -4.082   1.00 109.85 ? 498  LEU   A HA   1 
ATOM   7519  H  HB2  . LEU   A  1  498 ? 45.389  17.530  -3.967   1.00 111.24 ? 498  LEU   A HB2  1 
ATOM   7520  H  HB3  . LEU   A  1  498 ? 46.357  16.284  -4.158   1.00 111.24 ? 498  LEU   A HB3  1 
ATOM   7521  H  HG   . LEU   A  1  498 ? 47.187  16.603  -2.006   1.00 114.70 ? 498  LEU   A HG   1 
ATOM   7522  H  HD11 . LEU   A  1  498 ? 46.315  18.172  -0.564   1.00 119.79 ? 498  LEU   A HD11 1 
ATOM   7523  H  HD12 . LEU   A  1  498 ? 46.871  18.920  -1.851   1.00 119.79 ? 498  LEU   A HD12 1 
ATOM   7524  H  HD13 . LEU   A  1  498 ? 45.309  18.678  -1.685   1.00 119.79 ? 498  LEU   A HD13 1 
ATOM   7525  H  HD21 . LEU   A  1  498 ? 45.365  15.836  -0.826   1.00 112.95 ? 498  LEU   A HD21 1 
ATOM   7526  H  HD22 . LEU   A  1  498 ? 44.376  16.402  -1.933   1.00 112.95 ? 498  LEU   A HD22 1 
ATOM   7527  H  HD23 . LEU   A  1  498 ? 45.332  15.180  -2.272   1.00 112.95 ? 498  LEU   A HD23 1 
ATOM   7528  N  N    . LEU   A  1  499 ? 49.386  18.649  -3.202   1.00 91.74  ? 499  LEU   A N    1 
ATOM   7529  C  CA   . LEU   A  1  499 ? 50.700  18.389  -2.631   1.00 92.04  ? 499  LEU   A CA   1 
ATOM   7530  C  C    . LEU   A  1  499 ? 50.570  17.667  -1.294   1.00 94.95  ? 499  LEU   A C    1 
ATOM   7531  O  O    . LEU   A  1  499 ? 49.639  17.916  -0.522   1.00 93.50  ? 499  LEU   A O    1 
ATOM   7532  C  CB   . LEU   A  1  499 ? 51.470  19.697  -2.440   1.00 90.92  ? 499  LEU   A CB   1 
ATOM   7533  C  CG   . LEU   A  1  499 ? 51.562  20.608  -3.666   1.00 91.40  ? 499  LEU   A CG   1 
ATOM   7534  C  CD1  . LEU   A  1  499 ? 52.155  21.963  -3.299   1.00 95.01  ? 499  LEU   A CD1  1 
ATOM   7535  C  CD2  . LEU   A  1  499 ? 52.374  19.955  -4.776   1.00 89.57  ? 499  LEU   A CD2  1 
ATOM   7536  H  H    . LEU   A  1  499 ? 49.104  19.453  -3.083   1.00 110.12 ? 499  LEU   A H    1 
ATOM   7537  H  HA   . LEU   A  1  499 ? 51.204  17.823  -3.236   1.00 110.49 ? 499  LEU   A HA   1 
ATOM   7538  H  HB2  . LEU   A  1  499 ? 51.034  20.204  -1.737   1.00 109.14 ? 499  LEU   A HB2  1 
ATOM   7539  H  HB3  . LEU   A  1  499 ? 52.377  19.477  -2.176   1.00 109.14 ? 499  LEU   A HB3  1 
ATOM   7540  H  HG   . LEU   A  1  499 ? 50.664  20.755  -4.001   1.00 109.72 ? 499  LEU   A HG   1 
ATOM   7541  H  HD11 . LEU   A  1  499 ? 52.273  22.485  -4.108   1.00 114.05 ? 499  LEU   A HD11 1 
ATOM   7542  H  HD12 . LEU   A  1  499 ? 51.549  22.420  -2.696   1.00 114.05 ? 499  LEU   A HD12 1 
ATOM   7543  H  HD13 . LEU   A  1  499 ? 53.012  21.825  -2.866   1.00 114.05 ? 499  LEU   A HD13 1 
ATOM   7544  H  HD21 . LEU   A  1  499 ? 52.490  20.591  -5.499   1.00 107.52 ? 499  LEU   A HD21 1 
ATOM   7545  H  HD22 . LEU   A  1  499 ? 53.239  19.695  -4.423   1.00 107.52 ? 499  LEU   A HD22 1 
ATOM   7546  H  HD23 . LEU   A  1  499 ? 51.899  19.172  -5.097   1.00 107.52 ? 499  LEU   A HD23 1 
ATOM   7547  N  N    . ASP   A  1  500 ? 51.518  16.770  -1.028   1.00 99.15  ? 500  ASP   A N    1 
ATOM   7548  C  CA   . ASP   A  1  500 ? 51.587  16.029  0.231    1.00 104.70 ? 500  ASP   A CA   1 
ATOM   7549  C  C    . ASP   A  1  500 ? 50.270  15.313  0.526    1.00 108.27 ? 500  ASP   A C    1 
ATOM   7550  O  O    . ASP   A  1  500 ? 49.668  15.475  1.590    1.00 110.85 ? 500  ASP   A O    1 
ATOM   7551  C  CB   . ASP   A  1  500 ? 51.971  16.956  1.388    1.00 107.50 ? 500  ASP   A CB   1 
ATOM   7552  C  CG   . ASP   A  1  500 ? 52.758  16.243  2.476    1.00 110.53 ? 500  ASP   A CG   1 
ATOM   7553  O  OD1  . ASP   A  1  500 ? 53.250  15.122  2.227    1.00 108.51 ? 500  ASP   A OD1  1 
ATOM   7554  O  OD2  . ASP   A  1  500 ? 52.885  16.803  3.585    1.00 111.90 ? 500  ASP   A OD2  1 
ATOM   7555  H  H    . ASP   A  1  500 ? 52.150  16.568  -1.575   1.00 119.02 ? 500  ASP   A H    1 
ATOM   7556  H  HA   . ASP   A  1  500 ? 52.275  15.350  0.144    1.00 125.68 ? 500  ASP   A HA   1 
ATOM   7557  H  HB2  . ASP   A  1  500 ? 52.520  17.679  1.045    1.00 129.04 ? 500  ASP   A HB2  1 
ATOM   7558  H  HB3  . ASP   A  1  500 ? 51.163  17.315  1.787    1.00 129.04 ? 500  ASP   A HB3  1 
ATOM   7559  N  N    . LYS   A  1  501 ? 49.822  14.496  -0.430   1.00 109.81 ? 501  LYS   A N    1 
ATOM   7560  C  CA   . LYS   A  1  501 ? 48.565  13.784  -0.232   1.00 112.23 ? 501  LYS   A CA   1 
ATOM   7561  C  C    . LYS   A  1  501 ? 48.675  12.728  0.862    1.00 114.66 ? 501  LYS   A C    1 
ATOM   7562  O  O    . LYS   A  1  501 ? 47.670  12.403  1.503    1.00 115.48 ? 501  LYS   A O    1 
ATOM   7563  C  CB   . LYS   A  1  501 ? 48.099  13.128  -1.532   1.00 111.93 ? 501  LYS   A CB   1 
ATOM   7564  C  CG   . LYS   A  1  501 ? 46.764  12.400  -1.379   1.00 115.06 ? 501  LYS   A CG   1 
ATOM   7565  C  CD   . LYS   A  1  501 ? 46.275  11.787  -2.679   1.00 116.35 ? 501  LYS   A CD   1 
ATOM   7566  C  CE   . LYS   A  1  501 ? 44.955  11.054  -2.473   1.00 122.82 ? 501  LYS   A CE   1 
ATOM   7567  N  NZ   . LYS   A  1  501 ? 44.445  10.437  -3.728   1.00 127.06 ? 501  LYS   A NZ   1 
ATOM   7568  H  H    . LYS   A  1  501 ? 50.216  14.342  -1.179   1.00 131.81 ? 501  LYS   A H    1 
ATOM   7569  H  HA   . LYS   A  1  501 ? 47.896  14.435  0.032    1.00 134.71 ? 501  LYS   A HA   1 
ATOM   7570  H  HB2  . LYS   A  1  501 ? 47.991  13.812  -2.211   1.00 134.35 ? 501  LYS   A HB2  1 
ATOM   7571  H  HB3  . LYS   A  1  501 ? 48.763  12.481  -1.816   1.00 134.35 ? 501  LYS   A HB3  1 
ATOM   7572  H  HG2  . LYS   A  1  501 ? 46.867  11.685  -0.732   1.00 138.11 ? 501  LYS   A HG2  1 
ATOM   7573  H  HG3  . LYS   A  1  501 ? 46.093  13.030  -1.075   1.00 138.11 ? 501  LYS   A HG3  1 
ATOM   7574  H  HD2  . LYS   A  1  501 ? 46.138  12.488  -3.335   1.00 139.66 ? 501  LYS   A HD2  1 
ATOM   7575  H  HD3  . LYS   A  1  501 ? 46.932  11.151  -3.004   1.00 139.66 ? 501  LYS   A HD3  1 
ATOM   7576  H  HE2  . LYS   A  1  501 ? 45.083  10.347  -1.821   1.00 147.42 ? 501  LYS   A HE2  1 
ATOM   7577  H  HE3  . LYS   A  1  501 ? 44.289  11.683  -2.154   1.00 147.42 ? 501  LYS   A HE3  1 
ATOM   7578  H  HZ1  . LYS   A  1  501 ? 43.838  9.816   -3.537   1.00 152.51 ? 501  LYS   A HZ1  1 
ATOM   7579  H  HZ2  . LYS   A  1  501 ? 44.070  11.059  -4.242   1.00 152.51 ? 501  LYS   A HZ2  1 
ATOM   7580  H  HZ3  . LYS   A  1  501 ? 45.115  10.059  -4.175   1.00 152.51 ? 501  LYS   A HZ3  1 
ATOM   7581  N  N    . LEU   A  1  502 ? 49.872  12.178  1.089    1.00 117.70 ? 502  LEU   A N    1 
ATOM   7582  C  CA   . LEU   A  1  502 ? 50.002  11.100  2.066    1.00 123.83 ? 502  LEU   A CA   1 
ATOM   7583  C  C    . LEU   A  1  502 ? 49.469  11.527  3.427    1.00 126.92 ? 502  LEU   A C    1 
ATOM   7584  O  O    . LEU   A  1  502 ? 48.774  10.756  4.100    1.00 127.30 ? 502  LEU   A O    1 
ATOM   7585  C  CB   . LEU   A  1  502 ? 51.459  10.649  2.181    1.00 126.54 ? 502  LEU   A CB   1 
ATOM   7586  C  CG   . LEU   A  1  502 ? 52.027  9.773   1.057    1.00 126.70 ? 502  LEU   A CG   1 
ATOM   7587  C  CD1  . LEU   A  1  502 ? 53.356  9.162   1.482    1.00 130.35 ? 502  LEU   A CD1  1 
ATOM   7588  C  CD2  . LEU   A  1  502 ? 51.054  8.677   0.621    1.00 125.06 ? 502  LEU   A CD2  1 
ATOM   7589  H  H    . LEU   A  1  502 ? 50.604  12.406  0.700    1.00 141.28 ? 502  LEU   A H    1 
ATOM   7590  H  HA   . LEU   A  1  502 ? 49.483  10.342  1.757    1.00 148.63 ? 502  LEU   A HA   1 
ATOM   7591  H  HB2  . LEU   A  1  502 ? 52.013  11.445  2.222    1.00 151.88 ? 502  LEU   A HB2  1 
ATOM   7592  H  HB3  . LEU   A  1  502 ? 51.547  10.141  3.003    1.00 151.88 ? 502  LEU   A HB3  1 
ATOM   7593  H  HG   . LEU   A  1  502 ? 52.171  10.342  0.284    1.00 152.08 ? 502  LEU   A HG   1 
ATOM   7594  H  HD11 . LEU   A  1  502 ? 53.830  8.857   0.693    1.00 156.46 ? 502  LEU   A HD11 1 
ATOM   7595  H  HD12 . LEU   A  1  502 ? 53.880  9.836   1.943    1.00 156.46 ? 502  LEU   A HD12 1 
ATOM   7596  H  HD13 . LEU   A  1  502 ? 53.184  8.414   2.075    1.00 156.46 ? 502  LEU   A HD13 1 
ATOM   7597  H  HD21 . LEU   A  1  502 ? 51.453  8.170   -0.103   1.00 150.11 ? 502  LEU   A HD21 1 
ATOM   7598  H  HD22 . LEU   A  1  502 ? 50.877  8.094   1.376    1.00 150.11 ? 502  LEU   A HD22 1 
ATOM   7599  H  HD23 . LEU   A  1  502 ? 50.229  9.089   0.321    1.00 150.11 ? 502  LEU   A HD23 1 
ATOM   7600  N  N    . LYS   A  1  503 ? 49.780  12.748  3.850    1.00 128.80 ? 503  LYS   A N    1 
ATOM   7601  C  CA   . LYS   A  1  503 ? 49.215  13.263  5.087    1.00 133.52 ? 503  LYS   A CA   1 
ATOM   7602  C  C    . LYS   A  1  503 ? 47.704  13.401  4.951    1.00 142.52 ? 503  LYS   A C    1 
ATOM   7603  O  O    . LYS   A  1  503 ? 47.194  13.879  3.934    1.00 145.26 ? 503  LYS   A O    1 
ATOM   7604  C  CB   . LYS   A  1  503 ? 49.851  14.607  5.435    1.00 127.80 ? 503  LYS   A CB   1 
ATOM   7605  C  CG   . LYS   A  1  503 ? 51.360  14.536  5.637    1.00 124.46 ? 503  LYS   A CG   1 
ATOM   7606  C  CD   . LYS   A  1  503 ? 51.731  13.453  6.638    1.00 126.12 ? 503  LYS   A CD   1 
ATOM   7607  C  CE   . LYS   A  1  503 ? 52.955  13.823  7.454    1.00 128.11 ? 503  LYS   A CE   1 
ATOM   7608  N  NZ   . LYS   A  1  503 ? 53.192  12.837  8.544    1.00 131.67 ? 503  LYS   A NZ   1 
ATOM   7609  H  H    . LYS   A  1  503 ? 50.308  13.290  3.442    1.00 154.60 ? 503  LYS   A H    1 
ATOM   7610  H  HA   . LYS   A  1  503 ? 49.401  12.651  5.817    1.00 160.26 ? 503  LYS   A HA   1 
ATOM   7611  H  HB2  . LYS   A  1  503 ? 49.678  15.231  4.712    1.00 153.40 ? 503  LYS   A HB2  1 
ATOM   7612  H  HB3  . LYS   A  1  503 ? 49.457  14.935  6.258    1.00 153.40 ? 503  LYS   A HB3  1 
ATOM   7613  H  HG2  . LYS   A  1  503 ? 51.790  14.332  4.791    1.00 149.39 ? 503  LYS   A HG2  1 
ATOM   7614  H  HG3  . LYS   A  1  503 ? 51.681  15.387  5.974    1.00 149.39 ? 503  LYS   A HG3  1 
ATOM   7615  H  HD2  . LYS   A  1  503 ? 50.990  13.316  7.249    1.00 151.39 ? 503  LYS   A HD2  1 
ATOM   7616  H  HD3  . LYS   A  1  503 ? 51.923  12.630  6.161    1.00 151.39 ? 503  LYS   A HD3  1 
ATOM   7617  H  HE2  . LYS   A  1  503 ? 53.735  13.836  6.877    1.00 153.77 ? 503  LYS   A HE2  1 
ATOM   7618  H  HE3  . LYS   A  1  503 ? 52.823  14.697  7.854    1.00 153.77 ? 503  LYS   A HE3  1 
ATOM   7619  H  HZ1  . LYS   A  1  503 ? 54.065  12.757  8.698    1.00 158.04 ? 503  LYS   A HZ1  1 
ATOM   7620  H  HZ2  . LYS   A  1  503 ? 52.790  13.107  9.291    1.00 158.04 ? 503  LYS   A HZ2  1 
ATOM   7621  H  HZ3  . LYS   A  1  503 ? 52.866  12.042  8.312    1.00 158.04 ? 503  LYS   A HZ3  1 
ATOM   7622  N  N    . GLN   A  1  504 ? 46.988  12.971  5.985    1.00 150.42 ? 504  GLN   A N    1 
ATOM   7623  C  CA   . GLN   A  1  504 ? 45.535  12.929  5.992    1.00 151.53 ? 504  GLN   A CA   1 
ATOM   7624  C  C    . GLN   A  1  504 ? 45.005  13.979  6.968    1.00 148.42 ? 504  GLN   A C    1 
ATOM   7625  O  O    . GLN   A  1  504 ? 45.754  14.828  7.464    1.00 147.31 ? 504  GLN   A O    1 
ATOM   7626  C  CB   . GLN   A  1  504 ? 45.074  11.508  6.330    1.00 156.95 ? 504  GLN   A CB   1 
ATOM   7627  C  CG   . GLN   A  1  504 ? 45.713  10.451  5.428    1.00 154.13 ? 504  GLN   A CG   1 
ATOM   7628  C  CD   . GLN   A  1  504 ? 44.953  9.138   5.405    1.00 157.44 ? 504  GLN   A CD   1 
ATOM   7629  O  OE1  . GLN   A  1  504 ? 44.583  8.600   6.448    1.00 162.24 ? 504  GLN   A OE1  1 
ATOM   7630  N  NE2  . GLN   A  1  504 ? 44.719  8.614   4.206    1.00 156.28 ? 504  GLN   A NE2  1 
ATOM   7631  H  H    . GLN   A  1  504 ? 47.337  12.689  6.718    1.00 180.55 ? 504  GLN   A H    1 
ATOM   7632  H  HA   . GLN   A  1  504 ? 45.192  13.149  5.112    1.00 181.87 ? 504  GLN   A HA   1 
ATOM   7633  H  HB2  . GLN   A  1  504 ? 45.316  11.307  7.248    1.00 188.38 ? 504  GLN   A HB2  1 
ATOM   7634  H  HB3  . GLN   A  1  504 ? 44.111  11.454  6.222    1.00 188.38 ? 504  GLN   A HB3  1 
ATOM   7635  H  HG2  . GLN   A  1  504 ? 45.745  10.791  4.521    1.00 184.99 ? 504  GLN   A HG2  1 
ATOM   7636  H  HG3  . GLN   A  1  504 ? 46.611  10.269  5.747    1.00 184.99 ? 504  GLN   A HG3  1 
ATOM   7637  H  HE21 . GLN   A  1  504 ? 44.994  9.019   3.498    1.00 187.57 ? 504  GLN   A HE21 1 
ATOM   7638  H  HE22 . GLN   A  1  504 ? 44.292  7.871   4.137    1.00 187.57 ? 504  GLN   A HE22 1 
ATOM   7639  N  N    . LYS   A  1  505 ? 43.699  13.935  7.235    1.00 143.99 ? 505  LYS   A N    1 
ATOM   7640  C  CA   . LYS   A  1  505 ? 43.098  14.917  8.129    1.00 143.59 ? 505  LYS   A CA   1 
ATOM   7641  C  C    . LYS   A  1  505 ? 43.830  14.931  9.466    1.00 142.88 ? 505  LYS   A C    1 
ATOM   7642  O  O    . LYS   A  1  505 ? 44.170  13.881  10.018   1.00 138.10 ? 505  LYS   A O    1 
ATOM   7643  C  CB   . LYS   A  1  505 ? 41.614  14.617  8.357    1.00 147.26 ? 505  LYS   A CB   1 
ATOM   7644  C  CG   . LYS   A  1  505 ? 40.720  14.774  7.134    1.00 144.84 ? 505  LYS   A CG   1 
ATOM   7645  C  CD   . LYS   A  1  505 ? 39.298  15.139  7.554    1.00 148.89 ? 505  LYS   A CD   1 
ATOM   7646  C  CE   . LYS   A  1  505 ? 38.255  14.652  6.560    1.00 148.17 ? 505  LYS   A CE   1 
ATOM   7647  N  NZ   . LYS   A  1  505 ? 37.881  13.229  6.798    1.00 149.72 ? 505  LYS   A NZ   1 
ATOM   7648  H  H    . LYS   A  1  505 ? 43.150  13.356  6.915    1.00 172.83 ? 505  LYS   A H    1 
ATOM   7649  H  HA   . LYS   A  1  505 ? 43.165  15.794  7.720    1.00 172.35 ? 505  LYS   A HA   1 
ATOM   7650  H  HB2  . LYS   A  1  505 ? 41.532  13.700  8.660    1.00 176.75 ? 505  LYS   A HB2  1 
ATOM   7651  H  HB3  . LYS   A  1  505 ? 41.282  15.223  9.037    1.00 176.75 ? 505  LYS   A HB3  1 
ATOM   7652  H  HG2  . LYS   A  1  505 ? 41.065  15.481  6.567    1.00 173.84 ? 505  LYS   A HG2  1 
ATOM   7653  H  HG3  . LYS   A  1  505 ? 40.692  13.938  6.643    1.00 173.84 ? 505  LYS   A HG3  1 
ATOM   7654  H  HD2  . LYS   A  1  505 ? 39.106  14.733  8.414    1.00 178.71 ? 505  LYS   A HD2  1 
ATOM   7655  H  HD3  . LYS   A  1  505 ? 39.223  16.104  7.620    1.00 178.71 ? 505  LYS   A HD3  1 
ATOM   7656  H  HE2  . LYS   A  1  505 ? 37.455  15.194  6.644    1.00 177.84 ? 505  LYS   A HE2  1 
ATOM   7657  H  HE3  . LYS   A  1  505 ? 38.612  14.725  5.661    1.00 177.84 ? 505  LYS   A HE3  1 
ATOM   7658  H  HZ1  . LYS   A  1  505 ? 37.250  12.980  6.222    1.00 179.70 ? 505  LYS   A HZ1  1 
ATOM   7659  H  HZ2  . LYS   A  1  505 ? 38.592  12.705  6.692    1.00 179.70 ? 505  LYS   A HZ2  1 
ATOM   7660  H  HZ3  . LYS   A  1  505 ? 37.571  13.130  7.627    1.00 179.70 ? 505  LYS   A HZ3  1 
ATOM   7661  N  N    . GLY   A  1  506 ? 44.069  16.132  9.987    1.00 144.24 ? 506  GLY   A N    1 
ATOM   7662  C  CA   . GLY   A  1  506 ? 44.770  16.283  11.244   1.00 147.19 ? 506  GLY   A CA   1 
ATOM   7663  C  C    . GLY   A  1  506 ? 46.274  16.179  11.155   1.00 140.91 ? 506  GLY   A C    1 
ATOM   7664  O  O    . GLY   A  1  506 ? 46.933  16.075  12.196   1.00 142.68 ? 506  GLY   A O    1 
ATOM   7665  H  H    . GLY   A  1  506 ? 43.831  16.875  9.624    1.00 173.13 ? 506  GLY   A H    1 
ATOM   7666  H  HA2  . GLY   A  1  506 ? 44.556  17.153  11.615   1.00 176.66 ? 506  GLY   A HA2  1 
ATOM   7667  H  HA3  . GLY   A  1  506 ? 44.462  15.595  11.854   1.00 176.66 ? 506  GLY   A HA3  1 
ATOM   7668  N  N    . ALA   A  1  507 ? 46.843  16.206  9.950    1.00 132.79 ? 507  ALA   A N    1 
ATOM   7669  C  CA   . ALA   A  1  507 ? 48.280  16.073  9.753    1.00 127.43 ? 507  ALA   A CA   1 
ATOM   7670  C  C    . ALA   A  1  507 ? 48.773  17.180  8.833    1.00 123.45 ? 507  ALA   A C    1 
ATOM   7671  O  O    . ALA   A  1  507 ? 48.093  17.552  7.872    1.00 119.01 ? 507  ALA   A O    1 
ATOM   7672  C  CB   . ALA   A  1  507 ? 48.633  14.700  9.170    1.00 124.79 ? 507  ALA   A CB   1 
ATOM   7673  H  H    . ALA   A  1  507 ? 46.405  16.303  9.216    1.00 159.38 ? 507  ALA   A H    1 
ATOM   7674  H  HA   . ALA   A  1  507 ? 48.737  16.166  10.604   1.00 152.95 ? 507  ALA   A HA   1 
ATOM   7675  H  HB1  . ALA   A  1  507 ? 49.595  14.576  9.213    1.00 149.78 ? 507  ALA   A HB1  1 
ATOM   7676  H  HB2  . ALA   A  1  507 ? 48.188  14.012  9.690    1.00 149.78 ? 507  ALA   A HB2  1 
ATOM   7677  H  HB3  . ALA   A  1  507 ? 48.336  14.662  8.248    1.00 149.78 ? 507  ALA   A HB3  1 
ATOM   7678  N  N    . ILE   A  1  508 ? 49.972  17.689  9.125    1.00 126.22 ? 508  ILE   A N    1 
ATOM   7679  C  CA   . ILE   A  1  508 ? 50.474  18.884  8.457    1.00 133.99 ? 508  ILE   A CA   1 
ATOM   7680  C  C    . ILE   A  1  508 ? 50.916  18.547  7.038    1.00 141.52 ? 508  ILE   A C    1 
ATOM   7681  O  O    . ILE   A  1  508 ? 51.539  17.506  6.791    1.00 148.53 ? 508  ILE   A O    1 
ATOM   7682  C  CB   . ILE   A  1  508 ? 51.641  19.494  9.253    1.00 133.12 ? 508  ILE   A CB   1 
ATOM   7683  C  CG1  . ILE   A  1  508 ? 51.284  19.644  10.736   1.00 134.88 ? 508  ILE   A CG1  1 
ATOM   7684  C  CG2  . ILE   A  1  508 ? 52.026  20.847  8.664    1.00 131.65 ? 508  ILE   A CG2  1 
ATOM   7685  C  CD1  . ILE   A  1  508 ? 52.481  19.948  11.619   1.00 136.25 ? 508  ILE   A CD1  1 
ATOM   7686  H  H    . ILE   A  1  508 ? 50.513  17.359  9.707    1.00 151.50 ? 508  ILE   A H    1 
ATOM   7687  H  HA   . ILE   A  1  508 ? 49.754  19.532  8.409    1.00 160.82 ? 508  ILE   A HA   1 
ATOM   7688  H  HB   . ILE   A  1  508 ? 52.397  18.889  9.187    1.00 159.78 ? 508  ILE   A HB   1 
ATOM   7689  H  HG12 . ILE   A  1  508 ? 50.650  20.372  10.833   1.00 161.89 ? 508  ILE   A HG12 1 
ATOM   7690  H  HG13 . ILE   A  1  508 ? 50.887  18.815  11.047   1.00 161.89 ? 508  ILE   A HG13 1 
ATOM   7691  H  HG21 . ILE   A  1  508 ? 52.695  21.260  9.233    1.00 158.01 ? 508  ILE   A HG21 1 
ATOM   7692  H  HG22 . ILE   A  1  508 ? 52.386  20.713  7.774    1.00 158.01 ? 508  ILE   A HG22 1 
ATOM   7693  H  HG23 . ILE   A  1  508 ? 51.236  21.409  8.620    1.00 158.01 ? 508  ILE   A HG23 1 
ATOM   7694  H  HD11 . ILE   A  1  508 ? 52.185  20.017  12.540   1.00 163.53 ? 508  ILE   A HD11 1 
ATOM   7695  H  HD12 . ILE   A  1  508 ? 53.128  19.230  11.533   1.00 163.53 ? 508  ILE   A HD12 1 
ATOM   7696  H  HD13 . ILE   A  1  508 ? 52.878  20.786  11.336   1.00 163.53 ? 508  ILE   A HD13 1 
ATOM   7697  N  N    . ARG   A  1  509 ? 50.610  19.442  6.099    1.00 140.52 ? 509  ARG   A N    1 
ATOM   7698  C  CA   . ARG   A  1  509 ? 51.085  19.323  4.725    1.00 140.25 ? 509  ARG   A CA   1 
ATOM   7699  C  C    . ARG   A  1  509 ? 52.363  20.143  4.580    1.00 133.00 ? 509  ARG   A C    1 
ATOM   7700  O  O    . ARG   A  1  509 ? 52.339  21.369  4.737    1.00 133.47 ? 509  ARG   A O    1 
ATOM   7701  C  CB   . ARG   A  1  509 ? 50.033  19.806  3.726    1.00 144.00 ? 509  ARG   A CB   1 
ATOM   7702  C  CG   . ARG   A  1  509 ? 48.590  19.615  4.171    1.00 144.15 ? 509  ARG   A CG   1 
ATOM   7703  C  CD   . ARG   A  1  509 ? 48.233  18.146  4.335    1.00 142.17 ? 509  ARG   A CD   1 
ATOM   7704  N  NE   . ARG   A  1  509 ? 47.778  17.539  3.084    1.00 137.62 ? 509  ARG   A NE   1 
ATOM   7705  C  CZ   . ARG   A  1  509 ? 46.515  17.211  2.810    1.00 138.47 ? 509  ARG   A CZ   1 
ATOM   7706  N  NH1  . ARG   A  1  509 ? 46.215  16.664  1.640    1.00 135.76 ? 509  ARG   A NH1  1 
ATOM   7707  N  NH2  . ARG   A  1  509 ? 45.550  17.418  3.698    1.00 142.88 ? 509  ARG   A NH2  1 
ATOM   7708  H  H    . ARG   A  1  509 ? 50.122  20.136  6.237    1.00 168.66 ? 509  ARG   A H    1 
ATOM   7709  H  HA   . ARG   A  1  509 ? 51.273  18.392  4.531    1.00 168.34 ? 509  ARG   A HA   1 
ATOM   7710  H  HB2  . ARG   A  1  509 ? 50.167  20.754  3.572    1.00 172.83 ? 509  ARG   A HB2  1 
ATOM   7711  H  HB3  . ARG   A  1  509 ? 50.149  19.316  2.897    1.00 172.83 ? 509  ARG   A HB3  1 
ATOM   7712  H  HG2  . ARG   A  1  509 ? 48.458  20.056  5.025    1.00 173.02 ? 509  ARG   A HG2  1 
ATOM   7713  H  HG3  . ARG   A  1  509 ? 47.997  19.999  3.506    1.00 173.02 ? 509  ARG   A HG3  1 
ATOM   7714  H  HD2  . ARG   A  1  509 ? 49.016  17.660  4.638    1.00 170.65 ? 509  ARG   A HD2  1 
ATOM   7715  H  HD3  . ARG   A  1  509 ? 47.519  18.063  4.986    1.00 170.65 ? 509  ARG   A HD3  1 
ATOM   7716  H  HE   . ARG   A  1  509 ? 48.370  17.381  2.480    1.00 165.18 ? 509  ARG   A HE   1 
ATOM   7717  H  HH11 . ARG   A  1  509 ? 46.835  16.521  1.061    1.00 162.95 ? 509  ARG   A HH11 1 
ATOM   7718  H  HH12 . ARG   A  1  509 ? 45.402  16.452  1.460    1.00 162.95 ? 509  ARG   A HH12 1 
ATOM   7719  H  HH21 . ARG   A  1  509 ? 45.736  17.767  4.462    1.00 171.50 ? 509  ARG   A HH21 1 
ATOM   7720  H  HH22 . ARG   A  1  509 ? 44.739  17.202  3.510    1.00 171.50 ? 509  ARG   A HH22 1 
ATOM   7721  N  N    . ARG   A  1  510 ? 53.472  19.469  4.275    1.00 126.61 ? 510  ARG   A N    1 
ATOM   7722  C  CA   . ARG   A  1  510 ? 54.758  20.155  4.218    1.00 123.71 ? 510  ARG   A CA   1 
ATOM   7723  C  C    . ARG   A  1  510 ? 54.896  21.019  2.971    1.00 119.48 ? 510  ARG   A C    1 
ATOM   7724  O  O    . ARG   A  1  510 ? 55.556  22.063  3.017    1.00 123.87 ? 510  ARG   A O    1 
ATOM   7725  C  CB   . ARG   A  1  510 ? 55.888  19.128  4.281    1.00 121.57 ? 510  ARG   A CB   1 
ATOM   7726  C  CG   . ARG   A  1  510 ? 55.922  18.367  5.594    1.00 117.16 ? 510  ARG   A CG   1 
ATOM   7727  C  CD   . ARG   A  1  510 ? 56.637  17.036  5.475    1.00 109.61 ? 510  ARG   A CD   1 
ATOM   7728  N  NE   . ARG   A  1  510 ? 55.925  16.116  4.594    1.00 100.29 ? 510  ARG   A NE   1 
ATOM   7729  C  CZ   . ARG   A  1  510 ? 56.140  14.806  4.544    1.00 97.97  ? 510  ARG   A CZ   1 
ATOM   7730  N  NH1  . ARG   A  1  510 ? 57.048  14.245  5.332    1.00 99.65  ? 510  ARG   A NH1  1 
ATOM   7731  N  NH2  . ARG   A  1  510 ? 55.439  14.052  3.708    1.00 95.04  ? 510  ARG   A NH2  1 
ATOM   7732  H  H    . ARG   A  1  510 ? 53.505  18.628  4.099    1.00 151.97 ? 510  ARG   A H    1 
ATOM   7733  H  HA   . ARG   A  1  510 ? 54.833  20.742  4.986    1.00 148.49 ? 510  ARG   A HA   1 
ATOM   7734  H  HB2  . ARG   A  1  510 ? 55.769  18.484  3.566    1.00 145.92 ? 510  ARG   A HB2  1 
ATOM   7735  H  HB3  . ARG   A  1  510 ? 56.736  19.586  4.178    1.00 145.92 ? 510  ARG   A HB3  1 
ATOM   7736  H  HG2  . ARG   A  1  510 ? 56.387  18.900  6.258    1.00 140.63 ? 510  ARG   A HG2  1 
ATOM   7737  H  HG3  . ARG   A  1  510 ? 55.013  18.195  5.885    1.00 140.63 ? 510  ARG   A HG3  1 
ATOM   7738  H  HD2  . ARG   A  1  510 ? 57.524  17.181  5.110    1.00 131.57 ? 510  ARG   A HD2  1 
ATOM   7739  H  HD3  . ARG   A  1  510 ? 56.702  16.627  6.352    1.00 131.57 ? 510  ARG   A HD3  1 
ATOM   7740  H  HE   . ARG   A  1  510 ? 55.325  16.445  4.071    1.00 120.39 ? 510  ARG   A HE   1 
ATOM   7741  H  HH11 . ARG   A  1  510 ? 57.501  14.731  5.879    1.00 119.62 ? 510  ARG   A HH11 1 
ATOM   7742  H  HH12 . ARG   A  1  510 ? 57.183  13.397  5.296    1.00 119.62 ? 510  ARG   A HH12 1 
ATOM   7743  H  HH21 . ARG   A  1  510 ? 54.847  14.412  3.199    1.00 114.08 ? 510  ARG   A HH21 1 
ATOM   7744  H  HH22 . ARG   A  1  510 ? 55.577  13.204  3.674    1.00 114.08 ? 510  ARG   A HH22 1 
ATOM   7745  N  N    . ALA   A  1  511 ? 54.290  20.615  1.859    1.00 111.53 ? 511  ALA   A N    1 
ATOM   7746  C  CA   . ALA   A  1  511 ? 54.433  21.321  0.594    1.00 105.10 ? 511  ALA   A CA   1 
ATOM   7747  C  C    . ALA   A  1  511 ? 53.190  22.148  0.290    1.00 103.20 ? 511  ALA   A C    1 
ATOM   7748  O  O    . ALA   A  1  511 ? 52.060  21.695  0.496    1.00 104.06 ? 511  ALA   A O    1 
ATOM   7749  C  CB   . ALA   A  1  511 ? 54.696  20.336  -0.548   1.00 98.85  ? 511  ALA   A CB   1 
ATOM   7750  H  H    . ALA   A  1  511 ? 53.782  19.922  1.813    1.00 133.87 ? 511  ALA   A H    1 
ATOM   7751  H  HA   . ALA   A  1  511 ? 55.184  21.931  0.656    1.00 126.16 ? 511  ALA   A HA   1 
ATOM   7752  H  HB1  . ALA   A  1  511 ? 54.559  20.790  -1.394   1.00 118.66 ? 511  ALA   A HB1  1 
ATOM   7753  H  HB2  . ALA   A  1  511 ? 55.610  20.019  -0.487   1.00 118.66 ? 511  ALA   A HB2  1 
ATOM   7754  H  HB3  . ALA   A  1  511 ? 54.081  19.590  -0.469   1.00 118.66 ? 511  ALA   A HB3  1 
ATOM   7755  N  N    . LEU   A  1  512 ? 53.413  23.366  -0.205   1.00 101.32 ? 512  LEU   A N    1 
ATOM   7756  C  CA   . LEU   A  1  512 ? 52.345  24.277  -0.587   1.00 100.85 ? 512  LEU   A CA   1 
ATOM   7757  C  C    . LEU   A  1  512 ? 52.704  24.928  -1.915   1.00 101.35 ? 512  LEU   A C    1 
ATOM   7758  O  O    . LEU   A  1  512 ? 53.881  25.129  -2.225   1.00 101.86 ? 512  LEU   A O    1 
ATOM   7759  C  CB   . LEU   A  1  512 ? 52.116  25.362  0.476    1.00 104.01 ? 512  LEU   A CB   1 
ATOM   7760  C  CG   . LEU   A  1  512 ? 51.877  24.899  1.915    1.00 104.08 ? 512  LEU   A CG   1 
ATOM   7761  C  CD1  . LEU   A  1  512 ? 51.919  26.092  2.860    1.00 110.02 ? 512  LEU   A CD1  1 
ATOM   7762  C  CD2  . LEU   A  1  512 ? 50.554  24.159  2.043    1.00 99.34  ? 512  LEU   A CD2  1 
ATOM   7763  H  H    . LEU   A  1  512 ? 54.198  23.693  -0.331   1.00 121.62 ? 512  LEU   A H    1 
ATOM   7764  H  HA   . LEU   A  1  512 ? 51.518  23.781  -0.696   1.00 121.06 ? 512  LEU   A HA   1 
ATOM   7765  H  HB2  . LEU   A  1  512 ? 52.900  25.934  0.490    1.00 124.85 ? 512  LEU   A HB2  1 
ATOM   7766  H  HB3  . LEU   A  1  512 ? 51.336  25.876  0.213    1.00 124.85 ? 512  LEU   A HB3  1 
ATOM   7767  H  HG   . LEU   A  1  512 ? 52.581  24.280  2.166    1.00 124.93 ? 512  LEU   A HG   1 
ATOM   7768  H  HD11 . LEU   A  1  512 ? 51.796  25.778  3.770    1.00 132.06 ? 512  LEU   A HD11 1 
ATOM   7769  H  HD12 . LEU   A  1  512 ? 52.778  26.533  2.775    1.00 132.06 ? 512  LEU   A HD12 1 
ATOM   7770  H  HD13 . LEU   A  1  512 ? 51.206  26.706  2.624    1.00 132.06 ? 512  LEU   A HD13 1 
ATOM   7771  H  HD21 . LEU   A  1  512 ? 50.423  23.904  2.970    1.00 119.25 ? 512  LEU   A HD21 1 
ATOM   7772  H  HD22 . LEU   A  1  512 ? 49.836  24.744  1.756    1.00 119.25 ? 512  LEU   A HD22 1 
ATOM   7773  H  HD23 . LEU   A  1  512 ? 50.580  23.367  1.483    1.00 119.25 ? 512  LEU   A HD23 1 
ATOM   7774  N  N    . PHE   A  1  513 ? 51.679  25.260  -2.696   1.00 104.33 ? 513  PHE   A N    1 
ATOM   7775  C  CA   . PHE   A  1  513 ? 51.894  25.912  -3.979   1.00 109.12 ? 513  PHE   A CA   1 
ATOM   7776  C  C    . PHE   A  1  513 ? 52.251  27.381  -3.782   1.00 118.44 ? 513  PHE   A C    1 
ATOM   7777  O  O    . PHE   A  1  513 ? 51.758  28.048  -2.867   1.00 120.76 ? 513  PHE   A O    1 
ATOM   7778  C  CB   . PHE   A  1  513 ? 50.654  25.783  -4.864   1.00 106.77 ? 513  PHE   A CB   1 
ATOM   7779  C  CG   . PHE   A  1  513 ? 50.499  24.426  -5.487   1.00 101.29 ? 513  PHE   A CG   1 
ATOM   7780  C  CD1  . PHE   A  1  513 ? 51.404  23.982  -6.436   1.00 100.53 ? 513  PHE   A CD1  1 
ATOM   7781  C  CD2  . PHE   A  1  513 ? 49.451  23.595  -5.127   1.00 98.47  ? 513  PHE   A CD2  1 
ATOM   7782  C  CE1  . PHE   A  1  513 ? 51.271  22.734  -7.012   1.00 96.31  ? 513  PHE   A CE1  1 
ATOM   7783  C  CE2  . PHE   A  1  513 ? 49.310  22.347  -5.704   1.00 94.24  ? 513  PHE   A CE2  1 
ATOM   7784  C  CZ   . PHE   A  1  513 ? 50.222  21.916  -6.648   1.00 93.19  ? 513  PHE   A CZ   1 
ATOM   7785  H  H    . PHE   A  1  513 ? 50.853  25.118  -2.504   1.00 125.23 ? 513  PHE   A H    1 
ATOM   7786  H  HA   . PHE   A  1  513 ? 52.632  25.484  -4.441   1.00 130.98 ? 513  PHE   A HA   1 
ATOM   7787  H  HB2  . PHE   A  1  513 ? 49.866  25.954  -4.325   1.00 128.16 ? 513  PHE   A HB2  1 
ATOM   7788  H  HB3  . PHE   A  1  513 ? 50.713  26.434  -5.581   1.00 128.16 ? 513  PHE   A HB3  1 
ATOM   7789  H  HD1  . PHE   A  1  513 ? 52.111  24.531  -6.688   1.00 120.67 ? 513  PHE   A HD1  1 
ATOM   7790  H  HD2  . PHE   A  1  513 ? 48.836  23.880  -4.491   1.00 118.20 ? 513  PHE   A HD2  1 
ATOM   7791  H  HE1  . PHE   A  1  513 ? 51.889  22.445  -7.645   1.00 115.61 ? 513  PHE   A HE1  1 
ATOM   7792  H  HE2  . PHE   A  1  513 ? 48.602  21.797  -5.457   1.00 113.13 ? 513  PHE   A HE2  1 
ATOM   7793  H  HZ   . PHE   A  1  513 ? 50.129  21.076  -7.037   1.00 111.87 ? 513  PHE   A HZ   1 
ATOM   7794  N  N    . LEU   A  1  514 ? 53.116  27.884  -4.664   1.00 127.95 ? 514  LEU   A N    1 
ATOM   7795  C  CA   . LEU   A  1  514 ? 53.688  29.213  -4.478   1.00 133.49 ? 514  LEU   A CA   1 
ATOM   7796  C  C    . LEU   A  1  514 ? 52.606  30.287  -4.485   1.00 137.67 ? 514  LEU   A C    1 
ATOM   7797  O  O    . LEU   A  1  514 ? 52.436  31.025  -3.508   1.00 143.73 ? 514  LEU   A O    1 
ATOM   7798  C  CB   . LEU   A  1  514 ? 54.728  29.487  -5.566   1.00 134.92 ? 514  LEU   A CB   1 
ATOM   7799  C  CG   . LEU   A  1  514 ? 55.680  30.655  -5.303   1.00 140.70 ? 514  LEU   A CG   1 
ATOM   7800  C  CD1  . LEU   A  1  514 ? 56.598  30.345  -4.129   1.00 141.77 ? 514  LEU   A CD1  1 
ATOM   7801  C  CD2  . LEU   A  1  514 ? 56.487  30.969  -6.551   1.00 143.08 ? 514  LEU   A CD2  1 
ATOM   7802  H  H    . LEU   A  1  514 ? 53.386  27.477  -5.372   1.00 153.57 ? 514  LEU   A H    1 
ATOM   7803  H  HA   . LEU   A  1  514 ? 54.133  29.243  -3.616   1.00 160.22 ? 514  LEU   A HA   1 
ATOM   7804  H  HB2  . LEU   A  1  514 ? 55.271  28.691  -5.673   1.00 161.94 ? 514  LEU   A HB2  1 
ATOM   7805  H  HB3  . LEU   A  1  514 ? 54.257  29.681  -6.392   1.00 161.94 ? 514  LEU   A HB3  1 
ATOM   7806  H  HG   . LEU   A  1  514 ? 55.162  31.443  -5.073   1.00 168.87 ? 514  LEU   A HG   1 
ATOM   7807  H  HD11 . LEU   A  1  514 ? 57.221  31.080  -4.012   1.00 170.16 ? 514  LEU   A HD11 1 
ATOM   7808  H  HD12 . LEU   A  1  514 ? 56.061  30.237  -3.328   1.00 170.16 ? 514  LEU   A HD12 1 
ATOM   7809  H  HD13 . LEU   A  1  514 ? 57.083  29.526  -4.314   1.00 170.16 ? 514  LEU   A HD13 1 
ATOM   7810  H  HD21 . LEU   A  1  514 ? 57.099  31.695  -6.357   1.00 171.73 ? 514  LEU   A HD21 1 
ATOM   7811  H  HD22 . LEU   A  1  514 ? 56.984  30.178  -6.813   1.00 171.73 ? 514  LEU   A HD22 1 
ATOM   7812  H  HD23 . LEU   A  1  514 ? 55.880  31.228  -7.263   1.00 171.73 ? 514  LEU   A HD23 1 
ATOM   7813  N  N    . TYR   A  1  515 ? 51.863  30.390  -5.588   1.00 138.22 ? 515  TYR   A N    1 
ATOM   7814  C  CA   . TYR   A  1  515 ? 50.867  31.447  -5.718   1.00 143.95 ? 515  TYR   A CA   1 
ATOM   7815  C  C    . TYR   A  1  515 ? 49.777  31.314  -4.662   1.00 143.40 ? 515  TYR   A C    1 
ATOM   7816  O  O    . TYR   A  1  515 ? 49.518  32.246  -3.891   1.00 152.20 ? 515  TYR   A O    1 
ATOM   7817  C  CB   . TYR   A  1  515 ? 50.263  31.417  -7.123   1.00 145.70 ? 515  TYR   A CB   1 
ATOM   7818  C  CG   . TYR   A  1  515 ? 51.091  32.155  -8.145   1.00 148.59 ? 515  TYR   A CG   1 
ATOM   7819  C  CD1  . TYR   A  1  515 ? 52.295  31.635  -8.598   1.00 145.86 ? 515  TYR   A CD1  1 
ATOM   7820  C  CD2  . TYR   A  1  515 ? 50.670  33.375  -8.653   1.00 152.84 ? 515  TYR   A CD2  1 
ATOM   7821  C  CE1  . TYR   A  1  515 ? 53.057  32.310  -9.531   1.00 149.08 ? 515  TYR   A CE1  1 
ATOM   7822  C  CE2  . TYR   A  1  515 ? 51.424  34.057  -9.586   1.00 155.58 ? 515  TYR   A CE2  1 
ATOM   7823  C  CZ   . TYR   A  1  515 ? 52.616  33.521  -10.021  1.00 155.65 ? 515  TYR   A CZ   1 
ATOM   7824  O  OH   . TYR   A  1  515 ? 53.369  34.199  -10.951  1.00 162.51 ? 515  TYR   A OH   1 
ATOM   7825  H  H    . TYR   A  1  515 ? 51.918  29.865  -6.267   1.00 165.90 ? 515  TYR   A H    1 
ATOM   7826  H  HA   . TYR   A  1  515 ? 51.303  32.304  -5.590   1.00 172.78 ? 515  TYR   A HA   1 
ATOM   7827  H  HB2  . TYR   A  1  515 ? 50.187  30.494  -7.412   1.00 174.88 ? 515  TYR   A HB2  1 
ATOM   7828  H  HB3  . TYR   A  1  515 ? 49.386  31.829  -7.096   1.00 174.88 ? 515  TYR   A HB3  1 
ATOM   7829  H  HD1  . TYR   A  1  515 ? 52.594  30.819  -8.269   1.00 175.07 ? 515  TYR   A HD1  1 
ATOM   7830  H  HD2  . TYR   A  1  515 ? 49.866  33.740  -8.360   1.00 183.44 ? 515  TYR   A HD2  1 
ATOM   7831  H  HE1  . TYR   A  1  515 ? 53.862  31.951  -9.826   1.00 178.93 ? 515  TYR   A HE1  1 
ATOM   7832  H  HE2  . TYR   A  1  515 ? 51.129  34.874  -9.918   1.00 186.73 ? 515  TYR   A HE2  1 
ATOM   7833  H  HH   . TYR   A  1  515 ? 52.998  34.928  -11.145  1.00 195.05 ? 515  TYR   A HH   1 
ATOM   7834  N  N    . SER   A  1  516 ? 49.127  30.150  -4.609   1.00 134.55 ? 516  SER   A N    1 
ATOM   7835  C  CA   . SER   A  1  516 ? 47.958  29.992  -3.754   1.00 129.39 ? 516  SER   A CA   1 
ATOM   7836  C  C    . SER   A  1  516 ? 48.326  29.911  -2.279   1.00 127.39 ? 516  SER   A C    1 
ATOM   7837  O  O    . SER   A  1  516 ? 47.505  30.255  -1.420   1.00 132.58 ? 516  SER   A O    1 
ATOM   7838  C  CB   . SER   A  1  516 ? 47.185  28.739  -4.166   1.00 123.56 ? 516  SER   A CB   1 
ATOM   7839  O  OG   . SER   A  1  516 ? 46.308  28.321  -3.136   1.00 123.70 ? 516  SER   A OG   1 
ATOM   7840  H  H    . SER   A  1  516 ? 49.343  29.447  -5.054   1.00 161.49 ? 516  SER   A H    1 
ATOM   7841  H  HA   . SER   A  1  516 ? 47.386  30.766  -3.872   1.00 155.30 ? 516  SER   A HA   1 
ATOM   7842  H  HB2  . SER   A  1  516 ? 46.666  28.936  -4.961   1.00 148.31 ? 516  SER   A HB2  1 
ATOM   7843  H  HB3  . SER   A  1  516 ? 47.816  28.026  -4.350   1.00 148.31 ? 516  SER   A HB3  1 
ATOM   7844  H  HG   . SER   A  1  516 ? 46.287  27.482  -3.099   1.00 148.48 ? 516  SER   A HG   1 
ATOM   7845  N  N    . ARG   A  1  517 ? 49.540  29.465  -1.960   1.00 122.94 ? 517  ARG   A N    1 
ATOM   7846  C  CA   . ARG   A  1  517 ? 49.925  29.182  -0.579   1.00 123.43 ? 517  ARG   A CA   1 
ATOM   7847  C  C    . ARG   A  1  517 ? 49.018  28.112  0.026    1.00 120.48 ? 517  ARG   A C    1 
ATOM   7848  O  O    . ARG   A  1  517 ? 48.688  28.148  1.215    1.00 120.63 ? 517  ARG   A O    1 
ATOM   7849  C  CB   . ARG   A  1  517 ? 49.908  30.450  0.280    1.00 129.68 ? 517  ARG   A CB   1 
ATOM   7850  C  CG   . ARG   A  1  517 ? 50.801  31.580  -0.217   1.00 132.67 ? 517  ARG   A CG   1 
ATOM   7851  C  CD   . ARG   A  1  517 ? 50.756  32.750  0.757    1.00 136.16 ? 517  ARG   A CD   1 
ATOM   7852  N  NE   . ARG   A  1  517 ? 51.446  33.940  0.266    1.00 138.64 ? 517  ARG   A NE   1 
ATOM   7853  C  CZ   . ARG   A  1  517 ? 51.514  35.089  0.933    1.00 143.23 ? 517  ARG   A CZ   1 
ATOM   7854  N  NH1  . ARG   A  1  517 ? 52.160  36.124  0.415    1.00 147.68 ? 517  ARG   A NH1  1 
ATOM   7855  N  NH2  . ARG   A  1  517 ? 50.934  35.205  2.121    1.00 143.16 ? 517  ARG   A NH2  1 
ATOM   7856  H  H    . ARG   A  1  517 ? 50.165  29.318  -2.532   1.00 147.57 ? 517  ARG   A H    1 
ATOM   7857  H  HA   . ARG   A  1  517 ? 50.833  28.842  -0.573   1.00 148.16 ? 517  ARG   A HA   1 
ATOM   7858  H  HB2  . ARG   A  1  517 ? 48.999  30.788  0.309    1.00 155.66 ? 517  ARG   A HB2  1 
ATOM   7859  H  HB3  . ARG   A  1  517 ? 50.204  30.218  1.175    1.00 155.66 ? 517  ARG   A HB3  1 
ATOM   7860  H  HG2  . ARG   A  1  517 ? 51.717  31.267  -0.285   1.00 159.24 ? 517  ARG   A HG2  1 
ATOM   7861  H  HG3  . ARG   A  1  517 ? 50.490  31.885  -1.084   1.00 159.24 ? 517  ARG   A HG3  1 
ATOM   7862  H  HD2  . ARG   A  1  517 ? 49.830  32.989  0.918    1.00 163.43 ? 517  ARG   A HD2  1 
ATOM   7863  H  HD3  . ARG   A  1  517 ? 51.179  32.483  1.588    1.00 163.43 ? 517  ARG   A HD3  1 
ATOM   7864  H  HE   . ARG   A  1  517 ? 51.832  33.895  -0.501   1.00 166.41 ? 517  ARG   A HE   1 
ATOM   7865  H  HH11 . ARG   A  1  517 ? 52.537  36.054  -0.355   1.00 177.25 ? 517  ARG   A HH11 1 
ATOM   7866  H  HH12 . ARG   A  1  517 ? 52.202  36.866  0.848    1.00 177.25 ? 517  ARG   A HH12 1 
ATOM   7867  H  HH21 . ARG   A  1  517 ? 50.514  34.536  2.462    1.00 171.83 ? 517  ARG   A HH21 1 
ATOM   7868  H  HH22 . ARG   A  1  517 ? 50.979  35.948  2.551    1.00 171.83 ? 517  ARG   A HH22 1 
ATOM   7869  N  N    . SER   A  1  518 ? 48.598  27.158  -0.801   1.00 117.32 ? 518  SER   A N    1 
ATOM   7870  C  CA   . SER   A  1  518 ? 47.794  26.029  -0.365   1.00 113.53 ? 518  SER   A CA   1 
ATOM   7871  C  C    . SER   A  1  518 ? 48.191  24.817  -1.193   1.00 109.33 ? 518  SER   A C    1 
ATOM   7872  O  O    . SER   A  1  518 ? 48.678  24.973  -2.321   1.00 110.88 ? 518  SER   A O    1 
ATOM   7873  C  CB   . SER   A  1  518 ? 46.291  26.307  -0.514   1.00 113.40 ? 518  SER   A CB   1 
ATOM   7874  O  OG   . SER   A  1  518 ? 45.869  26.142  -1.856   1.00 110.67 ? 518  SER   A OG   1 
ATOM   7875  H  H    . SER   A  1  518 ? 48.773  27.146  -1.643   1.00 140.83 ? 518  SER   A H    1 
ATOM   7876  H  HA   . SER   A  1  518 ? 47.972  25.839  0.569    1.00 136.27 ? 518  SER   A HA   1 
ATOM   7877  H  HB2  . SER   A  1  518 ? 45.800  25.687  0.048    1.00 136.11 ? 518  SER   A HB2  1 
ATOM   7878  H  HB3  . SER   A  1  518 ? 46.112  27.219  -0.238   1.00 136.11 ? 518  SER   A HB3  1 
ATOM   7879  H  HG   . SER   A  1  518 ? 45.345  25.487  -1.914   1.00 132.84 ? 518  SER   A HG   1 
ATOM   7880  N  N    . PRO   A  1  519 ? 47.993  23.605  -0.675   1.00 106.69 ? 519  PRO   A N    1 
ATOM   7881  C  CA   . PRO   A  1  519 ? 48.484  22.414  -1.376   1.00 108.46 ? 519  PRO   A CA   1 
ATOM   7882  C  C    . PRO   A  1  519 ? 47.577  21.917  -2.489   1.00 109.01 ? 519  PRO   A C    1 
ATOM   7883  O  O    . PRO   A  1  519 ? 47.948  20.957  -3.173   1.00 108.48 ? 519  PRO   A O    1 
ATOM   7884  C  CB   . PRO   A  1  519 ? 48.580  21.382  -0.245   1.00 107.50 ? 519  PRO   A CB   1 
ATOM   7885  C  CG   . PRO   A  1  519 ? 47.455  21.744  0.661    1.00 108.61 ? 519  PRO   A CG   1 
ATOM   7886  C  CD   . PRO   A  1  519 ? 47.299  23.253  0.578    1.00 108.03 ? 519  PRO   A CD   1 
ATOM   7887  H  HA   . PRO   A  1  519 ? 49.367  22.579  -1.741   1.00 130.19 ? 519  PRO   A HA   1 
ATOM   7888  H  HB2  . PRO   A  1  519 ? 48.471  20.486  -0.600   1.00 129.04 ? 519  PRO   A HB2  1 
ATOM   7889  H  HB3  . PRO   A  1  519 ? 49.434  21.459  0.207    1.00 129.04 ? 519  PRO   A HB3  1 
ATOM   7890  H  HG2  . PRO   A  1  519 ? 46.645  21.301  0.364    1.00 130.37 ? 519  PRO   A HG2  1 
ATOM   7891  H  HG3  . PRO   A  1  519 ? 47.669  21.473  1.567    1.00 130.37 ? 519  PRO   A HG3  1 
ATOM   7892  H  HD2  . PRO   A  1  519 ? 46.362  23.500  0.534    1.00 129.68 ? 519  PRO   A HD2  1 
ATOM   7893  H  HD3  . PRO   A  1  519 ? 47.721  23.684  1.338    1.00 129.68 ? 519  PRO   A HD3  1 
ATOM   7894  N  N    . SER   A  1  520 ? 46.413  22.528  -2.698   1.00 109.73 ? 520  SER   A N    1 
ATOM   7895  C  CA   . SER   A  1  520 ? 45.494  22.129  -3.755   1.00 108.88 ? 520  SER   A CA   1 
ATOM   7896  C  C    . SER   A  1  520 ? 45.512  23.174  -4.862   1.00 111.53 ? 520  SER   A C    1 
ATOM   7897  O  O    . SER   A  1  520 ? 45.427  24.376  -4.588   1.00 119.12 ? 520  SER   A O    1 
ATOM   7898  C  CB   . SER   A  1  520 ? 44.070  21.958  -3.219   1.00 110.19 ? 520  SER   A CB   1 
ATOM   7899  O  OG   . SER   A  1  520 ? 43.413  23.208  -3.100   1.00 111.50 ? 520  SER   A OG   1 
ATOM   7900  H  H    . SER   A  1  520 ? 46.130  23.190  -2.228   1.00 131.72 ? 520  SER   A H    1 
ATOM   7901  H  HA   . SER   A  1  520 ? 45.783  21.280  -4.126   1.00 130.69 ? 520  SER   A HA   1 
ATOM   7902  H  HB2  . SER   A  1  520 ? 43.569  21.397  -3.831   1.00 132.26 ? 520  SER   A HB2  1 
ATOM   7903  H  HB3  . SER   A  1  520 ? 44.112  21.540  -2.345   1.00 132.26 ? 520  SER   A HB3  1 
ATOM   7904  H  HG   . SER   A  1  520 ? 42.582  23.094  -3.071   1.00 133.84 ? 520  SER   A HG   1 
ATOM   7905  N  N    . HIS   A  1  521 ? 45.629  22.713  -6.105   1.00 106.59 ? 521  HIS   A N    1 
ATOM   7906  C  CA   . HIS   A  1  521 ? 45.554  23.574  -7.278   1.00 104.46 ? 521  HIS   A CA   1 
ATOM   7907  C  C    . HIS   A  1  521 ? 44.663  22.909  -8.316   1.00 106.06 ? 521  HIS   A C    1 
ATOM   7908  O  O    . HIS   A  1  521 ? 44.898  21.757  -8.694   1.00 103.71 ? 521  HIS   A O    1 
ATOM   7909  C  CB   . HIS   A  1  521 ? 46.942  23.844  -7.869   1.00 96.27  ? 521  HIS   A CB   1 
ATOM   7910  C  CG   . HIS   A  1  521 ? 46.905  24.528  -9.200   1.00 95.71  ? 521  HIS   A CG   1 
ATOM   7911  N  ND1  . HIS   A  1  521 ? 46.937  23.837  -10.392  1.00 94.40  ? 521  HIS   A ND1  1 
ATOM   7912  C  CD2  . HIS   A  1  521 ? 46.829  25.839  -9.528   1.00 99.39  ? 521  HIS   A CD2  1 
ATOM   7913  C  CE1  . HIS   A  1  521 ? 46.887  24.693  -11.397  1.00 96.22  ? 521  HIS   A CE1  1 
ATOM   7914  N  NE2  . HIS   A  1  521 ? 46.821  25.914  -10.900  1.00 99.30  ? 521  HIS   A NE2  1 
ATOM   7915  H  H    . HIS   A  1  521 ? 45.755  21.885  -6.297   1.00 127.95 ? 521  HIS   A H    1 
ATOM   7916  H  HA   . HIS   A  1  521 ? 45.163  24.426  -7.030   1.00 125.39 ? 521  HIS   A HA   1 
ATOM   7917  H  HB2  . HIS   A  1  521 ? 47.436  24.412  -7.257   1.00 115.56 ? 521  HIS   A HB2  1 
ATOM   7918  H  HB3  . HIS   A  1  521 ? 47.403  22.998  -7.982   1.00 115.56 ? 521  HIS   A HB3  1 
ATOM   7919  H  HD2  . HIS   A  1  521 ? 46.790  26.555  -8.936   1.00 119.31 ? 521  HIS   A HD2  1 
ATOM   7920  H  HE1  . HIS   A  1  521 ? 46.897  24.473  -12.300  1.00 115.50 ? 521  HIS   A HE1  1 
ATOM   7921  H  HE2  . HIS   A  1  521 ? 46.780  26.640  -11.360  1.00 119.20 ? 521  HIS   A HE2  1 
ATOM   7922  N  N    . SER   A  1  522 ? 43.646  23.635  -8.773   1.00 113.26 ? 522  SER   A N    1 
ATOM   7923  C  CA   . SER   A  1  522 ? 42.693  23.140  -9.753   1.00 116.42 ? 522  SER   A CA   1 
ATOM   7924  C  C    . SER   A  1  522 ? 42.932  23.818  -11.096  1.00 116.18 ? 522  SER   A C    1 
ATOM   7925  O  O    . SER   A  1  522 ? 43.614  24.843  -11.185  1.00 119.77 ? 522  SER   A O    1 
ATOM   7926  C  CB   . SER   A  1  522 ? 41.255  23.385  -9.285   1.00 121.85 ? 522  SER   A CB   1 
ATOM   7927  O  OG   . SER   A  1  522 ? 40.374  22.407  -9.809   1.00 125.37 ? 522  SER   A OG   1 
ATOM   7928  H  H    . SER   A  1  522 ? 43.485  24.441  -8.520   1.00 135.95 ? 522  SER   A H    1 
ATOM   7929  H  HA   . SER   A  1  522 ? 42.810  22.184  -9.872   1.00 139.74 ? 522  SER   A HA   1 
ATOM   7930  H  HB2  . SER   A  1  522 ? 41.228  23.346  -8.316   1.00 146.26 ? 522  SER   A HB2  1 
ATOM   7931  H  HB3  . SER   A  1  522 ? 40.970  24.261  -9.589   1.00 146.26 ? 522  SER   A HB3  1 
ATOM   7932  H  HG   . SER   A  1  522 ? 39.586  22.573  -9.569   1.00 150.48 ? 522  SER   A HG   1 
ATOM   7933  N  N    . LYS   A  1  523 ? 42.359  23.236  -12.151  1.00 111.97 ? 523  LYS   A N    1 
ATOM   7934  C  CA   . LYS   A  1  523 ? 42.622  23.729  -13.498  1.00 110.29 ? 523  LYS   A CA   1 
ATOM   7935  C  C    . LYS   A  1  523 ? 41.722  23.090  -14.550  1.00 110.26 ? 523  LYS   A C    1 
ATOM   7936  O  O    . LYS   A  1  523 ? 41.684  21.863  -14.682  1.00 104.93 ? 523  LYS   A O    1 
ATOM   7937  C  CB   . LYS   A  1  523 ? 44.091  23.476  -13.858  1.00 106.04 ? 523  LYS   A CB   1 
ATOM   7938  C  CG   . LYS   A  1  523 ? 44.486  23.911  -15.258  1.00 105.40 ? 523  LYS   A CG   1 
ATOM   7939  C  CD   . LYS   A  1  523 ? 44.610  25.417  -15.341  1.00 107.45 ? 523  LYS   A CD   1 
ATOM   7940  C  CE   . LYS   A  1  523 ? 44.872  25.870  -16.761  1.00 107.16 ? 523  LYS   A CE   1 
ATOM   7941  N  NZ   . LYS   A  1  523 ? 45.145  27.329  -16.823  1.00 111.31 ? 523  LYS   A NZ   1 
ATOM   7942  H  H    . LYS   A  1  523 ? 41.822  22.566  -12.111  1.00 134.40 ? 523  LYS   A H    1 
ATOM   7943  H  HA   . LYS   A  1  523 ? 42.436  24.681  -13.509  1.00 132.38 ? 523  LYS   A HA   1 
ATOM   7944  H  HB2  . LYS   A  1  523 ? 44.650  23.963  -13.232  1.00 127.29 ? 523  LYS   A HB2  1 
ATOM   7945  H  HB3  . LYS   A  1  523 ? 44.266  22.524  -13.788  1.00 127.29 ? 523  LYS   A HB3  1 
ATOM   7946  H  HG2  . LYS   A  1  523 ? 45.343  23.520  -15.489  1.00 126.52 ? 523  LYS   A HG2  1 
ATOM   7947  H  HG3  . LYS   A  1  523 ? 43.809  23.623  -15.889  1.00 126.52 ? 523  LYS   A HG3  1 
ATOM   7948  H  HD2  . LYS   A  1  523 ? 43.784  25.825  -15.038  1.00 128.98 ? 523  LYS   A HD2  1 
ATOM   7949  H  HD3  . LYS   A  1  523 ? 45.348  25.710  -14.786  1.00 128.98 ? 523  LYS   A HD3  1 
ATOM   7950  H  HE2  . LYS   A  1  523 ? 45.645  25.399  -17.111  1.00 128.63 ? 523  LYS   A HE2  1 
ATOM   7951  H  HE3  . LYS   A  1  523 ? 44.093  25.681  -17.308  1.00 128.63 ? 523  LYS   A HE3  1 
ATOM   7952  H  HZ1  . LYS   A  1  523 ? 45.300  27.574  -17.664  1.00 133.61 ? 523  LYS   A HZ1  1 
ATOM   7953  H  HZ2  . LYS   A  1  523 ? 44.445  27.783  -16.514  1.00 133.61 ? 523  LYS   A HZ2  1 
ATOM   7954  H  HZ3  . LYS   A  1  523 ? 45.858  27.527  -16.328  1.00 133.61 ? 523  LYS   A HZ3  1 
ATOM   7955  N  N    . ASN   A  1  524 ? 41.007  23.918  -15.308  1.00 118.14 ? 524  ASN   A N    1 
ATOM   7956  C  CA   . ASN   A  1  524 ? 40.336  23.456  -16.515  1.00 118.22 ? 524  ASN   A CA   1 
ATOM   7957  C  C    . ASN   A  1  524 ? 41.334  23.397  -17.667  1.00 120.36 ? 524  ASN   A C    1 
ATOM   7958  O  O    . ASN   A  1  524 ? 42.270  24.197  -17.746  1.00 123.47 ? 524  ASN   A O    1 
ATOM   7959  C  CB   . ASN   A  1  524 ? 39.175  24.382  -16.884  1.00 123.77 ? 524  ASN   A CB   1 
ATOM   7960  C  CG   . ASN   A  1  524 ? 38.092  24.417  -15.822  1.00 128.55 ? 524  ASN   A CG   1 
ATOM   7961  O  OD1  . ASN   A  1  524 ? 37.980  23.506  -15.004  1.00 126.02 ? 524  ASN   A OD1  1 
ATOM   7962  N  ND2  . ASN   A  1  524 ? 37.281  25.470  -15.837  1.00 136.68 ? 524  ASN   A ND2  1 
ATOM   7963  H  H    . ASN   A  1  524 ? 40.894  24.754  -15.143  1.00 141.81 ? 524  ASN   A H    1 
ATOM   7964  H  HA   . ASN   A  1  524 ? 39.970  22.570  -16.367  1.00 141.90 ? 524  ASN   A HA   1 
ATOM   7965  H  HB2  . ASN   A  1  524 ? 39.514  25.284  -16.996  1.00 148.56 ? 524  ASN   A HB2  1 
ATOM   7966  H  HB3  . ASN   A  1  524 ? 38.774  24.073  -17.711  1.00 148.56 ? 524  ASN   A HB3  1 
ATOM   7967  H  HD21 . ASN   A  1  524 ? 36.650  25.535  -15.255  1.00 164.05 ? 524  ASN   A HD21 1 
ATOM   7968  H  HD22 . ASN   A  1  524 ? 37.386  26.085  -16.428  1.00 164.05 ? 524  ASN   A HD22 1 
ATOM   7969  N  N    . MET   A  1  525 ? 41.128  22.436  -18.567  1.00 122.29 ? 525  MET   A N    1 
ATOM   7970  C  CA   . MET   A  1  525 ? 42.011  22.247  -19.709  1.00 122.61 ? 525  MET   A CA   1 
ATOM   7971  C  C    . MET   A  1  525 ? 41.200  21.830  -20.926  1.00 126.99 ? 525  MET   A C    1 
ATOM   7972  O  O    . MET   A  1  525 ? 40.115  21.256  -20.805  1.00 133.27 ? 525  MET   A O    1 
ATOM   7973  C  CB   . MET   A  1  525 ? 43.084  21.189  -19.430  1.00 118.04 ? 525  MET   A CB   1 
ATOM   7974  C  CG   . MET   A  1  525 ? 44.342  21.720  -18.783  1.00 118.70 ? 525  MET   A CG   1 
ATOM   7975  S  SD   . MET   A  1  525 ? 45.591  20.427  -18.772  1.00 115.55 ? 525  MET   A SD   1 
ATOM   7976  C  CE   . MET   A  1  525 ? 46.334  20.609  -20.388  1.00 116.69 ? 525  MET   A CE   1 
ATOM   7977  H  H    . MET   A  1  525 ? 40.476  21.876  -18.534  1.00 146.78 ? 525  MET   A H    1 
ATOM   7978  H  HA   . MET   A  1  525 ? 42.452  23.090  -19.897  1.00 147.17 ? 525  MET   A HA   1 
ATOM   7979  H  HB2  . MET   A  1  525 ? 42.709  20.520  -18.836  1.00 141.68 ? 525  MET   A HB2  1 
ATOM   7980  H  HB3  . MET   A  1  525 ? 43.338  20.780  -20.272  1.00 141.68 ? 525  MET   A HB3  1 
ATOM   7981  H  HG2  . MET   A  1  525 ? 44.677  22.478  -19.287  1.00 142.48 ? 525  MET   A HG2  1 
ATOM   7982  H  HG3  . MET   A  1  525 ? 44.156  21.986  -17.869  1.00 142.48 ? 525  MET   A HG3  1 
ATOM   7983  H  HE1  . MET   A  1  525 ? 46.988  19.905  -20.516  1.00 140.07 ? 525  MET   A HE1  1 
ATOM   7984  H  HE2  . MET   A  1  525 ? 45.641  20.544  -21.063  1.00 140.07 ? 525  MET   A HE2  1 
ATOM   7985  H  HE3  . MET   A  1  525 ? 46.766  21.476  -20.440  1.00 140.07 ? 525  MET   A HE3  1 
ATOM   7986  N  N    . THR   A  1  526 ? 41.747  22.121  -22.106  1.00 126.44 ? 526  THR   A N    1 
ATOM   7987  C  CA   . THR   A  1  526 ? 41.138  21.751  -23.377  1.00 127.88 ? 526  THR   A CA   1 
ATOM   7988  C  C    . THR   A  1  526 ? 42.166  21.003  -24.213  1.00 124.22 ? 526  THR   A C    1 
ATOM   7989  O  O    . THR   A  1  526 ? 43.278  21.498  -24.423  1.00 123.64 ? 526  THR   A O    1 
ATOM   7990  C  CB   . THR   A  1  526 ? 40.633  22.988  -24.132  1.00 134.88 ? 526  THR   A CB   1 
ATOM   7991  O  OG1  . THR   A  1  526 ? 39.585  23.612  -23.379  1.00 135.96 ? 526  THR   A OG1  1 
ATOM   7992  C  CG2  . THR   A  1  526 ? 40.111  22.610  -25.518  1.00 138.33 ? 526  THR   A CG2  1 
ATOM   7993  H  H    . THR   A  1  526 ? 42.491  22.543  -22.195  1.00 151.76 ? 526  THR   A H    1 
ATOM   7994  H  HA   . THR   A  1  526 ? 40.382  21.164  -23.220  1.00 153.49 ? 526  THR   A HA   1 
ATOM   7995  H  HB   . THR   A  1  526 ? 41.365  23.612  -24.250  1.00 161.89 ? 526  THR   A HB   1 
ATOM   7996  H  HG1  . THR   A  1  526 ? 39.150  23.031  -22.956  1.00 163.19 ? 526  THR   A HG1  1 
ATOM   7997  H  HG21 . THR   A  1  526 ? 39.832  23.407  -25.997  1.00 166.03 ? 526  THR   A HG21 1 
ATOM   7998  H  HG22 . THR   A  1  526 ? 40.808  22.166  -26.026  1.00 166.03 ? 526  THR   A HG22 1 
ATOM   7999  H  HG23 . THR   A  1  526 ? 39.352  22.011  -25.435  1.00 166.03 ? 526  THR   A HG23 1 
ATOM   8000  N  N    . ILE   A  1  527 ? 41.788  19.822  -24.696  1.00 123.54 ? 527  ILE   A N    1 
ATOM   8001  C  CA   . ILE   A  1  527 ? 42.680  18.964  -25.468  1.00 121.31 ? 527  ILE   A CA   1 
ATOM   8002  C  C    . ILE   A  1  527 ? 41.921  18.414  -26.666  1.00 120.29 ? 527  ILE   A C    1 
ATOM   8003  O  O    . ILE   A  1  527 ? 40.751  18.031  -26.554  1.00 118.00 ? 527  ILE   A O    1 
ATOM   8004  C  CB   . ILE   A  1  527 ? 43.253  17.826  -24.595  1.00 118.46 ? 527  ILE   A CB   1 
ATOM   8005  C  CG1  . ILE   A  1  527 ? 44.468  18.336  -23.817  1.00 119.03 ? 527  ILE   A CG1  1 
ATOM   8006  C  CG2  . ILE   A  1  527 ? 43.622  16.615  -25.449  1.00 118.35 ? 527  ILE   A CG2  1 
ATOM   8007  C  CD1  . ILE   A  1  527 ? 44.651  17.704  -22.453  1.00 119.90 ? 527  ILE   A CD1  1 
ATOM   8008  H  H    . ILE   A  1  527 ? 41.003  19.489  -24.586  1.00 148.29 ? 527  ILE   A H    1 
ATOM   8009  H  HA   . ILE   A  1  527 ? 43.421  19.490  -25.807  1.00 145.61 ? 527  ILE   A HA   1 
ATOM   8010  H  HB   . ILE   A  1  527 ? 42.570  17.544  -23.966  1.00 142.19 ? 527  ILE   A HB   1 
ATOM   8011  H  HG12 . ILE   A  1  527 ? 45.267  18.151  -24.335  1.00 142.87 ? 527  ILE   A HG12 1 
ATOM   8012  H  HG13 . ILE   A  1  527 ? 44.372  19.293  -23.686  1.00 142.87 ? 527  ILE   A HG13 1 
ATOM   8013  H  HG21 . ILE   A  1  527 ? 44.161  16.007  -24.918  1.00 142.05 ? 527  ILE   A HG21 1 
ATOM   8014  H  HG22 . ILE   A  1  527 ? 42.809  16.171  -25.736  1.00 142.05 ? 527  ILE   A HG22 1 
ATOM   8015  H  HG23 . ILE   A  1  527 ? 44.125  16.915  -26.221  1.00 142.05 ? 527  ILE   A HG23 1 
ATOM   8016  H  HD11 . ILE   A  1  527 ? 44.863  18.398  -21.809  1.00 143.92 ? 527  ILE   A HD11 1 
ATOM   8017  H  HD12 . ILE   A  1  527 ? 43.828  17.258  -22.199  1.00 143.92 ? 527  ILE   A HD12 1 
ATOM   8018  H  HD13 . ILE   A  1  527 ? 45.376  17.061  -22.497  1.00 143.92 ? 527  ILE   A HD13 1 
ATOM   8019  N  N    . SER   A  1  528 ? 42.593  18.373  -27.813  1.00 119.87 ? 528  SER   A N    1 
ATOM   8020  C  CA   . SER   A  1  528 ? 42.011  17.895  -29.059  1.00 123.13 ? 528  SER   A CA   1 
ATOM   8021  C  C    . SER   A  1  528 ? 42.449  16.462  -29.330  1.00 118.50 ? 528  SER   A C    1 
ATOM   8022  O  O    . SER   A  1  528 ? 43.596  16.091  -29.062  1.00 115.92 ? 528  SER   A O    1 
ATOM   8023  C  CB   . SER   A  1  528 ? 42.422  18.797  -30.226  1.00 127.83 ? 528  SER   A CB   1 
ATOM   8024  O  OG   . SER   A  1  528 ? 43.805  19.102  -30.172  1.00 122.01 ? 528  SER   A OG   1 
ATOM   8025  H  H    . SER   A  1  528 ? 43.412  18.624  -27.895  1.00 143.88 ? 528  SER   A H    1 
ATOM   8026  H  HA   . SER   A  1  528 ? 41.043  17.905  -28.989  1.00 147.79 ? 528  SER   A HA   1 
ATOM   8027  H  HB2  . SER   A  1  528 ? 42.233  18.339  -31.060  1.00 153.43 ? 528  SER   A HB2  1 
ATOM   8028  H  HB3  . SER   A  1  528 ? 41.915  19.623  -30.179  1.00 153.43 ? 528  SER   A HB3  1 
ATOM   8029  H  HG   . SER   A  1  528 ? 44.040  19.499  -30.874  1.00 146.44 ? 528  SER   A HG   1 
ATOM   8030  N  N    . ARG   A  1  529 ? 41.526  15.660  -29.864  1.00 114.82 ? 529  ARG   A N    1 
ATOM   8031  C  CA   . ARG   A  1  529 ? 41.833  14.273  -30.190  1.00 110.77 ? 529  ARG   A CA   1 
ATOM   8032  C  C    . ARG   A  1  529 ? 43.066  14.192  -31.080  1.00 111.59 ? 529  ARG   A C    1 
ATOM   8033  O  O    . ARG   A  1  529 ? 43.212  14.954  -32.039  1.00 117.65 ? 529  ARG   A O    1 
ATOM   8034  C  CB   . ARG   A  1  529 ? 40.647  13.611  -30.896  1.00 111.22 ? 529  ARG   A CB   1 
ATOM   8035  C  CG   . ARG   A  1  529 ? 39.477  13.265  -29.994  1.00 110.17 ? 529  ARG   A CG   1 
ATOM   8036  C  CD   . ARG   A  1  529 ? 38.499  12.335  -30.705  1.00 112.20 ? 529  ARG   A CD   1 
ATOM   8037  N  NE   . ARG   A  1  529 ? 38.195  12.794  -32.061  1.00 115.45 ? 529  ARG   A NE   1 
ATOM   8038  C  CZ   . ARG   A  1  529 ? 38.597  12.194  -33.182  1.00 116.76 ? 529  ARG   A CZ   1 
ATOM   8039  N  NH1  . ARG   A  1  529 ? 39.322  11.083  -33.144  1.00 115.23 ? 529  ARG   A NH1  1 
ATOM   8040  N  NH2  . ARG   A  1  529 ? 38.259  12.709  -34.357  1.00 121.08 ? 529  ARG   A NH2  1 
ATOM   8041  H  H    . ARG   A  1  529 ? 40.720  15.896  -30.046  1.00 137.82 ? 529  ARG   A H    1 
ATOM   8042  H  HA   . ARG   A  1  529 ? 42.007  13.790  -29.367  1.00 132.97 ? 529  ARG   A HA   1 
ATOM   8043  H  HB2  . ARG   A  1  529 ? 40.319  14.216  -31.579  1.00 133.50 ? 529  ARG   A HB2  1 
ATOM   8044  H  HB3  . ARG   A  1  529 ? 40.955  12.786  -31.303  1.00 133.50 ? 529  ARG   A HB3  1 
ATOM   8045  H  HG2  . ARG   A  1  529 ? 39.803  12.817  -29.198  1.00 132.24 ? 529  ARG   A HG2  1 
ATOM   8046  H  HG3  . ARG   A  1  529 ? 39.006  14.076  -29.749  1.00 132.24 ? 529  ARG   A HG3  1 
ATOM   8047  H  HD2  . ARG   A  1  529 ? 38.888  11.449  -30.765  1.00 134.68 ? 529  ARG   A HD2  1 
ATOM   8048  H  HD3  . ARG   A  1  529 ? 37.669  12.300  -30.204  1.00 134.68 ? 529  ARG   A HD3  1 
ATOM   8049  H  HE   . ARG   A  1  529 ? 37.719  13.506  -32.141  1.00 138.58 ? 529  ARG   A HE   1 
ATOM   8050  H  HH11 . ARG   A  1  529 ? 39.540  10.738  -32.387  1.00 138.31 ? 529  ARG   A HH11 1 
ATOM   8051  H  HH12 . ARG   A  1  529 ? 39.574  10.708  -33.876  1.00 138.31 ? 529  ARG   A HH12 1 
ATOM   8052  H  HH21 . ARG   A  1  529 ? 37.784  13.425  -34.392  1.00 145.33 ? 529  ARG   A HH21 1 
ATOM   8053  H  HH22 . ARG   A  1  529 ? 38.516  12.327  -35.084  1.00 145.33 ? 529  ARG   A HH22 1 
ATOM   8054  N  N    . GLY   A  1  530 ? 43.952  13.252  -30.760  1.00 106.14 ? 530  GLY   A N    1 
ATOM   8055  C  CA   . GLY   A  1  530 ? 45.162  13.080  -31.534  1.00 109.21 ? 530  GLY   A CA   1 
ATOM   8056  C  C    . GLY   A  1  530 ? 46.167  14.197  -31.394  1.00 113.77 ? 530  GLY   A C    1 
ATOM   8057  O  O    . GLY   A  1  530 ? 47.151  14.222  -32.139  1.00 117.13 ? 530  GLY   A O    1 
ATOM   8058  H  H    . GLY   A  1  530 ? 43.870  12.706  -30.100  1.00 127.40 ? 530  GLY   A H    1 
ATOM   8059  H  HA2  . GLY   A  1  530 ? 45.594  12.257  -31.257  1.00 131.08 ? 530  GLY   A HA2  1 
ATOM   8060  H  HA3  . GLY   A  1  530 ? 44.924  13.012  -32.472  1.00 131.08 ? 530  GLY   A HA3  1 
ATOM   8061  N  N    . GLY   A  1  531 ? 45.951  15.126  -30.464  1.00 115.71 ? 531  GLY   A N    1 
ATOM   8062  C  CA   . GLY   A  1  531 ? 46.875  16.220  -30.275  1.00 118.40 ? 531  GLY   A CA   1 
ATOM   8063  C  C    . GLY   A  1  531 ? 48.122  15.804  -29.522  1.00 117.61 ? 531  GLY   A C    1 
ATOM   8064  O  O    . GLY   A  1  531 ? 48.235  14.697  -28.995  1.00 119.29 ? 531  GLY   A O    1 
ATOM   8065  H  H    . GLY   A  1  531 ? 45.275  15.138  -29.932  1.00 138.88 ? 531  GLY   A H    1 
ATOM   8066  H  HA2  . GLY   A  1  531 ? 47.143  16.566  -31.141  1.00 142.12 ? 531  GLY   A HA2  1 
ATOM   8067  H  HA3  . GLY   A  1  531 ? 46.438  16.926  -29.775  1.00 142.12 ? 531  GLY   A HA3  1 
ATOM   8068  N  N    . LEU   A  1  532 ? 49.081  16.723  -29.478  1.00 123.28 ? 532  LEU   A N    1 
ATOM   8069  C  CA   . LEU   A  1  532 ? 50.322  16.486  -28.763  1.00 127.22 ? 532  LEU   A CA   1 
ATOM   8070  C  C    . LEU   A  1  532 ? 50.109  16.636  -27.259  1.00 132.92 ? 532  LEU   A C    1 
ATOM   8071  O  O    . LEU   A  1  532 ? 49.134  17.236  -26.798  1.00 137.69 ? 532  LEU   A O    1 
ATOM   8072  C  CB   . LEU   A  1  532 ? 51.407  17.452  -29.239  1.00 129.40 ? 532  LEU   A CB   1 
ATOM   8073  C  CG   . LEU   A  1  532 ? 51.833  17.306  -30.701  1.00 132.73 ? 532  LEU   A CG   1 
ATOM   8074  C  CD1  . LEU   A  1  532 ? 52.748  18.453  -31.102  1.00 136.99 ? 532  LEU   A CD1  1 
ATOM   8075  C  CD2  . LEU   A  1  532 ? 52.516  15.966  -30.931  1.00 131.62 ? 532  LEU   A CD2  1 
ATOM   8076  H  H    . LEU   A  1  532 ? 49.033  17.494  -29.856  1.00 147.97 ? 532  LEU   A H    1 
ATOM   8077  H  HA   . LEU   A  1  532 ? 50.628  15.582  -28.937  1.00 152.70 ? 532  LEU   A HA   1 
ATOM   8078  H  HB2  . LEU   A  1  532 ? 51.078  18.357  -29.123  1.00 155.32 ? 532  LEU   A HB2  1 
ATOM   8079  H  HB3  . LEU   A  1  532 ? 52.197  17.313  -28.694  1.00 155.32 ? 532  LEU   A HB3  1 
ATOM   8080  H  HG   . LEU   A  1  532 ? 51.045  17.338  -31.266  1.00 159.31 ? 532  LEU   A HG   1 
ATOM   8081  H  HD11 . LEU   A  1  532 ? 53.012  18.337  -32.028  1.00 164.43 ? 532  LEU   A HD11 1 
ATOM   8082  H  HD12 . LEU   A  1  532 ? 52.269  19.290  -30.997  1.00 164.43 ? 532  LEU   A HD12 1 
ATOM   8083  H  HD13 . LEU   A  1  532 ? 53.532  18.446  -30.531  1.00 164.43 ? 532  LEU   A HD13 1 
ATOM   8084  H  HD21 . LEU   A  1  532 ? 52.824  15.921  -31.849  1.00 157.98 ? 532  LEU   A HD21 1 
ATOM   8085  H  HD22 . LEU   A  1  532 ? 53.269  15.887  -30.325  1.00 157.98 ? 532  LEU   A HD22 1 
ATOM   8086  H  HD23 . LEU   A  1  532 ? 51.879  15.254  -30.760  1.00 157.98 ? 532  LEU   A HD23 1 
ATOM   8087  N  N    . MET   A  1  533 ? 51.044  16.076  -26.492  1.00 136.72 ? 533  MET   A N    1 
ATOM   8088  C  CA   . MET   A  1  533 ? 50.965  16.132  -25.038  1.00 138.48 ? 533  MET   A CA   1 
ATOM   8089  C  C    . MET   A  1  533 ? 50.972  17.582  -24.567  1.00 134.35 ? 533  MET   A C    1 
ATOM   8090  O  O    . MET   A  1  533 ? 52.024  18.229  -24.530  1.00 138.76 ? 533  MET   A O    1 
ATOM   8091  C  CB   . MET   A  1  533 ? 52.120  15.347  -24.409  1.00 146.29 ? 533  MET   A CB   1 
ATOM   8092  C  CG   . MET   A  1  533 ? 51.998  15.172  -22.900  1.00 151.00 ? 533  MET   A CG   1 
ATOM   8093  S  SD   . MET   A  1  533 ? 53.289  14.142  -22.169  1.00 159.06 ? 533  MET   A SD   1 
ATOM   8094  C  CE   . MET   A  1  533 ? 52.758  12.498  -22.646  1.00 157.86 ? 533  MET   A CE   1 
ATOM   8095  H  H    . MET   A  1  533 ? 51.733  15.659  -26.792  1.00 164.11 ? 533  MET   A H    1 
ATOM   8096  H  HA   . MET   A  1  533 ? 50.142  15.712  -24.744  1.00 166.22 ? 533  MET   A HA   1 
ATOM   8097  H  HB2  . MET   A  1  533 ? 52.150  14.463  -24.807  1.00 175.59 ? 533  MET   A HB2  1 
ATOM   8098  H  HB3  . MET   A  1  533 ? 52.950  15.818  -24.585  1.00 175.59 ? 533  MET   A HB3  1 
ATOM   8099  H  HG2  . MET   A  1  533 ? 52.045  16.046  -22.481  1.00 181.24 ? 533  MET   A HG2  1 
ATOM   8100  H  HG3  . MET   A  1  533 ? 51.143  14.757  -22.703  1.00 181.24 ? 533  MET   A HG3  1 
ATOM   8101  H  HE1  . MET   A  1  533 ? 53.438  11.858  -22.384  1.00 189.47 ? 533  MET   A HE1  1 
ATOM   8102  H  HE2  . MET   A  1  533 ? 51.922  12.294  -22.199  1.00 189.47 ? 533  MET   A HE2  1 
ATOM   8103  H  HE3  . MET   A  1  533 ? 52.634  12.473  -23.608  1.00 189.47 ? 533  MET   A HE3  1 
ATOM   8104  N  N    . GLN   A  1  534 ? 49.796  18.096  -24.213  1.00 140.15 ? 534  GLN   A N    1 
ATOM   8105  C  CA   . GLN   A  1  534 ? 49.639  19.481  -23.779  1.00 147.03 ? 534  GLN   A CA   1 
ATOM   8106  C  C    . GLN   A  1  534 ? 49.964  19.587  -22.291  1.00 138.93 ? 534  GLN   A C    1 
ATOM   8107  O  O    . GLN   A  1  534 ? 49.275  18.991  -21.457  1.00 144.75 ? 534  GLN   A O    1 
ATOM   8108  C  CB   . GLN   A  1  534 ? 48.212  19.942  -24.075  1.00 146.11 ? 534  GLN   A CB   1 
ATOM   8109  C  CG   . GLN   A  1  534 ? 47.872  21.360  -23.648  1.00 131.49 ? 534  GLN   A CG   1 
ATOM   8110  C  CD   . GLN   A  1  534 ? 46.410  21.705  -23.899  1.00 116.52 ? 534  GLN   A CD   1 
ATOM   8111  O  OE1  . GLN   A  1  534 ? 45.767  22.358  -23.077  1.00 109.22 ? 534  GLN   A OE1  1 
ATOM   8112  N  NE2  . GLN   A  1  534 ? 45.880  21.265  -25.037  1.00 112.07 ? 534  GLN   A NE2  1 
ATOM   8113  H  H    . GLN   A  1  534 ? 49.059  17.654  -24.216  1.00 168.22 ? 534  GLN   A H    1 
ATOM   8114  H  HA   . GLN   A  1  534 ? 50.255  20.059  -24.256  1.00 176.47 ? 534  GLN   A HA   1 
ATOM   8115  H  HB2  . GLN   A  1  534 ? 48.069  19.888  -25.033  1.00 175.37 ? 534  GLN   A HB2  1 
ATOM   8116  H  HB3  . GLN   A  1  534 ? 47.600  19.348  -23.613  1.00 175.37 ? 534  GLN   A HB3  1 
ATOM   8117  H  HG2  . GLN   A  1  534 ? 48.046  21.457  -22.699  1.00 157.82 ? 534  GLN   A HG2  1 
ATOM   8118  H  HG3  . GLN   A  1  534 ? 48.419  21.984  -24.151  1.00 157.82 ? 534  GLN   A HG3  1 
ATOM   8119  H  HE21 . GLN   A  1  534 ? 46.360  20.811  -25.588  1.00 134.52 ? 534  GLN   A HE21 1 
ATOM   8120  H  HE22 . GLN   A  1  534 ? 45.058  21.434  -25.223  1.00 134.52 ? 534  GLN   A HE22 1 
ATOM   8121  N  N    . CYS   A  1  535 ? 51.007  20.346  -21.959  1.00 128.29 ? 535  CYS   A N    1 
ATOM   8122  C  CA   . CYS   A  1  535 ? 51.551  20.409  -20.610  1.00 123.11 ? 535  CYS   A CA   1 
ATOM   8123  C  C    . CYS   A  1  535 ? 51.287  21.765  -19.966  1.00 122.72 ? 535  CYS   A C    1 
ATOM   8124  O  O    . CYS   A  1  535 ? 50.841  22.718  -20.611  1.00 124.53 ? 535  CYS   A O    1 
ATOM   8125  C  CB   . CYS   A  1  535 ? 53.063  20.146  -20.619  1.00 130.44 ? 535  CYS   A CB   1 
ATOM   8126  S  SG   . CYS   A  1  535 ? 53.564  18.464  -21.006  1.00 129.12 ? 535  CYS   A SG   1 
ATOM   8127  H  H    . CYS   A  1  535 ? 51.427  20.848  -22.518  1.00 153.98 ? 535  CYS   A H    1 
ATOM   8128  H  HA   . CYS   A  1  535 ? 51.107  19.729  -20.080  1.00 147.76 ? 535  CYS   A HA   1 
ATOM   8129  H  HB2  . CYS   A  1  535 ? 53.468  20.726  -21.282  1.00 156.56 ? 535  CYS   A HB2  1 
ATOM   8130  H  HB3  . CYS   A  1  535 ? 53.413  20.354  -19.738  1.00 156.56 ? 535  CYS   A HB3  1 
ATOM   8131  N  N    . GLU   A  1  536 ? 51.587  21.838  -18.669  1.00 120.99 ? 536  GLU   A N    1 
ATOM   8132  C  CA   . GLU   A  1  536 ? 51.547  23.092  -17.930  1.00 122.85 ? 536  GLU   A CA   1 
ATOM   8133  C  C    . GLU   A  1  536 ? 52.453  22.983  -16.710  1.00 118.72 ? 536  GLU   A C    1 
ATOM   8134  O  O    . GLU   A  1  536 ? 52.517  21.930  -16.070  1.00 114.88 ? 536  GLU   A O    1 
ATOM   8135  C  CB   . GLU   A  1  536 ? 50.121  23.450  -17.500  1.00 126.08 ? 536  GLU   A CB   1 
ATOM   8136  C  CG   . GLU   A  1  536 ? 49.555  24.633  -18.261  1.00 131.55 ? 536  GLU   A CG   1 
ATOM   8137  C  CD   . GLU   A  1  536 ? 48.231  25.111  -17.711  1.00 136.02 ? 536  GLU   A CD   1 
ATOM   8138  O  OE1  . GLU   A  1  536 ? 47.470  25.740  -18.475  1.00 138.82 ? 536  GLU   A OE1  1 
ATOM   8139  O  OE2  . GLU   A  1  536 ? 47.953  24.861  -16.519  1.00 137.19 ? 536  GLU   A OE2  1 
ATOM   8140  H  H    . GLU   A  1  536 ? 51.819  21.163  -18.190  1.00 145.23 ? 536  GLU   A H    1 
ATOM   8141  H  HA   . GLU   A  1  536 ? 51.883  23.804  -18.496  1.00 147.46 ? 536  GLU   A HA   1 
ATOM   8142  H  HB2  . GLU   A  1  536 ? 49.543  22.687  -17.659  1.00 151.34 ? 536  GLU   A HB2  1 
ATOM   8143  H  HB3  . GLU   A  1  536 ? 50.123  23.674  -16.556  1.00 151.34 ? 536  GLU   A HB3  1 
ATOM   8144  H  HG2  . GLU   A  1  536 ? 50.183  25.370  -18.210  1.00 157.89 ? 536  GLU   A HG2  1 
ATOM   8145  H  HG3  . GLU   A  1  536 ? 49.418  24.377  -19.187  1.00 157.89 ? 536  GLU   A HG3  1 
ATOM   8146  N  N    . GLU   A  1  537 ? 53.144  24.079  -16.398  1.00 118.72 ? 537  GLU   A N    1 
ATOM   8147  C  CA   . GLU   A  1  537 ? 54.057  24.154  -15.268  1.00 114.39 ? 537  GLU   A CA   1 
ATOM   8148  C  C    . GLU   A  1  537 ? 53.521  25.096  -14.195  1.00 109.89 ? 537  GLU   A C    1 
ATOM   8149  O  O    . GLU   A  1  537 ? 52.799  26.054  -14.485  1.00 109.74 ? 537  GLU   A O    1 
ATOM   8150  C  CB   . GLU   A  1  537 ? 55.441  24.653  -15.699  1.00 116.80 ? 537  GLU   A CB   1 
ATOM   8151  C  CG   . GLU   A  1  537 ? 56.322  23.639  -16.399  1.00 114.69 ? 537  GLU   A CG   1 
ATOM   8152  C  CD   . GLU   A  1  537 ? 57.748  24.137  -16.542  1.00 118.19 ? 537  GLU   A CD   1 
ATOM   8153  O  OE1  . GLU   A  1  537 ? 58.378  24.433  -15.504  1.00 119.25 ? 537  GLU   A OE1  1 
ATOM   8154  O  OE2  . GLU   A  1  537 ? 58.232  24.252  -17.687  1.00 120.99 ? 537  GLU   A OE2  1 
ATOM   8155  H  H    . GLU   A  1  537 ? 53.097  24.813  -16.843  1.00 142.51 ? 537  GLU   A H    1 
ATOM   8156  H  HA   . GLU   A  1  537 ? 54.142  23.265  -14.889  1.00 137.31 ? 537  GLU   A HA   1 
ATOM   8157  H  HB2  . GLU   A  1  537 ? 55.319  25.397  -16.310  1.00 140.20 ? 537  GLU   A HB2  1 
ATOM   8158  H  HB3  . GLU   A  1  537 ? 55.918  24.949  -14.908  1.00 140.20 ? 537  GLU   A HB3  1 
ATOM   8159  H  HG2  . GLU   A  1  537 ? 56.337  22.817  -15.883  1.00 137.66 ? 537  GLU   A HG2  1 
ATOM   8160  H  HG3  . GLU   A  1  537 ? 55.970  23.467  -17.286  1.00 137.66 ? 537  GLU   A HG3  1 
ATOM   8161  N  N    . LEU   A  1  538 ? 53.896  24.812  -12.949  1.00 103.89 ? 538  LEU   A N    1 
ATOM   8162  C  CA   . LEU   A  1  538 ? 53.704  25.737  -11.840  1.00 103.06 ? 538  LEU   A CA   1 
ATOM   8163  C  C    . LEU   A  1  538 ? 54.767  25.422  -10.793  1.00 101.05 ? 538  LEU   A C    1 
ATOM   8164  O  O    . LEU   A  1  538 ? 55.516  24.451  -10.920  1.00 100.10 ? 538  LEU   A O    1 
ATOM   8165  C  CB   . LEU   A  1  538 ? 52.283  25.656  -11.271  1.00 100.33 ? 538  LEU   A CB   1 
ATOM   8166  C  CG   . LEU   A  1  538 ? 51.946  24.629  -10.190  1.00 96.59  ? 538  LEU   A CG   1 
ATOM   8167  C  CD1  . LEU   A  1  538 ? 50.581  24.967  -9.607   1.00 95.40  ? 538  LEU   A CD1  1 
ATOM   8168  C  CD2  . LEU   A  1  538 ? 51.962  23.209  -10.732  1.00 94.30  ? 538  LEU   A CD2  1 
ATOM   8169  H  H    . LEU   A  1  538 ? 54.272  24.074  -12.717  1.00 124.70 ? 538  LEU   A H    1 
ATOM   8170  H  HA   . LEU   A  1  538 ? 53.831  26.652  -12.138  1.00 123.71 ? 538  LEU   A HA   1 
ATOM   8171  H  HB2  . LEU   A  1  538 ? 52.077  26.525  -10.890  1.00 120.43 ? 538  LEU   A HB2  1 
ATOM   8172  H  HB3  . LEU   A  1  538 ? 51.687  25.471  -12.013  1.00 120.43 ? 538  LEU   A HB3  1 
ATOM   8173  H  HG   . LEU   A  1  538 ? 52.619  24.662  -9.492   1.00 115.95 ? 538  LEU   A HG   1 
ATOM   8174  H  HD11 . LEU   A  1  538 ? 50.347  24.300  -8.943   1.00 114.52 ? 538  LEU   A HD11 1 
ATOM   8175  H  HD12 . LEU   A  1  538 ? 50.623  25.844  -9.195   1.00 114.52 ? 538  LEU   A HD12 1 
ATOM   8176  H  HD13 . LEU   A  1  538 ? 49.925  24.969  -10.321  1.00 114.52 ? 538  LEU   A HD13 1 
ATOM   8177  H  HD21 . LEU   A  1  538 ? 51.738  22.594  -10.016  1.00 113.20 ? 538  LEU   A HD21 1 
ATOM   8178  H  HD22 . LEU   A  1  538 ? 51.310  23.136  -11.446  1.00 113.20 ? 538  LEU   A HD22 1 
ATOM   8179  H  HD23 . LEU   A  1  538 ? 52.849  23.011  -11.073  1.00 113.20 ? 538  LEU   A HD23 1 
ATOM   8180  N  N    . ILE   A  1  539 ? 54.837  26.255  -9.755   1.00 101.09 ? 539  ILE   A N    1 
ATOM   8181  C  CA   . ILE   A  1  539 ? 55.933  26.205  -8.792   1.00 101.54 ? 539  ILE   A CA   1 
ATOM   8182  C  C    . ILE   A  1  539 ? 55.380  26.152  -7.374   1.00 100.82 ? 539  ILE   A C    1 
ATOM   8183  O  O    . ILE   A  1  539 ? 54.399  26.831  -7.051   1.00 104.74 ? 539  ILE   A O    1 
ATOM   8184  C  CB   . ILE   A  1  539 ? 56.883  27.410  -8.973   1.00 107.69 ? 539  ILE   A CB   1 
ATOM   8185  C  CG1  . ILE   A  1  539 ? 57.613  27.289  -10.315  1.00 106.45 ? 539  ILE   A CG1  1 
ATOM   8186  C  CG2  . ILE   A  1  539 ? 57.878  27.493  -7.819   1.00 109.33 ? 539  ILE   A CG2  1 
ATOM   8187  C  CD1  . ILE   A  1  539 ? 58.385  28.523  -10.728  1.00 106.78 ? 539  ILE   A CD1  1 
ATOM   8188  H  H    . ILE   A  1  539 ? 54.253  26.864  -9.587   1.00 121.35 ? 539  ILE   A H    1 
ATOM   8189  H  HA   . ILE   A  1  539 ? 56.433  25.385  -8.929   1.00 121.89 ? 539  ILE   A HA   1 
ATOM   8190  H  HB   . ILE   A  1  539 ? 56.359  28.226  -8.970   1.00 129.27 ? 539  ILE   A HB   1 
ATOM   8191  H  HG12 . ILE   A  1  539 ? 58.245  26.555  -10.258  1.00 127.78 ? 539  ILE   A HG12 1 
ATOM   8192  H  HG13 . ILE   A  1  539 ? 56.958  27.109  -11.008  1.00 127.78 ? 539  ILE   A HG13 1 
ATOM   8193  H  HG21 . ILE   A  1  539 ? 58.509  28.208  -7.997   1.00 131.24 ? 539  ILE   A HG21 1 
ATOM   8194  H  HG22 . ILE   A  1  539 ? 57.395  27.676  -6.998   1.00 131.24 ? 539  ILE   A HG22 1 
ATOM   8195  H  HG23 . ILE   A  1  539 ? 58.348  26.648  -7.745   1.00 131.24 ? 539  ILE   A HG23 1 
ATOM   8196  H  HD11 . ILE   A  1  539 ? 58.772  28.374  -11.605  1.00 128.18 ? 539  ILE   A HD11 1 
ATOM   8197  H  HD12 . ILE   A  1  539 ? 57.778  29.279  -10.758  1.00 128.18 ? 539  ILE   A HD12 1 
ATOM   8198  H  HD13 . ILE   A  1  539 ? 59.087  28.688  -10.080  1.00 128.18 ? 539  ILE   A HD13 1 
ATOM   8199  N  N    . ALA   A  1  540 ? 56.028  25.351  -6.526   1.00 99.60  ? 540  ALA   A N    1 
ATOM   8200  C  CA   . ALA   A  1  540 ? 55.641  25.139  -5.136   1.00 101.60 ? 540  ALA   A CA   1 
ATOM   8201  C  C    . ALA   A  1  540 ? 56.870  25.289  -4.243   1.00 105.95 ? 540  ALA   A C    1 
ATOM   8202  O  O    . ALA   A  1  540 ? 57.983  25.530  -4.721   1.00 107.95 ? 540  ALA   A O    1 
ATOM   8203  C  CB   . ALA   A  1  540 ? 54.997  23.759  -4.950   1.00 97.89  ? 540  ALA   A CB   1 
ATOM   8204  H  H    . ALA   A  1  540 ? 56.727  24.900  -6.746   1.00 119.56 ? 540  ALA   A H    1 
ATOM   8205  H  HA   . ALA   A  1  540 ? 54.995  25.817  -4.879   1.00 121.95 ? 540  ALA   A HA   1 
ATOM   8206  H  HB1  . ALA   A  1  540 ? 54.741  23.653  -4.020   1.00 117.50 ? 540  ALA   A HB1  1 
ATOM   8207  H  HB2  . ALA   A  1  540 ? 54.213  23.697  -5.518   1.00 117.50 ? 540  ALA   A HB2  1 
ATOM   8208  H  HB3  . ALA   A  1  540 ? 55.639  23.075  -5.196   1.00 117.50 ? 540  ALA   A HB3  1 
ATOM   8209  N  N    . TYR   A  1  541 ? 56.673  25.135  -2.933   1.00 109.36 ? 541  TYR   A N    1 
ATOM   8210  C  CA   . TYR   A  1  541 ? 57.750  25.344  -1.971   1.00 112.26 ? 541  TYR   A CA   1 
ATOM   8211  C  C    . TYR   A  1  541 ? 57.439  24.572  -0.691   1.00 113.23 ? 541  TYR   A C    1 
ATOM   8212  O  O    . TYR   A  1  541 ? 56.413  23.893  -0.584   1.00 112.47 ? 541  TYR   A O    1 
ATOM   8213  C  CB   . TYR   A  1  541 ? 57.952  26.839  -1.697   1.00 116.02 ? 541  TYR   A CB   1 
ATOM   8214  C  CG   . TYR   A  1  541 ? 56.856  27.488  -0.879   1.00 118.60 ? 541  TYR   A CG   1 
ATOM   8215  C  CD1  . TYR   A  1  541 ? 55.671  27.906  -1.470   1.00 119.14 ? 541  TYR   A CD1  1 
ATOM   8216  C  CD2  . TYR   A  1  541 ? 57.016  27.697  0.483    1.00 119.36 ? 541  TYR   A CD2  1 
ATOM   8217  C  CE1  . TYR   A  1  541 ? 54.673  28.505  -0.723   1.00 122.18 ? 541  TYR   A CE1  1 
ATOM   8218  C  CE2  . TYR   A  1  541 ? 56.025  28.294  1.238    1.00 122.80 ? 541  TYR   A CE2  1 
ATOM   8219  C  CZ   . TYR   A  1  541 ? 54.855  28.697  0.630    1.00 124.57 ? 541  TYR   A CZ   1 
ATOM   8220  O  OH   . TYR   A  1  541 ? 53.865  29.293  1.377    1.00 129.89 ? 541  TYR   A OH   1 
ATOM   8221  H  H    . TYR   A  1  541 ? 55.923  24.911  -2.579   1.00 131.26 ? 541  TYR   A H    1 
ATOM   8222  H  HA   . TYR   A  1  541 ? 58.571  24.978  -2.337   1.00 134.75 ? 541  TYR   A HA   1 
ATOM   8223  H  HB2  . TYR   A  1  541 ? 58.785  26.954  -1.213   1.00 139.26 ? 541  TYR   A HB2  1 
ATOM   8224  H  HB3  . TYR   A  1  541 ? 57.996  27.304  -2.547   1.00 139.26 ? 541  TYR   A HB3  1 
ATOM   8225  H  HD1  . TYR   A  1  541 ? 55.547  27.781  -2.383   1.00 143.00 ? 541  TYR   A HD1  1 
ATOM   8226  H  HD2  . TYR   A  1  541 ? 57.805  27.430  0.896    1.00 143.27 ? 541  TYR   A HD2  1 
ATOM   8227  H  HE1  . TYR   A  1  541 ? 53.883  28.777  -1.131   1.00 146.66 ? 541  TYR   A HE1  1 
ATOM   8228  H  HE2  . TYR   A  1  541 ? 56.146  28.424  2.151    1.00 147.40 ? 541  TYR   A HE2  1 
ATOM   8229  H  HH   . TYR   A  1  541 ? 54.060  29.259  2.193    1.00 155.90 ? 541  TYR   A HH   1 
ATOM   8230  N  N    . LEU   A  1  542 ? 58.347  24.676  0.282    1.00 116.84 ? 542  LEU   A N    1 
ATOM   8231  C  CA   . LEU   A  1  542 ? 58.250  23.978  1.557    1.00 118.33 ? 542  LEU   A CA   1 
ATOM   8232  C  C    . LEU   A  1  542 ? 58.000  24.962  2.695    1.00 124.07 ? 542  LEU   A C    1 
ATOM   8233  O  O    . LEU   A  1  542 ? 58.364  26.139  2.613    1.00 128.87 ? 542  LEU   A O    1 
ATOM   8234  C  CB   . LEU   A  1  542 ? 59.533  23.190  1.863    1.00 115.16 ? 542  LEU   A CB   1 
ATOM   8235  C  CG   . LEU   A  1  542 ? 59.701  21.756  1.355    1.00 112.87 ? 542  LEU   A CG   1 
ATOM   8236  C  CD1  . LEU   A  1  542 ? 61.056  21.211  1.795    1.00 110.92 ? 542  LEU   A CD1  1 
ATOM   8237  C  CD2  . LEU   A  1  542 ? 58.585  20.850  1.850    1.00 113.82 ? 542  LEU   A CD2  1 
ATOM   8238  H  H    . LEU   A  1  542 ? 59.053  25.163  0.220    1.00 140.24 ? 542  LEU   A H    1 
ATOM   8239  H  HA   . LEU   A  1  542 ? 57.504  23.360  1.511    1.00 142.03 ? 542  LEU   A HA   1 
ATOM   8240  H  HB2  . LEU   A  1  542 ? 60.273  23.695  1.490    1.00 138.22 ? 542  LEU   A HB2  1 
ATOM   8241  H  HB3  . LEU   A  1  542 ? 59.616  23.144  2.828    1.00 138.22 ? 542  LEU   A HB3  1 
ATOM   8242  H  HG   . LEU   A  1  542 ? 59.657  21.762  0.386    1.00 135.48 ? 542  LEU   A HG   1 
ATOM   8243  H  HD11 . LEU   A  1  542 ? 61.154  20.304  1.465    1.00 133.13 ? 542  LEU   A HD11 1 
ATOM   8244  H  HD12 . LEU   A  1  542 ? 61.757  21.773  1.428    1.00 133.13 ? 542  LEU   A HD12 1 
ATOM   8245  H  HD13 . LEU   A  1  542 ? 61.100  21.217  2.764    1.00 133.13 ? 542  LEU   A HD13 1 
ATOM   8246  H  HD21 . LEU   A  1  542 ? 58.752  19.946  1.543    1.00 136.62 ? 542  LEU   A HD21 1 
ATOM   8247  H  HD22 . LEU   A  1  542 ? 58.567  20.872  2.820    1.00 136.62 ? 542  LEU   A HD22 1 
ATOM   8248  H  HD23 . LEU   A  1  542 ? 57.739  21.169  1.498    1.00 136.62 ? 542  LEU   A HD23 1 
ATOM   8249  N  N    . ARG   A  1  543 ? 57.389  24.461  3.768    1.00 123.97 ? 543  ARG   A N    1 
ATOM   8250  C  CA   . ARG   A  1  543 ? 57.178  25.250  4.970    1.00 129.16 ? 543  ARG   A CA   1 
ATOM   8251  C  C    . ARG   A  1  543 ? 58.487  25.399  5.747    1.00 133.59 ? 543  ARG   A C    1 
ATOM   8252  O  O    . ARG   A  1  543 ? 59.500  24.764  5.443    1.00 138.41 ? 543  ARG   A O    1 
ATOM   8253  C  CB   . ARG   A  1  543 ? 56.125  24.602  5.869    1.00 128.54 ? 543  ARG   A CB   1 
ATOM   8254  C  CG   . ARG   A  1  543 ? 54.760  24.367  5.236    1.00 126.14 ? 543  ARG   A CG   1 
ATOM   8255  C  CD   . ARG   A  1  543 ? 53.857  23.628  6.220    1.00 123.34 ? 543  ARG   A CD   1 
ATOM   8256  N  NE   . ARG   A  1  543 ? 52.461  23.556  5.793    1.00 123.48 ? 543  ARG   A NE   1 
ATOM   8257  C  CZ   . ARG   A  1  543 ? 51.502  24.391  6.192    1.00 128.33 ? 543  ARG   A CZ   1 
ATOM   8258  N  NH1  . ARG   A  1  543 ? 50.262  24.231  5.749    1.00 129.03 ? 543  ARG   A NH1  1 
ATOM   8259  N  NH2  . ARG   A  1  543 ? 51.773  25.384  7.029    1.00 132.94 ? 543  ARG   A NH2  1 
ATOM   8260  H  H    . ARG   A  1  543 ? 57.087  23.657  3.821    1.00 148.80 ? 543  ARG   A H    1 
ATOM   8261  H  HA   . ARG   A  1  543 ? 56.862  26.129  4.710    1.00 155.03 ? 543  ARG   A HA   1 
ATOM   8262  H  HB2  . ARG   A  1  543 ? 56.460  23.738  6.156    1.00 154.29 ? 543  ARG   A HB2  1 
ATOM   8263  H  HB3  . ARG   A  1  543 ? 55.988  25.176  6.639    1.00 154.29 ? 543  ARG   A HB3  1 
ATOM   8264  H  HG2  . ARG   A  1  543 ? 54.351  25.218  5.013    1.00 151.40 ? 543  ARG   A HG2  1 
ATOM   8265  H  HG3  . ARG   A  1  543 ? 54.859  23.827  4.436    1.00 151.40 ? 543  ARG   A HG3  1 
ATOM   8266  H  HD2  . ARG   A  1  543 ? 54.183  22.720  6.323    1.00 148.04 ? 543  ARG   A HD2  1 
ATOM   8267  H  HD3  . ARG   A  1  543 ? 53.883  24.089  7.073    1.00 148.04 ? 543  ARG   A HD3  1 
ATOM   8268  H  HE   . ARG   A  1  543 ? 52.242  22.930  5.245    1.00 148.21 ? 543  ARG   A HE   1 
ATOM   8269  H  HH11 . ARG   A  1  543 ? 50.079  23.590  5.205    1.00 154.87 ? 543  ARG   A HH11 1 
ATOM   8270  H  HH12 . ARG   A  1  543 ? 49.642  24.768  6.005    1.00 154.87 ? 543  ARG   A HH12 1 
ATOM   8271  H  HH21 . ARG   A  1  543 ? 52.575  25.494  7.320    1.00 159.56 ? 543  ARG   A HH21 1 
ATOM   8272  H  HH22 . ARG   A  1  543 ? 51.147  25.917  7.281    1.00 159.56 ? 543  ARG   A HH22 1 
ATOM   8273  N  N    . ASP   A  1  544 ? 58.454  26.246  6.774    1.00 136.52 ? 544  ASP   A N    1 
ATOM   8274  C  CA   . ASP   A  1  544 ? 59.614  26.411  7.638    1.00 137.63 ? 544  ASP   A CA   1 
ATOM   8275  C  C    . ASP   A  1  544 ? 59.848  25.154  8.471    1.00 138.09 ? 544  ASP   A C    1 
ATOM   8276  O  O    . ASP   A  1  544 ? 58.917  24.409  8.791    1.00 138.42 ? 544  ASP   A O    1 
ATOM   8277  C  CB   . ASP   A  1  544 ? 59.437  27.619  8.559    1.00 140.71 ? 544  ASP   A CB   1 
ATOM   8278  C  CG   . ASP   A  1  544 ? 60.015  28.892  7.970    1.00 141.00 ? 544  ASP   A CG   1 
ATOM   8279  O  OD1  . ASP   A  1  544 ? 60.061  29.008  6.727    1.00 138.60 ? 544  ASP   A OD1  1 
ATOM   8280  O  OD2  . ASP   A  1  544 ? 60.438  29.771  8.751    1.00 143.08 ? 544  ASP   A OD2  1 
ATOM   8281  H  H    . ASP   A  1  544 ? 57.777  26.731  6.989    1.00 163.86 ? 544  ASP   A H    1 
ATOM   8282  H  HA   . ASP   A  1  544 ? 60.399  26.566  7.090    1.00 165.20 ? 544  ASP   A HA   1 
ATOM   8283  H  HB2  . ASP   A  1  544 ? 58.490  27.762  8.715    1.00 168.88 ? 544  ASP   A HB2  1 
ATOM   8284  H  HB3  . ASP   A  1  544 ? 59.889  27.445  9.400    1.00 168.88 ? 544  ASP   A HB3  1 
ATOM   8285  N  N    . GLU   A  1  545 ? 61.116  24.926  8.826    1.00 136.59 ? 545  GLU   A N    1 
ATOM   8286  C  CA   . GLU   A  1  545 ? 61.473  23.734  9.590    1.00 134.91 ? 545  GLU   A CA   1 
ATOM   8287  C  C    . GLU   A  1  545 ? 60.654  23.626  10.870   1.00 134.88 ? 545  GLU   A C    1 
ATOM   8288  O  O    . GLU   A  1  545 ? 60.252  22.528  11.271   1.00 133.28 ? 545  GLU   A O    1 
ATOM   8289  C  CB   . GLU   A  1  545 ? 62.966  23.751  9.925    1.00 138.51 ? 545  GLU   A CB   1 
ATOM   8290  C  CG   . GLU   A  1  545 ? 63.890  23.606  8.727    1.00 141.74 ? 545  GLU   A CG   1 
ATOM   8291  C  CD   . GLU   A  1  545 ? 65.353  23.565  9.127    1.00 148.74 ? 545  GLU   A CD   1 
ATOM   8292  O  OE1  . GLU   A  1  545 ? 65.681  24.047  10.232   1.00 152.62 ? 545  GLU   A OE1  1 
ATOM   8293  O  OE2  . GLU   A  1  545 ? 66.173  23.046  8.341    1.00 149.49 ? 545  GLU   A OE2  1 
ATOM   8294  H  H    . GLU   A  1  545 ? 61.779  25.441  8.638    1.00 163.95 ? 545  GLU   A H    1 
ATOM   8295  H  HA   . GLU   A  1  545 ? 61.290  22.954  9.044    1.00 161.92 ? 545  GLU   A HA   1 
ATOM   8296  H  HB2  . GLU   A  1  545 ? 63.175  24.596  10.354   1.00 166.25 ? 545  GLU   A HB2  1 
ATOM   8297  H  HB3  . GLU   A  1  545 ? 63.154  23.017  10.530   1.00 166.25 ? 545  GLU   A HB3  1 
ATOM   8298  H  HG2  . GLU   A  1  545 ? 63.681  22.780  8.264    1.00 170.12 ? 545  GLU   A HG2  1 
ATOM   8299  H  HG3  . GLU   A  1  545 ? 63.761  24.361  8.133    1.00 170.12 ? 545  GLU   A HG3  1 
ATOM   8300  N  N    . SER   A  1  546 ? 60.398  24.761  11.526   1.00 134.31 ? 546  SER   A N    1 
ATOM   8301  C  CA   . SER   A  1  546 ? 59.697  24.740  12.805   1.00 135.75 ? 546  SER   A CA   1 
ATOM   8302  C  C    . SER   A  1  546 ? 58.299  24.151  12.682   1.00 130.56 ? 546  SER   A C    1 
ATOM   8303  O  O    . SER   A  1  546 ? 57.794  23.548  13.636   1.00 127.36 ? 546  SER   A O    1 
ATOM   8304  C  CB   . SER   A  1  546 ? 59.615  26.158  13.370   1.00 145.84 ? 546  SER   A CB   1 
ATOM   8305  O  OG   . SER   A  1  546 ? 59.093  27.053  12.401   1.00 149.42 ? 546  SER   A OG   1 
ATOM   8306  H  H    . SER   A  1  546 ? 60.617  25.546  11.253   1.00 161.21 ? 546  SER   A H    1 
ATOM   8307  H  HA   . SER   A  1  546 ? 60.200  24.186  13.422   1.00 162.94 ? 546  SER   A HA   1 
ATOM   8308  H  HB2  . SER   A  1  546 ? 59.032  26.156  14.145   1.00 175.05 ? 546  SER   A HB2  1 
ATOM   8309  H  HB3  . SER   A  1  546 ? 60.504  26.449  13.624   1.00 175.05 ? 546  SER   A HB3  1 
ATOM   8310  H  HG   . SER   A  1  546 ? 59.120  27.840  12.694   1.00 179.34 ? 546  SER   A HG   1 
ATOM   8311  N  N    . GLU   A  1  547 ? 57.659  24.310  11.524   1.00 128.83 ? 547  GLU   A N    1 
ATOM   8312  C  CA   . GLU   A  1  547 ? 56.253  23.946  11.402   1.00 128.89 ? 547  GLU   A CA   1 
ATOM   8313  C  C    . GLU   A  1  547 ? 56.047  22.442  11.268   1.00 122.80 ? 547  GLU   A C    1 
ATOM   8314  O  O    . GLU   A  1  547 ? 54.982  21.938  11.638   1.00 122.18 ? 547  GLU   A O    1 
ATOM   8315  C  CB   . GLU   A  1  547 ? 55.632  24.677  10.212   1.00 130.73 ? 547  GLU   A CB   1 
ATOM   8316  C  CG   . GLU   A  1  547 ? 55.811  26.187  10.280   1.00 133.42 ? 547  GLU   A CG   1 
ATOM   8317  C  CD   . GLU   A  1  547 ? 54.899  26.935  9.329    1.00 134.10 ? 547  GLU   A CD   1 
ATOM   8318  O  OE1  . GLU   A  1  547 ? 54.072  26.285  8.656    1.00 132.07 ? 547  GLU   A OE1  1 
ATOM   8319  O  OE2  . GLU   A  1  547 ? 55.008  28.178  9.257    1.00 136.78 ? 547  GLU   A OE2  1 
ATOM   8320  H  H    . GLU   A  1  547 ? 58.012  24.623  10.805   1.00 154.63 ? 547  GLU   A H    1 
ATOM   8321  H  HA   . GLU   A  1  547 ? 55.788  24.226  12.206   1.00 154.71 ? 547  GLU   A HA   1 
ATOM   8322  H  HB2  . GLU   A  1  547 ? 56.052  24.363  9.396    1.00 156.91 ? 547  GLU   A HB2  1 
ATOM   8323  H  HB3  . GLU   A  1  547 ? 54.681  24.489  10.188   1.00 156.91 ? 547  GLU   A HB3  1 
ATOM   8324  H  HG2  . GLU   A  1  547 ? 55.614  26.487  11.182   1.00 160.14 ? 547  GLU   A HG2  1 
ATOM   8325  H  HG3  . GLU   A  1  547 ? 56.728  26.406  10.051   1.00 160.14 ? 547  GLU   A HG3  1 
ATOM   8326  N  N    . PHE   A  1  548 ? 57.035  21.709  10.755   1.00 118.86 ? 548  PHE   A N    1 
ATOM   8327  C  CA   . PHE   A  1  548 ? 56.917  20.262  10.615   1.00 116.14 ? 548  PHE   A CA   1 
ATOM   8328  C  C    . PHE   A  1  548 ? 58.221  19.607  11.042   1.00 119.34 ? 548  PHE   A C    1 
ATOM   8329  O  O    . PHE   A  1  548 ? 59.278  19.889  10.470   1.00 120.13 ? 548  PHE   A O    1 
ATOM   8330  C  CB   . PHE   A  1  548 ? 56.559  19.869  9.174    1.00 109.73 ? 548  PHE   A CB   1 
ATOM   8331  C  CG   . PHE   A  1  548 ? 57.630  20.179  8.162    1.00 106.18 ? 548  PHE   A CG   1 
ATOM   8332  C  CD1  . PHE   A  1  548 ? 57.708  21.431  7.573    1.00 106.95 ? 548  PHE   A CD1  1 
ATOM   8333  C  CD2  . PHE   A  1  548 ? 58.543  19.207  7.779    1.00 102.76 ? 548  PHE   A CD2  1 
ATOM   8334  C  CE1  . PHE   A  1  548 ? 58.685  21.711  6.634    1.00 105.97 ? 548  PHE   A CE1  1 
ATOM   8335  C  CE2  . PHE   A  1  548 ? 59.520  19.483  6.840    1.00 102.19 ? 548  PHE   A CE2  1 
ATOM   8336  C  CZ   . PHE   A  1  548 ? 59.591  20.735  6.267    1.00 103.84 ? 548  PHE   A CZ   1 
ATOM   8337  H  H    . PHE   A  1  548 ? 57.784  22.030  10.482   1.00 142.67 ? 548  PHE   A H    1 
ATOM   8338  H  HA   . PHE   A  1  548 ? 56.216  19.943  11.204   1.00 139.41 ? 548  PHE   A HA   1 
ATOM   8339  H  HB2  . PHE   A  1  548 ? 56.396  18.913  9.146    1.00 131.71 ? 548  PHE   A HB2  1 
ATOM   8340  H  HB3  . PHE   A  1  548 ? 55.759  20.350  8.912    1.00 131.71 ? 548  PHE   A HB3  1 
ATOM   8341  H  HD1  . PHE   A  1  548 ? 57.097  22.090  7.812    1.00 128.38 ? 548  PHE   A HD1  1 
ATOM   8342  H  HD2  . PHE   A  1  548 ? 58.497  18.359  8.158    1.00 123.35 ? 548  PHE   A HD2  1 
ATOM   8343  H  HE1  . PHE   A  1  548 ? 58.731  22.557  6.250    1.00 127.20 ? 548  PHE   A HE1  1 
ATOM   8344  H  HE2  . PHE   A  1  548 ? 60.129  18.824  6.595    1.00 122.67 ? 548  PHE   A HE2  1 
ATOM   8345  H  HZ   . PHE   A  1  548 ? 60.247  20.922  5.635    1.00 124.65 ? 548  PHE   A HZ   1 
ATOM   8346  N  N    . ARG   A  1  549 ? 58.146  18.745  12.058   1.00 122.94 ? 549  ARG   A N    1 
ATOM   8347  C  CA   . ARG   A  1  549 ? 59.269  17.904  12.445   1.00 126.15 ? 549  ARG   A CA   1 
ATOM   8348  C  C    . ARG   A  1  549 ? 59.213  16.532  11.782   1.00 126.12 ? 549  ARG   A C    1 
ATOM   8349  O  O    . ARG   A  1  549 ? 59.770  15.568  12.319   1.00 127.80 ? 549  ARG   A O    1 
ATOM   8350  C  CB   . ARG   A  1  549 ? 59.332  17.758  13.970   1.00 129.27 ? 549  ARG   A CB   1 
ATOM   8351  C  CG   . ARG   A  1  549 ? 58.209  16.946  14.606   1.00 129.55 ? 549  ARG   A CG   1 
ATOM   8352  C  CD   . ARG   A  1  549 ? 58.465  16.725  16.098   1.00 131.02 ? 549  ARG   A CD   1 
ATOM   8353  N  NE   . ARG   A  1  549 ? 58.711  17.977  16.811   1.00 131.95 ? 549  ARG   A NE   1 
ATOM   8354  C  CZ   . ARG   A  1  549 ? 58.949  18.067  18.117   1.00 133.11 ? 549  ARG   A CZ   1 
ATOM   8355  N  NH1  . ARG   A  1  549 ? 59.161  19.253  18.670   1.00 133.94 ? 549  ARG   A NH1  1 
ATOM   8356  N  NH2  . ARG   A  1  549 ? 58.974  16.977  18.873   1.00 133.68 ? 549  ARG   A NH2  1 
ATOM   8357  H  H    . ARG   A  1  549 ? 57.444  18.631  12.541   1.00 147.56 ? 549  ARG   A H    1 
ATOM   8358  H  HA   . ARG   A  1  549 ? 60.089  18.339  12.165   1.00 151.42 ? 549  ARG   A HA   1 
ATOM   8359  H  HB2  . ARG   A  1  549 ? 60.168  17.321  14.199   1.00 155.16 ? 549  ARG   A HB2  1 
ATOM   8360  H  HB3  . ARG   A  1  549 ? 59.303  18.645  14.362   1.00 155.16 ? 549  ARG   A HB3  1 
ATOM   8361  H  HG2  . ARG   A  1  549 ? 57.370  17.422  14.506   1.00 155.50 ? 549  ARG   A HG2  1 
ATOM   8362  H  HG3  . ARG   A  1  549 ? 58.151  16.080  14.173   1.00 155.50 ? 549  ARG   A HG3  1 
ATOM   8363  H  HD2  . ARG   A  1  549 ? 57.688  16.300  16.494   1.00 157.27 ? 549  ARG   A HD2  1 
ATOM   8364  H  HD3  . ARG   A  1  549 ? 59.245  16.158  16.206   1.00 157.27 ? 549  ARG   A HD3  1 
ATOM   8365  H  HE   . ARG   A  1  549 ? 58.701  18.706  16.355   1.00 158.38 ? 549  ARG   A HE   1 
ATOM   8366  H  HH11 . ARG   A  1  549 ? 59.145  19.963  18.185   1.00 160.76 ? 549  ARG   A HH11 1 
ATOM   8367  H  HH12 . ARG   A  1  549 ? 59.315  19.313  19.514   1.00 160.76 ? 549  ARG   A HH12 1 
ATOM   8368  H  HH21 . ARG   A  1  549 ? 58.836  16.205  18.520   1.00 160.46 ? 549  ARG   A HH21 1 
ATOM   8369  H  HH22 . ARG   A  1  549 ? 59.128  17.042  19.717   1.00 160.46 ? 549  ARG   A HH22 1 
ATOM   8370  N  N    . ASP   A  1  550 ? 58.546  16.427  10.633   1.00 124.91 ? 550  ASP   A N    1 
ATOM   8371  C  CA   . ASP   A  1  550 ? 58.500  15.203  9.837    1.00 125.03 ? 550  ASP   A CA   1 
ATOM   8372  C  C    . ASP   A  1  550 ? 59.244  15.479  8.534    1.00 122.16 ? 550  ASP   A C    1 
ATOM   8373  O  O    . ASP   A  1  550 ? 58.688  16.073  7.605    1.00 122.07 ? 550  ASP   A O    1 
ATOM   8374  C  CB   . ASP   A  1  550 ? 57.063  14.766  9.572    1.00 122.82 ? 550  ASP   A CB   1 
ATOM   8375  C  CG   . ASP   A  1  550 ? 56.983  13.459  8.804    1.00 120.66 ? 550  ASP   A CG   1 
ATOM   8376  O  OD1  . ASP   A  1  550 ? 58.042  12.837  8.574    1.00 118.48 ? 550  ASP   A OD1  1 
ATOM   8377  O  OD2  . ASP   A  1  550 ? 55.862  13.054  8.430    1.00 119.96 ? 550  ASP   A OD2  1 
ATOM   8378  H  H    . ASP   A  1  550 ? 58.099  17.073  10.284   1.00 149.93 ? 550  ASP   A H    1 
ATOM   8379  H  HA   . ASP   A  1  550 ? 58.949  14.490  10.316   1.00 150.08 ? 550  ASP   A HA   1 
ATOM   8380  H  HB2  . ASP   A  1  550 ? 56.607  14.645  10.420   1.00 147.42 ? 550  ASP   A HB2  1 
ATOM   8381  H  HB3  . ASP   A  1  550 ? 56.615  15.450  9.049    1.00 147.42 ? 550  ASP   A HB3  1 
ATOM   8382  N  N    . LYS   A  1  551 ? 60.505  15.055  8.475    1.00 117.68 ? 551  LYS   A N    1 
ATOM   8383  C  CA   . LYS   A  1  551 ? 61.315  15.158  7.270    1.00 115.97 ? 551  LYS   A CA   1 
ATOM   8384  C  C    . LYS   A  1  551 ? 61.582  13.797  6.640    1.00 112.30 ? 551  LYS   A C    1 
ATOM   8385  O  O    . LYS   A  1  551 ? 62.360  13.707  5.684    1.00 107.23 ? 551  LYS   A O    1 
ATOM   8386  C  CB   . LYS   A  1  551 ? 62.640  15.853  7.585    1.00 120.69 ? 551  LYS   A CB   1 
ATOM   8387  C  CG   . LYS   A  1  551 ? 62.491  17.234  8.193    1.00 124.20 ? 551  LYS   A CG   1 
ATOM   8388  C  CD   . LYS   A  1  551 ? 63.842  17.789  8.597    1.00 125.59 ? 551  LYS   A CD   1 
ATOM   8389  C  CE   . LYS   A  1  551 ? 63.706  19.079  9.385    1.00 126.92 ? 551  LYS   A CE   1 
ATOM   8390  N  NZ   . LYS   A  1  551 ? 65.033  19.625  9.778    1.00 128.14 ? 551  LYS   A NZ   1 
ATOM   8391  H  H    . LYS   A  1  551 ? 60.920  14.696  9.137    1.00 141.25 ? 551  LYS   A H    1 
ATOM   8392  H  HA   . LYS   A  1  551 ? 60.840  15.702  6.622    1.00 139.20 ? 551  LYS   A HA   1 
ATOM   8393  H  HB2  . LYS   A  1  551 ? 63.134  15.306  8.216    1.00 144.86 ? 551  LYS   A HB2  1 
ATOM   8394  H  HB3  . LYS   A  1  551 ? 63.145  15.947  6.762    1.00 144.86 ? 551  LYS   A HB3  1 
ATOM   8395  H  HG2  . LYS   A  1  551 ? 62.093  17.833  7.542    1.00 149.07 ? 551  LYS   A HG2  1 
ATOM   8396  H  HG3  . LYS   A  1  551 ? 61.930  17.182  8.983    1.00 149.07 ? 551  LYS   A HG3  1 
ATOM   8397  H  HD2  . LYS   A  1  551 ? 64.302  17.141  9.152    1.00 150.75 ? 551  LYS   A HD2  1 
ATOM   8398  H  HD3  . LYS   A  1  551 ? 64.364  17.973  7.800    1.00 150.75 ? 551  LYS   A HD3  1 
ATOM   8399  H  HE2  . LYS   A  1  551 ? 63.254  19.742  8.839    1.00 152.34 ? 551  LYS   A HE2  1 
ATOM   8400  H  HE3  . LYS   A  1  551 ? 63.196  18.909  10.192   1.00 152.34 ? 551  LYS   A HE3  1 
ATOM   8401  H  HZ1  . LYS   A  1  551 ? 64.949  20.473  10.037   1.00 153.81 ? 551  LYS   A HZ1  1 
ATOM   8402  H  HZ2  . LYS   A  1  551 ? 65.371  19.150  10.450   1.00 153.81 ? 551  LYS   A HZ2  1 
ATOM   8403  H  HZ3  . LYS   A  1  551 ? 65.594  19.589  9.088    1.00 153.81 ? 551  LYS   A HZ3  1 
ATOM   8404  N  N    . LEU   A  1  552 ? 60.951  12.739  7.151    1.00 109.17 ? 552  LEU   A N    1 
ATOM   8405  C  CA   . LEU   A  1  552 ? 61.226  11.378  6.704    1.00 108.55 ? 552  LEU   A CA   1 
ATOM   8406  C  C    . LEU   A  1  552 ? 60.254  10.925  5.618    1.00 107.22 ? 552  LEU   A C    1 
ATOM   8407  O  O    . LEU   A  1  552 ? 60.668  10.627  4.493    1.00 107.92 ? 552  LEU   A O    1 
ATOM   8408  C  CB   . LEU   A  1  552 ? 61.170  10.418  7.899    1.00 108.32 ? 552  LEU   A CB   1 
ATOM   8409  C  CG   . LEU   A  1  552 ? 62.500  9.969   8.506    1.00 107.42 ? 552  LEU   A CG   1 
ATOM   8410  C  CD1  . LEU   A  1  552 ? 63.353  11.156  8.928    1.00 108.61 ? 552  LEU   A CD1  1 
ATOM   8411  C  CD2  . LEU   A  1  552 ? 62.237  9.046   9.688    1.00 109.64 ? 552  LEU   A CD2  1 
ATOM   8412  H  H    . LEU   A  1  552 ? 60.352  12.787  7.766    1.00 131.04 ? 552  LEU   A H    1 
ATOM   8413  H  HA   . LEU   A  1  552 ? 62.120  11.356  6.330    1.00 130.30 ? 552  LEU   A HA   1 
ATOM   8414  H  HB2  . LEU   A  1  552 ? 60.671  10.855  8.607    1.00 130.03 ? 552  LEU   A HB2  1 
ATOM   8415  H  HB3  . LEU   A  1  552 ? 60.707  9.616   7.613    1.00 130.03 ? 552  LEU   A HB3  1 
ATOM   8416  H  HG   . LEU   A  1  552 ? 63.006  9.484   7.835    1.00 128.95 ? 552  LEU   A HG   1 
ATOM   8417  H  HD11 . LEU   A  1  552 ? 64.174  10.829  9.328    1.00 130.36 ? 552  LEU   A HD11 1 
ATOM   8418  H  HD12 . LEU   A  1  552 ? 63.558  11.692  8.145    1.00 130.36 ? 552  LEU   A HD12 1 
ATOM   8419  H  HD13 . LEU   A  1  552 ? 62.859  11.687  9.572    1.00 130.36 ? 552  LEU   A HD13 1 
ATOM   8420  H  HD21 . LEU   A  1  552 ? 63.084  8.723   10.032   1.00 131.60 ? 552  LEU   A HD21 1 
ATOM   8421  H  HD22 . LEU   A  1  552 ? 61.767  9.541   10.377   1.00 131.60 ? 552  LEU   A HD22 1 
ATOM   8422  H  HD23 . LEU   A  1  552 ? 61.695  8.298   9.389    1.00 131.60 ? 552  LEU   A HD23 1 
ATOM   8423  N  N    . THR   A  1  553 ? 58.965  10.857  5.941    1.00 105.15 ? 553  THR   A N    1 
ATOM   8424  C  CA   . THR   A  1  553 ? 57.993  10.357  4.979    1.00 99.22  ? 553  THR   A CA   1 
ATOM   8425  C  C    . THR   A  1  553 ? 58.078  11.181  3.698    1.00 92.79  ? 553  THR   A C    1 
ATOM   8426  O  O    . THR   A  1  553 ? 58.114  12.418  3.765    1.00 91.33  ? 553  THR   A O    1 
ATOM   8427  C  CB   . THR   A  1  553 ? 56.568  10.416  5.533    1.00 100.19 ? 553  THR   A CB   1 
ATOM   8428  O  OG1  . THR   A  1  553 ? 56.174  11.782  5.713    1.00 101.39 ? 553  THR   A OG1  1 
ATOM   8429  C  CG2  . THR   A  1  553 ? 56.467  9.674   6.859    1.00 103.25 ? 553  THR   A CG2  1 
ATOM   8430  H  H    . THR   A  1  553 ? 58.634  11.092  6.699    1.00 126.22 ? 553  THR   A H    1 
ATOM   8431  H  HA   . THR   A  1  553 ? 58.195  9.428   4.785    1.00 119.11 ? 553  THR   A HA   1 
ATOM   8432  H  HB   . THR   A  1  553 ? 55.965  9.988   4.905    1.00 120.27 ? 553  THR   A HB   1 
ATOM   8433  H  HG1  . THR   A  1  553 ? 55.336  11.843  5.700    1.00 121.71 ? 553  THR   A HG1  1 
ATOM   8434  H  HG21 . THR   A  1  553 ? 55.539  9.619   7.138    1.00 123.94 ? 553  THR   A HG21 1 
ATOM   8435  H  HG22 . THR   A  1  553 ? 56.821  8.776   6.764    1.00 123.94 ? 553  THR   A HG22 1 
ATOM   8436  H  HG23 . THR   A  1  553 ? 56.974  10.142  7.540    1.00 123.94 ? 553  THR   A HG23 1 
ATOM   8437  N  N    . PRO   A  1  554 ? 58.112  10.552  2.527    1.00 90.81  ? 554  PRO   A N    1 
ATOM   8438  C  CA   . PRO   A  1  554 ? 58.224  11.327  1.290    1.00 91.01  ? 554  PRO   A CA   1 
ATOM   8439  C  C    . PRO   A  1  554 ? 56.981  12.160  1.036    1.00 93.16  ? 554  PRO   A C    1 
ATOM   8440  O  O    . PRO   A  1  554 ? 55.862  11.779  1.387    1.00 91.61  ? 554  PRO   A O    1 
ATOM   8441  C  CB   . PRO   A  1  554 ? 58.403  10.255  0.209    1.00 90.51  ? 554  PRO   A CB   1 
ATOM   8442  C  CG   . PRO   A  1  554 ? 57.786  9.031   0.781    1.00 90.79  ? 554  PRO   A CG   1 
ATOM   8443  C  CD   . PRO   A  1  554 ? 57.996  9.105   2.266    1.00 91.22  ? 554  PRO   A CD   1 
ATOM   8444  H  HA   . PRO   A  1  554 ? 59.005  11.903  1.313    1.00 109.24 ? 554  PRO   A HA   1 
ATOM   8445  H  HB2  . PRO   A  1  554 ? 57.948  10.525  -0.604   1.00 108.64 ? 554  PRO   A HB2  1 
ATOM   8446  H  HB3  . PRO   A  1  554 ? 59.346  10.118  0.032    1.00 108.64 ? 554  PRO   A HB3  1 
ATOM   8447  H  HG2  . PRO   A  1  554 ? 56.839  9.016   0.571    1.00 108.99 ? 554  PRO   A HG2  1 
ATOM   8448  H  HG3  . PRO   A  1  554 ? 58.221  8.246   0.413    1.00 108.99 ? 554  PRO   A HG3  1 
ATOM   8449  H  HD2  . PRO   A  1  554 ? 57.238  8.729   2.740    1.00 109.50 ? 554  PRO   A HD2  1 
ATOM   8450  H  HD3  . PRO   A  1  554 ? 58.810  8.643   2.522    1.00 109.50 ? 554  PRO   A HD3  1 
ATOM   8451  N  N    . ILE   A  1  555 ? 57.195  13.317  0.420    1.00 95.68  ? 555  ILE   A N    1 
ATOM   8452  C  CA   . ILE   A  1  555 ? 56.094  14.156  -0.035   1.00 100.60 ? 555  ILE   A CA   1 
ATOM   8453  C  C    . ILE   A  1  555 ? 55.607  13.606  -1.368   1.00 107.67 ? 555  ILE   A C    1 
ATOM   8454  O  O    . ILE   A  1  555 ? 56.385  13.486  -2.321   1.00 112.76 ? 555  ILE   A O    1 
ATOM   8455  C  CB   . ILE   A  1  555 ? 56.526  15.621  -0.176   1.00 99.00  ? 555  ILE   A CB   1 
ATOM   8456  C  CG1  . ILE   A  1  555 ? 57.109  16.148  1.136    1.00 99.38  ? 555  ILE   A CG1  1 
ATOM   8457  C  CG2  . ILE   A  1  555 ? 55.341  16.470  -0.622   1.00 98.02  ? 555  ILE   A CG2  1 
ATOM   8458  C  CD1  . ILE   A  1  555 ? 58.178  17.195  0.928    1.00 98.67  ? 555  ILE   A CD1  1 
ATOM   8459  H  H    . ILE   A  1  555 ? 57.975  13.640  0.253    1.00 114.85 ? 555  ILE   A H    1 
ATOM   8460  H  HA   . ILE   A  1  555 ? 55.371  14.116  0.611    1.00 120.76 ? 555  ILE   A HA   1 
ATOM   8461  H  HB   . ILE   A  1  555 ? 57.222  15.672  -0.850   1.00 118.83 ? 555  ILE   A HB   1 
ATOM   8462  H  HG12 . ILE   A  1  555 ? 56.396  16.547  1.659    1.00 119.29 ? 555  ILE   A HG12 1 
ATOM   8463  H  HG13 . ILE   A  1  555 ? 57.504  15.408  1.624    1.00 119.29 ? 555  ILE   A HG13 1 
ATOM   8464  H  HG21 . ILE   A  1  555 ? 55.596  17.406  -0.598   1.00 117.66 ? 555  ILE   A HG21 1 
ATOM   8465  H  HG22 . ILE   A  1  555 ? 55.095  16.218  -1.526   1.00 117.66 ? 555  ILE   A HG22 1 
ATOM   8466  H  HG23 . ILE   A  1  555 ? 54.596  16.314  -0.021   1.00 117.66 ? 555  ILE   A HG23 1 
ATOM   8467  H  HD11 . ILE   A  1  555 ? 58.640  17.346  1.767    1.00 118.44 ? 555  ILE   A HD11 1 
ATOM   8468  H  HD12 . ILE   A  1  555 ? 58.804  16.878  0.258    1.00 118.44 ? 555  ILE   A HD12 1 
ATOM   8469  H  HD13 . ILE   A  1  555 ? 57.761  18.017  0.627    1.00 118.44 ? 555  ILE   A HD13 1 
ATOM   8470  N  N    . THR   A  1  556 ? 54.325  13.274  -1.441   1.00 110.77 ? 556  THR   A N    1 
ATOM   8471  C  CA   . THR   A  1  556 ? 53.723  12.787  -2.673   1.00 110.63 ? 556  THR   A CA   1 
ATOM   8472  C  C    . THR   A  1  556 ? 52.900  13.896  -3.309   1.00 106.77 ? 556  THR   A C    1 
ATOM   8473  O  O    . THR   A  1  556 ? 52.101  14.552  -2.632   1.00 109.68 ? 556  THR   A O    1 
ATOM   8474  C  CB   . THR   A  1  556 ? 52.841  11.563  -2.421   1.00 114.65 ? 556  THR   A CB   1 
ATOM   8475  O  OG1  . THR   A  1  556 ? 51.936  11.831  -1.343   1.00 118.63 ? 556  THR   A OG1  1 
ATOM   8476  C  CG2  . THR   A  1  556 ? 53.696  10.345  -2.096   1.00 113.95 ? 556  THR   A CG2  1 
ATOM   8477  H  H    . THR   A  1  556 ? 53.776  13.323  -0.781   1.00 132.96 ? 556  THR   A H    1 
ATOM   8478  H  HA   . THR   A  1  556 ? 54.427  12.527  -3.287   1.00 132.80 ? 556  THR   A HA   1 
ATOM   8479  H  HB   . THR   A  1  556 ? 52.327  11.362  -3.219   1.00 137.62 ? 556  THR   A HB   1 
ATOM   8480  H  HG1  . THR   A  1  556 ? 51.207  12.119  -1.645   1.00 142.39 ? 556  THR   A HG1  1 
ATOM   8481  H  HG21 . THR   A  1  556 ? 53.133  9.560   -2.003   1.00 136.78 ? 556  THR   A HG21 1 
ATOM   8482  H  HG22 . THR   A  1  556 ? 54.337  10.190  -2.808   1.00 136.78 ? 556  THR   A HG22 1 
ATOM   8483  H  HG23 . THR   A  1  556 ? 54.176  10.488  -1.266   1.00 136.78 ? 556  THR   A HG23 1 
ATOM   8484  N  N    . ILE   A  1  557 ? 53.110  14.108  -4.602   1.00 98.83  ? 557  ILE   A N    1 
ATOM   8485  C  CA   . ILE   A  1  557 ? 52.315  15.039  -5.392   1.00 100.51 ? 557  ILE   A CA   1 
ATOM   8486  C  C    . ILE   A  1  557 ? 51.310  14.214  -6.181   1.00 99.31  ? 557  ILE   A C    1 
ATOM   8487  O  O    . ILE   A  1  557 ? 51.692  13.337  -6.965   1.00 91.18  ? 557  ILE   A O    1 
ATOM   8488  C  CB   . ILE   A  1  557 ? 53.201  15.890  -6.315   1.00 98.40  ? 557  ILE   A CB   1 
ATOM   8489  C  CG1  . ILE   A  1  557 ? 54.030  16.871  -5.479   1.00 98.03  ? 557  ILE   A CG1  1 
ATOM   8490  C  CG2  . ILE   A  1  557 ? 52.363  16.656  -7.337   1.00 96.95  ? 557  ILE   A CG2  1 
ATOM   8491  C  CD1  . ILE   A  1  557 ? 55.502  16.534  -5.407   1.00 95.21  ? 557  ILE   A CD1  1 
ATOM   8492  H  H    . ILE   A  1  557 ? 53.724  13.713  -5.056   1.00 118.63 ? 557  ILE   A H    1 
ATOM   8493  H  HA   . ILE   A  1  557 ? 51.831  15.644  -4.809   1.00 120.65 ? 557  ILE   A HA   1 
ATOM   8494  H  HB   . ILE   A  1  557 ? 53.793  15.292  -6.797   1.00 118.11 ? 557  ILE   A HB   1 
ATOM   8495  H  HG12 . ILE   A  1  557 ? 53.950  17.755  -5.870   1.00 117.67 ? 557  ILE   A HG12 1 
ATOM   8496  H  HG13 . ILE   A  1  557 ? 53.684  16.875  -4.573   1.00 117.67 ? 557  ILE   A HG13 1 
ATOM   8497  H  HG21 . ILE   A  1  557 ? 52.948  17.000  -8.030   1.00 116.37 ? 557  ILE   A HG21 1 
ATOM   8498  H  HG22 . ILE   A  1  557 ? 51.709  16.053  -7.724   1.00 116.37 ? 557  ILE   A HG22 1 
ATOM   8499  H  HG23 . ILE   A  1  557 ? 51.912  17.389  -6.890   1.00 116.37 ? 557  ILE   A HG23 1 
ATOM   8500  H  HD11 . ILE   A  1  557 ? 55.976  17.040  -6.085   1.00 114.29 ? 557  ILE   A HD11 1 
ATOM   8501  H  HD12 . ILE   A  1  557 ? 55.836  16.767  -4.526   1.00 114.29 ? 557  ILE   A HD12 1 
ATOM   8502  H  HD13 . ILE   A  1  557 ? 55.616  15.583  -5.563   1.00 114.29 ? 557  ILE   A HD13 1 
ATOM   8503  N  N    . PHE   A  1  558 ? 50.028  14.497  -5.979   1.00 99.97  ? 558  PHE   A N    1 
ATOM   8504  C  CA   . PHE   A  1  558 ? 48.946  13.715  -6.557   1.00 96.59  ? 558  PHE   A CA   1 
ATOM   8505  C  C    . PHE   A  1  558 ? 48.227  14.533  -7.619   1.00 92.43  ? 558  PHE   A C    1 
ATOM   8506  O  O    . PHE   A  1  558 ? 47.882  15.696  -7.385   1.00 96.18  ? 558  PHE   A O    1 
ATOM   8507  C  CB   . PHE   A  1  558 ? 47.966  13.278  -5.470   1.00 99.31  ? 558  PHE   A CB   1 
ATOM   8508  C  CG   . PHE   A  1  558 ? 46.862  12.404  -5.970   1.00 95.97  ? 558  PHE   A CG   1 
ATOM   8509  C  CD1  . PHE   A  1  558 ? 47.084  11.060  -6.203   1.00 92.68  ? 558  PHE   A CD1  1 
ATOM   8510  C  CD2  . PHE   A  1  558 ? 45.600  12.922  -6.199   1.00 96.18  ? 558  PHE   A CD2  1 
ATOM   8511  C  CE1  . PHE   A  1  558 ? 46.072  10.251  -6.656   1.00 92.37  ? 558  PHE   A CE1  1 
ATOM   8512  C  CE2  . PHE   A  1  558 ? 44.582  12.116  -6.656   1.00 96.22  ? 558  PHE   A CE2  1 
ATOM   8513  C  CZ   . PHE   A  1  558 ? 44.816  10.780  -6.882   1.00 93.81  ? 558  PHE   A CZ   1 
ATOM   8514  H  H    . PHE   A  1  558 ? 49.755  15.155  -5.498   1.00 120.00 ? 558  PHE   A H    1 
ATOM   8515  H  HA   . PHE   A  1  558 ? 49.309  12.925  -6.988   1.00 115.94 ? 558  PHE   A HA   1 
ATOM   8516  H  HB2  . PHE   A  1  558 ? 48.452  12.783  -4.793   1.00 119.21 ? 558  PHE   A HB2  1 
ATOM   8517  H  HB3  . PHE   A  1  558 ? 47.563  14.068  -5.078   1.00 119.21 ? 558  PHE   A HB3  1 
ATOM   8518  H  HD1  . PHE   A  1  558 ? 47.928  10.699  -6.052   1.00 111.25 ? 558  PHE   A HD1  1 
ATOM   8519  H  HD2  . PHE   A  1  558 ? 45.438  13.824  -6.043   1.00 115.45 ? 558  PHE   A HD2  1 
ATOM   8520  H  HE1  . PHE   A  1  558 ? 46.231  9.348   -6.810   1.00 110.88 ? 558  PHE   A HE1  1 
ATOM   8521  H  HE2  . PHE   A  1  558 ? 43.738  12.475  -6.811   1.00 115.50 ? 558  PHE   A HE2  1 
ATOM   8522  H  HZ   . PHE   A  1  558 ? 44.129  10.233  -7.188   1.00 112.61 ? 558  PHE   A HZ   1 
ATOM   8523  N  N    . MET   A  1  559 ? 48.004  13.923  -8.781   1.00 87.99  ? 559  MET   A N    1 
ATOM   8524  C  CA   . MET   A  1  559 ? 47.287  14.549  -9.882   1.00 95.17  ? 559  MET   A CA   1 
ATOM   8525  C  C    . MET   A  1  559 ? 46.084  13.696  -10.259  1.00 98.82  ? 559  MET   A C    1 
ATOM   8526  O  O    . MET   A  1  559 ? 46.221  12.491  -10.496  1.00 95.82  ? 559  MET   A O    1 
ATOM   8527  C  CB   . MET   A  1  559 ? 48.197  14.731  -11.096  1.00 93.46  ? 559  MET   A CB   1 
ATOM   8528  C  CG   . MET   A  1  559 ? 47.496  15.328  -12.296  1.00 95.99  ? 559  MET   A CG   1 
ATOM   8529  S  SD   . MET   A  1  559 ? 48.426  15.037  -13.798  1.00 99.43  ? 559  MET   A SD   1 
ATOM   8530  C  CE   . MET   A  1  559 ? 47.438  15.953  -14.963  1.00 104.20 ? 559  MET   A CE   1 
ATOM   8531  H  H    . MET   A  1  559 ? 48.266  13.123  -8.957   1.00 105.62 ? 559  MET   A H    1 
ATOM   8532  H  HA   . MET   A  1  559 ? 46.979  15.424  -9.599   1.00 114.24 ? 559  MET   A HA   1 
ATOM   8533  H  HB2  . MET   A  1  559 ? 48.927  15.322  -10.854  1.00 112.19 ? 559  MET   A HB2  1 
ATOM   8534  H  HB3  . MET   A  1  559 ? 48.545  13.864  -11.358  1.00 112.19 ? 559  MET   A HB3  1 
ATOM   8535  H  HG2  . MET   A  1  559 ? 46.621  14.922  -12.393  1.00 115.22 ? 559  MET   A HG2  1 
ATOM   8536  H  HG3  . MET   A  1  559 ? 47.405  16.286  -12.172  1.00 115.22 ? 559  MET   A HG3  1 
ATOM   8537  H  HE1  . MET   A  1  559 ? 47.680  15.685  -15.863  1.00 125.07 ? 559  MET   A HE1  1 
ATOM   8538  H  HE2  . MET   A  1  559 ? 46.501  15.762  -14.802  1.00 125.07 ? 559  MET   A HE2  1 
ATOM   8539  H  HE3  . MET   A  1  559 ? 47.607  16.901  -14.844  1.00 125.07 ? 559  MET   A HE3  1 
ATOM   8540  N  N    . GLU   A  1  560 ? 44.918  14.331  -10.334  1.00 101.34 ? 560  GLU   A N    1 
ATOM   8541  C  CA   . GLU   A  1  560 ? 43.664  13.683  -10.692  1.00 102.72 ? 560  GLU   A CA   1 
ATOM   8542  C  C    . GLU   A  1  560 ? 43.071  14.403  -11.894  1.00 98.97  ? 560  GLU   A C    1 
ATOM   8543  O  O    . GLU   A  1  560 ? 43.051  15.637  -11.933  1.00 99.99  ? 560  GLU   A O    1 
ATOM   8544  C  CB   . GLU   A  1  560 ? 42.687  13.720  -9.514   1.00 108.01 ? 560  GLU   A CB   1 
ATOM   8545  C  CG   . GLU   A  1  560 ? 42.063  12.383  -9.163   1.00 109.41 ? 560  GLU   A CG   1 
ATOM   8546  C  CD   . GLU   A  1  560 ? 41.127  12.478  -7.973   1.00 113.68 ? 560  GLU   A CD   1 
ATOM   8547  O  OE1  . GLU   A  1  560 ? 40.971  13.591  -7.425   1.00 115.03 ? 560  GLU   A OE1  1 
ATOM   8548  O  OE2  . GLU   A  1  560 ? 40.548  11.442  -7.585   1.00 114.42 ? 560  GLU   A OE2  1 
ATOM   8549  H  H    . GLU   A  1  560 ? 44.826  15.171  -10.174  1.00 121.65 ? 560  GLU   A H    1 
ATOM   8550  H  HA   . GLU   A  1  560 ? 43.812  12.755  -10.932  1.00 123.30 ? 560  GLU   A HA   1 
ATOM   8551  H  HB2  . GLU   A  1  560 ? 43.162  14.035  -8.729   1.00 129.65 ? 560  GLU   A HB2  1 
ATOM   8552  H  HB3  . GLU   A  1  560 ? 41.965  14.330  -9.731   1.00 129.65 ? 560  GLU   A HB3  1 
ATOM   8553  H  HG2  . GLU   A  1  560 ? 41.554  12.061  -9.922   1.00 131.32 ? 560  GLU   A HG2  1 
ATOM   8554  H  HG3  . GLU   A  1  560 ? 42.767  11.752  -8.943   1.00 131.32 ? 560  GLU   A HG3  1 
ATOM   8555  N  N    . TYR   A  1  561 ? 42.592  13.639  -12.878  1.00 95.72  ? 561  TYR   A N    1 
ATOM   8556  C  CA   . TYR   A  1  561 ? 42.031  14.209  -14.099  1.00 93.72  ? 561  TYR   A CA   1 
ATOM   8557  C  C    . TYR   A  1  561 ? 40.715  13.522  -14.426  1.00 98.05  ? 561  TYR   A C    1 
ATOM   8558  O  O    . TYR   A  1  561 ? 40.678  12.305  -14.638  1.00 94.62  ? 561  TYR   A O    1 
ATOM   8559  C  CB   . TYR   A  1  561 ? 43.017  14.096  -15.271  1.00 90.35  ? 561  TYR   A CB   1 
ATOM   8560  C  CG   . TYR   A  1  561 ? 43.317  12.692  -15.763  1.00 91.71  ? 561  TYR   A CG   1 
ATOM   8561  C  CD1  . TYR   A  1  561 ? 42.529  12.093  -16.738  1.00 93.43  ? 561  TYR   A CD1  1 
ATOM   8562  C  CD2  . TYR   A  1  561 ? 44.410  11.979  -15.280  1.00 91.80  ? 561  TYR   A CD2  1 
ATOM   8563  C  CE1  . TYR   A  1  561 ? 42.804  10.820  -17.201  1.00 92.99  ? 561  TYR   A CE1  1 
ATOM   8564  C  CE2  . TYR   A  1  561 ? 44.695  10.704  -15.743  1.00 91.11  ? 561  TYR   A CE2  1 
ATOM   8565  C  CZ   . TYR   A  1  561 ? 43.890  10.133  -16.707  1.00 91.82  ? 561  TYR   A CZ   1 
ATOM   8566  O  OH   . TYR   A  1  561 ? 44.162  8.864   -17.169  1.00 90.94  ? 561  TYR   A OH   1 
ATOM   8567  H  H    . TYR   A  1  561 ? 42.581  12.779  -12.859  1.00 114.90 ? 561  TYR   A H    1 
ATOM   8568  H  HA   . TYR   A  1  561 ? 41.841  15.149  -13.950  1.00 112.51 ? 561  TYR   A HA   1 
ATOM   8569  H  HB2  . TYR   A  1  561 ? 42.651  14.589  -16.023  1.00 108.45 ? 561  TYR   A HB2  1 
ATOM   8570  H  HB3  . TYR   A  1  561 ? 43.860  14.489  -14.996  1.00 108.45 ? 561  TYR   A HB3  1 
ATOM   8571  H  HD1  . TYR   A  1  561 ? 41.802  12.558  -17.086  1.00 112.16 ? 561  TYR   A HD1  1 
ATOM   8572  H  HD2  . TYR   A  1  561 ? 44.959  12.365  -14.635  1.00 110.20 ? 561  TYR   A HD2  1 
ATOM   8573  H  HE1  . TYR   A  1  561 ? 42.257  10.428  -17.844  1.00 111.62 ? 561  TYR   A HE1  1 
ATOM   8574  H  HE2  . TYR   A  1  561 ? 45.425  10.236  -15.406  1.00 109.37 ? 561  TYR   A HE2  1 
ATOM   8575  H  HH   . TYR   A  1  561 ? 44.882  8.586   -16.837  1.00 109.16 ? 561  TYR   A HH   1 
ATOM   8576  N  N    . ARG   A  1  562 ? 39.639  14.302  -14.457  1.00 109.24 ? 562  ARG   A N    1 
ATOM   8577  C  CA   . ARG   A  1  562 ? 38.308  13.841  -14.825  1.00 118.63 ? 562  ARG   A CA   1 
ATOM   8578  C  C    . ARG   A  1  562 ? 37.879  14.530  -16.116  1.00 117.35 ? 562  ARG   A C    1 
ATOM   8579  O  O    . ARG   A  1  562 ? 38.613  15.340  -16.690  1.00 118.22 ? 562  ARG   A O    1 
ATOM   8580  C  CB   . ARG   A  1  562 ? 37.304  14.105  -13.698  1.00 129.43 ? 562  ARG   A CB   1 
ATOM   8581  C  CG   . ARG   A  1  562 ? 37.792  13.632  -12.335  1.00 134.65 ? 562  ARG   A CG   1 
ATOM   8582  C  CD   . ARG   A  1  562 ? 36.646  13.251  -11.415  1.00 140.04 ? 562  ARG   A CD   1 
ATOM   8583  N  NE   . ARG   A  1  562 ? 36.895  11.983  -10.732  1.00 140.47 ? 562  ARG   A NE   1 
ATOM   8584  C  CZ   . ARG   A  1  562 ? 36.360  11.645  -9.563   1.00 147.62 ? 562  ARG   A CZ   1 
ATOM   8585  N  NH1  . ARG   A  1  562 ? 35.557  12.487  -8.928   1.00 156.57 ? 562  ARG   A NH1  1 
ATOM   8586  N  NH2  . ARG   A  1  562 ? 36.638  10.468  -9.019   1.00 144.73 ? 562  ARG   A NH2  1 
ATOM   8587  H  H    . ARG   A  1  562 ? 39.659  15.139  -14.260  1.00 131.12 ? 562  ARG   A H    1 
ATOM   8588  H  HA   . ARG   A  1  562 ? 38.337  12.883  -14.975  1.00 142.39 ? 562  ARG   A HA   1 
ATOM   8589  H  HB2  . ARG   A  1  562 ? 37.140  15.059  -13.642  1.00 155.36 ? 562  ARG   A HB2  1 
ATOM   8590  H  HB3  . ARG   A  1  562 ? 36.478  13.637  -13.898  1.00 155.36 ? 562  ARG   A HB3  1 
ATOM   8591  H  HG2  . ARG   A  1  562 ? 38.357  12.853  -12.452  1.00 161.62 ? 562  ARG   A HG2  1 
ATOM   8592  H  HG3  . ARG   A  1  562 ? 38.295  14.346  -11.912  1.00 161.62 ? 562  ARG   A HG3  1 
ATOM   8593  H  HD2  . ARG   A  1  562 ? 36.533  13.941  -10.743  1.00 168.08 ? 562  ARG   A HD2  1 
ATOM   8594  H  HD3  . ARG   A  1  562 ? 35.833  13.160  -11.937  1.00 168.08 ? 562  ARG   A HD3  1 
ATOM   8595  H  HE   . ARG   A  1  562 ? 37.423  11.420  -11.111  1.00 168.61 ? 562  ARG   A HE   1 
ATOM   8596  H  HH11 . ARG   A  1  562 ? 35.380  13.255  -9.272   1.00 187.92 ? 562  ARG   A HH11 1 
ATOM   8597  H  HH12 . ARG   A  1  562 ? 35.212  12.265  -8.172   1.00 187.92 ? 562  ARG   A HH12 1 
ATOM   8598  H  HH21 . ARG   A  1  562 ? 37.166  9.922   -9.423   1.00 173.71 ? 562  ARG   A HH21 1 
ATOM   8599  H  HH22 . ARG   A  1  562 ? 36.291  10.251  -8.263   1.00 173.71 ? 562  ARG   A HH22 1 
ATOM   8600  N  N    . LEU   A  1  563 ? 36.676  14.198  -16.581  1.00 116.47 ? 563  LEU   A N    1 
ATOM   8601  C  CA   . LEU   A  1  563 ? 36.153  14.765  -17.813  1.00 118.61 ? 563  LEU   A CA   1 
ATOM   8602  C  C    . LEU   A  1  563 ? 34.758  15.334  -17.601  1.00 125.02 ? 563  LEU   A C    1 
ATOM   8603  O  O    . LEU   A  1  563 ? 34.008  14.901  -16.719  1.00 127.56 ? 563  LEU   A O    1 
ATOM   8604  C  CB   . LEU   A  1  563 ? 36.090  13.732  -18.954  1.00 115.34 ? 563  LEU   A CB   1 
ATOM   8605  C  CG   . LEU   A  1  563 ? 36.965  13.940  -20.193  1.00 115.46 ? 563  LEU   A CG   1 
ATOM   8606  C  CD1  . LEU   A  1  563 ? 36.465  13.041  -21.310  1.00 115.08 ? 563  LEU   A CD1  1 
ATOM   8607  C  CD2  . LEU   A  1  563 ? 36.989  15.383  -20.660  1.00 119.18 ? 563  LEU   A CD2  1 
ATOM   8608  H  H    . LEU   A  1  563 ? 36.144  13.643  -16.195  1.00 139.81 ? 563  LEU   A H    1 
ATOM   8609  H  HA   . LEU   A  1  563 ? 36.744  15.488  -18.076  1.00 142.37 ? 563  LEU   A HA   1 
ATOM   8610  H  HB2  . LEU   A  1  563 ? 36.342  12.872  -18.581  1.00 138.44 ? 563  LEU   A HB2  1 
ATOM   8611  H  HB3  . LEU   A  1  563 ? 35.173  13.701  -19.267  1.00 138.44 ? 563  LEU   A HB3  1 
ATOM   8612  H  HG   . LEU   A  1  563 ? 37.879  13.712  -19.962  1.00 138.59 ? 563  LEU   A HG   1 
ATOM   8613  H  HD11 . LEU   A  1  563 ? 37.226  12.693  -21.800  1.00 138.14 ? 563  LEU   A HD11 1 
ATOM   8614  H  HD12 . LEU   A  1  563 ? 35.958  12.310  -20.924  1.00 138.14 ? 563  LEU   A HD12 1 
ATOM   8615  H  HD13 . LEU   A  1  563 ? 35.898  13.559  -21.903  1.00 138.14 ? 563  LEU   A HD13 1 
ATOM   8616  H  HD21 . LEU   A  1  563 ? 37.589  15.460  -21.418  1.00 143.06 ? 563  LEU   A HD21 1 
ATOM   8617  H  HD22 . LEU   A  1  563 ? 36.092  15.646  -20.920  1.00 143.06 ? 563  LEU   A HD22 1 
ATOM   8618  H  HD23 . LEU   A  1  563 ? 37.301  15.945  -19.933  1.00 143.06 ? 563  LEU   A HD23 1 
ATOM   8619  N  N    . ASP   A  1  564 ? 34.429  16.318  -18.434  1.00 129.49 ? 564  ASP   A N    1 
ATOM   8620  C  CA   . ASP   A  1  564 ? 33.069  16.833  -18.556  1.00 136.16 ? 564  ASP   A CA   1 
ATOM   8621  C  C    . ASP   A  1  564 ? 32.419  16.079  -19.708  1.00 137.75 ? 564  ASP   A C    1 
ATOM   8622  O  O    . ASP   A  1  564 ? 32.785  16.271  -20.874  1.00 134.85 ? 564  ASP   A O    1 
ATOM   8623  C  CB   . ASP   A  1  564 ? 33.059  18.342  -18.792  1.00 140.16 ? 564  ASP   A CB   1 
ATOM   8624  C  CG   . ASP   A  1  564 ? 31.715  18.978  -18.451  1.00 145.39 ? 564  ASP   A CG   1 
ATOM   8625  O  OD1  . ASP   A  1  564 ? 30.688  18.268  -18.499  1.00 146.13 ? 564  ASP   A OD1  1 
ATOM   8626  O  OD2  . ASP   A  1  564 ? 31.685  20.188  -18.133  1.00 148.37 ? 564  ASP   A OD2  1 
ATOM   8627  H  H    . ASP   A  1  564 ? 34.991  16.714  -18.951  1.00 155.43 ? 564  ASP   A H    1 
ATOM   8628  H  HA   . ASP   A  1  564 ? 32.574  16.675  -17.737  1.00 163.43 ? 564  ASP   A HA   1 
ATOM   8629  H  HB2  . ASP   A  1  564 ? 33.737  18.755  -18.234  1.00 168.22 ? 564  ASP   A HB2  1 
ATOM   8630  H  HB3  . ASP   A  1  564 ? 33.247  18.518  -19.727  1.00 168.22 ? 564  ASP   A HB3  1 
ATOM   8631  N  N    . TYR   A  1  565 ? 31.476  15.197  -19.383  1.00 142.11 ? 565  TYR   A N    1 
ATOM   8632  C  CA   . TYR   A  1  565 ? 30.945  14.301  -20.402  1.00 147.48 ? 565  TYR   A CA   1 
ATOM   8633  C  C    . TYR   A  1  565 ? 29.890  14.973  -21.270  1.00 160.52 ? 565  TYR   A C    1 
ATOM   8634  O  O    . TYR   A  1  565 ? 29.807  14.683  -22.467  1.00 165.24 ? 565  TYR   A O    1 
ATOM   8635  C  CB   . TYR   A  1  565 ? 30.364  13.048  -19.750  1.00 144.77 ? 565  TYR   A CB   1 
ATOM   8636  C  CG   . TYR   A  1  565 ? 31.412  12.117  -19.190  1.00 138.02 ? 565  TYR   A CG   1 
ATOM   8637  C  CD1  . TYR   A  1  565 ? 32.573  11.838  -19.900  1.00 131.27 ? 565  TYR   A CD1  1 
ATOM   8638  C  CD2  . TYR   A  1  565 ? 31.246  11.523  -17.949  1.00 139.38 ? 565  TYR   A CD2  1 
ATOM   8639  C  CE1  . TYR   A  1  565 ? 33.533  10.993  -19.394  1.00 126.40 ? 565  TYR   A CE1  1 
ATOM   8640  C  CE2  . TYR   A  1  565 ? 32.204  10.674  -17.432  1.00 134.09 ? 565  TYR   A CE2  1 
ATOM   8641  C  CZ   . TYR   A  1  565 ? 33.346  10.412  -18.160  1.00 125.94 ? 565  TYR   A CZ   1 
ATOM   8642  O  OH   . TYR   A  1  565 ? 34.306  9.568   -17.654  1.00 118.47 ? 565  TYR   A OH   1 
ATOM   8643  H  H    . TYR   A  1  565 ? 31.137  15.101  -18.599  1.00 170.57 ? 565  TYR   A H    1 
ATOM   8644  H  HA   . TYR   A  1  565 ? 31.678  14.035  -20.978  1.00 177.02 ? 565  TYR   A HA   1 
ATOM   8645  H  HB2  . TYR   A  1  565 ? 29.784  13.316  -19.020  1.00 173.76 ? 565  TYR   A HB2  1 
ATOM   8646  H  HB3  . TYR   A  1  565 ? 29.856  12.557  -20.415  1.00 173.76 ? 565  TYR   A HB3  1 
ATOM   8647  H  HD1  . TYR   A  1  565 ? 32.703  12.230  -20.733  1.00 157.56 ? 565  TYR   A HD1  1 
ATOM   8648  H  HD2  . TYR   A  1  565 ? 30.478  11.700  -17.457  1.00 167.29 ? 565  TYR   A HD2  1 
ATOM   8649  H  HE1  . TYR   A  1  565 ? 34.305  10.816  -19.882  1.00 151.72 ? 565  TYR   A HE1  1 
ATOM   8650  H  HE2  . TYR   A  1  565 ? 32.080  10.282  -16.598  1.00 160.95 ? 565  TYR   A HE2  1 
ATOM   8651  H  HH   . TYR   A  1  565 ? 34.049  9.248   -16.920  1.00 142.20 ? 565  TYR   A HH   1 
ATOM   8652  N  N    . ARG   A  1  566 ? 29.075  15.863  -20.696  1.00 166.38 ? 566  ARG   A N    1 
ATOM   8653  C  CA   . ARG   A  1  566 ? 27.989  16.457  -21.469  1.00 163.69 ? 566  ARG   A CA   1 
ATOM   8654  C  C    . ARG   A  1  566 ? 28.517  17.273  -22.643  1.00 161.07 ? 566  ARG   A C    1 
ATOM   8655  O  O    . ARG   A  1  566 ? 27.890  17.309  -23.709  1.00 162.93 ? 566  ARG   A O    1 
ATOM   8656  C  CB   . ARG   A  1  566 ? 27.121  17.328  -20.559  1.00 164.87 ? 566  ARG   A CB   1 
ATOM   8657  C  CG   . ARG   A  1  566 ? 26.368  16.547  -19.491  1.00 162.77 ? 566  ARG   A CG   1 
ATOM   8658  C  CD   . ARG   A  1  566 ? 25.350  17.417  -18.767  1.00 163.41 ? 566  ARG   A CD   1 
ATOM   8659  N  NE   . ARG   A  1  566 ? 24.219  17.771  -19.625  1.00 160.61 ? 566  ARG   A NE   1 
ATOM   8660  C  CZ   . ARG   A  1  566 ? 24.124  18.895  -20.332  1.00 155.09 ? 566  ARG   A CZ   1 
ATOM   8661  N  NH1  . ARG   A  1  566 ? 25.093  19.802  -20.297  1.00 150.54 ? 566  ARG   A NH1  1 
ATOM   8662  N  NH2  . ARG   A  1  566 ? 23.051  19.114  -21.080  1.00 156.24 ? 566  ARG   A NH2  1 
ATOM   8663  H  H    . ARG   A  1  566 ? 29.130  16.131  -19.881  1.00 199.70 ? 566  ARG   A H    1 
ATOM   8664  H  HA   . ARG   A  1  566 ? 27.433  15.748  -21.827  1.00 196.47 ? 566  ARG   A HA   1 
ATOM   8665  H  HB2  . ARG   A  1  566 ? 27.690  17.971  -20.109  1.00 197.88 ? 566  ARG   A HB2  1 
ATOM   8666  H  HB3  . ARG   A  1  566 ? 26.465  17.790  -21.104  1.00 197.88 ? 566  ARG   A HB3  1 
ATOM   8667  H  HG2  . ARG   A  1  566 ? 25.896  15.809  -19.907  1.00 195.36 ? 566  ARG   A HG2  1 
ATOM   8668  H  HG3  . ARG   A  1  566 ? 27.000  16.210  -18.836  1.00 195.36 ? 566  ARG   A HG3  1 
ATOM   8669  H  HD2  . ARG   A  1  566 ? 25.007  16.935  -17.999  1.00 196.13 ? 566  ARG   A HD2  1 
ATOM   8670  H  HD3  . ARG   A  1  566 ? 25.779  18.238  -18.479  1.00 196.13 ? 566  ARG   A HD3  1 
ATOM   8671  H  HE   . ARG   A  1  566 ? 23.568  17.213  -19.675  1.00 192.76 ? 566  ARG   A HE   1 
ATOM   8672  H  HH11 . ARG   A  1  566 ? 25.791  19.666  -19.814  1.00 180.68 ? 566  ARG   A HH11 1 
ATOM   8673  H  HH12 . ARG   A  1  566 ? 25.023  20.524  -20.758  1.00 180.68 ? 566  ARG   A HH12 1 
ATOM   8674  H  HH21 . ARG   A  1  566 ? 22.419  18.531  -21.107  1.00 187.52 ? 566  ARG   A HH21 1 
ATOM   8675  H  HH22 . ARG   A  1  566 ? 22.987  19.839  -21.538  1.00 187.52 ? 566  ARG   A HH22 1 
ATOM   8676  N  N    . THR   A  1  567 ? 29.669  17.923  -22.476  1.00 159.49 ? 567  THR   A N    1 
ATOM   8677  C  CA   . THR   A  1  567 ? 30.178  18.811  -23.515  1.00 161.27 ? 567  THR   A CA   1 
ATOM   8678  C  C    . THR   A  1  567 ? 30.678  18.058  -24.743  1.00 157.84 ? 567  THR   A C    1 
ATOM   8679  O  O    . THR   A  1  567 ? 30.785  18.657  -25.817  1.00 157.35 ? 567  THR   A O    1 
ATOM   8680  C  CB   . THR   A  1  567 ? 31.302  19.688  -22.953  1.00 161.85 ? 567  THR   A CB   1 
ATOM   8681  O  OG1  . THR   A  1  567 ? 31.649  20.698  -23.908  1.00 161.40 ? 567  THR   A OG1  1 
ATOM   8682  C  CG2  . THR   A  1  567 ? 32.536  18.854  -22.633  1.00 161.48 ? 567  THR   A CG2  1 
ATOM   8683  H  H    . THR   A  1  567 ? 30.168  17.867  -21.778  1.00 191.43 ? 567  THR   A H    1 
ATOM   8684  H  HA   . THR   A  1  567 ? 29.454  19.390  -23.800  1.00 193.56 ? 567  THR   A HA   1 
ATOM   8685  H  HB   . THR   A  1  567 ? 30.997  20.105  -22.132  1.00 194.26 ? 567  THR   A HB   1 
ATOM   8686  H  HG1  . THR   A  1  567 ? 31.317  21.435  -23.680  1.00 193.72 ? 567  THR   A HG1  1 
ATOM   8687  H  HG21 . THR   A  1  567 ? 32.989  19.218  -21.857  1.00 193.81 ? 567  THR   A HG21 1 
ATOM   8688  H  HG22 . THR   A  1  567 ? 32.278  17.938  -22.448  1.00 193.81 ? 567  THR   A HG22 1 
ATOM   8689  H  HG23 . THR   A  1  567 ? 33.146  18.863  -23.387  1.00 193.81 ? 567  THR   A HG23 1 
ATOM   8690  N  N    . ALA   A  1  568 ? 30.975  16.764  -24.618  1.00 156.10 ? 568  ALA   A N    1 
ATOM   8691  C  CA   . ALA   A  1  568 ? 31.515  15.972  -25.714  1.00 157.33 ? 568  ALA   A CA   1 
ATOM   8692  C  C    . ALA   A  1  568 ? 30.443  15.180  -26.459  1.00 152.73 ? 568  ALA   A C    1 
ATOM   8693  O  O    . ALA   A  1  568 ? 30.776  14.265  -27.219  1.00 147.07 ? 568  ALA   A O    1 
ATOM   8694  C  CB   . ALA   A  1  568 ? 32.592  15.022  -25.188  1.00 161.64 ? 568  ALA   A CB   1 
ATOM   8695  H  H    . ALA   A  1  568 ? 30.869  16.316  -23.891  1.00 187.35 ? 568  ALA   A H    1 
ATOM   8696  H  HA   . ALA   A  1  568 ? 31.924  16.579  -26.352  1.00 188.84 ? 568  ALA   A HA   1 
ATOM   8697  H  HB1  . ALA   A  1  568 ? 32.934  14.492  -25.925  1.00 194.01 ? 568  ALA   A HB1  1 
ATOM   8698  H  HB2  . ALA   A  1  568 ? 33.310  15.544  -24.795  1.00 194.01 ? 568  ALA   A HB2  1 
ATOM   8699  H  HB3  . ALA   A  1  568 ? 32.201  14.441  -24.517  1.00 194.01 ? 568  ALA   A HB3  1 
ATOM   8700  N  N    . ALA   A  1  569 ? 29.169  15.525  -26.271  1.00 156.87 ? 569  ALA   A N    1 
ATOM   8701  C  CA   . ALA   A  1  569 ? 28.070  14.730  -26.798  1.00 161.97 ? 569  ALA   A CA   1 
ATOM   8702  C  C    . ALA   A  1  569 ? 28.118  14.641  -28.326  1.00 165.50 ? 569  ALA   A C    1 
ATOM   8703  O  O    . ALA   A  1  569 ? 28.894  15.323  -29.000  1.00 171.50 ? 569  ALA   A O    1 
ATOM   8704  C  CB   . ALA   A  1  569 ? 26.732  15.324  -26.358  1.00 167.42 ? 569  ALA   A CB   1 
ATOM   8705  H  H    . ALA   A  1  569 ? 28.916  16.223  -25.838  1.00 188.28 ? 569  ALA   A H    1 
ATOM   8706  H  HA   . ALA   A  1  569 ? 28.147  13.828  -26.448  1.00 194.41 ? 569  ALA   A HA   1 
ATOM   8707  H  HB1  . ALA   A  1  569 ? 26.024  14.692  -26.558  1.00 200.95 ? 569  ALA   A HB1  1 
ATOM   8708  H  HB2  . ALA   A  1  569 ? 26.762  15.497  -25.404  1.00 200.95 ? 569  ALA   A HB2  1 
ATOM   8709  H  HB3  . ALA   A  1  569 ? 26.581  16.153  -26.840  1.00 200.95 ? 569  ALA   A HB3  1 
ATOM   8710  N  N    . ASP   A  1  570 ? 27.252  13.781  -28.864  1.00 163.72 ? 570  ASP   A N    1 
ATOM   8711  C  CA   . ASP   A  1  570 ? 27.136  13.531  -30.294  1.00 164.52 ? 570  ASP   A CA   1 
ATOM   8712  C  C    . ASP   A  1  570 ? 25.676  13.652  -30.716  1.00 165.30 ? 570  ASP   A C    1 
ATOM   8713  O  O    . ASP   A  1  570 ? 24.770  13.747  -29.883  1.00 159.41 ? 570  ASP   A O    1 
ATOM   8714  C  CB   . ASP   A  1  570 ? 27.679  12.141  -30.659  1.00 173.21 ? 570  ASP   A CB   1 
ATOM   8715  C  CG   . ASP   A  1  570 ? 29.182  12.132  -30.841  1.00 180.14 ? 570  ASP   A CG   1 
ATOM   8716  O  OD1  . ASP   A  1  570 ? 29.664  12.701  -31.843  1.00 182.89 ? 570  ASP   A OD1  1 
ATOM   8717  O  OD2  . ASP   A  1  570 ? 29.883  11.566  -29.976  1.00 181.16 ? 570  ASP   A OD2  1 
ATOM   8718  H  H    . ASP   A  1  570 ? 26.700  13.313  -28.399  1.00 196.50 ? 570  ASP   A H    1 
ATOM   8719  H  HA   . ASP   A  1  570 ? 27.646  14.200  -30.778  1.00 197.47 ? 570  ASP   A HA   1 
ATOM   8720  H  HB2  . ASP   A  1  570 ? 27.458  11.519  -29.949  1.00 207.89 ? 570  ASP   A HB2  1 
ATOM   8721  H  HB3  . ASP   A  1  570 ? 27.274  11.852  -31.492  1.00 207.89 ? 570  ASP   A HB3  1 
ATOM   8722  N  N    . THR   A  1  571 ? 25.456  13.650  -32.036  1.00 159.30 ? 571  THR   A N    1 
ATOM   8723  C  CA   . THR   A  1  571 ? 24.094  13.688  -32.564  1.00 160.05 ? 571  THR   A CA   1 
ATOM   8724  C  C    . THR   A  1  571 ? 23.225  12.616  -31.922  1.00 155.44 ? 571  THR   A C    1 
ATOM   8725  O  O    . THR   A  1  571 ? 22.038  12.838  -31.656  1.00 158.20 ? 571  THR   A O    1 
ATOM   8726  C  CB   . THR   A  1  571 ? 24.108  13.511  -34.086  1.00 159.98 ? 571  THR   A CB   1 
ATOM   8727  O  OG1  . THR   A  1  571 ? 22.765  13.350  -34.562  1.00 160.68 ? 571  THR   A OG1  1 
ATOM   8728  C  CG2  . THR   A  1  571 ? 24.938  12.292  -34.491  1.00 155.05 ? 571  THR   A CG2  1 
ATOM   8729  H  H    . THR   A  1  571 ? 26.070  13.627  -32.637  1.00 191.20 ? 571  THR   A H    1 
ATOM   8730  H  HA   . THR   A  1  571 ? 23.710  14.557  -32.366  1.00 192.09 ? 571  THR   A HA   1 
ATOM   8731  H  HB   . THR   A  1  571 ? 24.508  14.295  -34.493  1.00 192.02 ? 571  THR   A HB   1 
ATOM   8732  H  HG1  . THR   A  1  571 ? 22.768  13.225  -35.392  1.00 192.85 ? 571  THR   A HG1  1 
ATOM   8733  H  HG21 . THR   A  1  571 ? 24.902  12.171  -35.453  1.00 186.10 ? 571  THR   A HG21 1 
ATOM   8734  H  HG22 . THR   A  1  571 ? 25.862  12.416  -34.224  1.00 186.10 ? 571  THR   A HG22 1 
ATOM   8735  H  HG23 . THR   A  1  571 ? 24.590  11.495  -34.060  1.00 186.10 ? 571  THR   A HG23 1 
ATOM   8736  N  N    . THR   A  1  572 ? 23.804  11.441  -31.668  1.00 145.89 ? 572  THR   A N    1 
ATOM   8737  C  CA   . THR   A  1  572 ? 23.082  10.386  -30.971  1.00 142.30 ? 572  THR   A CA   1 
ATOM   8738  C  C    . THR   A  1  572 ? 22.581  10.848  -29.610  1.00 138.11 ? 572  THR   A C    1 
ATOM   8739  O  O    . THR   A  1  572 ? 21.560  10.350  -29.122  1.00 139.87 ? 572  THR   A O    1 
ATOM   8740  C  CB   . THR   A  1  572 ? 23.994  9.170   -30.801  1.00 138.88 ? 572  THR   A CB   1 
ATOM   8741  O  OG1  . THR   A  1  572 ? 25.279  9.601   -30.332  1.00 137.78 ? 572  THR   A OG1  1 
ATOM   8742  C  CG2  . THR   A  1  572 ? 24.159  8.428   -32.121  1.00 136.36 ? 572  THR   A CG2  1 
ATOM   8743  H  H    . THR   A  1  572 ? 24.609  11.234  -31.889  1.00 175.10 ? 572  THR   A H    1 
ATOM   8744  H  HA   . THR   A  1  572 ? 22.313  10.130  -31.504  1.00 170.80 ? 572  THR   A HA   1 
ATOM   8745  H  HB   . THR   A  1  572 ? 23.600  8.559   -30.159  1.00 166.69 ? 572  THR   A HB   1 
ATOM   8746  H  HG1  . THR   A  1  572 ? 25.795  8.942   -30.259  1.00 165.38 ? 572  THR   A HG1  1 
ATOM   8747  H  HG21 . THR   A  1  572 ? 24.728  7.652   -31.996  1.00 163.66 ? 572  THR   A HG21 1 
ATOM   8748  H  HG22 . THR   A  1  572 ? 23.294  8.134   -32.448  1.00 163.66 ? 572  THR   A HG22 1 
ATOM   8749  H  HG23 . THR   A  1  572 ? 24.563  9.012   -32.782  1.00 163.66 ? 572  THR   A HG23 1 
ATOM   8750  N  N    . GLY   A  1  573 ? 23.271  11.803  -28.995  1.00 132.41 ? 573  GLY   A N    1 
ATOM   8751  C  CA   . GLY   A  1  573 ? 23.103  12.087  -27.588  1.00 127.41 ? 573  GLY   A CA   1 
ATOM   8752  C  C    . GLY   A  1  573 ? 24.036  11.299  -26.702  1.00 119.28 ? 573  GLY   A C    1 
ATOM   8753  O  O    . GLY   A  1  573 ? 23.865  11.308  -25.477  1.00 117.38 ? 573  GLY   A O    1 
ATOM   8754  H  H    . GLY   A  1  573 ? 23.852  12.306  -29.383  1.00 158.93 ? 573  GLY   A H    1 
ATOM   8755  H  HA2  . GLY   A  1  573 ? 23.264  13.031  -27.434  1.00 152.93 ? 573  GLY   A HA2  1 
ATOM   8756  H  HA3  . GLY   A  1  573 ? 22.191  11.877  -27.330  1.00 152.93 ? 573  GLY   A HA3  1 
ATOM   8757  N  N    . LEU   A  1  574 ? 25.029  10.635  -27.288  1.00 111.54 ? 574  LEU   A N    1 
ATOM   8758  C  CA   . LEU   A  1  574 ? 25.854  9.650   -26.602  1.00 107.83 ? 574  LEU   A CA   1 
ATOM   8759  C  C    . LEU   A  1  574 ? 27.179  10.302  -26.231  1.00 105.99 ? 574  LEU   A C    1 
ATOM   8760  O  O    . LEU   A  1  574 ? 28.010  10.581  -27.102  1.00 104.55 ? 574  LEU   A O    1 
ATOM   8761  C  CB   . LEU   A  1  574 ? 26.064  8.434   -27.501  1.00 103.81 ? 574  LEU   A CB   1 
ATOM   8762  C  CG   . LEU   A  1  574 ? 26.264  7.056   -26.870  1.00 99.91  ? 574  LEU   A CG   1 
ATOM   8763  C  CD1  . LEU   A  1  574 ? 25.088  6.669   -25.988  1.00 101.47 ? 574  LEU   A CD1  1 
ATOM   8764  C  CD2  . LEU   A  1  574 ? 26.456  6.033   -27.978  1.00 97.51  ? 574  LEU   A CD2  1 
ATOM   8765  H  H    . LEU   A  1  574 ? 25.250  10.743  -28.112  1.00 133.88 ? 574  LEU   A H    1 
ATOM   8766  H  HA   . LEU   A  1  574 ? 25.421  9.363   -25.783  1.00 129.44 ? 574  LEU   A HA   1 
ATOM   8767  H  HB2  . LEU   A  1  574 ? 25.285  8.360   -28.073  1.00 124.61 ? 574  LEU   A HB2  1 
ATOM   8768  H  HB3  . LEU   A  1  574 ? 26.855  8.604   -28.037  1.00 124.61 ? 574  LEU   A HB3  1 
ATOM   8769  H  HG   . LEU   A  1  574 ? 27.049  7.074   -26.301  1.00 119.93 ? 574  LEU   A HG   1 
ATOM   8770  H  HD11 . LEU   A  1  574 ? 25.236  5.777   -25.637  1.00 121.81 ? 574  LEU   A HD11 1 
ATOM   8771  H  HD12 . LEU   A  1  574 ? 25.018  7.304   -25.258  1.00 121.81 ? 574  LEU   A HD12 1 
ATOM   8772  H  HD13 . LEU   A  1  574 ? 24.276  6.685   -26.518  1.00 121.81 ? 574  LEU   A HD13 1 
ATOM   8773  H  HD21 . LEU   A  1  574 ? 26.586  5.158   -27.580  1.00 117.05 ? 574  LEU   A HD21 1 
ATOM   8774  H  HD22 . LEU   A  1  574 ? 25.666  6.026   -28.541  1.00 117.05 ? 574  LEU   A HD22 1 
ATOM   8775  H  HD23 . LEU   A  1  574 ? 27.234  6.277   -28.502  1.00 117.05 ? 574  LEU   A HD23 1 
ATOM   8776  N  N    . GLN   A  1  575 ? 27.370  10.543  -24.946  1.00 104.60 ? 575  GLN   A N    1 
ATOM   8777  C  CA   . GLN   A  1  575 ? 28.594  11.159  -24.466  1.00 100.36 ? 575  GLN   A CA   1 
ATOM   8778  C  C    . GLN   A  1  575 ? 29.710  10.119  -24.403  1.00 95.35  ? 575  GLN   A C    1 
ATOM   8779  O  O    . GLN   A  1  575 ? 29.451  8.934   -24.182  1.00 95.29  ? 575  GLN   A O    1 
ATOM   8780  C  CB   . GLN   A  1  575 ? 28.376  11.761  -23.081  1.00 101.86 ? 575  GLN   A CB   1 
ATOM   8781  C  CG   . GLN   A  1  575 ? 27.092  12.571  -22.939  1.00 107.55 ? 575  GLN   A CG   1 
ATOM   8782  C  CD   . GLN   A  1  575 ? 26.696  12.780  -21.491  1.00 115.44 ? 575  GLN   A CD   1 
ATOM   8783  O  OE1  . GLN   A  1  575 ? 27.410  12.371  -20.575  1.00 118.54 ? 575  GLN   A OE1  1 
ATOM   8784  N  NE2  . GLN   A  1  575 ? 25.547  13.409  -21.277  1.00 122.06 ? 575  GLN   A NE2  1 
ATOM   8785  H  H    . GLN   A  1  575 ? 26.803  10.359  -24.326  1.00 125.55 ? 575  GLN   A H    1 
ATOM   8786  H  HA   . GLN   A  1  575 ? 28.864  11.871  -25.066  1.00 120.47 ? 575  GLN   A HA   1 
ATOM   8787  H  HB2  . GLN   A  1  575 ? 28.341  11.040  -22.433  1.00 122.26 ? 575  GLN   A HB2  1 
ATOM   8788  H  HB3  . GLN   A  1  575 ? 29.119  12.351  -22.881  1.00 122.26 ? 575  GLN   A HB3  1 
ATOM   8789  H  HG2  . GLN   A  1  575 ? 27.220  13.442  -23.345  1.00 129.10 ? 575  GLN   A HG2  1 
ATOM   8790  H  HG3  . GLN   A  1  575 ? 26.369  12.101  -23.384  1.00 129.10 ? 575  GLN   A HG3  1 
ATOM   8791  H  HE21 . GLN   A  1  575 ? 25.072  13.675  -21.942  1.00 146.51 ? 575  GLN   A HE21 1 
ATOM   8792  H  HE22 . GLN   A  1  575 ? 25.279  13.552  -20.472  1.00 146.51 ? 575  GLN   A HE22 1 
ATOM   8793  N  N    . PRO   A  1  576 ? 30.958  10.531  -24.596  1.00 91.45  ? 576  PRO   A N    1 
ATOM   8794  C  CA   . PRO   A  1  576 ? 32.075  9.598   -24.437  1.00 88.68  ? 576  PRO   A CA   1 
ATOM   8795  C  C    . PRO   A  1  576 ? 32.390  9.375   -22.965  1.00 87.78  ? 576  PRO   A C    1 
ATOM   8796  O  O    . PRO   A  1  576 ? 31.935  10.101  -22.081  1.00 89.52  ? 576  PRO   A O    1 
ATOM   8797  C  CB   . PRO   A  1  576 ? 33.226  10.303  -25.158  1.00 87.70  ? 576  PRO   A CB   1 
ATOM   8798  C  CG   . PRO   A  1  576 ? 32.931  11.746  -24.967  1.00 90.13  ? 576  PRO   A CG   1 
ATOM   8799  C  CD   . PRO   A  1  576 ? 31.423  11.871  -24.999  1.00 92.63  ? 576  PRO   A CD   1 
ATOM   8800  H  HA   . PRO   A  1  576 ? 31.895  8.748   -24.869  1.00 106.45 ? 576  PRO   A HA   1 
ATOM   8801  H  HB2  . PRO   A  1  576 ? 34.073  10.060  -24.753  1.00 105.27 ? 576  PRO   A HB2  1 
ATOM   8802  H  HB3  . PRO   A  1  576 ? 33.227  10.066  -26.098  1.00 105.27 ? 576  PRO   A HB3  1 
ATOM   8803  H  HG2  . PRO   A  1  576 ? 33.282  12.041  -24.112  1.00 108.19 ? 576  PRO   A HG2  1 
ATOM   8804  H  HG3  . PRO   A  1  576 ? 33.334  12.259  -25.685  1.00 108.19 ? 576  PRO   A HG3  1 
ATOM   8805  H  HD2  . PRO   A  1  576 ? 31.120  12.544  -24.370  1.00 111.19 ? 576  PRO   A HD2  1 
ATOM   8806  H  HD3  . PRO   A  1  576 ? 31.115  12.089  -25.892  1.00 111.19 ? 576  PRO   A HD3  1 
ATOM   8807  N  N    . ILE   A  1  577 ? 33.187  8.342   -22.717  1.00 85.28  ? 577  ILE   A N    1 
ATOM   8808  C  CA   . ILE   A  1  577 ? 33.589  7.963   -21.370  1.00 86.47  ? 577  ILE   A CA   1 
ATOM   8809  C  C    . ILE   A  1  577 ? 35.091  7.722   -21.371  1.00 87.50  ? 577  ILE   A C    1 
ATOM   8810  O  O    . ILE   A  1  577 ? 35.666  7.277   -22.369  1.00 89.26  ? 577  ILE   A O    1 
ATOM   8811  C  CB   . ILE   A  1  577 ? 32.823  6.711   -20.882  1.00 83.47  ? 577  ILE   A CB   1 
ATOM   8812  C  CG1  . ILE   A  1  577 ? 33.115  6.429   -19.407  1.00 78.38  ? 577  ILE   A CG1  1 
ATOM   8813  C  CG2  . ILE   A  1  577 ? 33.177  5.501   -21.741  1.00 84.44  ? 577  ILE   A CG2  1 
ATOM   8814  C  CD1  . ILE   A  1  577 ? 32.177  5.405   -18.789  1.00 78.34  ? 577  ILE   A CD1  1 
ATOM   8815  H  H    . ILE   A  1  577 ? 33.515  7.833   -23.328  1.00 102.37 ? 577  ILE   A H    1 
ATOM   8816  H  HA   . ILE   A  1  577 ? 33.401  8.686   -20.752  1.00 103.80 ? 577  ILE   A HA   1 
ATOM   8817  H  HB   . ILE   A  1  577 ? 31.873  6.887   -20.971  1.00 100.20 ? 577  ILE   A HB   1 
ATOM   8818  H  HG12 . ILE   A  1  577 ? 34.021  6.091   -19.326  1.00 94.10  ? 577  ILE   A HG12 1 
ATOM   8819  H  HG13 . ILE   A  1  577 ? 33.024  7.255   -18.906  1.00 94.10  ? 577  ILE   A HG13 1 
ATOM   8820  H  HG21 . ILE   A  1  577 ? 32.634  4.747   -21.463  1.00 101.36 ? 577  ILE   A HG21 1 
ATOM   8821  H  HG22 . ILE   A  1  577 ? 32.998  5.711   -22.671  1.00 101.36 ? 577  ILE   A HG22 1 
ATOM   8822  H  HG23 . ILE   A  1  577 ? 34.117  5.294   -21.623  1.00 101.36 ? 577  ILE   A HG23 1 
ATOM   8823  H  HD11 . ILE   A  1  577 ? 32.429  5.263   -17.863  1.00 94.04  ? 577  ILE   A HD11 1 
ATOM   8824  H  HD12 . ILE   A  1  577 ? 31.268  5.739   -18.838  1.00 94.04  ? 577  ILE   A HD12 1 
ATOM   8825  H  HD13 . ILE   A  1  577 ? 32.250  4.572   -19.283  1.00 94.04  ? 577  ILE   A HD13 1 
ATOM   8826  N  N    . LEU   A  1  578 ? 35.730  8.038   -20.249  1.00 87.97  ? 578  LEU   A N    1 
ATOM   8827  C  CA   . LEU   A  1  578 ? 37.150  7.758   -20.102  1.00 85.19  ? 578  LEU   A CA   1 
ATOM   8828  C  C    . LEU   A  1  578 ? 37.374  6.258   -19.951  1.00 85.41  ? 578  LEU   A C    1 
ATOM   8829  O  O    . LEU   A  1  578 ? 36.549  5.540   -19.380  1.00 85.43  ? 578  LEU   A O    1 
ATOM   8830  C  CB   . LEU   A  1  578 ? 37.720  8.493   -18.889  1.00 83.35  ? 578  LEU   A CB   1 
ATOM   8831  C  CG   . LEU   A  1  578 ? 37.893  10.005  -19.030  1.00 85.41  ? 578  LEU   A CG   1 
ATOM   8832  C  CD1  . LEU   A  1  578 ? 38.186  10.641  -17.680  1.00 88.96  ? 578  LEU   A CD1  1 
ATOM   8833  C  CD2  . LEU   A  1  578 ? 39.004  10.311  -20.019  1.00 83.72  ? 578  LEU   A CD2  1 
ATOM   8834  H  H    . LEU   A  1  578 ? 35.367  8.412   -19.566  1.00 105.60 ? 578  LEU   A H    1 
ATOM   8835  H  HA   . LEU   A  1  578 ? 37.627  8.066   -20.888  1.00 102.26 ? 578  LEU   A HA   1 
ATOM   8836  H  HB2  . LEU   A  1  578 ? 37.124  8.342   -18.139  1.00 100.05 ? 578  LEU   A HB2  1 
ATOM   8837  H  HB3  . LEU   A  1  578 ? 38.595  8.122   -18.697  1.00 100.05 ? 578  LEU   A HB3  1 
ATOM   8838  H  HG   . LEU   A  1  578 ? 37.068  10.391  -19.366  1.00 102.53 ? 578  LEU   A HG   1 
ATOM   8839  H  HD11 . LEU   A  1  578 ? 38.178  11.606  -17.777  1.00 106.78 ? 578  LEU   A HD11 1 
ATOM   8840  H  HD12 . LEU   A  1  578 ? 37.505  10.366  -17.047  1.00 106.78 ? 578  LEU   A HD12 1 
ATOM   8841  H  HD13 . LEU   A  1  578 ? 39.059  10.347  -17.375  1.00 106.78 ? 578  LEU   A HD13 1 
ATOM   8842  H  HD21 . LEU   A  1  578 ? 39.209  11.259  -19.980  1.00 100.50 ? 578  LEU   A HD21 1 
ATOM   8843  H  HD22 . LEU   A  1  578 ? 39.789  9.793   -19.782  1.00 100.50 ? 578  LEU   A HD22 1 
ATOM   8844  H  HD23 . LEU   A  1  578 ? 38.707  10.074  -20.911  1.00 100.50 ? 578  LEU   A HD23 1 
ATOM   8845  N  N    . ASN   A  1  579 ? 38.500  5.781   -20.474  1.00 85.29  ? 579  ASN   A N    1 
ATOM   8846  C  CA   . ASN   A  1  579 ? 38.837  4.373   -20.314  1.00 89.19  ? 579  ASN   A CA   1 
ATOM   8847  C  C    . ASN   A  1  579 ? 39.044  4.070   -18.836  1.00 92.68  ? 579  ASN   A C    1 
ATOM   8848  O  O    . ASN   A  1  579 ? 39.898  4.677   -18.182  1.00 87.62  ? 579  ASN   A O    1 
ATOM   8849  C  CB   . ASN   A  1  579 ? 40.089  4.016   -21.113  1.00 89.18  ? 579  ASN   A CB   1 
ATOM   8850  C  CG   . ASN   A  1  579 ? 40.401  2.527   -21.072  1.00 90.52  ? 579  ASN   A CG   1 
ATOM   8851  O  OD1  . ASN   A  1  579 ? 39.968  1.815   -20.165  1.00 91.50  ? 579  ASN   A OD1  1 
ATOM   8852  N  ND2  . ASN   A  1  579 ? 41.154  2.050   -22.056  1.00 90.53  ? 579  ASN   A ND2  1 
ATOM   8853  H  H    . ASN   A  1  579 ? 39.074  6.244   -20.917  1.00 102.38 ? 579  ASN   A H    1 
ATOM   8854  H  HA   . ASN   A  1  579 ? 38.111  3.829   -20.657  1.00 107.06 ? 579  ASN   A HA   1 
ATOM   8855  H  HB2  . ASN   A  1  579 ? 39.956  4.271   -22.040  1.00 107.06 ? 579  ASN   A HB2  1 
ATOM   8856  H  HB3  . ASN   A  1  579 ? 40.848  4.494   -20.744  1.00 107.06 ? 579  ASN   A HB3  1 
ATOM   8857  H  HD21 . ASN   A  1  579 ? 41.357  1.215   -22.076  1.00 108.67 ? 579  ASN   A HD21 1 
ATOM   8858  H  HD22 . ASN   A  1  579 ? 41.438  2.577   -22.674  1.00 108.67 ? 579  ASN   A HD22 1 
ATOM   8859  N  N    . GLN   A  1  580 ? 38.254  3.133   -18.311  1.00 98.36  ? 580  GLN   A N    1 
ATOM   8860  C  CA   . GLN   A  1  580 ? 38.362  2.790   -16.899  1.00 104.77 ? 580  GLN   A CA   1 
ATOM   8861  C  C    . GLN   A  1  580 ? 39.666  2.065   -16.598  1.00 107.81 ? 580  GLN   A C    1 
ATOM   8862  O  O    . GLN   A  1  580 ? 40.195  2.178   -15.487  1.00 110.88 ? 580  GLN   A O    1 
ATOM   8863  C  CB   . GLN   A  1  580 ? 37.170  1.929   -16.479  1.00 108.01 ? 580  GLN   A CB   1 
ATOM   8864  C  CG   . GLN   A  1  580 ? 35.808  2.550   -16.768  1.00 111.36 ? 580  GLN   A CG   1 
ATOM   8865  C  CD   . GLN   A  1  580 ? 35.432  3.640   -15.784  1.00 116.50 ? 580  GLN   A CD   1 
ATOM   8866  O  OE1  . GLN   A  1  580 ? 35.472  4.827   -16.109  1.00 116.49 ? 580  GLN   A OE1  1 
ATOM   8867  N  NE2  . GLN   A  1  580 ? 35.048  3.241   -14.577  1.00 121.43 ? 580  GLN   A NE2  1 
ATOM   8868  H  H    . GLN   A  1  580 ? 37.659  2.690   -18.745  1.00 118.07 ? 580  GLN   A H    1 
ATOM   8869  H  HA   . GLN   A  1  580 ? 38.343  3.607   -16.376  1.00 125.76 ? 580  GLN   A HA   1 
ATOM   8870  H  HB2  . GLN   A  1  580 ? 37.215  1.085   -16.956  1.00 129.65 ? 580  GLN   A HB2  1 
ATOM   8871  H  HB3  . GLN   A  1  580 ? 37.224  1.772   -15.523  1.00 129.65 ? 580  GLN   A HB3  1 
ATOM   8872  H  HG2  . GLN   A  1  580 ? 35.823  2.941   -17.656  1.00 133.66 ? 580  GLN   A HG2  1 
ATOM   8873  H  HG3  . GLN   A  1  580 ? 35.130  1.858   -16.721  1.00 133.66 ? 580  GLN   A HG3  1 
ATOM   8874  H  HE21 . GLN   A  1  580 ? 35.024  2.402   -14.389  1.00 145.76 ? 580  GLN   A HE21 1 
ATOM   8875  H  HE22 . GLN   A  1  580 ? 34.825  3.821   -13.983  1.00 145.76 ? 580  GLN   A HE22 1 
ATOM   8876  N  N    . PHE   A  1  581 ? 40.201  1.325   -17.573  1.00 111.03 ? 581  PHE   A N    1 
ATOM   8877  C  CA   . PHE   A  1  581 ? 41.409  0.541   -17.332  1.00 114.81 ? 581  PHE   A CA   1 
ATOM   8878  C  C    . PHE   A  1  581 ? 42.620  1.439   -17.100  1.00 124.09 ? 581  PHE   A C    1 
ATOM   8879  O  O    . PHE   A  1  581 ? 43.500  1.103   -16.300  1.00 134.65 ? 581  PHE   A O    1 
ATOM   8880  C  CB   . PHE   A  1  581 ? 41.645  -0.412  -18.505  1.00 109.41 ? 581  PHE   A CB   1 
ATOM   8881  C  CG   . PHE   A  1  581 ? 40.550  -1.433  -18.686  1.00 111.19 ? 581  PHE   A CG   1 
ATOM   8882  C  CD1  . PHE   A  1  581 ? 40.003  -2.085  -17.592  1.00 114.69 ? 581  PHE   A CD1  1 
ATOM   8883  C  CD2  . PHE   A  1  581 ? 40.061  -1.733  -19.948  1.00 111.66 ? 581  PHE   A CD2  1 
ATOM   8884  C  CE1  . PHE   A  1  581 ? 38.996  -3.019  -17.752  1.00 117.68 ? 581  PHE   A CE1  1 
ATOM   8885  C  CE2  . PHE   A  1  581 ? 39.052  -2.667  -20.113  1.00 115.42 ? 581  PHE   A CE2  1 
ATOM   8886  C  CZ   . PHE   A  1  581 ? 38.520  -3.309  -19.013  1.00 118.68 ? 581  PHE   A CZ   1 
ATOM   8887  H  H    . PHE   A  1  581 ? 39.888  1.262   -18.371  1.00 133.27 ? 581  PHE   A H    1 
ATOM   8888  H  HA   . PHE   A  1  581 ? 41.286  0.007   -16.532  1.00 137.80 ? 581  PHE   A HA   1 
ATOM   8889  H  HB2  . PHE   A  1  581 ? 41.705  0.107   -19.322  1.00 131.33 ? 581  PHE   A HB2  1 
ATOM   8890  H  HB3  . PHE   A  1  581 ? 42.475  -0.891  -18.355  1.00 131.33 ? 581  PHE   A HB3  1 
ATOM   8891  H  HD1  . PHE   A  1  581 ? 40.317  -1.891  -16.738  1.00 137.66 ? 581  PHE   A HD1  1 
ATOM   8892  H  HD2  . PHE   A  1  581 ? 40.414  -1.301  -20.692  1.00 134.03 ? 581  PHE   A HD2  1 
ATOM   8893  H  HE1  . PHE   A  1  581 ? 38.639  -3.451  -17.010  1.00 141.25 ? 581  PHE   A HE1  1 
ATOM   8894  H  HE2  . PHE   A  1  581 ? 38.733  -2.861  -20.965  1.00 138.54 ? 581  PHE   A HE2  1 
ATOM   8895  H  HZ   . PHE   A  1  581 ? 37.842  -3.936  -19.123  1.00 142.46 ? 581  PHE   A HZ   1 
ATOM   8896  N  N    . THR   A  1  582 ? 42.686  2.582   -17.784  1.00 126.23 ? 582  THR   A N    1 
ATOM   8897  C  CA   . THR   A  1  582 ? 43.736  3.562   -17.524  1.00 125.21 ? 582  THR   A CA   1 
ATOM   8898  C  C    . THR   A  1  582 ? 43.409  4.320   -16.242  1.00 121.13 ? 582  THR   A C    1 
ATOM   8899  O  O    . THR   A  1  582 ? 42.409  5.048   -16.201  1.00 121.30 ? 582  THR   A O    1 
ATOM   8900  C  CB   . THR   A  1  582 ? 43.876  4.547   -18.689  1.00 128.98 ? 582  THR   A CB   1 
ATOM   8901  O  OG1  . THR   A  1  582 ? 42.635  5.237   -18.887  1.00 133.28 ? 582  THR   A OG1  1 
ATOM   8902  C  CG2  . THR   A  1  582 ? 44.260  3.823   -19.971  1.00 127.23 ? 582  THR   A CG2  1 
ATOM   8903  H  H    . THR   A  1  582 ? 42.134  2.812   -18.402  1.00 151.51 ? 582  THR   A H    1 
ATOM   8904  H  HA   . THR   A  1  582 ? 44.583  3.100   -17.420  1.00 150.29 ? 582  THR   A HA   1 
ATOM   8905  H  HB   . THR   A  1  582 ? 44.575  5.186   -18.482  1.00 154.81 ? 582  THR   A HB   1 
ATOM   8906  H  HG1  . THR   A  1  582 ? 42.396  5.609   -18.172  1.00 159.97 ? 582  THR   A HG1  1 
ATOM   8907  H  HG21 . THR   A  1  582 ? 44.504  4.467   -20.654  1.00 152.71 ? 582  THR   A HG21 1 
ATOM   8908  H  HG22 . THR   A  1  582 ? 45.015  3.237   -19.807  1.00 152.71 ? 582  THR   A HG22 1 
ATOM   8909  H  HG23 . THR   A  1  582 ? 43.513  3.293   -20.289  1.00 152.71 ? 582  THR   A HG23 1 
ATOM   8910  N  N    . PRO   A  1  583 ? 44.204  4.186   -15.178  1.00 115.04 ? 583  PRO   A N    1 
ATOM   8911  C  CA   . PRO   A  1  583 ? 43.897  4.929   -13.950  1.00 110.55 ? 583  PRO   A CA   1 
ATOM   8912  C  C    . PRO   A  1  583 ? 43.891  6.430   -14.197  1.00 101.89 ? 583  PRO   A C    1 
ATOM   8913  O  O    . PRO   A  1  583 ? 44.779  6.974   -14.858  1.00 98.97  ? 583  PRO   A O    1 
ATOM   8914  C  CB   . PRO   A  1  583 ? 45.020  4.516   -12.991  1.00 114.52 ? 583  PRO   A CB   1 
ATOM   8915  C  CG   . PRO   A  1  583 ? 45.506  3.211   -13.512  1.00 116.97 ? 583  PRO   A CG   1 
ATOM   8916  C  CD   . PRO   A  1  583 ? 45.378  3.311   -15.003  1.00 116.26 ? 583  PRO   A CD   1 
ATOM   8917  H  HA   . PRO   A  1  583 ? 43.040  4.655   -13.586  1.00 132.70 ? 583  PRO   A HA   1 
ATOM   8918  H  HB2  . PRO   A  1  583 ? 45.727  5.180   -13.004  1.00 137.46 ? 583  PRO   A HB2  1 
ATOM   8919  H  HB3  . PRO   A  1  583 ? 44.670  4.422   -12.091  1.00 137.46 ? 583  PRO   A HB3  1 
ATOM   8920  H  HG2  . PRO   A  1  583 ? 46.431  3.075   -13.253  1.00 140.40 ? 583  PRO   A HG2  1 
ATOM   8921  H  HG3  . PRO   A  1  583 ? 44.955  2.491   -13.166  1.00 140.40 ? 583  PRO   A HG3  1 
ATOM   8922  H  HD2  . PRO   A  1  583 ? 46.170  3.713   -15.392  1.00 139.55 ? 583  PRO   A HD2  1 
ATOM   8923  H  HD3  . PRO   A  1  583 ? 45.221  2.439   -15.397  1.00 139.55 ? 583  PRO   A HD3  1 
ATOM   8924  N  N    . ALA   A  1  584 ? 42.871  7.099   -13.658  1.00 96.63  ? 584  ALA   A N    1 
ATOM   8925  C  CA   . ALA   A  1  584 ? 42.706  8.535   -13.827  1.00 93.45  ? 584  ALA   A CA   1 
ATOM   8926  C  C    . ALA   A  1  584 ? 43.394  9.334   -12.729  1.00 90.03  ? 584  ALA   A C    1 
ATOM   8927  O  O    . ALA   A  1  584 ? 43.086  10.518  -12.545  1.00 88.83  ? 584  ALA   A O    1 
ATOM   8928  C  CB   . ALA   A  1  584 ? 41.219  8.892   -13.889  1.00 95.23  ? 584  ALA   A CB   1 
ATOM   8929  H  H    . ALA   A  1  584 ? 42.255  6.733   -13.183  1.00 116.00 ? 584  ALA   A H    1 
ATOM   8930  H  HA   . ALA   A  1  584 ? 43.105  8.791   -14.673  1.00 112.18 ? 584  ALA   A HA   1 
ATOM   8931  H  HB1  . ALA   A  1  584 ? 41.130  9.846   -14.039  1.00 114.31 ? 584  ALA   A HB1  1 
ATOM   8932  H  HB2  . ALA   A  1  584 ? 40.807  8.402   -14.618  1.00 114.31 ? 584  ALA   A HB2  1 
ATOM   8933  H  HB3  . ALA   A  1  584 ? 40.801  8.649   -13.048  1.00 114.31 ? 584  ALA   A HB3  1 
ATOM   8934  N  N    . ASN   A  1  585 ? 44.310  8.711   -11.995  1.00 87.47  ? 585  ASN   A N    1 
ATOM   8935  C  CA   . ASN   A  1  585 ? 45.168  9.400   -11.048  1.00 87.28  ? 585  ASN   A CA   1 
ATOM   8936  C  C    . ASN   A  1  585 ? 46.604  8.949   -11.270  1.00 87.39  ? 585  ASN   A C    1 
ATOM   8937  O  O    . ASN   A  1  585 ? 46.860  7.795   -11.626  1.00 88.78  ? 585  ASN   A O    1 
ATOM   8938  C  CB   . ASN   A  1  585 ? 44.745  9.136   -9.593   1.00 87.65  ? 585  ASN   A CB   1 
ATOM   8939  C  CG   . ASN   A  1  585 ? 44.528  7.663   -9.297   1.00 86.56  ? 585  ASN   A CG   1 
ATOM   8940  O  OD1  . ASN   A  1  585 ? 45.434  6.846   -9.457   1.00 85.36  ? 585  ASN   A OD1  1 
ATOM   8941  N  ND2  . ASN   A  1  585 ? 43.331  7.323   -8.826   1.00 85.92  ? 585  ASN   A ND2  1 
ATOM   8942  H  H    . ASN   A  1  585 ? 44.454  7.864   -12.032  1.00 105.00 ? 585  ASN   A H    1 
ATOM   8943  H  HA   . ASN   A  1  585 ? 45.120  10.358  -11.193  1.00 104.78 ? 585  ASN   A HA   1 
ATOM   8944  H  HB2  . ASN   A  1  585 ? 45.439  9.461   -8.999   1.00 105.22 ? 585  ASN   A HB2  1 
ATOM   8945  H  HB3  . ASN   A  1  585 ? 43.913  9.602   -9.418   1.00 105.22 ? 585  ASN   A HB3  1 
ATOM   8946  H  HD21 . ASN   A  1  585 ? 43.159  6.501   -8.642   1.00 103.14 ? 585  ASN   A HD21 1 
ATOM   8947  H  HD22 . ASN   A  1  585 ? 42.730  7.926   -8.704   1.00 103.14 ? 585  ASN   A HD22 1 
ATOM   8948  N  N    . ILE   A  1  586 ? 47.540  9.877   -11.081  1.00 88.06  ? 586  ILE   A N    1 
ATOM   8949  C  CA   . ILE   A  1  586 ? 48.966  9.581   -11.159  1.00 87.87  ? 586  ILE   A CA   1 
ATOM   8950  C  C    . ILE   A  1  586 ? 49.670  10.349  -10.053  1.00 86.45  ? 586  ILE   A C    1 
ATOM   8951  O  O    . ILE   A  1  586 ? 49.281  11.469  -9.704   1.00 87.34  ? 586  ILE   A O    1 
ATOM   8952  C  CB   . ILE   A  1  586 ? 49.575  9.936   -12.535  1.00 89.65  ? 586  ILE   A CB   1 
ATOM   8953  C  CG1  . ILE   A  1  586 ? 49.253  11.386  -12.910  1.00 92.09  ? 586  ILE   A CG1  1 
ATOM   8954  C  CG2  . ILE   A  1  586 ? 49.083  8.959   -13.596  1.00 91.59  ? 586  ILE   A CG2  1 
ATOM   8955  C  CD1  . ILE   A  1  586 ? 49.794  11.810  -14.266  1.00 92.74  ? 586  ILE   A CD1  1 
ATOM   8956  H  H    . ILE   A  1  586 ? 47.369  10.701  -10.902  1.00 105.71 ? 586  ILE   A H    1 
ATOM   8957  H  HA   . ILE   A  1  586 ? 49.097  8.630   -11.019  1.00 105.48 ? 586  ILE   A HA   1 
ATOM   8958  H  HB   . ILE   A  1  586 ? 50.540  9.857   -12.480  1.00 107.61 ? 586  ILE   A HB   1 
ATOM   8959  H  HG12 . ILE   A  1  586 ? 48.290  11.496  -12.929  1.00 110.54 ? 586  ILE   A HG12 1 
ATOM   8960  H  HG13 . ILE   A  1  586 ? 49.641  11.973  -12.241  1.00 110.54 ? 586  ILE   A HG13 1 
ATOM   8961  H  HG21 . ILE   A  1  586 ? 49.615  9.072   -14.400  1.00 109.94 ? 586  ILE   A HG21 1 
ATOM   8962  H  HG22 . ILE   A  1  586 ? 49.179  8.054   -13.261  1.00 109.94 ? 586  ILE   A HG22 1 
ATOM   8963  H  HG23 . ILE   A  1  586 ? 48.150  9.144   -13.788  1.00 109.94 ? 586  ILE   A HG23 1 
ATOM   8964  H  HD11 . ILE   A  1  586 ? 49.410  12.668  -14.505  1.00 111.33 ? 586  ILE   A HD11 1 
ATOM   8965  H  HD12 . ILE   A  1  586 ? 50.760  11.884  -14.212  1.00 111.33 ? 586  ILE   A HD12 1 
ATOM   8966  H  HD13 . ILE   A  1  586 ? 49.550  11.143  -14.926  1.00 111.33 ? 586  ILE   A HD13 1 
ATOM   8967  N  N    . SER   A  1  587 ? 50.714  9.741   -9.497   1.00 87.34  ? 587  SER   A N    1 
ATOM   8968  C  CA   . SER   A  1  587 ? 51.416  10.336  -8.373   1.00 87.37  ? 587  SER   A CA   1 
ATOM   8969  C  C    . SER   A  1  587 ? 52.920  10.216  -8.556   1.00 86.97  ? 587  SER   A C    1 
ATOM   8970  O  O    . SER   A  1  587 ? 53.425  9.205   -9.051   1.00 85.26  ? 587  SER   A O    1 
ATOM   8971  C  CB   . SER   A  1  587 ? 51.002  9.683   -7.048   1.00 89.44  ? 587  SER   A CB   1 
ATOM   8972  O  OG   . SER   A  1  587 ? 51.534  8.375   -6.932   1.00 92.15  ? 587  SER   A OG   1 
ATOM   8973  H  H    . SER   A  1  587 ? 51.031  8.985   -9.755   1.00 104.84 ? 587  SER   A H    1 
ATOM   8974  H  HA   . SER   A  1  587 ? 51.202  11.282  -8.338   1.00 104.89 ? 587  SER   A HA   1 
ATOM   8975  H  HB2  . SER   A  1  587 ? 51.334  10.223  -6.314   1.00 107.36 ? 587  SER   A HB2  1 
ATOM   8976  H  HB3  . SER   A  1  587 ? 50.034  9.632   -7.012   1.00 107.36 ? 587  SER   A HB3  1 
ATOM   8977  H  HG   . SER   A  1  587 ? 51.087  7.931   -6.376   1.00 110.62 ? 587  SER   A HG   1 
ATOM   8978  N  N    . ARG   A  1  588 ? 53.617  11.272  -8.151   1.00 89.05  ? 588  ARG   A N    1 
ATOM   8979  C  CA   . ARG   A  1  588 ? 55.067  11.328  -8.089   1.00 89.80  ? 588  ARG   A CA   1 
ATOM   8980  C  C    . ARG   A  1  588 ? 55.440  11.801  -6.694   1.00 91.86  ? 588  ARG   A C    1 
ATOM   8981  O  O    . ARG   A  1  588 ? 54.658  12.494  -6.038   1.00 94.93  ? 588  ARG   A O    1 
ATOM   8982  C  CB   . ARG   A  1  588 ? 55.636  12.282  -9.141   1.00 90.05  ? 588  ARG   A CB   1 
ATOM   8983  C  CG   . ARG   A  1  588 ? 55.475  11.800  -10.568  1.00 92.81  ? 588  ARG   A CG   1 
ATOM   8984  C  CD   . ARG   A  1  588 ? 56.569  10.817  -10.942  1.00 97.25  ? 588  ARG   A CD   1 
ATOM   8985  N  NE   . ARG   A  1  588 ? 56.549  10.493  -12.365  1.00 100.09 ? 588  ARG   A NE   1 
ATOM   8986  C  CZ   . ARG   A  1  588 ? 55.675  9.668   -12.932  1.00 98.88  ? 588  ARG   A CZ   1 
ATOM   8987  N  NH1  . ARG   A  1  588 ? 54.735  9.083   -12.200  1.00 95.50  ? 588  ARG   A NH1  1 
ATOM   8988  N  NH2  . ARG   A  1  588 ? 55.735  9.432   -14.235  1.00 99.08  ? 588  ARG   A NH2  1 
ATOM   8989  H  H    . ARG   A  1  588 ? 53.250  12.006  -7.894   1.00 106.89 ? 588  ARG   A H    1 
ATOM   8990  H  HA   . ARG   A  1  588 ? 55.460  10.456  -8.252   1.00 107.80 ? 588  ARG   A HA   1 
ATOM   8991  H  HB2  . ARG   A  1  588 ? 55.180  13.134  -9.066   1.00 108.10 ? 588  ARG   A HB2  1 
ATOM   8992  H  HB3  . ARG   A  1  588 ? 56.585  12.397  -8.975   1.00 108.10 ? 588  ARG   A HB3  1 
ATOM   8993  H  HG2  . ARG   A  1  588 ? 54.618  11.355  -10.663  1.00 111.41 ? 588  ARG   A HG2  1 
ATOM   8994  H  HG3  . ARG   A  1  588 ? 55.525  12.557  -11.172  1.00 111.41 ? 588  ARG   A HG3  1 
ATOM   8995  H  HD2  . ARG   A  1  588 ? 57.433  11.205  -10.731  1.00 116.74 ? 588  ARG   A HD2  1 
ATOM   8996  H  HD3  . ARG   A  1  588 ? 56.444  9.995   -10.442  1.00 116.74 ? 588  ARG   A HD3  1 
ATOM   8997  H  HE   . ARG   A  1  588 ? 57.141  10.859  -12.869  1.00 120.15 ? 588  ARG   A HE   1 
ATOM   8998  H  HH11 . ARG   A  1  588 ? 54.691  9.237   -11.355  1.00 114.64 ? 588  ARG   A HH11 1 
ATOM   8999  H  HH12 . ARG   A  1  588 ? 54.171  8.550   -12.571  1.00 114.64 ? 588  ARG   A HH12 1 
ATOM   9000  H  HH21 . ARG   A  1  588 ? 56.340  9.813   -14.714  1.00 118.93 ? 588  ARG   A HH21 1 
ATOM   9001  H  HH22 . ARG   A  1  588 ? 55.170  8.899   -14.603  1.00 118.93 ? 588  ARG   A HH22 1 
ATOM   9002  N  N    . GLN   A  1  589 ? 56.630  11.427  -6.233   1.00 88.82  ? 589  GLN   A N    1 
ATOM   9003  C  CA   . GLN   A  1  589 ? 57.026  11.754  -4.872   1.00 89.43  ? 589  GLN   A CA   1 
ATOM   9004  C  C    . GLN   A  1  589 ? 58.381  12.443  -4.847   1.00 89.00  ? 589  GLN   A C    1 
ATOM   9005  O  O    . GLN   A  1  589 ? 59.269  12.149  -5.656   1.00 89.28  ? 589  GLN   A O    1 
ATOM   9006  C  CB   . GLN   A  1  589 ? 57.034  10.504  -3.973   1.00 89.22  ? 589  GLN   A CB   1 
ATOM   9007  C  CG   . GLN   A  1  589 ? 58.220  9.570   -4.114   1.00 91.81  ? 589  GLN   A CG   1 
ATOM   9008  C  CD   . GLN   A  1  589 ? 58.015  8.295   -3.312   1.00 93.19  ? 589  GLN   A CD   1 
ATOM   9009  O  OE1  . GLN   A  1  589 ? 57.014  8.152   -2.609   1.00 91.24  ? 589  GLN   A OE1  1 
ATOM   9010  N  NE2  . GLN   A  1  589 ? 58.957  7.366   -3.414   1.00 94.32  ? 589  GLN   A NE2  1 
ATOM   9011  H  H    . GLN   A  1  589 ? 57.216  10.988  -6.685   1.00 106.62 ? 589  GLN   A H    1 
ATOM   9012  H  HA   . GLN   A  1  589 ? 56.387  12.386  -4.506   1.00 107.36 ? 589  GLN   A HA   1 
ATOM   9013  H  HB2  . GLN   A  1  589 ? 57.014  10.799  -3.049   1.00 107.10 ? 589  GLN   A HB2  1 
ATOM   9014  H  HB3  . GLN   A  1  589 ? 56.239  9.985   -4.173   1.00 107.10 ? 589  GLN   A HB3  1 
ATOM   9015  H  HG2  . GLN   A  1  589 ? 58.331  9.330   -5.047   1.00 110.20 ? 589  GLN   A HG2  1 
ATOM   9016  H  HG3  . GLN   A  1  589 ? 59.019  10.012  -3.787   1.00 110.20 ? 589  GLN   A HG3  1 
ATOM   9017  H  HE21 . GLN   A  1  589 ? 59.641  7.501   -3.917   1.00 113.22 ? 589  GLN   A HE21 1 
ATOM   9018  H  HE22 . GLN   A  1  589 ? 58.882  6.629   -2.978   1.00 113.22 ? 589  GLN   A HE22 1 
ATOM   9019  N  N    . ALA   A  1  590 ? 58.508  13.381  -3.915   1.00 89.42  ? 590  ALA   A N    1 
ATOM   9020  C  CA   . ALA   A  1  590 ? 59.722  14.141  -3.674   1.00 88.88  ? 590  ALA   A CA   1 
ATOM   9021  C  C    . ALA   A  1  590 ? 60.155  13.918  -2.233   1.00 89.07  ? 590  ALA   A C    1 
ATOM   9022  O  O    . ALA   A  1  590 ? 59.322  13.702  -1.347   1.00 87.39  ? 590  ALA   A O    1 
ATOM   9023  C  CB   . ALA   A  1  590 ? 59.498  15.635  -3.937   1.00 89.62  ? 590  ALA   A CB   1 
ATOM   9024  H  H    . ALA   A  1  590 ? 57.870  13.604  -3.383   1.00 107.34 ? 590  ALA   A H    1 
ATOM   9025  H  HA   . ALA   A  1  590 ? 60.433  13.844  -4.263   1.00 106.69 ? 590  ALA   A HA   1 
ATOM   9026  H  HB1  . ALA   A  1  590 ? 60.318  16.116  -3.745   1.00 107.58 ? 590  ALA   A HB1  1 
ATOM   9027  H  HB2  . ALA   A  1  590 ? 59.252  15.759  -4.868   1.00 107.58 ? 590  ALA   A HB2  1 
ATOM   9028  H  HB3  . ALA   A  1  590 ? 58.785  15.954  -3.362   1.00 107.58 ? 590  ALA   A HB3  1 
ATOM   9029  N  N    . HIS   A  1  591 ? 61.463  13.968  -1.998   1.00 92.09  ? 591  HIS   A N    1 
ATOM   9030  C  CA   . HIS   A  1  591 ? 62.024  13.663  -0.692   1.00 93.72  ? 591  HIS   A CA   1 
ATOM   9031  C  C    . HIS   A  1  591 ? 62.767  14.867  -0.129   1.00 94.80  ? 591  HIS   A C    1 
ATOM   9032  O  O    . HIS   A  1  591 ? 63.168  15.779  -0.857   1.00 95.88  ? 591  HIS   A O    1 
ATOM   9033  C  CB   . HIS   A  1  591 ? 62.973  12.461  -0.762   1.00 96.18  ? 591  HIS   A CB   1 
ATOM   9034  C  CG   . HIS   A  1  591 ? 62.280  11.159  -1.011   1.00 99.97  ? 591  HIS   A CG   1 
ATOM   9035  N  ND1  . HIS   A  1  591 ? 61.777  10.806  -2.245   1.00 100.24 ? 591  HIS   A ND1  1 
ATOM   9036  C  CD2  . HIS   A  1  591 ? 62.005  10.124  -0.183   1.00 102.23 ? 591  HIS   A CD2  1 
ATOM   9037  C  CE1  . HIS   A  1  591 ? 61.223  9.609   -2.166   1.00 100.49 ? 591  HIS   A CE1  1 
ATOM   9038  N  NE2  . HIS   A  1  591 ? 61.349  9.172   -0.926   1.00 101.44 ? 591  HIS   A NE2  1 
ATOM   9039  H  H    . HIS   A  1  591 ? 62.051  14.179  -2.590   1.00 110.54 ? 591  HIS   A H    1 
ATOM   9040  H  HA   . HIS   A  1  591 ? 61.298  13.452  -0.085   1.00 112.50 ? 591  HIS   A HA   1 
ATOM   9041  H  HB2  . HIS   A  1  591 ? 63.604  12.603  -1.485   1.00 115.45 ? 591  HIS   A HB2  1 
ATOM   9042  H  HB3  . HIS   A  1  591 ? 63.446  12.388  0.081    1.00 115.45 ? 591  HIS   A HB3  1 
ATOM   9043  H  HD2  . HIS   A  1  591 ? 62.220  10.067  0.720    1.00 122.71 ? 591  HIS   A HD2  1 
ATOM   9044  H  HE1  . HIS   A  1  591 ? 60.814  9.152   -2.865   1.00 120.63 ? 591  HIS   A HE1  1 
ATOM   9045  H  HE2  . HIS   A  1  591 ? 61.067  8.415   -0.632   1.00 121.76 ? 591  HIS   A HE2  1 
ATOM   9046  N  N    . ILE   A  1  592 ? 62.945  14.848  1.190    1.00 93.02  ? 592  ILE   A N    1 
ATOM   9047  C  CA   . ILE   A  1  592 ? 63.633  15.907  1.917    1.00 92.83  ? 592  ILE   A CA   1 
ATOM   9048  C  C    . ILE   A  1  592 ? 65.070  15.471  2.167    1.00 92.97  ? 592  ILE   A C    1 
ATOM   9049  O  O    . ILE   A  1  592 ? 65.321  14.337  2.593    1.00 92.78  ? 592  ILE   A O    1 
ATOM   9050  C  CB   . ILE   A  1  592 ? 62.913  16.234  3.238    1.00 93.96  ? 592  ILE   A CB   1 
ATOM   9051  C  CG1  . ILE   A  1  592 ? 61.577  16.930  2.945    1.00 93.90  ? 592  ILE   A CG1  1 
ATOM   9052  C  CG2  . ILE   A  1  592 ? 63.805  17.096  4.133    1.00 95.82  ? 592  ILE   A CG2  1 
ATOM   9053  C  CD1  . ILE   A  1  592 ? 60.714  17.210  4.172    1.00 94.91  ? 592  ILE   A CD1  1 
ATOM   9054  H  H    . ILE   A  1  592 ? 62.667  14.213  1.698    1.00 111.66 ? 592  ILE   A H    1 
ATOM   9055  H  HA   . ILE   A  1  592 ? 63.651  16.710  1.373    1.00 111.44 ? 592  ILE   A HA   1 
ATOM   9056  H  HB   . ILE   A  1  592 ? 62.728  15.407  3.711    1.00 112.79 ? 592  ILE   A HB   1 
ATOM   9057  H  HG12 . ILE   A  1  592 ? 61.761  17.781  2.519    1.00 112.72 ? 592  ILE   A HG12 1 
ATOM   9058  H  HG13 . ILE   A  1  592 ? 61.061  16.365  2.349    1.00 112.72 ? 592  ILE   A HG13 1 
ATOM   9059  H  HG21 . ILE   A  1  592 ? 63.304  17.357  4.921    1.00 115.02 ? 592  ILE   A HG21 1 
ATOM   9060  H  HG22 . ILE   A  1  592 ? 64.585  16.581  4.391    1.00 115.02 ? 592  ILE   A HG22 1 
ATOM   9061  H  HG23 . ILE   A  1  592 ? 64.079  17.885  3.639    1.00 115.02 ? 592  ILE   A HG23 1 
ATOM   9062  H  HD11 . ILE   A  1  592 ? 60.067  17.899  3.953    1.00 113.93 ? 592  ILE   A HD11 1 
ATOM   9063  H  HD12 . ILE   A  1  592 ? 60.254  16.395  4.428    1.00 113.93 ? 592  ILE   A HD12 1 
ATOM   9064  H  HD13 . ILE   A  1  592 ? 61.284  17.510  4.898    1.00 113.93 ? 592  ILE   A HD13 1 
ATOM   9065  N  N    . LEU   A  1  593 ? 66.011  16.374  1.901    1.00 94.77  ? 593  LEU   A N    1 
ATOM   9066  C  CA   . LEU   A  1  593 ? 67.419  16.104  2.159    1.00 95.81  ? 593  LEU   A CA   1 
ATOM   9067  C  C    . LEU   A  1  593 ? 67.678  16.027  3.659    1.00 96.76  ? 593  LEU   A C    1 
ATOM   9068  O  O    . LEU   A  1  593 ? 67.070  16.756  4.449    1.00 94.62  ? 593  LEU   A O    1 
ATOM   9069  C  CB   . LEU   A  1  593 ? 68.282  17.197  1.524    1.00 96.32  ? 593  LEU   A CB   1 
ATOM   9070  C  CG   . LEU   A  1  593 ? 69.797  17.162  1.743    1.00 98.61  ? 593  LEU   A CG   1 
ATOM   9071  C  CD1  . LEU   A  1  593 ? 70.425  15.947  1.094    1.00 100.21 ? 593  LEU   A CD1  1 
ATOM   9072  C  CD2  . LEU   A  1  593 ? 70.437  18.426  1.197    1.00 100.67 ? 593  LEU   A CD2  1 
ATOM   9073  H  H    . LEU   A  1  593 ? 65.859  17.153  1.571    1.00 113.77 ? 593  LEU   A H    1 
ATOM   9074  H  HA   . LEU   A  1  593 ? 67.671  15.253  1.767    1.00 115.01 ? 593  LEU   A HA   1 
ATOM   9075  H  HB2  . LEU   A  1  593 ? 68.142  17.158  0.565    1.00 115.63 ? 593  LEU   A HB2  1 
ATOM   9076  H  HB3  . LEU   A  1  593 ? 67.974  18.049  1.870    1.00 115.63 ? 593  LEU   A HB3  1 
ATOM   9077  H  HG   . LEU   A  1  593 ? 69.964  17.109  2.697    1.00 118.37 ? 593  LEU   A HG   1 
ATOM   9078  H  HD11 . LEU   A  1  593 ? 71.209  15.687  1.602    1.00 120.29 ? 593  LEU   A HD11 1 
ATOM   9079  H  HD12 . LEU   A  1  593 ? 69.779  15.223  1.090    1.00 120.29 ? 593  LEU   A HD12 1 
ATOM   9080  H  HD13 . LEU   A  1  593 ? 70.678  16.170  0.185    1.00 120.29 ? 593  LEU   A HD13 1 
ATOM   9081  H  HD21 . LEU   A  1  593 ? 71.402  18.335  1.238    1.00 120.85 ? 593  LEU   A HD21 1 
ATOM   9082  H  HD22 . LEU   A  1  593 ? 70.156  18.550  0.277    1.00 120.85 ? 593  LEU   A HD22 1 
ATOM   9083  H  HD23 . LEU   A  1  593 ? 70.153  19.182  1.734    1.00 120.85 ? 593  LEU   A HD23 1 
ATOM   9084  N  N    . LEU   A  1  594 ? 68.586  15.136  4.051    1.00 101.17 ? 594  LEU   A N    1 
ATOM   9085  C  CA   . LEU   A  1  594 ? 68.929  14.920  5.450    1.00 105.60 ? 594  LEU   A CA   1 
ATOM   9086  C  C    . LEU   A  1  594 ? 70.422  15.135  5.653    1.00 115.17 ? 594  LEU   A C    1 
ATOM   9087  O  O    . LEU   A  1  594 ? 71.243  14.658  4.863    1.00 118.93 ? 594  LEU   A O    1 
ATOM   9088  C  CB   . LEU   A  1  594 ? 68.537  13.508  5.900    1.00 100.03 ? 594  LEU   A CB   1 
ATOM   9089  C  CG   . LEU   A  1  594 ? 67.072  13.133  5.666    1.00 94.39  ? 594  LEU   A CG   1 
ATOM   9090  C  CD1  . LEU   A  1  594 ? 66.828  11.672  6.021    1.00 93.47  ? 594  LEU   A CD1  1 
ATOM   9091  C  CD2  . LEU   A  1  594 ? 66.136  14.038  6.453    1.00 93.15  ? 594  LEU   A CD2  1 
ATOM   9092  H  H    . LEU   A  1  594 ? 69.027  14.634  3.510    1.00 121.44 ? 594  LEU   A H    1 
ATOM   9093  H  HA   . LEU   A  1  594 ? 68.454  15.559  6.003    1.00 126.76 ? 594  LEU   A HA   1 
ATOM   9094  H  HB2  . LEU   A  1  594 ? 69.082  12.870  5.413    1.00 120.08 ? 594  LEU   A HB2  1 
ATOM   9095  H  HB3  . LEU   A  1  594 ? 68.708  13.432  6.852    1.00 120.08 ? 594  LEU   A HB3  1 
ATOM   9096  H  HG   . LEU   A  1  594 ? 66.872  13.254  4.725    1.00 113.31 ? 594  LEU   A HG   1 
ATOM   9097  H  HD11 . LEU   A  1  594 ? 65.900  11.454  5.844    1.00 112.20 ? 594  LEU   A HD11 1 
ATOM   9098  H  HD12 . LEU   A  1  594 ? 67.408  11.114  5.480    1.00 112.20 ? 594  LEU   A HD12 1 
ATOM   9099  H  HD13 . LEU   A  1  594 ? 67.025  11.538  6.962    1.00 112.20 ? 594  LEU   A HD13 1 
ATOM   9100  H  HD21 . LEU   A  1  594 ? 65.220  13.761  6.293    1.00 111.81 ? 594  LEU   A HD21 1 
ATOM   9101  H  HD22 . LEU   A  1  594 ? 66.345  13.964  7.397    1.00 111.81 ? 594  LEU   A HD22 1 
ATOM   9102  H  HD23 . LEU   A  1  594 ? 66.260  14.954  6.157    1.00 111.81 ? 594  LEU   A HD23 1 
ATOM   9103  N  N    . ASP   A  1  595 ? 70.767  15.857  6.716    1.00 120.68 ? 595  ASP   A N    1 
ATOM   9104  C  CA   . ASP   A  1  595 ? 72.161  16.144  7.034    1.00 122.51 ? 595  ASP   A CA   1 
ATOM   9105  C  C    . ASP   A  1  595 ? 72.453  15.886  8.509    1.00 121.30 ? 595  ASP   A C    1 
ATOM   9106  O  O    . ASP   A  1  595 ? 73.608  15.899  8.933    1.00 122.22 ? 595  ASP   A O    1 
ATOM   9107  C  CB   . ASP   A  1  595 ? 72.503  17.593  6.680    1.00 127.77 ? 595  ASP   A CB   1 
ATOM   9108  C  CG   . ASP   A  1  595 ? 72.551  17.830  5.184    1.00 134.98 ? 595  ASP   A CG   1 
ATOM   9109  O  OD1  . ASP   A  1  595 ? 73.024  16.933  4.454    1.00 138.43 ? 595  ASP   A OD1  1 
ATOM   9110  O  OD2  . ASP   A  1  595 ? 72.116  18.912  4.738    1.00 138.07 ? 595  ASP   A OD2  1 
ATOM   9111  H  H    . ASP   A  1  595 ? 70.206  16.195  7.274    1.00 144.86 ? 595  ASP   A H    1 
ATOM   9112  H  HA   . ASP   A  1  595 ? 72.731  15.561  6.509    1.00 147.05 ? 595  ASP   A HA   1 
ATOM   9113  H  HB2  . ASP   A  1  595 ? 71.827  18.178  7.055    1.00 153.36 ? 595  ASP   A HB2  1 
ATOM   9114  H  HB3  . ASP   A  1  595 ? 73.373  17.812  7.048    1.00 153.36 ? 595  ASP   A HB3  1 
ATOM   9115  N  N    . GLY   B  2  1   ? 54.413  -5.867  15.525   1.00 153.90 ? 5    GLY   B N    1 
ATOM   9116  C  CA   . GLY   B  2  1   ? 53.154  -6.576  15.657   1.00 147.29 ? 5    GLY   B CA   1 
ATOM   9117  C  C    . GLY   B  2  1   ? 51.955  -5.676  15.450   1.00 141.85 ? 5    GLY   B C    1 
ATOM   9118  O  O    . GLY   B  2  1   ? 51.349  -5.672  14.378   1.00 140.38 ? 5    GLY   B O    1 
ATOM   9119  H  HA2  . GLY   B  2  1   ? 53.118  -7.288  14.999   1.00 176.79 ? 5    GLY   B HA2  1 
ATOM   9120  H  HA3  . GLY   B  2  1   ? 53.096  -6.962  16.545   1.00 176.79 ? 5    GLY   B HA3  1 
ATOM   9121  N  N    . CYS   B  2  2   ? 51.608  -4.907  16.482   1.00 139.60 ? 6    CYS   B N    1 
ATOM   9122  C  CA   . CYS   B  2  2   ? 50.484  -3.982  16.425   1.00 139.50 ? 6    CYS   B CA   1 
ATOM   9123  C  C    . CYS   B  2  2   ? 50.940  -2.527  16.456   1.00 142.19 ? 6    CYS   B C    1 
ATOM   9124  O  O    . CYS   B  2  2   ? 50.197  -1.640  16.885   1.00 140.31 ? 6    CYS   B O    1 
ATOM   9125  C  CB   . CYS   B  2  2   ? 49.503  -4.278  17.555   1.00 139.23 ? 6    CYS   B CB   1 
ATOM   9126  S  SG   . CYS   B  2  2   ? 47.987  -4.965  16.901   1.00 136.74 ? 6    CYS   B SG   1 
ATOM   9127  H  H    . CYS   B  2  2   ? 52.018  -4.905  17.238   1.00 167.55 ? 6    CYS   B H    1 
ATOM   9128  H  HA   . CYS   B  2  2   ? 50.013  -4.111  15.587   1.00 167.43 ? 6    CYS   B HA   1 
ATOM   9129  H  HB2  . CYS   B  2  2   ? 49.896  -4.920  18.167   1.00 167.11 ? 6    CYS   B HB2  1 
ATOM   9130  H  HB3  . CYS   B  2  2   ? 49.293  -3.456  18.026   1.00 167.11 ? 6    CYS   B HB3  1 
ATOM   9131  N  N    . ALA   B  2  3   ? 52.162  -2.273  15.987   1.00 142.78 ? 7    ALA   B N    1 
ATOM   9132  C  CA   . ALA   B  2  3   ? 52.677  -0.927  15.777   1.00 147.32 ? 7    ALA   B CA   1 
ATOM   9133  C  C    . ALA   B  2  3   ? 52.745  -0.576  14.295   1.00 151.94 ? 7    ALA   B C    1 
ATOM   9134  O  O    . ALA   B  2  3   ? 53.513  0.308   13.901   1.00 156.46 ? 7    ALA   B O    1 
ATOM   9135  C  CB   . ALA   B  2  3   ? 54.055  -0.784  16.423   1.00 148.98 ? 7    ALA   B CB   1 
ATOM   9136  H  H    . ALA   B  2  3   ? 52.727  -2.886  15.778   1.00 171.37 ? 7    ALA   B H    1 
ATOM   9137  H  HA   . ALA   B  2  3   ? 52.082  -0.292  16.205   1.00 176.82 ? 7    ALA   B HA   1 
ATOM   9138  H  HB1  . ALA   B  2  3   ? 54.521  -0.039  16.011   1.00 178.81 ? 7    ALA   B HB1  1 
ATOM   9139  H  HB2  . ALA   B  2  3   ? 53.944  -0.621  17.372   1.00 178.81 ? 7    ALA   B HB2  1 
ATOM   9140  H  HB3  . ALA   B  2  3   ? 54.555  -1.604  16.284   1.00 178.81 ? 7    ALA   B HB3  1 
ATOM   9141  N  N    . LEU   B  2  4   ? 51.952  -1.250  13.468   1.00 149.57 ? 8    LEU   B N    1 
ATOM   9142  C  CA   . LEU   B  2  4   ? 52.044  -1.116  12.024   1.00 147.60 ? 8    LEU   B CA   1 
ATOM   9143  C  C    . LEU   B  2  4   ? 51.384  0.181   11.560   1.00 146.14 ? 8    LEU   B C    1 
ATOM   9144  O  O    . LEU   B  2  4   ? 50.726  0.891   12.326   1.00 147.76 ? 8    LEU   B O    1 
ATOM   9145  C  CB   . LEU   B  2  4   ? 51.400  -2.326  11.347   1.00 143.41 ? 8    LEU   B CB   1 
ATOM   9146  C  CG   . LEU   B  2  4   ? 51.991  -2.866  10.042   1.00 142.24 ? 8    LEU   B CG   1 
ATOM   9147  C  CD1  . LEU   B  2  4   ? 53.508  -3.006  10.100   1.00 144.79 ? 8    LEU   B CD1  1 
ATOM   9148  C  CD2  . LEU   B  2  4   ? 51.357  -4.216  9.738    1.00 136.41 ? 8    LEU   B CD2  1 
ATOM   9149  H  H    . LEU   B  2  4   ? 51.342  -1.800  13.726   1.00 179.52 ? 8    LEU   B H    1 
ATOM   9150  H  HA   . LEU   B  2  4   ? 52.977  -1.080  11.761   1.00 177.15 ? 8    LEU   B HA   1 
ATOM   9151  H  HB2  . LEU   B  2  4   ? 51.427  -3.059  11.982   1.00 172.13 ? 8    LEU   B HB2  1 
ATOM   9152  H  HB3  . LEU   B  2  4   ? 50.479  -2.090  11.152   1.00 172.13 ? 8    LEU   B HB3  1 
ATOM   9153  H  HG   . LEU   B  2  4   ? 51.799  -2.234  9.331    1.00 170.73 ? 8    LEU   B HG   1 
ATOM   9154  H  HD11 . LEU   B  2  4   ? 53.826  -3.348  9.250    1.00 173.78 ? 8    LEU   B HD11 1 
ATOM   9155  H  HD12 . LEU   B  2  4   ? 53.899  -2.136  10.274   1.00 173.78 ? 8    LEU   B HD12 1 
ATOM   9156  H  HD13 . LEU   B  2  4   ? 53.741  -3.622  10.812   1.00 173.78 ? 8    LEU   B HD13 1 
ATOM   9157  H  HD21 . LEU   B  2  4   ? 51.480  -4.418  8.797    1.00 163.73 ? 8    LEU   B HD21 1 
ATOM   9158  H  HD22 . LEU   B  2  4   ? 51.785  -4.896  10.281   1.00 163.73 ? 8    LEU   B HD22 1 
ATOM   9159  H  HD23 . LEU   B  2  4   ? 50.410  -4.175  9.946    1.00 163.73 ? 8    LEU   B HD23 1 
ATOM   9160  N  N    . GLY   B  2  5   ? 51.576  0.488   10.277   1.00 145.69 ? 9    GLY   B N    1 
ATOM   9161  C  CA   . GLY   B  2  5   ? 51.030  1.693   9.683    1.00 144.02 ? 9    GLY   B CA   1 
ATOM   9162  C  C    . GLY   B  2  5   ? 49.559  1.881   9.985    1.00 142.05 ? 9    GLY   B C    1 
ATOM   9163  O  O    . GLY   B  2  5   ? 48.790  0.916   9.996    1.00 137.52 ? 9    GLY   B O    1 
ATOM   9164  H  H    . GLY   B  2  5   ? 52.026  0.003   9.726    1.00 174.86 ? 9    GLY   B H    1 
ATOM   9165  H  HA2  . GLY   B  2  5   ? 51.512  2.463   10.024   1.00 172.86 ? 9    GLY   B HA2  1 
ATOM   9166  H  HA3  . GLY   B  2  5   ? 51.140  1.652   8.720    1.00 172.86 ? 9    GLY   B HA3  1 
ATOM   9167  N  N    . GLY   B  2  6   ? 49.156  3.126   10.221   1.00 143.32 ? 10   GLY   B N    1 
ATOM   9168  C  CA   . GLY   B  2  6   ? 47.825  3.405   10.717   1.00 139.34 ? 10   GLY   B CA   1 
ATOM   9169  C  C    . GLY   B  2  6   ? 47.831  3.404   12.229   1.00 138.92 ? 10   GLY   B C    1 
ATOM   9170  O  O    . GLY   B  2  6   ? 48.820  3.814   12.845   1.00 144.40 ? 10   GLY   B O    1 
ATOM   9171  H  H    . GLY   B  2  6   ? 49.641  3.826   10.101   1.00 172.02 ? 10   GLY   B H    1 
ATOM   9172  H  HA2  . GLY   B  2  6   ? 47.529  4.273   10.401   1.00 167.24 ? 10   GLY   B HA2  1 
ATOM   9173  H  HA3  . GLY   B  2  6   ? 47.206  2.727   10.402   1.00 167.24 ? 10   GLY   B HA3  1 
ATOM   9174  N  N    . ALA   B  2  7   ? 46.744  2.943   12.842   1.00 134.24 ? 11   ALA   B N    1 
ATOM   9175  C  CA   . ALA   B  2  7   ? 46.678  2.776   14.291   1.00 131.35 ? 11   ALA   B CA   1 
ATOM   9176  C  C    . ALA   B  2  7   ? 47.108  4.052   15.013   1.00 134.50 ? 11   ALA   B C    1 
ATOM   9177  O  O    . ALA   B  2  7   ? 47.979  4.043   15.885   1.00 137.54 ? 11   ALA   B O    1 
ATOM   9178  C  CB   . ALA   B  2  7   ? 47.529  1.586   14.735   1.00 131.31 ? 11   ALA   B CB   1 
ATOM   9179  H  H    . ALA   B  2  7   ? 46.021  2.717   12.434   1.00 161.13 ? 11   ALA   B H    1 
ATOM   9180  H  HA   . ALA   B  2  7   ? 45.756  2.601   14.536   1.00 157.66 ? 11   ALA   B HA   1 
ATOM   9181  H  HB1  . ALA   B  2  7   ? 47.416  1.455   15.689   1.00 157.61 ? 11   ALA   B HB1  1 
ATOM   9182  H  HB2  . ALA   B  2  7   ? 47.239  0.794   14.255   1.00 157.61 ? 11   ALA   B HB2  1 
ATOM   9183  H  HB3  . ALA   B  2  7   ? 48.460  1.771   14.534   1.00 157.61 ? 11   ALA   B HB3  1 
ATOM   9184  N  N    . GLU   B  2  8   ? 46.491  5.168   14.627   1.00 132.69 ? 12   GLU   B N    1 
ATOM   9185  C  CA   . GLU   B  2  8   ? 46.668  6.441   15.314   1.00 136.17 ? 12   GLU   B CA   1 
ATOM   9186  C  C    . GLU   B  2  8   ? 45.417  6.845   16.085   1.00 134.37 ? 12   GLU   B C    1 
ATOM   9187  O  O    . GLU   B  2  8   ? 45.296  8.003   16.498   1.00 141.19 ? 12   GLU   B O    1 
ATOM   9188  C  CB   . GLU   B  2  8   ? 47.064  7.531   14.315   1.00 137.06 ? 12   GLU   B CB   1 
ATOM   9189  C  CG   . GLU   B  2  8   ? 48.525  7.960   14.428   1.00 135.51 ? 12   GLU   B CG   1 
ATOM   9190  C  CD   . GLU   B  2  8   ? 48.994  8.798   13.254   1.00 136.83 ? 12   GLU   B CD   1 
ATOM   9191  O  OE1  . GLU   B  2  8   ? 48.198  9.017   12.316   1.00 137.68 ? 12   GLU   B OE1  1 
ATOM   9192  O  OE2  . GLU   B  2  8   ? 50.164  9.236   13.268   1.00 140.37 ? 12   GLU   B OE2  1 
ATOM   9193  H  H    . GLU   B  2  8   ? 45.954  5.211   13.956   1.00 159.27 ? 12   GLU   B H    1 
ATOM   9194  H  HA   . GLU   B  2  8   ? 47.395  6.360   15.951   1.00 163.44 ? 12   GLU   B HA   1 
ATOM   9195  H  HB2  . GLU   B  2  8   ? 46.921  7.198   13.415   1.00 164.50 ? 12   GLU   B HB2  1 
ATOM   9196  H  HB3  . GLU   B  2  8   ? 46.512  8.314   14.470   1.00 164.50 ? 12   GLU   B HB3  1 
ATOM   9197  H  HG2  . GLU   B  2  8   ? 48.636  8.488   15.235   1.00 162.65 ? 12   GLU   B HG2  1 
ATOM   9198  H  HG3  . GLU   B  2  8   ? 49.083  7.167   14.471   1.00 162.65 ? 12   GLU   B HG3  1 
ATOM   9199  N  N    . THR   B  2  9   ? 44.490  5.911   16.290   1.00 123.11 ? 13   THR   B N    1 
ATOM   9200  C  CA   . THR   B  2  9   ? 43.276  6.148   17.056   1.00 113.00 ? 13   THR   B CA   1 
ATOM   9201  C  C    . THR   B  2  9   ? 42.908  4.852   17.764   1.00 107.81 ? 13   THR   B C    1 
ATOM   9202  O  O    . THR   B  2  9   ? 43.230  3.760   17.287   1.00 101.79 ? 13   THR   B O    1 
ATOM   9203  C  CB   . THR   B  2  9   ? 42.122  6.613   16.159   1.00 107.62 ? 13   THR   B CB   1 
ATOM   9204  O  OG1  . THR   B  2  9   ? 42.553  7.713   15.348   1.00 108.89 ? 13   THR   B OG1  1 
ATOM   9205  C  CG2  . THR   B  2  9   ? 40.926  7.045   16.997   1.00 107.49 ? 13   THR   B CG2  1 
ATOM   9206  H  H    . THR   B  2  9   ? 44.545  5.109   15.986   1.00 147.77 ? 13   THR   B H    1 
ATOM   9207  H  HA   . THR   B  2  9   ? 43.429  6.838   17.721   1.00 135.64 ? 13   THR   B HA   1 
ATOM   9208  H  HB   . THR   B  2  9   ? 41.845  5.879   15.589   1.00 129.18 ? 13   THR   B HB   1 
ATOM   9209  H  HG1  . THR   B  2  9   ? 41.901  8.032   14.925   1.00 130.71 ? 13   THR   B HG1  1 
ATOM   9210  H  HG21 . THR   B  2  9   ? 40.348  7.624   16.476   1.00 129.02 ? 13   THR   B HG21 1 
ATOM   9211  H  HG22 . THR   B  2  9   ? 40.421  6.267   17.279   1.00 129.02 ? 13   THR   B HG22 1 
ATOM   9212  H  HG23 . THR   B  2  9   ? 41.228  7.527   17.783   1.00 129.02 ? 13   THR   B HG23 1 
ATOM   9213  N  N    . CYS   B  2  10  ? 42.237  4.978   18.912   1.00 110.93 ? 14   CYS   B N    1 
ATOM   9214  C  CA   . CYS   B  2  10  ? 41.857  3.788   19.668   1.00 112.20 ? 14   CYS   B CA   1 
ATOM   9215  C  C    . CYS   B  2  10  ? 41.038  2.837   18.802   1.00 109.84 ? 14   CYS   B C    1 
ATOM   9216  O  O    . CYS   B  2  10  ? 41.306  1.631   18.756   1.00 105.66 ? 14   CYS   B O    1 
ATOM   9217  C  CB   . CYS   B  2  10  ? 41.078  4.183   20.925   1.00 117.10 ? 14   CYS   B CB   1 
ATOM   9218  S  SG   . CYS   B  2  10  ? 41.050  2.889   22.200   1.00 116.36 ? 14   CYS   B SG   1 
ATOM   9219  H  H    . CYS   B  2  10  ? 41.997  5.724   19.265   1.00 133.15 ? 14   CYS   B H    1 
ATOM   9220  H  HA   . CYS   B  2  10  ? 42.661  3.327   19.953   1.00 134.68 ? 14   CYS   B HA   1 
ATOM   9221  H  HB2  . CYS   B  2  10  ? 41.488  4.972   21.311   1.00 140.55 ? 14   CYS   B HB2  1 
ATOM   9222  H  HB3  . CYS   B  2  10  ? 40.160  4.374   20.676   1.00 140.55 ? 14   CYS   B HB3  1 
ATOM   9223  N  N    . GLU   B  2  11  ? 40.037  3.370   18.097   1.00 111.08 ? 15   GLU   B N    1 
ATOM   9224  C  CA   . GLU   B  2  11  ? 39.236  2.542   17.202   1.00 112.52 ? 15   GLU   B CA   1 
ATOM   9225  C  C    . GLU   B  2  11  ? 40.075  2.013   16.045   1.00 111.29 ? 15   GLU   B C    1 
ATOM   9226  O  O    . GLU   B  2  11  ? 39.882  0.875   15.601   1.00 111.11 ? 15   GLU   B O    1 
ATOM   9227  C  CB   . GLU   B  2  11  ? 38.047  3.350   16.683   1.00 120.67 ? 15   GLU   B CB   1 
ATOM   9228  C  CG   . GLU   B  2  11  ? 36.915  2.526   16.094   1.00 127.73 ? 15   GLU   B CG   1 
ATOM   9229  C  CD   . GLU   B  2  11  ? 35.765  3.395   15.622   1.00 135.27 ? 15   GLU   B CD   1 
ATOM   9230  O  OE1  . GLU   B  2  11  ? 35.869  4.634   15.743   1.00 139.51 ? 15   GLU   B OE1  1 
ATOM   9231  O  OE2  . GLU   B  2  11  ? 34.759  2.841   15.131   1.00 135.24 ? 15   GLU   B OE2  1 
ATOM   9232  H  H    . GLU   B  2  11  ? 39.806  4.198   18.120   1.00 133.34 ? 15   GLU   B H    1 
ATOM   9233  H  HA   . GLU   B  2  11  ? 38.892  1.779   17.693   1.00 135.06 ? 15   GLU   B HA   1 
ATOM   9234  H  HB2  . GLU   B  2  11  ? 37.680  3.862   17.420   1.00 144.84 ? 15   GLU   B HB2  1 
ATOM   9235  H  HB3  . GLU   B  2  11  ? 38.363  3.948   15.988   1.00 144.84 ? 15   GLU   B HB3  1 
ATOM   9236  H  HG2  . GLU   B  2  11  ? 37.248  2.025   15.333   1.00 153.32 ? 15   GLU   B HG2  1 
ATOM   9237  H  HG3  . GLU   B  2  11  ? 36.578  1.918   16.770   1.00 153.32 ? 15   GLU   B HG3  1 
ATOM   9238  N  N    . ASP   B  2  12  ? 41.008  2.825   15.540   1.00 111.59 ? 16   ASP   B N    1 
ATOM   9239  C  CA   . ASP   B  2  12  ? 41.931  2.340   14.519   1.00 109.84 ? 16   ASP   B CA   1 
ATOM   9240  C  C    . ASP   B  2  12  ? 42.806  1.222   15.067   1.00 110.77 ? 16   ASP   B C    1 
ATOM   9241  O  O    . ASP   B  2  12  ? 43.079  0.234   14.374   1.00 103.79 ? 16   ASP   B O    1 
ATOM   9242  C  CB   . ASP   B  2  12  ? 42.802  3.488   14.007   1.00 108.77 ? 16   ASP   B CB   1 
ATOM   9243  C  CG   . ASP   B  2  12  ? 42.088  4.358   12.991   1.00 106.24 ? 16   ASP   B CG   1 
ATOM   9244  O  OD1  . ASP   B  2  12  ? 40.912  4.078   12.679   1.00 103.35 ? 16   ASP   B OD1  1 
ATOM   9245  O  OD2  . ASP   B  2  12  ? 42.710  5.324   12.499   1.00 107.01 ? 16   ASP   B OD2  1 
ATOM   9246  H  H    . ASP   B  2  12  ? 41.123  3.646   15.768   1.00 133.95 ? 16   ASP   B H    1 
ATOM   9247  H  HA   . ASP   B  2  12  ? 41.418  1.994   13.772   1.00 131.85 ? 16   ASP   B HA   1 
ATOM   9248  H  HB2  . ASP   B  2  12  ? 43.057  4.049   14.755   1.00 130.57 ? 16   ASP   B HB2  1 
ATOM   9249  H  HB3  . ASP   B  2  12  ? 43.593  3.119   13.583   1.00 130.57 ? 16   ASP   B HB3  1 
ATOM   9250  N  N    . CYS   B  2  13  ? 43.259  1.367   16.313   1.00 116.91 ? 17   CYS   B N    1 
ATOM   9251  C  CA   . CYS   B  2  13  ? 44.082  0.340   16.937   1.00 120.78 ? 17   CYS   B CA   1 
ATOM   9252  C  C    . CYS   B  2  13  ? 43.290  -0.928  17.222   1.00 117.37 ? 17   CYS   B C    1 
ATOM   9253  O  O    . CYS   B  2  13  ? 43.867  -2.020  17.268   1.00 116.62 ? 17   CYS   B O    1 
ATOM   9254  C  CB   . CYS   B  2  13  ? 44.675  0.881   18.234   1.00 124.22 ? 17   CYS   B CB   1 
ATOM   9255  S  SG   . CYS   B  2  13  ? 45.572  -0.335  19.202   1.00 121.23 ? 17   CYS   B SG   1 
ATOM   9256  H  H    . CYS   B  2  13  ? 43.104  2.048   16.814   1.00 140.33 ? 17   CYS   B H    1 
ATOM   9257  H  HA   . CYS   B  2  13  ? 44.805  0.110   16.333   1.00 144.98 ? 17   CYS   B HA   1 
ATOM   9258  H  HB2  . CYS   B  2  13  ? 45.293  1.597   18.016   1.00 149.10 ? 17   CYS   B HB2  1 
ATOM   9259  H  HB3  . CYS   B  2  13  ? 43.954  1.222   18.786   1.00 149.10 ? 17   CYS   B HB3  1 
ATOM   9260  N  N    . LEU   B  2  14  ? 41.979  -0.810  17.432   1.00 116.78 ? 18   LEU   B N    1 
ATOM   9261  C  CA   . LEU   B  2  14  ? 41.192  -1.988  17.772   1.00 112.83 ? 18   LEU   B CA   1 
ATOM   9262  C  C    . LEU   B  2  14  ? 41.117  -2.969  16.611   1.00 109.93 ? 18   LEU   B C    1 
ATOM   9263  O  O    . LEU   B  2  14  ? 41.086  -4.185  16.832   1.00 109.46 ? 18   LEU   B O    1 
ATOM   9264  C  CB   . LEU   B  2  14  ? 39.780  -1.582  18.199   1.00 110.78 ? 18   LEU   B CB   1 
ATOM   9265  C  CG   . LEU   B  2  14  ? 39.572  -1.041  19.618   1.00 113.35 ? 18   LEU   B CG   1 
ATOM   9266  C  CD1  . LEU   B  2  14  ? 38.087  -0.897  19.895   1.00 111.26 ? 18   LEU   B CD1  1 
ATOM   9267  C  CD2  . LEU   B  2  14  ? 40.210  -1.920  20.682   1.00 113.48 ? 18   LEU   B CD2  1 
ATOM   9268  H  H    . LEU   B  2  14  ? 41.534  -0.076  17.384   1.00 140.17 ? 18   LEU   B H    1 
ATOM   9269  H  HA   . LEU   B  2  14  ? 41.618  -2.432  18.521   1.00 135.43 ? 18   LEU   B HA   1 
ATOM   9270  H  HB2  . LEU   B  2  14  ? 39.479  -0.888  17.592   1.00 132.97 ? 18   LEU   B HB2  1 
ATOM   9271  H  HB3  . LEU   B  2  14  ? 39.213  -2.365  18.116   1.00 132.97 ? 18   LEU   B HB3  1 
ATOM   9272  H  HG   . LEU   B  2  14  ? 40.006  -0.175  19.671   1.00 136.06 ? 18   LEU   B HG   1 
ATOM   9273  H  HD11 . LEU   B  2  14  ? 37.966  -0.536  20.787   1.00 133.55 ? 18   LEU   B HD11 1 
ATOM   9274  H  HD12 . LEU   B  2  14  ? 37.700  -0.296  19.240   1.00 133.55 ? 18   LEU   B HD12 1 
ATOM   9275  H  HD13 . LEU   B  2  14  ? 37.669  -1.770  19.832   1.00 133.55 ? 18   LEU   B HD13 1 
ATOM   9276  H  HD21 . LEU   B  2  14  ? 40.168  -1.463  21.537   1.00 136.21 ? 18   LEU   B HD21 1 
ATOM   9277  H  HD22 . LEU   B  2  14  ? 39.725  -2.759  20.732   1.00 136.21 ? 18   LEU   B HD22 1 
ATOM   9278  H  HD23 . LEU   B  2  14  ? 41.135  -2.086  20.442   1.00 136.21 ? 18   LEU   B HD23 1 
ATOM   9279  N  N    . LEU   B  2  15  ? 41.095  -2.471  15.378   1.00 109.45 ? 19   LEU   B N    1 
ATOM   9280  C  CA   . LEU   B  2  15  ? 40.853  -3.328  14.228   1.00 110.57 ? 19   LEU   B CA   1 
ATOM   9281  C  C    . LEU   B  2  15  ? 42.110  -4.011  13.705   1.00 114.61 ? 19   LEU   B C    1 
ATOM   9282  O  O    . LEU   B  2  15  ? 41.997  -5.021  13.002   1.00 108.42 ? 19   LEU   B O    1 
ATOM   9283  C  CB   . LEU   B  2  15  ? 40.205  -2.512  13.104   1.00 109.83 ? 19   LEU   B CB   1 
ATOM   9284  C  CG   . LEU   B  2  15  ? 39.959  -3.237  11.780   1.00 110.50 ? 19   LEU   B CG   1 
ATOM   9285  C  CD1  . LEU   B  2  15  ? 39.255  -4.570  11.998   1.00 107.43 ? 19   LEU   B CD1  1 
ATOM   9286  C  CD2  . LEU   B  2  15  ? 39.145  -2.354  10.846   1.00 112.56 ? 19   LEU   B CD2  1 
ATOM   9287  H  H    . LEU   B  2  15  ? 41.218  -1.642  15.184   1.00 131.38 ? 19   LEU   B H    1 
ATOM   9288  H  HA   . LEU   B  2  15  ? 40.235  -4.029  14.486   1.00 132.72 ? 19   LEU   B HA   1 
ATOM   9289  H  HB2  . LEU   B  2  15  ? 39.343  -2.199  13.420   1.00 131.83 ? 19   LEU   B HB2  1 
ATOM   9290  H  HB3  . LEU   B  2  15  ? 40.782  -1.757  12.911   1.00 131.83 ? 19   LEU   B HB3  1 
ATOM   9291  H  HG   . LEU   B  2  15  ? 40.816  -3.426  11.365   1.00 132.64 ? 19   LEU   B HG   1 
ATOM   9292  H  HD11 . LEU   B  2  15  ? 39.016  -4.946  11.137   1.00 128.95 ? 19   LEU   B HD11 1 
ATOM   9293  H  HD12 . LEU   B  2  15  ? 39.854  -5.171  12.467   1.00 128.95 ? 19   LEU   B HD12 1 
ATOM   9294  H  HD13 . LEU   B  2  15  ? 38.455  -4.421  12.527   1.00 128.95 ? 19   LEU   B HD13 1 
ATOM   9295  H  HD21 . LEU   B  2  15  ? 38.905  -2.866  10.058   1.00 135.10 ? 19   LEU   B HD21 1 
ATOM   9296  H  HD22 . LEU   B  2  15  ? 38.344  -2.062  11.307   1.00 135.10 ? 19   LEU   B HD22 1 
ATOM   9297  H  HD23 . LEU   B  2  15  ? 39.680  -1.586  10.592   1.00 135.10 ? 19   LEU   B HD23 1 
ATOM   9298  N  N    . ILE   B  2  16  ? 43.303  -3.508  14.024   1.00 120.70 ? 20   ILE   B N    1 
ATOM   9299  C  CA   . ILE   B  2  16  ? 44.491  -4.131  13.448   1.00 124.88 ? 20   ILE   B CA   1 
ATOM   9300  C  C    . ILE   B  2  16  ? 44.675  -5.552  13.984   1.00 124.10 ? 20   ILE   B C    1 
ATOM   9301  O  O    . ILE   B  2  16  ? 45.123  -6.439  13.249   1.00 134.27 ? 20   ILE   B O    1 
ATOM   9302  C  CB   . ILE   B  2  16  ? 45.742  -3.261  13.682   1.00 130.32 ? 20   ILE   B CB   1 
ATOM   9303  C  CG1  . ILE   B  2  16  ? 45.999  -3.059  15.171   1.00 128.38 ? 20   ILE   B CG1  1 
ATOM   9304  C  CG2  . ILE   B  2  16  ? 45.597  -1.908  12.993   1.00 133.12 ? 20   ILE   B CG2  1 
ATOM   9305  C  CD1  . ILE   B  2  16  ? 47.210  -2.186  15.464   1.00 126.65 ? 20   ILE   B CD1  1 
ATOM   9306  H  H    . ILE   B  2  16  ? 43.444  -2.840  14.546   1.00 144.88 ? 20   ILE   B H    1 
ATOM   9307  H  HA   . ILE   B  2  16  ? 44.360  -4.191  12.489   1.00 149.89 ? 20   ILE   B HA   1 
ATOM   9308  H  HB   . ILE   B  2  16  ? 46.498  -3.732  13.299   1.00 156.42 ? 20   ILE   B HB   1 
ATOM   9309  H  HG12 . ILE   B  2  16  ? 45.223  -2.633  15.567   1.00 154.09 ? 20   ILE   B HG12 1 
ATOM   9310  H  HG13 . ILE   B  2  16  ? 46.149  -3.924  15.582   1.00 154.09 ? 20   ILE   B HG13 1 
ATOM   9311  H  HG21 . ILE   B  2  16  ? 46.435  -1.426  13.064   1.00 159.78 ? 20   ILE   B HG21 1 
ATOM   9312  H  HG22 . ILE   B  2  16  ? 45.376  -2.052  12.059   1.00 159.78 ? 20   ILE   B HG22 1 
ATOM   9313  H  HG23 . ILE   B  2  16  ? 44.888  -1.407  13.426   1.00 159.78 ? 20   ILE   B HG23 1 
ATOM   9314  H  HD11 . ILE   B  2  16  ? 47.459  -2.295  16.395   1.00 152.02 ? 20   ILE   B HD11 1 
ATOM   9315  H  HD12 . ILE   B  2  16  ? 47.943  -2.460  14.891   1.00 152.02 ? 20   ILE   B HD12 1 
ATOM   9316  H  HD13 . ILE   B  2  16  ? 46.981  -1.260  15.289   1.00 152.02 ? 20   ILE   B HD13 1 
ATOM   9317  N  N    . GLY   B  2  17  ? 44.316  -5.806  15.245   1.00 115.09 ? 21   GLY   B N    1 
ATOM   9318  C  CA   . GLY   B  2  17  ? 44.445  -7.130  15.819   1.00 114.07 ? 21   GLY   B CA   1 
ATOM   9319  C  C    . GLY   B  2  17  ? 43.605  -7.324  17.071   1.00 112.31 ? 21   GLY   B C    1 
ATOM   9320  O  O    . GLY   B  2  17  ? 43.024  -6.362  17.594   1.00 113.67 ? 21   GLY   B O    1 
ATOM   9321  H  H    . GLY   B  2  17  ? 43.994  -5.220  15.784   1.00 138.14 ? 21   GLY   B H    1 
ATOM   9322  H  HA2  . GLY   B  2  17  ? 44.168  -7.789  15.164   1.00 136.92 ? 21   GLY   B HA2  1 
ATOM   9323  H  HA3  . GLY   B  2  17  ? 45.374  -7.286  16.052   1.00 136.92 ? 21   GLY   B HA3  1 
ATOM   9324  N  N    . PRO   B  2  18  ? 43.512  -8.558  17.573   1.00 113.69 ? 22   PRO   B N    1 
ATOM   9325  C  CA   . PRO   B  2  18  ? 42.729  -8.803  18.795   1.00 113.93 ? 22   PRO   B CA   1 
ATOM   9326  C  C    . PRO   B  2  18  ? 43.536  -8.762  20.083   1.00 115.55 ? 22   PRO   B C    1 
ATOM   9327  O  O    . PRO   B  2  18  ? 42.940  -8.735  21.172   1.00 114.84 ? 22   PRO   B O    1 
ATOM   9328  C  CB   . PRO   B  2  18  ? 42.153  -10.210 18.555   1.00 115.81 ? 22   PRO   B CB   1 
ATOM   9329  C  CG   . PRO   B  2  18  ? 43.214  -10.896 17.769   1.00 118.62 ? 22   PRO   B CG   1 
ATOM   9330  C  CD   . PRO   B  2  18  ? 43.903  -9.835  16.926   1.00 117.39 ? 22   PRO   B CD   1 
ATOM   9331  H  HA   . PRO   B  2  18  ? 41.997  -8.170  18.859   1.00 136.75 ? 22   PRO   B HA   1 
ATOM   9332  H  HB2  . PRO   B  2  18  ? 41.997  -10.657 19.401   1.00 139.01 ? 22   PRO   B HB2  1 
ATOM   9333  H  HB3  . PRO   B  2  18  ? 41.325  -10.152 18.053   1.00 139.01 ? 22   PRO   B HB3  1 
ATOM   9334  H  HG2  . PRO   B  2  18  ? 43.847  -11.310 18.375   1.00 142.38 ? 22   PRO   B HG2  1 
ATOM   9335  H  HG3  . PRO   B  2  18  ? 42.809  -11.569 17.201   1.00 142.38 ? 22   PRO   B HG3  1 
ATOM   9336  H  HD2  . PRO   B  2  18  ? 44.866  -9.950  16.948   1.00 140.91 ? 22   PRO   B HD2  1 
ATOM   9337  H  HD3  . PRO   B  2  18  ? 43.587  -9.865  16.009   1.00 140.91 ? 22   PRO   B HD3  1 
ATOM   9338  N  N    . GLN   B  2  19  ? 44.864  -8.754  20.008   1.00 119.84 ? 23   GLN   B N    1 
ATOM   9339  C  CA   . GLN   B  2  19  ? 45.713  -8.752  21.193   1.00 122.63 ? 23   GLN   B CA   1 
ATOM   9340  C  C    . GLN   B  2  19  ? 46.275  -7.372  21.524   1.00 125.09 ? 23   GLN   B C    1 
ATOM   9341  O  O    . GLN   B  2  19  ? 47.112  -7.256  22.424   1.00 131.04 ? 23   GLN   B O    1 
ATOM   9342  C  CB   . GLN   B  2  19  ? 46.863  -9.754  21.012   1.00 126.99 ? 23   GLN   B CB   1 
ATOM   9343  C  CG   . GLN   B  2  19  ? 47.740  -9.975  22.239   1.00 136.16 ? 23   GLN   B CG   1 
ATOM   9344  C  CD   . GLN   B  2  19  ? 48.792  -11.023 22.026   1.00 142.35 ? 23   GLN   B CD   1 
ATOM   9345  O  OE1  . GLN   B  2  19  ? 49.578  -10.958 21.079   1.00 146.63 ? 23   GLN   B OE1  1 
ATOM   9346  N  NE2  . GLN   B  2  19  ? 48.862  -11.964 22.951   1.00 141.61 ? 23   GLN   B NE2  1 
ATOM   9347  H  H    . GLN   B  2  19  ? 45.303  -8.749  19.268   1.00 143.85 ? 23   GLN   B H    1 
ATOM   9348  H  HA   . GLN   B  2  19  ? 45.177  -9.036  21.950   1.00 147.19 ? 23   GLN   B HA   1 
ATOM   9349  H  HB2  . GLN   B  2  19  ? 46.484  -10.613 20.770   1.00 152.43 ? 23   GLN   B HB2  1 
ATOM   9350  H  HB3  . GLN   B  2  19  ? 47.438  -9.432  20.301   1.00 152.43 ? 23   GLN   B HB3  1 
ATOM   9351  H  HG2  . GLN   B  2  19  ? 48.186  -9.144  22.461   1.00 163.43 ? 23   GLN   B HG2  1 
ATOM   9352  H  HG3  . GLN   B  2  19  ? 47.180  -10.259 22.978   1.00 163.43 ? 23   GLN   B HG3  1 
ATOM   9353  H  HE21 . GLN   B  2  19  ? 48.324  -11.949 23.622   1.00 169.97 ? 23   GLN   B HE21 1 
ATOM   9354  H  HE22 . GLN   B  2  19  ? 49.447  -12.592 22.883   1.00 169.97 ? 23   GLN   B HE22 1 
ATOM   9355  N  N    . CYS   B  2  20  ? 45.829  -6.326  20.849   1.00 121.86 ? 24   CYS   B N    1 
ATOM   9356  C  CA   . CYS   B  2  20  ? 46.453  -5.018  20.973   1.00 125.35 ? 24   CYS   B CA   1 
ATOM   9357  C  C    . CYS   B  2  20  ? 45.643  -4.098  21.875   1.00 121.66 ? 24   CYS   B C    1 
ATOM   9358  O  O    . CYS   B  2  20  ? 44.431  -4.260  22.035   1.00 119.02 ? 24   CYS   B O    1 
ATOM   9359  C  CB   . CYS   B  2  20  ? 46.626  -4.432  19.579   1.00 129.80 ? 24   CYS   B CB   1 
ATOM   9360  S  SG   . CYS   B  2  20  ? 47.048  -5.802  18.479   1.00 132.48 ? 24   CYS   B SG   1 
ATOM   9361  H  H    . CYS   B  2  20  ? 45.160  -6.347  20.308   1.00 146.27 ? 24   CYS   B H    1 
ATOM   9362  H  HA   . CYS   B  2  20  ? 47.324  -5.089  21.395   1.00 150.46 ? 24   CYS   B HA   1 
ATOM   9363  H  HB2  . CYS   B  2  20  ? 45.800  -4.020  19.282   1.00 155.80 ? 24   CYS   B HB2  1 
ATOM   9364  H  HB3  . CYS   B  2  20  ? 47.344  -3.779  19.574   1.00 155.80 ? 24   CYS   B HB3  1 
ATOM   9365  N  N    . ALA   B  2  21  ? 46.343  -3.139  22.487   1.00 120.12 ? 25   ALA   B N    1 
ATOM   9366  C  CA   . ALA   B  2  21  ? 45.785  -2.228  23.478   1.00 117.93 ? 25   ALA   B CA   1 
ATOM   9367  C  C    . ALA   B  2  21  ? 46.038  -0.779  23.061   1.00 114.15 ? 25   ALA   B C    1 
ATOM   9368  O  O    . ALA   B  2  21  ? 46.672  -0.502  22.038   1.00 111.44 ? 25   ALA   B O    1 
ATOM   9369  C  CB   . ALA   B  2  21  ? 46.385  -2.495  24.867   1.00 122.52 ? 25   ALA   B CB   1 
ATOM   9370  H  H    . ALA   B  2  21  ? 47.177  -2.994  22.335   1.00 144.19 ? 25   ALA   B H    1 
ATOM   9371  H  HA   . ALA   B  2  21  ? 44.825  -2.366  23.514   1.00 141.55 ? 25   ALA   B HA   1 
ATOM   9372  H  HB1  . ALA   B  2  21  ? 45.898  -1.976  25.527   1.00 147.06 ? 25   ALA   B HB1  1 
ATOM   9373  H  HB2  . ALA   B  2  21  ? 46.308  -3.441  25.068   1.00 147.06 ? 25   ALA   B HB2  1 
ATOM   9374  H  HB3  . ALA   B  2  21  ? 47.319  -2.233  24.864   1.00 147.06 ? 25   ALA   B HB3  1 
ATOM   9375  N  N    . TRP   B  2  22  ? 45.530  0.149   23.881   1.00 111.96 ? 26   TRP   B N    1 
ATOM   9376  C  CA   . TRP   B  2  22  ? 45.665  1.589   23.683   1.00 113.79 ? 26   TRP   B CA   1 
ATOM   9377  C  C    . TRP   B  2  22  ? 46.014  2.249   25.015   1.00 125.04 ? 26   TRP   B C    1 
ATOM   9378  O  O    . TRP   B  2  22  ? 45.642  1.754   26.080   1.00 125.62 ? 26   TRP   B O    1 
ATOM   9379  C  CB   . TRP   B  2  22  ? 44.363  2.177   23.111   1.00 108.33 ? 26   TRP   B CB   1 
ATOM   9380  C  CG   . TRP   B  2  22  ? 44.435  3.613   22.716   1.00 107.87 ? 26   TRP   B CG   1 
ATOM   9381  C  CD1  . TRP   B  2  22  ? 43.914  4.677   23.394   1.00 114.30 ? 26   TRP   B CD1  1 
ATOM   9382  C  CD2  . TRP   B  2  22  ? 45.050  4.149   21.539   1.00 108.35 ? 26   TRP   B CD2  1 
ATOM   9383  N  NE1  . TRP   B  2  22  ? 44.171  5.843   22.714   1.00 113.07 ? 26   TRP   B NE1  1 
ATOM   9384  C  CE2  . TRP   B  2  22  ? 44.868  5.546   21.572   1.00 111.67 ? 26   TRP   B CE2  1 
ATOM   9385  C  CE3  . TRP   B  2  22  ? 45.740  3.583   20.461   1.00 107.60 ? 26   TRP   B CE3  1 
ATOM   9386  C  CZ2  . TRP   B  2  22  ? 45.351  6.386   20.571   1.00 114.24 ? 26   TRP   B CZ2  1 
ATOM   9387  C  CZ3  . TRP   B  2  22  ? 46.219  4.417   19.469   1.00 112.19 ? 26   TRP   B CZ3  1 
ATOM   9388  C  CH2  . TRP   B  2  22  ? 46.023  5.803   19.530   1.00 115.34 ? 26   TRP   B CH2  1 
ATOM   9389  H  H    . TRP   B  2  22  ? 45.083  -0.044  24.590   1.00 134.39 ? 26   TRP   B H    1 
ATOM   9390  H  HA   . TRP   B  2  22  ? 46.387  1.782   23.065   1.00 136.59 ? 26   TRP   B HA   1 
ATOM   9391  H  HB2  . TRP   B  2  22  ? 44.119  1.671   22.321   1.00 130.04 ? 26   TRP   B HB2  1 
ATOM   9392  H  HB3  . TRP   B  2  22  ? 43.669  2.096   23.784   1.00 130.04 ? 26   TRP   B HB3  1 
ATOM   9393  H  HD1  . TRP   B  2  22  ? 43.453  4.620   24.199   1.00 137.19 ? 26   TRP   B HD1  1 
ATOM   9394  H  HE1  . TRP   B  2  22  ? 43.933  6.630   22.965   1.00 135.73 ? 26   TRP   B HE1  1 
ATOM   9395  H  HE3  . TRP   B  2  22  ? 45.873  2.664   20.413   1.00 129.16 ? 26   TRP   B HE3  1 
ATOM   9396  H  HZ2  . TRP   B  2  22  ? 45.223  7.306   20.608   1.00 137.13 ? 26   TRP   B HZ2  1 
ATOM   9397  H  HZ3  . TRP   B  2  22  ? 46.680  4.052   18.748   1.00 134.67 ? 26   TRP   B HZ3  1 
ATOM   9398  H  HH2  . TRP   B  2  22  ? 46.356  6.340   18.848   1.00 138.45 ? 26   TRP   B HH2  1 
ATOM   9399  N  N    . CYS   B  2  23  ? 46.739  3.372   24.951   1.00 137.32 ? 27   CYS   B N    1 
ATOM   9400  C  CA   . CYS   B  2  23  ? 47.189  4.100   26.136   1.00 146.58 ? 27   CYS   B CA   1 
ATOM   9401  C  C    . CYS   B  2  23  ? 46.713  5.548   26.091   1.00 132.40 ? 27   CYS   B C    1 
ATOM   9402  O  O    . CYS   B  2  23  ? 46.485  6.103   25.014   1.00 132.92 ? 27   CYS   B O    1 
ATOM   9403  C  CB   . CYS   B  2  23  ? 48.717  4.067   26.245   1.00 160.21 ? 27   CYS   B CB   1 
ATOM   9404  S  SG   . CYS   B  2  23  ? 49.391  4.844   27.716   1.00 159.85 ? 27   CYS   B SG   1 
ATOM   9405  H  H    . CYS   B  2  23  ? 46.987  3.738   24.213   1.00 164.82 ? 27   CYS   B H    1 
ATOM   9406  H  HA   . CYS   B  2  23  ? 46.807  3.689   26.927   1.00 175.93 ? 27   CYS   B HA   1 
ATOM   9407  H  HB2  . CYS   B  2  23  ? 49.004  3.141   26.247   1.00 192.29 ? 27   CYS   B HB2  1 
ATOM   9408  H  HB3  . CYS   B  2  23  ? 49.089  4.528   25.476   1.00 192.29 ? 27   CYS   B HB3  1 
ATOM   9409  N  N    . ALA   B  2  24  ? 46.580  6.172   27.271   1.00 118.40 ? 28   ALA   B N    1 
ATOM   9410  C  CA   . ALA   B  2  24  ? 46.052  7.530   27.375   1.00 119.96 ? 28   ALA   B CA   1 
ATOM   9411  C  C    . ALA   B  2  24  ? 46.952  8.439   28.210   1.00 125.95 ? 28   ALA   B C    1 
ATOM   9412  O  O    . ALA   B  2  24  ? 47.357  8.088   29.321   1.00 128.76 ? 28   ALA   B O    1 
ATOM   9413  C  CB   . ALA   B  2  24  ? 44.633  7.511   27.964   1.00 117.86 ? 28   ALA   B CB   1 
ATOM   9414  H  H    . ALA   B  2  24  ? 46.793  5.822   28.027   1.00 142.11 ? 28   ALA   B H    1 
ATOM   9415  H  HA   . ALA   B  2  24  ? 46.039  7.912   26.483   1.00 143.99 ? 28   ALA   B HA   1 
ATOM   9416  H  HB1  . ALA   B  2  24  ? 44.320  8.424   28.063   1.00 141.47 ? 28   ALA   B HB1  1 
ATOM   9417  H  HB2  . ALA   B  2  24  ? 44.048  7.025   27.363   1.00 141.47 ? 28   ALA   B HB2  1 
ATOM   9418  H  HB3  . ALA   B  2  24  ? 44.656  7.074   28.830   1.00 141.47 ? 28   ALA   B HB3  1 
ATOM   9419  N  N    . GLN   B  2  25  ? 47.247  9.612   27.637   1.00 129.32 ? 29   GLN   B N    1 
ATOM   9420  C  CA   . GLN   B  2  25  ? 47.854  10.829  28.201   1.00 136.01 ? 29   GLN   B CA   1 
ATOM   9421  C  C    . GLN   B  2  25  ? 49.356  10.760  28.502   1.00 139.33 ? 29   GLN   B C    1 
ATOM   9422  O  O    . GLN   B  2  25  ? 49.896  11.728  29.058   1.00 142.53 ? 29   GLN   B O    1 
ATOM   9423  C  CB   . GLN   B  2  25  ? 47.132  11.308  29.472   1.00 139.16 ? 29   GLN   B CB   1 
ATOM   9424  C  CG   . GLN   B  2  25  ? 47.507  12.742  29.942   1.00 144.57 ? 29   GLN   B CG   1 
ATOM   9425  C  CD   . GLN   B  2  25  ? 47.610  13.766  28.804   1.00 142.90 ? 29   GLN   B CD   1 
ATOM   9426  O  OE1  . GLN   B  2  25  ? 48.314  13.556  27.816   1.00 139.75 ? 29   GLN   B OE1  1 
ATOM   9427  N  NE2  . GLN   B  2  25  ? 46.917  14.885  28.956   1.00 144.37 ? 29   GLN   B NE2  1 
ATOM   9428  H  H    . GLN   B  2  25  ? 47.081  9.747   26.804   1.00 155.22 ? 29   GLN   B H    1 
ATOM   9429  H  HA   . GLN   B  2  25  ? 47.757  11.492  27.500   1.00 163.25 ? 29   GLN   B HA   1 
ATOM   9430  H  HB2  . GLN   B  2  25  ? 46.177  11.298  29.304   1.00 167.02 ? 29   GLN   B HB2  1 
ATOM   9431  H  HB3  . GLN   B  2  25  ? 47.348  10.700  30.196   1.00 167.02 ? 29   GLN   B HB3  1 
ATOM   9432  H  HG2  . GLN   B  2  25  ? 46.827  13.055  30.559   1.00 173.53 ? 29   GLN   B HG2  1 
ATOM   9433  H  HG3  . GLN   B  2  25  ? 48.368  12.709  30.387   1.00 173.53 ? 29   GLN   B HG3  1 
ATOM   9434  H  HE21 . GLN   B  2  25  ? 46.444  15.006  29.664   1.00 173.29 ? 29   GLN   B HE21 1 
ATOM   9435  H  HE22 . GLN   B  2  25  ? 46.941  15.492  28.347   1.00 173.29 ? 29   GLN   B HE22 1 
ATOM   9436  N  N    . GLU   B  2  26  ? 50.064  9.687   28.138   1.00 138.61 ? 30   GLU   B N    1 
ATOM   9437  C  CA   . GLU   B  2  26  ? 51.513  9.567   28.351   1.00 141.94 ? 30   GLU   B CA   1 
ATOM   9438  C  C    . GLU   B  2  26  ? 52.046  10.257  29.609   1.00 146.58 ? 30   GLU   B C    1 
ATOM   9439  O  O    . GLU   B  2  26  ? 53.026  11.009  29.549   1.00 149.01 ? 30   GLU   B O    1 
ATOM   9440  C  CB   . GLU   B  2  26  ? 52.272  10.103  27.122   1.00 140.26 ? 30   GLU   B CB   1 
ATOM   9441  C  CG   . GLU   B  2  26  ? 52.638  9.021   26.116   1.00 135.64 ? 30   GLU   B CG   1 
ATOM   9442  C  CD   . GLU   B  2  26  ? 53.861  9.368   25.286   1.00 136.40 ? 30   GLU   B CD   1 
ATOM   9443  O  OE1  . GLU   B  2  26  ? 53.726  10.138  24.312   1.00 135.46 ? 30   GLU   B OE1  1 
ATOM   9444  O  OE2  . GLU   B  2  26  ? 54.960  8.870   25.609   1.00 137.67 ? 30   GLU   B OE2  1 
ATOM   9445  H  H    . GLU   B  2  26  ? 49.722  8.996   27.756   1.00 166.37 ? 30   GLU   B H    1 
ATOM   9446  H  HA   . GLU   B  2  26  ? 51.683  8.620   28.478   1.00 170.36 ? 30   GLU   B HA   1 
ATOM   9447  H  HB2  . GLU   B  2  26  ? 51.714  10.754  26.669   1.00 168.35 ? 30   GLU   B HB2  1 
ATOM   9448  H  HB3  . GLU   B  2  26  ? 53.094  10.522  27.421   1.00 168.35 ? 30   GLU   B HB3  1 
ATOM   9449  H  HG2  . GLU   B  2  26  ? 52.825  8.197   26.593   1.00 162.80 ? 30   GLU   B HG2  1 
ATOM   9450  H  HG3  . GLU   B  2  26  ? 51.892  8.890   25.509   1.00 162.80 ? 30   GLU   B HG3  1 
ATOM   9451  N  N    . ASN   B  2  27  ? 51.449  9.972   30.762   1.00 147.27 ? 31   ASN   B N    1 
ATOM   9452  C  CA   . ASN   B  2  27  ? 51.879  10.565  32.032   1.00 155.60 ? 31   ASN   B CA   1 
ATOM   9453  C  C    . ASN   B  2  27  ? 53.360  10.306  32.306   1.00 161.53 ? 31   ASN   B C    1 
ATOM   9454  O  O    . ASN   B  2  27  ? 54.035  11.114  32.949   1.00 168.95 ? 31   ASN   B O    1 
ATOM   9455  C  CB   . ASN   B  2  27  ? 51.019  10.010  33.175   1.00 152.20 ? 31   ASN   B CB   1 
ATOM   9456  C  CG   . ASN   B  2  27  ? 51.411  10.560  34.538   1.00 160.02 ? 31   ASN   B CG   1 
ATOM   9457  O  OD1  . ASN   B  2  27  ? 52.570  10.492  34.945   1.00 164.08 ? 31   ASN   B OD1  1 
ATOM   9458  N  ND2  . ASN   B  2  27  ? 50.432  11.100  35.256   1.00 161.00 ? 31   ASN   B ND2  1 
ATOM   9459  H  H    . ASN   B  2  27  ? 50.784  9.432   30.841   1.00 176.77 ? 31   ASN   B H    1 
ATOM   9460  H  HA   . ASN   B  2  27  ? 51.763  11.527  31.990   1.00 186.76 ? 31   ASN   B HA   1 
ATOM   9461  H  HB2  . ASN   B  2  27  ? 50.092  10.245  33.014   1.00 182.67 ? 31   ASN   B HB2  1 
ATOM   9462  H  HB3  . ASN   B  2  27  ? 51.117  9.046   33.203   1.00 182.67 ? 31   ASN   B HB3  1 
ATOM   9463  H  HD21 . ASN   B  2  27  ? 50.599  11.426  36.035   1.00 193.24 ? 31   ASN   B HD21 1 
ATOM   9464  H  HD22 . ASN   B  2  27  ? 49.631  11.124  34.943   1.00 193.24 ? 31   ASN   B HD22 1 
ATOM   9465  N  N    . GLY   B  2  35  ? 51.954  9.342   19.548   1.00 145.64 ? 39   GLY   B N    1 
ATOM   9466  C  CA   . GLY   B  2  35  ? 52.754  8.696   18.526   1.00 143.09 ? 39   GLY   B CA   1 
ATOM   9467  C  C    . GLY   B  2  35  ? 52.289  7.287   18.214   1.00 138.21 ? 39   GLY   B C    1 
ATOM   9468  O  O    . GLY   B  2  35  ? 51.491  7.077   17.300   1.00 137.34 ? 39   GLY   B O    1 
ATOM   9469  H  HA2  . GLY   B  2  35  ? 52.710  9.218   17.709   1.00 171.75 ? 39   GLY   B HA2  1 
ATOM   9470  H  HA3  . GLY   B  2  35  ? 53.676  8.652   18.823   1.00 171.75 ? 39   GLY   B HA3  1 
ATOM   9471  N  N    . GLU   B  2  36  ? 52.787  6.313   18.980   1.00 138.92 ? 40   GLU   B N    1 
ATOM   9472  C  CA   . GLU   B  2  36  ? 52.462  4.902   18.775   1.00 135.55 ? 40   GLU   B CA   1 
ATOM   9473  C  C    . GLU   B  2  36  ? 52.043  4.299   20.120   1.00 131.34 ? 40   GLU   B C    1 
ATOM   9474  O  O    . GLU   B  2  36  ? 52.781  3.535   20.745   1.00 127.62 ? 40   GLU   B O    1 
ATOM   9475  C  CB   . GLU   B  2  36  ? 53.645  4.151   18.155   1.00 142.83 ? 40   GLU   B CB   1 
ATOM   9476  C  CG   . GLU   B  2  36  ? 53.286  2.833   17.467   1.00 143.68 ? 40   GLU   B CG   1 
ATOM   9477  C  CD   . GLU   B  2  36  ? 52.213  2.985   16.400   1.00 141.53 ? 40   GLU   B CD   1 
ATOM   9478  O  OE1  . GLU   B  2  36  ? 51.041  3.233   16.756   1.00 138.23 ? 40   GLU   B OE1  1 
ATOM   9479  O  OE2  . GLU   B  2  36  ? 52.541  2.855   15.202   1.00 141.54 ? 40   GLU   B OE2  1 
ATOM   9480  H  H    . GLU   B  2  36  ? 53.325  6.449   19.637   1.00 166.73 ? 40   GLU   B H    1 
ATOM   9481  H  HA   . GLU   B  2  36  ? 51.708  4.831   18.168   1.00 162.69 ? 40   GLU   B HA   1 
ATOM   9482  H  HB2  . GLU   B  2  36  ? 54.057  4.724   17.490   1.00 171.44 ? 40   GLU   B HB2  1 
ATOM   9483  H  HB3  . GLU   B  2  36  ? 54.282  3.948   18.858   1.00 171.44 ? 40   GLU   B HB3  1 
ATOM   9484  H  HG2  . GLU   B  2  36  ? 54.080  2.474   17.042   1.00 172.46 ? 40   GLU   B HG2  1 
ATOM   9485  H  HG3  . GLU   B  2  36  ? 52.956  2.211   18.134   1.00 172.46 ? 40   GLU   B HG3  1 
ATOM   9486  N  N    . ARG   B  2  37  ? 50.835  4.653   20.559   1.00 127.14 ? 41   ARG   B N    1 
ATOM   9487  C  CA   . ARG   B  2  37  ? 50.275  4.146   21.804   1.00 128.15 ? 41   ARG   B CA   1 
ATOM   9488  C  C    . ARG   B  2  37  ? 49.675  2.755   21.656   1.00 130.00 ? 41   ARG   B C    1 
ATOM   9489  O  O    . ARG   B  2  37  ? 49.295  2.150   22.665   1.00 127.07 ? 41   ARG   B O    1 
ATOM   9490  C  CB   . ARG   B  2  37  ? 49.193  5.102   22.311   1.00 123.20 ? 41   ARG   B CB   1 
ATOM   9491  C  CG   . ARG   B  2  37  ? 49.628  6.554   22.393   1.00 120.37 ? 41   ARG   B CG   1 
ATOM   9492  C  CD   . ARG   B  2  37  ? 48.435  7.463   22.625   1.00 115.76 ? 41   ARG   B CD   1 
ATOM   9493  N  NE   . ARG   B  2  37  ? 48.620  8.323   23.790   1.00 115.42 ? 41   ARG   B NE   1 
ATOM   9494  C  CZ   . ARG   B  2  37  ? 49.181  9.528   23.757   1.00 117.71 ? 41   ARG   B CZ   1 
ATOM   9495  N  NH1  . ARG   B  2  37  ? 49.621  10.036  22.612   1.00 117.28 ? 41   ARG   B NH1  1 
ATOM   9496  N  NH2  . ARG   B  2  37  ? 49.303  10.230  24.875   1.00 122.51 ? 41   ARG   B NH2  1 
ATOM   9497  H  H    . ARG   B  2  37  ? 50.312  5.196   20.144   1.00 152.60 ? 41   ARG   B H    1 
ATOM   9498  H  HA   . ARG   B  2  37  ? 50.981  4.101   22.467   1.00 153.82 ? 41   ARG   B HA   1 
ATOM   9499  H  HB2  . ARG   B  2  37  ? 48.434  5.057   21.710   1.00 147.88 ? 41   ARG   B HB2  1 
ATOM   9500  H  HB3  . ARG   B  2  37  ? 48.929  4.825   23.202   1.00 147.88 ? 41   ARG   B HB3  1 
ATOM   9501  H  HG2  . ARG   B  2  37  ? 50.248  6.665   23.130   1.00 144.48 ? 41   ARG   B HG2  1 
ATOM   9502  H  HG3  . ARG   B  2  37  ? 50.054  6.812   21.560   1.00 144.48 ? 41   ARG   B HG3  1 
ATOM   9503  H  HD2  . ARG   B  2  37  ? 48.309  8.029   21.848   1.00 138.95 ? 41   ARG   B HD2  1 
ATOM   9504  H  HD3  . ARG   B  2  37  ? 47.644  6.920   22.772   1.00 138.95 ? 41   ARG   B HD3  1 
ATOM   9505  H  HE   . ARG   B  2  37  ? 48.348  8.030   24.551   1.00 138.55 ? 41   ARG   B HE   1 
ATOM   9506  H  HH11 . ARG   B  2  37  ? 49.544  9.585   21.884   1.00 140.77 ? 41   ARG   B HH11 1 
ATOM   9507  H  HH12 . ARG   B  2  37  ? 49.982  10.816  22.598   1.00 140.77 ? 41   ARG   B HH12 1 
ATOM   9508  H  HH21 . ARG   B  2  37  ? 49.019  9.905   25.619   1.00 147.05 ? 41   ARG   B HH21 1 
ATOM   9509  H  HH22 . ARG   B  2  37  ? 49.665  11.009  24.856   1.00 147.05 ? 41   ARG   B HH22 1 
ATOM   9510  N  N    . CYS   B  2  38  ? 49.583  2.244   20.433   1.00 134.18 ? 42   CYS   B N    1 
ATOM   9511  C  CA   . CYS   B  2  38  ? 48.899  0.990   20.135   1.00 137.51 ? 42   CYS   B CA   1 
ATOM   9512  C  C    . CYS   B  2  38  ? 49.913  -0.146  20.075   1.00 149.27 ? 42   CYS   B C    1 
ATOM   9513  O  O    . CYS   B  2  38  ? 50.641  -0.281  19.091   1.00 158.90 ? 42   CYS   B O    1 
ATOM   9514  C  CB   . CYS   B  2  38  ? 48.151  1.115   18.813   1.00 132.64 ? 42   CYS   B CB   1 
ATOM   9515  S  SG   . CYS   B  2  38  ? 47.366  -0.397  18.266   1.00 125.42 ? 42   CYS   B SG   1 
ATOM   9516  H  H    . CYS   B  2  38  ? 49.921  2.618   19.736   1.00 161.05 ? 42   CYS   B H    1 
ATOM   9517  H  HA   . CYS   B  2  38  ? 48.279  0.793   20.855   1.00 165.04 ? 42   CYS   B HA   1 
ATOM   9518  H  HB2  . CYS   B  2  38  ? 47.459  1.787   18.912   1.00 159.21 ? 42   CYS   B HB2  1 
ATOM   9519  H  HB3  . CYS   B  2  38  ? 48.780  1.385   18.126   1.00 159.21 ? 42   CYS   B HB3  1 
ATOM   9520  N  N    . ASP   B  2  39  ? 49.939  -0.977  21.119   1.00 154.55 ? 43   ASP   B N    1 
ATOM   9521  C  CA   . ASP   B  2  39  ? 50.808  -2.150  21.177   1.00 157.69 ? 43   ASP   B CA   1 
ATOM   9522  C  C    . ASP   B  2  39  ? 50.234  -3.119  22.208   1.00 154.38 ? 43   ASP   B C    1 
ATOM   9523  O  O    . ASP   B  2  39  ? 49.207  -2.848  22.837   1.00 156.15 ? 43   ASP   B O    1 
ATOM   9524  C  CB   . ASP   B  2  39  ? 52.252  -1.769  21.525   1.00 169.71 ? 43   ASP   B CB   1 
ATOM   9525  C  CG   . ASP   B  2  39  ? 53.003  -1.156  20.356   1.00 183.57 ? 43   ASP   B CG   1 
ATOM   9526  O  OD1  . ASP   B  2  39  ? 52.679  -1.482  19.195   1.00 187.68 ? 43   ASP   B OD1  1 
ATOM   9527  O  OD2  . ASP   B  2  39  ? 53.933  -0.359  20.602   1.00 191.90 ? 43   ASP   B OD2  1 
ATOM   9528  H  H    . ASP   B  2  39  ? 49.452  -0.879  21.821   1.00 185.50 ? 43   ASP   B H    1 
ATOM   9529  H  HA   . ASP   B  2  39  ? 50.806  -2.577  20.306   1.00 189.26 ? 43   ASP   B HA   1 
ATOM   9530  H  HB2  . ASP   B  2  39  ? 52.242  -1.120  22.247   1.00 203.69 ? 43   ASP   B HB2  1 
ATOM   9531  H  HB3  . ASP   B  2  39  ? 52.730  -2.566  21.803   1.00 203.69 ? 43   ASP   B HB3  1 
ATOM   9532  N  N    . THR   B  2  40  ? 50.917  -4.260  22.384   1.00 147.68 ? 44   THR   B N    1 
ATOM   9533  C  CA   . THR   B  2  40  ? 50.495  -5.295  23.325   1.00 145.55 ? 44   THR   B CA   1 
ATOM   9534  C  C    . THR   B  2  40  ? 50.293  -4.702  24.716   1.00 142.59 ? 44   THR   B C    1 
ATOM   9535  O  O    . THR   B  2  40  ? 50.993  -3.751  25.087   1.00 138.91 ? 44   THR   B O    1 
ATOM   9536  C  CB   . THR   B  2  40  ? 51.522  -6.431  23.407   1.00 146.49 ? 44   THR   B CB   1 
ATOM   9537  O  OG1  . THR   B  2  40  ? 52.717  -5.952  24.037   1.00 150.60 ? 44   THR   B OG1  1 
ATOM   9538  C  CG2  . THR   B  2  40  ? 51.860  -6.973  22.024   1.00 143.68 ? 44   THR   B CG2  1 
ATOM   9539  H  H    . THR   B  2  40  ? 51.640  -4.457  21.961   1.00 177.26 ? 44   THR   B H    1 
ATOM   9540  H  HA   . THR   B  2  40  ? 49.653  -5.660  23.010   1.00 174.69 ? 44   THR   B HA   1 
ATOM   9541  H  HB   . THR   B  2  40  ? 51.146  -7.158  23.927   1.00 175.82 ? 44   THR   B HB   1 
ATOM   9542  H  HG1  . THR   B  2  40  ? 53.129  -6.591  24.395   1.00 180.75 ? 44   THR   B HG1  1 
ATOM   9543  H  HG21 . THR   B  2  40  ? 52.397  -7.777  22.105   1.00 172.46 ? 44   THR   B HG21 1 
ATOM   9544  H  HG22 . THR   B  2  40  ? 51.045  -7.186  21.542   1.00 172.46 ? 44   THR   B HG22 1 
ATOM   9545  H  HG23 . THR   B  2  40  ? 52.359  -6.311  21.521   1.00 172.46 ? 44   THR   B HG23 1 
ATOM   9546  N  N    . PRO   B  2  41  ? 49.368  -5.237  25.522   1.00 139.06 ? 45   PRO   B N    1 
ATOM   9547  C  CA   . PRO   B  2  41  ? 49.120  -4.620  26.838   1.00 138.87 ? 45   PRO   B CA   1 
ATOM   9548  C  C    . PRO   B  2  41  ? 50.323  -4.638  27.768   1.00 141.27 ? 45   PRO   B C    1 
ATOM   9549  O  O    . PRO   B  2  41  ? 50.521  -3.676  28.520   1.00 145.91 ? 45   PRO   B O    1 
ATOM   9550  C  CB   . PRO   B  2  41  ? 47.948  -5.442  27.403   1.00 137.45 ? 45   PRO   B CB   1 
ATOM   9551  C  CG   . PRO   B  2  41  ? 47.891  -6.687  26.589   1.00 136.84 ? 45   PRO   B CG   1 
ATOM   9552  C  CD   . PRO   B  2  41  ? 48.430  -6.338  25.238   1.00 135.96 ? 45   PRO   B CD   1 
ATOM   9553  H  HA   . PRO   B  2  41  ? 48.837  -3.702  26.708   1.00 166.69 ? 45   PRO   B HA   1 
ATOM   9554  H  HB2  . PRO   B  2  41  ? 48.115  -5.649  28.335   1.00 164.98 ? 45   PRO   B HB2  1 
ATOM   9555  H  HB3  . PRO   B  2  41  ? 47.124  -4.938  27.317   1.00 164.98 ? 45   PRO   B HB3  1 
ATOM   9556  H  HG2  . PRO   B  2  41  ? 48.436  -7.373  27.006   1.00 164.24 ? 45   PRO   B HG2  1 
ATOM   9557  H  HG3  . PRO   B  2  41  ? 46.972  -6.989  26.522   1.00 164.24 ? 45   PRO   B HG3  1 
ATOM   9558  H  HD2  . PRO   B  2  41  ? 48.894  -7.094  24.845   1.00 163.19 ? 45   PRO   B HD2  1 
ATOM   9559  H  HD3  . PRO   B  2  41  ? 47.719  -6.042  24.649   1.00 163.19 ? 45   PRO   B HD3  1 
ATOM   9560  N  N    . ALA   B  2  42  ? 51.133  -5.700  27.751   1.00 139.98 ? 46   ALA   B N    1 
ATOM   9561  C  CA   . ALA   B  2  42  ? 52.299  -5.736  28.628   1.00 145.08 ? 46   ALA   B CA   1 
ATOM   9562  C  C    . ALA   B  2  42  ? 53.271  -4.610  28.297   1.00 148.43 ? 46   ALA   B C    1 
ATOM   9563  O  O    . ALA   B  2  42  ? 53.860  -4.002  29.200   1.00 154.54 ? 46   ALA   B O    1 
ATOM   9564  C  CB   . ALA   B  2  42  ? 52.999  -7.092  28.528   1.00 145.18 ? 46   ALA   B CB   1 
ATOM   9565  H  H    . ALA   B  2  42  ? 51.030  -6.394  27.253   1.00 168.01 ? 46   ALA   B H    1 
ATOM   9566  H  HA   . ALA   B  2  42  ? 52.001  -5.622  29.544   1.00 174.13 ? 46   ALA   B HA   1 
ATOM   9567  H  HB1  . ALA   B  2  42  ? 53.776  -7.089  29.109   1.00 174.26 ? 46   ALA   B HB1  1 
ATOM   9568  H  HB2  . ALA   B  2  42  ? 52.382  -7.787  28.805   1.00 174.26 ? 46   ALA   B HB2  1 
ATOM   9569  H  HB3  . ALA   B  2  42  ? 53.273  -7.239  27.609   1.00 174.26 ? 46   ALA   B HB3  1 
ATOM   9570  N  N    . ASN   B  2  43  ? 53.450  -4.312  27.008   1.00 145.86 ? 47   ASN   B N    1 
ATOM   9571  C  CA   . ASN   B  2  43  ? 54.380  -3.257  26.619   1.00 149.00 ? 47   ASN   B CA   1 
ATOM   9572  C  C    . ASN   B  2  43  ? 53.926  -1.899  27.142   1.00 152.86 ? 47   ASN   B C    1 
ATOM   9573  O  O    . ASN   B  2  43  ? 54.756  -1.058  27.508   1.00 158.94 ? 47   ASN   B O    1 
ATOM   9574  C  CB   . ASN   B  2  43  ? 54.529  -3.213  25.097   1.00 144.89 ? 47   ASN   B CB   1 
ATOM   9575  C  CG   . ASN   B  2  43  ? 55.187  -4.465  24.526   1.00 146.07 ? 47   ASN   B CG   1 
ATOM   9576  O  OD1  . ASN   B  2  43  ? 54.940  -4.830  23.377   1.00 145.39 ? 47   ASN   B OD1  1 
ATOM   9577  N  ND2  . ASN   B  2  43  ? 56.025  -5.123  25.323   1.00 148.42 ? 47   ASN   B ND2  1 
ATOM   9578  H  H    . ASN   B  2  43  ? 53.052  -4.701  26.352   1.00 175.07 ? 47   ASN   B H    1 
ATOM   9579  H  HA   . ASN   B  2  43  ? 55.248  -3.457  27.002   1.00 178.84 ? 47   ASN   B HA   1 
ATOM   9580  H  HB2  . ASN   B  2  43  ? 53.649  -3.130  24.696   1.00 173.90 ? 47   ASN   B HB2  1 
ATOM   9581  H  HB3  . ASN   B  2  43  ? 55.077  -2.451  24.855   1.00 173.90 ? 47   ASN   B HB3  1 
ATOM   9582  H  HD21 . ASN   B  2  43  ? 56.418  -5.834  25.040   1.00 178.15 ? 47   ASN   B HD21 1 
ATOM   9583  H  HD22 . ASN   B  2  43  ? 56.174  -4.838  26.121   1.00 178.15 ? 47   ASN   B HD22 1 
ATOM   9584  N  N    . LEU   B  2  44  ? 52.613  -1.664  27.184   1.00 149.45 ? 48   LEU   B N    1 
ATOM   9585  C  CA   . LEU   B  2  44  ? 52.118  -0.369  27.639   1.00 152.99 ? 48   LEU   B CA   1 
ATOM   9586  C  C    . LEU   B  2  44  ? 52.379  -0.174  29.128   1.00 161.82 ? 48   LEU   B C    1 
ATOM   9587  O  O    . LEU   B  2  44  ? 52.696  0.937   29.568   1.00 167.49 ? 48   LEU   B O    1 
ATOM   9588  C  CB   . LEU   B  2  44  ? 50.627  -0.240  27.329   1.00 146.94 ? 48   LEU   B CB   1 
ATOM   9589  C  CG   . LEU   B  2  44  ? 50.186  -0.652  25.920   1.00 143.19 ? 48   LEU   B CG   1 
ATOM   9590  C  CD1  . LEU   B  2  44  ? 48.788  -0.124  25.632   1.00 141.27 ? 48   LEU   B CD1  1 
ATOM   9591  C  CD2  . LEU   B  2  44  ? 51.166  -0.182  24.850   1.00 144.87 ? 48   LEU   B CD2  1 
ATOM   9592  H  H    . LEU   B  2  44  ? 52.003  -2.226  26.960   1.00 179.38 ? 48   LEU   B H    1 
ATOM   9593  H  HA   . LEU   B  2  44  ? 52.584  0.333   27.159   1.00 183.63 ? 48   LEU   B HA   1 
ATOM   9594  H  HB2  . LEU   B  2  44  ? 50.140  -0.797  27.955   1.00 176.36 ? 48   LEU   B HB2  1 
ATOM   9595  H  HB3  . LEU   B  2  44  ? 50.375  0.690   27.446   1.00 176.36 ? 48   LEU   B HB3  1 
ATOM   9596  H  HG   . LEU   B  2  44  ? 50.170  -1.621  25.881   1.00 171.87 ? 48   LEU   B HG   1 
ATOM   9597  H  HD11 . LEU   B  2  44  ? 48.532  -0.381  24.733   1.00 169.56 ? 48   LEU   B HD11 1 
ATOM   9598  H  HD12 . LEU   B  2  44  ? 48.168  -0.505  26.274   1.00 169.56 ? 48   LEU   B HD12 1 
ATOM   9599  H  HD13 . LEU   B  2  44  ? 48.793  0.843   25.711   1.00 169.56 ? 48   LEU   B HD13 1 
ATOM   9600  H  HD21 . LEU   B  2  44  ? 50.824  -0.433  23.977   1.00 173.88 ? 48   LEU   B HD21 1 
ATOM   9601  H  HD22 . LEU   B  2  44  ? 51.255  0.782   24.905   1.00 173.88 ? 48   LEU   B HD22 1 
ATOM   9602  H  HD23 . LEU   B  2  44  ? 52.026  -0.604  25.002   1.00 173.88 ? 48   LEU   B HD23 1 
ATOM   9603  N  N    . LEU   B  2  45  ? 52.250  -1.242  29.920   1.00 162.07 ? 49   LEU   B N    1 
ATOM   9604  C  CA   . LEU   B  2  45  ? 52.608  -1.157  31.332   1.00 166.74 ? 49   LEU   B CA   1 
ATOM   9605  C  C    . LEU   B  2  45  ? 54.104  -0.921  31.501   1.00 178.31 ? 49   LEU   B C    1 
ATOM   9606  O  O    . LEU   B  2  45  ? 54.527  -0.199  32.411   1.00 196.37 ? 49   LEU   B O    1 
ATOM   9607  C  CB   . LEU   B  2  45  ? 52.182  -2.431  32.063   1.00 160.71 ? 49   LEU   B CB   1 
ATOM   9608  C  CG   . LEU   B  2  45  ? 50.685  -2.616  32.331   1.00 152.79 ? 49   LEU   B CG   1 
ATOM   9609  C  CD1  . LEU   B  2  45  ? 50.393  -4.008  32.867   1.00 150.18 ? 49   LEU   B CD1  1 
ATOM   9610  C  CD2  . LEU   B  2  45  ? 50.182  -1.570  33.310   1.00 154.96 ? 49   LEU   B CD2  1 
ATOM   9611  H  H    . LEU   B  2  45  ? 51.962  -2.012  29.667   1.00 194.52 ? 49   LEU   B H    1 
ATOM   9612  H  HA   . LEU   B  2  45  ? 52.134  -0.411  31.731   1.00 200.12 ? 49   LEU   B HA   1 
ATOM   9613  H  HB2  . LEU   B  2  45  ? 52.469  -3.190  31.531   1.00 192.89 ? 49   LEU   B HB2  1 
ATOM   9614  H  HB3  . LEU   B  2  45  ? 52.627  -2.443  32.925   1.00 192.89 ? 49   LEU   B HB3  1 
ATOM   9615  H  HG   . LEU   B  2  45  ? 50.211  -2.507  31.492   1.00 183.39 ? 49   LEU   B HG   1 
ATOM   9616  H  HD11 . LEU   B  2  45  ? 49.442  -4.087  33.040   1.00 180.25 ? 49   LEU   B HD11 1 
ATOM   9617  H  HD12 . LEU   B  2  45  ? 50.664  -4.664  32.206   1.00 180.25 ? 49   LEU   B HD12 1 
ATOM   9618  H  HD13 . LEU   B  2  45  ? 50.891  -4.142  33.689   1.00 180.25 ? 49   LEU   B HD13 1 
ATOM   9619  H  HD21 . LEU   B  2  45  ? 49.218  -1.650  33.389   1.00 185.99 ? 49   LEU   B HD21 1 
ATOM   9620  H  HD22 . LEU   B  2  45  ? 50.598  -1.720  34.174   1.00 185.99 ? 49   LEU   B HD22 1 
ATOM   9621  H  HD23 . LEU   B  2  45  ? 50.415  -0.689  32.979   1.00 185.99 ? 49   LEU   B HD23 1 
ATOM   9622  N  N    . ALA   B  2  46  ? 54.920  -1.522  30.630   1.00 170.25 ? 50   ALA   B N    1 
ATOM   9623  C  CA   . ALA   B  2  46  ? 56.361  -1.314  30.702   1.00 176.19 ? 50   ALA   B CA   1 
ATOM   9624  C  C    . ALA   B  2  46  ? 56.735  0.132   30.407   1.00 179.84 ? 50   ALA   B C    1 
ATOM   9625  O  O    . ALA   B  2  46  ? 57.721  0.639   30.955   1.00 185.82 ? 50   ALA   B O    1 
ATOM   9626  C  CB   . ALA   B  2  46  ? 57.073  -2.250  29.726   1.00 175.87 ? 50   ALA   B CB   1 
ATOM   9627  H  H    . ALA   B  2  46  ? 54.665  -2.046  29.998   1.00 204.33 ? 50   ALA   B H    1 
ATOM   9628  H  HA   . ALA   B  2  46  ? 56.660  -1.526  31.600   1.00 211.46 ? 50   ALA   B HA   1 
ATOM   9629  H  HB1  . ALA   B  2  46  ? 58.029  -2.095  29.781   1.00 211.09 ? 50   ALA   B HB1  1 
ATOM   9630  H  HB2  . ALA   B  2  46  ? 56.873  -3.168  29.966   1.00 211.09 ? 50   ALA   B HB2  1 
ATOM   9631  H  HB3  . ALA   B  2  46  ? 56.760  -2.067  28.827   1.00 211.09 ? 50   ALA   B HB3  1 
ATOM   9632  N  N    . LYS   B  2  47  ? 55.968  0.808   29.554   1.00 176.74 ? 51   LYS   B N    1 
ATOM   9633  C  CA   . LYS   B  2  47  ? 56.262  2.174   29.147   1.00 181.73 ? 51   LYS   B CA   1 
ATOM   9634  C  C    . LYS   B  2  47  ? 55.444  3.209   29.911   1.00 175.97 ? 51   LYS   B C    1 
ATOM   9635  O  O    . LYS   B  2  47  ? 55.391  4.370   29.494   1.00 175.49 ? 51   LYS   B O    1 
ATOM   9636  C  CB   . LYS   B  2  47  ? 56.038  2.324   27.641   1.00 181.17 ? 51   LYS   B CB   1 
ATOM   9637  C  CG   . LYS   B  2  47  ? 56.945  1.427   26.817   1.00 175.04 ? 51   LYS   B CG   1 
ATOM   9638  C  CD   . LYS   B  2  47  ? 56.737  1.622   25.329   1.00 160.73 ? 51   LYS   B CD   1 
ATOM   9639  C  CE   . LYS   B  2  47  ? 57.667  0.724   24.532   1.00 152.38 ? 51   LYS   B CE   1 
ATOM   9640  N  NZ   . LYS   B  2  47  ? 57.535  0.942   23.068   1.00 143.52 ? 51   LYS   B NZ   1 
ATOM   9641  H  H    . LYS   B  2  47  ? 55.257  0.487   29.191   1.00 212.13 ? 51   LYS   B H    1 
ATOM   9642  H  HA   . LYS   B  2  47  ? 57.196  2.357   29.329   1.00 218.12 ? 51   LYS   B HA   1 
ATOM   9643  H  HB2  . LYS   B  2  47  ? 55.119  2.093   27.435   1.00 217.44 ? 51   LYS   B HB2  1 
ATOM   9644  H  HB3  . LYS   B  2  47  ? 56.214  3.243   27.387   1.00 217.44 ? 51   LYS   B HB3  1 
ATOM   9645  H  HG2  . LYS   B  2  47  ? 57.870  1.632   27.023   1.00 210.09 ? 51   LYS   B HG2  1 
ATOM   9646  H  HG3  . LYS   B  2  47  ? 56.755  0.500   27.030   1.00 210.09 ? 51   LYS   B HG3  1 
ATOM   9647  H  HD2  . LYS   B  2  47  ? 55.822  1.400   25.098   1.00 192.92 ? 51   LYS   B HD2  1 
ATOM   9648  H  HD3  . LYS   B  2  47  ? 56.924  2.544   25.094   1.00 192.92 ? 51   LYS   B HD3  1 
ATOM   9649  H  HE2  . LYS   B  2  47  ? 58.585  0.911   24.784   1.00 182.89 ? 51   LYS   B HE2  1 
ATOM   9650  H  HE3  . LYS   B  2  47  ? 57.453  -0.203  24.720   1.00 182.89 ? 51   LYS   B HE3  1 
ATOM   9651  H  HZ1  . LYS   B  2  47  ? 58.110  0.422   22.630   1.00 172.27 ? 51   LYS   B HZ1  1 
ATOM   9652  H  HZ2  . LYS   B  2  47  ? 56.708  0.745   22.804   1.00 172.27 ? 51   LYS   B HZ2  1 
ATOM   9653  H  HZ3  . LYS   B  2  47  ? 57.707  1.793   22.870   1.00 172.27 ? 51   LYS   B HZ3  1 
ATOM   9654  N  N    . GLY   B  2  48  ? 54.801  2.817   31.010   1.00 173.76 ? 52   GLY   B N    1 
ATOM   9655  C  CA   . GLY   B  2  48  ? 54.250  3.764   31.956   1.00 175.37 ? 52   GLY   B CA   1 
ATOM   9656  C  C    . GLY   B  2  48  ? 52.750  3.960   31.917   1.00 175.51 ? 52   GLY   B C    1 
ATOM   9657  O  O    . GLY   B  2  48  ? 52.239  4.809   32.657   1.00 179.39 ? 52   GLY   B O    1 
ATOM   9658  H  H    . GLY   B  2  48  ? 54.674  1.995   31.227   1.00 208.55 ? 52   GLY   B H    1 
ATOM   9659  H  HA2  . GLY   B  2  48  ? 54.480  3.470   32.851   1.00 210.48 ? 52   GLY   B HA2  1 
ATOM   9660  H  HA3  . GLY   B  2  48  ? 54.658  4.629   31.794   1.00 210.48 ? 52   GLY   B HA3  1 
ATOM   9661  N  N    . CYS   B  2  49  ? 52.027  3.213   31.089   1.00 176.18 ? 53   CYS   B N    1 
ATOM   9662  C  CA   . CYS   B  2  49  ? 50.575  3.332   31.035   1.00 167.90 ? 53   CYS   B CA   1 
ATOM   9663  C  C    . CYS   B  2  49  ? 49.964  2.642   32.247   1.00 165.44 ? 53   CYS   B C    1 
ATOM   9664  O  O    . CYS   B  2  49  ? 50.158  1.440   32.445   1.00 160.88 ? 53   CYS   B O    1 
ATOM   9665  C  CB   . CYS   B  2  49  ? 50.051  2.727   29.738   1.00 158.34 ? 53   CYS   B CB   1 
ATOM   9666  S  SG   . CYS   B  2  49  ? 50.799  3.512   28.311   1.00 155.90 ? 53   CYS   B SG   1 
ATOM   9667  H  H    . CYS   B  2  49  ? 52.354  2.630   30.549   1.00 211.45 ? 53   CYS   B H    1 
ATOM   9668  H  HA   . CYS   B  2  49  ? 50.319  4.267   31.059   1.00 201.52 ? 53   CYS   B HA   1 
ATOM   9669  H  HB2  . CYS   B  2  49  ? 50.263  1.781   29.715   1.00 190.05 ? 53   CYS   B HB2  1 
ATOM   9670  H  HB3  . CYS   B  2  49  ? 49.090  2.853   29.689   1.00 190.05 ? 53   CYS   B HB3  1 
ATOM   9671  N  N    . GLN   B  2  50  ? 49.227  3.399   33.054   1.00 166.92 ? 54   GLN   B N    1 
ATOM   9672  C  CA   . GLN   B  2  50  ? 48.667  2.851   34.278   1.00 169.58 ? 54   GLN   B CA   1 
ATOM   9673  C  C    . GLN   B  2  50  ? 47.486  1.934   33.970   1.00 169.05 ? 54   GLN   B C    1 
ATOM   9674  O  O    . GLN   B  2  50  ? 46.830  2.042   32.930   1.00 173.59 ? 54   GLN   B O    1 
ATOM   9675  C  CB   . GLN   B  2  50  ? 48.227  3.974   35.217   1.00 168.35 ? 54   GLN   B CB   1 
ATOM   9676  C  CG   . GLN   B  2  50  ? 49.357  4.900   35.642   1.00 166.93 ? 54   GLN   B CG   1 
ATOM   9677  C  CD   . GLN   B  2  50  ? 48.876  6.053   36.501   1.00 166.53 ? 54   GLN   B CD   1 
ATOM   9678  O  OE1  . GLN   B  2  50  ? 47.761  6.031   37.024   1.00 164.77 ? 54   GLN   B OE1  1 
ATOM   9679  N  NE2  . GLN   B  2  50  ? 49.716  7.071   36.648   1.00 169.35 ? 54   GLN   B NE2  1 
ATOM   9680  H  H    . GLN   B  2  50  ? 49.039  4.227   32.914   1.00 200.34 ? 54   GLN   B H    1 
ATOM   9681  H  HA   . GLN   B  2  50  ? 49.344  2.326   34.733   1.00 203.53 ? 54   GLN   B HA   1 
ATOM   9682  H  HB2  . GLN   B  2  50  ? 47.558  4.512   34.765   1.00 202.05 ? 54   GLN   B HB2  1 
ATOM   9683  H  HB3  . GLN   B  2  50  ? 47.850  3.580   36.019   1.00 202.05 ? 54   GLN   B HB3  1 
ATOM   9684  H  HG2  . GLN   B  2  50  ? 50.005  4.392   36.156   1.00 200.35 ? 54   GLN   B HG2  1 
ATOM   9685  H  HG3  . GLN   B  2  50  ? 49.778  5.270   34.851   1.00 200.35 ? 54   GLN   B HG3  1 
ATOM   9686  H  HE21 . GLN   B  2  50  ? 50.486  7.052   36.266   1.00 203.25 ? 54   GLN   B HE21 1 
ATOM   9687  H  HE22 . GLN   B  2  50  ? 49.490  7.750   37.126   1.00 203.25 ? 54   GLN   B HE22 1 
ATOM   9688  N  N    . LEU   B  2  51  ? 47.216  1.022   34.907   1.00 163.82 ? 55   LEU   B N    1 
ATOM   9689  C  CA   . LEU   B  2  51  ? 46.142  0.053   34.721   1.00 161.72 ? 55   LEU   B CA   1 
ATOM   9690  C  C    . LEU   B  2  51  ? 44.820  0.749   34.421   1.00 162.10 ? 55   LEU   B C    1 
ATOM   9691  O  O    . LEU   B  2  51  ? 44.095  0.364   33.497   1.00 157.72 ? 55   LEU   B O    1 
ATOM   9692  C  CB   . LEU   B  2  51  ? 46.013  -0.825  35.967   1.00 163.08 ? 55   LEU   B CB   1 
ATOM   9693  C  CG   . LEU   B  2  51  ? 47.289  -1.543  36.407   1.00 168.39 ? 55   LEU   B CG   1 
ATOM   9694  C  CD1  . LEU   B  2  51  ? 47.184  -1.960  37.863   1.00 175.18 ? 55   LEU   B CD1  1 
ATOM   9695  C  CD2  . LEU   B  2  51  ? 47.560  -2.747  35.522   1.00 163.79 ? 55   LEU   B CD2  1 
ATOM   9696  H  H    . LEU   B  2  51  ? 47.638  0.945   35.652   1.00 196.63 ? 55   LEU   B H    1 
ATOM   9697  H  HA   . LEU   B  2  51  ? 46.360  -0.518  33.967   1.00 194.10 ? 55   LEU   B HA   1 
ATOM   9698  H  HB2  . LEU   B  2  51  ? 45.728  -0.264  36.705   1.00 195.73 ? 55   LEU   B HB2  1 
ATOM   9699  H  HB3  . LEU   B  2  51  ? 45.345  -1.506  35.790   1.00 195.73 ? 55   LEU   B HB3  1 
ATOM   9700  H  HG   . LEU   B  2  51  ? 48.041  -0.935  36.321   1.00 202.11 ? 55   LEU   B HG   1 
ATOM   9701  H  HD11 . LEU   B  2  51  ? 48.008  -2.398  38.127   1.00 210.26 ? 55   LEU   B HD11 1 
ATOM   9702  H  HD12 . LEU   B  2  51  ? 47.039  -1.171  38.408   1.00 210.26 ? 55   LEU   B HD12 1 
ATOM   9703  H  HD13 . LEU   B  2  51  ? 46.438  -2.572  37.962   1.00 210.26 ? 55   LEU   B HD13 1 
ATOM   9704  H  HD21 . LEU   B  2  51  ? 48.470  -3.050  35.670   1.00 196.59 ? 55   LEU   B HD21 1 
ATOM   9705  H  HD22 . LEU   B  2  51  ? 46.935  -3.453  35.750   1.00 196.59 ? 55   LEU   B HD22 1 
ATOM   9706  H  HD23 . LEU   B  2  51  ? 47.444  -2.489  34.594   1.00 196.59 ? 55   LEU   B HD23 1 
ATOM   9707  N  N    . ASN   B  2  52  ? 44.491  1.783   35.199   1.00 164.73 ? 56   ASN   B N    1 
ATOM   9708  C  CA   . ASN   B  2  52  ? 43.241  2.502   34.976   1.00 162.71 ? 56   ASN   B CA   1 
ATOM   9709  C  C    . ASN   B  2  52  ? 43.201  3.121   33.584   1.00 157.59 ? 56   ASN   B C    1 
ATOM   9710  O  O    . ASN   B  2  52  ? 42.145  3.155   32.942   1.00 152.45 ? 56   ASN   B O    1 
ATOM   9711  C  CB   . ASN   B  2  52  ? 43.059  3.581   36.045   1.00 169.34 ? 56   ASN   B CB   1 
ATOM   9712  C  CG   . ASN   B  2  52  ? 43.196  3.037   37.455   1.00 171.06 ? 56   ASN   B CG   1 
ATOM   9713  O  OD1  . ASN   B  2  52  ? 43.910  2.062   37.689   1.00 168.28 ? 56   ASN   B OD1  1 
ATOM   9714  N  ND2  . ASN   B  2  52  ? 42.511  3.668   38.403   1.00 175.17 ? 56   ASN   B ND2  1 
ATOM   9715  H  H    . ASN   B  2  52  ? 44.967  2.082   35.850   1.00 197.71 ? 56   ASN   B H    1 
ATOM   9716  H  HA   . ASN   B  2  52  ? 42.504  1.876   35.050   1.00 195.29 ? 56   ASN   B HA   1 
ATOM   9717  H  HB2  . ASN   B  2  52  ? 43.734  4.266   35.921   1.00 203.24 ? 56   ASN   B HB2  1 
ATOM   9718  H  HB3  . ASN   B  2  52  ? 42.174  3.967   35.957   1.00 203.24 ? 56   ASN   B HB3  1 
ATOM   9719  H  HD21 . ASN   B  2  52  ? 42.556  3.397   39.218   1.00 210.25 ? 56   ASN   B HD21 1 
ATOM   9720  H  HD22 . ASN   B  2  52  ? 42.023  4.346   38.202   1.00 210.25 ? 56   ASN   B HD22 1 
ATOM   9721  N  N    . PHE   B  2  53  ? 44.346  3.608   33.095   1.00 160.23 ? 57   PHE   B N    1 
ATOM   9722  C  CA   . PHE   B  2  53  ? 44.371  4.308   31.816   1.00 158.74 ? 57   PHE   B CA   1 
ATOM   9723  C  C    . PHE   B  2  53  ? 44.405  3.355   30.628   1.00 153.12 ? 57   PHE   B C    1 
ATOM   9724  O  O    . PHE   B  2  53  ? 43.914  3.704   29.549   1.00 149.29 ? 57   PHE   B O    1 
ATOM   9725  C  CB   . PHE   B  2  53  ? 45.582  5.240   31.742   1.00 162.28 ? 57   PHE   B CB   1 
ATOM   9726  C  CG   . PHE   B  2  53  ? 45.642  6.254   32.848   1.00 167.18 ? 57   PHE   B CG   1 
ATOM   9727  C  CD1  . PHE   B  2  53  ? 44.495  6.650   33.516   1.00 168.54 ? 57   PHE   B CD1  1 
ATOM   9728  C  CD2  . PHE   B  2  53  ? 46.853  6.815   33.216   1.00 170.32 ? 57   PHE   B CD2  1 
ATOM   9729  C  CE1  . PHE   B  2  53  ? 44.556  7.583   34.531   1.00 173.62 ? 57   PHE   B CE1  1 
ATOM   9730  C  CE2  . PHE   B  2  53  ? 46.920  7.749   34.230   1.00 174.68 ? 57   PHE   B CE2  1 
ATOM   9731  C  CZ   . PHE   B  2  53  ? 45.770  8.133   34.888   1.00 176.31 ? 57   PHE   B CZ   1 
ATOM   9732  H  H    . PHE   B  2  53  ? 45.111  3.546   33.483   1.00 192.31 ? 57   PHE   B H    1 
ATOM   9733  H  HA   . PHE   B  2  53  ? 43.564  4.843   31.755   1.00 190.52 ? 57   PHE   B HA   1 
ATOM   9734  H  HB2  . PHE   B  2  53  ? 46.390  4.705   31.789   1.00 194.77 ? 57   PHE   B HB2  1 
ATOM   9735  H  HB3  . PHE   B  2  53  ? 45.552  5.723   30.901   1.00 194.77 ? 57   PHE   B HB3  1 
ATOM   9736  H  HD1  . PHE   B  2  53  ? 43.675  6.282   33.278   1.00 202.28 ? 57   PHE   B HD1  1 
ATOM   9737  H  HD2  . PHE   B  2  53  ? 47.630  6.560   32.775   1.00 204.42 ? 57   PHE   B HD2  1 
ATOM   9738  H  HE1  . PHE   B  2  53  ? 43.780  7.841   34.973   1.00 208.39 ? 57   PHE   B HE1  1 
ATOM   9739  H  HE2  . PHE   B  2  53  ? 47.739  8.118   34.469   1.00 209.65 ? 57   PHE   B HE2  1 
ATOM   9740  H  HZ   . PHE   B  2  53  ? 45.813  8.763   35.571   1.00 211.61 ? 57   PHE   B HZ   1 
ATOM   9741  N  N    . ILE   B  2  54  ? 44.986  2.165   30.794   1.00 151.43 ? 58   ILE   B N    1 
ATOM   9742  C  CA   . ILE   B  2  54  ? 45.079  1.238   29.675   1.00 149.47 ? 58   ILE   B CA   1 
ATOM   9743  C  C    . ILE   B  2  54  ? 43.676  0.866   29.203   1.00 142.39 ? 58   ILE   B C    1 
ATOM   9744  O  O    . ILE   B  2  54  ? 42.728  0.769   29.993   1.00 140.55 ? 58   ILE   B O    1 
ATOM   9745  C  CB   . ILE   B  2  54  ? 45.891  -0.010  30.061   1.00 153.95 ? 58   ILE   B CB   1 
ATOM   9746  C  CG1  . ILE   B  2  54  ? 47.356  0.376   30.286   1.00 158.17 ? 58   ILE   B CG1  1 
ATOM   9747  C  CG2  . ILE   B  2  54  ? 45.790  -1.078  28.975   1.00 152.17 ? 58   ILE   B CG2  1 
ATOM   9748  C  CD1  . ILE   B  2  54  ? 48.205  -0.724  30.881   1.00 159.25 ? 58   ILE   B CD1  1 
ATOM   9749  H  H    . ILE   B  2  54  ? 45.327  1.879   31.530   1.00 181.75 ? 58   ILE   B H    1 
ATOM   9750  H  HA   . ILE   B  2  54  ? 45.540  1.672   28.940   1.00 179.40 ? 58   ILE   B HA   1 
ATOM   9751  H  HB   . ILE   B  2  54  ? 45.525  -0.373  30.883   1.00 184.78 ? 58   ILE   B HB   1 
ATOM   9752  H  HG12 . ILE   B  2  54  ? 47.747  0.619   29.432   1.00 189.84 ? 58   ILE   B HG12 1 
ATOM   9753  H  HG13 . ILE   B  2  54  ? 47.388  1.132   30.892   1.00 189.84 ? 58   ILE   B HG13 1 
ATOM   9754  H  HG21 . ILE   B  2  54  ? 46.359  -1.826  29.214   1.00 182.63 ? 58   ILE   B HG21 1 
ATOM   9755  H  HG22 . ILE   B  2  54  ? 44.868  -1.372  28.906   1.00 182.63 ? 58   ILE   B HG22 1 
ATOM   9756  H  HG23 . ILE   B  2  54  ? 46.080  -0.698  28.131   1.00 182.63 ? 58   ILE   B HG23 1 
ATOM   9757  H  HD11 . ILE   B  2  54  ? 49.103  -0.387  31.027   1.00 191.13 ? 58   ILE   B HD11 1 
ATOM   9758  H  HD12 . ILE   B  2  54  ? 47.815  -1.003  31.724   1.00 191.13 ? 58   ILE   B HD12 1 
ATOM   9759  H  HD13 . ILE   B  2  54  ? 48.229  -1.473  30.264   1.00 191.13 ? 58   ILE   B HD13 1 
ATOM   9760  N  N    . GLU   B  2  55  ? 43.547  0.659   27.894   1.00 136.35 ? 59   GLU   B N    1 
ATOM   9761  C  CA   . GLU   B  2  55  ? 42.267  0.403   27.247   1.00 132.36 ? 59   GLU   B CA   1 
ATOM   9762  C  C    . GLU   B  2  55  ? 42.413  -0.776  26.299   1.00 123.85 ? 59   GLU   B C    1 
ATOM   9763  O  O    . GLU   B  2  55  ? 43.325  -0.794  25.466   1.00 121.68 ? 59   GLU   B O    1 
ATOM   9764  C  CB   . GLU   B  2  55  ? 41.790  1.645   26.488   1.00 134.73 ? 59   GLU   B CB   1 
ATOM   9765  C  CG   . GLU   B  2  55  ? 40.967  2.602   27.328   1.00 135.76 ? 59   GLU   B CG   1 
ATOM   9766  C  CD   . GLU   B  2  55  ? 39.488  2.284   27.275   1.00 131.13 ? 59   GLU   B CD   1 
ATOM   9767  O  OE1  . GLU   B  2  55  ? 38.713  3.134   26.788   1.00 129.87 ? 59   GLU   B OE1  1 
ATOM   9768  O  OE2  . GLU   B  2  55  ? 39.101  1.176   27.704   1.00 128.10 ? 59   GLU   B OE2  1 
ATOM   9769  H  H    . GLU   B  2  55  ? 44.209  0.662   27.345   1.00 163.65 ? 59   GLU   B H    1 
ATOM   9770  H  HA   . GLU   B  2  55  ? 41.601  0.171   27.913   1.00 158.86 ? 59   GLU   B HA   1 
ATOM   9771  H  HB2  . GLU   B  2  55  ? 42.565  2.128   26.163   1.00 161.72 ? 59   GLU   B HB2  1 
ATOM   9772  H  HB3  . GLU   B  2  55  ? 41.240  1.360   25.741   1.00 161.72 ? 59   GLU   B HB3  1 
ATOM   9773  H  HG2  . GLU   B  2  55  ? 41.256  2.543   28.252   1.00 162.95 ? 59   GLU   B HG2  1 
ATOM   9774  H  HG3  . GLU   B  2  55  ? 41.095  3.505   26.998   1.00 162.95 ? 59   GLU   B HG3  1 
ATOM   9775  N  N    . ASN   B  2  56  ? 41.514  -1.755  26.419   1.00 116.56 ? 60   ASN   B N    1 
ATOM   9776  C  CA   . ASN   B  2  56  ? 41.595  -2.952  25.591   1.00 108.57 ? 60   ASN   B CA   1 
ATOM   9777  C  C    . ASN   B  2  56  ? 40.400  -3.871  25.823   1.00 105.02 ? 60   ASN   B C    1 
ATOM   9778  O  O    . ASN   B  2  56  ? 40.417  -4.685  26.755   1.00 105.19 ? 60   ASN   B O    1 
ATOM   9779  C  CB   . ASN   B  2  56  ? 42.902  -3.698  25.881   1.00 107.92 ? 60   ASN   B CB   1 
ATOM   9780  C  CG   . ASN   B  2  56  ? 42.891  -5.126  25.368   1.00 104.38 ? 60   ASN   B CG   1 
ATOM   9781  O  OD1  . ASN   B  2  56  ? 42.221  -5.445  24.385   1.00 103.48 ? 60   ASN   B OD1  1 
ATOM   9782  N  ND2  . ASN   B  2  56  ? 43.638  -5.995  26.038   1.00 103.26 ? 60   ASN   B ND2  1 
ATOM   9783  H  H    . ASN   B  2  56  ? 40.855  -1.747  26.971   1.00 139.91 ? 60   ASN   B H    1 
ATOM   9784  H  HA   . ASN   B  2  56  ? 41.575  -2.688  24.657   1.00 130.32 ? 60   ASN   B HA   1 
ATOM   9785  H  HB2  . ASN   B  2  56  ? 43.634  -3.230  25.451   1.00 129.54 ? 60   ASN   B HB2  1 
ATOM   9786  H  HB3  . ASN   B  2  56  ? 43.043  -3.725  26.841   1.00 129.54 ? 60   ASN   B HB3  1 
ATOM   9787  H  HD21 . ASN   B  2  56  ? 43.668  -6.818  25.788   1.00 123.94 ? 60   ASN   B HD21 1 
ATOM   9788  H  HD22 . ASN   B  2  56  ? 44.091  -5.736  26.721   1.00 123.94 ? 60   ASN   B HD22 1 
ATOM   9789  N  N    . PRO   B  2  57  ? 39.352  -3.783  25.004   1.00 102.04 ? 61   PRO   B N    1 
ATOM   9790  C  CA   . PRO   B  2  57  ? 38.240  -4.731  25.137   1.00 99.84  ? 61   PRO   B CA   1 
ATOM   9791  C  C    . PRO   B  2  57  ? 38.636  -6.121  24.665   1.00 97.87  ? 61   PRO   B C    1 
ATOM   9792  O  O    . PRO   B  2  57  ? 39.540  -6.290  23.844   1.00 97.94  ? 61   PRO   B O    1 
ATOM   9793  C  CB   . PRO   B  2  57  ? 37.150  -4.128  24.243   1.00 96.54  ? 61   PRO   B CB   1 
ATOM   9794  C  CG   . PRO   B  2  57  ? 37.897  -3.335  23.229   1.00 96.35  ? 61   PRO   B CG   1 
ATOM   9795  C  CD   . PRO   B  2  57  ? 39.107  -2.793  23.939   1.00 99.93  ? 61   PRO   B CD   1 
ATOM   9796  H  HA   . PRO   B  2  57  ? 37.925  -4.773  26.054   1.00 119.84 ? 61   PRO   B HA   1 
ATOM   9797  H  HB2  . PRO   B  2  57  ? 36.635  -4.835  23.824   1.00 115.89 ? 61   PRO   B HB2  1 
ATOM   9798  H  HB3  . PRO   B  2  57  ? 36.566  -3.560  24.769   1.00 115.89 ? 61   PRO   B HB3  1 
ATOM   9799  H  HG2  . PRO   B  2  57  ? 38.160  -3.911  22.493   1.00 115.66 ? 61   PRO   B HG2  1 
ATOM   9800  H  HG3  . PRO   B  2  57  ? 37.338  -2.613  22.902   1.00 115.66 ? 61   PRO   B HG3  1 
ATOM   9801  H  HD2  . PRO   B  2  57  ? 39.866  -2.741  23.336   1.00 119.95 ? 61   PRO   B HD2  1 
ATOM   9802  H  HD3  . PRO   B  2  57  ? 38.923  -1.919  24.316   1.00 119.95 ? 61   PRO   B HD3  1 
ATOM   9803  N  N    . VAL   B  2  58  ? 37.940  -7.126  25.197   1.00 94.75  ? 62   VAL   B N    1 
ATOM   9804  C  CA   . VAL   B  2  58  ? 38.200  -8.519  24.859   1.00 92.10  ? 62   VAL   B CA   1 
ATOM   9805  C  C    . VAL   B  2  58  ? 36.876  -9.240  24.650   1.00 87.65  ? 62   VAL   B C    1 
ATOM   9806  O  O    . VAL   B  2  58  ? 35.865  -8.924  25.284   1.00 85.67  ? 62   VAL   B O    1 
ATOM   9807  C  CB   . VAL   B  2  58  ? 39.034  -9.233  25.947   1.00 94.05  ? 62   VAL   B CB   1 
ATOM   9808  C  CG1  . VAL   B  2  58  ? 38.263  -9.292  27.261   1.00 89.89  ? 62   VAL   B CG1  1 
ATOM   9809  C  CG2  . VAL   B  2  58  ? 39.432  -10.632 25.484   1.00 95.03  ? 62   VAL   B CG2  1 
ATOM   9810  H  H    . VAL   B  2  58  ? 37.303  -7.021  25.766   1.00 113.74 ? 62   VAL   B H    1 
ATOM   9811  H  HA   . VAL   B  2  58  ? 38.694  -8.547  24.024   1.00 110.56 ? 62   VAL   B HA   1 
ATOM   9812  H  HB   . VAL   B  2  58  ? 39.847  -8.728  26.103   1.00 112.90 ? 62   VAL   B HB   1 
ATOM   9813  H  HG11 . VAL   B  2  58  ? 38.818  -9.716  27.934   1.00 107.91 ? 62   VAL   B HG11 1 
ATOM   9814  H  HG12 . VAL   B  2  58  ? 38.041  -8.389  27.538   1.00 107.91 ? 62   VAL   B HG12 1 
ATOM   9815  H  HG13 . VAL   B  2  58  ? 37.452  -9.806  27.129   1.00 107.91 ? 62   VAL   B HG13 1 
ATOM   9816  H  HG21 . VAL   B  2  58  ? 39.993  -11.041 26.161   1.00 114.07 ? 62   VAL   B HG21 1 
ATOM   9817  H  HG22 . VAL   B  2  58  ? 38.630  -11.161 25.354   1.00 114.07 ? 62   VAL   B HG22 1 
ATOM   9818  H  HG23 . VAL   B  2  58  ? 39.920  -10.560 24.649   1.00 114.07 ? 62   VAL   B HG23 1 
ATOM   9819  N  N    . SER   B  2  59  ? 36.895  -10.223 23.752   1.00 86.76  ? 63   SER   B N    1 
ATOM   9820  C  CA   . SER   B  2  59  ? 35.713  -11.035 23.503   1.00 84.92  ? 63   SER   B CA   1 
ATOM   9821  C  C    . SER   B  2  59  ? 35.266  -11.729 24.785   1.00 84.69  ? 63   SER   B C    1 
ATOM   9822  O  O    . SER   B  2  59  ? 36.089  -12.188 25.582   1.00 83.63  ? 63   SER   B O    1 
ATOM   9823  C  CB   . SER   B  2  59  ? 36.012  -12.069 22.417   1.00 87.21  ? 63   SER   B CB   1 
ATOM   9824  O  OG   . SER   B  2  59  ? 36.742  -11.486 21.351   1.00 90.35  ? 63   SER   B OG   1 
ATOM   9825  H  H    . SER   B  2  59  ? 37.578  -10.437 23.277   1.00 104.15 ? 63   SER   B H    1 
ATOM   9826  H  HA   . SER   B  2  59  ? 34.986  -10.471 23.194   1.00 101.94 ? 63   SER   B HA   1 
ATOM   9827  H  HB2  . SER   B  2  59  ? 36.536  -12.788 22.802   1.00 104.69 ? 63   SER   B HB2  1 
ATOM   9828  H  HB3  . SER   B  2  59  ? 35.174  -12.416 22.072   1.00 104.69 ? 63   SER   B HB3  1 
ATOM   9829  H  HG   . SER   B  2  59  ? 36.985  -12.080 20.810   1.00 108.46 ? 63   SER   B HG   1 
ATOM   9830  N  N    . GLN   B  2  60  ? 33.951  -11.811 24.979   1.00 87.79  ? 64   GLN   B N    1 
ATOM   9831  C  CA   . GLN   B  2  60  ? 33.393  -12.383 26.196   1.00 88.17  ? 64   GLN   B CA   1 
ATOM   9832  C  C    . GLN   B  2  60  ? 32.038  -13.006 25.894   1.00 85.58  ? 64   GLN   B C    1 
ATOM   9833  O  O    . GLN   B  2  60  ? 31.324  -12.569 24.988   1.00 83.66  ? 64   GLN   B O    1 
ATOM   9834  C  CB   . GLN   B  2  60  ? 33.248  -11.321 27.293   1.00 92.34  ? 64   GLN   B CB   1 
ATOM   9835  C  CG   . GLN   B  2  60  ? 32.367  -10.149 26.891   1.00 96.75  ? 64   GLN   B CG   1 
ATOM   9836  C  CD   . GLN   B  2  60  ? 32.388  -9.021  27.902   1.00 100.81 ? 64   GLN   B CD   1 
ATOM   9837  O  OE1  . GLN   B  2  60  ? 32.394  -9.253  29.111   1.00 101.70 ? 64   GLN   B OE1  1 
ATOM   9838  N  NE2  . GLN   B  2  60  ? 32.405  -7.788  27.409   1.00 100.84 ? 64   GLN   B NE2  1 
ATOM   9839  H  H    . GLN   B  2  60  ? 33.360  -11.539 24.416   1.00 105.39 ? 64   GLN   B H    1 
ATOM   9840  H  HA   . GLN   B  2  60  ? 33.979  -13.086 26.516   1.00 105.84 ? 64   GLN   B HA   1 
ATOM   9841  H  HB2  . GLN   B  2  60  ? 32.854  -11.734 28.078   1.00 110.85 ? 64   GLN   B HB2  1 
ATOM   9842  H  HB3  . GLN   B  2  60  ? 34.127  -10.972 27.508   1.00 110.85 ? 64   GLN   B HB3  1 
ATOM   9843  H  HG2  . GLN   B  2  60  ? 32.679  -9.797  26.042   1.00 116.13 ? 64   GLN   B HG2  1 
ATOM   9844  H  HG3  . GLN   B  2  60  ? 31.452  -10.458 26.805   1.00 116.13 ? 64   GLN   B HG3  1 
ATOM   9845  H  HE21 . GLN   B  2  60  ? 32.403  -7.665  26.558   1.00 121.05 ? 64   GLN   B HE21 1 
ATOM   9846  H  HE22 . GLN   B  2  60  ? 32.417  -7.112  27.941   1.00 121.05 ? 64   GLN   B HE22 1 
ATOM   9847  N  N    . VAL   B  2  61  ? 31.691  -14.030 26.673   1.00 84.06  ? 65   VAL   B N    1 
ATOM   9848  C  CA   . VAL   B  2  61  ? 30.424  -14.740 26.548   1.00 80.05  ? 65   VAL   B CA   1 
ATOM   9849  C  C    . VAL   B  2  61  ? 29.573  -14.429 27.771   1.00 83.27  ? 65   VAL   B C    1 
ATOM   9850  O  O    . VAL   B  2  61  ? 30.088  -14.363 28.894   1.00 85.75  ? 65   VAL   B O    1 
ATOM   9851  C  CB   . VAL   B  2  61  ? 30.631  -16.264 26.424   1.00 76.85  ? 65   VAL   B CB   1 
ATOM   9852  C  CG1  . VAL   B  2  61  ? 29.304  -16.960 26.144   1.00 76.78  ? 65   VAL   B CG1  1 
ATOM   9853  C  CG2  . VAL   B  2  61  ? 31.653  -16.588 25.349   1.00 74.54  ? 65   VAL   B CG2  1 
ATOM   9854  H  H    . VAL   B  2  61  ? 32.191  -14.339 27.301   1.00 100.91 ? 65   VAL   B H    1 
ATOM   9855  H  HA   . VAL   B  2  61  ? 29.967  -14.424 25.753   1.00 96.10  ? 65   VAL   B HA   1 
ATOM   9856  H  HB   . VAL   B  2  61  ? 30.977  -16.600 27.265   1.00 92.26  ? 65   VAL   B HB   1 
ATOM   9857  H  HG11 . VAL   B  2  61  ? 29.465  -17.909 26.020   1.00 92.17  ? 65   VAL   B HG11 1 
ATOM   9858  H  HG12 . VAL   B  2  61  ? 28.710  -16.822 26.899   1.00 92.17  ? 65   VAL   B HG12 1 
ATOM   9859  H  HG13 . VAL   B  2  61  ? 28.912  -16.583 25.341   1.00 92.17  ? 65   VAL   B HG13 1 
ATOM   9860  H  HG21 . VAL   B  2  61  ? 31.729  -17.551 25.265   1.00 89.48  ? 65   VAL   B HG21 1 
ATOM   9861  H  HG22 . VAL   B  2  61  ? 31.359  -16.206 24.507   1.00 89.48  ? 65   VAL   B HG22 1 
ATOM   9862  H  HG23 . VAL   B  2  61  ? 32.509  -16.209 25.602   1.00 89.48  ? 65   VAL   B HG23 1 
ATOM   9863  N  N    . GLU   B  2  62  ? 28.273  -14.248 27.557   1.00 85.56  ? 66   GLU   B N    1 
ATOM   9864  C  CA   . GLU   B  2  62  ? 27.307  -14.171 28.645   1.00 88.60  ? 66   GLU   B CA   1 
ATOM   9865  C  C    . GLU   B  2  62  ? 26.291  -15.290 28.477   1.00 86.61  ? 66   GLU   B C    1 
ATOM   9866  O  O    . GLU   B  2  62  ? 25.681  -15.428 27.411   1.00 85.12  ? 66   GLU   B O    1 
ATOM   9867  C  CB   . GLU   B  2  62  ? 26.585  -12.823 28.693   1.00 93.67  ? 66   GLU   B CB   1 
ATOM   9868  C  CG   . GLU   B  2  62  ? 25.644  -12.704 29.889   1.00 101.20 ? 66   GLU   B CG   1 
ATOM   9869  C  CD   . GLU   B  2  62  ? 24.745  -11.487 29.828   1.00 108.20 ? 66   GLU   B CD   1 
ATOM   9870  O  OE1  . GLU   B  2  62  ? 24.923  -10.653 28.916   1.00 109.95 ? 66   GLU   B OE1  1 
ATOM   9871  O  OE2  . GLU   B  2  62  ? 23.851  -11.372 30.693   1.00 111.30 ? 66   GLU   B OE2  1 
ATOM   9872  H  H    . GLU   B  2  62  ? 27.922  -14.165 26.776   1.00 102.71 ? 66   GLU   B H    1 
ATOM   9873  H  HA   . GLU   B  2  62  ? 27.778  -14.282 29.486   1.00 106.36 ? 66   GLU   B HA   1 
ATOM   9874  H  HB2  . GLU   B  2  62  ? 27.244  -12.113 28.757   1.00 112.45 ? 66   GLU   B HB2  1 
ATOM   9875  H  HB3  . GLU   B  2  62  ? 26.060  -12.716 27.885   1.00 112.45 ? 66   GLU   B HB3  1 
ATOM   9876  H  HG2  . GLU   B  2  62  ? 25.078  -13.491 29.922   1.00 121.47 ? 66   GLU   B HG2  1 
ATOM   9877  H  HG3  . GLU   B  2  62  ? 26.173  -12.642 30.700   1.00 121.47 ? 66   GLU   B HG3  1 
ATOM   9878  N  N    . ILE   B  2  63  ? 26.110  -16.076 29.530   1.00 86.05  ? 67   ILE   B N    1 
ATOM   9879  C  CA   . ILE   B  2  63  ? 25.141  -17.164 29.534   1.00 79.87  ? 67   ILE   B CA   1 
ATOM   9880  C  C    . ILE   B  2  63  ? 23.823  -16.626 30.076   1.00 80.83  ? 67   ILE   B C    1 
ATOM   9881  O  O    . ILE   B  2  63  ? 23.752  -16.176 31.225   1.00 86.05  ? 67   ILE   B O    1 
ATOM   9882  C  CB   . ILE   B  2  63  ? 25.644  -18.352 30.367   1.00 77.67  ? 67   ILE   B CB   1 
ATOM   9883  C  CG1  . ILE   B  2  63  ? 26.953  -18.883 29.773   1.00 76.30  ? 67   ILE   B CG1  1 
ATOM   9884  C  CG2  . ILE   B  2  63  ? 24.587  -19.448 30.419   1.00 76.75  ? 67   ILE   B CG2  1 
ATOM   9885  C  CD1  . ILE   B  2  63  ? 27.567  -20.039 30.534   1.00 77.88  ? 67   ILE   B CD1  1 
ATOM   9886  H  H    . ILE   B  2  63  ? 26.544  -15.998 30.269   1.00 103.29 ? 67   ILE   B H    1 
ATOM   9887  H  HA   . ILE   B  2  63  ? 24.994  -17.471 28.626   1.00 95.88  ? 67   ILE   B HA   1 
ATOM   9888  H  HB   . ILE   B  2  63  ? 25.813  -18.053 31.274   1.00 93.25  ? 67   ILE   B HB   1 
ATOM   9889  H  HG12 . ILE   B  2  63  ? 26.781  -19.188 28.868   1.00 91.60  ? 67   ILE   B HG12 1 
ATOM   9890  H  HG13 . ILE   B  2  63  ? 27.602  -18.162 29.762   1.00 91.60  ? 67   ILE   B HG13 1 
ATOM   9891  H  HG21 . ILE   B  2  63  ? 24.914  -20.175 30.972   1.00 92.14  ? 67   ILE   B HG21 1 
ATOM   9892  H  HG22 . ILE   B  2  63  ? 23.772  -19.084 30.799   1.00 92.14  ? 67   ILE   B HG22 1 
ATOM   9893  H  HG23 . ILE   B  2  63  ? 24.419  -19.768 29.519   1.00 92.14  ? 67   ILE   B HG23 1 
ATOM   9894  H  HD11 . ILE   B  2  63  ? 28.402  -20.289 30.109   1.00 93.49  ? 67   ILE   B HD11 1 
ATOM   9895  H  HD12 . ILE   B  2  63  ? 27.731  -19.762 31.449   1.00 93.49  ? 67   ILE   B HD12 1 
ATOM   9896  H  HD13 . ILE   B  2  63  ? 26.952  -20.788 30.521   1.00 93.49  ? 67   ILE   B HD13 1 
ATOM   9897  N  N    . LEU   B  2  64  ? 22.781  -16.670 29.248   1.00 80.68  ? 68   LEU   B N    1 
ATOM   9898  C  CA   . LEU   B  2  64  ? 21.456  -16.199 29.631   1.00 84.51  ? 68   LEU   B CA   1 
ATOM   9899  C  C    . LEU   B  2  64  ? 20.512  -17.332 30.010   1.00 87.04  ? 68   LEU   B C    1 
ATOM   9900  O  O    . LEU   B  2  64  ? 19.740  -17.193 30.962   1.00 90.62  ? 68   LEU   B O    1 
ATOM   9901  C  CB   . LEU   B  2  64  ? 20.834  -15.388 28.491   1.00 84.90  ? 68   LEU   B CB   1 
ATOM   9902  C  CG   . LEU   B  2  64  ? 21.651  -14.202 27.976   1.00 85.51  ? 68   LEU   B CG   1 
ATOM   9903  C  CD1  . LEU   B  2  64  ? 20.868  -13.470 26.900   1.00 86.24  ? 68   LEU   B CD1  1 
ATOM   9904  C  CD2  . LEU   B  2  64  ? 22.025  -13.257 29.106   1.00 87.81  ? 68   LEU   B CD2  1 
ATOM   9905  H  H    . LEU   B  2  64  ? 22.820  -16.974 28.445   1.00 96.86  ? 68   LEU   B H    1 
ATOM   9906  H  HA   . LEU   B  2  64  ? 21.544  -15.615 30.400   1.00 101.45 ? 68   LEU   B HA   1 
ATOM   9907  H  HB2  . LEU   B  2  64  ? 20.693  -15.984 27.739   1.00 101.92 ? 68   LEU   B HB2  1 
ATOM   9908  H  HB3  . LEU   B  2  64  ? 19.985  -15.036 28.800   1.00 101.92 ? 68   LEU   B HB3  1 
ATOM   9909  H  HG   . LEU   B  2  64  ? 22.479  -14.529 27.592   1.00 102.65 ? 68   LEU   B HG   1 
ATOM   9910  H  HD11 . LEU   B  2  64  ? 21.364  -12.682 26.629   1.00 103.52 ? 68   LEU   B HD11 1 
ATOM   9911  H  HD12 . LEU   B  2  64  ? 20.746  -14.061 26.140   1.00 103.52 ? 68   LEU   B HD12 1 
ATOM   9912  H  HD13 . LEU   B  2  64  ? 20.004  -13.211 27.258   1.00 103.52 ? 68   LEU   B HD13 1 
ATOM   9913  H  HD21 . LEU   B  2  64  ? 22.506  -12.499 28.738   1.00 105.41 ? 68   LEU   B HD21 1 
ATOM   9914  H  HD22 . LEU   B  2  64  ? 21.216  -12.953 29.546   1.00 105.41 ? 68   LEU   B HD22 1 
ATOM   9915  H  HD23 . LEU   B  2  64  ? 22.588  -13.729 29.740   1.00 105.41 ? 68   LEU   B HD23 1 
ATOM   9916  N  N    . LYS   B  2  65  ? 20.553  -18.448 29.285   1.00 86.96  ? 69   LYS   B N    1 
ATOM   9917  C  CA   . LYS   B  2  65  ? 19.729  -19.612 29.593   1.00 89.17  ? 69   LYS   B CA   1 
ATOM   9918  C  C    . LYS   B  2  65  ? 20.592  -20.857 29.467   1.00 81.90  ? 69   LYS   B C    1 
ATOM   9919  O  O    . LYS   B  2  65  ? 21.128  -21.134 28.390   1.00 80.82  ? 69   LYS   B O    1 
ATOM   9920  C  CB   . LYS   B  2  65  ? 18.514  -19.699 28.664   1.00 94.59  ? 69   LYS   B CB   1 
ATOM   9921  C  CG   . LYS   B  2  65  ? 17.474  -18.611 28.903   1.00 100.78 ? 69   LYS   B CG   1 
ATOM   9922  C  CD   . LYS   B  2  65  ? 16.184  -18.879 28.135   1.00 105.47 ? 69   LYS   B CD   1 
ATOM   9923  C  CE   . LYS   B  2  65  ? 16.015  -17.925 26.963   1.00 112.09 ? 69   LYS   B CE   1 
ATOM   9924  N  NZ   . LYS   B  2  65  ? 14.754  -18.176 26.210   1.00 121.58 ? 69   LYS   B NZ   1 
ATOM   9925  H  H    . LYS   B  2  65  ? 21.058  -18.556 28.597   1.00 104.39 ? 69   LYS   B H    1 
ATOM   9926  H  HA   . LYS   B  2  65  ? 19.408  -19.549 30.506   1.00 107.05 ? 69   LYS   B HA   1 
ATOM   9927  H  HB2  . LYS   B  2  65  ? 18.818  -19.620 27.746   1.00 113.54 ? 69   LYS   B HB2  1 
ATOM   9928  H  HB3  . LYS   B  2  65  ? 18.081  -20.556 28.797   1.00 113.54 ? 69   LYS   B HB3  1 
ATOM   9929  H  HG2  . LYS   B  2  65  ? 17.261  -18.574 29.849   1.00 120.97 ? 69   LYS   B HG2  1 
ATOM   9930  H  HG3  . LYS   B  2  65  ? 17.830  -17.758 28.609   1.00 120.97 ? 69   LYS   B HG3  1 
ATOM   9931  H  HD2  . LYS   B  2  65  ? 16.200  -19.785 27.790   1.00 126.60 ? 69   LYS   B HD2  1 
ATOM   9932  H  HD3  . LYS   B  2  65  ? 15.427  -18.765 28.731   1.00 126.60 ? 69   LYS   B HD3  1 
ATOM   9933  H  HE2  . LYS   B  2  65  ? 15.993  -17.014 27.294   1.00 134.55 ? 69   LYS   B HE2  1 
ATOM   9934  H  HE3  . LYS   B  2  65  ? 16.760  -18.037 26.351   1.00 134.55 ? 69   LYS   B HE3  1 
ATOM   9935  H  HZ1  . LYS   B  2  65  ? 14.694  -17.615 25.522   1.00 145.93 ? 69   LYS   B HZ1  1 
ATOM   9936  H  HZ2  . LYS   B  2  65  ? 14.744  -19.012 25.903   1.00 145.93 ? 69   LYS   B HZ2  1 
ATOM   9937  H  HZ3  . LYS   B  2  65  ? 14.052  -18.057 26.744   1.00 145.93 ? 69   LYS   B HZ3  1 
ATOM   9938  N  N    . ASN   B  2  66  ? 20.729  -21.602 30.565   1.00 77.31  ? 70   ASN   B N    1 
ATOM   9939  C  CA   . ASN   B  2  66  ? 21.543  -22.810 30.593   1.00 72.61  ? 70   ASN   B CA   1 
ATOM   9940  C  C    . ASN   B  2  66  ? 20.880  -23.855 31.493   1.00 72.63  ? 70   ASN   B C    1 
ATOM   9941  O  O    . ASN   B  2  66  ? 21.455  -24.351 32.458   1.00 70.30  ? 70   ASN   B O    1 
ATOM   9942  C  CB   . ASN   B  2  66  ? 22.963  -22.500 31.065   1.00 70.80  ? 70   ASN   B CB   1 
ATOM   9943  C  CG   . ASN   B  2  66  ? 23.901  -23.679 30.902   1.00 71.03  ? 70   ASN   B CG   1 
ATOM   9944  O  OD1  . ASN   B  2  66  ? 23.693  -24.539 30.046   1.00 70.52  ? 70   ASN   B OD1  1 
ATOM   9945  N  ND2  . ASN   B  2  66  ? 24.941  -23.726 31.726   1.00 71.80  ? 70   ASN   B ND2  1 
ATOM   9946  H  H    . ASN   B  2  66  ? 20.352  -21.422 31.317   1.00 92.80  ? 70   ASN   B H    1 
ATOM   9947  H  HA   . ASN   B  2  66  ? 21.588  -23.170 29.694   1.00 87.17  ? 70   ASN   B HA   1 
ATOM   9948  H  HB2  . ASN   B  2  66  ? 23.315  -21.761 30.545   1.00 84.99  ? 70   ASN   B HB2  1 
ATOM   9949  H  HB3  . ASN   B  2  66  ? 22.939  -22.262 32.006   1.00 84.99  ? 70   ASN   B HB3  1 
ATOM   9950  H  HD21 . ASN   B  2  66  ? 25.502  -24.375 31.673   1.00 86.19  ? 70   ASN   B HD21 1 
ATOM   9951  H  HD22 . ASN   B  2  66  ? 25.054  -23.107 32.312   1.00 86.19  ? 70   ASN   B HD22 1 
ATOM   9952  N  N    . LYS   B  2  67  ? 19.638  -24.195 31.171   1.00 74.08  ? 71   LYS   B N    1 
ATOM   9953  C  CA   . LYS   B  2  67  ? 18.949  -25.246 31.903   1.00 75.81  ? 71   LYS   B CA   1 
ATOM   9954  C  C    . LYS   B  2  67  ? 19.658  -26.579 31.672   1.00 71.76  ? 71   LYS   B C    1 
ATOM   9955  O  O    . LYS   B  2  67  ? 20.035  -26.892 30.536   1.00 70.39  ? 71   LYS   B O    1 
ATOM   9956  C  CB   . LYS   B  2  67  ? 17.490  -25.336 31.452   1.00 78.41  ? 71   LYS   B CB   1 
ATOM   9957  C  CG   . LYS   B  2  67  ? 16.637  -26.299 32.262   1.00 86.46  ? 71   LYS   B CG   1 
ATOM   9958  C  CD   . LYS   B  2  67  ? 15.191  -26.288 31.784   1.00 94.77  ? 71   LYS   B CD   1 
ATOM   9959  C  CE   . LYS   B  2  67  ? 14.317  -27.208 32.622   1.00 104.54 ? 71   LYS   B CE   1 
ATOM   9960  N  NZ   . LYS   B  2  67  ? 12.935  -27.336 32.076   1.00 109.73 ? 71   LYS   B NZ   1 
ATOM   9961  H  H    . LYS   B  2  67  ? 19.177  -23.836 30.540   1.00 88.93  ? 71   LYS   B H    1 
ATOM   9962  H  HA   . LYS   B  2  67  ? 18.960  -25.052 32.853   1.00 91.01  ? 71   LYS   B HA   1 
ATOM   9963  H  HB2  . LYS   B  2  67  ? 17.089  -24.456 31.527   1.00 94.12  ? 71   LYS   B HB2  1 
ATOM   9964  H  HB3  . LYS   B  2  67  ? 17.470  -25.633 30.529   1.00 94.12  ? 71   LYS   B HB3  1 
ATOM   9965  H  HG2  . LYS   B  2  67  ? 16.985  -27.200 32.164   1.00 103.78 ? 71   LYS   B HG2  1 
ATOM   9966  H  HG3  . LYS   B  2  67  ? 16.653  -26.038 33.196   1.00 103.78 ? 71   LYS   B HG3  1 
ATOM   9967  H  HD2  . LYS   B  2  67  ? 14.837  -25.387 31.852   1.00 113.76 ? 71   LYS   B HD2  1 
ATOM   9968  H  HD3  . LYS   B  2  67  ? 15.155  -26.590 30.863   1.00 113.76 ? 71   LYS   B HD3  1 
ATOM   9969  H  HE2  . LYS   B  2  67  ? 14.715  -28.092 32.643   1.00 125.49 ? 71   LYS   B HE2  1 
ATOM   9970  H  HE3  . LYS   B  2  67  ? 14.253  -26.852 33.522   1.00 125.49 ? 71   LYS   B HE3  1 
ATOM   9971  H  HZ1  . LYS   B  2  67  ? 12.458  -27.892 32.581   1.00 131.72 ? 71   LYS   B HZ1  1 
ATOM   9972  H  HZ2  . LYS   B  2  67  ? 12.537  -26.540 32.068   1.00 131.72 ? 71   LYS   B HZ2  1 
ATOM   9973  H  HZ3  . LYS   B  2  67  ? 12.965  -27.653 31.245   1.00 131.72 ? 71   LYS   B HZ3  1 
ATOM   9974  N  N    . PRO   B  2  68  ? 19.859  -27.389 32.714   1.00 70.19  ? 72   PRO   B N    1 
ATOM   9975  C  CA   . PRO   B  2  68  ? 20.589  -28.646 32.523   1.00 69.02  ? 72   PRO   B CA   1 
ATOM   9976  C  C    . PRO   B  2  68  ? 19.854  -29.572 31.566   1.00 67.50  ? 72   PRO   B C    1 
ATOM   9977  O  O    . PRO   B  2  68  ? 18.631  -29.514 31.423   1.00 66.35  ? 72   PRO   B O    1 
ATOM   9978  C  CB   . PRO   B  2  68  ? 20.661  -29.243 33.935   1.00 70.56  ? 72   PRO   B CB   1 
ATOM   9979  C  CG   . PRO   B  2  68  ? 20.296  -28.131 34.865   1.00 73.73  ? 72   PRO   B CG   1 
ATOM   9980  C  CD   . PRO   B  2  68  ? 19.372  -27.249 34.097   1.00 70.94  ? 72   PRO   B CD   1 
ATOM   9981  H  HA   . PRO   B  2  68  ? 21.486  -28.477 32.194   1.00 82.86  ? 72   PRO   B HA   1 
ATOM   9982  H  HB2  . PRO   B  2  68  ? 20.032  -29.977 34.013   1.00 84.71  ? 72   PRO   B HB2  1 
ATOM   9983  H  HB3  . PRO   B  2  68  ? 21.562  -29.557 34.112   1.00 84.71  ? 72   PRO   B HB3  1 
ATOM   9984  H  HG2  . PRO   B  2  68  ? 19.854  -28.492 35.650   1.00 88.51  ? 72   PRO   B HG2  1 
ATOM   9985  H  HG3  . PRO   B  2  68  ? 21.094  -27.648 35.128   1.00 88.51  ? 72   PRO   B HG3  1 
ATOM   9986  H  HD2  . PRO   B  2  68  ? 18.455  -27.555 34.175   1.00 85.17  ? 72   PRO   B HD2  1 
ATOM   9987  H  HD3  . PRO   B  2  68  ? 19.441  -26.329 34.397   1.00 85.17  ? 72   PRO   B HD3  1 
ATOM   9988  N  N    . LEU   B  2  69  ? 20.621  -30.431 30.899   1.00 67.09  ? 73   LEU   B N    1 
ATOM   9989  C  CA   . LEU   B  2  69  ? 20.030  -31.416 30.004   1.00 65.13  ? 73   LEU   B CA   1 
ATOM   9990  C  C    . LEU   B  2  69  ? 19.137  -32.370 30.789   1.00 67.22  ? 73   LEU   B C    1 
ATOM   9991  O  O    . LEU   B  2  69  ? 19.481  -32.804 31.891   1.00 68.20  ? 73   LEU   B O    1 
ATOM   9992  C  CB   . LEU   B  2  69  ? 21.126  -32.197 29.282   1.00 61.21  ? 73   LEU   B CB   1 
ATOM   9993  C  CG   . LEU   B  2  69  ? 21.928  -31.432 28.229   1.00 59.54  ? 73   LEU   B CG   1 
ATOM   9994  C  CD1  . LEU   B  2  69  ? 23.222  -32.168 27.936   1.00 61.75  ? 73   LEU   B CD1  1 
ATOM   9995  C  CD2  . LEU   B  2  69  ? 21.111  -31.259 26.960   1.00 58.64  ? 73   LEU   B CD2  1 
ATOM   9996  H  H    . LEU   B  2  69  ? 21.479  -30.463 30.947   1.00 80.54  ? 73   LEU   B H    1 
ATOM   9997  H  HA   . LEU   B  2  69  ? 19.489  -30.967 29.336   1.00 78.19  ? 73   LEU   B HA   1 
ATOM   9998  H  HB2  . LEU   B  2  69  ? 21.758  -32.513 29.947   1.00 73.49  ? 73   LEU   B HB2  1 
ATOM   9999  H  HB3  . LEU   B  2  69  ? 20.712  -32.950 28.832   1.00 73.49  ? 73   LEU   B HB3  1 
ATOM   10000 H  HG   . LEU   B  2  69  ? 22.145  -30.548 28.565   1.00 71.48  ? 73   LEU   B HG   1 
ATOM   10001 H  HD11 . LEU   B  2  69  ? 23.715  -31.681 27.257   1.00 74.14  ? 73   LEU   B HD11 1 
ATOM   10002 H  HD12 . LEU   B  2  69  ? 23.746  -32.222 28.751   1.00 74.14  ? 73   LEU   B HD12 1 
ATOM   10003 H  HD13 . LEU   B  2  69  ? 23.013  -33.060 27.618   1.00 74.14  ? 73   LEU   B HD13 1 
ATOM   10004 H  HD21 . LEU   B  2  69  ? 21.643  -30.781 26.305   1.00 70.40  ? 73   LEU   B HD21 1 
ATOM   10005 H  HD22 . LEU   B  2  69  ? 20.872  -32.134 26.616   1.00 70.40  ? 73   LEU   B HD22 1 
ATOM   10006 H  HD23 . LEU   B  2  69  ? 20.309  -30.755 27.167   1.00 70.40  ? 73   LEU   B HD23 1 
ATOM   10007 N  N    . SER   B  2  70  ? 17.984  -32.702 30.212   1.00 70.05  ? 74   SER   B N    1 
ATOM   10008 C  CA   . SER   B  2  70  ? 17.024  -33.558 30.894   1.00 72.24  ? 74   SER   B CA   1 
ATOM   10009 C  C    . SER   B  2  70  ? 17.505  -35.001 30.864   1.00 74.03  ? 74   SER   B C    1 
ATOM   10010 O  O    . SER   B  2  70  ? 17.953  -35.500 29.829   1.00 76.69  ? 74   SER   B O    1 
ATOM   10011 C  CB   . SER   B  2  70  ? 15.644  -33.454 30.244   1.00 71.71  ? 74   SER   B CB   1 
ATOM   10012 O  OG   . SER   B  2  70  ? 15.533  -34.328 29.134   1.00 70.15  ? 74   SER   B OG   1 
ATOM   10013 H  H    . SER   B  2  70  ? 17.737  -32.444 29.430   1.00 84.10  ? 74   SER   B H    1 
ATOM   10014 H  HA   . SER   B  2  70  ? 16.937  -33.275 31.817   1.00 86.72  ? 74   SER   B HA   1 
ATOM   10015 H  HB2  . SER   B  2  70  ? 14.969  -33.691 30.899   1.00 86.09  ? 74   SER   B HB2  1 
ATOM   10016 H  HB3  . SER   B  2  70  ? 15.507  -32.543 29.941   1.00 86.09  ? 74   SER   B HB3  1 
ATOM   10017 H  HG   . SER   B  2  70  ? 14.730  -34.393 28.899   1.00 84.22  ? 74   SER   B HG   1 
ATOM   10018 N  N    . VAL   B  2  71  ? 17.403  -35.670 32.010   1.00 77.17  ? 75   VAL   B N    1 
ATOM   10019 C  CA   . VAL   B  2  71  ? 17.881  -37.036 32.183   1.00 77.06  ? 75   VAL   B CA   1 
ATOM   10020 C  C    . VAL   B  2  71  ? 16.675  -37.954 32.326   1.00 75.18  ? 75   VAL   B C    1 
ATOM   10021 O  O    . VAL   B  2  71  ? 15.762  -37.673 33.113   1.00 73.97  ? 75   VAL   B O    1 
ATOM   10022 C  CB   . VAL   B  2  71  ? 18.814  -37.153 33.402   1.00 79.35  ? 75   VAL   B CB   1 
ATOM   10023 C  CG1  . VAL   B  2  71  ? 18.094  -36.717 34.675   1.00 85.25  ? 75   VAL   B CG1  1 
ATOM   10024 C  CG2  . VAL   B  2  71  ? 19.342  -38.573 33.534   1.00 82.19  ? 75   VAL   B CG2  1 
ATOM   10025 H  H    . VAL   B  2  71  ? 17.049  -35.342 32.722   1.00 92.64  ? 75   VAL   B H    1 
ATOM   10026 H  HA   . VAL   B  2  71  ? 18.374  -37.306 31.392   1.00 92.51  ? 75   VAL   B HA   1 
ATOM   10027 H  HB   . VAL   B  2  71  ? 19.572  -36.562 33.273   1.00 95.26  ? 75   VAL   B HB   1 
ATOM   10028 H  HG11 . VAL   B  2  71  ? 18.715  -36.764 35.420   1.00 102.34 ? 75   VAL   B HG11 1 
ATOM   10029 H  HG12 . VAL   B  2  71  ? 17.779  -35.807 34.564   1.00 102.34 ? 75   VAL   B HG12 1 
ATOM   10030 H  HG13 . VAL   B  2  71  ? 17.343  -37.310 34.833   1.00 102.34 ? 75   VAL   B HG13 1 
ATOM   10031 H  HG21 . VAL   B  2  71  ? 19.950  -38.615 34.289   1.00 98.67  ? 75   VAL   B HG21 1 
ATOM   10032 H  HG22 . VAL   B  2  71  ? 18.595  -39.176 33.677   1.00 98.67  ? 75   VAL   B HG22 1 
ATOM   10033 H  HG23 . VAL   B  2  71  ? 19.810  -38.814 32.719   1.00 98.67  ? 75   VAL   B HG23 1 
ATOM   10034 N  N    . GLY   B  2  72  ? 16.673  -39.045 31.567   1.00 70.19  ? 76   GLY   B N    1 
ATOM   10035 C  CA   . GLY   B  2  72  ? 15.630  -40.041 31.664   1.00 71.98  ? 76   GLY   B CA   1 
ATOM   10036 C  C    . GLY   B  2  72  ? 14.381  -39.662 30.892   1.00 75.18  ? 76   GLY   B C    1 
ATOM   10037 O  O    . GLY   B  2  72  ? 14.241  -38.564 30.350   1.00 75.21  ? 76   GLY   B O    1 
ATOM   10038 H  H    . GLY   B  2  72  ? 17.276  -39.228 30.981   1.00 84.26  ? 76   GLY   B H    1 
ATOM   10039 H  HA2  . GLY   B  2  72  ? 15.960  -40.884 31.315   1.00 86.41  ? 76   GLY   B HA2  1 
ATOM   10040 H  HA3  . GLY   B  2  72  ? 15.388  -40.159 32.596   1.00 86.41  ? 76   GLY   B HA3  1 
ATOM   10041 N  N    . ARG   B  2  73  ? 13.451  -40.611 30.843   1.00 77.13  ? 77   ARG   B N    1 
ATOM   10042 C  CA   . ARG   B  2  73  ? 12.187  -40.384 30.159   1.00 79.12  ? 77   ARG   B CA   1 
ATOM   10043 C  C    . ARG   B  2  73  ? 11.370  -39.332 30.899   1.00 78.33  ? 77   ARG   B C    1 
ATOM   10044 O  O    . ARG   B  2  73  ? 11.161  -39.431 32.112   1.00 80.27  ? 77   ARG   B O    1 
ATOM   10045 C  CB   . ARG   B  2  73  ? 11.400  -41.689 30.053   1.00 89.96  ? 77   ARG   B CB   1 
ATOM   10046 C  CG   . ARG   B  2  73  ? 10.084  -41.521 29.330   1.00 94.10  ? 77   ARG   B CG   1 
ATOM   10047 C  CD   . ARG   B  2  73  ? 9.384   -42.837 29.063   1.00 96.08  ? 77   ARG   B CD   1 
ATOM   10048 N  NE   . ARG   B  2  73  ? 8.149   -42.604 28.323   1.00 100.82 ? 77   ARG   B NE   1 
ATOM   10049 C  CZ   . ARG   B  2  73  ? 7.058   -42.055 28.849   1.00 108.02 ? 77   ARG   B CZ   1 
ATOM   10050 N  NH1  . ARG   B  2  73  ? 7.044   -41.686 30.123   1.00 110.46 ? 77   ARG   B NH1  1 
ATOM   10051 N  NH2  . ARG   B  2  73  ? 5.981   -41.871 28.099   1.00 114.99 ? 77   ARG   B NH2  1 
ATOM   10052 H  H    . ARG   B  2  73  ? 13.528  -41.391 31.196   1.00 92.59  ? 77   ARG   B H    1 
ATOM   10053 H  HA   . ARG   B  2  73  ? 12.360  -40.062 29.260   1.00 94.98  ? 77   ARG   B HA   1 
ATOM   10054 H  HB2  . ARG   B  2  73  ? 11.930  -42.338 29.564   1.00 107.99 ? 77   ARG   B HB2  1 
ATOM   10055 H  HB3  . ARG   B  2  73  ? 11.213  -42.018 30.946   1.00 107.99 ? 77   ARG   B HB3  1 
ATOM   10056 H  HG2  . ARG   B  2  73  ? 9.494   -40.973 29.872   1.00 112.95 ? 77   ARG   B HG2  1 
ATOM   10057 H  HG3  . ARG   B  2  73  ? 10.245  -41.090 28.476   1.00 112.95 ? 77   ARG   B HG3  1 
ATOM   10058 H  HD2  . ARG   B  2  73  ? 9.959   -43.412 28.535   1.00 115.33 ? 77   ARG   B HD2  1 
ATOM   10059 H  HD3  . ARG   B  2  73  ? 9.166   -43.268 29.905   1.00 115.33 ? 77   ARG   B HD3  1 
ATOM   10060 H  HE   . ARG   B  2  73  ? 8.125   -42.835 27.495   1.00 121.02 ? 77   ARG   B HE   1 
ATOM   10061 H  HH11 . ARG   B  2  73  ? 7.742   -41.802 30.612   1.00 132.59 ? 77   ARG   B HH11 1 
ATOM   10062 H  HH12 . ARG   B  2  73  ? 6.336   -41.332 30.461   1.00 132.59 ? 77   ARG   B HH12 1 
ATOM   10063 H  HH21 . ARG   B  2  73  ? 5.987   -42.107 27.272   1.00 138.03 ? 77   ARG   B HH21 1 
ATOM   10064 H  HH22 . ARG   B  2  73  ? 5.275   -41.516 28.440   1.00 138.03 ? 77   ARG   B HH22 1 
ATOM   10065 N  N    . GLN   B  2  74  ? 10.906  -38.325 30.163   1.00 74.55  ? 78   GLN   B N    1 
ATOM   10066 C  CA   . GLN   B  2  74  ? 10.142  -37.219 30.724   1.00 80.26  ? 78   GLN   B CA   1 
ATOM   10067 C  C    . GLN   B  2  74  ? 8.663   -37.425 30.424   1.00 90.13  ? 78   GLN   B C    1 
ATOM   10068 O  O    . GLN   B  2  74  ? 8.264   -37.470 29.255   1.00 89.62  ? 78   GLN   B O    1 
ATOM   10069 C  CB   . GLN   B  2  74  ? 10.618  -35.886 30.149   1.00 73.70  ? 78   GLN   B CB   1 
ATOM   10070 C  CG   . GLN   B  2  74  ? 12.095  -35.630 30.348   1.00 71.88  ? 78   GLN   B CG   1 
ATOM   10071 C  CD   . GLN   B  2  74  ? 12.475  -35.584 31.813   1.00 74.93  ? 78   GLN   B CD   1 
ATOM   10072 O  OE1  . GLN   B  2  74  ? 11.878  -34.847 32.598   1.00 77.75  ? 78   GLN   B OE1  1 
ATOM   10073 N  NE2  . GLN   B  2  74  ? 13.464  -36.382 32.193   1.00 74.44  ? 78   GLN   B NE2  1 
ATOM   10074 H  H    . GLN   B  2  74  ? 11.026  -38.260 29.314   1.00 89.50  ? 78   GLN   B H    1 
ATOM   10075 H  HA   . GLN   B  2  74  ? 10.260  -37.205 31.687   1.00 96.34  ? 78   GLN   B HA   1 
ATOM   10076 H  HB2  . GLN   B  2  74  ? 10.441  -35.877 29.196   1.00 88.47  ? 78   GLN   B HB2  1 
ATOM   10077 H  HB3  . GLN   B  2  74  ? 10.132  -35.167 30.583   1.00 88.47  ? 78   GLN   B HB3  1 
ATOM   10078 H  HG2  . GLN   B  2  74  ? 12.601  -36.342 29.927   1.00 86.30  ? 78   GLN   B HG2  1 
ATOM   10079 H  HG3  . GLN   B  2  74  ? 12.327  -34.777 29.949   1.00 86.30  ? 78   GLN   B HG3  1 
ATOM   10080 H  HE21 . GLN   B  2  74  ? 13.852  -36.890 31.617   1.00 89.36  ? 78   GLN   B HE21 1 
ATOM   10081 H  HE22 . GLN   B  2  74  ? 13.717  -36.393 33.015   1.00 89.36  ? 78   GLN   B HE22 1 
ATOM   10082 N  N    . LYS   B  2  75  ? 7.852   -37.544 31.478   1.00 97.30  ? 79   LYS   B N    1 
ATOM   10083 C  CA   . LYS   B  2  75  ? 6.411   -37.645 31.288   1.00 103.17 ? 79   LYS   B CA   1 
ATOM   10084 C  C    . LYS   B  2  75  ? 5.809   -36.351 30.755   1.00 107.01 ? 79   LYS   B C    1 
ATOM   10085 O  O    . LYS   B  2  75  ? 4.682   -36.371 30.249   1.00 113.93 ? 79   LYS   B O    1 
ATOM   10086 C  CB   . LYS   B  2  75  ? 5.725   -38.023 32.603   1.00 105.95 ? 79   LYS   B CB   1 
ATOM   10087 C  CG   . LYS   B  2  75  ? 6.025   -39.433 33.092   1.00 105.20 ? 79   LYS   B CG   1 
ATOM   10088 C  CD   . LYS   B  2  75  ? 5.322   -39.715 34.415   1.00 107.99 ? 79   LYS   B CD   1 
ATOM   10089 C  CE   . LYS   B  2  75  ? 5.617   -41.119 34.924   1.00 108.26 ? 79   LYS   B CE   1 
ATOM   10090 N  NZ   . LYS   B  2  75  ? 4.950   -41.398 36.228   1.00 113.00 ? 79   LYS   B NZ   1 
ATOM   10091 H  H    . LYS   B  2  75  ? 8.110   -37.568 32.298   1.00 116.80 ? 79   LYS   B H    1 
ATOM   10092 H  HA   . LYS   B  2  75  ? 6.236   -38.351 30.646   1.00 123.84 ? 79   LYS   B HA   1 
ATOM   10093 H  HB2  . LYS   B  2  75  ? 6.018   -37.406 33.292   1.00 127.17 ? 79   LYS   B HB2  1 
ATOM   10094 H  HB3  . LYS   B  2  75  ? 4.765   -37.953 32.482   1.00 127.17 ? 79   LYS   B HB3  1 
ATOM   10095 H  HG2  . LYS   B  2  75  ? 5.712   -40.075 32.436   1.00 126.27 ? 79   LYS   B HG2  1 
ATOM   10096 H  HG3  . LYS   B  2  75  ? 6.980   -39.532 33.225   1.00 126.27 ? 79   LYS   B HG3  1 
ATOM   10097 H  HD2  . LYS   B  2  75  ? 5.627   -39.080 35.081   1.00 129.63 ? 79   LYS   B HD2  1 
ATOM   10098 H  HD3  . LYS   B  2  75  ? 4.363   -39.633 34.292   1.00 129.63 ? 79   LYS   B HD3  1 
ATOM   10099 H  HE2  . LYS   B  2  75  ? 5.298   -41.766 34.276   1.00 129.94 ? 79   LYS   B HE2  1 
ATOM   10100 H  HE3  . LYS   B  2  75  ? 6.574   -41.217 35.047   1.00 129.94 ? 79   LYS   B HE3  1 
ATOM   10101 H  HZ1  . LYS   B  2  75  ? 5.136   -42.227 36.494   1.00 135.64 ? 79   LYS   B HZ1  1 
ATOM   10102 H  HZ2  . LYS   B  2  75  ? 5.237   -40.825 36.846   1.00 135.64 ? 79   LYS   B HZ2  1 
ATOM   10103 H  HZ3  . LYS   B  2  75  ? 4.068   -41.314 36.143   1.00 135.64 ? 79   LYS   B HZ3  1 
ATOM   10104 N  N    . ASN   B  2  76  ? 6.529   -35.236 30.852   1.00 104.53 ? 80   ASN   B N    1 
ATOM   10105 C  CA   . ASN   B  2  76  ? 6.040   -33.933 30.424   1.00 107.66 ? 80   ASN   B CA   1 
ATOM   10106 C  C    . ASN   B  2  76  ? 6.937   -33.392 29.321   1.00 105.04 ? 80   ASN   B C    1 
ATOM   10107 O  O    . ASN   B  2  76  ? 8.157   -33.298 29.496   1.00 102.02 ? 80   ASN   B O    1 
ATOM   10108 C  CB   . ASN   B  2  76  ? 5.991   -32.956 31.601   1.00 112.07 ? 80   ASN   B CB   1 
ATOM   10109 C  CG   . ASN   B  2  76  ? 5.611   -31.555 31.178   1.00 118.19 ? 80   ASN   B CG   1 
ATOM   10110 O  OD1  . ASN   B  2  76  ? 6.416   -30.630 31.273   1.00 118.98 ? 80   ASN   B OD1  1 
ATOM   10111 N  ND2  . ASN   B  2  76  ? 4.383   -31.391 30.697   1.00 123.06 ? 80   ASN   B ND2  1 
ATOM   10112 H  H    . ASN   B  2  76  ? 7.327   -35.211 31.173   1.00 125.47 ? 80   ASN   B H    1 
ATOM   10113 H  HA   . ASN   B  2  76  ? 5.144   -34.023 30.064   1.00 129.23 ? 80   ASN   B HA   1 
ATOM   10114 H  HB2  . ASN   B  2  76  ? 5.332   -33.265 32.242   1.00 134.52 ? 80   ASN   B HB2  1 
ATOM   10115 H  HB3  . ASN   B  2  76  ? 6.866   -32.917 32.017   1.00 134.52 ? 80   ASN   B HB3  1 
ATOM   10116 H  HD21 . ASN   B  2  76  ? 4.121   -30.612 30.444   1.00 147.71 ? 80   ASN   B HD21 1 
ATOM   10117 H  HD22 . ASN   B  2  76  ? 3.851   -32.064 30.640   1.00 147.71 ? 80   ASN   B HD22 1 
ATOM   10118 N  N    . SER   B  2  77  ? 6.328   -33.032 28.188   1.00 91.51  ? 81   SER   B N    1 
ATOM   10119 C  CA   . SER   B  2  77  ? 7.102   -32.557 27.046   1.00 92.97  ? 81   SER   B CA   1 
ATOM   10120 C  C    . SER   B  2  77  ? 7.890   -31.297 27.377   1.00 93.44  ? 81   SER   B C    1 
ATOM   10121 O  O    . SER   B  2  77  ? 8.925   -31.032 26.753   1.00 90.48  ? 81   SER   B O    1 
ATOM   10122 C  CB   . SER   B  2  77  ? 6.173   -32.292 25.859   1.00 94.71  ? 81   SER   B CB   1 
ATOM   10123 O  OG   . SER   B  2  77  ? 5.590   -33.492 25.384   1.00 94.43  ? 81   SER   B OG   1 
ATOM   10124 H  H    . SER   B  2  77  ? 5.478   -33.054 28.058   1.00 109.85 ? 81   SER   B H    1 
ATOM   10125 H  HA   . SER   B  2  77  ? 7.733   -33.249 26.794   1.00 111.60 ? 81   SER   B HA   1 
ATOM   10126 H  HB2  . SER   B  2  77  ? 5.466   -31.690 26.142   1.00 113.68 ? 81   SER   B HB2  1 
ATOM   10127 H  HB3  . SER   B  2  77  ? 6.686   -31.887 25.143   1.00 113.68 ? 81   SER   B HB3  1 
ATOM   10128 H  HG   . SER   B  2  77  ? 5.115   -33.334 24.709   1.00 113.35 ? 81   SER   B HG   1 
ATOM   10129 N  N    . SER   B  2  78  ? 7.425   -30.513 28.351   1.00 97.08  ? 82   SER   B N    1 
ATOM   10130 C  CA   . SER   B  2  78  ? 8.030   -29.218 28.630   1.00 98.16  ? 82   SER   B CA   1 
ATOM   10131 C  C    . SER   B  2  78  ? 9.334   -29.325 29.408   1.00 94.98  ? 82   SER   B C    1 
ATOM   10132 O  O    . SER   B  2  78  ? 10.098  -28.354 29.443   1.00 95.20  ? 82   SER   B O    1 
ATOM   10133 C  CB   . SER   B  2  78  ? 7.044   -28.343 29.407   1.00 104.37 ? 82   SER   B CB   1 
ATOM   10134 O  OG   . SER   B  2  78  ? 5.723   -28.535 28.932   1.00 108.44 ? 82   SER   B OG   1 
ATOM   10135 H  H    . SER   B  2  78  ? 6.762   -30.711 28.861   1.00 116.53 ? 82   SER   B H    1 
ATOM   10136 H  HA   . SER   B  2  78  ? 8.228   -28.781 27.787   1.00 117.83 ? 82   SER   B HA   1 
ATOM   10137 H  HB2  . SER   B  2  78  ? 7.080   -28.583 30.346   1.00 125.28 ? 82   SER   B HB2  1 
ATOM   10138 H  HB3  . SER   B  2  78  ? 7.289   -27.412 29.292   1.00 125.28 ? 82   SER   B HB3  1 
ATOM   10139 H  HG   . SER   B  2  78  ? 5.195   -28.020 29.334   1.00 130.16 ? 82   SER   B HG   1 
ATOM   10140 N  N    . ASP   B  2  79  ? 9.606   -30.471 30.029   1.00 94.37  ? 83   ASP   B N    1 
ATOM   10141 C  CA   . ASP   B  2  79  ? 10.825  -30.673 30.799   1.00 95.00  ? 83   ASP   B CA   1 
ATOM   10142 C  C    . ASP   B  2  79  ? 11.897  -31.413 30.010   1.00 93.43  ? 83   ASP   B C    1 
ATOM   10143 O  O    . ASP   B  2  79  ? 12.936  -31.767 30.576   1.00 94.60  ? 83   ASP   B O    1 
ATOM   10144 C  CB   . ASP   B  2  79  ? 10.506  -31.423 32.092   1.00 96.58  ? 83   ASP   B CB   1 
ATOM   10145 C  CG   . ASP   B  2  79  ? 9.601   -30.630 33.013   1.00 106.25 ? 83   ASP   B CG   1 
ATOM   10146 O  OD1  . ASP   B  2  79  ? 9.689   -29.383 33.002   1.00 107.97 ? 83   ASP   B OD1  1 
ATOM   10147 O  OD2  . ASP   B  2  79  ? 8.799   -31.249 33.743   1.00 110.32 ? 83   ASP   B OD2  1 
ATOM   10148 H  H    . ASP   B  2  79  ? 9.089   -31.157 30.017   1.00 113.28 ? 83   ASP   B H    1 
ATOM   10149 H  HA   . ASP   B  2  79  ? 11.187  -29.806 31.041   1.00 114.04 ? 83   ASP   B HA   1 
ATOM   10150 H  HB2  . ASP   B  2  79  ? 10.059  -32.256 31.874   1.00 115.93 ? 83   ASP   B HB2  1 
ATOM   10151 H  HB3  . ASP   B  2  79  ? 11.333  -31.605 32.566   1.00 115.93 ? 83   ASP   B HB3  1 
ATOM   10152 N  N    . ILE   B  2  80  ? 11.668  -31.657 28.724   1.00 87.72  ? 84   ILE   B N    1 
ATOM   10153 C  CA   . ILE   B  2  80  ? 12.698  -32.218 27.858   1.00 79.28  ? 84   ILE   B CA   1 
ATOM   10154 C  C    . ILE   B  2  80  ? 13.706  -31.126 27.533   1.00 73.59  ? 84   ILE   B C    1 
ATOM   10155 O  O    . ILE   B  2  80  ? 13.334  -30.019 27.125   1.00 73.65  ? 84   ILE   B O    1 
ATOM   10156 C  CB   . ILE   B  2  80  ? 12.080  -32.803 26.577   1.00 74.25  ? 84   ILE   B CB   1 
ATOM   10157 C  CG1  . ILE   B  2  80  ? 11.275  -34.063 26.909   1.00 72.57  ? 84   ILE   B CG1  1 
ATOM   10158 C  CG2  . ILE   B  2  80  ? 13.169  -33.106 25.544   1.00 68.41  ? 84   ILE   B CG2  1 
ATOM   10159 C  CD1  . ILE   B  2  80  ? 10.505  -34.637 25.734   1.00 67.57  ? 84   ILE   B CD1  1 
ATOM   10160 H  H    . ILE   B  2  80  ? 10.921  -31.505 28.326   1.00 105.31 ? 84   ILE   B H    1 
ATOM   10161 H  HA   . ILE   B  2  80  ? 13.155  -32.935 28.325   1.00 95.17  ? 84   ILE   B HA   1 
ATOM   10162 H  HB   . ILE   B  2  80  ? 11.478  -32.145 26.196   1.00 89.14  ? 84   ILE   B HB   1 
ATOM   10163 H  HG12 . ILE   B  2  80  ? 11.886  -34.747 27.223   1.00 87.12  ? 84   ILE   B HG12 1 
ATOM   10164 H  HG13 . ILE   B  2  80  ? 10.633  -33.846 27.604   1.00 87.12  ? 84   ILE   B HG13 1 
ATOM   10165 H  HG21 . ILE   B  2  80  ? 12.761  -33.517 24.766   1.00 82.13  ? 84   ILE   B HG21 1 
ATOM   10166 H  HG22 . ILE   B  2  80  ? 13.603  -32.276 25.290   1.00 82.13  ? 84   ILE   B HG22 1 
ATOM   10167 H  HG23 . ILE   B  2  80  ? 13.817  -33.711 25.936   1.00 82.13  ? 84   ILE   B HG23 1 
ATOM   10168 H  HD11 . ILE   B  2  80  ? 10.017  -35.422 26.030   1.00 81.12  ? 84   ILE   B HD11 1 
ATOM   10169 H  HD12 . ILE   B  2  80  ? 9.886   -33.967 25.405   1.00 81.12  ? 84   ILE   B HD12 1 
ATOM   10170 H  HD13 . ILE   B  2  80  ? 11.131  -34.881 25.035   1.00 81.12  ? 84   ILE   B HD13 1 
ATOM   10171 N  N    . VAL   B  2  81  ? 14.987  -31.436 27.713   1.00 69.67  ? 85   VAL   B N    1 
ATOM   10172 C  CA   . VAL   B  2  81  ? 16.077  -30.523 27.389   1.00 66.62  ? 85   VAL   B CA   1 
ATOM   10173 C  C    . VAL   B  2  81  ? 17.133  -31.349 26.670   1.00 62.92  ? 85   VAL   B C    1 
ATOM   10174 O  O    . VAL   B  2  81  ? 17.795  -32.190 27.290   1.00 63.44  ? 85   VAL   B O    1 
ATOM   10175 C  CB   . VAL   B  2  81  ? 16.670  -29.843 28.631   1.00 64.65  ? 85   VAL   B CB   1 
ATOM   10176 C  CG1  . VAL   B  2  81  ? 17.775  -28.871 28.232   1.00 65.64  ? 85   VAL   B CG1  1 
ATOM   10177 C  CG2  . VAL   B  2  81  ? 15.578  -29.128 29.410   1.00 60.89  ? 85   VAL   B CG2  1 
ATOM   10178 H  H    . VAL   B  2  81  ? 15.255  -32.189 28.029   1.00 83.65  ? 85   VAL   B H    1 
ATOM   10179 H  HA   . VAL   B  2  81  ? 15.760  -29.828 26.792   1.00 79.98  ? 85   VAL   B HA   1 
ATOM   10180 H  HB   . VAL   B  2  81  ? 17.060  -30.519 29.207   1.00 77.62  ? 85   VAL   B HB   1 
ATOM   10181 H  HG11 . VAL   B  2  81  ? 18.123  -28.443 29.031   1.00 78.81  ? 85   VAL   B HG11 1 
ATOM   10182 H  HG12 . VAL   B  2  81  ? 18.482  -29.362 27.786   1.00 78.81  ? 85   VAL   B HG12 1 
ATOM   10183 H  HG13 . VAL   B  2  81  ? 17.407  -28.203 27.633   1.00 78.81  ? 85   VAL   B HG13 1 
ATOM   10184 H  HG21 . VAL   B  2  81  ? 15.973  -28.691 30.181   1.00 73.11  ? 85   VAL   B HG21 1 
ATOM   10185 H  HG22 . VAL   B  2  81  ? 15.159  -28.469 28.835   1.00 73.11  ? 85   VAL   B HG22 1 
ATOM   10186 H  HG23 . VAL   B  2  81  ? 14.919  -29.779 29.701   1.00 73.11  ? 85   VAL   B HG23 1 
ATOM   10187 N  N    . GLN   B  2  82  ? 17.285  -31.123 25.366   1.00 57.32  ? 86   GLN   B N    1 
ATOM   10188 C  CA   . GLN   B  2  82  ? 18.212  -31.893 24.552   1.00 56.44  ? 86   GLN   B CA   1 
ATOM   10189 C  C    . GLN   B  2  82  ? 19.447  -31.109 24.133   1.00 57.37  ? 86   GLN   B C    1 
ATOM   10190 O  O    . GLN   B  2  82  ? 20.385  -31.711 23.602   1.00 58.96  ? 86   GLN   B O    1 
ATOM   10191 C  CB   . GLN   B  2  82  ? 17.495  -32.427 23.301   1.00 56.99  ? 86   GLN   B CB   1 
ATOM   10192 C  CG   . GLN   B  2  82  ? 16.267  -33.280 23.611   1.00 60.89  ? 86   GLN   B CG   1 
ATOM   10193 C  CD   . GLN   B  2  82  ? 15.723  -34.002 22.391   1.00 61.83  ? 86   GLN   B CD   1 
ATOM   10194 O  OE1  . GLN   B  2  82  ? 15.936  -35.203 22.222   1.00 60.31  ? 86   GLN   B OE1  1 
ATOM   10195 N  NE2  . GLN   B  2  82  ? 15.009  -33.275 21.539   1.00 63.79  ? 86   GLN   B NE2  1 
ATOM   10196 H  H    . GLN   B  2  82  ? 16.856  -30.520 24.928   1.00 68.82  ? 86   GLN   B H    1 
ATOM   10197 H  HA   . GLN   B  2  82  ? 18.516  -32.657 25.067   1.00 67.77  ? 86   GLN   B HA   1 
ATOM   10198 H  HB2  . GLN   B  2  82  ? 17.205  -31.674 22.763   1.00 68.43  ? 86   GLN   B HB2  1 
ATOM   10199 H  HB3  . GLN   B  2  82  ? 18.117  -32.975 22.796   1.00 68.43  ? 86   GLN   B HB3  1 
ATOM   10200 H  HG2  . GLN   B  2  82  ? 16.506  -33.948 24.272   1.00 73.11  ? 86   GLN   B HG2  1 
ATOM   10201 H  HG3  . GLN   B  2  82  ? 15.565  -32.707 23.956   1.00 73.11  ? 86   GLN   B HG3  1 
ATOM   10202 H  HE21 . GLN   B  2  82  ? 14.877  -32.440 21.692   1.00 76.59  ? 86   GLN   B HE21 1 
ATOM   10203 H  HE22 . GLN   B  2  82  ? 14.680  -33.640 20.833   1.00 76.59  ? 86   GLN   B HE22 1 
ATOM   10204 N  N    . ILE   B  2  83  ? 19.479  -29.796 24.356   1.00 54.45  ? 87   ILE   B N    1 
ATOM   10205 C  CA   . ILE   B  2  83  ? 20.648  -28.973 24.063   1.00 53.35  ? 87   ILE   B CA   1 
ATOM   10206 C  C    . ILE   B  2  83  ? 20.841  -27.986 25.207   1.00 58.16  ? 87   ILE   B C    1 
ATOM   10207 O  O    . ILE   B  2  83  ? 19.867  -27.457 25.754   1.00 62.29  ? 87   ILE   B O    1 
ATOM   10208 C  CB   . ILE   B  2  83  ? 20.506  -28.234 22.715   1.00 48.31  ? 87   ILE   B CB   1 
ATOM   10209 C  CG1  . ILE   B  2  83  ? 21.857  -27.658 22.278   1.00 46.38  ? 87   ILE   B CG1  1 
ATOM   10210 C  CG2  . ILE   B  2  83  ? 19.469  -27.122 22.818   1.00 47.29  ? 87   ILE   B CG2  1 
ATOM   10211 C  CD1  . ILE   B  2  83  ? 21.857  -27.077 20.874   1.00 46.43  ? 87   ILE   B CD1  1 
ATOM   10212 H  H    . ILE   B  2  83  ? 18.821  -29.350 24.685   1.00 65.38  ? 87   ILE   B H    1 
ATOM   10213 H  HA   . ILE   B  2  83  ? 21.433  -29.541 24.012   1.00 64.06  ? 87   ILE   B HA   1 
ATOM   10214 H  HB   . ILE   B  2  83  ? 20.209  -28.874 22.050   1.00 58.01  ? 87   ILE   B HB   1 
ATOM   10215 H  HG12 . ILE   B  2  83  ? 22.104  -26.947 22.891   1.00 55.70  ? 87   ILE   B HG12 1 
ATOM   10216 H  HG13 . ILE   B  2  83  ? 22.520  -28.365 22.305   1.00 55.70  ? 87   ILE   B HG13 1 
ATOM   10217 H  HG21 . ILE   B  2  83  ? 19.304  -26.760 21.933   1.00 56.79  ? 87   ILE   B HG21 1 
ATOM   10218 H  HG22 . ILE   B  2  83  ? 18.648  -27.488 23.184   1.00 56.79  ? 87   ILE   B HG22 1 
ATOM   10219 H  HG23 . ILE   B  2  83  ? 19.809  -26.426 23.402   1.00 56.79  ? 87   ILE   B HG23 1 
ATOM   10220 H  HD11 . ILE   B  2  83  ? 22.739  -26.721 20.680   1.00 55.75  ? 87   ILE   B HD11 1 
ATOM   10221 H  HD12 . ILE   B  2  83  ? 21.638  -27.780 20.242   1.00 55.75  ? 87   ILE   B HD12 1 
ATOM   10222 H  HD13 . ILE   B  2  83  ? 21.196  -26.369 20.824   1.00 55.75  ? 87   ILE   B HD13 1 
ATOM   10223 N  N    . ALA   B  2  84  ? 22.103  -27.738 25.569   1.00 57.43  ? 88   ALA   B N    1 
ATOM   10224 C  CA   . ALA   B  2  84  ? 22.435  -26.800 26.634   1.00 56.71  ? 88   ALA   B CA   1 
ATOM   10225 C  C    . ALA   B  2  84  ? 23.805  -26.201 26.342   1.00 58.50  ? 88   ALA   B C    1 
ATOM   10226 O  O    . ALA   B  2  84  ? 24.727  -26.951 25.985   1.00 62.45  ? 88   ALA   B O    1 
ATOM   10227 C  CB   . ALA   B  2  84  ? 22.442  -27.476 28.006   1.00 54.27  ? 88   ALA   B CB   1 
ATOM   10228 H  H    . ALA   B  2  84  ? 22.789  -28.107 25.205   1.00 68.95  ? 88   ALA   B H    1 
ATOM   10229 H  HA   . ALA   B  2  84  ? 21.782  -26.083 26.640   1.00 68.09  ? 88   ALA   B HA   1 
ATOM   10230 H  HB1  . ALA   B  2  84  ? 22.677  -26.820 28.680   1.00 65.16  ? 88   ALA   B HB1  1 
ATOM   10231 H  HB2  . ALA   B  2  84  ? 21.558  -27.834 28.187   1.00 65.16  ? 88   ALA   B HB2  1 
ATOM   10232 H  HB3  . ALA   B  2  84  ? 23.094  -28.194 28.001   1.00 65.16  ? 88   ALA   B HB3  1 
ATOM   10233 N  N    . PRO   B  2  85  ? 23.984  -24.873 26.480   1.00 59.38  ? 89   PRO   B N    1 
ATOM   10234 C  CA   . PRO   B  2  85  ? 23.003  -23.873 26.922   1.00 62.95  ? 89   PRO   B CA   1 
ATOM   10235 C  C    . PRO   B  2  85  ? 21.887  -23.676 25.903   1.00 62.04  ? 89   PRO   B C    1 
ATOM   10236 O  O    . PRO   B  2  85  ? 21.876  -24.351 24.874   1.00 59.06  ? 89   PRO   B O    1 
ATOM   10237 C  CB   . PRO   B  2  85  ? 23.834  -22.588 27.069   1.00 63.67  ? 89   PRO   B CB   1 
ATOM   10238 C  CG   . PRO   B  2  85  ? 25.269  -23.000 26.928   1.00 62.73  ? 89   PRO   B CG   1 
ATOM   10239 C  CD   . PRO   B  2  85  ? 25.262  -24.245 26.111   1.00 60.27  ? 89   PRO   B CD   1 
ATOM   10240 H  HA   . PRO   B  2  85  ? 22.627  -24.114 27.783   1.00 75.58  ? 89   PRO   B HA   1 
ATOM   10241 H  HB2  . PRO   B  2  85  ? 23.588  -21.960 26.372   1.00 76.44  ? 89   PRO   B HB2  1 
ATOM   10242 H  HB3  . PRO   B  2  85  ? 23.674  -22.195 27.941   1.00 76.44  ? 89   PRO   B HB3  1 
ATOM   10243 H  HG2  . PRO   B  2  85  ? 25.768  -22.299 26.480   1.00 75.32  ? 89   PRO   B HG2  1 
ATOM   10244 H  HG3  . PRO   B  2  85  ? 25.648  -23.168 27.805   1.00 75.32  ? 89   PRO   B HG3  1 
ATOM   10245 H  HD2  . PRO   B  2  85  ? 25.286  -24.039 25.164   1.00 72.36  ? 89   PRO   B HD2  1 
ATOM   10246 H  HD3  . PRO   B  2  85  ? 26.010  -24.818 26.345   1.00 72.36  ? 89   PRO   B HD3  1 
ATOM   10247 N  N    . GLN   B  2  86  ? 20.962  -22.761 26.191   1.00 63.44  ? 90   GLN   B N    1 
ATOM   10248 C  CA   . GLN   B  2  86  ? 19.854  -22.477 25.295   1.00 64.10  ? 90   GLN   B CA   1 
ATOM   10249 C  C    . GLN   B  2  86  ? 19.798  -21.025 24.843   1.00 64.41  ? 90   GLN   B C    1 
ATOM   10250 O  O    . GLN   B  2  86  ? 19.035  -20.715 23.922   1.00 65.85  ? 90   GLN   B O    1 
ATOM   10251 C  CB   . GLN   B  2  86  ? 18.518  -22.848 25.959   1.00 66.95  ? 90   GLN   B CB   1 
ATOM   10252 C  CG   . GLN   B  2  86  ? 18.411  -24.315 26.365   1.00 68.47  ? 90   GLN   B CG   1 
ATOM   10253 C  CD   . GLN   B  2  86  ? 18.857  -24.572 27.795   1.00 73.48  ? 90   GLN   B CD   1 
ATOM   10254 O  OE1  . GLN   B  2  86  ? 18.879  -23.662 28.625   1.00 73.87  ? 90   GLN   B OE1  1 
ATOM   10255 N  NE2  . GLN   B  2  86  ? 19.212  -25.818 28.089   1.00 74.42  ? 90   GLN   B NE2  1 
ATOM   10256 H  H    . GLN   B  2  86  ? 20.958  -22.289 26.910   1.00 76.17  ? 90   GLN   B H    1 
ATOM   10257 H  HA   . GLN   B  2  86  ? 19.947  -23.028 24.502   1.00 76.96  ? 90   GLN   B HA   1 
ATOM   10258 H  HB2  . GLN   B  2  86  ? 18.410  -22.311 26.761   1.00 80.37  ? 90   GLN   B HB2  1 
ATOM   10259 H  HB3  . GLN   B  2  86  ? 17.798  -22.661 25.336   1.00 80.37  ? 90   GLN   B HB3  1 
ATOM   10260 H  HG2  . GLN   B  2  86  ? 17.487  -24.598 26.286   1.00 82.20  ? 90   GLN   B HG2  1 
ATOM   10261 H  HG3  . GLN   B  2  86  ? 18.972  -24.846 25.778   1.00 82.20  ? 90   GLN   B HG3  1 
ATOM   10262 H  HE21 . GLN   B  2  86  ? 19.182  -26.428 27.484   1.00 89.34  ? 90   GLN   B HE21 1 
ATOM   10263 H  HE22 . GLN   B  2  86  ? 19.472  -26.014 28.885   1.00 89.34  ? 90   GLN   B HE22 1 
ATOM   10264 N  N    . SER   B  2  87  ? 20.576  -20.134 25.455   1.00 67.42  ? 91   SER   B N    1 
ATOM   10265 C  CA   . SER   B  2  87  ? 20.635  -18.743 25.023   1.00 70.03  ? 91   SER   B CA   1 
ATOM   10266 C  C    . SER   B  2  87  ? 21.951  -18.147 25.498   1.00 71.29  ? 91   SER   B C    1 
ATOM   10267 O  O    . SER   B  2  87  ? 22.284  -18.244 26.683   1.00 69.32  ? 91   SER   B O    1 
ATOM   10268 C  CB   . SER   B  2  87  ? 19.452  -17.941 25.572   1.00 70.78  ? 91   SER   B CB   1 
ATOM   10269 O  OG   . SER   B  2  87  ? 19.421  -16.636 25.020   1.00 71.56  ? 91   SER   B OG   1 
ATOM   10270 H  H    . SER   B  2  87  ? 21.083  -20.314 26.126   1.00 80.94  ? 91   SER   B H    1 
ATOM   10271 H  HA   . SER   B  2  87  ? 20.606  -18.700 24.055   1.00 84.07  ? 91   SER   B HA   1 
ATOM   10272 H  HB2  . SER   B  2  87  ? 18.628  -18.399 25.344   1.00 84.97  ? 91   SER   B HB2  1 
ATOM   10273 H  HB3  . SER   B  2  87  ? 19.537  -17.873 26.536   1.00 84.97  ? 91   SER   B HB3  1 
ATOM   10274 H  HG   . SER   B  2  87  ? 18.766  -16.209 25.327   1.00 85.91  ? 91   SER   B HG   1 
ATOM   10275 N  N    . LEU   B  2  88  ? 22.692  -17.537 24.575   1.00 71.86  ? 92   LEU   B N    1 
ATOM   10276 C  CA   . LEU   B  2  88  ? 23.984  -16.945 24.881   1.00 72.86  ? 92   LEU   B CA   1 
ATOM   10277 C  C    . LEU   B  2  88  ? 24.084  -15.571 24.234   1.00 76.20  ? 92   LEU   B C    1 
ATOM   10278 O  O    . LEU   B  2  88  ? 23.412  -15.277 23.242   1.00 74.67  ? 92   LEU   B O    1 
ATOM   10279 C  CB   . LEU   B  2  88  ? 25.146  -17.819 24.384   1.00 69.11  ? 92   LEU   B CB   1 
ATOM   10280 C  CG   . LEU   B  2  88  ? 25.340  -19.202 25.005   1.00 69.55  ? 92   LEU   B CG   1 
ATOM   10281 C  CD1  . LEU   B  2  88  ? 26.431  -19.960 24.268   1.00 63.79  ? 92   LEU   B CD1  1 
ATOM   10282 C  CD2  . LEU   B  2  88  ? 25.686  -19.079 26.470   1.00 76.19  ? 92   LEU   B CD2  1 
ATOM   10283 H  H    . LEU   B  2  88  ? 22.460  -17.453 23.751   1.00 86.27  ? 92   LEU   B H    1 
ATOM   10284 H  HA   . LEU   B  2  88  ? 24.056  -16.843 25.843   1.00 87.47  ? 92   LEU   B HA   1 
ATOM   10285 H  HB2  . LEU   B  2  88  ? 25.019  -17.960 23.432   1.00 82.97  ? 92   LEU   B HB2  1 
ATOM   10286 H  HB3  . LEU   B  2  88  ? 25.968  -17.328 24.540   1.00 82.97  ? 92   LEU   B HB3  1 
ATOM   10287 H  HG   . LEU   B  2  88  ? 24.513  -19.703 24.930   1.00 83.50  ? 92   LEU   B HG   1 
ATOM   10288 H  HD11 . LEU   B  2  88  ? 26.556  -20.824 24.690   1.00 76.59  ? 92   LEU   B HD11 1 
ATOM   10289 H  HD12 . LEU   B  2  88  ? 26.164  -20.079 23.343   1.00 76.59  ? 92   LEU   B HD12 1 
ATOM   10290 H  HD13 . LEU   B  2  88  ? 27.255  -19.449 24.311   1.00 76.59  ? 92   LEU   B HD13 1 
ATOM   10291 H  HD21 . LEU   B  2  88  ? 25.866  -19.963 26.827   1.00 91.46  ? 92   LEU   B HD21 1 
ATOM   10292 H  HD22 . LEU   B  2  88  ? 26.472  -18.519 26.563   1.00 91.46  ? 92   LEU   B HD22 1 
ATOM   10293 H  HD23 . LEU   B  2  88  ? 24.937  -18.679 26.939   1.00 91.46  ? 92   LEU   B HD23 1 
ATOM   10294 N  N    . ILE   B  2  89  ? 24.935  -14.730 24.814   1.00 80.34  ? 93   ILE   B N    1 
ATOM   10295 C  CA   . ILE   B  2  89  ? 25.389  -13.495 24.188   1.00 83.69  ? 93   ILE   B CA   1 
ATOM   10296 C  C    . ILE   B  2  89  ? 26.882  -13.633 23.943   1.00 79.15  ? 93   ILE   B C    1 
ATOM   10297 O  O    . ILE   B  2  89  ? 27.630  -14.020 24.849   1.00 80.04  ? 93   ILE   B O    1 
ATOM   10298 C  CB   . ILE   B  2  89  ? 25.107  -12.254 25.055   1.00 93.32  ? 93   ILE   B CB   1 
ATOM   10299 C  CG1  . ILE   B  2  89  ? 23.603  -12.059 25.257   1.00 98.17  ? 93   ILE   B CG1  1 
ATOM   10300 C  CG2  . ILE   B  2  89  ? 25.743  -11.017 24.419   1.00 96.57  ? 93   ILE   B CG2  1 
ATOM   10301 C  CD1  . ILE   B  2  89  ? 22.867  -11.548 24.037   1.00 99.72  ? 93   ILE   B CD1  1 
ATOM   10302 H  H    . ILE   B  2  89  ? 25.273  -14.859 25.595   1.00 96.44  ? 93   ILE   B H    1 
ATOM   10303 H  HA   . ILE   B  2  89  ? 24.925  -13.378 23.344   1.00 100.47 ? 93   ILE   B HA   1 
ATOM   10304 H  HB   . ILE   B  2  89  ? 25.504  -12.392 25.929   1.00 112.02 ? 93   ILE   B HB   1 
ATOM   10305 H  HG12 . ILE   B  2  89  ? 23.210  -12.912 25.500   1.00 117.84 ? 93   ILE   B HG12 1 
ATOM   10306 H  HG13 . ILE   B  2  89  ? 23.468  -11.416 25.972   1.00 117.84 ? 93   ILE   B HG13 1 
ATOM   10307 H  HG21 . ILE   B  2  89  ? 25.472  -10.231 24.918   1.00 115.92 ? 93   ILE   B HG21 1 
ATOM   10308 H  HG22 . ILE   B  2  89  ? 26.708  -11.109 24.446   1.00 115.92 ? 93   ILE   B HG22 1 
ATOM   10309 H  HG23 . ILE   B  2  89  ? 25.443  -10.944 23.500   1.00 115.92 ? 93   ILE   B HG23 1 
ATOM   10310 H  HD11 . ILE   B  2  89  ? 21.921  -11.484 24.243   1.00 119.71 ? 93   ILE   B HD11 1 
ATOM   10311 H  HD12 . ILE   B  2  89  ? 23.214  -10.673 23.803   1.00 119.71 ? 93   ILE   B HD12 1 
ATOM   10312 H  HD13 . ILE   B  2  89  ? 23.005  -12.166 23.303   1.00 119.71 ? 93   ILE   B HD13 1 
ATOM   10313 N  N    . LEU   B  2  90  ? 27.314  -13.310 22.730   1.00 77.91  ? 94   LEU   B N    1 
ATOM   10314 C  CA   . LEU   B  2  90  ? 28.717  -13.404 22.347   1.00 77.01  ? 94   LEU   B CA   1 
ATOM   10315 C  C    . LEU   B  2  90  ? 29.182  -12.033 21.875   1.00 79.81  ? 94   LEU   B C    1 
ATOM   10316 O  O    . LEU   B  2  90  ? 28.815  -11.589 20.782   1.00 80.10  ? 94   LEU   B O    1 
ATOM   10317 C  CB   . LEU   B  2  90  ? 28.913  -14.463 21.264   1.00 73.68  ? 94   LEU   B CB   1 
ATOM   10318 C  CG   . LEU   B  2  90  ? 30.348  -14.823 20.879   1.00 73.53  ? 94   LEU   B CG   1 
ATOM   10319 C  CD1  . LEU   B  2  90  ? 31.156  -15.257 22.085   1.00 74.57  ? 94   LEU   B CD1  1 
ATOM   10320 C  CD2  . LEU   B  2  90  ? 30.322  -15.928 19.839   1.00 72.45  ? 94   LEU   B CD2  1 
ATOM   10321 H  H    . LEU   B  2  90  ? 26.802  -13.027 22.099   1.00 93.52  ? 94   LEU   B H    1 
ATOM   10322 H  HA   . LEU   B  2  90  ? 29.250  -13.653 23.118   1.00 92.45  ? 94   LEU   B HA   1 
ATOM   10323 H  HB2  . LEU   B  2  90  ? 28.491  -15.281 21.569   1.00 88.45  ? 94   LEU   B HB2  1 
ATOM   10324 H  HB3  . LEU   B  2  90  ? 28.477  -14.145 20.457   1.00 88.45  ? 94   LEU   B HB3  1 
ATOM   10325 H  HG   . LEU   B  2  90  ? 30.783  -14.039 20.510   1.00 88.27  ? 94   LEU   B HG   1 
ATOM   10326 H  HD11 . LEU   B  2  90  ? 32.058  -15.472 21.800   1.00 89.52  ? 94   LEU   B HD11 1 
ATOM   10327 H  HD12 . LEU   B  2  90  ? 31.177  -14.532 22.729   1.00 89.52  ? 94   LEU   B HD12 1 
ATOM   10328 H  HD13 . LEU   B  2  90  ? 30.739  -16.039 22.480   1.00 89.52  ? 94   LEU   B HD13 1 
ATOM   10329 H  HD21 . LEU   B  2  90  ? 31.233  -16.173 19.617   1.00 86.97  ? 94   LEU   B HD21 1 
ATOM   10330 H  HD22 . LEU   B  2  90  ? 29.853  -16.694 20.204   1.00 86.97  ? 94   LEU   B HD22 1 
ATOM   10331 H  HD23 . LEU   B  2  90  ? 29.863  -15.606 19.047   1.00 86.97  ? 94   LEU   B HD23 1 
ATOM   10332 N  N    . LYS   B  2  91  ? 29.976  -11.364 22.707   1.00 82.80  ? 95   LYS   B N    1 
ATOM   10333 C  CA   . LYS   B  2  91  ? 30.614  -10.105 22.342   1.00 85.91  ? 95   LYS   B CA   1 
ATOM   10334 C  C    . LYS   B  2  91  ? 31.996  -10.430 21.788   1.00 85.03  ? 95   LYS   B C    1 
ATOM   10335 O  O    . LYS   B  2  91  ? 32.867  -10.904 22.522   1.00 84.74  ? 95   LYS   B O    1 
ATOM   10336 C  CB   . LYS   B  2  91  ? 30.715  -9.178  23.548   1.00 91.09  ? 95   LYS   B CB   1 
ATOM   10337 C  CG   . LYS   B  2  91  ? 29.387  -8.700  24.099   1.00 93.95  ? 95   LYS   B CG   1 
ATOM   10338 C  CD   . LYS   B  2  91  ? 29.623  -7.714  25.227   1.00 101.56 ? 95   LYS   B CD   1 
ATOM   10339 C  CE   . LYS   B  2  91  ? 28.354  -7.398  25.991   1.00 108.90 ? 95   LYS   B CE   1 
ATOM   10340 N  NZ   . LYS   B  2  91  ? 28.649  -6.563  27.187   1.00 115.93 ? 95   LYS   B NZ   1 
ATOM   10341 H  H    . LYS   B  2  91  ? 30.163  -11.625 23.504   1.00 99.40  ? 95   LYS   B H    1 
ATOM   10342 H  HA   . LYS   B  2  91  ? 30.091  -9.656  21.660   1.00 103.13 ? 95   LYS   B HA   1 
ATOM   10343 H  HB2  . LYS   B  2  91  ? 31.173  -9.650  24.261   1.00 109.34 ? 95   LYS   B HB2  1 
ATOM   10344 H  HB3  . LYS   B  2  91  ? 31.223  -8.393  23.290   1.00 109.34 ? 95   LYS   B HB3  1 
ATOM   10345 H  HG2  . LYS   B  2  91  ? 28.882  -8.257  23.398   1.00 112.78 ? 95   LYS   B HG2  1 
ATOM   10346 H  HG3  . LYS   B  2  91  ? 28.884  -9.455  24.443   1.00 112.78 ? 95   LYS   B HG3  1 
ATOM   10347 H  HD2  . LYS   B  2  91  ? 30.264  -8.091  25.850   1.00 121.91 ? 95   LYS   B HD2  1 
ATOM   10348 H  HD3  . LYS   B  2  91  ? 29.967  -6.885  24.859   1.00 121.91 ? 95   LYS   B HD3  1 
ATOM   10349 H  HE2  . LYS   B  2  91  ? 27.743  -6.909  25.417   1.00 130.71 ? 95   LYS   B HE2  1 
ATOM   10350 H  HE3  . LYS   B  2  91  ? 27.940  -8.224  26.287   1.00 130.71 ? 95   LYS   B HE3  1 
ATOM   10351 H  HZ1  . LYS   B  2  91  ? 27.898  -6.392  27.632   1.00 139.15 ? 95   LYS   B HZ1  1 
ATOM   10352 H  HZ2  . LYS   B  2  91  ? 29.213  -6.991  27.726   1.00 139.15 ? 95   LYS   B HZ2  1 
ATOM   10353 H  HZ3  . LYS   B  2  91  ? 29.018  -5.792  26.936   1.00 139.15 ? 95   LYS   B HZ3  1 
ATOM   10354 N  N    . LEU   B  2  92  ? 32.198  -10.180 20.497   1.00 82.82  ? 96   LEU   B N    1 
ATOM   10355 C  CA   . LEU   B  2  92  ? 33.417  -10.578 19.805   1.00 83.99  ? 96   LEU   B CA   1 
ATOM   10356 C  C    . LEU   B  2  92  ? 34.151  -9.347  19.300   1.00 89.14  ? 96   LEU   B C    1 
ATOM   10357 O  O    . LEU   B  2  92  ? 33.583  -8.541  18.555   1.00 88.04  ? 96   LEU   B O    1 
ATOM   10358 C  CB   . LEU   B  2  92  ? 33.103  -11.519 18.641   1.00 79.96  ? 96   LEU   B CB   1 
ATOM   10359 C  CG   . LEU   B  2  92  ? 33.353  -13.008 18.874   1.00 78.17  ? 96   LEU   B CG   1 
ATOM   10360 C  CD1  . LEU   B  2  92  ? 32.772  -13.806 17.721   1.00 74.52  ? 96   LEU   B CD1  1 
ATOM   10361 C  CD2  . LEU   B  2  92  ? 34.842  -13.295 19.033   1.00 79.76  ? 96   LEU   B CD2  1 
ATOM   10362 H  H    . LEU   B  2  92  ? 31.632  -9.773  19.993   1.00 99.42  ? 96   LEU   B H    1 
ATOM   10363 H  HA   . LEU   B  2  92  ? 33.996  -11.034 20.435   1.00 100.83 ? 96   LEU   B HA   1 
ATOM   10364 H  HB2  . LEU   B  2  92  ? 32.164  -11.419 18.420   1.00 95.98  ? 96   LEU   B HB2  1 
ATOM   10365 H  HB3  . LEU   B  2  92  ? 33.651  -11.253 17.885   1.00 95.98  ? 96   LEU   B HB3  1 
ATOM   10366 H  HG   . LEU   B  2  92  ? 32.918  -13.283 19.696   1.00 93.84  ? 96   LEU   B HG   1 
ATOM   10367 H  HD11 . LEU   B  2  92  ? 32.645  -14.725 18.005   1.00 89.46  ? 96   LEU   B HD11 1 
ATOM   10368 H  HD12 . LEU   B  2  92  ? 31.921  -13.418 17.465   1.00 89.46  ? 96   LEU   B HD12 1 
ATOM   10369 H  HD13 . LEU   B  2  92  ? 33.388  -13.774 16.972   1.00 89.46  ? 96   LEU   B HD13 1 
ATOM   10370 H  HD21 . LEU   B  2  92  ? 35.087  -14.027 18.446   1.00 95.75  ? 96   LEU   B HD21 1 
ATOM   10371 H  HD22 . LEU   B  2  92  ? 35.344  -12.499 18.797   1.00 95.75  ? 96   LEU   B HD22 1 
ATOM   10372 H  HD23 . LEU   B  2  92  ? 35.020  -13.536 19.956   1.00 95.75  ? 96   LEU   B HD23 1 
ATOM   10373 N  N    . ARG   B  2  93  ? 35.407  -9.212  19.701   1.00 96.82  ? 97   ARG   B N    1 
ATOM   10374 C  CA   . ARG   B  2  93  ? 36.262  -8.181  19.139   1.00 102.68 ? 97   ARG   B CA   1 
ATOM   10375 C  C    . ARG   B  2  93  ? 36.664  -8.571  17.718   1.00 103.30 ? 97   ARG   B C    1 
ATOM   10376 O  O    . ARG   B  2  93  ? 36.861  -9.757  17.434   1.00 104.17 ? 97   ARG   B O    1 
ATOM   10377 C  CB   . ARG   B  2  93  ? 37.502  -8.001  20.010   1.00 107.58 ? 97   ARG   B CB   1 
ATOM   10378 C  CG   . ARG   B  2  93  ? 38.447  -6.920  19.539   1.00 109.86 ? 97   ARG   B CG   1 
ATOM   10379 C  CD   . ARG   B  2  93  ? 39.624  -6.776  20.482   1.00 107.96 ? 97   ARG   B CD   1 
ATOM   10380 N  NE   . ARG   B  2  93  ? 40.701  -6.000  19.875   1.00 106.77 ? 97   ARG   B NE   1 
ATOM   10381 C  CZ   . ARG   B  2  93  ? 41.668  -5.393  20.556   1.00 108.74 ? 97   ARG   B CZ   1 
ATOM   10382 N  NH1  . ARG   B  2  93  ? 42.603  -4.715  19.906   1.00 109.27 ? 97   ARG   B NH1  1 
ATOM   10383 N  NH2  . ARG   B  2  93  ? 41.697  -5.452  21.881   1.00 108.36 ? 97   ARG   B NH2  1 
ATOM   10384 H  H    . ARG   B  2  93  ? 35.788  -9.703  20.296   1.00 116.22 ? 97   ARG   B H    1 
ATOM   10385 H  HA   . ARG   B  2  93  ? 35.791  -7.333  19.102   1.00 123.25 ? 97   ARG   B HA   1 
ATOM   10386 H  HB2  . ARG   B  2  93  ? 37.218  -7.770  20.909   1.00 129.14 ? 97   ARG   B HB2  1 
ATOM   10387 H  HB3  . ARG   B  2  93  ? 37.995  -8.836  20.023   1.00 129.14 ? 97   ARG   B HB3  1 
ATOM   10388 H  HG2  . ARG   B  2  93  ? 38.785  -7.148  18.659   1.00 131.87 ? 97   ARG   B HG2  1 
ATOM   10389 H  HG3  . ARG   B  2  93  ? 37.977  -6.072  19.504   1.00 131.87 ? 97   ARG   B HG3  1 
ATOM   10390 H  HD2  . ARG   B  2  93  ? 39.336  -6.320  21.288   1.00 129.59 ? 97   ARG   B HD2  1 
ATOM   10391 H  HD3  . ARG   B  2  93  ? 39.968  -7.655  20.703   1.00 129.59 ? 97   ARG   B HD3  1 
ATOM   10392 H  HE   . ARG   B  2  93  ? 40.711  -5.931  19.018   1.00 128.16 ? 97   ARG   B HE   1 
ATOM   10393 H  HH11 . ARG   B  2  93  ? 42.582  -4.668  19.048   1.00 131.16 ? 97   ARG   B HH11 1 
ATOM   10394 H  HH12 . ARG   B  2  93  ? 43.230  -4.321  20.344   1.00 131.16 ? 97   ARG   B HH12 1 
ATOM   10395 H  HH21 . ARG   B  2  93  ? 41.087  -5.886  22.306   1.00 130.07 ? 97   ARG   B HH21 1 
ATOM   10396 H  HH22 . ARG   B  2  93  ? 42.325  -5.057  22.315   1.00 130.07 ? 97   ARG   B HH22 1 
ATOM   10397 N  N    . PRO   B  2  94  ? 36.780  -7.610  16.800   1.00 105.49 ? 98   PRO   B N    1 
ATOM   10398 C  CA   . PRO   B  2  94  ? 37.212  -7.950  15.439   1.00 102.91 ? 98   PRO   B CA   1 
ATOM   10399 C  C    . PRO   B  2  94  ? 38.513  -8.737  15.447   1.00 111.43 ? 98   PRO   B C    1 
ATOM   10400 O  O    . PRO   B  2  94  ? 39.442  -8.436  16.200   1.00 101.32 ? 98   PRO   B O    1 
ATOM   10401 C  CB   . PRO   B  2  94  ? 37.385  -6.584  14.767   1.00 109.76 ? 98   PRO   B CB   1 
ATOM   10402 C  CG   . PRO   B  2  94  ? 36.489  -5.678  15.508   1.00 112.51 ? 98   PRO   B CG   1 
ATOM   10403 C  CD   . PRO   B  2  94  ? 36.410  -6.188  16.921   1.00 110.05 ? 98   PRO   B CD   1 
ATOM   10404 H  HA   . PRO   B  2  94  ? 36.524  -8.458  14.981   1.00 123.53 ? 98   PRO   B HA   1 
ATOM   10405 H  HB2  . PRO   B  2  94  ? 38.308  -6.296  14.840   1.00 131.75 ? 98   PRO   B HB2  1 
ATOM   10406 H  HB3  . PRO   B  2  94  ? 37.128  -6.640  13.834   1.00 131.75 ? 98   PRO   B HB3  1 
ATOM   10407 H  HG2  . PRO   B  2  94  ? 36.855  -4.780  15.492   1.00 135.05 ? 98   PRO   B HG2  1 
ATOM   10408 H  HG3  . PRO   B  2  94  ? 35.611  -5.686  15.096   1.00 135.05 ? 98   PRO   B HG3  1 
ATOM   10409 H  HD2  . PRO   B  2  94  ? 37.036  -5.717  17.492   1.00 132.10 ? 98   PRO   B HD2  1 
ATOM   10410 H  HD3  . PRO   B  2  94  ? 35.509  -6.096  17.270   1.00 132.10 ? 98   PRO   B HD3  1 
ATOM   10411 N  N    . GLY   B  2  95  ? 38.573  -9.757  14.597   1.00 116.67 ? 99   GLY   B N    1 
ATOM   10412 C  CA   . GLY   B  2  95  ? 39.770  -10.560 14.500   1.00 127.25 ? 99   GLY   B CA   1 
ATOM   10413 C  C    . GLY   B  2  95  ? 40.045  -11.416 15.710   1.00 123.83 ? 99   GLY   B C    1 
ATOM   10414 O  O    . GLY   B  2  95  ? 41.171  -11.882 15.878   1.00 128.83 ? 99   GLY   B O    1 
ATOM   10415 H  H    . GLY   B  2  95  ? 37.935  -9.999  14.072   1.00 140.05 ? 99   GLY   B H    1 
ATOM   10416 H  HA2  . GLY   B  2  95  ? 39.692  -11.147 13.732   1.00 152.74 ? 99   GLY   B HA2  1 
ATOM   10417 H  HA3  . GLY   B  2  95  ? 40.531  -9.973  14.372   1.00 152.74 ? 99   GLY   B HA3  1 
ATOM   10418 N  N    . GLY   B  2  96  ? 39.044  -11.648 16.552   1.00 114.37 ? 100  GLY   B N    1 
ATOM   10419 C  CA   . GLY   B  2  96  ? 39.205  -12.500 17.712   1.00 106.66 ? 100  GLY   B CA   1 
ATOM   10420 C  C    . GLY   B  2  96  ? 38.231  -13.652 17.647   1.00 98.58  ? 100  GLY   B C    1 
ATOM   10421 O  O    . GLY   B  2  96  ? 37.225  -13.572 16.934   1.00 94.90  ? 100  GLY   B O    1 
ATOM   10422 H  H    . GLY   B  2  96  ? 38.254  -11.318 16.469   1.00 137.29 ? 100  GLY   B H    1 
ATOM   10423 H  HA2  . GLY   B  2  96  ? 40.109  -12.851 17.739   1.00 128.03 ? 100  GLY   B HA2  1 
ATOM   10424 H  HA3  . GLY   B  2  96  ? 39.039  -11.991 18.520   1.00 128.03 ? 100  GLY   B HA3  1 
ATOM   10425 N  N    . ALA   B  2  97  ? 38.508  -14.728 18.374   1.00 89.59  ? 101  ALA   B N    1 
ATOM   10426 C  CA   . ALA   B  2  97  ? 37.692  -15.929 18.314   1.00 84.20  ? 101  ALA   B CA   1 
ATOM   10427 C  C    . ALA   B  2  97  ? 37.375  -16.404 19.721   1.00 78.25  ? 101  ALA   B C    1 
ATOM   10428 O  O    . ALA   B  2  97  ? 38.234  -16.376 20.608   1.00 80.72  ? 101  ALA   B O    1 
ATOM   10429 C  CB   . ALA   B  2  97  ? 38.398  -17.037 17.528   1.00 85.55  ? 101  ALA   B CB   1 
ATOM   10430 H  H    . ALA   B  2  97  ? 39.174  -14.785 18.916   1.00 107.55 ? 101  ALA   B H    1 
ATOM   10431 H  HA   . ALA   B  2  97  ? 36.852  -15.730 17.871   1.00 101.08 ? 101  ALA   B HA   1 
ATOM   10432 H  HB1  . ALA   B  2  97  ? 37.809  -17.806 17.467   1.00 102.69 ? 101  ALA   B HB1  1 
ATOM   10433 H  HB2  . ALA   B  2  97  ? 38.608  -16.710 16.640   1.00 102.69 ? 101  ALA   B HB2  1 
ATOM   10434 H  HB3  . ALA   B  2  97  ? 39.214  -17.282 17.992   1.00 102.69 ? 101  ALA   B HB3  1 
ATOM   10435 N  N    . GLN   B  2  98  ? 36.132  -16.832 19.916   1.00 69.02  ? 102  GLN   B N    1 
ATOM   10436 C  CA   . GLN   B  2  98  ? 35.664  -17.369 21.184   1.00 63.77  ? 102  GLN   B CA   1 
ATOM   10437 C  C    . GLN   B  2  98  ? 35.080  -18.750 20.936   1.00 59.62  ? 102  GLN   B C    1 
ATOM   10438 O  O    . GLN   B  2  98  ? 34.310  -18.941 19.988   1.00 58.38  ? 102  GLN   B O    1 
ATOM   10439 C  CB   . GLN   B  2  98  ? 34.616  -16.451 21.815   1.00 65.14  ? 102  GLN   B CB   1 
ATOM   10440 C  CG   . GLN   B  2  98  ? 34.781  -16.251 23.312   1.00 72.60  ? 102  GLN   B CG   1 
ATOM   10441 C  CD   . GLN   B  2  98  ? 36.081  -15.556 23.667   1.00 78.29  ? 102  GLN   B CD   1 
ATOM   10442 O  OE1  . GLN   B  2  98  ? 36.871  -15.207 22.790   1.00 80.17  ? 102  GLN   B OE1  1 
ATOM   10443 N  NE2  . GLN   B  2  98  ? 36.311  -15.354 24.958   1.00 82.38  ? 102  GLN   B NE2  1 
ATOM   10444 H  H    . GLN   B  2  98  ? 35.525  -16.820 19.308   1.00 82.86  ? 102  GLN   B H    1 
ATOM   10445 H  HA   . GLN   B  2  98  ? 36.403  -17.451 21.807   1.00 76.56  ? 102  GLN   B HA   1 
ATOM   10446 H  HB2  . GLN   B  2  98  ? 34.675  -15.579 21.394   1.00 78.20  ? 102  GLN   B HB2  1 
ATOM   10447 H  HB3  . GLN   B  2  98  ? 33.738  -16.834 21.664   1.00 78.20  ? 102  GLN   B HB3  1 
ATOM   10448 H  HG2  . GLN   B  2  98  ? 34.049  -15.706 23.641   1.00 87.15  ? 102  GLN   B HG2  1 
ATOM   10449 H  HG3  . GLN   B  2  98  ? 34.773  -17.117 23.750   1.00 87.15  ? 102  GLN   B HG3  1 
ATOM   10450 H  HE21 . GLN   B  2  98  ? 35.736  -15.613 25.543   1.00 98.89  ? 102  GLN   B HE21 1 
ATOM   10451 H  HE22 . GLN   B  2  98  ? 37.035  -14.963 25.211   1.00 98.89  ? 102  GLN   B HE22 1 
ATOM   10452 N  N    . THR   B  2  99  ? 35.450  -19.707 21.780   1.00 59.54  ? 103  THR   B N    1 
ATOM   10453 C  CA   . THR   B  2  99  ? 34.988  -21.083 21.664   1.00 59.25  ? 103  THR   B CA   1 
ATOM   10454 C  C    . THR   B  2  99  ? 33.821  -21.298 22.619   1.00 58.65  ? 103  THR   B C    1 
ATOM   10455 O  O    . THR   B  2  99  ? 33.952  -21.064 23.825   1.00 58.95  ? 103  THR   B O    1 
ATOM   10456 C  CB   . THR   B  2  99  ? 36.113  -22.068 21.982   1.00 58.69  ? 103  THR   B CB   1 
ATOM   10457 O  OG1  . THR   B  2  99  ? 37.297  -21.701 21.262   1.00 62.97  ? 103  THR   B OG1  1 
ATOM   10458 C  CG2  . THR   B  2  99  ? 35.693  -23.491 21.609   1.00 52.75  ? 103  THR   B CG2  1 
ATOM   10459 H  H    . THR   B  2  99  ? 35.980  -19.579 22.445   1.00 71.49  ? 103  THR   B H    1 
ATOM   10460 H  HA   . THR   B  2  99  ? 34.686  -21.241 20.756   1.00 71.14  ? 103  THR   B HA   1 
ATOM   10461 H  HB   . THR   B  2  99  ? 36.305  -22.050 22.932   1.00 70.47  ? 103  THR   B HB   1 
ATOM   10462 H  HG1  . THR   B  2  99  ? 37.465  -22.275 20.673   1.00 75.60  ? 103  THR   B HG1  1 
ATOM   10463 H  HG21 . THR   B  2  99  ? 36.422  -24.108 21.783   1.00 63.34  ? 103  THR   B HG21 1 
ATOM   10464 H  HG22 . THR   B  2  99  ? 34.923  -23.759 22.135   1.00 63.34  ? 103  THR   B HG22 1 
ATOM   10465 H  HG23 . THR   B  2  99  ? 35.463  -23.534 20.668   1.00 63.34  ? 103  THR   B HG23 1 
ATOM   10466 N  N    . LEU   B  2  100 ? 32.691  -21.746 22.082   1.00 56.89  ? 104  LEU   B N    1 
ATOM   10467 C  CA   . LEU   B  2  100 ? 31.525  -22.088 22.883   1.00 60.52  ? 104  LEU   B CA   1 
ATOM   10468 C  C    . LEU   B  2  100 ? 31.444  -23.599 23.057   1.00 63.24  ? 104  LEU   B C    1 
ATOM   10469 O  O    . LEU   B  2  100 ? 31.731  -24.358 22.126   1.00 62.80  ? 104  LEU   B O    1 
ATOM   10470 C  CB   . LEU   B  2  100 ? 30.241  -21.581 22.227   1.00 61.98  ? 104  LEU   B CB   1 
ATOM   10471 C  CG   . LEU   B  2  100 ? 30.239  -20.129 21.751   1.00 64.56  ? 104  LEU   B CG   1 
ATOM   10472 C  CD1  . LEU   B  2  100 ? 29.040  -19.891 20.854   1.00 63.34  ? 104  LEU   B CD1  1 
ATOM   10473 C  CD2  . LEU   B  2  100 ? 30.229  -19.168 22.927   1.00 69.67  ? 104  LEU   B CD2  1 
ATOM   10474 H  H    . LEU   B  2  100 ? 32.574  -21.863 21.238   1.00 68.30  ? 104  LEU   B H    1 
ATOM   10475 H  HA   . LEU   B  2  100 ? 31.604  -21.676 23.757   1.00 72.66  ? 104  LEU   B HA   1 
ATOM   10476 H  HB2  . LEU   B  2  100 ? 30.062  -22.135 21.451   1.00 74.41  ? 104  LEU   B HB2  1 
ATOM   10477 H  HB3  . LEU   B  2  100 ? 29.521  -21.669 22.870   1.00 74.41  ? 104  LEU   B HB3  1 
ATOM   10478 H  HG   . LEU   B  2  100 ? 31.049  -19.957 21.245   1.00 77.51  ? 104  LEU   B HG   1 
ATOM   10479 H  HD11 . LEU   B  2  100 ? 29.042  -18.966 20.563   1.00 76.04  ? 104  LEU   B HD11 1 
ATOM   10480 H  HD12 . LEU   B  2  100 ? 29.100  -20.479 20.084   1.00 76.04  ? 104  LEU   B HD12 1 
ATOM   10481 H  HD13 . LEU   B  2  100 ? 28.230  -20.080 21.352   1.00 76.04  ? 104  LEU   B HD13 1 
ATOM   10482 H  HD21 . LEU   B  2  100 ? 30.214  -18.258 22.591   1.00 83.64  ? 104  LEU   B HD21 1 
ATOM   10483 H  HD22 . LEU   B  2  100 ? 29.439  -19.335 23.464   1.00 83.64  ? 104  LEU   B HD22 1 
ATOM   10484 H  HD23 . LEU   B  2  100 ? 31.027  -19.311 23.459   1.00 83.64  ? 104  LEU   B HD23 1 
ATOM   10485 N  N    . GLN   B  2  101 ? 31.052  -24.031 24.252   1.00 65.75  ? 105  GLN   B N    1 
ATOM   10486 C  CA   . GLN   B  2  101 ? 30.829  -25.441 24.544   1.00 68.65  ? 105  GLN   B CA   1 
ATOM   10487 C  C    . GLN   B  2  101 ? 29.334  -25.723 24.472   1.00 71.22  ? 105  GLN   B C    1 
ATOM   10488 O  O    . GLN   B  2  101 ? 28.541  -25.074 25.163   1.00 73.07  ? 105  GLN   B O    1 
ATOM   10489 C  CB   . GLN   B  2  101 ? 31.384  -25.814 25.917   1.00 74.46  ? 105  GLN   B CB   1 
ATOM   10490 C  CG   . GLN   B  2  101 ? 32.901  -25.756 26.003   1.00 80.97  ? 105  GLN   B CG   1 
ATOM   10491 C  CD   . GLN   B  2  101 ? 33.576  -26.720 25.046   1.00 86.98  ? 105  GLN   B CD   1 
ATOM   10492 O  OE1  . GLN   B  2  101 ? 34.396  -26.320 24.220   1.00 88.96  ? 105  GLN   B OE1  1 
ATOM   10493 N  NE2  . GLN   B  2  101 ? 33.235  -27.999 25.155   1.00 88.08  ? 105  GLN   B NE2  1 
ATOM   10494 H  H    . GLN   B  2  101 ? 30.906  -23.513 24.923   1.00 78.94  ? 105  GLN   B H    1 
ATOM   10495 H  HA   . GLN   B  2  101 ? 31.281  -25.985 23.881   1.00 82.42  ? 105  GLN   B HA   1 
ATOM   10496 H  HB2  . GLN   B  2  101 ? 31.027  -25.197 26.575   1.00 89.39  ? 105  GLN   B HB2  1 
ATOM   10497 H  HB3  . GLN   B  2  101 ? 31.111  -26.720 26.128   1.00 89.39  ? 105  GLN   B HB3  1 
ATOM   10498 H  HG2  . GLN   B  2  101 ? 33.196  -24.858 25.785   1.00 97.21  ? 105  GLN   B HG2  1 
ATOM   10499 H  HG3  . GLN   B  2  101 ? 33.175  -25.985 26.905   1.00 97.21  ? 105  GLN   B HG3  1 
ATOM   10500 H  HE21 . GLN   B  2  101 ? 32.658  -28.241 25.745   1.00 105.73 ? 105  GLN   B HE21 1 
ATOM   10501 H  HE22 . GLN   B  2  101 ? 33.590  -28.584 24.635   1.00 105.73 ? 105  GLN   B HE22 1 
ATOM   10502 N  N    . VAL   B  2  102 ? 28.954  -26.687 23.638   1.00 70.36  ? 106  VAL   B N    1 
ATOM   10503 C  CA   . VAL   B  2  102 ? 27.557  -27.026 23.396   1.00 67.23  ? 106  VAL   B CA   1 
ATOM   10504 C  C    . VAL   B  2  102 ? 27.373  -28.509 23.679   1.00 67.14  ? 106  VAL   B C    1 
ATOM   10505 O  O    . VAL   B  2  102 ? 28.152  -29.339 23.198   1.00 69.03  ? 106  VAL   B O    1 
ATOM   10506 C  CB   . VAL   B  2  102 ? 27.134  -26.684 21.956   1.00 65.71  ? 106  VAL   B CB   1 
ATOM   10507 C  CG1  . VAL   B  2  102 ? 25.648  -26.950 21.756   1.00 67.52  ? 106  VAL   B CG1  1 
ATOM   10508 C  CG2  . VAL   B  2  102 ? 27.470  -25.234 21.640   1.00 66.05  ? 106  VAL   B CG2  1 
ATOM   10509 H  H    . VAL   B  2  102 ? 29.505  -27.172 23.189   1.00 84.46  ? 106  VAL   B H    1 
ATOM   10510 H  HA   . VAL   B  2  102 ? 26.993  -26.526 24.006   1.00 80.72  ? 106  VAL   B HA   1 
ATOM   10511 H  HB   . VAL   B  2  102 ? 27.622  -27.252 21.340   1.00 78.89  ? 106  VAL   B HB   1 
ATOM   10512 H  HG11 . VAL   B  2  102 ? 25.399  -26.689 20.855   1.00 81.06  ? 106  VAL   B HG11 1 
ATOM   10513 H  HG12 . VAL   B  2  102 ? 25.476  -27.896 21.886   1.00 81.06  ? 106  VAL   B HG12 1 
ATOM   10514 H  HG13 . VAL   B  2  102 ? 25.144  -26.430 22.401   1.00 81.06  ? 106  VAL   B HG13 1 
ATOM   10515 H  HG21 . VAL   B  2  102 ? 27.166  -25.028 20.742   1.00 79.30  ? 106  VAL   B HG21 1 
ATOM   10516 H  HG22 . VAL   B  2  102 ? 27.023  -24.660 22.281   1.00 79.30  ? 106  VAL   B HG22 1 
ATOM   10517 H  HG23 . VAL   B  2  102 ? 28.431  -25.113 21.700   1.00 79.30  ? 106  VAL   B HG23 1 
ATOM   10518 N  N    . HIS   B  2  103 ? 26.342  -28.838 24.453   1.00 67.43  ? 107  HIS   B N    1 
ATOM   10519 C  CA   . HIS   B  2  103 ? 26.083  -30.200 24.897   1.00 66.94  ? 107  HIS   B CA   1 
ATOM   10520 C  C    . HIS   B  2  103 ? 24.716  -30.638 24.398   1.00 66.32  ? 107  HIS   B C    1 
ATOM   10521 O  O    . HIS   B  2  103 ? 23.721  -29.935 24.606   1.00 67.71  ? 107  HIS   B O    1 
ATOM   10522 C  CB   . HIS   B  2  103 ? 26.149  -30.292 26.423   1.00 68.14  ? 107  HIS   B CB   1 
ATOM   10523 C  CG   . HIS   B  2  103 ? 27.384  -29.679 27.005   1.00 72.52  ? 107  HIS   B CG   1 
ATOM   10524 N  ND1  . HIS   B  2  103 ? 28.590  -30.342 27.056   1.00 72.24  ? 107  HIS   B ND1  1 
ATOM   10525 C  CD2  . HIS   B  2  103 ? 27.603  -28.459 27.552   1.00 73.25  ? 107  HIS   B CD2  1 
ATOM   10526 C  CE1  . HIS   B  2  103 ? 29.498  -29.561 27.611   1.00 73.67  ? 107  HIS   B CE1  1 
ATOM   10527 N  NE2  . HIS   B  2  103 ? 28.925  -28.413 27.923   1.00 73.82  ? 107  HIS   B NE2  1 
ATOM   10528 H  H    . HIS   B  2  103 ? 25.764  -28.270 24.741   1.00 80.95  ? 107  HIS   B H    1 
ATOM   10529 H  HA   . HIS   B  2  103 ? 26.747  -30.801 24.523   1.00 80.36  ? 107  HIS   B HA   1 
ATOM   10530 H  HB2  . HIS   B  2  103 ? 25.383  -29.830 26.797   1.00 81.81  ? 107  HIS   B HB2  1 
ATOM   10531 H  HB3  . HIS   B  2  103 ? 26.132  -31.227 26.681   1.00 81.81  ? 107  HIS   B HB3  1 
ATOM   10532 H  HD2  . HIS   B  2  103 ? 26.976  -27.780 27.656   1.00 87.93  ? 107  HIS   B HD2  1 
ATOM   10533 H  HE1  . HIS   B  2  103 ? 30.390  -29.782 27.758   1.00 88.44  ? 107  HIS   B HE1  1 
ATOM   10534 H  HE2  . HIS   B  2  103 ? 29.316  -27.745 28.297   1.00 88.62  ? 107  HIS   B HE2  1 
ATOM   10535 N  N    . VAL   B  2  104 ? 24.668  -31.797 23.746   1.00 64.25  ? 108  VAL   B N    1 
ATOM   10536 C  CA   . VAL   B  2  104 ? 23.436  -32.340 23.193   1.00 62.60  ? 108  VAL   B CA   1 
ATOM   10537 C  C    . VAL   B  2  104 ? 23.204  -33.723 23.781   1.00 68.27  ? 108  VAL   B C    1 
ATOM   10538 O  O    . VAL   B  2  104 ? 24.149  -34.495 23.982   1.00 67.58  ? 108  VAL   B O    1 
ATOM   10539 C  CB   . VAL   B  2  104 ? 23.476  -32.408 21.652   1.00 55.23  ? 108  VAL   B CB   1 
ATOM   10540 C  CG1  . VAL   B  2  104 ? 22.159  -32.949 21.106   1.00 55.48  ? 108  VAL   B CG1  1 
ATOM   10541 C  CG2  . VAL   B  2  104 ? 23.772  -31.036 21.069   1.00 53.25  ? 108  VAL   B CG2  1 
ATOM   10542 H  H    . VAL   B  2  104 ? 25.355  -32.296 23.609   1.00 77.13  ? 108  VAL   B H    1 
ATOM   10543 H  HA   . VAL   B  2  104 ? 22.697  -31.768 23.452   1.00 75.16  ? 108  VAL   B HA   1 
ATOM   10544 H  HB   . VAL   B  2  104 ? 24.186  -33.011 21.382   1.00 66.32  ? 108  VAL   B HB   1 
ATOM   10545 H  HG11 . VAL   B  2  104 ? 22.192  -32.943 20.137   1.00 66.61  ? 108  VAL   B HG11 1 
ATOM   10546 H  HG12 . VAL   B  2  104 ? 22.033  -33.856 21.427   1.00 66.61  ? 108  VAL   B HG12 1 
ATOM   10547 H  HG13 . VAL   B  2  104 ? 21.433  -32.385 21.416   1.00 66.61  ? 108  VAL   B HG13 1 
ATOM   10548 H  HG21 . VAL   B  2  104 ? 23.779  -31.099 20.101   1.00 63.94  ? 108  VAL   B HG21 1 
ATOM   10549 H  HG22 . VAL   B  2  104 ? 23.083  -30.416 21.356   1.00 63.94  ? 108  VAL   B HG22 1 
ATOM   10550 H  HG23 . VAL   B  2  104 ? 24.639  -30.738 21.388   1.00 63.94  ? 108  VAL   B HG23 1 
ATOM   10551 N  N    . ARG   B  2  105 ? 21.938  -34.030 24.053   1.00 71.59  ? 109  ARG   B N    1 
ATOM   10552 C  CA   . ARG   B  2  105 ? 21.535  -35.328 24.573   1.00 70.12  ? 109  ARG   B CA   1 
ATOM   10553 C  C    . ARG   B  2  105 ? 20.112  -35.586 24.109   1.00 65.23  ? 109  ARG   B C    1 
ATOM   10554 O  O    . ARG   B  2  105 ? 19.236  -34.738 24.300   1.00 64.50  ? 109  ARG   B O    1 
ATOM   10555 C  CB   . ARG   B  2  105 ? 21.615  -35.363 26.101   1.00 73.14  ? 109  ARG   B CB   1 
ATOM   10556 C  CG   . ARG   B  2  105 ? 21.264  -36.706 26.717   1.00 77.97  ? 109  ARG   B CG   1 
ATOM   10557 C  CD   . ARG   B  2  105 ? 21.192  -36.597 28.228   1.00 85.01  ? 109  ARG   B CD   1 
ATOM   10558 N  NE   . ARG   B  2  105 ? 20.709  -37.825 28.852   1.00 94.73  ? 109  ARG   B NE   1 
ATOM   10559 C  CZ   . ARG   B  2  105 ? 19.443  -38.230 28.828   1.00 102.59 ? 109  ARG   B CZ   1 
ATOM   10560 N  NH1  . ARG   B  2  105 ? 18.522  -37.513 28.197   1.00 104.91 ? 109  ARG   B NH1  1 
ATOM   10561 N  NH2  . ARG   B  2  105 ? 19.099  -39.360 29.429   1.00 107.37 ? 109  ARG   B NH2  1 
ATOM   10562 H  H    . ARG   B  2  105 ? 21.280  -33.488 23.941   1.00 85.95  ? 109  ARG   B H    1 
ATOM   10563 H  HA   . ARG   B  2  105 ? 22.115  -36.025 24.230   1.00 84.18  ? 109  ARG   B HA   1 
ATOM   10564 H  HB2  . ARG   B  2  105 ? 22.522  -35.146 26.369   1.00 87.81  ? 109  ARG   B HB2  1 
ATOM   10565 H  HB3  . ARG   B  2  105 ? 20.997  -34.706 26.459   1.00 87.81  ? 109  ARG   B HB3  1 
ATOM   10566 H  HG2  . ARG   B  2  105 ? 20.400  -36.999 26.387   1.00 93.60  ? 109  ARG   B HG2  1 
ATOM   10567 H  HG3  . ARG   B  2  105 ? 21.945  -37.357 26.486   1.00 93.60  ? 109  ARG   B HG3  1 
ATOM   10568 H  HD2  . ARG   B  2  105 ? 22.078  -36.411 28.575   1.00 102.04 ? 109  ARG   B HD2  1 
ATOM   10569 H  HD3  . ARG   B  2  105 ? 20.585  -35.880 28.466   1.00 102.04 ? 109  ARG   B HD3  1 
ATOM   10570 H  HE   . ARG   B  2  105 ? 21.281  -38.319 29.262   1.00 113.71 ? 109  ARG   B HE   1 
ATOM   10571 H  HH11 . ARG   B  2  105 ? 18.742  -36.782 27.801   1.00 125.93 ? 109  ARG   B HH11 1 
ATOM   10572 H  HH12 . ARG   B  2  105 ? 17.704  -37.779 28.185   1.00 125.93 ? 109  ARG   B HH12 1 
ATOM   10573 H  HH21 . ARG   B  2  105 ? 19.695  -39.830 29.833   1.00 128.88 ? 109  ARG   B HH21 1 
ATOM   10574 H  HH22 . ARG   B  2  105 ? 18.281  -39.623 29.414   1.00 128.88 ? 109  ARG   B HH22 1 
ATOM   10575 N  N    . GLN   B  2  106 ? 19.884  -36.741 23.495   1.00 61.23  ? 110  GLN   B N    1 
ATOM   10576 C  CA   . GLN   B  2  106 ? 18.559  -37.094 23.010   1.00 57.64  ? 110  GLN   B CA   1 
ATOM   10577 C  C    . GLN   B  2  106 ? 17.757  -37.727 24.138   1.00 61.19  ? 110  GLN   B C    1 
ATOM   10578 O  O    . GLN   B  2  106 ? 18.236  -38.644 24.813   1.00 63.65  ? 110  GLN   B O    1 
ATOM   10579 C  CB   . GLN   B  2  106 ? 18.650  -38.044 21.816   1.00 53.16  ? 110  GLN   B CB   1 
ATOM   10580 C  CG   . GLN   B  2  106 ? 19.239  -37.398 20.573   1.00 51.75  ? 110  GLN   B CG   1 
ATOM   10581 C  CD   . GLN   B  2  106 ? 18.897  -38.150 19.302   1.00 57.66  ? 110  GLN   B CD   1 
ATOM   10582 O  OE1  . GLN   B  2  106 ? 19.774  -38.702 18.638   1.00 62.52  ? 110  GLN   B OE1  1 
ATOM   10583 N  NE2  . GLN   B  2  106 ? 17.616  -38.166 18.952   1.00 62.46  ? 110  GLN   B NE2  1 
ATOM   10584 H  H    . GLN   B  2  106 ? 20.485  -37.339 23.348   1.00 73.52  ? 110  GLN   B H    1 
ATOM   10585 H  HA   . GLN   B  2  106 ? 18.097  -36.294 22.715   1.00 69.20  ? 110  GLN   B HA   1 
ATOM   10586 H  HB2  . GLN   B  2  106 ? 19.214  -38.796 22.057   1.00 63.83  ? 110  GLN   B HB2  1 
ATOM   10587 H  HB3  . GLN   B  2  106 ? 17.758  -38.356 21.596   1.00 63.83  ? 110  GLN   B HB3  1 
ATOM   10588 H  HG2  . GLN   B  2  106 ? 18.891  -36.496 20.491   1.00 62.14  ? 110  GLN   B HG2  1 
ATOM   10589 H  HG3  . GLN   B  2  106 ? 20.205  -37.374 20.656   1.00 62.14  ? 110  GLN   B HG3  1 
ATOM   10590 H  HE21 . GLN   B  2  106 ? 17.032  -37.763 19.438   1.00 74.99  ? 110  GLN   B HE21 1 
ATOM   10591 H  HE22 . GLN   B  2  106 ? 17.371  -38.579 18.239   1.00 74.99  ? 110  GLN   B HE22 1 
ATOM   10592 N  N    . THR   B  2  107 ? 16.544  -37.224 24.349   1.00 58.94  ? 111  THR   B N    1 
ATOM   10593 C  CA   . THR   B  2  107 ? 15.677  -37.782 25.375   1.00 63.87  ? 111  THR   B CA   1 
ATOM   10594 C  C    . THR   B  2  107 ? 15.187  -39.160 24.945   1.00 65.58  ? 111  THR   B C    1 
ATOM   10595 O  O    . THR   B  2  107 ? 15.089  -39.466 23.753   1.00 65.36  ? 111  THR   B O    1 
ATOM   10596 C  CB   . THR   B  2  107 ? 14.494  -36.850 25.641   1.00 68.00  ? 111  THR   B CB   1 
ATOM   10597 O  OG1  . THR   B  2  107 ? 13.787  -37.288 26.809   1.00 70.09  ? 111  THR   B OG1  1 
ATOM   10598 C  CG2  . THR   B  2  107 ? 13.540  -36.827 24.454   1.00 67.58  ? 111  THR   B CG2  1 
ATOM   10599 H  H    . THR   B  2  107 ? 16.204  -36.565 23.914   1.00 70.76  ? 111  THR   B H    1 
ATOM   10600 H  HA   . THR   B  2  107 ? 16.165  -37.877 26.208   1.00 76.68  ? 111  THR   B HA   1 
ATOM   10601 H  HB   . THR   B  2  107 ? 14.826  -35.949 25.781   1.00 81.64  ? 111  THR   B HB   1 
ATOM   10602 H  HG1  . THR   B  2  107 ? 13.154  -36.762 26.975   1.00 84.14  ? 111  THR   B HG1  1 
ATOM   10603 H  HG21 . THR   B  2  107 ? 12.839  -36.173 24.605   1.00 81.13  ? 111  THR   B HG21 1 
ATOM   10604 H  HG22 . THR   B  2  107 ? 14.021  -36.591 23.646   1.00 81.13  ? 111  THR   B HG22 1 
ATOM   10605 H  HG23 . THR   B  2  107 ? 13.136  -37.701 24.336   1.00 81.13  ? 111  THR   B HG23 1 
ATOM   10606 N  N    . GLU   B  2  108 ? 14.874  -40.000 25.933   1.00 69.48  ? 112  GLU   B N    1 
ATOM   10607 C  CA   . GLU   B  2  108 ? 14.547  -41.389 25.631   1.00 71.68  ? 112  GLU   B CA   1 
ATOM   10608 C  C    . GLU   B  2  108 ? 13.224  -41.519 24.887   1.00 73.25  ? 112  GLU   B C    1 
ATOM   10609 O  O    . GLU   B  2  108 ? 13.058  -42.447 24.088   1.00 73.34  ? 112  GLU   B O    1 
ATOM   10610 C  CB   . GLU   B  2  108 ? 14.508  -42.218 26.914   1.00 75.22  ? 112  GLU   B CB   1 
ATOM   10611 C  CG   . GLU   B  2  108 ? 15.866  -42.412 27.570   1.00 78.80  ? 112  GLU   B CG   1 
ATOM   10612 C  CD   . GLU   B  2  108 ? 16.295  -41.215 28.393   1.00 84.45  ? 112  GLU   B CD   1 
ATOM   10613 O  OE1  . GLU   B  2  108 ? 15.589  -40.186 28.360   1.00 85.79  ? 112  GLU   B OE1  1 
ATOM   10614 O  OE2  . GLU   B  2  108 ? 17.337  -41.303 29.076   1.00 89.59  ? 112  GLU   B OE2  1 
ATOM   10615 H  H    . GLU   B  2  108 ? 14.845  -39.794 26.768   1.00 83.41  ? 112  GLU   B H    1 
ATOM   10616 H  HA   . GLU   B  2  108 ? 15.247  -41.746 25.061   1.00 86.05  ? 112  GLU   B HA   1 
ATOM   10617 H  HB2  . GLU   B  2  108 ? 13.933  -41.771 27.555   1.00 90.30  ? 112  GLU   B HB2  1 
ATOM   10618 H  HB3  . GLU   B  2  108 ? 14.153  -43.096 26.706   1.00 90.30  ? 112  GLU   B HB3  1 
ATOM   10619 H  HG2  . GLU   B  2  108 ? 15.826  -43.182 28.158   1.00 94.59  ? 112  GLU   B HG2  1 
ATOM   10620 H  HG3  . GLU   B  2  108 ? 16.532  -42.556 26.880   1.00 94.59  ? 112  GLU   B HG3  1 
ATOM   10621 N  N    . ASP   B  2  109 ? 12.276  -40.617 25.131   1.00 74.14  ? 113  ASP   B N    1 
ATOM   10622 C  CA   . ASP   B  2  109 ? 10.970  -40.652 24.477   1.00 73.24  ? 113  ASP   B CA   1 
ATOM   10623 C  C    . ASP   B  2  109 ? 10.748  -39.315 23.777   1.00 69.11  ? 113  ASP   B C    1 
ATOM   10624 O  O    . ASP   B  2  109 ? 10.452  -38.306 24.427   1.00 68.05  ? 113  ASP   B O    1 
ATOM   10625 C  CB   . ASP   B  2  109 ? 9.858   -40.944 25.482   1.00 77.88  ? 113  ASP   B CB   1 
ATOM   10626 C  CG   . ASP   B  2  109 ? 8.571   -41.385 24.812   1.00 79.45  ? 113  ASP   B CG   1 
ATOM   10627 O  OD1  . ASP   B  2  109 ? 8.358   -41.022 23.636   1.00 78.67  ? 113  ASP   B OD1  1 
ATOM   10628 O  OD2  . ASP   B  2  109 ? 7.773   -42.097 25.459   1.00 85.76  ? 113  ASP   B OD2  1 
ATOM   10629 H  H    . ASP   B  2  109 ? 12.369  -39.963 25.682   1.00 89.01  ? 113  ASP   B H    1 
ATOM   10630 H  HA   . ASP   B  2  109 ? 10.971  -41.352 23.805   1.00 87.93  ? 113  ASP   B HA   1 
ATOM   10631 H  HB2  . ASP   B  2  109 ? 10.147  -41.654 26.076   1.00 93.50  ? 113  ASP   B HB2  1 
ATOM   10632 H  HB3  . ASP   B  2  109 ? 9.672   -40.140 25.991   1.00 93.50  ? 113  ASP   B HB3  1 
ATOM   10633 N  N    . TYR   B  2  110 ? 10.890  -39.310 22.452   1.00 67.05  ? 114  TYR   B N    1 
ATOM   10634 C  CA   . TYR   B  2  110 ? 10.670  -38.118 21.645   1.00 60.26  ? 114  TYR   B CA   1 
ATOM   10635 C  C    . TYR   B  2  110 ? 9.675   -38.461 20.543   1.00 55.84  ? 114  TYR   B C    1 
ATOM   10636 O  O    . TYR   B  2  110 ? 9.822   -39.503 19.880   1.00 55.96  ? 114  TYR   B O    1 
ATOM   10637 C  CB   . TYR   B  2  110 ? 11.989  -37.605 21.047   1.00 56.52  ? 114  TYR   B CB   1 
ATOM   10638 C  CG   . TYR   B  2  110 ? 11.980  -36.129 20.709   1.00 55.69  ? 114  TYR   B CG   1 
ATOM   10639 C  CD1  . TYR   B  2  110 ? 11.824  -35.171 21.703   1.00 58.31  ? 114  TYR   B CD1  1 
ATOM   10640 C  CD2  . TYR   B  2  110 ? 12.141  -35.692 19.400   1.00 52.73  ? 114  TYR   B CD2  1 
ATOM   10641 C  CE1  . TYR   B  2  110 ? 11.818  -33.822 21.403   1.00 57.35  ? 114  TYR   B CE1  1 
ATOM   10642 C  CE2  . TYR   B  2  110 ? 12.139  -34.343 19.091   1.00 51.59  ? 114  TYR   B CE2  1 
ATOM   10643 C  CZ   . TYR   B  2  110 ? 11.976  -33.413 20.097   1.00 55.13  ? 114  TYR   B CZ   1 
ATOM   10644 O  OH   . TYR   B  2  110 ? 11.972  -32.069 19.800   1.00 54.99  ? 114  TYR   B OH   1 
ATOM   10645 H  H    . TYR   B  2  110 ? 11.118  -40.000 21.991   1.00 80.50  ? 114  TYR   B H    1 
ATOM   10646 H  HA   . TYR   B  2  110 ? 10.296  -37.414 22.197   1.00 72.35  ? 114  TYR   B HA   1 
ATOM   10647 H  HB2  . TYR   B  2  110 ? 12.700  -37.756 21.688   1.00 67.86  ? 114  TYR   B HB2  1 
ATOM   10648 H  HB3  . TYR   B  2  110 ? 12.170  -38.094 20.229   1.00 67.86  ? 114  TYR   B HB3  1 
ATOM   10649 H  HD1  . TYR   B  2  110 ? 11.723  -35.443 22.586   1.00 70.01  ? 114  TYR   B HD1  1 
ATOM   10650 H  HD2  . TYR   B  2  110 ? 12.252  -36.317 18.720   1.00 63.31  ? 114  TYR   B HD2  1 
ATOM   10651 H  HE1  . TYR   B  2  110 ? 11.708  -33.193 22.079   1.00 68.85  ? 114  TYR   B HE1  1 
ATOM   10652 H  HE2  . TYR   B  2  110 ? 12.247  -34.065 18.210   1.00 61.95  ? 114  TYR   B HE2  1 
ATOM   10653 H  HH   . TYR   B  2  110 ? 12.052  -31.957 18.971   1.00 66.03  ? 114  TYR   B HH   1 
ATOM   10654 N  N    . PRO   B  2  111 ? 8.656   -37.632 20.315   1.00 59.76  ? 115  PRO   B N    1 
ATOM   10655 C  CA   . PRO   B  2  111 ? 7.672   -37.948 19.273   1.00 59.69  ? 115  PRO   B CA   1 
ATOM   10656 C  C    . PRO   B  2  111 ? 8.304   -37.981 17.889   1.00 53.06  ? 115  PRO   B C    1 
ATOM   10657 O  O    . PRO   B  2  111 ? 9.379   -37.428 17.650   1.00 50.37  ? 115  PRO   B O    1 
ATOM   10658 C  CB   . PRO   B  2  111 ? 6.641   -36.817 19.393   1.00 63.44  ? 115  PRO   B CB   1 
ATOM   10659 C  CG   . PRO   B  2  111 ? 7.327   -35.732 20.155   1.00 65.06  ? 115  PRO   B CG   1 
ATOM   10660 C  CD   . PRO   B  2  111 ? 8.313   -36.401 21.049   1.00 64.10  ? 115  PRO   B CD   1 
ATOM   10661 H  HA   . PRO   B  2  111 ? 7.244   -38.800 19.454   1.00 71.66  ? 115  PRO   B HA   1 
ATOM   10662 H  HB2  . PRO   B  2  111 ? 6.385   -36.510 18.509   1.00 76.17  ? 115  PRO   B HB2  1 
ATOM   10663 H  HB3  . PRO   B  2  111 ? 5.860   -37.134 19.873   1.00 76.17  ? 115  PRO   B HB3  1 
ATOM   10664 H  HG2  . PRO   B  2  111 ? 7.778   -35.136 19.536   1.00 78.10  ? 115  PRO   B HG2  1 
ATOM   10665 H  HG3  . PRO   B  2  111 ? 6.675   -35.238 20.675   1.00 78.10  ? 115  PRO   B HG3  1 
ATOM   10666 H  HD2  . PRO   B  2  111 ? 9.098   -35.845 21.175   1.00 76.95  ? 115  PRO   B HD2  1 
ATOM   10667 H  HD3  . PRO   B  2  111 ? 7.913   -36.612 21.907   1.00 76.95  ? 115  PRO   B HD3  1 
ATOM   10668 N  N    . VAL   B  2  112 ? 7.609   -38.646 16.966   1.00 53.78  ? 116  VAL   B N    1 
ATOM   10669 C  CA   . VAL   B  2  112 ? 8.125   -38.905 15.626   1.00 53.64  ? 116  VAL   B CA   1 
ATOM   10670 C  C    . VAL   B  2  112 ? 6.978   -38.762 14.633   1.00 58.45  ? 116  VAL   B C    1 
ATOM   10671 O  O    . VAL   B  2  112 ? 6.031   -39.557 14.656   1.00 61.45  ? 116  VAL   B O    1 
ATOM   10672 C  CB   . VAL   B  2  112 ? 8.761   -40.299 15.506   1.00 50.82  ? 116  VAL   B CB   1 
ATOM   10673 C  CG1  . VAL   B  2  112 ? 9.263   -40.541 14.085   1.00 45.30  ? 116  VAL   B CG1  1 
ATOM   10674 C  CG2  . VAL   B  2  112 ? 9.892   -40.458 16.512   1.00 50.86  ? 116  VAL   B CG2  1 
ATOM   10675 H  H    . VAL   B  2  112 ? 6.821   -38.964 17.097   1.00 64.57  ? 116  VAL   B H    1 
ATOM   10676 H  HA   . VAL   B  2  112 ? 8.789   -38.231 15.412   1.00 64.40  ? 116  VAL   B HA   1 
ATOM   10677 H  HB   . VAL   B  2  112 ? 8.087   -40.968 15.703   1.00 61.02  ? 116  VAL   B HB   1 
ATOM   10678 H  HG11 . VAL   B  2  112 ? 9.701   -41.406 14.048   1.00 54.39  ? 116  VAL   B HG11 1 
ATOM   10679 H  HG12 . VAL   B  2  112 ? 8.508   -40.527 13.477   1.00 54.39  ? 116  VAL   B HG12 1 
ATOM   10680 H  HG13 . VAL   B  2  112 ? 9.892   -39.842 13.849   1.00 54.39  ? 116  VAL   B HG13 1 
ATOM   10681 H  HG21 . VAL   B  2  112 ? 10.278  -41.343 16.417   1.00 61.07  ? 116  VAL   B HG21 1 
ATOM   10682 H  HG22 . VAL   B  2  112 ? 10.567  -39.783 16.338   1.00 61.07  ? 116  VAL   B HG22 1 
ATOM   10683 H  HG23 . VAL   B  2  112 ? 9.536   -40.346 17.408   1.00 61.07  ? 116  VAL   B HG23 1 
ATOM   10684 N  N    . ASP   B  2  113 ? 7.063   -37.759 13.763   1.00 58.69  ? 117  ASP   B N    1 
ATOM   10685 C  CA   . ASP   B  2  113 ? 6.195   -37.664 12.600   1.00 57.64  ? 117  ASP   B CA   1 
ATOM   10686 C  C    . ASP   B  2  113 ? 6.879   -38.317 11.407   1.00 57.29  ? 117  ASP   B C    1 
ATOM   10687 O  O    . ASP   B  2  113 ? 8.079   -38.128 11.186   1.00 60.29  ? 117  ASP   B O    1 
ATOM   10688 C  CB   . ASP   B  2  113 ? 5.873   -36.208 12.268   1.00 56.41  ? 117  ASP   B CB   1 
ATOM   10689 C  CG   . ASP   B  2  113 ? 5.064   -35.526 13.348   1.00 59.57  ? 117  ASP   B CG   1 
ATOM   10690 O  OD1  . ASP   B  2  113 ? 4.384   -36.229 14.124   1.00 59.73  ? 117  ASP   B OD1  1 
ATOM   10691 O  OD2  . ASP   B  2  113 ? 5.105   -34.280 13.409   1.00 58.01  ? 117  ASP   B OD2  1 
ATOM   10692 H  H    . ASP   B  2  113 ? 7.625   -37.112 13.828   1.00 70.47  ? 117  ASP   B H    1 
ATOM   10693 H  HA   . ASP   B  2  113 ? 5.358   -38.120 12.783   1.00 69.20  ? 117  ASP   B HA   1 
ATOM   10694 H  HB2  . ASP   B  2  113 ? 6.703   -35.717 12.160   1.00 67.73  ? 117  ASP   B HB2  1 
ATOM   10695 H  HB3  . ASP   B  2  113 ? 5.360   -36.177 11.445   1.00 67.73  ? 117  ASP   B HB3  1 
ATOM   10696 N  N    . LEU   B  2  114 ? 6.113   -39.087 10.638   1.00 55.60  ? 118  LEU   B N    1 
ATOM   10697 C  CA   . LEU   B  2  114 ? 6.613   -39.710 9.419    1.00 51.61  ? 118  LEU   B CA   1 
ATOM   10698 C  C    . LEU   B  2  114 ? 5.606   -39.482 8.304    1.00 48.96  ? 118  LEU   B C    1 
ATOM   10699 O  O    . LEU   B  2  114 ? 4.464   -39.942 8.393    1.00 49.39  ? 118  LEU   B O    1 
ATOM   10700 C  CB   . LEU   B  2  114 ? 6.861   -41.209 9.618    1.00 55.72  ? 118  LEU   B CB   1 
ATOM   10701 C  CG   . LEU   B  2  114 ? 7.562   -41.904 8.447    1.00 57.24  ? 118  LEU   B CG   1 
ATOM   10702 C  CD1  . LEU   B  2  114 ? 8.461   -43.020 8.948    1.00 57.12  ? 118  LEU   B CD1  1 
ATOM   10703 C  CD2  . LEU   B  2  114 ? 6.557   -42.455 7.444    1.00 59.27  ? 118  LEU   B CD2  1 
ATOM   10704 H  H    . LEU   B  2  114 ? 5.288   -39.264 10.806   1.00 66.76  ? 118  LEU   B H    1 
ATOM   10705 H  HA   . LEU   B  2  114 ? 7.451   -39.293 9.167    1.00 61.97  ? 118  LEU   B HA   1 
ATOM   10706 H  HB2  . LEU   B  2  114 ? 7.419   -41.326 10.404   1.00 66.90  ? 118  LEU   B HB2  1 
ATOM   10707 H  HB3  . LEU   B  2  114 ? 6.006   -41.648 9.750    1.00 66.90  ? 118  LEU   B HB3  1 
ATOM   10708 H  HG   . LEU   B  2  114 ? 8.108   -41.246 7.988    1.00 68.73  ? 118  LEU   B HG   1 
ATOM   10709 H  HD11 . LEU   B  2  114 ? 8.897   -43.438 8.190    1.00 68.58  ? 118  LEU   B HD11 1 
ATOM   10710 H  HD12 . LEU   B  2  114 ? 9.125   -42.644 9.547    1.00 68.58  ? 118  LEU   B HD12 1 
ATOM   10711 H  HD13 . LEU   B  2  114 ? 7.920   -43.672 9.421    1.00 68.58  ? 118  LEU   B HD13 1 
ATOM   10712 H  HD21 . LEU   B  2  114 ? 7.038   -42.882 6.718    1.00 71.17  ? 118  LEU   B HD21 1 
ATOM   10713 H  HD22 . LEU   B  2  114 ? 5.989   -43.102 7.890    1.00 71.17  ? 118  LEU   B HD22 1 
ATOM   10714 H  HD23 . LEU   B  2  114 ? 6.020   -41.724 7.101    1.00 71.17  ? 118  LEU   B HD23 1 
ATOM   10715 N  N    . TYR   B  2  115 ? 6.027   -38.784 7.255    1.00 46.12  ? 119  TYR   B N    1 
ATOM   10716 C  CA   . TYR   B  2  115 ? 5.199   -38.578 6.075    1.00 45.08  ? 119  TYR   B CA   1 
ATOM   10717 C  C    . TYR   B  2  115 ? 5.695   -39.495 4.962    1.00 45.57  ? 119  TYR   B C    1 
ATOM   10718 O  O    . TYR   B  2  115 ? 6.852   -39.397 4.538    1.00 43.67  ? 119  TYR   B O    1 
ATOM   10719 C  CB   . TYR   B  2  115 ? 5.222   -37.118 5.628    1.00 44.51  ? 119  TYR   B CB   1 
ATOM   10720 C  CG   . TYR   B  2  115 ? 4.152   -36.790 4.612    1.00 45.28  ? 119  TYR   B CG   1 
ATOM   10721 C  CD1  . TYR   B  2  115 ? 2.818   -36.701 4.987    1.00 48.48  ? 119  TYR   B CD1  1 
ATOM   10722 C  CD2  . TYR   B  2  115 ? 4.475   -36.574 3.280    1.00 46.78  ? 119  TYR   B CD2  1 
ATOM   10723 C  CE1  . TYR   B  2  115 ? 1.836   -36.404 4.061    1.00 49.46  ? 119  TYR   B CE1  1 
ATOM   10724 C  CE2  . TYR   B  2  115 ? 3.503   -36.277 2.350    1.00 48.14  ? 119  TYR   B CE2  1 
ATOM   10725 C  CZ   . TYR   B  2  115 ? 2.188   -36.193 2.744    1.00 48.53  ? 119  TYR   B CZ   1 
ATOM   10726 O  OH   . TYR   B  2  115 ? 1.225   -35.896 1.811    1.00 52.65  ? 119  TYR   B OH   1 
ATOM   10727 H  H    . TYR   B  2  115 ? 6.802   -38.414 7.203    1.00 55.38  ? 119  TYR   B H    1 
ATOM   10728 H  HA   . TYR   B  2  115 ? 4.279   -38.810 6.280    1.00 54.13  ? 119  TYR   B HA   1 
ATOM   10729 H  HB2  . TYR   B  2  115 ? 5.083   -36.550 6.402    1.00 53.44  ? 119  TYR   B HB2  1 
ATOM   10730 H  HB3  . TYR   B  2  115 ? 6.084   -36.926 5.227    1.00 53.44  ? 119  TYR   B HB3  1 
ATOM   10731 H  HD1  . TYR   B  2  115 ? 2.581   -36.843 5.875    1.00 58.21  ? 119  TYR   B HD1  1 
ATOM   10732 H  HD2  . TYR   B  2  115 ? 5.363   -36.631 3.011    1.00 56.17  ? 119  TYR   B HD2  1 
ATOM   10733 H  HE1  . TYR   B  2  115 ? 0.946   -36.348 4.324    1.00 59.39  ? 119  TYR   B HE1  1 
ATOM   10734 H  HE2  . TYR   B  2  115 ? 3.734   -36.134 1.460    1.00 57.80  ? 119  TYR   B HE2  1 
ATOM   10735 H  HH   . TYR   B  2  115 ? 0.462   -35.953 2.157    1.00 63.22  ? 119  TYR   B HH   1 
ATOM   10736 N  N    . TYR   B  2  116 ? 4.819   -40.384 4.501    1.00 45.27  ? 120  TYR   B N    1 
ATOM   10737 C  CA   . TYR   B  2  116 ? 5.149   -41.367 3.473    1.00 47.06  ? 120  TYR   B CA   1 
ATOM   10738 C  C    . TYR   B  2  116 ? 4.788   -40.776 2.115    1.00 51.44  ? 120  TYR   B C    1 
ATOM   10739 O  O    . TYR   B  2  116 ? 3.607   -40.678 1.766    1.00 50.79  ? 120  TYR   B O    1 
ATOM   10740 C  CB   . TYR   B  2  116 ? 4.398   -42.670 3.739    1.00 48.70  ? 120  TYR   B CB   1 
ATOM   10741 C  CG   . TYR   B  2  116 ? 4.907   -43.888 2.995    1.00 52.51  ? 120  TYR   B CG   1 
ATOM   10742 C  CD1  . TYR   B  2  116 ? 4.392   -44.233 1.751    1.00 54.95  ? 120  TYR   B CD1  1 
ATOM   10743 C  CD2  . TYR   B  2  116 ? 5.879   -44.711 3.550    1.00 55.58  ? 120  TYR   B CD2  1 
ATOM   10744 C  CE1  . TYR   B  2  116 ? 4.845   -45.352 1.074    1.00 56.39  ? 120  TYR   B CE1  1 
ATOM   10745 C  CE2  . TYR   B  2  116 ? 6.337   -45.833 2.881    1.00 57.90  ? 120  TYR   B CE2  1 
ATOM   10746 C  CZ   . TYR   B  2  116 ? 5.814   -46.150 1.645    1.00 57.43  ? 120  TYR   B CZ   1 
ATOM   10747 O  OH   . TYR   B  2  116 ? 6.269   -47.263 0.976    1.00 59.31  ? 120  TYR   B OH   1 
ATOM   10748 H  H    . TYR   B  2  116 ? 4.006   -40.440 4.775    1.00 54.36  ? 120  TYR   B H    1 
ATOM   10749 H  HA   . TYR   B  2  116 ? 6.101   -41.556 3.479    1.00 56.51  ? 120  TYR   B HA   1 
ATOM   10750 H  HB2  . TYR   B  2  116 ? 4.457   -42.867 4.687    1.00 58.47  ? 120  TYR   B HB2  1 
ATOM   10751 H  HB3  . TYR   B  2  116 ? 3.471   -42.544 3.483    1.00 58.47  ? 120  TYR   B HB3  1 
ATOM   10752 H  HD1  . TYR   B  2  116 ? 3.732   -43.702 1.367    1.00 65.98  ? 120  TYR   B HD1  1 
ATOM   10753 H  HD2  . TYR   B  2  116 ? 6.229   -44.504 4.386    1.00 66.73  ? 120  TYR   B HD2  1 
ATOM   10754 H  HE1  . TYR   B  2  116 ? 4.497   -45.565 0.238    1.00 67.71  ? 120  TYR   B HE1  1 
ATOM   10755 H  HE2  . TYR   B  2  116 ? 6.993   -46.370 3.262    1.00 69.52  ? 120  TYR   B HE2  1 
ATOM   10756 H  HH   . TYR   B  2  116 ? 6.099   -47.195 0.156    1.00 71.21  ? 120  TYR   B HH   1 
ATOM   10757 N  N    . LEU   B  2  117 ? 5.804   -40.376 1.354    1.00 52.85  ? 121  LEU   B N    1 
ATOM   10758 C  CA   . LEU   B  2  117 ? 5.628   -39.741 0.052    1.00 49.89  ? 121  LEU   B CA   1 
ATOM   10759 C  C    . LEU   B  2  117 ? 6.053   -40.728 -1.026   1.00 52.89  ? 121  LEU   B C    1 
ATOM   10760 O  O    . LEU   B  2  117 ? 7.221   -41.129 -1.075   1.00 53.64  ? 121  LEU   B O    1 
ATOM   10761 C  CB   . LEU   B  2  117 ? 6.446   -38.454 -0.033   1.00 47.72  ? 121  LEU   B CB   1 
ATOM   10762 C  CG   . LEU   B  2  117 ? 6.371   -37.687 -1.351   1.00 51.37  ? 121  LEU   B CG   1 
ATOM   10763 C  CD1  . LEU   B  2  117 ? 4.927   -37.393 -1.723   1.00 54.80  ? 121  LEU   B CD1  1 
ATOM   10764 C  CD2  . LEU   B  2  117 ? 7.174   -36.404 -1.236   1.00 51.52  ? 121  LEU   B CD2  1 
ATOM   10765 H  H    . LEU   B  2  117 ? 6.629   -40.465 1.578    1.00 63.45  ? 121  LEU   B H    1 
ATOM   10766 H  HA   . LEU   B  2  117 ? 4.695   -39.518 -0.088   1.00 59.90  ? 121  LEU   B HA   1 
ATOM   10767 H  HB2  . LEU   B  2  117 ? 6.136   -37.855 0.664    1.00 57.30  ? 121  LEU   B HB2  1 
ATOM   10768 H  HB3  . LEU   B  2  117 ? 7.378   -38.680 0.114    1.00 57.30  ? 121  LEU   B HB3  1 
ATOM   10769 H  HG   . LEU   B  2  117 ? 6.749   -38.226 -2.064   1.00 61.68  ? 121  LEU   B HG   1 
ATOM   10770 H  HD11 . LEU   B  2  117 ? 4.909   -36.913 -2.565   1.00 65.80  ? 121  LEU   B HD11 1 
ATOM   10771 H  HD12 . LEU   B  2  117 ? 4.446   -38.231 -1.809   1.00 65.80  ? 121  LEU   B HD12 1 
ATOM   10772 H  HD13 . LEU   B  2  117 ? 4.525   -36.852 -1.025   1.00 65.80  ? 121  LEU   B HD13 1 
ATOM   10773 H  HD21 . LEU   B  2  117 ? 7.125   -35.924 -2.077   1.00 61.86  ? 121  LEU   B HD21 1 
ATOM   10774 H  HD22 . LEU   B  2  117 ? 6.802   -35.862 -0.523   1.00 61.86  ? 121  LEU   B HD22 1 
ATOM   10775 H  HD23 . LEU   B  2  117 ? 8.097   -36.626 -1.035   1.00 61.86  ? 121  LEU   B HD23 1 
ATOM   10776 N  N    . MET   B  2  118 ? 5.114   -41.109 -1.893   1.00 52.39  ? 122  MET   B N    1 
ATOM   10777 C  CA   . MET   B  2  118 ? 5.298   -42.271 -2.751   1.00 50.49  ? 122  MET   B CA   1 
ATOM   10778 C  C    . MET   B  2  118 ? 5.083   -41.937 -4.220   1.00 48.36  ? 122  MET   B C    1 
ATOM   10779 O  O    . MET   B  2  118 ? 4.123   -41.248 -4.581   1.00 46.63  ? 122  MET   B O    1 
ATOM   10780 C  CB   . MET   B  2  118 ? 4.344   -43.396 -2.334   1.00 50.95  ? 122  MET   B CB   1 
ATOM   10781 C  CG   . MET   B  2  118 ? 4.535   -44.683 -3.110   1.00 52.87  ? 122  MET   B CG   1 
ATOM   10782 S  SD   . MET   B  2  118 ? 3.495   -46.019 -2.498   1.00 57.05  ? 122  MET   B SD   1 
ATOM   10783 C  CE   . MET   B  2  118 ? 3.767   -47.255 -3.764   1.00 59.16  ? 122  MET   B CE   1 
ATOM   10784 H  H    . MET   B  2  118 ? 4.362   -40.706 -2.000   1.00 62.91  ? 122  MET   B H    1 
ATOM   10785 H  HA   . MET   B  2  118 ? 6.219   -42.562 -2.658   1.00 60.62  ? 122  MET   B HA   1 
ATOM   10786 H  HB2  . MET   B  2  118 ? 4.488   -43.593 -1.395   1.00 61.17  ? 122  MET   B HB2  1 
ATOM   10787 H  HB3  . MET   B  2  118 ? 3.432   -43.098 -2.475   1.00 61.17  ? 122  MET   B HB3  1 
ATOM   10788 H  HG2  . MET   B  2  118 ? 4.310   -44.528 -4.040   1.00 63.49  ? 122  MET   B HG2  1 
ATOM   10789 H  HG3  . MET   B  2  118 ? 5.461   -44.964 -3.034   1.00 63.49  ? 122  MET   B HG3  1 
ATOM   10790 H  HE1  . MET   B  2  118 ? 3.194   -48.018 -3.588   1.00 71.03  ? 122  MET   B HE1  1 
ATOM   10791 H  HE2  . MET   B  2  118 ? 3.553   -46.874 -4.630   1.00 71.03  ? 122  MET   B HE2  1 
ATOM   10792 H  HE3  . MET   B  2  118 ? 4.697   -47.529 -3.743   1.00 71.03  ? 122  MET   B HE3  1 
ATOM   10793 N  N    . ASP   B  2  119 ? 5.997   -42.432 -5.053   1.00 47.76  ? 123  ASP   B N    1 
ATOM   10794 C  CA   . ASP   B  2  119 ? 5.802   -42.493 -6.495   1.00 50.36  ? 123  ASP   B CA   1 
ATOM   10795 C  C    . ASP   B  2  119 ? 4.635   -43.419 -6.820   1.00 53.30  ? 123  ASP   B C    1 
ATOM   10796 O  O    . ASP   B  2  119 ? 4.613   -44.574 -6.389   1.00 56.04  ? 123  ASP   B O    1 
ATOM   10797 C  CB   . ASP   B  2  119 ? 7.097   -43.004 -7.136   1.00 50.78  ? 123  ASP   B CB   1 
ATOM   10798 C  CG   . ASP   B  2  119 ? 7.047   -43.040 -8.650   1.00 50.84  ? 123  ASP   B CG   1 
ATOM   10799 O  OD1  . ASP   B  2  119 ? 5.944   -42.990 -9.230   1.00 51.03  ? 123  ASP   B OD1  1 
ATOM   10800 O  OD2  . ASP   B  2  119 ? 8.131   -43.134 -9.265   1.00 49.42  ? 123  ASP   B OD2  1 
ATOM   10801 H  H    . ASP   B  2  119 ? 6.757   -42.746 -4.800   1.00 57.35  ? 123  ASP   B H    1 
ATOM   10802 H  HA   . ASP   B  2  119 ? 5.596   -41.617 -6.857   1.00 60.47  ? 123  ASP   B HA   1 
ATOM   10803 H  HB2  . ASP   B  2  119 ? 7.827   -42.420 -6.876   1.00 60.98  ? 123  ASP   B HB2  1 
ATOM   10804 H  HB3  . ASP   B  2  119 ? 7.267   -43.906 -6.822   1.00 60.98  ? 123  ASP   B HB3  1 
ATOM   10805 N  N    . LEU   B  2  120 ? 3.652   -42.912 -7.573   1.00 52.83  ? 124  LEU   B N    1 
ATOM   10806 C  CA   . LEU   B  2  120 ? 2.512   -43.723 -7.993   1.00 58.86  ? 124  LEU   B CA   1 
ATOM   10807 C  C    . LEU   B  2  120 ? 2.432   -43.869 -9.511   1.00 62.53  ? 124  LEU   B C    1 
ATOM   10808 O  O    . LEU   B  2  120 ? 1.349   -44.121 -10.049  1.00 61.63  ? 124  LEU   B O    1 
ATOM   10809 C  CB   . LEU   B  2  120 ? 1.198   -43.151 -7.450   1.00 59.26  ? 124  LEU   B CB   1 
ATOM   10810 C  CG   . LEU   B  2  120 ? 0.799   -43.503 -6.011   1.00 60.97  ? 124  LEU   B CG   1 
ATOM   10811 C  CD1  . LEU   B  2  120 ? -0.615  -43.012 -5.725   1.00 68.06  ? 124  LEU   B CD1  1 
ATOM   10812 C  CD2  . LEU   B  2  120 ? 0.888   -45.000 -5.733   1.00 59.43  ? 124  LEU   B CD2  1 
ATOM   10813 H  H    . LEU   B  2  120 ? 3.626   -42.099 -7.852   1.00 63.44  ? 124  LEU   B H    1 
ATOM   10814 H  HA   . LEU   B  2  120 ? 2.627   -44.610 -7.616   1.00 70.67  ? 124  LEU   B HA   1 
ATOM   10815 H  HB2  . LEU   B  2  120 ? 1.258   -42.184 -7.494   1.00 71.15  ? 124  LEU   B HB2  1 
ATOM   10816 H  HB3  . LEU   B  2  120 ? 0.481   -43.465 -8.023   1.00 71.15  ? 124  LEU   B HB3  1 
ATOM   10817 H  HG   . LEU   B  2  120 ? 1.425   -43.062 -5.415   1.00 73.20  ? 124  LEU   B HG   1 
ATOM   10818 H  HD11 . LEU   B  2  120 ? -0.825  -43.180 -4.793   1.00 81.71  ? 124  LEU   B HD11 1 
ATOM   10819 H  HD12 . LEU   B  2  120 ? -0.662  -42.061 -5.908   1.00 81.71  ? 124  LEU   B HD12 1 
ATOM   10820 H  HD13 . LEU   B  2  120 ? -1.237  -43.490 -6.295   1.00 81.71  ? 124  LEU   B HD13 1 
ATOM   10821 H  HD21 . LEU   B  2  120 ? 0.572   -45.173 -4.833   1.00 71.35  ? 124  LEU   B HD21 1 
ATOM   10822 H  HD22 . LEU   B  2  120 ? 0.336   -45.474 -6.375   1.00 71.35  ? 124  LEU   B HD22 1 
ATOM   10823 H  HD23 . LEU   B  2  120 ? 1.812   -45.282 -5.819   1.00 71.35  ? 124  LEU   B HD23 1 
ATOM   10824 N  N    . SER   B  2  121 ? 3.550   -43.727 -10.215  1.00 66.47  ? 125  SER   B N    1 
ATOM   10825 C  CA   . SER   B  2  121 ? 3.559   -44.086 -11.623  1.00 65.23  ? 125  SER   B CA   1 
ATOM   10826 C  C    . SER   B  2  121 ? 3.342   -45.595 -11.765  1.00 61.06  ? 125  SER   B C    1 
ATOM   10827 O  O    . SER   B  2  121 ? 3.310   -46.343 -10.784  1.00 58.07  ? 125  SER   B O    1 
ATOM   10828 C  CB   . SER   B  2  121 ? 4.862   -43.641 -12.287  1.00 66.60  ? 125  SER   B CB   1 
ATOM   10829 O  OG   . SER   B  2  121 ? 5.995   -44.241 -11.685  1.00 71.71  ? 125  SER   B OG   1 
ATOM   10830 H  H    . SER   B  2  121 ? 4.297   -43.433 -9.906   1.00 79.80  ? 125  SER   B H    1 
ATOM   10831 H  HA   . SER   B  2  121 ? 2.839   -43.632 -12.088  1.00 78.31  ? 125  SER   B HA   1 
ATOM   10832 H  HB2  . SER   B  2  121 ? 4.836   -43.893 -13.223  1.00 79.95  ? 125  SER   B HB2  1 
ATOM   10833 H  HB3  . SER   B  2  121 ? 4.939   -42.677 -12.205  1.00 79.95  ? 125  SER   B HB3  1 
ATOM   10834 N  N    . ALA   B  2  122 ? 3.193   -46.042 -13.013  1.00 60.02  ? 126  ALA   B N    1 
ATOM   10835 C  CA   . ALA   B  2  122 ? 2.691   -47.392 -13.254  1.00 55.47  ? 126  ALA   B CA   1 
ATOM   10836 C  C    . ALA   B  2  122 ? 3.608   -48.467 -12.682  1.00 55.09  ? 126  ALA   B C    1 
ATOM   10837 O  O    . ALA   B  2  122 ? 3.138   -49.560 -12.344  1.00 55.86  ? 126  ALA   B O    1 
ATOM   10838 C  CB   . ALA   B  2  122 ? 2.488   -47.611 -14.753  1.00 53.14  ? 126  ALA   B CB   1 
ATOM   10839 H  H    . ALA   B  2  122 ? 3.371   -45.592 -13.724  1.00 72.07  ? 126  ALA   B H    1 
ATOM   10840 H  HA   . ALA   B  2  122 ? 1.832   -47.479 -12.810  1.00 66.60  ? 126  ALA   B HA   1 
ATOM   10841 H  HB1  . ALA   B  2  122 ? 2.205   -48.527 -14.902  1.00 63.80  ? 126  ALA   B HB1  1 
ATOM   10842 H  HB2  . ALA   B  2  122 ? 1.808   -46.998 -15.073  1.00 63.80  ? 126  ALA   B HB2  1 
ATOM   10843 H  HB3  . ALA   B  2  122 ? 3.326   -47.445 -15.212  1.00 63.80  ? 126  ALA   B HB3  1 
ATOM   10844 N  N    . SER   B  2  123 ? 4.905   -48.192 -12.558  1.00 51.39  ? 127  SER   B N    1 
ATOM   10845 C  CA   . SER   B  2  123 ? 5.833   -49.207 -12.073  1.00 49.83  ? 127  SER   B CA   1 
ATOM   10846 C  C    . SER   B  2  123 ? 5.736   -49.442 -10.569  1.00 53.11  ? 127  SER   B C    1 
ATOM   10847 O  O    . SER   B  2  123 ? 6.510   -50.247 -10.036  1.00 54.00  ? 127  SER   B O    1 
ATOM   10848 C  CB   . SER   B  2  123 ? 7.270   -48.824 -12.441  1.00 50.27  ? 127  SER   B CB   1 
ATOM   10849 O  OG   . SER   B  2  123 ? 7.657   -47.617 -11.809  1.00 51.59  ? 127  SER   B OG   1 
ATOM   10850 H  H    . SER   B  2  123 ? 5.266   -47.435 -12.747  1.00 61.71  ? 127  SER   B H    1 
ATOM   10851 H  HA   . SER   B  2  123 ? 5.624   -50.045 -12.515  1.00 59.84  ? 127  SER   B HA   1 
ATOM   10852 H  HB2  . SER   B  2  123 ? 7.867   -49.534 -12.155  1.00 60.36  ? 127  SER   B HB2  1 
ATOM   10853 H  HB3  . SER   B  2  123 ? 7.328   -48.708 -13.402  1.00 60.36  ? 127  SER   B HB3  1 
ATOM   10854 H  HG   . SER   B  2  123 ? 8.039   -47.785 -11.080  1.00 61.95  ? 127  SER   B HG   1 
ATOM   10855 N  N    . MET   B  2  124 ? 4.809   -48.776 -9.878   1.00 55.38  ? 128  MET   B N    1 
ATOM   10856 C  CA   . MET   B  2  124 ? 4.654   -48.910 -8.435   1.00 59.32  ? 128  MET   B CA   1 
ATOM   10857 C  C    . MET   B  2  124 ? 3.348   -49.596 -8.051   1.00 61.90  ? 128  MET   B C    1 
ATOM   10858 O  O    . MET   B  2  124 ? 2.963   -49.562 -6.877   1.00 60.20  ? 128  MET   B O    1 
ATOM   10859 C  CB   . MET   B  2  124 ? 4.738   -47.533 -7.773   1.00 58.43  ? 128  MET   B CB   1 
ATOM   10860 C  CG   . MET   B  2  124 ? 5.996   -46.750 -8.132   1.00 58.38  ? 128  MET   B CG   1 
ATOM   10861 S  SD   . MET   B  2  124 ? 7.494   -47.413 -7.376   1.00 58.26  ? 128  MET   B SD   1 
ATOM   10862 C  CE   . MET   B  2  124 ? 7.198   -47.047 -5.647   1.00 55.91  ? 128  MET   B CE   1 
ATOM   10863 H  H    . MET   B  2  124 ? 4.248   -48.230 -10.234  1.00 66.50  ? 128  MET   B H    1 
ATOM   10864 H  HA   . MET   B  2  124 ? 5.388   -49.447 -8.098   1.00 71.23  ? 128  MET   B HA   1 
ATOM   10865 H  HB2  . MET   B  2  124 ? 3.973   -47.007 -8.052   1.00 70.16  ? 128  MET   B HB2  1 
ATOM   10866 H  HB3  . MET   B  2  124 ? 4.728   -47.650 -6.810   1.00 70.16  ? 128  MET   B HB3  1 
ATOM   10867 H  HG2  . MET   B  2  124 ? 6.115   -46.771 -9.094   1.00 70.09  ? 128  MET   B HG2  1 
ATOM   10868 H  HG3  . MET   B  2  124 ? 5.892   -45.834 -7.831   1.00 70.09  ? 128  MET   B HG3  1 
ATOM   10869 H  HE1  . MET   B  2  124 ? 7.945   -47.376 -5.122   1.00 67.13  ? 128  MET   B HE1  1 
ATOM   10870 H  HE2  . MET   B  2  124 ? 7.113   -46.087 -5.537   1.00 67.13  ? 128  MET   B HE2  1 
ATOM   10871 H  HE3  . MET   B  2  124 ? 6.379   -47.486 -5.367   1.00 67.13  ? 128  MET   B HE3  1 
ATOM   10872 N  N    . ASP   B  2  125 ? 2.655   -50.212 -9.012   1.00 66.94  ? 129  ASP   B N    1 
ATOM   10873 C  CA   . ASP   B  2  125 ? 1.437   -50.948 -8.690   1.00 71.97  ? 129  ASP   B CA   1 
ATOM   10874 C  C    . ASP   B  2  125 ? 1.733   -52.113 -7.756   1.00 73.28  ? 129  ASP   B C    1 
ATOM   10875 O  O    . ASP   B  2  125 ? 1.007   -52.340 -6.781   1.00 76.00  ? 129  ASP   B O    1 
ATOM   10876 C  CB   . ASP   B  2  125 ? 0.778   -51.447 -9.976   1.00 78.75  ? 129  ASP   B CB   1 
ATOM   10877 C  CG   . ASP   B  2  125 ? -0.540  -52.152 -9.724   1.00 86.54  ? 129  ASP   B CG   1 
ATOM   10878 O  OD1  . ASP   B  2  125 ? -1.544  -51.462 -9.446   1.00 89.12  ? 129  ASP   B OD1  1 
ATOM   10879 O  OD2  . ASP   B  2  125 ? -0.574  -53.398 -9.808   1.00 92.30  ? 129  ASP   B OD2  1 
ATOM   10880 H  H    . ASP   B  2  125 ? 2.867   -50.218 -9.845   1.00 80.37  ? 129  ASP   B H    1 
ATOM   10881 H  HA   . ASP   B  2  125 ? 0.815   -50.352 -8.243   1.00 86.40  ? 129  ASP   B HA   1 
ATOM   10882 H  HB2  . ASP   B  2  125 ? 0.606   -50.690 -10.558  1.00 94.54  ? 129  ASP   B HB2  1 
ATOM   10883 H  HB3  . ASP   B  2  125 ? 1.375   -52.073 -10.414  1.00 94.54  ? 129  ASP   B HB3  1 
ATOM   10884 N  N    . ASP   B  2  126 ? 2.795   -52.869 -8.044   1.00 69.14  ? 130  ASP   B N    1 
ATOM   10885 C  CA   . ASP   B  2  126 ? 3.201   -53.945 -7.148   1.00 66.37  ? 130  ASP   B CA   1 
ATOM   10886 C  C    . ASP   B  2  126 ? 3.543   -53.404 -5.767   1.00 63.02  ? 130  ASP   B C    1 
ATOM   10887 O  O    . ASP   B  2  126 ? 3.190   -54.009 -4.747   1.00 65.40  ? 130  ASP   B O    1 
ATOM   10888 C  CB   . ASP   B  2  126 ? 4.398   -54.691 -7.737   1.00 68.42  ? 130  ASP   B CB   1 
ATOM   10889 C  CG   . ASP   B  2  126 ? 5.554   -53.764 -8.064   1.00 67.72  ? 130  ASP   B CG   1 
ATOM   10890 O  OD1  . ASP   B  2  126 ? 5.296   -52.672 -8.609   1.00 69.62  ? 130  ASP   B OD1  1 
ATOM   10891 O  OD2  . ASP   B  2  126 ? 6.716   -54.116 -7.771   1.00 69.24  ? 130  ASP   B OD2  1 
ATOM   10892 H  H    . ASP   B  2  126 ? 3.289   -52.779 -8.743   1.00 83.01  ? 130  ASP   B H    1 
ATOM   10893 H  HA   . ASP   B  2  126 ? 2.468   -54.573 -7.056   1.00 79.68  ? 130  ASP   B HA   1 
ATOM   10894 H  HB2  . ASP   B  2  126 ? 4.711   -55.347 -7.095   1.00 82.14  ? 130  ASP   B HB2  1 
ATOM   10895 H  HB3  . ASP   B  2  126 ? 4.125   -55.132 -8.556   1.00 82.14  ? 130  ASP   B HB3  1 
ATOM   10896 N  N    . ASP   B  2  127 ? 4.232   -52.261 -5.714   1.00 57.73  ? 131  ASP   B N    1 
ATOM   10897 C  CA   . ASP   B  2  127 ? 4.603   -51.680 -4.429   1.00 56.97  ? 131  ASP   B CA   1 
ATOM   10898 C  C    . ASP   B  2  127 ? 3.377   -51.418 -3.564   1.00 57.79  ? 131  ASP   B C    1 
ATOM   10899 O  O    . ASP   B  2  127 ? 3.440   -51.558 -2.337   1.00 59.25  ? 131  ASP   B O    1 
ATOM   10900 C  CB   . ASP   B  2  127 ? 5.387   -50.386 -4.656   1.00 54.82  ? 131  ASP   B CB   1 
ATOM   10901 C  CG   . ASP   B  2  127 ? 6.647   -50.605 -5.470   1.00 56.39  ? 131  ASP   B CG   1 
ATOM   10902 O  OD1  . ASP   B  2  127 ? 6.535   -50.998 -6.650   1.00 56.53  ? 131  ASP   B OD1  1 
ATOM   10903 O  OD2  . ASP   B  2  127 ? 7.751   -50.384 -4.929   1.00 57.58  ? 131  ASP   B OD2  1 
ATOM   10904 H  H    . ASP   B  2  127 ? 4.492   -51.811 -6.399   1.00 69.32  ? 131  ASP   B H    1 
ATOM   10905 H  HA   . ASP   B  2  127 ? 5.178   -52.298 -3.952   1.00 68.40  ? 131  ASP   B HA   1 
ATOM   10906 H  HB2  . ASP   B  2  127 ? 4.826   -49.755 -5.134   1.00 65.83  ? 131  ASP   B HB2  1 
ATOM   10907 H  HB3  . ASP   B  2  127 ? 5.645   -50.016 -3.797   1.00 65.83  ? 131  ASP   B HB3  1 
ATOM   10908 N  N    . LEU   B  2  128 ? 2.254   -51.047 -4.182   1.00 57.25  ? 132  LEU   B N    1 
ATOM   10909 C  CA   . LEU   B  2  128 ? 1.041   -50.784 -3.415   1.00 62.07  ? 132  LEU   B CA   1 
ATOM   10910 C  C    . LEU   B  2  128 ? 0.478   -52.062 -2.805   1.00 70.40  ? 132  LEU   B C    1 
ATOM   10911 O  O    . LEU   B  2  128 ? -0.007  -52.052 -1.668   1.00 72.23  ? 132  LEU   B O    1 
ATOM   10912 C  CB   . LEU   B  2  128 ? -0.012  -50.120 -4.301   1.00 58.03  ? 132  LEU   B CB   1 
ATOM   10913 C  CG   . LEU   B  2  128 ? 0.035   -48.601 -4.465   1.00 59.09  ? 132  LEU   B CG   1 
ATOM   10914 C  CD1  . LEU   B  2  128 ? -1.066  -48.168 -5.416   1.00 59.50  ? 132  LEU   B CD1  1 
ATOM   10915 C  CD2  . LEU   B  2  128 ? -0.109  -47.892 -3.127   1.00 60.42  ? 132  LEU   B CD2  1 
ATOM   10916 H  H    . LEU   B  2  128 ? 2.171   -50.943 -5.032   1.00 68.74  ? 132  LEU   B H    1 
ATOM   10917 H  HA   . LEU   B  2  128 ? 1.264   -50.174 -2.695   1.00 74.52  ? 132  LEU   B HA   1 
ATOM   10918 H  HB2  . LEU   B  2  128 ? 0.072   -50.499 -5.190   1.00 69.67  ? 132  LEU   B HB2  1 
ATOM   10919 H  HB3  . LEU   B  2  128 ? -0.883  -50.333 -3.931   1.00 69.67  ? 132  LEU   B HB3  1 
ATOM   10920 H  HG   . LEU   B  2  128 ? 0.896   -48.346 -4.831   1.00 70.94  ? 132  LEU   B HG   1 
ATOM   10921 H  HD11 . LEU   B  2  128 ? -1.043  -47.203 -5.507   1.00 71.44  ? 132  LEU   B HD11 1 
ATOM   10922 H  HD12 . LEU   B  2  128 ? -0.921  -48.586 -6.279   1.00 71.44  ? 132  LEU   B HD12 1 
ATOM   10923 H  HD13 . LEU   B  2  128 ? -1.923  -48.445 -5.054   1.00 71.44  ? 132  LEU   B HD13 1 
ATOM   10924 H  HD21 . LEU   B  2  128 ? -0.124  -46.934 -3.277   1.00 72.53  ? 132  LEU   B HD21 1 
ATOM   10925 H  HD22 . LEU   B  2  128 ? -0.937  -48.174 -2.707   1.00 72.53  ? 132  LEU   B HD22 1 
ATOM   10926 H  HD23 . LEU   B  2  128 ? 0.644   -48.127 -2.562   1.00 72.53  ? 132  LEU   B HD23 1 
ATOM   10927 N  N    . ASN   B  2  129 ? 0.524   -53.171 -3.547   1.00 74.32  ? 133  ASN   B N    1 
ATOM   10928 C  CA   . ASN   B  2  129 ? -0.068  -54.408 -3.050   1.00 78.93  ? 133  ASN   B CA   1 
ATOM   10929 C  C    . ASN   B  2  129 ? 0.648   -54.924 -1.809   1.00 76.65  ? 133  ASN   B C    1 
ATOM   10930 O  O    . ASN   B  2  129 ? 0.033   -55.602 -0.978   1.00 79.06  ? 133  ASN   B O    1 
ATOM   10931 C  CB   . ASN   B  2  129 ? -0.051  -55.477 -4.143   1.00 84.30  ? 133  ASN   B CB   1 
ATOM   10932 C  CG   . ASN   B  2  129 ? -1.176  -55.307 -5.142   1.00 89.80  ? 133  ASN   B CG   1 
ATOM   10933 O  OD1  . ASN   B  2  129 ? -2.344  -55.192 -4.768   1.00 92.88  ? 133  ASN   B OD1  1 
ATOM   10934 N  ND2  . ASN   B  2  129 ? -0.830  -55.284 -6.423   1.00 92.78  ? 133  ASN   B ND2  1 
ATOM   10935 H  H    . ASN   B  2  129 ? 0.885   -53.231 -4.325   1.00 89.22  ? 133  ASN   B H    1 
ATOM   10936 H  HA   . ASN   B  2  129 ? -0.991  -54.229 -2.811   1.00 94.76  ? 133  ASN   B HA   1 
ATOM   10937 H  HB2  . ASN   B  2  129 ? 0.789   -55.424 -4.624   1.00 101.20 ? 133  ASN   B HB2  1 
ATOM   10938 H  HB3  . ASN   B  2  129 ? -0.144  -56.351 -3.732   1.00 101.20 ? 133  ASN   B HB3  1 
ATOM   10939 H  HD21 . ASN   B  2  129 ? -1.432  -55.189 -7.029   1.00 111.37 ? 133  ASN   B HD21 1 
ATOM   10940 H  HD22 . ASN   B  2  129 ? -0.003  -55.364 -6.646   1.00 111.37 ? 133  ASN   B HD22 1 
ATOM   10941 N  N    . THR   B  2  130 ? 1.935   -54.619 -1.661   1.00 71.39  ? 134  THR   B N    1 
ATOM   10942 C  CA   . THR   B  2  130 ? 2.717   -55.167 -0.562   1.00 72.31  ? 134  THR   B CA   1 
ATOM   10943 C  C    . THR   B  2  130 ? 2.734   -54.279 0.678    1.00 69.64  ? 134  THR   B C    1 
ATOM   10944 O  O    . THR   B  2  130 ? 3.203   -54.730 1.728    1.00 70.85  ? 134  THR   B O    1 
ATOM   10945 C  CB   . THR   B  2  130 ? 4.161   -55.426 -1.015   1.00 73.59  ? 134  THR   B CB   1 
ATOM   10946 O  OG1  . THR   B  2  130 ? 4.758   -54.201 -1.454   1.00 75.58  ? 134  THR   B OG1  1 
ATOM   10947 C  CG2  . THR   B  2  130 ? 4.196   -56.443 -2.151   1.00 73.87  ? 134  THR   B CG2  1 
ATOM   10948 H  H    . THR   B  2  130 ? 2.376   -54.098 -2.184   1.00 85.71  ? 134  THR   B H    1 
ATOM   10949 H  HA   . THR   B  2  130 ? 2.324   -56.016 -0.307   1.00 86.81  ? 134  THR   B HA   1 
ATOM   10950 H  HB   . THR   B  2  130 ? 4.670   -55.784 -0.271   1.00 88.35  ? 134  THR   B HB   1 
ATOM   10951 H  HG1  . THR   B  2  130 ? 5.310   -54.354 -2.068   1.00 90.74  ? 134  THR   B HG1  1 
ATOM   10952 H  HG21 . THR   B  2  130 ? 5.114   -56.622 -2.407   1.00 88.68  ? 134  THR   B HG21 1 
ATOM   10953 H  HG22 . THR   B  2  130 ? 3.780   -57.272 -1.867   1.00 88.68  ? 134  THR   B HG22 1 
ATOM   10954 H  HG23 . THR   B  2  130 ? 3.716   -56.097 -2.920   1.00 88.68  ? 134  THR   B HG23 1 
ATOM   10955 N  N    . ILE   B  2  131 ? 2.239   -53.045 0.595    1.00 66.95  ? 135  ILE   B N    1 
ATOM   10956 C  CA   . ILE   B  2  131 ? 2.204   -52.151 1.746    1.00 68.39  ? 135  ILE   B CA   1 
ATOM   10957 C  C    . ILE   B  2  131 ? 0.779   -51.971 2.273    1.00 73.23  ? 135  ILE   B C    1 
ATOM   10958 O  O    . ILE   B  2  131 ? 0.492   -50.993 2.960    1.00 68.62  ? 135  ILE   B O    1 
ATOM   10959 C  CB   . ILE   B  2  131 ? 2.846   -50.789 1.426    1.00 64.94  ? 135  ILE   B CB   1 
ATOM   10960 C  CG1  . ILE   B  2  131 ? 2.134   -50.104 0.256    1.00 59.49  ? 135  ILE   B CG1  1 
ATOM   10961 C  CG2  . ILE   B  2  131 ? 4.329   -50.957 1.123    1.00 65.37  ? 135  ILE   B CG2  1 
ATOM   10962 C  CD1  . ILE   B  2  131 ? 2.543   -48.652 0.062    1.00 52.95  ? 135  ILE   B CD1  1 
ATOM   10963 H  H    . ILE   B  2  131 ? 1.915   -52.703 -0.124   1.00 80.37  ? 135  ILE   B H    1 
ATOM   10964 H  HA   . ILE   B  2  131 ? 2.725   -52.566 2.451    1.00 82.11  ? 135  ILE   B HA   1 
ATOM   10965 H  HB   . ILE   B  2  131 ? 2.750   -50.223 2.208    1.00 77.96  ? 135  ILE   B HB   1 
ATOM   10966 H  HG12 . ILE   B  2  131 ? 2.342   -50.583 -0.562   1.00 71.42  ? 135  ILE   B HG12 1 
ATOM   10967 H  HG13 . ILE   B  2  131 ? 1.177   -50.124 0.417    1.00 71.42  ? 135  ILE   B HG13 1 
ATOM   10968 H  HG21 . ILE   B  2  131 ? 4.723   -50.083 0.976    1.00 78.48  ? 135  ILE   B HG21 1 
ATOM   10969 H  HG22 . ILE   B  2  131 ? 4.758   -51.390 1.878    1.00 78.48  ? 135  ILE   B HG22 1 
ATOM   10970 H  HG23 . ILE   B  2  131 ? 4.429   -51.503 0.328    1.00 78.48  ? 135  ILE   B HG23 1 
ATOM   10971 H  HD11 . ILE   B  2  131 ? 2.049   -48.282 -0.687   1.00 63.57  ? 135  ILE   B HD11 1 
ATOM   10972 H  HD12 . ILE   B  2  131 ? 2.338   -48.156 0.870    1.00 63.57  ? 135  ILE   B HD12 1 
ATOM   10973 H  HD13 . ILE   B  2  131 ? 3.495   -48.614 -0.118   1.00 63.57  ? 135  ILE   B HD13 1 
ATOM   10974 N  N    . LYS   B  2  132 ? -0.122  -52.911 1.970    1.00 81.73  ? 136  LYS   B N    1 
ATOM   10975 C  CA   . LYS   B  2  132 ? -1.508  -52.771 2.405    1.00 82.12  ? 136  LYS   B CA   1 
ATOM   10976 C  C    . LYS   B  2  132 ? -1.624  -52.692 3.922    1.00 79.61  ? 136  LYS   B C    1 
ATOM   10977 O  O    . LYS   B  2  132 ? -2.593  -52.125 4.439    1.00 77.95  ? 136  LYS   B O    1 
ATOM   10978 C  CB   . LYS   B  2  132 ? -2.344  -53.938 1.883    1.00 87.42  ? 136  LYS   B CB   1 
ATOM   10979 C  CG   . LYS   B  2  132 ? -2.675  -53.859 0.404    1.00 91.40  ? 136  LYS   B CG   1 
ATOM   10980 C  CD   . LYS   B  2  132 ? -3.192  -55.195 -0.109   1.00 99.19  ? 136  LYS   B CD   1 
ATOM   10981 C  CE   . LYS   B  2  132 ? -3.611  -55.114 -1.567   1.00 104.82 ? 136  LYS   B CE   1 
ATOM   10982 N  NZ   . LYS   B  2  132 ? -3.842  -56.461 -2.162   1.00 115.28 ? 136  LYS   B NZ   1 
ATOM   10983 H  H    . LYS   B  2  132 ? 0.044   -53.626 1.521    1.00 98.11  ? 136  LYS   B H    1 
ATOM   10984 H  HA   . LYS   B  2  132 ? -1.862  -51.948 2.032    1.00 98.59  ? 136  LYS   B HA   1 
ATOM   10985 H  HB2  . LYS   B  2  132 ? -1.853  -54.762 2.030    1.00 104.94 ? 136  LYS   B HB2  1 
ATOM   10986 H  HB3  . LYS   B  2  132 ? -3.183  -53.961 2.370    1.00 104.94 ? 136  LYS   B HB3  1 
ATOM   10987 H  HG2  . LYS   B  2  132 ? -3.362  -53.189 0.262    1.00 109.72 ? 136  LYS   B HG2  1 
ATOM   10988 H  HG3  . LYS   B  2  132 ? -1.876  -53.627 -0.094   1.00 109.72 ? 136  LYS   B HG3  1 
ATOM   10989 H  HD2  . LYS   B  2  132 ? -2.491  -55.861 -0.030   1.00 119.07 ? 136  LYS   B HD2  1 
ATOM   10990 H  HD3  . LYS   B  2  132 ? -3.964  -55.462 0.415    1.00 119.07 ? 136  LYS   B HD3  1 
ATOM   10991 H  HE2  . LYS   B  2  132 ? -4.437  -54.609 -1.634   1.00 125.82 ? 136  LYS   B HE2  1 
ATOM   10992 H  HE3  . LYS   B  2  132 ? -2.912  -54.675 -2.076   1.00 125.82 ? 136  LYS   B HE3  1 
ATOM   10993 H  HZ1  . LYS   B  2  132 ? -4.083  -56.380 -3.015   1.00 138.37 ? 136  LYS   B HZ1  1 
ATOM   10994 H  HZ2  . LYS   B  2  132 ? -3.097  -56.945 -2.117   1.00 138.37 ? 136  LYS   B HZ2  1 
ATOM   10995 H  HZ3  . LYS   B  2  132 ? -4.488  -56.883 -1.719   1.00 138.37 ? 136  LYS   B HZ3  1 
ATOM   10996 N  N    . GLU   B  2  133 ? -0.659  -53.256 4.649    1.00 81.19  ? 137  GLU   B N    1 
ATOM   10997 C  CA   . GLU   B  2  133 ? -0.679  -53.261 6.108    1.00 85.52  ? 137  GLU   B CA   1 
ATOM   10998 C  C    . GLU   B  2  133 ? 0.578   -52.631 6.695    1.00 83.12  ? 137  GLU   B C    1 
ATOM   10999 O  O    . GLU   B  2  133 ? 0.941   -52.922 7.839    1.00 82.50  ? 137  GLU   B O    1 
ATOM   11000 C  CB   . GLU   B  2  133 ? -0.859  -54.689 6.627    1.00 93.46  ? 137  GLU   B CB   1 
ATOM   11001 C  CG   . GLU   B  2  133 ? -2.205  -55.299 6.262    1.00 102.35 ? 137  GLU   B CG   1 
ATOM   11002 C  CD   . GLU   B  2  133 ? -2.312  -56.764 6.638    1.00 117.29 ? 137  GLU   B CD   1 
ATOM   11003 O  OE1  . GLU   B  2  133 ? -1.311  -57.331 7.126    1.00 121.00 ? 137  GLU   B OE1  1 
ATOM   11004 O  OE2  . GLU   B  2  133 ? -3.398  -57.350 6.443    1.00 123.20 ? 137  GLU   B OE2  1 
ATOM   11005 H  H    . GLU   B  2  133 ? 0.029   -53.648 4.313    1.00 97.47  ? 137  GLU   B H    1 
ATOM   11006 H  HA   . GLU   B  2  133 ? -1.435  -52.736 6.413    1.00 102.66 ? 137  GLU   B HA   1 
ATOM   11007 H  HB2  . GLU   B  2  133 ? -0.165  -55.251 6.247    1.00 112.19 ? 137  GLU   B HB2  1 
ATOM   11008 H  HB3  . GLU   B  2  133 ? -0.788  -54.683 7.594    1.00 112.19 ? 137  GLU   B HB3  1 
ATOM   11009 H  HG2  . GLU   B  2  133 ? -2.906  -54.819 6.729    1.00 122.86 ? 137  GLU   B HG2  1 
ATOM   11010 H  HG3  . GLU   B  2  133 ? -2.335  -55.226 5.303    1.00 122.86 ? 137  GLU   B HG3  1 
ATOM   11011 N  N    . LEU   B  2  134 ? 1.249   -51.766 5.931    1.00 77.65  ? 138  LEU   B N    1 
ATOM   11012 C  CA   . LEU   B  2  134 ? 2.439   -51.095 6.443    1.00 69.97  ? 138  LEU   B CA   1 
ATOM   11013 C  C    . LEU   B  2  134 ? 2.092   -50.164 7.598    1.00 64.63  ? 138  LEU   B C    1 
ATOM   11014 O  O    . LEU   B  2  134 ? 2.851   -50.062 8.569    1.00 61.74  ? 138  LEU   B O    1 
ATOM   11015 C  CB   . LEU   B  2  134 ? 3.124   -50.316 5.319    1.00 65.87  ? 138  LEU   B CB   1 
ATOM   11016 C  CG   . LEU   B  2  134 ? 4.380   -49.533 5.708    1.00 61.06  ? 138  LEU   B CG   1 
ATOM   11017 C  CD1  . LEU   B  2  134 ? 5.501   -50.477 6.116    1.00 61.75  ? 138  LEU   B CD1  1 
ATOM   11018 C  CD2  . LEU   B  2  134 ? 4.820   -48.630 4.567    1.00 57.23  ? 138  LEU   B CD2  1 
ATOM   11019 H  H    . LEU   B  2  134 ? 1.038   -51.554 5.124    1.00 93.22  ? 138  LEU   B H    1 
ATOM   11020 H  HA   . LEU   B  2  134 ? 3.060   -51.764 6.770    1.00 84.00  ? 138  LEU   B HA   1 
ATOM   11021 H  HB2  . LEU   B  2  134 ? 3.382   -50.947 4.629    1.00 79.08  ? 138  LEU   B HB2  1 
ATOM   11022 H  HB3  . LEU   B  2  134 ? 2.486   -49.677 4.963    1.00 79.08  ? 138  LEU   B HB3  1 
ATOM   11023 H  HG   . LEU   B  2  134 ? 4.175   -48.971 6.472    1.00 73.31  ? 138  LEU   B HG   1 
ATOM   11024 H  HD11 . LEU   B  2  134 ? 6.274   -49.953 6.378    1.00 74.14  ? 138  LEU   B HD11 1 
ATOM   11025 H  HD12 . LEU   B  2  134 ? 5.201   -51.020 6.861    1.00 74.14  ? 138  LEU   B HD12 1 
ATOM   11026 H  HD13 . LEU   B  2  134 ? 5.726   -51.044 5.362    1.00 74.14  ? 138  LEU   B HD13 1 
ATOM   11027 H  HD21 . LEU   B  2  134 ? 5.599   -48.124 4.847    1.00 68.71  ? 138  LEU   B HD21 1 
ATOM   11028 H  HD22 . LEU   B  2  134 ? 5.042   -49.178 3.798    1.00 68.71  ? 138  LEU   B HD22 1 
ATOM   11029 H  HD23 . LEU   B  2  134 ? 4.095   -48.025 4.344    1.00 68.71  ? 138  LEU   B HD23 1 
ATOM   11030 N  N    . GLY   B  2  135 ? 0.954   -49.474 7.507    1.00 64.68  ? 139  GLY   B N    1 
ATOM   11031 C  CA   . GLY   B  2  135 ? 0.574   -48.547 8.561    1.00 62.02  ? 139  GLY   B CA   1 
ATOM   11032 C  C    . GLY   B  2  135 ? 0.600   -49.182 9.936    1.00 62.20  ? 139  GLY   B C    1 
ATOM   11033 O  O    . GLY   B  2  135 ? 1.174   -48.632 10.879   1.00 63.24  ? 139  GLY   B O    1 
ATOM   11034 H  H    . GLY   B  2  135 ? 0.395   -49.526 6.854    1.00 77.65  ? 139  GLY   B H    1 
ATOM   11035 H  HA2  . GLY   B  2  135 ? 1.186   -47.795 8.562    1.00 74.46  ? 139  GLY   B HA2  1 
ATOM   11036 H  HA3  . GLY   B  2  135 ? -0.325  -48.223 8.393    1.00 74.46  ? 139  GLY   B HA3  1 
ATOM   11037 N  N    . SER   B  2  136 ? -0.016  -50.357 10.069   1.00 62.87  ? 140  SER   B N    1 
ATOM   11038 C  CA   . SER   B  2  136 ? -0.046  -51.027 11.366   1.00 70.68  ? 140  SER   B CA   1 
ATOM   11039 C  C    . SER   B  2  136 ? 1.311   -51.637 11.698   1.00 77.46  ? 140  SER   B C    1 
ATOM   11040 O  O    . SER   B  2  136 ? 1.822   -51.466 12.811   1.00 81.60  ? 140  SER   B O    1 
ATOM   11041 C  CB   . SER   B  2  136 ? -1.141  -52.095 11.382   1.00 71.66  ? 140  SER   B CB   1 
ATOM   11042 O  OG   . SER   B  2  136 ? -0.940  -53.056 10.362   1.00 72.14  ? 140  SER   B OG   1 
ATOM   11043 H  H    . SER   B  2  136 ? -0.417  -50.779 9.436    1.00 75.48  ? 140  SER   B H    1 
ATOM   11044 H  HA   . SER   B  2  136 ? -0.257  -50.372 12.050   1.00 84.86  ? 140  SER   B HA   1 
ATOM   11045 H  HB2  . SER   B  2  136 ? -1.128  -52.543 12.242   1.00 86.02  ? 140  SER   B HB2  1 
ATOM   11046 H  HB3  . SER   B  2  136 ? -1.999  -51.665 11.244   1.00 86.02  ? 140  SER   B HB3  1 
ATOM   11047 H  HG   . SER   B  2  136 ? -1.476  -53.695 10.460   1.00 86.60  ? 140  SER   B HG   1 
ATOM   11048 N  N    . ARG   B  2  137 ? 1.911   -52.356 10.745   1.00 79.73  ? 141  ARG   B N    1 
ATOM   11049 C  CA   . ARG   B  2  137 ? 3.230   -52.940 10.975   1.00 81.50  ? 141  ARG   B CA   1 
ATOM   11050 C  C    . ARG   B  2  137 ? 4.222   -51.879 11.438   1.00 78.52  ? 141  ARG   B C    1 
ATOM   11051 O  O    . ARG   B  2  137 ? 4.935   -52.066 12.430   1.00 77.09  ? 141  ARG   B O    1 
ATOM   11052 C  CB   . ARG   B  2  137 ? 3.735   -53.625 9.701    1.00 83.60  ? 141  ARG   B CB   1 
ATOM   11053 C  CG   . ARG   B  2  137 ? 3.074   -54.964 9.405    1.00 89.71  ? 141  ARG   B CG   1 
ATOM   11054 C  CD   . ARG   B  2  137 ? 3.428   -55.503 8.016    1.00 96.47  ? 141  ARG   B CD   1 
ATOM   11055 N  NE   . ARG   B  2  137 ? 4.833   -55.894 7.887    1.00 106.28 ? 141  ARG   B NE   1 
ATOM   11056 C  CZ   . ARG   B  2  137 ? 5.644   -55.526 6.893    1.00 117.08 ? 141  ARG   B CZ   1 
ATOM   11057 N  NH1  . ARG   B  2  137 ? 5.210   -54.752 5.905    1.00 116.54 ? 141  ARG   B NH1  1 
ATOM   11058 N  NH2  . ARG   B  2  137 ? 6.901   -55.948 6.881    1.00 123.84 ? 141  ARG   B NH2  1 
ATOM   11059 H  H    . ARG   B  2  137 ? 1.579   -52.516 9.968    1.00 95.71  ? 141  ARG   B H    1 
ATOM   11060 H  HA   . ARG   B  2  137 ? 3.154   -53.614 11.668   1.00 97.84  ? 141  ARG   B HA   1 
ATOM   11061 H  HB2  . ARG   B  2  137 ? 3.565   -53.040 8.947    1.00 100.36 ? 141  ARG   B HB2  1 
ATOM   11062 H  HB3  . ARG   B  2  137 ? 4.688   -53.781 9.791    1.00 100.36 ? 141  ARG   B HB3  1 
ATOM   11063 H  HG2  . ARG   B  2  137 ? 3.367   -55.615 10.062   1.00 107.69 ? 141  ARG   B HG2  1 
ATOM   11064 H  HG3  . ARG   B  2  137 ? 2.111   -54.859 9.449    1.00 107.69 ? 141  ARG   B HG3  1 
ATOM   11065 H  HD2  . ARG   B  2  137 ? 2.883   -56.285 7.834    1.00 115.81 ? 141  ARG   B HD2  1 
ATOM   11066 H  HD3  . ARG   B  2  137 ? 3.249   -54.814 7.357    1.00 115.81 ? 141  ARG   B HD3  1 
ATOM   11067 H  HE   . ARG   B  2  137 ? 5.162   -56.400 8.500    1.00 127.57 ? 141  ARG   B HE   1 
ATOM   11068 H  HH11 . ARG   B  2  137 ? 4.395   -54.479 5.899    1.00 139.88 ? 141  ARG   B HH11 1 
ATOM   11069 H  HH12 . ARG   B  2  137 ? 5.745   -54.523 5.272    1.00 139.88 ? 141  ARG   B HH12 1 
ATOM   11070 H  HH21 . ARG   B  2  137 ? 7.190   -56.456 7.512    1.00 148.65 ? 141  ARG   B HH21 1 
ATOM   11071 H  HH22 . ARG   B  2  137 ? 7.427   -55.714 6.243    1.00 148.65 ? 141  ARG   B HH22 1 
ATOM   11072 N  N    . LEU   B  2  138 ? 4.272   -50.750 10.730   1.00 76.04  ? 142  LEU   B N    1 
ATOM   11073 C  CA   . LEU   B  2  138 ? 5.237   -49.708 11.067   1.00 72.02  ? 142  LEU   B CA   1 
ATOM   11074 C  C    . LEU   B  2  138 ? 4.938   -49.099 12.431   1.00 71.54  ? 142  LEU   B C    1 
ATOM   11075 O  O    . LEU   B  2  138 ? 5.837   -48.954 13.267   1.00 71.70  ? 142  LEU   B O    1 
ATOM   11076 C  CB   . LEU   B  2  138 ? 5.238   -48.628 9.985    1.00 66.89  ? 142  LEU   B CB   1 
ATOM   11077 C  CG   . LEU   B  2  138 ? 6.188   -47.452 10.218   1.00 66.28  ? 142  LEU   B CG   1 
ATOM   11078 C  CD1  . LEU   B  2  138 ? 7.626   -47.930 10.356   1.00 65.81  ? 142  LEU   B CD1  1 
ATOM   11079 C  CD2  . LEU   B  2  138 ? 6.063   -46.449 9.086    1.00 64.11  ? 142  LEU   B CD2  1 
ATOM   11080 H  H    . LEU   B  2  138 ? 3.766   -50.566 10.060   1.00 91.29  ? 142  LEU   B H    1 
ATOM   11081 H  HA   . LEU   B  2  138 ? 6.122   -50.103 11.102   1.00 86.46  ? 142  LEU   B HA   1 
ATOM   11082 H  HB2  . LEU   B  2  138 ? 5.493   -49.042 9.145    1.00 80.31  ? 142  LEU   B HB2  1 
ATOM   11083 H  HB3  . LEU   B  2  138 ? 4.342   -48.265 9.918    1.00 80.31  ? 142  LEU   B HB3  1 
ATOM   11084 H  HG   . LEU   B  2  138 ? 5.947   -47.012 11.048   1.00 79.57  ? 142  LEU   B HG   1 
ATOM   11085 H  HD11 . LEU   B  2  138 ? 8.204   -47.160 10.480   1.00 79.01  ? 142  LEU   B HD11 1 
ATOM   11086 H  HD12 . LEU   B  2  138 ? 7.691   -48.520 11.123   1.00 79.01  ? 142  LEU   B HD12 1 
ATOM   11087 H  HD13 . LEU   B  2  138 ? 7.880   -48.406 9.550    1.00 79.01  ? 142  LEU   B HD13 1 
ATOM   11088 H  HD21 . LEU   B  2  138 ? 6.687   -45.723 9.237    1.00 76.96  ? 142  LEU   B HD21 1 
ATOM   11089 H  HD22 . LEU   B  2  138 ? 6.267   -46.892 8.247    1.00 76.96  ? 142  LEU   B HD22 1 
ATOM   11090 H  HD23 . LEU   B  2  138 ? 5.156   -46.107 9.066    1.00 76.96  ? 142  LEU   B HD23 1 
ATOM   11091 N  N    . SER   B  2  139 ? 3.678   -48.730 12.674   1.00 72.61  ? 143  SER   B N    1 
ATOM   11092 C  CA   . SER   B  2  139 ? 3.337   -48.083 13.936   1.00 77.91  ? 143  SER   B CA   1 
ATOM   11093 C  C    . SER   B  2  139 ? 3.510   -49.026 15.121   1.00 78.64  ? 143  SER   B C    1 
ATOM   11094 O  O    . SER   B  2  139 ? 3.781   -48.568 16.237   1.00 73.71  ? 143  SER   B O    1 
ATOM   11095 C  CB   . SER   B  2  139 ? 1.907   -47.545 13.884   1.00 83.28  ? 143  SER   B CB   1 
ATOM   11096 O  OG   . SER   B  2  139 ? 1.001   -48.528 13.419   1.00 92.59  ? 143  SER   B OG   1 
ATOM   11097 H  H    . SER   B  2  139 ? 3.017   -48.842 12.135   1.00 87.17  ? 143  SER   B H    1 
ATOM   11098 H  HA   . SER   B  2  139 ? 3.934   -47.330 14.069   1.00 93.53  ? 143  SER   B HA   1 
ATOM   11099 H  HB2  . SER   B  2  139 ? 1.642   -47.271 14.776   1.00 99.97  ? 143  SER   B HB2  1 
ATOM   11100 H  HB3  . SER   B  2  139 ? 1.880   -46.785 13.282   1.00 99.97  ? 143  SER   B HB3  1 
ATOM   11101 H  HG   . SER   B  2  139 ? 0.902   -48.459 12.588   1.00 111.14 ? 143  SER   B HG   1 
ATOM   11102 N  N    . LYS   B  2  140 ? 3.360   -50.336 14.909   1.00 80.58  ? 144  LYS   B N    1 
ATOM   11103 C  CA   . LYS   B  2  140 ? 3.614   -51.279 15.994   1.00 88.39  ? 144  LYS   B CA   1 
ATOM   11104 C  C    . LYS   B  2  140 ? 5.096   -51.317 16.345   1.00 92.10  ? 144  LYS   B C    1 
ATOM   11105 O  O    . LYS   B  2  140 ? 5.461   -51.307 17.526   1.00 94.66  ? 144  LYS   B O    1 
ATOM   11106 C  CB   . LYS   B  2  140 ? 3.117   -52.676 15.619   1.00 93.47  ? 144  LYS   B CB   1 
ATOM   11107 C  CG   . LYS   B  2  140 ? 3.393   -53.735 16.691   1.00 96.23  ? 144  LYS   B CG   1 
ATOM   11108 C  CD   . LYS   B  2  140 ? 2.303   -54.804 16.746   1.00 101.65 ? 144  LYS   B CD   1 
ATOM   11109 C  CE   . LYS   B  2  140 ? 2.795   -56.161 16.256   1.00 108.26 ? 144  LYS   B CE   1 
ATOM   11110 N  NZ   . LYS   B  2  140 ? 3.744   -56.813 17.203   1.00 115.71 ? 144  LYS   B NZ   1 
ATOM   11111 H  H    . LYS   B  2  140 ? 3.119   -50.694 14.165   1.00 96.73  ? 144  LYS   B H    1 
ATOM   11112 H  HA   . LYS   B  2  140 ? 3.120   -50.991 16.777   1.00 106.10 ? 144  LYS   B HA   1 
ATOM   11113 H  HB2  . LYS   B  2  140 ? 2.158   -52.639 15.478   1.00 112.21 ? 144  LYS   B HB2  1 
ATOM   11114 H  HB3  . LYS   B  2  140 ? 3.562   -52.957 14.804   1.00 112.21 ? 144  LYS   B HB3  1 
ATOM   11115 H  HG2  . LYS   B  2  140 ? 4.236   -54.174 16.496   1.00 115.51 ? 144  LYS   B HG2  1 
ATOM   11116 H  HG3  . LYS   B  2  140 ? 3.436   -53.305 17.560   1.00 115.51 ? 144  LYS   B HG3  1 
ATOM   11117 H  HD2  . LYS   B  2  140 ? 2.002   -54.906 17.662   1.00 122.02 ? 144  LYS   B HD2  1 
ATOM   11118 H  HD3  . LYS   B  2  140 ? 1.562   -54.532 16.182   1.00 122.02 ? 144  LYS   B HD3  1 
ATOM   11119 H  HE2  . LYS   B  2  140 ? 2.034   -56.751 16.143   1.00 129.95 ? 144  LYS   B HE2  1 
ATOM   11120 H  HE3  . LYS   B  2  140 ? 3.253   -56.043 15.408   1.00 129.95 ? 144  LYS   B HE3  1 
ATOM   11121 H  HZ1  . LYS   B  2  140 ? 3.999   -57.603 16.884   1.00 138.89 ? 144  LYS   B HZ1  1 
ATOM   11122 H  HZ2  . LYS   B  2  140 ? 4.464   -56.301 17.313   1.00 138.89 ? 144  LYS   B HZ2  1 
ATOM   11123 H  HZ3  . LYS   B  2  140 ? 3.352   -56.933 17.993   1.00 138.89 ? 144  LYS   B HZ3  1 
ATOM   11124 N  N    . GLU   B  2  141 ? 5.964   -51.356 15.332   1.00 90.77  ? 145  GLU   B N    1 
ATOM   11125 C  CA   . GLU   B  2  141 ? 7.399   -51.338 15.595   1.00 83.24  ? 145  GLU   B CA   1 
ATOM   11126 C  C    . GLU   B  2  141 ? 7.830   -50.007 16.197   1.00 77.13  ? 145  GLU   B C    1 
ATOM   11127 O  O    . GLU   B  2  141 ? 8.667   -49.974 17.107   1.00 77.28  ? 145  GLU   B O    1 
ATOM   11128 C  CB   . GLU   B  2  141 ? 8.170   -51.625 14.308   1.00 78.71  ? 145  GLU   B CB   1 
ATOM   11129 C  CG   . GLU   B  2  141 ? 8.119   -53.082 13.878   1.00 85.60  ? 145  GLU   B CG   1 
ATOM   11130 C  CD   . GLU   B  2  141 ? 8.713   -54.012 14.917   1.00 96.60  ? 145  GLU   B CD   1 
ATOM   11131 O  OE1  . GLU   B  2  141 ? 9.537   -53.544 15.732   1.00 100.62 ? 145  GLU   B OE1  1 
ATOM   11132 O  OE2  . GLU   B  2  141 ? 8.350   -55.207 14.927   1.00 102.18 ? 145  GLU   B OE2  1 
ATOM   11133 H  H    . GLU   B  2  141 ? 5.751   -51.393 14.500   1.00 108.97 ? 145  GLU   B H    1 
ATOM   11134 H  HA   . GLU   B  2  141 ? 7.610   -52.038 16.233   1.00 99.92  ? 145  GLU   B HA   1 
ATOM   11135 H  HB2  . GLU   B  2  141 ? 7.792   -51.091 13.592   1.00 94.49  ? 145  GLU   B HB2  1 
ATOM   11136 H  HB3  . GLU   B  2  141 ? 9.101   -51.388 14.442   1.00 94.49  ? 145  GLU   B HB3  1 
ATOM   11137 H  HG2  . GLU   B  2  141 ? 7.195   -53.339 13.736   1.00 102.76 ? 145  GLU   B HG2  1 
ATOM   11138 H  HG3  . GLU   B  2  141 ? 8.623   -53.188 13.056   1.00 102.76 ? 145  GLU   B HG3  1 
ATOM   11139 N  N    . MET   B  2  142 ? 7.269   -48.900 15.707   1.00 74.18  ? 146  MET   B N    1 
ATOM   11140 C  CA   . MET   B  2  142 ? 7.608   -47.594 16.258   1.00 73.96  ? 146  MET   B CA   1 
ATOM   11141 C  C    . MET   B  2  142 ? 7.045   -47.396 17.659   1.00 74.21  ? 146  MET   B C    1 
ATOM   11142 O  O    . MET   B  2  142 ? 7.504   -46.500 18.375   1.00 69.95  ? 146  MET   B O    1 
ATOM   11143 C  CB   . MET   B  2  142 ? 7.102   -46.489 15.330   1.00 73.53  ? 146  MET   B CB   1 
ATOM   11144 C  CG   . MET   B  2  142 ? 7.799   -46.450 13.976   1.00 70.52  ? 146  MET   B CG   1 
ATOM   11145 S  SD   . MET   B  2  142 ? 9.566   -46.104 14.097   1.00 67.46  ? 146  MET   B SD   1 
ATOM   11146 C  CE   . MET   B  2  142 ? 9.555   -44.500 14.899   1.00 67.30  ? 146  MET   B CE   1 
ATOM   11147 H  H    . MET   B  2  142 ? 6.698   -48.881 15.064   1.00 89.05  ? 146  MET   B H    1 
ATOM   11148 H  HA   . MET   B  2  142 ? 8.574   -47.520 16.303   1.00 88.79  ? 146  MET   B HA   1 
ATOM   11149 H  HB2  . MET   B  2  142 ? 6.155   -46.626 15.171   1.00 88.27  ? 146  MET   B HB2  1 
ATOM   11150 H  HB3  . MET   B  2  142 ? 7.246   -45.631 15.761   1.00 88.27  ? 146  MET   B HB3  1 
ATOM   11151 H  HG2  . MET   B  2  142 ? 7.693   -47.311 13.543   1.00 84.66  ? 146  MET   B HG2  1 
ATOM   11152 H  HG3  . MET   B  2  142 ? 7.395   -45.754 13.435   1.00 84.66  ? 146  MET   B HG3  1 
ATOM   11153 H  HE1  . MET   B  2  142 ? 10.469  -44.193 15.003   1.00 80.80  ? 146  MET   B HE1  1 
ATOM   11154 H  HE2  . MET   B  2  142 ? 9.056   -43.876 14.349   1.00 80.80  ? 146  MET   B HE2  1 
ATOM   11155 H  HE3  . MET   B  2  142 ? 9.133   -44.585 15.768   1.00 80.80  ? 146  MET   B HE3  1 
ATOM   11156 N  N    . SER   B  2  143 ? 6.066   -48.209 18.068   1.00 78.98  ? 147  SER   B N    1 
ATOM   11157 C  CA   . SER   B  2  143 ? 5.532   -48.108 19.420   1.00 85.58  ? 147  SER   B CA   1 
ATOM   11158 C  C    . SER   B  2  143 ? 6.534   -48.563 20.471   1.00 83.03  ? 147  SER   B C    1 
ATOM   11159 O  O    . SER   B  2  143 ? 6.439   -48.137 21.627   1.00 82.24  ? 147  SER   B O    1 
ATOM   11160 C  CB   . SER   B  2  143 ? 4.250   -48.932 19.546   1.00 96.41  ? 147  SER   B CB   1 
ATOM   11161 O  OG   . SER   B  2  143 ? 3.210   -48.382 18.758   1.00 103.71 ? 147  SER   B OG   1 
ATOM   11162 H  H    . SER   B  2  143 ? 5.701   -48.818 17.584   1.00 94.82  ? 147  SER   B H    1 
ATOM   11163 H  HA   . SER   B  2  143 ? 5.311   -47.179 19.595   1.00 102.73 ? 147  SER   B HA   1 
ATOM   11164 H  HB2  . SER   B  2  143 ? 4.428   -49.837 19.245   1.00 115.73 ? 147  SER   B HB2  1 
ATOM   11165 H  HB3  . SER   B  2  143 ? 3.971   -48.940 20.475   1.00 115.73 ? 147  SER   B HB3  1 
ATOM   11166 H  HG   . SER   B  2  143 ? 3.478   -48.265 17.970   1.00 124.49 ? 147  SER   B HG   1 
ATOM   11167 N  N    . LYS   B  2  144 ? 7.485   -49.420 20.100   1.00 82.73  ? 148  LYS   B N    1 
ATOM   11168 C  CA   . LYS   B  2  144 ? 8.520   -49.865 21.022   1.00 84.06  ? 148  LYS   B CA   1 
ATOM   11169 C  C    . LYS   B  2  144 ? 9.598   -48.813 21.245   1.00 84.26  ? 148  LYS   B C    1 
ATOM   11170 O  O    . LYS   B  2  144 ? 10.374  -48.937 22.199   1.00 88.02  ? 148  LYS   B O    1 
ATOM   11171 C  CB   . LYS   B  2  144 ? 9.168   -51.152 20.497   1.00 83.02  ? 148  LYS   B CB   1 
ATOM   11172 C  CG   . LYS   B  2  144 ? 8.182   -52.250 20.104   1.00 83.23  ? 148  LYS   B CG   1 
ATOM   11173 C  CD   . LYS   B  2  144 ? 8.896   -53.425 19.441   1.00 84.20  ? 148  LYS   B CD   1 
ATOM   11174 C  CE   . LYS   B  2  144 ? 7.920   -54.502 18.982   1.00 86.88  ? 148  LYS   B CE   1 
ATOM   11175 N  NZ   . LYS   B  2  144 ? 8.598   -55.581 18.206   1.00 88.63  ? 148  LYS   B NZ   1 
ATOM   11176 H  H    . LYS   B  2  144 ? 7.550   -49.760 19.312   1.00 99.31  ? 148  LYS   B H    1 
ATOM   11177 H  HA   . LYS   B  2  144 ? 8.111   -50.063 21.879   1.00 100.91 ? 148  LYS   B HA   1 
ATOM   11178 H  HB2  . LYS   B  2  144 ? 9.692   -50.934 19.711   1.00 99.66  ? 148  LYS   B HB2  1 
ATOM   11179 H  HB3  . LYS   B  2  144 ? 9.744   -51.511 21.190   1.00 99.66  ? 148  LYS   B HB3  1 
ATOM   11180 H  HG2  . LYS   B  2  144 ? 7.729   -52.575 20.897   1.00 99.92  ? 148  LYS   B HG2  1 
ATOM   11181 H  HG3  . LYS   B  2  144 ? 7.535   -51.891 19.476   1.00 99.92  ? 148  LYS   B HG3  1 
ATOM   11182 H  HD2  . LYS   B  2  144 ? 9.381   -53.106 18.664   1.00 101.07 ? 148  LYS   B HD2  1 
ATOM   11183 H  HD3  . LYS   B  2  144 ? 9.510   -53.824 20.076   1.00 101.07 ? 148  LYS   B HD3  1 
ATOM   11184 H  HE2  . LYS   B  2  144 ? 7.502   -54.905 19.759   1.00 104.29 ? 148  LYS   B HE2  1 
ATOM   11185 H  HE3  . LYS   B  2  144 ? 7.245   -54.099 18.414   1.00 104.29 ? 148  LYS   B HE3  1 
ATOM   11186 H  HZ1  . LYS   B  2  144 ? 8.222   -56.367 18.386   1.00 106.40 ? 148  LYS   B HZ1  1 
ATOM   11187 H  HZ2  . LYS   B  2  144 ? 8.525   -55.420 17.334   1.00 106.40 ? 148  LYS   B HZ2  1 
ATOM   11188 H  HZ3  . LYS   B  2  144 ? 9.460   -55.616 18.423   1.00 106.40 ? 148  LYS   B HZ3  1 
ATOM   11189 N  N    . LEU   B  2  145 ? 9.653   -47.781 20.401   1.00 81.33  ? 149  LEU   B N    1 
ATOM   11190 C  CA   . LEU   B  2  145 ? 10.715  -46.784 20.428   1.00 73.76  ? 149  LEU   B CA   1 
ATOM   11191 C  C    . LEU   B  2  145 ? 10.242  -45.406 20.857   1.00 71.23  ? 149  LEU   B C    1 
ATOM   11192 O  O    . LEU   B  2  145 ? 11.018  -44.659 21.456   1.00 70.62  ? 149  LEU   B O    1 
ATOM   11193 C  CB   . LEU   B  2  145 ? 11.359  -46.669 19.041   1.00 70.23  ? 149  LEU   B CB   1 
ATOM   11194 C  CG   . LEU   B  2  145 ? 11.758  -47.992 18.384   1.00 71.47  ? 149  LEU   B CG   1 
ATOM   11195 C  CD1  . LEU   B  2  145 ? 12.066  -47.786 16.911   1.00 72.60  ? 149  LEU   B CD1  1 
ATOM   11196 C  CD2  . LEU   B  2  145 ? 12.950  -48.604 19.097   1.00 72.80  ? 149  LEU   B CD2  1 
ATOM   11197 H  H    . LEU   B  2  145 ? 9.069   -47.636 19.787   1.00 97.63  ? 149  LEU   B H    1 
ATOM   11198 H  HA   . LEU   B  2  145 ? 11.397  -47.071 21.055   1.00 88.55  ? 149  LEU   B HA   1 
ATOM   11199 H  HB2  . LEU   B  2  145 ? 10.728  -46.231 18.448   1.00 84.32  ? 149  LEU   B HB2  1 
ATOM   11200 H  HB3  . LEU   B  2  145 ? 12.164  -46.133 19.123   1.00 84.32  ? 149  LEU   B HB3  1 
ATOM   11201 H  HG   . LEU   B  2  145 ? 11.016  -48.612 18.451   1.00 85.80  ? 149  LEU   B HG   1 
ATOM   11202 H  HD11 . LEU   B  2  145 ? 12.299  -48.640 16.515   1.00 87.15  ? 149  LEU   B HD11 1 
ATOM   11203 H  HD12 . LEU   B  2  145 ? 11.282  -47.420 16.473   1.00 87.15  ? 149  LEU   B HD12 1 
ATOM   11204 H  HD13 . LEU   B  2  145 ? 12.810  -47.169 16.827   1.00 87.15  ? 149  LEU   B HD13 1 
ATOM   11205 H  HD21 . LEU   B  2  145 ? 13.182  -49.440 18.664   1.00 87.39  ? 149  LEU   B HD21 1 
ATOM   11206 H  HD22 . LEU   B  2  145 ? 13.697  -47.988 19.050   1.00 87.39  ? 149  LEU   B HD22 1 
ATOM   11207 H  HD23 . LEU   B  2  145 ? 12.713  -48.767 20.024   1.00 87.39  ? 149  LEU   B HD23 1 
ATOM   11208 N  N    . THR   B  2  146 ? 8.997   -45.051 20.550   1.00 69.78  ? 150  THR   B N    1 
ATOM   11209 C  CA   . THR   B  2  146 ? 8.411   -43.786 20.962   1.00 71.70  ? 150  THR   B CA   1 
ATOM   11210 C  C    . THR   B  2  146 ? 6.944   -44.019 21.280   1.00 74.93  ? 150  THR   B C    1 
ATOM   11211 O  O    . THR   B  2  146 ? 6.285   -44.854 20.654   1.00 74.68  ? 150  THR   B O    1 
ATOM   11212 C  CB   . THR   B  2  146 ? 8.531   -42.707 19.877   1.00 69.80  ? 150  THR   B CB   1 
ATOM   11213 O  OG1  . THR   B  2  146 ? 7.994   -41.472 20.367   1.00 71.26  ? 150  THR   B OG1  1 
ATOM   11214 C  CG2  . THR   B  2  146 ? 7.769   -43.124 18.622   1.00 67.89  ? 150  THR   B CG2  1 
ATOM   11215 H  H    . THR   B  2  146 ? 8.460   -45.541 20.092   1.00 83.78  ? 150  THR   B H    1 
ATOM   11216 H  HA   . THR   B  2  146 ? 8.867   -43.462 21.754   1.00 86.08  ? 150  THR   B HA   1 
ATOM   11217 H  HB   . THR   B  2  146 ? 9.465   -42.585 19.643   1.00 83.79  ? 150  THR   B HB   1 
ATOM   11218 H  HG1  . THR   B  2  146 ? 8.481   -40.831 20.126   1.00 85.55  ? 150  THR   B HG1  1 
ATOM   11219 H  HG21 . THR   B  2  146 ? 7.883   -42.456 17.928   1.00 81.51  ? 150  THR   B HG21 1 
ATOM   11220 H  HG22 . THR   B  2  146 ? 8.104   -43.975 18.298   1.00 81.51  ? 150  THR   B HG22 1 
ATOM   11221 H  HG23 . THR   B  2  146 ? 6.824   -43.213 18.821   1.00 81.51  ? 150  THR   B HG23 1 
ATOM   11222 N  N    . SER   B  2  147 ? 6.434   -43.274 22.254   1.00 77.21  ? 151  SER   B N    1 
ATOM   11223 C  CA   . SER   B  2  147 ? 5.022   -43.354 22.593   1.00 83.11  ? 151  SER   B CA   1 
ATOM   11224 C  C    . SER   B  2  147 ? 4.156   -42.442 21.733   1.00 81.07  ? 151  SER   B C    1 
ATOM   11225 O  O    . SER   B  2  147 ? 2.926   -42.531 21.812   1.00 88.03  ? 151  SER   B O    1 
ATOM   11226 C  CB   . SER   B  2  147 ? 4.812   -43.014 24.073   1.00 88.99  ? 151  SER   B CB   1 
ATOM   11227 O  OG   . SER   B  2  147 ? 5.371   -41.753 24.396   1.00 95.55  ? 151  SER   B OG   1 
ATOM   11228 H  H    . SER   B  2  147 ? 6.885   -42.718 22.730   1.00 92.69  ? 151  SER   B H    1 
ATOM   11229 H  HA   . SER   B  2  147 ? 4.719   -44.265 22.456   1.00 99.76  ? 151  SER   B HA   1 
ATOM   11230 H  HB2  . SER   B  2  147 ? 3.861   -42.992 24.258   1.00 106.83 ? 151  SER   B HB2  1 
ATOM   11231 H  HB3  . SER   B  2  147 ? 5.240   -43.695 24.615   1.00 106.83 ? 151  SER   B HB3  1 
ATOM   11232 H  HG   . SER   B  2  147 ? 6.014   -41.852 24.928   1.00 114.70 ? 151  SER   B HG   1 
ATOM   11233 N  N    . ASN   B  2  148 ? 4.761   -41.580 20.907   1.00 70.85  ? 152  ASN   B N    1 
ATOM   11234 C  CA   . ASN   B  2  148 ? 4.031   -40.617 20.079   1.00 64.77  ? 152  ASN   B CA   1 
ATOM   11235 C  C    . ASN   B  2  148 ? 4.502   -40.744 18.632   1.00 61.97  ? 152  ASN   B C    1 
ATOM   11236 O  O    . ASN   B  2  148 ? 5.327   -39.958 18.162   1.00 64.40  ? 152  ASN   B O    1 
ATOM   11237 C  CB   . ASN   B  2  148 ? 4.225   -39.201 20.602   1.00 64.17  ? 152  ASN   B CB   1 
ATOM   11238 C  CG   . ASN   B  2  148 ? 3.475   -38.947 21.888   1.00 71.21  ? 152  ASN   B CG   1 
ATOM   11239 O  OD1  . ASN   B  2  148 ? 3.924   -39.323 22.971   1.00 73.94  ? 152  ASN   B OD1  1 
ATOM   11240 N  ND2  . ASN   B  2  148 ? 2.326   -38.295 21.778   1.00 74.92  ? 152  ASN   B ND2  1 
ATOM   11241 H  H    . ASN   B  2  148 ? 5.615   -41.534 20.809   1.00 85.05  ? 152  ASN   B H    1 
ATOM   11242 H  HA   . ASN   B  2  148 ? 3.088   -40.846 20.106   1.00 77.76  ? 152  ASN   B HA   1 
ATOM   11243 H  HB2  . ASN   B  2  148 ? 5.169   -39.053 20.771   1.00 77.04  ? 152  ASN   B HB2  1 
ATOM   11244 H  HB3  . ASN   B  2  148 ? 3.904   -38.571 19.938   1.00 77.04  ? 152  ASN   B HB3  1 
ATOM   11245 H  HD21 . ASN   B  2  148 ? 1.859   -38.125 22.480   1.00 89.95  ? 152  ASN   B HD21 1 
ATOM   11246 H  HD22 . ASN   B  2  148 ? 2.047   -38.042 21.005   1.00 89.95  ? 152  ASN   B HD22 1 
ATOM   11247 N  N    . PHE   B  2  149 ? 3.964   -41.730 17.922   1.00 58.53  ? 153  PHE   B N    1 
ATOM   11248 C  CA   . PHE   B  2  149 ? 4.210   -41.895 16.497   1.00 56.21  ? 153  PHE   B CA   1 
ATOM   11249 C  C    . PHE   B  2  149 ? 2.952   -41.520 15.725   1.00 60.07  ? 153  PHE   B C    1 
ATOM   11250 O  O    . PHE   B  2  149 ? 1.852   -41.974 16.059   1.00 59.85  ? 153  PHE   B O    1 
ATOM   11251 C  CB   . PHE   B  2  149 ? 4.627   -43.329 16.165   1.00 55.58  ? 153  PHE   B CB   1 
ATOM   11252 C  CG   . PHE   B  2  149 ? 4.893   -43.559 14.703   1.00 56.44  ? 153  PHE   B CG   1 
ATOM   11253 C  CD1  . PHE   B  2  149 ? 5.988   -42.978 14.084   1.00 55.05  ? 153  PHE   B CD1  1 
ATOM   11254 C  CD2  . PHE   B  2  149 ? 4.050   -44.359 13.949   1.00 57.62  ? 153  PHE   B CD2  1 
ATOM   11255 C  CE1  . PHE   B  2  149 ? 6.236   -43.188 12.740   1.00 53.81  ? 153  PHE   B CE1  1 
ATOM   11256 C  CE2  . PHE   B  2  149 ? 4.293   -44.573 12.605   1.00 56.78  ? 153  PHE   B CE2  1 
ATOM   11257 C  CZ   . PHE   B  2  149 ? 5.388   -43.987 12.000   1.00 54.39  ? 153  PHE   B CZ   1 
ATOM   11258 H  H    . PHE   B  2  149 ? 3.442   -42.329 18.253   1.00 70.28  ? 153  PHE   B H    1 
ATOM   11259 H  HA   . PHE   B  2  149 ? 4.929   -41.304 16.224   1.00 67.49  ? 153  PHE   B HA   1 
ATOM   11260 H  HB2  . PHE   B  2  149 ? 5.440   -43.538 16.651   1.00 66.73  ? 153  PHE   B HB2  1 
ATOM   11261 H  HB3  . PHE   B  2  149 ? 3.916   -43.931 16.435   1.00 66.73  ? 153  PHE   B HB3  1 
ATOM   11262 H  HD1  . PHE   B  2  149 ? 6.564   -42.441 14.579   1.00 66.10  ? 153  PHE   B HD1  1 
ATOM   11263 H  HD2  . PHE   B  2  149 ? 3.312   -44.757 14.352   1.00 69.18  ? 153  PHE   B HD2  1 
ATOM   11264 H  HE1  . PHE   B  2  149 ? 6.974   -42.792 12.335   1.00 64.61  ? 153  PHE   B HE1  1 
ATOM   11265 H  HE2  . PHE   B  2  149 ? 3.720   -45.111 12.108   1.00 68.17  ? 153  PHE   B HE2  1 
ATOM   11266 H  HZ   . PHE   B  2  149 ? 5.553   -44.130 11.096   1.00 65.30  ? 153  PHE   B HZ   1 
ATOM   11267 N  N    . ARG   B  2  150 ? 3.121   -40.680 14.710   1.00 64.48  ? 154  ARG   B N    1 
ATOM   11268 C  CA   . ARG   B  2  150 ? 2.058   -40.323 13.784   1.00 65.08  ? 154  ARG   B CA   1 
ATOM   11269 C  C    . ARG   B  2  150 ? 2.584   -40.498 12.369   1.00 63.16  ? 154  ARG   B C    1 
ATOM   11270 O  O    . ARG   B  2  150 ? 3.789   -40.386 12.125   1.00 59.20  ? 154  ARG   B O    1 
ATOM   11271 C  CB   . ARG   B  2  150 ? 1.581   -38.879 13.980   1.00 66.20  ? 154  ARG   B CB   1 
ATOM   11272 C  CG   . ARG   B  2  150 ? 0.969   -38.582 15.337   1.00 67.64  ? 154  ARG   B CG   1 
ATOM   11273 C  CD   . ARG   B  2  150 ? 0.298   -37.220 15.319   1.00 70.44  ? 154  ARG   B CD   1 
ATOM   11274 N  NE   . ARG   B  2  150 ? 1.192   -36.191 14.793   1.00 76.78  ? 154  ARG   B NE   1 
ATOM   11275 C  CZ   . ARG   B  2  150 ? 0.789   -35.053 14.236   1.00 85.54  ? 154  ARG   B CZ   1 
ATOM   11276 N  NH1  . ARG   B  2  150 ? -0.504  -34.781 14.115   1.00 95.41  ? 154  ARG   B NH1  1 
ATOM   11277 N  NH2  . ARG   B  2  150 ? 1.686   -34.185 13.789   1.00 87.08  ? 154  ARG   B NH2  1 
ATOM   11278 H  H    . ARG   B  2  150 ? 3.867   -40.291 14.532   1.00 77.41  ? 154  ARG   B H    1 
ATOM   11279 H  HA   . ARG   B  2  150 ? 1.293   -40.903 13.922   1.00 78.14  ? 154  ARG   B HA   1 
ATOM   11280 H  HB2  . ARG   B  2  150 ? 2.342   -38.288 13.868   1.00 79.48  ? 154  ARG   B HB2  1 
ATOM   11281 H  HB3  . ARG   B  2  150 ? 0.908   -38.685 13.309   1.00 79.48  ? 154  ARG   B HB3  1 
ATOM   11282 H  HG2  . ARG   B  2  150 ? 0.302   -39.254 15.549   1.00 81.20  ? 154  ARG   B HG2  1 
ATOM   11283 H  HG3  . ARG   B  2  150 ? 1.663   -38.578 16.015   1.00 81.20  ? 154  ARG   B HG3  1 
ATOM   11284 H  HD2  . ARG   B  2  150 ? -0.490  -37.257 14.754   1.00 84.57  ? 154  ARG   B HD2  1 
ATOM   11285 H  HD3  . ARG   B  2  150 ? 0.046   -36.973 16.222   1.00 84.57  ? 154  ARG   B HD3  1 
ATOM   11286 H  HE   . ARG   B  2  150 ? 2.038   -36.332 14.848   1.00 92.18  ? 154  ARG   B HE   1 
ATOM   11287 H  HH11 . ARG   B  2  150 ? -1.089  -35.344 14.398   1.00 114.53 ? 154  ARG   B HH11 1 
ATOM   11288 H  HH12 . ARG   B  2  150 ? -0.756  -34.043 13.753   1.00 114.53 ? 154  ARG   B HH12 1 
ATOM   11289 H  HH21 . ARG   B  2  150 ? 2.526   -34.359 13.860   1.00 104.53 ? 154  ARG   B HH21 1 
ATOM   11290 H  HH22 . ARG   B  2  150 ? 1.429   -33.447 13.428   1.00 104.53 ? 154  ARG   B HH22 1 
ATOM   11291 N  N    . LEU   B  2  151 ? 1.679   -40.773 11.434   1.00 62.32  ? 155  LEU   B N    1 
ATOM   11292 C  CA   . LEU   B  2  151 ? 2.097   -40.943 10.051   1.00 61.94  ? 155  LEU   B CA   1 
ATOM   11293 C  C    . LEU   B  2  151 ? 0.997   -40.468 9.115    1.00 61.10  ? 155  LEU   B C    1 
ATOM   11294 O  O    . LEU   B  2  151 ? -0.194  -40.560 9.425    1.00 64.61  ? 155  LEU   B O    1 
ATOM   11295 C  CB   . LEU   B  2  151 ? 2.468   -42.402 9.749    1.00 62.05  ? 155  LEU   B CB   1 
ATOM   11296 C  CG   . LEU   B  2  151 ? 1.342   -43.391 9.445    1.00 65.71  ? 155  LEU   B CG   1 
ATOM   11297 C  CD1  . LEU   B  2  151 ? 1.928   -44.761 9.134    1.00 65.79  ? 155  LEU   B CD1  1 
ATOM   11298 C  CD2  . LEU   B  2  151 ? 0.353   -43.478 10.594   1.00 71.11  ? 155  LEU   B CD2  1 
ATOM   11299 H  H    . LEU   B  2  151 ? 0.836   -40.864 11.575   1.00 74.82  ? 155  LEU   B H    1 
ATOM   11300 H  HA   . LEU   B  2  151 ? 2.876   -40.389 9.888    1.00 74.36  ? 155  LEU   B HA   1 
ATOM   11301 H  HB2  . LEU   B  2  151 ? 3.052   -42.401 8.974    1.00 74.50  ? 155  LEU   B HB2  1 
ATOM   11302 H  HB3  . LEU   B  2  151 ? 2.942   -42.750 10.520   1.00 74.50  ? 155  LEU   B HB3  1 
ATOM   11303 H  HG   . LEU   B  2  151 ? 0.851   -43.077 8.670    1.00 78.89  ? 155  LEU   B HG   1 
ATOM   11304 H  HD11 . LEU   B  2  151 ? 1.206   -45.373 8.924    1.00 78.98  ? 155  LEU   B HD11 1 
ATOM   11305 H  HD12 . LEU   B  2  151 ? 2.527   -44.683 8.374    1.00 78.98  ? 155  LEU   B HD12 1 
ATOM   11306 H  HD13 . LEU   B  2  151 ? 2.417   -45.079 9.909    1.00 78.98  ? 155  LEU   B HD13 1 
ATOM   11307 H  HD21 . LEU   B  2  151 ? -0.333  -44.127 10.371   1.00 85.36  ? 155  LEU   B HD21 1 
ATOM   11308 H  HD22 . LEU   B  2  151 ? 0.823   -43.755 11.395   1.00 85.36  ? 155  LEU   B HD22 1 
ATOM   11309 H  HD23 . LEU   B  2  151 ? -0.049  -42.606 10.731   1.00 85.36  ? 155  LEU   B HD23 1 
ATOM   11310 N  N    . GLY   B  2  152 ? 1.425   -39.947 7.964    1.00 56.73  ? 156  GLY   B N    1 
ATOM   11311 C  CA   . GLY   B  2  152 ? 0.520   -39.504 6.924    1.00 55.16  ? 156  GLY   B CA   1 
ATOM   11312 C  C    . GLY   B  2  152 ? 1.003   -40.017 5.578    1.00 52.69  ? 156  GLY   B C    1 
ATOM   11313 O  O    . GLY   B  2  152 ? 2.037   -40.678 5.485    1.00 51.82  ? 156  GLY   B O    1 
ATOM   11314 H  H    . GLY   B  2  152 ? 2.255   -39.840 7.765    1.00 68.11  ? 156  GLY   B H    1 
ATOM   11315 H  HA2  . GLY   B  2  152 ? -0.372  -39.846 7.092    1.00 66.23  ? 156  GLY   B HA2  1 
ATOM   11316 H  HA3  . GLY   B  2  152 ? 0.489   -38.535 6.902    1.00 66.23  ? 156  GLY   B HA3  1 
ATOM   11317 N  N    . PHE   B  2  153 ? 0.235   -39.694 4.541    1.00 54.13  ? 157  PHE   B N    1 
ATOM   11318 C  CA   . PHE   B  2  153 ? 0.504   -40.250 3.224    1.00 51.55  ? 157  PHE   B CA   1 
ATOM   11319 C  C    . PHE   B  2  153 ? 0.241   -39.224 2.133    1.00 52.27  ? 157  PHE   B C    1 
ATOM   11320 O  O    . PHE   B  2  153 ? -0.713  -38.445 2.209    1.00 52.82  ? 157  PHE   B O    1 
ATOM   11321 C  CB   . PHE   B  2  153 ? -0.351  -41.498 2.975    1.00 50.86  ? 157  PHE   B CB   1 
ATOM   11322 C  CG   . PHE   B  2  153 ? -0.100  -42.148 1.648    1.00 50.75  ? 157  PHE   B CG   1 
ATOM   11323 C  CD1  . PHE   B  2  153 ? -0.717  -41.674 0.503    1.00 50.25  ? 157  PHE   B CD1  1 
ATOM   11324 C  CD2  . PHE   B  2  153 ? 0.745   -43.239 1.545    1.00 54.06  ? 157  PHE   B CD2  1 
ATOM   11325 C  CE1  . PHE   B  2  153 ? -0.491  -42.266 -0.719   1.00 51.76  ? 157  PHE   B CE1  1 
ATOM   11326 C  CE2  . PHE   B  2  153 ? 0.975   -43.839 0.323    1.00 53.83  ? 157  PHE   B CE2  1 
ATOM   11327 C  CZ   . PHE   B  2  153 ? 0.355   -43.352 -0.811   1.00 52.57  ? 157  PHE   B CZ   1 
ATOM   11328 H  H    . PHE   B  2  153 ? -0.439  -39.162 4.578    1.00 65.00  ? 157  PHE   B H    1 
ATOM   11329 H  HA   . PHE   B  2  153 ? 1.443   -40.485 3.170    1.00 61.90  ? 157  PHE   B HA   1 
ATOM   11330 H  HB2  . PHE   B  2  153 ? -0.158  -42.151 3.666    1.00 61.07  ? 157  PHE   B HB2  1 
ATOM   11331 H  HB3  . PHE   B  2  153 ? -1.287  -41.247 3.009    1.00 61.07  ? 157  PHE   B HB3  1 
ATOM   11332 H  HD1  . PHE   B  2  153 ? -1.292  -40.945 0.560    1.00 60.34  ? 157  PHE   B HD1  1 
ATOM   11333 H  HD2  . PHE   B  2  153 ? 1.163   -43.571 2.306    1.00 64.91  ? 157  PHE   B HD2  1 
ATOM   11334 H  HE1  . PHE   B  2  153 ? -0.907  -41.935 -1.482   1.00 62.14  ? 157  PHE   B HE1  1 
ATOM   11335 H  HE2  . PHE   B  2  153 ? 1.546   -44.570 0.263    1.00 64.64  ? 157  PHE   B HE2  1 
ATOM   11336 H  HZ   . PHE   B  2  153 ? 0.507   -43.755 -1.635   1.00 63.12  ? 157  PHE   B HZ   1 
ATOM   11337 N  N    . GLY   B  2  154 ? 1.099   -39.246 1.116    1.00 52.23  ? 158  GLY   B N    1 
ATOM   11338 C  CA   . GLY   B  2  154 ? 0.908   -38.444 -0.077   1.00 49.81  ? 158  GLY   B CA   1 
ATOM   11339 C  C    . GLY   B  2  154 ? 1.561   -39.140 -1.251   1.00 50.74  ? 158  GLY   B C    1 
ATOM   11340 O  O    . GLY   B  2  154 ? 2.444   -39.988 -1.083   1.00 49.46  ? 158  GLY   B O    1 
ATOM   11341 H  H    . GLY   B  2  154 ? 1.811   -39.728 1.097    1.00 62.72  ? 158  GLY   B H    1 
ATOM   11342 H  HA2  . GLY   B  2  154 ? -0.039  -38.334 -0.257   1.00 59.80  ? 158  GLY   B HA2  1 
ATOM   11343 H  HA3  . GLY   B  2  154 ? 1.311   -37.569 0.041    1.00 59.80  ? 158  GLY   B HA3  1 
ATOM   11344 N  N    . SER   B  2  155 ? 1.117   -38.773 -2.451   1.00 52.08  ? 159  SER   B N    1 
ATOM   11345 C  CA   . SER   B  2  155 ? 1.558   -39.440 -3.666   1.00 52.82  ? 159  SER   B CA   1 
ATOM   11346 C  C    . SER   B  2  155 ? 1.878   -38.410 -4.738   1.00 48.80  ? 159  SER   B C    1 
ATOM   11347 O  O    . SER   B  2  155 ? 1.321   -37.310 -4.751   1.00 46.56  ? 159  SER   B O    1 
ATOM   11348 C  CB   . SER   B  2  155 ? 0.492   -40.417 -4.174   1.00 51.79  ? 159  SER   B CB   1 
ATOM   11349 O  OG   . SER   B  2  155 ? -0.741  -39.757 -4.406   1.00 51.69  ? 159  SER   B OG   1 
ATOM   11350 H  H    . SER   B  2  155 ? 0.555   -38.135 -2.585   1.00 62.54  ? 159  SER   B H    1 
ATOM   11351 H  HA   . SER   B  2  155 ? 2.374   -39.934 -3.487   1.00 63.42  ? 159  SER   B HA   1 
ATOM   11352 H  HB2  . SER   B  2  155 ? 0.798   -40.812 -5.006   1.00 62.18  ? 159  SER   B HB2  1 
ATOM   11353 H  HB3  . SER   B  2  155 ? 0.357   -41.110 -3.509   1.00 62.18  ? 159  SER   B HB3  1 
ATOM   11354 H  HG   . SER   B  2  155 ? -0.716  -39.351 -5.141   1.00 62.07  ? 159  SER   B HG   1 
ATOM   11355 N  N    . PHE   B  2  156 ? 2.785   -38.781 -5.643   1.00 46.13  ? 160  PHE   B N    1 
ATOM   11356 C  CA   . PHE   B  2  156 ? 3.187   -37.910 -6.738   1.00 44.43  ? 160  PHE   B CA   1 
ATOM   11357 C  C    . PHE   B  2  156 ? 3.419   -38.738 -7.994   1.00 43.45  ? 160  PHE   B C    1 
ATOM   11358 O  O    . PHE   B  2  156 ? 3.663   -39.945 -7.933   1.00 41.89  ? 160  PHE   B O    1 
ATOM   11359 C  CB   . PHE   B  2  156 ? 4.462   -37.121 -6.402   1.00 42.61  ? 160  PHE   B CB   1 
ATOM   11360 C  CG   . PHE   B  2  156 ? 5.709   -37.965 -6.363   1.00 45.59  ? 160  PHE   B CG   1 
ATOM   11361 C  CD1  . PHE   B  2  156 ? 6.426   -38.227 -7.522   1.00 49.15  ? 160  PHE   B CD1  1 
ATOM   11362 C  CD2  . PHE   B  2  156 ? 6.170   -38.489 -5.167   1.00 46.32  ? 160  PHE   B CD2  1 
ATOM   11363 C  CE1  . PHE   B  2  156 ? 7.570   -39.000 -7.488   1.00 48.46  ? 160  PHE   B CE1  1 
ATOM   11364 C  CE2  . PHE   B  2  156 ? 7.316   -39.262 -5.127   1.00 46.89  ? 160  PHE   B CE2  1 
ATOM   11365 C  CZ   . PHE   B  2  156 ? 8.017   -39.517 -6.289   1.00 47.07  ? 160  PHE   B CZ   1 
ATOM   11366 H  H    . PHE   B  2  156 ? 3.185   -39.542 -5.640   1.00 55.39  ? 160  PHE   B H    1 
ATOM   11367 H  HA   . PHE   B  2  156 ? 2.468   -37.283 -6.913   1.00 53.35  ? 160  PHE   B HA   1 
ATOM   11368 H  HB2  . PHE   B  2  156 ? 4.590   -36.435 -7.076   1.00 51.17  ? 160  PHE   B HB2  1 
ATOM   11369 H  HB3  . PHE   B  2  156 ? 4.355   -36.712 -5.529   1.00 51.17  ? 160  PHE   B HB3  1 
ATOM   11370 H  HD1  . PHE   B  2  156 ? 6.132   -37.877 -8.332   1.00 59.02  ? 160  PHE   B HD1  1 
ATOM   11371 H  HD2  . PHE   B  2  156 ? 5.703   -38.319 -4.380   1.00 55.62  ? 160  PHE   B HD2  1 
ATOM   11372 H  HE1  . PHE   B  2  156 ? 8.039   -39.172 -8.273   1.00 58.19  ? 160  PHE   B HE1  1 
ATOM   11373 H  HE2  . PHE   B  2  156 ? 7.615   -39.610 -4.318   1.00 56.30  ? 160  PHE   B HE2  1 
ATOM   11374 H  HZ   . PHE   B  2  156 ? 8.788   -40.036 -6.264   1.00 56.52  ? 160  PHE   B HZ   1 
ATOM   11375 N  N    . VAL   B  2  157 ? 3.348   -38.062 -9.141   1.00 44.16  ? 161  VAL   B N    1 
ATOM   11376 C  CA   . VAL   B  2  157 ? 3.707   -38.668 -10.419  1.00 42.18  ? 161  VAL   B CA   1 
ATOM   11377 C  C    . VAL   B  2  157 ? 4.524   -37.676 -11.237  1.00 41.45  ? 161  VAL   B C    1 
ATOM   11378 O  O    . VAL   B  2  157 ? 5.745   -37.819 -11.366  1.00 40.83  ? 161  VAL   B O    1 
ATOM   11379 C  CB   . VAL   B  2  157 ? 2.464   -39.125 -11.203  1.00 44.45  ? 161  VAL   B CB   1 
ATOM   11380 C  CG1  . VAL   B  2  157 ? 2.875   -39.752 -12.535  1.00 43.29  ? 161  VAL   B CG1  1 
ATOM   11381 C  CG2  . VAL   B  2  157 ? 1.650   -40.104 -10.378  1.00 48.99  ? 161  VAL   B CG2  1 
ATOM   11382 H  H    . VAL   B  2  157 ? 3.093   -37.244 -9.205   1.00 53.03  ? 161  VAL   B H    1 
ATOM   11383 H  HA   . VAL   B  2  157 ? 4.255   -39.448 -10.242  1.00 50.65  ? 161  VAL   B HA   1 
ATOM   11384 H  HB   . VAL   B  2  157 ? 1.909   -38.352 -11.392  1.00 53.38  ? 161  VAL   B HB   1 
ATOM   11385 H  HG11 . VAL   B  2  157 ? 2.080   -40.062 -12.996  1.00 51.98  ? 161  VAL   B HG11 1 
ATOM   11386 H  HG12 . VAL   B  2  157 ? 3.329   -39.085 -13.072  1.00 51.98  ? 161  VAL   B HG12 1 
ATOM   11387 H  HG13 . VAL   B  2  157 ? 3.469   -40.499 -12.362  1.00 51.98  ? 161  VAL   B HG13 1 
ATOM   11388 H  HG21 . VAL   B  2  157 ? 0.884   -40.394 -10.898  1.00 58.83  ? 161  VAL   B HG21 1 
ATOM   11389 H  HG22 . VAL   B  2  157 ? 2.206   -40.867 -10.154  1.00 58.83  ? 161  VAL   B HG22 1 
ATOM   11390 H  HG23 . VAL   B  2  157 ? 1.352   -39.663 -9.568   1.00 58.83  ? 161  VAL   B HG23 1 
ATOM   11391 N  N    . GLU   B  2  158 ? 3.863   -36.664 -11.795  1.00 41.39  ? 162  GLU   B N    1 
ATOM   11392 C  CA   . GLU   B  2  158 ? 4.513   -35.797 -12.768  1.00 43.96  ? 162  GLU   B CA   1 
ATOM   11393 C  C    . GLU   B  2  158 ? 3.641   -34.576 -13.019  1.00 49.14  ? 162  GLU   B C    1 
ATOM   11394 O  O    . GLU   B  2  158 ? 2.422   -34.611 -12.824  1.00 51.26  ? 162  GLU   B O    1 
ATOM   11395 C  CB   . GLU   B  2  158 ? 4.767   -36.550 -14.078  1.00 48.25  ? 162  GLU   B CB   1 
ATOM   11396 C  CG   . GLU   B  2  158 ? 5.551   -35.776 -15.119  1.00 49.59  ? 162  GLU   B CG   1 
ATOM   11397 C  CD   . GLU   B  2  158 ? 6.952   -35.444 -14.654  1.00 44.59  ? 162  GLU   B CD   1 
ATOM   11398 O  OE1  . GLU   B  2  158 ? 7.130   -34.392 -14.003  1.00 43.00  ? 162  GLU   B OE1  1 
ATOM   11399 O  OE2  . GLU   B  2  158 ? 7.872   -36.245 -14.926  1.00 43.12  ? 162  GLU   B OE2  1 
ATOM   11400 H  H    . GLU   B  2  158 ? 3.044   -36.464 -11.627  1.00 49.71  ? 162  GLU   B H    1 
ATOM   11401 H  HA   . GLU   B  2  158 ? 5.356   -35.482 -12.406  1.00 52.79  ? 162  GLU   B HA   1 
ATOM   11402 H  HB2  . GLU   B  2  158 ? 5.268   -37.356 -13.877  1.00 57.94  ? 162  GLU   B HB2  1 
ATOM   11403 H  HB3  . GLU   B  2  158 ? 3.911   -36.781 -14.471  1.00 57.94  ? 162  GLU   B HB3  1 
ATOM   11404 H  HG2  . GLU   B  2  158 ? 5.619   -36.310 -15.926  1.00 59.55  ? 162  GLU   B HG2  1 
ATOM   11405 H  HG3  . GLU   B  2  158 ? 5.090   -34.944 -15.309  1.00 59.55  ? 162  GLU   B HG3  1 
ATOM   11406 N  N    . LYS   B  2  159 ? 4.283   -33.495 -13.455  1.00 48.67  ? 163  LYS   B N    1 
ATOM   11407 C  CA   . LYS   B  2  159 ? 3.551   -32.337 -13.953  1.00 48.05  ? 163  LYS   B CA   1 
ATOM   11408 C  C    . LYS   B  2  159 ? 2.655   -32.786 -15.103  1.00 46.42  ? 163  LYS   B C    1 
ATOM   11409 O  O    . LYS   B  2  159 ? 3.170   -33.268 -16.123  1.00 44.79  ? 163  LYS   B O    1 
ATOM   11410 C  CB   . LYS   B  2  159 ? 4.499   -31.243 -14.437  1.00 49.48  ? 163  LYS   B CB   1 
ATOM   11411 C  CG   . LYS   B  2  159 ? 5.254   -30.511 -13.341  1.00 52.88  ? 163  LYS   B CG   1 
ATOM   11412 C  CD   . LYS   B  2  159 ? 6.113   -29.400 -13.933  1.00 53.29  ? 163  LYS   B CD   1 
ATOM   11413 C  CE   . LYS   B  2  159 ? 6.914   -28.667 -12.869  1.00 52.42  ? 163  LYS   B CE   1 
ATOM   11414 N  NZ   . LYS   B  2  159 ? 6.044   -28.020 -11.850  1.00 56.74  ? 163  LYS   B NZ   1 
ATOM   11415 H  H    . LYS   B  2  159 ? 5.138   -33.408 -13.471  1.00 58.44  ? 163  LYS   B H    1 
ATOM   11416 H  HA   . LYS   B  2  159 ? 3.017   -31.961 -13.236  1.00 57.70  ? 163  LYS   B HA   1 
ATOM   11417 H  HB2  . LYS   B  2  159 ? 5.158   -31.645 -15.024  1.00 59.41  ? 163  LYS   B HB2  1 
ATOM   11418 H  HB3  . LYS   B  2  159 ? 3.981   -30.582 -14.923  1.00 59.41  ? 163  LYS   B HB3  1 
ATOM   11419 H  HG2  . LYS   B  2  159 ? 4.623   -30.115 -12.720  1.00 63.50  ? 163  LYS   B HG2  1 
ATOM   11420 H  HG3  . LYS   B  2  159 ? 5.833   -31.134 -12.874  1.00 63.50  ? 163  LYS   B HG3  1 
ATOM   11421 H  HD2  . LYS   B  2  159 ? 6.737   -29.784 -14.570  1.00 63.99  ? 163  LYS   B HD2  1 
ATOM   11422 H  HD3  . LYS   B  2  159 ? 5.540   -28.756 -14.378  1.00 63.99  ? 163  LYS   B HD3  1 
ATOM   11423 H  HE2  . LYS   B  2  159 ? 7.491   -29.300 -12.414  1.00 62.94  ? 163  LYS   B HE2  1 
ATOM   11424 H  HE3  . LYS   B  2  159 ? 7.447   -27.976 -13.292  1.00 62.94  ? 163  LYS   B HE3  1 
ATOM   11425 H  HZ1  . LYS   B  2  159 ? 6.314   -27.185 -11.705  1.00 68.12  ? 163  LYS   B HZ1  1 
ATOM   11426 H  HZ2  . LYS   B  2  159 ? 5.201   -28.006 -12.134  1.00 68.12  ? 163  LYS   B HZ2  1 
ATOM   11427 H  HZ3  . LYS   B  2  159 ? 6.083   -28.473 -11.085  1.00 68.12  ? 163  LYS   B HZ3  1 
ATOM   11428 N  N    . PRO   B  2  160 ? 1.333   -32.650 -14.995  1.00 44.49  ? 164  PRO   B N    1 
ATOM   11429 C  CA   . PRO   B  2  160 ? 0.441   -33.164 -16.049  1.00 47.60  ? 164  PRO   B CA   1 
ATOM   11430 C  C    . PRO   B  2  160 ? 0.359   -32.232 -17.254  1.00 51.04  ? 164  PRO   B C    1 
ATOM   11431 O  O    . PRO   B  2  160 ? -0.695  -31.677 -17.579  1.00 54.17  ? 164  PRO   B O    1 
ATOM   11432 C  CB   . PRO   B  2  160 ? -0.896  -33.287 -15.307  1.00 45.63  ? 164  PRO   B CB   1 
ATOM   11433 C  CG   . PRO   B  2  160 ? -0.866  -32.149 -14.346  1.00 41.43  ? 164  PRO   B CG   1 
ATOM   11434 C  CD   . PRO   B  2  160 ? 0.572   -32.023 -13.897  1.00 41.27  ? 164  PRO   B CD   1 
ATOM   11435 H  HA   . PRO   B  2  160 ? 0.735   -34.041 -16.341  1.00 57.15  ? 164  PRO   B HA   1 
ATOM   11436 H  HB2  . PRO   B  2  160 ? -1.635  -33.204 -15.929  1.00 54.79  ? 164  PRO   B HB2  1 
ATOM   11437 H  HB3  . PRO   B  2  160 ? -0.946  -34.138 -14.844  1.00 54.79  ? 164  PRO   B HB3  1 
ATOM   11438 H  HG2  . PRO   B  2  160 ? -1.160  -31.339 -14.791  1.00 49.75  ? 164  PRO   B HG2  1 
ATOM   11439 H  HG3  . PRO   B  2  160 ? -1.446  -32.343 -13.593  1.00 49.75  ? 164  PRO   B HG3  1 
ATOM   11440 H  HD2  . PRO   B  2  160 ? 0.820   -31.091 -13.795  1.00 49.56  ? 164  PRO   B HD2  1 
ATOM   11441 H  HD3  . PRO   B  2  160 ? 0.715   -32.498 -13.064  1.00 49.56  ? 164  PRO   B HD3  1 
ATOM   11442 N  N    . VAL   B  2  161 ? 1.491   -32.051 -17.931  1.00 50.83  ? 165  VAL   B N    1 
ATOM   11443 C  CA   . VAL   B  2  161 ? 1.561   -31.210 -19.118  1.00 48.02  ? 165  VAL   B CA   1 
ATOM   11444 C  C    . VAL   B  2  161 ? 2.456   -31.880 -20.147  1.00 44.70  ? 165  VAL   B C    1 
ATOM   11445 O  O    . VAL   B  2  161 ? 3.338   -32.676 -19.810  1.00 44.23  ? 165  VAL   B O    1 
ATOM   11446 C  CB   . VAL   B  2  161 ? 2.096   -29.794 -18.806  1.00 47.21  ? 165  VAL   B CB   1 
ATOM   11447 C  CG1  . VAL   B  2  161 ? 1.127   -29.045 -17.916  1.00 48.87  ? 165  VAL   B CG1  1 
ATOM   11448 C  CG2  . VAL   B  2  161 ? 3.478   -29.875 -18.164  1.00 41.46  ? 165  VAL   B CG2  1 
ATOM   11449 H  H    . VAL   B  2  161 ? 2.241   -32.412 -17.718  1.00 61.03  ? 165  VAL   B H    1 
ATOM   11450 H  HA   . VAL   B  2  161 ? 0.667   -31.127 -19.486  1.00 57.66  ? 165  VAL   B HA   1 
ATOM   11451 H  HB   . VAL   B  2  161 ? 2.182   -29.299 -19.636  1.00 56.69  ? 165  VAL   B HB   1 
ATOM   11452 H  HG11 . VAL   B  2  161 ? 1.506   -28.181 -17.693  1.00 58.69  ? 165  VAL   B HG11 1 
ATOM   11453 H  HG12 . VAL   B  2  161 ? 0.290   -28.926 -18.391  1.00 58.69  ? 165  VAL   B HG12 1 
ATOM   11454 H  HG13 . VAL   B  2  161 ? 0.978   -29.560 -17.108  1.00 58.69  ? 165  VAL   B HG13 1 
ATOM   11455 H  HG21 . VAL   B  2  161 ? 3.782   -28.978 -17.953  1.00 49.79  ? 165  VAL   B HG21 1 
ATOM   11456 H  HG22 . VAL   B  2  161 ? 3.419   -30.403 -17.352  1.00 49.79  ? 165  VAL   B HG22 1 
ATOM   11457 H  HG23 . VAL   B  2  161 ? 4.092   -30.294 -18.787  1.00 49.79  ? 165  VAL   B HG23 1 
ATOM   11458 N  N    . SER   B  2  162 ? 2.222   -31.551 -21.412  1.00 46.60  ? 166  SER   B N    1 
ATOM   11459 C  CA   . SER   B  2  162 ? 3.152   -31.952 -22.448  1.00 46.83  ? 166  SER   B CA   1 
ATOM   11460 C  C    . SER   B  2  162 ? 4.499   -31.275 -22.194  1.00 45.63  ? 166  SER   B C    1 
ATOM   11461 O  O    . SER   B  2  162 ? 4.547   -30.132 -21.729  1.00 46.72  ? 166  SER   B O    1 
ATOM   11462 C  CB   . SER   B  2  162 ? 2.617   -31.575 -23.825  1.00 47.38  ? 166  SER   B CB   1 
ATOM   11463 O  OG   . SER   B  2  162 ? 3.313   -32.277 -24.838  1.00 51.27  ? 166  SER   B OG   1 
ATOM   11464 H  H    . SER   B  2  162 ? 1.541   -31.104 -21.688  1.00 55.96  ? 166  SER   B H    1 
ATOM   11465 H  HA   . SER   B  2  162 ? 3.276   -32.914 -22.437  1.00 56.24  ? 166  SER   B HA   1 
ATOM   11466 H  HB2  . SER   B  2  162 ? 1.675   -31.802 -23.873  1.00 56.90  ? 166  SER   B HB2  1 
ATOM   11467 H  HB3  . SER   B  2  162 ? 2.737   -30.622 -23.962  1.00 56.90  ? 166  SER   B HB3  1 
ATOM   11468 H  HG   . SER   B  2  162 ? 2.969   -32.116 -25.587  1.00 61.57  ? 166  SER   B HG   1 
ATOM   11469 N  N    . PRO   B  2  163 ? 5.618   -31.946 -22.509  1.00 42.28  ? 167  PRO   B N    1 
ATOM   11470 C  CA   . PRO   B  2  163 ? 5.760   -33.248 -23.167  1.00 40.76  ? 167  PRO   B CA   1 
ATOM   11471 C  C    . PRO   B  2  163 ? 5.963   -34.443 -22.235  1.00 42.55  ? 167  PRO   B C    1 
ATOM   11472 O  O    . PRO   B  2  163 ? 6.451   -35.476 -22.693  1.00 45.11  ? 167  PRO   B O    1 
ATOM   11473 C  CB   . PRO   B  2  163 ? 7.012   -33.042 -24.014  1.00 41.42  ? 167  PRO   B CB   1 
ATOM   11474 C  CG   . PRO   B  2  163 ? 7.869   -32.192 -23.129  1.00 39.56  ? 167  PRO   B CG   1 
ATOM   11475 C  CD   . PRO   B  2  163 ? 6.923   -31.271 -22.382  1.00 40.81  ? 167  PRO   B CD   1 
ATOM   11476 H  HA   . PRO   B  2  163 ? 4.973   -33.420 -23.707  1.00 48.95  ? 167  PRO   B HA   1 
ATOM   11477 H  HB2  . PRO   B  2  163 ? 7.434   -33.893 -24.207  1.00 49.74  ? 167  PRO   B HB2  1 
ATOM   11478 H  HB3  . PRO   B  2  163 ? 6.791   -32.585 -24.841  1.00 49.74  ? 167  PRO   B HB3  1 
ATOM   11479 H  HG2  . PRO   B  2  163 ? 8.358   -32.756 -22.510  1.00 47.51  ? 167  PRO   B HG2  1 
ATOM   11480 H  HG3  . PRO   B  2  163 ? 8.489   -31.679 -23.671  1.00 47.51  ? 167  PRO   B HG3  1 
ATOM   11481 H  HD2  . PRO   B  2  163 ? 7.182   -31.193 -21.451  1.00 49.01  ? 167  PRO   B HD2  1 
ATOM   11482 H  HD3  . PRO   B  2  163 ? 6.899   -30.394 -22.794  1.00 49.01  ? 167  PRO   B HD3  1 
ATOM   11483 N  N    . PHE   B  2  164 ? 5.604   -34.317 -20.960  1.00 42.55  ? 168  PHE   B N    1 
ATOM   11484 C  CA   . PHE   B  2  164 ? 5.794   -35.408 -20.012  1.00 42.76  ? 168  PHE   B CA   1 
ATOM   11485 C  C    . PHE   B  2  164 ? 4.616   -36.373 -19.972  1.00 42.27  ? 168  PHE   B C    1 
ATOM   11486 O  O    . PHE   B  2  164 ? 4.745   -37.456 -19.393  1.00 44.17  ? 168  PHE   B O    1 
ATOM   11487 C  CB   . PHE   B  2  164 ? 6.044   -34.843 -18.613  1.00 44.03  ? 168  PHE   B CB   1 
ATOM   11488 C  CG   . PHE   B  2  164 ? 7.127   -33.804 -18.570  1.00 45.11  ? 168  PHE   B CG   1 
ATOM   11489 C  CD1  . PHE   B  2  164 ? 8.352   -34.035 -19.174  1.00 47.87  ? 168  PHE   B CD1  1 
ATOM   11490 C  CD2  . PHE   B  2  164 ? 6.912   -32.590 -17.944  1.00 47.32  ? 168  PHE   B CD2  1 
ATOM   11491 C  CE1  . PHE   B  2  164 ? 9.347   -33.077 -19.141  1.00 49.66  ? 168  PHE   B CE1  1 
ATOM   11492 C  CE2  . PHE   B  2  164 ? 7.902   -31.627 -17.910  1.00 50.14  ? 168  PHE   B CE2  1 
ATOM   11493 C  CZ   . PHE   B  2  164 ? 9.121   -31.871 -18.510  1.00 50.05  ? 168  PHE   B CZ   1 
ATOM   11494 H  H    . PHE   B  2  164 ? 5.250   -33.610 -20.622  1.00 51.10  ? 168  PHE   B H    1 
ATOM   11495 H  HA   . PHE   B  2  164 ? 6.578   -35.917 -20.272  1.00 51.35  ? 168  PHE   B HA   1 
ATOM   11496 H  HB2  . PHE   B  2  164 ? 5.227   -34.433 -18.290  1.00 52.87  ? 168  PHE   B HB2  1 
ATOM   11497 H  HB3  . PHE   B  2  164 ? 6.306   -35.569 -18.025  1.00 52.87  ? 168  PHE   B HB3  1 
ATOM   11498 H  HD1  . PHE   B  2  164 ? 8.507   -34.844 -19.605  1.00 57.48  ? 168  PHE   B HD1  1 
ATOM   11499 H  HD2  . PHE   B  2  164 ? 6.091   -32.419 -17.541  1.00 56.82  ? 168  PHE   B HD2  1 
ATOM   11500 H  HE1  . PHE   B  2  164 ? 10.168  -33.244 -19.545  1.00 59.63  ? 168  PHE   B HE1  1 
ATOM   11501 H  HE2  . PHE   B  2  164 ? 7.747   -30.816 -17.483  1.00 60.21  ? 168  PHE   B HE2  1 
ATOM   11502 H  HZ   . PHE   B  2  164 ? 9.788   -31.224 -18.488  1.00 60.10  ? 168  PHE   B HZ   1 
ATOM   11503 N  N    . VAL   B  2  165 ? 3.482   -36.010 -20.569  1.00 42.58  ? 169  VAL   B N    1 
ATOM   11504 C  CA   . VAL   B  2  165 ? 2.324   -36.887 -20.669  1.00 43.51  ? 169  VAL   B CA   1 
ATOM   11505 C  C    . VAL   B  2  165 ? 1.786   -36.822 -22.091  1.00 45.71  ? 169  VAL   B C    1 
ATOM   11506 O  O    . VAL   B  2  165 ? 1.912   -35.803 -22.776  1.00 46.22  ? 169  VAL   B O    1 
ATOM   11507 C  CB   . VAL   B  2  165 ? 1.209   -36.504 -19.669  1.00 41.28  ? 169  VAL   B CB   1 
ATOM   11508 C  CG1  . VAL   B  2  165 ? 1.734   -36.507 -18.241  1.00 38.53  ? 169  VAL   B CG1  1 
ATOM   11509 C  CG2  . VAL   B  2  165 ? 0.613   -35.144 -20.028  1.00 39.02  ? 169  VAL   B CG2  1 
ATOM   11510 H  H    . VAL   B  2  165 ? 3.359   -35.241 -20.932  1.00 51.13  ? 169  VAL   B H    1 
ATOM   11511 H  HA   . VAL   B  2  165 ? 2.607   -37.795 -20.479  1.00 52.25  ? 169  VAL   B HA   1 
ATOM   11512 H  HB   . VAL   B  2  165 ? 0.502   -37.165 -19.723  1.00 49.57  ? 169  VAL   B HB   1 
ATOM   11513 H  HG11 . VAL   B  2  165 ? 1.011   -36.273 -17.638  1.00 46.27  ? 169  VAL   B HG11 1 
ATOM   11514 H  HG12 . VAL   B  2  165 ? 2.067   -37.394 -18.030  1.00 46.27  ? 169  VAL   B HG12 1 
ATOM   11515 H  HG13 . VAL   B  2  165 ? 2.451   -35.858 -18.167  1.00 46.27  ? 169  VAL   B HG13 1 
ATOM   11516 H  HG21 . VAL   B  2  165 ? -0.039  -34.897 -19.354  1.00 46.87  ? 169  VAL   B HG21 1 
ATOM   11517 H  HG22 . VAL   B  2  165 ? 1.325   -34.485 -20.056  1.00 46.87  ? 169  VAL   B HG22 1 
ATOM   11518 H  HG23 . VAL   B  2  165 ? 0.185   -35.206 -20.896  1.00 46.87  ? 169  VAL   B HG23 1 
ATOM   11519 N  N    . LYS   B  2  166 ? 1.177   -37.920 -22.531  1.00 49.32  ? 170  LYS   B N    1 
ATOM   11520 C  CA   . LYS   B  2  166 ? 0.393   -37.884 -23.757  1.00 52.94  ? 170  LYS   B CA   1 
ATOM   11521 C  C    . LYS   B  2  166 ? -0.805  -36.963 -23.558  1.00 58.16  ? 170  LYS   B C    1 
ATOM   11522 O  O    . LYS   B  2  166 ? -1.414  -36.937 -22.484  1.00 59.70  ? 170  LYS   B O    1 
ATOM   11523 C  CB   . LYS   B  2  166 ? -0.078  -39.287 -24.137  1.00 52.60  ? 170  LYS   B CB   1 
ATOM   11524 C  CG   . LYS   B  2  166 ? 1.035   -40.262 -24.488  1.00 52.39  ? 170  LYS   B CG   1 
ATOM   11525 C  CD   . LYS   B  2  166 ? 1.722   -39.889 -25.791  1.00 58.36  ? 170  LYS   B CD   1 
ATOM   11526 C  CE   . LYS   B  2  166 ? 2.585   -41.028 -26.314  1.00 65.96  ? 170  LYS   B CE   1 
ATOM   11527 N  NZ   . LYS   B  2  166 ? 1.770   -42.200 -26.743  1.00 73.96  ? 170  LYS   B NZ   1 
ATOM   11528 H  H    . LYS   B  2  166 ? 1.203   -38.687 -22.143  1.00 59.22  ? 170  LYS   B H    1 
ATOM   11529 H  HA   . LYS   B  2  166 ? 0.936   -37.551 -24.488  1.00 63.56  ? 170  LYS   B HA   1 
ATOM   11530 H  HB2  . LYS   B  2  166 ? -0.567  -39.661 -23.387  1.00 63.16  ? 170  LYS   B HB2  1 
ATOM   11531 H  HB3  . LYS   B  2  166 ? -0.659  -39.217 -24.910  1.00 63.16  ? 170  LYS   B HB3  1 
ATOM   11532 H  HG2  . LYS   B  2  166 ? 1.700   -40.256 -23.782  1.00 62.90  ? 170  LYS   B HG2  1 
ATOM   11533 H  HG3  . LYS   B  2  166 ? 0.662   -41.152 -24.585  1.00 62.90  ? 170  LYS   B HG3  1 
ATOM   11534 H  HD2  . LYS   B  2  166 ? 1.050   -39.683 -26.461  1.00 70.07  ? 170  LYS   B HD2  1 
ATOM   11535 H  HD3  . LYS   B  2  166 ? 2.291   -39.117 -25.645  1.00 70.07  ? 170  LYS   B HD3  1 
ATOM   11536 H  HE2  . LYS   B  2  166 ? 3.093   -40.717 -27.080  1.00 79.19  ? 170  LYS   B HE2  1 
ATOM   11537 H  HE3  . LYS   B  2  166 ? 3.188   -41.319 -25.612  1.00 79.19  ? 170  LYS   B HE3  1 
ATOM   11538 H  HZ1  . LYS   B  2  166 ? 2.284   -42.789 -27.169  1.00 88.78  ? 170  LYS   B HZ1  1 
ATOM   11539 H  HZ2  . LYS   B  2  166 ? 1.407   -42.595 -26.032  1.00 88.78  ? 170  LYS   B HZ2  1 
ATOM   11540 H  HZ3  . LYS   B  2  166 ? 1.120   -41.935 -27.289  1.00 88.78  ? 170  LYS   B HZ3  1 
ATOM   11541 N  N    . THR   B  2  167 ? -1.147  -36.202 -24.600  1.00 59.44  ? 171  THR   B N    1 
ATOM   11542 C  CA   . THR   B  2  167 ? -2.204  -35.201 -24.504  1.00 54.56  ? 171  THR   B CA   1 
ATOM   11543 C  C    . THR   B  2  167 ? -3.354  -35.461 -25.473  1.00 54.51  ? 171  THR   B C    1 
ATOM   11544 O  O    . THR   B  2  167 ? -4.079  -34.528 -25.831  1.00 53.40  ? 171  THR   B O    1 
ATOM   11545 C  CB   . THR   B  2  167 ? -1.630  -33.801 -24.729  1.00 51.76  ? 171  THR   B CB   1 
ATOM   11546 O  OG1  . THR   B  2  167 ? -0.808  -33.800 -25.903  1.00 54.38  ? 171  THR   B OG1  1 
ATOM   11547 C  CG2  . THR   B  2  167 ? -0.802  -33.368 -23.526  1.00 50.07  ? 171  THR   B CG2  1 
ATOM   11548 H  H    . THR   B  2  167 ? -0.779  -36.250 -25.375  1.00 71.36  ? 171  THR   B H    1 
ATOM   11549 H  HA   . THR   B  2  167 ? -2.574  -35.240 -23.608  1.00 65.51  ? 171  THR   B HA   1 
ATOM   11550 H  HB   . THR   B  2  167 ? -2.354  -33.166 -24.846  1.00 62.14  ? 171  THR   B HB   1 
ATOM   11551 H  HG1  . THR   B  2  167 ? -0.135  -33.312 -25.782  1.00 65.29  ? 171  THR   B HG1  1 
ATOM   11552 H  HG21 . THR   B  2  167 ? -0.466  -32.468 -23.662  1.00 60.13  ? 171  THR   B HG21 1 
ATOM   11553 H  HG22 . THR   B  2  167 ? -1.349  -33.382 -22.725  1.00 60.13  ? 171  THR   B HG22 1 
ATOM   11554 H  HG23 . THR   B  2  167 ? -0.051  -33.969 -23.406  1.00 60.13  ? 171  THR   B HG23 1 
ATOM   11555 N  N    . THR   B  2  168 ? -3.540  -36.706 -25.906  1.00 55.78  ? 172  THR   B N    1 
ATOM   11556 C  CA   . THR   B  2  168 ? -4.773  -37.041 -26.599  1.00 54.85  ? 172  THR   B CA   1 
ATOM   11557 C  C    . THR   B  2  168 ? -5.886  -37.251 -25.574  1.00 55.16  ? 172  THR   B C    1 
ATOM   11558 O  O    . THR   B  2  168 ? -5.619  -37.644 -24.435  1.00 53.07  ? 172  THR   B O    1 
ATOM   11559 C  CB   . THR   B  2  168 ? -4.602  -38.301 -27.440  1.00 59.77  ? 172  THR   B CB   1 
ATOM   11560 O  OG1  . THR   B  2  168 ? -4.337  -39.421 -26.585  1.00 61.18  ? 172  THR   B OG1  1 
ATOM   11561 C  CG2  . THR   B  2  168 ? -3.456  -38.139 -28.429  1.00 63.43  ? 172  THR   B CG2  1 
ATOM   11562 H  H    . THR   B  2  168 ? -2.982  -37.354 -25.812  1.00 66.97  ? 172  THR   B H    1 
ATOM   11563 H  HA   . THR   B  2  168 ? -5.022  -36.322 -27.201  1.00 65.86  ? 172  THR   B HA   1 
ATOM   11564 H  HB   . THR   B  2  168 ? -5.416  -38.464 -27.941  1.00 71.76  ? 172  THR   B HB   1 
ATOM   11565 H  HG1  . THR   B  2  168 ? -4.276  -40.123 -27.043  1.00 73.45  ? 172  THR   B HG1  1 
ATOM   11566 H  HG21 . THR   B  2  168 ? -3.361  -38.943 -28.962  1.00 76.15  ? 172  THR   B HG21 1 
ATOM   11567 H  HG22 . THR   B  2  168 ? -3.630  -37.389 -29.019  1.00 76.15  ? 172  THR   B HG22 1 
ATOM   11568 H  HG23 . THR   B  2  168 ? -2.626  -37.978 -27.952  1.00 76.15  ? 172  THR   B HG23 1 
ATOM   11569 N  N    . PRO   B  2  169 ? -7.143  -36.995 -25.946  1.00 59.84  ? 173  PRO   B N    1 
ATOM   11570 C  CA   . PRO   B  2  169 ? -8.227  -37.133 -24.957  1.00 57.10  ? 173  PRO   B CA   1 
ATOM   11571 C  C    . PRO   B  2  169 ? -8.231  -38.481 -24.261  1.00 59.22  ? 173  PRO   B C    1 
ATOM   11572 O  O    . PRO   B  2  169 ? -8.453  -38.554 -23.046  1.00 59.47  ? 173  PRO   B O    1 
ATOM   11573 C  CB   . PRO   B  2  169 ? -9.495  -36.925 -25.798  1.00 55.69  ? 173  PRO   B CB   1 
ATOM   11574 C  CG   . PRO   B  2  169 ? -9.046  -36.163 -26.996  1.00 55.95  ? 173  PRO   B CG   1 
ATOM   11575 C  CD   . PRO   B  2  169 ? -7.658  -36.649 -27.283  1.00 59.07  ? 173  PRO   B CD   1 
ATOM   11576 H  HA   . PRO   B  2  169 ? -8.162  -36.426 -24.297  1.00 68.56  ? 173  PRO   B HA   1 
ATOM   11577 H  HB2  . PRO   B  2  169 ? -9.867  -37.784 -26.053  1.00 66.86  ? 173  PRO   B HB2  1 
ATOM   11578 H  HB3  . PRO   B  2  169 ? -10.149 -36.418 -25.290  1.00 66.86  ? 173  PRO   B HB3  1 
ATOM   11579 H  HG2  . PRO   B  2  169 ? -9.637  -36.347 -27.743  1.00 67.18  ? 173  PRO   B HG2  1 
ATOM   11580 H  HG3  . PRO   B  2  169 ? -9.045  -35.213 -26.799  1.00 67.18  ? 173  PRO   B HG3  1 
ATOM   11581 H  HD2  . PRO   B  2  169 ? -7.677  -37.429 -27.859  1.00 70.92  ? 173  PRO   B HD2  1 
ATOM   11582 H  HD3  . PRO   B  2  169 ? -7.124  -35.949 -27.689  1.00 70.92  ? 173  PRO   B HD3  1 
ATOM   11583 N  N    . GLU   B  2  170 ? -7.972  -39.557 -25.006  1.00 64.65  ? 174  GLU   B N    1 
ATOM   11584 C  CA   . GLU   B  2  170 ? -8.029  -40.894 -24.430  1.00 73.43  ? 174  GLU   B CA   1 
ATOM   11585 C  C    . GLU   B  2  170 ? -6.967  -41.074 -23.352  1.00 70.87  ? 174  GLU   B C    1 
ATOM   11586 O  O    . GLU   B  2  170 ? -7.249  -41.591 -22.265  1.00 71.69  ? 174  GLU   B O    1 
ATOM   11587 C  CB   . GLU   B  2  170 ? -7.865  -41.943 -25.532  1.00 83.17  ? 174  GLU   B CB   1 
ATOM   11588 C  CG   . GLU   B  2  170 ? -8.974  -41.943 -26.583  1.00 95.81  ? 174  GLU   B CG   1 
ATOM   11589 C  CD   . GLU   B  2  170 ? -8.820  -40.843 -27.617  1.00 107.15 ? 174  GLU   B CD   1 
ATOM   11590 O  OE1  . GLU   B  2  170 ? -7.836  -40.078 -27.537  1.00 110.92 ? 174  GLU   B OE1  1 
ATOM   11591 O  OE2  . GLU   B  2  170 ? -9.687  -40.743 -28.511  1.00 113.79 ? 174  GLU   B OE2  1 
ATOM   11592 H  H    . GLU   B  2  170 ? -7.763  -39.537 -25.840  1.00 77.62  ? 174  GLU   B H    1 
ATOM   11593 H  HA   . GLU   B  2  170 ? -8.898  -41.021 -24.017  1.00 88.16  ? 174  GLU   B HA   1 
ATOM   11594 H  HB2  . GLU   B  2  170 ? -7.027  -41.778 -25.991  1.00 99.84  ? 174  GLU   B HB2  1 
ATOM   11595 H  HB3  . GLU   B  2  170 ? -7.851  -42.822 -25.121  1.00 99.84  ? 174  GLU   B HB3  1 
ATOM   11596 H  HG2  . GLU   B  2  170 ? -8.964  -42.794 -27.049  1.00 115.01 ? 174  GLU   B HG2  1 
ATOM   11597 H  HG3  . GLU   B  2  170 ? -9.827  -41.818 -26.139  1.00 115.01 ? 174  GLU   B HG3  1 
ATOM   11598 N  N    . GLU   B  2  171 ? -5.733  -40.649 -23.635  1.00 68.11  ? 175  GLU   B N    1 
ATOM   11599 C  CA   . GLU   B  2  171 ? -4.648  -40.833 -22.677  1.00 62.53  ? 175  GLU   B CA   1 
ATOM   11600 C  C    . GLU   B  2  171 ? -4.736  -39.848 -21.516  1.00 55.79  ? 175  GLU   B C    1 
ATOM   11601 O  O    . GLU   B  2  171 ? -4.224  -40.138 -20.429  1.00 54.14  ? 175  GLU   B O    1 
ATOM   11602 C  CB   . GLU   B  2  171 ? -3.296  -40.700 -23.384  1.00 66.09  ? 175  GLU   B CB   1 
ATOM   11603 C  CG   . GLU   B  2  171 ? -3.056  -41.729 -24.492  1.00 72.84  ? 175  GLU   B CG   1 
ATOM   11604 C  CD   . GLU   B  2  171 ? -2.374  -42.994 -24.002  1.00 81.63  ? 175  GLU   B CD   1 
ATOM   11605 O  OE1  . GLU   B  2  171 ? -2.251  -43.176 -22.773  1.00 84.85  ? 175  GLU   B OE1  1 
ATOM   11606 O  OE2  . GLU   B  2  171 ? -1.954  -43.808 -24.852  1.00 85.77  ? 175  GLU   B OE2  1 
ATOM   11607 H  H    . GLU   B  2  171 ? -5.503  -40.258 -24.365  1.00 81.77  ? 175  GLU   B H    1 
ATOM   11608 H  HA   . GLU   B  2  171 ? -4.705  -41.729 -22.310  1.00 75.07  ? 175  GLU   B HA   1 
ATOM   11609 H  HB2  . GLU   B  2  171 ? -3.242  -39.819 -23.785  1.00 79.34  ? 175  GLU   B HB2  1 
ATOM   11610 H  HB3  . GLU   B  2  171 ? -2.592  -40.809 -22.726  1.00 79.34  ? 175  GLU   B HB3  1 
ATOM   11611 H  HG2  . GLU   B  2  171 ? -3.911  -41.981 -24.876  1.00 87.45  ? 175  GLU   B HG2  1 
ATOM   11612 H  HG3  . GLU   B  2  171 ? -2.491  -41.331 -25.173  1.00 87.45  ? 175  GLU   B HG3  1 
ATOM   11613 N  N    . ILE   B  2  172 ? -5.370  -38.690 -21.713  1.00 55.63  ? 176  ILE   B N    1 
ATOM   11614 C  CA   . ILE   B  2  172 ? -5.598  -37.779 -20.594  1.00 56.46  ? 176  ILE   B CA   1 
ATOM   11615 C  C    . ILE   B  2  172 ? -6.565  -38.407 -19.598  1.00 56.78  ? 176  ILE   B C    1 
ATOM   11616 O  O    . ILE   B  2  172 ? -6.334  -38.387 -18.385  1.00 57.74  ? 176  ILE   B O    1 
ATOM   11617 C  CB   . ILE   B  2  172 ? -6.116  -36.417 -21.093  1.00 58.02  ? 176  ILE   B CB   1 
ATOM   11618 C  CG1  . ILE   B  2  172 ? -5.032  -35.690 -21.893  1.00 61.61  ? 176  ILE   B CG1  1 
ATOM   11619 C  CG2  . ILE   B  2  172 ? -6.574  -35.554 -19.912  1.00 57.45  ? 176  ILE   B CG2  1 
ATOM   11620 C  CD1  . ILE   B  2  172 ? -5.487  -34.372 -22.504  1.00 65.03  ? 176  ILE   B CD1  1 
ATOM   11621 H  H    . ILE   B  2  172 ? -5.671  -38.415 -22.470  1.00 66.80  ? 176  ILE   B H    1 
ATOM   11622 H  HA   . ILE   B  2  172 ? -4.751  -37.627 -20.147  1.00 67.79  ? 176  ILE   B HA   1 
ATOM   11623 H  HB   . ILE   B  2  172 ? -6.875  -36.576 -21.676  1.00 69.66  ? 176  ILE   B HB   1 
ATOM   11624 H  HG12 . ILE   B  2  172 ? -4.286  -35.499 -21.303  1.00 73.97  ? 176  ILE   B HG12 1 
ATOM   11625 H  HG13 . ILE   B  2  172 ? -4.742  -36.266 -22.618  1.00 73.97  ? 176  ILE   B HG13 1 
ATOM   11626 H  HG21 . ILE   B  2  172 ? -6.872  -34.694 -20.246  1.00 68.98  ? 176  ILE   B HG21 1 
ATOM   11627 H  HG22 . ILE   B  2  172 ? -7.303  -36.003 -19.457  1.00 68.98  ? 176  ILE   B HG22 1 
ATOM   11628 H  HG23 . ILE   B  2  172 ? -5.829  -35.432 -19.303  1.00 68.98  ? 176  ILE   B HG23 1 
ATOM   11629 H  HD11 . ILE   B  2  172 ? -4.760  -33.998 -23.025  1.00 78.08  ? 176  ILE   B HD11 1 
ATOM   11630 H  HD12 . ILE   B  2  172 ? -6.253  -34.537 -23.075  1.00 78.08  ? 176  ILE   B HD12 1 
ATOM   11631 H  HD13 . ILE   B  2  172 ? -5.731  -33.761 -21.791  1.00 78.08  ? 176  ILE   B HD13 1 
ATOM   11632 N  N    . ALA   B  2  173 ? -7.665  -38.972 -20.100  1.00 53.40  ? 177  ALA   B N    1 
ATOM   11633 C  CA   . ALA   B  2  173 ? -8.653  -39.583 -19.220  1.00 53.80  ? 177  ALA   B CA   1 
ATOM   11634 C  C    . ALA   B  2  173 ? -8.102  -40.823 -18.533  1.00 56.59  ? 177  ALA   B C    1 
ATOM   11635 O  O    . ALA   B  2  173 ? -8.446  -41.098 -17.378  1.00 58.40  ? 177  ALA   B O    1 
ATOM   11636 C  CB   . ALA   B  2  173 ? -9.908  -39.941 -20.016  1.00 54.29  ? 177  ALA   B CB   1 
ATOM   11637 H  H    . ALA   B  2  173 ? -7.860  -39.012 -20.937  1.00 64.12  ? 177  ALA   B H    1 
ATOM   11638 H  HA   . ALA   B  2  173 ? -8.899  -38.942 -18.534  1.00 64.59  ? 177  ALA   B HA   1 
ATOM   11639 H  HB1  . ALA   B  2  173 ? -10.556 -40.345 -19.418  1.00 65.18  ? 177  ALA   B HB1  1 
ATOM   11640 H  HB2  . ALA   B  2  173 ? -10.277 -39.132 -20.404  1.00 65.18  ? 177  ALA   B HB2  1 
ATOM   11641 H  HB3  . ALA   B  2  173 ? -9.669  -40.566 -20.717  1.00 65.18  ? 177  ALA   B HB3  1 
ATOM   11642 N  N    . ASN   B  2  174 ? -7.247  -41.576 -19.223  1.00 56.74  ? 178  ASN   B N    1 
ATOM   11643 C  CA   . ASN   B  2  174 ? -6.704  -42.827 -18.694  1.00 53.47  ? 178  ASN   B CA   1 
ATOM   11644 C  C    . ASN   B  2  174 ? -5.341  -43.040 -19.333  1.00 52.71  ? 178  ASN   B C    1 
ATOM   11645 O  O    . ASN   B  2  174 ? -5.229  -43.644 -20.407  1.00 55.28  ? 178  ASN   B O    1 
ATOM   11646 C  CB   . ASN   B  2  174 ? -7.638  -44.002 -18.979  1.00 54.43  ? 178  ASN   B CB   1 
ATOM   11647 C  CG   . ASN   B  2  174 ? -7.077  -45.330 -18.508  1.00 58.86  ? 178  ASN   B CG   1 
ATOM   11648 O  OD1  . ASN   B  2  174 ? -5.979  -45.400 -17.955  1.00 59.90  ? 178  ASN   B OD1  1 
ATOM   11649 N  ND2  . ASN   B  2  174 ? -7.839  -46.397 -18.719  1.00 63.95  ? 178  ASN   B ND2  1 
ATOM   11650 H  H    . ASN   B  2  174 ? -6.962  -41.382 -20.011  1.00 68.12  ? 178  ASN   B H    1 
ATOM   11651 H  HA   . ASN   B  2  174 ? -6.587  -42.764 -17.734  1.00 64.20  ? 178  ASN   B HA   1 
ATOM   11652 H  HB2  . ASN   B  2  174 ? -8.480  -43.854 -18.520  1.00 65.36  ? 178  ASN   B HB2  1 
ATOM   11653 H  HB3  . ASN   B  2  174 ? -7.788  -44.062 -19.935  1.00 65.36  ? 178  ASN   B HB3  1 
ATOM   11654 H  HD21 . ASN   B  2  174 ? -7.569  -47.174 -18.471  1.00 76.78  ? 178  ASN   B HD21 1 
ATOM   11655 H  HD22 . ASN   B  2  174 ? -8.604  -46.309 -19.102  1.00 76.78  ? 178  ASN   B HD22 1 
ATOM   11656 N  N    . PRO   B  2  175 ? -4.271  -42.549 -18.698  1.00 49.58  ? 179  PRO   B N    1 
ATOM   11657 C  CA   . PRO   B  2  175 ? -2.946  -42.606 -19.340  1.00 47.71  ? 179  PRO   B CA   1 
ATOM   11658 C  C    . PRO   B  2  175 ? -2.456  -44.013 -19.644  1.00 53.07  ? 179  PRO   B C    1 
ATOM   11659 O  O    . PRO   B  2  175 ? -1.444  -44.151 -20.343  1.00 54.20  ? 179  PRO   B O    1 
ATOM   11660 C  CB   . PRO   B  2  175 ? -2.028  -41.903 -18.328  1.00 42.25  ? 179  PRO   B CB   1 
ATOM   11661 C  CG   . PRO   B  2  175 ? -2.768  -41.931 -17.035  1.00 41.13  ? 179  PRO   B CG   1 
ATOM   11662 C  CD   . PRO   B  2  175 ? -4.218  -41.878 -17.387  1.00 47.73  ? 179  PRO   B CD   1 
ATOM   11663 H  HA   . PRO   B  2  175 ? -2.964  -42.096 -20.165  1.00 57.28  ? 179  PRO   B HA   1 
ATOM   11664 H  HB2  . PRO   B  2  175 ? -1.190  -42.385 -18.256  1.00 50.74  ? 179  PRO   B HB2  1 
ATOM   11665 H  HB3  . PRO   B  2  175 ? -1.864  -40.991 -18.612  1.00 50.74  ? 179  PRO   B HB3  1 
ATOM   11666 H  HG2  . PRO   B  2  175 ? -2.561  -42.749 -16.558  1.00 49.39  ? 179  PRO   B HG2  1 
ATOM   11667 H  HG3  . PRO   B  2  175 ? -2.517  -41.162 -16.500  1.00 49.39  ? 179  PRO   B HG3  1 
ATOM   11668 H  HD2  . PRO   B  2  175 ? -4.751  -42.356 -16.732  1.00 57.31  ? 179  PRO   B HD2  1 
ATOM   11669 H  HD3  . PRO   B  2  175 ? -4.524  -40.960 -17.457  1.00 57.31  ? 179  PRO   B HD3  1 
ATOM   11670 N  N    . CYS   B  2  176 ? -3.128  -45.052 -19.148  1.00 56.54  ? 180  CYS   B N    1 
ATOM   11671 C  CA   . CYS   B  2  176 ? -2.785  -46.432 -19.467  1.00 61.94  ? 180  CYS   B CA   1 
ATOM   11672 C  C    . CYS   B  2  176 ? -3.842  -47.095 -20.344  1.00 65.60  ? 180  CYS   B C    1 
ATOM   11673 O  O    . CYS   B  2  176 ? -3.912  -48.327 -20.402  1.00 66.80  ? 180  CYS   B O    1 
ATOM   11674 C  CB   . CYS   B  2  176 ? -2.589  -47.236 -18.183  1.00 61.47  ? 180  CYS   B CB   1 
ATOM   11675 S  SG   . CYS   B  2  176 ? -1.552  -46.422 -16.949  1.00 65.16  ? 180  CYS   B SG   1 
ATOM   11676 H  H    . CYS   B  2  176 ? -3.799  -44.979 -18.615  1.00 67.89  ? 180  CYS   B H    1 
ATOM   11677 H  HA   . CYS   B  2  176 ? -1.947  -46.437 -19.956  1.00 74.37  ? 180  CYS   B HA   1 
ATOM   11678 H  HB2  . CYS   B  2  176 ? -3.458  -47.393 -17.780  1.00 73.80  ? 180  CYS   B HB2  1 
ATOM   11679 H  HB3  . CYS   B  2  176 ? -2.171  -48.082 -18.407  1.00 73.80  ? 180  CYS   B HB3  1 
ATOM   11680 N  N    . SER   B  2  177 ? -4.668  -46.299 -21.030  1.00 65.24  ? 181  SER   B N    1 
ATOM   11681 C  CA   . SER   B  2  177 ? -5.741  -46.872 -21.836  1.00 67.50  ? 181  SER   B CA   1 
ATOM   11682 C  C    . SER   B  2  177 ? -5.198  -47.785 -22.925  1.00 69.93  ? 181  SER   B C    1 
ATOM   11683 O  O    . SER   B  2  177 ? -5.860  -48.756 -23.309  1.00 72.83  ? 181  SER   B O    1 
ATOM   11684 C  CB   . SER   B  2  177 ? -6.587  -45.759 -22.457  1.00 68.45  ? 181  SER   B CB   1 
ATOM   11685 O  OG   . SER   B  2  177 ? -5.801  -44.914 -23.280  1.00 70.06  ? 181  SER   B OG   1 
ATOM   11686 H  H    . SER   B  2  177 ? -4.628  -45.440 -21.044  1.00 78.33  ? 181  SER   B H    1 
ATOM   11687 H  HA   . SER   B  2  177 ? -6.314  -47.399 -21.257  1.00 81.04  ? 181  SER   B HA   1 
ATOM   11688 H  HB2  . SER   B  2  177 ? -7.286  -46.160 -22.997  1.00 82.18  ? 181  SER   B HB2  1 
ATOM   11689 H  HB3  . SER   B  2  177 ? -6.979  -45.229 -21.746  1.00 82.18  ? 181  SER   B HB3  1 
ATOM   11690 H  HG   . SER   B  2  177 ? -5.447  -44.310 -22.816  1.00 84.11  ? 181  SER   B HG   1 
ATOM   11691 N  N    . SER   B  2  178 ? -4.000  -47.494 -23.433  1.00 71.39  ? 182  SER   B N    1 
ATOM   11692 C  CA   . SER   B  2  178 ? -3.426  -48.301 -24.500  1.00 74.70  ? 182  SER   B CA   1 
ATOM   11693 C  C    . SER   B  2  178 ? -2.945  -49.660 -24.010  1.00 77.54  ? 182  SER   B C    1 
ATOM   11694 O  O    . SER   B  2  178 ? -2.779  -50.574 -24.825  1.00 80.29  ? 182  SER   B O    1 
ATOM   11695 C  CB   . SER   B  2  178 ? -2.257  -47.556 -25.146  1.00 75.75  ? 182  SER   B CB   1 
ATOM   11696 O  OG   . SER   B  2  178 ? -1.196  -47.387 -24.220  1.00 80.21  ? 182  SER   B OG   1 
ATOM   11697 H  H    . SER   B  2  178 ? -3.505  -46.839 -23.177  1.00 85.70  ? 182  SER   B H    1 
ATOM   11698 H  HA   . SER   B  2  178 ? -4.109  -48.448 -25.173  1.00 89.67  ? 182  SER   B HA   1 
ATOM   11699 H  HB2  . SER   B  2  178 ? -1.936  -48.069 -25.905  1.00 90.94  ? 182  SER   B HB2  1 
ATOM   11700 H  HB3  . SER   B  2  178 ? -2.562  -46.684 -25.440  1.00 90.94  ? 182  SER   B HB3  1 
ATOM   11701 H  HG   . SER   B  2  178 ? -0.479  -47.236 -24.630  1.00 96.28  ? 182  SER   B HG   1 
ATOM   11702 N  N    . ILE   B  2  179 ? -2.730  -49.817 -22.703  1.00 75.23  ? 183  ILE   B N    1 
ATOM   11703 C  CA   . ILE   B  2  179 ? -2.038  -51.008 -22.209  1.00 77.54  ? 183  ILE   B CA   1 
ATOM   11704 C  C    . ILE   B  2  179 ? -2.830  -52.282 -22.480  1.00 81.27  ? 183  ILE   B C    1 
ATOM   11705 O  O    . ILE   B  2  179 ? -2.253  -53.233 -23.032  1.00 88.34  ? 183  ILE   B O    1 
ATOM   11706 C  CB   . ILE   B  2  179 ? -1.664  -50.821 -20.726  1.00 78.85  ? 183  ILE   B CB   1 
ATOM   11707 C  CG1  . ILE   B  2  179 ? -0.486  -49.835 -20.633  1.00 75.01  ? 183  ILE   B CG1  1 
ATOM   11708 C  CG2  . ILE   B  2  179 ? -1.319  -52.153 -20.072  1.00 80.47  ? 183  ILE   B CG2  1 
ATOM   11709 C  CD1  . ILE   B  2  179 ? 0.222   -49.781 -19.287  1.00 75.73  ? 183  ILE   B CD1  1 
ATOM   11710 H  H    . ILE   B  2  179 ? -2.969  -49.260 -22.093  1.00 90.31  ? 183  ILE   B H    1 
ATOM   11711 H  HA   . ILE   B  2  179 ? -1.206  -51.088 -22.700  1.00 93.09  ? 183  ILE   B HA   1 
ATOM   11712 H  HB   . ILE   B  2  179 ? -2.426  -50.458 -20.247  1.00 94.66  ? 183  ILE   B HB   1 
ATOM   11713 H  HG12 . ILE   B  2  179 ? 0.175   -50.087 -21.296  1.00 90.05  ? 183  ILE   B HG12 1 
ATOM   11714 H  HG13 . ILE   B  2  179 ? -0.820  -48.943 -20.818  1.00 90.05  ? 183  ILE   B HG13 1 
ATOM   11715 H  HG21 . ILE   B  2  179 ? -1.051  -51.995 -19.154  1.00 96.60  ? 183  ILE   B HG21 1 
ATOM   11716 H  HG22 . ILE   B  2  179 ? -2.101  -52.727 -20.095  1.00 96.60  ? 183  ILE   B HG22 1 
ATOM   11717 H  HG23 . ILE   B  2  179 ? -0.591  -52.566 -20.563  1.00 96.60  ? 183  ILE   B HG23 1 
ATOM   11718 H  HD11 . ILE   B  2  179 ? 0.806   -49.007 -19.268  1.00 90.91  ? 183  ILE   B HD11 1 
ATOM   11719 H  HD12 . ILE   B  2  179 ? -0.441  -49.713 -18.583  1.00 90.91  ? 183  ILE   B HD12 1 
ATOM   11720 H  HD13 . ILE   B  2  179 ? 0.744   -50.591 -19.172  1.00 90.91  ? 183  ILE   B HD13 1 
ATOM   11721 N  N    . PRO   B  2  180 ? -4.123  -52.388 -22.125  1.00 77.77  ? 184  PRO   B N    1 
ATOM   11722 C  CA   . PRO   B  2  180 ? -4.979  -51.529 -21.301  1.00 76.50  ? 184  PRO   B CA   1 
ATOM   11723 C  C    . PRO   B  2  180 ? -4.862  -51.848 -19.817  1.00 71.15  ? 184  PRO   B C    1 
ATOM   11724 O  O    . PRO   B  2  180 ? -4.608  -52.990 -19.449  1.00 68.07  ? 184  PRO   B O    1 
ATOM   11725 C  CB   . PRO   B  2  180 ? -6.387  -51.852 -21.809  1.00 76.90  ? 184  PRO   B CB   1 
ATOM   11726 C  CG   . PRO   B  2  180 ? -6.295  -53.262 -22.251  1.00 78.78  ? 184  PRO   B CG   1 
ATOM   11727 C  CD   . PRO   B  2  180 ? -4.916  -53.410 -22.835  1.00 79.99  ? 184  PRO   B CD   1 
ATOM   11728 H  HA   . PRO   B  2  180 ? -4.781  -50.592 -21.452  1.00 91.84  ? 184  PRO   B HA   1 
ATOM   11729 H  HB2  . PRO   B  2  180 ? -7.033  -51.750 -21.092  1.00 92.31  ? 184  PRO   B HB2  1 
ATOM   11730 H  HB3  . PRO   B  2  180 ? -6.618  -51.267 -22.548  1.00 92.31  ? 184  PRO   B HB3  1 
ATOM   11731 H  HG2  . PRO   B  2  180 ? -6.413  -53.853 -21.491  1.00 94.58  ? 184  PRO   B HG2  1 
ATOM   11732 H  HG3  . PRO   B  2  180 ? -6.974  -53.442 -22.920  1.00 94.58  ? 184  PRO   B HG3  1 
ATOM   11733 H  HD2  . PRO   B  2  180 ? -4.564  -54.298 -22.663  1.00 96.02  ? 184  PRO   B HD2  1 
ATOM   11734 H  HD3  . PRO   B  2  180 ? -4.926  -53.236 -23.789  1.00 96.02  ? 184  PRO   B HD3  1 
ATOM   11735 N  N    . TYR   B  2  181 ? -5.058  -50.833 -18.982  1.00 67.24  ? 185  TYR   B N    1 
ATOM   11736 C  CA   . TYR   B  2  181 ? -4.978  -50.975 -17.536  1.00 67.84  ? 185  TYR   B CA   1 
ATOM   11737 C  C    . TYR   B  2  181 ? -5.668  -49.762 -16.935  1.00 62.53  ? 185  TYR   B C    1 
ATOM   11738 O  O    . TYR   B  2  181 ? -5.677  -48.686 -17.539  1.00 59.73  ? 185  TYR   B O    1 
ATOM   11739 C  CB   . TYR   B  2  181 ? -3.524  -51.072 -17.062  1.00 69.69  ? 185  TYR   B CB   1 
ATOM   11740 C  CG   . TYR   B  2  181 ? -3.369  -51.628 -15.668  1.00 66.15  ? 185  TYR   B CG   1 
ATOM   11741 C  CD1  . TYR   B  2  181 ? -3.337  -50.789 -14.563  1.00 62.68  ? 185  TYR   B CD1  1 
ATOM   11742 C  CD2  . TYR   B  2  181 ? -3.253  -52.995 -15.458  1.00 64.31  ? 185  TYR   B CD2  1 
ATOM   11743 C  CE1  . TYR   B  2  181 ? -3.195  -51.297 -13.287  1.00 62.12  ? 185  TYR   B CE1  1 
ATOM   11744 C  CE2  . TYR   B  2  181 ? -3.111  -53.512 -14.187  1.00 65.59  ? 185  TYR   B CE2  1 
ATOM   11745 C  CZ   . TYR   B  2  181 ? -3.082  -52.659 -13.105  1.00 65.87  ? 185  TYR   B CZ   1 
ATOM   11746 O  OH   . TYR   B  2  181 ? -2.941  -53.169 -11.835  1.00 71.26  ? 185  TYR   B OH   1 
ATOM   11747 H  H    . TYR   B  2  181 ? -5.243  -50.033 -19.236  1.00 80.72  ? 185  TYR   B H    1 
ATOM   11748 H  HA   . TYR   B  2  181 ? -5.432  -51.779 -17.240  1.00 81.45  ? 185  TYR   B HA   1 
ATOM   11749 H  HB2  . TYR   B  2  181 ? -3.038  -51.652 -17.668  1.00 83.66  ? 185  TYR   B HB2  1 
ATOM   11750 H  HB3  . TYR   B  2  181 ? -3.135  -50.183 -17.070  1.00 83.66  ? 185  TYR   B HB3  1 
ATOM   11751 H  HD1  . TYR   B  2  181 ? -3.412  -49.870 -14.685  1.00 75.25  ? 185  TYR   B HD1  1 
ATOM   11752 H  HD2  . TYR   B  2  181 ? -3.271  -53.573 -16.186  1.00 77.20  ? 185  TYR   B HD2  1 
ATOM   11753 H  HE1  . TYR   B  2  181 ? -3.176  -50.723 -12.555  1.00 74.58  ? 185  TYR   B HE1  1 
ATOM   11754 H  HE2  . TYR   B  2  181 ? -3.035  -54.431 -14.061  1.00 78.75  ? 185  TYR   B HE2  1 
ATOM   11755 H  HH   . TYR   B  2  181 ? -3.021  -52.554 -11.268  1.00 85.55  ? 185  TYR   B HH   1 
ATOM   11756 N  N    . PHE   B  2  182 ? -6.255  -49.934 -15.753  1.00 62.94  ? 186  PHE   B N    1 
ATOM   11757 C  CA   . PHE   B  2  182 ? -6.991  -48.834 -15.140  1.00 59.78  ? 186  PHE   B CA   1 
ATOM   11758 C  C    . PHE   B  2  182 ? -6.015  -47.913 -14.421  1.00 56.38  ? 186  PHE   B C    1 
ATOM   11759 O  O    . PHE   B  2  182 ? -5.437  -48.286 -13.394  1.00 59.81  ? 186  PHE   B O    1 
ATOM   11760 C  CB   . PHE   B  2  182 ? -8.059  -49.325 -14.172  1.00 59.96  ? 186  PHE   B CB   1 
ATOM   11761 C  CG   . PHE   B  2  182 ? -8.840  -48.203 -13.554  1.00 60.78  ? 186  PHE   B CG   1 
ATOM   11762 C  CD1  . PHE   B  2  182 ? -9.839  -47.568 -14.274  1.00 65.31  ? 186  PHE   B CD1  1 
ATOM   11763 C  CD2  . PHE   B  2  182 ? -8.547  -47.752 -12.278  1.00 61.15  ? 186  PHE   B CD2  1 
ATOM   11764 C  CE1  . PHE   B  2  182 ? -10.550 -46.520 -13.726  1.00 67.04  ? 186  PHE   B CE1  1 
ATOM   11765 C  CE2  . PHE   B  2  182 ? -9.256  -46.702 -11.721  1.00 63.20  ? 186  PHE   B CE2  1 
ATOM   11766 C  CZ   . PHE   B  2  182 ? -10.258 -46.084 -12.447  1.00 66.82  ? 186  PHE   B CZ   1 
ATOM   11767 H  H    . PHE   B  2  182 ? -6.241  -50.663 -15.297  1.00 75.57  ? 186  PHE   B H    1 
ATOM   11768 H  HA   . PHE   B  2  182 ? -7.435  -48.346 -15.852  1.00 71.77  ? 186  PHE   B HA   1 
ATOM   11769 H  HB2  . PHE   B  2  182 ? -8.680  -49.896 -14.650  1.00 71.99  ? 186  PHE   B HB2  1 
ATOM   11770 H  HB3  . PHE   B  2  182 ? -7.632  -49.823 -13.457  1.00 71.99  ? 186  PHE   B HB3  1 
ATOM   11771 H  HD1  . PHE   B  2  182 ? -10.033 -47.851 -15.139  1.00 78.41  ? 186  PHE   B HD1  1 
ATOM   11772 H  HD2  . PHE   B  2  182 ? -7.868  -48.158 -11.790  1.00 73.42  ? 186  PHE   B HD2  1 
ATOM   11773 H  HE1  . PHE   B  2  182 ? -11.225 -46.107 -14.216  1.00 80.49  ? 186  PHE   B HE1  1 
ATOM   11774 H  HE2  . PHE   B  2  182 ? -9.059  -46.412 -10.859  1.00 75.88  ? 186  PHE   B HE2  1 
ATOM   11775 H  HZ   . PHE   B  2  182 ? -10.735 -45.377 -12.075  1.00 80.22  ? 186  PHE   B HZ   1 
ATOM   11776 N  N    . CYS   B  2  183 ? -5.843  -46.708 -14.950  1.00 53.83  ? 187  CYS   B N    1 
ATOM   11777 C  CA   . CYS   B  2  183 ? -5.011  -45.690 -14.333  1.00 58.21  ? 187  CYS   B CA   1 
ATOM   11778 C  C    . CYS   B  2  183 ? -5.820  -44.416 -14.162  1.00 59.99  ? 187  CYS   B C    1 
ATOM   11779 O  O    . CYS   B  2  183 ? -6.771  -44.158 -14.905  1.00 64.03  ? 187  CYS   B O    1 
ATOM   11780 C  CB   . CYS   B  2  183 ? -3.761  -45.394 -15.168  1.00 61.50  ? 187  CYS   B CB   1 
ATOM   11781 S  SG   . CYS   B  2  183 ? -2.552  -46.736 -15.210  1.00 64.03  ? 187  CYS   B SG   1 
ATOM   11782 H  H    . CYS   B  2  183 ? -6.208  -46.452 -15.685  1.00 64.64  ? 187  CYS   B H    1 
ATOM   11783 H  HA   . CYS   B  2  183 ? -4.723  -45.996 -13.459  1.00 69.89  ? 187  CYS   B HA   1 
ATOM   11784 H  HB2  . CYS   B  2  183 ? -4.036  -45.219 -16.082  1.00 73.83  ? 187  CYS   B HB2  1 
ATOM   11785 H  HB3  . CYS   B  2  183 ? -3.320  -44.614 -14.798  1.00 73.83  ? 187  CYS   B HB3  1 
ATOM   11786 N  N    . LEU   B  2  184 ? -5.442  -43.641 -13.187  1.00 59.15  ? 188  LEU   B N    1 
ATOM   11787 C  CA   . LEU   B  2  184 ? -6.056  -42.335 -13.023  1.00 54.74  ? 188  LEU   B CA   1 
ATOM   11788 C  C    . LEU   B  2  184 ? -5.259  -41.282 -13.786  1.00 53.13  ? 188  LEU   B C    1 
ATOM   11789 O  O    . LEU   B  2  184 ? -4.052  -41.439 -13.995  1.00 54.05  ? 188  LEU   B O    1 
ATOM   11790 C  CB   . LEU   B  2  184 ? -6.122  -41.961 -11.547  1.00 53.84  ? 188  LEU   B CB   1 
ATOM   11791 C  CG   . LEU   B  2  184 ? -6.992  -42.879 -10.687  1.00 57.72  ? 188  LEU   B CG   1 
ATOM   11792 C  CD1  . LEU   B  2  184 ? -6.961  -42.425 -9.240   1.00 57.26  ? 188  LEU   B CD1  1 
ATOM   11793 C  CD2  . LEU   B  2  184 ? -8.423  -42.920 -11.206  1.00 59.74  ? 188  LEU   B CD2  1 
ATOM   11794 H  H    . LEU   B  2  184 ? -4.839  -43.835 -12.605  1.00 71.01  ? 188  LEU   B H    1 
ATOM   11795 H  HA   . LEU   B  2  184 ? -6.962  -42.347 -13.368  1.00 65.72  ? 188  LEU   B HA   1 
ATOM   11796 H  HB2  . LEU   B  2  184 ? -5.223  -41.986 -11.184  1.00 64.64  ? 188  LEU   B HB2  1 
ATOM   11797 H  HB3  . LEU   B  2  184 ? -6.484  -41.064 -11.475  1.00 64.64  ? 188  LEU   B HB3  1 
ATOM   11798 H  HG   . LEU   B  2  184 ? -6.638  -43.781 -10.733  1.00 69.31  ? 188  LEU   B HG   1 
ATOM   11799 H  HD11 . LEU   B  2  184 ? -7.537  -43.003 -8.716   1.00 68.75  ? 188  LEU   B HD11 1 
ATOM   11800 H  HD12 . LEU   B  2  184 ? -6.050  -42.480 -8.912   1.00 68.75  ? 188  LEU   B HD12 1 
ATOM   11801 H  HD13 . LEU   B  2  184 ? -7.276  -41.509 -9.190   1.00 68.75  ? 188  LEU   B HD13 1 
ATOM   11802 H  HD21 . LEU   B  2  184 ? -8.963  -43.454 -10.602  1.00 71.72  ? 188  LEU   B HD21 1 
ATOM   11803 H  HD22 . LEU   B  2  184 ? -8.770  -42.015 -11.246  1.00 71.72  ? 188  LEU   B HD22 1 
ATOM   11804 H  HD23 . LEU   B  2  184 ? -8.427  -43.315 -12.091  1.00 71.72  ? 188  LEU   B HD23 1 
ATOM   11805 N  N    . PRO   B  2  185 ? -5.910  -40.207 -14.226  1.00 52.77  ? 189  PRO   B N    1 
ATOM   11806 C  CA   . PRO   B  2  185 ? -5.188  -39.162 -14.959  1.00 52.16  ? 189  PRO   B CA   1 
ATOM   11807 C  C    . PRO   B  2  185 ? -3.978  -38.662 -14.181  1.00 51.83  ? 189  PRO   B C    1 
ATOM   11808 O  O    . PRO   B  2  185 ? -4.003  -38.553 -12.954  1.00 54.16  ? 189  PRO   B O    1 
ATOM   11809 C  CB   . PRO   B  2  185 ? -6.243  -38.063 -15.149  1.00 52.17  ? 189  PRO   B CB   1 
ATOM   11810 C  CG   . PRO   B  2  185 ? -7.405  -38.445 -14.273  1.00 52.24  ? 189  PRO   B CG   1 
ATOM   11811 C  CD   . PRO   B  2  185 ? -7.353  -39.926 -14.149  1.00 51.90  ? 189  PRO   B CD   1 
ATOM   11812 H  HA   . PRO   B  2  185 ? -4.900  -39.491 -15.825  1.00 62.63  ? 189  PRO   B HA   1 
ATOM   11813 H  HB2  . PRO   B  2  185 ? -5.874  -37.208 -14.877  1.00 62.64  ? 189  PRO   B HB2  1 
ATOM   11814 H  HB3  . PRO   B  2  185 ? -6.512  -38.027 -16.080  1.00 62.64  ? 189  PRO   B HB3  1 
ATOM   11815 H  HG2  . PRO   B  2  185 ? -7.311  -38.024 -13.404  1.00 62.72  ? 189  PRO   B HG2  1 
ATOM   11816 H  HG3  . PRO   B  2  185 ? -8.235  -38.165 -14.690  1.00 62.72  ? 189  PRO   B HG3  1 
ATOM   11817 H  HD2  . PRO   B  2  185 ? -7.719  -40.216 -13.298  1.00 62.32  ? 189  PRO   B HD2  1 
ATOM   11818 H  HD3  . PRO   B  2  185 ? -7.830  -40.353 -14.878  1.00 62.32  ? 189  PRO   B HD3  1 
ATOM   11819 N  N    . THR   B  2  186 ? -2.910  -38.359 -14.918  1.00 51.61  ? 190  THR   B N    1 
ATOM   11820 C  CA   . THR   B  2  186 ? -1.651  -37.955 -14.306  1.00 50.61  ? 190  THR   B CA   1 
ATOM   11821 C  C    . THR   B  2  186 ? -1.845  -36.738 -13.408  1.00 51.57  ? 190  THR   B C    1 
ATOM   11822 O  O    . THR   B  2  186 ? -2.641  -35.843 -13.706  1.00 55.48  ? 190  THR   B O    1 
ATOM   11823 C  CB   . THR   B  2  186 ? -0.620  -37.646 -15.394  1.00 46.95  ? 190  THR   B CB   1 
ATOM   11824 O  OG1  . THR   B  2  186 ? -0.643  -38.679 -16.387  1.00 46.67  ? 190  THR   B OG1  1 
ATOM   11825 C  CG2  . THR   B  2  186 ? 0.776   -37.562 -14.799  1.00 46.41  ? 190  THR   B CG2  1 
ATOM   11826 H  H    . THR   B  2  186 ? -2.890  -38.381 -15.778  1.00 61.97  ? 190  THR   B H    1 
ATOM   11827 H  HA   . THR   B  2  186 ? -1.316  -38.681 -13.757  1.00 60.77  ? 190  THR   B HA   1 
ATOM   11828 H  HB   . THR   B  2  186 ? -0.833  -36.793 -15.804  1.00 56.37  ? 190  THR   B HB   1 
ATOM   11829 H  HG1  . THR   B  2  186 ? -0.139  -39.310 -16.158  1.00 56.04  ? 190  THR   B HG1  1 
ATOM   11830 H  HG21 . THR   B  2  186 ? 1.424   -37.379 -15.498  1.00 55.73  ? 190  THR   B HG21 1 
ATOM   11831 H  HG22 . THR   B  2  186 ? 0.814   -36.852 -14.140  1.00 55.73  ? 190  THR   B HG22 1 
ATOM   11832 H  HG23 . THR   B  2  186 ? 1.005   -38.402 -14.370  1.00 55.73  ? 190  THR   B HG23 1 
ATOM   11833 N  N    . PHE   B  2  187 ? -1.101  -36.707 -12.303  1.00 47.95  ? 191  PHE   B N    1 
ATOM   11834 C  CA   . PHE   B  2  187 ? -1.211  -35.643 -11.316  1.00 46.05  ? 191  PHE   B CA   1 
ATOM   11835 C  C    . PHE   B  2  187 ? 0.162   -35.345 -10.732  1.00 47.07  ? 191  PHE   B C    1 
ATOM   11836 O  O    . PHE   B  2  187 ? 1.043   -36.208 -10.704  1.00 45.40  ? 191  PHE   B O    1 
ATOM   11837 C  CB   . PHE   B  2  187 ? -2.188  -36.020 -10.195  1.00 43.37  ? 191  PHE   B CB   1 
ATOM   11838 C  CG   . PHE   B  2  187 ? -1.764  -37.225 -9.403   1.00 45.13  ? 191  PHE   B CG   1 
ATOM   11839 C  CD1  . PHE   B  2  187 ? -2.152  -38.497 -9.789   1.00 46.24  ? 191  PHE   B CD1  1 
ATOM   11840 C  CD2  . PHE   B  2  187 ? -0.977  -37.084 -8.272   1.00 47.50  ? 191  PHE   B CD2  1 
ATOM   11841 C  CE1  . PHE   B  2  187 ? -1.763  -39.606 -9.062   1.00 49.94  ? 191  PHE   B CE1  1 
ATOM   11842 C  CE2  . PHE   B  2  187 ? -0.584  -38.188 -7.542   1.00 52.81  ? 191  PHE   B CE2  1 
ATOM   11843 C  CZ   . PHE   B  2  187 ? -0.978  -39.451 -7.936   1.00 53.36  ? 191  PHE   B CZ   1 
ATOM   11844 H  H    . PHE   B  2  187 ? -0.516  -37.305 -12.101  1.00 57.57  ? 191  PHE   B H    1 
ATOM   11845 H  HA   . PHE   B  2  187 ? -1.534  -34.835 -11.746  1.00 55.30  ? 191  PHE   B HA   1 
ATOM   11846 H  HB2  . PHE   B  2  187 ? -2.261  -35.273 -9.581   1.00 52.08  ? 191  PHE   B HB2  1 
ATOM   11847 H  HB3  . PHE   B  2  187 ? -3.054  -36.214 -10.587  1.00 52.08  ? 191  PHE   B HB3  1 
ATOM   11848 H  HD1  . PHE   B  2  187 ? -2.681  -38.606 -10.547  1.00 55.52  ? 191  PHE   B HD1  1 
ATOM   11849 H  HD2  . PHE   B  2  187 ? -0.709  -36.235 -8.002   1.00 57.04  ? 191  PHE   B HD2  1 
ATOM   11850 H  HE1  . PHE   B  2  187 ? -2.029  -40.456 -9.330   1.00 59.96  ? 191  PHE   B HE1  1 
ATOM   11851 H  HE2  . PHE   B  2  187 ? -0.055  -38.081 -6.784   1.00 63.41  ? 191  PHE   B HE2  1 
ATOM   11852 H  HZ   . PHE   B  2  187 ? -0.716  -40.196 -7.445   1.00 64.07  ? 191  PHE   B HZ   1 
ATOM   11853 N  N    . GLY   B  2  188 ? 0.329   -34.114 -10.251  1.00 47.60  ? 192  GLY   B N    1 
ATOM   11854 C  CA   . GLY   B  2  188 ? 1.608   -33.657 -9.740   1.00 46.45  ? 192  GLY   B CA   1 
ATOM   11855 C  C    . GLY   B  2  188 ? 1.900   -34.109 -8.324   1.00 48.15  ? 192  GLY   B C    1 
ATOM   11856 O  O    . GLY   B  2  188 ? 2.870   -34.834 -8.087   1.00 47.84  ? 192  GLY   B O    1 
ATOM   11857 H  H    . GLY   B  2  188 ? -0.293  -33.521 -10.212  1.00 57.16  ? 192  GLY   B H    1 
ATOM   11858 H  HA2  . GLY   B  2  188 ? 2.314   -33.994 -10.313  1.00 55.78  ? 192  GLY   B HA2  1 
ATOM   11859 H  HA3  . GLY   B  2  188 ? 1.624   -32.688 -9.755   1.00 55.78  ? 192  GLY   B HA3  1 
ATOM   11860 N  N    . PHE   B  2  189 ? 1.079   -33.676 -7.368   1.00 52.18  ? 193  PHE   B N    1 
ATOM   11861 C  CA   . PHE   B  2  189 ? 1.228   -34.098 -5.981   1.00 52.13  ? 193  PHE   B CA   1 
ATOM   11862 C  C    . PHE   B  2  189 ? -0.131  -34.085 -5.300   1.00 52.62  ? 193  PHE   B C    1 
ATOM   11863 O  O    . PHE   B  2  189 ? -0.837  -33.073 -5.335   1.00 49.35  ? 193  PHE   B O    1 
ATOM   11864 C  CB   . PHE   B  2  189 ? 2.203   -33.195 -5.216   1.00 51.41  ? 193  PHE   B CB   1 
ATOM   11865 C  CG   . PHE   B  2  189 ? 2.168   -33.398 -3.726   1.00 51.67  ? 193  PHE   B CG   1 
ATOM   11866 C  CD1  . PHE   B  2  189 ? 2.404   -34.649 -3.180   1.00 52.26  ? 193  PHE   B CD1  1 
ATOM   11867 C  CD2  . PHE   B  2  189 ? 1.897   -32.341 -2.872   1.00 49.26  ? 193  PHE   B CD2  1 
ATOM   11868 C  CE1  . PHE   B  2  189 ? 2.369   -34.843 -1.811   1.00 52.38  ? 193  PHE   B CE1  1 
ATOM   11869 C  CE2  . PHE   B  2  189 ? 1.863   -32.529 -1.502   1.00 45.64  ? 193  PHE   B CE2  1 
ATOM   11870 C  CZ   . PHE   B  2  189 ? 2.098   -33.782 -0.972   1.00 50.44  ? 193  PHE   B CZ   1 
ATOM   11871 H  H    . PHE   B  2  189 ? 0.424   -33.134 -7.501   1.00 62.65  ? 193  PHE   B H    1 
ATOM   11872 H  HA   . PHE   B  2  189 ? 1.572   -35.005 -5.968   1.00 62.59  ? 193  PHE   B HA   1 
ATOM   11873 H  HB2  . PHE   B  2  189 ? 3.105   -33.381 -5.520   1.00 61.73  ? 193  PHE   B HB2  1 
ATOM   11874 H  HB3  . PHE   B  2  189 ? 1.977   -32.269 -5.395   1.00 61.73  ? 193  PHE   B HB3  1 
ATOM   11875 H  HD1  . PHE   B  2  189 ? 2.588   -35.367 -3.741   1.00 62.75  ? 193  PHE   B HD1  1 
ATOM   11876 H  HD2  . PHE   B  2  189 ? 1.736   -31.495 -3.224   1.00 59.15  ? 193  PHE   B HD2  1 
ATOM   11877 H  HE1  . PHE   B  2  189 ? 2.527   -35.688 -1.457   1.00 62.89  ? 193  PHE   B HE1  1 
ATOM   11878 H  HE2  . PHE   B  2  189 ? 1.682   -31.812 -0.938   1.00 54.80  ? 193  PHE   B HE2  1 
ATOM   11879 H  HZ   . PHE   B  2  189 ? 2.075   -33.910 -0.051   1.00 60.56  ? 193  PHE   B HZ   1 
ATOM   11880 N  N    . LYS   B  2  190 ? -0.486  -35.210 -4.683   1.00 57.20  ? 194  LYS   B N    1 
ATOM   11881 C  CA   . LYS   B  2  190 ? -1.717  -35.350 -3.914   1.00 57.61  ? 194  LYS   B CA   1 
ATOM   11882 C  C    . LYS   B  2  190 ? -1.348  -35.565 -2.449   1.00 53.09  ? 194  LYS   B C    1 
ATOM   11883 O  O    . LYS   B  2  190 ? -0.774  -36.601 -2.097   1.00 51.15  ? 194  LYS   B O    1 
ATOM   11884 C  CB   . LYS   B  2  190 ? -2.558  -36.517 -4.430   1.00 59.52  ? 194  LYS   B CB   1 
ATOM   11885 C  CG   . LYS   B  2  190 ? -3.344  -36.242 -5.702   1.00 61.54  ? 194  LYS   B CG   1 
ATOM   11886 C  CD   . LYS   B  2  190 ? -4.023  -37.514 -6.197   1.00 68.14  ? 194  LYS   B CD   1 
ATOM   11887 C  CE   . LYS   B  2  190 ? -4.922  -37.251 -7.395   1.00 78.32  ? 194  LYS   B CE   1 
ATOM   11888 N  NZ   . LYS   B  2  190 ? -5.441  -38.516 -7.988   1.00 84.88  ? 194  LYS   B NZ   1 
ATOM   11889 H  H    . LYS   B  2  190 ? -0.013  -35.928 -4.697   1.00 68.68  ? 194  LYS   B H    1 
ATOM   11890 H  HA   . LYS   B  2  190 ? -2.234  -34.534 -3.993   1.00 69.17  ? 194  LYS   B HA   1 
ATOM   11891 H  HB2  . LYS   B  2  190 ? -1.966  -37.264 -4.612   1.00 71.47  ? 194  LYS   B HB2  1 
ATOM   11892 H  HB3  . LYS   B  2  190 ? -3.197  -36.761 -3.742   1.00 71.47  ? 194  LYS   B HB3  1 
ATOM   11893 H  HG2  . LYS   B  2  190 ? -4.027  -35.576 -5.524   1.00 73.88  ? 194  LYS   B HG2  1 
ATOM   11894 H  HG3  . LYS   B  2  190 ? -2.743  -35.923 -6.393   1.00 73.88  ? 194  LYS   B HG3  1 
ATOM   11895 H  HD2  . LYS   B  2  190 ? -3.345  -38.155 -6.462   1.00 81.81  ? 194  LYS   B HD2  1 
ATOM   11896 H  HD3  . LYS   B  2  190 ? -4.569  -37.883 -5.485   1.00 81.81  ? 194  LYS   B HD3  1 
ATOM   11897 H  HE2  . LYS   B  2  190 ? -5.679  -36.714 -7.114   1.00 94.02  ? 194  LYS   B HE2  1 
ATOM   11898 H  HE3  . LYS   B  2  190 ? -4.416  -36.781 -8.076   1.00 94.02  ? 194  LYS   B HE3  1 
ATOM   11899 H  HZ1  . LYS   B  2  190 ? -5.948  -38.334 -8.697   1.00 101.89 ? 194  LYS   B HZ1  1 
ATOM   11900 H  HZ2  . LYS   B  2  190 ? -4.764  -39.034 -8.242   1.00 101.89 ? 194  LYS   B HZ2  1 
ATOM   11901 H  HZ3  . LYS   B  2  190 ? -5.931  -38.955 -7.388   1.00 101.89 ? 194  LYS   B HZ3  1 
ATOM   11902 N  N    . HIS   B  2  191 ? -1.668  -34.587 -1.603   1.00 50.32  ? 195  HIS   B N    1 
ATOM   11903 C  CA   . HIS   B  2  191 ? -1.579  -34.759 -0.156   1.00 51.85  ? 195  HIS   B CA   1 
ATOM   11904 C  C    . HIS   B  2  191 ? -2.874  -35.409 0.311    1.00 54.75  ? 195  HIS   B C    1 
ATOM   11905 O  O    . HIS   B  2  191 ? -3.939  -34.781 0.281    1.00 57.64  ? 195  HIS   B O    1 
ATOM   11906 C  CB   . HIS   B  2  191 ? -1.347  -33.424 0.546    1.00 52.27  ? 195  HIS   B CB   1 
ATOM   11907 C  CG   . HIS   B  2  191 ? -1.482  -33.498 2.036    1.00 55.12  ? 195  HIS   B CG   1 
ATOM   11908 N  ND1  . HIS   B  2  191 ? -1.172  -34.633 2.753    1.00 54.46  ? 195  HIS   B ND1  1 
ATOM   11909 C  CD2  . HIS   B  2  191 ? -1.896  -32.583 2.944    1.00 55.58  ? 195  HIS   B CD2  1 
ATOM   11910 C  CE1  . HIS   B  2  191 ? -1.385  -34.414 4.038    1.00 55.97  ? 195  HIS   B CE1  1 
ATOM   11911 N  NE2  . HIS   B  2  191 ? -1.826  -33.177 4.181    1.00 56.34  ? 195  HIS   B NE2  1 
ATOM   11912 H  H    . HIS   B  2  191 ? -1.942  -33.808 -1.846   1.00 60.42  ? 195  HIS   B H    1 
ATOM   11913 H  HA   . HIS   B  2  191 ? -0.828  -35.333 0.062    1.00 62.25  ? 195  HIS   B HA   1 
ATOM   11914 H  HB2  . HIS   B  2  191 ? -0.450  -33.117 0.344    1.00 62.76  ? 195  HIS   B HB2  1 
ATOM   11915 H  HB3  . HIS   B  2  191 ? -1.999  -32.783 0.221    1.00 62.76  ? 195  HIS   B HB3  1 
ATOM   11916 H  HD2  . HIS   B  2  191 ? -2.175  -31.714 2.764    1.00 66.73  ? 195  HIS   B HD2  1 
ATOM   11917 H  HE1  . HIS   B  2  191 ? -1.248  -35.026 4.725    1.00 67.20  ? 195  HIS   B HE1  1 
ATOM   11918 H  HE2  . HIS   B  2  191 ? -2.036  -32.805 4.927    1.00 67.64  ? 195  HIS   B HE2  1 
ATOM   11919 N  N    . ILE   B  2  192 ? -2.792  -36.661 0.745    1.00 55.50  ? 196  ILE   B N    1 
ATOM   11920 C  CA   . ILE   B  2  192 ? -3.970  -37.489 0.968    1.00 56.42  ? 196  ILE   B CA   1 
ATOM   11921 C  C    . ILE   B  2  192 ? -4.308  -37.608 2.448    1.00 56.44  ? 196  ILE   B C    1 
ATOM   11922 O  O    . ILE   B  2  192 ? -5.445  -37.359 2.850    1.00 59.44  ? 196  ILE   B O    1 
ATOM   11923 C  CB   . ILE   B  2  192 ? -3.764  -38.878 0.321    1.00 57.59  ? 196  ILE   B CB   1 
ATOM   11924 C  CG1  . ILE   B  2  192 ? -3.516  -38.713 -1.183   1.00 56.26  ? 196  ILE   B CG1  1 
ATOM   11925 C  CG2  . ILE   B  2  192 ? -4.971  -39.773 0.582    1.00 60.56  ? 196  ILE   B CG2  1 
ATOM   11926 C  CD1  . ILE   B  2  192 ? -3.168  -39.993 -1.909   1.00 59.51  ? 196  ILE   B CD1  1 
ATOM   11927 H  H    . ILE   B  2  192 ? -2.050  -37.060 0.920    1.00 66.63  ? 196  ILE   B H    1 
ATOM   11928 H  HA   . ILE   B  2  192 ? -4.729  -37.065 0.537    1.00 67.74  ? 196  ILE   B HA   1 
ATOM   11929 H  HB   . ILE   B  2  192 ? -2.988  -39.302 0.719    1.00 69.15  ? 196  ILE   B HB   1 
ATOM   11930 H  HG12 . ILE   B  2  192 ? -4.320  -38.355 -1.591   1.00 67.55  ? 196  ILE   B HG12 1 
ATOM   11931 H  HG13 . ILE   B  2  192 ? -2.778  -38.096 -1.308   1.00 67.55  ? 196  ILE   B HG13 1 
ATOM   11932 H  HG21 . ILE   B  2  192 ? -4.834  -40.625 0.141    1.00 72.71  ? 196  ILE   B HG21 1 
ATOM   11933 H  HG22 . ILE   B  2  192 ? -5.064  -39.907 1.538    1.00 72.71  ? 196  ILE   B HG22 1 
ATOM   11934 H  HG23 . ILE   B  2  192 ? -5.766  -39.342 0.230    1.00 72.71  ? 196  ILE   B HG23 1 
ATOM   11935 H  HD11 . ILE   B  2  192 ? -3.021  -39.795 -2.847   1.00 71.45  ? 196  ILE   B HD11 1 
ATOM   11936 H  HD12 . ILE   B  2  192 ? -2.361  -40.367 -1.520   1.00 71.45  ? 196  ILE   B HD12 1 
ATOM   11937 H  HD13 . ILE   B  2  192 ? -3.902  -40.620 -1.814   1.00 71.45  ? 196  ILE   B HD13 1 
ATOM   11938 N  N    . LEU   B  2  193 ? -3.341  -37.990 3.273    1.00 55.48  ? 197  LEU   B N    1 
ATOM   11939 C  CA   . LEU   B  2  193 ? -3.584  -38.226 4.696    1.00 54.56  ? 197  LEU   B CA   1 
ATOM   11940 C  C    . LEU   B  2  193 ? -2.649  -37.377 5.542    1.00 50.91  ? 197  LEU   B C    1 
ATOM   11941 O  O    . LEU   B  2  193 ? -1.429  -37.627 5.548    1.00 53.07  ? 197  LEU   B O    1 
ATOM   11942 C  CB   . LEU   B  2  193 ? -3.400  -39.707 5.032    1.00 55.58  ? 197  LEU   B CB   1 
ATOM   11943 C  CG   . LEU   B  2  193 ? -3.444  -40.073 6.519    1.00 55.83  ? 197  LEU   B CG   1 
ATOM   11944 C  CD1  . LEU   B  2  193 ? -4.785  -39.699 7.135    1.00 53.39  ? 197  LEU   B CD1  1 
ATOM   11945 C  CD2  . LEU   B  2  193 ? -3.157  -41.553 6.715    1.00 57.07  ? 197  LEU   B CD2  1 
ATOM   11946 H  H    . LEU   B  2  193 ? -2.526  -38.121 3.032    1.00 66.61  ? 197  LEU   B H    1 
ATOM   11947 H  HA   . LEU   B  2  193 ? -4.495  -37.965 4.903    1.00 65.51  ? 197  LEU   B HA   1 
ATOM   11948 H  HB2  . LEU   B  2  193 ? -4.106  -40.206 4.593    1.00 66.73  ? 197  LEU   B HB2  1 
ATOM   11949 H  HB3  . LEU   B  2  193 ? -2.535  -39.988 4.694    1.00 66.73  ? 197  LEU   B HB3  1 
ATOM   11950 H  HG   . LEU   B  2  193 ? -2.758  -39.568 6.983    1.00 67.03  ? 197  LEU   B HG   1 
ATOM   11951 H  HD11 . LEU   B  2  193 ? -4.781  -39.943 8.073    1.00 64.11  ? 197  LEU   B HD11 1 
ATOM   11952 H  HD12 . LEU   B  2  193 ? -4.920  -38.743 7.042    1.00 64.11  ? 197  LEU   B HD12 1 
ATOM   11953 H  HD13 . LEU   B  2  193 ? -5.490  -40.179 6.672    1.00 64.11  ? 197  LEU   B HD13 1 
ATOM   11954 H  HD21 . LEU   B  2  193 ? -3.157  -41.752 7.664    1.00 68.52  ? 197  LEU   B HD21 1 
ATOM   11955 H  HD22 . LEU   B  2  193 ? -3.846  -42.070 6.269    1.00 68.52  ? 197  LEU   B HD22 1 
ATOM   11956 H  HD23 . LEU   B  2  193 ? -2.290  -41.759 6.334    1.00 68.52  ? 197  LEU   B HD23 1 
ATOM   11957 N  N    . PRO   B  2  194 ? -3.146  -36.377 6.270    1.00 50.63  ? 198  PRO   B N    1 
ATOM   11958 C  CA   . PRO   B  2  194 ? -2.281  -35.670 7.218    1.00 51.98  ? 198  PRO   B CA   1 
ATOM   11959 C  C    . PRO   B  2  194 ? -1.832  -36.604 8.332    1.00 54.01  ? 198  PRO   B C    1 
ATOM   11960 O  O    . PRO   B  2  194 ? -2.425  -37.657 8.576    1.00 57.18  ? 198  PRO   B O    1 
ATOM   11961 C  CB   . PRO   B  2  194 ? -3.172  -34.540 7.753    1.00 52.95  ? 198  PRO   B CB   1 
ATOM   11962 C  CG   . PRO   B  2  194 ? -4.330  -34.457 6.801    1.00 51.69  ? 198  PRO   B CG   1 
ATOM   11963 C  CD   . PRO   B  2  194 ? -4.517  -35.838 6.273    1.00 49.35  ? 198  PRO   B CD   1 
ATOM   11964 H  HA   . PRO   B  2  194 ? -1.510  -35.283 6.773    1.00 62.42  ? 198  PRO   B HA   1 
ATOM   11965 H  HB2  . PRO   B  2  194 ? -3.476  -34.758 8.648    1.00 63.57  ? 198  PRO   B HB2  1 
ATOM   11966 H  HB3  . PRO   B  2  194 ? -2.675  -33.707 7.766    1.00 63.57  ? 198  PRO   B HB3  1 
ATOM   11967 H  HG2  . PRO   B  2  194 ? -5.123  -34.159 7.274    1.00 62.06  ? 198  PRO   B HG2  1 
ATOM   11968 H  HG3  . PRO   B  2  194 ? -4.121  -33.839 6.083    1.00 62.06  ? 198  PRO   B HG3  1 
ATOM   11969 H  HD2  . PRO   B  2  194 ? -5.092  -36.358 6.856    1.00 59.26  ? 198  PRO   B HD2  1 
ATOM   11970 H  HD3  . PRO   B  2  194 ? -4.884  -35.820 5.376    1.00 59.26  ? 198  PRO   B HD3  1 
ATOM   11971 N  N    . LEU   B  2  195 ? -0.761  -36.203 9.011    1.00 53.88  ? 199  LEU   B N    1 
ATOM   11972 C  CA   . LEU   B  2  195 ? -0.193  -37.022 10.073   1.00 53.21  ? 199  LEU   B CA   1 
ATOM   11973 C  C    . LEU   B  2  195 ? -1.250  -37.369 11.113   1.00 55.16  ? 199  LEU   B C    1 
ATOM   11974 O  O    . LEU   B  2  195 ? -2.005  -36.503 11.564   1.00 53.25  ? 199  LEU   B O    1 
ATOM   11975 C  CB   . LEU   B  2  195 ? 0.970   -36.280 10.730   1.00 53.56  ? 199  LEU   B CB   1 
ATOM   11976 C  CG   . LEU   B  2  195 ? 2.166   -36.042 9.809    1.00 54.87  ? 199  LEU   B CG   1 
ATOM   11977 C  CD1  . LEU   B  2  195 ? 3.045   -34.934 10.350   1.00 57.05  ? 199  LEU   B CD1  1 
ATOM   11978 C  CD2  . LEU   B  2  195 ? 2.963   -37.322 9.643    1.00 52.06  ? 199  LEU   B CD2  1 
ATOM   11979 H  H    . LEU   B  2  195 ? -0.345  -35.462 8.874    1.00 64.70  ? 199  LEU   B H    1 
ATOM   11980 H  HA   . LEU   B  2  195 ? 0.143   -37.850 9.696    1.00 63.88  ? 199  LEU   B HA   1 
ATOM   11981 H  HB2  . LEU   B  2  195 ? 0.654   -35.415 11.031   1.00 64.30  ? 199  LEU   B HB2  1 
ATOM   11982 H  HB3  . LEU   B  2  195 ? 1.281   -36.802 11.486   1.00 64.30  ? 199  LEU   B HB3  1 
ATOM   11983 H  HG   . LEU   B  2  195 ? 1.845   -35.767 8.935    1.00 65.88  ? 199  LEU   B HG   1 
ATOM   11984 H  HD11 . LEU   B  2  195 ? 3.794   -34.802 9.748    1.00 68.49  ? 199  LEU   B HD11 1 
ATOM   11985 H  HD12 . LEU   B  2  195 ? 2.523   -34.118 10.412   1.00 68.49  ? 199  LEU   B HD12 1 
ATOM   11986 H  HD13 . LEU   B  2  195 ? 3.368   -35.187 11.229   1.00 68.49  ? 199  LEU   B HD13 1 
ATOM   11987 H  HD21 . LEU   B  2  195 ? 3.718   -37.150 9.059    1.00 62.51  ? 199  LEU   B HD21 1 
ATOM   11988 H  HD22 . LEU   B  2  195 ? 3.277   -37.613 10.514   1.00 62.51  ? 199  LEU   B HD22 1 
ATOM   11989 H  HD23 . LEU   B  2  195 ? 2.391   -38.002 9.254    1.00 62.51  ? 199  LEU   B HD23 1 
ATOM   11990 N  N    . THR   B  2  196 ? -1.301  -38.645 11.489   1.00 58.23  ? 200  THR   B N    1 
ATOM   11991 C  CA   . THR   B  2  196 ? -2.247  -39.101 12.494   1.00 63.17  ? 200  THR   B CA   1 
ATOM   11992 C  C    . THR   B  2  196 ? -1.708  -40.359 13.155   1.00 70.06  ? 200  THR   B C    1 
ATOM   11993 O  O    . THR   B  2  196 ? -0.868  -41.069 12.598   1.00 70.25  ? 200  THR   B O    1 
ATOM   11994 C  CB   . THR   B  2  196 ? -3.629  -39.383 11.893   1.00 65.44  ? 200  THR   B CB   1 
ATOM   11995 O  OG1  . THR   B  2  196 ? -4.472  -39.974 12.891   1.00 66.13  ? 200  THR   B OG1  1 
ATOM   11996 C  CG2  . THR   B  2  196 ? -3.511  -40.328 10.704   1.00 66.65  ? 200  THR   B CG2  1 
ATOM   11997 H  H    . THR   B  2  196 ? -0.794  -39.265 11.175   1.00 69.92  ? 200  THR   B H    1 
ATOM   11998 H  HA   . THR   B  2  196 ? -2.336  -38.409 13.168   1.00 75.84  ? 200  THR   B HA   1 
ATOM   11999 H  HB   . THR   B  2  196 ? -4.026  -38.554 11.584   1.00 78.57  ? 200  THR   B HB   1 
ATOM   12000 H  HG1  . THR   B  2  196 ? -5.234  -40.126 12.571   1.00 79.39  ? 200  THR   B HG1  1 
ATOM   12001 H  HG21 . THR   B  2  196 ? -4.391  -40.526 10.349   1.00 80.01  ? 200  THR   B HG21 1 
ATOM   12002 H  HG22 . THR   B  2  196 ? -2.974  -39.919 10.007   1.00 80.01  ? 200  THR   B HG22 1 
ATOM   12003 H  HG23 . THR   B  2  196 ? -3.090  -41.158 10.980   1.00 80.01  ? 200  THR   B HG23 1 
ATOM   12004 N  N    . ASN   B  2  197 ? -2.216  -40.622 14.360   1.00 78.33  ? 201  ASN   B N    1 
ATOM   12005 C  CA   . ASN   B  2  197 ? -1.903  -41.847 15.080   1.00 82.30  ? 201  ASN   B CA   1 
ATOM   12006 C  C    . ASN   B  2  197 ? -2.755  -43.027 14.634   1.00 81.91  ? 201  ASN   B C    1 
ATOM   12007 O  O    . ASN   B  2  197 ? -2.411  -44.173 14.944   1.00 81.18  ? 201  ASN   B O    1 
ATOM   12008 C  CB   . ASN   B  2  197 ? -2.093  -41.629 16.582   1.00 88.80  ? 201  ASN   B CB   1 
ATOM   12009 C  CG   . ASN   B  2  197 ? -3.457  -41.053 16.917   1.00 97.27  ? 201  ASN   B CG   1 
ATOM   12010 O  OD1  . ASN   B  2  197 ? -3.597  -39.852 17.147   1.00 100.96 ? 201  ASN   B OD1  1 
ATOM   12011 N  ND2  . ASN   B  2  197 ? -4.473  -41.907 16.929   1.00 99.88  ? 201  ASN   B ND2  1 
ATOM   12012 H  H    . ASN   B  2  197 ? -2.752  -40.099 14.784   1.00 94.03  ? 201  ASN   B H    1 
ATOM   12013 H  HA   . ASN   B  2  197 ? -0.973  -42.072 14.918   1.00 98.80  ? 201  ASN   B HA   1 
ATOM   12014 H  HB2  . ASN   B  2  197 ? -2.005  -42.480 17.040   1.00 106.60 ? 201  ASN   B HB2  1 
ATOM   12015 H  HB3  . ASN   B  2  197 ? -1.418  -41.009 16.901   1.00 106.60 ? 201  ASN   B HB3  1 
ATOM   12016 H  HD21 . ASN   B  2  197 ? -5.266  -41.629 17.114   1.00 119.89 ? 201  ASN   B HD21 1 
ATOM   12017 H  HD22 . ASN   B  2  197 ? -4.338  -42.738 16.753   1.00 119.89 ? 201  ASN   B HD22 1 
ATOM   12018 N  N    . ASP   B  2  198 ? -3.852  -42.777 13.924   1.00 78.03  ? 202  ASP   B N    1 
ATOM   12019 C  CA   . ASP   B  2  198 ? -4.753  -43.836 13.475   1.00 74.39  ? 202  ASP   B CA   1 
ATOM   12020 C  C    . ASP   B  2  198 ? -4.087  -44.595 12.335   1.00 70.25  ? 202  ASP   B C    1 
ATOM   12021 O  O    . ASP   B  2  198 ? -4.150  -44.181 11.176   1.00 68.22  ? 202  ASP   B O    1 
ATOM   12022 C  CB   . ASP   B  2  198 ? -6.087  -43.238 13.044   1.00 73.77  ? 202  ASP   B CB   1 
ATOM   12023 C  CG   . ASP   B  2  198 ? -7.113  -44.294 12.691   1.00 76.28  ? 202  ASP   B CG   1 
ATOM   12024 O  OD1  . ASP   B  2  198 ? -6.778  -45.494 12.761   1.00 77.73  ? 202  ASP   B OD1  1 
ATOM   12025 O  OD2  . ASP   B  2  198 ? -8.255  -43.922 12.345   1.00 77.01  ? 202  ASP   B OD2  1 
ATOM   12026 H  H    . ASP   B  2  198 ? -4.100  -41.989 13.685   1.00 93.68  ? 202  ASP   B H    1 
ATOM   12027 H  HA   . ASP   B  2  198 ? -4.918  -44.458 14.201   1.00 89.30  ? 202  ASP   B HA   1 
ATOM   12028 H  HB2  . ASP   B  2  198 ? -6.444  -42.704 13.770   1.00 88.56  ? 202  ASP   B HB2  1 
ATOM   12029 H  HB3  . ASP   B  2  198 ? -5.947  -42.683 12.261   1.00 88.56  ? 202  ASP   B HB3  1 
ATOM   12030 N  N    . ALA   B  2  199 ? -3.445  -45.719 12.662   1.00 72.76  ? 203  ALA   B N    1 
ATOM   12031 C  CA   . ALA   B  2  199 ? -2.691  -46.460 11.657   1.00 75.23  ? 203  ALA   B CA   1 
ATOM   12032 C  C    . ALA   B  2  199 ? -3.594  -47.257 10.724   1.00 75.96  ? 203  ALA   B C    1 
ATOM   12033 O  O    . ALA   B  2  199 ? -3.239  -47.461 9.557    1.00 71.62  ? 203  ALA   B O    1 
ATOM   12034 C  CB   . ALA   B  2  199 ? -1.686  -47.393 12.334   1.00 79.40  ? 203  ALA   B CB   1 
ATOM   12035 H  H    . ALA   B  2  199 ? -3.432  -46.068 13.448   1.00 87.35  ? 203  ALA   B H    1 
ATOM   12036 H  HA   . ALA   B  2  199 ? -2.195  -45.824 11.117   1.00 90.31  ? 203  ALA   B HA   1 
ATOM   12037 H  HB1  . ALA   B  2  199 ? -1.197  -47.880 11.652   1.00 95.32  ? 203  ALA   B HB1  1 
ATOM   12038 H  HB2  . ALA   B  2  199 ? -1.072  -46.864 12.867   1.00 95.32  ? 203  ALA   B HB2  1 
ATOM   12039 H  HB3  . ALA   B  2  199 ? -2.166  -48.015 12.903   1.00 95.32  ? 203  ALA   B HB3  1 
ATOM   12040 N  N    . GLU   B  2  200 ? -4.749  -47.723 11.205   1.00 81.22  ? 204  GLU   B N    1 
ATOM   12041 C  CA   . GLU   B  2  200 ? -5.682  -48.406 10.314   1.00 84.69  ? 204  GLU   B CA   1 
ATOM   12042 C  C    . GLU   B  2  200 ? -6.203  -47.465 9.236    1.00 84.13  ? 204  GLU   B C    1 
ATOM   12043 O  O    . GLU   B  2  200 ? -6.528  -47.908 8.128    1.00 82.00  ? 204  GLU   B O    1 
ATOM   12044 C  CB   . GLU   B  2  200 ? -6.847  -48.996 11.111   1.00 87.20  ? 204  GLU   B CB   1 
ATOM   12045 C  CG   . GLU   B  2  200 ? -6.566  -50.371 11.705   1.00 94.92  ? 204  GLU   B CG   1 
ATOM   12046 C  CD   . GLU   B  2  200 ? -6.293  -51.423 10.646   1.00 102.25 ? 204  GLU   B CD   1 
ATOM   12047 O  OE1  . GLU   B  2  200 ? -6.683  -51.208 9.479    1.00 103.87 ? 204  GLU   B OE1  1 
ATOM   12048 O  OE2  . GLU   B  2  200 ? -5.683  -52.461 10.979   1.00 105.56 ? 204  GLU   B OE2  1 
ATOM   12049 H  H    . GLU   B  2  200 ? -5.009  -47.657 12.022   1.00 97.51  ? 204  GLU   B H    1 
ATOM   12050 H  HA   . GLU   B  2  200 ? -5.219  -49.140 9.882    1.00 101.67 ? 204  GLU   B HA   1 
ATOM   12051 H  HB2  . GLU   B  2  200 ? -7.056  -48.396 11.844   1.00 104.68 ? 204  GLU   B HB2  1 
ATOM   12052 H  HB3  . GLU   B  2  200 ? -7.613  -49.081 10.522   1.00 104.68 ? 204  GLU   B HB3  1 
ATOM   12053 H  HG2  . GLU   B  2  200 ? -5.786  -50.314 12.280   1.00 113.94 ? 204  GLU   B HG2  1 
ATOM   12054 H  HG3  . GLU   B  2  200 ? -7.337  -50.656 12.220   1.00 113.94 ? 204  GLU   B HG3  1 
ATOM   12055 N  N    . ARG   B  2  201 ? -6.292  -46.169 9.541    1.00 83.43  ? 205  ARG   B N    1 
ATOM   12056 C  CA   . ARG   B  2  201 ? -6.679  -45.193 8.528    1.00 82.21  ? 205  ARG   B CA   1 
ATOM   12057 C  C    . ARG   B  2  201 ? -5.633  -45.117 7.424    1.00 72.41  ? 205  ARG   B C    1 
ATOM   12058 O  O    . ARG   B  2  201 ? -5.973  -45.064 6.237    1.00 71.03  ? 205  ARG   B O    1 
ATOM   12059 C  CB   . ARG   B  2  201 ? -6.886  -43.829 9.186    1.00 89.21  ? 205  ARG   B CB   1 
ATOM   12060 C  CG   . ARG   B  2  201 ? -7.296  -42.707 8.244    1.00 93.36  ? 205  ARG   B CG   1 
ATOM   12061 C  CD   . ARG   B  2  201 ? -8.655  -42.951 7.608    1.00 99.50  ? 205  ARG   B CD   1 
ATOM   12062 N  NE   . ARG   B  2  201 ? -9.048  -41.836 6.750    1.00 105.38 ? 205  ARG   B NE   1 
ATOM   12063 C  CZ   . ARG   B  2  201 ? -9.915  -41.923 5.745    1.00 115.73 ? 205  ARG   B CZ   1 
ATOM   12064 N  NH1  . ARG   B  2  201 ? -10.487 -43.083 5.448    1.00 122.37 ? 205  ARG   B NH1  1 
ATOM   12065 N  NH2  . ARG   B  2  201 ? -10.203 -40.847 5.027    1.00 119.68 ? 205  ARG   B NH2  1 
ATOM   12066 H  H    . ARG   B  2  201 ? -6.135  -45.835 10.318   1.00 100.16 ? 205  ARG   B H    1 
ATOM   12067 H  HA   . ARG   B  2  201 ? -7.519  -45.459 8.122    1.00 98.69  ? 205  ARG   B HA   1 
ATOM   12068 H  HB2  . ARG   B  2  201 ? -7.584  -43.915 9.855    1.00 107.09 ? 205  ARG   B HB2  1 
ATOM   12069 H  HB3  . ARG   B  2  201 ? -6.054  -43.563 9.608    1.00 107.09 ? 205  ARG   B HB3  1 
ATOM   12070 H  HG2  . ARG   B  2  201 ? -7.342  -41.875 8.741    1.00 112.07 ? 205  ARG   B HG2  1 
ATOM   12071 H  HG3  . ARG   B  2  201 ? -6.640  -42.633 7.533    1.00 112.07 ? 205  ARG   B HG3  1 
ATOM   12072 H  HD2  . ARG   B  2  201 ? -8.616  -43.755 7.066    1.00 119.44 ? 205  ARG   B HD2  1 
ATOM   12073 H  HD3  . ARG   B  2  201 ? -9.322  -43.052 8.304    1.00 119.44 ? 205  ARG   B HD3  1 
ATOM   12074 H  HE   . ARG   B  2  201 ? -8.694  -41.068 6.906    1.00 126.50 ? 205  ARG   B HE   1 
ATOM   12075 H  HH11 . ARG   B  2  201 ? -10.298 -43.786 5.907    1.00 146.88 ? 205  ARG   B HH11 1 
ATOM   12076 H  HH12 . ARG   B  2  201 ? -11.047 -43.132 4.797    1.00 146.88 ? 205  ARG   B HH12 1 
ATOM   12077 H  HH21 . ARG   B  2  201 ? -9.830  -40.094 5.211    1.00 143.66 ? 205  ARG   B HH21 1 
ATOM   12078 H  HH22 . ARG   B  2  201 ? -10.763 -40.901 4.377    1.00 143.66 ? 205  ARG   B HH22 1 
ATOM   12079 N  N    . PHE   B  2  202 ? -4.351  -45.112 7.798    1.00 64.96  ? 206  PHE   B N    1 
ATOM   12080 C  CA   . PHE   B  2  202 ? -3.279  -45.225 6.815    1.00 62.24  ? 206  PHE   B CA   1 
ATOM   12081 C  C    . PHE   B  2  202 ? -3.469  -46.466 5.950    1.00 61.98  ? 206  PHE   B C    1 
ATOM   12082 O  O    . PHE   B  2  202 ? -3.380  -46.401 4.719    1.00 57.77  ? 206  PHE   B O    1 
ATOM   12083 C  CB   . PHE   B  2  202 ? -1.932  -45.265 7.540    1.00 60.77  ? 206  PHE   B CB   1 
ATOM   12084 C  CG   . PHE   B  2  202 ? -0.740  -45.157 6.633    1.00 58.36  ? 206  PHE   B CG   1 
ATOM   12085 C  CD1  . PHE   B  2  202 ? -0.172  -46.288 6.074    1.00 58.64  ? 206  PHE   B CD1  1 
ATOM   12086 C  CD2  . PHE   B  2  202 ? -0.171  -43.924 6.361    1.00 56.05  ? 206  PHE   B CD2  1 
ATOM   12087 C  CE1  . PHE   B  2  202 ? 0.934   -46.191 5.249    1.00 56.60  ? 206  PHE   B CE1  1 
ATOM   12088 C  CE2  . PHE   B  2  202 ? 0.935   -43.820 5.540    1.00 52.85  ? 206  PHE   B CE2  1 
ATOM   12089 C  CZ   . PHE   B  2  202 ? 1.487   -44.954 4.982    1.00 52.83  ? 206  PHE   B CZ   1 
ATOM   12090 H  H    . PHE   B  2  202 ? -4.080  -45.044 8.612    1.00 77.99  ? 206  PHE   B H    1 
ATOM   12091 H  HA   . PHE   B  2  202 ? -3.287  -44.450 6.232    1.00 74.73  ? 206  PHE   B HA   1 
ATOM   12092 H  HB2  . PHE   B  2  202 ? -1.895  -44.524 8.165    1.00 72.96  ? 206  PHE   B HB2  1 
ATOM   12093 H  HB3  . PHE   B  2  202 ? -1.863  -46.106 8.018    1.00 72.96  ? 206  PHE   B HB3  1 
ATOM   12094 H  HD1  . PHE   B  2  202 ? -0.538  -47.124 6.254    1.00 70.41  ? 206  PHE   B HD1  1 
ATOM   12095 H  HD2  . PHE   B  2  202 ? -0.539  -43.156 6.735    1.00 67.30  ? 206  PHE   B HD2  1 
ATOM   12096 H  HE1  . PHE   B  2  202 ? 1.304   -46.957 4.874    1.00 67.96  ? 206  PHE   B HE1  1 
ATOM   12097 H  HE2  . PHE   B  2  202 ? 1.307   -42.986 5.364    1.00 63.46  ? 206  PHE   B HE2  1 
ATOM   12098 H  HZ   . PHE   B  2  202 ? 2.231   -44.887 4.428    1.00 63.43  ? 206  PHE   B HZ   1 
ATOM   12099 N  N    . ASN   B  2  203 ? -3.737  -47.611 6.584    1.00 66.39  ? 207  ASN   B N    1 
ATOM   12100 C  CA   . ASN   B  2  203 ? -4.003  -48.832 5.832    1.00 70.59  ? 207  ASN   B CA   1 
ATOM   12101 C  C    . ASN   B  2  203 ? -5.132  -48.624 4.830    1.00 81.77  ? 207  ASN   B C    1 
ATOM   12102 O  O    . ASN   B  2  203 ? -5.028  -49.027 3.665    1.00 85.44  ? 207  ASN   B O    1 
ATOM   12103 C  CB   . ASN   B  2  203 ? -4.348  -49.979 6.787    1.00 68.93  ? 207  ASN   B CB   1 
ATOM   12104 C  CG   . ASN   B  2  203 ? -3.129  -50.549 7.486    1.00 64.58  ? 207  ASN   B CG   1 
ATOM   12105 O  OD1  . ASN   B  2  203 ? -1.993  -50.209 7.157    1.00 61.58  ? 207  ASN   B OD1  1 
ATOM   12106 N  ND2  . ASN   B  2  203 ? -3.361  -51.437 8.447    1.00 65.75  ? 207  ASN   B ND2  1 
ATOM   12107 H  H    . ASN   B  2  203 ? -3.770  -47.703 7.438    1.00 79.70  ? 207  ASN   B H    1 
ATOM   12108 H  HA   . ASN   B  2  203 ? -3.199  -49.075 5.345    1.00 84.75  ? 207  ASN   B HA   1 
ATOM   12109 H  HB2  . ASN   B  2  203 ? -4.957  -49.651 7.467    1.00 82.75  ? 207  ASN   B HB2  1 
ATOM   12110 H  HB3  . ASN   B  2  203 ? -4.767  -50.694 6.283    1.00 82.75  ? 207  ASN   B HB3  1 
ATOM   12111 H  HD21 . ASN   B  2  203 ? -2.703  -51.790 8.875    1.00 78.94  ? 207  ASN   B HD21 1 
ATOM   12112 H  HD22 . ASN   B  2  203 ? -4.169  -51.658 8.643    1.00 78.94  ? 207  ASN   B HD22 1 
ATOM   12113 N  N    . GLU   B  2  204 ? -6.223  -47.989 5.266    1.00 88.85  ? 208  GLU   B N    1 
ATOM   12114 C  CA   . GLU   B  2  204 ? -7.388  -47.845 4.400    1.00 91.37  ? 208  GLU   B CA   1 
ATOM   12115 C  C    . GLU   B  2  204 ? -7.048  -47.052 3.144    1.00 83.62  ? 208  GLU   B C    1 
ATOM   12116 O  O    . GLU   B  2  204 ? -7.370  -47.471 2.027    1.00 81.16  ? 208  GLU   B O    1 
ATOM   12117 C  CB   . GLU   B  2  204 ? -8.536  -47.170 5.154    1.00 99.35  ? 208  GLU   B CB   1 
ATOM   12118 C  CG   . GLU   B  2  204 ? -9.834  -47.110 4.350    1.00 108.80 ? 208  GLU   B CG   1 
ATOM   12119 C  CD   . GLU   B  2  204 ? -10.872 -46.189 4.959    1.00 123.00 ? 208  GLU   B CD   1 
ATOM   12120 O  OE1  . GLU   B  2  204 ? -11.719 -45.670 4.202    1.00 129.25 ? 208  GLU   B OE1  1 
ATOM   12121 O  OE2  . GLU   B  2  204 ? -10.840 -45.980 6.190    1.00 130.81 ? 208  GLU   B OE2  1 
ATOM   12122 H  H    . GLU   B  2  204 ? -6.310  -47.639 6.047    1.00 106.65 ? 208  GLU   B H    1 
ATOM   12123 H  HA   . GLU   B  2  204 ? -7.679  -48.731 4.135    1.00 109.68 ? 208  GLU   B HA   1 
ATOM   12124 H  HB2  . GLU   B  2  204 ? -8.712  -47.668 5.968    1.00 119.26 ? 208  GLU   B HB2  1 
ATOM   12125 H  HB3  . GLU   B  2  204 ? -8.277  -46.261 5.371    1.00 119.26 ? 208  GLU   B HB3  1 
ATOM   12126 H  HG2  . GLU   B  2  204 ? -9.635  -46.787 3.457    1.00 130.60 ? 208  GLU   B HG2  1 
ATOM   12127 H  HG3  . GLU   B  2  204 ? -10.216 -48.001 4.302    1.00 130.60 ? 208  GLU   B HG3  1 
ATOM   12128 N  N    . ILE   B  2  205 ? -6.403  -45.895 3.306    1.00 81.16  ? 209  ILE   B N    1 
ATOM   12129 C  CA   . ILE   B  2  205 ? -6.201  -45.023 2.155    1.00 77.85  ? 209  ILE   B CA   1 
ATOM   12130 C  C    . ILE   B  2  205 ? -5.205  -45.643 1.183    1.00 74.22  ? 209  ILE   B C    1 
ATOM   12131 O  O    . ILE   B  2  205 ? -5.331  -45.470 -0.034   1.00 74.69  ? 209  ILE   B O    1 
ATOM   12132 C  CB   . ILE   B  2  205 ? -5.766  -43.611 2.599    1.00 73.56  ? 209  ILE   B CB   1 
ATOM   12133 C  CG1  . ILE   B  2  205 ? -4.303  -43.590 3.041    1.00 77.87  ? 209  ILE   B CG1  1 
ATOM   12134 C  CG2  . ILE   B  2  205 ? -6.662  -43.091 3.718    1.00 70.01  ? 209  ILE   B CG2  1 
ATOM   12135 C  CD1  . ILE   B  2  205 ? -3.377  -43.042 1.985    1.00 81.43  ? 209  ILE   B CD1  1 
ATOM   12136 H  H    . ILE   B  2  205 ? -6.082  -45.603 4.049    1.00 97.43  ? 209  ILE   B H    1 
ATOM   12137 H  HA   . ILE   B  2  205 ? -7.050  -44.929 1.695    1.00 93.45  ? 209  ILE   B HA   1 
ATOM   12138 H  HB   . ILE   B  2  205 ? -5.857  -43.028 1.829    1.00 88.31  ? 209  ILE   B HB   1 
ATOM   12139 H  HG12 . ILE   B  2  205 ? -4.221  -43.032 3.830    1.00 93.48  ? 209  ILE   B HG12 1 
ATOM   12140 H  HG13 . ILE   B  2  205 ? -4.023  -44.496 3.245    1.00 93.48  ? 209  ILE   B HG13 1 
ATOM   12141 H  HG21 . ILE   B  2  205 ? -6.379  -42.195 3.958    1.00 84.04  ? 209  ILE   B HG21 1 
ATOM   12142 H  HG22 . ILE   B  2  205 ? -7.580  -43.076 3.406    1.00 84.04  ? 209  ILE   B HG22 1 
ATOM   12143 H  HG23 . ILE   B  2  205 ? -6.582  -43.680 4.485    1.00 84.04  ? 209  ILE   B HG23 1 
ATOM   12144 H  HD11 . ILE   B  2  205 ? -2.465  -43.085 2.312    1.00 97.75  ? 209  ILE   B HD11 1 
ATOM   12145 H  HD12 . ILE   B  2  205 ? -3.466  -43.576 1.180    1.00 97.75  ? 209  ILE   B HD12 1 
ATOM   12146 H  HD13 . ILE   B  2  205 ? -3.619  -42.121 1.800    1.00 97.75  ? 209  ILE   B HD13 1 
ATOM   12147 N  N    . VAL   B  2  206 ? -4.214  -46.383 1.689    1.00 71.57  ? 210  VAL   B N    1 
ATOM   12148 C  CA   . VAL   B  2  206 ? -3.293  -47.095 0.805    1.00 67.35  ? 210  VAL   B CA   1 
ATOM   12149 C  C    . VAL   B  2  206 ? -4.053  -48.131 -0.013   1.00 68.70  ? 210  VAL   B C    1 
ATOM   12150 O  O    . VAL   B  2  206 ? -3.860  -48.255 -1.229   1.00 67.38  ? 210  VAL   B O    1 
ATOM   12151 C  CB   . VAL   B  2  206 ? -2.158  -47.743 1.620    1.00 65.30  ? 210  VAL   B CB   1 
ATOM   12152 C  CG1  . VAL   B  2  206 ? -1.450  -48.824 0.804    1.00 64.21  ? 210  VAL   B CG1  1 
ATOM   12153 C  CG2  . VAL   B  2  206 ? -1.158  -46.690 2.075    1.00 63.74  ? 210  VAL   B CG2  1 
ATOM   12154 H  H    . VAL   B  2  206 ? -4.057  -46.486 2.528    1.00 85.92  ? 210  VAL   B H    1 
ATOM   12155 H  HA   . VAL   B  2  206 ? -2.895  -46.457 0.193    1.00 80.86  ? 210  VAL   B HA   1 
ATOM   12156 H  HB   . VAL   B  2  206 ? -2.545  -48.162 2.405    1.00 78.39  ? 210  VAL   B HB   1 
ATOM   12157 H  HG11 . VAL   B  2  206 ? -0.692  -49.156 1.310    1.00 77.09  ? 210  VAL   B HG11 1 
ATOM   12158 H  HG12 . VAL   B  2  206 ? -2.073  -49.546 0.628    1.00 77.09  ? 210  VAL   B HG12 1 
ATOM   12159 H  HG13 . VAL   B  2  206 ? -1.146  -48.439 -0.033   1.00 77.09  ? 210  VAL   B HG13 1 
ATOM   12160 H  HG21 . VAL   B  2  206 ? -0.459  -47.120 2.593    1.00 76.53  ? 210  VAL   B HG21 1 
ATOM   12161 H  HG22 . VAL   B  2  206 ? -0.774  -46.261 1.294    1.00 76.53  ? 210  VAL   B HG22 1 
ATOM   12162 H  HG23 . VAL   B  2  206 ? -1.617  -46.033 2.621    1.00 76.53  ? 210  VAL   B HG23 1 
ATOM   12163 N  N    . LYS   B  2  207 ? -4.928  -48.894 0.646    1.00 70.53  ? 211  LYS   B N    1 
ATOM   12164 C  CA   . LYS   B  2  207 ? -5.691  -49.923 -0.053   1.00 72.79  ? 211  LYS   B CA   1 
ATOM   12165 C  C    . LYS   B  2  207 ? -6.552  -49.330 -1.162   1.00 73.77  ? 211  LYS   B C    1 
ATOM   12166 O  O    . LYS   B  2  207 ? -6.822  -50.003 -2.163   1.00 76.13  ? 211  LYS   B O    1 
ATOM   12167 C  CB   . LYS   B  2  207 ? -6.567  -50.693 0.939    1.00 75.13  ? 211  LYS   B CB   1 
ATOM   12168 C  CG   . LYS   B  2  207 ? -5.804  -51.609 1.898    1.00 76.82  ? 211  LYS   B CG   1 
ATOM   12169 C  CD   . LYS   B  2  207 ? -6.721  -52.153 2.996    1.00 79.58  ? 211  LYS   B CD   1 
ATOM   12170 C  CE   . LYS   B  2  207 ? -5.952  -52.964 4.036    1.00 82.30  ? 211  LYS   B CE   1 
ATOM   12171 N  NZ   . LYS   B  2  207 ? -6.717  -53.132 5.308    1.00 84.45  ? 211  LYS   B NZ   1 
ATOM   12172 H  H    . LYS   B  2  207 ? -5.096  -48.836 1.488    1.00 84.67  ? 211  LYS   B H    1 
ATOM   12173 H  HA   . LYS   B  2  207 ? -5.069  -50.548 -0.457   1.00 87.38  ? 211  LYS   B HA   1 
ATOM   12174 H  HB2  . LYS   B  2  207 ? -7.057  -50.052 1.478    1.00 90.19  ? 211  LYS   B HB2  1 
ATOM   12175 H  HB3  . LYS   B  2  207 ? -7.185  -51.247 0.438    1.00 90.19  ? 211  LYS   B HB3  1 
ATOM   12176 H  HG2  . LYS   B  2  207 ? -5.440  -52.360 1.404    1.00 92.22  ? 211  LYS   B HG2  1 
ATOM   12177 H  HG3  . LYS   B  2  207 ? -5.087  -51.109 2.318    1.00 92.22  ? 211  LYS   B HG3  1 
ATOM   12178 H  HD2  . LYS   B  2  207 ? -7.151  -51.411 3.449    1.00 95.53  ? 211  LYS   B HD2  1 
ATOM   12179 H  HD3  . LYS   B  2  207 ? -7.390  -52.730 2.596    1.00 95.53  ? 211  LYS   B HD3  1 
ATOM   12180 H  HE2  . LYS   B  2  207 ? -5.767  -53.846 3.677    1.00 98.79  ? 211  LYS   B HE2  1 
ATOM   12181 H  HE3  . LYS   B  2  207 ? -5.121  -52.509 4.242    1.00 98.79  ? 211  LYS   B HE3  1 
ATOM   12182 H  HZ1  . LYS   B  2  207 ? -6.233  -53.595 5.895    1.00 101.37 ? 211  LYS   B HZ1  1 
ATOM   12183 H  HZ2  . LYS   B  2  207 ? -6.908  -52.336 5.656    1.00 101.37 ? 211  LYS   B HZ2  1 
ATOM   12184 H  HZ3  . LYS   B  2  207 ? -7.476  -53.569 5.152    1.00 101.37 ? 211  LYS   B HZ3  1 
ATOM   12185 N  N    . ASN   B  2  208 ? -6.990  -48.081 -1.008   1.00 68.45  ? 212  ASN   B N    1 
ATOM   12186 C  CA   . ASN   B  2  208 ? -7.849  -47.432 -1.988   1.00 71.96  ? 212  ASN   B CA   1 
ATOM   12187 C  C    . ASN   B  2  208 ? -7.074  -46.694 -3.074   1.00 70.82  ? 212  ASN   B C    1 
ATOM   12188 O  O    . ASN   B  2  208 ? -7.698  -46.095 -3.956   1.00 71.20  ? 212  ASN   B O    1 
ATOM   12189 C  CB   . ASN   B  2  208 ? -8.796  -46.446 -1.294   1.00 79.10  ? 212  ASN   B CB   1 
ATOM   12190 C  CG   . ASN   B  2  208 ? -9.776  -47.131 -0.362   1.00 83.22  ? 212  ASN   B CG   1 
ATOM   12191 O  OD1  . ASN   B  2  208 ? -10.107 -48.304 -0.540   1.00 82.44  ? 212  ASN   B OD1  1 
ATOM   12192 N  ND2  . ASN   B  2  208 ? -10.254 -46.397 0.637    1.00 85.24  ? 212  ASN   B ND2  1 
ATOM   12193 H  H    . ASN   B  2  208 ? -6.799  -47.585 -0.332   1.00 82.18  ? 212  ASN   B H    1 
ATOM   12194 H  HA   . ASN   B  2  208 ? -8.384  -48.118 -2.418   1.00 86.39  ? 212  ASN   B HA   1 
ATOM   12195 H  HB2  . ASN   B  2  208 ? -8.272  -45.820 -0.770   1.00 94.96  ? 212  ASN   B HB2  1 
ATOM   12196 H  HB3  . ASN   B  2  208 ? -9.306  -45.969 -1.967   1.00 94.96  ? 212  ASN   B HB3  1 
ATOM   12197 H  HD21 . ASN   B  2  208 ? -10.813 -46.739 1.193    1.00 102.32 ? 212  ASN   B HD21 1 
ATOM   12198 H  HD22 . ASN   B  2  208 ? -10.003 -45.579 0.727    1.00 102.32 ? 212  ASN   B HD22 1 
ATOM   12199 N  N    . GLN   B  2  209 ? -5.745  -46.719 -3.039   1.00 70.74  ? 213  GLN   B N    1 
ATOM   12200 C  CA   . GLN   B  2  209 ? -4.961  -45.969 -4.009   1.00 64.89  ? 213  GLN   B CA   1 
ATOM   12201 C  C    . GLN   B  2  209 ? -4.915  -46.688 -5.352   1.00 63.51  ? 213  GLN   B C    1 
ATOM   12202 O  O    . GLN   B  2  209 ? -4.931  -47.920 -5.429   1.00 62.93  ? 213  GLN   B O    1 
ATOM   12203 C  CB   . GLN   B  2  209 ? -3.534  -45.744 -3.505   1.00 63.39  ? 213  GLN   B CB   1 
ATOM   12204 C  CG   . GLN   B  2  209 ? -3.404  -44.662 -2.447   1.00 64.42  ? 213  GLN   B CG   1 
ATOM   12205 C  CD   . GLN   B  2  209 ? -3.929  -43.318 -2.913   1.00 67.31  ? 213  GLN   B CD   1 
ATOM   12206 O  OE1  . GLN   B  2  209 ? -3.411  -42.729 -3.862   1.00 73.42  ? 213  GLN   B OE1  1 
ATOM   12207 N  NE2  . GLN   B  2  209 ? -4.971  -42.829 -2.249   1.00 65.69  ? 213  GLN   B NE2  1 
ATOM   12208 H  H    . GLN   B  2  209 ? -5.278  -47.160 -2.467   1.00 84.92  ? 213  GLN   B H    1 
ATOM   12209 H  HA   . GLN   B  2  209 ? -5.378  -45.103 -4.140   1.00 77.91  ? 213  GLN   B HA   1 
ATOM   12210 H  HB2  . GLN   B  2  209 ? -3.209  -46.572 -3.119   1.00 76.11  ? 213  GLN   B HB2  1 
ATOM   12211 H  HB3  . GLN   B  2  209 ? -2.978  -45.488 -4.257   1.00 76.11  ? 213  GLN   B HB3  1 
ATOM   12212 H  HG2  . GLN   B  2  209 ? -3.909  -44.925 -1.662   1.00 77.34  ? 213  GLN   B HG2  1 
ATOM   12213 H  HG3  . GLN   B  2  209 ? -2.468  -44.555 -2.218   1.00 77.34  ? 213  GLN   B HG3  1 
ATOM   12214 H  HE21 . GLN   B  2  209 ? -5.310  -43.272 -1.594   1.00 78.86  ? 213  GLN   B HE21 1 
ATOM   12215 H  HE22 . GLN   B  2  209 ? -5.307  -42.070 -2.474   1.00 78.86  ? 213  GLN   B HE22 1 
ATOM   12216 N  N    . LYS   B  2  210 ? -4.854  -45.893 -6.416   1.00 62.45  ? 214  LYS   B N    1 
ATOM   12217 C  CA   . LYS   B  2  210 ? -4.733  -46.389 -7.777   1.00 68.82  ? 214  LYS   B CA   1 
ATOM   12218 C  C    . LYS   B  2  210 ? -3.589  -45.654 -8.462   1.00 65.46  ? 214  LYS   B C    1 
ATOM   12219 O  O    . LYS   B  2  210 ? -3.330  -44.480 -8.184   1.00 64.60  ? 214  LYS   B O    1 
ATOM   12220 C  CB   . LYS   B  2  210 ? -6.041  -46.201 -8.562   1.00 77.57  ? 214  LYS   B CB   1 
ATOM   12221 C  CG   . LYS   B  2  210 ? -7.266  -46.857 -7.917   1.00 86.58  ? 214  LYS   B CG   1 
ATOM   12222 C  CD   . LYS   B  2  210 ? -7.218  -48.381 -8.003   1.00 96.47  ? 214  LYS   B CD   1 
ATOM   12223 C  CE   . LYS   B  2  210 ? -8.480  -49.019 -7.430   1.00 107.08 ? 214  LYS   B CE   1 
ATOM   12224 N  NZ   . LYS   B  2  210 ? -8.636  -50.443 -7.847   1.00 113.20 ? 214  LYS   B NZ   1 
ATOM   12225 H  H    . LYS   B  2  210 ? -4.882  -45.035 -6.371   1.00 74.98  ? 214  LYS   B H    1 
ATOM   12226 H  HA   . LYS   B  2  210 ? -4.528  -47.338 -7.775   1.00 82.62  ? 214  LYS   B HA   1 
ATOM   12227 H  HB2  . LYS   B  2  210 ? -6.223  -45.251 -8.637   1.00 93.13  ? 214  LYS   B HB2  1 
ATOM   12228 H  HB3  . LYS   B  2  210 ? -5.931  -46.589 -9.444   1.00 93.13  ? 214  LYS   B HB3  1 
ATOM   12229 H  HG2  . LYS   B  2  210 ? -7.303  -46.609 -6.980   1.00 103.93 ? 214  LYS   B HG2  1 
ATOM   12230 H  HG3  . LYS   B  2  210 ? -8.066  -46.554 -8.373   1.00 103.93 ? 214  LYS   B HG3  1 
ATOM   12231 H  HD2  . LYS   B  2  210 ? -7.138  -48.647 -8.932   1.00 115.81 ? 214  LYS   B HD2  1 
ATOM   12232 H  HD3  . LYS   B  2  210 ? -6.456  -48.706 -7.498   1.00 115.81 ? 214  LYS   B HD3  1 
ATOM   12233 H  HE2  . LYS   B  2  210 ? -8.438  -48.992 -6.461   1.00 128.53 ? 214  LYS   B HE2  1 
ATOM   12234 H  HE3  . LYS   B  2  210 ? -9.255  -48.527 -7.742   1.00 128.53 ? 214  LYS   B HE3  1 
ATOM   12235 H  HZ1  . LYS   B  2  210 ? -9.389  -50.779 -7.511   1.00 135.87 ? 214  LYS   B HZ1  1 
ATOM   12236 H  HZ2  . LYS   B  2  210 ? -8.667  -50.499 -8.735   1.00 135.87 ? 214  LYS   B HZ2  1 
ATOM   12237 H  HZ3  . LYS   B  2  210 ? -7.948  -50.924 -7.551   1.00 135.87 ? 214  LYS   B HZ3  1 
ATOM   12238 N  N    . ILE   B  2  211 ? -2.903  -46.358 -9.361   1.00 60.80  ? 215  ILE   B N    1 
ATOM   12239 C  CA   . ILE   B  2  211 ? -1.730  -45.794 -10.017  1.00 53.85  ? 215  ILE   B CA   1 
ATOM   12240 C  C    . ILE   B  2  211 ? -2.156  -44.868 -11.152  1.00 47.40  ? 215  ILE   B C    1 
ATOM   12241 O  O    . ILE   B  2  211 ? -3.265  -44.953 -11.685  1.00 47.39  ? 215  ILE   B O    1 
ATOM   12242 C  CB   . ILE   B  2  211 ? -0.800  -46.906 -10.538  1.00 55.53  ? 215  ILE   B CB   1 
ATOM   12243 C  CG1  . ILE   B  2  211 ? -1.579  -47.851 -11.458  1.00 59.35  ? 215  ILE   B CG1  1 
ATOM   12244 C  CG2  . ILE   B  2  211 ? -0.170  -47.663 -9.377   1.00 56.37  ? 215  ILE   B CG2  1 
ATOM   12245 C  CD1  . ILE   B  2  211 ? -0.711  -48.663 -12.386  1.00 62.39  ? 215  ILE   B CD1  1 
ATOM   12246 H  H    . ILE   B  2  211 ? -3.095  -47.160 -9.605   1.00 73.00  ? 215  ILE   B H    1 
ATOM   12247 H  HA   . ILE   B  2  211 ? -1.241  -45.264 -9.368   1.00 64.65  ? 215  ILE   B HA   1 
ATOM   12248 H  HB   . ILE   B  2  211 ? -0.085  -46.500 -11.051  1.00 66.68  ? 215  ILE   B HB   1 
ATOM   12249 H  HG12 . ILE   B  2  211 ? -2.085  -48.471 -10.910  1.00 71.26  ? 215  ILE   B HG12 1 
ATOM   12250 H  HG13 . ILE   B  2  211 ? -2.183  -47.324 -12.005  1.00 71.26  ? 215  ILE   B HG13 1 
ATOM   12251 H  HG21 . ILE   B  2  211 ? 0.416   -48.351 -9.730   1.00 67.68  ? 215  ILE   B HG21 1 
ATOM   12252 H  HG22 . ILE   B  2  211 ? 0.341   -47.042 -8.834   1.00 67.68  ? 215  ILE   B HG22 1 
ATOM   12253 H  HG23 . ILE   B  2  211 ? -0.872  -48.067 -8.845   1.00 67.68  ? 215  ILE   B HG23 1 
ATOM   12254 H  HD11 . ILE   B  2  211 ? -1.277  -49.241 -12.922  1.00 74.90  ? 215  ILE   B HD11 1 
ATOM   12255 H  HD12 . ILE   B  2  211 ? -0.215  -48.061 -12.961  1.00 74.90  ? 215  ILE   B HD12 1 
ATOM   12256 H  HD13 . ILE   B  2  211 ? -0.098  -49.197 -11.858  1.00 74.90  ? 215  ILE   B HD13 1 
ATOM   12257 N  N    . SER   B  2  212 ? -1.249  -43.973 -11.525  1.00 44.62  ? 216  SER   B N    1 
ATOM   12258 C  CA   . SER   B  2  212 ? -1.346  -43.192 -12.749  1.00 45.51  ? 216  SER   B CA   1 
ATOM   12259 C  C    . SER   B  2  212 ? -0.139  -43.528 -13.624  1.00 45.99  ? 216  SER   B C    1 
ATOM   12260 O  O    . SER   B  2  212 ? 0.573   -44.507 -13.383  1.00 43.75  ? 216  SER   B O    1 
ATOM   12261 C  CB   . SER   B  2  212 ? -1.427  -41.698 -12.440  1.00 51.71  ? 216  SER   B CB   1 
ATOM   12262 O  OG   . SER   B  2  212 ? -1.543  -40.945 -13.634  1.00 57.62  ? 216  SER   B OG   1 
ATOM   12263 H  H    . SER   B  2  212 ? -0.542  -43.796 -11.068  1.00 53.58  ? 216  SER   B H    1 
ATOM   12264 H  HA   . SER   B  2  212 ? -2.159  -43.434 -13.219  1.00 54.65  ? 216  SER   B HA   1 
ATOM   12265 H  HB2  . SER   B  2  212 ? -2.204  -41.532 -11.884  1.00 62.08  ? 216  SER   B HB2  1 
ATOM   12266 H  HB3  . SER   B  2  212 ? -0.621  -41.428 -11.972  1.00 62.08  ? 216  SER   B HB3  1 
ATOM   12267 H  HG   . SER   B  2  212 ? -2.325  -41.003 -13.936  1.00 69.18  ? 216  SER   B HG   1 
ATOM   12268 N  N    . ALA   B  2  213 ? 0.098   -42.710 -14.645  1.00 49.07  ? 217  ALA   B N    1 
ATOM   12269 C  CA   . ALA   B  2  213 ? 1.235   -42.946 -15.523  1.00 48.04  ? 217  ALA   B CA   1 
ATOM   12270 C  C    . ALA   B  2  213 ? 1.613   -41.658 -16.239  1.00 44.15  ? 217  ALA   B C    1 
ATOM   12271 O  O    . ALA   B  2  213 ? 0.932   -40.634 -16.141  1.00 44.81  ? 217  ALA   B O    1 
ATOM   12272 C  CB   . ALA   B  2  213 ? 0.936   -44.058 -16.535  1.00 45.72  ? 217  ALA   B CB   1 
ATOM   12273 H  H    . ALA   B  2  213 ? -0.378  -42.022 -14.845  1.00 58.93  ? 217  ALA   B H    1 
ATOM   12274 H  HA   . ALA   B  2  213 ? 1.990   -43.209 -14.974  1.00 57.69  ? 217  ALA   B HA   1 
ATOM   12275 H  HB1  . ALA   B  2  213 ? 1.724   -44.208 -17.080  1.00 54.90  ? 217  ALA   B HB1  1 
ATOM   12276 H  HB2  . ALA   B  2  213 ? 0.707   -44.869 -16.054  1.00 54.90  ? 217  ALA   B HB2  1 
ATOM   12277 H  HB3  . ALA   B  2  213 ? 0.193   -43.784 -17.095  1.00 54.90  ? 217  ALA   B HB3  1 
ATOM   12278 N  N    . ASN   B  2  214 ? 2.724   -41.738 -16.959  1.00 43.55  ? 218  ASN   B N    1 
ATOM   12279 C  CA   . ASN   B  2  214 ? 3.291   -40.664 -17.769  1.00 45.66  ? 218  ASN   B CA   1 
ATOM   12280 C  C    . ASN   B  2  214 ? 4.372   -41.331 -18.616  1.00 49.14  ? 218  ASN   B C    1 
ATOM   12281 O  O    . ASN   B  2  214 ? 4.616   -42.535 -18.486  1.00 51.45  ? 218  ASN   B O    1 
ATOM   12282 C  CB   . ASN   B  2  214 ? 3.813   -39.519 -16.901  1.00 47.76  ? 218  ASN   B CB   1 
ATOM   12283 C  CG   . ASN   B  2  214 ? 5.118   -39.850 -16.211  1.00 49.58  ? 218  ASN   B CG   1 
ATOM   12284 O  OD1  . ASN   B  2  214 ? 6.083   -39.096 -16.306  1.00 51.23  ? 218  ASN   B OD1  1 
ATOM   12285 N  ND2  . ASN   B  2  214 ? 5.155   -40.978 -15.510  1.00 51.63  ? 218  ASN   B ND2  1 
ATOM   12286 H  H    . ASN   B  2  214 ? 3.201   -42.453 -16.999  1.00 52.30  ? 218  ASN   B H    1 
ATOM   12287 H  HA   . ASN   B  2  214 ? 2.627   -40.272 -18.358  1.00 54.83  ? 218  ASN   B HA   1 
ATOM   12288 H  HB2  . ASN   B  2  214 ? 3.960   -38.740 -17.461  1.00 57.34  ? 218  ASN   B HB2  1 
ATOM   12289 H  HB3  . ASN   B  2  214 ? 3.156   -39.316 -16.217  1.00 57.34  ? 218  ASN   B HB3  1 
ATOM   12290 H  HD21 . ASN   B  2  214 ? 5.876   -41.207 -15.100  1.00 62.00  ? 218  ASN   B HD21 1 
ATOM   12291 H  HD22 . ASN   B  2  214 ? 4.458   -41.480 -15.465  1.00 62.00  ? 218  ASN   B HD22 1 
ATOM   12292 N  N    . ILE   B  2  215 ? 5.019   -40.560 -19.489  1.00 53.90  ? 219  ILE   B N    1 
ATOM   12293 C  CA   . ILE   B  2  215 ? 5.795   -41.160 -20.569  1.00 61.75  ? 219  ILE   B CA   1 
ATOM   12294 C  C    . ILE   B  2  215 ? 7.308   -40.998 -20.432  1.00 58.77  ? 219  ILE   B C    1 
ATOM   12295 O  O    . ILE   B  2  215 ? 8.045   -41.712 -21.130  1.00 63.40  ? 219  ILE   B O    1 
ATOM   12296 C  CB   . ILE   B  2  215 ? 5.335   -40.631 -21.944  1.00 72.38  ? 219  ILE   B CB   1 
ATOM   12297 C  CG1  . ILE   B  2  215 ? 5.458   -39.110 -22.015  1.00 79.56  ? 219  ILE   B CG1  1 
ATOM   12298 C  CG2  . ILE   B  2  215 ? 3.905   -41.069 -22.221  1.00 78.06  ? 219  ILE   B CG2  1 
ATOM   12299 C  CD1  . ILE   B  2  215 ? 5.197   -38.553 -23.397  1.00 86.25  ? 219  ILE   B CD1  1 
ATOM   12300 H  H    . ILE   B  2  215 ? 5.024   -39.701 -19.475  1.00 64.72  ? 219  ILE   B H    1 
ATOM   12301 H  HA   . ILE   B  2  215 ? 5.628   -42.115 -20.535  1.00 74.14  ? 219  ILE   B HA   1 
ATOM   12302 H  HB   . ILE   B  2  215 ? 5.915   -41.007 -22.625  1.00 86.90  ? 219  ILE   B HB   1 
ATOM   12303 H  HG12 . ILE   B  2  215 ? 4.814   -38.714 -21.408  1.00 95.50  ? 219  ILE   B HG12 1 
ATOM   12304 H  HG13 . ILE   B  2  215 ? 6.358   -38.856 -21.757  1.00 95.50  ? 219  ILE   B HG13 1 
ATOM   12305 H  HG21 . ILE   B  2  215 ? 3.674   -40.834 -23.133  1.00 93.70  ? 219  ILE   B HG21 1 
ATOM   12306 H  HG22 . ILE   B  2  215 ? 3.841   -42.029 -22.100  1.00 93.70  ? 219  ILE   B HG22 1 
ATOM   12307 H  HG23 . ILE   B  2  215 ? 3.311   -40.617 -21.601  1.00 93.70  ? 219  ILE   B HG23 1 
ATOM   12308 H  HD11 . ILE   B  2  215 ? 5.330   -37.593 -23.381  1.00 103.54 ? 219  ILE   B HD11 1 
ATOM   12309 H  HD12 . ILE   B  2  215 ? 5.814   -38.962 -24.024  1.00 103.54 ? 219  ILE   B HD12 1 
ATOM   12310 H  HD13 . ILE   B  2  215 ? 4.283   -38.757 -23.652  1.00 103.54 ? 219  ILE   B HD13 1 
ATOM   12311 N  N    . ASP   B  2  216 ? 7.802   -40.107 -19.578  1.00 46.39  ? 220  ASP   B N    1 
ATOM   12312 C  CA   . ASP   B  2  216 ? 9.241   -39.928 -19.421  1.00 46.25  ? 220  ASP   B CA   1 
ATOM   12313 C  C    . ASP   B  2  216 ? 9.685   -40.413 -18.046  1.00 44.90  ? 220  ASP   B C    1 
ATOM   12314 O  O    . ASP   B  2  216 ? 8.964   -40.254 -17.053  1.00 42.70  ? 220  ASP   B O    1 
ATOM   12315 C  CB   . ASP   B  2  216 ? 9.656   -38.467 -19.637  1.00 46.24  ? 220  ASP   B CB   1 
ATOM   12316 C  CG   . ASP   B  2  216 ? 9.326   -37.582 -18.459  1.00 48.18  ? 220  ASP   B CG   1 
ATOM   12317 O  OD1  . ASP   B  2  216 ? 8.336   -37.870 -17.757  1.00 50.36  ? 220  ASP   B OD1  1 
ATOM   12318 O  OD2  . ASP   B  2  216 ? 10.059  -36.594 -18.240  1.00 46.08  ? 220  ASP   B OD2  1 
ATOM   12319 H  H    . ASP   B  2  216 ? 7.324   -39.594 -19.080  1.00 55.71  ? 220  ASP   B H    1 
ATOM   12320 H  HA   . ASP   B  2  216 ? 9.702   -40.463 -20.086  1.00 55.53  ? 220  ASP   B HA   1 
ATOM   12321 H  HB2  . ASP   B  2  216 ? 10.614  -38.429 -19.781  1.00 55.53  ? 220  ASP   B HB2  1 
ATOM   12322 H  HB3  . ASP   B  2  216 ? 9.190   -38.119 -20.413  1.00 55.53  ? 220  ASP   B HB3  1 
ATOM   12323 N  N    . THR   B  2  217 ? 10.884  -41.000 -18.001  1.00 48.05  ? 221  THR   B N    1 
ATOM   12324 C  CA   . THR   B  2  217 ? 11.321  -41.726 -16.810  1.00 48.45  ? 221  THR   B CA   1 
ATOM   12325 C  C    . THR   B  2  217 ? 11.420  -40.841 -15.577  1.00 47.50  ? 221  THR   B C    1 
ATOM   12326 O  O    . THR   B  2  217 ? 10.836  -41.201 -14.540  1.00 48.60  ? 221  THR   B O    1 
ATOM   12327 C  CB   . THR   B  2  217 ? 12.658  -42.421 -17.099  1.00 47.97  ? 221  THR   B CB   1 
ATOM   12328 O  OG1  . THR   B  2  217 ? 12.460  -43.469 -18.058  1.00 47.92  ? 221  THR   B OG1  1 
ATOM   12329 C  CG2  . THR   B  2  217 ? 13.255  -43.009 -15.824  1.00 51.87  ? 221  THR   B CG2  1 
ATOM   12330 H  H    . THR   B  2  217 ? 11.458  -40.992 -18.642  1.00 57.69  ? 221  THR   B H    1 
ATOM   12331 H  HA   . THR   B  2  217 ? 10.653  -42.405 -16.626  1.00 58.18  ? 221  THR   B HA   1 
ATOM   12332 H  HB   . THR   B  2  217 ? 13.285  -41.771 -17.452  1.00 57.60  ? 221  THR   B HB   1 
ATOM   12333 H  HG1  . THR   B  2  217 ? 13.185  -43.867 -18.202  1.00 57.54  ? 221  THR   B HG1  1 
ATOM   12334 H  HG21 . THR   B  2  217 ? 14.064  -43.502 -16.033  1.00 62.28  ? 221  THR   B HG21 1 
ATOM   12335 H  HG22 . THR   B  2  217 ? 13.471  -42.298 -15.200  1.00 62.28  ? 221  THR   B HG22 1 
ATOM   12336 H  HG23 . THR   B  2  217 ? 12.619  -43.611 -15.407  1.00 62.28  ? 221  THR   B HG23 1 
ATOM   12337 N  N    . PRO   B  2  218 ? 12.130  -39.714 -15.594  1.00 46.20  ? 222  PRO   B N    1 
ATOM   12338 C  CA   . PRO   B  2  218 ? 12.227  -38.903 -14.374  1.00 51.25  ? 222  PRO   B CA   1 
ATOM   12339 C  C    . PRO   B  2  218 ? 10.858  -38.382 -13.966  1.00 53.75  ? 222  PRO   B C    1 
ATOM   12340 O  O    . PRO   B  2  218 ? 10.043  -37.999 -14.807  1.00 72.06  ? 222  PRO   B O    1 
ATOM   12341 C  CB   . PRO   B  2  218 ? 13.177  -37.764 -14.771  1.00 48.02  ? 222  PRO   B CB   1 
ATOM   12342 C  CG   . PRO   B  2  218 ? 13.831  -38.211 -16.045  1.00 44.76  ? 222  PRO   B CG   1 
ATOM   12343 C  CD   . PRO   B  2  218 ? 12.832  -39.083 -16.724  1.00 45.01  ? 222  PRO   B CD   1 
ATOM   12344 H  HA   . PRO   B  2  218 ? 12.621  -39.409 -13.647  1.00 61.53  ? 222  PRO   B HA   1 
ATOM   12345 H  HB2  . PRO   B  2  218 ? 12.671  -36.949 -14.910  1.00 57.67  ? 222  PRO   B HB2  1 
ATOM   12346 H  HB3  . PRO   B  2  218 ? 13.837  -37.630 -14.073  1.00 57.67  ? 222  PRO   B HB3  1 
ATOM   12347 H  HG2  . PRO   B  2  218 ? 14.044  -37.439 -16.593  1.00 53.74  ? 222  PRO   B HG2  1 
ATOM   12348 H  HG3  . PRO   B  2  218 ? 14.640  -38.706 -15.842  1.00 53.74  ? 222  PRO   B HG3  1 
ATOM   12349 H  HD2  . PRO   B  2  218 ? 12.220  -38.557 -17.262  1.00 54.04  ? 222  PRO   B HD2  1 
ATOM   12350 H  HD3  . PRO   B  2  218 ? 13.270  -39.749 -17.276  1.00 54.04  ? 222  PRO   B HD3  1 
ATOM   12351 N  N    . GLU   B  2  219 ? 10.611  -38.372 -12.662  1.00 49.94  ? 223  GLU   B N    1 
ATOM   12352 C  CA   . GLU   B  2  219 ? 9.315   -38.012 -12.108  1.00 50.23  ? 223  GLU   B CA   1 
ATOM   12353 C  C    . GLU   B  2  219 ? 9.418   -36.692 -11.353  1.00 47.17  ? 223  GLU   B C    1 
ATOM   12354 O  O    . GLU   B  2  219 ? 10.502  -36.128 -11.177  1.00 41.43  ? 223  GLU   B O    1 
ATOM   12355 C  CB   . GLU   B  2  219 ? 8.794   -39.128 -11.194  1.00 54.27  ? 223  GLU   B CB   1 
ATOM   12356 C  CG   . GLU   B  2  219 ? 8.900   -40.534 -11.790  1.00 59.79  ? 223  GLU   B CG   1 
ATOM   12357 C  CD   . GLU   B  2  219 ? 7.963   -40.764 -12.965  1.00 61.70  ? 223  GLU   B CD   1 
ATOM   12358 O  OE1  . GLU   B  2  219 ? 7.563   -39.781 -13.623  1.00 61.58  ? 223  GLU   B OE1  1 
ATOM   12359 O  OE2  . GLU   B  2  219 ? 7.623   -41.936 -13.229  1.00 70.31  ? 223  GLU   B OE2  1 
ATOM   12360 H  H    . GLU   B  2  219 ? 11.194  -38.577 -12.064  1.00 59.96  ? 223  GLU   B H    1 
ATOM   12361 H  HA   . GLU   B  2  219 ? 8.675   -37.893 -12.828  1.00 60.32  ? 223  GLU   B HA   1 
ATOM   12362 H  HB2  . GLU   B  2  219 ? 9.308   -39.118 -10.371  1.00 65.16  ? 223  GLU   B HB2  1 
ATOM   12363 H  HB3  . GLU   B  2  219 ? 7.858   -38.960 -11.003  1.00 65.16  ? 223  GLU   B HB3  1 
ATOM   12364 H  HG2  . GLU   B  2  219 ? 9.808   -40.675 -12.102  1.00 71.79  ? 223  GLU   B HG2  1 
ATOM   12365 H  HG3  . GLU   B  2  219 ? 8.681   -41.183 -11.104  1.00 71.79  ? 223  GLU   B HG3  1 
ATOM   12366 N  N    . GLY   B  2  220 ? 8.264   -36.202 -10.903  1.00 45.06  ? 224  GLY   B N    1 
ATOM   12367 C  CA   . GLY   B  2  220 ? 8.188   -34.893 -10.283  1.00 41.00  ? 224  GLY   B CA   1 
ATOM   12368 C  C    . GLY   B  2  220 ? 8.149   -34.940 -8.771   1.00 41.67  ? 224  GLY   B C    1 
ATOM   12369 O  O    . GLY   B  2  220 ? 7.465   -34.132 -8.134   1.00 42.67  ? 224  GLY   B O    1 
ATOM   12370 H  H    . GLY   B  2  220 ? 7.510   -36.614 -10.947  1.00 54.11  ? 224  GLY   B H    1 
ATOM   12371 H  HA2  . GLY   B  2  220 ? 8.963   -34.373 -10.548  1.00 49.24  ? 224  GLY   B HA2  1 
ATOM   12372 H  HA3  . GLY   B  2  220 ? 7.386   -34.444 -10.591  1.00 49.24  ? 224  GLY   B HA3  1 
ATOM   12373 N  N    . GLY   B  2  221 ? 8.885   -35.884 -8.183   1.00 43.31  ? 225  GLY   B N    1 
ATOM   12374 C  CA   . GLY   B  2  221 ? 8.905   -35.994 -6.735   1.00 46.27  ? 225  GLY   B CA   1 
ATOM   12375 C  C    . GLY   B  2  221 ? 9.377   -34.725 -6.050   1.00 46.68  ? 225  GLY   B C    1 
ATOM   12376 O  O    . GLY   B  2  221 ? 8.891   -34.373 -4.973   1.00 45.29  ? 225  GLY   B O    1 
ATOM   12377 H  H    . GLY   B  2  221 ? 9.371   -36.460 -8.596   1.00 52.01  ? 225  GLY   B H    1 
ATOM   12378 H  HA2  . GLY   B  2  221 ? 8.010   -36.194 -6.418   1.00 55.56  ? 225  GLY   B HA2  1 
ATOM   12379 H  HA3  . GLY   B  2  221 ? 9.500   -36.716 -6.478   1.00 55.56  ? 225  GLY   B HA3  1 
ATOM   12380 N  N    . PHE   B  2  222 ? 10.331  -34.019 -6.663   1.00 43.74  ? 226  PHE   B N    1 
ATOM   12381 C  CA   . PHE   B  2  222 ? 10.859  -32.808 -6.041   1.00 43.80  ? 226  PHE   B CA   1 
ATOM   12382 C  C    . PHE   B  2  222 ? 9.751   -31.795 -5.783   1.00 44.96  ? 226  PHE   B C    1 
ATOM   12383 O  O    . PHE   B  2  222 ? 9.766   -31.094 -4.764   1.00 46.49  ? 226  PHE   B O    1 
ATOM   12384 C  CB   . PHE   B  2  222 ? 11.953  -32.194 -6.915   1.00 45.71  ? 226  PHE   B CB   1 
ATOM   12385 C  CG   . PHE   B  2  222 ? 13.296  -32.861 -6.775   1.00 43.14  ? 226  PHE   B CG   1 
ATOM   12386 C  CD1  . PHE   B  2  222 ? 13.408  -34.142 -6.260   1.00 41.90  ? 226  PHE   B CD1  1 
ATOM   12387 C  CD2  . PHE   B  2  222 ? 14.450  -32.194 -7.150   1.00 44.82  ? 226  PHE   B CD2  1 
ATOM   12388 C  CE1  . PHE   B  2  222 ? 14.643  -34.747 -6.131   1.00 45.10  ? 226  PHE   B CE1  1 
ATOM   12389 C  CE2  . PHE   B  2  222 ? 15.687  -32.792 -7.021   1.00 42.73  ? 226  PHE   B CE2  1 
ATOM   12390 C  CZ   . PHE   B  2  222 ? 15.784  -34.071 -6.511   1.00 42.44  ? 226  PHE   B CZ   1 
ATOM   12391 H  H    . PHE   B  2  222 ? 10.681  -34.216 -7.424   1.00 52.52  ? 226  PHE   B H    1 
ATOM   12392 H  HA   . PHE   B  2  222 ? 11.258  -33.046 -5.189   1.00 52.59  ? 226  PHE   B HA   1 
ATOM   12393 H  HB2  . PHE   B  2  222 ? 11.685  -32.264 -7.844   1.00 54.88  ? 226  PHE   B HB2  1 
ATOM   12394 H  HB3  . PHE   B  2  222 ? 12.060  -31.262 -6.669   1.00 54.88  ? 226  PHE   B HB3  1 
ATOM   12395 H  HD1  . PHE   B  2  222 ? 12.643  -34.601 -5.998   1.00 50.32  ? 226  PHE   B HD1  1 
ATOM   12396 H  HD2  . PHE   B  2  222 ? 14.391  -31.331 -7.492   1.00 53.82  ? 226  PHE   B HD2  1 
ATOM   12397 H  HE1  . PHE   B  2  222 ? 14.706  -35.609 -5.789   1.00 54.16  ? 226  PHE   B HE1  1 
ATOM   12398 H  HE2  . PHE   B  2  222 ? 16.455  -32.335 -7.279   1.00 51.31  ? 226  PHE   B HE2  1 
ATOM   12399 H  HZ   . PHE   B  2  222 ? 16.617  -34.475 -6.424   1.00 50.96  ? 226  PHE   B HZ   1 
ATOM   12400 N  N    . ASP   B  2  223 ? 8.781   -31.699 -6.695   1.00 47.70  ? 227  ASP   B N    1 
ATOM   12401 C  CA   . ASP   B  2  223 ? 7.617   -30.858 -6.436   1.00 47.06  ? 227  ASP   B CA   1 
ATOM   12402 C  C    . ASP   B  2  223 ? 6.903   -31.297 -5.165   1.00 47.39  ? 227  ASP   B C    1 
ATOM   12403 O  O    . ASP   B  2  223 ? 6.485   -30.461 -4.355   1.00 47.15  ? 227  ASP   B O    1 
ATOM   12404 C  CB   . ASP   B  2  223 ? 6.657   -30.899 -7.626   1.00 48.02  ? 227  ASP   B CB   1 
ATOM   12405 C  CG   . ASP   B  2  223 ? 6.943   -29.818 -8.654   1.00 47.59  ? 227  ASP   B CG   1 
ATOM   12406 O  OD1  . ASP   B  2  223 ? 7.870   -29.010 -8.438   1.00 50.08  ? 227  ASP   B OD1  1 
ATOM   12407 O  OD2  . ASP   B  2  223 ? 6.234   -29.774 -9.680   1.00 47.28  ? 227  ASP   B OD2  1 
ATOM   12408 H  H    . ASP   B  2  223 ? 8.774   -32.102 -7.454   1.00 57.28  ? 227  ASP   B H    1 
ATOM   12409 H  HA   . ASP   B  2  223 ? 7.914   -29.941 -6.323   1.00 56.51  ? 227  ASP   B HA   1 
ATOM   12410 H  HB2  . ASP   B  2  223 ? 6.736   -31.760 -8.066   1.00 57.66  ? 227  ASP   B HB2  1 
ATOM   12411 H  HB3  . ASP   B  2  223 ? 5.750   -30.774 -7.304   1.00 57.66  ? 227  ASP   B HB3  1 
ATOM   12412 N  N    . ALA   B  2  224 ? 6.760   -32.610 -4.969   1.00 49.07  ? 228  ALA   B N    1 
ATOM   12413 C  CA   . ALA   B  2  224 ? 6.059   -33.110 -3.792   1.00 48.14  ? 228  ALA   B CA   1 
ATOM   12414 C  C    . ALA   B  2  224 ? 6.890   -32.924 -2.527   1.00 45.66  ? 228  ALA   B C    1 
ATOM   12415 O  O    . ALA   B  2  224 ? 6.347   -32.592 -1.467   1.00 41.41  ? 228  ALA   B O    1 
ATOM   12416 C  CB   . ALA   B  2  224 ? 5.702   -34.583 -3.986   1.00 47.29  ? 228  ALA   B CB   1 
ATOM   12417 H  H    . ALA   B  2  224 ? 7.056   -33.221 -5.496   1.00 58.92  ? 228  ALA   B H    1 
ATOM   12418 H  HA   . ALA   B  2  224 ? 5.235   -32.610 -3.683   1.00 57.81  ? 228  ALA   B HA   1 
ATOM   12419 H  HB1  . ALA   B  2  224 ? 5.220   -34.897 -3.205   1.00 56.79  ? 228  ALA   B HB1  1 
ATOM   12420 H  HB2  . ALA   B  2  224 ? 5.146   -34.672 -4.776   1.00 56.79  ? 228  ALA   B HB2  1 
ATOM   12421 H  HB3  . ALA   B  2  224 ? 6.519   -35.094 -4.098   1.00 56.79  ? 228  ALA   B HB3  1 
ATOM   12422 N  N    . ILE   B  2  225 ? 8.206   -33.137 -2.615   1.00 43.86  ? 229  ILE   B N    1 
ATOM   12423 C  CA   . ILE   B  2  225 ? 9.069   -32.935 -1.452   1.00 42.01  ? 229  ILE   B CA   1 
ATOM   12424 C  C    . ILE   B  2  225 ? 8.925   -31.511 -0.933   1.00 43.63  ? 229  ILE   B C    1 
ATOM   12425 O  O    . ILE   B  2  225 ? 8.721   -31.283 0.265    1.00 46.42  ? 229  ILE   B O    1 
ATOM   12426 C  CB   . ILE   B  2  225 ? 10.533  -33.259 -1.803   1.00 42.95  ? 229  ILE   B CB   1 
ATOM   12427 C  CG1  . ILE   B  2  225 ? 10.708  -34.765 -2.023   1.00 45.79  ? 229  ILE   B CG1  1 
ATOM   12428 C  CG2  . ILE   B  2  225 ? 11.475  -32.757 -0.703   1.00 40.59  ? 229  ILE   B CG2  1 
ATOM   12429 C  CD1  . ILE   B  2  225 ? 12.111  -35.171 -2.454   1.00 45.20  ? 229  ILE   B CD1  1 
ATOM   12430 H  H    . ILE   B  2  225 ? 8.617   -33.395 -3.325   1.00 52.67  ? 229  ILE   B H    1 
ATOM   12431 H  HA   . ILE   B  2  225 ? 8.788   -33.544 -0.751   1.00 50.45  ? 229  ILE   B HA   1 
ATOM   12432 H  HB   . ILE   B  2  225 ? 10.759  -32.801 -2.628   1.00 51.58  ? 229  ILE   B HB   1 
ATOM   12433 H  HG12 . ILE   B  2  225 ? 10.510  -35.225 -1.193   1.00 54.98  ? 229  ILE   B HG12 1 
ATOM   12434 H  HG13 . ILE   B  2  225 ? 10.092  -35.051 -2.716   1.00 54.98  ? 229  ILE   B HG13 1 
ATOM   12435 H  HG21 . ILE   B  2  225 ? 12.387  -32.995 -0.934   1.00 48.75  ? 229  ILE   B HG21 1 
ATOM   12436 H  HG22 . ILE   B  2  225 ? 11.393  -31.793 -0.632   1.00 48.75  ? 229  ILE   B HG22 1 
ATOM   12437 H  HG23 . ILE   B  2  225 ? 11.229  -33.173 0.138    1.00 48.75  ? 229  ILE   B HG23 1 
ATOM   12438 H  HD11 . ILE   B  2  225 ? 12.135  -36.132 -2.585   1.00 54.28  ? 229  ILE   B HD11 1 
ATOM   12439 H  HD12 . ILE   B  2  225 ? 12.330  -34.719 -3.284   1.00 54.28  ? 229  ILE   B HD12 1 
ATOM   12440 H  HD13 . ILE   B  2  225 ? 12.740  -34.916 -1.762   1.00 54.28  ? 229  ILE   B HD13 1 
ATOM   12441 N  N    . MET   B  2  226 ? 9.043   -30.531 -1.831   1.00 45.89  ? 230  MET   B N    1 
ATOM   12442 C  CA   . MET   B  2  226 ? 8.925   -29.133 -1.431   1.00 46.65  ? 230  MET   B CA   1 
ATOM   12443 C  C    . MET   B  2  226 ? 7.626   -28.889 -0.674   1.00 47.67  ? 230  MET   B C    1 
ATOM   12444 O  O    . MET   B  2  226 ? 7.624   -28.298 0.412    1.00 50.40  ? 230  MET   B O    1 
ATOM   12445 C  CB   . MET   B  2  226 ? 9.002   -28.234 -2.667   1.00 42.00  ? 230  MET   B CB   1 
ATOM   12446 C  CG   . MET   B  2  226 ? 8.721   -26.766 -2.388   1.00 45.14  ? 230  MET   B CG   1 
ATOM   12447 S  SD   . MET   B  2  226 ? 10.007  -26.010 -1.382   1.00 51.66  ? 230  MET   B SD   1 
ATOM   12448 C  CE   . MET   B  2  226 ? 11.323  -25.890 -2.590   1.00 50.84  ? 230  MET   B CE   1 
ATOM   12449 H  H    . MET   B  2  226 ? 9.191   -30.649 -2.670   1.00 55.11  ? 230  MET   B H    1 
ATOM   12450 H  HA   . MET   B  2  226 ? 9.671   -28.911 -0.852   1.00 56.02  ? 230  MET   B HA   1 
ATOM   12451 H  HB2  . MET   B  2  226 ? 9.895   -28.297 -3.041   1.00 50.44  ? 230  MET   B HB2  1 
ATOM   12452 H  HB3  . MET   B  2  226 ? 8.348   -28.541 -3.315   1.00 50.44  ? 230  MET   B HB3  1 
ATOM   12453 H  HG2  . MET   B  2  226 ? 8.673   -26.286 -3.229   1.00 54.20  ? 230  MET   B HG2  1 
ATOM   12454 H  HG3  . MET   B  2  226 ? 7.880   -26.688 -1.912   1.00 54.20  ? 230  MET   B HG3  1 
ATOM   12455 H  HE1  . MET   B  2  226 ? 12.089  -25.459 -2.181   1.00 61.04  ? 230  MET   B HE1  1 
ATOM   12456 H  HE2  . MET   B  2  226 ? 11.563  -26.782 -2.885   1.00 61.04  ? 230  MET   B HE2  1 
ATOM   12457 H  HE3  . MET   B  2  226 ? 11.012  -25.365 -3.344   1.00 61.04  ? 230  MET   B HE3  1 
ATOM   12458 N  N    . GLN   B  2  227 ? 6.504   -29.336 -1.242   1.00 43.50  ? 231  GLN   B N    1 
ATOM   12459 C  CA   . GLN   B  2  227 ? 5.211   -29.095 -0.612   1.00 45.24  ? 231  GLN   B CA   1 
ATOM   12460 C  C    . GLN   B  2  227 ? 5.127   -29.759 0.756    1.00 46.86  ? 231  GLN   B C    1 
ATOM   12461 O  O    . GLN   B  2  227 ? 4.652   -29.150 1.721    1.00 44.31  ? 231  GLN   B O    1 
ATOM   12462 C  CB   . GLN   B  2  227 ? 4.088   -29.594 -1.520   1.00 45.17  ? 231  GLN   B CB   1 
ATOM   12463 C  CG   . GLN   B  2  227 ? 3.885   -28.746 -2.761   1.00 45.54  ? 231  GLN   B CG   1 
ATOM   12464 C  CD   . GLN   B  2  227 ? 3.514   -27.315 -2.426   1.00 46.33  ? 231  GLN   B CD   1 
ATOM   12465 O  OE1  . GLN   B  2  227 ? 2.429   -27.048 -1.909   1.00 49.71  ? 231  GLN   B OE1  1 
ATOM   12466 N  NE2  . GLN   B  2  227 ? 4.421   -26.388 -2.706   1.00 45.21  ? 231  GLN   B NE2  1 
ATOM   12467 H  H    . GLN   B  2  227 ? 6.467   -29.775 -1.981   1.00 52.23  ? 231  GLN   B H    1 
ATOM   12468 H  HA   . GLN   B  2  227 ? 5.098   -28.139 -0.488   1.00 54.32  ? 231  GLN   B HA   1 
ATOM   12469 H  HB2  . GLN   B  2  227 ? 4.298   -30.496 -1.808   1.00 54.24  ? 231  GLN   B HB2  1 
ATOM   12470 H  HB3  . GLN   B  2  227 ? 3.257   -29.591 -1.019   1.00 54.24  ? 231  GLN   B HB3  1 
ATOM   12471 H  HG2  . GLN   B  2  227 ? 4.708   -28.732 -3.275   1.00 54.68  ? 231  GLN   B HG2  1 
ATOM   12472 H  HG3  . GLN   B  2  227 ? 3.168   -29.127 -3.293   1.00 54.68  ? 231  GLN   B HG3  1 
ATOM   12473 H  HE21 . GLN   B  2  227 ? 5.172   -26.613 -3.058   1.00 54.29  ? 231  GLN   B HE21 1 
ATOM   12474 H  HE22 . GLN   B  2  227 ? 4.257   -25.561 -2.534   1.00 54.29  ? 231  GLN   B HE22 1 
ATOM   12475 N  N    . ALA   B  2  228 ? 5.582   -31.009 0.860    1.00 47.96  ? 232  ALA   B N    1 
ATOM   12476 C  CA   . ALA   B  2  228 ? 5.518   -31.703 2.141    1.00 46.37  ? 232  ALA   B CA   1 
ATOM   12477 C  C    . ALA   B  2  228 ? 6.361   -31.003 3.198    1.00 45.75  ? 232  ALA   B C    1 
ATOM   12478 O  O    . ALA   B  2  228 ? 6.028   -31.051 4.388    1.00 50.73  ? 232  ALA   B O    1 
ATOM   12479 C  CB   . ALA   B  2  228 ? 5.971   -33.153 1.980    1.00 45.59  ? 232  ALA   B CB   1 
ATOM   12480 H  H    . ALA   B  2  228 ? 5.925   -31.467 0.218    1.00 57.59  ? 232  ALA   B H    1 
ATOM   12481 H  HA   . ALA   B  2  228 ? 4.597   -31.709 2.445    1.00 55.68  ? 232  ALA   B HA   1 
ATOM   12482 H  HB1  . ALA   B  2  228 ? 5.907   -33.602 2.837    1.00 54.75  ? 232  ALA   B HB1  1 
ATOM   12483 H  HB2  . ALA   B  2  228 ? 5.398   -33.593 1.332    1.00 54.75  ? 232  ALA   B HB2  1 
ATOM   12484 H  HB3  . ALA   B  2  228 ? 6.890   -33.164 1.669    1.00 54.75  ? 232  ALA   B HB3  1 
ATOM   12485 N  N    . ALA   B  2  229 ? 7.446   -30.346 2.789    1.00 45.08  ? 233  ALA   B N    1 
ATOM   12486 C  CA   . ALA   B  2  229 ? 8.321   -29.688 3.752    1.00 49.58  ? 233  ALA   B CA   1 
ATOM   12487 C  C    . ALA   B  2  229 ? 7.771   -28.343 4.208    1.00 54.92  ? 233  ALA   B C    1 
ATOM   12488 O  O    . ALA   B  2  229 ? 8.017   -27.935 5.347    1.00 57.42  ? 233  ALA   B O    1 
ATOM   12489 C  CB   . ALA   B  2  229 ? 9.716   -29.497 3.152    1.00 46.94  ? 233  ALA   B CB   1 
ATOM   12490 H  H    . ALA   B  2  229 ? 7.694   -30.268 1.969    1.00 54.13  ? 233  ALA   B H    1 
ATOM   12491 H  HA   . ALA   B  2  229 ? 8.401   -30.259 4.532    1.00 59.53  ? 233  ALA   B HA   1 
ATOM   12492 H  HB1  . ALA   B  2  229 ? 10.279  -29.046 3.800    1.00 56.37  ? 233  ALA   B HB1  1 
ATOM   12493 H  HB2  . ALA   B  2  229 ? 10.089  -30.366 2.938    1.00 56.37  ? 233  ALA   B HB2  1 
ATOM   12494 H  HB3  . ALA   B  2  229 ? 9.643   -28.961 2.347    1.00 56.37  ? 233  ALA   B HB3  1 
ATOM   12495 N  N    . VAL   B  2  230 ? 7.024   -27.653 3.352    1.00 57.18  ? 234  VAL   B N    1 
ATOM   12496 C  CA   . VAL   B  2  230 ? 6.597   -26.285 3.617    1.00 59.96  ? 234  VAL   B CA   1 
ATOM   12497 C  C    . VAL   B  2  230 ? 5.190   -26.229 4.199    1.00 61.25  ? 234  VAL   B C    1 
ATOM   12498 O  O    . VAL   B  2  230 ? 4.906   -25.387 5.052    1.00 65.37  ? 234  VAL   B O    1 
ATOM   12499 C  CB   . VAL   B  2  230 ? 6.699   -25.449 2.321    1.00 64.78  ? 234  VAL   B CB   1 
ATOM   12500 C  CG1  . VAL   B  2  230 ? 5.964   -24.125 2.468    1.00 73.64  ? 234  VAL   B CG1  1 
ATOM   12501 C  CG2  . VAL   B  2  230 ? 8.161   -25.210 1.965    1.00 62.20  ? 234  VAL   B CG2  1 
ATOM   12502 H  H    . VAL   B  2  230 ? 6.748   -27.961 2.598    1.00 68.66  ? 234  VAL   B H    1 
ATOM   12503 H  HA   . VAL   B  2  230 ? 7.191   -25.897 4.278    1.00 71.99  ? 234  VAL   B HA   1 
ATOM   12504 H  HB   . VAL   B  2  230 ? 6.280   -25.943 1.599    1.00 77.77  ? 234  VAL   B HB   1 
ATOM   12505 H  HG11 . VAL   B  2  230 ? 6.133   -23.581 1.682    1.00 88.40  ? 234  VAL   B HG11 1 
ATOM   12506 H  HG12 . VAL   B  2  230 ? 5.013   -24.299 2.550    1.00 88.40  ? 234  VAL   B HG12 1 
ATOM   12507 H  HG13 . VAL   B  2  230 ? 6.287   -23.670 3.261    1.00 88.40  ? 234  VAL   B HG13 1 
ATOM   12508 H  HG21 . VAL   B  2  230 ? 8.205   -24.662 1.166    1.00 74.68  ? 234  VAL   B HG21 1 
ATOM   12509 H  HG22 . VAL   B  2  230 ? 8.595   -24.756 2.703    1.00 74.68  ? 234  VAL   B HG22 1 
ATOM   12510 H  HG23 . VAL   B  2  230 ? 8.590   -26.065 1.804    1.00 74.68  ? 234  VAL   B HG23 1 
ATOM   12511 N  N    . CYS   B  2  231 ? 4.293   -27.111 3.755    1.00 59.53  ? 235  CYS   B N    1 
ATOM   12512 C  CA   . CYS   B  2  231 ? 2.886   -27.058 4.160    1.00 59.19  ? 235  CYS   B CA   1 
ATOM   12513 C  C    . CYS   B  2  231 ? 2.726   -27.675 5.552    1.00 61.77  ? 235  CYS   B C    1 
ATOM   12514 O  O    . CYS   B  2  231 ? 2.133   -28.739 5.740    1.00 63.72  ? 235  CYS   B O    1 
ATOM   12515 C  CB   . CYS   B  2  231 ? 2.012   -27.771 3.137    1.00 56.74  ? 235  CYS   B CB   1 
ATOM   12516 S  SG   . CYS   B  2  231 ? 2.068   -27.102 1.457    1.00 59.99  ? 235  CYS   B SG   1 
ATOM   12517 H  H    . CYS   B  2  231 ? 4.475   -27.754 3.214    1.00 71.47  ? 235  CYS   B H    1 
ATOM   12518 H  HA   . CYS   B  2  231 ? 2.615   -26.128 4.207    1.00 71.07  ? 235  CYS   B HA   1 
ATOM   12519 H  HB2  . CYS   B  2  231 ? 2.294   -28.698 3.088    1.00 68.13  ? 235  CYS   B HB2  1 
ATOM   12520 H  HB3  . CYS   B  2  231 ? 1.090   -27.721 3.437    1.00 68.13  ? 235  CYS   B HB3  1 
ATOM   12521 N  N    . LYS   B  2  232 ? 3.259   -26.964 6.549    1.00 61.86  ? 236  LYS   B N    1 
ATOM   12522 C  CA   . LYS   B  2  232 ? 3.270   -27.492 7.911    1.00 64.10  ? 236  LYS   B CA   1 
ATOM   12523 C  C    . LYS   B  2  232 ? 1.856   -27.744 8.425    1.00 69.30  ? 236  LYS   B C    1 
ATOM   12524 O  O    . LYS   B  2  232 ? 1.564   -28.817 8.964    1.00 68.81  ? 236  LYS   B O    1 
ATOM   12525 C  CB   . LYS   B  2  232 ? 4.020   -26.533 8.839    1.00 62.46  ? 236  LYS   B CB   1 
ATOM   12526 C  CG   . LYS   B  2  232 ? 3.834   -26.813 10.332   1.00 63.29  ? 236  LYS   B CG   1 
ATOM   12527 C  CD   . LYS   B  2  232 ? 4.817   -26.000 11.170   1.00 63.82  ? 236  LYS   B CD   1 
ATOM   12528 C  CE   . LYS   B  2  232 ? 4.458   -25.990 12.655   1.00 71.30  ? 236  LYS   B CE   1 
ATOM   12529 N  NZ   . LYS   B  2  232 ? 5.019   -27.147 13.410   1.00 71.49  ? 236  LYS   B NZ   1 
ATOM   12530 H  H    . LYS   B  2  232 ? 3.614   -26.186 6.463    1.00 74.27  ? 236  LYS   B H    1 
ATOM   12531 H  HA   . LYS   B  2  232 ? 3.740   -28.340 7.908    1.00 76.95  ? 236  LYS   B HA   1 
ATOM   12532 H  HB2  . LYS   B  2  232 ? 4.968   -26.595 8.646    1.00 74.99  ? 236  LYS   B HB2  1 
ATOM   12533 H  HB3  . LYS   B  2  232 ? 3.705   -25.631 8.670    1.00 74.99  ? 236  LYS   B HB3  1 
ATOM   12534 H  HG2  . LYS   B  2  232 ? 2.932   -26.571 10.596   1.00 75.99  ? 236  LYS   B HG2  1 
ATOM   12535 H  HG3  . LYS   B  2  232 ? 3.988   -27.755 10.506   1.00 75.99  ? 236  LYS   B HG3  1 
ATOM   12536 H  HD2  . LYS   B  2  232 ? 5.704   -26.383 11.078   1.00 76.62  ? 236  LYS   B HD2  1 
ATOM   12537 H  HD3  . LYS   B  2  232 ? 4.818   -25.083 10.856   1.00 76.62  ? 236  LYS   B HD3  1 
ATOM   12538 H  HE2  . LYS   B  2  232 ? 4.804   -25.178 13.056   1.00 85.60  ? 236  LYS   B HE2  1 
ATOM   12539 H  HE3  . LYS   B  2  232 ? 3.492   -26.018 12.744   1.00 85.60  ? 236  LYS   B HE3  1 
ATOM   12540 H  HZ1  . LYS   B  2  232 ? 5.089   -26.942 14.273   1.00 85.83  ? 236  LYS   B HZ1  1 
ATOM   12541 H  HZ2  . LYS   B  2  232 ? 4.487   -27.855 13.323   1.00 85.83  ? 236  LYS   B HZ2  1 
ATOM   12542 H  HZ3  . LYS   B  2  232 ? 5.826   -27.353 13.096   1.00 85.83  ? 236  LYS   B HZ3  1 
ATOM   12543 N  N    . GLU   B  2  233 ? 0.961   -26.764 8.274    1.00 76.32  ? 237  GLU   B N    1 
ATOM   12544 C  CA   . GLU   B  2  233 ? -0.382  -26.916 8.827    1.00 82.78  ? 237  GLU   B CA   1 
ATOM   12545 C  C    . GLU   B  2  233 ? -1.123  -28.065 8.155    1.00 76.72  ? 237  GLU   B C    1 
ATOM   12546 O  O    . GLU   B  2  233 ? -1.704  -28.924 8.829    1.00 77.65  ? 237  GLU   B O    1 
ATOM   12547 C  CB   . GLU   B  2  233 ? -1.173  -25.614 8.683    1.00 95.10  ? 237  GLU   B CB   1 
ATOM   12548 C  CG   . GLU   B  2  233 ? -2.521  -25.645 9.403    1.00 111.32 ? 237  GLU   B CG   1 
ATOM   12549 C  CD   . GLU   B  2  233 ? -3.385  -24.436 9.105    1.00 126.57 ? 237  GLU   B CD   1 
ATOM   12550 O  OE1  . GLU   B  2  233 ? -3.202  -23.817 8.036    1.00 133.47 ? 237  GLU   B OE1  1 
ATOM   12551 O  OE2  . GLU   B  2  233 ? -4.251  -24.106 9.943    1.00 136.50 ? 237  GLU   B OE2  1 
ATOM   12552 H  H    . GLU   B  2  233 ? 1.104   -26.021 7.866    1.00 91.63  ? 237  GLU   B H    1 
ATOM   12553 H  HA   . GLU   B  2  233 ? -0.302  -27.112 9.774    1.00 99.37  ? 237  GLU   B HA   1 
ATOM   12554 H  HB2  . GLU   B  2  233 ? -0.652  -24.887 9.057    1.00 114.16 ? 237  GLU   B HB2  1 
ATOM   12555 H  HB3  . GLU   B  2  233 ? -1.341  -25.452 7.741    1.00 114.16 ? 237  GLU   B HB3  1 
ATOM   12556 H  HG2  . GLU   B  2  233 ? -3.009  -26.436 9.124    1.00 133.63 ? 237  GLU   B HG2  1 
ATOM   12557 H  HG3  . GLU   B  2  233 ? -2.366  -25.672 10.360   1.00 133.63 ? 237  GLU   B HG3  1 
ATOM   12558 N  N    . LYS   B  2  234 ? -1.111  -28.100 6.821    1.00 70.77  ? 238  LYS   B N    1 
ATOM   12559 C  CA   . LYS   B  2  234 ? -1.894  -29.103 6.106    1.00 62.11  ? 238  LYS   B CA   1 
ATOM   12560 C  C    . LYS   B  2  234 ? -1.262  -30.487 6.219    1.00 58.33  ? 238  LYS   B C    1 
ATOM   12561 O  O    . LYS   B  2  234 ? -1.973  -31.483 6.402    1.00 58.32  ? 238  LYS   B O    1 
ATOM   12562 C  CB   . LYS   B  2  234 ? -2.061  -28.687 4.643    1.00 56.71  ? 238  LYS   B CB   1 
ATOM   12563 C  CG   . LYS   B  2  234 ? -3.174  -27.657 4.424    1.00 60.87  ? 238  LYS   B CG   1 
ATOM   12564 C  CD   . LYS   B  2  234 ? -3.089  -26.994 3.053    1.00 66.98  ? 238  LYS   B CD   1 
ATOM   12565 C  CE   . LYS   B  2  234 ? -4.406  -26.332 2.653    1.00 74.35  ? 238  LYS   B CE   1 
ATOM   12566 N  NZ   . LYS   B  2  234 ? -5.323  -27.277 1.950    1.00 75.67  ? 238  LYS   B NZ   1 
ATOM   12567 H  H    . LYS   B  2  234 ? -0.666  -27.564 6.317    1.00 84.96  ? 238  LYS   B H    1 
ATOM   12568 H  HA   . LYS   B  2  234 ? -2.778  -29.156 6.501    1.00 74.57  ? 238  LYS   B HA   1 
ATOM   12569 H  HB2  . LYS   B  2  234 ? -1.230  -28.296 4.332    1.00 68.09  ? 238  LYS   B HB2  1 
ATOM   12570 H  HB3  . LYS   B  2  234 ? -2.275  -29.473 4.117    1.00 68.09  ? 238  LYS   B HB3  1 
ATOM   12571 H  HG2  . LYS   B  2  234 ? -4.035  -28.100 4.491    1.00 73.08  ? 238  LYS   B HG2  1 
ATOM   12572 H  HG3  . LYS   B  2  234 ? -3.104  -26.964 5.099    1.00 73.08  ? 238  LYS   B HG3  1 
ATOM   12573 H  HD2  . LYS   B  2  234 ? -2.401  -26.310 3.071    1.00 80.41  ? 238  LYS   B HD2  1 
ATOM   12574 H  HD3  . LYS   B  2  234 ? -2.873  -27.665 2.386    1.00 80.41  ? 238  LYS   B HD3  1 
ATOM   12575 H  HE2  . LYS   B  2  234 ? -4.856  -26.012 3.450    1.00 89.26  ? 238  LYS   B HE2  1 
ATOM   12576 H  HE3  . LYS   B  2  234 ? -4.221  -25.591 2.055    1.00 89.26  ? 238  LYS   B HE3  1 
ATOM   12577 H  HZ1  . LYS   B  2  234 ? -5.409  -27.039 1.097    1.00 90.84  ? 238  LYS   B HZ1  1 
ATOM   12578 H  HZ2  . LYS   B  2  234 ? -4.996  -28.103 1.989    1.00 90.84  ? 238  LYS   B HZ2  1 
ATOM   12579 H  HZ3  . LYS   B  2  234 ? -6.125  -27.265 2.336    1.00 90.84  ? 238  LYS   B HZ3  1 
ATOM   12580 N  N    . ILE   B  2  235 ? 0.067   -30.578 6.116    1.00 55.02  ? 239  ILE   B N    1 
ATOM   12581 C  CA   . ILE   B  2  235 ? 0.731   -31.855 6.367    1.00 52.92  ? 239  ILE   B CA   1 
ATOM   12582 C  C    . ILE   B  2  235 ? 0.518   -32.279 7.813    1.00 52.81  ? 239  ILE   B C    1 
ATOM   12583 O  O    . ILE   B  2  235 ? 0.258   -33.453 8.102    1.00 51.34  ? 239  ILE   B O    1 
ATOM   12584 C  CB   . ILE   B  2  235 ? 2.231   -31.766 6.027    1.00 57.62  ? 239  ILE   B CB   1 
ATOM   12585 C  CG1  . ILE   B  2  235 ? 2.432   -31.525 4.527    1.00 58.85  ? 239  ILE   B CG1  1 
ATOM   12586 C  CG2  . ILE   B  2  235 ? 2.959   -33.037 6.474    1.00 57.66  ? 239  ILE   B CG2  1 
ATOM   12587 C  CD1  . ILE   B  2  235 ? 1.950   -32.661 3.640    1.00 59.40  ? 239  ILE   B CD1  1 
ATOM   12588 H  H    . ILE   B  2  235 ? 0.592   -29.930 5.908    1.00 66.06  ? 239  ILE   B H    1 
ATOM   12589 H  HA   . ILE   B  2  235 ? 0.335   -32.523 5.786    1.00 63.54  ? 239  ILE   B HA   1 
ATOM   12590 H  HB   . ILE   B  2  235 ? 2.606   -31.012 6.507    1.00 69.17  ? 239  ILE   B HB   1 
ATOM   12591 H  HG12 . ILE   B  2  235 ? 1.942   -30.727 4.274    1.00 70.66  ? 239  ILE   B HG12 1 
ATOM   12592 H  HG13 . ILE   B  2  235 ? 3.379   -31.401 4.358    1.00 70.66  ? 239  ILE   B HG13 1 
ATOM   12593 H  HG21 . ILE   B  2  235 ? 3.882   -32.993 6.179    1.00 69.23  ? 239  ILE   B HG21 1 
ATOM   12594 H  HG22 . ILE   B  2  235 ? 2.924   -33.097 7.442    1.00 69.23  ? 239  ILE   B HG22 1 
ATOM   12595 H  HG23 . ILE   B  2  235 ? 2.521   -33.807 6.079    1.00 69.23  ? 239  ILE   B HG23 1 
ATOM   12596 H  HD11 . ILE   B  2  235 ? 2.110   -32.427 2.712    1.00 71.32  ? 239  ILE   B HD11 1 
ATOM   12597 H  HD12 . ILE   B  2  235 ? 2.440   -33.467 3.866    1.00 71.32  ? 239  ILE   B HD12 1 
ATOM   12598 H  HD13 . ILE   B  2  235 ? 1.001   -32.797 3.788    1.00 71.32  ? 239  ILE   B HD13 1 
ATOM   12599 N  N    . GLY   B  2  236 ? 0.630   -31.335 8.740    1.00 52.42  ? 240  GLY   B N    1 
ATOM   12600 C  CA   . GLY   B  2  236 ? 0.438   -31.613 10.143   1.00 52.03  ? 240  GLY   B CA   1 
ATOM   12601 C  C    . GLY   B  2  236 ? 1.700   -31.759 10.965   1.00 57.05  ? 240  GLY   B C    1 
ATOM   12602 O  O    . GLY   B  2  236 ? 1.623   -32.289 12.079   1.00 62.43  ? 240  GLY   B O    1 
ATOM   12603 H  H    . GLY   B  2  236 ? 0.821   -30.514 8.572    1.00 62.94  ? 240  GLY   B H    1 
ATOM   12604 H  HA2  . GLY   B  2  236 ? -0.080  -30.890 10.530   1.00 62.48  ? 240  GLY   B HA2  1 
ATOM   12605 H  HA3  . GLY   B  2  236 ? -0.062  -32.440 10.227   1.00 62.48  ? 240  GLY   B HA3  1 
ATOM   12606 N  N    . TRP   B  2  237 ? 2.853   -31.327 10.455   1.00 59.53  ? 241  TRP   B N    1 
ATOM   12607 C  CA   . TRP   B  2  237 ? 4.074   -31.355 11.250   1.00 63.70  ? 241  TRP   B CA   1 
ATOM   12608 C  C    . TRP   B  2  237 ? 3.840   -30.652 12.581   1.00 74.02  ? 241  TRP   B C    1 
ATOM   12609 O  O    . TRP   B  2  237 ? 3.428   -29.488 12.612   1.00 77.10  ? 241  TRP   B O    1 
ATOM   12610 C  CB   . TRP   B  2  237 ? 5.227   -30.669 10.510   1.00 59.03  ? 241  TRP   B CB   1 
ATOM   12611 C  CG   . TRP   B  2  237 ? 5.601   -31.241 9.174    1.00 53.16  ? 241  TRP   B CG   1 
ATOM   12612 C  CD1  . TRP   B  2  237 ? 5.560   -30.595 7.973    1.00 51.68  ? 241  TRP   B CD1  1 
ATOM   12613 C  CD2  . TRP   B  2  237 ? 6.096   -32.559 8.903    1.00 49.85  ? 241  TRP   B CD2  1 
ATOM   12614 N  NE1  . TRP   B  2  237 ? 5.993   -31.428 6.971    1.00 50.84  ? 241  TRP   B NE1  1 
ATOM   12615 C  CE2  . TRP   B  2  237 ? 6.326   -32.640 7.514    1.00 49.45  ? 241  TRP   B CE2  1 
ATOM   12616 C  CE3  . TRP   B  2  237 ? 6.363   -33.679 9.697    1.00 50.79  ? 241  TRP   B CE3  1 
ATOM   12617 C  CZ2  . TRP   B  2  237 ? 6.807   -33.796 6.903    1.00 50.51  ? 241  TRP   B CZ2  1 
ATOM   12618 C  CZ3  . TRP   B  2  237 ? 6.840   -34.827 9.086    1.00 51.46  ? 241  TRP   B CZ3  1 
ATOM   12619 C  CH2  . TRP   B  2  237 ? 7.057   -34.875 7.704    1.00 51.84  ? 241  TRP   B CH2  1 
ATOM   12620 H  H    . TRP   B  2  237 ? 2.952   -31.018 9.659    1.00 71.48  ? 241  TRP   B H    1 
ATOM   12621 H  HA   . TRP   B  2  237 ? 4.326   -32.279 11.401   1.00 76.48  ? 241  TRP   B HA   1 
ATOM   12622 H  HB2  . TRP   B  2  237 ? 4.981   -29.742 10.363   1.00 70.87  ? 241  TRP   B HB2  1 
ATOM   12623 H  HB3  . TRP   B  2  237 ? 6.016   -30.718 11.071   1.00 70.87  ? 241  TRP   B HB3  1 
ATOM   12624 H  HD1  . TRP   B  2  237 ? 5.280   -29.717 7.850    1.00 62.06  ? 241  TRP   B HD1  1 
ATOM   12625 H  HE1  . TRP   B  2  237 ? 6.046   -31.222 6.138    1.00 61.05  ? 241  TRP   B HE1  1 
ATOM   12626 H  HE3  . TRP   B  2  237 ? 6.223   -33.653 10.616   1.00 60.98  ? 241  TRP   B HE3  1 
ATOM   12627 H  HZ2  . TRP   B  2  237 ? 6.951   -33.831 5.985    1.00 60.65  ? 241  TRP   B HZ2  1 
ATOM   12628 H  HZ3  . TRP   B  2  237 ? 7.019   -35.579 9.604    1.00 61.79  ? 241  TRP   B HZ3  1 
ATOM   12629 H  HH2  . TRP   B  2  237 ? 7.380   -35.659 7.321    1.00 62.25  ? 241  TRP   B HH2  1 
ATOM   12630 N  N    . ARG   B  2  238 ? 4.100   -31.352 13.679   1.00 79.64  ? 242  ARG   B N    1 
ATOM   12631 C  CA   . ARG   B  2  238 ? 4.015   -30.761 15.007   1.00 89.25  ? 242  ARG   B CA   1 
ATOM   12632 C  C    . ARG   B  2  238 ? 5.406   -30.344 15.471   1.00 87.64  ? 242  ARG   B C    1 
ATOM   12633 O  O    . ARG   B  2  238 ? 6.405   -30.985 15.133   1.00 83.73  ? 242  ARG   B O    1 
ATOM   12634 C  CB   . ARG   B  2  238 ? 3.393   -31.740 16.009   1.00 96.41  ? 242  ARG   B CB   1 
ATOM   12635 C  CG   . ARG   B  2  238 ? 4.204   -33.006 16.252   1.00 99.26  ? 242  ARG   B CG   1 
ATOM   12636 C  CD   . ARG   B  2  238 ? 3.462   -33.987 17.152   1.00 108.42 ? 242  ARG   B CD   1 
ATOM   12637 N  NE   . ARG   B  2  238 ? 3.870   -35.366 16.897   1.00 119.02 ? 242  ARG   B NE   1 
ATOM   12638 C  CZ   . ARG   B  2  238 ? 3.382   -36.427 17.534   1.00 138.04 ? 242  ARG   B CZ   1 
ATOM   12639 N  NH1  . ARG   B  2  238 ? 2.461   -36.282 18.478   1.00 148.71 ? 242  ARG   B NH1  1 
ATOM   12640 N  NH2  . ARG   B  2  238 ? 3.820   -37.640 17.224   1.00 142.69 ? 242  ARG   B NH2  1 
ATOM   12641 H  H    . ARG   B  2  238 ? 4.331   -32.180 13.680   1.00 95.60  ? 242  ARG   B H    1 
ATOM   12642 H  HA   . ARG   B  2  238 ? 3.448   -29.974 14.981   1.00 107.13 ? 242  ARG   B HA   1 
ATOM   12643 H  HB2  . ARG   B  2  238 ? 3.296   -31.288 16.862   1.00 115.73 ? 242  ARG   B HB2  1 
ATOM   12644 H  HB3  . ARG   B  2  238 ? 2.523   -32.011 15.676   1.00 115.73 ? 242  ARG   B HB3  1 
ATOM   12645 H  HG2  . ARG   B  2  238 ? 4.378   -33.443 15.404   1.00 119.15 ? 242  ARG   B HG2  1 
ATOM   12646 H  HG3  . ARG   B  2  238 ? 5.041   -32.772 16.683   1.00 119.15 ? 242  ARG   B HG3  1 
ATOM   12647 H  HD2  . ARG   B  2  238 ? 3.653   -33.779 18.079   1.00 130.15 ? 242  ARG   B HD2  1 
ATOM   12648 H  HD3  . ARG   B  2  238 ? 2.509   -33.916 16.985   1.00 130.15 ? 242  ARG   B HD3  1 
ATOM   12649 H  HE   . ARG   B  2  238 ? 4.468   -35.502 16.294   1.00 142.86 ? 242  ARG   B HE   1 
ATOM   12650 H  HH11 . ARG   B  2  238 ? 2.175   -35.497 18.682   1.00 178.49 ? 242  ARG   B HH11 1 
ATOM   12651 H  HH12 . ARG   B  2  238 ? 2.150   -36.973 18.885   1.00 178.49 ? 242  ARG   B HH12 1 
ATOM   12652 H  HH21 . ARG   B  2  238 ? 4.417   -37.738 16.613   1.00 171.27 ? 242  ARG   B HH21 1 
ATOM   12653 H  HH22 . ARG   B  2  238 ? 3.506   -38.328 17.634   1.00 171.27 ? 242  ARG   B HH22 1 
ATOM   12654 N  N    . ASN   B  2  239 ? 5.468   -29.257 16.247   1.00 88.88  ? 243  ASN   B N    1 
ATOM   12655 C  CA   . ASN   B  2  239 ? 6.747   -28.813 16.785   1.00 90.50  ? 243  ASN   B CA   1 
ATOM   12656 C  C    . ASN   B  2  239 ? 7.426   -29.947 17.549   1.00 86.95  ? 243  ASN   B C    1 
ATOM   12657 O  O    . ASN   B  2  239 ? 6.839   -31.017 17.738   1.00 90.01  ? 243  ASN   B O    1 
ATOM   12658 C  CB   . ASN   B  2  239 ? 6.621   -27.652 17.773   1.00 105.12 ? 243  ASN   B CB   1 
ATOM   12659 C  CG   . ASN   B  2  239 ? 5.970   -26.407 17.205   1.00 120.48 ? 243  ASN   B CG   1 
ATOM   12660 O  OD1  . ASN   B  2  239 ? 5.434   -26.372 16.096   1.00 125.38 ? 243  ASN   B OD1  1 
ATOM   12661 N  ND2  . ASN   B  2  239 ? 6.024   -25.354 18.024   1.00 132.09 ? 243  ASN   B ND2  1 
ATOM   12662 H  H    . ASN   B  2  239 ? 4.794   -28.771 16.469   1.00 106.70 ? 243  ASN   B H    1 
ATOM   12663 H  HA   . ASN   B  2  239 ? 7.269   -28.521 16.022   1.00 108.63 ? 243  ASN   B HA   1 
ATOM   12664 H  HB2  . ASN   B  2  239 ? 6.085   -27.944 18.527   1.00 126.18 ? 243  ASN   B HB2  1 
ATOM   12665 H  HB3  . ASN   B  2  239 ? 7.510   -27.405 18.075   1.00 126.18 ? 243  ASN   B HB3  1 
ATOM   12666 H  HD21 . ASN   B  2  239 ? 6.439   -25.482 18.766   1.00 158.54 ? 243  ASN   B HD21 1 
ATOM   12667 N  N    . ASP   B  2  240 ? 8.646   -29.692 18.017   1.00 82.58  ? 244  ASP   B N    1 
ATOM   12668 C  CA   . ASP   B  2  240 ? 9.311   -30.510 19.030   1.00 81.34  ? 244  ASP   B CA   1 
ATOM   12669 C  C    . ASP   B  2  240 ? 9.064   -31.999 18.810   1.00 75.23  ? 244  ASP   B C    1 
ATOM   12670 O  O    . ASP   B  2  240 ? 8.675   -32.739 19.716   1.00 72.69  ? 244  ASP   B O    1 
ATOM   12671 C  CB   . ASP   B  2  240 ? 8.870   -30.085 20.431   1.00 88.30  ? 244  ASP   B CB   1 
ATOM   12672 C  CG   . ASP   B  2  240 ? 9.439   -28.741 20.838   1.00 96.97  ? 244  ASP   B CG   1 
ATOM   12673 O  OD1  . ASP   B  2  240 ? 10.653  -28.523 20.639   1.00 98.99  ? 244  ASP   B OD1  1 
ATOM   12674 O  OD2  . ASP   B  2  240 ? 8.673   -27.900 21.353   1.00 102.37 ? 244  ASP   B OD2  1 
ATOM   12675 H  H    . ASP   B  2  240 ? 9.125   -29.027 17.755   1.00 99.13  ? 244  ASP   B H    1 
ATOM   12676 H  HA   . ASP   B  2  240 ? 10.267  -30.368 18.946   1.00 97.65  ? 244  ASP   B HA   1 
ATOM   12677 H  HB2  . ASP   B  2  240 ? 7.903   -30.021 20.453   1.00 106.00 ? 244  ASP   B HB2  1 
ATOM   12678 H  HB3  . ASP   B  2  240 ? 9.173   -30.747 21.072   1.00 106.00 ? 244  ASP   B HB3  1 
ATOM   12679 N  N    . SER   B  2  241 ? 9.287   -32.437 17.574   1.00 70.53  ? 245  SER   B N    1 
ATOM   12680 C  CA   . SER   B  2  241 ? 9.273   -33.854 17.247   1.00 66.89  ? 245  SER   B CA   1 
ATOM   12681 C  C    . SER   B  2  241 ? 10.143  -34.066 16.018   1.00 62.48  ? 245  SER   B C    1 
ATOM   12682 O  O    . SER   B  2  241 ? 10.535  -33.115 15.336   1.00 61.90  ? 245  SER   B O    1 
ATOM   12683 C  CB   . SER   B  2  241 ? 7.854   -34.375 16.995   1.00 67.00  ? 245  SER   B CB   1 
ATOM   12684 O  OG   . SER   B  2  241 ? 7.440   -34.117 15.665   1.00 65.83  ? 245  SER   B OG   1 
ATOM   12685 H  H    . SER   B  2  241 ? 9.449   -31.925 16.902   1.00 84.68  ? 245  SER   B H    1 
ATOM   12686 H  HA   . SER   B  2  241 ? 9.645   -34.351 17.992   1.00 80.31  ? 245  SER   B HA   1 
ATOM   12687 H  HB2  . SER   B  2  241 ? 7.840   -35.333 17.148   1.00 80.44  ? 245  SER   B HB2  1 
ATOM   12688 H  HB3  . SER   B  2  241 ? 7.244   -33.932 17.605   1.00 80.44  ? 245  SER   B HB3  1 
ATOM   12689 H  HG   . SER   B  2  241 ? 7.214   -33.312 15.585   1.00 79.04  ? 245  SER   B HG   1 
ATOM   12690 N  N    . LEU   B  2  242 ? 10.449  -35.329 15.745   1.00 61.34  ? 246  LEU   B N    1 
ATOM   12691 C  CA   . LEU   B  2  242 ? 11.176  -35.666 14.531   1.00 60.15  ? 246  LEU   B CA   1 
ATOM   12692 C  C    . LEU   B  2  242 ? 10.255  -35.557 13.323   1.00 59.01  ? 246  LEU   B C    1 
ATOM   12693 O  O    . LEU   B  2  242 ? 9.062   -35.866 13.399   1.00 63.08  ? 246  LEU   B O    1 
ATOM   12694 C  CB   . LEU   B  2  242 ? 11.751  -37.077 14.623   1.00 59.68  ? 246  LEU   B CB   1 
ATOM   12695 C  CG   . LEU   B  2  242 ? 13.267  -37.218 14.770   1.00 61.25  ? 246  LEU   B CG   1 
ATOM   12696 C  CD1  . LEU   B  2  242 ? 13.630  -38.689 14.730   1.00 62.95  ? 246  LEU   B CD1  1 
ATOM   12697 C  CD2  . LEU   B  2  242 ? 14.013  -36.458 13.685   1.00 64.19  ? 246  LEU   B CD2  1 
ATOM   12698 H  H    . LEU   B  2  242 ? 10.248  -36.002 16.241   1.00 73.64  ? 246  LEU   B H    1 
ATOM   12699 H  HA   . LEU   B  2  242 ? 11.916  -35.050 14.416   1.00 72.22  ? 246  LEU   B HA   1 
ATOM   12700 H  HB2  . LEU   B  2  242 ? 11.354  -37.509 15.395   1.00 71.65  ? 246  LEU   B HB2  1 
ATOM   12701 H  HB3  . LEU   B  2  242 ? 11.503  -37.551 13.813   1.00 71.65  ? 246  LEU   B HB3  1 
ATOM   12702 H  HG   . LEU   B  2  242 ? 13.541  -36.836 15.618   1.00 73.54  ? 246  LEU   B HG   1 
ATOM   12703 H  HD11 . LEU   B  2  242 ? 14.594  -38.778 14.791   1.00 75.57  ? 246  LEU   B HD11 1 
ATOM   12704 H  HD12 . LEU   B  2  242 ? 13.208  -39.139 15.478   1.00 75.57  ? 246  LEU   B HD12 1 
ATOM   12705 H  HD13 . LEU   B  2  242 ? 13.315  -39.070 13.895   1.00 75.57  ? 246  LEU   B HD13 1 
ATOM   12706 H  HD21 . LEU   B  2  242 ? 14.961  -36.644 13.765   1.00 77.07  ? 246  LEU   B HD21 1 
ATOM   12707 H  HD22 . LEU   B  2  242 ? 13.691  -36.749 12.818   1.00 77.07  ? 246  LEU   B HD22 1 
ATOM   12708 H  HD23 . LEU   B  2  242 ? 13.851  -35.508 13.797   1.00 77.07  ? 246  LEU   B HD23 1 
ATOM   12709 N  N    . HIS   B  2  243 ? 10.816  -35.118 12.201   1.00 54.72  ? 247  HIS   B N    1 
ATOM   12710 C  CA   . HIS   B  2  243 ? 10.077  -34.946 10.953   1.00 48.00  ? 247  HIS   B CA   1 
ATOM   12711 C  C    . HIS   B  2  243 ? 10.744  -35.815 9.893    1.00 44.34  ? 247  HIS   B C    1 
ATOM   12712 O  O    . HIS   B  2  243 ? 11.733  -35.404 9.277    1.00 43.21  ? 247  HIS   B O    1 
ATOM   12713 C  CB   . HIS   B  2  243 ? 10.050  -33.482 10.530   1.00 47.29  ? 247  HIS   B CB   1 
ATOM   12714 C  CG   . HIS   B  2  243 ? 9.486   -32.564 11.567   1.00 52.31  ? 247  HIS   B CG   1 
ATOM   12715 N  ND1  . HIS   B  2  243 ? 10.017  -31.319 11.824   1.00 53.84  ? 247  HIS   B ND1  1 
ATOM   12716 C  CD2  . HIS   B  2  243 ? 8.436   -32.707 12.410   1.00 54.93  ? 247  HIS   B CD2  1 
ATOM   12717 C  CE1  . HIS   B  2  243 ? 9.320   -30.735 12.782   1.00 56.91  ? 247  HIS   B CE1  1 
ATOM   12718 N  NE2  . HIS   B  2  243 ? 8.354   -31.556 13.154   1.00 56.46  ? 247  HIS   B NE2  1 
ATOM   12719 H  H    . HIS   B  2  243 ? 11.647  -34.906 12.136   1.00 65.70  ? 247  HIS   B H    1 
ATOM   12720 H  HA   . HIS   B  2  243 ? 9.164   -35.249 11.075   1.00 57.63  ? 247  HIS   B HA   1 
ATOM   12721 H  HB2  . HIS   B  2  243 ? 10.958  -33.195 10.343   1.00 56.78  ? 247  HIS   B HB2  1 
ATOM   12722 H  HB3  . HIS   B  2  243 ? 9.505   -33.398 9.732    1.00 56.78  ? 247  HIS   B HB3  1 
ATOM   12723 H  HD1  . HIS   B  2  243 ? 10.696  -30.975 11.423   1.00 64.65  ? 247  HIS   B HD1  1 
ATOM   12724 H  HD2  . HIS   B  2  243 ? 7.875   -33.446 12.473   1.00 65.95  ? 247  HIS   B HD2  1 
ATOM   12725 H  HE1  . HIS   B  2  243 ? 9.481   -29.889 13.135   1.00 68.33  ? 247  HIS   B HE1  1 
ATOM   12726 H  HE2  . HIS   B  2  243 ? 7.769   -31.395 13.764   1.00 67.79  ? 247  HIS   B HE2  1 
ATOM   12727 N  N    . LEU   B  2  244 ? 10.203  -37.009 9.677    1.00 47.13  ? 248  LEU   B N    1 
ATOM   12728 C  CA   . LEU   B  2  244 ? 10.762  -37.963 8.727    1.00 49.34  ? 248  LEU   B CA   1 
ATOM   12729 C  C    . LEU   B  2  244 ? 9.916   -37.950 7.461    1.00 50.99  ? 248  LEU   B C    1 
ATOM   12730 O  O    . LEU   B  2  244 ? 8.747   -38.346 7.479    1.00 52.49  ? 248  LEU   B O    1 
ATOM   12731 C  CB   . LEU   B  2  244 ? 10.819  -39.362 9.334    1.00 50.16  ? 248  LEU   B CB   1 
ATOM   12732 C  CG   . LEU   B  2  244 ? 11.663  -39.477 10.603   1.00 51.41  ? 248  LEU   B CG   1 
ATOM   12733 C  CD1  . LEU   B  2  244 ? 11.574  -40.885 11.156   1.00 52.48  ? 248  LEU   B CD1  1 
ATOM   12734 C  CD2  . LEU   B  2  244 ? 13.114  -39.092 10.340   1.00 48.82  ? 248  LEU   B CD2  1 
ATOM   12735 H  H    . LEU   B  2  244 ? 9.497   -37.295 10.076   1.00 56.60  ? 248  LEU   B H    1 
ATOM   12736 H  HA   . LEU   B  2  244 ? 11.664  -37.691 8.495    1.00 59.25  ? 248  LEU   B HA   1 
ATOM   12737 H  HB2  . LEU   B  2  244 ? 9.915   -39.636 9.558    1.00 60.23  ? 248  LEU   B HB2  1 
ATOM   12738 H  HB3  . LEU   B  2  244 ? 11.195  -39.967 8.676    1.00 60.23  ? 248  LEU   B HB3  1 
ATOM   12739 H  HG   . LEU   B  2  244 ? 11.319  -38.860 11.267   1.00 61.73  ? 248  LEU   B HG   1 
ATOM   12740 H  HD11 . LEU   B  2  244 ? 12.137  -40.952 11.942   1.00 63.02  ? 248  LEU   B HD11 1 
ATOM   12741 H  HD12 . LEU   B  2  244 ? 10.652  -41.073 11.393   1.00 63.02  ? 248  LEU   B HD12 1 
ATOM   12742 H  HD13 . LEU   B  2  244 ? 11.875  -41.510 10.478   1.00 63.02  ? 248  LEU   B HD13 1 
ATOM   12743 H  HD21 . LEU   B  2  244 ? 13.620  -39.190 11.161   1.00 58.62  ? 248  LEU   B HD21 1 
ATOM   12744 H  HD22 . LEU   B  2  244 ? 13.477  -39.676 9.656    1.00 58.62  ? 248  LEU   B HD22 1 
ATOM   12745 H  HD23 . LEU   B  2  244 ? 13.146  -38.170 10.039   1.00 58.62  ? 248  LEU   B HD23 1 
ATOM   12746 N  N    . LEU   B  2  245 ? 10.511  -37.491 6.366    1.00 49.29  ? 249  LEU   B N    1 
ATOM   12747 C  CA   . LEU   B  2  245 ? 9.872   -37.499 5.056    1.00 46.32  ? 249  LEU   B CA   1 
ATOM   12748 C  C    . LEU   B  2  245 ? 10.477  -38.645 4.254    1.00 48.98  ? 249  LEU   B C    1 
ATOM   12749 O  O    . LEU   B  2  245 ? 11.652  -38.592 3.874    1.00 50.31  ? 249  LEU   B O    1 
ATOM   12750 C  CB   . LEU   B  2  245 ? 10.065  -36.162 4.348    1.00 40.83  ? 249  LEU   B CB   1 
ATOM   12751 C  CG   . LEU   B  2  245 ? 9.348   -36.010 3.006    1.00 44.19  ? 249  LEU   B CG   1 
ATOM   12752 C  CD1  . LEU   B  2  245 ? 7.843   -36.166 3.167    1.00 43.38  ? 249  LEU   B CD1  1 
ATOM   12753 C  CD2  . LEU   B  2  245 ? 9.684   -34.666 2.389    1.00 47.62  ? 249  LEU   B CD2  1 
ATOM   12754 H  H    . LEU   B  2  245 ? 11.305  -37.160 6.356    1.00 59.18  ? 249  LEU   B H    1 
ATOM   12755 H  HA   . LEU   B  2  245 ? 8.919   -37.651 5.152    1.00 55.62  ? 249  LEU   B HA   1 
ATOM   12756 H  HB2  . LEU   B  2  245 ? 9.736   -35.460 4.931    1.00 49.04  ? 249  LEU   B HB2  1 
ATOM   12757 H  HB3  . LEU   B  2  245 ? 11.013  -36.041 4.183    1.00 49.04  ? 249  LEU   B HB3  1 
ATOM   12758 H  HG   . LEU   B  2  245 ? 9.649   -36.711 2.407    1.00 53.07  ? 249  LEU   B HG   1 
ATOM   12759 H  HD11 . LEU   B  2  245 ? 7.421   -36.064 2.299    1.00 52.10  ? 249  LEU   B HD11 1 
ATOM   12760 H  HD12 . LEU   B  2  245 ? 7.652   -37.046 3.527    1.00 52.10  ? 249  LEU   B HD12 1 
ATOM   12761 H  HD13 . LEU   B  2  245 ? 7.518   -35.483 3.774    1.00 52.10  ? 249  LEU   B HD13 1 
ATOM   12762 H  HD21 . LEU   B  2  245 ? 9.229   -34.588 1.535    1.00 57.18  ? 249  LEU   B HD21 1 
ATOM   12763 H  HD22 . LEU   B  2  245 ? 9.389   -33.961 2.987    1.00 57.18  ? 249  LEU   B HD22 1 
ATOM   12764 H  HD23 . LEU   B  2  245 ? 10.644  -34.609 2.259    1.00 57.18  ? 249  LEU   B HD23 1 
ATOM   12765 N  N    . VAL   B  2  246 ? 9.681   -39.679 4.004    1.00 47.76  ? 250  VAL   B N    1 
ATOM   12766 C  CA   . VAL   B  2  246 ? 10.150  -40.890 3.344    1.00 45.57  ? 250  VAL   B CA   1 
ATOM   12767 C  C    . VAL   B  2  246 ? 9.732   -40.820 1.882    1.00 50.04  ? 250  VAL   B C    1 
ATOM   12768 O  O    . VAL   B  2  246 ? 8.556   -40.997 1.544    1.00 55.74  ? 250  VAL   B O    1 
ATOM   12769 C  CB   . VAL   B  2  246 ? 9.611   -42.153 4.025    1.00 46.93  ? 250  VAL   B CB   1 
ATOM   12770 C  CG1  . VAL   B  2  246 ? 10.258  -43.390 3.422    1.00 49.46  ? 250  VAL   B CG1  1 
ATOM   12771 C  CG2  . VAL   B  2  246 ? 9.867   -42.091 5.525    1.00 48.62  ? 250  VAL   B CG2  1 
ATOM   12772 H  H    . VAL   B  2  246 ? 8.847   -39.701 4.212    1.00 57.35  ? 250  VAL   B H    1 
ATOM   12773 H  HA   . VAL   B  2  246 ? 11.119  -40.916 3.379    1.00 54.73  ? 250  VAL   B HA   1 
ATOM   12774 H  HB   . VAL   B  2  246 ? 8.653   -42.210 3.883    1.00 56.35  ? 250  VAL   B HB   1 
ATOM   12775 H  HG11 . VAL   B  2  246 ? 9.942   -44.175 3.897    1.00 59.39  ? 250  VAL   B HG11 1 
ATOM   12776 H  HG12 . VAL   B  2  246 ? 10.013  -43.449 2.485    1.00 59.39  ? 250  VAL   B HG12 1 
ATOM   12777 H  HG13 . VAL   B  2  246 ? 11.221  -43.316 3.508    1.00 59.39  ? 250  VAL   B HG13 1 
ATOM   12778 H  HG21 . VAL   B  2  246 ? 9.559   -42.916 5.932    1.00 58.38  ? 250  VAL   B HG21 1 
ATOM   12779 H  HG22 . VAL   B  2  246 ? 10.818  -41.981 5.679    1.00 58.38  ? 250  VAL   B HG22 1 
ATOM   12780 H  HG23 . VAL   B  2  246 ? 9.382   -41.338 5.897    1.00 58.38  ? 250  VAL   B HG23 1 
ATOM   12781 N  N    . PHE   B  2  247 ? 10.708  -40.563 1.018    1.00 51.34  ? 251  PHE   B N    1 
ATOM   12782 C  CA   . PHE   B  2  247 ? 10.500  -40.442 -0.421   1.00 46.15  ? 251  PHE   B CA   1 
ATOM   12783 C  C    . PHE   B  2  247 ? 10.717  -41.813 -1.048   1.00 46.07  ? 251  PHE   B C    1 
ATOM   12784 O  O    . PHE   B  2  247 ? 11.843  -42.320 -1.076   1.00 50.30  ? 251  PHE   B O    1 
ATOM   12785 C  CB   . PHE   B  2  247 ? 11.462  -39.393 -0.976   1.00 43.75  ? 251  PHE   B CB   1 
ATOM   12786 C  CG   . PHE   B  2  247 ? 11.417  -39.235 -2.465   1.00 43.93  ? 251  PHE   B CG   1 
ATOM   12787 C  CD1  . PHE   B  2  247 ? 12.220  -40.012 -3.282   1.00 46.14  ? 251  PHE   B CD1  1 
ATOM   12788 C  CD2  . PHE   B  2  247 ? 10.602  -38.281 -3.047   1.00 45.33  ? 251  PHE   B CD2  1 
ATOM   12789 C  CE1  . PHE   B  2  247 ? 12.195  -39.855 -4.653   1.00 47.09  ? 251  PHE   B CE1  1 
ATOM   12790 C  CE2  . PHE   B  2  247 ? 10.574  -38.118 -4.413   1.00 45.25  ? 251  PHE   B CE2  1 
ATOM   12791 C  CZ   . PHE   B  2  247 ? 11.371  -38.906 -5.220   1.00 46.07  ? 251  PHE   B CZ   1 
ATOM   12792 H  H    . PHE   B  2  247 ? 11.528  -40.451 1.250    1.00 61.65  ? 251  PHE   B H    1 
ATOM   12793 H  HA   . PHE   B  2  247 ? 9.593   -40.166 -0.623   1.00 55.42  ? 251  PHE   B HA   1 
ATOM   12794 H  HB2  . PHE   B  2  247 ? 11.242  -38.534 -0.584   1.00 52.53  ? 251  PHE   B HB2  1 
ATOM   12795 H  HB3  . PHE   B  2  247 ? 12.367  -39.646 -0.736   1.00 52.53  ? 251  PHE   B HB3  1 
ATOM   12796 H  HD1  . PHE   B  2  247 ? 12.783  -40.647 -2.903   1.00 55.40  ? 251  PHE   B HD1  1 
ATOM   12797 H  HD2  . PHE   B  2  247 ? 10.067  -37.744 -2.509   1.00 54.43  ? 251  PHE   B HD2  1 
ATOM   12798 H  HE1  . PHE   B  2  247 ? 12.732  -40.389 -5.193   1.00 56.55  ? 251  PHE   B HE1  1 
ATOM   12799 H  HE2  . PHE   B  2  247 ? 10.018  -37.477 -4.794   1.00 54.33  ? 251  PHE   B HE2  1 
ATOM   12800 H  HZ   . PHE   B  2  247 ? 11.352  -38.797 -6.143   1.00 55.32  ? 251  PHE   B HZ   1 
ATOM   12801 N  N    . VAL   B  2  248 ? 9.640   -42.419 -1.541   1.00 47.84  ? 252  VAL   B N    1 
ATOM   12802 C  CA   . VAL   B  2  248 ? 9.660   -43.784 -2.057   1.00 49.02  ? 252  VAL   B CA   1 
ATOM   12803 C  C    . VAL   B  2  248 ? 9.428   -43.715 -3.559   1.00 46.66  ? 252  VAL   B C    1 
ATOM   12804 O  O    . VAL   B  2  248 ? 8.335   -43.358 -4.015   1.00 46.96  ? 252  VAL   B O    1 
ATOM   12805 C  CB   . VAL   B  2  248 ? 8.607   -44.668 -1.374   1.00 49.50  ? 252  VAL   B CB   1 
ATOM   12806 C  CG1  . VAL   B  2  248 ? 8.706   -46.103 -1.875   1.00 48.37  ? 252  VAL   B CG1  1 
ATOM   12807 C  CG2  . VAL   B  2  248 ? 8.774   -44.616 0.135    1.00 52.36  ? 252  VAL   B CG2  1 
ATOM   12808 H  H    . VAL   B  2  248 ? 8.865   -42.048 -1.589   1.00 57.44  ? 252  VAL   B H    1 
ATOM   12809 H  HA   . VAL   B  2  248 ? 10.536  -44.170 -1.901   1.00 58.86  ? 252  VAL   B HA   1 
ATOM   12810 H  HB   . VAL   B  2  248 ? 7.724   -44.333 -1.596   1.00 59.44  ? 252  VAL   B HB   1 
ATOM   12811 H  HG11 . VAL   B  2  248 ? 8.021   -46.636 -1.442   1.00 58.08  ? 252  VAL   B HG11 1 
ATOM   12812 H  HG12 . VAL   B  2  248 ? 8.575   -46.113 -2.836   1.00 58.08  ? 252  VAL   B HG12 1 
ATOM   12813 H  HG13 . VAL   B  2  248 ? 9.584   -46.453 -1.657   1.00 58.08  ? 252  VAL   B HG13 1 
ATOM   12814 H  HG21 . VAL   B  2  248 ? 8.096   -45.173 0.547    1.00 62.87  ? 252  VAL   B HG21 1 
ATOM   12815 H  HG22 . VAL   B  2  248 ? 9.657   -44.944 0.366    1.00 62.87  ? 252  VAL   B HG22 1 
ATOM   12816 H  HG23 . VAL   B  2  248 ? 8.674   -43.698 0.432    1.00 62.87  ? 252  VAL   B HG23 1 
ATOM   12817 N  N    . SER   B  2  249 ? 10.454  -44.065 -4.331   1.00 46.07  ? 253  SER   B N    1 
ATOM   12818 C  CA   . SER   B  2  249 ? 10.364  -44.041 -5.781   1.00 47.66  ? 253  SER   B CA   1 
ATOM   12819 C  C    . SER   B  2  249 ? 11.365  -45.030 -6.353   1.00 47.82  ? 253  SER   B C    1 
ATOM   12820 O  O    . SER   B  2  249 ? 12.293  -45.470 -5.671   1.00 49.53  ? 253  SER   B O    1 
ATOM   12821 C  CB   . SER   B  2  249 ? 10.632  -42.639 -6.342   1.00 47.35  ? 253  SER   B CB   1 
ATOM   12822 O  OG   . SER   B  2  249 ? 10.559  -42.639 -7.757   1.00 49.01  ? 253  SER   B OG   1 
ATOM   12823 H  H    . SER   B  2  249 ? 11.218  -44.323 -4.032   1.00 55.32  ? 253  SER   B H    1 
ATOM   12824 H  HA   . SER   B  2  249 ? 9.472   -44.313 -6.049   1.00 57.23  ? 253  SER   B HA   1 
ATOM   12825 H  HB2  . SER   B  2  249 ? 9.966   -42.027 -5.991   1.00 56.85  ? 253  SER   B HB2  1 
ATOM   12826 H  HB3  . SER   B  2  249 ? 11.519  -42.356 -6.071   1.00 56.85  ? 253  SER   B HB3  1 
ATOM   12827 H  HG   . SER   B  2  249 ? 9.805   -42.915 -8.005   1.00 58.85  ? 253  SER   B HG   1 
ATOM   12828 N  N    . ASP   B  2  250 ? 11.163  -45.381 -7.618   1.00 45.83  ? 254  ASP   B N    1 
ATOM   12829 C  CA   . ASP   B  2  250 ? 12.091  -46.219 -8.361   1.00 49.23  ? 254  ASP   B CA   1 
ATOM   12830 C  C    . ASP   B  2  250 ? 12.560  -45.508 -9.625   1.00 47.32  ? 254  ASP   B C    1 
ATOM   12831 O  O    . ASP   B  2  250 ? 12.733  -46.126 -10.676  1.00 47.72  ? 254  ASP   B O    1 
ATOM   12832 C  CB   . ASP   B  2  250 ? 11.457  -47.567 -8.705   1.00 53.22  ? 254  ASP   B CB   1 
ATOM   12833 C  CG   . ASP   B  2  250 ? 10.325  -47.449 -9.713   1.00 59.85  ? 254  ASP   B CG   1 
ATOM   12834 O  OD1  . ASP   B  2  250 ? 9.974   -46.315 -10.102  1.00 59.49  ? 254  ASP   B OD1  1 
ATOM   12835 O  OD2  . ASP   B  2  250 ? 9.785   -48.499 -10.121  1.00 63.30  ? 254  ASP   B OD2  1 
ATOM   12836 H  H    . ASP   B  2  250 ? 10.477  -45.138 -8.077   1.00 55.03  ? 254  ASP   B H    1 
ATOM   12837 H  HA   . ASP   B  2  250 ? 12.868  -46.390 -7.806   1.00 59.11  ? 254  ASP   B HA   1 
ATOM   12838 H  HB2  . ASP   B  2  250 ? 12.136  -48.148 -9.083   1.00 63.91  ? 254  ASP   B HB2  1 
ATOM   12839 H  HB3  . ASP   B  2  250 ? 11.096  -47.961 -7.895   1.00 63.91  ? 254  ASP   B HB3  1 
ATOM   12840 N  N    . ALA   B  2  251 ? 12.770  -44.194 -9.544   1.00 47.47  ? 255  ALA   B N    1 
ATOM   12841 C  CA   . ALA   B  2  251 ? 13.056  -43.438 -10.752  1.00 50.74  ? 255  ALA   B CA   1 
ATOM   12842 C  C    . ALA   B  2  251 ? 13.839  -42.170 -10.446  1.00 54.55  ? 255  ALA   B C    1 
ATOM   12843 O  O    . ALA   B  2  251 ? 13.863  -41.674 -9.316   1.00 52.73  ? 255  ALA   B O    1 
ATOM   12844 C  CB   . ALA   B  2  251 ? 11.765  -43.071 -11.493  1.00 50.81  ? 255  ALA   B CB   1 
ATOM   12845 H  H    . ALA   B  2  251 ? 12.753  -43.734 -8.817   1.00 57.00  ? 255  ALA   B H    1 
ATOM   12846 H  HA   . ALA   B  2  251 ? 13.620  -43.993 -11.312  1.00 60.93  ? 255  ALA   B HA   1 
ATOM   12847 H  HB1  . ALA   B  2  251 ? 11.991  -42.721 -12.369  1.00 61.01  ? 255  ALA   B HB1  1 
ATOM   12848 H  HB2  . ALA   B  2  251 ? 11.217  -43.866 -11.586  1.00 61.01  ? 255  ALA   B HB2  1 
ATOM   12849 H  HB3  . ALA   B  2  251 ? 11.288  -42.398 -10.981  1.00 61.01  ? 255  ALA   B HB3  1 
ATOM   12850 N  N    . ASP   B  2  252 ? 14.483  -41.665 -11.499  1.00 61.99  ? 256  ASP   B N    1 
ATOM   12851 C  CA   . ASP   B  2  252 ? 15.137  -40.363 -11.542  1.00 66.03  ? 256  ASP   B CA   1 
ATOM   12852 C  C    . ASP   B  2  252 ? 14.182  -39.261 -11.095  1.00 56.26  ? 256  ASP   B C    1 
ATOM   12853 O  O    . ASP   B  2  252 ? 12.971  -39.485 -11.018  1.00 58.45  ? 256  ASP   B O    1 
ATOM   12854 C  CB   . ASP   B  2  252 ? 15.628  -40.114 -12.973  1.00 79.25  ? 256  ASP   B CB   1 
ATOM   12855 C  CG   . ASP   B  2  252 ? 16.852  -39.225 -13.038  1.00 95.15  ? 256  ASP   B CG   1 
ATOM   12856 O  OD1  . ASP   B  2  252 ? 17.219  -38.622 -12.010  1.00 103.63 ? 256  ASP   B OD1  1 
ATOM   12857 O  OD2  . ASP   B  2  252 ? 17.452  -39.134 -14.130  1.00 102.33 ? 256  ASP   B OD2  1 
ATOM   12858 H  H    . ASP   B  2  252 ? 14.558  -42.084 -12.246  1.00 74.43  ? 256  ASP   B H    1 
ATOM   12859 H  HA   . ASP   B  2  252 ? 15.895  -40.343 -10.937  1.00 79.27  ? 256  ASP   B HA   1 
ATOM   12860 H  HB2  . ASP   B  2  252 ? 15.856  -40.964 -13.380  1.00 95.13  ? 256  ASP   B HB2  1 
ATOM   12861 H  HB3  . ASP   B  2  252 ? 14.921  -39.684 -13.478  1.00 95.13  ? 256  ASP   B HB3  1 
ATOM   12862 N  N    . SER   B  2  253 ? 14.703  -38.067 -10.803  1.00 46.99  ? 257  SER   B N    1 
ATOM   12863 C  CA   . SER   B  2  253 ? 13.873  -36.940 -10.389  1.00 48.80  ? 257  SER   B CA   1 
ATOM   12864 C  C    . SER   B  2  253 ? 14.136  -35.732 -11.276  1.00 50.90  ? 257  SER   B C    1 
ATOM   12865 O  O    . SER   B  2  253 ? 15.291  -35.353 -11.493  1.00 51.65  ? 257  SER   B O    1 
ATOM   12866 C  CB   . SER   B  2  253 ? 14.128  -36.560 -8.925   1.00 49.56  ? 257  SER   B CB   1 
ATOM   12867 O  OG   . SER   B  2  253 ? 13.612  -37.534 -8.038   1.00 51.94  ? 257  SER   B OG   1 
ATOM   12868 H  H    . SER   B  2  253 ? 15.543  -37.886 -10.838  1.00 56.43  ? 257  SER   B H    1 
ATOM   12869 H  HA   . SER   B  2  253 ? 12.944  -37.198 -10.495  1.00 58.59  ? 257  SER   B HA   1 
ATOM   12870 H  HB2  . SER   B  2  253 ? 15.085  -36.483 -8.784   1.00 59.50  ? 257  SER   B HB2  1 
ATOM   12871 H  HB3  . SER   B  2  253 ? 13.697  -35.711 -8.743   1.00 59.50  ? 257  SER   B HB3  1 
ATOM   12872 H  HG   . SER   B  2  253 ? 14.181  -38.139 -7.913   1.00 62.37  ? 257  SER   B HG   1 
ATOM   12873 N  N    . HIS   B  2  254 ? 13.060  -35.129 -11.778  1.00 51.38  ? 258  HIS   B N    1 
ATOM   12874 C  CA   . HIS   B  2  254 ? 13.162  -33.837 -12.441  1.00 47.62  ? 258  HIS   B CA   1 
ATOM   12875 C  C    . HIS   B  2  254 ? 13.606  -32.774 -11.443  1.00 43.47  ? 258  HIS   B C    1 
ATOM   12876 O  O    . HIS   B  2  254 ? 13.309  -32.850 -10.248  1.00 42.57  ? 258  HIS   B O    1 
ATOM   12877 C  CB   . HIS   B  2  254 ? 11.816  -33.439 -13.050  1.00 44.35  ? 258  HIS   B CB   1 
ATOM   12878 C  CG   . HIS   B  2  254 ? 11.595  -33.959 -14.436  1.00 43.63  ? 258  HIS   B CG   1 
ATOM   12879 N  ND1  . HIS   B  2  254 ? 12.568  -33.919 -15.412  1.00 43.55  ? 258  HIS   B ND1  1 
ATOM   12880 C  CD2  . HIS   B  2  254 ? 10.507  -34.522 -15.013  1.00 43.01  ? 258  HIS   B CD2  1 
ATOM   12881 C  CE1  . HIS   B  2  254 ? 12.090  -34.439 -16.529  1.00 45.24  ? 258  HIS   B CE1  1 
ATOM   12882 N  NE2  . HIS   B  2  254 ? 10.842  -34.813 -16.314  1.00 43.54  ? 258  HIS   B NE2  1 
ATOM   12883 H  H    . HIS   B  2  254 ? 12.262  -35.448 -11.747  1.00 61.70  ? 258  HIS   B H    1 
ATOM   12884 H  HA   . HIS   B  2  254 ? 13.814  -33.891 -13.157  1.00 57.18  ? 258  HIS   B HA   1 
ATOM   12885 H  HB2  . HIS   B  2  254 ? 11.106  -33.786 -12.489  1.00 53.26  ? 258  HIS   B HB2  1 
ATOM   12886 H  HB3  . HIS   B  2  254 ? 11.766  -32.471 -13.088  1.00 53.26  ? 258  HIS   B HB3  1 
ATOM   12887 H  HD1  . HIS   B  2  254 ? 13.363  -33.606 -15.309  1.00 52.29  ? 258  HIS   B HD1  1 
ATOM   12888 H  HD2  . HIS   B  2  254 ? 9.687   -34.682 -14.605  1.00 51.65  ? 258  HIS   B HD2  1 
ATOM   12889 H  HE1  . HIS   B  2  254 ? 12.554  -34.526 -17.330  1.00 54.33  ? 258  HIS   B HE1  1 
ATOM   12890 H  HE2  . HIS   B  2  254 ? 10.323  -35.179 -16.893  1.00 52.28  ? 258  HIS   B HE2  1 
ATOM   12891 N  N    . PHE   B  2  255 ? 14.321  -31.768 -11.942  1.00 42.94  ? 259  PHE   B N    1 
ATOM   12892 C  CA   . PHE   B  2  255 ? 14.764  -30.674 -11.090  1.00 41.95  ? 259  PHE   B CA   1 
ATOM   12893 C  C    . PHE   B  2  255 ? 14.855  -29.391 -11.901  1.00 42.10  ? 259  PHE   B C    1 
ATOM   12894 O  O    . PHE   B  2  255 ? 15.079  -29.414 -13.114  1.00 42.57  ? 259  PHE   B O    1 
ATOM   12895 C  CB   . PHE   B  2  255 ? 16.119  -30.978 -10.436  1.00 43.76  ? 259  PHE   B CB   1 
ATOM   12896 C  CG   . PHE   B  2  255 ? 17.236  -31.194 -11.418  1.00 47.98  ? 259  PHE   B CG   1 
ATOM   12897 C  CD1  . PHE   B  2  255 ? 17.426  -32.432 -12.008  1.00 49.86  ? 259  PHE   B CD1  1 
ATOM   12898 C  CD2  . PHE   B  2  255 ? 18.103  -30.163 -11.742  1.00 50.46  ? 259  PHE   B CD2  1 
ATOM   12899 C  CE1  . PHE   B  2  255 ? 18.455  -32.635 -12.907  1.00 51.38  ? 259  PHE   B CE1  1 
ATOM   12900 C  CE2  . PHE   B  2  255 ? 19.133  -30.362 -12.643  1.00 53.34  ? 259  PHE   B CE2  1 
ATOM   12901 C  CZ   . PHE   B  2  255 ? 19.309  -31.600 -13.225  1.00 53.33  ? 259  PHE   B CZ   1 
ATOM   12902 H  H    . PHE   B  2  255 ? 14.559  -31.698 -12.765  1.00 51.56  ? 259  PHE   B H    1 
ATOM   12903 H  HA   . PHE   B  2  255 ? 14.106  -30.539 -10.391  1.00 50.38  ? 259  PHE   B HA   1 
ATOM   12904 H  HB2  . PHE   B  2  255 ? 16.365  -30.231 -9.868   1.00 52.55  ? 259  PHE   B HB2  1 
ATOM   12905 H  HB3  . PHE   B  2  255 ? 16.034  -31.784 -9.903   1.00 52.55  ? 259  PHE   B HB3  1 
ATOM   12906 H  HD1  . PHE   B  2  255 ? 16.855  -33.134 -11.797  1.00 59.87  ? 259  PHE   B HD1  1 
ATOM   12907 H  HD2  . PHE   B  2  255 ? 17.990  -29.327 -11.350  1.00 60.59  ? 259  PHE   B HD2  1 
ATOM   12908 H  HE1  . PHE   B  2  255 ? 18.572  -33.471 -13.298  1.00 61.69  ? 259  PHE   B HE1  1 
ATOM   12909 H  HE2  . PHE   B  2  255 ? 19.707  -29.662 -12.856  1.00 64.05  ? 259  PHE   B HE2  1 
ATOM   12910 H  HZ   . PHE   B  2  255 ? 20.001  -31.736 -13.831  1.00 64.03  ? 259  PHE   B HZ   1 
ATOM   12911 N  N    . GLY   B  2  256 ? 14.664  -28.270 -11.207  1.00 39.23  ? 260  GLY   B N    1 
ATOM   12912 C  CA   . GLY   B  2  256 ? 14.861  -26.951 -11.774  1.00 43.28  ? 260  GLY   B CA   1 
ATOM   12913 C  C    . GLY   B  2  256 ? 14.190  -26.700 -13.108  1.00 46.37  ? 260  GLY   B C    1 
ATOM   12914 O  O    . GLY   B  2  256 ? 12.965  -26.797 -13.232  1.00 45.10  ? 260  GLY   B O    1 
ATOM   12915 H  H    . GLY   B  2  256 ? 14.414  -28.253 -10.385  1.00 47.12  ? 260  GLY   B H    1 
ATOM   12916 H  HA2  . GLY   B  2  256 ? 14.518  -26.294 -11.148  1.00 51.98  ? 260  GLY   B HA2  1 
ATOM   12917 H  HA3  . GLY   B  2  256 ? 15.812  -26.807 -11.894  1.00 51.98  ? 260  GLY   B HA3  1 
ATOM   12918 N  N    . MET   B  2  257 ? 14.996  -26.373 -14.117  1.00 44.97  ? 261  MET   B N    1 
ATOM   12919 C  CA   . MET   B  2  257 ? 14.499  -25.896 -15.398  1.00 45.58  ? 261  MET   B CA   1 
ATOM   12920 C  C    . MET   B  2  257 ? 14.173  -27.016 -16.377  1.00 42.60  ? 261  MET   B C    1 
ATOM   12921 O  O    . MET   B  2  257 ? 13.999  -26.744 -17.569  1.00 42.21  ? 261  MET   B O    1 
ATOM   12922 C  CB   . MET   B  2  257 ? 15.517  -24.943 -16.032  1.00 49.64  ? 261  MET   B CB   1 
ATOM   12923 C  CG   . MET   B  2  257 ? 15.722  -23.654 -15.252  1.00 52.41  ? 261  MET   B CG   1 
ATOM   12924 S  SD   . MET   B  2  257 ? 16.857  -23.834 -13.863  1.00 54.87  ? 261  MET   B SD   1 
ATOM   12925 C  CE   . MET   B  2  257 ? 18.432  -23.805 -14.714  1.00 56.67  ? 261  MET   B CE   1 
ATOM   12926 H  H    . MET   B  2  257 ? 15.854  -26.422 -14.080  1.00 54.00  ? 261  MET   B H    1 
ATOM   12927 H  HA   . MET   B  2  257 ? 13.684  -25.398 -15.229  1.00 54.73  ? 261  MET   B HA   1 
ATOM   12928 H  HB2  . MET   B  2  257 ? 16.373  -25.395 -16.088  1.00 59.61  ? 261  MET   B HB2  1 
ATOM   12929 H  HB3  . MET   B  2  257 ? 15.209  -24.705 -16.921  1.00 59.61  ? 261  MET   B HB3  1 
ATOM   12930 H  HG2  . MET   B  2  257 ? 16.086  -22.981 -15.848  1.00 62.93  ? 261  MET   B HG2  1 
ATOM   12931 H  HG3  . MET   B  2  257 ? 14.867  -23.360 -14.901  1.00 62.93  ? 261  MET   B HG3  1 
ATOM   12932 H  HE1  . MET   B  2  257 ? 19.145  -23.882 -14.061  1.00 68.04  ? 261  MET   B HE1  1 
ATOM   12933 H  HE2  . MET   B  2  257 ? 18.470  -24.550 -15.334  1.00 68.04  ? 261  MET   B HE2  1 
ATOM   12934 H  HE3  . MET   B  2  257 ? 18.515  -22.968 -15.197  1.00 68.04  ? 261  MET   B HE3  1 
ATOM   12935 N  N    . ASP   B  2  258 ? 14.088  -28.266 -15.915  1.00 41.96  ? 262  ASP   B N    1 
ATOM   12936 C  CA   . ASP   B  2  258 ? 13.541  -29.310 -16.773  1.00 43.42  ? 262  ASP   B CA   1 
ATOM   12937 C  C    . ASP   B  2  258 ? 12.172  -28.906 -17.302  1.00 47.93  ? 262  ASP   B C    1 
ATOM   12938 O  O    . ASP   B  2  258 ? 11.820  -29.232 -18.441  1.00 49.28  ? 262  ASP   B O    1 
ATOM   12939 C  CB   . ASP   B  2  258 ? 13.437  -30.633 -16.012  1.00 43.80  ? 262  ASP   B CB   1 
ATOM   12940 C  CG   . ASP   B  2  258 ? 14.786  -31.283 -15.781  1.00 45.85  ? 262  ASP   B CG   1 
ATOM   12941 O  OD1  . ASP   B  2  258 ? 15.805  -30.717 -16.227  1.00 48.96  ? 262  ASP   B OD1  1 
ATOM   12942 O  OD2  . ASP   B  2  258 ? 14.826  -32.363 -15.155  1.00 44.76  ? 262  ASP   B OD2  1 
ATOM   12943 H  H    . ASP   B  2  258 ? 14.333  -28.525 -15.133  1.00 50.39  ? 262  ASP   B H    1 
ATOM   12944 H  HA   . ASP   B  2  258 ? 14.142  -29.452 -17.521  1.00 52.14  ? 262  ASP   B HA   1 
ATOM   12945 H  HB2  . ASP   B  2  258 ? 13.030  -30.469 -15.147  1.00 52.60  ? 262  ASP   B HB2  1 
ATOM   12946 H  HB3  . ASP   B  2  258 ? 12.890  -31.250 -16.524  1.00 52.60  ? 262  ASP   B HB3  1 
ATOM   12947 N  N    . SER   B  2  259 ? 11.399  -28.179 -16.493  1.00 47.62  ? 263  SER   B N    1 
ATOM   12948 C  CA   . SER   B  2  259 ? 10.058  -27.755 -16.873  1.00 46.03  ? 263  SER   B CA   1 
ATOM   12949 C  C    . SER   B  2  259 ? 10.051  -26.794 -18.053  1.00 43.46  ? 263  SER   B C    1 
ATOM   12950 O  O    . SER   B  2  259 ? 8.976   -26.519 -18.597  1.00 48.75  ? 263  SER   B O    1 
ATOM   12951 C  CB   . SER   B  2  259 ? 9.373   -27.100 -15.672  1.00 49.32  ? 263  SER   B CB   1 
ATOM   12952 O  OG   . SER   B  2  259 ? 10.037  -25.905 -15.296  1.00 51.27  ? 263  SER   B OG   1 
ATOM   12953 H  H    . SER   B  2  259 ? 11.633  -27.915 -15.708  1.00 57.18  ? 263  SER   B H    1 
ATOM   12954 H  HA   . SER   B  2  259 ? 9.547   -28.537 -17.132  1.00 55.27  ? 263  SER   B HA   1 
ATOM   12955 H  HB2  . SER   B  2  259 ? 8.456   -26.890 -15.908  1.00 59.22  ? 263  SER   B HB2  1 
ATOM   12956 H  HB3  . SER   B  2  259 ? 9.389   -27.718 -14.924  1.00 59.22  ? 263  SER   B HB3  1 
ATOM   12957 H  HG   . SER   B  2  259 ? 9.915   -25.313 -15.879  1.00 61.56  ? 263  SER   B HG   1 
ATOM   12958 N  N    . LYS   B  2  260 ? 11.212  -26.272 -18.456  1.00 43.45  ? 264  LYS   B N    1 
ATOM   12959 C  CA   . LYS   B  2  260 ? 11.260  -25.368 -19.601  1.00 43.89  ? 264  LYS   B CA   1 
ATOM   12960 C  C    . LYS   B  2  260 ? 10.741  -26.040 -20.865  1.00 42.58  ? 264  LYS   B C    1 
ATOM   12961 O  O    . LYS   B  2  260 ? 10.174  -25.369 -21.735  1.00 40.13  ? 264  LYS   B O    1 
ATOM   12962 C  CB   . LYS   B  2  260 ? 12.692  -24.876 -19.804  1.00 39.57  ? 264  LYS   B CB   1 
ATOM   12963 C  CG   . LYS   B  2  260 ? 12.889  -23.907 -20.954  1.00 41.88  ? 264  LYS   B CG   1 
ATOM   12964 C  CD   . LYS   B  2  260 ? 14.337  -23.447 -20.977  1.00 47.80  ? 264  LYS   B CD   1 
ATOM   12965 C  CE   . LYS   B  2  260 ? 14.719  -22.757 -22.272  1.00 53.41  ? 264  LYS   B CE   1 
ATOM   12966 N  NZ   . LYS   B  2  260 ? 14.275  -21.341 -22.308  1.00 58.73  ? 264  LYS   B NZ   1 
ATOM   12967 H  H    . LYS   B  2  260 ? 11.974  -26.424 -18.088  1.00 52.18  ? 264  LYS   B H    1 
ATOM   12968 H  HA   . LYS   B  2  260 ? 10.697  -24.598 -19.424  1.00 52.70  ? 264  LYS   B HA   1 
ATOM   12969 H  HB2  . LYS   B  2  260 ? 12.977  -24.426 -18.994  1.00 47.52  ? 264  LYS   B HB2  1 
ATOM   12970 H  HB3  . LYS   B  2  260 ? 13.258  -25.645 -19.973  1.00 47.52  ? 264  LYS   B HB3  1 
ATOM   12971 H  HG2  . LYS   B  2  260 ? 12.686  -24.347 -21.795  1.00 50.29  ? 264  LYS   B HG2  1 
ATOM   12972 H  HG3  . LYS   B  2  260 ? 12.315  -23.134 -20.837  1.00 50.29  ? 264  LYS   B HG3  1 
ATOM   12973 H  HD2  . LYS   B  2  260 ? 14.480  -22.819 -20.251  1.00 57.39  ? 264  LYS   B HD2  1 
ATOM   12974 H  HD3  . LYS   B  2  260 ? 14.915  -24.218 -20.867  1.00 57.39  ? 264  LYS   B HD3  1 
ATOM   12975 H  HE2  . LYS   B  2  260 ? 15.684  -22.774 -22.369  1.00 64.13  ? 264  LYS   B HE2  1 
ATOM   12976 H  HE3  . LYS   B  2  260 ? 14.303  -23.223 -23.015  1.00 64.13  ? 264  LYS   B HE3  1 
ATOM   12977 H  HZ1  . LYS   B  2  260 ? 14.793  -20.872 -22.859  1.00 70.51  ? 264  LYS   B HZ1  1 
ATOM   12978 H  HZ2  . LYS   B  2  260 ? 13.433  -21.292 -22.592  1.00 70.51  ? 264  LYS   B HZ2  1 
ATOM   12979 H  HZ3  . LYS   B  2  260 ? 14.325  -20.986 -21.493  1.00 70.51  ? 264  LYS   B HZ3  1 
ATOM   12980 N  N    . LEU   B  2  261 ? 10.925  -27.357 -20.987  1.00 39.31  ? 265  LEU   B N    1 
ATOM   12981 C  CA   . LEU   B  2  261 ? 10.375  -28.072 -22.133  1.00 40.16  ? 265  LEU   B CA   1 
ATOM   12982 C  C    . LEU   B  2  261 ? 8.869   -27.869 -22.233  1.00 41.67  ? 265  LEU   B C    1 
ATOM   12983 O  O    . LEU   B  2  261 ? 8.320   -27.759 -23.336  1.00 43.93  ? 265  LEU   B O    1 
ATOM   12984 C  CB   . LEU   B  2  261 ? 10.700  -29.563 -22.035  1.00 43.16  ? 265  LEU   B CB   1 
ATOM   12985 C  CG   . LEU   B  2  261 ? 12.172  -29.978 -21.976  1.00 50.73  ? 265  LEU   B CG   1 
ATOM   12986 C  CD1  . LEU   B  2  261 ? 12.294  -31.481 -22.147  1.00 54.41  ? 265  LEU   B CD1  1 
ATOM   12987 C  CD2  . LEU   B  2  261 ? 12.992  -29.259 -23.027  1.00 56.30  ? 265  LEU   B CD2  1 
ATOM   12988 H  H    . LEU   B  2  261 ? 11.356  -27.850 -20.429  1.00 47.21  ? 265  LEU   B H    1 
ATOM   12989 H  HA   . LEU   B  2  261 ? 10.788  -27.726 -22.940  1.00 48.23  ? 265  LEU   B HA   1 
ATOM   12990 H  HB2  . LEU   B  2  261 ? 10.283  -29.902 -21.227  1.00 51.82  ? 265  LEU   B HB2  1 
ATOM   12991 H  HB3  . LEU   B  2  261 ? 10.319  -29.999 -22.813  1.00 51.82  ? 265  LEU   B HB3  1 
ATOM   12992 H  HG   . LEU   B  2  261 ? 12.530  -29.729 -21.109  1.00 60.91  ? 265  LEU   B HG   1 
ATOM   12993 H  HD11 . LEU   B  2  261 ? 13.233  -31.725 -22.137  1.00 65.33  ? 265  LEU   B HD11 1 
ATOM   12994 H  HD12 . LEU   B  2  261 ? 11.831  -31.921 -21.417  1.00 65.33  ? 265  LEU   B HD12 1 
ATOM   12995 H  HD13 . LEU   B  2  261 ? 11.895  -31.736 -22.994  1.00 65.33  ? 265  LEU   B HD13 1 
ATOM   12996 H  HD21 . LEU   B  2  261 ? 13.910  -29.571 -22.979  1.00 67.59  ? 265  LEU   B HD21 1 
ATOM   12997 H  HD22 . LEU   B  2  261 ? 12.623  -29.453 -23.903  1.00 67.59  ? 265  LEU   B HD22 1 
ATOM   12998 H  HD23 . LEU   B  2  261 ? 12.958  -28.305 -22.857  1.00 67.59  ? 265  LEU   B HD23 1 
ATOM   12999 N  N    . ALA   B  2  262 ? 8.187   -27.812 -21.092  1.00 40.43  ? 266  ALA   B N    1 
ATOM   13000 C  CA   . ALA   B  2  262 ? 6.739   -27.682 -21.047  1.00 42.27  ? 266  ALA   B CA   1 
ATOM   13001 C  C    . ALA   B  2  262 ? 6.270   -26.233 -21.101  1.00 47.70  ? 266  ALA   B C    1 
ATOM   13002 O  O    . ALA   B  2  262 ? 5.069   -25.979 -20.960  1.00 50.92  ? 266  ALA   B O    1 
ATOM   13003 C  CB   . ALA   B  2  262 ? 6.195   -28.349 -19.780  1.00 39.69  ? 266  ALA   B CB   1 
ATOM   13004 H  H    . ALA   B  2  262 ? 8.551   -27.849 -20.314  1.00 48.55  ? 266  ALA   B H    1 
ATOM   13005 H  HA   . ALA   B  2  262 ? 6.367   -28.141 -21.816  1.00 50.76  ? 266  ALA   B HA   1 
ATOM   13006 H  HB1  . ALA   B  2  262 ? 5.229   -28.269 -19.770  1.00 47.67  ? 266  ALA   B HB1  1 
ATOM   13007 H  HB2  . ALA   B  2  262 ? 6.449   -29.286 -19.783  1.00 47.67  ? 266  ALA   B HB2  1 
ATOM   13008 H  HB3  . ALA   B  2  262 ? 6.572   -27.907 -19.004  1.00 47.67  ? 266  ALA   B HB3  1 
ATOM   13009 N  N    . GLY   B  2  263 ? 7.179   -25.283 -21.301  1.00 47.52  ? 267  GLY   B N    1 
ATOM   13010 C  CA   . GLY   B  2  263 ? 6.813   -23.882 -21.306  1.00 49.77  ? 267  GLY   B CA   1 
ATOM   13011 C  C    . GLY   B  2  263 ? 6.685   -23.255 -19.938  1.00 52.30  ? 267  GLY   B C    1 
ATOM   13012 O  O    . GLY   B  2  263 ? 6.143   -22.150 -19.828  1.00 55.29  ? 267  GLY   B O    1 
ATOM   13013 H  H    . GLY   B  2  263 ? 8.016   -25.430 -21.437  1.00 57.06  ? 267  GLY   B H    1 
ATOM   13014 H  HA2  . GLY   B  2  263 ? 7.487   -23.386 -21.797  1.00 59.76  ? 267  GLY   B HA2  1 
ATOM   13015 H  HA3  . GLY   B  2  263 ? 5.959   -23.786 -21.757  1.00 59.76  ? 267  GLY   B HA3  1 
ATOM   13016 N  N    . ILE   B  2  264 ? 7.163   -23.923 -18.893  1.00 50.76  ? 268  ILE   B N    1 
ATOM   13017 C  CA   . ILE   B  2  264 ? 7.097   -23.421 -17.525  1.00 49.82  ? 268  ILE   B CA   1 
ATOM   13018 C  C    . ILE   B  2  264 ? 8.455   -22.816 -17.191  1.00 47.91  ? 268  ILE   B C    1 
ATOM   13019 O  O    . ILE   B  2  264 ? 9.470   -23.523 -17.180  1.00 47.42  ? 268  ILE   B O    1 
ATOM   13020 C  CB   . ILE   B  2  264 ? 6.724   -24.541 -16.540  1.00 49.84  ? 268  ILE   B CB   1 
ATOM   13021 C  CG1  . ILE   B  2  264 ? 5.392   -25.182 -16.946  1.00 48.65  ? 268  ILE   B CG1  1 
ATOM   13022 C  CG2  . ILE   B  2  264 ? 6.647   -24.005 -15.117  1.00 51.84  ? 268  ILE   B CG2  1 
ATOM   13023 C  CD1  . ILE   B  2  264 ? 5.034   -26.432 -16.159  1.00 46.45  ? 268  ILE   B CD1  1 
ATOM   13024 H  H    . ILE   B  2  264 ? 7.542   -24.693 -18.953  1.00 60.95  ? 268  ILE   B H    1 
ATOM   13025 H  HA   . ILE   B  2  264 ? 6.425   -22.725 -17.459  1.00 59.82  ? 268  ILE   B HA   1 
ATOM   13026 H  HB   . ILE   B  2  264 ? 7.418   -25.219 -16.572  1.00 59.84  ? 268  ILE   B HB   1 
ATOM   13027 H  HG12 . ILE   B  2  264 ? 4.682   -24.535 -16.809  1.00 58.42  ? 268  ILE   B HG12 1 
ATOM   13028 H  HG13 . ILE   B  2  264 ? 5.439   -25.429 -17.883  1.00 58.42  ? 268  ILE   B HG13 1 
ATOM   13029 H  HG21 . ILE   B  2  264 ? 6.445   -24.737 -14.514  1.00 62.25  ? 268  ILE   B HG21 1 
ATOM   13030 H  HG22 . ILE   B  2  264 ? 7.501   -23.609 -14.882  1.00 62.25  ? 268  ILE   B HG22 1 
ATOM   13031 H  HG23 . ILE   B  2  264 ? 5.947   -23.335 -15.070  1.00 62.25  ? 268  ILE   B HG23 1 
ATOM   13032 H  HD11 . ILE   B  2  264 ? 4.191   -26.782 -16.487  1.00 55.78  ? 268  ILE   B HD11 1 
ATOM   13033 H  HD12 . ILE   B  2  264 ? 5.735   -27.092 -16.278  1.00 55.78  ? 268  ILE   B HD12 1 
ATOM   13034 H  HD13 . ILE   B  2  264 ? 4.953   -26.201 -15.220  1.00 55.78  ? 268  ILE   B HD13 1 
ATOM   13035 N  N    . VAL   B  2  265 ? 8.478   -21.511 -16.918  1.00 45.90  ? 269  VAL   B N    1 
ATOM   13036 C  CA   . VAL   B  2  265 ? 9.737   -20.790 -16.765  1.00 45.15  ? 269  VAL   B CA   1 
ATOM   13037 C  C    . VAL   B  2  265 ? 9.648   -19.743 -15.662  1.00 49.60  ? 269  VAL   B C    1 
ATOM   13038 O  O    . VAL   B  2  265 ? 10.346  -18.724 -15.707  1.00 55.85  ? 269  VAL   B O    1 
ATOM   13039 C  CB   . VAL   B  2  265 ? 10.149  -20.129 -18.094  1.00 44.09  ? 269  VAL   B CB   1 
ATOM   13040 C  CG1  . VAL   B  2  265 ? 10.524  -21.185 -19.118  1.00 43.44  ? 269  VAL   B CG1  1 
ATOM   13041 C  CG2  . VAL   B  2  265 ? 9.022   -19.245 -18.616  1.00 43.39  ? 269  VAL   B CG2  1 
ATOM   13042 H  H    . VAL   B  2  265 ? 7.777   -21.022 -16.819  1.00 55.12  ? 269  VAL   B H    1 
ATOM   13043 H  HA   . VAL   B  2  265 ? 10.410  -21.433 -16.493  1.00 54.22  ? 269  VAL   B HA   1 
ATOM   13044 H  HB   . VAL   B  2  265 ? 10.926  -19.569 -17.943  1.00 52.94  ? 269  VAL   B HB   1 
ATOM   13045 H  HG11 . VAL   B  2  265 ? 10.835  -20.747 -19.925  1.00 52.16  ? 269  VAL   B HG11 1 
ATOM   13046 H  HG12 . VAL   B  2  265 ? 11.229  -21.743 -18.752  1.00 52.16  ? 269  VAL   B HG12 1 
ATOM   13047 H  HG13 . VAL   B  2  265 ? 9.743   -21.726 -19.314  1.00 52.16  ? 269  VAL   B HG13 1 
ATOM   13048 H  HG21 . VAL   B  2  265 ? 9.305   -18.828 -19.445  1.00 52.11  ? 269  VAL   B HG21 1 
ATOM   13049 H  HG22 . VAL   B  2  265 ? 8.238   -19.794 -18.773  1.00 52.11  ? 269  VAL   B HG22 1 
ATOM   13050 H  HG23 . VAL   B  2  265 ? 8.822   -18.565 -17.955  1.00 52.11  ? 269  VAL   B HG23 1 
ATOM   13051 N  N    . CYS   B  2  266 ? 8.795   -19.979 -14.669  1.00 48.40  ? 270  CYS   B N    1 
ATOM   13052 C  CA   . CYS   B  2  266 ? 8.746   -19.130 -13.486  1.00 54.36  ? 270  CYS   B CA   1 
ATOM   13053 C  C    . CYS   B  2  266 ? 9.246   -19.938 -12.298  1.00 54.10  ? 270  CYS   B C    1 
ATOM   13054 O  O    . CYS   B  2  266 ? 8.629   -20.957 -11.954  1.00 53.97  ? 270  CYS   B O    1 
ATOM   13055 C  CB   . CYS   B  2  266 ? 7.328   -18.614 -13.241  1.00 59.63  ? 270  CYS   B CB   1 
ATOM   13056 S  SG   . CYS   B  2  266 ? 6.605   -17.835 -14.711  1.00 71.58  ? 270  CYS   B SG   1 
ATOM   13057 H  H    . CYS   B  2  266 ? 8.231   -20.628 -14.659  1.00 58.11  ? 270  CYS   B H    1 
ATOM   13058 H  HA   . CYS   B  2  266 ? 9.317   -18.355 -13.607  1.00 65.27  ? 270  CYS   B HA   1 
ATOM   13059 H  HB2  . CYS   B  2  266 ? 6.760   -19.359 -12.985  1.00 71.59  ? 270  CYS   B HB2  1 
ATOM   13060 H  HB3  . CYS   B  2  266 ? 7.350   -17.955 -12.530  1.00 71.59  ? 270  CYS   B HB3  1 
ATOM   13061 N  N    . PRO   B  2  267 ? 10.353  -19.552 -11.660  1.00 52.99  ? 271  PRO   B N    1 
ATOM   13062 C  CA   . PRO   B  2  267 ? 10.978  -20.442 -10.674  1.00 50.05  ? 271  PRO   B CA   1 
ATOM   13063 C  C    . PRO   B  2  267 ? 10.054  -20.771 -9.512   1.00 47.25  ? 271  PRO   B C    1 
ATOM   13064 O  O    . PRO   B  2  267 ? 9.185   -19.984 -9.131   1.00 51.44  ? 271  PRO   B O    1 
ATOM   13065 C  CB   . PRO   B  2  267 ? 12.202  -19.645 -10.200  1.00 52.58  ? 271  PRO   B CB   1 
ATOM   13066 C  CG   . PRO   B  2  267 ? 12.474  -18.672 -11.291  1.00 53.77  ? 271  PRO   B CG   1 
ATOM   13067 C  CD   . PRO   B  2  267 ? 11.135  -18.317 -11.852  1.00 54.14  ? 271  PRO   B CD   1 
ATOM   13068 H  HA   . PRO   B  2  267 ? 11.256  -21.267 -11.102  1.00 60.09  ? 271  PRO   B HA   1 
ATOM   13069 H  HB2  . PRO   B  2  267 ? 11.996  -19.187 -9.370   1.00 63.13  ? 271  PRO   B HB2  1 
ATOM   13070 H  HB3  . PRO   B  2  267 ? 12.955  -20.242 -10.072  1.00 63.13  ? 271  PRO   B HB3  1 
ATOM   13071 H  HG2  . PRO   B  2  267 ? 12.915  -17.887 -10.929  1.00 64.56  ? 271  PRO   B HG2  1 
ATOM   13072 H  HG3  . PRO   B  2  267 ? 13.033  -19.084 -11.968  1.00 64.56  ? 271  PRO   B HG3  1 
ATOM   13073 H  HD2  . PRO   B  2  267 ? 10.740  -17.578 -11.363  1.00 65.00  ? 271  PRO   B HD2  1 
ATOM   13074 H  HD3  . PRO   B  2  267 ? 11.203  -18.094 -12.793  1.00 65.00  ? 271  PRO   B HD3  1 
ATOM   13075 N  N    . ASN   B  2  268 ? 10.254  -21.966 -8.955   1.00 43.12  ? 272  ASN   B N    1 
ATOM   13076 C  CA   . ASN   B  2  268 ? 9.568   -22.356 -7.732   1.00 44.40  ? 272  ASN   B CA   1 
ATOM   13077 C  C    . ASN   B  2  268 ? 9.743   -21.273 -6.675   1.00 47.39  ? 272  ASN   B C    1 
ATOM   13078 O  O    . ASN   B  2  268 ? 10.784  -20.614 -6.600   1.00 45.94  ? 272  ASN   B O    1 
ATOM   13079 C  CB   . ASN   B  2  268 ? 10.122  -23.692 -7.229   1.00 46.01  ? 272  ASN   B CB   1 
ATOM   13080 C  CG   . ASN   B  2  268 ? 9.202   -24.372 -6.235   1.00 47.38  ? 272  ASN   B CG   1 
ATOM   13081 O  OD1  . ASN   B  2  268 ? 9.241   -24.089 -5.038   1.00 47.44  ? 272  ASN   B OD1  1 
ATOM   13082 N  ND2  . ASN   B  2  268 ? 8.374   -25.287 -6.728   1.00 49.74  ? 272  ASN   B ND2  1 
ATOM   13083 H  H    . ASN   B  2  268 ? 10.784  -22.567 -9.268   1.00 51.78  ? 272  ASN   B H    1 
ATOM   13084 H  HA   . ASN   B  2  268 ? 8.619   -22.470 -7.899   1.00 53.31  ? 272  ASN   B HA   1 
ATOM   13085 H  HB2  . ASN   B  2  268 ? 10.241  -24.289 -7.984   1.00 55.25  ? 272  ASN   B HB2  1 
ATOM   13086 H  HB3  . ASN   B  2  268 ? 10.973  -23.536 -6.791   1.00 55.25  ? 272  ASN   B HB3  1 
ATOM   13087 H  HD21 . ASN   B  2  268 ? 7.832   -25.702 -6.205   1.00 59.73  ? 272  ASN   B HD21 1 
ATOM   13088 H  HD22 . ASN   B  2  268 ? 8.381   -25.464 -7.569   1.00 59.73  ? 272  ASN   B HD22 1 
ATOM   13089 N  N    . ASP   B  2  269 ? 8.712   -21.084 -5.851   1.00 49.93  ? 273  ASP   B N    1 
ATOM   13090 C  CA   . ASP   B  2  269 ? 8.695   -20.003 -4.875   1.00 52.68  ? 273  ASP   B CA   1 
ATOM   13091 C  C    . ASP   B  2  269 ? 8.798   -20.489 -3.436   1.00 52.60  ? 273  ASP   B C    1 
ATOM   13092 O  O    . ASP   B  2  269 ? 8.781   -19.662 -2.517   1.00 56.31  ? 273  ASP   B O    1 
ATOM   13093 C  CB   . ASP   B  2  269 ? 7.425   -19.158 -5.045   1.00 59.03  ? 273  ASP   B CB   1 
ATOM   13094 C  CG   . ASP   B  2  269 ? 6.157   -19.933 -4.737   1.00 65.86  ? 273  ASP   B CG   1 
ATOM   13095 O  OD1  . ASP   B  2  269 ? 6.244   -21.150 -4.471   1.00 69.59  ? 273  ASP   B OD1  1 
ATOM   13096 O  OD2  . ASP   B  2  269 ? 5.069   -19.320 -4.761   1.00 68.08  ? 273  ASP   B OD2  1 
ATOM   13097 H  H    . ASP   B  2  269 ? 8.006   -21.575 -5.842   1.00 59.95  ? 273  ASP   B H    1 
ATOM   13098 H  HA   . ASP   B  2  269 ? 9.460   -19.431 -5.043   1.00 63.26  ? 273  ASP   B HA   1 
ATOM   13099 H  HB2  . ASP   B  2  269 ? 7.467   -18.400 -4.441   1.00 70.88  ? 273  ASP   B HB2  1 
ATOM   13100 H  HB3  . ASP   B  2  269 ? 7.372   -18.849 -5.963   1.00 70.88  ? 273  ASP   B HB3  1 
ATOM   13101 N  N    . GLY   B  2  270 ? 8.907   -21.796 -3.212   1.00 50.42  ? 274  GLY   B N    1 
ATOM   13102 C  CA   . GLY   B  2  270 ? 9.067   -22.307 -1.863   1.00 50.04  ? 274  GLY   B CA   1 
ATOM   13103 C  C    . GLY   B  2  270 ? 7.890   -22.056 -0.951   1.00 49.07  ? 274  GLY   B C    1 
ATOM   13104 O  O    . GLY   B  2  270 ? 8.055   -22.049 0.272    1.00 54.32  ? 274  GLY   B O    1 
ATOM   13105 H  H    . GLY   B  2  270 ? 8.891   -22.401 -3.823   1.00 60.54  ? 274  GLY   B H    1 
ATOM   13106 H  HA2  . GLY   B  2  270 ? 9.208   -23.265 -1.908   1.00 60.08  ? 274  GLY   B HA2  1 
ATOM   13107 H  HA3  . GLY   B  2  270 ? 9.846   -21.891 -1.463   1.00 60.08  ? 274  GLY   B HA3  1 
ATOM   13108 N  N    . LEU   B  2  271 ? 6.702   -21.850 -1.510   1.00 46.01  ? 275  LEU   B N    1 
ATOM   13109 C  CA   . LEU   B  2  271 ? 5.495   -21.601 -0.739   1.00 50.13  ? 275  LEU   B CA   1 
ATOM   13110 C  C    . LEU   B  2  271 ? 4.538   -22.779 -0.863   1.00 51.70  ? 275  LEU   B C    1 
ATOM   13111 O  O    . LEU   B  2  271 ? 4.594   -23.558 -1.817   1.00 53.20  ? 275  LEU   B O    1 
ATOM   13112 C  CB   . LEU   B  2  271 ? 4.798   -20.322 -1.210   1.00 50.67  ? 275  LEU   B CB   1 
ATOM   13113 C  CG   . LEU   B  2  271 ? 5.650   -19.054 -1.192   1.00 51.05  ? 275  LEU   B CG   1 
ATOM   13114 C  CD1  . LEU   B  2  271 ? 4.844   -17.876 -1.710   1.00 52.92  ? 275  LEU   B CD1  1 
ATOM   13115 C  CD2  . LEU   B  2  271 ? 6.166   -18.780 0.209    1.00 52.27  ? 275  LEU   B CD2  1 
ATOM   13116 H  H    . LEU   B  2  271 ? 6.569   -21.851 -2.359   1.00 55.25  ? 275  LEU   B H    1 
ATOM   13117 H  HA   . LEU   B  2  271 ? 5.731   -21.495 0.196    1.00 60.20  ? 275  LEU   B HA   1 
ATOM   13118 H  HB2  . LEU   B  2  271 ? 4.504   -20.457 -2.125   1.00 60.85  ? 275  LEU   B HB2  1 
ATOM   13119 H  HB3  . LEU   B  2  271 ? 4.034   -20.164 -0.635   1.00 60.85  ? 275  LEU   B HB3  1 
ATOM   13120 H  HG   . LEU   B  2  271 ? 6.418   -19.173 -1.772   1.00 61.30  ? 275  LEU   B HG   1 
ATOM   13121 H  HD11 . LEU   B  2  271 ? 5.393   -17.077 -1.673   1.00 63.54  ? 275  LEU   B HD11 1 
ATOM   13122 H  HD12 . LEU   B  2  271 ? 4.579   -18.054 -2.626   1.00 63.54  ? 275  LEU   B HD12 1 
ATOM   13123 H  HD13 . LEU   B  2  271 ? 4.057   -17.763 -1.155   1.00 63.54  ? 275  LEU   B HD13 1 
ATOM   13124 H  HD21 . LEU   B  2  271 ? 6.652   -17.941 0.208    1.00 62.76  ? 275  LEU   B HD21 1 
ATOM   13125 H  HD22 . LEU   B  2  271 ? 5.413   -18.725 0.818    1.00 62.76  ? 275  LEU   B HD22 1 
ATOM   13126 H  HD23 . LEU   B  2  271 ? 6.754   -19.504 0.475    1.00 62.76  ? 275  LEU   B HD23 1 
ATOM   13127 N  N    . CYS   B  2  272 ? 3.652   -22.898 0.121    1.00 52.72  ? 276  CYS   B N    1 
ATOM   13128 C  CA   . CYS   B  2  272 ? 2.620   -23.922 0.065    1.00 54.05  ? 276  CYS   B CA   1 
ATOM   13129 C  C    . CYS   B  2  272 ? 1.586   -23.560 -0.994   1.00 55.25  ? 276  CYS   B C    1 
ATOM   13130 O  O    . CYS   B  2  272 ? 1.176   -22.402 -1.113   1.00 56.19  ? 276  CYS   B O    1 
ATOM   13131 C  CB   . CYS   B  2  272 ? 1.946   -24.082 1.426    1.00 59.98  ? 276  CYS   B CB   1 
ATOM   13132 S  SG   . CYS   B  2  272 ? 0.825   -25.495 1.502    1.00 65.89  ? 276  CYS   B SG   1 
ATOM   13133 H  H    . CYS   B  2  272 ? 3.627   -22.403 0.823    1.00 63.30  ? 276  CYS   B H    1 
ATOM   13134 H  HA   . CYS   B  2  272 ? 3.020   -24.775 -0.168   1.00 64.90  ? 276  CYS   B HA   1 
ATOM   13135 H  HB2  . CYS   B  2  272 ? 2.629   -24.206 2.103    1.00 72.01  ? 276  CYS   B HB2  1 
ATOM   13136 H  HB3  . CYS   B  2  272 ? 1.431   -23.282 1.617    1.00 72.01  ? 276  CYS   B HB3  1 
ATOM   13137 N  N    . HIS   B  2  273 ? 1.169   -24.560 -1.773   1.00 50.93  ? 277  HIS   B N    1 
ATOM   13138 C  CA   . HIS   B  2  273 ? 0.183   -24.368 -2.829   1.00 50.84  ? 277  HIS   B CA   1 
ATOM   13139 C  C    . HIS   B  2  273 ? -0.720  -25.600 -2.933   1.00 53.98  ? 277  HIS   B C    1 
ATOM   13140 O  O    . HIS   B  2  273 ? -0.863  -26.217 -3.984   1.00 56.91  ? 277  HIS   B O    1 
ATOM   13141 C  CB   . HIS   B  2  273 ? 0.855   -24.092 -4.174   1.00 54.27  ? 277  HIS   B CB   1 
ATOM   13142 C  CG   . HIS   B  2  273 ? 1.535   -22.761 -4.255   1.00 56.72  ? 277  HIS   B CG   1 
ATOM   13143 N  ND1  . HIS   B  2  273 ? 0.844   -21.568 -4.253   1.00 58.09  ? 277  HIS   B ND1  1 
ATOM   13144 C  CD2  . HIS   B  2  273 ? 2.845   -22.436 -4.366   1.00 54.59  ? 277  HIS   B CD2  1 
ATOM   13145 C  CE1  . HIS   B  2  273 ? 1.700   -20.566 -4.347   1.00 58.14  ? 277  HIS   B CE1  1 
ATOM   13146 N  NE2  . HIS   B  2  273 ? 2.920   -21.065 -4.417   1.00 55.65  ? 277  HIS   B NE2  1 
ATOM   13147 H  H    . HIS   B  2  273 ? 1.448   -25.370 -1.704   1.00 61.15  ? 277  HIS   B H    1 
ATOM   13148 H  HA   . HIS   B  2  273 ? -0.363  -23.604 -2.584   1.00 61.05  ? 277  HIS   B HA   1 
ATOM   13149 H  HB2  . HIS   B  2  273 ? 1.525   -24.775 -4.332   1.00 65.16  ? 277  HIS   B HB2  1 
ATOM   13150 H  HB3  . HIS   B  2  273 ? 0.181   -24.121 -4.870   1.00 65.16  ? 277  HIS   B HB3  1 
ATOM   13151 H  HD2  . HIS   B  2  273 ? 3.560   -23.030 -4.400   1.00 65.54  ? 277  HIS   B HD2  1 
ATOM   13152 H  HE1  . HIS   B  2  273 ? 1.479   -19.663 -4.361   1.00 69.81  ? 277  HIS   B HE1  1 
ATOM   13153 H  HE2  . HIS   B  2  273 ? 3.645   -20.606 -4.483   1.00 66.81  ? 277  HIS   B HE2  1 
ATOM   13154 N  N    . LEU   B  2  274 ? -1.348  -25.969 -1.821   1.00 58.08  ? 278  LEU   B N    1 
ATOM   13155 C  CA   . LEU   B  2  274 ? -2.310  -27.064 -1.792   1.00 63.17  ? 278  LEU   B CA   1 
ATOM   13156 C  C    . LEU   B  2  274 ? -3.713  -26.478 -1.889   1.00 68.83  ? 278  LEU   B C    1 
ATOM   13157 O  O    . LEU   B  2  274 ? -4.108  -25.661 -1.050   1.00 71.64  ? 278  LEU   B O    1 
ATOM   13158 C  CB   . LEU   B  2  274 ? -2.152  -27.895 -0.520   1.00 65.56  ? 278  LEU   B CB   1 
ATOM   13159 C  CG   . LEU   B  2  274 ? -0.819  -28.632 -0.369   1.00 65.63  ? 278  LEU   B CG   1 
ATOM   13160 C  CD1  . LEU   B  2  274 ? -0.773  -29.385 0.950    1.00 66.10  ? 278  LEU   B CD1  1 
ATOM   13161 C  CD2  . LEU   B  2  274 ? -0.589  -29.584 -1.534   1.00 67.60  ? 278  LEU   B CD2  1 
ATOM   13162 H  H    . LEU   B  2  274 ? -1.230  -25.592 -1.057   1.00 69.73  ? 278  LEU   B H    1 
ATOM   13163 H  HA   . LEU   B  2  274 ? -2.165  -27.650 -2.551   1.00 75.84  ? 278  LEU   B HA   1 
ATOM   13164 H  HB2  . LEU   B  2  274 ? -2.243  -27.303 0.243    1.00 78.71  ? 278  LEU   B HB2  1 
ATOM   13165 H  HB3  . LEU   B  2  274 ? -2.855  -28.564 -0.506   1.00 78.71  ? 278  LEU   B HB3  1 
ATOM   13166 H  HG   . LEU   B  2  274 ? -0.101  -27.980 -0.373   1.00 78.79  ? 278  LEU   B HG   1 
ATOM   13167 H  HD11 . LEU   B  2  274 ? 0.068   -29.865 1.010    1.00 79.35  ? 278  LEU   B HD11 1 
ATOM   13168 H  HD12 . LEU   B  2  274 ? -0.843  -28.749 1.679    1.00 79.35  ? 278  LEU   B HD12 1 
ATOM   13169 H  HD13 . LEU   B  2  274 ? -1.514  -30.010 0.983    1.00 79.35  ? 278  LEU   B HD13 1 
ATOM   13170 H  HD21 . LEU   B  2  274 ? 0.236   -30.073 -1.385   1.00 81.15  ? 278  LEU   B HD21 1 
ATOM   13171 H  HD22 . LEU   B  2  274 ? -1.334  -30.202 -1.590   1.00 81.15  ? 278  LEU   B HD22 1 
ATOM   13172 H  HD23 . LEU   B  2  274 ? -0.524  -29.070 -2.354   1.00 81.15  ? 278  LEU   B HD23 1 
ATOM   13173 N  N    . ASP   B  2  275 ? -4.461  -26.893 -2.909   1.00 66.95  ? 279  ASP   B N    1 
ATOM   13174 C  CA   . ASP   B  2  275 ? -5.772  -26.321 -3.172   1.00 70.04  ? 279  ASP   B CA   1 
ATOM   13175 C  C    . ASP   B  2  275 ? -6.828  -27.033 -2.326   1.00 68.87  ? 279  ASP   B C    1 
ATOM   13176 O  O    . ASP   B  2  275 ? -6.516  -27.749 -1.370   1.00 61.83  ? 279  ASP   B O    1 
ATOM   13177 C  CB   . ASP   B  2  275 ? -6.088  -26.384 -4.668   1.00 70.18  ? 279  ASP   B CB   1 
ATOM   13178 C  CG   . ASP   B  2  275 ? -6.159  -27.805 -5.202   1.00 67.49  ? 279  ASP   B CG   1 
ATOM   13179 O  OD1  . ASP   B  2  275 ? -6.324  -28.751 -4.404   1.00 68.19  ? 279  ASP   B OD1  1 
ATOM   13180 O  OD2  . ASP   B  2  275 ? -6.046  -27.976 -6.434   1.00 65.77  ? 279  ASP   B OD2  1 
ATOM   13181 H  H    . ASP   B  2  275 ? -4.227  -27.507 -3.464   1.00 80.37  ? 279  ASP   B H    1 
ATOM   13182 H  HA   . ASP   B  2  275 ? -5.753  -25.389 -2.906   1.00 84.08  ? 279  ASP   B HA   1 
ATOM   13183 H  HB2  . ASP   B  2  275 ? -6.947  -25.961 -4.826   1.00 84.25  ? 279  ASP   B HB2  1 
ATOM   13184 H  HB3  . ASP   B  2  275 ? -5.393  -25.915 -5.156   1.00 84.25  ? 279  ASP   B HB3  1 
ATOM   13185 N  N    . SER   B  2  276 ? -8.101  -26.836 -2.675   1.00 77.46  ? 280  SER   B N    1 
ATOM   13186 C  CA   . SER   B  2  276 ? -9.185  -27.423 -1.894   1.00 85.87  ? 280  SER   B CA   1 
ATOM   13187 C  C    . SER   B  2  276 ? -9.137  -28.944 -1.919   1.00 86.14  ? 280  SER   B C    1 
ATOM   13188 O  O    . SER   B  2  276 ? -9.480  -29.591 -0.922   1.00 88.07  ? 280  SER   B O    1 
ATOM   13189 C  CB   . SER   B  2  276 ? -10.530 -26.920 -2.417   1.00 93.08  ? 280  SER   B CB   1 
ATOM   13190 O  OG   . SER   B  2  276 ? -10.501 -26.758 -3.824   1.00 96.50  ? 280  SER   B OG   1 
ATOM   13191 H  H    . SER   B  2  276 ? -8.360  -26.371 -3.351   1.00 92.99  ? 280  SER   B H    1 
ATOM   13192 H  HA   . SER   B  2  276 ? -9.095  -27.141 -0.971   1.00 103.07 ? 280  SER   B HA   1 
ATOM   13193 H  HB2  . SER   B  2  276 ? -11.218 -27.565 -2.188   1.00 111.73 ? 280  SER   B HB2  1 
ATOM   13194 H  HB3  . SER   B  2  276 ? -10.728 -26.064 -2.005   1.00 111.73 ? 280  SER   B HB3  1 
ATOM   13195 H  HG   . SER   B  2  276 ? -11.237 -26.457 -4.094   1.00 115.84 ? 280  SER   B HG   1 
ATOM   13196 N  N    . LYS   B  2  277 ? -8.718  -29.532 -3.035   1.00 87.08  ? 281  LYS   B N    1 
ATOM   13197 C  CA   . LYS   B  2  277 ? -8.556  -30.976 -3.140   1.00 91.20  ? 281  LYS   B CA   1 
ATOM   13198 C  C    . LYS   B  2  277 ? -7.266  -31.473 -2.502   1.00 84.80  ? 281  LYS   B C    1 
ATOM   13199 O  O    . LYS   B  2  277 ? -6.945  -32.659 -2.633   1.00 86.65  ? 281  LYS   B O    1 
ATOM   13200 C  CB   . LYS   B  2  277 ? -8.600  -31.396 -4.612   1.00 97.98  ? 281  LYS   B CB   1 
ATOM   13201 C  CG   . LYS   B  2  277 ? -9.978  -31.272 -5.240   1.00 105.42 ? 281  LYS   B CG   1 
ATOM   13202 C  CD   . LYS   B  2  277 ? -9.917  -31.262 -6.761   1.00 111.14 ? 281  LYS   B CD   1 
ATOM   13203 C  CE   . LYS   B  2  277 ? -9.463  -32.598 -7.326   1.00 118.87 ? 281  LYS   B CE   1 
ATOM   13204 N  NZ   . LYS   B  2  277 ? -9.427  -32.577 -8.815   1.00 127.34 ? 281  LYS   B NZ   1 
ATOM   13205 H  H    . LYS   B  2  277 ? -8.518  -29.108 -3.756   1.00 104.53 ? 281  LYS   B H    1 
ATOM   13206 H  HA   . LYS   B  2  277 ? -9.296  -31.405 -2.683   1.00 109.48 ? 281  LYS   B HA   1 
ATOM   13207 H  HB2  . LYS   B  2  277 ? -7.992  -30.832 -5.116   1.00 117.61 ? 281  LYS   B HB2  1 
ATOM   13208 H  HB3  . LYS   B  2  277 ? -8.325  -32.324 -4.680   1.00 117.61 ? 281  LYS   B HB3  1 
ATOM   13209 H  HG2  . LYS   B  2  277 ? -10.523 -32.025 -4.964   1.00 126.55 ? 281  LYS   B HG2  1 
ATOM   13210 H  HG3  . LYS   B  2  277 ? -10.387 -30.442 -4.949   1.00 126.55 ? 281  LYS   B HG3  1 
ATOM   13211 H  HD2  . LYS   B  2  277 ? -10.800 -31.069 -7.114   1.00 133.40 ? 281  LYS   B HD2  1 
ATOM   13212 H  HD3  . LYS   B  2  277 ? -9.288  -30.582 -7.050   1.00 133.40 ? 281  LYS   B HD3  1 
ATOM   13213 H  HE2  . LYS   B  2  277 ? -8.571  -32.797 -7.001   1.00 142.68 ? 281  LYS   B HE2  1 
ATOM   13214 H  HE3  . LYS   B  2  277 ? -10.081 -33.291 -7.046   1.00 142.68 ? 281  LYS   B HE3  1 
ATOM   13215 H  HZ1  . LYS   B  2  277 ? -9.156  -33.367 -9.124   1.00 152.84 ? 281  LYS   B HZ1  1 
ATOM   13216 H  HZ2  . LYS   B  2  277 ? -10.238 -32.403 -9.137   1.00 152.84 ? 281  LYS   B HZ2  1 
ATOM   13217 H  HZ3  . LYS   B  2  277 ? -8.863  -31.948 -9.097   1.00 152.84 ? 281  LYS   B HZ3  1 
ATOM   13218 N  N    . ASN   B  2  278 ? -6.530  -30.604 -1.807   1.00 77.96  ? 282  ASN   B N    1 
ATOM   13219 C  CA   . ASN   B  2  278 ? -5.213  -30.949 -1.271   1.00 75.53  ? 282  ASN   B CA   1 
ATOM   13220 C  C    . ASN   B  2  278 ? -4.291  -31.444 -2.383   1.00 67.29  ? 282  ASN   B C    1 
ATOM   13221 O  O    . ASN   B  2  278 ? -3.535  -32.402 -2.212   1.00 63.30  ? 282  ASN   B O    1 
ATOM   13222 C  CB   . ASN   B  2  278 ? -5.319  -31.983 -0.148   1.00 79.22  ? 282  ASN   B CB   1 
ATOM   13223 C  CG   . ASN   B  2  278 ? -5.439  -31.347 1.226    1.00 82.17  ? 282  ASN   B CG   1 
ATOM   13224 O  OD1  . ASN   B  2  278 ? -5.246  -30.141 1.388    1.00 85.23  ? 282  ASN   B OD1  1 
ATOM   13225 N  ND2  . ASN   B  2  278 ? -5.740  -32.163 2.229    1.00 81.28  ? 282  ASN   B ND2  1 
ATOM   13226 H  H    . ASN   B  2  278 ? -6.775  -29.799 -1.631   1.00 93.58  ? 282  ASN   B H    1 
ATOM   13227 H  HA   . ASN   B  2  278 ? -4.818  -30.148 -0.892   1.00 90.67  ? 282  ASN   B HA   1 
ATOM   13228 H  HB2  . ASN   B  2  278 ? -6.107  -32.530 -0.295   1.00 95.11  ? 282  ASN   B HB2  1 
ATOM   13229 H  HB3  . ASN   B  2  278 ? -4.524  -32.538 -0.153   1.00 95.11  ? 282  ASN   B HB3  1 
ATOM   13230 H  HD21 . ASN   B  2  278 ? -5.820  -31.852 3.027    1.00 97.57  ? 282  ASN   B HD21 1 
ATOM   13231 H  HD22 . ASN   B  2  278 ? -5.856  -33.002 2.081    1.00 97.57  ? 282  ASN   B HD22 1 
ATOM   13232 N  N    . GLU   B  2  279 ? -4.360  -30.786 -3.535   1.00 68.53  ? 283  GLU   B N    1 
ATOM   13233 C  CA   . GLU   B  2  279 ? -3.468  -31.052 -4.653   1.00 70.22  ? 283  GLU   B CA   1 
ATOM   13234 C  C    . GLU   B  2  279 ? -2.575  -29.841 -4.886   1.00 65.20  ? 283  GLU   B C    1 
ATOM   13235 O  O    . GLU   B  2  279 ? -3.012  -28.696 -4.734   1.00 65.95  ? 283  GLU   B O    1 
ATOM   13236 C  CB   . GLU   B  2  279 ? -4.250  -31.374 -5.928   1.00 78.13  ? 283  GLU   B CB   1 
ATOM   13237 C  CG   . GLU   B  2  279 ? -5.044  -32.667 -5.859   1.00 92.98  ? 283  GLU   B CG   1 
ATOM   13238 C  CD   . GLU   B  2  279 ? -5.499  -33.150 -7.225   1.00 104.75 ? 283  GLU   B CD   1 
ATOM   13239 O  OE1  . GLU   B  2  279 ? -4.998  -32.626 -8.243   1.00 108.75 ? 283  GLU   B OE1  1 
ATOM   13240 O  OE2  . GLU   B  2  279 ? -6.357  -34.056 -7.280   1.00 110.64 ? 283  GLU   B OE2  1 
ATOM   13241 H  H    . GLU   B  2  279 ? -4.932  -30.165 -3.696   1.00 82.27  ? 283  GLU   B H    1 
ATOM   13242 H  HA   . GLU   B  2  279 ? -2.908  -31.817 -4.446   1.00 84.30  ? 283  GLU   B HA   1 
ATOM   13243 H  HB2  . GLU   B  2  279 ? -4.876  -30.653 -6.099   1.00 93.79  ? 283  GLU   B HB2  1 
ATOM   13244 H  HB3  . GLU   B  2  279 ? -3.624  -31.452 -6.665   1.00 93.79  ? 283  GLU   B HB3  1 
ATOM   13245 H  HG2  . GLU   B  2  279 ? -4.489  -33.359 -5.466   1.00 111.62 ? 283  GLU   B HG2  1 
ATOM   13246 H  HG3  . GLU   B  2  279 ? -5.833  -32.525 -5.313   1.00 111.62 ? 283  GLU   B HG3  1 
ATOM   13247 N  N    . TYR   B  2  280 ? -1.322  -30.101 -5.247   1.00 56.51  ? 284  TYR   B N    1 
ATOM   13248 C  CA   . TYR   B  2  280 ? -0.378  -29.031 -5.556   1.00 57.11  ? 284  TYR   B CA   1 
ATOM   13249 C  C    . TYR   B  2  280 ? -0.855  -28.297 -6.804   1.00 58.92  ? 284  TYR   B C    1 
ATOM   13250 O  O    . TYR   B  2  280 ? -0.825  -28.848 -7.909   1.00 58.47  ? 284  TYR   B O    1 
ATOM   13251 C  CB   . TYR   B  2  280 ? 1.020   -29.610 -5.743   1.00 57.40  ? 284  TYR   B CB   1 
ATOM   13252 C  CG   . TYR   B  2  280 ? 2.055   -28.596 -6.167   1.00 57.80  ? 284  TYR   B CG   1 
ATOM   13253 C  CD1  . TYR   B  2  280 ? 2.187   -27.386 -5.499   1.00 58.24  ? 284  TYR   B CD1  1 
ATOM   13254 C  CD2  . TYR   B  2  280 ? 2.911   -28.856 -7.227   1.00 55.02  ? 284  TYR   B CD2  1 
ATOM   13255 C  CE1  . TYR   B  2  280 ? 3.136   -26.458 -5.885   1.00 56.45  ? 284  TYR   B CE1  1 
ATOM   13256 C  CE2  . TYR   B  2  280 ? 3.862   -27.937 -7.618   1.00 51.99  ? 284  TYR   B CE2  1 
ATOM   13257 C  CZ   . TYR   B  2  280 ? 3.971   -26.740 -6.944   1.00 54.47  ? 284  TYR   B CZ   1 
ATOM   13258 O  OH   . TYR   B  2  280 ? 4.920   -25.825 -7.335   1.00 56.76  ? 284  TYR   B OH   1 
ATOM   13259 H  H    . TYR   B  2  280 ? -0.992  -30.892 -5.320   1.00 67.85  ? 284  TYR   B H    1 
ATOM   13260 H  HA   . TYR   B  2  280 ? -0.342  -28.397 -4.823   1.00 68.57  ? 284  TYR   B HA   1 
ATOM   13261 H  HB2  . TYR   B  2  280 ? 1.312   -29.995 -4.902   1.00 68.92  ? 284  TYR   B HB2  1 
ATOM   13262 H  HB3  . TYR   B  2  280 ? 0.983   -30.296 -6.428   1.00 68.92  ? 284  TYR   B HB3  1 
ATOM   13263 H  HD1  . TYR   B  2  280 ? 1.628   -27.196 -4.781   1.00 69.93  ? 284  TYR   B HD1  1 
ATOM   13264 H  HD2  . TYR   B  2  280 ? 2.842   -29.664 -7.683   1.00 66.06  ? 284  TYR   B HD2  1 
ATOM   13265 H  HE1  . TYR   B  2  280 ? 3.211   -25.649 -5.432   1.00 67.78  ? 284  TYR   B HE1  1 
ATOM   13266 H  HE2  . TYR   B  2  280 ? 4.428   -28.125 -8.332   1.00 62.43  ? 284  TYR   B HE2  1 
ATOM   13267 H  HH   . TYR   B  2  280 ? 5.363   -26.128 -7.981   1.00 68.15  ? 284  TYR   B HH   1 
ATOM   13268 N  N    . SER   B  2  281 ? -1.294  -27.048 -6.630   1.00 59.35  ? 285  SER   B N    1 
ATOM   13269 C  CA   . SER   B  2  281 ? -1.991  -26.345 -7.701   1.00 59.19  ? 285  SER   B CA   1 
ATOM   13270 C  C    . SER   B  2  281 ? -1.040  -25.706 -8.706   1.00 61.27  ? 285  SER   B C    1 
ATOM   13271 O  O    . SER   B  2  281 ? -1.417  -25.516 -9.868   1.00 64.79  ? 285  SER   B O    1 
ATOM   13272 C  CB   . SER   B  2  281 ? -2.910  -25.276 -7.108   1.00 60.22  ? 285  SER   B CB   1 
ATOM   13273 O  OG   . SER   B  2  281 ? -2.177  -24.356 -6.318   1.00 61.00  ? 285  SER   B OG   1 
ATOM   13274 H  H    . SER   B  2  281 ? -1.202  -26.592 -5.907   1.00 71.26  ? 285  SER   B H    1 
ATOM   13275 H  HA   . SER   B  2  281 ? -2.533  -26.988 -8.183   1.00 71.06  ? 285  SER   B HA   1 
ATOM   13276 H  HB2  . SER   B  2  281 ? -3.342  -24.796 -7.831   1.00 72.31  ? 285  SER   B HB2  1 
ATOM   13277 H  HB3  . SER   B  2  281 ? -3.576  -25.708 -6.551   1.00 72.31  ? 285  SER   B HB3  1 
ATOM   13278 H  HG   . SER   B  2  281 ? -2.697  -23.786 -5.985   1.00 73.23  ? 285  SER   B HG   1 
ATOM   13279 N  N    . MET   B  2  282 ? 0.179   -25.365 -8.294   1.00 57.91  ? 286  MET   B N    1 
ATOM   13280 C  CA   . MET   B  2  282 ? 1.144   -24.735 -9.184   1.00 55.86  ? 286  MET   B CA   1 
ATOM   13281 C  C    . MET   B  2  282 ? 1.951   -25.749 -9.986   1.00 49.99  ? 286  MET   B C    1 
ATOM   13282 O  O    . MET   B  2  282 ? 2.957   -25.375 -10.599  1.00 45.71  ? 286  MET   B O    1 
ATOM   13283 C  CB   . MET   B  2  282 ? 2.096   -23.842 -8.384   1.00 55.87  ? 286  MET   B CB   1 
ATOM   13284 C  CG   . MET   B  2  282 ? 1.394   -22.795 -7.538   1.00 58.86  ? 286  MET   B CG   1 
ATOM   13285 S  SD   . MET   B  2  282 ? 0.469   -21.586 -8.507   1.00 65.49  ? 286  MET   B SD   1 
ATOM   13286 C  CE   . MET   B  2  282 ? 1.793   -20.549 -9.123   1.00 65.49  ? 286  MET   B CE   1 
ATOM   13287 H  H    . MET   B  2  282 ? 0.470   -25.490 -7.495   1.00 69.53  ? 286  MET   B H    1 
ATOM   13288 H  HA   . MET   B  2  282 ? 0.658   -24.168 -9.803   1.00 67.07  ? 286  MET   B HA   1 
ATOM   13289 H  HB2  . MET   B  2  282 ? 2.619   -24.401 -7.788   1.00 67.08  ? 286  MET   B HB2  1 
ATOM   13290 H  HB3  . MET   B  2  282 ? 2.681   -23.378 -9.003   1.00 67.08  ? 286  MET   B HB3  1 
ATOM   13291 H  HG2  . MET   B  2  282 ? 0.770   -23.239 -6.943   1.00 70.67  ? 286  MET   B HG2  1 
ATOM   13292 H  HG3  . MET   B  2  282 ? 2.059   -22.313 -7.021   1.00 70.67  ? 286  MET   B HG3  1 
ATOM   13293 H  HE1  . MET   B  2  282 ? 1.411   -19.828 -9.648   1.00 78.63  ? 286  MET   B HE1  1 
ATOM   13294 H  HE2  . MET   B  2  282 ? 2.286   -20.186 -8.371   1.00 78.63  ? 286  MET   B HE2  1 
ATOM   13295 H  HE3  . MET   B  2  282 ? 2.382   -21.085 -9.677   1.00 78.63  ? 286  MET   B HE3  1 
ATOM   13296 N  N    . SER   B  2  283 ? 1.532   -27.017 -9.994   1.00 47.71  ? 287  SER   B N    1 
ATOM   13297 C  CA   . SER   B  2  283 ? 2.276   -28.049 -10.709  1.00 46.45  ? 287  SER   B CA   1 
ATOM   13298 C  C    . SER   B  2  283 ? 2.567   -27.636 -12.145  1.00 45.03  ? 287  SER   B C    1 
ATOM   13299 O  O    . SER   B  2  283 ? 3.664   -27.879 -12.661  1.00 44.64  ? 287  SER   B O    1 
ATOM   13300 C  CB   . SER   B  2  283 ? 1.492   -29.362 -10.682  1.00 52.09  ? 287  SER   B CB   1 
ATOM   13301 O  OG   . SER   B  2  283 ? 2.148   -30.367 -11.434  1.00 59.43  ? 287  SER   B OG   1 
ATOM   13302 H  H    . SER   B  2  283 ? 0.825   -27.301 -9.595   1.00 57.28  ? 287  SER   B H    1 
ATOM   13303 H  HA   . SER   B  2  283 ? 3.125   -28.188 -10.261  1.00 55.78  ? 287  SER   B HA   1 
ATOM   13304 H  HB2  . SER   B  2  283 ? 1.411   -29.660 -9.763   1.00 62.54  ? 287  SER   B HB2  1 
ATOM   13305 H  HB3  . SER   B  2  283 ? 0.612   -29.210 -11.061  1.00 62.54  ? 287  SER   B HB3  1 
ATOM   13306 H  HG   . SER   B  2  283 ? 1.687   -31.069 -11.438  1.00 71.35  ? 287  SER   B HG   1 
ATOM   13307 N  N    . THR   B  2  284 ? 1.599   -27.005 -12.806  1.00 45.65  ? 288  THR   B N    1 
ATOM   13308 C  CA   . THR   B  2  284 ? 1.729   -26.609 -14.199  1.00 47.96  ? 288  THR   B CA   1 
ATOM   13309 C  C    . THR   B  2  284 ? 2.174   -25.164 -14.364  1.00 50.26  ? 288  THR   B C    1 
ATOM   13310 O  O    . THR   B  2  284 ? 2.121   -24.634 -15.479  1.00 51.30  ? 288  THR   B O    1 
ATOM   13311 C  CB   . THR   B  2  284 ? 0.398   -26.815 -14.927  1.00 51.74  ? 288  THR   B CB   1 
ATOM   13312 O  OG1  . THR   B  2  284 ? -0.606  -25.976 -14.339  1.00 55.01  ? 288  THR   B OG1  1 
ATOM   13313 C  CG2  . THR   B  2  284 ? -0.044  -28.266 -14.834  1.00 50.87  ? 288  THR   B CG2  1 
ATOM   13314 H  H    . THR   B  2  284 ? 0.842   -26.792 -12.457  1.00 54.82  ? 288  THR   B H    1 
ATOM   13315 H  HA   . THR   B  2  284 ? 2.398   -27.176 -14.613  1.00 57.59  ? 288  THR   B HA   1 
ATOM   13316 H  HB   . THR   B  2  284 ? 0.503   -26.586 -15.864  1.00 62.12  ? 288  THR   B HB   1 
ATOM   13317 H  HG1  . THR   B  2  284 ? -1.333  -26.068 -14.749  1.00 66.05  ? 288  THR   B HG1  1 
ATOM   13318 H  HG21 . THR   B  2  284 ? -0.851  -28.402 -15.354  1.00 61.09  ? 288  THR   B HG21 1 
ATOM   13319 H  HG22 . THR   B  2  284 ? 0.653   -28.848 -15.177  1.00 61.09  ? 288  THR   B HG22 1 
ATOM   13320 H  HG23 . THR   B  2  284 ? -0.221  -28.500 -13.909  1.00 61.09  ? 288  THR   B HG23 1 
ATOM   13321 N  N    . VAL   B  2  285 ? 2.614   -24.506 -13.294  1.00 51.56  ? 289  VAL   B N    1 
ATOM   13322 C  CA   . VAL   B  2  285 ? 2.864   -23.078 -13.310  1.00 50.34  ? 289  VAL   B CA   1 
ATOM   13323 C  C    . VAL   B  2  285 ? 4.295   -22.750 -12.931  1.00 46.91  ? 289  VAL   B C    1 
ATOM   13324 O  O    . VAL   B  2  285 ? 4.886   -21.799 -13.460  1.00 48.42  ? 289  VAL   B O    1 
ATOM   13325 C  CB   . VAL   B  2  285 ? 1.881   -22.341 -12.376  1.00 55.90  ? 289  VAL   B CB   1 
ATOM   13326 C  CG1  . VAL   B  2  285 ? 2.131   -20.840 -12.414  1.00 56.74  ? 289  VAL   B CG1  1 
ATOM   13327 C  CG2  . VAL   B  2  285 ? 0.445   -22.668 -12.753  1.00 58.53  ? 289  VAL   B CG2  1 
ATOM   13328 H  H    . VAL   B  2  285 ? 2.776   -24.877 -12.536  1.00 61.91  ? 289  VAL   B H    1 
ATOM   13329 H  HA   . VAL   B  2  285 ? 2.726   -22.751 -14.213  1.00 60.45  ? 289  VAL   B HA   1 
ATOM   13330 H  HB   . VAL   B  2  285 ? 2.024   -22.641 -11.464  1.00 67.12  ? 289  VAL   B HB   1 
ATOM   13331 H  HG11 . VAL   B  2  285 ? 1.440   -20.391 -11.902  1.00 68.12  ? 289  VAL   B HG11 1 
ATOM   13332 H  HG12 . VAL   B  2  285 ? 3.001   -20.655 -12.028  1.00 68.12  ? 289  VAL   B HG12 1 
ATOM   13333 H  HG13 . VAL   B  2  285 ? 2.107   -20.540 -13.336  1.00 68.12  ? 289  VAL   B HG13 1 
ATOM   13334 H  HG21 . VAL   B  2  285 ? -0.154  -22.149 -12.194  1.00 70.28  ? 289  VAL   B HG21 1 
ATOM   13335 H  HG22 . VAL   B  2  285 ? 0.305   -22.444 -13.686  1.00 70.28  ? 289  VAL   B HG22 1 
ATOM   13336 H  HG23 . VAL   B  2  285 ? 0.290   -23.615 -12.613  1.00 70.28  ? 289  VAL   B HG23 1 
ATOM   13337 N  N    . LEU   B  2  286 ? 4.870   -23.517 -12.012  1.00 47.57  ? 290  LEU   B N    1 
ATOM   13338 C  CA   . LEU   B  2  286 ? 6.180   -23.226 -11.461  1.00 46.00  ? 290  LEU   B CA   1 
ATOM   13339 C  C    . LEU   B  2  286 ? 7.163   -24.332 -11.815  1.00 48.01  ? 290  LEU   B C    1 
ATOM   13340 O  O    . LEU   B  2  286 ? 6.798   -25.506 -11.922  1.00 50.39  ? 290  LEU   B O    1 
ATOM   13341 C  CB   . LEU   B  2  286 ? 6.119   -23.060 -9.936   1.00 44.09  ? 290  LEU   B CB   1 
ATOM   13342 C  CG   . LEU   B  2  286 ? 5.221   -21.929 -9.428   1.00 43.62  ? 290  LEU   B CG   1 
ATOM   13343 C  CD1  . LEU   B  2  286 ? 5.235   -21.862 -7.906   1.00 42.81  ? 290  LEU   B CD1  1 
ATOM   13344 C  CD2  . LEU   B  2  286 ? 5.643   -20.595 -10.021  1.00 44.02  ? 290  LEU   B CD2  1 
ATOM   13345 H  H    . LEU   B  2  286 ? 4.510   -24.227 -11.688  1.00 57.12  ? 290  LEU   B H    1 
ATOM   13346 H  HA   . LEU   B  2  286 ? 6.509   -22.399 -11.846  1.00 55.24  ? 290  LEU   B HA   1 
ATOM   13347 H  HB2  . LEU   B  2  286 ? 5.785   -23.887 -9.554   1.00 52.94  ? 290  LEU   B HB2  1 
ATOM   13348 H  HB3  . LEU   B  2  286 ? 7.016   -22.884 -9.614   1.00 52.94  ? 290  LEU   B HB3  1 
ATOM   13349 H  HG   . LEU   B  2  286 ? 4.311   -22.109 -9.711   1.00 52.39  ? 290  LEU   B HG   1 
ATOM   13350 H  HD11 . LEU   B  2  286 ? 4.631   -21.161 -7.615   1.00 51.41  ? 290  LEU   B HD11 1 
ATOM   13351 H  HD12 . LEU   B  2  286 ? 4.945   -22.717 -7.551   1.00 51.41  ? 290  LEU   B HD12 1 
ATOM   13352 H  HD13 . LEU   B  2  286 ? 6.136   -21.668 -7.607   1.00 51.41  ? 290  LEU   B HD13 1 
ATOM   13353 H  HD21 . LEU   B  2  286 ? 5.096   -19.892 -9.638   1.00 52.86  ? 290  LEU   B HD21 1 
ATOM   13354 H  HD22 . LEU   B  2  286 ? 6.578   -20.438 -9.813   1.00 52.86  ? 290  LEU   B HD22 1 
ATOM   13355 H  HD23 . LEU   B  2  286 ? 5.519   -20.624 -10.983  1.00 52.86  ? 290  LEU   B HD23 1 
ATOM   13356 N  N    . GLU   B  2  287 ? 8.418   -23.934 -11.998  1.00 48.09  ? 291  GLU   B N    1 
ATOM   13357 C  CA   . GLU   B  2  287 ? 9.477   -24.887 -12.279  1.00 52.83  ? 291  GLU   B CA   1 
ATOM   13358 C  C    . GLU   B  2  287 ? 9.598   -25.894 -11.140  1.00 46.83  ? 291  GLU   B C    1 
ATOM   13359 O  O    . GLU   B  2  287 ? 9.183   -25.642 -10.005  1.00 43.83  ? 291  GLU   B O    1 
ATOM   13360 C  CB   . GLU   B  2  287 ? 10.808  -24.160 -12.470  1.00 58.13  ? 291  GLU   B CB   1 
ATOM   13361 C  CG   . GLU   B  2  287 ? 10.787  -23.109 -13.568  1.00 65.01  ? 291  GLU   B CG   1 
ATOM   13362 C  CD   . GLU   B  2  287 ? 12.104  -22.367 -13.696  1.00 73.24  ? 291  GLU   B CD   1 
ATOM   13363 O  OE1  . GLU   B  2  287 ? 12.850  -22.297 -12.696  1.00 74.47  ? 291  GLU   B OE1  1 
ATOM   13364 O  OE2  . GLU   B  2  287 ? 12.393  -21.856 -14.798  1.00 76.17  ? 291  GLU   B OE2  1 
ATOM   13365 H  H    . GLU   B  2  287 ? 8.681   -23.116 -11.964  1.00 57.75  ? 291  GLU   B H    1 
ATOM   13366 H  HA   . GLU   B  2  287 ? 9.273   -25.370 -13.095  1.00 63.43  ? 291  GLU   B HA   1 
ATOM   13367 H  HB2  . GLU   B  2  287 ? 11.040  -23.714 -11.641  1.00 69.79  ? 291  GLU   B HB2  1 
ATOM   13368 H  HB3  . GLU   B  2  287 ? 11.488  -24.812 -12.699  1.00 69.79  ? 291  GLU   B HB3  1 
ATOM   13369 H  HG2  . GLU   B  2  287 ? 10.603  -23.542 -14.416  1.00 78.05  ? 291  GLU   B HG2  1 
ATOM   13370 H  HG3  . GLU   B  2  287 ? 10.094  -22.459 -13.370  1.00 78.05  ? 291  GLU   B HG3  1 
ATOM   13371 N  N    . TYR   B  2  288 ? 10.166  -27.055 -11.456  1.00 45.97  ? 292  TYR   B N    1 
ATOM   13372 C  CA   . TYR   B  2  288 ? 10.576  -27.960 -10.398  1.00 46.11  ? 292  TYR   B CA   1 
ATOM   13373 C  C    . TYR   B  2  288 ? 11.545  -27.221 -9.476   1.00 44.48  ? 292  TYR   B C    1 
ATOM   13374 O  O    . TYR   B  2  288 ? 12.320  -26.375 -9.932   1.00 44.52  ? 292  TYR   B O    1 
ATOM   13375 C  CB   . TYR   B  2  288 ? 11.262  -29.202 -10.962  1.00 45.47  ? 292  TYR   B CB   1 
ATOM   13376 C  CG   . TYR   B  2  288 ? 10.445  -30.002 -11.950  1.00 47.65  ? 292  TYR   B CG   1 
ATOM   13377 C  CD1  . TYR   B  2  288 ? 9.576   -30.998 -11.522  1.00 48.72  ? 292  TYR   B CD1  1 
ATOM   13378 C  CD2  . TYR   B  2  288 ? 10.564  -29.779 -13.314  1.00 49.22  ? 292  TYR   B CD2  1 
ATOM   13379 C  CE1  . TYR   B  2  288 ? 8.838   -31.739 -12.428  1.00 50.34  ? 292  TYR   B CE1  1 
ATOM   13380 C  CE2  . TYR   B  2  288 ? 9.831   -30.512 -14.225  1.00 49.65  ? 292  TYR   B CE2  1 
ATOM   13381 C  CZ   . TYR   B  2  288 ? 8.969   -31.489 -13.778  1.00 50.80  ? 292  TYR   B CZ   1 
ATOM   13382 O  OH   . TYR   B  2  288 ? 8.241   -32.220 -14.689  1.00 52.52  ? 292  TYR   B OH   1 
ATOM   13383 H  H    . TYR   B  2  288 ? 10.320  -27.331 -12.255  1.00 55.20  ? 292  TYR   B H    1 
ATOM   13384 H  HA   . TYR   B  2  288 ? 9.799   -28.256 -9.901   1.00 55.37  ? 292  TYR   B HA   1 
ATOM   13385 H  HB2  . TYR   B  2  288 ? 12.073  -28.924 -11.415  1.00 54.60  ? 292  TYR   B HB2  1 
ATOM   13386 H  HB3  . TYR   B  2  288 ? 11.480  -29.792 -10.223  1.00 54.60  ? 292  TYR   B HB3  1 
ATOM   13387 H  HD1  . TYR   B  2  288 ? 9.489   -31.170 -10.612  1.00 58.49  ? 292  TYR   B HD1  1 
ATOM   13388 H  HD2  . TYR   B  2  288 ? 11.148  -29.124 -13.620  1.00 59.10  ? 292  TYR   B HD2  1 
ATOM   13389 H  HE1  . TYR   B  2  288 ? 8.257   -32.401 -12.128  1.00 60.45  ? 292  TYR   B HE1  1 
ATOM   13390 H  HE2  . TYR   B  2  288 ? 9.918   -30.347 -15.136  1.00 59.61  ? 292  TYR   B HE2  1 
ATOM   13391 H  HH   . TYR   B  2  288 ? 8.048   -32.972 -14.367  1.00 63.06  ? 292  TYR   B HH   1 
ATOM   13392 N  N    . PRO   B  2  289 ? 11.524  -27.504 -8.177   1.00 45.14  ? 293  PRO   B N    1 
ATOM   13393 C  CA   . PRO   B  2  289 ? 12.525  -26.895 -7.297   1.00 44.76  ? 293  PRO   B CA   1 
ATOM   13394 C  C    . PRO   B  2  289 ? 13.925  -27.368 -7.653   1.00 44.59  ? 293  PRO   B C    1 
ATOM   13395 O  O    . PRO   B  2  289 ? 14.124  -28.469 -8.171   1.00 43.64  ? 293  PRO   B O    1 
ATOM   13396 C  CB   . PRO   B  2  289 ? 12.110  -27.359 -5.894   1.00 44.02  ? 293  PRO   B CB   1 
ATOM   13397 C  CG   . PRO   B  2  289 ? 11.176  -28.492 -6.098   1.00 46.32  ? 293  PRO   B CG   1 
ATOM   13398 C  CD   . PRO   B  2  289 ? 10.524  -28.284 -7.426   1.00 45.25  ? 293  PRO   B CD   1 
ATOM   13399 H  HA   . PRO   B  2  289 ? 12.481  -25.927 -7.340   1.00 53.75  ? 293  PRO   B HA   1 
ATOM   13400 H  HB2  . PRO   B  2  289 ? 12.895  -27.646 -5.400   1.00 52.86  ? 293  PRO   B HB2  1 
ATOM   13401 H  HB3  . PRO   B  2  289 ? 11.671  -26.632 -5.426   1.00 52.86  ? 293  PRO   B HB3  1 
ATOM   13402 H  HG2  . PRO   B  2  289 ? 11.673  -29.325 -6.091   1.00 55.62  ? 293  PRO   B HG2  1 
ATOM   13403 H  HG3  . PRO   B  2  289 ? 10.513  -28.495 -5.391   1.00 55.62  ? 293  PRO   B HG3  1 
ATOM   13404 H  HD2  . PRO   B  2  289 ? 10.350  -29.133 -7.861   1.00 54.34  ? 293  PRO   B HD2  1 
ATOM   13405 H  HD3  . PRO   B  2  289 ? 9.698   -27.785 -7.330   1.00 54.34  ? 293  PRO   B HD3  1 
ATOM   13406 N  N    . THR   B  2  290 ? 14.899  -26.505 -7.387   1.00 46.38  ? 294  THR   B N    1 
ATOM   13407 C  CA   . THR   B  2  290 ? 16.300  -26.866 -7.504   1.00 48.97  ? 294  THR   B CA   1 
ATOM   13408 C  C    . THR   B  2  290 ? 16.765  -27.501 -6.196   1.00 54.34  ? 294  THR   B C    1 
ATOM   13409 O  O    . THR   B  2  290 ? 16.088  -27.430 -5.169   1.00 55.42  ? 294  THR   B O    1 
ATOM   13410 C  CB   . THR   B  2  290 ? 17.155  -25.641 -7.829   1.00 49.64  ? 294  THR   B CB   1 
ATOM   13411 O  OG1  . THR   B  2  290 ? 17.331  -24.851 -6.646   1.00 48.11  ? 294  THR   B OG1  1 
ATOM   13412 C  CG2  . THR   B  2  290 ? 16.497  -24.787 -8.908   1.00 51.03  ? 294  THR   B CG2  1 
ATOM   13413 H  H    . THR   B  2  290 ? 14.769  -25.694 -7.133   1.00 55.69  ? 294  THR   B H    1 
ATOM   13414 H  HA   . THR   B  2  290 ? 16.413  -27.500 -8.229   1.00 58.80  ? 294  THR   B HA   1 
ATOM   13415 H  HB   . THR   B  2  290 ? 18.019  -25.933 -8.159   1.00 59.61  ? 294  THR   B HB   1 
ATOM   13416 H  HG1  . THR   B  2  290 ? 18.082  -24.476 -6.660   1.00 57.77  ? 294  THR   B HG1  1 
ATOM   13417 H  HG21 . THR   B  2  290 ? 17.046  -24.010 -9.098   1.00 61.27  ? 294  THR   B HG21 1 
ATOM   13418 H  HG22 . THR   B  2  290 ? 16.391  -25.304 -9.722   1.00 61.27  ? 294  THR   B HG22 1 
ATOM   13419 H  HG23 . THR   B  2  290 ? 15.623  -24.489 -8.609   1.00 61.27  ? 294  THR   B HG23 1 
ATOM   13420 N  N    . ILE   B  2  291 ? 17.939  -28.132 -6.237   1.00 58.65  ? 295  ILE   B N    1 
ATOM   13421 C  CA   . ILE   B  2  291 ? 18.497  -28.692 -5.009   1.00 61.58  ? 295  ILE   B CA   1 
ATOM   13422 C  C    . ILE   B  2  291 ? 18.701  -27.589 -3.980   1.00 58.92  ? 295  ILE   B C    1 
ATOM   13423 O  O    . ILE   B  2  291 ? 18.388  -27.758 -2.795   1.00 56.19  ? 295  ILE   B O    1 
ATOM   13424 C  CB   . ILE   B  2  291 ? 19.806  -29.447 -5.300   1.00 69.60  ? 295  ILE   B CB   1 
ATOM   13425 C  CG1  . ILE   B  2  291 ? 19.508  -30.893 -5.701   1.00 75.82  ? 295  ILE   B CG1  1 
ATOM   13426 C  CG2  . ILE   B  2  291 ? 20.715  -29.443 -4.078   1.00 72.25  ? 295  ILE   B CG2  1 
ATOM   13427 C  CD1  . ILE   B  2  291 ? 18.625  -31.027 -6.916   1.00 83.20  ? 295  ILE   B CD1  1 
ATOM   13428 H  H    . ILE   B  2  291 ? 18.418  -28.247 -6.942   1.00 70.42  ? 295  ILE   B H    1 
ATOM   13429 H  HA   . ILE   B  2  291 ? 17.865  -29.333 -4.647   1.00 73.93  ? 295  ILE   B HA   1 
ATOM   13430 H  HB   . ILE   B  2  291 ? 20.252  -28.994 -6.032   1.00 83.56  ? 295  ILE   B HB   1 
ATOM   13431 H  HG12 . ILE   B  2  291 ? 20.347  -31.340 -5.896   1.00 91.02  ? 295  ILE   B HG12 1 
ATOM   13432 H  HG13 . ILE   B  2  291 ? 19.061  -31.334 -4.962   1.00 91.02  ? 295  ILE   B HG13 1 
ATOM   13433 H  HG21 . ILE   B  2  291 ? 21.470  -30.028 -4.244   1.00 86.73  ? 295  ILE   B HG21 1 
ATOM   13434 H  HG22 . ILE   B  2  291 ? 21.026  -28.538 -3.919   1.00 86.73  ? 295  ILE   B HG22 1 
ATOM   13435 H  HG23 . ILE   B  2  291 ? 20.213  -29.760 -3.310   1.00 86.73  ? 295  ILE   B HG23 1 
ATOM   13436 H  HD11 . ILE   B  2  291 ? 18.535  -31.967 -7.139   1.00 99.87  ? 295  ILE   B HD11 1 
ATOM   13437 H  HD12 . ILE   B  2  291 ? 17.754  -30.650 -6.716   1.00 99.87  ? 295  ILE   B HD12 1 
ATOM   13438 H  HD13 . ILE   B  2  291 ? 19.031  -30.550 -7.656   1.00 99.87  ? 295  ILE   B HD13 1 
ATOM   13439 N  N    . GLY   B  2  292 ? 19.229  -26.443 -4.414   1.00 59.15  ? 296  GLY   B N    1 
ATOM   13440 C  CA   . GLY   B  2  292 ? 19.418  -25.335 -3.493   1.00 57.00  ? 296  GLY   B CA   1 
ATOM   13441 C  C    . GLY   B  2  292 ? 18.131  -24.925 -2.806   1.00 56.84  ? 296  GLY   B C    1 
ATOM   13442 O  O    . GLY   B  2  292 ? 18.123  -24.619 -1.611   1.00 57.22  ? 296  GLY   B O    1 
ATOM   13443 H  H    . GLY   B  2  292 ? 19.481  -26.288 -5.222   1.00 71.02  ? 296  GLY   B H    1 
ATOM   13444 H  HA2  . GLY   B  2  292 ? 20.060  -25.591 -2.812   1.00 68.43  ? 296  GLY   B HA2  1 
ATOM   13445 H  HA3  . GLY   B  2  292 ? 19.762  -24.569 -3.979   1.00 68.43  ? 296  GLY   B HA3  1 
ATOM   13446 N  N    . GLN   B  2  293 ? 17.021  -24.923 -3.548   1.00 55.78  ? 297  GLN   B N    1 
ATOM   13447 C  CA   . GLN   B  2  293 ? 15.744  -24.525 -2.966   1.00 52.76  ? 297  GLN   B CA   1 
ATOM   13448 C  C    . GLN   B  2  293 ? 15.245  -25.559 -1.964   1.00 50.98  ? 297  GLN   B C    1 
ATOM   13449 O  O    . GLN   B  2  293 ? 14.766  -25.199 -0.882   1.00 51.52  ? 297  GLN   B O    1 
ATOM   13450 C  CB   . GLN   B  2  293 ? 14.713  -24.309 -4.073   1.00 51.83  ? 297  GLN   B CB   1 
ATOM   13451 C  CG   . GLN   B  2  293 ? 15.001  -23.101 -4.951   1.00 54.30  ? 297  GLN   B CG   1 
ATOM   13452 C  CD   . GLN   B  2  293 ? 14.046  -22.988 -6.122   1.00 55.62  ? 297  GLN   B CD   1 
ATOM   13453 O  OE1  . GLN   B  2  293 ? 13.748  -23.976 -6.792   1.00 58.80  ? 297  GLN   B OE1  1 
ATOM   13454 N  NE2  . GLN   B  2  293 ? 13.557  -21.780 -6.373   1.00 57.85  ? 297  GLN   B NE2  1 
ATOM   13455 H  H    . GLN   B  2  293 ? 16.984  -25.145 -4.378   1.00 66.97  ? 297  GLN   B H    1 
ATOM   13456 H  HA   . GLN   B  2  293 ? 15.862  -23.686 -2.495   1.00 63.35  ? 297  GLN   B HA   1 
ATOM   13457 H  HB2  . GLN   B  2  293 ? 14.700  -25.093 -4.644   1.00 62.24  ? 297  GLN   B HB2  1 
ATOM   13458 H  HB3  . GLN   B  2  293 ? 13.842  -24.179 -3.667   1.00 62.24  ? 297  GLN   B HB3  1 
ATOM   13459 H  HG2  . GLN   B  2  293 ? 14.917  -22.296 -4.417   1.00 65.20  ? 297  GLN   B HG2  1 
ATOM   13460 H  HG3  . GLN   B  2  293 ? 15.901  -23.174 -5.304   1.00 65.20  ? 297  GLN   B HG3  1 
ATOM   13461 H  HE21 . GLN   B  2  293 ? 13.787  -21.113 -5.881   1.00 69.45  ? 297  GLN   B HE21 1 
ATOM   13462 H  HE22 . GLN   B  2  293 ? 13.012  -21.664 -7.028   1.00 69.45  ? 297  GLN   B HE22 1 
ATOM   13463 N  N    . LEU   B  2  294 ? 15.344  -26.846 -2.304   1.00 52.48  ? 298  LEU   B N    1 
ATOM   13464 C  CA   . LEU   B  2  294 ? 14.896  -27.885 -1.383   1.00 49.01  ? 298  LEU   B CA   1 
ATOM   13465 C  C    . LEU   B  2  294 ? 15.701  -27.857 -0.090   1.00 50.57  ? 298  LEU   B C    1 
ATOM   13466 O  O    . LEU   B  2  294 ? 15.147  -28.053 0.999    1.00 51.01  ? 298  LEU   B O    1 
ATOM   13467 C  CB   . LEU   B  2  294 ? 14.998  -29.257 -2.048   1.00 47.33  ? 298  LEU   B CB   1 
ATOM   13468 C  CG   . LEU   B  2  294 ? 14.003  -29.524 -3.179   1.00 49.21  ? 298  LEU   B CG   1 
ATOM   13469 C  CD1  . LEU   B  2  294 ? 14.385  -30.782 -3.941   1.00 52.31  ? 298  LEU   B CD1  1 
ATOM   13470 C  CD2  . LEU   B  2  294 ? 12.585  -29.641 -2.636   1.00 49.96  ? 298  LEU   B CD2  1 
ATOM   13471 H  H    . LEU   B  2  294 ? 15.661  -27.137 -3.049   1.00 63.01  ? 298  LEU   B H    1 
ATOM   13472 H  HA   . LEU   B  2  294 ? 13.965  -27.727 -1.162   1.00 58.85  ? 298  LEU   B HA   1 
ATOM   13473 H  HB2  . LEU   B  2  294 ? 15.889  -29.348 -2.421   1.00 56.83  ? 298  LEU   B HB2  1 
ATOM   13474 H  HB3  . LEU   B  2  294 ? 14.851  -29.935 -1.369   1.00 56.83  ? 298  LEU   B HB3  1 
ATOM   13475 H  HG   . LEU   B  2  294 ? 14.026  -28.776 -3.796   1.00 59.09  ? 298  LEU   B HG   1 
ATOM   13476 H  HD11 . LEU   B  2  294 ? 13.728  -30.943 -4.635   1.00 62.81  ? 298  LEU   B HD11 1 
ATOM   13477 H  HD12 . LEU   B  2  294 ? 15.262  -30.657 -4.338   1.00 62.81  ? 298  LEU   B HD12 1 
ATOM   13478 H  HD13 . LEU   B  2  294 ? 14.406  -31.531 -3.325   1.00 62.81  ? 298  LEU   B HD13 1 
ATOM   13479 H  HD21 . LEU   B  2  294 ? 11.979  -29.816 -3.373   1.00 59.99  ? 298  LEU   B HD21 1 
ATOM   13480 H  HD22 . LEU   B  2  294 ? 12.550  -30.371 -1.999   1.00 59.99  ? 298  LEU   B HD22 1 
ATOM   13481 H  HD23 . LEU   B  2  294 ? 12.344  -28.809 -2.200   1.00 59.99  ? 298  LEU   B HD23 1 
ATOM   13482 N  N    . ILE   B  2  295 ? 17.012  -27.618 -0.186   1.00 50.61  ? 299  ILE   B N    1 
ATOM   13483 C  CA   . ILE   B  2  295 ? 17.830  -27.504 1.018    1.00 50.08  ? 299  ILE   B CA   1 
ATOM   13484 C  C    . ILE   B  2  295 ? 17.291  -26.397 1.913    1.00 54.81  ? 299  ILE   B C    1 
ATOM   13485 O  O    . ILE   B  2  295 ? 17.064  -26.597 3.112    1.00 56.91  ? 299  ILE   B O    1 
ATOM   13486 C  CB   . ILE   B  2  295 ? 19.305  -27.258 0.650    1.00 46.54  ? 299  ILE   B CB   1 
ATOM   13487 C  CG1  . ILE   B  2  295 ? 19.894  -28.496 -0.030   1.00 45.93  ? 299  ILE   B CG1  1 
ATOM   13488 C  CG2  . ILE   B  2  295 ? 20.113  -26.896 1.899    1.00 42.48  ? 299  ILE   B CG2  1 
ATOM   13489 C  CD1  . ILE   B  2  295 ? 21.327  -28.325 -0.505   1.00 45.35  ? 299  ILE   B CD1  1 
ATOM   13490 H  H    . ILE   B  2  295 ? 17.442  -27.520 -0.924   1.00 60.77  ? 299  ILE   B H    1 
ATOM   13491 H  HA   . ILE   B  2  295 ? 17.780  -28.342 1.504    1.00 60.14  ? 299  ILE   B HA   1 
ATOM   13492 H  HB   . ILE   B  2  295 ? 19.348  -26.514 0.030    1.00 55.89  ? 299  ILE   B HB   1 
ATOM   13493 H  HG12 . ILE   B  2  295 ? 19.879  -29.233 0.601    1.00 55.15  ? 299  ILE   B HG12 1 
ATOM   13494 H  HG13 . ILE   B  2  295 ? 19.351  -28.712 -0.805   1.00 55.15  ? 299  ILE   B HG13 1 
ATOM   13495 H  HG21 . ILE   B  2  295 ? 21.042  -26.769 1.648    1.00 51.01  ? 299  ILE   B HG21 1 
ATOM   13496 H  HG22 . ILE   B  2  295 ? 19.758  -26.077 2.278    1.00 51.01  ? 299  ILE   B HG22 1 
ATOM   13497 H  HG23 . ILE   B  2  295 ? 20.040  -27.617 2.543    1.00 51.01  ? 299  ILE   B HG23 1 
ATOM   13498 H  HD11 . ILE   B  2  295 ? 21.607  -29.134 -0.962   1.00 54.46  ? 299  ILE   B HD11 1 
ATOM   13499 H  HD12 . ILE   B  2  295 ? 21.370  -27.570 -1.112   1.00 54.46  ? 299  ILE   B HD12 1 
ATOM   13500 H  HD13 . ILE   B  2  295 ? 21.897  -28.165 0.263    1.00 54.46  ? 299  ILE   B HD13 1 
ATOM   13501 N  N    . ASP   B  2  296 ? 17.085  -25.210 1.339    1.00 56.10  ? 300  ASP   B N    1 
ATOM   13502 C  CA   . ASP   B  2  296 ? 16.623  -24.070 2.122    1.00 60.48  ? 300  ASP   B CA   1 
ATOM   13503 C  C    . ASP   B  2  296 ? 15.397  -24.433 2.952    1.00 59.98  ? 300  ASP   B C    1 
ATOM   13504 O  O    . ASP   B  2  296 ? 15.351  -24.180 4.161    1.00 62.72  ? 300  ASP   B O    1 
ATOM   13505 C  CB   . ASP   B  2  296 ? 16.312  -22.895 1.192    1.00 66.02  ? 300  ASP   B CB   1 
ATOM   13506 C  CG   . ASP   B  2  296 ? 16.274  -21.567 1.922    1.00 73.41  ? 300  ASP   B CG   1 
ATOM   13507 O  OD1  . ASP   B  2  296 ? 17.358  -21.021 2.217    1.00 74.98  ? 300  ASP   B OD1  1 
ATOM   13508 O  OD2  . ASP   B  2  296 ? 15.163  -21.068 2.201    1.00 76.34  ? 300  ASP   B OD2  1 
ATOM   13509 H  H    . ASP   B  2  296 ? 17.205  -25.042 0.505    1.00 67.36  ? 300  ASP   B H    1 
ATOM   13510 H  HA   . ASP   B  2  296 ? 17.328  -23.800 2.731    1.00 72.62  ? 300  ASP   B HA   1 
ATOM   13511 H  HB2  . ASP   B  2  296 ? 16.998  -22.843 0.509    1.00 79.26  ? 300  ASP   B HB2  1 
ATOM   13512 H  HB3  . ASP   B  2  296 ? 15.445  -23.037 0.781    1.00 79.26  ? 300  ASP   B HB3  1 
ATOM   13513 N  N    . LYS   B  2  297 ? 14.397  -25.048 2.318    1.00 59.81  ? 301  LYS   B N    1 
ATOM   13514 C  CA   . LYS   B  2  297 ? 13.123  -25.275 2.992    1.00 57.09  ? 301  LYS   B CA   1 
ATOM   13515 C  C    . LYS   B  2  297 ? 13.138  -26.522 3.867    1.00 53.42  ? 301  LYS   B C    1 
ATOM   13516 O  O    . LYS   B  2  297 ? 12.377  -26.593 4.839    1.00 55.43  ? 301  LYS   B O    1 
ATOM   13517 C  CB   . LYS   B  2  297 ? 11.998  -25.368 1.961    1.00 51.12  ? 301  LYS   B CB   1 
ATOM   13518 C  CG   . LYS   B  2  297 ? 11.795  -24.090 1.159    1.00 50.22  ? 301  LYS   B CG   1 
ATOM   13519 C  CD   . LYS   B  2  297 ? 11.360  -22.926 2.041    1.00 53.23  ? 301  LYS   B CD   1 
ATOM   13520 C  CE   . LYS   B  2  297 ? 11.327  -21.627 1.258    1.00 63.42  ? 301  LYS   B CE   1 
ATOM   13521 N  NZ   . LYS   B  2  297 ? 10.900  -20.473 2.093    1.00 73.79  ? 301  LYS   B NZ   1 
ATOM   13522 H  H    . LYS   B  2  297 ? 14.431  -25.338 1.510    1.00 71.81  ? 301  LYS   B H    1 
ATOM   13523 H  HA   . LYS   B  2  297 ? 12.943  -24.518 3.571    1.00 68.54  ? 301  LYS   B HA   1 
ATOM   13524 H  HB2  . LYS   B  2  297 ? 12.206  -26.080 1.336    1.00 61.38  ? 301  LYS   B HB2  1 
ATOM   13525 H  HB3  . LYS   B  2  297 ? 11.167  -25.564 2.422    1.00 61.38  ? 301  LYS   B HB3  1 
ATOM   13526 H  HG2  . LYS   B  2  297 ? 12.629  -23.848 0.727    1.00 60.30  ? 301  LYS   B HG2  1 
ATOM   13527 H  HG3  . LYS   B  2  297 ? 11.106  -24.238 0.491    1.00 60.30  ? 301  LYS   B HG3  1 
ATOM   13528 H  HD2  . LYS   B  2  297 ? 10.470  -23.098 2.387    1.00 63.91  ? 301  LYS   B HD2  1 
ATOM   13529 H  HD3  . LYS   B  2  297 ? 11.987  -22.826 2.774    1.00 63.91  ? 301  LYS   B HD3  1 
ATOM   13530 H  HE2  . LYS   B  2  297 ? 12.216  -21.440 0.917    1.00 76.14  ? 301  LYS   B HE2  1 
ATOM   13531 H  HE3  . LYS   B  2  297 ? 10.701  -21.715 0.523    1.00 76.14  ? 301  LYS   B HE3  1 
ATOM   13532 H  HZ1  . LYS   B  2  297 ? 10.865  -19.735 1.597    1.00 88.59  ? 301  LYS   B HZ1  1 
ATOM   13533 H  HZ2  . LYS   B  2  297 ? 10.094  -20.628 2.438    1.00 88.59  ? 301  LYS   B HZ2  1 
ATOM   13534 H  HZ3  . LYS   B  2  297 ? 11.479  -20.347 2.757    1.00 88.59  ? 301  LYS   B HZ3  1 
ATOM   13535 N  N    . LEU   B  2  298 ? 13.978  -27.509 3.552    1.00 49.73  ? 302  LEU   B N    1 
ATOM   13536 C  CA   . LEU   B  2  298 ? 14.080  -28.677 4.422    1.00 50.24  ? 302  LEU   B CA   1 
ATOM   13537 C  C    . LEU   B  2  298 ? 14.738  -28.314 5.747    1.00 54.47  ? 302  LEU   B C    1 
ATOM   13538 O  O    . LEU   B  2  298 ? 14.336  -28.812 6.806    1.00 55.04  ? 302  LEU   B O    1 
ATOM   13539 C  CB   . LEU   B  2  298 ? 14.860  -29.790 3.728    1.00 46.12  ? 302  LEU   B CB   1 
ATOM   13540 C  CG   . LEU   B  2  298 ? 14.106  -30.610 2.681    1.00 46.12  ? 302  LEU   B CG   1 
ATOM   13541 C  CD1  . LEU   B  2  298 ? 15.089  -31.482 1.922    1.00 45.78  ? 302  LEU   B CD1  1 
ATOM   13542 C  CD2  . LEU   B  2  298 ? 13.014  -31.461 3.322    1.00 46.29  ? 302  LEU   B CD2  1 
ATOM   13543 H  H    . LEU   B  2  298 ? 14.485  -27.526 2.858    1.00 59.71  ? 302  LEU   B H    1 
ATOM   13544 H  HA   . LEU   B  2  298 ? 13.186  -29.008 4.604    1.00 60.33  ? 302  LEU   B HA   1 
ATOM   13545 H  HB2  . LEU   B  2  298 ? 15.621  -29.389 3.280    1.00 55.38  ? 302  LEU   B HB2  1 
ATOM   13546 H  HB3  . LEU   B  2  298 ? 15.165  -30.411 4.408    1.00 55.38  ? 302  LEU   B HB3  1 
ATOM   13547 H  HG   . LEU   B  2  298 ? 13.668  -30.009 2.058    1.00 55.38  ? 302  LEU   B HG   1 
ATOM   13548 H  HD11 . LEU   B  2  298 ? 14.608  -31.984 1.245    1.00 54.98  ? 302  LEU   B HD11 1 
ATOM   13549 H  HD12 . LEU   B  2  298 ? 15.755  -30.915 1.503    1.00 54.98  ? 302  LEU   B HD12 1 
ATOM   13550 H  HD13 . LEU   B  2  298 ? 15.516  -32.091 2.544    1.00 54.98  ? 302  LEU   B HD13 1 
ATOM   13551 H  HD21 . LEU   B  2  298 ? 12.545  -31.949 2.627    1.00 55.59  ? 302  LEU   B HD21 1 
ATOM   13552 H  HD22 . LEU   B  2  298 ? 13.423  -32.083 3.945    1.00 55.59  ? 302  LEU   B HD22 1 
ATOM   13553 H  HD23 . LEU   B  2  298 ? 12.396  -30.880 3.793    1.00 55.59  ? 302  LEU   B HD23 1 
ATOM   13554 N  N    . VAL   B  2  299 ? 15.753  -27.449 5.709    1.00 53.65  ? 303  VAL   B N    1 
ATOM   13555 C  CA   . VAL   B  2  299 ? 16.401  -27.008 6.940    1.00 56.97  ? 303  VAL   B CA   1 
ATOM   13556 C  C    . VAL   B  2  299 ? 15.479  -26.077 7.717    1.00 62.67  ? 303  VAL   B C    1 
ATOM   13557 O  O    . VAL   B  2  299 ? 15.324  -26.205 8.937    1.00 67.72  ? 303  VAL   B O    1 
ATOM   13558 C  CB   . VAL   B  2  299 ? 17.746  -26.329 6.620    1.00 53.88  ? 303  VAL   B CB   1 
ATOM   13559 C  CG1  . VAL   B  2  299 ? 18.343  -25.706 7.872    1.00 53.18  ? 303  VAL   B CG1  1 
ATOM   13560 C  CG2  . VAL   B  2  299 ? 18.713  -27.330 6.007    1.00 53.30  ? 303  VAL   B CG2  1 
ATOM   13561 H  H    . VAL   B  2  299 ? 16.080  -27.107 4.991    1.00 64.41  ? 303  VAL   B H    1 
ATOM   13562 H  HA   . VAL   B  2  299 ? 16.579  -27.785 7.492    1.00 68.40  ? 303  VAL   B HA   1 
ATOM   13563 H  HB   . VAL   B  2  299 ? 17.593  -25.621 5.975    1.00 64.70  ? 303  VAL   B HB   1 
ATOM   13564 H  HG11 . VAL   B  2  299 ? 19.221  -25.352 7.661    1.00 63.85  ? 303  VAL   B HG11 1 
ATOM   13565 H  HG12 . VAL   B  2  299 ? 17.763  -24.991 8.177    1.00 63.85  ? 303  VAL   B HG12 1 
ATOM   13566 H  HG13 . VAL   B  2  299 ? 18.418  -26.387 8.559    1.00 63.85  ? 303  VAL   B HG13 1 
ATOM   13567 H  HG21 . VAL   B  2  299 ? 19.557  -26.886 5.831    1.00 64.00  ? 303  VAL   B HG21 1 
ATOM   13568 H  HG22 . VAL   B  2  299 ? 18.848  -28.061 6.631    1.00 64.00  ? 303  VAL   B HG22 1 
ATOM   13569 H  HG23 . VAL   B  2  299 ? 18.336  -27.667 5.179    1.00 64.00  ? 303  VAL   B HG23 1 
ATOM   13570 N  N    . GLN   B  2  300 ? 14.860  -25.122 7.022    1.00 62.93  ? 304  GLN   B N    1 
ATOM   13571 C  CA   . GLN   B  2  300 ? 13.976  -24.169 7.685    1.00 70.37  ? 304  GLN   B CA   1 
ATOM   13572 C  C    . GLN   B  2  300 ? 12.855  -24.883 8.431    1.00 65.31  ? 304  GLN   B C    1 
ATOM   13573 O  O    . GLN   B  2  300 ? 12.500  -24.495 9.550    1.00 65.46  ? 304  GLN   B O    1 
ATOM   13574 C  CB   . GLN   B  2  300 ? 13.407  -23.196 6.651    1.00 82.26  ? 304  GLN   B CB   1 
ATOM   13575 C  CG   . GLN   B  2  300 ? 12.571  -22.064 7.223    1.00 95.49  ? 304  GLN   B CG   1 
ATOM   13576 C  CD   . GLN   B  2  300 ? 12.179  -21.050 6.163    1.00 107.96 ? 304  GLN   B CD   1 
ATOM   13577 O  OE1  . GLN   B  2  300 ? 12.895  -20.856 5.181    1.00 111.81 ? 304  GLN   B OE1  1 
ATOM   13578 N  NE2  . GLN   B  2  300 ? 11.034  -20.404 6.352    1.00 114.78 ? 304  GLN   B NE2  1 
ATOM   13579 H  H    . GLN   B  2  300 ? 14.936  -25.005 6.173    1.00 75.56  ? 304  GLN   B H    1 
ATOM   13580 H  HA   . GLN   B  2  300 ? 14.485  -23.660 8.335    1.00 84.48  ? 304  GLN   B HA   1 
ATOM   13581 H  HB2  . GLN   B  2  300 ? 14.146  -22.796 6.168    1.00 98.75  ? 304  GLN   B HB2  1 
ATOM   13582 H  HB3  . GLN   B  2  300 ? 12.842  -23.694 6.040    1.00 98.75  ? 304  GLN   B HB3  1 
ATOM   13583 H  HG2  . GLN   B  2  300 ? 11.759  -22.430 7.607    1.00 114.63 ? 304  GLN   B HG2  1 
ATOM   13584 H  HG3  . GLN   B  2  300 ? 13.083  -21.604 7.907    1.00 114.63 ? 304  GLN   B HG3  1 
ATOM   13585 H  HE21 . GLN   B  2  300 ? 10.557  -20.570 7.049    1.00 137.78 ? 304  GLN   B HE21 1 
ATOM   13586 H  HE22 . GLN   B  2  300 ? 10.769  -19.820 5.779    1.00 137.78 ? 304  GLN   B HE22 1 
ATOM   13587 N  N    . ASN   B  2  301 ? 12.292  -25.930 7.835    1.00 62.16  ? 305  ASN   B N    1 
ATOM   13588 C  CA   . ASN   B  2  301 ? 11.198  -26.676 8.442    1.00 58.29  ? 305  ASN   B CA   1 
ATOM   13589 C  C    . ASN   B  2  301 ? 11.670  -27.883 9.243    1.00 58.71  ? 305  ASN   B C    1 
ATOM   13590 O  O    . ASN   B  2  301 ? 10.833  -28.629 9.762    1.00 55.27  ? 305  ASN   B O    1 
ATOM   13591 C  CB   . ASN   B  2  301 ? 10.212  -27.125 7.360    1.00 56.13  ? 305  ASN   B CB   1 
ATOM   13592 C  CG   . ASN   B  2  301 ? 9.418   -25.968 6.785    1.00 57.94  ? 305  ASN   B CG   1 
ATOM   13593 O  OD1  . ASN   B  2  301 ? 8.281   -25.722 7.186    1.00 65.71  ? 305  ASN   B OD1  1 
ATOM   13594 N  ND2  . ASN   B  2  301 ? 10.019  -25.247 5.847    1.00 54.18  ? 305  ASN   B ND2  1 
ATOM   13595 H  H    . ASN   B  2  301 ? 12.532  -26.232 7.066    1.00 74.63  ? 305  ASN   B H    1 
ATOM   13596 H  HA   . ASN   B  2  301 ? 10.724  -26.091 9.053    1.00 69.98  ? 305  ASN   B HA   1 
ATOM   13597 H  HB2  . ASN   B  2  301 ? 10.704  -27.542 6.635    1.00 67.40  ? 305  ASN   B HB2  1 
ATOM   13598 H  HB3  . ASN   B  2  301 ? 9.586   -27.759 7.743    1.00 67.40  ? 305  ASN   B HB3  1 
ATOM   13599 H  HD21 . ASN   B  2  301 ? 9.610   -24.580 5.490    1.00 65.06  ? 305  ASN   B HD21 1 
ATOM   13600 H  HD22 . ASN   B  2  301 ? 10.817  -25.446 5.596    1.00 65.06  ? 305  ASN   B HD22 1 
ATOM   13601 N  N    . ASN   B  2  302 ? 12.982  -28.092 9.359    1.00 60.46  ? 306  ASN   B N    1 
ATOM   13602 C  CA   . ASN   B  2  302 ? 13.538  -29.154 10.197   1.00 59.34  ? 306  ASN   B CA   1 
ATOM   13603 C  C    . ASN   B  2  302 ? 12.976  -30.518 9.797    1.00 55.41  ? 306  ASN   B C    1 
ATOM   13604 O  O    . ASN   B  2  302 ? 12.512  -31.297 10.632   1.00 54.82  ? 306  ASN   B O    1 
ATOM   13605 C  CB   . ASN   B  2  302 ? 13.279  -28.860 11.678   1.00 64.92  ? 306  ASN   B CB   1 
ATOM   13606 C  CG   . ASN   B  2  302 ? 14.016  -29.810 12.601   1.00 73.78  ? 306  ASN   B CG   1 
ATOM   13607 O  OD1  . ASN   B  2  302 ? 15.241  -29.915 12.552   1.00 78.89  ? 306  ASN   B OD1  1 
ATOM   13608 N  ND2  . ASN   B  2  302 ? 13.272  -30.496 13.461   1.00 80.60  ? 306  ASN   B ND2  1 
ATOM   13609 H  H    . ASN   B  2  302 ? 13.580  -27.624 8.955    1.00 72.59  ? 306  ASN   B H    1 
ATOM   13610 H  HA   . ASN   B  2  302 ? 14.498  -29.189 10.060   1.00 71.25  ? 306  ASN   B HA   1 
ATOM   13611 H  HB2  . ASN   B  2  302 ? 13.574  -27.958 11.877   1.00 77.94  ? 306  ASN   B HB2  1 
ATOM   13612 H  HB3  . ASN   B  2  302 ? 12.329  -28.945 11.855   1.00 77.94  ? 306  ASN   B HB3  1 
ATOM   13613 H  HD21 . ASN   B  2  302 ? 13.644  -31.048 14.006   1.00 96.76  ? 306  ASN   B HD21 1 
ATOM   13614 H  HD22 . ASN   B  2  302 ? 12.419  -30.388 13.474   1.00 96.76  ? 306  ASN   B HD22 1 
ATOM   13615 N  N    . VAL   B  2  303 ? 13.026  -30.805 8.497    1.00 52.89  ? 307  VAL   B N    1 
ATOM   13616 C  CA   . VAL   B  2  303 ? 12.515  -32.049 7.934    1.00 49.42  ? 307  VAL   B CA   1 
ATOM   13617 C  C    . VAL   B  2  303 ? 13.697  -32.911 7.515    1.00 47.07  ? 307  VAL   B C    1 
ATOM   13618 O  O    . VAL   B  2  303 ? 14.558  -32.464 6.748    1.00 50.17  ? 307  VAL   B O    1 
ATOM   13619 C  CB   . VAL   B  2  303 ? 11.579  -31.787 6.741    1.00 48.05  ? 307  VAL   B CB   1 
ATOM   13620 C  CG1  . VAL   B  2  303 ? 11.177  -33.098 6.075    1.00 46.44  ? 307  VAL   B CG1  1 
ATOM   13621 C  CG2  . VAL   B  2  303 ? 10.347  -31.021 7.195    1.00 49.86  ? 307  VAL   B CG2  1 
ATOM   13622 H  H    . VAL   B  2  303 ? 13.361  -30.277 7.907    1.00 63.51  ? 307  VAL   B H    1 
ATOM   13623 H  HA   . VAL   B  2  303 ? 12.016  -32.525 8.616    1.00 59.34  ? 307  VAL   B HA   1 
ATOM   13624 H  HB   . VAL   B  2  303 ? 12.051  -31.249 6.085    1.00 57.70  ? 307  VAL   B HB   1 
ATOM   13625 H  HG11 . VAL   B  2  303 ? 10.540  -32.911 5.368    1.00 55.77  ? 307  VAL   B HG11 1 
ATOM   13626 H  HG12 . VAL   B  2  303 ? 11.968  -33.520 5.705    1.00 55.77  ? 307  VAL   B HG12 1 
ATOM   13627 H  HG13 . VAL   B  2  303 ? 10.772  -33.678 6.739    1.00 55.77  ? 307  VAL   B HG13 1 
ATOM   13628 H  HG21 . VAL   B  2  303 ? 9.778   -30.855 6.427    1.00 59.87  ? 307  VAL   B HG21 1 
ATOM   13629 H  HG22 . VAL   B  2  303 ? 9.870   -31.551 7.852    1.00 59.87  ? 307  VAL   B HG22 1 
ATOM   13630 H  HG23 . VAL   B  2  303 ? 10.626  -30.179 7.588    1.00 59.87  ? 307  VAL   B HG23 1 
ATOM   13631 N  N    . LEU   B  2  304 ? 13.732  -34.144 8.012    1.00 46.84  ? 308  LEU   B N    1 
ATOM   13632 C  CA   . LEU   B  2  304 ? 14.762  -35.104 7.640    1.00 46.40  ? 308  LEU   B CA   1 
ATOM   13633 C  C    . LEU   B  2  304 ? 14.268  -35.929 6.460    1.00 48.97  ? 308  LEU   B C    1 
ATOM   13634 O  O    . LEU   B  2  304 ? 13.234  -36.599 6.551    1.00 52.17  ? 308  LEU   B O    1 
ATOM   13635 C  CB   . LEU   B  2  304 ? 15.114  -36.015 8.812    1.00 45.38  ? 308  LEU   B CB   1 
ATOM   13636 C  CG   . LEU   B  2  304 ? 15.893  -35.382 9.962    1.00 45.46  ? 308  LEU   B CG   1 
ATOM   13637 C  CD1  . LEU   B  2  304 ? 16.107  -36.415 11.048   1.00 47.72  ? 308  LEU   B CD1  1 
ATOM   13638 C  CD2  . LEU   B  2  304 ? 17.224  -34.825 9.484    1.00 42.88  ? 308  LEU   B CD2  1 
ATOM   13639 H  H    . LEU   B  2  304 ? 13.161  -34.451 8.576    1.00 56.24  ? 308  LEU   B H    1 
ATOM   13640 H  HA   . LEU   B  2  304 ? 15.564  -34.625 7.378    1.00 55.72  ? 308  LEU   B HA   1 
ATOM   13641 H  HB2  . LEU   B  2  304 ? 14.286  -36.357 9.184    1.00 54.50  ? 308  LEU   B HB2  1 
ATOM   13642 H  HB3  . LEU   B  2  304 ? 15.653  -36.746 8.472    1.00 54.50  ? 308  LEU   B HB3  1 
ATOM   13643 H  HG   . LEU   B  2  304 ? 15.387  -34.638 10.325   1.00 54.59  ? 308  LEU   B HG   1 
ATOM   13644 H  HD11 . LEU   B  2  304 ? 16.567  -35.999 11.794   1.00 57.30  ? 308  LEU   B HD11 1 
ATOM   13645 H  HD12 . LEU   B  2  304 ? 15.245  -36.752 11.338   1.00 57.30  ? 308  LEU   B HD12 1 
ATOM   13646 H  HD13 . LEU   B  2  304 ? 16.643  -37.141 10.693   1.00 57.30  ? 308  LEU   B HD13 1 
ATOM   13647 H  HD21 . LEU   B  2  304 ? 17.704  -34.459 10.243   1.00 51.50  ? 308  LEU   B HD21 1 
ATOM   13648 H  HD22 . LEU   B  2  304 ? 17.739  -35.541 9.080    1.00 51.50  ? 308  LEU   B HD22 1 
ATOM   13649 H  HD23 . LEU   B  2  304 ? 17.058  -34.128 8.830    1.00 51.50  ? 308  LEU   B HD23 1 
ATOM   13650 N  N    . LEU   B  2  305 ? 15.012  -35.887 5.362    1.00 48.34  ? 309  LEU   B N    1 
ATOM   13651 C  CA   . LEU   B  2  305 ? 14.625  -36.575 4.142    1.00 43.65  ? 309  LEU   B CA   1 
ATOM   13652 C  C    . LEU   B  2  305 ? 15.275  -37.949 4.080    1.00 47.86  ? 309  LEU   B C    1 
ATOM   13653 O  O    . LEU   B  2  305 ? 16.449  -38.114 4.424    1.00 50.96  ? 309  LEU   B O    1 
ATOM   13654 C  CB   . LEU   B  2  305 ? 15.021  -35.743 2.924    1.00 39.88  ? 309  LEU   B CB   1 
ATOM   13655 C  CG   . LEU   B  2  305 ? 14.562  -36.243 1.557    1.00 37.51  ? 309  LEU   B CG   1 
ATOM   13656 C  CD1  . LEU   B  2  305 ? 13.049  -36.390 1.497    1.00 36.29  ? 309  LEU   B CD1  1 
ATOM   13657 C  CD2  . LEU   B  2  305 ? 15.052  -35.272 0.504    1.00 37.48  ? 309  LEU   B CD2  1 
ATOM   13658 H  H    . LEU   B  2  305 ? 15.756  -35.461 5.300    1.00 58.05  ? 309  LEU   B H    1 
ATOM   13659 H  HA   . LEU   B  2  305 ? 13.663  -36.701 4.126    1.00 52.41  ? 309  LEU   B HA   1 
ATOM   13660 H  HB2  . LEU   B  2  305 ? 14.650  -34.854 3.038    1.00 47.90  ? 309  LEU   B HB2  1 
ATOM   13661 H  HB3  . LEU   B  2  305 ? 15.989  -35.698 2.897    1.00 47.90  ? 309  LEU   B HB3  1 
ATOM   13662 H  HG   . LEU   B  2  305 ? 14.931  -37.123 1.387    1.00 45.05  ? 309  LEU   B HG   1 
ATOM   13663 H  HD11 . LEU   B  2  305 ? 12.796  -36.687 0.609    1.00 43.58  ? 309  LEU   B HD11 1 
ATOM   13664 H  HD12 . LEU   B  2  305 ? 12.768  -37.043 2.157    1.00 43.58  ? 309  LEU   B HD12 1 
ATOM   13665 H  HD13 . LEU   B  2  305 ? 12.640  -35.531 1.687    1.00 43.58  ? 309  LEU   B HD13 1 
ATOM   13666 H  HD21 . LEU   B  2  305 ? 14.690  -35.533 -0.358   1.00 45.01  ? 309  LEU   B HD21 1 
ATOM   13667 H  HD22 . LEU   B  2  305 ? 14.750  -34.379 0.733    1.00 45.01  ? 309  LEU   B HD22 1 
ATOM   13668 H  HD23 . LEU   B  2  305 ? 16.021  -35.298 0.478    1.00 45.01  ? 309  LEU   B HD23 1 
ATOM   13669 N  N    . ILE   B  2  306 ? 14.500  -38.936 3.640    1.00 49.78  ? 310  ILE   B N    1 
ATOM   13670 C  CA   . ILE   B  2  306 ? 14.937  -40.325 3.564    1.00 49.32  ? 310  ILE   B CA   1 
ATOM   13671 C  C    . ILE   B  2  306 ? 14.568  -40.839 2.179    1.00 50.07  ? 310  ILE   B C    1 
ATOM   13672 O  O    . ILE   B  2  306 ? 13.384  -41.052 1.888    1.00 51.06  ? 310  ILE   B O    1 
ATOM   13673 C  CB   . ILE   B  2  306 ? 14.298  -41.191 4.660    1.00 49.60  ? 310  ILE   B CB   1 
ATOM   13674 C  CG1  . ILE   B  2  306 ? 14.873  -40.820 6.031    1.00 49.56  ? 310  ILE   B CG1  1 
ATOM   13675 C  CG2  . ILE   B  2  306 ? 14.512  -42.671 4.368    1.00 52.09  ? 310  ILE   B CG2  1 
ATOM   13676 C  CD1  . ILE   B  2  306 ? 14.127  -41.436 7.198    1.00 51.86  ? 310  ILE   B CD1  1 
ATOM   13677 H  H    . ILE   B  2  306 ? 13.691  -38.820 3.371    1.00 59.77  ? 310  ILE   B H    1 
ATOM   13678 H  HA   . ILE   B  2  306 ? 15.901  -40.369 3.659    1.00 59.23  ? 310  ILE   B HA   1 
ATOM   13679 H  HB   . ILE   B  2  306 ? 13.344  -41.018 4.669    1.00 59.56  ? 310  ILE   B HB   1 
ATOM   13680 H  HG12 . ILE   B  2  306 ? 15.793  -41.123 6.075    1.00 59.51  ? 310  ILE   B HG12 1 
ATOM   13681 H  HG13 . ILE   B  2  306 ? 14.837  -39.856 6.133    1.00 59.51  ? 310  ILE   B HG13 1 
ATOM   13682 H  HG21 . ILE   B  2  306 ? 14.166  -43.192 5.109    1.00 62.54  ? 310  ILE   B HG21 1 
ATOM   13683 H  HG22 . ILE   B  2  306 ? 14.041  -42.903 3.552    1.00 62.54  ? 310  ILE   B HG22 1 
ATOM   13684 H  HG23 . ILE   B  2  306 ? 15.461  -42.838 4.261    1.00 62.54  ? 310  ILE   B HG23 1 
ATOM   13685 H  HD11 . ILE   B  2  306 ? 14.540  -41.146 8.026    1.00 62.26  ? 310  ILE   B HD11 1 
ATOM   13686 H  HD12 . ILE   B  2  306 ? 13.202  -41.145 7.170    1.00 62.26  ? 310  ILE   B HD12 1 
ATOM   13687 H  HD13 . ILE   B  2  306 ? 14.171  -42.403 7.126    1.00 62.26  ? 310  ILE   B HD13 1 
ATOM   13688 N  N    . PHE   B  2  307 ? 15.572  -41.044 1.329    1.00 47.93  ? 311  PHE   B N    1 
ATOM   13689 C  CA   . PHE   B  2  307 ? 15.356  -41.541 -0.025   1.00 48.06  ? 311  PHE   B CA   1 
ATOM   13690 C  C    . PHE   B  2  307 ? 15.291  -43.064 0.007    1.00 51.08  ? 311  PHE   B C    1 
ATOM   13691 O  O    . PHE   B  2  307 ? 16.321  -43.734 0.145    1.00 52.55  ? 311  PHE   B O    1 
ATOM   13692 C  CB   . PHE   B  2  307 ? 16.469  -41.078 -0.963   1.00 48.99  ? 311  PHE   B CB   1 
ATOM   13693 C  CG   . PHE   B  2  307 ? 16.426  -39.613 -1.297   1.00 50.06  ? 311  PHE   B CG   1 
ATOM   13694 C  CD1  . PHE   B  2  307 ? 15.349  -39.072 -1.979   1.00 53.55  ? 311  PHE   B CD1  1 
ATOM   13695 C  CD2  . PHE   B  2  307 ? 17.480  -38.783 -0.955   1.00 52.28  ? 311  PHE   B CD2  1 
ATOM   13696 C  CE1  . PHE   B  2  307 ? 15.317  -37.727 -2.296   1.00 56.00  ? 311  PHE   B CE1  1 
ATOM   13697 C  CE2  . PHE   B  2  307 ? 17.454  -37.439 -1.270   1.00 54.02  ? 311  PHE   B CE2  1 
ATOM   13698 C  CZ   . PHE   B  2  307 ? 16.373  -36.912 -1.944   1.00 53.69  ? 311  PHE   B CZ   1 
ATOM   13699 H  H    . PHE   B  2  307 ? 16.399  -40.901 1.518    1.00 57.55  ? 311  PHE   B H    1 
ATOM   13700 H  HA   . PHE   B  2  307 ? 14.510  -41.195 -0.350   1.00 57.71  ? 311  PHE   B HA   1 
ATOM   13701 H  HB2  . PHE   B  2  307 ? 17.324  -41.258 -0.543   1.00 58.82  ? 311  PHE   B HB2  1 
ATOM   13702 H  HB3  . PHE   B  2  307 ? 16.398  -41.571 -1.796   1.00 58.82  ? 311  PHE   B HB3  1 
ATOM   13703 H  HD1  . PHE   B  2  307 ? 14.639  -39.620 -2.226   1.00 64.30  ? 311  PHE   B HD1  1 
ATOM   13704 H  HD2  . PHE   B  2  307 ? 18.215  -39.136 -0.507   1.00 62.77  ? 311  PHE   B HD2  1 
ATOM   13705 H  HE1  . PHE   B  2  307 ? 14.584  -37.372 -2.746   1.00 67.24  ? 311  PHE   B HE1  1 
ATOM   13706 H  HE2  . PHE   B  2  307 ? 18.165  -36.891 -1.028   1.00 64.86  ? 311  PHE   B HE2  1 
ATOM   13707 H  HZ   . PHE   B  2  307 ? 16.356  -36.008 -2.161   1.00 64.46  ? 311  PHE   B HZ   1 
ATOM   13708 N  N    . ALA   B  2  308 ? 14.086  -43.612 -0.128   1.00 52.48  ? 312  ALA   B N    1 
ATOM   13709 C  CA   . ALA   B  2  308 ? 13.881  -45.054 -0.251   1.00 52.21  ? 312  ALA   B CA   1 
ATOM   13710 C  C    . ALA   B  2  308 ? 13.705  -45.361 -1.734   1.00 54.51  ? 312  ALA   B C    1 
ATOM   13711 O  O    . ALA   B  2  308 ? 12.601  -45.250 -2.273   1.00 58.04  ? 312  ALA   B O    1 
ATOM   13712 C  CB   . ALA   B  2  308 ? 12.673  -45.508 0.561    1.00 53.14  ? 312  ALA   B CB   1 
ATOM   13713 H  H    . ALA   B  2  308 ? 13.355  -43.160 -0.151   1.00 63.02  ? 312  ALA   B H    1 
ATOM   13714 H  HA   . ALA   B  2  308 ? 14.661  -45.526 0.081    1.00 62.68  ? 312  ALA   B HA   1 
ATOM   13715 H  HB1  . ALA   B  2  308 ? 12.571  -46.468 0.466    1.00 63.81  ? 312  ALA   B HB1  1 
ATOM   13716 H  HB2  . ALA   B  2  308 ? 12.817  -45.281 1.493    1.00 63.81  ? 312  ALA   B HB2  1 
ATOM   13717 H  HB3  . ALA   B  2  308 ? 11.882  -45.057 0.228    1.00 63.81  ? 312  ALA   B HB3  1 
ATOM   13718 N  N    . VAL   B  2  309 ? 14.794  -45.750 -2.397   1.00 54.68  ? 313  VAL   B N    1 
ATOM   13719 C  CA   . VAL   B  2  309 ? 14.795  -45.906 -3.844   1.00 53.55  ? 313  VAL   B CA   1 
ATOM   13720 C  C    . VAL   B  2  309 ? 15.452  -47.225 -4.225   1.00 54.64  ? 313  VAL   B C    1 
ATOM   13721 O  O    . VAL   B  2  309 ? 16.179  -47.840 -3.441   1.00 54.25  ? 313  VAL   B O    1 
ATOM   13722 C  CB   . VAL   B  2  309 ? 15.503  -44.725 -4.546   1.00 53.87  ? 313  VAL   B CB   1 
ATOM   13723 C  CG1  . VAL   B  2  309 ? 14.821  -43.412 -4.177   1.00 56.23  ? 313  VAL   B CG1  1 
ATOM   13724 C  CG2  . VAL   B  2  309 ? 16.980  -44.684 -4.181   1.00 49.64  ? 313  VAL   B CG2  1 
ATOM   13725 H  H    . VAL   B  2  309 ? 15.548  -45.931 -2.024   1.00 65.66  ? 313  VAL   B H    1 
ATOM   13726 H  HA   . VAL   B  2  309 ? 13.877  -45.947 -4.154   1.00 64.30  ? 313  VAL   B HA   1 
ATOM   13727 H  HB   . VAL   B  2  309 ? 15.441  -44.845 -5.506   1.00 64.68  ? 313  VAL   B HB   1 
ATOM   13728 H  HG11 . VAL   B  2  309 ? 15.278  -42.682 -4.623   1.00 67.51  ? 313  VAL   B HG11 1 
ATOM   13729 H  HG12 . VAL   B  2  309 ? 13.895  -43.447 -4.464   1.00 67.51  ? 313  VAL   B HG12 1 
ATOM   13730 H  HG13 . VAL   B  2  309 ? 14.865  -43.292 -3.216   1.00 67.51  ? 313  VAL   B HG13 1 
ATOM   13731 H  HG21 . VAL   B  2  309 ? 17.391  -43.919 -4.612   1.00 59.60  ? 313  VAL   B HG21 1 
ATOM   13732 H  HG22 . VAL   B  2  309 ? 17.065  -44.606 -3.218   1.00 59.60  ? 313  VAL   B HG22 1 
ATOM   13733 H  HG23 . VAL   B  2  309 ? 17.403  -45.502 -4.485   1.00 59.60  ? 313  VAL   B HG23 1 
ATOM   13734 N  N    . THR   B  2  310 ? 15.179  -47.653 -5.455   1.00 55.92  ? 314  THR   B N    1 
ATOM   13735 C  CA   . THR   B  2  310 ? 15.656  -48.936 -5.944   1.00 58.27  ? 314  THR   B CA   1 
ATOM   13736 C  C    . THR   B  2  310 ? 17.152  -48.873 -6.253   1.00 66.81  ? 314  THR   B C    1 
ATOM   13737 O  O    . THR   B  2  310 ? 17.778  -47.809 -6.244   1.00 62.22  ? 314  THR   B O    1 
ATOM   13738 C  CB   . THR   B  2  310 ? 14.872  -49.356 -7.188   1.00 52.55  ? 314  THR   B CB   1 
ATOM   13739 O  OG1  . THR   B  2  310 ? 14.894  -48.297 -8.154   1.00 52.16  ? 314  THR   B OG1  1 
ATOM   13740 C  CG2  . THR   B  2  310 ? 13.429  -49.681 -6.823   1.00 49.32  ? 314  THR   B CG2  1 
ATOM   13741 H  H    . THR   B  2  310 ? 14.715  -47.213 -6.030   1.00 67.14  ? 314  THR   B H    1 
ATOM   13742 H  HA   . THR   B  2  310 ? 15.521  -49.608 -5.259   1.00 69.97  ? 314  THR   B HA   1 
ATOM   13743 H  HB   . THR   B  2  310 ? 15.276  -50.149 -7.573   1.00 63.10  ? 314  THR   B HB   1 
ATOM   13744 H  HG1  . THR   B  2  310 ? 14.483  -48.533 -8.847   1.00 62.63  ? 314  THR   B HG1  1 
ATOM   13745 H  HG21 . THR   B  2  310 ? 12.943  -49.964 -7.612   1.00 59.22  ? 314  THR   B HG21 1 
ATOM   13746 H  HG22 . THR   B  2  310 ? 13.406  -50.394 -6.166   1.00 59.22  ? 314  THR   B HG22 1 
ATOM   13747 H  HG23 . THR   B  2  310 ? 12.997  -48.896 -6.451   1.00 59.22  ? 314  THR   B HG23 1 
ATOM   13748 N  N    . GLN   B  2  311 ? 17.720  -50.046 -6.539   1.00 81.87  ? 315  GLN   B N    1 
ATOM   13749 C  CA   . GLN   B  2  311 ? 19.164  -50.155 -6.720   1.00 93.73  ? 315  GLN   B CA   1 
ATOM   13750 C  C    . GLN   B  2  311 ? 19.657  -49.262 -7.849   1.00 85.31  ? 315  GLN   B C    1 
ATOM   13751 O  O    . GLN   B  2  311 ? 20.708  -48.620 -7.731   1.00 78.24  ? 315  GLN   B O    1 
ATOM   13752 C  CB   . GLN   B  2  311 ? 19.538  -51.611 -6.992   1.00 110.32 ? 315  GLN   B CB   1 
ATOM   13753 C  CG   . GLN   B  2  311 ? 21.017  -51.854 -7.187   1.00 124.56 ? 315  GLN   B CG   1 
ATOM   13754 C  CD   . GLN   B  2  311 ? 21.334  -53.330 -7.291   1.00 132.56 ? 315  GLN   B CD   1 
ATOM   13755 O  OE1  . GLN   B  2  311 ? 20.441  -54.173 -7.202   1.00 128.74 ? 315  GLN   B OE1  1 
ATOM   13756 N  NE2  . GLN   B  2  311 ? 22.606  -53.653 -7.477   1.00 134.24 ? 315  GLN   B NE2  1 
ATOM   13757 H  H    . GLN   B  2  311 ? 17.294  -50.788 -6.633   1.00 98.28  ? 315  GLN   B H    1 
ATOM   13758 H  HA   . GLN   B  2  311 ? 19.603  -49.869 -5.903   1.00 112.52 ? 315  GLN   B HA   1 
ATOM   13759 H  HB2  . GLN   B  2  311 ? 19.249  -52.149 -6.238   1.00 132.43 ? 315  GLN   B HB2  1 
ATOM   13760 H  HB3  . GLN   B  2  311 ? 19.084  -51.900 -7.799   1.00 132.43 ? 315  GLN   B HB3  1 
ATOM   13761 H  HG2  . GLN   B  2  311 ? 21.306  -51.422 -8.006   1.00 149.51 ? 315  GLN   B HG2  1 
ATOM   13762 H  HG3  . GLN   B  2  311 ? 21.503  -51.490 -6.431   1.00 149.51 ? 315  GLN   B HG3  1 
ATOM   13763 H  HE21 . GLN   B  2  311 ? 23.202  -53.035 -7.533   1.00 161.13 ? 315  GLN   B HE21 1 
ATOM   13764 H  HE22 . GLN   B  2  311 ? 22.834  -54.479 -7.542   1.00 161.13 ? 315  GLN   B HE22 1 
ATOM   13765 N  N    . GLU   B  2  312 ? 18.913  -49.208 -8.955   1.00 82.45  ? 316  GLU   B N    1 
ATOM   13766 C  CA   . GLU   B  2  312 ? 19.353  -48.436 -10.109  1.00 77.12  ? 316  GLU   B CA   1 
ATOM   13767 C  C    . GLU   B  2  312 ? 19.500  -46.954 -9.791   1.00 64.37  ? 316  GLU   B C    1 
ATOM   13768 O  O    . GLU   B  2  312 ? 20.231  -46.250 -10.497  1.00 63.22  ? 316  GLU   B O    1 
ATOM   13769 C  CB   . GLU   B  2  312 ? 18.370  -48.615 -11.271  1.00 85.44  ? 316  GLU   B CB   1 
ATOM   13770 C  CG   . GLU   B  2  312 ? 18.258  -50.042 -11.803  1.00 99.47  ? 316  GLU   B CG   1 
ATOM   13771 C  CD   . GLU   B  2  312 ? 17.477  -50.961 -10.882  1.00 111.96 ? 316  GLU   B CD   1 
ATOM   13772 O  OE1  . GLU   B  2  312 ? 16.882  -50.459 -9.905   1.00 116.59 ? 316  GLU   B OE1  1 
ATOM   13773 O  OE2  . GLU   B  2  312 ? 17.461  -52.185 -11.132  1.00 119.94 ? 316  GLU   B OE2  1 
ATOM   13774 H  H    . GLU   B  2  312 ? 18.158  -49.607 -9.059   1.00 98.97  ? 316  GLU   B H    1 
ATOM   13775 H  HA   . GLU   B  2  312 ? 20.219  -48.771 -10.390  1.00 92.58  ? 316  GLU   B HA   1 
ATOM   13776 H  HB2  . GLU   B  2  312 ? 17.488  -48.346 -10.971  1.00 102.57 ? 316  GLU   B HB2  1 
ATOM   13777 H  HB3  . GLU   B  2  312 ? 18.657  -48.052 -12.006  1.00 102.57 ? 316  GLU   B HB3  1 
ATOM   13778 H  HG2  . GLU   B  2  312 ? 17.806  -50.024 -12.661  1.00 119.41 ? 316  GLU   B HG2  1 
ATOM   13779 H  HG3  . GLU   B  2  312 ? 19.149  -50.411 -11.906  1.00 119.41 ? 316  GLU   B HG3  1 
ATOM   13780 N  N    . GLN   B  2  313 ? 18.834  -46.467 -8.743   1.00 56.12  ? 317  GLN   B N    1 
ATOM   13781 C  CA   . GLN   B  2  313 ? 18.787  -45.046 -8.435   1.00 50.29  ? 317  GLN   B CA   1 
ATOM   13782 C  C    . GLN   B  2  313 ? 19.607  -44.658 -7.213   1.00 46.60  ? 317  GLN   B C    1 
ATOM   13783 O  O    . GLN   B  2  313 ? 19.711  -43.464 -6.912   1.00 42.10  ? 317  GLN   B O    1 
ATOM   13784 C  CB   . GLN   B  2  313 ? 17.334  -44.607 -8.210   1.00 51.37  ? 317  GLN   B CB   1 
ATOM   13785 C  CG   . GLN   B  2  313 ? 16.398  -44.932 -9.355   1.00 55.92  ? 317  GLN   B CG   1 
ATOM   13786 C  CD   . GLN   B  2  313 ? 16.736  -44.169 -10.616  1.00 56.75  ? 317  GLN   B CD   1 
ATOM   13787 O  OE1  . GLN   B  2  313 ? 17.319  -43.086 -10.564  1.00 57.62  ? 317  GLN   B OE1  1 
ATOM   13788 N  NE2  . GLN   B  2  313 ? 16.375  -44.733 -11.761  1.00 61.34  ? 317  GLN   B NE2  1 
ATOM   13789 H  H    . GLN   B  2  313 ? 18.395  -46.954 -8.187   1.00 67.38  ? 317  GLN   B H    1 
ATOM   13790 H  HA   . GLN   B  2  313 ? 19.146  -44.566 -9.197   1.00 60.38  ? 317  GLN   B HA   1 
ATOM   13791 H  HB2  . GLN   B  2  313 ? 16.996  -45.054 -7.418   1.00 61.68  ? 317  GLN   B HB2  1 
ATOM   13792 H  HB3  . GLN   B  2  313 ? 17.318  -43.646 -8.082   1.00 61.68  ? 317  GLN   B HB3  1 
ATOM   13793 H  HG2  . GLN   B  2  313 ? 16.456  -45.880 -9.552   1.00 67.14  ? 317  GLN   B HG2  1 
ATOM   13794 H  HG3  . GLN   B  2  313 ? 15.492  -44.702 -9.098   1.00 67.14  ? 317  GLN   B HG3  1 
ATOM   13795 H  HE21 . GLN   B  2  313 ? 15.971  -45.492 -11.758  1.00 73.64  ? 317  GLN   B HE21 1 
ATOM   13796 H  HE22 . GLN   B  2  313 ? 16.544  -44.339 -12.507  1.00 73.64  ? 317  GLN   B HE22 1 
ATOM   13797 N  N    . VAL   B  2  314 ? 20.191  -45.622 -6.502   1.00 49.76  ? 318  VAL   B N    1 
ATOM   13798 C  CA   . VAL   B  2  314 ? 20.803  -45.318 -5.211   1.00 56.75  ? 318  VAL   B CA   1 
ATOM   13799 C  C    . VAL   B  2  314 ? 21.950  -44.329 -5.376   1.00 56.48  ? 318  VAL   B C    1 
ATOM   13800 O  O    . VAL   B  2  314 ? 21.998  -43.292 -4.703   1.00 57.82  ? 318  VAL   B O    1 
ATOM   13801 C  CB   . VAL   B  2  314 ? 21.267  -46.614 -4.523   1.00 63.16  ? 318  VAL   B CB   1 
ATOM   13802 C  CG1  . VAL   B  2  314 ? 22.357  -46.320 -3.509   1.00 67.29  ? 318  VAL   B CG1  1 
ATOM   13803 C  CG2  . VAL   B  2  314 ? 20.086  -47.297 -3.847   1.00 65.30  ? 318  VAL   B CG2  1 
ATOM   13804 H  H    . VAL   B  2  314 ? 20.246  -46.446 -6.741   1.00 59.75  ? 318  VAL   B H    1 
ATOM   13805 H  HA   . VAL   B  2  314 ? 20.133  -44.899 -4.647   1.00 68.13  ? 318  VAL   B HA   1 
ATOM   13806 H  HB   . VAL   B  2  314 ? 21.633  -47.213 -5.192   1.00 75.83  ? 318  VAL   B HB   1 
ATOM   13807 H  HG11 . VAL   B  2  314 ? 22.627  -47.151 -3.087   1.00 80.79  ? 318  VAL   B HG11 1 
ATOM   13808 H  HG12 . VAL   B  2  314 ? 23.113  -45.919 -3.965   1.00 80.79  ? 318  VAL   B HG12 1 
ATOM   13809 H  HG13 . VAL   B  2  314 ? 22.010  -45.708 -2.841   1.00 80.79  ? 318  VAL   B HG13 1 
ATOM   13810 H  HG21 . VAL   B  2  314 ? 20.399  -48.098 -3.398   1.00 78.39  ? 318  VAL   B HG21 1 
ATOM   13811 H  HG22 . VAL   B  2  314 ? 19.695  -46.687 -3.202   1.00 78.39  ? 318  VAL   B HG22 1 
ATOM   13812 H  HG23 . VAL   B  2  314 ? 19.429  -47.532 -4.521   1.00 78.39  ? 318  VAL   B HG23 1 
ATOM   13813 N  N    . HIS   B  2  315 ? 22.905  -44.645 -6.253   1.00 57.74  ? 319  HIS   B N    1 
ATOM   13814 C  CA   . HIS   B  2  315 ? 24.086  -43.798 -6.391   1.00 63.56  ? 319  HIS   B CA   1 
ATOM   13815 C  C    . HIS   B  2  315 ? 23.695  -42.358 -6.700   1.00 58.63  ? 319  HIS   B C    1 
ATOM   13816 O  O    . HIS   B  2  315 ? 24.285  -41.416 -6.157   1.00 58.29  ? 319  HIS   B O    1 
ATOM   13817 C  CB   . HIS   B  2  315 ? 25.005  -44.354 -7.479   1.00 71.94  ? 319  HIS   B CB   1 
ATOM   13818 C  CG   . HIS   B  2  315 ? 26.345  -43.690 -7.538   1.00 83.94  ? 319  HIS   B CG   1 
ATOM   13819 N  ND1  . HIS   B  2  315 ? 26.762  -42.950 -8.623   1.00 88.20  ? 319  HIS   B ND1  1 
ATOM   13820 C  CD2  . HIS   B  2  315 ? 27.364  -43.656 -6.647   1.00 88.59  ? 319  HIS   B CD2  1 
ATOM   13821 C  CE1  . HIS   B  2  315 ? 27.979  -42.489 -8.398   1.00 91.26  ? 319  HIS   B CE1  1 
ATOM   13822 N  NE2  . HIS   B  2  315 ? 28.367  -42.903 -7.206   1.00 90.21  ? 319  HIS   B NE2  1 
ATOM   13823 H  H    . HIS   B  2  315 ? 22.892  -45.333 -6.770   1.00 69.33  ? 319  HIS   B H    1 
ATOM   13824 H  HA   . HIS   B  2  315 ? 24.576  -43.802 -5.554   1.00 76.31  ? 319  HIS   B HA   1 
ATOM   13825 H  HB2  . HIS   B  2  315 ? 25.150  -45.298 -7.311   1.00 86.37  ? 319  HIS   B HB2  1 
ATOM   13826 H  HB3  . HIS   B  2  315 ? 24.576  -44.233 -8.340   1.00 86.37  ? 319  HIS   B HB3  1 
ATOM   13827 H  HD2  . HIS   B  2  315 ? 27.381  -44.066 -5.812   1.00 106.34 ? 319  HIS   B HD2  1 
ATOM   13828 H  HE1  . HIS   B  2  315 ? 28.478  -41.963 -8.980   1.00 109.55 ? 319  HIS   B HE1  1 
ATOM   13829 H  HE2  . HIS   B  2  315 ? 29.125  -42.729 -6.838   1.00 108.29 ? 319  HIS   B HE2  1 
ATOM   13830 N  N    . LEU   B  2  316 ? 22.698  -42.168 -7.564   1.00 56.61  ? 320  LEU   B N    1 
ATOM   13831 C  CA   . LEU   B  2  316 ? 22.216  -40.826 -7.868   1.00 55.00  ? 320  LEU   B CA   1 
ATOM   13832 C  C    . LEU   B  2  316 ? 21.732  -40.122 -6.606   1.00 53.35  ? 320  LEU   B C    1 
ATOM   13833 O  O    . LEU   B  2  316 ? 22.191  -39.024 -6.273   1.00 50.90  ? 320  LEU   B O    1 
ATOM   13834 C  CB   . LEU   B  2  316 ? 21.095  -40.906 -8.905   1.00 54.33  ? 320  LEU   B CB   1 
ATOM   13835 C  CG   . LEU   B  2  316 ? 20.380  -39.609 -9.283   1.00 56.06  ? 320  LEU   B CG   1 
ATOM   13836 C  CD1  . LEU   B  2  316 ? 21.289  -38.686 -10.080  1.00 59.19  ? 320  LEU   B CD1  1 
ATOM   13837 C  CD2  . LEU   B  2  316 ? 19.125  -39.943 -10.063  1.00 59.83  ? 320  LEU   B CD2  1 
ATOM   13838 H  H    . LEU   B  2  316 ? 22.287  -42.797 -7.983   1.00 67.96  ? 320  LEU   B H    1 
ATOM   13839 H  HA   . LEU   B  2  316 ? 22.944  -40.305 -8.244   1.00 66.04  ? 320  LEU   B HA   1 
ATOM   13840 H  HB2  . LEU   B  2  316 ? 21.474  -41.265 -9.722   1.00 65.23  ? 320  LEU   B HB2  1 
ATOM   13841 H  HB3  . LEU   B  2  316 ? 20.417  -41.509 -8.560   1.00 65.23  ? 320  LEU   B HB3  1 
ATOM   13842 H  HG   . LEU   B  2  316 ? 20.134  -39.128 -8.477   1.00 67.31  ? 320  LEU   B HG   1 
ATOM   13843 H  HD11 . LEU   B  2  316 ? 20.774  -37.923 -10.387  1.00 71.06  ? 320  LEU   B HD11 1 
ATOM   13844 H  HD12 . LEU   B  2  316 ? 22.015  -38.387 -9.510   1.00 71.06  ? 320  LEU   B HD12 1 
ATOM   13845 H  HD13 . LEU   B  2  316 ? 21.644  -39.172 -10.841  1.00 71.06  ? 320  LEU   B HD13 1 
ATOM   13846 H  HD21 . LEU   B  2  316 ? 18.664  -39.120 -10.287  1.00 71.83  ? 320  LEU   B HD21 1 
ATOM   13847 H  HD22 . LEU   B  2  316 ? 19.373  -40.415 -10.873  1.00 71.83  ? 320  LEU   B HD22 1 
ATOM   13848 H  HD23 . LEU   B  2  316 ? 18.553  -40.504 -9.515   1.00 71.83  ? 320  LEU   B HD23 1 
ATOM   13849 N  N    . TYR   B  2  317 ? 20.799  -40.750 -5.887   1.00 51.56  ? 321  TYR   B N    1 
ATOM   13850 C  CA   . TYR   B  2  317 ? 20.206  -40.117 -4.717   1.00 49.58  ? 321  TYR   B CA   1 
ATOM   13851 C  C    . TYR   B  2  317 ? 21.174  -40.023 -3.547   1.00 50.87  ? 321  TYR   B C    1 
ATOM   13852 O  O    . TYR   B  2  317 ? 20.980  -39.175 -2.669   1.00 50.45  ? 321  TYR   B O    1 
ATOM   13853 C  CB   . TYR   B  2  317 ? 18.948  -40.877 -4.300   1.00 49.64  ? 321  TYR   B CB   1 
ATOM   13854 C  CG   . TYR   B  2  317 ? 17.756  -40.577 -5.178   1.00 45.22  ? 321  TYR   B CG   1 
ATOM   13855 C  CD1  . TYR   B  2  317 ? 16.916  -39.510 -4.893   1.00 43.10  ? 321  TYR   B CD1  1 
ATOM   13856 C  CD2  . TYR   B  2  317 ? 17.479  -41.350 -6.297   1.00 44.51  ? 321  TYR   B CD2  1 
ATOM   13857 C  CE1  . TYR   B  2  317 ? 15.828  -39.226 -5.693   1.00 41.39  ? 321  TYR   B CE1  1 
ATOM   13858 C  CE2  . TYR   B  2  317 ? 16.393  -41.073 -7.104   1.00 45.32  ? 321  TYR   B CE2  1 
ATOM   13859 C  CZ   . TYR   B  2  317 ? 15.570  -40.011 -6.796   1.00 43.87  ? 321  TYR   B CZ   1 
ATOM   13860 O  OH   . TYR   B  2  317 ? 14.486  -39.732 -7.596   1.00 47.44  ? 321  TYR   B OH   1 
ATOM   13861 H  H    . TYR   B  2  317 ? 20.496  -41.536 -6.058   1.00 61.91  ? 321  TYR   B H    1 
ATOM   13862 H  HA   . TYR   B  2  317 ? 19.947  -39.212 -4.951   1.00 59.53  ? 321  TYR   B HA   1 
ATOM   13863 H  HB2  . TYR   B  2  317 ? 19.124  -41.830 -4.351   1.00 59.60  ? 321  TYR   B HB2  1 
ATOM   13864 H  HB3  . TYR   B  2  317 ? 18.719  -40.631 -3.390   1.00 59.60  ? 321  TYR   B HB3  1 
ATOM   13865 H  HD1  . TYR   B  2  317 ? 17.088  -38.978 -4.150   1.00 51.76  ? 321  TYR   B HD1  1 
ATOM   13866 H  HD2  . TYR   B  2  317 ? 18.033  -42.066 -6.507   1.00 53.44  ? 321  TYR   B HD2  1 
ATOM   13867 H  HE1  . TYR   B  2  317 ? 15.272  -38.509 -5.489   1.00 49.71  ? 321  TYR   B HE1  1 
ATOM   13868 H  HE2  . TYR   B  2  317 ? 16.218  -41.600 -7.850   1.00 54.42  ? 321  TYR   B HE2  1 
ATOM   13869 H  HH   . TYR   B  2  317 ? 14.292  -40.404 -8.061   1.00 56.97  ? 321  TYR   B HH   1 
ATOM   13870 N  N    . GLU   B  2  318 ? 22.203  -40.867 -3.506   1.00 57.86  ? 322  GLU   B N    1 
ATOM   13871 C  CA   . GLU   B  2  318 ? 23.237  -40.693 -2.492   1.00 63.42  ? 322  GLU   B CA   1 
ATOM   13872 C  C    . GLU   B  2  318 ? 24.011  -39.405 -2.725   1.00 65.22  ? 322  GLU   B C    1 
ATOM   13873 O  O    . GLU   B  2  318 ? 24.308  -38.672 -1.776   1.00 66.13  ? 322  GLU   B O    1 
ATOM   13874 C  CB   . GLU   B  2  318 ? 24.175  -41.895 -2.484   1.00 70.07  ? 322  GLU   B CB   1 
ATOM   13875 C  CG   . GLU   B  2  318 ? 23.691  -43.003 -1.580   1.00 78.52  ? 322  GLU   B CG   1 
ATOM   13876 C  CD   . GLU   B  2  318 ? 24.543  -44.240 -1.673   1.00 91.88  ? 322  GLU   B CD   1 
ATOM   13877 O  OE1  . GLU   B  2  318 ? 25.150  -44.472 -2.739   1.00 97.08  ? 322  GLU   B OE1  1 
ATOM   13878 O  OE2  . GLU   B  2  318 ? 24.630  -44.970 -0.669   1.00 99.22  ? 322  GLU   B OE2  1 
ATOM   13879 H  H    . GLU   B  2  318 ? 22.323  -41.532 -4.039   1.00 69.47  ? 322  GLU   B H    1 
ATOM   13880 H  HA   . GLU   B  2  318 ? 22.818  -40.641 -1.619   1.00 76.14  ? 322  GLU   B HA   1 
ATOM   13881 H  HB2  . GLU   B  2  318 ? 24.242  -42.249 -3.384   1.00 84.13  ? 322  GLU   B HB2  1 
ATOM   13882 H  HB3  . GLU   B  2  318 ? 25.048  -41.612 -2.172   1.00 84.13  ? 322  GLU   B HB3  1 
ATOM   13883 H  HG2  . GLU   B  2  318 ? 23.710  -42.693 -0.661   1.00 94.27  ? 322  GLU   B HG2  1 
ATOM   13884 H  HG3  . GLU   B  2  318 ? 22.785  -43.243 -1.830   1.00 94.27  ? 322  GLU   B HG3  1 
ATOM   13885 N  N    . ASN   B  2  319 ? 24.336  -39.107 -3.984   1.00 67.34  ? 323  ASN   B N    1 
ATOM   13886 C  CA   . ASN   B  2  319 ? 25.000  -37.846 -4.292   1.00 66.90  ? 323  ASN   B CA   1 
ATOM   13887 C  C    . ASN   B  2  319 ? 24.119  -36.661 -3.919   1.00 61.99  ? 323  ASN   B C    1 
ATOM   13888 O  O    . ASN   B  2  319 ? 24.612  -35.651 -3.403   1.00 66.36  ? 323  ASN   B O    1 
ATOM   13889 C  CB   . ASN   B  2  319 ? 25.372  -37.802 -5.772   1.00 68.09  ? 323  ASN   B CB   1 
ATOM   13890 C  CG   . ASN   B  2  319 ? 26.576  -38.663 -6.093   1.00 75.02  ? 323  ASN   B CG   1 
ATOM   13891 O  OD1  . ASN   B  2  319 ? 26.469  -39.664 -6.801   1.00 74.81  ? 323  ASN   B OD1  1 
ATOM   13892 N  ND2  . ASN   B  2  319 ? 27.735  -38.275 -5.573   1.00 82.33  ? 323  ASN   B ND2  1 
ATOM   13893 H  H    . ASN   B  2  319 ? 24.185  -39.610 -4.665   1.00 80.85  ? 323  ASN   B H    1 
ATOM   13894 H  HA   . ASN   B  2  319 ? 25.819  -37.784 -3.777   1.00 80.32  ? 323  ASN   B HA   1 
ATOM   13895 H  HB2  . ASN   B  2  319 ? 24.623  -38.124 -6.298   1.00 81.74  ? 323  ASN   B HB2  1 
ATOM   13896 H  HB3  . ASN   B  2  319 ? 25.582  -36.888 -6.019   1.00 81.74  ? 323  ASN   B HB3  1 
ATOM   13897 H  HD21 . ASN   B  2  319 ? 28.449  -38.730 -5.726   1.00 98.83  ? 323  ASN   B HD21 1 
ATOM   13898 H  HD22 . ASN   B  2  319 ? 27.772  -37.568 -5.084   1.00 98.83  ? 323  ASN   B HD22 1 
ATOM   13899 N  N    . TYR   B  2  320 ? 22.812  -36.762 -4.172   1.00 55.26  ? 324  TYR   B N    1 
ATOM   13900 C  CA   . TYR   B  2  320 ? 21.894  -35.722 -3.720   1.00 53.65  ? 324  TYR   B CA   1 
ATOM   13901 C  C    . TYR   B  2  320 ? 21.923  -35.602 -2.200   1.00 47.82  ? 324  TYR   B C    1 
ATOM   13902 O  O    . TYR   B  2  320 ? 22.006  -34.497 -1.653   1.00 49.52  ? 324  TYR   B O    1 
ATOM   13903 C  CB   . TYR   B  2  320 ? 20.472  -36.020 -4.202   1.00 54.42  ? 324  TYR   B CB   1 
ATOM   13904 C  CG   . TYR   B  2  320 ? 20.205  -35.762 -5.675   1.00 55.48  ? 324  TYR   B CG   1 
ATOM   13905 C  CD1  . TYR   B  2  320 ? 20.977  -34.867 -6.409   1.00 62.33  ? 324  TYR   B CD1  1 
ATOM   13906 C  CD2  . TYR   B  2  320 ? 19.165  -36.413 -6.327   1.00 54.85  ? 324  TYR   B CD2  1 
ATOM   13907 C  CE1  . TYR   B  2  320 ? 20.722  -34.634 -7.751   1.00 67.19  ? 324  TYR   B CE1  1 
ATOM   13908 C  CE2  . TYR   B  2  320 ? 18.905  -36.187 -7.665   1.00 56.07  ? 324  TYR   B CE2  1 
ATOM   13909 C  CZ   . TYR   B  2  320 ? 19.684  -35.298 -8.372   1.00 66.26  ? 324  TYR   B CZ   1 
ATOM   13910 O  OH   . TYR   B  2  320 ? 19.422  -35.074 -9.704   1.00 73.94  ? 324  TYR   B OH   1 
ATOM   13911 H  H    . TYR   B  2  320 ? 22.441  -37.412 -4.596   1.00 66.35  ? 324  TYR   B H    1 
ATOM   13912 H  HA   . TYR   B  2  320 ? 22.170  -34.876 -4.106   1.00 64.42  ? 324  TYR   B HA   1 
ATOM   13913 H  HB2  . TYR   B  2  320 ? 20.284  -36.957 -4.035   1.00 65.34  ? 324  TYR   B HB2  1 
ATOM   13914 H  HB3  . TYR   B  2  320 ? 19.858  -35.464 -3.697   1.00 65.34  ? 324  TYR   B HB3  1 
ATOM   13915 H  HD1  . TYR   B  2  320 ? 21.675  -34.416 -5.992   1.00 74.83  ? 324  TYR   B HD1  1 
ATOM   13916 H  HD2  . TYR   B  2  320 ? 18.634  -37.011 -5.854   1.00 65.86  ? 324  TYR   B HD2  1 
ATOM   13917 H  HE1  . TYR   B  2  320 ? 21.247  -34.035 -8.230   1.00 80.66  ? 324  TYR   B HE1  1 
ATOM   13918 H  HE2  . TYR   B  2  320 ? 18.206  -36.633 -8.087   1.00 67.32  ? 324  TYR   B HE2  1 
ATOM   13919 H  HH   . TYR   B  2  320 ? 18.768  -35.540 -9.950   1.00 88.76  ? 324  TYR   B HH   1 
ATOM   13920 N  N    . ALA   B  2  321 ? 21.862  -36.738 -1.499   1.00 44.96  ? 325  ALA   B N    1 
ATOM   13921 C  CA   . ALA   B  2  321 ? 21.838  -36.713 -0.041   1.00 47.74  ? 325  ALA   B CA   1 
ATOM   13922 C  C    . ALA   B  2  321 ? 23.124  -36.152 0.549    1.00 57.71  ? 325  ALA   B C    1 
ATOM   13923 O  O    . ALA   B  2  321 ? 23.104  -35.651 1.679    1.00 63.90  ? 325  ALA   B O    1 
ATOM   13924 C  CB   . ALA   B  2  321 ? 21.585  -38.119 0.506    1.00 42.09  ? 325  ALA   B CB   1 
ATOM   13925 H  H    . ALA   B  2  321 ? 21.835  -37.526 -1.843   1.00 53.99  ? 325  ALA   B H    1 
ATOM   13926 H  HA   . ALA   B  2  321 ? 21.105  -36.144 0.244    1.00 57.32  ? 325  ALA   B HA   1 
ATOM   13927 H  HB1  . ALA   B  2  321 ? 21.580  -38.084 1.476    1.00 50.55  ? 325  ALA   B HB1  1 
ATOM   13928 H  HB2  . ALA   B  2  321 ? 20.727  -38.435 0.182    1.00 50.55  ? 325  ALA   B HB2  1 
ATOM   13929 H  HB3  . ALA   B  2  321 ? 22.292  -38.709 0.200    1.00 50.55  ? 325  ALA   B HB3  1 
ATOM   13930 N  N    . LYS   B  2  322 ? 24.241  -36.232 -0.177   1.00 59.72  ? 326  LYS   B N    1 
ATOM   13931 C  CA   . LYS   B  2  322 ? 25.467  -35.600 0.297    1.00 66.51  ? 326  LYS   B CA   1 
ATOM   13932 C  C    . LYS   B  2  322 ? 25.268  -34.101 0.488    1.00 67.57  ? 326  LYS   B C    1 
ATOM   13933 O  O    . LYS   B  2  322 ? 25.791  -33.512 1.442    1.00 73.81  ? 326  LYS   B O    1 
ATOM   13934 C  CB   . LYS   B  2  322 ? 26.614  -35.861 -0.682   1.00 71.90  ? 326  LYS   B CB   1 
ATOM   13935 C  CG   . LYS   B  2  322 ? 27.075  -37.311 -0.756   1.00 73.55  ? 326  LYS   B CG   1 
ATOM   13936 C  CD   . LYS   B  2  322 ? 28.269  -37.468 -1.692   1.00 78.54  ? 326  LYS   B CD   1 
ATOM   13937 C  CE   . LYS   B  2  322 ? 28.564  -38.931 -1.993   1.00 88.17  ? 326  LYS   B CE   1 
ATOM   13938 N  NZ   . LYS   B  2  322 ? 29.705  -39.096 -2.940   1.00 99.60  ? 326  LYS   B NZ   1 
ATOM   13939 H  H    . LYS   B  2  322 ? 24.313  -36.637 -0.932   1.00 71.70  ? 326  LYS   B H    1 
ATOM   13940 H  HA   . LYS   B  2  322 ? 25.708  -35.991 1.152    1.00 79.84  ? 326  LYS   B HA   1 
ATOM   13941 H  HB2  . LYS   B  2  322 ? 26.324  -35.601 -1.571   1.00 86.32  ? 326  LYS   B HB2  1 
ATOM   13942 H  HB3  . LYS   B  2  322 ? 27.377  -35.326 -0.413   1.00 86.32  ? 326  LYS   B HB3  1 
ATOM   13943 H  HG2  . LYS   B  2  322 ? 27.338  -37.611 0.128    1.00 88.30  ? 326  LYS   B HG2  1 
ATOM   13944 H  HG3  . LYS   B  2  322 ? 26.350  -37.863 -1.091   1.00 88.30  ? 326  LYS   B HG3  1 
ATOM   13945 H  HD2  . LYS   B  2  322 ? 28.080  -37.017 -2.530   1.00 94.29  ? 326  LYS   B HD2  1 
ATOM   13946 H  HD3  . LYS   B  2  322 ? 29.054  -37.079 -1.276   1.00 94.29  ? 326  LYS   B HD3  1 
ATOM   13947 H  HE2  . LYS   B  2  322 ? 28.790  -39.387 -1.167   1.00 105.84 ? 326  LYS   B HE2  1 
ATOM   13948 H  HE3  . LYS   B  2  322 ? 27.780  -39.338 -2.393   1.00 105.84 ? 326  LYS   B HE3  1 
ATOM   13949 H  HZ1  . LYS   B  2  322 ? 29.855  -39.960 -3.089   1.00 119.55 ? 326  LYS   B HZ1  1 
ATOM   13950 H  HZ2  . LYS   B  2  322 ? 29.519  -38.697 -3.713   1.00 119.55 ? 326  LYS   B HZ2  1 
ATOM   13951 H  HZ3  . LYS   B  2  322 ? 30.441  -38.730 -2.597   1.00 119.55 ? 326  LYS   B HZ3  1 
ATOM   13952 N  N    . LEU   B  2  323 ? 24.506  -33.469 -0.408   1.00 62.34  ? 327  LEU   B N    1 
ATOM   13953 C  CA   . LEU   B  2  323 ? 24.320  -32.024 -0.356   1.00 56.92  ? 327  LEU   B CA   1 
ATOM   13954 C  C    . LEU   B  2  323 ? 23.280  -31.612 0.677    1.00 58.47  ? 327  LEU   B C    1 
ATOM   13955 O  O    . LEU   B  2  323 ? 23.354  -30.501 1.214    1.00 61.66  ? 327  LEU   B O    1 
ATOM   13956 C  CB   . LEU   B  2  323 ? 23.902  -31.502 -1.734   1.00 53.28  ? 327  LEU   B CB   1 
ATOM   13957 C  CG   . LEU   B  2  323 ? 24.775  -31.921 -2.920   1.00 55.63  ? 327  LEU   B CG   1 
ATOM   13958 C  CD1  . LEU   B  2  323 ? 24.146  -31.512 -4.249   1.00 56.92  ? 327  LEU   B CD1  1 
ATOM   13959 C  CD2  . LEU   B  2  323 ? 26.163  -31.323 -2.791   1.00 59.40  ? 327  LEU   B CD2  1 
ATOM   13960 H  H    . LEU   B  2  323 ? 24.087  -33.856 -1.052   1.00 74.84  ? 327  LEU   B H    1 
ATOM   13961 H  HA   . LEU   B  2  323 ? 25.165  -31.615 -0.114   1.00 68.35  ? 327  LEU   B HA   1 
ATOM   13962 H  HB2  . LEU   B  2  323 ? 23.004  -31.821 -1.916   1.00 63.97  ? 327  LEU   B HB2  1 
ATOM   13963 H  HB3  . LEU   B  2  323 ? 23.910  -30.533 -1.703   1.00 63.97  ? 327  LEU   B HB3  1 
ATOM   13964 H  HG   . LEU   B  2  323 ? 24.851  -32.888 -2.917   1.00 66.79  ? 327  LEU   B HG   1 
ATOM   13965 H  HD11 . LEU   B  2  323 ? 24.703  -31.834 -4.974   1.00 68.34  ? 327  LEU   B HD11 1 
ATOM   13966 H  HD12 . LEU   B  2  323 ? 23.261  -31.904 -4.313   1.00 68.34  ? 327  LEU   B HD12 1 
ATOM   13967 H  HD13 . LEU   B  2  323 ? 24.083  -30.545 -4.284   1.00 68.34  ? 327  LEU   B HD13 1 
ATOM   13968 H  HD21 . LEU   B  2  323 ? 26.701  -31.606 -3.547   1.00 71.32  ? 327  LEU   B HD21 1 
ATOM   13969 H  HD22 . LEU   B  2  323 ? 26.091  -30.355 -2.780   1.00 71.32  ? 327  LEU   B HD22 1 
ATOM   13970 H  HD23 . LEU   B  2  323 ? 26.565  -31.633 -1.964   1.00 71.32  ? 327  LEU   B HD23 1 
ATOM   13971 N  N    . ILE   B  2  324 ? 22.318  -32.479 0.970    1.00 57.13  ? 328  ILE   B N    1 
ATOM   13972 C  CA   . ILE   B  2  324 ? 21.161  -32.126 1.786    1.00 57.05  ? 328  ILE   B CA   1 
ATOM   13973 C  C    . ILE   B  2  324 ? 21.481  -32.469 3.238    1.00 60.97  ? 328  ILE   B C    1 
ATOM   13974 O  O    . ILE   B  2  324 ? 21.782  -33.636 3.531    1.00 64.01  ? 328  ILE   B O    1 
ATOM   13975 C  CB   . ILE   B  2  324 ? 19.905  -32.868 1.312    1.00 57.14  ? 328  ILE   B CB   1 
ATOM   13976 C  CG1  . ILE   B  2  324 ? 19.695  -32.640 -0.187   1.00 55.08  ? 328  ILE   B CG1  1 
ATOM   13977 C  CG2  . ILE   B  2  324 ? 18.686  -32.402 2.099    1.00 58.36  ? 328  ILE   B CG2  1 
ATOM   13978 C  CD1  . ILE   B  2  324 ? 18.630  -33.517 -0.796   1.00 55.17  ? 328  ILE   B CD1  1 
ATOM   13979 H  H    . ILE   B  2  324 ? 22.313  -33.297 0.701    1.00 68.59  ? 328  ILE   B H    1 
ATOM   13980 H  HA   . ILE   B  2  324 ? 21.000  -31.172 1.725    1.00 68.50  ? 328  ILE   B HA   1 
ATOM   13981 H  HB   . ILE   B  2  324 ? 20.027  -33.817 1.469    1.00 68.61  ? 328  ILE   B HB   1 
ATOM   13982 H  HG12 . ILE   B  2  324 ? 19.432  -31.717 -0.328   1.00 66.13  ? 328  ILE   B HG12 1 
ATOM   13983 H  HG13 . ILE   B  2  324 ? 20.528  -32.822 -0.650   1.00 66.13  ? 328  ILE   B HG13 1 
ATOM   13984 H  HG21 . ILE   B  2  324 ? 17.903  -32.874 1.776    1.00 70.06  ? 328  ILE   B HG21 1 
ATOM   13985 H  HG22 . ILE   B  2  324 ? 18.825  -32.596 3.039    1.00 70.06  ? 328  ILE   B HG22 1 
ATOM   13986 H  HG23 . ILE   B  2  324 ? 18.574  -31.447 1.971    1.00 70.06  ? 328  ILE   B HG23 1 
ATOM   13987 H  HD11 . ILE   B  2  324 ? 18.595  -33.355 -1.752   1.00 66.24  ? 328  ILE   B HD11 1 
ATOM   13988 H  HD12 . ILE   B  2  324 ? 18.852  -34.446 -0.627   1.00 66.24  ? 328  ILE   B HD12 1 
ATOM   13989 H  HD13 . ILE   B  2  324 ? 17.775  -33.303 -0.392   1.00 66.24  ? 328  ILE   B HD13 1 
ATOM   13990 N  N    . PRO   B  2  325 ? 21.426  -31.510 4.163    1.00 62.49  ? 329  PRO   B N    1 
ATOM   13991 C  CA   . PRO   B  2  325 ? 21.711  -31.837 5.567    1.00 60.68  ? 329  PRO   B CA   1 
ATOM   13992 C  C    . PRO   B  2  325 ? 20.721  -32.858 6.111    1.00 57.62  ? 329  PRO   B C    1 
ATOM   13993 O  O    . PRO   B  2  325 ? 19.506  -32.710 5.965    1.00 59.69  ? 329  PRO   B O    1 
ATOM   13994 C  CB   . PRO   B  2  325 ? 21.583  -30.486 6.283    1.00 61.07  ? 329  PRO   B CB   1 
ATOM   13995 C  CG   . PRO   B  2  325 ? 21.731  -29.459 5.215    1.00 61.59  ? 329  PRO   B CG   1 
ATOM   13996 C  CD   . PRO   B  2  325 ? 21.150  -30.073 3.983    1.00 63.30  ? 329  PRO   B CD   1 
ATOM   13997 H  HA   . PRO   B  2  325 ? 22.616  -32.175 5.662    1.00 72.85  ? 329  PRO   B HA   1 
ATOM   13998 H  HB2  . PRO   B  2  325 ? 20.713  -30.420 6.708    1.00 73.32  ? 329  PRO   B HB2  1 
ATOM   13999 H  HB3  . PRO   B  2  325 ? 22.284  -30.398 6.947    1.00 73.32  ? 329  PRO   B HB3  1 
ATOM   14000 H  HG2  . PRO   B  2  325 ? 21.245  -28.656 5.461    1.00 73.94  ? 329  PRO   B HG2  1 
ATOM   14001 H  HG3  . PRO   B  2  325 ? 22.670  -29.252 5.086    1.00 73.94  ? 329  PRO   B HG3  1 
ATOM   14002 H  HD2  . PRO   B  2  325 ? 20.196  -29.908 3.931    1.00 75.99  ? 329  PRO   B HD2  1 
ATOM   14003 H  HD3  . PRO   B  2  325 ? 21.590  -29.734 3.187    1.00 75.99  ? 329  PRO   B HD3  1 
ATOM   14004 N  N    . GLY   B  2  326 ? 21.256  -33.904 6.739    1.00 54.94  ? 330  GLY   B N    1 
ATOM   14005 C  CA   . GLY   B  2  326 ? 20.444  -34.914 7.381    1.00 56.27  ? 330  GLY   B CA   1 
ATOM   14006 C  C    . GLY   B  2  326 ? 19.817  -35.933 6.456    1.00 56.53  ? 330  GLY   B C    1 
ATOM   14007 O  O    . GLY   B  2  326 ? 19.185  -36.879 6.944    1.00 60.14  ? 330  GLY   B O    1 
ATOM   14008 H  H    . GLY   B  2  326 ? 22.102  -34.046 6.805    1.00 65.97  ? 330  GLY   B H    1 
ATOM   14009 H  HA2  . GLY   B  2  326 ? 20.997  -35.396 8.015    1.00 67.56  ? 330  GLY   B HA2  1 
ATOM   14010 H  HA3  . GLY   B  2  326 ? 19.725  -34.473 7.860    1.00 67.56  ? 330  GLY   B HA3  1 
ATOM   14011 N  N    . ALA   B  2  327 ? 19.963  -35.779 5.143    1.00 51.97  ? 331  ALA   B N    1 
ATOM   14012 C  CA   . ALA   B  2  327 ? 19.379  -36.735 4.212    1.00 52.22  ? 331  ALA   B CA   1 
ATOM   14013 C  C    . ALA   B  2  327 ? 20.152  -38.048 4.232    1.00 54.17  ? 331  ALA   B C    1 
ATOM   14014 O  O    . ALA   B  2  327 ? 21.375  -38.068 4.398    1.00 59.09  ? 331  ALA   B O    1 
ATOM   14015 C  CB   . ALA   B  2  327 ? 19.366  -36.159 2.797    1.00 52.03  ? 331  ALA   B CB   1 
ATOM   14016 H  H    . ALA   B  2  327 ? 20.393  -35.135 4.769    1.00 62.40  ? 331  ALA   B H    1 
ATOM   14017 H  HA   . ALA   B  2  327 ? 18.463  -36.917 4.475    1.00 62.70  ? 331  ALA   B HA   1 
ATOM   14018 H  HB1  . ALA   B  2  327 ? 18.978  -36.812 2.194    1.00 62.47  ? 331  ALA   B HB1  1 
ATOM   14019 H  HB2  . ALA   B  2  327 ? 18.834  -35.347 2.791    1.00 62.47  ? 331  ALA   B HB2  1 
ATOM   14020 H  HB3  . ALA   B  2  327 ? 20.276  -35.960 2.528    1.00 62.47  ? 331  ALA   B HB3  1 
ATOM   14021 N  N    . THR   B  2  328 ? 19.425  -39.152 4.065    1.00 52.68  ? 332  THR   B N    1 
ATOM   14022 C  CA   . THR   B  2  328 ? 20.020  -40.478 3.979    1.00 54.44  ? 332  THR   B CA   1 
ATOM   14023 C  C    . THR   B  2  328 ? 19.329  -41.253 2.865    1.00 51.13  ? 332  THR   B C    1 
ATOM   14024 O  O    . THR   B  2  328 ? 18.342  -40.796 2.282    1.00 45.94  ? 332  THR   B O    1 
ATOM   14025 C  CB   . THR   B  2  328 ? 19.915  -41.233 5.309    1.00 60.01  ? 332  THR   B CB   1 
ATOM   14026 O  OG1  . THR   B  2  328 ? 18.537  -41.433 5.644    1.00 63.46  ? 332  THR   B OG1  1 
ATOM   14027 C  CG2  . THR   B  2  328 ? 20.597  -40.447 6.419    1.00 63.45  ? 332  THR   B CG2  1 
ATOM   14028 H  H    . THR   B  2  328 ? 18.568  -39.156 3.998    1.00 63.26  ? 332  THR   B H    1 
ATOM   14029 H  HA   . THR   B  2  328 ? 20.961  -40.394 3.756    1.00 65.36  ? 332  THR   B HA   1 
ATOM   14030 H  HB   . THR   B  2  328 ? 20.354  -42.094 5.229    1.00 72.05  ? 332  THR   B HB   1 
ATOM   14031 H  HG1  . THR   B  2  328 ? 18.475  -41.883 6.351    1.00 76.19  ? 332  THR   B HG1  1 
ATOM   14032 H  HG21 . THR   B  2  328 ? 20.547  -40.940 7.253    1.00 76.18  ? 332  THR   B HG21 1 
ATOM   14033 H  HG22 . THR   B  2  328 ? 21.529  -40.298 6.197    1.00 76.18  ? 332  THR   B HG22 1 
ATOM   14034 H  HG23 . THR   B  2  328 ? 20.160  -39.588 6.535    1.00 76.18  ? 332  THR   B HG23 1 
ATOM   14035 N  N    . VAL   B  2  329 ? 19.852  -42.442 2.574    1.00 51.23  ? 333  VAL   B N    1 
ATOM   14036 C  CA   . VAL   B  2  329 ? 19.372  -43.257 1.463    1.00 48.48  ? 333  VAL   B CA   1 
ATOM   14037 C  C    . VAL   B  2  329 ? 19.246  -44.705 1.914    1.00 51.86  ? 333  VAL   B C    1 
ATOM   14038 O  O    . VAL   B  2  329 ? 20.105  -45.222 2.635    1.00 54.73  ? 333  VAL   B O    1 
ATOM   14039 C  CB   . VAL   B  2  329 ? 20.309  -43.158 0.240    1.00 48.66  ? 333  VAL   B CB   1 
ATOM   14040 C  CG1  . VAL   B  2  329 ? 19.835  -44.086 -0.874   1.00 44.27  ? 333  VAL   B CG1  1 
ATOM   14041 C  CG2  . VAL   B  2  329 ? 20.388  -41.724 -0.254   1.00 50.10  ? 333  VAL   B CG2  1 
ATOM   14042 H  H    . VAL   B  2  329 ? 20.498  -42.804 3.013    1.00 61.51  ? 333  VAL   B H    1 
ATOM   14043 H  HA   . VAL   B  2  329 ? 18.490  -42.942 1.211    1.00 58.21  ? 333  VAL   B HA   1 
ATOM   14044 H  HB   . VAL   B  2  329 ? 21.200  -43.437 0.504    1.00 58.43  ? 333  VAL   B HB   1 
ATOM   14045 H  HG11 . VAL   B  2  329 ? 20.409  -43.970 -1.648   1.00 53.16  ? 333  VAL   B HG11 1 
ATOM   14046 H  HG12 . VAL   B  2  329 ? 19.881  -45.003 -0.562   1.00 53.16  ? 333  VAL   B HG12 1 
ATOM   14047 H  HG13 . VAL   B  2  329 ? 18.920  -43.861 -1.105   1.00 53.16  ? 333  VAL   B HG13 1 
ATOM   14048 H  HG21 . VAL   B  2  329 ? 20.965  -41.689 -1.033   1.00 60.16  ? 333  VAL   B HG21 1 
ATOM   14049 H  HG22 . VAL   B  2  329 ? 19.497  -41.421 -0.489   1.00 60.16  ? 333  VAL   B HG22 1 
ATOM   14050 H  HG23 . VAL   B  2  329 ? 20.752  -41.166 0.451    1.00 60.16  ? 333  VAL   B HG23 1 
ATOM   14051 N  N    . GLY   B  2  330 ? 18.178  -45.357 1.471    1.00 50.29  ? 334  GLY   B N    1 
ATOM   14052 C  CA   . GLY   B  2  330 ? 17.992  -46.773 1.716    1.00 49.90  ? 334  GLY   B CA   1 
ATOM   14053 C  C    . GLY   B  2  330 ? 17.616  -47.491 0.438    1.00 50.90  ? 334  GLY   B C    1 
ATOM   14054 O  O    . GLY   B  2  330 ? 16.914  -46.954 -0.420   1.00 49.61  ? 334  GLY   B O    1 
ATOM   14055 H  H    . GLY   B  2  330 ? 17.541  -44.994 1.022    1.00 60.38  ? 334  GLY   B H    1 
ATOM   14056 H  HA2  . GLY   B  2  330 ? 18.814  -47.157 2.060    1.00 59.92  ? 334  GLY   B HA2  1 
ATOM   14057 H  HA3  . GLY   B  2  330 ? 17.285  -46.903 2.368    1.00 59.92  ? 334  GLY   B HA3  1 
ATOM   14058 N  N    . LEU   B  2  331 ? 18.096  -48.728 0.322    1.00 49.77  ? 335  LEU   B N    1 
ATOM   14059 C  CA   . LEU   B  2  331 ? 17.934  -49.516 -0.894   1.00 51.66  ? 335  LEU   B CA   1 
ATOM   14060 C  C    . LEU   B  2  331 ? 16.586  -50.229 -0.860   1.00 55.24  ? 335  LEU   B C    1 
ATOM   14061 O  O    . LEU   B  2  331 ? 16.356  -51.101 -0.015   1.00 58.56  ? 335  LEU   B O    1 
ATOM   14062 C  CB   . LEU   B  2  331 ? 19.085  -50.511 -1.040   1.00 56.73  ? 335  LEU   B CB   1 
ATOM   14063 C  CG   . LEU   B  2  331 ? 18.986  -51.484 -2.216   1.00 62.13  ? 335  LEU   B CG   1 
ATOM   14064 C  CD1  . LEU   B  2  331 ? 18.673  -50.751 -3.504   1.00 65.52  ? 335  LEU   B CD1  1 
ATOM   14065 C  CD2  . LEU   B  2  331 ? 20.276  -52.268 -2.365   1.00 66.15  ? 335  LEU   B CD2  1 
ATOM   14066 H  H    . LEU   B  2  331 ? 18.525  -49.137 0.944    1.00 59.76  ? 335  LEU   B H    1 
ATOM   14067 H  HA   . LEU   B  2  331 ? 17.942  -48.931 -1.668   1.00 62.03  ? 335  LEU   B HA   1 
ATOM   14068 H  HB2  . LEU   B  2  331 ? 19.907  -50.009 -1.152   1.00 68.11  ? 335  LEU   B HB2  1 
ATOM   14069 H  HB3  . LEU   B  2  331 ? 19.129  -51.044 -0.231   1.00 68.11  ? 335  LEU   B HB3  1 
ATOM   14070 H  HG   . LEU   B  2  331 ? 18.263  -52.106 -2.041   1.00 74.59  ? 335  LEU   B HG   1 
ATOM   14071 H  HD11 . LEU   B  2  331 ? 18.667  -51.387 -4.236   1.00 78.66  ? 335  LEU   B HD11 1 
ATOM   14072 H  HD12 . LEU   B  2  331 ? 17.803  -50.330 -3.424   1.00 78.66  ? 335  LEU   B HD12 1 
ATOM   14073 H  HD13 . LEU   B  2  331 ? 19.354  -50.077 -3.657   1.00 78.66  ? 335  LEU   B HD13 1 
ATOM   14074 H  HD21 . LEU   B  2  331 ? 20.180  -52.898 -3.096   1.00 79.42  ? 335  LEU   B HD21 1 
ATOM   14075 H  HD22 . LEU   B  2  331 ? 21.000  -51.651 -2.553   1.00 79.42  ? 335  LEU   B HD22 1 
ATOM   14076 H  HD23 . LEU   B  2  331 ? 20.453  -52.745 -1.539   1.00 79.42  ? 335  LEU   B HD23 1 
ATOM   14077 N  N    . LEU   B  2  332 ? 15.705  -49.865 -1.788   1.00 56.49  ? 336  LEU   B N    1 
ATOM   14078 C  CA   . LEU   B  2  332 ? 14.327  -50.337 -1.811   1.00 56.27  ? 336  LEU   B CA   1 
ATOM   14079 C  C    . LEU   B  2  332 ? 14.173  -51.469 -2.818   1.00 59.10  ? 336  LEU   B C    1 
ATOM   14080 O  O    . LEU   B  2  332 ? 14.674  -51.377 -3.943   1.00 58.94  ? 336  LEU   B O    1 
ATOM   14081 C  CB   . LEU   B  2  332 ? 13.383  -49.187 -2.169   1.00 55.98  ? 336  LEU   B CB   1 
ATOM   14082 C  CG   . LEU   B  2  332 ? 11.882  -49.469 -2.189   1.00 61.86  ? 336  LEU   B CG   1 
ATOM   14083 C  CD1  . LEU   B  2  332 ? 11.345  -49.574 -0.774   1.00 66.54  ? 336  LEU   B CD1  1 
ATOM   14084 C  CD2  . LEU   B  2  332 ? 11.156  -48.384 -2.972   1.00 61.26  ? 336  LEU   B CD2  1 
ATOM   14085 H  H    . LEU   B  2  332 ? 15.890  -49.329 -2.435   1.00 67.83  ? 336  LEU   B H    1 
ATOM   14086 H  HA   . LEU   B  2  332 ? 14.090  -50.684 -0.936   1.00 67.56  ? 336  LEU   B HA   1 
ATOM   14087 H  HB2  . LEU   B  2  332 ? 13.525  -48.478 -1.522   1.00 67.21  ? 336  LEU   B HB2  1 
ATOM   14088 H  HB3  . LEU   B  2  332 ? 13.621  -48.877 -3.057   1.00 67.21  ? 336  LEU   B HB3  1 
ATOM   14089 H  HG   . LEU   B  2  332 ? 11.716  -50.316 -2.631   1.00 74.27  ? 336  LEU   B HG   1 
ATOM   14090 H  HD11 . LEU   B  2  332 ? 10.382  -49.684 -0.809   1.00 79.89  ? 336  LEU   B HD11 1 
ATOM   14091 H  HD12 . LEU   B  2  332 ? 11.750  -50.341 -0.338   1.00 79.89  ? 336  LEU   B HD12 1 
ATOM   14092 H  HD13 . LEU   B  2  332 ? 11.568  -48.763 -0.290   1.00 79.89  ? 336  LEU   B HD13 1 
ATOM   14093 H  HD21 . LEU   B  2  332 ? 10.203  -48.566 -2.954   1.00 73.55  ? 336  LEU   B HD21 1 
ATOM   14094 H  HD22 . LEU   B  2  332 ? 11.336  -47.524 -2.561   1.00 73.55  ? 336  LEU   B HD22 1 
ATOM   14095 H  HD23 . LEU   B  2  332 ? 11.476  -48.387 -3.887   1.00 73.55  ? 336  LEU   B HD23 1 
ATOM   14096 N  N    . GLN   B  2  333 ? 13.478  -52.528 -2.413   1.00 62.87  ? 337  GLN   B N    1 
ATOM   14097 C  CA   . GLN   B  2  333 ? 13.160  -53.603 -3.339   1.00 66.60  ? 337  GLN   B CA   1 
ATOM   14098 C  C    . GLN   B  2  333 ? 12.196  -53.104 -4.412   1.00 64.77  ? 337  GLN   B C    1 
ATOM   14099 O  O    . GLN   B  2  333 ? 11.513  -52.089 -4.252   1.00 59.95  ? 337  GLN   B O    1 
ATOM   14100 C  CB   . GLN   B  2  333 ? 12.555  -54.794 -2.596   1.00 69.36  ? 337  GLN   B CB   1 
ATOM   14101 C  CG   . GLN   B  2  333 ? 13.540  -55.503 -1.680   1.00 68.28  ? 337  GLN   B CG   1 
ATOM   14102 C  CD   . GLN   B  2  333 ? 12.927  -56.683 -0.952   1.00 68.15  ? 337  GLN   B CD   1 
ATOM   14103 O  OE1  . GLN   B  2  333 ? 11.841  -57.148 -1.298   1.00 68.89  ? 337  GLN   B OE1  1 
ATOM   14104 N  NE2  . GLN   B  2  333 ? 13.624  -57.175 0.067    1.00 68.48  ? 337  GLN   B NE2  1 
ATOM   14105 H  H    . GLN   B  2  333 ? 13.182  -52.646 -1.615   1.00 75.48  ? 337  GLN   B H    1 
ATOM   14106 H  HA   . GLN   B  2  333 ? 13.971  -53.910 -3.775   1.00 79.96  ? 337  GLN   B HA   1 
ATOM   14107 H  HB2  . GLN   B  2  333 ? 11.816  -54.480 -2.052   1.00 83.27  ? 337  GLN   B HB2  1 
ATOM   14108 H  HB3  . GLN   B  2  333 ? 12.237  -55.440 -3.247   1.00 83.27  ? 337  GLN   B HB3  1 
ATOM   14109 H  HG2  . GLN   B  2  333 ? 14.283  -55.832 -2.210   1.00 81.97  ? 337  GLN   B HG2  1 
ATOM   14110 H  HG3  . GLN   B  2  333 ? 13.859  -54.875 -1.014   1.00 81.97  ? 337  GLN   B HG3  1 
ATOM   14111 H  HE21 . GLN   B  2  333 ? 14.379  -56.823 0.281    1.00 82.21  ? 337  GLN   B HE21 1 
ATOM   14112 H  HE22 . GLN   B  2  333 ? 13.320  -57.844 0.513    1.00 82.21  ? 337  GLN   B HE22 1 
ATOM   14113 N  N    . LYS   B  2  334 ? 12.148  -53.839 -5.524   1.00 68.64  ? 338  LYS   B N    1 
ATOM   14114 C  CA   . LYS   B  2  334 ? 11.302  -53.433 -6.639   1.00 71.40  ? 338  LYS   B CA   1 
ATOM   14115 C  C    . LYS   B  2  334 ? 9.825   -53.421 -6.265   1.00 66.44  ? 338  LYS   B C    1 
ATOM   14116 O  O    . LYS   B  2  334 ? 9.030   -52.767 -6.949   1.00 62.16  ? 338  LYS   B O    1 
ATOM   14117 C  CB   . LYS   B  2  334 ? 11.537  -54.361 -7.834   1.00 82.06  ? 338  LYS   B CB   1 
ATOM   14118 C  CG   . LYS   B  2  334 ? 13.009  -54.535 -8.214   1.00 92.06  ? 338  LYS   B CG   1 
ATOM   14119 C  CD   . LYS   B  2  334 ? 13.663  -53.214 -8.606   1.00 100.87 ? 338  LYS   B CD   1 
ATOM   14120 C  CE   . LYS   B  2  334 ? 15.164  -53.368 -8.814   1.00 107.99 ? 338  LYS   B CE   1 
ATOM   14121 N  NZ   . LYS   B  2  334 ? 15.505  -54.412 -9.819   1.00 112.38 ? 338  LYS   B NZ   1 
ATOM   14122 H  H    . LYS   B  2  334 ? 12.589  -54.565 -5.654   1.00 82.40  ? 338  LYS   B H    1 
ATOM   14123 H  HA   . LYS   B  2  334 ? 11.545  -52.533 -6.908   1.00 85.72  ? 338  LYS   B HA   1 
ATOM   14124 H  HB2  . LYS   B  2  334 ? 11.183  -55.238 -7.620   1.00 98.51  ? 338  LYS   B HB2  1 
ATOM   14125 H  HB3  . LYS   B  2  334 ? 11.076  -53.996 -8.606   1.00 98.51  ? 338  LYS   B HB3  1 
ATOM   14126 H  HG2  . LYS   B  2  334 ? 13.493  -54.898 -7.456   1.00 110.50 ? 338  LYS   B HG2  1 
ATOM   14127 H  HG3  . LYS   B  2  334 ? 13.074  -55.140 -8.969   1.00 110.50 ? 338  LYS   B HG3  1 
ATOM   14128 H  HD2  . LYS   B  2  334 ? 13.272  -52.897 -9.436   1.00 121.09 ? 338  LYS   B HD2  1 
ATOM   14129 H  HD3  . LYS   B  2  334 ? 13.518  -52.563 -7.902   1.00 121.09 ? 338  LYS   B HD3  1 
ATOM   14130 H  HE2  . LYS   B  2  334 ? 15.528  -52.524 -9.124   1.00 129.63 ? 338  LYS   B HE2  1 
ATOM   14131 H  HE3  . LYS   B  2  334 ? 15.576  -53.617 -7.971   1.00 129.63 ? 338  LYS   B HE3  1 
ATOM   14132 H  HZ1  . LYS   B  2  334 ? 16.368  -54.362 -10.029  1.00 134.90 ? 338  LYS   B HZ1  1 
ATOM   14133 H  HZ2  . LYS   B  2  334 ? 15.335  -55.221 -9.487   1.00 134.90 ? 338  LYS   B HZ2  1 
ATOM   14134 H  HZ3  . LYS   B  2  334 ? 15.021  -54.295 -10.556  1.00 134.90 ? 338  LYS   B HZ3  1 
ATOM   14135 N  N    . ASP   B  2  335 ? 9.441   -54.117 -5.191   1.00 68.68  ? 339  ASP   B N    1 
ATOM   14136 C  CA   . ASP   B  2  335 ? 8.051   -54.182 -4.753   1.00 64.05  ? 339  ASP   B CA   1 
ATOM   14137 C  C    . ASP   B  2  335 ? 7.847   -53.554 -3.377   1.00 62.49  ? 339  ASP   B C    1 
ATOM   14138 O  O    . ASP   B  2  335 ? 6.814   -53.787 -2.742   1.00 64.11  ? 339  ASP   B O    1 
ATOM   14139 C  CB   . ASP   B  2  335 ? 7.565   -55.634 -4.747   1.00 63.95  ? 339  ASP   B CB   1 
ATOM   14140 C  CG   . ASP   B  2  335 ? 8.370   -56.517 -3.813   1.00 65.15  ? 339  ASP   B CG   1 
ATOM   14141 O  OD1  . ASP   B  2  335 ? 9.262   -55.995 -3.110   1.00 62.44  ? 339  ASP   B OD1  1 
ATOM   14142 O  OD2  . ASP   B  2  335 ? 8.109   -57.738 -3.783   1.00 68.35  ? 339  ASP   B OD2  1 
ATOM   14143 H  H    . ASP   B  2  335 ? 9.980   -54.567 -4.694   1.00 82.45  ? 339  ASP   B H    1 
ATOM   14144 H  HA   . ASP   B  2  335 ? 7.509   -53.681 -5.383   1.00 76.90  ? 339  ASP   B HA   1 
ATOM   14145 H  HB2  . ASP   B  2  335 ? 6.640   -55.656 -4.458   1.00 76.78  ? 339  ASP   B HB2  1 
ATOM   14146 H  HB3  . ASP   B  2  335 ? 7.642   -55.997 -5.643   1.00 76.78  ? 339  ASP   B HB3  1 
ATOM   14147 N  N    . SER   B  2  336 ? 8.807   -52.759 -2.903   1.00 58.71  ? 340  SER   B N    1 
ATOM   14148 C  CA   . SER   B  2  336 ? 8.754   -52.129 -1.585   1.00 53.60  ? 340  SER   B CA   1 
ATOM   14149 C  C    . SER   B  2  336 ? 8.665   -53.149 -0.453   1.00 54.33  ? 340  SER   B C    1 
ATOM   14150 O  O    . SER   B  2  336 ? 8.307   -52.798 0.675    1.00 51.30  ? 340  SER   B O    1 
ATOM   14151 C  CB   . SER   B  2  336 ? 7.580   -51.146 -1.483   1.00 50.61  ? 340  SER   B CB   1 
ATOM   14152 O  OG   . SER   B  2  336 ? 7.832   -49.963 -2.220   1.00 47.85  ? 340  SER   B OG   1 
ATOM   14153 H  H    . SER   B  2  336 ? 9.521   -52.565 -3.342   1.00 70.49  ? 340  SER   B H    1 
ATOM   14154 H  HA   . SER   B  2  336 ? 9.578   -51.632 -1.465   1.00 64.36  ? 340  SER   B HA   1 
ATOM   14155 H  HB2  . SER   B  2  336 ? 6.783   -51.572 -1.837   1.00 60.76  ? 340  SER   B HB2  1 
ATOM   14156 H  HB3  . SER   B  2  336 ? 7.446   -50.913 -0.551   1.00 60.76  ? 340  SER   B HB3  1 
ATOM   14157 H  HG   . SER   B  2  336 ? 7.843   -50.133 -3.042   1.00 57.45  ? 340  SER   B HG   1 
ATOM   14158 N  N    . GLY   B  2  337 ? 9.000   -54.411 -0.726   1.00 58.34  ? 341  GLY   B N    1 
ATOM   14159 C  CA   . GLY   B  2  337 ? 8.843   -55.455 0.273    1.00 50.60  ? 341  GLY   B CA   1 
ATOM   14160 C  C    . GLY   B  2  337 ? 9.614   -55.217 1.555    1.00 66.61  ? 341  GLY   B C    1 
ATOM   14161 O  O    . GLY   B  2  337 ? 9.283   -55.816 2.584    1.00 70.32  ? 341  GLY   B O    1 
ATOM   14162 H  H    . GLY   B  2  337 ? 9.318   -54.683 -1.477   1.00 70.04  ? 341  GLY   B H    1 
ATOM   14163 H  HA2  . GLY   B  2  337 ? 7.904   -55.530 0.500    1.00 60.53  ? 341  GLY   B HA2  1 
ATOM   14164 H  HA3  . GLY   B  2  337 ? 9.146   -56.296 -0.104   1.00 60.53  ? 341  GLY   B HA3  1 
ATOM   14165 N  N    . ASN   B  2  338 ? 10.632  -54.353 1.523    1.00 61.49  ? 342  ASN   B N    1 
ATOM   14166 C  CA   . ASN   B  2  338 ? 11.503  -54.125 2.671    1.00 59.44  ? 342  ASN   B CA   1 
ATOM   14167 C  C    . ASN   B  2  338 ? 11.439  -52.687 3.173    1.00 59.14  ? 342  ASN   B C    1 
ATOM   14168 O  O    . ASN   B  2  338 ? 12.369  -52.229 3.845    1.00 56.85  ? 342  ASN   B O    1 
ATOM   14169 C  CB   . ASN   B  2  338 ? 12.948  -54.476 2.315    1.00 58.58  ? 342  ASN   B CB   1 
ATOM   14170 C  CG   . ASN   B  2  338 ? 13.521  -53.548 1.263    1.00 59.41  ? 342  ASN   B CG   1 
ATOM   14171 O  OD1  . ASN   B  2  338 ? 12.816  -53.119 0.350    1.00 58.69  ? 342  ASN   B OD1  1 
ATOM   14172 N  ND2  . ASN   B  2  338 ? 14.802  -53.225 1.390    1.00 65.42  ? 342  ASN   B ND2  1 
ATOM   14173 H  H    . ASN   B  2  338 ? 10.839  -53.881 0.835    1.00 73.83  ? 342  ASN   B H    1 
ATOM   14174 H  HA   . ASN   B  2  338 ? 11.207  -54.703 3.392    1.00 71.37  ? 342  ASN   B HA   1 
ATOM   14175 H  HB2  . ASN   B  2  338 ? 13.497  -54.407 3.111    1.00 70.33  ? 342  ASN   B HB2  1 
ATOM   14176 H  HB3  . ASN   B  2  338 ? 12.979  -55.381 1.968    1.00 70.33  ? 342  ASN   B HB3  1 
ATOM   14177 H  HD21 . ASN   B  2  338 ? 15.173  -52.701 0.818    1.00 78.54  ? 342  ASN   B HD21 1 
ATOM   14178 H  HD22 . ASN   B  2  338 ? 15.262  -53.540 2.045    1.00 78.54  ? 342  ASN   B HD22 1 
ATOM   14179 N  N    . ILE   B  2  339 ? 10.363  -51.961 2.864    1.00 56.89  ? 343  ILE   B N    1 
ATOM   14180 C  CA   . ILE   B  2  339 ? 10.316  -50.550 3.235    1.00 51.54  ? 343  ILE   B CA   1 
ATOM   14181 C  C    . ILE   B  2  339 ? 10.271  -50.388 4.749    1.00 54.41  ? 343  ILE   B C    1 
ATOM   14182 O  O    . ILE   B  2  339 ? 10.830  -49.427 5.292    1.00 52.37  ? 343  ILE   B O    1 
ATOM   14183 C  CB   . ILE   B  2  339 ? 9.121   -49.854 2.555    1.00 47.37  ? 343  ILE   B CB   1 
ATOM   14184 C  CG1  . ILE   B  2  339 ? 9.086   -48.365 2.919    1.00 45.58  ? 343  ILE   B CG1  1 
ATOM   14185 C  CG2  . ILE   B  2  339 ? 7.808   -50.526 2.945    1.00 47.74  ? 343  ILE   B CG2  1 
ATOM   14186 C  CD1  . ILE   B  2  339 ? 10.332  -47.591 2.513    1.00 42.28  ? 343  ILE   B CD1  1 
ATOM   14187 H  H    . ILE   B  2  339 ? 9.668   -52.253 2.451    1.00 68.31  ? 343  ILE   B H    1 
ATOM   14188 H  HA   . ILE   B  2  339 ? 11.128  -50.126 2.916    1.00 61.89  ? 343  ILE   B HA   1 
ATOM   14189 H  HB   . ILE   B  2  339 ? 9.236   -49.936 1.595    1.00 56.88  ? 343  ILE   B HB   1 
ATOM   14190 H  HG12 . ILE   B  2  339 ? 8.327   -47.956 2.475    1.00 54.73  ? 343  ILE   B HG12 1 
ATOM   14191 H  HG13 . ILE   B  2  339 ? 8.990   -48.284 3.881    1.00 54.73  ? 343  ILE   B HG13 1 
ATOM   14192 H  HG21 . ILE   B  2  339 ? 7.077   -50.077 2.492    1.00 57.32  ? 343  ILE   B HG21 1 
ATOM   14193 H  HG22 . ILE   B  2  339 ? 7.839   -51.458 2.680    1.00 57.32  ? 343  ILE   B HG22 1 
ATOM   14194 H  HG23 . ILE   B  2  339 ? 7.693   -50.459 3.906    1.00 57.32  ? 343  ILE   B HG23 1 
ATOM   14195 H  HD11 . ILE   B  2  339 ? 10.220  -46.660 2.762    1.00 50.77  ? 343  ILE   B HD11 1 
ATOM   14196 H  HD12 . ILE   B  2  339 ? 11.100  -47.966 2.970    1.00 50.77  ? 343  ILE   B HD12 1 
ATOM   14197 H  HD13 . ILE   B  2  339 ? 10.450  -47.664 1.553    1.00 50.77  ? 343  ILE   B HD13 1 
ATOM   14198 N  N    . LEU   B  2  340 ? 9.616   -51.312 5.456    1.00 58.89  ? 344  LEU   B N    1 
ATOM   14199 C  CA   . LEU   B  2  340 ? 9.554   -51.219 6.912    1.00 61.55  ? 344  LEU   B CA   1 
ATOM   14200 C  C    . LEU   B  2  340 ? 10.950  -51.270 7.519    1.00 64.56  ? 344  LEU   B C    1 
ATOM   14201 O  O    . LEU   B  2  340 ? 11.297  -50.459 8.385    1.00 61.63  ? 344  LEU   B O    1 
ATOM   14202 C  CB   . LEU   B  2  340 ? 8.684   -52.345 7.470    1.00 62.94  ? 344  LEU   B CB   1 
ATOM   14203 C  CG   . LEU   B  2  340 ? 8.595   -52.447 8.994    1.00 65.97  ? 344  LEU   B CG   1 
ATOM   14204 C  CD1  . LEU   B  2  340 ? 8.042   -51.167 9.587    1.00 70.59  ? 344  LEU   B CD1  1 
ATOM   14205 C  CD2  . LEU   B  2  340 ? 7.738   -53.633 9.397    1.00 66.23  ? 344  LEU   B CD2  1 
ATOM   14206 H  H    . LEU   B  2  340 ? 9.207   -51.990 5.122    1.00 70.71  ? 344  LEU   B H    1 
ATOM   14207 H  HA   . LEU   B  2  340 ? 9.147   -50.374 7.157    1.00 73.90  ? 344  LEU   B HA   1 
ATOM   14208 H  HB2  . LEU   B  2  340 ? 7.781   -52.219 7.139    1.00 75.57  ? 344  LEU   B HB2  1 
ATOM   14209 H  HB3  . LEU   B  2  340 ? 9.040   -53.188 7.148    1.00 75.57  ? 344  LEU   B HB3  1 
ATOM   14210 H  HG   . LEU   B  2  340 ? 9.487   -52.582 9.352    1.00 79.20  ? 344  LEU   B HG   1 
ATOM   14211 H  HD11 . LEU   B  2  340 ? 7.984   -51.264 10.551   1.00 84.74  ? 344  LEU   B HD11 1 
ATOM   14212 H  HD12 . LEU   B  2  340 ? 8.636   -50.433 9.364    1.00 84.74  ? 344  LEU   B HD12 1 
ATOM   14213 H  HD13 . LEU   B  2  340 ? 7.160   -51.003 9.218    1.00 84.74  ? 344  LEU   B HD13 1 
ATOM   14214 H  HD21 . LEU   B  2  340 ? 7.690   -53.674 10.365   1.00 79.51  ? 344  LEU   B HD21 1 
ATOM   14215 H  HD22 . LEU   B  2  340 ? 6.848   -53.520 9.027    1.00 79.51  ? 344  LEU   B HD22 1 
ATOM   14216 H  HD23 . LEU   B  2  340 ? 8.139   -54.446 9.051    1.00 79.51  ? 344  LEU   B HD23 1 
ATOM   14217 N  N    . GLN   B  2  341 ? 11.769  -52.225 7.071    1.00 68.67  ? 345  GLN   B N    1 
ATOM   14218 C  CA   . GLN   B  2  341 ? 13.121  -52.348 7.602    1.00 73.57  ? 345  GLN   B CA   1 
ATOM   14219 C  C    . GLN   B  2  341 ? 13.944  -51.099 7.308    1.00 67.75  ? 345  GLN   B C    1 
ATOM   14220 O  O    . GLN   B  2  341 ? 14.699  -50.628 8.167    1.00 67.51  ? 345  GLN   B O    1 
ATOM   14221 C  CB   . GLN   B  2  341 ? 13.799  -53.590 7.023    1.00 85.03  ? 345  GLN   B CB   1 
ATOM   14222 C  CG   . GLN   B  2  341 ? 13.073  -54.904 7.313    1.00 98.91  ? 345  GLN   B CG   1 
ATOM   14223 C  CD   . GLN   B  2  341 ? 12.057  -55.275 6.247    1.00 112.33 ? 345  GLN   B CD   1 
ATOM   14224 O  OE1  . GLN   B  2  341 ? 11.078  -54.562 6.030    1.00 114.94 ? 345  GLN   B OE1  1 
ATOM   14225 N  NE2  . GLN   B  2  341 ? 12.288  -56.401 5.576    1.00 120.53 ? 345  GLN   B NE2  1 
ATOM   14226 H  H    . GLN   B  2  341 ? 11.566  -52.805 6.469    1.00 82.44  ? 345  GLN   B H    1 
ATOM   14227 H  HA   . GLN   B  2  341 ? 13.072  -52.454 8.565    1.00 88.32  ? 345  GLN   B HA   1 
ATOM   14228 H  HB2  . GLN   B  2  341 ? 13.852  -53.491 6.059    1.00 102.07 ? 345  GLN   B HB2  1 
ATOM   14229 H  HB3  . GLN   B  2  341 ? 14.691  -53.658 7.399    1.00 102.07 ? 345  GLN   B HB3  1 
ATOM   14230 H  HG2  . GLN   B  2  341 ? 13.727  -55.619 7.364    1.00 118.73 ? 345  GLN   B HG2  1 
ATOM   14231 H  HG3  . GLN   B  2  341 ? 12.603  -54.823 8.158    1.00 118.73 ? 345  GLN   B HG3  1 
ATOM   14232 H  HE21 . GLN   B  2  341 ? 12.983  -56.874 5.757    1.00 144.68 ? 345  GLN   B HE21 1 
ATOM   14233 H  HE22 . GLN   B  2  341 ? 11.742  -56.655 4.962    1.00 144.68 ? 345  GLN   B HE22 1 
ATOM   14234 N  N    . LEU   B  2  342 ? 13.813  -50.547 6.098    1.00 62.62  ? 346  LEU   B N    1 
ATOM   14235 C  CA   . LEU   B  2  342 ? 14.525  -49.317 5.767    1.00 57.66  ? 346  LEU   B CA   1 
ATOM   14236 C  C    . LEU   B  2  342 ? 14.199  -48.216 6.765    1.00 55.81  ? 346  LEU   B C    1 
ATOM   14237 O  O    . LEU   B  2  342 ? 15.097  -47.567 7.313    1.00 56.43  ? 346  LEU   B O    1 
ATOM   14238 C  CB   . LEU   B  2  342 ? 14.167  -48.864 4.351    1.00 57.36  ? 346  LEU   B CB   1 
ATOM   14239 C  CG   . LEU   B  2  342 ? 14.625  -49.750 3.194    1.00 63.29  ? 346  LEU   B CG   1 
ATOM   14240 C  CD1  . LEU   B  2  342 ? 14.070  -49.222 1.881    1.00 63.16  ? 346  LEU   B CD1  1 
ATOM   14241 C  CD2  . LEU   B  2  342 ? 16.142  -49.826 3.142    1.00 64.61  ? 346  LEU   B CD2  1 
ATOM   14242 H  H    . LEU   B  2  342 ? 13.326  -50.862 5.464    1.00 75.18  ? 346  LEU   B H    1 
ATOM   14243 H  HA   . LEU   B  2  342 ? 15.478  -49.493 5.798    1.00 69.22  ? 346  LEU   B HA   1 
ATOM   14244 H  HB2  . LEU   B  2  342 ? 13.201  -48.803 4.293    1.00 68.87  ? 346  LEU   B HB2  1 
ATOM   14245 H  HB3  . LEU   B  2  342 ? 14.564  -47.990 4.209    1.00 68.87  ? 346  LEU   B HB3  1 
ATOM   14246 H  HG   . LEU   B  2  342 ? 14.289  -50.650 3.330    1.00 75.98  ? 346  LEU   B HG   1 
ATOM   14247 H  HD11 . LEU   B  2  342 ? 14.331  -49.822 1.164    1.00 75.83  ? 346  LEU   B HD11 1 
ATOM   14248 H  HD12 . LEU   B  2  342 ? 13.103  -49.180 1.941    1.00 75.83  ? 346  LEU   B HD12 1 
ATOM   14249 H  HD13 . LEU   B  2  342 ? 14.430  -48.337 1.719    1.00 75.83  ? 346  LEU   B HD13 1 
ATOM   14250 H  HD21 . LEU   B  2  342 ? 16.405  -50.383 2.392    1.00 77.57  ? 346  LEU   B HD21 1 
ATOM   14251 H  HD22 . LEU   B  2  342 ? 16.499  -48.931 3.030    1.00 77.57  ? 346  LEU   B HD22 1 
ATOM   14252 H  HD23 . LEU   B  2  342 ? 16.468  -50.211 3.970    1.00 77.57  ? 346  LEU   B HD23 1 
ATOM   14253 N  N    . ILE   B  2  343 ? 12.908  -47.992 7.013    1.00 55.88  ? 347  ILE   B N    1 
ATOM   14254 C  CA   . ILE   B  2  343 ? 12.493  -46.906 7.894    1.00 54.73  ? 347  ILE   B CA   1 
ATOM   14255 C  C    . ILE   B  2  343 ? 13.081  -47.097 9.287    1.00 55.13  ? 347  ILE   B C    1 
ATOM   14256 O  O    . ILE   B  2  343 ? 13.686  -46.180 9.854    1.00 53.61  ? 347  ILE   B O    1 
ATOM   14257 C  CB   . ILE   B  2  343 ? 10.956  -46.809 7.925    1.00 56.42  ? 347  ILE   B CB   1 
ATOM   14258 C  CG1  . ILE   B  2  343 ? 10.453  -46.418 6.530    1.00 54.25  ? 347  ILE   B CG1  1 
ATOM   14259 C  CG2  . ILE   B  2  343 ? 10.498  -45.812 8.986    1.00 55.75  ? 347  ILE   B CG2  1 
ATOM   14260 C  CD1  . ILE   B  2  343 ? 8.950   -46.330 6.394    1.00 53.85  ? 347  ILE   B CD1  1 
ATOM   14261 H  H    . ILE   B  2  343 ? 12.259  -48.452 6.685    1.00 67.09  ? 347  ILE   B H    1 
ATOM   14262 H  HA   . ILE   B  2  343 ? 12.839  -46.070 7.545    1.00 65.71  ? 347  ILE   B HA   1 
ATOM   14263 H  HB   . ILE   B  2  343 ? 10.582  -47.672 8.163    1.00 67.74  ? 347  ILE   B HB   1 
ATOM   14264 H  HG12 . ILE   B  2  343 ? 10.816  -45.547 6.306    1.00 65.13  ? 347  ILE   B HG12 1 
ATOM   14265 H  HG13 . ILE   B  2  343 ? 10.764  -47.081 5.895    1.00 65.13  ? 347  ILE   B HG13 1 
ATOM   14266 H  HG21 . ILE   B  2  343 ? 9.531   -45.740 8.955    1.00 66.94  ? 347  ILE   B HG21 1 
ATOM   14267 H  HG22 . ILE   B  2  343 ? 10.778  -46.130 9.859    1.00 66.94  ? 347  ILE   B HG22 1 
ATOM   14268 H  HG23 . ILE   B  2  343 ? 10.900  -44.949 8.803    1.00 66.94  ? 347  ILE   B HG23 1 
ATOM   14269 H  HD11 . ILE   B  2  343 ? 8.728   -46.127 5.471    1.00 64.66  ? 347  ILE   B HD11 1 
ATOM   14270 H  HD12 . ILE   B  2  343 ? 8.559   -47.180 6.649    1.00 64.66  ? 347  ILE   B HD12 1 
ATOM   14271 H  HD13 . ILE   B  2  343 ? 8.620   -45.627 6.975    1.00 64.66  ? 347  ILE   B HD13 1 
ATOM   14272 N  N    . ILE   B  2  344 ? 12.918  -48.292 9.858    1.00 57.51  ? 348  ILE   B N    1 
ATOM   14273 C  CA   . ILE   B  2  344 ? 13.431  -48.539 11.204   1.00 60.16  ? 348  ILE   B CA   1 
ATOM   14274 C  C    . ILE   B  2  344 ? 14.940  -48.319 11.242   1.00 59.60  ? 348  ILE   B C    1 
ATOM   14275 O  O    . ILE   B  2  344 ? 15.464  -47.657 12.144   1.00 61.17  ? 348  ILE   B O    1 
ATOM   14276 C  CB   . ILE   B  2  344 ? 13.049  -49.952 11.679   1.00 61.38  ? 348  ILE   B CB   1 
ATOM   14277 C  CG1  . ILE   B  2  344 ? 11.524  -50.099 11.754   1.00 61.61  ? 348  ILE   B CG1  1 
ATOM   14278 C  CG2  . ILE   B  2  344 ? 13.678  -50.251 13.039   1.00 62.23  ? 348  ILE   B CG2  1 
ATOM   14279 C  CD1  . ILE   B  2  344 ? 10.843  -49.147 12.733   1.00 65.00  ? 348  ILE   B CD1  1 
ATOM   14280 H  H    . ILE   B  2  344 ? 12.523  -48.964 9.494    1.00 69.05  ? 348  ILE   B H    1 
ATOM   14281 H  HA   . ILE   B  2  344 ? 13.021  -47.903 11.811   1.00 72.23  ? 348  ILE   B HA   1 
ATOM   14282 H  HB   . ILE   B  2  344 ? 13.391  -50.590 11.033   1.00 73.69  ? 348  ILE   B HB   1 
ATOM   14283 H  HG12 . ILE   B  2  344 ? 11.153  -49.928 10.874   1.00 73.97  ? 348  ILE   B HG12 1 
ATOM   14284 H  HG13 . ILE   B  2  344 ? 11.314  -51.005 12.032   1.00 73.97  ? 348  ILE   B HG13 1 
ATOM   14285 H  HG21 . ILE   B  2  344 ? 13.373  -51.120 13.344   1.00 74.71  ? 348  ILE   B HG21 1 
ATOM   14286 H  HG22 . ILE   B  2  344 ? 14.643  -50.252 12.948   1.00 74.71  ? 348  ILE   B HG22 1 
ATOM   14287 H  HG23 . ILE   B  2  344 ? 13.406  -49.566 13.670   1.00 74.71  ? 348  ILE   B HG23 1 
ATOM   14288 H  HD11 . ILE   B  2  344 ? 9.889   -49.320 12.730   1.00 78.03  ? 348  ILE   B HD11 1 
ATOM   14289 H  HD12 . ILE   B  2  344 ? 11.204  -49.297 13.621   1.00 78.03  ? 348  ILE   B HD12 1 
ATOM   14290 H  HD13 . ILE   B  2  344 ? 11.015  -48.234 12.456   1.00 78.03  ? 348  ILE   B HD13 1 
ATOM   14291 N  N    . SER   B  2  345 ? 15.661  -48.867 10.260   1.00 57.55  ? 349  SER   B N    1 
ATOM   14292 C  CA   . SER   B  2  345 ? 17.106  -48.662 10.216   1.00 57.91  ? 349  SER   B CA   1 
ATOM   14293 C  C    . SER   B  2  345 ? 17.447  -47.178 10.186   1.00 53.61  ? 349  SER   B C    1 
ATOM   14294 O  O    . SER   B  2  345 ? 18.343  -46.722 10.906   1.00 51.30  ? 349  SER   B O    1 
ATOM   14295 C  CB   . SER   B  2  345 ? 17.708  -49.366 9.001    1.00 62.02  ? 349  SER   B CB   1 
ATOM   14296 O  OG   . SER   B  2  345 ? 17.675  -50.774 9.151    1.00 69.20  ? 349  SER   B OG   1 
ATOM   14297 H  H    . SER   B  2  345 ? 15.344  -49.350 9.623    1.00 69.09  ? 349  SER   B H    1 
ATOM   14298 H  HA   . SER   B  2  345 ? 17.498  -49.052 11.013   1.00 69.53  ? 349  SER   B HA   1 
ATOM   14299 H  HB2  . SER   B  2  345 ? 17.198  -49.123 8.212    1.00 74.46  ? 349  SER   B HB2  1 
ATOM   14300 H  HB3  . SER   B  2  345 ? 18.631  -49.084 8.899    1.00 74.46  ? 349  SER   B HB3  1 
ATOM   14301 H  HG   . SER   B  2  345 ? 16.884  -51.051 9.090    1.00 83.08  ? 349  SER   B HG   1 
ATOM   14302 N  N    . ALA   B  2  346 ? 16.740  -46.407 9.357    1.00 50.95  ? 350  ALA   B N    1 
ATOM   14303 C  CA   . ALA   B  2  346 ? 16.996  -44.973 9.278    1.00 47.17  ? 350  ALA   B CA   1 
ATOM   14304 C  C    . ALA   B  2  346 ? 16.731  -44.300 10.618   1.00 50.82  ? 350  ALA   B C    1 
ATOM   14305 O  O    . ALA   B  2  346 ? 17.546  -43.505 11.100   1.00 50.23  ? 350  ALA   B O    1 
ATOM   14306 C  CB   . ALA   B  2  346 ? 16.133  -44.350 8.182    1.00 40.66  ? 350  ALA   B CB   1 
ATOM   14307 H  H    . ALA   B  2  346 ? 16.116  -46.688 8.836    1.00 61.17  ? 350  ALA   B H    1 
ATOM   14308 H  HA   . ALA   B  2  346 ? 17.927  -44.831 9.047    1.00 56.64  ? 350  ALA   B HA   1 
ATOM   14309 H  HB1  . ALA   B  2  346 ? 16.309  -43.397 8.144    1.00 48.83  ? 350  ALA   B HB1  1 
ATOM   14310 H  HB2  . ALA   B  2  346 ? 16.356  -44.761 7.332    1.00 48.83  ? 350  ALA   B HB2  1 
ATOM   14311 H  HB3  . ALA   B  2  346 ? 15.198  -44.505 8.389    1.00 48.83  ? 350  ALA   B HB3  1 
ATOM   14312 N  N    . TYR   B  2  347 ? 15.589  -44.608 11.235   1.00 55.43  ? 351  TYR   B N    1 
ATOM   14313 C  CA   . TYR   B  2  347 ? 15.278  -44.031 12.538   1.00 57.42  ? 351  TYR   B CA   1 
ATOM   14314 C  C    . TYR   B  2  347 ? 16.343  -44.394 13.563   1.00 61.68  ? 351  TYR   B C    1 
ATOM   14315 O  O    . TYR   B  2  347 ? 16.771  -43.545 14.354   1.00 61.19  ? 351  TYR   B O    1 
ATOM   14316 C  CB   . TYR   B  2  347 ? 13.901  -44.504 13.003   1.00 56.04  ? 351  TYR   B CB   1 
ATOM   14317 C  CG   . TYR   B  2  347 ? 13.500  -43.992 14.368   1.00 53.14  ? 351  TYR   B CG   1 
ATOM   14318 C  CD1  . TYR   B  2  347 ? 13.232  -42.646 14.574   1.00 52.44  ? 351  TYR   B CD1  1 
ATOM   14319 C  CD2  . TYR   B  2  347 ? 13.378  -44.856 15.448   1.00 53.60  ? 351  TYR   B CD2  1 
ATOM   14320 C  CE1  . TYR   B  2  347 ? 12.861  -42.172 15.818   1.00 53.08  ? 351  TYR   B CE1  1 
ATOM   14321 C  CE2  . TYR   B  2  347 ? 13.005  -44.392 16.697   1.00 56.38  ? 351  TYR   B CE2  1 
ATOM   14322 C  CZ   . TYR   B  2  347 ? 12.747  -43.050 16.876   1.00 55.35  ? 351  TYR   B CZ   1 
ATOM   14323 O  OH   . TYR   B  2  347 ? 12.376  -42.582 18.115   1.00 54.52  ? 351  TYR   B OH   1 
ATOM   14324 H  H    . TYR   B  2  347 ? 14.988  -45.139 10.925   1.00 66.55  ? 351  TYR   B H    1 
ATOM   14325 H  HA   . TYR   B  2  347 ? 15.253  -43.065 12.458   1.00 68.94  ? 351  TYR   B HA   1 
ATOM   14326 H  HB2  . TYR   B  2  347 ? 13.237  -44.198 12.367   1.00 67.28  ? 351  TYR   B HB2  1 
ATOM   14327 H  HB3  . TYR   B  2  347 ? 13.903  -45.473 13.041   1.00 67.28  ? 351  TYR   B HB3  1 
ATOM   14328 H  HD1  . TYR   B  2  347 ? 13.303  -42.052 13.862   1.00 62.96  ? 351  TYR   B HD1  1 
ATOM   14329 H  HD2  . TYR   B  2  347 ? 13.549  -45.762 15.330   1.00 64.36  ? 351  TYR   B HD2  1 
ATOM   14330 H  HE1  . TYR   B  2  347 ? 12.689  -41.267 15.942   1.00 63.74  ? 351  TYR   B HE1  1 
ATOM   14331 H  HE2  . TYR   B  2  347 ? 12.930  -44.982 17.412   1.00 67.70  ? 351  TYR   B HE2  1 
ATOM   14332 H  HH   . TYR   B  2  347 ? 12.182  -43.225 18.619   1.00 65.46  ? 351  TYR   B HH   1 
ATOM   14333 N  N    . GLU   B  2  348 ? 16.790  -45.651 13.561   1.00 67.55  ? 352  GLU   B N    1 
ATOM   14334 C  CA   . GLU   B  2  348 ? 17.796  -46.073 14.528   1.00 72.79  ? 352  GLU   B CA   1 
ATOM   14335 C  C    . GLU   B  2  348 ? 19.131  -45.384 14.272   1.00 75.24  ? 352  GLU   B C    1 
ATOM   14336 O  O    . GLU   B  2  348 ? 19.793  -44.940 15.217   1.00 72.94  ? 352  GLU   B O    1 
ATOM   14337 C  CB   . GLU   B  2  348 ? 17.945  -47.593 14.496   1.00 72.46  ? 352  GLU   B CB   1 
ATOM   14338 C  CG   . GLU   B  2  348 ? 16.710  -48.316 15.013   1.00 74.31  ? 352  GLU   B CG   1 
ATOM   14339 C  CD   . GLU   B  2  348 ? 16.923  -49.805 15.190   1.00 78.52  ? 352  GLU   B CD   1 
ATOM   14340 O  OE1  . GLU   B  2  348 ? 17.764  -50.379 14.467   1.00 82.55  ? 352  GLU   B OE1  1 
ATOM   14341 O  OE2  . GLU   B  2  348 ? 16.251  -50.400 16.059   1.00 84.51  ? 352  GLU   B OE2  1 
ATOM   14342 H  H    . GLU   B  2  348 ? 16.530  -46.266 13.019   1.00 81.10  ? 352  GLU   B H    1 
ATOM   14343 H  HA   . GLU   B  2  348 ? 17.504  -45.823 15.419   1.00 87.38  ? 352  GLU   B HA   1 
ATOM   14344 H  HB2  . GLU   B  2  348 ? 18.097  -47.875 13.581   1.00 86.98  ? 352  GLU   B HB2  1 
ATOM   14345 H  HB3  . GLU   B  2  348 ? 18.697  -47.848 15.052   1.00 86.98  ? 352  GLU   B HB3  1 
ATOM   14346 H  HG2  . GLU   B  2  348 ? 16.466  -47.945 15.875   1.00 89.21  ? 352  GLU   B HG2  1 
ATOM   14347 H  HG3  . GLU   B  2  348 ? 15.985  -48.192 14.381   1.00 89.21  ? 352  GLU   B HG3  1 
ATOM   14348 N  N    . GLU   B  2  349 ? 19.546  -45.278 13.007   1.00 77.01  ? 353  GLU   B N    1 
ATOM   14349 C  CA   . GLU   B  2  349 ? 20.754  -44.516 12.710   1.00 78.64  ? 353  GLU   B CA   1 
ATOM   14350 C  C    . GLU   B  2  349 ? 20.615  -43.078 13.194   1.00 74.17  ? 353  GLU   B C    1 
ATOM   14351 O  O    . GLU   B  2  349 ? 21.562  -42.505 13.745   1.00 74.22  ? 353  GLU   B O    1 
ATOM   14352 C  CB   . GLU   B  2  349 ? 21.059  -44.548 11.211   1.00 87.16  ? 353  GLU   B CB   1 
ATOM   14353 C  CG   . GLU   B  2  349 ? 22.481  -44.099 10.879   1.00 101.13 ? 353  GLU   B CG   1 
ATOM   14354 C  CD   . GLU   B  2  349 ? 22.791  -44.137 9.395    1.00 115.57 ? 353  GLU   B CD   1 
ATOM   14355 O  OE1  . GLU   B  2  349 ? 21.962  -44.661 8.622    1.00 120.47 ? 353  GLU   B OE1  1 
ATOM   14356 O  OE2  . GLU   B  2  349 ? 23.868  -43.640 9.002    1.00 120.94 ? 353  GLU   B OE2  1 
ATOM   14357 H  H    . GLU   B  2  349 ? 19.156  -45.628 12.325   1.00 92.45  ? 353  GLU   B H    1 
ATOM   14358 H  HA   . GLU   B  2  349 ? 21.502  -44.929 13.168   1.00 94.40  ? 353  GLU   B HA   1 
ATOM   14359 H  HB2  . GLU   B  2  349 ? 20.949  -45.456 10.887   1.00 104.63 ? 353  GLU   B HB2  1 
ATOM   14360 H  HB3  . GLU   B  2  349 ? 20.444  -43.955 10.752   1.00 104.63 ? 353  GLU   B HB3  1 
ATOM   14361 H  HG2  . GLU   B  2  349 ? 22.602  -43.187 11.185   1.00 121.39 ? 353  GLU   B HG2  1 
ATOM   14362 H  HG3  . GLU   B  2  349 ? 23.109  -44.686 11.329   1.00 121.39 ? 353  GLU   B HG3  1 
ATOM   14363 N  N    . LEU   B  2  350 ? 19.433  -42.483 13.011   1.00 70.25  ? 354  LEU   B N    1 
ATOM   14364 C  CA   . LEU   B  2  350 ? 19.218  -41.107 13.449   1.00 63.61  ? 354  LEU   B CA   1 
ATOM   14365 C  C    . LEU   B  2  350 ? 19.356  -40.982 14.963   1.00 62.93  ? 354  LEU   B C    1 
ATOM   14366 O  O    . LEU   B  2  350 ? 20.056  -40.093 15.461   1.00 61.36  ? 354  LEU   B O    1 
ATOM   14367 C  CB   . LEU   B  2  350 ? 17.844  -40.615 12.992   1.00 62.44  ? 354  LEU   B CB   1 
ATOM   14368 C  CG   . LEU   B  2  350 ? 17.677  -40.287 11.507   1.00 60.85  ? 354  LEU   B CG   1 
ATOM   14369 C  CD1  . LEU   B  2  350 ? 16.224  -39.957 11.205   1.00 61.71  ? 354  LEU   B CD1  1 
ATOM   14370 C  CD2  . LEU   B  2  350 ? 18.577  -39.132 11.094   1.00 58.49  ? 354  LEU   B CD2  1 
ATOM   14371 H  H    . LEU   B  2  350 ? 18.749  -42.850 12.641   1.00 84.33  ? 354  LEU   B H    1 
ATOM   14372 H  HA   . LEU   B  2  350 ? 19.892  -40.543 13.037   1.00 76.37  ? 354  LEU   B HA   1 
ATOM   14373 H  HB2  . LEU   B  2  350 ? 17.196  -41.306 13.203   1.00 74.96  ? 354  LEU   B HB2  1 
ATOM   14374 H  HB3  . LEU   B  2  350 ? 17.638  -39.806 13.485   1.00 74.96  ? 354  LEU   B HB3  1 
ATOM   14375 H  HG   . LEU   B  2  350 ? 17.937  -41.063 10.986   1.00 73.06  ? 354  LEU   B HG   1 
ATOM   14376 H  HD11 . LEU   B  2  350 ? 16.135  -39.761 10.259   1.00 74.09  ? 354  LEU   B HD11 1 
ATOM   14377 H  HD12 . LEU   B  2  350 ? 15.672  -40.720 11.438   1.00 74.09  ? 354  LEU   B HD12 1 
ATOM   14378 H  HD13 . LEU   B  2  350 ? 15.960  -39.185 11.729   1.00 74.09  ? 354  LEU   B HD13 1 
ATOM   14379 H  HD21 . LEU   B  2  350 ? 18.435  -38.942 10.153   1.00 70.22  ? 354  LEU   B HD21 1 
ATOM   14380 H  HD22 . LEU   B  2  350 ? 18.354  -38.352 11.626   1.00 70.22  ? 354  LEU   B HD22 1 
ATOM   14381 H  HD23 . LEU   B  2  350 ? 19.502  -39.382 11.245   1.00 70.22  ? 354  LEU   B HD23 1 
ATOM   14382 N  N    . ARG   B  2  351 ? 18.691  -41.863 15.717   1.00 64.13  ? 355  ARG   B N    1 
ATOM   14383 C  CA   . ARG   B  2  351 ? 18.798  -41.801 17.171   1.00 67.03  ? 355  ARG   B CA   1 
ATOM   14384 C  C    . ARG   B  2  351 ? 20.193  -42.158 17.669   1.00 72.46  ? 355  ARG   B C    1 
ATOM   14385 O  O    . ARG   B  2  351 ? 20.466  -41.991 18.862   1.00 72.08  ? 355  ARG   B O    1 
ATOM   14386 C  CB   . ARG   B  2  351 ? 17.785  -42.735 17.842   1.00 64.75  ? 355  ARG   B CB   1 
ATOM   14387 C  CG   . ARG   B  2  351 ? 16.324  -42.521 17.465   1.00 63.28  ? 355  ARG   B CG   1 
ATOM   14388 C  CD   . ARG   B  2  351 ? 15.736  -41.196 17.961   1.00 64.85  ? 355  ARG   B CD   1 
ATOM   14389 N  NE   . ARG   B  2  351 ? 15.783  -40.999 19.413   1.00 68.09  ? 355  ARG   B NE   1 
ATOM   14390 C  CZ   . ARG   B  2  351 ? 15.144  -41.747 20.310   1.00 73.70  ? 355  ARG   B CZ   1 
ATOM   14391 N  NH1  . ARG   B  2  351 ? 14.416  -42.790 19.933   1.00 77.85  ? 355  ARG   B NH1  1 
ATOM   14392 N  NH2  . ARG   B  2  351 ? 15.249  -41.459 21.601   1.00 76.39  ? 355  ARG   B NH2  1 
ATOM   14393 H  H    . ARG   B  2  351 ? 18.185  -42.490 15.416   1.00 76.99  ? 355  ARG   B H    1 
ATOM   14394 H  HA   . ARG   B  2  351 ? 18.587  -40.894 17.441   1.00 80.47  ? 355  ARG   B HA   1 
ATOM   14395 H  HB2  . ARG   B  2  351 ? 18.012  -43.648 17.605   1.00 77.74  ? 355  ARG   B HB2  1 
ATOM   14396 H  HB3  . ARG   B  2  351 ? 17.854  -42.616 18.803   1.00 77.74  ? 355  ARG   B HB3  1 
ATOM   14397 H  HG2  . ARG   B  2  351 ? 16.247  -42.533 16.498   1.00 75.97  ? 355  ARG   B HG2  1 
ATOM   14398 H  HG3  . ARG   B  2  351 ? 15.795  -43.238 17.849   1.00 75.97  ? 355  ARG   B HG3  1 
ATOM   14399 H  HD2  . ARG   B  2  351 ? 16.232  -40.468 17.554   1.00 77.85  ? 355  ARG   B HD2  1 
ATOM   14400 H  HD3  . ARG   B  2  351 ? 14.805  -41.153 17.693   1.00 77.85  ? 355  ARG   B HD3  1 
ATOM   14401 H  HE   . ARG   B  2  351 ? 16.262  -40.349 19.708   1.00 81.74  ? 355  ARG   B HE   1 
ATOM   14402 H  HH11 . ARG   B  2  351 ? 14.352  -42.991 19.099   1.00 93.46  ? 355  ARG   B HH11 1 
ATOM   14403 H  HH12 . ARG   B  2  351 ? 14.007  -43.265 20.522   1.00 93.46  ? 355  ARG   B HH12 1 
ATOM   14404 H  HH21 . ARG   B  2  351 ? 15.729  -40.792 21.855   1.00 91.70  ? 355  ARG   B HH21 1 
ATOM   14405 H  HH22 . ARG   B  2  351 ? 14.838  -41.939 22.183   1.00 91.70  ? 355  ARG   B HH22 1 
ATOM   14406 N  N    . SER   B  2  352 ? 21.072  -42.649 16.794   1.00 77.98  ? 356  SER   B N    1 
ATOM   14407 C  CA   . SER   B  2  352 ? 22.424  -43.039 17.168   1.00 87.41  ? 356  SER   B CA   1 
ATOM   14408 C  C    . SER   B  2  352 ? 23.458  -41.970 16.849   1.00 84.79  ? 356  SER   B C    1 
ATOM   14409 O  O    . SER   B  2  352 ? 24.655  -42.214 17.030   1.00 85.29  ? 356  SER   B O    1 
ATOM   14410 C  CB   . SER   B  2  352 ? 22.811  -44.339 16.456   1.00 96.12  ? 356  SER   B CB   1 
ATOM   14411 O  OG   . SER   B  2  352 ? 22.831  -44.159 15.050   1.00 101.21 ? 356  SER   B OG   1 
ATOM   14412 H  H    . SER   B  2  352 ? 20.901  -42.766 15.960   1.00 93.61  ? 356  SER   B H    1 
ATOM   14413 H  HA   . SER   B  2  352 ? 22.442  -43.199 18.124   1.00 104.93 ? 356  SER   B HA   1 
ATOM   14414 H  HB2  . SER   B  2  352 ? 23.694  -44.611 16.752   1.00 115.39 ? 356  SER   B HB2  1 
ATOM   14415 H  HB3  . SER   B  2  352 ? 22.161  -45.025 16.677   1.00 115.39 ? 356  SER   B HB3  1 
ATOM   14416 H  HG   . SER   B  2  352 ? 23.241  -43.451 14.857   1.00 121.49 ? 356  SER   B HG   1 
ATOM   14417 N  N    . GLU   B  2  353 ? 23.033  -40.804 16.370   1.00 92.51  ? 357  GLU   B N    1 
ATOM   14418 C  CA   . GLU   B  2  353 ? 23.943  -39.742 15.982   1.00 86.60  ? 357  GLU   B CA   1 
ATOM   14419 C  C    . GLU   B  2  353 ? 23.516  -38.430 16.620   1.00 74.10  ? 357  GLU   B C    1 
ATOM   14420 O  O    . GLU   B  2  353 ? 22.397  -38.286 17.120   1.00 71.78  ? 357  GLU   B O    1 
ATOM   14421 C  CB   . GLU   B  2  353 ? 23.987  -39.555 14.458   1.00 91.49  ? 357  GLU   B CB   1 
ATOM   14422 C  CG   . GLU   B  2  353 ? 24.566  -40.719 13.680   1.00 101.01 ? 357  GLU   B CG   1 
ATOM   14423 C  CD   . GLU   B  2  353 ? 24.389  -40.549 12.183   1.00 106.56 ? 357  GLU   B CD   1 
ATOM   14424 O  OE1  . GLU   B  2  353 ? 23.562  -39.706 11.774   1.00 104.87 ? 357  GLU   B OE1  1 
ATOM   14425 O  OE2  . GLU   B  2  353 ? 25.079  -41.251 11.415   1.00 111.25 ? 357  GLU   B OE2  1 
ATOM   14426 H  H    . GLU   B  2  353 ? 22.204  -40.605 16.260   1.00 111.05 ? 357  GLU   B H    1 
ATOM   14427 H  HA   . GLU   B  2  353 ? 24.830  -39.971 16.299   1.00 103.95 ? 357  GLU   B HA   1 
ATOM   14428 H  HB2  . GLU   B  2  353 ? 23.081  -39.416 14.140   1.00 109.83 ? 357  GLU   B HB2  1 
ATOM   14429 H  HB3  . GLU   B  2  353 ? 24.531  -38.776 14.261   1.00 109.83 ? 357  GLU   B HB3  1 
ATOM   14430 H  HG2  . GLU   B  2  353 ? 25.515  -40.787 13.867   1.00 121.24 ? 357  GLU   B HG2  1 
ATOM   14431 H  HG3  . GLU   B  2  353 ? 24.116  -41.536 13.947   1.00 121.24 ? 357  GLU   B HG3  1 
ATOM   14432 N  N    . VAL   B  2  354 ? 24.439  -37.474 16.596   1.00 68.23  ? 358  VAL   B N    1 
ATOM   14433 C  CA   . VAL   B  2  354 ? 24.142  -36.070 16.850   1.00 60.54  ? 358  VAL   B CA   1 
ATOM   14434 C  C    . VAL   B  2  354 ? 25.026  -35.263 15.914   1.00 57.66  ? 358  VAL   B C    1 
ATOM   14435 O  O    . VAL   B  2  354 ? 26.256  -35.357 15.987   1.00 58.44  ? 358  VAL   B O    1 
ATOM   14436 C  CB   . VAL   B  2  354 ? 24.391  -35.653 18.308   1.00 59.59  ? 358  VAL   B CB   1 
ATOM   14437 C  CG1  . VAL   B  2  354 ? 24.178  -34.148 18.470   1.00 56.48  ? 358  VAL   B CG1  1 
ATOM   14438 C  CG2  . VAL   B  2  354 ? 23.480  -36.423 19.246   1.00 62.60  ? 358  VAL   B CG2  1 
ATOM   14439 H  H    . VAL   B  2  354 ? 25.270  -37.619 16.430   1.00 81.91  ? 358  VAL   B H    1 
ATOM   14440 H  HA   . VAL   B  2  354 ? 23.209  -35.895 16.653   1.00 72.69  ? 358  VAL   B HA   1 
ATOM   14441 H  HB   . VAL   B  2  354 ? 25.309  -35.859 18.543   1.00 71.54  ? 358  VAL   B HB   1 
ATOM   14442 H  HG11 . VAL   B  2  354 ? 24.313  -33.909 19.400   1.00 67.81  ? 358  VAL   B HG11 1 
ATOM   14443 H  HG12 . VAL   B  2  354 ? 24.816  -33.677 17.911   1.00 67.81  ? 358  VAL   B HG12 1 
ATOM   14444 H  HG13 . VAL   B  2  354 ? 23.274  -33.926 18.199   1.00 67.81  ? 358  VAL   B HG13 1 
ATOM   14445 H  HG21 . VAL   B  2  354 ? 23.652  -36.140 20.157   1.00 75.16  ? 358  VAL   B HG21 1 
ATOM   14446 H  HG22 . VAL   B  2  354 ? 22.557  -36.239 19.011   1.00 75.16  ? 358  VAL   B HG22 1 
ATOM   14447 H  HG23 . VAL   B  2  354 ? 23.661  -37.372 19.154   1.00 75.16  ? 358  VAL   B HG23 1 
ATOM   14448 N  N    . GLU   B  2  355 ? 24.410  -34.485 15.034   1.00 57.72  ? 359  GLU   B N    1 
ATOM   14449 C  CA   . GLU   B  2  355 ? 25.121  -33.598 14.127   1.00 58.63  ? 359  GLU   B CA   1 
ATOM   14450 C  C    . GLU   B  2  355 ? 24.669  -32.178 14.414   1.00 61.14  ? 359  GLU   B C    1 
ATOM   14451 O  O    . GLU   B  2  355 ? 23.468  -31.925 14.552   1.00 66.02  ? 359  GLU   B O    1 
ATOM   14452 C  CB   . GLU   B  2  355 ? 24.852  -33.960 12.666   1.00 63.42  ? 359  GLU   B CB   1 
ATOM   14453 C  CG   . GLU   B  2  355 ? 25.504  -33.019 11.665   1.00 70.13  ? 359  GLU   B CG   1 
ATOM   14454 C  CD   . GLU   B  2  355 ? 25.374  -33.511 10.238   1.00 78.53  ? 359  GLU   B CD   1 
ATOM   14455 O  OE1  . GLU   B  2  355 ? 24.910  -34.655 10.045   1.00 82.04  ? 359  GLU   B OE1  1 
ATOM   14456 O  OE2  . GLU   B  2  355 ? 25.734  -32.756 9.311    1.00 82.07  ? 359  GLU   B OE2  1 
ATOM   14457 H  H    . GLU   B  2  355 ? 23.556  -34.453 14.942   1.00 69.30  ? 359  GLU   B H    1 
ATOM   14458 H  HA   . GLU   B  2  355 ? 26.078  -33.665 14.272   1.00 70.40  ? 359  GLU   B HA   1 
ATOM   14459 H  HB2  . GLU   B  2  355 ? 25.194  -34.852 12.499   1.00 76.14  ? 359  GLU   B HB2  1 
ATOM   14460 H  HB3  . GLU   B  2  355 ? 23.894  -33.938 12.512   1.00 76.14  ? 359  GLU   B HB3  1 
ATOM   14461 H  HG2  . GLU   B  2  355 ? 25.078  -32.149 11.724   1.00 84.20  ? 359  GLU   B HG2  1 
ATOM   14462 H  HG3  . GLU   B  2  355 ? 26.448  -32.940 11.872   1.00 84.20  ? 359  GLU   B HG3  1 
ATOM   14463 N  N    . LEU   B  2  356 ? 25.618  -31.259 14.519   1.00 61.20  ? 360  LEU   B N    1 
ATOM   14464 C  CA   . LEU   B  2  356 ? 25.245  -29.883 14.795   1.00 58.11  ? 360  LEU   B CA   1 
ATOM   14465 C  C    . LEU   B  2  356 ? 24.911  -29.144 13.506   1.00 64.08  ? 360  LEU   B C    1 
ATOM   14466 O  O    . LEU   B  2  356 ? 25.255  -29.562 12.397   1.00 67.37  ? 360  LEU   B O    1 
ATOM   14467 C  CB   . LEU   B  2  356 ? 26.345  -29.141 15.553   1.00 52.40  ? 360  LEU   B CB   1 
ATOM   14468 C  CG   . LEU   B  2  356 ? 26.200  -29.111 17.079   1.00 52.74  ? 360  LEU   B CG   1 
ATOM   14469 C  CD1  . LEU   B  2  356 ? 27.288  -28.241 17.680   1.00 53.05  ? 360  LEU   B CD1  1 
ATOM   14470 C  CD2  . LEU   B  2  356 ? 24.824  -28.613 17.533   1.00 56.07  ? 360  LEU   B CD2  1 
ATOM   14471 H  H    . LEU   B  2  356 ? 26.462  -31.404 14.436   1.00 73.48  ? 360  LEU   B H    1 
ATOM   14472 H  HA   . LEU   B  2  356 ? 24.456  -29.889 15.359   1.00 69.77  ? 360  LEU   B HA   1 
ATOM   14473 H  HB2  . LEU   B  2  356 ? 27.192  -29.567 15.353   1.00 62.92  ? 360  LEU   B HB2  1 
ATOM   14474 H  HB3  . LEU   B  2  356 ? 26.356  -28.221 15.247   1.00 62.92  ? 360  LEU   B HB3  1 
ATOM   14475 H  HG   . LEU   B  2  356 ? 26.289  -30.021 17.403   1.00 63.32  ? 360  LEU   B HG   1 
ATOM   14476 H  HD11 . LEU   B  2  356 ? 27.188  -28.232 18.644   1.00 63.70  ? 360  LEU   B HD11 1 
ATOM   14477 H  HD12 . LEU   B  2  356 ? 28.153  -28.607 17.440   1.00 63.70  ? 360  LEU   B HD12 1 
ATOM   14478 H  HD13 . LEU   B  2  356 ? 27.201  -27.340 17.330   1.00 63.70  ? 360  LEU   B HD13 1 
ATOM   14479 H  HD21 . LEU   B  2  356 ? 24.820  -28.534 18.500   1.00 67.32  ? 360  LEU   B HD21 1 
ATOM   14480 H  HD22 . LEU   B  2  356 ? 24.652  -27.748 17.130   1.00 67.32  ? 360  LEU   B HD22 1 
ATOM   14481 H  HD23 . LEU   B  2  356 ? 24.149  -29.250 17.250   1.00 67.32  ? 360  LEU   B HD23 1 
ATOM   14482 N  N    . GLU   B  2  357 ? 24.226  -28.023 13.686   1.00 65.07  ? 361  GLU   B N    1 
ATOM   14483 C  CA   . GLU   B  2  357 ? 23.690  -27.213 12.606   1.00 66.82  ? 361  GLU   B CA   1 
ATOM   14484 C  C    . GLU   B  2  357 ? 23.736  -25.777 13.098   1.00 66.99  ? 361  GLU   B C    1 
ATOM   14485 O  O    . GLU   B  2  357 ? 23.390  -25.509 14.251   1.00 69.65  ? 361  GLU   B O    1 
ATOM   14486 C  CB   . GLU   B  2  357 ? 22.258  -27.638 12.267   1.00 73.85  ? 361  GLU   B CB   1 
ATOM   14487 C  CG   . GLU   B  2  357 ? 21.909  -27.648 10.790   1.00 80.58  ? 361  GLU   B CG   1 
ATOM   14488 C  CD   . GLU   B  2  357 ? 20.504  -28.168 10.543   1.00 86.62  ? 361  GLU   B CD   1 
ATOM   14489 O  OE1  . GLU   B  2  357 ? 19.790  -28.436 11.532   1.00 86.25  ? 361  GLU   B OE1  1 
ATOM   14490 O  OE2  . GLU   B  2  357 ? 20.116  -28.312 9.364    1.00 92.56  ? 361  GLU   B OE2  1 
ATOM   14491 H  H    . GLU   B  2  357 ? 24.050  -27.696 14.461   1.00 78.12  ? 361  GLU   B H    1 
ATOM   14492 H  HA   . GLU   B  2  357 ? 24.212  -27.294 11.793   1.00 80.23  ? 361  GLU   B HA   1 
ATOM   14493 H  HB2  . GLU   B  2  357 ? 22.119  -28.537 12.603   1.00 88.66  ? 361  GLU   B HB2  1 
ATOM   14494 H  HB3  . GLU   B  2  357 ? 21.647  -27.023 12.703   1.00 88.66  ? 361  GLU   B HB3  1 
ATOM   14495 H  HG2  . GLU   B  2  357 ? 21.963  -26.744 10.443   1.00 96.74  ? 361  GLU   B HG2  1 
ATOM   14496 H  HG3  . GLU   B  2  357 ? 22.532  -28.223 10.319   1.00 96.74  ? 361  GLU   B HG3  1 
ATOM   14497 N  N    . VAL   B  2  358 ? 24.183  -24.862 12.244   1.00 65.25  ? 362  VAL   B N    1 
ATOM   14498 C  CA   . VAL   B  2  358 ? 24.306  -23.459 12.619   1.00 63.75  ? 362  VAL   B CA   1 
ATOM   14499 C  C    . VAL   B  2  358 ? 23.575  -22.626 11.579   1.00 67.92  ? 362  VAL   B C    1 
ATOM   14500 O  O    . VAL   B  2  358 ? 23.971  -22.597 10.407   1.00 70.93  ? 362  VAL   B O    1 
ATOM   14501 C  CB   . VAL   B  2  358 ? 25.770  -23.014 12.749   1.00 62.55  ? 362  VAL   B CB   1 
ATOM   14502 C  CG1  . VAL   B  2  358 ? 25.833  -21.543 13.124   1.00 62.93  ? 362  VAL   B CG1  1 
ATOM   14503 C  CG2  . VAL   B  2  358 ? 26.481  -23.859 13.794   1.00 61.77  ? 362  VAL   B CG2  1 
ATOM   14504 H  H    . VAL   B  2  358 ? 24.424  -25.033 11.436   1.00 78.33  ? 362  VAL   B H    1 
ATOM   14505 H  HA   . VAL   B  2  358 ? 23.873  -23.319 13.476   1.00 76.54  ? 362  VAL   B HA   1 
ATOM   14506 H  HB   . VAL   B  2  358 ? 26.221  -23.135 11.898   1.00 75.09  ? 362  VAL   B HB   1 
ATOM   14507 H  HG11 . VAL   B  2  358 ? 26.761  -21.287 13.241   1.00 75.55  ? 362  VAL   B HG11 1 
ATOM   14508 H  HG12 . VAL   B  2  358 ? 25.432  -21.018 12.414   1.00 75.55  ? 362  VAL   B HG12 1 
ATOM   14509 H  HG13 . VAL   B  2  358 ? 25.346  -21.407 13.952   1.00 75.55  ? 362  VAL   B HG13 1 
ATOM   14510 H  HG21 . VAL   B  2  358 ? 27.392  -23.541 13.891   1.00 74.16  ? 362  VAL   B HG21 1 
ATOM   14511 H  HG22 . VAL   B  2  358 ? 26.011  -23.778 14.639   1.00 74.16  ? 362  VAL   B HG22 1 
ATOM   14512 H  HG23 . VAL   B  2  358 ? 26.483  -24.785 13.504   1.00 74.16  ? 362  VAL   B HG23 1 
ATOM   14513 N  N    . LEU   B  2  359 ? 22.515  -21.952 12.011   1.00 67.35  ? 363  LEU   B N    1 
ATOM   14514 C  CA   . LEU   B  2  359 ? 21.598  -21.247 11.133   1.00 67.67  ? 363  LEU   B CA   1 
ATOM   14515 C  C    . LEU   B  2  359 ? 21.549  -19.776 11.524   1.00 65.43  ? 363  LEU   B C    1 
ATOM   14516 O  O    . LEU   B  2  359 ? 21.986  -19.385 12.609   1.00 60.99  ? 363  LEU   B O    1 
ATOM   14517 C  CB   . LEU   B  2  359 ? 20.191  -21.861 11.207   1.00 72.20  ? 363  LEU   B CB   1 
ATOM   14518 C  CG   . LEU   B  2  359 ? 20.011  -23.312 10.742   1.00 75.22  ? 363  LEU   B CG   1 
ATOM   14519 C  CD1  . LEU   B  2  359 ? 20.705  -24.329 11.645   1.00 74.90  ? 363  LEU   B CD1  1 
ATOM   14520 C  CD2  . LEU   B  2  359 ? 18.531  -23.640 10.651   1.00 80.14  ? 363  LEU   B CD2  1 
ATOM   14521 H  H    . LEU   B  2  359 ? 22.300  -21.888 12.841   1.00 80.85  ? 363  LEU   B H    1 
ATOM   14522 H  HA   . LEU   B  2  359 ? 21.908  -21.306 10.216   1.00 81.24  ? 363  LEU   B HA   1 
ATOM   14523 H  HB2  . LEU   B  2  359 ? 19.904  -21.828 12.133   1.00 86.67  ? 363  LEU   B HB2  1 
ATOM   14524 H  HB3  . LEU   B  2  359 ? 19.604  -21.318 10.658   1.00 86.67  ? 363  LEU   B HB3  1 
ATOM   14525 H  HG   . LEU   B  2  359 ? 20.429  -23.389 9.869    1.00 90.30  ? 363  LEU   B HG   1 
ATOM   14526 H  HD11 . LEU   B  2  359 ? 20.464  -25.223 11.358   1.00 89.92  ? 363  LEU   B HD11 1 
ATOM   14527 H  HD12 . LEU   B  2  359 ? 21.665  -24.207 11.579   1.00 89.92  ? 363  LEU   B HD12 1 
ATOM   14528 H  HD13 . LEU   B  2  359 ? 20.416  -24.187 12.560   1.00 89.92  ? 363  LEU   B HD13 1 
ATOM   14529 H  HD21 . LEU   B  2  359 ? 18.428  -24.563 10.371   1.00 96.20  ? 363  LEU   B HD21 1 
ATOM   14530 H  HD22 . LEU   B  2  359 ? 18.126  -23.512 11.523   1.00 96.20  ? 363  LEU   B HD22 1 
ATOM   14531 H  HD23 . LEU   B  2  359 ? 18.116  -23.049 10.003   1.00 96.20  ? 363  LEU   B HD23 1 
ATOM   14532 N  N    . GLY   B  2  360 ? 21.008  -18.960 10.622   1.00 67.79  ? 364  GLY   B N    1 
ATOM   14533 C  CA   . GLY   B  2  360 ? 20.857  -17.542 10.883   1.00 74.77  ? 364  GLY   B CA   1 
ATOM   14534 C  C    . GLY   B  2  360 ? 21.796  -16.684 10.061   1.00 80.96  ? 364  GLY   B C    1 
ATOM   14535 O  O    . GLY   B  2  360 ? 22.185  -17.064 8.952    1.00 82.43  ? 364  GLY   B O    1 
ATOM   14536 H  H    . GLY   B  2  360 ? 20.722  -19.208 9.850    1.00 81.38  ? 364  GLY   B H    1 
ATOM   14537 H  HA2  . GLY   B  2  360 ? 19.947  -17.276 10.678   1.00 89.76  ? 364  GLY   B HA2  1 
ATOM   14538 H  HA3  . GLY   B  2  360 ? 21.033  -17.370 11.821   1.00 89.76  ? 364  GLY   B HA3  1 
ATOM   14539 N  N    . ASP   B  2  361 ? 22.166  -15.518 10.593   1.00 86.24  ? 365  ASP   B N    1 
ATOM   14540 C  CA   . ASP   B  2  361 ? 23.101  -14.616 9.922    1.00 92.87  ? 365  ASP   B CA   1 
ATOM   14541 C  C    . ASP   B  2  361 ? 24.519  -15.121 10.172   1.00 86.08  ? 365  ASP   B C    1 
ATOM   14542 O  O    . ASP   B  2  361 ? 25.250  -14.635 11.038   1.00 85.08  ? 365  ASP   B O    1 
ATOM   14543 C  CB   . ASP   B  2  361 ? 22.924  -13.184 10.413   1.00 105.49 ? 365  ASP   B CB   1 
ATOM   14544 C  CG   . ASP   B  2  361 ? 21.622  -12.562 9.948    1.00 123.04 ? 365  ASP   B CG   1 
ATOM   14545 O  OD1  . ASP   B  2  361 ? 20.974  -13.135 9.047    1.00 131.02 ? 365  ASP   B OD1  1 
ATOM   14546 O  OD2  . ASP   B  2  361 ? 21.244  -11.499 10.485   1.00 132.18 ? 365  ASP   B OD2  1 
ATOM   14547 H  H    . ASP   B  2  361 ? 21.885  -15.224 11.351   1.00 103.52 ? 365  ASP   B H    1 
ATOM   14548 H  HA   . ASP   B  2  361 ? 22.927  -14.633 8.967    1.00 111.48 ? 365  ASP   B HA   1 
ATOM   14549 H  HB2  . ASP   B  2  361 ? 22.929  -13.180 11.383   1.00 126.63 ? 365  ASP   B HB2  1 
ATOM   14550 H  HB3  . ASP   B  2  361 ? 23.654  -12.642 10.075   1.00 126.63 ? 365  ASP   B HB3  1 
ATOM   14551 N  N    . THR   B  2  362 ? 24.910  -16.124 9.389    1.00 81.56  ? 366  THR   B N    1 
ATOM   14552 C  CA   . THR   B  2  362 ? 26.237  -16.710 9.493    1.00 77.21  ? 366  THR   B CA   1 
ATOM   14553 C  C    . THR   B  2  362 ? 27.170  -16.281 8.369    1.00 77.32  ? 366  THR   B C    1 
ATOM   14554 O  O    . THR   B  2  362 ? 28.376  -16.529 8.461    1.00 74.27  ? 366  THR   B O    1 
ATOM   14555 C  CB   . THR   B  2  362 ? 26.143  -18.240 9.506    1.00 75.68  ? 366  THR   B CB   1 
ATOM   14556 O  OG1  . THR   B  2  362 ? 25.535  -18.695 8.291    1.00 84.15  ? 366  THR   B OG1  1 
ATOM   14557 C  CG2  . THR   B  2  362 ? 25.317  -18.707 10.689   1.00 70.10  ? 366  THR   B CG2  1 
ATOM   14558 H  H    . THR   B  2  362 ? 24.417  -16.485 8.783    1.00 97.91  ? 366  THR   B H    1 
ATOM   14559 H  HA   . THR   B  2  362 ? 26.632  -16.427 10.332   1.00 92.68  ? 366  THR   B HA   1 
ATOM   14560 H  HB   . THR   B  2  362 ? 27.032  -18.620 9.582    1.00 90.85  ? 366  THR   B HB   1 
ATOM   14561 H  HG1  . THR   B  2  362 ? 25.513  -19.534 8.278    1.00 101.01 ? 366  THR   B HG1  1 
ATOM   14562 H  HG21 . THR   B  2  362 ? 25.450  -19.657 10.832   1.00 84.16  ? 366  THR   B HG21 1 
ATOM   14563 H  HG22 . THR   B  2  362 ? 25.583  -18.228 11.489   1.00 84.16  ? 366  THR   B HG22 1 
ATOM   14564 H  HG23 . THR   B  2  362 ? 24.376  -18.543 10.522   1.00 84.16  ? 366  THR   B HG23 1 
ATOM   14565 N  N    . GLU   B  2  363 ? 26.650  -15.647 7.321    1.00 80.52  ? 367  GLU   B N    1 
ATOM   14566 C  CA   . GLU   B  2  363 ? 27.496  -15.235 6.210    1.00 79.96  ? 367  GLU   B CA   1 
ATOM   14567 C  C    . GLU   B  2  363 ? 28.613  -14.325 6.700    1.00 72.30  ? 367  GLU   B C    1 
ATOM   14568 O  O    . GLU   B  2  363 ? 28.398  -13.435 7.527    1.00 69.42  ? 367  GLU   B O    1 
ATOM   14569 C  CB   . GLU   B  2  363 ? 26.663  -14.526 5.143    1.00 89.07  ? 367  GLU   B CB   1 
ATOM   14570 C  CG   . GLU   B  2  363 ? 26.376  -15.387 3.925    1.00 93.91  ? 367  GLU   B CG   1 
ATOM   14571 C  CD   . GLU   B  2  363 ? 27.533  -15.409 2.946    1.00 98.62  ? 367  GLU   B CD   1 
ATOM   14572 O  OE1  . GLU   B  2  363 ? 27.673  -14.441 2.168    1.00 104.00 ? 367  GLU   B OE1  1 
ATOM   14573 O  OE2  . GLU   B  2  363 ? 28.307  -16.390 2.959    1.00 96.91  ? 367  GLU   B OE2  1 
ATOM   14574 H  H    . GLU   B  2  363 ? 25.818  -15.446 7.231    1.00 96.67  ? 367  GLU   B H    1 
ATOM   14575 H  HA   . GLU   B  2  363 ? 27.898  -16.019 5.805    1.00 95.98  ? 367  GLU   B HA   1 
ATOM   14576 H  HB2  . GLU   B  2  363 ? 25.812  -14.268 5.531    1.00 106.92 ? 367  GLU   B HB2  1 
ATOM   14577 H  HB3  . GLU   B  2  363 ? 27.143  -13.738 4.844    1.00 106.92 ? 367  GLU   B HB3  1 
ATOM   14578 H  HG2  . GLU   B  2  363 ? 26.208  -16.297 4.213    1.00 112.73 ? 367  GLU   B HG2  1 
ATOM   14579 H  HG3  . GLU   B  2  363 ? 25.598  -15.035 3.464    1.00 112.73 ? 367  GLU   B HG3  1 
ATOM   14580 N  N    . GLY   B  2  364 ? 29.817  -14.559 6.186    1.00 72.63  ? 368  GLY   B N    1 
ATOM   14581 C  CA   . GLY   B  2  364 ? 30.967  -13.772 6.574    1.00 72.42  ? 368  GLY   B CA   1 
ATOM   14582 C  C    . GLY   B  2  364 ? 31.571  -14.140 7.907    1.00 73.10  ? 368  GLY   B C    1 
ATOM   14583 O  O    . GLY   B  2  364 ? 32.490  -13.450 8.363    1.00 74.19  ? 368  GLY   B O    1 
ATOM   14584 H  H    . GLY   B  2  364 ? 29.989  -15.172 5.609    1.00 87.20  ? 368  GLY   B H    1 
ATOM   14585 H  HA2  . GLY   B  2  364 ? 31.655  -13.877 5.899    1.00 86.94  ? 368  GLY   B HA2  1 
ATOM   14586 H  HA3  . GLY   B  2  364 ? 30.705  -12.839 6.616    1.00 86.94  ? 368  GLY   B HA3  1 
ATOM   14587 N  N    . LEU   B  2  365 ? 31.088  -15.198 8.551    1.00 72.83  ? 369  LEU   B N    1 
ATOM   14588 C  CA   . LEU   B  2  365 ? 31.643  -15.660 9.812    1.00 69.94  ? 369  LEU   B CA   1 
ATOM   14589 C  C    . LEU   B  2  365 ? 32.545  -16.865 9.583    1.00 67.06  ? 369  LEU   B C    1 
ATOM   14590 O  O    . LEU   B  2  365 ? 32.370  -17.629 8.630    1.00 67.93  ? 369  LEU   B O    1 
ATOM   14591 C  CB   . LEU   B  2  365 ? 30.541  -16.035 10.807   1.00 73.24  ? 369  LEU   B CB   1 
ATOM   14592 C  CG   . LEU   B  2  365 ? 29.897  -14.914 11.626   1.00 81.76  ? 369  LEU   B CG   1 
ATOM   14593 C  CD1  . LEU   B  2  365 ? 28.894  -15.511 12.601   1.00 83.24  ? 369  LEU   B CD1  1 
ATOM   14594 C  CD2  . LEU   B  2  365 ? 30.936  -14.089 12.379   1.00 85.65  ? 369  LEU   B CD2  1 
ATOM   14595 H  H    . LEU   B  2  365 ? 30.427  -15.672 8.269    1.00 87.44  ? 369  LEU   B H    1 
ATOM   14596 H  HA   . LEU   B  2  365 ? 32.169  -14.945 10.202   1.00 83.97  ? 369  LEU   B HA   1 
ATOM   14597 H  HB2  . LEU   B  2  365 ? 29.826  -16.459 10.307   1.00 87.93  ? 369  LEU   B HB2  1 
ATOM   14598 H  HB3  . LEU   B  2  365 ? 30.919  -16.662 11.442   1.00 87.93  ? 369  LEU   B HB3  1 
ATOM   14599 H  HG   . LEU   B  2  365 ? 29.442  -14.310 11.020   1.00 98.14  ? 369  LEU   B HG   1 
ATOM   14600 H  HD11 . LEU   B  2  365 ? 28.104  -14.949 12.624   1.00 99.92  ? 369  LEU   B HD11 1 
ATOM   14601 H  HD12 . LEU   B  2  365 ? 28.657  -16.403 12.303   1.00 99.92  ? 369  LEU   B HD12 1 
ATOM   14602 H  HD13 . LEU   B  2  365 ? 29.297  -15.553 13.482   1.00 99.92  ? 369  LEU   B HD13 1 
ATOM   14603 H  HD21 . LEU   B  2  365 ? 30.492  -13.347 12.817   1.00 102.81 ? 369  LEU   B HD21 1 
ATOM   14604 H  HD22 . LEU   B  2  365 ? 31.369  -14.653 13.039   1.00 102.81 ? 369  LEU   B HD22 1 
ATOM   14605 H  HD23 . LEU   B  2  365 ? 31.593  -13.756 11.747   1.00 102.81 ? 369  LEU   B HD23 1 
ATOM   14606 N  N    . ASN   B  2  366 ? 33.516  -17.022 10.473   1.00 65.07  ? 370  ASN   B N    1 
ATOM   14607 C  CA   . ASN   B  2  366 ? 34.403  -18.175 10.475   1.00 62.80  ? 370  ASN   B CA   1 
ATOM   14608 C  C    . ASN   B  2  366 ? 33.984  -19.108 11.600   1.00 61.45  ? 370  ASN   B C    1 
ATOM   14609 O  O    . ASN   B  2  366 ? 33.867  -18.682 12.754   1.00 61.33  ? 370  ASN   B O    1 
ATOM   14610 C  CB   . ASN   B  2  366 ? 35.858  -17.744 10.649   1.00 65.34  ? 370  ASN   B CB   1 
ATOM   14611 C  CG   . ASN   B  2  366 ? 36.341  -16.859 9.518    1.00 67.88  ? 370  ASN   B CG   1 
ATOM   14612 O  OD1  . ASN   B  2  366 ? 36.161  -17.180 8.343    1.00 67.17  ? 370  ASN   B OD1  1 
ATOM   14613 N  ND2  . ASN   B  2  366 ? 36.949  -15.730 9.867    1.00 69.38  ? 370  ASN   B ND2  1 
ATOM   14614 H  H    . ASN   B  2  366 ? 33.685  -16.460 11.102   1.00 78.12  ? 370  ASN   B H    1 
ATOM   14615 H  HA   . ASN   B  2  366 ? 34.336  -18.650 9.632    1.00 75.39  ? 370  ASN   B HA   1 
ATOM   14616 H  HB2  . ASN   B  2  366 ? 35.945  -17.247 11.477   1.00 78.45  ? 370  ASN   B HB2  1 
ATOM   14617 H  HB3  . ASN   B  2  366 ? 36.422  -18.533 10.675   1.00 78.45  ? 370  ASN   B HB3  1 
ATOM   14618 H  HD21 . ASN   B  2  366 ? 37.241  -15.194 9.262    1.00 83.30  ? 370  ASN   B HD21 1 
ATOM   14619 H  HD22 . ASN   B  2  366 ? 37.050  -15.536 10.699   1.00 83.30  ? 370  ASN   B HD22 1 
ATOM   14620 N  N    . LEU   B  2  367 ? 33.745  -20.371 11.260   1.00 60.84  ? 371  LEU   B N    1 
ATOM   14621 C  CA   . LEU   B  2  367 ? 33.286  -21.364 12.219   1.00 59.37  ? 371  LEU   B CA   1 
ATOM   14622 C  C    . LEU   B  2  367 ? 34.222  -22.561 12.195   1.00 60.30  ? 371  LEU   B C    1 
ATOM   14623 O  O    . LEU   B  2  367 ? 34.575  -23.058 11.121   1.00 63.79  ? 371  LEU   B O    1 
ATOM   14624 C  CB   . LEU   B  2  367 ? 31.851  -21.806 11.911   1.00 59.74  ? 371  LEU   B CB   1 
ATOM   14625 C  CG   . LEU   B  2  367 ? 30.781  -20.713 11.977   1.00 60.71  ? 371  LEU   B CG   1 
ATOM   14626 C  CD1  . LEU   B  2  367 ? 29.413  -21.296 11.659   1.00 60.15  ? 371  LEU   B CD1  1 
ATOM   14627 C  CD2  . LEU   B  2  367 ? 30.768  -20.029 13.339   1.00 60.08  ? 371  LEU   B CD2  1 
ATOM   14628 H  H    . LEU   B  2  367 ? 33.845  -20.680 10.464   1.00 73.04  ? 371  LEU   B H    1 
ATOM   14629 H  HA   . LEU   B  2  367 ? 33.306  -20.983 13.111   1.00 71.28  ? 371  LEU   B HA   1 
ATOM   14630 H  HB2  . LEU   B  2  367 ? 31.833  -22.170 11.012   1.00 71.72  ? 371  LEU   B HB2  1 
ATOM   14631 H  HB3  . LEU   B  2  367 ? 31.602  -22.491 12.551   1.00 71.72  ? 371  LEU   B HB3  1 
ATOM   14632 H  HG   . LEU   B  2  367 ? 30.990  -20.035 11.315   1.00 72.88  ? 371  LEU   B HG   1 
ATOM   14633 H  HD11 . LEU   B  2  367 ? 28.728  -20.707 12.013   1.00 72.21  ? 371  LEU   B HD11 1 
ATOM   14634 H  HD12 . LEU   B  2  367 ? 29.318  -21.372 10.697   1.00 72.21  ? 371  LEU   B HD12 1 
ATOM   14635 H  HD13 . LEU   B  2  367 ? 29.340  -22.172 12.068   1.00 72.21  ? 371  LEU   B HD13 1 
ATOM   14636 H  HD21 . LEU   B  2  367 ? 30.079  -19.346 13.343   1.00 72.13  ? 371  LEU   B HD21 1 
ATOM   14637 H  HD22 . LEU   B  2  367 ? 30.581  -20.691 14.023   1.00 72.13  ? 371  LEU   B HD22 1 
ATOM   14638 H  HD23 . LEU   B  2  367 ? 31.635  -19.625 13.497   1.00 72.13  ? 371  LEU   B HD23 1 
ATOM   14639 N  N    . SER   B  2  368 ? 34.625  -23.011 13.379   1.00 59.64  ? 372  SER   B N    1 
ATOM   14640 C  CA   . SER   B  2  368 ? 35.398  -24.234 13.547   1.00 58.11  ? 372  SER   B CA   1 
ATOM   14641 C  C    . SER   B  2  368 ? 34.654  -25.126 14.527   1.00 53.23  ? 372  SER   B C    1 
ATOM   14642 O  O    . SER   B  2  368 ? 34.157  -24.655 15.555   1.00 56.79  ? 372  SER   B O    1 
ATOM   14643 C  CB   . SER   B  2  368 ? 36.816  -23.937 14.057   1.00 62.88  ? 372  SER   B CB   1 
ATOM   14644 O  OG   . SER   B  2  368 ? 37.587  -25.111 14.238   1.00 67.93  ? 372  SER   B OG   1 
ATOM   14645 H  H    . SER   B  2  368 ? 34.457  -22.612 14.122   1.00 71.60  ? 372  SER   B H    1 
ATOM   14646 H  HA   . SER   B  2  368 ? 35.490  -24.701 12.702   1.00 69.77  ? 372  SER   B HA   1 
ATOM   14647 H  HB2  . SER   B  2  368 ? 37.265  -23.370 13.410   1.00 75.50  ? 372  SER   B HB2  1 
ATOM   14648 H  HB3  . SER   B  2  368 ? 36.749  -23.478 14.909   1.00 75.50  ? 372  SER   B HB3  1 
ATOM   14649 H  HG   . SER   B  2  368 ? 38.251  -24.947 14.725   1.00 81.55  ? 372  SER   B HG   1 
ATOM   14650 N  N    . PHE   B  2  369 ? 34.564  -26.411 14.198   1.00 49.69  ? 373  PHE   B N    1 
ATOM   14651 C  CA   . PHE   B  2  369 ? 33.823  -27.375 14.996   1.00 52.13  ? 373  PHE   B CA   1 
ATOM   14652 C  C    . PHE   B  2  369 ? 34.756  -28.480 15.464   1.00 55.57  ? 373  PHE   B C    1 
ATOM   14653 O  O    . PHE   B  2  369 ? 35.523  -29.033 14.669   1.00 58.70  ? 373  PHE   B O    1 
ATOM   14654 C  CB   . PHE   B  2  369 ? 32.665  -27.980 14.200   1.00 51.31  ? 373  PHE   B CB   1 
ATOM   14655 C  CG   . PHE   B  2  369 ? 31.641  -26.976 13.765   1.00 56.58  ? 373  PHE   B CG   1 
ATOM   14656 C  CD1  . PHE   B  2  369 ? 30.564  -26.669 14.579   1.00 61.51  ? 373  PHE   B CD1  1 
ATOM   14657 C  CD2  . PHE   B  2  369 ? 31.755  -26.340 12.542   1.00 58.81  ? 373  PHE   B CD2  1 
ATOM   14658 C  CE1  . PHE   B  2  369 ? 29.618  -25.744 14.180   1.00 62.13  ? 373  PHE   B CE1  1 
ATOM   14659 C  CE2  . PHE   B  2  369 ? 30.815  -25.415 12.136   1.00 62.15  ? 373  PHE   B CE2  1 
ATOM   14660 C  CZ   . PHE   B  2  369 ? 29.744  -25.116 12.956   1.00 61.97  ? 373  PHE   B CZ   1 
ATOM   14661 H  H    . PHE   B  2  369 ? 34.933  -26.753 13.500   1.00 59.66  ? 373  PHE   B H    1 
ATOM   14662 H  HA   . PHE   B  2  369 ? 33.464  -26.926 15.778   1.00 62.59  ? 373  PHE   B HA   1 
ATOM   14663 H  HB2  . PHE   B  2  369 ? 33.021  -28.403 13.403   1.00 61.61  ? 373  PHE   B HB2  1 
ATOM   14664 H  HB3  . PHE   B  2  369 ? 32.217  -28.639 14.753   1.00 61.61  ? 373  PHE   B HB3  1 
ATOM   14665 H  HD1  . PHE   B  2  369 ? 30.476  -27.089 15.404   1.00 73.85  ? 373  PHE   B HD1  1 
ATOM   14666 H  HD2  . PHE   B  2  369 ? 32.474  -26.539 11.986   1.00 70.61  ? 373  PHE   B HD2  1 
ATOM   14667 H  HE1  . PHE   B  2  369 ? 28.898  -25.545 14.734   1.00 74.60  ? 373  PHE   B HE1  1 
ATOM   14668 H  HE2  . PHE   B  2  369 ? 30.902  -24.994 11.312   1.00 74.61  ? 373  PHE   B HE2  1 
ATOM   14669 H  HZ   . PHE   B  2  369 ? 29.109  -24.494 12.684   1.00 74.41  ? 373  PHE   B HZ   1 
ATOM   14670 N  N    . THR   B  2  370 ? 34.687  -28.793 16.754   1.00 56.30  ? 374  THR   B N    1 
ATOM   14671 C  CA   . THR   B  2  370 ? 35.367  -29.944 17.329   1.00 61.55  ? 374  THR   B CA   1 
ATOM   14672 C  C    . THR   B  2  370 ? 34.354  -30.725 18.150   1.00 63.42  ? 374  THR   B C    1 
ATOM   14673 O  O    . THR   B  2  370 ? 33.696  -30.161 19.030   1.00 63.92  ? 374  THR   B O    1 
ATOM   14674 C  CB   . THR   B  2  370 ? 36.555  -29.525 18.201   1.00 67.31  ? 374  THR   B CB   1 
ATOM   14675 O  OG1  . THR   B  2  370 ? 37.471  -28.739 17.427   1.00 68.96  ? 374  THR   B OG1  1 
ATOM   14676 C  CG2  . THR   B  2  370 ? 37.278  -30.751 18.737   1.00 73.02  ? 374  THR   B CG2  1 
ATOM   14677 H  H    . THR   B  2  370 ? 34.238  -28.340 17.332   1.00 67.60  ? 374  THR   B H    1 
ATOM   14678 H  HA   . THR   B  2  370 ? 35.712  -30.512 16.622   1.00 73.90  ? 374  THR   B HA   1 
ATOM   14679 H  HB   . THR   B  2  370 ? 36.233  -29.001 18.951   1.00 80.81  ? 374  THR   B HB   1 
ATOM   14680 H  HG1  . THR   B  2  370 ? 37.944  -29.240 16.947   1.00 82.79  ? 374  THR   B HG1  1 
ATOM   14681 H  HG21 . THR   B  2  370 ? 38.061  -30.480 19.243   1.00 87.67  ? 374  THR   B HG21 1 
ATOM   14682 H  HG22 . THR   B  2  370 ? 36.689  -31.257 19.318   1.00 87.67  ? 374  THR   B HG22 1 
ATOM   14683 H  HG23 . THR   B  2  370 ? 37.559  -31.318 18.002   1.00 87.67  ? 374  THR   B HG23 1 
ATOM   14684 N  N    . ALA   B  2  371 ? 34.225  -32.015 17.857   1.00 66.15  ? 375  ALA   B N    1 
ATOM   14685 C  CA   . ALA   B  2  371 ? 33.257  -32.878 18.517   1.00 65.02  ? 375  ALA   B CA   1 
ATOM   14686 C  C    . ALA   B  2  371 ? 33.942  -33.686 19.609   1.00 70.42  ? 375  ALA   B C    1 
ATOM   14687 O  O    . ALA   B  2  371 ? 35.040  -34.213 19.411   1.00 71.81  ? 375  ALA   B O    1 
ATOM   14688 C  CB   . ALA   B  2  371 ? 32.591  -33.817 17.511   1.00 62.93  ? 375  ALA   B CB   1 
ATOM   14689 H  H    . ALA   B  2  371 ? 34.698  -32.420 17.264   1.00 79.42  ? 375  ALA   B H    1 
ATOM   14690 H  HA   . ALA   B  2  371 ? 32.567  -32.334 18.928   1.00 78.06  ? 375  ALA   B HA   1 
ATOM   14691 H  HB1  . ALA   B  2  371 ? 31.932  -34.359 17.974   1.00 75.55  ? 375  ALA   B HB1  1 
ATOM   14692 H  HB2  . ALA   B  2  371 ? 32.159  -33.288 16.822   1.00 75.55  ? 375  ALA   B HB2  1 
ATOM   14693 H  HB3  . ALA   B  2  371 ? 33.268  -34.387 17.115   1.00 75.55  ? 375  ALA   B HB3  1 
ATOM   14694 N  N    . ILE   B  2  372 ? 33.287  -33.781 20.759   1.00 75.31  ? 376  ILE   B N    1 
ATOM   14695 C  CA   . ILE   B  2  372 ? 33.820  -34.488 21.921   1.00 78.87  ? 376  ILE   B CA   1 
ATOM   14696 C  C    . ILE   B  2  372 ? 32.819  -35.593 22.245   1.00 81.11  ? 376  ILE   B C    1 
ATOM   14697 O  O    . ILE   B  2  372 ? 31.834  -35.379 22.957   1.00 79.27  ? 376  ILE   B O    1 
ATOM   14698 C  CB   . ILE   B  2  372 ? 34.042  -33.562 23.119   1.00 77.11  ? 376  ILE   B CB   1 
ATOM   14699 C  CG1  . ILE   B  2  372 ? 34.769  -32.284 22.687   1.00 77.28  ? 376  ILE   B CG1  1 
ATOM   14700 C  CG2  . ILE   B  2  372 ? 34.839  -34.279 24.200   1.00 80.61  ? 376  ILE   B CG2  1 
ATOM   14701 C  CD1  . ILE   B  2  372 ? 34.772  -31.192 23.740   1.00 81.97  ? 376  ILE   B CD1  1 
ATOM   14702 H  H    . ILE   B  2  372 ? 32.511  -33.435 20.895   1.00 90.41  ? 376  ILE   B H    1 
ATOM   14703 H  HA   . ILE   B  2  372 ? 34.669  -34.897 21.691   1.00 94.68  ? 376  ILE   B HA   1 
ATOM   14704 H  HB   . ILE   B  2  372 ? 33.174  -33.316 23.477   1.00 92.56  ? 376  ILE   B HB   1 
ATOM   14705 H  HG12 . ILE   B  2  372 ? 35.693  -32.504 22.487   1.00 92.78  ? 376  ILE   B HG12 1 
ATOM   14706 H  HG13 . ILE   B  2  372 ? 34.334  -31.930 21.896   1.00 92.78  ? 376  ILE   B HG13 1 
ATOM   14707 H  HG21 . ILE   B  2  372 ? 34.944  -33.686 24.961   1.00 96.77  ? 376  ILE   B HG21 1 
ATOM   14708 H  HG22 . ILE   B  2  372 ? 34.361  -35.079 24.467   1.00 96.77  ? 376  ILE   B HG22 1 
ATOM   14709 H  HG23 . ILE   B  2  372 ? 35.710  -34.517 23.844   1.00 96.77  ? 376  ILE   B HG23 1 
ATOM   14710 H  HD11 . ILE   B  2  372 ? 35.219  -30.409 23.382   1.00 98.40  ? 376  ILE   B HD11 1 
ATOM   14711 H  HD12 . ILE   B  2  372 ? 33.856  -30.973 23.970   1.00 98.40  ? 376  ILE   B HD12 1 
ATOM   14712 H  HD13 . ILE   B  2  372 ? 35.243  -31.512 24.525   1.00 98.40  ? 376  ILE   B HD13 1 
ATOM   14713 N  N    . CYS   B  2  373 ? 33.066  -36.786 21.715   1.00 86.13  ? 377  CYS   B N    1 
ATOM   14714 C  CA   . CYS   B  2  373 ? 32.195  -37.933 21.917   1.00 94.37  ? 377  CYS   B CA   1 
ATOM   14715 C  C    . CYS   B  2  373 ? 32.752  -38.833 23.015   1.00 103.85 ? 377  CYS   B C    1 
ATOM   14716 O  O    . CYS   B  2  373 ? 33.852  -38.626 23.531   1.00 104.53 ? 377  CYS   B O    1 
ATOM   14717 C  CB   . CYS   B  2  373 ? 32.037  -38.724 20.614   1.00 95.52  ? 377  CYS   B CB   1 
ATOM   14718 S  SG   . CYS   B  2  373 ? 32.027  -37.714 19.108   1.00 88.41  ? 377  CYS   B SG   1 
ATOM   14719 H  H    . CYS   B  2  373 ? 33.750  -36.958 21.223   1.00 103.39 ? 377  CYS   B H    1 
ATOM   14720 H  HA   . CYS   B  2  373 ? 31.319  -37.620 22.191   1.00 113.28 ? 377  CYS   B HA   1 
ATOM   14721 H  HB2  . CYS   B  2  373 ? 32.776  -39.348 20.542   1.00 114.67 ? 377  CYS   B HB2  1 
ATOM   14722 H  HB3  . CYS   B  2  373 ? 31.197  -39.207 20.647   1.00 114.67 ? 377  CYS   B HB3  1 
ATOM   14723 N  N    . ASN   B  2  374 ? 31.966  -39.848 23.368   1.00 113.76 ? 378  ASN   B N    1 
ATOM   14724 C  CA   . ASN   B  2  374 ? 32.371  -40.866 24.334   1.00 127.40 ? 378  ASN   B CA   1 
ATOM   14725 C  C    . ASN   B  2  374 ? 32.936  -40.218 25.597   1.00 142.18 ? 378  ASN   B C    1 
ATOM   14726 O  O    . ASN   B  2  374 ? 34.073  -40.461 26.006   1.00 157.14 ? 378  ASN   B O    1 
ATOM   14727 C  CB   . ASN   B  2  374 ? 33.386  -41.825 23.707   1.00 129.09 ? 378  ASN   B CB   1 
ATOM   14728 C  CG   . ASN   B  2  374 ? 32.994  -42.250 22.305   1.00 123.89 ? 378  ASN   B CG   1 
ATOM   14729 O  OD1  . ASN   B  2  374 ? 31.858  -42.047 21.877   1.00 118.60 ? 378  ASN   B OD1  1 
ATOM   14730 N  ND2  . ASN   B  2  374 ? 33.936  -42.847 21.582   1.00 126.28 ? 378  ASN   B ND2  1 
ATOM   14731 H  H    . ASN   B  2  374 ? 31.175  -39.972 23.054   1.00 136.55 ? 378  ASN   B H    1 
ATOM   14732 H  HA   . ASN   B  2  374 ? 31.588  -41.377 24.592   1.00 152.91 ? 378  ASN   B HA   1 
ATOM   14733 H  HB2  . ASN   B  2  374 ? 34.249  -41.386 23.658   1.00 154.95 ? 378  ASN   B HB2  1 
ATOM   14734 H  HB3  . ASN   B  2  374 ? 33.450  -42.622 24.256   1.00 154.95 ? 378  ASN   B HB3  1 
ATOM   14735 H  HD21 . ASN   B  2  374 ? 33.762  -43.107 20.781   1.00 151.58 ? 378  ASN   B HD21 1 
ATOM   14736 H  HD22 . ASN   B  2  374 ? 34.718  -42.974 21.915   1.00 151.58 ? 378  ASN   B HD22 1 
ATOM   14737 N  N    . ASN   B  2  375 ? 32.111  -39.375 26.213   1.00 141.82 ? 379  ASN   B N    1 
ATOM   14738 C  CA   . ASN   B  2  375 ? 32.523  -38.570 27.370   1.00 147.16 ? 379  ASN   B CA   1 
ATOM   14739 C  C    . ASN   B  2  375 ? 33.692  -37.706 26.898   1.00 150.13 ? 379  ASN   B C    1 
ATOM   14740 O  O    . ASN   B  2  375 ? 33.576  -37.064 25.842   1.00 151.46 ? 379  ASN   B O    1 
ATOM   14741 C  CB   . ASN   B  2  375 ? 32.797  -39.490 28.555   1.00 152.74 ? 379  ASN   B CB   1 
ATOM   14742 C  CG   . ASN   B  2  375 ? 31.528  -40.118 29.105   1.00 154.22 ? 379  ASN   B CG   1 
ATOM   14743 O  OD1  . ASN   B  2  375 ? 30.438  -39.566 28.957   1.00 151.60 ? 379  ASN   B OD1  1 
ATOM   14744 N  ND2  . ASN   B  2  375 ? 31.663  -41.275 29.743   1.00 160.01 ? 379  ASN   B ND2  1 
ATOM   14745 H  H    . ASN   B  2  375 ? 31.294  -39.248 25.979   1.00 170.22 ? 379  ASN   B H    1 
ATOM   14746 H  HA   . ASN   B  2  375 ? 31.805  -37.971 27.628   1.00 176.63 ? 379  ASN   B HA   1 
ATOM   14747 H  HB2  . ASN   B  2  375 ? 33.389  -40.204 28.272   1.00 183.33 ? 379  ASN   B HB2  1 
ATOM   14748 H  HB3  . ASN   B  2  375 ? 33.212  -38.977 29.266   1.00 183.33 ? 379  ASN   B HB3  1 
ATOM   14749 H  HD21 . ASN   B  2  375 ? 30.972  -41.668 30.071   1.00 192.05 ? 379  ASN   B HD21 1 
ATOM   14750 H  HD22 . ASN   B  2  375 ? 32.441  -41.632 29.827   1.00 192.05 ? 379  ASN   B HD22 1 
ATOM   14751 N  N    . GLY   B  2  376 ? 34.810  -37.655 27.614   1.00 160.93 ? 380  GLY   B N    1 
ATOM   14752 C  CA   . GLY   B  2  376 ? 35.937  -36.833 27.225   1.00 165.21 ? 380  GLY   B CA   1 
ATOM   14753 C  C    . GLY   B  2  376 ? 37.033  -37.552 26.470   1.00 157.73 ? 380  GLY   B C    1 
ATOM   14754 O  O    . GLY   B  2  376 ? 38.086  -36.953 26.222   1.00 155.82 ? 380  GLY   B O    1 
ATOM   14755 H  H    . GLY   B  2  376 ? 34.937  -38.097 28.341   1.00 193.16 ? 380  GLY   B H    1 
ATOM   14756 H  HA2  . GLY   B  2  376 ? 35.614  -36.115 26.659   1.00 198.29 ? 380  GLY   B HA2  1 
ATOM   14757 H  HA3  . GLY   B  2  376 ? 36.332  -36.453 28.025   1.00 198.29 ? 380  GLY   B HA3  1 
ATOM   14758 N  N    . THR   B  2  377 ? 36.818  -38.808 26.073   1.00 136.59 ? 381  THR   B N    1 
ATOM   14759 C  CA   . THR   B  2  377 ? 37.915  -39.621 25.562   1.00 130.33 ? 381  THR   B CA   1 
ATOM   14760 C  C    . THR   B  2  377 ? 38.257  -39.296 24.111   1.00 125.36 ? 381  THR   B C    1 
ATOM   14761 O  O    . THR   B  2  377 ? 39.436  -39.304 23.738   1.00 130.68 ? 381  THR   B O    1 
ATOM   14762 C  CB   . THR   B  2  377 ? 37.572  -41.106 25.699   1.00 132.50 ? 381  THR   B CB   1 
ATOM   14763 O  OG1  . THR   B  2  377 ? 36.360  -41.390 24.988   1.00 128.96 ? 381  THR   B OG1  1 
ATOM   14764 C  CG2  . THR   B  2  377 ? 37.398  -41.481 27.166   1.00 136.33 ? 381  THR   B CG2  1 
ATOM   14765 H  H    . THR   B  2  377 ? 36.055  -39.205 26.090   1.00 163.95 ? 381  THR   B H    1 
ATOM   14766 H  HA   . THR   B  2  377 ? 38.702  -39.433 26.097   1.00 156.44 ? 381  THR   B HA   1 
ATOM   14767 H  HB   . THR   B  2  377 ? 38.293  -41.640 25.329   1.00 159.04 ? 381  THR   B HB   1 
ATOM   14768 H  HG1  . THR   B  2  377 ? 35.733  -41.525 25.531   1.00 154.79 ? 381  THR   B HG1  1 
ATOM   14769 H  HG21 . THR   B  2  377 ? 37.580  -42.426 27.291   1.00 163.63 ? 381  THR   B HG21 1 
ATOM   14770 H  HG22 . THR   B  2  377 ? 38.012  -40.968 27.714   1.00 163.63 ? 381  THR   B HG22 1 
ATOM   14771 H  HG23 . THR   B  2  377 ? 36.490  -41.295 27.451   1.00 163.63 ? 381  THR   B HG23 1 
ATOM   14772 N  N    . LEU   B  2  378 ? 37.260  -39.008 23.279   1.00 115.43 ? 382  LEU   B N    1 
ATOM   14773 C  CA   . LEU   B  2  378 ? 37.461  -38.864 21.842   1.00 108.98 ? 382  LEU   B CA   1 
ATOM   14774 C  C    . LEU   B  2  378 ? 37.286  -37.412 21.418   1.00 103.24 ? 382  LEU   B C    1 
ATOM   14775 O  O    . LEU   B  2  378 ? 36.316  -36.755 21.810   1.00 98.46  ? 382  LEU   B O    1 
ATOM   14776 C  CB   . LEU   B  2  378 ? 36.488  -39.754 21.063   1.00 105.49 ? 382  LEU   B CB   1 
ATOM   14777 C  CG   . LEU   B  2  378 ? 36.783  -39.869 19.566   1.00 107.56 ? 382  LEU   B CG   1 
ATOM   14778 C  CD1  . LEU   B  2  378 ? 38.076  -40.640 19.338   1.00 113.71 ? 382  LEU   B CD1  1 
ATOM   14779 C  CD2  . LEU   B  2  378 ? 35.624  -40.523 18.831   1.00 106.77 ? 382  LEU   B CD2  1 
ATOM   14780 H  H    . LEU   B  2  378 ? 36.445  -38.890 23.529   1.00 138.56 ? 382  LEU   B H    1 
ATOM   14781 H  HA   . LEU   B  2  378 ? 38.370  -39.127 21.630   1.00 130.81 ? 382  LEU   B HA   1 
ATOM   14782 H  HB2  . LEU   B  2  378 ? 36.522  -40.648 21.438   1.00 126.62 ? 382  LEU   B HB2  1 
ATOM   14783 H  HB3  . LEU   B  2  378 ? 35.595  -39.388 21.158   1.00 126.62 ? 382  LEU   B HB3  1 
ATOM   14784 H  HG   . LEU   B  2  378 ? 36.895  -38.978 19.199   1.00 129.11 ? 382  LEU   B HG   1 
ATOM   14785 H  HD11 . LEU   B  2  378 ? 38.189  -40.793 18.386   1.00 136.48 ? 382  LEU   B HD11 1 
ATOM   14786 H  HD12 . LEU   B  2  378 ? 38.819  -40.119 19.679   1.00 136.48 ? 382  LEU   B HD12 1 
ATOM   14787 H  HD13 . LEU   B  2  378 ? 38.025  -41.489 19.805   1.00 136.48 ? 382  LEU   B HD13 1 
ATOM   14788 H  HD21 . LEU   B  2  378 ? 35.818  -40.533 17.881   1.00 128.16 ? 382  LEU   B HD21 1 
ATOM   14789 H  HD22 . LEU   B  2  378 ? 35.515  -41.430 19.156   1.00 128.16 ? 382  LEU   B HD22 1 
ATOM   14790 H  HD23 . LEU   B  2  378 ? 34.816  -40.013 18.998   1.00 128.16 ? 382  LEU   B HD23 1 
ATOM   14791 N  N    . PHE   B  2  379 ? 38.224  -36.926 20.605   1.00 103.63 ? 383  PHE   B N    1 
ATOM   14792 C  CA   . PHE   B  2  379 ? 38.182  -35.588 20.031   1.00 102.57 ? 383  PHE   B CA   1 
ATOM   14793 C  C    . PHE   B  2  379 ? 38.263  -35.702 18.516   1.00 105.21 ? 383  PHE   B C    1 
ATOM   14794 O  O    . PHE   B  2  379 ? 39.181  -36.338 17.988   1.00 111.14 ? 383  PHE   B O    1 
ATOM   14795 C  CB   . PHE   B  2  379 ? 39.334  -34.725 20.551   1.00 102.65 ? 383  PHE   B CB   1 
ATOM   14796 C  CG   . PHE   B  2  379 ? 39.092  -34.140 21.912   1.00 97.74  ? 383  PHE   B CG   1 
ATOM   14797 C  CD1  . PHE   B  2  379 ? 39.265  -34.906 23.052   1.00 99.81  ? 383  PHE   B CD1  1 
ATOM   14798 C  CD2  . PHE   B  2  379 ? 38.701  -32.819 22.051   1.00 94.32  ? 383  PHE   B CD2  1 
ATOM   14799 C  CE1  . PHE   B  2  379 ? 39.045  -34.366 24.305   1.00 100.58 ? 383  PHE   B CE1  1 
ATOM   14800 C  CE2  . PHE   B  2  379 ? 38.481  -32.274 23.300   1.00 94.53  ? 383  PHE   B CE2  1 
ATOM   14801 C  CZ   . PHE   B  2  379 ? 38.653  -33.048 24.429   1.00 98.94  ? 383  PHE   B CZ   1 
ATOM   14802 H  H    . PHE   B  2  379 ? 38.919  -37.372 20.365   1.00 124.39 ? 383  PHE   B H    1 
ATOM   14803 H  HA   . PHE   B  2  379 ? 37.347  -35.158 20.271   1.00 123.12 ? 383  PHE   B HA   1 
ATOM   14804 H  HB2  . PHE   B  2  379 ? 40.134  -35.271 20.603   1.00 123.21 ? 383  PHE   B HB2  1 
ATOM   14805 H  HB3  . PHE   B  2  379 ? 39.474  -33.989 19.935   1.00 123.21 ? 383  PHE   B HB3  1 
ATOM   14806 H  HD1  . PHE   B  2  379 ? 39.531  -35.794 22.974   1.00 119.81 ? 383  PHE   B HD1  1 
ATOM   14807 H  HD2  . PHE   B  2  379 ? 38.586  -32.293 21.293   1.00 113.22 ? 383  PHE   B HD2  1 
ATOM   14808 H  HE1  . PHE   B  2  379 ? 39.161  -34.890 25.065   1.00 120.74 ? 383  PHE   B HE1  1 
ATOM   14809 H  HE2  . PHE   B  2  379 ? 38.217  -31.386 23.380   1.00 113.47 ? 383  PHE   B HE2  1 
ATOM   14810 H  HZ   . PHE   B  2  379 ? 38.506  -32.683 25.271   1.00 118.76 ? 383  PHE   B HZ   1 
ATOM   14811 N  N    . GLN   B  2  380 ? 37.308  -35.087 17.822   1.00 101.52 ? 384  GLN   B N    1 
ATOM   14812 C  CA   . GLN   B  2  380 ? 37.274  -35.117 16.367   1.00 98.94  ? 384  GLN   B CA   1 
ATOM   14813 C  C    . GLN   B  2  380 ? 36.854  -33.756 15.839   1.00 86.03  ? 384  GLN   B C    1 
ATOM   14814 O  O    . GLN   B  2  380 ? 36.017  -33.077 16.441   1.00 79.56  ? 384  GLN   B O    1 
ATOM   14815 C  CB   . GLN   B  2  380 ? 36.317  -36.196 15.851   1.00 103.64 ? 384  GLN   B CB   1 
ATOM   14816 C  CG   . GLN   B  2  380 ? 36.665  -37.596 16.317   1.00 112.77 ? 384  GLN   B CG   1 
ATOM   14817 C  CD   . GLN   B  2  380 ? 35.803  -38.654 15.662   1.00 121.58 ? 384  GLN   B CD   1 
ATOM   14818 O  OE1  . GLN   B  2  380 ? 34.623  -38.799 15.983   1.00 121.73 ? 384  GLN   B OE1  1 
ATOM   14819 N  NE2  . GLN   B  2  380 ? 36.387  -39.397 14.729   1.00 129.19 ? 384  GLN   B NE2  1 
ATOM   14820 H  H    . GLN   B  2  380 ? 36.664  -34.642 18.176   1.00 121.85 ? 384  GLN   B H    1 
ATOM   14821 H  HA   . GLN   B  2  380 ? 38.162  -35.310 16.028   1.00 118.76 ? 384  GLN   B HA   1 
ATOM   14822 H  HB2  . GLN   B  2  380 ? 35.421  -35.994 16.164   1.00 124.40 ? 384  GLN   B HB2  1 
ATOM   14823 H  HB3  . GLN   B  2  380 ? 36.338  -36.193 14.881   1.00 124.40 ? 384  GLN   B HB3  1 
ATOM   14824 H  HG2  . GLN   B  2  380 ? 37.591  -37.783 16.097   1.00 135.36 ? 384  GLN   B HG2  1 
ATOM   14825 H  HG3  . GLN   B  2  380 ? 36.534  -37.653 17.277   1.00 135.36 ? 384  GLN   B HG3  1 
ATOM   14826 H  HE21 . GLN   B  2  380 ? 37.212  -39.263 14.528   1.00 155.06 ? 384  GLN   B HE21 1 
ATOM   14827 H  HE22 . GLN   B  2  380 ? 35.940  -40.011 14.327   1.00 155.06 ? 384  GLN   B HE22 1 
ATOM   14828 N  N    . HIS   B  2  381 ? 37.435  -33.368 14.706   1.00 82.32  ? 385  HIS   B N    1 
ATOM   14829 C  CA   . HIS   B  2  381 ? 37.182  -32.057 14.111   1.00 78.15  ? 385  HIS   B CA   1 
ATOM   14830 C  C    . HIS   B  2  381 ? 36.052  -32.149 13.085   1.00 82.35  ? 385  HIS   B C    1 
ATOM   14831 O  O    . HIS   B  2  381 ? 36.201  -31.862 11.897   1.00 85.95  ? 385  HIS   B O    1 
ATOM   14832 C  CB   . HIS   B  2  381 ? 38.466  -31.510 13.506   1.00 75.46  ? 385  HIS   B CB   1 
ATOM   14833 C  CG   . HIS   B  2  381 ? 39.614  -31.514 14.465   1.00 72.57  ? 385  HIS   B CG   1 
ATOM   14834 N  ND1  . HIS   B  2  381 ? 39.533  -30.941 15.716   1.00 69.11  ? 385  HIS   B ND1  1 
ATOM   14835 C  CD2  . HIS   B  2  381 ? 40.857  -32.042 14.373   1.00 74.70  ? 385  HIS   B CD2  1 
ATOM   14836 C  CE1  . HIS   B  2  381 ? 40.680  -31.106 16.349   1.00 71.13  ? 385  HIS   B CE1  1 
ATOM   14837 N  NE2  . HIS   B  2  381 ? 41.501  -31.770 15.555   1.00 75.41  ? 385  HIS   B NE2  1 
ATOM   14838 H  H    . HIS   B  2  381 ? 37.986  -33.852 14.257   1.00 98.82  ? 385  HIS   B H    1 
ATOM   14839 H  HA   . HIS   B  2  381 ? 36.896  -31.440 14.803   1.00 93.82  ? 385  HIS   B HA   1 
ATOM   14840 H  HB2  . HIS   B  2  381 ? 38.712  -32.056 12.743   1.00 90.59  ? 385  HIS   B HB2  1 
ATOM   14841 H  HB3  . HIS   B  2  381 ? 38.315  -30.594 13.223   1.00 90.59  ? 385  HIS   B HB3  1 
ATOM   14842 H  HD2  . HIS   B  2  381 ? 41.208  -32.503 13.646   1.00 89.68  ? 385  HIS   B HD2  1 
ATOM   14843 H  HE1  . HIS   B  2  381 ? 40.877  -30.805 17.207   1.00 85.40  ? 385  HIS   B HE1  1 
ATOM   14844 H  HE2  . HIS   B  2  381 ? 42.309  -31.995 15.748   1.00 90.53  ? 385  HIS   B HE2  1 
ATOM   14845 N  N    . GLN   B  2  382 ? 34.898  -32.575 13.592   1.00 82.85  ? 386  GLN   B N    1 
ATOM   14846 C  CA   . GLN   B  2  382 ? 33.649  -32.607 12.854   1.00 80.25  ? 386  GLN   B CA   1 
ATOM   14847 C  C    . GLN   B  2  382 ? 32.597  -31.879 13.679   1.00 78.65  ? 386  GLN   B C    1 
ATOM   14848 O  O    . GLN   B  2  382 ? 32.882  -31.334 14.750   1.00 78.21  ? 386  GLN   B O    1 
ATOM   14849 C  CB   . GLN   B  2  382 ? 33.179  -34.040 12.572   1.00 79.83  ? 386  GLN   B CB   1 
ATOM   14850 C  CG   . GLN   B  2  382 ? 34.271  -35.057 12.298   1.00 87.67  ? 386  GLN   B CG   1 
ATOM   14851 C  CD   . GLN   B  2  382 ? 33.850  -36.455 12.709   1.00 94.03  ? 386  GLN   B CD   1 
ATOM   14852 O  OE1  . GLN   B  2  382 ? 33.288  -36.652 13.786   1.00 89.25  ? 386  GLN   B OE1  1 
ATOM   14853 N  NE2  . GLN   B  2  382 ? 34.109  -37.430 11.849   1.00 104.09 ? 386  GLN   B NE2  1 
ATOM   14854 H  H    . GLN   B  2  382 ? 34.815  -32.863 14.398   1.00 99.46  ? 386  GLN   B H    1 
ATOM   14855 H  HA   . GLN   B  2  382 ? 33.779  -32.160 12.003   1.00 96.34  ? 386  GLN   B HA   1 
ATOM   14856 H  HB2  . GLN   B  2  382 ? 32.683  -34.354 13.345   1.00 95.83  ? 386  GLN   B HB2  1 
ATOM   14857 H  HB3  . GLN   B  2  382 ? 32.601  -34.023 11.793   1.00 95.83  ? 386  GLN   B HB3  1 
ATOM   14858 H  HG2  . GLN   B  2  382 ? 34.469  -35.066 11.348   1.00 105.23 ? 386  GLN   B HG2  1 
ATOM   14859 H  HG3  . GLN   B  2  382 ? 35.065  -34.818 12.801   1.00 105.23 ? 386  GLN   B HG3  1 
ATOM   14860 H  HE21 . GLN   B  2  382 ? 34.498  -37.253 11.102   1.00 124.95 ? 386  GLN   B HE21 1 
ATOM   14861 H  HE22 . GLN   B  2  382 ? 33.889  -38.240 12.038   1.00 124.95 ? 386  GLN   B HE22 1 
ATOM   14862 N  N    . LYS   B  2  383 ? 31.369  -31.887 13.181   1.00 78.13  ? 387  LYS   B N    1 
ATOM   14863 C  CA   . LYS   B  2  383 ? 30.210  -31.408 13.920   1.00 79.20  ? 387  LYS   B CA   1 
ATOM   14864 C  C    . LYS   B  2  383 ? 29.238  -32.554 14.166   1.00 78.05  ? 387  LYS   B C    1 
ATOM   14865 O  O    . LYS   B  2  383 ? 28.020  -32.371 14.166   1.00 77.23  ? 387  LYS   B O    1 
ATOM   14866 C  CB   . LYS   B  2  383 ? 29.527  -30.261 13.179   1.00 80.14  ? 387  LYS   B CB   1 
ATOM   14867 C  CG   . LYS   B  2  383 ? 29.296  -30.531 11.700   1.00 84.77  ? 387  LYS   B CG   1 
ATOM   14868 C  CD   . LYS   B  2  383 ? 28.476  -29.430 11.039   1.00 91.82  ? 387  LYS   B CD   1 
ATOM   14869 C  CE   . LYS   B  2  383 ? 29.180  -28.084 11.102   1.00 103.20 ? 387  LYS   B CE   1 
ATOM   14870 N  NZ   . LYS   B  2  383 ? 28.827  -27.220 9.942    1.00 112.83 ? 387  LYS   B NZ   1 
ATOM   14871 H  H    . LYS   B  2  383 ? 31.176  -32.174 12.394   1.00 93.79  ? 387  LYS   B H    1 
ATOM   14872 H  HA   . LYS   B  2  383 ? 30.501  -31.066 14.780   1.00 95.08  ? 387  LYS   B HA   1 
ATOM   14873 H  HB2  . LYS   B  2  383 ? 28.663  -30.098 13.588   1.00 96.21  ? 387  LYS   B HB2  1 
ATOM   14874 H  HB3  . LYS   B  2  383 ? 30.083  -29.469 13.251   1.00 96.21  ? 387  LYS   B HB3  1 
ATOM   14875 H  HG2  . LYS   B  2  383 ? 30.152  -30.583 11.247   1.00 101.76 ? 387  LYS   B HG2  1 
ATOM   14876 H  HG3  . LYS   B  2  383 ? 28.815  -31.367 11.599   1.00 101.76 ? 387  LYS   B HG3  1 
ATOM   14877 H  HD2  . LYS   B  2  383 ? 28.333  -29.654 10.106   1.00 110.22 ? 387  LYS   B HD2  1 
ATOM   14878 H  HD3  . LYS   B  2  383 ? 27.624  -29.349 11.495   1.00 110.22 ? 387  LYS   B HD3  1 
ATOM   14879 H  HE2  . LYS   B  2  383 ? 28.917  -27.624 11.915   1.00 123.88 ? 387  LYS   B HE2  1 
ATOM   14880 H  HE3  . LYS   B  2  383 ? 30.140  -28.224 11.096   1.00 123.88 ? 387  LYS   B HE3  1 
ATOM   14881 H  HZ1  . LYS   B  2  383 ? 29.249  -26.439 10.004   1.00 135.44 ? 387  LYS   B HZ1  1 
ATOM   14882 H  HZ2  . LYS   B  2  383 ? 29.066  -27.617 9.182    1.00 135.44 ? 387  LYS   B HZ2  1 
ATOM   14883 H  HZ3  . LYS   B  2  383 ? 27.949  -27.073 9.927    1.00 135.44 ? 387  LYS   B HZ3  1 
ATOM   14884 N  N    . LYS   B  2  384 ? 29.771  -33.757 14.385   1.00 77.39  ? 388  LYS   B N    1 
ATOM   14885 C  CA   . LYS   B  2  384 ? 28.942  -34.950 14.485   1.00 73.64  ? 388  LYS   B CA   1 
ATOM   14886 C  C    . LYS   B  2  384 ? 29.587  -35.974 15.406   1.00 70.28  ? 388  LYS   B C    1 
ATOM   14887 O  O    . LYS   B  2  384 ? 30.789  -36.234 15.307   1.00 71.19  ? 388  LYS   B O    1 
ATOM   14888 C  CB   . LYS   B  2  384 ? 28.717  -35.561 13.095   1.00 78.74  ? 388  LYS   B CB   1 
ATOM   14889 C  CG   . LYS   B  2  384 ? 27.867  -36.821 13.081   1.00 82.23  ? 388  LYS   B CG   1 
ATOM   14890 C  CD   . LYS   B  2  384 ? 27.612  -37.275 11.651   1.00 87.60  ? 388  LYS   B CD   1 
ATOM   14891 C  CE   . LYS   B  2  384 ? 26.454  -38.252 11.564   1.00 91.63  ? 388  LYS   B CE   1 
ATOM   14892 N  NZ   . LYS   B  2  384 ? 26.000  -38.455 10.158   1.00 94.83  ? 388  LYS   B NZ   1 
ATOM   14893 H  H    . LYS   B  2  384 ? 30.613  -33.904 14.480   1.00 92.91  ? 388  LYS   B H    1 
ATOM   14894 H  HA   . LYS   B  2  384 ? 28.089  -34.708 14.878   1.00 88.40  ? 388  LYS   B HA   1 
ATOM   14895 H  HB2  . LYS   B  2  384 ? 28.272  -34.903 12.539   1.00 94.52  ? 388  LYS   B HB2  1 
ATOM   14896 H  HB3  . LYS   B  2  384 ? 29.580  -35.787 12.715   1.00 94.52  ? 388  LYS   B HB3  1 
ATOM   14897 H  HG2  . LYS   B  2  384 ? 28.330  -37.531 13.553   1.00 98.71  ? 388  LYS   B HG2  1 
ATOM   14898 H  HG3  . LYS   B  2  384 ? 27.013  -36.642 13.506   1.00 98.71  ? 388  LYS   B HG3  1 
ATOM   14899 H  HD2  . LYS   B  2  384 ? 27.399  -36.503 11.104   1.00 105.16 ? 388  LYS   B HD2  1 
ATOM   14900 H  HD3  . LYS   B  2  384 ? 28.406  -37.715 11.309   1.00 105.16 ? 388  LYS   B HD3  1 
ATOM   14901 H  HE2  . LYS   B  2  384 ? 26.733  -39.111 11.919   1.00 109.99 ? 388  LYS   B HE2  1 
ATOM   14902 H  HE3  . LYS   B  2  384 ? 25.706  -37.908 12.077   1.00 109.99 ? 388  LYS   B HE3  1 
ATOM   14903 H  HZ1  . LYS   B  2  384 ? 25.118  -38.570 10.137   1.00 113.83 ? 388  LYS   B HZ1  1 
ATOM   14904 H  HZ2  . LYS   B  2  384 ? 26.211  -37.745 9.665    1.00 113.83 ? 388  LYS   B HZ2  1 
ATOM   14905 H  HZ3  . LYS   B  2  384 ? 26.393  -39.174 9.812    1.00 113.83 ? 388  LYS   B HZ3  1 
ATOM   14906 N  N    . CYS   B  2  385 ? 28.779  -36.551 16.295   1.00 68.76  ? 389  CYS   B N    1 
ATOM   14907 C  CA   . CYS   B  2  385 ? 29.165  -37.690 17.118   1.00 70.95  ? 389  CYS   B CA   1 
ATOM   14908 C  C    . CYS   B  2  385 ? 28.265  -38.863 16.756   1.00 69.83  ? 389  CYS   B C    1 
ATOM   14909 O  O    . CYS   B  2  385 ? 27.037  -38.734 16.784   1.00 69.68  ? 389  CYS   B O    1 
ATOM   14910 C  CB   . CYS   B  2  385 ? 29.045  -37.378 18.613   1.00 74.33  ? 389  CYS   B CB   1 
ATOM   14911 S  SG   . CYS   B  2  385 ? 30.438  -36.463 19.316   1.00 82.31  ? 389  CYS   B SG   1 
ATOM   14912 H  H    . CYS   B  2  385 ? 27.974  -36.288 16.443   1.00 82.55  ? 389  CYS   B H    1 
ATOM   14913 H  HA   . CYS   B  2  385 ? 30.090  -37.925 16.940   1.00 85.17  ? 389  CYS   B HA   1 
ATOM   14914 H  HB2  . CYS   B  2  385 ? 28.247  -36.845 18.751   1.00 89.23  ? 389  CYS   B HB2  1 
ATOM   14915 H  HB3  . CYS   B  2  385 ? 28.973  -38.215 19.096   1.00 89.23  ? 389  CYS   B HB3  1 
ATOM   14916 N  N    . SER   B  2  386 ? 28.870  -39.996 16.421   1.00 69.14  ? 390  SER   B N    1 
ATOM   14917 C  CA   . SER   B  2  386 ? 28.145  -41.162 15.937   1.00 75.33  ? 390  SER   B CA   1 
ATOM   14918 C  C    . SER   B  2  386 ? 28.293  -42.321 16.917   1.00 81.03  ? 390  SER   B C    1 
ATOM   14919 O  O    . SER   B  2  386 ? 29.011  -42.238 17.916   1.00 86.79  ? 390  SER   B O    1 
ATOM   14920 C  CB   . SER   B  2  386 ? 28.642  -41.572 14.547   1.00 82.66  ? 390  SER   B CB   1 
ATOM   14921 O  OG   . SER   B  2  386 ? 28.395  -40.556 13.593   1.00 85.65  ? 390  SER   B OG   1 
ATOM   14922 H  H    . SER   B  2  386 ? 29.720  -40.115 16.467   1.00 83.00  ? 390  SER   B H    1 
ATOM   14923 H  HA   . SER   B  2  386 ? 27.204  -40.933 15.878   1.00 90.44  ? 390  SER   B HA   1 
ATOM   14924 H  HB2  . SER   B  2  386 ? 29.597  -41.736 14.591   1.00 99.22  ? 390  SER   B HB2  1 
ATOM   14925 H  HB3  . SER   B  2  386 ? 28.179  -42.379 14.273   1.00 99.22  ? 390  SER   B HB3  1 
ATOM   14926 H  HG   . SER   B  2  386 ? 28.657  -40.803 12.834   1.00 102.82 ? 390  SER   B HG   1 
ATOM   14927 N  N    . HIS   B  2  387 ? 27.591  -43.412 16.611   1.00 83.19  ? 391  HIS   B N    1 
ATOM   14928 C  CA   . HIS   B  2  387 ? 27.683  -44.655 17.372   1.00 80.57  ? 391  HIS   B CA   1 
ATOM   14929 C  C    . HIS   B  2  387 ? 27.502  -44.407 18.867   1.00 78.78  ? 391  HIS   B C    1 
ATOM   14930 O  O    . HIS   B  2  387 ? 28.307  -44.838 19.695   1.00 84.31  ? 391  HIS   B O    1 
ATOM   14931 C  CB   . HIS   B  2  387 ? 29.016  -45.358 17.106   1.00 81.35  ? 391  HIS   B CB   1 
ATOM   14932 C  CG   . HIS   B  2  387 ? 29.238  -45.725 15.673   1.00 87.22  ? 391  HIS   B CG   1 
ATOM   14933 N  ND1  . HIS   B  2  387 ? 29.785  -44.853 14.756   1.00 87.51  ? 391  HIS   B ND1  1 
ATOM   14934 C  CD2  . HIS   B  2  387 ? 28.996  -46.875 15.000   1.00 91.45  ? 391  HIS   B CD2  1 
ATOM   14935 C  CE1  . HIS   B  2  387 ? 29.867  -45.449 13.580   1.00 91.39  ? 391  HIS   B CE1  1 
ATOM   14936 N  NE2  . HIS   B  2  387 ? 29.395  -46.676 13.700   1.00 93.05  ? 391  HIS   B NE2  1 
ATOM   14937 H  H    . HIS   B  2  387 ? 27.042  -43.457 15.951   1.00 99.86  ? 391  HIS   B H    1 
ATOM   14938 H  HA   . HIS   B  2  387 ? 26.964  -45.237 17.080   1.00 96.72  ? 391  HIS   B HA   1 
ATOM   14939 H  HB2  . HIS   B  2  387 ? 29.737  -44.767 17.374   1.00 97.66  ? 391  HIS   B HB2  1 
ATOM   14940 H  HB3  . HIS   B  2  387 ? 29.046  -46.175 17.628   1.00 97.66  ? 391  HIS   B HB3  1 
ATOM   14941 H  HD2  . HIS   B  2  387 ? 28.629  -47.654 15.352   1.00 109.78 ? 391  HIS   B HD2  1 
ATOM   14942 H  HE1  . HIS   B  2  387 ? 30.201  -45.068 12.800   1.00 109.70 ? 391  HIS   B HE1  1 
ATOM   14943 H  HE2  . HIS   B  2  387 ? 29.344  -47.257 13.068   1.00 111.70 ? 391  HIS   B HE2  1 
ATOM   14944 N  N    . MET   B  2  388 ? 26.429  -43.704 19.215   1.00 67.95  ? 392  MET   B N    1 
ATOM   14945 C  CA   . MET   B  2  388 ? 26.134  -43.382 20.602   1.00 69.86  ? 392  MET   B CA   1 
ATOM   14946 C  C    . MET   B  2  388 ? 24.782  -43.957 21.002   1.00 73.30  ? 392  MET   B C    1 
ATOM   14947 O  O    . MET   B  2  388 ? 23.869  -44.082 20.179   1.00 72.85  ? 392  MET   B O    1 
ATOM   14948 C  CB   . MET   B  2  388 ? 26.155  -41.864 20.841   1.00 68.46  ? 392  MET   B CB   1 
ATOM   14949 C  CG   . MET   B  2  388 ? 25.353  -41.045 19.843   1.00 69.56  ? 392  MET   B CG   1 
ATOM   14950 S  SD   . MET   B  2  388 ? 25.641  -39.270 20.014   1.00 68.09  ? 392  MET   B SD   1 
ATOM   14951 C  CE   . MET   B  2  388 ? 25.340  -39.023 21.762   1.00 67.09  ? 392  MET   B CE   1 
ATOM   14952 H  H    . MET   B  2  388 ? 25.851  -43.399 18.656   1.00 81.58  ? 392  MET   B H    1 
ATOM   14953 H  HA   . MET   B  2  388 ? 26.813  -43.780 21.169   1.00 83.87  ? 392  MET   B HA   1 
ATOM   14954 H  HB2  . MET   B  2  388 ? 25.789  -41.687 21.722   1.00 82.19  ? 392  MET   B HB2  1 
ATOM   14955 H  HB3  . MET   B  2  388 ? 27.074  -41.559 20.795   1.00 82.19  ? 392  MET   B HB3  1 
ATOM   14956 H  HG2  . MET   B  2  388 ? 25.606  -41.305 18.943   1.00 83.50  ? 392  MET   B HG2  1 
ATOM   14957 H  HG3  . MET   B  2  388 ? 24.408  -41.211 19.983   1.00 83.50  ? 392  MET   B HG3  1 
ATOM   14958 H  HE1  . MET   B  2  388 ? 25.457  -38.083 21.973   1.00 80.55  ? 392  MET   B HE1  1 
ATOM   14959 H  HE2  . MET   B  2  388 ? 24.433  -39.298 21.968   1.00 80.55  ? 392  MET   B HE2  1 
ATOM   14960 H  HE3  . MET   B  2  388 ? 25.971  -39.557 22.270   1.00 80.55  ? 392  MET   B HE3  1 
ATOM   14961 N  N    . LYS   B  2  389 ? 24.671  -44.316 22.278   1.00 76.84  ? 393  LYS   B N    1 
ATOM   14962 C  CA   . LYS   B  2  389 ? 23.441  -44.858 22.835   1.00 79.87  ? 393  LYS   B CA   1 
ATOM   14963 C  C    . LYS   B  2  389 ? 22.554  -43.721 23.321   1.00 73.84  ? 393  LYS   B C    1 
ATOM   14964 O  O    . LYS   B  2  389 ? 23.033  -42.766 23.938   1.00 72.72  ? 393  LYS   B O    1 
ATOM   14965 C  CB   . LYS   B  2  389 ? 23.745  -45.815 23.991   1.00 87.71  ? 393  LYS   B CB   1 
ATOM   14966 C  CG   . LYS   B  2  389 ? 22.504  -46.374 24.686   1.00 93.96  ? 393  LYS   B CG   1 
ATOM   14967 C  CD   . LYS   B  2  389 ? 22.856  -47.247 25.886   1.00 101.48 ? 393  LYS   B CD   1 
ATOM   14968 C  CE   . LYS   B  2  389 ? 21.601  -47.814 26.541   1.00 104.78 ? 393  LYS   B CE   1 
ATOM   14969 N  NZ   . LYS   B  2  389 ? 21.897  -48.699 27.704   1.00 111.96 ? 393  LYS   B NZ   1 
ATOM   14970 H  H    . LYS   B  2  389 ? 25.309  -44.253 22.852   1.00 92.24  ? 393  LYS   B H    1 
ATOM   14971 H  HA   . LYS   B  2  389 ? 22.964  -45.355 22.153   1.00 95.88  ? 393  LYS   B HA   1 
ATOM   14972 H  HB2  . LYS   B  2  389 ? 24.251  -46.567 23.646   1.00 105.29 ? 393  LYS   B HB2  1 
ATOM   14973 H  HB3  . LYS   B  2  389 ? 24.266  -45.341 24.657   1.00 105.29 ? 393  LYS   B HB3  1 
ATOM   14974 H  HG2  . LYS   B  2  389 ? 21.956  -45.637 24.999   1.00 112.79 ? 393  LYS   B HG2  1 
ATOM   14975 H  HG3  . LYS   B  2  389 ? 22.003  -46.915 24.056   1.00 112.79 ? 393  LYS   B HG3  1 
ATOM   14976 H  HD2  . LYS   B  2  389 ? 23.411  -47.987 25.595   1.00 121.82 ? 393  LYS   B HD2  1 
ATOM   14977 H  HD3  . LYS   B  2  389 ? 23.331  -46.715 26.544   1.00 121.82 ? 393  LYS   B HD3  1 
ATOM   14978 H  HE2  . LYS   B  2  389 ? 21.051  -47.080 26.857   1.00 125.77 ? 393  LYS   B HE2  1 
ATOM   14979 H  HE3  . LYS   B  2  389 ? 21.112  -48.336 25.886   1.00 125.77 ? 393  LYS   B HE3  1 
ATOM   14980 H  HZ1  . LYS   B  2  389 ? 21.139  -49.019 28.044   1.00 134.38 ? 393  LYS   B HZ1  1 
ATOM   14981 H  HZ2  . LYS   B  2  389 ? 22.409  -49.380 27.446   1.00 134.38 ? 393  LYS   B HZ2  1 
ATOM   14982 H  HZ3  . LYS   B  2  389 ? 22.324  -48.239 28.335   1.00 134.38 ? 393  LYS   B HZ3  1 
ATOM   14983 N  N    . VAL   B  2  390 ? 21.254  -43.830 23.036   1.00 70.66  ? 394  VAL   B N    1 
ATOM   14984 C  CA   . VAL   B  2  390 ? 20.312  -42.809 23.476   1.00 69.27  ? 394  VAL   B CA   1 
ATOM   14985 C  C    . VAL   B  2  390 ? 20.496  -42.583 24.968   1.00 73.88  ? 394  VAL   B C    1 
ATOM   14986 O  O    . VAL   B  2  390 ? 20.576  -43.536 25.751   1.00 78.94  ? 394  VAL   B O    1 
ATOM   14987 C  CB   . VAL   B  2  390 ? 18.871  -43.223 23.131   1.00 69.85  ? 394  VAL   B CB   1 
ATOM   14988 C  CG1  . VAL   B  2  390 ? 17.885  -42.151 23.578   1.00 69.51  ? 394  VAL   B CG1  1 
ATOM   14989 C  CG2  . VAL   B  2  390 ? 18.736  -43.477 21.634   1.00 65.35  ? 394  VAL   B CG2  1 
ATOM   14990 H  H    . VAL   B  2  390 ? 20.900  -44.477 22.594   1.00 84.83  ? 394  VAL   B H    1 
ATOM   14991 H  HA   . VAL   B  2  390 ? 20.498  -41.978 23.013   1.00 83.17  ? 394  VAL   B HA   1 
ATOM   14992 H  HB   . VAL   B  2  390 ? 18.660  -44.045 23.602   1.00 83.86  ? 394  VAL   B HB   1 
ATOM   14993 H  HG11 . VAL   B  2  390 ? 16.987  -42.428 23.339   1.00 83.44  ? 394  VAL   B HG11 1 
ATOM   14994 H  HG12 . VAL   B  2  390 ? 17.952  -42.041 24.539   1.00 83.44  ? 394  VAL   B HG12 1 
ATOM   14995 H  HG13 . VAL   B  2  390 ? 18.103  -41.317 23.134   1.00 83.44  ? 394  VAL   B HG13 1 
ATOM   14996 H  HG21 . VAL   B  2  390 ? 17.814  -43.706 21.435   1.00 78.45  ? 394  VAL   B HG21 1 
ATOM   14997 H  HG22 . VAL   B  2  390 ? 18.988  -42.673 21.154   1.00 78.45  ? 394  VAL   B HG22 1 
ATOM   14998 H  HG23 . VAL   B  2  390 ? 19.320  -44.210 21.384   1.00 78.45  ? 394  VAL   B HG23 1 
ATOM   14999 N  N    . GLY   B  2  391 ? 20.570  -41.313 25.364   1.00 72.63  ? 395  GLY   B N    1 
ATOM   15000 C  CA   . GLY   B  2  391 ? 20.961  -40.920 26.694   1.00 74.12  ? 395  GLY   B CA   1 
ATOM   15001 C  C    . GLY   B  2  391 ? 22.398  -40.445 26.782   1.00 75.76  ? 395  GLY   B C    1 
ATOM   15002 O  O    . GLY   B  2  391 ? 22.719  -39.624 27.650   1.00 79.07  ? 395  GLY   B O    1 
ATOM   15003 H  H    . GLY   B  2  391 ? 20.390  -40.645 24.853   1.00 87.19  ? 395  GLY   B H    1 
ATOM   15004 H  HA2  . GLY   B  2  391 ? 20.385  -40.199 26.993   1.00 88.98  ? 395  GLY   B HA2  1 
ATOM   15005 H  HA3  . GLY   B  2  391 ? 20.856  -41.677 27.291   1.00 88.98  ? 395  GLY   B HA3  1 
ATOM   15006 N  N    . ASP   B  2  392 ? 23.266  -40.941 25.903   1.00 74.86  ? 396  ASP   B N    1 
ATOM   15007 C  CA   . ASP   B  2  392 ? 24.637  -40.456 25.853   1.00 72.19  ? 396  ASP   B CA   1 
ATOM   15008 C  C    . ASP   B  2  392 ? 24.660  -38.981 25.477   1.00 68.48  ? 396  ASP   B C    1 
ATOM   15009 O  O    . ASP   B  2  392 ? 23.757  -38.472 24.807   1.00 65.92  ? 396  ASP   B O    1 
ATOM   15010 C  CB   . ASP   B  2  392 ? 25.457  -41.262 24.845   1.00 72.00  ? 396  ASP   B CB   1 
ATOM   15011 C  CG   . ASP   B  2  392 ? 25.828  -42.638 25.359   1.00 75.29  ? 396  ASP   B CG   1 
ATOM   15012 O  OD1  . ASP   B  2  392 ? 25.643  -42.894 26.567   1.00 77.60  ? 396  ASP   B OD1  1 
ATOM   15013 O  OD2  . ASP   B  2  392 ? 26.305  -43.466 24.554   1.00 77.05  ? 396  ASP   B OD2  1 
ATOM   15014 H  H    . ASP   B  2  392 ? 23.085  -41.555 25.328   1.00 89.87  ? 396  ASP   B H    1 
ATOM   15015 H  HA   . ASP   B  2  392 ? 25.048  -40.562 26.725   1.00 86.67  ? 396  ASP   B HA   1 
ATOM   15016 H  HB2  . ASP   B  2  392 ? 24.938  -41.374 24.033   1.00 86.44  ? 396  ASP   B HB2  1 
ATOM   15017 H  HB3  . ASP   B  2  392 ? 26.278  -40.783 24.650   1.00 86.44  ? 396  ASP   B HB3  1 
ATOM   15018 N  N    . THR   B  2  393 ? 25.711  -38.294 25.910   1.00 68.77  ? 397  THR   B N    1 
ATOM   15019 C  CA   . THR   B  2  393 ? 25.865  -36.866 25.681   1.00 66.77  ? 397  THR   B CA   1 
ATOM   15020 C  C    . THR   B  2  393 ? 26.990  -36.626 24.685   1.00 62.62  ? 397  THR   B C    1 
ATOM   15021 O  O    . THR   B  2  393 ? 28.068  -37.219 24.801   1.00 62.61  ? 397  THR   B O    1 
ATOM   15022 C  CB   . THR   B  2  393 ? 26.158  -36.127 26.989   1.00 68.62  ? 397  THR   B CB   1 
ATOM   15023 O  OG1  . THR   B  2  393 ? 25.148  -36.442 27.955   1.00 71.26  ? 397  THR   B OG1  1 
ATOM   15024 C  CG2  . THR   B  2  393 ? 26.180  -34.622 26.758   1.00 68.61  ? 397  THR   B CG2  1 
ATOM   15025 H  H    . THR   B  2  393 ? 26.362  -38.644 26.350   1.00 82.56  ? 397  THR   B H    1 
ATOM   15026 H  HA   . THR   B  2  393 ? 25.044  -36.512 25.306   1.00 80.16  ? 397  THR   B HA   1 
ATOM   15027 H  HB   . THR   B  2  393 ? 27.026  -36.399 27.326   1.00 82.39  ? 397  THR   B HB   1 
ATOM   15028 H  HG1  . THR   B  2  393 ? 25.265  -35.989 28.652   1.00 85.54  ? 397  THR   B HG1  1 
ATOM   15029 H  HG21 . THR   B  2  393 ? 26.333  -34.160 27.598   1.00 82.37  ? 397  THR   B HG21 1 
ATOM   15030 H  HG22 . THR   B  2  393 ? 26.889  -34.392 26.138   1.00 82.37  ? 397  THR   B HG22 1 
ATOM   15031 H  HG23 . THR   B  2  393 ? 25.332  -34.331 26.389   1.00 82.37  ? 397  THR   B HG23 1 
ATOM   15032 N  N    . ALA   B  2  394 ? 26.731  -35.761 23.711   1.00 60.17  ? 398  ALA   B N    1 
ATOM   15033 C  CA   . ALA   B  2  394 ? 27.731  -35.313 22.754   1.00 61.75  ? 398  ALA   B CA   1 
ATOM   15034 C  C    . ALA   B  2  394 ? 28.035  -33.847 23.022   1.00 65.75  ? 398  ALA   B C    1 
ATOM   15035 O  O    . ALA   B  2  394 ? 27.117  -33.022 23.087   1.00 67.58  ? 398  ALA   B O    1 
ATOM   15036 C  CB   . ALA   B  2  394 ? 27.243  -35.501 21.316   1.00 59.56  ? 398  ALA   B CB   1 
ATOM   15037 H  H    . ALA   B  2  394 ? 25.957  -35.409 23.581   1.00 72.24  ? 398  ALA   B H    1 
ATOM   15038 H  HA   . ALA   B  2  394 ? 28.546  -35.828 22.860   1.00 74.14  ? 398  ALA   B HA   1 
ATOM   15039 H  HB1  . ALA   B  2  394 ? 27.932  -35.194 20.706   1.00 71.51  ? 398  ALA   B HB1  1 
ATOM   15040 H  HB2  . ALA   B  2  394 ? 27.063  -36.442 21.165   1.00 71.51  ? 398  ALA   B HB2  1 
ATOM   15041 H  HB3  . ALA   B  2  394 ? 26.433  -34.984 21.187   1.00 71.51  ? 398  ALA   B HB3  1 
ATOM   15042 N  N    . SER   B  2  395 ? 29.313  -33.529 23.190   1.00 68.00  ? 399  SER   B N    1 
ATOM   15043 C  CA   . SER   B  2  395 ? 29.756  -32.166 23.431   1.00 71.65  ? 399  SER   B CA   1 
ATOM   15044 C  C    . SER   B  2  395 ? 30.464  -31.633 22.194   1.00 69.93  ? 399  SER   B C    1 
ATOM   15045 O  O    . SER   B  2  395 ? 31.090  -32.386 21.442   1.00 73.28  ? 399  SER   B O    1 
ATOM   15046 C  CB   . SER   B  2  395 ? 30.694  -32.090 24.639   1.00 79.72  ? 399  SER   B CB   1 
ATOM   15047 O  OG   . SER   B  2  395 ? 30.100  -32.663 25.789   1.00 88.54  ? 399  SER   B OG   1 
ATOM   15048 H  H    . SER   B  2  395 ? 29.956  -34.101 23.168   1.00 81.63  ? 399  SER   B H    1 
ATOM   15049 H  HA   . SER   B  2  395 ? 28.988  -31.603 23.616   1.00 86.01  ? 399  SER   B HA   1 
ATOM   15050 H  HB2  . SER   B  2  395 ? 31.510  -32.572 24.434   1.00 95.70  ? 399  SER   B HB2  1 
ATOM   15051 H  HB3  . SER   B  2  395 ? 30.895  -31.158 24.821   1.00 95.70  ? 399  SER   B HB3  1 
ATOM   15052 H  HG   . SER   B  2  395 ? 29.548  -32.127 26.126   1.00 106.28 ? 399  SER   B HG   1 
ATOM   15053 N  N    . PHE   B  2  396 ? 30.359  -30.324 21.989   1.00 64.68  ? 400  PHE   B N    1 
ATOM   15054 C  CA   . PHE   B  2  396 ? 30.941  -29.678 20.824   1.00 63.08  ? 400  PHE   B CA   1 
ATOM   15055 C  C    . PHE   B  2  396 ? 31.630  -28.392 21.246   1.00 63.06  ? 400  PHE   B C    1 
ATOM   15056 O  O    . PHE   B  2  396 ? 31.162  -27.691 22.148   1.00 66.49  ? 400  PHE   B O    1 
ATOM   15057 C  CB   . PHE   B  2  396 ? 29.874  -29.377 19.764   1.00 60.85  ? 400  PHE   B CB   1 
ATOM   15058 C  CG   . PHE   B  2  396 ? 29.168  -30.599 19.256   1.00 59.67  ? 400  PHE   B CG   1 
ATOM   15059 C  CD1  . PHE   B  2  396 ? 29.690  -31.329 18.201   1.00 60.73  ? 400  PHE   B CD1  1 
ATOM   15060 C  CD2  . PHE   B  2  396 ? 27.983  -31.022 19.835   1.00 58.01  ? 400  PHE   B CD2  1 
ATOM   15061 C  CE1  . PHE   B  2  396 ? 29.044  -32.456 17.732   1.00 61.56  ? 400  PHE   B CE1  1 
ATOM   15062 C  CE2  . PHE   B  2  396 ? 27.331  -32.149 19.370   1.00 58.42  ? 400  PHE   B CE2  1 
ATOM   15063 C  CZ   . PHE   B  2  396 ? 27.863  -32.867 18.317   1.00 61.49  ? 400  PHE   B CZ   1 
ATOM   15064 H  H    . PHE   B  2  396 ? 29.949  -29.784 22.518   1.00 77.65  ? 400  PHE   B H    1 
ATOM   15065 H  HA   . PHE   B  2  396 ? 31.609  -30.261 20.431   1.00 75.74  ? 400  PHE   B HA   1 
ATOM   15066 H  HB2  . PHE   B  2  396 ? 29.207  -28.788 20.150   1.00 73.06  ? 400  PHE   B HB2  1 
ATOM   15067 H  HB3  . PHE   B  2  396 ? 30.300  -28.945 19.007   1.00 73.06  ? 400  PHE   B HB3  1 
ATOM   15068 H  HD1  . PHE   B  2  396 ? 30.486  -31.056 17.804   1.00 72.91  ? 400  PHE   B HD1  1 
ATOM   15069 H  HD2  . PHE   B  2  396 ? 27.621  -30.543 20.545   1.00 69.65  ? 400  PHE   B HD2  1 
ATOM   15070 H  HE1  . PHE   B  2  396 ? 29.404  -32.938 17.022   1.00 73.91  ? 400  PHE   B HE1  1 
ATOM   15071 H  HE2  . PHE   B  2  396 ? 26.536  -32.424 19.766   1.00 70.14  ? 400  PHE   B HE2  1 
ATOM   15072 H  HZ   . PHE   B  2  396 ? 27.426  -33.626 18.003   1.00 73.83  ? 400  PHE   B HZ   1 
ATOM   15073 N  N    . SER   B  2  397 ? 32.748  -28.096 20.591   1.00 60.00  ? 401  SER   B N    1 
ATOM   15074 C  CA   . SER   B  2  397 ? 33.475  -26.847 20.775   1.00 59.52  ? 401  SER   B CA   1 
ATOM   15075 C  C    . SER   B  2  397 ? 33.336  -26.053 19.481   1.00 55.96  ? 401  SER   B C    1 
ATOM   15076 O  O    . SER   B  2  397 ? 33.936  -26.410 18.461   1.00 62.39  ? 401  SER   B O    1 
ATOM   15077 C  CB   . SER   B  2  397 ? 34.941  -27.106 21.114   1.00 65.18  ? 401  SER   B CB   1 
ATOM   15078 O  OG   . SER   B  2  397 ? 35.079  -28.233 21.962   1.00 73.50  ? 401  SER   B OG   1 
ATOM   15079 H  H    . SER   B  2  397 ? 33.115  -28.621 20.017   1.00 72.04  ? 401  SER   B H    1 
ATOM   15080 H  HA   . SER   B  2  397 ? 33.089  -26.339 21.505   1.00 71.47  ? 401  SER   B HA   1 
ATOM   15081 H  HB2  . SER   B  2  397 ? 35.430  -27.268 20.292   1.00 78.25  ? 401  SER   B HB2  1 
ATOM   15082 H  HB3  . SER   B  2  397 ? 35.301  -26.327 21.566   1.00 78.25  ? 401  SER   B HB3  1 
ATOM   15083 H  HG   . SER   B  2  397 ? 35.341  -27.991 22.722   1.00 88.24  ? 401  SER   B HG   1 
ATOM   15084 N  N    . VAL   B  2  398 ? 32.538  -24.992 19.522   1.00 49.70  ? 402  VAL   B N    1 
ATOM   15085 C  CA   . VAL   B  2  398 ? 32.266  -24.152 18.363   1.00 54.58  ? 402  VAL   B CA   1 
ATOM   15086 C  C    . VAL   B  2  398 ? 33.009  -22.840 18.550   1.00 54.95  ? 402  VAL   B C    1 
ATOM   15087 O  O    . VAL   B  2  398 ? 32.843  -22.170 19.577   1.00 58.61  ? 402  VAL   B O    1 
ATOM   15088 C  CB   . VAL   B  2  398 ? 30.758  -23.895 18.190   1.00 58.41  ? 402  VAL   B CB   1 
ATOM   15089 C  CG1  . VAL   B  2  398 ? 30.493  -23.136 16.896   1.00 60.67  ? 402  VAL   B CG1  1 
ATOM   15090 C  CG2  . VAL   B  2  398 ? 29.980  -25.201 18.226   1.00 59.13  ? 402  VAL   B CG2  1 
ATOM   15091 H  H    . VAL   B  2  398 ? 32.130  -24.732 20.233   1.00 59.67  ? 402  VAL   B H    1 
ATOM   15092 H  HA   . VAL   B  2  398 ? 32.597  -24.592 17.565   1.00 65.53  ? 402  VAL   B HA   1 
ATOM   15093 H  HB   . VAL   B  2  398 ? 30.447  -23.348 18.927   1.00 70.12  ? 402  VAL   B HB   1 
ATOM   15094 H  HG11 . VAL   B  2  398 ? 29.538  -22.992 16.804   1.00 72.84  ? 402  VAL   B HG11 1 
ATOM   15095 H  HG12 . VAL   B  2  398 ? 30.955  -22.284 16.929   1.00 72.84  ? 402  VAL   B HG12 1 
ATOM   15096 H  HG13 . VAL   B  2  398 ? 30.822  -23.661 16.149   1.00 72.84  ? 402  VAL   B HG13 1 
ATOM   15097 H  HG21 . VAL   B  2  398 ? 29.032  -25.005 18.173   1.00 70.99  ? 402  VAL   B HG21 1 
ATOM   15098 H  HG22 . VAL   B  2  398 ? 30.248  -25.749 17.471   1.00 70.99  ? 402  VAL   B HG22 1 
ATOM   15099 H  HG23 . VAL   B  2  398 ? 30.177  -25.663 19.056   1.00 70.99  ? 402  VAL   B HG23 1 
ATOM   15100 N  N    . THR   B  2  399 ? 33.819  -22.469 17.566   1.00 50.87  ? 403  THR   B N    1 
ATOM   15101 C  CA   . THR   B  2  399 ? 34.524  -21.197 17.577   1.00 54.23  ? 403  THR   B CA   1 
ATOM   15102 C  C    . THR   B  2  399 ? 33.917  -20.281 16.533   1.00 57.70  ? 403  THR   B C    1 
ATOM   15103 O  O    . THR   B  2  399 ? 33.675  -20.700 15.396   1.00 59.28  ? 403  THR   B O    1 
ATOM   15104 C  CB   . THR   B  2  399 ? 36.010  -21.374 17.293   1.00 58.65  ? 403  THR   B CB   1 
ATOM   15105 O  OG1  . THR   B  2  399 ? 36.168  -21.914 15.983   1.00 72.73  ? 403  THR   B OG1  1 
ATOM   15106 C  CG2  . THR   B  2  399 ? 36.616  -22.280 18.324   1.00 52.02  ? 403  THR   B CG2  1 
ATOM   15107 H  H    . THR   B  2  399 ? 33.977  -22.947 16.869   1.00 61.08  ? 403  THR   B H    1 
ATOM   15108 H  HA   . THR   B  2  399 ? 34.428  -20.793 18.454   1.00 65.12  ? 403  THR   B HA   1 
ATOM   15109 H  HB   . THR   B  2  399 ? 36.477  -20.525 17.336   1.00 70.42  ? 403  THR   B HB   1 
ATOM   15110 H  HG1  . THR   B  2  399 ? 36.872  -21.617 15.633   1.00 87.32  ? 403  THR   B HG1  1 
ATOM   15111 H  HG21 . THR   B  2  399 ? 37.582  -22.287 18.232   1.00 62.46  ? 403  THR   B HG21 1 
ATOM   15112 H  HG22 . THR   B  2  399 ? 36.387  -21.970 19.214   1.00 62.46  ? 403  THR   B HG22 1 
ATOM   15113 H  HG23 . THR   B  2  399 ? 36.282  -23.183 18.209   1.00 62.46  ? 403  THR   B HG23 1 
ATOM   15114 N  N    . VAL   B  2  400 ? 33.686  -19.033 16.920   1.00 60.89  ? 404  VAL   B N    1 
ATOM   15115 C  CA   . VAL   B  2  400 ? 33.132  -18.014 16.043   1.00 60.28  ? 404  VAL   B CA   1 
ATOM   15116 C  C    . VAL   B  2  400 ? 34.151  -16.890 15.948   1.00 57.70  ? 404  VAL   B C    1 
ATOM   15117 O  O    . VAL   B  2  400 ? 34.698  -16.457 16.968   1.00 57.02  ? 404  VAL   B O    1 
ATOM   15118 C  CB   . VAL   B  2  400 ? 31.784  -17.490 16.570   1.00 62.29  ? 404  VAL   B CB   1 
ATOM   15119 C  CG1  . VAL   B  2  400 ? 31.091  -16.646 15.514   1.00 68.92  ? 404  VAL   B CG1  1 
ATOM   15120 C  CG2  . VAL   B  2  400 ? 30.897  -18.647 17.012   1.00 58.44  ? 404  VAL   B CG2  1 
ATOM   15121 H  H    . VAL   B  2  400 ? 33.849  -18.745 17.713   1.00 73.10  ? 404  VAL   B H    1 
ATOM   15122 H  HA   . VAL   B  2  400 ? 32.988  -18.382 15.157   1.00 72.37  ? 404  VAL   B HA   1 
ATOM   15123 H  HB   . VAL   B  2  400 ? 31.945  -16.927 17.343   1.00 74.79  ? 404  VAL   B HB   1 
ATOM   15124 H  HG11 . VAL   B  2  400 ? 30.210  -16.398 15.836   1.00 82.74  ? 404  VAL   B HG11 1 
ATOM   15125 H  HG12 . VAL   B  2  400 ? 31.619  -15.849 15.350   1.00 82.74  ? 404  VAL   B HG12 1 
ATOM   15126 H  HG13 . VAL   B  2  400 ? 31.011  -17.164 14.698   1.00 82.74  ? 404  VAL   B HG13 1 
ATOM   15127 H  HG21 . VAL   B  2  400 ? 30.072  -18.290 17.377   1.00 70.17  ? 404  VAL   B HG21 1 
ATOM   15128 H  HG22 . VAL   B  2  400 ? 30.705  -19.208 16.245   1.00 70.17  ? 404  VAL   B HG22 1 
ATOM   15129 H  HG23 . VAL   B  2  400 ? 31.363  -19.161 17.690   1.00 70.17  ? 404  VAL   B HG23 1 
ATOM   15130 N  N    . ASN   B  2  401 ? 34.414  -16.430 14.729   1.00 56.82  ? 405  ASN   B N    1 
ATOM   15131 C  CA   . ASN   B  2  401 ? 35.333  -15.326 14.499   1.00 63.43  ? 405  ASN   B CA   1 
ATOM   15132 C  C    . ASN   B  2  401 ? 34.693  -14.336 13.541   1.00 69.41  ? 405  ASN   B C    1 
ATOM   15133 O  O    . ASN   B  2  401 ? 34.119  -14.734 12.521   1.00 70.11  ? 405  ASN   B O    1 
ATOM   15134 C  CB   . ASN   B  2  401 ? 36.672  -15.818 13.940   1.00 65.54  ? 405  ASN   B CB   1 
ATOM   15135 C  CG   . ASN   B  2  401 ? 37.480  -14.706 13.300   1.00 67.51  ? 405  ASN   B CG   1 
ATOM   15136 O  OD1  . ASN   B  2  401 ? 37.858  -14.790 12.132   1.00 70.97  ? 405  ASN   B OD1  1 
ATOM   15137 N  ND2  . ASN   B  2  401 ? 37.736  -13.648 14.061   1.00 66.55  ? 405  ASN   B ND2  1 
ATOM   15138 H  H    . ASN   B  2  401 ? 34.065  -16.747 14.009   1.00 68.22  ? 405  ASN   B H    1 
ATOM   15139 H  HA   . ASN   B  2  401 ? 35.506  -14.871 15.338   1.00 76.15  ? 405  ASN   B HA   1 
ATOM   15140 H  HB2  . ASN   B  2  401 ? 37.198  -16.194 14.663   1.00 78.68  ? 405  ASN   B HB2  1 
ATOM   15141 H  HB3  . ASN   B  2  401 ? 36.504  -16.494 13.265   1.00 78.68  ? 405  ASN   B HB3  1 
ATOM   15142 H  HD21 . ASN   B  2  401 ? 38.191  -12.991 13.744   1.00 79.90  ? 405  ASN   B HD21 1 
ATOM   15143 H  HD22 . ASN   B  2  401 ? 37.447  -13.621 14.870   1.00 79.90  ? 405  ASN   B HD22 1 
ATOM   15144 N  N    . ILE   B  2  402 ? 34.784  -13.053 13.876   1.00 75.03  ? 406  ILE   B N    1 
ATOM   15145 C  CA   . ILE   B  2  402 ? 34.272  -11.976 13.035   1.00 79.92  ? 406  ILE   B CA   1 
ATOM   15146 C  C    . ILE   B  2  402 ? 35.471  -11.304 12.367   1.00 82.91  ? 406  ILE   B C    1 
ATOM   15147 O  O    . ILE   B  2  402 ? 36.296  -10.695 13.067   1.00 83.92  ? 406  ILE   B O    1 
ATOM   15148 C  CB   . ILE   B  2  402 ? 33.433  -10.978 13.850   1.00 82.95  ? 406  ILE   B CB   1 
ATOM   15149 C  CG1  . ILE   B  2  402 ? 32.753  -9.968  12.922   1.00 86.59  ? 406  ILE   B CG1  1 
ATOM   15150 C  CG2  . ILE   B  2  402 ? 34.274  -10.277 14.917   1.00 86.14  ? 406  ILE   B CG2  1 
ATOM   15151 C  CD1  . ILE   B  2  402 ? 31.595  -10.550 12.131   1.00 87.36  ? 406  ILE   B CD1  1 
ATOM   15152 H  H    . ILE   B  2  402 ? 35.149  -12.775 14.604   1.00 90.07  ? 406  ILE   B H    1 
ATOM   15153 H  HA   . ILE   B  2  402 ? 33.705  -12.341 12.338   1.00 95.94  ? 406  ILE   B HA   1 
ATOM   15154 H  HB   . ILE   B  2  402 ? 32.743  -11.479 14.312   1.00 99.58  ? 406  ILE   B HB   1 
ATOM   15155 H  HG12 . ILE   B  2  402 ? 32.407  -9.236  13.457   1.00 103.95 ? 406  ILE   B HG12 1 
ATOM   15156 H  HG13 . ILE   B  2  402 ? 33.407  -9.635  12.288   1.00 103.95 ? 406  ILE   B HG13 1 
ATOM   15157 H  HG21 . ILE   B  2  402 ? 33.811  -10.330 15.769   1.00 103.40 ? 406  ILE   B HG21 1 
ATOM   15158 H  HG22 . ILE   B  2  402 ? 35.135  -10.717 14.981   1.00 103.40 ? 406  ILE   B HG22 1 
ATOM   15159 H  HG23 . ILE   B  2  402 ? 34.394  -9.348  14.664   1.00 103.40 ? 406  ILE   B HG23 1 
ATOM   15160 H  HD11 . ILE   B  2  402 ? 31.587  -10.153 11.246   1.00 104.87 ? 406  ILE   B HD11 1 
ATOM   15161 H  HD12 . ILE   B  2  402 ? 31.712  -11.511 12.062   1.00 104.87 ? 406  ILE   B HD12 1 
ATOM   15162 H  HD13 . ILE   B  2  402 ? 30.766  -10.350 12.592   1.00 104.87 ? 406  ILE   B HD13 1 
ATOM   15163 N  N    . PRO   B  2  403 ? 35.628  -11.414 11.044   1.00 88.59  ? 407  PRO   B N    1 
ATOM   15164 C  CA   . PRO   B  2  403 ? 36.838  -10.850 10.411   1.00 93.51  ? 407  PRO   B CA   1 
ATOM   15165 C  C    . PRO   B  2  403 ? 36.983  -9.345  10.580   1.00 102.20 ? 407  PRO   B C    1 
ATOM   15166 O  O    . PRO   B  2  403 ? 38.075  -8.862  10.904   1.00 105.47 ? 407  PRO   B O    1 
ATOM   15167 C  CB   . PRO   B  2  403 ? 36.673  -11.241 8.934    1.00 92.61  ? 407  PRO   B CB   1 
ATOM   15168 C  CG   . PRO   B  2  403 ? 35.731  -12.386 8.920    1.00 91.86  ? 407  PRO   B CG   1 
ATOM   15169 C  CD   . PRO   B  2  403 ? 34.874  -12.301 10.140   1.00 89.31  ? 407  PRO   B CD   1 
ATOM   15170 H  HA   . PRO   B  2  403 ? 37.618  -11.288 10.784   1.00 112.25 ? 407  PRO   B HA   1 
ATOM   15171 H  HB2  . PRO   B  2  403 ? 36.310  -10.491 8.436    1.00 111.17 ? 407  PRO   B HB2  1 
ATOM   15172 H  HB3  . PRO   B  2  403 ? 37.533  -11.498 8.566    1.00 111.17 ? 407  PRO   B HB3  1 
ATOM   15173 H  HG2  . PRO   B  2  403 ? 35.182  -12.337 8.122    1.00 110.27 ? 407  PRO   B HG2  1 
ATOM   15174 H  HG3  . PRO   B  2  403 ? 36.237  -13.214 8.924    1.00 110.27 ? 407  PRO   B HG3  1 
ATOM   15175 H  HD2  . PRO   B  2  403 ? 34.010  -11.917 9.925    1.00 107.21 ? 407  PRO   B HD2  1 
ATOM   15176 H  HD3  . PRO   B  2  403 ? 34.758  -13.178 10.539   1.00 107.21 ? 407  PRO   B HD3  1 
ATOM   15177 N  N    . HIS   B  2  404 ? 35.913  -8.587  10.353   1.00 110.06 ? 408  HIS   B N    1 
ATOM   15178 C  CA   . HIS   B  2  404 ? 35.944  -7.132  10.395   1.00 114.90 ? 408  HIS   B CA   1 
ATOM   15179 C  C    . HIS   B  2  404 ? 34.859  -6.648  11.347   1.00 114.50 ? 408  HIS   B C    1 
ATOM   15180 O  O    . HIS   B  2  404 ? 33.921  -7.382  11.666   1.00 111.77 ? 408  HIS   B O    1 
ATOM   15181 C  CB   . HIS   B  2  404 ? 35.732  -6.531  8.995    1.00 121.07 ? 408  HIS   B CB   1 
ATOM   15182 C  CG   . HIS   B  2  404 ? 36.700  -7.033  7.967    1.00 130.71 ? 408  HIS   B CG   1 
ATOM   15183 N  ND1  . HIS   B  2  404 ? 36.295  -7.631  6.793    1.00 133.21 ? 408  HIS   B ND1  1 
ATOM   15184 C  CD2  . HIS   B  2  404 ? 38.053  -7.020  7.935    1.00 132.84 ? 408  HIS   B CD2  1 
ATOM   15185 C  CE1  . HIS   B  2  404 ? 37.358  -7.969  6.084    1.00 136.37 ? 408  HIS   B CE1  1 
ATOM   15186 N  NE2  . HIS   B  2  404 ? 38.437  -7.609  6.754    1.00 135.57 ? 408  HIS   B NE2  1 
ATOM   15187 H  H    . HIS   B  2  404 ? 35.135  -8.904  10.168   1.00 132.11 ? 408  HIS   B H    1 
ATOM   15188 H  HA   . HIS   B  2  404 ? 36.802  -6.823  10.726   1.00 137.91 ? 408  HIS   B HA   1 
ATOM   15189 H  HB2  . HIS   B  2  404 ? 34.838  -6.754  8.693    1.00 145.32 ? 408  HIS   B HB2  1 
ATOM   15190 H  HB3  . HIS   B  2  404 ? 35.833  -5.568  9.051    1.00 145.32 ? 408  HIS   B HB3  1 
ATOM   15191 H  HD2  . HIS   B  2  404 ? 38.618  -6.677  8.590    1.00 159.44 ? 408  HIS   B HD2  1 
ATOM   15192 H  HE1  . HIS   B  2  404 ? 37.347  -8.388  5.254    1.00 163.68 ? 408  HIS   B HE1  1 
ATOM   15193 H  HE2  . HIS   B  2  404 ? 39.249  -7.724  6.494    1.00 162.72 ? 408  HIS   B HE2  1 
ATOM   15194 N  N    . CYS   B  2  405 ? 34.983  -5.406  11.810   1.00 114.78 ? 409  CYS   B N    1 
ATOM   15195 C  CA   . CYS   B  2  405 ? 33.946  -4.876  12.684   1.00 115.44 ? 409  CYS   B CA   1 
ATOM   15196 C  C    . CYS   B  2  405 ? 32.674  -4.606  11.888   1.00 114.99 ? 409  CYS   B C    1 
ATOM   15197 O  O    . CYS   B  2  405 ? 32.713  -4.286  10.697   1.00 114.27 ? 409  CYS   B O    1 
ATOM   15198 C  CB   . CYS   B  2  405 ? 34.390  -3.595  13.389   1.00 120.13 ? 409  CYS   B CB   1 
ATOM   15199 S  SG   . CYS   B  2  405 ? 33.116  -3.029  14.557   1.00 125.28 ? 409  CYS   B SG   1 
ATOM   15200 H  H    . CYS   B  2  405 ? 35.634  -4.871  11.638   1.00 137.77 ? 409  CYS   B H    1 
ATOM   15201 H  HA   . CYS   B  2  405 ? 33.761  -5.532  13.375   1.00 138.56 ? 409  CYS   B HA   1 
ATOM   15202 H  HB2  . CYS   B  2  405 ? 35.208  -3.763  13.881   1.00 144.19 ? 409  CYS   B HB2  1 
ATOM   15203 H  HB3  . CYS   B  2  405 ? 34.536  -2.898  12.730   1.00 144.19 ? 409  CYS   B HB3  1 
ATOM   15204 N  N    . GLU   B  2  406 ? 31.537  -4.740  12.565   1.00 115.49 ? 410  GLU   B N    1 
ATOM   15205 C  CA   . GLU   B  2  406 ? 30.230  -4.576  11.949   1.00 117.91 ? 410  GLU   B CA   1 
ATOM   15206 C  C    . GLU   B  2  406 ? 29.359  -3.702  12.839   1.00 121.05 ? 410  GLU   B C    1 
ATOM   15207 O  O    . GLU   B  2  406 ? 29.611  -3.554  14.037   1.00 123.85 ? 410  GLU   B O    1 
ATOM   15208 C  CB   . GLU   B  2  406 ? 29.552  -5.931  11.717   1.00 113.84 ? 410  GLU   B CB   1 
ATOM   15209 C  CG   . GLU   B  2  406 ? 30.364  -6.885  10.859   1.00 111.30 ? 410  GLU   B CG   1 
ATOM   15210 C  CD   . GLU   B  2  406 ? 29.683  -8.226  10.678   1.00 108.46 ? 410  GLU   B CD   1 
ATOM   15211 O  OE1  . GLU   B  2  406 ? 28.853  -8.592  11.536   1.00 108.27 ? 410  GLU   B OE1  1 
ATOM   15212 O  OE2  . GLU   B  2  406 ? 29.974  -8.912  9.675    1.00 109.60 ? 410  GLU   B OE2  1 
ATOM   15213 H  H    . GLU   B  2  406 ? 31.499  -4.931  13.402   1.00 138.62 ? 410  GLU   B H    1 
ATOM   15214 H  HA   . GLU   B  2  406 ? 30.327  -4.133  11.092   1.00 141.52 ? 410  GLU   B HA   1 
ATOM   15215 H  HB2  . GLU   B  2  406 ? 29.406  -6.358  12.575   1.00 136.65 ? 410  GLU   B HB2  1 
ATOM   15216 H  HB3  . GLU   B  2  406 ? 28.704  -5.782  11.271   1.00 136.65 ? 410  GLU   B HB3  1 
ATOM   15217 H  HG2  . GLU   B  2  406 ? 30.492  -6.491  9.982    1.00 133.60 ? 410  GLU   B HG2  1 
ATOM   15218 H  HG3  . GLU   B  2  406 ? 31.223  -7.039  11.282   1.00 133.60 ? 410  GLU   B HG3  1 
ATOM   15219 N  N    . ARG   B  2  407 ? 28.320  -3.122  12.238   1.00 122.96 ? 411  ARG   B N    1 
ATOM   15220 C  CA   . ARG   B  2  407 ? 27.416  -2.237  12.959   1.00 122.59 ? 411  ARG   B CA   1 
ATOM   15221 C  C    . ARG   B  2  407 ? 26.134  -2.918  13.422   1.00 119.77 ? 411  ARG   B C    1 
ATOM   15222 O  O    . ARG   B  2  407 ? 25.350  -2.288  14.139   1.00 119.75 ? 411  ARG   B O    1 
ATOM   15223 C  CB   . ARG   B  2  407 ? 27.049  -1.026  12.090   1.00 128.97 ? 411  ARG   B CB   1 
ATOM   15224 C  CG   . ARG   B  2  407 ? 28.211  -0.081  11.821   1.00 135.44 ? 411  ARG   B CG   1 
ATOM   15225 C  CD   . ARG   B  2  407 ? 27.787  1.141   11.011   1.00 145.87 ? 411  ARG   B CD   1 
ATOM   15226 N  NE   . ARG   B  2  407 ? 28.927  2.002   10.702   1.00 150.98 ? 411  ARG   B NE   1 
ATOM   15227 C  CZ   . ARG   B  2  407 ? 28.875  3.075   9.918    1.00 158.50 ? 411  ARG   B CZ   1 
ATOM   15228 N  NH1  . ARG   B  2  407 ? 29.972  3.788   9.702    1.00 161.54 ? 411  ARG   B NH1  1 
ATOM   15229 N  NH2  . ARG   B  2  407 ? 27.734  3.436   9.345    1.00 162.57 ? 411  ARG   B NH2  1 
ATOM   15230 H  H    . ARG   B  2  407 ? 28.120  -3.228  11.408   1.00 147.59 ? 411  ARG   B H    1 
ATOM   15231 H  HA   . ARG   B  2  407 ? 27.880  -1.915  13.748   1.00 147.15 ? 411  ARG   B HA   1 
ATOM   15232 H  HB2  . ARG   B  2  407 ? 26.724  -1.345  11.233   1.00 154.81 ? 411  ARG   B HB2  1 
ATOM   15233 H  HB3  . ARG   B  2  407 ? 26.355  -0.519  12.540   1.00 154.81 ? 411  ARG   B HB3  1 
ATOM   15234 H  HG2  . ARG   B  2  407 ? 28.572  0.228   12.666   1.00 162.56 ? 411  ARG   B HG2  1 
ATOM   15235 H  HG3  . ARG   B  2  407 ? 28.895  -0.552  11.319   1.00 162.56 ? 411  ARG   B HG3  1 
ATOM   15236 H  HD2  . ARG   B  2  407 ? 27.389  0.851   10.175   1.00 175.07 ? 411  ARG   B HD2  1 
ATOM   15237 H  HD3  . ARG   B  2  407 ? 27.144  1.658   11.522   1.00 175.07 ? 411  ARG   B HD3  1 
ATOM   15238 H  HE   . ARG   B  2  407 ? 29.686  1.800   11.053   1.00 181.21 ? 411  ARG   B HE   1 
ATOM   15239 H  HH11 . ARG   B  2  407 ? 30.715  3.557   10.069   1.00 193.88 ? 411  ARG   B HH11 1 
ATOM   15240 H  HH12 . ARG   B  2  407 ? 29.941  4.482   9.195    1.00 193.88 ? 411  ARG   B HH12 1 
ATOM   15241 H  HH21 . ARG   B  2  407 ? 27.021  2.975   9.480    1.00 195.12 ? 411  ARG   B HH21 1 
ATOM   15242 H  HH22 . ARG   B  2  407 ? 27.708  4.131   8.839    1.00 195.12 ? 411  ARG   B HH22 1 
ATOM   15243 N  N    . ARG   B  2  408 ? 25.897  -4.175  13.046   1.00 117.82 ? 412  ARG   B N    1 
ATOM   15244 C  CA   . ARG   B  2  408 ? 24.660  -4.856  13.400   1.00 118.59 ? 412  ARG   B CA   1 
ATOM   15245 C  C    . ARG   B  2  408 ? 24.949  -6.209  14.031   1.00 107.31 ? 412  ARG   B C    1 
ATOM   15246 O  O    . ARG   B  2  408 ? 25.880  -6.913  13.627   1.00 102.38 ? 412  ARG   B O    1 
ATOM   15247 C  CB   . ARG   B  2  408 ? 23.751  -5.037  12.176   1.00 126.96 ? 412  ARG   B CB   1 
ATOM   15248 C  CG   . ARG   B  2  408 ? 23.195  -3.725  11.638   1.00 136.33 ? 412  ARG   B CG   1 
ATOM   15249 C  CD   . ARG   B  2  408 ? 21.833  -3.892  10.976   1.00 142.88 ? 412  ARG   B CD   1 
ATOM   15250 N  NE   . ARG   B  2  408 ? 21.854  -3.528  9.561    1.00 151.85 ? 412  ARG   B NE   1 
ATOM   15251 C  CZ   . ARG   B  2  408 ? 20.798  -3.087  8.881    1.00 164.01 ? 412  ARG   B CZ   1 
ATOM   15252 N  NH1  . ARG   B  2  408 ? 20.918  -2.787  7.595    1.00 168.00 ? 412  ARG   B NH1  1 
ATOM   15253 N  NH2  . ARG   B  2  408 ? 19.626  -2.931  9.483    1.00 170.68 ? 412  ARG   B NH2  1 
ATOM   15254 H  H    . ARG   B  2  408 ? 26.442  -4.652  12.583   1.00 141.42 ? 412  ARG   B H    1 
ATOM   15255 H  HA   . ARG   B  2  408 ? 24.191  -4.322  14.061   1.00 142.35 ? 412  ARG   B HA   1 
ATOM   15256 H  HB2  . ARG   B  2  408 ? 24.261  -5.457  11.466   1.00 152.39 ? 412  ARG   B HB2  1 
ATOM   15257 H  HB3  . ARG   B  2  408 ? 23.000  -5.599  12.424   1.00 152.39 ? 412  ARG   B HB3  1 
ATOM   15258 H  HG2  . ARG   B  2  408 ? 23.097  -3.097  12.372   1.00 163.63 ? 412  ARG   B HG2  1 
ATOM   15259 H  HG3  . ARG   B  2  408 ? 23.808  -3.368  10.977   1.00 163.63 ? 412  ARG   B HG3  1 
ATOM   15260 H  HD2  . ARG   B  2  408 ? 21.559  -4.820  11.044   1.00 171.50 ? 412  ARG   B HD2  1 
ATOM   15261 H  HD3  . ARG   B  2  408 ? 21.189  -3.322  11.425   1.00 171.50 ? 412  ARG   B HD3  1 
ATOM   15262 H  HE   . ARG   B  2  408 ? 22.599  -3.603  9.139    1.00 182.26 ? 412  ARG   B HE   1 
ATOM   15263 H  HH11 . ARG   B  2  408 ? 21.677  -2.877  7.202    1.00 201.64 ? 412  ARG   B HH11 1 
ATOM   15264 H  HH12 . ARG   B  2  408 ? 20.237  -2.502  7.155    1.00 201.64 ? 412  ARG   B HH12 1 
ATOM   15265 H  HH21 . ARG   B  2  408 ? 19.544  -3.116  10.319   1.00 204.85 ? 412  ARG   B HH21 1 
ATOM   15266 H  HH22 . ARG   B  2  408 ? 18.948  -2.646  9.038    1.00 204.85 ? 412  ARG   B HH22 1 
ATOM   15267 N  N    . SER   B  2  409 ? 24.140  -6.560  15.026   1.00 100.23 ? 413  SER   B N    1 
ATOM   15268 C  CA   . SER   B  2  409 ? 24.235  -7.853  15.680   1.00 93.55  ? 413  SER   B CA   1 
ATOM   15269 C  C    . SER   B  2  409 ? 23.659  -8.944  14.782   1.00 89.15  ? 413  SER   B C    1 
ATOM   15270 O  O    . SER   B  2  409 ? 22.834  -8.691  13.900   1.00 93.94  ? 413  SER   B O    1 
ATOM   15271 C  CB   . SER   B  2  409 ? 23.491  -7.833  17.014   1.00 94.46  ? 413  SER   B CB   1 
ATOM   15272 O  OG   . SER   B  2  409 ? 23.661  -6.592  17.676   1.00 94.71  ? 413  SER   B OG   1 
ATOM   15273 H  H    . SER   B  2  409 ? 23.518  -6.058  15.344   1.00 120.31 ? 413  SER   B H    1 
ATOM   15274 H  HA   . SER   B  2  409 ? 25.167  -8.059  15.855   1.00 112.30 ? 413  SER   B HA   1 
ATOM   15275 H  HB2  . SER   B  2  409 ? 22.545  -7.975  16.849   1.00 113.39 ? 413  SER   B HB2  1 
ATOM   15276 H  HB3  . SER   B  2  409 ? 23.838  -8.541  17.579   1.00 113.39 ? 413  SER   B HB3  1 
ATOM   15277 H  HG   . SER   B  2  409 ? 24.220  -6.672  18.298   1.00 113.69 ? 413  SER   B HG   1 
ATOM   15278 N  N    . ARG   B  2  410 ? 24.102  -10.175 15.021   1.00 81.41  ? 414  ARG   B N    1 
ATOM   15279 C  CA   . ARG   B  2  410 ? 23.652  -11.335 14.266   1.00 76.45  ? 414  ARG   B CA   1 
ATOM   15280 C  C    . ARG   B  2  410 ? 22.881  -12.273 15.182   1.00 71.16  ? 414  ARG   B C    1 
ATOM   15281 O  O    . ARG   B  2  410 ? 23.342  -12.587 16.284   1.00 68.48  ? 414  ARG   B O    1 
ATOM   15282 C  CB   . ARG   B  2  410 ? 24.833  -12.082 13.648   1.00 76.61  ? 414  ARG   B CB   1 
ATOM   15283 C  CG   . ARG   B  2  410 ? 25.672  -11.263 12.696   1.00 79.05  ? 414  ARG   B CG   1 
ATOM   15284 C  CD   . ARG   B  2  410 ? 27.100  -11.767 12.704   1.00 77.82  ? 414  ARG   B CD   1 
ATOM   15285 N  NE   . ARG   B  2  410 ? 27.838  -11.352 11.517   1.00 79.03  ? 414  ARG   B NE   1 
ATOM   15286 C  CZ   . ARG   B  2  410 ? 27.865  -12.034 10.376   1.00 78.45  ? 414  ARG   B CZ   1 
ATOM   15287 N  NH1  . ARG   B  2  410 ? 27.191  -13.171 10.255   1.00 76.38  ? 414  ARG   B NH1  1 
ATOM   15288 N  NH2  . ARG   B  2  410 ? 28.569  -11.576 9.350    1.00 80.86  ? 414  ARG   B NH2  1 
ATOM   15289 H  H    . ARG   B  2  410 ? 24.677  -10.365 15.632   1.00 97.73  ? 414  ARG   B H    1 
ATOM   15290 H  HA   . ARG   B  2  410 ? 23.063  -11.039 13.554   1.00 91.77  ? 414  ARG   B HA   1 
ATOM   15291 H  HB2  . ARG   B  2  410 ? 25.415  -12.384 14.363   1.00 91.97  ? 414  ARG   B HB2  1 
ATOM   15292 H  HB3  . ARG   B  2  410 ? 24.492  -12.844 13.154   1.00 91.97  ? 414  ARG   B HB3  1 
ATOM   15293 H  HG2  . ARG   B  2  410 ? 25.319  -11.343 11.796   1.00 94.89  ? 414  ARG   B HG2  1 
ATOM   15294 H  HG3  . ARG   B  2  410 ? 25.668  -10.333 12.972   1.00 94.89  ? 414  ARG   B HG3  1 
ATOM   15295 H  HD2  . ARG   B  2  410 ? 27.557  -11.414 13.483   1.00 93.42  ? 414  ARG   B HD2  1 
ATOM   15296 H  HD3  . ARG   B  2  410 ? 27.095  -12.737 12.733   1.00 93.42  ? 414  ARG   B HD3  1 
ATOM   15297 H  HE   . ARG   B  2  410 ? 28.286  -10.619 11.558   1.00 94.87  ? 414  ARG   B HE   1 
ATOM   15298 H  HH11 . ARG   B  2  410 ? 26.732  -13.472 10.918   1.00 91.70  ? 414  ARG   B HH11 1 
ATOM   15299 H  HH12 . ARG   B  2  410 ? 27.212  -13.607 9.514    1.00 91.70  ? 414  ARG   B HH12 1 
ATOM   15300 H  HH21 . ARG   B  2  410 ? 29.006  -10.840 9.424    1.00 97.07  ? 414  ARG   B HH21 1 
ATOM   15301 H  HH22 . ARG   B  2  410 ? 28.587  -12.016 8.611    1.00 97.07  ? 414  ARG   B HH22 1 
ATOM   15302 N  N    . HIS   B  2  411 ? 21.719  -12.721 14.721   1.00 75.14  ? 415  HIS   B N    1 
ATOM   15303 C  CA   . HIS   B  2  411 ? 20.933  -13.729 15.419   1.00 72.90  ? 415  HIS   B CA   1 
ATOM   15304 C  C    . HIS   B  2  411 ? 21.265  -15.088 14.818   1.00 67.30  ? 415  HIS   B C    1 
ATOM   15305 O  O    . HIS   B  2  411 ? 21.015  -15.321 13.630   1.00 65.91  ? 415  HIS   B O    1 
ATOM   15306 C  CB   . HIS   B  2  411 ? 19.438  -13.438 15.305   1.00 77.08  ? 415  HIS   B CB   1 
ATOM   15307 C  CG   . HIS   B  2  411 ? 19.020  -12.158 15.959   1.00 84.18  ? 415  HIS   B CG   1 
ATOM   15308 N  ND1  . HIS   B  2  411 ? 18.289  -12.125 17.127   1.00 86.83  ? 415  HIS   B ND1  1 
ATOM   15309 C  CD2  . HIS   B  2  411 ? 19.231  -10.867 15.610   1.00 88.09  ? 415  HIS   B CD2  1 
ATOM   15310 C  CE1  . HIS   B  2  411 ? 18.066  -10.868 17.469   1.00 89.95  ? 415  HIS   B CE1  1 
ATOM   15311 N  NE2  . HIS   B  2  411 ? 18.628  -10.085 16.565   1.00 90.88  ? 415  HIS   B NE2  1 
ATOM   15312 H  H    . HIS   B  2  411 ? 21.357  -12.450 13.990   1.00 90.21  ? 415  HIS   B H    1 
ATOM   15313 H  HA   . HIS   B  2  411 ? 21.162  -13.733 16.361   1.00 87.51  ? 415  HIS   B HA   1 
ATOM   15314 H  HB2  . HIS   B  2  411 ? 19.202  -13.381 14.366   1.00 92.53  ? 415  HIS   B HB2  1 
ATOM   15315 H  HB3  . HIS   B  2  411 ? 18.947  -14.160 15.727   1.00 92.53  ? 415  HIS   B HB3  1 
ATOM   15316 H  HD2  . HIS   B  2  411 ? 19.697  -10.566 14.864   1.00 105.74 ? 415  HIS   B HD2  1 
ATOM   15317 H  HE1  . HIS   B  2  411 ? 17.594  -10.583 18.218   1.00 107.98 ? 415  HIS   B HE1  1 
ATOM   15318 H  HE2  . HIS   B  2  411 ? 18.617  -9.225  16.574   1.00 109.10 ? 415  HIS   B HE2  1 
ATOM   15319 N  N    . ILE   B  2  412 ? 21.830  -15.975 15.631   1.00 64.17  ? 416  ILE   B N    1 
ATOM   15320 C  CA   . ILE   B  2  412 ? 22.296  -17.277 15.176   1.00 63.65  ? 416  ILE   B CA   1 
ATOM   15321 C  C    . ILE   B  2  412 ? 21.636  -18.354 16.024   1.00 65.30  ? 416  ILE   B C    1 
ATOM   15322 O  O    . ILE   B  2  412 ? 21.415  -18.164 17.224   1.00 68.08  ? 416  ILE   B O    1 
ATOM   15323 C  CB   . ILE   B  2  412 ? 23.835  -17.383 15.250   1.00 61.70  ? 416  ILE   B CB   1 
ATOM   15324 C  CG1  . ILE   B  2  412 ? 24.476  -16.205 14.510   1.00 63.63  ? 416  ILE   B CG1  1 
ATOM   15325 C  CG2  . ILE   B  2  412 ? 24.309  -18.709 14.669   1.00 60.21  ? 416  ILE   B CG2  1 
ATOM   15326 C  CD1  . ILE   B  2  412 ? 25.990  -16.201 14.536   1.00 63.00  ? 416  ILE   B CD1  1 
ATOM   15327 H  H    . ILE   B  2  412 ? 21.955  -15.840 16.471   1.00 77.04  ? 416  ILE   B H    1 
ATOM   15328 H  HA   . ILE   B  2  412 ? 22.026  -17.412 14.254   1.00 76.41  ? 416  ILE   B HA   1 
ATOM   15329 H  HB   . ILE   B  2  412 ? 24.104  -17.348 16.182   1.00 74.08  ? 416  ILE   B HB   1 
ATOM   15330 H  HG12 . ILE   B  2  412 ? 24.198  -16.235 13.581   1.00 76.39  ? 416  ILE   B HG12 1 
ATOM   15331 H  HG13 . ILE   B  2  412 ? 24.173  -15.379 14.920   1.00 76.39  ? 416  ILE   B HG13 1 
ATOM   15332 H  HG21 . ILE   B  2  412 ? 25.279  -18.715 14.645   1.00 72.28  ? 416  ILE   B HG21 1 
ATOM   15333 H  HG22 . ILE   B  2  412 ? 23.988  -19.433 15.229   1.00 72.28  ? 416  ILE   B HG22 1 
ATOM   15334 H  HG23 . ILE   B  2  412 ? 23.956  -18.805 13.771   1.00 72.28  ? 416  ILE   B HG23 1 
ATOM   15335 H  HD11 . ILE   B  2  412 ? 26.309  -15.324 14.272   1.00 75.64  ? 416  ILE   B HD11 1 
ATOM   15336 H  HD12 . ILE   B  2  412 ? 26.291  -16.406 15.435   1.00 75.64  ? 416  ILE   B HD12 1 
ATOM   15337 H  HD13 . ILE   B  2  412 ? 26.318  -16.872 13.917   1.00 75.64  ? 416  ILE   B HD13 1 
ATOM   15338 N  N    . ILE   B  2  413 ? 21.315  -19.481 15.394   1.00 65.36  ? 417  ILE   B N    1 
ATOM   15339 C  CA   . ILE   B  2  413 ? 20.712  -20.628 16.062   1.00 63.88  ? 417  ILE   B CA   1 
ATOM   15340 C  C    . ILE   B  2  413 ? 21.624  -21.829 15.859   1.00 61.57  ? 417  ILE   B C    1 
ATOM   15341 O  O    . ILE   B  2  413 ? 22.039  -22.116 14.731   1.00 64.97  ? 417  ILE   B O    1 
ATOM   15342 C  CB   . ILE   B  2  413 ? 19.294  -20.919 15.530   1.00 65.23  ? 417  ILE   B CB   1 
ATOM   15343 C  CG1  . ILE   B  2  413 ? 18.269  -20.004 16.213   1.00 67.27  ? 417  ILE   B CG1  1 
ATOM   15344 C  CG2  . ILE   B  2  413 ? 18.940  -22.394 15.728   1.00 63.76  ? 417  ILE   B CG2  1 
ATOM   15345 C  CD1  . ILE   B  2  413 ? 16.845  -20.160 15.694   1.00 73.82  ? 417  ILE   B CD1  1 
ATOM   15346 H  H    . ILE   B  2  413 ? 21.441  -19.608 14.552   1.00 78.47  ? 417  ILE   B H    1 
ATOM   15347 H  HA   . ILE   B  2  413 ? 20.647  -20.447 17.013   1.00 76.70  ? 417  ILE   B HA   1 
ATOM   15348 H  HB   . ILE   B  2  413 ? 19.275  -20.732 14.579   1.00 78.31  ? 417  ILE   B HB   1 
ATOM   15349 H  HG12 . ILE   B  2  413 ? 18.260  -20.203 17.162   1.00 80.76  ? 417  ILE   B HG12 1 
ATOM   15350 H  HG13 . ILE   B  2  413 ? 18.534  -19.082 16.070   1.00 80.76  ? 417  ILE   B HG13 1 
ATOM   15351 H  HG21 . ILE   B  2  413 ? 17.987  -22.511 15.596   1.00 76.54  ? 417  ILE   B HG21 1 
ATOM   15352 H  HG22 . ILE   B  2  413 ? 19.431  -22.926 15.081   1.00 76.54  ? 417  ILE   B HG22 1 
ATOM   15353 H  HG23 . ILE   B  2  413 ? 19.185  -22.660 16.628   1.00 76.54  ? 417  ILE   B HG23 1 
ATOM   15354 H  HD11 . ILE   B  2  413 ? 16.288  -19.472 16.090   1.00 88.63  ? 417  ILE   B HD11 1 
ATOM   15355 H  HD12 . ILE   B  2  413 ? 16.848  -20.069 14.729   1.00 88.63  ? 417  ILE   B HD12 1 
ATOM   15356 H  HD13 . ILE   B  2  413 ? 16.513  -21.038 15.942   1.00 88.63  ? 417  ILE   B HD13 1 
ATOM   15357 N  N    . ILE   B  2  414 ? 21.935  -22.525 16.950   1.00 58.03  ? 418  ILE   B N    1 
ATOM   15358 C  CA   . ILE   B  2  414 ? 22.701  -23.765 16.919   1.00 59.16  ? 418  ILE   B CA   1 
ATOM   15359 C  C    . ILE   B  2  414 ? 21.803  -24.870 17.454   1.00 61.89  ? 418  ILE   B C    1 
ATOM   15360 O  O    . ILE   B  2  414 ? 21.265  -24.750 18.560   1.00 64.14  ? 418  ILE   B O    1 
ATOM   15361 C  CB   . ILE   B  2  414 ? 23.994  -23.671 17.753   1.00 60.15  ? 418  ILE   B CB   1 
ATOM   15362 C  CG1  . ILE   B  2  414 ? 24.814  -22.441 17.344   1.00 58.31  ? 418  ILE   B CG1  1 
ATOM   15363 C  CG2  . ILE   B  2  414 ? 24.793  -24.964 17.605   1.00 64.08  ? 418  ILE   B CG2  1 
ATOM   15364 C  CD1  . ILE   B  2  414 ? 26.099  -22.237 18.152   1.00 56.15  ? 418  ILE   B CD1  1 
ATOM   15365 H  H    . ILE   B  2  414 ? 21.705  -22.290 17.745   1.00 69.68  ? 418  ILE   B H    1 
ATOM   15366 H  HA   . ILE   B  2  414 ? 22.950  -23.967 16.003   1.00 71.03  ? 418  ILE   B HA   1 
ATOM   15367 H  HB   . ILE   B  2  414 ? 23.763  -23.560 18.689   1.00 72.22  ? 418  ILE   B HB   1 
ATOM   15368 H  HG12 . ILE   B  2  414 ? 25.066  -22.534 16.412   1.00 70.01  ? 418  ILE   B HG12 1 
ATOM   15369 H  HG13 . ILE   B  2  414 ? 24.266  -21.650 17.463   1.00 70.01  ? 418  ILE   B HG13 1 
ATOM   15370 H  HG21 . ILE   B  2  414 ? 25.703  -24.808 17.904   1.00 76.94  ? 418  ILE   B HG21 1 
ATOM   15371 H  HG22 . ILE   B  2  414 ? 24.381  -25.654 18.148   1.00 76.94  ? 418  ILE   B HG22 1 
ATOM   15372 H  HG23 . ILE   B  2  414 ? 24.792  -25.231 16.673   1.00 76.94  ? 418  ILE   B HG23 1 
ATOM   15373 H  HD11 . ILE   B  2  414 ? 26.580  -21.475 17.793   1.00 67.42  ? 418  ILE   B HD11 1 
ATOM   15374 H  HD12 . ILE   B  2  414 ? 25.866  -22.075 19.079   1.00 67.42  ? 418  ILE   B HD12 1 
ATOM   15375 H  HD13 . ILE   B  2  414 ? 26.645  -23.036 18.083   1.00 67.42  ? 418  ILE   B HD13 1 
ATOM   15376 N  N    . LYS   B  2  415 ? 21.641  -25.938 16.683   1.00 61.35  ? 419  LYS   B N    1 
ATOM   15377 C  CA   . LYS   B  2  415 ? 20.736  -27.007 17.079   1.00 63.90  ? 419  LYS   B CA   1 
ATOM   15378 C  C    . LYS   B  2  415 ? 21.214  -28.316 16.477   1.00 59.96  ? 419  LYS   B C    1 
ATOM   15379 O  O    . LYS   B  2  415 ? 21.904  -28.318 15.450   1.00 61.33  ? 419  LYS   B O    1 
ATOM   15380 C  CB   . LYS   B  2  415 ? 19.297  -26.716 16.632   1.00 73.15  ? 419  LYS   B CB   1 
ATOM   15381 C  CG   . LYS   B  2  415 ? 19.086  -26.780 15.125   1.00 76.91  ? 419  LYS   B CG   1 
ATOM   15382 C  CD   . LYS   B  2  415 ? 17.616  -26.668 14.771   1.00 82.88  ? 419  LYS   B CD   1 
ATOM   15383 C  CE   . LYS   B  2  415 ? 17.415  -26.674 13.267   1.00 93.14  ? 419  LYS   B CE   1 
ATOM   15384 N  NZ   . LYS   B  2  415 ? 16.024  -26.317 12.880   1.00 99.75  ? 419  LYS   B NZ   1 
ATOM   15385 H  H    . LYS   B  2  415 ? 22.040  -26.065 15.932   1.00 73.66  ? 419  LYS   B H    1 
ATOM   15386 H  HA   . LYS   B  2  415 ? 20.755  -27.096 18.045   1.00 76.72  ? 419  LYS   B HA   1 
ATOM   15387 H  HB2  . LYS   B  2  415 ? 18.708  -27.370 17.039   1.00 87.82  ? 419  LYS   B HB2  1 
ATOM   15388 H  HB3  . LYS   B  2  415 ? 19.056  -25.823 16.925   1.00 87.82  ? 419  LYS   B HB3  1 
ATOM   15389 H  HG2  . LYS   B  2  415 ? 19.559  -26.046 14.702   1.00 92.33  ? 419  LYS   B HG2  1 
ATOM   15390 H  HG3  . LYS   B  2  415 ? 19.418  -27.627 14.789   1.00 92.33  ? 419  LYS   B HG3  1 
ATOM   15391 H  HD2  . LYS   B  2  415 ? 17.134  -27.421 15.148   1.00 99.49  ? 419  LYS   B HD2  1 
ATOM   15392 H  HD3  . LYS   B  2  415 ? 17.261  -25.837 15.125   1.00 99.49  ? 419  LYS   B HD3  1 
ATOM   15393 H  HE2  . LYS   B  2  415 ? 18.016  -26.028 12.864   1.00 111.81 ? 419  LYS   B HE2  1 
ATOM   15394 H  HE3  . LYS   B  2  415 ? 17.605  -27.562 12.925   1.00 111.81 ? 419  LYS   B HE3  1 
ATOM   15395 H  HZ1  . LYS   B  2  415 ? 15.844  -26.631 12.067   1.00 119.74 ? 419  LYS   B HZ1  1 
ATOM   15396 H  HZ2  . LYS   B  2  415 ? 15.447  -26.667 13.460   1.00 119.74 ? 419  LYS   B HZ2  1 
ATOM   15397 H  HZ3  . LYS   B  2  415 ? 15.927  -25.432 12.875   1.00 119.74 ? 419  LYS   B HZ3  1 
ATOM   15398 N  N    . PRO   B  2  416 ? 20.843  -29.448 17.072   1.00 57.78  ? 420  PRO   B N    1 
ATOM   15399 C  CA   . PRO   B  2  416 ? 21.119  -30.734 16.429   1.00 60.19  ? 420  PRO   B CA   1 
ATOM   15400 C  C    . PRO   B  2  416 ? 20.202  -30.926 15.235   1.00 63.49  ? 420  PRO   B C    1 
ATOM   15401 O  O    . PRO   B  2  416 ? 19.049  -30.490 15.235   1.00 67.85  ? 420  PRO   B O    1 
ATOM   15402 C  CB   . PRO   B  2  416 ? 20.825  -31.763 17.530   1.00 61.53  ? 420  PRO   B CB   1 
ATOM   15403 C  CG   . PRO   B  2  416 ? 20.205  -30.993 18.684   1.00 59.11  ? 420  PRO   B CG   1 
ATOM   15404 C  CD   . PRO   B  2  416 ? 19.925  -29.602 18.213   1.00 57.75  ? 420  PRO   B CD   1 
ATOM   15405 H  HA   . PRO   B  2  416 ? 22.048  -30.811 16.164   1.00 72.26  ? 420  PRO   B HA   1 
ATOM   15406 H  HB2  . PRO   B  2  416 ? 20.208  -32.431 17.193   1.00 73.87  ? 420  PRO   B HB2  1 
ATOM   15407 H  HB3  . PRO   B  2  416 ? 21.653  -32.187 17.807   1.00 73.87  ? 420  PRO   B HB3  1 
ATOM   15408 H  HG2  . PRO   B  2  416 ? 19.381  -31.429 18.951   1.00 70.97  ? 420  PRO   B HG2  1 
ATOM   15409 H  HG3  . PRO   B  2  416 ? 20.828  -30.977 19.427   1.00 70.97  ? 420  PRO   B HG3  1 
ATOM   15410 H  HD2  . PRO   B  2  416 ? 19.002  -29.512 17.929   1.00 69.34  ? 420  PRO   B HD2  1 
ATOM   15411 H  HD3  . PRO   B  2  416 ? 20.124  -28.955 18.907   1.00 69.34  ? 420  PRO   B HD3  1 
ATOM   15412 N  N    . VAL   B  2  417 ? 20.727  -31.582 14.200   1.00 64.40  ? 421  VAL   B N    1 
ATOM   15413 C  CA   . VAL   B  2  417 ? 19.908  -31.825 13.022   1.00 69.10  ? 421  VAL   B CA   1 
ATOM   15414 C  C    . VAL   B  2  417 ? 18.724  -32.693 13.423   1.00 67.57  ? 421  VAL   B C    1 
ATOM   15415 O  O    . VAL   B  2  417 ? 18.867  -33.672 14.168   1.00 65.41  ? 421  VAL   B O    1 
ATOM   15416 C  CB   . VAL   B  2  417 ? 20.721  -32.479 11.891   1.00 73.15  ? 421  VAL   B CB   1 
ATOM   15417 C  CG1  . VAL   B  2  417 ? 22.020  -31.712 11.636   1.00 68.93  ? 421  VAL   B CG1  1 
ATOM   15418 C  CG2  . VAL   B  2  417 ? 20.999  -33.949 12.190   1.00 78.70  ? 421  VAL   B CG2  1 
ATOM   15419 H  H    . VAL   B  2  417 ? 21.531  -31.886 14.159   1.00 77.32  ? 421  VAL   B H    1 
ATOM   15420 H  HA   . VAL   B  2  417 ? 19.587  -30.975 12.684   1.00 82.96  ? 421  VAL   B HA   1 
ATOM   15421 H  HB   . VAL   B  2  417 ? 20.194  -32.443 11.078   1.00 87.81  ? 421  VAL   B HB   1 
ATOM   15422 H  HG11 . VAL   B  2  417 ? 22.540  -32.186 10.968   1.00 82.75  ? 421  VAL   B HG11 1 
ATOM   15423 H  HG12 . VAL   B  2  417 ? 21.803  -30.822 11.316   1.00 82.75  ? 421  VAL   B HG12 1 
ATOM   15424 H  HG13 . VAL   B  2  417 ? 22.520  -31.654 12.464   1.00 82.75  ? 421  VAL   B HG13 1 
ATOM   15425 H  HG21 . VAL   B  2  417 ? 21.572  -34.310 11.495   1.00 94.47  ? 421  VAL   B HG21 1 
ATOM   15426 H  HG22 . VAL   B  2  417 ? 21.441  -34.018 13.051   1.00 94.47  ? 421  VAL   B HG22 1 
ATOM   15427 H  HG23 . VAL   B  2  417 ? 20.158  -34.432 12.210   1.00 94.47  ? 421  VAL   B HG23 1 
ATOM   15428 N  N    . GLY   B  2  418 ? 17.540  -32.323 12.944   1.00 69.09  ? 422  GLY   B N    1 
ATOM   15429 C  CA   . GLY   B  2  418 ? 16.348  -33.109 13.165   1.00 69.65  ? 422  GLY   B CA   1 
ATOM   15430 C  C    . GLY   B  2  418 ? 15.656  -32.906 14.495   1.00 67.38  ? 422  GLY   B C    1 
ATOM   15431 O  O    . GLY   B  2  418 ? 14.658  -33.587 14.758   1.00 67.16  ? 422  GLY   B O    1 
ATOM   15432 H  H    . GLY   B  2  418 ? 17.406  -31.609 12.484   1.00 82.94  ? 422  GLY   B H    1 
ATOM   15433 H  HA2  . GLY   B  2  418 ? 15.707  -32.896 12.468   1.00 83.62  ? 422  GLY   B HA2  1 
ATOM   15434 H  HA3  . GLY   B  2  418 ? 16.584  -34.048 13.100   1.00 83.62  ? 422  GLY   B HA3  1 
ATOM   15435 N  N    . LEU   B  2  419 ? 16.132  -31.997 15.342   1.00 64.06  ? 423  LEU   B N    1 
ATOM   15436 C  CA   . LEU   B  2  419 ? 15.562  -31.813 16.670   1.00 60.09  ? 423  LEU   B CA   1 
ATOM   15437 C  C    . LEU   B  2  419 ? 15.142  -30.365 16.876   1.00 64.48  ? 423  LEU   B C    1 
ATOM   15438 O  O    . LEU   B  2  419 ? 15.833  -29.435 16.447   1.00 67.32  ? 423  LEU   B O    1 
ATOM   15439 C  CB   . LEU   B  2  419 ? 16.552  -32.238 17.762   1.00 56.25  ? 423  LEU   B CB   1 
ATOM   15440 C  CG   . LEU   B  2  419 ? 16.866  -33.739 17.810   1.00 54.66  ? 423  LEU   B CG   1 
ATOM   15441 C  CD1  . LEU   B  2  419 ? 17.725  -34.073 19.021   1.00 52.67  ? 423  LEU   B CD1  1 
ATOM   15442 C  CD2  . LEU   B  2  419 ? 15.594  -34.589 17.814   1.00 56.04  ? 423  LEU   B CD2  1 
ATOM   15443 H  H    . LEU   B  2  419 ? 16.790  -31.472 15.167   1.00 76.91  ? 423  LEU   B H    1 
ATOM   15444 H  HA   . LEU   B  2  419 ? 14.766  -32.360 16.750   1.00 72.14  ? 423  LEU   B HA   1 
ATOM   15445 H  HB2  . LEU   B  2  419 ? 17.390  -31.771 17.614   1.00 67.54  ? 423  LEU   B HB2  1 
ATOM   15446 H  HB3  . LEU   B  2  419 ? 16.182  -31.991 18.624   1.00 67.54  ? 423  LEU   B HB3  1 
ATOM   15447 H  HG   . LEU   B  2  419 ? 17.361  -33.962 17.006   1.00 65.63  ? 423  LEU   B HG   1 
ATOM   15448 H  HD11 . LEU   B  2  419 ? 17.736  -35.035 19.146   1.00 63.24  ? 423  LEU   B HD11 1 
ATOM   15449 H  HD12 . LEU   B  2  419 ? 18.627  -33.750 18.867   1.00 63.24  ? 423  LEU   B HD12 1 
ATOM   15450 H  HD13 . LEU   B  2  419 ? 17.349  -33.642 19.804   1.00 63.24  ? 423  LEU   B HD13 1 
ATOM   15451 H  HD21 . LEU   B  2  419 ? 15.842  -35.527 17.800   1.00 67.29  ? 423  LEU   B HD21 1 
ATOM   15452 H  HD22 . LEU   B  2  419 ? 15.086  -34.393 18.617   1.00 67.29  ? 423  LEU   B HD22 1 
ATOM   15453 H  HD23 . LEU   B  2  419 ? 15.068  -34.374 17.029   1.00 67.29  ? 423  LEU   B HD23 1 
ATOM   15454 N  N    . GLY   B  2  420 ? 13.999  -30.191 17.542   1.00 70.77  ? 424  GLY   B N    1 
ATOM   15455 C  CA   . GLY   B  2  420 ? 13.456  -28.858 17.729   1.00 73.11  ? 424  GLY   B CA   1 
ATOM   15456 C  C    . GLY   B  2  420 ? 14.297  -27.997 18.652   1.00 74.05  ? 424  GLY   B C    1 
ATOM   15457 O  O    . GLY   B  2  420 ? 14.469  -26.800 18.407   1.00 72.38  ? 424  GLY   B O    1 
ATOM   15458 H  H    . GLY   B  2  420 ? 13.529  -30.822 17.888   1.00 84.96  ? 424  GLY   B H    1 
ATOM   15459 H  HA2  . GLY   B  2  420 ? 13.399  -28.413 16.869   1.00 87.77  ? 424  GLY   B HA2  1 
ATOM   15460 H  HA3  . GLY   B  2  420 ? 12.566  -28.927 18.109   1.00 87.77  ? 424  GLY   B HA3  1 
ATOM   15461 N  N    . ASP   B  2  421 ? 14.833  -28.588 19.719   1.00 75.50  ? 425  ASP   B N    1 
ATOM   15462 C  CA   . ASP   B  2  421 ? 15.570  -27.812 20.709   1.00 77.64  ? 425  ASP   B CA   1 
ATOM   15463 C  C    . ASP   B  2  421 ? 16.708  -27.055 20.039   1.00 73.88  ? 425  ASP   B C    1 
ATOM   15464 O  O    . ASP   B  2  421 ? 17.449  -27.616 19.228   1.00 74.37  ? 425  ASP   B O    1 
ATOM   15465 C  CB   . ASP   B  2  421 ? 16.127  -28.722 21.802   1.00 79.88  ? 425  ASP   B CB   1 
ATOM   15466 C  CG   . ASP   B  2  421 ? 15.082  -29.655 22.376   1.00 86.52  ? 425  ASP   B CG   1 
ATOM   15467 O  OD1  . ASP   B  2  421 ? 14.627  -30.560 21.645   1.00 88.73  ? 425  ASP   B OD1  1 
ATOM   15468 O  OD2  . ASP   B  2  421 ? 14.721  -29.486 23.559   1.00 89.32  ? 425  ASP   B OD2  1 
ATOM   15469 H  H    . ASP   B  2  421 ? 14.784  -29.429 19.891   1.00 90.64  ? 425  ASP   B H    1 
ATOM   15470 H  HA   . ASP   B  2  421 ? 14.967  -27.175 21.123   1.00 93.21  ? 425  ASP   B HA   1 
ATOM   15471 H  HB2  . ASP   B  2  421 ? 16.841  -29.264 21.430   1.00 95.89  ? 425  ASP   B HB2  1 
ATOM   15472 H  HB3  . ASP   B  2  421 ? 16.469  -28.174 22.526   1.00 95.89  ? 425  ASP   B HB3  1 
ATOM   15473 N  N    . ALA   B  2  422 ? 16.852  -25.778 20.385   1.00 73.84  ? 426  ALA   B N    1 
ATOM   15474 C  CA   . ALA   B  2  422 ? 17.852  -24.935 19.755   1.00 73.33  ? 426  ALA   B CA   1 
ATOM   15475 C  C    . ALA   B  2  422 ? 18.490  -24.008 20.777   1.00 71.16  ? 426  ALA   B C    1 
ATOM   15476 O  O    . ALA   B  2  422 ? 17.913  -23.695 21.822   1.00 73.79  ? 426  ALA   B O    1 
ATOM   15477 C  CB   . ALA   B  2  422 ? 17.250  -24.111 18.609   1.00 78.24  ? 426  ALA   B CB   1 
ATOM   15478 H  H    . ALA   B  2  422 ? 16.379  -25.380 20.984   1.00 88.64  ? 426  ALA   B H    1 
ATOM   15479 H  HA   . ALA   B  2  422 ? 18.554  -25.503 19.401   1.00 88.03  ? 426  ALA   B HA   1 
ATOM   15480 H  HB1  . ALA   B  2  422 ? 17.840  -23.367 18.410   1.00 93.93  ? 426  ALA   B HB1  1 
ATOM   15481 H  HB2  . ALA   B  2  422 ? 17.158  -24.678 17.827   1.00 93.93  ? 426  ALA   B HB2  1 
ATOM   15482 H  HB3  . ALA   B  2  422 ? 16.380  -23.779 18.881   1.00 93.93  ? 426  ALA   B HB3  1 
ATOM   15483 N  N    . LEU   B  2  423 ? 19.703  -23.577 20.448   1.00 69.72  ? 427  LEU   B N    1 
ATOM   15484 C  CA   . LEU   B  2  423 ? 20.466  -22.613 21.227   1.00 68.07  ? 427  LEU   B CA   1 
ATOM   15485 C  C    . LEU   B  2  423 ? 20.425  -21.284 20.487   1.00 68.28  ? 427  LEU   B C    1 
ATOM   15486 O  O    . LEU   B  2  423 ? 20.877  -21.198 19.341   1.00 69.38  ? 427  LEU   B O    1 
ATOM   15487 C  CB   . LEU   B  2  423 ? 21.906  -23.092 21.409   1.00 66.22  ? 427  LEU   B CB   1 
ATOM   15488 C  CG   . LEU   B  2  423 ? 22.826  -22.332 22.366   1.00 67.79  ? 427  LEU   B CG   1 
ATOM   15489 C  CD1  . LEU   B  2  423 ? 24.145  -23.071 22.499   1.00 65.87  ? 427  LEU   B CD1  1 
ATOM   15490 C  CD2  . LEU   B  2  423 ? 23.073  -20.901 21.911   1.00 71.66  ? 427  LEU   B CD2  1 
ATOM   15491 H  H    . LEU   B  2  423 ? 20.122  -23.843 19.745   1.00 83.70  ? 427  LEU   B H    1 
ATOM   15492 H  HA   . LEU   B  2  423 ? 20.072  -22.496 22.106   1.00 81.72  ? 427  LEU   B HA   1 
ATOM   15493 H  HB2  . LEU   B  2  423 ? 21.870  -24.006 21.732   1.00 79.50  ? 427  LEU   B HB2  1 
ATOM   15494 H  HB3  . LEU   B  2  423 ? 22.334  -23.065 20.539   1.00 79.50  ? 427  LEU   B HB3  1 
ATOM   15495 H  HG   . LEU   B  2  423 ? 22.391  -22.281 23.232   1.00 81.39  ? 427  LEU   B HG   1 
ATOM   15496 H  HD11 . LEU   B  2  423 ? 24.728  -22.574 23.095   1.00 79.08  ? 427  LEU   B HD11 1 
ATOM   15497 H  HD12 . LEU   B  2  423 ? 23.977  -23.955 22.862   1.00 79.08  ? 427  LEU   B HD12 1 
ATOM   15498 H  HD13 . LEU   B  2  423 ? 24.555  -23.146 21.622   1.00 79.08  ? 427  LEU   B HD13 1 
ATOM   15499 H  HD21 . LEU   B  2  423 ? 23.963  -20.631 22.188   1.00 86.03  ? 427  LEU   B HD21 1 
ATOM   15500 H  HD22 . LEU   B  2  423 ? 23.001  -20.861 20.945   1.00 86.03  ? 427  LEU   B HD22 1 
ATOM   15501 H  HD23 . LEU   B  2  423 ? 22.410  -20.322 22.317   1.00 86.03  ? 427  LEU   B HD23 1 
ATOM   15502 N  N    . GLU   B  2  424 ? 19.888  -20.254 21.134   1.00 67.96  ? 428  GLU   B N    1 
ATOM   15503 C  CA   . GLU   B  2  424 ? 19.825  -18.926 20.539   1.00 68.14  ? 428  GLU   B CA   1 
ATOM   15504 C  C    . GLU   B  2  424 ? 21.122  -18.190 20.851   1.00 63.74  ? 428  GLU   B C    1 
ATOM   15505 O  O    . GLU   B  2  424 ? 21.486  -18.034 22.021   1.00 66.42  ? 428  GLU   B O    1 
ATOM   15506 C  CB   . GLU   B  2  424 ? 18.621  -18.145 21.062   1.00 76.22  ? 428  GLU   B CB   1 
ATOM   15507 C  CG   . GLU   B  2  424 ? 17.342  -18.962 21.132   1.00 80.43  ? 428  GLU   B CG   1 
ATOM   15508 C  CD   . GLU   B  2  424 ? 16.113  -18.161 20.750   1.00 87.67  ? 428  GLU   B CD   1 
ATOM   15509 O  OE1  . GLU   B  2  424 ? 16.107  -16.932 20.971   1.00 90.99  ? 428  GLU   B OE1  1 
ATOM   15510 O  OE2  . GLU   B  2  424 ? 15.154  -18.761 20.220   1.00 89.99  ? 428  GLU   B OE2  1 
ATOM   15511 H  H    . GLU   B  2  424 ? 19.551  -20.302 21.924   1.00 81.59  ? 428  GLU   B H    1 
ATOM   15512 H  HA   . GLU   B  2  424 ? 19.730  -19.005 19.577   1.00 81.81  ? 428  GLU   B HA   1 
ATOM   15513 H  HB2  . GLU   B  2  424 ? 18.820  -17.830 21.958   1.00 91.50  ? 428  GLU   B HB2  1 
ATOM   15514 H  HB3  . GLU   B  2  424 ? 18.460  -17.391 20.474   1.00 91.50  ? 428  GLU   B HB3  1 
ATOM   15515 H  HG2  . GLU   B  2  424 ? 17.412  -19.712 20.521   1.00 96.55  ? 428  GLU   B HG2  1 
ATOM   15516 H  HG3  . GLU   B  2  424 ? 17.221  -19.283 22.039   1.00 96.55  ? 428  GLU   B HG3  1 
ATOM   15517 N  N    . LEU   B  2  425 ? 21.818  -17.744 19.811   1.00 64.63  ? 429  LEU   B N    1 
ATOM   15518 C  CA   . LEU   B  2  425 ? 23.093  -17.058 19.957   1.00 65.79  ? 429  LEU   B CA   1 
ATOM   15519 C  C    . LEU   B  2  425 ? 23.017  -15.700 19.279   1.00 72.48  ? 429  LEU   B C    1 
ATOM   15520 O  O    . LEU   B  2  425 ? 22.613  -15.601 18.115   1.00 74.82  ? 429  LEU   B O    1 
ATOM   15521 C  CB   . LEU   B  2  425 ? 24.236  -17.881 19.358   1.00 63.24  ? 429  LEU   B CB   1 
ATOM   15522 C  CG   . LEU   B  2  425 ? 25.614  -17.214 19.375   1.00 65.74  ? 429  LEU   B CG   1 
ATOM   15523 C  CD1  . LEU   B  2  425 ? 26.181  -17.159 20.788   1.00 66.27  ? 429  LEU   B CD1  1 
ATOM   15524 C  CD2  . LEU   B  2  425 ? 26.561  -17.937 18.436   1.00 62.97  ? 429  LEU   B CD2  1 
ATOM   15525 H  H    . LEU   B  2  425 ? 21.565  -17.830 18.993   1.00 77.59  ? 429  LEU   B H    1 
ATOM   15526 H  HA   . LEU   B  2  425 ? 23.276  -16.920 20.899   1.00 78.98  ? 429  LEU   B HA   1 
ATOM   15527 H  HB2  . LEU   B  2  425 ? 24.309  -18.708 19.859   1.00 75.92  ? 429  LEU   B HB2  1 
ATOM   15528 H  HB3  . LEU   B  2  425 ? 24.019  -18.072 18.432   1.00 75.92  ? 429  LEU   B HB3  1 
ATOM   15529 H  HG   . LEU   B  2  425 ? 25.523  -16.299 19.066   1.00 78.93  ? 429  LEU   B HG   1 
ATOM   15530 H  HD11 . LEU   B  2  425 ? 27.141  -17.028 20.738   1.00 79.56  ? 429  LEU   B HD11 1 
ATOM   15531 H  HD12 . LEU   B  2  425 ? 25.771  -16.420 21.264   1.00 79.56  ? 429  LEU   B HD12 1 
ATOM   15532 H  HD13 . LEU   B  2  425 ? 25.984  -17.994 21.241   1.00 79.56  ? 429  LEU   B HD13 1 
ATOM   15533 H  HD21 . LEU   B  2  425 ? 27.421  -17.489 18.448   1.00 75.60  ? 429  LEU   B HD21 1 
ATOM   15534 H  HD22 . LEU   B  2  425 ? 26.662  -18.855 18.735   1.00 75.60  ? 429  LEU   B HD22 1 
ATOM   15535 H  HD23 . LEU   B  2  425 ? 26.191  -17.920 17.540   1.00 75.60  ? 429  LEU   B HD23 1 
ATOM   15536 N  N    . LEU   B  2  426 ? 23.409  -14.662 20.008   1.00 76.31  ? 430  LEU   B N    1 
ATOM   15537 C  CA   . LEU   B  2  426 ? 23.499  -13.308 19.483   1.00 79.86  ? 430  LEU   B CA   1 
ATOM   15538 C  C    . LEU   B  2  426 ? 24.966  -12.913 19.451   1.00 76.86  ? 430  LEU   B C    1 
ATOM   15539 O  O    . LEU   B  2  426 ? 25.646  -12.964 20.482   1.00 74.14  ? 430  LEU   B O    1 
ATOM   15540 C  CB   . LEU   B  2  426 ? 22.704  -12.330 20.344   1.00 85.87  ? 430  LEU   B CB   1 
ATOM   15541 C  CG   . LEU   B  2  426 ? 22.280  -11.030 19.664   1.00 89.64  ? 430  LEU   B CG   1 
ATOM   15542 C  CD1  . LEU   B  2  426 ? 21.212  -11.299 18.614   1.00 90.03  ? 430  LEU   B CD1  1 
ATOM   15543 C  CD2  . LEU   B  2  426 ? 21.787  -10.043 20.704   1.00 91.42  ? 430  LEU   B CD2  1 
ATOM   15544 H  H    . LEU   B  2  426 ? 23.636  -14.720 20.836   1.00 91.61  ? 430  LEU   B H    1 
ATOM   15545 H  HA   . LEU   B  2  426 ? 23.139  -13.279 18.582   1.00 95.87  ? 430  LEU   B HA   1 
ATOM   15546 H  HB2  . LEU   B  2  426 ? 21.895  -12.776 20.640   1.00 103.08 ? 430  LEU   B HB2  1 
ATOM   15547 H  HB3  . LEU   B  2  426 ? 23.249  -12.090 21.110   1.00 103.08 ? 430  LEU   B HB3  1 
ATOM   15548 H  HG   . LEU   B  2  426 ? 23.042  -10.636 19.210   1.00 107.60 ? 430  LEU   B HG   1 
ATOM   15549 H  HD11 . LEU   B  2  426 ? 20.901  -10.453 18.257   1.00 108.07 ? 430  LEU   B HD11 1 
ATOM   15550 H  HD12 . LEU   B  2  426 ? 21.596  -11.837 17.905   1.00 108.07 ? 430  LEU   B HD12 1 
ATOM   15551 H  HD13 . LEU   B  2  426 ? 20.475  -11.774 19.029   1.00 108.07 ? 430  LEU   B HD13 1 
ATOM   15552 H  HD21 . LEU   B  2  426 ? 21.610  -9.192  20.274   1.00 109.74 ? 430  LEU   B HD21 1 
ATOM   15553 H  HD22 . LEU   B  2  426 ? 20.974  -10.386 21.105   1.00 109.74 ? 430  LEU   B HD22 1 
ATOM   15554 H  HD23 . LEU   B  2  426 ? 22.470  -9.933  21.384   1.00 109.74 ? 430  LEU   B HD23 1 
ATOM   15555 N  N    . VAL   B  2  427 ? 25.454  -12.530 18.278   1.00 78.52  ? 431  VAL   B N    1 
ATOM   15556 C  CA   . VAL   B  2  427 ? 26.820  -12.051 18.125   1.00 76.09  ? 431  VAL   B CA   1 
ATOM   15557 C  C    . VAL   B  2  427 ? 26.773  -10.533 18.095   1.00 80.23  ? 431  VAL   B C    1 
ATOM   15558 O  O    . VAL   B  2  427 ? 26.173  -9.939  17.190   1.00 80.51  ? 431  VAL   B O    1 
ATOM   15559 C  CB   . VAL   B  2  427 ? 27.486  -12.608 16.860   1.00 73.91  ? 431  VAL   B CB   1 
ATOM   15560 C  CG1  . VAL   B  2  427 ? 28.944  -12.179 16.810   1.00 73.87  ? 431  VAL   B CG1  1 
ATOM   15561 C  CG2  . VAL   B  2  427 ? 27.372  -14.120 16.828   1.00 72.92  ? 431  VAL   B CG2  1 
ATOM   15562 H  H    . VAL   B  2  427 ? 25.005  -12.538 17.545   1.00 94.26  ? 431  VAL   B H    1 
ATOM   15563 H  HA   . VAL   B  2  427 ? 27.348  -12.335 18.888   1.00 91.34  ? 431  VAL   B HA   1 
ATOM   15564 H  HB   . VAL   B  2  427 ? 27.034  -12.257 16.076   1.00 88.72  ? 431  VAL   B HB   1 
ATOM   15565 H  HG11 . VAL   B  2  427 ? 29.369  -12.592 16.043   1.00 88.68  ? 431  VAL   B HG11 1 
ATOM   15566 H  HG12 . VAL   B  2  427 ? 28.986  -11.213 16.732   1.00 88.68  ? 431  VAL   B HG12 1 
ATOM   15567 H  HG13 . VAL   B  2  427 ? 29.385  -12.464 17.626   1.00 88.68  ? 431  VAL   B HG13 1 
ATOM   15568 H  HG21 . VAL   B  2  427 ? 27.786  -14.450 16.016   1.00 87.54  ? 431  VAL   B HG21 1 
ATOM   15569 H  HG22 . VAL   B  2  427 ? 27.826  -14.486 17.604   1.00 87.54  ? 431  VAL   B HG22 1 
ATOM   15570 H  HG23 . VAL   B  2  427 ? 26.434  -14.366 16.846   1.00 87.54  ? 431  VAL   B HG23 1 
ATOM   15571 N  N    . SER   B  2  428 ? 27.394  -9.909  19.086   1.00 82.81  ? 432  SER   B N    1 
ATOM   15572 C  CA   . SER   B  2  428 ? 27.463  -8.465  19.160   1.00 90.42  ? 432  SER   B CA   1 
ATOM   15573 C  C    . SER   B  2  428 ? 28.905  -8.020  19.004   1.00 95.69  ? 432  SER   B C    1 
ATOM   15574 O  O    . SER   B  2  428 ? 29.787  -8.553  19.688   1.00 98.99  ? 432  SER   B O    1 
ATOM   15575 C  CB   . SER   B  2  428 ? 26.898  -7.967  20.492   1.00 91.14  ? 432  SER   B CB   1 
ATOM   15576 O  OG   . SER   B  2  428 ? 25.501  -8.198  20.556   1.00 89.30  ? 432  SER   B OG   1 
ATOM   15577 H  H    . SER   B  2  428 ? 27.788  -10.310 19.737   1.00 99.41  ? 432  SER   B H    1 
ATOM   15578 H  HA   . SER   B  2  428 ? 26.935  -8.073  18.446   1.00 108.54 ? 432  SER   B HA   1 
ATOM   15579 H  HB2  . SER   B  2  428 ? 27.332  -8.442  21.218   1.00 109.40 ? 432  SER   B HB2  1 
ATOM   15580 H  HB3  . SER   B  2  428 ? 27.066  -7.015  20.572   1.00 109.40 ? 432  SER   B HB3  1 
ATOM   15581 H  HG   . SER   B  2  428 ? 25.192  -7.895  21.276   1.00 107.20 ? 432  SER   B HG   1 
ATOM   15582 N  N    . PRO   B  2  429 ? 29.195  -7.074  18.119   1.00 97.22  ? 433  PRO   B N    1 
ATOM   15583 C  CA   . PRO   B  2  429 ? 30.577  -6.626  17.956   1.00 96.22  ? 433  PRO   B CA   1 
ATOM   15584 C  C    . PRO   B  2  429 ? 31.001  -5.711  19.092   1.00 99.42  ? 433  PRO   B C    1 
ATOM   15585 O  O    . PRO   B  2  429 ? 30.184  -5.039  19.725   1.00 100.98 ? 433  PRO   B O    1 
ATOM   15586 C  CB   . PRO   B  2  429 ? 30.543  -5.875  16.621   1.00 95.88  ? 433  PRO   B CB   1 
ATOM   15587 C  CG   . PRO   B  2  429 ? 29.163  -5.317  16.568   1.00 98.25  ? 433  PRO   B CG   1 
ATOM   15588 C  CD   . PRO   B  2  429 ? 28.274  -6.338  17.232   1.00 98.20  ? 433  PRO   B CD   1 
ATOM   15589 H  HA   . PRO   B  2  429 ? 31.190  -7.375  17.892   1.00 115.50 ? 433  PRO   B HA   1 
ATOM   15590 H  HB2  . PRO   B  2  429 ? 31.209  -5.169  16.615   1.00 115.09 ? 433  PRO   B HB2  1 
ATOM   15591 H  HB3  . PRO   B  2  429 ? 30.704  -6.488  15.887   1.00 115.09 ? 433  PRO   B HB3  1 
ATOM   15592 H  HG2  . PRO   B  2  429 ? 29.134  -4.474  17.046   1.00 117.93 ? 433  PRO   B HG2  1 
ATOM   15593 H  HG3  . PRO   B  2  429 ? 28.901  -5.183  15.643   1.00 117.93 ? 433  PRO   B HG3  1 
ATOM   15594 H  HD2  . PRO   B  2  429 ? 27.575  -5.904  17.745   1.00 117.87 ? 433  PRO   B HD2  1 
ATOM   15595 H  HD3  . PRO   B  2  429 ? 27.882  -6.933  16.573   1.00 117.87 ? 433  PRO   B HD3  1 
ATOM   15596 N  N    . GLU   B  2  430 ? 32.311  -5.702  19.349   1.00 100.59 ? 434  GLU   B N    1 
ATOM   15597 C  CA   . GLU   B  2  430 ? 32.911  -4.825  20.353   1.00 103.59 ? 434  GLU   B CA   1 
ATOM   15598 C  C    . GLU   B  2  430 ? 34.208  -4.285  19.756   1.00 107.56 ? 434  GLU   B C    1 
ATOM   15599 O  O    . GLU   B  2  430 ? 35.304  -4.767  20.051   1.00 107.35 ? 434  GLU   B O    1 
ATOM   15600 C  CB   . GLU   B  2  430 ? 33.150  -5.549  21.673   1.00 101.51 ? 434  GLU   B CB   1 
ATOM   15601 C  CG   . GLU   B  2  430 ? 31.899  -5.689  22.513   1.00 102.87 ? 434  GLU   B CG   1 
ATOM   15602 C  CD   . GLU   B  2  430 ? 32.166  -5.489  23.991   1.00 104.08 ? 434  GLU   B CD   1 
ATOM   15603 O  OE1  . GLU   B  2  430 ? 33.179  -6.020  24.493   1.00 102.61 ? 434  GLU   B OE1  1 
ATOM   15604 O  OE2  . GLU   B  2  430 ? 31.368  -4.789  24.648   1.00 106.44 ? 434  GLU   B OE2  1 
ATOM   15605 H  H    . GLU   B  2  430 ? 32.881  -6.205  18.946   1.00 120.75 ? 434  GLU   B H    1 
ATOM   15606 H  HA   . GLU   B  2  430 ? 32.313  -4.081  20.528   1.00 124.35 ? 434  GLU   B HA   1 
ATOM   15607 H  HB2  . GLU   B  2  430 ? 33.485  -6.440  21.486   1.00 121.85 ? 434  GLU   B HB2  1 
ATOM   15608 H  HB3  . GLU   B  2  430 ? 33.802  -5.052  22.191   1.00 121.85 ? 434  GLU   B HB3  1 
ATOM   15609 H  HG2  . GLU   B  2  430 ? 31.252  -5.023  22.231   1.00 123.48 ? 434  GLU   B HG2  1 
ATOM   15610 H  HG3  . GLU   B  2  430 ? 31.533  -6.579  22.391   1.00 123.48 ? 434  GLU   B HG3  1 
ATOM   15611 N  N    . CYS   B  2  431 ? 34.071  -3.274  18.900   1.00 112.03 ? 435  CYS   B N    1 
ATOM   15612 C  CA   . CYS   B  2  431 ? 35.207  -2.619  18.268   1.00 119.31 ? 435  CYS   B CA   1 
ATOM   15613 C  C    . CYS   B  2  431 ? 35.253  -1.138  18.629   1.00 121.37 ? 435  CYS   B C    1 
ATOM   15614 O  O    . CYS   B  2  431 ? 35.723  -0.311  17.844   1.00 123.96 ? 435  CYS   B O    1 
ATOM   15615 C  CB   . CYS   B  2  431 ? 35.169  -2.817  16.753   1.00 124.56 ? 435  CYS   B CB   1 
ATOM   15616 S  SG   . CYS   B  2  431 ? 34.047  -1.749  15.828   1.00 133.16 ? 435  CYS   B SG   1 
ATOM   15617 H  H    . CYS   B  2  431 ? 33.311  -2.945  18.666   1.00 134.47 ? 435  CYS   B H    1 
ATOM   15618 H  HA   . CYS   B  2  431 ? 36.027  -3.023  18.593   1.00 143.21 ? 435  CYS   B HA   1 
ATOM   15619 H  HB2  . CYS   B  2  431 ? 36.062  -2.660  16.407   1.00 149.50 ? 435  CYS   B HB2  1 
ATOM   15620 H  HB3  . CYS   B  2  431 ? 34.901  -3.733  16.577   1.00 149.50 ? 435  CYS   B HB3  1 
ATOM   15621 N  N    . ASN   B  2  432 ? 34.772  -0.796  19.823   1.00 117.34 ? 436  ASN   B N    1 
ATOM   15622 C  CA   . ASN   B  2  432 ? 34.874  0.548   20.369   1.00 118.74 ? 436  ASN   B CA   1 
ATOM   15623 C  C    . ASN   B  2  432 ? 35.626  0.507   21.693   1.00 117.07 ? 436  ASN   B C    1 
ATOM   15624 O  O    . ASN   B  2  432 ? 35.725  -0.536  22.346   1.00 114.57 ? 436  ASN   B O    1 
ATOM   15625 C  CB   . ASN   B  2  432 ? 33.489  1.175   20.578   1.00 121.66 ? 436  ASN   B CB   1 
ATOM   15626 C  CG   . ASN   B  2  432 ? 32.764  1.438   19.273   1.00 122.25 ? 436  ASN   B CG   1 
ATOM   15627 O  OD1  . ASN   B  2  432 ? 33.313  2.049   18.357   1.00 123.94 ? 436  ASN   B OD1  1 
ATOM   15628 N  ND2  . ASN   B  2  432 ? 31.524  0.970   19.181   1.00 121.54 ? 436  ASN   B ND2  1 
ATOM   15629 H  H    . ASN   B  2  432 ? 34.371  -1.345  20.348   1.00 140.85 ? 436  ASN   B H    1 
ATOM   15630 H  HA   . ASN   B  2  432 ? 35.368  1.109   19.751   1.00 142.53 ? 436  ASN   B HA   1 
ATOM   15631 H  HB2  . ASN   B  2  432 ? 32.944  0.571   21.107   1.00 146.03 ? 436  ASN   B HB2  1 
ATOM   15632 H  HB3  . ASN   B  2  432 ? 33.591  2.021   21.040   1.00 146.03 ? 436  ASN   B HB3  1 
ATOM   15633 H  HD21 . ASN   B  2  432 ? 31.071  1.093   18.460   1.00 145.89 ? 436  ASN   B HD21 1 
ATOM   15634 H  HD22 . ASN   B  2  432 ? 31.175  0.544   19.841   1.00 145.89 ? 436  ASN   B HD22 1 
ATOM   15635 N  N    . CYS   B  2  433 ? 36.159  1.662   22.081   1.00 118.43 ? 437  CYS   B N    1 
ATOM   15636 C  CA   . CYS   B  2  433 ? 36.868  1.822   23.341   1.00 121.30 ? 437  CYS   B CA   1 
ATOM   15637 C  C    . CYS   B  2  433 ? 35.988  2.562   24.342   1.00 130.58 ? 437  CYS   B C    1 
ATOM   15638 O  O    . CYS   B  2  433 ? 35.110  3.342   23.966   1.00 135.82 ? 437  CYS   B O    1 
ATOM   15639 C  CB   . CYS   B  2  433 ? 38.178  2.590   23.141   1.00 120.92 ? 437  CYS   B CB   1 
ATOM   15640 S  SG   . CYS   B  2  433 ? 39.309  1.876   21.918   1.00 117.15 ? 437  CYS   B SG   1 
ATOM   15641 H  H    . CYS   B  2  433 ? 36.122  2.385   21.617   1.00 142.16 ? 437  CYS   B H    1 
ATOM   15642 H  HA   . CYS   B  2  433 ? 37.084  0.948   23.703   1.00 145.60 ? 437  CYS   B HA   1 
ATOM   15643 H  HB2  . CYS   B  2  433 ? 37.963  3.489   22.848   1.00 145.14 ? 437  CYS   B HB2  1 
ATOM   15644 H  HB3  . CYS   B  2  433 ? 38.648  2.620   23.989   1.00 145.14 ? 437  CYS   B HB3  1 
ATOM   15645 N  N    . ASP   B  2  434 ? 36.234  2.309   25.631   1.00 135.11 ? 438  ASP   B N    1 
ATOM   15646 C  CA   . ASP   B  2  434 ? 35.492  3.019   26.668   1.00 140.73 ? 438  ASP   B CA   1 
ATOM   15647 C  C    . ASP   B  2  434 ? 35.750  4.520   26.600   1.00 147.54 ? 438  ASP   B C    1 
ATOM   15648 O  O    . ASP   B  2  434 ? 34.837  5.325   26.820   1.00 156.28 ? 438  ASP   B O    1 
ATOM   15649 C  CB   . ASP   B  2  434 ? 35.866  2.484   28.052   1.00 140.72 ? 438  ASP   B CB   1 
ATOM   15650 C  CG   . ASP   B  2  434 ? 34.840  1.509   28.603   1.00 141.66 ? 438  ASP   B CG   1 
ATOM   15651 O  OD1  . ASP   B  2  434 ? 34.027  0.980   27.816   1.00 141.54 ? 438  ASP   B OD1  1 
ATOM   15652 O  OD2  . ASP   B  2  434 ? 34.842  1.281   29.832   1.00 144.10 ? 438  ASP   B OD2  1 
ATOM   15653 H  H    . ASP   B  2  434 ? 36.812  1.744   25.923   1.00 162.17 ? 438  ASP   B H    1 
ATOM   15654 H  HA   . ASP   B  2  434 ? 34.545  2.863   26.530   1.00 168.91 ? 438  ASP   B HA   1 
ATOM   15655 H  HB2  . ASP   B  2  434 ? 36.716  2.021   27.993   1.00 168.91 ? 438  ASP   B HB2  1 
ATOM   15656 H  HB3  . ASP   B  2  434 ? 35.935  3.228   28.671   1.00 168.91 ? 438  ASP   B HB3  1 
ATOM   15657 N  N    . CYS   B  2  435 ? 36.986  4.915   26.293   1.00 147.33 ? 439  CYS   B N    1 
ATOM   15658 C  CA   . CYS   B  2  435 ? 37.363  6.322   26.308   1.00 151.55 ? 439  CYS   B CA   1 
ATOM   15659 C  C    . CYS   B  2  435 ? 36.828  7.102   25.115   1.00 160.25 ? 439  CYS   B C    1 
ATOM   15660 O  O    . CYS   B  2  435 ? 36.899  8.336   25.124   1.00 169.47 ? 439  CYS   B O    1 
ATOM   15661 C  CB   . CYS   B  2  435 ? 38.888  6.454   26.352   1.00 145.59 ? 439  CYS   B CB   1 
ATOM   15662 S  SG   . CYS   B  2  435 ? 39.721  5.757   24.912   1.00 139.06 ? 439  CYS   B SG   1 
ATOM   15663 H  H    . CYS   B  2  435 ? 37.625  4.383   26.072   1.00 176.83 ? 439  CYS   B H    1 
ATOM   15664 H  HA   . CYS   B  2  435 ? 36.999  6.726   27.111   1.00 181.89 ? 439  CYS   B HA   1 
ATOM   15665 H  HB2  . CYS   B  2  435 ? 39.118  7.395   26.400   1.00 174.75 ? 439  CYS   B HB2  1 
ATOM   15666 H  HB3  . CYS   B  2  435 ? 39.218  5.991   27.138   1.00 174.75 ? 439  CYS   B HB3  1 
ATOM   15667 N  N    . GLN   B  2  436 ? 36.302  6.428   24.091   1.00 154.08 ? 440  GLN   B N    1 
ATOM   15668 C  CA   . GLN   B  2  436 ? 35.771  7.155   22.944   1.00 155.51 ? 440  GLN   B CA   1 
ATOM   15669 C  C    . GLN   B  2  436 ? 34.563  8.000   23.325   1.00 158.69 ? 440  GLN   B C    1 
ATOM   15670 O  O    . GLN   B  2  436 ? 34.358  9.080   22.758   1.00 162.96 ? 440  GLN   B O    1 
ATOM   15671 C  CB   . GLN   B  2  436 ? 35.402  6.183   21.824   1.00 154.40 ? 440  GLN   B CB   1 
ATOM   15672 C  CG   . GLN   B  2  436 ? 36.584  5.759   20.975   1.00 153.29 ? 440  GLN   B CG   1 
ATOM   15673 C  CD   . GLN   B  2  436 ? 36.163  5.104   19.678   1.00 150.65 ? 440  GLN   B CD   1 
ATOM   15674 O  OE1  . GLN   B  2  436 ? 36.640  5.471   18.606   1.00 150.28 ? 440  GLN   B OE1  1 
ATOM   15675 N  NE2  . GLN   B  2  436 ? 35.265  4.130   19.767   1.00 148.70 ? 440  GLN   B NE2  1 
ATOM   15676 H  H    . GLN   B  2  436 ? 36.244  5.572   24.038   1.00 184.93 ? 440  GLN   B H    1 
ATOM   15677 H  HA   . GLN   B  2  436 ? 36.461  7.750   22.610   1.00 186.65 ? 440  GLN   B HA   1 
ATOM   15678 H  HB2  . GLN   B  2  436 ? 35.017  5.385   22.218   1.00 185.31 ? 440  GLN   B HB2  1 
ATOM   15679 H  HB3  . GLN   B  2  436 ? 34.755  6.610   21.241   1.00 185.31 ? 440  GLN   B HB3  1 
ATOM   15680 H  HG2  . GLN   B  2  436 ? 37.115  6.541   20.758   1.00 183.98 ? 440  GLN   B HG2  1 
ATOM   15681 H  HG3  . GLN   B  2  436 ? 37.120  5.122   21.474   1.00 183.98 ? 440  GLN   B HG3  1 
ATOM   15682 H  HE21 . GLN   B  2  436 ? 34.953  3.901   20.536   1.00 178.48 ? 440  GLN   B HE21 1 
ATOM   15683 H  HE22 . GLN   B  2  436 ? 34.995  3.727   19.057   1.00 178.48 ? 440  GLN   B HE22 1 
ATOM   15684 N  N    . LYS   B  2  437 ? 33.758  7.538   24.284   1.00 158.11 ? 441  LYS   B N    1 
ATOM   15685 C  CA   . LYS   B  2  437 ? 32.535  8.260   24.617   1.00 162.60 ? 441  LYS   B CA   1 
ATOM   15686 C  C    . LYS   B  2  437 ? 32.824  9.571   25.340   1.00 169.55 ? 441  LYS   B C    1 
ATOM   15687 O  O    . LYS   B  2  437 ? 32.094  10.550  25.151   1.00 170.96 ? 441  LYS   B O    1 
ATOM   15688 C  CB   . LYS   B  2  437 ? 31.614  7.377   25.465   1.00 161.66 ? 441  LYS   B CB   1 
ATOM   15689 C  CG   . LYS   B  2  437 ? 31.018  6.161   24.734   1.00 159.03 ? 441  LYS   B CG   1 
ATOM   15690 C  CD   . LYS   B  2  437 ? 30.705  6.435   23.260   1.00 159.16 ? 441  LYS   B CD   1 
ATOM   15691 C  CE   . LYS   B  2  437 ? 29.756  7.618   23.070   1.00 163.59 ? 441  LYS   B CE   1 
ATOM   15692 N  NZ   . LYS   B  2  437 ? 30.013  8.322   21.781   1.00 163.85 ? 441  LYS   B NZ   1 
ATOM   15693 H  H    . LYS   B  2  437 ? 33.895  6.825   24.745   1.00 189.77 ? 441  LYS   B H    1 
ATOM   15694 H  HA   . LYS   B  2  437 ? 32.071  8.473   23.793   1.00 195.16 ? 441  LYS   B HA   1 
ATOM   15695 H  HB2  . LYS   B  2  437 ? 32.122  7.041   26.220   1.00 194.03 ? 441  LYS   B HB2  1 
ATOM   15696 H  HB3  . LYS   B  2  437 ? 30.874  7.919   25.778   1.00 194.03 ? 441  LYS   B HB3  1 
ATOM   15697 H  HG2  . LYS   B  2  437 ? 31.652  5.429   24.773   1.00 190.87 ? 441  LYS   B HG2  1 
ATOM   15698 H  HG3  . LYS   B  2  437 ? 30.190  5.907   25.172   1.00 190.87 ? 441  LYS   B HG3  1 
ATOM   15699 H  HD2  . LYS   B  2  437 ? 31.531  6.636   22.793   1.00 191.03 ? 441  LYS   B HD2  1 
ATOM   15700 H  HD3  . LYS   B  2  437 ? 30.287  5.650   22.873   1.00 191.03 ? 441  LYS   B HD3  1 
ATOM   15701 H  HE2  . LYS   B  2  437 ? 28.840  7.297   23.065   1.00 196.35 ? 441  LYS   B HE2  1 
ATOM   15702 H  HE3  . LYS   B  2  437 ? 29.882  8.251   23.794   1.00 196.35 ? 441  LYS   B HE3  1 
ATOM   15703 H  HZ1  . LYS   B  2  437 ? 29.522  9.063   21.736   1.00 196.65 ? 441  LYS   B HZ1  1 
ATOM   15704 H  HZ2  . LYS   B  2  437 ? 30.874  8.541   21.721   1.00 196.65 ? 441  LYS   B HZ2  1 
ATOM   15705 H  HZ3  . LYS   B  2  437 ? 29.801  7.793   21.098   1.00 196.65 ? 441  LYS   B HZ3  1 
ATOM   15706 N  N    . GLU   B  2  438 ? 33.876  9.619   26.159   1.00 154.73 ? 442  GLU   B N    1 
ATOM   15707 C  CA   . GLU   B  2  438 ? 34.213  10.826  26.917   1.00 157.56 ? 442  GLU   B CA   1 
ATOM   15708 C  C    . GLU   B  2  438 ? 35.023  11.756  26.014   1.00 158.62 ? 442  GLU   B C    1 
ATOM   15709 O  O    . GLU   B  2  438 ? 36.254  11.831  26.068   1.00 168.69 ? 442  GLU   B O    1 
ATOM   15710 C  CB   . GLU   B  2  438 ? 34.959  10.462  28.195   1.00 156.41 ? 442  GLU   B CB   1 
ATOM   15711 C  CG   . GLU   B  2  438 ? 36.304  9.785   27.971   1.00 150.01 ? 442  GLU   B CG   1 
ATOM   15712 C  CD   . GLU   B  2  438 ? 36.759  8.962   29.161   1.00 146.82 ? 442  GLU   B CD   1 
ATOM   15713 O  OE1  . GLU   B  2  438 ? 35.999  8.856   30.145   1.00 148.11 ? 442  GLU   B OE1  1 
ATOM   15714 O  OE2  . GLU   B  2  438 ? 37.882  8.419   29.108   1.00 144.39 ? 442  GLU   B OE2  1 
ATOM   15715 H  H    . GLU   B  2  438 ? 34.413  8.962   26.294   1.00 185.72 ? 442  GLU   B H    1 
ATOM   15716 H  HA   . GLU   B  2  438 ? 33.398  11.290  27.167   1.00 189.10 ? 442  GLU   B HA   1 
ATOM   15717 H  HB2  . GLU   B  2  438 ? 35.121  11.274  28.700   1.00 187.72 ? 442  GLU   B HB2  1 
ATOM   15718 H  HB3  . GLU   B  2  438 ? 34.408  9.854   28.712   1.00 187.72 ? 442  GLU   B HB3  1 
ATOM   15719 H  HG2  . GLU   B  2  438 ? 36.234  9.191   27.207   1.00 180.05 ? 442  GLU   B HG2  1 
ATOM   15720 H  HG3  . GLU   B  2  438 ? 36.975  10.464  27.803   1.00 180.05 ? 442  GLU   B HG3  1 
ATOM   15721 N  N    . VAL   B  2  439 ? 34.296  12.496  25.170   1.00 149.06 ? 443  VAL   B N    1 
ATOM   15722 C  CA   . VAL   B  2  439 ? 34.938  13.319  24.148   1.00 153.20 ? 443  VAL   B CA   1 
ATOM   15723 C  C    . VAL   B  2  439 ? 35.649  14.523  24.759   1.00 156.07 ? 443  VAL   B C    1 
ATOM   15724 O  O    . VAL   B  2  439 ? 36.730  14.906  24.305   1.00 160.01 ? 443  VAL   B O    1 
ATOM   15725 C  CB   . VAL   B  2  439 ? 33.919  13.781  23.086   1.00 153.00 ? 443  VAL   B CB   1 
ATOM   15726 C  CG1  . VAL   B  2  439 ? 33.618  12.663  22.106   1.00 153.65 ? 443  VAL   B CG1  1 
ATOM   15727 C  CG2  . VAL   B  2  439 ? 32.639  14.318  23.737   1.00 154.76 ? 443  VAL   B CG2  1 
ATOM   15728 H  H    . VAL   B  2  439 ? 33.437  12.538  25.170   1.00 178.91 ? 443  VAL   B H    1 
ATOM   15729 H  HA   . VAL   B  2  439 ? 35.603  12.759  23.718   1.00 183.87 ? 443  VAL   B HA   1 
ATOM   15730 H  HB   . VAL   B  2  439 ? 34.311  14.512  22.584   1.00 183.64 ? 443  VAL   B HB   1 
ATOM   15731 H  HG11 . VAL   B  2  439 ? 33.075  13.015  21.382   1.00 184.42 ? 443  VAL   B HG11 1 
ATOM   15732 H  HG12 . VAL   B  2  439 ? 34.453  12.317  21.755   1.00 184.42 ? 443  VAL   B HG12 1 
ATOM   15733 H  HG13 . VAL   B  2  439 ? 33.136  11.959  22.568   1.00 184.42 ? 443  VAL   B HG13 1 
ATOM   15734 H  HG21 . VAL   B  2  439 ? 31.984  14.499  23.044   1.00 185.74 ? 443  VAL   B HG21 1 
ATOM   15735 H  HG22 . VAL   B  2  439 ? 32.294  13.652  24.352   1.00 185.74 ? 443  VAL   B HG22 1 
ATOM   15736 H  HG23 . VAL   B  2  439 ? 32.848  15.135  24.217   1.00 185.74 ? 443  VAL   B HG23 1 
ATOM   15737 N  N    . GLU   B  2  440 ? 35.040  15.178  25.743   1.00 148.34 ? 444  GLU   B N    1 
ATOM   15738 C  CA   . GLU   B  2  440 ? 35.610  16.395  26.324   1.00 143.46 ? 444  GLU   B CA   1 
ATOM   15739 C  C    . GLU   B  2  440 ? 35.967  17.401  25.226   1.00 134.92 ? 444  GLU   B C    1 
ATOM   15740 O  O    . GLU   B  2  440 ? 37.121  17.798  25.048   1.00 131.72 ? 444  GLU   B O    1 
ATOM   15741 C  CB   . GLU   B  2  440 ? 36.835  16.062  27.184   1.00 146.22 ? 444  GLU   B CB   1 
ATOM   15742 C  CG   . GLU   B  2  440 ? 36.489  15.495  28.554   1.00 148.02 ? 444  GLU   B CG   1 
ATOM   15743 C  CD   . GLU   B  2  440 ? 37.558  14.567  29.098   1.00 146.13 ? 444  GLU   B CD   1 
ATOM   15744 O  OE1  . GLU   B  2  440 ? 38.289  14.974  30.026   1.00 147.09 ? 444  GLU   B OE1  1 
ATOM   15745 O  OE2  . GLU   B  2  440 ? 37.669  13.429  28.595   1.00 143.66 ? 444  GLU   B OE2  1 
ATOM   15746 H  H    . GLU   B  2  440 ? 34.292  14.938  26.094   1.00 178.04 ? 444  GLU   B H    1 
ATOM   15747 H  HA   . GLU   B  2  440 ? 34.943  16.805  26.896   1.00 172.18 ? 444  GLU   B HA   1 
ATOM   15748 H  HB2  . GLU   B  2  440 ? 37.373  15.403  26.719   1.00 175.50 ? 444  GLU   B HB2  1 
ATOM   15749 H  HB3  . GLU   B  2  440 ? 37.349  16.873  27.321   1.00 175.50 ? 444  GLU   B HB3  1 
ATOM   15750 H  HG2  . GLU   B  2  440 ? 36.382  16.227  29.180   1.00 177.66 ? 444  GLU   B HG2  1 
ATOM   15751 H  HG3  . GLU   B  2  440 ? 35.662  14.992  28.487   1.00 177.66 ? 444  GLU   B HG3  1 
ATOM   15752 N  N    . VAL   B  2  441 ? 34.934  17.818  24.487   1.00 127.32 ? 445  VAL   B N    1 
ATOM   15753 C  CA   . VAL   B  2  441 ? 35.132  18.649  23.303   1.00 123.35 ? 445  VAL   B CA   1 
ATOM   15754 C  C    . VAL   B  2  441 ? 35.670  20.023  23.698   1.00 119.74 ? 445  VAL   B C    1 
ATOM   15755 O  O    . VAL   B  2  441 ? 35.447  20.516  24.812   1.00 119.82 ? 445  VAL   B O    1 
ATOM   15756 C  CB   . VAL   B  2  441 ? 33.820  18.783  22.504   1.00 124.66 ? 445  VAL   B CB   1 
ATOM   15757 C  CG1  . VAL   B  2  441 ? 34.109  19.239  21.077   1.00 122.89 ? 445  VAL   B CG1  1 
ATOM   15758 C  CG2  . VAL   B  2  441 ? 33.028  17.470  22.500   1.00 126.01 ? 445  VAL   B CG2  1 
ATOM   15759 H  H    . VAL   B  2  441 ? 34.110  17.632  24.652   1.00 152.83 ? 445  VAL   B H    1 
ATOM   15760 H  HA   . VAL   B  2  441 ? 35.793  18.218  22.739   1.00 148.06 ? 445  VAL   B HA   1 
ATOM   15761 H  HB   . VAL   B  2  441 ? 33.269  19.455  22.936   1.00 149.63 ? 445  VAL   B HB   1 
ATOM   15762 H  HG11 . VAL   B  2  441 ? 33.338  19.044  20.521   1.00 147.50 ? 445  VAL   B HG11 1 
ATOM   15763 H  HG12 . VAL   B  2  441 ? 34.282  20.193  21.079   1.00 147.50 ? 445  VAL   B HG12 1 
ATOM   15764 H  HG13 . VAL   B  2  441 ? 34.885  18.762  20.744   1.00 147.50 ? 445  VAL   B HG13 1 
ATOM   15765 H  HG21 . VAL   B  2  441 ? 32.311  17.535  21.850   1.00 151.25 ? 445  VAL   B HG21 1 
ATOM   15766 H  HG22 . VAL   B  2  441 ? 33.624  16.742  22.263   1.00 151.25 ? 445  VAL   B HG22 1 
ATOM   15767 H  HG23 . VAL   B  2  441 ? 32.659  17.320  23.385   1.00 151.25 ? 445  VAL   B HG23 1 
ATOM   15768 N  N    . ASN   B  2  442 ? 36.390  20.650  22.764   1.00 117.41 ? 446  ASN   B N    1 
ATOM   15769 C  CA   . ASN   B  2  442 ? 36.987  21.975  22.961   1.00 114.66 ? 446  ASN   B CA   1 
ATOM   15770 C  C    . ASN   B  2  442 ? 37.864  22.007  24.210   1.00 118.04 ? 446  ASN   B C    1 
ATOM   15771 O  O    . ASN   B  2  442 ? 37.820  22.949  25.004   1.00 121.71 ? 446  ASN   B O    1 
ATOM   15772 C  CB   . ASN   B  2  442 ? 35.916  23.069  23.019   1.00 112.46 ? 446  ASN   B CB   1 
ATOM   15773 C  CG   . ASN   B  2  442 ? 35.127  23.178  21.725   1.00 111.46 ? 446  ASN   B CG   1 
ATOM   15774 O  OD1  . ASN   B  2  442 ? 35.527  22.633  20.693   1.00 111.32 ? 446  ASN   B OD1  1 
ATOM   15775 N  ND2  . ASN   B  2  442 ? 34.006  23.890  21.772   1.00 113.24 ? 446  ASN   B ND2  1 
ATOM   15776 H  H    . ASN   B  2  442 ? 36.551  20.320  21.987   1.00 140.92 ? 446  ASN   B H    1 
ATOM   15777 H  HA   . ASN   B  2  442 ? 37.557  22.159  22.198   1.00 137.62 ? 446  ASN   B HA   1 
ATOM   15778 H  HB2  . ASN   B  2  442 ? 35.294  22.866  23.735   1.00 134.98 ? 446  ASN   B HB2  1 
ATOM   15779 H  HB3  . ASN   B  2  442 ? 36.344  23.924  23.184   1.00 134.98 ? 446  ASN   B HB3  1 
ATOM   15780 H  HD21 . ASN   B  2  442 ? 33.524  23.981  21.065   1.00 135.92 ? 446  ASN   B HD21 1 
ATOM   15781 H  HD22 . ASN   B  2  442 ? 33.762  24.260  22.509   1.00 135.92 ? 446  ASN   B HD22 1 
ATOM   15782 N  N    . SER   B  2  443 ? 38.678  20.967  24.375   1.00 120.01 ? 447  SER   B N    1 
ATOM   15783 C  CA   . SER   B  2  443 ? 39.593  20.890  25.502   1.00 124.77 ? 447  SER   B CA   1 
ATOM   15784 C  C    . SER   B  2  443 ? 40.736  21.886  25.342   1.00 127.93 ? 447  SER   B C    1 
ATOM   15785 O  O    . SER   B  2  443 ? 41.115  22.263  24.229   1.00 127.04 ? 447  SER   B O    1 
ATOM   15786 C  CB   . SER   B  2  443 ? 40.154  19.474  25.630   1.00 126.01 ? 447  SER   B CB   1 
ATOM   15787 O  OG   . SER   B  2  443 ? 41.292  19.297  24.804   1.00 126.76 ? 447  SER   B OG   1 
ATOM   15788 H  H    . SER   B  2  443 ? 38.719  20.291  23.844   1.00 144.05 ? 447  SER   B H    1 
ATOM   15789 H  HA   . SER   B  2  443 ? 39.116  21.106  26.319   1.00 149.76 ? 447  SER   B HA   1 
ATOM   15790 H  HB2  . SER   B  2  443 ? 40.408  19.319  26.554   1.00 151.25 ? 447  SER   B HB2  1 
ATOM   15791 H  HB3  . SER   B  2  443 ? 39.470  18.839  25.364   1.00 151.25 ? 447  SER   B HB3  1 
ATOM   15792 H  HG   . SER   B  2  443 ? 41.053  19.079  24.029   1.00 152.15 ? 447  SER   B HG   1 
ATOM   15793 N  N    . SER   B  2  444 ? 41.292  22.312  26.477   1.00 131.75 ? 448  SER   B N    1 
ATOM   15794 C  CA   . SER   B  2  444 ? 42.442  23.207  26.442   1.00 134.57 ? 448  SER   B CA   1 
ATOM   15795 C  C    . SER   B  2  444 ? 43.632  22.536  25.770   1.00 135.10 ? 448  SER   B C    1 
ATOM   15796 O  O    . SER   B  2  444 ? 44.399  23.180  25.045   1.00 138.48 ? 448  SER   B O    1 
ATOM   15797 C  CB   . SER   B  2  444 ? 42.813  23.633  27.861   1.00 138.33 ? 448  SER   B CB   1 
ATOM   15798 O  OG   . SER   B  2  444 ? 43.539  22.606  28.519   1.00 140.09 ? 448  SER   B OG   1 
ATOM   15799 H  H    . SER   B  2  444 ? 41.025  22.100  27.267   1.00 158.14 ? 448  SER   B H    1 
ATOM   15800 H  HA   . SER   B  2  444 ? 42.209  24.001  25.935   1.00 161.52 ? 448  SER   B HA   1 
ATOM   15801 H  HB2  . SER   B  2  444 ? 43.362  24.431  27.818   1.00 166.03 ? 448  SER   B HB2  1 
ATOM   15802 H  HB3  . SER   B  2  444 ? 42.001  23.815  28.359   1.00 166.03 ? 448  SER   B HB3  1 
ATOM   15803 H  HG   . SER   B  2  444 ? 43.060  22.250  29.110   1.00 168.14 ? 448  SER   B HG   1 
ATOM   15804 N  N    . LYS   B  2  445 ? 43.791  21.232  26.004   1.00 135.05 ? 449  LYS   B N    1 
ATOM   15805 C  CA   . LYS   B  2  445 ? 44.944  20.486  25.509   1.00 133.08 ? 449  LYS   B CA   1 
ATOM   15806 C  C    . LYS   B  2  445 ? 45.113  20.575  23.995   1.00 128.82 ? 449  LYS   B C    1 
ATOM   15807 O  O    . LYS   B  2  445 ? 46.242  20.472  23.500   1.00 128.91 ? 449  LYS   B O    1 
ATOM   15808 C  CB   . LYS   B  2  445 ? 44.802  19.029  25.946   1.00 132.24 ? 449  LYS   B CB   1 
ATOM   15809 C  CG   . LYS   B  2  445 ? 44.818  18.862  27.458   1.00 135.07 ? 449  LYS   B CG   1 
ATOM   15810 C  CD   . LYS   B  2  445 ? 44.236  17.529  27.893   1.00 133.47 ? 449  LYS   B CD   1 
ATOM   15811 C  CE   . LYS   B  2  445 ? 43.155  17.715  28.955   1.00 131.47 ? 449  LYS   B CE   1 
ATOM   15812 N  NZ   . LYS   B  2  445 ? 42.937  16.479  29.759   1.00 128.77 ? 449  LYS   B NZ   1 
ATOM   15813 H  H    . LYS   B  2  445 ? 43.238  20.751  26.453   1.00 162.10 ? 449  LYS   B H    1 
ATOM   15814 H  HA   . LYS   B  2  445 ? 45.749  20.865  25.895   1.00 159.73 ? 449  LYS   B HA   1 
ATOM   15815 H  HB2  . LYS   B  2  445 ? 43.959  18.681  25.615   1.00 158.72 ? 449  LYS   B HB2  1 
ATOM   15816 H  HB3  . LYS   B  2  445 ? 45.539  18.516  25.580   1.00 158.72 ? 449  LYS   B HB3  1 
ATOM   15817 H  HG2  . LYS   B  2  445 ? 45.733  18.909  27.774   1.00 162.12 ? 449  LYS   B HG2  1 
ATOM   15818 H  HG3  . LYS   B  2  445 ? 44.290  19.568  27.862   1.00 162.12 ? 449  LYS   B HG3  1 
ATOM   15819 H  HD2  . LYS   B  2  445 ? 43.838  17.085  27.128   1.00 160.20 ? 449  LYS   B HD2  1 
ATOM   15820 H  HD3  . LYS   B  2  445 ? 44.940  16.977  28.268   1.00 160.20 ? 449  LYS   B HD3  1 
ATOM   15821 H  HE2  . LYS   B  2  445 ? 43.421  18.426  29.559   1.00 157.80 ? 449  LYS   B HE2  1 
ATOM   15822 H  HE3  . LYS   B  2  445 ? 42.318  17.945  28.521   1.00 157.80 ? 449  LYS   B HE3  1 
ATOM   15823 H  HZ1  . LYS   B  2  445 ? 42.834  16.689  30.618   1.00 154.56 ? 449  LYS   B HZ1  1 
ATOM   15824 H  HZ2  . LYS   B  2  445 ? 42.208  16.056  29.476   1.00 154.56 ? 449  LYS   B HZ2  1 
ATOM   15825 H  HZ3  . LYS   B  2  445 ? 43.637  15.935  29.677   1.00 154.56 ? 449  LYS   B HZ3  1 
ATOM   15826 N  N    . CYS   B  2  446 ? 44.031  20.744  23.241   1.00 121.78 ? 450  CYS   B N    1 
ATOM   15827 C  CA   . CYS   B  2  446 ? 44.134  20.827  21.781   1.00 117.94 ? 450  CYS   B CA   1 
ATOM   15828 C  C    . CYS   B  2  446 ? 44.152  22.291  21.341   1.00 117.96 ? 450  CYS   B C    1 
ATOM   15829 O  O    . CYS   B  2  446 ? 43.265  22.795  20.650   1.00 118.21 ? 450  CYS   B O    1 
ATOM   15830 C  CB   . CYS   B  2  446 ? 43.004  20.040  21.119   1.00 113.83 ? 450  CYS   B CB   1 
ATOM   15831 S  SG   . CYS   B  2  446 ? 42.830  18.340  21.738   1.00 110.72 ? 450  CYS   B SG   1 
ATOM   15832 H  H    . CYS   B  2  446 ? 43.230  20.814  23.546   1.00 146.17 ? 450  CYS   B H    1 
ATOM   15833 H  HA   . CYS   B  2  446 ? 44.968  20.420  21.499   1.00 141.56 ? 450  CYS   B HA   1 
ATOM   15834 H  HB2  . CYS   B  2  446 ? 42.167  20.501  21.281   1.00 136.64 ? 450  CYS   B HB2  1 
ATOM   15835 H  HB3  . CYS   B  2  446 ? 43.177  19.991  20.165   1.00 136.64 ? 450  CYS   B HB3  1 
ATOM   15836 N  N    . HIS   B  2  447 ? 45.216  22.971  21.773   1.00 118.85 ? 451  HIS   B N    1 
ATOM   15837 C  CA   . HIS   B  2  447 ? 45.497  24.359  21.424   1.00 120.01 ? 451  HIS   B CA   1 
ATOM   15838 C  C    . HIS   B  2  447 ? 44.280  25.261  21.583   1.00 119.78 ? 451  HIS   B C    1 
ATOM   15839 O  O    . HIS   B  2  447 ? 43.618  25.608  20.599   1.00 119.10 ? 451  HIS   B O    1 
ATOM   15840 C  CB   . HIS   B  2  447 ? 46.029  24.452  19.991   1.00 119.44 ? 451  HIS   B CB   1 
ATOM   15841 C  CG   . HIS   B  2  447 ? 46.853  25.676  19.734   1.00 124.21 ? 451  HIS   B CG   1 
ATOM   15842 N  ND1  . HIS   B  2  447 ? 46.575  26.563  18.716   1.00 124.72 ? 451  HIS   B ND1  1 
ATOM   15843 C  CD2  . HIS   B  2  447 ? 47.944  26.164  20.371   1.00 127.56 ? 451  HIS   B CD2  1 
ATOM   15844 C  CE1  . HIS   B  2  447 ? 47.464  27.541  18.733   1.00 128.10 ? 451  HIS   B CE1  1 
ATOM   15845 N  NE2  . HIS   B  2  447 ? 48.305  27.323  19.728   1.00 129.92 ? 451  HIS   B NE2  1 
ATOM   15846 H  H    . HIS   B  2  447 ? 45.814  22.634  22.291   1.00 142.66 ? 451  HIS   B H    1 
ATOM   15847 H  HA   . HIS   B  2  447 ? 46.175  24.683  22.037   1.00 144.05 ? 451  HIS   B HA   1 
ATOM   15848 H  HB2  . HIS   B  2  447 ? 46.586  23.678  19.813   1.00 143.37 ? 451  HIS   B HB2  1 
ATOM   15849 H  HB3  . HIS   B  2  447 ? 45.277  24.467  19.378   1.00 143.37 ? 451  HIS   B HB3  1 
ATOM   15850 H  HD2  . HIS   B  2  447 ? 48.370  25.785  21.105   1.00 153.10 ? 451  HIS   B HD2  1 
ATOM   15851 H  HE1  . HIS   B  2  447 ? 47.492  28.261  18.145   1.00 153.76 ? 451  HIS   B HE1  1 
ATOM   15852 H  HE2  . HIS   B  2  447 ? 48.970  27.825  19.939   1.00 155.94 ? 451  HIS   B HE2  1 
ATOM   15853 N  N    . HIS   B  2  448 ? 43.986  25.651  22.821   1.00 120.52 ? 452  HIS   B N    1 
ATOM   15854 C  CA   . HIS   B  2  448 ? 42.978  26.668  23.107   1.00 122.47 ? 452  HIS   B CA   1 
ATOM   15855 C  C    . HIS   B  2  448 ? 41.636  26.321  22.464   1.00 118.25 ? 452  HIS   B C    1 
ATOM   15856 O  O    . HIS   B  2  448 ? 40.977  27.157  21.842   1.00 120.78 ? 452  HIS   B O    1 
ATOM   15857 C  CB   . HIS   B  2  448 ? 43.470  28.042  22.651   1.00 126.00 ? 452  HIS   B CB   1 
ATOM   15858 C  CG   . HIS   B  2  448 ? 44.820  28.408  23.187   1.00 126.55 ? 452  HIS   B CG   1 
ATOM   15859 N  ND1  . HIS   B  2  448 ? 45.073  28.546  24.535   1.00 128.84 ? 452  HIS   B ND1  1 
ATOM   15860 C  CD2  . HIS   B  2  448 ? 45.985  28.690  22.555   1.00 126.97 ? 452  HIS   B CD2  1 
ATOM   15861 C  CE1  . HIS   B  2  448 ? 46.338  28.885  24.711   1.00 131.44 ? 452  HIS   B CE1  1 
ATOM   15862 N  NE2  . HIS   B  2  448 ? 46.913  28.980  23.525   1.00 130.93 ? 452  HIS   B NE2  1 
ATOM   15863 H  H    . HIS   B  2  448 ? 44.363  25.334  23.525   1.00 144.66 ? 452  HIS   B H    1 
ATOM   15864 H  HA   . HIS   B  2  448 ? 42.832  26.696  24.066   1.00 147.00 ? 452  HIS   B HA   1 
ATOM   15865 H  HB2  . HIS   B  2  448 ? 43.525  28.047  21.682   1.00 151.23 ? 452  HIS   B HB2  1 
ATOM   15866 H  HB3  . HIS   B  2  448 ? 42.840  28.714  22.951   1.00 151.23 ? 452  HIS   B HB3  1 
ATOM   15867 H  HD2  . HIS   B  2  448 ? 46.129  28.687  21.636   1.00 152.40 ? 452  HIS   B HD2  1 
ATOM   15868 H  HE1  . HIS   B  2  448 ? 46.753  29.032  25.530   1.00 157.77 ? 452  HIS   B HE1  1 
ATOM   15869 H  HE2  . HIS   B  2  448 ? 47.734  29.191  23.384   1.00 157.15 ? 452  HIS   B HE2  1 
ATOM   15870 N  N    . GLY   B  2  449 ? 41.233  25.062  22.619   1.00 113.25 ? 453  GLY   B N    1 
ATOM   15871 C  CA   . GLY   B  2  449 ? 39.929  24.627  22.157   1.00 109.44 ? 453  GLY   B CA   1 
ATOM   15872 C  C    . GLY   B  2  449 ? 39.820  24.341  20.676   1.00 109.55 ? 453  GLY   B C    1 
ATOM   15873 O  O    . GLY   B  2  449 ? 38.724  24.441  20.115   1.00 108.38 ? 453  GLY   B O    1 
ATOM   15874 H  H    . GLY   B  2  449 ? 41.700  24.442  22.990   1.00 135.94 ? 453  GLY   B H    1 
ATOM   15875 H  HA2  . GLY   B  2  449 ? 39.690  23.815  22.630   1.00 131.36 ? 453  GLY   B HA2  1 
ATOM   15876 H  HA3  . GLY   B  2  449 ? 39.282  25.318  22.370   1.00 131.36 ? 453  GLY   B HA3  1 
ATOM   15877 N  N    . ASN   B  2  450 ? 40.922  23.978  20.021   1.00 111.11 ? 454  ASN   B N    1 
ATOM   15878 C  CA   . ASN   B  2  450 ? 40.928  23.716  18.586   1.00 113.94 ? 454  ASN   B CA   1 
ATOM   15879 C  C    . ASN   B  2  450 ? 40.721  22.243  18.245   1.00 119.23 ? 454  ASN   B C    1 
ATOM   15880 O  O    . ASN   B  2  450 ? 40.883  21.856  17.084   1.00 124.20 ? 454  ASN   B O    1 
ATOM   15881 C  CB   . ASN   B  2  450 ? 42.240  24.209  17.970   1.00 111.21 ? 454  ASN   B CB   1 
ATOM   15882 C  CG   . ASN   B  2  450 ? 42.122  25.606  17.392   1.00 107.02 ? 454  ASN   B CG   1 
ATOM   15883 O  OD1  . ASN   B  2  450 ? 41.082  25.981  16.852   1.00 105.49 ? 454  ASN   B OD1  1 
ATOM   15884 N  ND2  . ASN   B  2  450 ? 43.192  26.382  17.500   1.00 107.13 ? 454  ASN   B ND2  1 
ATOM   15885 H  H    . ASN   B  2  450 ? 41.690  23.875  20.394   1.00 133.37 ? 454  ASN   B H    1 
ATOM   15886 H  HA   . ASN   B  2  450 ? 40.200  24.214  18.183   1.00 136.76 ? 454  ASN   B HA   1 
ATOM   15887 H  HB2  . ASN   B  2  450 ? 42.926  24.224  18.656   1.00 133.49 ? 454  ASN   B HB2  1 
ATOM   15888 H  HB3  . ASN   B  2  450 ? 42.500  23.608  17.254   1.00 133.49 ? 454  ASN   B HB3  1 
ATOM   15889 H  HD21 . ASN   B  2  450 ? 43.175  27.183  17.188   1.00 128.59 ? 454  ASN   B HD21 1 
ATOM   15890 H  HD22 . ASN   B  2  450 ? 43.902  26.085  17.883   1.00 128.59 ? 454  ASN   B HD22 1 
ATOM   15891 N  N    . GLY   B  2  451 ? 40.361  21.426  19.223   1.00 120.97 ? 455  GLY   B N    1 
ATOM   15892 C  CA   . GLY   B  2  451 ? 40.082  20.029  18.980   1.00 119.69 ? 455  GLY   B CA   1 
ATOM   15893 C  C    . GLY   B  2  451 ? 39.405  19.446  20.195   1.00 121.32 ? 455  GLY   B C    1 
ATOM   15894 O  O    . GLY   B  2  451 ? 39.080  20.159  21.146   1.00 124.37 ? 455  GLY   B O    1 
ATOM   15895 H  H    . GLY   B  2  451 ? 40.271  21.662  20.045   1.00 145.21 ? 455  GLY   B H    1 
ATOM   15896 H  HA2  . GLY   B  2  451 ? 39.498  19.933  18.212   1.00 143.67 ? 455  GLY   B HA2  1 
ATOM   15897 H  HA3  . GLY   B  2  451 ? 40.907  19.547  18.812   1.00 143.67 ? 455  GLY   B HA3  1 
ATOM   15898 N  N    . SER   B  2  452 ? 39.198  18.135  20.158   1.00 117.27 ? 456  SER   B N    1 
ATOM   15899 C  CA   . SER   B  2  452 ? 38.575  17.412  21.258   1.00 119.72 ? 456  SER   B CA   1 
ATOM   15900 C  C    . SER   B  2  452 ? 39.550  16.379  21.795   1.00 120.14 ? 456  SER   B C    1 
ATOM   15901 O  O    . SER   B  2  452 ? 40.132  15.605  21.026   1.00 119.07 ? 456  SER   B O    1 
ATOM   15902 C  CB   . SER   B  2  452 ? 37.275  16.733  20.822   1.00 122.22 ? 456  SER   B CB   1 
ATOM   15903 O  OG   . SER   B  2  452 ? 37.278  16.456  19.435   1.00 121.86 ? 456  SER   B OG   1 
ATOM   15904 H  H    . SER   B  2  452 ? 39.414  17.633  19.493   1.00 140.75 ? 456  SER   B H    1 
ATOM   15905 H  HA   . SER   B  2  452 ? 38.364  18.038  21.969   1.00 143.70 ? 456  SER   B HA   1 
ATOM   15906 H  HB2  . SER   B  2  452 ? 37.179  15.899  21.308   1.00 146.70 ? 456  SER   B HB2  1 
ATOM   15907 H  HB3  . SER   B  2  452 ? 36.531  17.321  21.023   1.00 146.70 ? 456  SER   B HB3  1 
ATOM   15908 H  HG   . SER   B  2  452 ? 36.988  15.681  19.296   1.00 146.27 ? 456  SER   B HG   1 
ATOM   15909 N  N    . PHE   B  2  453 ? 39.729  16.374  23.110   1.00 120.18 ? 457  PHE   B N    1 
ATOM   15910 C  CA   . PHE   B  2  453 ? 40.567  15.373  23.760   1.00 118.78 ? 457  PHE   B CA   1 
ATOM   15911 C  C    . PHE   B  2  453 ? 39.767  14.091  23.902   1.00 119.63 ? 457  PHE   B C    1 
ATOM   15912 O  O    . PHE   B  2  453 ? 38.829  14.026  24.700   1.00 120.43 ? 457  PHE   B O    1 
ATOM   15913 C  CB   . PHE   B  2  453 ? 41.031  15.850  25.128   1.00 117.78 ? 457  PHE   B CB   1 
ATOM   15914 C  CG   . PHE   B  2  453 ? 42.242  15.128  25.639   1.00 116.19 ? 457  PHE   B CG   1 
ATOM   15915 C  CD1  . PHE   B  2  453 ? 43.419  15.139  24.913   1.00 114.20 ? 457  PHE   B CD1  1 
ATOM   15916 C  CD2  . PHE   B  2  453 ? 42.212  14.457  26.850   1.00 116.46 ? 457  PHE   B CD2  1 
ATOM   15917 C  CE1  . PHE   B  2  453 ? 44.535  14.490  25.378   1.00 114.38 ? 457  PHE   B CE1  1 
ATOM   15918 C  CE2  . PHE   B  2  453 ? 43.330  13.807  27.319   1.00 116.96 ? 457  PHE   B CE2  1 
ATOM   15919 C  CZ   . PHE   B  2  453 ? 44.491  13.833  26.587   1.00 116.04 ? 457  PHE   B CZ   1 
ATOM   15920 H  H    . PHE   B  2  453 ? 39.376  16.943  23.650   1.00 144.25 ? 457  PHE   B H    1 
ATOM   15921 H  HA   . PHE   B  2  453 ? 41.348  15.213  23.207   1.00 142.58 ? 457  PHE   B HA   1 
ATOM   15922 H  HB2  . PHE   B  2  453 ? 41.250  16.793  25.071   1.00 141.37 ? 457  PHE   B HB2  1 
ATOM   15923 H  HB3  . PHE   B  2  453 ? 40.313  15.713  25.766   1.00 141.37 ? 457  PHE   B HB3  1 
ATOM   15924 H  HD1  . PHE   B  2  453 ? 43.455  15.591  24.101   1.00 137.08 ? 457  PHE   B HD1  1 
ATOM   15925 H  HD2  . PHE   B  2  453 ? 41.429  14.446  27.352   1.00 139.79 ? 457  PHE   B HD2  1 
ATOM   15926 H  HE1  . PHE   B  2  453 ? 45.319  14.493  24.877   1.00 137.29 ? 457  PHE   B HE1  1 
ATOM   15927 H  HE2  . PHE   B  2  453 ? 43.299  13.351  28.129   1.00 140.38 ? 457  PHE   B HE2  1 
ATOM   15928 H  HZ   . PHE   B  2  453 ? 45.251  13.406  26.910   1.00 139.29 ? 457  PHE   B HZ   1 
ATOM   15929 N  N    . GLN   B  2  454 ? 40.139  13.056  23.154   1.00 121.96 ? 458  GLN   B N    1 
ATOM   15930 C  CA   . GLN   B  2  454 ? 39.327  11.848  23.123   1.00 121.41 ? 458  GLN   B CA   1 
ATOM   15931 C  C    . GLN   B  2  454 ? 39.923  10.737  23.983   1.00 132.38 ? 458  GLN   B C    1 
ATOM   15932 O  O    . GLN   B  2  454 ? 39.281  10.294  24.937   1.00 123.65 ? 458  GLN   B O    1 
ATOM   15933 C  CB   . GLN   B  2  454 ? 39.122  11.381  21.677   1.00 122.31 ? 458  GLN   B CB   1 
ATOM   15934 C  CG   . GLN   B  2  454 ? 38.245  10.141  21.546   1.00 123.25 ? 458  GLN   B CG   1 
ATOM   15935 C  CD   . GLN   B  2  454 ? 37.559  10.066  20.195   1.00 124.90 ? 458  GLN   B CD   1 
ATOM   15936 O  OE1  . GLN   B  2  454 ? 37.860  10.834  19.288   1.00 124.34 ? 458  GLN   B OE1  1 
ATOM   15937 N  NE2  . GLN   B  2  454 ? 36.601  9.170   20.074   1.00 128.26 ? 458  GLN   B NE2  1 
ATOM   15938 H  H    . GLN   B  2  454 ? 40.847  13.032  22.666   1.00 146.39 ? 458  GLN   B H    1 
ATOM   15939 H  HA   . GLN   B  2  454 ? 38.451  12.056  23.485   1.00 145.73 ? 458  GLN   B HA   1 
ATOM   15940 H  HB2  . GLN   B  2  454 ? 38.700  12.096  21.176   1.00 146.81 ? 458  GLN   B HB2  1 
ATOM   15941 H  HB3  . GLN   B  2  454 ? 39.988  11.172  21.292   1.00 146.81 ? 458  GLN   B HB3  1 
ATOM   15942 H  HG2  . GLN   B  2  454 ? 38.795  9.349   21.650   1.00 147.94 ? 458  GLN   B HG2  1 
ATOM   15943 H  HG3  . GLN   B  2  454 ? 37.560  10.162  22.232   1.00 147.94 ? 458  GLN   B HG3  1 
ATOM   15944 H  HE21 . GLN   B  2  454 ? 36.396  8.667   20.740   1.00 153.95 ? 458  GLN   B HE21 1 
ATOM   15945 H  HE22 . GLN   B  2  454 ? 36.181  9.088   19.328   1.00 153.95 ? 458  GLN   B HE22 1 
ATOM   15946 N  N    . CYS   B  2  455 ? 41.139  10.289  23.681   1.00 146.39 ? 459  CYS   B N    1 
ATOM   15947 C  CA   . CYS   B  2  455 ? 41.763  9.203   24.432   1.00 163.40 ? 459  CYS   B CA   1 
ATOM   15948 C  C    . CYS   B  2  455 ? 43.252  9.457   24.612   1.00 144.76 ? 459  CYS   B C    1 
ATOM   15949 O  O    . CYS   B  2  455 ? 44.074  8.549   24.457   1.00 94.17  ? 459  CYS   B O    1 
ATOM   15950 C  CB   . CYS   B  2  455 ? 41.550  7.859   23.736   1.00 174.92 ? 459  CYS   B CB   1 
ATOM   15951 S  SG   . CYS   B  2  455 ? 39.836  7.305   23.603   1.00 158.15 ? 459  CYS   B SG   1 
ATOM   15952 H  H    . CYS   B  2  455 ? 41.625  10.600  23.042   1.00 175.70 ? 459  CYS   B H    1 
ATOM   15953 H  HA   . CYS   B  2  455 ? 41.351  9.172   25.310   1.00 196.12 ? 459  CYS   B HA   1 
ATOM   15954 H  HB2  . CYS   B  2  455 ? 41.901  7.926   22.834   1.00 209.94 ? 459  CYS   B HB2  1 
ATOM   15955 H  HB3  . CYS   B  2  455 ? 42.034  7.180   24.231   1.00 209.94 ? 459  CYS   B HB3  1 
ATOM   15956 N  N    . GLY   B  2  456 ? 43.628  10.685  24.949   1.00 127.25 ? 460  GLY   B N    1 
ATOM   15957 C  CA   . GLY   B  2  456 ? 45.032  11.029  25.019   1.00 123.25 ? 460  GLY   B CA   1 
ATOM   15958 C  C    . GLY   B  2  456 ? 45.603  11.571  23.730   1.00 121.26 ? 460  GLY   B C    1 
ATOM   15959 O  O    . GLY   B  2  456 ? 46.785  11.938  23.696   1.00 126.49 ? 460  GLY   B O    1 
ATOM   15960 H  H    . GLY   B  2  456 ? 43.090  11.328  25.139   1.00 152.74 ? 460  GLY   B H    1 
ATOM   15961 H  HA2  . GLY   B  2  456 ? 45.155  11.702  25.706   1.00 147.94 ? 460  GLY   B HA2  1 
ATOM   15962 H  HA3  . GLY   B  2  456 ? 45.537  10.236  25.259   1.00 147.94 ? 460  GLY   B HA3  1 
ATOM   15963 N  N    . VAL   B  2  457 ? 44.800  11.628  22.671   1.00 115.20 ? 461  VAL   B N    1 
ATOM   15964 C  CA   . VAL   B  2  457 ? 45.190  12.177  21.381   1.00 113.14 ? 461  VAL   B CA   1 
ATOM   15965 C  C    . VAL   B  2  457 ? 44.116  13.176  20.978   1.00 112.88 ? 461  VAL   B C    1 
ATOM   15966 O  O    . VAL   B  2  457 ? 42.951  13.047  21.367   1.00 113.00 ? 461  VAL   B O    1 
ATOM   15967 C  CB   . VAL   B  2  457 ? 45.354  11.065  20.322   1.00 109.51 ? 461  VAL   B CB   1 
ATOM   15968 C  CG1  . VAL   B  2  457 ? 45.815  11.640  18.994   1.00 107.73 ? 461  VAL   B CG1  1 
ATOM   15969 C  CG2  . VAL   B  2  457 ? 46.324  10.000  20.822   1.00 110.16 ? 461  VAL   B CG2  1 
ATOM   15970 H  H    . VAL   B  2  457 ? 43.990  11.342  22.678   1.00 138.27 ? 461  VAL   B H    1 
ATOM   15971 H  HA   . VAL   B  2  457 ? 46.039  12.643  21.446   1.00 135.81 ? 461  VAL   B HA   1 
ATOM   15972 H  HB   . VAL   B  2  457 ? 44.492  10.646  20.173   1.00 131.45 ? 461  VAL   B HB   1 
ATOM   15973 H  HG11 . VAL   B  2  457 ? 46.027  10.911  18.390   1.00 129.31 ? 461  VAL   B HG11 1 
ATOM   15974 H  HG12 . VAL   B  2  457 ? 45.103  12.183  18.620   1.00 129.31 ? 461  VAL   B HG12 1 
ATOM   15975 H  HG13 . VAL   B  2  457 ? 46.603  12.185  19.143   1.00 129.31 ? 461  VAL   B HG13 1 
ATOM   15976 H  HG21 . VAL   B  2  457 ? 46.609  9.455   20.072   1.00 132.23 ? 461  VAL   B HG21 1 
ATOM   15977 H  HG22 . VAL   B  2  457 ? 47.091  10.435  21.225   1.00 132.23 ? 461  VAL   B HG22 1 
ATOM   15978 H  HG23 . VAL   B  2  457 ? 45.874  9.447   21.480   1.00 132.23 ? 461  VAL   B HG23 1 
ATOM   15979 N  N    . CYS   B  2  458 ? 44.508  14.186  20.207   1.00 110.18 ? 462  CYS   B N    1 
ATOM   15980 C  CA   . CYS   B  2  458 ? 43.589  15.255  19.839   1.00 106.74 ? 462  CYS   B CA   1 
ATOM   15981 C  C    . CYS   B  2  458 ? 42.895  14.937  18.521   1.00 108.15 ? 462  CYS   B C    1 
ATOM   15982 O  O    . CYS   B  2  458 ? 43.552  14.646  17.516   1.00 109.15 ? 462  CYS   B O    1 
ATOM   15983 C  CB   . CYS   B  2  458 ? 44.319  16.595  19.732   1.00 105.17 ? 462  CYS   B CB   1 
ATOM   15984 S  SG   . CYS   B  2  458 ? 44.600  17.429  21.316   1.00 107.39 ? 462  CYS   B SG   1 
ATOM   15985 H  H    . CYS   B  2  458 ? 45.301  14.274  19.886   1.00 132.25 ? 462  CYS   B H    1 
ATOM   15986 H  HA   . CYS   B  2  458 ? 42.912  15.328  20.529   1.00 128.13 ? 462  CYS   B HA   1 
ATOM   15987 H  HB2  . CYS   B  2  458 ? 45.186  16.443  19.324   1.00 126.24 ? 462  CYS   B HB2  1 
ATOM   15988 H  HB3  . CYS   B  2  458 ? 43.792  17.191  19.177   1.00 126.24 ? 462  CYS   B HB3  1 
ATOM   15989 N  N    . ALA   B  2  459 ? 41.566  14.987  18.539   1.00 109.60 ? 463  ALA   B N    1 
ATOM   15990 C  CA   . ALA   B  2  459 ? 40.755  14.948  17.324   1.00 109.78 ? 463  ALA   B CA   1 
ATOM   15991 C  C    . ALA   B  2  459 ? 40.557  16.391  16.880   1.00 110.49 ? 463  ALA   B C    1 
ATOM   15992 O  O    . ALA   B  2  459 ? 39.706  17.106  17.415   1.00 110.70 ? 463  ALA   B O    1 
ATOM   15993 C  CB   . ALA   B  2  459 ? 39.426  14.250  17.580   1.00 111.72 ? 463  ALA   B CB   1 
ATOM   15994 H  H    . ALA   B  2  459 ? 41.099  15.045  19.259   1.00 131.55 ? 463  ALA   B H    1 
ATOM   15995 H  HA   . ALA   B  2  459 ? 41.218  14.456  16.628   1.00 131.77 ? 463  ALA   B HA   1 
ATOM   15996 H  HB1  . ALA   B  2  459 ? 38.916  14.230  16.755   1.00 134.10 ? 463  ALA   B HB1  1 
ATOM   15997 H  HB2  . ALA   B  2  459 ? 39.598  13.345  17.885   1.00 134.10 ? 463  ALA   B HB2  1 
ATOM   15998 H  HB3  . ALA   B  2  459 ? 38.937  14.741  18.259   1.00 134.10 ? 463  ALA   B HB3  1 
ATOM   15999 N  N    . CYS   B  2  460 ? 41.348  16.828  15.904   1.00 113.11 ? 464  CYS   B N    1 
ATOM   16000 C  CA   . CYS   B  2  460 ? 41.360  18.236  15.543   1.00 119.23 ? 464  CYS   B CA   1 
ATOM   16001 C  C    . CYS   B  2  460 ? 40.066  18.638  14.844   1.00 120.31 ? 464  CYS   B C    1 
ATOM   16002 O  O    . CYS   B  2  460 ? 39.398  17.826  14.197   1.00 121.71 ? 464  CYS   B O    1 
ATOM   16003 C  CB   . CYS   B  2  460 ? 42.555  18.552  14.642   1.00 124.76 ? 464  CYS   B CB   1 
ATOM   16004 S  SG   . CYS   B  2  460 ? 44.165  18.376  15.454   1.00 127.43 ? 464  CYS   B SG   1 
ATOM   16005 H  H    . CYS   B  2  460 ? 41.880  16.333  15.443   1.00 135.77 ? 464  CYS   B H    1 
ATOM   16006 H  HA   . CYS   B  2  460 ? 41.440  18.766  16.352   1.00 143.12 ? 464  CYS   B HA   1 
ATOM   16007 H  HB2  . CYS   B  2  460 ? 42.540  17.947  13.884   1.00 149.74 ? 464  CYS   B HB2  1 
ATOM   16008 H  HB3  . CYS   B  2  460 ? 42.478  19.469  14.337   1.00 149.74 ? 464  CYS   B HB3  1 
ATOM   16009 N  N    . HIS   B  2  461 ? 39.715  19.910  14.995   1.00 118.20 ? 465  HIS   B N    1 
ATOM   16010 C  CA   . HIS   B  2  461 ? 38.591  20.493  14.288   1.00 118.02 ? 465  HIS   B CA   1 
ATOM   16011 C  C    . HIS   B  2  461 ? 38.964  20.738  12.830   1.00 119.27 ? 465  HIS   B C    1 
ATOM   16012 O  O    . HIS   B  2  461 ? 40.147  20.800  12.485   1.00 119.68 ? 465  HIS   B O    1 
ATOM   16013 C  CB   . HIS   B  2  461 ? 38.178  21.804  14.949   1.00 117.16 ? 465  HIS   B CB   1 
ATOM   16014 C  CG   . HIS   B  2  461 ? 37.459  21.628  16.251   1.00 114.54 ? 465  HIS   B CG   1 
ATOM   16015 N  ND1  . HIS   B  2  461 ? 36.959  20.413  16.668   1.00 113.09 ? 465  HIS   B ND1  1 
ATOM   16016 C  CD2  . HIS   B  2  461 ? 37.153  22.515  17.227   1.00 114.48 ? 465  HIS   B CD2  1 
ATOM   16017 C  CE1  . HIS   B  2  461 ? 36.377  20.558  17.844   1.00 113.23 ? 465  HIS   B CE1  1 
ATOM   16018 N  NE2  . HIS   B  2  461 ? 36.481  21.824  18.206   1.00 114.43 ? 465  HIS   B NE2  1 
ATOM   16019 H  H    . HIS   B  2  461 ? 40.121  20.464  15.513   1.00 141.87 ? 465  HIS   B H    1 
ATOM   16020 H  HA   . HIS   B  2  461 ? 37.831  19.891  14.317   1.00 141.66 ? 465  HIS   B HA   1 
ATOM   16021 H  HB2  . HIS   B  2  461 ? 38.975  22.330  15.121   1.00 140.63 ? 465  HIS   B HB2  1 
ATOM   16022 H  HB3  . HIS   B  2  461 ? 37.587  22.284  14.348   1.00 140.63 ? 465  HIS   B HB3  1 
ATOM   16023 H  HD2  . HIS   B  2  461 ? 37.359  23.422  17.234   1.00 137.41 ? 465  HIS   B HD2  1 
ATOM   16024 H  HE1  . HIS   B  2  461 ? 35.964  19.884  18.335   1.00 135.91 ? 465  HIS   B HE1  1 
ATOM   16025 H  HE2  . HIS   B  2  461 ? 36.177  22.162  18.937   1.00 137.35 ? 465  HIS   B HE2  1 
ATOM   16026 N  N    . PRO   B  2  462 ? 37.976  20.877  11.948   1.00 118.85 ? 466  PRO   B N    1 
ATOM   16027 C  CA   . PRO   B  2  462 ? 38.293  21.190  10.550   1.00 119.39 ? 466  PRO   B CA   1 
ATOM   16028 C  C    . PRO   B  2  462 ? 39.085  22.484  10.443   1.00 119.11 ? 466  PRO   B C    1 
ATOM   16029 O  O    . PRO   B  2  462 ? 38.806  23.467  11.134   1.00 115.24 ? 466  PRO   B O    1 
ATOM   16030 C  CB   . PRO   B  2  462 ? 36.916  21.306  9.881    1.00 121.29 ? 466  PRO   B CB   1 
ATOM   16031 C  CG   . PRO   B  2  462 ? 35.926  21.413  10.997   1.00 120.50 ? 466  PRO   B CG   1 
ATOM   16032 C  CD   . PRO   B  2  462 ? 36.529  20.700  12.162   1.00 118.60 ? 466  PRO   B CD   1 
ATOM   16033 H  HA   . PRO   B  2  462 ? 38.790  20.466  10.138   1.00 143.31 ? 466  PRO   B HA   1 
ATOM   16034 H  HB2  . PRO   B  2  462 ? 36.891  22.097  9.322    1.00 145.58 ? 466  PRO   B HB2  1 
ATOM   16035 H  HB3  . PRO   B  2  462 ? 36.746  20.515  9.346    1.00 145.58 ? 466  PRO   B HB3  1 
ATOM   16036 H  HG2  . PRO   B  2  462 ? 35.775  22.348  11.209   1.00 144.64 ? 466  PRO   B HG2  1 
ATOM   16037 H  HG3  . PRO   B  2  462 ? 35.092  20.994  10.733   1.00 144.64 ? 466  PRO   B HG3  1 
ATOM   16038 H  HD2  . PRO   B  2  462 ? 36.250  21.106  12.998   1.00 142.35 ? 466  PRO   B HD2  1 
ATOM   16039 H  HD3  . PRO   B  2  462 ? 36.290  19.760  12.154   1.00 142.35 ? 466  PRO   B HD3  1 
ATOM   16040 N  N    . GLY   B  2  463 ? 40.092  22.471  9.573    1.00 120.56 ? 467  GLY   B N    1 
ATOM   16041 C  CA   . GLY   B  2  463 ? 40.938  23.626  9.360    1.00 124.20 ? 467  GLY   B CA   1 
ATOM   16042 C  C    . GLY   B  2  463 ? 42.134  23.736  10.278   1.00 121.12 ? 467  GLY   B C    1 
ATOM   16043 O  O    . GLY   B  2  463 ? 42.810  24.772  10.260   1.00 126.33 ? 467  GLY   B O    1 
ATOM   16044 H  H    . GLY   B  2  463 ? 40.304  21.792  9.090    1.00 144.71 ? 467  GLY   B H    1 
ATOM   16045 H  HA2  . GLY   B  2  463 ? 41.269  23.600  8.449    1.00 149.08 ? 467  GLY   B HA2  1 
ATOM   16046 H  HA3  . GLY   B  2  463 ? 40.402  24.426  9.479    1.00 149.08 ? 467  GLY   B HA3  1 
ATOM   16047 N  N    . HIS   B  2  464 ? 42.422  22.710  11.078   1.00 111.73 ? 468  HIS   B N    1 
ATOM   16048 C  CA   . HIS   B  2  464 ? 43.548  22.725  12.002   1.00 110.91 ? 468  HIS   B CA   1 
ATOM   16049 C  C    . HIS   B  2  464 ? 44.319  21.417  11.896   1.00 112.45 ? 468  HIS   B C    1 
ATOM   16050 O  O    . HIS   B  2  464 ? 43.726  20.351  11.703   1.00 111.82 ? 468  HIS   B O    1 
ATOM   16051 C  CB   . HIS   B  2  464 ? 43.078  22.946  13.445   1.00 106.80 ? 468  HIS   B CB   1 
ATOM   16052 C  CG   . HIS   B  2  464 ? 42.580  24.333  13.712   1.00 108.24 ? 468  HIS   B CG   1 
ATOM   16053 N  ND1  . HIS   B  2  464 ? 41.275  24.712  13.487   1.00 108.52 ? 468  HIS   B ND1  1 
ATOM   16054 C  CD2  . HIS   B  2  464 ? 43.217  25.433  14.178   1.00 109.82 ? 468  HIS   B CD2  1 
ATOM   16055 C  CE1  . HIS   B  2  464 ? 41.127  25.986  13.807   1.00 109.99 ? 468  HIS   B CE1  1 
ATOM   16056 N  NE2  . HIS   B  2  464 ? 42.291  26.446  14.229   1.00 110.63 ? 468  HIS   B NE2  1 
ATOM   16057 H  H    . HIS   B  2  464 ? 41.969  21.980  11.102   1.00 134.11 ? 468  HIS   B H    1 
ATOM   16058 H  HA   . HIS   B  2  464 ? 44.153  23.446  11.765   1.00 133.12 ? 468  HIS   B HA   1 
ATOM   16059 H  HB2  . HIS   B  2  464 ? 42.354  22.330  13.635   1.00 128.20 ? 468  HIS   B HB2  1 
ATOM   16060 H  HB3  . HIS   B  2  464 ? 43.822  22.778  14.045   1.00 128.20 ? 468  HIS   B HB3  1 
ATOM   16061 H  HD2  . HIS   B  2  464 ? 44.113  25.492  14.419   1.00 131.83 ? 468  HIS   B HD2  1 
ATOM   16062 H  HE1  . HIS   B  2  464 ? 40.338  26.474  13.746   1.00 132.03 ? 468  HIS   B HE1  1 
ATOM   16063 H  HE2  . HIS   B  2  464 ? 42.444  27.250  14.493   1.00 132.79 ? 468  HIS   B HE2  1 
ATOM   16064 N  N    . MET   B  2  465 ? 45.643  21.505  12.029   1.00 114.63 ? 469  MET   B N    1 
ATOM   16065 C  CA   . MET   B  2  465 ? 46.529  20.362  11.864   1.00 115.62 ? 469  MET   B CA   1 
ATOM   16066 C  C    . MET   B  2  465 ? 47.550  20.329  12.995   1.00 112.64 ? 469  MET   B C    1 
ATOM   16067 O  O    . MET   B  2  465 ? 47.831  21.343  13.638   1.00 112.13 ? 469  MET   B O    1 
ATOM   16068 C  CB   . MET   B  2  465 ? 47.256  20.413  10.509   1.00 121.42 ? 469  MET   B CB   1 
ATOM   16069 C  CG   . MET   B  2  465 ? 46.330  20.400  9.296    1.00 124.84 ? 469  MET   B CG   1 
ATOM   16070 S  SD   . MET   B  2  465 ? 47.220  20.537  7.731    1.00 132.44 ? 469  MET   B SD   1 
ATOM   16071 C  CE   . MET   B  2  465 ? 45.960  20.028  6.561    1.00 136.04 ? 469  MET   B CE   1 
ATOM   16072 H  H    . MET   B  2  465 ? 46.057  22.234  12.219   1.00 137.59 ? 469  MET   B H    1 
ATOM   16073 H  HA   . MET   B  2  465 ? 46.003  19.548  11.899   1.00 138.78 ? 469  MET   B HA   1 
ATOM   16074 H  HB2  . MET   B  2  465 ? 47.780  21.228  10.469   1.00 145.74 ? 469  MET   B HB2  1 
ATOM   16075 H  HB3  . MET   B  2  465 ? 47.838  19.640  10.441   1.00 145.74 ? 469  MET   B HB3  1 
ATOM   16076 H  HG2  . MET   B  2  465 ? 45.833  19.567  9.286    1.00 149.85 ? 469  MET   B HG2  1 
ATOM   16077 H  HG3  . MET   B  2  465 ? 45.717  21.150  9.359    1.00 149.85 ? 469  MET   B HG3  1 
ATOM   16078 H  HE1  . MET   B  2  465 ? 46.230  20.297  5.669    1.00 163.28 ? 469  MET   B HE1  1 
ATOM   16079 H  HE2  . MET   B  2  465 ? 45.862  19.064  6.601    1.00 163.28 ? 469  MET   B HE2  1 
ATOM   16080 H  HE3  . MET   B  2  465 ? 45.121  20.455  6.795    1.00 163.28 ? 469  MET   B HE3  1 
ATOM   16081 N  N    . GLY   B  2  466 ? 48.104  19.138  13.231   1.00 110.03 ? 470  GLY   B N    1 
ATOM   16082 C  CA   . GLY   B  2  466 ? 49.127  18.946  14.234   1.00 108.84 ? 470  GLY   B CA   1 
ATOM   16083 C  C    . GLY   B  2  466 ? 48.681  18.012  15.342   1.00 105.20 ? 470  GLY   B C    1 
ATOM   16084 O  O    . GLY   B  2  466 ? 47.490  17.721  15.491   1.00 99.94  ? 470  GLY   B O    1 
ATOM   16085 H  H    . GLY   B  2  466 ? 47.895  18.418  12.809   1.00 132.08 ? 470  GLY   B H    1 
ATOM   16086 H  HA2  . GLY   B  2  466 ? 49.919  18.570  13.818   1.00 130.64 ? 470  GLY   B HA2  1 
ATOM   16087 H  HA3  . GLY   B  2  466 ? 49.354  19.803  14.629   1.00 130.64 ? 470  GLY   B HA3  1 
ATOM   16088 N  N    . PRO   B  2  467 ? 49.630  17.519  16.149   1.00 109.06 ? 471  PRO   B N    1 
ATOM   16089 C  CA   . PRO   B  2  467 ? 49.236  16.623  17.249   1.00 108.49 ? 471  PRO   B CA   1 
ATOM   16090 C  C    . PRO   B  2  467 ? 48.305  17.285  18.249   1.00 108.72 ? 471  PRO   B C    1 
ATOM   16091 O  O    . PRO   B  2  467 ? 47.339  16.657  18.697   1.00 109.02 ? 471  PRO   B O    1 
ATOM   16092 C  CB   . PRO   B  2  467 ? 50.576  16.234  17.893   1.00 112.12 ? 471  PRO   B CB   1 
ATOM   16093 C  CG   . PRO   B  2  467 ? 51.622  16.576  16.890   1.00 115.40 ? 471  PRO   B CG   1 
ATOM   16094 C  CD   . PRO   B  2  467 ? 51.087  17.733  16.105   1.00 113.80 ? 471  PRO   B CD   1 
ATOM   16095 H  HA   . PRO   B  2  467 ? 48.815  15.827  16.887   1.00 130.22 ? 471  PRO   B HA   1 
ATOM   16096 H  HB2  . PRO   B  2  467 ? 50.705  16.740  18.711   1.00 134.58 ? 471  PRO   B HB2  1 
ATOM   16097 H  HB3  . PRO   B  2  467 ? 50.583  15.284  18.087   1.00 134.58 ? 471  PRO   B HB3  1 
ATOM   16098 H  HG2  . PRO   B  2  467 ? 52.442  16.822  17.346   1.00 138.52 ? 471  PRO   B HG2  1 
ATOM   16099 H  HG3  . PRO   B  2  467 ? 51.780  15.814  16.311   1.00 138.52 ? 471  PRO   B HG3  1 
ATOM   16100 H  HD2  . PRO   B  2  467 ? 51.325  18.575  16.524   1.00 136.60 ? 471  PRO   B HD2  1 
ATOM   16101 H  HD3  . PRO   B  2  467 ? 51.412  17.712  15.192   1.00 136.60 ? 471  PRO   B HD3  1 
ATOM   16102 N  N    . ARG   B  2  468 ? 48.577  18.536  18.618   1.00 109.75 ? 472  ARG   B N    1 
ATOM   16103 C  CA   . ARG   B  2  468 ? 47.723  19.301  19.516   1.00 111.25 ? 472  ARG   B CA   1 
ATOM   16104 C  C    . ARG   B  2  468 ? 46.869  20.325  18.771   1.00 113.04 ? 472  ARG   B C    1 
ATOM   16105 O  O    . ARG   B  2  468 ? 46.267  21.196  19.406   1.00 112.05 ? 472  ARG   B O    1 
ATOM   16106 C  CB   . ARG   B  2  468 ? 48.576  19.990  20.588   1.00 113.18 ? 472  ARG   B CB   1 
ATOM   16107 C  CG   . ARG   B  2  468 ? 48.750  19.180  21.880   1.00 114.77 ? 472  ARG   B CG   1 
ATOM   16108 C  CD   . ARG   B  2  468 ? 49.782  19.813  22.816   1.00 120.66 ? 472  ARG   B CD   1 
ATOM   16109 N  NE   . ARG   B  2  468 ? 50.375  18.841  23.735   1.00 122.67 ? 472  ARG   B NE   1 
ATOM   16110 C  CZ   . ARG   B  2  468 ? 51.428  19.085  24.513   1.00 125.79 ? 472  ARG   B CZ   1 
ATOM   16111 N  NH1  . ARG   B  2  468 ? 52.016  20.274  24.491   1.00 128.80 ? 472  ARG   B NH1  1 
ATOM   16112 N  NH2  . ARG   B  2  468 ? 51.896  18.138  25.314   1.00 123.83 ? 472  ARG   B NH2  1 
ATOM   16113 H  H    . ARG   B  2  468 ? 49.269  18.972  18.353   1.00 131.73 ? 472  ARG   B H    1 
ATOM   16114 H  HA   . ARG   B  2  468 ? 47.119  18.693  19.970   1.00 133.54 ? 472  ARG   B HA   1 
ATOM   16115 H  HB2  . ARG   B  2  468 ? 49.460  20.153  20.223   1.00 135.86 ? 472  ARG   B HB2  1 
ATOM   16116 H  HB3  . ARG   B  2  468 ? 48.154  20.831  20.825   1.00 135.86 ? 472  ARG   B HB3  1 
ATOM   16117 H  HG2  . ARG   B  2  468 ? 47.902  19.138  22.348   1.00 137.76 ? 472  ARG   B HG2  1 
ATOM   16118 H  HG3  . ARG   B  2  468 ? 49.051  18.285  21.657   1.00 137.76 ? 472  ARG   B HG3  1 
ATOM   16119 H  HD2  . ARG   B  2  468 ? 50.497  20.199  22.286   1.00 144.83 ? 472  ARG   B HD2  1 
ATOM   16120 H  HD3  . ARG   B  2  468 ? 49.351  20.502  23.344   1.00 144.83 ? 472  ARG   B HD3  1 
ATOM   16121 H  HE   . ARG   B  2  468 ? 50.020  18.058  23.775   1.00 147.24 ? 472  ARG   B HE   1 
ATOM   16122 H  HH11 . ARG   B  2  468 ? 51.719  20.892  23.972   1.00 154.59 ? 472  ARG   B HH11 1 
ATOM   16123 H  HH12 . ARG   B  2  468 ? 52.696  20.427  24.995   1.00 154.59 ? 472  ARG   B HH12 1 
ATOM   16124 H  HH21 . ARG   B  2  468 ? 51.520  17.364  25.331   1.00 148.63 ? 472  ARG   B HH21 1 
ATOM   16125 H  HH22 . ARG   B  2  468 ? 52.576  18.297  25.817   1.00 148.63 ? 472  ARG   B HH22 1 
ATOM   16126 N  N    . CYS   B  2  469 ? 46.806  20.237  17.437   1.00 116.93 ? 473  CYS   B N    1 
ATOM   16127 C  CA   . CYS   B  2  469 ? 45.946  21.096  16.615   1.00 120.92 ? 473  CYS   B CA   1 
ATOM   16128 C  C    . CYS   B  2  469 ? 46.413  22.552  16.674   1.00 123.65 ? 473  CYS   B C    1 
ATOM   16129 O  O    . CYS   B  2  469 ? 45.619  23.477  16.849   1.00 123.76 ? 473  CYS   B O    1 
ATOM   16130 C  CB   . CYS   B  2  469 ? 44.481  20.971  17.039   1.00 121.13 ? 473  CYS   B CB   1 
ATOM   16131 S  SG   . CYS   B  2  469 ? 43.937  19.261  17.272   1.00 121.18 ? 473  CYS   B SG   1 
ATOM   16132 H  H    . CYS   B  2  469 ? 47.263  19.674  16.975   1.00 140.35 ? 473  CYS   B H    1 
ATOM   16133 H  HA   . CYS   B  2  469 ? 46.015  20.810  15.691   1.00 145.14 ? 473  CYS   B HA   1 
ATOM   16134 H  HB2  . CYS   B  2  469 ? 44.358  21.438  17.880   1.00 145.40 ? 473  CYS   B HB2  1 
ATOM   16135 H  HB3  . CYS   B  2  469 ? 43.922  21.369  16.353   1.00 145.40 ? 473  CYS   B HB3  1 
ATOM   16136 N  N    . GLU   B  2  470 ? 47.717  22.745  16.494   1.00 124.96 ? 474  GLU   B N    1 
ATOM   16137 C  CA   . GLU   B  2  470 ? 48.371  24.025  16.721   1.00 127.78 ? 474  GLU   B CA   1 
ATOM   16138 C  C    . GLU   B  2  470 ? 48.688  24.771  15.431   1.00 124.62 ? 474  GLU   B C    1 
ATOM   16139 O  O    . GLU   B  2  470 ? 49.178  25.903  15.491   1.00 127.35 ? 474  GLU   B O    1 
ATOM   16140 C  CB   . GLU   B  2  470 ? 49.653  23.799  17.530   1.00 135.44 ? 474  GLU   B CB   1 
ATOM   16141 C  CG   . GLU   B  2  470 ? 49.468  22.804  18.677   1.00 138.08 ? 474  GLU   B CG   1 
ATOM   16142 C  CD   . GLU   B  2  470 ? 50.763  22.458  19.380   1.00 145.26 ? 474  GLU   B CD   1 
ATOM   16143 O  OE1  . GLU   B  2  470 ? 51.474  21.548  18.903   1.00 146.70 ? 474  GLU   B OE1  1 
ATOM   16144 O  OE2  . GLU   B  2  470 ? 51.070  23.096  20.409   1.00 148.18 ? 474  GLU   B OE2  1 
ATOM   16145 H  H    . GLU   B  2  470 ? 48.259  22.129  16.234   1.00 149.98 ? 474  GLU   B H    1 
ATOM   16146 H  HA   . GLU   B  2  470 ? 47.782  24.597  17.238   1.00 153.37 ? 474  GLU   B HA   1 
ATOM   16147 H  HB2  . GLU   B  2  470 ? 50.340  23.451  16.940   1.00 162.56 ? 474  GLU   B HB2  1 
ATOM   16148 H  HB3  . GLU   B  2  470 ? 49.938  24.645  17.910   1.00 162.56 ? 474  GLU   B HB3  1 
ATOM   16149 H  HG2  . GLU   B  2  470 ? 48.866  23.190  19.333   1.00 165.73 ? 474  GLU   B HG2  1 
ATOM   16150 H  HG3  . GLU   B  2  470 ? 49.091  21.983  18.324   1.00 165.73 ? 474  GLU   B HG3  1 
ATOM   16151 N  N    . SER   B  2  471 ? 48.424  24.169  14.275   1.00 120.73 ? 475  SER   B N    1 
ATOM   16152 C  CA   . SER   B  2  471 ? 48.588  24.816  12.982   1.00 119.64 ? 475  SER   B CA   1 
ATOM   16153 C  C    . SER   B  2  471 ? 47.227  24.988  12.321   1.00 120.60 ? 475  SER   B C    1 
ATOM   16154 O  O    . SER   B  2  471 ? 46.302  24.206  12.557   1.00 117.81 ? 475  SER   B O    1 
ATOM   16155 C  CB   . SER   B  2  471 ? 49.515  24.005  12.071   1.00 114.99 ? 475  SER   B CB   1 
ATOM   16156 O  OG   . SER   B  2  471 ? 50.875  24.225  12.404   1.00 115.47 ? 475  SER   B OG   1 
ATOM   16157 H  H    . SER   B  2  471 ? 48.139  23.360  14.214   1.00 144.91 ? 475  SER   B H    1 
ATOM   16158 H  HA   . SER   B  2  471 ? 48.985  25.693  13.101   1.00 143.60 ? 475  SER   B HA   1 
ATOM   16159 H  HB2  . SER   B  2  471 ? 49.314  23.062  12.176   1.00 138.02 ? 475  SER   B HB2  1 
ATOM   16160 H  HB3  . SER   B  2  471 ? 49.368  24.275  11.151   1.00 138.02 ? 475  SER   B HB3  1 
ATOM   16161 H  HG   . SER   B  2  471 ? 51.373  23.883  11.821   1.00 138.61 ? 475  SER   B HG   1 
ATOM   16162 N  N    . GLY   B  2  472 ? 47.112  26.016  11.492   1.00 124.65 ? 476  GLY   B N    1 
ATOM   16163 C  CA   . GLY   B  2  472 ? 45.846  26.374  10.868   1.00 125.21 ? 476  GLY   B CA   1 
ATOM   16164 C  C    . GLY   B  2  472 ? 45.947  26.376  9.356    1.00 128.75 ? 476  GLY   B C    1 
ATOM   16165 O  O    . GLY   B  2  472 ? 46.926  26.870  8.793    1.00 133.66 ? 476  GLY   B O    1 
ATOM   16166 H  H    . GLY   B  2  472 ? 47.764  26.531  11.271   1.00 149.62 ? 476  GLY   B H    1 
ATOM   16167 H  HA2  . GLY   B  2  472 ? 45.163  25.737  11.131   1.00 150.28 ? 476  GLY   B HA2  1 
ATOM   16168 H  HA3  . GLY   B  2  472 ? 45.580  27.260  11.161   1.00 150.28 ? 476  GLY   B HA3  1 
ATOM   16169 N  N    . HIS   B  2  473 ? 44.925  25.828  8.707    1.00 130.11 ? 477  HIS   B N    1 
ATOM   16170 C  CA   . HIS   B  2  473 ? 44.878  25.772  7.251    1.00 133.47 ? 477  HIS   B CA   1 
ATOM   16171 C  C    . HIS   B  2  473 ? 43.435  25.794  6.756    1.00 132.29 ? 477  HIS   B C    1 
ATOM   16172 O  O    . HIS   B  2  473 ? 42.762  24.763  6.730    1.00 129.99 ? 477  HIS   B O    1 
ATOM   16173 C  CB   . HIS   B  2  473 ? 45.589  24.519  6.738    1.00 136.22 ? 477  HIS   B CB   1 
ATOM   16174 C  CG   . HIS   B  2  473 ? 45.615  24.411  5.246    1.00 145.22 ? 477  HIS   B CG   1 
ATOM   16175 N  ND1  . HIS   B  2  473 ? 46.217  25.355  4.442    1.00 150.95 ? 477  HIS   B ND1  1 
ATOM   16176 C  CD2  . HIS   B  2  473 ? 45.110  23.473  4.411    1.00 147.71 ? 477  HIS   B CD2  1 
ATOM   16177 C  CE1  . HIS   B  2  473 ? 46.083  25.002  3.177    1.00 154.24 ? 477  HIS   B CE1  1 
ATOM   16178 N  NE2  . HIS   B  2  473 ? 45.416  23.864  3.130    1.00 152.05 ? 477  HIS   B NE2  1 
ATOM   16179 H  H    . HIS   B  2  473 ? 44.240  25.479  9.091    1.00 156.17 ? 477  HIS   B H    1 
ATOM   16180 H  HA   . HIS   B  2  473 ? 45.336  26.546  6.888    1.00 160.20 ? 477  HIS   B HA   1 
ATOM   16181 H  HB2  . HIS   B  2  473 ? 46.507  24.532  7.051    1.00 163.50 ? 477  HIS   B HB2  1 
ATOM   16182 H  HB3  . HIS   B  2  473 ? 45.131  23.737  7.085    1.00 163.50 ? 477  HIS   B HB3  1 
ATOM   16183 H  HD2  . HIS   B  2  473 ? 44.643  22.707  4.658    1.00 177.29 ? 477  HIS   B HD2  1 
ATOM   16184 H  HE1  . HIS   B  2  473 ? 46.405  25.475  2.443    1.00 185.12 ? 477  HIS   B HE1  1 
ATOM   16185 H  HE2  . HIS   B  2  473 ? 45.206  23.436  2.414    1.00 182.50 ? 477  HIS   B HE2  1 
ATOM   16186 N  N    . ASP   C  3  1   ? -9.451  -56.283 -48.047  1.00 89.83  ? 1    ASP   C N    1 
ATOM   16187 C  CA   . ASP   C  3  1   ? -8.518  -55.337 -48.723  1.00 86.56  ? 1    ASP   C CA   1 
ATOM   16188 C  C    . ASP   C  3  1   ? -9.244  -54.505 -49.772  1.00 89.02  ? 1    ASP   C C    1 
ATOM   16189 O  O    . ASP   C  3  1   ? -10.320 -54.878 -50.241  1.00 95.52  ? 1    ASP   C O    1 
ATOM   16190 C  CB   . ASP   C  3  1   ? -7.363  -56.095 -49.382  1.00 87.26  ? 1    ASP   C CB   1 
ATOM   16191 C  CG   . ASP   C  3  1   ? -6.552  -56.903 -48.390  1.00 91.64  ? 1    ASP   C CG   1 
ATOM   16192 O  OD1  . ASP   C  3  1   ? -6.912  -56.916 -47.194  1.00 93.31  ? 1    ASP   C OD1  1 
ATOM   16193 O  OD2  . ASP   C  3  1   ? -5.552  -57.525 -48.808  1.00 93.23  ? 1    ASP   C OD2  1 
ATOM   16194 H  H1   . ASP   C  3  1   ? -8.988  -56.834 -47.525  1.00 107.83 ? 1    ASP   C H1   1 
ATOM   16195 H  H2   . ASP   C  3  1   ? -10.032 -55.824 -47.553  1.00 107.83 ? 1    ASP   C H2   1 
ATOM   16196 H  H3   . ASP   C  3  1   ? -9.891  -56.755 -48.661  1.00 107.83 ? 1    ASP   C H3   1 
ATOM   16197 H  HA   . ASP   C  3  1   ? -8.149  -54.737 -48.056  1.00 103.91 ? 1    ASP   C HA   1 
ATOM   16198 H  HB2  . ASP   C  3  1   ? -7.722  -56.707 -50.044  1.00 104.75 ? 1    ASP   C HB2  1 
ATOM   16199 H  HB3  . ASP   C  3  1   ? -6.768  -55.458 -49.808  1.00 104.75 ? 1    ASP   C HB3  1 
ATOM   16200 N  N    . ILE   C  3  2   ? -8.647  -53.375 -50.131  1.00 84.47  ? 2    ILE   C N    1 
ATOM   16201 C  CA   . ILE   C  3  2   ? -9.153  -52.549 -51.220  1.00 83.60  ? 2    ILE   C CA   1 
ATOM   16202 C  C    . ILE   C  3  2   ? -8.656  -53.127 -52.538  1.00 86.76  ? 2    ILE   C C    1 
ATOM   16203 O  O    . ILE   C  3  2   ? -7.450  -53.333 -52.722  1.00 81.48  ? 2    ILE   C O    1 
ATOM   16204 C  CB   . ILE   C  3  2   ? -8.700  -51.089 -51.055  1.00 79.67  ? 2    ILE   C CB   1 
ATOM   16205 C  CG1  . ILE   C  3  2   ? -9.071  -50.551 -49.668  1.00 79.32  ? 2    ILE   C CG1  1 
ATOM   16206 C  CG2  . ILE   C  3  2   ? -9.301  -50.215 -52.155  1.00 78.86  ? 2    ILE   C CG2  1 
ATOM   16207 C  CD1  . ILE   C  3  2   ? -10.554 -50.409 -49.435  1.00 82.76  ? 2    ILE   C CD1  1 
ATOM   16208 H  H    . ILE   C  3  2   ? -7.939  -53.061 -49.756  1.00 101.40 ? 2    ILE   C H    1 
ATOM   16209 H  HA   . ILE   C  3  2   ? -10.123 -52.569 -51.213  1.00 100.36 ? 2    ILE   C HA   1 
ATOM   16210 H  HB   . ILE   C  3  2   ? -7.733  -51.064 -51.135  1.00 95.64  ? 2    ILE   C HB   1 
ATOM   16211 H  HG12 . ILE   C  3  2   ? -8.726  -51.160 -48.997  1.00 95.22  ? 2    ILE   C HG12 1 
ATOM   16212 H  HG13 . ILE   C  3  2   ? -8.671  -49.675 -49.558  1.00 95.22  ? 2    ILE   C HG13 1 
ATOM   16213 H  HG21 . ILE   C  3  2   ? -9.031  -49.295 -52.010  1.00 94.67  ? 2    ILE   C HG21 1 
ATOM   16214 H  HG22 . ILE   C  3  2   ? -8.977  -50.524 -53.015  1.00 94.67  ? 2    ILE   C HG22 1 
ATOM   16215 H  HG23 . ILE   C  3  2   ? -10.268 -50.285 -52.121  1.00 94.67  ? 2    ILE   C HG23 1 
ATOM   16216 H  HD11 . ILE   C  3  2   ? -10.702 -50.083 -48.533  1.00 99.34  ? 2    ILE   C HD11 1 
ATOM   16217 H  HD12 . ILE   C  3  2   ? -10.916 -49.779 -50.078  1.00 99.34  ? 2    ILE   C HD12 1 
ATOM   16218 H  HD13 . ILE   C  3  2   ? -10.976 -51.275 -49.548  1.00 99.34  ? 2    ILE   C HD13 1 
ATOM   16219 N  N    . GLN   C  3  3   ? -9.580  -53.394 -53.455  1.00 95.25  ? 3    GLN   C N    1 
ATOM   16220 C  CA   . GLN   C  3  3   ? -9.228  -53.837 -54.798  1.00 100.26 ? 3    GLN   C CA   1 
ATOM   16221 C  C    . GLN   C  3  3   ? -9.127  -52.623 -55.711  1.00 96.97  ? 3    GLN   C C    1 
ATOM   16222 O  O    . GLN   C  3  3   ? -10.022 -51.771 -55.723  1.00 97.73  ? 3    GLN   C O    1 
ATOM   16223 C  CB   . GLN   C  3  3   ? -10.264 -54.828 -55.334  1.00 110.98 ? 3    GLN   C CB   1 
ATOM   16224 C  CG   . GLN   C  3  3   ? -10.060 -55.248 -56.795  1.00 117.51 ? 3    GLN   C CG   1 
ATOM   16225 C  CD   . GLN   C  3  3   ? -8.967  -56.286 -56.972  1.00 122.35 ? 3    GLN   C CD   1 
ATOM   16226 O  OE1  . GLN   C  3  3   ? -9.024  -57.370 -56.391  1.00 127.87 ? 3    GLN   C OE1  1 
ATOM   16227 N  NE2  . GLN   C  3  3   ? -7.966  -55.959 -57.783  1.00 123.36 ? 3    GLN   C NE2  1 
ATOM   16228 H  H    . GLN   C  3  3   ? -10.427 -53.324 -53.322  1.00 114.34 ? 3    GLN   C H    1 
ATOM   16229 H  HA   . GLN   C  3  3   ? -8.370  -54.289 -54.780  1.00 120.35 ? 3    GLN   C HA   1 
ATOM   16230 H  HB2  . GLN   C  3  3   ? -10.230 -55.632 -54.793  1.00 133.22 ? 3    GLN   C HB2  1 
ATOM   16231 H  HB3  . GLN   C  3  3   ? -11.141 -54.420 -55.269  1.00 133.22 ? 3    GLN   C HB3  1 
ATOM   16232 H  HG2  . GLN   C  3  3   ? -10.888 -55.626 -57.131  1.00 141.04 ? 3    GLN   C HG2  1 
ATOM   16233 H  HG3  . GLN   C  3  3   ? -9.816  -54.466 -57.315  1.00 141.04 ? 3    GLN   C HG3  1 
ATOM   16234 H  HE21 . GLN   C  3  3   ? -7.962  -55.194 -58.174  1.00 148.07 ? 3    GLN   C HE21 1 
ATOM   16235 H  HE22 . GLN   C  3  3   ? -7.322  -56.514 -57.916  1.00 148.07 ? 3    GLN   C HE22 1 
ATOM   16236 N  N    . MET   C  3  4   ? -8.036  -52.544 -56.467  1.00 92.96  ? 4    MET   C N    1 
ATOM   16237 C  CA   . MET   C  3  4   ? -7.828  -51.491 -57.452  1.00 91.06  ? 4    MET   C CA   1 
ATOM   16238 C  C    . MET   C  3  4   ? -7.844  -52.115 -58.839  1.00 93.59  ? 4    MET   C C    1 
ATOM   16239 O  O    . MET   C  3  4   ? -7.190  -53.137 -59.070  1.00 99.74  ? 4    MET   C O    1 
ATOM   16240 C  CB   . MET   C  3  4   ? -6.504  -50.764 -57.211  1.00 85.83  ? 4    MET   C CB   1 
ATOM   16241 C  CG   . MET   C  3  4   ? -6.338  -50.223 -55.798  1.00 82.14  ? 4    MET   C CG   1 
ATOM   16242 S  SD   . MET   C  3  4   ? -7.658  -49.097 -55.305  1.00 81.36  ? 4    MET   C SD   1 
ATOM   16243 C  CE   . MET   C  3  4   ? -7.464  -47.809 -56.530  1.00 81.25  ? 4    MET   C CE   1 
ATOM   16244 H  H    . MET   C  3  4   ? -7.386  -53.105 -56.425  1.00 111.59 ? 4    MET   C H    1 
ATOM   16245 H  HA   . MET   C  3  4   ? -8.538  -50.834 -57.382  1.00 109.31 ? 4    MET   C HA   1 
ATOM   16246 H  HB2  . MET   C  3  4   ? -5.776  -51.382 -57.377  1.00 103.03 ? 4    MET   C HB2  1 
ATOM   16247 H  HB3  . MET   C  3  4   ? -6.447  -50.012 -57.822  1.00 103.03 ? 4    MET   C HB3  1 
ATOM   16248 H  HG2  . MET   C  3  4   ? -6.334  -50.968 -55.176  1.00 98.60  ? 4    MET   C HG2  1 
ATOM   16249 H  HG3  . MET   C  3  4   ? -5.499  -49.741 -55.743  1.00 98.60  ? 4    MET   C HG3  1 
ATOM   16250 H  HE1  . MET   C  3  4   ? -8.069  -47.080 -56.321  1.00 97.54  ? 4    MET   C HE1  1 
ATOM   16251 H  HE2  . MET   C  3  4   ? -6.547  -47.493 -56.514  1.00 97.54  ? 4    MET   C HE2  1 
ATOM   16252 H  HE3  . MET   C  3  4   ? -7.674  -48.172 -57.405  1.00 97.54  ? 4    MET   C HE3  1 
ATOM   16253 N  N    . THR   C  3  5   ? -8.587  -51.501 -59.757  1.00 91.61  ? 5    THR   C N    1 
ATOM   16254 C  CA   . THR   C  3  5   ? -8.794  -52.056 -61.089  1.00 94.81  ? 5    THR   C CA   1 
ATOM   16255 C  C    . THR   C  3  5   ? -8.622  -50.964 -62.131  1.00 95.96  ? 5    THR   C C    1 
ATOM   16256 O  O    . THR   C  3  5   ? -9.312  -49.941 -62.085  1.00 95.59  ? 5    THR   C O    1 
ATOM   16257 C  CB   . THR   C  3  5   ? -10.184 -52.688 -61.213  1.00 97.71  ? 5    THR   C CB   1 
ATOM   16258 O  OG1  . THR   C  3  5   ? -11.160 -51.820 -60.624  1.00 98.39  ? 5    THR   C OG1  1 
ATOM   16259 C  CG2  . THR   C  3  5   ? -10.219 -54.042 -60.523  1.00 98.88  ? 5    THR   C CG2  1 
ATOM   16260 H  H    . THR   C  3  5   ? -8.987  -50.751 -59.629  1.00 109.97 ? 5    THR   C H    1 
ATOM   16261 H  HA   . THR   C  3  5   ? -8.120  -52.735 -61.251  1.00 113.81 ? 5    THR   C HA   1 
ATOM   16262 H  HB   . THR   C  3  5   ? -10.398 -52.821 -62.150  1.00 117.29 ? 5    THR   C HB   1 
ATOM   16263 H  HG1  . THR   C  3  5   ? -11.005 -51.023 -60.841  1.00 118.11 ? 5    THR   C HG1  1 
ATOM   16264 H  HG21 . THR   C  3  5   ? -11.103 -54.433 -60.605  1.00 118.70 ? 5    THR   C HG21 1 
ATOM   16265 H  HG22 . THR   C  3  5   ? -9.572  -54.638 -60.930  1.00 118.70 ? 5    THR   C HG22 1 
ATOM   16266 H  HG23 . THR   C  3  5   ? -10.005 -53.940 -59.582  1.00 118.70 ? 5    THR   C HG23 1 
ATOM   16267 N  N    . GLN   C  3  6   ? -7.705  -51.188 -63.067  1.00 99.02  ? 6    GLN   C N    1 
ATOM   16268 C  CA   . GLN   C  3  6   ? -7.536  -50.336 -64.241  1.00 101.22 ? 6    GLN   C CA   1 
ATOM   16269 C  C    . GLN   C  3  6   ? -8.182  -51.074 -65.408  1.00 106.37 ? 6    GLN   C C    1 
ATOM   16270 O  O    . GLN   C  3  6   ? -7.598  -52.004 -65.971  1.00 110.04 ? 6    GLN   C O    1 
ATOM   16271 C  CB   . GLN   C  3  6   ? -6.062  -50.033 -64.479  1.00 95.20  ? 6    GLN   C CB   1 
ATOM   16272 C  CG   . GLN   C  3  6   ? -5.424  -49.298 -63.306  1.00 87.86  ? 6    GLN   C CG   1 
ATOM   16273 C  CD   . GLN   C  3  6   ? -3.926  -49.124 -63.446  1.00 80.06  ? 6    GLN   C CD   1 
ATOM   16274 O  OE1  . GLN   C  3  6   ? -3.163  -49.512 -62.562  1.00 74.53  ? 6    GLN   C OE1  1 
ATOM   16275 N  NE2  . GLN   C  3  6   ? -3.497  -48.526 -64.550  1.00 79.69  ? 6    GLN   C NE2  1 
ATOM   16276 H  H    . GLN   C  3  6   ? -7.152  -51.847 -63.044  1.00 118.86 ? 6    GLN   C H    1 
ATOM   16277 H  HA   . GLN   C  3  6   ? -7.987  -49.486 -64.120  1.00 121.50 ? 6    GLN   C HA   1 
ATOM   16278 H  HB2  . GLN   C  3  6   ? -5.583  -50.866 -64.609  1.00 114.27 ? 6    GLN   C HB2  1 
ATOM   16279 H  HB3  . GLN   C  3  6   ? -5.976  -49.475 -65.268  1.00 114.27 ? 6    GLN   C HB3  1 
ATOM   16280 H  HG2  . GLN   C  3  6   ? -5.820  -48.415 -63.237  1.00 105.47 ? 6    GLN   C HG2  1 
ATOM   16281 H  HG3  . GLN   C  3  6   ? -5.590  -49.800 -62.494  1.00 105.47 ? 6    GLN   C HG3  1 
ATOM   16282 H  HE21 . GLN   C  3  6   ? -4.062  -48.259 -65.141  1.00 95.67  ? 6    GLN   C HE21 1 
ATOM   16283 H  HE22 . GLN   C  3  6   ? -2.655  -48.405 -64.674  1.00 95.67  ? 6    GLN   C HE22 1 
ATOM   16284 N  N    . THR   C  3  7   ? -9.405  -50.660 -65.751  1.00 107.57 ? 7    THR   C N    1 
ATOM   16285 C  CA   . THR   C  3  7   ? -10.204 -51.363 -66.749  1.00 114.12 ? 7    THR   C CA   1 
ATOM   16286 C  C    . THR   C  3  7   ? -9.383  -51.708 -67.985  1.00 111.15 ? 7    THR   C C    1 
ATOM   16287 O  O    . THR   C  3  7   ? -9.302  -52.872 -68.393  1.00 111.64 ? 7    THR   C O    1 
ATOM   16288 C  CB   . THR   C  3  7   ? -11.414 -50.506 -67.132  1.00 124.50 ? 7    THR   C CB   1 
ATOM   16289 O  OG1  . THR   C  3  7   ? -11.003 -49.141 -67.287  1.00 126.16 ? 7    THR   C OG1  1 
ATOM   16290 C  CG2  . THR   C  3  7   ? -12.495 -50.598 -66.065  1.00 129.57 ? 7    THR   C CG2  1 
ATOM   16291 H  H    . THR   C  3  7   ? -9.795  -49.971 -65.417  1.00 129.12 ? 7    THR   C H    1 
ATOM   16292 H  HA   . THR   C  3  7   ? -10.521 -52.194 -66.362  1.00 136.99 ? 7    THR   C HA   1 
ATOM   16293 H  HB   . THR   C  3  7   ? -11.788 -50.826 -67.968  1.00 149.44 ? 7    THR   C HB   1 
ATOM   16294 H  HG1  . THR   C  3  7   ? -11.657 -48.669 -67.520  1.00 151.43 ? 7    THR   C HG1  1 
ATOM   16295 H  HG21 . THR   C  3  7   ? -13.257 -50.053 -66.318  1.00 155.52 ? 7    THR   C HG21 1 
ATOM   16296 H  HG22 . THR   C  3  7   ? -12.785 -51.518 -65.965  1.00 155.52 ? 7    THR   C HG22 1 
ATOM   16297 H  HG23 . THR   C  3  7   ? -12.150 -50.282 -65.215  1.00 155.52 ? 7    THR   C HG23 1 
ATOM   16298 N  N    . THR   C  3  8   ? -8.766  -50.702 -68.594  1.00 109.09 ? 8    THR   C N    1 
ATOM   16299 C  CA   . THR   C  3  8   ? -7.963  -50.896 -69.793  1.00 110.32 ? 8    THR   C CA   1 
ATOM   16300 C  C    . THR   C  3  8   ? -6.549  -51.295 -69.390  1.00 111.78 ? 8    THR   C C    1 
ATOM   16301 O  O    . THR   C  3  8   ? -5.833  -50.508 -68.761  1.00 114.28 ? 8    THR   C O    1 
ATOM   16302 C  CB   . THR   C  3  8   ? -7.938  -49.623 -70.638  1.00 106.86 ? 8    THR   C CB   1 
ATOM   16303 O  OG1  . THR   C  3  8   ? -7.367  -48.551 -69.876  1.00 104.55 ? 8    THR   C OG1  1 
ATOM   16304 C  CG2  . THR   C  3  8   ? -9.347  -49.238 -71.064  1.00 109.36 ? 8    THR   C CG2  1 
ATOM   16305 H  H    . THR   C  3  8   ? -8.799  -49.885 -68.328  1.00 130.95 ? 8    THR   C H    1 
ATOM   16306 H  HA   . THR   C  3  8   ? -8.348  -51.609 -70.326  1.00 132.42 ? 8    THR   C HA   1 
ATOM   16307 H  HB   . THR   C  3  8   ? -7.406  -49.774 -71.434  1.00 128.26 ? 8    THR   C HB   1 
ATOM   16308 H  HG1  . THR   C  3  8   ? -6.720  -48.835 -69.421  1.00 125.50 ? 8    THR   C HG1  1 
ATOM   16309 H  HG21 . THR   C  3  8   ? -9.324  -48.420 -71.586  1.00 131.27 ? 8    THR   C HG21 1 
ATOM   16310 H  HG22 . THR   C  3  8   ? -9.735  -49.945 -71.604  1.00 131.27 ? 8    THR   C HG22 1 
ATOM   16311 H  HG23 . THR   C  3  8   ? -9.903  -49.097 -70.283  1.00 131.27 ? 8    THR   C HG23 1 
ATOM   16312 N  N    . SER   C  3  9   ? -6.150  -52.513 -69.749  1.00 111.40 ? 9    SER   C N    1 
ATOM   16313 C  CA   . SER   C  3  9   ? -4.792  -52.965 -69.482  1.00 106.23 ? 9    SER   C CA   1 
ATOM   16314 C  C    . SER   C  3  9   ? -3.786  -52.437 -70.497  1.00 99.04  ? 9    SER   C C    1 
ATOM   16315 O  O    . SER   C  3  9   ? -2.580  -52.505 -70.238  1.00 96.42  ? 9    SER   C O    1 
ATOM   16316 C  CB   . SER   C  3  9   ? -4.741  -54.495 -69.455  1.00 114.39 ? 9    SER   C CB   1 
ATOM   16317 O  OG   . SER   C  3  9   ? -5.531  -55.011 -68.396  1.00 119.07 ? 9    SER   C OG   1 
ATOM   16318 H  H    . SER   C  3  9   ? -6.646  -53.093 -70.147  1.00 133.72 ? 9    SER   C H    1 
ATOM   16319 H  HA   . SER   C  3  9   ? -4.525  -52.646 -68.606  1.00 127.51 ? 9    SER   C HA   1 
ATOM   16320 H  HB2  . SER   C  3  9   ? -5.080  -54.837 -70.297  1.00 137.30 ? 9    SER   C HB2  1 
ATOM   16321 H  HB3  . SER   C  3  9   ? -3.822  -54.778 -69.328  1.00 137.30 ? 9    SER   C HB3  1 
ATOM   16322 H  HG   . SER   C  3  9   ? -5.524  -55.850 -68.416  1.00 142.92 ? 9    SER   C HG   1 
ATOM   16323 N  N    . SER   C  3  10  ? -4.242  -51.913 -71.634  1.00 96.50  ? 10   SER   C N    1 
ATOM   16324 C  CA   . SER   C  3  10  ? -3.331  -51.363 -72.626  1.00 92.99  ? 10   SER   C CA   1 
ATOM   16325 C  C    . SER   C  3  10  ? -4.089  -50.435 -73.564  1.00 93.18  ? 10   SER   C C    1 
ATOM   16326 O  O    . SER   C  3  10  ? -5.247  -50.693 -73.904  1.00 94.73  ? 10   SER   C O    1 
ATOM   16327 C  CB   . SER   C  3  10  ? -2.646  -52.472 -73.432  1.00 95.73  ? 10   SER   C CB   1 
ATOM   16328 O  OG   . SER   C  3  10  ? -1.806  -51.921 -74.432  1.00 94.68  ? 10   SER   C OG   1 
ATOM   16329 H  H    . SER   C  3  10  ? -5.073  -51.867 -71.851  1.00 115.84 ? 10   SER   C H    1 
ATOM   16330 H  HA   . SER   C  3  10  ? -2.653  -50.841 -72.170  1.00 111.62 ? 10   SER   C HA   1 
ATOM   16331 H  HB2  . SER   C  3  10  ? -2.110  -53.014 -72.832  1.00 114.91 ? 10   SER   C HB2  1 
ATOM   16332 H  HB3  . SER   C  3  10  ? -3.325  -53.020 -73.857  1.00 114.91 ? 10   SER   C HB3  1 
ATOM   16333 H  HG   . SER   C  3  10  ? -1.507  -52.532 -74.925  1.00 113.65 ? 10   SER   C HG   1 
ATOM   16334 N  N    . LEU   C  3  11  ? -3.418  -49.362 -73.979  1.00 88.66  ? 11   LEU   C N    1 
ATOM   16335 C  CA   . LEU   C  3  11  ? -3.949  -48.418 -74.950  1.00 89.76  ? 11   LEU   C CA   1 
ATOM   16336 C  C    . LEU   C  3  11  ? -2.802  -47.942 -75.830  1.00 87.85  ? 11   LEU   C C    1 
ATOM   16337 O  O    . LEU   C  3  11  ? -1.628  -48.057 -75.468  1.00 86.45  ? 11   LEU   C O    1 
ATOM   16338 C  CB   . LEU   C  3  11  ? -4.630  -47.223 -74.270  1.00 90.30  ? 11   LEU   C CB   1 
ATOM   16339 C  CG   . LEU   C  3  11  ? -3.703  -46.285 -73.490  1.00 87.17  ? 11   LEU   C CG   1 
ATOM   16340 C  CD1  . LEU   C  3  11  ? -3.134  -45.175 -74.375  1.00 87.28  ? 11   LEU   C CD1  1 
ATOM   16341 C  CD2  . LEU   C  3  11  ? -4.432  -45.690 -72.297  1.00 85.31  ? 11   LEU   C CD2  1 
ATOM   16342 H  H    . LEU   C  3  11  ? -2.631  -49.155 -73.701  1.00 106.43 ? 11   LEU   C H    1 
ATOM   16343 H  HA   . LEU   C  3  11  ? -4.609  -48.857 -75.509  1.00 107.74 ? 11   LEU   C HA   1 
ATOM   16344 H  HB2  . LEU   C  3  11  ? -5.067  -46.692 -74.955  1.00 108.39 ? 11   LEU   C HB2  1 
ATOM   16345 H  HB3  . LEU   C  3  11  ? -5.288  -47.564 -73.644  1.00 108.39 ? 11   LEU   C HB3  1 
ATOM   16346 H  HG   . LEU   C  3  11  ? -2.951  -46.807 -73.169  1.00 104.64 ? 11   LEU   C HG   1 
ATOM   16347 H  HD11 . LEU   C  3  11  ? -2.629  -44.559 -73.822  1.00 104.78 ? 11   LEU   C HD11 1 
ATOM   16348 H  HD12 . LEU   C  3  11  ? -2.553  -45.571 -75.044  1.00 104.78 ? 11   LEU   C HD12 1 
ATOM   16349 H  HD13 . LEU   C  3  11  ? -3.866  -44.709 -74.807  1.00 104.78 ? 11   LEU   C HD13 1 
ATOM   16350 H  HD21 . LEU   C  3  11  ? -3.830  -45.094 -71.825  1.00 102.41 ? 11   LEU   C HD21 1 
ATOM   16351 H  HD22 . LEU   C  3  11  ? -5.205  -45.198 -72.613  1.00 102.41 ? 11   LEU   C HD22 1 
ATOM   16352 H  HD23 . LEU   C  3  11  ? -4.714  -46.409 -71.709  1.00 102.41 ? 11   LEU   C HD23 1 
ATOM   16353 N  N    . SER   C  3  12  ? -3.154  -47.385 -76.985  1.00 88.38  ? 12   SER   C N    1 
ATOM   16354 C  CA   . SER   C  3  12  ? -2.179  -46.899 -77.952  1.00 84.05  ? 12   SER   C CA   1 
ATOM   16355 C  C    . SER   C  3  12  ? -2.414  -45.421 -78.228  1.00 83.75  ? 12   SER   C C    1 
ATOM   16356 O  O    . SER   C  3  12  ? -3.559  -44.965 -78.301  1.00 87.04  ? 12   SER   C O    1 
ATOM   16357 C  CB   . SER   C  3  12  ? -2.254  -47.700 -79.254  1.00 83.90  ? 12   SER   C CB   1 
ATOM   16358 O  OG   . SER   C  3  12  ? -3.597  -47.998 -79.592  1.00 89.61  ? 12   SER   C OG   1 
ATOM   16359 H  H    . SER   C  3  12  ? -3.969  -47.277 -77.235  1.00 106.09 ? 12   SER   C H    1 
ATOM   16360 H  HA   . SER   C  3  12  ? -1.285  -46.993 -77.588  1.00 100.90 ? 12   SER   C HA   1 
ATOM   16361 H  HB2  . SER   C  3  12  ? -1.858  -47.178 -79.969  1.00 100.72 ? 12   SER   C HB2  1 
ATOM   16362 H  HB3  . SER   C  3  12  ? -1.767  -48.531 -79.141  1.00 100.72 ? 12   SER   C HB3  1 
ATOM   16363 H  HG   . SER   C  3  12  ? -3.619  -48.502 -80.263  1.00 107.57 ? 12   SER   C HG   1 
ATOM   16364 N  N    . ALA   C  3  13  ? -1.319  -44.677 -78.387  1.00 82.92  ? 13   ALA   C N    1 
ATOM   16365 C  CA   . ALA   C  3  13  ? -1.385  -43.234 -78.556  1.00 85.15  ? 13   ALA   C CA   1 
ATOM   16366 C  C    . ALA   C  3  13  ? -0.250  -42.777 -79.459  1.00 88.84  ? 13   ALA   C C    1 
ATOM   16367 O  O    . ALA   C  3  13  ? 0.788   -43.435 -79.558  1.00 88.81  ? 13   ALA   C O    1 
ATOM   16368 C  CB   . ALA   C  3  13  ? -1.305  -42.510 -77.206  1.00 80.99  ? 13   ALA   C CB   1 
ATOM   16369 H  H    . ALA   C  3  13  ? -0.519  -44.992 -78.400  1.00 99.54  ? 13   ALA   C H    1 
ATOM   16370 H  HA   . ALA   C  3  13  ? -2.223  -43.001 -78.985  1.00 102.22 ? 13   ALA   C HA   1 
ATOM   16371 H  HB1  . ALA   C  3  13  ? -1.349  -41.553 -77.358  1.00 97.22  ? 13   ALA   C HB1  1 
ATOM   16372 H  HB2  . ALA   C  3  13  ? -2.049  -42.792 -76.652  1.00 97.22  ? 13   ALA   C HB2  1 
ATOM   16373 H  HB3  . ALA   C  3  13  ? -0.466  -42.738 -76.775  1.00 97.22  ? 13   ALA   C HB3  1 
ATOM   16374 N  N    . SER   C  3  14  ? -0.461  -41.641 -80.115  1.00 91.11  ? 14   SER   C N    1 
ATOM   16375 C  CA   . SER   C  3  14  ? 0.553   -41.002 -80.938  1.00 90.63  ? 14   SER   C CA   1 
ATOM   16376 C  C    . SER   C  3  14  ? 1.178   -39.835 -80.181  1.00 88.47  ? 14   SER   C C    1 
ATOM   16377 O  O    . SER   C  3  14  ? 0.641   -39.352 -79.182  1.00 88.55  ? 14   SER   C O    1 
ATOM   16378 C  CB   . SER   C  3  14  ? -0.045  -40.511 -82.259  1.00 93.04  ? 14   SER   C CB   1 
ATOM   16379 O  OG   . SER   C  3  14  ? -0.406  -41.599 -83.091  1.00 93.19  ? 14   SER   C OG   1 
ATOM   16380 H  H    . SER   C  3  14  ? -1.206  -41.211 -80.096  1.00 109.37 ? 14   SER   C H    1 
ATOM   16381 H  HA   . SER   C  3  14  ? 1.250   -41.643 -81.148  1.00 108.79 ? 14   SER   C HA   1 
ATOM   16382 H  HB2  . SER   C  3  14  ? -0.837  -39.983 -82.069  1.00 111.69 ? 14   SER   C HB2  1 
ATOM   16383 H  HB3  . SER   C  3  14  ? 0.613   -39.967 -82.720  1.00 111.69 ? 14   SER   C HB3  1 
ATOM   16384 H  HG   . SER   C  3  14  ? -0.784  -41.316 -83.786  1.00 111.86 ? 14   SER   C HG   1 
ATOM   16385 N  N    . LEU   C  3  15  ? 2.331   -39.388 -80.673  1.00 89.00  ? 15   LEU   C N    1 
ATOM   16386 C  CA   . LEU   C  3  15  ? 3.026   -38.278 -80.036  1.00 86.35  ? 15   LEU   C CA   1 
ATOM   16387 C  C    . LEU   C  3  15  ? 2.143   -37.037 -80.027  1.00 87.76  ? 15   LEU   C C    1 
ATOM   16388 O  O    . LEU   C  3  15  ? 1.439   -36.746 -80.997  1.00 89.57  ? 15   LEU   C O    1 
ATOM   16389 C  CB   . LEU   C  3  15  ? 4.340   -37.990 -80.762  1.00 87.19  ? 15   LEU   C CB   1 
ATOM   16390 C  CG   . LEU   C  3  15  ? 5.337   -39.150 -80.805  1.00 91.39  ? 15   LEU   C CG   1 
ATOM   16391 C  CD1  . LEU   C  3  15  ? 6.559   -38.781 -81.632  1.00 95.55  ? 15   LEU   C CD1  1 
ATOM   16392 C  CD2  . LEU   C  3  15  ? 5.751   -39.565 -79.400  1.00 89.59  ? 15   LEU   C CD2  1 
ATOM   16393 H  H    . LEU   C  3  15  ? 2.726   -39.707 -81.367  1.00 106.84 ? 15   LEU   C H    1 
ATOM   16394 H  HA   . LEU   C  3  15  ? 3.236   -38.511 -79.118  1.00 103.65 ? 15   LEU   C HA   1 
ATOM   16395 H  HB2  . LEU   C  3  15  ? 4.134   -37.751 -81.680  1.00 104.66 ? 15   LEU   C HB2  1 
ATOM   16396 H  HB3  . LEU   C  3  15  ? 4.778   -37.248 -80.317  1.00 104.66 ? 15   LEU   C HB3  1 
ATOM   16397 H  HG   . LEU   C  3  15  ? 4.907   -39.910 -81.226  1.00 109.70 ? 15   LEU   C HG   1 
ATOM   16398 H  HD11 . LEU   C  3  15  ? 7.169   -39.534 -81.648  1.00 114.70 ? 15   LEU   C HD11 1 
ATOM   16399 H  HD12 . LEU   C  3  15  ? 6.276   -38.565 -82.535  1.00 114.70 ? 15   LEU   C HD12 1 
ATOM   16400 H  HD13 . LEU   C  3  15  ? 6.993   -38.012 -81.230  1.00 114.70 ? 15   LEU   C HD13 1 
ATOM   16401 H  HD21 . LEU   C  3  15  ? 6.393   -40.290 -79.461  1.00 107.55 ? 15   LEU   C HD21 1 
ATOM   16402 H  HD22 . LEU   C  3  15  ? 6.153   -38.804 -78.952  1.00 107.55 ? 15   LEU   C HD22 1 
ATOM   16403 H  HD23 . LEU   C  3  15  ? 4.965   -39.859 -78.913  1.00 107.55 ? 15   LEU   C HD23 1 
ATOM   16404 N  N    . GLY   C  3  16  ? 2.183   -36.303 -78.914  1.00 85.77  ? 16   GLY   C N    1 
ATOM   16405 C  CA   . GLY   C  3  16  ? 1.371   -35.119 -78.741  1.00 87.20  ? 16   GLY   C CA   1 
ATOM   16406 C  C    . GLY   C  3  16  ? -0.043  -35.371 -78.270  1.00 85.47  ? 16   GLY   C C    1 
ATOM   16407 O  O    . GLY   C  3  16  ? -0.708  -34.429 -77.821  1.00 86.62  ? 16   GLY   C O    1 
ATOM   16408 H  H    . GLY   C  3  16  ? 2.684   -36.481 -78.238  1.00 102.96 ? 16   GLY   C H    1 
ATOM   16409 H  HA2  . GLY   C  3  16  ? 1.800   -34.543 -78.089  1.00 104.68 ? 16   GLY   C HA2  1 
ATOM   16410 H  HA3  . GLY   C  3  16  ? 1.320   -34.653 -79.589  1.00 104.68 ? 16   GLY   C HA3  1 
ATOM   16411 N  N    . ASP   C  3  17  ? -0.529  -36.608 -78.352  1.00 84.88  ? 17   ASP   C N    1 
ATOM   16412 C  CA   . ASP   C  3  17  ? -1.891  -36.910 -77.945  1.00 87.38  ? 17   ASP   C CA   1 
ATOM   16413 C  C    . ASP   C  3  17  ? -2.067  -36.696 -76.443  1.00 88.17  ? 17   ASP   C C    1 
ATOM   16414 O  O    . ASP   C  3  17  ? -1.104  -36.576 -75.679  1.00 86.06  ? 17   ASP   C O    1 
ATOM   16415 C  CB   . ASP   C  3  17  ? -2.255  -38.351 -78.299  1.00 88.39  ? 17   ASP   C CB   1 
ATOM   16416 C  CG   . ASP   C  3  17  ? -2.323  -38.587 -79.793  1.00 96.16  ? 17   ASP   C CG   1 
ATOM   16417 O  OD1  . ASP   C  3  17  ? -2.318  -37.599 -80.557  1.00 99.74  ? 17   ASP   C OD1  1 
ATOM   16418 O  OD2  . ASP   C  3  17  ? -2.381  -39.766 -80.203  1.00 96.89  ? 17   ASP   C OD2  1 
ATOM   16419 H  H    . ASP   C  3  17  ? -0.088  -37.287 -78.640  1.00 101.89 ? 17   ASP   C H    1 
ATOM   16420 H  HA   . ASP   C  3  17  ? -2.493  -36.313 -78.416  1.00 104.89 ? 17   ASP   C HA   1 
ATOM   16421 H  HB2  . ASP   C  3  17  ? -1.583  -38.946 -77.932  1.00 106.10 ? 17   ASP   C HB2  1 
ATOM   16422 H  HB3  . ASP   C  3  17  ? -3.124  -38.560 -77.923  1.00 106.10 ? 17   ASP   C HB3  1 
ATOM   16423 N  N    . ARG   C  3  18  ? -3.329  -36.653 -76.025  1.00 93.87  ? 18   ARG   C N    1 
ATOM   16424 C  CA   . ARG   C  3  18  ? -3.696  -36.601 -74.616  1.00 97.09  ? 18   ARG   C CA   1 
ATOM   16425 C  C    . ARG   C  3  18  ? -4.172  -37.982 -74.187  1.00 88.86  ? 18   ARG   C C    1 
ATOM   16426 O  O    . ARG   C  3  18  ? -5.096  -38.540 -74.789  1.00 89.48  ? 18   ARG   C O    1 
ATOM   16427 C  CB   . ARG   C  3  18  ? -4.784  -35.559 -74.368  1.00 112.15 ? 18   ARG   C CB   1 
ATOM   16428 C  CG   . ARG   C  3  18  ? -5.726  -35.927 -73.234  1.00 120.91 ? 18   ARG   C CG   1 
ATOM   16429 C  CD   . ARG   C  3  18  ? -6.511  -34.729 -72.757  1.00 128.53 ? 18   ARG   C CD   1 
ATOM   16430 N  NE   . ARG   C  3  18  ? -5.641  -33.729 -72.149  1.00 131.86 ? 18   ARG   C NE   1 
ATOM   16431 C  CZ   . ARG   C  3  18  ? -6.074  -32.626 -71.548  1.00 139.24 ? 18   ARG   C CZ   1 
ATOM   16432 N  NH1  . ARG   C  3  18  ? -7.374  -32.377 -71.470  1.00 151.08 ? 18   ARG   C NH1  1 
ATOM   16433 N  NH2  . ARG   C  3  18  ? -5.205  -31.773 -71.024  1.00 141.26 ? 18   ARG   C NH2  1 
ATOM   16434 H  H    . ARG   C  3  18  ? -4.007  -36.652 -76.554  1.00 112.68 ? 18   ARG   C H    1 
ATOM   16435 H  HA   . ARG   C  3  18  ? -2.919  -36.357 -74.088  1.00 116.55 ? 18   ARG   C HA   1 
ATOM   16436 H  HB2  . ARG   C  3  18  ? -4.363  -34.714 -74.142  1.00 134.62 ? 18   ARG   C HB2  1 
ATOM   16437 H  HB3  . ARG   C  3  18  ? -5.313  -35.461 -75.174  1.00 134.62 ? 18   ARG   C HB3  1 
ATOM   16438 H  HG2  . ARG   C  3  18  ? -6.354  -36.599 -73.543  1.00 145.13 ? 18   ARG   C HG2  1 
ATOM   16439 H  HG3  . ARG   C  3  18  ? -5.212  -36.271 -72.487  1.00 145.13 ? 18   ARG   C HG3  1 
ATOM   16440 H  HD2  . ARG   C  3  18  ? -6.964  -34.321 -73.512  1.00 154.27 ? 18   ARG   C HD2  1 
ATOM   16441 H  HD3  . ARG   C  3  18  ? -7.160  -35.012 -72.094  1.00 154.27 ? 18   ARG   C HD3  1 
ATOM   16442 H  HE   . ARG   C  3  18  ? -4.791  -33.862 -72.182  1.00 158.27 ? 18   ARG   C HE   1 
ATOM   16443 H  HH11 . ARG   C  3  18  ? -7.939  -32.930 -71.808  1.00 181.33 ? 18   ARG   C HH11 1 
ATOM   16444 H  HH12 . ARG   C  3  18  ? -7.652  -31.663 -71.080  1.00 181.33 ? 18   ARG   C HH12 1 
ATOM   16445 H  HH21 . ARG   C  3  18  ? -4.362  -31.933 -71.072  1.00 169.55 ? 18   ARG   C HH21 1 
ATOM   16446 H  HH22 . ARG   C  3  18  ? -5.486  -31.059 -70.634  1.00 169.55 ? 18   ARG   C HH22 1 
ATOM   16447 N  N    . VAL   C  3  19  ? -3.551  -38.522 -73.143  1.00 82.44  ? 19   VAL   C N    1 
ATOM   16448 C  CA   . VAL   C  3  19  ? -3.840  -39.863 -72.650  1.00 80.31  ? 19   VAL   C CA   1 
ATOM   16449 C  C    . VAL   C  3  19  ? -4.462  -39.745 -71.267  1.00 78.81  ? 19   VAL   C C    1 
ATOM   16450 O  O    . VAL   C  3  19  ? -3.972  -38.986 -70.421  1.00 78.51  ? 19   VAL   C O    1 
ATOM   16451 C  CB   . VAL   C  3  19  ? -2.569  -40.730 -72.615  1.00 79.70  ? 19   VAL   C CB   1 
ATOM   16452 C  CG1  . VAL   C  3  19  ? -2.875  -42.114 -72.064  1.00 83.16  ? 19   VAL   C CG1  1 
ATOM   16453 C  CG2  . VAL   C  3  19  ? -1.964  -40.826 -74.008  1.00 77.85  ? 19   VAL   C CG2  1 
ATOM   16454 H  H    . VAL   C  3  19  ? -2.941  -38.118 -72.691  1.00 98.96  ? 19   VAL   C H    1 
ATOM   16455 H  HA   . VAL   C  3  19  ? -4.485  -40.290 -73.235  1.00 96.41  ? 19   VAL   C HA   1 
ATOM   16456 H  HB   . VAL   C  3  19  ? -1.919  -40.314 -72.027  1.00 95.68  ? 19   VAL   C HB   1 
ATOM   16457 H  HG11 . VAL   C  3  19  ? -2.066  -42.650 -72.090  1.00 99.83  ? 19   VAL   C HG11 1 
ATOM   16458 H  HG12 . VAL   C  3  19  ? -3.186  -42.029 -71.150  1.00 99.83  ? 19   VAL   C HG12 1 
ATOM   16459 H  HG13 . VAL   C  3  19  ? -3.562  -42.527 -72.611  1.00 99.83  ? 19   VAL   C HG13 1 
ATOM   16460 H  HG21 . VAL   C  3  19  ? -1.198  -41.421 -73.979  1.00 93.45  ? 19   VAL   C HG21 1 
ATOM   16461 H  HG22 . VAL   C  3  19  ? -2.631  -41.176 -74.618  1.00 93.45  ? 19   VAL   C HG22 1 
ATOM   16462 H  HG23 . VAL   C  3  19  ? -1.686  -39.942 -74.293  1.00 93.45  ? 19   VAL   C HG23 1 
ATOM   16463 N  N    . ILE   C  3  20  ? -5.537  -40.495 -71.040  1.00 79.82  ? 20   ILE   C N    1 
ATOM   16464 C  CA   . ILE   C  3  20  ? -6.247  -40.509 -69.767  1.00 80.08  ? 20   ILE   C CA   1 
ATOM   16465 C  C    . ILE   C  3  20  ? -6.368  -41.958 -69.320  1.00 80.48  ? 20   ILE   C C    1 
ATOM   16466 O  O    . ILE   C  3  20  ? -6.941  -42.786 -70.038  1.00 79.45  ? 20   ILE   C O    1 
ATOM   16467 C  CB   . ILE   C  3  20  ? -7.636  -39.855 -69.873  1.00 83.68  ? 20   ILE   C CB   1 
ATOM   16468 C  CG1  . ILE   C  3  20  ? -7.492  -38.389 -70.288  1.00 83.96  ? 20   ILE   C CG1  1 
ATOM   16469 C  CG2  . ILE   C  3  20  ? -8.387  -39.975 -68.548  1.00 85.30  ? 20   ILE   C CG2  1 
ATOM   16470 C  CD1  . ILE   C  3  20  ? -8.809  -37.672 -70.500  1.00 87.28  ? 20   ILE   C CD1  1 
ATOM   16471 H  H    . ILE   C  3  20  ? -5.884  -41.019 -71.628  1.00 95.82  ? 20   ILE   C H    1 
ATOM   16472 H  HA   . ILE   C  3  20  ? -5.733  -40.024 -69.103  1.00 96.13  ? 20   ILE   C HA   1 
ATOM   16473 H  HB   . ILE   C  3  20  ? -8.148  -40.321 -70.553  1.00 100.46 ? 20   ILE   C HB   1 
ATOM   16474 H  HG12 . ILE   C  3  20  ? -7.009  -37.915 -69.594  1.00 100.79 ? 20   ILE   C HG12 1 
ATOM   16475 H  HG13 . ILE   C  3  20  ? -6.999  -38.349 -71.122  1.00 100.79 ? 20   ILE   C HG13 1 
ATOM   16476 H  HG21 . ILE   C  3  20  ? -9.262  -39.566 -68.643  1.00 102.39 ? 20   ILE   C HG21 1 
ATOM   16477 H  HG22 . ILE   C  3  20  ? -8.484  -40.913 -68.323  1.00 102.39 ? 20   ILE   C HG22 1 
ATOM   16478 H  HG23 . ILE   C  3  20  ? -7.883  -39.519 -67.857  1.00 102.39 ? 20   ILE   C HG23 1 
ATOM   16479 H  HD11 . ILE   C  3  20  ? -8.631  -36.771 -70.813  1.00 104.77 ? 20   ILE   C HD11 1 
ATOM   16480 H  HD12 . ILE   C  3  20  ? -9.329  -38.155 -71.162  1.00 104.77 ? 20   ILE   C HD12 1 
ATOM   16481 H  HD13 . ILE   C  3  20  ? -9.291  -37.641 -69.659  1.00 104.77 ? 20   ILE   C HD13 1 
ATOM   16482 N  N    . ILE   C  3  21  ? -5.835  -42.261 -68.140  1.00 79.08  ? 21   ILE   C N    1 
ATOM   16483 C  CA   . ILE   C  3  21  ? -5.861  -43.605 -67.574  1.00 78.62  ? 21   ILE   C CA   1 
ATOM   16484 C  C    . ILE   C  3  21  ? -6.812  -43.600 -66.388  1.00 80.91  ? 21   ILE   C C    1 
ATOM   16485 O  O    . ILE   C  3  21  ? -6.771  -42.688 -65.555  1.00 78.36  ? 21   ILE   C O    1 
ATOM   16486 C  CB   . ILE   C  3  21  ? -4.452  -44.066 -67.165  1.00 71.43  ? 21   ILE   C CB   1 
ATOM   16487 C  CG1  . ILE   C  3  21  ? -3.565  -44.174 -68.407  1.00 69.52  ? 21   ILE   C CG1  1 
ATOM   16488 C  CG2  . ILE   C  3  21  ? -4.511  -45.408 -66.447  1.00 68.15  ? 21   ILE   C CG2  1 
ATOM   16489 C  CD1  . ILE   C  3  21  ? -2.115  -43.841 -68.161  1.00 67.04  ? 21   ILE   C CD1  1 
ATOM   16490 H  H    . ILE   C  3  21  ? -5.443  -41.687 -67.634  1.00 94.94  ? 21   ILE   C H    1 
ATOM   16491 H  HA   . ILE   C  3  21  ? -6.201  -44.231 -68.233  1.00 94.38  ? 21   ILE   C HA   1 
ATOM   16492 H  HB   . ILE   C  3  21  ? -4.077  -43.410 -66.556  1.00 85.75  ? 21   ILE   C HB   1 
ATOM   16493 H  HG12 . ILE   C  3  21  ? -3.606  -45.085 -68.739  1.00 83.46  ? 21   ILE   C HG12 1 
ATOM   16494 H  HG13 . ILE   C  3  21  ? -3.898  -43.560 -69.080  1.00 83.46  ? 21   ILE   C HG13 1 
ATOM   16495 H  HG21 . ILE   C  3  21  ? -3.608  -45.694 -66.236  1.00 81.81  ? 21   ILE   C HG21 1 
ATOM   16496 H  HG22 . ILE   C  3  21  ? -5.026  -45.308 -65.631  1.00 81.81  ? 21   ILE   C HG22 1 
ATOM   16497 H  HG23 . ILE   C  3  21  ? -4.936  -46.058 -67.028  1.00 81.81  ? 21   ILE   C HG23 1 
ATOM   16498 H  HD11 . ILE   C  3  21  ? -1.629  -43.911 -68.998  1.00 80.48  ? 21   ILE   C HD11 1 
ATOM   16499 H  HD12 . ILE   C  3  21  ? -2.053  -42.936 -67.818  1.00 80.48  ? 21   ILE   C HD12 1 
ATOM   16500 H  HD13 . ILE   C  3  21  ? -1.752  -44.466 -67.514  1.00 80.48  ? 21   ILE   C HD13 1 
ATOM   16501 N  N    . SER   C  3  22  ? -7.665  -44.619 -66.314  1.00 87.85  ? 22   SER   C N    1 
ATOM   16502 C  CA   . SER   C  3  22  ? -8.718  -44.703 -65.314  1.00 89.47  ? 22   SER   C CA   1 
ATOM   16503 C  C    . SER   C  3  22  ? -8.366  -45.737 -64.254  1.00 87.02  ? 22   SER   C C    1 
ATOM   16504 O  O    . SER   C  3  22  ? -7.790  -46.787 -64.557  1.00 89.87  ? 22   SER   C O    1 
ATOM   16505 C  CB   . SER   C  3  22  ? -10.056 -45.065 -65.965  1.00 100.04 ? 22   SER   C CB   1 
ATOM   16506 O  OG   . SER   C  3  22  ? -10.992 -45.507 -64.999  1.00 104.90 ? 22   SER   C OG   1 
ATOM   16507 H  H    . SER   C  3  22  ? -7.650  -45.291 -66.849  1.00 105.45 ? 22   SER   C H    1 
ATOM   16508 H  HA   . SER   C  3  22  ? -8.808  -43.844 -64.872  1.00 107.41 ? 22   SER   C HA   1 
ATOM   16509 H  HB2  . SER   C  3  22  ? -10.411 -44.280 -66.411  1.00 120.09 ? 22   SER   C HB2  1 
ATOM   16510 H  HB3  . SER   C  3  22  ? -9.910  -45.775 -66.610  1.00 120.09 ? 22   SER   C HB3  1 
ATOM   16511 H  HG   . SER   C  3  22  ? -11.724 -45.687 -65.369  1.00 125.92 ? 22   SER   C HG   1 
ATOM   16512 N  N    . CYS   C  3  23  ? -8.726  -45.431 -63.010  1.00 82.65  ? 23   CYS   C N    1 
ATOM   16513 C  CA   . CYS   C  3  23  ? -8.485  -46.302 -61.870  1.00 84.32  ? 23   CYS   C CA   1 
ATOM   16514 C  C    . CYS   C  3  23  ? -9.690  -46.220 -60.946  1.00 85.81  ? 23   CYS   C C    1 
ATOM   16515 O  O    . CYS   C  3  23  ? -10.199 -45.128 -60.679  1.00 84.79  ? 23   CYS   C O    1 
ATOM   16516 C  CB   . CYS   C  3  23  ? -7.208  -45.891 -61.127  1.00 83.87  ? 23   CYS   C CB   1 
ATOM   16517 S  SG   . CYS   C  3  23  ? -6.882  -46.763 -59.586  1.00 86.57  ? 23   CYS   C SG   1 
ATOM   16518 H  H    . CYS   C  3  23  ? -9.125  -44.699 -62.797  1.00 99.22  ? 23   CYS   C H    1 
ATOM   16519 H  HA   . CYS   C  3  23  ? -8.379  -47.223 -62.155  1.00 101.22 ? 23   CYS   C HA   1 
ATOM   16520 H  HB2  . CYS   C  3  23  ? -6.452  -46.051 -61.713  1.00 100.68 ? 23   CYS   C HB2  1 
ATOM   16521 H  HB3  . CYS   C  3  23  ? -7.271  -44.947 -60.916  1.00 100.68 ? 23   CYS   C HB3  1 
ATOM   16522 N  N    . ARG   C  3  24  ? -10.148 -47.374 -60.469  1.00 89.44  ? 24   ARG   C N    1 
ATOM   16523 C  CA   . ARG   C  3  24  ? -11.316 -47.450 -59.604  1.00 91.79  ? 24   ARG   C CA   1 
ATOM   16524 C  C    . ARG   C  3  24  ? -11.006 -48.322 -58.397  1.00 89.03  ? 24   ARG   C C    1 
ATOM   16525 O  O    . ARG   C  3  24  ? -10.406 -49.393 -58.531  1.00 89.53  ? 24   ARG   C O    1 
ATOM   16526 C  CB   . ARG   C  3  24  ? -12.533 -48.010 -60.355  1.00 100.12 ? 24   ARG   C CB   1 
ATOM   16527 C  CG   . ARG   C  3  24  ? -13.796 -48.084 -59.508  1.00 108.92 ? 24   ARG   C CG   1 
ATOM   16528 C  CD   . ARG   C  3  24  ? -14.941 -48.748 -60.254  1.00 120.47 ? 24   ARG   C CD   1 
ATOM   16529 N  NE   . ARG   C  3  24  ? -15.819 -47.781 -60.909  1.00 128.05 ? 24   ARG   C NE   1 
ATOM   16530 C  CZ   . ARG   C  3  24  ? -16.787 -47.109 -60.291  1.00 131.17 ? 24   ARG   C CZ   1 
ATOM   16531 N  NH1  . ARG   C  3  24  ? -17.537 -46.253 -60.970  1.00 134.12 ? 24   ARG   C NH1  1 
ATOM   16532 N  NH2  . ARG   C  3  24  ? -17.002 -47.285 -58.993  1.00 128.72 ? 24   ARG   C NH2  1 
ATOM   16533 H  H    . ARG   C  3  24  ? -9.792  -48.139 -60.637  1.00 107.36 ? 24   ARG   C H    1 
ATOM   16534 H  HA   . ARG   C  3  24  ? -11.539 -46.561 -59.285  1.00 110.18 ? 24   ARG   C HA   1 
ATOM   16535 H  HB2  . ARG   C  3  24  ? -12.720 -47.439 -61.116  1.00 120.18 ? 24   ARG   C HB2  1 
ATOM   16536 H  HB3  . ARG   C  3  24  ? -12.326 -48.908 -60.657  1.00 120.18 ? 24   ARG   C HB3  1 
ATOM   16537 H  HG2  . ARG   C  3  24  ? -13.615 -48.601 -58.708  1.00 130.74 ? 24   ARG   C HG2  1 
ATOM   16538 H  HG3  . ARG   C  3  24  ? -14.072 -47.186 -59.267  1.00 130.74 ? 24   ARG   C HG3  1 
ATOM   16539 H  HD2  . ARG   C  3  24  ? -14.578 -49.334 -60.936  1.00 144.60 ? 24   ARG   C HD2  1 
ATOM   16540 H  HD3  . ARG   C  3  24  ? -15.474 -49.260 -59.626  1.00 144.60 ? 24   ARG   C HD3  1 
ATOM   16541 H  HE   . ARG   C  3  24  ? -15.702 -47.636 -61.748  1.00 153.69 ? 24   ARG   C HE   1 
ATOM   16542 H  HH11 . ARG   C  3  24  ? -17.399 -46.132 -61.810  1.00 160.98 ? 24   ARG   C HH11 1 
ATOM   16543 H  HH12 . ARG   C  3  24  ? -18.163 -45.819 -60.570  1.00 160.98 ? 24   ARG   C HH12 1 
ATOM   16544 H  HH21 . ARG   C  3  24  ? -16.515 -47.836 -58.547  1.00 154.50 ? 24   ARG   C HH21 1 
ATOM   16545 H  HH22 . ARG   C  3  24  ? -17.629 -46.848 -58.598  1.00 154.50 ? 24   ARG   C HH22 1 
ATOM   16546 N  N    . ALA   C  3  25  ? -11.421 -47.859 -57.222  1.00 84.94  ? 25   ALA   C N    1 
ATOM   16547 C  CA   . ALA   C  3  25  ? -11.230 -48.579 -55.974  1.00 85.29  ? 25   ALA   C CA   1 
ATOM   16548 C  C    . ALA   C  3  25  ? -12.545 -49.193 -55.513  1.00 90.00  ? 25   ALA   C C    1 
ATOM   16549 O  O    . ALA   C  3  25  ? -13.629 -48.687 -55.818  1.00 92.33  ? 25   ALA   C O    1 
ATOM   16550 C  CB   . ALA   C  3  25  ? -10.683 -47.657 -54.880  1.00 83.53  ? 25   ALA   C CB   1 
ATOM   16551 H  H    . ALA   C  3  25  ? -11.827 -47.107 -57.122  1.00 101.96 ? 25   ALA   C H    1 
ATOM   16552 H  HA   . ALA   C  3  25  ? -10.592 -49.296 -56.114  1.00 102.38 ? 25   ALA   C HA   1 
ATOM   16553 H  HB1  . ALA   C  3  25  ? -10.537 -48.175 -54.073  1.00 100.27 ? 25   ALA   C HB1  1 
ATOM   16554 H  HB2  . ALA   C  3  25  ? -9.846  -47.271 -55.182  1.00 100.27 ? 25   ALA   C HB2  1 
ATOM   16555 H  HB3  . ALA   C  3  25  ? -11.328 -46.953 -54.709  1.00 100.27 ? 25   ALA   C HB3  1 
ATOM   16556 N  N    . SER   C  3  26  ? -12.437 -50.292 -54.767  1.00 91.46  ? 26   SER   C N    1 
ATOM   16557 C  CA   . SER   C  3  26  ? -13.607 -50.979 -54.237  1.00 94.66  ? 26   SER   C CA   1 
ATOM   16558 C  C    . SER   C  3  26  ? -14.236 -50.255 -53.054  1.00 95.71  ? 26   SER   C C    1 
ATOM   16559 O  O    . SER   C  3  26  ? -15.286 -50.694 -52.570  1.00 102.40 ? 26   SER   C O    1 
ATOM   16560 C  CB   . SER   C  3  26  ? -13.231 -52.404 -53.822  1.00 94.49  ? 26   SER   C CB   1 
ATOM   16561 O  OG   . SER   C  3  26  ? -12.283 -52.393 -52.769  1.00 94.53  ? 26   SER   C OG   1 
ATOM   16562 H  H    . SER   C  3  26  ? -11.690 -50.660 -54.554  1.00 109.78 ? 26   SER   C H    1 
ATOM   16563 H  HA   . SER   C  3  26  ? -14.274 -51.036 -54.939  1.00 113.62 ? 26   SER   C HA   1 
ATOM   16564 H  HB2  . SER   C  3  26  ? -14.030 -52.866 -53.522  1.00 113.43 ? 26   SER   C HB2  1 
ATOM   16565 H  HB3  . SER   C  3  26  ? -12.849 -52.864 -54.586  1.00 113.43 ? 26   SER   C HB3  1 
ATOM   16566 H  HG   . SER   C  3  26  ? -12.217 -53.160 -52.434  1.00 113.47 ? 26   SER   C HG   1 
ATOM   16567 N  N    . GLN   C  3  27  ? -13.625 -49.174 -52.572  1.00 92.73  ? 27   GLN   C N    1 
ATOM   16568 C  CA   . GLN   C  3  27  ? -14.164 -48.405 -51.461  1.00 94.26  ? 27   GLN   C CA   1 
ATOM   16569 C  C    . GLN   C  3  27  ? -13.681 -46.968 -51.585  1.00 90.89  ? 27   GLN   C C    1 
ATOM   16570 O  O    . GLN   C  3  27  ? -12.772 -46.660 -52.361  1.00 89.02  ? 27   GLN   C O    1 
ATOM   16571 C  CB   . GLN   C  3  27  ? -13.738 -48.975 -50.103  1.00 96.37  ? 27   GLN   C CB   1 
ATOM   16572 C  CG   . GLN   C  3  27  ? -13.958 -50.467 -49.923  1.00 103.00 ? 27   GLN   C CG   1 
ATOM   16573 C  CD   . GLN   C  3  27  ? -13.508 -50.951 -48.558  1.00 106.22 ? 27   GLN   C CD   1 
ATOM   16574 O  OE1  . GLN   C  3  27  ? -13.228 -50.150 -47.666  1.00 104.61 ? 27   GLN   C OE1  1 
ATOM   16575 N  NE2  . GLN   C  3  27  ? -13.423 -52.265 -48.393  1.00 110.43 ? 27   GLN   C NE2  1 
ATOM   16576 H  H    . GLN   C  3  27  ? -12.884 -48.864 -52.879  1.00 111.31 ? 27   GLN   C H    1 
ATOM   16577 H  HA   . GLN   C  3  27  ? -15.133 -48.428 -51.516  1.00 113.15 ? 27   GLN   C HA   1 
ATOM   16578 H  HB2  . GLN   C  3  27  ? -12.790 -48.807 -49.985  1.00 115.68 ? 27   GLN   C HB2  1 
ATOM   16579 H  HB3  . GLN   C  3  27  ? -14.243 -48.523 -49.409  1.00 115.68 ? 27   GLN   C HB3  1 
ATOM   16580 H  HG2  . GLN   C  3  27  ? -14.904 -50.663 -50.017  1.00 123.64 ? 27   GLN   C HG2  1 
ATOM   16581 H  HG3  . GLN   C  3  27  ? -13.452 -50.947 -50.597  1.00 123.64 ? 27   GLN   C HG3  1 
ATOM   16582 H  HE21 . GLN   C  3  27  ? -13.619 -52.794 -49.043  1.00 132.55 ? 27   GLN   C HE21 1 
ATOM   16583 H  HE22 . GLN   C  3  27  ? -13.172 -52.588 -47.637  1.00 132.55 ? 27   GLN   C HE22 1 
ATOM   16584 N  N    . ASP   C  3  28  ? -14.299 -46.084 -50.807  1.00 89.78  ? 28   ASP   C N    1 
ATOM   16585 C  CA   . ASP   C  3  28  ? -13.824 -44.709 -50.719  1.00 87.78  ? 28   ASP   C CA   1 
ATOM   16586 C  C    . ASP   C  3  28  ? -12.421 -44.695 -50.126  1.00 79.24  ? 28   ASP   C C    1 
ATOM   16587 O  O    . ASP   C  3  28  ? -12.206 -45.192 -49.016  1.00 77.70  ? 28   ASP   C O    1 
ATOM   16588 C  CB   . ASP   C  3  28  ? -14.776 -43.875 -49.863  1.00 90.61  ? 28   ASP   C CB   1 
ATOM   16589 C  CG   . ASP   C  3  28  ? -14.411 -42.403 -49.849  1.00 88.43  ? 28   ASP   C CG   1 
ATOM   16590 O  OD1  . ASP   C  3  28  ? -13.480 -42.012 -50.583  1.00 87.29  ? 28   ASP   C OD1  1 
ATOM   16591 O  OD2  . ASP   C  3  28  ? -15.056 -41.637 -49.103  1.00 88.74  ? 28   ASP   C OD2  1 
ATOM   16592 H  H    . ASP   C  3  28  ? -14.990 -46.254 -50.324  1.00 107.77 ? 28   ASP   C H    1 
ATOM   16593 H  HA   . ASP   C  3  28  ? -13.798 -44.314 -51.605  1.00 105.37 ? 28   ASP   C HA   1 
ATOM   16594 H  HB2  . ASP   C  3  28  ? -15.675 -43.959 -50.217  1.00 108.77 ? 28   ASP   C HB2  1 
ATOM   16595 H  HB3  . ASP   C  3  28  ? -14.748 -44.201 -48.950  1.00 108.77 ? 28   ASP   C HB3  1 
ATOM   16596 N  N    . ILE   C  3  29  ? -11.465 -44.136 -50.866  1.00 71.73  ? 29   ILE   C N    1 
ATOM   16597 C  CA   . ILE   C  3  29  ? -10.079 -44.070 -50.420  1.00 68.85  ? 29   ILE   C CA   1 
ATOM   16598 C  C    . ILE   C  3  29  ? -9.650  -42.642 -50.107  1.00 68.66  ? 29   ILE   C C    1 
ATOM   16599 O  O    . ILE   C  3  29  ? -8.457  -42.384 -49.914  1.00 67.52  ? 29   ILE   C O    1 
ATOM   16600 C  CB   . ILE   C  3  29  ? -9.128  -44.722 -51.440  1.00 66.02  ? 29   ILE   C CB   1 
ATOM   16601 C  CG1  . ILE   C  3  29  ? -9.269  -44.077 -52.821  1.00 61.89  ? 29   ILE   C CG1  1 
ATOM   16602 C  CG2  . ILE   C  3  29  ? -9.398  -46.220 -51.514  1.00 70.70  ? 29   ILE   C CG2  1 
ATOM   16603 C  CD1  . ILE   C  3  29  ? -8.304  -44.645 -53.855  1.00 58.58  ? 29   ILE   C CD1  1 
ATOM   16604 H  H    . ILE   C  3  29  ? -11.598 -43.784 -51.639  1.00 86.12  ? 29   ILE   C H    1 
ATOM   16605 H  HA   . ILE   C  3  29  ? -10.009 -44.573 -49.594  1.00 82.66  ? 29   ILE   C HA   1 
ATOM   16606 H  HB   . ILE   C  3  29  ? -8.217  -44.577 -51.142  1.00 79.26  ? 29   ILE   C HB   1 
ATOM   16607 H  HG12 . ILE   C  3  29  ? -10.171 -44.223 -53.145  1.00 74.30  ? 29   ILE   C HG12 1 
ATOM   16608 H  HG13 . ILE   C  3  29  ? -9.094  -43.126 -52.743  1.00 74.30  ? 29   ILE   C HG13 1 
ATOM   16609 H  HG21 . ILE   C  3  29  ? -8.742  -46.630 -52.100  1.00 84.88  ? 29   ILE   C HG21 1 
ATOM   16610 H  HG22 . ILE   C  3  29  ? -9.329  -46.598 -50.624  1.00 84.88  ? 29   ILE   C HG22 1 
ATOM   16611 H  HG23 . ILE   C  3  29  ? -10.291 -46.363 -51.866  1.00 84.88  ? 29   ILE   C HG23 1 
ATOM   16612 H  HD11 . ILE   C  3  29  ? -8.403  -44.152 -54.684  1.00 70.33  ? 29   ILE   C HD11 1 
ATOM   16613 H  HD12 . ILE   C  3  29  ? -7.397  -44.556 -53.523  1.00 70.33  ? 29   ILE   C HD12 1 
ATOM   16614 H  HD13 . ILE   C  3  29  ? -8.513  -45.581 -54.000  1.00 70.33  ? 29   ILE   C HD13 1 
ATOM   16615 N  N    . SER   C  3  30  ? -10.597 -41.704 -50.054  1.00 66.31  ? 30   SER   C N    1 
ATOM   16616 C  CA   . SER   C  3  30  ? -10.358 -40.371 -49.502  1.00 60.70  ? 30   SER   C CA   1 
ATOM   16617 C  C    . SER   C  3  30  ? -9.130  -39.712 -50.127  1.00 58.52  ? 30   SER   C C    1 
ATOM   16618 O  O    . SER   C  3  30  ? -8.313  -39.091 -49.444  1.00 59.89  ? 30   SER   C O    1 
ATOM   16619 C  CB   . SER   C  3  30  ? -10.226 -40.444 -47.979  1.00 61.45  ? 30   SER   C CB   1 
ATOM   16620 O  OG   . SER   C  3  30  ? -11.338 -41.118 -47.412  1.00 68.77  ? 30   SER   C OG   1 
ATOM   16621 H  H    . SER   C  3  30  ? -11.401 -41.818 -50.337  1.00 79.61  ? 30   SER   C H    1 
ATOM   16622 H  HA   . SER   C  3  30  ? -11.117 -39.809 -49.720  1.00 72.88  ? 30   SER   C HA   1 
ATOM   16623 H  HB2  . SER   C  3  30  ? -9.416  -40.927 -47.754  1.00 73.78  ? 30   SER   C HB2  1 
ATOM   16624 H  HB3  . SER   C  3  30  ? -10.186 -39.544 -47.621  1.00 73.78  ? 30   SER   C HB3  1 
ATOM   16625 H  HG   . SER   C  3  30  ? -11.199 -41.266 -46.597  1.00 82.56  ? 30   SER   C HG   1 
ATOM   16626 N  N    . ASN   C  3  31  ? -8.997  -39.857 -51.445  1.00 58.69  ? 31   ASN   C N    1 
ATOM   16627 C  CA   . ASN   C  3  31  ? -8.015  -39.142 -52.258  1.00 58.27  ? 31   ASN   C CA   1 
ATOM   16628 C  C    . ASN   C  3  31  ? -6.576  -39.577 -52.005  1.00 56.56  ? 31   ASN   C C    1 
ATOM   16629 O  O    . ASN   C  3  31  ? -5.642  -38.873 -52.408  1.00 56.04  ? 31   ASN   C O    1 
ATOM   16630 C  CB   . ASN   C  3  31  ? -8.125  -37.625 -52.057  1.00 60.78  ? 31   ASN   C CB   1 
ATOM   16631 C  CG   . ASN   C  3  31  ? -9.266  -37.020 -52.837  1.00 66.98  ? 31   ASN   C CG   1 
ATOM   16632 O  OD1  . ASN   C  3  31  ? -10.363 -36.833 -52.313  1.00 71.42  ? 31   ASN   C OD1  1 
ATOM   16633 N  ND2  . ASN   C  3  31  ? -9.016  -36.715 -54.105  1.00 68.90  ? 31   ASN   C ND2  1 
ATOM   16634 H  H    . ASN   C  3  31  ? -9.488  -40.388 -51.911  1.00 70.47  ? 31   ASN   C H    1 
ATOM   16635 H  HA   . ASN   C  3  31  ? -8.212  -39.352 -53.185  1.00 69.96  ? 31   ASN   C HA   1 
ATOM   16636 H  HB2  . ASN   C  3  31  ? -8.273  -37.441 -51.116  1.00 72.97  ? 31   ASN   C HB2  1 
ATOM   16637 H  HB3  . ASN   C  3  31  ? -7.302  -37.206 -52.352  1.00 72.97  ? 31   ASN   C HB3  1 
ATOM   16638 H  HD21 . ASN   C  3  31  ? -9.632  -36.367 -54.593  1.00 82.72  ? 31   ASN   C HD21 1 
ATOM   16639 H  HD22 . ASN   C  3  31  ? -8.237  -36.865 -54.437  1.00 82.72  ? 31   ASN   C HD22 1 
ATOM   16640 N  N    . TYR   C  3  32  ? -6.360  -40.715 -51.350  1.00 60.45  ? 32   TYR   C N    1 
ATOM   16641 C  CA   . TYR   C  3  32  ? -5.008  -41.243 -51.159  1.00 62.67  ? 32   TYR   C CA   1 
ATOM   16642 C  C    . TYR   C  3  32  ? -4.710  -42.281 -52.238  1.00 63.19  ? 32   TYR   C C    1 
ATOM   16643 O  O    . TYR   C  3  32  ? -4.568  -43.479 -51.988  1.00 63.80  ? 32   TYR   C O    1 
ATOM   16644 C  CB   . TYR   C  3  32  ? -4.853  -41.838 -49.764  1.00 63.08  ? 32   TYR   C CB   1 
ATOM   16645 C  CG   . TYR   C  3  32  ? -4.787  -40.822 -48.653  1.00 65.64  ? 32   TYR   C CG   1 
ATOM   16646 C  CD1  . TYR   C  3  32  ? -3.677  -40.000 -48.496  1.00 65.91  ? 32   TYR   C CD1  1 
ATOM   16647 C  CD2  . TYR   C  3  32  ? -5.827  -40.700 -47.745  1.00 68.29  ? 32   TYR   C CD2  1 
ATOM   16648 C  CE1  . TYR   C  3  32  ? -3.615  -39.076 -47.471  1.00 68.48  ? 32   TYR   C CE1  1 
ATOM   16649 C  CE2  . TYR   C  3  32  ? -5.775  -39.782 -46.720  1.00 69.14  ? 32   TYR   C CE2  1 
ATOM   16650 C  CZ   . TYR   C  3  32  ? -4.667  -38.971 -46.587  1.00 69.32  ? 32   TYR   C CZ   1 
ATOM   16651 O  OH   . TYR   C  3  32  ? -4.609  -38.053 -45.563  1.00 71.99  ? 32   TYR   C OH   1 
ATOM   16652 H  H    . TYR   C  3  32  ? -6.979  -41.202 -51.006  1.00 72.58  ? 32   TYR   C H    1 
ATOM   16653 H  HA   . TYR   C  3  32  ? -4.379  -40.510 -51.246  1.00 75.24  ? 32   TYR   C HA   1 
ATOM   16654 H  HB2  . TYR   C  3  32  ? -5.612  -42.415 -49.588  1.00 75.73  ? 32   TYR   C HB2  1 
ATOM   16655 H  HB3  . TYR   C  3  32  ? -4.031  -42.353 -49.738  1.00 75.73  ? 32   TYR   C HB3  1 
ATOM   16656 H  HD1  . TYR   C  3  32  ? -2.966  -40.074 -49.090  1.00 79.13  ? 32   TYR   C HD1  1 
ATOM   16657 H  HD2  . TYR   C  3  32  ? -6.574  -41.249 -47.830  1.00 81.98  ? 32   TYR   C HD2  1 
ATOM   16658 H  HE1  . TYR   C  3  32  ? -2.868  -38.530 -47.379  1.00 82.21  ? 32   TYR   C HE1  1 
ATOM   16659 H  HE2  . TYR   C  3  32  ? -6.482  -39.709 -46.120  1.00 83.01  ? 32   TYR   C HE2  1 
ATOM   16660 H  HH   . TYR   C  3  32  ? -5.385  -37.807 -45.354  1.00 86.43  ? 32   TYR   C HH   1 
ATOM   16661 N  N    . LEU   C  3  33  ? -4.619  -41.783 -53.464  1.00 55.08  ? 33   LEU   C N    1 
ATOM   16662 C  CA   . LEU   C  3  33  ? -4.298  -42.595 -54.626  1.00 58.93  ? 33   LEU   C CA   1 
ATOM   16663 C  C    . LEU   C  3  33  ? -3.076  -41.996 -55.301  1.00 52.38  ? 33   LEU   C C    1 
ATOM   16664 O  O    . LEU   C  3  33  ? -3.011  -40.779 -55.506  1.00 45.85  ? 33   LEU   C O    1 
ATOM   16665 C  CB   . LEU   C  3  33  ? -5.470  -42.652 -55.604  1.00 64.94  ? 33   LEU   C CB   1 
ATOM   16666 C  CG   . LEU   C  3  33  ? -5.278  -43.682 -56.717  1.00 67.56  ? 33   LEU   C CG   1 
ATOM   16667 C  CD1  . LEU   C  3  33  ? -6.125  -44.910 -56.456  1.00 75.90  ? 33   LEU   C CD1  1 
ATOM   16668 C  CD2  . LEU   C  3  33  ? -5.589  -43.098 -58.086  1.00 71.72  ? 33   LEU   C CD2  1 
ATOM   16669 H  H    . LEU   C  3  33  ? -4.744  -40.953 -53.651  1.00 66.13  ? 33   LEU   C H    1 
ATOM   16670 H  HA   . LEU   C  3  33  ? -4.095  -43.503 -54.352  1.00 70.75  ? 33   LEU   C HA   1 
ATOM   16671 H  HB2  . LEU   C  3  33  ? -6.274  -42.887 -55.115  1.00 77.96  ? 33   LEU   C HB2  1 
ATOM   16672 H  HB3  . LEU   C  3  33  ? -5.575  -41.781 -56.017  1.00 77.96  ? 33   LEU   C HB3  1 
ATOM   16673 H  HG   . LEU   C  3  33  ? -4.345  -43.948 -56.725  1.00 81.11  ? 33   LEU   C HG   1 
ATOM   16674 H  HD11 . LEU   C  3  33  ? -5.844  -45.620 -57.054  1.00 91.11  ? 33   LEU   C HD11 1 
ATOM   16675 H  HD12 . LEU   C  3  33  ? -6.004  -45.187 -55.534  1.00 91.11  ? 33   LEU   C HD12 1 
ATOM   16676 H  HD13 . LEU   C  3  33  ? -7.056  -44.692 -56.616  1.00 91.11  ? 33   LEU   C HD13 1 
ATOM   16677 H  HD21 . LEU   C  3  33  ? -5.988  -42.221 -57.973  1.00 86.10  ? 33   LEU   C HD21 1 
ATOM   16678 H  HD22 . LEU   C  3  33  ? -4.764  -43.023 -58.592  1.00 86.10  ? 33   LEU   C HD22 1 
ATOM   16679 H  HD23 . LEU   C  3  33  ? -6.207  -43.686 -58.548  1.00 86.10  ? 33   LEU   C HD23 1 
ATOM   16680 N  N    . SER   C  3  34  ? -2.111  -42.842 -55.640  1.00 54.64  ? 34   SER   C N    1 
ATOM   16681 C  CA   . SER   C  3  34  ? -0.868  -42.397 -56.248  1.00 56.55  ? 34   SER   C CA   1 
ATOM   16682 C  C    . SER   C  3  34  ? -0.659  -43.116 -57.572  1.00 60.73  ? 34   SER   C C    1 
ATOM   16683 O  O    . SER   C  3  34  ? -1.090  -44.259 -57.750  1.00 63.00  ? 34   SER   C O    1 
ATOM   16684 C  CB   . SER   C  3  34  ? 0.319   -42.652 -55.312  1.00 56.17  ? 34   SER   C CB   1 
ATOM   16685 O  OG   . SER   C  3  34  ? 0.005   -42.268 -53.982  1.00 60.37  ? 34   SER   C OG   1 
ATOM   16686 H  H    . SER   C  3  34  ? -2.156  -43.693 -55.525  1.00 65.61  ? 34   SER   C H    1 
ATOM   16687 H  HA   . SER   C  3  34  ? -0.909  -41.445 -56.429  1.00 67.90  ? 34   SER   C HA   1 
ATOM   16688 H  HB2  . SER   C  3  34  ? 0.534   -43.598 -55.325  1.00 67.44  ? 34   SER   C HB2  1 
ATOM   16689 H  HB3  . SER   C  3  34  ? 1.080   -42.134 -55.618  1.00 67.44  ? 34   SER   C HB3  1 
ATOM   16690 H  HG   . SER   C  3  34  ? 0.325   -42.825 -53.440  1.00 72.48  ? 34   SER   C HG   1 
ATOM   16691 N  N    . TRP   C  3  35  ? 0.004   -42.437 -58.505  1.00 62.31  ? 35   TRP   C N    1 
ATOM   16692 C  CA   . TRP   C  3  35  ? 0.319   -43.004 -59.808  1.00 66.13  ? 35   TRP   C CA   1 
ATOM   16693 C  C    . TRP   C  3  35  ? 1.824   -43.176 -59.962  1.00 62.65  ? 35   TRP   C C    1 
ATOM   16694 O  O    . TRP   C  3  35  ? 2.604   -42.284 -59.609  1.00 63.28  ? 35   TRP   C O    1 
ATOM   16695 C  CB   . TRP   C  3  35  ? -0.218  -42.129 -60.943  1.00 66.33  ? 35   TRP   C CB   1 
ATOM   16696 C  CG   . TRP   C  3  35  ? -1.709  -42.124 -61.033  1.00 67.89  ? 35   TRP   C CG   1 
ATOM   16697 C  CD1  . TRP   C  3  35  ? -2.568  -41.294 -60.374  1.00 65.73  ? 35   TRP   C CD1  1 
ATOM   16698 C  CD2  . TRP   C  3  35  ? -2.522  -42.996 -61.828  1.00 67.80  ? 35   TRP   C CD2  1 
ATOM   16699 N  NE1  . TRP   C  3  35  ? -3.867  -41.593 -60.712  1.00 66.42  ? 35   TRP   C NE1  1 
ATOM   16700 C  CE2  . TRP   C  3  35  ? -3.865  -42.634 -61.604  1.00 66.27  ? 35   TRP   C CE2  1 
ATOM   16701 C  CE3  . TRP   C  3  35  ? -2.243  -44.042 -62.714  1.00 68.71  ? 35   TRP   C CE3  1 
ATOM   16702 C  CZ2  . TRP   C  3  35  ? -4.928  -43.283 -62.231  1.00 68.15  ? 35   TRP   C CZ2  1 
ATOM   16703 C  CZ3  . TRP   C  3  35  ? -3.299  -44.686 -63.335  1.00 70.36  ? 35   TRP   C CZ3  1 
ATOM   16704 C  CH2  . TRP   C  3  35  ? -4.625  -44.305 -63.089  1.00 70.93  ? 35   TRP   C CH2  1 
ATOM   16705 H  H    . TRP   C  3  35  ? 0.285   -41.630 -58.402  1.00 74.81  ? 35   TRP   C H    1 
ATOM   16706 H  HA   . TRP   C  3  35  ? -0.094  -43.879 -59.876  1.00 79.40  ? 35   TRP   C HA   1 
ATOM   16707 H  HB2  . TRP   C  3  35  ? 0.075   -41.215 -60.800  1.00 79.63  ? 35   TRP   C HB2  1 
ATOM   16708 H  HB3  . TRP   C  3  35  ? 0.130   -42.460 -61.786  1.00 79.63  ? 35   TRP   C HB3  1 
ATOM   16709 H  HD1  . TRP   C  3  35  ? -2.313  -40.624 -59.782  1.00 78.92  ? 35   TRP   C HD1  1 
ATOM   16710 H  HE1  . TRP   C  3  35  ? -4.566  -41.192 -60.413  1.00 79.74  ? 35   TRP   C HE1  1 
ATOM   16711 H  HE3  . TRP   C  3  35  ? -1.365  -44.300 -62.882  1.00 82.49  ? 35   TRP   C HE3  1 
ATOM   16712 H  HZ2  . TRP   C  3  35  ? -5.809  -43.032 -62.071  1.00 81.82  ? 35   TRP   C HZ2  1 
ATOM   16713 H  HZ3  . TRP   C  3  35  ? -3.126  -45.383 -63.926  1.00 84.47  ? 35   TRP   C HZ3  1 
ATOM   16714 H  HH2  . TRP   C  3  35  ? -5.315  -44.756 -63.520  1.00 85.16  ? 35   TRP   C HH2  1 
ATOM   16715 N  N    . TYR   C  3  36  ? 2.217   -44.330 -60.494  1.00 61.41  ? 36   TYR   C N    1 
ATOM   16716 C  CA   . TYR   C  3  36  ? 3.610   -44.665 -60.741  1.00 59.08  ? 36   TYR   C CA   1 
ATOM   16717 C  C    . TYR   C  3  36  ? 3.802   -45.043 -62.204  1.00 62.70  ? 36   TYR   C C    1 
ATOM   16718 O  O    . TYR   C  3  36  ? 2.894   -45.575 -62.851  1.00 66.51  ? 36   TYR   C O    1 
ATOM   16719 C  CB   . TYR   C  3  36  ? 4.074   -45.830 -59.854  1.00 55.74  ? 36   TYR   C CB   1 
ATOM   16720 C  CG   . TYR   C  3  36  ? 3.899   -45.600 -58.370  1.00 54.38  ? 36   TYR   C CG   1 
ATOM   16721 C  CD1  . TYR   C  3  36  ? 2.706   -45.918 -57.735  1.00 57.05  ? 36   TYR   C CD1  1 
ATOM   16722 C  CD2  . TYR   C  3  36  ? 4.930   -45.077 -57.601  1.00 54.16  ? 36   TYR   C CD2  1 
ATOM   16723 C  CE1  . TYR   C  3  36  ? 2.541   -45.716 -56.379  1.00 56.92  ? 36   TYR   C CE1  1 
ATOM   16724 C  CE2  . TYR   C  3  36  ? 4.775   -44.872 -56.243  1.00 54.74  ? 36   TYR   C CE2  1 
ATOM   16725 C  CZ   . TYR   C  3  36  ? 3.579   -45.192 -55.638  1.00 53.01  ? 36   TYR   C CZ   1 
ATOM   16726 O  OH   . TYR   C  3  36  ? 3.419   -44.988 -54.286  1.00 52.83  ? 36   TYR   C OH   1 
ATOM   16727 H  H    . TYR   C  3  36  ? 1.674   -44.955 -60.728  1.00 73.73  ? 36   TYR   C H    1 
ATOM   16728 H  HA   . TYR   C  3  36  ? 4.161   -43.892 -60.545  1.00 70.93  ? 36   TYR   C HA   1 
ATOM   16729 H  HB2  . TYR   C  3  36  ? 3.562   -46.619 -60.090  1.00 66.92  ? 36   TYR   C HB2  1 
ATOM   16730 H  HB3  . TYR   C  3  36  ? 5.017   -45.984 -60.017  1.00 66.92  ? 36   TYR   C HB3  1 
ATOM   16731 H  HD1  . TYR   C  3  36  ? 2.005   -46.274 -58.232  1.00 68.50  ? 36   TYR   C HD1  1 
ATOM   16732 H  HD2  . TYR   C  3  36  ? 5.738   -44.861 -58.007  1.00 65.03  ? 36   TYR   C HD2  1 
ATOM   16733 H  HE1  . TYR   C  3  36  ? 1.736   -45.931 -55.968  1.00 68.34  ? 36   TYR   C HE1  1 
ATOM   16734 H  HE2  . TYR   C  3  36  ? 5.474   -44.520 -55.741  1.00 65.72  ? 36   TYR   C HE2  1 
ATOM   16735 H  HH   . TYR   C  3  36  ? 2.644   -45.211 -54.051  1.00 63.43  ? 36   TYR   C HH   1 
ATOM   16736 N  N    . GLN   C  3  37  ? 4.999   -44.768 -62.716  1.00 61.83  ? 37   GLN   C N    1 
ATOM   16737 C  CA   . GLN   C  3  37  ? 5.388   -45.111 -64.079  1.00 62.20  ? 37   GLN   C CA   1 
ATOM   16738 C  C    . GLN   C  3  37  ? 6.497   -46.152 -64.034  1.00 62.85  ? 37   GLN   C C    1 
ATOM   16739 O  O    . GLN   C  3  37  ? 7.516   -45.948 -63.366  1.00 59.41  ? 37   GLN   C O    1 
ATOM   16740 C  CB   . GLN   C  3  37  ? 5.862   -43.867 -64.838  1.00 62.10  ? 37   GLN   C CB   1 
ATOM   16741 C  CG   . GLN   C  3  37  ? 6.556   -44.135 -66.172  1.00 64.60  ? 37   GLN   C CG   1 
ATOM   16742 C  CD   . GLN   C  3  37  ? 7.422   -42.970 -66.609  1.00 67.39  ? 37   GLN   C CD   1 
ATOM   16743 O  OE1  . GLN   C  3  37  ? 8.509   -42.758 -66.072  1.00 69.09  ? 37   GLN   C OE1  1 
ATOM   16744 N  NE2  . GLN   C  3  37  ? 6.941   -42.205 -67.581  1.00 69.41  ? 37   GLN   C NE2  1 
ATOM   16745 H  H    . GLN   C  3  37  ? 5.623   -44.370 -62.277  1.00 74.23  ? 37   GLN   C H    1 
ATOM   16746 H  HA   . GLN   C  3  37  ? 4.629   -45.487 -64.551  1.00 74.68  ? 37   GLN   C HA   1 
ATOM   16747 H  HB2  . GLN   C  3  37  ? 5.091   -43.309 -65.021  1.00 74.55  ? 37   GLN   C HB2  1 
ATOM   16748 H  HB3  . GLN   C  3  37  ? 6.492   -43.389 -64.277  1.00 74.55  ? 37   GLN   C HB3  1 
ATOM   16749 H  HG2  . GLN   C  3  37  ? 7.123   -44.918 -66.085  1.00 77.56  ? 37   GLN   C HG2  1 
ATOM   16750 H  HG3  . GLN   C  3  37  ? 5.884   -44.287 -66.855  1.00 77.56  ? 37   GLN   C HG3  1 
ATOM   16751 H  HE21 . GLN   C  3  37  ? 6.175   -42.383 -67.929  1.00 83.33  ? 37   GLN   C HE21 1 
ATOM   16752 H  HE22 . GLN   C  3  37  ? 7.397   -41.532 -67.863  1.00 83.33  ? 37   GLN   C HE22 1 
ATOM   16753 N  N    . GLN   C  3  38  ? 6.306   -47.255 -64.756  1.00 65.72  ? 38   GLN   C N    1 
ATOM   16754 C  CA   . GLN   C  3  38  ? 7.328   -48.286 -64.891  1.00 64.38  ? 38   GLN   C CA   1 
ATOM   16755 C  C    . GLN   C  3  38  ? 7.718   -48.402 -66.356  1.00 62.82  ? 38   GLN   C C    1 
ATOM   16756 O  O    . GLN   C  3  38  ? 6.870   -48.685 -67.208  1.00 60.93  ? 38   GLN   C O    1 
ATOM   16757 C  CB   . GLN   C  3  38  ? 6.845   -49.638 -64.361  1.00 65.78  ? 38   GLN   C CB   1 
ATOM   16758 C  CG   . GLN   C  3  38  ? 7.936   -50.708 -64.364  1.00 67.56  ? 38   GLN   C CG   1 
ATOM   16759 C  CD   . GLN   C  3  38  ? 7.584   -51.916 -63.518  1.00 69.69  ? 38   GLN   C CD   1 
ATOM   16760 O  OE1  . GLN   C  3  38  ? 6.457   -52.409 -63.557  1.00 70.18  ? 38   GLN   C OE1  1 
ATOM   16761 N  NE2  . GLN   C  3  38  ? 8.551   -52.397 -62.742  1.00 71.70  ? 38   GLN   C NE2  1 
ATOM   16762 H  H    . GLN   C  3  38  ? 5.580   -47.429 -65.182  1.00 78.90  ? 38   GLN   C H    1 
ATOM   16763 H  HA   . GLN   C  3  38  ? 8.108   -48.023 -64.378  1.00 77.29  ? 38   GLN   C HA   1 
ATOM   16764 H  HB2  . GLN   C  3  38  ? 6.538   -49.527 -63.448  1.00 78.97  ? 38   GLN   C HB2  1 
ATOM   16765 H  HB3  . GLN   C  3  38  ? 6.117   -49.953 -64.920  1.00 78.97  ? 38   GLN   C HB3  1 
ATOM   16766 H  HG2  . GLN   C  3  38  ? 8.078   -51.012 -65.274  1.00 81.11  ? 38   GLN   C HG2  1 
ATOM   16767 H  HG3  . GLN   C  3  38  ? 8.754   -50.325 -64.011  1.00 81.11  ? 38   GLN   C HG3  1 
ATOM   16768 H  HE21 . GLN   C  3  38  ? 9.325   -52.024 -62.739  1.00 86.08  ? 38   GLN   C HE21 1 
ATOM   16769 H  HE22 . GLN   C  3  38  ? 8.401   -53.081 -62.243  1.00 86.08  ? 38   GLN   C HE22 1 
ATOM   16770 N  N    . LYS   C  3  39  ? 8.993   -48.189 -66.640  1.00 69.48  ? 39   LYS   C N    1 
ATOM   16771 C  CA   . LYS   C  3  39  ? 9.516   -48.304 -67.991  1.00 76.61  ? 39   LYS   C CA   1 
ATOM   16772 C  C    . LYS   C  3  39  ? 9.984   -49.728 -68.253  1.00 79.70  ? 39   LYS   C C    1 
ATOM   16773 O  O    . LYS   C  3  39  ? 10.200  -50.505 -67.319  1.00 79.70  ? 39   LYS   C O    1 
ATOM   16774 C  CB   . LYS   C  3  39  ? 10.655  -47.310 -68.188  1.00 79.21  ? 39   LYS   C CB   1 
ATOM   16775 C  CG   . LYS   C  3  39  ? 10.166  -45.875 -68.315  1.00 80.42  ? 39   LYS   C CG   1 
ATOM   16776 C  CD   . LYS   C  3  39  ? 11.270  -44.870 -68.050  1.00 84.44  ? 39   LYS   C CD   1 
ATOM   16777 C  CE   . LYS   C  3  39  ? 10.893  -43.492 -68.567  1.00 86.79  ? 39   LYS   C CE   1 
ATOM   16778 N  NZ   . LYS   C  3  39  ? 10.744  -43.485 -70.049  1.00 90.48  ? 39   LYS   C NZ   1 
ATOM   16779 H  H    . LYS   C  3  39  ? 9.587   -47.972 -66.057  1.00 83.41  ? 39   LYS   C H    1 
ATOM   16780 H  HA   . LYS   C  3  39  ? 8.827   -48.094 -68.640  1.00 91.97  ? 39   LYS   C HA   1 
ATOM   16781 H  HB2  . LYS   C  3  39  ? 11.253  -47.358 -67.426  1.00 95.09  ? 39   LYS   C HB2  1 
ATOM   16782 H  HB3  . LYS   C  3  39  ? 11.135  -47.536 -69.000  1.00 95.09  ? 39   LYS   C HB3  1 
ATOM   16783 H  HG2  . LYS   C  3  39  ? 9.834   -45.730 -69.214  1.00 96.54  ? 39   LYS   C HG2  1 
ATOM   16784 H  HG3  . LYS   C  3  39  ? 9.457   -45.722 -67.671  1.00 96.54  ? 39   LYS   C HG3  1 
ATOM   16785 H  HD2  . LYS   C  3  39  ? 11.426  -44.806 -67.094  1.00 101.37 ? 39   LYS   C HD2  1 
ATOM   16786 H  HD3  . LYS   C  3  39  ? 12.081  -45.154 -68.500  1.00 101.37 ? 39   LYS   C HD3  1 
ATOM   16787 H  HE2  . LYS   C  3  39  ? 10.047  -43.222 -68.174  1.00 104.19 ? 39   LYS   C HE2  1 
ATOM   16788 H  HE3  . LYS   C  3  39  ? 11.587  -42.858 -68.327  1.00 104.19 ? 39   LYS   C HE3  1 
ATOM   16789 H  HZ1  . LYS   C  3  39  ? 11.378  -42.981 -70.416  1.00 108.62 ? 39   LYS   C HZ1  1 
ATOM   16790 H  HZ2  . LYS   C  3  39  ? 10.814  -44.314 -70.366  1.00 108.62 ? 39   LYS   C HZ2  1 
ATOM   16791 H  HZ3  . LYS   C  3  39  ? 9.947   -43.157 -70.273  1.00 108.62 ? 39   LYS   C HZ3  1 
ATOM   16792 N  N    . PRO   C  3  40  ? 10.146  -50.107 -69.524  1.00 84.13  ? 40   PRO   C N    1 
ATOM   16793 C  CA   . PRO   C  3  40  ? 10.399  -51.524 -69.836  1.00 87.65  ? 40   PRO   C CA   1 
ATOM   16794 C  C    . PRO   C  3  40  ? 11.571  -52.126 -69.082  1.00 89.72  ? 40   PRO   C C    1 
ATOM   16795 O  O    . PRO   C  3  40  ? 11.563  -53.332 -68.806  1.00 90.51  ? 40   PRO   C O    1 
ATOM   16796 C  CB   . PRO   C  3  40  ? 10.658  -51.509 -71.350  1.00 93.24  ? 40   PRO   C CB   1 
ATOM   16797 C  CG   . PRO   C  3  40  ? 10.024  -50.257 -71.844  1.00 93.33  ? 40   PRO   C CG   1 
ATOM   16798 C  CD   . PRO   C  3  40  ? 10.143  -49.264 -70.732  1.00 88.26  ? 40   PRO   C CD   1 
ATOM   16799 H  HA   . PRO   C  3  40  ? 9.600   -52.042 -69.647  1.00 105.22 ? 40   PRO   C HA   1 
ATOM   16800 H  HB2  . PRO   C  3  40  ? 11.612  -51.504 -71.521  1.00 111.93 ? 40   PRO   C HB2  1 
ATOM   16801 H  HB3  . PRO   C  3  40  ? 10.251  -52.288 -71.761  1.00 111.93 ? 40   PRO   C HB3  1 
ATOM   16802 H  HG2  . PRO   C  3  40  ? 10.492  -49.945 -72.634  1.00 112.04 ? 40   PRO   C HG2  1 
ATOM   16803 H  HG3  . PRO   C  3  40  ? 9.092   -50.425 -72.055  1.00 112.04 ? 40   PRO   C HG3  1 
ATOM   16804 H  HD2  . PRO   C  3  40  ? 10.969  -48.761 -70.805  1.00 105.94 ? 40   PRO   C HD2  1 
ATOM   16805 H  HD3  . PRO   C  3  40  ? 9.385   -48.658 -70.728  1.00 105.94 ? 40   PRO   C HD3  1 
ATOM   16806 N  N    . ASP   C  3  41  ? 12.578  -51.326 -68.734  1.00 92.17  ? 41   ASP   C N    1 
ATOM   16807 C  CA   . ASP   C  3  41  ? 13.750  -51.858 -68.050  1.00 95.69  ? 41   ASP   C CA   1 
ATOM   16808 C  C    . ASP   C  3  41  ? 13.483  -52.203 -66.591  1.00 97.91  ? 41   ASP   C C    1 
ATOM   16809 O  O    . ASP   C  3  41  ? 14.378  -52.747 -65.933  1.00 104.94 ? 41   ASP   C O    1 
ATOM   16810 C  CB   . ASP   C  3  41  ? 14.907  -50.858 -68.142  1.00 97.44  ? 41   ASP   C CB   1 
ATOM   16811 C  CG   . ASP   C  3  41  ? 14.598  -49.536 -67.461  1.00 97.87  ? 41   ASP   C CG   1 
ATOM   16812 O  OD1  . ASP   C  3  41  ? 13.477  -49.376 -66.934  1.00 97.54  ? 41   ASP   C OD1  1 
ATOM   16813 O  OD2  . ASP   C  3  41  ? 15.483  -48.655 -67.454  1.00 100.60 ? 41   ASP   C OD2  1 
ATOM   16814 H  H    . ASP   C  3  41  ? 12.604  -50.479 -68.882  1.00 110.64 ? 41   ASP   C H    1 
ATOM   16815 H  HA   . ASP   C  3  41  ? 14.024  -52.673 -68.499  1.00 114.87 ? 41   ASP   C HA   1 
ATOM   16816 H  HB2  . ASP   C  3  41  ? 15.689  -51.239 -67.714  1.00 116.96 ? 41   ASP   C HB2  1 
ATOM   16817 H  HB3  . ASP   C  3  41  ? 15.095  -50.677 -69.076  1.00 116.96 ? 41   ASP   C HB3  1 
ATOM   16818 N  N    . GLY   C  3  42  ? 12.289  -51.915 -66.074  1.00 91.26  ? 42   GLY   C N    1 
ATOM   16819 C  CA   . GLY   C  3  42  ? 11.954  -52.149 -64.689  1.00 85.46  ? 42   GLY   C CA   1 
ATOM   16820 C  C    . GLY   C  3  42  ? 11.923  -50.898 -63.835  1.00 80.36  ? 42   GLY   C C    1 
ATOM   16821 O  O    . GLY   C  3  42  ? 11.336  -50.922 -62.747  1.00 80.13  ? 42   GLY   C O    1 
ATOM   16822 H  H    . GLY   C  3  42  ? 11.643  -51.574 -66.527  1.00 109.55 ? 42   GLY   C H    1 
ATOM   16823 H  HA2  . GLY   C  3  42  ? 11.078  -52.562 -64.644  1.00 102.58 ? 42   GLY   C HA2  1 
ATOM   16824 H  HA3  . GLY   C  3  42  ? 12.609  -52.754 -64.307  1.00 102.58 ? 42   GLY   C HA3  1 
ATOM   16825 N  N    . THR   C  3  43  ? 12.541  -49.813 -64.301  1.00 79.06  ? 43   THR   C N    1 
ATOM   16826 C  CA   . THR   C  3  43  ? 12.549  -48.560 -63.557  1.00 76.15  ? 43   THR   C CA   1 
ATOM   16827 C  C    . THR   C  3  43  ? 11.139  -48.185 -63.123  1.00 70.97  ? 43   THR   C C    1 
ATOM   16828 O  O    . THR   C  3  43  ? 10.177  -48.374 -63.867  1.00 72.09  ? 43   THR   C O    1 
ATOM   16829 C  CB   . THR   C  3  43  ? 13.145  -47.447 -64.424  1.00 79.54  ? 43   THR   C CB   1 
ATOM   16830 O  OG1  . THR   C  3  43  ? 14.520  -47.738 -64.704  1.00 81.50  ? 43   THR   C OG1  1 
ATOM   16831 C  CG2  . THR   C  3  43  ? 13.041  -46.096 -63.727  1.00 81.08  ? 43   THR   C CG2  1 
ATOM   16832 H  H    . THR   C  3  43  ? 12.964  -49.778 -65.048  1.00 94.91  ? 43   THR   C H    1 
ATOM   16833 H  HA   . THR   C  3  43  ? 13.097  -48.659 -62.762  1.00 91.42  ? 43   THR   C HA   1 
ATOM   16834 H  HB   . THR   C  3  43  ? 12.650  -47.392 -65.256  1.00 95.49  ? 43   THR   C HB   1 
ATOM   16835 H  HG1  . THR   C  3  43  ? 14.834  -47.165 -65.232  1.00 97.84  ? 43   THR   C HG1  1 
ATOM   16836 H  HG21 . THR   C  3  43  ? 13.512  -45.421 -64.241  1.00 97.33  ? 43   THR   C HG21 1 
ATOM   16837 H  HG22 . THR   C  3  43  ? 12.110  -45.836 -63.645  1.00 97.33  ? 43   THR   C HG22 1 
ATOM   16838 H  HG23 . THR   C  3  43  ? 13.433  -46.148 -62.842  1.00 97.33  ? 43   THR   C HG23 1 
ATOM   16839 N  N    . VAL   C  3  44  ? 11.025  -47.648 -61.909  1.00 62.45  ? 44   VAL   C N    1 
ATOM   16840 C  CA   . VAL   C  3  44  ? 9.751   -47.210 -61.350  1.00 59.40  ? 44   VAL   C CA   1 
ATOM   16841 C  C    . VAL   C  3  44  ? 9.929   -45.803 -60.798  1.00 56.43  ? 44   VAL   C C    1 
ATOM   16842 O  O    . VAL   C  3  44  ? 10.848  -45.553 -60.011  1.00 56.41  ? 44   VAL   C O    1 
ATOM   16843 C  CB   . VAL   C  3  44  ? 9.249   -48.158 -60.243  1.00 62.52  ? 44   VAL   C CB   1 
ATOM   16844 C  CG1  . VAL   C  3  44  ? 7.935   -47.649 -59.657  1.00 61.00  ? 44   VAL   C CG1  1 
ATOM   16845 C  CG2  . VAL   C  3  44  ? 9.085   -49.571 -60.781  1.00 66.23  ? 44   VAL   C CG2  1 
ATOM   16846 H  H    . VAL   C  3  44  ? 11.690  -47.524 -61.378  1.00 74.98  ? 44   VAL   C H    1 
ATOM   16847 H  HA   . VAL   C  3  44  ? 9.086   -47.186 -62.056  1.00 71.32  ? 44   VAL   C HA   1 
ATOM   16848 H  HB   . VAL   C  3  44  ? 9.907   -48.182 -59.531  1.00 75.06  ? 44   VAL   C HB   1 
ATOM   16849 H  HG11 . VAL   C  3  44  ? 7.613   -48.287 -59.001  1.00 73.24  ? 44   VAL   C HG11 1 
ATOM   16850 H  HG12 . VAL   C  3  44  ? 8.089   -46.790 -59.235  1.00 73.24  ? 44   VAL   C HG12 1 
ATOM   16851 H  HG13 . VAL   C  3  44  ? 7.286   -47.554 -60.372  1.00 73.24  ? 44   VAL   C HG13 1 
ATOM   16852 H  HG21 . VAL   C  3  44  ? 8.759   -50.144 -60.069  1.00 79.51  ? 44   VAL   C HG21 1 
ATOM   16853 H  HG22 . VAL   C  3  44  ? 8.448   -49.558 -61.513  1.00 79.51  ? 44   VAL   C HG22 1 
ATOM   16854 H  HG23 . VAL   C  3  44  ? 9.945   -49.890 -61.096  1.00 79.51  ? 44   VAL   C HG23 1 
ATOM   16855 N  N    . LYS   C  3  45  ? 9.046   -44.892 -61.203  1.00 56.84  ? 45   LYS   C N    1 
ATOM   16856 C  CA   . LYS   C  3  45  ? 9.056   -43.518 -60.726  1.00 58.08  ? 45   LYS   C CA   1 
ATOM   16857 C  C    . LYS   C  3  45  ? 7.688   -43.162 -60.167  1.00 59.18  ? 45   LYS   C C    1 
ATOM   16858 O  O    . LYS   C  3  45  ? 6.660   -43.570 -60.715  1.00 61.24  ? 45   LYS   C O    1 
ATOM   16859 C  CB   . LYS   C  3  45  ? 9.409   -42.533 -61.846  1.00 62.64  ? 45   LYS   C CB   1 
ATOM   16860 C  CG   . LYS   C  3  45  ? 10.822  -42.656 -62.383  1.00 73.38  ? 45   LYS   C CG   1 
ATOM   16861 C  CD   . LYS   C  3  45  ? 11.027  -41.771 -63.609  1.00 84.45  ? 45   LYS   C CD   1 
ATOM   16862 C  CE   . LYS   C  3  45  ? 10.799  -40.297 -63.295  1.00 88.27  ? 45   LYS   C CE   1 
ATOM   16863 N  NZ   . LYS   C  3  45  ? 11.079  -39.423 -64.467  1.00 93.40  ? 45   LYS   C NZ   1 
ATOM   16864 H  H    . LYS   C  3  45  ? 8.418   -45.054 -61.768  1.00 68.24  ? 45   LYS   C H    1 
ATOM   16865 H  HA   . LYS   C  3  45  ? 9.717   -43.436 -60.021  1.00 69.73  ? 45   LYS   C HA   1 
ATOM   16866 H  HB2  . LYS   C  3  45  ? 8.801   -42.680 -62.588  1.00 75.20  ? 45   LYS   C HB2  1 
ATOM   16867 H  HB3  . LYS   C  3  45  ? 9.304   -41.630 -61.506  1.00 75.20  ? 45   LYS   C HB3  1 
ATOM   16868 H  HG2  . LYS   C  3  45  ? 11.452  -42.381 -61.699  1.00 88.09  ? 45   LYS   C HG2  1 
ATOM   16869 H  HG3  . LYS   C  3  45  ? 10.990  -43.576 -62.639  1.00 88.09  ? 45   LYS   C HG3  1 
ATOM   16870 H  HD2  . LYS   C  3  45  ? 11.937  -41.875 -63.929  1.00 101.38 ? 45   LYS   C HD2  1 
ATOM   16871 H  HD3  . LYS   C  3  45  ? 10.400  -42.033 -64.301  1.00 101.38 ? 45   LYS   C HD3  1 
ATOM   16872 H  HE2  . LYS   C  3  45  ? 9.873   -40.166 -63.034  1.00 105.97 ? 45   LYS   C HE2  1 
ATOM   16873 H  HE3  . LYS   C  3  45  ? 11.388  -40.030 -62.571  1.00 105.97 ? 45   LYS   C HE3  1 
ATOM   16874 H  HZ1  . LYS   C  3  45  ? 10.959  -38.570 -64.247  1.00 112.12 ? 45   LYS   C HZ1  1 
ATOM   16875 H  HZ2  . LYS   C  3  45  ? 11.920  -39.536 -64.737  1.00 112.12 ? 45   LYS   C HZ2  1 
ATOM   16876 H  HZ3  . LYS   C  3  45  ? 10.531  -39.629 -65.138  1.00 112.12 ? 45   LYS   C HZ3  1 
ATOM   16877 N  N    . LEU   C  3  46  ? 7.678   -42.398 -59.078  1.00 57.51  ? 46   LEU   C N    1 
ATOM   16878 C  CA   . LEU   C  3  46  ? 6.442   -41.798 -58.599  1.00 55.72  ? 46   LEU   C CA   1 
ATOM   16879 C  C    . LEU   C  3  46  ? 6.126   -40.570 -59.443  1.00 58.69  ? 46   LEU   C C    1 
ATOM   16880 O  O    . LEU   C  3  46  ? 6.988   -39.710 -59.650  1.00 59.58  ? 46   LEU   C O    1 
ATOM   16881 C  CB   . LEU   C  3  46  ? 6.547   -41.408 -57.125  1.00 56.61  ? 46   LEU   C CB   1 
ATOM   16882 C  CG   . LEU   C  3  46  ? 5.340   -40.618 -56.598  1.00 54.67  ? 46   LEU   C CG   1 
ATOM   16883 C  CD1  . LEU   C  3  46  ? 4.079   -41.472 -56.595  1.00 53.93  ? 46   LEU   C CD1  1 
ATOM   16884 C  CD2  . LEU   C  3  46  ? 5.605   -40.063 -55.213  1.00 54.14  ? 46   LEU   C CD2  1 
ATOM   16885 H  H    . LEU   C  3  46  ? 8.371   -42.215 -58.602  1.00 69.05  ? 46   LEU   C H    1 
ATOM   16886 H  HA   . LEU   C  3  46  ? 5.721   -42.442 -58.679  1.00 66.90  ? 46   LEU   C HA   1 
ATOM   16887 H  HB2  . LEU   C  3  46  ? 6.624   -42.217 -56.595  1.00 67.97  ? 46   LEU   C HB2  1 
ATOM   16888 H  HB3  . LEU   C  3  46  ? 7.336   -40.856 -57.006  1.00 67.97  ? 46   LEU   C HB3  1 
ATOM   16889 H  HG   . LEU   C  3  46  ? 5.192   -39.868 -57.195  1.00 65.64  ? 46   LEU   C HG   1 
ATOM   16890 H  HD11 . LEU   C  3  46  ? 3.332   -40.932 -56.296  1.00 64.75  ? 46   LEU   C HD11 1 
ATOM   16891 H  HD12 . LEU   C  3  46  ? 3.914   -41.795 -57.495  1.00 64.75  ? 46   LEU   C HD12 1 
ATOM   16892 H  HD13 . LEU   C  3  46  ? 4.207   -42.222 -55.994  1.00 64.75  ? 46   LEU   C HD13 1 
ATOM   16893 H  HD21 . LEU   C  3  46  ? 4.838   -39.540 -54.930  1.00 65.01  ? 46   LEU   C HD21 1 
ATOM   16894 H  HD22 . LEU   C  3  46  ? 5.746   -40.801 -54.599  1.00 65.01  ? 46   LEU   C HD22 1 
ATOM   16895 H  HD23 . LEU   C  3  46  ? 6.395   -39.502 -55.243  1.00 65.01  ? 46   LEU   C HD23 1 
ATOM   16896 N  N    . LEU   C  3  47  ? 4.888   -40.493 -59.929  1.00 60.45  ? 47   LEU   C N    1 
ATOM   16897 C  CA   . LEU   C  3  47  ? 4.415   -39.343 -60.687  1.00 60.93  ? 47   LEU   C CA   1 
ATOM   16898 C  C    . LEU   C  3  47  ? 3.506   -38.456 -59.845  1.00 61.56  ? 47   LEU   C C    1 
ATOM   16899 O  O    . LEU   C  3  47  ? 3.777   -37.266 -59.659  1.00 62.19  ? 47   LEU   C O    1 
ATOM   16900 C  CB   . LEU   C  3  47  ? 3.655   -39.804 -61.935  1.00 62.56  ? 47   LEU   C CB   1 
ATOM   16901 C  CG   . LEU   C  3  47  ? 4.336   -40.767 -62.900  1.00 65.30  ? 47   LEU   C CG   1 
ATOM   16902 C  CD1  . LEU   C  3  47  ? 3.299   -41.254 -63.897  1.00 63.40  ? 47   LEU   C CD1  1 
ATOM   16903 C  CD2  . LEU   C  3  47  ? 5.501   -40.093 -63.602  1.00 69.08  ? 47   LEU   C CD2  1 
ATOM   16904 H  H    . LEU   C  3  47  ? 4.294   -41.108 -59.829  1.00 72.58  ? 47   LEU   C H    1 
ATOM   16905 H  HA   . LEU   C  3  47  ? 5.187   -38.828 -60.970  1.00 73.15  ? 47   LEU   C HA   1 
ATOM   16906 H  HB2  . LEU   C  3  47  ? 2.845   -40.245 -61.635  1.00 75.11  ? 47   LEU   C HB2  1 
ATOM   16907 H  HB3  . LEU   C  3  47  ? 3.432   -39.012 -62.449  1.00 75.11  ? 47   LEU   C HB3  1 
ATOM   16908 H  HG   . LEU   C  3  47  ? 4.702   -41.527 -62.422  1.00 78.40  ? 47   LEU   C HG   1 
ATOM   16909 H  HD11 . LEU   C  3  47  ? 3.722   -41.863 -64.521  1.00 76.12  ? 47   LEU   C HD11 1 
ATOM   16910 H  HD12 . LEU   C  3  47  ? 2.590   -41.710 -63.418  1.00 76.12  ? 47   LEU   C HD12 1 
ATOM   16911 H  HD13 . LEU   C  3  47  ? 2.937   -40.491 -64.374  1.00 76.12  ? 47   LEU   C HD13 1 
ATOM   16912 H  HD21 . LEU   C  3  47  ? 5.909   -40.726 -64.213  1.00 82.93  ? 47   LEU   C HD21 1 
ATOM   16913 H  HD22 . LEU   C  3  47  ? 5.172   -39.324 -64.092  1.00 82.93  ? 47   LEU   C HD22 1 
ATOM   16914 H  HD23 . LEU   C  3  47  ? 6.148   -39.810 -62.938  1.00 82.93  ? 47   LEU   C HD23 1 
ATOM   16915 N  N    . ILE   C  3  48  ? 2.422   -39.032 -59.330  1.00 59.49  ? 48   ILE   C N    1 
ATOM   16916 C  CA   . ILE   C  3  48  ? 1.363   -38.296 -58.658  1.00 53.26  ? 48   ILE   C CA   1 
ATOM   16917 C  C    . ILE   C  3  48  ? 1.137   -38.915 -57.289  1.00 49.68  ? 48   ILE   C C    1 
ATOM   16918 O  O    . ILE   C  3  48  ? 1.177   -40.141 -57.138  1.00 46.56  ? 48   ILE   C O    1 
ATOM   16919 C  CB   . ILE   C  3  48  ? 0.053   -38.324 -59.475  1.00 54.72  ? 48   ILE   C CB   1 
ATOM   16920 C  CG1  . ILE   C  3  48  ? 0.264   -37.710 -60.860  1.00 58.00  ? 48   ILE   C CG1  1 
ATOM   16921 C  CG2  . ILE   C  3  48  ? -1.061  -37.602 -58.725  1.00 57.72  ? 48   ILE   C CG2  1 
ATOM   16922 C  CD1  . ILE   C  3  48  ? 0.483   -36.231 -60.832  1.00 58.20  ? 48   ILE   C CD1  1 
ATOM   16923 H  H    . ILE   C  3  48  ? 2.276   -39.879 -59.361  1.00 71.42  ? 48   ILE   C H    1 
ATOM   16924 H  HA   . ILE   C  3  48  ? 1.639   -37.374 -58.540  1.00 63.95  ? 48   ILE   C HA   1 
ATOM   16925 H  HB   . ILE   C  3  48  ? -0.209  -39.251 -59.594  1.00 65.70  ? 48   ILE   C HB   1 
ATOM   16926 H  HG12 . ILE   C  3  48  ? 1.044   -38.118 -61.267  1.00 69.63  ? 48   ILE   C HG12 1 
ATOM   16927 H  HG13 . ILE   C  3  48  ? -0.522  -37.884 -61.402  1.00 69.63  ? 48   ILE   C HG13 1 
ATOM   16928 H  HG21 . ILE   C  3  48  ? -1.852  -37.572 -59.286  1.00 69.30  ? 48   ILE   C HG21 1 
ATOM   16929 H  HG22 . ILE   C  3  48  ? -1.255  -38.085 -57.906  1.00 69.30  ? 48   ILE   C HG22 1 
ATOM   16930 H  HG23 . ILE   C  3  48  ? -0.770  -36.701 -58.517  1.00 69.30  ? 48   ILE   C HG23 1 
ATOM   16931 H  HD11 . ILE   C  3  48  ? 0.725   -35.930 -61.722  1.00 69.88  ? 48   ILE   C HD11 1 
ATOM   16932 H  HD12 . ILE   C  3  48  ? -0.336  -35.795 -60.548  1.00 69.88  ? 48   ILE   C HD12 1 
ATOM   16933 H  HD13 . ILE   C  3  48  ? 1.198   -36.029 -60.209  1.00 69.88  ? 48   ILE   C HD13 1 
ATOM   16934 N  N    . PHE   C  3  49  ? 0.889   -38.068 -56.294  1.00 49.51  ? 49   PHE   C N    1 
ATOM   16935 C  CA   . PHE   C  3  49  ? 0.466   -38.535 -54.984  1.00 51.20  ? 49   PHE   C CA   1 
ATOM   16936 C  C    . PHE   C  3  49  ? -0.675  -37.658 -54.491  1.00 53.17  ? 49   PHE   C C    1 
ATOM   16937 O  O    . PHE   C  3  49  ? -0.860  -36.524 -54.941  1.00 49.72  ? 49   PHE   C O    1 
ATOM   16938 C  CB   . PHE   C  3  49  ? 1.621   -38.545 -53.973  1.00 52.78  ? 49   PHE   C CB   1 
ATOM   16939 C  CG   . PHE   C  3  49  ? 2.153   -37.183 -53.636  1.00 54.11  ? 49   PHE   C CG   1 
ATOM   16940 C  CD1  . PHE   C  3  49  ? 3.096   -36.573 -54.447  1.00 55.39  ? 49   PHE   C CD1  1 
ATOM   16941 C  CD2  . PHE   C  3  49  ? 1.725   -36.520 -52.499  1.00 52.83  ? 49   PHE   C CD2  1 
ATOM   16942 C  CE1  . PHE   C  3  49  ? 3.593   -35.323 -54.136  1.00 56.24  ? 49   PHE   C CE1  1 
ATOM   16943 C  CE2  . PHE   C  3  49  ? 2.219   -35.269 -52.182  1.00 50.87  ? 49   PHE   C CE2  1 
ATOM   16944 C  CZ   . PHE   C  3  49  ? 3.155   -34.671 -53.001  1.00 53.62  ? 49   PHE   C CZ   1 
ATOM   16945 H  H    . PHE   C  3  49  ? 0.959   -37.213 -56.356  1.00 59.45  ? 49   PHE   C H    1 
ATOM   16946 H  HA   . PHE   C  3  49  ? 0.137   -39.445 -55.058  1.00 61.48  ? 49   PHE   C HA   1 
ATOM   16947 H  HB2  . PHE   C  3  49  ? 1.309   -38.951 -53.149  1.00 63.37  ? 49   PHE   C HB2  1 
ATOM   16948 H  HB3  . PHE   C  3  49  ? 2.353   -39.064 -54.342  1.00 63.37  ? 49   PHE   C HB3  1 
ATOM   16949 H  HD1  . PHE   C  3  49  ? 3.397   -37.011 -55.210  1.00 66.50  ? 49   PHE   C HD1  1 
ATOM   16950 H  HD2  . PHE   C  3  49  ? 1.098   -36.921 -51.941  1.00 63.44  ? 49   PHE   C HD2  1 
ATOM   16951 H  HE1  . PHE   C  3  49  ? 4.223   -34.922 -54.690  1.00 67.53  ? 49   PHE   C HE1  1 
ATOM   16952 H  HE2  . PHE   C  3  49  ? 1.922   -34.831 -51.417  1.00 61.08  ? 49   PHE   C HE2  1 
ATOM   16953 H  HZ   . PHE   C  3  49  ? 3.490   -33.829 -52.789  1.00 64.39  ? 49   PHE   C HZ   1 
ATOM   16954 N  N    . TYR   C  3  50  ? -1.444  -38.212 -53.558  1.00 57.20  ? 50   TYR   C N    1 
ATOM   16955 C  CA   . TYR   C  3  50  ? -2.656  -37.576 -53.047  1.00 56.39  ? 50   TYR   C CA   1 
ATOM   16956 C  C    . TYR   C  3  50  ? -3.535  -37.085 -54.195  1.00 54.05  ? 50   TYR   C C    1 
ATOM   16957 O  O    . TYR   C  3  50  ? -3.993  -35.940 -54.221  1.00 55.44  ? 50   TYR   C O    1 
ATOM   16958 C  CB   . TYR   C  3  50  ? -2.317  -36.438 -52.083  1.00 54.10  ? 50   TYR   C CB   1 
ATOM   16959 C  CG   . TYR   C  3  50  ? -3.442  -36.120 -51.124  1.00 52.35  ? 50   TYR   C CG   1 
ATOM   16960 C  CD1  . TYR   C  3  50  ? -4.009  -37.116 -50.340  1.00 53.45  ? 50   TYR   C CD1  1 
ATOM   16961 C  CD2  . TYR   C  3  50  ? -3.936  -34.829 -50.999  1.00 50.70  ? 50   TYR   C CD2  1 
ATOM   16962 C  CE1  . TYR   C  3  50  ? -5.037  -36.840 -49.465  1.00 56.39  ? 50   TYR   C CE1  1 
ATOM   16963 C  CE2  . TYR   C  3  50  ? -4.965  -34.541 -50.122  1.00 53.75  ? 50   TYR   C CE2  1 
ATOM   16964 C  CZ   . TYR   C  3  50  ? -5.511  -35.551 -49.357  1.00 56.17  ? 50   TYR   C CZ   1 
ATOM   16965 O  OH   . TYR   C  3  50  ? -6.535  -35.273 -48.483  1.00 59.77  ? 50   TYR   C OH   1 
ATOM   16966 H  H    . TYR   C  3  50  ? -1.282  -38.975 -53.196  1.00 68.67  ? 50   TYR   C H    1 
ATOM   16967 H  HA   . TYR   C  3  50  ? -3.163  -38.238 -52.551  1.00 67.70  ? 50   TYR   C HA   1 
ATOM   16968 H  HB2  . TYR   C  3  50  ? -1.540  -36.690 -51.560  1.00 64.96  ? 50   TYR   C HB2  1 
ATOM   16969 H  HB3  . TYR   C  3  50  ? -2.125  -35.638 -52.596  1.00 64.96  ? 50   TYR   C HB3  1 
ATOM   16970 H  HD1  . TYR   C  3  50  ? -3.688  -37.986 -50.406  1.00 64.18  ? 50   TYR   C HD1  1 
ATOM   16971 H  HD2  . TYR   C  3  50  ? -3.568  -34.146 -51.513  1.00 60.88  ? 50   TYR   C HD2  1 
ATOM   16972 H  HE1  . TYR   C  3  50  ? -5.408  -37.519 -48.950  1.00 67.70  ? 50   TYR   C HE1  1 
ATOM   16973 H  HE2  . TYR   C  3  50  ? -5.288  -33.672 -50.047  1.00 64.54  ? 50   TYR   C HE2  1 
ATOM   16974 H  HH   . TYR   C  3  50  ? -6.769  -34.470 -48.559  1.00 71.76  ? 50   TYR   C HH   1 
ATOM   16975 N  N    . THR   C  3  51  ? -3.752  -37.974 -55.165  1.00 53.42  ? 51   THR   C N    1 
ATOM   16976 C  CA   . THR   C  3  51  ? -4.666  -37.751 -56.280  1.00 56.54  ? 51   THR   C CA   1 
ATOM   16977 C  C    . THR   C  3  51  ? -4.126  -36.766 -57.311  1.00 57.62  ? 51   THR   C C    1 
ATOM   16978 O  O    . THR   C  3  51  ? -4.238  -37.017 -58.515  1.00 62.34  ? 51   THR   C O    1 
ATOM   16979 C  CB   . THR   C  3  51  ? -6.030  -37.256 -55.781  1.00 56.28  ? 51   THR   C CB   1 
ATOM   16980 O  OG1  . THR   C  3  51  ? -6.593  -38.220 -54.883  1.00 58.72  ? 51   THR   C OG1  1 
ATOM   16981 C  CG2  . THR   C  3  51  ? -6.984  -37.039 -56.954  1.00 58.38  ? 51   THR   C CG2  1 
ATOM   16982 H  H    . THR   C  3  51  ? -3.367  -38.742 -55.199  1.00 64.14  ? 51   THR   C H    1 
ATOM   16983 H  HA   . THR   C  3  51  ? -4.774  -38.607 -56.724  1.00 67.89  ? 51   THR   C HA   1 
ATOM   16984 H  HB   . THR   C  3  51  ? -5.917  -36.412 -55.317  1.00 67.58  ? 51   THR   C HB   1 
ATOM   16985 H  HG1  . THR   C  3  51  ? -6.114  -38.289 -54.197  1.00 70.51  ? 51   THR   C HG1  1 
ATOM   16986 H  HG21 . THR   C  3  51  ? -7.867  -36.809 -56.626  1.00 70.09  ? 51   THR   C HG21 1 
ATOM   16987 H  HG22 . THR   C  3  51  ? -6.659  -36.319 -57.517  1.00 70.09  ? 51   THR   C HG22 1 
ATOM   16988 H  HG23 . THR   C  3  51  ? -7.046  -37.849 -57.485  1.00 70.09  ? 51   THR   C HG23 1 
ATOM   16989 N  N    . SER   C  3  52  ? -3.549  -35.639 -56.866  1.00 57.80  ? 52   SER   C N    1 
ATOM   16990 C  CA   . SER   C  3  52  ? -3.247  -34.574 -57.817  1.00 61.14  ? 52   SER   C CA   1 
ATOM   16991 C  C    . SER   C  3  52  ? -1.976  -33.790 -57.502  1.00 60.02  ? 52   SER   C C    1 
ATOM   16992 O  O    . SER   C  3  52  ? -1.794  -32.701 -58.059  1.00 59.81  ? 52   SER   C O    1 
ATOM   16993 C  CB   . SER   C  3  52  ? -4.413  -33.581 -57.875  1.00 62.37  ? 52   SER   C CB   1 
ATOM   16994 O  OG   . SER   C  3  52  ? -4.525  -32.874 -56.651  1.00 61.66  ? 52   SER   C OG   1 
ATOM   16995 H  H    . SER   C  3  52  ? -3.333  -35.478 -56.050  1.00 69.39  ? 52   SER   C H    1 
ATOM   16996 H  HA   . SER   C  3  52  ? -3.120  -34.992 -58.683  1.00 73.40  ? 52   SER   C HA   1 
ATOM   16997 H  HB2  . SER   C  3  52  ? -4.255  -32.948 -58.593  1.00 74.88  ? 52   SER   C HB2  1 
ATOM   16998 H  HB3  . SER   C  3  52  ? -5.236  -34.067 -58.037  1.00 74.88  ? 52   SER   C HB3  1 
ATOM   16999 H  HG   . SER   C  3  52  ? -5.179  -32.348 -56.681  1.00 74.03  ? 52   SER   C HG   1 
ATOM   17000 N  N    . LYS   C  3  53  ? -1.098  -34.291 -56.642  1.00 62.72  ? 53   LYS   C N    1 
ATOM   17001 C  CA   . LYS   C  3  53  ? 0.113   -33.575 -56.263  1.00 65.43  ? 53   LYS   C CA   1 
ATOM   17002 C  C    . LYS   C  3  53  ? 1.287   -34.120 -57.065  1.00 66.51  ? 53   LYS   C C    1 
ATOM   17003 O  O    . LYS   C  3  53  ? 1.580   -35.319 -57.010  1.00 62.53  ? 53   LYS   C O    1 
ATOM   17004 C  CB   . LYS   C  3  53  ? 0.368   -33.706 -54.763  1.00 62.72  ? 53   LYS   C CB   1 
ATOM   17005 C  CG   . LYS   C  3  53  ? -0.851  -33.376 -53.918  1.00 63.66  ? 53   LYS   C CG   1 
ATOM   17006 C  CD   . LYS   C  3  53  ? -1.365  -31.975 -54.210  1.00 66.02  ? 53   LYS   C CD   1 
ATOM   17007 C  CE   . LYS   C  3  53  ? -2.621  -31.670 -53.420  1.00 68.97  ? 53   LYS   C CE   1 
ATOM   17008 N  NZ   . LYS   C  3  53  ? -3.027  -30.248 -53.569  1.00 74.78  ? 53   LYS   C NZ   1 
ATOM   17009 H  H    . LYS   C  3  53  ? -1.183  -35.057 -56.260  1.00 75.30  ? 53   LYS   C H    1 
ATOM   17010 H  HA   . LYS   C  3  53  ? 0.015   -32.634 -56.475  1.00 78.55  ? 53   LYS   C HA   1 
ATOM   17011 H  HB2  . LYS   C  3  53  ? 0.629   -34.619 -54.567  1.00 75.31  ? 53   LYS   C HB2  1 
ATOM   17012 H  HB3  . LYS   C  3  53  ? 1.080   -33.096 -54.512  1.00 75.31  ? 53   LYS   C HB3  1 
ATOM   17013 H  HG2  . LYS   C  3  53  ? -1.559  -34.008 -54.114  1.00 76.43  ? 53   LYS   C HG2  1 
ATOM   17014 H  HG3  . LYS   C  3  53  ? -0.613  -33.424 -52.979  1.00 76.43  ? 53   LYS   C HG3  1 
ATOM   17015 H  HD2  . LYS   C  3  53  ? -0.687  -31.326 -53.966  1.00 79.26  ? 53   LYS   C HD2  1 
ATOM   17016 H  HD3  . LYS   C  3  53  ? -1.573  -31.899 -55.154  1.00 79.26  ? 53   LYS   C HD3  1 
ATOM   17017 H  HE2  . LYS   C  3  53  ? -3.346  -32.230 -53.741  1.00 82.80  ? 53   LYS   C HE2  1 
ATOM   17018 H  HE3  . LYS   C  3  53  ? -2.459  -31.845 -52.480  1.00 82.80  ? 53   LYS   C HE3  1 
ATOM   17019 H  HZ1  . LYS   C  3  53  ? -3.773  -30.094 -53.108  1.00 89.78  ? 53   LYS   C HZ1  1 
ATOM   17020 H  HZ2  . LYS   C  3  53  ? -2.384  -29.714 -53.265  1.00 89.78  ? 53   LYS   C HZ2  1 
ATOM   17021 H  HZ3  . LYS   C  3  53  ? -3.175  -30.062 -54.427  1.00 89.78  ? 53   LYS   C HZ3  1 
ATOM   17022 N  N    . LEU   C  3  54  ? 1.950   -33.241 -57.812  1.00 70.22  ? 54   LEU   C N    1 
ATOM   17023 C  CA   . LEU   C  3  54  ? 3.105   -33.655 -58.596  1.00 70.53  ? 54   LEU   C CA   1 
ATOM   17024 C  C    . LEU   C  3  54  ? 4.288   -33.928 -57.679  1.00 70.22  ? 54   LEU   C C    1 
ATOM   17025 O  O    . LEU   C  3  54  ? 4.606   -33.122 -56.798  1.00 70.92  ? 54   LEU   C O    1 
ATOM   17026 C  CB   . LEU   C  3  54  ? 3.485   -32.585 -59.617  1.00 74.31  ? 54   LEU   C CB   1 
ATOM   17027 C  CG   . LEU   C  3  54  ? 2.837   -32.600 -61.002  1.00 82.04  ? 54   LEU   C CG   1 
ATOM   17028 C  CD1  . LEU   C  3  54  ? 3.579   -31.645 -61.899  1.00 90.44  ? 54   LEU   C CD1  1 
ATOM   17029 C  CD2  . LEU   C  3  54  ? 2.847   -33.971 -61.634  1.00 84.63  ? 54   LEU   C CD2  1 
ATOM   17030 H  H    . LEU   C  3  54  ? 1.752   -32.407 -57.881  1.00 84.30  ? 54   LEU   C H    1 
ATOM   17031 H  HA   . LEU   C  3  54  ? 2.880   -34.467 -59.077  1.00 84.68  ? 54   LEU   C HA   1 
ATOM   17032 H  HB2  . LEU   C  3  54  ? 3.270   -31.724 -59.226  1.00 89.21  ? 54   LEU   C HB2  1 
ATOM   17033 H  HB3  . LEU   C  3  54  ? 4.442   -32.653 -59.763  1.00 89.21  ? 54   LEU   C HB3  1 
ATOM   17034 H  HG   . LEU   C  3  54  ? 1.909   -32.337 -60.903  1.00 98.49  ? 54   LEU   C HG   1 
ATOM   17035 H  HD11 . LEU   C  3  54  ? 3.017   -31.422 -62.658  1.00 108.56 ? 54   LEU   C HD11 1 
ATOM   17036 H  HD12 . LEU   C  3  54  ? 3.791   -30.842 -61.398  1.00 108.56 ? 54   LEU   C HD12 1 
ATOM   17037 H  HD13 . LEU   C  3  54  ? 4.396   -32.069 -62.205  1.00 108.56 ? 54   LEU   C HD13 1 
ATOM   17038 H  HD21 . LEU   C  3  54  ? 2.399   -33.926 -62.493  1.00 101.59 ? 54   LEU   C HD21 1 
ATOM   17039 H  HD22 . LEU   C  3  54  ? 3.767   -34.256 -61.755  1.00 101.59 ? 54   LEU   C HD22 1 
ATOM   17040 H  HD23 . LEU   C  3  54  ? 2.383   -34.591 -61.051  1.00 101.59 ? 54   LEU   C HD23 1 
ATOM   17041 N  N    . HIS   C  3  55  ? 4.943   -35.062 -57.890  1.00 68.44  ? 55   HIS   C N    1 
ATOM   17042 C  CA   . HIS   C  3  55  ? 6.168   -35.342 -57.166  1.00 66.23  ? 55   HIS   C CA   1 
ATOM   17043 C  C    . HIS   C  3  55  ? 7.312   -34.519 -57.743  1.00 68.90  ? 55   HIS   C C    1 
ATOM   17044 O  O    . HIS   C  3  55  ? 7.362   -34.242 -58.945  1.00 70.66  ? 55   HIS   C O    1 
ATOM   17045 C  CB   . HIS   C  3  55  ? 6.521   -36.825 -57.225  1.00 61.22  ? 55   HIS   C CB   1 
ATOM   17046 C  CG   . HIS   C  3  55  ? 7.761   -37.165 -56.463  1.00 60.83  ? 55   HIS   C CG   1 
ATOM   17047 N  ND1  . HIS   C  3  55  ? 8.812   -37.866 -57.016  1.00 61.82  ? 55   HIS   C ND1  1 
ATOM   17048 C  CD2  . HIS   C  3  55  ? 8.131   -36.871 -55.194  1.00 60.18  ? 55   HIS   C CD2  1 
ATOM   17049 C  CE1  . HIS   C  3  55  ? 9.768   -38.002 -56.115  1.00 63.32  ? 55   HIS   C CE1  1 
ATOM   17050 N  NE2  . HIS   C  3  55  ? 9.380   -37.407 -55.001  1.00 63.28  ? 55   HIS   C NE2  1 
ATOM   17051 H  H    . HIS   C  3  55  ? 4.700   -35.676 -58.441  1.00 82.17  ? 55   HIS   C H    1 
ATOM   17052 H  HA   . HIS   C  3  55  ? 6.049   -35.108 -56.232  1.00 79.52  ? 55   HIS   C HA   1 
ATOM   17053 H  HB2  . HIS   C  3  55  ? 5.789   -37.337 -56.847  1.00 73.50  ? 55   HIS   C HB2  1 
ATOM   17054 H  HB3  . HIS   C  3  55  ? 6.660   -37.078 -58.151  1.00 73.50  ? 55   HIS   C HB3  1 
ATOM   17055 H  HD2  . HIS   C  3  55  ? 7.632   -36.395 -54.571  1.00 72.26  ? 55   HIS   C HD2  1 
ATOM   17056 H  HE1  . HIS   C  3  55  ? 10.578  -38.442 -56.243  1.00 76.03  ? 55   HIS   C HE1  1 
ATOM   17057 H  HE2  . HIS   C  3  55  ? 9.836   -37.363 -54.273  1.00 75.97  ? 55   HIS   C HE2  1 
ATOM   17058 N  N    . SER   C  3  56  ? 8.230   -34.123 -56.870  1.00 69.92  ? 56   SER   C N    1 
ATOM   17059 C  CA   . SER   C  3  56  ? 9.379   -33.333 -57.290  1.00 73.04  ? 56   SER   C CA   1 
ATOM   17060 C  C    . SER   C  3  56  ? 10.075  -33.979 -58.478  1.00 71.88  ? 56   SER   C C    1 
ATOM   17061 O  O    . SER   C  3  56  ? 10.488  -35.141 -58.414  1.00 70.11  ? 56   SER   C O    1 
ATOM   17062 C  CB   . SER   C  3  56  ? 10.359  -33.181 -56.127  1.00 77.45  ? 56   SER   C CB   1 
ATOM   17063 O  OG   . SER   C  3  56  ? 11.634  -32.772 -56.593  1.00 84.64  ? 56   SER   C OG   1 
ATOM   17064 H  H    . SER   C  3  56  ? 8.211   -34.298 -56.028  1.00 83.95  ? 56   SER   C H    1 
ATOM   17065 H  HA   . SER   C  3  56  ? 9.074   -32.451 -57.554  1.00 87.69  ? 56   SER   C HA   1 
ATOM   17066 H  HB2  . SER   C  3  56  ? 10.018  -32.512 -55.512  1.00 92.98  ? 56   SER   C HB2  1 
ATOM   17067 H  HB3  . SER   C  3  56  ? 10.447  -34.034 -55.674  1.00 92.98  ? 56   SER   C HB3  1 
ATOM   17068 H  HG   . SER   C  3  56  ? 12.192  -32.801 -55.965  1.00 101.60 ? 56   SER   C HG   1 
ATOM   17069 N  N    . GLY   C  3  57  ? 10.192  -33.225 -59.570  1.00 75.61  ? 57   GLY   C N    1 
ATOM   17070 C  CA   . GLY   C  3  57  ? 11.016  -33.604 -60.691  1.00 77.50  ? 57   GLY   C CA   1 
ATOM   17071 C  C    . GLY   C  3  57  ? 10.271  -34.137 -61.898  1.00 77.42  ? 57   GLY   C C    1 
ATOM   17072 O  O    . GLY   C  3  57  ? 10.859  -34.201 -62.984  1.00 79.24  ? 57   GLY   C O    1 
ATOM   17073 H  H    . GLY   C  3  57  ? 9.790   -32.472 -59.677  1.00 90.77  ? 57   GLY   C H    1 
ATOM   17074 H  HA2  . GLY   C  3  57  ? 11.521  -32.827 -60.979  1.00 93.04  ? 57   GLY   C HA2  1 
ATOM   17075 H  HA3  . GLY   C  3  57  ? 11.635  -34.292 -60.401  1.00 93.04  ? 57   GLY   C HA3  1 
ATOM   17076 N  N    . VAL   C  3  58  ? 9.009   -34.527 -61.750  1.00 76.23  ? 58   VAL   C N    1 
ATOM   17077 C  CA   . VAL   C  3  58  ? 8.268   -35.078 -62.885  1.00 81.98  ? 58   VAL   C CA   1 
ATOM   17078 C  C    . VAL   C  3  58  ? 7.614   -33.927 -63.643  1.00 82.46  ? 58   VAL   C C    1 
ATOM   17079 O  O    . VAL   C  3  58  ? 7.257   -32.907 -63.035  1.00 83.17  ? 58   VAL   C O    1 
ATOM   17080 C  CB   . VAL   C  3  58  ? 7.242   -36.133 -62.436  1.00 84.65  ? 58   VAL   C CB   1 
ATOM   17081 C  CG1  . VAL   C  3  58  ? 7.954   -37.302 -61.757  1.00 84.75  ? 58   VAL   C CG1  1 
ATOM   17082 C  CG2  . VAL   C  3  58  ? 6.191   -35.535 -61.511  1.00 84.28  ? 58   VAL   C CG2  1 
ATOM   17083 H  H    . VAL   C  3  58  ? 8.565   -34.484 -61.015  1.00 91.51  ? 58   VAL   C H    1 
ATOM   17084 H  HA   . VAL   C  3  58  ? 8.887   -35.520 -63.487  1.00 98.42  ? 58   VAL   C HA   1 
ATOM   17085 H  HB   . VAL   C  3  58  ? 6.779   -36.462 -63.222  1.00 101.62 ? 58   VAL   C HB   1 
ATOM   17086 H  HG11 . VAL   C  3  58  ? 7.290   -37.930 -61.431  1.00 101.74 ? 58   VAL   C HG11 1 
ATOM   17087 H  HG12 . VAL   C  3  58  ? 8.532   -37.737 -62.403  1.00 101.74 ? 58   VAL   C HG12 1 
ATOM   17088 H  HG13 . VAL   C  3  58  ? 8.481   -36.963 -61.016  1.00 101.74 ? 58   VAL   C HG13 1 
ATOM   17089 H  HG21 . VAL   C  3  58  ? 5.351   -36.003 -61.644  1.00 101.17 ? 58   VAL   C HG21 1 
ATOM   17090 H  HG22 . VAL   C  3  58  ? 6.484   -35.637 -60.592  1.00 101.17 ? 58   VAL   C HG22 1 
ATOM   17091 H  HG23 . VAL   C  3  58  ? 6.083   -34.595 -61.722  1.00 101.17 ? 58   VAL   C HG23 1 
ATOM   17092 N  N    . PRO   C  3  59  ? 7.446   -34.038 -64.958  1.00 82.74  ? 59   PRO   C N    1 
ATOM   17093 C  CA   . PRO   C  3  59  ? 7.023   -32.878 -65.751  1.00 87.67  ? 59   PRO   C CA   1 
ATOM   17094 C  C    . PRO   C  3  59  ? 5.556   -32.521 -65.565  1.00 84.47  ? 59   PRO   C C    1 
ATOM   17095 O  O    . PRO   C  3  59  ? 4.740   -33.305 -65.075  1.00 82.42  ? 59   PRO   C O    1 
ATOM   17096 C  CB   . PRO   C  3  59  ? 7.306   -33.311 -67.196  1.00 88.47  ? 59   PRO   C CB   1 
ATOM   17097 C  CG   . PRO   C  3  59  ? 7.363   -34.802 -67.154  1.00 86.69  ? 59   PRO   C CG   1 
ATOM   17098 C  CD   . PRO   C  3  59  ? 7.883   -35.162 -65.803  1.00 81.42  ? 59   PRO   C CD   1 
ATOM   17099 H  HA   . PRO   C  3  59  ? 7.563   -32.107 -65.515  1.00 105.24 ? 59   PRO   C HA   1 
ATOM   17100 H  HB2  . PRO   C  3  59  ? 6.591   -33.008 -67.776  1.00 106.20 ? 59   PRO   C HB2  1 
ATOM   17101 H  HB3  . PRO   C  3  59  ? 8.153   -32.941 -67.491  1.00 106.20 ? 59   PRO   C HB3  1 
ATOM   17102 H  HG2  . PRO   C  3  59  ? 6.473   -35.165 -67.285  1.00 104.06 ? 59   PRO   C HG2  1 
ATOM   17103 H  HG3  . PRO   C  3  59  ? 7.959   -35.124 -67.847  1.00 104.06 ? 59   PRO   C HG3  1 
ATOM   17104 H  HD2  . PRO   C  3  59  ? 7.496   -35.997 -65.495  1.00 97.74  ? 59   PRO   C HD2  1 
ATOM   17105 H  HD3  . PRO   C  3  59  ? 8.851   -35.230 -65.813  1.00 97.74  ? 59   PRO   C HD3  1 
ATOM   17106 N  N    . SER   C  3  60  ? 5.235   -31.295 -65.991  1.00 84.71  ? 60   SER   C N    1 
ATOM   17107 C  CA   . SER   C  3  60  ? 3.895   -30.742 -65.842  1.00 86.32  ? 60   SER   C CA   1 
ATOM   17108 C  C    . SER   C  3  60  ? 2.870   -31.429 -66.732  1.00 85.23  ? 60   SER   C C    1 
ATOM   17109 O  O    . SER   C  3  60  ? 1.665   -31.254 -66.516  1.00 85.17  ? 60   SER   C O    1 
ATOM   17110 C  CB   . SER   C  3  60  ? 3.924   -29.245 -66.153  1.00 94.62  ? 60   SER   C CB   1 
ATOM   17111 O  OG   . SER   C  3  60  ? 4.724   -28.984 -67.295  1.00 102.65 ? 60   SER   C OG   1 
ATOM   17112 H  H    . SER   C  3  60  ? 5.786   -30.758 -66.375  1.00 101.69 ? 60   SER   C H    1 
ATOM   17113 H  HA   . SER   C  3  60  ? 3.610   -30.864 -64.923  1.00 103.62 ? 60   SER   C HA   1 
ATOM   17114 H  HB2  . SER   C  3  60  ? 3.019   -28.940 -66.325  1.00 113.58 ? 60   SER   C HB2  1 
ATOM   17115 H  HB3  . SER   C  3  60  ? 4.295   -28.771 -65.392  1.00 113.58 ? 60   SER   C HB3  1 
ATOM   17116 H  HG   . SER   C  3  60  ? 4.265   -28.607 -67.888  1.00 123.22 ? 60   SER   C HG   1 
ATOM   17117 N  N    . ARG   C  3  61  ? 3.313   -32.192 -67.734  1.00 86.28  ? 61   ARG   C N    1 
ATOM   17118 C  CA   . ARG   C  3  61  ? 2.369   -32.926 -68.568  1.00 85.33  ? 61   ARG   C CA   1 
ATOM   17119 C  C    . ARG   C  3  61  ? 1.465   -33.803 -67.717  1.00 81.94  ? 61   ARG   C C    1 
ATOM   17120 O  O    . ARG   C  3  61  ? 0.254   -33.885 -67.954  1.00 85.69  ? 61   ARG   C O    1 
ATOM   17121 C  CB   . ARG   C  3  61  ? 3.116   -33.786 -69.587  1.00 85.77  ? 61   ARG   C CB   1 
ATOM   17122 C  CG   . ARG   C  3  61  ? 4.270   -33.089 -70.280  1.00 91.43  ? 61   ARG   C CG   1 
ATOM   17123 C  CD   . ARG   C  3  61  ? 4.776   -33.908 -71.455  1.00 94.96  ? 61   ARG   C CD   1 
ATOM   17124 N  NE   . ARG   C  3  61  ? 5.183   -35.258 -71.066  1.00 86.59  ? 61   ARG   C NE   1 
ATOM   17125 C  CZ   . ARG   C  3  61  ? 6.437   -35.630 -70.811  1.00 84.41  ? 61   ARG   C CZ   1 
ATOM   17126 N  NH1  . ARG   C  3  61  ? 7.433   -34.759 -70.899  1.00 86.65  ? 61   ARG   C NH1  1 
ATOM   17127 N  NH2  . ARG   C  3  61  ? 6.697   -36.884 -70.469  1.00 82.27  ? 61   ARG   C NH2  1 
ATOM   17128 H  H    . ARG   C  3  61  ? 4.140   -32.299 -67.945  1.00 103.57 ? 61   ARG   C H    1 
ATOM   17129 H  HA   . ARG   C  3  61  ? 1.824   -32.289 -69.055  1.00 102.43 ? 61   ARG   C HA   1 
ATOM   17130 H  HB2  . ARG   C  3  61  ? 3.476   -34.562 -69.129  1.00 102.96 ? 61   ARG   C HB2  1 
ATOM   17131 H  HB3  . ARG   C  3  61  ? 2.490   -34.066 -70.272  1.00 102.96 ? 61   ARG   C HB3  1 
ATOM   17132 H  HG2  . ARG   C  3  61  ? 3.974   -32.227 -70.611  1.00 109.75 ? 61   ARG   C HG2  1 
ATOM   17133 H  HG3  . ARG   C  3  61  ? 5.000   -32.971 -69.652  1.00 109.75 ? 61   ARG   C HG3  1 
ATOM   17134 H  HD2  . ARG   C  3  61  ? 4.070   -33.986 -72.115  1.00 113.99 ? 61   ARG   C HD2  1 
ATOM   17135 H  HD3  . ARG   C  3  61  ? 5.545   -33.463 -71.844  1.00 113.99 ? 61   ARG   C HD3  1 
ATOM   17136 H  HE   . ARG   C  3  61  ? 4.568   -35.856 -70.996  1.00 103.94 ? 61   ARG   C HE   1 
ATOM   17137 H  HH11 . ARG   C  3  61  ? 7.273   -33.944 -71.123  1.00 104.01 ? 61   ARG   C HH11 1 
ATOM   17138 H  HH12 . ARG   C  3  61  ? 8.239   -35.010 -70.733  1.00 104.01 ? 61   ARG   C HH12 1 
ATOM   17139 H  HH21 . ARG   C  3  61  ? 6.057   -37.456 -70.411  1.00 98.76  ? 61   ARG   C HH21 1 
ATOM   17140 H  HH22 . ARG   C  3  61  ? 7.505   -37.126 -70.304  1.00 98.76  ? 61   ARG   C HH22 1 
ATOM   17141 N  N    . PHE   C  3  62  ? 2.040   -34.468 -66.721  1.00 75.86  ? 62   PHE   C N    1 
ATOM   17142 C  CA   . PHE   C  3  62  ? 1.266   -35.336 -65.850  1.00 75.10  ? 62   PHE   C CA   1 
ATOM   17143 C  C    . PHE   C  3  62  ? 0.423   -34.514 -64.883  1.00 76.95  ? 62   PHE   C C    1 
ATOM   17144 O  O    . PHE   C  3  62  ? 0.866   -33.491 -64.353  1.00 78.21  ? 62   PHE   C O    1 
ATOM   17145 C  CB   . PHE   C  3  62  ? 2.197   -36.274 -65.084  1.00 72.63  ? 62   PHE   C CB   1 
ATOM   17146 C  CG   . PHE   C  3  62  ? 2.993   -37.190 -65.972  1.00 73.55  ? 62   PHE   C CG   1 
ATOM   17147 C  CD1  . PHE   C  3  62  ? 2.440   -38.369 -66.443  1.00 74.31  ? 62   PHE   C CD1  1 
ATOM   17148 C  CD2  . PHE   C  3  62  ? 4.290   -36.870 -66.339  1.00 74.19  ? 62   PHE   C CD2  1 
ATOM   17149 C  CE1  . PHE   C  3  62  ? 3.166   -39.213 -67.261  1.00 75.69  ? 62   PHE   C CE1  1 
ATOM   17150 C  CE2  . PHE   C  3  62  ? 5.020   -37.711 -67.157  1.00 75.04  ? 62   PHE   C CE2  1 
ATOM   17151 C  CZ   . PHE   C  3  62  ? 4.457   -38.883 -67.616  1.00 75.51  ? 62   PHE   C CZ   1 
ATOM   17152 H  H    . PHE   C  3  62  ? 2.878   -34.433 -66.529  1.00 91.07  ? 62   PHE   C H    1 
ATOM   17153 H  HA   . PHE   C  3  62  ? 0.662   -35.878 -66.382  1.00 90.15  ? 62   PHE   C HA   1 
ATOM   17154 H  HB2  . PHE   C  3  62  ? 2.824   -35.741 -64.571  1.00 87.19  ? 62   PHE   C HB2  1 
ATOM   17155 H  HB3  . PHE   C  3  62  ? 1.666   -36.825 -64.489  1.00 87.19  ? 62   PHE   C HB3  1 
ATOM   17156 H  HD1  . PHE   C  3  62  ? 1.570   -38.596 -66.205  1.00 89.21  ? 62   PHE   C HD1  1 
ATOM   17157 H  HD2  . PHE   C  3  62  ? 4.674   -36.081 -66.032  1.00 89.07  ? 62   PHE   C HD2  1 
ATOM   17158 H  HE1  . PHE   C  3  62  ? 2.784   -40.002 -67.572  1.00 90.86  ? 62   PHE   C HE1  1 
ATOM   17159 H  HE2  . PHE   C  3  62  ? 5.890   -37.487 -67.397  1.00 90.08  ? 62   PHE   C HE2  1 
ATOM   17160 H  HZ   . PHE   C  3  62  ? 4.948   -39.452 -68.164  1.00 90.64  ? 62   PHE   C HZ   1 
ATOM   17161 N  N    . SER   C  3  63  ? -0.806  -34.974 -64.667  1.00 75.75  ? 63   SER   C N    1 
ATOM   17162 C  CA   . SER   C  3  63  ? -1.751  -34.345 -63.758  1.00 77.74  ? 63   SER   C CA   1 
ATOM   17163 C  C    . SER   C  3  63  ? -2.738  -35.424 -63.335  1.00 76.23  ? 63   SER   C C    1 
ATOM   17164 O  O    . SER   C  3  63  ? -2.994  -36.368 -64.086  1.00 75.02  ? 63   SER   C O    1 
ATOM   17165 C  CB   . SER   C  3  63  ? -2.471  -33.161 -64.416  1.00 83.82  ? 63   SER   C CB   1 
ATOM   17166 O  OG   . SER   C  3  63  ? -3.499  -33.601 -65.287  1.00 86.00  ? 63   SER   C OG   1 
ATOM   17167 H  H    . SER   C  3  63  ? -1.126  -35.674 -65.050  1.00 90.93  ? 63   SER   C H    1 
ATOM   17168 H  HA   . SER   C  3  63  ? -1.299  -33.998 -62.973  1.00 93.32  ? 63   SER   C HA   1 
ATOM   17169 H  HB2  . SER   C  3  63  ? -2.863  -32.608 -63.722  1.00 100.62 ? 63   SER   C HB2  1 
ATOM   17170 H  HB3  . SER   C  3  63  ? -1.826  -32.647 -64.926  1.00 100.62 ? 63   SER   C HB3  1 
ATOM   17171 H  HG   . SER   C  3  63  ? -3.854  -32.941 -65.667  1.00 103.23 ? 63   SER   C HG   1 
ATOM   17172 N  N    . GLY   C  3  64  ? -3.276  -35.287 -62.127  1.00 73.77  ? 64   GLY   C N    1 
ATOM   17173 C  CA   . GLY   C  3  64  ? -4.123  -36.309 -61.542  1.00 72.82  ? 64   GLY   C CA   1 
ATOM   17174 C  C    . GLY   C  3  64  ? -5.480  -35.761 -61.148  1.00 75.46  ? 64   GLY   C C    1 
ATOM   17175 O  O    . GLY   C  3  64  ? -5.622  -34.577 -60.840  1.00 76.61  ? 64   GLY   C O    1 
ATOM   17176 H  H    . GLY   C  3  64  ? -3.161  -34.600 -61.623  1.00 88.56  ? 64   GLY   C H    1 
ATOM   17177 H  HA2  . GLY   C  3  64  ? -4.255  -37.026 -62.183  1.00 87.42  ? 64   GLY   C HA2  1 
ATOM   17178 H  HA3  . GLY   C  3  64  ? -3.695  -36.670 -60.750  1.00 87.42  ? 64   GLY   C HA3  1 
ATOM   17179 N  N    . SER   C  3  65  ? -6.480  -36.641 -61.148  1.00 81.42  ? 65   SER   C N    1 
ATOM   17180 C  CA   . SER   C  3  65  ? -7.854  -36.230 -60.898  1.00 82.04  ? 65   SER   C CA   1 
ATOM   17181 C  C    . SER   C  3  65  ? -8.609  -37.347 -60.193  1.00 76.62  ? 65   SER   C C    1 
ATOM   17182 O  O    . SER   C  3  65  ? -8.259  -38.525 -60.301  1.00 75.58  ? 65   SER   C O    1 
ATOM   17183 C  CB   . SER   C  3  65  ? -8.572  -35.863 -62.202  1.00 90.28  ? 65   SER   C CB   1 
ATOM   17184 O  OG   . SER   C  3  65  ? -7.890  -34.829 -62.889  1.00 93.22  ? 65   SER   C OG   1 
ATOM   17185 H  H    . SER   C  3  65  ? -6.386  -37.484 -61.291  1.00 97.74  ? 65   SER   C H    1 
ATOM   17186 H  HA   . SER   C  3  65  ? -7.844  -35.459 -60.310  1.00 98.48  ? 65   SER   C HA   1 
ATOM   17187 H  HB2  . SER   C  3  65  ? -8.609  -36.647 -62.772  1.00 108.37 ? 65   SER   C HB2  1 
ATOM   17188 H  HB3  . SER   C  3  65  ? -9.470  -35.562 -61.993  1.00 108.37 ? 65   SER   C HB3  1 
ATOM   17189 H  HG   . SER   C  3  65  ? -8.396  -34.481 -63.461  1.00 111.90 ? 65   SER   C HG   1 
ATOM   17190 N  N    . GLY   C  3  66  ? -9.659  -36.959 -59.469  1.00 77.48  ? 66   GLY   C N    1 
ATOM   17191 C  CA   . GLY   C  3  66  ? -10.570 -37.924 -58.886  1.00 78.94  ? 66   GLY   C CA   1 
ATOM   17192 C  C    . GLY   C  3  66  ? -10.990 -37.645 -57.457  1.00 79.12  ? 66   GLY   C C    1 
ATOM   17193 O  O    . GLY   C  3  66  ? -10.566 -36.659 -56.846  1.00 77.89  ? 66   GLY   C O    1 
ATOM   17194 H  H    . GLY   C  3  66  ? -9.860  -36.139 -59.304  1.00 93.02  ? 66   GLY   C H    1 
ATOM   17195 H  HA2  . GLY   C  3  66  ? -11.375 -37.953 -59.427  1.00 94.76  ? 66   GLY   C HA2  1 
ATOM   17196 H  HA3  . GLY   C  3  66  ? -10.147 -38.796 -58.902  1.00 94.76  ? 66   GLY   C HA3  1 
ATOM   17197 N  N    . SER   C  3  67  ? -11.836 -38.523 -56.923  1.00 81.34  ? 67   SER   C N    1 
ATOM   17198 C  CA   . SER   C  3  67  ? -12.320 -38.463 -55.550  1.00 79.89  ? 67   SER   C CA   1 
ATOM   17199 C  C    . SER   C  3  67  ? -13.172 -39.702 -55.312  1.00 81.59  ? 67   SER   C C    1 
ATOM   17200 O  O    . SER   C  3  67  ? -13.610 -40.362 -56.259  1.00 82.89  ? 67   SER   C O    1 
ATOM   17201 C  CB   . SER   C  3  67  ? -13.139 -37.200 -55.277  1.00 81.16  ? 67   SER   C CB   1 
ATOM   17202 O  OG   . SER   C  3  67  ? -14.373 -37.239 -55.971  1.00 86.64  ? 67   SER   C OG   1 
ATOM   17203 H  H    . SER   C  3  67  ? -12.157 -39.193 -57.357  1.00 97.64  ? 67   SER   C H    1 
ATOM   17204 H  HA   . SER   C  3  67  ? -11.568 -38.470 -54.938  1.00 95.90  ? 67   SER   C HA   1 
ATOM   17205 H  HB2  . SER   C  3  67  ? -13.315 -37.137 -54.325  1.00 97.43  ? 67   SER   C HB2  1 
ATOM   17206 H  HB3  . SER   C  3  67  ? -12.634 -36.426 -55.572  1.00 97.43  ? 67   SER   C HB3  1 
ATOM   17207 H  HG   . SER   C  3  67  ? -14.811 -36.539 -55.818  1.00 104.00 ? 67   SER   C HG   1 
ATOM   17208 N  N    . GLY   C  3  68  ? -13.408 -40.004 -54.039  1.00 82.28  ? 68   GLY   C N    1 
ATOM   17209 C  CA   . GLY   C  3  68  ? -14.212 -41.155 -53.683  1.00 86.97  ? 68   GLY   C CA   1 
ATOM   17210 C  C    . GLY   C  3  68  ? -13.596 -42.463 -54.134  1.00 86.87  ? 68   GLY   C C    1 
ATOM   17211 O  O    . GLY   C  3  68  ? -12.646 -42.953 -53.516  1.00 84.31  ? 68   GLY   C O    1 
ATOM   17212 H  H    . GLY   C  3  68  ? -13.111 -39.556 -53.368  1.00 98.78  ? 68   GLY   C H    1 
ATOM   17213 H  HA2  . GLY   C  3  68  ? -14.318 -41.185 -52.719  1.00 104.40 ? 68   GLY   C HA2  1 
ATOM   17214 H  HA3  . GLY   C  3  68  ? -15.087 -41.074 -54.094  1.00 104.40 ? 68   GLY   C HA3  1 
ATOM   17215 N  N    . THR   C  3  69  ? -14.125 -43.036 -55.218  1.00 89.26  ? 69   THR   C N    1 
ATOM   17216 C  CA   . THR   C  3  69  ? -13.651 -44.312 -55.731  1.00 88.58  ? 69   THR   C CA   1 
ATOM   17217 C  C    . THR   C  3  69  ? -13.079 -44.245 -57.139  1.00 90.12  ? 69   THR   C C    1 
ATOM   17218 O  O    . THR   C  3  69  ? -12.393 -45.189 -57.546  1.00 95.22  ? 69   THR   C O    1 
ATOM   17219 C  CB   . THR   C  3  69  ? -14.786 -45.350 -55.727  1.00 89.47  ? 69   THR   C CB   1 
ATOM   17220 O  OG1  . THR   C  3  69  ? -15.843 -44.913 -56.590  1.00 95.92  ? 69   THR   C OG1  1 
ATOM   17221 C  CG2  . THR   C  3  69  ? -15.329 -45.543 -54.322  1.00 90.90  ? 69   THR   C CG2  1 
ATOM   17222 H  H    . THR   C  3  69  ? -14.769 -42.696 -55.677  1.00 107.15 ? 69   THR   C H    1 
ATOM   17223 H  HA   . THR   C  3  69  ? -12.949 -44.629 -55.142  1.00 106.34 ? 69   THR   C HA   1 
ATOM   17224 H  HB   . THR   C  3  69  ? -14.444 -46.201 -56.042  1.00 107.40 ? 69   THR   C HB   1 
ATOM   17225 H  HG1  . THR   C  3  69  ? -16.445 -45.499 -56.626  1.00 115.14 ? 69   THR   C HG1  1 
ATOM   17226 H  HG21 . THR   C  3  69  ? -15.997 -46.247 -54.318  1.00 109.12 ? 69   THR   C HG21 1 
ATOM   17227 H  HG22 . THR   C  3  69  ? -14.610 -45.789 -53.719  1.00 109.12 ? 69   THR   C HG22 1 
ATOM   17228 H  HG23 . THR   C  3  69  ? -15.736 -44.721 -54.007  1.00 109.12 ? 69   THR   C HG23 1 
ATOM   17229 N  N    . ASP   C  3  70  ? -13.329 -43.173 -57.887  1.00 86.70  ? 70   ASP   C N    1 
ATOM   17230 C  CA   . ASP   C  3  70  ? -12.908 -43.064 -59.277  1.00 85.54  ? 70   ASP   C CA   1 
ATOM   17231 C  C    . ASP   C  3  70  ? -11.822 -42.006 -59.408  1.00 78.79  ? 70   ASP   C C    1 
ATOM   17232 O  O    . ASP   C  3  70  ? -11.961 -40.897 -58.883  1.00 78.39  ? 70   ASP   C O    1 
ATOM   17233 C  CB   . ASP   C  3  70  ? -14.095 -42.722 -60.180  1.00 92.66  ? 70   ASP   C CB   1 
ATOM   17234 C  CG   . ASP   C  3  70  ? -15.116 -43.841 -60.244  1.00 100.65 ? 70   ASP   C CG   1 
ATOM   17235 O  OD1  . ASP   C  3  70  ? -16.007 -43.886 -59.370  1.00 104.40 ? 70   ASP   C OD1  1 
ATOM   17236 O  OD2  . ASP   C  3  70  ? -15.021 -44.682 -61.163  1.00 104.26 ? 70   ASP   C OD2  1 
ATOM   17237 H  H    . ASP   C  3  70  ? -13.752 -42.481 -57.602  1.00 104.07 ? 70   ASP   C H    1 
ATOM   17238 H  HA   . ASP   C  3  70  ? -12.535 -43.912 -59.567  1.00 102.69 ? 70   ASP   C HA   1 
ATOM   17239 H  HB2  . ASP   C  3  70  ? -14.537 -41.930 -59.836  1.00 111.23 ? 70   ASP   C HB2  1 
ATOM   17240 H  HB3  . ASP   C  3  70  ? -13.772 -42.558 -61.080  1.00 111.23 ? 70   ASP   C HB3  1 
ATOM   17241 N  N    . TYR   C  3  71  ? -10.747 -42.353 -60.114  1.00 75.16  ? 71   TYR   C N    1 
ATOM   17242 C  CA   . TYR   C  3  71  ? -9.596  -41.478 -60.271  1.00 74.05  ? 71   TYR   C CA   1 
ATOM   17243 C  C    . TYR   C  3  71  ? -9.018  -41.662 -61.666  1.00 75.43  ? 71   TYR   C C    1 
ATOM   17244 O  O    . TYR   C  3  71  ? -9.284  -42.659 -62.342  1.00 82.51  ? 71   TYR   C O    1 
ATOM   17245 C  CB   . TYR   C  3  71  ? -8.521  -41.767 -59.215  1.00 71.11  ? 71   TYR   C CB   1 
ATOM   17246 C  CG   . TYR   C  3  71  ? -9.005  -41.619 -57.791  1.00 73.42  ? 71   TYR   C CG   1 
ATOM   17247 C  CD1  . TYR   C  3  71  ? -9.670  -42.656 -57.151  1.00 77.00  ? 71   TYR   C CD1  1 
ATOM   17248 C  CD2  . TYR   C  3  71  ? -8.794  -40.443 -57.087  1.00 75.57  ? 71   TYR   C CD2  1 
ATOM   17249 C  CE1  . TYR   C  3  71  ? -10.118 -42.522 -55.851  1.00 83.11  ? 71   TYR   C CE1  1 
ATOM   17250 C  CE2  . TYR   C  3  71  ? -9.233  -40.301 -55.785  1.00 79.73  ? 71   TYR   C CE2  1 
ATOM   17251 C  CZ   . TYR   C  3  71  ? -9.891  -41.344 -55.171  1.00 83.24  ? 71   TYR   C CZ   1 
ATOM   17252 O  OH   . TYR   C  3  71  ? -10.331 -41.204 -53.875  1.00 84.80  ? 71   TYR   C OH   1 
ATOM   17253 H  H    . TYR   C  3  71  ? -10.662 -43.107 -60.518  1.00 90.22  ? 71   TYR   C H    1 
ATOM   17254 H  HA   . TYR   C  3  71  ? -9.876  -40.554 -60.177  1.00 88.90  ? 71   TYR   C HA   1 
ATOM   17255 H  HB2  . TYR   C  3  71  ? -8.211  -42.679 -59.329  1.00 85.37  ? 71   TYR   C HB2  1 
ATOM   17256 H  HB3  . TYR   C  3  71  ? -7.785  -41.149 -59.343  1.00 85.37  ? 71   TYR   C HB3  1 
ATOM   17257 H  HD1  . TYR   C  3  71  ? -9.817  -43.454 -57.605  1.00 92.44  ? 71   TYR   C HD1  1 
ATOM   17258 H  HD2  . TYR   C  3  71  ? -8.349  -39.738 -57.498  1.00 90.72  ? 71   TYR   C HD2  1 
ATOM   17259 H  HE1  . TYR   C  3  71  ? -10.569 -43.222 -55.437  1.00 99.77  ? 71   TYR   C HE1  1 
ATOM   17260 H  HE2  . TYR   C  3  71  ? -9.085  -39.506 -55.326  1.00 95.71  ? 71   TYR   C HE2  1 
ATOM   17261 H  HH   . TYR   C  3  71  ? -10.941 -41.760 -53.717  1.00 101.80 ? 71   TYR   C HH   1 
ATOM   17262 N  N    . SER   C  3  72  ? -8.213  -40.691 -62.092  1.00 68.20  ? 72   SER   C N    1 
ATOM   17263 C  CA   . SER   C  3  72  ? -7.641  -40.732 -63.429  1.00 73.60  ? 72   SER   C CA   1 
ATOM   17264 C  C    . SER   C  3  72  ? -6.344  -39.940 -63.481  1.00 73.84  ? 72   SER   C C    1 
ATOM   17265 O  O    . SER   C  3  72  ? -6.250  -38.841 -62.928  1.00 76.60  ? 72   SER   C O    1 
ATOM   17266 C  CB   . SER   C  3  72  ? -8.622  -40.176 -64.467  1.00 80.86  ? 72   SER   C CB   1 
ATOM   17267 O  OG   . SER   C  3  72  ? -8.834  -38.789 -64.270  1.00 83.28  ? 72   SER   C OG   1 
ATOM   17268 H  H    . SER   C  3  72  ? -7.986  -40.004 -61.627  1.00 81.88  ? 72   SER   C H    1 
ATOM   17269 H  HA   . SER   C  3  72  ? -7.429  -41.654 -63.644  1.00 88.36  ? 72   SER   C HA   1 
ATOM   17270 H  HB2  . SER   C  3  72  ? -8.256  -40.316 -65.354  1.00 97.07  ? 72   SER   C HB2  1 
ATOM   17271 H  HB3  . SER   C  3  72  ? -9.470  -40.640 -64.380  1.00 97.07  ? 72   SER   C HB3  1 
ATOM   17272 H  HG   . SER   C  3  72  ? -9.389  -38.500 -64.831  1.00 99.97  ? 72   SER   C HG   1 
ATOM   17273 N  N    . LEU   C  3  73  ? -5.352  -40.512 -64.157  1.00 72.58  ? 73   LEU   C N    1 
ATOM   17274 C  CA   . LEU   C  3  73  ? -4.107  -39.831 -64.485  1.00 69.98  ? 73   LEU   C CA   1 
ATOM   17275 C  C    . LEU   C  3  73  ? -4.197  -39.325 -65.916  1.00 71.99  ? 73   LEU   C C    1 
ATOM   17276 O  O    . LEU   C  3  73  ? -4.627  -40.060 -66.811  1.00 77.49  ? 73   LEU   C O    1 
ATOM   17277 C  CB   . LEU   C  3  73  ? -2.912  -40.772 -64.336  1.00 69.68  ? 73   LEU   C CB   1 
ATOM   17278 C  CG   . LEU   C  3  73  ? -1.554  -40.273 -64.836  1.00 70.75  ? 73   LEU   C CG   1 
ATOM   17279 C  CD1  . LEU   C  3  73  ? -0.941  -39.302 -63.841  1.00 68.46  ? 73   LEU   C CD1  1 
ATOM   17280 C  CD2  . LEU   C  3  73  ? -0.629  -41.450 -65.096  1.00 70.61  ? 73   LEU   C CD2  1 
ATOM   17281 H  H    . LEU   C  3  73  ? -5.379  -41.322 -64.446  1.00 87.13  ? 73   LEU   C H    1 
ATOM   17282 H  HA   . LEU   C  3  73  ? -3.973  -39.080 -63.886  1.00 84.02  ? 73   LEU   C HA   1 
ATOM   17283 H  HB2  . LEU   C  3  73  ? -2.808  -40.971 -63.392  1.00 83.65  ? 73   LEU   C HB2  1 
ATOM   17284 H  HB3  . LEU   C  3  73  ? -3.111  -41.584 -64.827  1.00 83.65  ? 73   LEU   C HB3  1 
ATOM   17285 H  HG   . LEU   C  3  73  ? -1.674  -39.796 -65.672  1.00 84.93  ? 73   LEU   C HG   1 
ATOM   17286 H  HD11 . LEU   C  3  73  ? -0.084  -39.001 -64.181  1.00 82.19  ? 73   LEU   C HD11 1 
ATOM   17287 H  HD12 . LEU   C  3  73  ? -1.538  -38.545 -63.730  1.00 82.19  ? 73   LEU   C HD12 1 
ATOM   17288 H  HD13 . LEU   C  3  73  ? -0.820  -39.755 -62.992  1.00 82.19  ? 73   LEU   C HD13 1 
ATOM   17289 H  HD21 . LEU   C  3  73  ? 0.243   -41.115 -65.358  1.00 84.77  ? 73   LEU   C HD21 1 
ATOM   17290 H  HD22 . LEU   C  3  73  ? -0.551  -41.977 -64.285  1.00 84.77  ? 73   LEU   C HD22 1 
ATOM   17291 H  HD23 . LEU   C  3  73  ? -1.002  -41.994 -65.809  1.00 84.77  ? 73   LEU   C HD23 1 
ATOM   17292 N  N    . THR   C  3  74  ? -3.783  -38.081 -66.132  1.00 71.82  ? 74   THR   C N    1 
ATOM   17293 C  CA   . THR   C  3  74  ? -3.857  -37.458 -67.444  1.00 78.04  ? 74   THR   C CA   1 
ATOM   17294 C  C    . THR   C  3  74  ? -2.461  -37.083 -67.916  1.00 76.51  ? 74   THR   C C    1 
ATOM   17295 O  O    . THR   C  3  74  ? -1.715  -36.411 -67.196  1.00 76.36  ? 74   THR   C O    1 
ATOM   17296 C  CB   . THR   C  3  74  ? -4.752  -36.216 -67.418  1.00 81.01  ? 74   THR   C CB   1 
ATOM   17297 O  OG1  . THR   C  3  74  ? -6.071  -36.586 -66.999  1.00 84.04  ? 74   THR   C OG1  1 
ATOM   17298 C  CG2  . THR   C  3  74  ? -4.819  -35.582 -68.801  1.00 85.47  ? 74   THR   C CG2  1 
ATOM   17299 H  H    . THR   C  3  74  ? -3.450  -37.573 -65.524  1.00 86.22  ? 74   THR   C H    1 
ATOM   17300 H  HA   . THR   C  3  74  ? -4.229  -38.093 -68.076  1.00 93.68  ? 74   THR   C HA   1 
ATOM   17301 H  HB   . THR   C  3  74  ? -4.387  -35.565 -66.799  1.00 97.25  ? 74   THR   C HB   1 
ATOM   17302 H  HG1  . THR   C  3  74  ? -6.556  -35.903 -66.940  1.00 100.88 ? 74   THR   C HG1  1 
ATOM   17303 H  HG21 . THR   C  3  74  ? -5.422  -34.822 -68.788  1.00 102.60 ? 74   THR   C HG21 1 
ATOM   17304 H  HG22 . THR   C  3  74  ? -3.938  -35.279 -69.070  1.00 102.60 ? 74   THR   C HG22 1 
ATOM   17305 H  HG23 . THR   C  3  74  ? -5.141  -36.229 -69.448  1.00 102.60 ? 74   THR   C HG23 1 
ATOM   17306 N  N    . ILE   C  3  75  ? -2.117  -37.521 -69.123  1.00 74.30  ? 75   ILE   C N    1 
ATOM   17307 C  CA   . ILE   C  3  75  ? -0.894  -37.112 -69.800  1.00 76.86  ? 75   ILE   C CA   1 
ATOM   17308 C  C    . ILE   C  3  75  ? -1.295  -36.214 -70.959  1.00 83.47  ? 75   ILE   C C    1 
ATOM   17309 O  O    . ILE   C  3  75  ? -2.069  -36.626 -71.833  1.00 86.26  ? 75   ILE   C O    1 
ATOM   17310 C  CB   . ILE   C  3  75  ? -0.078  -38.311 -70.307  1.00 76.77  ? 75   ILE   C CB   1 
ATOM   17311 C  CG1  . ILE   C  3  75  ? -0.032  -39.431 -69.264  1.00 74.36  ? 75   ILE   C CG1  1 
ATOM   17312 C  CG2  . ILE   C  3  75  ? 1.329   -37.850 -70.667  1.00 75.84  ? 75   ILE   C CG2  1 
ATOM   17313 C  CD1  . ILE   C  3  75  ? 0.650   -40.695 -69.760  1.00 72.45  ? 75   ILE   C CD1  1 
ATOM   17314 H  H    . ILE   C  3  75  ? -2.591  -38.072 -69.582  1.00 89.20  ? 75   ILE   C H    1 
ATOM   17315 H  HA   . ILE   C  3  75  ? -0.341  -36.612 -69.179  1.00 92.27  ? 75   ILE   C HA   1 
ATOM   17316 H  HB   . ILE   C  3  75  ? -0.512  -38.668 -71.098  1.00 92.17  ? 75   ILE   C HB   1 
ATOM   17317 H  HG12 . ILE   C  3  75  ? 0.455   -39.115 -68.488  1.00 89.26  ? 75   ILE   C HG12 1 
ATOM   17318 H  HG13 . ILE   C  3  75  ? -0.940  -39.662 -69.014  1.00 89.26  ? 75   ILE   C HG13 1 
ATOM   17319 H  HG21 . ILE   C  3  75  ? 1.821   -38.599 -71.037  1.00 91.05  ? 75   ILE   C HG21 1 
ATOM   17320 H  HG22 . ILE   C  3  75  ? 1.269   -37.137 -71.322  1.00 91.05  ? 75   ILE   C HG22 1 
ATOM   17321 H  HG23 . ILE   C  3  75  ? 1.770   -37.528 -69.866  1.00 91.05  ? 75   ILE   C HG23 1 
ATOM   17322 H  HD11 . ILE   C  3  75  ? 0.664   -41.348 -69.043  1.00 86.98  ? 75   ILE   C HD11 1 
ATOM   17323 H  HD12 . ILE   C  3  75  ? 0.155   -41.045 -70.517  1.00 86.98  ? 75   ILE   C HD12 1 
ATOM   17324 H  HD13 . ILE   C  3  75  ? 1.557   -40.479 -70.029  1.00 86.98  ? 75   ILE   C HD13 1 
ATOM   17325 N  N    . SER   C  3  76  ? -0.776  -34.993 -70.969  1.00 82.61  ? 76   SER   C N    1 
ATOM   17326 C  CA   . SER   C  3  76  ? -0.991  -34.056 -72.060  1.00 91.98  ? 76   SER   C CA   1 
ATOM   17327 C  C    . SER   C  3  76  ? 0.298   -33.925 -72.860  1.00 95.95  ? 76   SER   C C    1 
ATOM   17328 O  O    . SER   C  3  76  ? 1.393   -33.910 -72.291  1.00 102.64 ? 76   SER   C O    1 
ATOM   17329 C  CB   . SER   C  3  76  ? -1.433  -32.688 -71.533  1.00 94.56  ? 76   SER   C CB   1 
ATOM   17330 O  OG   . SER   C  3  76  ? -0.334  -31.948 -71.032  1.00 98.20  ? 76   SER   C OG   1 
ATOM   17331 H  H    . SER   C  3  76  ? -0.284  -34.678 -70.338  1.00 99.17  ? 76   SER   C H    1 
ATOM   17332 H  HA   . SER   C  3  76  ? -1.689  -34.381 -72.649  1.00 110.41 ? 76   SER   C HA   1 
ATOM   17333 H  HB2  . SER   C  3  76  ? -1.842  -32.190 -72.258  1.00 113.51 ? 76   SER   C HB2  1 
ATOM   17334 H  HB3  . SER   C  3  76  ? -2.074  -32.820 -70.817  1.00 113.51 ? 76   SER   C HB3  1 
ATOM   17335 H  HG   . SER   C  3  76  ? 0.064   -31.561 -71.663  1.00 117.88 ? 76   SER   C HG   1 
ATOM   17336 N  N    . ASN   C  3  77  ? 0.165   -33.843 -74.181  1.00 96.86  ? 77   ASN   C N    1 
ATOM   17337 C  CA   . ASN   C  3  77  ? 1.309   -33.753 -75.086  1.00 98.30  ? 77   ASN   C CA   1 
ATOM   17338 C  C    . ASN   C  3  77  ? 2.313   -34.874 -74.795  1.00 96.39  ? 77   ASN   C C    1 
ATOM   17339 O  O    . ASN   C  3  77  ? 3.436   -34.657 -74.340  1.00 100.06 ? 77   ASN   C O    1 
ATOM   17340 C  CB   . ASN   C  3  77  ? 1.968   -32.375 -74.978  1.00 105.29 ? 77   ASN   C CB   1 
ATOM   17341 C  CG   . ASN   C  3  77  ? 0.958   -31.260 -74.785  1.00 111.98 ? 77   ASN   C CG   1 
ATOM   17342 O  OD1  . ASN   C  3  77  ? 0.644   -30.881 -73.657  1.00 111.46 ? 77   ASN   C OD1  1 
ATOM   17343 N  ND2  . ASN   C  3  77  ? 0.442   -30.728 -75.887  1.00 116.99 ? 77   ASN   C ND2  1 
ATOM   17344 H  H    . ASN   C  3  77  ? -0.594  -33.838 -74.586  1.00 116.27 ? 77   ASN   C H    1 
ATOM   17345 H  HA   . ASN   C  3  77  ? 0.992   -33.868 -75.996  1.00 117.99 ? 77   ASN   C HA   1 
ATOM   17346 H  HB2  . ASN   C  3  77  ? 2.570   -32.370 -74.217  1.00 126.39 ? 77   ASN   C HB2  1 
ATOM   17347 H  HB3  . ASN   C  3  77  ? 2.462   -32.196 -75.793  1.00 126.39 ? 77   ASN   C HB3  1 
ATOM   17348 H  HD21 . ASN   C  3  77  ? -0.135  -30.093 -75.829  1.00 140.42 ? 77   ASN   C HD21 1 
ATOM   17349 H  HD22 . ASN   C  3  77  ? 0.685   -31.019 -76.659  1.00 140.42 ? 77   ASN   C HD22 1 
ATOM   17350 N  N    . LEU   C  3  78  ? 1.857   -36.092 -75.079  1.00 93.84  ? 78   LEU   C N    1 
ATOM   17351 C  CA   . LEU   C  3  78  ? 2.651   -37.285 -74.815  1.00 90.42  ? 78   LEU   C CA   1 
ATOM   17352 C  C    . LEU   C  3  78  ? 3.999   -37.220 -75.527  1.00 99.00  ? 78   LEU   C C    1 
ATOM   17353 O  O    . LEU   C  3  78  ? 4.102   -36.749 -76.663  1.00 102.04 ? 78   LEU   C O    1 
ATOM   17354 C  CB   . LEU   C  3  78  ? 1.865   -38.522 -75.257  1.00 80.73  ? 78   LEU   C CB   1 
ATOM   17355 C  CG   . LEU   C  3  78  ? 2.464   -39.900 -74.984  1.00 76.91  ? 78   LEU   C CG   1 
ATOM   17356 C  CD1  . LEU   C  3  78  ? 1.368   -40.884 -74.605  1.00 72.70  ? 78   LEU   C CD1  1 
ATOM   17357 C  CD2  . LEU   C  3  78  ? 3.219   -40.396 -76.204  1.00 72.04  ? 78   LEU   C CD2  1 
ATOM   17358 H  H    . LEU   C  3  78  ? 1.088   -36.254 -75.426  1.00 112.65 ? 78   LEU   C H    1 
ATOM   17359 H  HA   . LEU   C  3  78  ? 2.833   -37.355 -73.864  1.00 108.54 ? 78   LEU   C HA   1 
ATOM   17360 H  HB2  . LEU   C  3  78  ? 1.006   -38.499 -74.808  1.00 96.91  ? 78   LEU   C HB2  1 
ATOM   17361 H  HB3  . LEU   C  3  78  ? 1.739   -38.460 -76.217  1.00 96.91  ? 78   LEU   C HB3  1 
ATOM   17362 H  HG   . LEU   C  3  78  ? 3.087   -39.837 -74.243  1.00 92.32  ? 78   LEU   C HG   1 
ATOM   17363 H  HD11 . LEU   C  3  78  ? 1.768   -41.752 -74.436  1.00 87.27  ? 78   LEU   C HD11 1 
ATOM   17364 H  HD12 . LEU   C  3  78  ? 0.920   -40.565 -73.806  1.00 87.27  ? 78   LEU   C HD12 1 
ATOM   17365 H  HD13 . LEU   C  3  78  ? 0.734   -40.948 -75.336  1.00 87.27  ? 78   LEU   C HD13 1 
ATOM   17366 H  HD21 . LEU   C  3  78  ? 3.584   -41.274 -76.014  1.00 86.26  ? 78   LEU   C HD21 1 
ATOM   17367 H  HD22 . LEU   C  3  78  ? 2.607   -40.447 -76.955  1.00 86.26  ? 78   LEU   C HD22 1 
ATOM   17368 H  HD23 . LEU   C  3  78  ? 3.937   -39.775 -76.404  1.00 86.26  ? 78   LEU   C HD23 1 
ATOM   17369 N  N    . ASP   C  3  79  ? 5.036   -37.705 -74.847  1.00 100.01 ? 79   ASP   C N    1 
ATOM   17370 C  CA   . ASP   C  3  79  ? 6.413   -37.676 -75.324  1.00 102.76 ? 79   ASP   C CA   1 
ATOM   17371 C  C    . ASP   C  3  79  ? 6.861   -39.083 -75.707  1.00 102.98 ? 79   ASP   C C    1 
ATOM   17372 O  O    . ASP   C  3  79  ? 6.213   -40.079 -75.377  1.00 101.30 ? 79   ASP   C O    1 
ATOM   17373 C  CB   . ASP   C  3  79  ? 7.338   -37.098 -74.245  1.00 102.16 ? 79   ASP   C CB   1 
ATOM   17374 C  CG   . ASP   C  3  79  ? 8.541   -36.379 -74.826  1.00 107.73 ? 79   ASP   C CG   1 
ATOM   17375 O  OD1  . ASP   C  3  79  ? 8.513   -35.131 -74.895  1.00 108.45 ? 79   ASP   C OD1  1 
ATOM   17376 O  OD2  . ASP   C  3  79  ? 9.512   -37.059 -75.217  1.00 106.91 ? 79   ASP   C OD2  1 
ATOM   17377 H  H    . ASP   C  3  79  ? 4.962   -38.071 -74.072  1.00 120.05 ? 79   ASP   C H    1 
ATOM   17378 H  HA   . ASP   C  3  79  ? 6.470   -37.114 -76.112  1.00 123.35 ? 79   ASP   C HA   1 
ATOM   17379 H  HB2  . ASP   C  3  79  ? 6.840   -36.462 -73.708  1.00 122.63 ? 79   ASP   C HB2  1 
ATOM   17380 H  HB3  . ASP   C  3  79  ? 7.663   -37.821 -73.686  1.00 122.63 ? 79   ASP   C HB3  1 
ATOM   17381 N  N    . GLN   C  3  80  ? 7.993   -39.163 -76.415  1.00 107.02 ? 80   GLN   C N    1 
ATOM   17382 C  CA   . GLN   C  3  80  ? 8.534   -40.472 -76.771  1.00 107.86 ? 80   GLN   C CA   1 
ATOM   17383 C  C    . GLN   C  3  80  ? 8.892   -41.272 -75.525  1.00 105.39 ? 80   GLN   C C    1 
ATOM   17384 O  O    . GLN   C  3  80  ? 8.711   -42.494 -75.491  1.00 105.30 ? 80   GLN   C O    1 
ATOM   17385 C  CB   . GLN   C  3  80  ? 9.761   -40.321 -77.674  1.00 109.49 ? 80   GLN   C CB   1 
ATOM   17386 C  CG   . GLN   C  3  80  ? 10.471  -41.641 -77.993  1.00 112.23 ? 80   GLN   C CG   1 
ATOM   17387 C  CD   . GLN   C  3  80  ? 9.581   -42.633 -78.720  1.00 115.42 ? 80   GLN   C CD   1 
ATOM   17388 O  OE1  . GLN   C  3  80  ? 9.019   -42.326 -79.772  1.00 120.36 ? 80   GLN   C OE1  1 
ATOM   17389 N  NE2  . GLN   C  3  80  ? 9.448   -43.831 -78.160  1.00 114.26 ? 80   GLN   C NE2  1 
ATOM   17390 H  H    . GLN   C  3  80  ? 8.452   -38.491 -76.693  1.00 128.46 ? 80   GLN   C H    1 
ATOM   17391 H  HA   . GLN   C  3  80  ? 7.858   -40.959 -77.269  1.00 129.47 ? 80   GLN   C HA   1 
ATOM   17392 H  HB2  . GLN   C  3  80  ? 9.480   -39.926 -78.515  1.00 131.42 ? 80   GLN   C HB2  1 
ATOM   17393 H  HB3  . GLN   C  3  80  ? 10.401  -39.741 -77.233  1.00 131.42 ? 80   GLN   C HB3  1 
ATOM   17394 H  HG2  . GLN   C  3  80  ? 11.238  -41.457 -78.559  1.00 134.72 ? 80   GLN   C HG2  1 
ATOM   17395 H  HG3  . GLN   C  3  80  ? 10.761  -42.051 -77.164  1.00 134.72 ? 80   GLN   C HG3  1 
ATOM   17396 H  HE21 . GLN   C  3  80  ? 9.856   -44.010 -77.425  1.00 137.15 ? 80   GLN   C HE21 1 
ATOM   17397 H  HE22 . GLN   C  3  80  ? 8.954   -44.428 -78.534  1.00 137.15 ? 80   GLN   C HE22 1 
ATOM   17398 N  N    . GLU   C  3  81  ? 9.403   -40.603 -74.491  1.00 107.98 ? 81   GLU   C N    1 
ATOM   17399 C  CA   . GLU   C  3  81  ? 9.803   -41.290 -73.268  1.00 110.06 ? 81   GLU   C CA   1 
ATOM   17400 C  C    . GLU   C  3  81  ? 8.612   -41.715 -72.418  1.00 103.99 ? 81   GLU   C C    1 
ATOM   17401 O  O    . GLU   C  3  81  ? 8.781   -42.514 -71.490  1.00 102.54 ? 81   GLU   C O    1 
ATOM   17402 C  CB   . GLU   C  3  81  ? 10.740  -40.391 -72.452  1.00 115.23 ? 81   GLU   C CB   1 
ATOM   17403 C  CG   . GLU   C  3  81  ? 10.215  -38.978 -72.200  1.00 119.20 ? 81   GLU   C CG   1 
ATOM   17404 C  CD   . GLU   C  3  81  ? 11.141  -38.160 -71.319  1.00 123.60 ? 81   GLU   C CD   1 
ATOM   17405 O  OE1  . GLU   C  3  81  ? 11.268  -36.940 -71.555  1.00 127.95 ? 81   GLU   C OE1  1 
ATOM   17406 O  OE2  . GLU   C  3  81  ? 11.747  -38.740 -70.393  1.00 125.25 ? 81   GLU   C OE2  1 
ATOM   17407 H  H    . GLU   C  3  81  ? 9.528   -39.752 -74.474  1.00 129.62 ? 81   GLU   C H    1 
ATOM   17408 H  HA   . GLU   C  3  81  ? 10.296  -42.093 -73.500  1.00 132.11 ? 81   GLU   C HA   1 
ATOM   17409 H  HB2  . GLU   C  3  81  ? 10.889  -40.805 -71.588  1.00 138.32 ? 81   GLU   C HB2  1 
ATOM   17410 H  HB3  . GLU   C  3  81  ? 11.581  -40.308 -72.930  1.00 138.32 ? 81   GLU   C HB3  1 
ATOM   17411 H  HG2  . GLU   C  3  81  ? 10.124  -38.518 -73.049  1.00 143.07 ? 81   GLU   C HG2  1 
ATOM   17412 H  HG3  . GLU   C  3  81  ? 9.353   -39.035 -71.759  1.00 143.07 ? 81   GLU   C HG3  1 
ATOM   17413 N  N    . ASP   C  3  82  ? 7.411   -41.213 -72.720  1.00 100.46 ? 82   ASP   C N    1 
ATOM   17414 C  CA   . ASP   C  3  82  ? 6.230   -41.535 -71.925  1.00 88.93  ? 82   ASP   C CA   1 
ATOM   17415 C  C    . ASP   C  3  82  ? 5.800   -42.996 -72.057  1.00 84.79  ? 82   ASP   C C    1 
ATOM   17416 O  O    . ASP   C  3  82  ? 5.172   -43.532 -71.137  1.00 82.69  ? 82   ASP   C O    1 
ATOM   17417 C  CB   . ASP   C  3  82  ? 5.081   -40.610 -72.330  1.00 87.24  ? 82   ASP   C CB   1 
ATOM   17418 C  CG   . ASP   C  3  82  ? 5.005   -39.370 -71.470  1.00 90.90  ? 82   ASP   C CG   1 
ATOM   17419 O  OD1  . ASP   C  3  82  ? 4.393   -39.442 -70.386  1.00 90.26  ? 82   ASP   C OD1  1 
ATOM   17420 O  OD2  . ASP   C  3  82  ? 5.571   -38.328 -71.864  1.00 96.29  ? 82   ASP   C OD2  1 
ATOM   17421 H  H    . ASP   C  3  82  ? 7.256   -40.684 -73.381  1.00 120.58 ? 82   ASP   C H    1 
ATOM   17422 H  HA   . ASP   C  3  82  ? 6.443   -41.388 -70.990  1.00 106.76 ? 82   ASP   C HA   1 
ATOM   17423 H  HB2  . ASP   C  3  82  ? 5.209   -40.330 -73.250  1.00 104.72 ? 82   ASP   C HB2  1 
ATOM   17424 H  HB3  . ASP   C  3  82  ? 4.243   -41.089 -72.243  1.00 104.72 ? 82   ASP   C HB3  1 
ATOM   17425 N  N    . ILE   C  3  83  ? 6.097   -43.652 -73.180  1.00 89.72  ? 83   ILE   C N    1 
ATOM   17426 C  CA   . ILE   C  3  83  ? 5.704   -45.049 -73.368  1.00 94.12  ? 83   ILE   C CA   1 
ATOM   17427 C  C    . ILE   C  3  83  ? 6.164   -45.888 -72.179  1.00 87.10  ? 83   ILE   C C    1 
ATOM   17428 O  O    . ILE   C  3  83  ? 7.362   -46.118 -71.977  1.00 86.85  ? 83   ILE   C O    1 
ATOM   17429 C  CB   . ILE   C  3  83  ? 6.253   -45.615 -74.694  1.00 107.36 ? 83   ILE   C CB   1 
ATOM   17430 C  CG1  . ILE   C  3  83  ? 7.776   -45.485 -74.753  1.00 115.51 ? 83   ILE   C CG1  1 
ATOM   17431 C  CG2  . ILE   C  3  83  ? 5.617   -44.898 -75.881  1.00 114.65 ? 83   ILE   C CG2  1 
ATOM   17432 C  CD1  . ILE   C  3  83  ? 8.415   -46.254 -75.866  1.00 126.66 ? 83   ILE   C CD1  1 
ATOM   17433 H  H    . ILE   C  3  83  ? 6.524   -43.312 -73.844  1.00 107.70 ? 83   ILE   C H    1 
ATOM   17434 H  HA   . ILE   C  3  83  ? 4.735   -45.089 -73.399  1.00 112.98 ? 83   ILE   C HA   1 
ATOM   17435 H  HB   . ILE   C  3  83  ? 6.026   -46.557 -74.735  1.00 128.87 ? 83   ILE   C HB   1 
ATOM   17436 H  HG12 . ILE   C  3  83  ? 8.003   -44.549 -74.874  1.00 138.65 ? 83   ILE   C HG12 1 
ATOM   17437 H  HG13 . ILE   C  3  83  ? 8.148   -45.811 -73.919  1.00 138.65 ? 83   ILE   C HG13 1 
ATOM   17438 H  HG21 . ILE   C  3  83  ? 6.288   -44.772 -76.570  1.00 137.61 ? 83   ILE   C HG21 1 
ATOM   17439 H  HG22 . ILE   C  3  83  ? 4.889   -45.439 -76.223  1.00 137.61 ? 83   ILE   C HG22 1 
ATOM   17440 H  HG23 . ILE   C  3  83  ? 5.280   -44.038 -75.586  1.00 137.61 ? 83   ILE   C HG23 1 
ATOM   17441 H  HD11 . ILE   C  3  83  ? 9.377   -46.248 -75.741  1.00 152.03 ? 83   ILE   C HD11 1 
ATOM   17442 H  HD12 . ILE   C  3  83  ? 8.085   -47.165 -75.850  1.00 152.03 ? 83   ILE   C HD12 1 
ATOM   17443 H  HD13 . ILE   C  3  83  ? 8.189   -45.834 -76.710  1.00 152.03 ? 83   ILE   C HD13 1 
ATOM   17444 N  N    . ALA   C  3  84  ? 5.215   -46.360 -71.381  1.00 80.42  ? 84   ALA   C N    1 
ATOM   17445 C  CA   . ALA   C  3  84  ? 5.538   -47.070 -70.150  1.00 75.31  ? 84   ALA   C CA   1 
ATOM   17446 C  C    . ALA   C  3  84  ? 4.240   -47.658 -69.614  1.00 70.71  ? 84   ALA   C C    1 
ATOM   17447 O  O    . ALA   C  3  84  ? 3.162   -47.426 -70.165  1.00 71.45  ? 84   ALA   C O    1 
ATOM   17448 C  CB   . ALA   C  3  84  ? 6.206   -46.136 -69.133  1.00 77.11  ? 84   ALA   C CB   1 
ATOM   17449 H  H    . ALA   C  3  84  ? 4.372   -46.283 -71.532  1.00 96.55  ? 84   ALA   C H    1 
ATOM   17450 H  HA   . ALA   C  3  84  ? 6.150   -47.800 -70.328  1.00 90.40  ? 84   ALA   C HA   1 
ATOM   17451 H  HB1  . ALA   C  3  84  ? 6.375   -46.630 -68.315  1.00 92.57  ? 84   ALA   C HB1  1 
ATOM   17452 H  HB2  . ALA   C  3  84  ? 7.042   -45.813 -69.503  1.00 92.57  ? 84   ALA   C HB2  1 
ATOM   17453 H  HB3  . ALA   C  3  84  ? 5.613   -45.390 -68.953  1.00 92.57  ? 84   ALA   C HB3  1 
ATOM   17454 N  N    . THR   C  3  85  ? 4.355   -48.434 -68.543  1.00 68.48  ? 85   THR   C N    1 
ATOM   17455 C  CA   . THR   C  3  85  ? 3.184   -48.945 -67.844  1.00 71.16  ? 85   THR   C CA   1 
ATOM   17456 C  C    . THR   C  3  85  ? 2.894   -48.052 -66.645  1.00 72.89  ? 85   THR   C C    1 
ATOM   17457 O  O    . THR   C  3  85  ? 3.814   -47.613 -65.947  1.00 76.23  ? 85   THR   C O    1 
ATOM   17458 C  CB   . THR   C  3  85  ? 3.381   -50.391 -67.388  1.00 72.91  ? 85   THR   C CB   1 
ATOM   17459 O  OG1  . THR   C  3  85  ? 3.880   -51.178 -68.477  1.00 71.66  ? 85   THR   C OG1  1 
ATOM   17460 C  CG2  . THR   C  3  85  ? 2.054   -50.978 -66.917  1.00 75.66  ? 85   THR   C CG2  1 
ATOM   17461 H  H    . THR   C  3  85  ? 5.104   -48.680 -68.201  1.00 82.22  ? 85   THR   C H    1 
ATOM   17462 H  HA   . THR   C  3  85  ? 2.419   -48.936 -68.442  1.00 85.43  ? 85   THR   C HA   1 
ATOM   17463 H  HB   . THR   C  3  85  ? 4.015   -50.416 -66.654  1.00 87.53  ? 85   THR   C HB   1 
ATOM   17464 H  HG1  . THR   C  3  85  ? 3.827   -51.995 -68.289  1.00 86.03  ? 85   THR   C HG1  1 
ATOM   17465 H  HG21 . THR   C  3  85  ? 2.155   -51.926 -66.741  1.00 90.83  ? 85   THR   C HG21 1 
ATOM   17466 H  HG22 . THR   C  3  85  ? 1.766   -50.536 -66.103  1.00 90.83  ? 85   THR   C HG22 1 
ATOM   17467 H  HG23 . THR   C  3  85  ? 1.376   -50.855 -67.599  1.00 90.83  ? 85   THR   C HG23 1 
ATOM   17468 N  N    . TYR   C  3  86  ? 1.612   -47.779 -66.416  1.00 70.56  ? 86   TYR   C N    1 
ATOM   17469 C  CA   . TYR   C  3  86  ? 1.176   -46.875 -65.358  1.00 68.39  ? 86   TYR   C CA   1 
ATOM   17470 C  C    . TYR   C  3  86  ? 0.270   -47.627 -64.395  1.00 68.32  ? 86   TYR   C C    1 
ATOM   17471 O  O    . TYR   C  3  86  ? -0.739  -48.208 -64.809  1.00 68.41  ? 86   TYR   C O    1 
ATOM   17472 C  CB   . TYR   C  3  86  ? 0.460   -45.658 -65.947  1.00 66.04  ? 86   TYR   C CB   1 
ATOM   17473 C  CG   . TYR   C  3  86  ? 1.374   -44.784 -66.773  1.00 67.98  ? 86   TYR   C CG   1 
ATOM   17474 C  CD1  . TYR   C  3  86  ? 1.598   -45.055 -68.116  1.00 68.75  ? 86   TYR   C CD1  1 
ATOM   17475 C  CD2  . TYR   C  3  86  ? 2.025   -43.697 -66.207  1.00 67.55  ? 86   TYR   C CD2  1 
ATOM   17476 C  CE1  . TYR   C  3  86  ? 2.439   -44.264 -68.874  1.00 70.91  ? 86   TYR   C CE1  1 
ATOM   17477 C  CE2  . TYR   C  3  86  ? 2.868   -42.900 -66.957  1.00 68.72  ? 86   TYR   C CE2  1 
ATOM   17478 C  CZ   . TYR   C  3  86  ? 3.071   -43.187 -68.290  1.00 71.34  ? 86   TYR   C CZ   1 
ATOM   17479 O  OH   . TYR   C  3  86  ? 3.911   -42.394 -69.038  1.00 74.19  ? 86   TYR   C OH   1 
ATOM   17480 H  H    . TYR   C  3  86  ? 0.963   -48.113 -66.871  1.00 84.71  ? 86   TYR   C H    1 
ATOM   17481 H  HA   . TYR   C  3  86  ? 1.948   -46.568 -64.858  1.00 82.10  ? 86   TYR   C HA   1 
ATOM   17482 H  HB2  . TYR   C  3  86  ? -0.262  -45.962 -66.518  1.00 79.28  ? 86   TYR   C HB2  1 
ATOM   17483 H  HB3  . TYR   C  3  86  ? 0.105   -45.120 -65.222  1.00 79.28  ? 86   TYR   C HB3  1 
ATOM   17484 H  HD1  . TYR   C  3  86  ? 1.174   -45.782 -68.512  1.00 82.53  ? 86   TYR   C HD1  1 
ATOM   17485 H  HD2  . TYR   C  3  86  ? 1.893   -43.503 -65.308  1.00 81.10  ? 86   TYR   C HD2  1 
ATOM   17486 H  HE1  . TYR   C  3  86  ? 2.579   -44.457 -69.773  1.00 85.13  ? 86   TYR   C HE1  1 
ATOM   17487 H  HE2  . TYR   C  3  86  ? 3.295   -42.173 -66.565  1.00 82.50  ? 86   TYR   C HE2  1 
ATOM   17488 H  HH   . TYR   C  3  86  ? 4.101   -42.778 -69.760  1.00 89.06  ? 86   TYR   C HH   1 
ATOM   17489 N  N    . PHE   C  3  87  ? 0.638   -47.616 -63.116  1.00 67.37  ? 87   PHE   C N    1 
ATOM   17490 C  CA   . PHE   C  3  87  ? -0.132  -48.244 -62.056  1.00 67.61  ? 87   PHE   C CA   1 
ATOM   17491 C  C    . PHE   C  3  87  ? -0.725  -47.180 -61.140  1.00 69.84  ? 87   PHE   C C    1 
ATOM   17492 O  O    . PHE   C  3  87  ? -0.169  -46.088 -60.990  1.00 72.28  ? 87   PHE   C O    1 
ATOM   17493 C  CB   . PHE   C  3  87  ? 0.736   -49.191 -61.218  1.00 66.86  ? 87   PHE   C CB   1 
ATOM   17494 C  CG   . PHE   C  3  87  ? 1.307   -50.347 -61.987  1.00 66.15  ? 87   PHE   C CG   1 
ATOM   17495 C  CD1  . PHE   C  3  87  ? 0.598   -51.530 -62.115  1.00 66.59  ? 87   PHE   C CD1  1 
ATOM   17496 C  CD2  . PHE   C  3  87  ? 2.564   -50.261 -62.561  1.00 67.05  ? 87   PHE   C CD2  1 
ATOM   17497 C  CE1  . PHE   C  3  87  ? 1.127   -52.600 -62.812  1.00 67.67  ? 87   PHE   C CE1  1 
ATOM   17498 C  CE2  . PHE   C  3  87  ? 3.099   -51.327 -63.259  1.00 69.06  ? 87   PHE   C CE2  1 
ATOM   17499 C  CZ   . PHE   C  3  87  ? 2.379   -52.498 -63.385  1.00 69.39  ? 87   PHE   C CZ   1 
ATOM   17500 H  H    . PHE   C  3  87  ? 1.355   -47.236 -62.832  1.00 80.89  ? 87   PHE   C H    1 
ATOM   17501 H  HA   . PHE   C  3  87  ? -0.853  -48.758 -62.453  1.00 81.17  ? 87   PHE   C HA   1 
ATOM   17502 H  HB2  . PHE   C  3  87  ? 1.478   -48.686 -60.851  1.00 80.27  ? 87   PHE   C HB2  1 
ATOM   17503 H  HB3  . PHE   C  3  87  ? 0.194   -49.554 -60.500  1.00 80.27  ? 87   PHE   C HB3  1 
ATOM   17504 H  HD1  . PHE   C  3  87  ? -0.243  -51.606 -61.727  1.00 79.94  ? 87   PHE   C HD1  1 
ATOM   17505 H  HD2  . PHE   C  3  87  ? 3.055   -49.475 -62.476  1.00 80.50  ? 87   PHE   C HD2  1 
ATOM   17506 H  HE1  . PHE   C  3  87  ? 0.640   -53.388 -62.896  1.00 81.24  ? 87   PHE   C HE1  1 
ATOM   17507 H  HE2  . PHE   C  3  87  ? 3.942   -51.255 -63.645  1.00 82.91  ? 87   PHE   C HE2  1 
ATOM   17508 H  HZ   . PHE   C  3  87  ? 2.737   -53.217 -63.854  1.00 83.31  ? 87   PHE   C HZ   1 
ATOM   17509 N  N    . CYS   C  3  88  ? -1.855  -47.515 -60.522  1.00 69.49  ? 88   CYS   C N    1 
ATOM   17510 C  CA   . CYS   C  3  88  ? -2.489  -46.675 -59.516  1.00 69.97  ? 88   CYS   C CA   1 
ATOM   17511 C  C    . CYS   C  3  88  ? -2.481  -47.410 -58.182  1.00 72.75  ? 88   CYS   C C    1 
ATOM   17512 O  O    . CYS   C  3  88  ? -2.663  -48.631 -58.139  1.00 74.91  ? 88   CYS   C O    1 
ATOM   17513 C  CB   . CYS   C  3  88  ? -3.923  -46.313 -59.914  1.00 69.44  ? 88   CYS   C CB   1 
ATOM   17514 S  SG   . CYS   C  3  88  ? -5.101  -47.685 -59.919  1.00 71.68  ? 88   CYS   C SG   1 
ATOM   17515 H  H    . CYS   C  3  88  ? -2.283  -48.244 -60.675  1.00 83.43  ? 88   CYS   C H    1 
ATOM   17516 H  HA   . CYS   C  3  88  ? -1.995  -45.846 -59.415  1.00 84.00  ? 88   CYS   C HA   1 
ATOM   17517 H  HB2  . CYS   C  3  88  ? -4.255  -45.650 -59.288  1.00 83.36  ? 88   CYS   C HB2  1 
ATOM   17518 H  HB3  . CYS   C  3  88  ? -3.906  -45.943 -60.811  1.00 83.36  ? 88   CYS   C HB3  1 
ATOM   17519 N  N    . GLN   C  3  89  ? -2.271  -46.670 -57.093  1.00 73.06  ? 89   GLN   C N    1 
ATOM   17520 C  CA   . GLN   C  3  89  ? -2.088  -47.280 -55.783  1.00 69.71  ? 89   GLN   C CA   1 
ATOM   17521 C  C    . GLN   C  3  89  ? -2.799  -46.477 -54.707  1.00 64.55  ? 89   GLN   C C    1 
ATOM   17522 O  O    . GLN   C  3  89  ? -2.574  -45.271 -54.578  1.00 64.01  ? 89   GLN   C O    1 
ATOM   17523 C  CB   . GLN   C  3  89  ? -0.599  -47.390 -55.433  1.00 70.88  ? 89   GLN   C CB   1 
ATOM   17524 C  CG   . GLN   C  3  89  ? -0.338  -48.006 -54.064  1.00 71.64  ? 89   GLN   C CG   1 
ATOM   17525 C  CD   . GLN   C  3  89  ? 0.118   -46.990 -53.031  1.00 67.06  ? 89   GLN   C CD   1 
ATOM   17526 O  OE1  . GLN   C  3  89  ? 0.758   -45.991 -53.361  1.00 61.96  ? 89   GLN   C OE1  1 
ATOM   17527 N  NE2  . GLN   C  3  89  ? -0.212  -47.244 -51.769  1.00 64.13  ? 89   GLN   C NE2  1 
ATOM   17528 H  H    . GLN   C  3  89  ? -2.230  -45.811 -57.091  1.00 87.71  ? 89   GLN   C H    1 
ATOM   17529 H  HA   . GLN   C  3  89  ? -2.487  -48.164 -55.801  1.00 83.69  ? 89   GLN   C HA   1 
ATOM   17530 H  HB2  . GLN   C  3  89  ? -0.162  -47.946 -56.097  1.00 85.09  ? 89   GLN   C HB2  1 
ATOM   17531 H  HB3  . GLN   C  3  89  ? -0.211  -46.501 -55.437  1.00 85.09  ? 89   GLN   C HB3  1 
ATOM   17532 H  HG2  . GLN   C  3  89  ? -1.156  -48.414 -53.742  1.00 86.01  ? 89   GLN   C HG2  1 
ATOM   17533 H  HG3  . GLN   C  3  89  ? 0.357   -48.677 -54.149  1.00 86.01  ? 89   GLN   C HG3  1 
ATOM   17534 H  HE21 . GLN   C  3  89  ? -0.659  -47.953 -51.576  1.00 76.99  ? 89   GLN   C HE21 1 
ATOM   17535 H  HE22 . GLN   C  3  89  ? 0.022   -46.700 -51.146  1.00 76.99  ? 89   GLN   C HE22 1 
ATOM   17536 N  N    . GLN   C  3  90  ? -3.634  -47.156 -53.922  1.00 63.22  ? 90   GLN   C N    1 
ATOM   17537 C  CA   . GLN   C  3  90  ? -4.300  -46.537 -52.785  1.00 63.68  ? 90   GLN   C CA   1 
ATOM   17538 C  C    . GLN   C  3  90  ? -3.408  -46.623 -51.554  1.00 62.52  ? 90   GLN   C C    1 
ATOM   17539 O  O    . GLN   C  3  90  ? -2.766  -47.648 -51.305  1.00 60.59  ? 90   GLN   C O    1 
ATOM   17540 C  CB   . GLN   C  3  90  ? -5.647  -47.210 -52.505  1.00 66.16  ? 90   GLN   C CB   1 
ATOM   17541 C  CG   . GLN   C  3  90  ? -5.554  -48.638 -51.970  1.00 67.99  ? 90   GLN   C CG   1 
ATOM   17542 C  CD   . GLN   C  3  90  ? -5.546  -48.707 -50.451  1.00 69.84  ? 90   GLN   C CD   1 
ATOM   17543 O  OE1  . GLN   C  3  90  ? -5.840  -47.725 -49.768  1.00 68.62  ? 90   GLN   C OE1  1 
ATOM   17544 N  NE2  . GLN   C  3  90  ? -5.210  -49.876 -49.917  1.00 72.74  ? 90   GLN   C NE2  1 
ATOM   17545 H  H    . GLN   C  3  90  ? -3.830  -47.986 -54.031  1.00 75.90  ? 90   GLN   C H    1 
ATOM   17546 H  HA   . GLN   C  3  90  ? -4.471  -45.603 -52.981  1.00 76.46  ? 90   GLN   C HA   1 
ATOM   17547 H  HB2  . GLN   C  3  90  ? -6.123  -46.682 -51.846  1.00 79.43  ? 90   GLN   C HB2  1 
ATOM   17548 H  HB3  . GLN   C  3  90  ? -6.152  -47.242 -53.333  1.00 79.43  ? 90   GLN   C HB3  1 
ATOM   17549 H  HG2  . GLN   C  3  90  ? -6.319  -49.143 -52.287  1.00 81.62  ? 90   GLN   C HG2  1 
ATOM   17550 H  HG3  . GLN   C  3  90  ? -4.733  -49.042 -52.292  1.00 81.62  ? 90   GLN   C HG3  1 
ATOM   17551 H  HE21 . GLN   C  3  90  ? -5.013  -50.541 -50.425  1.00 87.33  ? 90   GLN   C HE21 1 
ATOM   17552 H  HE22 . GLN   C  3  90  ? -5.190  -49.968 -49.062  1.00 87.33  ? 90   GLN   C HE22 1 
ATOM   17553 N  N    . GLY   C  3  91  ? -3.369  -45.534 -50.790  1.00 61.83  ? 91   GLY   C N    1 
ATOM   17554 C  CA   . GLY   C  3  91  ? -2.588  -45.483 -49.572  1.00 59.43  ? 91   GLY   C CA   1 
ATOM   17555 C  C    . GLY   C  3  91  ? -3.430  -45.087 -48.378  1.00 64.18  ? 91   GLY   C C    1 
ATOM   17556 O  O    . GLY   C  3  91  ? -2.906  -44.632 -47.357  1.00 65.26  ? 91   GLY   C O    1 
ATOM   17557 H  H    . GLY   C  3  91  ? -3.794  -44.806 -50.963  1.00 74.24  ? 91   GLY   C H    1 
ATOM   17558 H  HA2  . GLY   C  3  91  ? -2.201  -46.356 -49.400  1.00 71.36  ? 91   GLY   C HA2  1 
ATOM   17559 H  HA3  . GLY   C  3  91  ? -1.874  -44.835 -49.673  1.00 71.36  ? 91   GLY   C HA3  1 
ATOM   17560 N  N    . ASN   C  3  92  ? -4.747  -45.262 -48.498  1.00 67.25  ? 92   ASN   C N    1 
ATOM   17561 C  CA   . ASN   C  3  92  ? -5.653  -44.881 -47.423  1.00 68.01  ? 92   ASN   C CA   1 
ATOM   17562 C  C    . ASN   C  3  92  ? -5.678  -45.909 -46.302  1.00 67.59  ? 92   ASN   C C    1 
ATOM   17563 O  O    . ASN   C  3  92  ? -5.987  -45.563 -45.156  1.00 67.92  ? 92   ASN   C O    1 
ATOM   17564 C  CB   . ASN   C  3  92  ? -7.067  -44.690 -47.975  1.00 68.54  ? 92   ASN   C CB   1 
ATOM   17565 C  CG   . ASN   C  3  92  ? -8.022  -44.122 -46.945  1.00 72.20  ? 92   ASN   C CG   1 
ATOM   17566 O  OD1  . ASN   C  3  92  ? -7.660  -43.241 -46.165  1.00 75.46  ? 92   ASN   C OD1  1 
ATOM   17567 N  ND2  . ASN   C  3  92  ? -9.247  -44.633 -46.930  1.00 74.52  ? 92   ASN   C ND2  1 
ATOM   17568 H  H    . ASN   C  3  92  ? -5.136  -45.597 -49.188  1.00 80.73  ? 92   ASN   C H    1 
ATOM   17569 H  HA   . ASN   C  3  92  ? -5.353  -44.036 -47.052  1.00 81.65  ? 92   ASN   C HA   1 
ATOM   17570 H  HB2  . ASN   C  3  92  ? -7.034  -44.075 -48.725  1.00 82.28  ? 92   ASN   C HB2  1 
ATOM   17571 H  HB3  . ASN   C  3  92  ? -7.412  -45.549 -48.264  1.00 82.28  ? 92   ASN   C HB3  1 
ATOM   17572 H  HD21 . ASN   C  3  92  ? -9.827  -44.344 -46.363  1.00 89.46  ? 92   ASN   C HD21 1 
ATOM   17573 H  HD22 . ASN   C  3  92  ? -9.462  -45.252 -47.486  1.00 89.46  ? 92   ASN   C HD22 1 
ATOM   17574 N  N    . THR   C  3  93  ? -5.356  -47.165 -46.604  1.00 66.46  ? 93   THR   C N    1 
ATOM   17575 C  CA   . THR   C  3  93  ? -5.461  -48.231 -45.620  1.00 67.85  ? 93   THR   C CA   1 
ATOM   17576 C  C    . THR   C  3  93  ? -4.516  -49.360 -46.001  1.00 65.62  ? 93   THR   C C    1 
ATOM   17577 O  O    . THR   C  3  93  ? -4.271  -49.609 -47.184  1.00 62.91  ? 93   THR   C O    1 
ATOM   17578 C  CB   . THR   C  3  93  ? -6.902  -48.751 -45.522  1.00 73.94  ? 93   THR   C CB   1 
ATOM   17579 O  OG1  . THR   C  3  93  ? -6.956  -49.869 -44.629  1.00 80.05  ? 93   THR   C OG1  1 
ATOM   17580 C  CG2  . THR   C  3  93  ? -7.420  -49.169 -46.896  1.00 72.72  ? 93   THR   C CG2  1 
ATOM   17581 H  H    . THR   C  3  93  ? -5.073  -47.423 -47.374  1.00 79.78  ? 93   THR   C H    1 
ATOM   17582 H  HA   . THR   C  3  93  ? -5.191  -47.897 -44.750  1.00 81.45  ? 93   THR   C HA   1 
ATOM   17583 H  HB   . THR   C  3  93  ? -7.475  -48.045 -45.185  1.00 88.77  ? 93   THR   C HB   1 
ATOM   17584 H  HG1  . THR   C  3  93  ? -7.739  -50.170 -44.592  1.00 96.10  ? 93   THR   C HG1  1 
ATOM   17585 H  HG21 . THR   C  3  93  ? -8.332  -49.489 -46.823  1.00 87.30  ? 93   THR   C HG21 1 
ATOM   17586 H  HG22 . THR   C  3  93  ? -7.399  -48.413 -47.503  1.00 87.30  ? 93   THR   C HG22 1 
ATOM   17587 H  HG23 . THR   C  3  93  ? -6.865  -49.878 -47.258  1.00 87.30  ? 93   THR   C HG23 1 
ATOM   17588 N  N    . PHE   C  3  94  ? -3.984  -50.036 -44.979  1.00 66.16  ? 94   PHE   C N    1 
ATOM   17589 C  CA   . PHE   C  3  94  ? -3.131  -51.191 -45.212  1.00 66.34  ? 94   PHE   C CA   1 
ATOM   17590 C  C    . PHE   C  3  94  ? -3.980  -52.445 -45.420  1.00 65.65  ? 94   PHE   C C    1 
ATOM   17591 O  O    . PHE   C  3  94  ? -5.045  -52.589 -44.816  1.00 67.08  ? 94   PHE   C O    1 
ATOM   17592 C  CB   . PHE   C  3  94  ? -2.187  -51.408 -44.032  1.00 67.54  ? 94   PHE   C CB   1 
ATOM   17593 C  CG   . PHE   C  3  94  ? -1.086  -50.388 -43.927  1.00 63.12  ? 94   PHE   C CG   1 
ATOM   17594 C  CD1  . PHE   C  3  94  ? -0.357  -50.004 -45.042  1.00 61.25  ? 94   PHE   C CD1  1 
ATOM   17595 C  CD2  . PHE   C  3  94  ? -0.775  -49.818 -42.704  1.00 63.39  ? 94   PHE   C CD2  1 
ATOM   17596 C  CE1  . PHE   C  3  94  ? 0.656   -49.069 -44.937  1.00 61.26  ? 94   PHE   C CE1  1 
ATOM   17597 C  CE2  . PHE   C  3  94  ? 0.235   -48.883 -42.593  1.00 63.78  ? 94   PHE   C CE2  1 
ATOM   17598 C  CZ   . PHE   C  3  94  ? 0.952   -48.508 -43.711  1.00 62.23  ? 94   PHE   C CZ   1 
ATOM   17599 H  H    . PHE   C  3  94  ? -4.104  -49.844 -44.150  1.00 79.43  ? 94   PHE   C H    1 
ATOM   17600 H  HA   . PHE   C  3  94  ? -2.594  -51.041 -46.006  1.00 79.65  ? 94   PHE   C HA   1 
ATOM   17601 H  HB2  . PHE   C  3  94  ? -2.702  -51.371 -43.212  1.00 81.08  ? 94   PHE   C HB2  1 
ATOM   17602 H  HB3  . PHE   C  3  94  ? -1.772  -52.280 -44.124  1.00 81.08  ? 94   PHE   C HB3  1 
ATOM   17603 H  HD1  . PHE   C  3  94  ? -0.552  -50.380 -45.870  1.00 73.54  ? 94   PHE   C HD1  1 
ATOM   17604 H  HD2  . PHE   C  3  94  ? -1.254  -50.068 -41.946  1.00 76.11  ? 94   PHE   C HD2  1 
ATOM   17605 H  HE1  . PHE   C  3  94  ? 1.138   -48.819 -45.692  1.00 73.54  ? 94   PHE   C HE1  1 
ATOM   17606 H  HE2  . PHE   C  3  94  ? 0.433   -48.507 -41.766  1.00 76.58  ? 94   PHE   C HE2  1 
ATOM   17607 H  HZ   . PHE   C  3  94  ? 1.632   -47.878 -43.639  1.00 74.72  ? 94   PHE   C HZ   1 
ATOM   17608 N  N    . PRO   C  3  95  ? -3.525  -53.378 -46.272  1.00 64.78  ? 95   PRO   C N    1 
ATOM   17609 C  CA   . PRO   C  3  95  ? -2.286  -53.276 -47.050  1.00 63.96  ? 95   PRO   C CA   1 
ATOM   17610 C  C    . PRO   C  3  95  ? -2.430  -52.344 -48.246  1.00 62.69  ? 95   PRO   C C    1 
ATOM   17611 O  O    . PRO   C  3  95  ? -3.520  -52.232 -48.806  1.00 62.39  ? 95   PRO   C O    1 
ATOM   17612 C  CB   . PRO   C  3  95  ? -2.044  -54.715 -47.507  1.00 68.88  ? 95   PRO   C CB   1 
ATOM   17613 C  CG   . PRO   C  3  95  ? -3.406  -55.298 -47.612  1.00 70.69  ? 95   PRO   C CG   1 
ATOM   17614 C  CD   . PRO   C  3  95  ? -4.220  -54.656 -46.517  1.00 67.69  ? 95   PRO   C CD   1 
ATOM   17615 H  HA   . PRO   C  3  95  ? -1.547  -52.981 -46.495  1.00 76.79  ? 95   PRO   C HA   1 
ATOM   17616 H  HB2  . PRO   C  3  95  ? -1.594  -54.720 -48.366  1.00 82.69  ? 95   PRO   C HB2  1 
ATOM   17617 H  HB3  . PRO   C  3  95  ? -1.510  -55.188 -46.850  1.00 82.69  ? 95   PRO   C HB3  1 
ATOM   17618 H  HG2  . PRO   C  3  95  ? -3.782  -55.095 -48.483  1.00 84.87  ? 95   PRO   C HG2  1 
ATOM   17619 H  HG3  . PRO   C  3  95  ? -3.360  -56.259 -47.487  1.00 84.87  ? 95   PRO   C HG3  1 
ATOM   17620 H  HD2  . PRO   C  3  95  ? -5.131  -54.501 -46.811  1.00 81.26  ? 95   PRO   C HD2  1 
ATOM   17621 H  HD3  . PRO   C  3  95  ? -4.218  -55.207 -45.719  1.00 81.26  ? 95   PRO   C HD3  1 
ATOM   17622 N  N    . TYR   C  3  96  ? -1.347  -51.669 -48.619  1.00 63.17  ? 96   TYR   C N    1 
ATOM   17623 C  CA   . TYR   C  3  96  ? -1.347  -50.905 -49.857  1.00 61.48  ? 96   TYR   C CA   1 
ATOM   17624 C  C    . TYR   C  3  96  ? -1.590  -51.850 -51.028  1.00 64.48  ? 96   TYR   C C    1 
ATOM   17625 O  O    . TYR   C  3  96  ? -0.988  -52.926 -51.107  1.00 66.50  ? 96   TYR   C O    1 
ATOM   17626 C  CB   . TYR   C  3  96  ? -0.021  -50.162 -50.029  1.00 58.37  ? 96   TYR   C CB   1 
ATOM   17627 C  CG   . TYR   C  3  96  ? 0.173   -48.974 -49.101  1.00 60.54  ? 96   TYR   C CG   1 
ATOM   17628 C  CD1  . TYR   C  3  96  ? -0.864  -48.502 -48.305  1.00 62.73  ? 96   TYR   C CD1  1 
ATOM   17629 C  CD2  . TYR   C  3  96  ? 1.397   -48.318 -49.031  1.00 60.62  ? 96   TYR   C CD2  1 
ATOM   17630 C  CE1  . TYR   C  3  96  ? -0.687  -47.418 -47.464  1.00 61.09  ? 96   TYR   C CE1  1 
ATOM   17631 C  CE2  . TYR   C  3  96  ? 1.582   -47.232 -48.192  1.00 59.12  ? 96   TYR   C CE2  1 
ATOM   17632 C  CZ   . TYR   C  3  96  ? 0.535   -46.787 -47.413  1.00 59.55  ? 96   TYR   C CZ   1 
ATOM   17633 O  OH   . TYR   C  3  96  ? 0.709   -45.708 -46.576  1.00 59.93  ? 96   TYR   C OH   1 
ATOM   17634 H  H    . TYR   C  3  96  ? -0.609  -51.638 -48.177  1.00 75.85  ? 96   TYR   C H    1 
ATOM   17635 H  HA   . TYR   C  3  96  ? -2.051  -50.238 -49.836  1.00 73.82  ? 96   TYR   C HA   1 
ATOM   17636 H  HB2  . TYR   C  3  96  ? 0.704   -50.785 -49.861  1.00 70.07  ? 96   TYR   C HB2  1 
ATOM   17637 H  HB3  . TYR   C  3  96  ? 0.030   -49.832 -50.940  1.00 70.07  ? 96   TYR   C HB3  1 
ATOM   17638 H  HD1  . TYR   C  3  96  ? -1.693  -48.923 -48.338  1.00 75.32  ? 96   TYR   C HD1  1 
ATOM   17639 H  HD2  . TYR   C  3  96  ? 2.104   -48.614 -49.557  1.00 72.78  ? 96   TYR   C HD2  1 
ATOM   17640 H  HE1  . TYR   C  3  96  ? -1.391  -47.118 -46.936  1.00 73.34  ? 96   TYR   C HE1  1 
ATOM   17641 H  HE2  . TYR   C  3  96  ? 2.407   -46.805 -48.155  1.00 70.98  ? 96   TYR   C HE2  1 
ATOM   17642 H  HH   . TYR   C  3  96  ? 1.457   -45.354 -46.715  1.00 71.96  ? 96   TYR   C HH   1 
ATOM   17643 N  N    . THR   C  3  97  ? -2.487  -51.458 -51.927  1.00 62.19  ? 97   THR   C N    1 
ATOM   17644 C  CA   . THR   C  3  97  ? -2.862  -52.283 -53.065  1.00 64.13  ? 97   THR   C CA   1 
ATOM   17645 C  C    . THR   C  3  97  ? -2.736  -51.469 -54.343  1.00 65.42  ? 97   THR   C C    1 
ATOM   17646 O  O    . THR   C  3  97  ? -3.018  -50.267 -54.355  1.00 65.10  ? 97   THR   C O    1 
ATOM   17647 C  CB   . THR   C  3  97  ? -4.295  -52.818 -52.926  1.00 65.23  ? 97   THR   C CB   1 
ATOM   17648 O  OG1  . THR   C  3  97  ? -5.215  -51.723 -52.841  1.00 65.23  ? 97   THR   C OG1  1 
ATOM   17649 C  CG2  . THR   C  3  97  ? -4.423  -53.687 -51.682  1.00 68.46  ? 97   THR   C CG2  1 
ATOM   17650 H  H    . THR   C  3  97  ? -2.898  -50.703 -51.897  1.00 74.67  ? 97   THR   C H    1 
ATOM   17651 H  HA   . THR   C  3  97  ? -2.261  -53.042 -53.125  1.00 76.99  ? 97   THR   C HA   1 
ATOM   17652 H  HB   . THR   C  3  97  ? -4.513  -53.360 -53.700  1.00 78.32  ? 97   THR   C HB   1 
ATOM   17653 H  HG1  . THR   C  3  97  ? -6.002  -52.012 -52.794  1.00 78.31  ? 97   THR   C HG1  1 
ATOM   17654 H  HG21 . THR   C  3  97  ? -5.323  -54.044 -51.618  1.00 82.19  ? 97   THR   C HG21 1 
ATOM   17655 H  HG22 . THR   C  3  97  ? -3.794  -54.423 -51.726  1.00 82.19  ? 97   THR   C HG22 1 
ATOM   17656 H  HG23 . THR   C  3  97  ? -4.237  -53.160 -50.889  1.00 82.19  ? 97   THR   C HG23 1 
ATOM   17657 N  N    . PHE   C  3  98  ? -2.311  -52.132 -55.414  1.00 66.00  ? 98   PHE   C N    1 
ATOM   17658 C  CA   . PHE   C  3  98  ? -2.119  -51.503 -56.710  1.00 64.64  ? 98   PHE   C CA   1 
ATOM   17659 C  C    . PHE   C  3  98  ? -3.201  -51.956 -57.681  1.00 68.55  ? 98   PHE   C C    1 
ATOM   17660 O  O    . PHE   C  3  98  ? -3.900  -52.947 -57.453  1.00 74.78  ? 98   PHE   C O    1 
ATOM   17661 C  CB   . PHE   C  3  98  ? -0.745  -51.849 -57.297  1.00 63.15  ? 98   PHE   C CB   1 
ATOM   17662 C  CG   . PHE   C  3  98  ? 0.416   -51.365 -56.474  1.00 57.19  ? 98   PHE   C CG   1 
ATOM   17663 C  CD1  . PHE   C  3  98  ? 0.838   -52.073 -55.361  1.00 57.58  ? 98   PHE   C CD1  1 
ATOM   17664 C  CD2  . PHE   C  3  98  ? 1.099   -50.214 -56.828  1.00 55.54  ? 98   PHE   C CD2  1 
ATOM   17665 C  CE1  . PHE   C  3  98  ? 1.912   -51.634 -54.608  1.00 57.04  ? 98   PHE   C CE1  1 
ATOM   17666 C  CE2  . PHE   C  3  98  ? 2.173   -49.769 -56.079  1.00 54.99  ? 98   PHE   C CE2  1 
ATOM   17667 C  CZ   . PHE   C  3  98  ? 2.581   -50.481 -54.969  1.00 55.33  ? 98   PHE   C CZ   1 
ATOM   17668 H  H    . PHE   C  3  98  ? -2.123  -52.971 -55.411  1.00 79.24  ? 98   PHE   C H    1 
ATOM   17669 H  HA   . PHE   C  3  98  ? -2.177  -50.541 -56.601  1.00 77.61  ? 98   PHE   C HA   1 
ATOM   17670 H  HB2  . PHE   C  3  98  ? -0.672  -52.813 -57.370  1.00 75.82  ? 98   PHE   C HB2  1 
ATOM   17671 H  HB3  . PHE   C  3  98  ? -0.672  -51.443 -58.175  1.00 75.82  ? 98   PHE   C HB3  1 
ATOM   17672 H  HD1  . PHE   C  3  98  ? 0.394   -52.853 -55.117  1.00 69.14  ? 98   PHE   C HD1  1 
ATOM   17673 H  HD2  . PHE   C  3  98  ? 0.833   -49.734 -57.579  1.00 66.68  ? 98   PHE   C HD2  1 
ATOM   17674 H  HE1  . PHE   C  3  98  ? 2.184   -52.115 -53.859  1.00 68.48  ? 98   PHE   C HE1  1 
ATOM   17675 H  HE2  . PHE   C  3  98  ? 2.621   -48.992 -56.324  1.00 66.03  ? 98   PHE   C HE2  1 
ATOM   17676 H  HZ   . PHE   C  3  98  ? 3.304   -50.185 -54.465  1.00 66.43  ? 98   PHE   C HZ   1 
ATOM   17677 N  N    . GLY   C  3  99  ? -3.332  -51.204 -58.777  1.00 68.79  ? 99   GLY   C N    1 
ATOM   17678 C  CA   . GLY   C  3  99  ? -4.130  -51.646 -59.899  1.00 67.94  ? 99   GLY   C CA   1 
ATOM   17679 C  C    . GLY   C  3  99  ? -3.335  -52.545 -60.830  1.00 71.49  ? 99   GLY   C C    1 
ATOM   17680 O  O    . GLY   C  3  99  ? -2.117  -52.678 -60.719  1.00 72.24  ? 99   GLY   C O    1 
ATOM   17681 H  H    . GLY   C  3  99  ? -2.964  -50.435 -58.887  1.00 82.59  ? 99   GLY   C H    1 
ATOM   17682 H  HA2  . GLY   C  3  99  ? -4.900  -52.140 -59.575  1.00 81.56  ? 99   GLY   C HA2  1 
ATOM   17683 H  HA3  . GLY   C  3  99  ? -4.438  -50.876 -60.401  1.00 81.56  ? 99   GLY   C HA3  1 
ATOM   17684 N  N    . GLY   C  3  100 ? -4.050  -53.170 -61.768  1.00 70.11  ? 100  GLY   C N    1 
ATOM   17685 C  CA   . GLY   C  3  100 ? -3.413  -54.134 -62.649  1.00 72.06  ? 100  GLY   C CA   1 
ATOM   17686 C  C    . GLY   C  3  100 ? -2.363  -53.526 -63.558  1.00 70.66  ? 100  GLY   C C    1 
ATOM   17687 O  O    . GLY   C  3  100 ? -1.407  -54.202 -63.945  1.00 70.06  ? 100  GLY   C O    1 
ATOM   17688 H  H    . GLY   C  3  100 ? -4.890  -53.053 -61.909  1.00 84.16  ? 100  GLY   C H    1 
ATOM   17689 H  HA2  . GLY   C  3  100 ? -2.985  -54.819 -62.112  1.00 86.50  ? 100  GLY   C HA2  1 
ATOM   17690 H  HA3  . GLY   C  3  100 ? -4.090  -54.548 -63.207  1.00 86.50  ? 100  GLY   C HA3  1 
ATOM   17691 N  N    . GLY   C  3  101 ? -2.522  -52.262 -63.912  1.00 67.61  ? 101  GLY   C N    1 
ATOM   17692 C  CA   . GLY   C  3  101 ? -1.577  -51.584 -64.772  1.00 69.48  ? 101  GLY   C CA   1 
ATOM   17693 C  C    . GLY   C  3  101 ? -2.171  -51.275 -66.137  1.00 73.29  ? 101  GLY   C C    1 
ATOM   17694 O  O    . GLY   C  3  101 ? -2.978  -52.038 -66.685  1.00 78.47  ? 101  GLY   C O    1 
ATOM   17695 H  H    . GLY   C  3  101 ? -3.181  -51.769 -63.662  1.00 81.17  ? 101  GLY   C H    1 
ATOM   17696 H  HA2  . GLY   C  3  101 ? -1.305  -50.749 -64.359  1.00 83.41  ? 101  GLY   C HA2  1 
ATOM   17697 H  HA3  . GLY   C  3  101 ? -0.794  -52.143 -64.897  1.00 83.41  ? 101  GLY   C HA3  1 
ATOM   17698 N  N    . THR   C  3  102 ? -1.765  -50.134 -66.695  1.00 75.80  ? 102  THR   C N    1 
ATOM   17699 C  CA   . THR   C  3  102 ? -2.165  -49.718 -68.034  1.00 77.64  ? 102  THR   C CA   1 
ATOM   17700 C  C    . THR   C  3  102 ? -0.908  -49.423 -68.838  1.00 77.89  ? 102  THR   C C    1 
ATOM   17701 O  O    . THR   C  3  102 ? -0.081  -48.603 -68.424  1.00 74.11  ? 102  THR   C O    1 
ATOM   17702 C  CB   . THR   C  3  102 ? -3.078  -48.489 -67.996  1.00 73.86  ? 102  THR   C CB   1 
ATOM   17703 O  OG1  . THR   C  3  102 ? -4.315  -48.830 -67.357  1.00 76.67  ? 102  THR   C OG1  1 
ATOM   17704 C  CG2  . THR   C  3  102 ? -3.363  -47.984 -69.408  1.00 73.67  ? 102  THR   C CG2  1 
ATOM   17705 H  H    . THR   C  3  102 ? -1.245  -49.571 -66.304  1.00 90.99  ? 102  THR   C H    1 
ATOM   17706 H  HA   . THR   C  3  102 ? -2.650  -50.439 -68.464  1.00 93.20  ? 102  THR   C HA   1 
ATOM   17707 H  HB   . THR   C  3  102 ? -2.641  -47.779 -67.501  1.00 88.67  ? 102  THR   C HB   1 
ATOM   17708 H  HG1  . THR   C  3  102 ? -4.738  -49.383 -67.827  1.00 92.04  ? 102  THR   C HG1  1 
ATOM   17709 H  HG21 . THR   C  3  102 ? -4.013  -47.265 -69.378  1.00 88.44  ? 102  THR   C HG21 1 
ATOM   17710 H  HG22 . THR   C  3  102 ? -2.546  -47.655 -69.814  1.00 88.44  ? 102  THR   C HG22 1 
ATOM   17711 H  HG23 . THR   C  3  102 ? -3.717  -48.705 -69.952  1.00 88.44  ? 102  THR   C HG23 1 
ATOM   17712 N  N    . LYS   C  3  103 ? -0.776  -50.079 -69.985  1.00 80.85  ? 103  LYS   C N    1 
ATOM   17713 C  CA   . LYS   C  3  103 ? 0.416   -49.998 -70.818  1.00 81.84  ? 103  LYS   C CA   1 
ATOM   17714 C  C    . LYS   C  3  103 ? 0.143   -49.041 -71.972  1.00 80.85  ? 103  LYS   C C    1 
ATOM   17715 O  O    . LYS   C  3  103 ? -0.810  -49.238 -72.733  1.00 82.65  ? 103  LYS   C O    1 
ATOM   17716 C  CB   . LYS   C  3  103 ? 0.796   -51.388 -71.332  1.00 88.52  ? 103  LYS   C CB   1 
ATOM   17717 C  CG   . LYS   C  3  103 ? 0.701   -52.474 -70.257  1.00 94.54  ? 103  LYS   C CG   1 
ATOM   17718 C  CD   . LYS   C  3  103 ? 0.641   -53.880 -70.835  1.00 98.94  ? 103  LYS   C CD   1 
ATOM   17719 C  CE   . LYS   C  3  103 ? -0.297  -54.772 -70.021  1.00 105.10 ? 103  LYS   C CE   1 
ATOM   17720 N  NZ   . LYS   C  3  103 ? -0.187  -54.565 -68.546  1.00 102.49 ? 103  LYS   C NZ   1 
ATOM   17721 H  H    . LYS   C  3  103 ? -1.383  -50.594 -70.311  1.00 97.06  ? 103  LYS   C H    1 
ATOM   17722 H  HA   . LYS   C  3  103 ? 1.162   -49.647 -70.306  1.00 98.24  ? 103  LYS   C HA   1 
ATOM   17723 H  HB2  . LYS   C  3  103 ? 0.197   -51.630 -72.055  1.00 106.27 ? 103  LYS   C HB2  1 
ATOM   17724 H  HB3  . LYS   C  3  103 ? 1.711   -51.365 -71.654  1.00 106.27 ? 103  LYS   C HB3  1 
ATOM   17725 H  HG2  . LYS   C  3  103 ? 1.482   -52.420 -69.684  1.00 113.49 ? 103  LYS   C HG2  1 
ATOM   17726 H  HG3  . LYS   C  3  103 ? -0.103  -52.331 -69.734  1.00 113.49 ? 103  LYS   C HG3  1 
ATOM   17727 H  HD2  . LYS   C  3  103 ? 0.311   -53.840 -71.746  1.00 118.77 ? 103  LYS   C HD2  1 
ATOM   17728 H  HD3  . LYS   C  3  103 ? 1.527   -54.273 -70.819  1.00 118.77 ? 103  LYS   C HD3  1 
ATOM   17729 H  HE2  . LYS   C  3  103 ? -1.213  -54.583 -70.280  1.00 126.16 ? 103  LYS   C HE2  1 
ATOM   17730 H  HE3  . LYS   C  3  103 ? -0.086  -55.701 -70.206  1.00 126.16 ? 103  LYS   C HE3  1 
ATOM   17731 H  HZ1  . LYS   C  3  103 ? -0.443  -55.300 -68.115  1.00 123.03 ? 103  LYS   C HZ1  1 
ATOM   17732 H  HZ2  . LYS   C  3  103 ? 0.656   -54.380 -68.326  1.00 123.03 ? 103  LYS   C HZ2  1 
ATOM   17733 H  HZ3  . LYS   C  3  103 ? -0.706  -53.887 -68.294  1.00 123.03 ? 103  LYS   C HZ3  1 
ATOM   17734 N  N    . VAL   C  3  104 ? 0.972   -48.008 -72.095  1.00 79.08  ? 104  VAL   C N    1 
ATOM   17735 C  CA   . VAL   C  3  104 ? 0.824   -46.995 -73.134  1.00 78.20  ? 104  VAL   C CA   1 
ATOM   17736 C  C    . VAL   C  3  104 ? 1.871   -47.259 -74.207  1.00 84.16  ? 104  VAL   C C    1 
ATOM   17737 O  O    . VAL   C  3  104 ? 3.077   -47.155 -73.951  1.00 83.15  ? 104  VAL   C O    1 
ATOM   17738 C  CB   . VAL   C  3  104 ? 0.961   -45.576 -72.559  1.00 69.27  ? 104  VAL   C CB   1 
ATOM   17739 C  CG1  . VAL   C  3  104 ? 0.963   -44.541 -73.678  1.00 68.64  ? 104  VAL   C CG1  1 
ATOM   17740 C  CG2  . VAL   C  3  104 ? -0.167  -45.296 -71.575  1.00 65.57  ? 104  VAL   C CG2  1 
ATOM   17741 H  H    . VAL   C  3  104 ? 1.643   -47.870 -71.575  1.00 94.93  ? 104  VAL   C H    1 
ATOM   17742 H  HA   . VAL   C  3  104 ? -0.054  -47.076 -73.538  1.00 93.88  ? 104  VAL   C HA   1 
ATOM   17743 H  HB   . VAL   C  3  104 ? 1.805   -45.508 -72.086  1.00 83.16  ? 104  VAL   C HB   1 
ATOM   17744 H  HG11 . VAL   C  3  104 ? 0.974   -43.653 -73.287  1.00 82.40  ? 104  VAL   C HG11 1 
ATOM   17745 H  HG12 . VAL   C  3  104 ? 1.752   -44.670 -74.227  1.00 82.40  ? 104  VAL   C HG12 1 
ATOM   17746 H  HG13 . VAL   C  3  104 ? 0.164   -44.655 -74.216  1.00 82.40  ? 104  VAL   C HG13 1 
ATOM   17747 H  HG21 . VAL   C  3  104 ? -0.074  -44.392 -71.236  1.00 78.72  ? 104  VAL   C HG21 1 
ATOM   17748 H  HG22 . VAL   C  3  104 ? -1.017  -45.391 -72.034  1.00 78.72  ? 104  VAL   C HG22 1 
ATOM   17749 H  HG23 . VAL   C  3  104 ? -0.114  -45.931 -70.844  1.00 78.72  ? 104  VAL   C HG23 1 
ATOM   17750 N  N    . GLU   C  3  105 ? 1.409   -47.592 -75.409  1.00 91.28  ? 105  GLU   C N    1 
ATOM   17751 C  CA   . GLU   C  3  105 ? 2.276   -47.917 -76.530  1.00 98.65  ? 105  GLU   C CA   1 
ATOM   17752 C  C    . GLU   C  3  105 ? 2.057   -46.921 -77.660  1.00 97.98  ? 105  GLU   C C    1 
ATOM   17753 O  O    . GLU   C  3  105 ? 0.967   -46.362 -77.817  1.00 101.45 ? 105  GLU   C O    1 
ATOM   17754 C  CB   . GLU   C  3  105 ? 2.013   -49.343 -77.033  1.00 108.83 ? 105  GLU   C CB   1 
ATOM   17755 C  CG   . GLU   C  3  105 ? 2.351   -50.426 -76.019  1.00 114.44 ? 105  GLU   C CG   1 
ATOM   17756 C  CD   . GLU   C  3  105 ? 1.970   -51.815 -76.494  1.00 125.70 ? 105  GLU   C CD   1 
ATOM   17757 O  OE1  . GLU   C  3  105 ? 1.292   -51.924 -77.538  1.00 130.72 ? 105  GLU   C OE1  1 
ATOM   17758 O  OE2  . GLU   C  3  105 ? 2.348   -52.798 -75.823  1.00 128.90 ? 105  GLU   C OE2  1 
ATOM   17759 H  H    . GLU   C  3  105 ? 0.573   -47.637 -75.602  1.00 109.58 ? 105  GLU   C H    1 
ATOM   17760 H  HA   . GLU   C  3  105 ? 3.204   -47.858 -76.254  1.00 118.42 ? 105  GLU   C HA   1 
ATOM   17761 H  HB2  . GLU   C  3  105 ? 1.073   -49.427 -77.253  1.00 130.64 ? 105  GLU   C HB2  1 
ATOM   17762 H  HB3  . GLU   C  3  105 ? 2.554   -49.499 -77.823  1.00 130.64 ? 105  GLU   C HB3  1 
ATOM   17763 H  HG2  . GLU   C  3  105 ? 3.306   -50.417 -75.853  1.00 137.36 ? 105  GLU   C HG2  1 
ATOM   17764 H  HG3  . GLU   C  3  105 ? 1.870   -50.249 -75.195  1.00 137.36 ? 105  GLU   C HG3  1 
ATOM   17765 N  N    . MET   C  3  106 ? 3.107   -46.700 -78.445  1.00 95.67  ? 106  MET   C N    1 
ATOM   17766 C  CA   . MET   C  3  106 ? 3.014   -45.796 -79.580  1.00 96.54  ? 106  MET   C CA   1 
ATOM   17767 C  C    . MET   C  3  106 ? 2.083   -46.364 -80.646  1.00 98.99  ? 106  MET   C C    1 
ATOM   17768 O  O    . MET   C  3  106 ? 1.850   -47.573 -80.732  1.00 96.41  ? 106  MET   C O    1 
ATOM   17769 C  CB   . MET   C  3  106 ? 4.397   -45.546 -80.181  1.00 94.85  ? 106  MET   C CB   1 
ATOM   17770 C  CG   . MET   C  3  106 ? 5.106   -44.328 -79.615  1.00 92.88  ? 106  MET   C CG   1 
ATOM   17771 S  SD   . MET   C  3  106 ? 4.299   -42.781 -80.073  1.00 94.43  ? 106  MET   C SD   1 
ATOM   17772 C  CE   . MET   C  3  106 ? 4.618   -42.737 -81.836  1.00 101.98 ? 106  MET   C CE   1 
ATOM   17773 H  H    . MET   C  3  106 ? 3.881   -47.061 -78.341  1.00 114.84 ? 106  MET   C H    1 
ATOM   17774 H  HA   . MET   C  3  106 ? 2.662   -44.945 -79.274  1.00 115.88 ? 106  MET   C HA   1 
ATOM   17775 H  HB2  . MET   C  3  106 ? 4.956   -46.320 -80.008  1.00 113.86 ? 106  MET   C HB2  1 
ATOM   17776 H  HB3  . MET   C  3  106 ? 4.301   -45.414 -81.137  1.00 113.86 ? 106  MET   C HB3  1 
ATOM   17777 H  HG2  . MET   C  3  106 ? 5.114   -44.388 -78.647  1.00 111.50 ? 106  MET   C HG2  1 
ATOM   17778 H  HG3  . MET   C  3  106 ? 6.014   -44.305 -79.954  1.00 111.50 ? 106  MET   C HG3  1 
ATOM   17779 H  HE1  . MET   C  3  106 ? 4.213   -41.939 -82.210  1.00 122.41 ? 106  MET   C HE1  1 
ATOM   17780 H  HE2  . MET   C  3  106 ? 5.577   -42.722 -81.983  1.00 122.41 ? 106  MET   C HE2  1 
ATOM   17781 H  HE3  . MET   C  3  106 ? 4.233   -43.527 -82.246  1.00 122.41 ? 106  MET   C HE3  1 
ATOM   17782 N  N    . ARG   C  3  107 ? 1.545   -45.467 -81.466  1.00 102.52 ? 107  ARG   C N    1 
ATOM   17783 C  CA   . ARG   C  3  107 ? 0.718   -45.847 -82.600  1.00 107.42 ? 107  ARG   C CA   1 
ATOM   17784 C  C    . ARG   C  3  107 ? 1.556   -45.870 -83.871  1.00 106.48 ? 107  ARG   C C    1 
ATOM   17785 O  O    . ARG   C  3  107 ? 2.524   -45.119 -84.016  1.00 105.12 ? 107  ARG   C O    1 
ATOM   17786 C  CB   . ARG   C  3  107 ? -0.462  -44.892 -82.780  1.00 111.04 ? 107  ARG   C CB   1 
ATOM   17787 C  CG   . ARG   C  3  107 ? -1.749  -45.386 -82.147  1.00 110.93 ? 107  ARG   C CG   1 
ATOM   17788 C  CD   . ARG   C  3  107 ? -2.966  -44.897 -82.912  1.00 113.66 ? 107  ARG   C CD   1 
ATOM   17789 N  NE   . ARG   C  3  107 ? -4.208  -45.276 -82.245  1.00 117.43 ? 107  ARG   C NE   1 
ATOM   17790 C  CZ   . ARG   C  3  107 ? -4.865  -44.508 -81.380  1.00 120.41 ? 107  ARG   C CZ   1 
ATOM   17791 N  NH1  . ARG   C  3  107 ? -4.410  -43.301 -81.068  1.00 119.54 ? 107  ARG   C NH1  1 
ATOM   17792 N  NH2  . ARG   C  3  107 ? -5.986  -44.948 -80.826  1.00 122.99 ? 107  ARG   C NH2  1 
ATOM   17793 H  H    . ARG   C  3  107 ? 1.647   -44.617 -81.383  1.00 123.06 ? 107  ARG   C H    1 
ATOM   17794 H  HA   . ARG   C  3  107 ? 0.359   -46.735 -82.446  1.00 128.95 ? 107  ARG   C HA   1 
ATOM   17795 H  HB2  . ARG   C  3  107 ? -0.239  -44.041 -82.372  1.00 133.28 ? 107  ARG   C HB2  1 
ATOM   17796 H  HB3  . ARG   C  3  107 ? -0.625  -44.773 -83.729  1.00 133.28 ? 107  ARG   C HB3  1 
ATOM   17797 H  HG2  . ARG   C  3  107 ? -1.757  -46.356 -82.148  1.00 133.15 ? 107  ARG   C HG2  1 
ATOM   17798 H  HG3  . ARG   C  3  107 ? -1.807  -45.055 -81.237  1.00 133.15 ? 107  ARG   C HG3  1 
ATOM   17799 H  HD2  . ARG   C  3  107 ? -2.937  -43.930 -82.976  1.00 136.43 ? 107  ARG   C HD2  1 
ATOM   17800 H  HD3  . ARG   C  3  107 ? -2.965  -45.288 -83.800  1.00 136.43 ? 107  ARG   C HD3  1 
ATOM   17801 H  HE   . ARG   C  3  107 ? -4.538  -46.050 -82.424  1.00 140.95 ? 107  ARG   C HE   1 
ATOM   17802 H  HH11 . ARG   C  3  107 ? -3.684  -43.010 -81.426  1.00 143.48 ? 107  ARG   C HH11 1 
ATOM   17803 H  HH12 . ARG   C  3  107 ? -4.840  -42.811 -80.508  1.00 143.48 ? 107  ARG   C HH12 1 
ATOM   17804 H  HH21 . ARG   C  3  107 ? -6.287  -45.729 -81.026  1.00 147.63 ? 107  ARG   C HH21 1 
ATOM   17805 H  HH22 . ARG   C  3  107 ? -6.412  -44.454 -80.267  1.00 147.63 ? 107  ARG   C HH22 1 
ATOM   17806 N  N    . ARG   C  3  108 ? 1.165   -46.741 -84.796  1.00 105.96 ? 108  ARG   C N    1 
ATOM   17807 C  CA   . ARG   C  3  108 ? 1.929   -46.948 -86.013  1.00 102.51 ? 108  ARG   C CA   1 
ATOM   17808 C  C    . ARG   C  3  108 ? 0.987   -47.387 -87.121  1.00 103.17 ? 108  ARG   C C    1 
ATOM   17809 O  O    . ARG   C  3  108 ? -0.090  -47.933 -86.868  1.00 104.25 ? 108  ARG   C O    1 
ATOM   17810 C  CB   . ARG   C  3  108 ? 3.025   -47.999 -85.806  1.00 100.65 ? 108  ARG   C CB   1 
ATOM   17811 C  CG   . ARG   C  3  108 ? 4.290   -47.751 -86.601  1.00 101.96 ? 108  ARG   C CG   1 
ATOM   17812 C  CD   . ARG   C  3  108 ? 5.177   -48.983 -86.602  1.00 103.48 ? 108  ARG   C CD   1 
ATOM   17813 N  NE   . ARG   C  3  108 ? 6.124   -48.972 -87.712  1.00 107.31 ? 108  ARG   C NE   1 
ATOM   17814 C  CZ   . ARG   C  3  108 ? 5.801   -49.261 -88.969  1.00 110.43 ? 108  ARG   C CZ   1 
ATOM   17815 N  NH1  . ARG   C  3  108 ? 4.550   -49.577 -89.282  1.00 111.65 ? 108  ARG   C NH1  1 
ATOM   17816 N  NH2  . ARG   C  3  108 ? 6.727   -49.228 -89.917  1.00 113.37 ? 108  ARG   C NH2  1 
ATOM   17817 H  H    . ARG   C  3  108 ? 0.457   -47.226 -84.739  1.00 127.19 ? 108  ARG   C H    1 
ATOM   17818 H  HA   . ARG   C  3  108 ? 2.344   -46.113 -86.279  1.00 123.05 ? 108  ARG   C HA   1 
ATOM   17819 H  HB2  . ARG   C  3  108 ? 3.267   -48.013 -84.867  1.00 120.82 ? 108  ARG   C HB2  1 
ATOM   17820 H  HB3  . ARG   C  3  108 ? 2.677   -48.865 -86.071  1.00 120.82 ? 108  ARG   C HB3  1 
ATOM   17821 H  HG2  . ARG   C  3  108 ? 4.059   -47.538 -87.519  1.00 122.39 ? 108  ARG   C HG2  1 
ATOM   17822 H  HG3  . ARG   C  3  108 ? 4.783   -47.016 -86.204  1.00 122.39 ? 108  ARG   C HG3  1 
ATOM   17823 H  HD2  . ARG   C  3  108 ? 5.682   -49.013 -85.774  1.00 124.21 ? 108  ARG   C HD2  1 
ATOM   17824 H  HD3  . ARG   C  3  108 ? 4.624   -49.775 -86.682  1.00 124.21 ? 108  ARG   C HD3  1 
ATOM   17825 H  HE   . ARG   C  3  108 ? 6.941   -48.765 -87.543  1.00 128.81 ? 108  ARG   C HE   1 
ATOM   17826 H  HH11 . ARG   C  3  108 ? 3.946   -49.595 -88.670  1.00 134.01 ? 108  ARG   C HH11 1 
ATOM   17827 H  HH12 . ARG   C  3  108 ? 4.345   -49.764 -90.095  1.00 134.01 ? 108  ARG   C HH12 1 
ATOM   17828 H  HH21 . ARG   C  3  108 ? 7.537   -49.020 -89.719  1.00 136.08 ? 108  ARG   C HH21 1 
ATOM   17829 H  HH22 . ARG   C  3  108 ? 6.517   -49.416 -90.729  1.00 136.08 ? 108  ARG   C HH22 1 
ATOM   17830 N  N    . ALA   C  3  109 ? 1.404   -47.137 -88.357  1.00 102.77 ? 109  ALA   C N    1 
ATOM   17831 C  CA   . ALA   C  3  109 ? 0.705   -47.706 -89.497  1.00 105.58 ? 109  ALA   C CA   1 
ATOM   17832 C  C    . ALA   C  3  109 ? 0.891   -49.217 -89.496  1.00 107.95 ? 109  ALA   C C    1 
ATOM   17833 O  O    . ALA   C  3  109 ? 1.989   -49.721 -89.243  1.00 106.65 ? 109  ALA   C O    1 
ATOM   17834 C  CB   . ALA   C  3  109 ? 1.224   -47.105 -90.801  1.00 105.00 ? 109  ALA   C CB   1 
ATOM   17835 H  H    . ALA   C  3  109 ? 2.081   -46.646 -88.558  1.00 123.36 ? 109  ALA   C H    1 
ATOM   17836 H  HA   . ALA   C  3  109 ? -0.243  -47.505 -89.444  1.00 126.73 ? 109  ALA   C HA   1 
ATOM   17837 H  HB1  . ALA   C  3  109 ? 0.743   -47.499 -91.545  1.00 126.04 ? 109  ALA   C HB1  1 
ATOM   17838 H  HB2  . ALA   C  3  109 ? 1.081   -46.145 -90.785  1.00 126.04 ? 109  ALA   C HB2  1 
ATOM   17839 H  HB3  . ALA   C  3  109 ? 2.172   -47.296 -90.881  1.00 126.04 ? 109  ALA   C HB3  1 
ATOM   17840 N  N    . ASP   C  3  110 ? -0.191  -49.944 -89.762  1.00 111.16 ? 110  ASP   C N    1 
ATOM   17841 C  CA   . ASP   C  3  110 ? -0.126  -51.398 -89.753  1.00 111.97 ? 110  ASP   C CA   1 
ATOM   17842 C  C    . ASP   C  3  110 ? 0.986   -51.884 -90.673  1.00 111.63 ? 110  ASP   C C    1 
ATOM   17843 O  O    . ASP   C  3  110 ? 1.203   -51.338 -91.758  1.00 89.83  ? 110  ASP   C O    1 
ATOM   17844 C  CB   . ASP   C  3  110 ? -1.466  -51.997 -90.183  1.00 115.84 ? 110  ASP   C CB   1 
ATOM   17845 C  CG   . ASP   C  3  110 ? -2.497  -51.973 -89.072  1.00 114.60 ? 110  ASP   C CG   1 
ATOM   17846 O  OD1  . ASP   C  3  110 ? -2.290  -51.239 -88.083  1.00 109.51 ? 110  ASP   C OD1  1 
ATOM   17847 O  OD2  . ASP   C  3  110 ? -3.510  -52.695 -89.184  1.00 114.52 ? 110  ASP   C OD2  1 
ATOM   17848 H  H    . ASP   C  3  110 ? -0.967  -49.621 -89.948  1.00 133.42 ? 110  ASP   C H    1 
ATOM   17849 H  HA   . ASP   C  3  110 ? 0.062   -51.705 -88.852  1.00 134.40 ? 110  ASP   C HA   1 
ATOM   17850 H  HB2  . ASP   C  3  110 ? -1.816  -51.487 -90.930  1.00 139.05 ? 110  ASP   C HB2  1 
ATOM   17851 H  HB3  . ASP   C  3  110 ? -1.330  -52.921 -90.446  1.00 139.05 ? 110  ASP   C HB3  1 
ATOM   17852 N  N    . ALA   C  3  111 ? 1.700   -52.912 -90.225  1.00 106.03 ? 111  ALA   C N    1 
ATOM   17853 C  CA   . ALA   C  3  111 ? 2.799   -53.489 -90.979  1.00 98.73  ? 111  ALA   C CA   1 
ATOM   17854 C  C    . ALA   C  3  111 ? 2.670   -55.003 -90.974  1.00 100.41 ? 111  ALA   C C    1 
ATOM   17855 O  O    . ALA   C  3  111 ? 2.023   -55.591 -90.103  1.00 101.33 ? 111  ALA   C O    1 
ATOM   17856 C  CB   . ALA   C  3  111 ? 4.159   -53.073 -90.405  1.00 92.07  ? 111  ALA   C CB   1 
ATOM   17857 H  H    . ALA   C  3  111 ? 1.560   -53.299 -89.469  1.00 127.28 ? 111  ALA   C H    1 
ATOM   17858 H  HA   . ALA   C  3  111 ? 2.757   -53.183 -91.899  1.00 118.51 ? 111  ALA   C HA   1 
ATOM   17859 H  HB1  . ALA   C  3  111 ? 4.859   -53.559 -90.867  1.00 110.52 ? 111  ALA   C HB1  1 
ATOM   17860 H  HB2  . ALA   C  3  111 ? 4.278   -52.119 -90.534  1.00 110.52 ? 111  ALA   C HB2  1 
ATOM   17861 H  HB3  . ALA   C  3  111 ? 4.180   -53.283 -89.458  1.00 110.52 ? 111  ALA   C HB3  1 
ATOM   17862 N  N    . ALA   C  3  112 ? 3.300   -55.630 -91.963  1.00 102.25 ? 112  ALA   C N    1 
ATOM   17863 C  CA   . ALA   C  3  112 ? 3.219   -57.077 -92.073  1.00 102.31 ? 112  ALA   C CA   1 
ATOM   17864 C  C    . ALA   C  3  112 ? 4.491   -57.723 -91.540  1.00 102.11 ? 112  ALA   C C    1 
ATOM   17865 O  O    . ALA   C  3  112 ? 5.594   -57.225 -91.796  1.00 102.20 ? 112  ALA   C O    1 
ATOM   17866 C  CB   . ALA   C  3  112 ? 3.009   -57.500 -93.527  1.00 103.79 ? 112  ALA   C CB   1 
ATOM   17867 H  H    . ALA   C  3  112 ? 3.771   -55.246 -92.571  1.00 122.74 ? 112  ALA   C H    1 
ATOM   17868 H  HA   . ALA   C  3  112 ? 2.467   -57.402 -91.555  1.00 122.81 ? 112  ALA   C HA   1 
ATOM   17869 H  HB1  . ALA   C  3  112 ? 2.981   -58.469 -93.573  1.00 124.59 ? 112  ALA   C HB1  1 
ATOM   17870 H  HB2  . ALA   C  3  112 ? 2.172   -57.129 -93.846  1.00 124.59 ? 112  ALA   C HB2  1 
ATOM   17871 H  HB3  . ALA   C  3  112 ? 3.745   -57.165 -94.063  1.00 124.59 ? 112  ALA   C HB3  1 
ATOM   17872 N  N    . PRO   C  3  113 ? 4.378   -58.824 -90.801  1.00 102.11 ? 113  PRO   C N    1 
ATOM   17873 C  CA   . PRO   C  3  113 ? 5.583   -59.464 -90.266  1.00 102.73 ? 113  PRO   C CA   1 
ATOM   17874 C  C    . PRO   C  3  113 ? 6.420   -60.088 -91.369  1.00 103.41 ? 113  PRO   C C    1 
ATOM   17875 O  O    . PRO   C  3  113 ? 5.899   -60.732 -92.282  1.00 103.78 ? 113  PRO   C O    1 
ATOM   17876 C  CB   . PRO   C  3  113 ? 5.028   -60.532 -89.313  1.00 104.03 ? 113  PRO   C CB   1 
ATOM   17877 C  CG   . PRO   C  3  113 ? 3.650   -60.811 -89.803  1.00 104.88 ? 113  PRO   C CG   1 
ATOM   17878 C  CD   . PRO   C  3  113 ? 3.146   -59.541 -90.421  1.00 103.44 ? 113  PRO   C CD   1 
ATOM   17879 H  HA   . PRO   C  3  113 ? 6.119   -58.827 -89.769  1.00 123.31 ? 113  PRO   C HA   1 
ATOM   17880 H  HB2  . PRO   C  3  113 ? 5.579   -61.330 -89.356  1.00 124.88 ? 113  PRO   C HB2  1 
ATOM   17881 H  HB3  . PRO   C  3  113 ? 5.011   -60.188 -88.407  1.00 124.88 ? 113  PRO   C HB3  1 
ATOM   17882 H  HG2  . PRO   C  3  113 ? 3.678   -61.522 -90.462  1.00 125.89 ? 113  PRO   C HG2  1 
ATOM   17883 H  HG3  . PRO   C  3  113 ? 3.088   -61.072 -89.057  1.00 125.89 ? 113  PRO   C HG3  1 
ATOM   17884 H  HD2  . PRO   C  3  113 ? 2.604   -59.730 -91.202  1.00 124.16 ? 113  PRO   C HD2  1 
ATOM   17885 H  HD3  . PRO   C  3  113 ? 2.633   -59.026 -89.778  1.00 124.16 ? 113  PRO   C HD3  1 
ATOM   17886 N  N    . THR   C  3  114 ? 7.731   -59.876 -91.286  1.00 97.06  ? 114  THR   C N    1 
ATOM   17887 C  CA   . THR   C  3  114 ? 8.672   -60.651 -92.082  1.00 97.20  ? 114  THR   C CA   1 
ATOM   17888 C  C    . THR   C  3  114 ? 8.870   -61.991 -91.389  1.00 95.08  ? 114  THR   C C    1 
ATOM   17889 O  O    . THR   C  3  114 ? 9.301   -62.036 -90.231  1.00 91.66  ? 114  THR   C O    1 
ATOM   17890 C  CB   . THR   C  3  114 ? 10.007  -59.931 -92.235  1.00 95.48  ? 114  THR   C CB   1 
ATOM   17891 O  OG1  . THR   C  3  114 ? 9.792   -58.609 -92.740  1.00 99.12  ? 114  THR   C OG1  1 
ATOM   17892 C  CG2  . THR   C  3  114 ? 10.911  -60.698 -93.192  1.00 97.61  ? 114  THR   C CG2  1 
ATOM   17893 H  H    . THR   C  3  114 ? 8.098   -59.288 -90.776  1.00 116.51 ? 114  THR   C H    1 
ATOM   17894 H  HA   . THR   C  3  114 ? 8.314   -60.781 -92.975  1.00 116.68 ? 114  THR   C HA   1 
ATOM   17895 H  HB   . THR   C  3  114 ? 10.446  -59.875 -91.371  1.00 114.61 ? 114  THR   C HB   1 
ATOM   17896 H  HG1  . THR   C  3  114 ? 10.528  -58.245 -92.916  1.00 118.98 ? 114  THR   C HG1  1 
ATOM   17897 H  HG21 . THR   C  3  114 ? 11.713  -60.184 -93.375  1.00 117.16 ? 114  THR   C HG21 1 
ATOM   17898 H  HG22 . THR   C  3  114 ? 11.165  -61.549 -92.800  1.00 117.16 ? 114  THR   C HG22 1 
ATOM   17899 H  HG23 . THR   C  3  114 ? 10.446  -60.863 -94.027  1.00 117.16 ? 114  THR   C HG23 1 
ATOM   17900 N  N    . VAL   C  3  115 ? 8.551   -63.074 -92.087  1.00 98.36  ? 115  VAL   C N    1 
ATOM   17901 C  CA   . VAL   C  3  115 ? 8.547   -64.408 -91.508  1.00 98.80  ? 115  VAL   C CA   1 
ATOM   17902 C  C    . VAL   C  3  115 ? 9.669   -65.226 -92.116  1.00 98.58  ? 115  VAL   C C    1 
ATOM   17903 O  O    . VAL   C  3  115 ? 9.903   -65.173 -93.328  1.00 98.10  ? 115  VAL   C O    1 
ATOM   17904 C  CB   . VAL   C  3  115 ? 7.197   -65.115 -91.719  1.00 106.25 ? 115  VAL   C CB   1 
ATOM   17905 C  CG1  . VAL   C  3  115 ? 7.171   -66.409 -90.865  1.00 106.15 ? 115  VAL   C CG1  1 
ATOM   17906 C  CG2  . VAL   C  3  115 ? 6.073   -64.134 -91.424  1.00 107.57 ? 115  VAL   C CG2  1 
ATOM   17907 H  H    . VAL   C  3  115 ? 8.329   -63.059 -92.918  1.00 118.07 ? 115  VAL   C H    1 
ATOM   17908 H  HA   . VAL   C  3  115 ? 8.710   -64.326 -90.555  1.00 118.60 ? 115  VAL   C HA   1 
ATOM   17909 H  HB   . VAL   C  3  115 ? 7.064   -65.399 -92.638  1.00 127.53 ? 115  VAL   C HB   1 
ATOM   17910 H  HG11 . VAL   C  3  115 ? 6.265   -66.752 -90.839  1.00 127.42 ? 115  VAL   C HG11 1 
ATOM   17911 H  HG12 . VAL   C  3  115 ? 7.762   -67.064 -91.266  1.00 127.42 ? 115  VAL   C HG12 1 
ATOM   17912 H  HG13 . VAL   C  3  115 ? 7.471   -66.200 -89.966  1.00 127.42 ? 115  VAL   C HG13 1 
ATOM   17913 H  HG21 . VAL   C  3  115 ? 5.334   -64.614 -91.017  1.00 129.12 ? 115  VAL   C HG21 1 
ATOM   17914 H  HG22 . VAL   C  3  115 ? 6.400   -63.453 -90.815  1.00 129.12 ? 115  VAL   C HG22 1 
ATOM   17915 H  HG23 . VAL   C  3  115 ? 5.784   -63.725 -92.254  1.00 129.12 ? 115  VAL   C HG23 1 
ATOM   17916 N  N    . SER   C  3  116 ? 10.347  -65.999 -91.274  1.00 100.83 ? 116  SER   C N    1 
ATOM   17917 C  CA   . SER   C  3  116 ? 11.404  -66.890 -91.723  1.00 101.43 ? 116  SER   C CA   1 
ATOM   17918 C  C    . SER   C  3  116 ? 11.394  -68.131 -90.845  1.00 99.24  ? 116  SER   C C    1 
ATOM   17919 O  O    . SER   C  3  116 ? 11.259  -68.030 -89.623  1.00 95.84  ? 116  SER   C O    1 
ATOM   17920 C  CB   . SER   C  3  116 ? 12.771  -66.201 -91.670  1.00 98.13  ? 116  SER   C CB   1 
ATOM   17921 O  OG   . SER   C  3  116 ? 12.874  -65.358 -90.536  1.00 98.21  ? 116  SER   C OG   1 
ATOM   17922 H  H    . SER   C  3  116 ? 10.210  -66.023 -90.425  1.00 121.03 ? 116  SER   C H    1 
ATOM   17923 H  HA   . SER   C  3  116 ? 11.244  -67.165 -92.639  1.00 121.75 ? 116  SER   C HA   1 
ATOM   17924 H  HB2  . SER   C  3  116 ? 13.464  -66.879 -91.623  1.00 117.79 ? 116  SER   C HB2  1 
ATOM   17925 H  HB3  . SER   C  3  116 ? 12.885  -65.666 -92.471  1.00 117.79 ? 116  SER   C HB3  1 
ATOM   17926 H  HG   . SER   C  3  116 ? 12.714  -64.563 -90.753  1.00 117.89 ? 116  SER   C HG   1 
ATOM   17927 N  N    . ILE   C  3  117 ? 11.530  -69.296 -91.473  1.00 100.47 ? 117  ILE   C N    1 
ATOM   17928 C  CA   . ILE   C  3  117 ? 11.545  -70.575 -90.774  1.00 99.09  ? 117  ILE   C CA   1 
ATOM   17929 C  C    . ILE   C  3  117 ? 12.941  -71.167 -90.891  1.00 96.97  ? 117  ILE   C C    1 
ATOM   17930 O  O    . ILE   C  3  117 ? 13.598  -71.032 -91.930  1.00 99.19  ? 117  ILE   C O    1 
ATOM   17931 C  CB   . ILE   C  3  117 ? 10.488  -71.549 -91.332  1.00 103.67 ? 117  ILE   C CB   1 
ATOM   17932 C  CG1  . ILE   C  3  117 ? 10.338  -72.744 -90.388  1.00 103.03 ? 117  ILE   C CG1  1 
ATOM   17933 C  CG2  . ILE   C  3  117 ? 10.870  -72.017 -92.737  1.00 105.46 ? 117  ILE   C CG2  1 
ATOM   17934 C  CD1  . ILE   C  3  117 ? 9.176   -73.657 -90.717  1.00 112.38 ? 117  ILE   C CD1  1 
ATOM   17935 H  H    . ILE   C  3  117 ? 11.617  -69.372 -92.325  1.00 120.60 ? 117  ILE   C H    1 
ATOM   17936 H  HA   . ILE   C  3  117 ? 11.346  -70.425 -89.836  1.00 118.94 ? 117  ILE   C HA   1 
ATOM   17937 H  HB   . ILE   C  3  117 ? 9.639   -71.084 -91.391  1.00 124.44 ? 117  ILE   C HB   1 
ATOM   17938 H  HG12 . ILE   C  3  117 ? 11.149  -73.275 -90.430  1.00 123.68 ? 117  ILE   C HG12 1 
ATOM   17939 H  HG13 . ILE   C  3  117 ? 10.205  -72.412 -89.487  1.00 123.68 ? 117  ILE   C HG13 1 
ATOM   17940 H  HG21 . ILE   C  3  117 ? 10.168  -72.593 -93.079  1.00 126.59 ? 117  ILE   C HG21 1 
ATOM   17941 H  HG22 . ILE   C  3  117 ? 10.972  -71.242 -93.312  1.00 126.59 ? 117  ILE   C HG22 1 
ATOM   17942 H  HG23 . ILE   C  3  117 ? 11.706  -72.507 -92.691  1.00 126.59 ? 117  ILE   C HG23 1 
ATOM   17943 H  HD11 . ILE   C  3  117 ? 9.215   -74.437 -90.143  1.00 134.89 ? 117  ILE   C HD11 1 
ATOM   17944 H  HD12 . ILE   C  3  117 ? 8.346   -73.177 -90.569  1.00 134.89 ? 117  ILE   C HD12 1 
ATOM   17945 H  HD13 . ILE   C  3  117 ? 9.240   -73.927 -91.647  1.00 134.89 ? 117  ILE   C HD13 1 
ATOM   17946 N  N    . PHE   C  3  118 ? 13.391  -71.830 -89.826  1.00 92.71  ? 118  PHE   C N    1 
ATOM   17947 C  CA   . PHE   C  3  118 ? 14.724  -72.409 -89.787  1.00 87.17  ? 118  PHE   C CA   1 
ATOM   17948 C  C    . PHE   C  3  118 ? 14.643  -73.857 -89.320  1.00 84.75  ? 118  PHE   C C    1 
ATOM   17949 O  O    . PHE   C  3  118 ? 14.031  -74.138 -88.275  1.00 85.56  ? 118  PHE   C O    1 
ATOM   17950 C  CB   . PHE   C  3  118 ? 15.639  -71.603 -88.861  1.00 80.07  ? 118  PHE   C CB   1 
ATOM   17951 C  CG   . PHE   C  3  118 ? 15.877  -70.202 -89.329  1.00 82.48  ? 118  PHE   C CG   1 
ATOM   17952 C  CD1  . PHE   C  3  118 ? 14.983  -69.195 -89.013  1.00 85.16  ? 118  PHE   C CD1  1 
ATOM   17953 C  CD2  . PHE   C  3  118 ? 16.988  -69.892 -90.093  1.00 84.41  ? 118  PHE   C CD2  1 
ATOM   17954 C  CE1  . PHE   C  3  118 ? 15.194  -67.904 -89.445  1.00 86.89  ? 118  PHE   C CE1  1 
ATOM   17955 C  CE2  . PHE   C  3  118 ? 17.206  -68.602 -90.528  1.00 86.38  ? 118  PHE   C CE2  1 
ATOM   17956 C  CZ   . PHE   C  3  118 ? 16.306  -67.606 -90.203  1.00 87.63  ? 118  PHE   C CZ   1 
ATOM   17957 H  H    . PHE   C  3  118 ? 12.934  -71.956 -89.108  1.00 111.29 ? 118  PHE   C H    1 
ATOM   17958 H  HA   . PHE   C  3  118 ? 15.096  -72.402 -90.682  1.00 104.64 ? 118  PHE   C HA   1 
ATOM   17959 H  HB2  . PHE   C  3  118 ? 15.233  -71.557 -87.982  1.00 96.13  ? 118  PHE   C HB2  1 
ATOM   17960 H  HB3  . PHE   C  3  118 ? 16.499  -72.048 -88.807  1.00 96.13  ? 118  PHE   C HB3  1 
ATOM   17961 H  HD1  . PHE   C  3  118 ? 14.230  -69.391 -88.503  1.00 102.23 ? 118  PHE   C HD1  1 
ATOM   17962 H  HD2  . PHE   C  3  118 ? 17.595  -70.562 -90.315  1.00 101.33 ? 118  PHE   C HD2  1 
ATOM   17963 H  HE1  . PHE   C  3  118 ? 14.588  -67.234 -89.226  1.00 104.30 ? 118  PHE   C HE1  1 
ATOM   17964 H  HE2  . PHE   C  3  118 ? 17.957  -68.403 -91.039  1.00 103.70 ? 118  PHE   C HE2  1 
ATOM   17965 H  HZ   . PHE   C  3  118 ? 16.451  -66.735 -90.496  1.00 105.19 ? 118  PHE   C HZ   1 
ATOM   17966 N  N    . PRO   C  3  119 ? 15.239  -74.795 -90.049  1.00 85.13  ? 119  PRO   C N    1 
ATOM   17967 C  CA   . PRO   C  3  119 ? 15.255  -76.184 -89.601  1.00 86.87  ? 119  PRO   C CA   1 
ATOM   17968 C  C    . PRO   C  3  119 ? 16.293  -76.385 -88.514  1.00 86.31  ? 119  PRO   C C    1 
ATOM   17969 O  O    . PRO   C  3  119 ? 17.133  -75.505 -88.274  1.00 86.48  ? 119  PRO   C O    1 
ATOM   17970 C  CB   . PRO   C  3  119 ? 15.615  -76.960 -90.877  1.00 89.22  ? 119  PRO   C CB   1 
ATOM   17971 C  CG   . PRO   C  3  119 ? 16.419  -76.003 -91.674  1.00 89.29  ? 119  PRO   C CG   1 
ATOM   17972 C  CD   . PRO   C  3  119 ? 15.886  -74.632 -91.364  1.00 86.98  ? 119  PRO   C CD   1 
ATOM   17973 H  HA   . PRO   C  3  119 ? 14.383  -76.465 -89.282  1.00 104.28 ? 119  PRO   C HA   1 
ATOM   17974 H  HB2  . PRO   C  3  119 ? 16.133  -77.749 -90.651  1.00 107.10 ? 119  PRO   C HB2  1 
ATOM   17975 H  HB3  . PRO   C  3  119 ? 14.808  -77.217 -91.349  1.00 107.10 ? 119  PRO   C HB3  1 
ATOM   17976 H  HG2  . PRO   C  3  119 ? 17.352  -76.072 -91.420  1.00 107.18 ? 119  PRO   C HG2  1 
ATOM   17977 H  HG3  . PRO   C  3  119 ? 16.317  -76.203 -92.618  1.00 107.18 ? 119  PRO   C HG3  1 
ATOM   17978 H  HD2  . PRO   C  3  119 ? 16.609  -73.987 -91.313  1.00 104.41 ? 119  PRO   C HD2  1 
ATOM   17979 H  HD3  . PRO   C  3  119 ? 15.241  -74.355 -92.033  1.00 104.41 ? 119  PRO   C HD3  1 
ATOM   17980 N  N    . PRO   C  3  120 ? 16.272  -77.530 -87.836  1.00 83.62  ? 120  PRO   C N    1 
ATOM   17981 C  CA   . PRO   C  3  120 ? 17.223  -77.751 -86.741  1.00 81.87  ? 120  PRO   C CA   1 
ATOM   17982 C  C    . PRO   C  3  120 ? 18.655  -77.809 -87.249  1.00 78.40  ? 120  PRO   C C    1 
ATOM   17983 O  O    . PRO   C  3  120 ? 18.938  -78.379 -88.305  1.00 82.80  ? 120  PRO   C O    1 
ATOM   17984 C  CB   . PRO   C  3  120 ? 16.779  -79.097 -86.157  1.00 86.46  ? 120  PRO   C CB   1 
ATOM   17985 C  CG   . PRO   C  3  120 ? 16.099  -79.787 -87.301  1.00 89.38  ? 120  PRO   C CG   1 
ATOM   17986 C  CD   . PRO   C  3  120 ? 15.415  -78.704 -88.073  1.00 87.38  ? 120  PRO   C CD   1 
ATOM   17987 H  HA   . PRO   C  3  120 ? 17.145  -77.057 -86.068  1.00 98.28  ? 120  PRO   C HA   1 
ATOM   17988 H  HB2  . PRO   C  3  120 ? 17.551  -79.600 -85.853  1.00 103.79 ? 120  PRO   C HB2  1 
ATOM   17989 H  HB3  . PRO   C  3  120 ? 16.165  -78.955 -85.419  1.00 103.79 ? 120  PRO   C HB3  1 
ATOM   17990 H  HG2  . PRO   C  3  120 ? 16.759  -80.238 -87.851  1.00 107.29 ? 120  PRO   C HG2  1 
ATOM   17991 H  HG3  . PRO   C  3  120 ? 15.455  -80.428 -86.962  1.00 107.29 ? 120  PRO   C HG3  1 
ATOM   17992 H  HD2  . PRO   C  3  120 ? 15.380  -78.922 -89.018  1.00 104.89 ? 120  PRO   C HD2  1 
ATOM   17993 H  HD3  . PRO   C  3  120 ? 14.518  -78.551 -87.735  1.00 104.89 ? 120  PRO   C HD3  1 
ATOM   17994 N  N    . SER   C  3  121 ? 19.561  -77.209 -86.481  1.00 74.91  ? 121  SER   C N    1 
ATOM   17995 C  CA   . SER   C  3  121 ? 20.969  -77.223 -86.850  1.00 77.03  ? 121  SER   C CA   1 
ATOM   17996 C  C    . SER   C  3  121 ? 21.510  -78.647 -86.816  1.00 76.93  ? 121  SER   C C    1 
ATOM   17997 O  O    . SER   C  3  121 ? 21.012  -79.509 -86.088  1.00 74.28  ? 121  SER   C O    1 
ATOM   17998 C  CB   . SER   C  3  121 ? 21.783  -76.339 -85.905  1.00 77.34  ? 121  SER   C CB   1 
ATOM   17999 O  OG   . SER   C  3  121 ? 21.833  -76.895 -84.602  1.00 79.77  ? 121  SER   C OG   1 
ATOM   18000 H  H    . SER   C  3  121 ? 19.388  -76.792 -85.749  1.00 89.93  ? 121  SER   C H    1 
ATOM   18001 H  HA   . SER   C  3  121 ? 21.067  -76.874 -87.750  1.00 92.47  ? 121  SER   C HA   1 
ATOM   18002 H  HB2  . SER   C  3  121 ? 22.687  -76.260 -86.248  1.00 92.84  ? 121  SER   C HB2  1 
ATOM   18003 H  HB3  . SER   C  3  121 ? 21.368  -75.464 -85.857  1.00 92.84  ? 121  SER   C HB3  1 
ATOM   18004 H  HG   . SER   C  3  121 ? 21.081  -76.831 -84.233  1.00 95.76  ? 121  SER   C HG   1 
ATOM   18005 N  N    . SER   C  3  122 ? 22.546  -78.892 -87.621  1.00 80.64  ? 122  SER   C N    1 
ATOM   18006 C  CA   . SER   C  3  122 ? 23.215  -80.186 -87.564  1.00 84.51  ? 122  SER   C CA   1 
ATOM   18007 C  C    . SER   C  3  122 ? 23.850  -80.413 -86.200  1.00 82.66  ? 122  SER   C C    1 
ATOM   18008 O  O    . SER   C  3  122 ? 23.873  -81.546 -85.709  1.00 82.11  ? 122  SER   C O    1 
ATOM   18009 C  CB   . SER   C  3  122 ? 24.268  -80.286 -88.667  1.00 88.74  ? 122  SER   C CB   1 
ATOM   18010 O  OG   . SER   C  3  122 ? 23.662  -80.233 -89.946  1.00 94.58  ? 122  SER   C OG   1 
ATOM   18011 H  H    . SER   C  3  122 ? 22.871  -78.339 -88.193  1.00 96.81  ? 122  SER   C H    1 
ATOM   18012 H  HA   . SER   C  3  122 ? 22.563  -80.887 -87.717  1.00 101.45 ? 122  SER   C HA   1 
ATOM   18013 H  HB2  . SER   C  3  122 ? 24.888  -79.546 -88.580  1.00 106.53 ? 122  SER   C HB2  1 
ATOM   18014 H  HB3  . SER   C  3  122 ? 24.741  -81.128 -88.576  1.00 106.53 ? 122  SER   C HB3  1 
ATOM   18015 H  HG   . SER   C  3  122 ? 24.200  -80.506 -90.530  1.00 113.53 ? 122  SER   C HG   1 
ATOM   18016 N  N    . GLU   C  3  123 ? 24.361  -79.350 -85.571  1.00 83.55  ? 123  GLU   C N    1 
ATOM   18017 C  CA   . GLU   C  3  123 ? 24.888  -79.472 -84.216  1.00 85.62  ? 123  GLU   C CA   1 
ATOM   18018 C  C    . GLU   C  3  123 ? 23.848  -80.066 -83.276  1.00 85.23  ? 123  GLU   C C    1 
ATOM   18019 O  O    . GLU   C  3  123 ? 24.158  -80.940 -82.459  1.00 86.70  ? 123  GLU   C O    1 
ATOM   18020 C  CB   . GLU   C  3  123 ? 25.335  -78.105 -83.694  1.00 86.62  ? 123  GLU   C CB   1 
ATOM   18021 C  CG   . GLU   C  3  123 ? 26.585  -77.534 -84.346  1.00 89.15  ? 123  GLU   C CG   1 
ATOM   18022 C  CD   . GLU   C  3  123 ? 26.325  -76.960 -85.726  1.00 89.56  ? 123  GLU   C CD   1 
ATOM   18023 O  OE1  . GLU   C  3  123 ? 25.241  -77.222 -86.288  1.00 89.71  ? 123  GLU   C OE1  1 
ATOM   18024 O  OE2  . GLU   C  3  123 ? 27.205  -76.242 -86.247  1.00 90.12  ? 123  GLU   C OE2  1 
ATOM   18025 H  H    . GLU   C  3  123 ? 24.412  -78.559 -85.904  1.00 100.29 ? 123  GLU   C H    1 
ATOM   18026 H  HA   . GLU   C  3  123 ? 25.661  -80.058 -84.238  1.00 102.79 ? 123  GLU   C HA   1 
ATOM   18027 H  HB2  . GLU   C  3  123 ? 24.616  -77.471 -83.842  1.00 103.98 ? 123  GLU   C HB2  1 
ATOM   18028 H  HB3  . GLU   C  3  123 ? 25.516  -78.185 -82.744  1.00 103.98 ? 123  GLU   C HB3  1 
ATOM   18029 H  HG2  . GLU   C  3  123 ? 26.935  -76.821 -83.788  1.00 107.01 ? 123  GLU   C HG2  1 
ATOM   18030 H  HG3  . GLU   C  3  123 ? 27.245  -78.239 -84.435  1.00 107.01 ? 123  GLU   C HG3  1 
ATOM   18031 N  N    . GLN   C  3  124 ? 22.603  -79.598 -83.381  1.00 85.03  ? 124  GLN   C N    1 
ATOM   18032 C  CA   . GLN   C  3  124 ? 21.560  -80.040 -82.463  1.00 86.76  ? 124  GLN   C CA   1 
ATOM   18033 C  C    . GLN   C  3  124 ? 21.155  -81.484 -82.731  1.00 87.69  ? 124  GLN   C C    1 
ATOM   18034 O  O    . GLN   C  3  124 ? 20.923  -82.253 -81.790  1.00 87.87  ? 124  GLN   C O    1 
ATOM   18035 C  CB   . GLN   C  3  124 ? 20.352  -79.111 -82.579  1.00 85.10  ? 124  GLN   C CB   1 
ATOM   18036 C  CG   . GLN   C  3  124 ? 19.218  -79.433 -81.630  1.00 83.92  ? 124  GLN   C CG   1 
ATOM   18037 C  CD   . GLN   C  3  124 ? 18.118  -78.394 -81.682  1.00 81.70  ? 124  GLN   C CD   1 
ATOM   18038 O  OE1  . GLN   C  3  124 ? 17.796  -77.866 -82.747  1.00 81.45  ? 124  GLN   C OE1  1 
ATOM   18039 N  NE2  . GLN   C  3  124 ? 17.544  -78.083 -80.527  1.00 81.45  ? 124  GLN   C NE2  1 
ATOM   18040 H  H    . GLN   C  3  124 ? 22.340  -79.029 -83.971  1.00 102.07 ? 124  GLN   C H    1 
ATOM   18041 H  HA   . GLN   C  3  124 ? 21.898  -79.993 -81.555  1.00 104.15 ? 124  GLN   C HA   1 
ATOM   18042 H  HB2  . GLN   C  3  124 ? 20.641  -78.204 -82.392  1.00 102.16 ? 124  GLN   C HB2  1 
ATOM   18043 H  HB3  . GLN   C  3  124 ? 20.004  -79.169 -83.482  1.00 102.16 ? 124  GLN   C HB3  1 
ATOM   18044 H  HG2  . GLN   C  3  124 ? 18.835  -80.291 -81.872  1.00 100.74 ? 124  GLN   C HG2  1 
ATOM   18045 H  HG3  . GLN   C  3  124 ? 19.560  -79.466 -80.723  1.00 100.74 ? 124  GLN   C HG3  1 
ATOM   18046 H  HE21 . GLN   C  3  124 ? 17.801  -78.467 -79.802  1.00 97.77  ? 124  GLN   C HE21 1 
ATOM   18047 H  HE22 . GLN   C  3  124 ? 16.914  -77.498 -80.504  1.00 97.77  ? 124  GLN   C HE22 1 
ATOM   18048 N  N    . LEU   C  3  125 ? 21.066  -81.873 -84.004  1.00 89.19  ? 125  LEU   C N    1 
ATOM   18049 C  CA   . LEU   C  3  125 ? 20.598  -83.217 -84.326  1.00 91.48  ? 125  LEU   C CA   1 
ATOM   18050 C  C    . LEU   C  3  125 ? 21.576  -84.288 -83.853  1.00 94.85  ? 125  LEU   C C    1 
ATOM   18051 O  O    . LEU   C  3  125 ? 21.163  -85.425 -83.598  1.00 100.43 ? 125  LEU   C O    1 
ATOM   18052 C  CB   . LEU   C  3  125 ? 20.345  -83.334 -85.830  1.00 91.89  ? 125  LEU   C CB   1 
ATOM   18053 C  CG   . LEU   C  3  125 ? 19.091  -82.602 -86.322  1.00 96.30  ? 125  LEU   C CG   1 
ATOM   18054 C  CD1  . LEU   C  3  125 ? 19.112  -82.420 -87.832  1.00 98.95  ? 125  LEU   C CD1  1 
ATOM   18055 C  CD2  . LEU   C  3  125 ? 17.833  -83.347 -85.900  1.00 100.32 ? 125  LEU   C CD2  1 
ATOM   18056 H  H    . LEU   C  3  125 ? 21.266  -81.387 -84.685  1.00 107.07 ? 125  LEU   C H    1 
ATOM   18057 H  HA   . LEU   C  3  125 ? 19.756  -83.374 -83.870  1.00 109.81 ? 125  LEU   C HA   1 
ATOM   18058 H  HB2  . LEU   C  3  125 ? 21.107  -82.961 -86.301  1.00 110.31 ? 125  LEU   C HB2  1 
ATOM   18059 H  HB3  . LEU   C  3  125 ? 20.244  -84.272 -86.053  1.00 110.31 ? 125  LEU   C HB3  1 
ATOM   18060 H  HG   . LEU   C  3  125 ? 19.078  -81.720 -85.918  1.00 115.59 ? 125  LEU   C HG   1 
ATOM   18061 H  HD11 . LEU   C  3  125 ? 18.315  -81.939 -88.103  1.00 118.77 ? 125  LEU   C HD11 1 
ATOM   18062 H  HD12 . LEU   C  3  125 ? 19.903  -81.916 -88.079  1.00 118.77 ? 125  LEU   C HD12 1 
ATOM   18063 H  HD13 . LEU   C  3  125 ? 19.131  -83.293 -88.255  1.00 118.77 ? 125  LEU   C HD13 1 
ATOM   18064 H  HD21 . LEU   C  3  125 ? 17.057  -82.874 -86.239  1.00 120.43 ? 125  LEU   C HD21 1 
ATOM   18065 H  HD22 . LEU   C  3  125 ? 17.859  -84.245 -86.268  1.00 120.43 ? 125  LEU   C HD22 1 
ATOM   18066 H  HD23 . LEU   C  3  125 ? 17.799  -83.387 -84.932  1.00 120.43 ? 125  LEU   C HD23 1 
ATOM   18067 N  N    . THR   C  3  126 ? 22.866  -83.957 -83.723  1.00 92.83  ? 126  THR   C N    1 
ATOM   18068 C  CA   . THR   C  3  126 ? 23.797  -84.915 -83.132  1.00 94.94  ? 126  THR   C CA   1 
ATOM   18069 C  C    . THR   C  3  126 ? 23.590  -85.026 -81.629  1.00 97.58  ? 126  THR   C C    1 
ATOM   18070 O  O    . THR   C  3  126 ? 23.914  -86.059 -81.032  1.00 101.76 ? 126  THR   C O    1 
ATOM   18071 C  CB   . THR   C  3  126 ? 25.250  -84.528 -83.415  1.00 95.10  ? 126  THR   C CB   1 
ATOM   18072 O  OG1  . THR   C  3  126 ? 25.614  -83.391 -82.623  1.00 93.59  ? 126  THR   C OG1  1 
ATOM   18073 C  CG2  . THR   C  3  126 ? 25.443  -84.211 -84.876  1.00 95.99  ? 126  THR   C CG2  1 
ATOM   18074 H  H    . THR   C  3  126 ? 23.214  -83.208 -83.962  1.00 111.43 ? 126  THR   C H    1 
ATOM   18075 H  HA   . THR   C  3  126 ? 23.637  -85.778 -83.546  1.00 113.96 ? 126  THR   C HA   1 
ATOM   18076 H  HB   . THR   C  3  126 ? 25.829  -85.273 -83.189  1.00 114.15 ? 126  THR   C HB   1 
ATOM   18077 H  HG1  . THR   C  3  126 ? 25.065  -82.768 -82.745  1.00 112.35 ? 126  THR   C HG1  1 
ATOM   18078 H  HG21 . THR   C  3  126 ? 26.386  -84.091 -85.068  1.00 115.22 ? 126  THR   C HG21 1 
ATOM   18079 H  HG22 . THR   C  3  126 ? 25.101  -84.936 -85.422  1.00 115.22 ? 126  THR   C HG22 1 
ATOM   18080 H  HG23 . THR   C  3  126 ? 24.970  -83.395 -85.104  1.00 115.22 ? 126  THR   C HG23 1 
ATOM   18081 N  N    . SER   C  3  127 ? 23.064  -83.973 -81.004  1.00 97.29  ? 127  SER   C N    1 
ATOM   18082 C  CA   . SER   C  3  127 ? 22.724  -84.022 -79.591  1.00 97.42  ? 127  SER   C CA   1 
ATOM   18083 C  C    . SER   C  3  127 ? 21.475  -84.846 -79.322  1.00 98.06  ? 127  SER   C C    1 
ATOM   18084 O  O    . SER   C  3  127 ? 21.163  -85.104 -78.154  1.00 103.09 ? 127  SER   C O    1 
ATOM   18085 C  CB   . SER   C  3  127 ? 22.503  -82.606 -79.055  1.00 99.51  ? 127  SER   C CB   1 
ATOM   18086 O  OG   . SER   C  3  127 ? 23.631  -81.781 -79.277  1.00 103.44 ? 127  SER   C OG   1 
ATOM   18087 H  H    . SER   C  3  127 ? 22.896  -83.218 -81.380  1.00 116.79 ? 127  SER   C H    1 
ATOM   18088 H  HA   . SER   C  3  127 ? 23.467  -84.421 -79.112  1.00 116.94 ? 127  SER   C HA   1 
ATOM   18089 H  HB2  . SER   C  3  127 ? 21.738  -82.217 -79.506  1.00 119.45 ? 127  SER   C HB2  1 
ATOM   18090 H  HB3  . SER   C  3  127 ? 22.336  -82.656 -78.101  1.00 119.45 ? 127  SER   C HB3  1 
ATOM   18091 H  HG   . SER   C  3  127 ? 23.482  -81.006 -78.990  1.00 124.17 ? 127  SER   C HG   1 
ATOM   18092 N  N    . GLY   C  3  128 ? 20.765  -85.267 -80.364  1.00 98.59  ? 128  GLY   C N    1 
ATOM   18093 C  CA   . GLY   C  3  128 ? 19.405  -85.732 -80.197  1.00 103.71 ? 128  GLY   C CA   1 
ATOM   18094 C  C    . GLY   C  3  128 ? 18.496  -84.531 -80.040  1.00 106.55 ? 128  GLY   C C    1 
ATOM   18095 O  O    . GLY   C  3  128 ? 18.918  -83.508 -79.491  1.00 107.39 ? 128  GLY   C O    1 
ATOM   18096 H  H    . GLY   C  3  128 ? 21.053  -85.291 -81.174  1.00 118.34 ? 128  GLY   C H    1 
ATOM   18097 H  HA2  . GLY   C  3  128 ? 19.129  -86.245 -80.973  1.00 124.49 ? 128  GLY   C HA2  1 
ATOM   18098 H  HA3  . GLY   C  3  128 ? 19.337  -86.292 -79.408  1.00 124.49 ? 128  GLY   C HA3  1 
ATOM   18099 N  N    . GLY   C  3  129 ? 17.269  -84.626 -80.525  1.00 105.00 ? 129  GLY   C N    1 
ATOM   18100 C  CA   . GLY   C  3  129 ? 16.357  -83.490 -80.452  1.00 102.25 ? 129  GLY   C CA   1 
ATOM   18101 C  C    . GLY   C  3  129 ? 16.558  -82.538 -81.611  1.00 93.16  ? 129  GLY   C C    1 
ATOM   18102 O  O    . GLY   C  3  129 ? 17.641  -82.404 -82.167  1.00 89.54  ? 129  GLY   C O    1 
ATOM   18103 H  H    . GLY   C  3  129 ? 16.940  -85.327 -80.898  1.00 126.04 ? 129  GLY   C H    1 
ATOM   18104 H  HA2  . GLY   C  3  129 ? 15.441  -83.808 -80.469  1.00 122.74 ? 129  GLY   C HA2  1 
ATOM   18105 H  HA3  . GLY   C  3  129 ? 16.507  -83.005 -79.625  1.00 122.74 ? 129  GLY   C HA3  1 
ATOM   18106 N  N    . ALA   C  3  130 ? 15.471  -81.845 -81.975  1.00 90.15  ? 130  ALA   C N    1 
ATOM   18107 C  CA   . ALA   C  3  130 ? 15.462  -81.003 -83.169  1.00 84.74  ? 130  ALA   C CA   1 
ATOM   18108 C  C    . ALA   C  3  130 ? 14.508  -79.843 -82.944  1.00 84.53  ? 130  ALA   C C    1 
ATOM   18109 O  O    . ALA   C  3  130 ? 13.304  -80.059 -82.775  1.00 89.33  ? 130  ALA   C O    1 
ATOM   18110 C  CB   . ALA   C  3  130 ? 15.043  -81.814 -84.395  1.00 83.40  ? 130  ALA   C CB   1 
ATOM   18111 H  H    . ALA   C  3  130 ? 14.727  -81.848 -81.544  1.00 108.21 ? 130  ALA   C H    1 
ATOM   18112 H  HA   . ALA   C  3  130 ? 16.350  -80.640 -83.318  1.00 101.73 ? 130  ALA   C HA   1 
ATOM   18113 H  HB1  . ALA   C  3  130 ? 15.000  -81.224 -85.164  1.00 100.12 ? 130  ALA   C HB1  1 
ATOM   18114 H  HB2  . ALA   C  3  130 ? 15.698  -82.513 -84.550  1.00 100.12 ? 130  ALA   C HB2  1 
ATOM   18115 H  HB3  . ALA   C  3  130 ? 14.172  -82.207 -84.230  1.00 100.12 ? 130  ALA   C HB3  1 
ATOM   18116 N  N    . SER   C  3  131 ? 15.037  -78.623 -82.945  1.00 80.92  ? 131  SER   C N    1 
ATOM   18117 C  CA   . SER   C  3  131 ? 14.231  -77.422 -82.782  1.00 80.63  ? 131  SER   C CA   1 
ATOM   18118 C  C    . SER   C  3  131 ? 14.022  -76.753 -84.134  1.00 84.26  ? 131  SER   C C    1 
ATOM   18119 O  O    . SER   C  3  131 ? 14.986  -76.496 -84.863  1.00 84.57  ? 131  SER   C O    1 
ATOM   18120 C  CB   . SER   C  3  131 ? 14.892  -76.441 -81.811  1.00 76.76  ? 131  SER   C CB   1 
ATOM   18121 O  OG   . SER   C  3  131 ? 14.752  -76.877 -80.471  1.00 77.98  ? 131  SER   C OG   1 
ATOM   18122 H  H    . SER   C  3  131 ? 15.877  -78.465 -83.040  1.00 97.14  ? 131  SER   C H    1 
ATOM   18123 H  HA   . SER   C  3  131 ? 13.364  -77.669 -82.424  1.00 96.79  ? 131  SER   C HA   1 
ATOM   18124 H  HB2  . SER   C  3  131 ? 15.836  -76.376 -82.024  1.00 92.14  ? 131  SER   C HB2  1 
ATOM   18125 H  HB3  . SER   C  3  131 ? 14.470  -75.573 -81.905  1.00 92.14  ? 131  SER   C HB3  1 
ATOM   18126 H  HG   . SER   C  3  131 ? 14.947  -77.692 -80.412  1.00 93.61  ? 131  SER   C HG   1 
ATOM   18127 N  N    . VAL   C  3  132 ? 12.764  -76.481 -84.463  1.00 85.97  ? 132  VAL   C N    1 
ATOM   18128 C  CA   . VAL   C  3  132 ? 12.400  -75.695 -85.636  1.00 87.57  ? 132  VAL   C CA   1 
ATOM   18129 C  C    . VAL   C  3  132 ? 12.002  -74.311 -85.144  1.00 88.40  ? 132  VAL   C C    1 
ATOM   18130 O  O    . VAL   C  3  132 ? 11.083  -74.176 -84.327  1.00 92.06  ? 132  VAL   C O    1 
ATOM   18131 C  CB   . VAL   C  3  132 ? 11.258  -76.352 -86.427  1.00 92.01  ? 132  VAL   C CB   1 
ATOM   18132 C  CG1  . VAL   C  3  132 ? 11.028  -75.611 -87.737  1.00 93.68  ? 132  VAL   C CG1  1 
ATOM   18133 C  CG2  . VAL   C  3  132 ? 11.559  -77.822 -86.681  1.00 91.65  ? 132  VAL   C CG2  1 
ATOM   18134 H  H    . VAL   C  3  132 ? 12.084  -76.749 -84.010  1.00 103.20 ? 132  VAL   C H    1 
ATOM   18135 H  HA   . VAL   C  3  132 ? 13.164  -75.615 -86.228  1.00 105.12 ? 132  VAL   C HA   1 
ATOM   18136 H  HB   . VAL   C  3  132 ? 10.443  -76.301 -85.904  1.00 110.45 ? 132  VAL   C HB   1 
ATOM   18137 H  HG11 . VAL   C  3  132 ? 10.310  -76.046 -88.223  1.00 112.45 ? 132  VAL   C HG11 1 
ATOM   18138 H  HG12 . VAL   C  3  132 ? 10.786  -74.692 -87.542  1.00 112.45 ? 132  VAL   C HG12 1 
ATOM   18139 H  HG13 . VAL   C  3  132 ? 11.844  -75.635 -88.261  1.00 112.45 ? 132  VAL   C HG13 1 
ATOM   18140 H  HG21 . VAL   C  3  132 ? 10.832  -78.209 -87.195  1.00 110.02 ? 132  VAL   C HG21 1 
ATOM   18141 H  HG22 . VAL   C  3  132 ? 12.389  -77.894 -87.176  1.00 110.02 ? 132  VAL   C HG22 1 
ATOM   18142 H  HG23 . VAL   C  3  132 ? 11.641  -78.280 -85.829  1.00 110.02 ? 132  VAL   C HG23 1 
ATOM   18143 N  N    . VAL   C  3  133 ? 12.691  -73.284 -85.632  1.00 84.61  ? 133  VAL   C N    1 
ATOM   18144 C  CA   . VAL   C  3  133 ? 12.511  -71.918 -85.159  1.00 83.64  ? 133  VAL   C CA   1 
ATOM   18145 C  C    . VAL   C  3  133 ? 11.891  -71.085 -86.271  1.00 84.14  ? 133  VAL   C C    1 
ATOM   18146 O  O    . VAL   C  3  133 ? 12.266  -71.211 -87.442  1.00 81.59  ? 133  VAL   C O    1 
ATOM   18147 C  CB   . VAL   C  3  133 ? 13.846  -71.304 -84.693  1.00 81.14  ? 133  VAL   C CB   1 
ATOM   18148 C  CG1  . VAL   C  3  133 ? 13.650  -69.857 -84.264  1.00 81.25  ? 133  VAL   C CG1  1 
ATOM   18149 C  CG2  . VAL   C  3  133 ? 14.434  -72.127 -83.556  1.00 78.12  ? 133  VAL   C CG2  1 
ATOM   18150 H  H    . VAL   C  3  133 ? 13.282  -73.357 -86.253  1.00 101.57 ? 133  VAL   C H    1 
ATOM   18151 H  HA   . VAL   C  3  133 ? 11.897  -71.922 -84.409  1.00 100.41 ? 133  VAL   C HA   1 
ATOM   18152 H  HB   . VAL   C  3  133 ? 14.474  -71.314 -85.433  1.00 97.40  ? 133  VAL   C HB   1 
ATOM   18153 H  HG11 . VAL   C  3  133 ? 14.491  -69.510 -83.927  1.00 97.54  ? 133  VAL   C HG11 1 
ATOM   18154 H  HG12 . VAL   C  3  133 ? 13.361  -69.336 -85.030  1.00 97.54  ? 133  VAL   C HG12 1 
ATOM   18155 H  HG13 . VAL   C  3  133 ? 12.976  -69.822 -83.567  1.00 97.54  ? 133  VAL   C HG13 1 
ATOM   18156 H  HG21 . VAL   C  3  133 ? 15.224  -71.678 -83.217  1.00 93.78  ? 133  VAL   C HG21 1 
ATOM   18157 H  HG22 . VAL   C  3  133 ? 13.772  -72.209 -82.851  1.00 93.78  ? 133  VAL   C HG22 1 
ATOM   18158 H  HG23 . VAL   C  3  133 ? 14.671  -73.005 -83.891  1.00 93.78  ? 133  VAL   C HG23 1 
ATOM   18159 N  N    . CYS   C  3  134 ? 10.940  -70.230 -85.896  1.00 85.76  ? 134  CYS   C N    1 
ATOM   18160 C  CA   . CYS   C  3  134 ? 10.276  -69.324 -86.824  1.00 84.99  ? 134  CYS   C CA   1 
ATOM   18161 C  C    . CYS   C  3  134 ? 10.308  -67.918 -86.243  1.00 80.95  ? 134  CYS   C C    1 
ATOM   18162 O  O    . CYS   C  3  134 ? 9.961   -67.720 -85.074  1.00 77.35  ? 134  CYS   C O    1 
ATOM   18163 C  CB   . CYS   C  3  134 ? 8.832   -69.762 -87.083  1.00 89.36  ? 134  CYS   C CB   1 
ATOM   18164 S  SG   . CYS   C  3  134 ? 8.069   -68.977 -88.519  1.00 94.94  ? 134  CYS   C SG   1 
ATOM   18165 H  H    . CYS   C  3  134 ? 10.657  -70.157 -85.088  1.00 102.95 ? 134  CYS   C H    1 
ATOM   18166 H  HA   . CYS   C  3  134 ? 10.748  -69.317 -87.671  1.00 102.02 ? 134  CYS   C HA   1 
ATOM   18167 H  HB2  . CYS   C  3  134 ? 8.820   -70.721 -87.231  1.00 107.27 ? 134  CYS   C HB2  1 
ATOM   18168 H  HB3  . CYS   C  3  134 ? 8.296   -69.540 -86.306  1.00 107.27 ? 134  CYS   C HB3  1 
ATOM   18169 N  N    . PHE   C  3  135 ? 10.721  -66.948 -87.056  1.00 82.92  ? 135  PHE   C N    1 
ATOM   18170 C  CA   . PHE   C  3  135 ? 10.845  -65.558 -86.636  1.00 85.54  ? 135  PHE   C CA   1 
ATOM   18171 C  C    . PHE   C  3  135 ? 9.830   -64.704 -87.384  1.00 91.36  ? 135  PHE   C C    1 
ATOM   18172 O  O    . PHE   C  3  135 ? 9.839   -64.666 -88.618  1.00 93.68  ? 135  PHE   C O    1 
ATOM   18173 C  CB   . PHE   C  3  135 ? 12.255  -65.025 -86.899  1.00 84.07  ? 135  PHE   C CB   1 
ATOM   18174 C  CG   . PHE   C  3  135 ? 13.298  -65.532 -85.943  1.00 81.15  ? 135  PHE   C CG   1 
ATOM   18175 C  CD1  . PHE   C  3  135 ? 13.059  -65.578 -84.579  1.00 80.42  ? 135  PHE   C CD1  1 
ATOM   18176 C  CD2  . PHE   C  3  135 ? 14.531  -65.947 -86.415  1.00 78.90  ? 135  PHE   C CD2  1 
ATOM   18177 C  CE1  . PHE   C  3  135 ? 14.028  -66.036 -83.708  1.00 80.31  ? 135  PHE   C CE1  1 
ATOM   18178 C  CE2  . PHE   C  3  135 ? 15.502  -66.406 -85.551  1.00 75.61  ? 135  PHE   C CE2  1 
ATOM   18179 C  CZ   . PHE   C  3  135 ? 15.251  -66.451 -84.195  1.00 76.19  ? 135  PHE   C CZ   1 
ATOM   18180 H  H    . PHE   C  3  135 ? 10.940  -67.077 -87.878  1.00 99.54  ? 135  PHE   C H    1 
ATOM   18181 H  HA   . PHE   C  3  135 ? 10.656  -65.507 -85.686  1.00 102.69 ? 135  PHE   C HA   1 
ATOM   18182 H  HB2  . PHE   C  3  135 ? 12.524  -65.289 -87.793  1.00 100.92 ? 135  PHE   C HB2  1 
ATOM   18183 H  HB3  . PHE   C  3  135 ? 12.238  -64.058 -86.829  1.00 100.92 ? 135  PHE   C HB3  1 
ATOM   18184 H  HD1  . PHE   C  3  135 ? 12.237  -65.297 -84.247  1.00 96.54  ? 135  PHE   C HD1  1 
ATOM   18185 H  HD2  . PHE   C  3  135 ? 14.707  -65.916 -87.328  1.00 94.72  ? 135  PHE   C HD2  1 
ATOM   18186 H  HE1  . PHE   C  3  135 ? 13.857  -66.066 -82.795  1.00 96.41  ? 135  PHE   C HE1  1 
ATOM   18187 H  HE2  . PHE   C  3  135 ? 16.325  -66.685 -85.881  1.00 90.77  ? 135  PHE   C HE2  1 
ATOM   18188 H  HZ   . PHE   C  3  135 ? 15.905  -66.760 -83.611  1.00 91.46  ? 135  PHE   C HZ   1 
ATOM   18189 N  N    . LEU   C  3  136 ? 8.970   -64.019 -86.635  1.00 92.02  ? 136  LEU   C N    1 
ATOM   18190 C  CA   . LEU   C  3  136 ? 8.082   -62.987 -87.159  1.00 93.47  ? 136  LEU   C CA   1 
ATOM   18191 C  C    . LEU   C  3  136 ? 8.584   -61.644 -86.642  1.00 89.72  ? 136  LEU   C C    1 
ATOM   18192 O  O    . LEU   C  3  136 ? 8.580   -61.415 -85.428  1.00 91.48  ? 136  LEU   C O    1 
ATOM   18193 C  CB   . LEU   C  3  136 ? 6.639   -63.225 -86.711  1.00 97.86  ? 136  LEU   C CB   1 
ATOM   18194 C  CG   . LEU   C  3  136 ? 5.914   -64.507 -87.116  1.00 105.13 ? 136  LEU   C CG   1 
ATOM   18195 C  CD1  . LEU   C  3  136 ? 4.574   -64.622 -86.509  1.00 108.18 ? 136  LEU   C CD1  1 
ATOM   18196 C  CD2  . LEU   C  3  136 ? 5.744   -64.408 -88.517  1.00 116.10 ? 136  LEU   C CD2  1 
ATOM   18197 H  H    . LEU   C  3  136 ? 8.880   -64.139 -85.789  1.00 110.46 ? 136  LEU   C H    1 
ATOM   18198 H  HA   . LEU   C  3  136 ? 8.101   -62.990 -88.129  1.00 112.20 ? 136  LEU   C HA   1 
ATOM   18199 H  HB2  . LEU   C  3  136 ? 6.634   -63.207 -85.741  1.00 117.47 ? 136  LEU   C HB2  1 
ATOM   18200 H  HB3  . LEU   C  3  136 ? 6.106   -62.492 -87.058  1.00 117.47 ? 136  LEU   C HB3  1 
ATOM   18201 H  HG   . LEU   C  3  136 ? 6.421   -65.282 -86.828  1.00 126.19 ? 136  LEU   C HG   1 
ATOM   18202 H  HD11 . LEU   C  3  136 ? 3.907   -64.624 -87.214  1.00 129.85 ? 136  LEU   C HD11 1 
ATOM   18203 H  HD12 . LEU   C  3  136 ? 4.525   -65.449 -86.005  1.00 129.85 ? 136  LEU   C HD12 1 
ATOM   18204 H  HD13 . LEU   C  3  136 ? 4.429   -63.865 -85.919  1.00 129.85 ? 136  LEU   C HD13 1 
ATOM   18205 H  HD21 . LEU   C  3  136 ? 6.183   -65.162 -88.942  1.00 139.36 ? 136  LEU   C HD21 1 
ATOM   18206 H  HD22 . LEU   C  3  136 ? 4.796   -64.418 -88.722  1.00 139.36 ? 136  LEU   C HD22 1 
ATOM   18207 H  HD23 . LEU   C  3  136 ? 6.141   -63.578 -88.826  1.00 139.36 ? 136  LEU   C HD23 1 
ATOM   18208 N  N    . ASN   C  3  137 ? 9.012   -60.760 -87.545  1.00 88.02  ? 137  ASN   C N    1 
ATOM   18209 C  CA   . ASN   C  3  137 ? 9.683   -59.534 -87.135  1.00 84.88  ? 137  ASN   C CA   1 
ATOM   18210 C  C    . ASN   C  3  137 ? 9.018   -58.296 -87.719  1.00 87.88  ? 137  ASN   C C    1 
ATOM   18211 O  O    . ASN   C  3  137 ? 8.487   -58.311 -88.833  1.00 90.83  ? 137  ASN   C O    1 
ATOM   18212 C  CB   . ASN   C  3  137 ? 11.163  -59.548 -87.540  1.00 82.03  ? 137  ASN   C CB   1 
ATOM   18213 C  CG   . ASN   C  3  137 ? 11.911  -60.725 -86.954  1.00 78.16  ? 137  ASN   C CG   1 
ATOM   18214 O  OD1  . ASN   C  3  137 ? 11.653  -61.138 -85.823  1.00 74.54  ? 137  ASN   C OD1  1 
ATOM   18215 N  ND2  . ASN   C  3  137 ? 12.840  -61.278 -87.724  1.00 79.23  ? 137  ASN   C ND2  1 
ATOM   18216 H  H    . ASN   C  3  137 ? 8.924   -60.851 -88.396  1.00 105.66 ? 137  ASN   C H    1 
ATOM   18217 H  HA   . ASN   C  3  137 ? 9.609   -59.464 -86.170  1.00 101.90 ? 137  ASN   C HA   1 
ATOM   18218 H  HB2  . ASN   C  3  137 ? 11.227  -59.601 -88.506  1.00 98.47  ? 137  ASN   C HB2  1 
ATOM   18219 H  HB3  . ASN   C  3  137 ? 11.586  -58.734 -87.223  1.00 98.47  ? 137  ASN   C HB3  1 
ATOM   18220 H  HD21 . ASN   C  3  137 ? 13.293  -61.950 -87.436  1.00 95.12  ? 137  ASN   C HD21 1 
ATOM   18221 H  HD22 . ASN   C  3  137 ? 12.990  -60.964 -88.511  1.00 95.12  ? 137  ASN   C HD22 1 
ATOM   18222 N  N    . ASN   C  3  138 ? 9.068   -57.218 -86.931  1.00 86.54  ? 138  ASN   C N    1 
ATOM   18223 C  CA   . ASN   C  3  138 ? 8.608   -55.889 -87.321  1.00 89.66  ? 138  ASN   C CA   1 
ATOM   18224 C  C    . ASN   C  3  138 ? 7.187   -55.921 -87.862  1.00 94.15  ? 138  ASN   C C    1 
ATOM   18225 O  O    . ASN   C  3  138 ? 6.966   -55.831 -89.074  1.00 99.60  ? 138  ASN   C O    1 
ATOM   18226 C  CB   . ASN   C  3  138 ? 9.573   -55.281 -88.340  1.00 89.83  ? 138  ASN   C CB   1 
ATOM   18227 C  CG   . ASN   C  3  138 ? 11.012  -55.300 -87.855  1.00 90.28  ? 138  ASN   C CG   1 
ATOM   18228 O  OD1  . ASN   C  3  138 ? 11.684  -56.329 -87.923  1.00 89.01  ? 138  ASN   C OD1  1 
ATOM   18229 N  ND2  . ASN   C  3  138 ? 11.486  -54.167 -87.348  1.00 94.27  ? 138  ASN   C ND2  1 
ATOM   18230 H  H    . ASN   C  3  138 ? 9.379   -57.234 -86.130  1.00 103.88 ? 138  ASN   C H    1 
ATOM   18231 H  HA   . ASN   C  3  138 ? 8.595   -55.318 -86.538  1.00 107.63 ? 138  ASN   C HA   1 
ATOM   18232 H  HB2  . ASN   C  3  138 ? 9.526   -55.788 -89.166  1.00 107.83 ? 138  ASN   C HB2  1 
ATOM   18233 H  HB3  . ASN   C  3  138 ? 9.322   -54.358 -88.504  1.00 107.83 ? 138  ASN   C HB3  1 
ATOM   18234 H  HD21 . ASN   C  3  138 ? 12.296  -54.131 -87.060  1.00 113.15 ? 138  ASN   C HD21 1 
ATOM   18235 H  HD22 . ASN   C  3  138 ? 10.983  -53.471 -87.308  1.00 113.15 ? 138  ASN   C HD22 1 
ATOM   18236 N  N    . PHE   C  3  139 ? 6.220   -56.045 -86.955  1.00 94.27  ? 139  PHE   C N    1 
ATOM   18237 C  CA   . PHE   C  3  139 ? 4.806   -56.011 -87.286  1.00 99.23  ? 139  PHE   C CA   1 
ATOM   18238 C  C    . PHE   C  3  139 ? 4.073   -55.180 -86.244  1.00 99.58  ? 139  PHE   C C    1 
ATOM   18239 O  O    . PHE   C  3  139 ? 4.423   -55.202 -85.060  1.00 100.93 ? 139  PHE   C O    1 
ATOM   18240 C  CB   . PHE   C  3  139 ? 4.210   -57.422 -87.335  1.00 97.50  ? 139  PHE   C CB   1 
ATOM   18241 C  CG   . PHE   C  3  139 ? 4.297   -58.156 -86.029  1.00 87.60  ? 139  PHE   C CG   1 
ATOM   18242 C  CD1  . PHE   C  3  139 ? 5.370   -58.988 -85.755  1.00 82.30  ? 139  PHE   C CD1  1 
ATOM   18243 C  CD2  . PHE   C  3  139 ? 3.310   -58.007 -85.069  1.00 84.13  ? 139  PHE   C CD2  1 
ATOM   18244 C  CE1  . PHE   C  3  139 ? 5.453   -59.660 -84.552  1.00 76.61  ? 139  PHE   C CE1  1 
ATOM   18245 C  CE2  . PHE   C  3  139 ? 3.389   -58.673 -83.865  1.00 78.80  ? 139  PHE   C CE2  1 
ATOM   18246 C  CZ   . PHE   C  3  139 ? 4.461   -59.502 -83.605  1.00 76.32  ? 139  PHE   C CZ   1 
ATOM   18247 H  H    . PHE   C  3  139 ? 6.368   -56.154 -86.115  1.00 113.16 ? 139  PHE   C H    1 
ATOM   18248 H  HA   . PHE   C  3  139 ? 4.682   -55.597 -88.154  1.00 119.11 ? 139  PHE   C HA   1 
ATOM   18249 H  HB2  . PHE   C  3  139 ? 3.273   -57.357 -87.578  1.00 117.04 ? 139  PHE   C HB2  1 
ATOM   18250 H  HB3  . PHE   C  3  139 ? 4.690   -57.941 -88.000  1.00 117.04 ? 139  PHE   C HB3  1 
ATOM   18251 H  HD1  . PHE   C  3  139 ? 6.042   -59.094 -86.389  1.00 98.79  ? 139  PHE   C HD1  1 
ATOM   18252 H  HD2  . PHE   C  3  139 ? 2.584   -57.450 -85.240  1.00 101.00 ? 139  PHE   C HD2  1 
ATOM   18253 H  HE1  . PHE   C  3  139 ? 6.176   -60.218 -84.379  1.00 91.97  ? 139  PHE   C HE1  1 
ATOM   18254 H  HE2  . PHE   C  3  139 ? 2.720   -58.564 -83.228  1.00 94.60  ? 139  PHE   C HE2  1 
ATOM   18255 H  HZ   . PHE   C  3  139 ? 4.515   -59.954 -82.794  1.00 91.62  ? 139  PHE   C HZ   1 
ATOM   18256 N  N    . TYR   C  3  140 ? 3.057   -54.451 -86.694  1.00 91.62  ? 140  TYR   C N    1 
ATOM   18257 C  CA   . TYR   C  3  140 ? 2.175   -53.682 -85.834  1.00 91.59  ? 140  TYR   C CA   1 
ATOM   18258 C  C    . TYR   C  3  140 ? 0.738   -54.066 -86.158  1.00 98.21  ? 140  TYR   C C    1 
ATOM   18259 O  O    . TYR   C  3  140 ? 0.391   -54.186 -87.339  1.00 98.09  ? 140  TYR   C O    1 
ATOM   18260 C  CB   . TYR   C  3  140 ? 2.381   -52.175 -86.050  1.00 91.24  ? 140  TYR   C CB   1 
ATOM   18261 C  CG   . TYR   C  3  140 ? 1.634   -51.312 -85.062  1.00 94.87  ? 140  TYR   C CG   1 
ATOM   18262 C  CD1  . TYR   C  3  140 ? 0.297   -50.997 -85.258  1.00 97.72  ? 140  TYR   C CD1  1 
ATOM   18263 C  CD2  . TYR   C  3  140 ? 2.267   -50.814 -83.931  1.00 94.67  ? 140  TYR   C CD2  1 
ATOM   18264 C  CE1  . TYR   C  3  140 ? -0.391  -50.212 -84.356  1.00 102.70 ? 140  TYR   C CE1  1 
ATOM   18265 C  CE2  . TYR   C  3  140 ? 1.588   -50.027 -83.023  1.00 98.98  ? 140  TYR   C CE2  1 
ATOM   18266 C  CZ   . TYR   C  3  140 ? 0.258   -49.731 -83.240  1.00 103.89 ? 140  TYR   C CZ   1 
ATOM   18267 O  OH   . TYR   C  3  140 ? -0.427  -48.949 -82.340  1.00 109.49 ? 140  TYR   C OH   1 
ATOM   18268 H  H    . TYR   C  3  140 ? 2.853   -54.385 -87.527  1.00 109.98 ? 140  TYR   C H    1 
ATOM   18269 H  HA   . TYR   C  3  140 ? 2.354   -53.873 -84.900  1.00 109.94 ? 140  TYR   C HA   1 
ATOM   18270 H  HB2  . TYR   C  3  140 ? 3.326   -51.973 -85.964  1.00 109.53 ? 140  TYR   C HB2  1 
ATOM   18271 H  HB3  . TYR   C  3  140 ? 2.071   -51.942 -86.939  1.00 109.53 ? 140  TYR   C HB3  1 
ATOM   18272 H  HD1  . TYR   C  3  140 ? -0.143  -51.321 -86.010  1.00 117.30 ? 140  TYR   C HD1  1 
ATOM   18273 H  HD2  . TYR   C  3  140 ? 3.164   -51.013 -83.783  1.00 113.64 ? 140  TYR   C HD2  1 
ATOM   18274 H  HE1  . TYR   C  3  140 ? -1.287  -50.009 -84.500  1.00 123.27 ? 140  TYR   C HE1  1 
ATOM   18275 H  HE2  . TYR   C  3  140 ? 2.024   -49.699 -82.269  1.00 118.81 ? 140  TYR   C HE2  1 
ATOM   18276 H  HH   . TYR   C  3  140 ? -0.090  -49.028 -81.575  1.00 131.43 ? 140  TYR   C HH   1 
ATOM   18277 N  N    . PRO   C  3  141 ? -0.131  -54.268 -85.147  1.00 105.03 ? 141  PRO   C N    1 
ATOM   18278 C  CA   . PRO   C  3  141 ? -0.002  -54.247 -83.681  1.00 108.26 ? 141  PRO   C CA   1 
ATOM   18279 C  C    . PRO   C  3  141 ? 0.520   -55.541 -83.037  1.00 109.62 ? 141  PRO   C C    1 
ATOM   18280 O  O    . PRO   C  3  141 ? 0.885   -56.488 -83.734  1.00 109.39 ? 141  PRO   C O    1 
ATOM   18281 C  CB   . PRO   C  3  141 ? -1.445  -53.984 -83.209  1.00 114.47 ? 141  PRO   C CB   1 
ATOM   18282 C  CG   . PRO   C  3  141 ? -2.186  -53.515 -84.420  1.00 114.99 ? 141  PRO   C CG   1 
ATOM   18283 C  CD   . PRO   C  3  141 ? -1.545  -54.231 -85.553  1.00 108.12 ? 141  PRO   C CD   1 
ATOM   18284 H  HA   . PRO   C  3  141 ? 0.595   -53.524 -83.435  1.00 129.94 ? 141  PRO   C HA   1 
ATOM   18285 H  HB2  . PRO   C  3  141 ? -1.832  -54.804 -82.865  1.00 137.40 ? 141  PRO   C HB2  1 
ATOM   18286 H  HB3  . PRO   C  3  141 ? -1.445  -53.302 -82.520  1.00 137.40 ? 141  PRO   C HB3  1 
ATOM   18287 H  HG2  . PRO   C  3  141 ? -3.124  -53.749 -84.347  1.00 138.03 ? 141  PRO   C HG2  1 
ATOM   18288 H  HG3  . PRO   C  3  141 ? -2.090  -52.555 -84.517  1.00 138.03 ? 141  PRO   C HG3  1 
ATOM   18289 H  HD2  . PRO   C  3  141 ? -1.904  -55.127 -85.646  1.00 129.78 ? 141  PRO   C HD2  1 
ATOM   18290 H  HD3  . PRO   C  3  141 ? -1.657  -53.741 -86.382  1.00 129.78 ? 141  PRO   C HD3  1 
ATOM   18291 N  N    . LYS   C  3  142 ? 0.530   -55.566 -81.698  1.00 113.89 ? 142  LYS   C N    1 
ATOM   18292 C  CA   . LYS   C  3  142 ? 1.140   -56.674 -80.965  1.00 113.67 ? 142  LYS   C CA   1 
ATOM   18293 C  C    . LYS   C  3  142 ? 0.330   -57.962 -81.068  1.00 116.81 ? 142  LYS   C C    1 
ATOM   18294 O  O    . LYS   C  3  142 ? 0.901   -59.054 -80.966  1.00 111.65 ? 142  LYS   C O    1 
ATOM   18295 C  CB   . LYS   C  3  142 ? 1.325   -56.285 -79.494  1.00 120.07 ? 142  LYS   C CB   1 
ATOM   18296 C  CG   . LYS   C  3  142 ? 1.533   -57.471 -78.551  1.00 121.16 ? 142  LYS   C CG   1 
ATOM   18297 C  CD   . LYS   C  3  142 ? 2.417   -57.124 -77.360  1.00 120.91 ? 142  LYS   C CD   1 
ATOM   18298 C  CE   . LYS   C  3  142 ? 3.477   -58.194 -77.152  1.00 117.94 ? 142  LYS   C CE   1 
ATOM   18299 N  NZ   . LYS   C  3  142 ? 4.297   -57.950 -75.936  1.00 119.08 ? 142  LYS   C NZ   1 
ATOM   18300 H  H    . LYS   C  3  142 ? 0.192   -54.955 -81.195  1.00 136.70 ? 142  LYS   C H    1 
ATOM   18301 H  HA   . LYS   C  3  142 ? 2.012   -56.848 -81.353  1.00 136.45 ? 142  LYS   C HA   1 
ATOM   18302 H  HB2  . LYS   C  3  142 ? 2.104   -55.712 -79.420  1.00 144.12 ? 142  LYS   C HB2  1 
ATOM   18303 H  HB3  . LYS   C  3  142 ? 0.534   -55.809 -79.197  1.00 144.12 ? 142  LYS   C HB3  1 
ATOM   18304 H  HG2  . LYS   C  3  142 ? 0.672   -57.761 -78.211  1.00 145.43 ? 142  LYS   C HG2  1 
ATOM   18305 H  HG3  . LYS   C  3  142 ? 1.958   -58.194 -79.039  1.00 145.43 ? 142  LYS   C HG3  1 
ATOM   18306 H  HD2  . LYS   C  3  142 ? 2.861   -56.277 -77.521  1.00 145.13 ? 142  LYS   C HD2  1 
ATOM   18307 H  HD3  . LYS   C  3  142 ? 1.874   -57.067 -76.558  1.00 145.13 ? 142  LYS   C HD3  1 
ATOM   18308 H  HE2  . LYS   C  3  142 ? 3.044   -59.057 -77.056  1.00 141.57 ? 142  LYS   C HE2  1 
ATOM   18309 H  HE3  . LYS   C  3  142 ? 4.072   -58.206 -77.919  1.00 141.57 ? 142  LYS   C HE3  1 
ATOM   18310 H  HZ1  . LYS   C  3  142 ? 4.797   -58.665 -75.758  1.00 142.93 ? 142  LYS   C HZ1  1 
ATOM   18311 H  HZ2  . LYS   C  3  142 ? 4.831   -57.250 -76.064  1.00 142.93 ? 142  LYS   C HZ2  1 
ATOM   18312 H  HZ3  . LYS   C  3  142 ? 3.767   -57.787 -75.240  1.00 142.93 ? 142  LYS   C HZ3  1 
ATOM   18313 N  N    . ASP   C  3  143 ? -0.984  -57.871 -81.261  1.00 116.78 ? 143  ASP   C N    1 
ATOM   18314 C  CA   . ASP   C  3  143 ? -1.806  -59.074 -81.305  1.00 119.50 ? 143  ASP   C CA   1 
ATOM   18315 C  C    . ASP   C  3  143 ? -1.363  -59.968 -82.456  1.00 117.23 ? 143  ASP   C C    1 
ATOM   18316 O  O    . ASP   C  3  143 ? -1.292  -59.527 -83.606  1.00 117.22 ? 143  ASP   C O    1 
ATOM   18317 C  CB   . ASP   C  3  143 ? -3.280  -58.711 -81.469  1.00 128.31 ? 143  ASP   C CB   1 
ATOM   18318 C  CG   . ASP   C  3  143 ? -3.731  -57.645 -80.493  1.00 132.30 ? 143  ASP   C CG   1 
ATOM   18319 O  OD1  . ASP   C  3  143 ? -3.805  -57.938 -79.281  1.00 132.91 ? 143  ASP   C OD1  1 
ATOM   18320 O  OD2  . ASP   C  3  143 ? -4.001  -56.509 -80.938  1.00 134.03 ? 143  ASP   C OD2  1 
ATOM   18321 H  H    . ASP   C  3  143 ? -1.417  -57.135 -81.367  1.00 140.17 ? 143  ASP   C H    1 
ATOM   18322 H  HA   . ASP   C  3  143 ? -1.705  -59.559 -80.471  1.00 143.44 ? 143  ASP   C HA   1 
ATOM   18323 H  HB2  . ASP   C  3  143 ? -3.426  -58.375 -82.367  1.00 154.01 ? 143  ASP   C HB2  1 
ATOM   18324 H  HB3  . ASP   C  3  143 ? -3.820  -59.502 -81.319  1.00 154.01 ? 143  ASP   C HB3  1 
ATOM   18325 N  N    . ILE   C  3  144 ? -1.068  -61.230 -82.145  1.00 115.07 ? 144  ILE   C N    1 
ATOM   18326 C  CA   . ILE   C  3  144 ? -0.594  -62.173 -83.149  1.00 113.37 ? 144  ILE   C CA   1 
ATOM   18327 C  C    . ILE   C  3  144 ? -0.872  -63.584 -82.660  1.00 115.07 ? 144  ILE   C C    1 
ATOM   18328 O  O    . ILE   C  3  144 ? -0.958  -63.831 -81.456  1.00 117.38 ? 144  ILE   C O    1 
ATOM   18329 C  CB   . ILE   C  3  144 ? 0.913   -61.966 -83.437  1.00 112.31 ? 144  ILE   C CB   1 
ATOM   18330 C  CG1  . ILE   C  3  144 ? 1.344   -62.850 -84.594  1.00 117.91 ? 144  ILE   C CG1  1 
ATOM   18331 C  CG2  . ILE   C  3  144 ? 1.747   -62.291 -82.204  1.00 109.64 ? 144  ILE   C CG2  1 
ATOM   18332 C  CD1  . ILE   C  3  144 ? 2.659   -62.473 -85.117  1.00 118.75 ? 144  ILE   C CD1  1 
ATOM   18333 H  H    . ILE   C  3  144 ? -1.135  -61.563 -81.355  1.00 138.12 ? 144  ILE   C H    1 
ATOM   18334 H  HA   . ILE   C  3  144 ? -1.094  -62.032 -83.968  1.00 136.08 ? 144  ILE   C HA   1 
ATOM   18335 H  HB   . ILE   C  3  144 ? 1.052   -61.035 -83.670  1.00 134.81 ? 144  ILE   C HB   1 
ATOM   18336 H  HG12 . ILE   C  3  144 ? 1.392   -63.770 -84.291  1.00 141.53 ? 144  ILE   C HG12 1 
ATOM   18337 H  HG13 . ILE   C  3  144 ? 0.698   -62.771 -85.313  1.00 141.53 ? 144  ILE   C HG13 1 
ATOM   18338 H  HG21 . ILE   C  3  144 ? 2.647   -61.954 -82.333  1.00 131.61 ? 144  ILE   C HG21 1 
ATOM   18339 H  HG22 . ILE   C  3  144 ? 1.343   -61.869 -81.429  1.00 131.61 ? 144  ILE   C HG22 1 
ATOM   18340 H  HG23 . ILE   C  3  144 ? 1.769   -63.253 -82.083  1.00 131.61 ? 144  ILE   C HG23 1 
ATOM   18341 H  HD11 . ILE   C  3  144 ? 2.755   -62.825 -86.016  1.00 142.54 ? 144  ILE   C HD11 1 
ATOM   18342 H  HD12 . ILE   C  3  144 ? 2.728   -61.505 -85.132  1.00 142.54 ? 144  ILE   C HD12 1 
ATOM   18343 H  HD13 . ILE   C  3  144 ? 3.347   -62.844 -84.542  1.00 142.54 ? 144  ILE   C HD13 1 
ATOM   18344 N  N    . ASN   C  3  145 ? -0.999  -64.515 -83.603  1.00 118.34 ? 145  ASN   C N    1 
ATOM   18345 C  CA   . ASN   C  3  145 ? -1.164  -65.926 -83.284  1.00 122.02 ? 145  ASN   C CA   1 
ATOM   18346 C  C    . ASN   C  3  145 ? -0.367  -66.762 -84.272  1.00 123.71 ? 145  ASN   C C    1 
ATOM   18347 O  O    . ASN   C  3  145 ? -0.303  -66.442 -85.463  1.00 125.03 ? 145  ASN   C O    1 
ATOM   18348 C  CB   . ASN   C  3  145 ? -2.641  -66.339 -83.308  1.00 126.57 ? 145  ASN   C CB   1 
ATOM   18349 C  CG   . ASN   C  3  145 ? -3.417  -65.777 -82.133  1.00 132.42 ? 145  ASN   C CG   1 
ATOM   18350 O  OD1  . ASN   C  3  145 ? -2.838  -65.429 -81.106  1.00 133.16 ? 145  ASN   C OD1  1 
ATOM   18351 N  ND2  . ASN   C  3  145 ? -4.734  -65.691 -82.277  1.00 137.43 ? 145  ASN   C ND2  1 
ATOM   18352 H  H    . ASN   C  3  145 ? -0.992  -64.350 -84.447  1.00 142.04 ? 145  ASN   C H    1 
ATOM   18353 H  HA   . ASN   C  3  145 ? -0.819  -66.101 -82.394  1.00 146.46 ? 145  ASN   C HA   1 
ATOM   18354 H  HB2  . ASN   C  3  145 ? -3.049  -66.010 -84.124  1.00 151.92 ? 145  ASN   C HB2  1 
ATOM   18355 H  HB3  . ASN   C  3  145 ? -2.700  -67.306 -83.273  1.00 151.92 ? 145  ASN   C HB3  1 
ATOM   18356 H  HD21 . ASN   C  3  145 ? -5.217  -65.379 -81.638  1.00 164.96 ? 145  ASN   C HD21 1 
ATOM   18357 H  HD22 . ASN   C  3  145 ? -5.104  -65.948 -83.009  1.00 164.96 ? 145  ASN   C HD22 1 
ATOM   18358 N  N    . VAL   C  3  146 ? 0.243   -67.831 -83.765  1.00 120.73 ? 146  VAL   C N    1 
ATOM   18359 C  CA   . VAL   C  3  146 ? 1.067   -68.731 -84.559  1.00 116.76 ? 146  VAL   C CA   1 
ATOM   18360 C  C    . VAL   C  3  146 ? 0.576   -70.153 -84.345  1.00 117.94 ? 146  VAL   C C    1 
ATOM   18361 O  O    . VAL   C  3  146 ? 0.159   -70.518 -83.239  1.00 121.17 ? 146  VAL   C O    1 
ATOM   18362 C  CB   . VAL   C  3  146 ? 2.562   -68.618 -84.190  1.00 112.51 ? 146  VAL   C CB   1 
ATOM   18363 C  CG1  . VAL   C  3  146 ? 3.094   -67.236 -84.534  1.00 109.75 ? 146  VAL   C CG1  1 
ATOM   18364 C  CG2  . VAL   C  3  146 ? 2.773   -68.928 -82.712  1.00 112.09 ? 146  VAL   C CG2  1 
ATOM   18365 H  H    . VAL   C  3  146 ? 0.191   -68.061 -82.938  1.00 144.92 ? 146  VAL   C H    1 
ATOM   18366 H  HA   . VAL   C  3  146 ? 0.967   -68.506 -85.498  1.00 140.15 ? 146  VAL   C HA   1 
ATOM   18367 H  HB   . VAL   C  3  146 ? 3.063   -69.268 -84.707  1.00 135.05 ? 146  VAL   C HB   1 
ATOM   18368 H  HG11 . VAL   C  3  146 ? 4.019   -67.173 -84.247  1.00 131.74 ? 146  VAL   C HG11 1 
ATOM   18369 H  HG12 . VAL   C  3  146 ? 3.036   -67.104 -85.493  1.00 131.74 ? 146  VAL   C HG12 1 
ATOM   18370 H  HG13 . VAL   C  3  146 ? 2.560   -66.569 -84.075  1.00 131.74 ? 146  VAL   C HG13 1 
ATOM   18371 H  HG21 . VAL   C  3  146 ? 3.717   -68.845 -82.503  1.00 134.55 ? 146  VAL   C HG21 1 
ATOM   18372 H  HG22 . VAL   C  3  146 ? 2.260   -68.299 -82.181  1.00 134.55 ? 146  VAL   C HG22 1 
ATOM   18373 H  HG23 . VAL   C  3  146 ? 2.474   -69.833 -82.534  1.00 134.55 ? 146  VAL   C HG23 1 
ATOM   18374 N  N    . LYS   C  3  147 ? 0.631   -70.956 -85.403  1.00 117.61 ? 147  LYS   C N    1 
ATOM   18375 C  CA   . LYS   C  3  147 ? 0.237   -72.355 -85.359  1.00 119.26 ? 147  LYS   C CA   1 
ATOM   18376 C  C    . LYS   C  3  147 ? 1.276   -73.167 -86.114  1.00 118.76 ? 147  LYS   C C    1 
ATOM   18377 O  O    . LYS   C  3  147 ? 1.735   -72.756 -87.183  1.00 115.20 ? 147  LYS   C O    1 
ATOM   18378 C  CB   . LYS   C  3  147 ? -1.153  -72.561 -85.972  1.00 123.03 ? 147  LYS   C CB   1 
ATOM   18379 C  CG   . LYS   C  3  147 ? -2.247  -72.841 -84.954  1.00 127.13 ? 147  LYS   C CG   1 
ATOM   18380 C  CD   . LYS   C  3  147 ? -3.624  -72.486 -85.498  1.00 133.83 ? 147  LYS   C CD   1 
ATOM   18381 C  CE   . LYS   C  3  147 ? -4.720  -72.804 -84.491  1.00 140.39 ? 147  LYS   C CE   1 
ATOM   18382 N  NZ   . LYS   C  3  147 ? -5.919  -71.932 -84.660  1.00 146.59 ? 147  LYS   C NZ   1 
ATOM   18383 H  H    . LYS   C  3  147 ? 0.902   -70.703 -86.179  1.00 141.17 ? 147  LYS   C H    1 
ATOM   18384 H  HA   . LYS   C  3  147 ? 0.204   -72.670 -84.443  1.00 143.15 ? 147  LYS   C HA   1 
ATOM   18385 H  HB2  . LYS   C  3  147 ? -1.401  -71.758 -86.457  1.00 147.67 ? 147  LYS   C HB2  1 
ATOM   18386 H  HB3  . LYS   C  3  147 ? -1.116  -73.317 -86.579  1.00 147.67 ? 147  LYS   C HB3  1 
ATOM   18387 H  HG2  . LYS   C  3  147 ? -2.243  -73.785 -84.729  1.00 152.59 ? 147  LYS   C HG2  1 
ATOM   18388 H  HG3  . LYS   C  3  147 ? -2.088  -72.310 -84.158  1.00 152.59 ? 147  LYS   C HG3  1 
ATOM   18389 H  HD2  . LYS   C  3  147 ? -3.656  -71.536 -85.695  1.00 160.63 ? 147  LYS   C HD2  1 
ATOM   18390 H  HD3  . LYS   C  3  147 ? -3.793  -72.998 -86.304  1.00 160.63 ? 147  LYS   C HD3  1 
ATOM   18391 H  HE2  . LYS   C  3  147 ? -4.999  -73.725 -84.606  1.00 168.50 ? 147  LYS   C HE2  1 
ATOM   18392 H  HE3  . LYS   C  3  147 ? -4.376  -72.671 -83.594  1.00 168.50 ? 147  LYS   C HE3  1 
ATOM   18393 H  HZ1  . LYS   C  3  147 ? -6.503  -72.088 -84.007  1.00 175.94 ? 147  LYS   C HZ1  1 
ATOM   18394 H  HZ2  . LYS   C  3  147 ? -5.678  -71.076 -84.634  1.00 175.94 ? 147  LYS   C HZ2  1 
ATOM   18395 H  HZ3  . LYS   C  3  147 ? -6.309  -72.100 -85.442  1.00 175.94 ? 147  LYS   C HZ3  1 
ATOM   18396 N  N    . TRP   C  3  148 ? 1.652   -74.312 -85.552  1.00 118.51 ? 148  TRP   C N    1 
ATOM   18397 C  CA   . TRP   C  3  148 ? 2.666   -75.176 -86.143  1.00 117.19 ? 148  TRP   C CA   1 
ATOM   18398 C  C    . TRP   C  3  148 ? 1.980   -76.341 -86.844  1.00 122.52 ? 148  TRP   C C    1 
ATOM   18399 O  O    . TRP   C  3  148 ? 1.214   -77.084 -86.221  1.00 128.86 ? 148  TRP   C O    1 
ATOM   18400 C  CB   . TRP   C  3  148 ? 3.645   -75.679 -85.082  1.00 111.33 ? 148  TRP   C CB   1 
ATOM   18401 C  CG   . TRP   C  3  148 ? 4.665   -74.653 -84.671  1.00 99.69  ? 148  TRP   C CG   1 
ATOM   18402 C  CD1  . TRP   C  3  148 ? 4.559   -73.754 -83.649  1.00 93.79  ? 148  TRP   C CD1  1 
ATOM   18403 C  CD2  . TRP   C  3  148 ? 5.946   -74.423 -85.275  1.00 93.48  ? 148  TRP   C CD2  1 
ATOM   18404 N  NE1  . TRP   C  3  148 ? 5.693   -72.981 -83.579  1.00 87.14  ? 148  TRP   C NE1  1 
ATOM   18405 C  CE2  . TRP   C  3  148 ? 6.560   -73.371 -84.566  1.00 87.39  ? 148  TRP   C CE2  1 
ATOM   18406 C  CE3  . TRP   C  3  148 ? 6.633   -75.005 -86.346  1.00 93.39  ? 148  TRP   C CE3  1 
ATOM   18407 C  CZ2  . TRP   C  3  148 ? 7.826   -72.888 -84.893  1.00 85.76  ? 148  TRP   C CZ2  1 
ATOM   18408 C  CZ3  . TRP   C  3  148 ? 7.891   -74.523 -86.669  1.00 89.92  ? 148  TRP   C CZ3  1 
ATOM   18409 C  CH2  . TRP   C  3  148 ? 8.473   -73.476 -85.944  1.00 86.59  ? 148  TRP   C CH2  1 
ATOM   18410 H  H    . TRP   C  3  148 ? 1.328   -74.615 -84.816  1.00 142.25 ? 148  TRP   C H    1 
ATOM   18411 H  HA   . TRP   C  3  148 ? 3.170   -74.675 -86.804  1.00 140.66 ? 148  TRP   C HA   1 
ATOM   18412 H  HB2  . TRP   C  3  148 ? 3.145   -75.934 -84.291  1.00 133.64 ? 148  TRP   C HB2  1 
ATOM   18413 H  HB3  . TRP   C  3  148 ? 4.121   -76.447 -85.436  1.00 133.64 ? 148  TRP   C HB3  1 
ATOM   18414 H  HD1  . TRP   C  3  148 ? 3.826   -73.677 -83.082  1.00 112.59 ? 148  TRP   C HD1  1 
ATOM   18415 H  HE1  . TRP   C  3  148 ? 5.836   -72.354 -83.008  1.00 104.60 ? 148  TRP   C HE1  1 
ATOM   18416 H  HE3  . TRP   C  3  148 ? 6.252   -75.700 -86.832  1.00 112.10 ? 148  TRP   C HE3  1 
ATOM   18417 H  HZ2  . TRP   C  3  148 ? 8.216   -72.193 -84.413  1.00 102.94 ? 148  TRP   C HZ2  1 
ATOM   18418 H  HZ3  . TRP   C  3  148 ? 8.357   -74.902 -87.379  1.00 107.94 ? 148  TRP   C HZ3  1 
ATOM   18419 H  HH2  . TRP   C  3  148 ? 9.319   -73.173 -86.184  1.00 103.94 ? 148  TRP   C HH2  1 
ATOM   18420 N  N    . LYS   C  3  149 ? 2.256   -76.491 -88.137  1.00 125.73 ? 149  LYS   C N    1 
ATOM   18421 C  CA   . LYS   C  3  149 ? 1.676   -77.539 -88.967  1.00 132.43 ? 149  LYS   C CA   1 
ATOM   18422 C  C    . LYS   C  3  149 ? 2.809   -78.390 -89.517  1.00 135.11 ? 149  LYS   C C    1 
ATOM   18423 O  O    . LYS   C  3  149 ? 3.728   -77.866 -90.155  1.00 135.95 ? 149  LYS   C O    1 
ATOM   18424 C  CB   . LYS   C  3  149 ? 0.848   -76.933 -90.101  1.00 137.99 ? 149  LYS   C CB   1 
ATOM   18425 C  CG   . LYS   C  3  149 ? 0.104   -77.936 -90.967  1.00 144.37 ? 149  LYS   C CG   1 
ATOM   18426 C  CD   . LYS   C  3  149 ? -0.718  -77.210 -92.027  1.00 148.10 ? 149  LYS   C CD   1 
ATOM   18427 C  CE   . LYS   C  3  149 ? -1.463  -78.173 -92.935  1.00 156.63 ? 149  LYS   C CE   1 
ATOM   18428 N  NZ   . LYS   C  3  149 ? -2.263  -77.469 -93.977  1.00 162.51 ? 149  LYS   C NZ   1 
ATOM   18429 H  H    . LYS   C  3  149 ? 2.795   -75.979 -88.569  1.00 150.92 ? 149  LYS   C H    1 
ATOM   18430 H  HA   . LYS   C  3  149 ? 1.095   -78.106 -88.435  1.00 158.95 ? 149  LYS   C HA   1 
ATOM   18431 H  HB2  . LYS   C  3  149 ? 0.186   -76.339 -89.714  1.00 165.62 ? 149  LYS   C HB2  1 
ATOM   18432 H  HB3  . LYS   C  3  149 ? 1.443   -76.434 -90.682  1.00 165.62 ? 149  LYS   C HB3  1 
ATOM   18433 H  HG2  . LYS   C  3  149 ? 0.740   -78.518 -91.413  1.00 173.28 ? 149  LYS   C HG2  1 
ATOM   18434 H  HG3  . LYS   C  3  149 ? -0.496  -78.462 -90.416  1.00 173.28 ? 149  LYS   C HG3  1 
ATOM   18435 H  HD2  . LYS   C  3  149 ? -1.370  -76.641 -91.589  1.00 177.76 ? 149  LYS   C HD2  1 
ATOM   18436 H  HD3  . LYS   C  3  149 ? -0.126  -76.674 -92.577  1.00 177.76 ? 149  LYS   C HD3  1 
ATOM   18437 H  HE2  . LYS   C  3  149 ? -0.822  -78.746 -93.384  1.00 187.99 ? 149  LYS   C HE2  1 
ATOM   18438 H  HE3  . LYS   C  3  149 ? -2.070  -78.708 -92.400  1.00 187.99 ? 149  LYS   C HE3  1 
ATOM   18439 H  HZ1  . LYS   C  3  149 ? -1.924  -77.633 -94.783  1.00 195.05 ? 149  LYS   C HZ1  1 
ATOM   18440 H  HZ2  . LYS   C  3  149 ? -3.107  -77.752 -93.955  1.00 195.05 ? 149  LYS   C HZ2  1 
ATOM   18441 H  HZ3  . LYS   C  3  149 ? -2.249  -76.591 -93.830  1.00 195.05 ? 149  LYS   C HZ3  1 
ATOM   18442 N  N    . ILE   C  3  150 ? 2.749   -79.695 -89.266  1.00 133.77 ? 150  ILE   C N    1 
ATOM   18443 C  CA   . ILE   C  3  150 ? 3.789   -80.613 -89.725  1.00 133.13 ? 150  ILE   C CA   1 
ATOM   18444 C  C    . ILE   C  3  150 ? 3.276   -81.256 -91.014  1.00 139.17 ? 150  ILE   C C    1 
ATOM   18445 O  O    . ILE   C  3  150 ? 3.118   -80.558 -92.021  1.00 140.90 ? 150  ILE   C O    1 
ATOM   18446 C  CB   . ILE   C  3  150 ? 4.163   -81.603 -88.608  1.00 130.29 ? 150  ILE   C CB   1 
ATOM   18447 C  CG1  . ILE   C  3  150 ? 4.411   -80.801 -87.318  1.00 124.29 ? 150  ILE   C CG1  1 
ATOM   18448 C  CG2  . ILE   C  3  150 ? 5.426   -82.357 -88.961  1.00 129.51 ? 150  ILE   C CG2  1 
ATOM   18449 C  CD1  . ILE   C  3  150 ? 4.924   -81.588 -86.125  1.00 122.83 ? 150  ILE   C CD1  1 
ATOM   18450 H  H    . ILE   C  3  150 ? 2.114   -80.075 -88.829  1.00 160.56 ? 150  ILE   C H    1 
ATOM   18451 H  HA   . ILE   C  3  150 ? 4.616   -80.158 -89.948  1.00 159.79 ? 150  ILE   C HA   1 
ATOM   18452 H  HB   . ILE   C  3  150 ? 3.439   -82.239 -88.494  1.00 156.39 ? 150  ILE   C HB   1 
ATOM   18453 H  HG12 . ILE   C  3  150 ? 5.068   -80.114 -87.510  1.00 149.18 ? 150  ILE   C HG12 1 
ATOM   18454 H  HG13 . ILE   C  3  150 ? 3.573   -80.392 -87.050  1.00 149.18 ? 150  ILE   C HG13 1 
ATOM   18455 H  HG21 . ILE   C  3  150 ? 5.474   -83.161 -88.422  1.00 155.45 ? 150  ILE   C HG21 1 
ATOM   18456 H  HG22 . ILE   C  3  150 ? 5.401   -82.591 -89.902  1.00 155.45 ? 150  ILE   C HG22 1 
ATOM   18457 H  HG23 . ILE   C  3  150 ? 6.192   -81.791 -88.781  1.00 155.45 ? 150  ILE   C HG23 1 
ATOM   18458 H  HD11 . ILE   C  3  150 ? 4.998   -80.994 -85.362  1.00 147.43 ? 150  ILE   C HD11 1 
ATOM   18459 H  HD12 . ILE   C  3  150 ? 4.300   -82.304 -85.927  1.00 147.43 ? 150  ILE   C HD12 1 
ATOM   18460 H  HD13 . ILE   C  3  150 ? 5.794   -81.959 -86.341  1.00 147.43 ? 150  ILE   C HD13 1 
ATOM   18461 N  N    . ASP   C  3  151 ? 2.993   -82.561 -91.022  1.00 140.94 ? 151  ASP   C N    1 
ATOM   18462 C  CA   . ASP   C  3  151 ? 2.410   -83.177 -92.221  1.00 144.38 ? 151  ASP   C CA   1 
ATOM   18463 C  C    . ASP   C  3  151 ? 0.884   -83.086 -92.154  1.00 146.21 ? 151  ASP   C C    1 
ATOM   18464 O  O    . ASP   C  3  151 ? 0.168   -84.081 -92.029  1.00 150.70 ? 151  ASP   C O    1 
ATOM   18465 C  CB   . ASP   C  3  151 ? 2.852   -84.628 -92.376  1.00 147.26 ? 151  ASP   C CB   1 
ATOM   18466 C  CG   . ASP   C  3  151 ? 4.350   -84.788 -92.403  1.00 140.90 ? 151  ASP   C CG   1 
ATOM   18467 O  OD1  . ASP   C  3  151 ? 5.022   -84.059 -93.160  1.00 137.54 ? 151  ASP   C OD1  1 
ATOM   18468 O  OD2  . ASP   C  3  151 ? 4.850   -85.663 -91.668  1.00 139.13 ? 151  ASP   C OD2  1 
ATOM   18469 H  H    . ASP   C  3  151 ? 3.125   -83.098 -90.363  1.00 169.17 ? 151  ASP   C H    1 
ATOM   18470 H  HA   . ASP   C  3  151 ? 2.728   -82.680 -92.990  1.00 173.29 ? 151  ASP   C HA   1 
ATOM   18471 H  HB2  . ASP   C  3  151 ? 2.510   -85.143 -91.629  1.00 176.75 ? 151  ASP   C HB2  1 
ATOM   18472 H  HB3  . ASP   C  3  151 ? 2.500   -84.977 -93.210  1.00 176.75 ? 151  ASP   C HB3  1 
ATOM   18473 N  N    . GLY   C  3  152 ? 0.389   -81.855 -92.249  1.00 143.60 ? 152  GLY   C N    1 
ATOM   18474 C  CA   . GLY   C  3  152 ? -1.042  -81.644 -92.188  1.00 147.83 ? 152  GLY   C CA   1 
ATOM   18475 C  C    . GLY   C  3  152 ? -1.635  -81.800 -90.809  1.00 152.75 ? 152  GLY   C C    1 
ATOM   18476 O  O    . GLY   C  3  152 ? -2.847  -81.989 -90.683  1.00 156.13 ? 152  GLY   C O    1 
ATOM   18477 H  H    . GLY   C  3  152 ? 0.857   -81.141 -92.348  1.00 172.36 ? 152  GLY   C H    1 
ATOM   18478 H  HA2  . GLY   C  3  152 ? -1.239  -80.746 -92.497  1.00 177.43 ? 152  GLY   C HA2  1 
ATOM   18479 H  HA3  . GLY   C  3  152 ? -1.478  -82.283 -92.773  1.00 177.43 ? 152  GLY   C HA3  1 
ATOM   18480 N  N    . SER   C  3  153 ? -0.811  -81.725 -89.766  1.00 147.77 ? 153  SER   C N    1 
ATOM   18481 C  CA   . SER   C  3  153 ? -1.265  -81.891 -88.395  1.00 149.90 ? 153  SER   C CA   1 
ATOM   18482 C  C    . SER   C  3  153 ? -0.710  -80.773 -87.526  1.00 147.21 ? 153  SER   C C    1 
ATOM   18483 O  O    . SER   C  3  153 ? 0.346   -80.204 -87.814  1.00 145.01 ? 153  SER   C O    1 
ATOM   18484 C  CB   . SER   C  3  153 ? -0.836  -83.249 -87.823  1.00 147.91 ? 153  SER   C CB   1 
ATOM   18485 O  OG   . SER   C  3  153 ? -1.558  -84.307 -88.427  1.00 146.44 ? 153  SER   C OG   1 
ATOM   18486 H  H    . SER   C  3  153 ? 0.033   -81.575 -89.832  1.00 177.37 ? 153  SER   C H    1 
ATOM   18487 H  HA   . SER   C  3  153 ? -2.233  -81.840 -88.370  1.00 179.91 ? 153  SER   C HA   1 
ATOM   18488 H  HB2  . SER   C  3  153 ? 0.111   -83.377 -87.992  1.00 177.52 ? 153  SER   C HB2  1 
ATOM   18489 H  HB3  . SER   C  3  153 ? -1.006  -83.257 -86.868  1.00 177.52 ? 153  SER   C HB3  1 
ATOM   18490 H  HG   . SER   C  3  153 ? -1.514  -84.996 -87.949  1.00 175.76 ? 153  SER   C HG   1 
ATOM   18491 N  N    . GLU   C  3  154 ? -1.438  -80.468 -86.457  1.00 146.53 ? 154  GLU   C N    1 
ATOM   18492 C  CA   . GLU   C  3  154 ? -1.038  -79.470 -85.475  1.00 139.72 ? 154  GLU   C CA   1 
ATOM   18493 C  C    . GLU   C  3  154 ? -0.635  -80.179 -84.190  1.00 139.58 ? 154  GLU   C C    1 
ATOM   18494 O  O    . GLU   C  3  154 ? -1.380  -81.027 -83.689  1.00 142.25 ? 154  GLU   C O    1 
ATOM   18495 C  CB   . GLU   C  3  154 ? -2.176  -78.487 -85.190  1.00 138.37 ? 154  GLU   C CB   1 
ATOM   18496 C  CG   . GLU   C  3  154 ? -2.511  -77.542 -86.332  1.00 139.80 ? 154  GLU   C CG   1 
ATOM   18497 C  CD   . GLU   C  3  154 ? -3.313  -76.342 -85.865  1.00 143.14 ? 154  GLU   C CD   1 
ATOM   18498 O  OE1  . GLU   C  3  154 ? -3.185  -75.966 -84.681  1.00 142.23 ? 154  GLU   C OE1  1 
ATOM   18499 O  OE2  . GLU   C  3  154 ? -4.075  -75.777 -86.678  1.00 146.49 ? 154  GLU   C OE2  1 
ATOM   18500 H  H    . GLU   C  3  154 ? -2.192  -80.839 -86.274  1.00 175.88 ? 154  GLU   C H    1 
ATOM   18501 H  HA   . GLU   C  3  154 ? -0.280  -78.967 -85.812  1.00 167.70 ? 154  GLU   C HA   1 
ATOM   18502 H  HB2  . GLU   C  3  154 ? -2.977  -78.996 -84.989  1.00 166.08 ? 154  GLU   C HB2  1 
ATOM   18503 H  HB3  . GLU   C  3  154 ? -1.928  -77.944 -84.426  1.00 166.08 ? 154  GLU   C HB3  1 
ATOM   18504 H  HG2  . GLU   C  3  154 ? -1.687  -77.219 -86.730  1.00 167.79 ? 154  GLU   C HG2  1 
ATOM   18505 H  HG3  . GLU   C  3  154 ? -3.036  -78.017 -86.995  1.00 167.79 ? 154  GLU   C HG3  1 
ATOM   18506 N  N    . ARG   C  3  155 ? 0.537   -79.829 -83.659  1.00 136.41 ? 155  ARG   C N    1 
ATOM   18507 C  CA   . ARG   C  3  155 ? 1.020   -80.433 -82.421  1.00 137.88 ? 155  ARG   C CA   1 
ATOM   18508 C  C    . ARG   C  3  155 ? 0.669   -79.595 -81.194  1.00 134.68 ? 155  ARG   C C    1 
ATOM   18509 O  O    . ARG   C  3  155 ? 0.057   -80.100 -80.250  1.00 137.83 ? 155  ARG   C O    1 
ATOM   18510 C  CB   . ARG   C  3  155 ? 2.536   -80.647 -82.483  1.00 135.95 ? 155  ARG   C CB   1 
ATOM   18511 C  CG   . ARG   C  3  155 ? 3.127   -81.089 -81.143  1.00 134.21 ? 155  ARG   C CG   1 
ATOM   18512 C  CD   . ARG   C  3  155 ? 4.520   -81.685 -81.276  1.00 128.05 ? 155  ARG   C CD   1 
ATOM   18513 N  NE   . ARG   C  3  155 ? 4.599   -82.605 -82.407  1.00 129.25 ? 155  ARG   C NE   1 
ATOM   18514 C  CZ   . ARG   C  3  155 ? 4.613   -83.933 -82.319  1.00 133.14 ? 155  ARG   C CZ   1 
ATOM   18515 N  NH1  . ARG   C  3  155 ? 4.676   -84.655 -83.428  1.00 136.86 ? 155  ARG   C NH1  1 
ATOM   18516 N  NH2  . ARG   C  3  155 ? 4.579   -84.544 -81.140  1.00 131.16 ? 155  ARG   C NH2  1 
ATOM   18517 H  H    . ARG   C  3  155 ? 1.069   -79.244 -83.997  1.00 163.73 ? 155  ARG   C H    1 
ATOM   18518 H  HA   . ARG   C  3  155 ? 0.590   -81.298 -82.332  1.00 165.50 ? 155  ARG   C HA   1 
ATOM   18519 H  HB2  . ARG   C  3  155 ? 2.731   -81.334 -83.139  1.00 163.17 ? 155  ARG   C HB2  1 
ATOM   18520 H  HB3  . ARG   C  3  155 ? 2.962   -79.814 -82.739  1.00 163.17 ? 155  ARG   C HB3  1 
ATOM   18521 H  HG2  . ARG   C  3  155 ? 3.187   -80.319 -80.555  1.00 161.08 ? 155  ARG   C HG2  1 
ATOM   18522 H  HG3  . ARG   C  3  155 ? 2.550   -81.762 -80.750  1.00 161.08 ? 155  ARG   C HG3  1 
ATOM   18523 H  HD2  . ARG   C  3  155 ? 5.163   -80.973 -81.417  1.00 153.70 ? 155  ARG   C HD2  1 
ATOM   18524 H  HD3  . ARG   C  3  155 ? 4.738   -82.175 -80.468  1.00 153.70 ? 155  ARG   C HD3  1 
ATOM   18525 H  HE   . ARG   C  3  155 ? 4.640   -82.261 -83.194  1.00 155.13 ? 155  ARG   C HE   1 
ATOM   18526 H  HH11 . ARG   C  3  155 ? 4.708   -84.265 -84.193  1.00 164.27 ? 155  ARG   C HH11 1 
ATOM   18527 H  HH12 . ARG   C  3  155 ? 4.685   -85.514 -83.382  1.00 164.27 ? 155  ARG   C HH12 1 
ATOM   18528 H  HH21 . ARG   C  3  155 ? 4.547   -84.081 -80.416  1.00 157.43 ? 155  ARG   C HH21 1 
ATOM   18529 H  HH22 . ARG   C  3  155 ? 4.589   -85.403 -81.101  1.00 157.43 ? 155  ARG   C HH22 1 
ATOM   18530 N  N    . GLN   C  3  156 ? 1.065   -78.322 -81.191  1.00 130.02 ? 156  GLN   C N    1 
ATOM   18531 C  CA   . GLN   C  3  156 ? 0.770   -77.405 -80.090  1.00 129.78 ? 156  GLN   C CA   1 
ATOM   18532 C  C    . GLN   C  3  156 ? 1.202   -77.973 -78.740  1.00 129.12 ? 156  GLN   C C    1 
ATOM   18533 O  O    . GLN   C  3  156 ? 0.545   -77.753 -77.719  1.00 134.56 ? 156  GLN   C O    1 
ATOM   18534 C  CB   . GLN   C  3  156 ? -0.720  -77.057 -80.036  1.00 136.76 ? 156  GLN   C CB   1 
ATOM   18535 C  CG   . GLN   C  3  156 ? -1.396  -76.780 -81.363  1.00 141.03 ? 156  GLN   C CG   1 
ATOM   18536 C  CD   . GLN   C  3  156 ? -2.897  -76.596 -81.204  1.00 146.57 ? 156  GLN   C CD   1 
ATOM   18537 O  OE1  . GLN   C  3  156 ? -3.478  -75.653 -81.740  1.00 148.29 ? 156  GLN   C OE1  1 
ATOM   18538 N  NE2  . GLN   C  3  156 ? -3.531  -77.500 -80.460  1.00 148.70 ? 156  GLN   C NE2  1 
ATOM   18539 H  H    . GLN   C  3  156 ? 1.515   -77.959 -81.828  1.00 156.06 ? 156  GLN   C H    1 
ATOM   18540 H  HA   . GLN   C  3  156 ? 1.280   -76.597 -80.257  1.00 155.77 ? 156  GLN   C HA   1 
ATOM   18541 H  HB2  . GLN   C  3  156 ? -1.188  -77.801 -79.627  1.00 164.14 ? 156  GLN   C HB2  1 
ATOM   18542 H  HB3  . GLN   C  3  156 ? -0.823  -76.261 -79.492  1.00 164.14 ? 156  GLN   C HB3  1 
ATOM   18543 H  HG2  . GLN   C  3  156 ? -1.029  -75.968 -81.746  1.00 169.28 ? 156  GLN   C HG2  1 
ATOM   18544 H  HG3  . GLN   C  3  156 ? -1.244  -77.528 -81.962  1.00 169.28 ? 156  GLN   C HG3  1 
ATOM   18545 H  HE21 . GLN   C  3  156 ? -3.091  -78.145 -80.100  1.00 178.48 ? 156  GLN   C HE21 1 
ATOM   18546 H  HE22 . GLN   C  3  156 ? -4.380  -77.439 -80.340  1.00 178.48 ? 156  GLN   C HE22 1 
ATOM   18547 N  N    . ASN   C  3  157 ? 2.310   -78.711 -78.719  1.00 127.83 ? 157  ASN   C N    1 
ATOM   18548 C  CA   . ASN   C  3  157 ? 2.776   -79.311 -77.473  1.00 129.59 ? 157  ASN   C CA   1 
ATOM   18549 C  C    . ASN   C  3  157 ? 4.187   -78.883 -77.101  1.00 127.71 ? 157  ASN   C C    1 
ATOM   18550 O  O    . ASN   C  3  157 ? 4.410   -78.435 -75.971  1.00 131.06 ? 157  ASN   C O    1 
ATOM   18551 C  CB   . ASN   C  3  157 ? 2.691   -80.846 -77.548  1.00 132.44 ? 157  ASN   C CB   1 
ATOM   18552 C  CG   . ASN   C  3  157 ? 2.209   -81.464 -76.242  1.00 136.33 ? 157  ASN   C CG   1 
ATOM   18553 O  OD1  . ASN   C  3  157 ? 1.904   -80.755 -75.282  1.00 136.22 ? 157  ASN   C OD1  1 
ATOM   18554 N  ND2  . ASN   C  3  157 ? 2.125   -82.788 -76.205  1.00 139.41 ? 157  ASN   C ND2  1 
ATOM   18555 H  H    . ASN   C  3  157 ? 2.801   -78.877 -79.406  1.00 153.43 ? 157  ASN   C H    1 
ATOM   18556 H  HA   . ASN   C  3  157 ? 2.186   -79.018 -76.760  1.00 155.54 ? 157  ASN   C HA   1 
ATOM   18557 H  HB2  . ASN   C  3  157 ? 2.068   -81.096 -78.248  1.00 158.96 ? 157  ASN   C HB2  1 
ATOM   18558 H  HB3  . ASN   C  3  157 ? 3.571   -81.203 -77.744  1.00 158.96 ? 157  ASN   C HB3  1 
ATOM   18559 H  HD21 . ASN   C  3  157 ? 1.858   -83.183 -75.489  1.00 167.33 ? 157  ASN   C HD21 1 
ATOM   18560 H  HD22 . ASN   C  3  157 ? 2.338   -83.252 -76.898  1.00 167.33 ? 157  ASN   C HD22 1 
ATOM   18561 N  N    . GLY   C  3  158 ? 5.149   -79.006 -78.010  1.00 122.10 ? 158  GLY   C N    1 
ATOM   18562 C  CA   . GLY   C  3  158 ? 6.511   -78.598 -77.738  1.00 118.47 ? 158  GLY   C CA   1 
ATOM   18563 C  C    . GLY   C  3  158 ? 6.836   -77.173 -78.123  1.00 115.15 ? 158  GLY   C C    1 
ATOM   18564 O  O    . GLY   C  3  158 ? 8.000   -76.767 -78.038  1.00 112.75 ? 158  GLY   C O    1 
ATOM   18565 H  H    . GLY   C  3  158 ? 5.030   -79.328 -78.799  1.00 146.56 ? 158  GLY   C H    1 
ATOM   18566 H  HA2  . GLY   C  3  158 ? 6.679   -78.694 -76.787  1.00 142.20 ? 158  GLY   C HA2  1 
ATOM   18567 H  HA3  . GLY   C  3  158 ? 7.113   -79.181 -78.225  1.00 142.20 ? 158  GLY   C HA3  1 
ATOM   18568 N  N    . VAL   C  3  159 ? 5.836   -76.395 -78.538  1.00 119.50 ? 159  VAL   C N    1 
ATOM   18569 C  CA   . VAL   C  3  159 ? 6.070   -75.034 -79.000  1.00 109.21 ? 159  VAL   C CA   1 
ATOM   18570 C  C    . VAL   C  3  159 ? 6.402   -74.127 -77.822  1.00 106.25 ? 159  VAL   C C    1 
ATOM   18571 O  O    . VAL   C  3  159 ? 5.853   -74.274 -76.722  1.00 109.33 ? 159  VAL   C O    1 
ATOM   18572 C  CB   . VAL   C  3  159 ? 4.836   -74.524 -79.767  1.00 105.00 ? 159  VAL   C CB   1 
ATOM   18573 C  CG1  . VAL   C  3  159 ? 3.590   -74.575 -78.881  1.00 110.23 ? 159  VAL   C CG1  1 
ATOM   18574 C  CG2  . VAL   C  3  159 ? 5.070   -73.115 -80.290  1.00 96.76  ? 159  VAL   C CG2  1 
ATOM   18575 H  H    . VAL   C  3  159 ? 5.010   -76.635 -78.560  1.00 143.43 ? 159  VAL   C H    1 
ATOM   18576 H  HA   . VAL   C  3  159 ? 6.832   -75.030 -79.600  1.00 131.09 ? 159  VAL   C HA   1 
ATOM   18577 H  HB   . VAL   C  3  159 ? 4.684   -75.103 -80.530  1.00 126.04 ? 159  VAL   C HB   1 
ATOM   18578 H  HG11 . VAL   C  3  159 ? 2.833   -74.232 -79.381  1.00 132.31 ? 159  VAL   C HG11 1 
ATOM   18579 H  HG12 . VAL   C  3  159 ? 3.424   -75.495 -78.622  1.00 132.31 ? 159  VAL   C HG12 1 
ATOM   18580 H  HG13 . VAL   C  3  159 ? 3.740   -74.031 -78.093  1.00 132.31 ? 159  VAL   C HG13 1 
ATOM   18581 H  HG21 . VAL   C  3  159 ? 4.353   -72.881 -80.900  1.00 116.15 ? 159  VAL   C HG21 1 
ATOM   18582 H  HG22 . VAL   C  3  159 ? 5.081   -72.498 -79.541  1.00 116.15 ? 159  VAL   C HG22 1 
ATOM   18583 H  HG23 . VAL   C  3  159 ? 5.921   -73.088 -80.754  1.00 116.15 ? 159  VAL   C HG23 1 
ATOM   18584 N  N    . LEU   C  3  160 ? 7.314   -73.180 -78.050  1.00 101.04 ? 160  LEU   C N    1 
ATOM   18585 C  CA   . LEU   C  3  160 ? 7.624   -72.132 -77.086  1.00 95.00  ? 160  LEU   C CA   1 
ATOM   18586 C  C    . LEU   C  3  160 ? 7.776   -70.813 -77.829  1.00 90.54  ? 160  LEU   C C    1 
ATOM   18587 O  O    . LEU   C  3  160 ? 8.331   -70.774 -78.931  1.00 91.24  ? 160  LEU   C O    1 
ATOM   18588 C  CB   . LEU   C  3  160 ? 8.903   -72.435 -76.292  1.00 93.37  ? 160  LEU   C CB   1 
ATOM   18589 C  CG   . LEU   C  3  160 ? 8.758   -73.336 -75.062  1.00 100.25 ? 160  LEU   C CG   1 
ATOM   18590 C  CD1  . LEU   C  3  160 ? 10.097  -73.478 -74.354  1.00 100.60 ? 160  LEU   C CD1  1 
ATOM   18591 C  CD2  . LEU   C  3  160 ? 7.702   -72.804 -74.097  1.00 104.53 ? 160  LEU   C CD2  1 
ATOM   18592 H  H    . LEU   C  3  160 ? 7.775   -73.125 -78.774  1.00 121.28 ? 160  LEU   C H    1 
ATOM   18593 H  HA   . LEU   C  3  160 ? 6.896   -72.054 -76.450  1.00 114.03 ? 160  LEU   C HA   1 
ATOM   18594 H  HB2  . LEU   C  3  160 ? 9.530   -72.871 -76.890  1.00 112.08 ? 160  LEU   C HB2  1 
ATOM   18595 H  HB3  . LEU   C  3  160 ? 9.270   -71.592 -75.984  1.00 112.08 ? 160  LEU   C HB3  1 
ATOM   18596 H  HG   . LEU   C  3  160 ? 8.465   -74.213 -75.358  1.00 120.34 ? 160  LEU   C HG   1 
ATOM   18597 H  HD11 . LEU   C  3  160 ? 10.109  -74.317 -73.867  1.00 120.76 ? 160  LEU   C HD11 1 
ATOM   18598 H  HD12 . LEU   C  3  160 ? 10.806  -73.469 -75.015  1.00 120.76 ? 160  LEU   C HD12 1 
ATOM   18599 H  HD13 . LEU   C  3  160 ? 10.208  -72.737 -73.738  1.00 120.76 ? 160  LEU   C HD13 1 
ATOM   18600 H  HD21 . LEU   C  3  160 ? 7.707   -73.347 -73.293  1.00 125.48 ? 160  LEU   C HD21 1 
ATOM   18601 H  HD22 . LEU   C  3  160 ? 7.912   -71.884 -73.875  1.00 125.48 ? 160  LEU   C HD22 1 
ATOM   18602 H  HD23 . LEU   C  3  160 ? 6.832   -72.852 -74.523  1.00 125.48 ? 160  LEU   C HD23 1 
ATOM   18603 N  N    . ASN   C  3  161 ? 7.289   -69.736 -77.216  1.00 86.91  ? 161  ASN   C N    1 
ATOM   18604 C  CA   . ASN   C  3  161 ? 7.202   -68.442 -77.873  1.00 81.58  ? 161  ASN   C CA   1 
ATOM   18605 C  C    . ASN   C  3  161 ? 7.780   -67.350 -76.986  1.00 79.77  ? 161  ASN   C C    1 
ATOM   18606 O  O    . ASN   C  3  161 ? 7.748   -67.439 -75.756  1.00 82.00  ? 161  ASN   C O    1 
ATOM   18607 C  CB   . ASN   C  3  161 ? 5.750   -68.100 -78.227  1.00 79.75  ? 161  ASN   C CB   1 
ATOM   18608 C  CG   . ASN   C  3  161 ? 5.125   -69.116 -79.160  1.00 79.70  ? 161  ASN   C CG   1 
ATOM   18609 O  OD1  . ASN   C  3  161 ? 5.781   -69.629 -80.068  1.00 79.62  ? 161  ASN   C OD1  1 
ATOM   18610 N  ND2  . ASN   C  3  161 ? 3.852   -69.419 -78.937  1.00 79.49  ? 161  ASN   C ND2  1 
ATOM   18611 H  H    . ASN   C  3  161 ? 6.999   -69.734 -76.406  1.00 104.33 ? 161  ASN   C H    1 
ATOM   18612 H  HA   . ASN   C  3  161 ? 7.729   -68.465 -78.687  1.00 97.93  ? 161  ASN   C HA   1 
ATOM   18613 H  HB2  . ASN   C  3  161 ? 5.223   -68.075 -77.413  1.00 95.74  ? 161  ASN   C HB2  1 
ATOM   18614 H  HB3  . ASN   C  3  161 ? 5.726   -67.235 -78.664  1.00 95.74  ? 161  ASN   C HB3  1 
ATOM   18615 H  HD21 . ASN   C  3  161 ? 3.452   -69.991 -79.440  1.00 95.43  ? 161  ASN   C HD21 1 
ATOM   18616 H  HD22 . ASN   C  3  161 ? 3.428   -69.043 -78.290  1.00 95.43  ? 161  ASN   C HD22 1 
ATOM   18617 N  N    . SER   C  3  162 ? 8.304   -66.311 -77.634  1.00 76.99  ? 162  SER   C N    1 
ATOM   18618 C  CA   . SER   C  3  162 ? 8.865   -65.156 -76.950  1.00 73.53  ? 162  SER   C CA   1 
ATOM   18619 C  C    . SER   C  3  162 ? 8.506   -63.901 -77.730  1.00 75.13  ? 162  SER   C C    1 
ATOM   18620 O  O    . SER   C  3  162 ? 8.449   -63.921 -78.962  1.00 73.69  ? 162  SER   C O    1 
ATOM   18621 C  CB   . SER   C  3  162 ? 10.388  -65.275 -76.810  1.00 66.79  ? 162  SER   C CB   1 
ATOM   18622 O  OG   . SER   C  3  162 ? 10.887  -64.346 -75.864  1.00 63.98  ? 162  SER   C OG   1 
ATOM   18623 H  H    . SER   C  3  162 ? 8.345   -66.253 -78.491  1.00 92.42  ? 162  SER   C H    1 
ATOM   18624 H  HA   . SER   C  3  162 ? 8.489   -65.083 -76.059  1.00 88.27  ? 162  SER   C HA   1 
ATOM   18625 H  HB2  . SER   C  3  162 ? 10.608  -66.173 -76.516  1.00 80.18  ? 162  SER   C HB2  1 
ATOM   18626 H  HB3  . SER   C  3  162 ? 10.798  -65.097 -77.671  1.00 80.18  ? 162  SER   C HB3  1 
ATOM   18627 H  HG   . SER   C  3  162 ? 11.716  -64.447 -75.772  1.00 76.81  ? 162  SER   C HG   1 
ATOM   18628 N  N    . TRP   C  3  163 ? 8.264   -62.812 -77.003  1.00 78.64  ? 163  TRP   C N    1 
ATOM   18629 C  CA   . TRP   C  3  163 ? 7.866   -61.537 -77.580  1.00 78.82  ? 163  TRP   C CA   1 
ATOM   18630 C  C    . TRP   C  3  163 ? 8.873   -60.463 -77.198  1.00 78.84  ? 163  TRP   C C    1 
ATOM   18631 O  O    . TRP   C  3  163 ? 9.290   -60.380 -76.038  1.00 83.33  ? 163  TRP   C O    1 
ATOM   18632 C  CB   . TRP   C  3  163 ? 6.480   -61.111 -77.090  1.00 80.27  ? 163  TRP   C CB   1 
ATOM   18633 C  CG   . TRP   C  3  163 ? 5.355   -61.980 -77.541  1.00 82.27  ? 163  TRP   C CG   1 
ATOM   18634 C  CD1  . TRP   C  3  163 ? 4.451   -61.699 -78.521  1.00 84.85  ? 163  TRP   C CD1  1 
ATOM   18635 C  CD2  . TRP   C  3  163 ? 4.999   -63.267 -77.022  1.00 81.47  ? 163  TRP   C CD2  1 
ATOM   18636 N  NE1  . TRP   C  3  163 ? 3.554   -62.729 -78.647  1.00 85.17  ? 163  TRP   C NE1  1 
ATOM   18637 C  CE2  . TRP   C  3  163 ? 3.870   -63.706 -77.739  1.00 82.74  ? 163  TRP   C CE2  1 
ATOM   18638 C  CE3  . TRP   C  3  163 ? 5.526   -64.090 -76.023  1.00 81.68  ? 163  TRP   C CE3  1 
ATOM   18639 C  CZ2  . TRP   C  3  163 ? 3.259   -64.932 -77.492  1.00 82.50  ? 163  TRP   C CZ2  1 
ATOM   18640 C  CZ3  . TRP   C  3  163 ? 4.917   -65.308 -75.778  1.00 83.98  ? 163  TRP   C CZ3  1 
ATOM   18641 C  CH2  . TRP   C  3  163 ? 3.795   -65.717 -76.510  1.00 83.92  ? 163  TRP   C CH2  1 
ATOM   18642 H  H    . TRP   C  3  163 ? 8.328   -62.789 -76.146  1.00 94.41  ? 163  TRP   C H    1 
ATOM   18643 H  HA   . TRP   C  3  163 ? 7.844   -61.622 -78.547  1.00 94.62  ? 163  TRP   C HA   1 
ATOM   18644 H  HB2  . TRP   C  3  163 ? 6.482   -61.119 -76.120  1.00 96.36  ? 163  TRP   C HB2  1 
ATOM   18645 H  HB3  . TRP   C  3  163 ? 6.302   -60.214 -77.414  1.00 96.36  ? 163  TRP   C HB3  1 
ATOM   18646 H  HD1  . TRP   C  3  163 ? 4.444   -60.921 -79.031  1.00 101.85 ? 163  TRP   C HD1  1 
ATOM   18647 H  HE1  . TRP   C  3  163 ? 2.900   -62.758 -79.205  1.00 102.24 ? 163  TRP   C HE1  1 
ATOM   18648 H  HE3  . TRP   C  3  163 ? 6.270   -63.825 -75.532  1.00 98.05  ? 163  TRP   C HE3  1 
ATOM   18649 H  HZ2  . TRP   C  3  163 ? 2.514   -65.207 -77.976  1.00 99.04  ? 163  TRP   C HZ2  1 
ATOM   18650 H  HZ3  . TRP   C  3  163 ? 5.258   -65.865 -75.116  1.00 100.81 ? 163  TRP   C HZ3  1 
ATOM   18651 H  HH2  . TRP   C  3  163 ? 3.407   -66.541 -76.324  1.00 100.74 ? 163  TRP   C HH2  1 
ATOM   18652 N  N    . THR   C  3  164 ? 9.249   -59.634 -78.164  1.00 74.31  ? 164  THR   C N    1 
ATOM   18653 C  CA   . THR   C  3  164 ? 10.116  -58.503 -77.883  1.00 77.83  ? 164  THR   C CA   1 
ATOM   18654 C  C    . THR   C  3  164 ? 9.291   -57.302 -77.438  1.00 81.11  ? 164  THR   C C    1 
ATOM   18655 O  O    . THR   C  3  164 ? 8.092   -57.200 -77.712  1.00 83.22  ? 164  THR   C O    1 
ATOM   18656 C  CB   . THR   C  3  164 ? 10.945  -58.112 -79.108  1.00 81.40  ? 164  THR   C CB   1 
ATOM   18657 O  OG1  . THR   C  3  164 ? 10.082  -57.610 -80.136  1.00 81.72  ? 164  THR   C OG1  1 
ATOM   18658 C  CG2  . THR   C  3  164 ? 11.715  -59.301 -79.637  1.00 81.86  ? 164  THR   C CG2  1 
ATOM   18659 H  H    . THR   C  3  164 ? 9.015   -59.708 -78.989  1.00 89.20  ? 164  THR   C H    1 
ATOM   18660 H  HA   . THR   C  3  164 ? 10.728  -58.754 -77.174  1.00 93.43  ? 164  THR   C HA   1 
ATOM   18661 H  HB   . THR   C  3  164 ? 11.581  -57.425 -78.855  1.00 97.72  ? 164  THR   C HB   1 
ATOM   18662 H  HG1  . THR   C  3  164 ? 10.508  -57.089 -80.639  1.00 98.10  ? 164  THR   C HG1  1 
ATOM   18663 H  HG21 . THR   C  3  164 ? 12.245  -59.038 -80.406  1.00 98.27  ? 164  THR   C HG21 1 
ATOM   18664 H  HG22 . THR   C  3  164 ? 12.308  -59.645 -78.950  1.00 98.27  ? 164  THR   C HG22 1 
ATOM   18665 H  HG23 . THR   C  3  164 ? 11.101  -60.003 -79.903  1.00 98.27  ? 164  THR   C HG23 1 
ATOM   18666 N  N    . ASP   C  3  165 ? 9.954   -56.388 -76.741  1.00 79.77  ? 165  ASP   C N    1 
ATOM   18667 C  CA   . ASP   C  3  165 ? 9.336   -55.115 -76.421  1.00 83.44  ? 165  ASP   C CA   1 
ATOM   18668 C  C    . ASP   C  3  165 ? 9.174   -54.277 -77.685  1.00 82.54  ? 165  ASP   C C    1 
ATOM   18669 O  O    . ASP   C  3  165 ? 9.797   -54.529 -78.720  1.00 84.52  ? 165  ASP   C O    1 
ATOM   18670 C  CB   . ASP   C  3  165 ? 10.169  -54.355 -75.391  1.00 91.21  ? 165  ASP   C CB   1 
ATOM   18671 C  CG   . ASP   C  3  165 ? 9.946   -54.853 -73.978  1.00 94.49  ? 165  ASP   C CG   1 
ATOM   18672 O  OD1  . ASP   C  3  165 ? 8.854   -55.391 -73.701  1.00 95.54  ? 165  ASP   C OD1  1 
ATOM   18673 O  OD2  . ASP   C  3  165 ? 10.861  -54.700 -73.141  1.00 95.94  ? 165  ASP   C OD2  1 
ATOM   18674 H  H    . ASP   C  3  165 ? 10.756  -56.482 -76.445  1.00 95.76  ? 165  ASP   C H    1 
ATOM   18675 H  HA   . ASP   C  3  165 ? 8.457   -55.268 -76.038  1.00 100.17 ? 165  ASP   C HA   1 
ATOM   18676 H  HB2  . ASP   C  3  165 ? 11.110  -54.463 -75.602  1.00 109.49 ? 165  ASP   C HB2  1 
ATOM   18677 H  HB3  . ASP   C  3  165 ? 9.929   -53.416 -75.420  1.00 109.49 ? 165  ASP   C HB3  1 
ATOM   18678 N  N    . GLN   C  3  166 ? 8.310   -53.274 -77.592  1.00 82.64  ? 166  GLN   C N    1 
ATOM   18679 C  CA   . GLN   C  3  166 ? 8.134   -52.335 -78.691  1.00 82.97  ? 166  GLN   C CA   1 
ATOM   18680 C  C    . GLN   C  3  166 ? 9.438   -51.605 -78.978  1.00 88.42  ? 166  GLN   C C    1 
ATOM   18681 O  O    . GLN   C  3  166 ? 10.032  -50.991 -78.087  1.00 91.43  ? 166  GLN   C O    1 
ATOM   18682 C  CB   . GLN   C  3  166 ? 7.026   -51.345 -78.340  1.00 83.55  ? 166  GLN   C CB   1 
ATOM   18683 C  CG   . GLN   C  3  166 ? 6.958   -50.120 -79.217  1.00 84.34  ? 166  GLN   C CG   1 
ATOM   18684 C  CD   . GLN   C  3  166 ? 5.579   -49.513 -79.233  1.00 82.69  ? 166  GLN   C CD   1 
ATOM   18685 O  OE1  . GLN   C  3  166 ? 5.297   -48.561 -78.507  1.00 83.68  ? 166  GLN   C OE1  1 
ATOM   18686 N  NE2  . GLN   C  3  166 ? 4.711   -50.049 -80.081  1.00 80.38  ? 166  GLN   C NE2  1 
ATOM   18687 H  H    . GLN   C  3  166 ? 7.815   -53.115 -76.907  1.00 99.20  ? 166  GLN   C H    1 
ATOM   18688 H  HA   . GLN   C  3  166 ? 7.877   -52.811 -79.496  1.00 99.60  ? 166  GLN   C HA   1 
ATOM   18689 H  HB2  . GLN   C  3  166 ? 6.173   -51.802 -78.412  1.00 100.29 ? 166  GLN   C HB2  1 
ATOM   18690 H  HB3  . GLN   C  3  166 ? 7.164   -51.042 -77.428  1.00 100.29 ? 166  GLN   C HB3  1 
ATOM   18691 H  HG2  . GLN   C  3  166 ? 7.579   -49.454 -78.883  1.00 101.25 ? 166  GLN   C HG2  1 
ATOM   18692 H  HG3  . GLN   C  3  166 ? 7.192   -50.365 -80.126  1.00 101.25 ? 166  GLN   C HG3  1 
ATOM   18693 H  HE21 . GLN   C  3  166 ? 4.949   -50.706 -80.582  1.00 96.49  ? 166  GLN   C HE21 1 
ATOM   18694 H  HE22 . GLN   C  3  166 ? 3.910   -49.740 -80.130  1.00 96.49  ? 166  GLN   C HE22 1 
ATOM   18695 N  N    . ASP   C  3  167 ? 9.888   -51.671 -80.227  1.00 92.40  ? 167  ASP   C N    1 
ATOM   18696 C  CA   . ASP   C  3  167 ? 11.156  -51.050 -80.586  1.00 96.29  ? 167  ASP   C CA   1 
ATOM   18697 C  C    . ASP   C  3  167 ? 11.041  -49.530 -80.495  1.00 99.26  ? 167  ASP   C C    1 
ATOM   18698 O  O    . ASP   C  3  167 ? 9.980   -48.952 -80.741  1.00 98.25  ? 167  ASP   C O    1 
ATOM   18699 C  CB   . ASP   C  3  167 ? 11.574  -51.481 -81.992  1.00 98.08  ? 167  ASP   C CB   1 
ATOM   18700 C  CG   . ASP   C  3  167 ? 13.044  -51.232 -82.267  1.00 105.96 ? 167  ASP   C CG   1 
ATOM   18701 O  OD1  . ASP   C  3  167 ? 13.451  -50.054 -82.330  1.00 112.37 ? 167  ASP   C OD1  1 
ATOM   18702 O  OD2  . ASP   C  3  167 ? 13.796  -52.220 -82.408  1.00 106.20 ? 167  ASP   C OD2  1 
ATOM   18703 H  H    . ASP   C  3  167 ? 9.484   -52.064 -80.876  1.00 110.92 ? 167  ASP   C H    1 
ATOM   18704 H  HA   . ASP   C  3  167 ? 11.854  -51.332 -79.974  1.00 115.58 ? 167  ASP   C HA   1 
ATOM   18705 H  HB2  . ASP   C  3  167 ? 11.406  -52.431 -82.095  1.00 117.73 ? 167  ASP   C HB2  1 
ATOM   18706 H  HB3  . ASP   C  3  167 ? 11.058  -50.981 -82.643  1.00 117.73 ? 167  ASP   C HB3  1 
ATOM   18707 N  N    . SER   C  3  168 ? 12.154  -48.882 -80.122  1.00 102.72 ? 168  SER   C N    1 
ATOM   18708 C  CA   . SER   C  3  168 ? 12.155  -47.431 -79.936  1.00 105.29 ? 168  SER   C CA   1 
ATOM   18709 C  C    . SER   C  3  168 ? 12.133  -46.689 -81.273  1.00 108.09 ? 168  SER   C C    1 
ATOM   18710 O  O    . SER   C  3  168 ? 11.378  -45.724 -81.440  1.00 110.46 ? 168  SER   C O    1 
ATOM   18711 C  CB   . SER   C  3  168 ? 13.375  -47.009 -79.110  1.00 108.27 ? 168  SER   C CB   1 
ATOM   18712 O  OG   . SER   C  3  168 ? 14.481  -47.870 -79.328  1.00 110.64 ? 168  SER   C OG   1 
ATOM   18713 H  H    . SER   C  3  168 ? 12.913  -49.258 -79.971  1.00 123.30 ? 168  SER   C H    1 
ATOM   18714 H  HA   . SER   C  3  168 ? 11.354  -47.182 -79.448  1.00 126.38 ? 168  SER   C HA   1 
ATOM   18715 H  HB2  . SER   C  3  168 ? 13.628  -46.107 -79.362  1.00 129.96 ? 168  SER   C HB2  1 
ATOM   18716 H  HB3  . SER   C  3  168 ? 13.140  -47.036 -78.169  1.00 129.96 ? 168  SER   C HB3  1 
ATOM   18717 H  HG   . SER   C  3  168 ? 15.010  -47.523 -79.881  1.00 132.81 ? 168  SER   C HG   1 
ATOM   18718 N  N    . LYS   C  3  169 ? 12.949  -47.124 -82.239  1.00 110.37 ? 169  LYS   C N    1 
ATOM   18719 C  CA   . LYS   C  3  169 ? 13.086  -46.381 -83.490  1.00 116.89 ? 169  LYS   C CA   1 
ATOM   18720 C  C    . LYS   C  3  169 ? 11.803  -46.446 -84.312  1.00 117.38 ? 169  LYS   C C    1 
ATOM   18721 O  O    . LYS   C  3  169 ? 11.339  -45.434 -84.852  1.00 126.06 ? 169  LYS   C O    1 
ATOM   18722 C  CB   . LYS   C  3  169 ? 14.247  -46.939 -84.316  1.00 122.54 ? 169  LYS   C CB   1 
ATOM   18723 C  CG   . LYS   C  3  169 ? 15.492  -47.326 -83.540  1.00 127.56 ? 169  LYS   C CG   1 
ATOM   18724 C  CD   . LYS   C  3  169 ? 16.251  -48.404 -84.289  1.00 127.08 ? 169  LYS   C CD   1 
ATOM   18725 C  CE   . LYS   C  3  169 ? 17.750  -48.263 -84.106  1.00 132.93 ? 169  LYS   C CE   1 
ATOM   18726 N  NZ   . LYS   C  3  169 ? 18.497  -48.823 -85.266  1.00 135.92 ? 169  LYS   C NZ   1 
ATOM   18727 H  H    . LYS   C  3  169 ? 13.428  -47.836 -82.193  1.00 132.48 ? 169  LYS   C H    1 
ATOM   18728 H  HA   . LYS   C  3  169 ? 13.275  -45.455 -83.272  1.00 140.30 ? 169  LYS   C HA   1 
ATOM   18729 H  HB2  . LYS   C  3  169 ? 13.937  -47.735 -84.775  1.00 147.09 ? 169  LYS   C HB2  1 
ATOM   18730 H  HB3  . LYS   C  3  169 ? 14.511  -46.265 -84.962  1.00 147.09 ? 169  LYS   C HB3  1 
ATOM   18731 H  HG2  . LYS   C  3  169 ? 16.069  -46.553 -83.438  1.00 153.11 ? 169  LYS   C HG2  1 
ATOM   18732 H  HG3  . LYS   C  3  169 ? 15.241  -47.670 -82.668  1.00 153.11 ? 169  LYS   C HG3  1 
ATOM   18733 H  HD2  . LYS   C  3  169 ? 15.984  -49.275 -83.955  1.00 152.53 ? 169  LYS   C HD2  1 
ATOM   18734 H  HD3  . LYS   C  3  169 ? 16.052  -48.337 -85.236  1.00 152.53 ? 169  LYS   C HD3  1 
ATOM   18735 H  HE2  . LYS   C  3  169 ? 17.976  -47.323 -84.022  1.00 159.56 ? 169  LYS   C HE2  1 
ATOM   18736 H  HE3  . LYS   C  3  169 ? 18.022  -48.742 -83.308  1.00 159.56 ? 169  LYS   C HE3  1 
ATOM   18737 H  HZ1  . LYS   C  3  169 ? 19.370  -48.831 -85.091  1.00 163.15 ? 169  LYS   C HZ1  1 
ATOM   18738 H  HZ2  . LYS   C  3  169 ? 18.227  -49.655 -85.430  1.00 163.15 ? 169  LYS   C HZ2  1 
ATOM   18739 H  HZ3  . LYS   C  3  169 ? 18.353  -48.325 -85.990  1.00 163.15 ? 169  LYS   C HZ3  1 
ATOM   18740 N  N    . ASP   C  3  170 ? 11.250  -47.649 -84.450  1.00 111.11 ? 170  ASP   C N    1 
ATOM   18741 C  CA   . ASP   C  3  170 ? 10.005  -47.919 -85.154  1.00 108.70 ? 170  ASP   C CA   1 
ATOM   18742 C  C    . ASP   C  3  170 ? 9.119   -48.706 -84.198  1.00 107.69 ? 170  ASP   C C    1 
ATOM   18743 O  O    . ASP   C  3  170 ? 9.593   -49.622 -83.524  1.00 105.30 ? 170  ASP   C O    1 
ATOM   18744 C  CB   . ASP   C  3  170 ? 10.250  -48.715 -86.440  1.00 106.51 ? 170  ASP   C CB   1 
ATOM   18745 C  CG   . ASP   C  3  170 ? 10.503  -50.183 -86.169  1.00 102.82 ? 170  ASP   C CG   1 
ATOM   18746 O  OD1  . ASP   C  3  170 ? 9.535   -50.903 -85.843  1.00 100.76 ? 170  ASP   C OD1  1 
ATOM   18747 O  OD2  . ASP   C  3  170 ? 11.671  -50.614 -86.254  1.00 104.13 ? 170  ASP   C OD2  1 
ATOM   18748 H  H    . ASP   C  3  170 ? 11.600  -48.364 -84.125  1.00 133.37 ? 170  ASP   C H    1 
ATOM   18749 H  HA   . ASP   C  3  170 ? 9.558   -47.097 -85.412  1.00 130.48 ? 170  ASP   C HA   1 
ATOM   18750 H  HB2  . ASP   C  3  170 ? 9.469   -48.644 -87.011  1.00 127.85 ? 170  ASP   C HB2  1 
ATOM   18751 H  HB3  . ASP   C  3  170 ? 11.027  -48.353 -86.893  1.00 127.85 ? 170  ASP   C HB3  1 
ATOM   18752 N  N    . SER   C  3  171 ? 7.844   -48.351 -84.120  1.00 105.36 ? 171  SER   C N    1 
ATOM   18753 C  CA   . SER   C  3  171 ? 7.045   -48.859 -83.008  1.00 103.99 ? 171  SER   C CA   1 
ATOM   18754 C  C    . SER   C  3  171 ? 6.654   -50.340 -83.141  1.00 99.42  ? 171  SER   C C    1 
ATOM   18755 O  O    . SER   C  3  171 ? 6.040   -50.864 -82.202  1.00 97.13  ? 171  SER   C O    1 
ATOM   18756 C  CB   . SER   C  3  171 ? 5.800   -47.983 -82.854  1.00 107.39 ? 171  SER   C CB   1 
ATOM   18757 O  OG   . SER   C  3  171 ? 6.161   -46.638 -82.564  1.00 110.45 ? 171  SER   C OG   1 
ATOM   18758 H  H    . SER   C  3  171 ? 7.432   -47.839 -84.675  1.00 126.47 ? 171  SER   C H    1 
ATOM   18759 H  HA   . SER   C  3  171 ? 7.567   -48.797 -82.194  1.00 124.83 ? 171  SER   C HA   1 
ATOM   18760 H  HB2  . SER   C  3  171 ? 5.295   -48.002 -83.683  1.00 128.90 ? 171  SER   C HB2  1 
ATOM   18761 H  HB3  . SER   C  3  171 ? 5.258   -48.328 -82.128  1.00 128.90 ? 171  SER   C HB3  1 
ATOM   18762 H  HG   . SER   C  3  171 ? 5.884   -46.128 -83.171  1.00 132.58 ? 171  SER   C HG   1 
ATOM   18763 N  N    . THR   C  3  172 ? 7.010   -51.036 -84.225  1.00 96.53  ? 172  THR   C N    1 
ATOM   18764 C  CA   . THR   C  3  172 ? 6.639   -52.441 -84.392  1.00 93.98  ? 172  THR   C CA   1 
ATOM   18765 C  C    . THR   C  3  172 ? 7.240   -53.332 -83.295  1.00 89.84  ? 172  THR   C C    1 
ATOM   18766 O  O    . THR   C  3  172 ? 8.173   -52.951 -82.585  1.00 89.15  ? 172  THR   C O    1 
ATOM   18767 C  CB   . THR   C  3  172 ? 7.119   -52.992 -85.738  1.00 94.85  ? 172  THR   C CB   1 
ATOM   18768 O  OG1  . THR   C  3  172 ? 8.545   -53.160 -85.707  1.00 92.39  ? 172  THR   C OG1  1 
ATOM   18769 C  CG2  . THR   C  3  172 ? 6.746   -52.075 -86.878  1.00 98.42  ? 172  THR   C CG2  1 
ATOM   18770 H  H    . THR   C  3  172 ? 7.467   -50.715 -84.879  1.00 115.88 ? 172  THR   C H    1 
ATOM   18771 H  HA   . THR   C  3  172 ? 5.671   -52.477 -84.344  1.00 112.81 ? 172  THR   C HA   1 
ATOM   18772 H  HB   . THR   C  3  172 ? 6.691   -53.847 -85.897  1.00 113.86 ? 172  THR   C HB   1 
ATOM   18773 H  HG1  . THR   C  3  172 ? 8.881   -52.660 -85.122  1.00 110.91 ? 172  THR   C HG1  1 
ATOM   18774 H  HG21 . THR   C  3  172 ? 6.881   -52.528 -87.726  1.00 118.14 ? 172  THR   C HG21 1 
ATOM   18775 H  HG22 . THR   C  3  172 ? 5.814   -51.817 -86.805  1.00 118.14 ? 172  THR   C HG22 1 
ATOM   18776 H  HG23 . THR   C  3  172 ? 7.296   -51.277 -86.857  1.00 118.14 ? 172  THR   C HG23 1 
ATOM   18777 N  N    . TYR   C  3  173 ? 6.708   -54.562 -83.210  1.00 89.72  ? 173  TYR   C N    1 
ATOM   18778 C  CA   . TYR   C  3  173 ? 7.104   -55.618 -82.274  1.00 89.09  ? 173  TYR   C CA   1 
ATOM   18779 C  C    . TYR   C  3  173 ? 7.650   -56.822 -83.049  1.00 87.40  ? 173  TYR   C C    1 
ATOM   18780 O  O    . TYR   C  3  173 ? 7.666   -56.837 -84.283  1.00 90.08  ? 173  TYR   C O    1 
ATOM   18781 C  CB   . TYR   C  3  173 ? 5.921   -56.070 -81.403  1.00 91.11  ? 173  TYR   C CB   1 
ATOM   18782 C  CG   . TYR   C  3  173 ? 4.992   -54.967 -80.946  1.00 95.59  ? 173  TYR   C CG   1 
ATOM   18783 C  CD1  . TYR   C  3  173 ? 4.164   -54.315 -81.850  1.00 99.29  ? 173  TYR   C CD1  1 
ATOM   18784 C  CD2  . TYR   C  3  173 ? 4.921   -54.597 -79.609  1.00 97.29  ? 173  TYR   C CD2  1 
ATOM   18785 C  CE1  . TYR   C  3  173 ? 3.313   -53.311 -81.444  1.00 100.41 ? 173  TYR   C CE1  1 
ATOM   18786 C  CE2  . TYR   C  3  173 ? 4.066   -53.594 -79.191  1.00 102.90 ? 173  TYR   C CE2  1 
ATOM   18787 C  CZ   . TYR   C  3  173 ? 3.263   -52.956 -80.115  1.00 106.61 ? 173  TYR   C CZ   1 
ATOM   18788 O  OH   . TYR   C  3  173 ? 2.407   -51.956 -79.715  1.00 115.69 ? 173  TYR   C OH   1 
ATOM   18789 H  H    . TYR   C  3  173 ? 6.070   -54.823 -83.724  1.00 107.70 ? 173  TYR   C H    1 
ATOM   18790 H  HA   . TYR   C  3  173 ? 7.800   -55.259 -81.700  1.00 106.94 ? 173  TYR   C HA   1 
ATOM   18791 H  HB2  . TYR   C  3  173 ? 5.391   -56.702 -81.913  1.00 109.36 ? 173  TYR   C HB2  1 
ATOM   18792 H  HB3  . TYR   C  3  173 ? 6.274   -56.499 -80.607  1.00 109.36 ? 173  TYR   C HB3  1 
ATOM   18793 H  HD1  . TYR   C  3  173 ? 4.185   -54.560 -82.746  1.00 119.19 ? 173  TYR   C HD1  1 
ATOM   18794 H  HD2  . TYR   C  3  173 ? 5.458   -55.030 -78.986  1.00 116.78 ? 173  TYR   C HD2  1 
ATOM   18795 H  HE1  . TYR   C  3  173 ? 2.775   -52.875 -82.065  1.00 120.53 ? 173  TYR   C HE1  1 
ATOM   18796 H  HE2  . TYR   C  3  173 ? 4.032   -53.350 -78.294  1.00 123.52 ? 173  TYR   C HE2  1 
ATOM   18797 H  HH   . TYR   C  3  173 ? 1.763   -52.282 -79.288  1.00 138.86 ? 173  TYR   C HH   1 
ATOM   18798 N  N    . SER   C  3  174 ? 8.079   -57.853 -82.316  1.00 83.93  ? 174  SER   C N    1 
ATOM   18799 C  CA   . SER   C  3  174 ? 8.597   -59.065 -82.942  1.00 78.98  ? 174  SER   C CA   1 
ATOM   18800 C  C    . SER   C  3  174 ? 8.253   -60.287 -82.096  1.00 75.83  ? 174  SER   C C    1 
ATOM   18801 O  O    . SER   C  3  174 ? 7.998   -60.189 -80.893  1.00 77.32  ? 174  SER   C O    1 
ATOM   18802 C  CB   . SER   C  3  174 ? 10.113  -58.980 -83.162  1.00 77.81  ? 174  SER   C CB   1 
ATOM   18803 O  OG   . SER   C  3  174 ? 10.433  -57.949 -84.080  1.00 78.99  ? 174  SER   C OG   1 
ATOM   18804 H  H    . SER   C  3  174 ? 8.078   -57.872 -81.456  1.00 100.75 ? 174  SER   C H    1 
ATOM   18805 H  HA   . SER   C  3  174 ? 8.160   -59.176 -83.801  1.00 94.82  ? 174  SER   C HA   1 
ATOM   18806 H  HB2  . SER   C  3  174 ? 10.545  -58.792 -82.314  1.00 93.41  ? 174  SER   C HB2  1 
ATOM   18807 H  HB3  . SER   C  3  174 ? 10.429  -59.826 -83.515  1.00 93.41  ? 174  SER   C HB3  1 
ATOM   18808 H  HG   . SER   C  3  174 ? 11.216  -58.053 -84.367  1.00 94.83  ? 174  SER   C HG   1 
ATOM   18809 N  N    . PHE   C  3  175 ? 8.277   -61.450 -82.752  1.00 75.66  ? 175  PHE   C N    1 
ATOM   18810 C  CA   . PHE   C  3  175 ? 7.788   -62.712 -82.203  1.00 80.55  ? 175  PHE   C CA   1 
ATOM   18811 C  C    . PHE   C  3  175 ? 8.744   -63.821 -82.620  1.00 82.46  ? 175  PHE   C C    1 
ATOM   18812 O  O    . PHE   C  3  175 ? 9.128   -63.895 -83.791  1.00 82.13  ? 175  PHE   C O    1 
ATOM   18813 C  CB   . PHE   C  3  175 ? 6.369   -62.993 -82.727  1.00 85.33  ? 175  PHE   C CB   1 
ATOM   18814 C  CG   . PHE   C  3  175 ? 5.652   -64.132 -82.044  1.00 87.48  ? 175  PHE   C CG   1 
ATOM   18815 C  CD1  . PHE   C  3  175 ? 6.091   -65.442 -82.168  1.00 88.39  ? 175  PHE   C CD1  1 
ATOM   18816 C  CD2  . PHE   C  3  175 ? 4.496   -63.890 -81.321  1.00 91.30  ? 175  PHE   C CD2  1 
ATOM   18817 C  CE1  . PHE   C  3  175 ? 5.407   -66.480 -81.552  1.00 90.66  ? 175  PHE   C CE1  1 
ATOM   18818 C  CE2  . PHE   C  3  175 ? 3.810   -64.922 -80.711  1.00 93.24  ? 175  PHE   C CE2  1 
ATOM   18819 C  CZ   . PHE   C  3  175 ? 4.265   -66.216 -80.824  1.00 92.28  ? 175  PHE   C CZ   1 
ATOM   18820 H  H    . PHE   C  3  175 ? 8.585   -61.535 -83.550  1.00 90.83  ? 175  PHE   C H    1 
ATOM   18821 H  HA   . PHE   C  3  175 ? 7.764   -62.684 -81.234  1.00 96.70  ? 175  PHE   C HA   1 
ATOM   18822 H  HB2  . PHE   C  3  175 ? 5.831   -62.195 -82.603  1.00 102.43 ? 175  PHE   C HB2  1 
ATOM   18823 H  HB3  . PHE   C  3  175 ? 6.427   -63.211 -83.671  1.00 102.43 ? 175  PHE   C HB3  1 
ATOM   18824 H  HD1  . PHE   C  3  175 ? 6.851   -65.627 -82.671  1.00 106.10 ? 175  PHE   C HD1  1 
ATOM   18825 H  HD2  . PHE   C  3  175 ? 4.178   -63.019 -81.245  1.00 109.60 ? 175  PHE   C HD2  1 
ATOM   18826 H  HE1  . PHE   C  3  175 ? 5.718   -67.353 -81.629  1.00 108.83 ? 175  PHE   C HE1  1 
ATOM   18827 H  HE2  . PHE   C  3  175 ? 3.039   -64.741 -80.222  1.00 111.93 ? 175  PHE   C HE2  1 
ATOM   18828 H  HZ   . PHE   C  3  175 ? 3.804   -66.910 -80.411  1.00 110.78 ? 175  PHE   C HZ   1 
ATOM   18829 N  N    . SER   C  3  176 ? 9.130   -64.673 -81.671  1.00 84.89  ? 176  SER   C N    1 
ATOM   18830 C  CA   . SER   C  3  176 ? 9.971   -65.835 -81.942  1.00 80.92  ? 176  SER   C CA   1 
ATOM   18831 C  C    . SER   C  3  176 ? 9.246   -67.094 -81.495  1.00 80.59  ? 176  SER   C C    1 
ATOM   18832 O  O    . SER   C  3  176 ? 8.752   -67.160 -80.364  1.00 84.48  ? 176  SER   C O    1 
ATOM   18833 C  CB   . SER   C  3  176 ? 11.320  -65.733 -81.223  1.00 79.20  ? 176  SER   C CB   1 
ATOM   18834 O  OG   . SER   C  3  176 ? 11.939  -67.006 -81.116  1.00 79.64  ? 176  SER   C OG   1 
ATOM   18835 H  H    . SER   C  3  176 ? 8.911   -64.596 -80.843  1.00 101.91 ? 176  SER   C H    1 
ATOM   18836 H  HA   . SER   C  3  176 ? 10.137  -65.889 -82.896  1.00 97.14  ? 176  SER   C HA   1 
ATOM   18837 H  HB2  . SER   C  3  176 ? 11.901  -65.142 -81.727  1.00 95.08  ? 176  SER   C HB2  1 
ATOM   18838 H  HB3  . SER   C  3  176 ? 11.176  -65.377 -80.332  1.00 95.08  ? 176  SER   C HB3  1 
ATOM   18839 H  HG   . SER   C  3  176 ? 11.589  -67.443 -80.490  1.00 95.61  ? 176  SER   C HG   1 
ATOM   18840 N  N    . SER   C  3  177 ? 9.194   -68.094 -82.372  1.00 77.77  ? 177  SER   C N    1 
ATOM   18841 C  CA   . SER   C  3  177 ? 8.510   -69.347 -82.083  1.00 77.77  ? 177  SER   C CA   1 
ATOM   18842 C  C    . SER   C  3  177 ? 9.446   -70.515 -82.352  1.00 79.06  ? 177  SER   C C    1 
ATOM   18843 O  O    . SER   C  3  177 ? 10.056  -70.593 -83.423  1.00 79.56  ? 177  SER   C O    1 
ATOM   18844 C  CB   . SER   C  3  177 ? 7.237   -69.490 -82.920  1.00 75.29  ? 177  SER   C CB   1 
ATOM   18845 O  OG   . SER   C  3  177 ? 6.414   -70.517 -82.401  1.00 74.36  ? 177  SER   C OG   1 
ATOM   18846 H  H    . SER   C  3  177 ? 9.553   -68.068 -83.153  1.00 93.37  ? 177  SER   C H    1 
ATOM   18847 H  HA   . SER   C  3  177 ? 8.267   -69.367 -81.144  1.00 93.36  ? 177  SER   C HA   1 
ATOM   18848 H  HB2  . SER   C  3  177 ? 6.749   -68.651 -82.901  1.00 90.38  ? 177  SER   C HB2  1 
ATOM   18849 H  HB3  . SER   C  3  177 ? 7.482   -69.710 -83.833  1.00 90.38  ? 177  SER   C HB3  1 
ATOM   18850 H  HG   . SER   C  3  177 ? 6.486   -70.548 -81.565  1.00 89.27  ? 177  SER   C HG   1 
ATOM   18851 N  N    . THR   C  3  178 ? 9.546   -71.424 -81.382  1.00 77.64  ? 178  THR   C N    1 
ATOM   18852 C  CA   . THR   C  3  178 ? 10.413  -72.592 -81.477  1.00 79.45  ? 178  THR   C CA   1 
ATOM   18853 C  C    . THR   C  3  178 ? 9.612   -73.834 -81.120  1.00 86.76  ? 178  THR   C C    1 
ATOM   18854 O  O    . THR   C  3  178 ? 9.015   -73.901 -80.041  1.00 92.32  ? 178  THR   C O    1 
ATOM   18855 C  CB   . THR   C  3  178 ? 11.624  -72.463 -80.547  1.00 74.77  ? 178  THR   C CB   1 
ATOM   18856 O  OG1  . THR   C  3  178 ? 12.380  -71.297 -80.896  1.00 67.30  ? 178  THR   C OG1  1 
ATOM   18857 C  CG2  . THR   C  3  178 ? 12.515  -73.697 -80.649  1.00 74.84  ? 178  THR   C CG2  1 
ATOM   18858 H  H    . THR   C  3  178 ? 9.109   -71.382 -80.643  1.00 93.21  ? 178  THR   C H    1 
ATOM   18859 H  HA   . THR   C  3  178 ? 10.728  -72.678 -82.390  1.00 95.38  ? 178  THR   C HA   1 
ATOM   18860 H  HB   . THR   C  3  178 ? 11.319  -72.384 -79.629  1.00 89.76  ? 178  THR   C HB   1 
ATOM   18861 H  HG1  . THR   C  3  178 ? 12.950  -71.135 -80.300  1.00 80.80  ? 178  THR   C HG1  1 
ATOM   18862 H  HG21 . THR   C  3  178 ? 13.312  -73.577 -80.110  1.00 89.84  ? 178  THR   C HG21 1 
ATOM   18863 H  HG22 . THR   C  3  178 ? 12.036  -74.479 -80.333  1.00 89.84  ? 178  THR   C HG22 1 
ATOM   18864 H  HG23 . THR   C  3  178 ? 12.777  -73.841 -81.572  1.00 89.84  ? 178  THR   C HG23 1 
ATOM   18865 N  N    . LEU   C  3  179 ? 9.607   -74.811 -82.021  1.00 88.22  ? 179  LEU   C N    1 
ATOM   18866 C  CA   . LEU   C  3  179 ? 9.021   -76.122 -81.778  1.00 88.85  ? 179  LEU   C CA   1 
ATOM   18867 C  C    . LEU   C  3  179 ? 10.148  -77.128 -81.591  1.00 86.25  ? 179  LEU   C C    1 
ATOM   18868 O  O    . LEU   C  3  179 ? 11.024  -77.246 -82.452  1.00 81.36  ? 179  LEU   C O    1 
ATOM   18869 C  CB   . LEU   C  3  179 ? 8.119   -76.545 -82.939  1.00 90.55  ? 179  LEU   C CB   1 
ATOM   18870 C  CG   . LEU   C  3  179 ? 7.733   -78.027 -82.989  1.00 95.39  ? 179  LEU   C CG   1 
ATOM   18871 C  CD1  . LEU   C  3  179 ? 6.840   -78.405 -81.816  1.00 99.45  ? 179  LEU   C CD1  1 
ATOM   18872 C  CD2  . LEU   C  3  179 ? 7.060   -78.356 -84.309  1.00 96.97  ? 179  LEU   C CD2  1 
ATOM   18873 H  H    . LEU   C  3  179 ? 9.948   -74.734 -82.807  1.00 105.90 ? 179  LEU   C H    1 
ATOM   18874 H  HA   . LEU   C  3  179 ? 8.481   -76.100 -80.972  1.00 106.65 ? 179  LEU   C HA   1 
ATOM   18875 H  HB2  . LEU   C  3  179 ? 7.295   -76.036 -82.882  1.00 108.69 ? 179  LEU   C HB2  1 
ATOM   18876 H  HB3  . LEU   C  3  179 ? 8.578   -76.341 -83.768  1.00 108.69 ? 179  LEU   C HB3  1 
ATOM   18877 H  HG   . LEU   C  3  179 ? 8.541   -78.560 -82.921  1.00 114.51 ? 179  LEU   C HG   1 
ATOM   18878 H  HD11 . LEU   C  3  179 ? 6.992   -79.336 -81.590  1.00 119.37 ? 179  LEU   C HD11 1 
ATOM   18879 H  HD12 . LEU   C  3  179 ? 7.059   -77.840 -81.058  1.00 119.37 ? 179  LEU   C HD12 1 
ATOM   18880 H  HD13 . LEU   C  3  179 ? 5.913   -78.273 -82.069  1.00 119.37 ? 179  LEU   C HD13 1 
ATOM   18881 H  HD21 . LEU   C  3  179 ? 6.557   -79.180 -84.211  1.00 116.40 ? 179  LEU   C HD21 1 
ATOM   18882 H  HD22 . LEU   C  3  179 ? 6.463   -77.631 -84.549  1.00 116.40 ? 179  LEU   C HD22 1 
ATOM   18883 H  HD23 . LEU   C  3  179 ? 7.740   -78.464 -84.992  1.00 116.40 ? 179  LEU   C HD23 1 
ATOM   18884 N  N    . THR   C  3  180 ? 10.119  -77.856 -80.477  1.00 91.55  ? 180  THR   C N    1 
ATOM   18885 C  CA   . THR   C  3  180 ? 11.168  -78.807 -80.136  1.00 101.10 ? 180  THR   C CA   1 
ATOM   18886 C  C    . THR   C  3  180 ? 10.600  -80.218 -80.133  1.00 109.25 ? 180  THR   C C    1 
ATOM   18887 O  O    . THR   C  3  180 ? 9.562   -80.475 -79.513  1.00 112.73 ? 180  THR   C O    1 
ATOM   18888 C  CB   . THR   C  3  180 ? 11.787  -78.486 -78.772  1.00 106.09 ? 180  THR   C CB   1 
ATOM   18889 O  OG1  . THR   C  3  180 ? 10.851  -78.792 -77.730  1.00 116.23 ? 180  THR   C OG1  1 
ATOM   18890 C  CG2  . THR   C  3  180 ? 12.170  -77.013 -78.695  1.00 98.73  ? 180  THR   C CG2  1 
ATOM   18891 H  H    . THR   C  3  180 ? 9.489   -77.813 -79.893  1.00 109.90 ? 180  THR   C H    1 
ATOM   18892 H  HA   . THR   C  3  180 ? 11.866  -78.764 -80.809  1.00 121.36 ? 180  THR   C HA   1 
ATOM   18893 H  HB   . THR   C  3  180 ? 12.589  -79.018 -78.648  1.00 127.34 ? 180  THR   C HB   1 
ATOM   18894 H  HG1  . THR   C  3  180 ? 10.072  -78.816 -78.042  1.00 139.51 ? 180  THR   C HG1  1 
ATOM   18895 H  HG21 . THR   C  3  180 ? 12.854  -76.883 -78.020  1.00 118.52 ? 180  THR   C HG21 1 
ATOM   18896 H  HG22 . THR   C  3  180 ? 12.512  -76.714 -79.552  1.00 118.52 ? 180  THR   C HG22 1 
ATOM   18897 H  HG23 . THR   C  3  180 ? 11.393  -76.480 -78.463  1.00 118.52 ? 180  THR   C HG23 1 
ATOM   18898 N  N    . LEU   C  3  181 ? 11.284  -81.127 -80.826  1.00 111.47 ? 181  LEU   C N    1 
ATOM   18899 C  CA   . LEU   C  3  181 ? 10.886  -82.523 -80.902  1.00 115.97 ? 181  LEU   C CA   1 
ATOM   18900 C  C    . LEU   C  3  181 ? 12.116  -83.399 -80.719  1.00 117.44 ? 181  LEU   C C    1 
ATOM   18901 O  O    . LEU   C  3  181 ? 13.256  -82.933 -80.783  1.00 112.65 ? 181  LEU   C O    1 
ATOM   18902 C  CB   . LEU   C  3  181 ? 10.219  -82.854 -82.242  1.00 115.97 ? 181  LEU   C CB   1 
ATOM   18903 C  CG   . LEU   C  3  181 ? 9.132   -81.914 -82.760  1.00 110.85 ? 181  LEU   C CG   1 
ATOM   18904 C  CD1  . LEU   C  3  181 ? 8.960   -82.131 -84.255  1.00 114.48 ? 181  LEU   C CD1  1 
ATOM   18905 C  CD2  . LEU   C  3  181 ? 7.820   -82.131 -82.022  1.00 109.40 ? 181  LEU   C CD2  1 
ATOM   18906 H  H    . LEU   C  3  181 ? 11.999  -80.951 -81.271  1.00 133.81 ? 181  LEU   C H    1 
ATOM   18907 H  HA   . LEU   C  3  181 ? 10.256  -82.703 -80.187  1.00 139.20 ? 181  LEU   C HA   1 
ATOM   18908 H  HB2  . LEU   C  3  181 ? 10.913  -82.875 -82.919  1.00 139.21 ? 181  LEU   C HB2  1 
ATOM   18909 H  HB3  . LEU   C  3  181 ? 9.811   -83.730 -82.158  1.00 139.21 ? 181  LEU   C HB3  1 
ATOM   18910 H  HG   . LEU   C  3  181 ? 9.393   -80.993 -82.602  1.00 133.06 ? 181  LEU   C HG   1 
ATOM   18911 H  HD11 . LEU   C  3  181 ? 8.047   -81.915 -84.503  1.00 137.41 ? 181  LEU   C HD11 1 
ATOM   18912 H  HD12 . LEU   C  3  181 ? 9.577   -81.553 -84.731  1.00 137.41 ? 181  LEU   C HD12 1 
ATOM   18913 H  HD13 . LEU   C  3  181 ? 9.149   -83.059 -84.464  1.00 137.41 ? 181  LEU   C HD13 1 
ATOM   18914 H  HD21 . LEU   C  3  181 ? 7.107   -81.688 -82.509  1.00 131.32 ? 181  LEU   C HD21 1 
ATOM   18915 H  HD22 . LEU   C  3  181 ? 7.641   -83.082 -81.967  1.00 131.32 ? 181  LEU   C HD22 1 
ATOM   18916 H  HD23 . LEU   C  3  181 ? 7.893   -81.756 -81.131  1.00 131.32 ? 181  LEU   C HD23 1 
ATOM   18917 N  N    . THR   C  3  182 ? 11.870  -84.687 -80.500  1.00 109.30 ? 182  THR   C N    1 
ATOM   18918 C  CA   . THR   C  3  182 ? 12.950  -85.657 -80.447  1.00 110.74 ? 182  THR   C CA   1 
ATOM   18919 C  C    . THR   C  3  182 ? 13.482  -85.903 -81.857  1.00 107.16 ? 182  THR   C C    1 
ATOM   18920 O  O    . THR   C  3  182 ? 12.793  -85.674 -82.855  1.00 105.28 ? 182  THR   C O    1 
ATOM   18921 C  CB   . THR   C  3  182 ? 12.475  -86.976 -79.832  1.00 120.14 ? 182  THR   C CB   1 
ATOM   18922 O  OG1  . THR   C  3  182 ? 11.805  -87.758 -80.830  1.00 126.94 ? 182  THR   C OG1  1 
ATOM   18923 C  CG2  . THR   C  3  182 ? 11.517  -86.734 -78.662  1.00 127.74 ? 182  THR   C CG2  1 
ATOM   18924 H  H    . THR   C  3  182 ? 11.087  -85.022 -80.380  1.00 131.20 ? 182  THR   C H    1 
ATOM   18925 H  HA   . THR   C  3  182 ? 13.668  -85.317 -79.889  1.00 132.93 ? 182  THR   C HA   1 
ATOM   18926 H  HB   . THR   C  3  182 ? 13.245  -87.459 -79.494  1.00 144.21 ? 182  THR   C HB   1 
ATOM   18927 H  HG1  . THR   C  3  182 ? 11.354  -88.364 -80.464  1.00 152.37 ? 182  THR   C HG1  1 
ATOM   18928 H  HG21 . THR   C  3  182 ? 11.225  -87.581 -78.291  1.00 153.33 ? 182  THR   C HG21 1 
ATOM   18929 H  HG22 . THR   C  3  182 ? 11.963  -86.224 -77.968  1.00 153.33 ? 182  THR   C HG22 1 
ATOM   18930 H  HG23 . THR   C  3  182 ? 10.740  -86.239 -78.966  1.00 153.33 ? 182  THR   C HG23 1 
ATOM   18931 N  N    . LYS   C  3  183 ? 14.729  -86.368 -81.938  1.00 105.95 ? 183  LYS   C N    1 
ATOM   18932 C  CA   . LYS   C  3  183 ? 15.309  -86.651 -83.247  1.00 110.50 ? 183  LYS   C CA   1 
ATOM   18933 C  C    . LYS   C  3  183 ? 14.499  -87.712 -83.979  1.00 111.39 ? 183  LYS   C C    1 
ATOM   18934 O  O    . LYS   C  3  183 ? 14.142  -87.542 -85.150  1.00 109.26 ? 183  LYS   C O    1 
ATOM   18935 C  CB   . LYS   C  3  183 ? 16.764  -87.092 -83.105  1.00 113.67 ? 183  LYS   C CB   1 
ATOM   18936 C  CG   . LYS   C  3  183 ? 17.309  -87.788 -84.346  1.00 112.38 ? 183  LYS   C CG   1 
ATOM   18937 C  CD   . LYS   C  3  183 ? 18.759  -87.439 -84.585  1.00 103.88 ? 183  LYS   C CD   1 
ATOM   18938 C  CE   . LYS   C  3  183 ? 19.560  -88.659 -84.966  1.00 100.03 ? 183  LYS   C CE   1 
ATOM   18939 N  NZ   . LYS   C  3  183 ? 21.001  -88.374 -84.879  1.00 91.66  ? 183  LYS   C NZ   1 
ATOM   18940 H  H    . LYS   C  3  183 ? 15.246  -86.524 -81.268  1.00 127.18 ? 183  LYS   C H    1 
ATOM   18941 H  HA   . LYS   C  3  183 ? 15.297  -85.836 -83.773  1.00 132.64 ? 183  LYS   C HA   1 
ATOM   18942 H  HB2  . LYS   C  3  183 ? 17.313  -86.310 -82.937  1.00 136.45 ? 183  LYS   C HB2  1 
ATOM   18943 H  HB3  . LYS   C  3  183 ? 16.833  -87.711 -82.362  1.00 136.45 ? 183  LYS   C HB3  1 
ATOM   18944 H  HG2  . LYS   C  3  183 ? 17.241  -88.749 -84.231  1.00 134.90 ? 183  LYS   C HG2  1 
ATOM   18945 H  HG3  . LYS   C  3  183 ? 16.796  -87.510 -85.121  1.00 134.90 ? 183  LYS   C HG3  1 
ATOM   18946 H  HD2  . LYS   C  3  183 ? 18.820  -86.795 -85.309  1.00 124.69 ? 183  LYS   C HD2  1 
ATOM   18947 H  HD3  . LYS   C  3  183 ? 19.138  -87.064 -83.775  1.00 124.69 ? 183  LYS   C HD3  1 
ATOM   18948 H  HE2  . LYS   C  3  183 ? 19.351  -89.387 -84.359  1.00 120.07 ? 183  LYS   C HE2  1 
ATOM   18949 H  HE3  . LYS   C  3  183 ? 19.349  -88.916 -85.877  1.00 120.07 ? 183  LYS   C HE3  1 
ATOM   18950 H  HZ1  . LYS   C  3  183 ? 21.418  -88.692 -85.598  1.00 110.03 ? 183  LYS   C HZ1  1 
ATOM   18951 H  HZ2  . LYS   C  3  183 ? 21.135  -87.495 -84.833  1.00 110.03 ? 183  LYS   C HZ2  1 
ATOM   18952 H  HZ3  . LYS   C  3  183 ? 21.344  -88.757 -84.153  1.00 110.03 ? 183  LYS   C HZ3  1 
ATOM   18953 N  N    . ASP   C  3  184 ? 14.201  -88.821 -83.300  1.00 115.63 ? 184  ASP   C N    1 
ATOM   18954 C  CA   . ASP   C  3  184 ? 13.410  -89.877 -83.922  1.00 121.89 ? 184  ASP   C CA   1 
ATOM   18955 C  C    . ASP   C  3  184 ? 12.082  -89.331 -84.431  1.00 123.32 ? 184  ASP   C C    1 
ATOM   18956 O  O    . ASP   C  3  184 ? 11.671  -89.621 -85.560  1.00 127.19 ? 184  ASP   C O    1 
ATOM   18957 C  CB   . ASP   C  3  184 ? 13.188  -91.014 -82.927  1.00 126.73 ? 184  ASP   C CB   1 
ATOM   18958 C  CG   . ASP   C  3  184 ? 14.487  -91.653 -82.478  1.00 124.66 ? 184  ASP   C CG   1 
ATOM   18959 O  OD1  . ASP   C  3  184 ? 15.500  -91.508 -83.195  1.00 121.37 ? 184  ASP   C OD1  1 
ATOM   18960 O  OD2  . ASP   C  3  184 ? 14.496  -92.301 -81.410  1.00 125.11 ? 184  ASP   C OD2  1 
ATOM   18961 H  H    . ASP   C  3  184 ? 14.441  -88.983 -82.490  1.00 138.79 ? 184  ASP   C H    1 
ATOM   18962 H  HA   . ASP   C  3  184 ? 13.897  -90.235 -84.681  1.00 146.31 ? 184  ASP   C HA   1 
ATOM   18963 H  HB2  . ASP   C  3  184 ? 12.737  -90.666 -82.142  1.00 152.12 ? 184  ASP   C HB2  1 
ATOM   18964 H  HB3  . ASP   C  3  184 ? 12.644  -91.700 -83.345  1.00 152.12 ? 184  ASP   C HB3  1 
ATOM   18965 N  N    . GLU   C  3  185 ? 11.402  -88.524 -83.614  1.00 121.28 ? 185  GLU   C N    1 
ATOM   18966 C  CA   . GLU   C  3  185 ? 10.148  -87.921 -84.053  1.00 125.85 ? 185  GLU   C CA   1 
ATOM   18967 C  C    . GLU   C  3  185 ? 10.378  -86.977 -85.226  1.00 122.69 ? 185  GLU   C C    1 
ATOM   18968 O  O    . GLU   C  3  185 ? 9.618   -86.988 -86.201  1.00 124.65 ? 185  GLU   C O    1 
ATOM   18969 C  CB   . GLU   C  3  185 ? 9.490   -87.179 -82.891  1.00 128.68 ? 185  GLU   C CB   1 
ATOM   18970 C  CG   . GLU   C  3  185 ? 8.029   -86.842 -83.119  1.00 134.75 ? 185  GLU   C CG   1 
ATOM   18971 C  CD   . GLU   C  3  185 ? 7.318   -86.469 -81.835  1.00 139.41 ? 185  GLU   C CD   1 
ATOM   18972 O  OE1  . GLU   C  3  185 ? 7.994   -85.996 -80.897  1.00 137.41 ? 185  GLU   C OE1  1 
ATOM   18973 O  OE2  . GLU   C  3  185 ? 6.086   -86.660 -81.758  1.00 145.47 ? 185  GLU   C OE2  1 
ATOM   18974 H  H    . GLU   C  3  185 ? 11.641  -88.315 -82.815  1.00 145.58 ? 185  GLU   C H    1 
ATOM   18975 H  HA   . GLU   C  3  185 ? 9.544   -88.622 -84.342  1.00 151.06 ? 185  GLU   C HA   1 
ATOM   18976 H  HB2  . GLU   C  3  185 ? 9.544   -87.734 -82.098  1.00 154.45 ? 185  GLU   C HB2  1 
ATOM   18977 H  HB3  . GLU   C  3  185 ? 9.965   -86.346 -82.746  1.00 154.45 ? 185  GLU   C HB3  1 
ATOM   18978 H  HG2  . GLU   C  3  185 ? 7.967   -86.089 -83.728  1.00 161.73 ? 185  GLU   C HG2  1 
ATOM   18979 H  HG3  . GLU   C  3  185 ? 7.580   -87.613 -83.500  1.00 161.73 ? 185  GLU   C HG3  1 
ATOM   18980 N  N    . TYR   C  3  186 ? 11.423  -86.150 -85.147  1.00 117.37 ? 186  TYR   C N    1 
ATOM   18981 C  CA   . TYR   C  3  186 ? 11.750  -85.272 -86.264  1.00 113.75 ? 186  TYR   C CA   1 
ATOM   18982 C  C    . TYR   C  3  186 ? 12.011  -86.073 -87.533  1.00 115.52 ? 186  TYR   C C    1 
ATOM   18983 O  O    . TYR   C  3  186 ? 11.584  -85.680 -88.625  1.00 119.38 ? 186  TYR   C O    1 
ATOM   18984 C  CB   . TYR   C  3  186 ? 12.967  -84.414 -85.918  1.00 106.38 ? 186  TYR   C CB   1 
ATOM   18985 C  CG   . TYR   C  3  186 ? 13.367  -83.470 -87.027  1.00 101.67 ? 186  TYR   C CG   1 
ATOM   18986 C  CD1  . TYR   C  3  186 ? 12.548  -82.409 -87.383  1.00 100.15 ? 186  TYR   C CD1  1 
ATOM   18987 C  CD2  . TYR   C  3  186 ? 14.559  -83.640 -87.718  1.00 100.18 ? 186  TYR   C CD2  1 
ATOM   18988 C  CE1  . TYR   C  3  186 ? 12.902  -81.543 -88.397  1.00 99.80  ? 186  TYR   C CE1  1 
ATOM   18989 C  CE2  . TYR   C  3  186 ? 14.923  -82.777 -88.735  1.00 100.18 ? 186  TYR   C CE2  1 
ATOM   18990 C  CZ   . TYR   C  3  186 ? 14.089  -81.731 -89.070  1.00 101.20 ? 186  TYR   C CZ   1 
ATOM   18991 O  OH   . TYR   C  3  186 ? 14.443  -80.867 -90.080  1.00 103.22 ? 186  TYR   C OH   1 
ATOM   18992 H  H    . TYR   C  3  186 ? 11.948  -86.081 -84.470  1.00 140.88 ? 186  TYR   C H    1 
ATOM   18993 H  HA   . TYR   C  3  186 ? 11.000  -84.679 -86.427  1.00 136.54 ? 186  TYR   C HA   1 
ATOM   18994 H  HB2  . TYR   C  3  186 ? 12.763  -83.882 -85.133  1.00 127.70 ? 186  TYR   C HB2  1 
ATOM   18995 H  HB3  . TYR   C  3  186 ? 13.721  -84.997 -85.737  1.00 127.70 ? 186  TYR   C HB3  1 
ATOM   18996 H  HD1  . TYR   C  3  186 ? 11.746  -82.279 -86.931  1.00 120.22 ? 186  TYR   C HD1  1 
ATOM   18997 H  HD2  . TYR   C  3  186 ? 15.122  -84.346 -87.494  1.00 120.25 ? 186  TYR   C HD2  1 
ATOM   18998 H  HE1  . TYR   C  3  186 ? 12.342  -80.836 -88.624  1.00 119.80 ? 186  TYR   C HE1  1 
ATOM   18999 H  HE2  . TYR   C  3  186 ? 15.725  -82.900 -89.189  1.00 120.26 ? 186  TYR   C HE2  1 
ATOM   19000 H  HH   . TYR   C  3  186 ? 15.089  -81.182 -90.515  1.00 123.90 ? 186  TYR   C HH   1 
ATOM   19001 N  N    . GLU   C  3  187 ? 12.706  -87.205 -87.407  1.00 116.08 ? 187  GLU   C N    1 
ATOM   19002 C  CA   . GLU   C  3  187 ? 13.054  -88.004 -88.574  1.00 121.30 ? 187  GLU   C CA   1 
ATOM   19003 C  C    . GLU   C  3  187 ? 11.848  -88.700 -89.192  1.00 131.40 ? 187  GLU   C C    1 
ATOM   19004 O  O    . GLU   C  3  187 ? 11.920  -89.116 -90.353  1.00 141.32 ? 187  GLU   C O    1 
ATOM   19005 C  CB   . GLU   C  3  187 ? 14.113  -89.044 -88.196  1.00 121.80 ? 187  GLU   C CB   1 
ATOM   19006 C  CG   . GLU   C  3  187 ? 15.482  -88.452 -87.891  1.00 118.46 ? 187  GLU   C CG   1 
ATOM   19007 C  CD   . GLU   C  3  187 ? 16.508  -89.504 -87.516  1.00 121.95 ? 187  GLU   C CD   1 
ATOM   19008 O  OE1  . GLU   C  3  187 ? 16.107  -90.637 -87.175  1.00 126.58 ? 187  GLU   C OE1  1 
ATOM   19009 O  OE2  . GLU   C  3  187 ? 17.716  -89.197 -87.566  1.00 121.27 ? 187  GLU   C OE2  1 
ATOM   19010 H  H    . GLU   C  3  187 ? 12.986  -87.527 -86.660  1.00 139.34 ? 187  GLU   C H    1 
ATOM   19011 H  HA   . GLU   C  3  187 ? 13.431  -87.416 -89.247  1.00 145.59 ? 187  GLU   C HA   1 
ATOM   19012 H  HB2  . GLU   C  3  187 ? 13.813  -89.519 -87.405  1.00 146.20 ? 187  GLU   C HB2  1 
ATOM   19013 H  HB3  . GLU   C  3  187 ? 14.217  -89.664 -88.936  1.00 146.20 ? 187  GLU   C HB3  1 
ATOM   19014 H  HG2  . GLU   C  3  187 ? 15.806  -87.984 -88.676  1.00 142.19 ? 187  GLU   C HG2  1 
ATOM   19015 H  HG3  . GLU   C  3  187 ? 15.401  -87.835 -87.147  1.00 142.19 ? 187  GLU   C HG3  1 
ATOM   19016 N  N    . ARG   C  3  188 ? 10.743  -88.832 -88.456  1.00 129.17 ? 188  ARG   C N    1 
ATOM   19017 C  CA   . ARG   C  3  188 ? 9.593   -89.557 -88.984  1.00 135.13 ? 188  ARG   C CA   1 
ATOM   19018 C  C    . ARG   C  3  188 ? 8.805   -88.742 -90.002  1.00 136.36 ? 188  ARG   C C    1 
ATOM   19019 O  O    . ARG   C  3  188 ? 8.218   -89.317 -90.925  1.00 138.35 ? 188  ARG   C O    1 
ATOM   19020 C  CB   . ARG   C  3  188 ? 8.668   -89.988 -87.843  1.00 139.43 ? 188  ARG   C CB   1 
ATOM   19021 C  CG   . ARG   C  3  188 ? 9.240   -91.105 -86.990  1.00 141.82 ? 188  ARG   C CG   1 
ATOM   19022 C  CD   . ARG   C  3  188 ? 8.153   -91.897 -86.291  1.00 150.09 ? 188  ARG   C CD   1 
ATOM   19023 N  NE   . ARG   C  3  188 ? 8.648   -93.198 -85.849  1.00 154.42 ? 188  ARG   C NE   1 
ATOM   19024 C  CZ   . ARG   C  3  188 ? 8.699   -94.284 -86.616  1.00 161.20 ? 188  ARG   C CZ   1 
ATOM   19025 N  NH1  . ARG   C  3  188 ? 8.284   -94.238 -87.875  1.00 165.26 ? 188  ARG   C NH1  1 
ATOM   19026 N  NH2  . ARG   C  3  188 ? 9.169   -95.421 -86.121  1.00 164.29 ? 188  ARG   C NH2  1 
ATOM   19027 H  H    . ARG   C  3  188 ? 10.637  -88.516 -87.663  1.00 155.05 ? 188  ARG   C H    1 
ATOM   19028 H  HA   . ARG   C  3  188 ? 9.918   -90.355 -89.429  1.00 162.19 ? 188  ARG   C HA   1 
ATOM   19029 H  HB2  . ARG   C  3  188 ? 8.508   -89.225 -87.265  1.00 167.35 ? 188  ARG   C HB2  1 
ATOM   19030 H  HB3  . ARG   C  3  188 ? 7.831   -90.300 -88.220  1.00 167.35 ? 188  ARG   C HB3  1 
ATOM   19031 H  HG2  . ARG   C  3  188 ? 9.742   -91.713 -87.555  1.00 170.22 ? 188  ARG   C HG2  1 
ATOM   19032 H  HG3  . ARG   C  3  188 ? 9.821   -90.724 -86.313  1.00 170.22 ? 188  ARG   C HG3  1 
ATOM   19033 H  HD2  . ARG   C  3  188 ? 7.847   -91.406 -85.513  1.00 180.15 ? 188  ARG   C HD2  1 
ATOM   19034 H  HD3  . ARG   C  3  188 ? 7.415   -92.042 -86.904  1.00 180.15 ? 188  ARG   C HD3  1 
ATOM   19035 H  HE   . ARG   C  3  188 ? 8.925   -93.267 -85.038  1.00 185.35 ? 188  ARG   C HE   1 
ATOM   19036 H  HH11 . ARG   C  3  188 ? 7.979   -93.503 -88.200  1.00 198.35 ? 188  ARG   C HH11 1 
ATOM   19037 H  HH12 . ARG   C  3  188 ? 8.320   -94.943 -88.366  1.00 198.35 ? 188  ARG   C HH12 1 
ATOM   19038 H  HH21 . ARG   C  3  188 ? 9.440   -95.456 -85.305  1.00 197.18 ? 188  ARG   C HH21 1 
ATOM   19039 H  HH22 . ARG   C  3  188 ? 9.203   -96.124 -86.615  1.00 197.18 ? 188  ARG   C HH22 1 
ATOM   19040 N  N    . HIS   C  3  189 ? 8.784   -87.421 -89.862  1.00 133.95 ? 189  HIS   C N    1 
ATOM   19041 C  CA   . HIS   C  3  189 ? 7.954   -86.551 -90.681  1.00 137.11 ? 189  HIS   C CA   1 
ATOM   19042 C  C    . HIS   C  3  189 ? 8.811   -85.769 -91.668  1.00 136.93 ? 189  HIS   C C    1 
ATOM   19043 O  O    . HIS   C  3  189 ? 10.029  -85.652 -91.511  1.00 137.78 ? 189  HIS   C O    1 
ATOM   19044 C  CB   . HIS   C  3  189 ? 7.147   -85.605 -89.789  1.00 131.68 ? 189  HIS   C CB   1 
ATOM   19045 C  CG   . HIS   C  3  189 ? 6.447   -86.304 -88.665  1.00 127.72 ? 189  HIS   C CG   1 
ATOM   19046 N  ND1  . HIS   C  3  189 ? 5.387   -87.162 -88.866  1.00 132.37 ? 189  HIS   C ND1  1 
ATOM   19047 C  CD2  . HIS   C  3  189 ? 6.670   -86.290 -87.329  1.00 124.03 ? 189  HIS   C CD2  1 
ATOM   19048 C  CE1  . HIS   C  3  189 ? 4.980   -87.637 -87.702  1.00 134.07 ? 189  HIS   C CE1  1 
ATOM   19049 N  NE2  . HIS   C  3  189 ? 5.742   -87.123 -86.754  1.00 129.90 ? 189  HIS   C NE2  1 
ATOM   19050 H  H    . HIS   C  3  189 ? 9.256   -86.995 -89.283  1.00 160.78 ? 189  HIS   C H    1 
ATOM   19051 H  HA   . HIS   C  3  189 ? 7.331   -87.081 -91.204  1.00 164.57 ? 189  HIS   C HA   1 
ATOM   19052 H  HB2  . HIS   C  3  189 ? 7.748   -84.949 -89.403  1.00 158.05 ? 189  HIS   C HB2  1 
ATOM   19053 H  HB3  . HIS   C  3  189 ? 6.474   -85.162 -90.329  1.00 158.05 ? 189  HIS   C HB3  1 
ATOM   19054 H  HD2  . HIS   C  3  189 ? 7.329   -85.806 -86.885  1.00 148.88 ? 189  HIS   C HD2  1 
ATOM   19055 H  HE1  . HIS   C  3  189 ? 4.278   -88.233 -87.573  1.00 160.92 ? 189  HIS   C HE1  1 
ATOM   19056 H  HE2  . HIS   C  3  189 ? 5.669   -87.284 -85.912  1.00 155.91 ? 189  HIS   C HE2  1 
ATOM   19057 N  N    . ASN   C  3  190 ? 8.155   -85.228 -92.696  1.00 137.59 ? 190  ASN   C N    1 
ATOM   19058 C  CA   . ASN   C  3  190 ? 8.843   -84.624 -93.831  1.00 141.04 ? 190  ASN   C CA   1 
ATOM   19059 C  C    . ASN   C  3  190 ? 8.638   -83.120 -93.936  1.00 143.28 ? 190  ASN   C C    1 
ATOM   19060 O  O    . ASN   C  3  190 ? 9.612   -82.380 -94.101  1.00 145.18 ? 190  ASN   C O    1 
ATOM   19061 C  CB   . ASN   C  3  190 ? 8.384   -85.302 -95.133  1.00 146.63 ? 190  ASN   C CB   1 
ATOM   19062 C  CG   . ASN   C  3  190 ? 9.472   -85.332 -96.189  1.00 150.36 ? 190  ASN   C CG   1 
ATOM   19063 O  OD1  . ASN   C  3  190 ? 10.419  -86.112 -96.096  1.00 152.45 ? 190  ASN   C OD1  1 
ATOM   19064 N  ND2  . ASN   C  3  190 ? 9.338   -84.486 -97.204  1.00 152.40 ? 190  ASN   C ND2  1 
ATOM   19065 H  H    . ASN   C  3  190 ? 7.298   -85.201 -92.757  1.00 165.15 ? 190  ASN   C H    1 
ATOM   19066 H  HA   . ASN   C  3  190 ? 9.795   -84.774 -93.725  1.00 169.29 ? 190  ASN   C HA   1 
ATOM   19067 H  HB2  . ASN   C  3  190 ? 8.127   -86.217 -94.940  1.00 175.99 ? 190  ASN   C HB2  1 
ATOM   19068 H  HB3  . ASN   C  3  190 ? 7.627   -84.813 -95.494  1.00 175.99 ? 190  ASN   C HB3  1 
ATOM   19069 H  HD21 . ASN   C  3  190 ? 9.930   -84.466 -97.828  1.00 182.92 ? 190  ASN   C HD21 1 
ATOM   19070 H  HD22 . ASN   C  3  190 ? 8.660   -83.959 -97.238  1.00 182.92 ? 190  ASN   C HD22 1 
ATOM   19071 N  N    . SER   C  3  191 ? 7.400   -82.639 -93.854  1.00 139.67 ? 191  SER   C N    1 
ATOM   19072 C  CA   . SER   C  3  191 ? 7.114   -81.222 -94.026  1.00 134.89 ? 191  SER   C CA   1 
ATOM   19073 C  C    . SER   C  3  191 ? 6.986   -80.529 -92.674  1.00 126.32 ? 191  SER   C C    1 
ATOM   19074 O  O    . SER   C  3  191 ? 6.518   -81.114 -91.693  1.00 126.39 ? 191  SER   C O    1 
ATOM   19075 C  CB   . SER   C  3  191 ? 5.831   -81.012 -94.835  1.00 139.70 ? 191  SER   C CB   1 
ATOM   19076 O  OG   . SER   C  3  191 ? 4.682   -81.111 -94.013  1.00 143.21 ? 191  SER   C OG   1 
ATOM   19077 H  H    . SER   C  3  191 ? 6.705   -83.120 -93.697  1.00 167.64 ? 191  SER   C H    1 
ATOM   19078 H  HA   . SER   C  3  191 ? 7.848   -80.810 -94.509  1.00 161.90 ? 191  SER   C HA   1 
ATOM   19079 H  HB2  . SER   C  3  191 ? 5.854   -80.130 -95.238  1.00 167.68 ? 191  SER   C HB2  1 
ATOM   19080 H  HB3  . SER   C  3  191 ? 5.782   -81.691 -95.526  1.00 167.68 ? 191  SER   C HB3  1 
ATOM   19081 H  HG   . SER   C  3  191 ? 4.624   -80.436 -93.517  1.00 171.89 ? 191  SER   C HG   1 
ATOM   19082 N  N    . TYR   C  3  192 ? 7.405   -79.265 -92.639  1.00 119.02 ? 192  TYR   C N    1 
ATOM   19083 C  CA   . TYR   C  3  192 ? 7.374   -78.454 -91.428  1.00 111.65 ? 192  TYR   C CA   1 
ATOM   19084 C  C    . TYR   C  3  192 ? 7.004   -77.030 -91.810  1.00 115.21 ? 192  TYR   C C    1 
ATOM   19085 O  O    . TYR   C  3  192 ? 7.623   -76.447 -92.705  1.00 105.73 ? 192  TYR   C O    1 
ATOM   19086 C  CB   . TYR   C  3  192 ? 8.726   -78.493 -90.709  1.00 106.81 ? 192  TYR   C CB   1 
ATOM   19087 C  CG   . TYR   C  3  192 ? 9.035   -79.835 -90.080  1.00 108.62 ? 192  TYR   C CG   1 
ATOM   19088 C  CD1  . TYR   C  3  192 ? 8.602   -80.134 -88.795  1.00 108.98 ? 192  TYR   C CD1  1 
ATOM   19089 C  CD2  . TYR   C  3  192 ? 9.752   -80.805 -90.771  1.00 109.43 ? 192  TYR   C CD2  1 
ATOM   19090 C  CE1  . TYR   C  3  192 ? 8.876   -81.356 -88.214  1.00 111.32 ? 192  TYR   C CE1  1 
ATOM   19091 C  CE2  . TYR   C  3  192 ? 10.032  -82.033 -90.196  1.00 110.76 ? 192  TYR   C CE2  1 
ATOM   19092 C  CZ   . TYR   C  3  192 ? 9.591   -82.302 -88.917  1.00 111.59 ? 192  TYR   C CZ   1 
ATOM   19093 O  OH   . TYR   C  3  192 ? 9.863   -83.520 -88.336  1.00 112.39 ? 192  TYR   C OH   1 
ATOM   19094 H  H    . TYR   C  3  192 ? 7.719   -78.847 -93.321  1.00 142.86 ? 192  TYR   C H    1 
ATOM   19095 H  HA   . TYR   C  3  192 ? 6.700   -78.788 -90.816  1.00 134.02 ? 192  TYR   C HA   1 
ATOM   19096 H  HB2  . TYR   C  3  192 ? 9.428   -78.296 -91.349  1.00 128.21 ? 192  TYR   C HB2  1 
ATOM   19097 H  HB3  . TYR   C  3  192 ? 8.725   -77.827 -90.003  1.00 128.21 ? 192  TYR   C HB3  1 
ATOM   19098 H  HD1  . TYR   C  3  192 ? 8.119   -79.499 -88.318  1.00 130.82 ? 192  TYR   C HD1  1 
ATOM   19099 H  HD2  . TYR   C  3  192 ? 10.050  -80.625 -91.634  1.00 131.36 ? 192  TYR   C HD2  1 
ATOM   19100 H  HE1  . TYR   C  3  192 ? 8.580   -81.540 -87.351  1.00 133.63 ? 192  TYR   C HE1  1 
ATOM   19101 H  HE2  . TYR   C  3  192 ? 10.514  -82.672 -90.669  1.00 132.95 ? 192  TYR   C HE2  1 
ATOM   19102 H  HH   . TYR   C  3  192 ? 10.448  -83.926 -88.782  1.00 134.91 ? 192  TYR   C HH   1 
ATOM   19103 N  N    . THR   C  3  193 ? 6.005   -76.471 -91.127  1.00 117.69 ? 193  THR   C N    1 
ATOM   19104 C  CA   . THR   C  3  193 ? 5.370   -75.235 -91.559  1.00 122.89 ? 193  THR   C CA   1 
ATOM   19105 C  C    . THR   C  3  193 ? 5.138   -74.314 -90.370  1.00 117.02 ? 193  THR   C C    1 
ATOM   19106 O  O    . THR   C  3  193 ? 4.961   -74.763 -89.235  1.00 94.94  ? 193  THR   C O    1 
ATOM   19107 C  CB   . THR   C  3  193 ? 4.038   -75.529 -92.269  1.00 96.68  ? 193  THR   C CB   1 
ATOM   19108 O  OG1  . THR   C  3  193 ? 4.282   -76.353 -93.418  1.00 97.24  ? 193  THR   C OG1  1 
ATOM   19109 C  CG2  . THR   C  3  193 ? 3.344   -74.244 -92.705  1.00 112.47 ? 193  THR   C CG2  1 
ATOM   19110 H  H    . THR   C  3  193 ? 5.676   -76.796 -90.401  1.00 141.27 ? 193  THR   C H    1 
ATOM   19111 H  HA   . THR   C  3  193 ? 5.959   -74.764 -92.170  1.00 147.51 ? 193  THR   C HA   1 
ATOM   19112 H  HB   . THR   C  3  193 ? 3.446   -75.990 -91.654  1.00 115.83 ? 193  THR   C HB   1 
ATOM   19113 H  HG1  . THR   C  3  193 ? 3.561   -76.500 -93.823  1.00 116.50 ? 193  THR   C HG1  1 
ATOM   19114 H  HG21 . THR   C  3  193 ? 2.553   -74.454 -93.225  1.00 135.00 ? 193  THR   C HG21 1 
ATOM   19115 H  HG22 . THR   C  3  193 ? 3.082   -73.729 -91.926  1.00 135.00 ? 193  THR   C HG22 1 
ATOM   19116 H  HG23 . THR   C  3  193 ? 3.946   -73.710 -93.247  1.00 135.00 ? 193  THR   C HG23 1 
ATOM   19117 N  N    . CYS   C  3  194 ? 5.129   -73.011 -90.656  1.00 106.64 ? 194  CYS   C N    1 
ATOM   19118 C  CA   . CYS   C  3  194 ? 4.967   -71.962 -89.654  1.00 104.61 ? 194  CYS   C CA   1 
ATOM   19119 C  C    . CYS   C  3  194 ? 3.903   -70.991 -90.152  1.00 107.55 ? 194  CYS   C C    1 
ATOM   19120 O  O    . CYS   C  3  194 ? 4.157   -70.206 -91.072  1.00 105.87 ? 194  CYS   C O    1 
ATOM   19121 C  CB   . CYS   C  3  194 ? 6.294   -71.246 -89.405  1.00 101.64 ? 194  CYS   C CB   1 
ATOM   19122 S  SG   . CYS   C  3  194 ? 6.166   -69.684 -88.513  1.00 111.62 ? 194  CYS   C SG   1 
ATOM   19123 H  H    . CYS   C  3  194 ? 5.220   -72.701 -91.453  1.00 128.01 ? 194  CYS   C H    1 
ATOM   19124 H  HA   . CYS   C  3  194 ? 4.659   -72.345 -88.818  1.00 125.56 ? 194  CYS   C HA   1 
ATOM   19125 H  HB2  . CYS   C  3  194 ? 6.865   -71.832 -88.884  1.00 122.00 ? 194  CYS   C HB2  1 
ATOM   19126 H  HB3  . CYS   C  3  194 ? 6.707   -71.058 -90.262  1.00 122.00 ? 194  CYS   C HB3  1 
ATOM   19127 N  N    . GLU   C  3  195 ? 2.720   -71.037 -89.542  1.00 111.27 ? 195  GLU   C N    1 
ATOM   19128 C  CA   . GLU   C  3  195 ? 1.555   -70.285 -89.996  1.00 114.94 ? 195  GLU   C CA   1 
ATOM   19129 C  C    . GLU   C  3  195 ? 1.293   -69.116 -89.056  1.00 120.56 ? 195  GLU   C C    1 
ATOM   19130 O  O    . GLU   C  3  195 ? 1.029   -69.319 -87.866  1.00 110.78 ? 195  GLU   C O    1 
ATOM   19131 C  CB   . GLU   C  3  195 ? 0.322   -71.185 -90.069  1.00 116.59 ? 195  GLU   C CB   1 
ATOM   19132 C  CG   . GLU   C  3  195 ? 0.156   -71.913 -91.386  1.00 113.86 ? 195  GLU   C CG   1 
ATOM   19133 C  CD   . GLU   C  3  195 ? -1.155  -72.671 -91.465  1.00 118.10 ? 195  GLU   C CD   1 
ATOM   19134 O  OE1  . GLU   C  3  195 ? -1.132  -73.868 -91.818  1.00 118.91 ? 195  GLU   C OE1  1 
ATOM   19135 O  OE2  . GLU   C  3  195 ? -2.208  -72.069 -91.166  1.00 123.15 ? 195  GLU   C OE2  1 
ATOM   19136 H  H    . GLU   C  3  195 ? 2.564   -71.512 -88.842  1.00 133.56 ? 195  GLU   C H    1 
ATOM   19137 H  HA   . GLU   C  3  195 ? 1.742   -69.925 -90.877  1.00 137.96 ? 195  GLU   C HA   1 
ATOM   19138 H  HB2  . GLU   C  3  195 ? 0.386   -71.855 -89.370  1.00 139.95 ? 195  GLU   C HB2  1 
ATOM   19139 H  HB3  . GLU   C  3  195 ? -0.468  -70.639 -89.933  1.00 139.95 ? 195  GLU   C HB3  1 
ATOM   19140 H  HG2  . GLU   C  3  195 ? 0.175   -71.268 -92.110  1.00 136.67 ? 195  GLU   C HG2  1 
ATOM   19141 H  HG3  . GLU   C  3  195 ? 0.879   -72.550 -91.491  1.00 136.67 ? 195  GLU   C HG3  1 
ATOM   19142 N  N    . ALA   C  3  196 ? 1.341   -67.902 -89.598  1.00 108.41 ? 196  ALA   C N    1 
ATOM   19143 C  CA   . ALA   C  3  196 ? 1.105   -66.683 -88.839  1.00 112.52 ? 196  ALA   C CA   1 
ATOM   19144 C  C    . ALA   C  3  196 ? -0.230  -66.068 -89.234  1.00 148.38 ? 196  ALA   C C    1 
ATOM   19145 O  O    . ALA   C  3  196 ? -0.555  -65.977 -90.422  1.00 114.68 ? 196  ALA   C O    1 
ATOM   19146 C  CB   . ALA   C  3  196 ? 2.228   -65.669 -89.070  1.00 111.52 ? 196  ALA   C CB   1 
ATOM   19147 H  H    . ALA   C  3  196 ? 1.513   -67.757 -90.428  1.00 129.91 ? 196  ALA   C H    1 
ATOM   19148 H  HA   . ALA   C  3  196 ? 1.072   -66.897 -87.893  1.00 134.84 ? 196  ALA   C HA   1 
ATOM   19149 H  HB1  . ALA   C  3  196 ? 2.039   -64.866 -88.560  1.00 133.64 ? 196  ALA   C HB1  1 
ATOM   19150 H  HB2  . ALA   C  3  196 ? 3.068   -66.056 -88.778  1.00 133.64 ? 196  ALA   C HB2  1 
ATOM   19151 H  HB3  . ALA   C  3  196 ? 2.273   -65.458 -90.016  1.00 133.64 ? 196  ALA   C HB3  1 
ATOM   19152 N  N    . THR   C  3  197 ? -1.000  -65.650 -88.232  1.00 155.51 ? 197  THR   C N    1 
ATOM   19153 C  CA   . THR   C  3  197 ? -2.262  -64.950 -88.439  1.00 154.35 ? 197  THR   C CA   1 
ATOM   19154 C  C    . THR   C  3  197 ? -2.147  -63.565 -87.816  1.00 156.82 ? 197  THR   C C    1 
ATOM   19155 O  O    . THR   C  3  197 ? -1.962  -63.444 -86.600  1.00 163.99 ? 197  THR   C O    1 
ATOM   19156 C  CB   . THR   C  3  197 ? -3.436  -65.721 -87.829  1.00 153.38 ? 197  THR   C CB   1 
ATOM   19157 O  OG1  . THR   C  3  197 ? -3.293  -65.780 -86.405  1.00 159.73 ? 197  THR   C OG1  1 
ATOM   19158 C  CG2  . THR   C  3  197 ? -3.492  -67.139 -88.378  1.00 146.78 ? 197  THR   C CG2  1 
ATOM   19159 H  H    . THR   C  3  197 ? -0.806  -65.764 -87.402  1.00 186.65 ? 197  THR   C H    1 
ATOM   19160 H  HA   . THR   C  3  197 ? -2.429  -64.853 -89.390  1.00 185.26 ? 197  THR   C HA   1 
ATOM   19161 H  HB   . THR   C  3  197 ? -4.263  -65.267 -88.054  1.00 184.09 ? 197  THR   C HB   1 
ATOM   19162 H  HG1  . THR   C  3  197 ? -2.872  -65.107 -86.130  1.00 191.72 ? 197  THR   C HG1  1 
ATOM   19163 H  HG21 . THR   C  3  197 ? -4.238  -67.618 -87.985  1.00 176.17 ? 197  THR   C HG21 1 
ATOM   19164 H  HG22 . THR   C  3  197 ? -3.603  -67.117 -89.342  1.00 176.17 ? 197  THR   C HG22 1 
ATOM   19165 H  HG23 . THR   C  3  197 ? -2.670  -67.609 -88.167  1.00 176.17 ? 197  THR   C HG23 1 
ATOM   19166 N  N    . HIS   C  3  198 ? -2.253  -62.531 -88.645  1.00 121.57 ? 198  HIS   C N    1 
ATOM   19167 C  CA   . HIS   C  3  198 ? -2.132  -61.152 -88.201  1.00 120.70 ? 198  HIS   C CA   1 
ATOM   19168 C  C    . HIS   C  3  198 ? -3.328  -60.359 -88.709  1.00 129.56 ? 198  HIS   C C    1 
ATOM   19169 O  O    . HIS   C  3  198 ? -3.986  -60.743 -89.680  1.00 140.14 ? 198  HIS   C O    1 
ATOM   19170 C  CB   . HIS   C  3  198 ? -0.821  -60.522 -88.696  1.00 112.52 ? 198  HIS   C CB   1 
ATOM   19171 C  CG   . HIS   C  3  198 ? -0.415  -59.293 -87.944  1.00 101.03 ? 198  HIS   C CG   1 
ATOM   19172 N  ND1  . HIS   C  3  198 ? -0.602  -59.153 -86.586  1.00 98.38  ? 198  HIS   C ND1  1 
ATOM   19173 C  CD2  . HIS   C  3  198 ? 0.182   -58.151 -88.360  1.00 97.86  ? 198  HIS   C CD2  1 
ATOM   19174 C  CE1  . HIS   C  3  198 ? -0.146  -57.975 -86.199  1.00 95.73  ? 198  HIS   C CE1  1 
ATOM   19175 N  NE2  . HIS   C  3  198 ? 0.336   -57.348 -87.256  1.00 96.73  ? 198  HIS   C NE2  1 
ATOM   19176 H  H    . HIS   C  3  198 ? -2.399  -62.608 -89.489  1.00 145.92 ? 198  HIS   C H    1 
ATOM   19177 H  HA   . HIS   C  3  198 ? -2.135  -61.112 -87.232  1.00 144.88 ? 198  HIS   C HA   1 
ATOM   19178 H  HB2  . HIS   C  3  198 ? -0.108  -61.174 -88.603  1.00 135.06 ? 198  HIS   C HB2  1 
ATOM   19179 H  HB3  . HIS   C  3  198 ? -0.926  -60.277 -89.628  1.00 135.06 ? 198  HIS   C HB3  1 
ATOM   19180 H  HD1  . HIS   C  3  198 ? -0.960  -59.742 -86.070  1.00 118.10 ? 198  HIS   C HD1  1 
ATOM   19181 H  HD2  . HIS   C  3  198 ? 0.439   -57.948 -89.230  1.00 117.47 ? 198  HIS   C HD2  1 
ATOM   19182 H  HE1  . HIS   C  3  198 ? -0.162  -57.645 -85.330  1.00 114.92 ? 198  HIS   C HE1  1 
ATOM   19183 N  N    . LYS   C  3  199 ? -3.609  -59.241 -88.036  1.00 127.95 ? 199  LYS   C N    1 
ATOM   19184 C  CA   . LYS   C  3  199 ? -4.762  -58.432 -88.414  1.00 131.39 ? 199  LYS   C CA   1 
ATOM   19185 C  C    . LYS   C  3  199 ? -4.600  -57.826 -89.804  1.00 133.25 ? 199  LYS   C C    1 
ATOM   19186 O  O    . LYS   C  3  199 ? -5.600  -57.545 -90.474  1.00 140.11 ? 199  LYS   C O    1 
ATOM   19187 C  CB   . LYS   C  3  199 ? -4.991  -57.322 -87.384  1.00 133.82 ? 199  LYS   C CB   1 
ATOM   19188 C  CG   . LYS   C  3  199 ? -5.446  -57.817 -86.015  1.00 137.91 ? 199  LYS   C CG   1 
ATOM   19189 C  CD   . LYS   C  3  199 ? -5.648  -56.662 -85.037  1.00 141.38 ? 199  LYS   C CD   1 
ATOM   19190 C  CE   . LYS   C  3  199 ? -6.133  -57.154 -83.678  1.00 143.51 ? 199  LYS   C CE   1 
ATOM   19191 N  NZ   . LYS   C  3  199 ? -6.303  -56.044 -82.695  1.00 145.11 ? 199  LYS   C NZ   1 
ATOM   19192 H  H    . LYS   C  3  199 ? -3.156  -58.937 -87.371  1.00 153.58 ? 199  LYS   C H    1 
ATOM   19193 H  HA   . LYS   C  3  199 ? -5.546  -59.003 -88.424  1.00 157.71 ? 199  LYS   C HA   1 
ATOM   19194 H  HB2  . LYS   C  3  199 ? -4.158  -56.840 -87.260  1.00 160.63 ? 199  LYS   C HB2  1 
ATOM   19195 H  HB3  . LYS   C  3  199 ? -5.674  -56.723 -87.722  1.00 160.63 ? 199  LYS   C HB3  1 
ATOM   19196 H  HG2  . LYS   C  3  199 ? -6.289  -58.287 -86.109  1.00 165.53 ? 199  LYS   C HG2  1 
ATOM   19197 H  HG3  . LYS   C  3  199 ? -4.773  -58.411 -85.649  1.00 165.53 ? 199  LYS   C HG3  1 
ATOM   19198 H  HD2  . LYS   C  3  199 ? -4.806  -56.199 -84.909  1.00 169.69 ? 199  LYS   C HD2  1 
ATOM   19199 H  HD3  . LYS   C  3  199 ? -6.312  -56.052 -85.394  1.00 169.69 ? 199  LYS   C HD3  1 
ATOM   19200 H  HE2  . LYS   C  3  199 ? -6.992  -57.593 -83.787  1.00 172.24 ? 199  LYS   C HE2  1 
ATOM   19201 H  HE3  . LYS   C  3  199 ? -5.485  -57.779 -83.317  1.00 172.24 ? 199  LYS   C HE3  1 
ATOM   19202 H  HZ1  . LYS   C  3  199 ? -6.906  -56.271 -82.081  1.00 174.17 ? 199  LYS   C HZ1  1 
ATOM   19203 H  HZ2  . LYS   C  3  199 ? -5.529  -55.875 -82.290  1.00 174.17 ? 199  LYS   C HZ2  1 
ATOM   19204 H  HZ3  . LYS   C  3  199 ? -6.579  -55.308 -83.112  1.00 174.17 ? 199  LYS   C HZ3  1 
ATOM   19205 N  N    . THR   C  3  200 ? -3.360  -57.630 -90.260  1.00 131.60 ? 200  THR   C N    1 
ATOM   19206 C  CA   . THR   C  3  200 ? -3.144  -56.878 -91.493  1.00 137.31 ? 200  THR   C CA   1 
ATOM   19207 C  C    . THR   C  3  200 ? -3.663  -57.618 -92.722  1.00 145.16 ? 200  THR   C C    1 
ATOM   19208 O  O    . THR   C  3  200 ? -4.098  -56.975 -93.685  1.00 158.33 ? 200  THR   C O    1 
ATOM   19209 C  CB   . THR   C  3  200 ? -1.657  -56.546 -91.657  1.00 131.80 ? 200  THR   C CB   1 
ATOM   19210 O  OG1  . THR   C  3  200 ? -1.473  -55.733 -92.824  1.00 136.38 ? 200  THR   C OG1  1 
ATOM   19211 C  CG2  . THR   C  3  200 ? -0.818  -57.812 -91.786  1.00 126.95 ? 200  THR   C CG2  1 
ATOM   19212 H  H    . THR   C  3  200 ? -2.643  -57.917 -89.882  1.00 157.95 ? 200  THR   C H    1 
ATOM   19213 H  HA   . THR   C  3  200 ? -3.633  -56.043 -91.427  1.00 164.81 ? 200  THR   C HA   1 
ATOM   19214 H  HB   . THR   C  3  200 ? -1.351  -56.066 -90.872  1.00 158.20 ? 200  THR   C HB   1 
ATOM   19215 H  HG1  . THR   C  3  200 ? -0.710  -55.381 -92.811  1.00 163.69 ? 200  THR   C HG1  1 
ATOM   19216 H  HG21 . THR   C  3  200 ? 0.121   -57.603 -91.659  1.00 152.38 ? 200  THR   C HG21 1 
ATOM   19217 H  HG22 . THR   C  3  200 ? -1.090  -58.460 -91.117  1.00 152.38 ? 200  THR   C HG22 1 
ATOM   19218 H  HG23 . THR   C  3  200 ? -0.937  -58.201 -92.667  1.00 152.38 ? 200  THR   C HG23 1 
ATOM   19219 N  N    . SER   C  3  201 ? -3.635  -58.951 -92.720  1.00 139.79 ? 201  SER   C N    1 
ATOM   19220 C  CA   . SER   C  3  201 ? -4.125  -59.738 -93.844  1.00 140.50 ? 201  SER   C CA   1 
ATOM   19221 C  C    . SER   C  3  201 ? -5.007  -60.873 -93.344  1.00 135.87 ? 201  SER   C C    1 
ATOM   19222 O  O    . SER   C  3  201 ? -4.700  -61.509 -92.332  1.00 127.00 ? 201  SER   C O    1 
ATOM   19223 C  CB   . SER   C  3  201 ? -2.970  -60.310 -94.676  1.00 141.99 ? 201  SER   C CB   1 
ATOM   19224 O  OG   . SER   C  3  201 ? -2.224  -59.274 -95.290  1.00 144.57 ? 201  SER   C OG   1 
ATOM   19225 H  H    . SER   C  3  201 ? -3.332  -59.425 -92.069  1.00 167.78 ? 201  SER   C H    1 
ATOM   19226 H  HA   . SER   C  3  201 ? -4.664  -59.169 -94.416  1.00 168.64 ? 201  SER   C HA   1 
ATOM   19227 H  HB2  . SER   C  3  201 ? -2.383  -60.817 -94.093  1.00 170.42 ? 201  SER   C HB2  1 
ATOM   19228 H  HB3  . SER   C  3  201 ? -3.333  -60.888 -95.365  1.00 170.42 ? 201  SER   C HB3  1 
ATOM   19229 H  HG   . SER   C  3  201 ? -2.735  -58.644 -95.511  1.00 173.52 ? 201  SER   C HG   1 
ATOM   19230 N  N    . THR   C  3  202 ? -6.102  -61.125 -94.066  1.00 143.36 ? 202  THR   C N    1 
ATOM   19231 C  CA   . THR   C  3  202 ? -7.014  -62.203 -93.705  1.00 146.30 ? 202  THR   C CA   1 
ATOM   19232 C  C    . THR   C  3  202 ? -6.467  -63.578 -94.061  1.00 148.09 ? 202  THR   C C    1 
ATOM   19233 O  O    . THR   C  3  202 ? -6.950  -64.581 -93.525  1.00 150.44 ? 202  THR   C O    1 
ATOM   19234 C  CB   . THR   C  3  202 ? -8.370  -62.016 -94.394  1.00 152.35 ? 202  THR   C CB   1 
ATOM   19235 O  OG1  . THR   C  3  202 ? -9.271  -63.046 -93.966  1.00 157.13 ? 202  THR   C OG1  1 
ATOM   19236 C  CG2  . THR   C  3  202 ? -8.221  -62.077 -95.913  1.00 154.33 ? 202  THR   C CG2  1 
ATOM   19237 H  H    . THR   C  3  202 ? -6.336  -60.686 -94.768  1.00 172.07 ? 202  THR   C H    1 
ATOM   19238 H  HA   . THR   C  3  202 ? -7.157  -62.167 -92.746  1.00 175.60 ? 202  THR   C HA   1 
ATOM   19239 H  HB   . THR   C  3  202 ? -8.731  -61.147 -94.160  1.00 182.85 ? 202  THR   C HB   1 
ATOM   19240 H  HG1  . THR   C  3  202 ? -10.004 -62.972 -94.369  1.00 188.59 ? 202  THR   C HG1  1 
ATOM   19241 H  HG21 . THR   C  3  202 ? -9.087  -61.972 -96.336  1.00 185.23 ? 202  THR   C HG21 1 
ATOM   19242 H  HG22 . THR   C  3  202 ? -7.634  -61.367 -96.218  1.00 185.23 ? 202  THR   C HG22 1 
ATOM   19243 H  HG23 . THR   C  3  202 ? -7.843  -62.931 -96.176  1.00 185.23 ? 202  THR   C HG23 1 
ATOM   19244 N  N    . SER   C  3  203 ? -5.484  -63.646 -94.958  1.00 149.31 ? 203  SER   C N    1 
ATOM   19245 C  CA   . SER   C  3  203 ? -4.903  -64.910 -95.379  1.00 152.45 ? 203  SER   C CA   1 
ATOM   19246 C  C    . SER   C  3  203 ? -3.641  -65.167 -94.571  1.00 145.25 ? 203  SER   C C    1 
ATOM   19247 O  O    . SER   C  3  203 ? -2.651  -64.441 -94.748  1.00 142.95 ? 203  SER   C O    1 
ATOM   19248 C  CB   . SER   C  3  203 ? -4.585  -64.877 -96.872  1.00 159.55 ? 203  SER   C CB   1 
ATOM   19249 O  OG   . SER   C  3  203 ? -3.881  -63.695 -97.212  1.00 162.23 ? 203  SER   C OG   1 
ATOM   19250 H  H    . SER   C  3  203 ? -5.133  -62.960 -95.341  1.00 179.21 ? 203  SER   C H    1 
ATOM   19251 H  HA   . SER   C  3  203 ? -5.530  -65.631 -95.211  1.00 182.97 ? 203  SER   C HA   1 
ATOM   19252 H  HB2  . SER   C  3  203 ? -4.038  -65.646 -97.096  1.00 191.50 ? 203  SER   C HB2  1 
ATOM   19253 H  HB3  . SER   C  3  203 ? -5.416  -64.905 -97.373  1.00 191.50 ? 203  SER   C HB3  1 
ATOM   19254 H  HG   . SER   C  3  203 ? -3.271  -63.553 -96.652  1.00 194.71 ? 203  SER   C HG   1 
ATOM   19255 N  N    . PRO   C  3  204 ? -3.616  -66.161 -93.684  1.00 143.10 ? 204  PRO   C N    1 
ATOM   19256 C  CA   . PRO   C  3  204 ? -2.431  -66.366 -92.841  1.00 138.53 ? 204  PRO   C CA   1 
ATOM   19257 C  C    . PRO   C  3  204 ? -1.154  -66.473 -93.662  1.00 138.22 ? 204  PRO   C C    1 
ATOM   19258 O  O    . PRO   C  3  204 ? -1.094  -67.194 -94.660  1.00 144.14 ? 204  PRO   C O    1 
ATOM   19259 C  CB   . PRO   C  3  204 ? -2.743  -67.678 -92.111  1.00 139.43 ? 204  PRO   C CB   1 
ATOM   19260 C  CG   . PRO   C  3  204 ? -4.228  -67.754 -92.089  1.00 145.73 ? 204  PRO   C CG   1 
ATOM   19261 C  CD   . PRO   C  3  204 ? -4.689  -67.123 -93.369  1.00 148.61 ? 204  PRO   C CD   1 
ATOM   19262 H  HA   . PRO   C  3  204 ? -2.343  -65.640 -92.203  1.00 166.28 ? 204  PRO   C HA   1 
ATOM   19263 H  HB2  . PRO   C  3  204 ? -2.363  -68.426 -92.598  1.00 167.35 ? 204  PRO   C HB2  1 
ATOM   19264 H  HB3  . PRO   C  3  204 ? -2.383  -67.650 -91.211  1.00 167.35 ? 204  PRO   C HB3  1 
ATOM   19265 H  HG2  . PRO   C  3  204 ? -4.508  -68.681 -92.043  1.00 174.91 ? 204  PRO   C HG2  1 
ATOM   19266 H  HG3  . PRO   C  3  204 ? -4.569  -67.266 -91.323  1.00 174.91 ? 204  PRO   C HG3  1 
ATOM   19267 H  HD2  . PRO   C  3  204 ? -4.773  -67.788 -94.070  1.00 178.37 ? 204  PRO   C HD2  1 
ATOM   19268 H  HD3  . PRO   C  3  204 ? -5.536  -66.666 -93.242  1.00 178.37 ? 204  PRO   C HD3  1 
ATOM   19269 N  N    . ILE   C  3  205 ? -0.123  -65.740 -93.238  1.00 130.99 ? 205  ILE   C N    1 
ATOM   19270 C  CA   . ILE   C  3  205 ? 1.188   -65.883 -93.858  1.00 127.57 ? 205  ILE   C CA   1 
ATOM   19271 C  C    . ILE   C  3  205 ? 1.794   -67.206 -93.415  1.00 126.93 ? 205  ILE   C C    1 
ATOM   19272 O  O    . ILE   C  3  205 ? 1.759   -67.560 -92.228  1.00 124.11 ? 205  ILE   C O    1 
ATOM   19273 C  CB   . ILE   C  3  205 ? 2.102   -64.699 -93.504  1.00 120.39 ? 205  ILE   C CB   1 
ATOM   19274 C  CG1  . ILE   C  3  205 ? 1.552   -63.410 -94.128  1.00 124.39 ? 205  ILE   C CG1  1 
ATOM   19275 C  CG2  . ILE   C  3  205 ? 3.535   -64.968 -93.980  1.00 116.26 ? 205  ILE   C CG2  1 
ATOM   19276 C  CD1  . ILE   C  3  205 ? 2.526   -62.237 -94.133  1.00 122.74 ? 205  ILE   C CD1  1 
ATOM   19277 H  H    . ILE   C  3  205 ? -0.159  -65.162 -92.602  1.00 157.22 ? 205  ILE   C H    1 
ATOM   19278 H  HA   . ILE   C  3  205 ? 1.085   -65.891 -94.822  1.00 153.12 ? 205  ILE   C HA   1 
ATOM   19279 H  HB   . ILE   C  3  205 ? 2.117   -64.592 -92.540  1.00 144.51 ? 205  ILE   C HB   1 
ATOM   19280 H  HG12 . ILE   C  3  205 ? 1.312   -63.593 -95.050  1.00 149.30 ? 205  ILE   C HG12 1 
ATOM   19281 H  HG13 . ILE   C  3  205 ? 0.768   -63.136 -93.629  1.00 149.30 ? 205  ILE   C HG13 1 
ATOM   19282 H  HG21 . ILE   C  3  205 ? 4.103   -64.232 -93.705  1.00 139.55 ? 205  ILE   C HG21 1 
ATOM   19283 H  HG22 . ILE   C  3  205 ? 3.850   -65.795 -93.582  1.00 139.55 ? 205  ILE   C HG22 1 
ATOM   19284 H  HG23 . ILE   C  3  205 ? 3.538   -65.045 -94.947  1.00 139.55 ? 205  ILE   C HG23 1 
ATOM   19285 H  HD11 . ILE   C  3  205 ? 2.066   -61.446 -94.454  1.00 147.32 ? 205  ILE   C HD11 1 
ATOM   19286 H  HD12 . ILE   C  3  205 ? 2.847   -62.089 -93.229  1.00 147.32 ? 205  ILE   C HD12 1 
ATOM   19287 H  HD13 . ILE   C  3  205 ? 3.271   -62.447 -94.718  1.00 147.32 ? 205  ILE   C HD13 1 
ATOM   19288 N  N    . VAL   C  3  206 ? 2.360   -67.939 -94.368  1.00 126.59 ? 206  VAL   C N    1 
ATOM   19289 C  CA   . VAL   C  3  206 ? 2.856   -69.288 -94.139  1.00 122.38 ? 206  VAL   C CA   1 
ATOM   19290 C  C    . VAL   C  3  206 ? 4.288   -69.372 -94.645  1.00 117.52 ? 206  VAL   C C    1 
ATOM   19291 O  O    . VAL   C  3  206 ? 4.629   -68.783 -95.676  1.00 120.26 ? 206  VAL   C O    1 
ATOM   19292 C  CB   . VAL   C  3  206 ? 1.968   -70.338 -94.841  1.00 128.78 ? 206  VAL   C CB   1 
ATOM   19293 C  CG1  . VAL   C  3  206 ? 2.275   -71.732 -94.324  1.00 128.14 ? 206  VAL   C CG1  1 
ATOM   19294 C  CG2  . VAL   C  3  206 ? 0.492   -69.998 -94.655  1.00 132.82 ? 206  VAL   C CG2  1 
ATOM   19295 H  H    . VAL   C  3  206 ? 2.469   -67.668 -95.176  1.00 151.95 ? 206  VAL   C H    1 
ATOM   19296 H  HA   . VAL   C  3  206 ? 2.861   -69.474 -93.187  1.00 146.89 ? 206  VAL   C HA   1 
ATOM   19297 H  HB   . VAL   C  3  206 ? 2.159   -70.326 -95.792  1.00 154.58 ? 206  VAL   C HB   1 
ATOM   19298 H  HG11 . VAL   C  3  206 ? 1.698   -72.370 -94.772  1.00 153.81 ? 206  VAL   C HG11 1 
ATOM   19299 H  HG12 . VAL   C  3  206 ? 3.205   -71.940 -94.509  1.00 153.81 ? 206  VAL   C HG12 1 
ATOM   19300 H  HG13 . VAL   C  3  206 ? 2.115   -71.757 -93.367  1.00 153.81 ? 206  VAL   C HG13 1 
ATOM   19301 H  HG21 . VAL   C  3  206 ? -0.046  -70.722 -95.014  1.00 159.42 ? 206  VAL   C HG21 1 
ATOM   19302 H  HG22 . VAL   C  3  206 ? 0.310   -69.888 -93.709  1.00 159.42 ? 206  VAL   C HG22 1 
ATOM   19303 H  HG23 . VAL   C  3  206 ? 0.296   -69.174 -95.128  1.00 159.42 ? 206  VAL   C HG23 1 
ATOM   19304 N  N    . LYS   C  3  207 ? 5.128   -70.097 -93.909  1.00 111.59 ? 207  LYS   C N    1 
ATOM   19305 C  CA   . LYS   C  3  207 ? 6.504   -70.362 -94.309  1.00 108.91 ? 207  LYS   C CA   1 
ATOM   19306 C  C    . LYS   C  3  207 ? 6.843   -71.781 -93.882  1.00 107.73 ? 207  LYS   C C    1 
ATOM   19307 O  O    . LYS   C  3  207 ? 6.660   -72.134 -92.713  1.00 105.33 ? 207  LYS   C O    1 
ATOM   19308 C  CB   . LYS   C  3  207 ? 7.479   -69.360 -93.678  1.00 103.95 ? 207  LYS   C CB   1 
ATOM   19309 C  CG   . LYS   C  3  207 ? 7.212   -67.903 -94.051  1.00 105.12 ? 207  LYS   C CG   1 
ATOM   19310 C  CD   . LYS   C  3  207 ? 7.531   -67.605 -95.517  1.00 109.61 ? 207  LYS   C CD   1 
ATOM   19311 C  CE   . LYS   C  3  207 ? 8.961   -67.117 -95.708  1.00 107.37 ? 207  LYS   C CE   1 
ATOM   19312 N  NZ   . LYS   C  3  207 ? 9.041   -66.029 -96.725  1.00 109.30 ? 207  LYS   C NZ   1 
ATOM   19313 H  H    . LYS   C  3  207 ? 4.917   -70.454 -93.156  1.00 133.95 ? 207  LYS   C H    1 
ATOM   19314 H  HA   . LYS   C  3  207 ? 6.596   -70.288 -95.272  1.00 130.72 ? 207  LYS   C HA   1 
ATOM   19315 H  HB2  . LYS   C  3  207 ? 7.415   -69.432 -92.713  1.00 124.77 ? 207  LYS   C HB2  1 
ATOM   19316 H  HB3  . LYS   C  3  207 ? 8.378   -69.578 -93.969  1.00 124.77 ? 207  LYS   C HB3  1 
ATOM   19317 H  HG2  . LYS   C  3  207 ? 6.275   -67.704 -93.900  1.00 126.18 ? 207  LYS   C HG2  1 
ATOM   19318 H  HG3  . LYS   C  3  207 ? 7.767   -67.329 -93.500  1.00 126.18 ? 207  LYS   C HG3  1 
ATOM   19319 H  HD2  . LYS   C  3  207 ? 7.416   -68.415 -96.038  1.00 131.56 ? 207  LYS   C HD2  1 
ATOM   19320 H  HD3  . LYS   C  3  207 ? 6.930   -66.915 -95.839  1.00 131.56 ? 207  LYS   C HD3  1 
ATOM   19321 H  HE2  . LYS   C  3  207 ? 9.298   -66.772 -94.867  1.00 128.89 ? 207  LYS   C HE2  1 
ATOM   19322 H  HE3  . LYS   C  3  207 ? 9.514   -67.855 -96.009  1.00 128.89 ? 207  LYS   C HE3  1 
ATOM   19323 H  HZ1  . LYS   C  3  207 ? 9.872   -65.714 -96.769  1.00 131.20 ? 207  LYS   C HZ1  1 
ATOM   19324 H  HZ2  . LYS   C  3  207 ? 8.808   -66.342 -97.525  1.00 131.20 ? 207  LYS   C HZ2  1 
ATOM   19325 H  HZ3  . LYS   C  3  207 ? 8.491   -65.365 -96.504  1.00 131.20 ? 207  LYS   C HZ3  1 
ATOM   19326 N  N    . SER   C  3  208 ? 7.323   -72.593 -94.822  1.00 110.92 ? 208  SER   C N    1 
ATOM   19327 C  CA   . SER   C  3  208 ? 7.537   -74.005 -94.548  1.00 115.18 ? 208  SER   C CA   1 
ATOM   19328 C  C    . SER   C  3  208 ? 8.733   -74.519 -95.335  1.00 116.47 ? 208  SER   C C    1 
ATOM   19329 O  O    . SER   C  3  208 ? 9.289   -73.831 -96.196  1.00 117.10 ? 208  SER   C O    1 
ATOM   19330 C  CB   . SER   C  3  208 ? 6.294   -74.833 -94.892  1.00 122.50 ? 208  SER   C CB   1 
ATOM   19331 O  OG   . SER   C  3  208 ? 6.042   -74.821 -96.286  1.00 131.44 ? 208  SER   C OG   1 
ATOM   19332 H  H    . SER   C  3  208 ? 7.530   -72.348 -95.620  1.00 133.15 ? 208  SER   C H    1 
ATOM   19333 H  HA   . SER   C  3  208 ? 7.738   -74.098 -93.604  1.00 138.25 ? 208  SER   C HA   1 
ATOM   19334 H  HB2  . SER   C  3  208 ? 6.436   -75.748 -94.605  1.00 147.03 ? 208  SER   C HB2  1 
ATOM   19335 H  HB3  . SER   C  3  208 ? 5.528   -74.456 -94.431  1.00 147.03 ? 208  SER   C HB3  1 
ATOM   19336 H  HG   . SER   C  3  208 ? 5.329   -75.233 -96.453  1.00 157.76 ? 208  SER   C HG   1 
ATOM   19337 N  N    . PHE   C  3  209 ? 9.114   -75.755 -95.022  1.00 116.34 ? 209  PHE   C N    1 
ATOM   19338 C  CA   . PHE   C  3  209 ? 10.193  -76.449 -95.706  1.00 119.93 ? 209  PHE   C CA   1 
ATOM   19339 C  C    . PHE   C  3  209 ? 9.913   -77.943 -95.629  1.00 124.59 ? 209  PHE   C C    1 
ATOM   19340 O  O    . PHE   C  3  209 ? 9.008   -78.389 -94.919  1.00 126.78 ? 209  PHE   C O    1 
ATOM   19341 C  CB   . PHE   C  3  209 ? 11.557  -76.112 -95.091  1.00 113.27 ? 209  PHE   C CB   1 
ATOM   19342 C  CG   . PHE   C  3  209 ? 11.734  -76.620 -93.687  1.00 105.58 ? 209  PHE   C CG   1 
ATOM   19343 C  CD1  . PHE   C  3  209 ? 11.352  -75.849 -92.601  1.00 98.31  ? 209  PHE   C CD1  1 
ATOM   19344 C  CD2  . PHE   C  3  209 ? 12.288  -77.868 -93.452  1.00 105.81 ? 209  PHE   C CD2  1 
ATOM   19345 C  CE1  . PHE   C  3  209 ? 11.516  -76.314 -91.309  1.00 93.92  ? 209  PHE   C CE1  1 
ATOM   19346 C  CE2  . PHE   C  3  209 ? 12.453  -78.339 -92.164  1.00 100.90 ? 209  PHE   C CE2  1 
ATOM   19347 C  CZ   . PHE   C  3  209 ? 12.068  -77.560 -91.091  1.00 95.08  ? 209  PHE   C CZ   1 
ATOM   19348 H  H    . PHE   C  3  209 ? 8.751   -76.224 -94.399  1.00 139.64 ? 209  PHE   C H    1 
ATOM   19349 H  HA   . PHE   C  3  209 ? 10.215  -76.182 -96.638  1.00 143.95 ? 209  PHE   C HA   1 
ATOM   19350 H  HB2  . PHE   C  3  209 ? 12.252  -76.509 -95.639  1.00 135.96 ? 209  PHE   C HB2  1 
ATOM   19351 H  HB3  . PHE   C  3  209 ? 11.660  -75.148 -95.072  1.00 135.96 ? 209  PHE   C HB3  1 
ATOM   19352 H  HD1  . PHE   C  3  209 ? 10.980  -75.008 -92.743  1.00 118.01 ? 209  PHE   C HD1  1 
ATOM   19353 H  HD2  . PHE   C  3  209 ? 12.552  -78.396 -94.171  1.00 127.00 ? 209  PHE   C HD2  1 
ATOM   19354 H  HE1  . PHE   C  3  209 ? 11.255  -75.788 -90.588  1.00 112.74 ? 209  PHE   C HE1  1 
ATOM   19355 H  HE2  . PHE   C  3  209 ? 12.823  -79.179 -92.019  1.00 121.11 ? 209  PHE   C HE2  1 
ATOM   19356 H  HZ   . PHE   C  3  209 ? 12.181  -77.875 -90.223  1.00 114.13 ? 209  PHE   C HZ   1 
ATOM   19357 N  N    . ASN   C  3  210 ? 10.699  -78.717 -96.371  1.00 128.05 ? 210  ASN   C N    1 
ATOM   19358 C  CA   . ASN   C  3  210 ? 10.600  -80.171 -96.372  1.00 132.52 ? 210  ASN   C CA   1 
ATOM   19359 C  C    . ASN   C  3  210 ? 11.956  -80.760 -96.011  1.00 133.83 ? 210  ASN   C C    1 
ATOM   19360 O  O    . ASN   C  3  210 ? 12.970  -80.422 -96.631  1.00 136.81 ? 210  ASN   C O    1 
ATOM   19361 C  CB   . ASN   C  3  210 ? 10.118  -80.690 -97.730  1.00 140.64 ? 210  ASN   C CB   1 
ATOM   19362 C  CG   . ASN   C  3  210 ? 8.617   -80.543 -97.908  1.00 146.18 ? 210  ASN   C CG   1 
ATOM   19363 O  OD1  . ASN   C  3  210 ? 7.849   -80.758 -96.970  1.00 145.53 ? 210  ASN   C OD1  1 
ATOM   19364 N  ND2  . ASN   C  3  210 ? 8.191   -80.171 -99.110  1.00 149.89 ? 210  ASN   C ND2  1 
ATOM   19365 H  H    . ASN   C  3  210 ? 11.312  -78.415 -96.893  1.00 153.69 ? 210  ASN   C H    1 
ATOM   19366 H  HA   . ASN   C  3  210 ? 9.960   -80.460 -95.702  1.00 159.06 ? 210  ASN   C HA   1 
ATOM   19367 H  HB2  . ASN   C  3  210 ? 10.555  -80.186 -98.435  1.00 168.80 ? 210  ASN   C HB2  1 
ATOM   19368 H  HB3  . ASN   C  3  210 ? 10.340  -81.631 -97.808  1.00 168.80 ? 210  ASN   C HB3  1 
ATOM   19369 H  HD21 . ASN   C  3  210 ? 7.350   -80.075 -99.258  1.00 179.90 ? 210  ASN   C HD21 1 
ATOM   19370 H  HD22 . ASN   C  3  210 ? 8.758   -80.026 -99.740  1.00 179.90 ? 210  ASN   C HD22 1 
ATOM   19371 N  N    . ARG   C  3  211 ? 11.966  -81.638 -95.005  1.00 136.59 ? 211  ARG   C N    1 
ATOM   19372 C  CA   . ARG   C  3  211 ? 13.222  -82.154 -94.469  1.00 138.12 ? 211  ARG   C CA   1 
ATOM   19373 C  C    . ARG   C  3  211 ? 14.011  -82.912 -95.530  1.00 151.02 ? 211  ARG   C C    1 
ATOM   19374 O  O    . ARG   C  3  211 ? 15.215  -82.689 -95.703  1.00 150.47 ? 211  ARG   C O    1 
ATOM   19375 C  CB   . ARG   C  3  211 ? 12.932  -83.051 -93.264  1.00 134.18 ? 211  ARG   C CB   1 
ATOM   19376 C  CG   . ARG   C  3  211 ? 14.163  -83.659 -92.616  1.00 134.89 ? 211  ARG   C CG   1 
ATOM   19377 C  CD   . ARG   C  3  211 ? 13.787  -84.481 -91.393  1.00 134.50 ? 211  ARG   C CD   1 
ATOM   19378 N  NE   . ARG   C  3  211 ? 12.967  -85.639 -91.742  1.00 140.18 ? 211  ARG   C NE   1 
ATOM   19379 C  CZ   . ARG   C  3  211 ? 13.454  -86.800 -92.170  1.00 146.34 ? 211  ARG   C CZ   1 
ATOM   19380 N  NH1  . ARG   C  3  211 ? 14.763  -86.966 -92.311  1.00 148.78 ? 211  ARG   C NH1  1 
ATOM   19381 N  NH2  . ARG   C  3  211 ? 12.630  -87.798 -92.463  1.00 151.60 ? 211  ARG   C NH2  1 
ATOM   19382 H  H    . ARG   C  3  211 ? 11.263  -81.948 -94.619  1.00 163.95 ? 211  ARG   C H    1 
ATOM   19383 H  HA   . ARG   C  3  211 ? 13.768  -81.408 -94.174  1.00 165.78 ? 211  ARG   C HA   1 
ATOM   19384 H  HB2  . ARG   C  3  211 ? 12.477  -82.524 -92.589  1.00 161.05 ? 211  ARG   C HB2  1 
ATOM   19385 H  HB3  . ARG   C  3  211 ? 12.364  -83.782 -93.554  1.00 161.05 ? 211  ARG   C HB3  1 
ATOM   19386 H  HG2  . ARG   C  3  211 ? 14.609  -84.241 -93.252  1.00 161.90 ? 211  ARG   C HG2  1 
ATOM   19387 H  HG3  . ARG   C  3  211 ? 14.765  -82.951 -92.337  1.00 161.90 ? 211  ARG   C HG3  1 
ATOM   19388 H  HD2  . ARG   C  3  211 ? 14.595  -84.801 -90.963  1.00 161.44 ? 211  ARG   C HD2  1 
ATOM   19389 H  HD3  . ARG   C  3  211 ? 13.282  -83.926 -90.779  1.00 161.44 ? 211  ARG   C HD3  1 
ATOM   19390 H  HE   . ARG   C  3  211 ? 12.114  -85.565 -91.665  1.00 168.25 ? 211  ARG   C HE   1 
ATOM   19391 H  HH11 . ARG   C  3  211 ? 15.300  -86.321 -92.125  1.00 178.58 ? 211  ARG   C HH11 1 
ATOM   19392 H  HH12 . ARG   C  3  211 ? 15.073  -87.718 -92.588  1.00 178.58 ? 211  ARG   C HH12 1 
ATOM   19393 H  HH21 . ARG   C  3  211 ? 11.781  -87.694 -92.375  1.00 181.96 ? 211  ARG   C HH21 1 
ATOM   19394 H  HH22 . ARG   C  3  211 ? 12.945  -88.549 -92.740  1.00 181.96 ? 211  ARG   C HH22 1 
ATOM   19395 N  N    . ASN   C  3  212 ? 13.350  -83.822 -96.247  1.00 163.44 ? 212  ASN   C N    1 
ATOM   19396 C  CA   . ASN   C  3  212 ? 14.050  -84.614 -97.252  1.00 174.55 ? 212  ASN   C CA   1 
ATOM   19397 C  C    . ASN   C  3  212 ? 14.617  -83.728 -98.355  1.00 179.59 ? 212  ASN   C C    1 
ATOM   19398 O  O    . ASN   C  3  212 ? 15.737  -83.953 -98.829  1.00 187.15 ? 212  ASN   C O    1 
ATOM   19399 C  CB   . ASN   C  3  212 ? 13.104  -85.661 -97.842  1.00 180.39 ? 212  ASN   C CB   1 
ATOM   19400 C  CG   . ASN   C  3  212 ? 13.827  -86.694 -98.685  1.00 186.47 ? 212  ASN   C CG   1 
ATOM   19401 O  OD1  . ASN   C  3  212 ? 14.977  -87.038 -98.412  1.00 184.99 ? 212  ASN   C OD1  1 
ATOM   19402 N  ND2  . ASN   C  3  212 ? 13.155  -87.193 -99.717  1.00 191.97 ? 212  ASN   C ND2  1 
ATOM   19403 H  H    . ASN   C  3  212 ? 12.511  -83.996 -96.172  1.00 196.17 ? 212  ASN   C H    1 
ATOM   19404 H  HA   . ASN   C  3  212 ? 14.789  -85.078 -96.828  1.00 209.49 ? 212  ASN   C HA   1 
ATOM   19405 H  HB2  . ASN   C  3  212 ? 12.655  -86.125 -97.119  1.00 216.50 ? 212  ASN   C HB2  1 
ATOM   19406 H  HB3  . ASN   C  3  212 ? 12.452  -85.216 -98.406  1.00 216.50 ? 212  ASN   C HB3  1 
ATOM   19407 H  HD21 . ASN   C  3  212 ? 13.522  -87.782 -100.225 1.00 230.40 ? 212  ASN   C HD21 1 
ATOM   19408 H  HD22 . ASN   C  3  212 ? 12.352  -86.927 -99.877  1.00 230.40 ? 212  ASN   C HD22 1 
ATOM   19409 N  N    . GLU   C  3  213 ? 13.868  -82.707 -98.763  1.00 175.53 ? 213  GLU   C N    1 
ATOM   19410 C  CA   . GLU   C  3  213 ? 14.223  -81.911 -99.925  1.00 184.54 ? 213  GLU   C CA   1 
ATOM   19411 C  C    . GLU   C  3  213 ? 15.278  -80.860 -99.581  1.00 182.53 ? 213  GLU   C C    1 
ATOM   19412 O  O    . GLU   C  3  213 ? 15.599  -80.610 -98.415  1.00 175.45 ? 213  GLU   C O    1 
ATOM   19413 C  CB   . GLU   C  3  213 ? 12.981  -81.231 -100.500 1.00 184.05 ? 213  GLU   C CB   1 
ATOM   19414 C  CG   . GLU   C  3  213 ? 11.816  -82.177 -100.733 1.00 189.88 ? 213  GLU   C CG   1 
ATOM   19415 C  CD   . GLU   C  3  213 ? 10.779  -81.606 -101.679 1.00 196.21 ? 213  GLU   C CD   1 
ATOM   19416 O  OE1  . GLU   C  3  213 ? 10.987  -80.485 -102.188 1.00 195.41 ? 213  GLU   C OE1  1 
ATOM   19417 O  OE2  . GLU   C  3  213 ? 9.755   -82.281 -101.916 1.00 201.03 ? 213  GLU   C OE2  1 
ATOM   19418 H  H    . GLU   C  3  213 ? 13.141  -82.456 -98.377  1.00 210.67 ? 213  GLU   C H    1 
ATOM   19419 H  HA   . GLU   C  3  213 ? 14.599  -82.500 -100.597 1.00 221.48 ? 213  GLU   C HA   1 
ATOM   19420 H  HB2  . GLU   C  3  213 ? 12.686  -80.546 -99.880  1.00 220.90 ? 213  GLU   C HB2  1 
ATOM   19421 H  HB3  . GLU   C  3  213 ? 13.212  -80.830 -101.352 1.00 220.90 ? 213  GLU   C HB3  1 
ATOM   19422 H  HG2  . GLU   C  3  213 ? 12.151  -83.002 -101.118 1.00 227.89 ? 213  GLU   C HG2  1 
ATOM   19423 H  HG3  . GLU   C  3  213 ? 11.382  -82.359 -99.885  1.00 227.89 ? 213  GLU   C HG3  1 
ATOM   19424 N  N    . CYS   C  3  214 ? 15.815  -80.238 -100.628 1.00 190.10 ? 214  CYS   C N    1 
ATOM   19425 C  CA   . CYS   C  3  214 ? 16.794  -79.163 -100.488 1.00 192.09 ? 214  CYS   C CA   1 
ATOM   19426 C  C    . CYS   C  3  214 ? 16.868  -78.340 -101.769 1.00 203.81 ? 214  CYS   C C    1 
ATOM   19427 O  O    . CYS   C  3  214 ? 15.918  -77.645 -102.127 1.00 206.61 ? 214  CYS   C O    1 
ATOM   19428 C  CB   . CYS   C  3  214 ? 18.174  -79.727 -100.148 1.00 191.38 ? 214  CYS   C CB   1 
ATOM   19429 S  SG   . CYS   C  3  214 ? 19.474  -78.496 -99.806  1.00 195.87 ? 214  CYS   C SG   1 
ATOM   19430 H  H    . CYS   C  3  214 ? 15.626  -80.424 -101.446 1.00 228.15 ? 214  CYS   C H    1 
ATOM   19431 H  HA   . CYS   C  3  214 ? 16.526  -78.580 -99.761  1.00 230.55 ? 214  CYS   C HA   1 
ATOM   19432 H  HB2  . CYS   C  3  214 ? 18.088  -80.282 -99.357  1.00 229.69 ? 214  CYS   C HB2  1 
ATOM   19433 H  HB3  . CYS   C  3  214 ? 18.476  -80.263 -100.898 1.00 229.69 ? 214  CYS   C HB3  1 
ATOM   19434 H  HG   . CYS   C  3  214 ? 19.144  -77.832 -98.862  1.00 235.09 ? 214  CYS   C HG   1 
ATOM   19435 N  N    . GLN   D  4  1   ? 18.547  -36.034 -55.072  1.00 102.81 ? 1    GLN   D N    1 
ATOM   19436 C  CA   . GLN   D  4  1   ? 19.686  -36.976 -55.271  1.00 98.88  ? 1    GLN   D CA   1 
ATOM   19437 C  C    . GLN   D  4  1   ? 19.525  -38.189 -54.361  1.00 89.49  ? 1    GLN   D C    1 
ATOM   19438 O  O    . GLN   D  4  1   ? 20.489  -38.688 -53.782  1.00 89.75  ? 1    GLN   D O    1 
ATOM   19439 C  CB   . GLN   D  4  1   ? 21.013  -36.261 -55.016  1.00 106.43 ? 1    GLN   D CB   1 
ATOM   19440 C  CG   . GLN   D  4  1   ? 21.250  -35.111 -55.986  1.00 115.63 ? 1    GLN   D CG   1 
ATOM   19441 C  CD   . GLN   D  4  1   ? 22.457  -34.267 -55.635  1.00 126.69 ? 1    GLN   D CD   1 
ATOM   19442 O  OE1  . GLN   D  4  1   ? 22.876  -34.206 -54.479  1.00 130.29 ? 1    GLN   D OE1  1 
ATOM   19443 N  NE2  . GLN   D  4  1   ? 23.023  -33.605 -56.638  1.00 132.12 ? 1    GLN   D NE2  1 
ATOM   19444 H  H1   . GLN   D  4  1   ? 18.102  -35.940 -55.837  1.00 123.40 ? 1    GLN   D H1   1 
ATOM   19445 H  H2   . GLN   D  4  1   ? 17.999  -36.358 -54.449  1.00 123.40 ? 1    GLN   D H2   1 
ATOM   19446 H  H3   . GLN   D  4  1   ? 18.858  -35.243 -54.810  1.00 123.40 ? 1    GLN   D H3   1 
ATOM   19447 H  HA   . GLN   D  4  1   ? 19.706  -37.294 -56.188  1.00 118.69 ? 1    GLN   D HA   1 
ATOM   19448 H  HB2  . GLN   D  4  1   ? 21.010  -35.901 -54.115  1.00 127.75 ? 1    GLN   D HB2  1 
ATOM   19449 H  HB3  . GLN   D  4  1   ? 21.739  -36.896 -55.117  1.00 127.75 ? 1    GLN   D HB3  1 
ATOM   19450 H  HG2  . GLN   D  4  1   ? 21.389  -35.474 -56.874  1.00 138.80 ? 1    GLN   D HG2  1 
ATOM   19451 H  HG3  . GLN   D  4  1   ? 20.472  -34.532 -55.982  1.00 138.80 ? 1    GLN   D HG3  1 
ATOM   19452 H  HE21 . GLN   D  4  1   ? 22.700  -33.670 -57.433  1.00 158.58 ? 1    GLN   D HE21 1 
ATOM   19453 H  HE22 . GLN   D  4  1   ? 23.712  -33.111 -56.493  1.00 158.58 ? 1    GLN   D HE22 1 
ATOM   19454 N  N    . VAL   D  4  2   ? 18.283  -38.649 -54.251  1.00 81.97  ? 2    VAL   D N    1 
ATOM   19455 C  CA   . VAL   D  4  2   ? 17.958  -39.837 -53.471  1.00 75.27  ? 2    VAL   D CA   1 
ATOM   19456 C  C    . VAL   D  4  2   ? 18.203  -41.067 -54.333  1.00 73.72  ? 2    VAL   D C    1 
ATOM   19457 O  O    . VAL   D  4  2   ? 17.779  -41.121 -55.493  1.00 73.17  ? 2    VAL   D O    1 
ATOM   19458 C  CB   . VAL   D  4  2   ? 16.501  -39.780 -52.985  1.00 73.15  ? 2    VAL   D CB   1 
ATOM   19459 C  CG1  . VAL   D  4  2   ? 16.134  -41.050 -52.230  1.00 71.75  ? 2    VAL   D CG1  1 
ATOM   19460 C  CG2  . VAL   D  4  2   ? 16.276  -38.547 -52.118  1.00 74.05  ? 2    VAL   D CG2  1 
ATOM   19461 H  H    . VAL   D  4  2   ? 17.599  -38.285 -54.624  1.00 98.40  ? 2    VAL   D H    1 
ATOM   19462 H  HA   . VAL   D  4  2   ? 18.537  -39.884 -52.694  1.00 90.36  ? 2    VAL   D HA   1 
ATOM   19463 H  HB   . VAL   D  4  2   ? 15.916  -39.716 -53.756  1.00 87.82  ? 2    VAL   D HB   1 
ATOM   19464 H  HG11 . VAL   D  4  2   ? 15.229  -40.966 -51.892  1.00 86.14  ? 2    VAL   D HG11 1 
ATOM   19465 H  HG12 . VAL   D  4  2   ? 16.192  -41.805 -52.836  1.00 86.14  ? 2    VAL   D HG12 1 
ATOM   19466 H  HG13 . VAL   D  4  2   ? 16.754  -41.169 -51.494  1.00 86.14  ? 2    VAL   D HG13 1 
ATOM   19467 H  HG21 . VAL   D  4  2   ? 15.356  -38.541 -51.809  1.00 88.89  ? 2    VAL   D HG21 1 
ATOM   19468 H  HG22 . VAL   D  4  2   ? 16.879  -38.580 -51.359  1.00 88.89  ? 2    VAL   D HG22 1 
ATOM   19469 H  HG23 . VAL   D  4  2   ? 16.453  -37.753 -52.646  1.00 88.89  ? 2    VAL   D HG23 1 
ATOM   19470 N  N    . GLN   D  4  3   ? 18.886  -42.061 -53.769  1.00 75.83  ? 3    GLN   D N    1 
ATOM   19471 C  CA   . GLN   D  4  3   ? 19.196  -43.285 -54.494  1.00 75.34  ? 3    GLN   D CA   1 
ATOM   19472 C  C    . GLN   D  4  3   ? 19.062  -44.481 -53.566  1.00 70.99  ? 3    GLN   D C    1 
ATOM   19473 O  O    . GLN   D  4  3   ? 19.586  -44.465 -52.448  1.00 72.10  ? 3    GLN   D O    1 
ATOM   19474 C  CB   . GLN   D  4  3   ? 20.613  -43.244 -55.076  1.00 83.80  ? 3    GLN   D CB   1 
ATOM   19475 C  CG   . GLN   D  4  3   ? 20.872  -42.098 -56.032  1.00 90.72  ? 3    GLN   D CG   1 
ATOM   19476 C  CD   . GLN   D  4  3   ? 22.300  -42.090 -56.541  1.00 100.01 ? 3    GLN   D CD   1 
ATOM   19477 O  OE1  . GLN   D  4  3   ? 23.006  -43.095 -56.453  1.00 103.48 ? 3    GLN   D OE1  1 
ATOM   19478 N  NE2  . GLN   D  4  3   ? 22.735  -40.953 -57.069  1.00 104.24 ? 3    GLN   D NE2  1 
ATOM   19479 H  H    . GLN   D  4  3   ? 19.181  -42.048 -52.961  1.00 91.04  ? 3    GLN   D H    1 
ATOM   19480 H  HA   . GLN   D  4  3   ? 18.561  -43.388 -55.220  1.00 90.45  ? 3    GLN   D HA   1 
ATOM   19481 H  HB2  . GLN   D  4  3   ? 21.245  -43.163 -54.344  1.00 100.60 ? 3    GLN   D HB2  1 
ATOM   19482 H  HB3  . GLN   D  4  3   ? 20.772  -44.070 -55.560  1.00 100.60 ? 3    GLN   D HB3  1 
ATOM   19483 H  HG2  . GLN   D  4  3   ? 20.279  -42.179 -56.796  1.00 108.89 ? 3    GLN   D HG2  1 
ATOM   19484 H  HG3  . GLN   D  4  3   ? 20.709  -41.258 -55.575  1.00 108.89 ? 3    GLN   D HG3  1 
ATOM   19485 H  HE21 . GLN   D  4  3   ? 22.214  -40.270 -57.108  1.00 125.13 ? 3    GLN   D HE21 1 
ATOM   19486 H  HE22 . GLN   D  4  3   ? 23.539  -40.899 -57.371  1.00 125.13 ? 3    GLN   D HE22 1 
ATOM   19487 N  N    . LEU   D  4  4   ? 18.368  -45.514 -54.038  1.00 62.90  ? 4    LEU   D N    1 
ATOM   19488 C  CA   . LEU   D  4  4   ? 18.255  -46.789 -53.337  1.00 66.24  ? 4    LEU   D CA   1 
ATOM   19489 C  C    . LEU   D  4  4   ? 18.910  -47.852 -54.210  1.00 68.31  ? 4    LEU   D C    1 
ATOM   19490 O  O    . LEU   D  4  4   ? 18.392  -48.186 -55.281  1.00 67.96  ? 4    LEU   D O    1 
ATOM   19491 C  CB   . LEU   D  4  4   ? 16.795  -47.136 -53.045  1.00 68.11  ? 4    LEU   D CB   1 
ATOM   19492 C  CG   . LEU   D  4  4   ? 15.965  -46.070 -52.322  1.00 70.38  ? 4    LEU   D CG   1 
ATOM   19493 C  CD1  . LEU   D  4  4   ? 14.601  -46.627 -51.938  1.00 70.54  ? 4    LEU   D CD1  1 
ATOM   19494 C  CD2  . LEU   D  4  4   ? 16.686  -45.534 -51.092  1.00 73.03  ? 4    LEU   D CD2  1 
ATOM   19495 H  H    . LEU   D  4  4   ? 17.941  -45.498 -54.784  1.00 75.51  ? 4    LEU   D H    1 
ATOM   19496 H  HA   . LEU   D  4  4   ? 18.724  -46.741 -52.490  1.00 79.53  ? 4    LEU   D HA   1 
ATOM   19497 H  HB2  . LEU   D  4  4   ? 16.354  -47.314 -53.891  1.00 81.77  ? 4    LEU   D HB2  1 
ATOM   19498 H  HB3  . LEU   D  4  4   ? 16.781  -47.931 -52.490  1.00 81.77  ? 4    LEU   D HB3  1 
ATOM   19499 H  HG   . LEU   D  4  4   ? 15.835  -45.324 -52.929  1.00 84.49  ? 4    LEU   D HG   1 
ATOM   19500 H  HD11 . LEU   D  4  4   ? 14.088  -45.931 -51.497  1.00 84.68  ? 4    LEU   D HD11 1 
ATOM   19501 H  HD12 . LEU   D  4  4   ? 14.141  -46.918 -52.741  1.00 84.68  ? 4    LEU   D HD12 1 
ATOM   19502 H  HD13 . LEU   D  4  4   ? 14.724  -47.378 -51.337  1.00 84.68  ? 4    LEU   D HD13 1 
ATOM   19503 H  HD21 . LEU   D  4  4   ? 16.129  -44.865 -50.666  1.00 87.67  ? 4    LEU   D HD21 1 
ATOM   19504 H  HD22 . LEU   D  4  4   ? 16.851  -46.267 -50.479  1.00 87.67  ? 4    LEU   D HD22 1 
ATOM   19505 H  HD23 . LEU   D  4  4   ? 17.528  -45.137 -51.367  1.00 87.67  ? 4    LEU   D HD23 1 
ATOM   19506 N  N    . GLN   D  4  5   ? 20.046  -48.374 -53.757  1.00 72.44  ? 5    GLN   D N    1 
ATOM   19507 C  CA   . GLN   D  4  5   ? 20.800  -49.385 -54.488  1.00 79.54  ? 5    GLN   D CA   1 
ATOM   19508 C  C    . GLN   D  4  5   ? 20.515  -50.752 -53.879  1.00 80.74  ? 5    GLN   D C    1 
ATOM   19509 O  O    . GLN   D  4  5   ? 20.850  -50.997 -52.715  1.00 84.68  ? 5    GLN   D O    1 
ATOM   19510 C  CB   . GLN   D  4  5   ? 22.298  -49.084 -54.449  1.00 91.46  ? 5    GLN   D CB   1 
ATOM   19511 C  CG   . GLN   D  4  5   ? 22.700  -47.809 -55.174  1.00 104.13 ? 5    GLN   D CG   1 
ATOM   19512 C  CD   . GLN   D  4  5   ? 24.189  -47.532 -55.082  1.00 117.91 ? 5    GLN   D CD   1 
ATOM   19513 O  OE1  . GLN   D  4  5   ? 24.873  -48.044 -54.195  1.00 123.54 ? 5    GLN   D OE1  1 
ATOM   19514 N  NE2  . GLN   D  4  5   ? 24.699  -46.722 -56.002  1.00 122.73 ? 5    GLN   D NE2  1 
ATOM   19515 H  H    . GLN   D  4  5   ? 20.409  -48.153 -53.009  1.00 86.96  ? 5    GLN   D H    1 
ATOM   19516 H  HA   . GLN   D  4  5   ? 20.514  -49.393 -55.415  1.00 95.48  ? 5    GLN   D HA   1 
ATOM   19517 H  HB2  . GLN   D  4  5   ? 22.571  -48.994 -53.522  1.00 109.79 ? 5    GLN   D HB2  1 
ATOM   19518 H  HB3  . GLN   D  4  5   ? 22.773  -49.821 -54.864  1.00 109.79 ? 5    GLN   D HB3  1 
ATOM   19519 H  HG2  . GLN   D  4  5   ? 22.467  -47.891 -56.112  1.00 124.99 ? 5    GLN   D HG2  1 
ATOM   19520 H  HG3  . GLN   D  4  5   ? 22.230  -47.059 -54.779  1.00 124.99 ? 5    GLN   D HG3  1 
ATOM   19521 H  HE21 . GLN   D  4  5   ? 24.190  -46.385 -56.608  1.00 147.32 ? 5    GLN   D HE21 1 
ATOM   19522 H  HE22 . GLN   D  4  5   ? 25.538  -46.534 -55.993  1.00 147.32 ? 5    GLN   D HE22 1 
ATOM   19523 N  N    . GLN   D  4  6   ? 19.903  -51.634 -54.661  1.00 76.50  ? 6    GLN   D N    1 
ATOM   19524 C  CA   . GLN   D  4  6   ? 19.551  -52.969 -54.203  1.00 71.55  ? 6    GLN   D CA   1 
ATOM   19525 C  C    . GLN   D  4  6   ? 20.608  -53.981 -54.631  1.00 69.08  ? 6    GLN   D C    1 
ATOM   19526 O  O    . GLN   D  4  6   ? 21.329  -53.790 -55.613  1.00 65.96  ? 6    GLN   D O    1 
ATOM   19527 C  CB   . GLN   D  4  6   ? 18.182  -53.386 -54.743  1.00 67.80  ? 6    GLN   D CB   1 
ATOM   19528 C  CG   . GLN   D  4  6   ? 17.018  -52.655 -54.103  1.00 62.04  ? 6    GLN   D CG   1 
ATOM   19529 C  CD   . GLN   D  4  6   ? 15.678  -53.206 -54.544  1.00 58.30  ? 6    GLN   D CD   1 
ATOM   19530 O  OE1  . GLN   D  4  6   ? 14.952  -52.570 -55.308  1.00 53.79  ? 6    GLN   D OE1  1 
ATOM   19531 N  NE2  . GLN   D  4  6   ? 15.343  -54.398 -54.064  1.00 59.15  ? 6    GLN   D NE2  1 
ATOM   19532 H  H    . GLN   D  4  6   ? 19.677  -51.477 -55.476  1.00 91.84  ? 6    GLN   D H    1 
ATOM   19533 H  HA   . GLN   D  4  6   ? 19.508  -52.969 -53.234  1.00 85.89  ? 6    GLN   D HA   1 
ATOM   19534 H  HB2  . GLN   D  4  6   ? 18.155  -53.206 -55.696  1.00 81.40  ? 6    GLN   D HB2  1 
ATOM   19535 H  HB3  . GLN   D  4  6   ? 18.059  -54.335 -54.581  1.00 81.40  ? 6    GLN   D HB3  1 
ATOM   19536 H  HG2  . GLN   D  4  6   ? 17.078  -52.744 -53.139  1.00 74.49  ? 6    GLN   D HG2  1 
ATOM   19537 H  HG3  . GLN   D  4  6   ? 17.055  -51.718 -54.352  1.00 74.49  ? 6    GLN   D HG3  1 
ATOM   19538 H  HE21 . GLN   D  4  6   ? 15.877  -54.813 -53.533  1.00 71.02  ? 6    GLN   D HE21 1 
ATOM   19539 H  HE22 . GLN   D  4  6   ? 14.593  -54.755 -54.285  1.00 71.02  ? 6    GLN   D HE22 1 
ATOM   19540 N  N    . SER   D  4  7   ? 20.685  -55.073 -53.874  1.00 69.39  ? 7    SER   D N    1 
ATOM   19541 C  CA   . SER   D  4  7   ? 21.673  -56.104 -54.143  1.00 71.22  ? 7    SER   D CA   1 
ATOM   19542 C  C    . SER   D  4  7   ? 21.333  -56.834 -55.442  1.00 70.53  ? 7    SER   D C    1 
ATOM   19543 O  O    . SER   D  4  7   ? 20.303  -56.595 -56.078  1.00 65.66  ? 7    SER   D O    1 
ATOM   19544 C  CB   . SER   D  4  7   ? 21.752  -57.083 -52.974  1.00 71.96  ? 7    SER   D CB   1 
ATOM   19545 O  OG   . SER   D  4  7   ? 20.598  -57.902 -52.912  1.00 70.81  ? 7    SER   D OG   1 
ATOM   19546 H  H    . SER   D  4  7   ? 20.176  -55.237 -53.201  1.00 83.30  ? 7    SER   D H    1 
ATOM   19547 H  HA   . SER   D  4  7   ? 22.542  -55.685 -54.246  1.00 85.50  ? 7    SER   D HA   1 
ATOM   19548 H  HB2  . SER   D  4  7   ? 22.533  -57.647 -53.089  1.00 86.39  ? 7    SER   D HB2  1 
ATOM   19549 H  HB3  . SER   D  4  7   ? 21.825  -56.580 -52.148  1.00 86.39  ? 7    SER   D HB3  1 
ATOM   19550 H  HG   . SER   D  4  7   ? 20.697  -58.493 -52.324  1.00 85.00  ? 7    SER   D HG   1 
ATOM   19551 N  N    . GLY   D  4  8   ? 22.220  -57.747 -55.834  1.00 77.90  ? 8    GLY   D N    1 
ATOM   19552 C  CA   . GLY   D  4  8   ? 22.087  -58.449 -57.090  1.00 78.15  ? 8    GLY   D CA   1 
ATOM   19553 C  C    . GLY   D  4  8   ? 21.115  -59.611 -57.025  1.00 75.49  ? 8    GLY   D C    1 
ATOM   19554 O  O    . GLY   D  4  8   ? 20.563  -59.957 -55.981  1.00 72.69  ? 8    GLY   D O    1 
ATOM   19555 H  H    . GLY   D  4  8   ? 22.913  -57.975 -55.379  1.00 93.52  ? 8    GLY   D H    1 
ATOM   19556 H  HA2  . GLY   D  4  8   ? 21.773  -57.830 -57.768  1.00 93.82  ? 8    GLY   D HA2  1 
ATOM   19557 H  HA3  . GLY   D  4  8   ? 22.954  -58.794 -57.354  1.00 93.82  ? 8    GLY   D HA3  1 
ATOM   19558 N  N    . ALA   D  4  9   ? 20.916  -60.228 -58.188  1.00 77.30  ? 9    ALA   D N    1 
ATOM   19559 C  CA   . ALA   D  4  9   ? 19.971  -61.329 -58.306  1.00 79.26  ? 9    ALA   D CA   1 
ATOM   19560 C  C    . ALA   D  4  9   ? 20.330  -62.458 -57.349  1.00 84.38  ? 9    ALA   D C    1 
ATOM   19561 O  O    . ALA   D  4  9   ? 21.504  -62.781 -57.151  1.00 89.93  ? 9    ALA   D O    1 
ATOM   19562 C  CB   . ALA   D  4  9   ? 19.949  -61.850 -59.744  1.00 80.80  ? 9    ALA   D CB   1 
ATOM   19563 H  H    . ALA   D  4  9   ? 21.315  -60.026 -58.923  1.00 92.79  ? 9    ALA   D H    1 
ATOM   19564 H  HA   . ALA   D  4  9   ? 19.083  -61.012 -58.079  1.00 95.15  ? 9    ALA   D HA   1 
ATOM   19565 H  HB1  . ALA   D  4  9   ? 19.321  -62.586 -59.804  1.00 97.00  ? 9    ALA   D HB1  1 
ATOM   19566 H  HB2  . ALA   D  4  9   ? 19.675  -61.132 -60.336  1.00 97.00  ? 9    ALA   D HB2  1 
ATOM   19567 H  HB3  . ALA   D  4  9   ? 20.839  -62.154 -59.983  1.00 97.00  ? 9    ALA   D HB3  1 
ATOM   19568 N  N    . GLU   D  4  10  ? 19.303  -63.060 -56.756  1.00 85.19  ? 10   GLU   D N    1 
ATOM   19569 C  CA   . GLU   D  4  10  ? 19.455  -64.195 -55.860  1.00 88.90  ? 10   GLU   D CA   1 
ATOM   19570 C  C    . GLU   D  4  10  ? 18.934  -65.453 -56.542  1.00 94.21  ? 10   GLU   D C    1 
ATOM   19571 O  O    . GLU   D  4  10  ? 17.914  -65.416 -57.238  1.00 95.80  ? 10   GLU   D O    1 
ATOM   19572 C  CB   . GLU   D  4  10  ? 18.699  -63.968 -54.546  1.00 89.03  ? 10   GLU   D CB   1 
ATOM   19573 C  CG   . GLU   D  4  10  ? 19.127  -62.729 -53.763  1.00 87.45  ? 10   GLU   D CG   1 
ATOM   19574 C  CD   . GLU   D  4  10  ? 20.346  -62.967 -52.890  1.00 92.69  ? 10   GLU   D CD   1 
ATOM   19575 O  OE1  . GLU   D  4  10  ? 20.857  -64.106 -52.867  1.00 96.86  ? 10   GLU   D OE1  1 
ATOM   19576 O  OE2  . GLU   D  4  10  ? 20.790  -62.010 -52.221  1.00 92.51  ? 10   GLU   D OE2  1 
ATOM   19577 H  H    . GLU   D  4  10  ? 18.484  -62.819 -56.862  1.00 102.27 ? 10   GLU   D H    1 
ATOM   19578 H  HA   . GLU   D  4  10  ? 20.394  -64.320 -55.651  1.00 106.71 ? 10   GLU   D HA   1 
ATOM   19579 H  HB2  . GLU   D  4  10  ? 17.755  -63.874 -54.747  1.00 106.87 ? 10   GLU   D HB2  1 
ATOM   19580 H  HB3  . GLU   D  4  10  ? 18.841  -64.738 -53.973  1.00 106.87 ? 10   GLU   D HB3  1 
ATOM   19581 H  HG2  . GLU   D  4  10  ? 19.342  -62.020 -54.389  1.00 104.97 ? 10   GLU   D HG2  1 
ATOM   19582 H  HG3  . GLU   D  4  10  ? 18.397  -62.454 -53.187  1.00 104.97 ? 10   GLU   D HG3  1 
ATOM   19583 N  N    . LEU   D  4  11  ? 19.645  -66.560 -56.348  1.00 92.94  ? 11   LEU   D N    1 
ATOM   19584 C  CA   . LEU   D  4  11  ? 19.201  -67.879 -56.774  1.00 94.09  ? 11   LEU   D CA   1 
ATOM   19585 C  C    . LEU   D  4  11  ? 19.124  -68.775 -55.545  1.00 94.31  ? 11   LEU   D C    1 
ATOM   19586 O  O    . LEU   D  4  11  ? 19.993  -68.710 -54.669  1.00 96.54  ? 11   LEU   D O    1 
ATOM   19587 C  CB   . LEU   D  4  11  ? 20.155  -68.496 -57.805  1.00 100.75 ? 11   LEU   D CB   1 
ATOM   19588 C  CG   . LEU   D  4  11  ? 20.743  -67.589 -58.888  1.00 102.90 ? 11   LEU   D CG   1 
ATOM   19589 C  CD1  . LEU   D  4  11  ? 21.889  -68.309 -59.581  1.00 108.10 ? 11   LEU   D CD1  1 
ATOM   19590 C  CD2  . LEU   D  4  11  ? 19.692  -67.159 -59.902  1.00 101.70 ? 11   LEU   D CD2  1 
ATOM   19591 H  H    . LEU   D  4  11  ? 20.412  -66.570 -55.959  1.00 111.56 ? 11   LEU   D H    1 
ATOM   19592 H  HA   . LEU   D  4  11  ? 18.326  -67.817 -57.188  1.00 112.94 ? 11   LEU   D HA   1 
ATOM   19593 H  HB2  . LEU   D  4  11  ? 20.906  -68.872 -57.320  1.00 120.94 ? 11   LEU   D HB2  1 
ATOM   19594 H  HB3  . LEU   D  4  11  ? 19.672  -69.200 -58.265  1.00 120.94 ? 11   LEU   D HB3  1 
ATOM   19595 H  HG   . LEU   D  4  11  ? 21.076  -66.780 -58.470  1.00 123.52 ? 11   LEU   D HG   1 
ATOM   19596 H  HD11 . LEU   D  4  11  ? 22.298  -67.707 -60.222  1.00 129.75 ? 11   LEU   D HD11 1 
ATOM   19597 H  HD12 . LEU   D  4  11  ? 22.542  -68.577 -58.916  1.00 129.75 ? 11   LEU   D HD12 1 
ATOM   19598 H  HD13 . LEU   D  4  11  ? 21.540  -69.091 -60.037  1.00 129.75 ? 11   LEU   D HD13 1 
ATOM   19599 H  HD21 . LEU   D  4  11  ? 20.109  -66.586 -60.565  1.00 122.07 ? 11   LEU   D HD21 1 
ATOM   19600 H  HD22 . LEU   D  4  11  ? 19.325  -67.947 -60.331  1.00 122.07 ? 11   LEU   D HD22 1 
ATOM   19601 H  HD23 . LEU   D  4  11  ? 18.989  -66.674 -59.442  1.00 122.07 ? 11   LEU   D HD23 1 
ATOM   19602 N  N    . ALA   D  4  12  ? 18.088  -69.607 -55.474  1.00 90.09  ? 12   ALA   D N    1 
ATOM   19603 C  CA   . ALA   D  4  12  ? 17.929  -70.471 -54.313  1.00 88.86  ? 12   ALA   D CA   1 
ATOM   19604 C  C    . ALA   D  4  12  ? 17.102  -71.691 -54.686  1.00 95.01  ? 12   ALA   D C    1 
ATOM   19605 O  O    . ALA   D  4  12  ? 16.259  -71.638 -55.584  1.00 94.45  ? 12   ALA   D O    1 
ATOM   19606 C  CB   . ALA   D  4  12  ? 17.271  -69.722 -53.148  1.00 79.80  ? 12   ALA   D CB   1 
ATOM   19607 H  H    . ALA   D  4  12  ? 17.478  -69.687 -56.074  1.00 108.15 ? 12   ALA   D H    1 
ATOM   19608 H  HA   . ALA   D  4  12  ? 18.804  -70.782 -54.034  1.00 106.67 ? 12   ALA   D HA   1 
ATOM   19609 H  HB1  . ALA   D  4  12  ? 17.194  -70.323 -52.390  1.00 95.80  ? 12   ALA   D HB1  1 
ATOM   19610 H  HB2  . ALA   D  4  12  ? 17.821  -68.960 -52.912  1.00 95.80  ? 12   ALA   D HB2  1 
ATOM   19611 H  HB3  . ALA   D  4  12  ? 16.390  -69.422 -53.423  1.00 95.80  ? 12   ALA   D HB3  1 
ATOM   19612 N  N    . GLU   D  4  13  ? 17.360  -72.787 -53.980  1.00 100.42 ? 13   GLU   D N    1 
ATOM   19613 C  CA   . GLU   D  4  13  ? 16.597  -74.011 -54.149  1.00 103.54 ? 13   GLU   D CA   1 
ATOM   19614 C  C    . GLU   D  4  13  ? 15.297  -73.934 -53.355  1.00 100.28 ? 13   GLU   D C    1 
ATOM   19615 O  O    . GLU   D  4  13  ? 15.191  -73.171 -52.391  1.00 95.82  ? 13   GLU   D O    1 
ATOM   19616 C  CB   . GLU   D  4  13  ? 17.423  -75.208 -53.691  1.00 108.83 ? 13   GLU   D CB   1 
ATOM   19617 C  CG   . GLU   D  4  13  ? 18.753  -75.356 -54.413  1.00 114.48 ? 13   GLU   D CG   1 
ATOM   19618 C  CD   . GLU   D  4  13  ? 19.598  -76.486 -53.857  1.00 120.92 ? 13   GLU   D CD   1 
ATOM   19619 O  OE1  . GLU   D  4  13  ? 19.876  -76.480 -52.639  1.00 122.46 ? 13   GLU   D OE1  1 
ATOM   19620 O  OE2  . GLU   D  4  13  ? 19.978  -77.384 -54.638  1.00 127.34 ? 13   GLU   D OE2  1 
ATOM   19621 H  H    . GLU   D  4  13  ? 17.981  -72.846 -53.389  1.00 120.54 ? 13   GLU   D H    1 
ATOM   19622 H  HA   . GLU   D  4  13  ? 16.378  -74.138 -55.086  1.00 124.29 ? 13   GLU   D HA   1 
ATOM   19623 H  HB2  . GLU   D  4  13  ? 17.610  -75.112 -52.744  1.00 130.63 ? 13   GLU   D HB2  1 
ATOM   19624 H  HB3  . GLU   D  4  13  ? 16.911  -76.017 -53.848  1.00 130.63 ? 13   GLU   D HB3  1 
ATOM   19625 H  HG2  . GLU   D  4  13  ? 18.586  -75.539 -55.350  1.00 137.41 ? 13   GLU   D HG2  1 
ATOM   19626 H  HG3  . GLU   D  4  13  ? 19.257  -74.531 -54.320  1.00 137.41 ? 13   GLU   D HG3  1 
ATOM   19627 N  N    . PRO   D  4  14  ? 14.286  -74.714 -53.738  1.00 103.64 ? 14   PRO   D N    1 
ATOM   19628 C  CA   . PRO   D  4  14  ? 13.020  -74.683 -52.995  1.00 102.60 ? 14   PRO   D CA   1 
ATOM   19629 C  C    . PRO   D  4  14  ? 13.228  -75.034 -51.529  1.00 106.27 ? 14   PRO   D C    1 
ATOM   19630 O  O    . PRO   D  4  14  ? 14.060  -75.875 -51.182  1.00 112.00 ? 14   PRO   D O    1 
ATOM   19631 C  CB   . PRO   D  4  14  ? 12.159  -75.729 -53.713  1.00 104.78 ? 14   PRO   D CB   1 
ATOM   19632 C  CG   . PRO   D  4  14  ? 12.746  -75.834 -55.080  1.00 105.83 ? 14   PRO   D CG   1 
ATOM   19633 C  CD   . PRO   D  4  14  ? 14.218  -75.612 -54.905  1.00 107.40 ? 14   PRO   D CD   1 
ATOM   19634 H  HA   . PRO   D  4  14  ? 12.602  -73.810 -53.065  1.00 123.16 ? 14   PRO   D HA   1 
ATOM   19635 H  HB2  . PRO   D  4  14  ? 12.211  -76.577 -53.246  1.00 125.77 ? 14   PRO   D HB2  1 
ATOM   19636 H  HB3  . PRO   D  4  14  ? 11.238  -75.428 -53.752  1.00 125.77 ? 14   PRO   D HB3  1 
ATOM   19637 H  HG2  . PRO   D  4  14  ? 12.572  -76.715 -55.445  1.00 127.03 ? 14   PRO   D HG2  1 
ATOM   19638 H  HG3  . PRO   D  4  14  ? 12.362  -75.154 -55.655  1.00 127.03 ? 14   PRO   D HG3  1 
ATOM   19639 H  HD2  . PRO   D  4  14  ? 14.674  -76.449 -54.724  1.00 128.92 ? 14   PRO   D HD2  1 
ATOM   19640 H  HD3  . PRO   D  4  14  ? 14.600  -75.189 -55.690  1.00 128.92 ? 14   PRO   D HD3  1 
ATOM   19641 N  N    . GLY   D  4  15  ? 12.457  -74.372 -50.664  1.00 104.70 ? 15   GLY   D N    1 
ATOM   19642 C  CA   . GLY   D  4  15  ? 12.572  -74.550 -49.234  1.00 107.75 ? 15   GLY   D CA   1 
ATOM   19643 C  C    . GLY   D  4  15  ? 13.652  -73.726 -48.568  1.00 109.03 ? 15   GLY   D C    1 
ATOM   19644 O  O    . GLY   D  4  15  ? 13.626  -73.573 -47.341  1.00 112.19 ? 15   GLY   D O    1 
ATOM   19645 H  H    . GLY   D  4  15  ? 11.852  -73.807 -50.894  1.00 125.68 ? 15   GLY   D H    1 
ATOM   19646 H  HA2  . GLY   D  4  15  ? 11.726  -74.312 -48.824  1.00 129.33 ? 15   GLY   D HA2  1 
ATOM   19647 H  HA3  . GLY   D  4  15  ? 12.760  -75.484 -49.052  1.00 129.33 ? 15   GLY   D HA3  1 
ATOM   19648 N  N    . ALA   D  4  16  ? 14.601  -73.186 -49.332  1.00 104.60 ? 16   ALA   D N    1 
ATOM   19649 C  CA   . ALA   D  4  16  ? 15.691  -72.403 -48.765  1.00 106.50 ? 16   ALA   D CA   1 
ATOM   19650 C  C    . ALA   D  4  16  ? 15.240  -70.976 -48.478  1.00 95.58  ? 16   ALA   D C    1 
ATOM   19651 O  O    . ALA   D  4  16  ? 14.037  -70.695 -48.439  1.00 91.96  ? 16   ALA   D O    1 
ATOM   19652 C  CB   . ALA   D  4  16  ? 16.893  -72.399 -49.712  1.00 112.90 ? 16   ALA   D CB   1 
ATOM   19653 H  H    . ALA   D  4  16  ? 14.634  -73.260 -50.188  1.00 125.55 ? 16   ALA   D H    1 
ATOM   19654 H  HA   . ALA   D  4  16  ? 15.967  -72.805 -47.926  1.00 127.84 ? 16   ALA   D HA   1 
ATOM   19655 H  HB1  . ALA   D  4  16  ? 17.620  -71.908 -49.299  1.00 135.51 ? 16   ALA   D HB1  1 
ATOM   19656 H  HB2  . ALA   D  4  16  ? 17.166  -73.315 -49.880  1.00 135.51 ? 16   ALA   D HB2  1 
ATOM   19657 H  HB3  . ALA   D  4  16  ? 16.637  -71.972 -50.545  1.00 135.51 ? 16   ALA   D HB3  1 
ATOM   19658 N  N    . SER   D  4  17  ? 16.196  -70.072 -48.272  1.00 98.38  ? 17   SER   D N    1 
ATOM   19659 C  CA   . SER   D  4  17  ? 15.897  -68.670 -48.032  1.00 90.65  ? 17   SER   D CA   1 
ATOM   19660 C  C    . SER   D  4  17  ? 16.937  -67.810 -48.734  1.00 88.58  ? 17   SER   D C    1 
ATOM   19661 O  O    . SER   D  4  17  ? 18.015  -68.279 -49.108  1.00 93.75  ? 17   SER   D O    1 
ATOM   19662 C  CB   . SER   D  4  17  ? 15.878  -68.338 -46.534  1.00 94.10  ? 17   SER   D CB   1 
ATOM   19663 O  OG   . SER   D  4  17  ? 17.192  -68.127 -46.047  1.00 95.10  ? 17   SER   D OG   1 
ATOM   19664 H  H    . SER   D  4  17  ? 17.036  -70.253 -48.268  1.00 118.09 ? 17   SER   D H    1 
ATOM   19665 H  HA   . SER   D  4  17  ? 15.025  -68.464 -48.403  1.00 108.82 ? 17   SER   D HA   1 
ATOM   19666 H  HB2  . SER   D  4  17  ? 15.357  -67.532 -46.396  1.00 112.96 ? 17   SER   D HB2  1 
ATOM   19667 H  HB3  . SER   D  4  17  ? 15.478  -69.079 -46.052  1.00 112.96 ? 17   SER   D HB3  1 
ATOM   19668 H  HG   . SER   D  4  17  ? 17.176  -68.020 -45.214  1.00 114.16 ? 17   SER   D HG   1 
ATOM   19669 N  N    . VAL   D  4  18  ? 16.595  -66.533 -48.909  1.00 77.59  ? 18   VAL   D N    1 
ATOM   19670 C  CA   . VAL   D  4  18  ? 17.501  -65.540 -49.467  1.00 74.92  ? 18   VAL   D CA   1 
ATOM   19671 C  C    . VAL   D  4  18  ? 17.360  -64.261 -48.654  1.00 83.59  ? 18   VAL   D C    1 
ATOM   19672 O  O    . VAL   D  4  18  ? 16.338  -64.015 -48.011  1.00 85.58  ? 18   VAL   D O    1 
ATOM   19673 C  CB   . VAL   D  4  18  ? 17.226  -65.253 -50.960  1.00 84.19  ? 18   VAL   D CB   1 
ATOM   19674 C  CG1  . VAL   D  4  18  ? 17.500  -66.490 -51.798  1.00 78.46  ? 18   VAL   D CG1  1 
ATOM   19675 C  CG2  . VAL   D  4  18  ? 15.795  -64.769 -51.159  1.00 81.73  ? 18   VAL   D CG2  1 
ATOM   19676 H  H    . VAL   D  4  18  ? 15.823  -66.214 -48.705  1.00 92.93  ? 18   VAL   D H    1 
ATOM   19677 H  HA   . VAL   D  4  18  ? 18.413  -65.861 -49.391  1.00 89.72  ? 18   VAL   D HA   1 
ATOM   19678 H  HB   . VAL   D  4  18  ? 17.823  -64.549 -51.260  1.00 101.06 ? 18   VAL   D HB   1 
ATOM   19679 H  HG11 . VAL   D  4  18  ? 17.325  -66.285 -52.730  1.00 93.97  ? 18   VAL   D HG11 1 
ATOM   19680 H  HG12 . VAL   D  4  18  ? 18.427  -66.749 -51.684  1.00 93.97  ? 18   VAL   D HG12 1 
ATOM   19681 H  HG13 . VAL   D  4  18  ? 16.917  -67.207 -51.502  1.00 93.97  ? 18   VAL   D HG13 1 
ATOM   19682 H  HG21 . VAL   D  4  18  ? 15.644  -64.607 -52.103  1.00 98.11  ? 18   VAL   D HG21 1 
ATOM   19683 H  HG22 . VAL   D  4  18  ? 15.184  -65.450 -50.838  1.00 98.11  ? 18   VAL   D HG22 1 
ATOM   19684 H  HG23 . VAL   D  4  18  ? 15.667  -63.948 -50.658  1.00 98.11  ? 18   VAL   D HG23 1 
ATOM   19685 N  N    . LYS   D  4  19  ? 18.408  -63.443 -48.691  1.00 79.14  ? 19   LYS   D N    1 
ATOM   19686 C  CA   . LYS   D  4  19  ? 18.420  -62.154 -48.012  1.00 75.59  ? 19   LYS   D CA   1 
ATOM   19687 C  C    . LYS   D  4  19  ? 18.982  -61.118 -48.971  1.00 76.10  ? 19   LYS   D C    1 
ATOM   19688 O  O    . LYS   D  4  19  ? 20.118  -61.250 -49.437  1.00 83.03  ? 19   LYS   D O    1 
ATOM   19689 C  CB   . LYS   D  4  19  ? 19.248  -62.210 -46.727  1.00 76.96  ? 19   LYS   D CB   1 
ATOM   19690 C  CG   . LYS   D  4  19  ? 18.967  -61.078 -45.751  1.00 76.83  ? 19   LYS   D CG   1 
ATOM   19691 C  CD   . LYS   D  4  19  ? 19.973  -61.093 -44.615  1.00 81.30  ? 19   LYS   D CD   1 
ATOM   19692 C  CE   . LYS   D  4  19  ? 19.614  -60.110 -43.517  1.00 81.02  ? 19   LYS   D CE   1 
ATOM   19693 N  NZ   . LYS   D  4  19  ? 20.662  -60.087 -42.460  1.00 85.43  ? 19   LYS   D NZ   1 
ATOM   19694 H  H    . LYS   D  4  19  ? 19.137  -63.617 -49.112  1.00 95.01  ? 19   LYS   D H    1 
ATOM   19695 H  HA   . LYS   D  4  19  ? 17.515  -61.899 -47.774  1.00 90.74  ? 19   LYS   D HA   1 
ATOM   19696 H  HB2  . LYS   D  4  19  ? 19.058  -63.045 -46.272  1.00 92.39  ? 19   LYS   D HB2  1 
ATOM   19697 H  HB3  . LYS   D  4  19  ? 20.188  -62.167 -46.963  1.00 92.39  ? 19   LYS   D HB3  1 
ATOM   19698 H  HG2  . LYS   D  4  19  ? 19.034  -60.227 -46.212  1.00 92.24  ? 19   LYS   D HG2  1 
ATOM   19699 H  HG3  . LYS   D  4  19  ? 18.078  -61.184 -45.378  1.00 92.24  ? 19   LYS   D HG3  1 
ATOM   19700 H  HD2  . LYS   D  4  19  ? 20.001  -61.982 -44.227  1.00 97.60  ? 19   LYS   D HD2  1 
ATOM   19701 H  HD3  . LYS   D  4  19  ? 20.847  -60.854 -44.961  1.00 97.60  ? 19   LYS   D HD3  1 
ATOM   19702 H  HE2  . LYS   D  4  19  ? 19.537  -59.219 -43.893  1.00 97.26  ? 19   LYS   D HE2  1 
ATOM   19703 H  HE3  . LYS   D  4  19  ? 18.773  -60.372 -43.110  1.00 97.26  ? 19   LYS   D HE3  1 
ATOM   19704 H  HZ1  . LYS   D  4  19  ? 20.428  -59.525 -41.811  1.00 102.56 ? 19   LYS   D HZ1  1 
ATOM   19705 H  HZ2  . LYS   D  4  19  ? 20.763  -60.901 -42.114  1.00 102.56 ? 19   LYS   D HZ2  1 
ATOM   19706 H  HZ3  . LYS   D  4  19  ? 21.438  -59.822 -42.806  1.00 102.56 ? 19   LYS   D HZ3  1 
ATOM   19707 N  N    . MET   D  4  20  ? 18.185  -60.095 -49.264  1.00 70.19  ? 20   MET   D N    1 
ATOM   19708 C  CA   . MET   D  4  20  ? 18.547  -59.043 -50.198  1.00 70.27  ? 20   MET   D CA   1 
ATOM   19709 C  C    . MET   D  4  20  ? 18.644  -57.722 -49.451  1.00 70.95  ? 20   MET   D C    1 
ATOM   19710 O  O    . MET   D  4  20  ? 18.009  -57.534 -48.409  1.00 73.16  ? 20   MET   D O    1 
ATOM   19711 C  CB   . MET   D  4  20  ? 17.514  -58.932 -51.319  1.00 72.26  ? 20   MET   D CB   1 
ATOM   19712 C  CG   . MET   D  4  20  ? 16.122  -58.584 -50.815  1.00 73.15  ? 20   MET   D CG   1 
ATOM   19713 S  SD   . MET   D  4  20  ? 14.846  -58.750 -52.074  1.00 73.43  ? 20   MET   D SD   1 
ATOM   19714 C  CE   . MET   D  4  20  ? 14.897  -60.515 -52.375  1.00 76.83  ? 20   MET   D CE   1 
ATOM   19715 H  H    . MET   D  4  20  ? 17.404  -59.989 -48.921  1.00 84.27  ? 20   MET   D H    1 
ATOM   19716 H  HA   . MET   D  4  20  ? 19.405  -59.241 -50.604  1.00 84.36  ? 20   MET   D HA   1 
ATOM   19717 H  HB2  . MET   D  4  20  ? 17.792  -58.236 -51.934  1.00 86.75  ? 20   MET   D HB2  1 
ATOM   19718 H  HB3  . MET   D  4  20  ? 17.460  -59.783 -51.782  1.00 86.75  ? 20   MET   D HB3  1 
ATOM   19719 H  HG2  . MET   D  4  20  ? 15.896  -59.178 -50.082  1.00 87.82  ? 20   MET   D HG2  1 
ATOM   19720 H  HG3  . MET   D  4  20  ? 16.120  -57.664 -50.510  1.00 87.82  ? 20   MET   D HG3  1 
ATOM   19721 H  HE1  . MET   D  4  20  ? 14.200  -60.748 -53.008  1.00 92.23  ? 20   MET   D HE1  1 
ATOM   19722 H  HE2  . MET   D  4  20  ? 15.765  -60.748 -52.739  1.00 92.23  ? 20   MET   D HE2  1 
ATOM   19723 H  HE3  . MET   D  4  20  ? 14.753  -60.983 -51.538  1.00 92.23  ? 20   MET   D HE3  1 
ATOM   19724 N  N    . SER   D  4  21  ? 19.437  -56.804 -49.990  1.00 70.60  ? 21   SER   D N    1 
ATOM   19725 C  CA   . SER   D  4  21  ? 19.698  -55.531 -49.338  1.00 66.68  ? 21   SER   D CA   1 
ATOM   19726 C  C    . SER   D  4  21  ? 19.188  -54.379 -50.198  1.00 63.38  ? 21   SER   D C    1 
ATOM   19727 O  O    . SER   D  4  21  ? 18.702  -54.563 -51.318  1.00 63.73  ? 21   SER   D O    1 
ATOM   19728 C  CB   . SER   D  4  21  ? 21.192  -55.365 -49.043  1.00 68.63  ? 21   SER   D CB   1 
ATOM   19729 O  OG   . SER   D  4  21  ? 21.934  -55.193 -50.236  1.00 71.91  ? 21   SER   D OG   1 
ATOM   19730 H  H    . SER   D  4  21  ? 19.839  -56.900 -50.744  1.00 84.76  ? 21   SER   D H    1 
ATOM   19731 H  HA   . SER   D  4  21  ? 19.213  -55.514 -48.498  1.00 80.05  ? 21   SER   D HA   1 
ATOM   19732 H  HB2  . SER   D  4  21  ? 21.316  -54.584 -48.481  1.00 82.39  ? 21   SER   D HB2  1 
ATOM   19733 H  HB3  . SER   D  4  21  ? 21.512  -56.158 -48.585  1.00 82.39  ? 21   SER   D HB3  1 
ATOM   19734 H  HG   . SER   D  4  21  ? 22.751  -55.110 -50.057  1.00 86.33  ? 21   SER   D HG   1 
ATOM   19735 N  N    . CYS   D  4  22  ? 19.320  -53.176 -49.644  1.00 64.65  ? 22   CYS   D N    1 
ATOM   19736 C  CA   . CYS   D  4  22  ? 18.790  -51.953 -50.230  1.00 66.30  ? 22   CYS   D CA   1 
ATOM   19737 C  C    . CYS   D  4  22  ? 19.413  -50.769 -49.501  1.00 66.91  ? 22   CYS   D C    1 
ATOM   19738 O  O    . CYS   D  4  22  ? 18.948  -50.392 -48.421  1.00 64.55  ? 22   CYS   D O    1 
ATOM   19739 C  CB   . CYS   D  4  22  ? 17.264  -51.925 -50.121  1.00 67.38  ? 22   CYS   D CB   1 
ATOM   19740 S  SG   . CYS   D  4  22  ? 16.478  -50.333 -50.486  1.00 70.41  ? 22   CYS   D SG   1 
ATOM   19741 H  H    . CYS   D  4  22  ? 19.728  -53.039 -48.900  1.00 77.62  ? 22   CYS   D H    1 
ATOM   19742 H  HA   . CYS   D  4  22  ? 19.003  -51.898 -51.175  1.00 79.60  ? 22   CYS   D HA   1 
ATOM   19743 H  HB2  . CYS   D  4  22  ? 16.903  -52.574 -50.745  1.00 80.89  ? 22   CYS   D HB2  1 
ATOM   19744 H  HB3  . CYS   D  4  22  ? 17.020  -52.166 -49.214  1.00 80.89  ? 22   CYS   D HB3  1 
ATOM   19745 N  N    . LYS   D  4  23  ? 20.474  -50.193 -50.063  1.00 70.79  ? 23   LYS   D N    1 
ATOM   19746 C  CA   . LYS   D  4  23  ? 21.221  -49.135 -49.395  1.00 74.52  ? 23   LYS   D CA   1 
ATOM   19747 C  C    . LYS   D  4  23  ? 20.711  -47.777 -49.855  1.00 68.14  ? 23   LYS   D C    1 
ATOM   19748 O  O    . LYS   D  4  23  ? 20.579  -47.530 -51.058  1.00 68.94  ? 23   LYS   D O    1 
ATOM   19749 C  CB   . LYS   D  4  23  ? 22.721  -49.252 -49.673  1.00 83.95  ? 23   LYS   D CB   1 
ATOM   19750 C  CG   . LYS   D  4  23  ? 23.550  -48.207 -48.928  1.00 91.89  ? 23   LYS   D CG   1 
ATOM   19751 C  CD   . LYS   D  4  23  ? 25.040  -48.351 -49.197  1.00 104.26 ? 23   LYS   D CD   1 
ATOM   19752 C  CE   . LYS   D  4  23  ? 25.842  -47.249 -48.510  1.00 113.01 ? 23   LYS   D CE   1 
ATOM   19753 N  NZ   . LYS   D  4  23  ? 25.925  -47.414 -47.030  1.00 117.31 ? 23   LYS   D NZ   1 
ATOM   19754 H  H    . LYS   D  4  23  ? 20.783  -50.401 -50.839  1.00 84.98  ? 23   LYS   D H    1 
ATOM   19755 H  HA   . LYS   D  4  23  ? 21.087  -49.213 -48.437  1.00 89.46  ? 23   LYS   D HA   1 
ATOM   19756 H  HB2  . LYS   D  4  23  ? 23.026  -50.130 -49.394  1.00 100.77 ? 23   LYS   D HB2  1 
ATOM   19757 H  HB3  . LYS   D  4  23  ? 22.875  -49.134 -50.623  1.00 100.77 ? 23   LYS   D HB3  1 
ATOM   19758 H  HG2  . LYS   D  4  23  ? 23.277  -47.322 -49.214  1.00 110.30 ? 23   LYS   D HG2  1 
ATOM   19759 H  HG3  . LYS   D  4  23  ? 23.406  -48.308 -47.974  1.00 110.30 ? 23   LYS   D HG3  1 
ATOM   19760 H  HD2  . LYS   D  4  23  ? 25.346  -49.207 -48.859  1.00 125.15 ? 23   LYS   D HD2  1 
ATOM   19761 H  HD3  . LYS   D  4  23  ? 25.200  -48.294 -50.152  1.00 125.15 ? 23   LYS   D HD3  1 
ATOM   19762 H  HE2  . LYS   D  4  23  ? 26.746  -47.253 -48.861  1.00 135.65 ? 23   LYS   D HE2  1 
ATOM   19763 H  HE3  . LYS   D  4  23  ? 25.420  -46.394 -48.691  1.00 135.65 ? 23   LYS   D HE3  1 
ATOM   19764 H  HZ1  . LYS   D  4  23  ? 26.326  -46.707 -46.666  1.00 140.81 ? 23   LYS   D HZ1  1 
ATOM   19765 H  HZ2  . LYS   D  4  23  ? 25.108  -47.491 -46.686  1.00 140.81 ? 23   LYS   D HZ2  1 
ATOM   19766 H  HZ3  . LYS   D  4  23  ? 26.392  -48.145 -46.831  1.00 140.81 ? 23   LYS   D HZ3  1 
ATOM   19767 N  N    . ALA   D  4  24  ? 20.440  -46.900 -48.895  1.00 64.30  ? 24   ALA   D N    1 
ATOM   19768 C  CA   . ALA   D  4  24  ? 19.883  -45.586 -49.167  1.00 61.09  ? 24   ALA   D CA   1 
ATOM   19769 C  C    . ALA   D  4  24  ? 20.959  -44.511 -49.091  1.00 61.41  ? 24   ALA   D C    1 
ATOM   19770 O  O    . ALA   D  4  24  ? 21.907  -44.601 -48.305  1.00 62.61  ? 24   ALA   D O    1 
ATOM   19771 C  CB   . ALA   D  4  24  ? 18.760  -45.256 -48.182  1.00 59.12  ? 24   ALA   D CB   1 
ATOM   19772 H  H    . ALA   D  4  24  ? 20.574  -47.049 -48.058  1.00 77.19  ? 24   ALA   D H    1 
ATOM   19773 H  HA   . ALA   D  4  24  ? 19.518  -45.580 -50.066  1.00 73.35  ? 24   ALA   D HA   1 
ATOM   19774 H  HB1  . ALA   D  4  24  ? 18.404  -44.379 -48.391  1.00 70.99  ? 24   ALA   D HB1  1 
ATOM   19775 H  HB2  . ALA   D  4  24  ? 18.062  -45.925 -48.264  1.00 70.99  ? 24   ALA   D HB2  1 
ATOM   19776 H  HB3  . ALA   D  4  24  ? 19.119  -45.262 -47.281  1.00 70.99  ? 24   ALA   D HB3  1 
ATOM   19777 N  N    . SER   D  4  25  ? 20.796  -43.488 -49.926  1.00 57.88  ? 25   SER   D N    1 
ATOM   19778 C  CA   . SER   D  4  25  ? 21.661  -42.320 -49.918  1.00 59.67  ? 25   SER   D CA   1 
ATOM   19779 C  C    . SER   D  4  25  ? 20.839  -41.125 -50.377  1.00 59.61  ? 25   SER   D C    1 
ATOM   19780 O  O    . SER   D  4  25  ? 19.799  -41.277 -51.022  1.00 62.25  ? 25   SER   D O    1 
ATOM   19781 C  CB   . SER   D  4  25  ? 22.886  -42.512 -50.820  1.00 64.40  ? 25   SER   D CB   1 
ATOM   19782 O  OG   . SER   D  4  25  ? 22.497  -42.700 -52.169  1.00 62.88  ? 25   SER   D OG   1 
ATOM   19783 H  H    . SER   D  4  25  ? 20.176  -43.449 -50.520  1.00 69.49  ? 25   SER   D H    1 
ATOM   19784 H  HA   . SER   D  4  25  ? 21.983  -42.153 -49.019  1.00 71.64  ? 25   SER   D HA   1 
ATOM   19785 H  HB2  . SER   D  4  25  ? 23.448  -41.724 -50.761  1.00 77.31  ? 25   SER   D HB2  1 
ATOM   19786 H  HB3  . SER   D  4  25  ? 23.377  -43.294 -50.522  1.00 77.31  ? 25   SER   D HB3  1 
ATOM   19787 H  HG   . SER   D  4  25  ? 23.175  -42.819 -52.650  1.00 75.50  ? 25   SER   D HG   1 
ATOM   19788 N  N    . GLY   D  4  26  ? 21.313  -39.932 -50.032  1.00 59.39  ? 26   GLY   D N    1 
ATOM   19789 C  CA   . GLY   D  4  26  ? 20.632  -38.711 -50.405  1.00 58.09  ? 26   GLY   D CA   1 
ATOM   19790 C  C    . GLY   D  4  26  ? 19.582  -38.235 -49.427  1.00 54.74  ? 26   GLY   D C    1 
ATOM   19791 O  O    . GLY   D  4  26  ? 18.978  -37.179 -49.660  1.00 54.89  ? 26   GLY   D O    1 
ATOM   19792 H  H    . GLY   D  4  26  ? 22.032  -39.808 -49.578  1.00 71.30  ? 26   GLY   D H    1 
ATOM   19793 H  HA2  . GLY   D  4  26  ? 21.291  -38.005 -50.497  1.00 69.74  ? 26   GLY   D HA2  1 
ATOM   19794 H  HA3  . GLY   D  4  26  ? 20.197  -38.849 -51.261  1.00 69.74  ? 26   GLY   D HA3  1 
ATOM   19795 N  N    . TYR   D  4  27  ? 19.335  -38.976 -48.350  1.00 53.75  ? 27   TYR   D N    1 
ATOM   19796 C  CA   . TYR   D  4  27  ? 18.412  -38.540 -47.311  1.00 51.86  ? 27   TYR   D CA   1 
ATOM   19797 C  C    . TYR   D  4  27  ? 18.750  -39.291 -46.032  1.00 55.08  ? 27   TYR   D C    1 
ATOM   19798 O  O    . TYR   D  4  27  ? 19.515  -40.259 -46.038  1.00 57.80  ? 27   TYR   D O    1 
ATOM   19799 C  CB   . TYR   D  4  27  ? 16.952  -38.771 -47.714  1.00 49.58  ? 27   TYR   D CB   1 
ATOM   19800 C  CG   . TYR   D  4  27  ? 16.523  -40.220 -47.672  1.00 51.46  ? 27   TYR   D CG   1 
ATOM   19801 C  CD1  . TYR   D  4  27  ? 16.822  -41.083 -48.717  1.00 53.66  ? 27   TYR   D CD1  1 
ATOM   19802 C  CD2  . TYR   D  4  27  ? 15.814  -40.725 -46.589  1.00 53.72  ? 27   TYR   D CD2  1 
ATOM   19803 C  CE1  . TYR   D  4  27  ? 16.431  -42.408 -48.684  1.00 56.94  ? 27   TYR   D CE1  1 
ATOM   19804 C  CE2  . TYR   D  4  27  ? 15.418  -42.049 -46.547  1.00 57.61  ? 27   TYR   D CE2  1 
ATOM   19805 C  CZ   . TYR   D  4  27  ? 15.730  -42.886 -47.598  1.00 59.69  ? 27   TYR   D CZ   1 
ATOM   19806 O  OH   . TYR   D  4  27  ? 15.338  -44.204 -47.562  1.00 63.32  ? 27   TYR   D OH   1 
ATOM   19807 H  H    . TYR   D  4  27  ? 19.694  -39.742 -48.198  1.00 64.54  ? 27   TYR   D H    1 
ATOM   19808 H  HA   . TYR   D  4  27  ? 18.533  -37.590 -47.156  1.00 62.27  ? 27   TYR   D HA   1 
ATOM   19809 H  HB2  . TYR   D  4  27  ? 16.380  -38.277 -47.107  1.00 59.53  ? 27   TYR   D HB2  1 
ATOM   19810 H  HB3  . TYR   D  4  27  ? 16.826  -38.453 -48.622  1.00 59.53  ? 27   TYR   D HB3  1 
ATOM   19811 H  HD1  . TYR   D  4  27  ? 17.294  -40.764 -49.451  1.00 64.43  ? 27   TYR   D HD1  1 
ATOM   19812 H  HD2  . TYR   D  4  27  ? 15.601  -40.162 -45.880  1.00 64.49  ? 27   TYR   D HD2  1 
ATOM   19813 H  HE1  . TYR   D  4  27  ? 16.640  -42.974 -49.392  1.00 68.37  ? 27   TYR   D HE1  1 
ATOM   19814 H  HE2  . TYR   D  4  27  ? 14.945  -42.373 -45.815  1.00 69.17  ? 27   TYR   D HE2  1 
ATOM   19815 H  HH   . TYR   D  4  27  ? 14.956  -44.371 -46.833  1.00 76.03  ? 27   TYR   D HH   1 
ATOM   19816 N  N    . THR   D  4  28  ? 18.167  -38.829 -44.929  1.00 54.33  ? 28   THR   D N    1 
ATOM   19817 C  CA   . THR   D  4  28  ? 18.401  -39.436 -43.621  1.00 53.56  ? 28   THR   D CA   1 
ATOM   19818 C  C    . THR   D  4  28  ? 17.600  -40.731 -43.549  1.00 54.65  ? 28   THR   D C    1 
ATOM   19819 O  O    . THR   D  4  28  ? 16.381  -40.721 -43.360  1.00 53.10  ? 28   THR   D O    1 
ATOM   19820 C  CB   . THR   D  4  28  ? 18.031  -38.468 -42.505  1.00 53.64  ? 28   THR   D CB   1 
ATOM   19821 O  OG1  . THR   D  4  28  ? 18.823  -37.279 -42.632  1.00 54.21  ? 28   THR   D OG1  1 
ATOM   19822 C  CG2  . THR   D  4  28  ? 18.290  -39.098 -41.144  1.00 54.07  ? 28   THR   D CG2  1 
ATOM   19823 H  H    . THR   D  4  28  ? 17.628  -38.159 -44.912  1.00 65.24  ? 28   THR   D H    1 
ATOM   19824 H  HA   . THR   D  4  28  ? 19.341  -39.656 -43.522  1.00 64.31  ? 28   THR   D HA   1 
ATOM   19825 H  HB   . THR   D  4  28  ? 17.089  -38.246 -42.565  1.00 64.41  ? 28   THR   D HB   1 
ATOM   19826 H  HG1  . THR   D  4  28  ? 18.410  -36.623 -42.308  1.00 65.09  ? 28   THR   D HG1  1 
ATOM   19827 H  HG21 . THR   D  4  28  ? 18.084  -38.463 -40.440  1.00 64.92  ? 28   THR   D HG21 1 
ATOM   19828 H  HG22 . THR   D  4  28  ? 17.733  -39.884 -41.031  1.00 64.92  ? 28   THR   D HG22 1 
ATOM   19829 H  HG23 . THR   D  4  28  ? 19.221  -39.359 -41.070  1.00 64.92  ? 28   THR   D HG23 1 
ATOM   19830 N  N    . PHE   D  4  29  ? 18.309  -41.850 -43.698  1.00 55.90  ? 29   PHE   D N    1 
ATOM   19831 C  CA   . PHE   D  4  29  ? 17.674  -43.161 -43.790  1.00 54.09  ? 29   PHE   D CA   1 
ATOM   19832 C  C    . PHE   D  4  29  ? 16.782  -43.449 -42.589  1.00 54.94  ? 29   PHE   D C    1 
ATOM   19833 O  O    . PHE   D  4  29  ? 15.683  -43.996 -42.742  1.00 54.49  ? 29   PHE   D O    1 
ATOM   19834 C  CB   . PHE   D  4  29  ? 18.773  -44.217 -43.926  1.00 53.35  ? 29   PHE   D CB   1 
ATOM   19835 C  CG   . PHE   D  4  29  ? 18.281  -45.631 -43.905  1.00 50.39  ? 29   PHE   D CG   1 
ATOM   19836 C  CD1  . PHE   D  4  29  ? 17.690  -46.190 -45.024  1.00 50.72  ? 29   PHE   D CD1  1 
ATOM   19837 C  CD2  . PHE   D  4  29  ? 18.447  -46.414 -42.776  1.00 52.39  ? 29   PHE   D CD2  1 
ATOM   19838 C  CE1  . PHE   D  4  29  ? 17.254  -47.499 -45.011  1.00 54.87  ? 29   PHE   D CE1  1 
ATOM   19839 C  CE2  . PHE   D  4  29  ? 18.018  -47.724 -42.757  1.00 54.62  ? 29   PHE   D CE2  1 
ATOM   19840 C  CZ   . PHE   D  4  29  ? 17.419  -48.268 -43.875  1.00 55.51  ? 29   PHE   D CZ   1 
ATOM   19841 H  H    . PHE   D  4  29  ? 19.167  -41.878 -43.750  1.00 67.12  ? 29   PHE   D H    1 
ATOM   19842 H  HA   . PHE   D  4  29  ? 17.102  -43.193 -44.573  1.00 64.94  ? 29   PHE   D HA   1 
ATOM   19843 H  HB2  . PHE   D  4  29  ? 19.232  -44.079 -44.769  1.00 64.06  ? 29   PHE   D HB2  1 
ATOM   19844 H  HB3  . PHE   D  4  29  ? 19.394  -44.113 -43.188  1.00 64.06  ? 29   PHE   D HB3  1 
ATOM   19845 H  HD1  . PHE   D  4  29  ? 17.586  -45.678 -45.793  1.00 60.90  ? 29   PHE   D HD1  1 
ATOM   19846 H  HD2  . PHE   D  4  29  ? 18.853  -46.053 -42.022  1.00 62.90  ? 29   PHE   D HD2  1 
ATOM   19847 H  HE1  . PHE   D  4  29  ? 16.850  -47.863 -45.765  1.00 65.88  ? 29   PHE   D HE1  1 
ATOM   19848 H  HE2  . PHE   D  4  29  ? 18.131  -48.240 -41.992  1.00 65.58  ? 29   PHE   D HE2  1 
ATOM   19849 H  HZ   . PHE   D  4  29  ? 17.126  -49.151 -43.864  1.00 66.65  ? 29   PHE   D HZ   1 
ATOM   19850 N  N    . SER   D  4  30  ? 17.229  -43.081 -41.388  1.00 56.32  ? 30   SER   D N    1 
ATOM   19851 C  CA   . SER   D  4  30  ? 16.522  -43.469 -40.174  1.00 62.26  ? 30   SER   D CA   1 
ATOM   19852 C  C    . SER   D  4  30  ? 15.170  -42.782 -40.022  1.00 59.81  ? 30   SER   D C    1 
ATOM   19853 O  O    . SER   D  4  30  ? 14.323  -43.275 -39.270  1.00 60.11  ? 30   SER   D O    1 
ATOM   19854 C  CB   . SER   D  4  30  ? 17.381  -43.155 -38.950  1.00 70.49  ? 30   SER   D CB   1 
ATOM   19855 O  OG   . SER   D  4  30  ? 17.604  -41.759 -38.843  1.00 75.96  ? 30   SER   D OG   1 
ATOM   19856 H  H    . SER   D  4  30  ? 17.936  -42.610 -41.252  1.00 67.62  ? 30   SER   D H    1 
ATOM   19857 H  HA   . SER   D  4  30  ? 16.364  -44.426 -40.212  1.00 74.75  ? 30   SER   D HA   1 
ATOM   19858 H  HB2  . SER   D  4  30  ? 16.924  -43.464 -38.153  1.00 84.63  ? 30   SER   D HB2  1 
ATOM   19859 H  HB3  . SER   D  4  30  ? 18.236  -43.606 -39.038  1.00 84.63  ? 30   SER   D HB3  1 
ATOM   19860 H  HG   . SER   D  4  30  ? 18.009  -41.586 -38.128  1.00 91.19  ? 30   SER   D HG   1 
ATOM   19861 N  N    . SER   D  4  31  ? 14.948  -41.664 -40.707  1.00 57.60  ? 31   SER   D N    1 
ATOM   19862 C  CA   . SER   D  4  31  ? 13.760  -40.852 -40.485  1.00 53.85  ? 31   SER   D CA   1 
ATOM   19863 C  C    . SER   D  4  31  ? 12.600  -41.205 -41.405  1.00 54.06  ? 31   SER   D C    1 
ATOM   19864 O  O    . SER   D  4  31  ? 11.545  -40.568 -41.312  1.00 52.74  ? 31   SER   D O    1 
ATOM   19865 C  CB   . SER   D  4  31  ? 14.103  -39.368 -40.656  1.00 53.28  ? 31   SER   D CB   1 
ATOM   19866 O  OG   . SER   D  4  31  ? 15.067  -38.952 -39.706  1.00 54.61  ? 31   SER   D OG   1 
ATOM   19867 H  H    . SER   D  4  31  ? 15.476  -41.354 -41.311  1.00 69.16  ? 31   SER   D H    1 
ATOM   19868 H  HA   . SER   D  4  31  ? 13.464  -40.996 -39.572  1.00 64.66  ? 31   SER   D HA   1 
ATOM   19869 H  HB2  . SER   D  4  31  ? 14.460  -39.228 -41.547  1.00 63.97  ? 31   SER   D HB2  1 
ATOM   19870 H  HB3  . SER   D  4  31  ? 13.296  -38.843 -40.536  1.00 63.97  ? 31   SER   D HB3  1 
ATOM   19871 H  HG   . SER   D  4  31  ? 15.189  -38.123 -39.764  1.00 65.57  ? 31   SER   D HG   1 
ATOM   19872 N  N    . PHE   D  4  32  ? 12.755  -42.196 -42.280  1.00 55.05  ? 32   PHE   D N    1 
ATOM   19873 C  CA   . PHE   D  4  32  ? 11.710  -42.530 -43.237  1.00 52.12  ? 32   PHE   D CA   1 
ATOM   19874 C  C    . PHE   D  4  32  ? 11.530  -44.035 -43.323  1.00 53.45  ? 32   PHE   D C    1 
ATOM   19875 O  O    . PHE   D  4  32  ? 12.507  -44.788 -43.362  1.00 58.50  ? 32   PHE   D O    1 
ATOM   19876 C  CB   . PHE   D  4  32  ? 12.031  -41.963 -44.622  1.00 51.86  ? 32   PHE   D CB   1 
ATOM   19877 C  CG   . PHE   D  4  32  ? 12.122  -40.471 -44.646  1.00 51.01  ? 32   PHE   D CG   1 
ATOM   19878 C  CD1  . PHE   D  4  32  ? 10.994  -39.700 -44.868  1.00 52.65  ? 32   PHE   D CD1  1 
ATOM   19879 C  CD2  . PHE   D  4  32  ? 13.332  -39.838 -44.428  1.00 52.37  ? 32   PHE   D CD2  1 
ATOM   19880 C  CE1  . PHE   D  4  32  ? 11.074  -38.323 -44.882  1.00 54.31  ? 32   PHE   D CE1  1 
ATOM   19881 C  CE2  . PHE   D  4  32  ? 13.419  -38.463 -44.440  1.00 54.33  ? 32   PHE   D CE2  1 
ATOM   19882 C  CZ   . PHE   D  4  32  ? 12.288  -37.702 -44.667  1.00 53.19  ? 32   PHE   D CZ   1 
ATOM   19883 H  H    . PHE   D  4  32  ? 13.458  -42.689 -42.338  1.00 66.10  ? 32   PHE   D H    1 
ATOM   19884 H  HA   . PHE   D  4  32  ? 10.869  -42.155 -42.931  1.00 62.58  ? 32   PHE   D HA   1 
ATOM   19885 H  HB2  . PHE   D  4  32  ? 12.884  -42.318 -44.916  1.00 62.27  ? 32   PHE   D HB2  1 
ATOM   19886 H  HB3  . PHE   D  4  32  ? 11.331  -42.228 -45.239  1.00 62.27  ? 32   PHE   D HB3  1 
ATOM   19887 H  HD1  . PHE   D  4  32  ? 10.174  -40.115 -45.009  1.00 63.22  ? 32   PHE   D HD1  1 
ATOM   19888 H  HD2  . PHE   D  4  32  ? 14.095  -40.345 -44.271  1.00 62.88  ? 32   PHE   D HD2  1 
ATOM   19889 H  HE1  . PHE   D  4  32  ? 10.311  -37.814 -45.037  1.00 65.21  ? 32   PHE   D HE1  1 
ATOM   19890 H  HE2  . PHE   D  4  32  ? 14.239  -38.047 -44.297  1.00 65.23  ? 32   PHE   D HE2  1 
ATOM   19891 H  HZ   . PHE   D  4  32  ? 12.345  -36.774 -44.674  1.00 63.87  ? 32   PHE   D HZ   1 
ATOM   19892 N  N    . TRP   D  4  33  ? 10.271  -44.461 -43.352  1.00 51.41  ? 33   TRP   D N    1 
ATOM   19893 C  CA   . TRP   D  4  33  ? 9.964   -45.871 -43.520  1.00 52.09  ? 33   TRP   D CA   1 
ATOM   19894 C  C    . TRP   D  4  33  ? 10.475  -46.368 -44.866  1.00 52.22  ? 33   TRP   D C    1 
ATOM   19895 O  O    . TRP   D  4  33  ? 10.624  -45.604 -45.824  1.00 47.48  ? 33   TRP   D O    1 
ATOM   19896 C  CB   . TRP   D  4  33  ? 8.459   -46.110 -43.432  1.00 53.10  ? 33   TRP   D CB   1 
ATOM   19897 C  CG   . TRP   D  4  33  ? 7.845   -45.752 -42.120  1.00 54.80  ? 33   TRP   D CG   1 
ATOM   19898 C  CD1  . TRP   D  4  33  ? 8.489   -45.333 -40.992  1.00 54.73  ? 33   TRP   D CD1  1 
ATOM   19899 C  CD2  . TRP   D  4  33  ? 6.452   -45.783 -41.799  1.00 54.75  ? 33   TRP   D CD2  1 
ATOM   19900 N  NE1  . TRP   D  4  33  ? 7.580   -45.102 -39.988  1.00 53.20  ? 33   TRP   D NE1  1 
ATOM   19901 C  CE2  . TRP   D  4  33  ? 6.321   -45.371 -40.459  1.00 53.67  ? 33   TRP   D CE2  1 
ATOM   19902 C  CE3  . TRP   D  4  33  ? 5.300   -46.120 -42.517  1.00 55.77  ? 33   TRP   D CE3  1 
ATOM   19903 C  CZ2  . TRP   D  4  33  ? 5.086   -45.287 -39.822  1.00 54.50  ? 33   TRP   D CZ2  1 
ATOM   19904 C  CZ3  . TRP   D  4  33  ? 4.076   -46.036 -41.885  1.00 57.10  ? 33   TRP   D CZ3  1 
ATOM   19905 C  CH2  . TRP   D  4  33  ? 3.977   -45.623 -40.551  1.00 56.45  ? 33   TRP   D CH2  1 
ATOM   19906 H  H    . TRP   D  4  33  ? 9.580   -43.954 -43.277  1.00 61.73  ? 33   TRP   D H    1 
ATOM   19907 H  HA   . TRP   D  4  33  ? 10.396  -46.375 -42.812  1.00 62.54  ? 33   TRP   D HA   1 
ATOM   19908 H  HB2  . TRP   D  4  33  ? 8.022   -45.576 -44.114  1.00 63.76  ? 33   TRP   D HB2  1 
ATOM   19909 H  HB3  . TRP   D  4  33  ? 8.287   -47.052 -43.588  1.00 63.76  ? 33   TRP   D HB3  1 
ATOM   19910 H  HD1  . TRP   D  4  33  ? 9.409   -45.221 -40.915  1.00 65.72  ? 33   TRP   D HD1  1 
ATOM   19911 H  HE1  . TRP   D  4  33  ? 7.769   -44.833 -39.193  1.00 63.88  ? 33   TRP   D HE1  1 
ATOM   19912 H  HE3  . TRP   D  4  33  ? 5.358   -46.396 -43.403  1.00 66.96  ? 33   TRP   D HE3  1 
ATOM   19913 H  HZ2  . TRP   D  4  33  ? 5.016   -45.014 -38.936  1.00 65.43  ? 33   TRP   D HZ2  1 
ATOM   19914 H  HZ3  . TRP   D  4  33  ? 3.304   -46.259 -42.353  1.00 68.56  ? 33   TRP   D HZ3  1 
ATOM   19915 H  HH2  . TRP   D  4  33  ? 3.139   -45.574 -40.152  1.00 67.78  ? 33   TRP   D HH2  1 
ATOM   19916 N  N    . MET   D  4  34  ? 10.735  -47.669 -44.932  1.00 56.16  ? 34   MET   D N    1 
ATOM   19917 C  CA   . MET   D  4  34  ? 11.111  -48.342 -46.167  1.00 57.52  ? 34   MET   D CA   1 
ATOM   19918 C  C    . MET   D  4  34  ? 10.057  -49.394 -46.473  1.00 61.55  ? 34   MET   D C    1 
ATOM   19919 O  O    . MET   D  4  34  ? 9.780   -50.260 -45.635  1.00 63.36  ? 34   MET   D O    1 
ATOM   19920 C  CB   . MET   D  4  34  ? 12.492  -48.986 -46.049  1.00 56.86  ? 34   MET   D CB   1 
ATOM   19921 C  CG   . MET   D  4  34  ? 13.009  -49.552 -47.359  1.00 57.40  ? 34   MET   D CG   1 
ATOM   19922 S  SD   . MET   D  4  34  ? 13.447  -48.259 -48.534  1.00 57.37  ? 34   MET   D SD   1 
ATOM   19923 C  CE   . MET   D  4  34  ? 14.939  -47.622 -47.776  1.00 59.01  ? 34   MET   D CE   1 
ATOM   19924 H  H    . MET   D  4  34  ? 10.698  -48.197 -44.254  1.00 67.43  ? 34   MET   D H    1 
ATOM   19925 H  HA   . MET   D  4  34  ? 11.146  -47.695 -46.888  1.00 69.06  ? 34   MET   D HA   1 
ATOM   19926 H  HB2  . MET   D  4  34  ? 13.124  -48.316 -45.745  1.00 68.27  ? 34   MET   D HB2  1 
ATOM   19927 H  HB3  . MET   D  4  34  ? 12.445  -49.713 -45.409  1.00 68.27  ? 34   MET   D HB3  1 
ATOM   19928 H  HG2  . MET   D  4  34  ? 13.801  -50.084 -47.185  1.00 68.91  ? 34   MET   D HG2  1 
ATOM   19929 H  HG3  . MET   D  4  34  ? 12.320  -50.104 -47.760  1.00 68.91  ? 34   MET   D HG3  1 
ATOM   19930 H  HE1  . MET   D  4  34  ? 15.273  -46.884 -48.308  1.00 70.85  ? 34   MET   D HE1  1 
ATOM   19931 H  HE2  . MET   D  4  34  ? 14.732  -47.317 -46.879  1.00 70.85  ? 34   MET   D HE2  1 
ATOM   19932 H  HE3  . MET   D  4  34  ? 15.602  -48.330 -47.739  1.00 70.85  ? 34   MET   D HE3  1 
ATOM   19933 N  N    . HIS   D  4  35  ? 9.472   -49.316 -47.661  1.00 63.74  ? 35   HIS   D N    1 
ATOM   19934 C  CA   . HIS   D  4  35  ? 8.486   -50.282 -48.117  1.00 61.60  ? 35   HIS   D CA   1 
ATOM   19935 C  C    . HIS   D  4  35  ? 9.138   -51.293 -49.053  1.00 60.60  ? 35   HIS   D C    1 
ATOM   19936 O  O    . HIS   D  4  35  ? 10.172  -51.028 -49.671  1.00 59.33  ? 35   HIS   D O    1 
ATOM   19937 C  CB   . HIS   D  4  35  ? 7.329   -49.576 -48.828  1.00 58.83  ? 35   HIS   D CB   1 
ATOM   19938 C  CG   . HIS   D  4  35  ? 6.571   -48.627 -47.952  1.00 62.75  ? 35   HIS   D CG   1 
ATOM   19939 N  ND1  . HIS   D  4  35  ? 5.255   -48.830 -47.599  1.00 64.53  ? 35   HIS   D ND1  1 
ATOM   19940 C  CD2  . HIS   D  4  35  ? 6.946   -47.471 -47.355  1.00 62.85  ? 35   HIS   D CD2  1 
ATOM   19941 C  CE1  . HIS   D  4  35  ? 4.850   -47.839 -46.825  1.00 64.31  ? 35   HIS   D CE1  1 
ATOM   19942 N  NE2  . HIS   D  4  35  ? 5.857   -47.001 -46.661  1.00 62.79  ? 35   HIS   D NE2  1 
ATOM   19943 H  H    . HIS   D  4  35  ? 9.635   -48.696 -48.234  1.00 76.53  ? 35   HIS   D H    1 
ATOM   19944 H  HA   . HIS   D  4  35  ? 8.123   -50.760 -47.355  1.00 73.96  ? 35   HIS   D HA   1 
ATOM   19945 H  HB2  . HIS   D  4  35  ? 7.684   -49.070 -49.575  1.00 70.63  ? 35   HIS   D HB2  1 
ATOM   19946 H  HB3  . HIS   D  4  35  ? 6.705   -50.246 -49.148  1.00 70.63  ? 35   HIS   D HB3  1 
ATOM   19947 H  HD2  . HIS   D  4  35  ? 7.784   -47.070 -47.405  1.00 75.46  ? 35   HIS   D HD2  1 
ATOM   19948 H  HE1  . HIS   D  4  35  ? 4.000   -47.747 -46.458  1.00 77.21  ? 35   HIS   D HE1  1 
ATOM   19949 H  HE2  . HIS   D  4  35  ? 5.836   -46.279 -46.195  1.00 75.39  ? 35   HIS   D HE2  1 
ATOM   19950 N  N    . TRP   D  4  36  ? 8.519   -52.468 -49.143  1.00 59.20  ? 36   TRP   D N    1 
ATOM   19951 C  CA   . TRP   D  4  36  ? 8.954   -53.516 -50.055  1.00 57.70  ? 36   TRP   D CA   1 
ATOM   19952 C  C    . TRP   D  4  36  ? 7.776   -53.944 -50.917  1.00 56.59  ? 36   TRP   D C    1 
ATOM   19953 O  O    . TRP   D  4  36  ? 6.639   -54.010 -50.441  1.00 53.22  ? 36   TRP   D O    1 
ATOM   19954 C  CB   . TRP   D  4  36  ? 9.529   -54.721 -49.298  1.00 59.42  ? 36   TRP   D CB   1 
ATOM   19955 C  CG   . TRP   D  4  36  ? 10.828  -54.430 -48.602  1.00 60.65  ? 36   TRP   D CG   1 
ATOM   19956 C  CD1  . TRP   D  4  36  ? 10.988  -53.913 -47.349  1.00 59.24  ? 36   TRP   D CD1  1 
ATOM   19957 C  CD2  . TRP   D  4  36  ? 12.149  -54.642 -49.119  1.00 62.97  ? 36   TRP   D CD2  1 
ATOM   19958 N  NE1  . TRP   D  4  36  ? 12.324  -53.789 -47.054  1.00 59.87  ? 36   TRP   D NE1  1 
ATOM   19959 C  CE2  . TRP   D  4  36  ? 13.058  -54.229 -48.124  1.00 61.79  ? 36   TRP   D CE2  1 
ATOM   19960 C  CE3  . TRP   D  4  36  ? 12.651  -55.140 -50.326  1.00 65.44  ? 36   TRP   D CE3  1 
ATOM   19961 C  CZ2  . TRP   D  4  36  ? 14.440  -54.299 -48.299  1.00 62.76  ? 36   TRP   D CZ2  1 
ATOM   19962 C  CZ3  . TRP   D  4  36  ? 14.024  -55.207 -50.498  1.00 67.58  ? 36   TRP   D CZ3  1 
ATOM   19963 C  CH2  . TRP   D  4  36  ? 14.901  -54.789 -49.489  1.00 66.95  ? 36   TRP   D CH2  1 
ATOM   19964 H  H    . TRP   D  4  36  ? 7.831   -52.683 -48.675  1.00 71.07  ? 36   TRP   D H    1 
ATOM   19965 H  HA   . TRP   D  4  36  ? 9.652   -53.176 -50.638  1.00 69.28  ? 36   TRP   D HA   1 
ATOM   19966 H  HB2  . TRP   D  4  36  ? 8.888   -55.002 -48.626  1.00 71.35  ? 36   TRP   D HB2  1 
ATOM   19967 H  HB3  . TRP   D  4  36  ? 9.685   -55.441 -49.929  1.00 71.35  ? 36   TRP   D HB3  1 
ATOM   19968 H  HD1  . TRP   D  4  36  ? 10.293  -53.679 -46.777  1.00 71.12  ? 36   TRP   D HD1  1 
ATOM   19969 H  HE1  . TRP   D  4  36  ? 12.648  -53.484 -46.318  1.00 71.88  ? 36   TRP   D HE1  1 
ATOM   19970 H  HE3  . TRP   D  4  36  ? 12.075  -55.420 -51.000  1.00 78.57  ? 36   TRP   D HE3  1 
ATOM   19971 H  HZ2  . TRP   D  4  36  ? 15.025  -54.022 -47.631  1.00 75.35  ? 36   TRP   D HZ2  1 
ATOM   19972 H  HZ3  . TRP   D  4  36  ? 14.369  -55.536 -51.296  1.00 81.14  ? 36   TRP   D HZ3  1 
ATOM   19973 H  HH2  . TRP   D  4  36  ? 15.819  -54.846 -49.632  1.00 80.38  ? 36   TRP   D HH2  1 
ATOM   19974 N  N    . VAL   D  4  37  ? 8.057   -54.232 -52.187  1.00 57.71  ? 37   VAL   D N    1 
ATOM   19975 C  CA   . VAL   D  4  37  ? 7.027   -54.559 -53.165  1.00 58.97  ? 37   VAL   D CA   1 
ATOM   19976 C  C    . VAL   D  4  37  ? 7.482   -55.764 -53.975  1.00 62.10  ? 37   VAL   D C    1 
ATOM   19977 O  O    . VAL   D  4  37  ? 8.671   -55.937 -54.258  1.00 64.11  ? 37   VAL   D O    1 
ATOM   19978 C  CB   . VAL   D  4  37  ? 6.725   -53.356 -54.089  1.00 59.12  ? 37   VAL   D CB   1 
ATOM   19979 C  CG1  . VAL   D  4  37  ? 5.693   -53.726 -55.149  1.00 61.47  ? 37   VAL   D CG1  1 
ATOM   19980 C  CG2  . VAL   D  4  37  ? 6.247   -52.167 -53.265  1.00 55.75  ? 37   VAL   D CG2  1 
ATOM   19981 H  H    . VAL   D  4  37  ? 8.853   -54.244 -52.511  1.00 69.29  ? 37   VAL   D H    1 
ATOM   19982 H  HA   . VAL   D  4  37  ? 6.210   -54.804 -52.704  1.00 70.80  ? 37   VAL   D HA   1 
ATOM   19983 H  HB   . VAL   D  4  37  ? 7.541   -53.103 -54.548  1.00 70.99  ? 37   VAL   D HB   1 
ATOM   19984 H  HG11 . VAL   D  4  37  ? 5.501   -52.943 -55.689  1.00 73.80  ? 37   VAL   D HG11 1 
ATOM   19985 H  HG12 . VAL   D  4  37  ? 6.054   -54.432 -55.708  1.00 73.80  ? 37   VAL   D HG12 1 
ATOM   19986 H  HG13 . VAL   D  4  37  ? 4.884   -54.032 -54.710  1.00 73.80  ? 37   VAL   D HG13 1 
ATOM   19987 H  HG21 . VAL   D  4  37  ? 6.050   -51.428 -53.861  1.00 66.93  ? 37   VAL   D HG21 1 
ATOM   19988 H  HG22 . VAL   D  4  37  ? 5.448   -52.422 -52.777  1.00 66.93  ? 37   VAL   D HG22 1 
ATOM   19989 H  HG23 . VAL   D  4  37  ? 6.947   -51.912 -52.643  1.00 66.93  ? 37   VAL   D HG23 1 
ATOM   19990 N  N    . LYS   D  4  38  ? 6.516   -56.601 -54.349  1.00 63.75  ? 38   LYS   D N    1 
ATOM   19991 C  CA   . LYS   D  4  38  ? 6.760   -57.821 -55.105  1.00 66.52  ? 38   LYS   D CA   1 
ATOM   19992 C  C    . LYS   D  4  38  ? 6.104   -57.707 -56.473  1.00 70.64  ? 38   LYS   D C    1 
ATOM   19993 O  O    . LYS   D  4  38  ? 4.965   -57.246 -56.589  1.00 69.25  ? 38   LYS   D O    1 
ATOM   19994 C  CB   . LYS   D  4  38  ? 6.207   -59.040 -54.359  1.00 67.60  ? 38   LYS   D CB   1 
ATOM   19995 C  CG   . LYS   D  4  38  ? 6.432   -60.379 -55.045  1.00 71.70  ? 38   LYS   D CG   1 
ATOM   19996 C  CD   . LYS   D  4  38  ? 5.711   -61.483 -54.285  1.00 75.84  ? 38   LYS   D CD   1 
ATOM   19997 C  CE   . LYS   D  4  38  ? 5.886   -62.841 -54.939  1.00 82.31  ? 38   LYS   D CE   1 
ATOM   19998 N  NZ   . LYS   D  4  38  ? 5.016   -63.868 -54.299  1.00 86.79  ? 38   LYS   D NZ   1 
ATOM   19999 H  H    . LYS   D  4  38  ? 5.685   -56.476 -54.170  1.00 76.53  ? 38   LYS   D H    1 
ATOM   20000 H  HA   . LYS   D  4  38  ? 7.713   -57.947 -55.235  1.00 79.86  ? 38   LYS   D HA   1 
ATOM   20001 H  HB2  . LYS   D  4  38  ? 6.634   -59.085 -53.489  1.00 81.16  ? 38   LYS   D HB2  1 
ATOM   20002 H  HB3  . LYS   D  4  38  ? 5.250   -58.926 -54.253  1.00 81.16  ? 38   LYS   D HB3  1 
ATOM   20003 H  HG2  . LYS   D  4  38  ? 6.082   -60.345 -55.949  1.00 86.07  ? 38   LYS   D HG2  1 
ATOM   20004 H  HG3  . LYS   D  4  38  ? 7.380   -60.581 -55.063  1.00 86.07  ? 38   LYS   D HG3  1 
ATOM   20005 H  HD2  . LYS   D  4  38  ? 6.068   -61.534 -53.384  1.00 91.05  ? 38   LYS   D HD2  1 
ATOM   20006 H  HD3  . LYS   D  4  38  ? 4.763   -61.282 -54.255  1.00 91.05  ? 38   LYS   D HD3  1 
ATOM   20007 H  HE2  . LYS   D  4  38  ? 5.647   -62.780 -55.877  1.00 98.81  ? 38   LYS   D HE2  1 
ATOM   20008 H  HE3  . LYS   D  4  38  ? 6.810   -63.125 -54.850  1.00 98.81  ? 38   LYS   D HE3  1 
ATOM   20009 H  HZ1  . LYS   D  4  38  ? 5.111   -64.649 -54.714  1.00 104.19 ? 38   LYS   D HZ1  1 
ATOM   20010 H  HZ2  . LYS   D  4  38  ? 5.241   -63.966 -53.443  1.00 104.19 ? 38   LYS   D HZ2  1 
ATOM   20011 H  HZ3  . LYS   D  4  38  ? 4.164   -63.617 -54.346  1.00 104.19 ? 38   LYS   D HZ3  1 
ATOM   20012 N  N    . GLN   D  4  39  ? 6.828   -58.130 -57.509  1.00 75.76  ? 39   GLN   D N    1 
ATOM   20013 C  CA   . GLN   D  4  39  ? 6.311   -58.122 -58.874  1.00 80.90  ? 39   GLN   D CA   1 
ATOM   20014 C  C    . GLN   D  4  39  ? 6.738   -59.414 -59.555  1.00 89.81  ? 39   GLN   D C    1 
ATOM   20015 O  O    . GLN   D  4  39  ? 7.916   -59.582 -59.885  1.00 87.55  ? 39   GLN   D O    1 
ATOM   20016 C  CB   . GLN   D  4  39  ? 6.816   -56.909 -59.655  1.00 76.94  ? 39   GLN   D CB   1 
ATOM   20017 C  CG   . GLN   D  4  39  ? 6.204   -56.774 -61.041  1.00 75.88  ? 39   GLN   D CG   1 
ATOM   20018 C  CD   . GLN   D  4  39  ? 6.607   -55.489 -61.735  1.00 73.02  ? 39   GLN   D CD   1 
ATOM   20019 O  OE1  . GLN   D  4  39  ? 7.703   -54.972 -61.523  1.00 69.68  ? 39   GLN   D OE1  1 
ATOM   20020 N  NE2  . GLN   D  4  39  ? 5.715   -54.962 -62.566  1.00 71.34  ? 39   GLN   D NE2  1 
ATOM   20021 H  H    . GLN   D  4  39  ? 7.632   -58.429 -57.444  1.00 90.95  ? 39   GLN   D H    1 
ATOM   20022 H  HA   . GLN   D  4  39  ? 5.342   -58.092 -58.847  1.00 97.12  ? 39   GLN   D HA   1 
ATOM   20023 H  HB2  . GLN   D  4  39  ? 6.599   -56.105 -59.157  1.00 92.36  ? 39   GLN   D HB2  1 
ATOM   20024 H  HB3  . GLN   D  4  39  ? 7.777   -56.984 -59.761  1.00 92.36  ? 39   GLN   D HB3  1 
ATOM   20025 H  HG2  . GLN   D  4  39  ? 6.499   -57.518 -61.591  1.00 91.10  ? 39   GLN   D HG2  1 
ATOM   20026 H  HG3  . GLN   D  4  39  ? 5.237   -56.783 -60.963  1.00 91.10  ? 39   GLN   D HG3  1 
ATOM   20027 H  HE21 . GLN   D  4  39  ? 4.957   -55.349 -62.685  1.00 85.64  ? 39   GLN   D HE21 1 
ATOM   20028 H  HE22 . GLN   D  4  39  ? 5.896   -54.232 -62.984  1.00 85.64  ? 39   GLN   D HE22 1 
ATOM   20029 N  N    . ARG   D  4  40  ? 5.788   -60.319 -59.768  1.00 98.68  ? 40   ARG   D N    1 
ATOM   20030 C  CA   . ARG   D  4  40  ? 6.092   -61.538 -60.495  1.00 107.52 ? 40   ARG   D CA   1 
ATOM   20031 C  C    . ARG   D  4  40  ? 6.281   -61.226 -61.978  1.00 102.69 ? 40   ARG   D C    1 
ATOM   20032 O  O    . ARG   D  4  40  ? 5.700   -60.268 -62.497  1.00 95.40  ? 40   ARG   D O    1 
ATOM   20033 C  CB   . ARG   D  4  40  ? 4.980   -62.567 -60.326  1.00 118.85 ? 40   ARG   D CB   1 
ATOM   20034 C  CG   . ARG   D  4  40  ? 5.147   -63.469 -59.120  1.00 122.63 ? 40   ARG   D CG   1 
ATOM   20035 C  CD   . ARG   D  4  40  ? 4.459   -64.803 -59.338  1.00 127.41 ? 40   ARG   D CD   1 
ATOM   20036 N  NE   . ARG   D  4  40  ? 3.891   -65.317 -58.098  1.00 130.79 ? 40   ARG   D NE   1 
ATOM   20037 C  CZ   . ARG   D  4  40  ? 2.701   -64.966 -57.621  1.00 137.02 ? 40   ARG   D CZ   1 
ATOM   20038 N  NH1  . ARG   D  4  40  ? 1.945   -64.097 -58.280  1.00 138.71 ? 40   ARG   D NH1  1 
ATOM   20039 N  NH2  . ARG   D  4  40  ? 2.265   -65.485 -56.482  1.00 144.63 ? 40   ARG   D NH2  1 
ATOM   20040 H  H    . ARG   D  4  40  ? 4.973   -60.250 -59.504  1.00 118.45 ? 40   ARG   D H    1 
ATOM   20041 H  HA   . ARG   D  4  40  ? 6.910   -61.926 -60.148  1.00 129.06 ? 40   ARG   D HA   1 
ATOM   20042 H  HB2  . ARG   D  4  40  ? 4.136   -62.099 -60.228  1.00 142.66 ? 40   ARG   D HB2  1 
ATOM   20043 H  HB3  . ARG   D  4  40  ? 4.956   -63.131 -61.115  1.00 142.66 ? 40   ARG   D HB3  1 
ATOM   20044 H  HG2  . ARG   D  4  40  ? 6.091   -63.633 -58.968  1.00 147.19 ? 40   ARG   D HG2  1 
ATOM   20045 H  HG3  . ARG   D  4  40  ? 4.754   -63.044 -58.342  1.00 147.19 ? 40   ARG   D HG3  1 
ATOM   20046 H  HD2  . ARG   D  4  40  ? 3.740   -64.692 -59.980  1.00 152.93 ? 40   ARG   D HD2  1 
ATOM   20047 H  HD3  . ARG   D  4  40  ? 5.104   -65.447 -59.669  1.00 152.93 ? 40   ARG   D HD3  1 
ATOM   20048 H  HE   . ARG   D  4  40  ? 4.355   -65.884 -57.647  1.00 156.98 ? 40   ARG   D HE   1 
ATOM   20049 H  HH11 . ARG   D  4  40  ? 2.225   -63.757 -59.019  1.00 166.49 ? 40   ARG   D HH11 1 
ATOM   20050 H  HH12 . ARG   D  4  40  ? 1.176   -63.872 -57.968  1.00 166.49 ? 40   ARG   D HH12 1 
ATOM   20051 H  HH21 . ARG   D  4  40  ? 2.752   -66.048 -56.051  1.00 173.59 ? 40   ARG   D HH21 1 
ATOM   20052 H  HH22 . ARG   D  4  40  ? 1.495   -65.258 -56.173  1.00 173.59 ? 40   ARG   D HH22 1 
ATOM   20053 N  N    . PRO   D  4  41  ? 7.089   -62.016 -62.681  1.00 106.43 ? 41   PRO   D N    1 
ATOM   20054 C  CA   . PRO   D  4  41  ? 7.303   -61.764 -64.111  1.00 110.43 ? 41   PRO   D CA   1 
ATOM   20055 C  C    . PRO   D  4  41  ? 5.989   -61.594 -64.857  1.00 114.40 ? 41   PRO   D C    1 
ATOM   20056 O  O    . PRO   D  4  41  ? 5.076   -62.416 -64.748  1.00 116.33 ? 41   PRO   D O    1 
ATOM   20057 C  CB   . PRO   D  4  41  ? 8.067   -63.009 -64.572  1.00 112.78 ? 41   PRO   D CB   1 
ATOM   20058 C  CG   . PRO   D  4  41  ? 8.803   -63.457 -63.355  1.00 109.89 ? 41   PRO   D CG   1 
ATOM   20059 C  CD   . PRO   D  4  41  ? 7.885   -63.161 -62.200  1.00 107.09 ? 41   PRO   D CD   1 
ATOM   20060 H  HA   . PRO   D  4  41  ? 7.851   -60.974 -64.241  1.00 132.56 ? 41   PRO   D HA   1 
ATOM   20061 H  HB2  . PRO   D  4  41  ? 7.445   -63.689 -64.876  1.00 135.38 ? 41   PRO   D HB2  1 
ATOM   20062 H  HB3  . PRO   D  4  41  ? 8.680   -62.778 -65.287  1.00 135.38 ? 41   PRO   D HB3  1 
ATOM   20063 H  HG2  . PRO   D  4  41  ? 8.988   -64.407 -63.414  1.00 131.90 ? 41   PRO   D HG2  1 
ATOM   20064 H  HG3  . PRO   D  4  41  ? 9.633   -62.962 -63.272  1.00 131.90 ? 41   PRO   D HG3  1 
ATOM   20065 H  HD2  . PRO   D  4  41  ? 7.315   -63.922 -62.009  1.00 128.55 ? 41   PRO   D HD2  1 
ATOM   20066 H  HD3  . PRO   D  4  41  ? 8.393   -62.920 -61.409  1.00 128.55 ? 41   PRO   D HD3  1 
ATOM   20067 N  N    . GLY   D  4  42  ? 5.892   -60.500 -65.612  1.00 116.11 ? 42   GLY   D N    1 
ATOM   20068 C  CA   . GLY   D  4  42  ? 4.706   -60.213 -66.393  1.00 118.56 ? 42   GLY   D CA   1 
ATOM   20069 C  C    . GLY   D  4  42  ? 3.465   -59.890 -65.595  1.00 115.23 ? 42   GLY   D C    1 
ATOM   20070 O  O    . GLY   D  4  42  ? 2.392   -59.741 -66.187  1.00 114.71 ? 42   GLY   D O    1 
ATOM   20071 H  H    . GLY   D  4  42  ? 6.509   -59.905 -65.684  1.00 139.36 ? 42   GLY   D H    1 
ATOM   20072 H  HA2  . GLY   D  4  42  ? 4.892   -59.454 -66.968  1.00 142.31 ? 42   GLY   D HA2  1 
ATOM   20073 H  HA3  . GLY   D  4  42  ? 4.507   -60.986 -66.945  1.00 142.31 ? 42   GLY   D HA3  1 
ATOM   20074 N  N    . GLN   D  4  43  ? 3.573   -59.766 -64.275  1.00 108.93 ? 43   GLN   D N    1 
ATOM   20075 C  CA   . GLN   D  4  43  ? 2.432   -59.537 -63.405  1.00 107.03 ? 43   GLN   D CA   1 
ATOM   20076 C  C    . GLN   D  4  43  ? 2.462   -58.110 -62.859  1.00 101.46 ? 43   GLN   D C    1 
ATOM   20077 O  O    . GLN   D  4  43  ? 3.296   -57.285 -63.252  1.00 99.30  ? 43   GLN   D O    1 
ATOM   20078 C  CB   . GLN   D  4  43  ? 2.421   -60.578 -62.282  1.00 107.23 ? 43   GLN   D CB   1 
ATOM   20079 C  CG   . GLN   D  4  43  ? 1.967   -61.955 -62.734  1.00 110.65 ? 43   GLN   D CG   1 
ATOM   20080 C  CD   . GLN   D  4  43  ? 0.537   -61.953 -63.239  1.00 112.09 ? 43   GLN   D CD   1 
ATOM   20081 O  OE1  . GLN   D  4  43  ? 0.250   -62.448 -64.329  1.00 115.15 ? 43   GLN   D OE1  1 
ATOM   20082 N  NE2  . GLN   D  4  43  ? -0.369  -61.392 -62.446  1.00 110.24 ? 43   GLN   D NE2  1 
ATOM   20083 H  H    . GLN   D  4  43  ? 4.320   -59.814 -63.852  1.00 130.76 ? 43   GLN   D H    1 
ATOM   20084 H  HA   . GLN   D  4  43  ? 1.620   -59.637 -63.926  1.00 128.48 ? 43   GLN   D HA   1 
ATOM   20085 H  HB2  . GLN   D  4  43  ? 3.320   -60.663 -61.927  1.00 128.72 ? 43   GLN   D HB2  1 
ATOM   20086 H  HB3  . GLN   D  4  43  ? 1.816   -60.280 -61.586  1.00 128.72 ? 43   GLN   D HB3  1 
ATOM   20087 H  HG2  . GLN   D  4  43  ? 2.541   -62.258 -63.455  1.00 132.82 ? 43   GLN   D HG2  1 
ATOM   20088 H  HG3  . GLN   D  4  43  ? 2.022   -62.569 -61.986  1.00 132.82 ? 43   GLN   D HG3  1 
ATOM   20089 H  HE21 . GLN   D  4  43  ? -0.130  -61.055 -61.692  1.00 132.32 ? 43   GLN   D HE21 1 
ATOM   20090 H  HE22 . GLN   D  4  43  ? -1.194  -61.366 -62.687  1.00 132.32 ? 43   GLN   D HE22 1 
ATOM   20091 N  N    . GLY   D  4  44  ? 1.537   -57.819 -61.950  1.00 97.11  ? 44   GLY   D N    1 
ATOM   20092 C  CA   . GLY   D  4  44  ? 1.415   -56.508 -61.351  1.00 94.29  ? 44   GLY   D CA   1 
ATOM   20093 C  C    . GLY   D  4  44  ? 2.234   -56.374 -60.086  1.00 92.59  ? 44   GLY   D C    1 
ATOM   20094 O  O    . GLY   D  4  44  ? 3.169   -57.137 -59.831  1.00 96.55  ? 44   GLY   D O    1 
ATOM   20095 H  H    . GLY   D  4  44  ? 0.956   -58.383 -61.661  1.00 116.56 ? 44   GLY   D H    1 
ATOM   20096 H  HA2  . GLY   D  4  44  ? 1.717   -55.837 -61.983  1.00 113.18 ? 44   GLY   D HA2  1 
ATOM   20097 H  HA3  . GLY   D  4  44  ? 0.485   -56.340 -61.132  1.00 113.18 ? 44   GLY   D HA3  1 
ATOM   20098 N  N    . LEU   D  4  45  ? 1.862   -55.389 -59.275  1.00 78.22  ? 45   LEU   D N    1 
ATOM   20099 C  CA   . LEU   D  4  45  ? 2.610   -55.029 -58.080  1.00 72.56  ? 45   LEU   D CA   1 
ATOM   20100 C  C    . LEU   D  4  45  ? 1.862   -55.466 -56.828  1.00 70.91  ? 45   LEU   D C    1 
ATOM   20101 O  O    . LEU   D  4  45  ? 0.644   -55.291 -56.721  1.00 68.20  ? 45   LEU   D O    1 
ATOM   20102 C  CB   . LEU   D  4  45  ? 2.873   -53.522 -58.040  1.00 69.23  ? 45   LEU   D CB   1 
ATOM   20103 C  CG   . LEU   D  4  45  ? 3.734   -53.008 -59.197  1.00 73.46  ? 45   LEU   D CG   1 
ATOM   20104 C  CD1  . LEU   D  4  45  ? 3.783   -51.492 -59.194  1.00 72.12  ? 45   LEU   D CD1  1 
ATOM   20105 C  CD2  . LEU   D  4  45  ? 5.141   -53.588 -59.129  1.00 77.66  ? 45   LEU   D CD2  1 
ATOM   20106 H  H    . LEU   D  4  45  ? 1.163   -54.903 -59.401  1.00 93.90  ? 45   LEU   D H    1 
ATOM   20107 H  HA   . LEU   D  4  45  ? 3.463   -55.490 -58.083  1.00 87.11  ? 45   LEU   D HA   1 
ATOM   20108 H  HB2  . LEU   D  4  45  ? 2.022   -53.058 -58.077  1.00 83.11  ? 45   LEU   D HB2  1 
ATOM   20109 H  HB3  . LEU   D  4  45  ? 3.332   -53.309 -57.213  1.00 83.11  ? 45   LEU   D HB3  1 
ATOM   20110 H  HG   . LEU   D  4  45  ? 3.334   -53.296 -60.032  1.00 88.19  ? 45   LEU   D HG   1 
ATOM   20111 H  HD11 . LEU   D  4  45  ? 4.317   -51.192 -59.946  1.00 86.58  ? 45   LEU   D HD11 1 
ATOM   20112 H  HD12 . LEU   D  4  45  ? 2.880   -51.147 -59.271  1.00 86.58  ? 45   LEU   D HD12 1 
ATOM   20113 H  HD13 . LEU   D  4  45  ? 4.183   -51.191 -58.363  1.00 86.58  ? 45   LEU   D HD13 1 
ATOM   20114 H  HD21 . LEU   D  4  45  ? 5.657   -53.253 -59.879  1.00 93.23  ? 45   LEU   D HD21 1 
ATOM   20115 H  HD22 . LEU   D  4  45  ? 5.555   -53.315 -58.295  1.00 93.23  ? 45   LEU   D HD22 1 
ATOM   20116 H  HD23 . LEU   D  4  45  ? 5.086   -54.555 -59.170  1.00 93.23  ? 45   LEU   D HD23 1 
ATOM   20117 N  N    . GLU   D  4  46  ? 2.611   -56.030 -55.884  1.00 74.15  ? 46   GLU   D N    1 
ATOM   20118 C  CA   . GLU   D  4  46  ? 2.080   -56.578 -54.645  1.00 75.78  ? 46   GLU   D CA   1 
ATOM   20119 C  C    . GLU   D  4  46  ? 2.874   -55.989 -53.490  1.00 71.94  ? 46   GLU   D C    1 
ATOM   20120 O  O    . GLU   D  4  46  ? 4.108   -56.024 -53.504  1.00 73.15  ? 46   GLU   D O    1 
ATOM   20121 C  CB   . GLU   D  4  46  ? 2.177   -58.107 -54.649  1.00 81.44  ? 46   GLU   D CB   1 
ATOM   20122 C  CG   . GLU   D  4  46  ? 1.156   -58.823 -53.785  1.00 89.24  ? 46   GLU   D CG   1 
ATOM   20123 C  CD   . GLU   D  4  46  ? 1.147   -60.319 -54.036  1.00 96.89  ? 46   GLU   D CD   1 
ATOM   20124 O  OE1  . GLU   D  4  46  ? 2.081   -60.814 -54.702  1.00 99.51  ? 46   GLU   D OE1  1 
ATOM   20125 O  OE2  . GLU   D  4  46  ? 0.206   -60.999 -53.576  1.00 104.92 ? 46   GLU   D OE2  1 
ATOM   20126 H  H    . GLU   D  4  46  ? 3.466   -56.108 -55.943  1.00 89.01  ? 46   GLU   D H    1 
ATOM   20127 H  HA   . GLU   D  4  46  ? 1.147   -56.337 -54.531  1.00 90.97  ? 46   GLU   D HA   1 
ATOM   20128 H  HB2  . GLU   D  4  46  ? 2.056   -58.418 -55.560  1.00 97.76  ? 46   GLU   D HB2  1 
ATOM   20129 H  HB3  . GLU   D  4  46  ? 3.057   -58.358 -54.327  1.00 97.76  ? 46   GLU   D HB3  1 
ATOM   20130 H  HG2  . GLU   D  4  46  ? 1.369   -58.674 -52.851  1.00 107.12 ? 46   GLU   D HG2  1 
ATOM   20131 H  HG3  . GLU   D  4  46  ? 0.272   -58.477 -53.984  1.00 107.12 ? 46   GLU   D HG3  1 
ATOM   20132 N  N    . TRP   D  4  47  ? 2.172   -55.447 -52.499  1.00 68.58  ? 47   TRP   D N    1 
ATOM   20133 C  CA   . TRP   D  4  47  ? 2.811   -54.753 -51.389  1.00 66.16  ? 47   TRP   D CA   1 
ATOM   20134 C  C    . TRP   D  4  47  ? 3.050   -55.717 -50.235  1.00 68.04  ? 47   TRP   D C    1 
ATOM   20135 O  O    . TRP   D  4  47  ? 2.119   -56.379 -49.764  1.00 72.34  ? 47   TRP   D O    1 
ATOM   20136 C  CB   . TRP   D  4  47  ? 1.946   -53.577 -50.938  1.00 65.54  ? 47   TRP   D CB   1 
ATOM   20137 C  CG   . TRP   D  4  47  ? 2.499   -52.811 -49.784  1.00 67.04  ? 47   TRP   D CG   1 
ATOM   20138 C  CD1  . TRP   D  4  47  ? 3.450   -51.834 -49.827  1.00 67.09  ? 47   TRP   D CD1  1 
ATOM   20139 C  CD2  . TRP   D  4  47  ? 2.119   -52.943 -48.411  1.00 66.98  ? 47   TRP   D CD2  1 
ATOM   20140 N  NE1  . TRP   D  4  47  ? 3.690   -51.353 -48.562  1.00 64.46  ? 47   TRP   D NE1  1 
ATOM   20141 C  CE2  . TRP   D  4  47  ? 2.885   -52.019 -47.675  1.00 64.24  ? 47   TRP   D CE2  1 
ATOM   20142 C  CE3  . TRP   D  4  47  ? 1.208   -53.757 -47.732  1.00 72.56  ? 47   TRP   D CE3  1 
ATOM   20143 C  CZ2  . TRP   D  4  47  ? 2.766   -51.883 -46.293  1.00 66.57  ? 47   TRP   D CZ2  1 
ATOM   20144 C  CZ3  . TRP   D  4  47  ? 1.094   -53.625 -46.360  1.00 76.67  ? 47   TRP   D CZ3  1 
ATOM   20145 C  CH2  . TRP   D  4  47  ? 1.867   -52.695 -45.655  1.00 72.48  ? 47   TRP   D CH2  1 
ATOM   20146 H  H    . TRP   D  4  47  ? 1.314   -55.469 -52.448  1.00 82.34  ? 47   TRP   D H    1 
ATOM   20147 H  HA   . TRP   D  4  47  ? 3.674   -54.410 -51.671  1.00 79.43  ? 47   TRP   D HA   1 
ATOM   20148 H  HB2  . TRP   D  4  47  ? 1.852   -52.960 -51.681  1.00 78.68  ? 47   TRP   D HB2  1 
ATOM   20149 H  HB3  . TRP   D  4  47  ? 1.076   -53.915 -50.676  1.00 78.68  ? 47   TRP   D HB3  1 
ATOM   20150 H  HD1  . TRP   D  4  47  ? 3.873   -51.536 -50.599  1.00 80.54  ? 47   TRP   D HD1  1 
ATOM   20151 H  HE1  . TRP   D  4  47  ? 4.253   -50.735 -48.361  1.00 77.38  ? 47   TRP   D HE1  1 
ATOM   20152 H  HE3  . TRP   D  4  47  ? 0.688   -54.374 -48.193  1.00 87.11  ? 47   TRP   D HE3  1 
ATOM   20153 H  HZ2  . TRP   D  4  47  ? 3.277   -51.265 -45.823  1.00 79.93  ? 47   TRP   D HZ2  1 
ATOM   20154 H  HZ3  . TRP   D  4  47  ? 0.494   -54.164 -45.898  1.00 92.04  ? 47   TRP   D HZ3  1 
ATOM   20155 H  HH2  . TRP   D  4  47  ? 1.768   -52.626 -44.733  1.00 87.01  ? 47   TRP   D HH2  1 
ATOM   20156 N  N    . ILE   D  4  48  ? 4.298   -55.786 -49.781  1.00 63.67  ? 48   ILE   D N    1 
ATOM   20157 C  CA   . ILE   D  4  48  ? 4.697   -56.735 -48.747  1.00 65.78  ? 48   ILE   D CA   1 
ATOM   20158 C  C    . ILE   D  4  48  ? 4.555   -56.130 -47.358  1.00 67.90  ? 48   ILE   D C    1 
ATOM   20159 O  O    . ILE   D  4  48  ? 3.953   -56.730 -46.463  1.00 72.77  ? 48   ILE   D O    1 
ATOM   20160 C  CB   . ILE   D  4  48  ? 6.144   -57.206 -49.006  1.00 63.87  ? 48   ILE   D CB   1 
ATOM   20161 C  CG1  . ILE   D  4  48  ? 6.265   -57.812 -50.407  1.00 64.80  ? 48   ILE   D CG1  1 
ATOM   20162 C  CG2  . ILE   D  4  48  ? 6.580   -58.217 -47.949  1.00 65.42  ? 48   ILE   D CG2  1 
ATOM   20163 C  CD1  . ILE   D  4  48  ? 7.692   -58.089 -50.828  1.00 63.43  ? 48   ILE   D CD1  1 
ATOM   20164 H  H    . ILE   D  4  48  ? 4.941   -55.287 -50.060  1.00 76.44  ? 48   ILE   D H    1 
ATOM   20165 H  HA   . ILE   D  4  48  ? 4.111   -57.507 -48.793  1.00 78.97  ? 48   ILE   D HA   1 
ATOM   20166 H  HB   . ILE   D  4  48  ? 6.729   -56.434 -48.952  1.00 76.68  ? 48   ILE   D HB   1 
ATOM   20167 H  HG12 . ILE   D  4  48  ? 5.782   -58.653 -50.426  1.00 77.80  ? 48   ILE   D HG12 1 
ATOM   20168 H  HG13 . ILE   D  4  48  ? 5.881   -57.195 -51.048  1.00 77.80  ? 48   ILE   D HG13 1 
ATOM   20169 H  HG21 . ILE   D  4  48  ? 7.499   -58.475 -48.119  1.00 78.54  ? 48   ILE   D HG21 1 
ATOM   20170 H  HG22 . ILE   D  4  48  ? 6.507   -57.808 -47.073  1.00 78.54  ? 48   ILE   D HG22 1 
ATOM   20171 H  HG23 . ILE   D  4  48  ? 6.003   -58.995 -48.000  1.00 78.54  ? 48   ILE   D HG23 1 
ATOM   20172 H  HD11 . ILE   D  4  48  ? 7.691   -58.450 -51.728  1.00 76.16  ? 48   ILE   D HD11 1 
ATOM   20173 H  HD12 . ILE   D  4  48  ? 8.194   -57.260 -50.804  1.00 76.16  ? 48   ILE   D HD12 1 
ATOM   20174 H  HD13 . ILE   D  4  48  ? 8.083   -58.731 -50.215  1.00 76.16  ? 48   ILE   D HD13 1 
ATOM   20175 N  N    . GLY   D  4  49  ? 5.110   -54.947 -47.157  1.00 65.85  ? 49   GLY   D N    1 
ATOM   20176 C  CA   . GLY   D  4  49  ? 5.088   -54.315 -45.855  1.00 66.55  ? 49   GLY   D CA   1 
ATOM   20177 C  C    . GLY   D  4  49  ? 6.108   -53.199 -45.793  1.00 63.20  ? 49   GLY   D C    1 
ATOM   20178 O  O    . GLY   D  4  49  ? 6.767   -52.868 -46.780  1.00 60.39  ? 49   GLY   D O    1 
ATOM   20179 H  H    . GLY   D  4  49  ? 5.509   -54.487 -47.764  1.00 79.06  ? 49   GLY   D H    1 
ATOM   20180 H  HA2  . GLY   D  4  49  ? 4.208   -53.946 -45.683  1.00 79.89  ? 49   GLY   D HA2  1 
ATOM   20181 H  HA3  . GLY   D  4  49  ? 5.297   -54.968 -45.168  1.00 79.89  ? 49   GLY   D HA3  1 
ATOM   20182 N  N    . TYR   D  4  50  ? 6.224   -52.622 -44.599  1.00 61.53  ? 50   TYR   D N    1 
ATOM   20183 C  CA   . TYR   D  4  50  ? 7.174   -51.546 -44.361  1.00 59.86  ? 50   TYR   D CA   1 
ATOM   20184 C  C    . TYR   D  4  50  ? 7.878   -51.782 -43.034  1.00 63.51  ? 50   TYR   D C    1 
ATOM   20185 O  O    . TYR   D  4  50  ? 7.428   -52.567 -42.195  1.00 66.17  ? 50   TYR   D O    1 
ATOM   20186 C  CB   . TYR   D  4  50  ? 6.491   -50.167 -44.359  1.00 58.73  ? 50   TYR   D CB   1 
ATOM   20187 C  CG   . TYR   D  4  50  ? 5.821   -49.796 -43.050  1.00 59.10  ? 50   TYR   D CG   1 
ATOM   20188 C  CD1  . TYR   D  4  50  ? 6.553   -49.247 -42.002  1.00 58.92  ? 50   TYR   D CD1  1 
ATOM   20189 C  CD2  . TYR   D  4  50  ? 4.457   -49.977 -42.869  1.00 62.21  ? 50   TYR   D CD2  1 
ATOM   20190 C  CE1  . TYR   D  4  50  ? 5.948   -48.907 -40.808  1.00 60.07  ? 50   TYR   D CE1  1 
ATOM   20191 C  CE2  . TYR   D  4  50  ? 3.842   -49.634 -41.679  1.00 65.16  ? 50   TYR   D CE2  1 
ATOM   20192 C  CZ   . TYR   D  4  50  ? 4.593   -49.099 -40.652  1.00 61.97  ? 50   TYR   D CZ   1 
ATOM   20193 O  OH   . TYR   D  4  50  ? 3.984   -48.758 -39.467  1.00 61.00  ? 50   TYR   D OH   1 
ATOM   20194 H  H    . TYR   D  4  50  ? 5.760   -52.840 -43.909  1.00 73.88  ? 50   TYR   D H    1 
ATOM   20195 H  HA   . TYR   D  4  50  ? 7.841   -51.552 -45.065  1.00 71.87  ? 50   TYR   D HA   1 
ATOM   20196 H  HB2  . TYR   D  4  50  ? 7.161   -49.491 -44.547  1.00 70.51  ? 50   TYR   D HB2  1 
ATOM   20197 H  HB3  . TYR   D  4  50  ? 5.809   -50.160 -45.049  1.00 70.51  ? 50   TYR   D HB3  1 
ATOM   20198 H  HD1  . TYR   D  4  50  ? 7.466   -49.107 -42.107  1.00 70.74  ? 50   TYR   D HD1  1 
ATOM   20199 H  HD2  . TYR   D  4  50  ? 3.948   -50.336 -43.560  1.00 74.69  ? 50   TYR   D HD2  1 
ATOM   20200 H  HE1  . TYR   D  4  50  ? 6.453   -48.550 -40.113  1.00 72.12  ? 50   TYR   D HE1  1 
ATOM   20201 H  HE2  . TYR   D  4  50  ? 2.928   -49.763 -41.571  1.00 78.23  ? 50   TYR   D HE2  1 
ATOM   20202 H  HH   . TYR   D  4  50  ? 3.800   -47.939 -39.464  1.00 73.24  ? 50   TYR   D HH   1 
ATOM   20203 N  N    . ILE   D  4  51  ? 8.993   -51.078 -42.853  1.00 62.83  ? 51   ILE   D N    1 
ATOM   20204 C  CA   . ILE   D  4  51  ? 9.770   -51.125 -41.623  1.00 61.48  ? 51   ILE   D CA   1 
ATOM   20205 C  C    . ILE   D  4  51  ? 10.146  -49.704 -41.231  1.00 62.29  ? 51   ILE   D C    1 
ATOM   20206 O  O    . ILE   D  4  51  ? 10.541  -48.898 -42.081  1.00 59.95  ? 51   ILE   D O    1 
ATOM   20207 C  CB   . ILE   D  4  51  ? 11.038  -51.990 -41.776  1.00 60.08  ? 51   ILE   D CB   1 
ATOM   20208 C  CG1  . ILE   D  4  51  ? 11.829  -52.007 -40.465  1.00 59.87  ? 51   ILE   D CG1  1 
ATOM   20209 C  CG2  . ILE   D  4  51  ? 11.905  -51.460 -42.911  1.00 58.93  ? 51   ILE   D CG2  1 
ATOM   20210 C  CD1  . ILE   D  4  51  ? 12.961  -53.013 -40.439  1.00 57.63  ? 51   ILE   D CD1  1 
ATOM   20211 H  H    . ILE   D  4  51  ? 9.326   -50.553 -43.447  1.00 75.43  ? 51   ILE   D H    1 
ATOM   20212 H  HA   . ILE   D  4  51  ? 9.223   -51.506 -40.919  1.00 73.81  ? 51   ILE   D HA   1 
ATOM   20213 H  HB   . ILE   D  4  51  ? 10.769  -52.897 -41.989  1.00 72.13  ? 51   ILE   D HB   1 
ATOM   20214 H  HG12 . ILE   D  4  51  ? 12.213  -51.127 -40.322  1.00 71.89  ? 51   ILE   D HG12 1 
ATOM   20215 H  HG13 . ILE   D  4  51  ? 11.223  -52.226 -39.740  1.00 71.89  ? 51   ILE   D HG13 1 
ATOM   20216 H  HG21 . ILE   D  4  51  ? 12.681  -52.034 -43.010  1.00 70.75  ? 51   ILE   D HG21 1 
ATOM   20217 H  HG22 . ILE   D  4  51  ? 11.387  -51.460 -43.731  1.00 70.75  ? 51   ILE   D HG22 1 
ATOM   20218 H  HG23 . ILE   D  4  51  ? 12.187  -50.556 -42.698  1.00 70.75  ? 51   ILE   D HG23 1 
ATOM   20219 H  HD11 . ILE   D  4  51  ? 13.393  -52.979 -39.571  1.00 69.19  ? 51   ILE   D HD11 1 
ATOM   20220 H  HD12 . ILE   D  4  51  ? 12.599  -53.899 -40.594  1.00 69.19  ? 51   ILE   D HD12 1 
ATOM   20221 H  HD13 . ILE   D  4  51  ? 13.598  -52.789 -41.135  1.00 69.19  ? 51   ILE   D HD13 1 
ATOM   20222 N  N    . ASN   D  4  52  ? 10.016  -49.397 -39.944  1.00 65.72  ? 52   ASN   D N    1 
ATOM   20223 C  CA   . ASN   D  4  52  ? 10.558  -48.162 -39.392  1.00 65.88  ? 52   ASN   D CA   1 
ATOM   20224 C  C    . ASN   D  4  52  ? 12.035  -48.400 -39.101  1.00 63.19  ? 52   ASN   D C    1 
ATOM   20225 O  O    . ASN   D  4  52  ? 12.366  -49.080 -38.121  1.00 62.68  ? 52   ASN   D O    1 
ATOM   20226 C  CB   . ASN   D  4  52  ? 9.802   -47.751 -38.129  1.00 70.64  ? 52   ASN   D CB   1 
ATOM   20227 C  CG   . ASN   D  4  52  ? 10.266  -46.414 -37.578  1.00 74.91  ? 52   ASN   D CG   1 
ATOM   20228 O  OD1  . ASN   D  4  52  ? 11.437  -46.052 -37.688  1.00 72.33  ? 52   ASN   D OD1  1 
ATOM   20229 N  ND2  . ASN   D  4  52  ? 9.342   -45.671 -36.979  1.00 82.47  ? 52   ASN   D ND2  1 
ATOM   20230 H  H    . ASN   D  4  52  ? 9.615   -49.892 -39.367  1.00 78.90  ? 52   ASN   D H    1 
ATOM   20231 H  HA   . ASN   D  4  52  ? 10.465  -47.430 -40.021  1.00 79.09  ? 52   ASN   D HA   1 
ATOM   20232 H  HB2  . ASN   D  4  52  ? 8.857   -47.680 -38.334  1.00 84.81  ? 52   ASN   D HB2  1 
ATOM   20233 H  HB3  . ASN   D  4  52  ? 9.943   -48.423 -37.443  1.00 84.81  ? 52   ASN   D HB3  1 
ATOM   20234 H  HD21 . ASN   D  4  52  ? 9.553   -44.905 -36.650  1.00 99.00  ? 52   ASN   D HD21 1 
ATOM   20235 H  HD22 . ASN   D  4  52  ? 8.533   -45.956 -36.921  1.00 99.00  ? 52   ASN   D HD22 1 
ATOM   20236 N  N    . PRO   D  4  53  ? 12.952  -47.862 -39.914  1.00 64.03  ? 53   PRO   D N    1 
ATOM   20237 C  CA   . PRO   D  4  53  ? 14.359  -48.276 -39.781  1.00 67.95  ? 53   PRO   D CA   1 
ATOM   20238 C  C    . PRO   D  4  53  ? 14.931  -48.049 -38.396  1.00 73.11  ? 53   PRO   D C    1 
ATOM   20239 O  O    . PRO   D  4  53  ? 15.671  -48.900 -37.887  1.00 77.09  ? 53   PRO   D O    1 
ATOM   20240 C  CB   . PRO   D  4  53  ? 15.082  -47.417 -40.831  1.00 64.37  ? 53   PRO   D CB   1 
ATOM   20241 C  CG   . PRO   D  4  53  ? 14.021  -46.914 -41.743  1.00 63.15  ? 53   PRO   D CG   1 
ATOM   20242 C  CD   . PRO   D  4  53  ? 12.784  -46.798 -40.918  1.00 61.15  ? 53   PRO   D CD   1 
ATOM   20243 H  HA   . PRO   D  4  53  ? 14.440  -49.214 -40.015  1.00 81.57  ? 53   PRO   D HA   1 
ATOM   20244 H  HB2  . PRO   D  4  53  ? 15.538  -46.681 -40.394  1.00 77.28  ? 53   PRO   D HB2  1 
ATOM   20245 H  HB3  . PRO   D  4  53  ? 15.722  -47.962 -41.315  1.00 77.28  ? 53   PRO   D HB3  1 
ATOM   20246 H  HG2  . PRO   D  4  53  ? 14.279  -46.049 -42.098  1.00 75.82  ? 53   PRO   D HG2  1 
ATOM   20247 H  HG3  . PRO   D  4  53  ? 13.890  -47.544 -42.469  1.00 75.82  ? 53   PRO   D HG3  1 
ATOM   20248 H  HD2  . PRO   D  4  53  ? 12.732  -45.927 -40.494  1.00 73.42  ? 53   PRO   D HD2  1 
ATOM   20249 H  HD3  . PRO   D  4  53  ? 11.993  -46.952 -41.457  1.00 73.42  ? 53   PRO   D HD3  1 
ATOM   20250 N  N    . ASN   D  4  54  ? 14.607  -46.920 -37.767  1.00 72.42  ? 54   ASN   D N    1 
ATOM   20251 C  CA   . ASN   D  4  54  ? 15.225  -46.582 -36.493  1.00 77.58  ? 54   ASN   D CA   1 
ATOM   20252 C  C    . ASN   D  4  54  ? 14.704  -47.438 -35.347  1.00 76.23  ? 54   ASN   D C    1 
ATOM   20253 O  O    . ASN   D  4  54  ? 15.403  -47.585 -34.338  1.00 78.56  ? 54   ASN   D O    1 
ATOM   20254 C  CB   . ASN   D  4  54  ? 14.994  -45.102 -36.182  1.00 83.44  ? 54   ASN   D CB   1 
ATOM   20255 C  CG   . ASN   D  4  54  ? 16.130  -44.492 -35.386  1.00 84.66  ? 54   ASN   D CG   1 
ATOM   20256 O  OD1  . ASN   D  4  54  ? 17.294  -44.850 -35.566  1.00 84.18  ? 54   ASN   D OD1  1 
ATOM   20257 N  ND2  . ASN   D  4  54  ? 15.797  -43.565 -34.497  1.00 95.31  ? 54   ASN   D ND2  1 
ATOM   20258 H  H    . ASN   D  4  54  ? 14.039  -46.342 -38.055  1.00 86.94  ? 54   ASN   D H    1 
ATOM   20259 H  HA   . ASN   D  4  54  ? 16.180  -46.732 -36.563  1.00 93.14  ? 54   ASN   D HA   1 
ATOM   20260 H  HB2  . ASN   D  4  54  ? 14.913  -44.612 -37.015  1.00 100.16 ? 54   ASN   D HB2  1 
ATOM   20261 H  HB3  . ASN   D  4  54  ? 14.180  -45.011 -35.662  1.00 100.16 ? 54   ASN   D HB3  1 
ATOM   20262 H  HD21 . ASN   D  4  54  ? 16.405  -43.188 -34.020  1.00 114.41 ? 54   ASN   D HD21 1 
ATOM   20263 H  HD22 . ASN   D  4  54  ? 14.972  -43.342 -34.398  1.00 114.41 ? 54   ASN   D HD22 1 
ATOM   20264 N  N    . SER   D  4  55  ? 13.506  -48.012 -35.476  1.00 71.74  ? 55   SER   D N    1 
ATOM   20265 C  CA   . SER   D  4  55  ? 12.892  -48.767 -34.393  1.00 65.60  ? 55   SER   D CA   1 
ATOM   20266 C  C    . SER   D  4  55  ? 12.719  -50.248 -34.697  1.00 66.56  ? 55   SER   D C    1 
ATOM   20267 O  O    . SER   D  4  55  ? 12.434  -51.019 -33.774  1.00 69.30  ? 55   SER   D O    1 
ATOM   20268 C  CB   . SER   D  4  55  ? 11.519  -48.173 -34.045  1.00 62.34  ? 55   SER   D CB   1 
ATOM   20269 O  OG   . SER   D  4  55  ? 10.571  -48.455 -35.060  1.00 63.54  ? 55   SER   D OG   1 
ATOM   20270 H  H    . SER   D  4  55  ? 13.028  -47.975 -36.190  1.00 86.13  ? 55   SER   D H    1 
ATOM   20271 H  HA   . SER   D  4  55  ? 13.464  -48.692 -33.613  1.00 78.76  ? 55   SER   D HA   1 
ATOM   20272 H  HB2  . SER   D  4  55  ? 11.211  -48.559 -33.211  1.00 74.85  ? 55   SER   D HB2  1 
ATOM   20273 H  HB3  . SER   D  4  55  ? 11.606  -47.211 -33.953  1.00 74.85  ? 55   SER   D HB3  1 
ATOM   20274 H  HG   . SER   D  4  55  ? 9.796   -48.286 -34.784  1.00 76.29  ? 55   SER   D HG   1 
ATOM   20275 N  N    . GLY   D  4  56  ? 12.875  -50.669 -35.951  1.00 65.70  ? 56   GLY   D N    1 
ATOM   20276 C  CA   . GLY   D  4  56  ? 12.665  -52.052 -36.319  1.00 66.85  ? 56   GLY   D CA   1 
ATOM   20277 C  C    . GLY   D  4  56  ? 11.219  -52.489 -36.378  1.00 69.71  ? 56   GLY   D C    1 
ATOM   20278 O  O    . GLY   D  4  56  ? 10.953  -53.623 -36.795  1.00 70.45  ? 56   GLY   D O    1 
ATOM   20279 H  H    . GLY   D  4  56  ? 13.105  -50.162 -36.607  1.00 78.88  ? 56   GLY   D H    1 
ATOM   20280 H  HA2  . GLY   D  4  56  ? 13.053  -52.201 -37.196  1.00 80.26  ? 56   GLY   D HA2  1 
ATOM   20281 H  HA3  . GLY   D  4  56  ? 13.117  -52.616 -35.673  1.00 80.26  ? 56   GLY   D HA3  1 
ATOM   20282 N  N    . TYR   D  4  57  ? 10.276  -51.643 -35.969  1.00 72.98  ? 57   TYR   D N    1 
ATOM   20283 C  CA   . TYR   D  4  57  ? 8.866   -51.986 -36.087  1.00 78.29  ? 57   TYR   D CA   1 
ATOM   20284 C  C    . TYR   D  4  57  ? 8.509   -52.235 -37.546  1.00 73.47  ? 57   TYR   D C    1 
ATOM   20285 O  O    . TYR   D  4  57  ? 8.975   -51.530 -38.445  1.00 66.61  ? 57   TYR   D O    1 
ATOM   20286 C  CB   . TYR   D  4  57  ? 7.998   -50.865 -35.516  1.00 82.81  ? 57   TYR   D CB   1 
ATOM   20287 C  CG   . TYR   D  4  57  ? 6.515   -51.092 -35.697  1.00 84.53  ? 57   TYR   D CG   1 
ATOM   20288 C  CD1  . TYR   D  4  57  ? 5.821   -51.963 -34.869  1.00 87.42  ? 57   TYR   D CD1  1 
ATOM   20289 C  CD2  . TYR   D  4  57  ? 5.808   -50.436 -36.697  1.00 84.21  ? 57   TYR   D CD2  1 
ATOM   20290 C  CE1  . TYR   D  4  57  ? 4.466   -52.176 -35.030  1.00 90.10  ? 57   TYR   D CE1  1 
ATOM   20291 C  CE2  . TYR   D  4  57  ? 4.452   -50.642 -36.865  1.00 87.27  ? 57   TYR   D CE2  1 
ATOM   20292 C  CZ   . TYR   D  4  57  ? 3.786   -51.513 -36.029  1.00 92.60  ? 57   TYR   D CZ   1 
ATOM   20293 O  OH   . TYR   D  4  57  ? 2.436   -51.723 -36.191  1.00 99.73  ? 57   TYR   D OH   1 
ATOM   20294 H  H    . TYR   D  4  57  ? 10.427  -50.871 -35.622  1.00 87.61  ? 57   TYR   D H    1 
ATOM   20295 H  HA   . TYR   D  4  57  ? 8.684   -52.793 -35.581  1.00 93.98  ? 57   TYR   D HA   1 
ATOM   20296 H  HB2  . TYR   D  4  57  ? 8.172   -50.789 -34.565  1.00 99.41  ? 57   TYR   D HB2  1 
ATOM   20297 H  HB3  . TYR   D  4  57  ? 8.228   -50.035 -35.962  1.00 99.41  ? 57   TYR   D HB3  1 
ATOM   20298 H  HD1  . TYR   D  4  57  ? 6.277   -52.411 -34.193  1.00 104.95 ? 57   TYR   D HD1  1 
ATOM   20299 H  HD2  . TYR   D  4  57  ? 6.255   -49.848 -37.262  1.00 101.09 ? 57   TYR   D HD2  1 
ATOM   20300 H  HE1  . TYR   D  4  57  ? 4.015   -52.763 -34.467  1.00 108.15 ? 57   TYR   D HE1  1 
ATOM   20301 H  HE2  . TYR   D  4  57  ? 3.991   -50.195 -37.538  1.00 104.76 ? 57   TYR   D HE2  1 
ATOM   20302 H  HH   . TYR   D  4  57  ? 2.162   -51.315 -36.873  1.00 119.71 ? 57   TYR   D HH   1 
ATOM   20303 N  N    . THR   D  4  58  ? 7.678   -53.250 -37.781  1.00 75.36  ? 58   THR   D N    1 
ATOM   20304 C  CA   . THR   D  4  58  ? 7.258   -53.597 -39.129  1.00 71.26  ? 58   THR   D CA   1 
ATOM   20305 C  C    . THR   D  4  58  ? 5.763   -53.881 -39.149  1.00 73.19  ? 58   THR   D C    1 
ATOM   20306 O  O    . THR   D  4  58  ? 5.154   -54.220 -38.131  1.00 76.74  ? 58   THR   D O    1 
ATOM   20307 C  CB   . THR   D  4  58  ? 8.006   -54.826 -39.672  1.00 68.85  ? 58   THR   D CB   1 
ATOM   20308 O  OG1  . THR   D  4  58  ? 7.652   -55.984 -38.904  1.00 74.11  ? 58   THR   D OG1  1 
ATOM   20309 C  CG2  . THR   D  4  58  ? 9.510   -54.621 -39.610  1.00 64.50  ? 58   THR   D CG2  1 
ATOM   20310 H  H    . THR   D  4  58  ? 7.345   -53.754 -37.169  1.00 90.47  ? 58   THR   D H    1 
ATOM   20311 H  HA   . THR   D  4  58  ? 7.439   -52.837 -39.704  1.00 85.55  ? 58   THR   D HA   1 
ATOM   20312 H  HB   . THR   D  4  58  ? 7.759   -54.963 -40.600  1.00 82.66  ? 58   THR   D HB   1 
ATOM   20313 H  HG1  . THR   D  4  58  ? 8.031   -56.664 -39.218  1.00 88.97  ? 58   THR   D HG1  1 
ATOM   20314 H  HG21 . THR   D  4  58  ? 9.966   -55.399 -39.968  1.00 77.44  ? 58   THR   D HG21 1 
ATOM   20315 H  HG22 . THR   D  4  58  ? 9.760   -53.842 -40.131  1.00 77.44  ? 58   THR   D HG22 1 
ATOM   20316 H  HG23 . THR   D  4  58  ? 9.789   -54.488 -38.691  1.00 77.44  ? 58   THR   D HG23 1 
ATOM   20317 N  N    . GLU   D  4  59  ? 5.182   -53.727 -40.336  1.00 70.64  ? 59   GLU   D N    1 
ATOM   20318 C  CA   . GLU   D  4  59  ? 3.841   -54.200 -40.646  1.00 75.39  ? 59   GLU   D CA   1 
ATOM   20319 C  C    . GLU   D  4  59  ? 3.901   -54.911 -41.990  1.00 73.17  ? 59   GLU   D C    1 
ATOM   20320 O  O    . GLU   D  4  59  ? 4.603   -54.462 -42.902  1.00 69.30  ? 59   GLU   D O    1 
ATOM   20321 C  CB   . GLU   D  4  59  ? 2.817   -53.058 -40.704  1.00 81.07  ? 59   GLU   D CB   1 
ATOM   20322 C  CG   . GLU   D  4  59  ? 2.464   -52.446 -39.355  1.00 87.49  ? 59   GLU   D CG   1 
ATOM   20323 C  CD   . GLU   D  4  59  ? 1.266   -51.518 -39.433  1.00 93.93  ? 59   GLU   D CD   1 
ATOM   20324 O  OE1  . GLU   D  4  59  ? 0.284   -51.869 -40.120  1.00 96.25  ? 59   GLU   D OE1  1 
ATOM   20325 O  OE2  . GLU   D  4  59  ? 1.310   -50.435 -38.813  1.00 94.98  ? 59   GLU   D OE2  1 
ATOM   20326 H  H    . GLU   D  4  59  ? 5.561   -53.336 -41.001  1.00 84.80  ? 59   GLU   D H    1 
ATOM   20327 H  HA   . GLU   D  4  59  ? 3.539   -54.816 -39.960  1.00 90.51  ? 59   GLU   D HA   1 
ATOM   20328 H  HB2  . GLU   D  4  59  ? 3.177   -52.349 -41.260  1.00 97.32  ? 59   GLU   D HB2  1 
ATOM   20329 H  HB3  . GLU   D  4  59  ? 1.996   -53.399 -41.092  1.00 97.32  ? 59   GLU   D HB3  1 
ATOM   20330 H  HG2  . GLU   D  4  59  ? 2.253   -53.158 -38.730  1.00 105.03 ? 59   GLU   D HG2  1 
ATOM   20331 H  HG3  . GLU   D  4  59  ? 3.222   -51.934 -39.031  1.00 105.03 ? 59   GLU   D HG3  1 
ATOM   20332 N  N    . CYS   D  4  60  ? 3.175   -56.019 -42.108  1.00 79.40  ? 60   CYS   D N    1 
ATOM   20333 C  CA   . CYS   D  4  60  ? 3.177   -56.819 -43.323  1.00 77.97  ? 60   CYS   D CA   1 
ATOM   20334 C  C    . CYS   D  4  60  ? 1.755   -57.025 -43.819  1.00 74.38  ? 60   CYS   D C    1 
ATOM   20335 O  O    . CYS   D  4  60  ? 0.803   -57.055 -43.034  1.00 73.87  ? 60   CYS   D O    1 
ATOM   20336 C  CB   . CYS   D  4  60  ? 3.826   -58.198 -43.102  1.00 86.52  ? 60   CYS   D CB   1 
ATOM   20337 S  SG   . CYS   D  4  60  ? 5.618   -58.183 -42.865  1.00 88.42  ? 60   CYS   D SG   1 
ATOM   20338 H  H    . CYS   D  4  60  ? 2.668   -56.331 -41.488  1.00 95.32  ? 60   CYS   D H    1 
ATOM   20339 H  HA   . CYS   D  4  60  ? 3.678   -56.342 -44.003  1.00 93.61  ? 60   CYS   D HA   1 
ATOM   20340 H  HB2  . CYS   D  4  60  ? 3.433   -58.597 -42.310  1.00 103.86 ? 60   CYS   D HB2  1 
ATOM   20341 H  HB3  . CYS   D  4  60  ? 3.642   -58.750 -43.878  1.00 103.86 ? 60   CYS   D HB3  1 
ATOM   20342 H  HG   . CYS   D  4  60  ? 6.004   -59.311 -42.730  1.00 106.14 ? 60   CYS   D HG   1 
ATOM   20343 N  N    . ASN   D  4  61  ? 1.622   -57.156 -45.135  1.00 71.95  ? 61   ASN   D N    1 
ATOM   20344 C  CA   . ASN   D  4  61  ? 0.416   -57.744 -45.697  1.00 79.02  ? 61   ASN   D CA   1 
ATOM   20345 C  C    . ASN   D  4  61  ? 0.213   -59.121 -45.078  1.00 88.82  ? 61   ASN   D C    1 
ATOM   20346 O  O    . ASN   D  4  61  ? 1.174   -59.861 -44.851  1.00 67.87  ? 61   ASN   D O    1 
ATOM   20347 C  CB   . ASN   D  4  61  ? 0.539   -57.851 -47.218  1.00 76.56  ? 61   ASN   D CB   1 
ATOM   20348 C  CG   . ASN   D  4  61  ? -0.759  -58.268 -47.887  1.00 78.68  ? 61   ASN   D CG   1 
ATOM   20349 O  OD1  . ASN   D  4  61  ? -1.602  -58.930 -47.282  1.00 84.61  ? 61   ASN   D OD1  1 
ATOM   20350 N  ND2  . ASN   D  4  61  ? -0.921  -57.885 -49.149  1.00 75.72  ? 61   ASN   D ND2  1 
ATOM   20351 H  H    . ASN   D  4  61  ? 2.208   -56.914 -45.716  1.00 86.37  ? 61   ASN   D H    1 
ATOM   20352 H  HA   . ASN   D  4  61  ? -0.357  -57.190 -45.508  1.00 94.86  ? 61   ASN   D HA   1 
ATOM   20353 H  HB2  . ASN   D  4  61  ? 0.795   -56.986 -47.575  1.00 91.91  ? 61   ASN   D HB2  1 
ATOM   20354 H  HB3  . ASN   D  4  61  ? 1.214   -58.513 -47.435  1.00 91.91  ? 61   ASN   D HB3  1 
ATOM   20355 H  HD21 . ASN   D  4  61  ? -1.638  -58.095 -49.574  1.00 90.90  ? 61   ASN   D HD21 1 
ATOM   20356 H  HD22 . ASN   D  4  61  ? -0.308  -57.426 -49.541  1.00 90.90  ? 61   ASN   D HD22 1 
ATOM   20357 N  N    . GLU   D  4  62  ? -1.044  -59.461 -44.783  1.00 98.10  ? 62   GLU   D N    1 
ATOM   20358 C  CA   . GLU   D  4  62  ? -1.324  -60.770 -44.202  1.00 104.95 ? 62   GLU   D CA   1 
ATOM   20359 C  C    . GLU   D  4  62  ? -0.676  -61.885 -45.011  1.00 102.54 ? 62   GLU   D C    1 
ATOM   20360 O  O    . GLU   D  4  62  ? -0.231  -62.889 -44.444  1.00 104.45 ? 62   GLU   D O    1 
ATOM   20361 C  CB   . GLU   D  4  62  ? -2.833  -60.998 -44.110  1.00 114.63 ? 62   GLU   D CB   1 
ATOM   20362 C  CG   . GLU   D  4  62  ? -3.533  -60.122 -43.082  1.00 122.45 ? 62   GLU   D CG   1 
ATOM   20363 C  CD   . GLU   D  4  62  ? -5.028  -60.368 -43.024  1.00 133.55 ? 62   GLU   D CD   1 
ATOM   20364 O  OE1  . GLU   D  4  62  ? -5.502  -61.315 -43.687  1.00 140.80 ? 62   GLU   D OE1  1 
ATOM   20365 O  OE2  . GLU   D  4  62  ? -5.728  -59.614 -42.316  1.00 139.44 ? 62   GLU   D OE2  1 
ATOM   20366 H  H    . GLU   D  4  62  ? -1.734  -58.963 -44.907  1.00 117.76 ? 62   GLU   D H    1 
ATOM   20367 H  HA   . GLU   D  4  62  ? -0.963  -60.796 -43.302  1.00 125.98 ? 62   GLU   D HA   1 
ATOM   20368 H  HB2  . GLU   D  4  62  ? -3.229  -60.810 -44.975  1.00 137.59 ? 62   GLU   D HB2  1 
ATOM   20369 H  HB3  . GLU   D  4  62  ? -2.993  -61.923 -43.865  1.00 137.59 ? 62   GLU   D HB3  1 
ATOM   20370 H  HG2  . GLU   D  4  62  ? -3.163  -60.307 -42.204  1.00 146.97 ? 62   GLU   D HG2  1 
ATOM   20371 H  HG3  . GLU   D  4  62  ? -3.390  -59.190 -43.311  1.00 146.97 ? 62   GLU   D HG3  1 
ATOM   20372 N  N    . ILE   D  4  63  ? -0.600  -61.716 -46.334  1.00 99.59  ? 63   ILE   D N    1 
ATOM   20373 C  CA   . ILE   D  4  63  ? -0.034  -62.745 -47.205  1.00 99.83  ? 63   ILE   D CA   1 
ATOM   20374 C  C    . ILE   D  4  63  ? 1.370   -63.120 -46.746  1.00 97.53  ? 63   ILE   D C    1 
ATOM   20375 O  O    . ILE   D  4  63  ? 1.672   -64.292 -46.491  1.00 102.11 ? 63   ILE   D O    1 
ATOM   20376 C  CB   . ILE   D  4  63  ? -0.029  -62.263 -48.668  1.00 97.46  ? 63   ILE   D CB   1 
ATOM   20377 C  CG1  . ILE   D  4  63  ? -1.461  -62.016 -49.154  1.00 102.44 ? 63   ILE   D CG1  1 
ATOM   20378 C  CG2  . ILE   D  4  63  ? 0.681   -63.274 -49.566  1.00 99.28  ? 63   ILE   D CG2  1 
ATOM   20379 C  CD1  . ILE   D  4  63  ? -1.546  -61.291 -50.485  1.00 101.16 ? 63   ILE   D CD1  1 
ATOM   20380 H  H    . ILE   D  4  63  ? -0.869  -61.013 -46.751  1.00 119.54 ? 63   ILE   D H    1 
ATOM   20381 H  HA   . ILE   D  4  63  ? -0.589  -63.538 -47.145  1.00 119.84 ? 63   ILE   D HA   1 
ATOM   20382 H  HB   . ILE   D  4  63  ? 0.457   -61.425 -48.710  1.00 116.99 ? 63   ILE   D HB   1 
ATOM   20383 H  HG12 . ILE   D  4  63  ? -1.907  -62.872 -49.255  1.00 122.97 ? 63   ILE   D HG12 1 
ATOM   20384 H  HG13 . ILE   D  4  63  ? -1.925  -61.477 -48.494  1.00 122.97 ? 63   ILE   D HG13 1 
ATOM   20385 H  HG21 . ILE   D  4  63  ? 0.642   -62.963 -50.484  1.00 119.17 ? 63   ILE   D HG21 1 
ATOM   20386 H  HG22 . ILE   D  4  63  ? 1.606   -63.353 -49.282  1.00 119.17 ? 63   ILE   D HG22 1 
ATOM   20387 H  HG23 . ILE   D  4  63  ? 0.237   -64.132 -49.488  1.00 119.17 ? 63   ILE   D HG23 1 
ATOM   20388 H  HD11 . ILE   D  4  63  ? -2.479  -61.158 -50.714  1.00 121.42 ? 63   ILE   D HD11 1 
ATOM   20389 H  HD12 . ILE   D  4  63  ? -1.099  -60.433 -50.406  1.00 121.42 ? 63   ILE   D HD12 1 
ATOM   20390 H  HD13 . ILE   D  4  63  ? -1.112  -61.829 -51.166  1.00 121.42 ? 63   ILE   D HD13 1 
ATOM   20391 N  N    . PHE   D  4  64  ? 2.251   -62.125 -46.639  1.00 92.57  ? 64   PHE   D N    1 
ATOM   20392 C  CA   . PHE   D  4  64  ? 3.671   -62.356 -46.421  1.00 91.31  ? 64   PHE   D CA   1 
ATOM   20393 C  C    . PHE   D  4  64  ? 4.056   -62.380 -44.944  1.00 92.45  ? 64   PHE   D C    1 
ATOM   20394 O  O    . PHE   D  4  64  ? 5.245   -62.261 -44.626  1.00 90.14  ? 64   PHE   D O    1 
ATOM   20395 C  CB   . PHE   D  4  64  ? 4.494   -61.283 -47.140  1.00 84.74  ? 64   PHE   D CB   1 
ATOM   20396 C  CG   . PHE   D  4  64  ? 4.135   -61.105 -48.588  1.00 81.15  ? 64   PHE   D CG   1 
ATOM   20397 C  CD1  . PHE   D  4  64  ? 4.777   -61.840 -49.571  1.00 80.00  ? 64   PHE   D CD1  1 
ATOM   20398 C  CD2  . PHE   D  4  64  ? 3.162   -60.194 -48.968  1.00 80.17  ? 64   PHE   D CD2  1 
ATOM   20399 C  CE1  . PHE   D  4  64  ? 4.451   -61.674 -50.904  1.00 78.80  ? 64   PHE   D CE1  1 
ATOM   20400 C  CE2  . PHE   D  4  64  ? 2.833   -60.024 -50.299  1.00 78.72  ? 64   PHE   D CE2  1 
ATOM   20401 C  CZ   . PHE   D  4  64  ? 3.478   -60.764 -51.268  1.00 78.29  ? 64   PHE   D CZ   1 
ATOM   20402 H  H    . PHE   D  4  64  ? 2.042   -61.292 -46.692  1.00 111.12 ? 64   PHE   D H    1 
ATOM   20403 H  HA   . PHE   D  4  64  ? 3.889   -63.222 -46.799  1.00 109.61 ? 64   PHE   D HA   1 
ATOM   20404 H  HB2  . PHE   D  4  64  ? 4.353   -60.433 -46.695  1.00 101.73 ? 64   PHE   D HB2  1 
ATOM   20405 H  HB3  . PHE   D  4  64  ? 5.431   -61.529 -47.097  1.00 101.73 ? 64   PHE   D HB3  1 
ATOM   20406 H  HD1  . PHE   D  4  64  ? 5.434   -62.452 -49.331  1.00 96.03  ? 64   PHE   D HD1  1 
ATOM   20407 H  HD2  . PHE   D  4  64  ? 2.726   -59.691 -48.318  1.00 96.24  ? 64   PHE   D HD2  1 
ATOM   20408 H  HE1  . PHE   D  4  64  ? 4.887   -62.174 -51.555  1.00 94.59  ? 64   PHE   D HE1  1 
ATOM   20409 H  HE2  . PHE   D  4  64  ? 2.176   -59.411 -50.541  1.00 94.50  ? 64   PHE   D HE2  1 
ATOM   20410 H  HZ   . PHE   D  4  64  ? 3.258   -60.651 -52.164  1.00 93.99  ? 64   PHE   D HZ   1 
ATOM   20411 N  N    . ARG   D  4  65  ? 3.088   -62.536 -44.037  1.00 96.95  ? 65   ARG   D N    1 
ATOM   20412 C  CA   . ARG   D  4  65  ? 3.398   -62.444 -42.613  1.00 103.20 ? 65   ARG   D CA   1 
ATOM   20413 C  C    . ARG   D  4  65  ? 4.455   -63.467 -42.213  1.00 108.82 ? 65   ARG   D C    1 
ATOM   20414 O  O    . ARG   D  4  65  ? 5.410   -63.143 -41.497  1.00 109.01 ? 65   ARG   D O    1 
ATOM   20415 C  CB   . ARG   D  4  65  ? 2.124   -62.617 -41.782  1.00 108.86 ? 65   ARG   D CB   1 
ATOM   20416 C  CG   . ARG   D  4  65  ? 1.498   -64.008 -41.821  1.00 124.31 ? 65   ARG   D CG   1 
ATOM   20417 C  CD   . ARG   D  4  65  ? 0.146   -64.007 -41.115  1.00 133.17 ? 65   ARG   D CD   1 
ATOM   20418 N  NE   . ARG   D  4  65  ? -0.357  -65.351 -40.833  1.00 141.28 ? 65   ARG   D NE   1 
ATOM   20419 C  CZ   . ARG   D  4  65  ? -1.181  -66.036 -41.623  1.00 147.55 ? 65   ARG   D CZ   1 
ATOM   20420 N  NH1  . ARG   D  4  65  ? -1.608  -65.520 -42.768  1.00 145.40 ? 65   ARG   D NH1  1 
ATOM   20421 N  NH2  . ARG   D  4  65  ? -1.580  -67.249 -41.264  1.00 155.09 ? 65   ARG   D NH2  1 
ATOM   20422 H  H    . ARG   D  4  65  ? 2.262   -62.692 -44.218  1.00 116.38 ? 65   ARG   D H    1 
ATOM   20423 H  HA   . ARG   D  4  65  ? 3.754   -61.560 -42.428  1.00 123.88 ? 65   ARG   D HA   1 
ATOM   20424 H  HB2  . ARG   D  4  65  ? 2.336   -62.422 -40.855  1.00 130.67 ? 65   ARG   D HB2  1 
ATOM   20425 H  HB3  . ARG   D  4  65  ? 1.459   -61.992 -42.109  1.00 130.67 ? 65   ARG   D HB3  1 
ATOM   20426 H  HG2  . ARG   D  4  65  ? 1.365   -64.278 -42.743  1.00 149.21 ? 65   ARG   D HG2  1 
ATOM   20427 H  HG3  . ARG   D  4  65  ? 2.081   -64.639 -41.371  1.00 149.21 ? 65   ARG   D HG3  1 
ATOM   20428 H  HD2  . ARG   D  4  65  ? 0.232   -63.537 -40.270  1.00 159.85 ? 65   ARG   D HD2  1 
ATOM   20429 H  HD3  . ARG   D  4  65  ? -0.503  -63.558 -41.679  1.00 159.85 ? 65   ARG   D HD3  1 
ATOM   20430 H  HE   . ARG   D  4  65  ? -0.102  -65.726 -40.102  1.00 169.57 ? 65   ARG   D HE   1 
ATOM   20431 H  HH11 . ARG   D  4  65  ? -1.353  -64.734 -43.007  1.00 174.51 ? 65   ARG   D HH11 1 
ATOM   20432 H  HH12 . ARG   D  4  65  ? -2.141  -65.970 -43.271  1.00 174.51 ? 65   ARG   D HH12 1 
ATOM   20433 H  HH21 . ARG   D  4  65  ? -1.307  -67.591 -40.524  1.00 186.15 ? 65   ARG   D HH21 1 
ATOM   20434 H  HH22 . ARG   D  4  65  ? -2.113  -67.695 -41.772  1.00 186.15 ? 65   ARG   D HH22 1 
ATOM   20435 N  N    . ASP   D  4  66  ? 4.308   -64.708 -42.674  1.00 112.88 ? 66   ASP   D N    1 
ATOM   20436 C  CA   . ASP   D  4  66  ? 5.276   -65.757 -42.386  1.00 116.05 ? 66   ASP   D CA   1 
ATOM   20437 C  C    . ASP   D  4  66  ? 6.344   -65.896 -43.462  1.00 116.56 ? 66   ASP   D C    1 
ATOM   20438 O  O    . ASP   D  4  66  ? 7.341   -66.591 -43.235  1.00 123.06 ? 66   ASP   D O    1 
ATOM   20439 C  CB   . ASP   D  4  66  ? 4.562   -67.102 -42.211  1.00 121.56 ? 66   ASP   D CB   1 
ATOM   20440 C  CG   . ASP   D  4  66  ? 3.888   -67.233 -40.859  1.00 124.59 ? 66   ASP   D CG   1 
ATOM   20441 O  OD1  . ASP   D  4  66  ? 4.506   -66.844 -39.846  1.00 125.98 ? 66   ASP   D OD1  1 
ATOM   20442 O  OD2  . ASP   D  4  66  ? 2.741   -67.724 -40.811  1.00 132.15 ? 66   ASP   D OD2  1 
ATOM   20443 H  H    . ASP   D  4  66  ? 3.648   -64.967 -43.161  1.00 135.49 ? 66   ASP   D H    1 
ATOM   20444 H  HA   . ASP   D  4  66  ? 5.721   -65.542 -41.551  1.00 139.30 ? 66   ASP   D HA   1 
ATOM   20445 H  HB2  . ASP   D  4  66  ? 3.881   -67.190 -42.896  1.00 145.91 ? 66   ASP   D HB2  1 
ATOM   20446 H  HB3  . ASP   D  4  66  ? 5.210   -67.818 -42.294  1.00 145.91 ? 66   ASP   D HB3  1 
ATOM   20447 N  N    . LYS   D  4  67  ? 6.168   -65.254 -44.618  1.00 110.36 ? 67   LYS   D N    1 
ATOM   20448 C  CA   . LYS   D  4  67  ? 7.141   -65.386 -45.697  1.00 106.80 ? 67   LYS   D CA   1 
ATOM   20449 C  C    . LYS   D  4  67  ? 8.339   -64.468 -45.486  1.00 96.57  ? 67   LYS   D C    1 
ATOM   20450 O  O    . LYS   D  4  67  ? 9.490   -64.917 -45.534  1.00 95.79  ? 67   LYS   D O    1 
ATOM   20451 C  CB   . LYS   D  4  67  ? 6.479   -65.084 -47.044  1.00 107.89 ? 67   LYS   D CB   1 
ATOM   20452 C  CG   . LYS   D  4  67  ? 5.452   -66.114 -47.484  1.00 122.05 ? 67   LYS   D CG   1 
ATOM   20453 C  CD   . LYS   D  4  67  ? 4.833   -65.749 -48.827  1.00 124.59 ? 67   LYS   D CD   1 
ATOM   20454 C  CE   . LYS   D  4  67  ? 3.775   -66.760 -49.242  1.00 132.07 ? 67   LYS   D CE   1 
ATOM   20455 N  NZ   . LYS   D  4  67  ? 3.133   -66.413 -50.541  1.00 130.75 ? 67   LYS   D NZ   1 
ATOM   20456 H  H    . LYS   D  4  67  ? 5.501   -64.742 -44.799  1.00 132.47 ? 67   LYS   D H    1 
ATOM   20457 H  HA   . LYS   D  4  67  ? 7.459   -66.302 -45.711  1.00 128.20 ? 67   LYS   D HA   1 
ATOM   20458 H  HB2  . LYS   D  4  67  ? 6.028   -64.228 -46.982  1.00 129.51 ? 67   LYS   D HB2  1 
ATOM   20459 H  HB3  . LYS   D  4  67  ? 7.168   -65.047 -47.726  1.00 129.51 ? 67   LYS   D HB3  1 
ATOM   20460 H  HG2  . LYS   D  4  67  ? 5.882   -66.979 -47.572  1.00 146.49 ? 67   LYS   D HG2  1 
ATOM   20461 H  HG3  . LYS   D  4  67  ? 4.742   -66.162 -46.824  1.00 146.49 ? 67   LYS   D HG3  1 
ATOM   20462 H  HD2  . LYS   D  4  67  ? 4.413   -64.877 -48.761  1.00 149.55 ? 67   LYS   D HD2  1 
ATOM   20463 H  HD3  . LYS   D  4  67  ? 5.525   -65.734 -49.507  1.00 149.55 ? 67   LYS   D HD3  1 
ATOM   20464 H  HE2  . LYS   D  4  67  ? 4.189   -67.632 -49.334  1.00 158.52 ? 67   LYS   D HE2  1 
ATOM   20465 H  HE3  . LYS   D  4  67  ? 3.083   -66.791 -48.563  1.00 158.52 ? 67   LYS   D HE3  1 
ATOM   20466 H  HZ1  . LYS   D  4  67  ? 2.316   -66.764 -50.580  1.00 156.93 ? 67   LYS   D HZ1  1 
ATOM   20467 H  HZ2  . LYS   D  4  67  ? 3.071   -65.529 -50.624  1.00 156.93 ? 67   LYS   D HZ2  1 
ATOM   20468 H  HZ3  . LYS   D  4  67  ? 3.617   -66.733 -51.215  1.00 156.93 ? 67   LYS   D HZ3  1 
ATOM   20469 N  N    . ALA   D  4  68  ? 8.091   -63.183 -45.249  1.00 87.22  ? 68   ALA   D N    1 
ATOM   20470 C  CA   . ALA   D  4  68  ? 9.135   -62.172 -45.245  1.00 83.81  ? 68   ALA   D CA   1 
ATOM   20471 C  C    . ALA   D  4  68  ? 9.400   -61.654 -43.838  1.00 77.11  ? 68   ALA   D C    1 
ATOM   20472 O  O    . ALA   D  4  68  ? 8.518   -61.658 -42.974  1.00 79.04  ? 68   ALA   D O    1 
ATOM   20473 C  CB   . ALA   D  4  68  ? 8.762   -60.997 -46.154  1.00 87.18  ? 68   ALA   D CB   1 
ATOM   20474 H  H    . ALA   D  4  68  ? 7.307   -62.869 -45.085  1.00 104.70 ? 68   ALA   D H    1 
ATOM   20475 H  HA   . ALA   D  4  68  ? 9.956   -62.576 -45.568  1.00 100.61 ? 68   ALA   D HA   1 
ATOM   20476 H  HB1  . ALA   D  4  68  ? 9.476   -60.341 -46.131  1.00 104.65 ? 68   ALA   D HB1  1 
ATOM   20477 H  HB2  . ALA   D  4  68  ? 8.641   -61.324 -47.059  1.00 104.65 ? 68   ALA   D HB2  1 
ATOM   20478 H  HB3  . ALA   D  4  68  ? 7.937   -60.599 -45.833  1.00 104.65 ? 68   ALA   D HB3  1 
ATOM   20479 N  N    . THR   D  4  69  ? 10.636  -61.207 -43.626  1.00 72.74  ? 69   THR   D N    1 
ATOM   20480 C  CA   . THR   D  4  69  ? 11.042  -60.538 -42.396  1.00 73.22  ? 69   THR   D CA   1 
ATOM   20481 C  C    . THR   D  4  69  ? 11.954  -59.385 -42.784  1.00 72.63  ? 69   THR   D C    1 
ATOM   20482 O  O    . THR   D  4  69  ? 12.957  -59.596 -43.472  1.00 71.27  ? 69   THR   D O    1 
ATOM   20483 C  CB   . THR   D  4  69  ? 11.760  -61.498 -41.442  1.00 74.66  ? 69   THR   D CB   1 
ATOM   20484 O  OG1  . THR   D  4  69  ? 13.035  -61.863 -41.985  1.00 77.06  ? 69   THR   D OG1  1 
ATOM   20485 C  CG2  . THR   D  4  69  ? 10.934  -62.759 -41.230  1.00 79.57  ? 69   THR   D CG2  1 
ATOM   20486 H  H    . THR   D  4  69  ? 11.275  -61.283 -44.198  1.00 87.33  ? 69   THR   D H    1 
ATOM   20487 H  HA   . THR   D  4  69  ? 10.263  -60.191 -41.934  1.00 87.90  ? 69   THR   D HA   1 
ATOM   20488 H  HB   . THR   D  4  69  ? 11.886  -61.059 -40.586  1.00 89.63  ? 69   THR   D HB   1 
ATOM   20489 H  HG1  . THR   D  4  69  ? 13.408  -61.189 -42.320  1.00 92.51  ? 69   THR   D HG1  1 
ATOM   20490 H  HG21 . THR   D  4  69  ? 11.386  -63.352 -40.610  1.00 95.53  ? 69   THR   D HG21 1 
ATOM   20491 H  HG22 . THR   D  4  69  ? 10.064  -62.529 -40.868  1.00 95.53  ? 69   THR   D HG22 1 
ATOM   20492 H  HG23 . THR   D  4  69  ? 10.811  -63.221 -42.075  1.00 95.53  ? 69   THR   D HG23 1 
ATOM   20493 N  N    . MET   D  4  70  ? 11.610  -58.177 -42.351  1.00 72.86  ? 70   MET   D N    1 
ATOM   20494 C  CA   . MET   D  4  70  ? 12.348  -56.978 -42.719  1.00 70.93  ? 70   MET   D CA   1 
ATOM   20495 C  C    . MET   D  4  70  ? 13.201  -56.502 -41.552  1.00 70.74  ? 70   MET   D C    1 
ATOM   20496 O  O    . MET   D  4  70  ? 12.771  -56.538 -40.395  1.00 73.85  ? 70   MET   D O    1 
ATOM   20497 C  CB   . MET   D  4  70  ? 11.389  -55.869 -43.149  1.00 68.61  ? 70   MET   D CB   1 
ATOM   20498 C  CG   . MET   D  4  70  ? 10.490  -56.264 -44.299  1.00 67.99  ? 70   MET   D CG   1 
ATOM   20499 S  SD   . MET   D  4  70  ? 8.981   -55.291 -44.354  1.00 67.35  ? 70   MET   D SD   1 
ATOM   20500 C  CE   . MET   D  4  70  ? 8.166   -56.078 -45.736  1.00 78.13  ? 70   MET   D CE   1 
ATOM   20501 H  H    . MET   D  4  70  ? 10.940  -58.026 -41.834  1.00 87.47  ? 70   MET   D H    1 
ATOM   20502 H  HA   . MET   D  4  70  ? 12.932  -57.183 -43.466  1.00 85.16  ? 70   MET   D HA   1 
ATOM   20503 H  HB2  . MET   D  4  70  ? 10.823  -55.635 -42.396  1.00 82.36  ? 70   MET   D HB2  1 
ATOM   20504 H  HB3  . MET   D  4  70  ? 11.907  -55.098 -43.427  1.00 82.36  ? 70   MET   D HB3  1 
ATOM   20505 H  HG2  . MET   D  4  70  ? 10.965  -56.131 -45.134  1.00 81.62  ? 70   MET   D HG2  1 
ATOM   20506 H  HG3  . MET   D  4  70  ? 10.243  -57.197 -44.203  1.00 81.62  ? 70   MET   D HG3  1 
ATOM   20507 H  HE1  . MET   D  4  70  ? 7.330   -55.619 -45.912  1.00 93.79  ? 70   MET   D HE1  1 
ATOM   20508 H  HE2  . MET   D  4  70  ? 8.743   -56.026 -46.514  1.00 93.79  ? 70   MET   D HE2  1 
ATOM   20509 H  HE3  . MET   D  4  70  ? 7.993   -57.006 -45.513  1.00 93.79  ? 70   MET   D HE3  1 
ATOM   20510 N  N    . THR   D  4  71  ? 14.413  -56.054 -41.867  1.00 67.58  ? 71   THR   D N    1 
ATOM   20511 C  CA   . THR   D  4  71  ? 15.344  -55.538 -40.875  1.00 69.22  ? 71   THR   D CA   1 
ATOM   20512 C  C    . THR   D  4  71  ? 16.044  -54.324 -41.468  1.00 66.72  ? 71   THR   D C    1 
ATOM   20513 O  O    . THR   D  4  71  ? 15.891  -54.012 -42.652  1.00 67.53  ? 71   THR   D O    1 
ATOM   20514 C  CB   . THR   D  4  71  ? 16.358  -56.607 -40.448  1.00 73.12  ? 71   THR   D CB   1 
ATOM   20515 O  OG1  . THR   D  4  71  ? 17.107  -57.045 -41.587  1.00 76.09  ? 71   THR   D OG1  1 
ATOM   20516 C  CG2  . THR   D  4  71  ? 15.646  -57.801 -39.829  1.00 78.12  ? 71   THR   D CG2  1 
ATOM   20517 H  H    . THR   D  4  71  ? 14.725  -56.040 -42.668  1.00 81.13  ? 71   THR   D H    1 
ATOM   20518 H  HA   . THR   D  4  71  ? 14.861  -55.258 -40.083  1.00 83.10  ? 71   THR   D HA   1 
ATOM   20519 H  HB   . THR   D  4  71  ? 16.962  -56.230 -39.789  1.00 87.78  ? 71   THR   D HB   1 
ATOM   20520 H  HG1  . THR   D  4  71  ? 17.831  -56.622 -41.635  1.00 91.35  ? 71   THR   D HG1  1 
ATOM   20521 H  HG21 . THR   D  4  71  ? 16.294  -58.469 -39.557  1.00 93.78  ? 71   THR   D HG21 1 
ATOM   20522 H  HG22 . THR   D  4  71  ? 15.139  -57.518 -39.052  1.00 93.78  ? 71   THR   D HG22 1 
ATOM   20523 H  HG23 . THR   D  4  71  ? 15.039  -58.196 -40.474  1.00 93.78  ? 71   THR   D HG23 1 
ATOM   20524 N  N    . ALA   D  4  72  ? 16.816  -53.630 -40.636  1.00 63.60  ? 72   ALA   D N    1 
ATOM   20525 C  CA   . ALA   D  4  72  ? 17.496  -52.429 -41.097  1.00 64.92  ? 72   ALA   D CA   1 
ATOM   20526 C  C    . ALA   D  4  72  ? 18.721  -52.164 -40.236  1.00 70.40  ? 72   ALA   D C    1 
ATOM   20527 O  O    . ALA   D  4  72  ? 18.681  -52.329 -39.014  1.00 75.01  ? 72   ALA   D O    1 
ATOM   20528 C  CB   . ALA   D  4  72  ? 16.560  -51.215 -41.072  1.00 64.76  ? 72   ALA   D CB   1 
ATOM   20529 H  H    . ALA   D  4  72  ? 16.958  -53.832 -39.812  1.00 76.35  ? 72   ALA   D H    1 
ATOM   20530 H  HA   . ALA   D  4  72  ? 17.801  -52.573 -42.006  1.00 77.94  ? 72   ALA   D HA   1 
ATOM   20531 H  HB1  . ALA   D  4  72  ? 17.048  -50.434 -41.377  1.00 77.75  ? 72   ALA   D HB1  1 
ATOM   20532 H  HB2  . ALA   D  4  72  ? 15.807  -51.386 -41.658  1.00 77.75  ? 72   ALA   D HB2  1 
ATOM   20533 H  HB3  . ALA   D  4  72  ? 16.248  -51.076 -40.164  1.00 77.75  ? 72   ALA   D HB3  1 
ATOM   20534 N  N    . ASP   D  4  73  ? 19.800  -51.746 -40.891  1.00 71.73  ? 73   ASP   D N    1 
ATOM   20535 C  CA   . ASP   D  4  73  ? 21.060  -51.386 -40.247  1.00 74.09  ? 73   ASP   D CA   1 
ATOM   20536 C  C    . ASP   D  4  73  ? 21.225  -49.877 -40.408  1.00 74.57  ? 73   ASP   D C    1 
ATOM   20537 O  O    . ASP   D  4  73  ? 21.580  -49.394 -41.487  1.00 75.35  ? 73   ASP   D O    1 
ATOM   20538 C  CB   . ASP   D  4  73  ? 22.220  -52.158 -40.870  1.00 76.91  ? 73   ASP   D CB   1 
ATOM   20539 C  CG   . ASP   D  4  73  ? 23.559  -51.817 -40.244  1.00 84.75  ? 73   ASP   D CG   1 
ATOM   20540 O  OD1  . ASP   D  4  73  ? 23.600  -50.960 -39.337  1.00 87.64  ? 73   ASP   D OD1  1 
ATOM   20541 O  OD2  . ASP   D  4  73  ? 24.576  -52.412 -40.663  1.00 88.87  ? 73   ASP   D OD2  1 
ATOM   20542 H  H    . ASP   D  4  73  ? 19.827  -51.660 -41.746  1.00 86.11  ? 73   ASP   D H    1 
ATOM   20543 H  HA   . ASP   D  4  73  ? 21.032  -51.598 -39.301  1.00 88.95  ? 73   ASP   D HA   1 
ATOM   20544 H  HB2  . ASP   D  4  73  ? 22.066  -53.108 -40.751  1.00 92.33  ? 73   ASP   D HB2  1 
ATOM   20545 H  HB3  . ASP   D  4  73  ? 22.268  -51.946 -41.816  1.00 92.33  ? 73   ASP   D HB3  1 
ATOM   20546 N  N    . THR   D  4  74  ? 20.965  -49.134 -39.330  1.00 76.11  ? 74   THR   D N    1 
ATOM   20547 C  CA   . THR   D  4  74  ? 20.984  -47.678 -39.415  1.00 75.62  ? 74   THR   D CA   1 
ATOM   20548 C  C    . THR   D  4  74  ? 22.384  -47.141 -39.686  1.00 78.44  ? 74   THR   D C    1 
ATOM   20549 O  O    . THR   D  4  74  ? 22.531  -46.105 -40.343  1.00 78.69  ? 74   THR   D O    1 
ATOM   20550 C  CB   . THR   D  4  74  ? 20.438  -47.067 -38.124  1.00 78.47  ? 74   THR   D CB   1 
ATOM   20551 O  OG1  . THR   D  4  74  ? 21.229  -47.504 -37.011  1.00 84.03  ? 74   THR   D OG1  1 
ATOM   20552 C  CG2  . THR   D  4  74  ? 18.988  -47.476 -37.907  1.00 77.02  ? 74   THR   D CG2  1 
ATOM   20553 H  H    . THR   D  4  74  ? 20.777  -49.446 -38.551  1.00 91.37  ? 74   THR   D H    1 
ATOM   20554 H  HA   . THR   D  4  74  ? 20.410  -47.409 -40.149  1.00 90.78  ? 74   THR   D HA   1 
ATOM   20555 H  HB   . THR   D  4  74  ? 20.474  -46.099 -38.185  1.00 94.19  ? 74   THR   D HB   1 
ATOM   20556 H  HG1  . THR   D  4  74  ? 20.930  -47.173 -36.299  1.00 100.87 ? 74   THR   D HG1  1 
ATOM   20557 H  HG21 . THR   D  4  74  ? 18.672  -47.138 -37.055  1.00 92.46  ? 74   THR   D HG21 1 
ATOM   20558 H  HG22 . THR   D  4  74  ? 18.432  -47.114 -38.615  1.00 92.46  ? 74   THR   D HG22 1 
ATOM   20559 H  HG23 . THR   D  4  74  ? 18.913  -48.443 -37.910  1.00 92.46  ? 74   THR   D HG23 1 
ATOM   20560 N  N    . SER   D  4  75  ? 23.419  -47.825 -39.194  1.00 83.45  ? 75   SER   D N    1 
ATOM   20561 C  CA   . SER   D  4  75  ? 24.776  -47.308 -39.337  1.00 89.33  ? 75   SER   D CA   1 
ATOM   20562 C  C    . SER   D  4  75  ? 25.227  -47.287 -40.792  1.00 87.80  ? 75   SER   D C    1 
ATOM   20563 O  O    . SER   D  4  75  ? 26.063  -46.456 -41.166  1.00 92.25  ? 75   SER   D O    1 
ATOM   20564 C  CB   . SER   D  4  75  ? 25.744  -48.140 -38.497  1.00 95.68  ? 75   SER   D CB   1 
ATOM   20565 O  OG   . SER   D  4  75  ? 25.737  -49.496 -38.906  1.00 101.10 ? 75   SER   D OG   1 
ATOM   20566 H  H    . SER   D  4  75  ? 23.363  -48.577 -38.781  1.00 100.17 ? 75   SER   D H    1 
ATOM   20567 H  HA   . SER   D  4  75  ? 24.794  -46.396 -39.007  1.00 107.23 ? 75   SER   D HA   1 
ATOM   20568 H  HB2  . SER   D  4  75  ? 26.640  -47.783 -38.603  1.00 114.85 ? 75   SER   D HB2  1 
ATOM   20569 H  HB3  . SER   D  4  75  ? 25.476  -48.091 -37.566  1.00 114.85 ? 75   SER   D HB3  1 
ATOM   20570 H  HG   . SER   D  4  75  ? 24.964  -49.815 -38.832  1.00 121.36 ? 75   SER   D HG   1 
ATOM   20571 N  N    . SER   D  4  76  ? 24.696  -48.184 -41.622  1.00 82.87  ? 76   SER   D N    1 
ATOM   20572 C  CA   . SER   D  4  76  ? 25.057  -48.252 -43.031  1.00 82.24  ? 76   SER   D CA   1 
ATOM   20573 C  C    . SER   D  4  76  ? 23.954  -47.750 -43.952  1.00 78.58  ? 76   SER   D C    1 
ATOM   20574 O  O    . SER   D  4  76  ? 24.130  -47.773 -45.174  1.00 79.13  ? 76   SER   D O    1 
ATOM   20575 C  CB   . SER   D  4  76  ? 25.425  -49.691 -43.412  1.00 80.37  ? 76   SER   D CB   1 
ATOM   20576 O  OG   . SER   D  4  76  ? 24.349  -50.578 -43.158  1.00 80.03  ? 76   SER   D OG   1 
ATOM   20577 H  H    . SER   D  4  76  ? 24.114  -48.772 -41.386  1.00 99.48  ? 76   SER   D H    1 
ATOM   20578 H  HA   . SER   D  4  76  ? 25.838  -47.695 -43.173  1.00 98.72  ? 76   SER   D HA   1 
ATOM   20579 H  HB2  . SER   D  4  76  ? 25.641  -49.721 -44.357  1.00 96.49  ? 76   SER   D HB2  1 
ATOM   20580 H  HB3  . SER   D  4  76  ? 26.192  -49.969 -42.887  1.00 96.49  ? 76   SER   D HB3  1 
ATOM   20581 H  HG   . SER   D  4  76  ? 24.587  -51.369 -43.312  1.00 96.08  ? 76   SER   D HG   1 
ATOM   20582 N  N    . SER   D  4  77  ? 22.829  -47.291 -43.403  1.00 72.90  ? 77   SER   D N    1 
ATOM   20583 C  CA   . SER   D  4  77  ? 21.697  -46.833 -44.206  1.00 67.51  ? 77   SER   D CA   1 
ATOM   20584 C  C    . SER   D  4  77  ? 21.245  -47.926 -45.175  1.00 66.09  ? 77   SER   D C    1 
ATOM   20585 O  O    . SER   D  4  77  ? 21.059  -47.692 -46.371  1.00 64.76  ? 77   SER   D O    1 
ATOM   20586 C  CB   . SER   D  4  77  ? 22.043  -45.545 -44.958  1.00 68.80  ? 77   SER   D CB   1 
ATOM   20587 O  OG   . SER   D  4  77  ? 22.293  -44.481 -44.056  1.00 71.40  ? 77   SER   D OG   1 
ATOM   20588 H  H    . SER   D  4  77  ? 22.696  -47.235 -42.555  1.00 87.52  ? 77   SER   D H    1 
ATOM   20589 H  HA   . SER   D  4  77  ? 20.955  -46.640 -43.612  1.00 81.05  ? 77   SER   D HA   1 
ATOM   20590 H  HB2  . SER   D  4  77  ? 22.837  -45.696 -45.493  1.00 82.60  ? 77   SER   D HB2  1 
ATOM   20591 H  HB3  . SER   D  4  77  ? 21.298  -45.304 -45.530  1.00 82.60  ? 77   SER   D HB3  1 
ATOM   20592 H  HG   . SER   D  4  77  ? 21.949  -43.772 -44.346  1.00 85.71  ? 77   SER   D HG   1 
ATOM   20593 N  N    . THR   D  4  78  ? 21.066  -49.134 -44.643  1.00 66.48  ? 78   THR   D N    1 
ATOM   20594 C  CA   . THR   D  4  78  ? 20.701  -50.294 -45.445  1.00 67.07  ? 78   THR   D CA   1 
ATOM   20595 C  C    . THR   D  4  78  ? 19.492  -50.986 -44.836  1.00 64.60  ? 78   THR   D C    1 
ATOM   20596 O  O    . THR   D  4  78  ? 19.438  -51.203 -43.621  1.00 64.68  ? 78   THR   D O    1 
ATOM   20597 C  CB   . THR   D  4  78  ? 21.864  -51.289 -45.550  1.00 71.16  ? 78   THR   D CB   1 
ATOM   20598 O  OG1  . THR   D  4  78  ? 23.006  -50.637 -46.120  1.00 75.30  ? 78   THR   D OG1  1 
ATOM   20599 C  CG2  . THR   D  4  78  ? 21.474  -52.481 -46.419  1.00 71.29  ? 78   THR   D CG2  1 
ATOM   20600 H  H    . THR   D  4  78  ? 21.153  -49.307 -43.805  1.00 79.81  ? 78   THR   D H    1 
ATOM   20601 H  HA   . THR   D  4  78  ? 20.463  -49.992 -46.335  1.00 80.52  ? 78   THR   D HA   1 
ATOM   20602 H  HB   . THR   D  4  78  ? 22.089  -51.616 -44.665  1.00 85.43  ? 78   THR   D HB   1 
ATOM   20603 H  HG1  . THR   D  4  78  ? 23.656  -51.169 -46.147  1.00 90.40  ? 78   THR   D HG1  1 
ATOM   20604 H  HG21 . THR   D  4  78  ? 22.232  -53.078 -46.521  1.00 85.59  ? 78   THR   D HG21 1 
ATOM   20605 H  HG22 . THR   D  4  78  ? 20.743  -52.967 -46.006  1.00 85.59  ? 78   THR   D HG22 1 
ATOM   20606 H  HG23 . THR   D  4  78  ? 21.194  -52.175 -47.295  1.00 85.59  ? 78   THR   D HG23 1 
ATOM   20607 N  N    . ALA   D  4  79  ? 18.531  -51.335 -45.687  1.00 62.42  ? 79   ALA   D N    1 
ATOM   20608 C  CA   . ALA   D  4  79  ? 17.389  -52.154 -45.313  1.00 60.11  ? 79   ALA   D CA   1 
ATOM   20609 C  C    . ALA   D  4  79  ? 17.564  -53.546 -45.904  1.00 58.58  ? 79   ALA   D C    1 
ATOM   20610 O  O    . ALA   D  4  79  ? 18.077  -53.697 -47.017  1.00 60.52  ? 79   ALA   D O    1 
ATOM   20611 C  CB   . ALA   D  4  79  ? 16.080  -51.535 -45.808  1.00 62.67  ? 79   ALA   D CB   1 
ATOM   20612 H  H    . ALA   D  4  79  ? 18.522  -51.099 -46.514  1.00 74.94  ? 79   ALA   D H    1 
ATOM   20613 H  HA   . ALA   D  4  79  ? 17.335  -52.227 -44.348  1.00 72.17  ? 79   ALA   D HA   1 
ATOM   20614 H  HB1  . ALA   D  4  79  ? 15.342  -52.112 -45.554  1.00 75.24  ? 79   ALA   D HB1  1 
ATOM   20615 H  HB2  . ALA   D  4  79  ? 15.971  -50.661 -45.403  1.00 75.24  ? 79   ALA   D HB2  1 
ATOM   20616 H  HB3  . ALA   D  4  79  ? 16.115  -51.450 -46.774  1.00 75.24  ? 79   ALA   D HB3  1 
ATOM   20617 N  N    . TYR   D  4  80  ? 17.140  -54.560 -45.155  1.00 59.21  ? 80   TYR   D N    1 
ATOM   20618 C  CA   . TYR   D  4  80  ? 17.245  -55.947 -45.578  1.00 60.60  ? 80   TYR   D CA   1 
ATOM   20619 C  C    . TYR   D  4  80  ? 15.868  -56.591 -45.557  1.00 61.39  ? 80   TYR   D C    1 
ATOM   20620 O  O    . TYR   D  4  80  ? 15.037  -56.277 -44.701  1.00 61.18  ? 80   TYR   D O    1 
ATOM   20621 C  CB   . TYR   D  4  80  ? 18.177  -56.750 -44.662  1.00 60.00  ? 80   TYR   D CB   1 
ATOM   20622 C  CG   . TYR   D  4  80  ? 19.599  -56.248 -44.596  1.00 60.25  ? 80   TYR   D CG   1 
ATOM   20623 C  CD1  . TYR   D  4  80  ? 19.971  -55.277 -43.676  1.00 62.73  ? 80   TYR   D CD1  1 
ATOM   20624 C  CD2  . TYR   D  4  80  ? 20.575  -56.760 -45.440  1.00 62.50  ? 80   TYR   D CD2  1 
ATOM   20625 C  CE1  . TYR   D  4  80  ? 21.274  -54.821 -43.606  1.00 65.71  ? 80   TYR   D CE1  1 
ATOM   20626 C  CE2  . TYR   D  4  80  ? 21.880  -56.312 -45.377  1.00 65.78  ? 80   TYR   D CE2  1 
ATOM   20627 C  CZ   . TYR   D  4  80  ? 22.224  -55.343 -44.459  1.00 67.43  ? 80   TYR   D CZ   1 
ATOM   20628 O  OH   . TYR   D  4  80  ? 23.523  -54.894 -44.393  1.00 72.92  ? 80   TYR   D OH   1 
ATOM   20629 H  H    . TYR   D  4  80  ? 16.781  -54.465 -44.380  1.00 71.08  ? 80   TYR   D H    1 
ATOM   20630 H  HA   . TYR   D  4  80  ? 17.599  -55.976 -46.481  1.00 72.76  ? 80   TYR   D HA   1 
ATOM   20631 H  HB2  . TYR   D  4  80  ? 17.818  -56.725 -43.761  1.00 72.04  ? 80   TYR   D HB2  1 
ATOM   20632 H  HB3  . TYR   D  4  80  ? 18.206  -57.666 -44.982  1.00 72.04  ? 80   TYR   D HB3  1 
ATOM   20633 H  HD1  . TYR   D  4  80  ? 19.333  -54.927 -43.098  1.00 75.31  ? 80   TYR   D HD1  1 
ATOM   20634 H  HD2  . TYR   D  4  80  ? 20.346  -57.417 -46.057  1.00 75.04  ? 80   TYR   D HD2  1 
ATOM   20635 H  HE1  . TYR   D  4  80  ? 21.509  -54.167 -42.988  1.00 78.89  ? 80   TYR   D HE1  1 
ATOM   20636 H  HE2  . TYR   D  4  80  ? 22.523  -56.662 -45.951  1.00 78.98  ? 80   TYR   D HE2  1 
ATOM   20637 H  HH   . TYR   D  4  80  ? 23.988  -55.273 -44.981  1.00 87.54  ? 80   TYR   D HH   1 
ATOM   20638 N  N    . MET   D  4  81  ? 15.629  -57.495 -46.505  1.00 66.58  ? 81   MET   D N    1 
ATOM   20639 C  CA   . MET   D  4  81  ? 14.481  -58.386 -46.441  1.00 73.36  ? 81   MET   D CA   1 
ATOM   20640 C  C    . MET   D  4  81  ? 14.941  -59.815 -46.678  1.00 73.38  ? 81   MET   D C    1 
ATOM   20641 O  O    . MET   D  4  81  ? 15.820  -60.067 -47.509  1.00 74.76  ? 81   MET   D O    1 
ATOM   20642 C  CB   . MET   D  4  81  ? 13.404  -58.035 -47.461  1.00 79.67  ? 81   MET   D CB   1 
ATOM   20643 C  CG   . MET   D  4  81  ? 12.190  -58.939 -47.338  1.00 84.91  ? 81   MET   D CG   1 
ATOM   20644 S  SD   . MET   D  4  81  ? 10.825  -58.441 -48.390  1.00 95.58  ? 81   MET   D SD   1 
ATOM   20645 C  CE   . MET   D  4  81  ? 11.573  -58.683 -49.996  1.00 100.55 ? 81   MET   D CE   1 
ATOM   20646 H  H    . MET   D  4  81  ? 16.123  -57.609 -47.199  1.00 79.94  ? 81   MET   D H    1 
ATOM   20647 H  HA   . MET   D  4  81  ? 14.086  -58.302 -45.560  1.00 88.07  ? 81   MET   D HA   1 
ATOM   20648 H  HB2  . MET   D  4  81  ? 13.117  -57.120 -47.319  1.00 95.64  ? 81   MET   D HB2  1 
ATOM   20649 H  HB3  . MET   D  4  81  ? 13.767  -58.135 -48.355  1.00 95.64  ? 81   MET   D HB3  1 
ATOM   20650 H  HG2  . MET   D  4  81  ? 12.444  -59.842 -47.587  1.00 101.93 ? 81   MET   D HG2  1 
ATOM   20651 H  HG3  . MET   D  4  81  ? 11.879  -58.924 -46.419  1.00 101.93 ? 81   MET   D HG3  1 
ATOM   20652 H  HE1  . MET   D  4  81  ? 10.922  -58.471 -50.683  1.00 120.69 ? 81   MET   D HE1  1 
ATOM   20653 H  HE2  . MET   D  4  81  ? 12.342  -58.098 -50.078  1.00 120.69 ? 81   MET   D HE2  1 
ATOM   20654 H  HE3  . MET   D  4  81  ? 11.851  -59.609 -50.079  1.00 120.69 ? 81   MET   D HE3  1 
ATOM   20655 N  N    . GLN   D  4  82  ? 14.329  -60.744 -45.952  1.00 69.42  ? 82   GLN   D N    1 
ATOM   20656 C  CA   . GLN   D  4  82  ? 14.656  -62.159 -46.039  1.00 71.46  ? 82   GLN   D CA   1 
ATOM   20657 C  C    . GLN   D  4  82  ? 13.393  -62.936 -46.378  1.00 75.65  ? 82   GLN   D C    1 
ATOM   20658 O  O    . GLN   D  4  82  ? 12.387  -62.834 -45.668  1.00 75.47  ? 82   GLN   D O    1 
ATOM   20659 C  CB   . GLN   D  4  82  ? 15.262  -62.659 -44.729  1.00 71.04  ? 82   GLN   D CB   1 
ATOM   20660 C  CG   . GLN   D  4  82  ? 15.865  -64.043 -44.820  1.00 76.56  ? 82   GLN   D CG   1 
ATOM   20661 C  CD   . GLN   D  4  82  ? 16.530  -64.466 -43.529  1.00 74.59  ? 82   GLN   D CD   1 
ATOM   20662 O  OE1  . GLN   D  4  82  ? 15.955  -64.333 -42.449  1.00 72.59  ? 82   GLN   D OE1  1 
ATOM   20663 N  NE2  . GLN   D  4  82  ? 17.754  -64.969 -43.631  1.00 78.52  ? 82   GLN   D NE2  1 
ATOM   20664 H  H    . GLN   D  4  82  ? 13.704  -60.572 -45.386  1.00 83.35  ? 82   GLN   D H    1 
ATOM   20665 H  HA   . GLN   D  4  82  ? 15.299  -62.301 -46.751  1.00 85.78  ? 82   GLN   D HA   1 
ATOM   20666 H  HB2  . GLN   D  4  82  ? 15.964  -62.047 -44.458  1.00 85.28  ? 82   GLN   D HB2  1 
ATOM   20667 H  HB3  . GLN   D  4  82  ? 14.565  -62.684 -44.054  1.00 85.28  ? 82   GLN   D HB3  1 
ATOM   20668 H  HG2  . GLN   D  4  82  ? 15.165  -64.683 -45.023  1.00 91.90  ? 82   GLN   D HG2  1 
ATOM   20669 H  HG3  . GLN   D  4  82  ? 16.536  -64.052 -45.521  1.00 91.90  ? 82   GLN   D HG3  1 
ATOM   20670 H  HE21 . GLN   D  4  82  ? 18.127  -65.039 -44.402  1.00 94.26  ? 82   GLN   D HE21 1 
ATOM   20671 H  HE22 . GLN   D  4  82  ? 18.174  -65.224 -42.925  1.00 94.26  ? 82   GLN   D HE22 1 
ATOM   20672 N  N    . LEU   D  4  83  ? 13.449  -63.704 -47.461  1.00 79.07  ? 83   LEU   D N    1 
ATOM   20673 C  CA   . LEU   D  4  83  ? 12.360  -64.578 -47.872  1.00 86.58  ? 83   LEU   D CA   1 
ATOM   20674 C  C    . LEU   D  4  83  ? 12.689  -66.002 -47.447  1.00 96.80  ? 83   LEU   D C    1 
ATOM   20675 O  O    . LEU   D  4  83  ? 13.760  -66.519 -47.781  1.00 103.84 ? 83   LEU   D O    1 
ATOM   20676 C  CB   . LEU   D  4  83  ? 12.149  -64.507 -49.383  1.00 86.35  ? 83   LEU   D CB   1 
ATOM   20677 C  CG   . LEU   D  4  83  ? 11.883  -63.101 -49.922  1.00 80.86  ? 83   LEU   D CG   1 
ATOM   20678 C  CD1  . LEU   D  4  83  ? 11.828  -63.114 -51.439  1.00 81.80  ? 83   LEU   D CD1  1 
ATOM   20679 C  CD2  . LEU   D  4  83  ? 10.594  -62.543 -49.337  1.00 77.35  ? 83   LEU   D CD2  1 
ATOM   20680 H  H    . LEU   D  4  83  ? 14.127  -63.735 -47.989  1.00 94.92  ? 83   LEU   D H    1 
ATOM   20681 H  HA   . LEU   D  4  83  ? 11.534  -64.308 -47.441  1.00 103.93 ? 83   LEU   D HA   1 
ATOM   20682 H  HB2  . LEU   D  4  83  ? 12.946  -64.843 -49.822  1.00 103.66 ? 83   LEU   D HB2  1 
ATOM   20683 H  HB3  . LEU   D  4  83  ? 11.385  -65.059 -49.614  1.00 103.66 ? 83   LEU   D HB3  1 
ATOM   20684 H  HG   . LEU   D  4  83  ? 12.609  -62.516 -49.657  1.00 97.06  ? 83   LEU   D HG   1 
ATOM   20685 H  HD11 . LEU   D  4  83  ? 11.681  -62.209 -51.757  1.00 98.20  ? 83   LEU   D HD11 1 
ATOM   20686 H  HD12 . LEU   D  4  83  ? 12.669  -63.453 -51.782  1.00 98.20  ? 83   LEU   D HD12 1 
ATOM   20687 H  HD13 . LEU   D  4  83  ? 11.099  -63.687 -51.724  1.00 98.20  ? 83   LEU   D HD13 1 
ATOM   20688 H  HD21 . LEU   D  4  83  ? 10.435  -61.661 -49.708  1.00 92.86  ? 83   LEU   D HD21 1 
ATOM   20689 H  HD22 . LEU   D  4  83  ? 9.860   -63.135 -49.566  1.00 92.86  ? 83   LEU   D HD22 1 
ATOM   20690 H  HD23 . LEU   D  4  83  ? 10.684  -62.485 -48.373  1.00 92.86  ? 83   LEU   D HD23 1 
ATOM   20691 N  N    . SER   D  4  84  ? 11.772  -66.630 -46.717  1.00 94.87  ? 84   SER   D N    1 
ATOM   20692 C  CA   . SER   D  4  84  ? 12.005  -67.938 -46.127  1.00 95.70  ? 84   SER   D CA   1 
ATOM   20693 C  C    . SER   D  4  84  ? 10.939  -68.925 -46.584  1.00 95.00  ? 84   SER   D C    1 
ATOM   20694 O  O    . SER   D  4  84  ? 9.801   -68.547 -46.877  1.00 93.80  ? 84   SER   D O    1 
ATOM   20695 C  CB   . SER   D  4  84  ? 12.020  -67.849 -44.597  1.00 96.61  ? 84   SER   D CB   1 
ATOM   20696 O  OG   . SER   D  4  84  ? 10.992  -66.993 -44.129  1.00 94.50  ? 84   SER   D OG   1 
ATOM   20697 H  H    . SER   D  4  84  ? 10.993  -66.308 -46.548  1.00 113.88 ? 84   SER   D H    1 
ATOM   20698 H  HA   . SER   D  4  84  ? 12.862  -68.281 -46.424  1.00 114.87 ? 84   SER   D HA   1 
ATOM   20699 H  HB2  . SER   D  4  84  ? 11.885  -68.735 -44.228  1.00 115.97 ? 84   SER   D HB2  1 
ATOM   20700 H  HB3  . SER   D  4  84  ? 12.877  -67.497 -44.310  1.00 115.97 ? 84   SER   D HB3  1 
ATOM   20701 H  HG   . SER   D  4  84  ? 10.942  -67.034 -43.292  1.00 113.44 ? 84   SER   D HG   1 
ATOM   20702 N  N    . GLY   D  4  85  ? 11.323  -70.200 -46.637  1.00 77.14  ? 85   GLY   D N    1 
ATOM   20703 C  CA   . GLY   D  4  85  ? 10.435  -71.241 -47.117  1.00 83.19  ? 85   GLY   D CA   1 
ATOM   20704 C  C    . GLY   D  4  85  ? 10.108  -71.049 -48.582  1.00 88.95  ? 85   GLY   D C    1 
ATOM   20705 O  O    . GLY   D  4  85  ? 8.939   -71.066 -48.978  1.00 91.60  ? 85   GLY   D O    1 
ATOM   20706 H  H    . GLY   D  4  85  ? 12.099  -70.483 -46.398  1.00 92.60  ? 85   GLY   D H    1 
ATOM   20707 H  HA2  . GLY   D  4  85  ? 10.858  -72.107 -47.003  1.00 99.86  ? 85   GLY   D HA2  1 
ATOM   20708 H  HA3  . GLY   D  4  85  ? 9.609   -71.224 -46.609  1.00 99.86  ? 85   GLY   D HA3  1 
ATOM   20709 N  N    . LEU   D  4  86  ? 11.146  -70.878 -49.395  1.00 89.43  ? 86   LEU   D N    1 
ATOM   20710 C  CA   . LEU   D  4  86  ? 10.970  -70.435 -50.769  1.00 91.89  ? 86   LEU   D CA   1 
ATOM   20711 C  C    . LEU   D  4  86  ? 10.228  -71.470 -51.607  1.00 97.76  ? 86   LEU   D C    1 
ATOM   20712 O  O    . LEU   D  4  86  ? 10.281  -72.675 -51.348  1.00 102.57 ? 86   LEU   D O    1 
ATOM   20713 C  CB   . LEU   D  4  86  ? 12.328  -70.135 -51.402  1.00 90.13  ? 86   LEU   D CB   1 
ATOM   20714 C  CG   . LEU   D  4  86  ? 12.984  -68.834 -50.940  1.00 84.97  ? 86   LEU   D CG   1 
ATOM   20715 C  CD1  . LEU   D  4  86  ? 14.443  -68.788 -51.359  1.00 83.36  ? 86   LEU   D CD1  1 
ATOM   20716 C  CD2  . LEU   D  4  86  ? 12.228  -67.638 -51.499  1.00 81.23  ? 86   LEU   D CD2  1 
ATOM   20717 H  H    . LEU   D  4  86  ? 11.966  -71.012 -49.173  1.00 107.35 ? 86   LEU   D H    1 
ATOM   20718 H  HA   . LEU   D  4  86  ? 10.437  -69.624 -50.771  1.00 110.31 ? 86   LEU   D HA   1 
ATOM   20719 H  HB2  . LEU   D  4  86  ? 12.934  -70.861 -51.183  1.00 108.19 ? 86   LEU   D HB2  1 
ATOM   20720 H  HB3  . LEU   D  4  86  ? 12.212  -70.078 -52.363  1.00 108.19 ? 86   LEU   D HB3  1 
ATOM   20721 H  HG   . LEU   D  4  86  ? 12.953  -68.789 -49.972  1.00 102.00 ? 86   LEU   D HG   1 
ATOM   20722 H  HD11 . LEU   D  4  86  ? 14.830  -67.948 -51.066  1.00 100.07 ? 86   LEU   D HD11 1 
ATOM   20723 H  HD12 . LEU   D  4  86  ? 14.913  -69.530 -50.948  1.00 100.07 ? 86   LEU   D HD12 1 
ATOM   20724 H  HD13 . LEU   D  4  86  ? 14.497  -68.857 -52.326  1.00 100.07 ? 86   LEU   D HD13 1 
ATOM   20725 H  HD21 . LEU   D  4  86  ? 12.677  -66.824 -51.224  1.00 97.51  ? 86   LEU   D HD21 1 
ATOM   20726 H  HD22 . LEU   D  4  86  ? 12.213  -67.698 -52.467  1.00 97.51  ? 86   LEU   D HD22 1 
ATOM   20727 H  HD23 . LEU   D  4  86  ? 11.321  -67.648 -51.154  1.00 97.51  ? 86   LEU   D HD23 1 
ATOM   20728 N  N    . THR   D  4  87  ? 9.527   -70.974 -52.625  1.00 96.95  ? 87   THR   D N    1 
ATOM   20729 C  CA   . THR   D  4  87  ? 8.819   -71.805 -53.588  1.00 98.43  ? 87   THR   D CA   1 
ATOM   20730 C  C    . THR   D  4  87  ? 9.020   -71.189 -54.969  1.00 98.25  ? 87   THR   D C    1 
ATOM   20731 O  O    . THR   D  4  87  ? 9.774   -70.225 -55.136  1.00 97.82  ? 87   THR   D O    1 
ATOM   20732 C  CB   . THR   D  4  87  ? 7.328   -71.918 -53.241  1.00 101.76 ? 87   THR   D CB   1 
ATOM   20733 O  OG1  . THR   D  4  87  ? 6.666   -70.689 -53.567  1.00 103.46 ? 87   THR   D OG1  1 
ATOM   20734 C  CG2  . THR   D  4  87  ? 7.133   -72.212 -51.760  1.00 101.31 ? 87   THR   D CG2  1 
ATOM   20735 H  H    . THR   D  4  87  ? 9.446   -70.132 -52.782  1.00 116.38 ? 87   THR   D H    1 
ATOM   20736 H  HA   . THR   D  4  87  ? 9.209   -72.693 -53.564  1.00 118.15 ? 87   THR   D HA   1 
ATOM   20737 H  HB   . THR   D  4  87  ? 6.937   -72.646 -53.748  1.00 122.15 ? 87   THR   D HB   1 
ATOM   20738 H  HG1  . THR   D  4  87  ? 5.845   -70.752 -53.401  1.00 124.19 ? 87   THR   D HG1  1 
ATOM   20739 H  HG21 . THR   D  4  87  ? 6.188   -72.306 -51.562  1.00 121.61 ? 87   THR   D HG21 1 
ATOM   20740 H  HG22 . THR   D  4  87  ? 7.588   -73.036 -51.523  1.00 121.61 ? 87   THR   D HG22 1 
ATOM   20741 H  HG23 . THR   D  4  87  ? 7.496   -71.487 -51.227  1.00 121.61 ? 87   THR   D HG23 1 
ATOM   20742 N  N    . SER   D  4  88  ? 8.332   -71.743 -55.969  1.00 103.36 ? 88   SER   D N    1 
ATOM   20743 C  CA   . SER   D  4  88  ? 8.358   -71.157 -57.302  1.00 103.22 ? 88   SER   D CA   1 
ATOM   20744 C  C    . SER   D  4  88  ? 7.494   -69.908 -57.399  1.00 105.16 ? 88   SER   D C    1 
ATOM   20745 O  O    . SER   D  4  88  ? 7.714   -69.086 -58.296  1.00 100.79 ? 88   SER   D O    1 
ATOM   20746 C  CB   . SER   D  4  88  ? 7.895   -72.180 -58.341  1.00 104.18 ? 88   SER   D CB   1 
ATOM   20747 O  OG   . SER   D  4  88  ? 6.539   -72.534 -58.140  1.00 107.36 ? 88   SER   D OG   1 
ATOM   20748 H  H    . SER   D  4  88  ? 7.849   -72.451 -55.898  1.00 124.07 ? 88   SER   D H    1 
ATOM   20749 H  HA   . SER   D  4  88  ? 9.272   -70.912 -57.517  1.00 123.90 ? 88   SER   D HA   1 
ATOM   20750 H  HB2  . SER   D  4  88  ? 7.992   -71.795 -59.226  1.00 125.05 ? 88   SER   D HB2  1 
ATOM   20751 H  HB3  . SER   D  4  88  ? 8.443   -72.977 -58.264  1.00 125.05 ? 88   SER   D HB3  1 
ATOM   20752 H  HG   . SER   D  4  88  ? 6.295   -73.082 -58.728  1.00 128.87 ? 88   SER   D HG   1 
ATOM   20753 N  N    . GLU   D  4  89  ? 6.519   -69.748 -56.501  1.00 108.97 ? 89   GLU   D N    1 
ATOM   20754 C  CA   . GLU   D  4  89  ? 5.701   -68.544 -56.476  1.00 112.67 ? 89   GLU   D CA   1 
ATOM   20755 C  C    . GLU   D  4  89  ? 6.440   -67.351 -55.887  1.00 103.88 ? 89   GLU   D C    1 
ATOM   20756 O  O    . GLU   D  4  89  ? 6.002   -66.211 -56.079  1.00 103.25 ? 89   GLU   D O    1 
ATOM   20757 C  CB   . GLU   D  4  89  ? 4.417   -68.797 -55.681  1.00 122.08 ? 89   GLU   D CB   1 
ATOM   20758 C  CG   . GLU   D  4  89  ? 3.442   -69.745 -56.365  1.00 134.07 ? 89   GLU   D CG   1 
ATOM   20759 C  CD   . GLU   D  4  89  ? 2.218   -69.034 -56.909  1.00 140.73 ? 89   GLU   D CD   1 
ATOM   20760 O  OE1  . GLU   D  4  89  ? 1.386   -68.572 -56.100  1.00 147.59 ? 89   GLU   D OE1  1 
ATOM   20761 O  OE2  . GLU   D  4  89  ? 2.091   -68.931 -58.148  1.00 148.41 ? 89   GLU   D OE2  1 
ATOM   20762 H  H    . GLU   D  4  89  ? 6.315   -70.325 -55.897  1.00 130.80 ? 89   GLU   D H    1 
ATOM   20763 H  HA   . GLU   D  4  89  ? 5.447   -68.319 -57.385  1.00 135.24 ? 89   GLU   D HA   1 
ATOM   20764 H  HB2  . GLU   D  4  89  ? 4.653   -69.184 -54.824  1.00 146.53 ? 89   GLU   D HB2  1 
ATOM   20765 H  HB3  . GLU   D  4  89  ? 3.962   -67.950 -55.549  1.00 146.53 ? 89   GLU   D HB3  1 
ATOM   20766 H  HG2  . GLU   D  4  89  ? 3.891   -70.180 -57.106  1.00 160.92 ? 89   GLU   D HG2  1 
ATOM   20767 H  HG3  . GLU   D  4  89  ? 3.143   -70.407 -55.722  1.00 160.92 ? 89   GLU   D HG3  1 
ATOM   20768 N  N    . ASP   D  4  90  ? 7.542   -67.584 -55.172  1.00 95.49  ? 90   ASP   D N    1 
ATOM   20769 C  CA   . ASP   D  4  90  ? 8.366   -66.494 -54.670  1.00 82.54  ? 90   ASP   D CA   1 
ATOM   20770 C  C    . ASP   D  4  90  ? 9.341   -65.969 -55.715  1.00 76.95  ? 90   ASP   D C    1 
ATOM   20771 O  O    . ASP   D  4  90  ? 9.980   -64.938 -55.477  1.00 72.70  ? 90   ASP   D O    1 
ATOM   20772 C  CB   . ASP   D  4  90  ? 9.139   -66.944 -53.426  1.00 78.41  ? 90   ASP   D CB   1 
ATOM   20773 C  CG   . ASP   D  4  90  ? 8.232   -67.202 -52.238  1.00 77.43  ? 90   ASP   D CG   1 
ATOM   20774 O  OD1  . ASP   D  4  90  ? 7.213   -66.492 -52.100  1.00 78.42  ? 90   ASP   D OD1  1 
ATOM   20775 O  OD2  . ASP   D  4  90  ? 8.537   -68.114 -51.441  1.00 78.32  ? 90   ASP   D OD2  1 
ATOM   20776 H  H    . ASP   D  4  90  ? 7.831   -68.368 -54.967  1.00 114.62 ? 90   ASP   D H    1 
ATOM   20777 H  HA   . ASP   D  4  90  ? 7.787   -65.762 -54.406  1.00 99.08  ? 90   ASP   D HA   1 
ATOM   20778 H  HB2  . ASP   D  4  90  ? 9.611   -67.767 -53.628  1.00 94.13  ? 90   ASP   D HB2  1 
ATOM   20779 H  HB3  . ASP   D  4  90  ? 9.770   -66.251 -53.178  1.00 94.13  ? 90   ASP   D HB3  1 
ATOM   20780 N  N    . SER   D  4  91  ? 9.473   -66.645 -56.855  1.00 77.96  ? 91   SER   D N    1 
ATOM   20781 C  CA   . SER   D  4  91  ? 10.321  -66.149 -57.932  1.00 76.70  ? 91   SER   D CA   1 
ATOM   20782 C  C    . SER   D  4  91  ? 9.725   -64.864 -58.494  1.00 76.82  ? 91   SER   D C    1 
ATOM   20783 O  O    . SER   D  4  91  ? 8.630   -64.878 -59.066  1.00 78.74  ? 91   SER   D O    1 
ATOM   20784 C  CB   . SER   D  4  91  ? 10.457  -67.198 -59.032  1.00 77.46  ? 91   SER   D CB   1 
ATOM   20785 O  OG   . SER   D  4  91  ? 10.899  -68.439 -58.512  1.00 79.21  ? 91   SER   D OG   1 
ATOM   20786 H  H    . SER   D  4  91  ? 9.082   -67.392 -57.027  1.00 93.59  ? 91   SER   D H    1 
ATOM   20787 H  HA   . SER   D  4  91  ? 11.206  -65.962 -57.584  1.00 92.07  ? 91   SER   D HA   1 
ATOM   20788 H  HB2  . SER   D  4  91  ? 9.592   -67.325 -59.453  1.00 92.99  ? 91   SER   D HB2  1 
ATOM   20789 H  HB3  . SER   D  4  91  ? 11.102  -66.885 -59.685  1.00 92.99  ? 91   SER   D HB3  1 
ATOM   20790 H  HG   . SER   D  4  91  ? 10.247  -68.870 -58.203  1.00 95.09  ? 91   SER   D HG   1 
ATOM   20791 N  N    . ALA   D  4  92  ? 10.446  -63.755 -58.337  1.00 73.65  ? 92   ALA   D N    1 
ATOM   20792 C  CA   . ALA   D  4  92  ? 9.942   -62.459 -58.772  1.00 76.43  ? 92   ALA   D CA   1 
ATOM   20793 C  C    . ALA   D  4  92  ? 10.986  -61.371 -58.565  1.00 72.78  ? 92   ALA   D C    1 
ATOM   20794 O  O    . ALA   D  4  92  ? 12.082  -61.640 -58.063  1.00 72.62  ? 92   ALA   D O    1 
ATOM   20795 C  CB   . ALA   D  4  92  ? 8.660   -62.107 -58.014  1.00 80.46  ? 92   ALA   D CB   1 
ATOM   20796 H  H    . ALA   D  4  92  ? 11.229  -63.728 -57.981  1.00 88.41  ? 92   ALA   D H    1 
ATOM   20797 H  HA   . ALA   D  4  92  ? 9.738   -62.505 -59.720  1.00 91.76  ? 92   ALA   D HA   1 
ATOM   20798 H  HB1  . ALA   D  4  92  ? 8.356   -61.230 -58.298  1.00 96.59  ? 92   ALA   D HB1  1 
ATOM   20799 H  HB2  . ALA   D  4  92  ? 7.983   -62.772 -58.213  1.00 96.59  ? 92   ALA   D HB2  1 
ATOM   20800 H  HB3  . ALA   D  4  92  ? 8.848   -62.100 -57.063  1.00 96.59  ? 92   ALA   D HB3  1 
ATOM   20801 N  N    . VAL   D  4  93  ? 10.657  -60.143 -58.953  1.00 70.93  ? 93   VAL   D N    1 
ATOM   20802 C  CA   . VAL   D  4  93  ? 11.483  -58.982 -58.645  1.00 71.05  ? 93   VAL   D CA   1 
ATOM   20803 C  C    . VAL   D  4  93  ? 10.952  -58.351 -57.368  1.00 71.49  ? 93   VAL   D C    1 
ATOM   20804 O  O    . VAL   D  4  93  ? 9.738   -58.177 -57.207  1.00 74.68  ? 93   VAL   D O    1 
ATOM   20805 C  CB   . VAL   D  4  93  ? 11.481  -57.971 -59.803  1.00 69.12  ? 93   VAL   D CB   1 
ATOM   20806 C  CG1  . VAL   D  4  93  ? 12.218  -56.695 -59.400  1.00 62.81  ? 93   VAL   D CG1  1 
ATOM   20807 C  CG2  . VAL   D  4  93  ? 12.116  -58.582 -61.040  1.00 74.62  ? 93   VAL   D CG2  1 
ATOM   20808 H  H    . VAL   D  4  93  ? 9.949   -59.954 -59.403  1.00 85.15  ? 93   VAL   D H    1 
ATOM   20809 H  HA   . VAL   D  4  93  ? 12.399  -59.266 -58.500  1.00 85.29  ? 93   VAL   D HA   1 
ATOM   20810 H  HB   . VAL   D  4  93  ? 10.563  -57.739 -60.015  1.00 82.98  ? 93   VAL   D HB   1 
ATOM   20811 H  HG11 . VAL   D  4  93  ? 12.253  -56.096 -60.163  1.00 75.41  ? 93   VAL   D HG11 1 
ATOM   20812 H  HG12 . VAL   D  4  93  ? 11.740  -56.271 -58.670  1.00 75.41  ? 93   VAL   D HG12 1 
ATOM   20813 H  HG13 . VAL   D  4  93  ? 13.117  -56.925 -59.118  1.00 75.41  ? 93   VAL   D HG13 1 
ATOM   20814 H  HG21 . VAL   D  4  93  ? 12.115  -57.924 -61.753  1.00 89.58  ? 93   VAL   D HG21 1 
ATOM   20815 H  HG22 . VAL   D  4  93  ? 13.027  -58.841 -60.832  1.00 89.58  ? 93   VAL   D HG22 1 
ATOM   20816 H  HG23 . VAL   D  4  93  ? 11.603  -59.361 -61.307  1.00 89.58  ? 93   VAL   D HG23 1 
ATOM   20817 N  N    . TYR   D  4  94  ? 11.859  -58.009 -56.459  1.00 67.91  ? 94   TYR   D N    1 
ATOM   20818 C  CA   . TYR   D  4  94  ? 11.507  -57.420 -55.174  1.00 64.55  ? 94   TYR   D CA   1 
ATOM   20819 C  C    . TYR   D  4  94  ? 12.109  -56.026 -55.096  1.00 63.21  ? 94   TYR   D C    1 
ATOM   20820 O  O    . TYR   D  4  94  ? 13.331  -55.866 -55.178  1.00 60.95  ? 94   TYR   D O    1 
ATOM   20821 C  CB   . TYR   D  4  94  ? 11.995  -58.302 -54.023  1.00 64.95  ? 94   TYR   D CB   1 
ATOM   20822 C  CG   . TYR   D  4  94  ? 11.234  -59.606 -53.916  1.00 68.49  ? 94   TYR   D CG   1 
ATOM   20823 C  CD1  . TYR   D  4  94  ? 10.055  -59.683 -53.188  1.00 69.63  ? 94   TYR   D CD1  1 
ATOM   20824 C  CD2  . TYR   D  4  94  ? 11.686  -60.755 -54.554  1.00 70.82  ? 94   TYR   D CD2  1 
ATOM   20825 C  CE1  . TYR   D  4  94  ? 9.350   -60.868 -53.090  1.00 72.07  ? 94   TYR   D CE1  1 
ATOM   20826 C  CE2  . TYR   D  4  94  ? 10.986  -61.946 -54.463  1.00 73.29  ? 94   TYR   D CE2  1 
ATOM   20827 C  CZ   . TYR   D  4  94  ? 9.817   -61.995 -53.731  1.00 74.85  ? 94   TYR   D CZ   1 
ATOM   20828 O  OH   . TYR   D  4  94  ? 9.114   -63.174 -53.632  1.00 77.95  ? 94   TYR   D OH   1 
ATOM   20829 H  H    . TYR   D  4  94  ? 12.706  -58.111 -56.568  1.00 81.53  ? 94   TYR   D H    1 
ATOM   20830 H  HA   . TYR   D  4  94  ? 10.544  -57.334 -55.100  1.00 77.50  ? 94   TYR   D HA   1 
ATOM   20831 H  HB2  . TYR   D  4  94  ? 12.931  -58.512 -54.161  1.00 77.98  ? 94   TYR   D HB2  1 
ATOM   20832 H  HB3  . TYR   D  4  94  ? 11.882  -57.820 -53.188  1.00 77.98  ? 94   TYR   D HB3  1 
ATOM   20833 H  HD1  . TYR   D  4  94  ? 9.733   -58.924 -52.758  1.00 83.59  ? 94   TYR   D HD1  1 
ATOM   20834 H  HD2  . TYR   D  4  94  ? 12.472  -60.723 -55.051  1.00 85.02  ? 94   TYR   D HD2  1 
ATOM   20835 H  HE1  . TYR   D  4  94  ? 8.564   -60.904 -52.594  1.00 86.53  ? 94   TYR   D HE1  1 
ATOM   20836 H  HE2  . TYR   D  4  94  ? 11.301  -62.708 -54.893  1.00 87.99  ? 94   TYR   D HE2  1 
ATOM   20837 H  HH   . TYR   D  4  94  ? 9.426   -63.740 -54.169  1.00 93.58  ? 94   TYR   D HH   1 
ATOM   20838 N  N    . TYR   D  4  95  ? 11.248  -55.023 -54.949  1.00 66.07  ? 95   TYR   D N    1 
ATOM   20839 C  CA   . TYR   D  4  95  ? 11.658  -53.631 -54.880  1.00 63.71  ? 95   TYR   D CA   1 
ATOM   20840 C  C    . TYR   D  4  95  ? 11.613  -53.132 -53.442  1.00 62.30  ? 95   TYR   D C    1 
ATOM   20841 O  O    . TYR   D  4  95  ? 10.780  -53.563 -52.641  1.00 60.40  ? 95   TYR   D O    1 
ATOM   20842 C  CB   . TYR   D  4  95  ? 10.748  -52.744 -55.736  1.00 60.93  ? 95   TYR   D CB   1 
ATOM   20843 C  CG   . TYR   D  4  95  ? 10.790  -53.009 -57.223  1.00 59.58  ? 95   TYR   D CG   1 
ATOM   20844 C  CD1  . TYR   D  4  95  ? 11.767  -52.432 -58.023  1.00 58.62  ? 95   TYR   D CD1  1 
ATOM   20845 C  CD2  . TYR   D  4  95  ? 9.834   -53.811 -57.832  1.00 62.32  ? 95   TYR   D CD2  1 
ATOM   20846 C  CE1  . TYR   D  4  95  ? 11.801  -52.659 -59.387  1.00 61.60  ? 95   TYR   D CE1  1 
ATOM   20847 C  CE2  . TYR   D  4  95  ? 9.859   -54.044 -59.194  1.00 62.97  ? 95   TYR   D CE2  1 
ATOM   20848 C  CZ   . TYR   D  4  95  ? 10.845  -53.467 -59.966  1.00 62.69  ? 95   TYR   D CZ   1 
ATOM   20849 O  OH   . TYR   D  4  95  ? 10.870  -53.696 -61.323  1.00 66.14  ? 95   TYR   D OH   1 
ATOM   20850 H  H    . TYR   D  4  95  ? 10.397  -55.131 -54.886  1.00 79.33  ? 95   TYR   D H    1 
ATOM   20851 H  HA   . TYR   D  4  95  ? 12.567  -53.559 -55.211  1.00 76.49  ? 95   TYR   D HA   1 
ATOM   20852 H  HB2  . TYR   D  4  95  ? 9.832   -52.877 -55.445  1.00 73.16  ? 95   TYR   D HB2  1 
ATOM   20853 H  HB3  . TYR   D  4  95  ? 11.009  -51.820 -55.600  1.00 73.16  ? 95   TYR   D HB3  1 
ATOM   20854 H  HD1  . TYR   D  4  95  ? 12.410  -51.884 -57.635  1.00 70.38  ? 95   TYR   D HD1  1 
ATOM   20855 H  HD2  . TYR   D  4  95  ? 9.164   -54.197 -57.315  1.00 74.82  ? 95   TYR   D HD2  1 
ATOM   20856 H  HE1  . TYR   D  4  95  ? 12.464  -52.269 -59.910  1.00 73.96  ? 95   TYR   D HE1  1 
ATOM   20857 H  HE2  . TYR   D  4  95  ? 9.215   -54.588 -59.588  1.00 75.60  ? 95   TYR   D HE2  1 
ATOM   20858 H  HH   . TYR   D  4  95  ? 11.104  -52.998 -61.727  1.00 79.41  ? 95   TYR   D HH   1 
ATOM   20859 N  N    . CYS   D  4  96  ? 12.521  -52.217 -53.124  1.00 64.28  ? 96   CYS   D N    1 
ATOM   20860 C  CA   . CYS   D  4  96  ? 12.414  -51.382 -51.938  1.00 65.18  ? 96   CYS   D CA   1 
ATOM   20861 C  C    . CYS   D  4  96  ? 12.064  -49.966 -52.374  1.00 66.28  ? 96   CYS   D C    1 
ATOM   20862 O  O    . CYS   D  4  96  ? 12.458  -49.517 -53.454  1.00 63.11  ? 96   CYS   D O    1 
ATOM   20863 C  CB   . CYS   D  4  96  ? 13.711  -51.379 -51.122  1.00 65.00  ? 96   CYS   D CB   1 
ATOM   20864 S  SG   . CYS   D  4  96  ? 15.172  -50.750 -51.987  1.00 67.67  ? 96   CYS   D SG   1 
ATOM   20865 H  H    . CYS   D  4  96  ? 13.225  -52.058 -53.593  1.00 77.17  ? 96   CYS   D H    1 
ATOM   20866 H  HA   . CYS   D  4  96  ? 11.717  -51.722 -51.354  1.00 78.26  ? 96   CYS   D HA   1 
ATOM   20867 H  HB2  . CYS   D  4  96  ? 13.577  -50.822 -50.339  1.00 78.04  ? 96   CYS   D HB2  1 
ATOM   20868 H  HB3  . CYS   D  4  96  ? 13.904  -52.290 -50.853  1.00 78.04  ? 96   CYS   D HB3  1 
ATOM   20869 N  N    . ALA   D  4  97  ? 11.309  -49.266 -51.531  1.00 70.86  ? 97   ALA   D N    1 
ATOM   20870 C  CA   . ALA   D  4  97  ? 10.857  -47.923 -51.868  1.00 71.23  ? 97   ALA   D CA   1 
ATOM   20871 C  C    . ALA   D  4  97  ? 10.684  -47.117 -50.593  1.00 68.60  ? 97   ALA   D C    1 
ATOM   20872 O  O    . ALA   D  4  97  ? 10.056  -47.586 -49.639  1.00 73.51  ? 97   ALA   D O    1 
ATOM   20873 C  CB   . ALA   D  4  97  ? 9.541   -47.966 -52.655  1.00 72.60  ? 97   ALA   D CB   1 
ATOM   20874 H  H    . ALA   D  4  97  ? 11.047  -49.547 -50.762  1.00 85.07  ? 97   ALA   D H    1 
ATOM   20875 H  HA   . ALA   D  4  97  ? 11.529  -47.485 -52.413  1.00 85.52  ? 97   ALA   D HA   1 
ATOM   20876 H  HB1  . ALA   D  4  97  ? 9.267   -47.059 -52.860  1.00 87.15  ? 97   ALA   D HB1  1 
ATOM   20877 H  HB2  . ALA   D  4  97  ? 9.681   -48.463 -53.476  1.00 87.15  ? 97   ALA   D HB2  1 
ATOM   20878 H  HB3  . ALA   D  4  97  ? 8.864   -48.403 -52.115  1.00 87.15  ? 97   ALA   D HB3  1 
ATOM   20879 N  N    . SER   D  4  98  ? 11.241  -45.909 -50.582  1.00 63.84  ? 98   SER   D N    1 
ATOM   20880 C  CA   . SER   D  4  98  ? 11.119  -45.046 -49.422  1.00 59.96  ? 98   SER   D CA   1 
ATOM   20881 C  C    . SER   D  4  98  ? 9.706   -44.473 -49.337  1.00 57.96  ? 98   SER   D C    1 
ATOM   20882 O  O    . SER   D  4  98  ? 8.913   -44.538 -50.281  1.00 58.57  ? 98   SER   D O    1 
ATOM   20883 C  CB   . SER   D  4  98  ? 12.150  -43.920 -49.477  1.00 60.60  ? 98   SER   D CB   1 
ATOM   20884 O  OG   . SER   D  4  98  ? 11.968  -43.111 -50.625  1.00 62.19  ? 98   SER   D OG   1 
ATOM   20885 H  H    . SER   D  4  98  ? 11.692  -45.572 -51.232  1.00 76.65  ? 98   SER   D H    1 
ATOM   20886 H  HA   . SER   D  4  98  ? 11.286  -45.562 -48.619  1.00 71.98  ? 98   SER   D HA   1 
ATOM   20887 H  HB2  . SER   D  4  98  ? 12.055  -43.368 -48.686  1.00 72.76  ? 98   SER   D HB2  1 
ATOM   20888 H  HB3  . SER   D  4  98  ? 13.038  -44.309 -49.506  1.00 72.76  ? 98   SER   D HB3  1 
ATOM   20889 H  HG   . SER   D  4  98  ? 11.262  -42.661 -50.550  1.00 74.67  ? 98   SER   D HG   1 
ATOM   20890 N  N    . PHE   D  4  99  ? 9.401   -43.902 -48.180  1.00 53.60  ? 99   PHE   D N    1 
ATOM   20891 C  CA   . PHE   D  4  99  ? 8.065   -43.419 -47.858  1.00 51.03  ? 99   PHE   D CA   1 
ATOM   20892 C  C    . PHE   D  4  99  ? 8.009   -41.918 -48.105  1.00 54.52  ? 99   PHE   D C    1 
ATOM   20893 O  O    . PHE   D  4  99  ? 8.723   -41.151 -47.450  1.00 56.05  ? 99   PHE   D O    1 
ATOM   20894 C  CB   . PHE   D  4  99  ? 7.735   -43.743 -46.401  1.00 56.42  ? 99   PHE   D CB   1 
ATOM   20895 C  CG   . PHE   D  4  99  ? 6.270   -43.659 -46.053  1.00 57.23  ? 99   PHE   D CG   1 
ATOM   20896 C  CD1  . PHE   D  4  99  ? 5.282   -43.753 -47.021  1.00 58.25  ? 99   PHE   D CD1  1 
ATOM   20897 C  CD2  . PHE   D  4  99  ? 5.887   -43.494 -44.732  1.00 57.85  ? 99   PHE   D CD2  1 
ATOM   20898 C  CE1  . PHE   D  4  99  ? 3.946   -43.681 -46.676  1.00 59.91  ? 99   PHE   D CE1  1 
ATOM   20899 C  CE2  . PHE   D  4  99  ? 4.556   -43.420 -44.382  1.00 59.88  ? 99   PHE   D CE2  1 
ATOM   20900 C  CZ   . PHE   D  4  99  ? 3.583   -43.513 -45.354  1.00 61.60  ? 99   PHE   D CZ   1 
ATOM   20901 H  H    . PHE   D  4  99  ? 9.968   -43.780 -47.545  1.00 64.35  ? 99   PHE   D H    1 
ATOM   20902 H  HA   . PHE   D  4  99  ? 7.406   -43.842 -48.432  1.00 61.27  ? 99   PHE   D HA   1 
ATOM   20903 H  HB2  . PHE   D  4  99  ? 8.028   -44.648 -46.213  1.00 67.74  ? 99   PHE   D HB2  1 
ATOM   20904 H  HB3  . PHE   D  4  99  ? 8.207   -43.116 -45.832  1.00 67.74  ? 99   PHE   D HB3  1 
ATOM   20905 H  HD1  . PHE   D  4  99  ? 5.521   -43.866 -47.913  1.00 69.94  ? 99   PHE   D HD1  1 
ATOM   20906 H  HD2  . PHE   D  4  99  ? 6.538   -43.433 -44.071  1.00 69.46  ? 99   PHE   D HD2  1 
ATOM   20907 H  HE1  . PHE   D  4  99  ? 3.291   -43.745 -47.333  1.00 71.93  ? 99   PHE   D HE1  1 
ATOM   20908 H  HE2  . PHE   D  4  99  ? 4.314   -43.307 -43.491  1.00 71.89  ? 99   PHE   D HE2  1 
ATOM   20909 H  HZ   . PHE   D  4  99  ? 2.685   -43.464 -45.120  1.00 73.96  ? 99   PHE   D HZ   1 
ATOM   20910 N  N    . LEU   D  4  100 ? 7.169   -41.500 -49.054  1.00 55.98  ? 100  LEU   D N    1 
ATOM   20911 C  CA   . LEU   D  4  100 ? 6.966   -40.072 -49.261  1.00 55.80  ? 100  LEU   D CA   1 
ATOM   20912 C  C    . LEU   D  4  100 ? 6.249   -39.439 -48.080  1.00 56.74  ? 100  LEU   D C    1 
ATOM   20913 O  O    . LEU   D  4  100 ? 6.527   -38.288 -47.725  1.00 58.01  ? 100  LEU   D O    1 
ATOM   20914 C  CB   . LEU   D  4  100 ? 6.152   -39.822 -50.534  1.00 55.90  ? 100  LEU   D CB   1 
ATOM   20915 C  CG   . LEU   D  4  100 ? 5.824   -38.360 -50.873  1.00 54.73  ? 100  LEU   D CG   1 
ATOM   20916 C  CD1  . LEU   D  4  100 ? 7.090   -37.531 -51.042  1.00 57.65  ? 100  LEU   D CD1  1 
ATOM   20917 C  CD2  . LEU   D  4  100 ? 4.970   -38.270 -52.133  1.00 57.84  ? 100  LEU   D CD2  1 
ATOM   20918 H  H    . LEU   D  4  100 ? 6.717   -42.012 -49.577  1.00 67.22  ? 100  LEU   D H    1 
ATOM   20919 H  HA   . LEU   D  4  100 ? 7.835   -39.655 -49.367  1.00 66.99  ? 100  LEU   D HA   1 
ATOM   20920 H  HB2  . LEU   D  4  100 ? 6.651   -40.181 -51.284  1.00 67.11  ? 100  LEU   D HB2  1 
ATOM   20921 H  HB3  . LEU   D  4  100 ? 5.306   -40.289 -50.445  1.00 67.11  ? 100  LEU   D HB3  1 
ATOM   20922 H  HG   . LEU   D  4  100 ? 5.320   -37.989 -50.132  1.00 65.71  ? 100  LEU   D HG   1 
ATOM   20923 H  HD11 . LEU   D  4  100 ? 6.917   -36.626 -50.739  1.00 69.22  ? 100  LEU   D HD11 1 
ATOM   20924 H  HD12 . LEU   D  4  100 ? 7.800   -37.928 -50.513  1.00 69.22  ? 100  LEU   D HD12 1 
ATOM   20925 H  HD13 . LEU   D  4  100 ? 7.339   -37.524 -51.979  1.00 69.22  ? 100  LEU   D HD13 1 
ATOM   20926 H  HD21 . LEU   D  4  100 ? 4.877   -37.339 -52.385  1.00 69.44  ? 100  LEU   D HD21 1 
ATOM   20927 H  HD22 . LEU   D  4  100 ? 5.406   -38.764 -52.845  1.00 69.44  ? 100  LEU   D HD22 1 
ATOM   20928 H  HD23 . LEU   D  4  100 ? 4.098   -38.653 -51.950  1.00 69.44  ? 100  LEU   D HD23 1 
ATOM   20929 N  N    . GLY   D  4  101 ? 5.361   -40.189 -47.444  1.00 55.30  ? 101  GLY   D N    1 
ATOM   20930 C  CA   . GLY   D  4  101 ? 4.224   -39.621 -46.754  1.00 57.02  ? 101  GLY   D CA   1 
ATOM   20931 C  C    . GLY   D  4  101 ? 3.009   -39.655 -47.660  1.00 55.27  ? 101  GLY   D C    1 
ATOM   20932 O  O    . GLY   D  4  101 ? 3.065   -40.079 -48.818  1.00 52.51  ? 101  GLY   D O    1 
ATOM   20933 H  H    . GLY   D  4  101 ? 5.400   -41.047 -47.399  1.00 66.40  ? 101  GLY   D H    1 
ATOM   20934 H  HA2  . GLY   D  4  101 ? 4.035   -40.132 -45.951  1.00 68.46  ? 101  GLY   D HA2  1 
ATOM   20935 H  HA3  . GLY   D  4  101 ? 4.410   -38.702 -46.507  1.00 68.46  ? 101  GLY   D HA3  1 
ATOM   20936 N  N    . ARG   D  4  102 ? 1.886   -39.196 -47.116  1.00 56.31  ? 102  ARG   D N    1 
ATOM   20937 C  CA   . ARG   D  4  102 ? 0.626   -39.162 -47.859  1.00 59.16  ? 102  ARG   D CA   1 
ATOM   20938 C  C    . ARG   D  4  102 ? 0.331   -40.509 -48.517  1.00 58.91  ? 102  ARG   D C    1 
ATOM   20939 O  O    . ARG   D  4  102 ? -0.222  -40.574 -49.619  1.00 58.19  ? 102  ARG   D O    1 
ATOM   20940 C  CB   . ARG   D  4  102 ? 0.630   -38.054 -48.916  1.00 59.81  ? 102  ARG   D CB   1 
ATOM   20941 C  CG   . ARG   D  4  102 ? 1.472   -36.829 -48.588  1.00 56.22  ? 102  ARG   D CG   1 
ATOM   20942 C  CD   . ARG   D  4  102 ? 1.063   -36.168 -47.283  1.00 56.94  ? 102  ARG   D CD   1 
ATOM   20943 N  NE   . ARG   D  4  102 ? -0.386  -36.072 -47.123  1.00 58.62  ? 102  ARG   D NE   1 
ATOM   20944 C  CZ   . ARG   D  4  102 ? -1.154  -35.165 -47.720  1.00 60.47  ? 102  ARG   D CZ   1 
ATOM   20945 N  NH1  . ARG   D  4  102 ? -2.462  -35.163 -47.501  1.00 63.96  ? 102  ARG   D NH1  1 
ATOM   20946 N  NH2  . ARG   D  4  102 ? -0.624  -34.267 -48.540  1.00 59.59  ? 102  ARG   D NH2  1 
ATOM   20947 H  H    . ARG   D  4  102 ? 1.825   -38.896 -46.312  1.00 67.61  ? 102  ARG   D H    1 
ATOM   20948 H  HA   . ARG   D  4  102 ? -0.086  -38.975 -47.226  1.00 71.02  ? 102  ARG   D HA   1 
ATOM   20949 H  HB2  . ARG   D  4  102 ? 0.973   -38.426 -49.744  1.00 71.81  ? 102  ARG   D HB2  1 
ATOM   20950 H  HB3  . ARG   D  4  102 ? -0.283  -37.751 -49.041  1.00 71.81  ? 102  ARG   D HB3  1 
ATOM   20951 H  HG2  . ARG   D  4  102 ? 2.401   -37.095 -48.511  1.00 67.49  ? 102  ARG   D HG2  1 
ATOM   20952 H  HG3  . ARG   D  4  102 ? 1.371   -36.176 -49.299  1.00 67.49  ? 102  ARG   D HG3  1 
ATOM   20953 H  HD2  . ARG   D  4  102 ? 1.413   -36.688 -46.543  1.00 68.36  ? 102  ARG   D HD2  1 
ATOM   20954 H  HD3  . ARG   D  4  102 ? 1.427   -35.269 -47.257  1.00 68.36  ? 102  ARG   D HD3  1 
ATOM   20955 H  HE   . ARG   D  4  102 ? -0.769  -36.642 -46.606  1.00 70.38  ? 102  ARG   D HE   1 
ATOM   20956 H  HH11 . ARG   D  4  102 ? -2.812  -35.746 -46.975  1.00 76.78  ? 102  ARG   D HH11 1 
ATOM   20957 H  HH12 . ARG   D  4  102 ? -2.962  -34.577 -47.886  1.00 76.78  ? 102  ARG   D HH12 1 
ATOM   20958 H  HH21 . ARG   D  4  102 ? 0.223   -34.269 -48.689  1.00 71.54  ? 102  ARG   D HH21 1 
ATOM   20959 H  HH22 . ARG   D  4  102 ? -1.127  -33.684 -48.922  1.00 71.54  ? 102  ARG   D HH22 1 
ATOM   20960 N  N    . GLY   D  4  103 ? 0.711   -41.596 -47.853  1.00 60.06  ? 103  GLY   D N    1 
ATOM   20961 C  CA   . GLY   D  4  103 ? 0.422   -42.921 -48.375  1.00 56.47  ? 103  GLY   D CA   1 
ATOM   20962 C  C    . GLY   D  4  103 ? 1.015   -43.195 -49.738  1.00 54.20  ? 103  GLY   D C    1 
ATOM   20963 O  O    . GLY   D  4  103 ? 0.441   -43.968 -50.513  1.00 55.10  ? 103  GLY   D O    1 
ATOM   20964 H  H    . GLY   D  4  103 ? 1.134   -41.592 -47.105  1.00 72.11  ? 103  GLY   D H    1 
ATOM   20965 H  HA2  . GLY   D  4  103 ? 0.772   -43.584 -47.759  1.00 67.81  ? 103  GLY   D HA2  1 
ATOM   20966 H  HA3  . GLY   D  4  103 ? -0.540  -43.028 -48.442  1.00 67.81  ? 103  GLY   D HA3  1 
ATOM   20967 N  N    . ALA   D  4  104 ? 2.154   -42.581 -50.055  1.00 55.29  ? 104  ALA   D N    1 
ATOM   20968 C  CA   . ALA   D  4  104 ? 2.827   -42.766 -51.331  1.00 54.59  ? 104  ALA   D CA   1 
ATOM   20969 C  C    . ALA   D  4  104 ? 4.288   -43.114 -51.082  1.00 52.19  ? 104  ALA   D C    1 
ATOM   20970 O  O    . ALA   D  4  104 ? 4.815   -42.920 -49.983  1.00 54.08  ? 104  ALA   D O    1 
ATOM   20971 C  CB   . ALA   D  4  104 ? 2.719   -41.510 -52.209  1.00 56.91  ? 104  ALA   D CB   1 
ATOM   20972 H  H    . ALA   D  4  104 ? 2.564   -42.038 -49.529  1.00 66.39  ? 104  ALA   D H    1 
ATOM   20973 H  HA   . ALA   D  4  104 ? 2.420   -43.503 -51.813  1.00 65.54  ? 104  ALA   D HA   1 
ATOM   20974 H  HB1  . ALA   D  4  104 ? 3.120   -41.693 -53.073  1.00 68.33  ? 104  ALA   D HB1  1 
ATOM   20975 H  HB2  . ALA   D  4  104 ? 1.783   -41.281 -52.319  1.00 68.33  ? 104  ALA   D HB2  1 
ATOM   20976 H  HB3  . ALA   D  4  104 ? 3.189   -40.780 -51.775  1.00 68.33  ? 104  ALA   D HB3  1 
ATOM   20977 N  N    . MET   D  4  105 ? 4.943   -43.635 -52.119  1.00 52.87  ? 105  MET   D N    1 
ATOM   20978 C  CA   . MET   D  4  105 ? 6.340   -44.063 -52.043  1.00 58.85  ? 105  MET   D CA   1 
ATOM   20979 C  C    . MET   D  4  105 ? 7.111   -43.362 -53.154  1.00 59.91  ? 105  MET   D C    1 
ATOM   20980 O  O    . MET   D  4  105 ? 6.892   -43.643 -54.337  1.00 61.17  ? 105  MET   D O    1 
ATOM   20981 C  CB   . MET   D  4  105 ? 6.442   -45.585 -52.159  1.00 62.58  ? 105  MET   D CB   1 
ATOM   20982 C  CG   . MET   D  4  105 ? 5.726   -46.325 -51.029  1.00 64.12  ? 105  MET   D CG   1 
ATOM   20983 S  SD   . MET   D  4  105 ? 5.242   -48.017 -51.436  1.00 65.69  ? 105  MET   D SD   1 
ATOM   20984 C  CE   . MET   D  4  105 ? 3.819   -47.733 -52.487  1.00 66.09  ? 105  MET   D CE   1 
ATOM   20985 H  H    . MET   D  4  105 ? 4.592   -43.753 -52.894  1.00 63.49  ? 105  MET   D H    1 
ATOM   20986 H  HA   . MET   D  4  105 ? 6.720   -43.801 -51.190  1.00 70.65  ? 105  MET   D HA   1 
ATOM   20987 H  HB2  . MET   D  4  105 ? 6.043   -45.863 -52.998  1.00 75.13  ? 105  MET   D HB2  1 
ATOM   20988 H  HB3  . MET   D  4  105 ? 7.378   -45.839 -52.136  1.00 75.13  ? 105  MET   D HB3  1 
ATOM   20989 H  HG2  . MET   D  4  105 ? 6.318   -46.366 -50.262  1.00 76.98  ? 105  MET   D HG2  1 
ATOM   20990 H  HG3  . MET   D  4  105 ? 4.920   -45.837 -50.800  1.00 76.98  ? 105  MET   D HG3  1 
ATOM   20991 H  HE1  . MET   D  4  105 ? 3.364   -48.577 -52.637  1.00 79.34  ? 105  MET   D HE1  1 
ATOM   20992 H  HE2  . MET   D  4  105 ? 3.221   -47.109 -52.047  1.00 79.34  ? 105  MET   D HE2  1 
ATOM   20993 H  HE3  . MET   D  4  105 ? 4.119   -47.364 -53.332  1.00 79.34  ? 105  MET   D HE3  1 
ATOM   20994 N  N    . ASP   D  4  106 ? 8.023   -42.461 -52.778  1.00 59.81  ? 106  ASP   D N    1 
ATOM   20995 C  CA   . ASP   D  4  106 ? 8.579   -41.515 -53.741  1.00 60.90  ? 106  ASP   D CA   1 
ATOM   20996 C  C    . ASP   D  4  106 ? 9.770   -42.055 -54.531  1.00 57.30  ? 106  ASP   D C    1 
ATOM   20997 O  O    . ASP   D  4  106 ? 9.906   -41.731 -55.715  1.00 56.60  ? 106  ASP   D O    1 
ATOM   20998 C  CB   . ASP   D  4  106 ? 8.981   -40.209 -53.038  1.00 61.98  ? 106  ASP   D CB   1 
ATOM   20999 C  CG   . ASP   D  4  106 ? 9.730   -40.440 -51.739  1.00 61.48  ? 106  ASP   D CG   1 
ATOM   21000 O  OD1  . ASP   D  4  106 ? 9.976   -41.612 -51.385  1.00 62.25  ? 106  ASP   D OD1  1 
ATOM   21001 O  OD2  . ASP   D  4  106 ? 10.066  -39.443 -51.067  1.00 60.04  ? 106  ASP   D OD2  1 
ATOM   21002 H  H    . ASP   D  4  106 ? 8.332   -42.381 -51.979  1.00 71.81  ? 106  ASP   D H    1 
ATOM   21003 H  HA   . ASP   D  4  106 ? 7.879   -41.318 -54.384  1.00 73.11  ? 106  ASP   D HA   1 
ATOM   21004 H  HB2  . ASP   D  4  106 ? 9.558   -39.699 -53.628  1.00 74.42  ? 106  ASP   D HB2  1 
ATOM   21005 H  HB3  . ASP   D  4  106 ? 8.181   -39.701 -52.835  1.00 74.42  ? 106  ASP   D HB3  1 
ATOM   21006 N  N    . TYR   D  4  107 ? 10.639  -42.864 -53.927  1.00 55.76  ? 107  TYR   D N    1 
ATOM   21007 C  CA   . TYR   D  4  107 ? 11.836  -43.343 -54.611  1.00 57.10  ? 107  TYR   D CA   1 
ATOM   21008 C  C    . TYR   D  4  107 ? 11.932  -44.858 -54.502  1.00 61.49  ? 107  TYR   D C    1 
ATOM   21009 O  O    . TYR   D  4  107 ? 11.787  -45.416 -53.410  1.00 63.63  ? 107  TYR   D O    1 
ATOM   21010 C  CB   . TYR   D  4  107 ? 13.094  -42.677 -54.042  1.00 53.59  ? 107  TYR   D CB   1 
ATOM   21011 C  CG   . TYR   D  4  107 ? 13.100  -41.173 -54.219  1.00 52.40  ? 107  TYR   D CG   1 
ATOM   21012 C  CD1  . TYR   D  4  107 ? 13.477  -40.597 -55.426  1.00 52.66  ? 107  TYR   D CD1  1 
ATOM   21013 C  CD2  . TYR   D  4  107 ? 12.719  -40.331 -53.183  1.00 52.93  ? 107  TYR   D CD2  1 
ATOM   21014 C  CE1  . TYR   D  4  107 ? 13.479  -39.223 -55.593  1.00 54.77  ? 107  TYR   D CE1  1 
ATOM   21015 C  CE2  . TYR   D  4  107 ? 12.718  -38.957 -53.340  1.00 56.29  ? 107  TYR   D CE2  1 
ATOM   21016 C  CZ   . TYR   D  4  107 ? 13.098  -38.409 -54.547  1.00 56.37  ? 107  TYR   D CZ   1 
ATOM   21017 O  OH   . TYR   D  4  107 ? 13.099  -37.042 -54.707  1.00 57.96  ? 107  TYR   D OH   1 
ATOM   21018 H  H    . TYR   D  4  107 ? 10.556  -43.148 -53.119  1.00 66.94  ? 107  TYR   D H    1 
ATOM   21019 H  HA   . TYR   D  4  107 ? 11.772  -43.129 -55.555  1.00 68.56  ? 107  TYR   D HA   1 
ATOM   21020 H  HB2  . TYR   D  4  107 ? 13.148  -42.867 -53.093  1.00 64.35  ? 107  TYR   D HB2  1 
ATOM   21021 H  HB3  . TYR   D  4  107 ? 13.872  -43.035 -54.497  1.00 64.35  ? 107  TYR   D HB3  1 
ATOM   21022 H  HD1  . TYR   D  4  107 ? 13.733  -41.143 -56.133  1.00 63.22  ? 107  TYR   D HD1  1 
ATOM   21023 H  HD2  . TYR   D  4  107 ? 12.460  -40.698 -52.368  1.00 63.55  ? 107  TYR   D HD2  1 
ATOM   21024 H  HE1  . TYR   D  4  107 ? 13.735  -38.851 -56.406  1.00 65.76  ? 107  TYR   D HE1  1 
ATOM   21025 H  HE2  . TYR   D  4  107 ? 12.462  -38.406 -52.636  1.00 67.59  ? 107  TYR   D HE2  1 
ATOM   21026 H  HH   . TYR   D  4  107 ? 12.807  -36.671 -54.012  1.00 69.59  ? 107  TYR   D HH   1 
ATOM   21027 N  N    . TRP   D  4  108 ? 12.186  -45.512 -55.636  1.00 62.54  ? 108  TRP   D N    1 
ATOM   21028 C  CA   . TRP   D  4  108 ? 12.218  -46.962 -55.746  1.00 60.59  ? 108  TRP   D CA   1 
ATOM   21029 C  C    . TRP   D  4  108 ? 13.609  -47.433 -56.146  1.00 57.35  ? 108  TRP   D C    1 
ATOM   21030 O  O    . TRP   D  4  108 ? 14.305  -46.768 -56.918  1.00 55.71  ? 108  TRP   D O    1 
ATOM   21031 C  CB   . TRP   D  4  108 ? 11.214  -47.458 -56.795  1.00 63.01  ? 108  TRP   D CB   1 
ATOM   21032 C  CG   . TRP   D  4  108 ? 9.778   -47.361 -56.391  1.00 61.50  ? 108  TRP   D CG   1 
ATOM   21033 C  CD1  . TRP   D  4  108 ? 9.110   -46.243 -55.985  1.00 60.49  ? 108  TRP   D CD1  1 
ATOM   21034 C  CD2  . TRP   D  4  108 ? 8.821   -48.427 -56.382  1.00 60.16  ? 108  TRP   D CD2  1 
ATOM   21035 N  NE1  . TRP   D  4  108 ? 7.798   -46.550 -55.712  1.00 60.87  ? 108  TRP   D NE1  1 
ATOM   21036 C  CE2  . TRP   D  4  108 ? 7.596   -47.884 -55.949  1.00 60.56  ? 108  TRP   D CE2  1 
ATOM   21037 C  CE3  . TRP   D  4  108 ? 8.884   -49.788 -56.694  1.00 60.58  ? 108  TRP   D CE3  1 
ATOM   21038 C  CZ2  . TRP   D  4  108 ? 6.443   -48.656 -55.819  1.00 61.22  ? 108  TRP   D CZ2  1 
ATOM   21039 C  CZ3  . TRP   D  4  108 ? 7.740   -50.552 -56.563  1.00 67.54  ? 108  TRP   D CZ3  1 
ATOM   21040 C  CH2  . TRP   D  4  108 ? 6.536   -49.984 -56.131  1.00 67.63  ? 108  TRP   D CH2  1 
ATOM   21041 H  H    . TRP   D  4  108 ? 12.349  -45.117 -56.383  1.00 75.09  ? 108  TRP   D H    1 
ATOM   21042 H  HA   . TRP   D  4  108 ? 11.996  -47.346 -54.883  1.00 72.75  ? 108  TRP   D HA   1 
ATOM   21043 H  HB2  . TRP   D  4  108 ? 11.325  -46.930 -57.601  1.00 75.64  ? 108  TRP   D HB2  1 
ATOM   21044 H  HB3  . TRP   D  4  108 ? 11.400  -48.391 -56.981  1.00 75.64  ? 108  TRP   D HB3  1 
ATOM   21045 H  HD1  . TRP   D  4  108 ? 9.487   -45.397 -55.904  1.00 72.62  ? 108  TRP   D HD1  1 
ATOM   21046 H  HE1  . TRP   D  4  108 ? 7.201   -45.995 -55.437  1.00 73.08  ? 108  TRP   D HE1  1 
ATOM   21047 H  HE3  . TRP   D  4  108 ? 9.681   -50.172 -56.983  1.00 72.74  ? 108  TRP   D HE3  1 
ATOM   21048 H  HZ2  . TRP   D  4  108 ? 5.642   -48.282 -55.530  1.00 73.50  ? 108  TRP   D HZ2  1 
ATOM   21049 H  HZ3  . TRP   D  4  108 ? 7.771   -51.459 -56.766  1.00 81.08  ? 108  TRP   D HZ3  1 
ATOM   21050 H  HH2  . TRP   D  4  108 ? 5.781   -50.522 -56.055  1.00 81.19  ? 108  TRP   D HH2  1 
ATOM   21051 N  N    . GLY   D  4  109 ? 14.004  -48.600 -55.624  1.00 57.04  ? 109  GLY   D N    1 
ATOM   21052 C  CA   . GLY   D  4  109 ? 15.220  -49.246 -56.070  1.00 54.64  ? 109  GLY   D CA   1 
ATOM   21053 C  C    . GLY   D  4  109 ? 15.034  -49.963 -57.397  1.00 54.28  ? 109  GLY   D C    1 
ATOM   21054 O  O    . GLY   D  4  109 ? 13.930  -50.082 -57.927  1.00 55.10  ? 109  GLY   D O    1 
ATOM   21055 H  H    . GLY   D  4  109 ? 13.580  -49.030 -55.011  1.00 68.49  ? 109  GLY   D H    1 
ATOM   21056 H  HA2  . GLY   D  4  109 ? 15.918  -48.580 -56.176  1.00 65.60  ? 109  GLY   D HA2  1 
ATOM   21057 H  HA3  . GLY   D  4  109 ? 15.502  -49.896 -55.407  1.00 65.60  ? 109  GLY   D HA3  1 
ATOM   21058 N  N    . GLN   D  4  110 ? 16.151  -50.457 -57.939  1.00 58.72  ? 110  GLN   D N    1 
ATOM   21059 C  CA   . GLN   D  4  110 ? 16.120  -51.068 -59.263  1.00 61.80  ? 110  GLN   D CA   1 
ATOM   21060 C  C    . GLN   D  4  110 ? 15.436  -52.429 -59.265  1.00 64.08  ? 110  GLN   D C    1 
ATOM   21061 O  O    . GLN   D  4  110 ? 15.051  -52.911 -60.335  1.00 69.23  ? 110  GLN   D O    1 
ATOM   21062 C  CB   . GLN   D  4  110 ? 17.542  -51.207 -59.820  1.00 66.76  ? 110  GLN   D CB   1 
ATOM   21063 C  CG   . GLN   D  4  110 ? 18.362  -52.378 -59.262  1.00 74.20  ? 110  GLN   D CG   1 
ATOM   21064 C  CD   . GLN   D  4  110 ? 19.131  -52.024 -58.007  1.00 80.76  ? 110  GLN   D CD   1 
ATOM   21065 O  OE1  . GLN   D  4  110 ? 18.928  -50.964 -57.415  1.00 74.21  ? 110  GLN   D OE1  1 
ATOM   21066 N  NE2  . GLN   D  4  110 ? 20.024  -52.916 -57.593  1.00 90.63  ? 110  GLN   D NE2  1 
ATOM   21067 H  H    . GLN   D  4  110 ? 16.925  -50.451 -57.564  1.00 70.51  ? 110  GLN   D H    1 
ATOM   21068 H  HA   . GLN   D  4  110 ? 15.621  -50.482 -59.853  1.00 74.20  ? 110  GLN   D HA   1 
ATOM   21069 H  HB2  . GLN   D  4  110 ? 17.482  -51.329 -60.781  1.00 80.15  ? 110  GLN   D HB2  1 
ATOM   21070 H  HB3  . GLN   D  4  110 ? 18.029  -50.393 -59.619  1.00 80.15  ? 110  GLN   D HB3  1 
ATOM   21071 H  HG2  . GLN   D  4  110 ? 17.761  -53.109 -59.047  1.00 89.07  ? 110  GLN   D HG2  1 
ATOM   21072 H  HG3  . GLN   D  4  110 ? 19.002  -52.662 -59.933  1.00 89.07  ? 110  GLN   D HG3  1 
ATOM   21073 H  HE21 . GLN   D  4  110 ? 20.138  -53.646 -58.033  1.00 108.80 ? 110  GLN   D HE21 1 
ATOM   21074 H  HE22 . GLN   D  4  110 ? 20.487  -52.764 -56.885  1.00 108.80 ? 110  GLN   D HE22 1 
ATOM   21075 N  N    . GLY   D  4  111 ? 15.294  -53.063 -58.104  1.00 63.62  ? 111  GLY   D N    1 
ATOM   21076 C  CA   . GLY   D  4  111 ? 14.713  -54.387 -58.037  1.00 60.65  ? 111  GLY   D CA   1 
ATOM   21077 C  C    . GLY   D  4  111 ? 15.755  -55.482 -57.950  1.00 58.14  ? 111  GLY   D C    1 
ATOM   21078 O  O    . GLY   D  4  111 ? 16.816  -55.396 -58.575  1.00 59.28  ? 111  GLY   D O    1 
ATOM   21079 H  H    . GLY   D  4  111 ? 15.529  -52.741 -57.342  1.00 76.38  ? 111  GLY   D H    1 
ATOM   21080 H  HA2  . GLY   D  4  111 ? 14.144  -54.446 -57.253  1.00 72.81  ? 111  GLY   D HA2  1 
ATOM   21081 H  HA3  . GLY   D  4  111 ? 14.175  -54.541 -58.830  1.00 72.81  ? 111  GLY   D HA3  1 
ATOM   21082 N  N    . THR   D  4  112 ? 15.457  -56.519 -57.171  1.00 78.08  ? 112  THR   D N    1 
ATOM   21083 C  CA   . THR   D  4  112 ? 16.326  -57.679 -57.006  1.00 78.89  ? 112  THR   D CA   1 
ATOM   21084 C  C    . THR   D  4  112 ? 15.553  -58.906 -57.468  1.00 77.19  ? 112  THR   D C    1 
ATOM   21085 O  O    . THR   D  4  112 ? 14.597  -59.326 -56.807  1.00 77.40  ? 112  THR   D O    1 
ATOM   21086 C  CB   . THR   D  4  112 ? 16.774  -57.830 -55.551  1.00 80.95  ? 112  THR   D CB   1 
ATOM   21087 O  OG1  . THR   D  4  112 ? 17.697  -56.786 -55.217  1.00 84.25  ? 112  THR   D OG1  1 
ATOM   21088 C  CG2  . THR   D  4  112 ? 17.435  -59.186 -55.321  1.00 69.68  ? 112  THR   D CG2  1 
ATOM   21089 H  H    . THR   D  4  112 ? 14.731  -56.574 -56.713  1.00 93.73  ? 112  THR   D H    1 
ATOM   21090 H  HA   . THR   D  4  112 ? 17.117  -57.577 -57.558  1.00 94.71  ? 112  THR   D HA   1 
ATOM   21091 H  HB   . THR   D  4  112 ? 15.998  -57.772 -54.972  1.00 97.17  ? 112  THR   D HB   1 
ATOM   21092 H  HG1  . THR   D  4  112 ? 18.435  -56.923 -55.594  1.00 101.14 ? 112  THR   D HG1  1 
ATOM   21093 H  HG21 . THR   D  4  112 ? 17.779  -59.238 -54.415  1.00 83.43  ? 112  THR   D HG21 1 
ATOM   21094 H  HG22 . THR   D  4  112 ? 16.789  -59.897 -55.453  1.00 83.43  ? 112  THR   D HG22 1 
ATOM   21095 H  HG23 . THR   D  4  112 ? 18.168  -59.308 -55.944  1.00 83.43  ? 112  THR   D HG23 1 
ATOM   21096 N  N    . SER   D  4  113 ? 15.960  -59.479 -58.596  1.00 78.62  ? 113  SER   D N    1 
ATOM   21097 C  CA   . SER   D  4  113 ? 15.304  -60.681 -59.087  1.00 79.30  ? 113  SER   D CA   1 
ATOM   21098 C  C    . SER   D  4  113 ? 15.659  -61.869 -58.204  1.00 77.10  ? 113  SER   D C    1 
ATOM   21099 O  O    . SER   D  4  113 ? 16.816  -62.056 -57.816  1.00 78.65  ? 113  SER   D O    1 
ATOM   21100 C  CB   . SER   D  4  113 ? 15.705  -60.964 -60.533  1.00 84.36  ? 113  SER   D CB   1 
ATOM   21101 O  OG   . SER   D  4  113 ? 17.070  -61.331 -60.623  1.00 88.12  ? 113  SER   D OG   1 
ATOM   21102 H  H    . SER   D  4  113 ? 16.606  -59.194 -59.088  1.00 94.39  ? 113  SER   D H    1 
ATOM   21103 H  HA   . SER   D  4  113 ? 14.342  -60.554 -59.066  1.00 95.20  ? 113  SER   D HA   1 
ATOM   21104 H  HB2  . SER   D  4  113 ? 15.161  -61.690 -60.874  1.00 101.27 ? 113  SER   D HB2  1 
ATOM   21105 H  HB3  . SER   D  4  113 ? 15.560  -60.163 -61.062  1.00 101.27 ? 113  SER   D HB3  1 
ATOM   21106 H  HG   . SER   D  4  113 ? 17.294  -61.408 -61.429  1.00 105.79 ? 113  SER   D HG   1 
ATOM   21107 N  N    . VAL   D  4  114 ? 14.649  -62.669 -57.879  1.00 78.80  ? 114  VAL   D N    1 
ATOM   21108 C  CA   . VAL   D  4  114 ? 14.807  -63.880 -57.085  1.00 80.82  ? 114  VAL   D CA   1 
ATOM   21109 C  C    . VAL   D  4  114 ? 14.264  -65.032 -57.917  1.00 84.14  ? 114  VAL   D C    1 
ATOM   21110 O  O    . VAL   D  4  114 ? 13.108  -64.993 -58.356  1.00 86.16  ? 114  VAL   D O    1 
ATOM   21111 C  CB   . VAL   D  4  114 ? 14.081  -63.774 -55.734  1.00 82.52  ? 114  VAL   D CB   1 
ATOM   21112 C  CG1  . VAL   D  4  114 ? 14.014  -65.128 -55.037  1.00 83.98  ? 114  VAL   D CG1  1 
ATOM   21113 C  CG2  . VAL   D  4  114 ? 14.776  -62.754 -54.843  1.00 84.77  ? 114  VAL   D CG2  1 
ATOM   21114 H  H    . VAL   D  4  114 ? 13.835  -62.524 -58.117  1.00 94.60  ? 114  VAL   D H    1 
ATOM   21115 H  HA   . VAL   D  4  114 ? 15.746  -64.043 -56.906  1.00 97.02  ? 114  VAL   D HA   1 
ATOM   21116 H  HB   . VAL   D  4  114 ? 13.171  -63.479 -55.896  1.00 99.06  ? 114  VAL   D HB   1 
ATOM   21117 H  HG11 . VAL   D  4  114 ? 13.590  -65.017 -54.171  1.00 100.81 ? 114  VAL   D HG11 1 
ATOM   21118 H  HG12 . VAL   D  4  114 ? 13.495  -65.739 -55.583  1.00 100.81 ? 114  VAL   D HG12 1 
ATOM   21119 H  HG13 . VAL   D  4  114 ? 14.914  -65.470 -54.923  1.00 100.81 ? 114  VAL   D HG13 1 
ATOM   21120 H  HG21 . VAL   D  4  114 ? 14.312  -62.710 -53.992  1.00 101.77 ? 114  VAL   D HG21 1 
ATOM   21121 H  HG22 . VAL   D  4  114 ? 15.695  -63.031 -54.704  1.00 101.77 ? 114  VAL   D HG22 1 
ATOM   21122 H  HG23 . VAL   D  4  114 ? 14.753  -61.887 -55.277  1.00 101.77 ? 114  VAL   D HG23 1 
ATOM   21123 N  N    . THR   D  4  115 ? 15.097  -66.042 -58.148  1.00 86.20  ? 115  THR   D N    1 
ATOM   21124 C  CA   . THR   D  4  115 ? 14.722  -67.207 -58.937  1.00 86.99  ? 115  THR   D CA   1 
ATOM   21125 C  C    . THR   D  4  115 ? 14.849  -68.451 -58.071  1.00 88.35  ? 115  THR   D C    1 
ATOM   21126 O  O    . THR   D  4  115 ? 15.889  -68.670 -57.441  1.00 88.05  ? 115  THR   D O    1 
ATOM   21127 C  CB   . THR   D  4  115 ? 15.595  -67.336 -60.187  1.00 85.67  ? 115  THR   D CB   1 
ATOM   21128 O  OG1  . THR   D  4  115 ? 15.787  -66.043 -60.774  1.00 86.00  ? 115  THR   D OG1  1 
ATOM   21129 C  CG2  . THR   D  4  115 ? 14.930  -68.249 -61.204  1.00 86.83  ? 115  THR   D CG2  1 
ATOM   21130 H  H    . THR   D  4  115 ? 15.903  -66.075 -57.850  1.00 103.47 ? 115  THR   D H    1 
ATOM   21131 H  HA   . THR   D  4  115 ? 13.799  -67.124 -59.224  1.00 104.43 ? 115  THR   D HA   1 
ATOM   21132 H  HB   . THR   D  4  115 ? 16.455  -67.714 -59.944  1.00 102.85 ? 115  THR   D HB   1 
ATOM   21133 H  HG1  . THR   D  4  115 ? 16.222  -66.114 -61.489  1.00 103.24 ? 115  THR   D HG1  1 
ATOM   21134 H  HG21 . THR   D  4  115 ? 15.479  -68.314 -62.000  1.00 104.23 ? 115  THR   D HG21 1 
ATOM   21135 H  HG22 . THR   D  4  115 ? 14.813  -69.135 -60.828  1.00 104.23 ? 115  THR   D HG22 1 
ATOM   21136 H  HG23 . THR   D  4  115 ? 14.061  -67.894 -61.449  1.00 104.23 ? 115  THR   D HG23 1 
ATOM   21137 N  N    . VAL   D  4  116 ? 13.794  -69.261 -58.045  1.00 92.49  ? 116  VAL   D N    1 
ATOM   21138 C  CA   . VAL   D  4  116 ? 13.714  -70.433 -57.179  1.00 96.54  ? 116  VAL   D CA   1 
ATOM   21139 C  C    . VAL   D  4  116 ? 13.583  -71.652 -58.080  1.00 97.60  ? 116  VAL   D C    1 
ATOM   21140 O  O    . VAL   D  4  116 ? 12.488  -71.971 -58.559  1.00 96.63  ? 116  VAL   D O    1 
ATOM   21141 C  CB   . VAL   D  4  116 ? 12.546  -70.344 -56.191  1.00 104.22 ? 116  VAL   D CB   1 
ATOM   21142 C  CG1  . VAL   D  4  116 ? 12.512  -71.578 -55.299  1.00 107.76 ? 116  VAL   D CG1  1 
ATOM   21143 C  CG2  . VAL   D  4  116 ? 12.654  -69.075 -55.358  1.00 106.52 ? 116  VAL   D CG2  1 
ATOM   21144 H  H    . VAL   D  4  116 ? 13.095  -69.149 -58.533  1.00 111.02 ? 116  VAL   D H    1 
ATOM   21145 H  HA   . VAL   D  4  116 ? 14.541  -70.513 -56.677  1.00 115.89 ? 116  VAL   D HA   1 
ATOM   21146 H  HB   . VAL   D  4  116 ? 11.713  -70.309 -56.686  1.00 125.10 ? 116  VAL   D HB   1 
ATOM   21147 H  HG11 . VAL   D  4  116 ? 11.801  -71.476 -54.646  1.00 129.35 ? 116  VAL   D HG11 1 
ATOM   21148 H  HG12 . VAL   D  4  116 ? 12.347  -72.360 -55.848  1.00 129.35 ? 116  VAL   D HG12 1 
ATOM   21149 H  HG13 . VAL   D  4  116 ? 13.366  -71.665 -54.847  1.00 129.35 ? 116  VAL   D HG13 1 
ATOM   21150 H  HG21 . VAL   D  4  116 ? 11.916  -69.045 -54.730  1.00 127.86 ? 116  VAL   D HG21 1 
ATOM   21151 H  HG22 . VAL   D  4  116 ? 13.497  -69.083 -54.878  1.00 127.86 ? 116  VAL   D HG22 1 
ATOM   21152 H  HG23 . VAL   D  4  116 ? 12.617  -68.306 -55.948  1.00 127.86 ? 116  VAL   D HG23 1 
ATOM   21153 N  N    . SER   D  4  117 ? 14.697  -72.344 -58.307  1.00 98.85  ? 117  SER   D N    1 
ATOM   21154 C  CA   . SER   D  4  117 ? 14.706  -73.562 -59.099  1.00 102.70 ? 117  SER   D CA   1 
ATOM   21155 C  C    . SER   D  4  117 ? 15.675  -74.553 -58.475  1.00 105.27 ? 117  SER   D C    1 
ATOM   21156 O  O    . SER   D  4  117 ? 16.552  -74.187 -57.689  1.00 105.80 ? 117  SER   D O    1 
ATOM   21157 C  CB   . SER   D  4  117 ? 15.101  -73.290 -60.557  1.00 102.14 ? 117  SER   D CB   1 
ATOM   21158 O  OG   . SER   D  4  117 ? 15.168  -74.497 -61.296  1.00 104.17 ? 117  SER   D OG   1 
ATOM   21159 H  H    . SER   D  4  117 ? 15.471  -72.122 -58.005  1.00 118.65 ? 117  SER   D H    1 
ATOM   21160 H  HA   . SER   D  4  117 ? 13.818  -73.954 -59.094  1.00 123.27 ? 117  SER   D HA   1 
ATOM   21161 H  HB2  . SER   D  4  117 ? 14.437  -72.709 -60.960  1.00 122.61 ? 117  SER   D HB2  1 
ATOM   21162 H  HB3  . SER   D  4  117 ? 15.971  -72.861 -60.573  1.00 122.61 ? 117  SER   D HB3  1 
ATOM   21163 H  HG   . SER   D  4  117 ? 15.836  -74.485 -61.805  1.00 125.04 ? 117  SER   D HG   1 
ATOM   21164 N  N    . SER   D  4  118 ? 15.499  -75.824 -58.832  1.00 106.15 ? 118  SER   D N    1 
ATOM   21165 C  CA   . SER   D  4  118 ? 16.414  -76.870 -58.403  1.00 104.50 ? 118  SER   D CA   1 
ATOM   21166 C  C    . SER   D  4  118 ? 17.594  -77.039 -59.348  1.00 102.97 ? 118  SER   D C    1 
ATOM   21167 O  O    . SER   D  4  118 ? 18.641  -77.543 -58.925  1.00 106.28 ? 118  SER   D O    1 
ATOM   21168 C  CB   . SER   D  4  118 ? 15.670  -78.203 -58.282  1.00 104.34 ? 118  SER   D CB   1 
ATOM   21169 O  OG   . SER   D  4  118 ? 14.633  -78.119 -57.320  1.00 106.25 ? 118  SER   D OG   1 
ATOM   21170 H  H    . SER   D  4  118 ? 14.852  -76.104 -59.325  1.00 127.42 ? 118  SER   D H    1 
ATOM   21171 H  HA   . SER   D  4  118 ? 16.761  -76.645 -57.526  1.00 125.44 ? 118  SER   D HA   1 
ATOM   21172 H  HB2  . SER   D  4  118 ? 15.284  -78.428 -59.143  1.00 125.24 ? 118  SER   D HB2  1 
ATOM   21173 H  HB3  . SER   D  4  118 ? 16.297  -78.891 -58.011  1.00 125.24 ? 118  SER   D HB3  1 
ATOM   21174 H  HG   . SER   D  4  118 ? 14.223  -78.851 -57.275  1.00 127.54 ? 118  SER   D HG   1 
ATOM   21175 N  N    . ALA   D  4  119 ? 17.446  -76.629 -60.608  1.00 98.31  ? 119  ALA   D N    1 
ATOM   21176 C  CA   . ALA   D  4  119 ? 18.527  -76.749 -61.574  1.00 98.26  ? 119  ALA   D CA   1 
ATOM   21177 C  C    . ALA   D  4  119 ? 19.814  -76.156 -61.018  1.00 96.84  ? 119  ALA   D C    1 
ATOM   21178 O  O    . ALA   D  4  119 ? 19.797  -75.241 -60.189  1.00 98.55  ? 119  ALA   D O    1 
ATOM   21179 C  CB   . ALA   D  4  119 ? 18.153  -76.043 -62.879  1.00 99.96  ? 119  ALA   D CB   1 
ATOM   21180 H  H    . ALA   D  4  119 ? 16.728  -76.278 -60.925  1.00 118.00 ? 119  ALA   D H    1 
ATOM   21181 H  HA   . ALA   D  4  119 ? 18.680  -77.688 -61.766  1.00 117.94 ? 119  ALA   D HA   1 
ATOM   21182 H  HB1  . ALA   D  4  119 ? 18.888  -76.126 -63.506  1.00 119.98 ? 119  ALA   D HB1  1 
ATOM   21183 H  HB2  . ALA   D  4  119 ? 17.357  -76.458 -63.246  1.00 119.98 ? 119  ALA   D HB2  1 
ATOM   21184 H  HB3  . ALA   D  4  119 ? 17.981  -75.106 -62.693  1.00 119.98 ? 119  ALA   D HB3  1 
ATOM   21185 N  N    . LYS   D  4  120 ? 20.937  -76.696 -61.476  1.00 94.63  ? 120  LYS   D N    1 
ATOM   21186 C  CA   . LYS   D  4  120 ? 22.253  -76.160 -61.169  1.00 94.16  ? 120  LYS   D CA   1 
ATOM   21187 C  C    . LYS   D  4  120 ? 22.843  -75.525 -62.421  1.00 90.21  ? 120  LYS   D C    1 
ATOM   21188 O  O    . LYS   D  4  120 ? 22.372  -75.748 -63.540  1.00 89.72  ? 120  LYS   D O    1 
ATOM   21189 C  CB   . LYS   D  4  120 ? 23.186  -77.251 -60.630  1.00 96.72  ? 120  LYS   D CB   1 
ATOM   21190 C  CG   . LYS   D  4  120 ? 22.684  -77.916 -59.352  1.00 101.54 ? 120  LYS   D CG   1 
ATOM   21191 C  CD   . LYS   D  4  120 ? 23.818  -78.547 -58.552  1.00 106.55 ? 120  LYS   D CD   1 
ATOM   21192 C  CE   . LYS   D  4  120 ? 23.290  -79.275 -57.322  1.00 112.70 ? 120  LYS   D CE   1 
ATOM   21193 N  NZ   . LYS   D  4  120 ? 24.382  -79.771 -56.437  1.00 119.53 ? 120  LYS   D NZ   1 
ATOM   21194 H  H    . LYS   D  4  120 ? 20.961  -77.392 -61.980  1.00 113.59 ? 120  LYS   D H    1 
ATOM   21195 H  HA   . LYS   D  4  120 ? 22.179  -75.479 -60.482  1.00 113.02 ? 120  LYS   D HA   1 
ATOM   21196 H  HB2  . LYS   D  4  120 ? 23.280  -77.942 -61.305  1.00 116.10 ? 120  LYS   D HB2  1 
ATOM   21197 H  HB3  . LYS   D  4  120 ? 24.050  -76.855 -60.438  1.00 116.10 ? 120  LYS   D HB3  1 
ATOM   21198 H  HG2  . LYS   D  4  120 ? 22.255  -77.249 -58.793  1.00 121.89 ? 120  LYS   D HG2  1 
ATOM   21199 H  HG3  . LYS   D  4  120 ? 22.051  -78.613 -59.582  1.00 121.89 ? 120  LYS   D HG3  1 
ATOM   21200 H  HD2  . LYS   D  4  120 ? 24.286  -79.189 -59.109  1.00 127.90 ? 120  LYS   D HD2  1 
ATOM   21201 H  HD3  . LYS   D  4  120 ? 24.430  -77.854 -58.258  1.00 127.90 ? 120  LYS   D HD3  1 
ATOM   21202 H  HE2  . LYS   D  4  120 ? 22.739  -78.666 -56.806  1.00 135.27 ? 120  LYS   D HE2  1 
ATOM   21203 H  HE3  . LYS   D  4  120 ? 22.764  -80.038 -57.607  1.00 135.27 ? 120  LYS   D HE3  1 
ATOM   21204 H  HZ1  . LYS   D  4  120 ? 24.038  -80.221 -55.751  1.00 143.47 ? 120  LYS   D HZ1  1 
ATOM   21205 H  HZ2  . LYS   D  4  120 ? 24.923  -80.310 -56.894  1.00 143.47 ? 120  LYS   D HZ2  1 
ATOM   21206 H  HZ3  . LYS   D  4  120 ? 24.856  -79.085 -56.125  1.00 143.47 ? 120  LYS   D HZ3  1 
ATOM   21207 N  N    . THR   D  4  121 ? 23.878  -74.716 -62.212  1.00 88.48  ? 121  THR   D N    1 
ATOM   21208 C  CA   . THR   D  4  121 ? 24.519  -73.998 -63.308  1.00 88.32  ? 121  THR   D CA   1 
ATOM   21209 C  C    . THR   D  4  121 ? 24.845  -74.939 -64.463  1.00 90.83  ? 121  THR   D C    1 
ATOM   21210 O  O    . THR   D  4  121 ? 25.432  -76.006 -64.266  1.00 94.60  ? 121  THR   D O    1 
ATOM   21211 C  CB   . THR   D  4  121 ? 25.790  -73.312 -62.794  1.00 86.94  ? 121  THR   D CB   1 
ATOM   21212 O  OG1  . THR   D  4  121 ? 26.503  -72.721 -63.887  1.00 86.28  ? 121  THR   D OG1  1 
ATOM   21213 C  CG2  . THR   D  4  121 ? 26.697  -74.306 -62.070  1.00 88.96  ? 121  THR   D CG2  1 
ATOM   21214 H  H    . THR   D  4  121 ? 24.229  -74.564 -61.442  1.00 106.21 ? 121  THR   D H    1 
ATOM   21215 H  HA   . THR   D  4  121 ? 23.917  -73.316 -63.645  1.00 106.03 ? 121  THR   D HA   1 
ATOM   21216 H  HB   . THR   D  4  121 ? 25.541  -72.619 -62.162  1.00 104.37 ? 121  THR   D HB   1 
ATOM   21217 H  HG1  . THR   D  4  121 ? 27.225  -72.389 -63.614  1.00 103.57 ? 121  THR   D HG1  1 
ATOM   21218 H  HG21 . THR   D  4  121 ? 27.512  -73.865 -61.785  1.00 106.78 ? 121  THR   D HG21 1 
ATOM   21219 H  HG22 . THR   D  4  121 ? 26.242  -74.662 -61.291  1.00 106.78 ? 121  THR   D HG22 1 
ATOM   21220 H  HG23 . THR   D  4  121 ? 26.926  -75.038 -62.663  1.00 106.78 ? 121  THR   D HG23 1 
ATOM   21221 N  N    . THR   D  4  122 ? 24.454  -74.539 -65.676  1.00 89.15  ? 122  THR   D N    1 
ATOM   21222 C  CA   . THR   D  4  122 ? 24.624  -75.365 -66.865  1.00 87.66  ? 122  THR   D CA   1 
ATOM   21223 C  C    . THR   D  4  122 ? 25.010  -74.496 -68.053  1.00 86.55  ? 122  THR   D C    1 
ATOM   21224 O  O    . THR   D  4  122 ? 24.420  -73.434 -68.271  1.00 89.91  ? 122  THR   D O    1 
ATOM   21225 C  CB   . THR   D  4  122 ? 23.341  -76.139 -67.201  1.00 86.57  ? 122  THR   D CB   1 
ATOM   21226 O  OG1  . THR   D  4  122 ? 22.917  -76.892 -66.058  1.00 87.82  ? 122  THR   D OG1  1 
ATOM   21227 C  CG2  . THR   D  4  122 ? 23.574  -77.083 -68.374  1.00 87.92  ? 122  THR   D CG2  1 
ATOM   21228 H  H    . THR   D  4  122 ? 24.082  -73.780 -65.834  1.00 107.02 ? 122  THR   D H    1 
ATOM   21229 H  HA   . THR   D  4  122 ? 25.341  -75.999 -66.705  1.00 105.23 ? 122  THR   D HA   1 
ATOM   21230 H  HB   . THR   D  4  122 ? 22.643  -75.512 -67.448  1.00 103.92 ? 122  THR   D HB   1 
ATOM   21231 H  HG1  . THR   D  4  122 ? 22.531  -76.388 -65.508  1.00 105.42 ? 122  THR   D HG1  1 
ATOM   21232 H  HG21 . THR   D  4  122 ? 22.776  -77.610 -68.539  1.00 105.54 ? 122  THR   D HG21 1 
ATOM   21233 H  HG22 . THR   D  4  122 ? 23.785  -76.574 -69.172  1.00 105.54 ? 122  THR   D HG22 1 
ATOM   21234 H  HG23 . THR   D  4  122 ? 24.312  -77.681 -68.177  1.00 105.54 ? 122  THR   D HG23 1 
ATOM   21235 N  N    . ALA   D  4  123 ? 25.994  -74.968 -68.836  1.00 85.03  ? 123  ALA   D N    1 
ATOM   21236 C  CA   . ALA   D  4  123 ? 26.488  -74.220 -69.982  1.00 88.60  ? 123  ALA   D CA   1 
ATOM   21237 C  C    . ALA   D  4  123 ? 25.515  -74.312 -71.158  1.00 92.83  ? 123  ALA   D C    1 
ATOM   21238 O  O    . ALA   D  4  123 ? 24.771  -75.289 -71.284  1.00 94.59  ? 123  ALA   D O    1 
ATOM   21239 C  CB   . ALA   D  4  123 ? 27.855  -74.744 -70.411  1.00 89.75  ? 123  ALA   D CB   1 
ATOM   21240 H  H    . ALA   D  4  123 ? 26.388  -75.723 -68.717  1.00 102.08 ? 123  ALA   D H    1 
ATOM   21241 H  HA   . ALA   D  4  123 ? 26.579  -73.286 -69.738  1.00 106.36 ? 123  ALA   D HA   1 
ATOM   21242 H  HB1  . ALA   D  4  123 ? 28.157  -74.244 -71.185  1.00 107.74 ? 123  ALA   D HB1  1 
ATOM   21243 H  HB2  . ALA   D  4  123 ? 28.481  -74.630 -69.678  1.00 107.74 ? 123  ALA   D HB2  1 
ATOM   21244 H  HB3  . ALA   D  4  123 ? 27.777  -75.685 -70.635  1.00 107.74 ? 123  ALA   D HB3  1 
ATOM   21245 N  N    . PRO   D  4  124 ? 25.500  -73.307 -72.032  1.00 95.13  ? 124  PRO   D N    1 
ATOM   21246 C  CA   . PRO   D  4  124 ? 24.558  -73.316 -73.154  1.00 94.28  ? 124  PRO   D CA   1 
ATOM   21247 C  C    . PRO   D  4  124 ? 24.965  -74.243 -74.290  1.00 94.57  ? 124  PRO   D C    1 
ATOM   21248 O  O    . PRO   D  4  124 ? 26.113  -74.675 -74.417  1.00 94.49  ? 124  PRO   D O    1 
ATOM   21249 C  CB   . PRO   D  4  124 ? 24.552  -71.857 -73.636  1.00 97.15  ? 124  PRO   D CB   1 
ATOM   21250 C  CG   . PRO   D  4  124 ? 25.769  -71.235 -73.069  1.00 99.96  ? 124  PRO   D CG   1 
ATOM   21251 C  CD   . PRO   D  4  124 ? 26.109  -71.981 -71.823  1.00 98.84  ? 124  PRO   D CD   1 
ATOM   21252 H  HA   . PRO   D  4  124 ? 23.681  -73.575 -72.832  1.00 113.17 ? 124  PRO   D HA   1 
ATOM   21253 H  HB2  . PRO   D  4  124 ? 24.574  -71.833 -74.606  1.00 116.62 ? 124  PRO   D HB2  1 
ATOM   21254 H  HB3  . PRO   D  4  124 ? 23.755  -71.409 -73.312  1.00 116.62 ? 124  PRO   D HB3  1 
ATOM   21255 H  HG2  . PRO   D  4  124 ? 26.493  -71.302 -73.711  1.00 119.99 ? 124  PRO   D HG2  1 
ATOM   21256 H  HG3  . PRO   D  4  124 ? 25.590  -70.304 -72.867  1.00 119.99 ? 124  PRO   D HG3  1 
ATOM   21257 H  HD2  . PRO   D  4  124 ? 27.071  -72.057 -71.720  1.00 118.65 ? 124  PRO   D HD2  1 
ATOM   21258 H  HD3  . PRO   D  4  124 ? 25.725  -71.545 -71.046  1.00 118.65 ? 124  PRO   D HD3  1 
ATOM   21259 N  N    . SER   D  4  125 ? 23.969  -74.542 -75.119  1.00 79.73  ? 125  SER   D N    1 
ATOM   21260 C  CA   . SER   D  4  125 ? 24.140  -75.183 -76.417  1.00 79.24  ? 125  SER   D CA   1 
ATOM   21261 C  C    . SER   D  4  125 ? 23.777  -74.141 -77.467  1.00 76.95  ? 125  SER   D C    1 
ATOM   21262 O  O    . SER   D  4  125 ? 22.602  -73.788 -77.611  1.00 78.70  ? 125  SER   D O    1 
ATOM   21263 C  CB   . SER   D  4  125 ? 23.251  -76.417 -76.544  1.00 82.81  ? 125  SER   D CB   1 
ATOM   21264 O  OG   . SER   D  4  125 ? 23.845  -77.558 -75.953  1.00 86.40  ? 125  SER   D OG   1 
ATOM   21265 H  H    . SER   D  4  125 ? 23.145  -74.375 -74.941  1.00 95.72  ? 125  SER   D H    1 
ATOM   21266 H  HA   . SER   D  4  125 ? 25.060  -75.467 -76.535  1.00 95.13  ? 125  SER   D HA   1 
ATOM   21267 H  HB2  . SER   D  4  125 ? 22.406  -76.240 -76.100  1.00 99.41  ? 125  SER   D HB2  1 
ATOM   21268 H  HB3  . SER   D  4  125 ? 23.099  -76.597 -77.485  1.00 99.41  ? 125  SER   D HB3  1 
ATOM   21269 H  HG   . SER   D  4  125 ? 23.386  -78.241 -76.122  1.00 103.72 ? 125  SER   D HG   1 
ATOM   21270 N  N    . VAL   D  4  126 ? 24.774  -73.639 -78.188  1.00 74.37  ? 126  VAL   D N    1 
ATOM   21271 C  CA   . VAL   D  4  126 ? 24.567  -72.581 -79.170  1.00 72.80  ? 126  VAL   D CA   1 
ATOM   21272 C  C    . VAL   D  4  126 ? 24.500  -73.217 -80.549  1.00 71.26  ? 126  VAL   D C    1 
ATOM   21273 O  O    . VAL   D  4  126 ? 25.454  -73.869 -80.992  1.00 72.29  ? 126  VAL   D O    1 
ATOM   21274 C  CB   . VAL   D  4  126 ? 25.672  -71.516 -79.098  1.00 73.99  ? 126  VAL   D CB   1 
ATOM   21275 C  CG1  . VAL   D  4  126 ? 25.419  -70.422 -80.129  1.00 71.83  ? 126  VAL   D CG1  1 
ATOM   21276 C  CG2  . VAL   D  4  126 ? 25.734  -70.925 -77.698  1.00 72.90  ? 126  VAL   D CG2  1 
ATOM   21277 H  H    . VAL   D  4  126 ? 25.591  -73.900 -78.125  1.00 89.28  ? 126  VAL   D H    1 
ATOM   21278 H  HA   . VAL   D  4  126 ? 23.719  -72.145 -78.994  1.00 87.40  ? 126  VAL   D HA   1 
ATOM   21279 H  HB   . VAL   D  4  126 ? 26.528  -71.927 -79.296  1.00 88.82  ? 126  VAL   D HB   1 
ATOM   21280 H  HG11 . VAL   D  4  126 ? 26.113  -69.749 -80.052  1.00 86.23  ? 126  VAL   D HG11 1 
ATOM   21281 H  HG12 . VAL   D  4  126 ? 25.435  -70.815 -81.016  1.00 86.23  ? 126  VAL   D HG12 1 
ATOM   21282 H  HG13 . VAL   D  4  126 ? 24.551  -70.023 -79.959  1.00 86.23  ? 126  VAL   D HG13 1 
ATOM   21283 H  HG21 . VAL   D  4  126 ? 26.434  -70.255 -77.668  1.00 87.51  ? 126  VAL   D HG21 1 
ATOM   21284 H  HG22 . VAL   D  4  126 ? 24.878  -70.519 -77.489  1.00 87.51  ? 126  VAL   D HG22 1 
ATOM   21285 H  HG23 . VAL   D  4  126 ? 25.927  -71.634 -77.064  1.00 87.51  ? 126  VAL   D HG23 1 
ATOM   21286 N  N    . TYR   D  4  127 ? 23.374  -73.017 -81.230  1.00 70.61  ? 127  TYR   D N    1 
ATOM   21287 C  CA   . TYR   D  4  127 ? 23.096  -73.649 -82.512  1.00 71.37  ? 127  TYR   D CA   1 
ATOM   21288 C  C    . TYR   D  4  127 ? 22.942  -72.582 -83.586  1.00 72.00  ? 127  TYR   D C    1 
ATOM   21289 O  O    . TYR   D  4  127 ? 22.096  -71.684 -83.439  1.00 69.82  ? 127  TYR   D O    1 
ATOM   21290 C  CB   . TYR   D  4  127 ? 21.824  -74.495 -82.420  1.00 67.19  ? 127  TYR   D CB   1 
ATOM   21291 C  CG   . TYR   D  4  127 ? 21.917  -75.635 -81.435  1.00 67.56  ? 127  TYR   D CG   1 
ATOM   21292 C  CD1  . TYR   D  4  127 ? 23.039  -76.452 -81.393  1.00 68.27  ? 127  TYR   D CD1  1 
ATOM   21293 C  CD2  . TYR   D  4  127 ? 20.887  -75.892 -80.541  1.00 69.52  ? 127  TYR   D CD2  1 
ATOM   21294 C  CE1  . TYR   D  4  127 ? 23.129  -77.495 -80.494  1.00 72.59  ? 127  TYR   D CE1  1 
ATOM   21295 C  CE2  . TYR   D  4  127 ? 20.968  -76.932 -79.636  1.00 73.28  ? 127  TYR   D CE2  1 
ATOM   21296 C  CZ   . TYR   D  4  127 ? 22.091  -77.732 -79.620  1.00 75.53  ? 127  TYR   D CZ   1 
ATOM   21297 O  OH   . TYR   D  4  127 ? 22.180  -78.769 -78.720  1.00 80.47  ? 127  TYR   D OH   1 
ATOM   21298 H  H    . TYR   D  4  127 ? 22.739  -72.504 -80.960  1.00 84.77  ? 127  TYR   D H    1 
ATOM   21299 H  HA   . TYR   D  4  127 ? 23.841  -74.220 -82.757  1.00 85.68  ? 127  TYR   D HA   1 
ATOM   21300 H  HB2  . TYR   D  4  127 ? 21.090  -73.924 -82.143  1.00 80.67  ? 127  TYR   D HB2  1 
ATOM   21301 H  HB3  . TYR   D  4  127 ? 21.639  -74.873 -83.294  1.00 80.67  ? 127  TYR   D HB3  1 
ATOM   21302 H  HD1  . TYR   D  4  127 ? 23.741  -76.293 -81.981  1.00 81.97  ? 127  TYR   D HD1  1 
ATOM   21303 H  HD2  . TYR   D  4  127 ? 20.128  -75.353 -80.551  1.00 83.46  ? 127  TYR   D HD2  1 
ATOM   21304 H  HE1  . TYR   D  4  127 ? 23.887  -78.034 -80.478  1.00 87.15  ? 127  TYR   D HE1  1 
ATOM   21305 H  HE2  . TYR   D  4  127 ? 20.271  -77.092 -79.042  1.00 87.97  ? 127  TYR   D HE2  1 
ATOM   21306 H  HH   . TYR   D  4  127 ? 21.481  -78.807 -78.255  1.00 96.60  ? 127  TYR   D HH   1 
ATOM   21307 N  N    . PRO   D  4  128 ? 23.707  -72.628 -84.674  1.00 77.49  ? 128  PRO   D N    1 
ATOM   21308 C  CA   . PRO   D  4  128 ? 23.485  -71.667 -85.757  1.00 82.43  ? 128  PRO   D CA   1 
ATOM   21309 C  C    . PRO   D  4  128 ? 22.197  -71.988 -86.492  1.00 87.62  ? 128  PRO   D C    1 
ATOM   21310 O  O    . PRO   D  4  128 ? 21.813  -73.150 -86.639  1.00 93.18  ? 128  PRO   D O    1 
ATOM   21311 C  CB   . PRO   D  4  128 ? 24.708  -71.863 -86.657  1.00 85.68  ? 128  PRO   D CB   1 
ATOM   21312 C  CG   . PRO   D  4  128 ? 25.044  -73.303 -86.485  1.00 86.13  ? 128  PRO   D CG   1 
ATOM   21313 C  CD   . PRO   D  4  128 ? 24.709  -73.645 -85.049  1.00 81.73  ? 128  PRO   D CD   1 
ATOM   21314 H  HA   . PRO   D  4  128 ? 23.469  -70.754 -85.431  1.00 98.95  ? 128  PRO   D HA   1 
ATOM   21315 H  HB2  . PRO   D  4  128 ? 24.481  -71.662 -87.579  1.00 102.86 ? 128  PRO   D HB2  1 
ATOM   21316 H  HB3  . PRO   D  4  128 ? 25.436  -71.293 -86.363  1.00 102.86 ? 128  PRO   D HB3  1 
ATOM   21317 H  HG2  . PRO   D  4  128 ? 24.514  -73.837 -87.097  1.00 103.40 ? 128  PRO   D HG2  1 
ATOM   21318 H  HG3  . PRO   D  4  128 ? 25.989  -73.440 -86.657  1.00 103.40 ? 128  PRO   D HG3  1 
ATOM   21319 H  HD2  . PRO   D  4  128 ? 24.333  -74.537 -84.986  1.00 98.11  ? 128  PRO   D HD2  1 
ATOM   21320 H  HD3  . PRO   D  4  128 ? 25.496  -73.576 -84.486  1.00 98.11  ? 128  PRO   D HD3  1 
ATOM   21321 N  N    . LEU   D  4  129 ? 21.521  -70.940 -86.949  1.00 85.35  ? 129  LEU   D N    1 
ATOM   21322 C  CA   . LEU   D  4  129 ? 20.290  -71.085 -87.721  1.00 85.56  ? 129  LEU   D CA   1 
ATOM   21323 C  C    . LEU   D  4  129 ? 20.505  -70.421 -89.076  1.00 87.23  ? 129  LEU   D C    1 
ATOM   21324 O  O    . LEU   D  4  129 ? 20.464  -69.191 -89.190  1.00 86.46  ? 129  LEU   D O    1 
ATOM   21325 C  CB   . LEU   D  4  129 ? 19.096  -70.484 -86.987  1.00 88.14  ? 129  LEU   D CB   1 
ATOM   21326 C  CG   . LEU   D  4  129 ? 18.776  -71.068 -85.609  1.00 91.30  ? 129  LEU   D CG   1 
ATOM   21327 C  CD1  . LEU   D  4  129 ? 17.555  -70.377 -85.020  1.00 92.85  ? 129  LEU   D CD1  1 
ATOM   21328 C  CD2  . LEU   D  4  129 ? 18.558  -72.574 -85.685  1.00 95.50  ? 129  LEU   D CD2  1 
ATOM   21329 H  H    . LEU   D  4  129 ? 21.758  -70.123 -86.822  1.00 102.46 ? 129  LEU   D H    1 
ATOM   21330 H  HA   . LEU   D  4  129 ? 20.114  -72.029 -87.863  1.00 102.71 ? 129  LEU   D HA   1 
ATOM   21331 H  HB2  . LEU   D  4  129 ? 19.266  -69.537 -86.862  1.00 105.81 ? 129  LEU   D HB2  1 
ATOM   21332 H  HB3  . LEU   D  4  129 ? 18.309  -70.610 -87.540  1.00 105.81 ? 129  LEU   D HB3  1 
ATOM   21333 H  HG   . LEU   D  4  129 ? 19.531  -70.915 -85.021  1.00 109.59 ? 129  LEU   D HG   1 
ATOM   21334 H  HD11 . LEU   D  4  129 ? 17.362  -70.765 -84.152  1.00 111.46 ? 129  LEU   D HD11 1 
ATOM   21335 H  HD12 . LEU   D  4  129 ? 17.744  -69.431 -84.925  1.00 111.46 ? 129  LEU   D HD12 1 
ATOM   21336 H  HD13 . LEU   D  4  129 ? 16.801  -70.506 -85.616  1.00 111.46 ? 129  LEU   D HD13 1 
ATOM   21337 H  HD21 . LEU   D  4  129 ? 18.341  -72.906 -84.800  1.00 114.64 ? 129  LEU   D HD21 1 
ATOM   21338 H  HD22 . LEU   D  4  129 ? 17.826  -72.757 -86.296  1.00 114.64 ? 129  LEU   D HD22 1 
ATOM   21339 H  HD23 . LEU   D  4  129 ? 19.370  -72.995 -86.007  1.00 114.64 ? 129  LEU   D HD23 1 
ATOM   21340 N  N    . ALA   D  4  130 ? 20.745  -71.240 -90.094  1.00 93.51  ? 130  ALA   D N    1 
ATOM   21341 C  CA   . ALA   D  4  130 ? 20.820  -70.783 -91.468  1.00 94.49  ? 130  ALA   D CA   1 
ATOM   21342 C  C    . ALA   D  4  130 ? 19.531  -71.126 -92.206  1.00 95.32  ? 130  ALA   D C    1 
ATOM   21343 O  O    . ALA   D  4  130 ? 18.838  -72.083 -91.847  1.00 92.68  ? 130  ALA   D O    1 
ATOM   21344 C  CB   . ALA   D  4  130 ? 22.007  -71.424 -92.193  1.00 97.30  ? 130  ALA   D CB   1 
ATOM   21345 H  H    . ALA   D  4  130 ? 20.871  -72.086 -90.009  1.00 112.25 ? 130  ALA   D H    1 
ATOM   21346 H  HA   . ALA   D  4  130 ? 20.946  -69.821 -91.488  1.00 113.43 ? 130  ALA   D HA   1 
ATOM   21347 H  HB1  . ALA   D  4  130 ? 22.028  -71.103 -93.108  1.00 116.80 ? 130  ALA   D HB1  1 
ATOM   21348 H  HB2  . ALA   D  4  130 ? 22.826  -71.177 -91.736  1.00 116.80 ? 130  ALA   D HB2  1 
ATOM   21349 H  HB3  . ALA   D  4  130 ? 21.900  -72.388 -92.182  1.00 116.80 ? 130  ALA   D HB3  1 
ATOM   21350 N  N    . PRO   D  4  131 ? 19.179  -70.364 -93.240  1.00 98.00  ? 131  PRO   D N    1 
ATOM   21351 C  CA   . PRO   D  4  131 ? 17.933  -70.643 -93.969  1.00 102.60 ? 131  PRO   D CA   1 
ATOM   21352 C  C    . PRO   D  4  131 ? 17.953  -71.978 -94.697  1.00 110.21 ? 131  PRO   D C    1 
ATOM   21353 O  O    . PRO   D  4  131 ? 18.941  -72.717 -94.635  1.00 116.71 ? 131  PRO   D O    1 
ATOM   21354 C  CB   . PRO   D  4  131 ? 17.832  -69.468 -94.953  1.00 104.68 ? 131  PRO   D CB   1 
ATOM   21355 C  CG   . PRO   D  4  131 ? 19.218  -68.915 -95.054  1.00 102.90 ? 131  PRO   D CG   1 
ATOM   21356 C  CD   . PRO   D  4  131 ? 19.853  -69.149 -93.727  1.00 96.70  ? 131  PRO   D CD   1 
ATOM   21357 H  HA   . PRO   D  4  131 ? 17.180  -70.625 -93.359  1.00 123.15 ? 131  PRO   D HA   1 
ATOM   21358 H  HB2  . PRO   D  4  131 ? 17.523  -69.787 -95.816  1.00 125.65 ? 131  PRO   D HB2  1 
ATOM   21359 H  HB3  . PRO   D  4  131 ? 17.217  -68.802 -94.608  1.00 125.65 ? 131  PRO   D HB3  1 
ATOM   21360 H  HG2  . PRO   D  4  131 ? 19.705  -69.378 -95.753  1.00 123.52 ? 131  PRO   D HG2  1 
ATOM   21361 H  HG3  . PRO   D  4  131 ? 19.177  -67.966 -95.251  1.00 123.52 ? 131  PRO   D HG3  1 
ATOM   21362 H  HD2  . PRO   D  4  131 ? 20.807  -69.297 -93.821  1.00 116.08 ? 131  PRO   D HD2  1 
ATOM   21363 H  HD3  . PRO   D  4  131 ? 19.692  -68.402 -93.129  1.00 116.08 ? 131  PRO   D HD3  1 
ATOM   21364 N  N    . VAL   D  4  132 ? 16.856  -72.295 -95.386  1.00 113.08 ? 132  VAL   D N    1 
ATOM   21365 C  CA   . VAL   D  4  132 ? 16.728  -73.531 -96.148  1.00 122.92 ? 132  VAL   D CA   1 
ATOM   21366 C  C    . VAL   D  4  132 ? 17.171  -73.271 -97.581  1.00 130.08 ? 132  VAL   D C    1 
ATOM   21367 O  O    . VAL   D  4  132 ? 17.025  -72.165 -98.111  1.00 128.95 ? 132  VAL   D O    1 
ATOM   21368 C  CB   . VAL   D  4  132 ? 15.282  -74.070 -96.100  1.00 126.41 ? 132  VAL   D CB   1 
ATOM   21369 C  CG1  . VAL   D  4  132 ? 15.234  -75.518 -96.578  1.00 134.54 ? 132  VAL   D CG1  1 
ATOM   21370 C  CG2  . VAL   D  4  132 ? 14.708  -73.948 -94.699  1.00 119.92 ? 132  VAL   D CG2  1 
ATOM   21371 H  H    . VAL   D  4  132 ? 16.156  -71.796 -95.427  1.00 135.73 ? 132  VAL   D H    1 
ATOM   21372 H  HA   . VAL   D  4  132 ? 17.311  -74.202 -95.758  1.00 147.54 ? 132  VAL   D HA   1 
ATOM   21373 H  HB   . VAL   D  4  132 ? 14.732  -73.537 -96.696  1.00 151.73 ? 132  VAL   D HB   1 
ATOM   21374 H  HG11 . VAL   D  4  132 ? 14.318  -75.834 -96.535  1.00 161.48 ? 132  VAL   D HG11 1 
ATOM   21375 H  HG12 . VAL   D  4  132 ? 15.557  -75.560 -97.491  1.00 161.48 ? 132  VAL   D HG12 1 
ATOM   21376 H  HG13 . VAL   D  4  132 ? 15.798  -76.058 -96.003  1.00 161.48 ? 132  VAL   D HG13 1 
ATOM   21377 H  HG21 . VAL   D  4  132 ? 13.813  -74.323 -94.690  1.00 143.95 ? 132  VAL   D HG21 1 
ATOM   21378 H  HG22 . VAL   D  4  132 ? 15.276  -74.434 -94.082  1.00 143.95 ? 132  VAL   D HG22 1 
ATOM   21379 H  HG23 . VAL   D  4  132 ? 14.676  -73.011 -94.451  1.00 143.95 ? 132  VAL   D HG23 1 
ATOM   21380 N  N    . CYS   D  4  133 ? 17.713  -74.305 -98.216  1.00 140.40 ? 133  CYS   D N    1 
ATOM   21381 C  CA   . CYS   D  4  133 ? 18.212  -74.199 -99.583  1.00 155.24 ? 133  CYS   D CA   1 
ATOM   21382 C  C    . CYS   D  4  133 ? 17.083  -73.925 -100.571 1.00 167.61 ? 133  CYS   D C    1 
ATOM   21383 O  O    . CYS   D  4  133 ? 17.162  -72.995 -101.375 1.00 173.08 ? 133  CYS   D O    1 
ATOM   21384 C  CB   . CYS   D  4  133 ? 18.952  -75.483 -99.971  1.00 164.72 ? 133  CYS   D CB   1 
ATOM   21385 S  SG   . CYS   D  4  133 ? 18.536  -76.917 -98.931  1.00 170.37 ? 133  CYS   D SG   1 
ATOM   21386 H  H    . CYS   D  4  133 ? 17.804  -75.089 -97.874  1.00 168.51 ? 133  CYS   D H    1 
ATOM   21387 H  HA   . CYS   D  4  133 ? 18.833  -73.456 -99.636  1.00 186.32 ? 133  CYS   D HA   1 
ATOM   21388 H  HB2  . CYS   D  4  133 ? 18.728  -75.707 -100.887 1.00 197.70 ? 133  CYS   D HB2  1 
ATOM   21389 H  HB3  . CYS   D  4  133 ? 19.907  -75.327 -99.892  1.00 197.70 ? 133  CYS   D HB3  1 
ATOM   21390 N  N    . GLY   D  4  138 ? 14.479  -61.729 -103.149 1.00 146.00 ? 138  GLY   D N    1 
ATOM   21391 C  CA   . GLY   D  4  138 ? 15.617  -62.116 -102.337 1.00 141.42 ? 138  GLY   D CA   1 
ATOM   21392 C  C    . GLY   D  4  138 ? 16.557  -60.959 -102.066 1.00 139.28 ? 138  GLY   D C    1 
ATOM   21393 O  O    . GLY   D  4  138 ? 17.728  -60.996 -102.444 1.00 141.11 ? 138  GLY   D O    1 
ATOM   21394 H  HA2  . GLY   D  4  138 ? 15.302  -62.459 -101.486 1.00 169.74 ? 138  GLY   D HA2  1 
ATOM   21395 H  HA3  . GLY   D  4  138 ? 16.114  -62.813 -102.793 1.00 169.74 ? 138  GLY   D HA3  1 
ATOM   21396 N  N    . SER   D  4  139 ? 16.041  -59.925 -101.403 1.00 137.53 ? 139  SER   D N    1 
ATOM   21397 C  CA   . SER   D  4  139 ? 16.800  -58.710 -101.129 1.00 138.45 ? 139  SER   D CA   1 
ATOM   21398 C  C    . SER   D  4  139 ? 17.458  -58.715 -99.756  1.00 133.93 ? 139  SER   D C    1 
ATOM   21399 O  O    . SER   D  4  139 ? 18.585  -58.230 -99.617  1.00 136.84 ? 139  SER   D O    1 
ATOM   21400 C  CB   . SER   D  4  139 ? 15.889  -57.485 -101.246 1.00 141.45 ? 139  SER   D CB   1 
ATOM   21401 O  OG   . SER   D  4  139 ? 14.914  -57.477 -100.218 1.00 139.63 ? 139  SER   D OG   1 
ATOM   21402 H  H    . SER   D  4  139 ? 15.238  -59.905 -101.096 1.00 165.07 ? 139  SER   D H    1 
ATOM   21403 H  HA   . SER   D  4  139 ? 17.502  -58.628 -101.793 1.00 166.17 ? 139  SER   D HA   1 
ATOM   21404 H  HB2  . SER   D  4  139 ? 16.429  -56.683 -101.175 1.00 169.78 ? 139  SER   D HB2  1 
ATOM   21405 H  HB3  . SER   D  4  139 ? 15.439  -57.507 -102.106 1.00 169.78 ? 139  SER   D HB3  1 
ATOM   21406 H  HG   . SER   D  4  139 ? 14.426  -56.797 -100.290 1.00 167.59 ? 139  SER   D HG   1 
ATOM   21407 N  N    . SER   D  4  140 ? 16.783  -59.244 -98.740  1.00 124.56 ? 140  SER   D N    1 
ATOM   21408 C  CA   . SER   D  4  140 ? 17.332  -59.349 -97.398  1.00 117.54 ? 140  SER   D CA   1 
ATOM   21409 C  C    . SER   D  4  140 ? 17.288  -60.800 -96.939  1.00 118.46 ? 140  SER   D C    1 
ATOM   21410 O  O    . SER   D  4  140 ? 16.497  -61.608 -97.433  1.00 121.59 ? 140  SER   D O    1 
ATOM   21411 C  CB   . SER   D  4  140 ? 16.565  -58.465 -96.407  1.00 112.07 ? 140  SER   D CB   1 
ATOM   21412 O  OG   . SER   D  4  140 ? 15.249  -58.950 -96.206  1.00 110.06 ? 140  SER   D OG   1 
ATOM   21413 H  H    . SER   D  4  140 ? 15.984  -59.556 -98.808  1.00 149.51 ? 140  SER   D H    1 
ATOM   21414 H  HA   . SER   D  4  140 ? 18.258  -59.057 -97.406  1.00 141.08 ? 140  SER   D HA   1 
ATOM   21415 H  HB2  . SER   D  4  140 ? 17.034  -58.464 -95.558  1.00 134.53 ? 140  SER   D HB2  1 
ATOM   21416 H  HB3  . SER   D  4  140 ? 16.518  -57.563 -96.761  1.00 134.53 ? 140  SER   D HB3  1 
ATOM   21417 H  HG   . SER   D  4  140 ? 14.832  -58.441 -95.684  1.00 132.11 ? 140  SER   D HG   1 
ATOM   21418 N  N    . VAL   D  4  141 ? 18.149  -61.122 -95.977  1.00 111.78 ? 141  VAL   D N    1 
ATOM   21419 C  CA   . VAL   D  4  141 ? 18.288  -62.477 -95.462  1.00 105.81 ? 141  VAL   D CA   1 
ATOM   21420 C  C    . VAL   D  4  141 ? 18.232  -62.430 -93.943  1.00 100.19 ? 141  VAL   D C    1 
ATOM   21421 O  O    . VAL   D  4  141 ? 18.812  -61.536 -93.318  1.00 98.87  ? 141  VAL   D O    1 
ATOM   21422 C  CB   . VAL   D  4  141 ? 19.603  -63.132 -95.937  1.00 104.34 ? 141  VAL   D CB   1 
ATOM   21423 C  CG1  . VAL   D  4  141 ? 20.805  -62.312 -95.484  1.00 99.99  ? 141  VAL   D CG1  1 
ATOM   21424 C  CG2  . VAL   D  4  141 ? 19.701  -64.564 -95.428  1.00 99.29  ? 141  VAL   D CG2  1 
ATOM   21425 H  H    . VAL   D  4  141 ? 18.675  -60.556 -95.599  1.00 134.17 ? 141  VAL   D H    1 
ATOM   21426 H  HA   . VAL   D  4  141 ? 17.546  -63.016 -95.777  1.00 127.01 ? 141  VAL   D HA   1 
ATOM   21427 H  HB   . VAL   D  4  141 ? 19.607  -63.159 -96.907  1.00 125.24 ? 141  VAL   D HB   1 
ATOM   21428 H  HG11 . VAL   D  4  141 ? 21.613  -62.717 -95.835  1.00 120.02 ? 141  VAL   D HG11 1 
ATOM   21429 H  HG12 . VAL   D  4  141 ? 20.715  -61.407 -95.822  1.00 120.02 ? 141  VAL   D HG12 1 
ATOM   21430 H  HG13 . VAL   D  4  141 ? 20.833  -62.302 -94.515  1.00 120.02 ? 141  VAL   D HG13 1 
ATOM   21431 H  HG21 . VAL   D  4  141 ? 20.515  -64.966 -95.770  1.00 119.19 ? 141  VAL   D HG21 1 
ATOM   21432 H  HG22 . VAL   D  4  141 ? 19.719  -64.554 -94.458  1.00 119.19 ? 141  VAL   D HG22 1 
ATOM   21433 H  HG23 . VAL   D  4  141 ? 18.930  -65.063 -95.740  1.00 119.19 ? 141  VAL   D HG23 1 
ATOM   21434 N  N    . THR   D  4  142 ? 17.536  -63.397 -93.353  1.00 97.03  ? 142  THR   D N    1 
ATOM   21435 C  CA   . THR   D  4  142 ? 17.424  -63.528 -91.907  1.00 89.23  ? 142  THR   D CA   1 
ATOM   21436 C  C    . THR   D  4  142 ? 18.199  -64.764 -91.468  1.00 85.20  ? 142  THR   D C    1 
ATOM   21437 O  O    . THR   D  4  142 ? 17.898  -65.879 -91.907  1.00 86.32  ? 142  THR   D O    1 
ATOM   21438 C  CB   . THR   D  4  142 ? 15.960  -63.630 -91.474  1.00 89.01  ? 142  THR   D CB   1 
ATOM   21439 O  OG1  . THR   D  4  142 ? 15.263  -62.437 -91.857  1.00 92.31  ? 142  THR   D OG1  1 
ATOM   21440 C  CG2  . THR   D  4  142 ? 15.849  -63.815 -89.961  1.00 83.58  ? 142  THR   D CG2  1 
ATOM   21441 H  H    . THR   D  4  142 ? 17.108  -64.006 -93.784  1.00 116.48 ? 142  THR   D H    1 
ATOM   21442 H  HA   . THR   D  4  142 ? 17.814  -62.750 -91.480  1.00 107.12 ? 142  THR   D HA   1 
ATOM   21443 H  HB   . THR   D  4  142 ? 15.553  -64.398 -91.903  1.00 106.85 ? 142  THR   D HB   1 
ATOM   21444 H  HG1  . THR   D  4  142 ? 15.589  -61.773 -91.459  1.00 110.81 ? 142  THR   D HG1  1 
ATOM   21445 H  HG21 . THR   D  4  142 ? 14.916  -63.839 -89.698  1.00 100.33 ? 142  THR   D HG21 1 
ATOM   21446 H  HG22 . THR   D  4  142 ? 16.272  -64.646 -89.697  1.00 100.33 ? 142  THR   D HG22 1 
ATOM   21447 H  HG23 . THR   D  4  142 ? 16.287  -63.080 -89.504  1.00 100.33 ? 142  THR   D HG23 1 
ATOM   21448 N  N    . LEU   D  4  143 ? 19.204  -64.558 -90.623  1.00 84.13  ? 143  LEU   D N    1 
ATOM   21449 C  CA   . LEU   D  4  143 ? 19.912  -65.632 -89.946  1.00 83.20  ? 143  LEU   D CA   1 
ATOM   21450 C  C    . LEU   D  4  143 ? 19.487  -65.657 -88.483  1.00 81.30  ? 143  LEU   D C    1 
ATOM   21451 O  O    . LEU   D  4  143 ? 18.895  -64.703 -87.972  1.00 78.90  ? 143  LEU   D O    1 
ATOM   21452 C  CB   . LEU   D  4  143 ? 21.429  -65.450 -90.052  1.00 82.23  ? 143  LEU   D CB   1 
ATOM   21453 C  CG   . LEU   D  4  143 ? 22.027  -65.371 -91.458  1.00 87.15  ? 143  LEU   D CG   1 
ATOM   21454 C  CD1  . LEU   D  4  143 ? 23.531  -65.192 -91.362  1.00 87.94  ? 143  LEU   D CD1  1 
ATOM   21455 C  CD2  . LEU   D  4  143 ? 21.683  -66.604 -92.279  1.00 90.82  ? 143  LEU   D CD2  1 
ATOM   21456 H  H    . LEU   D  4  143 ? 19.501  -63.777 -90.421  1.00 100.99 ? 143  LEU   D H    1 
ATOM   21457 H  HA   . LEU   D  4  143 ? 19.694  -66.484 -90.354  1.00 99.88  ? 143  LEU   D HA   1 
ATOM   21458 H  HB2  . LEU   D  4  143 ? 21.662  -64.624 -89.600  1.00 98.71  ? 143  LEU   D HB2  1 
ATOM   21459 H  HB3  . LEU   D  4  143 ? 21.851  -66.202 -89.607  1.00 98.71  ? 143  LEU   D HB3  1 
ATOM   21460 H  HG   . LEU   D  4  143 ? 21.647  -64.608 -91.920  1.00 104.62 ? 143  LEU   D HG   1 
ATOM   21461 H  HD11 . LEU   D  4  143 ? 23.894  -65.082 -92.255  1.00 105.56 ? 143  LEU   D HD11 1 
ATOM   21462 H  HD12 . LEU   D  4  143 ? 23.722  -64.405 -90.828  1.00 105.56 ? 143  LEU   D HD12 1 
ATOM   21463 H  HD13 . LEU   D  4  143 ? 23.917  -65.977 -90.943  1.00 105.56 ? 143  LEU   D HD13 1 
ATOM   21464 H  HD21 . LEU   D  4  143 ? 22.052  -66.503 -93.170  1.00 109.02 ? 143  LEU   D HD21 1 
ATOM   21465 H  HD22 . LEU   D  4  143 ? 22.064  -67.386 -91.850  1.00 109.02 ? 143  LEU   D HD22 1 
ATOM   21466 H  HD23 . LEU   D  4  143 ? 20.718  -66.692 -92.329  1.00 109.02 ? 143  LEU   D HD23 1 
ATOM   21467 N  N    . GLY   D  4  144 ? 19.798  -66.764 -87.803  1.00 82.66  ? 144  GLY   D N    1 
ATOM   21468 C  CA   . GLY   D  4  144 ? 19.359  -66.945 -86.437  1.00 82.23  ? 144  GLY   D CA   1 
ATOM   21469 C  C    . GLY   D  4  144 ? 20.414  -67.619 -85.584  1.00 80.67  ? 144  GLY   D C    1 
ATOM   21470 O  O    . GLY   D  4  144 ? 21.419  -68.138 -86.079  1.00 83.83  ? 144  GLY   D O    1 
ATOM   21471 H  H    . GLY   D  4  144 ? 20.260  -67.417 -88.118  1.00 99.23  ? 144  GLY   D H    1 
ATOM   21472 H  HA2  . GLY   D  4  144 ? 19.155  -66.081 -86.047  1.00 98.71  ? 144  GLY   D HA2  1 
ATOM   21473 H  HA3  . GLY   D  4  144 ? 18.559  -67.494 -86.426  1.00 98.71  ? 144  GLY   D HA3  1 
ATOM   21474 N  N    . CYS   D  4  145 ? 20.155  -67.604 -84.278  1.00 76.90  ? 145  CYS   D N    1 
ATOM   21475 C  CA   . CYS   D  4  145 ? 21.013  -68.252 -83.296  1.00 76.54  ? 145  CYS   D CA   1 
ATOM   21476 C  C    . CYS   D  4  145 ? 20.132  -68.745 -82.159  1.00 72.24  ? 145  CYS   D C    1 
ATOM   21477 O  O    . CYS   D  4  145 ? 19.293  -67.993 -81.655  1.00 69.34  ? 145  CYS   D O    1 
ATOM   21478 C  CB   . CYS   D  4  145 ? 22.080  -67.288 -82.769  1.00 80.99  ? 145  CYS   D CB   1 
ATOM   21479 S  SG   . CYS   D  4  145 ? 23.446  -68.075 -81.889  1.00 87.64  ? 145  CYS   D SG   1 
ATOM   21480 H  H    . CYS   D  4  145 ? 19.472  -67.215 -83.930  1.00 92.32  ? 145  CYS   D H    1 
ATOM   21481 H  HA   . CYS   D  4  145 ? 21.468  -69.010 -83.695  1.00 91.88  ? 145  CYS   D HA   1 
ATOM   21482 H  HB2  . CYS   D  4  145 ? 22.457  -66.806 -83.522  1.00 97.23  ? 145  CYS   D HB2  1 
ATOM   21483 H  HB3  . CYS   D  4  145 ? 21.658  -66.667 -82.156  1.00 97.23  ? 145  CYS   D HB3  1 
ATOM   21484 N  N    . LEU   D  4  146 ? 20.321  -70.002 -81.765  1.00 70.24  ? 146  LEU   D N    1 
ATOM   21485 C  CA   . LEU   D  4  146 ? 19.528  -70.635 -80.718  1.00 68.70  ? 146  LEU   D CA   1 
ATOM   21486 C  C    . LEU   D  4  146 ? 20.446  -70.986 -79.556  1.00 71.12  ? 146  LEU   D C    1 
ATOM   21487 O  O    . LEU   D  4  146 ? 21.421  -71.726 -79.732  1.00 73.58  ? 146  LEU   D O    1 
ATOM   21488 C  CB   . LEU   D  4  146 ? 18.822  -71.883 -81.256  1.00 68.96  ? 146  LEU   D CB   1 
ATOM   21489 C  CG   . LEU   D  4  146 ? 17.995  -72.721 -80.279  1.00 68.45  ? 146  LEU   D CG   1 
ATOM   21490 C  CD1  . LEU   D  4  146 ? 16.798  -71.940 -79.761  1.00 67.45  ? 146  LEU   D CD1  1 
ATOM   21491 C  CD2  . LEU   D  4  146 ? 17.542  -74.012 -80.950  1.00 69.96  ? 146  LEU   D CD2  1 
ATOM   21492 H  H    . LEU   D  4  146 ? 20.920  -70.520 -82.100  1.00 84.32  ? 146  LEU   D H    1 
ATOM   21493 H  HA   . LEU   D  4  146 ? 18.854  -70.018 -80.394  1.00 82.48  ? 146  LEU   D HA   1 
ATOM   21494 H  HB2  . LEU   D  4  146 ? 18.217  -71.598 -81.959  1.00 82.79  ? 146  LEU   D HB2  1 
ATOM   21495 H  HB3  . LEU   D  4  146 ? 19.501  -72.471 -81.621  1.00 82.79  ? 146  LEU   D HB3  1 
ATOM   21496 H  HG   . LEU   D  4  146 ? 18.547  -72.948 -79.515  1.00 82.17  ? 146  LEU   D HG   1 
ATOM   21497 H  HD11 . LEU   D  4  146 ? 16.301  -72.497 -79.142  1.00 80.98  ? 146  LEU   D HD11 1 
ATOM   21498 H  HD12 . LEU   D  4  146 ? 17.114  -71.143 -79.307  1.00 80.98  ? 146  LEU   D HD12 1 
ATOM   21499 H  HD13 . LEU   D  4  146 ? 16.234  -71.692 -80.510  1.00 80.98  ? 146  LEU   D HD13 1 
ATOM   21500 H  HD21 . LEU   D  4  146 ? 17.062  -74.553 -80.303  1.00 83.99  ? 146  LEU   D HD21 1 
ATOM   21501 H  HD22 . LEU   D  4  146 ? 16.961  -73.794 -81.695  1.00 83.99  ? 146  LEU   D HD22 1 
ATOM   21502 H  HD23 . LEU   D  4  146 ? 18.322  -74.493 -81.269  1.00 83.99  ? 146  LEU   D HD23 1 
ATOM   21503 N  N    . VAL   D  4  147 ? 20.138  -70.451 -78.378  1.00 65.98  ? 147  VAL   D N    1 
ATOM   21504 C  CA   . VAL   D  4  147 ? 20.889  -70.710 -77.154  1.00 67.04  ? 147  VAL   D CA   1 
ATOM   21505 C  C    . VAL   D  4  147 ? 19.971  -71.502 -76.234  1.00 70.16  ? 147  VAL   D C    1 
ATOM   21506 O  O    . VAL   D  4  147 ? 18.969  -70.971 -75.739  1.00 70.71  ? 147  VAL   D O    1 
ATOM   21507 C  CB   . VAL   D  4  147 ? 21.360  -69.412 -76.485  1.00 66.61  ? 147  VAL   D CB   1 
ATOM   21508 C  CG1  . VAL   D  4  147 ? 22.316  -69.718 -75.339  1.00 70.20  ? 147  VAL   D CG1  1 
ATOM   21509 C  CG2  . VAL   D  4  147 ? 22.012  -68.486 -77.506  1.00 64.31  ? 147  VAL   D CG2  1 
ATOM   21510 H  H    . VAL   D  4  147 ? 19.475  -69.916 -78.259  1.00 79.21  ? 147  VAL   D H    1 
ATOM   21511 H  HA   . VAL   D  4  147 ? 21.671  -71.246 -77.357  1.00 80.48  ? 147  VAL   D HA   1 
ATOM   21512 H  HB   . VAL   D  4  147 ? 20.590  -68.951 -76.117  1.00 79.96  ? 147  VAL   D HB   1 
ATOM   21513 H  HG11 . VAL   D  4  147 ? 22.597  -68.884 -74.931  1.00 84.27  ? 147  VAL   D HG11 1 
ATOM   21514 H  HG12 . VAL   D  4  147 ? 21.858  -70.269 -74.685  1.00 84.27  ? 147  VAL   D HG12 1 
ATOM   21515 H  HG13 . VAL   D  4  147 ? 23.087  -70.192 -75.688  1.00 84.27  ? 147  VAL   D HG13 1 
ATOM   21516 H  HG21 . VAL   D  4  147 ? 22.291  -67.671 -77.060  1.00 77.20  ? 147  VAL   D HG21 1 
ATOM   21517 H  HG22 . VAL   D  4  147 ? 22.783  -68.932 -77.890  1.00 77.20  ? 147  VAL   D HG22 1 
ATOM   21518 H  HG23 . VAL   D  4  147 ? 21.368  -68.279 -78.201  1.00 77.20  ? 147  VAL   D HG23 1 
ATOM   21519 N  N    . LYS   D  4  148 ? 20.307  -72.768 -75.994  1.00 73.41  ? 148  LYS   D N    1 
ATOM   21520 C  CA   . LYS   D  4  148 ? 19.397  -73.695 -75.340  1.00 79.96  ? 148  LYS   D CA   1 
ATOM   21521 C  C    . LYS   D  4  148 ? 20.062  -74.366 -74.147  1.00 83.44  ? 148  LYS   D C    1 
ATOM   21522 O  O    . LYS   D  4  148 ? 21.271  -74.615 -74.142  1.00 81.66  ? 148  LYS   D O    1 
ATOM   21523 C  CB   . LYS   D  4  148 ? 18.913  -74.761 -76.335  1.00 82.97  ? 148  LYS   D CB   1 
ATOM   21524 C  CG   . LYS   D  4  148 ? 17.636  -75.472 -75.931  1.00 86.77  ? 148  LYS   D CG   1 
ATOM   21525 C  CD   . LYS   D  4  148 ? 17.093  -76.294 -77.091  1.00 87.17  ? 148  LYS   D CD   1 
ATOM   21526 C  CE   . LYS   D  4  148 ? 15.919  -77.161 -76.672  1.00 89.68  ? 148  LYS   D CE   1 
ATOM   21527 N  NZ   . LYS   D  4  148 ? 16.289  -78.113 -75.589  1.00 87.85  ? 148  LYS   D NZ   1 
ATOM   21528 H  H    . LYS   D  4  148 ? 21.066  -73.114 -76.203  1.00 88.13  ? 148  LYS   D H    1 
ATOM   21529 H  HA   . LYS   D  4  148 ? 18.633  -73.206 -74.996  1.00 95.99  ? 148  LYS   D HA   1 
ATOM   21530 H  HB2  . LYS   D  4  148 ? 18.750  -74.332 -77.190  1.00 99.60  ? 148  LYS   D HB2  1 
ATOM   21531 H  HB3  . LYS   D  4  148 ? 19.606  -75.433 -76.427  1.00 99.60  ? 148  LYS   D HB3  1 
ATOM   21532 H  HG2  . LYS   D  4  148 ? 17.818  -76.069 -75.188  1.00 104.16 ? 148  LYS   D HG2  1 
ATOM   21533 H  HG3  . LYS   D  4  148 ? 16.967  -74.819 -75.675  1.00 104.16 ? 148  LYS   D HG3  1 
ATOM   21534 H  HD2  . LYS   D  4  148 ? 16.793  -75.696 -77.793  1.00 104.64 ? 148  LYS   D HD2  1 
ATOM   21535 H  HD3  . LYS   D  4  148 ? 17.794  -76.875 -77.426  1.00 104.64 ? 148  LYS   D HD3  1 
ATOM   21536 H  HE2  . LYS   D  4  148 ? 15.204  -76.593 -76.345  1.00 107.65 ? 148  LYS   D HE2  1 
ATOM   21537 H  HE3  . LYS   D  4  148 ? 15.612  -77.674 -77.435  1.00 107.65 ? 148  LYS   D HE3  1 
ATOM   21538 H  HZ1  . LYS   D  4  148 ? 15.667  -78.746 -75.514  1.00 105.46 ? 148  LYS   D HZ1  1 
ATOM   21539 H  HZ2  . LYS   D  4  148 ? 17.070  -78.497 -75.774  1.00 105.46 ? 148  LYS   D HZ2  1 
ATOM   21540 H  HZ3  . LYS   D  4  148 ? 16.356  -77.682 -74.813  1.00 105.46 ? 148  LYS   D HZ3  1 
ATOM   21541 N  N    . GLY   D  4  149 ? 19.249  -74.649 -73.130  1.00 86.12  ? 149  GLY   D N    1 
ATOM   21542 C  CA   . GLY   D  4  149 ? 19.667  -75.437 -71.986  1.00 93.53  ? 149  GLY   D CA   1 
ATOM   21543 C  C    . GLY   D  4  149 ? 20.773  -74.834 -71.145  1.00 93.71  ? 149  GLY   D C    1 
ATOM   21544 O  O    . GLY   D  4  149 ? 21.718  -75.536 -70.772  1.00 98.23  ? 149  GLY   D O    1 
ATOM   21545 H  H    . GLY   D  4  149 ? 18.431  -74.387 -73.082  1.00 103.38 ? 149  GLY   D H    1 
ATOM   21546 H  HA2  . GLY   D  4  149 ? 18.900  -75.572 -71.408  1.00 112.28 ? 149  GLY   D HA2  1 
ATOM   21547 H  HA3  . GLY   D  4  149 ? 19.979  -76.299 -72.303  1.00 112.28 ? 149  GLY   D HA3  1 
ATOM   21548 N  N    . TYR   D  4  150 ? 20.668  -73.547 -70.824  1.00 89.59  ? 150  TYR   D N    1 
ATOM   21549 C  CA   . TYR   D  4  150 ? 21.648  -72.869 -69.989  1.00 88.85  ? 150  TYR   D CA   1 
ATOM   21550 C  C    . TYR   D  4  150 ? 20.980  -72.370 -68.715  1.00 88.27  ? 150  TYR   D C    1 
ATOM   21551 O  O    . TYR   D  4  150 ? 19.782  -72.074 -68.696  1.00 86.79  ? 150  TYR   D O    1 
ATOM   21552 C  CB   . TYR   D  4  150 ? 22.300  -71.693 -70.729  1.00 85.85  ? 150  TYR   D CB   1 
ATOM   21553 C  CG   . TYR   D  4  150 ? 21.397  -70.494 -70.907  1.00 83.98  ? 150  TYR   D CG   1 
ATOM   21554 C  CD1  . TYR   D  4  150 ? 20.625  -70.345 -72.051  1.00 79.77  ? 150  TYR   D CD1  1 
ATOM   21555 C  CD2  . TYR   D  4  150 ? 21.322  -69.507 -69.933  1.00 86.15  ? 150  TYR   D CD2  1 
ATOM   21556 C  CE1  . TYR   D  4  150 ? 19.801  -69.249 -72.218  1.00 77.53  ? 150  TYR   D CE1  1 
ATOM   21557 C  CE2  . TYR   D  4  150 ? 20.500  -68.410 -70.090  1.00 84.98  ? 150  TYR   D CE2  1 
ATOM   21558 C  CZ   . TYR   D  4  150 ? 19.743  -68.285 -71.234  1.00 81.09  ? 150  TYR   D CZ   1 
ATOM   21559 O  OH   . TYR   D  4  150 ? 18.924  -67.191 -71.394  1.00 80.92  ? 150  TYR   D OH   1 
ATOM   21560 H  H    . TYR   D  4  150 ? 20.025  -73.038 -71.084  1.00 107.54 ? 150  TYR   D H    1 
ATOM   21561 H  HA   . TYR   D  4  150 ? 22.349  -73.492 -69.742  1.00 106.66 ? 150  TYR   D HA   1 
ATOM   21562 H  HB2  . TYR   D  4  150 ? 23.078  -71.404 -70.226  1.00 103.06 ? 150  TYR   D HB2  1 
ATOM   21563 H  HB3  . TYR   D  4  150 ? 22.569  -71.993 -71.611  1.00 103.06 ? 150  TYR   D HB3  1 
ATOM   21564 H  HD1  . TYR   D  4  150 ? 20.663  -70.994 -72.716  1.00 95.76  ? 150  TYR   D HD1  1 
ATOM   21565 H  HD2  . TYR   D  4  150 ? 21.835  -69.587 -69.162  1.00 103.41 ? 150  TYR   D HD2  1 
ATOM   21566 H  HE1  . TYR   D  4  150 ? 19.288  -69.162 -72.989  1.00 93.08  ? 150  TYR   D HE1  1 
ATOM   21567 H  HE2  . TYR   D  4  150 ? 20.458  -67.759 -69.427  1.00 102.01 ? 150  TYR   D HE2  1 
ATOM   21568 H  HH   . TYR   D  4  150 ? 19.073  -66.629 -70.787  1.00 97.14  ? 150  TYR   D HH   1 
ATOM   21569 N  N    . PHE   D  4  151 ? 21.774  -72.273 -67.645  1.00 90.72  ? 151  PHE   D N    1 
ATOM   21570 C  CA   . PHE   D  4  151 ? 21.254  -71.842 -66.355  1.00 89.70  ? 151  PHE   D CA   1 
ATOM   21571 C  C    . PHE   D  4  151 ? 22.416  -71.387 -65.493  1.00 91.79  ? 151  PHE   D C    1 
ATOM   21572 O  O    . PHE   D  4  151 ? 23.468  -72.040 -65.510  1.00 93.34  ? 151  PHE   D O    1 
ATOM   21573 C  CB   . PHE   D  4  151 ? 20.493  -72.981 -65.666  1.00 91.95  ? 151  PHE   D CB   1 
ATOM   21574 C  CG   . PHE   D  4  151 ? 19.901  -72.607 -64.334  1.00 97.11  ? 151  PHE   D CG   1 
ATOM   21575 C  CD1  . PHE   D  4  151 ? 20.680  -72.605 -63.188  1.00 102.97 ? 151  PHE   D CD1  1 
ATOM   21576 C  CD2  . PHE   D  4  151 ? 18.559  -72.280 -64.224  1.00 97.23  ? 151  PHE   D CD2  1 
ATOM   21577 C  CE1  . PHE   D  4  151 ? 20.137  -72.269 -61.963  1.00 108.75 ? 151  PHE   D CE1  1 
ATOM   21578 C  CE2  . PHE   D  4  151 ? 18.010  -71.945 -63.000  1.00 102.52 ? 151  PHE   D CE2  1 
ATOM   21579 C  CZ   . PHE   D  4  151 ? 18.801  -71.941 -61.869  1.00 108.12 ? 151  PHE   D CZ   1 
ATOM   21580 H  H    . PHE   D  4  151 ? 22.615  -72.451 -67.645  1.00 108.90 ? 151  PHE   D H    1 
ATOM   21581 H  HA   . PHE   D  4  151 ? 20.652  -71.091 -66.475  1.00 107.67 ? 151  PHE   D HA   1 
ATOM   21582 H  HB2  . PHE   D  4  151 ? 19.766  -73.262 -66.243  1.00 110.38 ? 151  PHE   D HB2  1 
ATOM   21583 H  HB3  . PHE   D  4  151 ? 21.105  -73.719 -65.519  1.00 110.38 ? 151  PHE   D HB3  1 
ATOM   21584 H  HD1  . PHE   D  4  151 ? 21.580  -72.832 -63.245  1.00 123.61 ? 151  PHE   D HD1  1 
ATOM   21585 H  HD2  . PHE   D  4  151 ? 18.021  -72.286 -64.983  1.00 116.71 ? 151  PHE   D HD2  1 
ATOM   21586 H  HE1  . PHE   D  4  151 ? 20.673  -72.264 -61.203  1.00 130.54 ? 151  PHE   D HE1  1 
ATOM   21587 H  HE2  . PHE   D  4  151 ? 17.109  -71.723 -62.939  1.00 123.06 ? 151  PHE   D HE2  1 
ATOM   21588 H  HZ   . PHE   D  4  151 ? 18.433  -71.717 -61.044  1.00 129.78 ? 151  PHE   D HZ   1 
ATOM   21589 N  N    . PRO   D  4  152 ? 22.281  -70.285 -64.736  1.00 92.66  ? 152  PRO   D N    1 
ATOM   21590 C  CA   . PRO   D  4  152 ? 21.127  -69.384 -64.683  1.00 91.18  ? 152  PRO   D CA   1 
ATOM   21591 C  C    . PRO   D  4  152 ? 21.216  -68.272 -65.714  1.00 88.17  ? 152  PRO   D C    1 
ATOM   21592 O  O    . PRO   D  4  152 ? 22.205  -68.189 -66.443  1.00 82.77  ? 152  PRO   D O    1 
ATOM   21593 C  CB   . PRO   D  4  152 ? 21.219  -68.805 -63.274  1.00 94.60  ? 152  PRO   D CB   1 
ATOM   21594 C  CG   . PRO   D  4  152 ? 22.690  -68.699 -63.046  1.00 96.52  ? 152  PRO   D CG   1 
ATOM   21595 C  CD   . PRO   D  4  152 ? 23.310  -69.889 -63.756  1.00 96.25  ? 152  PRO   D CD   1 
ATOM   21596 H  HA   . PRO   D  4  152 ? 20.296  -69.871 -64.794  1.00 109.45 ? 152  PRO   D HA   1 
ATOM   21597 H  HB2  . PRO   D  4  152 ? 20.792  -67.934 -63.239  1.00 113.56 ? 152  PRO   D HB2  1 
ATOM   21598 H  HB3  . PRO   D  4  152 ? 20.803  -69.404 -62.635  1.00 113.56 ? 152  PRO   D HB3  1 
ATOM   21599 H  HG2  . PRO   D  4  152 ? 23.020  -67.867 -63.419  1.00 115.86 ? 152  PRO   D HG2  1 
ATOM   21600 H  HG3  . PRO   D  4  152 ? 22.876  -68.733 -62.094  1.00 115.86 ? 152  PRO   D HG3  1 
ATOM   21601 H  HD2  . PRO   D  4  152 ? 24.131  -69.632 -64.204  1.00 115.54 ? 152  PRO   D HD2  1 
ATOM   21602 H  HD3  . PRO   D  4  152 ? 23.485  -70.610 -63.131  1.00 115.54 ? 152  PRO   D HD3  1 
ATOM   21603 N  N    . GLU   D  4  153 ? 20.191  -67.430 -65.779  1.00 90.92  ? 153  GLU   D N    1 
ATOM   21604 C  CA   . GLU   D  4  153 ? 20.373  -66.128 -66.390  1.00 93.64  ? 153  GLU   D CA   1 
ATOM   21605 C  C    . GLU   D  4  153 ? 21.524  -65.421 -65.674  1.00 93.18  ? 153  GLU   D C    1 
ATOM   21606 O  O    . GLU   D  4  153 ? 21.784  -65.684 -64.495  1.00 96.08  ? 153  GLU   D O    1 
ATOM   21607 C  CB   . GLU   D  4  153 ? 19.095  -65.296 -66.293  1.00 99.08  ? 153  GLU   D CB   1 
ATOM   21608 C  CG   . GLU   D  4  153 ? 17.935  -65.819 -67.134  1.00 96.39  ? 153  GLU   D CG   1 
ATOM   21609 C  CD   . GLU   D  4  153 ? 17.922  -65.254 -68.541  1.00 91.80  ? 153  GLU   D CD   1 
ATOM   21610 O  OE1  . GLU   D  4  153 ? 17.040  -64.420 -68.838  1.00 89.15  ? 153  GLU   D OE1  1 
ATOM   21611 O  OE2  . GLU   D  4  153 ? 18.792  -65.642 -69.348  1.00 85.98  ? 153  GLU   D OE2  1 
ATOM   21612 H  H    . GLU   D  4  153 ? 19.399  -67.588 -65.482  1.00 109.14 ? 153  GLU   D H    1 
ATOM   21613 H  HA   . GLU   D  4  153 ? 20.582  -66.218 -67.333  1.00 112.40 ? 153  GLU   D HA   1 
ATOM   21614 H  HB2  . GLU   D  4  153 ? 18.803  -65.284 -65.368  1.00 118.93 ? 153  GLU   D HB2  1 
ATOM   21615 H  HB3  . GLU   D  4  153 ? 19.290  -64.394 -66.592  1.00 118.93 ? 153  GLU   D HB3  1 
ATOM   21616 H  HG2  . GLU   D  4  153 ? 18.004  -66.784 -67.200  1.00 115.71 ? 153  GLU   D HG2  1 
ATOM   21617 H  HG3  . GLU   D  4  153 ? 17.100  -65.574 -66.706  1.00 115.71 ? 153  GLU   D HG3  1 
ATOM   21618 N  N    . PRO   D  4  154 ? 22.237  -64.515 -66.355  1.00 90.43  ? 154  PRO   D N    1 
ATOM   21619 C  CA   . PRO   D  4  154 ? 22.028  -64.082 -67.734  1.00 85.27  ? 154  PRO   D CA   1 
ATOM   21620 C  C    . PRO   D  4  154 ? 22.950  -64.744 -68.748  1.00 86.86  ? 154  PRO   D C    1 
ATOM   21621 O  O    . PRO   D  4  154 ? 23.953  -65.366 -68.396  1.00 92.09  ? 154  PRO   D O    1 
ATOM   21622 C  CB   . PRO   D  4  154 ? 22.333  -62.588 -67.655  1.00 85.91  ? 154  PRO   D CB   1 
ATOM   21623 C  CG   . PRO   D  4  154 ? 23.455  -62.522 -66.654  1.00 90.69  ? 154  PRO   D CG   1 
ATOM   21624 C  CD   . PRO   D  4  154 ? 23.247  -63.677 -65.684  1.00 90.80  ? 154  PRO   D CD   1 
ATOM   21625 H  HA   . PRO   D  4  154 ? 21.109  -64.245 -67.998  1.00 102.37 ? 154  PRO   D HA   1 
ATOM   21626 H  HB2  . PRO   D  4  154 ? 22.611  -62.254 -68.522  1.00 103.13 ? 154  PRO   D HB2  1 
ATOM   21627 H  HB3  . PRO   D  4  154 ? 21.553  -62.101 -67.347  1.00 103.13 ? 154  PRO   D HB3  1 
ATOM   21628 H  HG2  . PRO   D  4  154 ? 24.304  -62.612 -67.113  1.00 108.87 ? 154  PRO   D HG2  1 
ATOM   21629 H  HG3  . PRO   D  4  154 ? 23.420  -61.673 -66.185  1.00 108.87 ? 154  PRO   D HG3  1 
ATOM   21630 H  HD2  . PRO   D  4  154 ? 24.073  -64.170 -65.554  1.00 108.99 ? 154  PRO   D HD2  1 
ATOM   21631 H  HD3  . PRO   D  4  154 ? 22.916  -63.355 -64.831  1.00 108.99 ? 154  PRO   D HD3  1 
ATOM   21632 N  N    . VAL   D  4  155 ? 22.577  -64.606 -70.014  1.00 85.86  ? 155  VAL   D N    1 
ATOM   21633 C  CA   . VAL   D  4  155 ? 23.462  -64.846 -71.144  1.00 85.51  ? 155  VAL   D CA   1 
ATOM   21634 C  C    . VAL   D  4  155 ? 23.525  -63.546 -71.931  1.00 81.93  ? 155  VAL   D C    1 
ATOM   21635 O  O    . VAL   D  4  155 ? 22.597  -62.731 -71.886  1.00 81.17  ? 155  VAL   D O    1 
ATOM   21636 C  CB   . VAL   D  4  155 ? 22.979  -66.012 -72.035  1.00 87.19  ? 155  VAL   D CB   1 
ATOM   21637 C  CG1  . VAL   D  4  155 ? 21.680  -65.647 -72.744  1.00 89.50  ? 155  VAL   D CG1  1 
ATOM   21638 C  CG2  . VAL   D  4  155 ? 24.053  -66.406 -73.042  1.00 86.57  ? 155  VAL   D CG2  1 
ATOM   21639 H  H    . VAL   D  4  155 ? 21.787  -64.364 -70.253  1.00 103.07 ? 155  VAL   D H    1 
ATOM   21640 H  HA   . VAL   D  4  155 ? 24.349  -65.082 -70.832  1.00 102.65 ? 155  VAL   D HA   1 
ATOM   21641 H  HB   . VAL   D  4  155 ? 22.806  -66.781 -71.469  1.00 104.67 ? 155  VAL   D HB   1 
ATOM   21642 H  HG11 . VAL   D  4  155 ? 21.368  -66.416 -73.246  1.00 107.43 ? 155  VAL   D HG11 1 
ATOM   21643 H  HG12 . VAL   D  4  155 ? 21.019  -65.394 -72.081  1.00 107.43 ? 155  VAL   D HG12 1 
ATOM   21644 H  HG13 . VAL   D  4  155 ? 21.847  -64.905 -73.346  1.00 107.43 ? 155  VAL   D HG13 1 
ATOM   21645 H  HG21 . VAL   D  4  155 ? 23.718  -67.131 -73.593  1.00 103.92 ? 155  VAL   D HG21 1 
ATOM   21646 H  HG22 . VAL   D  4  155 ? 24.262  -65.638 -73.597  1.00 103.92 ? 155  VAL   D HG22 1 
ATOM   21647 H  HG23 . VAL   D  4  155 ? 24.845  -66.693 -72.563  1.00 103.92 ? 155  VAL   D HG23 1 
ATOM   21648 N  N    . THR   D  4  156 ? 24.628  -63.343 -72.640  1.00 79.15  ? 156  THR   D N    1 
ATOM   21649 C  CA   . THR   D  4  156 ? 24.798  -62.180 -73.496  1.00 80.57  ? 156  THR   D CA   1 
ATOM   21650 C  C    . THR   D  4  156 ? 25.076  -62.650 -74.915  1.00 76.80  ? 156  THR   D C    1 
ATOM   21651 O  O    . THR   D  4  156 ? 25.875  -63.566 -75.130  1.00 78.46  ? 156  THR   D O    1 
ATOM   21652 C  CB   . THR   D  4  156 ? 25.934  -61.278 -73.007  1.00 87.12  ? 156  THR   D CB   1 
ATOM   21653 O  OG1  . THR   D  4  156 ? 27.187  -61.951 -73.167  1.00 90.28  ? 156  THR   D OG1  1 
ATOM   21654 C  CG2  . THR   D  4  156 ? 25.734  -60.920 -71.542  1.00 92.03  ? 156  THR   D CG2  1 
ATOM   21655 H  H    . THR   D  4  156 ? 25.303  -63.876 -72.640  1.00 95.02  ? 156  THR   D H    1 
ATOM   21656 H  HA   . THR   D  4  156 ? 23.985  -61.650 -73.495  1.00 96.72  ? 156  THR   D HA   1 
ATOM   21657 H  HB   . THR   D  4  156 ? 25.942  -60.458 -73.525  1.00 104.58 ? 156  THR   D HB   1 
ATOM   21658 H  HG1  . THR   D  4  156 ? 27.819  -61.431 -72.977  1.00 108.37 ? 156  THR   D HG1  1 
ATOM   21659 H  HG21 . THR   D  4  156 ? 26.450  -60.338 -71.242  1.00 110.48 ? 156  THR   D HG21 1 
ATOM   21660 H  HG22 . THR   D  4  156 ? 24.887  -60.462 -71.425  1.00 110.48 ? 156  THR   D HG22 1 
ATOM   21661 H  HG23 . THR   D  4  156 ? 25.734  -61.724 -71.000  1.00 110.48 ? 156  THR   D HG23 1 
ATOM   21662 N  N    . LEU   D  4  157 ? 24.408  -62.023 -75.878  1.00 72.23  ? 157  LEU   D N    1 
ATOM   21663 C  CA   . LEU   D  4  157 ? 24.487  -62.430 -77.271  1.00 69.10  ? 157  LEU   D CA   1 
ATOM   21664 C  C    . LEU   D  4  157 ? 24.751  -61.216 -78.146  1.00 69.41  ? 157  LEU   D C    1 
ATOM   21665 O  O    . LEU   D  4  157 ? 24.164  -60.149 -77.941  1.00 70.07  ? 157  LEU   D O    1 
ATOM   21666 C  CB   . LEU   D  4  157 ? 23.196  -63.128 -77.713  1.00 66.96  ? 157  LEU   D CB   1 
ATOM   21667 C  CG   . LEU   D  4  157 ? 23.163  -63.646 -79.150  1.00 66.53  ? 157  LEU   D CG   1 
ATOM   21668 C  CD1  . LEU   D  4  157 ? 22.328  -64.912 -79.223  1.00 68.39  ? 157  LEU   D CD1  1 
ATOM   21669 C  CD2  . LEU   D  4  157 ? 22.613  -62.590 -80.101  1.00 63.72  ? 157  LEU   D CD2  1 
ATOM   21670 H  H    . LEU   D  4  157 ? 23.894  -61.347 -75.743  1.00 86.71  ? 157  LEU   D H    1 
ATOM   21671 H  HA   . LEU   D  4  157 ? 25.226  -63.047 -77.390  1.00 82.95  ? 157  LEU   D HA   1 
ATOM   21672 H  HB2  . LEU   D  4  157 ? 23.053  -63.891 -77.131  1.00 80.39  ? 157  LEU   D HB2  1 
ATOM   21673 H  HB3  . LEU   D  4  157 ? 22.466  -62.497 -77.619  1.00 80.39  ? 157  LEU   D HB3  1 
ATOM   21674 H  HG   . LEU   D  4  157 ? 24.068  -63.850 -79.433  1.00 79.87  ? 157  LEU   D HG   1 
ATOM   21675 H  HD11 . LEU   D  4  157 ? 22.300  -65.219 -80.143  1.00 82.11  ? 157  LEU   D HD11 1 
ATOM   21676 H  HD12 . LEU   D  4  157 ? 22.732  -65.590 -78.660  1.00 82.11  ? 157  LEU   D HD12 1 
ATOM   21677 H  HD13 . LEU   D  4  157 ? 21.430  -64.716 -78.913  1.00 82.11  ? 157  LEU   D HD13 1 
ATOM   21678 H  HD21 . LEU   D  4  157 ? 22.558  -62.967 -80.993  1.00 76.50  ? 157  LEU   D HD21 1 
ATOM   21679 H  HD22 . LEU   D  4  157 ? 21.730  -62.324 -79.800  1.00 76.50  ? 157  LEU   D HD22 1 
ATOM   21680 H  HD23 . LEU   D  4  157 ? 23.207  -61.824 -80.101  1.00 76.50  ? 157  LEU   D HD23 1 
ATOM   21681 N  N    . THR   D  4  158 ? 25.636  -61.391 -79.124  1.00 71.95  ? 158  THR   D N    1 
ATOM   21682 C  CA   . THR   D  4  158 ? 25.944  -60.347 -80.089  1.00 74.95  ? 158  THR   D CA   1 
ATOM   21683 C  C    . THR   D  4  158 ? 26.219  -60.994 -81.438  1.00 76.97  ? 158  THR   D C    1 
ATOM   21684 O  O    . THR   D  4  158 ? 26.461  -62.200 -81.535  1.00 76.39  ? 158  THR   D O    1 
ATOM   21685 C  CB   . THR   D  4  158 ? 27.147  -59.501 -79.649  1.00 77.47  ? 158  THR   D CB   1 
ATOM   21686 O  OG1  . THR   D  4  158 ? 28.296  -60.341 -79.485  1.00 78.63  ? 158  THR   D OG1  1 
ATOM   21687 C  CG2  . THR   D  4  158 ? 26.850  -58.789 -78.338  1.00 78.28  ? 158  THR   D CG2  1 
ATOM   21688 H  H    . THR   D  4  158 ? 26.078  -62.118 -79.249  1.00 86.37  ? 158  THR   D H    1 
ATOM   21689 H  HA   . THR   D  4  158 ? 25.178  -59.758 -80.178  1.00 89.98  ? 158  THR   D HA   1 
ATOM   21690 H  HB   . THR   D  4  158 ? 27.333  -58.831 -80.326  1.00 93.00  ? 158  THR   D HB   1 
ATOM   21691 H  HG1  . THR   D  4  158 ? 28.574  -60.598 -80.235  1.00 94.39  ? 158  THR   D HG1  1 
ATOM   21692 H  HG21 . THR   D  4  158 ? 27.602  -58.229 -78.087  1.00 93.97  ? 158  THR   D HG21 1 
ATOM   21693 H  HG22 . THR   D  4  158 ? 26.061  -58.233 -78.434  1.00 93.97  ? 158  THR   D HG22 1 
ATOM   21694 H  HG23 . THR   D  4  158 ? 26.694  -59.440 -77.636  1.00 93.97  ? 158  THR   D HG23 1 
ATOM   21695 N  N    . TRP   D  4  159 ? 26.173  -60.173 -82.484  1.00 80.86  ? 159  TRP   D N    1 
ATOM   21696 C  CA   . TRP   D  4  159 ? 26.432  -60.612 -83.848  1.00 84.11  ? 159  TRP   D CA   1 
ATOM   21697 C  C    . TRP   D  4  159 ? 27.660  -59.888 -84.376  1.00 85.68  ? 159  TRP   D C    1 
ATOM   21698 O  O    . TRP   D  4  159 ? 27.726  -58.655 -84.327  1.00 86.18  ? 159  TRP   D O    1 
ATOM   21699 C  CB   . TRP   D  4  159 ? 25.226  -60.350 -84.750  1.00 87.01  ? 159  TRP   D CB   1 
ATOM   21700 C  CG   . TRP   D  4  159 ? 24.058  -61.219 -84.423  1.00 85.08  ? 159  TRP   D CG   1 
ATOM   21701 C  CD1  . TRP   D  4  159 ? 23.031  -60.928 -83.574  1.00 82.41  ? 159  TRP   D CD1  1 
ATOM   21702 C  CD2  . TRP   D  4  159 ? 23.799  -62.532 -84.932  1.00 83.88  ? 159  TRP   D CD2  1 
ATOM   21703 N  NE1  . TRP   D  4  159 ? 22.146  -61.977 -83.526  1.00 77.79  ? 159  TRP   D NE1  1 
ATOM   21704 C  CE2  . TRP   D  4  159 ? 22.595  -62.974 -84.351  1.00 79.83  ? 159  TRP   D CE2  1 
ATOM   21705 C  CE3  . TRP   D  4  159 ? 24.468  -63.375 -85.824  1.00 86.58  ? 159  TRP   D CE3  1 
ATOM   21706 C  CZ2  . TRP   D  4  159 ? 22.046  -64.222 -84.633  1.00 79.04  ? 159  TRP   D CZ2  1 
ATOM   21707 C  CZ3  . TRP   D  4  159 ? 23.921  -64.611 -86.103  1.00 88.96  ? 159  TRP   D CZ3  1 
ATOM   21708 C  CH2  . TRP   D  4  159 ? 22.722  -65.023 -85.511  1.00 85.46  ? 159  TRP   D CH2  1 
ATOM   21709 H  H    . TRP   D  4  159 ? 25.988  -59.336 -82.425  1.00 97.07  ? 159  TRP   D H    1 
ATOM   21710 H  HA   . TRP   D  4  159 ? 26.613  -61.565 -83.858  1.00 100.97 ? 159  TRP   D HA   1 
ATOM   21711 H  HB2  . TRP   D  4  159 ? 24.950  -59.426 -84.648  1.00 104.45 ? 159  TRP   D HB2  1 
ATOM   21712 H  HB3  . TRP   D  4  159 ? 25.478  -60.521 -85.671  1.00 104.45 ? 159  TRP   D HB3  1 
ATOM   21713 H  HD1  . TRP   D  4  159 ? 22.943  -60.134 -83.098  1.00 98.93  ? 159  TRP   D HD1  1 
ATOM   21714 H  HE1  . TRP   D  4  159 ? 21.428  -62.004 -83.054  1.00 93.39  ? 159  TRP   D HE1  1 
ATOM   21715 H  HE3  . TRP   D  4  159 ? 25.266  -63.108 -86.221  1.00 103.93 ? 159  TRP   D HE3  1 
ATOM   21716 H  HZ2  . TRP   D  4  159 ? 21.250  -64.500 -84.240  1.00 94.88  ? 159  TRP   D HZ2  1 
ATOM   21717 H  HZ3  . TRP   D  4  159 ? 24.357  -65.180 -86.696  1.00 106.79 ? 159  TRP   D HZ3  1 
ATOM   21718 H  HH2  . TRP   D  4  159 ? 22.377  -65.861 -85.720  1.00 102.59 ? 159  TRP   D HH2  1 
ATOM   21719 N  N    . ASN   D  4  160 ? 28.620  -60.655 -84.885  1.00 85.35  ? 160  ASN   D N    1 
ATOM   21720 C  CA   . ASN   D  4  160 ? 29.914  -60.125 -85.302  1.00 87.49  ? 160  ASN   D CA   1 
ATOM   21721 C  C    . ASN   D  4  160 ? 30.450  -59.146 -84.262  1.00 90.38  ? 160  ASN   D C    1 
ATOM   21722 O  O    . ASN   D  4  160 ? 30.906  -58.042 -84.571  1.00 93.89  ? 160  ASN   D O    1 
ATOM   21723 C  CB   . ASN   D  4  160 ? 29.822  -59.482 -86.684  1.00 89.03  ? 160  ASN   D CB   1 
ATOM   21724 C  CG   . ASN   D  4  160 ? 29.743  -60.510 -87.798  1.00 90.77  ? 160  ASN   D CG   1 
ATOM   21725 O  OD1  . ASN   D  4  160 ? 30.285  -61.609 -87.679  1.00 93.37  ? 160  ASN   D OD1  1 
ATOM   21726 N  ND2  . ASN   D  4  160 ? 29.069  -60.159 -88.886  1.00 92.16  ? 160  ASN   D ND2  1 
ATOM   21727 H  H    . ASN   D  4  160 ? 28.543  -61.504 -85.000  1.00 102.46 ? 160  ASN   D H    1 
ATOM   21728 H  HA   . ASN   D  4  160 ? 30.545  -60.860 -85.366  1.00 105.03 ? 160  ASN   D HA   1 
ATOM   21729 H  HB2  . ASN   D  4  160 ? 29.024  -58.931 -86.726  1.00 106.87 ? 160  ASN   D HB2  1 
ATOM   21730 H  HB3  . ASN   D  4  160 ? 30.609  -58.935 -86.833  1.00 106.87 ? 160  ASN   D HB3  1 
ATOM   21731 H  HD21 . ASN   D  4  160 ? 28.997  -60.709 -89.544  1.00 110.63 ? 160  ASN   D HD21 1 
ATOM   21732 H  HD22 . ASN   D  4  160 ? 28.704  -59.382 -88.934  1.00 110.63 ? 160  ASN   D HD22 1 
ATOM   21733 N  N    . SER   D  4  161 ? 30.371  -59.567 -82.998  1.00 93.16  ? 161  SER   D N    1 
ATOM   21734 C  CA   . SER   D  4  161 ? 30.974  -58.854 -81.876  1.00 95.38  ? 161  SER   D CA   1 
ATOM   21735 C  C    . SER   D  4  161 ? 30.278  -57.527 -81.590  1.00 96.28  ? 161  SER   D C    1 
ATOM   21736 O  O    . SER   D  4  161 ? 30.903  -56.589 -81.090  1.00 101.91 ? 161  SER   D O    1 
ATOM   21737 C  CB   . SER   D  4  161 ? 32.469  -58.623 -82.121  1.00 99.56  ? 161  SER   D CB   1 
ATOM   21738 O  OG   . SER   D  4  161 ? 33.081  -59.796 -82.630  1.00 98.61  ? 161  SER   D OG   1 
ATOM   21739 H  H    . SER   D  4  161 ? 29.960  -60.285 -82.761  1.00 111.83 ? 161  SER   D H    1 
ATOM   21740 H  HA   . SER   D  4  161 ? 30.874  -59.402 -81.082  1.00 114.49 ? 161  SER   D HA   1 
ATOM   21741 H  HB2  . SER   D  4  161 ? 32.576  -57.906 -82.765  1.00 119.51 ? 161  SER   D HB2  1 
ATOM   21742 H  HB3  . SER   D  4  161 ? 32.893  -58.383 -81.283  1.00 119.51 ? 161  SER   D HB3  1 
ATOM   21743 H  HG   . SER   D  4  161 ? 33.896  -59.654 -82.777  1.00 118.36 ? 161  SER   D HG   1 
ATOM   21744 N  N    . GLY   D  4  162 ? 28.985  -57.435 -81.890  1.00 91.64  ? 162  GLY   D N    1 
ATOM   21745 C  CA   . GLY   D  4  162 ? 28.240  -56.213 -81.683  1.00 92.17  ? 162  GLY   D CA   1 
ATOM   21746 C  C    . GLY   D  4  162 ? 28.293  -55.238 -82.836  1.00 93.76  ? 162  GLY   D C    1 
ATOM   21747 O  O    . GLY   D  4  162 ? 27.644  -54.186 -82.770  1.00 93.70  ? 162  GLY   D O    1 
ATOM   21748 H  H    . GLY   D  4  162 ? 28.518  -58.078 -82.218  1.00 110.00 ? 162  GLY   D H    1 
ATOM   21749 H  HA2  . GLY   D  4  162 ? 27.309  -56.438 -81.528  1.00 110.64 ? 162  GLY   D HA2  1 
ATOM   21750 H  HA3  . GLY   D  4  162 ? 28.590  -55.763 -80.898  1.00 110.64 ? 162  GLY   D HA3  1 
ATOM   21751 N  N    . SER   D  4  163 ? 29.053  -55.549 -83.888  1.00 107.17 ? 163  SER   D N    1 
ATOM   21752 C  CA   . SER   D  4  163 ? 29.083  -54.687 -85.064  1.00 110.46 ? 163  SER   D CA   1 
ATOM   21753 C  C    . SER   D  4  163 ? 27.703  -54.579 -85.700  1.00 111.51 ? 163  SER   D C    1 
ATOM   21754 O  O    . SER   D  4  163 ? 27.310  -53.506 -86.173  1.00 114.16 ? 163  SER   D O    1 
ATOM   21755 C  CB   . SER   D  4  163 ? 30.101  -55.228 -86.066  1.00 111.70 ? 163  SER   D CB   1 
ATOM   21756 O  OG   . SER   D  4  163 ? 29.949  -54.622 -87.333  1.00 115.72 ? 163  SER   D OG   1 
ATOM   21757 H  H    . SER   D  4  163 ? 29.553  -56.246 -83.944  1.00 128.64 ? 163  SER   D H    1 
ATOM   21758 H  HA   . SER   D  4  163 ? 29.359  -53.795 -84.802  1.00 132.59 ? 163  SER   D HA   1 
ATOM   21759 H  HB2  . SER   D  4  163 ? 30.994  -55.045 -85.736  1.00 134.08 ? 163  SER   D HB2  1 
ATOM   21760 H  HB3  . SER   D  4  163 ? 29.972  -56.185 -86.159  1.00 134.08 ? 163  SER   D HB3  1 
ATOM   21761 H  HG   . SER   D  4  163 ? 30.513  -54.934 -87.871  1.00 138.90 ? 163  SER   D HG   1 
ATOM   21762 N  N    . LEU   D  4  164 ? 26.953  -55.679 -85.718  1.00 109.14 ? 164  LEU   D N    1 
ATOM   21763 C  CA   . LEU   D  4  164 ? 25.598  -55.699 -86.258  1.00 103.26 ? 164  LEU   D CA   1 
ATOM   21764 C  C    . LEU   D  4  164 ? 24.619  -55.471 -85.111  1.00 102.59 ? 164  LEU   D C    1 
ATOM   21765 O  O    . LEU   D  4  164 ? 24.463  -56.333 -84.241  1.00 105.47 ? 164  LEU   D O    1 
ATOM   21766 C  CB   . LEU   D  4  164 ? 25.315  -57.026 -86.957  1.00 100.34 ? 164  LEU   D CB   1 
ATOM   21767 C  CG   . LEU   D  4  164 ? 26.311  -57.488 -88.024  1.00 103.75 ? 164  LEU   D CG   1 
ATOM   21768 C  CD1  . LEU   D  4  164 ? 25.954  -58.886 -88.512  1.00 104.94 ? 164  LEU   D CD1  1 
ATOM   21769 C  CD2  . LEU   D  4  164 ? 26.355  -56.514 -89.188  1.00 105.34 ? 164  LEU   D CD2  1 
ATOM   21770 H  H    . LEU   D  4  164 ? 27.214  -56.441 -85.418  1.00 131.00 ? 164  LEU   D H    1 
ATOM   21771 H  HA   . LEU   D  4  164 ? 25.497  -54.983 -86.905  1.00 123.95 ? 164  LEU   D HA   1 
ATOM   21772 H  HB2  . LEU   D  4  164 ? 25.288  -57.719 -86.279  1.00 120.44 ? 164  LEU   D HB2  1 
ATOM   21773 H  HB3  . LEU   D  4  164 ? 24.451  -56.954 -87.392  1.00 120.44 ? 164  LEU   D HB3  1 
ATOM   21774 H  HG   . LEU   D  4  164 ? 27.197  -57.517 -87.630  1.00 124.53 ? 164  LEU   D HG   1 
ATOM   21775 H  HD11 . LEU   D  4  164 ? 26.598  -59.160 -89.184  1.00 125.97 ? 164  LEU   D HD11 1 
ATOM   21776 H  HD12 . LEU   D  4  164 ? 25.980  -59.499 -87.760  1.00 125.97 ? 164  LEU   D HD12 1 
ATOM   21777 H  HD13 . LEU   D  4  164 ? 25.063  -58.869 -88.894  1.00 125.97 ? 164  LEU   D HD13 1 
ATOM   21778 H  HD21 . LEU   D  4  164 ? 26.992  -56.835 -89.845  1.00 126.45 ? 164  LEU   D HD21 1 
ATOM   21779 H  HD22 . LEU   D  4  164 ? 25.472  -56.455 -89.585  1.00 126.45 ? 164  LEU   D HD22 1 
ATOM   21780 H  HD23 . LEU   D  4  164 ? 26.629  -55.642 -88.861  1.00 126.45 ? 164  LEU   D HD23 1 
ATOM   21781 N  N    . SER   D  4  165 ? 23.963  -54.310 -85.105  1.00 105.21 ? 165  SER   D N    1 
ATOM   21782 C  CA   . SER   D  4  165 ? 22.969  -53.989 -84.085  1.00 106.76 ? 165  SER   D CA   1 
ATOM   21783 C  C    . SER   D  4  165 ? 21.602  -53.722 -84.701  1.00 104.11 ? 165  SER   D C    1 
ATOM   21784 O  O    . SER   D  4  165 ? 20.639  -54.422 -84.371  1.00 100.13 ? 165  SER   D O    1 
ATOM   21785 C  CB   . SER   D  4  165 ? 23.432  -52.787 -83.253  1.00 113.65 ? 165  SER   D CB   1 
ATOM   21786 O  OG   . SER   D  4  165 ? 23.520  -51.616 -84.045  1.00 120.08 ? 165  SER   D OG   1 
ATOM   21787 H  H    . SER   D  4  165 ? 24.078  -53.687 -85.687  1.00 126.29 ? 165  SER   D H    1 
ATOM   21788 H  HA   . SER   D  4  165 ? 22.883  -54.748 -83.487  1.00 128.15 ? 165  SER   D HA   1 
ATOM   21789 H  HB2  . SER   D  4  165 ? 22.795  -52.635 -82.538  1.00 136.42 ? 165  SER   D HB2  1 
ATOM   21790 H  HB3  . SER   D  4  165 ? 24.307  -52.981 -82.881  1.00 136.42 ? 165  SER   D HB3  1 
ATOM   21791 H  HG   . SER   D  4  165 ? 23.757  -50.965 -83.570  1.00 144.13 ? 165  SER   D HG   1 
ATOM   21792 N  N    . ALA   D  4  166 ? 21.481  -52.723 -85.574  1.00 104.88 ? 166  ALA   D N    1 
ATOM   21793 C  CA   . ALA   D  4  166 ? 20.254  -52.559 -86.340  1.00 105.82 ? 166  ALA   D CA   1 
ATOM   21794 C  C    . ALA   D  4  166 ? 19.909  -53.868 -87.038  1.00 100.30 ? 166  ALA   D C    1 
ATOM   21795 O  O    . ALA   D  4  166 ? 20.790  -54.625 -87.455  1.00 98.79  ? 166  ALA   D O    1 
ATOM   21796 C  CB   . ALA   D  4  166 ? 20.406  -51.435 -87.366  1.00 112.26 ? 166  ALA   D CB   1 
ATOM   21797 H  H    . ALA   D  4  166 ? 22.088  -52.136 -85.738  1.00 125.90 ? 166  ALA   D H    1 
ATOM   21798 H  HA   . ALA   D  4  166 ? 19.526  -52.318 -85.746  1.00 127.01 ? 166  ALA   D HA   1 
ATOM   21799 H  HB1  . ALA   D  4  166 ? 19.591  -51.371 -87.887  1.00 134.75 ? 166  ALA   D HB1  1 
ATOM   21800 H  HB2  . ALA   D  4  166 ? 20.567  -50.600 -86.899  1.00 134.75 ? 166  ALA   D HB2  1 
ATOM   21801 H  HB3  . ALA   D  4  166 ? 21.156  -51.638 -87.948  1.00 134.75 ? 166  ALA   D HB3  1 
ATOM   21802 N  N    . GLY   D  4  167 ? 18.613  -54.143 -87.152  1.00 96.79  ? 167  GLY   D N    1 
ATOM   21803 C  CA   . GLY   D  4  167 ? 18.178  -55.372 -87.781  1.00 94.33  ? 167  GLY   D CA   1 
ATOM   21804 C  C    . GLY   D  4  167 ? 18.364  -56.618 -86.948  1.00 91.23  ? 167  GLY   D C    1 
ATOM   21805 O  O    . GLY   D  4  167 ? 18.177  -57.723 -87.466  1.00 92.98  ? 167  GLY   D O    1 
ATOM   21806 H  H    . GLY   D  4  167 ? 17.976  -53.636 -86.875  1.00 116.18 ? 167  GLY   D H    1 
ATOM   21807 H  HA2  . GLY   D  4  167 ? 17.234  -55.296 -87.991  1.00 113.23 ? 167  GLY   D HA2  1 
ATOM   21808 H  HA3  . GLY   D  4  167 ? 18.675  -55.491 -88.606  1.00 113.23 ? 167  GLY   D HA3  1 
ATOM   21809 N  N    . VAL   D  4  168 ? 18.735  -56.478 -85.678  1.00 89.16  ? 168  VAL   D N    1 
ATOM   21810 C  CA   . VAL   D  4  168 ? 18.856  -57.604 -84.758  1.00 87.91  ? 168  VAL   D CA   1 
ATOM   21811 C  C    . VAL   D  4  168 ? 17.638  -57.612 -83.848  1.00 86.61  ? 168  VAL   D C    1 
ATOM   21812 O  O    . VAL   D  4  168 ? 17.152  -56.553 -83.430  1.00 84.80  ? 168  VAL   D O    1 
ATOM   21813 C  CB   . VAL   D  4  168 ? 20.157  -57.522 -83.937  1.00 85.13  ? 168  VAL   D CB   1 
ATOM   21814 C  CG1  . VAL   D  4  168 ? 20.233  -58.668 -82.933  1.00 84.20  ? 168  VAL   D CG1  1 
ATOM   21815 C  CG2  . VAL   D  4  168 ? 21.368  -57.536 -84.857  1.00 86.44  ? 168  VAL   D CG2  1 
ATOM   21816 H  H    . VAL   D  4  168 ? 18.926  -55.721 -85.317  1.00 107.03 ? 168  VAL   D H    1 
ATOM   21817 H  HA   . VAL   D  4  168 ? 18.874  -58.430 -85.266  1.00 105.53 ? 168  VAL   D HA   1 
ATOM   21818 H  HB   . VAL   D  4  168 ? 20.161  -56.688 -83.442  1.00 102.19 ? 168  VAL   D HB   1 
ATOM   21819 H  HG11 . VAL   D  4  168 ? 21.075  -58.612 -82.454  1.00 101.07 ? 168  VAL   D HG11 1 
ATOM   21820 H  HG12 . VAL   D  4  168 ? 19.493  -58.592 -82.311  1.00 101.07 ? 168  VAL   D HG12 1 
ATOM   21821 H  HG13 . VAL   D  4  168 ? 20.179  -59.510 -83.411  1.00 101.07 ? 168  VAL   D HG13 1 
ATOM   21822 H  HG21 . VAL   D  4  168 ? 22.174  -57.487 -84.319  1.00 103.76 ? 168  VAL   D HG21 1 
ATOM   21823 H  HG22 . VAL   D  4  168 ? 21.364  -58.359 -85.372  1.00 103.76 ? 168  VAL   D HG22 1 
ATOM   21824 H  HG23 . VAL   D  4  168 ? 21.321  -56.773 -85.453  1.00 103.76 ? 168  VAL   D HG23 1 
ATOM   21825 N  N    . HIS   D  4  169 ? 17.139  -58.808 -83.542  1.00 85.88  ? 169  HIS   D N    1 
ATOM   21826 C  CA   . HIS   D  4  169 ? 16.031  -58.977 -82.603  1.00 85.00  ? 169  HIS   D CA   1 
ATOM   21827 C  C    . HIS   D  4  169 ? 16.385  -60.136 -81.676  1.00 87.02  ? 169  HIS   D C    1 
ATOM   21828 O  O    . HIS   D  4  169 ? 16.194  -61.303 -82.033  1.00 89.04  ? 169  HIS   D O    1 
ATOM   21829 C  CB   . HIS   D  4  169 ? 14.712  -59.230 -83.325  1.00 85.14  ? 169  HIS   D CB   1 
ATOM   21830 C  CG   . HIS   D  4  169 ? 14.172  -58.031 -84.042  1.00 81.98  ? 169  HIS   D CG   1 
ATOM   21831 N  ND1  . HIS   D  4  169 ? 13.834  -56.864 -83.391  1.00 81.20  ? 169  HIS   D ND1  1 
ATOM   21832 C  CD2  . HIS   D  4  169 ? 13.900  -57.824 -85.352  1.00 82.42  ? 169  HIS   D CD2  1 
ATOM   21833 C  CE1  . HIS   D  4  169 ? 13.383  -55.987 -84.271  1.00 81.78  ? 169  HIS   D CE1  1 
ATOM   21834 N  NE2  . HIS   D  4  169 ? 13.413  -56.544 -85.468  1.00 82.81  ? 169  HIS   D NE2  1 
ATOM   21835 H  H    . HIS   D  4  169 ? 17.428  -59.548 -83.871  1.00 103.10 ? 169  HIS   D H    1 
ATOM   21836 H  HA   . HIS   D  4  169 ? 15.938  -58.169 -82.073  1.00 102.03 ? 169  HIS   D HA   1 
ATOM   21837 H  HB2  . HIS   D  4  169 ? 14.847  -59.931 -83.982  1.00 102.20 ? 169  HIS   D HB2  1 
ATOM   21838 H  HB3  . HIS   D  4  169 ? 14.049  -59.508 -82.674  1.00 102.20 ? 169  HIS   D HB3  1 
ATOM   21839 H  HD2  . HIS   D  4  169 ? 14.020  -58.433 -86.044  1.00 98.94  ? 169  HIS   D HD2  1 
ATOM   21840 H  HE1  . HIS   D  4  169 ? 13.094  -55.124 -84.079  1.00 98.18  ? 169  HIS   D HE1  1 
ATOM   21841 H  HE2  . HIS   D  4  169 ? 13.167  -56.167 -86.201  1.00 99.41  ? 169  HIS   D HE2  1 
ATOM   21842 N  N    . THR   D  4  170 ? 16.907  -59.813 -80.496  1.00 87.80  ? 170  THR   D N    1 
ATOM   21843 C  CA   . THR   D  4  170 ? 17.159  -60.808 -79.462  1.00 82.52  ? 170  THR   D CA   1 
ATOM   21844 C  C    . THR   D  4  170 ? 15.939  -60.872 -78.550  1.00 77.55  ? 170  THR   D C    1 
ATOM   21845 O  O    . THR   D  4  170 ? 15.518  -59.851 -77.995  1.00 75.46  ? 170  THR   D O    1 
ATOM   21846 C  CB   . THR   D  4  170 ? 18.413  -60.470 -78.658  1.00 81.27  ? 170  THR   D CB   1 
ATOM   21847 O  OG1  . THR   D  4  170 ? 19.547  -60.418 -79.534  1.00 82.51  ? 170  THR   D OG1  1 
ATOM   21848 C  CG2  . THR   D  4  170 ? 18.658  -61.522 -77.579  1.00 82.11  ? 170  THR   D CG2  1 
ATOM   21849 H  H    . THR   D  4  170 ? 17.127  -59.013 -80.269  1.00 105.40 ? 170  THR   D H    1 
ATOM   21850 H  HA   . THR   D  4  170 ? 17.299  -61.675 -79.873  1.00 99.06  ? 170  THR   D HA   1 
ATOM   21851 H  HB   . THR   D  4  170 ? 18.298  -59.609 -78.227  1.00 97.56  ? 170  THR   D HB   1 
ATOM   21852 H  HG1  . THR   D  4  170 ? 20.241  -60.240 -79.096  1.00 99.05  ? 170  THR   D HG1  1 
ATOM   21853 H  HG21 . THR   D  4  170 ? 19.468  -61.311 -77.088  1.00 98.57  ? 170  THR   D HG21 1 
ATOM   21854 H  HG22 . THR   D  4  170 ? 17.911  -61.543 -76.961  1.00 98.57  ? 170  THR   D HG22 1 
ATOM   21855 H  HG23 . THR   D  4  170 ? 18.756  -62.397 -77.985  1.00 98.57  ? 170  THR   D HG23 1 
ATOM   21856 N  N    . PHE   D  4  171 ? 15.383  -62.061 -78.397  1.00 75.85  ? 171  PHE   D N    1 
ATOM   21857 C  CA   . PHE   D  4  171 ? 14.157  -62.253 -77.640  1.00 76.78  ? 171  PHE   D CA   1 
ATOM   21858 C  C    . PHE   D  4  171 ? 14.470  -62.599 -76.191  1.00 79.26  ? 171  PHE   D C    1 
ATOM   21859 O  O    . PHE   D  4  171 ? 15.559  -63.087 -75.876  1.00 84.44  ? 171  PHE   D O    1 
ATOM   21860 C  CB   . PHE   D  4  171 ? 13.325  -63.362 -78.280  1.00 79.01  ? 171  PHE   D CB   1 
ATOM   21861 C  CG   . PHE   D  4  171 ? 12.949  -63.085 -79.709  1.00 78.29  ? 171  PHE   D CG   1 
ATOM   21862 C  CD1  . PHE   D  4  171 ? 13.849  -63.316 -80.738  1.00 78.70  ? 171  PHE   D CD1  1 
ATOM   21863 C  CD2  . PHE   D  4  171 ? 11.697  -62.587 -80.023  1.00 76.06  ? 171  PHE   D CD2  1 
ATOM   21864 C  CE1  . PHE   D  4  171 ? 13.506  -63.053 -82.053  1.00 78.10  ? 171  PHE   D CE1  1 
ATOM   21865 C  CE2  . PHE   D  4  171 ? 11.347  -62.324 -81.335  1.00 74.90  ? 171  PHE   D CE2  1 
ATOM   21866 C  CZ   . PHE   D  4  171 ? 12.252  -62.557 -82.350  1.00 77.76  ? 171  PHE   D CZ   1 
ATOM   21867 H  H    . PHE   D  4  171 ? 15.701  -62.788 -78.729  1.00 91.06  ? 171  PHE   D H    1 
ATOM   21868 H  HA   . PHE   D  4  171 ? 13.634  -61.436 -77.646  1.00 92.17  ? 171  PHE   D HA   1 
ATOM   21869 H  HB2  . PHE   D  4  171 ? 13.836  -64.186 -78.262  1.00 94.85  ? 171  PHE   D HB2  1 
ATOM   21870 H  HB3  . PHE   D  4  171 ? 12.505  -63.469 -77.773  1.00 94.85  ? 171  PHE   D HB3  1 
ATOM   21871 H  HD1  . PHE   D  4  171 ? 14.694  -63.652 -80.542  1.00 94.48  ? 171  PHE   D HD1  1 
ATOM   21872 H  HD2  . PHE   D  4  171 ? 11.083  -62.426 -79.343  1.00 91.31  ? 171  PHE   D HD2  1 
ATOM   21873 H  HE1  . PHE   D  4  171 ? 14.119  -63.210 -82.734  1.00 93.75  ? 171  PHE   D HE1  1 
ATOM   21874 H  HE2  . PHE   D  4  171 ? 10.502  -61.990 -81.533  1.00 89.92  ? 171  PHE   D HE2  1 
ATOM   21875 H  HZ   . PHE   D  4  171 ? 12.018  -62.381 -83.233  1.00 93.34  ? 171  PHE   D HZ   1 
ATOM   21876 N  N    . PRO   D  4  172 ? 13.539  -62.341 -75.273  1.00 78.14  ? 172  PRO   D N    1 
ATOM   21877 C  CA   . PRO   D  4  172 ? 13.751  -62.759 -73.884  1.00 79.25  ? 172  PRO   D CA   1 
ATOM   21878 C  C    . PRO   D  4  172 ? 13.710  -64.272 -73.739  1.00 82.23  ? 172  PRO   D C    1 
ATOM   21879 O  O    . PRO   D  4  172 ? 13.074  -64.981 -74.523  1.00 85.78  ? 172  PRO   D O    1 
ATOM   21880 C  CB   . PRO   D  4  172 ? 12.596  -62.092 -73.124  1.00 79.41  ? 172  PRO   D CB   1 
ATOM   21881 C  CG   . PRO   D  4  172 ? 11.578  -61.758 -74.159  1.00 77.81  ? 172  PRO   D CG   1 
ATOM   21882 C  CD   . PRO   D  4  172 ? 12.337  -61.502 -75.422  1.00 75.82  ? 172  PRO   D CD   1 
ATOM   21883 H  HA   . PRO   D  4  172 ? 14.597  -62.422 -73.549  1.00 95.14  ? 172  PRO   D HA   1 
ATOM   21884 H  HB2  . PRO   D  4  172 ? 12.234  -62.710 -72.470  1.00 95.33  ? 172  PRO   D HB2  1 
ATOM   21885 H  HB3  . PRO   D  4  172 ? 12.915  -61.290 -72.681  1.00 95.33  ? 172  PRO   D HB3  1 
ATOM   21886 H  HG2  . PRO   D  4  172 ? 10.970  -62.506 -74.271  1.00 93.41  ? 172  PRO   D HG2  1 
ATOM   21887 H  HG3  . PRO   D  4  172 ? 11.086  -60.968 -73.889  1.00 93.41  ? 172  PRO   D HG3  1 
ATOM   21888 H  HD2  . PRO   D  4  172 ? 11.819  -61.773 -76.197  1.00 91.02  ? 172  PRO   D HD2  1 
ATOM   21889 H  HD3  . PRO   D  4  172 ? 12.577  -60.565 -75.496  1.00 91.02  ? 172  PRO   D HD3  1 
ATOM   21890 N  N    . ALA   D  4  173 ? 14.405  -64.760 -72.715  1.00 83.49  ? 173  ALA   D N    1 
ATOM   21891 C  CA   . ALA   D  4  173 ? 14.508  -66.192 -72.486  1.00 83.43  ? 173  ALA   D CA   1 
ATOM   21892 C  C    . ALA   D  4  173 ? 13.189  -66.754 -71.964  1.00 80.70  ? 173  ALA   D C    1 
ATOM   21893 O  O    . ALA   D  4  173 ? 12.318  -66.028 -71.478  1.00 77.95  ? 173  ALA   D O    1 
ATOM   21894 C  CB   . ALA   D  4  173 ? 15.631  -66.494 -71.493  1.00 84.98  ? 173  ALA   D CB   1 
ATOM   21895 H  H    . ALA   D  4  173 ? 14.827  -64.280 -72.139  1.00 100.23 ? 173  ALA   D H    1 
ATOM   21896 H  HA   . ALA   D  4  173 ? 14.715  -66.636 -73.323  1.00 100.16 ? 173  ALA   D HA   1 
ATOM   21897 H  HB1  . ALA   D  4  173 ? 15.688  -67.453 -71.364  1.00 102.01 ? 173  ALA   D HB1  1 
ATOM   21898 H  HB2  . ALA   D  4  173 ? 16.468  -66.158 -71.851  1.00 102.01 ? 173  ALA   D HB2  1 
ATOM   21899 H  HB3  . ALA   D  4  173 ? 15.433  -66.057 -70.650  1.00 102.01 ? 173  ALA   D HB3  1 
ATOM   21900 N  N    . VAL   D  4  174 ? 13.052  -68.075 -72.072  1.00 84.55  ? 174  VAL   D N    1 
ATOM   21901 C  CA   . VAL   D  4  174 ? 11.873  -68.785 -71.596  1.00 87.55  ? 174  VAL   D CA   1 
ATOM   21902 C  C    . VAL   D  4  174 ? 12.326  -70.029 -70.846  1.00 93.08  ? 174  VAL   D C    1 
ATOM   21903 O  O    . VAL   D  4  174 ? 13.366  -70.619 -71.154  1.00 94.50  ? 174  VAL   D O    1 
ATOM   21904 C  CB   . VAL   D  4  174 ? 10.921  -69.175 -72.750  1.00 89.51  ? 174  VAL   D CB   1 
ATOM   21905 C  CG1  . VAL   D  4  174 ? 9.559   -69.577 -72.202  1.00 91.87  ? 174  VAL   D CG1  1 
ATOM   21906 C  CG2  . VAL   D  4  174 ? 10.790  -68.036 -73.750  1.00 86.08  ? 174  VAL   D CG2  1 
ATOM   21907 H  H    . VAL   D  4  174 ? 13.643  -68.590 -72.425  1.00 101.50 ? 174  VAL   D H    1 
ATOM   21908 H  HA   . VAL   D  4  174 ? 11.386  -68.211 -70.984  1.00 105.09 ? 174  VAL   D HA   1 
ATOM   21909 H  HB   . VAL   D  4  174 ? 11.294  -69.938 -73.219  1.00 107.45 ? 174  VAL   D HB   1 
ATOM   21910 H  HG11 . VAL   D  4  174 ? 8.975   -69.805 -72.943  1.00 110.28 ? 174  VAL   D HG11 1 
ATOM   21911 H  HG12 . VAL   D  4  174 ? 9.667   -70.343 -71.618  1.00 110.28 ? 174  VAL   D HG12 1 
ATOM   21912 H  HG13 . VAL   D  4  174 ? 9.186   -68.832 -71.705  1.00 110.28 ? 174  VAL   D HG13 1 
ATOM   21913 H  HG21 . VAL   D  4  174 ? 10.146  -68.287 -74.431  1.00 103.34 ? 174  VAL   D HG21 1 
ATOM   21914 H  HG22 . VAL   D  4  174 ? 10.487  -67.241 -73.285  1.00 103.34 ? 174  VAL   D HG22 1 
ATOM   21915 H  HG23 . VAL   D  4  174 ? 11.655  -67.872 -74.157  1.00 103.34 ? 174  VAL   D HG23 1 
ATOM   21916 N  N    . LEU   D  4  175 ? 11.537  -70.424 -69.851  1.00 97.30  ? 175  LEU   D N    1 
ATOM   21917 C  CA   . LEU   D  4  175 ? 11.795  -71.665 -69.135  1.00 103.69 ? 175  LEU   D CA   1 
ATOM   21918 C  C    . LEU   D  4  175 ? 11.374  -72.852 -69.991  1.00 111.51 ? 175  LEU   D C    1 
ATOM   21919 O  O    . LEU   D  4  175 ? 10.353  -72.810 -70.683  1.00 110.48 ? 175  LEU   D O    1 
ATOM   21920 C  CB   . LEU   D  4  175 ? 11.056  -71.686 -67.799  1.00 102.55 ? 175  LEU   D CB   1 
ATOM   21921 C  CG   . LEU   D  4  175 ? 11.694  -70.877 -66.665  1.00 102.96 ? 175  LEU   D CG   1 
ATOM   21922 C  CD1  . LEU   D  4  175 ? 10.804  -70.896 -65.432  1.00 105.54 ? 175  LEU   D CD1  1 
ATOM   21923 C  CD2  . LEU   D  4  175 ? 13.084  -71.405 -66.325  1.00 105.77 ? 175  LEU   D CD2  1 
ATOM   21924 H  H    . LEU   D  4  175 ? 10.848  -69.992 -69.573  1.00 116.80 ? 175  LEU   D H    1 
ATOM   21925 H  HA   . LEU   D  4  175 ? 12.743  -71.740 -68.945  1.00 124.46 ? 175  LEU   D HA   1 
ATOM   21926 H  HB2  . LEU   D  4  175 ? 10.165  -71.328 -67.940  1.00 123.10 ? 175  LEU   D HB2  1 
ATOM   21927 H  HB3  . LEU   D  4  175 ? 11.001  -72.606 -67.498  1.00 123.10 ? 175  LEU   D HB3  1 
ATOM   21928 H  HG   . LEU   D  4  175 ? 11.792  -69.958 -66.960  1.00 123.59 ? 175  LEU   D HG   1 
ATOM   21929 H  HD11 . LEU   D  4  175 ? 11.231  -70.384 -64.727  1.00 126.68 ? 175  LEU   D HD11 1 
ATOM   21930 H  HD12 . LEU   D  4  175 ? 9.947   -70.501 -65.655  1.00 126.68 ? 175  LEU   D HD12 1 
ATOM   21931 H  HD13 . LEU   D  4  175 ? 10.681  -71.814 -65.145  1.00 126.68 ? 175  LEU   D HD13 1 
ATOM   21932 H  HD21 . LEU   D  4  175 ? 13.439  -70.900 -65.577  1.00 126.96 ? 175  LEU   D HD21 1 
ATOM   21933 H  HD22 . LEU   D  4  175 ? 13.016  -72.343 -66.088  1.00 126.96 ? 175  LEU   D HD22 1 
ATOM   21934 H  HD23 . LEU   D  4  175 ? 13.660  -71.300 -67.098  1.00 126.96 ? 175  LEU   D HD23 1 
ATOM   21935 N  N    . GLN   D  4  176 ? 12.171  -73.917 -69.934  1.00 120.26 ? 176  GLN   D N    1 
ATOM   21936 C  CA   . GLN   D  4  176 ? 11.994  -75.060 -70.827  1.00 125.95 ? 176  GLN   D CA   1 
ATOM   21937 C  C    . GLN   D  4  176 ? 12.575  -76.280 -70.118  1.00 129.46 ? 176  GLN   D C    1 
ATOM   21938 O  O    . GLN   D  4  176 ? 13.788  -76.504 -70.158  1.00 130.60 ? 176  GLN   D O    1 
ATOM   21939 C  CB   . GLN   D  4  176 ? 12.674  -74.802 -72.164  1.00 127.62 ? 176  GLN   D CB   1 
ATOM   21940 C  CG   . GLN   D  4  176 ? 12.506  -75.898 -73.195  1.00 130.19 ? 176  GLN   D CG   1 
ATOM   21941 C  CD   . GLN   D  4  176 ? 13.255  -75.586 -74.473  1.00 128.73 ? 176  GLN   D CD   1 
ATOM   21942 O  OE1  . GLN   D  4  176 ? 14.479  -75.469 -74.471  1.00 127.19 ? 176  GLN   D OE1  1 
ATOM   21943 N  NE2  . GLN   D  4  176 ? 12.521  -75.429 -75.570  1.00 128.71 ? 176  GLN   D NE2  1 
ATOM   21944 H  H    . GLN   D  4  176 ? 12.827  -74.003 -69.384  1.00 144.35 ? 176  GLN   D H    1 
ATOM   21945 H  HA   . GLN   D  4  176 ? 11.050  -75.219 -70.985  1.00 151.18 ? 176  GLN   D HA   1 
ATOM   21946 H  HB2  . GLN   D  4  176 ? 12.306  -73.989 -72.543  1.00 153.18 ? 176  GLN   D HB2  1 
ATOM   21947 H  HB3  . GLN   D  4  176 ? 13.625  -74.695 -72.007  1.00 153.18 ? 176  GLN   D HB3  1 
ATOM   21948 H  HG2  . GLN   D  4  176 ? 12.850  -76.731 -72.836  1.00 156.26 ? 176  GLN   D HG2  1 
ATOM   21949 H  HG3  . GLN   D  4  176 ? 11.564  -75.994 -73.410  1.00 156.26 ? 176  GLN   D HG3  1 
ATOM   21950 H  HE21 . GLN   D  4  176 ? 11.666  -75.507 -75.530  1.00 154.49 ? 176  GLN   D HE21 1 
ATOM   21951 H  HE22 . GLN   D  4  176 ? 12.902  -75.251 -76.320  1.00 154.49 ? 176  GLN   D HE22 1 
ATOM   21952 N  N    . SER   D  4  177 ? 11.705  -77.056 -69.472  1.00 130.93 ? 177  SER   D N    1 
ATOM   21953 C  CA   . SER   D  4  177 ? 12.132  -78.202 -68.670  1.00 137.97 ? 177  SER   D CA   1 
ATOM   21954 C  C    . SER   D  4  177 ? 13.088  -77.762 -67.563  1.00 132.36 ? 177  SER   D C    1 
ATOM   21955 O  O    . SER   D  4  177 ? 14.060  -78.450 -67.247  1.00 135.70 ? 177  SER   D O    1 
ATOM   21956 C  CB   . SER   D  4  177 ? 12.775  -79.281 -69.545  1.00 150.91 ? 177  SER   D CB   1 
ATOM   21957 O  OG   . SER   D  4  177 ? 11.856  -79.776 -70.502  1.00 156.04 ? 177  SER   D OG   1 
ATOM   21958 H  H    . SER   D  4  177 ? 10.853  -76.939 -69.483  1.00 157.15 ? 177  SER   D H    1 
ATOM   21959 H  HA   . SER   D  4  177 ? 11.351  -78.591 -68.248  1.00 165.60 ? 177  SER   D HA   1 
ATOM   21960 H  HB2  . SER   D  4  177 ? 13.536  -78.898 -70.008  1.00 181.12 ? 177  SER   D HB2  1 
ATOM   21961 H  HB3  . SER   D  4  177 ? 13.066  -80.013 -68.979  1.00 181.12 ? 177  SER   D HB3  1 
ATOM   21962 H  HG   . SER   D  4  177 ? 12.243  -80.309 -71.023  1.00 187.29 ? 177  SER   D HG   1 
ATOM   21963 N  N    . SER   D  4  178 ? 12.810  -76.595 -66.979  1.00 124.51 ? 178  SER   D N    1 
ATOM   21964 C  CA   . SER   D  4  178 ? 13.576  -76.021 -65.876  1.00 125.06 ? 178  SER   D CA   1 
ATOM   21965 C  C    . SER   D  4  178 ? 14.932  -75.477 -66.313  1.00 125.30 ? 178  SER   D C    1 
ATOM   21966 O  O    . SER   D  4  178 ? 15.854  -75.382 -65.497  1.00 125.94 ? 178  SER   D O    1 
ATOM   21967 C  CB   . SER   D  4  178 ? 13.767  -77.038 -64.742  1.00 131.14 ? 178  SER   D CB   1 
ATOM   21968 O  OG   . SER   D  4  178 ? 12.518  -77.477 -64.238  1.00 131.95 ? 178  SER   D OG   1 
ATOM   21969 H  H    . SER   D  4  178 ? 12.151  -76.097 -67.217  1.00 149.45 ? 178  SER   D H    1 
ATOM   21970 H  HA   . SER   D  4  178 ? 13.069  -75.272 -65.527  1.00 150.11 ? 178  SER   D HA   1 
ATOM   21971 H  HB2  . SER   D  4  178 ? 14.256  -77.803 -65.084  1.00 157.40 ? 178  SER   D HB2  1 
ATOM   21972 H  HB3  . SER   D  4  178 ? 14.267  -76.618 -64.024  1.00 157.40 ? 178  SER   D HB3  1 
ATOM   21973 H  HG   . SER   D  4  178 ? 12.637  -78.038 -63.624  1.00 158.37 ? 178  SER   D HG   1 
ATOM   21974 N  N    . LEU   D  4  179 ? 15.079  -75.113 -67.586  1.00 91.88  ? 179  LEU   D N    1 
ATOM   21975 C  CA   . LEU   D  4  179 ? 16.279  -74.447 -68.070  1.00 86.33  ? 179  LEU   D CA   1 
ATOM   21976 C  C    . LEU   D  4  179 ? 15.875  -73.343 -69.037  1.00 86.83  ? 179  LEU   D C    1 
ATOM   21977 O  O    . LEU   D  4  179 ? 14.803  -73.383 -69.646  1.00 89.08  ? 179  LEU   D O    1 
ATOM   21978 C  CB   . LEU   D  4  179 ? 17.244  -75.425 -68.756  1.00 79.89  ? 179  LEU   D CB   1 
ATOM   21979 C  CG   . LEU   D  4  179 ? 17.984  -76.411 -67.849  1.00 76.76  ? 179  LEU   D CG   1 
ATOM   21980 C  CD1  . LEU   D  4  179 ? 18.768  -77.403 -68.689  1.00 74.75  ? 179  LEU   D CD1  1 
ATOM   21981 C  CD2  . LEU   D  4  179 ? 18.914  -75.687 -66.888  1.00 74.73  ? 179  LEU   D CD2  1 
ATOM   21982 H  H    . LEU   D  4  179 ? 14.486  -75.244 -68.195  1.00 110.30 ? 179  LEU   D H    1 
ATOM   21983 H  HA   . LEU   D  4  179 ? 16.747  -74.045 -67.321  1.00 103.63 ? 179  LEU   D HA   1 
ATOM   21984 H  HB2  . LEU   D  4  179 ? 16.735  -75.951 -69.392  1.00 95.91  ? 179  LEU   D HB2  1 
ATOM   21985 H  HB3  . LEU   D  4  179 ? 17.918  -74.904 -69.220  1.00 95.91  ? 179  LEU   D HB3  1 
ATOM   21986 H  HG   . LEU   D  4  179 ? 17.332  -76.894 -67.318  1.00 92.15  ? 179  LEU   D HG   1 
ATOM   21987 H  HD11 . LEU   D  4  179 ? 19.236  -78.015 -68.100  1.00 89.74  ? 179  LEU   D HD11 1 
ATOM   21988 H  HD12 . LEU   D  4  179 ? 18.151  -77.894 -69.255  1.00 89.74  ? 179  LEU   D HD12 1 
ATOM   21989 H  HD13 . LEU   D  4  179 ? 19.405  -76.919 -69.238  1.00 89.74  ? 179  LEU   D HD13 1 
ATOM   21990 H  HD21 . LEU   D  4  179 ? 19.384  -76.343 -66.349  1.00 89.71  ? 179  LEU   D HD21 1 
ATOM   21991 H  HD22 . LEU   D  4  179 ? 19.549  -75.161 -67.398  1.00 89.71  ? 179  LEU   D HD22 1 
ATOM   21992 H  HD23 . LEU   D  4  179 ? 18.387  -75.106 -66.317  1.00 89.71  ? 179  LEU   D HD23 1 
ATOM   21993 N  N    . TYR   D  4  180 ? 16.753  -72.353 -69.174  1.00 87.13  ? 180  TYR   D N    1 
ATOM   21994 C  CA   . TYR   D  4  180 ? 16.474  -71.183 -69.994  1.00 90.26  ? 180  TYR   D CA   1 
ATOM   21995 C  C    . TYR   D  4  180 ? 16.824  -71.448 -71.452  1.00 88.41  ? 180  TYR   D C    1 
ATOM   21996 O  O    . TYR   D  4  180 ? 17.802  -72.137 -71.757  1.00 87.39  ? 180  TYR   D O    1 
ATOM   21997 C  CB   . TYR   D  4  180 ? 17.256  -69.970 -69.486  1.00 91.15  ? 180  TYR   D CB   1 
ATOM   21998 C  CG   . TYR   D  4  180 ? 16.766  -69.422 -68.164  1.00 95.44  ? 180  TYR   D CG   1 
ATOM   21999 C  CD1  . TYR   D  4  180 ? 15.479  -68.914 -68.033  1.00 97.84  ? 180  TYR   D CD1  1 
ATOM   22000 C  CD2  . TYR   D  4  180 ? 17.594  -69.401 -67.049  1.00 95.26  ? 180  TYR   D CD2  1 
ATOM   22001 C  CE1  . TYR   D  4  180 ? 15.028  -68.408 -66.827  1.00 99.79  ? 180  TYR   D CE1  1 
ATOM   22002 C  CE2  . TYR   D  4  180 ? 17.152  -68.895 -65.839  1.00 97.43  ? 180  TYR   D CE2  1 
ATOM   22003 C  CZ   . TYR   D  4  180 ? 15.870  -68.397 -65.735  1.00 99.66  ? 180  TYR   D CZ   1 
ATOM   22004 O  OH   . TYR   D  4  180 ? 15.429  -67.896 -64.532  1.00 101.54 ? 180  TYR   D OH   1 
ATOM   22005 H  H    . TYR   D  4  180 ? 17.526  -72.338 -68.797  1.00 104.59 ? 180  TYR   D H    1 
ATOM   22006 H  HA   . TYR   D  4  180 ? 15.526  -70.983 -69.942  1.00 108.35 ? 180  TYR   D HA   1 
ATOM   22007 H  HB2  . TYR   D  4  180 ? 18.185  -70.225 -69.373  1.00 109.41 ? 180  TYR   D HB2  1 
ATOM   22008 H  HB3  . TYR   D  4  180 ? 17.185  -69.259 -70.143  1.00 109.41 ? 180  TYR   D HB3  1 
ATOM   22009 H  HD1  . TYR   D  4  180 ? 14.912  -68.913 -68.770  1.00 117.45 ? 180  TYR   D HD1  1 
ATOM   22010 H  HD2  . TYR   D  4  180 ? 18.460  -69.732 -67.116  1.00 114.35 ? 180  TYR   D HD2  1 
ATOM   22011 H  HE1  . TYR   D  4  180 ? 14.162  -68.078 -66.754  1.00 119.79 ? 180  TYR   D HE1  1 
ATOM   22012 H  HE2  . TYR   D  4  180 ? 17.716  -68.890 -65.100  1.00 116.95 ? 180  TYR   D HE2  1 
ATOM   22013 H  HH   . TYR   D  4  180 ? 14.590  -67.902 -64.508  1.00 121.88 ? 180  TYR   D HH   1 
ATOM   22014 N  N    . THR   D  4  181 ? 16.017  -70.886 -72.350  1.00 83.70  ? 181  THR   D N    1 
ATOM   22015 C  CA   . THR   D  4  181 ? 16.218  -71.006 -73.788  1.00 80.20  ? 181  THR   D CA   1 
ATOM   22016 C  C    . THR   D  4  181 ? 16.051  -69.630 -74.414  1.00 78.03  ? 181  THR   D C    1 
ATOM   22017 O  O    . THR   D  4  181 ? 15.072  -68.932 -74.131  1.00 80.49  ? 181  THR   D O    1 
ATOM   22018 C  CB   . THR   D  4  181 ? 15.226  -71.994 -74.411  1.00 83.28  ? 181  THR   D CB   1 
ATOM   22019 O  OG1  . THR   D  4  181 ? 15.248  -73.228 -73.681  1.00 85.90  ? 181  THR   D OG1  1 
ATOM   22020 C  CG2  . THR   D  4  181 ? 15.578  -72.262 -75.870  1.00 82.04  ? 181  THR   D CG2  1 
ATOM   22021 H  H    . THR   D  4  181 ? 15.327  -70.418 -72.142  1.00 100.48 ? 181  THR   D H    1 
ATOM   22022 H  HA   . THR   D  4  181 ? 17.115  -71.328 -73.968  1.00 96.28  ? 181  THR   D HA   1 
ATOM   22023 H  HB   . THR   D  4  181 ? 14.333  -71.617 -74.378  1.00 99.97  ? 181  THR   D HB   1 
ATOM   22024 H  HG1  . THR   D  4  181 ? 15.568  -73.839 -74.159  1.00 103.11 ? 181  THR   D HG1  1 
ATOM   22025 H  HG21 . THR   D  4  181 ? 15.296  -73.156 -76.121  1.00 98.49  ? 181  THR   D HG21 1 
ATOM   22026 H  HG22 . THR   D  4  181 ? 15.133  -71.619 -76.443  1.00 98.49  ? 181  THR   D HG22 1 
ATOM   22027 H  HG23 . THR   D  4  181 ? 16.537  -72.187 -75.999  1.00 98.49  ? 181  THR   D HG23 1 
ATOM   22028 N  N    . LEU   D  4  182 ? 17.002  -69.246 -75.260  1.00 76.06  ? 182  LEU   D N    1 
ATOM   22029 C  CA   . LEU   D  4  182 ? 17.018  -67.928 -75.875  1.00 73.14  ? 182  LEU   D CA   1 
ATOM   22030 C  C    . LEU   D  4  182 ? 17.308  -68.065 -77.362  1.00 70.96  ? 182  LEU   D C    1 
ATOM   22031 O  O    . LEU   D  4  182 ? 17.994  -68.995 -77.795  1.00 71.15  ? 182  LEU   D O    1 
ATOM   22032 C  CB   . LEU   D  4  182 ? 18.065  -67.021 -75.206  1.00 73.21  ? 182  LEU   D CB   1 
ATOM   22033 C  CG   . LEU   D  4  182 ? 18.092  -65.549 -75.619  1.00 75.58  ? 182  LEU   D CG   1 
ATOM   22034 C  CD1  . LEU   D  4  182 ? 18.507  -64.685 -74.438  1.00 74.59  ? 182  LEU   D CD1  1 
ATOM   22035 C  CD2  . LEU   D  4  182 ? 19.034  -65.327 -76.792  1.00 79.58  ? 182  LEU   D CD2  1 
ATOM   22036 H  H    . LEU   D  4  182 ? 17.662  -69.744 -75.497  1.00 91.31  ? 182  LEU   D H    1 
ATOM   22037 H  HA   . LEU   D  4  182 ? 16.150  -67.505 -75.782  1.00 87.80  ? 182  LEU   D HA   1 
ATOM   22038 H  HB2  . LEU   D  4  182 ? 17.907  -67.041 -74.249  1.00 87.88  ? 182  LEU   D HB2  1 
ATOM   22039 H  HB3  . LEU   D  4  182 ? 18.942  -67.385 -75.404  1.00 87.88  ? 182  LEU   D HB3  1 
ATOM   22040 H  HG   . LEU   D  4  182 ? 17.202  -65.286 -75.903  1.00 90.73  ? 182  LEU   D HG   1 
ATOM   22041 H  HD11 . LEU   D  4  182 ? 18.905  -63.865 -74.771  1.00 89.55  ? 182  LEU   D HD11 1 
ATOM   22042 H  HD12 . LEU   D  4  182 ? 17.723  -64.479 -73.906  1.00 89.55  ? 182  LEU   D HD12 1 
ATOM   22043 H  HD13 . LEU   D  4  182 ? 19.153  -65.172 -73.902  1.00 89.55  ? 182  LEU   D HD13 1 
ATOM   22044 H  HD21 . LEU   D  4  182 ? 18.720  -64.571 -77.311  1.00 95.54  ? 182  LEU   D HD21 1 
ATOM   22045 H  HD22 . LEU   D  4  182 ? 19.925  -65.148 -76.451  1.00 95.54  ? 182  LEU   D HD22 1 
ATOM   22046 H  HD23 . LEU   D  4  182 ? 19.046  -66.125 -77.343  1.00 95.54  ? 182  LEU   D HD23 1 
ATOM   22047 N  N    . SER   D  4  183 ? 16.775  -67.126 -78.140  1.00 68.43  ? 183  SER   D N    1 
ATOM   22048 C  CA   . SER   D  4  183 ? 16.967  -67.106 -79.581  1.00 72.74  ? 183  SER   D CA   1 
ATOM   22049 C  C    . SER   D  4  183 ? 17.175  -65.668 -80.034  1.00 73.70  ? 183  SER   D C    1 
ATOM   22050 O  O    . SER   D  4  183 ? 16.769  -64.718 -79.359  1.00 58.63  ? 183  SER   D O    1 
ATOM   22051 C  CB   . SER   D  4  183 ? 15.774  -67.731 -80.317  1.00 74.81  ? 183  SER   D CB   1 
ATOM   22052 O  OG   . SER   D  4  183 ? 14.556  -67.127 -79.915  1.00 73.78  ? 183  SER   D OG   1 
ATOM   22053 H  H    . SER   D  4  183 ? 16.290  -66.479 -77.848  1.00 82.16  ? 183  SER   D H    1 
ATOM   22054 H  HA   . SER   D  4  183 ? 17.762  -67.612 -79.812  1.00 87.32  ? 183  SER   D HA   1 
ATOM   22055 H  HB2  . SER   D  4  183 ? 15.889  -67.603 -81.271  1.00 89.81  ? 183  SER   D HB2  1 
ATOM   22056 H  HB3  . SER   D  4  183 ? 15.738  -68.678 -80.111  1.00 89.81  ? 183  SER   D HB3  1 
ATOM   22057 H  HG   . SER   D  4  183 ? 13.950  -67.309 -80.467  1.00 88.58  ? 183  SER   D HG   1 
ATOM   22058 N  N    . SER   D  4  184 ? 17.819  -65.515 -81.189  1.00 73.90  ? 184  SER   D N    1 
ATOM   22059 C  CA   . SER   D  4  184 ? 18.101  -64.194 -81.731  1.00 70.58  ? 184  SER   D CA   1 
ATOM   22060 C  C    . SER   D  4  184 ? 18.172  -64.273 -83.247  1.00 72.24  ? 184  SER   D C    1 
ATOM   22061 O  O    . SER   D  4  184 ? 18.687  -65.248 -83.802  1.00 72.39  ? 184  SER   D O    1 
ATOM   22062 C  CB   . SER   D  4  184 ? 19.413  -63.630 -81.172  1.00 66.23  ? 184  SER   D CB   1 
ATOM   22063 O  OG   . SER   D  4  184 ? 19.643  -62.314 -81.644  1.00 64.97  ? 184  SER   D OG   1 
ATOM   22064 H  H    . SER   D  4  184 ? 18.103  -66.164 -81.677  1.00 88.72  ? 184  SER   D H    1 
ATOM   22065 H  HA   . SER   D  4  184 ? 17.379  -63.590 -81.494  1.00 84.73  ? 184  SER   D HA   1 
ATOM   22066 H  HB2  . SER   D  4  184 ? 19.361  -63.613 -80.204  1.00 79.52  ? 184  SER   D HB2  1 
ATOM   22067 H  HB3  . SER   D  4  184 ? 20.146  -64.199 -81.456  1.00 79.52  ? 184  SER   D HB3  1 
ATOM   22068 H  HG   . SER   D  4  184 ? 19.659  -61.777 -80.998  1.00 78.00  ? 184  SER   D HG   1 
ATOM   22069 N  N    . SER   D  4  185 ? 17.654  -63.240 -83.907  1.00 74.60  ? 185  SER   D N    1 
ATOM   22070 C  CA   . SER   D  4  185 ? 17.668  -63.137 -85.358  1.00 80.35  ? 185  SER   D CA   1 
ATOM   22071 C  C    . SER   D  4  185 ? 18.440  -61.894 -85.774  1.00 79.51  ? 185  SER   D C    1 
ATOM   22072 O  O    . SER   D  4  185 ? 18.347  -60.846 -85.127  1.00 78.61  ? 185  SER   D O    1 
ATOM   22073 C  CB   . SER   D  4  185 ? 16.249  -63.068 -85.929  1.00 87.65  ? 185  SER   D CB   1 
ATOM   22074 O  OG   . SER   D  4  185 ? 15.842  -61.720 -86.094  1.00 93.62  ? 185  SER   D OG   1 
ATOM   22075 H  H    . SER   D  4  185 ? 17.279  -62.569 -83.523  1.00 89.56  ? 185  SER   D H    1 
ATOM   22076 H  HA   . SER   D  4  185 ? 18.109  -63.918 -85.728  1.00 96.46  ? 185  SER   D HA   1 
ATOM   22077 H  HB2  . SER   D  4  185 ? 16.232  -63.511 -86.792  1.00 105.22 ? 185  SER   D HB2  1 
ATOM   22078 H  HB3  . SER   D  4  185 ? 15.639  -63.510 -85.317  1.00 105.22 ? 185  SER   D HB3  1 
ATOM   22079 H  HG   . SER   D  4  185 ? 15.023  -61.644 -85.924  1.00 112.38 ? 185  SER   D HG   1 
ATOM   22080 N  N    . VAL   D  4  186 ? 19.204  -62.021 -86.855  1.00 76.91  ? 186  VAL   D N    1 
ATOM   22081 C  CA   . VAL   D  4  186 ? 19.894  -60.905 -87.487  1.00 77.65  ? 186  VAL   D CA   1 
ATOM   22082 C  C    . VAL   D  4  186 ? 19.465  -60.867 -88.946  1.00 78.26  ? 186  VAL   D C    1 
ATOM   22083 O  O    . VAL   D  4  186 ? 19.380  -61.912 -89.601  1.00 78.48  ? 186  VAL   D O    1 
ATOM   22084 C  CB   . VAL   D  4  186 ? 21.427  -61.036 -87.364  1.00 79.54  ? 186  VAL   D CB   1 
ATOM   22085 C  CG1  . VAL   D  4  186 ? 21.907  -62.332 -88.006  1.00 82.58  ? 186  VAL   D CG1  1 
ATOM   22086 C  CG2  . VAL   D  4  186 ? 22.124  -59.834 -87.990  1.00 82.33  ? 186  VAL   D CG2  1 
ATOM   22087 H  H    . VAL   D  4  186 ? 19.341  -62.771 -87.252  1.00 92.32  ? 186  VAL   D H    1 
ATOM   22088 H  HA   . VAL   D  4  186 ? 19.635  -60.073 -87.061  1.00 93.22  ? 186  VAL   D HA   1 
ATOM   22089 H  HB   . VAL   D  4  186 ? 21.662  -61.060 -86.424  1.00 95.49  ? 186  VAL   D HB   1 
ATOM   22090 H  HG11 . VAL   D  4  186 ? 22.867  -62.405 -87.888  1.00 99.13  ? 186  VAL   D HG11 1 
ATOM   22091 H  HG12 . VAL   D  4  186 ? 21.462  -63.080 -87.577  1.00 99.13  ? 186  VAL   D HG12 1 
ATOM   22092 H  HG13 . VAL   D  4  186 ? 21.689  -62.315 -88.951  1.00 99.13  ? 186  VAL   D HG13 1 
ATOM   22093 H  HG21 . VAL   D  4  186 ? 23.082  -59.930 -87.877  1.00 98.83  ? 186  VAL   D HG21 1 
ATOM   22094 H  HG22 . VAL   D  4  186 ? 21.904  -59.798 -88.934  1.00 98.83  ? 186  VAL   D HG22 1 
ATOM   22095 H  HG23 . VAL   D  4  186 ? 21.818  -59.027 -87.548  1.00 98.83  ? 186  VAL   D HG23 1 
ATOM   22096 N  N    . THR   D  4  187 ? 19.185  -59.669 -89.452  1.00 79.05  ? 187  THR   D N    1 
ATOM   22097 C  CA   . THR   D  4  187 ? 18.741  -59.485 -90.828  1.00 84.84  ? 187  THR   D CA   1 
ATOM   22098 C  C    . THR   D  4  187 ? 19.713  -58.555 -91.539  1.00 89.51  ? 187  THR   D C    1 
ATOM   22099 O  O    . THR   D  4  187 ? 19.928  -57.420 -91.098  1.00 90.39  ? 187  THR   D O    1 
ATOM   22100 C  CB   . THR   D  4  187 ? 17.317  -58.926 -90.882  1.00 86.14  ? 187  THR   D CB   1 
ATOM   22101 O  OG1  . THR   D  4  187 ? 16.426  -59.819 -90.201  1.00 85.56  ? 187  THR   D OG1  1 
ATOM   22102 C  CG2  . THR   D  4  187 ? 16.859  -58.765 -92.326  1.00 90.05  ? 187  THR   D CG2  1 
ATOM   22103 H  H    . THR   D  4  187 ? 19.245  -58.935 -89.007  1.00 94.89  ? 187  THR   D H    1 
ATOM   22104 H  HA   . THR   D  4  187 ? 18.748  -60.340 -91.286  1.00 101.85 ? 187  THR   D HA   1 
ATOM   22105 H  HB   . THR   D  4  187 ? 17.296  -58.055 -90.455  1.00 103.41 ? 187  THR   D HB   1 
ATOM   22106 H  HG1  . THR   D  4  187 ? 15.633  -59.557 -90.291  1.00 102.70 ? 187  THR   D HG1  1 
ATOM   22107 H  HG21 . THR   D  4  187 ? 15.945  -58.441 -92.350  1.00 108.09 ? 187  THR   D HG21 1 
ATOM   22108 H  HG22 . THR   D  4  187 ? 17.430  -58.131 -92.787  1.00 108.09 ? 187  THR   D HG22 1 
ATOM   22109 H  HG23 . THR   D  4  187 ? 16.902  -59.619 -92.785  1.00 108.09 ? 187  THR   D HG23 1 
ATOM   22110 N  N    . VAL   D  4  188 ? 20.292  -59.036 -92.639  1.00 93.80  ? 188  VAL   D N    1 
ATOM   22111 C  CA   . VAL   D  4  188 ? 21.266  -58.286 -93.417  1.00 100.09 ? 188  VAL   D CA   1 
ATOM   22112 C  C    . VAL   D  4  188 ? 20.847  -58.311 -94.881  1.00 103.78 ? 188  VAL   D C    1 
ATOM   22113 O  O    . VAL   D  4  188 ? 19.901  -58.996 -95.273  1.00 104.26 ? 188  VAL   D O    1 
ATOM   22114 C  CB   . VAL   D  4  188 ? 22.696  -58.845 -93.255  1.00 101.85 ? 188  VAL   D CB   1 
ATOM   22115 C  CG1  . VAL   D  4  188 ? 23.160  -58.706 -91.812  1.00 97.25  ? 188  VAL   D CG1  1 
ATOM   22116 C  CG2  . VAL   D  4  188 ? 22.755  -60.301 -93.704  1.00 104.21 ? 188  VAL   D CG2  1 
ATOM   22117 H  H    . VAL   D  4  188 ? 20.128  -59.817 -92.960  1.00 112.60 ? 188  VAL   D H    1 
ATOM   22118 H  HA   . VAL   D  4  188 ? 21.265  -57.363 -93.118  1.00 120.15 ? 188  VAL   D HA   1 
ATOM   22119 H  HB   . VAL   D  4  188 ? 23.300  -58.335 -93.816  1.00 122.25 ? 188  VAL   D HB   1 
ATOM   22120 H  HG11 . VAL   D  4  188 ? 24.061  -59.057 -91.734  1.00 116.73 ? 188  VAL   D HG11 1 
ATOM   22121 H  HG12 . VAL   D  4  188 ? 23.148  -57.768 -91.565  1.00 116.73 ? 188  VAL   D HG12 1 
ATOM   22122 H  HG13 . VAL   D  4  188 ? 22.560  -59.207 -91.237  1.00 116.73 ? 188  VAL   D HG13 1 
ATOM   22123 H  HG21 . VAL   D  4  188 ? 23.662  -60.628 -93.600  1.00 125.09 ? 188  VAL   D HG21 1 
ATOM   22124 H  HG22 . VAL   D  4  188 ? 22.149  -60.825 -93.157  1.00 125.09 ? 188  VAL   D HG22 1 
ATOM   22125 H  HG23 . VAL   D  4  188 ? 22.489  -60.355 -94.636  1.00 125.09 ? 188  VAL   D HG23 1 
ATOM   22126 N  N    . VAL   D  4  189 ? 21.578  -57.547 -95.695  1.00 105.30 ? 189  VAL   D N    1 
ATOM   22127 C  CA   . VAL   D  4  189 ? 21.305  -57.494 -97.124  1.00 114.41 ? 189  VAL   D CA   1 
ATOM   22128 C  C    . VAL   D  4  189 ? 21.621  -58.848 -97.746  1.00 121.80 ? 189  VAL   D C    1 
ATOM   22129 O  O    . VAL   D  4  189 ? 22.560  -59.541 -97.331  1.00 124.15 ? 189  VAL   D O    1 
ATOM   22130 C  CB   . VAL   D  4  189 ? 22.124  -56.373 -97.788  1.00 121.00 ? 189  VAL   D CB   1 
ATOM   22131 C  CG1  . VAL   D  4  189 ? 21.702  -56.187 -99.241  1.00 122.77 ? 189  VAL   D CG1  1 
ATOM   22132 C  CG2  . VAL   D  4  189 ? 21.976  -55.064 -97.016  1.00 124.79 ? 189  VAL   D CG2  1 
ATOM   22133 H  H    . VAL   D  4  189 ? 22.235  -57.053 -95.441  1.00 126.39 ? 189  VAL   D H    1 
ATOM   22134 H  HA   . VAL   D  4  189 ? 20.365  -57.301 -97.262  1.00 137.33 ? 189  VAL   D HA   1 
ATOM   22135 H  HB   . VAL   D  4  189 ? 23.060  -56.625 -97.774  1.00 145.24 ? 189  VAL   D HB   1 
ATOM   22136 H  HG11 . VAL   D  4  189 ? 22.230  -55.475 -99.634  1.00 147.36 ? 189  VAL   D HG11 1 
ATOM   22137 H  HG12 . VAL   D  4  189 ? 21.852  -57.016 -99.722  1.00 147.36 ? 189  VAL   D HG12 1 
ATOM   22138 H  HG13 . VAL   D  4  189 ? 20.760  -55.954 -99.269  1.00 147.36 ? 189  VAL   D HG13 1 
ATOM   22139 H  HG21 . VAL   D  4  189 ? 22.469  -54.368 -97.477  1.00 149.79 ? 189  VAL   D HG21 1 
ATOM   22140 H  HG22 . VAL   D  4  189 ? 21.036  -54.829 -96.970  1.00 149.79 ? 189  VAL   D HG22 1 
ATOM   22141 H  HG23 . VAL   D  4  189 ? 22.331  -55.184 -96.121  1.00 149.79 ? 189  VAL   D HG23 1 
ATOM   22142 N  N    . ALA   D  4  190 ? 20.830  -59.236 -98.751  1.00 127.87 ? 190  ALA   D N    1 
ATOM   22143 C  CA   . ALA   D  4  190 ? 21.041  -60.527 -99.396  1.00 133.72 ? 190  ALA   D CA   1 
ATOM   22144 C  C    . ALA   D  4  190 ? 22.445  -60.632 -99.979  1.00 134.80 ? 190  ALA   D C    1 
ATOM   22145 O  O    . ALA   D  4  190 ? 23.061  -61.704 -99.947  1.00 140.38 ? 190  ALA   D O    1 
ATOM   22146 C  CB   . ALA   D  4  190 ? 19.996  -60.746 -100.490 1.00 142.03 ? 190  ALA   D CB   1 
ATOM   22147 H  H    . ALA   D  4  190 ? 20.177  -58.777 -99.070  1.00 153.49 ? 190  ALA   D H    1 
ATOM   22148 H  HA   . ALA   D  4  190 ? 20.937  -61.226 -98.732  1.00 160.50 ? 190  ALA   D HA   1 
ATOM   22149 H  HB1  . ALA   D  4  190 ? 20.159  -61.602 -100.916 1.00 170.47 ? 190  ALA   D HB1  1 
ATOM   22150 H  HB2  . ALA   D  4  190 ? 19.113  -60.740 -100.088 1.00 170.47 ? 190  ALA   D HB2  1 
ATOM   22151 H  HB3  . ALA   D  4  190 ? 20.068  -60.033 -101.143 1.00 170.47 ? 190  ALA   D HB3  1 
ATOM   22152 N  N    . SER   D  4  191 ? 22.968  -59.529 -100.514 1.00 131.85 ? 191  SER   D N    1 
ATOM   22153 C  CA   . SER   D  4  191 ? 24.263  -59.538 -101.180 1.00 138.10 ? 191  SER   D CA   1 
ATOM   22154 C  C    . SER   D  4  191 ? 25.440  -59.570 -100.214 1.00 136.69 ? 191  SER   D C    1 
ATOM   22155 O  O    . SER   D  4  191 ? 26.577  -59.753 -100.662 1.00 142.71 ? 191  SER   D O    1 
ATOM   22156 C  CB   . SER   D  4  191 ? 24.388  -58.310 -102.086 1.00 142.75 ? 191  SER   D CB   1 
ATOM   22157 O  OG   . SER   D  4  191 ? 24.324  -57.113 -101.329 1.00 140.57 ? 191  SER   D OG   1 
ATOM   22158 H  H    . SER   D  4  191 ? 22.588  -58.757 -100.501 1.00 158.26 ? 191  SER   D H    1 
ATOM   22159 H  HA   . SER   D  4  191 ? 24.316  -60.334 -101.733 1.00 165.76 ? 191  SER   D HA   1 
ATOM   22160 H  HB2  . SER   D  4  191 ? 25.239  -58.345 -102.549 1.00 171.33 ? 191  SER   D HB2  1 
ATOM   22161 H  HB3  . SER   D  4  191 ? 23.661  -58.316 -102.728 1.00 171.33 ? 191  SER   D HB3  1 
ATOM   22162 H  HG   . SER   D  4  191 ? 24.372  -56.448 -101.839 1.00 168.72 ? 191  SER   D HG   1 
ATOM   22163 N  N    . THR   D  4  192 ? 25.206  -59.398 -98.914  1.00 130.39 ? 192  THR   D N    1 
ATOM   22164 C  CA   . THR   D  4  192 ? 26.278  -59.369 -97.929  1.00 130.59 ? 192  THR   D CA   1 
ATOM   22165 C  C    . THR   D  4  192 ? 26.388  -60.660 -97.129  1.00 125.42 ? 192  THR   D C    1 
ATOM   22166 O  O    . THR   D  4  192 ? 27.229  -60.745 -96.227  1.00 121.68 ? 192  THR   D O    1 
ATOM   22167 C  CB   . THR   D  4  192 ? 26.085  -58.186 -96.972  1.00 129.63 ? 192  THR   D CB   1 
ATOM   22168 O  OG1  . THR   D  4  192 ? 24.820  -58.299 -96.309  1.00 129.65 ? 192  THR   D OG1  1 
ATOM   22169 C  CG2  . THR   D  4  192 ? 26.149  -56.869 -97.736  1.00 131.39 ? 192  THR   D CG2  1 
ATOM   22170 H  H    . THR   D  4  192 ? 24.421  -59.295 -98.577  1.00 156.50 ? 192  THR   D H    1 
ATOM   22171 H  HA   . THR   D  4  192 ? 27.118  -59.240 -98.396  1.00 156.74 ? 192  THR   D HA   1 
ATOM   22172 H  HB   . THR   D  4  192 ? 26.792  -58.188 -96.308  1.00 155.59 ? 192  THR   D HB   1 
ATOM   22173 H  HG1  . THR   D  4  192 ? 24.343  -58.872 -96.695  1.00 155.61 ? 192  THR   D HG1  1 
ATOM   22174 H  HG21 . THR   D  4  192 ? 26.032  -56.125 -97.125  1.00 157.70 ? 192  THR   D HG21 1 
ATOM   22175 H  HG22 . THR   D  4  192 ? 27.009  -56.782 -98.177  1.00 157.70 ? 192  THR   D HG22 1 
ATOM   22176 H  HG23 . THR   D  4  192 ? 25.448  -56.840 -98.406  1.00 157.70 ? 192  THR   D HG23 1 
ATOM   22177 N  N    . TRP   D  4  193 ? 25.564  -61.663 -97.429  1.00 129.01 ? 193  TRP   D N    1 
ATOM   22178 C  CA   . TRP   D  4  193 ? 25.701  -62.986 -96.845  1.00 121.87 ? 193  TRP   D CA   1 
ATOM   22179 C  C    . TRP   D  4  193 ? 25.299  -63.972 -97.933  1.00 123.70 ? 193  TRP   D C    1 
ATOM   22180 O  O    . TRP   D  4  193 ? 24.286  -63.755 -98.612  1.00 126.27 ? 193  TRP   D O    1 
ATOM   22181 C  CB   . TRP   D  4  193 ? 24.825  -63.184 -95.599  1.00 114.45 ? 193  TRP   D CB   1 
ATOM   22182 C  CG   . TRP   D  4  193 ? 25.104  -64.474 -94.877  1.00 104.11 ? 193  TRP   D CG   1 
ATOM   22183 C  CD1  . TRP   D  4  193 ? 26.087  -64.704 -93.956  1.00 97.53  ? 193  TRP   D CD1  1 
ATOM   22184 C  CD2  . TRP   D  4  193 ? 24.397  -65.713 -95.025  1.00 99.82  ? 193  TRP   D CD2  1 
ATOM   22185 N  NE1  . TRP   D  4  193 ? 26.035  -66.008 -93.523  1.00 91.96  ? 193  TRP   D NE1  1 
ATOM   22186 C  CE2  . TRP   D  4  193 ? 25.007  -66.648 -94.164  1.00 94.27  ? 193  TRP   D CE2  1 
ATOM   22187 C  CE3  . TRP   D  4  193 ? 23.308  -66.121 -95.801  1.00 101.68 ? 193  TRP   D CE3  1 
ATOM   22188 C  CZ2  . TRP   D  4  193 ? 24.562  -67.963 -94.056  1.00 94.29  ? 193  TRP   D CZ2  1 
ATOM   22189 C  CZ3  . TRP   D  4  193 ? 22.869  -67.429 -95.693  1.00 101.45 ? 193  TRP   D CZ3  1 
ATOM   22190 C  CH2  . TRP   D  4  193 ? 23.495  -68.334 -94.827  1.00 98.30  ? 193  TRP   D CH2  1 
ATOM   22191 H  H    . TRP   D  4  193 ? 24.907  -61.595 -97.979  1.00 154.85 ? 193  TRP   D H    1 
ATOM   22192 H  HA   . TRP   D  4  193 ? 26.615  -63.143 -96.563  1.00 146.28 ? 193  TRP   D HA   1 
ATOM   22193 H  HB2  . TRP   D  4  193 ? 24.989  -62.454 -94.981  1.00 137.38 ? 193  TRP   D HB2  1 
ATOM   22194 H  HB3  . TRP   D  4  193 ? 23.893  -63.188 -95.868  1.00 137.38 ? 193  TRP   D HB3  1 
ATOM   22195 H  HD1  . TRP   D  4  193 ? 26.702  -64.071 -93.663  1.00 117.07 ? 193  TRP   D HD1  1 
ATOM   22196 H  HE1  . TRP   D  4  193 ? 26.563  -66.364 -92.945  1.00 110.39 ? 193  TRP   D HE1  1 
ATOM   22197 H  HE3  . TRP   D  4  193 ? 22.888  -65.526 -96.378  1.00 122.05 ? 193  TRP   D HE3  1 
ATOM   22198 H  HZ2  . TRP   D  4  193 ? 24.975  -68.567 -93.482  1.00 113.19 ? 193  TRP   D HZ2  1 
ATOM   22199 H  HZ3  . TRP   D  4  193 ? 22.146  -67.712 -96.204  1.00 121.78 ? 193  TRP   D HZ3  1 
ATOM   22200 H  HH2  . TRP   D  4  193 ? 23.178  -69.206 -94.775  1.00 118.00 ? 193  TRP   D HH2  1 
ATOM   22201 N  N    . PRO   D  4  194 ? 26.055  -65.071 -98.120  1.00 121.64 ? 194  PRO   D N    1 
ATOM   22202 C  CA   . PRO   D  4  194 ? 27.224  -65.477 -97.330  1.00 117.79 ? 194  PRO   D CA   1 
ATOM   22203 C  C    . PRO   D  4  194 ? 28.562  -64.857 -97.747  1.00 122.47 ? 194  PRO   D C    1 
ATOM   22204 O  O    . PRO   D  4  194 ? 29.593  -65.325 -97.267  1.00 121.88 ? 194  PRO   D O    1 
ATOM   22205 C  CB   . PRO   D  4  194 ? 27.276  -67.003 -97.543  1.00 114.98 ? 194  PRO   D CB   1 
ATOM   22206 C  CG   . PRO   D  4  194 ? 26.010  -67.370 -98.277  1.00 115.79 ? 194  PRO   D CG   1 
ATOM   22207 C  CD   . PRO   D  4  194 ? 25.617  -66.146 -99.024  1.00 121.10 ? 194  PRO   D CD   1 
ATOM   22208 H  HA   . PRO   D  4  194 ? 27.060  -65.248 -96.402  1.00 141.39 ? 194  PRO   D HA   1 
ATOM   22209 H  HB2  . PRO   D  4  194 ? 28.057  -67.231 -98.071  1.00 138.01 ? 194  PRO   D HB2  1 
ATOM   22210 H  HB3  . PRO   D  4  194 ? 27.316  -67.450 -96.683  1.00 138.01 ? 194  PRO   D HB3  1 
ATOM   22211 H  HG2  . PRO   D  4  194 ? 26.184  -68.105 -98.886  1.00 138.99 ? 194  PRO   D HG2  1 
ATOM   22212 H  HG3  . PRO   D  4  194 ? 25.322  -67.622 -97.641  1.00 138.99 ? 194  PRO   D HG3  1 
ATOM   22213 H  HD2  . PRO   D  4  194 ? 26.077  -66.094 -99.876  1.00 145.35 ? 194  PRO   D HD2  1 
ATOM   22214 H  HD3  . PRO   D  4  194 ? 24.657  -66.115 -99.163  1.00 145.35 ? 194  PRO   D HD3  1 
ATOM   22215 N  N    . SER   D  4  195 ? 28.558  -63.830 -98.601  1.00 127.81 ? 195  SER   D N    1 
ATOM   22216 C  CA   . SER   D  4  195 ? 29.823  -63.259 -99.058  1.00 134.82 ? 195  SER   D CA   1 
ATOM   22217 C  C    . SER   D  4  195 ? 30.675  -62.794 -97.883  1.00 135.67 ? 195  SER   D C    1 
ATOM   22218 O  O    . SER   D  4  195 ? 31.906  -62.910 -97.913  1.00 140.19 ? 195  SER   D O    1 
ATOM   22219 C  CB   . SER   D  4  195 ? 29.565  -62.103 -100.024 1.00 140.07 ? 195  SER   D CB   1 
ATOM   22220 O  OG   . SER   D  4  195 ? 28.937  -61.019 -99.365  1.00 137.75 ? 195  SER   D OG   1 
ATOM   22221 H  H    . SER   D  4  195 ? 27.853  -63.455 -98.922  1.00 153.41 ? 195  SER   D H    1 
ATOM   22222 H  HA   . SER   D  4  195 ? 30.317  -63.944 -99.537  1.00 161.82 ? 195  SER   D HA   1 
ATOM   22223 H  HB2  . SER   D  4  195 ? 30.413  -61.801 -100.387 1.00 168.12 ? 195  SER   D HB2  1 
ATOM   22224 H  HB3  . SER   D  4  195 ? 28.989  -62.413 -100.740 1.00 168.12 ? 195  SER   D HB3  1 
ATOM   22225 H  HG   . SER   D  4  195 ? 28.329  -60.701 -99.850  1.00 165.33 ? 195  SER   D HG   1 
ATOM   22226 N  N    . GLN   D  4  196 ? 30.039  -62.265 -96.841  1.00 133.69 ? 196  GLN   D N    1 
ATOM   22227 C  CA   . GLN   D  4  196 ? 30.709  -61.874 -95.610  1.00 132.23 ? 196  GLN   D CA   1 
ATOM   22228 C  C    . GLN   D  4  196 ? 30.204  -62.756 -94.476  1.00 123.07 ? 196  GLN   D C    1 
ATOM   22229 O  O    . GLN   D  4  196 ? 29.053  -63.203 -94.485  1.00 116.54 ? 196  GLN   D O    1 
ATOM   22230 C  CB   . GLN   D  4  196 ? 30.465  -60.396 -95.292  1.00 136.03 ? 196  GLN   D CB   1 
ATOM   22231 C  CG   . GLN   D  4  196 ? 30.904  -59.455 -96.405  1.00 148.37 ? 196  GLN   D CG   1 
ATOM   22232 C  CD   . GLN   D  4  196 ? 30.337  -58.059 -96.248  1.00 158.43 ? 196  GLN   D CD   1 
ATOM   22233 O  OE1  . GLN   D  4  196 ? 29.178  -57.807 -96.579  1.00 163.73 ? 196  GLN   D OE1  1 
ATOM   22234 N  NE2  . GLN   D  4  196 ? 31.151  -57.143 -95.742  1.00 162.52 ? 196  GLN   D NE2  1 
ATOM   22235 H  H    . GLN   D  4  196 ? 29.192  -62.118 -96.826  1.00 160.46 ? 196  GLN   D H    1 
ATOM   22236 H  HA   . GLN   D  4  196 ? 31.668  -61.999 -95.690  1.00 158.71 ? 196  GLN   D HA   1 
ATOM   22237 H  HB2  . GLN   D  4  196 ? 29.515  -60.260 -95.146  1.00 163.27 ? 196  GLN   D HB2  1 
ATOM   22238 H  HB3  . GLN   D  4  196 ? 30.960  -60.162 -94.492  1.00 163.27 ? 196  GLN   D HB3  1 
ATOM   22239 H  HG2  . GLN   D  4  196 ? 31.872  -59.388 -96.398  1.00 178.08 ? 196  GLN   D HG2  1 
ATOM   22240 H  HG3  . GLN   D  4  196 ? 30.601  -59.808 -97.256  1.00 178.08 ? 196  GLN   D HG3  1 
ATOM   22241 H  HE21 . GLN   D  4  196 ? 31.955  -57.357 -95.523  1.00 195.06 ? 196  GLN   D HE21 1 
ATOM   22242 H  HE22 . GLN   D  4  196 ? 30.876  -56.336 -95.634  1.00 195.06 ? 196  GLN   D HE22 1 
ATOM   22243 N  N    . SER   D  4  197 ? 31.070  -63.005 -93.498  1.00 119.20 ? 197  SER   D N    1 
ATOM   22244 C  CA   . SER   D  4  197 ? 30.796  -63.998 -92.469  1.00 115.33 ? 197  SER   D CA   1 
ATOM   22245 C  C    . SER   D  4  197 ? 30.058  -63.364 -91.298  1.00 110.49 ? 197  SER   D C    1 
ATOM   22246 O  O    . SER   D  4  197 ? 30.472  -62.320 -90.783  1.00 113.22 ? 197  SER   D O    1 
ATOM   22247 C  CB   . SER   D  4  197 ? 32.095  -64.643 -91.984  1.00 118.30 ? 197  SER   D CB   1 
ATOM   22248 O  OG   . SER   D  4  197 ? 32.577  -64.004 -90.816  1.00 115.81 ? 197  SER   D OG   1 
ATOM   22249 H  H    . SER   D  4  197 ? 31.828  -62.608 -93.410  1.00 143.07 ? 197  SER   D H    1 
ATOM   22250 H  HA   . SER   D  4  197 ? 30.227  -64.689 -92.843  1.00 138.44 ? 197  SER   D HA   1 
ATOM   22251 H  HB2  . SER   D  4  197 ? 31.927  -65.578 -91.785  1.00 142.00 ? 197  SER   D HB2  1 
ATOM   22252 H  HB3  . SER   D  4  197 ? 32.764  -64.568 -92.683  1.00 142.00 ? 197  SER   D HB3  1 
ATOM   22253 H  HG   . SER   D  4  197 ? 33.323  -64.323 -90.601  1.00 139.01 ? 197  SER   D HG   1 
ATOM   22254 N  N    . ILE   D  4  198 ? 28.970  -64.004 -90.879  1.00 102.02 ? 198  ILE   D N    1 
ATOM   22255 C  CA   . ILE   D  4  198 ? 28.167  -63.565 -89.744  1.00 92.61  ? 198  ILE   D CA   1 
ATOM   22256 C  C    . ILE   D  4  198 ? 28.311  -64.599 -88.638  1.00 88.65  ? 198  ILE   D C    1 
ATOM   22257 O  O    . ILE   D  4  198 ? 28.121  -65.799 -88.872  1.00 87.89  ? 198  ILE   D O    1 
ATOM   22258 C  CB   . ILE   D  4  198 ? 26.693  -63.371 -90.142  1.00 88.14  ? 198  ILE   D CB   1 
ATOM   22259 C  CG1  . ILE   D  4  198 ? 26.584  -62.196 -91.118  1.00 94.01  ? 198  ILE   D CG1  1 
ATOM   22260 C  CG2  . ILE   D  4  198 ? 25.821  -63.146 -88.907  1.00 81.98  ? 198  ILE   D CG2  1 
ATOM   22261 C  CD1  . ILE   D  4  198 ? 25.178  -61.879 -91.567  1.00 97.44  ? 198  ILE   D CD1  1 
ATOM   22262 H  H    . ILE   D  4  198 ? 28.668  -64.719 -91.249  1.00 122.46 ? 198  ILE   D H    1 
ATOM   22263 H  HA   . ILE   D  4  198 ? 28.502  -62.717 -89.414  1.00 111.17 ? 198  ILE   D HA   1 
ATOM   22264 H  HB   . ILE   D  4  198 ? 26.373  -64.175 -90.580  1.00 105.80 ? 198  ILE   D HB   1 
ATOM   22265 H  HG12 . ILE   D  4  198 ? 26.939  -61.403 -90.687  1.00 112.85 ? 198  ILE   D HG12 1 
ATOM   22266 H  HG13 . ILE   D  4  198 ? 27.104  -62.404 -91.910  1.00 112.85 ? 198  ILE   D HG13 1 
ATOM   22267 H  HG21 . ILE   D  4  198 ? 24.900  -63.029 -89.188  1.00 98.41  ? 198  ILE   D HG21 1 
ATOM   22268 H  HG22 . ILE   D  4  198 ? 25.894  -63.917 -88.324  1.00 98.41  ? 198  ILE   D HG22 1 
ATOM   22269 H  HG23 . ILE   D  4  198 ? 26.129  -62.351 -88.444  1.00 98.41  ? 198  ILE   D HG23 1 
ATOM   22270 H  HD11 . ILE   D  4  198 ? 25.209  -61.159 -92.217  1.00 116.96 ? 198  ILE   D HD11 1 
ATOM   22271 H  HD12 . ILE   D  4  198 ? 24.789  -62.671 -91.970  1.00 116.96 ? 198  ILE   D HD12 1 
ATOM   22272 H  HD13 . ILE   D  4  198 ? 24.654  -61.608 -90.798  1.00 116.96 ? 198  ILE   D HD13 1 
ATOM   22273 N  N    . THR   D  4  199 ? 28.644  -64.134 -87.436  1.00 87.91  ? 199  THR   D N    1 
ATOM   22274 C  CA   . THR   D  4  199 ? 28.904  -65.010 -86.305  1.00 86.61  ? 199  THR   D CA   1 
ATOM   22275 C  C    . THR   D  4  199 ? 28.046  -64.606 -85.118  1.00 85.06  ? 199  THR   D C    1 
ATOM   22276 O  O    . THR   D  4  199 ? 27.845  -63.416 -84.854  1.00 85.04  ? 199  THR   D O    1 
ATOM   22277 C  CB   . THR   D  4  199 ? 30.382  -64.978 -85.896  1.00 90.92  ? 199  THR   D CB   1 
ATOM   22278 O  OG1  . THR   D  4  199 ? 31.193  -65.418 -86.991  1.00 95.82  ? 199  THR   D OG1  1 
ATOM   22279 C  CG2  . THR   D  4  199 ? 30.626  -65.880 -84.687  1.00 89.59  ? 199  THR   D CG2  1 
ATOM   22280 H  H    . THR   D  4  199 ? 28.726  -63.298 -87.250  1.00 105.53 ? 199  THR   D H    1 
ATOM   22281 H  HA   . THR   D  4  199 ? 28.670  -65.918 -86.555  1.00 103.97 ? 199  THR   D HA   1 
ATOM   22282 H  HB   . THR   D  4  199 ? 30.630  -64.073 -85.653  1.00 109.14 ? 199  THR   D HB   1 
ATOM   22283 H  HG1  . THR   D  4  199 ? 32.004  -65.405 -86.772  1.00 115.02 ? 199  THR   D HG1  1 
ATOM   22284 H  HG21 . THR   D  4  199 ? 31.572  -65.900 -84.474  1.00 107.54 ? 199  THR   D HG21 1 
ATOM   22285 H  HG22 . THR   D  4  199 ? 30.137  -65.546 -83.919  1.00 107.54 ? 199  THR   D HG22 1 
ATOM   22286 H  HG23 . THR   D  4  199 ? 30.328  -66.783 -84.881  1.00 107.54 ? 199  THR   D HG23 1 
ATOM   22287 N  N    . CYS   D  4  200 ? 27.557  -65.612 -84.404  1.00 84.91  ? 200  CYS   D N    1 
ATOM   22288 C  CA   . CYS   D  4  200 ? 26.790  -65.434 -83.178  1.00 85.08  ? 200  CYS   D CA   1 
ATOM   22289 C  C    . CYS   D  4  200 ? 27.739  -65.603 -81.997  1.00 84.66  ? 200  CYS   D C    1 
ATOM   22290 O  O    . CYS   D  4  200 ? 28.241  -66.704 -81.749  1.00 87.97  ? 200  CYS   D O    1 
ATOM   22291 C  CB   . CYS   D  4  200 ? 25.647  -66.444 -83.128  1.00 86.19  ? 200  CYS   D CB   1 
ATOM   22292 S  SG   . CYS   D  4  200 ? 24.750  -66.551 -81.568  1.00 91.10  ? 200  CYS   D SG   1 
ATOM   22293 H  H    . CYS   D  4  200 ? 27.659  -66.439 -84.617  1.00 101.92 ? 200  CYS   D H    1 
ATOM   22294 H  HA   . CYS   D  4  200 ? 26.414  -64.540 -83.139  1.00 102.13 ? 200  CYS   D HA   1 
ATOM   22295 H  HB2  . CYS   D  4  200 ? 25.002  -66.206 -83.813  1.00 103.46 ? 200  CYS   D HB2  1 
ATOM   22296 H  HB3  . CYS   D  4  200 ? 26.013  -67.324 -83.308  1.00 103.46 ? 200  CYS   D HB3  1 
ATOM   22297 N  N    . ASN   D  4  201 ? 27.997  -64.511 -81.278  1.00 81.46  ? 201  ASN   D N    1 
ATOM   22298 C  CA   . ASN   D  4  201 ? 28.870  -64.524 -80.108  1.00 78.92  ? 201  ASN   D CA   1 
ATOM   22299 C  C    . ASN   D  4  201 ? 27.994  -64.636 -78.864  1.00 75.71  ? 201  ASN   D C    1 
ATOM   22300 O  O    . ASN   D  4  201 ? 27.221  -63.721 -78.559  1.00 72.17  ? 201  ASN   D O    1 
ATOM   22301 C  CB   . ASN   D  4  201 ? 29.736  -63.267 -80.051  1.00 80.29  ? 201  ASN   D CB   1 
ATOM   22302 C  CG   . ASN   D  4  201 ? 30.174  -62.793 -81.424  1.00 82.05  ? 201  ASN   D CG   1 
ATOM   22303 O  OD1  . ASN   D  4  201 ? 29.701  -61.769 -81.917  1.00 82.92  ? 201  ASN   D OD1  1 
ATOM   22304 N  ND2  . ASN   D  4  201 ? 31.088  -63.530 -82.044  1.00 82.04  ? 201  ASN   D ND2  1 
ATOM   22305 H  H    . ASN   D  4  201 ? 27.671  -63.735 -81.453  1.00 97.79  ? 201  ASN   D H    1 
ATOM   22306 H  HA   . ASN   D  4  201 ? 29.457  -65.295 -80.153  1.00 94.74  ? 201  ASN   D HA   1 
ATOM   22307 H  HB2  . ASN   D  4  201 ? 29.229  -62.553 -79.635  1.00 96.38  ? 201  ASN   D HB2  1 
ATOM   22308 H  HB3  . ASN   D  4  201 ? 30.533  -63.455 -79.531  1.00 96.38  ? 201  ASN   D HB3  1 
ATOM   22309 H  HD21 . ASN   D  4  201 ? 31.367  -63.301 -82.825  1.00 98.48  ? 201  ASN   D HD21 1 
ATOM   22310 H  HD22 . ASN   D  4  201 ? 31.400  -64.235 -81.665  1.00 98.48  ? 201  ASN   D HD22 1 
ATOM   22311 N  N    . VAL   D  4  202 ? 28.115  -65.752 -78.150  1.00 75.66  ? 202  VAL   D N    1 
ATOM   22312 C  CA   . VAL   D  4  202 ? 27.331  -66.016 -76.950  1.00 77.67  ? 202  VAL   D CA   1 
ATOM   22313 C  C    . VAL   D  4  202 ? 28.282  -66.160 -75.772  1.00 78.14  ? 202  VAL   D C    1 
ATOM   22314 O  O    . VAL   D  4  202 ? 29.368  -66.736 -75.904  1.00 83.80  ? 202  VAL   D O    1 
ATOM   22315 C  CB   . VAL   D  4  202 ? 26.460  -67.280 -77.106  1.00 78.05  ? 202  VAL   D CB   1 
ATOM   22316 C  CG1  . VAL   D  4  202 ? 25.690  -67.566 -75.823  1.00 78.39  ? 202  VAL   D CG1  1 
ATOM   22317 C  CG2  . VAL   D  4  202 ? 25.503  -67.123 -78.278  1.00 76.31  ? 202  VAL   D CG2  1 
ATOM   22318 H  H    . VAL   D  4  202 ? 28.660  -66.387 -78.348  1.00 90.83  ? 202  VAL   D H    1 
ATOM   22319 H  HA   . VAL   D  4  202 ? 26.745  -65.262 -76.780  1.00 93.24  ? 202  VAL   D HA   1 
ATOM   22320 H  HB   . VAL   D  4  202 ? 27.039  -68.038 -77.283  1.00 93.70  ? 202  VAL   D HB   1 
ATOM   22321 H  HG11 . VAL   D  4  202 ? 25.136  -68.352 -75.955  1.00 94.11  ? 202  VAL   D HG11 1 
ATOM   22322 H  HG12 . VAL   D  4  202 ? 26.322  -67.724 -75.104  1.00 94.11  ? 202  VAL   D HG12 1 
ATOM   22323 H  HG13 . VAL   D  4  202 ? 25.132  -66.801 -75.611  1.00 94.11  ? 202  VAL   D HG13 1 
ATOM   22324 H  HG21 . VAL   D  4  202 ? 24.975  -67.932 -78.364  1.00 91.60  ? 202  VAL   D HG21 1 
ATOM   22325 H  HG22 . VAL   D  4  202 ? 24.923  -66.364 -78.112  1.00 91.60  ? 202  VAL   D HG22 1 
ATOM   22326 H  HG23 . VAL   D  4  202 ? 26.017  -66.976 -79.087  1.00 91.60  ? 202  VAL   D HG23 1 
ATOM   22327 N  N    . ALA   D  4  203 ? 27.869  -65.640 -74.618  1.00 77.73  ? 203  ALA   D N    1 
ATOM   22328 C  CA   . ALA   D  4  203 ? 28.664  -65.712 -73.400  1.00 74.74  ? 203  ALA   D CA   1 
ATOM   22329 C  C    . ALA   D  4  203 ? 27.749  -66.000 -72.221  1.00 73.22  ? 203  ALA   D C    1 
ATOM   22330 O  O    . ALA   D  4  203 ? 26.755  -65.297 -72.020  1.00 73.12  ? 203  ALA   D O    1 
ATOM   22331 C  CB   . ALA   D  4  203 ? 29.434  -64.409 -73.161  1.00 80.26  ? 203  ALA   D CB   1 
ATOM   22332 H  H    . ALA   D  4  203 ? 27.118  -65.233 -74.516  1.00 93.31  ? 203  ALA   D H    1 
ATOM   22333 H  HA   . ALA   D  4  203 ? 29.303  -66.438 -73.476  1.00 89.72  ? 203  ALA   D HA   1 
ATOM   22334 H  HB1  . ALA   D  4  203 ? 29.952  -64.493 -72.345  1.00 96.34  ? 203  ALA   D HB1  1 
ATOM   22335 H  HB2  . ALA   D  4  203 ? 30.026  -64.249 -73.913  1.00 96.34  ? 203  ALA   D HB2  1 
ATOM   22336 H  HB3  . ALA   D  4  203 ? 28.801  -63.678 -73.078  1.00 96.34  ? 203  ALA   D HB3  1 
ATOM   22337 N  N    . HIS   D  4  204 ? 28.087  -67.029 -71.450  1.00 72.59  ? 204  HIS   D N    1 
ATOM   22338 C  CA   . HIS   D  4  204 ? 27.359  -67.376 -70.228  1.00 76.29  ? 204  HIS   D CA   1 
ATOM   22339 C  C    . HIS   D  4  204 ? 28.317  -67.240 -69.053  1.00 82.67  ? 204  HIS   D C    1 
ATOM   22340 O  O    . HIS   D  4  204 ? 29.090  -68.173 -68.769  1.00 83.17  ? 204  HIS   D O    1 
ATOM   22341 C  CB   . HIS   D  4  204 ? 26.793  -68.792 -70.307  1.00 75.08  ? 204  HIS   D CB   1 
ATOM   22342 C  CG   . HIS   D  4  204 ? 25.789  -69.099 -69.240  1.00 75.60  ? 204  HIS   D CG   1 
ATOM   22343 N  ND1  . HIS   D  4  204 ? 25.859  -70.230 -68.455  1.00 76.49  ? 204  HIS   D ND1  1 
ATOM   22344 C  CD2  . HIS   D  4  204 ? 24.693  -68.421 -68.824  1.00 76.51  ? 204  HIS   D CD2  1 
ATOM   22345 C  CE1  . HIS   D  4  204 ? 24.849  -70.237 -67.604  1.00 78.48  ? 204  HIS   D CE1  1 
ATOM   22346 N  NE2  . HIS   D  4  204 ? 24.126  -69.150 -67.807  1.00 78.97  ? 204  HIS   D NE2  1 
ATOM   22347 H  H    . HIS   D  4  204 ? 28.748  -67.554 -71.615  1.00 87.14  ? 204  HIS   D H    1 
ATOM   22348 H  HA   . HIS   D  4  204 ? 26.613  -66.768 -70.104  1.00 91.58  ? 204  HIS   D HA   1 
ATOM   22349 H  HB2  . HIS   D  4  204 ? 26.356  -68.906 -71.166  1.00 90.13  ? 204  HIS   D HB2  1 
ATOM   22350 H  HB3  . HIS   D  4  204 ? 27.522  -69.425 -70.219  1.00 90.13  ? 204  HIS   D HB3  1 
ATOM   22351 H  HD2  . HIS   D  4  204 ? 24.382  -67.613 -69.164  1.00 91.84  ? 204  HIS   D HD2  1 
ATOM   22352 H  HE1  . HIS   D  4  204 ? 24.676  -70.895 -66.970  1.00 94.21  ? 204  HIS   D HE1  1 
ATOM   22353 H  HE2  . HIS   D  4  204 ? 23.416  -68.933 -67.372  1.00 94.80  ? 204  HIS   D HE2  1 
ATOM   22354 N  N    . PRO   D  4  205 ? 28.308  -66.111 -68.337  1.00 86.57  ? 205  PRO   D N    1 
ATOM   22355 C  CA   . PRO   D  4  205 ? 29.340  -65.906 -67.307  1.00 90.22  ? 205  PRO   D CA   1 
ATOM   22356 C  C    . PRO   D  4  205 ? 29.290  -66.937 -66.197  1.00 95.12  ? 205  PRO   D C    1 
ATOM   22357 O  O    . PRO   D  4  205 ? 30.339  -67.339 -65.679  1.00 96.67  ? 205  PRO   D O    1 
ATOM   22358 C  CB   . PRO   D  4  205 ? 29.031  -64.494 -66.790  1.00 90.44  ? 205  PRO   D CB   1 
ATOM   22359 C  CG   . PRO   D  4  205 ? 27.566  -64.341 -67.001  1.00 88.96  ? 205  PRO   D CG   1 
ATOM   22360 C  CD   . PRO   D  4  205 ? 27.267  -65.068 -68.286  1.00 85.86  ? 205  PRO   D CD   1 
ATOM   22361 H  HA   . PRO   D  4  205 ? 30.221  -65.916 -67.714  1.00 108.30 ? 205  PRO   D HA   1 
ATOM   22362 H  HB2  . PRO   D  4  205 ? 29.258  -64.427 -65.849  1.00 108.56 ? 205  PRO   D HB2  1 
ATOM   22363 H  HB3  . PRO   D  4  205 ? 29.530  -63.836 -67.299  1.00 108.56 ? 205  PRO   D HB3  1 
ATOM   22364 H  HG2  . PRO   D  4  205 ? 27.084  -64.739 -66.260  1.00 106.78 ? 205  PRO   D HG2  1 
ATOM   22365 H  HG3  . PRO   D  4  205 ? 27.342  -63.400 -67.077  1.00 106.78 ? 205  PRO   D HG3  1 
ATOM   22366 H  HD2  . PRO   D  4  205 ? 26.382  -65.464 -68.260  1.00 103.07 ? 205  PRO   D HD2  1 
ATOM   22367 H  HD3  . PRO   D  4  205 ? 27.341  -64.469 -69.046  1.00 103.07 ? 205  PRO   D HD3  1 
ATOM   22368 N  N    . ALA   D  4  206 ? 28.090  -67.382 -65.820  1.00 100.58 ? 206  ALA   D N    1 
ATOM   22369 C  CA   . ALA   D  4  206 ? 27.965  -68.355 -64.742  1.00 108.40 ? 206  ALA   D CA   1 
ATOM   22370 C  C    . ALA   D  4  206 ? 28.765  -69.620 -65.025  1.00 109.77 ? 206  ALA   D C    1 
ATOM   22371 O  O    . ALA   D  4  206 ? 29.163  -70.322 -64.088  1.00 115.26 ? 206  ALA   D O    1 
ATOM   22372 C  CB   . ALA   D  4  206 ? 26.494  -68.703 -64.526  1.00 108.45 ? 206  ALA   D CB   1 
ATOM   22373 H  H    . ALA   D  4  206 ? 27.343  -67.137 -66.168  1.00 120.73 ? 206  ALA   D H    1 
ATOM   22374 H  HA   . ALA   D  4  206 ? 28.311  -67.961 -63.927  1.00 130.12 ? 206  ALA   D HA   1 
ATOM   22375 H  HB1  . ALA   D  4  206 ? 26.425  -69.354 -63.810  1.00 130.18 ? 206  ALA   D HB1  1 
ATOM   22376 H  HB2  . ALA   D  4  206 ? 26.011  -67.897 -64.288  1.00 130.18 ? 206  ALA   D HB2  1 
ATOM   22377 H  HB3  . ALA   D  4  206 ? 26.133  -69.075 -65.347  1.00 130.18 ? 206  ALA   D HB3  1 
ATOM   22378 N  N    . SER   D  4  207 ? 29.014  -69.925 -66.298  1.00 104.52 ? 207  SER   D N    1 
ATOM   22379 C  CA   . SER   D  4  207 ? 29.716  -71.140 -66.688  1.00 103.17 ? 207  SER   D CA   1 
ATOM   22380 C  C    . SER   D  4  207 ? 31.092  -70.865 -67.280  1.00 103.07 ? 207  SER   D C    1 
ATOM   22381 O  O    . SER   D  4  207 ? 31.735  -71.794 -67.779  1.00 104.61 ? 207  SER   D O    1 
ATOM   22382 C  CB   . SER   D  4  207 ? 28.876  -71.932 -67.694  1.00 100.60 ? 207  SER   D CB   1 
ATOM   22383 O  OG   . SER   D  4  207 ? 27.655  -72.362 -67.119  1.00 103.73 ? 207  SER   D OG   1 
ATOM   22384 H  H    . SER   D  4  207 ? 28.780  -69.434 -66.963  1.00 125.47 ? 207  SER   D H    1 
ATOM   22385 H  HA   . SER   D  4  207 ? 29.839  -71.684 -65.894  1.00 123.84 ? 207  SER   D HA   1 
ATOM   22386 H  HB2  . SER   D  4  207 ? 28.681  -71.365 -68.456  1.00 120.76 ? 207  SER   D HB2  1 
ATOM   22387 H  HB3  . SER   D  4  207 ? 29.379  -72.710 -67.980  1.00 120.76 ? 207  SER   D HB3  1 
ATOM   22388 H  HG   . SER   D  4  207 ? 27.033  -71.847 -67.347  1.00 124.52 ? 207  SER   D HG   1 
ATOM   22389 N  N    . SER   D  4  208 ? 31.564  -69.620 -67.232  1.00 101.00 ? 208  SER   D N    1 
ATOM   22390 C  CA   . SER   D  4  208 ? 32.806  -69.243 -67.904  1.00 103.07 ? 208  SER   D CA   1 
ATOM   22391 C  C    . SER   D  4  208 ? 32.791  -69.732 -69.350  1.00 100.20 ? 208  SER   D C    1 
ATOM   22392 O  O    . SER   D  4  208 ? 33.787  -70.237 -69.873  1.00 102.15 ? 208  SER   D O    1 
ATOM   22393 C  CB   . SER   D  4  208 ? 34.025  -69.784 -67.155  1.00 109.57 ? 208  SER   D CB   1 
ATOM   22394 O  OG   . SER   D  4  208 ? 34.081  -69.271 -65.835  1.00 115.00 ? 208  SER   D OG   1 
ATOM   22395 H  H    . SER   D  4  208 ? 31.182  -68.972 -66.814  1.00 121.24 ? 208  SER   D H    1 
ATOM   22396 H  HA   . SER   D  4  208 ? 32.876  -68.276 -67.914  1.00 123.72 ? 208  SER   D HA   1 
ATOM   22397 H  HB2  . SER   D  4  208 ? 33.965  -70.751 -67.115  1.00 131.53 ? 208  SER   D HB2  1 
ATOM   22398 H  HB3  . SER   D  4  208 ? 34.828  -69.520 -67.630  1.00 131.53 ? 208  SER   D HB3  1 
ATOM   22399 H  HG   . SER   D  4  208 ? 34.789  -69.522 -65.460  1.00 138.04 ? 208  SER   D HG   1 
ATOM   22400 N  N    . THR   D  4  209 ? 31.637  -69.590 -69.996  1.00 95.31  ? 209  THR   D N    1 
ATOM   22401 C  CA   . THR   D  4  209 ? 31.427  -70.053 -71.358  1.00 91.36  ? 209  THR   D CA   1 
ATOM   22402 C  C    . THR   D  4  209 ? 31.553  -68.889 -72.330  1.00 88.66  ? 209  THR   D C    1 
ATOM   22403 O  O    . THR   D  4  209 ? 31.125  -67.770 -72.036  1.00 87.63  ? 209  THR   D O    1 
ATOM   22404 C  CB   . THR   D  4  209 ? 30.046  -70.700 -71.506  1.00 92.02  ? 209  THR   D CB   1 
ATOM   22405 O  OG1  . THR   D  4  209 ? 29.900  -71.751 -70.543  1.00 95.99  ? 209  THR   D OG1  1 
ATOM   22406 C  CG2  . THR   D  4  209 ? 29.860  -71.270 -72.909  1.00 88.14  ? 209  THR   D CG2  1 
ATOM   22407 H  H    . THR   D  4  209 ? 30.942  -69.216 -69.653  1.00 114.41 ? 209  THR   D H    1 
ATOM   22408 H  HA   . THR   D  4  209 ? 32.101  -70.714 -71.580  1.00 109.67 ? 209  THR   D HA   1 
ATOM   22409 H  HB   . THR   D  4  209 ? 29.362  -70.028 -71.360  1.00 110.46 ? 209  THR   D HB   1 
ATOM   22410 H  HG1  . THR   D  4  209 ? 29.751  -72.480 -70.934  1.00 115.23 ? 209  THR   D HG1  1 
ATOM   22411 H  HG21 . THR   D  4  209 ? 28.994  -71.700 -72.980  1.00 105.80 ? 209  THR   D HG21 1 
ATOM   22412 H  HG22 . THR   D  4  209 ? 29.913  -70.558 -73.566  1.00 105.80 ? 209  THR   D HG22 1 
ATOM   22413 H  HG23 . THR   D  4  209 ? 30.552  -71.923 -73.097  1.00 105.80 ? 209  THR   D HG23 1 
ATOM   22414 N  N    . LYS   D  4  210 ? 32.144  -69.162 -73.491  1.00 90.31  ? 210  LYS   D N    1 
ATOM   22415 C  CA   . LYS   D  4  210 ? 32.219  -68.176 -74.567  1.00 94.10  ? 210  LYS   D CA   1 
ATOM   22416 C  C    . LYS   D  4  210 ? 32.301  -68.932 -75.885  1.00 96.36  ? 210  LYS   D C    1 
ATOM   22417 O  O    . LYS   D  4  210 ? 33.348  -69.500 -76.209  1.00 98.59  ? 210  LYS   D O    1 
ATOM   22418 C  CB   . LYS   D  4  210 ? 33.417  -67.248 -74.392  1.00 97.75  ? 210  LYS   D CB   1 
ATOM   22419 C  CG   . LYS   D  4  210 ? 33.048  -65.839 -73.960  1.00 99.41  ? 210  LYS   D CG   1 
ATOM   22420 C  CD   . LYS   D  4  210 ? 34.254  -64.915 -74.012  1.00 104.86 ? 210  LYS   D CD   1 
ATOM   22421 C  CE   . LYS   D  4  210 ? 33.917  -63.524 -73.501  1.00 108.65 ? 210  LYS   D CE   1 
ATOM   22422 N  NZ   . LYS   D  4  210 ? 33.500  -63.544 -72.073  1.00 112.80 ? 210  LYS   D NZ   1 
ATOM   22423 H  H    . LYS   D  4  210 ? 32.513  -69.915 -73.682  1.00 108.41 ? 210  LYS   D H    1 
ATOM   22424 H  HA   . LYS   D  4  210 ? 31.413  -67.637 -74.564  1.00 112.96 ? 210  LYS   D HA   1 
ATOM   22425 H  HB2  . LYS   D  4  210 ? 34.003  -67.620 -73.715  1.00 117.33 ? 210  LYS   D HB2  1 
ATOM   22426 H  HB3  . LYS   D  4  210 ? 33.886  -67.184 -75.239  1.00 117.33 ? 210  LYS   D HB3  1 
ATOM   22427 H  HG2  . LYS   D  4  210 ? 32.367  -65.487 -74.555  1.00 119.33 ? 210  LYS   D HG2  1 
ATOM   22428 H  HG3  . LYS   D  4  210 ? 32.715  -65.857 -73.049  1.00 119.33 ? 210  LYS   D HG3  1 
ATOM   22429 H  HD2  . LYS   D  4  210 ? 34.961  -65.280 -73.458  1.00 125.87 ? 210  LYS   D HD2  1 
ATOM   22430 H  HD3  . LYS   D  4  210 ? 34.558  -64.836 -74.930  1.00 125.87 ? 210  LYS   D HD3  1 
ATOM   22431 H  HE2  . LYS   D  4  210 ? 34.699  -62.956 -73.581  1.00 130.42 ? 210  LYS   D HE2  1 
ATOM   22432 H  HE3  . LYS   D  4  210 ? 33.187  -63.159 -74.026  1.00 130.42 ? 210  LYS   D HE3  1 
ATOM   22433 H  HZ1  . LYS   D  4  210 ? 33.467  -62.713 -71.754  1.00 135.40 ? 210  LYS   D HZ1  1 
ATOM   22434 H  HZ2  . LYS   D  4  210 ? 32.695  -63.915 -71.996  1.00 135.40 ? 210  LYS   D HZ2  1 
ATOM   22435 H  HZ3  . LYS   D  4  210 ? 34.083  -64.014 -71.592  1.00 135.40 ? 210  LYS   D HZ3  1 
ATOM   22436 N  N    . VAL   D  4  211 ? 31.204  -68.936 -76.636  1.00 92.13  ? 211  VAL   D N    1 
ATOM   22437 C  CA   . VAL   D  4  211 ? 31.126  -69.603 -77.929  1.00 91.66  ? 211  VAL   D CA   1 
ATOM   22438 C  C    . VAL   D  4  211 ? 30.966  -68.547 -79.012  1.00 90.74  ? 211  VAL   D C    1 
ATOM   22439 O  O    . VAL   D  4  211 ? 30.277  -67.539 -78.818  1.00 87.90  ? 211  VAL   D O    1 
ATOM   22440 C  CB   . VAL   D  4  211 ? 29.964  -70.615 -77.973  1.00 93.66  ? 211  VAL   D CB   1 
ATOM   22441 C  CG1  . VAL   D  4  211 ? 29.822  -71.214 -79.369  1.00 95.39  ? 211  VAL   D CG1  1 
ATOM   22442 C  CG2  . VAL   D  4  211 ? 30.177  -71.712 -76.939  1.00 95.12  ? 211  VAL   D CG2  1 
ATOM   22443 H  H    . VAL   D  4  211 ? 30.471  -68.547 -76.410  1.00 110.59 ? 211  VAL   D H    1 
ATOM   22444 H  HA   . VAL   D  4  211 ? 31.954  -70.083 -78.089  1.00 110.03 ? 211  VAL   D HA   1 
ATOM   22445 H  HB   . VAL   D  4  211 ? 29.139  -70.152 -77.761  1.00 112.43 ? 211  VAL   D HB   1 
ATOM   22446 H  HG11 . VAL   D  4  211 ? 29.124  -71.887 -79.354  1.00 114.50 ? 211  VAL   D HG11 1 
ATOM   22447 H  HG12 . VAL   D  4  211 ? 29.587  -70.508 -79.993  1.00 114.50 ? 211  VAL   D HG12 1 
ATOM   22448 H  HG13 . VAL   D  4  211 ? 30.665  -71.617 -79.628  1.00 114.50 ? 211  VAL   D HG13 1 
ATOM   22449 H  HG21 . VAL   D  4  211 ? 29.441  -72.342 -76.990  1.00 114.18 ? 211  VAL   D HG21 1 
ATOM   22450 H  HG22 . VAL   D  4  211 ? 31.013  -72.166 -77.128  1.00 114.18 ? 211  VAL   D HG22 1 
ATOM   22451 H  HG23 . VAL   D  4  211 ? 30.210  -71.312 -76.056  1.00 114.18 ? 211  VAL   D HG23 1 
ATOM   22452 N  N    . ASP   D  4  212 ? 31.613  -68.782 -80.153  1.00 96.25  ? 212  ASP   D N    1 
ATOM   22453 C  CA   . ASP   D  4  212 ? 31.474  -67.954 -81.351  1.00 96.51  ? 212  ASP   D CA   1 
ATOM   22454 C  C    . ASP   D  4  212 ? 31.073  -68.901 -82.481  1.00 93.67  ? 212  ASP   D C    1 
ATOM   22455 O  O    . ASP   D  4  212 ? 31.933  -69.524 -83.111  1.00 93.80  ? 212  ASP   D O    1 
ATOM   22456 C  CB   . ASP   D  4  212 ? 32.770  -67.203 -81.670  1.00 102.29 ? 212  ASP   D CB   1 
ATOM   22457 C  CG   . ASP   D  4  212 ? 33.153  -66.210 -80.591  1.00 102.93 ? 212  ASP   D CG   1 
ATOM   22458 O  OD1  . ASP   D  4  212 ? 32.243  -65.590 -80.002  1.00 100.38 ? 212  ASP   D OD1  1 
ATOM   22459 O  OD2  . ASP   D  4  212 ? 34.365  -66.049 -80.333  1.00 106.15 ? 212  ASP   D OD2  1 
ATOM   22460 H  H    . ASP   D  4  212 ? 32.157  -69.439 -80.261  1.00 115.54 ? 212  ASP   D H    1 
ATOM   22461 H  HA   . ASP   D  4  212 ? 30.777  -67.293 -81.217  1.00 115.85 ? 212  ASP   D HA   1 
ATOM   22462 H  HB2  . ASP   D  4  212 ? 33.493  -67.843 -81.760  1.00 122.79 ? 212  ASP   D HB2  1 
ATOM   22463 H  HB3  . ASP   D  4  212 ? 32.655  -66.714 -82.500  1.00 122.79 ? 212  ASP   D HB3  1 
ATOM   22464 N  N    . LYS   D  4  213 ? 29.769  -69.011 -82.732  1.00 92.56  ? 213  LYS   D N    1 
ATOM   22465 C  CA   . LYS   D  4  213 ? 29.231  -69.947 -83.714  1.00 93.38  ? 213  LYS   D CA   1 
ATOM   22466 C  C    . LYS   D  4  213 ? 28.999  -69.223 -85.037  1.00 88.30  ? 213  LYS   D C    1 
ATOM   22467 O  O    . LYS   D  4  213 ? 28.059  -68.431 -85.162  1.00 84.37  ? 213  LYS   D O    1 
ATOM   22468 C  CB   . LYS   D  4  213 ? 27.933  -70.577 -83.210  1.00 97.21  ? 213  LYS   D CB   1 
ATOM   22469 C  CG   . LYS   D  4  213 ? 28.074  -72.021 -82.757  1.00 96.61  ? 213  LYS   D CG   1 
ATOM   22470 C  CD   . LYS   D  4  213 ? 28.459  -72.934 -83.914  1.00 96.94  ? 213  LYS   D CD   1 
ATOM   22471 C  CE   . LYS   D  4  213 ? 28.672  -74.361 -83.449  1.00 96.14  ? 213  LYS   D CE   1 
ATOM   22472 N  NZ   . LYS   D  4  213 ? 29.139  -75.242 -84.555  1.00 97.28  ? 213  LYS   D NZ   1 
ATOM   22473 H  H    . LYS   D  4  213 ? 29.165  -68.545 -82.336  1.00 111.11 ? 213  LYS   D H    1 
ATOM   22474 H  HA   . LYS   D  4  213 ? 29.886  -70.646 -83.865  1.00 112.09 ? 213  LYS   D HA   1 
ATOM   22475 H  HB2  . LYS   D  4  213 ? 27.613  -70.061 -82.453  1.00 116.69 ? 213  LYS   D HB2  1 
ATOM   22476 H  HB3  . LYS   D  4  213 ? 27.280  -70.555 -83.926  1.00 116.69 ? 213  LYS   D HB3  1 
ATOM   22477 H  HG2  . LYS   D  4  213 ? 28.766  -72.080 -82.080  1.00 115.97 ? 213  LYS   D HG2  1 
ATOM   22478 H  HG3  . LYS   D  4  213 ? 27.228  -72.329 -82.395  1.00 115.97 ? 213  LYS   D HG3  1 
ATOM   22479 H  HD2  . LYS   D  4  213 ? 27.749  -72.931 -84.575  1.00 116.37 ? 213  LYS   D HD2  1 
ATOM   22480 H  HD3  . LYS   D  4  213 ? 29.284  -72.616 -84.313  1.00 116.37 ? 213  LYS   D HD3  1 
ATOM   22481 H  HE2  . LYS   D  4  213 ? 29.343  -74.372 -82.749  1.00 115.40 ? 213  LYS   D HE2  1 
ATOM   22482 H  HE3  . LYS   D  4  213 ? 27.835  -74.716 -83.112  1.00 115.40 ? 213  LYS   D HE3  1 
ATOM   22483 H  HZ1  . LYS   D  4  213 ? 29.166  -76.088 -84.280  1.00 116.78 ? 213  LYS   D HZ1  1 
ATOM   22484 H  HZ2  . LYS   D  4  213 ? 28.584  -75.181 -85.248  1.00 116.78 ? 213  LYS   D HZ2  1 
ATOM   22485 H  HZ3  . LYS   D  4  213 ? 29.954  -74.997 -84.816  1.00 116.78 ? 213  LYS   D HZ3  1 
ATOM   22486 N  N    . LYS   D  4  214 ? 29.846  -69.507 -86.023  1.00 88.30  ? 214  LYS   D N    1 
ATOM   22487 C  CA   . LYS   D  4  214 ? 29.653  -68.962 -87.357  1.00 90.19  ? 214  LYS   D CA   1 
ATOM   22488 C  C    . LYS   D  4  214 ? 28.497  -69.672 -88.060  1.00 90.61  ? 214  LYS   D C    1 
ATOM   22489 O  O    . LYS   D  4  214 ? 28.142  -70.811 -87.742  1.00 92.98  ? 214  LYS   D O    1 
ATOM   22490 C  CB   . LYS   D  4  214 ? 30.932  -69.104 -88.187  1.00 94.63  ? 214  LYS   D CB   1 
ATOM   22491 C  CG   . LYS   D  4  214 ? 31.314  -67.859 -88.984  1.00 98.76  ? 214  LYS   D CG   1 
ATOM   22492 C  CD   . LYS   D  4  214 ? 32.222  -68.197 -90.166  1.00 103.75 ? 214  LYS   D CD   1 
ATOM   22493 C  CE   . LYS   D  4  214 ? 33.543  -67.437 -90.110  1.00 110.26 ? 214  LYS   D CE   1 
ATOM   22494 N  NZ   . LYS   D  4  214 ? 34.239  -67.412 -91.430  1.00 117.60 ? 214  LYS   D NZ   1 
ATOM   22495 H  H    . LYS   D  4  214 ? 30.538  -70.011 -85.943  1.00 106.00 ? 214  LYS   D H    1 
ATOM   22496 H  HA   . LYS   D  4  214 ? 29.441  -68.018 -87.292  1.00 108.26 ? 214  LYS   D HA   1 
ATOM   22497 H  HB2  . LYS   D  4  214 ? 31.668  -69.305 -87.588  1.00 113.59 ? 214  LYS   D HB2  1 
ATOM   22498 H  HB3  . LYS   D  4  214 ? 30.811  -69.830 -88.819  1.00 113.59 ? 214  LYS   D HB3  1 
ATOM   22499 H  HG2  . LYS   D  4  214 ? 30.510  -67.441 -89.329  1.00 118.55 ? 214  LYS   D HG2  1 
ATOM   22500 H  HG3  . LYS   D  4  214 ? 31.788  -67.242 -88.404  1.00 118.55 ? 214  LYS   D HG3  1 
ATOM   22501 H  HD2  . LYS   D  4  214 ? 32.419  -69.146 -90.156  1.00 124.53 ? 214  LYS   D HD2  1 
ATOM   22502 H  HD3  . LYS   D  4  214 ? 31.772  -67.959 -90.992  1.00 124.53 ? 214  LYS   D HD3  1 
ATOM   22503 H  HE2  . LYS   D  4  214 ? 33.372  -66.521 -89.842  1.00 132.35 ? 214  LYS   D HE2  1 
ATOM   22504 H  HE3  . LYS   D  4  214 ? 34.130  -67.867 -89.468  1.00 132.35 ? 214  LYS   D HE3  1 
ATOM   22505 H  HZ1  . LYS   D  4  214 ? 34.720  -66.668 -91.507  1.00 141.16 ? 214  LYS   D HZ1  1 
ATOM   22506 H  HZ2  . LYS   D  4  214 ? 34.780  -68.115 -91.502  1.00 141.16 ? 214  LYS   D HZ2  1 
ATOM   22507 H  HZ3  . LYS   D  4  214 ? 33.641  -67.440 -92.090  1.00 141.16 ? 214  LYS   D HZ3  1 
ATOM   22508 N  N    . ILE   D  4  215 ? 27.905  -68.977 -89.029  1.00 91.29  ? 215  ILE   D N    1 
ATOM   22509 C  CA   . ILE   D  4  215 ? 26.822  -69.503 -89.855  1.00 95.36  ? 215  ILE   D CA   1 
ATOM   22510 C  C    . ILE   D  4  215 ? 27.347  -69.602 -91.282  1.00 104.13 ? 215  ILE   D C    1 
ATOM   22511 O  O    . ILE   D  4  215 ? 27.779  -68.595 -91.856  1.00 107.39 ? 215  ILE   D O    1 
ATOM   22512 C  CB   . ILE   D  4  215 ? 25.576  -68.606 -89.786  1.00 97.44  ? 215  ILE   D CB   1 
ATOM   22513 C  CG1  . ILE   D  4  215 ? 25.035  -68.550 -88.355  1.00 95.17  ? 215  ILE   D CG1  1 
ATOM   22514 C  CG2  . ILE   D  4  215 ? 24.496  -69.105 -90.741  1.00 100.97 ? 215  ILE   D CG2  1 
ATOM   22515 C  CD1  . ILE   D  4  215 ? 23.992  -67.478 -88.144  1.00 97.38  ? 215  ILE   D CD1  1 
ATOM   22516 H  H    . ILE   D  4  215 ? 28.122  -68.170 -89.232  1.00 109.58 ? 215  ILE   D H    1 
ATOM   22517 H  HA   . ILE   D  4  215 ? 26.577  -70.390 -89.550  1.00 114.47 ? 215  ILE   D HA   1 
ATOM   22518 H  HB   . ILE   D  4  215 ? 25.835  -67.712 -90.057  1.00 116.96 ? 215  ILE   D HB   1 
ATOM   22519 H  HG12 . ILE   D  4  215 ? 24.630  -69.405 -88.140  1.00 114.24 ? 215  ILE   D HG12 1 
ATOM   22520 H  HG13 . ILE   D  4  215 ? 25.772  -68.370 -87.750  1.00 114.24 ? 215  ILE   D HG13 1 
ATOM   22521 H  HG21 . ILE   D  4  215 ? 23.786  -68.447 -90.786  1.00 121.20 ? 215  ILE   D HG21 1 
ATOM   22522 H  HG22 . ILE   D  4  215 ? 24.886  -69.232 -91.620  1.00 121.20 ? 215  ILE   D HG22 1 
ATOM   22523 H  HG23 . ILE   D  4  215 ? 24.146  -69.947 -90.410  1.00 121.20 ? 215  ILE   D HG23 1 
ATOM   22524 H  HD11 . ILE   D  4  215 ? 23.562  -67.620 -87.286  1.00 116.89 ? 215  ILE   D HD11 1 
ATOM   22525 H  HD12 . ILE   D  4  215 ? 24.424  -66.609 -88.157  1.00 116.89 ? 215  ILE   D HD12 1 
ATOM   22526 H  HD13 . ILE   D  4  215 ? 23.336  -67.531 -88.856  1.00 116.89 ? 215  ILE   D HD13 1 
ATOM   22527 N  N    . GLU   D  4  216 ? 27.299  -70.805 -91.865  1.00 110.85 ? 216  GLU   D N    1 
ATOM   22528 C  CA   . GLU   D  4  216 ? 27.919  -70.993 -93.172  1.00 119.18 ? 216  GLU   D CA   1 
ATOM   22529 C  C    . GLU   D  4  216 ? 26.923  -71.250 -94.302  1.00 123.98 ? 216  GLU   D C    1 
ATOM   22530 O  O    . GLU   D  4  216 ? 26.993  -70.568 -95.332  1.00 130.04 ? 216  GLU   D O    1 
ATOM   22531 C  CB   . GLU   D  4  216 ? 28.945  -72.130 -93.099  1.00 119.91 ? 216  GLU   D CB   1 
ATOM   22532 C  CG   . GLU   D  4  216 ? 30.363  -71.631 -92.821  1.00 121.70 ? 216  GLU   D CG   1 
ATOM   22533 C  CD   . GLU   D  4  216 ? 31.187  -72.587 -91.979  1.00 123.76 ? 216  GLU   D CD   1 
ATOM   22534 O  OE1  . GLU   D  4  216 ? 30.603  -73.321 -91.154  1.00 122.72 ? 216  GLU   D OE1  1 
ATOM   22535 O  OE2  . GLU   D  4  216 ? 32.425  -72.601 -92.139  1.00 128.40 ? 216  GLU   D OE2  1 
ATOM   22536 H  H    . GLU   D  4  216 ? 26.924  -71.503 -91.531  1.00 133.05 ? 216  GLU   D H    1 
ATOM   22537 H  HA   . GLU   D  4  216 ? 28.355  -70.159 -93.404  1.00 143.05 ? 216  GLU   D HA   1 
ATOM   22538 H  HB2  . GLU   D  4  216 ? 28.695  -72.735 -92.383  1.00 143.93 ? 216  GLU   D HB2  1 
ATOM   22539 H  HB3  . GLU   D  4  216 ? 28.954  -72.603 -93.945  1.00 143.93 ? 216  GLU   D HB3  1 
ATOM   22540 H  HG2  . GLU   D  4  216 ? 30.823  -71.508 -93.667  1.00 146.07 ? 216  GLU   D HG2  1 
ATOM   22541 H  HG3  . GLU   D  4  216 ? 30.311  -70.786 -92.347  1.00 146.07 ? 216  GLU   D HG3  1 
ATOM   22542 N  N    . PRO   D  4  217 ? 25.989  -72.211 -94.177  1.00 121.59 ? 217  PRO   D N    1 
ATOM   22543 C  CA   . PRO   D  4  217 ? 25.141  -72.453 -95.348  1.00 123.25 ? 217  PRO   D CA   1 
ATOM   22544 C  C    . PRO   D  4  217 ? 23.821  -71.687 -95.304  1.00 123.67 ? 217  PRO   D C    1 
ATOM   22545 O  O    . PRO   D  4  217 ? 22.764  -72.270 -95.551  1.00 126.45 ? 217  PRO   D O    1 
ATOM   22546 C  CB   . PRO   D  4  217 ? 24.906  -73.962 -95.284  1.00 122.77 ? 217  PRO   D CB   1 
ATOM   22547 C  CG   . PRO   D  4  217 ? 24.894  -74.266 -93.806  1.00 120.25 ? 217  PRO   D CG   1 
ATOM   22548 C  CD   . PRO   D  4  217 ? 25.705  -73.178 -93.101  1.00 118.13 ? 217  PRO   D CD   1 
ATOM   22549 H  HA   . PRO   D  4  217 ? 25.606  -72.224 -96.168  1.00 147.93 ? 217  PRO   D HA   1 
ATOM   22550 H  HB2  . PRO   D  4  217 ? 24.056  -74.186 -95.695  1.00 147.36 ? 217  PRO   D HB2  1 
ATOM   22551 H  HB3  . PRO   D  4  217 ? 25.626  -74.432 -95.732  1.00 147.36 ? 217  PRO   D HB3  1 
ATOM   22552 H  HG2  . PRO   D  4  217 ? 23.978  -74.263 -93.487  1.00 144.33 ? 217  PRO   D HG2  1 
ATOM   22553 H  HG3  . PRO   D  4  217 ? 25.295  -75.136 -93.656  1.00 144.33 ? 217  PRO   D HG3  1 
ATOM   22554 H  HD2  . PRO   D  4  217 ? 25.185  -72.764 -92.394  1.00 141.79 ? 217  PRO   D HD2  1 
ATOM   22555 H  HD3  . PRO   D  4  217 ? 26.527  -73.542 -92.738  1.00 141.79 ? 217  PRO   D HD3  1 
HETATM 22556 C  C1   . NAG   E  5  .   ? 67.889  25.458  -5.611   1.00 108.38 ? 1    NAG   E C1   1 
HETATM 22557 C  C2   . NAG   E  5  .   ? 68.447  24.341  -6.446   1.00 107.34 ? 1    NAG   E C2   1 
HETATM 22558 C  C3   . NAG   E  5  .   ? 68.293  24.680  -7.917   1.00 106.28 ? 1    NAG   E C3   1 
HETATM 22559 C  C4   . NAG   E  5  .   ? 66.851  25.064  -8.231   1.00 110.24 ? 1    NAG   E C4   1 
HETATM 22560 C  C5   . NAG   E  5  .   ? 66.216  25.992  -7.193   1.00 109.89 ? 1    NAG   E C5   1 
HETATM 22561 C  C6   . NAG   E  5  .   ? 64.709  26.002  -7.296   1.00 108.80 ? 1    NAG   E C6   1 
HETATM 22562 C  C7   . NAG   E  5  .   ? 70.196  23.106  -5.264   1.00 107.78 ? 1    NAG   E C7   1 
HETATM 22563 C  C8   . NAG   E  5  .   ? 71.667  22.956  -5.019   1.00 107.60 ? 1    NAG   E C8   1 
HETATM 22564 N  N2   . NAG   E  5  .   ? 69.837  24.075  -6.112   1.00 107.03 ? 1    NAG   E N2   1 
HETATM 22565 O  O3   . NAG   E  5  .   ? 68.647  23.539  -8.690   1.00 102.83 ? 1    NAG   E O3   1 
HETATM 22566 O  O4   . NAG   E  5  .   ? 66.815  25.773  -9.460   1.00 114.01 ? 1    NAG   E O4   1 
HETATM 22567 O  O5   . NAG   E  5  .   ? 66.523  25.580  -5.854   1.00 108.89 ? 1    NAG   E O5   1 
HETATM 22568 O  O6   . NAG   E  5  .   ? 64.173  24.707  -7.056   1.00 107.11 ? 1    NAG   E O6   1 
HETATM 22569 O  O7   . NAG   E  5  .   ? 69.369  22.381  -4.721   1.00 108.72 ? 1    NAG   E O7   1 
HETATM 22570 C  C1   . NAG   E  5  .   ? 66.055  24.952  -10.323  1.00 117.16 ? 2    NAG   E C1   1 
HETATM 22571 C  C2   . NAG   E  5  .   ? 65.863  25.719  -11.624  1.00 119.78 ? 2    NAG   E C2   1 
HETATM 22572 C  C3   . NAG   E  5  .   ? 65.222  24.829  -12.683  1.00 119.34 ? 2    NAG   E C3   1 
HETATM 22573 C  C4   . NAG   E  5  .   ? 65.997  23.527  -12.818  1.00 121.36 ? 2    NAG   E C4   1 
HETATM 22574 C  C5   . NAG   E  5  .   ? 66.119  22.862  -11.456  1.00 121.73 ? 2    NAG   E C5   1 
HETATM 22575 C  C6   . NAG   E  5  .   ? 66.948  21.599  -11.480  1.00 124.67 ? 2    NAG   E C6   1 
HETATM 22576 C  C7   . NAG   E  5  .   ? 65.556  28.064  -10.957  1.00 131.89 ? 2    NAG   E C7   1 
HETATM 22577 C  C8   . NAG   E  5  .   ? 64.572  29.180  -10.776  1.00 131.53 ? 2    NAG   E C8   1 
HETATM 22578 N  N2   . NAG   E  5  .   ? 65.054  26.906  -11.399  1.00 125.42 ? 2    NAG   E N2   1 
HETATM 22579 O  O3   . NAG   E  5  .   ? 65.210  25.516  -13.928  1.00 118.42 ? 2    NAG   E O3   1 
HETATM 22580 O  O4   . NAG   E  5  .   ? 65.342  22.650  -13.724  1.00 122.42 ? 2    NAG   E O4   1 
HETATM 22581 O  O5   . NAG   E  5  .   ? 66.776  23.768  -10.565  1.00 118.86 ? 2    NAG   E O5   1 
HETATM 22582 O  O6   . NAG   E  5  .   ? 66.267  20.542  -12.140  1.00 126.84 ? 2    NAG   E O6   1 
HETATM 22583 O  O7   . NAG   E  5  .   ? 66.751  28.206  -10.718  1.00 136.59 ? 2    NAG   E O7   1 
HETATM 22584 C  C1   . BMA   E  5  .   ? 66.260  22.455  -14.815  1.00 120.20 ? 3    BMA   E C1   1 
HETATM 22585 C  C2   . BMA   E  5  .   ? 65.635  21.406  -15.730  1.00 121.78 ? 3    BMA   E C2   1 
HETATM 22586 C  C3   . BMA   E  5  .   ? 66.517  21.218  -16.951  1.00 126.90 ? 3    BMA   E C3   1 
HETATM 22587 C  C4   . BMA   E  5  .   ? 66.837  22.562  -17.627  1.00 127.60 ? 3    BMA   E C4   1 
HETATM 22588 C  C5   . BMA   E  5  .   ? 67.403  23.568  -16.608  1.00 123.22 ? 3    BMA   E C5   1 
HETATM 22589 C  C6   . BMA   E  5  .   ? 67.598  24.953  -17.207  1.00 121.35 ? 3    BMA   E C6   1 
HETATM 22590 O  O2   . BMA   E  5  .   ? 64.373  21.859  -16.195  1.00 115.73 ? 3    BMA   E O2   1 
HETATM 22591 O  O3   . BMA   E  5  .   ? 65.912  20.337  -17.884  1.00 128.32 ? 3    BMA   E O3   1 
HETATM 22592 O  O4   . BMA   E  5  .   ? 67.784  22.360  -18.666  1.00 130.55 ? 3    BMA   E O4   1 
HETATM 22593 O  O5   . BMA   E  5  .   ? 66.481  23.681  -15.513  1.00 118.67 ? 3    BMA   E O5   1 
HETATM 22594 O  O6   . BMA   E  5  .   ? 68.277  25.772  -16.263  1.00 120.89 ? 3    BMA   E O6   1 
HETATM 22595 C  C1   . NAG   F  5  .   ? -4.951  -14.549 -25.503  1.00 61.37  ? 1    NAG   I C1   1 
HETATM 22596 C  C2   . NAG   F  5  .   ? -4.632  -14.100 -24.080  1.00 66.67  ? 1    NAG   I C2   1 
HETATM 22597 C  C3   . NAG   F  5  .   ? -5.191  -15.103 -23.068  1.00 71.81  ? 1    NAG   I C3   1 
HETATM 22598 C  C4   . NAG   F  5  .   ? -6.645  -15.458 -23.362  1.00 75.80  ? 1    NAG   I C4   1 
HETATM 22599 C  C5   . NAG   F  5  .   ? -6.849  -15.777 -24.840  1.00 73.04  ? 1    NAG   I C5   1 
HETATM 22600 C  C6   . NAG   F  5  .   ? -8.300  -15.954 -25.221  1.00 76.27  ? 1    NAG   I C6   1 
HETATM 22601 C  C7   . NAG   F  5  .   ? -2.518  -12.852 -24.232  1.00 68.69  ? 1    NAG   I C7   1 
HETATM 22602 C  C8   . NAG   F  5  .   ? -1.041  -12.890 -23.973  1.00 66.41  ? 1    NAG   I C8   1 
HETATM 22603 N  N2   . NAG   F  5  .   ? -3.197  -13.954 -23.900  1.00 66.98  ? 1    NAG   I N2   1 
HETATM 22604 O  O3   . NAG   F  5  .   ? -5.083  -14.558 -21.758  1.00 74.35  ? 1    NAG   I O3   1 
HETATM 22605 O  O4   . NAG   F  5  .   ? -6.974  -16.623 -22.612  1.00 85.78  ? 1    NAG   I O4   1 
HETATM 22606 O  O5   . NAG   F  5  .   ? -6.341  -14.708 -25.647  1.00 69.56  ? 1    NAG   I O5   1 
HETATM 22607 O  O6   . NAG   F  5  .   ? -8.459  -16.006 -26.633  1.00 81.92  ? 1    NAG   I O6   1 
HETATM 22608 O  O7   . NAG   F  5  .   ? -3.068  -11.871 -24.719  1.00 72.81  ? 1    NAG   I O7   1 
HETATM 22609 H  H4   . NAG   F  5  .   ? -7.216  -14.703 -23.125  1.00 91.00  ? 1    NAG   I H4   1 
HETATM 22610 H  H5   . NAG   F  5  .   ? -6.362  -16.596 -25.052  1.00 87.68  ? 1    NAG   I H5   1 
HETATM 22611 H  H61  . NAG   F  5  .   ? -8.817  -15.205 -24.869  1.00 91.56  ? 1    NAG   I H61  1 
HETATM 22612 H  H62  . NAG   F  5  .   ? -8.634  -16.784 -24.831  1.00 91.56  ? 1    NAG   I H62  1 
HETATM 22613 H  H81  . NAG   F  5  .   ? -0.648  -12.027 -24.203  1.00 79.73  ? 1    NAG   I H81  1 
HETATM 22614 H  H82  . NAG   F  5  .   ? -0.633  -13.589 -24.520  1.00 79.73  ? 1    NAG   I H82  1 
HETATM 22615 H  H83  . NAG   F  5  .   ? -0.881  -13.080 -23.029  1.00 79.73  ? 1    NAG   I H83  1 
HETATM 22616 H  HN2  . NAG   F  5  .   ? -2.735  -14.654 -23.540  1.00 80.41  ? 1    NAG   I HN2  1 
HETATM 22617 H  HO6  . NAG   F  5  .   ? -7.793  -15.566 -27.022  1.00 98.34  ? 1    NAG   I HO6  1 
HETATM 22618 C  C1   . NAG   F  5  .   ? -8.160  -16.471 -21.804  1.00 95.93  ? 2    NAG   I C1   1 
HETATM 22619 C  C2   . NAG   F  5  .   ? -8.502  -17.848 -21.255  1.00 103.11 ? 2    NAG   I C2   1 
HETATM 22620 C  C3   . NAG   F  5  .   ? -9.370  -17.702 -20.022  1.00 103.17 ? 2    NAG   I C3   1 
HETATM 22621 C  C4   . NAG   F  5  .   ? -8.530  -17.133 -18.890  1.00 103.90 ? 2    NAG   I C4   1 
HETATM 22622 C  C5   . NAG   F  5  .   ? -7.588  -16.040 -19.404  1.00 103.48 ? 2    NAG   I C5   1 
HETATM 22623 C  C6   . NAG   F  5  .   ? -6.154  -16.506 -19.543  1.00 105.83 ? 2    NAG   I C6   1 
HETATM 22624 C  C7   . NAG   F  5  .   ? -8.539  -19.633 -22.941  1.00 112.08 ? 2    NAG   I C7   1 
HETATM 22625 C  C8   . NAG   F  5  .   ? -7.090  -19.839 -22.613  1.00 110.02 ? 2    NAG   I C8   1 
HETATM 22626 N  N2   . NAG   F  5  .   ? -9.164  -18.664 -22.261  1.00 108.66 ? 2    NAG   I N2   1 
HETATM 22627 O  O3   . NAG   F  5  .   ? -9.887  -18.977 -19.656  1.00 104.43 ? 2    NAG   I O3   1 
HETATM 22628 O  O4   . NAG   F  5  .   ? -9.362  -16.607 -17.861  1.00 109.11 ? 2    NAG   I O4   1 
HETATM 22629 O  O5   . NAG   F  5  .   ? -7.990  -15.525 -20.687  1.00 100.15 ? 2    NAG   I O5   1 
HETATM 22630 O  O6   . NAG   F  5  .   ? -5.258  -15.618 -18.888  1.00 106.96 ? 2    NAG   I O6   1 
HETATM 22631 O  O7   . NAG   F  5  .   ? -9.118  -20.311 -23.784  1.00 114.57 ? 2    NAG   I O7   1 
HETATM 22632 H  H4   . NAG   F  5  .   ? -7.991  -17.856 -18.516  1.00 124.72 ? 2    NAG   I H4   1 
HETATM 22633 H  H5   . NAG   F  5  .   ? -7.634  -15.297 -18.772  1.00 124.21 ? 2    NAG   I H5   1 
HETATM 22634 H  H61  . NAG   F  5  .   ? -5.923  -16.551 -20.490  1.00 127.03 ? 2    NAG   I H61  1 
HETATM 22635 H  H62  . NAG   F  5  .   ? -6.067  -17.395 -19.150  1.00 127.03 ? 2    NAG   I H62  1 
HETATM 22636 H  H81  . NAG   F  5  .   ? -6.731  -20.560 -23.164  1.00 132.06 ? 2    NAG   I H81  1 
HETATM 22637 H  H82  . NAG   F  5  .   ? -7.000  -20.075 -21.670  1.00 132.06 ? 2    NAG   I H82  1 
HETATM 22638 H  H83  . NAG   F  5  .   ? -6.596  -19.017 -22.792  1.00 132.06 ? 2    NAG   I H83  1 
HETATM 22639 H  HN2  . NAG   F  5  .   ? -10.045 -18.509 -22.436  1.00 130.43 ? 2    NAG   I HN2  1 
HETATM 22640 H  HO6  . NAG   F  5  .   ? -4.868  -15.096 -19.491  1.00 128.39 ? 2    NAG   I HO6  1 
HETATM 22641 C  C1   . BMA   F  5  .   ? -8.949  -17.277 -16.649  1.00 116.19 ? 3    BMA   I C1   1 
HETATM 22642 C  C2   . BMA   F  5  .   ? -9.473  -16.514 -15.422  1.00 120.02 ? 3    BMA   I C2   1 
HETATM 22643 C  C3   . BMA   F  5  .   ? -8.994  -17.248 -14.175  1.00 121.13 ? 3    BMA   I C3   1 
HETATM 22644 C  C4   . BMA   F  5  .   ? -9.366  -18.752 -14.209  1.00 119.22 ? 3    BMA   I C4   1 
HETATM 22645 C  C5   . BMA   F  5  .   ? -8.966  -19.408 -15.557  1.00 118.51 ? 3    BMA   I C5   1 
HETATM 22646 C  C6   . BMA   F  5  .   ? -9.559  -20.796 -15.747  1.00 117.23 ? 3    BMA   I C6   1 
HETATM 22647 O  O2   . BMA   F  5  .   ? -10.890 -16.530 -15.385  1.00 121.53 ? 3    BMA   I O2   1 
HETATM 22648 O  O3   . BMA   F  5  .   ? -9.496  -16.648 -12.986  1.00 124.13 ? 3    BMA   I O3   1 
HETATM 22649 O  O4   . BMA   F  5  .   ? -8.699  -19.414 -13.142  1.00 117.43 ? 3    BMA   I O4   1 
HETATM 22650 O  O5   . BMA   F  5  .   ? -9.455  -18.602 -16.637  1.00 118.67 ? 3    BMA   I O5   1 
HETATM 22651 O  O6   . BMA   F  5  .   ? -10.911 -20.641 -16.166  1.00 115.68 ? 3    BMA   I O6   1 
HETATM 22652 H  H4   . BMA   F  5  .   ? -10.463 -18.831 -14.141  1.00 143.10 ? 3    BMA   I H4   1 
HETATM 22653 H  H5   . BMA   F  5  .   ? -7.865  -19.469 -15.592  1.00 142.25 ? 3    BMA   I H5   1 
HETATM 22654 H  H61  . BMA   F  5  .   ? -9.489  -21.340 -14.793  1.00 140.71 ? 3    BMA   I H61  1 
HETATM 22655 H  H62  . BMA   F  5  .   ? -8.959  -21.333 -16.498  1.00 140.71 ? 3    BMA   I H62  1 
HETATM 22656 H  HO4  . BMA   F  5  .   ? -8.983  -20.337 -13.187  1.00 140.95 ? 3    BMA   I HO4  1 
HETATM 22657 H  HO6  . BMA   F  5  .   ? -10.986 -19.784 -16.605  1.00 138.85 ? 3    BMA   I HO6  1 
HETATM 22658 C  C1   . NAG   G  6  .   ? 34.960  -35.882 -40.054  1.00 67.65  ? 1    NAG   F C1   1 
HETATM 22659 C  C2   . NAG   G  6  .   ? 35.843  -37.105 -40.302  1.00 73.53  ? 1    NAG   F C2   1 
HETATM 22660 C  C3   . NAG   G  6  .   ? 37.255  -36.849 -39.790  1.00 81.22  ? 1    NAG   F C3   1 
HETATM 22661 C  C4   . NAG   G  6  .   ? 37.821  -35.594 -40.439  1.00 87.27  ? 1    NAG   F C4   1 
HETATM 22662 C  C5   . NAG   G  6  .   ? 36.887  -34.415 -40.174  1.00 81.00  ? 1    NAG   F C5   1 
HETATM 22663 C  C6   . NAG   G  6  .   ? 37.317  -33.150 -40.879  1.00 81.84  ? 1    NAG   F C6   1 
HETATM 22664 C  C7   . NAG   G  6  .   ? 34.509  -39.163 -40.356  1.00 77.03  ? 1    NAG   F C7   1 
HETATM 22665 C  C8   . NAG   G  6  .   ? 34.012  -40.341 -39.573  1.00 79.37  ? 1    NAG   F C8   1 
HETATM 22666 N  N2   . NAG   G  6  .   ? 35.279  -38.297 -39.688  1.00 73.94  ? 1    NAG   F N2   1 
HETATM 22667 O  O3   . NAG   G  6  .   ? 38.084  -37.969 -40.082  1.00 82.49  ? 1    NAG   F O3   1 
HETATM 22668 O  O4   . NAG   G  6  .   ? 39.120  -35.311 -39.931  1.00 99.67  ? 1    NAG   F O4   1 
HETATM 22669 O  O5   . NAG   G  6  .   ? 35.567  -34.719 -40.649  1.00 74.43  ? 1    NAG   F O5   1 
HETATM 22670 O  O6   . NAG   G  6  .   ? 36.932  -33.164 -42.247  1.00 84.87  ? 1    NAG   F O6   1 
HETATM 22671 O  O7   . NAG   G  6  .   ? 34.226  -39.002 -41.539  1.00 79.57  ? 1    NAG   F O7   1 
HETATM 22672 H  H4   . NAG   G  6  .   ? 37.896  -35.732 -41.402  1.00 104.76 ? 1    NAG   F H4   1 
HETATM 22673 H  H5   . NAG   G  6  .   ? 36.851  -34.252 -39.212  1.00 97.23  ? 1    NAG   F H5   1 
HETATM 22674 H  H61  . NAG   G  6  .   ? 38.288  -33.067 -40.822  1.00 98.25  ? 1    NAG   F H61  1 
HETATM 22675 H  H62  . NAG   G  6  .   ? 36.904  -32.383 -40.440  1.00 98.25  ? 1    NAG   F H62  1 
HETATM 22676 H  H81  . NAG   G  6  .   ? 33.472  -40.912 -40.152  1.00 95.28  ? 1    NAG   F H81  1 
HETATM 22677 H  H82  . NAG   G  6  .   ? 33.468  -40.029 -38.826  1.00 95.28  ? 1    NAG   F H82  1 
HETATM 22678 H  H83  . NAG   G  6  .   ? 34.772  -40.849 -39.232  1.00 95.28  ? 1    NAG   F H83  1 
HETATM 22679 H  HN2  . NAG   G  6  .   ? 35.458  -38.461 -38.809  1.00 88.77  ? 1    NAG   F HN2  1 
HETATM 22680 H  HO6  . NAG   G  6  .   ? 36.213  -33.677 -42.350  1.00 101.88 ? 1    NAG   F HO6  1 
HETATM 22681 C  C1   . NAG   G  6  .   ? 40.083  -35.367 -41.011  1.00 106.10 ? 2    NAG   F C1   1 
HETATM 22682 C  C2   . NAG   G  6  .   ? 41.273  -34.462 -40.677  1.00 106.70 ? 2    NAG   F C2   1 
HETATM 22683 C  C3   . NAG   G  6  .   ? 42.325  -34.544 -41.783  1.00 112.82 ? 2    NAG   F C3   1 
HETATM 22684 C  C4   . NAG   G  6  .   ? 42.708  -35.993 -42.058  1.00 117.08 ? 2    NAG   F C4   1 
HETATM 22685 C  C5   . NAG   G  6  .   ? 41.460  -36.836 -42.313  1.00 113.22 ? 2    NAG   F C5   1 
HETATM 22686 C  C6   . NAG   G  6  .   ? 41.761  -38.310 -42.456  1.00 113.92 ? 2    NAG   F C6   1 
HETATM 22687 C  C7   . NAG   G  6  .   ? 40.579  -32.558 -39.284  1.00 99.45  ? 2    NAG   F C7   1 
HETATM 22688 C  C8   . NAG   G  6  .   ? 40.755  -33.472 -38.108  1.00 99.31  ? 2    NAG   F C8   1 
HETATM 22689 N  N2   . NAG   G  6  .   ? 40.841  -33.086 -40.484  1.00 101.80 ? 2    NAG   F N2   1 
HETATM 22690 O  O3   . NAG   G  6  .   ? 43.478  -33.804 -41.395  1.00 113.70 ? 2    NAG   F O3   1 
HETATM 22691 O  O4   . NAG   G  6  .   ? 43.560  -36.063 -43.198  1.00 126.45 ? 2    NAG   F O4   1 
HETATM 22692 O  O5   . NAG   G  6  .   ? 40.546  -36.708 -41.214  1.00 110.45 ? 2    NAG   F O5   1 
HETATM 22693 O  O6   . NAG   G  6  .   ? 41.497  -39.011 -41.249  1.00 115.01 ? 2    NAG   F O6   1 
HETATM 22694 O  O7   . NAG   G  6  .   ? 40.217  -31.393 -39.152  1.00 99.07  ? 2    NAG   F O7   1 
HETATM 22695 H  H4   . NAG   G  6  .   ? 43.179  -36.350 -41.281  1.00 140.53 ? 2    NAG   F H4   1 
HETATM 22696 H  H5   . NAG   G  6  .   ? 41.025  -36.515 -43.126  1.00 135.91 ? 2    NAG   F H5   1 
HETATM 22697 H  H61  . NAG   G  6  .   ? 42.702  -38.422 -42.691  1.00 136.74 ? 2    NAG   F H61  1 
HETATM 22698 H  H62  . NAG   G  6  .   ? 41.207  -38.681 -43.168  1.00 136.74 ? 2    NAG   F H62  1 
HETATM 22699 H  H81  . NAG   G  6  .   ? 40.544  -32.989 -37.286  1.00 119.21 ? 2    NAG   F H81  1 
HETATM 22700 H  H82  . NAG   G  6  .   ? 41.679  -33.784 -38.074  1.00 119.21 ? 2    NAG   F H82  1 
HETATM 22701 H  H83  . NAG   G  6  .   ? 40.157  -34.237 -38.198  1.00 119.21 ? 2    NAG   F H83  1 
HETATM 22702 H  HN2  . NAG   G  6  .   ? 40.745  -32.556 -41.220  1.00 122.19 ? 2    NAG   F HN2  1 
HETATM 22703 H  HO6  . NAG   G  6  .   ? 41.048  -38.484 -40.693  1.00 138.05 ? 2    NAG   F HO6  1 
HETATM 22704 C  C1   . BMA   G  6  .   ? 44.792  -36.733 -42.843  1.00 131.44 ? 3    BMA   F C1   1 
HETATM 22705 C  C2   . BMA   G  6  .   ? 45.398  -37.427 -44.091  1.00 135.15 ? 3    BMA   F C2   1 
HETATM 22706 C  C3   . BMA   G  6  .   ? 46.689  -38.128 -43.674  1.00 140.11 ? 3    BMA   F C3   1 
HETATM 22707 C  C4   . BMA   G  6  .   ? 47.656  -37.168 -42.938  1.00 137.41 ? 3    BMA   F C4   1 
HETATM 22708 C  C5   . BMA   G  6  .   ? 46.927  -36.420 -41.780  1.00 137.08 ? 3    BMA   F C5   1 
HETATM 22709 C  C6   . BMA   G  6  .   ? 47.760  -35.299 -41.129  1.00 140.31 ? 3    BMA   F C6   1 
HETATM 22710 O  O2   . BMA   G  6  .   ? 45.754  -36.480 -45.091  1.00 133.86 ? 3    BMA   F O2   1 
HETATM 22711 O  O3   . BMA   G  6  .   ? 47.345  -38.738 -44.782  1.00 145.12 ? 3    BMA   F O3   1 
HETATM 22712 O  O4   . BMA   G  6  .   ? 48.746  -37.923 -42.424  1.00 134.01 ? 3    BMA   F O4   1 
HETATM 22713 O  O5   . BMA   G  6  .   ? 45.728  -35.813 -42.297  1.00 134.85 ? 3    BMA   F O5   1 
HETATM 22714 O  O6   . BMA   G  6  .   ? 46.919  -34.134 -40.957  1.00 143.67 ? 3    BMA   F O6   1 
HETATM 22715 H  H4   . BMA   G  6  .   ? 47.985  -36.391 -43.647  1.00 164.93 ? 3    BMA   F H4   1 
HETATM 22716 H  H5   . BMA   G  6  .   ? 46.678  -37.163 -41.004  1.00 164.54 ? 3    BMA   F H5   1 
HETATM 22717 H  H61  . BMA   G  6  .   ? 48.619  -35.084 -41.783  1.00 168.41 ? 3    BMA   F H61  1 
HETATM 22718 H  H62  . BMA   G  6  .   ? 48.141  -35.668 -40.164  1.00 168.41 ? 3    BMA   F H62  1 
HETATM 22719 H  HO4  . BMA   G  6  .   ? 49.207  -37.335 -41.810  1.00 160.84 ? 3    BMA   F HO4  1 
HETATM 22720 C  C1   . MAN   G  6  .   ? 47.688  -33.011 -40.450  1.00 145.29 ? 4    MAN   F C1   1 
HETATM 22721 C  C2   . MAN   G  6  .   ? 46.987  -32.462 -39.164  1.00 142.86 ? 4    MAN   F C2   1 
HETATM 22722 C  C3   . MAN   G  6  .   ? 45.694  -31.724 -39.526  1.00 141.49 ? 4    MAN   F C3   1 
HETATM 22723 C  C4   . MAN   G  6  .   ? 45.935  -30.685 -40.621  1.00 140.81 ? 4    MAN   F C4   1 
HETATM 22724 C  C5   . MAN   G  6  .   ? 46.624  -31.294 -41.847  1.00 143.27 ? 4    MAN   F C5   1 
HETATM 22725 C  C6   . MAN   G  6  .   ? 46.993  -30.217 -42.889  1.00 143.00 ? 4    MAN   F C6   1 
HETATM 22726 O  O2   . MAN   G  6  .   ? 47.809  -31.500 -38.491  1.00 140.44 ? 4    MAN   F O2   1 
HETATM 22727 O  O3   . MAN   G  6  .   ? 45.120  -31.041 -38.409  1.00 139.92 ? 4    MAN   F O3   1 
HETATM 22728 O  O4   . MAN   G  6  .   ? 44.688  -30.130 -41.017  1.00 137.55 ? 4    MAN   F O4   1 
HETATM 22729 O  O5   . MAN   G  6  .   ? 47.840  -31.982 -41.440  1.00 146.13 ? 4    MAN   F O5   1 
HETATM 22730 O  O6   . MAN   G  6  .   ? 46.995  -28.919 -42.247  1.00 144.15 ? 4    MAN   F O6   1 
HETATM 22731 H  H3   . MAN   G  6  .   ? 44.979  -32.479 -39.870  1.00 169.82 ? 4    MAN   F H3   1 
HETATM 22732 H  H4   . MAN   G  6  .   ? 46.629  -29.932 -40.212  1.00 169.01 ? 4    MAN   F H4   1 
HETATM 22733 H  H5   . MAN   G  6  .   ? 45.957  -32.030 -42.315  1.00 171.96 ? 4    MAN   F H5   1 
HETATM 22734 H  H61  . MAN   G  6  .   ? 46.255  -30.260 -43.705  1.00 171.64 ? 4    MAN   F H61  1 
HETATM 22735 H  H62  . MAN   G  6  .   ? 47.983  -30.462 -43.302  1.00 171.64 ? 4    MAN   F H62  1 
HETATM 22736 H  HO4  . MAN   G  6  .   ? 44.537  -30.451 -41.921  1.00 165.10 ? 4    MAN   F HO4  1 
HETATM 22737 C  C1   . MAN   G  6  .   ? 43.995  -31.746 -37.858  1.00 135.69 ? 5    MAN   F C1   1 
HETATM 22738 C  C2   . MAN   G  6  .   ? 43.156  -30.733 -37.068  1.00 136.16 ? 5    MAN   F C2   1 
HETATM 22739 C  C3   . MAN   G  6  .   ? 44.028  -30.121 -35.976  1.00 138.84 ? 5    MAN   F C3   1 
HETATM 22740 C  C4   . MAN   G  6  .   ? 44.739  -31.213 -35.137  1.00 135.15 ? 5    MAN   F C4   1 
HETATM 22741 C  C5   . MAN   G  6  .   ? 45.409  -32.276 -36.048  1.00 135.52 ? 5    MAN   F C5   1 
HETATM 22742 C  C6   . MAN   G  6  .   ? 45.898  -33.500 -35.297  1.00 136.05 ? 5    MAN   F C6   1 
HETATM 22743 O  O2   . MAN   G  6  .   ? 42.076  -31.364 -36.375  1.00 132.83 ? 5    MAN   F O2   1 
HETATM 22744 O  O3   . MAN   G  6  .   ? 43.281  -29.255 -35.119  1.00 143.03 ? 5    MAN   F O3   1 
HETATM 22745 O  O4   . MAN   G  6  .   ? 45.726  -30.594 -34.324  1.00 132.63 ? 5    MAN   F O4   1 
HETATM 22746 O  O5   . MAN   G  6  .   ? 44.459  -32.744 -37.024  1.00 134.26 ? 5    MAN   F O5   1 
HETATM 22747 O  O6   . MAN   G  6  .   ? 44.793  -34.064 -34.597  1.00 137.98 ? 5    MAN   F O6   1 
HETATM 22748 H  H3   . MAN   G  6  .   ? 44.798  -29.507 -36.455  1.00 166.65 ? 5    MAN   F H3   1 
HETATM 22749 H  H4   . MAN   G  6  .   ? 43.975  -31.743 -34.544  1.00 162.22 ? 5    MAN   F H4   1 
HETATM 22750 H  H5   . MAN   G  6  .   ? 46.264  -31.799 -36.546  1.00 162.66 ? 5    MAN   F H5   1 
HETATM 22751 H  H61  . MAN   G  6  .   ? 46.698  -33.191 -34.606  1.00 163.30 ? 5    MAN   F H61  1 
HETATM 22752 H  H62  . MAN   G  6  .   ? 46.321  -34.210 -36.024  1.00 163.30 ? 5    MAN   F H62  1 
HETATM 22753 H  HO3  . MAN   G  6  .   ? 42.465  -29.736 -34.903  1.00 171.67 ? 5    MAN   F HO3  1 
HETATM 22754 H  HO4  . MAN   G  6  .   ? 46.288  -31.313 -34.004  1.00 159.19 ? 5    MAN   F HO4  1 
HETATM 22755 H  HO6  . MAN   G  6  .   ? 43.994  -33.863 -35.100  1.00 165.62 ? 5    MAN   F HO6  1 
HETATM 22756 C  C1   . MAN   G  6  .   ? 46.394  -27.921 -43.110  1.00 147.46 ? 6    MAN   F C1   1 
HETATM 22757 C  C2   . MAN   G  6  .   ? 47.166  -26.566 -42.933  1.00 147.65 ? 6    MAN   F C2   1 
HETATM 22758 C  C3   . MAN   G  6  .   ? 46.781  -25.884 -41.615  1.00 145.94 ? 6    MAN   F C3   1 
HETATM 22759 C  C4   . MAN   G  6  .   ? 45.255  -25.787 -41.464  1.00 146.08 ? 6    MAN   F C4   1 
HETATM 22760 C  C5   . MAN   G  6  .   ? 44.643  -27.191 -41.566  1.00 151.56 ? 6    MAN   F C5   1 
HETATM 22761 C  C6   . MAN   G  6  .   ? 43.120  -27.195 -41.474  1.00 155.38 ? 6    MAN   F C6   1 
HETATM 22762 O  O2   . MAN   G  6  .   ? 46.836  -25.630 -43.965  1.00 149.79 ? 6    MAN   F O2   1 
HETATM 22763 O  O3   . MAN   G  6  .   ? 47.374  -24.590 -41.487  1.00 145.26 ? 6    MAN   F O3   1 
HETATM 22764 O  O4   . MAN   G  6  .   ? 44.935  -25.224 -40.198  1.00 142.69 ? 6    MAN   F O4   1 
HETATM 22765 O  O5   . MAN   G  6  .   ? 44.998  -27.776 -42.843  1.00 149.92 ? 6    MAN   F O5   1 
HETATM 22766 O  O6   . MAN   G  6  .   ? 42.746  -27.831 -40.254  1.00 156.52 ? 6    MAN   F O6   1 
HETATM 22767 H  H3   . MAN   G  6  .   ? 47.168  -26.486 -40.787  1.00 175.17 ? 6    MAN   F H3   1 
HETATM 22768 H  H4   . MAN   G  6  .   ? 44.854  -25.174 -42.289  1.00 175.33 ? 6    MAN   F H4   1 
HETATM 22769 H  H5   . MAN   G  6  .   ? 45.046  -27.803 -40.748  1.00 181.91 ? 6    MAN   F H5   1 
HETATM 22770 H  H61  . MAN   G  6  .   ? 42.719  -27.732 -42.348  1.00 186.49 ? 6    MAN   F H61  1 
HETATM 22771 H  H62  . MAN   G  6  .   ? 42.765  -26.154 -41.511  1.00 186.49 ? 6    MAN   F H62  1 
HETATM 22772 H  HO3  . MAN   G  6  .   ? 47.334  -24.193 -42.372  1.00 174.34 ? 6    MAN   F HO3  1 
HETATM 22773 H  HO4  . MAN   G  6  .   ? 44.021  -24.907 -40.277  1.00 171.27 ? 6    MAN   F HO4  1 
HETATM 22774 H  HO6  . MAN   G  6  .   ? 43.107  -28.727 -40.267  1.00 187.86 ? 6    MAN   F HO6  1 
HETATM 22775 C  C1   . NAG   H  7  .   ? 31.730  -37.531 -25.632  1.00 41.24  ? 1    NAG   G C1   1 
HETATM 22776 C  C2   . NAG   H  7  .   ? 32.551  -38.605 -26.336  1.00 48.38  ? 1    NAG   G C2   1 
HETATM 22777 C  C3   . NAG   H  7  .   ? 31.636  -39.507 -27.158  1.00 47.68  ? 1    NAG   G C3   1 
HETATM 22778 C  C4   . NAG   H  7  .   ? 30.515  -40.067 -26.292  1.00 47.25  ? 1    NAG   G C4   1 
HETATM 22779 C  C5   . NAG   H  7  .   ? 29.796  -38.941 -25.552  1.00 48.47  ? 1    NAG   G C5   1 
HETATM 22780 C  C6   . NAG   H  7  .   ? 28.785  -39.442 -24.547  1.00 52.26  ? 1    NAG   G C6   1 
HETATM 22781 C  C7   . NAG   H  7  .   ? 34.786  -37.667 -26.725  1.00 62.92  ? 1    NAG   G C7   1 
HETATM 22782 C  C8   . NAG   H  7  .   ? 35.721  -37.072 -27.734  1.00 68.44  ? 1    NAG   G C8   1 
HETATM 22783 N  N2   . NAG   H  7  .   ? 33.577  -38.013 -27.179  1.00 56.21  ? 1    NAG   G N2   1 
HETATM 22784 O  O3   . NAG   H  7  .   ? 32.396  -40.568 -27.727  1.00 50.23  ? 1    NAG   G O3   1 
HETATM 22785 O  O4   . NAG   H  7  .   ? 29.567  -40.732 -27.122  1.00 51.11  ? 1    NAG   G O4   1 
HETATM 22786 O  O5   . NAG   H  7  .   ? 30.738  -38.147 -24.819  1.00 46.09  ? 1    NAG   G O5   1 
HETATM 22787 O  O6   . NAG   H  7  .   ? 29.327  -40.474 -23.735  1.00 58.42  ? 1    NAG   G O6   1 
HETATM 22788 O  O7   . NAG   H  7  .   ? 35.108  -37.825 -25.552  1.00 63.78  ? 1    NAG   G O7   1 
HETATM 22789 H  H4   . NAG   H  7  .   ? 30.894  -40.689 -25.642  1.00 56.73  ? 1    NAG   G H4   1 
HETATM 22790 H  H5   . NAG   H  7  .   ? 29.347  -38.375 -26.209  1.00 58.20  ? 1    NAG   G H5   1 
HETATM 22791 H  H61  . NAG   H  7  .   ? 28.006  -39.787 -25.023  1.00 62.75  ? 1    NAG   G H61  1 
HETATM 22792 H  H62  . NAG   H  7  .   ? 28.508  -38.700 -23.976  1.00 62.75  ? 1    NAG   G H62  1 
HETATM 22793 H  H81  . NAG   H  7  .   ? 36.596  -36.934 -27.324  1.00 82.16  ? 1    NAG   G H81  1 
HETATM 22794 H  H82  . NAG   H  7  .   ? 35.367  -36.216 -28.041  1.00 82.16  ? 1    NAG   G H82  1 
HETATM 22795 H  H83  . NAG   H  7  .   ? 35.810  -37.679 -28.493  1.00 82.16  ? 1    NAG   G H83  1 
HETATM 22796 H  HN2  . NAG   H  7  .   ? 33.387  -37.871 -28.060  1.00 67.49  ? 1    NAG   G HN2  1 
HETATM 22797 H  HO6  . NAG   H  7  .   ? 28.812  -40.593 -23.021  1.00 70.14  ? 1    NAG   G HO6  1 
HETATM 22798 C  C1   . NAG   H  7  .   ? 29.476  -42.141 -26.845  1.00 54.06  ? 2    NAG   G C1   1 
HETATM 22799 C  C2   . NAG   H  7  .   ? 28.203  -42.627 -27.532  1.00 58.18  ? 2    NAG   G C2   1 
HETATM 22800 C  C3   . NAG   H  7  .   ? 28.043  -44.132 -27.349  1.00 60.20  ? 2    NAG   G C3   1 
HETATM 22801 C  C4   . NAG   H  7  .   ? 29.294  -44.861 -27.818  1.00 61.68  ? 2    NAG   G C4   1 
HETATM 22802 C  C5   . NAG   H  7  .   ? 30.530  -44.284 -27.133  1.00 58.15  ? 2    NAG   G C5   1 
HETATM 22803 C  C6   . NAG   H  7  .   ? 31.820  -44.859 -27.672  1.00 56.30  ? 2    NAG   G C6   1 
HETATM 22804 C  C7   . NAG   H  7  .   ? 26.424  -40.947 -27.699  1.00 61.77  ? 2    NAG   G C7   1 
HETATM 22805 C  C8   . NAG   H  7  .   ? 25.238  -40.327 -27.026  1.00 60.55  ? 2    NAG   G C8   1 
HETATM 22806 N  N2   . NAG   H  7  .   ? 27.038  -41.923 -27.022  1.00 59.96  ? 2    NAG   G N2   1 
HETATM 22807 O  O3   . NAG   H  7  .   ? 26.918  -44.581 -28.095  1.00 57.61  ? 2    NAG   G O3   1 
HETATM 22808 O  O4   . NAG   H  7  .   ? 29.180  -46.246 -27.510  1.00 68.40  ? 2    NAG   G O4   1 
HETATM 22809 O  O5   . NAG   H  7  .   ? 30.597  -42.866 -27.348  1.00 57.93  ? 2    NAG   G O5   1 
HETATM 22810 O  O6   . NAG   H  7  .   ? 32.004  -44.515 -29.039  1.00 56.68  ? 2    NAG   G O6   1 
HETATM 22811 O  O7   . NAG   H  7  .   ? 26.809  -40.581 -28.805  1.00 62.99  ? 2    NAG   G O7   1 
HETATM 22812 H  H4   . NAG   H  7  .   ? 29.393  -44.752 -28.783  1.00 74.05  ? 2    NAG   G H4   1 
HETATM 22813 H  H5   . NAG   H  7  .   ? 30.470  -44.458 -26.175  1.00 69.81  ? 2    NAG   G H5   1 
HETATM 22814 H  H61  . NAG   H  7  .   ? 31.798  -45.831 -27.587  1.00 67.59  ? 2    NAG   G H61  1 
HETATM 22815 H  H62  . NAG   H  7  .   ? 32.568  -44.509 -27.151  1.00 67.59  ? 2    NAG   G H62  1 
HETATM 22816 H  H81  . NAG   H  7  .   ? 24.848  -39.650 -27.612  1.00 72.70  ? 2    NAG   G H81  1 
HETATM 22817 H  H82  . NAG   H  7  .   ? 25.520  -39.910 -26.190  1.00 72.70  ? 2    NAG   G H82  1 
HETATM 22818 H  H83  . NAG   H  7  .   ? 24.573  -41.017 -26.838  1.00 72.70  ? 2    NAG   G H83  1 
HETATM 22819 H  HN2  . NAG   H  7  .   ? 26.711  -42.157 -26.204  1.00 71.99  ? 2    NAG   G HN2  1 
HETATM 22820 H  HO6  . NAG   H  7  .   ? 32.694  -44.966 -29.370  1.00 68.06  ? 2    NAG   G HO6  1 
HETATM 22821 C  C1   . BMA   H  7  .   ? 29.424  -47.020 -28.702  1.00 77.13  ? 3    BMA   G C1   1 
HETATM 22822 C  C2   . BMA   H  7  .   ? 30.221  -48.278 -28.287  1.00 82.84  ? 3    BMA   G C2   1 
HETATM 22823 C  C3   . BMA   H  7  .   ? 30.412  -49.191 -29.494  1.00 85.03  ? 3    BMA   G C3   1 
HETATM 22824 C  C4   . BMA   H  7  .   ? 29.084  -49.459 -30.182  1.00 81.20  ? 3    BMA   G C4   1 
HETATM 22825 C  C5   . BMA   H  7  .   ? 28.419  -48.139 -30.573  1.00 81.12  ? 3    BMA   G C5   1 
HETATM 22826 C  C6   . BMA   H  7  .   ? 27.090  -48.362 -31.275  1.00 87.03  ? 3    BMA   G C6   1 
HETATM 22827 O  O2   . BMA   H  7  .   ? 29.501  -49.025 -27.318  1.00 83.14  ? 3    BMA   G O2   1 
HETATM 22828 O  O3   . BMA   H  7  .   ? 30.976  -50.429 -29.128  1.00 90.69  ? 3    BMA   G O3   1 
HETATM 22829 O  O4   . BMA   H  7  .   ? 29.296  -50.248 -31.340  1.00 82.41  ? 3    BMA   G O4   1 
HETATM 22830 O  O5   . BMA   H  7  .   ? 28.205  -47.377 -29.368  1.00 79.14  ? 3    BMA   G O5   1 
HETATM 22831 O  O6   . BMA   H  7  .   ? 26.575  -49.609 -30.834  1.00 95.17  ? 3    BMA   G O6   1 
HETATM 22832 H  H4   . BMA   H  7  .   ? 28.418  -49.965 -29.463  1.00 97.48  ? 3    BMA   G H4   1 
HETATM 22833 H  H5   . BMA   H  7  .   ? 29.070  -47.559 -31.248  1.00 97.38  ? 3    BMA   G H5   1 
HETATM 22834 H  H61  . BMA   H  7  .   ? 27.261  -48.351 -32.362  1.00 104.47 ? 3    BMA   G H61  1 
HETATM 22835 H  H62  . BMA   H  7  .   ? 26.415  -47.529 -31.021  1.00 104.47 ? 3    BMA   G H62  1 
HETATM 22836 H  HO4  . BMA   H  7  .   ? 30.161  -50.670 -31.204  1.00 98.93  ? 3    BMA   G HO4  1 
HETATM 22837 C  C1   . MAN   H  7  .   ? 32.395  -50.408 -29.369  1.00 95.02  ? 4    MAN   G C1   1 
HETATM 22838 C  C2   . MAN   H  7  .   ? 32.805  -51.865 -29.594  1.00 97.09  ? 4    MAN   G C2   1 
HETATM 22839 C  C3   . MAN   H  7  .   ? 32.499  -52.657 -28.326  1.00 97.13  ? 4    MAN   G C3   1 
HETATM 22840 C  C4   . MAN   H  7  .   ? 33.138  -51.988 -27.093  1.00 96.20  ? 4    MAN   G C4   1 
HETATM 22841 C  C5   . MAN   H  7  .   ? 32.709  -50.509 -27.013  1.00 96.46  ? 4    MAN   G C5   1 
HETATM 22842 C  C6   . MAN   H  7  .   ? 33.393  -49.743 -25.897  1.00 99.40  ? 4    MAN   G C6   1 
HETATM 22843 O  O2   . MAN   H  7  .   ? 34.213  -51.983 -29.800  1.00 103.74 ? 4    MAN   G O2   1 
HETATM 22844 O  O3   . MAN   H  7  .   ? 32.915  -54.016 -28.425  1.00 96.72  ? 4    MAN   G O3   1 
HETATM 22845 O  O4   . MAN   H  7  .   ? 32.729  -52.674 -25.919  1.00 96.35  ? 4    MAN   G O4   1 
HETATM 22846 O  O5   . MAN   H  7  .   ? 33.044  -49.863 -28.255  1.00 95.67  ? 4    MAN   G O5   1 
HETATM 22847 O  O6   . MAN   H  7  .   ? 33.094  -50.403 -24.671  1.00 101.41 ? 4    MAN   G O6   1 
HETATM 22848 H  H3   . MAN   H  7  .   ? 31.413  -52.681 -28.181  1.00 116.60 ? 4    MAN   G H3   1 
HETATM 22849 H  H4   . MAN   H  7  .   ? 34.235  -52.008 -27.210  1.00 115.48 ? 4    MAN   G H4   1 
HETATM 22850 H  H5   . MAN   H  7  .   ? 31.625  -50.464 -26.843  1.00 115.79 ? 4    MAN   G H5   1 
HETATM 22851 H  H61  . MAN   H  7  .   ? 33.020  -48.707 -25.902  1.00 119.32 ? 4    MAN   G H61  1 
HETATM 22852 H  H62  . MAN   H  7  .   ? 34.476  -49.725 -26.095  1.00 119.32 ? 4    MAN   G H62  1 
HETATM 22853 H  HO3  . MAN   H  7  .   ? 33.653  -54.018 -29.055  1.00 116.10 ? 4    MAN   G HO3  1 
HETATM 22854 H  HO4  . MAN   H  7  .   ? 32.811  -52.031 -25.200  1.00 115.66 ? 4    MAN   G HO4  1 
HETATM 22855 H  HO6  . MAN   H  7  .   ? 33.698  -50.061 -24.001  1.00 121.72 ? 4    MAN   G HO6  1 
HETATM 22856 C  C1   . MAN   H  7  .   ? 25.773  -50.219 -31.864  1.00 99.59  ? 5    MAN   G C1   1 
HETATM 22857 C  C2   . MAN   H  7  .   ? 24.484  -49.399 -31.981  1.00 102.47 ? 5    MAN   G C2   1 
HETATM 22858 C  C3   . MAN   H  7  .   ? 23.705  -49.515 -30.676  1.00 104.01 ? 5    MAN   G C3   1 
HETATM 22859 C  C4   . MAN   H  7  .   ? 23.497  -50.995 -30.286  1.00 100.11 ? 5    MAN   G C4   1 
HETATM 22860 C  C5   . MAN   H  7  .   ? 24.858  -51.720 -30.241  1.00 99.93  ? 5    MAN   G C5   1 
HETATM 22861 C  C6   . MAN   H  7  .   ? 24.754  -53.216 -29.951  1.00 100.54 ? 5    MAN   G C6   1 
HETATM 22862 O  O2   . MAN   H  7  .   ? 23.622  -49.917 -32.998  1.00 100.82 ? 5    MAN   G O2   1 
HETATM 22863 O  O3   . MAN   H  7  .   ? 22.454  -48.838 -30.746  1.00 109.16 ? 5    MAN   G O3   1 
HETATM 22864 O  O4   . MAN   H  7  .   ? 22.866  -51.071 -29.015  1.00 98.22  ? 5    MAN   G O4   1 
HETATM 22865 O  O5   . MAN   H  7  .   ? 25.504  -51.558 -31.521  1.00 99.34  ? 5    MAN   G O5   1 
HETATM 22866 O  O6   . MAN   H  7  .   ? 24.605  -53.381 -28.541  1.00 101.22 ? 5    MAN   G O6   1 
HETATM 22867 H  H3   . MAN   H  7  .   ? 24.276  -49.032 -29.876  1.00 124.85 ? 5    MAN   G H3   1 
HETATM 22868 H  H4   . MAN   H  7  .   ? 22.884  -51.482 -31.064  1.00 120.17 ? 5    MAN   G H4   1 
HETATM 22869 H  H5   . MAN   H  7  .   ? 25.472  -51.273 -29.448  1.00 119.95 ? 5    MAN   G H5   1 
HETATM 22870 H  H61  . MAN   H  7  .   ? 25.666  -53.710 -30.322  1.00 120.68 ? 5    MAN   G H61  1 
HETATM 22871 H  H62  . MAN   H  7  .   ? 23.890  -53.621 -30.500  1.00 120.68 ? 5    MAN   G H62  1 
HETATM 22872 H  HO3  . MAN   H  7  .   ? 21.924  -49.200 -30.017  1.00 131.03 ? 5    MAN   G HO3  1 
HETATM 22873 H  HO4  . MAN   H  7  .   ? 23.393  -51.701 -28.502  1.00 117.90 ? 5    MAN   G HO4  1 
HETATM 22874 H  HO6  . MAN   H  7  .   ? 24.659  -54.327 -28.348  1.00 121.50 ? 5    MAN   G HO6  1 
HETATM 22875 CA CA   . CA    I  8  .   ? 35.481  -27.063 -37.754  1.00 55.31  ? 2001 CA    A CA   1 
HETATM 22876 CA CA   . CA    J  8  .   ? 37.080  -5.452  -25.142  1.00 63.62  ? 2002 CA    A CA   1 
HETATM 22877 CA CA   . CA    K  8  .   ? 26.820  1.298   -31.072  1.00 70.66  ? 2003 CA    A CA   1 
HETATM 22878 CA CA   . CA    L  8  .   ? 40.514  -17.596 -27.927  1.00 61.78  ? 2004 CA    A CA   1 
HETATM 22879 C  C1   . GOL   M  9  .   ? 12.596  -34.849 -42.196  1.00 68.20  ? 2005 GOL   A C1   1 
HETATM 22880 O  O1   . GOL   M  9  .   ? 12.023  -33.581 -42.243  1.00 70.02  ? 2005 GOL   A O1   1 
HETATM 22881 C  C2   . GOL   M  9  .   ? 14.124  -34.644 -42.073  1.00 64.88  ? 2005 GOL   A C2   1 
HETATM 22882 O  O2   . GOL   M  9  .   ? 14.476  -34.089 -40.853  1.00 60.10  ? 2005 GOL   A O2   1 
HETATM 22883 C  C3   . GOL   M  9  .   ? 14.722  -36.051 -42.270  1.00 67.61  ? 2005 GOL   A C3   1 
HETATM 22884 O  O3   . GOL   M  9  .   ? 15.706  -35.938 -43.250  1.00 72.11  ? 2005 GOL   A O3   1 
HETATM 22885 H  H31  . GOL   M  9  .   ? 14.010  -36.665 -42.509  1.00 81.17  ? 2005 GOL   A H31  1 
HETATM 22886 H  H32  . GOL   M  9  .   ? 15.061  -36.371 -41.419  1.00 81.17  ? 2005 GOL   A H32  1 
HETATM 22887 H  HO3  . GOL   M  9  .   ? 16.435  -35.770 -42.846  1.00 86.57  ? 2005 GOL   A HO3  1 
HETATM 22888 C  C1   . GOL   N  9  .   ? 9.652   -24.033 -25.702  1.00 66.61  ? 2006 GOL   A C1   1 
HETATM 22889 O  O1   . GOL   N  9  .   ? 8.534   -24.271 -24.911  1.00 67.79  ? 2006 GOL   A O1   1 
HETATM 22890 C  C2   . GOL   N  9  .   ? 10.456  -22.908 -25.025  1.00 67.68  ? 2006 GOL   A C2   1 
HETATM 22891 O  O2   . GOL   N  9  .   ? 10.292  -22.920 -23.649  1.00 66.91  ? 2006 GOL   A O2   1 
HETATM 22892 C  C3   . GOL   N  9  .   ? 11.912  -23.194 -25.429  1.00 76.26  ? 2006 GOL   A C3   1 
HETATM 22893 O  O3   . GOL   N  9  .   ? 12.561  -21.969 -25.533  1.00 79.62  ? 2006 GOL   A O3   1 
HETATM 22894 H  H31  . GOL   N  9  .   ? 11.912  -23.699 -26.258  1.00 91.55  ? 2006 GOL   A H31  1 
HETATM 22895 H  H32  . GOL   N  9  .   ? 12.309  -23.783 -24.770  1.00 91.55  ? 2006 GOL   A H32  1 
HETATM 22896 H  HO3  . GOL   N  9  .   ? 13.376  -22.143 -25.698  1.00 95.58  ? 2006 GOL   A HO3  1 
HETATM 22897 C  C1   . GOL   O  9  .   ? 25.369  -42.653 -31.593  1.00 101.11 ? 2007 GOL   A C1   1 
HETATM 22898 O  O1   . GOL   O  9  .   ? 26.244  -41.581 -31.742  1.00 103.00 ? 2007 GOL   A O1   1 
HETATM 22899 C  C2   . GOL   O  9  .   ? 26.098  -43.907 -32.130  1.00 99.75  ? 2007 GOL   A C2   1 
HETATM 22900 O  O2   . GOL   O  9  .   ? 27.216  -44.224 -31.371  1.00 99.78  ? 2007 GOL   A O2   1 
HETATM 22901 C  C3   . GOL   O  9  .   ? 25.033  -45.021 -32.099  1.00 98.95  ? 2007 GOL   A C3   1 
HETATM 22902 O  O3   . GOL   O  9  .   ? 24.766  -45.361 -33.424  1.00 99.96  ? 2007 GOL   A O3   1 
HETATM 22903 H  H31  . GOL   O  9  .   ? 24.254  -44.697 -31.620  1.00 118.78 ? 2007 GOL   A H31  1 
HETATM 22904 H  H32  . GOL   O  9  .   ? 25.369  -45.762 -31.572  1.00 118.78 ? 2007 GOL   A H32  1 
HETATM 22905 H  HO3  . GOL   O  9  .   ? 24.144  -45.940 -33.406  1.00 119.99 ? 2007 GOL   A HO3  1 
HETATM 22906 C  C1   . GOL   P  9  .   ? 12.854  -17.127 -7.674   1.00 85.18  ? 2008 GOL   A C1   1 
HETATM 22907 O  O1   . GOL   P  9  .   ? 12.006  -17.553 -6.654   1.00 84.94  ? 2008 GOL   A O1   1 
HETATM 22908 C  C2   . GOL   P  9  .   ? 14.302  -17.331 -7.172   1.00 85.08  ? 2008 GOL   A C2   1 
HETATM 22909 O  O2   . GOL   P  9  .   ? 14.872  -16.141 -6.738   1.00 85.37  ? 2008 GOL   A O2   1 
HETATM 22910 C  C3   . GOL   P  9  .   ? 15.057  -17.938 -8.376   1.00 85.43  ? 2008 GOL   A C3   1 
HETATM 22911 O  O3   . GOL   P  9  .   ? 15.794  -19.015 -7.886   1.00 85.72  ? 2008 GOL   A O3   1 
HETATM 22912 H  H31  . GOL   P  9  .   ? 15.605  -17.249 -8.783   1.00 102.55 ? 2008 GOL   A H31  1 
HETATM 22913 H  H32  . GOL   P  9  .   ? 14.414  -18.189 -9.056   1.00 102.55 ? 2008 GOL   A H32  1 
HETATM 22914 H  HO3  . GOL   P  9  .   ? 16.119  -19.416 -8.561   1.00 102.90 ? 2008 GOL   A HO3  1 
HETATM 22915 MG MG   . MG    Q  10 .   ? 7.572   -44.002 -13.147  1.00 45.34  ? 2001 MG    B MG   1 
HETATM 22916 CA CA   . CA    R  8  .   ? 8.174   -38.544 -15.549  1.00 39.63  ? 2002 CA    B CA   1 
HETATM 22917 CA CA   . CA    S  8  .   ? 7.518   -51.933 -8.569   1.00 55.08  ? 2003 CA    B CA   1 
HETATM 22918 C  C15  . A1A6A T  11 .   ? 13.898  -46.899 -23.822  1.00 59.20  ? 2004 A1A6A B C15  1 
HETATM 22919 C  C17  . A1A6A T  11 .   ? 15.036  -45.774 -25.490  1.00 57.60  ? 2004 A1A6A B C17  1 
HETATM 22920 C  C18  . A1A6A T  11 .   ? 14.373  -46.509 -26.475  1.00 55.27  ? 2004 A1A6A B C18  1 
HETATM 22921 C  C19  . A1A6A T  11 .   ? 14.671  -46.247 -27.988  1.00 53.94  ? 2004 A1A6A B C19  1 
HETATM 22922 C  C21  . A1A6A T  11 .   ? 16.464  -44.705 -27.186  1.00 59.23  ? 2004 A1A6A B C21  1 
HETATM 22923 C  C20  . A1A6A T  11 .   ? 15.356  -44.901 -28.183  1.00 55.90  ? 2004 A1A6A B C20  1 
HETATM 22924 C  C13  . A1A6A T  11 .   ? 12.088  -47.022 -22.045  1.00 66.95  ? 2004 A1A6A B C13  1 
HETATM 22925 C  C14  . A1A6A T  11 .   ? 13.616  -47.121 -22.311  1.00 62.58  ? 2004 A1A6A B C14  1 
HETATM 22926 C  C12  . A1A6A T  11 .   ? 11.729  -45.992 -20.951  1.00 64.28  ? 2004 A1A6A B C12  1 
HETATM 22927 C  C11  . A1A6A T  11 .   ? 10.183  -45.761 -20.880  1.00 61.24  ? 2004 A1A6A B C11  1 
HETATM 22928 C  C23  . A1A6A T  11 .   ? 13.428  -47.474 -26.122  1.00 55.78  ? 2004 A1A6A B C23  1 
HETATM 22929 C  C02  . A1A6A T  11 .   ? 5.532   -44.416 -15.809  1.00 57.46  ? 2004 A1A6A B C02  1 
HETATM 22930 C  C04  . A1A6A T  11 .   ? 5.821   -45.041 -17.144  1.00 60.42  ? 2004 A1A6A B C04  1 
HETATM 22931 C  C06  . A1A6A T  11 .   ? 7.647   -43.569 -17.724  1.00 68.22  ? 2004 A1A6A B C06  1 
HETATM 22932 C  C07  . A1A6A T  11 .   ? 8.742   -43.609 -18.529  1.00 66.62  ? 2004 A1A6A B C07  1 
HETATM 22933 C  C08  . A1A6A T  11 .   ? 8.601   -44.865 -19.378  1.00 62.09  ? 2004 A1A6A B C08  1 
HETATM 22934 C  C09  . A1A6A T  11 .   ? 7.600   -45.788 -18.568  1.00 63.76  ? 2004 A1A6A B C09  1 
HETATM 22935 C  C24  . A1A6A T  11 .   ? 13.196  -47.662 -24.758  1.00 58.61  ? 2004 A1A6A B C24  1 
HETATM 22936 C  C25  . A1A6A T  11 .   ? 5.286   -46.506 -17.140  1.00 53.71  ? 2004 A1A6A B C25  1 
HETATM 22937 C  C26  . A1A6A T  11 .   ? 5.905   -47.482 -16.358  1.00 51.92  ? 2004 A1A6A B C26  1 
HETATM 22938 C  C27  . A1A6A T  11 .   ? 5.413   -48.792 -16.360  1.00 49.82  ? 2004 A1A6A B C27  1 
HETATM 22939 C  C28  . A1A6A T  11 .   ? 4.304   -49.122 -17.137  1.00 49.22  ? 2004 A1A6A B C28  1 
HETATM 22940 C  C29  . A1A6A T  11 .   ? 3.683   -48.146 -17.914  1.00 49.55  ? 2004 A1A6A B C29  1 
HETATM 22941 C  C30  . A1A6A T  11 .   ? 4.175   -46.836 -17.914  1.00 50.24  ? 2004 A1A6A B C30  1 
HETATM 22942 N  N05  . A1A6A T  11 .   ? 7.270   -45.000 -17.388  1.00 65.79  ? 2004 A1A6A B N05  1 
HETATM 22943 N  N16  . A1A6A T  11 .   ? 14.779  -45.991 -24.196  1.00 58.62  ? 2004 A1A6A B N16  1 
HETATM 22944 N  N22  . A1A6A T  11 .   ? 16.032  -44.744 -25.823  1.00 57.22  ? 2004 A1A6A B N22  1 
HETATM 22945 O  O01  . A1A6A T  11 .   ? 6.477   -44.214 -14.984  1.00 58.04  ? 2004 A1A6A B O01  1 
HETATM 22946 O  O03  . A1A6A T  11 .   ? 4.354   -44.097 -15.511  1.00 53.57  ? 2004 A1A6A B O03  1 
HETATM 22947 O  O10  . A1A6A T  11 .   ? 9.827   -45.467 -19.516  1.00 60.64  ? 2004 A1A6A B O10  1 
HETATM 22948 C  C1   . NAG   U  12 .   ? 4.826   -28.637 32.498   1.00 124.74 ? 2005 NAG   B C1   1 
HETATM 22949 C  C2   . NAG   U  12 .   ? 3.434   -28.160 32.938   1.00 127.19 ? 2005 NAG   B C2   1 
HETATM 22950 C  C3   . NAG   U  12 .   ? 2.656   -29.295 33.601   1.00 128.43 ? 2005 NAG   B C3   1 
HETATM 22951 C  C4   . NAG   U  12 .   ? 3.608   -30.370 34.102   1.00 125.92 ? 2005 NAG   B C4   1 
HETATM 22952 C  C5   . NAG   U  12 .   ? 4.840   -29.702 34.699   1.00 125.43 ? 2005 NAG   B C5   1 
HETATM 22953 C  C6   . NAG   U  12 .   ? 5.770   -30.679 35.379   1.00 126.54 ? 2005 NAG   B C6   1 
HETATM 22954 C  C7   . NAG   U  12 .   ? 2.994   -25.824 33.544   1.00 129.32 ? 2005 NAG   B C7   1 
HETATM 22955 C  C8   . NAG   U  12 .   ? 3.189   -24.753 34.575   1.00 129.81 ? 2005 NAG   B C8   1 
HETATM 22956 N  N2   . NAG   U  12 .   ? 3.530   -27.015 33.829   1.00 128.70 ? 2005 NAG   B N2   1 
HETATM 22957 O  O3   . NAG   U  12 .   ? 1.741   -29.854 32.666   1.00 131.40 ? 2005 NAG   B O3   1 
HETATM 22958 O  O4   . NAG   U  12 .   ? 2.972   -31.160 35.100   1.00 122.95 ? 2005 NAG   B O4   1 
HETATM 22959 O  O5   . NAG   U  12 .   ? 5.594   -29.065 33.657   1.00 124.38 ? 2005 NAG   B O5   1 
HETATM 22960 O  O6   . NAG   U  12 .   ? 7.064   -30.121 35.565   1.00 127.63 ? 2005 NAG   B O6   1 
HETATM 22961 O  O7   . NAG   U  12 .   ? 2.378   -25.620 32.503   1.00 128.61 ? 2005 NAG   B O7   1 
HETATM 22962 H  H4   . NAG   U  12 .   ? 3.871   -30.951 33.364   1.00 151.14 ? 2005 NAG   B H4   1 
HETATM 22963 H  H5   . NAG   U  12 .   ? 4.557   -29.028 35.346   1.00 150.55 ? 2005 NAG   B H5   1 
HETATM 22964 H  H61  . NAG   U  12 .   ? 5.846   -31.482 34.830   1.00 151.89 ? 2005 NAG   B H61  1 
HETATM 22965 H  H62  . NAG   U  12 .   ? 5.399   -30.919 36.249   1.00 151.89 ? 2005 NAG   B H62  1 
HETATM 22966 H  H81  . NAG   U  12 .   ? 2.777   -23.924 34.264   1.00 155.81 ? 2005 NAG   B H81  1 
HETATM 22967 H  H82  . NAG   U  12 .   ? 4.144   -24.608 34.717   1.00 155.81 ? 2005 NAG   B H82  1 
HETATM 22968 H  H83  . NAG   U  12 .   ? 2.773   -25.029 35.413   1.00 155.81 ? 2005 NAG   B H83  1 
HETATM 22969 H  HN2  . NAG   U  12 .   ? 3.977   -27.114 34.617   1.00 154.48 ? 2005 NAG   B HN2  1 
HETATM 22970 H  HO4  . NAG   U  12 .   ? 3.323   -31.976 35.098   1.00 147.57 ? 2005 NAG   B HO4  1 
HETATM 22971 H  HO6  . NAG   U  12 .   ? 7.652   -30.565 35.069   1.00 153.20 ? 2005 NAG   B HO6  1 
HETATM 22972 C  C1   . GOL   V  9  .   ? 25.152  -34.558 5.568    1.00 108.82 ? 2006 GOL   B C1   1 
HETATM 22973 O  O1   . GOL   V  9  .   ? 24.164  -34.729 4.603    1.00 109.93 ? 2006 GOL   B O1   1 
HETATM 22974 C  C2   . GOL   V  9  .   ? 24.976  -35.696 6.596    1.00 107.25 ? 2006 GOL   B C2   1 
HETATM 22975 O  O2   . GOL   V  9  .   ? 24.747  -36.916 5.982    1.00 109.47 ? 2006 GOL   B O2   1 
HETATM 22976 C  C3   . GOL   V  9  .   ? 26.287  -35.690 7.410    1.00 104.01 ? 2006 GOL   B C3   1 
HETATM 22977 O  O3   . GOL   V  9  .   ? 26.412  -36.956 7.979    1.00 101.66 ? 2006 GOL   B O3   1 
HETATM 22978 H  H31  . GOL   V  9  .   ? 26.248  -34.975 8.064    1.00 124.85 ? 2006 GOL   B H31  1 
HETATM 22979 H  H32  . GOL   V  9  .   ? 27.022  -35.458 6.821    1.00 124.85 ? 2006 GOL   B H32  1 
HETATM 22980 H  HO3  . GOL   V  9  .   ? 26.007  -37.496 7.462    1.00 122.03 ? 2006 GOL   B HO3  1 
HETATM 22981 C  C1   . GOL   W  9  .   ? 28.724  -22.026 26.569   1.00 77.88  ? 2007 GOL   B C1   1 
HETATM 22982 O  O1   . GOL   W  9  .   ? 28.822  -22.968 27.589   1.00 78.37  ? 2007 GOL   B O1   1 
HETATM 22983 C  C2   . GOL   W  9  .   ? 30.143  -21.454 26.351   1.00 80.40  ? 2007 GOL   B C2   1 
HETATM 22984 O  O2   . GOL   W  9  .   ? 31.114  -22.443 26.401   1.00 78.42  ? 2007 GOL   B O2   1 
HETATM 22985 C  C3   . GOL   W  9  .   ? 30.325  -20.404 27.466   1.00 85.26  ? 2007 GOL   B C3   1 
HETATM 22986 O  O3   . GOL   W  9  .   ? 31.602  -19.871 27.301   1.00 89.67  ? 2007 GOL   B O3   1 
HETATM 22987 H  H31  . GOL   W  9  .   ? 30.193  -20.831 28.327   1.00 102.35 ? 2007 GOL   B H31  1 
HETATM 22988 H  H32  . GOL   W  9  .   ? 29.619  -19.743 27.396   1.00 102.35 ? 2007 GOL   B H32  1 
HETATM 22989 H  HO3  . GOL   W  9  .   ? 32.113  -20.526 27.120   1.00 107.64 ? 2007 GOL   B HO3  1 
HETATM 22990 C  C    . ACT   X  13 .   ? 9.338   -45.846 24.717   1.00 91.89  ? 2008 ACT   B C    1 
HETATM 22991 O  O    . ACT   X  13 .   ? 10.498  -45.428 24.446   1.00 90.62  ? 2008 ACT   B O    1 
HETATM 22992 O  OXT  . ACT   X  13 .   ? 8.680   -46.768 24.160   1.00 93.31  ? 2008 ACT   B OXT  1 
HETATM 22993 C  CH3  . ACT   X  13 .   ? 8.604   -45.136 25.903   1.00 91.02  ? 2008 ACT   B CH3  1 
HETATM 22994 C  C1   . NAG   Y  12 .   ? 5.490   -24.020 17.860   1.00 82.39  ? 2009 NAG   B C1   1 
HETATM 22995 C  C2   . NAG   Y  12 .   ? 6.133   -23.054 16.863   1.00 89.37  ? 2009 NAG   B C2   1 
HETATM 22996 C  C3   . NAG   Y  12 .   ? 5.597   -21.640 17.096   1.00 95.24  ? 2009 NAG   B C3   1 
HETATM 22997 C  C4   . NAG   Y  12 .   ? 4.072   -21.636 17.127   1.00 97.61  ? 2009 NAG   B C4   1 
HETATM 22998 C  C5   . NAG   Y  12 .   ? 3.543   -22.709 18.077   1.00 95.93  ? 2009 NAG   B C5   1 
HETATM 22999 C  C6   . NAG   Y  12 .   ? 2.039   -22.847 18.049   1.00 95.74  ? 2009 NAG   B C6   1 
HETATM 23000 C  C7   . NAG   Y  12 .   ? 8.392   -22.339 16.206   1.00 100.24 ? 2009 NAG   B C7   1 
HETATM 23001 C  C8   . NAG   Y  12 .   ? 9.861   -22.482 16.470   1.00 104.99 ? 2009 NAG   B C8   1 
HETATM 23002 N  N2   . NAG   Y  12 .   ? 7.583   -23.074 16.978   1.00 93.83  ? 2009 NAG   B N2   1 
HETATM 23003 O  O3   . NAG   Y  12 .   ? 6.067   -20.766 16.075   1.00 97.45  ? 2009 NAG   B O3   1 
HETATM 23004 O  O4   . NAG   Y  12 .   ? 3.605   -20.363 17.563   1.00 98.43  ? 2009 NAG   B O4   1 
HETATM 23005 O  O5   . NAG   Y  12 .   ? 4.081   -23.987 17.712   1.00 94.31  ? 2009 NAG   B O5   1 
HETATM 23006 O  O6   . NAG   Y  12 .   ? 1.623   -24.083 18.615   1.00 96.38  ? 2009 NAG   B O6   1 
HETATM 23007 O  O7   . NAG   Y  12 .   ? 7.958   -21.593 15.332   1.00 99.44  ? 2009 NAG   B O7   1 
HETATM 23008 H  H4   . NAG   Y  12 .   ? 3.739   -21.821 16.229   1.00 117.17 ? 2009 NAG   B H4   1 
HETATM 23009 H  H5   . NAG   Y  12 .   ? 3.824   -22.490 18.986   1.00 115.16 ? 2009 NAG   B H5   1 
HETATM 23010 H  H61  . NAG   Y  12 .   ? 1.731   -22.799 17.124   1.00 114.93 ? 2009 NAG   B H61  1 
HETATM 23011 H  H62  . NAG   Y  12 .   ? 1.642   -22.114 18.556   1.00 114.93 ? 2009 NAG   B H62  1 
HETATM 23012 H  H81  . NAG   Y  12 .   ? 10.165  -23.356 16.158   1.00 126.02 ? 2009 NAG   B H81  1 
HETATM 23013 H  H82  . NAG   Y  12 .   ? 10.029  -22.403 17.428   1.00 126.02 ? 2009 NAG   B H82  1 
HETATM 23014 H  H83  . NAG   Y  12 .   ? 10.347  -21.781 15.995   1.00 126.02 ? 2009 NAG   B H83  1 
HETATM 23015 H  HN2  . NAG   Y  12 .   ? 7.960   -23.614 17.609   1.00 112.63 ? 2009 NAG   B HN2  1 
HETATM 23016 H  HO4  . NAG   Y  12 .   ? 2.718   -20.371 17.605   1.00 118.15 ? 2009 NAG   B HO4  1 
HETATM 23017 H  HO6  . NAG   Y  12 .   ? 0.737   -24.132 18.600   1.00 115.69 ? 2009 NAG   B HO6  1 
HETATM 23018 C  C1   . GOL   Z  9  .   ? -3.607  -43.334 -44.070  1.00 87.59  ? 301  GOL   C C1   1 
HETATM 23019 O  O1   . GOL   Z  9  .   ? -4.956  -42.991 -44.064  1.00 86.95  ? 301  GOL   C O1   1 
HETATM 23020 C  C2   . GOL   Z  9  .   ? -2.885  -42.299 -44.961  1.00 88.82  ? 301  GOL   C C2   1 
HETATM 23021 O  O2   . GOL   Z  9  .   ? -3.072  -41.004 -44.502  1.00 87.57  ? 301  GOL   C O2   1 
HETATM 23022 C  C3   . GOL   Z  9  .   ? -1.401  -42.720 -44.921  1.00 90.74  ? 301  GOL   C C3   1 
HETATM 23023 O  O3   . GOL   Z  9  .   ? -1.382  -44.113 -44.963  1.00 91.03  ? 301  GOL   C O3   1 
HETATM 23024 H  H31  . GOL   Z  9  .   ? -0.990  -42.353 -44.123  1.00 108.93 ? 301  GOL   C H31  1 
HETATM 23025 H  H32  . GOL   Z  9  .   ? -0.935  -42.305 -45.663  1.00 108.93 ? 301  GOL   C H32  1 
HETATM 23026 H  HO3  . GOL   Z  9  .   ? -0.699  -44.335 -45.418  1.00 109.27 ? 301  GOL   C HO3  1 
HETATM 23027 C  C1   . GOL   AA 9  .   ? 14.923  -55.763 -61.832  1.00 101.57 ? 301  GOL   D C1   1 
HETATM 23028 O  O1   . GOL   AA 9  .   ? 14.026  -55.526 -62.871  1.00 102.77 ? 301  GOL   D O1   1 
HETATM 23029 C  C2   . GOL   AA 9  .   ? 16.241  -56.244 -62.481  1.00 100.20 ? 301  GOL   D C2   1 
HETATM 23030 O  O2   . GOL   AA 9  .   ? 16.601  -57.511 -62.042  1.00 100.73 ? 301  GOL   D O2   1 
HETATM 23031 C  C3   . GOL   AA 9  .   ? 17.284  -55.176 -62.089  1.00 98.74  ? 301  GOL   D C3   1 
HETATM 23032 O  O3   . GOL   AA 9  .   ? 18.388  -55.370 -62.917  1.00 99.77  ? 301  GOL   D O3   1 
HETATM 23033 H  H31  . GOL   AA 9  .   ? 17.489  -55.267 -61.145  1.00 118.52 ? 301  GOL   D H31  1 
HETATM 23034 H  H32  . GOL   AA 9  .   ? 16.884  -54.297 -62.181  1.00 118.52 ? 301  GOL   D H32  1 
HETATM 23035 H  HO3  . GOL   AA 9  .   ? 18.910  -54.713 -62.787  1.00 119.76 ? 301  GOL   D HO3  1 
HETATM 23036 C  C    . ACT   BA 13 .   ? 10.784  -35.455 -51.145  1.00 76.90  ? 302  ACT   D C    1 
HETATM 23037 O  O    . ACT   BA 13 .   ? 10.442  -35.202 -49.958  1.00 74.63  ? 302  ACT   D O    1 
HETATM 23038 O  OXT  . ACT   BA 13 .   ? 11.611  -34.843 -51.878  1.00 81.77  ? 302  ACT   D OXT  1 
HETATM 23039 C  CH3  . ACT   BA 13 .   ? 10.101  -36.689 -51.811  1.00 71.79  ? 302  ACT   D CH3  1 
HETATM 23040 O  O    . HOH   CA 14 .   ? 42.144  -19.128 -27.366  1.00 72.95  ? 2101 HOH   A O    1 
HETATM 23041 O  O    . HOH   CA 14 .   ? 13.112  -11.514 -12.306  1.00 72.46  ? 2102 HOH   A O    1 
HETATM 23042 O  O    . HOH   CA 14 .   ? 38.628  -5.986  -23.309  1.00 61.61  ? 2103 HOH   A O    1 
HETATM 23043 O  O    . HOH   CA 14 .   ? 35.001  -28.883 -39.243  1.00 53.42  ? 2104 HOH   A O    1 
HETATM 23044 O  O    . HOH   CA 14 .   ? 11.863  -26.772 -45.815  1.00 47.68  ? 2105 HOH   A O    1 
HETATM 23045 O  O    . HOH   CA 14 .   ? 16.797  -36.263 -45.458  1.00 63.60  ? 2106 HOH   A O    1 
HETATM 23046 O  O    . HOH   CA 14 .   ? 16.789  -21.553 -7.990   1.00 64.47  ? 2107 HOH   A O    1 
HETATM 23047 O  O    . HOH   CA 14 .   ? -6.045  -34.837 -35.012  1.00 60.14  ? 2108 HOH   A O    1 
HETATM 23048 O  O    . HOH   CA 14 .   ? -2.845  -17.144 -31.465  1.00 71.09  ? 2109 HOH   A O    1 
HETATM 23049 O  O    . HOH   CA 14 .   ? 10.202  -33.162 -25.369  1.00 50.57  ? 2110 HOH   A O    1 
HETATM 23050 O  O    . HOH   CA 14 .   ? 19.655  -27.896 -8.481   1.00 44.44  ? 2111 HOH   A O    1 
HETATM 23051 O  O    . HOH   CA 14 .   ? 24.021  -38.049 -23.862  1.00 57.88  ? 2112 HOH   A O    1 
HETATM 23052 O  O    . HOH   CA 14 .   ? 5.849   -37.603 -35.046  1.00 67.10  ? 2113 HOH   A O    1 
HETATM 23053 O  O    . HOH   CA 14 .   ? 2.585   -20.136 -26.959  1.00 58.70  ? 2114 HOH   A O    1 
HETATM 23054 O  O    . HOH   CA 14 .   ? 0.536   -36.651 -26.971  1.00 62.86  ? 2115 HOH   A O    1 
HETATM 23055 O  O    . HOH   CA 14 .   ? 21.052  -26.230 -6.735   1.00 58.62  ? 2116 HOH   A O    1 
HETATM 23056 O  O    . HOH   CA 14 .   ? 20.806  -37.839 -30.877  1.00 49.09  ? 2117 HOH   A O    1 
HETATM 23057 O  O    . HOH   CA 14 .   ? 3.815   -31.789 -54.513  1.00 61.27  ? 2118 HOH   A O    1 
HETATM 23058 O  O    . HOH   CA 14 .   ? 26.307  3.018   -29.641  1.00 59.10  ? 2119 HOH   A O    1 
HETATM 23059 O  O    . HOH   CA 14 .   ? 29.012  -26.572 -39.921  1.00 43.94  ? 2120 HOH   A O    1 
HETATM 23060 O  O    . HOH   CA 14 .   ? 11.386  -27.418 -35.814  1.00 41.34  ? 2121 HOH   A O    1 
HETATM 23061 O  O    . HOH   CA 14 .   ? 12.469  -40.997 -20.243  1.00 44.72  ? 2122 HOH   A O    1 
HETATM 23062 O  O    . HOH   CA 14 .   ? 2.211   -18.215 -34.425  1.00 44.19  ? 2123 HOH   A O    1 
HETATM 23063 O  O    . HOH   CA 14 .   ? 10.982  -38.068 -29.024  1.00 46.38  ? 2124 HOH   A O    1 
HETATM 23064 O  O    . HOH   CA 14 .   ? 28.881  -24.561 -41.697  1.00 57.63  ? 2125 HOH   A O    1 
HETATM 23065 O  O    . HOH   CA 14 .   ? 27.620  -19.201 -31.606  1.00 51.01  ? 2126 HOH   A O    1 
HETATM 23066 O  O    . HOH   CA 14 .   ? 11.032  -30.078 -36.147  1.00 47.84  ? 2127 HOH   A O    1 
HETATM 23067 O  O    . HOH   CA 14 .   ? -4.568  -25.942 -31.626  1.00 25.38  ? 2128 HOH   A O    1 
HETATM 23068 O  O    . HOH   CA 14 .   ? 13.773  -12.084 -20.990  1.00 55.22  ? 2129 HOH   A O    1 
HETATM 23069 O  O    . HOH   CA 14 .   ? 31.044  -22.474 -41.244  1.00 48.97  ? 2130 HOH   A O    1 
HETATM 23070 O  O    . HOH   CA 14 .   ? 1.394   -20.410 -24.631  1.00 52.50  ? 2131 HOH   A O    1 
HETATM 23071 O  O    . HOH   CA 14 .   ? 25.412  -38.696 -30.659  1.00 54.59  ? 2132 HOH   A O    1 
HETATM 23072 O  O    . HOH   CA 14 .   ? 29.099  -38.820 -29.728  1.00 46.83  ? 2133 HOH   A O    1 
HETATM 23073 O  O    . HOH   DA 14 .   ? 17.536  -36.624 -11.281  1.00 72.79  ? 2101 HOH   B O    1 
HETATM 23074 O  O    . HOH   DA 14 .   ? 9.623   -50.693 -8.089   1.00 57.60  ? 2102 HOH   B O    1 
HETATM 23075 O  O    . HOH   DA 14 .   ? 8.725   -44.394 -11.354  1.00 48.44  ? 2103 HOH   B O    1 
HETATM 23076 O  O    . HOH   DA 14 .   ? 12.534  -23.880 -9.442   1.00 47.62  ? 2104 HOH   B O    1 
HETATM 23077 O  O    . HOH   DA 14 .   ? 6.682   -26.667 -9.007   1.00 51.15  ? 2105 HOH   B O    1 
HETATM 23078 O  O    . HOH   DA 14 .   ? 11.037  -40.396 -8.934   1.00 44.82  ? 2106 HOH   B O    1 
HETATM 23079 O  O    . HOH   DA 14 .   ? 8.338   -45.894 -13.620  1.00 52.82  ? 2107 HOH   B O    1 
HETATM 23080 O  O    . HOH   DA 14 .   ? 11.133  -34.109 -9.365   1.00 42.61  ? 2108 HOH   B O    1 
HETATM 23081 O  O    . HOH   DA 14 .   ? -0.523  -31.480 -8.266   1.00 43.83  ? 2109 HOH   B O    1 
HETATM 23082 O  O    . HOH   DA 14 .   ? 2.003   -34.711 -25.254  1.00 47.47  ? 2110 HOH   B O    1 
HETATM 23083 O  O    . HOH   DA 14 .   ? 10.897  -37.636 -8.673   1.00 34.93  ? 2111 HOH   B O    1 
HETATM 23084 O  O    . HOH   DA 14 .   ? 4.110   -31.492 -9.737   1.00 45.23  ? 2112 HOH   B O    1 
HETATM 23085 O  O    . HOH   DA 14 .   ? -3.589  -36.117 -16.537  1.00 50.68  ? 2113 HOH   B O    1 
HETATM 23086 O  O    . HOH   DA 14 .   ? 8.307   -54.060 4.696    1.00 75.42  ? 2114 HOH   B O    1 
HETATM 23087 O  O    . HOH   DA 14 .   ? 9.606   -43.891 -14.300  1.00 55.59  ? 2115 HOH   B O    1 
HETATM 23088 O  O    . HOH   DA 14 .   ? 11.316  -46.168 -13.531  1.00 66.64  ? 2116 HOH   B O    1 
HETATM 23089 O  O    . HOH   DA 14 .   ? 8.027   -53.055 -10.550  1.00 65.64  ? 2117 HOH   B O    1 
HETATM 23090 O  O    . HOH   EA 14 .   ? 23.080  -61.720 -51.403  1.00 93.29  ? 401  HOH   D O    1 
HETATM 23091 O  O    . HOH   EA 14 .   ? 25.138  -57.963 -81.920  1.00 69.84  ? 402  HOH   D O    1 
HETATM 23092 O  O    . HOH   EA 14 .   ? 17.070  -56.110 -52.709  1.00 74.64  ? 403  HOH   D O    1 
HETATM 23093 O  O    . HOH   EA 14 .   ? 13.826  -53.694 -44.273  1.00 56.40  ? 404  HOH   D O    1 
HETATM 23094 O  O    . HOH   EA 14 .   ? 9.127   -37.657 -47.886  1.00 45.11  ? 405  HOH   D O    1 
HETATM 23095 O  O    . HOH   EA 14 .   ? 21.504  -41.805 -44.338  1.00 62.82  ? 406  HOH   D O    1 
HETATM 23096 O  O    . HOH   EA 14 .   ? 19.781  -55.683 -58.766  1.00 64.49  ? 407  HOH   D O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . PHE A 1   ? 1.0790 0.8550 0.9909 -0.3267 -0.2448 0.1861  1   PHE A N   
2     C CA  . PHE A 1   ? 1.1498 0.8892 1.0205 -0.3532 -0.2423 0.1653  1   PHE A CA  
3     C C   . PHE A 1   ? 1.1760 0.8520 1.0260 -0.3410 -0.2267 0.1492  1   PHE A C   
4     O O   . PHE A 1   ? 1.2511 0.8898 1.0749 -0.3559 -0.2213 0.1262  1   PHE A O   
5     C CB  . PHE A 1   ? 1.0256 0.7882 0.8986 -0.3926 -0.2523 0.1737  1   PHE A CB  
6     C CG  . PHE A 1   ? 1.2043 0.9694 1.1008 -0.3932 -0.2484 0.1891  1   PHE A CG  
7     C CD1 . PHE A 1   ? 1.3085 1.0247 1.1850 -0.4006 -0.2371 0.1802  1   PHE A CD1 
8     C CD2 . PHE A 1   ? 1.1854 1.0032 1.1283 -0.3882 -0.2555 0.2123  1   PHE A CD2 
9     C CE1 . PHE A 1   ? 1.2918 1.0141 1.1864 -0.4055 -0.2331 0.1956  1   PHE A CE1 
10    C CE2 . PHE A 1   ? 1.1551 0.9808 1.1199 -0.3918 -0.2488 0.2228  1   PHE A CE2 
11    C CZ  . PHE A 1   ? 1.2077 0.9869 1.1444 -0.4019 -0.2377 0.2152  1   PHE A CZ  
23    N N   . ASN A 2   ? 1.1260 0.7907 0.9903 -0.3159 -0.2196 0.1609  2   ASN A N   
24    C CA  . ASN A 2   ? 1.1062 0.7148 0.9562 -0.3088 -0.2097 0.1558  2   ASN A CA  
25    C C   . ASN A 2   ? 1.0962 0.6755 0.9418 -0.2747 -0.2032 0.1475  2   ASN A C   
26    O O   . ASN A 2   ? 1.1284 0.6653 0.9695 -0.2648 -0.1981 0.1506  2   ASN A O   
27    C CB  . ASN A 2   ? 1.0777 0.6939 0.9405 -0.3127 -0.2072 0.1775  2   ASN A CB  
28    C CG  . ASN A 2   ? 1.0366 0.7007 0.9262 -0.2926 -0.2063 0.1920  2   ASN A CG  
29    O OD1 . ASN A 2   ? 1.0161 0.7217 0.9259 -0.2871 -0.2122 0.1925  2   ASN A OD1 
30    N ND2 . ASN A 2   ? 1.0513 0.7112 0.9432 -0.2839 -0.1987 0.2039  2   ASN A ND2 
37    N N   . LEU A 3   ? 1.0483 0.6497 0.8971 -0.2580 -0.2048 0.1396  3   LEU A N   
38    C CA  . LEU A 3   ? 1.0886 0.6641 0.9349 -0.2274 -0.1989 0.1297  3   LEU A CA  
39    C C   . LEU A 3   ? 1.1931 0.7167 1.0251 -0.2323 -0.1924 0.1048  3   LEU A C   
40    O O   . LEU A 3   ? 1.2519 0.7746 1.0714 -0.2576 -0.1915 0.0855  3   LEU A O   
41    C CB  . LEU A 3   ? 1.0416 0.6547 0.8962 -0.2117 -0.2016 0.1265  3   LEU A CB  
42    C CG  . LEU A 3   ? 0.9573 0.6102 0.8367 -0.1938 -0.2037 0.1457  3   LEU A CG  
43    C CD1 . LEU A 3   ? 0.8904 0.5794 0.7830 -0.1840 -0.2083 0.1438  3   LEU A CD1 
44    C CD2 . LEU A 3   ? 0.9597 0.5916 0.8395 -0.1689 -0.1972 0.1509  3   LEU A CD2 
56    N N   . ASP A 4   ? 1.2350 0.7174 1.0726 -0.2095 -0.1880 0.1048  4   ASP A N   
57    C CA  . ASP A 4   ? 1.2773 0.7067 1.1163 -0.2089 -0.1807 0.0804  4   ASP A CA  
58    C C   . ASP A 4   ? 1.3092 0.7466 1.1498 -0.1924 -0.1748 0.0551  4   ASP A C   
59    O O   . ASP A 4   ? 1.3372 0.7789 1.1887 -0.1622 -0.1755 0.0615  4   ASP A O   
60    C CB  . ASP A 4   ? 1.2636 0.6465 1.1168 -0.1919 -0.1819 0.0970  4   ASP A CB  
61    C CG  . ASP A 4   ? 1.3126 0.6388 1.1831 -0.1853 -0.1746 0.0722  4   ASP A CG  
62    O OD1 . ASP A 4   ? 1.3451 0.6662 1.2120 -0.2011 -0.1653 0.0372  4   ASP A OD1 
63    O OD2 . ASP A 4   ? 1.3531 0.6422 1.2438 -0.1657 -0.1783 0.0872  4   ASP A OD2 
68    N N   . VAL A 5   ? 1.3087 0.7515 1.1370 -0.2154 -0.1686 0.0254  5   VAL A N   
69    C CA  . VAL A 5   ? 1.2984 0.7523 1.1252 -0.2065 -0.1605 -0.0023 5   VAL A CA  
70    C C   . VAL A 5   ? 1.3781 0.7820 1.2199 -0.2025 -0.1457 -0.0382 5   VAL A C   
71    O O   . VAL A 5   ? 1.3902 0.7992 1.2382 -0.1903 -0.1360 -0.0636 5   VAL A O   
72    C CB  . VAL A 5   ? 1.2368 0.7398 1.0389 -0.2379 -0.1627 -0.0123 5   VAL A CB  
73    C CG1 . VAL A 5   ? 1.1839 0.7361 0.9859 -0.2385 -0.1783 0.0243  5   VAL A CG1 
74    C CG2 . VAL A 5   ? 1.2375 0.7277 1.0228 -0.2786 -0.1580 -0.0342 5   VAL A CG2 
84    N N   . ASP A 6   ? 1.4282 0.7839 1.2815 -0.2126 -0.1427 -0.0420 6   ASP A N   
85    C CA  . ASP A 6   ? 1.5230 0.8280 1.4023 -0.2093 -0.1274 -0.0792 6   ASP A CA  
86    C C   . ASP A 6   ? 1.5537 0.8313 1.4707 -0.1666 -0.1278 -0.0719 6   ASP A C   
87    O O   . ASP A 6   ? 1.6210 0.8787 1.5646 -0.1554 -0.1137 -0.1073 6   ASP A O   
88    C CB  . ASP A 6   ? 1.5874 0.8452 1.4756 -0.2320 -0.1256 -0.0822 6   ASP A CB  
89    C CG  . ASP A 6   ? 1.6450 0.9308 1.4980 -0.2775 -0.1254 -0.0927 6   ASP A CG  
90    O OD1 . ASP A 6   ? 1.6502 0.9757 1.4788 -0.2975 -0.1190 -0.1191 6   ASP A OD1 
91    O OD2 . ASP A 6   ? 1.6787 0.9496 1.5281 -0.2956 -0.1327 -0.0727 6   ASP A OD2 
96    N N   . SER A 7   ? 1.5093 0.7896 1.4308 -0.1443 -0.1432 -0.0279 7   SER A N   
97    C CA  . SER A 7   ? 1.4569 0.7137 1.4133 -0.1069 -0.1480 -0.0137 7   SER A CA  
98    C C   . SER A 7   ? 1.3858 0.6830 1.3267 -0.0891 -0.1622 0.0251  7   SER A C   
99    O O   . SER A 7   ? 1.4069 0.6959 1.3472 -0.0857 -0.1744 0.0622  7   SER A O   
100   C CB  . SER A 7   ? 1.4787 0.6729 1.4694 -0.1036 -0.1526 0.0001  7   SER A CB  
101   O OG  . SER A 7   ? 1.4673 0.6572 1.4358 -0.1276 -0.1612 0.0281  7   SER A OG  
107   N N   . PRO A 8   ? 1.3078 0.6510 1.2360 -0.0801 -0.1598 0.0162  8   PRO A N   
108   C CA  . PRO A 8   ? 1.2288 0.6091 1.1495 -0.0615 -0.1704 0.0461  8   PRO A CA  
109   C C   . PRO A 8   ? 1.2184 0.5878 1.1674 -0.0278 -0.1741 0.0510  8   PRO A C   
110   O O   . PRO A 8   ? 1.2531 0.5938 1.2319 -0.0156 -0.1670 0.0273  8   PRO A O   
111   C CB  . PRO A 8   ? 1.1868 0.6186 1.0864 -0.0708 -0.1662 0.0326  8   PRO A CB  
112   C CG  . PRO A 8   ? 1.2167 0.6375 1.1200 -0.0802 -0.1524 -0.0084 8   PRO A CG  
113   C CD  . PRO A 8   ? 1.2818 0.6497 1.1984 -0.0931 -0.1469 -0.0215 8   PRO A CD  
121   N N   . ALA A 9   ? 1.1640 0.5601 1.1067 -0.0140 -0.1848 0.0806  9   ALA A N   
122   C CA  . ALA A 9   ? 1.1304 0.5259 1.0963 0.0153  -0.1919 0.0908  9   ALA A CA  
123   C C   . ALA A 9   ? 1.1142 0.5469 1.0809 0.0286  -0.1848 0.0683  9   ALA A C   
124   O O   . ALA A 9   ? 1.0987 0.5736 1.0433 0.0219  -0.1837 0.0705  9   ALA A O   
125   C CB  . ALA A 9   ? 1.1005 0.5120 1.0546 0.0184  -0.2060 0.1308  9   ALA A CB  
131   N N   . GLU A 10  ? 1.1328 0.5501 1.1306 0.0472  -0.1797 0.0471  10  GLU A N   
132   C CA  . GLU A 10  ? 1.1041 0.5528 1.1055 0.0566  -0.1701 0.0205  10  GLU A CA  
133   C C   . GLU A 10  ? 1.1399 0.6018 1.1652 0.0858  -0.1791 0.0332  10  GLU A C   
134   O O   . GLU A 10  ? 1.1952 0.6278 1.2586 0.1039  -0.1841 0.0364  10  GLU A O   
135   C CB  . GLU A 10  ? 1.0898 0.5172 1.1094 0.0502  -0.1530 -0.0216 10  GLU A CB  
136   C CG  . GLU A 10  ? 1.1039 0.5654 1.1248 0.0540  -0.1404 -0.0519 10  GLU A CG  
137   C CD  . GLU A 10  ? 1.2095 0.6540 1.2450 0.0415  -0.1201 -0.0980 10  GLU A CD  
138   O OE1 . GLU A 10  ? 1.2168 0.6318 1.2465 0.0207  -0.1150 -0.1080 10  GLU A OE1 
139   O OE2 . GLU A 10  ? 1.2235 0.6860 1.2767 0.0502  -0.1077 -0.1267 10  GLU A OE2 
146   N N   . TYR A 11  ? 1.1187 0.6251 1.1263 0.0897  -0.1819 0.0410  11  TYR A N   
147   C CA  . TYR A 11  ? 1.1381 0.6659 1.1630 0.1134  -0.1901 0.0507  11  TYR A CA  
148   C C   . TYR A 11  ? 1.1272 0.6845 1.1590 0.1200  -0.1786 0.0219  11  TYR A C   
149   O O   . TYR A 11  ? 1.1692 0.7450 1.1798 0.1029  -0.1685 0.0059  11  TYR A O   
150   C CB  . TYR A 11  ? 1.0947 0.6526 1.0957 0.1104  -0.2010 0.0801  11  TYR A CB  
151   C CG  . TYR A 11  ? 1.1328 0.6694 1.1222 0.0996  -0.2116 0.1105  11  TYR A CG  
152   C CD1 . TYR A 11  ? 1.1315 0.6592 1.0981 0.0763  -0.2070 0.1132  11  TYR A CD1 
153   C CD2 . TYR A 11  ? 1.1887 0.7176 1.1900 0.1101  -0.2277 0.1389  11  TYR A CD2 
154   C CE1 . TYR A 11  ? 1.1806 0.6910 1.1362 0.0640  -0.2156 0.1408  11  TYR A CE1 
155   C CE2 . TYR A 11  ? 1.2230 0.7349 1.2108 0.0962  -0.2379 0.1697  11  TYR A CE2 
156   C CZ  . TYR A 11  ? 1.2267 0.7290 1.1914 0.0732  -0.2306 0.1693  11  TYR A CZ  
157   O OH  . TYR A 11  ? 1.2761 0.7635 1.2271 0.0570  -0.2397 0.1998  11  TYR A OH  
167   N N   . SER A 12  ? 1.0424 0.6065 1.1057 0.1433  -0.1818 0.0180  12  SER A N   
168   C CA  . SER A 12  ? 0.9869 0.5794 1.0614 0.1501  -0.1705 -0.0094 12  SER A CA  
169   C C   . SER A 12  ? 0.9577 0.5823 1.0431 0.1687  -0.1811 0.0046  12  SER A C   
170   O O   . SER A 12  ? 0.9986 0.6178 1.0954 0.1808  -0.1972 0.0309  12  SER A O   
171   C CB  . SER A 12  ? 1.0099 0.5796 1.1232 0.1585  -0.1576 -0.0416 12  SER A CB  
172   O OG  . SER A 12  ? 1.0981 0.6413 1.2561 0.1812  -0.1691 -0.0280 12  SER A OG  
178   N N   . GLY A 13  ? 0.8981 0.5584 0.9788 0.1678  -0.1728 -0.0121 13  GLY A N   
179   C CA  . GLY A 13  ? 0.8705 0.5638 0.9637 0.1833  -0.1801 -0.0058 13  GLY A CA  
180   C C   . GLY A 13  ? 0.8569 0.5666 0.9792 0.1938  -0.1689 -0.0345 13  GLY A C   
181   O O   . GLY A 13  ? 0.8582 0.5542 0.9913 0.1886  -0.1539 -0.0615 13  GLY A O   
185   N N   . PRO A 14  ? 0.8063 0.5488 0.9418 0.2064  -0.1745 -0.0318 14  PRO A N   
186   C CA  . PRO A 14  ? 0.7659 0.5294 0.9316 0.2157  -0.1633 -0.0592 14  PRO A CA  
187   C C   . PRO A 14  ? 0.7828 0.5598 0.9266 0.1944  -0.1444 -0.0839 14  PRO A C   
188   O O   . PRO A 14  ? 0.7932 0.5796 0.9022 0.1760  -0.1447 -0.0740 14  PRO A O   
189   C CB  . PRO A 14  ? 0.7178 0.5180 0.8911 0.2269  -0.1748 -0.0468 14  PRO A CB  
190   C CG  . PRO A 14  ? 0.7217 0.5149 0.8784 0.2278  -0.1937 -0.0135 14  PRO A CG  
191   C CD  . PRO A 14  ? 0.7307 0.4959 0.8546 0.2100  -0.1899 -0.0063 14  PRO A CD  
199   N N   . GLU A 15  ? 0.8420 0.6224 1.0098 0.1952  -0.1280 -0.1157 15  GLU A N   
200   C CA  . GLU A 15  ? 0.9120 0.7112 1.0561 0.1700  -0.1101 -0.1387 15  GLU A CA  
201   C C   . GLU A 15  ? 0.9061 0.7449 1.0367 0.1637  -0.1127 -0.1306 15  GLU A C   
202   O O   . GLU A 15  ? 0.9218 0.7827 1.0784 0.1806  -0.1164 -0.1314 15  GLU A O   
203   C CB  . GLU A 15  ? 0.9960 0.7982 1.1713 0.1707  -0.0891 -0.1791 15  GLU A CB  
204   C CG  . GLU A 15  ? 1.0830 0.9078 1.2267 0.1374  -0.0698 -0.2036 15  GLU A CG  
205   C CD  . GLU A 15  ? 1.2162 1.0549 1.3915 0.1354  -0.0450 -0.2493 15  GLU A CD  
206   O OE1 . GLU A 15  ? 1.2838 1.1309 1.4340 0.1049  -0.0263 -0.2756 15  GLU A OE1 
207   O OE2 . GLU A 15  ? 1.2319 1.0768 1.4588 0.1626  -0.0438 -0.2598 15  GLU A OE2 
214   N N   . GLY A 16  ? 0.8594 0.7073 0.9539 0.1384  -0.1120 -0.1217 16  GLY A N   
215   C CA  . GLY A 16  ? 0.8129 0.6938 0.8996 0.1295  -0.1145 -0.1124 16  GLY A CA  
216   C C   . GLY A 16  ? 0.7822 0.6651 0.8677 0.1388  -0.1304 -0.0853 16  GLY A C   
217   O O   . GLY A 16  ? 0.7899 0.6977 0.8772 0.1331  -0.1323 -0.0789 16  GLY A O   
221   N N   . SER A 17  ? 0.7883 0.6469 0.8722 0.1505  -0.1406 -0.0704 17  SER A N   
222   C CA  . SER A 17  ? 0.7939 0.6583 0.8752 0.1563  -0.1527 -0.0492 17  SER A CA  
223   C C   . SER A 17  ? 0.7724 0.6311 0.8331 0.1383  -0.1552 -0.0334 17  SER A C   
224   O O   . SER A 17  ? 0.7433 0.6088 0.8045 0.1402  -0.1617 -0.0201 17  SER A O   
225   C CB  . SER A 17  ? 0.8170 0.6642 0.9059 0.1743  -0.1633 -0.0383 17  SER A CB  
226   O OG  . SER A 17  ? 0.8449 0.6579 0.9216 0.1695  -0.1640 -0.0324 17  SER A OG  
232   N N   . TYR A 18  ? 0.7796 0.6296 0.8247 0.1192  -0.1499 -0.0358 18  TYR A N   
233   C CA  . TYR A 18  ? 0.7453 0.5902 0.7762 0.1021  -0.1546 -0.0185 18  TYR A CA  
234   C C   . TYR A 18  ? 0.7510 0.5752 0.7763 0.1094  -0.1613 -0.0052 18  TYR A C   
235   O O   . TYR A 18  ? 0.7287 0.5573 0.7535 0.1026  -0.1656 0.0094  18  TYR A O   
236   C CB  . TYR A 18  ? 0.7240 0.5947 0.7681 0.0946  -0.1576 -0.0080 18  TYR A CB  
237   C CG  . TYR A 18  ? 0.6991 0.5894 0.7431 0.0772  -0.1538 -0.0116 18  TYR A CG  
238   C CD1 . TYR A 18  ? 0.7289 0.6195 0.7590 0.0691  -0.1449 -0.0295 18  TYR A CD1 
239   C CD2 . TYR A 18  ? 0.6690 0.5786 0.7298 0.0665  -0.1586 0.0028  18  TYR A CD2 
240   C CE1 . TYR A 18  ? 0.7509 0.6648 0.7756 0.0478  -0.1408 -0.0320 18  TYR A CE1 
241   C CE2 . TYR A 18  ? 0.6776 0.6066 0.7371 0.0469  -0.1576 0.0053  18  TYR A CE2 
242   C CZ  . TYR A 18  ? 0.7252 0.6583 0.7624 0.0360  -0.1487 -0.0116 18  TYR A CZ  
243   O OH  . TYR A 18  ? 0.7520 0.7096 0.7827 0.0114  -0.1471 -0.0085 18  TYR A OH  
253   N N   . PHE A 19  ? 0.8001 0.6027 0.8256 0.1225  -0.1621 -0.0097 19  PHE A N   
254   C CA  . PHE A 19  ? 0.7910 0.5707 0.8078 0.1250  -0.1690 0.0053  19  PHE A CA  
255   C C   . PHE A 19  ? 0.8048 0.5720 0.8040 0.1043  -0.1682 0.0132  19  PHE A C   
256   O O   . PHE A 19  ? 0.8102 0.5648 0.8005 0.0918  -0.1629 0.0028  19  PHE A O   
257   C CB  . PHE A 19  ? 0.8577 0.6111 0.8843 0.1391  -0.1705 0.0001  19  PHE A CB  
258   C CG  . PHE A 19  ? 0.9222 0.6481 0.9408 0.1391  -0.1789 0.0188  19  PHE A CG  
259   C CD1 . PHE A 19  ? 0.9492 0.6465 0.9554 0.1249  -0.1758 0.0187  19  PHE A CD1 
260   C CD2 . PHE A 19  ? 0.9567 0.6875 0.9786 0.1500  -0.1904 0.0372  19  PHE A CD2 
261   C CE1 . PHE A 19  ? 1.0165 0.6877 1.0163 0.1230  -0.1835 0.0373  19  PHE A CE1 
262   C CE2 . PHE A 19  ? 1.0136 0.7211 1.0261 0.1464  -0.1990 0.0580  19  PHE A CE2 
263   C CZ  . PHE A 19  ? 1.0434 0.7193 1.0463 0.1336  -0.1953 0.0583  19  PHE A CZ  
273   N N   . GLY A 20  ? 0.7759 0.5504 0.7717 0.0986  -0.1727 0.0293  20  GLY A N   
274   C CA  . GLY A 20  ? 0.7851 0.5545 0.7710 0.0791  -0.1734 0.0390  20  GLY A CA  
275   C C   . GLY A 20  ? 0.7372 0.5344 0.7365 0.0682  -0.1739 0.0447  20  GLY A C   
276   O O   . GLY A 20  ? 0.6773 0.4752 0.6749 0.0515  -0.1766 0.0551  20  GLY A O   
280   N N   . PHE A 21  ? 0.7256 0.5457 0.7431 0.0767  -0.1724 0.0397  21  PHE A N   
281   C CA  . PHE A 21  ? 0.6691 0.5130 0.7107 0.0680  -0.1739 0.0474  21  PHE A CA  
282   C C   . PHE A 21  ? 0.6731 0.5242 0.7312 0.0659  -0.1743 0.0570  21  PHE A C   
283   O O   . PHE A 21  ? 0.6789 0.5444 0.7634 0.0560  -0.1769 0.0669  21  PHE A O   
284   C CB  . PHE A 21  ? 0.6677 0.5314 0.7287 0.0784  -0.1712 0.0380  21  PHE A CB  
285   C CG  . PHE A 21  ? 0.6407 0.5250 0.7329 0.0689  -0.1737 0.0468  21  PHE A CG  
286   C CD1 . PHE A 21  ? 0.6574 0.5479 0.7473 0.0530  -0.1780 0.0544  21  PHE A CD1 
287   C CD2 . PHE A 21  ? 0.5758 0.4746 0.7026 0.0740  -0.1717 0.0473  21  PHE A CD2 
288   C CE1 . PHE A 21  ? 0.6323 0.5409 0.7561 0.0432  -0.1838 0.0689  21  PHE A CE1 
289   C CE2 . PHE A 21  ? 0.5532 0.4675 0.7204 0.0667  -0.1748 0.0565  21  PHE A CE2 
290   C CZ  . PHE A 21  ? 0.5850 0.5032 0.7519 0.0519  -0.1827 0.0706  21  PHE A CZ  
300   N N   . ALA A 22  ? 0.6834 0.5271 0.7296 0.0735  -0.1720 0.0552  22  ALA A N   
301   C CA  . ALA A 22  ? 0.7030 0.5573 0.7610 0.0687  -0.1689 0.0602  22  ALA A CA  
302   C C   . ALA A 22  ? 0.7397 0.5749 0.7671 0.0679  -0.1700 0.0657  22  ALA A C   
303   O O   . ALA A 22  ? 0.7568 0.5777 0.7649 0.0777  -0.1730 0.0637  22  ALA A O   
304   C CB  . ALA A 22  ? 0.7047 0.5859 0.7886 0.0762  -0.1620 0.0486  22  ALA A CB  
310   N N   . VAL A 23  ? 0.7026 0.5383 0.7303 0.0556  -0.1685 0.0744  23  VAL A N   
311   C CA  . VAL A 23  ? 0.7165 0.5328 0.7157 0.0504  -0.1705 0.0837  23  VAL A CA  
312   C C   . VAL A 23  ? 0.7511 0.5883 0.7586 0.0389  -0.1636 0.0869  23  VAL A C   
313   O O   . VAL A 23  ? 0.7846 0.6418 0.8233 0.0322  -0.1587 0.0843  23  VAL A O   
314   C CB  . VAL A 23  ? 0.7308 0.5160 0.7134 0.0413  -0.1759 0.0910  23  VAL A CB  
315   C CG1 . VAL A 23  ? 0.7661 0.5289 0.7371 0.0519  -0.1791 0.0832  23  VAL A CG1 
316   C CG2 . VAL A 23  ? 0.7512 0.5481 0.7524 0.0277  -0.1768 0.0942  23  VAL A CG2 
326   N N   . ASP A 24  ? 0.7513 0.5859 0.7339 0.0352  -0.1636 0.0934  24  ASP A N   
327   C CA  . ASP A 24  ? 0.7596 0.6160 0.7431 0.0196  -0.1552 0.0954  24  ASP A CA  
328   C C   . ASP A 24  ? 0.8338 0.6735 0.7794 0.0112  -0.1611 0.1127  24  ASP A C   
329   O O   . ASP A 24  ? 0.9098 0.7284 0.8363 0.0210  -0.1716 0.1212  24  ASP A O   
330   C CB  . ASP A 24  ? 0.7702 0.6682 0.7755 0.0200  -0.1428 0.0770  24  ASP A CB  
331   C CG  . ASP A 24  ? 0.8128 0.7398 0.8370 0.0030  -0.1286 0.0704  24  ASP A CG  
332   O OD1 . ASP A 24  ? 0.8329 0.7500 0.8405 -0.0110 -0.1298 0.0843  24  ASP A OD1 
333   O OD2 . ASP A 24  ? 0.8447 0.8048 0.9044 0.0029  -0.1150 0.0494  24  ASP A OD2 
338   N N   . PHE A 25  ? 0.8437 0.6943 0.7837 -0.0079 -0.1549 0.1194  25  PHE A N   
339   C CA  . PHE A 25  ? 0.8601 0.7012 0.7649 -0.0214 -0.1602 0.1391  25  PHE A CA  
340   C C   . PHE A 25  ? 0.8682 0.7482 0.7587 -0.0288 -0.1548 0.1351  25  PHE A C   
341   O O   . PHE A 25  ? 0.8340 0.7538 0.7455 -0.0316 -0.1398 0.1122  25  PHE A O   
342   C CB  . PHE A 25  ? 0.8452 0.6852 0.7479 -0.0429 -0.1549 0.1482  25  PHE A CB  
343   C CG  . PHE A 25  ? 0.8373 0.6347 0.7396 -0.0427 -0.1638 0.1581  25  PHE A CG  
344   C CD1 . PHE A 25  ? 0.8947 0.6494 0.7729 -0.0425 -0.1764 0.1766  25  PHE A CD1 
345   C CD2 . PHE A 25  ? 0.8193 0.6211 0.7487 -0.0449 -0.1600 0.1491  25  PHE A CD2 
346   C CE1 . PHE A 25  ? 0.9391 0.6554 0.8182 -0.0452 -0.1817 0.1799  25  PHE A CE1 
347   C CE2 . PHE A 25  ? 0.8528 0.6205 0.7773 -0.0498 -0.1678 0.1560  25  PHE A CE2 
348   C CZ  . PHE A 25  ? 0.9070 0.6316 0.8052 -0.0505 -0.1769 0.1684  25  PHE A CZ  
358   N N   . PHE A 26  ? 0.9046 0.7742 0.7618 -0.0340 -0.1675 0.1576  26  PHE A N   
359   C CA  . PHE A 26  ? 0.8387 0.7485 0.6726 -0.0479 -0.1660 0.1595  26  PHE A CA  
360   C C   . PHE A 26  ? 1.0218 0.9342 0.8219 -0.0758 -0.1695 0.1861  26  PHE A C   
361   O O   . PHE A 26  ? 1.0400 0.9122 0.8254 -0.0753 -0.1872 0.2167  26  PHE A O   
362   C CB  . PHE A 26  ? 0.9913 0.8955 0.8170 -0.0312 -0.1826 0.1680  26  PHE A CB  
363   C CG  . PHE A 26  ? 1.0235 0.9752 0.8230 -0.0484 -0.1831 0.1700  26  PHE A CG  
364   C CD1 . PHE A 26  ? 0.8554 0.8589 0.6579 -0.0654 -0.1610 0.1405  26  PHE A CD1 
365   C CD2 . PHE A 26  ? 1.0767 1.0238 0.8526 -0.0492 -0.2058 0.2004  26  PHE A CD2 
366   C CE1 . PHE A 26  ? 1.0318 1.0840 0.8061 -0.0863 -0.1597 0.1380  26  PHE A CE1 
367   C CE2 . PHE A 26  ? 0.9290 0.9258 0.6765 -0.0697 -0.2086 0.2044  26  PHE A CE2 
368   C CZ  . PHE A 26  ? 0.9178 0.9684 0.6605 -0.0900 -0.1845 0.1714  26  PHE A CZ  
378   N N   . VAL A 27  ? 1.0440 1.0043 0.8357 -0.1015 -0.1515 0.1733  27  VAL A N   
379   C CA  . VAL A 27  ? 1.0796 1.0527 0.8358 -0.1341 -0.1521 0.1972  27  VAL A CA  
380   C C   . VAL A 27  ? 1.1289 1.1609 0.8546 -0.1588 -0.1455 0.1916  27  VAL A C   
381   O O   . VAL A 27  ? 1.0888 1.1695 0.8289 -0.1695 -0.1205 0.1549  27  VAL A O   
382   C CB  . VAL A 27  ? 1.0569 1.0367 0.8300 -0.1496 -0.1337 0.1864  27  VAL A CB  
383   C CG1 . VAL A 27  ? 0.9962 0.9199 0.7912 -0.1313 -0.1434 0.1956  27  VAL A CG1 
384   C CG2 . VAL A 27  ? 1.0608 1.0892 0.8706 -0.1510 -0.1062 0.1428  27  VAL A CG2 
394   N N   . PRO A 28  ? 1.2718 1.3040 0.9589 -0.1696 -0.1673 0.2261  28  PRO A N   
395   C CA  . PRO A 28  ? 1.3833 1.4789 1.0332 -0.2016 -0.1621 0.2236  28  PRO A CA  
396   C C   . PRO A 28  ? 1.5288 1.6653 1.1561 -0.2428 -0.1410 0.2185  28  PRO A C   
397   O O   . PRO A 28  ? 1.6089 1.7183 1.2372 -0.2506 -0.1408 0.2358  28  PRO A O   
398   C CB  . PRO A 28  ? 1.4125 1.4907 1.0304 -0.2041 -0.1971 0.2740  28  PRO A CB  
399   C CG  . PRO A 28  ? 1.3621 1.3748 1.0161 -0.1614 -0.2149 0.2837  28  PRO A CG  
400   C CD  . PRO A 28  ? 1.3083 1.2867 0.9927 -0.1496 -0.1985 0.2647  28  PRO A CD  
408   N N   . SER A 29  ? 1.6441 1.8496 1.2514 -0.2717 -0.1216 0.1915  29  SER A N   
409   C CA  . SER A 29  ? 1.8022 2.0582 1.3920 -0.3135 -0.0950 0.1761  29  SER A CA  
410   C C   . SER A 29  ? 1.9883 2.2486 1.5208 -0.3516 -0.1127 0.2278  29  SER A C   
411   O O   . SER A 29  ? 2.0782 2.3667 1.5980 -0.3848 -0.0935 0.2237  29  SER A O   
412   C CB  . SER A 29  ? 1.8235 2.1550 1.4090 -0.3363 -0.0669 0.1271  29  SER A CB  
413   O OG  . SER A 29  ? 1.8636 2.2482 1.4423 -0.3757 -0.0349 0.1019  29  SER A OG  
419   N N   . ALA A 30  ? 2.0323 2.2665 1.5348 -0.3483 -0.1494 0.2780  30  ALA A N   
420   C CA  . ALA A 30  ? 2.1537 2.3910 1.6050 -0.3856 -0.1713 0.3348  30  ALA A CA  
421   C C   . ALA A 30  ? 2.1460 2.3086 1.6136 -0.3707 -0.1899 0.3749  30  ALA A C   
422   O O   . ALA A 30  ? 2.2734 2.4135 1.7136 -0.3862 -0.2201 0.4328  30  ALA A O   
423   C CB  . ALA A 30  ? 2.2385 2.4917 1.6551 -0.3933 -0.2042 0.3730  30  ALA A CB  
429   N N   . SER A 31  ? 2.0103 2.1351 1.5242 -0.3431 -0.1735 0.3465  31  SER A N   
430   C CA  . SER A 31  ? 1.9581 2.0149 1.4888 -0.3319 -0.1869 0.3760  31  SER A CA  
431   C C   . SER A 31  ? 1.8956 1.8922 1.4287 -0.3098 -0.2257 0.4241  31  SER A C   
432   O O   . SER A 31  ? 1.9434 1.8975 1.4697 -0.3201 -0.2450 0.4683  31  SER A O   
433   C CB  . SER A 31  ? 2.0419 2.1186 1.5421 -0.3777 -0.1782 0.3969  31  SER A CB  
434   O OG  . SER A 31  ? 2.1536 2.2455 1.6036 -0.4121 -0.2021 0.4492  31  SER A OG  
440   N N   . SER A 32  ? 1.8084 1.8015 1.3573 -0.2794 -0.2368 0.4144  32  SER A N   
441   C CA  . SER A 32  ? 1.8249 1.7649 1.3891 -0.2536 -0.2714 0.4532  32  SER A CA  
442   C C   . SER A 32  ? 1.7824 1.6534 1.3963 -0.2126 -0.2700 0.4362  32  SER A C   
443   O O   . SER A 32  ? 1.7372 1.6003 1.3666 -0.2099 -0.2473 0.4055  32  SER A O   
444   C CB  . SER A 32  ? 1.8327 1.8073 1.3918 -0.2429 -0.2835 0.4501  32  SER A CB  
445   O OG  . SER A 32  ? 1.9073 1.9483 1.4151 -0.2866 -0.2870 0.4685  32  SER A OG  
451   N N   . ARG A 33  ? 1.7552 1.5791 1.3966 -0.1821 -0.2943 0.4557  33  ARG A N   
452   C CA  . ARG A 33  ? 1.6927 1.4577 1.3789 -0.1457 -0.2908 0.4339  33  ARG A CA  
453   C C   . ARG A 33  ? 1.5805 1.3705 1.2823 -0.1275 -0.2648 0.3787  33  ARG A C   
454   O O   . ARG A 33  ? 1.5915 1.4347 1.2817 -0.1308 -0.2553 0.3580  33  ARG A O   
455   C CB  . ARG A 33  ? 1.7270 1.4492 1.4456 -0.1154 -0.3174 0.4558  33  ARG A CB  
456   C CG  . ARG A 33  ? 1.8217 1.5043 1.5439 -0.1271 -0.3459 0.5126  33  ARG A CG  
457   C CD  . ARG A 33  ? 1.8491 1.4990 1.6255 -0.0904 -0.3601 0.5144  33  ARG A CD  
458   N NE  . ARG A 33  ? 2.0038 1.6311 1.8030 -0.0966 -0.3750 0.5495  33  ARG A NE  
459   C CZ  . ARG A 33  ? 2.0970 1.6999 1.9466 -0.0706 -0.3891 0.5589  33  ARG A CZ  
460   N NH1 . ARG A 33  ? 2.1332 1.7159 2.0051 -0.0790 -0.4039 0.5933  33  ARG A NH1 
461   N NH2 . ARG A 33  ? 2.1294 1.7295 2.0101 -0.0371 -0.3884 0.5342  33  ARG A NH2 
475   N N   . MET A 34  ? 1.4598 1.2115 1.1892 -0.1107 -0.2539 0.3559  34  MET A N   
476   C CA  . MET A 34  ? 1.3193 1.0865 1.0705 -0.0922 -0.2339 0.3104  34  MET A CA  
477   C C   . MET A 34  ? 1.2832 1.0166 1.0647 -0.0566 -0.2431 0.2998  34  MET A C   
478   O O   . MET A 34  ? 1.2906 0.9759 1.0861 -0.0450 -0.2596 0.3202  34  MET A O   
479   C CB  . MET A 34  ? 1.2337 0.9896 0.9948 -0.1012 -0.2171 0.2937  34  MET A CB  
480   C CG  . MET A 34  ? 1.2036 0.9975 0.9410 -0.1367 -0.2046 0.2998  34  MET A CG  
481   S SD  . MET A 34  ? 1.2494 1.0248 1.0013 -0.1499 -0.1911 0.2907  34  MET A SD  
482   C CE  . MET A 34  ? 1.2778 1.1248 1.0152 -0.1845 -0.1678 0.2790  34  MET A CE  
492   N N   . PHE A 35  ? 1.2343 0.9943 1.0301 -0.0404 -0.2314 0.2667  35  PHE A N   
493   C CA  . PHE A 35  ? 1.1957 0.9341 1.0185 -0.0095 -0.2370 0.2529  35  PHE A CA  
494   C C   . PHE A 35  ? 1.0873 0.8313 0.9301 0.0008  -0.2193 0.2168  35  PHE A C   
495   O O   . PHE A 35  ? 1.0738 0.8413 0.9153 -0.0133 -0.2042 0.2034  35  PHE A O   
496   C CB  . PHE A 35  ? 0.9429 0.7132 0.7630 -0.0003 -0.2468 0.2562  35  PHE A CB  
497   C CG  . PHE A 35  ? 1.1146 0.8902 0.9137 -0.0146 -0.2676 0.2966  35  PHE A CG  
498   C CD1 . PHE A 35  ? 1.0977 0.9203 0.8610 -0.0453 -0.2644 0.3071  35  PHE A CD1 
499   C CD2 . PHE A 35  ? 1.1676 0.9033 0.9861 0.0005  -0.2904 0.3247  35  PHE A CD2 
500   C CE1 . PHE A 35  ? 1.1335 0.9656 0.8731 -0.0635 -0.2862 0.3494  35  PHE A CE1 
501   C CE2 . PHE A 35  ? 1.2116 0.9528 1.0156 -0.0139 -0.3139 0.3691  35  PHE A CE2 
502   C CZ  . PHE A 35  ? 1.1745 0.9650 0.9351 -0.0475 -0.3130 0.3838  35  PHE A CZ  
512   N N   . LEU A 36  ? 1.0607 0.7850 0.9258 0.0248  -0.2220 0.2027  36  LEU A N   
513   C CA  . LEU A 36  ? 1.0067 0.7387 0.8906 0.0342  -0.2090 0.1730  36  LEU A CA  
514   C C   . LEU A 36  ? 1.0223 0.7853 0.9169 0.0495  -0.2078 0.1574  36  LEU A C   
515   O O   . LEU A 36  ? 1.1099 0.8683 1.0075 0.0628  -0.2195 0.1654  36  LEU A O   
516   C CB  . LEU A 36  ? 0.9808 0.6692 0.8787 0.0438  -0.2103 0.1655  36  LEU A CB  
517   C CG  . LEU A 36  ? 1.0328 0.6896 0.9240 0.0274  -0.2090 0.1731  36  LEU A CG  
518   C CD1 . LEU A 36  ? 1.1313 0.7632 1.0102 0.0181  -0.2206 0.2025  36  LEU A CD1 
519   C CD2 . LEU A 36  ? 1.0457 0.6700 0.9506 0.0344  -0.2065 0.1556  36  LEU A CD2 
531   N N   . LEU A 37  ? 0.9192 0.7138 0.8249 0.0471  -0.1944 0.1364  37  LEU A N   
532   C CA  . LEU A 37  ? 0.8751 0.6963 0.7962 0.0603  -0.1911 0.1179  37  LEU A CA  
533   C C   . LEU A 37  ? 0.8130 0.6188 0.7557 0.0722  -0.1875 0.1025  37  LEU A C   
534   O O   . LEU A 37  ? 0.7708 0.5700 0.7210 0.0639  -0.1815 0.0990  37  LEU A O   
535   C CB  . LEU A 37  ? 0.8622 0.7287 0.7888 0.0486  -0.1777 0.1030  37  LEU A CB  
536   C CG  . LEU A 37  ? 0.8890 0.7820 0.7894 0.0294  -0.1773 0.1136  37  LEU A CG  
537   C CD1 . LEU A 37  ? 0.8877 0.8285 0.8007 0.0176  -0.1591 0.0885  37  LEU A CD1 
538   C CD2 . LEU A 37  ? 0.8951 0.7888 0.7752 0.0340  -0.1944 0.1317  37  LEU A CD2 
550   N N   . VAL A 38  ? 0.8215 0.6253 0.7741 0.0891  -0.1918 0.0947  38  VAL A N   
551   C CA  . VAL A 38  ? 0.8222 0.6153 0.7909 0.0971  -0.1880 0.0802  38  VAL A CA  
552   C C   . VAL A 38  ? 0.7927 0.6132 0.7778 0.1083  -0.1856 0.0654  38  VAL A C   
553   O O   . VAL A 38  ? 0.8151 0.6440 0.7999 0.1189  -0.1921 0.0668  38  VAL A O   
554   C CB  . VAL A 38  ? 0.8933 0.6485 0.8605 0.1047  -0.1935 0.0822  38  VAL A CB  
555   C CG1 . VAL A 38  ? 0.9299 0.6822 0.9086 0.1070  -0.1869 0.0639  38  VAL A CG1 
556   C CG2 . VAL A 38  ? 0.9197 0.6453 0.8726 0.0919  -0.1958 0.0962  38  VAL A CG2 
566   N N   . GLY A 39  ? 0.7917 0.6268 0.7940 0.1049  -0.1779 0.0536  39  GLY A N   
567   C CA  . GLY A 39  ? 0.7642 0.6220 0.7849 0.1135  -0.1751 0.0396  39  GLY A CA  
568   C C   . GLY A 39  ? 0.7240 0.5687 0.7485 0.1224  -0.1765 0.0325  39  GLY A C   
569   O O   . GLY A 39  ? 0.7327 0.5587 0.7524 0.1158  -0.1752 0.0328  39  GLY A O   
573   N N   . ALA A 40  ? 0.6772 0.5361 0.7105 0.1349  -0.1783 0.0241  40  ALA A N   
574   C CA  . ALA A 40  ? 0.6686 0.5244 0.7116 0.1431  -0.1766 0.0124  40  ALA A CA  
575   C C   . ALA A 40  ? 0.6473 0.5341 0.7088 0.1458  -0.1730 0.0010  40  ALA A C   
576   O O   . ALA A 40  ? 0.6518 0.5536 0.7219 0.1574  -0.1763 -0.0049 40  ALA A O   
577   C CB  . ALA A 40  ? 0.7021 0.5425 0.7464 0.1578  -0.1832 0.0140  40  ALA A CB  
583   N N   . PRO A 41  ? 0.6130 0.5103 0.6854 0.1345  -0.1677 -0.0007 41  PRO A N   
584   C CA  . PRO A 41  ? 0.6053 0.5300 0.7005 0.1351  -0.1644 -0.0101 41  PRO A CA  
585   C C   . PRO A 41  ? 0.6004 0.5373 0.7053 0.1420  -0.1630 -0.0218 41  PRO A C   
586   O O   . PRO A 41  ? 0.5963 0.5563 0.7195 0.1436  -0.1611 -0.0306 41  PRO A O   
587   C CB  . PRO A 41  ? 0.5730 0.4995 0.6855 0.1210  -0.1612 -0.0042 41  PRO A CB  
588   C CG  . PRO A 41  ? 0.5833 0.4878 0.6774 0.1121  -0.1637 0.0068  41  PRO A CG  
589   C CD  . PRO A 41  ? 0.6207 0.5062 0.6901 0.1196  -0.1664 0.0087  41  PRO A CD  
597   N N   . LYS A 42  ? 0.6117 0.5360 0.7079 0.1448  -0.1621 -0.0251 42  LYS A N   
598   C CA  . LYS A 42  ? 0.6830 0.6226 0.7915 0.1508  -0.1585 -0.0392 42  LYS A CA  
599   C C   . LYS A 42  ? 0.7418 0.6790 0.8546 0.1691  -0.1628 -0.0444 42  LYS A C   
600   O O   . LYS A 42  ? 0.7561 0.7053 0.8840 0.1759  -0.1588 -0.0580 42  LYS A O   
601   C CB  . LYS A 42  ? 0.7369 0.6728 0.8395 0.1368  -0.1512 -0.0441 42  LYS A CB  
602   C CG  . LYS A 42  ? 0.7304 0.6808 0.8410 0.1190  -0.1499 -0.0369 42  LYS A CG  
603   C CD  . LYS A 42  ? 0.7699 0.7261 0.8704 0.1006  -0.1440 -0.0403 42  LYS A CD  
604   C CE  . LYS A 42  ? 0.8165 0.7914 0.9315 0.0831  -0.1460 -0.0284 42  LYS A CE  
605   N NZ  . LYS A 42  ? 0.8507 0.8344 0.9486 0.0570  -0.1434 -0.0240 42  LYS A NZ  
619   N N   . ALA A 43  ? 0.7775 0.7015 0.8812 0.1762  -0.1715 -0.0323 43  ALA A N   
620   C CA  . ALA A 43  ? 0.7633 0.6835 0.8776 0.1933  -0.1800 -0.0301 43  ALA A CA  
621   C C   . ALA A 43  ? 0.7830 0.7376 0.9154 0.2023  -0.1858 -0.0345 43  ALA A C   
622   O O   . ALA A 43  ? 0.7568 0.7337 0.8842 0.1950  -0.1869 -0.0340 43  ALA A O   
623   C CB  . ALA A 43  ? 0.7149 0.6145 0.8134 0.1942  -0.1905 -0.0098 43  ALA A CB  
629   N N   . ASN A 44  ? 0.8026 0.7631 0.9602 0.2175  -0.1887 -0.0412 44  ASN A N   
630   C CA  . ASN A 44  ? 0.8373 0.8322 1.0150 0.2268  -0.1981 -0.0420 44  ASN A CA  
631   C C   . ASN A 44  ? 0.8175 0.8164 0.9856 0.2298  -0.2169 -0.0185 44  ASN A C   
632   O O   . ASN A 44  ? 0.8778 0.8484 1.0359 0.2315  -0.2240 -0.0012 44  ASN A O   
633   C CB  . ASN A 44  ? 0.9168 0.9189 1.1324 0.2427  -0.1960 -0.0553 44  ASN A CB  
634   C CG  . ASN A 44  ? 0.9726 0.9935 1.1972 0.2352  -0.1790 -0.0794 44  ASN A CG  
635   O OD1 . ASN A 44  ? 0.9187 0.9638 1.1372 0.2249  -0.1767 -0.0833 44  ASN A OD1 
636   N ND2 . ASN A 44  ? 1.1530 1.1639 1.3932 0.2377  -0.1659 -0.0966 44  ASN A ND2 
642   N N   . THR A 45  ? 0.7484 0.7850 0.9180 0.2269  -0.2252 -0.0175 45  THR A N   
643   C CA  . THR A 45  ? 0.7156 0.7672 0.8690 0.2222  -0.2432 0.0045  45  THR A CA  
644   C C   . THR A 45  ? 0.6815 0.7714 0.8599 0.2310  -0.2597 0.0093  45  THR A C   
645   O O   . THR A 45  ? 0.6647 0.7714 0.8731 0.2401  -0.2545 -0.0080 45  THR A O   
646   C CB  . THR A 45  ? 0.6944 0.7617 0.8158 0.2007  -0.2361 -0.0004 45  THR A CB  
647   O OG1 . THR A 45  ? 0.6532 0.7550 0.7855 0.1947  -0.2286 -0.0222 45  THR A OG1 
648   C CG2 . THR A 45  ? 0.6381 0.6724 0.7444 0.1926  -0.2202 -0.0056 45  THR A CG2 
656   N N   . THR A 46  ? 0.7210 0.8281 0.8864 0.2256  -0.2807 0.0349  46  THR A N   
657   C CA  . THR A 46  ? 0.8375 0.9876 1.0231 0.2295  -0.3013 0.0457  46  THR A CA  
658   C C   . THR A 46  ? 0.8768 1.0743 1.0454 0.2106  -0.2966 0.0271  46  THR A C   
659   O O   . THR A 46  ? 0.9380 1.1780 1.1207 0.2099  -0.3132 0.0328  46  THR A O   
660   C CB  . THR A 46  ? 0.8986 1.0514 1.0761 0.2270  -0.3294 0.0865  46  THR A CB  
661   O OG1 . THR A 46  ? 0.8832 1.0401 1.0083 0.2015  -0.3273 0.0941  46  THR A OG1 
662   C CG2 . THR A 46  ? 0.9527 1.0569 1.1595 0.2475  -0.3354 0.1045  46  THR A CG2 
670   N N   . GLN A 47  ? 0.8674 1.0592 1.0110 0.1950  -0.2751 0.0049  47  GLN A N   
671   C CA  . GLN A 47  ? 0.8006 1.0332 0.9347 0.1762  -0.2674 -0.0178 47  GLN A CA  
672   C C   . GLN A 47  ? 0.7495 1.0080 0.9196 0.1857  -0.2674 -0.0342 47  GLN A C   
673   O O   . GLN A 47  ? 0.7265 0.9630 0.9224 0.2000  -0.2554 -0.0458 47  GLN A O   
674   C CB  . GLN A 47  ? 0.7188 0.9325 0.8397 0.1636  -0.2421 -0.0407 47  GLN A CB  
675   C CG  . GLN A 47  ? 0.6285 0.8254 0.7156 0.1508  -0.2400 -0.0286 47  GLN A CG  
676   C CD  . GLN A 47  ? 0.5993 0.7726 0.6867 0.1436  -0.2164 -0.0479 47  GLN A CD  
677   O OE1 . GLN A 47  ? 0.5869 0.7215 0.6828 0.1545  -0.2099 -0.0438 47  GLN A OE1 
678   N NE2 . GLN A 47  ? 0.6046 0.8031 0.6865 0.1238  -0.2037 -0.0697 47  GLN A NE2 
687   N N   . PRO A 48  ? 0.7549 1.0635 0.9267 0.1755  -0.2801 -0.0360 48  PRO A N   
688   C CA  . PRO A 48  ? 0.7678 1.1045 0.9773 0.1843  -0.2816 -0.0501 48  PRO A CA  
689   C C   . PRO A 48  ? 0.7570 1.0824 0.9791 0.1810  -0.2552 -0.0825 48  PRO A C   
690   O O   . PRO A 48  ? 0.7705 1.1008 0.9769 0.1619  -0.2408 -0.1019 48  PRO A O   
691   C CB  . PRO A 48  ? 0.6268 1.0222 0.8247 0.1651  -0.2987 -0.0480 48  PRO A CB  
692   C CG  . PRO A 48  ? 0.6704 1.0677 0.8301 0.1526  -0.3146 -0.0203 48  PRO A CG  
693   C CD  . PRO A 48  ? 0.7389 1.0857 0.8771 0.1525  -0.2950 -0.0241 48  PRO A CD  
701   N N   . GLY A 49  ? 0.5595 0.8711 0.8140 0.1983  -0.2485 -0.0883 49  GLY A N   
702   C CA  . GLY A 49  ? 0.5340 0.8413 0.8039 0.1932  -0.2273 -0.1134 49  GLY A CA  
703   C C   . GLY A 49  ? 0.6194 0.8835 0.8742 0.1879  -0.2088 -0.1178 49  GLY A C   
704   O O   . GLY A 49  ? 0.6185 0.8788 0.8862 0.1804  -0.1934 -0.1336 49  GLY A O   
708   N N   . ILE A 50  ? 0.6290 0.8620 0.8592 0.1900  -0.2113 -0.1018 50  ILE A N   
709   C CA  . ILE A 50  ? 0.5638 0.7595 0.7808 0.1836  -0.1964 -0.1032 50  ILE A CA  
710   C C   . ILE A 50  ? 0.5629 0.7261 0.7842 0.1969  -0.1933 -0.0951 50  ILE A C   
711   O O   . ILE A 50  ? 0.5697 0.7211 0.7888 0.2099  -0.2041 -0.0805 50  ILE A O   
712   C CB  . ILE A 50  ? 0.6083 0.7943 0.7960 0.1736  -0.1984 -0.0943 50  ILE A CB  
713   C CG1 . ILE A 50  ? 0.6476 0.8716 0.8304 0.1564  -0.1984 -0.1088 50  ILE A CG1 
714   C CG2 . ILE A 50  ? 0.6373 0.7878 0.8192 0.1678  -0.1843 -0.0946 50  ILE A CG2 
715   C CD1 . ILE A 50  ? 0.6492 0.8883 0.8584 0.1469  -0.1846 -0.1343 50  ILE A CD1 
727   N N   . VAL A 51  ? 0.5824 0.7323 0.8112 0.1911  -0.1787 -0.1044 51  VAL A N   
728   C CA  . VAL A 51  ? 0.6241 0.7464 0.8513 0.1963  -0.1721 -0.1016 51  VAL A CA  
729   C C   . VAL A 51  ? 0.6249 0.7148 0.8291 0.1862  -0.1672 -0.0918 51  VAL A C   
730   O O   . VAL A 51  ? 0.5982 0.6887 0.8029 0.1726  -0.1615 -0.0936 51  VAL A O   
731   C CB  . VAL A 51  ? 0.6420 0.7780 0.8886 0.1911  -0.1601 -0.1164 51  VAL A CB  
732   C CG1 . VAL A 51  ? 0.6689 0.7819 0.9094 0.1915  -0.1512 -0.1177 51  VAL A CG1 
733   C CG2 . VAL A 51  ? 0.5020 0.6746 0.7764 0.2006  -0.1646 -0.1273 51  VAL A CG2 
743   N N   . GLU A 52  ? 0.6209 0.6828 0.8109 0.1926  -0.1698 -0.0817 52  GLU A N   
744   C CA  . GLU A 52  ? 0.6523 0.6845 0.8214 0.1828  -0.1661 -0.0717 52  GLU A CA  
745   C C   . GLU A 52  ? 0.6838 0.7201 0.8461 0.1731  -0.1671 -0.0669 52  GLU A C   
746   O O   . GLU A 52  ? 0.7041 0.7328 0.8690 0.1608  -0.1606 -0.0656 52  GLU A O   
747   C CB  . GLU A 52  ? 0.6622 0.6868 0.8318 0.1704  -0.1550 -0.0763 52  GLU A CB  
748   C CG  . GLU A 52  ? 0.7378 0.7577 0.9107 0.1757  -0.1493 -0.0863 52  GLU A CG  
749   C CD  . GLU A 52  ? 0.7757 0.7871 0.9361 0.1568  -0.1391 -0.0882 52  GLU A CD  
750   O OE1 . GLU A 52  ? 0.8034 0.8142 0.9578 0.1409  -0.1395 -0.0772 52  GLU A OE1 
751   O OE2 . GLU A 52  ? 0.7825 0.7899 0.9417 0.1564  -0.1309 -0.1007 52  GLU A OE2 
758   N N   . GLY A 53  ? 0.6349 0.6865 0.7918 0.1771  -0.1756 -0.0646 53  GLY A N   
759   C CA  . GLY A 53  ? 0.6347 0.6918 0.7825 0.1658  -0.1738 -0.0641 53  GLY A CA  
760   C C   . GLY A 53  ? 0.6419 0.6708 0.7706 0.1615  -0.1731 -0.0504 53  GLY A C   
761   O O   . GLY A 53  ? 0.5283 0.5598 0.6567 0.1504  -0.1671 -0.0528 53  GLY A O   
765   N N   . GLY A 54  ? 0.6512 0.6540 0.7686 0.1692  -0.1778 -0.0386 54  GLY A N   
766   C CA  . GLY A 54  ? 0.6616 0.6373 0.7602 0.1641  -0.1781 -0.0251 54  GLY A CA  
767   C C   . GLY A 54  ? 0.6817 0.6618 0.7608 0.1623  -0.1868 -0.0130 54  GLY A C   
768   O O   . GLY A 54  ? 0.6411 0.6500 0.7188 0.1613  -0.1921 -0.0156 54  GLY A O   
772   N N   . GLN A 55  ? 0.7408 0.6948 0.8025 0.1586  -0.1888 0.0014  55  GLN A N   
773   C CA  . GLN A 55  ? 0.7756 0.7329 0.8155 0.1529  -0.1974 0.0173  55  GLN A CA  
774   C C   . GLN A 55  ? 0.7505 0.6808 0.7750 0.1436  -0.1942 0.0286  55  GLN A C   
775   O O   . GLN A 55  ? 0.7450 0.6511 0.7750 0.1439  -0.1886 0.0266  55  GLN A O   
776   C CB  . GLN A 55  ? 0.8023 0.7561 0.8420 0.1656  -0.2143 0.0329  55  GLN A CB  
777   C CG  . GLN A 55  ? 0.8262 0.7440 0.8798 0.1795  -0.2160 0.0359  55  GLN A CG  
778   C CD  . GLN A 55  ? 0.8713 0.7892 0.9439 0.1960  -0.2316 0.0470  55  GLN A CD  
779   O OE1 . GLN A 55  ? 0.8811 0.8305 0.9562 0.1973  -0.2432 0.0539  55  GLN A OE1 
780   N NE2 . GLN A 55  ? 0.8625 0.7467 0.9527 0.2078  -0.2320 0.0480  55  GLN A NE2 
789   N N   . VAL A 56  ? 0.7846 0.7237 0.7880 0.1319  -0.1978 0.0408  56  VAL A N   
790   C CA  . VAL A 56  ? 0.7522 0.6691 0.7389 0.1211  -0.1964 0.0544  56  VAL A CA  
791   C C   . VAL A 56  ? 0.7824 0.6809 0.7526 0.1238  -0.2129 0.0805  56  VAL A C   
792   O O   . VAL A 56  ? 0.8033 0.7232 0.7663 0.1238  -0.2250 0.0913  56  VAL A O   
793   C CB  . VAL A 56  ? 0.7136 0.6577 0.6928 0.1019  -0.1850 0.0470  56  VAL A CB  
794   C CG1 . VAL A 56  ? 0.7285 0.6535 0.6907 0.0893  -0.1839 0.0625  56  VAL A CG1 
795   C CG2 . VAL A 56  ? 0.6601 0.6182 0.6692 0.1012  -0.1699 0.0231  56  VAL A CG2 
805   N N   . LEU A 57  ? 0.7841 0.6438 0.7510 0.1244  -0.2147 0.0920  57  LEU A N   
806   C CA  . LEU A 57  ? 0.8262 0.6599 0.7873 0.1279  -0.2305 0.1178  57  LEU A CA  
807   C C   . LEU A 57  ? 0.8147 0.6359 0.7516 0.1088  -0.2307 0.1360  57  LEU A C   
808   O O   . LEU A 57  ? 0.7977 0.6108 0.7308 0.0990  -0.2180 0.1267  57  LEU A O   
809   C CB  . LEU A 57  ? 0.8566 0.6508 0.8408 0.1447  -0.2319 0.1134  57  LEU A CB  
810   C CG  . LEU A 57  ? 0.8342 0.6380 0.8466 0.1641  -0.2320 0.0966  57  LEU A CG  
811   C CD1 . LEU A 57  ? 0.8110 0.6201 0.8295 0.1629  -0.2150 0.0693  57  LEU A CD1 
812   C CD2 . LEU A 57  ? 0.8477 0.6181 0.8872 0.1805  -0.2412 0.1037  57  LEU A CD2 
824   N N   . LYS A 58  ? 0.8323 0.6544 0.7546 0.1020  -0.2465 0.1646  58  LYS A N   
825   C CA  . LYS A 58  ? 0.8993 0.7049 0.7995 0.0832  -0.2499 0.1878  58  LYS A CA  
826   C C   . LYS A 58  ? 0.9609 0.7134 0.8784 0.0945  -0.2618 0.2058  58  LYS A C   
827   O O   . LYS A 58  ? 0.9774 0.7189 0.9182 0.1117  -0.2767 0.2167  58  LYS A O   
828   C CB  . LYS A 58  ? 0.9486 0.7905 0.8203 0.0634  -0.2609 0.2113  58  LYS A CB  
829   C CG  . LYS A 58  ? 1.0565 0.8884 0.9014 0.0388  -0.2634 0.2368  58  LYS A CG  
830   C CD  . LYS A 58  ? 1.1364 1.0219 0.9454 0.0101  -0.2632 0.2455  58  LYS A CD  
831   C CE  . LYS A 58  ? 1.2115 1.1146 1.0101 0.0066  -0.2897 0.2793  58  LYS A CE  
832   N NZ  . LYS A 58  ? 1.2366 1.2058 1.0016 -0.0201 -0.2859 0.2736  58  LYS A NZ  
846   N N   . CYS A 59  ? 1.0025 0.7233 0.9143 0.0846  -0.2548 0.2071  59  CYS A N   
847   C CA  . CYS A 59  ? 1.1077 0.7749 1.0399 0.0932  -0.2612 0.2156  59  CYS A CA  
848   C C   . CYS A 59  ? 1.2041 0.8493 1.1187 0.0731  -0.2698 0.2470  59  CYS A C   
849   O O   . CYS A 59  ? 1.2193 0.8760 1.1088 0.0519  -0.2594 0.2458  59  CYS A O   
850   C CB  . CYS A 59  ? 1.0923 0.7382 1.0358 0.0974  -0.2442 0.1842  59  CYS A CB  
851   S SG  . CYS A 59  ? 1.0812 0.7507 1.0448 0.1168  -0.2336 0.1492  59  CYS A SG  
856   N N   . ASP A 60  ? 1.2678 0.8820 1.2012 0.0796  -0.2890 0.2761  60  ASP A N   
857   C CA  . ASP A 60  ? 1.3391 0.9244 1.2618 0.0606  -0.2990 0.3091  60  ASP A CA  
858   C C   . ASP A 60  ? 1.3760 0.9230 1.3009 0.0533  -0.2836 0.2903  60  ASP A C   
859   O O   . ASP A 60  ? 1.2995 0.8266 1.2466 0.0678  -0.2720 0.2585  60  ASP A O   
860   C CB  . ASP A 60  ? 1.3674 0.9187 1.3248 0.0728  -0.3240 0.3439  60  ASP A CB  
861   C CG  . ASP A 60  ? 1.4026 0.9945 1.3587 0.0769  -0.3443 0.3692  60  ASP A CG  
862   O OD1 . ASP A 60  ? 1.3896 1.0344 1.3182 0.0719  -0.3359 0.3528  60  ASP A OD1 
863   O OD2 . ASP A 60  ? 1.4688 1.0529 1.4544 0.0826  -0.3575 0.3942  60  ASP A OD2 
868   N N   . TRP A 61  ? 1.5075 1.0477 1.4077 0.0274  -0.2836 0.3099  61  TRP A N   
869   C CA  . TRP A 61  ? 1.6200 1.1220 1.5231 0.0168  -0.2728 0.2980  61  TRP A CA  
870   C C   . TRP A 61  ? 1.8279 1.2719 1.7576 0.0175  -0.2880 0.3243  61  TRP A C   
871   O O   . TRP A 61  ? 2.0352 1.4743 1.9531 0.0006  -0.3029 0.3646  61  TRP A O   
872   C CB  . TRP A 61  ? 1.5302 1.0581 1.3981 -0.0123 -0.2620 0.3006  61  TRP A CB  
873   C CG  . TRP A 61  ? 1.4353 0.9225 1.3080 -0.0253 -0.2551 0.2938  61  TRP A CG  
874   C CD1 . TRP A 61  ? 1.3810 0.8484 1.2688 -0.0188 -0.2432 0.2608  61  TRP A CD1 
875   C CD2 . TRP A 61  ? 1.3985 0.8620 1.2598 -0.0504 -0.2602 0.3208  61  TRP A CD2 
876   N NE1 . TRP A 61  ? 1.3898 0.8234 1.2761 -0.0382 -0.2405 0.2634  61  TRP A NE1 
877   C CE2 . TRP A 61  ? 1.3953 0.8241 1.2673 -0.0568 -0.2505 0.3000  61  TRP A CE2 
878   C CE3 . TRP A 61  ? 1.3825 0.8537 1.2234 -0.0715 -0.2720 0.3611  61  TRP A CE3 
879   C CZ2 . TRP A 61  ? 1.4160 0.8151 1.2823 -0.0815 -0.2519 0.3167  61  TRP A CZ2 
880   C CZ3 . TRP A 61  ? 1.4106 0.8519 1.2452 -0.0963 -0.2735 0.3799  61  TRP A CZ3 
881   C CH2 . TRP A 61  ? 1.4313 0.8357 1.2803 -0.1000 -0.2633 0.3570  61  TRP A CH2 
892   N N   . SER A 62  ? 1.7988 1.2005 1.7672 0.0355  -0.2836 0.3010  62  SER A N   
893   C CA  . SER A 62  ? 1.9827 1.3219 1.9854 0.0347  -0.2912 0.3138  62  SER A CA  
894   C C   . SER A 62  ? 2.0583 1.3980 2.0927 0.0455  -0.3069 0.3460  62  SER A C   
895   O O   . SER A 62  ? 2.1039 1.4068 2.1877 0.0585  -0.3056 0.3399  62  SER A O   
896   C CB  . SER A 62  ? 2.1018 1.4251 2.0774 0.0032  -0.2873 0.3266  62  SER A CB  
897   O OG  . SER A 62  ? 2.2082 1.4759 2.2199 0.0015  -0.2869 0.3264  62  SER A OG  
903   N N   . SER A 63  ? 2.0214 1.4059 2.0294 0.0380  -0.3203 0.3783  63  SER A N   
904   C CA  . SER A 63  ? 2.0489 1.4426 2.0857 0.0468  -0.3368 0.4089  63  SER A CA  
905   C C   . SER A 63  ? 1.9962 1.3721 2.0932 0.0804  -0.3345 0.3855  63  SER A C   
906   O O   . SER A 63  ? 2.0491 1.4012 2.1936 0.0901  -0.3421 0.3995  63  SER A O   
907   C CB  . SER A 63  ? 2.0216 1.4754 2.0202 0.0369  -0.3499 0.4347  63  SER A CB  
908   O OG  . SER A 63  ? 1.9916 1.4643 1.9418 0.0025  -0.3531 0.4620  63  SER A OG  
914   N N   . THR A 64  ? 1.8557 1.2444 1.9532 0.0972  -0.3237 0.3494  64  THR A N   
915   C CA  . THR A 64  ? 1.8808 1.2624 2.0326 0.1273  -0.3190 0.3232  64  THR A CA  
916   C C   . THR A 64  ? 1.7295 1.1061 1.8778 0.1367  -0.3005 0.2747  64  THR A C   
917   O O   . THR A 64  ? 1.6853 1.0420 1.8793 0.1555  -0.2890 0.2423  64  THR A O   
918   C CB  . THR A 64  ? 1.9137 1.3419 2.0736 0.1402  -0.3344 0.3430  64  THR A CB  
919   O OG1 . THR A 64  ? 1.7395 1.2086 1.8619 0.1409  -0.3309 0.3270  64  THR A OG1 
920   C CG2 . THR A 64  ? 2.0836 1.5316 2.2239 0.1213  -0.3556 0.3946  64  THR A CG2 
928   N N   . ARG A 65  ? 1.6915 1.0880 1.7870 0.1221  -0.2974 0.2691  65  ARG A N   
929   C CA  . ARG A 65  ? 1.6499 1.0672 1.7316 0.1263  -0.2763 0.2235  65  ARG A CA  
930   C C   . ARG A 65  ? 1.5919 1.0480 1.6886 0.1482  -0.2781 0.2120  65  ARG A C   
931   O O   . ARG A 65  ? 1.5459 1.0114 1.6528 0.1579  -0.2611 0.1730  65  ARG A O   
932   C CB  . ARG A 65  ? 1.6932 1.0701 1.8003 0.1274  -0.2576 0.1845  65  ARG A CB  
933   C CG  . ARG A 65  ? 1.7146 1.0637 1.7967 0.1008  -0.2501 0.1841  65  ARG A CG  
934   C CD  . ARG A 65  ? 1.6901 1.0334 1.7674 0.0922  -0.2264 0.1363  65  ARG A CD  
935   N NE  . ARG A 65  ? 1.7347 1.0611 1.8589 0.1116  -0.2162 0.1017  65  ARG A NE  
936   C CZ  . ARG A 65  ? 1.8208 1.1316 1.9521 0.1023  -0.1957 0.0585  65  ARG A CZ  
937   N NH1 . ARG A 65  ? 1.8099 1.1187 1.9040 0.0741  -0.1863 0.0481  65  ARG A NH1 
938   N NH2 . ARG A 65  ? 1.9036 1.2043 2.0805 0.1192  -0.1841 0.0245  65  ARG A NH2 
952   N N   . ARG A 66  ? 1.5902 1.0726 1.6861 0.1530  -0.2988 0.2461  66  ARG A N   
953   C CA  . ARG A 66  ? 1.5366 1.0587 1.6470 0.1716  -0.3032 0.2387  66  ARG A CA  
954   C C   . ARG A 66  ? 1.3823 0.9595 1.4423 0.1583  -0.2953 0.2307  66  ARG A C   
955   O O   . ARG A 66  ? 1.3937 0.9854 1.4117 0.1355  -0.2957 0.2469  66  ARG A O   
956   C CB  . ARG A 66  ? 1.6447 1.1811 1.7829 0.1791  -0.3228 0.2741  66  ARG A CB  
957   C CG  . ARG A 66  ? 1.7577 1.2578 1.9584 0.1946  -0.3206 0.2715  66  ARG A CG  
958   C CD  . ARG A 66  ? 1.8458 1.3706 2.0805 0.2056  -0.3388 0.3007  66  ARG A CD  
959   N NE  . ARG A 66  ? 1.9986 1.5427 2.2005 0.1847  -0.3596 0.3489  66  ARG A NE  
960   C CZ  . ARG A 66  ? 2.1528 1.6702 2.3682 0.1746  -0.3700 0.3804  66  ARG A CZ  
961   N NH1 . ARG A 66  ? 2.2325 1.7001 2.4963 0.1847  -0.3614 0.3679  66  ARG A NH1 
962   N NH2 . ARG A 66  ? 2.2027 1.7450 2.3833 0.1522  -0.3889 0.4233  66  ARG A NH2 
976   N N   . CYS A 67  ? 1.4096 0.6726 1.4117 0.1537  -0.1985 0.0528  67  CYS A N   
977   C CA  . CYS A 67  ? 1.3014 0.6311 1.2919 0.1421  -0.1927 0.0593  67  CYS A CA  
978   C C   . CYS A 67  ? 1.2807 0.6417 1.2848 0.1659  -0.2027 0.0762  67  CYS A C   
979   O O   . CYS A 67  ? 1.2779 0.6393 1.3107 0.1967  -0.2061 0.0653  67  CYS A O   
980   C CB  . CYS A 67  ? 1.2383 0.6132 1.2321 0.1389  -0.1765 0.0263  67  CYS A CB  
981   S SG  . CYS A 67  ? 1.2939 0.6437 1.2723 0.1094  -0.1672 0.0040  67  CYS A SG  
986   N N   . GLN A 68  ? 1.2842 0.6734 1.2691 0.1510  -0.2069 0.1013  68  GLN A N   
987   C CA  . GLN A 68  ? 1.3023 0.7259 1.2958 0.1683  -0.2177 0.1178  68  GLN A CA  
988   C C   . GLN A 68  ? 1.1988 0.6850 1.1796 0.1528  -0.2082 0.1163  68  GLN A C   
989   O O   . GLN A 68  ? 1.2295 0.7202 1.1853 0.1244  -0.2003 0.1215  68  GLN A O   
990   C CB  . GLN A 68  ? 1.3883 0.7739 1.3669 0.1668  -0.2377 0.1555  68  GLN A CB  
991   C CG  . GLN A 68  ? 1.4693 0.8158 1.4740 0.1947  -0.2495 0.1595  68  GLN A CG  
992   C CD  . GLN A 68  ? 1.5779 0.8947 1.5634 0.1862  -0.2618 0.1955  68  GLN A CD  
993   O OE1 . GLN A 68  ? 1.6215 0.9479 1.5744 0.1647  -0.2675 0.2206  68  GLN A OE1 
994   N NE2 . GLN A 68  ? 1.6651 0.9450 1.6693 0.2029  -0.2651 0.1979  68  GLN A NE2 
1003  N N   . PRO A 69  ? 1.0703 0.6055 1.0703 0.1705  -0.2078 0.1084  69  PRO A N   
1004  C CA  . PRO A 69  ? 0.9711 0.5617 0.9607 0.1559  -0.1980 0.1048  69  PRO A CA  
1005  C C   . PRO A 69  ? 0.9600 0.5556 0.9208 0.1359  -0.2052 0.1321  69  PRO A C   
1006  O O   . PRO A 69  ? 1.0227 0.5985 0.9768 0.1415  -0.2224 0.1565  69  PRO A O   
1007  C CB  . PRO A 69  ? 0.9416 0.5758 0.9609 0.1804  -0.1989 0.0936  69  PRO A CB  
1008  C CG  . PRO A 69  ? 0.9824 0.5890 1.0304 0.2069  -0.2022 0.0811  69  PRO A CG  
1009  C CD  . PRO A 69  ? 1.0419 0.5856 1.0778 0.2041  -0.2147 0.0997  69  PRO A CD  
1017  N N   . ILE A 70  ? 0.9269 0.5494 0.8701 0.1125  -0.1920 0.1277  70  ILE A N   
1018  C CA  . ILE A 70  ? 0.9665 0.6033 0.8822 0.0924  -0.1940 0.1474  70  ILE A CA  
1019  C C   . ILE A 70  ? 1.0453 0.7313 0.9693 0.1018  -0.1972 0.1457  70  ILE A C   
1020  O O   . ILE A 70  ? 1.0377 0.7589 0.9797 0.1078  -0.1865 0.1250  70  ILE A O   
1021  C CB  . ILE A 70  ? 0.8703 0.5155 0.7693 0.0644  -0.1770 0.1409  70  ILE A CB  
1022  C CG1 . ILE A 70  ? 0.8352 0.4331 0.7275 0.0521  -0.1749 0.1430  70  ILE A CG1 
1023  C CG2 . ILE A 70  ? 0.8367 0.5015 0.7082 0.0441  -0.1754 0.1569  70  ILE A CG2 
1024  C CD1 . ILE A 70  ? 0.8146 0.4250 0.6994 0.0261  -0.1587 0.1337  70  ILE A CD1 
1036  N N   . GLU A 71  ? 1.1590 0.8467 1.0680 0.1013  -0.2125 0.1681  71  GLU A N   
1037  C CA  . GLU A 71  ? 1.2007 0.9348 1.1159 0.1073  -0.2179 0.1672  71  GLU A CA  
1038  C C   . GLU A 71  ? 1.1766 0.9390 1.0674 0.0816  -0.2041 0.1634  71  GLU A C   
1039  O O   . GLU A 71  ? 1.2129 0.9725 1.0715 0.0642  -0.2087 0.1806  71  GLU A O   
1040  C CB  . GLU A 71  ? 1.2882 1.0143 1.1980 0.1178  -0.2430 0.1923  71  GLU A CB  
1041  C CG  . GLU A 71  ? 1.3408 1.1171 1.2602 0.1236  -0.2514 0.1904  71  GLU A CG  
1042  C CD  . GLU A 71  ? 1.4690 1.2404 1.3786 0.1309  -0.2794 0.2178  71  GLU A CD  
1043  O OE1 . GLU A 71  ? 1.5846 1.3206 1.5064 0.1491  -0.2954 0.2323  71  GLU A OE1 
1044  O OE2 . GLU A 71  ? 1.5196 1.3216 1.4090 0.1183  -0.2864 0.2247  71  GLU A OE2 
1051  N N   . PHE A 72  ? 1.1053 0.8944 1.0109 0.0792  -0.1865 0.1403  72  PHE A N   
1052  C CA  . PHE A 72  ? 1.0141 0.8336 0.9053 0.0598  -0.1735 0.1334  72  PHE A CA  
1053  C C   . PHE A 72  ? 0.9803 0.8374 0.8764 0.0645  -0.1805 0.1318  72  PHE A C   
1054  O O   . PHE A 72  ? 1.0120 0.8844 0.8845 0.0479  -0.1795 0.1363  72  PHE A O   
1055  C CB  . PHE A 72  ? 0.9115 0.7433 0.8181 0.0564  -0.1545 0.1118  72  PHE A CB  
1056  C CG  . PHE A 72  ? 0.8834 0.6880 0.7816 0.0433  -0.1457 0.1116  72  PHE A CG  
1057  C CD1 . PHE A 72  ? 0.8849 0.6941 0.7646 0.0204  -0.1344 0.1138  72  PHE A CD1 
1058  C CD2 . PHE A 72  ? 0.8829 0.6597 0.7936 0.0531  -0.1478 0.1071  72  PHE A CD2 
1059  C CE1 . PHE A 72  ? 0.9040 0.6933 0.7807 0.0070  -0.1263 0.1131  72  PHE A CE1 
1060  C CE2 . PHE A 72  ? 0.9080 0.6616 0.8125 0.0388  -0.1407 0.1059  72  PHE A CE2 
1061  C CZ  . PHE A 72  ? 0.9045 0.6659 0.7935 0.0155  -0.1304 0.1096  72  PHE A CZ  
1071  N N   . ASP A 73  ? 0.9112 0.7848 0.8382 0.0857  -0.1867 0.1237  73  ASP A N   
1072  C CA  . ASP A 73  ? 0.8416 0.7549 0.7805 0.0898  -0.1928 0.1196  73  ASP A CA  
1073  C C   . ASP A 73  ? 0.8487 0.7687 0.8215 0.1160  -0.2061 0.1197  73  ASP A C   
1074  O O   . ASP A 73  ? 0.8786 0.7955 0.8765 0.1298  -0.1973 0.1059  73  ASP A O   
1075  C CB  . ASP A 73  ? 0.8244 0.7667 0.7731 0.0817  -0.1740 0.0989  73  ASP A CB  
1076  C CG  . ASP A 73  ? 0.8542 0.8348 0.8281 0.0905  -0.1781 0.0902  73  ASP A CG  
1077  O OD1 . ASP A 73  ? 0.8908 0.8870 0.8616 0.0909  -0.1945 0.0999  73  ASP A OD1 
1078  O OD2 . ASP A 73  ? 0.8370 0.8333 0.8330 0.0953  -0.1653 0.0743  73  ASP A OD2 
1083  N N   . ALA A 74  ? 0.8703 0.8013 0.8442 0.1226  -0.2273 0.1344  74  ALA A N   
1084  C CA  . ALA A 74  ? 0.8723 0.8124 0.8835 0.1493  -0.2424 0.1363  74  ALA A CA  
1085  C C   . ALA A 74  ? 0.8363 0.8287 0.8785 0.1550  -0.2426 0.1229  74  ALA A C   
1086  O O   . ALA A 74  ? 0.8416 0.8506 0.9219 0.1775  -0.2529 0.1214  74  ALA A O   
1087  C CB  . ALA A 74  ? 0.8945 0.8142 0.8932 0.1559  -0.2697 0.1638  74  ALA A CB  
1093  N N   . THR A 75  ? 0.7742 0.7927 0.8041 0.1353  -0.2306 0.1123  75  THR A N   
1094  C CA  . THR A 75  ? 0.7378 0.8046 0.7923 0.1350  -0.2326 0.1020  75  THR A CA  
1095  C C   . THR A 75  ? 0.7125 0.7975 0.7951 0.1390  -0.2105 0.0798  75  THR A C   
1096  O O   . THR A 75  ? 0.7414 0.8035 0.8167 0.1373  -0.1930 0.0716  75  THR A O   
1097  C CB  . THR A 75  ? 0.7474 0.8301 0.7709 0.1095  -0.2332 0.1026  75  THR A CB  
1098  O OG1 . THR A 75  ? 0.7468 0.8219 0.7555 0.0933  -0.2087 0.0883  75  THR A OG1 
1099  C CG2 . THR A 75  ? 0.7685 0.8278 0.7514 0.0999  -0.2500 0.1244  75  THR A CG2 
1107  N N   . GLY A 76  ? 0.6537 0.7819 0.7681 0.1428  -0.2124 0.0709  76  GLY A N   
1108  C CA  . GLY A 76  ? 0.6312 0.7820 0.7684 0.1413  -0.1915 0.0517  76  GLY A CA  
1109  C C   . GLY A 76  ? 0.6195 0.7802 0.7372 0.1165  -0.1793 0.0442  76  GLY A C   
1110  O O   . GLY A 76  ? 0.6537 0.7927 0.7360 0.1011  -0.1785 0.0494  76  GLY A O   
1114  N N   . ASN A 77  ? 0.5809 0.7744 0.7234 0.1122  -0.1686 0.0312  77  ASN A N   
1115  C CA  . ASN A 77  ? 0.5792 0.7785 0.7081 0.0899  -0.1555 0.0227  77  ASN A CA  
1116  C C   . ASN A 77  ? 0.6889 0.9106 0.8116 0.0750  -0.1697 0.0244  77  ASN A C   
1117  O O   . ASN A 77  ? 0.7277 0.9840 0.8769 0.0800  -0.1839 0.0251  77  ASN A O   
1118  C CB  . ASN A 77  ? 0.5193 0.7402 0.6746 0.0888  -0.1376 0.0096  77  ASN A CB  
1119  C CG  . ASN A 77  ? 0.5730 0.7706 0.7247 0.0979  -0.1215 0.0060  77  ASN A CG  
1120  O OD1 . ASN A 77  ? 0.5928 0.7556 0.7192 0.0991  -0.1206 0.0110  77  ASN A OD1 
1121  N ND2 . ASN A 77  ? 0.5961 0.8146 0.7722 0.1024  -0.1085 -0.0032 77  ASN A ND2 
1128  N N   . ARG A 78  ? 0.7219 0.9260 0.8107 0.0564  -0.1658 0.0237  78  ARG A N   
1129  C CA  . ARG A 78  ? 0.6797 0.9044 0.7590 0.0379  -0.1746 0.0198  78  ARG A CA  
1130  C C   . ARG A 78  ? 0.6466 0.9015 0.7549 0.0286  -0.1653 0.0056  78  ARG A C   
1131  O O   . ARG A 78  ? 0.6461 0.8972 0.7699 0.0309  -0.1470 -0.0010 78  ARG A O   
1132  C CB  . ARG A 78  ? 0.6717 0.8698 0.7103 0.0199  -0.1664 0.0173  78  ARG A CB  
1133  C CG  . ARG A 78  ? 0.6973 0.8736 0.7021 0.0211  -0.1786 0.0320  78  ARG A CG  
1134  C CD  . ARG A 78  ? 0.6794 0.8324 0.6483 0.0033  -0.1650 0.0267  78  ARG A CD  
1135  N NE  . ARG A 78  ? 0.6653 0.7926 0.6372 0.0084  -0.1454 0.0234  78  ARG A NE  
1136  C CZ  . ARG A 78  ? 0.6696 0.7753 0.6180 -0.0019 -0.1323 0.0203  78  ARG A CZ  
1137  N NH1 . ARG A 78  ? 0.6660 0.7712 0.5831 -0.0184 -0.1340 0.0188  78  ARG A NH1 
1138  N NH2 . ARG A 78  ? 0.6697 0.7568 0.6261 0.0039  -0.1175 0.0180  78  ARG A NH2 
1152  N N   . ASP A 79  ? 0.6590 0.9442 0.7730 0.0160  -0.1786 0.0017  79  ASP A N   
1153  C CA  . ASP A 79  ? 0.6320 0.9475 0.7737 0.0029  -0.1716 -0.0118 79  ASP A CA  
1154  C C   . ASP A 79  ? 0.6337 0.9378 0.7500 -0.0228 -0.1641 -0.0236 79  ASP A C   
1155  O O   . ASP A 79  ? 0.6718 0.9699 0.7568 -0.0330 -0.1756 -0.0228 79  ASP A O   
1156  C CB  . ASP A 79  ? 0.5979 0.9616 0.7724 0.0063  -0.1930 -0.0103 79  ASP A CB  
1157  C CG  . ASP A 79  ? 0.6170 1.0017 0.8341 0.0299  -0.1922 -0.0066 79  ASP A CG  
1158  O OD1 . ASP A 79  ? 0.6234 0.9855 0.8419 0.0409  -0.1737 -0.0070 79  ASP A OD1 
1159  O OD2 . ASP A 79  ? 0.6593 1.0851 0.9098 0.0375  -0.2104 -0.0044 79  ASP A OD2 
1164  N N   . TYR A 80  ? 0.6270 0.9261 0.7553 -0.0336 -0.1442 -0.0348 80  TYR A N   
1165  C CA  . TYR A 80  ? 0.6928 0.9866 0.8084 -0.0585 -0.1381 -0.0493 80  TYR A CA  
1166  C C   . TYR A 80  ? 0.7032 1.0393 0.8408 -0.0732 -0.1518 -0.0575 80  TYR A C   
1167  O O   . TYR A 80  ? 0.7213 1.0598 0.8407 -0.0936 -0.1579 -0.0685 80  TYR A O   
1168  C CB  . TYR A 80  ? 0.7143 0.9832 0.8361 -0.0644 -0.1136 -0.0560 80  TYR A CB  
1169  C CG  . TYR A 80  ? 0.7092 0.9717 0.8266 -0.0893 -0.1064 -0.0724 80  TYR A CG  
1170  C CD1 . TYR A 80  ? 0.7086 0.9406 0.7953 -0.0986 -0.1002 -0.0810 80  TYR A CD1 
1171  C CD2 . TYR A 80  ? 0.7106 0.9975 0.8563 -0.1044 -0.1045 -0.0806 80  TYR A CD2 
1172  C CE1 . TYR A 80  ? 0.7190 0.9417 0.8028 -0.1206 -0.0926 -0.0988 80  TYR A CE1 
1173  C CE2 . TYR A 80  ? 0.7166 0.9932 0.8587 -0.1284 -0.0979 -0.0967 80  TYR A CE2 
1174  C CZ  . TYR A 80  ? 0.7297 0.9726 0.8405 -0.1357 -0.0921 -0.1064 80  TYR A CZ  
1175  O OH  . TYR A 80  ? 0.7789 1.0082 0.8872 -0.1589 -0.0845 -0.1251 80  TYR A OH  
1185  N N   . ALA A 81  ? 0.6771 1.0486 0.8548 -0.0640 -0.1560 -0.0538 81  ALA A N   
1186  C CA  . ALA A 81  ? 0.6883 1.1087 0.8964 -0.0754 -0.1711 -0.0602 81  ALA A CA  
1187  C C   . ALA A 81  ? 0.6868 1.1422 0.9366 -0.0528 -0.1776 -0.0510 81  ALA A C   
1188  O O   . ALA A 81  ? 0.7156 1.1526 0.9671 -0.0318 -0.1675 -0.0426 81  ALA A O   
1189  C CB  . ALA A 81  ? 0.7316 1.1570 0.9549 -0.1010 -0.1558 -0.0759 81  ALA A CB  
1195  N N   . LYS A 82  ? 0.6925 1.1997 0.9779 -0.0572 -0.1946 -0.0542 82  LYS A N   
1196  C CA  . LYS A 82  ? 0.7252 1.2707 1.0575 -0.0345 -0.2002 -0.0479 82  LYS A CA  
1197  C C   . LYS A 82  ? 0.7136 1.2554 1.0687 -0.0307 -0.1706 -0.0524 82  LYS A C   
1198  O O   . LYS A 82  ? 0.7244 1.2691 1.0870 -0.0528 -0.1534 -0.0625 82  LYS A O   
1199  C CB  . LYS A 82  ? 0.8026 1.4108 1.1769 -0.0427 -0.2218 -0.0528 82  LYS A CB  
1200  C CG  . LYS A 82  ? 0.8402 1.4871 1.2578 -0.0132 -0.2394 -0.0429 82  LYS A CG  
1201  C CD  . LYS A 82  ? 0.8776 1.5955 1.3530 -0.0210 -0.2537 -0.0506 82  LYS A CD  
1202  C CE  . LYS A 82  ? 0.9037 1.6596 1.4176 0.0086  -0.2817 -0.0388 82  LYS A CE  
1203  N NZ  . LYS A 82  ? 0.9538 1.6960 1.4295 0.0112  -0.3157 -0.0244 82  LYS A NZ  
1217  N N   . ASP A 83  ? 0.7526 1.2854 1.1158 -0.0038 -0.1646 -0.0447 83  ASP A N   
1218  C CA  . ASP A 83  ? 0.7923 1.3200 1.1698 0.0009  -0.1368 -0.0484 83  ASP A CA  
1219  C C   . ASP A 83  ? 0.8218 1.3006 1.1599 -0.0151 -0.1159 -0.0498 83  ASP A C   
1220  O O   . ASP A 83  ? 0.8159 1.2939 1.1625 -0.0242 -0.0934 -0.0538 83  ASP A O   
1221  C CB  . ASP A 83  ? 0.7997 1.3838 1.2301 -0.0082 -0.1285 -0.0582 83  ASP A CB  
1222  C CG  . ASP A 83  ? 0.9252 1.5629 1.4039 0.0109  -0.1489 -0.0575 83  ASP A CG  
1223  O OD1 . ASP A 83  ? 0.9784 1.6113 1.4659 0.0400  -0.1517 -0.0519 83  ASP A OD1 
1224  O OD2 . ASP A 83  ? 0.9633 1.6476 1.4728 -0.0031 -0.1631 -0.0629 83  ASP A OD2 
1229  N N   . ASP A 84  ? 0.7770 1.2153 1.0724 -0.0186 -0.1232 -0.0457 84  ASP A N   
1230  C CA  . ASP A 84  ? 0.6750 1.0666 0.9361 -0.0309 -0.1060 -0.0469 84  ASP A CA  
1231  C C   . ASP A 84  ? 0.6409 0.9921 0.8648 -0.0171 -0.1116 -0.0385 84  ASP A C   
1232  O O   . ASP A 84  ? 0.6374 0.9720 0.8338 -0.0257 -0.1212 -0.0391 84  ASP A O   
1233  C CB  . ASP A 84  ? 0.6751 1.0649 0.9287 -0.0592 -0.1060 -0.0570 84  ASP A CB  
1234  C CG  . ASP A 84  ? 0.6717 1.0204 0.9063 -0.0718 -0.0848 -0.0594 84  ASP A CG  
1235  O OD1 . ASP A 84  ? 0.6328 0.9484 0.8485 -0.0585 -0.0752 -0.0519 84  ASP A OD1 
1236  O OD2 . ASP A 84  ? 0.6502 0.9990 0.8902 -0.0951 -0.0789 -0.0686 84  ASP A OD2 
1241  N N   . PRO A 85  ? 0.5850 0.9202 0.8062 0.0029  -0.1049 -0.0317 85  PRO A N   
1242  C CA  . PRO A 85  ? 0.5815 0.8813 0.7713 0.0153  -0.1113 -0.0233 85  PRO A CA  
1243  C C   . PRO A 85  ? 0.5519 0.8131 0.7087 0.0024  -0.1014 -0.0249 85  PRO A C   
1244  O O   . PRO A 85  ? 0.5270 0.7768 0.6844 -0.0082 -0.0852 -0.0295 85  PRO A O   
1245  C CB  . PRO A 85  ? 0.5913 0.8837 0.7896 0.0361  -0.1028 -0.0194 85  PRO A CB  
1246  C CG  . PRO A 85  ? 0.5635 0.8968 0.8015 0.0383  -0.0966 -0.0255 85  PRO A CG  
1247  C CD  . PRO A 85  ? 0.5433 0.8932 0.7894 0.0137  -0.0907 -0.0326 85  PRO A CD  
1255  N N   . LEU A 86  ? 0.5627 0.8036 0.6914 0.0035  -0.1112 -0.0205 86  LEU A N   
1256  C CA  . LEU A 86  ? 0.5707 0.7772 0.6715 -0.0059 -0.1011 -0.0231 86  LEU A CA  
1257  C C   . LEU A 86  ? 0.5682 0.7466 0.6612 0.0067  -0.0903 -0.0171 86  LEU A C   
1258  O O   . LEU A 86  ? 0.5690 0.7244 0.6526 0.0005  -0.0777 -0.0200 86  LEU A O   
1259  C CB  . LEU A 86  ? 0.6099 0.8092 0.6824 -0.0117 -0.1135 -0.0215 86  LEU A CB  
1260  C CG  . LEU A 86  ? 0.6290 0.7979 0.6743 -0.0219 -0.1023 -0.0268 86  LEU A CG  
1261  C CD1 . LEU A 86  ? 0.6368 0.8047 0.6870 -0.0399 -0.0911 -0.0416 86  LEU A CD1 
1262  C CD2 . LEU A 86  ? 0.6578 0.8224 0.6723 -0.0262 -0.1140 -0.0227 86  LEU A CD2 
1274  N N   . GLU A 87  ? 0.5837 0.7637 0.6824 0.0244  -0.0958 -0.0096 87  GLU A N   
1275  C CA  . GLU A 87  ? 0.5703 0.7240 0.6590 0.0355  -0.0887 -0.0048 87  GLU A CA  
1276  C C   . GLU A 87  ? 0.5751 0.7411 0.6834 0.0513  -0.0877 -0.0038 87  GLU A C   
1277  O O   . GLU A 87  ? 0.5935 0.7890 0.7251 0.0561  -0.0936 -0.0057 87  GLU A O   
1278  C CB  . GLU A 87  ? 0.5929 0.7244 0.6575 0.0387  -0.0972 0.0022  87  GLU A CB  
1279  C CG  . GLU A 87  ? 0.6300 0.7738 0.6943 0.0451  -0.1159 0.0093  87  GLU A CG  
1280  C CD  . GLU A 87  ? 0.6531 0.7749 0.6873 0.0412  -0.1232 0.0175  87  GLU A CD  
1281  O OE1 . GLU A 87  ? 0.6511 0.7533 0.6678 0.0319  -0.1123 0.0146  87  GLU A OE1 
1282  O OE2 . GLU A 87  ? 0.6859 0.8105 0.7150 0.0473  -0.1399 0.0274  87  GLU A OE2 
1289  N N   . PHE A 88  ? 0.6003 0.7453 0.7005 0.0594  -0.0798 -0.0023 88  PHE A N   
1290  C CA  . PHE A 88  ? 0.5892 0.7421 0.7035 0.0736  -0.0756 -0.0046 88  PHE A CA  
1291  C C   . PHE A 88  ? 0.6124 0.7360 0.7106 0.0847  -0.0786 -0.0011 88  PHE A C   
1292  O O   . PHE A 88  ? 0.5974 0.7000 0.6795 0.0808  -0.0712 -0.0008 88  PHE A O   
1293  C CB  . PHE A 88  ? 0.5474 0.7082 0.6670 0.0671  -0.0593 -0.0093 88  PHE A CB  
1294  C CG  . PHE A 88  ? 0.5056 0.6889 0.6389 0.0521  -0.0548 -0.0122 88  PHE A CG  
1295  C CD1 . PHE A 88  ? 0.5285 0.6969 0.6498 0.0365  -0.0512 -0.0111 88  PHE A CD1 
1296  C CD2 . PHE A 88  ? 0.4796 0.6993 0.6411 0.0532  -0.0539 -0.0172 88  PHE A CD2 
1297  C CE1 . PHE A 88  ? 0.5250 0.7098 0.6590 0.0211  -0.0470 -0.0149 88  PHE A CE1 
1298  C CE2 . PHE A 88  ? 0.4598 0.7005 0.6353 0.0365  -0.0499 -0.0205 88  PHE A CE2 
1299  C CZ  . PHE A 88  ? 0.4732 0.6941 0.6333 0.0198  -0.0466 -0.0193 88  PHE A CZ  
1309  N N   . LYS A 89  ? 0.5875 0.7093 0.6917 0.0981  -0.0905 0.0020  89  LYS A N   
1310  C CA  . LYS A 89  ? 0.5768 0.6672 0.6661 0.1067  -0.0948 0.0059  89  LYS A CA  
1311  C C   . LYS A 89  ? 0.6088 0.6950 0.7073 0.1209  -0.0881 -0.0022 89  LYS A C   
1312  O O   . LYS A 89  ? 0.6148 0.6723 0.6993 0.1250  -0.0889 -0.0020 89  LYS A O   
1313  C CB  . LYS A 89  ? 0.5724 0.6551 0.6593 0.1127  -0.1124 0.0159  89  LYS A CB  
1314  C CG  . LYS A 89  ? 0.5828 0.6654 0.6517 0.0968  -0.1187 0.0230  89  LYS A CG  
1315  C CD  . LYS A 89  ? 0.6413 0.7163 0.7027 0.1016  -0.1373 0.0356  89  LYS A CD  
1316  C CE  . LYS A 89  ? 0.6505 0.7301 0.6904 0.0839  -0.1426 0.0406  89  LYS A CE  
1317  N NZ  . LYS A 89  ? 0.6665 0.7391 0.6933 0.0866  -0.1623 0.0556  89  LYS A NZ  
1331  N N   . SER A 90  ? 0.6189 0.7335 0.7405 0.1271  -0.0806 -0.0108 90  SER A N   
1332  C CA  . SER A 90  ? 0.6121 0.7247 0.7408 0.1398  -0.0712 -0.0218 90  SER A CA  
1333  C C   . SER A 90  ? 0.5895 0.6831 0.6921 0.1303  -0.0599 -0.0252 90  SER A C   
1334  O O   . SER A 90  ? 0.5671 0.6667 0.6596 0.1156  -0.0531 -0.0222 90  SER A O   
1335  C CB  . SER A 90  ? 0.5960 0.7487 0.7552 0.1453  -0.0618 -0.0315 90  SER A CB  
1336  O OG  . SER A 90  ? 0.6053 0.7789 0.7938 0.1566  -0.0749 -0.0286 90  SER A OG  
1342  N N   . HIS A 91  ? 0.6175 0.6869 0.7098 0.1386  -0.0592 -0.0313 91  HIS A N   
1343  C CA  . HIS A 91  ? 0.6290 0.6815 0.6960 0.1301  -0.0516 -0.0351 91  HIS A CA  
1344  C C   . HIS A 91  ? 0.6339 0.6711 0.6824 0.1155  -0.0571 -0.0236 91  HIS A C   
1345  O O   . HIS A 91  ? 0.6609 0.6944 0.6934 0.1057  -0.0518 -0.0230 91  HIS A O   
1346  C CB  . HIS A 91  ? 0.5787 0.6547 0.6445 0.1251  -0.0356 -0.0430 91  HIS A CB  
1347  C CG  . HIS A 91  ? 0.5912 0.6893 0.6791 0.1385  -0.0262 -0.0568 91  HIS A CG  
1348  N ND1 . HIS A 91  ? 0.6385 0.7250 0.7226 0.1496  -0.0205 -0.0717 91  HIS A ND1 
1349  C CD2 . HIS A 91  ? 0.5791 0.7122 0.6963 0.1426  -0.0210 -0.0597 91  HIS A CD2 
1350  C CE1 . HIS A 91  ? 0.6232 0.7369 0.7345 0.1615  -0.0107 -0.0838 91  HIS A CE1 
1351  N NE2 . HIS A 91  ? 0.5889 0.7331 0.7222 0.1574  -0.0112 -0.0761 91  HIS A NE2 
1359  N N   . GLN A 92  ? 0.6164 0.6457 0.6671 0.1140  -0.0679 -0.0142 92  GLN A N   
1360  C CA  . GLN A 92  ? 0.6153 0.6326 0.6521 0.1008  -0.0709 -0.0057 92  GLN A CA  
1361  C C   . GLN A 92  ? 0.6108 0.6010 0.6318 0.0984  -0.0739 -0.0059 92  GLN A C   
1362  O O   . GLN A 92  ? 0.5507 0.5341 0.5637 0.0878  -0.0747 -0.0006 92  GLN A O   
1363  C CB  . GLN A 92  ? 0.6067 0.6257 0.6468 0.0980  -0.0797 0.0028  92  GLN A CB  
1364  C CG  . GLN A 92  ? 0.6100 0.6103 0.6488 0.1068  -0.0907 0.0073  92  GLN A CG  
1365  C CD  . GLN A 92  ? 0.5760 0.5801 0.6131 0.1028  -0.1007 0.0175  92  GLN A CD  
1366  O OE1 . GLN A 92  ? 0.5309 0.5477 0.5640 0.0909  -0.0983 0.0193  92  GLN A OE1 
1367  N NE2 . GLN A 92  ? 0.6091 0.6006 0.6478 0.1124  -0.1125 0.0242  92  GLN A NE2 
1376  N N   . TRP A 93  ? 0.6310 0.6064 0.6503 0.1077  -0.0753 -0.0131 93  TRP A N   
1377  C CA  . TRP A 93  ? 0.5954 0.5449 0.6007 0.1035  -0.0787 -0.0153 93  TRP A CA  
1378  C C   . TRP A 93  ? 0.6006 0.5322 0.6019 0.0967  -0.0869 -0.0047 93  TRP A C   
1379  O O   . TRP A 93  ? 0.6349 0.5584 0.6281 0.0854  -0.0876 -0.0021 93  TRP A O   
1380  C CB  . TRP A 93  ? 0.5924 0.5471 0.5860 0.0935  -0.0741 -0.0175 93  TRP A CB  
1381  C CG  . TRP A 93  ? 0.5907 0.5515 0.5766 0.0974  -0.0671 -0.0292 93  TRP A CG  
1382  C CD1 . TRP A 93  ? 0.5801 0.5625 0.5716 0.1023  -0.0577 -0.0339 93  TRP A CD1 
1383  C CD2 . TRP A 93  ? 0.5958 0.5427 0.5649 0.0942  -0.0681 -0.0384 93  TRP A CD2 
1384  N NE1 . TRP A 93  ? 0.6136 0.5960 0.5902 0.1025  -0.0513 -0.0454 93  TRP A NE1 
1385  C CE2 . TRP A 93  ? 0.6120 0.5724 0.5734 0.0976  -0.0584 -0.0488 93  TRP A CE2 
1386  C CE3 . TRP A 93  ? 0.5899 0.5162 0.5496 0.0870  -0.0761 -0.0397 93  TRP A CE3 
1387  C CZ2 . TRP A 93  ? 0.6523 0.6048 0.5927 0.0943  -0.0570 -0.0609 93  TRP A CZ2 
1388  C CZ3 . TRP A 93  ? 0.6340 0.5529 0.5762 0.0837  -0.0763 -0.0518 93  TRP A CZ3 
1389  C CH2 . TRP A 93  ? 0.6725 0.6037 0.6031 0.0874  -0.0670 -0.0625 93  TRP A CH2 
1400  N N   . PHE A 94  ? 0.6584 0.5858 0.6659 0.1029  -0.0933 0.0021  94  PHE A N   
1401  C CA  . PHE A 94  ? 0.6488 0.5573 0.6473 0.0948  -0.1004 0.0135  94  PHE A CA  
1402  C C   . PHE A 94  ? 0.6527 0.5288 0.6437 0.0938  -0.1038 0.0110  94  PHE A C   
1403  O O   . PHE A 94  ? 0.6367 0.4978 0.6326 0.1061  -0.1061 0.0040  94  PHE A O   
1404  C CB  . PHE A 94  ? 0.6343 0.5444 0.6368 0.1009  -0.1091 0.0238  94  PHE A CB  
1405  C CG  . PHE A 94  ? 0.6804 0.5698 0.6675 0.0903  -0.1157 0.0374  94  PHE A CG  
1406  C CD1 . PHE A 94  ? 0.6843 0.5835 0.6608 0.0741  -0.1111 0.0421  94  PHE A CD1 
1407  C CD2 . PHE A 94  ? 0.7037 0.5622 0.6866 0.0959  -0.1253 0.0451  94  PHE A CD2 
1408  C CE1 . PHE A 94  ? 0.6990 0.5815 0.6588 0.0620  -0.1144 0.0539  94  PHE A CE1 
1409  C CE2 . PHE A 94  ? 0.7177 0.5559 0.6829 0.0833  -0.1304 0.0597  94  PHE A CE2 
1410  C CZ  . PHE A 94  ? 0.7192 0.5713 0.6717 0.0655  -0.1241 0.0639  94  PHE A CZ  
1420  N N   . GLY A 95  ? 0.6829 0.5486 0.6644 0.0786  -0.1036 0.0156  95  GLY A N   
1421  C CA  . GLY A 95  ? 0.7114 0.5488 0.6867 0.0732  -0.1062 0.0119  95  GLY A CA  
1422  C C   . GLY A 95  ? 0.6953 0.5394 0.6696 0.0683  -0.1023 -0.0007 95  GLY A C   
1423  O O   . GLY A 95  ? 0.7334 0.5554 0.7028 0.0635  -0.1051 -0.0073 95  GLY A O   
1427  N N   . ALA A 96  ? 0.6657 0.5381 0.6433 0.0684  -0.0970 -0.0036 96  ALA A N   
1428  C CA  . ALA A 96  ? 0.6731 0.5533 0.6473 0.0618  -0.0960 -0.0112 96  ALA A CA  
1429  C C   . ALA A 96  ? 0.6521 0.5282 0.6282 0.0463  -0.0990 -0.0071 96  ALA A C   
1430  O O   . ALA A 96  ? 0.6047 0.4785 0.5783 0.0395  -0.1026 -0.0140 96  ALA A O   
1431  C CB  . ALA A 96  ? 0.6598 0.5681 0.6374 0.0639  -0.0908 -0.0103 96  ALA A CB  
1437  N N   . SER A 97  ? 0.6550 0.5326 0.6356 0.0397  -0.0972 0.0032  97  SER A N   
1438  C CA  . SER A 97  ? 0.6858 0.5631 0.6714 0.0241  -0.0970 0.0067  97  SER A CA  
1439  C C   . SER A 97  ? 0.6975 0.5570 0.6767 0.0178  -0.0963 0.0167  97  SER A C   
1440  O O   . SER A 97  ? 0.7031 0.5664 0.6780 0.0229  -0.0945 0.0238  97  SER A O   
1441  C CB  . SER A 97  ? 0.7035 0.6099 0.7025 0.0199  -0.0919 0.0086  97  SER A CB  
1442  O OG  . SER A 97  ? 0.7770 0.6936 0.7760 0.0242  -0.0861 0.0139  97  SER A OG  
1448  N N   . VAL A 98  ? 0.7371 0.5770 0.7142 0.0051  -0.0985 0.0179  98  VAL A N   
1449  C CA  . VAL A 98  ? 0.7876 0.6058 0.7546 -0.0040 -0.0983 0.0300  98  VAL A CA  
1450  C C   . VAL A 98  ? 0.7519 0.5717 0.7248 -0.0255 -0.0940 0.0314  98  VAL A C   
1451  O O   . VAL A 98  ? 0.7636 0.5800 0.7446 -0.0323 -0.0974 0.0226  98  VAL A O   
1452  C CB  . VAL A 98  ? 0.8574 0.6369 0.8140 0.0042  -0.1064 0.0318  98  VAL A CB  
1453  C CG1 . VAL A 98  ? 0.9128 0.6685 0.8558 -0.0039 -0.1082 0.0492  98  VAL A CG1 
1454  C CG2 . VAL A 98  ? 0.8840 0.6680 0.8421 0.0265  -0.1095 0.0262  98  VAL A CG2 
1464  N N   . ARG A 99  ? 0.7862 0.6139 0.7552 -0.0375 -0.0862 0.0413  99  ARG A N   
1465  C CA  A ARG A 99  ? 0.8069 0.6401 0.7830 -0.0598 -0.0789 0.0432  99  ARG A CA  
1466  C CA  B ARG A 99  ? 0.8064 0.6381 0.7822 -0.0598 -0.0793 0.0432  99  ARG A CA  
1467  C C   . ARG A 99  ? 0.8144 0.6257 0.7687 -0.0728 -0.0753 0.0592  99  ARG A C   
1468  O O   . ARG A 99  ? 0.8202 0.6273 0.7571 -0.0650 -0.0764 0.0682  99  ARG A O   
1469  C CB  A ARG A 99  ? 0.7917 0.6667 0.7884 -0.0640 -0.0682 0.0369  99  ARG A CB  
1470  C CB  B ARG A 99  ? 0.7923 0.6662 0.7909 -0.0644 -0.0694 0.0358  99  ARG A CB  
1471  C CG  A ARG A 99  ? 0.7962 0.6922 0.8187 -0.0624 -0.0720 0.0249  99  ARG A CG  
1472  C CG  B ARG A 99  ? 0.7980 0.6893 0.8206 -0.0629 -0.0748 0.0237  99  ARG A CG  
1473  C CD  A ARG A 99  ? 0.8341 0.7251 0.8677 -0.0816 -0.0735 0.0225  99  ARG A CD  
1474  C CD  B ARG A 99  ? 0.8430 0.7250 0.8740 -0.0824 -0.0769 0.0218  99  ARG A CD  
1475  N NE  A ARG A 99  ? 0.8185 0.7338 0.8767 -0.0792 -0.0804 0.0115  99  ARG A NE  
1476  N NE  B ARG A 99  ? 0.8468 0.7541 0.8962 -0.1009 -0.0644 0.0230  99  ARG A NE  
1477  C CZ  A ARG A 99  ? 0.8258 0.7316 0.8784 -0.0687 -0.0930 0.0046  99  ARG A CZ  
1478  C CZ  B ARG A 99  ? 0.9072 0.8055 0.9593 -0.1236 -0.0604 0.0261  99  ARG A CZ  
1479  N NH1 A ARG A 99  ? 0.8342 0.7079 0.8622 -0.0584 -0.0979 0.0054  99  ARG A NH1 
1480  N NH1 B ARG A 99  ? 0.9232 0.8509 0.9951 -0.1400 -0.0463 0.0256  99  ARG A NH1 
1481  N NH2 A ARG A 99  ? 0.8346 0.7647 0.9066 -0.0683 -0.1008 -0.0033 99  ARG A NH2 
1482  N NH2 B ARG A 99  ? 0.9421 0.8015 0.9784 -0.1305 -0.0691 0.0290  99  ARG A NH2 
1509  N N   . SER A 100 ? 0.8571 0.6560 0.8118 -0.0943 -0.0715 0.0633  100 SER A N   
1510  C CA  . SER A 100 ? 0.9265 0.7018 0.8570 -0.1108 -0.0676 0.0810  100 SER A CA  
1511  C C   . SER A 100 ? 0.9407 0.7367 0.8810 -0.1377 -0.0522 0.0808  100 SER A C   
1512  O O   . SER A 100 ? 0.9560 0.7684 0.9231 -0.1459 -0.0501 0.0690  100 SER A O   
1513  C CB  . SER A 100 ? 1.0058 0.7289 0.9218 -0.1110 -0.0798 0.0903  100 SER A CB  
1514  O OG  . SER A 100 ? 1.1094 0.8062 0.9981 -0.1253 -0.0784 0.1118  100 SER A OG  
1520  N N   . LYS A 101 ? 0.9437 0.7418 0.8622 -0.1519 -0.0416 0.0935  101 LYS A N   
1521  C CA  . LYS A 101 ? 0.9938 0.8108 0.9180 -0.1801 -0.0237 0.0946  101 LYS A CA  
1522  C C   . LYS A 101 ? 1.0447 0.8328 0.9275 -0.1976 -0.0201 0.1171  101 LYS A C   
1523  O O   . LYS A 101 ? 1.0079 0.8044 0.8663 -0.1945 -0.0163 0.1236  101 LYS A O   
1524  C CB  . LYS A 101 ? 0.9695 0.8390 0.9159 -0.1789 -0.0076 0.0798  101 LYS A CB  
1525  C CG  . LYS A 101 ? 0.9508 0.8461 0.9081 -0.2071 0.0139  0.0779  101 LYS A CG  
1526  C CD  . LYS A 101 ? 0.9390 0.8825 0.9159 -0.2033 0.0314  0.0628  101 LYS A CD  
1527  C CE  . LYS A 101 ? 0.9816 0.9504 0.9632 -0.2322 0.0564  0.0613  101 LYS A CE  
1528  N NZ  . LYS A 101 ? 1.0632 1.0389 1.0762 -0.2504 0.0586  0.0588  101 LYS A NZ  
1542  N N   . GLN A 102 ? 1.1102 0.8629 0.9835 -0.2171 -0.0223 0.1297  102 GLN A N   
1543  C CA  . GLN A 102 ? 1.1738 0.8922 1.0048 -0.2359 -0.0209 0.1554  102 GLN A CA  
1544  C C   . GLN A 102 ? 1.1578 0.8493 0.9603 -0.2122 -0.0391 0.1689  102 GLN A C   
1545  O O   . GLN A 102 ? 1.1426 0.8051 0.9536 -0.1909 -0.0571 0.1676  102 GLN A O   
1546  C CB  . GLN A 102 ? 1.2218 0.9763 1.0435 -0.2617 0.0039  0.1561  102 GLN A CB  
1547  C CG  . GLN A 102 ? 1.2768 1.0567 1.1314 -0.2866 0.0211  0.1446  102 GLN A CG  
1548  C CD  . GLN A 102 ? 1.3335 1.1571 1.1857 -0.3090 0.0488  0.1403  102 GLN A CD  
1549  O OE1 . GLN A 102 ? 1.2801 1.1328 1.1253 -0.2980 0.0565  0.1322  102 GLN A OE1 
1550  N NE2 . GLN A 102 ? 1.4288 1.2578 1.2877 -0.3418 0.0653  0.1440  102 GLN A NE2 
1559  N N   . ASP A 103 ? 1.1743 0.8763 0.9451 -0.2146 -0.0354 0.1801  103 ASP A N   
1560  C CA  . ASP A 103 ? 1.2003 0.8790 0.9455 -0.1940 -0.0551 0.1949  103 ASP A CA  
1561  C C   . ASP A 103 ? 1.1583 0.8649 0.9259 -0.1632 -0.0625 0.1763  103 ASP A C   
1562  O O   . ASP A 103 ? 1.1898 0.8782 0.9499 -0.1415 -0.0811 0.1843  103 ASP A O   
1563  C CB  . ASP A 103 ? 1.2888 0.9696 0.9873 -0.2111 -0.0504 0.2146  103 ASP A CB  
1564  C CG  . ASP A 103 ? 1.4410 1.0818 1.1066 -0.2397 -0.0486 0.2414  103 ASP A CG  
1565  O OD1 . ASP A 103 ? 1.5158 1.1136 1.1909 -0.2390 -0.0591 0.2500  103 ASP A OD1 
1566  O OD2 . ASP A 103 ? 1.5383 1.1892 1.1670 -0.2640 -0.0359 0.2537  103 ASP A OD2 
1571  N N   . LYS A 104 ? 1.0699 0.8200 0.8667 -0.1609 -0.0486 0.1526  104 LYS A N   
1572  C CA  . LYS A 104 ? 0.9723 0.7510 0.7858 -0.1365 -0.0525 0.1368  104 LYS A CA  
1573  C C   . LYS A 104 ? 0.8617 0.6312 0.7048 -0.1139 -0.0647 0.1253  104 LYS A C   
1574  O O   . LYS A 104 ? 0.7958 0.5579 0.6589 -0.1194 -0.0630 0.1181  104 LYS A O   
1575  C CB  . LYS A 104 ? 0.9646 0.7904 0.7956 -0.1440 -0.0321 0.1178  104 LYS A CB  
1576  C CG  . LYS A 104 ? 1.0034 0.8421 0.8059 -0.1692 -0.0149 0.1243  104 LYS A CG  
1577  C CD  . LYS A 104 ? 1.0024 0.8839 0.8328 -0.1792 0.0086  0.1033  104 LYS A CD  
1578  C CE  . LYS A 104 ? 1.0284 0.9107 0.8819 -0.1971 0.0183  0.1017  104 LYS A CE  
1579  N NZ  . LYS A 104 ? 1.1024 0.9709 0.9235 -0.2279 0.0299  0.1185  104 LYS A NZ  
1593  N N   . ILE A 105 ? 0.8294 0.6012 0.6744 -0.0898 -0.0768 0.1229  105 ILE A N   
1594  C CA  . ILE A 105 ? 0.7779 0.5485 0.6487 -0.0678 -0.0855 0.1094  105 ILE A CA  
1595  C C   . ILE A 105 ? 0.7614 0.5697 0.6456 -0.0539 -0.0818 0.0957  105 ILE A C   
1596  O O   . ILE A 105 ? 0.7908 0.6080 0.6610 -0.0483 -0.0854 0.1011  105 ILE A O   
1597  C CB  . ILE A 105 ? 0.8184 0.5519 0.6824 -0.0507 -0.1034 0.1196  105 ILE A CB  
1598  C CG1 . ILE A 105 ? 0.9027 0.5917 0.7532 -0.0650 -0.1076 0.1344  105 ILE A CG1 
1599  C CG2 . ILE A 105 ? 0.7880 0.5253 0.6772 -0.0291 -0.1085 0.1021  105 ILE A CG2 
1600  C CD1 . ILE A 105 ? 0.9472 0.5945 0.7930 -0.0472 -0.1255 0.1455  105 ILE A CD1 
1612  N N   . LEU A 106 ? 0.7195 0.5487 0.6300 -0.0495 -0.0760 0.0789  106 LEU A N   
1613  C CA  . LEU A 106 ? 0.6932 0.5523 0.6185 -0.0361 -0.0733 0.0667  106 LEU A CA  
1614  C C   . LEU A 106 ? 0.7074 0.5600 0.6462 -0.0170 -0.0829 0.0591  106 LEU A C   
1615  O O   . LEU A 106 ? 0.7338 0.5785 0.6838 -0.0181 -0.0845 0.0525  106 LEU A O   
1616  C CB  . LEU A 106 ? 0.6823 0.5714 0.6272 -0.0452 -0.0592 0.0550  106 LEU A CB  
1617  C CG  . LEU A 106 ? 0.6230 0.5390 0.5837 -0.0330 -0.0557 0.0437  106 LEU A CG  
1618  C CD1 . LEU A 106 ? 0.6383 0.5605 0.5818 -0.0305 -0.0551 0.0468  106 LEU A CD1 
1619  C CD2 . LEU A 106 ? 0.5886 0.5302 0.5731 -0.0405 -0.0430 0.0334  106 LEU A CD2 
1631  N N   . ALA A 107 ? 0.7421 0.6000 0.6793 -0.0012 -0.0889 0.0590  107 ALA A N   
1632  C CA  . ALA A 107 ? 0.7412 0.5984 0.6904 0.0166  -0.0949 0.0505  107 ALA A CA  
1633  C C   . ALA A 107 ? 0.7086 0.5948 0.6666 0.0250  -0.0911 0.0441  107 ALA A C   
1634  O O   . ALA A 107 ? 0.6916 0.5895 0.6424 0.0225  -0.0900 0.0486  107 ALA A O   
1635  C CB  . ALA A 107 ? 0.7538 0.5845 0.6964 0.0288  -0.1064 0.0574  107 ALA A CB  
1641  N N   . CYS A 108 ? 0.7094 0.6063 0.6806 0.0331  -0.0895 0.0337  108 CYS A N   
1642  C CA  . CYS A 108 ? 0.6650 0.5870 0.6454 0.0376  -0.0844 0.0283  108 CYS A CA  
1643  C C   . CYS A 108 ? 0.6034 0.5294 0.5896 0.0519  -0.0872 0.0225  108 CYS A C   
1644  O O   . CYS A 108 ? 0.5894 0.5015 0.5745 0.0579  -0.0908 0.0184  108 CYS A O   
1645  C CB  . CYS A 108 ? 0.6722 0.6079 0.6639 0.0301  -0.0772 0.0231  108 CYS A CB  
1646  S SG  . CYS A 108 ? 0.7491 0.6892 0.7408 0.0132  -0.0689 0.0257  108 CYS A SG  
1651  N N   . ALA A 109 ? 0.5645 0.5104 0.5567 0.0558  -0.0840 0.0208  109 ALA A N   
1652  C CA  . ALA A 109 ? 0.5610 0.5173 0.5602 0.0667  -0.0833 0.0153  109 ALA A CA  
1653  C C   . ALA A 109 ? 0.5454 0.5174 0.5507 0.0628  -0.0761 0.0121  109 ALA A C   
1654  O O   . ALA A 109 ? 0.5246 0.5108 0.5354 0.0599  -0.0724 0.0127  109 ALA A O   
1655  C CB  . ALA A 109 ? 0.5848 0.5512 0.5884 0.0737  -0.0871 0.0178  109 ALA A CB  
1661  N N   . PRO A 110 ? 0.5800 0.5488 0.5842 0.0619  -0.0752 0.0092  110 PRO A N   
1662  C CA  . PRO A 110 ? 0.5786 0.5584 0.5885 0.0581  -0.0708 0.0100  110 PRO A CA  
1663  C C   . PRO A 110 ? 0.5798 0.5724 0.5916 0.0617  -0.0661 0.0090  110 PRO A C   
1664  O O   . PRO A 110 ? 0.5754 0.5735 0.5914 0.0580  -0.0627 0.0119  110 PRO A O   
1665  C CB  . PRO A 110 ? 0.6027 0.5758 0.6085 0.0564  -0.0750 0.0087  110 PRO A CB  
1666  C CG  . PRO A 110 ? 0.6322 0.5895 0.6321 0.0556  -0.0799 0.0064  110 PRO A CG  
1667  C CD  . PRO A 110 ? 0.6410 0.5941 0.6382 0.0628  -0.0798 0.0058  110 PRO A CD  
1675  N N   . LEU A 111 ? 0.5405 0.5380 0.5517 0.0686  -0.0654 0.0055  111 LEU A N   
1676  C CA  . LEU A 111 ? 0.5213 0.5353 0.5372 0.0699  -0.0588 0.0039  111 LEU A CA  
1677  C C   . LEU A 111 ? 0.5718 0.5996 0.5995 0.0711  -0.0587 0.0036  111 LEU A C   
1678  O O   . LEU A 111 ? 0.5508 0.5958 0.5869 0.0731  -0.0538 0.0006  111 LEU A O   
1679  C CB  . LEU A 111 ? 0.5118 0.5276 0.5207 0.0765  -0.0558 -0.0026 111 LEU A CB  
1680  C CG  . LEU A 111 ? 0.5421 0.5534 0.5366 0.0715  -0.0545 -0.0011 111 LEU A CG  
1681  C CD1 . LEU A 111 ? 0.5532 0.5624 0.5343 0.0764  -0.0521 -0.0105 111 LEU A CD1 
1682  C CD2 . LEU A 111 ? 0.4973 0.5196 0.4933 0.0644  -0.0482 0.0057  111 LEU A CD2 
1694  N N   . TYR A 112 ? 0.5951 0.6178 0.6231 0.0684  -0.0641 0.0064  112 TYR A N   
1695  C CA  . TYR A 112 ? 0.5914 0.6283 0.6272 0.0660  -0.0661 0.0069  112 TYR A CA  
1696  C C   . TYR A 112 ? 0.6309 0.6786 0.6732 0.0563  -0.0588 0.0056  112 TYR A C   
1697  O O   . TYR A 112 ? 0.6589 0.6970 0.6983 0.0493  -0.0554 0.0066  112 TYR A O   
1698  C CB  . TYR A 112 ? 0.5911 0.6176 0.6181 0.0621  -0.0728 0.0109  112 TYR A CB  
1699  C CG  . TYR A 112 ? 0.5574 0.5969 0.5854 0.0542  -0.0748 0.0109  112 TYR A CG  
1700  C CD1 . TYR A 112 ? 0.5416 0.5932 0.5731 0.0585  -0.0843 0.0131  112 TYR A CD1 
1701  C CD2 . TYR A 112 ? 0.4998 0.5392 0.5258 0.0426  -0.0681 0.0077  112 TYR A CD2 
1702  C CE1 . TYR A 112 ? 0.4969 0.5621 0.5265 0.0494  -0.0881 0.0124  112 TYR A CE1 
1703  C CE2 . TYR A 112 ? 0.4972 0.5473 0.5210 0.0336  -0.0695 0.0046  112 TYR A CE2 
1704  C CZ  . TYR A 112 ? 0.4890 0.5529 0.5128 0.0360  -0.0801 0.0072  112 TYR A CZ  
1705  O OH  . TYR A 112 ? 0.5277 0.6041 0.5465 0.0252  -0.0835 0.0036  112 TYR A OH  
1715  N N   . HIS A 113 ? 0.6021 0.6697 0.6562 0.0558  -0.0560 0.0030  113 HIS A N   
1716  C CA  . HIS A 113 ? 0.5637 0.6399 0.6252 0.0447  -0.0494 0.0016  113 HIS A CA  
1717  C C   . HIS A 113 ? 0.5786 0.6664 0.6452 0.0377  -0.0544 -0.0016 113 HIS A C   
1718  O O   . HIS A 113 ? 0.6464 0.7423 0.7130 0.0429  -0.0639 -0.0010 113 HIS A O   
1719  C CB  . HIS A 113 ? 0.5606 0.6536 0.6320 0.0441  -0.0416 0.0003  113 HIS A CB  
1720  C CG  . HIS A 113 ? 0.5465 0.6297 0.6074 0.0477  -0.0360 0.0032  113 HIS A CG  
1721  N ND1 . HIS A 113 ? 0.5634 0.6413 0.6164 0.0588  -0.0387 0.0012  113 HIS A ND1 
1722  C CD2 . HIS A 113 ? 0.5619 0.6387 0.6167 0.0407  -0.0287 0.0081  113 HIS A CD2 
1723  C CE1 . HIS A 113 ? 0.5830 0.6541 0.6237 0.0575  -0.0333 0.0033  113 HIS A CE1 
1724  N NE2 . HIS A 113 ? 0.5747 0.6453 0.6155 0.0469  -0.0279 0.0090  113 HIS A NE2 
1732  N N   . TRP A 114 ? 0.5368 0.6243 0.6069 0.0253  -0.0489 -0.0048 114 TRP A N   
1733  C CA  . TRP A 114 ? 0.5839 0.6842 0.6571 0.0156  -0.0533 -0.0105 114 TRP A CA  
1734  C C   . TRP A 114 ? 0.5728 0.6780 0.6576 0.0024  -0.0451 -0.0155 114 TRP A C   
1735  O O   . TRP A 114 ? 0.5584 0.6513 0.6460 0.0005  -0.0361 -0.0124 114 TRP A O   
1736  C CB  . TRP A 114 ? 0.6320 0.7184 0.6889 0.0117  -0.0565 -0.0124 114 TRP A CB  
1737  C CG  . TRP A 114 ? 0.6321 0.7051 0.6875 0.0004  -0.0476 -0.0197 114 TRP A CG  
1738  C CD1 . TRP A 114 ? 0.6763 0.7315 0.7372 0.0009  -0.0384 -0.0190 114 TRP A CD1 
1739  C CD2 . TRP A 114 ? 0.6483 0.7236 0.6964 -0.0124 -0.0475 -0.0297 114 TRP A CD2 
1740  N NE1 . TRP A 114 ? 0.7099 0.7550 0.7718 -0.0089 -0.0317 -0.0287 114 TRP A NE1 
1741  C CE2 . TRP A 114 ? 0.6814 0.7385 0.7339 -0.0181 -0.0360 -0.0369 114 TRP A CE2 
1742  C CE3 . TRP A 114 ? 0.7366 0.8277 0.7742 -0.0196 -0.0570 -0.0335 114 TRP A CE3 
1743  C CZ2 . TRP A 114 ? 0.7557 0.8088 0.8026 -0.0309 -0.0310 -0.0507 114 TRP A CZ2 
1744  C CZ3 . TRP A 114 ? 0.8035 0.8923 0.8310 -0.0343 -0.0533 -0.0462 114 TRP A CZ3 
1745  C CH2 . TRP A 114 ? 0.8205 0.8899 0.8528 -0.0399 -0.0391 -0.0562 114 TRP A CH2 
1756  N N   . ARG A 115 ? 0.5572 0.6797 0.6479 -0.0080 -0.0496 -0.0224 115 ARG A N   
1757  C CA  . ARG A 115 ? 0.5622 0.6954 0.6680 -0.0224 -0.0437 -0.0281 115 ARG A CA  
1758  C C   . ARG A 115 ? 0.5864 0.6971 0.6877 -0.0359 -0.0366 -0.0358 115 ARG A C   
1759  O O   . ARG A 115 ? 0.6521 0.7567 0.7643 -0.0465 -0.0280 -0.0373 115 ARG A O   
1760  C CB  . ARG A 115 ? 0.5636 0.7309 0.6814 -0.0278 -0.0543 -0.0332 115 ARG A CB  
1761  C CG  . ARG A 115 ? 0.5466 0.7289 0.6814 -0.0469 -0.0501 -0.0416 115 ARG A CG  
1762  C CD  . ARG A 115 ? 0.5663 0.7801 0.7076 -0.0540 -0.0650 -0.0485 115 ARG A CD  
1763  N NE  . ARG A 115 ? 0.5764 0.8125 0.7394 -0.0727 -0.0627 -0.0569 115 ARG A NE  
1764  C CZ  . ARG A 115 ? 0.5990 0.8216 0.7583 -0.0929 -0.0579 -0.0680 115 ARG A CZ  
1765  N NH1 . ARG A 115 ? 0.6360 0.8239 0.7722 -0.0952 -0.0536 -0.0730 115 ARG A NH1 
1766  N NH2 . ARG A 115 ? 0.5708 0.8149 0.7520 -0.1114 -0.0564 -0.0755 115 ARG A NH2 
1780  N N   . THR A 116 ? 0.5815 0.6786 0.6674 -0.0363 -0.0386 -0.0411 116 THR A N   
1781  C CA  . THR A 116 ? 0.6124 0.6929 0.6953 -0.0496 -0.0320 -0.0538 116 THR A CA  
1782  C C   . THR A 116 ? 0.6778 0.7796 0.7626 -0.0658 -0.0381 -0.0653 116 THR A C   
1783  O O   . THR A 116 ? 0.6312 0.7603 0.7280 -0.0672 -0.0453 -0.0618 116 THR A O   
1784  C CB  . THR A 116 ? 0.6016 0.6576 0.6972 -0.0527 -0.0200 -0.0527 116 THR A CB  
1785  O OG1 . THR A 116 ? 0.6028 0.6697 0.7130 -0.0643 -0.0179 -0.0527 116 THR A OG1 
1786  C CG2 . THR A 116 ? 0.5353 0.5776 0.6308 -0.0371 -0.0176 -0.0383 116 THR A CG2 
1794  N N   . GLU A 117 ? 0.7717 0.8633 0.8459 -0.0785 -0.0352 -0.0805 117 GLU A N   
1795  C CA  . GLU A 117 ? 0.8103 0.9224 0.8812 -0.0961 -0.0430 -0.0934 117 GLU A CA  
1796  C C   . GLU A 117 ? 0.8243 0.9326 0.9142 -0.1131 -0.0361 -0.1033 117 GLU A C   
1797  O O   . GLU A 117 ? 0.8822 1.0124 0.9745 -0.1294 -0.0439 -0.1138 117 GLU A O   
1798  C CB  . GLU A 117 ? 0.8918 0.9961 0.9362 -0.1043 -0.0428 -0.1074 117 GLU A CB  
1799  C CG  . GLU A 117 ? 0.9650 1.0881 0.9865 -0.0986 -0.0573 -0.0993 117 GLU A CG  
1800  C CD  . GLU A 117 ? 1.0660 1.1869 1.0566 -0.1129 -0.0575 -0.1143 117 GLU A CD  
1801  O OE1 . GLU A 117 ? 1.0857 1.1823 1.0696 -0.1161 -0.0413 -0.1269 117 GLU A OE1 
1802  O OE2 . GLU A 117 ? 1.0916 1.2363 1.0649 -0.1210 -0.0738 -0.1139 117 GLU A OE2 
1809  N N   . MET A 118 ? 0.8317 0.9126 0.9349 -0.1109 -0.0230 -0.0994 118 MET A N   
1810  C CA  . MET A 118 ? 0.9093 0.9792 1.0294 -0.1286 -0.0154 -0.1073 118 MET A CA  
1811  C C   . MET A 118 ? 0.9404 1.0300 1.0802 -0.1298 -0.0157 -0.0934 118 MET A C   
1812  O O   . MET A 118 ? 0.9791 1.1018 1.1301 -0.1419 -0.0228 -0.0978 118 MET A O   
1813  C CB  . MET A 118 ? 0.9703 0.9948 1.0935 -0.1268 -0.0013 -0.1106 118 MET A CB  
1814  C CG  . MET A 118 ? 1.0022 1.0103 1.1097 -0.1256 0.0026  -0.1277 118 MET A CG  
1815  S SD  . MET A 118 ? 1.0425 1.0633 1.1371 -0.1511 -0.0010 -0.1558 118 MET A SD  
1816  C CE  . MET A 118 ? 1.0660 1.0827 1.1321 -0.1442 0.0019  -0.1682 118 MET A CE  
1826  N N   . LYS A 119 ? 0.9588 1.0316 1.1030 -0.1180 -0.0081 -0.0772 119 LYS A N   
1827  C CA  . LYS A 119 ? 0.9696 1.0604 1.1283 -0.1198 -0.0051 -0.0644 119 LYS A CA  
1828  C C   . LYS A 119 ? 0.9259 1.0471 1.0821 -0.1017 -0.0127 -0.0545 119 LYS A C   
1829  O O   . LYS A 119 ? 0.9162 1.0356 1.0580 -0.0865 -0.0197 -0.0534 119 LYS A O   
1830  C CB  . LYS A 119 ? 1.0442 1.1000 1.2043 -0.1186 0.0066  -0.0510 119 LYS A CB  
1831  C CG  . LYS A 119 ? 1.1717 1.1932 1.3393 -0.1365 0.0148  -0.0584 119 LYS A CG  
1832  C CD  . LYS A 119 ? 1.2826 1.2667 1.4502 -0.1329 0.0234  -0.0407 119 LYS A CD  
1833  C CE  . LYS A 119 ? 1.4124 1.3575 1.5902 -0.1504 0.0310  -0.0469 119 LYS A CE  
1834  N NZ  . LYS A 119 ? 1.4829 1.3882 1.6604 -0.1465 0.0369  -0.0262 119 LYS A NZ  
1848  N N   . GLN A 120 ? 0.9036 1.0526 1.0756 -0.1042 -0.0099 -0.0481 120 GLN A N   
1849  C CA  . GLN A 120 ? 0.8558 1.0308 1.0294 -0.0862 -0.0140 -0.0400 120 GLN A CA  
1850  C C   . GLN A 120 ? 0.8125 0.9613 0.9719 -0.0733 -0.0060 -0.0267 120 GLN A C   
1851  O O   . GLN A 120 ? 0.8555 1.0006 1.0181 -0.0796 0.0049  -0.0184 120 GLN A O   
1852  C CB  . GLN A 120 ? 0.8927 1.1107 1.0921 -0.0938 -0.0117 -0.0412 120 GLN A CB  
1853  C CG  . GLN A 120 ? 0.9541 1.2087 1.1716 -0.1033 -0.0242 -0.0531 120 GLN A CG  
1854  C CD  . GLN A 120 ? 1.0076 1.3095 1.2579 -0.1099 -0.0208 -0.0544 120 GLN A CD  
1855  O OE1 . GLN A 120 ? 1.0071 1.3107 1.2645 -0.1133 -0.0053 -0.0478 120 GLN A OE1 
1856  N NE2 . GLN A 120 ? 1.1069 1.4498 1.3777 -0.1120 -0.0355 -0.0625 120 GLN A NE2 
1865  N N   . GLU A 121 ? 0.7584 0.8902 0.9008 -0.0571 -0.0119 -0.0241 121 GLU A N   
1866  C CA  . GLU A 121 ? 0.6546 0.7636 0.7830 -0.0448 -0.0077 -0.0126 121 GLU A CA  
1867  C C   . GLU A 121 ? 0.5687 0.6920 0.6907 -0.0265 -0.0145 -0.0103 121 GLU A C   
1868  O O   . GLU A 121 ? 0.5602 0.7089 0.6901 -0.0219 -0.0224 -0.0158 121 GLU A O   
1869  C CB  . GLU A 121 ? 0.6172 0.6894 0.7352 -0.0433 -0.0076 -0.0122 121 GLU A CB  
1870  C CG  . GLU A 121 ? 0.6704 0.7212 0.7964 -0.0596 -0.0006 -0.0154 121 GLU A CG  
1871  C CD  . GLU A 121 ? 0.8121 0.8507 0.9399 -0.0664 0.0082  -0.0020 121 GLU A CD  
1872  O OE1 . GLU A 121 ? 0.8663 0.9074 0.9841 -0.0568 0.0089  0.0100  121 GLU A OE1 
1873  O OE2 . GLU A 121 ? 0.8928 0.9177 1.0299 -0.0829 0.0144  -0.0034 121 GLU A OE2 
1880  N N   . ARG A 122 ? 0.5550 0.6602 0.6630 -0.0159 -0.0125 -0.0018 122 ARG A N   
1881  C CA  . ARG A 122 ? 0.5448 0.6556 0.6447 0.0006  -0.0181 -0.0005 122 ARG A CA  
1882  C C   . ARG A 122 ? 0.5154 0.5971 0.5987 0.0073  -0.0192 0.0064  122 ARG A C   
1883  O O   . ARG A 122 ? 0.5366 0.6117 0.6102 0.0104  -0.0155 0.0135  122 ARG A O   
1884  C CB  . ARG A 122 ? 0.6319 0.7663 0.7376 0.0049  -0.0122 -0.0002 122 ARG A CB  
1885  C CG  . ARG A 122 ? 0.7276 0.8687 0.8303 0.0223  -0.0187 -0.0029 122 ARG A CG  
1886  C CD  . ARG A 122 ? 0.7720 0.9372 0.8832 0.0277  -0.0105 -0.0064 122 ARG A CD  
1887  N NE  . ARG A 122 ? 0.7849 0.9513 0.8954 0.0455  -0.0171 -0.0107 122 ARG A NE  
1888  C CZ  . ARG A 122 ? 0.7796 0.9282 0.8717 0.0540  -0.0159 -0.0102 122 ARG A CZ  
1889  N NH1 . ARG A 122 ? 0.7816 0.9130 0.8534 0.0468  -0.0099 -0.0042 122 ARG A NH1 
1890  N NH2 . ARG A 122 ? 0.7721 0.9188 0.8661 0.0693  -0.0220 -0.0154 122 ARG A NH2 
1904  N N   . GLU A 123 ? 0.4745 0.5411 0.5546 0.0084  -0.0243 0.0036  123 GLU A N   
1905  C CA  . GLU A 123 ? 0.5027 0.5451 0.5752 0.0128  -0.0250 0.0088  123 GLU A CA  
1906  C C   . GLU A 123 ? 0.5176 0.5581 0.5810 0.0238  -0.0322 0.0084  123 GLU A C   
1907  O O   . GLU A 123 ? 0.5200 0.5650 0.5824 0.0243  -0.0365 0.0029  123 GLU A O   
1908  C CB  . GLU A 123 ? 0.5551 0.5822 0.6348 0.0053  -0.0224 0.0041  123 GLU A CB  
1909  C CG  . GLU A 123 ? 0.6158 0.6381 0.7051 -0.0071 -0.0154 0.0044  123 GLU A CG  
1910  C CD  . GLU A 123 ? 0.6579 0.6575 0.7557 -0.0123 -0.0117 -0.0009 123 GLU A CD  
1911  O OE1 . GLU A 123 ? 0.6634 0.6580 0.7606 -0.0076 -0.0132 -0.0081 123 GLU A OE1 
1912  O OE2 . GLU A 123 ? 0.6486 0.6345 0.7544 -0.0215 -0.0061 0.0016  123 GLU A OE2 
1919  N N   . PRO A 124 ? 0.5295 0.5625 0.5841 0.0309  -0.0341 0.0145  124 PRO A N   
1920  C CA  . PRO A 124 ? 0.4909 0.5205 0.5376 0.0394  -0.0408 0.0133  124 PRO A CA  
1921  C C   . PRO A 124 ? 0.4755 0.4929 0.5244 0.0386  -0.0429 0.0126  124 PRO A C   
1922  O O   . PRO A 124 ? 0.4993 0.5075 0.5476 0.0414  -0.0454 0.0165  124 PRO A O   
1923  C CB  . PRO A 124 ? 0.5374 0.5643 0.5735 0.0440  -0.0414 0.0181  124 PRO A CB  
1924  C CG  . PRO A 124 ? 0.5233 0.5438 0.5602 0.0380  -0.0374 0.0258  124 PRO A CG  
1925  C CD  . PRO A 124 ? 0.5218 0.5482 0.5708 0.0297  -0.0311 0.0232  124 PRO A CD  
1933  N N   . VAL A 125 ? 0.4549 0.4749 0.5069 0.0337  -0.0418 0.0066  125 VAL A N   
1934  C CA  . VAL A 125 ? 0.4578 0.4700 0.5120 0.0316  -0.0406 0.0034  125 VAL A CA  
1935  C C   . VAL A 125 ? 0.4890 0.4987 0.5342 0.0354  -0.0460 0.0052  125 VAL A C   
1936  O O   . VAL A 125 ? 0.5294 0.5342 0.5782 0.0339  -0.0444 0.0041  125 VAL A O   
1937  C CB  . VAL A 125 ? 0.5019 0.5180 0.5567 0.0228  -0.0362 -0.0052 125 VAL A CB  
1938  C CG1 . VAL A 125 ? 0.5558 0.5697 0.6215 0.0171  -0.0302 -0.0086 125 VAL A CG1 
1939  C CG2 . VAL A 125 ? 0.4802 0.5078 0.5235 0.0215  -0.0425 -0.0059 125 VAL A CG2 
1949  N N   . GLY A 126 ? 0.5367 0.5495 0.5728 0.0401  -0.0517 0.0075  126 GLY A N   
1950  C CA  . GLY A 126 ? 0.5873 0.5926 0.6145 0.0427  -0.0572 0.0096  126 GLY A CA  
1951  C C   . GLY A 126 ? 0.6326 0.6374 0.6516 0.0364  -0.0580 0.0091  126 GLY A C   
1952  O O   . GLY A 126 ? 0.6360 0.6457 0.6565 0.0288  -0.0524 0.0046  126 GLY A O   
1956  N N   . THR A 127 ? 0.5912 0.5881 0.5996 0.0387  -0.0648 0.0136  127 THR A N   
1957  C CA  . THR A 127 ? 0.5588 0.5527 0.5538 0.0312  -0.0667 0.0166  127 THR A CA  
1958  C C   . THR A 127 ? 0.5492 0.5261 0.5353 0.0309  -0.0709 0.0227  127 THR A C   
1959  O O   . THR A 127 ? 0.5179 0.4857 0.5080 0.0384  -0.0747 0.0233  127 THR A O   
1960  C CB  . THR A 127 ? 0.6235 0.6261 0.6124 0.0333  -0.0746 0.0193  127 THR A CB  
1961  O OG1 . THR A 127 ? 0.6069 0.6085 0.5779 0.0227  -0.0761 0.0225  127 THR A OG1 
1962  C CG2 . THR A 127 ? 0.6266 0.6227 0.6170 0.0459  -0.0848 0.0251  127 THR A CG2 
1970  N N   . CYS A 128 ? 0.6589 0.6307 0.6310 0.0203  -0.0695 0.0267  128 CYS A N   
1971  C CA  . CYS A 128 ? 0.6675 0.6208 0.6288 0.0163  -0.0732 0.0345  128 CYS A CA  
1972  C C   . CYS A 128 ? 0.6860 0.6328 0.6246 0.0103  -0.0796 0.0448  128 CYS A C   
1973  O O   . CYS A 128 ? 0.6885 0.6486 0.6184 0.0054  -0.0789 0.0435  128 CYS A O   
1974  C CB  . CYS A 128 ? 0.6831 0.6366 0.6498 0.0051  -0.0631 0.0311  128 CYS A CB  
1975  S SG  . CYS A 128 ? 0.7351 0.6972 0.7280 0.0115  -0.0595 0.0221  128 CYS A SG  
1980  N N   . PHE A 129 ? 0.6364 0.5608 0.5642 0.0098  -0.0869 0.0555  129 PHE A N   
1981  C CA  . PHE A 129 ? 0.6876 0.6002 0.5899 0.0020  -0.0942 0.0696  129 PHE A CA  
1982  C C   . PHE A 129 ? 0.7356 0.6299 0.6255 -0.0133 -0.0883 0.0764  129 PHE A C   
1983  O O   . PHE A 129 ? 0.7187 0.5981 0.6199 -0.0114 -0.0879 0.0749  129 PHE A O   
1984  C CB  . PHE A 129 ? 0.7280 0.6269 0.6297 0.0172  -0.1115 0.0800  129 PHE A CB  
1985  C CG  . PHE A 129 ? 0.7145 0.6367 0.6270 0.0285  -0.1178 0.0754  129 PHE A CG  
1986  C CD1 . PHE A 129 ? 0.7311 0.6654 0.6273 0.0228  -0.1254 0.0823  129 PHE A CD1 
1987  C CD2 . PHE A 129 ? 0.6766 0.6103 0.6144 0.0426  -0.1158 0.0641  129 PHE A CD2 
1988  C CE1 . PHE A 129 ? 0.7065 0.6651 0.6157 0.0311  -0.1319 0.0772  129 PHE A CE1 
1989  C CE2 . PHE A 129 ? 0.6260 0.5835 0.5763 0.0505  -0.1201 0.0597  129 PHE A CE2 
1990  C CZ  . PHE A 129 ? 0.6497 0.6203 0.5878 0.0448  -0.1285 0.0659  129 PHE A CZ  
2000  N N   . LEU A 130 ? 0.7933 0.6900 0.6589 -0.0303 -0.0831 0.0828  130 LEU A N   
2001  C CA  . LEU A 130 ? 0.8616 0.7442 0.7127 -0.0489 -0.0751 0.0904  130 LEU A CA  
2002  C C   . LEU A 130 ? 0.9711 0.8307 0.7882 -0.0558 -0.0871 0.1122  130 LEU A C   
2003  O O   . LEU A 130 ? 0.9204 0.7903 0.7147 -0.0602 -0.0912 0.1174  130 LEU A O   
2004  C CB  . LEU A 130 ? 0.7991 0.7061 0.6499 -0.0655 -0.0549 0.0786  130 LEU A CB  
2005  C CG  . LEU A 130 ? 0.7916 0.6911 0.6301 -0.0876 -0.0428 0.0846  130 LEU A CG  
2006  C CD1 . LEU A 130 ? 0.7872 0.6748 0.6506 -0.0862 -0.0428 0.0830  130 LEU A CD1 
2007  C CD2 . LEU A 130 ? 0.7988 0.7268 0.6380 -0.1024 -0.0211 0.0704  130 LEU A CD2 
2019  N N   . GLN A 131 ? 1.0946 0.9219 0.9075 -0.0576 -0.0938 0.1252  131 GLN A N   
2020  C CA  . GLN A 131 ? 1.2319 1.0296 1.0133 -0.0637 -0.1069 0.1497  131 GLN A CA  
2021  C C   . GLN A 131 ? 1.3280 1.1091 1.0908 -0.0896 -0.0950 0.1590  131 GLN A C   
2022  O O   . GLN A 131 ? 1.3403 1.1101 1.1223 -0.0934 -0.0884 0.1531  131 GLN A O   
2023  C CB  . GLN A 131 ? 1.2575 1.0247 1.0512 -0.0424 -0.1263 0.1585  131 GLN A CB  
2024  C CG  . GLN A 131 ? 1.3180 1.0465 1.0833 -0.0472 -0.1415 0.1863  131 GLN A CG  
2025  C CD  . GLN A 131 ? 1.3416 1.0418 1.1249 -0.0218 -0.1610 0.1926  131 GLN A CD  
2026  O OE1 . GLN A 131 ? 1.3660 1.0250 1.1494 -0.0222 -0.1659 0.2021  131 GLN A OE1 
2027  N NE2 . GLN A 131 ? 1.3188 1.0412 1.1196 0.0002  -0.1713 0.1860  131 GLN A NE2 
2036  N N   . ASP A 132 ? 1.3968 1.1781 1.1214 -0.1091 -0.0920 0.1732  132 ASP A N   
2037  C CA  . ASP A 132 ? 1.4768 1.2427 1.1795 -0.1368 -0.0793 0.1846  132 ASP A CA  
2038  C C   . ASP A 132 ? 1.5466 1.2640 1.2237 -0.1391 -0.0977 0.2144  132 ASP A C   
2039  O O   . ASP A 132 ? 1.4844 1.1703 1.1780 -0.1360 -0.1021 0.2181  132 ASP A O   
2040  C CB  . ASP A 132 ? 1.4986 1.2926 1.1713 -0.1599 -0.0617 0.1818  132 ASP A CB  
2041  C CG  . ASP A 132 ? 1.5768 1.3691 1.2395 -0.1896 -0.0400 0.1844  132 ASP A CG  
2042  O OD1 . ASP A 132 ? 1.6803 1.4362 1.3334 -0.1994 -0.0456 0.2035  132 ASP A OD1 
2043  O OD2 . ASP A 132 ? 1.6247 1.4521 1.2919 -0.2033 -0.0166 0.1664  132 ASP A OD2 
2048  N N   . GLY A 133 ? 1.6318 1.3413 1.2682 -0.1447 -0.1096 0.2357  133 GLY A N   
2049  C CA  . GLY A 133 ? 1.7216 1.3839 1.3348 -0.1421 -0.1319 0.2670  133 GLY A CA  
2050  C C   . GLY A 133 ? 1.7169 1.3816 1.3324 -0.1152 -0.1579 0.2741  133 GLY A C   
2051  O O   . GLY A 133 ? 1.7522 1.4141 1.4061 -0.0875 -0.1683 0.2635  133 GLY A O   
2055  N N   . THR A 134 ? 1.6876 1.3605 1.2621 -0.1242 -0.1682 0.2914  134 THR A N   
2056  C CA  . THR A 134 ? 1.7052 1.3953 1.2857 -0.1011 -0.1913 0.2934  134 THR A CA  
2057  C C   . THR A 134 ? 1.5532 1.2940 1.1601 -0.0934 -0.1786 0.2605  134 THR A C   
2058  O O   . THR A 134 ? 1.5238 1.2800 1.1629 -0.0679 -0.1913 0.2506  134 THR A O   
2059  C CB  . THR A 134 ? 1.8286 1.5148 1.3544 -0.1156 -0.2081 0.3216  134 THR A CB  
2060  O OG1 . THR A 134 ? 1.8700 1.5828 1.3586 -0.1466 -0.1853 0.3129  134 THR A OG1 
2061  C CG2 . THR A 134 ? 1.8841 1.5147 1.3837 -0.1211 -0.2245 0.3587  134 THR A CG2 
2069  N N   . LYS A 135 ? 1.4684 1.2349 1.0643 -0.1153 -0.1525 0.2430  135 LYS A N   
2070  C CA  . LYS A 135 ? 1.3751 1.1859 0.9891 -0.1114 -0.1406 0.2142  135 LYS A CA  
2071  C C   . LYS A 135 ? 1.2523 1.0717 0.9210 -0.0902 -0.1336 0.1913  135 LYS A C   
2072  O O   . LYS A 135 ? 1.2495 1.0554 0.9371 -0.0927 -0.1211 0.1857  135 LYS A O   
2073  C CB  . LYS A 135 ? 1.3748 1.2072 0.9638 -0.1399 -0.1135 0.2014  135 LYS A CB  
2074  C CG  . LYS A 135 ? 1.3317 1.2053 0.9349 -0.1380 -0.1008 0.1721  135 LYS A CG  
2075  C CD  . LYS A 135 ? 1.3647 1.2537 0.9437 -0.1354 -0.1203 0.1769  135 LYS A CD  
2076  C CE  . LYS A 135 ? 1.3956 1.3211 0.9908 -0.1344 -0.1079 0.1464  135 LYS A CE  
2077  N NZ  . LYS A 135 ? 1.4387 1.3801 1.0171 -0.1579 -0.0779 0.1276  135 LYS A NZ  
2091  N N   . THR A 136 ? 1.1253 0.9686 0.8180 -0.0711 -0.1421 0.1783  136 THR A N   
2092  C CA  . THR A 136 ? 0.9988 0.8563 0.7376 -0.0535 -0.1342 0.1557  136 THR A CA  
2093  C C   . THR A 136 ? 0.9008 0.7964 0.6462 -0.0555 -0.1251 0.1349  136 THR A C   
2094  O O   . THR A 136 ? 0.8749 0.7853 0.6030 -0.0569 -0.1368 0.1386  136 THR A O   
2095  C CB  . THR A 136 ? 0.9790 0.8238 0.7453 -0.0263 -0.1537 0.1611  136 THR A CB  
2096  O OG1 . THR A 136 ? 1.0341 0.8383 0.7956 -0.0244 -0.1615 0.1786  136 THR A OG1 
2097  C CG2 . THR A 136 ? 0.9207 0.7825 0.7286 -0.0106 -0.1445 0.1380  136 THR A CG2 
2105  N N   . VAL A 137 ? 0.8378 0.7479 0.6083 -0.0561 -0.1055 0.1135  137 VAL A N   
2106  C CA  . VAL A 137 ? 0.8231 0.7636 0.6041 -0.0573 -0.0954 0.0927  137 VAL A CA  
2107  C C   . VAL A 137 ? 0.7843 0.7322 0.6078 -0.0402 -0.0906 0.0777  137 VAL A C   
2108  O O   . VAL A 137 ? 0.8093 0.7438 0.6508 -0.0343 -0.0869 0.0777  137 VAL A O   
2109  C CB  . VAL A 137 ? 0.8370 0.7896 0.6013 -0.0793 -0.0729 0.0806  137 VAL A CB  
2110  C CG1 . VAL A 137 ? 0.8842 0.8308 0.5996 -0.0994 -0.0759 0.0954  137 VAL A CG1 
2111  C CG2 . VAL A 137 ? 0.8236 0.7707 0.6095 -0.0823 -0.0556 0.0739  137 VAL A CG2 
2121  N N   . GLU A 138 ? 0.7536 0.7230 0.5911 -0.0340 -0.0910 0.0650  138 GLU A N   
2122  C CA  . GLU A 138 ? 0.7504 0.7280 0.6233 -0.0213 -0.0845 0.0513  138 GLU A CA  
2123  C C   . GLU A 138 ? 0.7602 0.7460 0.6428 -0.0306 -0.0640 0.0357  138 GLU A C   
2124  O O   . GLU A 138 ? 0.8025 0.7977 0.6691 -0.0450 -0.0539 0.0279  138 GLU A O   
2125  C CB  . GLU A 138 ? 0.7119 0.7081 0.5976 -0.0126 -0.0928 0.0453  138 GLU A CB  
2126  C CG  . GLU A 138 ? 0.6863 0.6872 0.6050 0.0017  -0.0892 0.0367  138 GLU A CG  
2127  C CD  . GLU A 138 ? 0.6568 0.6781 0.5895 0.0068  -0.0945 0.0304  138 GLU A CD  
2128  O OE1 . GLU A 138 ? 0.6775 0.7117 0.5965 -0.0027 -0.0992 0.0286  138 GLU A OE1 
2129  O OE2 . GLU A 138 ? 0.6408 0.6665 0.5971 0.0184  -0.0937 0.0267  138 GLU A OE2 
2136  N N   . TYR A 139 ? 0.6790 0.6618 0.5881 -0.0220 -0.0582 0.0305  139 TYR A N   
2137  C CA  . TYR A 139 ? 0.6536 0.6446 0.5802 -0.0268 -0.0413 0.0172  139 TYR A CA  
2138  C C   . TYR A 139 ? 0.6147 0.6107 0.5702 -0.0131 -0.0417 0.0102  139 TYR A C   
2139  O O   . TYR A 139 ? 0.6580 0.6469 0.6272 -0.0042 -0.0458 0.0139  139 TYR A O   
2140  C CB  . TYR A 139 ? 0.6470 0.6297 0.5752 -0.0338 -0.0347 0.0212  139 TYR A CB  
2141  C CG  . TYR A 139 ? 0.6399 0.6349 0.5943 -0.0359 -0.0193 0.0080  139 TYR A CG  
2142  C CD1 . TYR A 139 ? 0.6666 0.6757 0.6228 -0.0439 -0.0043 -0.0058 139 TYR A CD1 
2143  C CD2 . TYR A 139 ? 0.6196 0.6126 0.5980 -0.0296 -0.0205 0.0085  139 TYR A CD2 
2144  C CE1 . TYR A 139 ? 0.6406 0.6613 0.6268 -0.0430 0.0094  -0.0181 139 TYR A CE1 
2145  C CE2 . TYR A 139 ? 0.5960 0.6028 0.6027 -0.0298 -0.0092 -0.0020 139 TYR A CE2 
2146  C CZ  . TYR A 139 ? 0.5956 0.6161 0.6084 -0.0353 0.0059  -0.0150 139 TYR A CZ  
2147  O OH  . TYR A 139 ? 0.5963 0.6310 0.6431 -0.0328 0.0167  -0.0257 139 TYR A OH  
2157  N N   . ALA A 140 ? 0.5453 0.5522 0.5075 -0.0131 -0.0376 0.0002  140 ALA A N   
2158  C CA  . ALA A 140 ? 0.5476 0.5578 0.5340 -0.0030 -0.0369 -0.0050 140 ALA A CA  
2159  C C   . ALA A 140 ? 0.5392 0.5540 0.5408 -0.0076 -0.0225 -0.0183 140 ALA A C   
2160  O O   . ALA A 140 ? 0.5274 0.5466 0.5302 -0.0114 -0.0183 -0.0276 140 ALA A O   
2161  C CB  . ALA A 140 ? 0.5740 0.5908 0.5586 0.0011  -0.0456 -0.0040 140 ALA A CB  
2167  N N   . PRO A 141 ? 0.5574 0.5716 0.5739 -0.0073 -0.0149 -0.0204 141 PRO A N   
2168  C CA  . PRO A 141 ? 0.5749 0.5941 0.6116 -0.0093 -0.0006 -0.0341 141 PRO A CA  
2169  C C   . PRO A 141 ? 0.5998 0.6152 0.6580 -0.0002 -0.0014 -0.0371 141 PRO A C   
2170  O O   . PRO A 141 ? 0.6151 0.6303 0.6873 -0.0019 0.0094  -0.0497 141 PRO A O   
2171  C CB  . PRO A 141 ? 0.5788 0.6019 0.6323 -0.0087 0.0041  -0.0329 141 PRO A CB  
2172  C CG  . PRO A 141 ? 0.5805 0.5967 0.6286 -0.0029 -0.0101 -0.0187 141 PRO A CG  
2173  C CD  . PRO A 141 ? 0.5869 0.5966 0.6063 -0.0049 -0.0192 -0.0116 141 PRO A CD  
2181  N N   . CYS A 142 ? 0.5640 0.5749 0.6246 0.0086  -0.0128 -0.0263 142 CYS A N   
2182  C CA  . CYS A 142 ? 0.5746 0.5803 0.6512 0.0149  -0.0137 -0.0259 142 CYS A CA  
2183  C C   . CYS A 142 ? 0.6009 0.6071 0.6674 0.0100  -0.0149 -0.0288 142 CYS A C   
2184  O O   . CYS A 142 ? 0.6150 0.6152 0.6938 0.0116  -0.0133 -0.0294 142 CYS A O   
2185  C CB  . CYS A 142 ? 0.6096 0.6123 0.6912 0.0244  -0.0237 -0.0134 142 CYS A CB  
2186  S SG  . CYS A 142 ? 0.6778 0.6803 0.7867 0.0315  -0.0234 -0.0114 142 CYS A SG  
2192  N N   . ARG A 143 ? 0.6081 0.6215 0.6535 0.0035  -0.0187 -0.0295 143 ARG A N   
2193  C CA  . ARG A 143 ? 0.5933 0.6124 0.6316 -0.0032 -0.0209 -0.0341 143 ARG A CA  
2194  C C   . ARG A 143 ? 0.6129 0.6303 0.6512 -0.0140 -0.0098 -0.0505 143 ARG A C   
2195  O O   . ARG A 143 ? 0.6424 0.6670 0.6610 -0.0245 -0.0096 -0.0576 143 ARG A O   
2196  C CB  . ARG A 143 ? 0.5939 0.6231 0.6123 -0.0047 -0.0320 -0.0277 143 ARG A CB  
2197  C CG  . ARG A 143 ? 0.6078 0.6491 0.6241 -0.0103 -0.0376 -0.0309 143 ARG A CG  
2198  C CD  . ARG A 143 ? 0.6010 0.6534 0.6047 -0.0070 -0.0516 -0.0216 143 ARG A CD  
2199  N NE  . ARG A 143 ? 0.5965 0.6473 0.5761 -0.0136 -0.0547 -0.0200 143 ARG A NE  
2200  C CZ  . ARG A 143 ? 0.6431 0.6931 0.6097 -0.0087 -0.0662 -0.0077 143 ARG A CZ  
2201  N NH1 . ARG A 143 ? 0.6291 0.6801 0.6072 0.0047  -0.0749 0.0012  143 ARG A NH1 
2202  N NH2 . ARG A 143 ? 0.6984 0.7447 0.6395 -0.0175 -0.0681 -0.0045 143 ARG A NH2 
2216  N N   . SER A 144 ? 0.6333 0.6397 0.6934 -0.0112 -0.0009 -0.0568 144 SER A N   
2217  C CA  . SER A 144 ? 0.6087 0.6091 0.6746 -0.0190 0.0119  -0.0753 144 SER A CA  
2218  C C   . SER A 144 ? 0.6312 0.6242 0.7043 -0.0250 0.0123  -0.0814 144 SER A C   
2219  O O   . SER A 144 ? 0.6303 0.6290 0.7001 -0.0258 0.0029  -0.0719 144 SER A O   
2220  C CB  . SER A 144 ? 0.5936 0.5855 0.6847 -0.0102 0.0216  -0.0788 144 SER A CB  
2221  O OG  . SER A 144 ? 0.5634 0.5438 0.6767 0.0007  0.0169  -0.0678 144 SER A OG  
2227  N N   . GLN A 145 ? 0.6198 0.6000 0.7048 -0.0299 0.0245  -0.0986 145 GLN A N   
2228  C CA  . GLN A 145 ? 0.6346 0.6018 0.7298 -0.0372 0.0266  -0.1058 145 GLN A CA  
2229  C C   . GLN A 145 ? 0.6520 0.5968 0.7761 -0.0262 0.0292  -0.0977 145 GLN A C   
2230  O O   . GLN A 145 ? 0.6675 0.5948 0.8028 -0.0322 0.0322  -0.1021 145 GLN A O   
2231  C CB  . GLN A 145 ? 0.7402 0.7033 0.8278 -0.0512 0.0379  -0.1320 145 GLN A CB  
2232  C CG  . GLN A 145 ? 0.7779 0.7637 0.8314 -0.0646 0.0321  -0.1374 145 GLN A CG  
2233  C CD  . GLN A 145 ? 0.7689 0.7539 0.8069 -0.0780 0.0450  -0.1636 145 GLN A CD  
2234  O OE1 . GLN A 145 ? 0.8058 0.7731 0.8622 -0.0766 0.0604  -0.1809 145 GLN A OE1 
2235  N NE2 . GLN A 145 ? 0.7399 0.7440 0.7434 -0.0910 0.0387  -0.1667 145 GLN A NE2 
2244  N N   . ASP A 146 ? 0.6691 0.6134 0.8048 -0.0115 0.0266  -0.0848 146 ASP A N   
2245  C CA  . ASP A 146 ? 0.6452 0.5709 0.8052 0.0004  0.0244  -0.0718 146 ASP A CA  
2246  C C   . ASP A 146 ? 0.6392 0.5711 0.7879 0.0022  0.0122  -0.0501 146 ASP A C   
2247  O O   . ASP A 146 ? 0.6855 0.6298 0.8271 0.0100  0.0046  -0.0382 146 ASP A O   
2248  C CB  . ASP A 146 ? 0.6620 0.5893 0.8415 0.0141  0.0267  -0.0711 146 ASP A CB  
2249  C CG  . ASP A 146 ? 0.7270 0.6329 0.9368 0.0268  0.0245  -0.0612 146 ASP A CG  
2250  O OD1 . ASP A 146 ? 0.7685 0.6528 0.9827 0.0234  0.0237  -0.0566 146 ASP A OD1 
2251  O OD2 . ASP A 146 ? 0.7662 0.6771 0.9962 0.0395  0.0225  -0.0570 146 ASP A OD2 
2256  N N   . ILE A 147 ? 0.6120 0.5352 0.7593 -0.0063 0.0115  -0.0464 147 ILE A N   
2257  C CA  . ILE A 147 ? 0.6626 0.5993 0.7958 -0.0094 0.0039  -0.0322 147 ILE A CA  
2258  C C   . ILE A 147 ? 0.6776 0.5991 0.8171 -0.0038 0.0002  -0.0125 147 ILE A C   
2259  O O   . ILE A 147 ? 0.7291 0.6261 0.8853 0.0008  0.0021  -0.0086 147 ILE A O   
2260  C CB  . ILE A 147 ? 0.7518 0.6978 0.8782 -0.0257 0.0057  -0.0413 147 ILE A CB  
2261  C CG1 . ILE A 147 ? 0.8226 0.7440 0.9633 -0.0364 0.0140  -0.0519 147 ILE A CG1 
2262  C CG2 . ILE A 147 ? 0.7894 0.7577 0.9008 -0.0305 0.0036  -0.0543 147 ILE A CG2 
2263  C CD1 . ILE A 147 ? 0.8846 0.7906 1.0325 -0.0420 0.0144  -0.0375 147 ILE A CD1 
2275  N N   . ASP A 148 ? 0.6534 0.5899 0.7786 -0.0038 -0.0053 0.0002  148 ASP A N   
2276  C CA  . ASP A 148 ? 0.7237 0.6506 0.8454 -0.0020 -0.0085 0.0196  148 ASP A CA  
2277  C C   . ASP A 148 ? 0.7289 0.6500 0.8517 0.0124  -0.0163 0.0310  148 ASP A C   
2278  O O   . ASP A 148 ? 0.6853 0.6115 0.8151 0.0205  -0.0180 0.0230  148 ASP A O   
2279  C CB  . ASP A 148 ? 0.7502 0.6507 0.8832 -0.0113 -0.0031 0.0239  148 ASP A CB  
2280  C CG  . ASP A 148 ? 0.7337 0.6367 0.8550 -0.0215 -0.0017 0.0387  148 ASP A CG  
2281  O OD1 . ASP A 148 ? 0.6716 0.5895 0.7769 -0.0167 -0.0060 0.0497  148 ASP A OD1 
2282  O OD2 . ASP A 148 ? 0.7348 0.6251 0.8627 -0.0357 0.0049  0.0379  148 ASP A OD2 
2287  N N   . ALA A 149 ? 0.7429 0.6554 0.8577 0.0139  -0.0214 0.0498  149 ALA A N   
2288  C CA  . ALA A 149 ? 0.7702 0.6787 0.8856 0.0263  -0.0318 0.0617  149 ALA A CA  
2289  C C   . ALA A 149 ? 0.7509 0.6414 0.8945 0.0352  -0.0330 0.0591  149 ALA A C   
2290  O O   . ALA A 149 ? 0.6970 0.5947 0.8511 0.0462  -0.0397 0.0587  149 ALA A O   
2291  C CB  . ALA A 149 ? 0.8265 0.7272 0.9241 0.0236  -0.0374 0.0834  149 ALA A CB  
2297  N N   . ASP A 150 ? 0.7989 0.6542 0.7806 -0.0023 -0.0141 -0.0030 150 ASP A N   
2298  C CA  . ASP A 150 ? 0.8242 0.6650 0.8023 0.0071  -0.0148 -0.0019 150 ASP A CA  
2299  C C   . ASP A 150 ? 0.7398 0.5951 0.7204 0.0177  -0.0163 -0.0042 150 ASP A C   
2300  O O   . ASP A 150 ? 0.7142 0.5692 0.6942 0.0271  -0.0166 0.0007  150 ASP A O   
2301  C CB  . ASP A 150 ? 0.9736 0.7964 0.9494 0.0031  -0.0144 -0.0099 150 ASP A CB  
2302  C CG  . ASP A 150 ? 1.2058 1.0085 1.1773 -0.0074 -0.0133 -0.0047 150 ASP A CG  
2303  O OD1 . ASP A 150 ? 1.3109 1.1078 1.2785 -0.0070 -0.0133 0.0065  150 ASP A OD1 
2304  O OD2 . ASP A 150 ? 1.2962 1.0890 1.2676 -0.0169 -0.0127 -0.0114 150 ASP A OD2 
2309  N N   . GLY A 151 ? 0.7085 0.5782 0.6920 0.0159  -0.0175 -0.0112 151 GLY A N   
2310  C CA  . GLY A 151 ? 0.6604 0.5440 0.6442 0.0237  -0.0191 -0.0124 151 GLY A CA  
2311  C C   . GLY A 151 ? 0.6346 0.5348 0.6225 0.0238  -0.0217 -0.0064 151 GLY A C   
2312  O O   . GLY A 151 ? 0.6648 0.5655 0.6544 0.0239  -0.0217 0.0014  151 GLY A O   
2316  N N   . GLN A 152 ? 0.5994 0.5123 0.5884 0.0237  -0.0250 -0.0100 152 GLN A N   
2317  C CA  . GLN A 152 ? 0.5798 0.5055 0.5728 0.0241  -0.0292 -0.0046 152 GLN A CA  
2318  C C   . GLN A 152 ? 0.5675 0.4990 0.5668 0.0186  -0.0329 -0.0096 152 GLN A C   
2319  O O   . GLN A 152 ? 0.5788 0.5196 0.5820 0.0198  -0.0384 -0.0076 152 GLN A O   
2320  C CB  . GLN A 152 ? 0.5695 0.5054 0.5587 0.0288  -0.0314 -0.0024 152 GLN A CB  
2321  C CG  . GLN A 152 ? 0.5994 0.5346 0.5839 0.0349  -0.0269 -0.0001 152 GLN A CG  
2322  C CD  . GLN A 152 ? 0.6466 0.5949 0.6254 0.0378  -0.0277 0.0001  152 GLN A CD  
2323  O OE1 . GLN A 152 ? 0.6791 0.6286 0.6522 0.0382  -0.0272 -0.0081 152 GLN A OE1 
2324  N NE2 . GLN A 152 ? 0.6509 0.6099 0.6307 0.0386  -0.0289 0.0097  152 GLN A NE2 
2333  N N   . GLY A 153 ? 0.5739 0.5004 0.5752 0.0125  -0.0304 -0.0162 153 GLY A N   
2334  C CA  . GLY A 153 ? 0.6006 0.5367 0.6100 0.0076  -0.0334 -0.0229 153 GLY A CA  
2335  C C   . GLY A 153 ? 0.5752 0.5183 0.5914 0.0075  -0.0352 -0.0197 153 GLY A C   
2336  O O   . GLY A 153 ? 0.5404 0.4945 0.5650 0.0076  -0.0401 -0.0245 153 GLY A O   
2340  N N   . PHE A 154 ? 0.6008 0.5380 0.6137 0.0079  -0.0319 -0.0123 154 PHE A N   
2341  C CA  . PHE A 154 ? 0.6372 0.5806 0.6550 0.0076  -0.0334 -0.0102 154 PHE A CA  
2342  C C   . PHE A 154 ? 0.6411 0.5838 0.6574 0.0135  -0.0368 -0.0013 154 PHE A C   
2343  O O   . PHE A 154 ? 0.6369 0.5807 0.6542 0.0133  -0.0370 0.0023  154 PHE A O   
2344  C CB  . PHE A 154 ? 0.6215 0.5613 0.6361 0.0012  -0.0274 -0.0093 154 PHE A CB  
2345  C CG  . PHE A 154 ? 0.6059 0.5505 0.6240 -0.0070 -0.0240 -0.0180 154 PHE A CG  
2346  C CD1 . PHE A 154 ? 0.6313 0.5686 0.6468 -0.0108 -0.0219 -0.0214 154 PHE A CD1 
2347  C CD2 . PHE A 154 ? 0.6397 0.5980 0.6646 -0.0115 -0.0230 -0.0240 154 PHE A CD2 
2348  C CE1 . PHE A 154 ? 0.6475 0.5908 0.6675 -0.0201 -0.0189 -0.0293 154 PHE A CE1 
2349  C CE2 . PHE A 154 ? 0.6497 0.6166 0.6793 -0.0202 -0.0192 -0.0323 154 PHE A CE2 
2350  C CZ  . PHE A 154 ? 0.6420 0.6013 0.6693 -0.0251 -0.0172 -0.0344 154 PHE A CZ  
2360  N N   . CYS A 155 ? 0.6466 0.5892 0.6604 0.0178  -0.0395 0.0019  155 CYS A N   
2361  C CA  . CYS A 155 ? 0.6271 0.5703 0.6390 0.0218  -0.0413 0.0112  155 CYS A CA  
2362  C C   . CYS A 155 ? 0.6201 0.5680 0.6387 0.0221  -0.0482 0.0135  155 CYS A C   
2363  O O   . CYS A 155 ? 0.6424 0.5906 0.6614 0.0230  -0.0495 0.0207  155 CYS A O   
2364  C CB  . CYS A 155 ? 0.6563 0.6011 0.6628 0.0249  -0.0414 0.0132  155 CYS A CB  
2365  S SG  . CYS A 155 ? 0.7172 0.6693 0.7236 0.0269  -0.0467 0.0232  155 CYS A SG  
2371  N N   . GLN A 156 ? 0.5704 0.5220 0.5955 0.0217  -0.0536 0.0070  156 GLN A N   
2372  C CA  . GLN A 156 ? 0.5682 0.5213 0.6008 0.0232  -0.0619 0.0079  156 GLN A CA  
2373  C C   . GLN A 156 ? 0.5369 0.4880 0.5663 0.0243  -0.0664 0.0190  156 GLN A C   
2374  O O   . GLN A 156 ? 0.5573 0.5066 0.5899 0.0238  -0.0700 0.0242  156 GLN A O   
2375  C CB  . GLN A 156 ? 0.5508 0.5048 0.5878 0.0218  -0.0607 0.0052  156 GLN A CB  
2376  C CG  . GLN A 156 ? 0.5802 0.5393 0.6199 0.0190  -0.0556 -0.0052 156 GLN A CG  
2377  C CD  . GLN A 156 ? 0.6195 0.5826 0.6631 0.0178  -0.0557 -0.0093 156 GLN A CD  
2378  O OE1 . GLN A 156 ? 0.6539 0.6174 0.6914 0.0142  -0.0493 -0.0080 156 GLN A OE1 
2379  N NE2 . GLN A 156 ? 0.6136 0.5793 0.6669 0.0212  -0.0637 -0.0145 156 GLN A NE2 
2388  N N   . GLY A 157 ? 0.5291 0.4818 0.5519 0.0249  -0.0660 0.0224  157 GLY A N   
2389  C CA  . GLY A 157 ? 0.5306 0.4845 0.5488 0.0243  -0.0691 0.0334  157 GLY A CA  
2390  C C   . GLY A 157 ? 0.5990 0.5491 0.6228 0.0236  -0.0802 0.0380  157 GLY A C   
2391  O O   . GLY A 157 ? 0.6205 0.5685 0.6486 0.0255  -0.0875 0.0330  157 GLY A O   
2395  N N   . GLY A 158 ? 0.5996 0.5482 0.6243 0.0210  -0.0824 0.0474  158 GLY A N   
2396  C CA  . GLY A 158 ? 0.5310 0.4720 0.5618 0.0194  -0.0937 0.0522  158 GLY A CA  
2397  C C   . GLY A 158 ? 0.4708 0.4072 0.5111 0.0195  -0.0959 0.0476  158 GLY A C   
2398  O O   . GLY A 158 ? 0.5042 0.4321 0.5506 0.0182  -0.1058 0.0506  158 GLY A O   
2402  N N   . PHE A 159 ? 0.4742 0.4150 0.5150 0.0207  -0.0876 0.0404  159 PHE A N   
2403  C CA  . PHE A 159 ? 0.4988 0.4381 0.5457 0.0200  -0.0886 0.0363  159 PHE A CA  
2404  C C   . PHE A 159 ? 0.5312 0.4676 0.5801 0.0158  -0.0937 0.0463  159 PHE A C   
2405  O O   . PHE A 159 ? 0.5972 0.5287 0.6529 0.0149  -0.0997 0.0428  159 PHE A O   
2406  C CB  . PHE A 159 ? 0.5383 0.4836 0.5807 0.0203  -0.0780 0.0325  159 PHE A CB  
2407  C CG  . PHE A 159 ? 0.5918 0.5379 0.6380 0.0196  -0.0782 0.0262  159 PHE A CG  
2408  C CD1 . PHE A 159 ? 0.6179 0.5661 0.6680 0.0211  -0.0779 0.0138  159 PHE A CD1 
2409  C CD2 . PHE A 159 ? 0.5870 0.5347 0.6327 0.0172  -0.0785 0.0320  159 PHE A CD2 
2410  C CE1 . PHE A 159 ? 0.6234 0.5749 0.6751 0.0201  -0.0774 0.0073  159 PHE A CE1 
2411  C CE2 . PHE A 159 ? 0.5728 0.5225 0.6202 0.0164  -0.0791 0.0257  159 PHE A CE2 
2412  C CZ  . PHE A 159 ? 0.5918 0.5433 0.6412 0.0177  -0.0782 0.0133  159 PHE A CZ  
2422  N N   . SER A 160 ? 0.5349 0.4755 0.5782 0.0125  -0.0915 0.0579  160 SER A N   
2423  C CA  . SER A 160 ? 0.5575 0.4979 0.6032 0.0065  -0.0960 0.0687  160 SER A CA  
2424  C C   . SER A 160 ? 0.5953 0.5414 0.6341 0.0028  -0.0947 0.0803  160 SER A C   
2425  O O   . SER A 160 ? 0.5976 0.5520 0.6291 0.0057  -0.0867 0.0794  160 SER A O   
2426  C CB  . SER A 160 ? 0.5138 0.4627 0.5613 0.0050  -0.0905 0.0695  160 SER A CB  
2427  O OG  . SER A 160 ? 0.4943 0.4545 0.5357 0.0073  -0.0803 0.0719  160 SER A OG  
2433  N N   . ILE A 161 ? 0.6207 0.5623 0.6611 -0.0042 -0.1026 0.0910  161 ILE A N   
2434  C CA  . ILE A 161 ? 0.6195 0.5673 0.6518 -0.0095 -0.1022 0.1033  161 ILE A CA  
2435  C C   . ILE A 161 ? 0.6300 0.5792 0.6655 -0.0202 -0.1066 0.1165  161 ILE A C   
2436  O O   . ILE A 161 ? 0.6721 0.6122 0.7167 -0.0232 -0.1133 0.1156  161 ILE A O   
2437  C CB  . ILE A 161 ? 0.6150 0.5516 0.6424 -0.0079 -0.1106 0.1044  161 ILE A CB  
2438  C CG1 . ILE A 161 ? 0.6347 0.5512 0.6714 -0.0077 -0.1248 0.1025  161 ILE A CG1 
2439  C CG2 . ILE A 161 ? 0.5953 0.5357 0.6187 0.0007  -0.1048 0.0926  161 ILE A CG2 
2440  C CD1 . ILE A 161 ? 0.6893 0.5938 0.7230 -0.0052 -0.1357 0.1046  161 ILE A CD1 
2452  N N   . ASP A 162 ? 0.6374 0.5995 0.6650 -0.0266 -0.1025 0.1281  162 ASP A N   
2453  C CA  . ASP A 162 ? 0.6618 0.6276 0.6910 -0.0394 -0.1063 0.1429  162 ASP A CA  
2454  C C   . ASP A 162 ? 0.6837 0.6646 0.7002 -0.0452 -0.1013 0.1541  162 ASP A C   
2455  O O   . ASP A 162 ? 0.6379 0.6309 0.6463 -0.0383 -0.0924 0.1483  162 ASP A O   
2456  C CB  . ASP A 162 ? 0.6689 0.6491 0.7078 -0.0426 -0.1007 0.1425  162 ASP A CB  
2457  C CG  . ASP A 162 ? 0.7036 0.6805 0.7488 -0.0566 -0.1087 0.1548  162 ASP A CG  
2458  O OD1 . ASP A 162 ? 0.7433 0.7073 0.7837 -0.0647 -0.1176 0.1659  162 ASP A OD1 
2459  O OD2 . ASP A 162 ? 0.7414 0.7280 0.7964 -0.0599 -0.1069 0.1538  162 ASP A OD2 
2464  N N   . PHE A 163 ? 0.7506 0.7306 0.7648 -0.0586 -0.1072 0.1700  163 PHE A N   
2465  C CA  . PHE A 163 ? 0.7497 0.7479 0.7510 -0.0672 -0.1020 0.1827  163 PHE A CA  
2466  C C   . PHE A 163 ? 0.7534 0.7794 0.7600 -0.0756 -0.0917 0.1883  163 PHE A C   
2467  O O   . PHE A 163 ? 0.7774 0.8017 0.7969 -0.0813 -0.0949 0.1901  163 PHE A O   
2468  C CB  . PHE A 163 ? 0.7577 0.7379 0.7511 -0.0786 -0.1154 0.1994  163 PHE A CB  
2469  C CG  . PHE A 163 ? 0.7603 0.7201 0.7457 -0.0705 -0.1249 0.1962  163 PHE A CG  
2470  C CD1 . PHE A 163 ? 0.7739 0.7457 0.7435 -0.0676 -0.1201 0.1969  163 PHE A CD1 
2471  C CD2 . PHE A 163 ? 0.7604 0.6906 0.7548 -0.0656 -0.1393 0.1918  163 PHE A CD2 
2472  C CE1 . PHE A 163 ? 0.7837 0.7388 0.7469 -0.0603 -0.1299 0.1939  163 PHE A CE1 
2473  C CE2 . PHE A 163 ? 0.7900 0.7042 0.7794 -0.0574 -0.1487 0.1883  163 PHE A CE2 
2474  C CZ  . PHE A 163 ? 0.7815 0.7083 0.7554 -0.0550 -0.1443 0.1899  163 PHE A CZ  
2484  N N   . THR A 164 ? 0.7336 0.7872 0.7311 -0.0761 -0.0798 0.1898  164 THR A N   
2485  C CA  . THR A 164 ? 0.7161 0.8007 0.7181 -0.0858 -0.0704 0.1969  164 THR A CA  
2486  C C   . THR A 164 ? 0.7726 0.8607 0.7650 -0.1047 -0.0750 0.2173  164 THR A C   
2487  O O   . THR A 164 ? 0.7816 0.8523 0.7599 -0.1078 -0.0832 0.2253  164 THR A O   
2488  C CB  . THR A 164 ? 0.6698 0.7852 0.6682 -0.0766 -0.0546 0.1868  164 THR A CB  
2489  O OG1 . THR A 164 ? 0.6394 0.7653 0.6194 -0.0804 -0.0513 0.1926  164 THR A OG1 
2490  C CG2 . THR A 164 ? 0.6681 0.7729 0.6704 -0.0580 -0.0519 0.1682  164 THR A CG2 
2498  N N   . LYS A 165 ? 0.8525 0.9642 0.8525 -0.1179 -0.0700 0.2265  165 LYS A N   
2499  C CA  . LYS A 165 ? 0.9859 1.1012 0.9771 -0.1389 -0.0743 0.2478  165 LYS A CA  
2500  C C   . LYS A 165 ? 0.9694 1.1029 0.9390 -0.1418 -0.0673 0.2541  165 LYS A C   
2501  O O   . LYS A 165 ? 0.9538 1.0829 0.9102 -0.1581 -0.0734 0.2731  165 LYS A O   
2502  C CB  . LYS A 165 ? 1.0777 1.2206 1.0829 -0.1534 -0.0686 0.2552  165 LYS A CB  
2503  C CG  . LYS A 165 ? 1.1483 1.3400 1.1548 -0.1520 -0.0502 0.2502  165 LYS A CG  
2504  C CD  . LYS A 165 ? 1.2341 1.4537 1.2538 -0.1706 -0.0465 0.2613  165 LYS A CD  
2505  C CE  . LYS A 165 ? 1.3096 1.5820 1.3323 -0.1694 -0.0281 0.2560  165 LYS A CE  
2506  N NZ  . LYS A 165 ? 1.3762 1.6804 1.4131 -0.1890 -0.0241 0.2670  165 LYS A NZ  
2520  N N   . ALA A 166 ? 0.9092 1.0620 0.8740 -0.1267 -0.0553 0.2387  166 ALA A N   
2521  C CA  . ALA A 166 ? 0.8693 1.0424 0.8133 -0.1280 -0.0477 0.2411  166 ALA A CA  
2522  C C   . ALA A 166 ? 0.9428 1.0907 0.8733 -0.1155 -0.0548 0.2336  166 ALA A C   
2523  O O   . ALA A 166 ? 0.9498 1.1147 0.8666 -0.1087 -0.0466 0.2258  166 ALA A O   
2524  C CB  . ALA A 166 ? 0.7664 0.9821 0.7145 -0.1204 -0.0292 0.2278  166 ALA A CB  
2530  N N   . ASP A 167 ? 1.0293 1.1382 0.9643 -0.1120 -0.0700 0.2346  167 ASP A N   
2531  C CA  . ASP A 167 ? 1.1599 1.2453 1.0844 -0.1014 -0.0786 0.2286  167 ASP A CA  
2532  C C   . ASP A 167 ? 1.0976 1.1929 1.0236 -0.0832 -0.0683 0.2063  167 ASP A C   
2533  O O   . ASP A 167 ? 1.1357 1.2364 1.0467 -0.0779 -0.0661 0.2011  167 ASP A O   
2534  C CB  . ASP A 167 ? 1.3320 1.4196 1.2329 -0.1121 -0.0837 0.2447  167 ASP A CB  
2535  C CG  . ASP A 167 ? 1.5186 1.5844 1.4174 -0.1287 -0.0985 0.2675  167 ASP A CG  
2536  O OD1 . ASP A 167 ? 1.5669 1.5972 1.4744 -0.1243 -0.1137 0.2674  167 ASP A OD1 
2537  O OD2 . ASP A 167 ? 1.5811 1.6654 1.4700 -0.1465 -0.0951 0.2851  167 ASP A OD2 
2542  N N   . ARG A 168 ? 0.9505 1.0476 0.8943 -0.0744 -0.0625 0.1934  168 ARG A N   
2543  C CA  . ARG A 168 ? 0.8196 0.9130 0.7681 -0.0571 -0.0572 0.1732  168 ARG A CA  
2544  C C   . ARG A 168 ? 0.7995 0.8619 0.7608 -0.0508 -0.0677 0.1674  168 ARG A C   
2545  O O   . ARG A 168 ? 0.8207 0.8719 0.7927 -0.0573 -0.0746 0.1746  168 ARG A O   
2546  C CB  . ARG A 168 ? 0.7515 0.8710 0.7096 -0.0506 -0.0427 0.1625  168 ARG A CB  
2547  C CG  . ARG A 168 ? 0.7303 0.8736 0.6771 -0.0440 -0.0309 0.1526  168 ARG A CG  
2548  C CD  . ARG A 168 ? 0.7226 0.8855 0.6821 -0.0337 -0.0189 0.1393  168 ARG A CD  
2549  N NE  . ARG A 168 ? 0.7830 0.9698 0.7327 -0.0272 -0.0077 0.1286  168 ARG A NE  
2550  C CZ  . ARG A 168 ? 0.8197 0.9971 0.7633 -0.0152 -0.0060 0.1135  168 ARG A CZ  
2551  N NH1 . ARG A 168 ? 0.8049 0.9513 0.7514 -0.0090 -0.0141 0.1080  168 ARG A NH1 
2552  N NH2 . ARG A 168 ? 0.8847 1.0849 0.8196 -0.0098 0.0040  0.1030  168 ARG A NH2 
2566  N N   . VAL A 169 ? 0.7274 0.7772 0.6875 -0.0387 -0.0687 0.1538  169 VAL A N   
2567  C CA  . VAL A 169 ? 0.6752 0.7013 0.6476 -0.0315 -0.0758 0.1451  169 VAL A CA  
2568  C C   . VAL A 169 ? 0.6339 0.6679 0.6167 -0.0228 -0.0658 0.1324  169 VAL A C   
2569  O O   . VAL A 169 ? 0.6114 0.6611 0.5902 -0.0167 -0.0553 0.1244  169 VAL A O   
2570  C CB  . VAL A 169 ? 0.6792 0.6889 0.6457 -0.0243 -0.0829 0.1376  169 VAL A CB  
2571  C CG1 . VAL A 169 ? 0.6456 0.6384 0.6252 -0.0154 -0.0858 0.1245  169 VAL A CG1 
2572  C CG2 . VAL A 169 ? 0.7609 0.7573 0.7200 -0.0318 -0.0966 0.1512  169 VAL A CG2 
2582  N N   . LEU A 170 ? 0.6292 0.6521 0.6252 -0.0222 -0.0698 0.1306  170 LEU A N   
2583  C CA  . LEU A 170 ? 0.6240 0.6485 0.6289 -0.0134 -0.0634 0.1190  170 LEU A CA  
2584  C C   . LEU A 170 ? 0.6523 0.6548 0.6612 -0.0075 -0.0700 0.1096  170 LEU A C   
2585  O O   . LEU A 170 ? 0.7060 0.6936 0.7202 -0.0112 -0.0801 0.1127  170 LEU A O   
2586  C CB  . LEU A 170 ? 0.5953 0.6297 0.6116 -0.0178 -0.0620 0.1237  170 LEU A CB  
2587  C CG  . LEU A 170 ? 0.5946 0.6295 0.6191 -0.0087 -0.0572 0.1133  170 LEU A CG  
2588  C CD1 . LEU A 170 ? 0.5669 0.6139 0.5868 0.0007  -0.0465 0.1051  170 LEU A CD1 
2589  C CD2 . LEU A 170 ? 0.6245 0.6699 0.6605 -0.0135 -0.0578 0.1185  170 LEU A CD2 
2601  N N   . LEU A 171 ? 0.6446 0.6454 0.6513 0.0014  -0.0644 0.0978  171 LEU A N   
2602  C CA  . LEU A 171 ? 0.5886 0.5730 0.5982 0.0063  -0.0689 0.0880  171 LEU A CA  
2603  C C   . LEU A 171 ? 0.5779 0.5620 0.5918 0.0124  -0.0620 0.0788  171 LEU A C   
2604  O O   . LEU A 171 ? 0.6095 0.6028 0.6204 0.0164  -0.0535 0.0762  171 LEU A O   
2605  C CB  . LEU A 171 ? 0.5929 0.5741 0.5941 0.0090  -0.0703 0.0833  171 LEU A CB  
2606  C CG  . LEU A 171 ? 0.5819 0.5505 0.5873 0.0136  -0.0744 0.0723  171 LEU A CG  
2607  C CD1 . LEU A 171 ? 0.6088 0.5732 0.6094 0.0133  -0.0826 0.0729  171 LEU A CD1 
2608  C CD2 . LEU A 171 ? 0.5372 0.5076 0.5414 0.0189  -0.0653 0.0613  171 LEU A CD2 
2620  N N   . GLY A 172 ? 0.5682 0.5417 0.5887 0.0132  -0.0663 0.0739  172 GLY A N   
2621  C CA  . GLY A 172 ? 0.5514 0.5233 0.5744 0.0175  -0.0611 0.0668  172 GLY A CA  
2622  C C   . GLY A 172 ? 0.5826 0.5454 0.6045 0.0203  -0.0612 0.0563  172 GLY A C   
2623  O O   . GLY A 172 ? 0.5506 0.5072 0.5754 0.0194  -0.0680 0.0533  172 GLY A O   
2627  N N   . GLY A 173 ? 0.5695 0.5316 0.5882 0.0238  -0.0541 0.0508  173 GLY A N   
2628  C CA  . GLY A 173 ? 0.6063 0.5616 0.6244 0.0246  -0.0528 0.0413  173 GLY A CA  
2629  C C   . GLY A 173 ? 0.6064 0.5587 0.6231 0.0255  -0.0474 0.0391  173 GLY A C   
2630  O O   . GLY A 173 ? 0.5896 0.5404 0.6018 0.0282  -0.0418 0.0393  173 GLY A O   
2634  N N   . PRO A 174 ? 0.5723 0.5231 0.5923 0.0234  -0.0496 0.0369  174 PRO A N   
2635  C CA  . PRO A 174 ? 0.5530 0.5020 0.5699 0.0234  -0.0457 0.0379  174 PRO A CA  
2636  C C   . PRO A 174 ? 0.5505 0.4929 0.5617 0.0226  -0.0400 0.0331  174 PRO A C   
2637  O O   . PRO A 174 ? 0.5443 0.4831 0.5511 0.0220  -0.0374 0.0356  174 PRO A O   
2638  C CB  . PRO A 174 ? 0.6186 0.5699 0.6395 0.0205  -0.0503 0.0353  174 PRO A CB  
2639  C CG  . PRO A 174 ? 0.6473 0.5986 0.6740 0.0197  -0.0549 0.0286  174 PRO A CG  
2640  C CD  . PRO A 174 ? 0.6065 0.5575 0.6332 0.0214  -0.0565 0.0330  174 PRO A CD  
2648  N N   . GLY A 175 ? 0.5611 0.5016 0.5721 0.0218  -0.0387 0.0269  175 GLY A N   
2649  C CA  . GLY A 175 ? 0.5377 0.4721 0.5447 0.0186  -0.0339 0.0218  175 GLY A CA  
2650  C C   . GLY A 175 ? 0.5418 0.4678 0.5436 0.0207  -0.0299 0.0219  175 GLY A C   
2651  O O   . GLY A 175 ? 0.5512 0.4689 0.5491 0.0171  -0.0263 0.0192  175 GLY A O   
2655  N N   . SER A 176 ? 0.5520 0.4804 0.5536 0.0261  -0.0305 0.0247  176 SER A N   
2656  C CA  . SER A 176 ? 0.5851 0.5069 0.5823 0.0292  -0.0271 0.0218  176 SER A CA  
2657  C C   . SER A 176 ? 0.5925 0.5019 0.5858 0.0309  -0.0240 0.0247  176 SER A C   
2658  O O   . SER A 176 ? 0.5766 0.4863 0.5702 0.0328  -0.0249 0.0317  176 SER A O   
2659  C CB  . SER A 176 ? 0.6249 0.5557 0.6222 0.0349  -0.0275 0.0243  176 SER A CB  
2660  O OG  . SER A 176 ? 0.6163 0.5555 0.6146 0.0328  -0.0310 0.0225  176 SER A OG  
2666  N N   . PHE A 177 ? 0.6145 0.5117 0.6041 0.0301  -0.0214 0.0193  177 PHE A N   
2667  C CA  . PHE A 177 ? 0.6688 0.5498 0.6543 0.0330  -0.0198 0.0219  177 PHE A CA  
2668  C C   . PHE A 177 ? 0.7233 0.5980 0.7059 0.0279  -0.0203 0.0291  177 PHE A C   
2669  O O   . PHE A 177 ? 0.6910 0.5632 0.6726 0.0326  -0.0219 0.0368  177 PHE A O   
2670  C CB  . PHE A 177 ? 0.6780 0.5626 0.6656 0.0440  -0.0199 0.0245  177 PHE A CB  
2671  C CG  . PHE A 177 ? 0.7026 0.6006 0.6919 0.0479  -0.0190 0.0190  177 PHE A CG  
2672  C CD1 . PHE A 177 ? 0.7182 0.6135 0.7046 0.0452  -0.0181 0.0097  177 PHE A CD1 
2673  C CD2 . PHE A 177 ? 0.7098 0.6245 0.7030 0.0531  -0.0193 0.0234  177 PHE A CD2 
2674  C CE1 . PHE A 177 ? 0.7202 0.6290 0.7058 0.0482  -0.0176 0.0053  177 PHE A CE1 
2675  C CE2 . PHE A 177 ? 0.7025 0.6309 0.6952 0.0551  -0.0182 0.0197  177 PHE A CE2 
2676  C CZ  . PHE A 177 ? 0.6969 0.6221 0.6849 0.0528  -0.0174 0.0108  177 PHE A CZ  
2686  N N   . TYR A 178 ? 0.6724 0.5466 0.6536 0.0179  -0.0191 0.0261  178 TYR A N   
2687  C CA  . TYR A 178 ? 0.6334 0.5061 0.6102 0.0109  -0.0186 0.0318  178 TYR A CA  
2688  C C   . TYR A 178 ? 0.5766 0.4616 0.5553 0.0147  -0.0215 0.0378  178 TYR A C   
2689  O O   . TYR A 178 ? 0.5762 0.4567 0.5500 0.0159  -0.0230 0.0461  178 TYR A O   
2690  C CB  . TYR A 178 ? 0.6755 0.5270 0.6441 0.0088  -0.0179 0.0379  178 TYR A CB  
2691  C CG  . TYR A 178 ? 0.7433 0.5857 0.7085 -0.0030 -0.0147 0.0337  178 TYR A CG  
2692  C CD1 . TYR A 178 ? 0.7652 0.6166 0.7280 -0.0146 -0.0120 0.0339  178 TYR A CD1 
2693  C CD2 . TYR A 178 ? 0.7888 0.6156 0.7539 -0.0032 -0.0141 0.0284  178 TYR A CD2 
2694  C CE1 . TYR A 178 ? 0.8031 0.6498 0.7642 -0.0269 -0.0084 0.0301  178 TYR A CE1 
2695  C CE2 . TYR A 178 ? 0.8303 0.6496 0.7934 -0.0157 -0.0114 0.0245  178 TYR A CE2 
2696  C CZ  . TYR A 178 ? 0.8589 0.6890 0.8204 -0.0279 -0.0084 0.0258  178 TYR A CZ  
2697  O OH  . TYR A 178 ? 0.9194 0.7453 0.8801 -0.0418 -0.0051 0.0220  178 TYR A OH  
2707  N N   . TRP A 179 ? 0.5722 0.4722 0.5580 0.0163  -0.0233 0.0338  179 TRP A N   
2708  C CA  . TRP A 179 ? 0.5368 0.4488 0.5260 0.0180  -0.0268 0.0374  179 TRP A CA  
2709  C C   . TRP A 179 ? 0.5416 0.4535 0.5309 0.0254  -0.0290 0.0456  179 TRP A C   
2710  O O   . TRP A 179 ? 0.5380 0.4574 0.5284 0.0256  -0.0321 0.0500  179 TRP A O   
2711  C CB  . TRP A 179 ? 0.5228 0.4389 0.5086 0.0107  -0.0264 0.0369  179 TRP A CB  
2712  C CG  . TRP A 179 ? 0.5001 0.4235 0.4903 0.0051  -0.0250 0.0269  179 TRP A CG  
2713  C CD1 . TRP A 179 ? 0.5136 0.4488 0.5123 0.0061  -0.0285 0.0208  179 TRP A CD1 
2714  C CD2 . TRP A 179 ? 0.5361 0.4563 0.5244 -0.0021 -0.0206 0.0216  179 TRP A CD2 
2715  N NE1 . TRP A 179 ? 0.5430 0.4838 0.5459 0.0015  -0.0267 0.0113  179 TRP A NE1 
2716  C CE2 . TRP A 179 ? 0.5429 0.4762 0.5397 -0.0043 -0.0214 0.0115  179 TRP A CE2 
2717  C CE3 . TRP A 179 ? 0.5782 0.4849 0.5590 -0.0072 -0.0167 0.0244  179 TRP A CE3 
2718  C CZ2 . TRP A 179 ? 0.5394 0.4767 0.5386 -0.0115 -0.0177 0.0036  179 TRP A CZ2 
2719  C CZ3 . TRP A 179 ? 0.5998 0.5084 0.5819 -0.0160 -0.0129 0.0173  179 TRP A CZ3 
2720  C CH2 . TRP A 179 ? 0.5857 0.5114 0.5774 -0.0181 -0.0131 0.0067  179 TRP A CH2 
2731  N N   . GLN A 180 ? 0.5512 0.4564 0.5406 0.0319  -0.0277 0.0464  180 GLN A N   
2732  C CA  . GLN A 180 ? 0.5523 0.4643 0.5460 0.0402  -0.0296 0.0516  180 GLN A CA  
2733  C C   . GLN A 180 ? 0.5285 0.4573 0.5294 0.0400  -0.0316 0.0514  180 GLN A C   
2734  O O   . GLN A 180 ? 0.5925 0.5316 0.5980 0.0423  -0.0344 0.0568  180 GLN A O   
2735  C CB  . GLN A 180 ? 0.5623 0.4669 0.5563 0.0480  -0.0273 0.0492  180 GLN A CB  
2736  C CG  . GLN A 180 ? 0.5486 0.4332 0.5367 0.0501  -0.0273 0.0516  180 GLN A CG  
2737  C CD  . GLN A 180 ? 0.5960 0.4726 0.5860 0.0596  -0.0260 0.0471  180 GLN A CD  
2738  O OE1 . GLN A 180 ? 0.6169 0.5070 0.6125 0.0653  -0.0243 0.0428  180 GLN A OE1 
2739  N NE2 . GLN A 180 ? 0.6217 0.4760 0.6067 0.0609  -0.0268 0.0478  180 GLN A NE2 
2748  N N   . GLY A 181 ? 0.5563 0.4877 0.5583 0.0368  -0.0311 0.0456  181 GLY A N   
2749  C CA  . GLY A 181 ? 0.6049 0.5487 0.6122 0.0360  -0.0338 0.0467  181 GLY A CA  
2750  C C   . GLY A 181 ? 0.6135 0.5640 0.6215 0.0409  -0.0314 0.0468  181 GLY A C   
2751  O O   . GLY A 181 ? 0.6336 0.5800 0.6394 0.0465  -0.0278 0.0447  181 GLY A O   
2755  N N   . GLN A 182 ? 0.6102 0.5712 0.6209 0.0385  -0.0338 0.0490  182 GLN A N   
2756  C CA  . GLN A 182 ? 0.5905 0.5610 0.5998 0.0413  -0.0310 0.0488  182 GLN A CA  
2757  C C   . GLN A 182 ? 0.5750 0.5573 0.5870 0.0365  -0.0348 0.0554  182 GLN A C   
2758  O O   . GLN A 182 ? 0.5677 0.5456 0.5814 0.0314  -0.0404 0.0567  182 GLN A O   
2759  C CB  . GLN A 182 ? 0.6031 0.5666 0.6060 0.0417  -0.0290 0.0406  182 GLN A CB  
2760  C CG  . GLN A 182 ? 0.6393 0.6136 0.6382 0.0445  -0.0259 0.0387  182 GLN A CG  
2761  C CD  . GLN A 182 ? 0.6584 0.6254 0.6508 0.0448  -0.0246 0.0291  182 GLN A CD  
2762  O OE1 . GLN A 182 ? 0.6637 0.6217 0.6555 0.0406  -0.0276 0.0256  182 GLN A OE1 
2763  N NE2 . GLN A 182 ? 0.6879 0.6603 0.6759 0.0498  -0.0201 0.0237  182 GLN A NE2 
2772  N N   . LEU A 183 ? 0.5744 0.5718 0.5873 0.0381  -0.0318 0.0593  183 LEU A N   
2773  C CA  . LEU A 183 ? 0.5431 0.5523 0.5562 0.0320  -0.0344 0.0667  183 LEU A CA  
2774  C C   . LEU A 183 ? 0.5499 0.5667 0.5546 0.0327  -0.0308 0.0640  183 LEU A C   
2775  O O   . LEU A 183 ? 0.6056 0.6278 0.6079 0.0393  -0.0244 0.0577  183 LEU A O   
2776  C CB  . LEU A 183 ? 0.5592 0.5850 0.5800 0.0307  -0.0333 0.0742  183 LEU A CB  
2777  C CG  . LEU A 183 ? 0.5499 0.5717 0.5788 0.0299  -0.0374 0.0769  183 LEU A CG  
2778  C CD1 . LEU A 183 ? 0.5588 0.6006 0.5964 0.0278  -0.0368 0.0841  183 LEU A CD1 
2779  C CD2 . LEU A 183 ? 0.5100 0.5181 0.5391 0.0234  -0.0452 0.0779  183 LEU A CD2 
2791  N N   . ILE A 184 ? 0.5552 0.5717 0.5551 0.0263  -0.0358 0.0684  184 ILE A N   
2792  C CA  . ILE A 184 ? 0.5520 0.5772 0.5416 0.0255  -0.0337 0.0673  184 ILE A CA  
2793  C C   . ILE A 184 ? 0.5551 0.5906 0.5422 0.0166  -0.0378 0.0800  184 ILE A C   
2794  O O   . ILE A 184 ? 0.5942 0.6195 0.5850 0.0110  -0.0462 0.0869  184 ILE A O   
2795  C CB  . ILE A 184 ? 0.5631 0.5748 0.5464 0.0265  -0.0374 0.0596  184 ILE A CB  
2796  C CG1 . ILE A 184 ? 0.5842 0.5843 0.5701 0.0329  -0.0336 0.0482  184 ILE A CG1 
2797  C CG2 . ILE A 184 ? 0.6070 0.6295 0.5781 0.0256  -0.0358 0.0583  184 ILE A CG2 
2798  C CD1 . ILE A 184 ? 0.5637 0.5523 0.5464 0.0324  -0.0373 0.0402  184 ILE A CD1 
2810  N N   . SER A 185 ? 0.5532 0.6089 0.5339 0.0150  -0.0319 0.0829  185 SER A N   
2811  C CA  . SER A 185 ? 0.6149 0.6823 0.5908 0.0045  -0.0348 0.0965  185 SER A CA  
2812  C C   . SER A 185 ? 0.6457 0.7235 0.6057 0.0029  -0.0328 0.0960  185 SER A C   
2813  O O   . SER A 185 ? 0.6778 0.7696 0.6330 0.0090  -0.0239 0.0864  185 SER A O   
2814  C CB  . SER A 185 ? 0.6585 0.7477 0.6423 0.0011  -0.0289 0.1030  185 SER A CB  
2815  O OG  . SER A 185 ? 0.6909 0.7931 0.6686 -0.0110 -0.0307 0.1169  185 SER A OG  
2821  N N   . ASP A 186 ? 0.6561 0.7265 0.6078 -0.0049 -0.0419 0.1058  186 ASP A N   
2822  C CA  . ASP A 186 ? 0.6741 0.7536 0.6085 -0.0077 -0.0422 0.1073  186 ASP A CA  
2823  C C   . ASP A 186 ? 0.7034 0.7898 0.6297 -0.0210 -0.0477 0.1262  186 ASP A C   
2824  O O   . ASP A 186 ? 0.7338 0.8061 0.6676 -0.0273 -0.0565 0.1372  186 ASP A O   
2825  C CB  . ASP A 186 ? 0.7375 0.7984 0.6673 -0.0031 -0.0503 0.0997  186 ASP A CB  
2826  C CG  . ASP A 186 ? 0.7726 0.8344 0.7017 0.0069  -0.0430 0.0815  186 ASP A CG  
2827  O OD1 . ASP A 186 ? 0.8248 0.9052 0.7452 0.0090  -0.0341 0.0757  186 ASP A OD1 
2828  O OD2 . ASP A 186 ? 0.7509 0.7951 0.6881 0.0123  -0.0461 0.0725  186 ASP A OD2 
2833  N N   . GLN A 187 ? 0.7573 0.8653 0.6677 -0.0257 -0.0425 0.1298  187 GLN A N   
2834  C CA  . GLN A 187 ? 0.7814 0.8966 0.6800 -0.0399 -0.0476 0.1493  187 GLN A CA  
2835  C C   . GLN A 187 ? 0.8175 0.9084 0.7078 -0.0421 -0.0633 0.1566  187 GLN A C   
2836  O O   . GLN A 187 ? 0.8748 0.9604 0.7576 -0.0348 -0.0660 0.1464  187 GLN A O   
2837  C CB  . GLN A 187 ? 0.8090 0.9572 0.6909 -0.0442 -0.0368 0.1497  187 GLN A CB  
2838  C CG  . GLN A 187 ? 0.8448 1.0197 0.7368 -0.0392 -0.0212 0.1394  187 GLN A CG  
2839  C CD  . GLN A 187 ? 0.9028 1.1103 0.7795 -0.0384 -0.0095 0.1320  187 GLN A CD  
2840  O OE1 . GLN A 187 ? 0.8799 1.0858 0.7407 -0.0350 -0.0113 0.1250  187 GLN A OE1 
2841  N NE2 . GLN A 187 ? 0.9834 1.2226 0.8653 -0.0413 0.0026  0.1321  187 GLN A NE2 
2850  N N   . VAL A 188 ? 0.8054 0.8811 0.6982 -0.0519 -0.0746 0.1737  188 VAL A N   
2851  C CA  . VAL A 188 ? 0.8350 0.8866 0.7217 -0.0528 -0.0912 0.1811  188 VAL A CA  
2852  C C   . VAL A 188 ? 0.8460 0.9101 0.7092 -0.0554 -0.0925 0.1848  188 VAL A C   
2853  O O   . VAL A 188 ? 0.8821 0.9321 0.7400 -0.0500 -0.1034 0.1818  188 VAL A O   
2854  C CB  . VAL A 188 ? 0.8550 0.8884 0.7463 -0.0643 -0.1036 0.2006  188 VAL A CB  
2855  C CG1 . VAL A 188 ? 0.8225 0.8442 0.7366 -0.0614 -0.1029 0.1950  188 VAL A CG1 
2856  C CG2 . VAL A 188 ? 0.9308 0.9839 0.8078 -0.0809 -0.0997 0.2200  188 VAL A CG2 
2866  N N   . ALA A 189 ? 0.8323 0.9254 0.6811 -0.0637 -0.0815 0.1906  189 ALA A N   
2867  C CA  . ALA A 189 ? 0.8344 0.9431 0.6584 -0.0667 -0.0817 0.1932  189 ALA A CA  
2868  C C   . ALA A 189 ? 0.8417 0.9523 0.6642 -0.0525 -0.0783 0.1706  189 ALA A C   
2869  O O   . ALA A 189 ? 0.8919 0.9980 0.7004 -0.0509 -0.0874 0.1703  189 ALA A O   
2870  C CB  . ALA A 189 ? 0.8040 0.9484 0.6145 -0.0776 -0.0678 0.2003  189 ALA A CB  
2876  N N   . GLU A 190 ? 0.8174 0.9341 0.6544 -0.0424 -0.0662 0.1519  190 GLU A N   
2877  C CA  . GLU A 190 ? 0.8265 0.9406 0.6642 -0.0299 -0.0637 0.1305  190 GLU A CA  
2878  C C   . GLU A 190 ? 0.8138 0.8990 0.6614 -0.0240 -0.0778 0.1272  190 GLU A C   
2879  O O   . GLU A 190 ? 0.8139 0.8964 0.6538 -0.0193 -0.0834 0.1185  190 GLU A O   
2880  C CB  . GLU A 190 ? 0.8025 0.9243 0.6550 -0.0209 -0.0494 0.1134  190 GLU A CB  
2881  C CG  . GLU A 190 ? 0.8304 0.9845 0.6734 -0.0216 -0.0346 0.1077  190 GLU A CG  
2882  C CD  . GLU A 190 ? 0.8999 1.0667 0.7240 -0.0183 -0.0325 0.0956  190 GLU A CD  
2883  O OE1 . GLU A 190 ? 0.9708 1.1537 0.7739 -0.0274 -0.0345 0.1062  190 GLU A OE1 
2884  O OE2 . GLU A 190 ? 0.9023 1.0624 0.7317 -0.0074 -0.0295 0.0759  190 GLU A OE2 
2891  N N   . ILE A 191 ? 0.8013 0.8667 0.6665 -0.0241 -0.0838 0.1330  191 ILE A N   
2892  C CA  . ILE A 191 ? 0.7717 0.8128 0.6497 -0.0171 -0.0954 0.1268  191 ILE A CA  
2893  C C   . ILE A 191 ? 0.7755 0.8094 0.6412 -0.0187 -0.1107 0.1343  191 ILE A C   
2894  O O   . ILE A 191 ? 0.7860 0.8123 0.6557 -0.0112 -0.1172 0.1228  191 ILE A O   
2895  C CB  . ILE A 191 ? 0.7216 0.7449 0.6183 -0.0181 -0.0998 0.1329  191 ILE A CB  
2896  C CG1 . ILE A 191 ? 0.7054 0.7359 0.6147 -0.0147 -0.0858 0.1235  191 ILE A CG1 
2897  C CG2 . ILE A 191 ? 0.7144 0.7153 0.6238 -0.0112 -0.1125 0.1267  191 ILE A CG2 
2898  C CD1 . ILE A 191 ? 0.7130 0.7308 0.6384 -0.0173 -0.0888 0.1298  191 ILE A CD1 
2910  N N   . VAL A 192 ? 0.7704 0.8073 0.6212 -0.0291 -0.1172 0.1543  192 VAL A N   
2911  C CA  . VAL A 192 ? 0.8516 0.8794 0.6901 -0.0307 -0.1341 0.1643  192 VAL A CA  
2912  C C   . VAL A 192 ? 0.8485 0.8975 0.6640 -0.0315 -0.1310 0.1600  192 VAL A C   
2913  O O   . VAL A 192 ? 0.8240 0.8686 0.6345 -0.0266 -0.1422 0.1556  192 VAL A O   
2914  C CB  . VAL A 192 ? 0.9449 0.9612 0.7772 -0.0425 -0.1450 0.1900  192 VAL A CB  
2915  C CG1 . VAL A 192 ? 0.9503 0.9488 0.8048 -0.0429 -0.1457 0.1924  192 VAL A CG1 
2916  C CG2 . VAL A 192 ? 0.9924 1.0329 0.8021 -0.0558 -0.1361 0.2042  192 VAL A CG2 
2926  N N   . SER A 193 ? 0.8443 0.9186 0.6463 -0.0372 -0.1160 0.1598  193 SER A N   
2927  C CA  . SER A 193 ? 0.8772 0.9738 0.6548 -0.0390 -0.1131 0.1560  193 SER A CA  
2928  C C   . SER A 193 ? 0.8749 0.9740 0.6575 -0.0273 -0.1095 0.1307  193 SER A C   
2929  O O   . SER A 193 ? 0.9204 1.0251 0.6884 -0.0259 -0.1169 0.1263  193 SER A O   
2930  C CB  . SER A 193 ? 0.9242 1.0501 0.6882 -0.0473 -0.0968 0.1598  193 SER A CB  
2931  O OG  . SER A 193 ? 0.9670 1.1048 0.7425 -0.0389 -0.0804 0.1385  193 SER A OG  
2937  N N   . LYS A 194 ? 0.8907 0.9855 0.6933 -0.0195 -0.0990 0.1143  194 LYS A N   
2938  C CA  . LYS A 194 ? 0.9398 1.0349 0.7481 -0.0100 -0.0950 0.0908  194 LYS A CA  
2939  C C   . LYS A 194 ? 0.9005 0.9746 0.7238 -0.0039 -0.1081 0.0852  194 LYS A C   
2940  O O   . LYS A 194 ? 0.8977 0.9716 0.7261 0.0022  -0.1066 0.0666  194 LYS A O   
2941  C CB  . LYS A 194 ? 0.9937 1.0913 0.8164 -0.0046 -0.0789 0.0768  194 LYS A CB  
2942  C CG  . LYS A 194 ? 1.0661 1.1865 0.8798 -0.0088 -0.0650 0.0803  194 LYS A CG  
2943  C CD  . LYS A 194 ? 1.1301 1.2747 0.9227 -0.0086 -0.0583 0.0696  194 LYS A CD  
2944  C CE  . LYS A 194 ? 1.1691 1.3388 0.9578 -0.0103 -0.0424 0.0685  194 LYS A CE  
2945  N NZ  . LYS A 194 ? 1.2898 1.4877 1.0555 -0.0117 -0.0356 0.0599  194 LYS A NZ  
2959  N N   . TYR A 195 ? 0.8705 0.9278 0.7020 -0.0056 -0.1211 0.0997  195 TYR A N   
2960  C CA  . TYR A 195 ? 0.8408 0.8812 0.6892 0.0013  -0.1330 0.0926  195 TYR A CA  
2961  C C   . TYR A 195 ? 0.8884 0.9363 0.7263 0.0038  -0.1426 0.0850  195 TYR A C   
2962  O O   . TYR A 195 ? 0.9247 0.9816 0.7413 -0.0011 -0.1500 0.0962  195 TYR A O   
2963  C CB  . TYR A 195 ? 0.8008 0.8223 0.6588 -0.0001 -0.1468 0.1091  195 TYR A CB  
2964  C CG  . TYR A 195 ? 0.7720 0.7795 0.6493 0.0083  -0.1588 0.0997  195 TYR A CG  
2965  C CD1 . TYR A 195 ? 0.7544 0.7581 0.6521 0.0144  -0.1511 0.0824  195 TYR A CD1 
2966  C CD2 . TYR A 195 ? 0.7971 0.7969 0.6724 0.0103  -0.1780 0.1079  195 TYR A CD2 
2967  C CE1 . TYR A 195 ? 0.7659 0.7616 0.6820 0.0214  -0.1606 0.0727  195 TYR A CE1 
2968  C CE2 . TYR A 195 ? 0.8175 0.8083 0.7128 0.0191  -0.1887 0.0975  195 TYR A CE2 
2969  C CZ  . TYR A 195 ? 0.7906 0.7809 0.7065 0.0243  -0.1792 0.0794  195 TYR A CZ  
2970  O OH  . TYR A 195 ? 0.7630 0.7487 0.6995 0.0324  -0.1885 0.0681  195 TYR A OH  
2980  N N   . ASP A 196 ? 0.8380 0.8831 0.6906 0.0105  -0.1426 0.0663  196 ASP A N   
2981  C CA  . ASP A 196 ? 0.8433 0.8955 0.6915 0.0134  -0.1520 0.0557  196 ASP A CA  
2982  C C   . ASP A 196 ? 0.7807 0.8228 0.6551 0.0199  -0.1565 0.0425  196 ASP A C   
2983  O O   . ASP A 196 ? 0.7467 0.7869 0.6337 0.0215  -0.1444 0.0284  196 ASP A O   
2984  C CB  . ASP A 196 ? 0.8710 0.9402 0.7044 0.0120  -0.1408 0.0409  196 ASP A CB  
2985  C CG  . ASP A 196 ? 0.9087 0.9872 0.7356 0.0136  -0.1513 0.0299  196 ASP A CG  
2986  O OD1 . ASP A 196 ? 0.9267 0.9986 0.7679 0.0175  -0.1646 0.0283  196 ASP A OD1 
2987  O OD2 . ASP A 196 ? 0.9127 1.0065 0.7207 0.0113  -0.1463 0.0216  196 ASP A OD2 
2992  N N   . PRO A 197 ? 0.8050 0.8411 0.6885 0.0238  -0.1736 0.0466  197 PRO A N   
2993  C CA  . PRO A 197 ? 0.7841 0.8143 0.6946 0.0300  -0.1767 0.0334  197 PRO A CA  
2994  C C   . PRO A 197 ? 0.7824 0.8241 0.6988 0.0308  -0.1719 0.0121  197 PRO A C   
2995  O O   . PRO A 197 ? 0.7777 0.8173 0.7162 0.0338  -0.1702 -0.0002 197 PRO A O   
2996  C CB  . PRO A 197 ? 0.7972 0.8212 0.7140 0.0349  -0.1977 0.0430  197 PRO A CB  
2997  C CG  . PRO A 197 ? 0.8283 0.8595 0.7187 0.0311  -0.2069 0.0557  197 PRO A CG  
2998  C CD  . PRO A 197 ? 0.8290 0.8646 0.6989 0.0231  -0.1914 0.0631  197 PRO A CD  
3006  N N   . ASN A 198 ? 0.8058 0.8602 0.7032 0.0275  -0.1698 0.0069  198 ASN A N   
3007  C CA  . ASN A 198 ? 0.7605 0.8243 0.6627 0.0268  -0.1650 -0.0139 198 ASN A CA  
3008  C C   . ASN A 198 ? 0.7455 0.8047 0.6501 0.0242  -0.1460 -0.0242 198 ASN A C   
3009  O O   . ASN A 198 ? 0.7066 0.7686 0.6185 0.0228  -0.1412 -0.0414 198 ASN A O   
3010  C CB  . ASN A 198 ? 0.7508 0.8297 0.6310 0.0246  -0.1718 -0.0169 198 ASN A CB  
3011  C CG  . ASN A 198 ? 0.7673 0.8515 0.6469 0.0278  -0.1927 -0.0093 198 ASN A CG  
3012  O OD1 . ASN A 198 ? 0.7721 0.8563 0.6738 0.0323  -0.2020 -0.0160 198 ASN A OD1 
3013  N ND2 . ASN A 198 ? 0.7952 0.8851 0.6498 0.0256  -0.2005 0.0050  198 ASN A ND2 
3020  N N   . VAL A 199 ? 0.7320 0.7839 0.6313 0.0234  -0.1360 -0.0138 199 VAL A N   
3021  C CA  . VAL A 199 ? 0.7071 0.7537 0.6087 0.0223  -0.1194 -0.0216 199 VAL A CA  
3022  C C   . VAL A 199 ? 0.7080 0.7414 0.6273 0.0239  -0.1152 -0.0153 199 VAL A C   
3023  O O   . VAL A 199 ? 0.7477 0.7768 0.6656 0.0242  -0.1184 0.0003  199 VAL A O   
3024  C CB  . VAL A 199 ? 0.6642 0.7180 0.5446 0.0206  -0.1104 -0.0170 199 VAL A CB  
3025  C CG1 . VAL A 199 ? 0.6353 0.6831 0.5204 0.0216  -0.0947 -0.0265 199 VAL A CG1 
3026  C CG2 . VAL A 199 ? 0.6173 0.6863 0.4780 0.0190  -0.1155 -0.0233 199 VAL A CG2 
3036  N N   . TYR A 200 ? 0.6960 0.7229 0.6308 0.0239  -0.1085 -0.0271 200 TYR A N   
3037  C CA  . TYR A 200 ? 0.6651 0.6814 0.6164 0.0250  -0.1050 -0.0232 200 TYR A CA  
3038  C C   . TYR A 200 ? 0.6178 0.6270 0.5655 0.0247  -0.0923 -0.0183 200 TYR A C   
3039  O O   . TYR A 200 ? 0.6185 0.6206 0.5748 0.0255  -0.0910 -0.0101 200 TYR A O   
3040  C CB  . TYR A 200 ? 0.6185 0.6335 0.5874 0.0238  -0.1037 -0.0372 200 TYR A CB  
3041  C CG  . TYR A 200 ? 0.6473 0.6732 0.6226 0.0241  -0.1156 -0.0451 200 TYR A CG  
3042  C CD1 . TYR A 200 ? 0.6403 0.6712 0.6143 0.0279  -0.1298 -0.0364 200 TYR A CD1 
3043  C CD2 . TYR A 200 ? 0.6436 0.6745 0.6268 0.0204  -0.1136 -0.0609 200 TYR A CD2 
3044  C CE1 . TYR A 200 ? 0.6123 0.6544 0.5934 0.0294  -0.1421 -0.0438 200 TYR A CE1 
3045  C CE2 . TYR A 200 ? 0.6113 0.6553 0.6023 0.0205  -0.1249 -0.0689 200 TYR A CE2 
3046  C CZ  . TYR A 200 ? 0.6092 0.6593 0.5993 0.0259  -0.1393 -0.0605 200 TYR A CZ  
3047  O OH  . TYR A 200 ? 0.6254 0.6897 0.6244 0.0273  -0.1518 -0.0686 200 TYR A OH  
3057  N N   . SER A 201 ? 0.6147 0.6264 0.5507 0.0242  -0.0835 -0.0240 201 SER A N   
3058  C CA  . SER A 201 ? 0.6276 0.6352 0.5608 0.0255  -0.0721 -0.0205 201 SER A CA  
3059  C C   . SER A 201 ? 0.6541 0.6741 0.5691 0.0256  -0.0702 -0.0150 201 SER A C   
3060  O O   . SER A 201 ? 0.6827 0.7094 0.5868 0.0262  -0.0667 -0.0255 201 SER A O   
3061  C CB  . SER A 201 ? 0.6850 0.6838 0.6229 0.0258  -0.0630 -0.0340 201 SER A CB  
3062  O OG  . SER A 201 ? 0.6990 0.6896 0.6518 0.0235  -0.0648 -0.0391 201 SER A OG  
3068  N N   . ILE A 202 ? 0.6808 0.7045 0.5924 0.0245  -0.0723 0.0008  202 ILE A N   
3069  C CA  . ILE A 202 ? 0.6892 0.7277 0.5828 0.0224  -0.0714 0.0088  202 ILE A CA  
3070  C C   . ILE A 202 ? 0.6991 0.7440 0.5901 0.0245  -0.0580 0.0068  202 ILE A C   
3071  O O   . ILE A 202 ? 0.7093 0.7468 0.6121 0.0261  -0.0527 0.0102  202 ILE A O   
3072  C CB  . ILE A 202 ? 0.6765 0.7152 0.5679 0.0185  -0.0808 0.0281  202 ILE A CB  
3073  C CG1 . ILE A 202 ? 0.7510 0.7858 0.6432 0.0183  -0.0957 0.0289  202 ILE A CG1 
3074  C CG2 . ILE A 202 ? 0.6624 0.7176 0.5354 0.0141  -0.0774 0.0391  202 ILE A CG2 
3075  C CD1 . ILE A 202 ? 0.8331 0.8603 0.7289 0.0161  -0.1073 0.0462  202 ILE A CD1 
3087  N N   . LYS A 203 ? 0.7404 0.8007 0.6158 0.0249  -0.0530 0.0006  203 LYS A N   
3088  C CA  . LYS A 203 ? 0.7269 0.7982 0.5994 0.0280  -0.0405 -0.0029 203 LYS A CA  
3089  C C   . LYS A 203 ? 0.7064 0.7934 0.5715 0.0228  -0.0394 0.0149  203 LYS A C   
3090  O O   . LYS A 203 ? 0.7673 0.8712 0.6148 0.0182  -0.0413 0.0199  203 LYS A O   
3091  C CB  . LYS A 203 ? 0.7444 0.8267 0.6044 0.0313  -0.0354 -0.0202 203 LYS A CB  
3092  C CG  . LYS A 203 ? 0.7395 0.8047 0.6081 0.0358  -0.0346 -0.0386 203 LYS A CG  
3093  C CD  . LYS A 203 ? 0.7311 0.8062 0.5876 0.0395  -0.0296 -0.0571 203 LYS A CD  
3094  C CE  . LYS A 203 ? 0.7781 0.8329 0.6442 0.0430  -0.0289 -0.0750 203 LYS A CE  
3095  N NZ  . LYS A 203 ? 0.7746 0.8183 0.6450 0.0375  -0.0390 -0.0767 203 LYS A NZ  
3109  N N   . TYR A 204 ? 0.6955 0.7777 0.5735 0.0224  -0.0368 0.0248  204 TYR A N   
3110  C CA  . TYR A 204 ? 0.7449 0.8418 0.6186 0.0161  -0.0350 0.0415  204 TYR A CA  
3111  C C   . TYR A 204 ? 0.7781 0.8953 0.6515 0.0198  -0.0213 0.0352  204 TYR A C   
3112  O O   . TYR A 204 ? 0.7826 0.8933 0.6702 0.0269  -0.0152 0.0274  204 TYR A O   
3113  C CB  . TYR A 204 ? 0.7406 0.8228 0.6292 0.0131  -0.0403 0.0548  204 TYR A CB  
3114  C CG  . TYR A 204 ? 0.7383 0.8012 0.6306 0.0111  -0.0539 0.0596  204 TYR A CG  
3115  C CD1 . TYR A 204 ? 0.7415 0.8061 0.6223 0.0046  -0.0644 0.0722  204 TYR A CD1 
3116  C CD2 . TYR A 204 ? 0.7522 0.7963 0.6600 0.0159  -0.0565 0.0517  204 TYR A CD2 
3117  C CE1 . TYR A 204 ? 0.7512 0.7985 0.6375 0.0048  -0.0778 0.0754  204 TYR A CE1 
3118  C CE2 . TYR A 204 ? 0.7433 0.7733 0.6566 0.0151  -0.0684 0.0541  204 TYR A CE2 
3119  C CZ  . TYR A 204 ? 0.7440 0.7755 0.6477 0.0105  -0.0793 0.0654  204 TYR A CZ  
3120  O OH  . TYR A 204 ? 0.7532 0.7711 0.6644 0.0116  -0.0922 0.0666  204 TYR A OH  
3130  N N   . ASN A 205 ? 0.8087 0.9513 0.6658 0.0154  -0.0168 0.0385  205 ASN A N   
3131  C CA  . ASN A 205 ? 0.8431 1.0102 0.7015 0.0185  -0.0037 0.0333  205 ASN A CA  
3132  C C   . ASN A 205 ? 0.8076 0.9780 0.6802 0.0145  -0.0015 0.0478  205 ASN A C   
3133  O O   . ASN A 205 ? 0.8212 0.9789 0.6971 0.0066  -0.0103 0.0641  205 ASN A O   
3134  C CB  . ASN A 205 ? 0.9502 1.1478 0.7867 0.0129  0.0011  0.0341  205 ASN A CB  
3135  C CG  . ASN A 205 ? 1.0793 1.3060 0.9176 0.0187  0.0158  0.0228  205 ASN A CG  
3136  O OD1 . ASN A 205 ? 1.1027 1.3237 0.9581 0.0293  0.0215  0.0111  205 ASN A OD1 
3137  N ND2 . ASN A 205 ? 1.2042 1.4632 1.0247 0.0118  0.0218  0.0262  205 ASN A ND2 
3144  N N   . ASN A 206 ? 0.7275 0.9149 0.6098 0.0207  0.0095  0.0404  206 ASN A N   
3145  C CA  . ASN A 206 ? 0.7300 0.9264 0.6266 0.0172  0.0125  0.0522  206 ASN A CA  
3146  C C   . ASN A 206 ? 0.6710 0.8377 0.5833 0.0175  0.0040  0.0589  206 ASN A C   
3147  O O   . ASN A 206 ? 0.6121 0.7803 0.5329 0.0103  0.0016  0.0731  206 ASN A O   
3148  C CB  . ASN A 206 ? 0.7813 1.0003 0.6670 0.0023  0.0127  0.0708  206 ASN A CB  
3149  C CG  . ASN A 206 ? 0.8405 1.0946 0.7099 0.0008  0.0227  0.0647  206 ASN A CG  
3150  O OD1 . ASN A 206 ? 0.8591 1.1305 0.7332 0.0115  0.0332  0.0473  206 ASN A OD1 
3151  N ND2 . ASN A 206 ? 0.8904 1.1553 0.7401 -0.0124 0.0192  0.0788  206 ASN A ND2 
3158  N N   . GLN A 207 ? 0.6927 0.8334 0.6087 0.0249  -0.0005 0.0483  207 GLN A N   
3159  C CA  . GLN A 207 ? 0.6542 0.7698 0.5848 0.0262  -0.0069 0.0520  207 GLN A CA  
3160  C C   . GLN A 207 ? 0.6774 0.7963 0.6236 0.0342  -0.0003 0.0469  207 GLN A C   
3161  O O   . GLN A 207 ? 0.7172 0.8459 0.6646 0.0435  0.0074  0.0340  207 GLN A O   
3162  C CB  . GLN A 207 ? 0.6249 0.7152 0.5542 0.0301  -0.0130 0.0424  207 GLN A CB  
3163  C CG  . GLN A 207 ? 0.5847 0.6517 0.5277 0.0308  -0.0188 0.0451  207 GLN A CG  
3164  C CD  . GLN A 207 ? 0.5980 0.6442 0.5404 0.0332  -0.0239 0.0356  207 GLN A CD  
3165  O OE1 . GLN A 207 ? 0.6169 0.6559 0.5608 0.0397  -0.0198 0.0227  207 GLN A OE1 
3166  N NE2 . GLN A 207 ? 0.6438 0.6805 0.5852 0.0278  -0.0334 0.0419  207 GLN A NE2 
3175  N N   . LEU A 208 ? 0.6428 0.7534 0.6012 0.0311  -0.0044 0.0567  208 LEU A N   
3176  C CA  . LEU A 208 ? 0.6233 0.7339 0.5968 0.0384  -0.0009 0.0536  208 LEU A CA  
3177  C C   . LEU A 208 ? 0.6162 0.6975 0.5960 0.0410  -0.0073 0.0516  208 LEU A C   
3178  O O   . LEU A 208 ? 0.6488 0.7159 0.6272 0.0342  -0.0151 0.0583  208 LEU A O   
3179  C CB  . LEU A 208 ? 0.6459 0.7752 0.6284 0.0317  0.0000  0.0662  208 LEU A CB  
3180  C CG  . LEU A 208 ? 0.6916 0.8545 0.6687 0.0264  0.0072  0.0702  208 LEU A CG  
3181  C CD1 . LEU A 208 ? 0.7142 0.8932 0.7017 0.0170  0.0066  0.0841  208 LEU A CD1 
3182  C CD2 . LEU A 208 ? 0.6546 0.8366 0.6334 0.0385  0.0175  0.0550  208 LEU A CD2 
3194  N N   . ALA A 209 ? 0.5984 0.6709 0.5852 0.0509  -0.0044 0.0425  209 ALA A N   
3195  C CA  . ALA A 209 ? 0.5938 0.6401 0.5843 0.0523  -0.0094 0.0405  209 ALA A CA  
3196  C C   . ALA A 209 ? 0.6175 0.6587 0.6171 0.0617  -0.0068 0.0362  209 ALA A C   
3197  O O   . ALA A 209 ? 0.6269 0.6739 0.6271 0.0707  -0.0015 0.0272  209 ALA A O   
3198  C CB  . ALA A 209 ? 0.6008 0.6310 0.5823 0.0523  -0.0112 0.0315  209 ALA A CB  
3204  N N   . THR A 210 ? 0.6335 0.6636 0.6400 0.0600  -0.0112 0.0422  210 THR A N   
3205  C CA  . THR A 210 ? 0.6235 0.6435 0.6362 0.0683  -0.0108 0.0393  210 THR A CA  
3206  C C   . THR A 210 ? 0.6665 0.6650 0.6731 0.0727  -0.0100 0.0292  210 THR A C   
3207  O O   . THR A 210 ? 0.6730 0.6616 0.6723 0.0672  -0.0114 0.0257  210 THR A O   
3208  C CB  . THR A 210 ? 0.5361 0.5478 0.5539 0.0640  -0.0163 0.0475  210 THR A CB  
3209  O OG1 . THR A 210 ? 0.5396 0.5361 0.5518 0.0564  -0.0203 0.0478  210 THR A OG1 
3210  C CG2 . THR A 210 ? 0.5250 0.5573 0.5505 0.0595  -0.0177 0.0568  210 THR A CG2 
3218  N N   . ARG A 211 ? 0.7061 0.6969 0.7166 0.0825  -0.0085 0.0246  211 ARG A N   
3219  C CA  . ARG A 211 ? 0.7742 0.7436 0.7797 0.0869  -0.0079 0.0146  211 ARG A CA  
3220  C C   . ARG A 211 ? 0.7764 0.7215 0.7820 0.0854  -0.0120 0.0187  211 ARG A C   
3221  O O   . ARG A 211 ? 0.8063 0.7530 0.8164 0.0846  -0.0149 0.0278  211 ARG A O   
3222  C CB  . ARG A 211 ? 0.8689 0.8443 0.8783 0.0998  -0.0040 0.0050  211 ARG A CB  
3223  C CG  . ARG A 211 ? 0.9199 0.9202 0.9264 0.1009  0.0015  -0.0016 211 ARG A CG  
3224  C CD  . ARG A 211 ? 1.0131 1.0248 1.0262 0.1151  0.0058  -0.0121 211 ARG A CD  
3225  N NE  . ARG A 211 ? 1.1315 1.1404 1.1369 0.1191  0.0092  -0.0274 211 ARG A NE  
3226  C CZ  . ARG A 211 ? 1.2605 1.2951 1.2607 0.1188  0.0148  -0.0339 211 ARG A CZ  
3227  N NH1 . ARG A 211 ? 1.3605 1.4251 1.3624 0.1138  0.0179  -0.0251 211 ARG A NH1 
3228  N NH2 . ARG A 211 ? 1.2964 1.3267 1.2887 0.1226  0.0171  -0.0492 211 ARG A NH2 
3242  N N   . THR A 212 ? 0.7394 0.6627 0.7390 0.0839  -0.0123 0.0119  212 THR A N   
3243  C CA  . THR A 212 ? 0.6924 0.5920 0.6901 0.0811  -0.0155 0.0158  212 THR A CA  
3244  C C   . THR A 212 ? 0.7354 0.6276 0.7382 0.0920  -0.0174 0.0189  212 THR A C   
3245  O O   . THR A 212 ? 0.7858 0.6806 0.7928 0.1033  -0.0159 0.0117  212 THR A O   
3246  C CB  . THR A 212 ? 0.6616 0.5402 0.6527 0.0765  -0.0151 0.0074  212 THR A CB  
3247  O OG1 . THR A 212 ? 0.7470 0.6355 0.7348 0.0683  -0.0141 0.0033  212 THR A OG1 
3248  C CG2 . THR A 212 ? 0.6539 0.5102 0.6417 0.0700  -0.0178 0.0134  212 THR A CG2 
3256  N N   . ALA A 213 ? 0.7302 0.6140 0.7327 0.0892  -0.0213 0.0291  213 ALA A N   
3257  C CA  . ALA A 213 ? 0.7295 0.6063 0.7364 0.0992  -0.0251 0.0344  213 ALA A CA  
3258  C C   . ALA A 213 ? 0.7217 0.5685 0.7207 0.0949  -0.0291 0.0396  213 ALA A C   
3259  O O   . ALA A 213 ? 0.7170 0.5517 0.7081 0.0833  -0.0278 0.0388  213 ALA A O   
3260  C CB  . ALA A 213 ? 0.6956 0.5943 0.7092 0.1000  -0.0273 0.0436  213 ALA A CB  
3266  N N   . GLN A 214 ? 0.7424 0.5783 0.7439 0.1041  -0.0342 0.0455  214 GLN A N   
3267  C CA  . GLN A 214 ? 0.7617 0.5672 0.7544 0.1005  -0.0391 0.0529  214 GLN A CA  
3268  C C   . GLN A 214 ? 0.7492 0.5550 0.7322 0.0844  -0.0386 0.0613  214 GLN A C   
3269  O O   . GLN A 214 ? 0.7242 0.5534 0.7095 0.0799  -0.0370 0.0633  214 GLN A O   
3270  C CB  . GLN A 214 ? 0.7185 0.5169 0.7158 0.1136  -0.0464 0.0604  214 GLN A CB  
3271  C CG  . GLN A 214 ? 0.7658 0.5642 0.7747 0.1316  -0.0473 0.0502  214 GLN A CG  
3272  C CD  . GLN A 214 ? 0.8267 0.6627 0.8486 0.1397  -0.0434 0.0448  214 GLN A CD  
3273  O OE1 . GLN A 214 ? 0.8224 0.6819 0.8442 0.1305  -0.0398 0.0476  214 GLN A OE1 
3274  N NE2 . GLN A 214 ? 0.9022 0.7443 0.9360 0.1567  -0.0444 0.0367  214 GLN A NE2 
3283  N N   . ALA A 215 ? 0.7662 0.5467 0.7388 0.0753  -0.0400 0.0658  215 ALA A N   
3284  C CA  . ALA A 215 ? 0.7489 0.5323 0.7123 0.0593  -0.0380 0.0713  215 ALA A CA  
3285  C C   . ALA A 215 ? 0.7650 0.5612 0.7256 0.0583  -0.0417 0.0824  215 ALA A C   
3286  O O   . ALA A 215 ? 0.7212 0.5295 0.6771 0.0471  -0.0393 0.0838  215 ALA A O   
3287  C CB  . ALA A 215 ? 0.7498 0.5046 0.7024 0.0486  -0.0384 0.0748  215 ALA A CB  
3293  N N   . ILE A 216 ? 0.8589 0.6539 0.8231 0.0703  -0.0479 0.0891  216 ILE A N   
3294  C CA  . ILE A 216 ? 0.9030 0.7117 0.8646 0.0695  -0.0523 0.0990  216 ILE A CA  
3295  C C   . ILE A 216 ? 0.8207 0.6595 0.7889 0.0657  -0.0488 0.0940  216 ILE A C   
3296  O O   . ILE A 216 ? 0.8189 0.6693 0.7827 0.0597  -0.0510 0.0995  216 ILE A O   
3297  C CB  . ILE A 216 ? 1.0105 0.8176 0.9787 0.0851  -0.0603 0.1051  216 ILE A CB  
3298  C CG1 . ILE A 216 ? 1.1072 0.9288 1.0716 0.0832  -0.0660 0.1155  216 ILE A CG1 
3299  C CG2 . ILE A 216 ? 1.0406 0.8657 1.0259 0.0984  -0.0582 0.0951  216 ILE A CG2 
3300  C CD1 . ILE A 216 ? 1.2016 1.0226 1.1723 0.0981  -0.0755 0.1228  216 ILE A CD1 
3312  N N   . PHE A 217 ? 0.7399 0.5907 0.7179 0.0686  -0.0441 0.0838  217 PHE A N   
3313  C CA  . PHE A 217 ? 0.6845 0.5605 0.6691 0.0651  -0.0419 0.0800  217 PHE A CA  
3314  C C   . PHE A 217 ? 0.6291 0.5065 0.6086 0.0524  -0.0376 0.0750  217 PHE A C   
3315  O O   . PHE A 217 ? 0.6017 0.4965 0.5865 0.0492  -0.0368 0.0715  217 PHE A O   
3316  C CB  . PHE A 217 ? 0.6328 0.5227 0.6293 0.0741  -0.0394 0.0732  217 PHE A CB  
3317  C CG  . PHE A 217 ? 0.6174 0.5119 0.6224 0.0878  -0.0430 0.0759  217 PHE A CG  
3318  C CD1 . PHE A 217 ? 0.5715 0.4859 0.5839 0.0908  -0.0470 0.0815  217 PHE A CD1 
3319  C CD2 . PHE A 217 ? 0.6165 0.4958 0.6232 0.0980  -0.0430 0.0718  217 PHE A CD2 
3320  C CE1 . PHE A 217 ? 0.5579 0.4798 0.5803 0.1041  -0.0507 0.0832  217 PHE A CE1 
3321  C CE2 . PHE A 217 ? 0.6040 0.4890 0.6206 0.1124  -0.0468 0.0728  217 PHE A CE2 
3322  C CZ  . PHE A 217 ? 0.5621 0.4698 0.5871 0.1156  -0.0505 0.0787  217 PHE A CZ  
3332  N N   . ASP A 218 ? 0.6156 0.4754 0.5859 0.0449  -0.0354 0.0743  218 ASP A N   
3333  C CA  . ASP A 218 ? 0.6708 0.5352 0.6383 0.0333  -0.0315 0.0686  218 ASP A CA  
3334  C C   . ASP A 218 ? 0.6649 0.5455 0.6313 0.0278  -0.0331 0.0706  218 ASP A C   
3335  O O   . ASP A 218 ? 0.6712 0.5541 0.6339 0.0293  -0.0371 0.0784  218 ASP A O   
3336  C CB  . ASP A 218 ? 0.7525 0.5978 0.7102 0.0244  -0.0291 0.0695  218 ASP A CB  
3337  C CG  . ASP A 218 ? 0.7985 0.6265 0.7578 0.0280  -0.0276 0.0644  218 ASP A CG  
3338  O OD1 . ASP A 218 ? 0.7999 0.6337 0.7674 0.0374  -0.0275 0.0586  218 ASP A OD1 
3339  O OD2 . ASP A 218 ? 0.8495 0.6585 0.8014 0.0207  -0.0266 0.0661  218 ASP A OD2 
3344  N N   . ASP A 219 ? 0.6689 0.5610 0.6391 0.0220  -0.0307 0.0628  219 ASP A N   
3345  C CA  . ASP A 219 ? 0.6765 0.5825 0.6462 0.0164  -0.0321 0.0615  219 ASP A CA  
3346  C C   . ASP A 219 ? 0.6947 0.6124 0.6699 0.0221  -0.0373 0.0655  219 ASP A C   
3347  O O   . ASP A 219 ? 0.7155 0.6395 0.6863 0.0194  -0.0403 0.0686  219 ASP A O   
3348  C CB  . ASP A 219 ? 0.6864 0.5877 0.6436 0.0078  -0.0307 0.0654  219 ASP A CB  
3349  C CG  . ASP A 219 ? 0.7683 0.6598 0.7209 -0.0003 -0.0252 0.0618  219 ASP A CG  
3350  O OD1 . ASP A 219 ? 0.7681 0.6678 0.7274 -0.0038 -0.0223 0.0518  219 ASP A OD1 
3351  O OD2 . ASP A 219 ? 0.7976 0.6729 0.7407 -0.0033 -0.0247 0.0692  219 ASP A OD2 
3356  N N   . SER A 220 ? 0.6754 0.5977 0.6600 0.0291  -0.0383 0.0650  220 SER A N   
3357  C CA  . SER A 220 ? 0.6225 0.5580 0.6145 0.0332  -0.0428 0.0686  220 SER A CA  
3358  C C   . SER A 220 ? 0.6097 0.5563 0.6095 0.0298  -0.0444 0.0634  220 SER A C   
3359  O O   . SER A 220 ? 0.6072 0.5639 0.6114 0.0287  -0.0491 0.0653  220 SER A O   
3360  C CB  . SER A 220 ? 0.6251 0.5619 0.6232 0.0426  -0.0427 0.0722  220 SER A CB  
3361  O OG  . SER A 220 ? 0.6839 0.6093 0.6765 0.0476  -0.0437 0.0777  220 SER A OG  
3367  N N   . TYR A 221 ? 0.5973 0.5415 0.5992 0.0282  -0.0418 0.0572  221 TYR A N   
3368  C CA  . TYR A 221 ? 0.5903 0.5413 0.5990 0.0253  -0.0447 0.0528  221 TYR A CA  
3369  C C   . TYR A 221 ? 0.5553 0.5150 0.5715 0.0281  -0.0471 0.0575  221 TYR A C   
3370  O O   . TYR A 221 ? 0.5301 0.4959 0.5521 0.0250  -0.0520 0.0583  221 TYR A O   
3371  C CB  . TYR A 221 ? 0.6565 0.6117 0.6656 0.0205  -0.0486 0.0493  221 TYR A CB  
3372  C CG  . TYR A 221 ? 0.6874 0.6396 0.6910 0.0160  -0.0456 0.0421  221 TYR A CG  
3373  C CD1 . TYR A 221 ? 0.6700 0.6148 0.6686 0.0150  -0.0400 0.0403  221 TYR A CD1 
3374  C CD2 . TYR A 221 ? 0.6601 0.6185 0.6640 0.0122  -0.0482 0.0360  221 TYR A CD2 
3375  C CE1 . TYR A 221 ? 0.6288 0.5740 0.6232 0.0092  -0.0367 0.0338  221 TYR A CE1 
3376  C CE2 . TYR A 221 ? 0.6327 0.5928 0.6322 0.0077  -0.0445 0.0284  221 TYR A CE2 
3377  C CZ  . TYR A 221 ? 0.6382 0.5927 0.6333 0.0057  -0.0385 0.0279  221 TYR A CZ  
3378  O OH  . TYR A 221 ? 0.7143 0.6737 0.7060 -0.0004 -0.0341 0.0206  221 TYR A OH  
3388  N N   . LEU A 222 ? 0.5151 0.4757 0.5315 0.0333  -0.0436 0.0603  222 LEU A N   
3389  C CA  . LEU A 222 ? 0.5185 0.4904 0.5413 0.0344  -0.0442 0.0639  222 LEU A CA  
3390  C C   . LEU A 222 ? 0.5265 0.4976 0.5502 0.0299  -0.0463 0.0611  222 LEU A C   
3391  O O   . LEU A 222 ? 0.5075 0.4706 0.5273 0.0293  -0.0449 0.0552  222 LEU A O   
3392  C CB  . LEU A 222 ? 0.5354 0.5098 0.5575 0.0414  -0.0390 0.0642  222 LEU A CB  
3393  C CG  . LEU A 222 ? 0.5357 0.5252 0.5626 0.0419  -0.0377 0.0669  222 LEU A CG  
3394  C CD1 . LEU A 222 ? 0.5427 0.5473 0.5782 0.0395  -0.0412 0.0738  222 LEU A CD1 
3395  C CD2 . LEU A 222 ? 0.5023 0.4951 0.5280 0.0499  -0.0318 0.0638  222 LEU A CD2 
3407  N N   . GLY A 223 ? 0.5522 0.5314 0.5816 0.0262  -0.0506 0.0658  223 GLY A N   
3408  C CA  . GLY A 223 ? 0.5325 0.5086 0.5628 0.0219  -0.0548 0.0651  223 GLY A CA  
3409  C C   . GLY A 223 ? 0.5630 0.5313 0.5962 0.0186  -0.0612 0.0605  223 GLY A C   
3410  O O   . GLY A 223 ? 0.5301 0.4932 0.5648 0.0166  -0.0660 0.0586  223 GLY A O   
3414  N N   . TYR A 224 ? 0.5781 0.5458 0.6119 0.0184  -0.0619 0.0580  224 TYR A N   
3415  C CA  . TYR A 224 ? 0.5561 0.5195 0.5935 0.0154  -0.0681 0.0522  224 TYR A CA  
3416  C C   . TYR A 224 ? 0.5684 0.5313 0.6130 0.0112  -0.0762 0.0564  224 TYR A C   
3417  O O   . TYR A 224 ? 0.5463 0.5018 0.5951 0.0099  -0.0828 0.0510  224 TYR A O   
3418  C CB  . TYR A 224 ? 0.5359 0.5021 0.5707 0.0152  -0.0673 0.0503  224 TYR A CB  
3419  C CG  . TYR A 224 ? 0.5192 0.4828 0.5546 0.0133  -0.0707 0.0404  224 TYR A CG  
3420  C CD1 . TYR A 224 ? 0.5007 0.4642 0.5428 0.0105  -0.0788 0.0378  224 TYR A CD1 
3421  C CD2 . TYR A 224 ? 0.5567 0.5192 0.5864 0.0139  -0.0658 0.0330  224 TYR A CD2 
3422  C CE1 . TYR A 224 ? 0.5680 0.5307 0.6111 0.0098  -0.0818 0.0264  224 TYR A CE1 
3423  C CE2 . TYR A 224 ? 0.5827 0.5471 0.6133 0.0122  -0.0678 0.0226  224 TYR A CE2 
3424  C CZ  . TYR A 224 ? 0.5935 0.5583 0.6309 0.0110  -0.0758 0.0185  224 TYR A CZ  
3425  O OH  . TYR A 224 ? 0.6011 0.5692 0.6398 0.0105  -0.0777 0.0058  224 TYR A OH  
3435  N N   . SER A 225 ? 0.5738 0.5448 0.6208 0.0088  -0.0761 0.0659  225 SER A N   
3436  C CA  . SER A 225 ? 0.5451 0.5161 0.5988 0.0024  -0.0835 0.0722  225 SER A CA  
3437  C C   . SER A 225 ? 0.5152 0.4989 0.5691 0.0003  -0.0794 0.0826  225 SER A C   
3438  O O   . SER A 225 ? 0.5114 0.5056 0.5632 0.0047  -0.0720 0.0838  225 SER A O   
3439  C CB  . SER A 225 ? 0.5727 0.5449 0.6321 -0.0013 -0.0895 0.0705  225 SER A CB  
3440  O OG  . SER A 225 ? 0.6358 0.6212 0.6951 0.0000  -0.0851 0.0740  225 SER A OG  
3446  N N   . VAL A 226 ? 0.5557 0.5384 0.6120 -0.0064 -0.0842 0.0903  226 VAL A N   
3447  C CA  . VAL A 226 ? 0.5702 0.5683 0.6260 -0.0100 -0.0796 0.1002  226 VAL A CA  
3448  C C   . VAL A 226 ? 0.5856 0.5850 0.6476 -0.0214 -0.0869 0.1101  226 VAL A C   
3449  O O   . VAL A 226 ? 0.6369 0.6196 0.7011 -0.0260 -0.0966 0.1102  226 VAL A O   
3450  C CB  . VAL A 226 ? 0.5354 0.5333 0.5822 -0.0072 -0.0750 0.1010  226 VAL A CB  
3451  C CG1 . VAL A 226 ? 0.5582 0.5540 0.5995 0.0027  -0.0679 0.0913  226 VAL A CG1 
3452  C CG2 . VAL A 226 ? 0.4944 0.4762 0.5389 -0.0111 -0.0839 0.1029  226 VAL A CG2 
3462  N N   . ALA A 227 ? 0.5819 0.6018 0.6477 -0.0261 -0.0823 0.1181  227 ALA A N   
3463  C CA  . ALA A 227 ? 0.6018 0.6276 0.6724 -0.0393 -0.0869 0.1299  227 ALA A CA  
3464  C C   . ALA A 227 ? 0.6050 0.6566 0.6737 -0.0413 -0.0771 0.1370  227 ALA A C   
3465  O O   . ALA A 227 ? 0.5892 0.6532 0.6552 -0.0313 -0.0677 0.1312  227 ALA A O   
3466  C CB  . ALA A 227 ? 0.5956 0.6241 0.6779 -0.0459 -0.0932 0.1304  227 ALA A CB  
3472  N N   . VAL A 228 ? 0.5931 0.6532 0.6632 -0.0546 -0.0792 0.1494  228 VAL A N   
3473  C CA  . VAL A 228 ? 0.5980 0.6858 0.6654 -0.0582 -0.0693 0.1562  228 VAL A CA  
3474  C C   . VAL A 228 ? 0.6689 0.7782 0.7479 -0.0718 -0.0696 0.1659  228 VAL A C   
3475  O O   . VAL A 228 ? 0.6883 0.7849 0.7732 -0.0834 -0.0797 0.1721  228 VAL A O   
3476  C CB  . VAL A 228 ? 0.5848 0.6664 0.6377 -0.0626 -0.0693 0.1634  228 VAL A CB  
3477  C CG1 . VAL A 228 ? 0.6083 0.6769 0.6511 -0.0486 -0.0667 0.1524  228 VAL A CG1 
3478  C CG2 . VAL A 228 ? 0.5994 0.6576 0.6509 -0.0752 -0.0825 0.1740  228 VAL A CG2 
3488  N N   . GLY A 229 ? 0.6708 0.8137 0.7544 -0.0702 -0.0587 0.1660  229 GLY A N   
3489  C CA  . GLY A 229 ? 0.6647 0.8355 0.7609 -0.0832 -0.0571 0.1746  229 GLY A CA  
3490  C C   . GLY A 229 ? 0.6331 0.8426 0.7342 -0.0761 -0.0435 0.1704  229 GLY A C   
3491  O O   . GLY A 229 ? 0.5950 0.8058 0.6934 -0.0590 -0.0374 0.1589  229 GLY A O   
3495  N N   . ASP A 230 ? 0.6432 0.8843 0.7521 -0.0897 -0.0390 0.1797  230 ASP A N   
3496  C CA  . ASP A 230 ? 0.6324 0.9160 0.7488 -0.0836 -0.0258 0.1750  230 ASP A CA  
3497  C C   . ASP A 230 ? 0.6032 0.9045 0.7398 -0.0753 -0.0263 0.1673  230 ASP A C   
3498  O O   . ASP A 230 ? 0.5925 0.8944 0.7412 -0.0860 -0.0342 0.1724  230 ASP A O   
3499  C CB  . ASP A 230 ? 0.6254 0.9404 0.7420 -0.1027 -0.0198 0.1880  230 ASP A CB  
3500  C CG  . ASP A 230 ? 0.6050 0.9651 0.7259 -0.0953 -0.0045 0.1813  230 ASP A CG  
3501  O OD1 . ASP A 230 ? 0.5766 0.9358 0.6949 -0.0749 0.0009  0.1672  230 ASP A OD1 
3502  O OD2 . ASP A 230 ? 0.5848 0.9817 0.7122 -0.1102 0.0021  0.1897  230 ASP A OD2 
3507  N N   . PHE A 231 ? 0.5922 0.9070 0.7325 -0.0559 -0.0190 0.1548  231 PHE A N   
3508  C CA  . PHE A 231 ? 0.5917 0.9220 0.7502 -0.0454 -0.0206 0.1475  231 PHE A CA  
3509  C C   . PHE A 231 ? 0.5834 0.9544 0.7535 -0.0329 -0.0092 0.1391  231 PHE A C   
3510  O O   . PHE A 231 ? 0.5947 0.9786 0.7800 -0.0207 -0.0109 0.1322  231 PHE A O   
3511  C CB  . PHE A 231 ? 0.5979 0.8922 0.7506 -0.0309 -0.0281 0.1394  231 PHE A CB  
3512  C CG  . PHE A 231 ? 0.5683 0.8277 0.7141 -0.0412 -0.0397 0.1446  231 PHE A CG  
3513  C CD1 . PHE A 231 ? 0.5651 0.8260 0.7231 -0.0493 -0.0488 0.1474  231 PHE A CD1 
3514  C CD2 . PHE A 231 ? 0.5576 0.7841 0.6858 -0.0425 -0.0421 0.1454  231 PHE A CD2 
3515  C CE1 . PHE A 231 ? 0.5684 0.7974 0.7207 -0.0579 -0.0597 0.1499  231 PHE A CE1 
3516  C CE2 . PHE A 231 ? 0.5429 0.7387 0.6667 -0.0504 -0.0531 0.1483  231 PHE A CE2 
3517  C CZ  . PHE A 231 ? 0.5564 0.7529 0.6921 -0.0579 -0.0617 0.1501  231 PHE A CZ  
3527  N N   . ASN A 232 ? 0.5984 0.9903 0.7616 -0.0348 0.0017  0.1390  232 ASN A N   
3528  C CA  . ASN A 232 ? 0.6033 1.0423 0.7805 -0.0266 0.0132  0.1313  232 ASN A CA  
3529  C C   . ASN A 232 ? 0.6514 1.1277 0.8297 -0.0462 0.0216  0.1410  232 ASN A C   
3530  O O   . ASN A 232 ? 0.6846 1.2008 0.8684 -0.0411 0.0338  0.1341  232 ASN A O   
3531  C CB  . ASN A 232 ? 0.6008 1.0349 0.7696 -0.0052 0.0204  0.1169  232 ASN A CB  
3532  C CG  . ASN A 232 ? 0.6573 1.0647 0.8007 -0.0089 0.0223  0.1186  232 ASN A CG  
3533  O OD1 . ASN A 232 ? 0.6875 1.0825 0.8194 -0.0272 0.0187  0.1314  232 ASN A OD1 
3534  N ND2 . ASN A 232 ? 0.7006 1.0985 0.8355 0.0085  0.0271  0.1056  232 ASN A ND2 
3541  N N   . GLY A 233 ? 0.6814 1.1451 0.8541 -0.0689 0.0152  0.1566  233 GLY A N   
3542  C CA  . GLY A 233 ? 0.6734 1.1726 0.8497 -0.0913 0.0212  0.1687  233 GLY A CA  
3543  C C   . GLY A 233 ? 0.7052 1.2245 0.8652 -0.0953 0.0336  0.1700  233 GLY A C   
3544  O O   . GLY A 233 ? 0.7303 1.2925 0.8960 -0.1104 0.0425  0.1768  233 GLY A O   
3548  N N   . ASP A 234 ? 0.7176 1.2090 0.8570 -0.0831 0.0345  0.1637  234 ASP A N   
3549  C CA  . ASP A 234 ? 0.7345 1.2427 0.8552 -0.0870 0.0451  0.1645  234 ASP A CA  
3550  C C   . ASP A 234 ? 0.7489 1.2254 0.8459 -0.1052 0.0380  0.1814  234 ASP A C   
3551  O O   . ASP A 234 ? 0.7279 1.2060 0.8041 -0.1062 0.0436  0.1819  234 ASP A O   
3552  C CB  . ASP A 234 ? 0.7233 1.2259 0.8368 -0.0619 0.0511  0.1452  234 ASP A CB  
3553  C CG  . ASP A 234 ? 0.7129 1.1592 0.8114 -0.0522 0.0405  0.1425  234 ASP A CG  
3554  O OD1 . ASP A 234 ? 0.7422 1.1549 0.8399 -0.0608 0.0282  0.1527  234 ASP A OD1 
3555  O OD2 . ASP A 234 ? 0.7296 1.1666 0.8179 -0.0360 0.0445  0.1292  234 ASP A OD2 
3560  N N   . GLY A 235 ? 0.7854 1.2327 0.8851 -0.1191 0.0250  0.1946  235 GLY A N   
3561  C CA  . GLY A 235 ? 0.7897 1.2034 0.8694 -0.1352 0.0158  0.2108  235 GLY A CA  
3562  C C   . GLY A 235 ? 0.8354 1.2043 0.8971 -0.1217 0.0088  0.2049  235 GLY A C   
3563  O O   . GLY A 235 ? 0.9044 1.2398 0.9525 -0.1323 -0.0019 0.2172  235 GLY A O   
3567  N N   . ILE A 236 ? 0.7770 1.1436 0.8389 -0.0989 0.0137  0.1866  236 ILE A N   
3568  C CA  . ILE A 236 ? 0.7700 1.0970 0.8165 -0.0864 0.0078  0.1797  236 ILE A CA  
3569  C C   . ILE A 236 ? 0.7502 1.0416 0.8071 -0.0786 -0.0037 0.1754  236 ILE A C   
3570  O O   . ILE A 236 ? 0.7142 1.0139 0.7873 -0.0670 -0.0020 0.1652  236 ILE A O   
3571  C CB  . ILE A 236 ? 0.7685 1.1095 0.8095 -0.0673 0.0186  0.1621  236 ILE A CB  
3572  C CG1 . ILE A 236 ? 0.7962 1.1745 0.8248 -0.0753 0.0303  0.1650  236 ILE A CG1 
3573  C CG2 . ILE A 236 ? 0.7322 1.0323 0.7594 -0.0554 0.0119  0.1545  236 ILE A CG2 
3574  C CD1 . ILE A 236 ? 0.8204 1.2215 0.8482 -0.0567 0.0424  0.1453  236 ILE A CD1 
3586  N N   . ASP A 237 ? 0.7625 1.0154 0.8100 -0.0846 -0.0159 0.1828  237 ASP A N   
3587  C CA  . ASP A 237 ? 0.7318 0.9516 0.7870 -0.0770 -0.0264 0.1771  237 ASP A CA  
3588  C C   . ASP A 237 ? 0.6943 0.9080 0.7504 -0.0555 -0.0219 0.1596  237 ASP A C   
3589  O O   . ASP A 237 ? 0.6971 0.9082 0.7405 -0.0469 -0.0170 0.1528  237 ASP A O   
3590  C CB  . ASP A 237 ? 0.7614 0.9422 0.8051 -0.0837 -0.0392 0.1848  237 ASP A CB  
3591  C CG  . ASP A 237 ? 0.8275 1.0025 0.8752 -0.1039 -0.0482 0.2013  237 ASP A CG  
3592  O OD1 . ASP A 237 ? 0.8549 1.0573 0.9147 -0.1142 -0.0442 0.2069  237 ASP A OD1 
3593  O OD2 . ASP A 237 ? 0.8400 0.9829 0.8798 -0.1096 -0.0600 0.2084  237 ASP A OD2 
3598  N N   . ASP A 238 ? 0.6683 0.8793 0.7387 -0.0476 -0.0243 0.1528  238 ASP A N   
3599  C CA  . ASP A 238 ? 0.6248 0.8263 0.6967 -0.0288 -0.0219 0.1383  238 ASP A CA  
3600  C C   . ASP A 238 ? 0.6146 0.7778 0.6826 -0.0257 -0.0321 0.1356  238 ASP A C   
3601  O O   . ASP A 238 ? 0.6480 0.7944 0.7161 -0.0365 -0.0415 0.1431  238 ASP A O   
3602  C CB  . ASP A 238 ? 0.5769 0.8034 0.6663 -0.0212 -0.0178 0.1331  238 ASP A CB  
3603  C CG  . ASP A 238 ? 0.5949 0.8642 0.6910 -0.0240 -0.0072 0.1343  238 ASP A CG  
3604  O OD1 . ASP A 238 ? 0.6013 0.8809 0.6872 -0.0195 0.0011  0.1298  238 ASP A OD1 
3605  O OD2 . ASP A 238 ? 0.5853 0.8801 0.6971 -0.0311 -0.0070 0.1391  238 ASP A OD2 
3610  N N   . PHE A 239 ? 0.5610 0.7105 0.6259 -0.0110 -0.0304 0.1241  239 PHE A N   
3611  C CA  . PHE A 239 ? 0.5811 0.6977 0.6405 -0.0076 -0.0379 0.1198  239 PHE A CA  
3612  C C   . PHE A 239 ? 0.5668 0.6778 0.6359 -0.0023 -0.0418 0.1156  239 PHE A C   
3613  O O   . PHE A 239 ? 0.5870 0.7080 0.6610 0.0082  -0.0371 0.1099  239 PHE A O   
3614  C CB  . PHE A 239 ? 0.5768 0.6810 0.6246 0.0026  -0.0337 0.1105  239 PHE A CB  
3615  C CG  . PHE A 239 ? 0.5821 0.6958 0.6190 -0.0007 -0.0290 0.1128  239 PHE A CG  
3616  C CD1 . PHE A 239 ? 0.6217 0.7387 0.6544 -0.0143 -0.0329 0.1245  239 PHE A CD1 
3617  C CD2 . PHE A 239 ? 0.6053 0.7239 0.6353 0.0092  -0.0214 0.1032  239 PHE A CD2 
3618  C CE1 . PHE A 239 ? 0.6667 0.7936 0.6869 -0.0180 -0.0290 0.1277  239 PHE A CE1 
3619  C CE2 . PHE A 239 ? 0.6447 0.7739 0.6631 0.0060  -0.0172 0.1043  239 PHE A CE2 
3620  C CZ  . PHE A 239 ? 0.6760 0.8104 0.6888 -0.0077 -0.0209 0.1170  239 PHE A CZ  
3630  N N   . VAL A 240 ? 0.5647 0.6590 0.6359 -0.0091 -0.0510 0.1182  240 VAL A N   
3631  C CA  . VAL A 240 ? 0.5410 0.6275 0.6180 -0.0052 -0.0559 0.1138  240 VAL A CA  
3632  C C   . VAL A 240 ? 0.5328 0.5919 0.6008 -0.0011 -0.0595 0.1068  240 VAL A C   
3633  O O   . VAL A 240 ? 0.5808 0.6255 0.6432 -0.0058 -0.0633 0.1077  240 VAL A O   
3634  C CB  . VAL A 240 ? 0.5414 0.6328 0.6286 -0.0167 -0.0638 0.1200  240 VAL A CB  
3635  C CG1 . VAL A 240 ? 0.5112 0.5983 0.6031 -0.0123 -0.0687 0.1147  240 VAL A CG1 
3636  C CG2 . VAL A 240 ? 0.5794 0.7007 0.6762 -0.0237 -0.0598 0.1278  240 VAL A CG2 
3646  N N   . SER A 241 ? 0.4382 0.4911 0.5049 0.0075  -0.0586 0.1002  241 SER A N   
3647  C CA  . SER A 241 ? 0.5172 0.5482 0.5758 0.0107  -0.0605 0.0931  241 SER A CA  
3648  C C   . SER A 241 ? 0.5993 0.6260 0.6582 0.0145  -0.0628 0.0891  241 SER A C   
3649  O O   . SER A 241 ? 0.5657 0.6029 0.6275 0.0201  -0.0605 0.0904  241 SER A O   
3650  C CB  . SER A 241 ? 0.5557 0.5810 0.6057 0.0177  -0.0537 0.0884  241 SER A CB  
3651  O OG  . SER A 241 ? 0.5825 0.5894 0.6261 0.0191  -0.0554 0.0816  241 SER A OG  
3657  N N   . GLY A 242 ? 0.6304 0.6425 0.6859 0.0119  -0.0677 0.0840  242 GLY A N   
3658  C CA  . GLY A 242 ? 0.6247 0.6331 0.6775 0.0142  -0.0697 0.0799  242 GLY A CA  
3659  C C   . GLY A 242 ? 0.6128 0.6115 0.6559 0.0206  -0.0641 0.0754  242 GLY A C   
3660  O O   . GLY A 242 ? 0.5914 0.5813 0.6302 0.0215  -0.0609 0.0717  242 GLY A O   
3664  N N   . VAL A 243 ? 0.5633 0.5637 0.6033 0.0245  -0.0636 0.0764  243 VAL A N   
3665  C CA  . VAL A 243 ? 0.5491 0.5391 0.5796 0.0295  -0.0590 0.0744  243 VAL A CA  
3666  C C   . VAL A 243 ? 0.5531 0.5403 0.5769 0.0275  -0.0622 0.0734  243 VAL A C   
3667  O O   . VAL A 243 ? 0.5644 0.5539 0.5854 0.0314  -0.0634 0.0783  243 VAL A O   
3668  C CB  . VAL A 243 ? 0.5673 0.5611 0.5993 0.0377  -0.0551 0.0786  243 VAL A CB  
3669  C CG1 . VAL A 243 ? 0.5860 0.5643 0.6086 0.0416  -0.0505 0.0760  243 VAL A CG1 
3670  C CG2 . VAL A 243 ? 0.6343 0.6392 0.6742 0.0385  -0.0525 0.0800  243 VAL A CG2 
3680  N N   . PRO A 244 ? 0.5258 0.5089 0.5466 0.0218  -0.0642 0.0668  244 PRO A N   
3681  C CA  . PRO A 244 ? 0.5411 0.5274 0.5566 0.0186  -0.0683 0.0650  244 PRO A CA  
3682  C C   . PRO A 244 ? 0.5791 0.5597 0.5813 0.0194  -0.0653 0.0668  244 PRO A C   
3683  O O   . PRO A 244 ? 0.6438 0.6294 0.6397 0.0171  -0.0691 0.0676  244 PRO A O   
3684  C CB  . PRO A 244 ? 0.5793 0.5634 0.5969 0.0134  -0.0706 0.0551  244 PRO A CB  
3685  C CG  . PRO A 244 ? 0.5455 0.5219 0.5650 0.0146  -0.0662 0.0521  244 PRO A CG  
3686  C CD  . PRO A 244 ? 0.5240 0.5017 0.5474 0.0187  -0.0637 0.0601  244 PRO A CD  
3694  N N   . ARG A 245 ? 0.5975 0.5678 0.5944 0.0216  -0.0593 0.0677  245 ARG A N   
3695  C CA  . ARG A 245 ? 0.6032 0.5655 0.5868 0.0209  -0.0569 0.0714  245 ARG A CA  
3696  C C   . ARG A 245 ? 0.5811 0.5379 0.5636 0.0283  -0.0577 0.0810  245 ARG A C   
3697  O O   . ARG A 245 ? 0.6566 0.6038 0.6277 0.0280  -0.0574 0.0864  245 ARG A O   
3698  C CB  . ARG A 245 ? 0.6039 0.5568 0.5822 0.0168  -0.0504 0.0656  245 ARG A CB  
3699  C CG  . ARG A 245 ? 0.5991 0.5587 0.5759 0.0098  -0.0496 0.0556  245 ARG A CG  
3700  C CD  . ARG A 245 ? 0.5886 0.5424 0.5596 0.0049  -0.0428 0.0507  245 ARG A CD  
3701  N NE  . ARG A 245 ? 0.5686 0.5143 0.5258 0.0016  -0.0401 0.0587  245 ARG A NE  
3702  C CZ  . ARG A 245 ? 0.6433 0.5939 0.5882 -0.0050 -0.0396 0.0599  245 ARG A CZ  
3703  N NH1 . ARG A 245 ? 0.7028 0.6681 0.6483 -0.0082 -0.0411 0.0516  245 ARG A NH1 
3704  N NH2 . ARG A 245 ? 0.6793 0.6197 0.6105 -0.0086 -0.0378 0.0695  245 ARG A NH2 
3718  N N   . ALA A 246 ? 0.5472 0.5102 0.5413 0.0348  -0.0590 0.0832  246 ALA A N   
3719  C CA  . ALA A 246 ? 0.5728 0.5326 0.5688 0.0440  -0.0599 0.0900  246 ALA A CA  
3720  C C   . ALA A 246 ? 0.6333 0.5985 0.6257 0.0462  -0.0670 0.0976  246 ALA A C   
3721  O O   . ALA A 246 ? 0.6732 0.6475 0.6626 0.0403  -0.0712 0.0970  246 ALA A O   
3722  C CB  . ALA A 246 ? 0.5423 0.5134 0.5528 0.0500  -0.0588 0.0889  246 ALA A CB  
3728  N N   . ALA A 247 ? 0.7140 0.6732 0.7067 0.0554  -0.0693 0.1041  247 ALA A N   
3729  C CA  . ALA A 247 ? 0.7410 0.7043 0.7306 0.0595  -0.0775 0.1126  247 ALA A CA  
3730  C C   . ALA A 247 ? 0.7607 0.7171 0.7319 0.0505  -0.0796 0.1158  247 ALA A C   
3731  O O   . ALA A 247 ? 0.7623 0.7305 0.7300 0.0479  -0.0861 0.1187  247 ALA A O   
3732  C CB  . ALA A 247 ? 0.7537 0.7415 0.7576 0.0616  -0.0828 0.1124  247 ALA A CB  
3738  N N   . ARG A 248 ? 0.7808 0.7197 0.7400 0.0449  -0.0740 0.1150  248 ARG A N   
3739  C CA  . ARG A 248 ? 0.7934 0.7275 0.7341 0.0346  -0.0737 0.1174  248 ARG A CA  
3740  C C   . ARG A 248 ? 0.7629 0.7161 0.7036 0.0272  -0.0751 0.1105  248 ARG A C   
3741  O O   . ARG A 248 ? 0.7748 0.7352 0.7045 0.0233  -0.0803 0.1142  248 ARG A O   
3742  C CB  . ARG A 248 ? 0.8664 0.7900 0.7938 0.0374  -0.0807 0.1309  248 ARG A CB  
3743  C CG  . ARG A 248 ? 1.0106 0.9099 0.9366 0.0442  -0.0804 0.1374  248 ARG A CG  
3744  C CD  . ARG A 248 ? 1.1314 1.0147 1.0511 0.0357  -0.0712 0.1328  248 ARG A CD  
3745  N NE  . ARG A 248 ? 1.2059 1.0762 1.1046 0.0246  -0.0708 0.1410  248 ARG A NE  
3746  C CZ  . ARG A 248 ? 1.2037 1.0664 1.0949 0.0132  -0.0627 0.1371  248 ARG A CZ  
3747  N NH1 . ARG A 248 ? 1.1839 1.0500 1.0869 0.0123  -0.0554 0.1247  248 ARG A NH1 
3748  N NH2 . ARG A 248 ? 1.2206 1.0740 1.0922 0.0018  -0.0621 0.1459  248 ARG A NH2 
3762  N N   . THR A 249 ? 0.7084 0.6691 0.6612 0.0255  -0.0712 0.1000  249 THR A N   
3763  C CA  . THR A 249 ? 0.7251 0.6994 0.6802 0.0187  -0.0719 0.0904  249 THR A CA  
3764  C C   . THR A 249 ? 0.6821 0.6722 0.6457 0.0207  -0.0802 0.0911  249 THR A C   
3765  O O   . THR A 249 ? 0.6850 0.6850 0.6497 0.0151  -0.0826 0.0830  249 THR A O   
3766  C CB  . THR A 249 ? 0.7876 0.7629 0.7260 0.0095  -0.0698 0.0871  249 THR A CB  
3767  O OG1 . THR A 249 ? 0.8059 0.7848 0.7311 0.0088  -0.0760 0.0960  249 THR A OG1 
3768  C CG2 . THR A 249 ? 0.8585 0.8199 0.7887 0.0055  -0.0616 0.0873  249 THR A CG2 
3776  N N   . LEU A 250 ? 0.6830 0.6766 0.6536 0.0287  -0.0850 0.0994  250 LEU A N   
3777  C CA  . LEU A 250 ? 0.6547 0.6659 0.6381 0.0298  -0.0919 0.0988  250 LEU A CA  
3778  C C   . LEU A 250 ? 0.6363 0.6524 0.6356 0.0280  -0.0891 0.0918  250 LEU A C   
3779  O O   . LEU A 250 ? 0.6503 0.6786 0.6584 0.0238  -0.0941 0.0882  250 LEU A O   
3780  C CB  . LEU A 250 ? 0.6293 0.6463 0.6194 0.0395  -0.0974 0.1085  250 LEU A CB  
3781  C CG  . LEU A 250 ? 0.6263 0.6438 0.6031 0.0414  -0.1051 0.1170  250 LEU A CG  
3782  C CD1 . LEU A 250 ? 0.5665 0.5876 0.5532 0.0538  -0.1103 0.1257  250 LEU A CD1 
3783  C CD2 . LEU A 250 ? 0.6686 0.7023 0.6423 0.0343  -0.1123 0.1134  250 LEU A CD2 
3795  N N   . GLY A 251 ? 0.6009 0.6069 0.6032 0.0302  -0.0819 0.0903  251 GLY A N   
3796  C CA  . GLY A 251 ? 0.6013 0.6110 0.6167 0.0287  -0.0795 0.0859  251 GLY A CA  
3797  C C   . GLY A 251 ? 0.5749 0.5958 0.6038 0.0350  -0.0798 0.0912  251 GLY A C   
3798  O O   . GLY A 251 ? 0.5619 0.5939 0.5952 0.0395  -0.0847 0.0967  251 GLY A O   
3802  N N   . MET A 252 ? 0.4982 0.5181 0.5340 0.0354  -0.0746 0.0893  252 MET A N   
3803  C CA  . MET A 252 ? 0.5087 0.5430 0.5576 0.0401  -0.0733 0.0929  252 MET A CA  
3804  C C   . MET A 252 ? 0.4788 0.5161 0.5342 0.0337  -0.0708 0.0906  252 MET A C   
3805  O O   . MET A 252 ? 0.4580 0.4828 0.5077 0.0287  -0.0697 0.0860  252 MET A O   
3806  C CB  . MET A 252 ? 0.5400 0.5690 0.5876 0.0508  -0.0683 0.0945  252 MET A CB  
3807  C CG  . MET A 252 ? 0.5978 0.6235 0.6409 0.0584  -0.0724 0.0992  252 MET A CG  
3808  S SD  . MET A 252 ? 0.6251 0.6434 0.6703 0.0726  -0.0683 0.1000  252 MET A SD  
3809  C CE  . MET A 252 ? 0.6210 0.6698 0.6873 0.0784  -0.0678 0.0999  252 MET A CE  
3819  N N   . VAL A 253 ? 0.4752 0.5306 0.5429 0.0339  -0.0703 0.0941  253 VAL A N   
3820  C CA  . VAL A 253 ? 0.4607 0.5207 0.5335 0.0281  -0.0673 0.0946  253 VAL A CA  
3821  C C   . VAL A 253 ? 0.5144 0.5886 0.5931 0.0353  -0.0607 0.0963  253 VAL A C   
3822  O O   . VAL A 253 ? 0.5053 0.5980 0.5938 0.0402  -0.0614 0.0989  253 VAL A O   
3823  C CB  . VAL A 253 ? 0.4935 0.5643 0.5757 0.0172  -0.0736 0.0975  253 VAL A CB  
3824  C CG1 . VAL A 253 ? 0.5212 0.5993 0.6085 0.0108  -0.0705 0.1012  253 VAL A CG1 
3825  C CG2 . VAL A 253 ? 0.4186 0.4734 0.4949 0.0108  -0.0800 0.0929  253 VAL A CG2 
3835  N N   . TYR A 254 ? 0.6133 0.6805 0.6865 0.0364  -0.0546 0.0939  254 TYR A N   
3836  C CA  . TYR A 254 ? 0.5707 0.6518 0.6480 0.0431  -0.0475 0.0932  254 TYR A CA  
3837  C C   . TYR A 254 ? 0.5557 0.6538 0.6384 0.0342  -0.0454 0.0972  254 TYR A C   
3838  O O   . TYR A 254 ? 0.5574 0.6457 0.6354 0.0245  -0.0481 0.0992  254 TYR A O   
3839  C CB  . TYR A 254 ? 0.5950 0.6588 0.6615 0.0498  -0.0421 0.0872  254 TYR A CB  
3840  C CG  . TYR A 254 ? 0.6089 0.6548 0.6691 0.0579  -0.0433 0.0844  254 TYR A CG  
3841  C CD1 . TYR A 254 ? 0.6123 0.6611 0.6764 0.0619  -0.0484 0.0877  254 TYR A CD1 
3842  C CD2 . TYR A 254 ? 0.6140 0.6401 0.6638 0.0606  -0.0399 0.0791  254 TYR A CD2 
3843  C CE1 . TYR A 254 ? 0.6450 0.6758 0.7013 0.0681  -0.0500 0.0871  254 TYR A CE1 
3844  C CE2 . TYR A 254 ? 0.6369 0.6453 0.6802 0.0660  -0.0410 0.0780  254 TYR A CE2 
3845  C CZ  . TYR A 254 ? 0.6717 0.6817 0.7175 0.0696  -0.0461 0.0827  254 TYR A CZ  
3846  O OH  . TYR A 254 ? 0.7425 0.7334 0.7799 0.0737  -0.0478 0.0835  254 TYR A OH  
3856  N N   . ILE A 255 ? 0.5676 0.6919 0.6604 0.0374  -0.0409 0.0986  255 ILE A N   
3857  C CA  . ILE A 255 ? 0.5509 0.6946 0.6467 0.0291  -0.0365 0.1026  255 ILE A CA  
3858  C C   . ILE A 255 ? 0.5678 0.7221 0.6613 0.0389  -0.0272 0.0966  255 ILE A C   
3859  O O   . ILE A 255 ? 0.5775 0.7429 0.6784 0.0512  -0.0244 0.0916  255 ILE A O   
3860  C CB  . ILE A 255 ? 0.5752 0.7471 0.6865 0.0214  -0.0385 0.1089  255 ILE A CB  
3861  C CG1 . ILE A 255 ? 0.5760 0.7355 0.6892 0.0116  -0.0487 0.1131  255 ILE A CG1 
3862  C CG2 . ILE A 255 ? 0.5996 0.7926 0.7123 0.0110  -0.0330 0.1144  255 ILE A CG2 
3863  C CD1 . ILE A 255 ? 0.5829 0.7677 0.7113 0.0010  -0.0520 0.1195  255 ILE A CD1 
3875  N N   . TYR A 256 ? 0.4993 0.6497 0.5823 0.0339  -0.0233 0.0966  256 TYR A N   
3876  C CA  . TYR A 256 ? 0.5152 0.6766 0.5939 0.0415  -0.0145 0.0898  256 TYR A CA  
3877  C C   . TYR A 256 ? 0.5596 0.7485 0.6390 0.0311  -0.0093 0.0956  256 TYR A C   
3878  O O   . TYR A 256 ? 0.5624 0.7503 0.6401 0.0167  -0.0137 0.1057  256 TYR A O   
3879  C CB  . TYR A 256 ? 0.5168 0.6514 0.5800 0.0446  -0.0140 0.0838  256 TYR A CB  
3880  C CG  . TYR A 256 ? 0.5260 0.6338 0.5863 0.0538  -0.0173 0.0777  256 TYR A CG  
3881  C CD1 . TYR A 256 ? 0.5249 0.6106 0.5816 0.0484  -0.0245 0.0808  256 TYR A CD1 
3882  C CD2 . TYR A 256 ? 0.5354 0.6399 0.5958 0.0673  -0.0133 0.0686  256 TYR A CD2 
3883  C CE1 . TYR A 256 ? 0.5291 0.5926 0.5816 0.0548  -0.0266 0.0762  256 TYR A CE1 
3884  C CE2 . TYR A 256 ? 0.5480 0.6265 0.6044 0.0736  -0.0166 0.0649  256 TYR A CE2 
3885  C CZ  . TYR A 256 ? 0.5586 0.6179 0.6105 0.0666  -0.0228 0.0693  256 TYR A CZ  
3886  O OH  . TYR A 256 ? 0.5686 0.6045 0.6154 0.0712  -0.0252 0.0665  256 TYR A OH  
3896  N N   . ASP A 257 ? 0.5879 0.8010 0.6691 0.0384  -0.0002 0.0891  257 ASP A N   
3897  C CA  . ASP A 257 ? 0.6183 0.8609 0.6977 0.0282  0.0064  0.0941  257 ASP A CA  
3898  C C   . ASP A 257 ? 0.6463 0.8722 0.7066 0.0192  0.0053  0.0980  257 ASP A C   
3899  O O   . ASP A 257 ? 0.6836 0.8896 0.7326 0.0271  0.0057  0.0896  257 ASP A O   
3900  C CB  . ASP A 257 ? 0.6566 0.9305 0.7422 0.0400  0.0170  0.0832  257 ASP A CB  
3901  C CG  . ASP A 257 ? 0.7772 1.0910 0.8642 0.0286  0.0250  0.0886  257 ASP A CG  
3902  O OD1 . ASP A 257 ? 0.8307 1.1409 0.9040 0.0135  0.0242  0.0985  257 ASP A OD1 
3903  O OD2 . ASP A 257 ? 0.8265 1.1761 0.9285 0.0346  0.0319  0.0833  257 ASP A OD2 
3908  N N   . GLY A 258 ? 0.6160 0.8495 0.6728 0.0023  0.0030  0.1111  258 GLY A N   
3909  C CA  . GLY A 258 ? 0.6167 0.8349 0.6557 -0.0067 0.0001  0.1170  258 GLY A CA  
3910  C C   . GLY A 258 ? 0.6291 0.8667 0.6552 -0.0052 0.0092  0.1124  258 GLY A C   
3911  O O   . GLY A 258 ? 0.5992 0.8261 0.6090 -0.0125 0.0063  0.1176  258 GLY A O   
3915  N N   . LYS A 259 ? 0.6606 0.9271 0.6935 0.0046  0.0195  0.1020  259 LYS A N   
3916  C CA  . LYS A 259 ? 0.7170 1.0056 0.7381 0.0075  0.0292  0.0944  259 LYS A CA  
3917  C C   . LYS A 259 ? 0.7164 0.9907 0.7337 0.0257  0.0318  0.0760  259 LYS A C   
3918  O O   . LYS A 259 ? 0.7326 1.0063 0.7338 0.0267  0.0348  0.0699  259 LYS A O   
3919  C CB  . LYS A 259 ? 0.8152 1.1516 0.8471 0.0053  0.0400  0.0939  259 LYS A CB  
3920  C CG  . LYS A 259 ? 0.8815 1.2460 0.9050 0.0130  0.0518  0.0805  259 LYS A CG  
3921  C CD  . LYS A 259 ? 0.9207 1.3376 0.9526 0.0059  0.0629  0.0828  259 LYS A CD  
3922  C CE  . LYS A 259 ? 0.9601 1.3930 0.9731 -0.0151 0.0653  0.0980  259 LYS A CE  
3923  N NZ  . LYS A 259 ? 0.9615 1.4490 0.9815 -0.0241 0.0775  0.1005  259 LYS A NZ  
3937  N N   . ASN A 260 ? 0.7772 1.0388 0.8083 0.0393  0.0300  0.0674  260 ASN A N   
3938  C CA  . ASN A 260 ? 0.8218 1.0667 0.8503 0.0557  0.0315  0.0507  260 ASN A CA  
3939  C C   . ASN A 260 ? 0.7476 0.9554 0.7809 0.0623  0.0230  0.0496  260 ASN A C   
3940  O O   . ASN A 260 ? 0.7340 0.9266 0.7680 0.0757  0.0236  0.0370  260 ASN A O   
3941  C CB  . ASN A 260 ? 0.9563 1.2310 0.9964 0.0697  0.0408  0.0370  260 ASN A CB  
3942  C CG  . ASN A 260 ? 1.0601 1.3597 1.1209 0.0701  0.0417  0.0425  260 ASN A CG  
3943  O OD1 . ASN A 260 ? 1.0516 1.3389 1.1192 0.0630  0.0341  0.0542  260 ASN A OD1 
3944  N ND2 . ASN A 260 ? 1.1752 1.5123 1.2471 0.0786  0.0508  0.0328  260 ASN A ND2 
3950  N N   . MET A 261 ? 0.7086 0.9013 0.7449 0.0528  0.0150  0.0619  261 MET A N   
3951  C CA  . MET A 261 ? 0.6477 0.8082 0.6870 0.0574  0.0074  0.0613  261 MET A CA  
3952  C C   . MET A 261 ? 0.6737 0.8360 0.7262 0.0719  0.0085  0.0539  261 MET A C   
3953  O O   . MET A 261 ? 0.7040 0.8396 0.7556 0.0791  0.0044  0.0497  261 MET A O   
3954  C CB  . MET A 261 ? 0.6177 0.7490 0.6431 0.0586  0.0047  0.0553  261 MET A CB  
3955  C CG  . MET A 261 ? 0.6315 0.7321 0.6576 0.0577  -0.0033 0.0577  261 MET A CG  
3956  S SD  . MET A 261 ? 0.6735 0.7691 0.7010 0.0428  -0.0115 0.0721  261 MET A SD  
3957  C CE  . MET A 261 ? 0.6533 0.7402 0.6653 0.0349  -0.0137 0.0732  261 MET A CE  
3967  N N   . SER A 262 ? 0.6994 0.8939 0.7644 0.0762  0.0137  0.0526  262 SER A N   
3968  C CA  . SER A 262 ? 0.6846 0.8834 0.7647 0.0905  0.0129  0.0471  262 SER A CA  
3969  C C   . SER A 262 ? 0.6743 0.8681 0.7637 0.0853  0.0049  0.0579  262 SER A C   
3970  O O   . SER A 262 ? 0.7074 0.9113 0.7981 0.0711  0.0028  0.0685  262 SER A O   
3971  C CB  . SER A 262 ? 0.6795 0.9190 0.7718 0.0978  0.0214  0.0401  262 SER A CB  
3972  O OG  . SER A 262 ? 0.7538 0.9993 0.8632 0.1126  0.0192  0.0352  262 SER A OG  
3978  N N   . SER A 263 ? 0.6318 0.8088 0.7269 0.0964  -0.0003 0.0553  263 SER A N   
3979  C CA  . SER A 263 ? 0.5745 0.7456 0.6761 0.0920  -0.0086 0.0645  263 SER A CA  
3980  C C   . SER A 263 ? 0.6215 0.8297 0.7413 0.0909  -0.0079 0.0684  263 SER A C   
3981  O O   . SER A 263 ? 0.6599 0.8919 0.7921 0.1029  -0.0037 0.0614  263 SER A O   
3982  C CB  . SER A 263 ? 0.5279 0.6724 0.6288 0.1038  -0.0145 0.0617  263 SER A CB  
3983  O OG  . SER A 263 ? 0.5286 0.6687 0.6334 0.0991  -0.0226 0.0704  263 SER A OG  
3989  N N   . LEU A 264 ? 0.6170 0.8307 0.7394 0.0765  -0.0126 0.0787  264 LEU A N   
3990  C CA  . LEU A 264 ? 0.6194 0.8691 0.7593 0.0715  -0.0125 0.0835  264 LEU A CA  
3991  C C   . LEU A 264 ? 0.5773 0.8241 0.7269 0.0726  -0.0223 0.0881  264 LEU A C   
3992  O O   . LEU A 264 ? 0.5768 0.8463 0.7427 0.0825  -0.0234 0.0857  264 LEU A O   
3993  C CB  . LEU A 264 ? 0.6603 0.9224 0.7968 0.0518  -0.0104 0.0923  264 LEU A CB  
3994  C CG  . LEU A 264 ? 0.6642 0.9490 0.7965 0.0478  0.0001  0.0905  264 LEU A CG  
3995  C CD1 . LEU A 264 ? 0.6641 0.9579 0.7936 0.0264  -0.0009 0.1029  264 LEU A CD1 
3996  C CD2 . LEU A 264 ? 0.6768 1.0013 0.8250 0.0590  0.0082  0.0824  264 LEU A CD2 
4008  N N   A TYR A 265 ? 0.5824 0.8030 0.7225 0.0632  -0.0298 0.0939  265 TYR A N   
4009  N N   B TYR A 265 ? 0.5825 0.8035 0.7227 0.0629  -0.0298 0.0940  265 TYR A N   
4010  C CA  A TYR A 265 ? 0.5091 0.7287 0.6563 0.0627  -0.0394 0.0979  265 TYR A CA  
4011  C CA  B TYR A 265 ? 0.5085 0.7277 0.6554 0.0616  -0.0394 0.0982  265 TYR A CA  
4012  C C   A TYR A 265 ? 0.6063 0.7882 0.7376 0.0611  -0.0456 0.0986  265 TYR A C   
4013  C C   B TYR A 265 ? 0.6046 0.7857 0.7355 0.0619  -0.0454 0.0983  265 TYR A C   
4014  O O   A TYR A 265 ? 0.5942 0.7543 0.7116 0.0557  -0.0434 0.0977  265 TYR A O   
4015  O O   B TYR A 265 ? 0.6011 0.7592 0.7176 0.0584  -0.0428 0.0966  265 TYR A O   
4016  C CB  A TYR A 265 ? 0.5786 0.8215 0.7373 0.0471  -0.0425 0.1050  265 TYR A CB  
4017  C CB  B TYR A 265 ? 0.5808 0.8178 0.7361 0.0443  -0.0430 0.1058  265 TYR A CB  
4018  C CG  A TYR A 265 ? 0.5210 0.7695 0.6893 0.0470  -0.0525 0.1077  265 TYR A CG  
4019  C CG  B TYR A 265 ? 0.5382 0.8175 0.7110 0.0409  -0.0374 0.1071  265 TYR A CG  
4020  C CD1 A TYR A 265 ? 0.5524 0.8295 0.7385 0.0573  -0.0540 0.1059  265 TYR A CD1 
4021  C CD1 B TYR A 265 ? 0.5448 0.8531 0.7365 0.0502  -0.0390 0.1049  265 TYR A CD1 
4022  C CD2 A TYR A 265 ? 0.5399 0.7666 0.6999 0.0374  -0.0609 0.1109  265 TYR A CD2 
4023  C CD2 B TYR A 265 ? 0.5337 0.8256 0.7043 0.0279  -0.0308 0.1111  265 TYR A CD2 
4024  C CE1 A TYR A 265 ? 0.5234 0.8068 0.7176 0.0572  -0.0642 0.1085  265 TYR A CE1 
4025  C CE1 B TYR A 265 ? 0.5173 0.8687 0.7269 0.0467  -0.0331 0.1052  265 TYR A CE1 
4026  C CE2 A TYR A 265 ? 0.5093 0.7423 0.6765 0.0369  -0.0704 0.1125  265 TYR A CE2 
4027  C CE2 B TYR A 265 ? 0.5010 0.8347 0.6870 0.0228  -0.0246 0.1128  265 TYR A CE2 
4028  C CZ  A TYR A 265 ? 0.4837 0.7448 0.6674 0.0465  -0.0723 0.1119  265 TYR A CZ  
4029  C CZ  B TYR A 265 ? 0.5153 0.8800 0.7217 0.0322  -0.0253 0.1091  265 TYR A CZ  
4030  O OH  A TYR A 265 ? 0.4397 0.7080 0.6299 0.0460  -0.0829 0.1137  265 TYR A OH  
4031  O OH  B TYR A 265 ? 0.5457 0.9563 0.7693 0.0269  -0.0184 0.1098  265 TYR A OH  
4050  N N   . ASN A 266 ? 0.6109 0.7879 0.7445 0.0657  -0.0536 0.1001  266 ASN A N   
4051  C CA  . ASN A 266 ? 0.6294 0.7755 0.7482 0.0646  -0.0593 0.1006  266 ASN A CA  
4052  C C   . ASN A 266 ? 0.6072 0.7588 0.7299 0.0568  -0.0687 0.1048  266 ASN A C   
4053  O O   . ASN A 266 ? 0.6526 0.8287 0.7897 0.0591  -0.0727 0.1069  266 ASN A O   
4054  C CB  . ASN A 266 ? 0.6569 0.7867 0.7699 0.0796  -0.0602 0.0982  266 ASN A CB  
4055  C CG  . ASN A 266 ? 0.7028 0.8150 0.8062 0.0851  -0.0526 0.0927  266 ASN A CG  
4056  O OD1 . ASN A 266 ? 0.7148 0.8180 0.8100 0.0766  -0.0482 0.0911  266 ASN A OD1 
4057  N ND2 . ASN A 266 ? 0.8210 0.9271 0.9256 0.0997  -0.0520 0.0896  266 ASN A ND2 
4064  N N   . PHE A 267 ? 0.5437 0.6739 0.6541 0.0481  -0.0724 0.1047  267 PHE A N   
4065  C CA  . PHE A 267 ? 0.5695 0.6991 0.6789 0.0423  -0.0817 0.1062  267 PHE A CA  
4066  C C   . PHE A 267 ? 0.6150 0.7192 0.7072 0.0463  -0.0838 0.1045  267 PHE A C   
4067  O O   . PHE A 267 ? 0.6384 0.7227 0.7194 0.0482  -0.0782 0.1018  267 PHE A O   
4068  C CB  . PHE A 267 ? 0.6270 0.7559 0.7381 0.0268  -0.0848 0.1060  267 PHE A CB  
4069  C CG  . PHE A 267 ? 0.6570 0.8089 0.7831 0.0192  -0.0827 0.1095  267 PHE A CG  
4070  C CD1 . PHE A 267 ? 0.6755 0.8272 0.8007 0.0173  -0.0748 0.1102  267 PHE A CD1 
4071  C CD2 . PHE A 267 ? 0.6471 0.8220 0.7877 0.0127  -0.0889 0.1122  267 PHE A CD2 
4072  C CE1 . PHE A 267 ? 0.6596 0.8338 0.7967 0.0085  -0.0723 0.1147  267 PHE A CE1 
4073  C CE2 . PHE A 267 ? 0.6396 0.8371 0.7940 0.0034  -0.0865 0.1163  267 PHE A CE2 
4074  C CZ  . PHE A 267 ? 0.6279 0.8251 0.7800 0.0010  -0.0779 0.1180  267 PHE A CZ  
4084  N N   . THR A 268 ? 0.6312 0.7376 0.7208 0.0468  -0.0919 0.1064  268 THR A N   
4085  C CA  . THR A 268 ? 0.6096 0.6949 0.6813 0.0489  -0.0939 0.1061  268 THR A CA  
4086  C C   . THR A 268 ? 0.6344 0.7215 0.7006 0.0400  -0.1019 0.1046  268 THR A C   
4087  O O   . THR A 268 ? 0.6359 0.7422 0.7125 0.0373  -0.1089 0.1060  268 THR A O   
4088  C CB  . THR A 268 ? 0.6637 0.7465 0.7328 0.0619  -0.0960 0.1110  268 THR A CB  
4089  O OG1 . THR A 268 ? 0.7082 0.7889 0.7831 0.0711  -0.0889 0.1100  268 THR A OG1 
4090  C CG2 . THR A 268 ? 0.6863 0.7463 0.7348 0.0614  -0.0977 0.1125  268 THR A CG2 
4098  N N   . GLY A 269 ? 0.6232 0.6919 0.6733 0.0354  -0.1007 0.1008  269 GLY A N   
4099  C CA  . GLY A 269 ? 0.6325 0.7025 0.6751 0.0277  -0.1074 0.0971  269 GLY A CA  
4100  C C   . GLY A 269 ? 0.6768 0.7537 0.7122 0.0319  -0.1150 0.1024  269 GLY A C   
4101  O O   . GLY A 269 ? 0.6910 0.7665 0.7249 0.0416  -0.1152 0.1096  269 GLY A O   
4105  N N   . GLU A 270 ? 0.7756 0.8595 0.8061 0.0247  -0.1222 0.0985  270 GLU A N   
4106  C CA  . GLU A 270 ? 0.8598 0.9528 0.8821 0.0270  -0.1311 0.1033  270 GLU A CA  
4107  C C   . GLU A 270 ? 0.8590 0.9403 0.8571 0.0233  -0.1311 0.1016  270 GLU A C   
4108  O O   . GLU A 270 ? 0.9356 1.0209 0.9220 0.0259  -0.1378 0.1082  270 GLU A O   
4109  C CB  . GLU A 270 ? 0.9687 1.0828 1.0027 0.0209  -0.1408 0.0998  270 GLU A CB  
4110  C CG  . GLU A 270 ? 1.1510 1.2830 1.2096 0.0228  -0.1418 0.1027  270 GLU A CG  
4111  C CD  . GLU A 270 ? 1.2794 1.4261 1.3451 0.0341  -0.1467 0.1116  270 GLU A CD  
4112  O OE1 . GLU A 270 ? 1.3207 1.4568 1.3826 0.0446  -0.1417 0.1171  270 GLU A OE1 
4113  O OE2 . GLU A 270 ? 1.3295 1.4983 1.4055 0.0328  -0.1563 0.1126  270 GLU A OE2 
4120  N N   . GLN A 271 ? 0.7995 0.8681 0.7897 0.0173  -0.1241 0.0934  271 GLN A N   
4121  C CA  . GLN A 271 ? 0.7508 0.8143 0.7196 0.0118  -0.1233 0.0893  271 GLN A CA  
4122  C C   . GLN A 271 ? 0.7888 0.8347 0.7490 0.0111  -0.1124 0.0874  271 GLN A C   
4123  O O   . GLN A 271 ? 0.8174 0.8564 0.7891 0.0117  -0.1064 0.0829  271 GLN A O   
4124  C CB  . GLN A 271 ? 0.7008 0.7735 0.6701 0.0032  -0.1277 0.0760  271 GLN A CB  
4125  C CG  . GLN A 271 ? 0.7336 0.8061 0.6807 -0.0026 -0.1265 0.0696  271 GLN A CG  
4126  C CD  . GLN A 271 ? 0.7739 0.8551 0.7232 -0.0097 -0.1309 0.0536  271 GLN A CD  
4127  O OE1 . GLN A 271 ? 0.7944 0.8693 0.7446 -0.0128 -0.1256 0.0414  271 GLN A OE1 
4128  N NE2 . GLN A 271 ? 0.7729 0.8686 0.7239 -0.0118 -0.1416 0.0527  271 GLN A NE2 
4137  N N   . MET A 272 ? 0.8126 0.8524 0.7520 0.0090  -0.1103 0.0913  272 MET A N   
4138  C CA  . MET A 272 ? 0.8152 0.8402 0.7458 0.0068  -0.1002 0.0901  272 MET A CA  
4139  C C   . MET A 272 ? 0.8011 0.8285 0.7347 0.0003  -0.0950 0.0744  272 MET A C   
4140  O O   . MET A 272 ? 0.8131 0.8515 0.7409 -0.0052 -0.0982 0.0651  272 MET A O   
4141  C CB  . MET A 272 ? 0.8931 0.9130 0.7998 0.0035  -0.0998 0.0988  272 MET A CB  
4142  C CG  . MET A 272 ? 0.9697 0.9809 0.8732 0.0113  -0.1050 0.1152  272 MET A CG  
4143  S SD  . MET A 272 ? 1.0345 1.0204 0.9338 0.0137  -0.0964 0.1229  272 MET A SD  
4144  C CE  . MET A 272 ? 1.1046 1.0840 1.0155 0.0284  -0.1045 0.1356  272 MET A CE  
4154  N N   . ALA A 273 ? 0.7598 0.7770 0.7026 0.0017  -0.0877 0.0707  273 ALA A N   
4155  C CA  . ALA A 273 ? 0.7661 0.7836 0.7121 -0.0028 -0.0828 0.0564  273 ALA A CA  
4156  C C   . ALA A 273 ? 0.7207 0.7466 0.6795 -0.0041 -0.0892 0.0454  273 ALA A C   
4157  O O   . ALA A 273 ? 0.7120 0.7416 0.6703 -0.0079 -0.0885 0.0317  273 ALA A O   
4158  C CB  . ALA A 273 ? 0.8060 0.8272 0.7336 -0.0096 -0.0778 0.0515  273 ALA A CB  
4164  N N   . ALA A 274 ? 0.6847 0.7138 0.6558 -0.0012 -0.0958 0.0509  274 ALA A N   
4165  C CA  . ALA A 274 ? 0.6620 0.6950 0.6475 -0.0036 -0.1020 0.0422  274 ALA A CA  
4166  C C   . ALA A 274 ? 0.6169 0.6397 0.6158 -0.0025 -0.0985 0.0386  274 ALA A C   
4167  O O   . ALA A 274 ? 0.5581 0.5800 0.5686 -0.0050 -0.1039 0.0316  274 ALA A O   
4168  C CB  . ALA A 274 ? 0.6521 0.6947 0.6468 -0.0028 -0.1101 0.0500  274 ALA A CB  
4174  N N   . TYR A 275 ? 0.6246 0.6388 0.6215 0.0010  -0.0906 0.0433  275 TYR A N   
4175  C CA  . TYR A 275 ? 0.5988 0.6042 0.6067 0.0026  -0.0876 0.0418  275 TYR A CA  
4176  C C   . TYR A 275 ? 0.5864 0.5943 0.6083 0.0030  -0.0922 0.0485  275 TYR A C   
4177  O O   . TYR A 275 ? 0.5642 0.5672 0.5962 0.0012  -0.0943 0.0456  275 TYR A O   
4178  C CB  . TYR A 275 ? 0.6027 0.6042 0.6136 0.0003  -0.0880 0.0278  275 TYR A CB  
4179  C CG  . TYR A 275 ? 0.6595 0.6534 0.6692 0.0024  -0.0804 0.0256  275 TYR A CG  
4180  C CD1 . TYR A 275 ? 0.6949 0.6813 0.7141 0.0048  -0.0797 0.0288  275 TYR A CD1 
4181  C CD2 . TYR A 275 ? 0.6808 0.6764 0.6793 0.0011  -0.0739 0.0209  275 TYR A CD2 
4182  C CE1 . TYR A 275 ? 0.6985 0.6791 0.7167 0.0066  -0.0736 0.0263  275 TYR A CE1 
4183  C CE2 . TYR A 275 ? 0.6850 0.6753 0.6837 0.0020  -0.0672 0.0186  275 TYR A CE2 
4184  C CZ  . TYR A 275 ? 0.6771 0.6597 0.6860 0.0052  -0.0675 0.0209  275 TYR A CZ  
4185  O OH  . TYR A 275 ? 0.6865 0.6649 0.6958 0.0060  -0.0618 0.0179  275 TYR A OH  
4195  N N   . PHE A 276 ? 0.6464 0.6630 0.6689 0.0051  -0.0940 0.0580  276 PHE A N   
4196  C CA  . PHE A 276 ? 0.6100 0.6338 0.6460 0.0056  -0.0963 0.0655  276 PHE A CA  
4197  C C   . PHE A 276 ? 0.6021 0.6190 0.6426 0.0083  -0.0898 0.0683  276 PHE A C   
4198  O O   . PHE A 276 ? 0.6302 0.6426 0.6649 0.0139  -0.0833 0.0715  276 PHE A O   
4199  C CB  . PHE A 276 ? 0.5587 0.5942 0.5941 0.0102  -0.0978 0.0743  276 PHE A CB  
4200  C CG  . PHE A 276 ? 0.5759 0.6245 0.6263 0.0112  -0.0992 0.0813  276 PHE A CG  
4201  C CD1 . PHE A 276 ? 0.5841 0.6464 0.6449 0.0054  -0.1070 0.0816  276 PHE A CD1 
4202  C CD2 . PHE A 276 ? 0.6248 0.6740 0.6791 0.0175  -0.0927 0.0867  276 PHE A CD2 
4203  C CE1 . PHE A 276 ? 0.5763 0.6546 0.6520 0.0051  -0.1076 0.0881  276 PHE A CE1 
4204  C CE2 . PHE A 276 ? 0.6260 0.6917 0.6945 0.0183  -0.0929 0.0921  276 PHE A CE2 
4205  C CZ  . PHE A 276 ? 0.5950 0.6762 0.6745 0.0117  -0.1000 0.0932  276 PHE A CZ  
4215  N N   . GLY A 277 ? 0.5292 0.5445 0.5795 0.0037  -0.0924 0.0674  277 GLY A N   
4216  C CA  . GLY A 277 ? 0.5056 0.5152 0.5587 0.0051  -0.0875 0.0700  277 GLY A CA  
4217  C C   . GLY A 277 ? 0.5346 0.5304 0.5863 0.0031  -0.0883 0.0623  277 GLY A C   
4218  O O   . GLY A 277 ? 0.5004 0.4911 0.5531 0.0041  -0.0852 0.0642  277 GLY A O   
4222  N N   . PHE A 278 ? 0.5451 0.5361 0.5945 0.0010  -0.0926 0.0528  278 PHE A N   
4223  C CA  . PHE A 278 ? 0.5420 0.5216 0.5933 0.0004  -0.0949 0.0439  278 PHE A CA  
4224  C C   . PHE A 278 ? 0.5775 0.5510 0.6383 -0.0033 -0.1004 0.0486  278 PHE A C   
4225  O O   . PHE A 278 ? 0.5543 0.5184 0.6163 -0.0019 -0.1007 0.0466  278 PHE A O   
4226  C CB  . PHE A 278 ? 0.5465 0.5254 0.5967 -0.0014 -0.1002 0.0318  278 PHE A CB  
4227  C CG  . PHE A 278 ? 0.5217 0.4906 0.5757 -0.0001 -0.1030 0.0201  278 PHE A CG  
4228  C CD1 . PHE A 278 ? 0.5262 0.4952 0.5745 0.0037  -0.0966 0.0124  278 PHE A CD1 
4229  C CD2 . PHE A 278 ? 0.5414 0.5009 0.6057 -0.0026 -0.1128 0.0166  278 PHE A CD2 
4230  C CE1 . PHE A 278 ? 0.5579 0.5208 0.6120 0.0061  -0.0996 0.0005  278 PHE A CE1 
4231  C CE2 . PHE A 278 ? 0.5882 0.5379 0.6576 0.0005  -0.1168 0.0051  278 PHE A CE2 
4232  C CZ  . PHE A 278 ? 0.5703 0.5233 0.6352 0.0055  -0.1101 -0.0035 278 PHE A CZ  
4242  N N   . SER A 279 ? 0.6085 0.5882 0.6761 -0.0088 -0.1052 0.0557  279 SER A N   
4243  C CA  . SER A 279 ? 0.6210 0.5956 0.6968 -0.0149 -0.1107 0.0626  279 SER A CA  
4244  C C   . SER A 279 ? 0.5918 0.5824 0.6720 -0.0189 -0.1083 0.0747  279 SER A C   
4245  O O   . SER A 279 ? 0.6230 0.6271 0.7035 -0.0177 -0.1066 0.0756  279 SER A O   
4246  C CB  . SER A 279 ? 0.6492 0.6127 0.7322 -0.0206 -0.1223 0.0561  279 SER A CB  
4247  O OG  . SER A 279 ? 0.7241 0.6963 0.8084 -0.0231 -0.1257 0.0519  279 SER A OG  
4253  N N   . VAL A 280 ? 0.6170 0.6077 0.7007 -0.0237 -0.1083 0.0839  280 VAL A N   
4254  C CA  . VAL A 280 ? 0.6063 0.6157 0.6958 -0.0288 -0.1054 0.0949  280 VAL A CA  
4255  C C   . VAL A 280 ? 0.5687 0.5728 0.6631 -0.0396 -0.1108 0.1038  280 VAL A C   
4256  O O   . VAL A 280 ? 0.5980 0.5848 0.6884 -0.0398 -0.1140 0.1037  280 VAL A O   
4257  C CB  . VAL A 280 ? 0.6066 0.6292 0.6910 -0.0208 -0.0940 0.0982  280 VAL A CB  
4258  C CG1 . VAL A 280 ? 0.6571 0.6823 0.7364 -0.0112 -0.0901 0.0916  280 VAL A CG1 
4259  C CG2 . VAL A 280 ? 0.6150 0.6272 0.6920 -0.0182 -0.0903 0.0988  280 VAL A CG2 
4269  N N   . ALA A 281 ? 0.5303 0.5499 0.6335 -0.0490 -0.1124 0.1123  281 ALA A N   
4270  C CA  . ALA A 281 ? 0.5337 0.5501 0.6411 -0.0620 -0.1173 0.1233  281 ALA A CA  
4271  C C   . ALA A 281 ? 0.5749 0.6206 0.6895 -0.0692 -0.1114 0.1334  281 ALA A C   
4272  O O   . ALA A 281 ? 0.6036 0.6692 0.7246 -0.0658 -0.1083 0.1306  281 ALA A O   
4273  C CB  . ALA A 281 ? 0.5299 0.5269 0.6439 -0.0712 -0.1309 0.1208  281 ALA A CB  
4279  N N   . ALA A 282 ? 0.5999 0.6496 0.7136 -0.0791 -0.1101 0.1454  282 ALA A N   
4280  C CA  . ALA A 282 ? 0.5697 0.6509 0.6908 -0.0876 -0.1035 0.1552  282 ALA A CA  
4281  C C   . ALA A 282 ? 0.6290 0.7055 0.7544 -0.1072 -0.1109 0.1681  282 ALA A C   
4282  O O   . ALA A 282 ? 0.6630 0.7208 0.7795 -0.1122 -0.1143 0.1752  282 ALA A O   
4283  C CB  . ALA A 282 ? 0.5352 0.6336 0.6482 -0.0799 -0.0906 0.1573  282 ALA A CB  
4289  N N   . THR A 283 ? 0.6350 0.7282 0.7742 -0.1187 -0.1142 0.1716  283 THR A N   
4290  C CA  . THR A 283 ? 0.6603 0.7510 0.8054 -0.1399 -0.1214 0.1848  283 THR A CA  
4291  C C   . THR A 283 ? 0.6754 0.7994 0.8374 -0.1499 -0.1198 0.1873  283 THR A C   
4292  O O   . THR A 283 ? 0.6733 0.8088 0.8432 -0.1411 -0.1200 0.1767  283 THR A O   
4293  C CB  . THR A 283 ? 0.7034 0.7536 0.8478 -0.1455 -0.1372 0.1826  283 THR A CB  
4294  O OG1 . THR A 283 ? 0.7691 0.8140 0.9190 -0.1674 -0.1451 0.1969  283 THR A OG1 
4295  C CG2 . THR A 283 ? 0.6874 0.7318 0.8397 -0.1388 -0.1439 0.1676  283 THR A CG2 
4303  N N   . ASP A 284 ? 0.6805 0.8214 0.8478 -0.1690 -0.1184 0.2017  284 ASP A N   
4304  C CA  . ASP A 284 ? 0.6697 0.8452 0.8553 -0.1813 -0.1173 0.2050  284 ASP A CA  
4305  C C   . ASP A 284 ? 0.7236 0.8771 0.9187 -0.1939 -0.1331 0.2033  284 ASP A C   
4306  O O   . ASP A 284 ? 0.7710 0.9020 0.9650 -0.2115 -0.1422 0.2138  284 ASP A O   
4307  C CB  . ASP A 284 ? 0.6497 0.8542 0.8374 -0.1988 -0.1091 0.2211  284 ASP A CB  
4308  C CG  . ASP A 284 ? 0.6691 0.9136 0.8780 -0.2128 -0.1075 0.2242  284 ASP A CG  
4309  O OD1 . ASP A 284 ? 0.6768 0.9343 0.8983 -0.2036 -0.1097 0.2125  284 ASP A OD1 
4310  O OD2 . ASP A 284 ? 0.7048 0.9689 0.9178 -0.2337 -0.1043 0.2387  284 ASP A OD2 
4315  N N   . ILE A 285 ? 0.7408 0.9001 0.9449 -0.1852 -0.1371 0.1901  285 ILE A N   
4316  C CA  . ILE A 285 ? 0.8046 0.9412 1.0160 -0.1943 -0.1526 0.1846  285 ILE A CA  
4317  C C   . ILE A 285 ? 0.8234 0.9871 1.0542 -0.2145 -0.1566 0.1905  285 ILE A C   
4318  O O   . ILE A 285 ? 0.8461 0.9894 1.0836 -0.2276 -0.1705 0.1886  285 ILE A O   
4319  C CB  . ILE A 285 ? 0.8383 0.9653 1.0466 -0.1753 -0.1560 0.1666  285 ILE A CB  
4320  C CG1 . ILE A 285 ? 0.9047 0.9944 1.1127 -0.1805 -0.1720 0.1582  285 ILE A CG1 
4321  C CG2 . ILE A 285 ? 0.8376 1.0040 1.0589 -0.1708 -0.1525 0.1613  285 ILE A CG2 
4322  C CD1 . ILE A 285 ? 0.9458 0.9939 1.1406 -0.1774 -0.1767 0.1587  285 ILE A CD1 
4334  N N   . ASN A 286 ? 0.8133 1.0231 1.0545 -0.2176 -0.1453 0.1965  286 ASN A N   
4335  C CA  . ASN A 286 ? 0.7826 1.0256 1.0450 -0.2353 -0.1482 0.2003  286 ASN A CA  
4336  C C   . ASN A 286 ? 0.7761 1.0483 1.0449 -0.2553 -0.1396 0.2174  286 ASN A C   
4337  O O   . ASN A 286 ? 0.7985 1.1086 1.0868 -0.2694 -0.1386 0.2209  286 ASN A O   
4338  C CB  . ASN A 286 ? 0.7509 1.0307 1.0251 -0.2199 -0.1441 0.1888  286 ASN A CB  
4339  C CG  . ASN A 286 ? 0.7330 1.0415 1.0034 -0.2020 -0.1279 0.1884  286 ASN A CG  
4340  O OD1 . ASN A 286 ? 0.7437 1.0343 0.9972 -0.1933 -0.1209 0.1909  286 ASN A OD1 
4341  N ND2 . ASN A 286 ? 0.6956 1.0488 0.9826 -0.1959 -0.1227 0.1845  286 ASN A ND2 
4348  N N   . GLY A 287 ? 0.7704 1.0287 1.0233 -0.2572 -0.1333 0.2281  287 GLY A N   
4349  C CA  . GLY A 287 ? 0.8060 1.0836 1.0610 -0.2807 -0.1278 0.2465  287 GLY A CA  
4350  C C   . GLY A 287 ? 0.8166 1.1528 1.0803 -0.2796 -0.1102 0.2495  287 GLY A C   
4351  O O   . GLY A 287 ? 0.8376 1.1992 1.1067 -0.3022 -0.1052 0.2642  287 GLY A O   
4355  N N   . ASP A 288 ? 0.7989 1.1578 1.0641 -0.2545 -0.1009 0.2362  288 ASP A N   
4356  C CA  . ASP A 288 ? 0.7828 1.1966 1.0567 -0.2502 -0.0842 0.2366  288 ASP A CA  
4357  C C   . ASP A 288 ? 0.7976 1.2086 1.0510 -0.2398 -0.0719 0.2395  288 ASP A C   
4358  O O   . ASP A 288 ? 0.8065 1.2597 1.0646 -0.2306 -0.0575 0.2358  288 ASP A O   
4359  C CB  . ASP A 288 ? 0.7690 1.2121 1.0587 -0.2287 -0.0818 0.2205  288 ASP A CB  
4360  C CG  . ASP A 288 ? 0.7999 1.2078 1.0753 -0.2019 -0.0854 0.2072  288 ASP A CG  
4361  O OD1 . ASP A 288 ? 0.8126 1.1751 1.0679 -0.1996 -0.0898 0.2090  288 ASP A OD1 
4362  O OD2 . ASP A 288 ? 0.7958 1.2224 1.0807 -0.1832 -0.0841 0.1954  288 ASP A OD2 
4367  N N   . ASP A 289 ? 0.7959 1.1594 1.0274 -0.2408 -0.0778 0.2452  289 ASP A N   
4368  C CA  . ASP A 289 ? 0.8062 1.1622 1.0163 -0.2321 -0.0685 0.2482  289 ASP A CA  
4369  C C   . ASP A 289 ? 0.7704 1.1311 0.9759 -0.2020 -0.0604 0.2315  289 ASP A C   
4370  O O   . ASP A 289 ? 0.7857 1.1489 0.9760 -0.1930 -0.0508 0.2313  289 ASP A O   
4371  C CB  . ASP A 289 ? 0.8805 1.2774 1.0897 -0.2495 -0.0557 0.2618  289 ASP A CB  
4372  C CG  . ASP A 289 ? 0.9862 1.3707 1.1937 -0.2812 -0.0638 0.2819  289 ASP A CG  
4373  O OD1 . ASP A 289 ? 1.0164 1.3490 1.2120 -0.2862 -0.0778 0.2878  289 ASP A OD1 
4374  O OD2 . ASP A 289 ? 1.0061 1.4331 1.2251 -0.3013 -0.0564 0.2919  289 ASP A OD2 
4379  N N   . TYR A 290 ? 0.7583 1.1195 0.9758 -0.1867 -0.0647 0.2179  290 TYR A N   
4380  C CA  . TYR A 290 ? 0.7410 1.0994 0.9535 -0.1590 -0.0595 0.2031  290 TYR A CA  
4381  C C   . TYR A 290 ? 0.7417 1.0487 0.9414 -0.1492 -0.0709 0.1968  290 TYR A C   
4382  O O   . TYR A 290 ? 0.7756 1.0665 0.9827 -0.1537 -0.0827 0.1941  290 TYR A O   
4383  C CB  . TYR A 290 ? 0.7473 1.1433 0.9808 -0.1477 -0.0565 0.1931  290 TYR A CB  
4384  C CG  . TYR A 290 ? 0.7245 1.1744 0.9697 -0.1471 -0.0420 0.1933  290 TYR A CG  
4385  C CD1 . TYR A 290 ? 0.6702 1.1305 0.9069 -0.1286 -0.0302 0.1858  290 TYR A CD1 
4386  C CD2 . TYR A 290 ? 0.7173 1.2093 0.9831 -0.1650 -0.0401 0.1997  290 TYR A CD2 
4387  C CE1 . TYR A 290 ? 0.6832 1.1944 0.9312 -0.1266 -0.0166 0.1835  290 TYR A CE1 
4388  C CE2 . TYR A 290 ? 0.7145 1.2601 0.9925 -0.1640 -0.0260 0.1983  290 TYR A CE2 
4389  C CZ  . TYR A 290 ? 0.7330 1.2880 1.0018 -0.1441 -0.0142 0.1897  290 TYR A CZ  
4390  O OH  . TYR A 290 ? 0.7719 1.3818 1.0534 -0.1418 0.0001  0.1860  290 TYR A OH  
4400  N N   . ALA A 291 ? 0.7113 0.9949 0.8925 -0.1362 -0.0673 0.1933  291 ALA A N   
4401  C CA  . ALA A 291 ? 0.6633 0.9014 0.8327 -0.1272 -0.0768 0.1868  291 ALA A CA  
4402  C C   . ALA A 291 ? 0.6082 0.8451 0.7854 -0.1124 -0.0807 0.1740  291 ALA A C   
4403  O O   . ALA A 291 ? 0.5639 0.8279 0.7486 -0.0997 -0.0735 0.1677  291 ALA A O   
4404  C CB  . ALA A 291 ? 0.6467 0.8671 0.7969 -0.1150 -0.0707 0.1843  291 ALA A CB  
4410  N N   . ASP A 292 ? 0.6371 0.8424 0.8119 -0.1139 -0.0927 0.1699  292 ASP A N   
4411  C CA  . ASP A 292 ? 0.6402 0.8416 0.8192 -0.1023 -0.0980 0.1587  292 ASP A CA  
4412  C C   . ASP A 292 ? 0.6612 0.8272 0.8240 -0.0889 -0.1002 0.1501  292 ASP A C   
4413  O O   . ASP A 292 ? 0.6939 0.8340 0.8457 -0.0919 -0.1021 0.1525  292 ASP A O   
4414  C CB  . ASP A 292 ? 0.6531 0.8534 0.8445 -0.1165 -0.1102 0.1591  292 ASP A CB  
4415  C CG  . ASP A 292 ? 0.6651 0.8997 0.8733 -0.1337 -0.1084 0.1690  292 ASP A CG  
4416  O OD1 . ASP A 292 ? 0.6585 0.9294 0.8742 -0.1287 -0.0978 0.1705  292 ASP A OD1 
4417  O OD2 . ASP A 292 ? 0.6987 0.9248 0.9133 -0.1526 -0.1177 0.1748  292 ASP A OD2 
4422  N N   . VAL A 293 ? 0.6492 0.8155 0.8110 -0.0745 -0.1003 0.1404  293 VAL A N   
4423  C CA  . VAL A 293 ? 0.6279 0.7684 0.7747 -0.0606 -0.0993 0.1322  293 VAL A CA  
4424  C C   . VAL A 293 ? 0.5982 0.7202 0.7432 -0.0603 -0.1096 0.1240  293 VAL A C   
4425  O O   . VAL A 293 ? 0.6066 0.7431 0.7592 -0.0595 -0.1137 0.1211  293 VAL A O   
4426  C CB  . VAL A 293 ? 0.6131 0.7673 0.7570 -0.0438 -0.0899 0.1283  293 VAL A CB  
4427  C CG1 . VAL A 293 ? 0.5895 0.7171 0.7184 -0.0318 -0.0894 0.1203  293 VAL A CG1 
4428  C CG2 . VAL A 293 ? 0.6229 0.7952 0.7674 -0.0432 -0.0793 0.1338  293 VAL A CG2 
4438  N N   . PHE A 294 ? 0.5676 0.6595 0.7027 -0.0605 -0.1139 0.1195  294 PHE A N   
4439  C CA  . PHE A 294 ? 0.5722 0.6461 0.7037 -0.0589 -0.1225 0.1092  294 PHE A CA  
4440  C C   . PHE A 294 ? 0.5835 0.6431 0.7012 -0.0451 -0.1174 0.1013  294 PHE A C   
4441  O O   . PHE A 294 ? 0.5111 0.5593 0.6217 -0.0415 -0.1124 0.1025  294 PHE A O   
4442  C CB  . PHE A 294 ? 0.6212 0.6725 0.7552 -0.0706 -0.1328 0.1086  294 PHE A CB  
4443  C CG  . PHE A 294 ? 0.6499 0.7123 0.7973 -0.0869 -0.1386 0.1173  294 PHE A CG  
4444  C CD1 . PHE A 294 ? 0.6347 0.7099 0.7860 -0.0949 -0.1332 0.1303  294 PHE A CD1 
4445  C CD2 . PHE A 294 ? 0.6715 0.7326 0.8272 -0.0953 -0.1494 0.1121  294 PHE A CD2 
4446  C CE1 . PHE A 294 ? 0.6165 0.7037 0.7803 -0.1120 -0.1379 0.1392  294 PHE A CE1 
4447  C CE2 . PHE A 294 ? 0.6612 0.7325 0.8302 -0.1120 -0.1551 0.1202  294 PHE A CE2 
4448  C CZ  . PHE A 294 ? 0.6475 0.7321 0.8208 -0.1209 -0.1491 0.1344  294 PHE A CZ  
4458  N N   . ILE A 295 ? 0.6257 0.6870 0.7391 -0.0385 -0.1190 0.0938  295 ILE A N   
4459  C CA  . ILE A 295 ? 0.5924 0.6430 0.6926 -0.0271 -0.1138 0.0872  295 ILE A CA  
4460  C C   . ILE A 295 ? 0.5843 0.6242 0.6790 -0.0276 -0.1208 0.0762  295 ILE A C   
4461  O O   . ILE A 295 ? 0.6227 0.6728 0.7212 -0.0311 -0.1272 0.0741  295 ILE A O   
4462  C CB  . ILE A 295 ? 0.5780 0.6441 0.6754 -0.0172 -0.1069 0.0906  295 ILE A CB  
4463  C CG1 . ILE A 295 ? 0.5765 0.6571 0.6808 -0.0160 -0.0998 0.0991  295 ILE A CG1 
4464  C CG2 . ILE A 295 ? 0.5495 0.6018 0.6326 -0.0077 -0.1017 0.0851  295 ILE A CG2 
4465  C CD1 . ILE A 295 ? 0.5775 0.6754 0.6836 -0.0057 -0.0949 0.1017  295 ILE A CD1 
4477  N N   . GLY A 296 ? 0.5182 0.5402 0.6044 -0.0240 -0.1195 0.0683  296 GLY A N   
4478  C CA  . GLY A 296 ? 0.5498 0.5632 0.6308 -0.0241 -0.1250 0.0557  296 GLY A CA  
4479  C C   . GLY A 296 ? 0.5887 0.6042 0.6561 -0.0162 -0.1187 0.0511  296 GLY A C   
4480  O O   . GLY A 296 ? 0.5769 0.5886 0.6382 -0.0103 -0.1104 0.0537  296 GLY A O   
4484  N N   . ALA A 297 ? 0.5943 0.6159 0.6564 -0.0171 -0.1231 0.0444  297 ALA A N   
4485  C CA  . ALA A 297 ? 0.5882 0.6121 0.6352 -0.0120 -0.1183 0.0404  297 ALA A CA  
4486  C C   . ALA A 297 ? 0.6251 0.6458 0.6674 -0.0148 -0.1232 0.0252  297 ALA A C   
4487  O O   . ALA A 297 ? 0.6187 0.6490 0.6563 -0.0175 -0.1287 0.0211  297 ALA A O   
4488  C CB  . ALA A 297 ? 0.5696 0.6083 0.6122 -0.0098 -0.1188 0.0491  297 ALA A CB  
4494  N N   . PRO A 298 ? 0.6412 0.6497 0.6846 -0.0137 -0.1217 0.0154  298 PRO A N   
4495  C CA  . PRO A 298 ? 0.6292 0.6347 0.6729 -0.0157 -0.1279 -0.0015 298 PRO A CA  
4496  C C   . PRO A 298 ? 0.6047 0.6215 0.6330 -0.0150 -0.1252 -0.0103 298 PRO A C   
4497  O O   . PRO A 298 ? 0.6299 0.6485 0.6576 -0.0169 -0.1307 -0.0256 298 PRO A O   
4498  C CB  . PRO A 298 ? 0.6620 0.6535 0.7116 -0.0123 -0.1259 -0.0086 298 PRO A CB  
4499  C CG  . PRO A 298 ? 0.6230 0.6092 0.6771 -0.0109 -0.1213 0.0062  298 PRO A CG  
4500  C CD  . PRO A 298 ? 0.6100 0.6081 0.6560 -0.0100 -0.1154 0.0184  298 PRO A CD  
4508  N N   . LEU A 299 ? 0.6176 0.6416 0.6328 -0.0128 -0.1173 -0.0015 299 LEU A N   
4509  C CA  . LEU A 299 ? 0.6566 0.6916 0.6544 -0.0138 -0.1144 -0.0072 299 LEU A CA  
4510  C C   . LEU A 299 ? 0.6677 0.7145 0.6569 -0.0157 -0.1188 0.0024  299 LEU A C   
4511  O O   . LEU A 299 ? 0.6747 0.7306 0.6465 -0.0169 -0.1167 0.0020  299 LEU A O   
4512  C CB  . LEU A 299 ? 0.6827 0.7158 0.6700 -0.0114 -0.1031 -0.0042 299 LEU A CB  
4513  C CG  . LEU A 299 ? 0.7192 0.7421 0.7164 -0.0086 -0.0985 -0.0109 299 LEU A CG  
4514  C CD1 . LEU A 299 ? 0.7466 0.7701 0.7331 -0.0079 -0.0876 -0.0081 299 LEU A CD1 
4515  C CD2 . LEU A 299 ? 0.7240 0.7469 0.7287 -0.0086 -0.1033 -0.0305 299 LEU A CD2 
4527  N N   . PHE A 300 ? 0.6453 0.6934 0.6463 -0.0162 -0.1251 0.0115  300 PHE A N   
4528  C CA  . PHE A 300 ? 0.6674 0.7287 0.6635 -0.0172 -0.1310 0.0198  300 PHE A CA  
4529  C C   . PHE A 300 ? 0.7052 0.7771 0.6918 -0.0219 -0.1380 0.0073  300 PHE A C   
4530  O O   . PHE A 300 ? 0.7145 0.7833 0.7076 -0.0252 -0.1425 -0.0078 300 PHE A O   
4531  C CB  . PHE A 300 ? 0.6699 0.7342 0.6845 -0.0181 -0.1368 0.0283  300 PHE A CB  
4532  C CG  . PHE A 300 ? 0.6407 0.7217 0.6547 -0.0188 -0.1443 0.0356  300 PHE A CG  
4533  C CD1 . PHE A 300 ? 0.6441 0.7349 0.6594 -0.0249 -0.1546 0.0268  300 PHE A CD1 
4534  C CD2 . PHE A 300 ? 0.6647 0.7516 0.6778 -0.0127 -0.1420 0.0503  300 PHE A CD2 
4535  C CE1 . PHE A 300 ? 0.6380 0.7461 0.6534 -0.0255 -0.1625 0.0332  300 PHE A CE1 
4536  C CE2 . PHE A 300 ? 0.6783 0.7818 0.6924 -0.0120 -0.1501 0.0568  300 PHE A CE2 
4537  C CZ  . PHE A 300 ? 0.6408 0.7559 0.6561 -0.0187 -0.1605 0.0486  300 PHE A CZ  
4547  N N   . MET A 301 ? 0.7532 0.8372 0.7239 -0.0219 -0.1398 0.0134  301 MET A N   
4548  C CA  . MET A 301 ? 0.7988 0.8954 0.7557 -0.0265 -0.1459 0.0023  301 MET A CA  
4549  C C   . MET A 301 ? 0.7907 0.9009 0.7517 -0.0285 -0.1576 0.0080  301 MET A C   
4550  O O   . MET A 301 ? 0.7417 0.8573 0.7004 -0.0248 -0.1588 0.0241  301 MET A O   
4551  C CB  . MET A 301 ? 0.8381 0.9398 0.7697 -0.0265 -0.1390 0.0048  301 MET A CB  
4552  C CG  . MET A 301 ? 0.8218 0.9161 0.7491 -0.0265 -0.1280 -0.0051 301 MET A CG  
4553  S SD  . MET A 301 ? 0.8064 0.9096 0.7031 -0.0299 -0.1195 -0.0017 301 MET A SD  
4554  C CE  . MET A 301 ? 0.8224 0.9140 0.7158 -0.0254 -0.1163 0.0246  301 MET A CE  
4564  N N   . ASP A 302 ? 0.8651 0.9806 0.8330 -0.0340 -0.1668 -0.0059 302 ASP A N   
4565  C CA  . ASP A 302 ? 0.9523 1.0831 0.9248 -0.0376 -0.1791 -0.0038 302 ASP A CA  
4566  C C   . ASP A 302 ? 0.9734 1.1197 0.9222 -0.0400 -0.1838 -0.0097 302 ASP A C   
4567  O O   . ASP A 302 ? 1.0005 1.1462 0.9313 -0.0406 -0.1777 -0.0192 302 ASP A O   
4568  C CB  . ASP A 302 ? 1.0647 1.1915 1.0576 -0.0440 -0.1875 -0.0158 302 ASP A CB  
4569  C CG  . ASP A 302 ? 1.1916 1.3347 1.1945 -0.0488 -0.2000 -0.0119 302 ASP A CG  
4570  O OD1 . ASP A 302 ? 1.2413 1.3974 1.2425 -0.0451 -0.2011 0.0035  302 ASP A OD1 
4571  O OD2 . ASP A 302 ? 1.2469 1.3899 1.2604 -0.0563 -0.2093 -0.0248 302 ASP A OD2 
4576  N N   . ARG A 303 ? 0.9891 1.1517 0.9379 -0.0418 -0.1948 -0.0039 303 ARG A N   
4577  C CA  . ARG A 303 ? 0.9677 1.1474 0.8942 -0.0450 -0.2019 -0.0091 303 ARG A CA  
4578  C C   . ARG A 303 ? 0.9611 1.1486 0.8954 -0.0526 -0.2131 -0.0285 303 ARG A C   
4579  O O   . ARG A 303 ? 0.9686 1.1555 0.9265 -0.0557 -0.2204 -0.0288 303 ARG A O   
4580  C CB  . ARG A 303 ? 0.9815 1.1748 0.9017 -0.0411 -0.2085 0.0102  303 ARG A CB  
4581  C CG  . ARG A 303 ? 1.0875 1.2956 0.9775 -0.0431 -0.2134 0.0107  303 ARG A CG  
4582  C CD  . ARG A 303 ? 1.1376 1.3367 1.0029 -0.0412 -0.2012 0.0166  303 ARG A CD  
4583  N NE  . ARG A 303 ? 1.1318 1.3191 0.9997 -0.0335 -0.1958 0.0383  303 ARG A NE  
4584  C CZ  . ARG A 303 ? 1.1575 1.3374 1.0035 -0.0320 -0.1883 0.0498  303 ARG A CZ  
4585  N NH1 . ARG A 303 ? 1.1818 1.3676 1.0009 -0.0385 -0.1843 0.0426  303 ARG A NH1 
4586  N NH2 . ARG A 303 ? 1.1372 1.3041 0.9881 -0.0245 -0.1848 0.0681  303 ARG A NH2 
4600  N N   . GLY A 304 ? 1.0471 1.2807 0.8330 -0.0594 -0.1906 0.1468  304 GLY A N   
4601  C CA  . GLY A 304 ? 1.0859 1.3273 0.8322 -0.1023 -0.2075 0.1192  304 GLY A CA  
4602  C C   . GLY A 304 ? 1.0862 1.4228 0.8074 -0.1132 -0.2236 0.1325  304 GLY A C   
4603  O O   . GLY A 304 ? 1.0553 1.4566 0.7902 -0.0801 -0.2216 0.1673  304 GLY A O   
4607  N N   . SER A 305 ? 1.1110 1.4544 0.7894 -0.1614 -0.2382 0.1039  305 SER A N   
4608  C CA  . SER A 305 ? 1.0971 1.5366 0.7437 -0.1829 -0.2555 0.1101  305 SER A CA  
4609  C C   . SER A 305 ? 1.1077 1.5637 0.7397 -0.1479 -0.2465 0.1318  305 SER A C   
4610  O O   . SER A 305 ? 1.1218 1.6772 0.7533 -0.1354 -0.2554 0.1588  305 SER A O   
4611  C CB  . SER A 305 ? 1.1405 1.5537 0.7291 -0.2460 -0.2655 0.0681  305 SER A CB  
4612  O OG  . SER A 305 ? 1.2156 1.6938 0.7817 -0.2608 -0.2684 0.0665  305 SER A OG  
4618  N N   . ASP A 306 ? 1.1383 1.5003 0.7603 -0.1298 -0.2266 0.1214  306 ASP A N   
4619  C CA  . ASP A 306 ? 1.1527 1.5170 0.7606 -0.0966 -0.2137 0.1415  306 ASP A CA  
4620  C C   . ASP A 306 ? 1.1064 1.4761 0.7568 -0.0423 -0.1966 0.1818  306 ASP A C   
4621  O O   . ASP A 306 ? 1.1140 1.4760 0.7527 -0.0123 -0.1812 0.2019  306 ASP A O   
4622  C CB  . ASP A 306 ? 1.1916 1.4572 0.7705 -0.1014 -0.1969 0.1133  306 ASP A CB  
4623  C CG  . ASP A 306 ? 1.1890 1.3679 0.7989 -0.0950 -0.1832 0.0982  306 ASP A CG  
4624  O OD1 . ASP A 306 ? 1.1835 1.3728 0.8343 -0.0901 -0.1870 0.1071  306 ASP A OD1 
4625  O OD2 . ASP A 306 ? 1.2328 1.3398 0.8257 -0.0935 -0.1682 0.0784  306 ASP A OD2 
4630  N N   . GLY A 307 ? 1.1163 1.4924 0.8099 -0.0302 -0.1959 0.1937  307 GLY A N   
4631  C CA  . GLY A 307 ? 1.1135 1.4783 0.8387 0.0190  -0.1745 0.2290  307 GLY A CA  
4632  C C   . GLY A 307 ? 1.1503 1.4108 0.8862 0.0324  -0.1484 0.2196  307 GLY A C   
4633  O O   . GLY A 307 ? 1.1217 1.3578 0.8711 0.0686  -0.1250 0.2463  307 GLY A O   
4637  N N   . LYS A 308 ? 1.1711 1.3707 0.8979 0.0042  -0.1494 0.1832  308 LYS A N   
4638  C CA  . LYS A 308 ? 1.2339 1.3523 0.9739 0.0129  -0.1268 0.1730  308 LYS A CA  
4639  C C   . LYS A 308 ? 1.1659 1.2532 0.9428 0.0072  -0.1258 0.1627  308 LYS A C   
4640  O O   . LYS A 308 ? 1.1548 1.2593 0.9374 -0.0154 -0.1444 0.1478  308 LYS A O   
4641  C CB  . LYS A 308 ? 1.3719 1.4495 1.0827 -0.0069 -0.1259 0.1430  308 LYS A CB  
4642  C CG  . LYS A 308 ? 1.4734 1.4868 1.1992 0.0016  -0.1033 0.1339  308 LYS A CG  
4643  C CD  . LYS A 308 ? 1.5709 1.5523 1.2672 -0.0112 -0.1007 0.1073  308 LYS A CD  
4644  C CE  . LYS A 308 ? 1.6882 1.6262 1.4051 -0.0023 -0.0792 0.1005  308 LYS A CE  
4645  N NZ  . LYS A 308 ? 1.7669 1.6787 1.4562 -0.0064 -0.0729 0.0785  308 LYS A NZ  
4659  N N   . LEU A 309 ? 1.0836 1.1249 0.8819 0.0245  -0.1029 0.1703  309 LEU A N   
4660  C CA  . LEU A 309 ? 0.9392 0.9486 0.7689 0.0168  -0.1004 0.1578  309 LEU A CA  
4661  C C   . LEU A 309 ? 0.8885 0.8633 0.7161 -0.0059 -0.1061 0.1253  309 LEU A C   
4662  O O   . LEU A 309 ? 0.8573 0.8128 0.6657 -0.0075 -0.0991 0.1153  309 LEU A O   
4663  C CB  . LEU A 309 ? 0.8889 0.8571 0.7337 0.0351  -0.0718 0.1719  309 LEU A CB  
4664  C CG  . LEU A 309 ? 0.8723 0.8524 0.7220 0.0631  -0.0587 0.2039  309 LEU A CG  
4665  C CD1 . LEU A 309 ? 0.8457 0.7625 0.6935 0.0743  -0.0235 0.2124  309 LEU A CD1 
4666  C CD2 . LEU A 309 ? 0.8551 0.8608 0.7292 0.0597  -0.0725 0.2028  309 LEU A CD2 
4678  N N   . GLN A 310 ? 0.9340 0.9016 0.7794 -0.0200 -0.1168 0.1110  310 GLN A N   
4679  C CA  . GLN A 310 ? 0.9884 0.9212 0.8304 -0.0344 -0.1195 0.0848  310 GLN A CA  
4680  C C   . GLN A 310 ? 0.9375 0.8562 0.8114 -0.0377 -0.1190 0.0798  310 GLN A C   
4681  O O   . GLN A 310 ? 0.9329 0.8701 0.8174 -0.0445 -0.1306 0.0833  310 GLN A O   
4682  C CB  . GLN A 310 ? 1.0855 1.0210 0.8936 -0.0549 -0.1366 0.0679  310 GLN A CB  
4683  C CG  . GLN A 310 ? 1.1876 1.1710 0.9910 -0.0693 -0.1550 0.0755  310 GLN A CG  
4684  C CD  . GLN A 310 ? 1.3388 1.3235 1.0967 -0.0979 -0.1683 0.0565  310 GLN A CD  
4685  O OE1 . GLN A 310 ? 1.4272 1.3811 1.1507 -0.0998 -0.1616 0.0433  310 GLN A OE1 
4686  N NE2 . GLN A 310 ? 1.4035 1.4227 1.1573 -0.1229 -0.1849 0.0540  310 GLN A NE2 
4695  N N   . GLU A 311 ? 0.8809 0.7747 0.7696 -0.0341 -0.1056 0.0722  311 GLU A N   
4696  C CA  . GLU A 311 ? 0.8233 0.7081 0.7392 -0.0390 -0.1050 0.0659  311 GLU A CA  
4697  C C   . GLU A 311 ? 0.7935 0.6691 0.7006 -0.0495 -0.1206 0.0509  311 GLU A C   
4698  O O   . GLU A 311 ? 0.7805 0.6372 0.6678 -0.0485 -0.1200 0.0386  311 GLU A O   
4699  C CB  . GLU A 311 ? 0.7994 0.6744 0.7296 -0.0370 -0.0881 0.0604  311 GLU A CB  
4700  C CG  . GLU A 311 ? 0.7783 0.6529 0.7345 -0.0445 -0.0871 0.0533  311 GLU A CG  
4701  C CD  . GLU A 311 ? 0.8027 0.6838 0.7725 -0.0488 -0.0706 0.0480  311 GLU A CD  
4702  O OE1 . GLU A 311 ? 0.8181 0.6924 0.7881 -0.0528 -0.0526 0.0551  311 GLU A OE1 
4703  O OE2 . GLU A 311 ? 0.7894 0.6846 0.7671 -0.0484 -0.0738 0.0378  311 GLU A OE2 
4710  N N   . VAL A 312 ? 0.7508 0.6357 0.6687 -0.0581 -0.1314 0.0532  312 VAL A N   
4711  C CA  . VAL A 312 ? 0.7547 0.6246 0.6594 -0.0716 -0.1437 0.0406  312 VAL A CA  
4712  C C   . VAL A 312 ? 0.7091 0.5806 0.6408 -0.0746 -0.1457 0.0412  312 VAL A C   
4713  O O   . VAL A 312 ? 0.7319 0.5850 0.6548 -0.0832 -0.1521 0.0322  312 VAL A O   
4714  C CB  . VAL A 312 ? 0.8241 0.7098 0.7028 -0.0891 -0.1578 0.0402  312 VAL A CB  
4715  C CG1 . VAL A 312 ? 0.8343 0.7143 0.6779 -0.0896 -0.1560 0.0355  312 VAL A CG1 
4716  C CG2 . VAL A 312 ? 0.8147 0.7491 0.7156 -0.0877 -0.1629 0.0587  312 VAL A CG2 
4726  N N   . GLY A 313 ? 0.7019 0.5889 0.6608 -0.0676 -0.1375 0.0519  313 GLY A N   
4727  C CA  . GLY A 313 ? 0.6875 0.5771 0.6685 -0.0714 -0.1378 0.0523  313 GLY A CA  
4728  C C   . GLY A 313 ? 0.6790 0.5915 0.6623 -0.0788 -0.1488 0.0602  313 GLY A C   
4729  O O   . GLY A 313 ? 0.6668 0.5977 0.6333 -0.0862 -0.1591 0.0629  313 GLY A O   
4733  N N   . GLN A 314 ? 0.6869 0.6043 0.6905 -0.0790 -0.1460 0.0633  314 GLN A N   
4734  C CA  . GLN A 314 ? 0.6958 0.6445 0.7071 -0.0829 -0.1532 0.0735  314 GLN A CA  
4735  C C   . GLN A 314 ? 0.7314 0.6733 0.7597 -0.0862 -0.1500 0.0703  314 GLN A C   
4736  O O   . GLN A 314 ? 0.7633 0.6852 0.8009 -0.0802 -0.1369 0.0666  314 GLN A O   
4737  C CB  . GLN A 314 ? 0.6952 0.6727 0.7124 -0.0639 -0.1440 0.0942  314 GLN A CB  
4738  C CG  . GLN A 314 ? 0.6850 0.7073 0.7158 -0.0599 -0.1473 0.1094  314 GLN A CG  
4739  C CD  . GLN A 314 ? 0.7042 0.7577 0.7371 -0.0316 -0.1353 0.1351  314 GLN A CD  
4740  O OE1 . GLN A 314 ? 0.7317 0.7611 0.7695 -0.0092 -0.1128 0.1456  314 GLN A OE1 
4741  N NE2 . GLN A 314 ? 0.6897 0.7952 0.7138 -0.0325 -0.1481 0.1457  314 GLN A NE2 
4750  N N   . VAL A 315 ? 0.7365 0.6975 0.7660 -0.0995 -0.1615 0.0708  315 VAL A N   
4751  C CA  . VAL A 315 ? 0.6910 0.6514 0.7347 -0.1031 -0.1591 0.0697  315 VAL A CA  
4752  C C   . VAL A 315 ? 0.7079 0.7139 0.7653 -0.0983 -0.1585 0.0858  315 VAL A C   
4753  O O   . VAL A 315 ? 0.7072 0.7536 0.7601 -0.1060 -0.1693 0.0933  315 VAL A O   
4754  C CB  . VAL A 315 ? 0.7357 0.6759 0.7661 -0.1220 -0.1701 0.0575  315 VAL A CB  
4755  C CG1 . VAL A 315 ? 0.7239 0.6720 0.7675 -0.1269 -0.1688 0.0591  315 VAL A CG1 
4756  C CG2 . VAL A 315 ? 0.7975 0.7006 0.8168 -0.1169 -0.1672 0.0461  315 VAL A CG2 
4766  N N   . SER A 316 ? 0.6853 0.6894 0.7573 -0.0862 -0.1447 0.0911  316 SER A N   
4767  C CA  . SER A 316 ? 0.6473 0.6954 0.7331 -0.0744 -0.1395 0.1087  316 SER A CA  
4768  C C   . SER A 316 ? 0.6122 0.6677 0.7056 -0.0896 -0.1440 0.1034  316 SER A C   
4769  O O   . SER A 316 ? 0.6405 0.6580 0.7316 -0.0955 -0.1395 0.0903  316 SER A O   
4770  C CB  . SER A 316 ? 0.6987 0.7300 0.7872 -0.0438 -0.1133 0.1212  316 SER A CB  
4771  O OG  . SER A 316 ? 0.8023 0.7909 0.8898 -0.0465 -0.0990 0.1092  316 SER A OG  
4777  N N   . VAL A 317 ? 0.5996 0.7117 0.7014 -0.0973 -0.1528 0.1143  317 VAL A N   
4778  C CA  . VAL A 317 ? 0.5498 0.6762 0.6572 -0.1155 -0.1575 0.1112  317 VAL A CA  
4779  C C   . VAL A 317 ? 0.5626 0.7398 0.6900 -0.0931 -0.1442 0.1310  317 VAL A C   
4780  O O   . VAL A 317 ? 0.5985 0.8431 0.7361 -0.0841 -0.1471 0.1493  317 VAL A O   
4781  C CB  . VAL A 317 ? 0.5359 0.6853 0.6308 -0.1517 -0.1774 0.1051  317 VAL A CB  
4782  C CG1 . VAL A 317 ? 0.5743 0.7290 0.6704 -0.1729 -0.1794 0.1019  317 VAL A CG1 
4783  C CG2 . VAL A 317 ? 0.5292 0.6220 0.5975 -0.1658 -0.1853 0.0881  317 VAL A CG2 
4793  N N   . SER A 318 ? 0.5955 0.7453 0.7265 -0.0827 -0.1287 0.1281  318 SER A N   
4794  C CA  . SER A 318 ? 0.6593 0.8420 0.8034 -0.0545 -0.1089 0.1463  318 SER A CA  
4795  C C   . SER A 318 ? 0.6410 0.8465 0.7928 -0.0718 -0.1118 0.1436  318 SER A C   
4796  O O   . SER A 318 ? 0.6224 0.7801 0.7656 -0.0783 -0.1048 0.1295  318 SER A O   
4797  C CB  . SER A 318 ? 0.7185 0.8386 0.8507 -0.0266 -0.0808 0.1444  318 SER A CB  
4798  O OG  . SER A 318 ? 0.8006 0.8878 0.9215 -0.0189 -0.0785 0.1426  318 SER A OG  
4804  N N   . LEU A 319 ? 0.6527 0.9374 0.8195 -0.0816 -0.1219 0.1575  319 LEU A N   
4805  C CA  . LEU A 319 ? 0.6499 0.9650 0.8245 -0.0996 -0.1231 0.1577  319 LEU A CA  
4806  C C   . LEU A 319 ? 0.6667 0.9890 0.8502 -0.0633 -0.0961 0.1703  319 LEU A C   
4807  O O   . LEU A 319 ? 0.6845 1.0516 0.8794 -0.0262 -0.0810 0.1928  319 LEU A O   
4808  C CB  . LEU A 319 ? 0.6138 1.0201 0.8007 -0.1260 -0.1401 0.1685  319 LEU A CB  
4809  C CG  . LEU A 319 ? 0.5950 0.9829 0.7619 -0.1767 -0.1629 0.1509  319 LEU A CG  
4810  C CD1 . LEU A 319 ? 0.6395 0.9509 0.7847 -0.1759 -0.1686 0.1353  319 LEU A CD1 
4811  C CD2 . LEU A 319 ? 0.5480 1.0345 0.7237 -0.2022 -0.1767 0.1619  319 LEU A CD2 
4823  N N   . GLN A 320 ? 0.6312 0.9088 0.8054 -0.0714 -0.0880 0.1569  320 GLN A N   
4824  C CA  . GLN A 320 ? 0.6305 0.9079 0.8062 -0.0412 -0.0601 0.1655  320 GLN A CA  
4825  C C   . GLN A 320 ? 0.6678 1.0407 0.8668 -0.0383 -0.0593 0.1862  320 GLN A C   
4826  O O   . GLN A 320 ? 0.6592 1.0759 0.8663 -0.0762 -0.0800 0.1838  320 GLN A O   
4827  C CB  . GLN A 320 ? 0.5742 0.7833 0.7301 -0.0560 -0.0536 0.1435  320 GLN A CB  
4828  C CG  . GLN A 320 ? 0.5851 0.7878 0.7350 -0.0309 -0.0235 0.1482  320 GLN A CG  
4829  C CD  . GLN A 320 ? 0.5958 0.7373 0.7224 -0.0496 -0.0183 0.1248  320 GLN A CD  
4830  O OE1 . GLN A 320 ? 0.6518 0.7711 0.7640 -0.0330 0.0083  0.1227  320 GLN A OE1 
4831  N NE2 . GLN A 320 ? 0.5668 0.6831 0.6864 -0.0822 -0.0420 0.1082  320 GLN A NE2 
4840  N N   . ARG A 321 ? 0.7296 1.1338 0.9362 0.0070  -0.0323 0.2075  321 ARG A N   
4841  C CA  . ARG A 321 ? 0.7827 1.2890 1.0142 0.0184  -0.0264 0.2309  321 ARG A CA  
4842  C C   . ARG A 321 ? 0.7992 1.2755 1.0202 0.0479  0.0066  0.2327  321 ARG A C   
4843  O O   . ARG A 321 ? 0.8501 1.2363 1.0436 0.0731  0.0318  0.2234  321 ARG A O   
4844  C CB  . ARG A 321 ? 0.8272 1.4245 1.0795 0.0546  -0.0231 0.2627  321 ARG A CB  
4845  C CG  . ARG A 321 ? 0.8938 1.5143 1.1495 0.0274  -0.0531 0.2593  321 ARG A CG  
4846  C CD  . ARG A 321 ? 0.9225 1.6775 1.2052 0.0449  -0.0596 0.2912  321 ARG A CD  
4847  N NE  . ARG A 321 ? 0.9474 1.7249 1.2336 0.1172  -0.0269 0.3230  321 ARG A NE  
4848  C CZ  . ARG A 321 ? 0.9246 1.8274 1.2345 0.1510  -0.0247 0.3590  321 ARG A CZ  
4849  N NH1 . ARG A 321 ? 0.9387 1.8456 1.2444 0.2248  0.0107  0.3901  321 ARG A NH1 
4850  N NH2 . ARG A 321 ? 0.9106 1.9354 1.2445 0.1110  -0.0557 0.3646  321 ARG A NH2 
4864  N N   . ALA A 322 ? 0.8028 1.3542 1.0421 0.0406  0.0080  0.2433  322 ALA A N   
4865  C CA  . ALA A 322 ? 0.8645 1.3906 1.0917 0.0654  0.0395  0.2438  322 ALA A CA  
4866  C C   . ALA A 322 ? 1.0133 1.5127 1.2264 0.1322  0.0802  0.2621  322 ALA A C   
4867  O O   . ALA A 322 ? 1.0373 1.4522 1.2180 0.1511  0.1112  0.2503  322 ALA A O   
4868  C CB  . ALA A 322 ? 0.7902 1.4219 1.0441 0.0521  0.0362  0.2587  322 ALA A CB  
4874  N N   . SER A 323 ? 1.1144 1.6808 1.3457 0.1682  0.0827  0.2910  323 SER A N   
4875  C CA  . SER A 323 ? 1.2182 1.7555 1.4311 0.2386  0.1247  0.3141  323 SER A CA  
4876  C C   . SER A 323 ? 1.3878 1.7786 1.5552 0.2444  0.1429  0.2921  323 SER A C   
4877  O O   . SER A 323 ? 1.6199 1.9586 1.7595 0.2996  0.1833  0.3080  323 SER A O   
4878  C CB  . SER A 323 ? 1.1195 1.7716 1.3622 0.2737  0.1182  0.3524  323 SER A CB  
4879  O OG  . SER A 323 ? 0.9893 1.6480 1.2405 0.2346  0.0808  0.3416  323 SER A OG  
4885  N N   . GLY A 324 ? 1.3556 1.6801 1.5123 0.1890  0.1163  0.2572  324 GLY A N   
4886  C CA  . GLY A 324 ? 1.4489 1.6484 1.5655 0.1845  0.1304  0.2339  324 GLY A CA  
4887  C C   . GLY A 324 ? 1.4628 1.6536 1.5814 0.1876  0.1170  0.2396  324 GLY A C   
4888  O O   . GLY A 324 ? 1.5372 1.6374 1.6292 0.1677  0.1182  0.2161  324 GLY A O   
4892  N N   . ASP A 325 ? 1.3583 1.6478 1.5071 0.2099  0.1043  0.2703  325 ASP A N   
4893  C CA  . ASP A 325 ? 1.3477 1.6377 1.4975 0.2139  0.0909  0.2777  325 ASP A CA  
4894  C C   . ASP A 325 ? 1.1673 1.4536 1.3278 0.1509  0.0469  0.2494  325 ASP A C   
4895  O O   . ASP A 325 ? 1.1141 1.3863 1.2769 0.1085  0.0302  0.2253  325 ASP A O   
4896  C CB  . ASP A 325 ? 1.4390 1.8510 1.6172 0.2537  0.0880  0.3193  325 ASP A CB  
4897  C CG  . ASP A 325 ? 1.5171 1.9265 1.6794 0.3291  0.1366  0.3533  325 ASP A CG  
4898  O OD1 . ASP A 325 ? 1.6338 1.9254 1.7545 0.3485  0.1756  0.3417  325 ASP A OD1 
4899  O OD2 . ASP A 325 ? 1.5576 2.0842 1.7456 0.3692  0.1375  0.3921  325 ASP A OD2 
4904  N N   . PHE A 326 ? 1.0282 1.3245 1.1914 0.1482  0.0304  0.2541  326 PHE A N   
4905  C CA  . PHE A 326 ? 0.8825 1.1832 1.0536 0.0961  -0.0085 0.2324  326 PHE A CA  
4906  C C   . PHE A 326 ? 0.8238 1.2162 1.0139 0.0991  -0.0299 0.2533  326 PHE A C   
4907  O O   . PHE A 326 ? 0.5367 0.9636 0.7274 0.1451  -0.0134 0.2822  326 PHE A O   
4908  C CB  . PHE A 326 ? 0.8201 1.0139 0.9642 0.0801  -0.0058 0.2064  326 PHE A CB  
4909  C CG  . PHE A 326 ? 0.7376 0.8590 0.8647 0.0575  0.0027  0.1789  326 PHE A CG  
4910  C CD1 . PHE A 326 ? 0.7475 0.8030 0.8484 0.0818  0.0406  0.1766  326 PHE A CD1 
4911  C CD2 . PHE A 326 ? 0.6477 0.7655 0.7795 0.0124  -0.0251 0.1560  326 PHE A CD2 
4912  C CE1 . PHE A 326 ? 0.7479 0.7455 0.8302 0.0563  0.0472  0.1497  326 PHE A CE1 
4913  C CE2 . PHE A 326 ? 0.6131 0.6771 0.7291 -0.0065 -0.0186 0.1336  326 PHE A CE2 
4914  C CZ  . PHE A 326 ? 0.6728 0.6818 0.7653 0.0129  0.0159  0.1293  326 PHE A CZ  
4924  N N   . GLN A 327 ? 0.7720 1.2022 0.9727 0.0497  -0.0648 0.2388  327 GLN A N   
4925  C CA  . GLN A 327 ? 0.6996 1.2168 0.9124 0.0368  -0.0890 0.2510  327 GLN A CA  
4926  C C   . GLN A 327 ? 0.6638 1.1169 0.8576 0.0037  -0.1083 0.2262  327 GLN A C   
4927  O O   . GLN A 327 ? 0.6068 1.0259 0.7929 -0.0408 -0.1258 0.2011  327 GLN A O   
4928  C CB  . GLN A 327 ? 0.7144 1.3323 0.9485 0.0015  -0.1088 0.2543  327 GLN A CB  
4929  C CG  . GLN A 327 ? 0.7638 1.4783 1.0055 -0.0253 -0.1351 0.2619  327 GLN A CG  
4930  C CD  . GLN A 327 ? 0.7984 1.6357 1.0636 -0.0515 -0.1461 0.2733  327 GLN A CD  
4931  O OE1 . GLN A 327 ? 0.8200 1.7611 1.1041 -0.0195 -0.1370 0.3027  327 GLN A OE1 
4932  N NE2 . GLN A 327 ? 0.8503 1.6666 1.1074 -0.1092 -0.1607 0.2490  327 GLN A NE2 
4941  N N   . THR A 328 ? 0.6664 1.1007 0.8496 0.0286  -0.1025 0.2350  328 THR A N   
4942  C CA  . THR A 328 ? 0.6409 0.9987 0.8037 0.0087  -0.1116 0.2126  328 THR A CA  
4943  C C   . THR A 328 ? 0.6392 1.0500 0.7988 -0.0138 -0.1368 0.2134  328 THR A C   
4944  O O   . THR A 328 ? 0.6232 1.1241 0.7931 0.0032  -0.1403 0.2383  328 THR A O   
4945  C CB  . THR A 328 ? 0.6409 0.9236 0.7870 0.0469  -0.0837 0.2177  328 THR A CB  
4946  O OG1 . THR A 328 ? 0.6622 0.8892 0.8030 0.0616  -0.0579 0.2130  328 THR A OG1 
4947  C CG2 . THR A 328 ? 0.6020 0.8144 0.7300 0.0242  -0.0925 0.1942  328 THR A CG2 
4955  N N   . THR A 329 ? 0.6618 1.0180 0.8041 -0.0505 -0.1528 0.1866  329 THR A N   
4956  C CA  . THR A 329 ? 0.7584 1.1380 0.8864 -0.0751 -0.1730 0.1806  329 THR A CA  
4957  C C   . THR A 329 ? 0.7535 1.0389 0.8597 -0.0814 -0.1719 0.1589  329 THR A C   
4958  O O   . THR A 329 ? 0.7351 0.9508 0.8387 -0.0821 -0.1633 0.1440  329 THR A O   
4959  C CB  . THR A 329 ? 0.8697 1.2947 0.9929 -0.1264 -0.1952 0.1683  329 THR A CB  
4960  O OG1 . THR A 329 ? 0.9550 1.4791 1.1024 -0.1234 -0.1956 0.1887  329 THR A OG1 
4961  C CG2 . THR A 329 ? 0.9738 1.4196 1.0736 -0.1549 -0.2130 0.1599  329 THR A CG2 
4969  N N   . LYS A 330 ? 0.7863 1.0784 0.8767 -0.0858 -0.1807 0.1579  330 LYS A N   
4970  C CA  . LYS A 330 ? 0.8071 1.0225 0.8774 -0.0888 -0.1788 0.1402  330 LYS A CA  
4971  C C   . LYS A 330 ? 0.8211 1.0223 0.8658 -0.1300 -0.1974 0.1185  330 LYS A C   
4972  O O   . LYS A 330 ? 0.8697 1.1245 0.9075 -0.1590 -0.2119 0.1180  330 LYS A O   
4973  C CB  . LYS A 330 ? 0.8169 1.0355 0.8820 -0.0575 -0.1683 0.1560  330 LYS A CB  
4974  C CG  . LYS A 330 ? 0.8304 1.0639 0.9104 -0.0133 -0.1452 0.1828  330 LYS A CG  
4975  C CD  . LYS A 330 ? 0.8685 1.0176 0.9466 0.0004  -0.1216 0.1738  330 LYS A CD  
4976  C CE  . LYS A 330 ? 0.9544 1.1028 1.0366 0.0424  -0.0930 0.1986  330 LYS A CE  
4977  N NZ  . LYS A 330 ? 1.0486 1.2281 1.1218 0.0779  -0.0826 0.2275  330 LYS A NZ  
4991  N N   . LEU A 331 ? 0.8187 0.9466 0.8459 -0.1330 -0.1945 0.1006  331 LEU A N   
4992  C CA  . LEU A 331 ? 0.7836 0.8739 0.7784 -0.1652 -0.2049 0.0793  331 LEU A CA  
4993  C C   . LEU A 331 ? 0.7761 0.8142 0.7549 -0.1511 -0.1982 0.0706  331 LEU A C   
4994  O O   . LEU A 331 ? 0.7907 0.7857 0.7786 -0.1346 -0.1877 0.0663  331 LEU A O   
4995  C CB  . LEU A 331 ? 0.7805 0.8310 0.7712 -0.1824 -0.2049 0.0671  331 LEU A CB  
4996  C CG  . LEU A 331 ? 0.8149 0.8382 0.7676 -0.2221 -0.2131 0.0507  331 LEU A CG  
4997  C CD1 . LEU A 331 ? 0.8561 0.9516 0.8068 -0.2541 -0.2244 0.0557  331 LEU A CD1 
4998  C CD2 . LEU A 331 ? 0.7704 0.7410 0.7181 -0.2261 -0.2077 0.0433  331 LEU A CD2 
5010  N N   . ASN A 332 ? 0.7718 0.8204 0.7264 -0.1594 -0.2039 0.0679  332 ASN A N   
5011  C CA  . ASN A 332 ? 0.8028 0.8147 0.7447 -0.1425 -0.1960 0.0635  332 ASN A CA  
5012  C C   . ASN A 332 ? 0.8585 0.8049 0.7668 -0.1559 -0.1948 0.0419  332 ASN A C   
5013  O O   . ASN A 332 ? 0.9364 0.8632 0.8169 -0.1840 -0.2009 0.0295  332 ASN A O   
5014  C CB  . ASN A 332 ? 0.8368 0.8941 0.7668 -0.1397 -0.2005 0.0736  332 ASN A CB  
5015  C CG  . ASN A 332 ? 0.8412 0.9514 0.8005 -0.1103 -0.1940 0.1007  332 ASN A CG  
5016  O OD1 . ASN A 332 ? 0.8342 0.9548 0.8204 -0.0983 -0.1880 0.1106  332 ASN A OD1 
5017  N ND2 . ASN A 332 ? 0.9297 1.0693 0.8796 -0.0957 -0.1925 0.1139  332 ASN A ND2 
5024  N N   . GLY A 333 ? 0.8510 0.7623 0.7589 -0.1347 -0.1840 0.0386  333 GLY A N   
5025  C CA  . GLY A 333 ? 0.8674 0.7215 0.7424 -0.1367 -0.1790 0.0224  333 GLY A CA  
5026  C C   . GLY A 333 ? 0.9097 0.7520 0.7388 -0.1560 -0.1827 0.0119  333 GLY A C   
5027  O O   . GLY A 333 ? 0.8919 0.7811 0.7174 -0.1687 -0.1915 0.0176  333 GLY A O   
5031  N N   . PHE A 334 ? 0.9427 0.7217 0.7320 -0.1570 -0.1742 -0.0031 334 PHE A N   
5032  C CA  . PHE A 334 ? 1.0102 0.7587 0.7429 -0.1788 -0.1731 -0.0182 334 PHE A CA  
5033  C C   . PHE A 334 ? 1.0481 0.7689 0.7605 -0.1559 -0.1606 -0.0227 334 PHE A C   
5034  O O   . PHE A 334 ? 1.1070 0.8267 0.7824 -0.1706 -0.1613 -0.0309 334 PHE A O   
5035  C CB  . PHE A 334 ? 1.0784 0.7579 0.7624 -0.2026 -0.1673 -0.0342 334 PHE A CB  
5036  C CG  . PHE A 334 ? 1.0562 0.7583 0.7576 -0.2267 -0.1772 -0.0303 334 PHE A CG  
5037  C CD1 . PHE A 334 ? 1.0597 0.8099 0.7528 -0.2673 -0.1907 -0.0328 334 PHE A CD1 
5038  C CD2 . PHE A 334 ? 0.9868 0.6712 0.7130 -0.2094 -0.1730 -0.0234 334 PHE A CD2 
5039  C CE1 . PHE A 334 ? 1.0695 0.8480 0.7804 -0.2896 -0.1984 -0.0284 334 PHE A CE1 
5040  C CE2 . PHE A 334 ? 0.9853 0.6904 0.7261 -0.2312 -0.1806 -0.0196 334 PHE A CE2 
5041  C CZ  . PHE A 334 ? 1.0306 0.7821 0.7646 -0.2711 -0.1927 -0.0220 334 PHE A CZ  
5051  N N   . GLU A 335 ? 1.0152 0.7211 0.7503 -0.1222 -0.1491 -0.0175 335 GLU A N   
5052  C CA  . GLU A 335 ? 0.9800 0.6679 0.7005 -0.0981 -0.1353 -0.0200 335 GLU A CA  
5053  C C   . GLU A 335 ? 0.9366 0.6767 0.7088 -0.0767 -0.1336 -0.0051 335 GLU A C   
5054  O O   . GLU A 335 ? 0.9244 0.6928 0.7405 -0.0718 -0.1368 0.0046  335 GLU A O   
5055  C CB  . GLU A 335 ? 0.9935 0.6225 0.6893 -0.0756 -0.1187 -0.0262 335 GLU A CB  
5056  C CG  . GLU A 335 ? 1.0963 0.6472 0.7225 -0.0929 -0.1105 -0.0425 335 GLU A CG  
5057  C CD  . GLU A 335 ? 1.2281 0.7198 0.8316 -0.0614 -0.0911 -0.0418 335 GLU A CD  
5058  O OE1 . GLU A 335 ? 1.2506 0.7551 0.8858 -0.0509 -0.0944 -0.0317 335 GLU A OE1 
5059  O OE2 . GLU A 335 ? 1.3406 0.7754 0.8932 -0.0439 -0.0713 -0.0496 335 GLU A OE2 
5066  N N   . VAL A 336 ? 0.9139 0.6610 0.6751 -0.0664 -0.1259 -0.0045 336 VAL A N   
5067  C CA  . VAL A 336 ? 0.8599 0.6473 0.6606 -0.0507 -0.1200 0.0088  336 VAL A CA  
5068  C C   . VAL A 336 ? 0.8156 0.6028 0.6406 -0.0301 -0.1080 0.0094  336 VAL A C   
5069  O O   . VAL A 336 ? 0.8606 0.6195 0.6624 -0.0153 -0.0987 0.0019  336 VAL A O   
5070  C CB  . VAL A 336 ? 0.9059 0.7013 0.6834 -0.0473 -0.1142 0.0104  336 VAL A CB  
5071  C CG1 . VAL A 336 ? 0.8904 0.7200 0.7032 -0.0353 -0.1053 0.0257  336 VAL A CG1 
5072  C CG2 . VAL A 336 ? 0.9626 0.7696 0.7108 -0.0696 -0.1279 0.0092  336 VAL A CG2 
5082  N N   . PHE A 337 ? 0.7646 0.5854 0.6332 -0.0288 -0.1062 0.0188  337 PHE A N   
5083  C CA  . PHE A 337 ? 0.7467 0.5875 0.6432 -0.0168 -0.0964 0.0196  337 PHE A CA  
5084  C C   . PHE A 337 ? 0.7876 0.6171 0.6848 -0.0099 -0.1003 0.0155  337 PHE A C   
5085  O O   . PHE A 337 ? 0.7878 0.6442 0.7054 0.0025  -0.0936 0.0172  337 PHE A O   
5086  C CB  . PHE A 337 ? 0.7192 0.5694 0.6066 -0.0008 -0.0814 0.0187  337 PHE A CB  
5087  C CG  . PHE A 337 ? 0.7034 0.5678 0.5929 -0.0065 -0.0738 0.0252  337 PHE A CG  
5088  C CD1 . PHE A 337 ? 0.6692 0.5528 0.5868 -0.0186 -0.0697 0.0333  337 PHE A CD1 
5089  C CD2 . PHE A 337 ? 0.7382 0.5900 0.5952 0.0008  -0.0679 0.0235  337 PHE A CD2 
5090  C CE1 . PHE A 337 ? 0.6655 0.5523 0.5783 -0.0210 -0.0587 0.0422  337 PHE A CE1 
5091  C CE2 . PHE A 337 ? 0.7311 0.5955 0.5870 -0.0025 -0.0598 0.0321  337 PHE A CE2 
5092  C CZ  . PHE A 337 ? 0.7045 0.5849 0.5881 -0.0123 -0.0547 0.0427  337 PHE A CZ  
5102  N N   . ALA A 338 ? 0.8010 0.5959 0.6747 -0.0188 -0.1102 0.0112  338 ALA A N   
5103  C CA  . ALA A 338 ? 0.7958 0.5726 0.6654 -0.0123 -0.1121 0.0099  338 ALA A CA  
5104  C C   . ALA A 338 ? 0.6939 0.5038 0.6041 -0.0214 -0.1194 0.0151  338 ALA A C   
5105  O O   . ALA A 338 ? 0.6860 0.4935 0.5989 -0.0132 -0.1202 0.0166  338 ALA A O   
5106  C CB  . ALA A 338 ? 0.8635 0.5853 0.6879 -0.0256 -0.1171 0.0023  338 ALA A CB  
5112  N N   . ARG A 339 ? 0.6693 0.5060 0.6059 -0.0358 -0.1221 0.0189  339 ARG A N   
5113  C CA  . ARG A 339 ? 0.6442 0.5057 0.6136 -0.0453 -0.1244 0.0219  339 ARG A CA  
5114  C C   . ARG A 339 ? 0.6718 0.5175 0.6366 -0.0531 -0.1351 0.0216  339 ARG A C   
5115  O O   . ARG A 339 ? 0.6617 0.5211 0.6432 -0.0535 -0.1364 0.0220  339 ARG A O   
5116  C CB  . ARG A 339 ? 0.5607 0.4571 0.5524 -0.0383 -0.1163 0.0210  339 ARG A CB  
5117  C CG  . ARG A 339 ? 0.5619 0.4801 0.5610 -0.0374 -0.1038 0.0213  339 ARG A CG  
5118  C CD  . ARG A 339 ? 0.5888 0.5546 0.6150 -0.0451 -0.0958 0.0191  339 ARG A CD  
5119  N NE  . ARG A 339 ? 0.6311 0.6156 0.6615 -0.0503 -0.0815 0.0189  339 ARG A NE  
5120  C CZ  . ARG A 339 ? 0.6529 0.6879 0.7019 -0.0599 -0.0718 0.0158  339 ARG A CZ  
5121  N NH1 . ARG A 339 ? 0.6761 0.7551 0.7424 -0.0633 -0.0765 0.0132  339 ARG A NH1 
5122  N NH2 . ARG A 339 ? 0.6818 0.7290 0.7310 -0.0681 -0.0571 0.0158  339 ARG A NH2 
5136  N N   . PHE A 340 ? 0.7201 0.5406 0.6598 -0.0627 -0.1425 0.0203  340 PHE A N   
5137  C CA  . PHE A 340 ? 0.7442 0.5554 0.6803 -0.0774 -0.1519 0.0206  340 PHE A CA  
5138  C C   . PHE A 340 ? 0.7007 0.5424 0.6724 -0.0820 -0.1528 0.0263  340 PHE A C   
5139  O O   . PHE A 340 ? 0.6525 0.5148 0.6424 -0.0818 -0.1480 0.0314  340 PHE A O   
5140  C CB  . PHE A 340 ? 0.7968 0.6024 0.7101 -0.0954 -0.1596 0.0195  340 PHE A CB  
5141  C CG  . PHE A 340 ? 0.8183 0.6263 0.7292 -0.1161 -0.1690 0.0202  340 PHE A CG  
5142  C CD1 . PHE A 340 ? 0.8469 0.6118 0.7227 -0.1285 -0.1696 0.0124  340 PHE A CD1 
5143  C CD2 . PHE A 340 ? 0.7885 0.6393 0.7281 -0.1223 -0.1740 0.0298  340 PHE A CD2 
5144  C CE1 . PHE A 340 ? 0.8362 0.6055 0.7084 -0.1525 -0.1769 0.0128  340 PHE A CE1 
5145  C CE2 . PHE A 340 ? 0.7550 0.6182 0.6947 -0.1415 -0.1819 0.0316  340 PHE A CE2 
5146  C CZ  . PHE A 340 ? 0.7645 0.5894 0.6718 -0.1597 -0.1842 0.0224  340 PHE A CZ  
5156  N N   . GLY A 341 ? 0.6874 0.5258 0.6637 -0.0848 -0.1560 0.0258  341 GLY A N   
5157  C CA  . GLY A 341 ? 0.6232 0.4851 0.6270 -0.0901 -0.1551 0.0289  341 GLY A CA  
5158  C C   . GLY A 341 ? 0.6580 0.5392 0.6800 -0.0842 -0.1477 0.0259  341 GLY A C   
5159  O O   . GLY A 341 ? 0.6325 0.5283 0.6720 -0.0920 -0.1433 0.0255  341 GLY A O   
5163  N N   . SER A 342 ? 0.6608 0.5466 0.6770 -0.0716 -0.1446 0.0236  342 SER A N   
5164  C CA  . SER A 342 ? 0.6029 0.5253 0.6375 -0.0702 -0.1394 0.0210  342 SER A CA  
5165  C C   . SER A 342 ? 0.6327 0.5670 0.6713 -0.0723 -0.1449 0.0219  342 SER A C   
5166  O O   . SER A 342 ? 0.6797 0.6483 0.7350 -0.0826 -0.1418 0.0177  342 SER A O   
5167  C CB  . SER A 342 ? 0.6030 0.5412 0.6318 -0.0516 -0.1351 0.0218  342 SER A CB  
5168  O OG  . SER A 342 ? 0.6544 0.5873 0.6807 -0.0516 -0.1282 0.0204  342 SER A OG  
5174  N N   . ALA A 343 ? 0.6797 0.5735 0.6464 -0.0248 -0.0956 0.0843  343 ALA A N   
5175  C CA  . ALA A 343 ? 0.6653 0.5718 0.6277 -0.0325 -0.1008 0.0794  343 ALA A CA  
5176  C C   . ALA A 343 ? 0.6502 0.5564 0.6104 -0.0362 -0.1097 0.0955  343 ALA A C   
5177  O O   . ALA A 343 ? 0.6584 0.5545 0.6106 -0.0347 -0.1226 0.1068  343 ALA A O   
5178  C CB  . ALA A 343 ? 0.6321 0.5425 0.5780 -0.0303 -0.1160 0.0748  343 ALA A CB  
5184  N N   . ILE A 344 ? 0.6444 0.5660 0.6120 -0.0439 -0.1013 0.0937  344 ILE A N   
5185  C CA  . ILE A 344 ? 0.6676 0.5956 0.6394 -0.0493 -0.1052 0.1083  344 ILE A CA  
5186  C C   . ILE A 344 ? 0.7405 0.6837 0.6990 -0.0595 -0.1068 0.1062  344 ILE A C   
5187  O O   . ILE A 344 ? 0.8026 0.7645 0.7643 -0.0650 -0.0911 0.0911  344 ILE A O   
5188  C CB  . ILE A 344 ? 0.6877 0.6250 0.6907 -0.0460 -0.0857 0.1127  344 ILE A CB  
5189  C CG1 . ILE A 344 ? 0.6730 0.6005 0.6882 -0.0338 -0.0830 0.1215  344 ILE A CG1 
5190  C CG2 . ILE A 344 ? 0.6948 0.6473 0.7071 -0.0517 -0.0908 0.1286  344 ILE A CG2 
5191  C CD1 . ILE A 344 ? 0.7091 0.6417 0.7623 -0.0246 -0.0579 0.1289  344 ILE A CD1 
5203  N N   . ALA A 345 ? 0.7254 0.6614 0.6685 -0.0636 -0.1236 0.1210  345 ALA A N   
5204  C CA  . ALA A 345 ? 0.6944 0.6450 0.6208 -0.0714 -0.1268 0.1275  345 ALA A CA  
5205  C C   . ALA A 345 ? 0.6966 0.6523 0.6266 -0.0828 -0.1259 0.1435  345 ALA A C   
5206  O O   . ALA A 345 ? 0.7139 0.6485 0.6440 -0.0862 -0.1378 0.1569  345 ALA A O   
5207  C CB  . ALA A 345 ? 0.6971 0.6319 0.6062 -0.0643 -0.1437 0.1368  345 ALA A CB  
5213  N N   . PRO A 346 ? 0.6850 0.6692 0.6194 -0.0916 -0.1100 0.1398  346 PRO A N   
5214  C CA  . PRO A 346 ? 0.7046 0.6992 0.6392 -0.1044 -0.1084 0.1571  346 PRO A CA  
5215  C C   . PRO A 346 ? 0.8017 0.7813 0.7125 -0.1080 -0.1239 0.1786  346 PRO A C   
5216  O O   . PRO A 346 ? 0.8286 0.8135 0.7189 -0.1023 -0.1300 0.1808  346 PRO A O   
5217  C CB  . PRO A 346 ? 0.6936 0.7250 0.6279 -0.1123 -0.0859 0.1440  346 PRO A CB  
5218  C CG  . PRO A 346 ? 0.6825 0.7141 0.6336 -0.1036 -0.0713 0.1178  346 PRO A CG  
5219  C CD  . PRO A 346 ? 0.6636 0.6709 0.6054 -0.0926 -0.0886 0.1162  346 PRO A CD  
5227  N N   . LEU A 347 ? 0.8293 0.7918 0.7471 -0.1177 -0.1294 0.1959  347 LEU A N   
5228  C CA  . LEU A 347 ? 0.8576 0.7916 0.7611 -0.1208 -0.1400 0.2185  347 LEU A CA  
5229  C C   . LEU A 347 ? 0.8776 0.8265 0.7748 -0.1369 -0.1317 0.2419  347 LEU A C   
5230  O O   . LEU A 347 ? 0.8754 0.7981 0.7635 -0.1397 -0.1365 0.2667  347 LEU A O   
5231  C CB  . LEU A 347 ? 0.8598 0.7528 0.7759 -0.1239 -0.1503 0.2170  347 LEU A CB  
5232  C CG  . LEU A 347 ? 0.8656 0.7398 0.7824 -0.1092 -0.1586 0.1975  347 LEU A CG  
5233  C CD1 . LEU A 347 ? 0.8316 0.6753 0.7569 -0.1192 -0.1665 0.1918  347 LEU A CD1 
5234  C CD2 . LEU A 347 ? 0.8957 0.7564 0.7971 -0.0920 -0.1634 0.2006  347 LEU A CD2 
5246  N N   . GLY A 348 ? 0.8626 0.8513 0.7667 -0.1468 -0.1162 0.2359  348 GLY A N   
5247  C CA  . GLY A 348 ? 0.8495 0.8517 0.7534 -0.1654 -0.1062 0.2575  348 GLY A CA  
5248  C C   . GLY A 348 ? 0.8308 0.8087 0.7622 -0.1790 -0.1104 0.2632  348 GLY A C   
5249  O O   . GLY A 348 ? 0.8221 0.7924 0.7744 -0.1753 -0.1179 0.2461  348 GLY A O   
5253  N N   . ASP A 349 ? 0.8695 0.8388 0.8002 -0.1972 -0.1053 0.2882  349 ASP A N   
5254  C CA  . ASP A 349 ? 0.8479 0.7941 0.8047 -0.2171 -0.1084 0.2919  349 ASP A CA  
5255  C C   . ASP A 349 ? 0.8446 0.7274 0.7912 -0.2151 -0.1187 0.3025  349 ASP A C   
5256  O O   . ASP A 349 ? 0.9099 0.7670 0.8467 -0.2219 -0.1123 0.3314  349 ASP A O   
5257  C CB  . ASP A 349 ? 0.9197 0.8928 0.8891 -0.2417 -0.0917 0.3106  349 ASP A CB  
5258  C CG  . ASP A 349 ? 0.9680 0.9377 0.9737 -0.2666 -0.0940 0.3058  349 ASP A CG  
5259  O OD1 . ASP A 349 ? 0.9737 0.9241 0.9908 -0.2650 -0.1095 0.2865  349 ASP A OD1 
5260  O OD2 . ASP A 349 ? 1.0040 0.9963 1.0264 -0.2900 -0.0800 0.3203  349 ASP A OD2 
5265  N N   . LEU A 350 ? 0.7878 0.6447 0.7384 -0.2047 -0.1320 0.2800  350 LEU A N   
5266  C CA  . LEU A 350 ? 0.8521 0.6470 0.7957 -0.1989 -0.1380 0.2835  350 LEU A CA  
5267  C C   . LEU A 350 ? 0.9565 0.7105 0.9168 -0.2267 -0.1309 0.2940  350 LEU A C   
5268  O O   . LEU A 350 ? 1.0160 0.7211 0.9719 -0.2247 -0.1238 0.3178  350 LEU A O   
5269  C CB  . LEU A 350 ? 0.8402 0.6228 0.7847 -0.1864 -0.1504 0.2525  350 LEU A CB  
5270  C CG  . LEU A 350 ? 0.9307 0.6499 0.8719 -0.1798 -0.1534 0.2467  350 LEU A CG  
5271  C CD1 . LEU A 350 ? 1.0051 0.7042 0.9323 -0.1541 -0.1511 0.2711  350 LEU A CD1 
5272  C CD2 . LEU A 350 ? 0.8890 0.6092 0.8286 -0.1724 -0.1635 0.2134  350 LEU A CD2 
5284  N N   . ASP A 351 ? 0.9308 0.7058 0.9141 -0.2533 -0.1313 0.2778  351 ASP A N   
5285  C CA  . ASP A 351 ? 0.9970 0.7373 1.0003 -0.2869 -0.1237 0.2799  351 ASP A CA  
5286  C C   . ASP A 351 ? 1.0271 0.7937 1.0429 -0.3093 -0.1083 0.3069  351 ASP A C   
5287  O O   . ASP A 351 ? 1.0766 0.8224 1.1146 -0.3427 -0.0995 0.3085  351 ASP A O   
5288  C CB  . ASP A 351 ? 1.0003 0.7561 1.0223 -0.3086 -0.1352 0.2439  351 ASP A CB  
5289  C CG  . ASP A 351 ? 0.9691 0.8066 1.0063 -0.3089 -0.1426 0.2364  351 ASP A CG  
5290  O OD1 . ASP A 351 ? 0.9227 0.7921 0.9492 -0.2815 -0.1422 0.2437  351 ASP A OD1 
5291  O OD2 . ASP A 351 ? 0.9893 0.8609 1.0524 -0.3368 -0.1478 0.2227  351 ASP A OD2 
5296  N N   . GLN A 352 ? 1.0159 0.8287 1.0180 -0.2945 -0.1024 0.3256  352 GLN A N   
5297  C CA  . GLN A 352 ? 1.0315 0.8737 1.0399 -0.3138 -0.0844 0.3527  352 GLN A CA  
5298  C C   . GLN A 352 ? 1.0593 0.9327 1.1070 -0.3489 -0.0803 0.3399  352 GLN A C   
5299  O O   . GLN A 352 ? 1.1244 0.9840 1.1884 -0.3790 -0.0657 0.3576  352 GLN A O   
5300  C CB  . GLN A 352 ? 1.0741 0.8623 1.0688 -0.3177 -0.0715 0.3922  352 GLN A CB  
5301  C CG  . GLN A 352 ? 1.0755 0.8615 1.0330 -0.2840 -0.0744 0.4162  352 GLN A CG  
5302  C CD  . GLN A 352 ? 1.0362 0.8964 0.9723 -0.2771 -0.0684 0.4229  352 GLN A CD  
5303  O OE1 . GLN A 352 ? 1.0696 0.9558 1.0011 -0.2940 -0.0514 0.4495  352 GLN A OE1 
5304  N NE2 . GLN A 352 ? 0.9158 0.8096 0.8388 -0.2545 -0.0794 0.3966  352 GLN A NE2 
5313  N N   . ASP A 353 ? 1.0295 0.9500 1.0956 -0.3450 -0.0928 0.3112  353 ASP A N   
5314  C CA  . ASP A 353 ? 1.0143 0.9839 1.1224 -0.3744 -0.0930 0.2996  353 ASP A CA  
5315  C C   . ASP A 353 ? 0.9328 0.9812 1.0611 -0.3677 -0.0821 0.3048  353 ASP A C   
5316  O O   . ASP A 353 ? 0.9337 1.0365 1.1039 -0.3884 -0.0812 0.2993  353 ASP A O   
5317  C CB  . ASP A 353 ? 1.0691 1.0449 1.1894 -0.3766 -0.1154 0.2677  353 ASP A CB  
5318  C CG  . ASP A 353 ? 1.0628 1.0749 1.1758 -0.3407 -0.1270 0.2562  353 ASP A CG  
5319  O OD1 . ASP A 353 ? 1.0516 1.0636 1.1435 -0.3129 -0.1185 0.2662  353 ASP A OD1 
5320  O OD2 . ASP A 353 ? 1.0494 1.0919 1.1777 -0.3420 -0.1437 0.2372  353 ASP A OD2 
5325  N N   . GLY A 354 ? 0.9085 0.9680 1.0111 -0.3405 -0.0724 0.3133  354 GLY A N   
5326  C CA  . GLY A 354 ? 0.9138 1.0408 1.0347 -0.3326 -0.0559 0.3132  354 GLY A CA  
5327  C C   . GLY A 354 ? 0.8962 1.0503 1.0229 -0.3006 -0.0617 0.2928  354 GLY A C   
5328  O O   . GLY A 354 ? 0.8738 1.0777 1.0195 -0.2907 -0.0435 0.2896  354 GLY A O   
5332  N N   . PHE A 355 ? 0.8821 1.0031 0.9954 -0.2845 -0.0827 0.2787  355 PHE A N   
5333  C CA  . PHE A 355 ? 0.8278 0.9672 0.9466 -0.2545 -0.0864 0.2628  355 PHE A CA  
5334  C C   . PHE A 355 ? 0.8031 0.8915 0.8788 -0.2343 -0.0962 0.2552  355 PHE A C   
5335  O O   . PHE A 355 ? 0.8285 0.8690 0.8837 -0.2404 -0.1108 0.2561  355 PHE A O   
5336  C CB  . PHE A 355 ? 0.8102 0.9799 0.9657 -0.2550 -0.1032 0.2548  355 PHE A CB  
5337  C CG  . PHE A 355 ? 0.7880 1.0218 0.9945 -0.2729 -0.0963 0.2629  355 PHE A CG  
5338  C CD1 . PHE A 355 ? 0.7861 1.0737 1.0283 -0.2566 -0.0758 0.2664  355 PHE A CD1 
5339  C CD2 . PHE A 355 ? 0.7830 1.0247 1.0062 -0.3071 -0.1077 0.2649  355 PHE A CD2 
5340  C CE1 . PHE A 355 ? 0.7851 1.1388 1.0812 -0.2707 -0.0683 0.2755  355 PHE A CE1 
5341  C CE2 . PHE A 355 ? 0.7885 1.0988 1.0636 -0.3258 -0.1021 0.2722  355 PHE A CE2 
5342  C CZ  . PHE A 355 ? 0.7681 1.1374 1.0809 -0.3058 -0.0830 0.2793  355 PHE A CZ  
5352  N N   . ASN A 356 ? 0.7589 0.8584 0.8251 -0.2112 -0.0858 0.2455  356 ASN A N   
5353  C CA  . ASN A 356 ? 0.7584 0.8208 0.7898 -0.1928 -0.0946 0.2363  356 ASN A CA  
5354  C C   . ASN A 356 ? 0.7865 0.8282 0.8238 -0.1834 -0.1145 0.2257  356 ASN A C   
5355  O O   . ASN A 356 ? 0.7875 0.8551 0.8557 -0.1860 -0.1204 0.2240  356 ASN A O   
5356  C CB  . ASN A 356 ? 0.6947 0.7786 0.7200 -0.1759 -0.0766 0.2224  356 ASN A CB  
5357  C CG  . ASN A 356 ? 0.7286 0.8339 0.7332 -0.1867 -0.0579 0.2291  356 ASN A CG  
5358  O OD1 . ASN A 356 ? 0.7510 0.8419 0.7313 -0.1998 -0.0628 0.2492  356 ASN A OD1 
5359  N ND2 . ASN A 356 ? 0.7382 0.8779 0.7525 -0.1815 -0.0338 0.2128  356 ASN A ND2 
5366  N N   . ASP A 357 ? 0.8159 0.8172 0.8230 -0.1722 -0.1249 0.2201  357 ASP A N   
5367  C CA  . ASP A 357 ? 0.8244 0.8015 0.8281 -0.1646 -0.1417 0.2090  357 ASP A CA  
5368  C C   . ASP A 357 ? 0.8370 0.8044 0.8245 -0.1409 -0.1398 0.1971  357 ASP A C   
5369  O O   . ASP A 357 ? 0.8718 0.8540 0.8534 -0.1334 -0.1262 0.1946  357 ASP A O   
5370  C CB  . ASP A 357 ? 0.8770 0.8085 0.8656 -0.1789 -0.1530 0.2121  357 ASP A CB  
5371  C CG  . ASP A 357 ? 0.9527 0.8906 0.9584 -0.2075 -0.1498 0.2238  357 ASP A CG  
5372  O OD1 . ASP A 357 ? 0.9595 0.9385 0.9939 -0.2197 -0.1514 0.2212  357 ASP A OD1 
5373  O OD2 . ASP A 357 ? 1.0099 0.9155 1.0038 -0.2177 -0.1445 0.2384  357 ASP A OD2 
5378  N N   . ILE A 358 ? 0.8286 0.7746 0.8088 -0.1318 -0.1519 0.1869  358 ILE A N   
5379  C CA  . ILE A 358 ? 0.7889 0.7307 0.7608 -0.1115 -0.1483 0.1752  358 ILE A CA  
5380  C C   . ILE A 358 ? 0.7470 0.6581 0.7037 -0.1058 -0.1617 0.1663  358 ILE A C   
5381  O O   . ILE A 358 ? 0.7327 0.6388 0.6915 -0.1163 -0.1724 0.1645  358 ILE A O   
5382  C CB  . ILE A 358 ? 0.7714 0.7459 0.7707 -0.1015 -0.1356 0.1726  358 ILE A CB  
5383  C CG1 . ILE A 358 ? 0.8061 0.7762 0.8005 -0.0862 -0.1225 0.1592  358 ILE A CG1 
5384  C CG2 . ILE A 358 ? 0.7755 0.7610 0.7891 -0.0996 -0.1469 0.1762  358 ILE A CG2 
5385  C CD1 . ILE A 358 ? 0.8342 0.8293 0.8589 -0.0794 -0.0991 0.1558  358 ILE A CD1 
5397  N N   . ALA A 359 ? 0.7265 0.6223 0.6684 -0.0912 -0.1601 0.1581  359 ALA A N   
5398  C CA  . ALA A 359 ? 0.7507 0.6213 0.6803 -0.0828 -0.1680 0.1474  359 ALA A CA  
5399  C C   . ALA A 359 ? 0.7279 0.6125 0.6629 -0.0688 -0.1607 0.1384  359 ALA A C   
5400  O O   . ALA A 359 ? 0.7478 0.6477 0.6902 -0.0628 -0.1484 0.1355  359 ALA A O   
5401  C CB  . ALA A 359 ? 0.7785 0.6215 0.6930 -0.0755 -0.1707 0.1483  359 ALA A CB  
5407  N N   . ILE A 360 ? 0.6957 0.5752 0.6261 -0.0662 -0.1663 0.1328  360 ILE A N   
5408  C CA  . ILE A 360 ? 0.6899 0.5788 0.6248 -0.0534 -0.1580 0.1291  360 ILE A CA  
5409  C C   . ILE A 360 ? 0.7190 0.5861 0.6343 -0.0477 -0.1622 0.1164  360 ILE A C   
5410  O O   . ILE A 360 ? 0.7576 0.6123 0.6586 -0.0554 -0.1722 0.1107  360 ILE A O   
5411  C CB  . ILE A 360 ? 0.6938 0.6104 0.6438 -0.0538 -0.1584 0.1418  360 ILE A CB  
5412  C CG1 . ILE A 360 ? 0.6492 0.5895 0.6270 -0.0557 -0.1495 0.1538  360 ILE A CG1 
5413  C CG2 . ILE A 360 ? 0.7005 0.6211 0.6538 -0.0396 -0.1481 0.1439  360 ILE A CG2 
5414  C CD1 . ILE A 360 ? 0.6383 0.6146 0.6384 -0.0555 -0.1533 0.1721  360 ILE A CD1 
5426  N N   . ALA A 361 ? 0.7058 0.5703 0.6224 -0.0363 -0.1523 0.1087  361 ALA A N   
5427  C CA  . ALA A 361 ? 0.7219 0.5701 0.6253 -0.0289 -0.1529 0.0961  361 ALA A CA  
5428  C C   . ALA A 361 ? 0.7554 0.6118 0.6546 -0.0247 -0.1463 0.0948  361 ALA A C   
5429  O O   . ALA A 361 ? 0.7280 0.6000 0.6417 -0.0213 -0.1354 0.1041  361 ALA A O   
5430  C CB  . ALA A 361 ? 0.7172 0.5679 0.6274 -0.0204 -0.1469 0.0893  361 ALA A CB  
5436  N N   . ALA A 362 ? 0.8249 0.6695 0.7046 -0.0250 -0.1503 0.0840  362 ALA A N   
5437  C CA  . ALA A 362 ? 0.7971 0.6507 0.6658 -0.0206 -0.1425 0.0814  362 ALA A CA  
5438  C C   . ALA A 362 ? 0.7666 0.6051 0.6327 -0.0115 -0.1347 0.0637  362 ALA A C   
5439  O O   . ALA A 362 ? 0.8035 0.6272 0.6527 -0.0125 -0.1364 0.0484  362 ALA A O   
5440  C CB  . ALA A 362 ? 0.7930 0.6571 0.6378 -0.0317 -0.1525 0.0809  362 ALA A CB  
5446  N N   . PRO A 363 ? 0.7650 0.6101 0.6508 -0.0036 -0.1246 0.0628  363 PRO A N   
5447  C CA  . PRO A 363 ? 0.7487 0.5888 0.6413 0.0061  -0.1212 0.0489  363 PRO A CA  
5448  C C   . PRO A 363 ? 0.8079 0.6450 0.6890 0.0113  -0.1114 0.0355  363 PRO A C   
5449  O O   . PRO A 363 ? 0.8302 0.6609 0.7188 0.0216  -0.1088 0.0235  363 PRO A O   
5450  C CB  . PRO A 363 ? 0.7146 0.5764 0.6310 0.0074  -0.1124 0.0493  363 PRO A CB  
5451  C CG  . PRO A 363 ? 0.7308 0.5975 0.6528 -0.0014 -0.1118 0.0612  363 PRO A CG  
5452  C CD  . PRO A 363 ? 0.7529 0.6129 0.6596 -0.0046 -0.1146 0.0723  363 PRO A CD  
5460  N N   . TYR A 364 ? 0.8450 0.6904 0.7095 0.0060  -0.1047 0.0393  364 TYR A N   
5461  C CA  . TYR A 364 ? 0.8686 0.7171 0.7175 0.0088  -0.0926 0.0265  364 TYR A CA  
5462  C C   . TYR A 364 ? 0.8827 0.7278 0.6959 -0.0013 -0.0990 0.0200  364 TYR A C   
5463  O O   . TYR A 364 ? 0.9036 0.7615 0.6943 -0.0036 -0.0887 0.0141  364 TYR A O   
5464  C CB  . TYR A 364 ? 0.8826 0.7507 0.7398 0.0095  -0.0750 0.0371  364 TYR A CB  
5465  C CG  . TYR A 364 ? 0.8695 0.7446 0.7624 0.0124  -0.0676 0.0375  364 TYR A CG  
5466  C CD1 . TYR A 364 ? 0.8446 0.7275 0.7568 0.0195  -0.0635 0.0213  364 TYR A CD1 
5467  C CD2 . TYR A 364 ? 0.8810 0.7593 0.7905 0.0072  -0.0637 0.0523  364 TYR A CD2 
5468  C CE1 . TYR A 364 ? 0.8352 0.7362 0.7781 0.0175  -0.0589 0.0184  364 TYR A CE1 
5469  C CE2 . TYR A 364 ? 0.8844 0.7715 0.8238 0.0043  -0.0551 0.0452  364 TYR A CE2 
5470  C CZ  . TYR A 364 ? 0.8627 0.7648 0.8165 0.0075  -0.0543 0.0274  364 TYR A CZ  
5471  O OH  . TYR A 364 ? 0.8677 0.7899 0.8493 0.0003  -0.0478 0.0173  364 TYR A OH  
5481  N N   . GLY A 365 ? 0.9067 0.7391 0.7133 -0.0103 -0.1151 0.0193  365 GLY A N   
5482  C CA  . GLY A 365 ? 0.9155 0.7487 0.6901 -0.0257 -0.1224 0.0066  365 GLY A CA  
5483  C C   . GLY A 365 ? 0.9770 0.7756 0.7457 -0.0264 -0.1169 -0.0249 365 GLY A C   
5484  O O   . GLY A 365 ? 0.9922 0.7699 0.7833 -0.0101 -0.1072 -0.0322 365 GLY A O   
5488  N N   . GLY A 366 ? 1.0438 0.8391 0.7848 -0.0460 -0.1222 -0.0440 366 GLY A N   
5489  C CA  . GLY A 366 ? 1.1391 0.8934 0.8762 -0.0498 -0.1123 -0.0783 366 GLY A CA  
5490  C C   . GLY A 366 ? 1.2696 1.0226 0.9938 -0.0412 -0.0903 -0.1036 366 GLY A C   
5491  O O   . GLY A 366 ? 1.2733 1.0609 0.9859 -0.0357 -0.0834 -0.0945 366 GLY A O   
5495  N N   . GLU A 367 ? 1.4122 1.1215 1.1420 -0.0397 -0.0757 -0.1356 367 GLU A N   
5496  C CA  . GLU A 367 ? 1.4925 1.1968 1.2131 -0.0318 -0.0502 -0.1663 367 GLU A CA  
5497  C C   . GLU A 367 ? 1.4645 1.1737 1.2231 0.0000  -0.0388 -0.1500 367 GLU A C   
5498  O O   . GLU A 367 ? 1.4096 1.0992 1.2085 0.0185  -0.0438 -0.1319 367 GLU A O   
5499  C CB  . GLU A 367 ? 1.6010 1.2507 1.3238 -0.0387 -0.0334 -0.2075 367 GLU A CB  
5500  C CG  . GLU A 367 ? 1.7037 1.3453 1.3976 -0.0749 -0.0453 -0.2270 367 GLU A CG  
5501  C CD  . GLU A 367 ? 1.8628 1.4427 1.5614 -0.0854 -0.0222 -0.2742 367 GLU A CD  
5502  O OE1 . GLU A 367 ? 1.9281 1.4545 1.6714 -0.0595 -0.0062 -0.2717 367 GLU A OE1 
5503  O OE2 . GLU A 367 ? 1.9688 1.5558 1.6282 -0.1201 -0.0188 -0.3137 367 GLU A OE2 
5510  N N   . ASP A 368 ? 1.4823 1.2242 1.2279 0.0044  -0.0236 -0.1557 368 ASP A N   
5511  C CA  . ASP A 368 ? 1.4949 1.2516 1.2779 0.0300  -0.0107 -0.1447 368 ASP A CA  
5512  C C   . ASP A 368 ? 1.3802 1.1523 1.1943 0.0388  -0.0294 -0.1069 368 ASP A C   
5513  O O   . ASP A 368 ? 1.3723 1.1459 1.2286 0.0594  -0.0275 -0.0979 368 ASP A O   
5514  C CB  . ASP A 368 ? 1.5967 1.3193 1.4147 0.0521  0.0094  -0.1676 368 ASP A CB  
5515  C CG  . ASP A 368 ? 1.7141 1.4251 1.5052 0.0450  0.0367  -0.2113 368 ASP A CG  
5516  O OD1 . ASP A 368 ? 1.7650 1.4605 1.5149 0.0193  0.0345  -0.2348 368 ASP A OD1 
5517  O OD2 . ASP A 368 ? 1.7434 1.4656 1.5554 0.0632  0.0614  -0.2247 368 ASP A OD2 
5522  N N   . LYS A 369 ? 1.3132 1.1019 1.1073 0.0226  -0.0469 -0.0856 369 LYS A N   
5523  C CA  . LYS A 369 ? 1.2224 1.0262 1.0415 0.0267  -0.0605 -0.0548 369 LYS A CA  
5524  C C   . LYS A 369 ? 1.1535 0.9362 1.0069 0.0399  -0.0701 -0.0482 369 LYS A C   
5525  O O   . LYS A 369 ? 1.1393 0.9412 1.0231 0.0507  -0.0724 -0.0339 369 LYS A O   
5526  C CB  . LYS A 369 ? 1.2797 1.1165 1.1151 0.0333  -0.0471 -0.0452 369 LYS A CB  
5527  C CG  . LYS A 369 ? 1.3451 1.2052 1.1488 0.0219  -0.0355 -0.0413 369 LYS A CG  
5528  C CD  . LYS A 369 ? 1.3078 1.1931 1.1350 0.0246  -0.0226 -0.0243 369 LYS A CD  
5529  C CE  . LYS A 369 ? 1.3685 1.2745 1.1793 0.0226  0.0017  -0.0306 369 LYS A CE  
5530  N NZ  . LYS A 369 ? 1.4096 1.3161 1.2369 0.0347  0.0173  -0.0585 369 LYS A NZ  
5544  N N   . LYS A 370 ? 1.1207 0.8661 0.9691 0.0370  -0.0748 -0.0583 370 LYS A N   
5545  C CA  . LYS A 370 ? 1.1303 0.8535 1.0097 0.0506  -0.0823 -0.0455 370 LYS A CA  
5546  C C   . LYS A 370 ? 1.1001 0.8300 0.9796 0.0401  -0.1024 -0.0202 370 LYS A C   
5547  O O   . LYS A 370 ? 1.1051 0.8258 1.0069 0.0502  -0.1096 -0.0037 370 LYS A O   
5548  C CB  . LYS A 370 ? 1.1887 0.8604 1.0693 0.0522  -0.0734 -0.0649 370 LYS A CB  
5549  C CG  . LYS A 370 ? 1.1813 0.8408 1.0791 0.0720  -0.0492 -0.0878 370 LYS A CG  
5550  C CD  . LYS A 370 ? 1.1898 0.7880 1.0996 0.0766  -0.0360 -0.1052 370 LYS A CD  
5551  C CE  . LYS A 370 ? 1.2264 0.8094 1.1494 0.0932  -0.0060 -0.1365 370 LYS A CE  
5552  N NZ  . LYS A 370 ? 1.3162 0.8299 1.2547 0.0968  0.0132  -0.1577 370 LYS A NZ  
5566  N N   . GLY A 371 ? 1.0474 0.7960 0.9043 0.0219  -0.1100 -0.0143 371 GLY A N   
5567  C CA  . GLY A 371 ? 0.9563 0.7160 0.8180 0.0136  -0.1247 0.0082  371 GLY A CA  
5568  C C   . GLY A 371 ? 0.9464 0.6816 0.7969 -0.0024 -0.1352 0.0088  371 GLY A C   
5569  O O   . GLY A 371 ? 0.9854 0.6849 0.8334 -0.0047 -0.1312 -0.0063 371 GLY A O   
5573  N N   . ILE A 372 ? 0.9314 0.6860 0.7796 -0.0147 -0.1459 0.0254  372 ILE A N   
5574  C CA  . ILE A 372 ? 0.9608 0.7032 0.8028 -0.0333 -0.1563 0.0280  372 ILE A CA  
5575  C C   . ILE A 372 ? 0.9216 0.6835 0.7786 -0.0354 -0.1640 0.0523  372 ILE A C   
5576  O O   . ILE A 372 ? 0.8857 0.6758 0.7504 -0.0289 -0.1612 0.0628  372 ILE A O   
5577  C CB  . ILE A 372 ? 0.9726 0.7324 0.7893 -0.0527 -0.1608 0.0160  372 ILE A CB  
5578  C CG1 . ILE A 372 ? 0.9972 0.7326 0.7947 -0.0569 -0.1511 -0.0157 372 ILE A CG1 
5579  C CG2 . ILE A 372 ? 0.9918 0.7581 0.8096 -0.0744 -0.1738 0.0230  372 ILE A CG2 
5580  C CD1 . ILE A 372 ? 1.0563 0.8216 0.8214 -0.0773 -0.1553 -0.0303 372 ILE A CD1 
5592  N N   . VAL A 373 ? 0.9120 0.6565 0.7745 -0.0460 -0.1701 0.0594  373 VAL A N   
5593  C CA  . VAL A 373 ? 0.9033 0.6674 0.7777 -0.0517 -0.1753 0.0800  373 VAL A CA  
5594  C C   . VAL A 373 ? 0.8919 0.6575 0.7638 -0.0752 -0.1831 0.0802  373 VAL A C   
5595  O O   . VAL A 373 ? 0.8622 0.5962 0.7285 -0.0879 -0.1835 0.0673  373 VAL A O   
5596  C CB  . VAL A 373 ? 0.9346 0.6855 0.8205 -0.0419 -0.1740 0.0944  373 VAL A CB  
5597  C CG1 . VAL A 373 ? 0.9505 0.7209 0.8435 -0.0528 -0.1771 0.1128  373 VAL A CG1 
5598  C CG2 . VAL A 373 ? 0.8872 0.6549 0.7791 -0.0221 -0.1690 0.0943  373 VAL A CG2 
5608  N N   . TYR A 374 ? 0.8940 0.6972 0.7745 -0.0817 -0.1870 0.0934  374 TYR A N   
5609  C CA  . TYR A 374 ? 0.8905 0.7119 0.7751 -0.1042 -0.1958 0.0959  374 TYR A CA  
5610  C C   . TYR A 374 ? 0.8773 0.7065 0.7808 -0.1098 -0.1943 0.1142  374 TYR A C   
5611  O O   . TYR A 374 ? 0.8292 0.6763 0.7433 -0.0970 -0.1876 0.1266  374 TYR A O   
5612  C CB  . TYR A 374 ? 0.8824 0.7519 0.7677 -0.1049 -0.2012 0.1014  374 TYR A CB  
5613  C CG  . TYR A 374 ? 0.8486 0.7196 0.7097 -0.1029 -0.2025 0.0857  374 TYR A CG  
5614  C CD1 . TYR A 374 ? 0.8383 0.7111 0.6800 -0.1249 -0.2109 0.0655  374 TYR A CD1 
5615  C CD2 . TYR A 374 ? 0.8252 0.6983 0.6821 -0.0822 -0.1931 0.0887  374 TYR A CD2 
5616  C CE1 . TYR A 374 ? 0.8951 0.7746 0.7095 -0.1251 -0.2101 0.0487  374 TYR A CE1 
5617  C CE2 . TYR A 374 ? 0.8458 0.7236 0.6787 -0.0812 -0.1917 0.0760  374 TYR A CE2 
5618  C CZ  . TYR A 374 ? 0.8948 0.7772 0.7043 -0.1020 -0.2003 0.0561  374 TYR A CZ  
5619  O OH  . TYR A 374 ? 0.9279 0.8201 0.7085 -0.1030 -0.1972 0.0411  374 TYR A OH  
5629  N N   . ILE A 375 ? 0.9097 0.7257 0.8173 -0.1317 -0.1979 0.1135  375 ILE A N   
5630  C CA  . ILE A 375 ? 0.8562 0.6814 0.7806 -0.1412 -0.1949 0.1316  375 ILE A CA  
5631  C C   . ILE A 375 ? 0.8408 0.7155 0.7830 -0.1586 -0.2016 0.1361  375 ILE A C   
5632  O O   . ILE A 375 ? 0.9017 0.7854 0.8417 -0.1793 -0.2112 0.1230  375 ILE A O   
5633  C CB  . ILE A 375 ? 0.9083 0.6851 0.8314 -0.1545 -0.1909 0.1330  375 ILE A CB  
5634  C CG1 . ILE A 375 ? 0.9130 0.6465 0.8246 -0.1324 -0.1850 0.1328  375 ILE A CG1 
5635  C CG2 . ILE A 375 ? 0.9435 0.7335 0.8811 -0.1650 -0.1855 0.1556  375 ILE A CG2 
5636  C CD1 . ILE A 375 ? 0.8818 0.6361 0.7925 -0.1097 -0.1815 0.1492  375 ILE A CD1 
5648  N N   . PHE A 376 ? 0.7829 0.6942 0.7448 -0.1510 -0.1956 0.1530  376 PHE A N   
5649  C CA  . PHE A 376 ? 0.7591 0.7248 0.7480 -0.1622 -0.1995 0.1628  376 PHE A CA  
5650  C C   . PHE A 376 ? 0.7669 0.7406 0.7742 -0.1746 -0.1902 0.1757  376 PHE A C   
5651  O O   . PHE A 376 ? 0.7777 0.7448 0.7840 -0.1619 -0.1767 0.1836  376 PHE A O   
5652  C CB  . PHE A 376 ? 0.7418 0.7458 0.7465 -0.1389 -0.1948 0.1730  376 PHE A CB  
5653  C CG  . PHE A 376 ? 0.7748 0.7816 0.7631 -0.1292 -0.2034 0.1664  376 PHE A CG  
5654  C CD1 . PHE A 376 ? 0.8089 0.7788 0.7747 -0.1124 -0.1972 0.1566  376 PHE A CD1 
5655  C CD2 . PHE A 376 ? 0.7569 0.8110 0.7521 -0.1380 -0.2177 0.1713  376 PHE A CD2 
5656  C CE1 . PHE A 376 ? 0.8027 0.7771 0.7521 -0.1047 -0.2022 0.1516  376 PHE A CE1 
5657  C CE2 . PHE A 376 ? 0.7587 0.8211 0.7334 -0.1301 -0.2248 0.1679  376 PHE A CE2 
5658  C CZ  . PHE A 376 ? 0.7849 0.8045 0.7362 -0.1135 -0.2156 0.1579  376 PHE A CZ  
5668  N N   . ASN A 377 ? 0.7491 0.7415 0.7721 -0.2023 -0.1964 0.1761  377 ASN A N   
5669  C CA  . ASN A 377 ? 0.8029 0.8077 0.8458 -0.2178 -0.1859 0.1897  377 ASN A CA  
5670  C C   . ASN A 377 ? 0.7995 0.8725 0.8801 -0.2120 -0.1809 0.2027  377 ASN A C   
5671  O O   . ASN A 377 ? 0.8110 0.9288 0.9095 -0.2081 -0.1920 0.2035  377 ASN A O   
5672  C CB  . ASN A 377 ? 0.8598 0.8490 0.9071 -0.2541 -0.1910 0.1831  377 ASN A CB  
5673  C CG  . ASN A 377 ? 0.8930 0.8075 0.9111 -0.2580 -0.1903 0.1712  377 ASN A CG  
5674  O OD1 . ASN A 377 ? 0.8877 0.7844 0.8917 -0.2624 -0.2000 0.1498  377 ASN A OD1 
5675  N ND2 . ASN A 377 ? 0.8864 0.7597 0.8965 -0.2551 -0.1771 0.1866  377 ASN A ND2 
5682  N N   . GLY A 378 ? 0.7871 0.8711 0.8806 -0.2101 -0.1629 0.2145  378 GLY A N   
5683  C CA  . GLY A 378 ? 0.7642 0.9095 0.8994 -0.2028 -0.1518 0.2257  378 GLY A CA  
5684  C C   . GLY A 378 ? 0.8007 0.9918 0.9706 -0.2315 -0.1550 0.2332  378 GLY A C   
5685  O O   . GLY A 378 ? 0.7910 0.9595 0.9508 -0.2612 -0.1612 0.2292  378 GLY A O   
5689  N N   . ARG A 379 ? 0.8171 1.0741 1.0337 -0.2222 -0.1483 0.2446  379 ARG A N   
5690  C CA  . ARG A 379 ? 0.8580 1.1750 1.1180 -0.2474 -0.1491 0.2535  379 ARG A CA  
5691  C C   . ARG A 379 ? 0.7913 1.1697 1.1034 -0.2241 -0.1295 0.2683  379 ARG A C   
5692  O O   . ARG A 379 ? 0.7632 1.1336 1.0779 -0.1903 -0.1172 0.2698  379 ARG A O   
5693  C CB  . ARG A 379 ? 0.9288 1.2799 1.1981 -0.2698 -0.1779 0.2482  379 ARG A CB  
5694  C CG  . ARG A 379 ? 0.9575 1.3318 1.2249 -0.2449 -0.1952 0.2504  379 ARG A CG  
5695  C CD  . ARG A 379 ? 1.0269 1.4399 1.2930 -0.2741 -0.2246 0.2407  379 ARG A CD  
5696  N NE  . ARG A 379 ? 1.1036 1.5619 1.3731 -0.2514 -0.2418 0.2510  379 ARG A NE  
5697  C CZ  . ARG A 379 ? 1.1641 1.6784 1.4327 -0.2722 -0.2691 0.2460  379 ARG A CZ  
5698  N NH1 . ARG A 379 ? 1.2149 1.7434 1.4824 -0.3192 -0.2811 0.2249  379 ARG A NH1 
5699  N NH2 . ARG A 379 ? 1.1711 1.7295 1.4396 -0.2481 -0.2831 0.2621  379 ARG A NH2 
5713  N N   . SER A 380 ? 0.7645 1.2033 1.1226 -0.2433 -0.1235 0.2780  380 SER A N   
5714  C CA  . SER A 380 ? 0.7076 1.2019 1.1200 -0.2221 -0.0975 0.2909  380 SER A CA  
5715  C C   . SER A 380 ? 0.7360 1.2670 1.1845 -0.1836 -0.1000 0.3035  380 SER A C   
5716  O O   . SER A 380 ? 0.7595 1.2981 1.2376 -0.1533 -0.0711 0.3081  380 SER A O   
5717  C CB  . SER A 380 ? 0.6384 1.2034 1.1016 -0.2507 -0.0945 0.3007  380 SER A CB  
5718  O OG  . SER A 380 ? 0.6165 1.2327 1.1014 -0.2701 -0.1266 0.3044  380 SER A OG  
5724  N N   . THR A 381 ? 0.7475 1.3013 1.1943 -0.1844 -0.1317 0.3094  381 THR A N   
5725  C CA  . THR A 381 ? 0.7634 1.3580 1.2462 -0.1469 -0.1347 0.3304  381 THR A CA  
5726  C C   . THR A 381 ? 0.7605 1.2835 1.2081 -0.1157 -0.1215 0.3235  381 THR A C   
5727  O O   . THR A 381 ? 0.7857 1.3213 1.2712 -0.0789 -0.1024 0.3394  381 THR A O   
5728  C CB  . THR A 381 ? 0.7775 1.4285 1.2629 -0.1601 -0.1739 0.3404  381 THR A CB  
5729  O OG1 . THR A 381 ? 0.8291 1.4152 1.2442 -0.1757 -0.1936 0.3187  381 THR A OG1 
5730  C CG2 . THR A 381 ? 0.7490 1.4733 1.2685 -0.1990 -0.1882 0.3411  381 THR A CG2 
5738  N N   . GLY A 382 ? 0.7456 1.1940 1.1264 -0.1298 -0.1291 0.3007  382 GLY A N   
5739  C CA  . GLY A 382 ? 0.7056 1.0902 1.0523 -0.1058 -0.1182 0.2911  382 GLY A CA  
5740  C C   . GLY A 382 ? 0.6972 1.0176 0.9764 -0.1252 -0.1355 0.2697  382 GLY A C   
5741  O O   . GLY A 382 ? 0.7592 1.0509 1.0126 -0.1492 -0.1338 0.2572  382 GLY A O   
5745  N N   . LEU A 383 ? 0.6723 0.9705 0.9249 -0.1137 -0.1500 0.2682  383 LEU A N   
5746  C CA  . LEU A 383 ? 0.7531 0.9968 0.9484 -0.1294 -0.1666 0.2485  383 LEU A CA  
5747  C C   . LEU A 383 ? 0.8337 1.1105 1.0216 -0.1484 -0.1963 0.2490  383 LEU A C   
5748  O O   . LEU A 383 ? 0.8268 1.1559 1.0364 -0.1353 -0.2065 0.2668  383 LEU A O   
5749  C CB  . LEU A 383 ? 0.7549 0.9496 0.9225 -0.1055 -0.1580 0.2408  383 LEU A CB  
5750  C CG  . LEU A 383 ? 0.7869 0.9247 0.9005 -0.1168 -0.1705 0.2203  383 LEU A CG  
5751  C CD1 . LEU A 383 ? 0.8079 0.9084 0.9019 -0.1319 -0.1627 0.2094  383 LEU A CD1 
5752  C CD2 . LEU A 383 ? 0.8120 0.9184 0.9075 -0.0935 -0.1635 0.2155  383 LEU A CD2 
5764  N N   . ASN A 384 ? 0.9129 1.1614 1.0711 -0.1798 -0.2086 0.2300  384 ASN A N   
5765  C CA  . ASN A 384 ? 0.9739 1.2448 1.1161 -0.2030 -0.2341 0.2193  384 ASN A CA  
5766  C C   . ASN A 384 ? 1.0265 1.2771 1.1349 -0.1838 -0.2412 0.2148  384 ASN A C   
5767  O O   . ASN A 384 ? 1.1258 1.3095 1.2004 -0.1741 -0.2324 0.2009  384 ASN A O   
5768  C CB  . ASN A 384 ? 0.9798 1.2055 1.0981 -0.2396 -0.2378 0.1953  384 ASN A CB  
5769  C CG  . ASN A 384 ? 0.9859 1.2379 1.0909 -0.2716 -0.2606 0.1758  384 ASN A CG  
5770  O OD1 . ASN A 384 ? 0.9725 1.2854 1.0811 -0.2666 -0.2771 0.1825  384 ASN A OD1 
5771  N ND2 . ASN A 384 ? 1.0015 1.2092 1.0914 -0.3059 -0.2599 0.1519  384 ASN A ND2 
5778  N N   . ALA A 385 ? 0.9883 1.3033 1.1073 -0.1780 -0.2569 0.2295  385 ALA A N   
5779  C CA  . ALA A 385 ? 0.9587 1.2644 1.0504 -0.1561 -0.2599 0.2336  385 ALA A CA  
5780  C C   . ALA A 385 ? 0.9529 1.2183 0.9903 -0.1767 -0.2710 0.2013  385 ALA A C   
5781  O O   . ALA A 385 ? 0.9577 1.2084 0.9675 -0.1603 -0.2703 0.2011  385 ALA A O   
5782  C CB  . ALA A 385 ? 0.9784 1.3727 1.0973 -0.1430 -0.2736 0.2662  385 ALA A CB  
5788  N N   . VAL A 386 ? 0.9582 1.2032 0.9827 -0.2118 -0.2775 0.1740  386 VAL A N   
5789  C CA  . VAL A 386 ? 0.9866 1.1875 0.9653 -0.2327 -0.2828 0.1385  386 VAL A CA  
5790  C C   . VAL A 386 ? 0.9666 1.0761 0.9330 -0.2298 -0.2645 0.1231  386 VAL A C   
5791  O O   . VAL A 386 ? 0.9601 1.0534 0.9479 -0.2410 -0.2571 0.1269  386 VAL A O   
5792  C CB  . VAL A 386 ? 1.0488 1.2914 1.0242 -0.2781 -0.3009 0.1151  386 VAL A CB  
5793  C CG1 . VAL A 386 ? 1.0977 1.2936 1.0259 -0.2986 -0.3015 0.0736  386 VAL A CG1 
5794  C CG2 . VAL A 386 ? 1.0600 1.4124 1.0548 -0.2807 -0.3223 0.1378  386 VAL A CG2 
5804  N N   . PRO A 387 ? 0.9598 1.0142 0.8943 -0.2147 -0.2567 0.1087  387 PRO A N   
5805  C CA  . PRO A 387 ? 0.9553 0.9320 0.8823 -0.2092 -0.2412 0.0992  387 PRO A CA  
5806  C C   . PRO A 387 ? 0.9810 0.9207 0.9039 -0.2432 -0.2408 0.0751  387 PRO A C   
5807  O O   . PRO A 387 ? 0.9940 0.9395 0.8997 -0.2679 -0.2483 0.0476  387 PRO A O   
5808  C CB  . PRO A 387 ? 0.9725 0.9156 0.8713 -0.1861 -0.2351 0.0889  387 PRO A CB  
5809  C CG  . PRO A 387 ? 1.0128 1.0012 0.8920 -0.1951 -0.2477 0.0790  387 PRO A CG  
5810  C CD  . PRO A 387 ? 0.9734 1.0388 0.8789 -0.2016 -0.2607 0.1030  387 PRO A CD  
5818  N N   . SER A 388 ? 0.9696 0.8711 0.9081 -0.2461 -0.2296 0.0851  388 SER A N   
5819  C CA  . SER A 388 ? 1.0000 0.8535 0.9407 -0.2765 -0.2231 0.0678  388 SER A CA  
5820  C C   . SER A 388 ? 0.9849 0.7584 0.9059 -0.2653 -0.2101 0.0515  388 SER A C   
5821  O O   . SER A 388 ? 0.9777 0.6985 0.9027 -0.2879 -0.1999 0.0357  388 SER A O   
5822  C CB  . SER A 388 ? 1.0489 0.8983 1.0161 -0.2842 -0.2144 0.0923  388 SER A CB  
5823  O OG  . SER A 388 ? 1.0606 0.8797 1.0237 -0.2526 -0.2033 0.1148  388 SER A OG  
5829  N N   . GLN A 389 ? 0.9770 0.7400 0.8823 -0.2313 -0.2077 0.0553  389 GLN A N   
5830  C CA  . GLN A 389 ? 0.9879 0.6833 0.8817 -0.2159 -0.1946 0.0431  389 GLN A CA  
5831  C C   . GLN A 389 ? 1.0024 0.7121 0.8794 -0.1849 -0.1959 0.0416  389 GLN A C   
5832  O O   . GLN A 389 ? 0.9708 0.7284 0.8496 -0.1700 -0.2026 0.0592  389 GLN A O   
5833  C CB  . GLN A 389 ? 0.9592 0.6092 0.8682 -0.2032 -0.1826 0.0692  389 GLN A CB  
5834  C CG  . GLN A 389 ? 1.0030 0.5801 0.9113 -0.1908 -0.1674 0.0600  389 GLN A CG  
5835  C CD  . GLN A 389 ? 1.0303 0.5663 0.9563 -0.1828 -0.1562 0.0923  389 GLN A CD  
5836  O OE1 . GLN A 389 ? 1.0584 0.6247 0.9910 -0.1845 -0.1601 0.1211  389 GLN A OE1 
5837  N NE2 . GLN A 389 ? 1.0510 0.5187 0.9856 -0.1730 -0.1401 0.0895  389 GLN A NE2 
5846  N N   . ILE A 390 ? 1.0589 0.7240 0.9236 -0.1758 -0.1858 0.0198  390 ILE A N   
5847  C CA  . ILE A 390 ? 1.0004 0.6753 0.8506 -0.1493 -0.1835 0.0147  390 ILE A CA  
5848  C C   . ILE A 390 ? 0.9733 0.5916 0.8316 -0.1259 -0.1684 0.0140  390 ILE A C   
5849  O O   . ILE A 390 ? 0.9982 0.5645 0.8583 -0.1343 -0.1560 -0.0078 390 ILE A O   
5850  C CB  . ILE A 390 ? 1.0181 0.7154 0.8420 -0.1642 -0.1866 -0.0165 390 ILE A CB  
5851  C CG1 . ILE A 390 ? 0.9802 0.7483 0.7999 -0.1811 -0.2043 -0.0064 390 ILE A CG1 
5852  C CG2 . ILE A 390 ? 1.0258 0.7241 0.8360 -0.1374 -0.1788 -0.0223 390 ILE A CG2 
5853  C CD1 . ILE A 390 ? 1.0075 0.8091 0.7984 -0.2043 -0.2112 -0.0351 390 ILE A CD1 
5865  N N   . LEU A 391 ? 0.9387 0.5692 0.8051 -0.0970 -0.1680 0.0369  391 LEU A N   
5866  C CA  . LEU A 391 ? 0.9576 0.5525 0.8362 -0.0702 -0.1568 0.0422  391 LEU A CA  
5867  C C   . LEU A 391 ? 0.9959 0.6043 0.8647 -0.0533 -0.1515 0.0236  391 LEU A C   
5868  O O   . LEU A 391 ? 0.9774 0.6314 0.8364 -0.0506 -0.1577 0.0264  391 LEU A O   
5869  C CB  . LEU A 391 ? 0.9493 0.5614 0.8424 -0.0527 -0.1610 0.0777  391 LEU A CB  
5870  C CG  . LEU A 391 ? 1.0304 0.6257 0.9336 -0.0657 -0.1620 0.1015  391 LEU A CG  
5871  C CD1 . LEU A 391 ? 1.0829 0.7030 0.9804 -0.0961 -0.1697 0.0975  391 LEU A CD1 
5872  C CD2 . LEU A 391 ? 1.0441 0.6655 0.9545 -0.0473 -0.1655 0.1347  391 LEU A CD2 
5884  N N   . GLU A 392 ? 1.0030 0.5700 0.8775 -0.0420 -0.1366 0.0053  392 GLU A N   
5885  C CA  . GLU A 392 ? 0.9902 0.5674 0.8562 -0.0284 -0.1271 -0.0165 392 GLU A CA  
5886  C C   . GLU A 392 ? 0.9715 0.5392 0.8650 0.0060  -0.1180 -0.0028 392 GLU A C   
5887  O O   . GLU A 392 ? 0.9950 0.5185 0.9118 0.0182  -0.1085 0.0052  392 GLU A O   
5888  C CB  . GLU A 392 ? 1.0968 0.6416 0.9458 -0.0463 -0.1138 -0.0577 392 GLU A CB  
5889  C CG  . GLU A 392 ? 1.1667 0.7407 0.9852 -0.0816 -0.1255 -0.0741 392 GLU A CG  
5890  C CD  . GLU A 392 ? 1.2726 0.8139 1.0740 -0.1070 -0.1124 -0.1194 392 GLU A CD  
5891  O OE1 . GLU A 392 ? 1.3256 0.8034 1.1473 -0.1072 -0.0958 -0.1318 392 GLU A OE1 
5892  O OE2 . GLU A 392 ? 1.2931 0.8729 1.0610 -0.1273 -0.1170 -0.1424 392 GLU A OE2 
5899  N N   . GLY A 393 ? 0.9431 0.5549 0.8378 0.0213  -0.1199 0.0020  393 GLY A N   
5900  C CA  . GLY A 393 ? 0.9579 0.5746 0.8810 0.0521  -0.1118 0.0108  393 GLY A CA  
5901  C C   . GLY A 393 ? 1.0592 0.6343 0.9929 0.0642  -0.0902 -0.0150 393 GLY A C   
5902  O O   . GLY A 393 ? 1.0736 0.6344 0.9833 0.0477  -0.0800 -0.0485 393 GLY A O   
5906  N N   . GLN A 394 ? 1.1391 0.6987 1.1102 0.0939  -0.0818 0.0011  394 GLN A N   
5907  C CA  . GLN A 394 ? 1.2556 0.7668 1.2479 0.1104  -0.0563 -0.0206 394 GLN A CA  
5908  C C   . GLN A 394 ? 1.2299 0.7735 1.2498 0.1409  -0.0442 -0.0243 394 GLN A C   
5909  O O   . GLN A 394 ? 1.2807 0.7885 1.3207 0.1566  -0.0186 -0.0465 394 GLN A O   
5910  C CB  . GLN A 394 ? 1.3863 0.8418 1.4109 0.1247  -0.0494 0.0038  394 GLN A CB  
5911  C CG  . GLN A 394 ? 1.5000 0.9167 1.5037 0.0924  -0.0559 0.0044  394 GLN A CG  
5912  C CD  . GLN A 394 ? 1.6418 1.0208 1.6175 0.0604  -0.0418 -0.0460 394 GLN A CD  
5913  O OE1 . GLN A 394 ? 1.7524 1.1158 1.7284 0.0663  -0.0207 -0.0818 394 GLN A OE1 
5914  N NE2 . GLN A 394 ? 1.6841 1.0553 1.6354 0.0248  -0.0531 -0.0506 394 GLN A NE2 
5923  N N   . TRP A 395 ? 1.1513 0.7616 1.1758 0.1479  -0.0588 -0.0063 395 TRP A N   
5924  C CA  . TRP A 395 ? 1.1298 0.7809 1.1880 0.1755  -0.0490 -0.0063 395 TRP A CA  
5925  C C   . TRP A 395 ? 1.1043 0.7975 1.1388 0.1604  -0.0449 -0.0305 395 TRP A C   
5926  O O   . TRP A 395 ? 1.0857 0.7979 1.0858 0.1345  -0.0579 -0.0308 395 TRP A O   
5927  C CB  . TRP A 395 ? 1.1063 0.8090 1.1979 0.1960  -0.0674 0.0349  395 TRP A CB  
5928  C CG  . TRP A 395 ? 1.1833 0.8483 1.2971 0.2127  -0.0704 0.0665  395 TRP A CG  
5929  C CD1 . TRP A 395 ? 1.2253 0.8676 1.3868 0.2488  -0.0558 0.0832  395 TRP A CD1 
5930  C CD2 . TRP A 395 ? 1.1973 0.8398 1.2897 0.1949  -0.0860 0.0886  395 TRP A CD2 
5931  N NE1 . TRP A 395 ? 1.3067 0.9107 1.4768 0.2546  -0.0613 0.1177  395 TRP A NE1 
5932  C CE2 . TRP A 395 ? 1.2514 0.8563 1.3776 0.2201  -0.0799 0.1203  395 TRP A CE2 
5933  C CE3 . TRP A 395 ? 1.1540 0.8057 1.2056 0.1614  -0.1022 0.0867  395 TRP A CE3 
5934  C CZ2 . TRP A 395 ? 1.2314 0.8080 1.3480 0.2098  -0.0895 0.1499  395 TRP A CZ2 
5935  C CZ3 . TRP A 395 ? 1.1874 0.8149 1.2314 0.1519  -0.1120 0.1128  395 TRP A CZ3 
5936  C CH2 . TRP A 395 ? 1.2378 0.8282 1.3121 0.1744  -0.1056 0.1439  395 TRP A CH2 
5947  N N   . ALA A 396 ? 1.1189 0.8262 1.1765 0.1787  -0.0239 -0.0482 396 ALA A N   
5948  C CA  . ALA A 396 ? 1.1047 0.8532 1.1472 0.1683  -0.0141 -0.0681 396 ALA A CA  
5949  C C   . ALA A 396 ? 1.1124 0.9240 1.2019 0.1902  -0.0138 -0.0537 396 ALA A C   
5950  O O   . ALA A 396 ? 1.1315 0.9522 1.2678 0.2196  -0.0148 -0.0351 396 ALA A O   
5951  C CB  . ALA A 396 ? 1.1479 0.8646 1.1725 0.1653  0.0147  -0.1077 396 ALA A CB  
5957  N N   . ALA A 397 ? 1.1481 1.0067 1.2277 0.1751  -0.0121 -0.0603 397 ALA A N   
5958  C CA  . ALA A 397 ? 1.1935 1.1206 1.3164 0.1866  -0.0125 -0.0509 397 ALA A CA  
5959  C C   . ALA A 397 ? 1.2724 1.2246 1.3949 0.1811  0.0131  -0.0752 397 ALA A C   
5960  O O   . ALA A 397 ? 1.2797 1.1993 1.3624 0.1678  0.0292  -0.0965 397 ALA A O   
5961  C CB  . ALA A 397 ? 1.1451 1.1113 1.2632 0.1678  -0.0363 -0.0317 397 ALA A CB  
5967  N N   . ARG A 398 ? 1.3449 1.3623 1.5116 0.1890  0.0170  -0.0715 398 ARG A N   
5968  C CA  . ARG A 398 ? 1.4293 1.4777 1.6058 0.1856  0.0443  -0.0919 398 ARG A CA  
5969  C C   . ARG A 398 ? 1.4667 1.5712 1.6526 0.1620  0.0426  -0.0882 398 ARG A C   
5970  O O   . ARG A 398 ? 1.5610 1.6983 1.7617 0.1573  0.0664  -0.1018 398 ARG A O   
5971  C CB  . ARG A 398 ? 1.4816 1.5577 1.7170 0.2204  0.0618  -0.0975 398 ARG A CB  
5972  C CG  . ARG A 398 ? 1.5850 1.5993 1.8227 0.2464  0.0717  -0.1039 398 ARG A CG  
5973  C CD  . ARG A 398 ? 1.6440 1.6867 1.9481 0.2842  0.0952  -0.1091 398 ARG A CD  
5974  N NE  . ARG A 398 ? 1.7113 1.6863 2.0087 0.3005  0.1234  -0.1339 398 ARG A NE  
5975  C CZ  . ARG A 398 ? 1.7761 1.7598 2.1148 0.3264  0.1580  -0.1544 398 ARG A CZ  
5976  N NH1 . ARG A 398 ? 1.8444 1.7588 2.1734 0.3370  0.1862  -0.1826 398 ARG A NH1 
5977  N NH2 . ARG A 398 ? 1.7747 1.8376 2.1666 0.3398  0.1671  -0.1500 398 ARG A NH2 
5991  N N   . SER A 399 ? 1.4449 1.5598 1.6241 0.1454  0.0187  -0.0725 399 SER A N   
5992  C CA  . SER A 399 ? 1.4173 1.5797 1.6101 0.1202  0.0211  -0.0740 399 SER A CA  
5993  C C   . SER A 399 ? 1.3357 1.4626 1.4846 0.0924  0.0144  -0.0681 399 SER A C   
5994  O O   . SER A 399 ? 1.3275 1.4443 1.4575 0.0734  0.0333  -0.0726 399 SER A O   
5995  C CB  . SER A 399 ? 1.4813 1.7130 1.7247 0.1260  0.0026  -0.0656 399 SER A CB  
5996  O OG  . SER A 399 ? 1.5397 1.7579 1.7812 0.1442  -0.0230 -0.0465 399 SER A OG  
6002  N N   . CYS A 400 ? 1.1335 1.2434 1.2692 0.0913  -0.0104 -0.0549 400 CYS A N   
6003  C CA  . CYS A 400 ? 1.0007 1.0778 1.1012 0.0698  -0.0175 -0.0476 400 CYS A CA  
6004  C C   . CYS A 400 ? 0.9403 0.9640 1.0053 0.0788  -0.0324 -0.0378 400 CYS A C   
6005  O O   . CYS A 400 ? 0.9540 0.9725 1.0302 0.0990  -0.0438 -0.0325 400 CYS A O   
6006  C CB  . CYS A 400 ? 0.9879 1.1032 1.1088 0.0546  -0.0309 -0.0453 400 CYS A CB  
6007  S SG  . CYS A 400 ? 0.9882 1.0694 1.0795 0.0282  -0.0319 -0.0403 400 CYS A SG  
6012  N N   . PRO A 401 ? 0.8674 0.8530 0.8938 0.0647  -0.0314 -0.0332 401 PRO A N   
6013  C CA  . PRO A 401 ? 0.8319 0.7723 0.8265 0.0695  -0.0434 -0.0283 401 PRO A CA  
6014  C C   . PRO A 401 ? 0.7727 0.7099 0.7781 0.0772  -0.0653 -0.0160 401 PRO A C   
6015  O O   . PRO A 401 ? 0.7432 0.7102 0.7646 0.0705  -0.0747 -0.0085 401 PRO A O   
6016  C CB  . PRO A 401 ? 0.8246 0.7460 0.7861 0.0506  -0.0421 -0.0201 401 PRO A CB  
6017  C CG  . PRO A 401 ? 0.8521 0.7952 0.8211 0.0421  -0.0203 -0.0230 401 PRO A CG  
6018  C CD  . PRO A 401 ? 0.8431 0.8265 0.8562 0.0448  -0.0168 -0.0307 401 PRO A CD  
6026  N N   . PRO A 402 ? 0.7930 0.6945 0.7894 0.0892  -0.0716 -0.0144 402 PRO A N   
6027  C CA  . PRO A 402 ? 0.8017 0.6970 0.8077 0.0970  -0.0904 0.0034  402 PRO A CA  
6028  C C   . PRO A 402 ? 0.7799 0.6820 0.7716 0.0786  -0.1043 0.0161  402 PRO A C   
6029  O O   . PRO A 402 ? 0.7874 0.7137 0.7928 0.0816  -0.1174 0.0303  402 PRO A O   
6030  C CB  . PRO A 402 ? 0.8192 0.6585 0.8094 0.1035  -0.0884 -0.0007 402 PRO A CB  
6031  C CG  . PRO A 402 ? 0.8322 0.6617 0.8176 0.1079  -0.0672 -0.0248 402 PRO A CG  
6032  C CD  . PRO A 402 ? 0.8201 0.6873 0.8008 0.0959  -0.0580 -0.0310 402 PRO A CD  
6040  N N   . SER A 403 ? 0.7389 0.6244 0.7044 0.0606  -0.1008 0.0129  403 SER A N   
6041  C CA  . SER A 403 ? 0.7326 0.6237 0.6900 0.0448  -0.1087 0.0233  403 SER A CA  
6042  C C   . SER A 403 ? 0.7512 0.6269 0.7031 0.0459  -0.1251 0.0382  403 SER A C   
6043  O O   . SER A 403 ? 0.7347 0.6316 0.6911 0.0392  -0.1325 0.0471  403 SER A O   
6044  C CB  . SER A 403 ? 0.7364 0.6704 0.7156 0.0376  -0.1038 0.0194  403 SER A CB  
6045  O OG  . SER A 403 ? 0.7657 0.7165 0.7582 0.0379  -0.0870 0.0065  403 SER A OG  
6051  N N   . PHE A 404 ? 0.7969 0.6349 0.7388 0.0520  -0.1280 0.0391  404 PHE A N   
6052  C CA  . PHE A 404 ? 0.7701 0.5858 0.7070 0.0499  -0.1399 0.0547  404 PHE A CA  
6053  C C   . PHE A 404 ? 0.7606 0.5782 0.6816 0.0301  -0.1452 0.0609  404 PHE A C   
6054  O O   . PHE A 404 ? 0.7710 0.5788 0.6766 0.0193  -0.1420 0.0538  404 PHE A O   
6055  C CB  . PHE A 404 ? 0.7778 0.5451 0.7086 0.0546  -0.1360 0.0477  404 PHE A CB  
6056  C CG  . PHE A 404 ? 0.7596 0.4953 0.6846 0.0463  -0.1442 0.0617  404 PHE A CG  
6057  C CD1 . PHE A 404 ? 0.7576 0.4801 0.6618 0.0238  -0.1482 0.0572  404 PHE A CD1 
6058  C CD2 . PHE A 404 ? 0.7987 0.5213 0.7420 0.0610  -0.1471 0.0822  404 PHE A CD2 
6059  C CE1 . PHE A 404 ? 0.8113 0.5072 0.7136 0.0128  -0.1538 0.0687  404 PHE A CE1 
6060  C CE2 . PHE A 404 ? 0.8354 0.5256 0.7747 0.0515  -0.1513 0.0974  404 PHE A CE2 
6061  C CZ  . PHE A 404 ? 0.8396 0.5157 0.7588 0.0257  -0.1540 0.0884  404 PHE A CZ  
6071  N N   . GLY A 405 ? 0.7559 0.5919 0.6815 0.0262  -0.1529 0.0756  405 GLY A N   
6072  C CA  . GLY A 405 ? 0.7396 0.5822 0.6569 0.0097  -0.1544 0.0810  405 GLY A CA  
6073  C C   . GLY A 405 ? 0.7463 0.6223 0.6719 0.0034  -0.1458 0.0740  405 GLY A C   
6074  O O   . GLY A 405 ? 0.7207 0.6029 0.6455 -0.0078 -0.1430 0.0778  405 GLY A O   
6078  N N   . TYR A 406 ? 0.7416 0.6386 0.6792 0.0091  -0.1386 0.0622  406 TYR A N   
6079  C CA  . TYR A 406 ? 0.7053 0.6296 0.6549 -0.0010 -0.1262 0.0509  406 TYR A CA  
6080  C C   . TYR A 406 ? 0.7278 0.6774 0.6775 -0.0115 -0.1291 0.0527  406 TYR A C   
6081  O O   . TYR A 406 ? 0.7381 0.6962 0.6946 -0.0241 -0.1154 0.0428  406 TYR A O   
6082  C CB  . TYR A 406 ? 0.6905 0.6402 0.6565 0.0037  -0.1194 0.0370  406 TYR A CB  
6083  C CG  . TYR A 406 ? 0.6388 0.6084 0.6206 -0.0107 -0.1012 0.0204  406 TYR A CG  
6084  C CD1 . TYR A 406 ? 0.5992 0.6071 0.5905 -0.0239 -0.1000 0.0083  406 TYR A CD1 
6085  C CD2 . TYR A 406 ? 0.6286 0.5793 0.6157 -0.0129 -0.0831 0.0166  406 TYR A CD2 
6086  C CE1 . TYR A 406 ? 0.5779 0.5981 0.5867 -0.0411 -0.0789 -0.0129 406 TYR A CE1 
6087  C CE2 . TYR A 406 ? 0.6068 0.5666 0.6136 -0.0267 -0.0614 0.0026  406 TYR A CE2 
6088  C CZ  . TYR A 406 ? 0.6155 0.6069 0.6349 -0.0419 -0.0582 -0.0150 406 TYR A CZ  
6089  O OH  . TYR A 406 ? 0.6771 0.6721 0.7192 -0.0595 -0.0324 -0.0348 406 TYR A OH  
6099  N N   . SER A 407 ? 0.7496 0.7115 0.6926 -0.0064 -0.1442 0.0659  407 SER A N   
6100  C CA  . SER A 407 ? 0.7542 0.7429 0.6893 -0.0172 -0.1480 0.0716  407 SER A CA  
6101  C C   . SER A 407 ? 0.7267 0.6924 0.6486 -0.0121 -0.1604 0.0972  407 SER A C   
6102  O O   . SER A 407 ? 0.7123 0.6519 0.6353 0.0020  -0.1682 0.1093  407 SER A O   
6103  C CB  . SER A 407 ? 0.8044 0.8506 0.7442 -0.0195 -0.1536 0.0656  407 SER A CB  
6104  O OG  . SER A 407 ? 0.8315 0.8863 0.7746 -0.0003 -0.1693 0.0860  407 SER A OG  
6110  N N   . MET A 408 ? 0.8952 0.5423 0.8070 0.0088  -0.1102 0.0746  408 MET A N   
6111  C CA  . MET A 408 ? 0.8566 0.5075 0.7617 0.0074  -0.1114 0.0760  408 MET A CA  
6112  C C   . MET A 408 ? 0.8428 0.5028 0.7435 0.0028  -0.1116 0.0712  408 MET A C   
6113  O O   . MET A 408 ? 0.8544 0.5176 0.7594 0.0025  -0.1098 0.0632  408 MET A O   
6114  C CB  . MET A 408 ? 0.8253 0.4747 0.7294 0.0105  -0.1096 0.0766  408 MET A CB  
6115  C CG  . MET A 408 ? 0.8330 0.4799 0.7392 0.0135  -0.1088 0.0796  408 MET A CG  
6116  S SD  . MET A 408 ? 0.8325 0.4818 0.7362 0.0160  -0.1079 0.0797  408 MET A SD  
6117  C CE  . MET A 408 ? 0.8165 0.4641 0.7250 0.0177  -0.1076 0.0799  408 MET A CE  
6127  N N   . LYS A 409 ? 0.8376 0.5040 0.7317 -0.0018 -0.1141 0.0758  409 LYS A N   
6128  C CA  . LYS A 409 ? 0.8625 0.5439 0.7495 -0.0084 -0.1133 0.0721  409 LYS A CA  
6129  C C   . LYS A 409 ? 0.8759 0.5613 0.7580 -0.0126 -0.1153 0.0804  409 LYS A C   
6130  O O   . LYS A 409 ? 0.8783 0.5576 0.7635 -0.0133 -0.1207 0.0908  409 LYS A O   
6131  C CB  . LYS A 409 ? 0.8688 0.5608 0.7515 -0.0147 -0.1166 0.0717  409 LYS A CB  
6132  C CG  . LYS A 409 ? 0.8648 0.5794 0.7389 -0.0231 -0.1144 0.0642  409 LYS A CG  
6133  C CD  . LYS A 409 ? 0.8257 0.5451 0.7083 -0.0201 -0.1086 0.0454  409 LYS A CD  
6134  C CE  . LYS A 409 ? 0.8968 0.6436 0.7735 -0.0285 -0.1047 0.0329  409 LYS A CE  
6135  N NZ  . LYS A 409 ? 1.0264 0.7778 0.9193 -0.0244 -0.0994 0.0111  409 LYS A NZ  
6149  N N   . GLY A 410 ? 0.8890 0.5853 0.7677 -0.0154 -0.1113 0.0752  410 GLY A N   
6150  C CA  . GLY A 410 ? 0.8654 0.5674 0.7408 -0.0207 -0.1127 0.0833  410 GLY A CA  
6151  C C   . GLY A 410 ? 0.8626 0.5889 0.7287 -0.0311 -0.1099 0.0801  410 GLY A C   
6152  O O   . GLY A 410 ? 0.8983 0.6391 0.7586 -0.0361 -0.1089 0.0740  410 GLY A O   
6156  N N   . ALA A 411 ? 0.8280 0.5617 0.6932 -0.0354 -0.1082 0.0834  411 ALA A N   
6157  C CA  . ALA A 411 ? 0.8096 0.5713 0.6665 -0.0463 -0.1037 0.0790  411 ALA A CA  
6158  C C   . ALA A 411 ? 0.8432 0.6236 0.6873 -0.0603 -0.1087 0.0920  411 ALA A C   
6159  O O   . ALA A 411 ? 0.8925 0.7021 0.7263 -0.0703 -0.1045 0.0844  411 ALA A O   
6160  C CB  . ALA A 411 ? 0.7769 0.5512 0.6375 -0.0431 -0.0958 0.0562  411 ALA A CB  
6166  N N   . THR A 412 ? 0.8643 0.6310 0.7108 -0.0617 -0.1184 0.1112  412 THR A N   
6167  C CA  . THR A 412 ? 0.8942 0.6779 0.7316 -0.0759 -0.1263 0.1293  412 THR A CA  
6168  C C   . THR A 412 ? 0.8723 0.6418 0.7213 -0.0788 -0.1360 0.1518  412 THR A C   
6169  O O   . THR A 412 ? 0.8482 0.5909 0.7135 -0.0679 -0.1403 0.1534  412 THR A O   
6170  C CB  . THR A 412 ? 0.9545 0.7368 0.7892 -0.0749 -0.1317 0.1299  412 THR A CB  
6171  O OG1 . THR A 412 ? 1.0286 0.8306 0.8537 -0.0760 -0.1238 0.1094  412 THR A OG1 
6172  C CG2 . THR A 412 ? 0.9524 0.7467 0.7824 -0.0883 -0.1440 0.1544  412 THR A CG2 
6180  N N   . ASP A 413 ? 0.9109 0.7008 0.7538 -0.0943 -0.1396 0.1684  413 ASP A N   
6181  C CA  . ASP A 413 ? 0.9356 0.7137 0.7942 -0.0995 -0.1508 0.1924  413 ASP A CA  
6182  C C   . ASP A 413 ? 0.9713 0.7500 0.8331 -0.1064 -0.1650 0.2135  413 ASP A C   
6183  O O   . ASP A 413 ? 0.9996 0.8047 0.8486 -0.1234 -0.1706 0.2310  413 ASP A O   
6184  C CB  . ASP A 413 ? 0.9472 0.7474 0.8002 -0.1142 -0.1483 0.2025  413 ASP A CB  
6185  C CG  . ASP A 413 ? 0.9864 0.7695 0.8626 -0.1174 -0.1589 0.2238  413 ASP A CG  
6186  O OD1 . ASP A 413 ? 0.9895 0.7427 0.8882 -0.1054 -0.1661 0.2243  413 ASP A OD1 
6187  O OD2 . ASP A 413 ? 1.0183 0.8197 0.8927 -0.1325 -0.1601 0.2392  413 ASP A OD2 
6192  N N   . ILE A 414 ? 0.9860 0.7381 0.8657 -0.0938 -0.1714 0.2119  414 ILE A N   
6193  C CA  . ILE A 414 ? 1.0418 0.7942 0.9274 -0.0983 -0.1851 0.2289  414 ILE A CA  
6194  C C   . ILE A 414 ? 1.0854 0.8323 0.9933 -0.1078 -0.2015 0.2587  414 ILE A C   
6195  O O   . ILE A 414 ? 1.1066 0.8647 1.0153 -0.1188 -0.2150 0.2811  414 ILE A O   
6196  C CB  . ILE A 414 ? 1.0198 0.7491 0.9189 -0.0821 -0.1855 0.2149  414 ILE A CB  
6197  C CG1 . ILE A 414 ? 1.0104 0.7454 0.9127 -0.0872 -0.1986 0.2293  414 ILE A CG1 
6198  C CG2 . ILE A 414 ? 1.0074 0.7083 0.9366 -0.0704 -0.1886 0.2123  414 ILE A CG2 
6199  C CD1 . ILE A 414 ? 0.9783 0.6981 0.8894 -0.0735 -0.1970 0.2136  414 ILE A CD1 
6211  N N   . ASP A 415 ? 1.0977 0.8276 1.0265 -0.1041 -0.2020 0.2602  415 ASP A N   
6212  C CA  . ASP A 415 ? 1.1452 0.8678 1.1019 -0.1131 -0.2183 0.2880  415 ASP A CA  
6213  C C   . ASP A 415 ? 1.2186 0.9638 1.1630 -0.1311 -0.2172 0.3051  415 ASP A C   
6214  O O   . ASP A 415 ? 1.2035 0.9415 1.1735 -0.1393 -0.2295 0.3281  415 ASP A O   
6215  C CB  . ASP A 415 ? 1.1099 0.8004 1.1045 -0.0986 -0.2215 0.2783  415 ASP A CB  
6216  C CG  . ASP A 415 ? 1.0775 0.7644 1.0690 -0.0936 -0.2084 0.2607  415 ASP A CG  
6217  O OD1 . ASP A 415 ? 1.0676 0.7713 1.0278 -0.0949 -0.1939 0.2474  415 ASP A OD1 
6218  O OD2 . ASP A 415 ? 1.0739 0.7421 1.0971 -0.0883 -0.2131 0.2590  415 ASP A OD2 
6223  N N   . LYS A 416 ? 1.2778 1.0513 1.1872 -0.1379 -0.2028 0.2935  416 LYS A N   
6224  C CA  . LYS A 416 ? 1.3344 1.1379 1.2285 -0.1575 -0.2002 0.3086  416 LYS A CA  
6225  C C   . LYS A 416 ? 1.2778 1.0656 1.1977 -0.1583 -0.2026 0.3166  416 LYS A C   
6226  O O   . LYS A 416 ? 1.3211 1.1221 1.2476 -0.1761 -0.2113 0.3445  416 LYS A O   
6227  C CB  . LYS A 416 ? 1.4385 1.2687 1.3230 -0.1788 -0.2142 0.3416  416 LYS A CB  
6228  C CG  . LYS A 416 ? 1.5085 1.3682 1.3601 -0.1837 -0.2092 0.3321  416 LYS A CG  
6229  C CD  . LYS A 416 ? 1.5990 1.4989 1.4177 -0.1944 -0.1916 0.3152  416 LYS A CD  
6230  C CE  . LYS A 416 ? 1.6973 1.6341 1.4859 -0.2039 -0.1890 0.3085  416 LYS A CE  
6231  N NZ  . LYS A 416 ? 1.8060 1.7836 1.5678 -0.2127 -0.1706 0.2849  416 LYS A NZ  
6245  N N   . ASN A 417 ? 1.1736 0.9346 1.1090 -0.1397 -0.1955 0.2925  417 ASN A N   
6246  C CA  . ASN A 417 ? 1.0867 0.8326 1.0476 -0.1384 -0.1967 0.2941  417 ASN A CA  
6247  C C   . ASN A 417 ? 1.0379 0.7986 0.9812 -0.1380 -0.1796 0.2743  417 ASN A C   
6248  O O   . ASN A 417 ? 1.0122 0.7615 0.9747 -0.1352 -0.1786 0.2706  417 ASN A O   
6249  C CB  . ASN A 417 ? 1.0445 0.7542 1.0385 -0.1194 -0.2018 0.2805  417 ASN A CB  
6250  C CG  . ASN A 417 ? 1.0896 0.7911 1.0726 -0.1018 -0.1863 0.2462  417 ASN A CG  
6251  O OD1 . ASN A 417 ? 1.1085 0.8226 1.0627 -0.0982 -0.1754 0.2315  417 ASN A OD1 
6252  N ND2 . ASN A 417 ? 1.0908 0.7724 1.0986 -0.0913 -0.1863 0.2334  417 ASN A ND2 
6259  N N   . GLY A 418 ? 1.0350 0.8215 0.9457 -0.1404 -0.1668 0.2600  418 GLY A N   
6260  C CA  . GLY A 418 ? 1.0526 0.8562 0.9501 -0.1403 -0.1513 0.2405  418 GLY A CA  
6261  C C   . GLY A 418 ? 1.0422 0.8286 0.9398 -0.1196 -0.1409 0.2091  418 GLY A C   
6262  O O   . GLY A 418 ? 1.0657 0.8647 0.9567 -0.1179 -0.1293 0.1921  418 GLY A O   
6266  N N   . TYR A 419 ? 1.0420 0.8022 0.9483 -0.1045 -0.1451 0.2016  419 TYR A N   
6267  C CA  . TYR A 419 ? 1.0323 0.7770 0.9394 -0.0864 -0.1369 0.1760  419 TYR A CA  
6268  C C   . TYR A 419 ? 1.0240 0.7624 0.9218 -0.0779 -0.1367 0.1677  419 TYR A C   
6269  O O   . TYR A 419 ? 1.0265 0.7550 0.9316 -0.0786 -0.1466 0.1802  419 TYR A O   
6270  C CB  . TYR A 419 ? 1.0139 0.7326 0.9466 -0.0765 -0.1420 0.1734  419 TYR A CB  
6271  C CG  . TYR A 419 ? 1.0387 0.7623 0.9837 -0.0837 -0.1419 0.1785  419 TYR A CG  
6272  C CD1 . TYR A 419 ? 1.0927 0.8205 1.0509 -0.0985 -0.1514 0.2028  419 TYR A CD1 
6273  C CD2 . TYR A 419 ? 1.0533 0.7777 0.9987 -0.0765 -0.1334 0.1605  419 TYR A CD2 
6274  C CE1 . TYR A 419 ? 1.1068 0.8394 1.0783 -0.1061 -0.1514 0.2081  419 TYR A CE1 
6275  C CE2 . TYR A 419 ? 1.0809 0.8106 1.0388 -0.0832 -0.1334 0.1643  419 TYR A CE2 
6276  C CZ  . TYR A 419 ? 1.0951 0.8287 1.0661 -0.0981 -0.1418 0.1875  419 TYR A CZ  
6277  O OH  . TYR A 419 ? 1.1351 0.8741 1.1208 -0.1057 -0.1419 0.1918  419 TYR A OH  
6287  N N   . PRO A 420 ? 1.0097 0.7532 0.8950 -0.0700 -0.1266 0.1472  420 PRO A N   
6288  C CA  . PRO A 420 ? 0.9697 0.7079 0.8482 -0.0630 -0.1264 0.1399  420 PRO A CA  
6289  C C   . PRO A 420 ? 0.9751 0.6860 0.8687 -0.0508 -0.1319 0.1390  420 PRO A C   
6290  O O   . PRO A 420 ? 0.9753 0.6724 0.8827 -0.0442 -0.1326 0.1358  420 PRO A O   
6291  C CB  . PRO A 420 ? 0.9723 0.7193 0.8424 -0.0567 -0.1151 0.1179  420 PRO A CB  
6292  C CG  . PRO A 420 ? 1.0033 0.7678 0.8726 -0.0633 -0.1093 0.1146  420 PRO A CG  
6293  C CD  . PRO A 420 ? 1.0110 0.7648 0.8925 -0.0667 -0.1159 0.1300  420 PRO A CD  
6301  N N   . ASP A 421 ? 0.9635 0.6702 0.8549 -0.0484 -0.1354 0.1402  421 ASP A N   
6302  C CA  . ASP A 421 ? 0.9464 0.6324 0.8528 -0.0384 -0.1402 0.1387  421 ASP A CA  
6303  C C   . ASP A 421 ? 0.9484 0.6310 0.8472 -0.0296 -0.1341 0.1243  421 ASP A C   
6304  O O   . ASP A 421 ? 0.9843 0.6792 0.8692 -0.0319 -0.1286 0.1173  421 ASP A O   
6305  C CB  . ASP A 421 ? 0.9635 0.6464 0.8816 -0.0444 -0.1527 0.1563  421 ASP A CB  
6306  C CG  . ASP A 421 ? 0.9628 0.6498 0.8911 -0.0554 -0.1606 0.1749  421 ASP A CG  
6307  O OD1 . ASP A 421 ? 0.9388 0.6179 0.8801 -0.0528 -0.1596 0.1720  421 ASP A OD1 
6308  O OD2 . ASP A 421 ? 0.9920 0.6918 0.9157 -0.0677 -0.1683 0.1932  421 ASP A OD2 
6313  N N   . LEU A 422 ? 0.9327 0.6003 0.8431 -0.0202 -0.1351 0.1189  422 LEU A N   
6314  C CA  . LEU A 422 ? 0.9389 0.6024 0.8448 -0.0122 -0.1292 0.1069  422 LEU A CA  
6315  C C   . LEU A 422 ? 0.9436 0.6006 0.8581 -0.0093 -0.1336 0.1085  422 LEU A C   
6316  O O   . LEU A 422 ? 0.9278 0.5777 0.8589 -0.0079 -0.1398 0.1124  422 LEU A O   
6317  C CB  . LEU A 422 ? 0.9184 0.5757 0.8283 -0.0045 -0.1244 0.0977  422 LEU A CB  
6318  C CG  . LEU A 422 ? 0.8945 0.5479 0.8024 0.0026  -0.1198 0.0894  422 LEU A CG  
6319  C CD1 . LEU A 422 ? 0.8885 0.5470 0.7869 0.0020  -0.1155 0.0854  422 LEU A CD1 
6320  C CD2 . LEU A 422 ? 0.8909 0.5425 0.8022 0.0078  -0.1172 0.0835  422 LEU A CD2 
6332  N N   . ILE A 423 ? 0.9081 0.5678 0.8147 -0.0084 -0.1307 0.1037  423 ILE A N   
6333  C CA  . ILE A 423 ? 0.8948 0.5496 0.8096 -0.0050 -0.1331 0.1027  423 ILE A CA  
6334  C C   . ILE A 423 ? 0.9010 0.5512 0.8160 0.0020  -0.1260 0.0928  423 ILE A C   
6335  O O   . ILE A 423 ? 0.9036 0.5556 0.8101 0.0030  -0.1205 0.0879  423 ILE A O   
6336  C CB  . ILE A 423 ? 0.9663 0.6293 0.8741 -0.0103 -0.1359 0.1053  423 ILE A CB  
6337  C CG1 . ILE A 423 ? 0.9925 0.6657 0.8961 -0.0200 -0.1434 0.1180  423 ILE A CG1 
6338  C CG2 . ILE A 423 ? 0.9750 0.6331 0.8941 -0.0069 -0.1391 0.1045  423 ILE A CG2 
6339  C CD1 . ILE A 423 ? 0.9957 0.6841 0.8875 -0.0273 -0.1453 0.1186  423 ILE A CD1 
6351  N N   . VAL A 424 ? 0.9211 0.5673 0.8481 0.0061  -0.1266 0.0901  424 VAL A N   
6352  C CA  . VAL A 424 ? 0.9088 0.5552 0.8354 0.0104  -0.1204 0.0833  424 VAL A CA  
6353  C C   . VAL A 424 ? 0.8845 0.5316 0.8202 0.0109  -0.1214 0.0818  424 VAL A C   
6354  O O   . VAL A 424 ? 0.9037 0.5505 0.8542 0.0115  -0.1264 0.0818  424 VAL A O   
6355  C CB  . VAL A 424 ? 0.9078 0.5558 0.8393 0.0136  -0.1179 0.0780  424 VAL A CB  
6356  C CG1 . VAL A 424 ? 0.9008 0.5544 0.8294 0.0154  -0.1119 0.0736  424 VAL A CG1 
6357  C CG2 . VAL A 424 ? 0.9337 0.5814 0.8578 0.0130  -0.1174 0.0792  424 VAL A CG2 
6367  N N   . GLY A 425 ? 0.8563 0.5044 0.7871 0.0107  -0.1174 0.0805  425 GLY A N   
6368  C CA  . GLY A 425 ? 0.8263 0.4766 0.7662 0.0107  -0.1172 0.0787  425 GLY A CA  
6369  C C   . GLY A 425 ? 0.7894 0.4459 0.7331 0.0122  -0.1112 0.0742  425 GLY A C   
6370  O O   . GLY A 425 ? 0.7741 0.4331 0.7100 0.0126  -0.1071 0.0745  425 GLY A O   
6374  N N   . ALA A 426 ? 0.7865 0.4487 0.7430 0.0122  -0.1109 0.0703  426 ALA A N   
6375  C CA  . ALA A 426 ? 0.7786 0.4532 0.7395 0.0116  -0.1042 0.0647  426 ALA A CA  
6376  C C   . ALA A 426 ? 0.8169 0.4960 0.7885 0.0097  -0.1034 0.0634  426 ALA A C   
6377  O O   . ALA A 426 ? 0.8529 0.5395 0.8417 0.0110  -0.1042 0.0557  426 ALA A O   
6378  C CB  . ALA A 426 ? 0.7453 0.4284 0.7177 0.0142  -0.1038 0.0544  426 ALA A CB  
6384  N N   . PHE A 427 ? 0.8285 0.5035 0.7935 0.0067  -0.1023 0.0699  427 PHE A N   
6385  C CA  . PHE A 427 ? 0.8635 0.5405 0.8395 0.0045  -0.1030 0.0692  427 PHE A CA  
6386  C C   . PHE A 427 ? 0.8860 0.5795 0.8723 0.0021  -0.0965 0.0639  427 PHE A C   
6387  O O   . PHE A 427 ? 0.9232 0.6217 0.9244 0.0015  -0.0975 0.0596  427 PHE A O   
6388  C CB  . PHE A 427 ? 0.8559 0.5251 0.8267 0.0015  -0.1034 0.0754  427 PHE A CB  
6389  C CG  . PHE A 427 ? 0.8424 0.5153 0.8100 -0.0024 -0.0977 0.0817  427 PHE A CG  
6390  C CD1 . PHE A 427 ? 0.8094 0.4922 0.7860 -0.0074 -0.0935 0.0836  427 PHE A CD1 
6391  C CD2 . PHE A 427 ? 0.8484 0.5160 0.8059 -0.0020 -0.0974 0.0876  427 PHE A CD2 
6392  C CE1 . PHE A 427 ? 0.8157 0.5034 0.7901 -0.0130 -0.0897 0.0936  427 PHE A CE1 
6393  C CE2 . PHE A 427 ? 0.8468 0.5180 0.8039 -0.0065 -0.0947 0.0971  427 PHE A CE2 
6394  C CZ  . PHE A 427 ? 0.8332 0.5145 0.7982 -0.0126 -0.0911 0.1014  427 PHE A CZ  
6404  N N   . GLY A 428 ? 0.8560 0.5615 0.8349 -0.0002 -0.0899 0.0636  428 GLY A N   
6405  C CA  . GLY A 428 ? 0.8384 0.5662 0.8251 -0.0046 -0.0824 0.0575  428 GLY A CA  
6406  C C   . GLY A 428 ? 0.8391 0.5784 0.8455 -0.0008 -0.0823 0.0411  428 GLY A C   
6407  O O   . GLY A 428 ? 0.8469 0.6064 0.8660 -0.0041 -0.0763 0.0324  428 GLY A O   
6411  N N   . VAL A 429 ? 0.8764 0.6046 0.8889 0.0056  -0.0891 0.0365  429 VAL A N   
6412  C CA  . VAL A 429 ? 0.8860 0.6200 0.9254 0.0104  -0.0926 0.0221  429 VAL A CA  
6413  C C   . VAL A 429 ? 0.9198 0.6351 0.9713 0.0144  -0.1046 0.0280  429 VAL A C   
6414  O O   . VAL A 429 ? 0.9169 0.6315 0.9936 0.0189  -0.1113 0.0204  429 VAL A O   
6415  C CB  . VAL A 429 ? 0.8096 0.5504 0.8532 0.0133  -0.0915 0.0110  429 VAL A CB  
6416  C CG1 . VAL A 429 ? 0.8025 0.5704 0.8366 0.0079  -0.0797 0.0023  429 VAL A CG1 
6417  C CG2 . VAL A 429 ? 0.7674 0.4887 0.7937 0.0153  -0.0971 0.0222  429 VAL A CG2 
6427  N N   . ASP A 430 ? 0.9633 0.6652 0.9993 0.0122  -0.1081 0.0413  430 ASP A N   
6428  C CA  . ASP A 430 ? 1.0191 0.7090 1.0623 0.0136  -0.1195 0.0481  430 ASP A CA  
6429  C C   . ASP A 430 ? 1.0568 0.7377 1.1065 0.0170  -0.1283 0.0506  430 ASP A C   
6430  O O   . ASP A 430 ? 1.0755 0.7548 1.1493 0.0196  -0.1380 0.0500  430 ASP A O   
6431  C CB  . ASP A 430 ? 1.0258 0.7238 1.0939 0.0141  -0.1224 0.0422  430 ASP A CB  
6432  C CG  . ASP A 430 ? 1.0721 0.7810 1.1365 0.0095  -0.1130 0.0398  430 ASP A CG  
6433  O OD1 . ASP A 430 ? 1.0826 0.7845 1.1298 0.0057  -0.1119 0.0486  430 ASP A OD1 
6434  O OD2 . ASP A 430 ? 1.0857 0.8117 1.1666 0.0090  -0.1065 0.0285  430 ASP A OD2 
6439  N N   . ARG A 431 ? 1.0725 0.7477 1.1029 0.0166  -0.1258 0.0546  431 ARG A N   
6440  C CA  . ARG A 431 ? 1.0567 0.7246 1.0926 0.0187  -0.1326 0.0572  431 ARG A CA  
6441  C C   . ARG A 431 ? 0.9671 0.6264 0.9765 0.0158  -0.1328 0.0680  431 ARG A C   
6442  O O   . ARG A 431 ? 0.9269 0.5869 0.9164 0.0142  -0.1254 0.0687  431 ARG A O   
6443  C CB  . ARG A 431 ? 1.1471 0.8228 1.1946 0.0218  -0.1274 0.0439  431 ARG A CB  
6444  C CG  . ARG A 431 ? 1.2577 0.9278 1.3312 0.0250  -0.1369 0.0417  431 ARG A CG  
6445  C CD  . ARG A 431 ? 1.3414 1.0179 1.4534 0.0287  -0.1419 0.0305  431 ARG A CD  
6446  N NE  . ARG A 431 ? 1.4326 1.1287 1.5525 0.0299  -0.1303 0.0104  431 ARG A NE  
6447  C CZ  . ARG A 431 ? 1.5459 1.2545 1.6960 0.0322  -0.1299 -0.0037 431 ARG A CZ  
6448  N NH1 . ARG A 431 ? 1.5835 1.2843 1.7608 0.0346  -0.1420 0.0012  431 ARG A NH1 
6449  N NH2 . ARG A 431 ? 1.6138 1.3456 1.7674 0.0314  -0.1177 -0.0226 431 ARG A NH2 
6463  N N   . ALA A 432 ? 0.9422 0.5947 0.9547 0.0147  -0.1421 0.0766  432 ALA A N   
6464  C CA  . ALA A 432 ? 0.9658 0.6140 0.9567 0.0114  -0.1420 0.0848  432 ALA A CA  
6465  C C   . ALA A 432 ? 0.9866 0.6303 0.9900 0.0116  -0.1488 0.0889  432 ALA A C   
6466  O O   . ALA A 432 ? 1.0146 0.6559 1.0415 0.0117  -0.1592 0.0935  432 ALA A O   
6467  C CB  . ALA A 432 ? 0.9864 0.6358 0.9636 0.0060  -0.1465 0.0940  432 ALA A CB  
6473  N N   . ILE A 433 ? 1.0021 0.6445 0.9933 0.0115  -0.1441 0.0878  433 ILE A N   
6474  C CA  . ILE A 433 ? 0.9931 0.6314 0.9982 0.0118  -0.1490 0.0892  433 ILE A CA  
6475  C C   . ILE A 433 ? 0.9522 0.5894 0.9389 0.0061  -0.1503 0.1004  433 ILE A C   
6476  O O   . ILE A 433 ? 0.9645 0.6050 0.9278 0.0049  -0.1429 0.0992  433 ILE A O   
6477  C CB  . ILE A 433 ? 1.0190 0.6610 1.0307 0.0167  -0.1417 0.0740  433 ILE A CB  
6478  C CG1 . ILE A 433 ? 1.0670 0.7166 1.0952 0.0207  -0.1383 0.0607  433 ILE A CG1 
6479  C CG2 . ILE A 433 ? 1.0488 0.6865 1.0804 0.0171  -0.1476 0.0729  433 ILE A CG2 
6480  C CD1 . ILE A 433 ? 1.1479 0.8063 1.1553 0.0206  -0.1272 0.0554  433 ILE A CD1 
6492  N N   . LEU A 434 ? 0.9323 0.5660 0.9327 0.0021  -0.1601 0.1114  434 LEU A N   
6493  C CA  . LEU A 434 ? 0.9619 0.5981 0.9477 -0.0049 -0.1613 0.1225  434 LEU A CA  
6494  C C   . LEU A 434 ? 0.9555 0.5869 0.9553 -0.0034 -0.1617 0.1192  434 LEU A C   
6495  O O   . LEU A 434 ? 1.0034 0.6283 1.0336 -0.0012 -0.1694 0.1184  434 LEU A O   
6496  C CB  . LEU A 434 ? 0.9990 0.6386 0.9875 -0.0140 -0.1732 0.1420  434 LEU A CB  
6497  C CG  . LEU A 434 ? 1.0335 0.6801 1.0101 -0.0239 -0.1753 0.1555  434 LEU A CG  
6498  C CD1 . LEU A 434 ? 1.0074 0.6665 0.9517 -0.0271 -0.1643 0.1495  434 LEU A CD1 
6499  C CD2 . LEU A 434 ? 1.1275 0.7786 1.1136 -0.0343 -0.1901 0.1785  434 LEU A CD2 
6511  N N   . TYR A 435 ? 0.9239 0.5589 0.9050 -0.0045 -0.1540 0.1159  435 TYR A N   
6512  C CA  . TYR A 435 ? 0.8935 0.5261 0.8849 -0.0043 -0.1540 0.1130  435 TYR A CA  
6513  C C   . TYR A 435 ? 0.8730 0.5102 0.8555 -0.0140 -0.1571 0.1280  435 TYR A C   
6514  O O   . TYR A 435 ? 0.8455 0.4922 0.8032 -0.0180 -0.1512 0.1299  435 TYR A O   
6515  C CB  . TYR A 435 ? 0.9127 0.5487 0.8914 0.0016  -0.1434 0.0977  435 TYR A CB  
6516  C CG  . TYR A 435 ? 0.9372 0.5742 0.9227 0.0089  -0.1394 0.0834  435 TYR A CG  
6517  C CD1 . TYR A 435 ? 0.9696 0.6069 0.9785 0.0128  -0.1410 0.0713  435 TYR A CD1 
6518  C CD2 . TYR A 435 ? 0.9331 0.5735 0.9033 0.0110  -0.1338 0.0810  435 TYR A CD2 
6519  C CE1 . TYR A 435 ? 0.9773 0.6218 0.9914 0.0178  -0.1361 0.0566  435 TYR A CE1 
6520  C CE2 . TYR A 435 ? 0.9603 0.6054 0.9358 0.0156  -0.1296 0.0694  435 TYR A CE2 
6521  C CZ  . TYR A 435 ? 0.9678 0.6167 0.9638 0.0186  -0.1303 0.0570  435 TYR A CZ  
6522  O OH  . TYR A 435 ? 0.9751 0.6347 0.9754 0.0216  -0.1249 0.0438  435 TYR A OH  
6532  N N   . ARG A 436 ? 0.9314 0.5638 0.9368 -0.0185 -0.1663 0.1379  436 ARG A N   
6533  C CA  . ARG A 436 ? 1.0117 0.6509 1.0112 -0.0300 -0.1699 0.1547  436 ARG A CA  
6534  C C   . ARG A 436 ? 0.9812 0.6211 0.9818 -0.0294 -0.1644 0.1470  436 ARG A C   
6535  O O   . ARG A 436 ? 0.9753 0.6070 0.9953 -0.0222 -0.1644 0.1342  436 ARG A O   
6536  C CB  . ARG A 436 ? 1.1221 0.7559 1.1487 -0.0375 -0.1856 0.1753  436 ARG A CB  
6537  C CG  . ARG A 436 ? 1.2034 0.8375 1.2317 -0.0383 -0.1930 0.1841  436 ARG A CG  
6538  C CD  . ARG A 436 ? 1.2401 0.8734 1.2901 -0.0491 -0.2101 0.2110  436 ARG A CD  
6539  N NE  . ARG A 436 ? 1.2695 0.8859 1.3658 -0.0448 -0.2209 0.2110  436 ARG A NE  
6540  C CZ  . ARG A 436 ? 1.3583 0.9702 1.4829 -0.0543 -0.2361 0.2341  436 ARG A CZ  
6541  N NH1 . ARG A 436 ? 1.4361 1.0620 1.5424 -0.0700 -0.2418 0.2611  436 ARG A NH1 
6542  N NH2 . ARG A 436 ? 1.3942 0.9898 1.5672 -0.0489 -0.2461 0.2300  436 ARG A NH2 
6556  N N   . ALA A 437 ? 0.9565 0.6090 0.9370 -0.0375 -0.1595 0.1532  437 ALA A N   
6557  C CA  . ALA A 437 ? 0.9660 0.6220 0.9455 -0.0373 -0.1536 0.1455  437 ALA A CA  
6558  C C   . ALA A 437 ? 0.9854 0.6380 0.9895 -0.0456 -0.1625 0.1590  437 ALA A C   
6559  O O   . ALA A 437 ? 0.9927 0.6520 0.9976 -0.0581 -0.1693 0.1800  437 ALA A O   
6560  C CB  . ALA A 437 ? 0.9567 0.6300 0.9084 -0.0420 -0.1439 0.1434  437 ALA A CB  
6566  N N   . ARG A 438 ? 0.9776 0.6214 1.0025 -0.0397 -0.1631 0.1472  438 ARG A N   
6567  C CA  . ARG A 438 ? 1.0009 0.6402 1.0543 -0.0469 -0.1715 0.1572  438 ARG A CA  
6568  C C   . ARG A 438 ? 1.0214 0.6753 1.0598 -0.0565 -0.1657 0.1634  438 ARG A C   
6569  O O   . ARG A 438 ? 1.0361 0.6999 1.0509 -0.0525 -0.1546 0.1503  438 ARG A O   
6570  C CB  . ARG A 438 ? 0.9937 0.6220 1.0757 -0.0372 -0.1733 0.1378  438 ARG A CB  
6571  C CG  . ARG A 438 ? 0.9932 0.6106 1.0967 -0.0284 -0.1787 0.1283  438 ARG A CG  
6572  C CD  . ARG A 438 ? 0.9880 0.6042 1.1078 -0.0179 -0.1751 0.1010  438 ARG A CD  
6573  N NE  . ARG A 438 ? 1.0106 0.6217 1.1667 -0.0204 -0.1821 0.0970  438 ARG A NE  
6574  C CZ  . ARG A 438 ? 1.0228 0.6355 1.1998 -0.0133 -0.1808 0.0720  438 ARG A CZ  
6575  N NH1 . ARG A 438 ? 0.9975 0.6189 1.1598 -0.0042 -0.1726 0.0508  438 ARG A NH1 
6576  N NH2 . ARG A 438 ? 1.0702 0.6781 1.2834 -0.0163 -0.1879 0.0680  438 ARG A NH2 
6590  N N   . PRO A 439 ? 1.0155 0.6719 1.0698 -0.0698 -0.1737 0.1840  439 PRO A N   
6591  C CA  . PRO A 439 ? 1.0237 0.6967 1.0669 -0.0801 -0.1675 0.1887  439 PRO A CA  
6592  C C   . PRO A 439 ? 1.0392 0.7076 1.0959 -0.0727 -0.1634 0.1696  439 PRO A C   
6593  O O   . PRO A 439 ? 1.0485 0.7013 1.1318 -0.0641 -0.1688 0.1581  439 PRO A O   
6594  C CB  . PRO A 439 ? 1.0142 0.6901 1.0761 -0.0973 -0.1795 0.2187  439 PRO A CB  
6595  C CG  . PRO A 439 ? 1.0050 0.6578 1.1034 -0.0922 -0.1938 0.2238  439 PRO A CG  
6596  C CD  . PRO A 439 ? 0.9995 0.6449 1.0855 -0.0771 -0.1896 0.2053  439 PRO A CD  
6604  N N   . VAL A 440 ? 1.0549 0.7400 1.0945 -0.0764 -0.1538 0.1645  440 VAL A N   
6605  C CA  . VAL A 440 ? 1.0469 0.7319 1.0926 -0.0685 -0.1486 0.1446  440 VAL A CA  
6606  C C   . VAL A 440 ? 1.0756 0.7676 1.1398 -0.0806 -0.1510 0.1540  440 VAL A C   
6607  O O   . VAL A 440 ? 1.0949 0.8053 1.1471 -0.0939 -0.1473 0.1679  440 VAL A O   
6608  C CB  . VAL A 440 ? 1.0322 0.7300 1.0486 -0.0611 -0.1365 0.1288  440 VAL A CB  
6609  C CG1 . VAL A 440 ? 1.0199 0.7193 1.0437 -0.0538 -0.1332 0.1109  440 VAL A CG1 
6610  C CG2 . VAL A 440 ? 1.0151 0.7052 1.0160 -0.0504 -0.1349 0.1214  440 VAL A CG2 
6620  N N   . ILE A 441 ? 1.0909 0.7710 1.1853 -0.0767 -0.1567 0.1451  441 ILE A N   
6621  C CA  . ILE A 441 ? 1.1258 0.8107 1.2429 -0.0868 -0.1594 0.1508  441 ILE A CA  
6622  C C   . ILE A 441 ? 1.1319 0.8276 1.2395 -0.0797 -0.1503 0.1291  441 ILE A C   
6623  O O   . ILE A 441 ? 1.0774 0.7666 1.1875 -0.0663 -0.1498 0.1079  441 ILE A O   
6624  C CB  . ILE A 441 ? 1.1466 0.8121 1.3093 -0.0871 -0.1727 0.1523  441 ILE A CB  
6625  C CG1 . ILE A 441 ? 1.1472 0.8008 1.3249 -0.0935 -0.1841 0.1754  441 ILE A CG1 
6626  C CG2 . ILE A 441 ? 1.1915 0.8616 1.3805 -0.0980 -0.1757 0.1578  441 ILE A CG2 
6627  C CD1 . ILE A 441 ? 1.1412 0.7730 1.3668 -0.0878 -0.1971 0.1687  441 ILE A CD1 
6639  N N   . THR A 442 ? 1.1499 0.8651 1.2477 -0.0893 -0.1436 0.1344  442 THR A N   
6640  C CA  . THR A 442 ? 1.1917 0.9181 1.2884 -0.0845 -0.1372 0.1163  442 THR A CA  
6641  C C   . THR A 442 ? 1.2367 0.9619 1.3670 -0.0930 -0.1431 0.1192  442 THR A C   
6642  O O   . THR A 442 ? 1.3160 1.0421 1.4622 -0.1081 -0.1482 0.1409  442 THR A O   
6643  C CB  . THR A 442 ? 1.2203 0.9710 1.2914 -0.0890 -0.1258 0.1160  442 THR A CB  
6644  O OG1 . THR A 442 ? 1.2024 0.9528 1.2472 -0.0794 -0.1209 0.1095  442 THR A OG1 
6645  C CG2 . THR A 442 ? 1.2198 0.9829 1.2967 -0.0851 -0.1209 0.0992  442 THR A CG2 
6653  N N   . VAL A 443 ? 1.1928 0.9173 1.3350 -0.0841 -0.1433 0.0984  443 VAL A N   
6654  C CA  . VAL A 443 ? 1.2113 0.9322 1.3900 -0.0897 -0.1500 0.0958  443 VAL A CA  
6655  C C   . VAL A 443 ? 1.2102 0.9487 1.3866 -0.0881 -0.1440 0.0809  443 VAL A C   
6656  O O   . VAL A 443 ? 1.2321 0.9763 1.3900 -0.0755 -0.1396 0.0632  443 VAL A O   
6657  C CB  . VAL A 443 ? 1.2194 0.9214 1.4242 -0.0801 -0.1593 0.0810  443 VAL A CB  
6658  C CG1 . VAL A 443 ? 1.2414 0.9401 1.4891 -0.0861 -0.1670 0.0756  443 VAL A CG1 
6659  C CG2 . VAL A 443 ? 1.2338 0.9188 1.4444 -0.0806 -0.1659 0.0946  443 VAL A CG2 
6669  N N   . ASN A 444 ? 1.1993 0.9471 1.3965 -0.1015 -0.1446 0.0896  444 ASN A N   
6670  C CA  . ASN A 444 ? 1.1913 0.9559 1.3950 -0.1014 -0.1405 0.0757  444 ASN A CA  
6671  C C   . ASN A 444 ? 1.1711 0.9259 1.4149 -0.1026 -0.1501 0.0665  444 ASN A C   
6672  O O   . ASN A 444 ? 1.1821 0.9308 1.4553 -0.1162 -0.1563 0.0824  444 ASN A O   
6673  C CB  . ASN A 444 ? 1.2437 1.0312 1.4425 -0.1170 -0.1326 0.0902  444 ASN A CB  
6674  C CG  . ASN A 444 ? 1.2989 1.1017 1.4616 -0.1155 -0.1221 0.0926  444 ASN A CG  
6675  O OD1 . ASN A 444 ? 1.3286 1.1210 1.4719 -0.1101 -0.1224 0.0973  444 ASN A OD1 
6676  N ND2 . ASN A 444 ? 1.2954 1.1243 1.4520 -0.1203 -0.1127 0.0875  444 ASN A ND2 
6683  N N   . ALA A 445 ? 1.1395 0.8945 1.3861 -0.0896 -0.1522 0.0414  445 ALA A N   
6684  C CA  . ALA A 445 ? 1.1029 0.8515 1.3876 -0.0893 -0.1611 0.0264  445 ALA A CA  
6685  C C   . ALA A 445 ? 1.1000 0.8674 1.3921 -0.0894 -0.1592 0.0116  445 ALA A C   
6686  O O   . ALA A 445 ? 1.1124 0.8946 1.3780 -0.0813 -0.1533 0.0024  445 ALA A O   
6687  C CB  . ALA A 445 ? 1.0726 0.8108 1.3578 -0.0755 -0.1661 0.0062  445 ALA A CB  
6693  N N   . GLY A 446 ? 1.0877 0.8542 1.4195 -0.0987 -0.1653 0.0097  446 GLY A N   
6694  C CA  . GLY A 446 ? 1.0595 0.8439 1.4039 -0.1000 -0.1647 -0.0046 446 GLY A CA  
6695  C C   . GLY A 446 ? 1.0568 0.8365 1.4396 -0.0978 -0.1747 -0.0268 446 GLY A C   
6696  O O   . GLY A 446 ? 1.0732 0.8351 1.4880 -0.1014 -0.1827 -0.0255 446 GLY A O   
6700  N N   . LEU A 447 ? 1.0301 0.8277 1.4124 -0.0918 -0.1751 -0.0485 447 LEU A N   
6701  C CA  . LEU A 447 ? 1.0631 0.8634 1.4798 -0.0897 -0.1841 -0.0745 447 LEU A CA  
6702  C C   . LEU A 447 ? 1.1625 0.9845 1.5892 -0.0931 -0.1837 -0.0841 447 LEU A C   
6703  O O   . LEU A 447 ? 1.1851 1.0246 1.5817 -0.0860 -0.1792 -0.0883 447 LEU A O   
6704  C CB  . LEU A 447 ? 1.0316 0.8354 1.4302 -0.0753 -0.1867 -0.0982 447 LEU A CB  
6705  C CG  . LEU A 447 ? 1.0179 0.8301 1.4493 -0.0728 -0.1954 -0.1303 447 LEU A CG  
6706  C CD1 . LEU A 447 ? 1.0245 0.8161 1.5067 -0.0796 -0.2028 -0.1327 447 LEU A CD1 
6707  C CD2 . LEU A 447 ? 1.0070 0.8330 1.4097 -0.0602 -0.1957 -0.1519 447 LEU A CD2 
6719  N N   . GLU A 448 ? 1.2186 1.0392 1.6908 -0.1041 -0.1893 -0.0871 448 GLU A N   
6720  C CA  . GLU A 448 ? 1.2708 1.1118 1.7594 -0.1091 -0.1896 -0.0962 448 GLU A CA  
6721  C C   . GLU A 448 ? 1.2304 1.0745 1.7597 -0.1083 -0.2002 -0.1253 448 GLU A C   
6722  O O   . GLU A 448 ? 1.2400 1.0662 1.8082 -0.1136 -0.2071 -0.1278 448 GLU A O   
6723  C CB  . GLU A 448 ? 1.3699 1.2112 1.8775 -0.1265 -0.1853 -0.0708 448 GLU A CB  
6724  C CG  . GLU A 448 ? 1.4420 1.2847 1.9125 -0.1299 -0.1743 -0.0438 448 GLU A CG  
6725  C CD  . GLU A 448 ? 1.6041 1.4517 2.0937 -0.1500 -0.1700 -0.0182 448 GLU A CD  
6726  O OE1 . GLU A 448 ? 1.6552 1.5042 2.1876 -0.1611 -0.1757 -0.0201 448 GLU A OE1 
6727  O OE2 . GLU A 448 ? 1.6511 1.5037 2.1135 -0.1558 -0.1610 0.0036  448 GLU A OE2 
6734  N N   . VAL A 449 ? 1.1502 1.0180 1.6732 -0.1020 -0.2023 -0.1477 449 VAL A N   
6735  C CA  . VAL A 449 ? 1.0848 0.9628 1.6426 -0.1011 -0.2120 -0.1795 449 VAL A CA  
6736  C C   . VAL A 449 ? 1.0555 0.9523 1.6352 -0.1088 -0.2131 -0.1834 449 VAL A C   
6737  O O   . VAL A 449 ? 1.0605 0.9796 1.6140 -0.1030 -0.2111 -0.1875 449 VAL A O   
6738  C CB  . VAL A 449 ? 1.0268 0.9219 1.5555 -0.0872 -0.2151 -0.2052 449 VAL A CB  
6739  C CG1 . VAL A 449 ? 1.0070 0.9199 1.5709 -0.0877 -0.2247 -0.2410 449 VAL A CG1 
6740  C CG2 . VAL A 449 ? 1.0024 0.8806 1.5119 -0.0804 -0.2132 -0.2023 449 VAL A CG2 
6750  N N   . TYR A 450 ? 1.0462 0.9342 1.6768 -0.1220 -0.2173 -0.1814 450 TYR A N   
6751  C CA  . TYR A 450 ? 1.0315 0.9374 1.6889 -0.1310 -0.2185 -0.1856 450 TYR A CA  
6752  C C   . TYR A 450 ? 1.0226 0.9277 1.7377 -0.1364 -0.2298 -0.2117 450 TYR A C   
6753  O O   . TYR A 450 ? 1.0188 0.9003 1.7712 -0.1425 -0.2349 -0.2087 450 TYR A O   
6754  C CB  . TYR A 450 ? 1.0469 0.9476 1.7110 -0.1460 -0.2105 -0.1518 450 TYR A CB  
6755  C CG  . TYR A 450 ? 1.1261 0.9987 1.8158 -0.1579 -0.2118 -0.1275 450 TYR A CG  
6756  C CD1 . TYR A 450 ? 1.1410 0.9952 1.8010 -0.1531 -0.2084 -0.1103 450 TYR A CD1 
6757  C CD2 . TYR A 450 ? 1.1903 1.0554 1.9357 -0.1747 -0.2176 -0.1196 450 TYR A CD2 
6758  C CE1 . TYR A 450 ? 1.1792 1.0089 1.8636 -0.1643 -0.2114 -0.0858 450 TYR A CE1 
6759  C CE2 . TYR A 450 ? 1.2123 1.0520 1.9838 -0.1866 -0.2211 -0.0934 450 TYR A CE2 
6760  C CZ  . TYR A 450 ? 1.2149 1.0374 1.9554 -0.1811 -0.2183 -0.0764 450 TYR A CZ  
6761  O OH  . TYR A 450 ? 1.2284 1.0265 1.9958 -0.1931 -0.2236 -0.0483 450 TYR A OH  
6771  N N   . PRO A 451 ? 1.0443 0.9751 1.7719 -0.1345 -0.2352 -0.2385 451 PRO A N   
6772  C CA  . PRO A 451 ? 1.0579 1.0177 1.7484 -0.1267 -0.2325 -0.2438 451 PRO A CA  
6773  C C   . PRO A 451 ? 1.0368 1.0065 1.6775 -0.1107 -0.2329 -0.2548 451 PRO A C   
6774  O O   . PRO A 451 ? 1.0699 1.0325 1.7111 -0.1056 -0.2367 -0.2706 451 PRO A O   
6775  C CB  . PRO A 451 ? 1.0974 1.0791 1.8284 -0.1313 -0.2415 -0.2716 451 PRO A CB  
6776  C CG  . PRO A 451 ? 1.1048 1.0730 1.8815 -0.1347 -0.2500 -0.2935 451 PRO A CG  
6777  C CD  . PRO A 451 ? 1.0928 1.0261 1.8805 -0.1413 -0.2458 -0.2653 451 PRO A CD  
6785  N N   . SER A 452 ? 1.0438 1.0310 1.6448 -0.1036 -0.2292 -0.2463 452 SER A N   
6786  C CA  . SER A 452 ? 1.0094 1.0067 1.5630 -0.0899 -0.2302 -0.2512 452 SER A CA  
6787  C C   . SER A 452 ? 1.0237 1.0519 1.5785 -0.0850 -0.2413 -0.2824 452 SER A C   
6788  O O   . SER A 452 ? 1.0364 1.0715 1.5742 -0.0789 -0.2452 -0.2987 452 SER A O   
6789  C CB  . SER A 452 ? 1.0140 1.0155 1.5299 -0.0844 -0.2232 -0.2275 452 SER A CB  
6790  O OG  . SER A 452 ? 1.0257 1.0364 1.4990 -0.0721 -0.2256 -0.2292 452 SER A OG  
6796  N N   . ILE A 453 ? 1.0266 1.0769 1.6011 -0.0885 -0.2464 -0.2913 453 ILE A N   
6797  C CA  . ILE A 453 ? 1.0275 1.1108 1.6066 -0.0860 -0.2582 -0.3212 453 ILE A CA  
6798  C C   . ILE A 453 ? 1.0473 1.1291 1.6758 -0.0941 -0.2636 -0.3496 453 ILE A C   
6799  O O   . ILE A 453 ? 1.0224 1.0859 1.6936 -0.1041 -0.2611 -0.3442 453 ILE A O   
6800  C CB  . ILE A 453 ? 1.0205 1.1291 1.6028 -0.0860 -0.2627 -0.3190 453 ILE A CB  
6801  C CG1 . ILE A 453 ? 1.0318 1.1437 1.5700 -0.0763 -0.2596 -0.2948 453 ILE A CG1 
6802  C CG2 . ILE A 453 ? 1.0244 1.1692 1.6173 -0.0857 -0.2763 -0.3504 453 ILE A CG2 
6803  C CD1 . ILE A 453 ? 1.0399 1.1295 1.5778 -0.0788 -0.2469 -0.2664 453 ILE A CD1 
6815  N N   . LEU A 454 ? 1.0527 1.1560 1.6779 -0.0907 -0.2713 -0.3803 454 LEU A N   
6816  C CA  . LEU A 454 ? 1.0664 1.1701 1.7404 -0.0969 -0.2768 -0.4131 454 LEU A CA  
6817  C C   . LEU A 454 ? 1.0901 1.2363 1.7764 -0.0982 -0.2883 -0.4482 454 LEU A C   
6818  O O   . LEU A 454 ? 1.1275 1.3058 1.7729 -0.0921 -0.2930 -0.4563 454 LEU A O   
6819  C CB  . LEU A 454 ? 1.0405 1.1327 1.7061 -0.0925 -0.2742 -0.4242 454 LEU A CB  
6820  C CG  . LEU A 454 ? 0.9810 1.0315 1.6377 -0.0916 -0.2643 -0.3918 454 LEU A CG  
6821  C CD1 . LEU A 454 ? 0.9099 0.9542 1.5603 -0.0865 -0.2631 -0.4070 454 LEU A CD1 
6822  C CD2 . LEU A 454 ? 0.9942 1.0144 1.7028 -0.1023 -0.2629 -0.3772 454 LEU A CD2 
6834  N N   . ASN A 455 ? 1.0543 1.2019 1.7977 -0.1072 -0.2935 -0.4680 455 ASN A N   
6835  C CA  . ASN A 455 ? 1.0743 1.2621 1.8383 -0.1102 -0.3050 -0.5047 455 ASN A CA  
6836  C C   . ASN A 455 ? 1.1094 1.3006 1.9194 -0.1141 -0.3097 -0.5462 455 ASN A C   
6837  O O   . ASN A 455 ? 1.0768 1.2359 1.9388 -0.1203 -0.3080 -0.5464 455 ASN A O   
6838  C CB  . ASN A 455 ? 1.0583 1.2495 1.8568 -0.1178 -0.3080 -0.4984 455 ASN A CB  
6839  C CG  . ASN A 455 ? 1.0561 1.2870 1.8848 -0.1222 -0.3207 -0.5387 455 ASN A CG  
6840  O OD1 . ASN A 455 ? 1.0669 1.3271 1.8870 -0.1198 -0.3272 -0.5721 455 ASN A OD1 
6841  N ND2 . ASN A 455 ? 1.0594 1.2950 1.9233 -0.1295 -0.3239 -0.5366 455 ASN A ND2 
6848  N N   . GLN A 456 ? 1.1887 1.4213 1.9822 -0.1114 -0.3164 -0.5818 456 GLN A N   
6849  C CA  . GLN A 456 ? 1.2581 1.5002 2.0935 -0.1141 -0.3201 -0.6272 456 GLN A CA  
6850  C C   . GLN A 456 ? 1.2886 1.5269 2.1906 -0.1205 -0.3231 -0.6462 456 GLN A C   
6851  O O   . GLN A 456 ? 1.3352 1.5483 2.2816 -0.1195 -0.3175 -0.6538 456 GLN A O   
6852  C CB  . GLN A 456 ? 1.2921 1.5884 2.0891 -0.1110 -0.3252 -0.6603 456 GLN A CB  
6853  C CG  . GLN A 456 ? 1.2674 1.5636 2.0023 -0.1031 -0.3177 -0.6421 456 GLN A CG  
6854  C CD  . GLN A 456 ? 1.2648 1.6184 1.9460 -0.1019 -0.3233 -0.6573 456 GLN A CD  
6855  O OE1 . GLN A 456 ? 1.2484 1.6225 1.9050 -0.1001 -0.3203 -0.6749 456 GLN A OE1 
6856  N NE2 . GLN A 456 ? 1.2617 1.6433 1.9248 -0.1036 -0.3320 -0.6491 456 GLN A NE2 
6865  N N   . ASP A 457 ? 1.3018 1.5640 2.2085 -0.1246 -0.3296 -0.6485 457 ASP A N   
6866  C CA  . ASP A 457 ? 1.3201 1.5827 2.2820 -0.1283 -0.3298 -0.6647 457 ASP A CA  
6867  C C   . ASP A 457 ? 1.3854 1.5969 2.3999 -0.1337 -0.3246 -0.6409 457 ASP A C   
6868  O O   . ASP A 457 ? 1.4550 1.6574 2.5223 -0.1348 -0.3233 -0.6552 457 ASP A O   
6869  C CB  . ASP A 457 ? 1.2894 1.5833 2.2458 -0.1324 -0.3378 -0.6655 457 ASP A CB  
6870  C CG  . ASP A 457 ? 1.3490 1.6988 2.2677 -0.1283 -0.3443 -0.6943 457 ASP A CG  
6871  O OD1 . ASP A 457 ? 1.3779 1.7441 2.2795 -0.1234 -0.3409 -0.7172 457 ASP A OD1 
6872  O OD2 . ASP A 457 ? 1.3779 1.7573 2.2844 -0.1305 -0.3527 -0.6931 457 ASP A OD2 
6877  N N   . ASN A 458 ? 1.4125 1.5923 2.4139 -0.1377 -0.3222 -0.6036 458 ASN A N   
6878  C CA  . ASN A 458 ? 1.3929 1.5286 2.4374 -0.1460 -0.3179 -0.5730 458 ASN A CA  
6879  C C   . ASN A 458 ? 1.4070 1.5094 2.4763 -0.1422 -0.3131 -0.5713 458 ASN A C   
6880  O O   . ASN A 458 ? 1.3910 1.4797 2.4293 -0.1378 -0.3101 -0.5612 458 ASN A O   
6881  C CB  . ASN A 458 ? 1.3571 1.4780 2.3694 -0.1504 -0.3143 -0.5314 458 ASN A CB  
6882  C CG  . ASN A 458 ? 1.3952 1.4764 2.4468 -0.1618 -0.3095 -0.4972 458 ASN A CG  
6883  O OD1 . ASN A 458 ? 1.4006 1.4488 2.4497 -0.1614 -0.3042 -0.4751 458 ASN A OD1 
6884  N ND2 . ASN A 458 ? 1.4362 1.5224 2.5264 -0.1731 -0.3118 -0.4925 458 ASN A ND2 
6890  N N   . LYS A 459 ? 1.4574 1.5469 2.5856 -0.1436 -0.3131 -0.5804 459 LYS A N   
6891  C CA  . LYS A 459 ? 1.5175 1.5796 2.6797 -0.1383 -0.3107 -0.5821 459 LYS A CA  
6892  C C   . LYS A 459 ? 1.5936 1.6220 2.8175 -0.1468 -0.3118 -0.5571 459 LYS A C   
6893  O O   . LYS A 459 ? 1.6355 1.6695 2.9109 -0.1458 -0.3150 -0.5779 459 LYS A O   
6894  C CB  . LYS A 459 ? 1.5176 1.6098 2.6925 -0.1273 -0.3112 -0.6305 459 LYS A CB  
6895  C CG  . LYS A 459 ? 1.4548 1.5933 2.5717 -0.1216 -0.3114 -0.6590 459 LYS A CG  
6896  C CD  . LYS A 459 ? 1.4264 1.6005 2.5652 -0.1139 -0.3111 -0.7079 459 LYS A CD  
6897  C CE  . LYS A 459 ? 1.4054 1.6203 2.4863 -0.1076 -0.3089 -0.7327 459 LYS A CE  
6898  N NZ  . LYS A 459 ? 1.4305 1.6632 2.5385 -0.0990 -0.3044 -0.7708 459 LYS A NZ  
6912  N N   . THR A 460 ? 1.6548 1.6498 2.8739 -0.1558 -0.3094 -0.5118 460 THR A N   
6913  C CA  . THR A 460 ? 1.7297 1.6925 3.0016 -0.1656 -0.3108 -0.4807 460 THR A CA  
6914  C C   . THR A 460 ? 1.7657 1.6939 3.0544 -0.1621 -0.3107 -0.4600 460 THR A C   
6915  O O   . THR A 460 ? 1.8367 1.7365 3.1621 -0.1711 -0.3126 -0.4256 460 THR A O   
6916  C CB  . THR A 460 ? 1.7294 1.6852 2.9880 -0.1815 -0.3080 -0.4413 460 THR A CB  
6917  O OG1 . THR A 460 ? 1.7307 1.6824 2.9332 -0.1821 -0.3034 -0.4208 460 THR A OG1 
6918  C CG2 . THR A 460 ? 1.7072 1.6959 2.9671 -0.1856 -0.3096 -0.4606 460 THR A CG2 
6926  N N   . CYS A 461 ? 2.0012 2.0098 2.7375 -0.4440 -0.2397 -0.4858 461 CYS A N   
6927  C CA  . CYS A 461 ? 2.0501 1.9386 2.7347 -0.4244 -0.2359 -0.4410 461 CYS A CA  
6928  C C   . CYS A 461 ? 2.0871 1.8630 2.7436 -0.3972 -0.2652 -0.4617 461 CYS A C   
6929  O O   . CYS A 461 ? 2.0778 1.8814 2.7455 -0.3695 -0.2843 -0.5081 461 CYS A O   
6930  C CB  . CYS A 461 ? 2.0473 1.9750 2.7134 -0.3599 -0.2194 -0.4173 461 CYS A CB  
6931  S SG  . CYS A 461 ? 2.0436 2.1385 2.7521 -0.3432 -0.2068 -0.4413 461 CYS A SG  
6937  N N   . SER A 462 ? 2.0770 1.7256 2.6944 -0.4019 -0.2712 -0.4296 462 SER A N   
6938  C CA  . SER A 462 ? 2.1741 1.7047 2.7654 -0.3807 -0.3019 -0.4523 462 SER A CA  
6939  C C   . SER A 462 ? 2.1041 1.5755 2.6598 -0.3090 -0.3034 -0.4332 462 SER A C   
6940  O O   . SER A 462 ? 1.9375 1.3861 2.4749 -0.3071 -0.2888 -0.3857 462 SER A O   
6941  C CB  . SER A 462 ? 2.2848 1.6981 2.8601 -0.4539 -0.3185 -0.4399 462 SER A CB  
6942  O OG  . SER A 462 ? 2.2703 1.6184 2.8141 -0.4771 -0.3068 -0.3813 462 SER A OG  
6948  N N   . LEU A 463 ? 2.1129 1.5676 2.6594 -0.2517 -0.3209 -0.4730 463 LEU A N   
6949  C CA  . LEU A 463 ? 2.0680 1.4792 2.5871 -0.1824 -0.3239 -0.4678 463 LEU A CA  
6950  C C   . LEU A 463 ? 2.1977 1.4609 2.6895 -0.1870 -0.3488 -0.4561 463 LEU A C   
6951  O O   . LEU A 463 ? 2.3910 1.5734 2.8774 -0.2356 -0.3702 -0.4674 463 LEU A O   
6952  C CB  . LEU A 463 ? 1.9877 1.4399 2.5042 -0.1263 -0.3331 -0.5204 463 LEU A CB  
6953  C CG  . LEU A 463 ? 1.8287 1.3167 2.3268 -0.0540 -0.3215 -0.5211 463 LEU A CG  
6954  C CD1 . LEU A 463 ? 1.7013 1.2728 2.2014 -0.0489 -0.2914 -0.4783 463 LEU A CD1 
6955  C CD2 . LEU A 463 ? 1.7580 1.2941 2.2486 -0.0169 -0.3299 -0.5760 463 LEU A CD2 
6967  N N   . PRO A 464 ? 2.1484 1.3713 2.6200 -0.1379 -0.3489 -0.4330 464 PRO A N   
6968  C CA  . PRO A 464 ? 2.2841 1.3606 2.7271 -0.1261 -0.3811 -0.4300 464 PRO A CA  
6969  C C   . PRO A 464 ? 2.3667 1.4050 2.7947 -0.1008 -0.4023 -0.4813 464 PRO A C   
6970  O O   . PRO A 464 ? 2.3758 1.4809 2.8166 -0.0522 -0.3999 -0.5266 464 PRO A O   
6971  C CB  . PRO A 464 ? 2.2604 1.3483 2.6948 -0.0600 -0.3744 -0.4092 464 PRO A CB  
6972  C CG  . PRO A 464 ? 2.1299 1.3434 2.5801 -0.0677 -0.3362 -0.3780 464 PRO A CG  
6973  C CD  . PRO A 464 ? 2.0641 1.3693 2.5370 -0.0942 -0.3227 -0.4071 464 PRO A CD  
6981  N N   . GLY A 465 ? 2.8424 1.7733 3.2359 -0.1363 -0.4212 -0.4724 465 GLY A N   
6982  C CA  . GLY A 465 ? 3.1238 2.0157 3.5012 -0.1297 -0.4404 -0.5185 465 GLY A CA  
6983  C C   . GLY A 465 ? 2.9180 1.8386 3.3072 -0.2068 -0.4360 -0.5295 465 GLY A C   
6984  O O   . GLY A 465 ? 3.0312 1.9753 3.4321 -0.2748 -0.4205 -0.4951 465 GLY A O   
6988  N N   . THR A 466 ? 2.4907 1.4201 2.8779 -0.1958 -0.4490 -0.5806 466 THR A N   
6989  C CA  . THR A 466 ? 2.6022 1.5576 2.9993 -0.2662 -0.4497 -0.5981 466 THR A CA  
6990  C C   . THR A 466 ? 2.5309 1.6339 2.9724 -0.2576 -0.4378 -0.6325 466 THR A C   
6991  O O   . THR A 466 ? 2.6118 1.7514 3.0643 -0.3012 -0.4433 -0.6586 466 THR A O   
6992  C CB  . THR A 466 ? 2.7467 1.6016 3.1064 -0.2705 -0.4763 -0.6309 466 THR A CB  
6993  O OG1 . THR A 466 ? 2.7138 1.5873 3.0693 -0.1884 -0.4877 -0.6779 466 THR A OG1 
6994  C CG2 . THR A 466 ? 2.9109 1.6127 3.2225 -0.2887 -0.4905 -0.5950 466 THR A CG2 
7002  N N   . ALA A 467 ? 2.6022 1.7906 3.0660 -0.2037 -0.4227 -0.6329 467 ALA A N   
7003  C CA  . ALA A 467 ? 2.6863 2.0077 3.1817 -0.1907 -0.4136 -0.6641 467 ALA A CA  
7004  C C   . ALA A 467 ? 2.6843 2.0846 3.2186 -0.2607 -0.4016 -0.6494 467 ALA A C   
7005  O O   . ALA A 467 ? 2.8696 2.3409 3.4222 -0.2815 -0.4075 -0.6810 467 ALA A O   
7006  C CB  . ALA A 467 ? 2.6749 2.0592 3.1754 -0.1253 -0.3984 -0.6623 467 ALA A CB  
7012  N N   . LEU A 468 ? 2.5096 1.9078 3.0578 -0.2953 -0.3844 -0.6025 468 LEU A N   
7013  C CA  . LEU A 468 ? 2.4929 1.9638 3.0769 -0.3685 -0.3693 -0.5849 468 LEU A CA  
7014  C C   . LEU A 468 ? 2.3461 1.9685 2.9740 -0.3585 -0.3635 -0.6181 468 LEU A C   
7015  O O   . LEU A 468 ? 2.4043 2.0963 3.0614 -0.4130 -0.3607 -0.6269 468 LEU A O   
7016  C CB  . LEU A 468 ? 2.6238 2.0247 3.1888 -0.4447 -0.3796 -0.5815 468 LEU A CB  
7017  C CG  . LEU A 468 ? 2.7537 1.9881 3.2607 -0.4583 -0.3917 -0.5531 468 LEU A CG  
7018  C CD1 . LEU A 468 ? 2.8803 2.0423 3.3584 -0.5031 -0.4119 -0.5788 468 LEU A CD1 
7019  C CD2 . LEU A 468 ? 2.7650 1.9636 3.2606 -0.5127 -0.3731 -0.4936 468 LEU A CD2 
7031  N N   . LYS A 469 ? 2.2613 1.9396 2.8901 -0.2894 -0.3624 -0.6360 469 LYS A N   
7032  C CA  . LYS A 469 ? 2.1954 2.0065 2.8520 -0.2733 -0.3625 -0.6655 469 LYS A CA  
7033  C C   . LYS A 469 ? 2.0076 1.8729 2.6412 -0.2084 -0.3428 -0.6407 469 LYS A C   
7034  O O   . LYS A 469 ? 2.1541 2.0202 2.7552 -0.1517 -0.3505 -0.6606 469 LYS A O   
7035  C CB  . LYS A 469 ? 2.1519 1.9719 2.7924 -0.2535 -0.3858 -0.7128 469 LYS A CB  
7036  C CG  . LYS A 469 ? 1.9825 1.7737 2.6297 -0.3147 -0.3990 -0.7272 469 LYS A CG  
7037  C CD  . LYS A 469 ? 1.8056 1.6088 2.4334 -0.2855 -0.4231 -0.7760 469 LYS A CD  
7038  C CE  . LYS A 469 ? 1.8013 1.5753 2.4333 -0.3486 -0.4390 -0.7936 469 LYS A CE  
7039  N NZ  . LYS A 469 ? 1.8492 1.6327 2.4609 -0.3202 -0.4636 -0.8419 469 LYS A NZ  
7053  N N   . VAL A 470 ? 1.7310 1.6439 2.3781 -0.2208 -0.3177 -0.5990 470 VAL A N   
7054  C CA  . VAL A 470 ? 1.5240 1.4835 2.1474 -0.1669 -0.3011 -0.5748 470 VAL A CA  
7055  C C   . VAL A 470 ? 1.5135 1.5641 2.1672 -0.1864 -0.2835 -0.5546 470 VAL A C   
7056  O O   . VAL A 470 ? 1.5833 1.6438 2.2686 -0.2426 -0.2722 -0.5403 470 VAL A O   
7057  C CB  . VAL A 470 ? 1.5223 1.4017 2.1081 -0.1387 -0.2871 -0.5361 470 VAL A CB  
7058  C CG1 . VAL A 470 ? 1.5535 1.3752 2.1070 -0.0961 -0.3027 -0.5645 470 VAL A CG1 
7059  C CG2 . VAL A 470 ? 1.5816 1.3907 2.1762 -0.1878 -0.2788 -0.5015 470 VAL A CG2 
7069  N N   . SER A 471 ? 1.3935 1.5084 2.0323 -0.1392 -0.2819 -0.5544 471 SER A N   
7070  C CA  . SER A 471 ? 1.3542 1.5509 2.0134 -0.1403 -0.2679 -0.5384 471 SER A CA  
7071  C C   . SER A 471 ? 1.3525 1.5091 1.9815 -0.1279 -0.2429 -0.4867 471 SER A C   
7072  O O   . SER A 471 ? 1.2090 1.3170 1.7930 -0.0882 -0.2416 -0.4711 471 SER A O   
7073  C CB  . SER A 471 ? 1.3463 1.6151 1.9954 -0.0916 -0.2866 -0.5650 471 SER A CB  
7074  O OG  . SER A 471 ? 1.3119 1.6715 1.9953 -0.0946 -0.2818 -0.5671 471 SER A OG  
7080  N N   . CYS A 472 ? 1.5536 1.7384 2.2067 -0.1636 -0.2225 -0.4623 472 CYS A N   
7081  C CA  . CYS A 472 ? 1.7396 1.8715 2.3653 -0.1651 -0.2008 -0.4132 472 CYS A CA  
7082  C C   . CYS A 472 ? 1.4063 1.6053 2.0418 -0.1687 -0.1817 -0.3947 472 CYS A C   
7083  O O   . CYS A 472 ? 1.3208 1.6117 1.9928 -0.1760 -0.1830 -0.4208 472 CYS A O   
7084  C CB  . CYS A 472 ? 2.0843 2.1375 2.7127 -0.2157 -0.1953 -0.3926 472 CYS A CB  
7085  S SG  . CYS A 472 ? 2.0518 2.1585 2.7241 -0.2955 -0.1796 -0.3894 472 CYS A SG  
7091  N N   . PHE A 473 ? 1.2264 1.3802 1.8299 -0.1617 -0.1652 -0.3522 473 PHE A N   
7092  C CA  . PHE A 473 ? 1.1505 1.3458 1.7500 -0.1627 -0.1459 -0.3288 473 PHE A CA  
7093  C C   . PHE A 473 ? 1.1867 1.3027 1.7504 -0.1688 -0.1330 -0.2816 473 PHE A C   
7094  O O   . PHE A 473 ? 1.1923 1.2311 1.7414 -0.1700 -0.1408 -0.2717 473 PHE A O   
7095  C CB  . PHE A 473 ? 1.0987 1.3400 1.6809 -0.1086 -0.1543 -0.3414 473 PHE A CB  
7096  C CG  . PHE A 473 ? 1.0886 1.2683 1.6202 -0.0653 -0.1631 -0.3267 473 PHE A CG  
7097  C CD1 . PHE A 473 ? 1.1214 1.2768 1.6428 -0.0462 -0.1811 -0.3490 473 PHE A CD1 
7098  C CD2 . PHE A 473 ? 1.0600 1.2113 1.5532 -0.0477 -0.1523 -0.2925 473 PHE A CD2 
7099  C CE1 . PHE A 473 ? 1.1343 1.2454 1.6083 -0.0118 -0.1849 -0.3370 473 PHE A CE1 
7100  C CE2 . PHE A 473 ? 1.0729 1.1783 1.5217 -0.0160 -0.1577 -0.2797 473 PHE A CE2 
7101  C CZ  . PHE A 473 ? 1.1092 1.1982 1.5485 0.0012  -0.1723 -0.3018 473 PHE A CZ  
7111  N N   . ASN A 474 ? 1.2156 1.3516 1.7647 -0.1685 -0.1161 -0.2556 474 ASN A N   
7112  C CA  . ASN A 474 ? 1.2197 1.2882 1.7356 -0.1753 -0.1064 -0.2114 474 ASN A CA  
7113  C C   . ASN A 474 ? 1.1419 1.2225 1.6263 -0.1406 -0.0999 -0.1933 474 ASN A C   
7114  O O   . ASN A 474 ? 1.1053 1.2469 1.5933 -0.1223 -0.0986 -0.2104 474 ASN A O   
7115  C CB  . ASN A 474 ? 1.2932 1.3521 1.8155 -0.2349 -0.0910 -0.1883 474 ASN A CB  
7116  C CG  . ASN A 474 ? 1.3480 1.5000 1.8893 -0.2567 -0.0715 -0.1968 474 ASN A CG  
7117  O OD1 . ASN A 474 ? 1.3443 1.5400 1.8758 -0.2224 -0.0670 -0.2005 474 ASN A OD1 
7118  N ND2 . ASN A 474 ? 1.4218 1.6049 1.9886 -0.3158 -0.0601 -0.2018 474 ASN A ND2 
7125  N N   . VAL A 475 ? 1.1258 1.1452 1.5791 -0.1309 -0.0990 -0.1604 475 VAL A N   
7126  C CA  . VAL A 475 ? 1.1007 1.1183 1.5201 -0.1051 -0.0944 -0.1391 475 VAL A CA  
7127  C C   . VAL A 475 ? 1.1180 1.1088 1.5218 -0.1327 -0.0825 -0.1016 475 VAL A C   
7128  O O   . VAL A 475 ? 1.1112 1.0483 1.5142 -0.1524 -0.0860 -0.0830 475 VAL A O   
7129  C CB  . VAL A 475 ? 1.0843 1.0664 1.4810 -0.0691 -0.1051 -0.1365 475 VAL A CB  
7130  C CG1 . VAL A 475 ? 1.0753 1.0504 1.4364 -0.0540 -0.1002 -0.1104 475 VAL A CG1 
7131  C CG2 . VAL A 475 ? 1.0546 1.0616 1.4535 -0.0428 -0.1174 -0.1711 475 VAL A CG2 
7141  N N   . ARG A 476 ? 1.1350 1.1572 1.5210 -0.1318 -0.0717 -0.0916 476 ARG A N   
7142  C CA  . ARG A 476 ? 1.2031 1.2072 1.5661 -0.1564 -0.0605 -0.0573 476 ARG A CA  
7143  C C   . ARG A 476 ? 1.1830 1.1741 1.5111 -0.1282 -0.0634 -0.0405 476 ARG A C   
7144  O O   . ARG A 476 ? 1.1089 1.1321 1.4260 -0.1065 -0.0634 -0.0561 476 ARG A O   
7145  C CB  . ARG A 476 ? 1.2718 1.3359 1.6443 -0.1883 -0.0422 -0.0652 476 ARG A CB  
7146  C CG  . ARG A 476 ? 1.3503 1.3967 1.6930 -0.2222 -0.0292 -0.0296 476 ARG A CG  
7147  C CD  . ARG A 476 ? 1.3865 1.5063 1.7423 -0.2596 -0.0069 -0.0434 476 ARG A CD  
7148  N NE  . ARG A 476 ? 1.4705 1.5745 1.7893 -0.2989 0.0074  -0.0083 476 ARG A NE  
7149  C CZ  . ARG A 476 ? 1.5345 1.6812 1.8285 -0.2988 0.0222  -0.0068 476 ARG A CZ  
7150  N NH1 . ARG A 476 ? 1.5122 1.7146 1.8154 -0.2590 0.0227  -0.0396 476 ARG A NH1 
7151  N NH2 . ARG A 476 ? 1.6385 1.7665 1.8924 -0.3378 0.0340  0.0270  476 ARG A NH2 
7165  N N   . PHE A 477 ? 1.2542 1.1964 1.5641 -0.1285 -0.0689 -0.0102 477 PHE A N   
7166  C CA  . PHE A 477 ? 1.2725 1.2051 1.5534 -0.1072 -0.0732 0.0053  477 PHE A CA  
7167  C C   . PHE A 477 ? 1.2918 1.2089 1.5467 -0.1278 -0.0690 0.0377  477 PHE A C   
7168  O O   . PHE A 477 ? 1.3387 1.2215 1.5933 -0.1481 -0.0721 0.0588  477 PHE A O   
7169  C CB  . PHE A 477 ? 1.2814 1.1884 1.5684 -0.0829 -0.0856 0.0054  477 PHE A CB  
7170  C CG  . PHE A 477 ? 1.3099 1.1750 1.6020 -0.0875 -0.0946 0.0275  477 PHE A CG  
7171  C CD1 . PHE A 477 ? 1.3264 1.1607 1.6420 -0.0862 -0.1037 0.0174  477 PHE A CD1 
7172  C CD2 . PHE A 477 ? 1.3441 1.1966 1.6153 -0.0896 -0.0984 0.0560  477 PHE A CD2 
7173  C CE1 . PHE A 477 ? 1.4053 1.1902 1.7209 -0.0834 -0.1182 0.0360  477 PHE A CE1 
7174  C CE2 . PHE A 477 ? 1.4195 1.2319 1.6934 -0.0872 -0.1126 0.0751  477 PHE A CE2 
7175  C CZ  . PHE A 477 ? 1.4521 1.2273 1.7472 -0.0819 -0.1235 0.0653  477 PHE A CZ  
7185  N N   . CYS A 478 ? 1.2770 1.2118 1.5034 -0.1225 -0.0652 0.0416  478 CYS A N   
7186  C CA  . CYS A 478 ? 1.2987 1.2238 1.4944 -0.1413 -0.0621 0.0692  478 CYS A CA  
7187  C C   . CYS A 478 ? 1.2917 1.2110 1.4584 -0.1254 -0.0702 0.0785  478 CYS A C   
7188  O O   . CYS A 478 ? 1.2835 1.2128 1.4425 -0.1063 -0.0729 0.0606  478 CYS A O   
7189  C CB  . CYS A 478 ? 1.3064 1.2699 1.4913 -0.1635 -0.0446 0.0607  478 CYS A CB  
7190  S SG  . CYS A 478 ? 1.4047 1.4082 1.6297 -0.1840 -0.0308 0.0341  478 CYS A SG  
7195  N N   . LEU A 479 ? 1.2752 1.1744 1.4209 -0.1365 -0.0765 0.1076  479 LEU A N   
7196  C CA  . LEU A 479 ? 1.2478 1.1451 1.3647 -0.1306 -0.0851 0.1186  479 LEU A CA  
7197  C C   . LEU A 479 ? 1.2368 1.1315 1.3169 -0.1520 -0.0828 0.1386  479 LEU A C   
7198  O O   . LEU A 479 ? 1.2566 1.1378 1.3319 -0.1718 -0.0804 0.1571  479 LEU A O   
7199  C CB  . LEU A 479 ? 1.2602 1.1459 1.3929 -0.1175 -0.1010 0.1319  479 LEU A CB  
7200  C CG  . LEU A 479 ? 1.2412 1.1411 1.3812 -0.1008 -0.1045 0.1175  479 LEU A CG  
7201  C CD1 . LEU A 479 ? 1.2310 1.1364 1.3837 -0.0897 -0.0965 0.0912  479 LEU A CD1 
7202  C CD2 . LEU A 479 ? 1.2140 1.1202 1.3822 -0.0883 -0.1162 0.1251  479 LEU A CD2 
7214  N N   . LYS A 480 ? 1.2210 1.1228 1.2681 -0.1503 -0.0852 0.1353  480 LYS A N   
7215  C CA  . LYS A 480 ? 1.1963 1.0977 1.2011 -0.1680 -0.0852 0.1508  480 LYS A CA  
7216  C C   . LYS A 480 ? 1.1841 1.0778 1.1652 -0.1624 -0.1013 0.1556  480 LYS A C   
7217  O O   . LYS A 480 ? 1.1851 1.0771 1.1674 -0.1496 -0.1048 0.1381  480 LYS A O   
7218  C CB  . LYS A 480 ? 1.1762 1.1054 1.1606 -0.1753 -0.0664 0.1285  480 LYS A CB  
7219  C CG  . LYS A 480 ? 1.2373 1.1730 1.1732 -0.1958 -0.0622 0.1410  480 LYS A CG  
7220  C CD  . LYS A 480 ? 1.2655 1.2406 1.1845 -0.1932 -0.0441 0.1071  480 LYS A CD  
7221  C CE  . LYS A 480 ? 1.3250 1.3105 1.1889 -0.2107 -0.0396 0.1133  480 LYS A CE  
7222  N NZ  . LYS A 480 ? 1.3570 1.3889 1.2067 -0.2012 -0.0223 0.0722  480 LYS A NZ  
7236  N N   . ALA A 481 ? 1.2050 1.0917 1.1604 -0.1748 -0.1132 0.1798  481 ALA A N   
7237  C CA  . ALA A 481 ? 1.2187 1.1048 1.1582 -0.1741 -0.1309 0.1842  481 ALA A CA  
7238  C C   . ALA A 481 ? 1.2973 1.1808 1.1877 -0.1905 -0.1389 0.1979  481 ALA A C   
7239  O O   . ALA A 481 ? 1.3519 1.2314 1.2224 -0.2027 -0.1348 0.2146  481 ALA A O   
7240  C CB  . ALA A 481 ? 1.1838 1.0766 1.1626 -0.1644 -0.1470 0.1977  481 ALA A CB  
7246  N N   . ASP A 482 ? 1.3086 1.1914 1.1741 -0.1943 -0.1515 0.1912  482 ASP A N   
7247  C CA  . ASP A 482 ? 1.3889 1.2697 1.2044 -0.2092 -0.1632 0.1994  482 ASP A CA  
7248  C C   . ASP A 482 ? 1.3820 1.2634 1.1917 -0.2153 -0.1834 0.1953  482 ASP A C   
7249  O O   . ASP A 482 ? 1.3360 1.2214 1.1777 -0.2109 -0.1849 0.1885  482 ASP A O   
7250  C CB  . ASP A 482 ? 1.4435 1.3215 1.2136 -0.2131 -0.1465 0.1784  482 ASP A CB  
7251  C CG  . ASP A 482 ? 1.5192 1.3991 1.2334 -0.2299 -0.1541 0.1896  482 ASP A CG  
7252  O OD1 . ASP A 482 ? 1.5390 1.4185 1.2498 -0.2381 -0.1740 0.2179  482 ASP A OD1 
7253  O OD2 . ASP A 482 ? 1.5618 1.4465 1.2344 -0.2320 -0.1418 0.1675  482 ASP A OD2 
7258  N N   . GLY A 483 ? 1.4269 1.3064 1.1922 -0.2297 -0.1985 0.1992  483 GLY A N   
7259  C CA  . GLY A 483 ? 1.4467 1.3275 1.2027 -0.2435 -0.2186 0.1939  483 GLY A CA  
7260  C C   . GLY A 483 ? 1.5500 1.4220 1.2461 -0.2594 -0.2337 0.1915  483 GLY A C   
7261  O O   . GLY A 483 ? 1.6162 1.4820 1.2732 -0.2581 -0.2252 0.1909  483 GLY A O   
7265  N N   . LYS A 484 ? 1.5983 1.4741 1.2861 -0.2780 -0.2556 0.1884  484 LYS A N   
7266  C CA  . LYS A 484 ? 1.7145 1.5830 1.3468 -0.2962 -0.2758 0.1839  484 LYS A CA  
7267  C C   . LYS A 484 ? 1.7211 1.6326 1.3802 -0.3121 -0.3040 0.1999  484 LYS A C   
7268  O O   . LYS A 484 ? 1.6954 1.6337 1.4037 -0.3191 -0.3073 0.2008  484 LYS A O   
7269  C CB  . LYS A 484 ? 1.7887 1.6076 1.3710 -0.3071 -0.2786 0.1535  484 LYS A CB  
7270  C CG  . LYS A 484 ? 1.8874 1.6707 1.4410 -0.2847 -0.2563 0.1293  484 LYS A CG  
7271  C CD  . LYS A 484 ? 1.9592 1.6811 1.4600 -0.2889 -0.2675 0.0974  484 LYS A CD  
7272  C CE  . LYS A 484 ? 2.0010 1.6966 1.4763 -0.2578 -0.2496 0.0666  484 LYS A CE  
7273  N NZ  . LYS A 484 ? 2.0846 1.7067 1.5035 -0.2541 -0.2673 0.0330  484 LYS A NZ  
7287  N N   . GLY A 485 ? 1.7889 1.7141 1.4156 -0.3179 -0.3244 0.2109  485 GLY A N   
7288  C CA  . GLY A 485 ? 1.8217 1.7947 1.4712 -0.3307 -0.3566 0.2218  485 GLY A CA  
7289  C C   . GLY A 485 ? 1.7900 1.8015 1.4826 -0.3074 -0.3690 0.2494  485 GLY A C   
7290  O O   . GLY A 485 ? 1.7898 1.7779 1.4693 -0.2885 -0.3576 0.2660  485 GLY A O   
7294  N N   . VAL A 486 ? 1.7691 1.8404 1.5129 -0.3096 -0.3945 0.2528  486 VAL A N   
7295  C CA  . VAL A 486 ? 1.8115 1.9211 1.5985 -0.2808 -0.4165 0.2743  486 VAL A CA  
7296  C C   . VAL A 486 ? 1.7532 1.8660 1.6020 -0.2549 -0.3941 0.2759  486 VAL A C   
7297  O O   . VAL A 486 ? 1.7407 1.8955 1.6454 -0.2591 -0.3848 0.2602  486 VAL A O   
7298  C CB  . VAL A 486 ? 1.8290 2.0170 1.6566 -0.2880 -0.4536 0.2695  486 VAL A CB  
7299  C CG1 . VAL A 486 ? 1.8090 2.0444 1.7013 -0.2476 -0.4758 0.2829  486 VAL A CG1 
7300  C CG2 . VAL A 486 ? 1.9176 2.1001 1.6799 -0.3074 -0.4834 0.2719  486 VAL A CG2 
7310  N N   . LEU A 487 ? 1.7628 1.8315 1.5978 -0.2317 -0.3855 0.2946  487 LEU A N   
7311  C CA  . LEU A 487 ? 1.7015 1.7647 1.5892 -0.2068 -0.3670 0.2950  487 LEU A CA  
7312  C C   . LEU A 487 ? 1.7515 1.7742 1.6249 -0.1817 -0.3802 0.3228  487 LEU A C   
7313  O O   . LEU A 487 ? 1.8489 1.8324 1.6549 -0.1919 -0.3888 0.3424  487 LEU A O   
7314  C CB  . LEU A 487 ? 1.6383 1.6646 1.5148 -0.2177 -0.3261 0.2797  487 LEU A CB  
7315  C CG  . LEU A 487 ? 1.6393 1.6831 1.5246 -0.2403 -0.3126 0.2545  487 LEU A CG  
7316  C CD1 . LEU A 487 ? 1.6234 1.6189 1.4860 -0.2425 -0.2796 0.2414  487 LEU A CD1 
7317  C CD2 . LEU A 487 ? 1.6352 1.7417 1.5934 -0.2338 -0.3167 0.2457  487 LEU A CD2 
7329  N N   . PRO A 488 ? 1.7065 1.7319 1.6347 -0.1511 -0.3827 0.3248  488 PRO A N   
7330  C CA  . PRO A 488 ? 1.7346 1.6990 1.6412 -0.1311 -0.3944 0.3517  488 PRO A CA  
7331  C C   . PRO A 488 ? 1.7149 1.6220 1.5881 -0.1490 -0.3560 0.3551  488 PRO A C   
7332  O O   . PRO A 488 ? 1.6818 1.6008 1.5632 -0.1647 -0.3224 0.3327  488 PRO A O   
7333  C CB  . PRO A 488 ? 1.7453 1.7369 1.7286 -0.0899 -0.4111 0.3427  488 PRO A CB  
7334  C CG  . PRO A 488 ? 1.6774 1.7298 1.7169 -0.0975 -0.3824 0.3096  488 PRO A CG  
7335  C CD  . PRO A 488 ? 1.6543 1.7365 1.6626 -0.1351 -0.3754 0.3010  488 PRO A CD  
7343  N N   . ARG A 489 ? 1.7794 1.6233 1.6125 -0.1474 -0.3637 0.3836  489 ARG A N   
7344  C CA  . ARG A 489 ? 1.7848 1.5822 1.5860 -0.1697 -0.3289 0.3887  489 ARG A CA  
7345  C C   . ARG A 489 ? 1.7546 1.5218 1.6022 -0.1507 -0.3225 0.3864  489 ARG A C   
7346  O O   . ARG A 489 ? 1.7590 1.4672 1.5742 -0.1641 -0.3159 0.4063  489 ARG A O   
7347  C CB  . ARG A 489 ? 1.8869 1.6336 1.6013 -0.1946 -0.3362 0.4229  489 ARG A CB  
7348  C CG  . ARG A 489 ? 1.9376 1.7100 1.5935 -0.2184 -0.3351 0.4209  489 ARG A CG  
7349  C CD  . ARG A 489 ? 2.0621 1.7855 1.6265 -0.2461 -0.3375 0.4555  489 ARG A CD  
7350  N NE  . ARG A 489 ? 2.1124 1.8592 1.6127 -0.2669 -0.3393 0.4528  489 ARG A NE  
7351  C CZ  . ARG A 489 ? 2.2370 1.9529 1.6469 -0.2933 -0.3433 0.4811  489 ARG A CZ  
7352  N NH1 . ARG A 489 ? 2.3423 1.9967 1.7125 -0.3065 -0.3463 0.5181  489 ARG A NH1 
7353  N NH2 . ARG A 489 ? 2.2587 2.0009 1.6119 -0.3093 -0.3450 0.4725  489 ARG A NH2 
7367  N N   . LYS A 490 ? 1.6975 1.5052 1.6179 -0.1231 -0.3238 0.3612  490 LYS A N   
7368  C CA  . LYS A 490 ? 1.6865 1.4705 1.6533 -0.1006 -0.3201 0.3526  490 LYS A CA  
7369  C C   . LYS A 490 ? 1.6118 1.4649 1.6505 -0.0786 -0.3131 0.3184  490 LYS A C   
7370  O O   . LYS A 490 ? 1.6239 1.5340 1.6863 -0.0675 -0.3314 0.3108  490 LYS A O   
7371  C CB  . LYS A 490 ? 1.7744 1.4997 1.7328 -0.0734 -0.3612 0.3777  490 LYS A CB  
7372  C CG  . LYS A 490 ? 1.7545 1.4484 1.7603 -0.0440 -0.3647 0.3647  490 LYS A CG  
7373  C CD  . LYS A 490 ? 1.8294 1.4450 1.8126 -0.0158 -0.4123 0.3912  490 LYS A CD  
7374  C CE  . LYS A 490 ? 1.8419 1.4368 1.8818 0.0278  -0.4262 0.3688  490 LYS A CE  
7375  N NZ  . LYS A 490 ? 1.7922 1.4852 1.9106 0.0703  -0.4339 0.3318  490 LYS A NZ  
7389  N N   . LEU A 491 ? 1.5465 1.3988 1.6173 -0.0763 -0.2864 0.2976  491 LEU A N   
7390  C CA  . LEU A 491 ? 1.4332 1.3475 1.5613 -0.0619 -0.2744 0.2661  491 LEU A CA  
7391  C C   . LEU A 491 ? 1.4247 1.3179 1.5909 -0.0396 -0.2669 0.2506  491 LEU A C   
7392  O O   . LEU A 491 ? 1.4425 1.2796 1.5875 -0.0513 -0.2547 0.2573  491 LEU A O   
7393  C CB  . LEU A 491 ? 1.3450 1.2863 1.4569 -0.0912 -0.2443 0.2511  491 LEU A CB  
7394  C CG  . LEU A 491 ? 1.3561 1.3263 1.4371 -0.1130 -0.2514 0.2559  491 LEU A CG  
7395  C CD1 . LEU A 491 ? 1.3288 1.2721 1.3583 -0.1414 -0.2283 0.2535  491 LEU A CD1 
7396  C CD2 . LEU A 491 ? 1.3457 1.3840 1.4662 -0.1127 -0.2523 0.2361  491 LEU A CD2 
7408  N N   . ASN A 492 ? 1.3930 1.3374 1.6156 -0.0096 -0.2734 0.2271  492 ASN A N   
7409  C CA  . ASN A 492 ? 1.3940 1.3261 1.6544 0.0157  -0.2677 0.2056  492 ASN A CA  
7410  C C   . ASN A 492 ? 1.3247 1.3018 1.6019 0.0025  -0.2341 0.1794  492 ASN A C   
7411  O O   . ASN A 492 ? 1.2675 1.3156 1.5654 -0.0005 -0.2278 0.1655  492 ASN A O   
7412  C CB  . ASN A 492 ? 1.4347 1.3973 1.7452 0.0637  -0.2972 0.1908  492 ASN A CB  
7413  C CG  . ASN A 492 ? 1.5327 1.4531 1.8227 0.0823  -0.3390 0.2173  492 ASN A CG  
7414  O OD1 . ASN A 492 ? 1.5443 1.5164 1.8693 0.1158  -0.3673 0.2084  492 ASN A OD1 
7415  N ND2 . ASN A 492 ? 1.6117 1.4425 1.8428 0.0595  -0.3439 0.2495  492 ASN A ND2 
7422  N N   . PHE A 493 ? 1.3044 1.2403 1.5698 -0.0080 -0.2144 0.1734  493 PHE A N   
7423  C CA  . PHE A 493 ? 1.2462 1.2105 1.5180 -0.0180 -0.1871 0.1505  493 PHE A CA  
7424  C C   . PHE A 493 ? 1.2282 1.1928 1.5372 0.0089  -0.1845 0.1245  493 PHE A C   
7425  O O   . PHE A 493 ? 1.2198 1.1348 1.5375 0.0259  -0.1987 0.1259  493 PHE A O   
7426  C CB  . PHE A 493 ? 1.2275 1.1562 1.4590 -0.0473 -0.1681 0.1568  493 PHE A CB  
7427  C CG  . PHE A 493 ? 1.1750 1.1181 1.3692 -0.0723 -0.1628 0.1671  493 PHE A CG  
7428  C CD1 . PHE A 493 ? 1.1777 1.1004 1.3394 -0.0861 -0.1736 0.1909  493 PHE A CD1 
7429  C CD2 . PHE A 493 ? 1.1219 1.0910 1.3059 -0.0829 -0.1494 0.1528  493 PHE A CD2 
7430  C CE1 . PHE A 493 ? 1.1548 1.0876 1.2794 -0.1075 -0.1705 0.1957  493 PHE A CE1 
7431  C CE2 . PHE A 493 ? 1.0946 1.0634 1.2390 -0.1051 -0.1486 0.1599  493 PHE A CE2 
7432  C CZ  . PHE A 493 ? 1.1174 1.0705 1.2346 -0.1162 -0.1588 0.1791  493 PHE A CZ  
7442  N N   . GLN A 494 ? 1.2258 1.2409 1.5500 0.0102  -0.1674 0.1010  494 GLN A N   
7443  C CA  . GLN A 494 ? 1.2476 1.2706 1.6002 0.0331  -0.1611 0.0717  494 GLN A CA  
7444  C C   . GLN A 494 ? 1.1395 1.1519 1.4671 0.0132  -0.1390 0.0622  494 GLN A C   
7445  O O   . GLN A 494 ? 1.0760 1.1225 1.3849 -0.0036 -0.1256 0.0596  494 GLN A O   
7446  C CB  . GLN A 494 ? 1.3248 1.4275 1.7157 0.0551  -0.1611 0.0488  494 GLN A CB  
7447  C CG  . GLN A 494 ? 1.4326 1.5414 1.8651 0.0978  -0.1874 0.0388  494 GLN A CG  
7448  C CD  . GLN A 494 ? 1.4865 1.5994 1.9183 0.0993  -0.2111 0.0637  494 GLN A CD  
7449  O OE1 . GLN A 494 ? 1.4686 1.6482 1.9045 0.0836  -0.2073 0.0678  494 GLN A OE1 
7450  N NE2 . GLN A 494 ? 1.5109 1.5491 1.9329 0.1154  -0.2378 0.0811  494 GLN A NE2 
7459  N N   . VAL A 495 ? 1.1296 1.0924 1.4545 0.0140  -0.1380 0.0569  495 VAL A N   
7460  C CA  . VAL A 495 ? 1.0880 1.0419 1.3937 0.0005  -0.1225 0.0450  495 VAL A CA  
7461  C C   . VAL A 495 ? 1.1036 1.0664 1.4317 0.0215  -0.1199 0.0138  495 VAL A C   
7462  O O   . VAL A 495 ? 1.1455 1.0898 1.5012 0.0428  -0.1319 0.0027  495 VAL A O   
7463  C CB  . VAL A 495 ? 1.0540 0.9622 1.3434 -0.0189 -0.1215 0.0573  495 VAL A CB  
7464  C CG1 . VAL A 495 ? 1.0097 0.9197 1.2901 -0.0251 -0.1097 0.0377  495 VAL A CG1 
7465  C CG2 . VAL A 495 ? 1.0564 0.9612 1.3165 -0.0395 -0.1218 0.0842  495 VAL A CG2 
7475  N N   . GLU A 496 ? 1.1044 1.0888 1.4144 0.0167  -0.1074 -0.0011 496 GLU A N   
7476  C CA  . GLU A 496 ? 1.1476 1.1432 1.4684 0.0338  -0.1040 -0.0319 496 GLU A CA  
7477  C C   . GLU A 496 ? 1.1381 1.1164 1.4335 0.0232  -0.0992 -0.0406 496 GLU A C   
7478  O O   . GLU A 496 ? 1.1443 1.1228 1.4053 0.0080  -0.0948 -0.0286 496 GLU A O   
7479  C CB  . GLU A 496 ? 1.1945 1.2493 1.5145 0.0419  -0.0949 -0.0450 496 GLU A CB  
7480  C CG  . GLU A 496 ? 1.2270 1.3121 1.5901 0.0723  -0.1011 -0.0653 496 GLU A CG  
7481  C CD  . GLU A 496 ? 1.2700 1.4340 1.6352 0.0759  -0.0871 -0.0817 496 GLU A CD  
7482  O OE1 . GLU A 496 ? 1.2935 1.4744 1.6188 0.0531  -0.0726 -0.0794 496 GLU A OE1 
7483  O OE2 . GLU A 496 ? 1.2999 1.5100 1.7046 0.1010  -0.0915 -0.0976 496 GLU A OE2 
7490  N N   . LEU A 497 ? 1.0859 1.0476 1.3982 0.0334  -0.1035 -0.0640 497 LEU A N   
7491  C CA  . LEU A 497 ? 1.0918 1.0472 1.3885 0.0286  -0.1031 -0.0790 497 LEU A CA  
7492  C C   . LEU A 497 ? 1.1054 1.0793 1.3981 0.0462  -0.1031 -0.1095 497 LEU A C   
7493  O O   . LEU A 497 ? 1.1415 1.1211 1.4584 0.0633  -0.1053 -0.1272 497 LEU A O   
7494  C CB  . LEU A 497 ? 1.1198 1.0463 1.4394 0.0176  -0.1087 -0.0822 497 LEU A CB  
7495  C CG  . LEU A 497 ? 1.1499 1.0630 1.4654 -0.0047 -0.1059 -0.0549 497 LEU A CG  
7496  C CD1 . LEU A 497 ? 1.1713 1.0588 1.5107 -0.0220 -0.1094 -0.0582 497 LEU A CD1 
7497  C CD2 . LEU A 497 ? 1.1588 1.0896 1.4454 -0.0109 -0.1009 -0.0521 497 LEU A CD2 
7509  N N   . LEU A 498 ? 1.0796 1.0603 1.3377 0.0449  -0.1031 -0.1175 498 LEU A N   
7510  C CA  . LEU A 498 ? 1.0795 1.0769 1.3204 0.0589  -0.1040 -0.1446 498 LEU A CA  
7511  C C   . LEU A 498 ? 1.0623 1.0487 1.2857 0.0606  -0.1153 -0.1594 498 LEU A C   
7512  O O   . LEU A 498 ? 1.0537 1.0315 1.2415 0.0554  -0.1193 -0.1461 498 LEU A O   
7513  C CB  . LEU A 498 ? 1.0994 1.1238 1.2978 0.0547  -0.0935 -0.1352 498 LEU A CB  
7514  C CG  . LEU A 498 ? 1.1430 1.1839 1.3036 0.0630  -0.0930 -0.1581 498 LEU A CG  
7515  C CD1 . LEU A 498 ? 1.1785 1.2376 1.3756 0.0844  -0.0933 -0.1940 498 LEU A CD1 
7516  C CD2 . LEU A 498 ? 1.1322 1.1993 1.2436 0.0469  -0.0796 -0.1425 498 LEU A CD2 
7528  N N   . LEU A 499 ? 1.0839 1.0697 1.3320 0.0700  -0.1236 -0.1897 499 LEU A N   
7529  C CA  . LEU A 499 ? 1.0902 1.0776 1.3294 0.0740  -0.1375 -0.2098 499 LEU A CA  
7530  C C   . LEU A 499 ? 1.1425 1.1388 1.3262 0.0871  -0.1430 -0.2211 499 LEU A C   
7531  O O   . LEU A 499 ? 1.1255 1.1346 1.2923 0.0930  -0.1346 -0.2285 499 LEU A O   
7532  C CB  . LEU A 499 ? 1.0617 1.0457 1.3472 0.0731  -0.1461 -0.2391 499 LEU A CB  
7533  C CG  . LEU A 499 ? 1.0595 1.0227 1.3907 0.0542  -0.1422 -0.2266 499 LEU A CG  
7534  C CD1 . LEU A 499 ? 1.0990 1.0454 1.4655 0.0489  -0.1529 -0.2560 499 LEU A CD1 
7535  C CD2 . LEU A 499 ? 1.0316 1.0028 1.3688 0.0359  -0.1392 -0.2074 499 LEU A CD2 
7547  N N   . ASP A 500 ? 1.2081 1.1990 1.3603 0.0928  -0.1585 -0.2234 500 ASP A N   
7548  C CA  . ASP A 500 ? 1.3015 1.2881 1.3887 0.1050  -0.1706 -0.2312 500 ASP A CA  
7549  C C   . ASP A 500 ? 1.3677 1.3474 1.3986 0.0942  -0.1559 -0.2058 500 ASP A C   
7550  O O   . ASP A 500 ? 1.4063 1.4009 1.4047 0.0957  -0.1499 -0.2164 500 ASP A O   
7551  C CB  . ASP A 500 ? 1.3277 1.3319 1.4249 0.1175  -0.1795 -0.2695 500 ASP A CB  
7552  C CG  . ASP A 500 ? 1.3868 1.3856 1.4273 0.1335  -0.2042 -0.2835 500 ASP A CG  
7553  O OD1 . ASP A 500 ? 1.3803 1.3579 1.3846 0.1390  -0.2191 -0.2672 500 ASP A OD1 
7554  O OD2 . ASP A 500 ? 1.4037 1.4158 1.4321 0.1433  -0.2117 -0.3125 500 ASP A OD2 
7559  N N   . LYS A 501 ? 1.3976 1.3594 1.4154 0.0801  -0.1494 -0.1735 501 LYS A N   
7560  C CA  . LYS A 501 ? 1.4457 1.4054 1.4130 0.0612  -0.1350 -0.1484 501 LYS A CA  
7561  C C   . LYS A 501 ? 1.5172 1.4471 1.3924 0.0588  -0.1484 -0.1415 501 LYS A C   
7562  O O   . LYS A 501 ? 1.5399 1.4806 1.3673 0.0394  -0.1341 -0.1300 501 LYS A O   
7563  C CB  . LYS A 501 ? 1.4461 1.3890 1.4177 0.0438  -0.1286 -0.1170 501 LYS A CB  
7564  C CG  . LYS A 501 ? 1.5000 1.4473 1.4244 0.0167  -0.1137 -0.0918 501 LYS A CG  
7565  C CD  . LYS A 501 ? 1.5196 1.4515 1.4496 -0.0021 -0.1098 -0.0636 501 LYS A CD  
7566  C CE  . LYS A 501 ? 1.6131 1.5559 1.4976 -0.0358 -0.0958 -0.0407 501 LYS A CE  
7567  N NZ  . LYS A 501 ? 1.6706 1.5985 1.5586 -0.0564 -0.0947 -0.0153 501 LYS A NZ  
7581  N N   . LEU A 502 ? 1.5771 1.4716 1.4235 0.0775  -0.1766 -0.1485 502 LEU A N   
7582  C CA  . LEU A 502 ? 1.7033 1.5518 1.4497 0.0774  -0.1965 -0.1372 502 LEU A CA  
7583  C C   . LEU A 502 ? 1.7464 1.6214 1.4545 0.0713  -0.1868 -0.1497 502 LEU A C   
7584  O O   . LEU A 502 ? 1.7872 1.6396 1.4100 0.0484  -0.1830 -0.1277 502 LEU A O   
7585  C CB  . LEU A 502 ? 1.7528 1.5693 1.4857 0.1098  -0.2340 -0.1524 502 LEU A CB  
7586  C CG  . LEU A 502 ? 1.7667 1.5452 1.5022 0.1195  -0.2502 -0.1399 502 LEU A CG  
7587  C CD1 . LEU A 502 ? 1.8332 1.5823 1.5373 0.1574  -0.2923 -0.1585 502 LEU A CD1 
7588  C CD2 . LEU A 502 ? 1.7860 1.5098 1.4559 0.0919  -0.2444 -0.1004 502 LEU A CD2 
7600  N N   . LYS A 503 ? 1.7355 1.6573 1.5012 0.0884  -0.1825 -0.1857 503 LYS A N   
7601  C CA  . LYS A 503 ? 1.7938 1.7498 1.5294 0.0854  -0.1703 -0.2042 503 LYS A CA  
7602  C C   . LYS A 503 ? 1.8924 1.8894 1.6334 0.0586  -0.1341 -0.1910 503 LYS A C   
7603  O O   . LYS A 503 ? 1.8956 1.9161 1.7074 0.0551  -0.1179 -0.1870 503 LYS A O   
7604  C CB  . LYS A 503 ? 1.6871 1.6790 1.4898 0.1100  -0.1752 -0.2494 503 LYS A CB  
7605  C CG  . LYS A 503 ? 1.6509 1.6211 1.4568 0.1341  -0.2111 -0.2686 503 LYS A CG  
7606  C CD  . LYS A 503 ? 1.7204 1.6511 1.4207 0.1397  -0.2373 -0.2580 503 LYS A CD  
7607  C CE  . LYS A 503 ? 1.7432 1.6808 1.4435 0.1678  -0.2705 -0.2948 503 LYS A CE  
7608  N NZ  . LYS A 503 ? 1.8409 1.7357 1.4262 0.1750  -0.2987 -0.2836 503 LYS A NZ  
7622  N N   . GLN A 504 ? 2.0139 2.0241 1.6775 0.0388  -0.1222 -0.1846 504 GLN A N   
7623  C CA  . GLN A 504 ? 2.0114 2.0748 1.6711 0.0083  -0.0870 -0.1734 504 GLN A CA  
7624  C C   . GLN A 504 ? 1.9407 2.0794 1.6193 0.0199  -0.0665 -0.2144 504 GLN A C   
7625  O O   . GLN A 504 ? 1.9172 2.0584 1.6214 0.0515  -0.0805 -0.2508 504 GLN A O   
7626  C CB  . GLN A 504 ? 2.1302 2.1528 1.6805 -0.0334 -0.0865 -0.1315 504 GLN A CB  
7627  C CG  . GLN A 504 ? 2.1324 2.0671 1.6566 -0.0369 -0.1138 -0.0974 504 GLN A CG  
7628  C CD  . GLN A 504 ? 2.2192 2.1105 1.6521 -0.0859 -0.1094 -0.0531 504 GLN A CD  
7629  O OE1 . GLN A 504 ? 2.3160 2.1960 1.6524 -0.1150 -0.1054 -0.0398 504 GLN A OE1 
7630  N NE2 . GLN A 504 ? 2.2055 2.0692 1.6631 -0.0993 -0.1106 -0.0295 504 GLN A NE2 
7639  N N   . LYS A 505 ? 1.8655 2.0713 1.5341 -0.0058 -0.0332 -0.2125 505 LYS A N   
7640  C CA  . LYS A 505 ? 1.8261 2.1147 1.5152 0.0090  -0.0113 -0.2572 505 LYS A CA  
7641  C C   . LYS A 505 ? 1.8484 2.1185 1.4620 0.0188  -0.0257 -0.2774 505 LYS A C   
7642  O O   . LYS A 505 ? 1.8387 2.0581 1.3503 -0.0056 -0.0383 -0.2476 505 LYS A O   
7643  C CB  . LYS A 505 ? 1.8489 2.2241 1.5222 -0.0265 0.0277  -0.2511 505 LYS A CB  
7644  C CG  . LYS A 505 ? 1.7765 2.1932 1.5335 -0.0318 0.0426  -0.2409 505 LYS A CG  
7645  C CD  . LYS A 505 ? 1.7776 2.3201 1.5596 -0.0429 0.0811  -0.2665 505 LYS A CD  
7646  C CE  . LYS A 505 ? 1.7411 2.3276 1.5610 -0.0739 0.0974  -0.2396 505 LYS A CE  
7647  N NZ  . LYS A 505 ? 1.7980 2.3693 1.5213 -0.1413 0.1090  -0.1936 505 LYS A NZ  
7661  N N   . GLY A 506 ? 1.8389 2.1436 1.4980 0.0554  -0.0275 -0.3288 506 GLY A N   
7662  C CA  . GLY A 506 ? 1.9014 2.1949 1.4960 0.0682  -0.0433 -0.3549 506 GLY A CA  
7663  C C   . GLY A 506 ? 1.8505 2.0640 1.4394 0.0889  -0.0867 -0.3527 506 GLY A C   
7664  O O   . GLY A 506 ? 1.9012 2.0973 1.4226 0.0967  -0.1064 -0.3674 506 GLY A O   
7668  N N   . ALA A 507 ? 1.7385 1.9106 1.3961 0.0978  -0.1025 -0.3371 507 ALA A N   
7669  C CA  . ALA A 507 ? 1.6884 1.8012 1.3521 0.1162  -0.1416 -0.3375 507 ALA A CA  
7670  C C   . ALA A 507 ? 1.5994 1.7147 1.3764 0.1372  -0.1477 -0.3615 507 ALA A C   
7671  O O   . ALA A 507 ? 1.5167 1.6476 1.3575 0.1325  -0.1283 -0.3526 507 ALA A O   
7672  C CB  . ALA A 507 ? 1.6923 1.7431 1.3059 0.0996  -0.1580 -0.2879 507 ALA A CB  
7678  N N   . ILE A 508 ? 1.6331 1.7317 1.4309 0.1575  -0.1767 -0.3908 508 ILE A N   
7679  C CA  . ILE A 508 ? 1.6986 1.7984 1.5941 0.1703  -0.1829 -0.4186 508 ILE A CA  
7680  C C   . ILE A 508 ? 1.7858 1.8586 1.7326 0.1611  -0.1870 -0.3872 508 ILE A C   
7681  O O   . ILE A 508 ? 1.8942 1.9417 1.8076 0.1576  -0.2028 -0.3619 508 ILE A O   
7682  C CB  . ILE A 508 ? 1.6872 1.7841 1.5867 0.1872  -0.2131 -0.4612 508 ILE A CB  
7683  C CG1 . ILE A 508 ? 1.7244 1.8460 1.5545 0.1964  -0.2120 -0.4912 508 ILE A CG1 
7684  C CG2 . ILE A 508 ? 1.6385 1.7320 1.6316 0.1920  -0.2173 -0.4917 508 ILE A CG2 
7685  C CD1 . ILE A 508 ? 1.7487 1.8657 1.5624 0.2115  -0.2476 -0.5284 508 ILE A CD1 
7697  N N   . ARG A 509 ? 1.7468 1.8216 1.7708 0.1592  -0.1751 -0.3905 509 ARG A N   
7698  C CA  . ARG A 509 ? 1.7335 1.7866 1.8087 0.1485  -0.1778 -0.3656 509 ARG A CA  
7699  C C   . ARG A 509 ? 1.6264 1.6721 1.7547 0.1509  -0.1992 -0.3942 509 ARG A C   
7700  O O   . ARG A 509 ? 1.6196 1.6629 1.7888 0.1543  -0.2005 -0.4245 509 ARG A O   
7701  C CB  . ARG A 509 ? 1.7651 1.8202 1.8859 0.1414  -0.1554 -0.3485 509 ARG A CB  
7702  C CG  . ARG A 509 ? 1.7666 1.8534 1.8570 0.1424  -0.1320 -0.3433 509 ARG A CG  
7703  C CD  . ARG A 509 ? 1.7649 1.8534 1.7837 0.1252  -0.1249 -0.3079 509 ARG A CD  
7704  N NE  . ARG A 509 ? 1.7058 1.7827 1.7403 0.1082  -0.1153 -0.2683 509 ARG A NE  
7705  C CZ  . ARG A 509 ? 1.7096 1.8144 1.7373 0.0944  -0.0935 -0.2490 509 ARG A CZ  
7706  N NH1 . ARG A 509 ? 1.6753 1.7660 1.7168 0.0788  -0.0893 -0.2152 509 ARG A NH1 
7707  N NH2 . ARG A 509 ? 1.7556 1.9099 1.7635 0.0952  -0.0756 -0.2659 509 ARG A NH2 
7721  N N   . ARG A 510 ? 1.5465 1.5896 1.6745 0.1487  -0.2171 -0.3869 510 ARG A N   
7722  C CA  . ARG A 510 ? 1.4894 1.5426 1.6683 0.1462  -0.2372 -0.4172 510 ARG A CA  
7723  C C   . ARG A 510 ? 1.4147 1.4585 1.6663 0.1244  -0.2266 -0.4106 510 ARG A C   
7724  O O   . ARG A 510 ? 1.4554 1.4992 1.7520 0.1136  -0.2366 -0.4393 510 ARG A O   
7725  C CB  . ARG A 510 ? 1.4639 1.5312 1.6239 0.1553  -0.2607 -0.4160 510 ARG A CB  
7726  C CG  . ARG A 510 ? 1.4358 1.5004 1.5153 0.1769  -0.2800 -0.4239 510 ARG A CG  
7727  C CD  . ARG A 510 ? 1.3554 1.4131 1.3963 0.1923  -0.3029 -0.4079 510 ARG A CD  
7728  N NE  . ARG A 510 ? 1.2554 1.2837 1.2715 0.1845  -0.2859 -0.3639 510 ARG A NE  
7729  C CZ  . ARG A 510 ? 1.2550 1.2543 1.2131 0.1982  -0.3035 -0.3424 510 ARG A CZ  
7730  N NH1 . ARG A 510 ? 1.2909 1.2868 1.2085 0.2247  -0.3406 -0.3596 510 ARG A NH1 
7731  N NH2 . ARG A 510 ? 1.2350 1.2036 1.1722 0.1869  -0.2876 -0.3048 510 ARG A NH2 
7745  N N   . ALA A 511 ? 1.3158 1.3474 1.5743 0.1142  -0.2082 -0.3727 511 ALA A N   
7746  C CA  . ALA A 511 ? 1.2201 1.2384 1.5348 0.0910  -0.1991 -0.3598 511 ALA A CA  
7747  C C   . ALA A 511 ? 1.2025 1.1909 1.5278 0.0910  -0.1849 -0.3503 511 ALA A C   
7748  O O   . ALA A 511 ? 1.2228 1.2144 1.5166 0.1042  -0.1726 -0.3357 511 ALA A O   
7749  C CB  . ALA A 511 ? 1.1381 1.1646 1.4533 0.0813  -0.1916 -0.3267 511 ALA A CB  
7755  N N   . LEU A 512 ? 1.1736 1.1333 1.5426 0.0752  -0.1886 -0.3595 512 LEU A N   
7756  C CA  . LEU A 512 ? 1.1763 1.0972 1.5585 0.0801  -0.1831 -0.3531 512 LEU A CA  
7757  C C   . LEU A 512 ? 1.1838 1.0669 1.6001 0.0497  -0.1832 -0.3306 512 LEU A C   
7758  O O   . LEU A 512 ? 1.1818 1.0688 1.6198 0.0213  -0.1891 -0.3362 512 LEU A O   
7759  C CB  . LEU A 512 ? 1.2219 1.1231 1.6070 0.0986  -0.1957 -0.3965 512 LEU A CB  
7760  C CG  . LEU A 512 ? 1.2229 1.1627 1.5689 0.1249  -0.1963 -0.4254 512 LEU A CG  
7761  C CD1 . LEU A 512 ? 1.3031 1.2208 1.6562 0.1395  -0.2118 -0.4747 512 LEU A CD1 
7762  C CD2 . LEU A 512 ? 1.1638 1.1324 1.4783 0.1435  -0.1766 -0.4064 512 LEU A CD2 
7774  N N   . PHE A 513 ? 1.2313 1.0824 1.6504 0.0540  -0.1773 -0.3056 513 PHE A N   
7775  C CA  . PHE A 513 ? 1.3011 1.1057 1.7394 0.0245  -0.1792 -0.2792 513 PHE A CA  
7776  C C   . PHE A 513 ? 1.4345 1.1754 1.8901 0.0128  -0.1985 -0.3028 513 PHE A C   
7777  O O   . PHE A 513 ? 1.4718 1.1909 1.9256 0.0411  -0.2107 -0.3353 513 PHE A O   
7778  C CB  . PHE A 513 ? 1.2794 1.0672 1.7100 0.0365  -0.1723 -0.2450 513 PHE A CB  
7779  C CG  . PHE A 513 ? 1.2005 1.0337 1.6145 0.0312  -0.1552 -0.2138 513 PHE A CG  
7780  C CD1 . PHE A 513 ? 1.1871 1.0290 1.6034 -0.0008 -0.1484 -0.1925 513 PHE A CD1 
7781  C CD2 . PHE A 513 ? 1.1595 1.0281 1.5538 0.0559  -0.1459 -0.2081 513 PHE A CD2 
7782  C CE1 . PHE A 513 ? 1.1285 1.0047 1.5261 -0.0023 -0.1357 -0.1684 513 PHE A CE1 
7783  C CE2 . PHE A 513 ? 1.1031 1.0010 1.4767 0.0478  -0.1336 -0.1801 513 PHE A CE2 
7784  C CZ  . PHE A 513 ? 1.0898 0.9870 1.4641 0.0216  -0.1301 -0.1613 513 PHE A CZ  
7794  N N   . LEU A 514 ? 1.5609 1.2706 2.0298 -0.0318 -0.2013 -0.2870 514 LEU A N   
7795  C CA  . LEU A 514 ? 1.6491 1.2933 2.1295 -0.0565 -0.2211 -0.3084 514 LEU A CA  
7796  C C   . LEU A 514 ? 1.7350 1.2911 2.2048 -0.0298 -0.2400 -0.3108 514 LEU A C   
7797  O O   . LEU A 514 ? 1.8221 1.3465 2.2925 -0.0062 -0.2577 -0.3511 514 LEU A O   
7798  C CB  . LEU A 514 ? 1.6682 1.2993 2.1588 -0.1184 -0.2162 -0.2836 514 LEU A CB  
7799  C CG  . LEU A 514 ? 1.7532 1.3357 2.2569 -0.1615 -0.2339 -0.3079 514 LEU A CG  
7800  C CD1 . LEU A 514 ? 1.7358 1.3893 2.2617 -0.1586 -0.2375 -0.3547 514 LEU A CD1 
7801  C CD2 . LEU A 514 ? 1.7879 1.3544 2.2942 -0.2294 -0.2250 -0.2750 514 LEU A CD2 
7813  N N   . TYR A 515 ? 1.7593 1.2747 2.2178 -0.0295 -0.2393 -0.2706 515 TYR A N   
7814  C CA  . TYR A 515 ? 1.8650 1.2909 2.3137 -0.0001 -0.2636 -0.2721 515 TYR A CA  
7815  C C   . TYR A 515 ? 1.8444 1.3064 2.2979 0.0646  -0.2658 -0.3079 515 TYR A C   
7816  O O   . TYR A 515 ? 1.9715 1.3853 2.4262 0.0925  -0.2873 -0.3474 515 TYR A O   
7817  C CB  . TYR A 515 ? 1.9048 1.2933 2.3378 -0.0087 -0.2637 -0.2202 515 TYR A CB  
7818  C CG  . TYR A 515 ? 1.9739 1.2821 2.3896 -0.0696 -0.2728 -0.1888 515 TYR A CG  
7819  C CD1 . TYR A 515 ? 1.9212 1.2789 2.3420 -0.1272 -0.2508 -0.1738 515 TYR A CD1 
7820  C CD2 . TYR A 515 ? 2.0777 1.2607 2.4687 -0.0700 -0.3045 -0.1751 515 TYR A CD2 
7821  C CE1 . TYR A 515 ? 1.9887 1.2840 2.3915 -0.1907 -0.2547 -0.1453 515 TYR A CE1 
7822  C CE2 . TYR A 515 ? 2.1484 1.2504 2.5125 -0.1341 -0.3126 -0.1419 515 TYR A CE2 
7823  C CZ  . TYR A 515 ? 2.1265 1.2903 2.4971 -0.1980 -0.2849 -0.1267 515 TYR A CZ  
7824  O OH  . TYR A 515 ? 2.2464 1.3403 2.5880 -0.2693 -0.2887 -0.0938 515 TYR A OH  
7834  N N   . SER A 516 ? 1.7032 1.2519 2.1571 0.0867  -0.2431 -0.2965 516 SER A N   
7835  C CA  . SER A 516 ? 1.6216 1.2157 2.0788 0.1417  -0.2406 -0.3252 516 SER A CA  
7836  C C   . SER A 516 ? 1.5830 1.2197 2.0377 0.1563  -0.2374 -0.3744 516 SER A C   
7837  O O   . SER A 516 ? 1.6425 1.2962 2.0987 0.2005  -0.2416 -0.4120 516 SER A O   
7838  C CB  . SER A 516 ? 1.5229 1.1954 1.9764 0.1493  -0.2168 -0.2953 516 SER A CB  
7839  O OG  . SER A 516 ? 1.5011 1.2446 1.9544 0.1875  -0.2056 -0.3251 516 SER A OG  
7845  N N   . ARG A 517 ? 1.5201 1.1805 1.9706 0.1223  -0.2311 -0.3777 517 ARG A N   
7846  C CA  . ARG A 517 ? 1.5133 1.2230 1.9537 0.1352  -0.2287 -0.4195 517 ARG A CA  
7847  C C   . ARG A 517 ? 1.4550 1.2468 1.8759 0.1642  -0.2072 -0.4197 517 ARG A C   
7848  O O   . ARG A 517 ? 1.4505 1.2763 1.8567 0.1914  -0.2058 -0.4583 517 ARG A O   
7849  C CB  . ARG A 517 ? 1.6088 1.2658 2.0527 0.1566  -0.2522 -0.4708 517 ARG A CB  
7850  C CG  . ARG A 517 ? 1.6739 1.2373 2.1297 0.1210  -0.2766 -0.4727 517 ARG A CG  
7851  C CD  . ARG A 517 ? 1.7376 1.2453 2.1905 0.1451  -0.3026 -0.5291 517 ARG A CD  
7852  N NE  . ARG A 517 ? 1.8040 1.2025 2.2613 0.1094  -0.3300 -0.5302 517 ARG A NE  
7853  C CZ  . ARG A 517 ? 1.8893 1.2121 2.3408 0.1223  -0.3591 -0.5768 517 ARG A CZ  
7854  N NH1 . ARG A 517 ? 1.9829 1.1967 2.4316 0.0804  -0.3849 -0.5718 517 ARG A NH1 
7855  N NH2 . ARG A 517 ? 1.8805 1.2346 2.3243 0.1744  -0.3625 -0.6292 517 ARG A NH2 
7869  N N   . SER A 518 ? 1.4062 1.2290 1.8225 0.1546  -0.1901 -0.3766 518 SER A N   
7870  C CA  . SER A 518 ? 1.3419 1.2372 1.7345 0.1687  -0.1692 -0.3687 518 SER A CA  
7871  C C   . SER A 518 ? 1.2868 1.2008 1.6663 0.1394  -0.1569 -0.3239 518 SER A C   
7872  O O   . SER A 518 ? 1.3130 1.1910 1.7088 0.1161  -0.1612 -0.2968 518 SER A O   
7873  C CB  . SER A 518 ? 1.3295 1.2448 1.7343 0.2002  -0.1636 -0.3711 518 SER A CB  
7874  O OG  . SER A 518 ? 1.2960 1.1936 1.7152 0.1893  -0.1627 -0.3289 518 SER A OG  
7880  N N   . PRO A 519 ? 1.2481 1.2131 1.5926 0.1389  -0.1427 -0.3157 519 PRO A N   
7881  C CA  . PRO A 519 ? 1.2741 1.2468 1.6001 0.1151  -0.1361 -0.2792 519 PRO A CA  
7882  C C   . PRO A 519 ? 1.2784 1.2560 1.6074 0.1077  -0.1250 -0.2411 519 PRO A C   
7883  O O   . PRO A 519 ? 1.2771 1.2550 1.5898 0.0892  -0.1209 -0.2125 519 PRO A O   
7884  C CB  . PRO A 519 ? 1.2667 1.2752 1.5427 0.1194  -0.1316 -0.2877 519 PRO A CB  
7885  C CG  . PRO A 519 ? 1.2732 1.3137 1.5397 0.1402  -0.1222 -0.3109 519 PRO A CG  
7886  C CD  . PRO A 519 ? 1.2592 1.2732 1.5723 0.1583  -0.1327 -0.3394 519 PRO A CD  
7894  N N   . SER A 520 ? 1.2788 1.2623 1.6283 0.1244  -0.1226 -0.2430 520 SER A N   
7895  C CA  . SER A 520 ? 1.2624 1.2561 1.6183 0.1190  -0.1158 -0.2098 520 SER A CA  
7896  C C   . SER A 520 ? 1.3025 1.2436 1.6915 0.1197  -0.1303 -0.1980 520 SER A C   
7897  O O   . SER A 520 ? 1.4020 1.3110 1.8130 0.1395  -0.1444 -0.2227 520 SER A O   
7898  C CB  . SER A 520 ? 1.2592 1.3124 1.6150 0.1376  -0.1039 -0.2204 520 SER A CB  
7899  O OG  . SER A 520 ? 1.2649 1.3140 1.6577 0.1700  -0.1142 -0.2475 520 SER A OG  
7905  N N   . HIS A 521 ? 1.2464 1.1719 1.6317 0.0976  -0.1288 -0.1605 521 HIS A N   
7906  C CA  . HIS A 521 ? 1.2309 1.1042 1.6340 0.0930  -0.1424 -0.1404 521 HIS A CA  
7907  C C   . HIS A 521 ? 1.2463 1.1398 1.6435 0.0880  -0.1381 -0.1065 521 HIS A C   
7908  O O   . HIS A 521 ? 1.2165 1.1330 1.5909 0.0666  -0.1258 -0.0862 521 HIS A O   
7909  C CB  . HIS A 521 ? 1.1432 0.9712 1.5434 0.0608  -0.1462 -0.1296 521 HIS A CB  
7910  C CG  . HIS A 521 ? 1.1538 0.9265 1.5562 0.0449  -0.1571 -0.0994 521 HIS A CG  
7911  N ND1 . HIS A 521 ? 1.1406 0.9192 1.5269 0.0220  -0.1494 -0.0633 521 HIS A ND1 
7912  C CD2 . HIS A 521 ? 1.2210 0.9241 1.6315 0.0479  -0.1775 -0.0990 521 HIS A CD2 
7913  C CE1 . HIS A 521 ? 1.1845 0.9044 1.5671 0.0098  -0.1629 -0.0402 521 HIS A CE1 
7914  N NE2 . HIS A 521 ? 1.2365 0.9046 1.6319 0.0246  -0.1814 -0.0594 521 HIS A NE2 
7922  N N   . SER A 522 ? 1.3347 1.2174 1.7512 0.1104  -0.1518 -0.1031 522 SER A N   
7923  C CA  . SER A 522 ? 1.3673 1.2733 1.7829 0.1091  -0.1529 -0.0747 522 SER A CA  
7924  C C   . SER A 522 ? 1.3890 1.2261 1.7991 0.0976  -0.1710 -0.0440 522 SER A C   
7925  O O   . SER A 522 ? 1.4571 1.2263 1.8673 0.0943  -0.1847 -0.0470 522 SER A O   
7926  C CB  . SER A 522 ? 1.4084 1.3698 1.8518 0.1463  -0.1572 -0.0956 522 SER A CB  
7927  O OG  . SER A 522 ? 1.4345 1.4541 1.8747 0.1360  -0.1487 -0.0756 522 SER A OG  
7933  N N   . LYS A 523 ? 1.3343 1.1863 1.7337 0.0875  -0.1720 -0.0133 523 LYS A N   
7934  C CA  . LYS A 523 ? 1.3401 1.1291 1.7212 0.0705  -0.1874 0.0208  523 LYS A CA  
7935  C C   . LYS A 523 ? 1.3339 1.1507 1.7049 0.0676  -0.1921 0.0488  523 LYS A C   
7936  O O   . LYS A 523 ? 1.2547 1.1202 1.6122 0.0485  -0.1743 0.0564  523 LYS A O   
7937  C CB  . LYS A 523 ? 1.3045 1.0639 1.6608 0.0286  -0.1732 0.0333  523 LYS A CB  
7938  C CG  . LYS A 523 ? 1.3251 1.0263 1.6534 0.0005  -0.1827 0.0699  523 LYS A CG  
7939  C CD  . LYS A 523 ? 1.3796 0.9956 1.7073 0.0057  -0.2075 0.0718  523 LYS A CD  
7940  C CE  . LYS A 523 ? 1.4106 0.9624 1.6986 -0.0258 -0.2190 0.1138  523 LYS A CE  
7941  N NZ  . LYS A 523 ? 1.5013 0.9515 1.7765 -0.0300 -0.2449 0.1190  523 LYS A NZ  
7955  N N   . ASN A 524 ? 1.4453 1.2250 1.8186 0.0871  -0.2200 0.0636  524 ASN A N   
7956  C CA  . ASN A 524 ? 1.4479 1.2398 1.8042 0.0797  -0.2301 0.0946  524 ASN A CA  
7957  C C   . ASN A 524 ? 1.5099 1.2439 1.8193 0.0374  -0.2268 0.1300  524 ASN A C   
7958  O O   . ASN A 524 ? 1.5769 1.2436 1.8708 0.0210  -0.2294 0.1357  524 ASN A O   
7959  C CB  . ASN A 524 ? 1.5174 1.2931 1.8922 0.1222  -0.2667 0.0956  524 ASN A CB  
7960  C CG  . ASN A 524 ? 1.5343 1.3889 1.9612 0.1661  -0.2681 0.0556  524 ASN A CG  
7961  O OD1 . ASN A 524 ? 1.4713 1.4038 1.9130 0.1565  -0.2399 0.0362  524 ASN A OD1 
7962  N ND2 . ASN A 524 ? 1.6357 1.4704 2.0870 0.2149  -0.3020 0.0424  524 ASN A ND2 
7969  N N   . MET A 525 ? 1.5322 1.2965 1.8176 0.0166  -0.2202 0.1520  525 MET A N   
7970  C CA  . MET A 525 ? 1.5646 1.2909 1.8031 -0.0233 -0.2133 0.1820  525 MET A CA  
7971  C C   . MET A 525 ? 1.6256 1.3618 1.8376 -0.0268 -0.2285 0.2095  525 MET A C   
7972  O O   . MET A 525 ? 1.6793 1.4721 1.9122 -0.0076 -0.2352 0.2016  525 MET A O   
7973  C CB  . MET A 525 ? 1.4985 1.2592 1.7272 -0.0522 -0.1803 0.1706  525 MET A CB  
7974  C CG  . MET A 525 ? 1.5127 1.2480 1.7493 -0.0658 -0.1673 0.1551  525 MET A CG  
7975  S SD  . MET A 525 ? 1.4627 1.2431 1.6844 -0.0941 -0.1357 0.1433  525 MET A SD  
7976  C CE  . MET A 525 ? 1.5015 1.2543 1.6779 -0.1355 -0.1305 0.1751  525 MET A CE  
7986  N N   . THR A 526 ? 1.6518 1.3369 1.8153 -0.0555 -0.2332 0.2411  526 THR A N   
7987  C CA  . THR A 526 ? 1.6818 1.3691 1.8080 -0.0638 -0.2482 0.2693  526 THR A CA  
7988  C C   . THR A 526 ? 1.6498 1.3411 1.7291 -0.1083 -0.2225 0.2822  526 THR A C   
7989  O O   . THR A 526 ? 1.6627 1.3160 1.7190 -0.1370 -0.2089 0.2904  526 THR A O   
7990  C CB  . THR A 526 ? 1.8039 1.4166 1.9043 -0.0502 -0.2874 0.2984  526 THR A CB  
7991  O OG1 . THR A 526 ? 1.7991 1.4188 1.9480 0.0008  -0.3144 0.2792  526 THR A OG1 
7992  C CG2 . THR A 526 ? 1.8639 1.4762 1.9158 -0.0621 -0.3044 0.3297  526 THR A CG2 
8000  N N   . ILE A 527 ? 1.6295 1.3699 1.6948 -0.1150 -0.2161 0.2811  527 ILE A N   
8001  C CA  . ILE A 527 ? 1.6111 1.3646 1.6335 -0.1493 -0.1925 0.2848  527 ILE A CA  
8002  C C   . ILE A 527 ? 1.6085 1.3719 1.5902 -0.1558 -0.2087 0.3045  527 ILE A C   
8003  O O   . ILE A 527 ? 1.5627 1.3565 1.5645 -0.1354 -0.2275 0.3005  527 ILE A O   
8004  C CB  . ILE A 527 ? 1.5517 1.3529 1.5964 -0.1496 -0.1653 0.2513  527 ILE A CB  
8005  C CG1 . ILE A 527 ? 1.5556 1.3460 1.6210 -0.1563 -0.1457 0.2352  527 ILE A CG1 
8006  C CG2 . ILE A 527 ? 1.5564 1.3813 1.5589 -0.1697 -0.1522 0.2489  527 ILE A CG2 
8007  C CD1 . ILE A 527 ? 1.5426 1.3666 1.6464 -0.1383 -0.1333 0.2018  527 ILE A CD1 
8019  N N   . SER A 528 ? 1.6287 1.3733 1.5526 -0.1869 -0.2006 0.3236  528 SER A N   
8020  C CA  . SER A 528 ? 1.6850 1.4345 1.5587 -0.1969 -0.2158 0.3424  528 SER A CA  
8021  C C   . SER A 528 ? 1.6181 1.4122 1.4722 -0.2113 -0.1927 0.3199  528 SER A C   
8022  O O   . SER A 528 ? 1.5807 1.3887 1.4351 -0.2240 -0.1627 0.3002  528 SER A O   
8023  C CB  . SER A 528 ? 1.7840 1.4796 1.5933 -0.2236 -0.2237 0.3796  528 SER A CB  
8024  O OG  . SER A 528 ? 1.7177 1.4037 1.5142 -0.2544 -0.1916 0.3767  528 SER A OG  
8030  N N   . ARG A 529 ? 1.5697 1.3857 1.4071 -0.2076 -0.2099 0.3200  529 ARG A N   
8031  C CA  . ARG A 529 ? 1.5180 1.3624 1.3285 -0.2195 -0.1949 0.2976  529 ARG A CA  
8032  C C   . ARG A 529 ? 1.5475 1.3876 1.3050 -0.2449 -0.1707 0.2977  529 ARG A C   
8033  O O   . ARG A 529 ? 1.6466 1.4640 1.3596 -0.2632 -0.1755 0.3262  529 ARG A O   
8034  C CB  . ARG A 529 ? 1.5260 1.3856 1.3142 -0.2198 -0.2220 0.3031  529 ARG A CB  
8035  C CG  . ARG A 529 ? 1.4849 1.3740 1.3271 -0.2022 -0.2387 0.2918  529 ARG A CG  
8036  C CD  . ARG A 529 ? 1.5109 1.4237 1.3285 -0.2125 -0.2604 0.2896  529 ARG A CD  
8037  N NE  . ARG A 529 ? 1.5730 1.4727 1.3408 -0.2195 -0.2832 0.3155  529 ARG A NE  
8038  C CZ  . ARG A 529 ? 1.6155 1.5052 1.3156 -0.2400 -0.2804 0.3159  529 ARG A CZ  
8039  N NH1 . ARG A 529 ? 1.6035 1.4941 1.2804 -0.2517 -0.2574 0.2884  529 ARG A NH1 
8040  N NH2 . ARG A 529 ? 1.6908 1.5676 1.3421 -0.2461 -0.3035 0.3424  529 ARG A NH2 
8054  N N   . GLY A 530 ? 1.4699 1.3336 1.2292 -0.2455 -0.1455 0.2647  530 GLY A N   
8055  C CA  . GLY A 530 ? 1.5171 1.3969 1.2353 -0.2656 -0.1192 0.2547  530 GLY A CA  
8056  C C   . GLY A 530 ? 1.5717 1.4493 1.3016 -0.2830 -0.0984 0.2650  530 GLY A C   
8057  O O   . GLY A 530 ? 1.6180 1.5195 1.3129 -0.3074 -0.0742 0.2603  530 GLY A O   
8061  N N   . GLY A 531 ? 1.5888 1.4415 1.3659 -0.2735 -0.1065 0.2767  531 GLY A N   
8062  C CA  . GLY A 531 ? 1.6232 1.4649 1.4108 -0.2944 -0.0901 0.2862  531 GLY A CA  
8063  C C   . GLY A 531 ? 1.5856 1.4725 1.4105 -0.2929 -0.0602 0.2474  531 GLY A C   
8064  O O   . GLY A 531 ? 1.5906 1.5070 1.4351 -0.2686 -0.0560 0.2137  531 GLY A O   
8068  N N   . LEU A 532 ? 1.6542 1.5435 1.4864 -0.3207 -0.0421 0.2527  532 LEU A N   
8069  C CA  . LEU A 532 ? 1.6728 1.6140 1.5469 -0.3209 -0.0159 0.2149  532 LEU A CA  
8070  C C   . LEU A 532 ? 1.7293 1.6555 1.6655 -0.2896 -0.0275 0.1991  532 LEU A C   
8071  O O   . LEU A 532 ? 1.8022 1.6784 1.7511 -0.2757 -0.0512 0.2197  532 LEU A O   
8072  C CB  . LEU A 532 ? 1.6992 1.6561 1.5613 -0.3698 0.0081  0.2255  532 LEU A CB  
8073  C CG  . LEU A 532 ? 1.7528 1.7405 1.5497 -0.4080 0.0278  0.2369  532 LEU A CG  
8074  C CD1 . LEU A 532 ? 1.8113 1.8027 1.5912 -0.4671 0.0494  0.2569  532 LEU A CD1 
8075  C CD2 . LEU A 532 ? 1.7100 1.7804 1.5105 -0.3896 0.0494  0.1889  532 LEU A CD2 
8087  N N   . MET A 533 ? 1.7489 1.7234 1.7226 -0.2760 -0.0118 0.1592  533 MET A N   
8088  C CA  . MET A 533 ? 1.7568 1.7225 1.7824 -0.2473 -0.0214 0.1407  533 MET A CA  
8089  C C   . MET A 533 ? 1.7095 1.6368 1.7586 -0.2645 -0.0269 0.1597  533 MET A C   
8090  O O   . MET A 533 ? 1.7534 1.7014 1.8174 -0.2929 -0.0106 0.1522  533 MET A O   
8091  C CB  . MET A 533 ? 1.8263 1.8508 1.8813 -0.2311 -0.0065 0.0950  533 MET A CB  
8092  C CG  . MET A 533 ? 1.8758 1.8899 1.9717 -0.1980 -0.0193 0.0749  533 MET A CG  
8093  S SD  . MET A 533 ? 1.9491 2.0237 2.0709 -0.1698 -0.0117 0.0215  533 MET A SD  
8094  C CE  . MET A 533 ? 1.9542 2.0156 2.0282 -0.1412 -0.0228 0.0115  533 MET A CE  
8104  N N   . GLN A 534 ? 2.0696 1.4226 1.8330 -0.3304 -0.0739 0.0723  534 GLN A N   
8105  C CA  . GLN A 534 ? 2.1640 1.4796 1.9429 -0.3278 -0.1168 0.0690  534 GLN A CA  
8106  C C   . GLN A 534 ? 2.0249 1.3952 1.8586 -0.2839 -0.1105 0.0417  534 GLN A C   
8107  O O   . GLN A 534 ? 2.0736 1.4850 1.9412 -0.2394 -0.1033 0.0293  534 GLN A O   
8108  C CB  . GLN A 534 ? 2.1721 1.4322 1.9474 -0.3148 -0.1608 0.0799  534 GLN A CB  
8109  C CG  . GLN A 534 ? 1.9974 1.2093 1.7892 -0.3027 -0.2148 0.0719  534 GLN A CG  
8110  C CD  . GLN A 534 ? 1.8202 0.9889 1.6179 -0.2807 -0.2583 0.0772  534 GLN A CD  
8111  O OE1 . GLN A 534 ? 1.7137 0.8848 1.5515 -0.2368 -0.2905 0.0559  534 GLN A OE1 
8112  N NE2 . GLN A 534 ? 1.7891 0.9214 1.5477 -0.3097 -0.2603 0.1032  534 GLN A NE2 
8121  N N   . CYS A 535 ? 1.8877 1.2599 1.7267 -0.3005 -0.1147 0.0340  535 CYS A N   
8122  C CA  . CYS A 535 ? 1.7895 1.2139 1.6741 -0.2665 -0.1052 0.0090  535 CYS A CA  
8123  C C   . CYS A 535 ? 1.7936 1.1762 1.6931 -0.2514 -0.1536 -0.0022 535 CYS A C   
8124  O O   . CYS A 535 ? 1.8500 1.1583 1.7233 -0.2716 -0.1976 0.0101  535 CYS A O   
8125  C CB  . CYS A 535 ? 1.8679 1.3361 1.7521 -0.2940 -0.0714 0.0056  535 CYS A CB  
8126  S SG  . CYS A 535 ? 1.8309 1.3632 1.7118 -0.2931 -0.0147 0.0035  535 CYS A SG  
8131  N N   . GLU A 536 ? 1.7435 1.1707 1.6829 -0.2152 -0.1486 -0.0271 536 GLU A N   
8132  C CA  . GLU A 536 ? 1.7741 1.1665 1.7273 -0.1979 -0.1924 -0.0440 536 GLU A CA  
8133  C C   . GLU A 536 ? 1.6920 1.1414 1.6773 -0.1790 -0.1725 -0.0654 536 GLU A C   
8134  O O   . GLU A 536 ? 1.6116 1.1314 1.6220 -0.1543 -0.1342 -0.0750 536 GLU A O   
8135  C CB  . GLU A 536 ? 1.8133 1.1907 1.7866 -0.1494 -0.2257 -0.0602 536 GLU A CB  
8136  C CG  . GLU A 536 ? 1.9233 1.2049 1.8700 -0.1641 -0.2855 -0.0512 536 GLU A CG  
8137  C CD  . GLU A 536 ? 1.9724 1.2471 1.9485 -0.1078 -0.3230 -0.0763 536 GLU A CD  
8138  O OE1 . GLU A 536 ? 2.0370 1.2418 1.9958 -0.1131 -0.3684 -0.0672 536 GLU A OE1 
8139  O OE2 . GLU A 536 ? 1.9510 1.2939 1.9676 -0.0588 -0.3083 -0.1062 536 GLU A OE2 
8146  N N   . GLU A 537 ? 1.7057 1.1186 1.6867 -0.1934 -0.2034 -0.0708 537 GLU A N   
8147  C CA  . GLU A 537 ? 1.6276 1.0834 1.6354 -0.1804 -0.1925 -0.0895 537 GLU A CA  
8148  C C   . GLU A 537 ? 1.5731 1.0040 1.5984 -0.1364 -0.2346 -0.1183 537 GLU A C   
8149  O O   . GLU A 537 ? 1.5996 0.9598 1.6100 -0.1294 -0.2843 -0.1215 537 GLU A O   
8150  C CB  . GLU A 537 ? 1.6692 1.1109 1.6578 -0.2362 -0.1941 -0.0732 537 GLU A CB  
8151  C CG  . GLU A 537 ? 1.6247 1.1239 1.6091 -0.2714 -0.1428 -0.0573 537 GLU A CG  
8152  C CD  . GLU A 537 ? 1.6670 1.1786 1.6451 -0.3204 -0.1415 -0.0478 537 GLU A CD  
8153  O OE1 . GLU A 537 ? 1.6641 1.1983 1.6687 -0.3061 -0.1469 -0.0632 537 GLU A OE1 
8154  O OE2 . GLU A 537 ? 1.7166 1.2186 1.6619 -0.3760 -0.1362 -0.0244 537 GLU A OE2 
8161  N N   . LEU A 538 ? 1.4676 0.9561 1.5236 -0.1057 -0.2168 -0.1413 538 LEU A N   
8162  C CA  . LEU A 538 ? 1.4586 0.9294 1.5278 -0.0686 -0.2535 -0.1723 538 LEU A CA  
8163  C C   . LEU A 538 ? 1.4081 0.9337 1.4975 -0.0661 -0.2289 -0.1833 538 LEU A C   
8164  O O   . LEU A 538 ? 1.3754 0.9546 1.4735 -0.0868 -0.1855 -0.1691 538 LEU A O   
8165  C CB  . LEU A 538 ? 1.4094 0.9039 1.4988 -0.0107 -0.2625 -0.1991 538 LEU A CB  
8166  C CG  . LEU A 538 ? 1.3192 0.9113 1.4395 0.0269  -0.2220 -0.2174 538 LEU A CG  
8167  C CD1 . LEU A 538 ? 1.2917 0.9035 1.4298 0.0807  -0.2437 -0.2489 538 LEU A CD1 
8168  C CD2 . LEU A 538 ? 1.2731 0.9160 1.3940 0.0073  -0.1732 -0.1915 538 LEU A CD2 
8180  N N   . ILE A 539 ? 1.4116 0.9212 1.5082 -0.0389 -0.2602 -0.2108 539 ILE A N   
8181  C CA  . ILE A 539 ? 1.4013 0.9453 1.5115 -0.0426 -0.2486 -0.2195 539 ILE A CA  
8182  C C   . ILE A 539 ? 1.3707 0.9582 1.5018 0.0127  -0.2492 -0.2568 539 ILE A C   
8183  O O   . ILE A 539 ? 1.4293 0.9915 1.5588 0.0517  -0.2818 -0.2834 539 ILE A O   
8184  C CB  . ILE A 539 ? 1.5106 0.9828 1.5984 -0.0802 -0.2915 -0.2111 539 ILE A CB  
8185  C CG1 . ILE A 539 ? 1.5073 0.9626 1.5747 -0.1445 -0.2801 -0.1718 539 ILE A CG1 
8186  C CG2 . ILE A 539 ? 1.5158 1.0193 1.6191 -0.0767 -0.2879 -0.2248 539 ILE A CG2 
8187  C CD1 . ILE A 539 ? 1.5475 0.9262 1.5836 -0.1934 -0.3285 -0.1554 539 ILE A CD1 
8199  N N   . ALA A 540 ? 1.3262 0.9817 1.4764 0.0160  -0.2148 -0.2603 540 ALA A N   
8200  C CA  . ALA A 540 ? 1.3285 1.0376 1.4941 0.0593  -0.2089 -0.2916 540 ALA A CA  
8201  C C   . ALA A 540 ? 1.3783 1.0976 1.5495 0.0477  -0.2100 -0.2967 540 ALA A C   
8202  O O   . ALA A 540 ? 1.4142 1.1059 1.5816 0.0072  -0.2140 -0.2759 540 ALA A O   
8203  C CB  . ALA A 540 ? 1.2498 1.0392 1.4302 0.0736  -0.1655 -0.2867 540 ALA A CB  
8209  N N   . TYR A 541 ? 1.4035 1.1686 1.5830 0.0808  -0.2063 -0.3240 541 TYR A N   
8210  C CA  . TYR A 541 ? 1.4372 1.2084 1.6198 0.0735  -0.2126 -0.3318 541 TYR A CA  
8211  C C   . TYR A 541 ? 1.4210 1.2683 1.6130 0.1018  -0.1901 -0.3511 541 TYR A C   
8212  O O   . TYR A 541 ? 1.3935 1.2910 1.5888 0.1231  -0.1697 -0.3565 541 TYR A O   
8213  C CB  . TYR A 541 ? 1.5168 1.2112 1.6801 0.0795  -0.2658 -0.3522 541 TYR A CB  
8214  C CG  . TYR A 541 ? 1.5535 1.2444 1.7083 0.1333  -0.2917 -0.3965 541 TYR A CG  
8215  C CD1 . TYR A 541 ? 1.5703 1.2358 1.7207 0.1594  -0.3100 -0.4094 541 TYR A CD1 
8216  C CD2 . TYR A 541 ? 1.5556 1.2721 1.7074 0.1590  -0.2993 -0.4280 541 TYR A CD2 
8217  C CE1 . TYR A 541 ? 1.6069 1.2803 1.7551 0.2136  -0.3340 -0.4560 541 TYR A CE1 
8218  C CE2 . TYR A 541 ? 1.5994 1.3231 1.7435 0.2109  -0.3212 -0.4744 541 TYR A CE2 
8219  C CZ  . TYR A 541 ? 1.6276 1.3332 1.7724 0.2399  -0.3381 -0.4900 541 TYR A CZ  
8220  O OH  . TYR A 541 ? 1.6896 1.4132 1.8323 0.2966  -0.3599 -0.5420 541 TYR A OH  
8230  N N   . LEU A 542 ? 1.4630 1.3197 1.6567 0.0971  -0.1958 -0.3590 542 LEU A N   
8231  C CA  . LEU A 542 ? 1.4586 1.3822 1.6552 0.1148  -0.1787 -0.3738 542 LEU A CA  
8232  C C   . LEU A 542 ? 1.5411 1.4525 1.7205 0.1460  -0.2091 -0.4143 542 LEU A C   
8233  O O   . LEU A 542 ? 1.6290 1.4709 1.7965 0.1464  -0.2470 -0.4262 542 LEU A O   
8234  C CB  . LEU A 542 ? 1.4049 1.3535 1.6169 0.0853  -0.1619 -0.3517 542 LEU A CB  
8235  C CG  . LEU A 542 ? 1.3553 1.3489 1.5844 0.0679  -0.1263 -0.3229 542 LEU A CG  
8236  C CD1 . LEU A 542 ? 1.3183 1.3299 1.5661 0.0462  -0.1213 -0.3102 542 LEU A CD1 
8237  C CD2 . LEU A 542 ? 1.3508 1.4016 1.5721 0.0879  -0.1074 -0.3278 542 LEU A CD2 
8249  N N   . ARG A 543 ? 1.5188 1.4983 1.6931 0.1697  -0.1944 -0.4353 543 ARG A N   
8250  C CA  . ARG A 543 ? 1.5895 1.5728 1.7452 0.2004  -0.2179 -0.4778 543 ARG A CA  
8251  C C   . ARG A 543 ? 1.6543 1.6171 1.8046 0.1794  -0.2306 -0.4736 543 ARG A C   
8252  O O   . ARG A 543 ? 1.7103 1.6720 1.8765 0.1437  -0.2173 -0.4391 543 ARG A O   
8253  C CB  . ARG A 543 ? 1.5525 1.6297 1.7019 0.2256  -0.1944 -0.4998 543 ARG A CB  
8254  C CG  . ARG A 543 ? 1.5063 1.6222 1.6643 0.2463  -0.1802 -0.5048 543 ARG A CG  
8255  C CD  . ARG A 543 ? 1.4371 1.6614 1.5877 0.2602  -0.1548 -0.5215 543 ARG A CD  
8256  N NE  . ARG A 543 ? 1.4188 1.6936 1.5793 0.2849  -0.1449 -0.5344 543 ARG A NE  
8257  C CZ  . ARG A 543 ? 1.4705 1.7752 1.6304 0.3309  -0.1600 -0.5840 543 ARG A CZ  
8258  N NH1 . ARG A 543 ? 1.4560 1.8151 1.6313 0.3508  -0.1498 -0.5924 543 ARG A NH1 
8259  N NH2 . ARG A 543 ? 1.5414 1.8232 1.6864 0.3589  -0.1871 -0.6273 543 ARG A NH2 
8273  N N   . ASP A 544 ? 1.7032 1.6525 1.8315 0.2042  -0.2579 -0.5118 544 ASP A N   
8274  C CA  . ASP A 544 ? 1.7260 1.6578 1.8456 0.1860  -0.2728 -0.5104 544 ASP A CA  
8275  C C   . ASP A 544 ? 1.7047 1.7146 1.8277 0.1712  -0.2409 -0.4964 544 ASP A C   
8276  O O   . ASP A 544 ? 1.6865 1.7677 1.8052 0.1840  -0.2150 -0.5027 544 ASP A O   
8277  C CB  . ASP A 544 ? 1.7875 1.6824 1.8763 0.2188  -0.3124 -0.5583 544 ASP A CB  
8278  C CG  . ASP A 544 ? 1.8302 1.6172 1.9101 0.2117  -0.3607 -0.5588 544 ASP A CG  
8279  O OD1 . ASP A 544 ? 1.8083 1.5552 1.9025 0.1927  -0.3634 -0.5318 544 ASP A OD1 
8280  O OD2 . ASP A 544 ? 1.8807 1.6207 1.9351 0.2213  -0.3986 -0.5845 544 ASP A OD2 
8285  N N   . GLU A 545 ? 1.6879 1.6836 1.8183 0.1412  -0.2470 -0.4756 545 GLU A N   
8286  C CA  . GLU A 545 ? 1.6454 1.7016 1.7788 0.1239  -0.2257 -0.4590 545 GLU A CA  
8287  C C   . GLU A 545 ? 1.6374 1.7500 1.7374 0.1460  -0.2221 -0.4910 545 GLU A C   
8288  O O   . GLU A 545 ? 1.5968 1.7752 1.6921 0.1370  -0.1982 -0.4788 545 GLU A O   
8289  C CB  . GLU A 545 ? 1.6963 1.7241 1.8425 0.0947  -0.2425 -0.4407 545 GLU A CB  
8290  C CG  . GLU A 545 ? 1.7340 1.7336 1.9179 0.0662  -0.2387 -0.4064 545 GLU A CG  
8291  C CD  . GLU A 545 ? 1.8198 1.8090 2.0226 0.0382  -0.2542 -0.3902 545 GLU A CD  
8292  O OE1 . GLU A 545 ? 1.8805 1.8569 2.0614 0.0411  -0.2781 -0.4076 545 GLU A OE1 
8293  O OE2 . GLU A 545 ? 1.8139 1.8120 2.0541 0.0141  -0.2429 -0.3620 545 GLU A OE2 
8300  N N   . SER A 546 ? 1.6475 1.7353 1.7205 0.1733  -0.2481 -0.5329 546 SER A N   
8301  C CA  . SER A 546 ? 1.6569 1.8057 1.6952 0.1941  -0.2446 -0.5689 546 SER A CA  
8302  C C   . SER A 546 ? 1.5643 1.7953 1.6009 0.2116  -0.2139 -0.5785 546 SER A C   
8303  O O   . SER A 546 ? 1.5051 1.8156 1.5182 0.2091  -0.1974 -0.5884 546 SER A O   
8304  C CB  . SER A 546 ? 1.8100 1.9110 1.8205 0.2278  -0.2811 -0.6186 546 SER A CB  
8305  O OG  . SER A 546 ? 1.8693 1.9175 1.8906 0.2545  -0.2981 -0.6343 546 SER A OG  
8311  N N   . GLU A 547 ? 1.5397 1.7560 1.5991 0.2253  -0.2074 -0.5739 547 GLU A N   
8312  C CA  . GLU A 547 ? 1.5145 1.8087 1.5741 0.2464  -0.1833 -0.5886 547 GLU A CA  
8313  C C   . GLU A 547 ? 1.4135 1.7725 1.4797 0.2126  -0.1499 -0.5462 547 GLU A C   
8314  O O   . GLU A 547 ? 1.3800 1.8269 1.4353 0.2186  -0.1292 -0.5559 547 GLU A O   
8315  C CB  . GLU A 547 ? 1.5458 1.7949 1.6262 0.2728  -0.1938 -0.5983 547 GLU A CB  
8316  C CG  . GLU A 547 ? 1.6099 1.7799 1.6797 0.3056  -0.2368 -0.6388 547 GLU A CG  
8317  C CD  . GLU A 547 ? 1.6244 1.7627 1.7081 0.3398  -0.2527 -0.6589 547 GLU A CD  
8318  O OE1 . GLU A 547 ? 1.5761 1.7630 1.6790 0.3394  -0.2267 -0.6431 547 GLU A OE1 
8319  O OE2 . GLU A 547 ? 1.6878 1.7477 1.7615 0.3663  -0.2958 -0.6898 547 GLU A OE2 
8326  N N   . PHE A 548 ? 1.3708 1.6912 1.4541 0.1771  -0.1466 -0.5007 548 PHE A N   
8327  C CA  . PHE A 548 ? 1.3199 1.6865 1.4064 0.1463  -0.1234 -0.4609 548 PHE A CA  
8328  C C   . PHE A 548 ? 1.3683 1.7096 1.4566 0.1138  -0.1321 -0.4324 548 PHE A C   
8329  O O   . PHE A 548 ? 1.3915 1.6689 1.5041 0.1058  -0.1438 -0.4189 548 PHE A O   
8330  C CB  . PHE A 548 ? 1.2364 1.5829 1.3499 0.1431  -0.1094 -0.4343 548 PHE A CB  
8331  C CG  . PHE A 548 ? 1.2098 1.4741 1.3503 0.1327  -0.1195 -0.4146 548 PHE A CG  
8332  C CD1 . PHE A 548 ? 1.2369 1.4415 1.3852 0.1513  -0.1375 -0.4337 548 PHE A CD1 
8333  C CD2 . PHE A 548 ? 1.1658 1.4156 1.3230 0.1032  -0.1132 -0.3775 548 PHE A CD2 
8334  C CE1 . PHE A 548 ? 1.2394 1.3782 1.4087 0.1337  -0.1462 -0.4126 548 PHE A CE1 
8335  C CE2 . PHE A 548 ? 1.1691 1.3608 1.3529 0.0922  -0.1188 -0.3620 548 PHE A CE2 
8336  C CZ  . PHE A 548 ? 1.2058 1.3454 1.3943 0.1040  -0.1337 -0.3777 548 PHE A CZ  
8346  N N   . ARG A 549 ? 1.4046 1.7997 1.4669 0.0931  -0.1287 -0.4233 549 ARG A N   
8347  C CA  . ARG A 549 ? 1.4510 1.8263 1.5160 0.0616  -0.1400 -0.3927 549 ARG A CA  
8348  C C   . ARG A 549 ? 1.4437 1.8272 1.5209 0.0384  -0.1297 -0.3514 549 ARG A C   
8349  O O   . ARG A 549 ? 1.4669 1.8537 1.5352 0.0119  -0.1411 -0.3271 549 ARG A O   
8350  C CB  . ARG A 549 ? 1.4907 1.9063 1.5146 0.0480  -0.1511 -0.4041 549 ARG A CB  
8351  C CG  . ARG A 549 ? 1.4783 1.9793 1.4647 0.0324  -0.1368 -0.3996 549 ARG A CG  
8352  C CD  . ARG A 549 ? 1.5006 2.0356 1.4422 0.0093  -0.1508 -0.4048 549 ARG A CD  
8353  N NE  . ARG A 549 ? 1.5210 2.0441 1.4483 0.0339  -0.1616 -0.4486 549 ARG A NE  
8354  C CZ  . ARG A 549 ? 1.5417 2.0887 1.4270 0.0199  -0.1746 -0.4626 549 ARG A CZ  
8355  N NH1 . ARG A 549 ? 1.5632 2.0908 1.4350 0.0461  -0.1866 -0.5051 549 ARG A NH1 
8356  N NH2 . ARG A 549 ? 1.5473 2.1325 1.3996 -0.0220 -0.1795 -0.4337 549 ARG A NH2 
8370  N N   . ASP A 550 ? 1.4234 1.8046 1.5181 0.0481  -0.1128 -0.3436 550 ASP A N   
8371  C CA  . ASP A 550 ? 1.4227 1.7995 1.5285 0.0300  -0.1053 -0.3070 550 ASP A CA  
8372  C C   . ASP A 550 ? 1.3928 1.7091 1.5395 0.0377  -0.1026 -0.2989 550 ASP A C   
8373  O O   . ASP A 550 ? 1.3923 1.6957 1.5501 0.0537  -0.0910 -0.3070 550 ASP A O   
8374  C CB  . ASP A 550 ? 1.3831 1.8131 1.4706 0.0298  -0.0879 -0.3021 550 ASP A CB  
8375  C CG  . ASP A 550 ? 1.3582 1.7769 1.4494 0.0091  -0.0855 -0.2634 550 ASP A CG  
8376  O OD1 . ASP A 550 ? 1.3400 1.7143 1.4472 -0.0022 -0.0981 -0.2441 550 ASP A OD1 
8377  O OD2 . ASP A 550 ? 1.3413 1.7964 1.4201 0.0054  -0.0732 -0.2541 550 ASP A OD2 
8382  N N   . LYS A 551 ? 1.3393 1.6234 1.5084 0.0253  -0.1146 -0.2839 551 LYS A N   
8383  C CA  . LYS A 551 ? 1.3186 1.5609 1.5269 0.0270  -0.1100 -0.2749 551 LYS A CA  
8384  C C   . LYS A 551 ? 1.2691 1.5075 1.4905 0.0159  -0.1076 -0.2479 551 LYS A C   
8385  O O   . LYS A 551 ? 1.2017 1.4161 1.4566 0.0166  -0.1029 -0.2419 551 LYS A O   
8386  C CB  . LYS A 551 ? 1.3793 1.5952 1.6112 0.0243  -0.1259 -0.2837 551 LYS A CB  
8387  C CG  . LYS A 551 ? 1.4326 1.6380 1.6483 0.0358  -0.1357 -0.3116 551 LYS A CG  
8388  C CD  . LYS A 551 ? 1.4524 1.6316 1.6879 0.0268  -0.1559 -0.3151 551 LYS A CD  
8389  C CE  . LYS A 551 ? 1.4832 1.6453 1.6937 0.0378  -0.1729 -0.3437 551 LYS A CE  
8390  N NZ  . LYS A 551 ? 1.5026 1.6363 1.7301 0.0248  -0.1959 -0.3439 551 LYS A NZ  
8404  N N   . LEU A 552 ? 1.2308 1.4934 1.4238 0.0046  -0.1129 -0.2324 552 LEU A N   
8405  C CA  . LEU A 552 ? 1.2257 1.4745 1.4243 -0.0054 -0.1210 -0.2077 552 LEU A CA  
8406  C C   . LEU A 552 ? 1.2124 1.4593 1.4023 -0.0034 -0.1040 -0.1953 552 LEU A C   
8407  O O   . LEU A 552 ? 1.2221 1.4417 1.4366 0.0027  -0.0967 -0.1899 552 LEU A O   
8408  C CB  . LEU A 552 ? 1.2286 1.4925 1.3947 -0.0259 -0.1465 -0.1926 552 LEU A CB  
8409  C CG  . LEU A 552 ? 1.2180 1.4603 1.4034 -0.0315 -0.1751 -0.1890 552 LEU A CG  
8410  C CD1 . LEU A 552 ? 1.2254 1.4662 1.4350 -0.0227 -0.1746 -0.2114 552 LEU A CD1 
8411  C CD2 . LEU A 552 ? 1.2571 1.5100 1.3986 -0.0573 -0.2043 -0.1706 552 LEU A CD2 
8423  N N   . THR A 553 ? 1.1864 1.4674 1.3414 -0.0097 -0.0977 -0.1914 553 THR A N   
8424  C CA  . THR A 553 ? 1.1147 1.3959 1.2594 -0.0113 -0.0852 -0.1763 553 THR A CA  
8425  C C   . THR A 553 ? 1.0329 1.2865 1.2063 0.0070  -0.0653 -0.1878 553 THR A C   
8426  O O   . THR A 553 ? 1.0101 1.2652 1.1948 0.0203  -0.0582 -0.2101 553 THR A O   
8427  C CB  . THR A 553 ? 1.1200 1.4572 1.2297 -0.0195 -0.0786 -0.1752 553 THR A CB  
8428  O OG1 . THR A 553 ? 1.1245 1.4855 1.2424 0.0012  -0.0645 -0.2059 553 THR A OG1 
8429  C CG2 . THR A 553 ? 1.1592 1.5308 1.2331 -0.0457 -0.0987 -0.1623 553 THR A CG2 
8437  N N   . PRO A 554 ? 1.0150 1.2392 1.1963 0.0064  -0.0593 -0.1734 554 PRO A N   
8438  C CA  . PRO A 554 ? 1.0189 1.2170 1.2219 0.0174  -0.0415 -0.1819 554 PRO A CA  
8439  C C   . PRO A 554 ? 1.0454 1.2586 1.2356 0.0249  -0.0301 -0.1894 554 PRO A C   
8440  O O   . PRO A 554 ? 1.0226 1.2694 1.1888 0.0207  -0.0299 -0.1818 554 PRO A O   
8441  C CB  . PRO A 554 ? 1.0214 1.1914 1.2261 0.0133  -0.0394 -0.1644 554 PRO A CB  
8442  C CG  . PRO A 554 ? 1.0318 1.2125 1.2053 0.0008  -0.0559 -0.1441 554 PRO A CG  
8443  C CD  . PRO A 554 ? 1.0305 1.2402 1.1952 -0.0059 -0.0719 -0.1486 554 PRO A CD  
8451  N N   . ILE A 555 ? 1.0795 1.2693 1.2866 0.0346  -0.0235 -0.2044 555 ILE A N   
8452  C CA  . ILE A 555 ? 1.1438 1.3348 1.3436 0.0456  -0.0181 -0.2133 555 ILE A CA  
8453  C C   . ILE A 555 ? 1.2427 1.4106 1.4378 0.0386  -0.0078 -0.1936 555 ILE A C   
8454  O O   . ILE A 555 ? 1.3153 1.4475 1.5216 0.0310  -0.0021 -0.1864 555 ILE A O   
8455  C CB  . ILE A 555 ? 1.1289 1.2902 1.3424 0.0557  -0.0247 -0.2349 555 ILE A CB  
8456  C CG1 . ILE A 555 ? 1.1279 1.3048 1.3432 0.0618  -0.0376 -0.2547 555 ILE A CG1 
8457  C CG2 . ILE A 555 ? 1.1204 1.2771 1.3267 0.0712  -0.0268 -0.2465 555 ILE A CG2 
8458  C CD1 . ILE A 555 ? 1.1275 1.2623 1.3591 0.0594  -0.0483 -0.2652 555 ILE A CD1 
8470  N N   . THR A 556 ? 1.2791 1.4727 1.4569 0.0398  -0.0051 -0.1856 556 THR A N   
8471  C CA  . THR A 556 ? 1.2879 1.4585 1.4571 0.0327  0.0021  -0.1663 556 THR A CA  
8472  C C   . THR A 556 ? 1.2416 1.4005 1.4147 0.0451  0.0023  -0.1776 556 THR A C   
8473  O O   . THR A 556 ? 1.2656 1.4614 1.4403 0.0612  -0.0031 -0.1957 556 THR A O   
8474  C CB  . THR A 556 ? 1.3359 1.5388 1.4817 0.0205  0.0001  -0.1442 556 THR A CB  
8475  O OG1 . THR A 556 ? 1.3673 1.6339 1.5061 0.0255  -0.0027 -0.1543 556 THR A OG1 
8476  C CG2 . THR A 556 ? 1.3336 1.5247 1.4714 0.0068  -0.0082 -0.1290 556 THR A CG2 
8484  N N   . ILE A 557 ? 1.1574 1.2662 1.3314 0.0380  0.0061  -0.1688 557 ILE A N   
8485  C CA  . ILE A 557 ? 1.1870 1.2714 1.3605 0.0453  0.0006  -0.1737 557 ILE A CA  
8486  C C   . ILE A 557 ? 1.1764 1.2629 1.3340 0.0369  0.0059  -0.1509 557 ILE A C   
8487  O O   . ILE A 557 ? 1.0863 1.1462 1.2319 0.0199  0.0141  -0.1308 557 ILE A O   
8488  C CB  . ILE A 557 ? 1.1786 1.2033 1.3567 0.0354  -0.0028 -0.1756 557 ILE A CB  
8489  C CG1 . ILE A 557 ? 1.1705 1.1918 1.3624 0.0431  -0.0145 -0.1979 557 ILE A CG1 
8490  C CG2 . ILE A 557 ? 1.1758 1.1618 1.3459 0.0360  -0.0134 -0.1729 557 ILE A CG2 
8491  C CD1 . ILE A 557 ? 1.1328 1.1493 1.3353 0.0269  -0.0064 -0.1938 557 ILE A CD1 
8503  N N   . PHE A 558 ? 1.1731 1.2939 1.3314 0.0499  -0.0002 -0.1561 558 PHE A N   
8504  C CA  . PHE A 558 ? 1.1301 1.2650 1.2747 0.0407  0.0021  -0.1336 558 PHE A CA  
8505  C C   . PHE A 558 ? 1.0887 1.1871 1.2361 0.0469  -0.0072 -0.1346 558 PHE A C   
8506  O O   . PHE A 558 ? 1.1299 1.2308 1.2937 0.0691  -0.0207 -0.1593 558 PHE A O   
8507  C CB  . PHE A 558 ? 1.1366 1.3555 1.2813 0.0459  0.0019  -0.1358 558 PHE A CB  
8508  C CG  . PHE A 558 ? 1.0918 1.3329 1.2216 0.0308  0.0020  -0.1090 558 PHE A CG  
8509  C CD1 . PHE A 558 ? 1.0641 1.2891 1.1680 0.0045  0.0035  -0.0782 558 PHE A CD1 
8510  C CD2 . PHE A 558 ? 1.0785 1.3552 1.2205 0.0437  -0.0035 -0.1153 558 PHE A CD2 
8511  C CE1 . PHE A 558 ? 1.0613 1.3013 1.1472 -0.0129 -0.0007 -0.0510 558 PHE A CE1 
8512  C CE2 . PHE A 558 ? 1.0752 1.3760 1.2046 0.0266  -0.0048 -0.0883 558 PHE A CE2 
8513  C CZ  . PHE A 558 ? 1.0616 1.3423 1.1605 -0.0039 -0.0036 -0.0545 558 PHE A CZ  
8523  N N   . MET A 559 ? 1.0514 1.1112 1.1804 0.0280  -0.0041 -0.1087 559 MET A N   
8524  C CA  . MET A 559 ? 1.1568 1.1764 1.2827 0.0280  -0.0155 -0.1035 559 MET A CA  
8525  C C   . MET A 559 ? 1.1982 1.2438 1.3127 0.0196  -0.0159 -0.0805 559 MET A C   
8526  O O   . MET A 559 ? 1.1692 1.2103 1.2612 -0.0009 -0.0070 -0.0565 559 MET A O   
8527  C CB  . MET A 559 ? 1.1669 1.1087 1.2755 0.0069  -0.0129 -0.0925 559 MET A CB  
8528  C CG  . MET A 559 ? 1.2193 1.1108 1.3169 0.0000  -0.0280 -0.0827 559 MET A CG  
8529  S SD  . MET A 559 ? 1.2986 1.1165 1.3627 -0.0361 -0.0177 -0.0614 559 MET A SD  
8530  C CE  . MET A 559 ? 1.3825 1.1431 1.4333 -0.0434 -0.0443 -0.0515 559 MET A CE  
8540  N N   . GLU A 560 ? 1.2167 1.2869 1.3469 0.0359  -0.0300 -0.0887 560 GLU A N   
8541  C CA  . GLU A 560 ? 1.2248 1.3279 1.3501 0.0282  -0.0336 -0.0677 560 GLU A CA  
8542  C C   . GLU A 560 ? 1.1958 1.2434 1.3211 0.0300  -0.0517 -0.0633 560 GLU A C   
8543  O O   . GLU A 560 ? 1.2100 1.2350 1.3541 0.0518  -0.0689 -0.0878 560 GLU A O   
8544  C CB  . GLU A 560 ? 1.2478 1.4576 1.3985 0.0474  -0.0343 -0.0841 560 GLU A CB  
8545  C CG  . GLU A 560 ? 1.2506 1.5214 1.3849 0.0228  -0.0266 -0.0554 560 GLU A CG  
8546  C CD  . GLU A 560 ? 1.2564 1.6479 1.4150 0.0366  -0.0248 -0.0727 560 GLU A CD  
8547  O OE1 . GLU A 560 ? 1.2515 1.6776 1.4415 0.0717  -0.0288 -0.1120 560 GLU A OE1 
8548  O OE2 . GLU A 560 ? 1.2503 1.7030 1.3941 0.0111  -0.0212 -0.0478 560 GLU A OE2 
8555  N N   . TYR A 561 ? 1.1726 1.1910 1.2732 0.0060  -0.0526 -0.0316 561 TYR A N   
8556  C CA  . TYR A 561 ? 1.1693 1.1284 1.2634 0.0015  -0.0718 -0.0221 561 TYR A CA  
8557  C C   . TYR A 561 ? 1.2123 1.2083 1.3048 -0.0071 -0.0790 0.0012  561 TYR A C   
8558  O O   . TYR A 561 ? 1.1783 1.1748 1.2421 -0.0329 -0.0689 0.0297  561 TYR A O   
8559  C CB  . TYR A 561 ? 1.1710 1.0348 1.2270 -0.0268 -0.0667 -0.0053 561 TYR A CB  
8560  C CG  . TYR A 561 ? 1.2065 1.0527 1.2253 -0.0549 -0.0500 0.0229  561 TYR A CG  
8561  C CD1 . TYR A 561 ? 1.2467 1.0644 1.2389 -0.0745 -0.0582 0.0508  561 TYR A CD1 
8562  C CD2 . TYR A 561 ? 1.2090 1.0610 1.2181 -0.0603 -0.0304 0.0199  561 TYR A CD2 
8563  C CE1 . TYR A 561 ? 1.2623 1.0549 1.2160 -0.0975 -0.0481 0.0735  561 TYR A CE1 
8564  C CE2 . TYR A 561 ? 1.2196 1.0481 1.1941 -0.0806 -0.0215 0.0409  561 TYR A CE2 
8565  C CZ  . TYR A 561 ? 1.2490 1.0456 1.1940 -0.0987 -0.0308 0.0669  561 TYR A CZ  
8566  O OH  . TYR A 561 ? 1.2610 1.0268 1.1675 -0.1163 -0.0269 0.0851  561 TYR A OH  
8576  N N   . ARG A 562 ? 1.3334 1.3598 1.4573 0.0154  -0.1001 -0.0118 562 ARG A N   
8577  C CA  . ARG A 562 ? 1.4366 1.5036 1.5670 0.0091  -0.1113 0.0084  562 ARG A CA  
8578  C C   . ARG A 562 ? 1.4491 1.4364 1.5734 0.0064  -0.1386 0.0169  562 ARG A C   
8579  O O   . ARG A 562 ? 1.4927 1.3952 1.6038 0.0059  -0.1489 0.0086  562 ARG A O   
8580  C CB  . ARG A 562 ? 1.5156 1.7075 1.6947 0.0394  -0.1137 -0.0166 562 ARG A CB  
8581  C CG  . ARG A 562 ? 1.5547 1.8238 1.7378 0.0418  -0.0898 -0.0292 562 ARG A CG  
8582  C CD  . ARG A 562 ? 1.5675 1.9742 1.7792 0.0476  -0.0856 -0.0335 562 ARG A CD  
8583  N NE  . ARG A 562 ? 1.5677 2.0191 1.7505 0.0138  -0.0671 -0.0076 562 ARG A NE  
8584  C CZ  . ARG A 562 ? 1.6120 2.1868 1.8100 0.0124  -0.0572 -0.0149 562 ARG A CZ  
8585  N NH1 . ARG A 562 ? 1.6758 2.3514 1.9218 0.0480  -0.0594 -0.0526 562 ARG A NH1 
8586  N NH2 . ARG A 562 ? 1.5792 2.1772 1.7427 -0.0248 -0.0476 0.0139  562 ARG A NH2 
8600  N N   . LEU A 563 ? 1.4264 1.4412 1.5579 0.0003  -0.1530 0.0361  563 LEU A N   
8601  C CA  . LEU A 563 ? 1.4808 1.4210 1.6049 -0.0051 -0.1831 0.0480  563 LEU A CA  
8602  C C   . LEU A 563 ? 1.5197 1.5332 1.6972 0.0264  -0.2095 0.0321  563 LEU A C   
8603  O O   . LEU A 563 ? 1.5014 1.6330 1.7122 0.0387  -0.1993 0.0253  563 LEU A O   
8604  C CB  . LEU A 563 ? 1.4781 1.3551 1.5491 -0.0499 -0.1803 0.0934  563 LEU A CB  
8605  C CG  . LEU A 563 ? 1.5388 1.2900 1.5581 -0.0778 -0.1842 0.1081  563 LEU A CG  
8606  C CD1 . LEU A 563 ? 1.5645 1.2687 1.5394 -0.1141 -0.1901 0.1482  563 LEU A CD1 
8607  C CD2 . LEU A 563 ? 1.6016 1.2925 1.6343 -0.0627 -0.2156 0.0896  563 LEU A CD2 
8619  N N   . ASP A 564 ? 1.5971 1.5410 1.7820 0.0378  -0.2460 0.0259  564 ASP A N   
8620  C CA  . ASP A 564 ? 1.6489 1.6425 1.8820 0.0658  -0.2793 0.0146  564 ASP A CA  
8621  C C   . ASP A 564 ? 1.6927 1.6461 1.8951 0.0268  -0.2897 0.0612  564 ASP A C   
8622  O O   . ASP A 564 ? 1.7105 1.5445 1.8685 -0.0002 -0.3067 0.0835  564 ASP A O   
8623  C CB  . ASP A 564 ? 1.7123 1.6432 1.9697 0.1020  -0.3227 -0.0192 564 ASP A CB  
8624  C CG  . ASP A 564 ? 1.7270 1.7435 2.0537 0.1513  -0.3553 -0.0508 564 ASP A CG  
8625  O OD1 . ASP A 564 ? 1.7013 1.8015 2.0495 0.1446  -0.3506 -0.0334 564 ASP A OD1 
8626  O OD2 . ASP A 564 ? 1.7584 1.7603 2.1188 0.1972  -0.3880 -0.0944 564 ASP A OD2 
8631  N N   . TYR A 565 ? 1.7082 1.7621 1.9293 0.0192  -0.2798 0.0778  565 TYR A N   
8632  C CA  . TYR A 565 ? 1.8017 1.8167 1.9853 -0.0237 -0.2871 0.1262  565 TYR A CA  
8633  C C   . TYR A 565 ? 1.9668 1.9562 2.1761 -0.0128 -0.3321 0.1299  565 TYR A C   
8634  O O   . TYR A 565 ? 2.0735 1.9679 2.2369 -0.0482 -0.3484 0.1659  565 TYR A O   
8635  C CB  . TYR A 565 ? 1.7296 1.8547 1.9162 -0.0444 -0.2645 0.1489  565 TYR A CB  
8636  C CG  . TYR A 565 ? 1.6608 1.7795 1.8037 -0.0686 -0.2282 0.1595  565 TYR A CG  
8637  C CD1 . TYR A 565 ? 1.6366 1.6330 1.7180 -0.0934 -0.2181 0.1740  565 TYR A CD1 
8638  C CD2 . TYR A 565 ? 1.6314 1.8699 1.7945 -0.0670 -0.2061 0.1535  565 TYR A CD2 
8639  C CE1 . TYR A 565 ? 1.5882 1.5794 1.6350 -0.1103 -0.1893 0.1799  565 TYR A CE1 
8640  C CE2 . TYR A 565 ? 1.5823 1.8076 1.7051 -0.0887 -0.1798 0.1636  565 TYR A CE2 
8641  C CZ  . TYR A 565 ? 1.5392 1.6392 1.6066 -0.1074 -0.1727 0.1755  565 TYR A CZ  
8642  O OH  . TYR A 565 ? 1.4606 1.5479 1.4929 -0.1239 -0.1506 0.1820  565 TYR A OH  
8652  N N   . ARG A 566 ? 1.9891 2.0617 2.2709 0.0369  -0.3548 0.0912  566 ARG A N   
8653  C CA  . ARG A 566 ? 1.9492 2.0070 2.2633 0.0514  -0.4024 0.0927  566 ARG A CA  
8654  C C   . ARG A 566 ? 1.9851 1.8772 2.2575 0.0400  -0.4385 0.1009  566 ARG A C   
8655  O O   . ARG A 566 ? 2.0337 1.8642 2.2927 0.0209  -0.4730 0.1282  566 ARG A O   
8656  C CB  . ARG A 566 ? 1.8929 2.0745 2.2968 0.1159  -0.4211 0.0394  566 ARG A CB  
8657  C CG  . ARG A 566 ? 1.7907 2.1551 2.2388 0.1216  -0.3896 0.0339  566 ARG A CG  
8658  C CD  . ARG A 566 ? 1.7238 2.2206 2.2645 0.1868  -0.4115 -0.0211 566 ARG A CD  
8659  N NE  . ARG A 566 ? 1.6770 2.1700 2.2553 0.1986  -0.4587 -0.0145 566 ARG A NE  
8660  C CZ  . ARG A 566 ? 1.6367 2.0267 2.2293 0.2305  -0.5118 -0.0348 566 ARG A CZ  
8661  N NH1 . ARG A 566 ? 1.6230 1.9038 2.1930 0.2513  -0.5251 -0.0620 566 ARG A NH1 
8662  N NH2 . ARG A 566 ? 1.6382 2.0319 2.2664 0.2389  -0.5561 -0.0261 566 ARG A NH2 
8676  N N   . THR A 567 ? 1.9976 1.8164 2.2460 0.0464  -0.4331 0.0804  567 THR A N   
8677  C CA  . THR A 567 ? 2.0835 1.7522 2.2920 0.0321  -0.4714 0.0871  567 THR A CA  
8678  C C   . THR A 567 ? 2.1030 1.6656 2.2287 -0.0330 -0.4608 0.1389  567 THR A C   
8679  O O   . THR A 567 ? 2.1481 1.5935 2.2370 -0.0552 -0.4980 0.1548  567 THR A O   
8680  C CB  . THR A 567 ? 2.1064 1.7334 2.3099 0.0514  -0.4686 0.0533  567 THR A CB  
8681  O OG1 . THR A 567 ? 2.1581 1.6463 2.3281 0.0378  -0.5165 0.0586  567 THR A OG1 
8682  C CG2 . THR A 567 ? 2.1182 1.7430 2.2742 0.0182  -0.4120 0.0671  567 THR A CG2 
8690  N N   . ALA A 568 ? 2.0799 1.6785 2.1726 -0.0644 -0.4146 0.1646  568 ALA A N   
8691  C CA  . ALA A 568 ? 2.1538 1.6581 2.1660 -0.1212 -0.4013 0.2070  568 ALA A CA  
8692  C C   . ALA A 568 ? 2.0988 1.6063 2.0978 -0.1469 -0.4165 0.2451  568 ALA A C   
8693  O O   . ALA A 568 ? 2.0687 1.5178 2.0013 -0.1915 -0.4008 0.2793  568 ALA A O   
8694  C CB  . ALA A 568 ? 2.2126 1.7381 2.1909 -0.1383 -0.3477 0.2095  568 ALA A CB  
8700  N N   . ALA A 569 ? 2.1081 1.6831 2.1690 -0.1186 -0.4487 0.2380  569 ALA A N   
8701  C CA  . ALA A 569 ? 2.1646 1.7662 2.2234 -0.1413 -0.4625 0.2738  569 ALA A CA  
8702  C C   . ALA A 569 ? 2.2793 1.7426 2.2662 -0.1882 -0.4884 0.3126  569 ALA A C   
8703  O O   . ALA A 569 ? 2.4064 1.7593 2.3504 -0.2023 -0.5004 0.3105  569 ALA A O   
8704  C CB  . ALA A 569 ? 2.1705 1.8733 2.3176 -0.0977 -0.4970 0.2528  569 ALA A CB  
8710  N N   . ASP A 570 ? 2.2586 1.7322 2.2297 -0.2163 -0.4985 0.3498  570 ASP A N   
8711  C CA  . ASP A 570 ? 2.3326 1.6857 2.2329 -0.2636 -0.5231 0.3897  570 ASP A CA  
8712  C C   . ASP A 570 ? 2.3191 1.7012 2.2603 -0.2602 -0.5702 0.4080  570 ASP A C   
8713  O O   . ASP A 570 ? 2.1750 1.6837 2.1979 -0.2242 -0.5771 0.3913  570 ASP A O   
8714  C CB  . ASP A 570 ? 2.4745 1.8071 2.2997 -0.3054 -0.4823 0.4130  570 ASP A CB  
8715  C CG  . ASP A 570 ? 2.5892 1.8898 2.3654 -0.3072 -0.4344 0.3798  570 ASP A CG  
8716  O OD1 . ASP A 570 ? 2.6509 1.9045 2.3935 -0.3125 -0.4319 0.3601  570 ASP A OD1 
8717  O OD2 . ASP A 570 ? 2.5939 1.9226 2.3666 -0.3038 -0.4019 0.3774  570 ASP A OD2 
8722  N N   . THR A 571 ? 2.2940 1.5779 2.1809 -0.2965 -0.5965 0.4327  571 THR A N   
8723  C CA  . THR A 571 ? 2.2885 1.5857 2.2068 -0.3005 -0.6448 0.4562  571 THR A CA  
8724  C C   . THR A 571 ? 2.1805 1.5929 2.1324 -0.3039 -0.6345 0.4810  571 THR A C   
8725  O O   . THR A 571 ? 2.1592 1.6653 2.1865 -0.2802 -0.6638 0.4781  571 THR A O   
8726  C CB  . THR A 571 ? 2.3244 1.5759 2.1784 -0.3343 -0.6350 0.4429  571 THR A CB  
8727  O OG1 . THR A 571 ? 2.3180 1.5865 2.2007 -0.3448 -0.6775 0.4679  571 THR A OG1 
8728  C CG2 . THR A 571 ? 2.2811 1.5470 2.0632 -0.3567 -0.5709 0.4311  571 THR A CG2 
8736  N N   . THR A 572 ? 2.0734 1.4964 1.9733 -0.3323 -0.5896 0.4963  572 THR A N   
8737  C CA  . THR A 572 ? 1.9804 1.5205 1.9059 -0.3410 -0.5764 0.5164  572 THR A CA  
8738  C C   . THR A 572 ? 1.8372 1.5436 1.8668 -0.2901 -0.5663 0.4784  572 THR A C   
8739  O O   . THR A 572 ? 1.8023 1.6319 1.8801 -0.2917 -0.5716 0.4911  572 THR A O   
8740  C CB  . THR A 572 ? 1.9632 1.4915 1.8220 -0.3676 -0.5251 0.5155  572 THR A CB  
8741  O OG1 . THR A 572 ? 1.9662 1.4590 1.8098 -0.3489 -0.4956 0.4887  572 THR A OG1 
8742  C CG2 . THR A 572 ? 1.9690 1.4469 1.7651 -0.3887 -0.5044 0.4897  572 THR A CG2 
8750  N N   . GLY A 573 ? 1.7505 1.4664 1.8141 -0.2469 -0.5531 0.4314  573 GLY A N   
8751  C CA  . GLY A 573 ? 1.6097 1.4773 1.7539 -0.2011 -0.5311 0.3910  573 GLY A CA  
8752  C C   . GLY A 573 ? 1.5057 1.4077 1.6187 -0.2116 -0.4793 0.3869  573 GLY A C   
8753  O O   . GLY A 573 ? 1.4174 1.4548 1.5875 -0.1837 -0.4574 0.3601  573 GLY A O   
8757  N N   . LEU A 574 ? 1.4765 1.2610 1.5004 -0.2499 -0.4608 0.4104  574 LEU A N   
8758  C CA  . LEU A 574 ? 1.4363 1.2399 1.4211 -0.2670 -0.4190 0.4150  574 LEU A CA  
8759  C C   . LEU A 574 ? 1.4308 1.1890 1.4073 -0.2421 -0.3926 0.3772  574 LEU A C   
8760  O O   . LEU A 574 ? 1.4726 1.1056 1.3943 -0.2559 -0.3937 0.3791  574 LEU A O   
8761  C CB  . LEU A 574 ? 1.4480 1.1544 1.3419 -0.3213 -0.4199 0.4618  574 LEU A CB  
8762  C CG  . LEU A 574 ? 1.3971 1.1437 1.2554 -0.3490 -0.3978 0.4839  574 LEU A CG  
8763  C CD1 . LEU A 574 ? 1.3464 1.2461 1.2631 -0.3513 -0.4052 0.4963  574 LEU A CD1 
8764  C CD2 . LEU A 574 ? 1.4239 1.0752 1.2060 -0.3826 -0.3971 0.4953  574 LEU A CD2 
8776  N N   . GLN A 575 ? 1.3605 1.2244 1.3892 -0.2087 -0.3693 0.3436  575 GLN A N   
8777  C CA  . GLN A 575 ? 1.3180 1.1509 1.3444 -0.1846 -0.3454 0.3074  575 GLN A CA  
8778  C C   . GLN A 575 ? 1.2937 1.0765 1.2526 -0.2144 -0.3120 0.3222  575 GLN A C   
8779  O O   . GLN A 575 ? 1.2901 1.1065 1.2241 -0.2416 -0.3040 0.3503  575 GLN A O   
8780  C CB  . GLN A 575 ? 1.2670 1.2322 1.3709 -0.1378 -0.3339 0.2648  575 GLN A CB  
8781  C CG  . GLN A 575 ? 1.2843 1.3361 1.4660 -0.1026 -0.3660 0.2459  575 GLN A CG  
8782  C CD  . GLN A 575 ? 1.3062 1.5208 1.5592 -0.0641 -0.3486 0.2084  575 GLN A CD  
8783  O OE1 . GLN A 575 ? 1.3356 1.5910 1.5773 -0.0655 -0.3139 0.1982  575 GLN A OE1 
8784  N NE2 . GLN A 575 ? 1.3328 1.6451 1.6599 -0.0290 -0.3736 0.1862  575 GLN A NE2 
8793  N N   . PRO A 576 ? 1.2811 0.9841 1.2097 -0.2104 -0.2957 0.3037  576 PRO A N   
8794  C CA  . PRO A 576 ? 1.2754 0.9433 1.1508 -0.2299 -0.2641 0.3094  576 PRO A CA  
8795  C C   . PRO A 576 ? 1.2174 0.9876 1.1304 -0.2079 -0.2386 0.2870  576 PRO A C   
8796  O O   . PRO A 576 ? 1.1873 1.0494 1.1645 -0.1749 -0.2403 0.2605  576 PRO A O   
8797  C CB  . PRO A 576 ? 1.3089 0.8731 1.1501 -0.2317 -0.2575 0.2940  576 PRO A CB  
8798  C CG  . PRO A 576 ? 1.3160 0.8963 1.2122 -0.1992 -0.2779 0.2663  576 PRO A CG  
8799  C CD  . PRO A 576 ? 1.3135 0.9526 1.2534 -0.1902 -0.3093 0.2776  576 PRO A CD  
8807  N N   . ILE A 577 ? 1.2064 0.9577 1.0760 -0.2261 -0.2173 0.2965  577 ILE A N   
8808  C CA  . ILE A 577 ? 1.1866 1.0204 1.0784 -0.2135 -0.1956 0.2812  577 ILE A CA  
8809  C C   . ILE A 577 ? 1.2341 1.0014 1.0891 -0.2138 -0.1722 0.2669  577 ILE A C   
8810  O O   . ILE A 577 ? 1.3068 0.9784 1.1063 -0.2341 -0.1716 0.2795  577 ILE A O   
8811  C CB  . ILE A 577 ? 1.1318 1.0291 1.0108 -0.2407 -0.2026 0.3140  577 ILE A CB  
8812  C CG1 . ILE A 577 ? 1.0267 1.0202 0.9312 -0.2307 -0.1843 0.2989  577 ILE A CG1 
8813  C CG2 . ILE A 577 ? 1.2027 1.0010 1.0045 -0.2773 -0.2101 0.3471  577 ILE A CG2 
8814  C CD1 . ILE A 577 ? 0.9989 1.0783 0.8993 -0.2609 -0.1957 0.3315  577 ILE A CD1 
8826  N N   . LEU A 578 ? 1.2106 1.0339 1.0979 -0.1900 -0.1531 0.2381  578 LEU A N   
8827  C CA  . LEU A 578 ? 1.1997 0.9766 1.0606 -0.1887 -0.1315 0.2236  578 LEU A CA  
8828  C C   . LEU A 578 ? 1.2221 0.9856 1.0377 -0.2126 -0.1313 0.2473  578 LEU A C   
8829  O O   . LEU A 578 ? 1.2019 1.0244 1.0195 -0.2266 -0.1430 0.2691  578 LEU A O   
8830  C CB  . LEU A 578 ? 1.1392 0.9804 1.0472 -0.1580 -0.1152 0.1881  578 LEU A CB  
8831  C CG  . LEU A 578 ? 1.1577 0.9866 1.1010 -0.1320 -0.1182 0.1585  578 LEU A CG  
8832  C CD1 . LEU A 578 ? 1.1610 1.0671 1.1518 -0.1006 -0.1073 0.1245  578 LEU A CD1 
8833  C CD2 . LEU A 578 ? 1.1819 0.9103 1.0887 -0.1433 -0.1112 0.1547  578 LEU A CD2 
8845  N N   . ASN A 579 ? 1.2602 0.9467 1.0337 -0.2182 -0.1207 0.2425  579 ASN A N   
8846  C CA  . ASN A 579 ? 1.3323 0.9942 1.0621 -0.2345 -0.1264 0.2588  579 ASN A CA  
8847  C C   . ASN A 579 ? 1.3417 1.0809 1.0988 -0.2255 -0.1217 0.2509  579 ASN A C   
8848  O O   . ASN A 579 ? 1.2590 1.0231 1.0469 -0.2025 -0.1025 0.2208  579 ASN A O   
8849  C CB  . ASN A 579 ? 1.3751 0.9504 1.0630 -0.2335 -0.1147 0.2449  579 ASN A CB  
8850  C CG  . ASN A 579 ? 1.4217 0.9570 1.0605 -0.2456 -0.1290 0.2586  579 ASN A CG  
8851  O OD1 . ASN A 579 ? 1.4200 0.9963 1.0601 -0.2541 -0.1451 0.2755  579 ASN A OD1 
8852  N ND2 . ASN A 579 ? 1.4640 0.9189 1.0568 -0.2472 -0.1260 0.2504  579 ASN A ND2 
8859  N N   . GLN A 580 ? 1.4059 1.1829 1.1484 -0.2479 -0.1416 0.2803  580 GLN A N   
8860  C CA  . GLN A 580 ? 1.4557 1.3087 1.2164 -0.2477 -0.1408 0.2778  580 GLN A CA  
8861  C C   . GLN A 580 ? 1.5205 1.3215 1.2542 -0.2422 -0.1390 0.2660  580 GLN A C   
8862  O O   . GLN A 580 ? 1.5348 1.3857 1.2926 -0.2308 -0.1301 0.2496  580 GLN A O   
8863  C CB  . GLN A 580 ? 1.4843 1.3909 1.2289 -0.2826 -0.1663 0.3175  580 GLN A CB  
8864  C CG  . GLN A 580 ? 1.4948 1.4652 1.2710 -0.2882 -0.1708 0.3296  580 GLN A CG  
8865  C CD  . GLN A 580 ? 1.4979 1.5866 1.3420 -0.2627 -0.1525 0.3014  580 GLN A CD  
8866  O OE1 . GLN A 580 ? 1.4846 1.5739 1.3675 -0.2314 -0.1399 0.2725  580 GLN A OE1 
8867  N NE2 . GLN A 580 ? 1.5236 1.7118 1.3785 -0.2773 -0.1541 0.3094  580 GLN A NE2 
8876  N N   . PHE A 581 ? 1.6105 1.3133 1.2949 -0.2481 -0.1487 0.2715  581 PHE A N   
8877  C CA  . PHE A 581 ? 1.6826 1.3365 1.3430 -0.2388 -0.1523 0.2575  581 PHE A CA  
8878  C C   . PHE A 581 ? 1.7831 1.4488 1.4830 -0.2065 -0.1207 0.2157  581 PHE A C   
8879  O O   . PHE A 581 ? 1.9114 1.5857 1.6190 -0.1948 -0.1203 0.2005  581 PHE A O   
8880  C CB  . PHE A 581 ? 1.6691 1.2192 1.2687 -0.2475 -0.1707 0.2669  581 PHE A CB  
8881  C CG  . PHE A 581 ? 1.7151 1.2417 1.2678 -0.2826 -0.2090 0.3107  581 PHE A CG  
8882  C CD1 . PHE A 581 ? 1.7446 1.3200 1.2930 -0.3061 -0.2343 0.3376  581 PHE A CD1 
8883  C CD2 . PHE A 581 ? 1.7567 1.2168 1.2689 -0.2955 -0.2209 0.3250  581 PHE A CD2 
8884  C CE1 . PHE A 581 ? 1.7916 1.3658 1.3138 -0.3355 -0.2662 0.3653  581 PHE A CE1 
8885  C CE2 . PHE A 581 ? 1.8017 1.2784 1.3051 -0.3128 -0.2477 0.3383  581 PHE A CE2 
8886  C CZ  . PHE A 581 ? 1.8228 1.3542 1.3324 -0.3339 -0.2704 0.3581  581 PHE A CZ  
8896  N N   . THR A 582 ? 1.8032 1.4665 1.5265 -0.1947 -0.0981 0.1987  582 THR A N   
8897  C CA  . THR A 582 ? 1.7716 1.4524 1.5333 -0.1701 -0.0712 0.1631  582 THR A CA  
8898  C C   . THR A 582 ? 1.6742 1.4427 1.4855 -0.1593 -0.0652 0.1543  582 THR A C   
8899  O O   . THR A 582 ? 1.6548 1.4650 1.4889 -0.1602 -0.0668 0.1601  582 THR A O   
8900  C CB  . THR A 582 ? 1.8313 1.4751 1.5941 -0.1684 -0.0558 0.1522  582 THR A CB  
8901  O OG1 . THR A 582 ? 1.8731 1.5406 1.6504 -0.1759 -0.0645 0.1678  582 THR A OG1 
8902  C CG2 . THR A 582 ? 1.8534 1.4170 1.5636 -0.1795 -0.0580 0.1565  582 THR A CG2 
8910  N N   . PRO A 583 ? 1.5805 1.3805 1.4098 -0.1473 -0.0602 0.1381  583 PRO A N   
8911  C CA  . PRO A 583 ? 1.4813 1.3659 1.3533 -0.1368 -0.0539 0.1266  583 PRO A CA  
8912  C C   . PRO A 583 ? 1.3546 1.2528 1.2641 -0.1177 -0.0379 0.1028  583 PRO A C   
8913  O O   . PRO A 583 ? 1.3326 1.1839 1.2438 -0.1095 -0.0257 0.0857  583 PRO A O   
8914  C CB  . PRO A 583 ? 1.5268 1.4199 1.4044 -0.1278 -0.0519 0.1115  583 PRO A CB  
8915  C CG  . PRO A 583 ? 1.5951 1.4202 1.4290 -0.1384 -0.0683 0.1248  583 PRO A CG  
8916  C CD  . PRO A 583 ? 1.6145 1.3770 1.4259 -0.1417 -0.0634 0.1283  583 PRO A CD  
8924  N N   . ALA A 584 ? 1.2559 1.2213 1.1945 -0.1116 -0.0410 0.1011  584 ALA A N   
8925  C CA  . ALA A 584 ? 1.2006 1.1757 1.1744 -0.0905 -0.0358 0.0776  584 ALA A CA  
8926  C C   . ALA A 584 ? 1.1319 1.1489 1.1401 -0.0669 -0.0257 0.0453  584 ALA A C   
8927  O O   . ALA A 584 ? 1.0986 1.1381 1.1383 -0.0459 -0.0278 0.0231  584 ALA A O   
8928  C CB  . ALA A 584 ? 1.2004 1.2259 1.1920 -0.0892 -0.0485 0.0865  584 ALA A CB  
8934  N N   . ASN A 585 ? 1.0996 1.1228 1.1010 -0.0691 -0.0190 0.0415  585 ASN A N   
8935  C CA  . ASN A 585 ? 1.0798 1.1285 1.1081 -0.0500 -0.0100 0.0124  585 ASN A CA  
8936  C C   . ASN A 585 ? 1.1029 1.0992 1.1184 -0.0539 -0.0020 0.0083  585 ASN A C   
8937  O O   . ASN A 585 ? 1.1407 1.1055 1.1272 -0.0684 -0.0060 0.0262  585 ASN A O   
8938  C CB  . ASN A 585 ? 1.0517 1.1871 1.0917 -0.0475 -0.0119 0.0085  585 ASN A CB  
8939  C CG  . ASN A 585 ? 1.0453 1.1911 1.0523 -0.0746 -0.0216 0.0392  585 ASN A CG  
8940  O OD1 . ASN A 585 ? 1.0547 1.1494 1.0394 -0.0836 -0.0249 0.0473  585 ASN A OD1 
8941  N ND2 . ASN A 585 ? 1.0150 1.2304 1.0191 -0.0882 -0.0293 0.0554  585 ASN A ND2 
8948  N N   . ILE A 586 ? 1.1069 1.0941 1.1448 -0.0399 0.0065  -0.0169 586 ILE A N   
8949  C CA  . ILE A 586 ? 1.1152 1.0717 1.1518 -0.0410 0.0154  -0.0258 586 ILE A CA  
8950  C C   . ILE A 586 ? 1.0759 1.0663 1.1426 -0.0256 0.0184  -0.0506 586 ILE A C   
8951  O O   . ILE A 586 ? 1.0742 1.0841 1.1603 -0.0129 0.0152  -0.0660 586 ILE A O   
8952  C CB  . ILE A 586 ? 1.1614 1.0578 1.1870 -0.0496 0.0241  -0.0269 586 ILE A CB  
8953  C CG1 . ILE A 586 ? 1.1918 1.0759 1.2313 -0.0463 0.0207  -0.0366 586 ILE A CG1 
8954  C CG2 . ILE A 586 ? 1.2111 1.0687 1.2002 -0.0652 0.0212  -0.0041 586 ILE A CG2 
8955  C CD1 . ILE A 586 ? 1.2249 1.0519 1.2470 -0.0638 0.0264  -0.0336 586 ILE A CD1 
8967  N N   . SER A 587 ? 1.0848 1.0787 1.1548 -0.0251 0.0209  -0.0559 587 SER A N   
8968  C CA  . SER A 587 ? 1.0664 1.0917 1.1618 -0.0131 0.0214  -0.0768 587 SER A CA  
8969  C C   . SER A 587 ? 1.0651 1.0674 1.1720 -0.0134 0.0285  -0.0876 587 SER A C   
8970  O O   . SER A 587 ? 1.0547 1.0350 1.1498 -0.0185 0.0295  -0.0801 587 SER A O   
8971  C CB  . SER A 587 ? 1.0766 1.1536 1.1679 -0.0131 0.0118  -0.0722 587 SER A CB  
8972  O OG  . SER A 587 ? 1.1216 1.1834 1.1963 -0.0230 0.0039  -0.0583 587 SER A OG  
8978  N N   . ARG A 588 ? 1.0810 1.0905 1.2119 -0.0067 0.0310  -0.1070 588 ARG A N   
8979  C CA  . ARG A 588 ? 1.0854 1.0909 1.2357 -0.0073 0.0368  -0.1195 588 ARG A CA  
8980  C C   . ARG A 588 ? 1.0940 1.1325 1.2637 0.0028  0.0286  -0.1344 588 ARG A C   
8981  O O   . ARG A 588 ? 1.1266 1.1843 1.2958 0.0110  0.0217  -0.1410 588 ARG A O   
8982  C CB  . ARG A 588 ? 1.0963 1.0732 1.2520 -0.0183 0.0459  -0.1250 588 ARG A CB  
8983  C CG  . ARG A 588 ? 1.1493 1.0945 1.2827 -0.0317 0.0560  -0.1123 588 ARG A CG  
8984  C CD  . ARG A 588 ? 1.2022 1.1524 1.3407 -0.0324 0.0667  -0.1174 588 ARG A CD  
8985  N NE  . ARG A 588 ? 1.2551 1.1778 1.3702 -0.0456 0.0786  -0.1109 588 ARG A NE  
8986  C CZ  . ARG A 588 ? 1.2585 1.1558 1.3427 -0.0463 0.0751  -0.0962 588 ARG A CZ  
8987  N NH1 . ARG A 588 ? 1.2179 1.1184 1.2924 -0.0376 0.0597  -0.0841 588 ARG A NH1 
8988  N NH2 . ARG A 588 ? 1.2777 1.1489 1.3380 -0.0591 0.0861  -0.0928 588 ARG A NH2 
9002  N N   . GLN A 589 ? 1.0465 1.0943 1.2339 0.0040  0.0280  -0.1421 589 GLN A N   
9003  C CA  . GLN A 589 ? 1.0399 1.1162 1.2419 0.0113  0.0180  -0.1543 589 GLN A CA  
9004  C C   . GLN A 589 ? 1.0257 1.0998 1.2560 0.0091  0.0202  -0.1688 589 GLN A C   
9005  O O   . GLN A 589 ? 1.0274 1.0939 1.2708 0.0027  0.0297  -0.1692 589 GLN A O   
9006  C CB  . GLN A 589 ? 1.0339 1.1292 1.2268 0.0121  0.0056  -0.1457 589 GLN A CB  
9007  C CG  . GLN A 589 ? 1.0652 1.1504 1.2726 0.0133  0.0011  -0.1466 589 GLN A CG  
9008  C CD  . GLN A 589 ? 1.0877 1.1767 1.2765 0.0113  -0.0206 -0.1335 589 GLN A CD  
9009  O OE1 . GLN A 589 ? 1.0651 1.1725 1.2291 0.0037  -0.0290 -0.1219 589 GLN A OE1 
9010  N NE2 . GLN A 589 ? 1.1032 1.1772 1.3033 0.0171  -0.0324 -0.1359 589 GLN A NE2 
9019  N N   . ALA A 590 ? 1.0244 1.1099 1.2633 0.0138  0.0110  -0.1821 590 ALA A N   
9020  C CA  . ALA A 590 ? 1.0093 1.0947 1.2729 0.0089  0.0075  -0.1943 590 ALA A CA  
9021  C C   . ALA A 590 ? 1.0003 1.1116 1.2723 0.0163  -0.0059 -0.2024 590 ALA A C   
9022  O O   . ALA A 590 ? 0.9795 1.1080 1.2330 0.0241  -0.0133 -0.2030 590 ALA A O   
9023  C CB  . ALA A 590 ? 1.0286 1.0884 1.2882 0.0051  0.0009  -0.2025 590 ALA A CB  
9029  N N   . HIS A 591 ? 1.0267 1.1460 1.3262 0.0113  -0.0094 -0.2085 591 HIS A N   
9030  C CA  . HIS A 591 ? 1.0375 1.1773 1.3461 0.0158  -0.0249 -0.2142 591 HIS A CA  
9031  C C   . HIS A 591 ? 1.0472 1.1846 1.3703 0.0112  -0.0353 -0.2275 591 HIS A C   
9032  O O   . HIS A 591 ? 1.0630 1.1842 1.3957 0.0005  -0.0317 -0.2297 591 HIS A O   
9033  C CB  . HIS A 591 ? 1.0567 1.2091 1.3885 0.0169  -0.0275 -0.2101 591 HIS A CB  
9034  C CG  . HIS A 591 ? 1.1138 1.2601 1.4246 0.0218  -0.0287 -0.1970 591 HIS A CG  
9035  N ND1 . HIS A 591 ? 1.1261 1.2565 1.4260 0.0212  -0.0137 -0.1895 591 HIS A ND1 
9036  C CD2 . HIS A 591 ? 1.1471 1.2963 1.4409 0.0235  -0.0475 -0.1880 591 HIS A CD2 
9037  C CE1 . HIS A 591 ? 1.1394 1.2613 1.4175 0.0241  -0.0237 -0.1771 591 HIS A CE1 
9038  N NE2 . HIS A 591 ? 1.1494 1.2820 1.4227 0.0240  -0.0454 -0.1748 591 HIS A NE2 
9046  N N   . ILE A 592 ? 1.0212 1.1723 1.3410 0.0157  -0.0515 -0.2344 592 ILE A N   
9047  C CA  . ILE A 592 ? 1.0178 1.1635 1.3460 0.0120  -0.0666 -0.2473 592 ILE A CA  
9048  C C   . ILE A 592 ? 1.0018 1.1643 1.3665 0.0038  -0.0739 -0.2453 592 ILE A C   
9049  O O   . ILE A 592 ? 0.9912 1.1706 1.3633 0.0082  -0.0794 -0.2398 592 ILE A O   
9050  C CB  . ILE A 592 ? 1.0394 1.1926 1.3379 0.0224  -0.0803 -0.2596 592 ILE A CB  
9051  C CG1 . ILE A 592 ? 1.0510 1.1942 1.3226 0.0347  -0.0750 -0.2688 592 ILE A CG1 
9052  C CG2 . ILE A 592 ? 1.0632 1.2085 1.3691 0.0183  -0.1004 -0.2725 592 ILE A CG2 
9053  C CD1 . ILE A 592 ? 1.0657 1.2324 1.3081 0.0487  -0.0839 -0.2865 592 ILE A CD1 
9065  N N   . LEU A 593 ? 1.0186 1.1762 1.4062 -0.0094 -0.0780 -0.2493 593 LEU A N   
9066  C CA  . LEU A 593 ? 1.0094 1.1928 1.4382 -0.0178 -0.0860 -0.2494 593 LEU A CA  
9067  C C   . LEU A 593 ? 1.0224 1.2087 1.4454 -0.0132 -0.1102 -0.2550 593 LEU A C   
9068  O O   . LEU A 593 ? 1.0129 1.1796 1.4028 -0.0101 -0.1217 -0.2632 593 LEU A O   
9069  C CB  . LEU A 593 ? 1.0093 1.1915 1.4591 -0.0403 -0.0861 -0.2492 593 LEU A CB  
9070  C CG  . LEU A 593 ? 1.0099 1.2292 1.5076 -0.0537 -0.0946 -0.2499 593 LEU A CG  
9071  C CD1 . LEU A 593 ? 1.0012 1.2668 1.5397 -0.0459 -0.0786 -0.2500 593 LEU A CD1 
9072  C CD2 . LEU A 593 ? 1.0352 1.2494 1.5405 -0.0841 -0.0988 -0.2457 593 LEU A CD2 
9084  N N   . LEU A 594 ? 1.0593 1.2706 1.5140 -0.0115 -0.1200 -0.2528 594 LEU A N   
9085  C CA  . LEU A 594 ? 1.1167 1.3296 1.5661 -0.0107 -0.1462 -0.2550 594 LEU A CA  
9086  C C   . LEU A 594 ? 1.2146 1.4486 1.7129 -0.0205 -0.1607 -0.2574 594 LEU A C   
9087  O O   . LEU A 594 ? 1.2364 1.5010 1.7814 -0.0200 -0.1520 -0.2570 594 LEU A O   
9088  C CB  . LEU A 594 ? 1.0491 1.2661 1.4856 -0.0008 -0.1552 -0.2471 594 LEU A CB  
9089  C CG  . LEU A 594 ? 0.9966 1.2025 1.3874 0.0048  -0.1416 -0.2410 594 LEU A CG  
9090  C CD1 . LEU A 594 ? 0.9892 1.1951 1.3670 0.0074  -0.1566 -0.2283 594 LEU A CD1 
9091  C CD2 . LEU A 594 ? 0.9979 1.1969 1.3443 0.0032  -0.1426 -0.2490 594 LEU A CD2 
9103  N N   . ASP A 595 ? 1.2917 1.5142 1.7795 -0.0291 -0.1830 -0.2617 595 ASP A N   
9104  C CA  . ASP A 595 ? 1.2933 1.5360 1.8257 -0.0417 -0.2010 -0.2623 595 ASP A CA  
9105  C C   . ASP A 595 ? 1.2849 1.5192 1.8047 -0.0419 -0.2327 -0.2631 595 ASP A C   
9106  O O   . ASP A 595 ? 1.2778 1.5299 1.8362 -0.0503 -0.2529 -0.2623 595 ASP A O   
9107  C CB  . ASP A 595 ? 1.3640 1.5939 1.8966 -0.0619 -0.2014 -0.2639 595 ASP A CB  
9108  C CG  . ASP A 595 ? 1.4434 1.6891 1.9959 -0.0712 -0.1747 -0.2595 595 ASP A CG  
9109  O OD1 . ASP A 595 ? 1.4593 1.7477 2.0527 -0.0657 -0.1585 -0.2580 595 ASP A OD1 
9110  O OD2 . ASP A 595 ? 1.5026 1.7161 2.0274 -0.0838 -0.1726 -0.2586 595 ASP A OD2 
9115  N N   . GLY B 1   ? 1.6146 1.6257 2.6071 -0.0868 -0.0955 0.2508  5   GLY B N   
9116  C CA  . GLY B 1   ? 1.5657 1.5653 2.4655 -0.0653 -0.0923 0.2293  5   GLY B CA  
9117  C C   . GLY B 1   ? 1.5538 1.5096 2.3261 -0.0614 -0.1024 0.2121  5   GLY B C   
9118  O O   . GLY B 1   ? 1.5589 1.5013 2.2738 -0.0583 -0.0614 0.2026  5   GLY B O   
9121  N N   . CYS B 2   ? 1.5481 1.4793 2.2767 -0.0633 -0.1572 0.2088  6   CYS B N   
9122  C CA  . CYS B 2   ? 1.5969 1.4849 2.2185 -0.0576 -0.1696 0.1933  6   CYS B CA  
9123  C C   . CYS B 2   ? 1.6404 1.4976 2.2644 -0.0764 -0.1925 0.2016  6   CYS B C   
9124  O O   . CYS B 2   ? 1.6535 1.4708 2.2068 -0.0736 -0.2194 0.1900  6   CYS B O   
9125  C CB  . CYS B 2   ? 1.6195 1.4952 2.1753 -0.0425 -0.2048 0.1764  6   CYS B CB  
9126  S SG  . CYS B 2   ? 1.6181 1.4906 2.0868 -0.0182 -0.1715 0.1571  6   CYS B SG  
9131  N N   . ALA B 3   ? 1.6137 1.4880 2.3233 -0.0959 -0.1789 0.2213  7   ALA B N   
9132  C CA  . ALA B 3   ? 1.6773 1.5240 2.3962 -0.1167 -0.1918 0.2318  7   ALA B CA  
9133  C C   . ALA B 3   ? 1.7402 1.5809 2.4520 -0.1241 -0.1409 0.2394  7   ALA B C   
9134  O O   . ALA B 3   ? 1.7881 1.6189 2.5379 -0.1455 -0.1384 0.2548  7   ALA B O   
9135  C CB  . ALA B 3   ? 1.6557 1.5251 2.4797 -0.1387 -0.2202 0.2519  7   ALA B CB  
9141  N N   . LEU B 4   ? 1.7267 1.5708 2.3855 -0.1101 -0.1015 0.2296  8   LEU B N   
9142  C CA  . LEU B 4   ? 1.7081 1.5472 2.3527 -0.1219 -0.0498 0.2371  8   LEU B CA  
9143  C C   . LEU B 4   ? 1.7310 1.5224 2.2992 -0.1284 -0.0628 0.2410  8   LEU B C   
9144  O O   . LEU B 4   ? 1.7758 1.5376 2.3007 -0.1189 -0.1063 0.2337  8   LEU B O   
9145  C CB  . LEU B 4   ? 1.6626 1.5175 2.2690 -0.1090 -0.0071 0.2246  8   LEU B CB  
9146  C CG  . LEU B 4   ? 1.6347 1.5036 2.2663 -0.1248 0.0598  0.2296  8   LEU B CG  
9147  C CD1 . LEU B 4   ? 1.6143 1.5150 2.3719 -0.1395 0.0795  0.2438  8   LEU B CD1 
9148  C CD2 . LEU B 4   ? 1.5668 1.4504 2.1657 -0.1103 0.0920  0.2124  8   LEU B CD2 
9160  N N   . GLY B 5   ? 1.7338 1.5152 2.2864 -0.1461 -0.0224 0.2531  9   GLY B N   
9161  C CA  . GLY B 5   ? 1.7495 1.4860 2.2366 -0.1555 -0.0324 0.2633  9   GLY B CA  
9162  C C   . GLY B 5   ? 1.7622 1.4722 2.1629 -0.1325 -0.0618 0.2514  9   GLY B C   
9163  O O   . GLY B 5   ? 1.7112 1.4377 2.0760 -0.1151 -0.0523 0.2376  9   GLY B O   
9167  N N   . GLY B 6   ? 1.8014 1.4699 2.1740 -0.1325 -0.0958 0.2572  10  GLY B N   
9168  C CA  . GLY B 6   ? 1.7799 1.4235 2.0908 -0.1081 -0.1259 0.2451  10  GLY B CA  
9169  C C   . GLY B 6   ? 1.7675 1.4104 2.1004 -0.0933 -0.1630 0.2253  10  GLY B C   
9170  O O   . GLY B 6   ? 1.8197 1.4607 2.2059 -0.1076 -0.1801 0.2278  10  GLY B O   
9174  N N   . ALA B 7   ? 1.7222 1.3658 2.0126 -0.0681 -0.1759 0.2064  11  ALA B N   
9175  C CA  . ALA B 7   ? 1.6835 1.3261 1.9810 -0.0565 -0.2068 0.1855  11  ALA B CA  
9176  C C   . ALA B 7   ? 1.7336 1.3331 2.0436 -0.0683 -0.2396 0.1841  11  ALA B C   
9177  O O   . ALA B 7   ? 1.7576 1.3619 2.1064 -0.0815 -0.2608 0.1804  11  ALA B O   
9178  C CB  . ALA B 7   ? 1.6501 1.3396 1.9996 -0.0611 -0.1998 0.1830  11  ALA B CB  
9184  N N   . GLU B 8   ? 1.7364 1.2912 2.0142 -0.0652 -0.2455 0.1888  12  GLU B N   
9185  C CA  . GLU B 8   ? 1.7974 1.3001 2.0763 -0.0733 -0.2747 0.1830  12  GLU B CA  
9186  C C   . GLU B 8   ? 1.8040 1.2687 2.0327 -0.0489 -0.2897 0.1591  12  GLU B C   
9187  O O   . GLU B 8   ? 1.9113 1.3218 2.1315 -0.0516 -0.3074 0.1523  12  GLU B O   
9188  C CB  . GLU B 8   ? 1.8137 1.2873 2.1065 -0.0912 -0.2689 0.2085  12  GLU B CB  
9189  C CG  . GLU B 8   ? 1.7744 1.2488 2.1255 -0.1228 -0.2773 0.2208  12  GLU B CG  
9190  C CD  . GLU B 8   ? 1.7917 1.2484 2.1587 -0.1435 -0.2625 0.2500  12  GLU B CD  
9191  O OE1 . GLU B 8   ? 1.8197 1.2632 2.1482 -0.1349 -0.2477 0.2628  12  GLU B OE1 
9192  O OE2 . GLU B 8   ? 1.8195 1.2758 2.2382 -0.1707 -0.2675 0.2623  12  GLU B OE2 
9199  N N   . THR B 9   ? 1.6629 1.1533 1.8616 -0.0256 -0.2802 0.1454  13  THR B N   
9200  C CA  . THR B 9   ? 1.5581 1.0197 1.7157 -0.0013 -0.2881 0.1212  13  THR B CA  
9201  C C   . THR B 9   ? 1.4854 0.9859 1.6250 0.0112  -0.2841 0.1028  13  THR B C   
9202  O O   . THR B 9   ? 1.3875 0.9377 1.5423 0.0088  -0.2695 0.1132  13  THR B O   
9203  C CB  . THR B 9   ? 1.5007 0.9477 1.6407 0.0183  -0.2769 0.1335  13  THR B CB  
9204  O OG1 . THR B 9   ? 1.5213 0.9363 1.6798 0.0033  -0.2803 0.1576  13  THR B OG1 
9205  C CG2 . THR B 9   ? 1.5193 0.9315 1.6331 0.0437  -0.2824 0.1085  13  THR B CG2 
9213  N N   . CYS B 10  ? 1.5449 1.0189 1.6509 0.0231  -0.2946 0.0746  14  CYS B N   
9214  C CA  . CYS B 10  ? 1.5577 1.0640 1.6415 0.0328  -0.2922 0.0576  14  CYS B CA  
9215  C C   . CYS B 10  ? 1.5143 1.0653 1.5938 0.0524  -0.2686 0.0676  14  CYS B C   
9216  O O   . CYS B 10  ? 1.4436 1.0401 1.5309 0.0506  -0.2609 0.0708  14  CYS B O   
9217  C CB  . CYS B 10  ? 1.6487 1.1127 1.6877 0.0424  -0.3001 0.0249  14  CYS B CB  
9218  S SG  . CYS B 10  ? 1.6413 1.1321 1.6478 0.0392  -0.3076 0.0043  14  CYS B SG  
9223  N N   . GLU B 11  ? 1.5379 1.0750 1.6077 0.0697  -0.2586 0.0742  15  GLU B N   
9224  C CA  . GLU B 11  ? 1.5456 1.1219 1.6076 0.0835  -0.2406 0.0865  15  GLU B CA  
9225  C C   . GLU B 11  ? 1.5127 1.1214 1.5943 0.0652  -0.2277 0.1115  15  GLU B C   
9226  O O   . GLU B 11  ? 1.4995 1.1484 1.5739 0.0674  -0.2116 0.1147  15  GLU B O   
9227  C CB  . GLU B 11  ? 1.6589 1.2114 1.7145 0.1023  -0.2393 0.0941  15  GLU B CB  
9228  C CG  . GLU B 11  ? 1.7408 1.3296 1.7828 0.1188  -0.2275 0.1013  15  GLU B CG  
9229  C CD  . GLU B 11  ? 1.8413 1.4078 1.8904 0.1367  -0.2318 0.1138  15  GLU B CD  
9230  O OE1 . GLU B 11  ? 1.9051 1.4252 1.9704 0.1377  -0.2415 0.1160  15  GLU B OE1 
9231  O OE2 . GLU B 11  ? 1.8336 1.4282 1.8766 0.1491  -0.2271 0.1230  15  GLU B OE2 
9238  N N   . ASP B 12  ? 1.5153 1.1041 1.6206 0.0454  -0.2314 0.1281  16  ASP B N   
9239  C CA  . ASP B 12  ? 1.4767 1.0936 1.6032 0.0249  -0.2130 0.1489  16  ASP B CA  
9240  C C   . ASP B 12  ? 1.4667 1.1212 1.6207 0.0173  -0.2072 0.1400  16  ASP B C   
9241  O O   . ASP B 12  ? 1.3636 1.0536 1.5263 0.0119  -0.1827 0.1474  16  ASP B O   
9242  C CB  . ASP B 12  ? 1.4651 1.0518 1.6161 0.0036  -0.2180 0.1677  16  ASP B CB  
9243  C CG  . ASP B 12  ? 1.4495 1.0085 1.5784 0.0051  -0.2173 0.1887  16  ASP B CG  
9244  O OD1 . ASP B 12  ? 1.4208 0.9864 1.5196 0.0226  -0.2152 0.1899  16  ASP B OD1 
9245  O OD2 . ASP B 12  ? 1.4633 0.9945 1.6080 -0.0129 -0.2211 0.2068  16  ASP B OD2 
9250  N N   . CYS B 13  ? 1.5435 1.1873 1.7112 0.0150  -0.2299 0.1249  17  CYS B N   
9251  C CA  . CYS B 13  ? 1.5703 1.2487 1.7703 0.0073  -0.2322 0.1211  17  CYS B CA  
9252  C C   . CYS B 13  ? 1.5250 1.2342 1.7004 0.0253  -0.2221 0.1086  17  CYS B C   
9253  O O   . CYS B 13  ? 1.4929 1.2389 1.6994 0.0211  -0.2126 0.1120  17  CYS B O   
9254  C CB  . CYS B 13  ? 1.6187 1.2725 1.8285 -0.0043 -0.2662 0.1105  17  CYS B CB  
9255  S SG  . CYS B 13  ? 1.5548 1.2478 1.8036 -0.0146 -0.2812 0.1101  17  CYS B SG  
9260  N N   . LEU B 14  ? 1.5385 1.2336 1.6650 0.0453  -0.2232 0.0952  18  LEU B N   
9261  C CA  . LEU B 14  ? 1.4868 1.2102 1.5899 0.0609  -0.2148 0.0832  18  LEU B CA  
9262  C C   . LEU B 14  ? 1.4362 1.1955 1.5451 0.0608  -0.1856 0.0953  18  LEU B C   
9263  O O   . LEU B 14  ? 1.4187 1.2087 1.5315 0.0648  -0.1761 0.0900  18  LEU B O   
9264  C CB  . LEU B 14  ? 1.4831 1.1850 1.5411 0.0819  -0.2192 0.0673  18  LEU B CB  
9265  C CG  . LEU B 14  ? 1.5345 1.2025 1.5699 0.0847  -0.2397 0.0444  18  LEU B CG  
9266  C CD1 . LEU B 14  ? 1.5235 1.1800 1.5238 0.1084  -0.2320 0.0286  18  LEU B CD1 
9267  C CD2 . LEU B 14  ? 1.5302 1.2145 1.5669 0.0739  -0.2529 0.0359  18  LEU B CD2 
9279  N N   . LEU B 15  ? 1.4338 1.1858 1.5392 0.0537  -0.1708 0.1115  19  LEU B N   
9280  C CA  . LEU B 15  ? 1.4442 1.2207 1.5364 0.0499  -0.1420 0.1202  19  LEU B CA  
9281  C C   . LEU B 15  ? 1.4738 1.2725 1.6084 0.0316  -0.1169 0.1281  19  LEU B C   
9282  O O   . LEU B 15  ? 1.3914 1.2113 1.5165 0.0284  -0.0888 0.1279  19  LEU B O   
9283  C CB  . LEU B 15  ? 1.4524 1.2082 1.5124 0.0460  -0.1387 0.1365  19  LEU B CB  
9284  C CG  . LEU B 15  ? 1.4653 1.2369 1.4963 0.0336  -0.1110 0.1476  19  LEU B CG  
9285  C CD1 . LEU B 15  ? 1.4230 1.2238 1.4349 0.0450  -0.1010 0.1332  19  LEU B CD1 
9286  C CD2 . LEU B 15  ? 1.5116 1.2598 1.5052 0.0293  -0.1198 0.1672  19  LEU B CD2 
9298  N N   . ILE B 16  ? 1.5359 1.3294 1.7207 0.0186  -0.1244 0.1345  20  ILE B N   
9299  C CA  . ILE B 16  ? 1.5634 1.3802 1.8013 0.0021  -0.0953 0.1437  20  ILE B CA  
9300  C C   . ILE B 16  ? 1.5324 1.3831 1.7996 0.0104  -0.0860 0.1341  20  ILE B C   
9301  O O   . ILE B 16  ? 1.6464 1.5174 1.9379 0.0035  -0.0490 0.1363  20  ILE B O   
9302  C CB  . ILE B 16  ? 1.6157 1.4235 1.9122 -0.0147 -0.1074 0.1558  20  ILE B CB  
9303  C CG1 . ILE B 16  ? 1.5847 1.3890 1.9042 -0.0099 -0.1489 0.1482  20  ILE B CG1 
9304  C CG2 . ILE B 16  ? 1.6723 1.4444 1.9412 -0.0251 -0.1116 0.1678  20  ILE B CG2 
9305  C CD1 . ILE B 16  ? 1.5471 1.3415 1.9236 -0.0298 -0.1671 0.1608  20  ILE B CD1 
9317  N N   . GLY B 17  ? 1.4187 1.2727 1.6813 0.0239  -0.1167 0.1233  21  GLY B N   
9318  C CA  . GLY B 17  ? 1.3874 1.2706 1.6761 0.0311  -0.1130 0.1175  21  GLY B CA  
9319  C C   . GLY B 17  ? 1.3794 1.2581 1.6298 0.0456  -0.1448 0.1040  21  GLY B C   
9320  O O   . GLY B 17  ? 1.4195 1.2704 1.6290 0.0497  -0.1691 0.0967  21  GLY B O   
9324  N N   . PRO B 18  ? 1.3851 1.2875 1.6471 0.0527  -0.1424 0.0997  22  PRO B N   
9325  C CA  . PRO B 18  ? 1.4034 1.3008 1.6245 0.0631  -0.1702 0.0875  22  PRO B CA  
9326  C C   . PRO B 18  ? 1.4140 1.3099 1.6664 0.0529  -0.2075 0.0929  22  PRO B C   
9327  O O   . PRO B 18  ? 1.4248 1.3070 1.6316 0.0559  -0.2326 0.0818  22  PRO B O   
9328  C CB  . PRO B 18  ? 1.4218 1.3440 1.6345 0.0734  -0.1470 0.0824  22  PRO B CB  
9329  C CG  . PRO B 18  ? 1.4275 1.3709 1.7085 0.0650  -0.1183 0.0945  22  PRO B CG  
9330  C CD  . PRO B 18  ? 1.4092 1.3400 1.7112 0.0524  -0.1077 0.1036  22  PRO B CD  
9338  N N   . GLN B 19  ? 1.4388 1.3477 1.7670 0.0385  -0.2123 0.1105  23  GLN B N   
9339  C CA  . GLN B 19  ? 1.4614 1.3717 1.8262 0.0242  -0.2538 0.1214  23  GLN B CA  
9340  C C   . GLN B 19  ? 1.5021 1.3835 1.8673 0.0070  -0.2824 0.1245  23  GLN B C   
9341  O O   . GLN B 19  ? 1.5664 1.4473 1.9651 -0.0110 -0.3203 0.1365  23  GLN B O   
9342  C CB  . GLN B 19  ? 1.4703 1.4187 1.9361 0.0188  -0.2455 0.1433  23  GLN B CB  
9343  C CG  . GLN B 19  ? 1.5675 1.5244 2.0817 0.0029  -0.2936 0.1617  23  GLN B CG  
9344  C CD  . GLN B 19  ? 1.5946 1.5918 2.2222 0.0016  -0.2834 0.1859  23  GLN B CD  
9345  O OE1 . GLN B 19  ? 1.6179 1.6323 2.3209 -0.0002 -0.2518 0.1957  23  GLN B OE1 
9346  N NE2 . GLN B 19  ? 1.5747 1.5857 2.2201 0.0008  -0.3108 0.1974  23  GLN B NE2 
9355  N N   . CYS B 20  ? 1.4822 1.3375 1.8106 0.0100  -0.2684 0.1155  24  CYS B N   
9356  C CA  . CYS B 20  ? 1.5325 1.3594 1.8709 -0.0072 -0.2899 0.1200  24  CYS B CA  
9357  C C   . CYS B 20  ? 1.5279 1.3079 1.7866 -0.0070 -0.3156 0.0991  24  CYS B C   
9358  O O   . CYS B 20  ? 1.5193 1.2883 1.7146 0.0108  -0.3053 0.0806  24  CYS B O   
9359  C CB  . CYS B 20  ? 1.5827 1.4083 1.9409 -0.0070 -0.2563 0.1276  24  CYS B CB  
9360  S SG  . CYS B 20  ? 1.5802 1.4544 1.9988 -0.0012 -0.2091 0.1396  24  CYS B SG  
9365  N N   . ALA B 21  ? 1.5157 1.2669 1.7815 -0.0287 -0.3480 0.1015  25  ALA B N   
9366  C CA  . ALA B 21  ? 1.5295 1.2283 1.7229 -0.0349 -0.3730 0.0795  25  ALA B CA  
9367  C C   . ALA B 21  ? 1.4944 1.1536 1.6891 -0.0443 -0.3754 0.0786  25  ALA B C   
9368  O O   . ALA B 21  ? 1.4366 1.1111 1.6865 -0.0479 -0.3601 0.0972  25  ALA B O   
9369  C CB  . ALA B 21  ? 1.5930 1.2842 1.7781 -0.0596 -0.4176 0.0809  25  ALA B CB  
9375  N N   . TRP B 22  ? 1.5063 1.1103 1.6374 -0.0497 -0.3924 0.0557  26  TRP B N   
9376  C CA  . TRP B 22  ? 1.5484 1.1030 1.6721 -0.0590 -0.3976 0.0507  26  TRP B CA  
9377  C C   . TRP B 22  ? 1.7217 1.2257 1.8033 -0.0870 -0.4359 0.0342  26  TRP B C   
9378  O O   . TRP B 22  ? 1.7501 1.2443 1.7788 -0.0917 -0.4498 0.0177  26  TRP B O   
9379  C CB  . TRP B 22  ? 1.5018 1.0298 1.5846 -0.0309 -0.3678 0.0349  26  TRP B CB  
9380  C CG  . TRP B 22  ? 1.5116 0.9905 1.5964 -0.0362 -0.3687 0.0342  26  TRP B CG  
9381  C CD1 . TRP B 22  ? 1.6304 1.0445 1.6678 -0.0374 -0.3759 0.0092  26  TRP B CD1 
9382  C CD2 . TRP B 22  ? 1.4978 0.9846 1.6344 -0.0420 -0.3595 0.0596  26  TRP B CD2 
9383  N NE1 . TRP B 22  ? 1.6181 0.9992 1.6790 -0.0422 -0.3745 0.0189  26  TRP B NE1 
9384  C CE2 . TRP B 22  ? 1.5660 0.9917 1.6854 -0.0461 -0.3656 0.0510  26  TRP B CE2 
9385  C CE3 . TRP B 22  ? 1.4526 0.9890 1.6467 -0.0455 -0.3434 0.0878  26  TRP B CE3 
9386  C CZ2 . TRP B 22  ? 1.5897 1.0041 1.7468 -0.0543 -0.3602 0.0730  26  TRP B CZ2 
9387  C CZ3 . TRP B 22  ? 1.5037 1.0287 1.7304 -0.0551 -0.3347 0.1074  26  TRP B CZ3 
9388  C CH2 . TRP B 22  ? 1.5698 1.0352 1.7775 -0.0597 -0.3451 0.1015  26  TRP B CH2 
9399  N N   . CYS B 23  ? 1.8829 1.3515 1.9830 -0.1091 -0.4531 0.0388  27  CYS B N   
9400  C CA  . CYS B 23  ? 2.0320 1.4463 2.0910 -0.1426 -0.4917 0.0237  27  CYS B CA  
9401  C C   . CYS B 23  ? 1.8895 1.2319 1.9093 -0.1419 -0.4834 0.0015  27  CYS B C   
9402  O O   . CYS B 23  ? 1.8856 1.2276 1.9373 -0.1238 -0.4584 0.0108  27  CYS B O   
9403  C CB  . CYS B 23  ? 2.1736 1.6117 2.3020 -0.1781 -0.5290 0.0531  27  CYS B CB  
9404  S SG  . CYS B 23  ? 2.2074 1.5822 2.2840 -0.2285 -0.5858 0.0397  27  CYS B SG  
9409  N N   . ALA B 24  ? 1.7575 1.0349 1.7061 -0.1641 -0.5046 -0.0276 28  ALA B N   
9410  C CA  . ALA B 24  ? 1.8170 1.0167 1.7241 -0.1629 -0.4934 -0.0545 28  ALA B CA  
9411  C C   . ALA B 24  ? 1.9212 1.0609 1.8034 -0.2092 -0.5329 -0.0636 28  ALA B C   
9412  O O   . ALA B 24  ? 1.9763 1.1034 1.8127 -0.2414 -0.5660 -0.0722 28  ALA B O   
9413  C CB  . ALA B 24  ? 1.8281 0.9913 1.6587 -0.1382 -0.4643 -0.0928 28  ALA B CB  
9419  N N   . GLN B 25  ? 1.9671 1.0685 1.8781 -0.2145 -0.5306 -0.0598 29  GLN B N   
9420  C CA  . GLN B 25  ? 2.0852 1.1113 1.9712 -0.2527 -0.5575 -0.0738 29  GLN B CA  
9421  C C   . GLN B 25  ? 2.1068 1.1532 2.0341 -0.3004 -0.6081 -0.0469 29  GLN B C   
9422  O O   . GLN B 25  ? 2.1774 1.1598 2.0784 -0.3381 -0.6358 -0.0588 29  GLN B O   
9423  C CB  . GLN B 25  ? 2.1894 1.1308 1.9670 -0.2650 -0.5559 -0.1236 29  GLN B CB  
9424  C CG  . GLN B 25  ? 2.3015 1.1475 2.0441 -0.2992 -0.5719 -0.1465 29  GLN B CG  
9425  C CD  . GLN B 25  ? 2.2629 1.0935 2.0731 -0.2837 -0.5555 -0.1298 29  GLN B CD  
9426  O OE1 . GLN B 25  ? 2.1744 1.0661 2.0694 -0.2809 -0.5622 -0.0880 29  GLN B OE1 
9427  N NE2 . GLN B 25  ? 2.3224 1.0679 2.0953 -0.2752 -0.5324 -0.1624 29  GLN B NE2 
9436  N N   . GLU B 26  ? 2.0461 1.1773 2.0433 -0.3012 -0.6208 -0.0104 30  GLU B N   
9437  C CA  . GLU B 26  ? 2.0577 1.2186 2.1167 -0.3437 -0.6682 0.0212  30  GLU B CA  
9438  C C   . GLU B 26  ? 2.1605 1.2525 2.1564 -0.3968 -0.7183 0.0035  30  GLU B C   
9439  O O   . GLU B 26  ? 2.1832 1.2582 2.2205 -0.4317 -0.7481 0.0190  30  GLU B O   
9440  C CB  . GLU B 26  ? 1.9942 1.1825 2.1525 -0.3428 -0.6574 0.0535  30  GLU B CB  
9441  C CG  . GLU B 26  ? 1.8725 1.1557 2.1253 -0.3196 -0.6352 0.0901  30  GLU B CG  
9442  C CD  . GLU B 26  ? 1.8355 1.1528 2.1943 -0.3393 -0.6407 0.1273  30  GLU B CD  
9443  O OE1 . GLU B 26  ? 1.8230 1.1232 2.2005 -0.3280 -0.6117 0.1321  30  GLU B OE1 
9444  O OE2 . GLU B 26  ? 1.8141 1.1756 2.2411 -0.3671 -0.6744 0.1539  30  GLU B OE2 
9451  N N   . ASN B 27  ? 2.2165 1.2689 2.1104 -0.4075 -0.7290 -0.0278 31  ASN B N   
9452  C CA  . ASN B 27  ? 2.3733 1.3528 2.1861 -0.4632 -0.7763 -0.0483 31  ASN B CA  
9453  C C   . ASN B 27  ? 2.4123 1.4321 2.2931 -0.5115 -0.8397 -0.0066 31  ASN B C   
9454  O O   . ASN B 27  ? 2.5283 1.5116 2.3793 -0.5490 -0.8670 -0.0083 31  ASN B O   
9455  C CB  . ASN B 27  ? 2.3811 1.3266 2.0751 -0.4672 -0.7744 -0.0828 31  ASN B CB  
9456  C CG  . ASN B 27  ? 2.5362 1.4138 2.1302 -0.5222 -0.8122 -0.1036 31  ASN B CG  
9457  O OD1 . ASN B 27  ? 2.5656 1.4766 2.1923 -0.5572 -0.8564 -0.0701 31  ASN B OD1 
9458  N ND2 . ASN B 27  ? 2.6138 1.4124 2.0912 -0.5202 -0.7799 -0.1548 31  ASN B ND2 
9465  N N   . GLY B 35  ? 1.8946 1.2990 2.3399 -0.2186 -0.4392 0.1784  39  GLY B N   
9466  C CA  . GLY B 35  ? 1.8161 1.2833 2.3375 -0.2236 -0.4119 0.2087  39  GLY B CA  
9467  C C   . GLY B 35  ? 1.7359 1.2594 2.2562 -0.1973 -0.3834 0.2075  39  GLY B C   
9468  O O   . GLY B 35  ? 1.7334 1.2621 2.2229 -0.1751 -0.3486 0.2083  39  GLY B O   
9471  N N   . GLU B 36  ? 1.7199 1.2842 2.2741 -0.2020 -0.4006 0.2074  40  GLU B N   
9472  C CA  . GLU B 36  ? 1.6567 1.2744 2.2190 -0.1794 -0.3756 0.2069  40  GLU B CA  
9473  C C   . GLU B 36  ? 1.6180 1.2327 2.1394 -0.1738 -0.4088 0.1871  40  GLU B C   
9474  O O   . GLU B 36  ? 1.5417 1.1930 2.1141 -0.1856 -0.4301 0.1975  40  GLU B O   
9475  C CB  . GLU B 36  ? 1.6936 1.3731 2.3603 -0.1913 -0.3543 0.2342  40  GLU B CB  
9476  C CG  . GLU B 36  ? 1.6854 1.4125 2.3615 -0.1676 -0.3106 0.2347  40  GLU B CG  
9477  C CD  . GLU B 36  ? 1.6876 1.3960 2.2937 -0.1480 -0.2715 0.2266  40  GLU B CD  
9478  O OE1 . GLU B 36  ? 1.6845 1.3592 2.2083 -0.1299 -0.2829 0.2067  40  GLU B OE1 
9479  O OE2 . GLU B 36  ? 1.6724 1.3991 2.3064 -0.1527 -0.2292 0.2411  40  GLU B OE2 
9486  N N   . ARG B 37  ? 1.6099 1.1800 2.0407 -0.1563 -0.4123 0.1599  41  ARG B N   
9487  C CA  . ARG B 37  ? 1.6449 1.2042 2.0200 -0.1513 -0.4370 0.1376  41  ARG B CA  
9488  C C   . ARG B 37  ? 1.6545 1.2613 2.0236 -0.1254 -0.4136 0.1355  41  ARG B C   
9489  O O   . ARG B 37  ? 1.6305 1.2369 1.9606 -0.1229 -0.4326 0.1214  41  ARG B O   
9490  C CB  . ARG B 37  ? 1.6350 1.1255 1.9207 -0.1424 -0.4420 0.1071  41  ARG B CB  
9491  C CG  . ARG B 37  ? 1.6190 1.0517 1.9028 -0.1654 -0.4605 0.1055  41  ARG B CG  
9492  C CD  . ARG B 37  ? 1.6083 0.9743 1.8159 -0.1484 -0.4517 0.0762  41  ARG B CD  
9493  N NE  . ARG B 37  ? 1.6407 0.9413 1.8036 -0.1743 -0.4847 0.0532  41  ARG B NE  
9494  C CZ  . ARG B 37  ? 1.6822 0.9339 1.8562 -0.1979 -0.5002 0.0553  41  ARG B CZ  
9495  N NH1 . ARG B 37  ? 1.6542 0.9169 1.8851 -0.1986 -0.4859 0.0816  41  ARG B NH1 
9496  N NH2 . ARG B 37  ? 1.7812 0.9692 1.9044 -0.2239 -0.5294 0.0304  41  ARG B NH2 
9510  N N   . CYS B 38  ? 1.6844 1.3280 2.0858 -0.1093 -0.3726 0.1487  42  CYS B N   
9511  C CA  . CYS B 38  ? 1.7179 1.3999 2.1068 -0.0845 -0.3453 0.1445  42  CYS B CA  
9512  C C   . CYS B 38  ? 1.8201 1.5591 2.2924 -0.0921 -0.3411 0.1647  42  CYS B C   
9513  O O   . CYS B 38  ? 1.9109 1.6778 2.4488 -0.0978 -0.3130 0.1835  42  CYS B O   
9514  C CB  . CYS B 38  ? 1.6639 1.3458 2.0300 -0.0662 -0.3035 0.1461  42  CYS B CB  
9515  S SG  . CYS B 38  ? 1.5626 1.2892 1.9136 -0.0411 -0.2676 0.1421  42  CYS B SG  
9520  N N   . ASP B 39  ? 1.8821 1.6369 2.3532 -0.0926 -0.3667 0.1612  43  ASP B N   
9521  C CA  . ASP B 39  ? 1.8757 1.6841 2.4316 -0.0965 -0.3659 0.1817  43  ASP B CA  
9522  C C   . ASP B 39  ? 1.8446 1.6604 2.3608 -0.0876 -0.3865 0.1719  43  ASP B C   
9523  O O   . ASP B 39  ? 1.9096 1.6900 2.3335 -0.0800 -0.3975 0.1483  43  ASP B O   
9524  C CB  . ASP B 39  ? 1.9940 1.8149 2.6393 -0.1268 -0.3980 0.2066  43  ASP B CB  
9525  C CG  . ASP B 39  ? 2.1448 1.9749 2.8550 -0.1355 -0.3671 0.2223  43  ASP B CG  
9526  O OD1 . ASP B 39  ? 2.1918 2.0362 2.9029 -0.1192 -0.3155 0.2207  43  ASP B OD1 
9527  O OD2 . ASP B 39  ? 2.2373 2.0590 2.9951 -0.1620 -0.3948 0.2370  43  ASP B OD2 
9532  N N   . THR B 40  ? 1.7193 1.5810 2.3111 -0.0890 -0.3899 0.1913  44  THR B N   
9533  C CA  . THR B 40  ? 1.6974 1.5700 2.2626 -0.0830 -0.4103 0.1883  44  THR B CA  
9534  C C   . THR B 40  ? 1.6981 1.5291 2.1905 -0.1035 -0.4642 0.1782  44  THR B C   
9535  O O   . THR B 40  ? 1.6551 1.4634 2.1595 -0.1295 -0.4969 0.1849  44  THR B O   
9536  C CB  . THR B 40  ? 1.6546 1.5790 2.3323 -0.0874 -0.4162 0.2181  44  THR B CB  
9537  O OG1 . THR B 40  ? 1.6827 1.6115 2.4279 -0.1176 -0.4635 0.2427  44  THR B OG1 
9538  C CG2 . THR B 40  ? 1.5816 1.5418 2.3360 -0.0715 -0.3569 0.2256  44  THR B CG2 
9546  N N   . PRO B 41  ? 1.6844 1.5017 2.0976 -0.0958 -0.4738 0.1616  45  PRO B N   
9547  C CA  . PRO B 41  ? 1.7264 1.4954 2.0548 -0.1188 -0.5188 0.1472  45  PRO B CA  
9548  C C   . PRO B 41  ? 1.7397 1.5135 2.1145 -0.1560 -0.5776 0.1740  45  PRO B C   
9549  O O   . PRO B 41  ? 1.8306 1.5586 2.1549 -0.1846 -0.6141 0.1655  45  PRO B O   
9550  C CB  . PRO B 41  ? 1.7366 1.5008 1.9853 -0.1025 -0.5092 0.1284  45  PRO B CB  
9551  C CG  . PRO B 41  ? 1.6899 1.5075 2.0018 -0.0774 -0.4747 0.1421  45  PRO B CG  
9552  C CD  . PRO B 41  ? 1.6465 1.4853 2.0341 -0.0678 -0.4404 0.1519  45  PRO B CD  
9560  N N   . ALA B 42  ? 1.6737 1.4997 2.1452 -0.1581 -0.5894 0.2069  46  ALA B N   
9561  C CA  . ALA B 42  ? 1.7165 1.5517 2.2440 -0.1950 -0.6515 0.2389  46  ALA B CA  
9562  C C   . ALA B 42  ? 1.7427 1.5700 2.3269 -0.2175 -0.6665 0.2500  46  ALA B C   
9563  O O   . ALA B 42  ? 1.8343 1.6352 2.4023 -0.2559 -0.7230 0.2593  46  ALA B O   
9564  C CB  . ALA B 42  ? 1.6586 1.5557 2.3020 -0.1881 -0.6560 0.2757  46  ALA B CB  
9570  N N   . ASN B 43  ? 1.6828 1.5301 2.3290 -0.1975 -0.6171 0.2498  47  ASN B N   
9571  C CA  . ASN B 43  ? 1.7050 1.5465 2.4099 -0.2189 -0.6270 0.2620  47  ASN B CA  
9572  C C   . ASN B 43  ? 1.8137 1.5846 2.4097 -0.2382 -0.6486 0.2342  47  ASN B C   
9573  O O   . ASN B 43  ? 1.8889 1.6413 2.5087 -0.2722 -0.6880 0.2459  47  ASN B O   
9574  C CB  . ASN B 43  ? 1.6199 1.4905 2.3946 -0.1945 -0.5634 0.2644  47  ASN B CB  
9575  C CG  . ASN B 43  ? 1.5715 1.5084 2.4701 -0.1800 -0.5371 0.2915  47  ASN B CG  
9576  O OD1 . ASN B 43  ? 1.5481 1.5050 2.4709 -0.1548 -0.4765 0.2851  47  ASN B OD1 
9577  N ND2 . ASN B 43  ? 1.5647 1.5329 2.5418 -0.1976 -0.5827 0.3225  47  ASN B ND2 
9584  N N   . LEU B 44  ? 1.8227 1.5524 2.3035 -0.2174 -0.6224 0.1973  48  LEU B N   
9585  C CA  . LEU B 44  ? 1.9240 1.5824 2.3066 -0.2319 -0.6346 0.1677  48  LEU B CA  
9586  C C   . LEU B 44  ? 2.0697 1.6892 2.3898 -0.2723 -0.6967 0.1648  48  LEU B C   
9587  O O   . LEU B 44  ? 2.1704 1.7389 2.4546 -0.3027 -0.7249 0.1553  48  LEU B O   
9588  C CB  . LEU B 44  ? 1.8885 1.5170 2.1775 -0.1976 -0.5891 0.1313  48  LEU B CB  
9589  C CG  . LEU B 44  ? 1.8139 1.4810 2.1458 -0.1593 -0.5307 0.1344  48  LEU B CG  
9590  C CD1 . LEU B 44  ? 1.8324 1.4596 2.0757 -0.1329 -0.4964 0.1014  48  LEU B CD1 
9591  C CD2 . LEU B 44  ? 1.7956 1.4860 2.2228 -0.1653 -0.5164 0.1581  48  LEU B CD2 
9603  N N   . LEU B 45  ? 2.0726 1.7115 2.3738 -0.2764 -0.7194 0.1732  49  LEU B N   
9604  C CA  . LEU B 45  ? 2.1628 1.7675 2.4050 -0.3216 -0.7838 0.1771  49  LEU B CA  
9605  C C   . LEU B 45  ? 2.2684 1.8962 2.6103 -0.3605 -0.8376 0.2172  49  LEU B C   
9606  O O   . LEU B 45  ? 2.5300 2.1108 2.8204 -0.4060 -0.8900 0.2153  49  LEU B O   
9607  C CB  . LEU B 45  ? 2.0910 1.7162 2.2991 -0.3181 -0.7968 0.1839  49  LEU B CB  
9608  C CG  . LEU B 45  ? 2.0430 1.6334 2.1289 -0.2935 -0.7585 0.1427  49  LEU B CG  
9609  C CD1 . LEU B 45  ? 2.0020 1.6250 2.0791 -0.2879 -0.7679 0.1574  49  LEU B CD1 
9610  C CD2 . LEU B 45  ? 2.1438 1.6494 2.0947 -0.3229 -0.7752 0.1053  49  LEU B CD2 
9622  N N   . ALA B 46  ? 2.0945 1.7932 2.5809 -0.3451 -0.8241 0.2532  50  ALA B N   
9623  C CA  . ALA B 46  ? 2.1210 1.8499 2.7234 -0.3792 -0.8706 0.2945  50  ALA B CA  
9624  C C   . ALA B 46  ? 2.1832 1.8710 2.7788 -0.4001 -0.8737 0.2832  50  ALA B C   
9625  O O   . ALA B 46  ? 2.2521 1.9315 2.8765 -0.4381 -0.9215 0.3057  50  ALA B O   
9626  C CB  . ALA B 46  ? 2.0353 1.8474 2.7997 -0.3531 -0.8408 0.3307  50  ALA B CB  
9632  N N   . LYS B 47  ? 2.1683 1.8282 2.7190 -0.3707 -0.8163 0.2509  51  LYS B N   
9633  C CA  . LYS B 47  ? 2.2456 1.8653 2.7941 -0.3861 -0.8126 0.2410  51  LYS B CA  
9634  C C   . LYS B 47  ? 2.2526 1.7808 2.6527 -0.4021 -0.8242 0.1977  51  LYS B C   
9635  O O   . LYS B 47  ? 2.2672 1.7517 2.6489 -0.4059 -0.8095 0.1816  51  LYS B O   
9636  C CB  . LYS B 47  ? 2.2114 1.8570 2.8151 -0.3471 -0.7437 0.2389  51  LYS B CB  
9637  C CG  . LYS B 47  ? 2.0561 1.7849 2.8098 -0.3354 -0.7242 0.2781  51  LYS B CG  
9638  C CD  . LYS B 47  ? 1.8562 1.6025 2.6484 -0.3041 -0.6552 0.2744  51  LYS B CD  
9639  C CE  . LYS B 47  ? 1.6757 1.4993 2.6146 -0.2952 -0.6289 0.3094  51  LYS B CE  
9640  N NZ  . LYS B 47  ? 1.5500 1.3857 2.5175 -0.2723 -0.5607 0.3060  51  LYS B NZ  
9654  N N   . GLY B 48  ? 2.2706 1.7662 2.5654 -0.4120 -0.8470 0.1781  52  GLY B N   
9655  C CA  . GLY B 48  ? 2.3667 1.7717 2.5248 -0.4392 -0.8657 0.1389  52  GLY B CA  
9656  C C   . GLY B 48  ? 2.4208 1.7791 2.4688 -0.4039 -0.8130 0.0914  52  GLY B C   
9657  O O   . GLY B 48  ? 2.5338 1.8114 2.4707 -0.4236 -0.8188 0.0541  52  GLY B O   
9661  N N   . CYS B 49  ? 2.4043 1.8087 2.4810 -0.3540 -0.7612 0.0908  53  CYS B N   
9662  C CA  . CYS B 49  ? 2.3422 1.7103 2.3272 -0.3195 -0.7127 0.0499  53  CYS B CA  
9663  C C   . CYS B 49  ? 2.3508 1.6981 2.2371 -0.3313 -0.7290 0.0323  53  CYS B C   
9664  O O   . CYS B 49  ? 2.2647 1.6654 2.1825 -0.3290 -0.7431 0.0566  53  CYS B O   
9665  C CB  . CYS B 49  ? 2.1804 1.6064 2.2294 -0.2681 -0.6576 0.0590  53  CYS B CB  
9666  S SG  . CYS B 49  ? 2.1071 1.5545 2.2617 -0.2603 -0.6371 0.0818  53  CYS B SG  
9671  N N   . GLN B 50  ? 2.4359 1.7030 2.2034 -0.3449 -0.7245 -0.0101 54  GLN B N   
9672  C CA  . GLN B 50  ? 2.5154 1.7526 2.1752 -0.3635 -0.7384 -0.0298 54  GLN B CA  
9673  C C   . GLN B 50  ? 2.5023 1.7735 2.1474 -0.3165 -0.6888 -0.0411 54  GLN B C   
9674  O O   . GLN B 50  ? 2.5388 1.8317 2.2252 -0.2711 -0.6391 -0.0477 54  GLN B O   
9675  C CB  . GLN B 50  ? 2.5758 1.7106 2.1100 -0.3939 -0.7401 -0.0763 54  GLN B CB  
9676  C CG  . GLN B 50  ? 2.5728 1.6641 2.1056 -0.4474 -0.7931 -0.0685 54  GLN B CG  
9677  C CD  . GLN B 50  ? 2.6471 1.6285 2.0518 -0.4768 -0.7872 -0.1200 54  GLN B CD  
9678  O OE1 . GLN B 50  ? 2.6722 1.6092 1.9791 -0.4647 -0.7495 -0.1607 54  GLN B OE1 
9679  N NE2 . GLN B 50  ? 2.6898 1.6401 2.1046 -0.5073 -0.8091 -0.1151 54  GLN B NE2 
9688  N N   . LEU B 51  ? 2.4559 1.7303 2.0384 -0.3314 -0.7059 -0.0414 55  LEU B N   
9689  C CA  . LEU B 51  ? 2.4229 1.7312 1.9906 -0.2922 -0.6640 -0.0496 55  LEU B CA  
9690  C C   . LEU B 51  ? 2.4589 1.7261 1.9741 -0.2578 -0.6036 -0.0940 55  LEU B C   
9691  O O   . LEU B 51  ? 2.3739 1.6831 1.9357 -0.2115 -0.5598 -0.0930 55  LEU B O   
9692  C CB  . LEU B 51  ? 2.4707 1.7695 1.9562 -0.3223 -0.6936 -0.0481 55  LEU B CB  
9693  C CG  . LEU B 51  ? 2.5084 1.8447 2.0450 -0.3600 -0.7610 0.0000  55  LEU B CG  
9694  C CD1 . LEU B 51  ? 2.6470 1.9424 2.0668 -0.4058 -0.7996 -0.0048 55  LEU B CD1 
9695  C CD2 . LEU B 51  ? 2.3791 1.8063 2.0379 -0.3250 -0.7516 0.0397  55  LEU B CD2 
9707  N N   . ASN B 52  ? 2.5519 1.7349 1.9720 -0.2814 -0.6009 -0.1330 56  ASN B N   
9708  C CA  . ASN B 52  ? 2.5539 1.6942 1.9342 -0.2486 -0.5426 -0.1751 56  ASN B CA  
9709  C C   . ASN B 52  ? 2.4489 1.6135 1.9252 -0.2101 -0.5154 -0.1645 56  ASN B C   
9710  O O   . ASN B 52  ? 2.3747 1.5506 1.8671 -0.1667 -0.4674 -0.1774 56  ASN B O   
9711  C CB  . ASN B 52  ? 2.7090 1.7475 1.9777 -0.2847 -0.5440 -0.2193 56  ASN B CB  
9712  C CG  . ASN B 52  ? 2.7781 1.7841 1.9373 -0.3329 -0.5758 -0.2284 56  ASN B CG  
9713  O OD1 . ASN B 52  ? 2.7191 1.7745 1.9001 -0.3531 -0.6204 -0.1909 56  ASN B OD1 
9714  N ND2 . ASN B 52  ? 2.8984 1.8184 1.9390 -0.3531 -0.5521 -0.2777 56  ASN B ND2 
9721  N N   . PHE B 53  ? 2.4573 1.6311 1.9994 -0.2276 -0.5471 -0.1383 57  PHE B N   
9722  C CA  . PHE B 53  ? 2.4072 1.5945 2.0296 -0.1984 -0.5234 -0.1277 57  PHE B CA  
9723  C C   . PHE B 53  ? 2.2757 1.5510 1.9911 -0.1638 -0.5069 -0.0926 57  PHE B C   
9724  O O   . PHE B 53  ? 2.2081 1.4966 1.9676 -0.1301 -0.4729 -0.0897 57  PHE B O   
9725  C CB  . PHE B 53  ? 2.4500 1.6102 2.1056 -0.2332 -0.5603 -0.1140 57  PHE B CB  
9726  C CG  . PHE B 53  ? 2.5744 1.6408 2.1370 -0.2725 -0.5783 -0.1492 57  PHE B CG  
9727  C CD1 . PHE B 53  ? 2.6443 1.6462 2.1133 -0.2640 -0.5438 -0.1962 57  PHE B CD1 
9728  C CD2 . PHE B 53  ? 2.6200 1.6612 2.1903 -0.3200 -0.6279 -0.1361 57  PHE B CD2 
9729  C CE1 . PHE B 53  ? 2.7705 1.6789 2.1475 -0.3029 -0.5550 -0.2328 57  PHE B CE1 
9730  C CE2 . PHE B 53  ? 2.7371 1.6861 2.2137 -0.3609 -0.6451 -0.1704 57  PHE B CE2 
9731  C CZ  . PHE B 53  ? 2.8145 1.6941 2.1903 -0.3527 -0.6069 -0.2205 57  PHE B CZ  
9741  N N   . ILE B 54  ? 2.2250 1.5577 1.9710 -0.1733 -0.5306 -0.0651 58  ILE B N   
9742  C CA  . ILE B 54  ? 2.1453 1.5557 1.9780 -0.1436 -0.5117 -0.0347 58  ILE B CA  
9743  C C   . ILE B 54  ? 2.0591 1.4822 1.8689 -0.1011 -0.4632 -0.0522 58  ILE B C   
9744  O O   . ILE B 54  ? 2.0713 1.4645 1.8045 -0.0968 -0.4504 -0.0809 58  ILE B O   
9745  C CB  . ILE B 54  ? 2.1720 1.6355 2.0421 -0.1607 -0.5441 -0.0044 58  ILE B CB  
9746  C CG1 . ILE B 54  ? 2.2080 1.6715 2.1301 -0.2000 -0.5925 0.0215  58  ILE B CG1 
9747  C CG2 . ILE B 54  ? 2.0994 1.6359 2.0463 -0.1275 -0.5148 0.0189  58  ILE B CG2 
9748  C CD1 . ILE B 54  ? 2.1945 1.7014 2.1548 -0.2228 -0.6342 0.0534  58  ILE B CD1 
9760  N N   . GLU B 55  ? 1.9455 1.4130 1.8220 -0.0723 -0.4357 -0.0341 59  GLU B N   
9761  C CA  . GLU B 55  ? 1.8933 1.3758 1.7599 -0.0340 -0.3936 -0.0447 59  GLU B CA  
9762  C C   . GLU B 55  ? 1.7417 1.2953 1.6687 -0.0172 -0.3793 -0.0177 59  GLU B C   
9763  O O   . GLU B 55  ? 1.6824 1.2641 1.6766 -0.0228 -0.3824 0.0079  59  GLU B O   
9764  C CB  . GLU B 55  ? 1.9322 1.3798 1.8072 -0.0177 -0.3723 -0.0528 59  GLU B CB  
9765  C CG  . GLU B 55  ? 1.9909 1.3687 1.7985 -0.0169 -0.3639 -0.0897 59  GLU B CG  
9766  C CD  . GLU B 55  ? 1.9387 1.3228 1.7208 0.0169  -0.3276 -0.1077 59  GLU B CD  
9767  O OE1 . GLU B 55  ? 1.9285 1.2863 1.7196 0.0390  -0.3046 -0.1168 59  GLU B OE1 
9768  O OE2 . GLU B 55  ? 1.8970 1.3139 1.6563 0.0211  -0.3232 -0.1102 59  GLU B OE2 
9775  N N   . ASN B 56  ? 1.6487 1.2286 1.5514 0.0019  -0.3607 -0.0247 60  ASN B N   
9776  C CA  . ASN B 56  ? 1.5106 1.1519 1.4624 0.0160  -0.3454 -0.0030 60  ASN B CA  
9777  C C   . ASN B 56  ? 1.4725 1.1321 1.3854 0.0364  -0.3244 -0.0159 60  ASN B C   
9778  O O   . ASN B 56  ? 1.4812 1.1479 1.3675 0.0264  -0.3385 -0.0185 60  ASN B O   
9779  C CB  . ASN B 56  ? 1.4758 1.1475 1.4773 -0.0068 -0.3733 0.0213  60  ASN B CB  
9780  C CG  . ASN B 56  ? 1.3987 1.1265 1.4407 0.0066  -0.3566 0.0375  60  ASN B CG  
9781  O OD1 . ASN B 56  ? 1.3776 1.1267 1.4273 0.0292  -0.3228 0.0370  60  ASN B OD1 
9782  N ND2 . ASN B 56  ? 1.3685 1.1181 1.4367 -0.0094 -0.3820 0.0533  60  ASN B ND2 
9789  N N   . PRO B 57  ? 1.4331 1.1011 1.3430 0.0627  -0.2935 -0.0214 61  PRO B N   
9790  C CA  . PRO B 57  ? 1.4061 1.0981 1.2891 0.0809  -0.2737 -0.0304 61  PRO B CA  
9791  C C   . PRO B 57  ? 1.3514 1.0956 1.2714 0.0815  -0.2697 -0.0104 61  PRO B C   
9792  O O   . PRO B 57  ? 1.3270 1.0932 1.3011 0.0758  -0.2695 0.0101  61  PRO B O   
9793  C CB  . PRO B 57  ? 1.3653 1.0533 1.2496 0.1056  -0.2475 -0.0352 61  PRO B CB  
9794  C CG  . PRO B 57  ? 1.3507 1.0331 1.2772 0.1006  -0.2505 -0.0175 61  PRO B CG  
9795  C CD  . PRO B 57  ? 1.4035 1.0585 1.3349 0.0748  -0.2783 -0.0171 61  PRO B CD  
9803  N N   . VAL B 58  ? 1.3155 1.0773 1.2073 0.0879  -0.2631 -0.0174 62  VAL B N   
9804  C CA  . VAL B 58  ? 1.2566 1.0627 1.1802 0.0892  -0.2575 -0.0012 62  VAL B CA  
9805  C C   . VAL B 58  ? 1.2026 1.0281 1.0995 0.1085  -0.2324 -0.0107 62  VAL B C   
9806  O O   . VAL B 58  ? 1.1995 1.0065 1.0491 0.1160  -0.2263 -0.0300 62  VAL B O   
9807  C CB  . VAL B 58  ? 1.2795 1.0888 1.2054 0.0686  -0.2869 0.0078  62  VAL B CB  
9808  C CG1 . VAL B 58  ? 1.2599 1.0438 1.1117 0.0629  -0.2958 -0.0117 62  VAL B CG1 
9809  C CG2 . VAL B 58  ? 1.2604 1.1137 1.2366 0.0716  -0.2792 0.0273  62  VAL B CG2 
9819  N N   . SER B 59  ? 1.1684 1.0304 1.0979 0.1150  -0.2156 0.0023  63  SER B N   
9820  C CA  . SER B 59  ? 1.1448 1.0285 1.0534 0.1294  -0.1946 -0.0039 63  SER B CA  
9821  C C   . SER B 59  ? 1.1551 1.0372 1.0255 0.1258  -0.2030 -0.0134 63  SER B C   
9822  O O   . SER B 59  ? 1.1409 1.0207 1.0159 0.1103  -0.2244 -0.0058 63  SER B O   
9823  C CB  . SER B 59  ? 1.1502 1.0667 1.0966 0.1303  -0.1768 0.0105  63  SER B CB  
9824  O OG  . SER B 59  ? 1.1794 1.0938 1.1599 0.1260  -0.1700 0.0213  63  SER B OG  
9830  N N   . GLN B 60  ? 1.2056 1.0897 1.0405 0.1386  -0.1869 -0.0278 64  GLN B N   
9831  C CA  . GLN B 60  ? 1.2267 1.1060 1.0174 0.1340  -0.1896 -0.0389 64  GLN B CA  
9832  C C   . GLN B 60  ? 1.1894 1.0931 0.9693 0.1495  -0.1647 -0.0452 64  GLN B C   
9833  O O   . GLN B 60  ? 1.1568 1.0699 0.9520 0.1644  -0.1491 -0.0463 64  GLN B O   
9834  C CB  . GLN B 60  ? 1.3100 1.1456 1.0531 0.1266  -0.1981 -0.0587 64  GLN B CB  
9835  C CG  . GLN B 60  ? 1.3725 1.1906 1.1128 0.1443  -0.1790 -0.0743 64  GLN B CG  
9836  C CD  . GLN B 60  ? 1.4555 1.2220 1.1530 0.1354  -0.1840 -0.0964 64  GLN B CD  
9837  O OE1 . GLN B 60  ? 1.4915 1.2362 1.1364 0.1189  -0.1903 -0.1090 64  GLN B OE1 
9838  N NE2 . GLN B 60  ? 1.4579 1.2002 1.1734 0.1438  -0.1808 -0.1013 64  GLN B NE2 
9847  N N   . VAL B 61  ? 1.1750 1.0890 0.9298 0.1437  -0.1640 -0.0467 65  VAL B N   
9848  C CA  . VAL B 61  ? 1.1196 1.0579 0.8641 0.1547  -0.1420 -0.0519 65  VAL B CA  
9849  C C   . VAL B 61  ? 1.1843 1.1021 0.8774 0.1532  -0.1334 -0.0722 65  VAL B C   
9850  O O   . VAL B 61  ? 1.2381 1.1285 0.8915 0.1357  -0.1484 -0.0774 65  VAL B O   
9851  C CB  . VAL B 61  ? 1.0653 1.0312 0.8234 0.1481  -0.1427 -0.0373 65  VAL B CB  
9852  C CG1 . VAL B 61  ? 1.0579 1.0501 0.8093 0.1579  -0.1206 -0.0417 65  VAL B CG1 
9853  C CG2 . VAL B 61  ? 1.0151 0.9937 0.8232 0.1462  -0.1467 -0.0204 65  VAL B CG2 
9863  N N   . GLU B 62  ? 1.2089 1.1392 0.9029 0.1694  -0.1089 -0.0830 66  GLU B N   
9864  C CA  . GLU B 62  ? 1.2656 1.1832 0.9175 0.1691  -0.0904 -0.1030 66  GLU B CA  
9865  C C   . GLU B 62  ? 1.2250 1.1812 0.8848 0.1745  -0.0731 -0.0982 66  GLU B C   
9866  O O   . GLU B 62  ? 1.1816 1.1691 0.8834 0.1888  -0.0648 -0.0893 66  GLU B O   
9867  C CB  . GLU B 62  ? 1.3361 1.2310 0.9921 0.1846  -0.0714 -0.1225 66  GLU B CB  
9868  C CG  . GLU B 62  ? 1.4524 1.3284 1.0643 0.1828  -0.0446 -0.1475 66  GLU B CG  
9869  C CD  . GLU B 62  ? 1.5391 1.3985 1.1735 0.2033  -0.0176 -0.1664 66  GLU B CD  
9870  O OE1 . GLU B 62  ? 1.5465 1.4046 1.2264 0.2175  -0.0254 -0.1584 66  GLU B OE1 
9871  O OE2 . GLU B 62  ? 1.5910 1.4377 1.2003 0.2049  0.0133  -0.1886 66  GLU B OE2 
9878  N N   . ILE B 63  ? 1.2336 1.1858 0.8500 0.1600  -0.0699 -0.1025 67  ILE B N   
9879  C CA  . ILE B 63  ? 1.1434 1.1289 0.7626 0.1618  -0.0531 -0.0986 67  ILE B CA  
9880  C C   . ILE B 63  ? 1.1599 1.1434 0.7678 0.1719  -0.0203 -0.1198 67  ILE B C   
9881  O O   . ILE B 63  ? 1.2549 1.2036 0.8112 0.1616  -0.0095 -0.1391 67  ILE B O   
9882  C CB  . ILE B 63  ? 1.1290 1.1112 0.7111 0.1395  -0.0669 -0.0885 67  ILE B CB  
9883  C CG1 . ILE B 63  ? 1.1002 1.0868 0.7121 0.1327  -0.0959 -0.0663 67  ILE B CG1 
9884  C CG2 . ILE B 63  ? 1.1066 1.1201 0.6895 0.1398  -0.0478 -0.0852 67  ILE B CG2 
9885  C CD1 . ILE B 63  ? 1.1286 1.1115 0.7190 0.1120  -0.1148 -0.0504 67  ILE B CD1 
9897  N N   . LEU B 64  ? 1.1297 1.1493 0.7866 0.1901  -0.0037 -0.1159 68  LEU B N   
9898  C CA  . LEU B 64  ? 1.1719 1.1984 0.8408 0.2032  0.0299  -0.1323 68  LEU B CA  
9899  C C   . LEU B 64  ? 1.1953 1.2531 0.8588 0.1971  0.0485  -0.1300 68  LEU B C   
9900  O O   . LEU B 64  ? 1.2512 1.3001 0.8919 0.1955  0.0789  -0.1484 68  LEU B O   
9901  C CB  . LEU B 64  ? 1.1464 1.1945 0.8851 0.2272  0.0333  -0.1255 68  LEU B CB  
9902  C CG  . LEU B 64  ? 1.1594 1.1784 0.9113 0.2345  0.0164  -0.1250 68  LEU B CG  
9903  C CD1 . LEU B 64  ? 1.1378 1.1796 0.9591 0.2566  0.0191  -0.1139 68  LEU B CD1 
9904  C CD2 . LEU B 64  ? 1.2211 1.1867 0.9286 0.2299  0.0272  -0.1510 68  LEU B CD2 
9916  N N   . LYS B 65  ? 1.1764 1.2681 0.8595 0.1921  0.0338  -0.1092 69  LYS B N   
9917  C CA  . LYS B 65  ? 1.1964 1.3169 0.8750 0.1836  0.0480  -0.1045 69  LYS B CA  
9918  C C   . LYS B 65  ? 1.1107 1.2327 0.7684 0.1657  0.0241  -0.0874 69  LYS B C   
9919  O O   . LYS B 65  ? 1.0833 1.2170 0.7703 0.1679  0.0051  -0.0729 69  LYS B O   
9920  C CB  . LYS B 65  ? 1.2278 1.3950 0.9711 0.1982  0.0593  -0.0957 69  LYS B CB  
9921  C CG  . LYS B 65  ? 1.2925 1.4642 1.0724 0.2174  0.0878  -0.1101 69  LYS B CG  
9922  C CD  . LYS B 65  ? 1.3112 1.5354 1.1607 0.2279  0.0962  -0.0964 69  LYS B CD  
9923  C CE  . LYS B 65  ? 1.3701 1.6069 1.2820 0.2463  0.0807  -0.0837 69  LYS B CE  
9924  N NZ  . LYS B 65  ? 1.4491 1.7385 1.4317 0.2531  0.0820  -0.0656 69  LYS B NZ  
9938  N N   . ASN B 66  ? 1.0742 1.1816 0.6814 0.1469  0.0265  -0.0886 70  ASN B N   
9939  C CA  . ASN B 66  ? 1.0201 1.1257 0.6131 0.1301  0.0040  -0.0703 70  ASN B CA  
9940  C C   . ASN B 66  ? 1.0294 1.1415 0.5888 0.1135  0.0177  -0.0676 70  ASN B C   
9941  O O   . ASN B 66  ? 1.0247 1.1115 0.5348 0.0933  0.0058  -0.0618 70  ASN B O   
9942  C CB  . ASN B 66  ? 1.0196 1.0874 0.5830 0.1193  -0.0234 -0.0664 70  ASN B CB  
9943  C CG  . ASN B 66  ? 1.0192 1.0881 0.5916 0.1066  -0.0481 -0.0436 70  ASN B CG  
9944  O OD1 . ASN B 66  ? 0.9918 1.0863 0.6012 0.1105  -0.0455 -0.0331 70  ASN B OD1 
9945  N ND2 . ASN B 66  ? 1.0495 1.0883 0.5901 0.0901  -0.0727 -0.0353 70  ASN B ND2 
9952  N N   . LYS B 67  ? 1.0266 1.1736 0.6145 0.1199  0.0411  -0.0694 71  LYS B N   
9953  C CA  . LYS B 67  ? 1.0535 1.2106 0.6164 0.1034  0.0558  -0.0650 71  LYS B CA  
9954  C C   . LYS B 67  ? 1.0027 1.1593 0.5646 0.0890  0.0316  -0.0430 71  LYS B C   
9955  O O   . LYS B 67  ? 0.9667 1.1367 0.5712 0.0965  0.0175  -0.0333 71  LYS B O   
9956  C CB  . LYS B 67  ? 1.0567 1.2570 0.6654 0.1136  0.0832  -0.0685 71  LYS B CB  
9957  C CG  . LYS B 67  ? 1.1620 1.3749 0.7480 0.0964  0.1048  -0.0660 71  LYS B CG  
9958  C CD  . LYS B 67  ? 1.2321 1.4922 0.8765 0.1070  0.1310  -0.0679 71  LYS B CD  
9959  C CE  . LYS B 67  ? 1.3580 1.6316 0.9825 0.0886  0.1562  -0.0658 71  LYS B CE  
9960  N NZ  . LYS B 67  ? 1.3834 1.7092 1.0768 0.0966  0.1773  -0.0629 71  LYS B NZ  
9974  N N   . PRO B 68  ? 1.0048 1.1432 0.5190 0.0671  0.0274  -0.0341 72  PRO B N   
9975  C CA  . PRO B 68  ? 0.9886 1.1228 0.5112 0.0551  0.0037  -0.0110 72  PRO B CA  
9976  C C   . PRO B 68  ? 0.9426 1.1108 0.5112 0.0585  0.0137  -0.0046 72  PRO B C   
9977  O O   . PRO B 68  ? 0.9142 1.1109 0.4961 0.0621  0.0378  -0.0130 72  PRO B O   
9978  C CB  . PRO B 68  ? 1.0377 1.1470 0.4963 0.0289  0.0000  -0.0017 72  PRO B CB  
9979  C CG  . PRO B 68  ? 1.1020 1.1922 0.5072 0.0254  0.0182  -0.0231 72  PRO B CG  
9980  C CD  . PRO B 68  ? 1.0421 1.1611 0.4922 0.0503  0.0464  -0.0439 72  PRO B CD  
9988  N N   . LEU B 69  ? 0.9297 1.0934 0.5259 0.0560  -0.0045 0.0104  73  LEU B N   
9989  C CA  . LEU B 69  ? 0.8857 1.0724 0.5164 0.0538  0.0036  0.0155  73  LEU B CA  
9990  C C   . LEU B 69  ? 0.9168 1.1119 0.5252 0.0363  0.0165  0.0226  73  LEU B C   
9991  O O   . LEU B 69  ? 0.9497 1.1224 0.5194 0.0211  0.0091  0.0336  73  LEU B O   
9992  C CB  . LEU B 69  ? 0.8318 1.0021 0.4918 0.0524  -0.0130 0.0276  73  LEU B CB  
9993  C CG  . LEU B 69  ? 0.8022 0.9681 0.4918 0.0673  -0.0200 0.0209  73  LEU B CG  
9994  C CD1 . LEU B 69  ? 0.8292 0.9715 0.5457 0.0644  -0.0334 0.0337  73  LEU B CD1 
9995  C CD2 . LEU B 69  ? 0.7747 0.9660 0.4873 0.0730  -0.0070 0.0108  73  LEU B CD2 
10007 N N   . SER B 70  ? 0.9339 1.1613 0.5665 0.0358  0.0338  0.0187  74  SER B N   
10008 C CA  . SER B 70  ? 0.9623 1.2025 0.5798 0.0186  0.0495  0.0250  74  SER B CA  
10009 C C   . SER B 70  ? 0.9906 1.2128 0.6093 0.0023  0.0368  0.0433  74  SER B C   
10010 O O   . SER B 70  ? 1.0148 1.2329 0.6661 0.0049  0.0278  0.0457  74  SER B O   
10011 C CB  . SER B 70  ? 0.9289 1.2128 0.5828 0.0221  0.0690  0.0178  74  SER B CB  
10012 O OG  . SER B 70  ? 0.8954 1.1891 0.5809 0.0157  0.0609  0.0244  74  SER B OG  
10018 N N   . VAL B 71  ? 1.0475 1.2555 0.6291 -0.0163 0.0381  0.0560  75  VAL B N   
10019 C CA  . VAL B 71  ? 1.0531 1.2390 0.6360 -0.0327 0.0246  0.0773  75  VAL B CA  
10020 C C   . VAL B 71  ? 1.0224 1.2287 0.6055 -0.0499 0.0433  0.0822  75  VAL B C   
10021 O O   . VAL B 71  ? 1.0110 1.2335 0.5660 -0.0581 0.0633  0.0779  75  VAL B O   
10022 C CB  . VAL B 71  ? 1.1085 1.2581 0.6485 -0.0448 0.0036  0.0954  75  VAL B CB  
10023 C CG1 . VAL B 71  ? 1.2042 1.3540 0.6810 -0.0596 0.0191  0.0919  75  VAL B CG1 
10024 C CG2 . VAL B 71  ? 1.1475 1.2737 0.7018 -0.0597 -0.0131 0.1219  75  VAL B CG2 
10034 N N   . GLY B 72  ? 0.9492 1.1527 0.5650 -0.0567 0.0398  0.0897  76  GLY B N   
10035 C CA  . GLY B 72  ? 0.9658 1.1844 0.5847 -0.0762 0.0538  0.0968  76  GLY B CA  
10036 C C   . GLY B 72  ? 0.9819 1.2456 0.6289 -0.0730 0.0723  0.0813  76  GLY B C   
10037 O O   . GLY B 72  ? 0.9702 1.2546 0.6327 -0.0550 0.0749  0.0661  76  GLY B O   
10041 N N   . ARG B 73  ? 0.9978 1.2771 0.6557 -0.0924 0.0827  0.0883  77  ARG B N   
10042 C CA  . ARG B 73  ? 0.9961 1.3220 0.6880 -0.0941 0.0963  0.0794  77  ARG B CA  
10043 C C   . ARG B 73  ? 0.9759 1.3355 0.6648 -0.0855 0.1177  0.0717  77  ARG B C   
10044 O O   . ARG B 73  ? 1.0141 1.3675 0.6682 -0.0955 0.1331  0.0772  77  ARG B O   
10045 C CB  . ARG B 73  ? 1.1269 1.4601 0.8311 -0.1205 0.1017  0.0905  77  ARG B CB  
10046 C CG  . ARG B 73  ? 1.1484 1.5325 0.8943 -0.1263 0.1104  0.0854  77  ARG B CG  
10047 C CD  . ARG B 73  ? 1.1677 1.5557 0.9272 -0.1552 0.1114  0.0957  77  ARG B CD  
10048 N NE  . ARG B 73  ? 1.1954 1.6353 1.0001 -0.1624 0.1140  0.0934  77  ARG B NE  
10049 C CZ  . ARG B 73  ? 1.2606 1.7501 1.0938 -0.1607 0.1330  0.0959  77  ARG B CZ  
10050 N NH1 . ARG B 73  ? 1.2995 1.7883 1.1091 -0.1540 0.1557  0.0966  77  ARG B NH1 
10051 N NH2 . ARG B 73  ? 1.3147 1.8535 1.2011 -0.1675 0.1300  0.0980  77  ARG B NH2 
10065 N N   . GLN B 74  ? 0.9050 1.2975 0.6300 -0.0683 0.1203  0.0595  78  GLN B N   
10066 C CA  . GLN B 74  ? 0.9629 1.3866 0.6998 -0.0555 0.1437  0.0498  78  GLN B CA  
10067 C C   . GLN B 74  ? 1.0520 1.5295 0.8430 -0.0646 0.1600  0.0539  78  GLN B C   
10068 O O   . GLN B 74  ? 1.0222 1.5250 0.8580 -0.0649 0.1445  0.0566  78  GLN B O   
10069 C CB  . GLN B 74  ? 0.8747 1.2990 0.6264 -0.0285 0.1347  0.0368  78  GLN B CB  
10070 C CG  . GLN B 74  ? 0.8826 1.2580 0.5907 -0.0199 0.1165  0.0338  78  GLN B CG  
10071 C CD  . GLN B 74  ? 0.9499 1.2962 0.6007 -0.0270 0.1275  0.0343  78  GLN B CD  
10072 O OE1 . GLN B 74  ? 0.9859 1.3431 0.6252 -0.0234 0.1530  0.0240  78  GLN B OE1 
10073 N NE2 . GLN B 74  ? 0.9690 1.2757 0.5836 -0.0392 0.1088  0.0468  78  GLN B NE2 
10082 N N   . LYS B 75  ? 1.1389 1.6333 0.9249 -0.0746 0.1910  0.0554  79  LYS B N   
10083 C CA  . LYS B 75  ? 1.1732 1.7243 1.0224 -0.0820 0.2102  0.0603  79  LYS B CA  
10084 C C   . LYS B 75  ? 1.1866 1.7789 1.1003 -0.0568 0.2166  0.0518  79  LYS B C   
10085 O O   . LYS B 75  ? 1.2329 1.8776 1.2182 -0.0604 0.2209  0.0601  79  LYS B O   
10086 C CB  . LYS B 75  ? 1.2132 1.7708 1.0415 -0.0988 0.2484  0.0627  79  LYS B CB  
10087 C CG  . LYS B 75  ? 1.2307 1.7568 1.0095 -0.1286 0.2417  0.0779  79  LYS B CG  
10088 C CD  . LYS B 75  ? 1.2735 1.8048 1.0250 -0.1478 0.2818  0.0810  79  LYS B CD  
10089 C CE  . LYS B 75  ? 1.3045 1.8021 1.0067 -0.1789 0.2725  0.1003  79  LYS B CE  
10090 N NZ  . LYS B 75  ? 1.3761 1.8753 1.0422 -0.2019 0.3121  0.1050  79  LYS B NZ  
10104 N N   . ASN B 76  ? 1.1690 1.7387 1.0638 -0.0325 0.2154  0.0379  80  ASN B N   
10105 C CA  . ASN B 76  ? 1.1776 1.7793 1.1336 -0.0066 0.2221  0.0305  80  ASN B CA  
10106 C C   . ASN B 76  ? 1.1514 1.7342 1.1056 0.0082  0.1846  0.0295  80  ASN B C   
10107 O O   . ASN B 76  ? 1.1493 1.6837 1.0435 0.0124  0.1720  0.0222  80  ASN B O   
10108 C CB  . ASN B 76  ? 1.2443 1.8331 1.1806 0.0084  0.2617  0.0119  80  ASN B CB  
10109 C CG  . ASN B 76  ? 1.2920 1.9050 1.2935 0.0382  0.2692  0.0032  80  ASN B CG  
10110 O OD1 . ASN B 76  ? 1.3233 1.9024 1.2951 0.0562  0.2650  -0.0105 80  ASN B OD1 
10111 N ND2 . ASN B 76  ? 1.3024 1.9745 1.3988 0.0430  0.2784  0.0136  80  ASN B ND2 
10118 N N   . SER B 77  ? 1.0432 1.6041 0.8296 -0.0144 0.1748  -0.0252 81  SER B N   
10119 C CA  . SER B 77  ? 1.0707 1.5825 0.8794 0.0052  0.1634  -0.0298 81  SER B CA  
10120 C C   . SER B 77  ? 1.0798 1.5831 0.8875 0.0247  0.1576  -0.0526 81  SER B C   
10121 O O   . SER B 77  ? 1.0543 1.5137 0.8699 0.0358  0.1454  -0.0504 81  SER B O   
10122 C CB  . SER B 77  ? 1.0808 1.5955 0.9221 0.0152  0.1685  -0.0405 81  SER B CB  
10123 O OG  . SER B 77  ? 1.0768 1.5902 0.9209 -0.0026 0.1712  -0.0180 81  SER B OG  
10129 N N   . SER B 78  ? 1.1151 1.6604 0.9129 0.0285  0.1660  -0.0752 82  SER B N   
10130 C CA  . SER B 78  ? 1.1308 1.6691 0.9298 0.0480  0.1605  -0.1007 82  SER B CA  
10131 C C   . SER B 78  ? 1.1062 1.6234 0.8790 0.0429  0.1496  -0.0904 82  SER B C   
10132 O O   . SER B 78  ? 1.1146 1.6128 0.8898 0.0580  0.1411  -0.1067 82  SER B O   
10133 C CB  . SER B 78  ? 1.1919 1.7836 0.9900 0.0551  0.1731  -0.1311 82  SER B CB  
10134 O OG  . SER B 78  ? 1.2264 1.8496 1.0441 0.0538  0.1851  -0.1358 82  SER B OG  
10140 N N   . ASP B 79  ? 1.1061 1.6254 0.8542 0.0216  0.1484  -0.0635 83  ASP B N   
10141 C CA  . ASP B 79  ? 1.1287 1.6296 0.8515 0.0157  0.1368  -0.0513 83  ASP B CA  
10142 C C   . ASP B 79  ? 1.1240 1.5723 0.8536 0.0147  0.1224  -0.0263 83  ASP B C   
10143 O O   . ASP B 79  ? 1.1509 1.5821 0.8614 0.0088  0.1113  -0.0120 83  ASP B O   
10144 C CB  . ASP B 79  ? 1.1479 1.6852 0.8364 -0.0070 0.1428  -0.0375 83  ASP B CB  
10145 C CG  . ASP B 79  ? 1.2551 1.8483 0.9337 -0.0055 0.1570  -0.0648 83  ASP B CG  
10146 O OD1 . ASP B 79  ? 1.2723 1.8685 0.9617 0.0146  0.1568  -0.0950 83  ASP B OD1 
10147 O OD2 . ASP B 79  ? 1.2990 1.9336 0.9590 -0.0246 0.1681  -0.0565 83  ASP B OD2 
10152 N N   . ILE B 80  ? 1.0509 1.4750 0.8072 0.0206  0.1219  -0.0214 84  ILE B N   
10153 C CA  . ILE B 80  ? 0.9568 1.3322 0.7233 0.0232  0.1088  -0.0028 84  ILE B CA  
10154 C C   . ILE B 80  ? 0.8891 1.2402 0.6669 0.0417  0.0993  -0.0192 84  ILE B C   
10155 O O   . ILE B 80  ? 0.8824 1.2390 0.6771 0.0565  0.1029  -0.0434 84  ILE B O   
10156 C CB  . ILE B 80  ? 0.8903 1.2504 0.6807 0.0231  0.1120  0.0058  84  ILE B CB  
10157 C CG1 . ILE B 80  ? 0.8677 1.2448 0.6449 0.0014  0.1182  0.0273  84  ILE B CG1 
10158 C CG2 . ILE B 80  ? 0.8276 1.1389 0.6328 0.0308  0.0993  0.0174  84  ILE B CG2 
10159 C CD1 . ILE B 80  ? 0.8002 1.1677 0.5994 -0.0006 0.1223  0.0340  84  ILE B CD1 
10171 N N   . VAL B 81  ? 0.8514 1.1755 0.6204 0.0405  0.0861  -0.0056 85  VAL B N   
10172 C CA  . VAL B 81  ? 0.8174 1.1170 0.5968 0.0551  0.0757  -0.0173 85  VAL B CA  
10173 C C   . VAL B 81  ? 0.7804 1.0421 0.5683 0.0543  0.0641  0.0046  85  VAL B C   
10174 O O   . VAL B 81  ? 0.7948 1.0503 0.5655 0.0446  0.0562  0.0239  85  VAL B O   
10175 C CB  . VAL B 81  ? 0.7949 1.1092 0.5522 0.0552  0.0709  -0.0283 85  VAL B CB  
10176 C CG1 . VAL B 81  ? 0.8119 1.1003 0.5818 0.0689  0.0596  -0.0404 85  VAL B CG1 
10177 C CG2 . VAL B 81  ? 0.7369 1.0924 0.4842 0.0556  0.0833  -0.0509 85  VAL B CG2 
10187 N N   . GLN B 82  ? 0.7087 0.9462 0.5229 0.0647  0.0625  0.0013  86  GLN B N   
10188 C CA  . GLN B 82  ? 0.7050 0.9093 0.5303 0.0655  0.0531  0.0192  86  GLN B CA  
10189 C C   . GLN B 82  ? 0.7196 0.9030 0.5570 0.0770  0.0428  0.0113  86  GLN B C   
10190 O O   . GLN B 82  ? 0.7449 0.9050 0.5906 0.0781  0.0342  0.0249  86  GLN B O   
10191 C CB  . GLN B 82  ? 0.7092 0.9020 0.5542 0.0662  0.0590  0.0244  86  GLN B CB  
10192 C CG  . GLN B 82  ? 0.7552 0.9679 0.5905 0.0530  0.0686  0.0338  86  GLN B CG  
10193 C CD  . GLN B 82  ? 0.7664 0.9634 0.6196 0.0518  0.0717  0.0424  86  GLN B CD  
10194 O OE1 . GLN B 82  ? 0.7541 0.9341 0.6035 0.0433  0.0670  0.0628  86  GLN B OE1 
10195 N NE2 . GLN B 82  ? 0.7834 0.9849 0.6556 0.0605  0.0785  0.0267  86  GLN B NE2 
10204 N N   . ILE B 83  ? 0.6794 0.8709 0.5186 0.0851  0.0431  -0.0104 87  ILE B N   
10205 C CA  . ILE B 83  ? 0.6682 0.8419 0.5171 0.0935  0.0328  -0.0180 87  ILE B CA  
10206 C C   . ILE B 83  ? 0.7291 0.9191 0.5617 0.0948  0.0299  -0.0347 87  ILE B C   
10207 O O   . ILE B 83  ? 0.7767 0.9891 0.6009 0.0955  0.0382  -0.0500 87  ILE B O   
10208 C CB  . ILE B 83  ? 0.6014 0.7583 0.4759 0.1036  0.0341  -0.0288 87  ILE B CB  
10209 C CG1 . ILE B 83  ? 0.5803 0.7167 0.4655 0.1087  0.0227  -0.0303 87  ILE B CG1 
10210 C CG2 . ILE B 83  ? 0.5828 0.7545 0.4596 0.1101  0.0411  -0.0516 87  ILE B CG2 
10211 C CD1 . ILE B 83  ? 0.5791 0.6970 0.4880 0.1160  0.0228  -0.0361 87  ILE B CD1 
10223 N N   . ALA B 84  ? 0.7244 0.9046 0.5530 0.0952  0.0180  -0.0327 88  ALA B N   
10224 C CA  . ALA B 84  ? 0.7164 0.9091 0.5292 0.0959  0.0131  -0.0485 88  ALA B CA  
10225 C C   . ALA B 84  ? 0.7422 0.9152 0.5653 0.1000  -0.0002 -0.0504 88  ALA B C   
10226 O O   . ALA B 84  ? 0.7943 0.9542 0.6244 0.0977  -0.0074 -0.0327 88  ALA B O   
10227 C CB  . ALA B 84  ? 0.6881 0.9020 0.4717 0.0851  0.0123  -0.0390 88  ALA B CB  
10233 N N   . PRO B 85  ? 0.7535 0.9242 0.5786 0.1058  -0.0043 -0.0718 89  PRO B N   
10234 C CA  . PRO B 85  ? 0.7962 0.9808 0.6148 0.1111  0.0020  -0.0962 89  PRO B CA  
10235 C C   . PRO B 85  ? 0.7798 0.9605 0.6168 0.1181  0.0120  -0.1029 89  PRO B C   
10236 O O   . PRO B 85  ? 0.7413 0.9088 0.5941 0.1176  0.0143  -0.0880 89  PRO B O   
10237 C CB  . PRO B 85  ? 0.8088 0.9806 0.6298 0.1155  -0.0098 -0.1132 89  PRO B CB  
10238 C CG  . PRO B 85  ? 0.8000 0.9585 0.6251 0.1103  -0.0216 -0.0964 89  PRO B CG  
10239 C CD  . PRO B 85  ? 0.7670 0.9192 0.6038 0.1079  -0.0170 -0.0734 89  PRO B CD  
10247 N N   . GLN B 86  ? 0.7941 0.9869 0.6295 0.1252  0.0171  -0.1261 90  GLN B N   
10248 C CA  . GLN B 86  ? 0.7970 0.9883 0.6503 0.1331  0.0254  -0.1345 90  GLN B CA  
10249 C C   . GLN B 86  ? 0.8020 0.9765 0.6688 0.1449  0.0188  -0.1572 90  GLN B C   
10250 O O   . GLN B 86  ? 0.8167 0.9838 0.7014 0.1523  0.0224  -0.1626 90  GLN B O   
10251 C CB  . GLN B 86  ? 0.8252 1.0507 0.6677 0.1319  0.0391  -0.1410 90  GLN B CB  
10252 C CG  . GLN B 86  ? 0.8439 1.0850 0.6725 0.1185  0.0455  -0.1171 90  GLN B CG  
10253 C CD  . GLN B 86  ? 0.9105 1.1710 0.7102 0.1095  0.0432  -0.1148 90  GLN B CD  
10254 O OE1 . GLN B 86  ? 0.9154 1.1881 0.7033 0.1135  0.0411  -0.1355 90  GLN B OE1 
10255 N NE2 . GLN B 86  ? 0.9259 1.1884 0.7134 0.0972  0.0426  -0.0898 90  GLN B NE2 
10264 N N   . SER B 87  ? 0.8454 1.0122 0.7039 0.1463  0.0081  -0.1700 91  SER B N   
10265 C CA  . SER B 87  ? 0.8817 1.0268 0.7522 0.1561  -0.0009 -0.1902 91  SER B CA  
10266 C C   . SER B 87  ? 0.9053 1.0356 0.7678 0.1518  -0.0152 -0.1928 91  SER B C   
10267 O O   . SER B 87  ? 0.8817 1.0290 0.7232 0.1472  -0.0167 -0.1970 91  SER B O   
10268 C CB  . SER B 87  ? 0.8864 1.0489 0.7539 0.1673  0.0043  -0.2178 91  SER B CB  
10269 O OG  . SER B 87  ? 0.9002 1.0370 0.7819 0.1780  -0.0058 -0.2361 91  SER B OG  
10275 N N   . LEU B 88  ? 0.9173 1.0172 0.7957 0.1521  -0.0259 -0.1900 92  LEU B N   
10276 C CA  . LEU B 88  ? 0.9364 1.0214 0.8106 0.1465  -0.0403 -0.1912 92  LEU B CA  
10277 C C   . LEU B 88  ? 0.9843 1.0395 0.8716 0.1520  -0.0517 -0.2064 92  LEU B C   
10278 O O   . LEU B 88  ? 0.9639 1.0055 0.8675 0.1584  -0.0495 -0.2080 92  LEU B O   
10279 C CB  . LEU B 88  ? 0.8888 0.9680 0.7692 0.1362  -0.0435 -0.1652 92  LEU B CB  
10280 C CG  . LEU B 88  ? 0.8910 0.9928 0.7589 0.1295  -0.0370 -0.1469 92  LEU B CG  
10281 C CD1 . LEU B 88  ? 0.8171 0.9094 0.6975 0.1229  -0.0411 -0.1238 92  LEU B CD1 
10282 C CD2 . LEU B 88  ? 0.9773 1.0965 0.8210 0.1257  -0.0416 -0.1552 92  LEU B CD2 
10294 N N   . ILE B 89  ? 1.0428 1.0872 0.9224 0.1488  -0.0650 -0.2171 93  ILE B N   
10295 C CA  . ILE B 89  ? 1.0924 1.1039 0.9836 0.1493  -0.0795 -0.2261 93  ILE B CA  
10296 C C   . ILE B 89  ? 1.0369 1.0389 0.9317 0.1359  -0.0893 -0.2090 93  ILE B C   
10297 O O   . ILE B 89  ? 1.0474 1.0649 0.9287 0.1291  -0.0920 -0.2054 93  ILE B O   
10298 C CB  . ILE B 89  ? 1.2204 1.2245 1.1007 0.1567  -0.0888 -0.2560 93  ILE B CB  
10299 C CG1 . ILE B 89  ? 1.2779 1.2944 1.1578 0.1718  -0.0790 -0.2753 93  ILE B CG1 
10300 C CG2 . ILE B 89  ? 1.2708 1.2365 1.1620 0.1542  -0.1065 -0.2620 93  ILE B CG2 
10301 C CD1 . ILE B 89  ? 1.2981 1.2917 1.1993 0.1807  -0.0802 -0.2773 93  ILE B CD1 
10313 N N   . LEU B 90  ? 1.0228 1.0015 0.9357 0.1317  -0.0950 -0.1987 94  LEU B N   
10314 C CA  . LEU B 90  ? 1.0113 0.9836 0.9312 0.1186  -0.1036 -0.1827 94  LEU B CA  
10315 C C   . LEU B 90  ? 1.0548 0.9956 0.9820 0.1141  -0.1196 -0.1917 94  LEU B C   
10316 O O   . LEU B 90  ? 1.0610 0.9808 1.0016 0.1155  -0.1210 -0.1892 94  LEU B O   
10317 C CB  . LEU B 90  ? 0.9622 0.9404 0.8969 0.1149  -0.0943 -0.1587 94  LEU B CB  
10318 C CG  . LEU B 90  ? 0.9564 0.9373 0.9002 0.1027  -0.1001 -0.1411 94  LEU B CG  
10319 C CD1 . LEU B 90  ? 0.9672 0.9682 0.8980 0.0982  -0.1041 -0.1398 94  LEU B CD1 
10320 C CD2 . LEU B 90  ? 0.9356 0.9240 0.8931 0.1023  -0.0890 -0.1212 94  LEU B CD2 
10332 N N   . LYS B 91  ? 1.0973 1.0341 1.0147 0.1079  -0.1325 -0.2017 95  LYS B N   
10333 C CA  . LYS B 91  ? 1.1449 1.0513 1.0681 0.1000  -0.1498 -0.2080 95  LYS B CA  
10334 C C   . LYS B 91  ? 1.1287 1.0391 1.0628 0.0839  -0.1545 -0.1869 95  LYS B C   
10335 O O   . LYS B 91  ? 1.1204 1.0511 1.0483 0.0773  -0.1565 -0.1818 95  LYS B O   
10336 C CB  . LYS B 91  ? 1.2182 1.1178 1.1249 0.1015  -0.1621 -0.2320 95  LYS B CB  
10337 C CG  . LYS B 91  ? 1.2588 1.1549 1.1560 0.1183  -0.1587 -0.2569 95  LYS B CG  
10338 C CD  . LYS B 91  ? 1.3635 1.2507 1.2447 0.1189  -0.1725 -0.2818 95  LYS B CD  
10339 C CE  . LYS B 91  ? 1.4580 1.3520 1.3276 0.1366  -0.1669 -0.3088 95  LYS B CE  
10340 N NZ  . LYS B 91  ? 1.5544 1.4443 1.4060 0.1369  -0.1794 -0.3339 95  LYS B NZ  
10354 N N   . LEU B 92  ? 1.1010 0.9943 1.0514 0.0774  -0.1565 -0.1746 96  LEU B N   
10355 C CA  . LEU B 92  ? 1.1085 1.0108 1.0720 0.0628  -0.1581 -0.1541 96  LEU B CA  
10356 C C   . LEU B 92  ? 1.1806 1.0561 1.1504 0.0485  -0.1750 -0.1550 96  LEU B C   
10357 O O   . LEU B 92  ? 1.1749 1.0214 1.1487 0.0494  -0.1803 -0.1587 96  LEU B O   
10358 C CB  . LEU B 92  ? 1.0498 0.9612 1.0269 0.0651  -0.1438 -0.1361 96  LEU B CB  
10359 C CG  . LEU B 92  ? 1.0159 0.9601 0.9942 0.0681  -0.1307 -0.1228 96  LEU B CG  
10360 C CD1 . LEU B 92  ? 0.9648 0.9120 0.9545 0.0727  -0.1172 -0.1098 96  LEU B CD1 
10361 C CD2 . LEU B 92  ? 1.0279 0.9897 1.0129 0.0558  -0.1369 -0.1118 96  LEU B CD2 
10373 N N   . ARG B 93  ? 1.2742 1.1594 1.2450 0.0349  -0.1845 -0.1509 97  ARG B N   
10374 C CA  . ARG B 93  ? 1.3528 1.2172 1.3313 0.0173  -0.2000 -0.1474 97  ARG B CA  
10375 C C   . ARG B 93  ? 1.3527 1.2229 1.3492 0.0077  -0.1934 -0.1259 97  ARG B C   
10376 O O   . ARG B 93  ? 1.3514 1.2508 1.3558 0.0109  -0.1796 -0.1127 97  ARG B O   
10377 C CB  . ARG B 93  ? 1.4113 1.2898 1.3867 0.0048  -0.2115 -0.1490 97  ARG B CB  
10378 C CG  . ARG B 93  ? 1.4441 1.3033 1.4269 -0.0159 -0.2286 -0.1456 97  ARG B CG  
10379 C CD  . ARG B 93  ? 1.4155 1.2913 1.3953 -0.0277 -0.2401 -0.1483 97  ARG B CD  
10380 N NE  . ARG B 93  ? 1.3994 1.2667 1.3906 -0.0509 -0.2537 -0.1393 97  ARG B NE  
10381 C CZ  . ARG B 93  ? 1.4249 1.2933 1.4135 -0.0654 -0.2697 -0.1445 97  ARG B CZ  
10382 N NH1 . ARG B 93  ? 1.4298 1.2918 1.4300 -0.0881 -0.2812 -0.1345 97  ARG B NH1 
10383 N NH2 . ARG B 93  ? 1.4223 1.2990 1.3960 -0.0585 -0.2744 -0.1594 97  ARG B NH2 
10397 N N   . PRO B 94  ? 1.3877 1.2301 1.3902 -0.0042 -0.2035 -0.1220 98  PRO B N   
10398 C CA  . PRO B 94  ? 1.3472 1.1979 1.3650 -0.0153 -0.1971 -0.1015 98  PRO B CA  
10399 C C   . PRO B 94  ? 1.4385 1.3277 1.4678 -0.0261 -0.1926 -0.0882 98  PRO B C   
10400 O O   . PRO B 94  ? 1.3078 1.2060 1.3360 -0.0357 -0.2030 -0.0916 98  PRO B O   
10401 C CB  . PRO B 94  ? 1.4460 1.2600 1.4645 -0.0311 -0.2141 -0.1006 98  PRO B CB  
10402 C CG  . PRO B 94  ? 1.4968 1.2765 1.5016 -0.0197 -0.2252 -0.1217 98  PRO B CG  
10403 C CD  . PRO B 94  ? 1.4622 1.2626 1.4567 -0.0069 -0.2211 -0.1363 98  PRO B CD  
10411 N N   . GLY B 95  ? 1.4932 1.4058 1.5341 -0.0239 -0.1776 -0.0739 99  GLY B N   
10412 C CA  . GLY B 95  ? 1.6099 1.5605 1.6645 -0.0317 -0.1727 -0.0620 99  GLY B CA  
10413 C C   . GLY B 95  ? 1.5593 1.5355 1.6101 -0.0211 -0.1698 -0.0667 99  GLY B C   
10414 O O   . GLY B 95  ? 1.6090 1.6150 1.6709 -0.0281 -0.1708 -0.0596 99  GLY B O   
10418 N N   . GLY B 96  ? 1.4477 1.4148 1.4832 -0.0046 -0.1663 -0.0782 100 GLY B N   
10419 C CA  . GLY B 96  ? 1.3446 1.3348 1.3732 0.0050  -0.1635 -0.0812 100 GLY B CA  
10420 C C   . GLY B 96  ? 1.2407 1.2390 1.2660 0.0221  -0.1474 -0.0782 100 GLY B C   
10421 O O   . GLY B 96  ? 1.2000 1.1812 1.2245 0.0282  -0.1401 -0.0789 100 GLY B O   
10425 N N   . ALA B 97  ? 1.1191 1.1425 1.1425 0.0292  -0.1428 -0.0740 101 ALA B N   
10426 C CA  . ALA B 97  ? 1.0488 1.0808 1.0697 0.0433  -0.1284 -0.0688 101 ALA B CA  
10427 C C   . ALA B 97  ? 0.9763 1.0176 0.9791 0.0516  -0.1290 -0.0750 101 ALA B C   
10428 O O   . ALA B 97  ? 1.0044 1.0591 1.0034 0.0470  -0.1386 -0.0760 101 ALA B O   
10429 C CB  . ALA B 97  ? 1.0519 1.1068 1.0916 0.0432  -0.1207 -0.0529 101 ALA B CB  
10435 N N   . GLN B 98  ? 0.8652 0.9008 0.8564 0.0630  -0.1190 -0.0788 102 GLN B N   
10436 C CA  . GLN B 98  ? 0.8016 0.8477 0.7735 0.0703  -0.1173 -0.0834 102 GLN B CA  
10437 C C   . GLN B 98  ? 0.7451 0.8020 0.7184 0.0790  -0.1039 -0.0714 102 GLN B C   
10438 O O   . GLN B 98  ? 0.7300 0.7776 0.7106 0.0832  -0.0941 -0.0687 102 GLN B O   
10439 C CB  . GLN B 98  ? 0.8301 0.8606 0.7843 0.0748  -0.1185 -0.1024 102 GLN B CB  
10440 C CG  . GLN B 98  ? 0.9282 0.9684 0.8617 0.0744  -0.1261 -0.1131 102 GLN B CG  
10441 C CD  . GLN B 98  ? 0.9990 1.0403 0.9354 0.0630  -0.1419 -0.1153 102 GLN B CD  
10442 O OE1 . GLN B 98  ? 1.0186 1.0544 0.9732 0.0547  -0.1469 -0.1085 102 GLN B OE1 
10443 N NE2 . GLN B 98  ? 1.0541 1.1040 0.9719 0.0616  -0.1499 -0.1248 102 GLN B NE2 
10452 N N   . THR B 99  ? 0.7404 0.8155 0.7064 0.0810  -0.1048 -0.0637 103 THR B N   
10453 C CA  . THR B 99  ? 0.7340 0.8176 0.6998 0.0880  -0.0946 -0.0510 103 THR B CA  
10454 C C   . THR B 99  ? 0.7337 0.8187 0.6761 0.0929  -0.0889 -0.0573 103 THR B C   
10455 O O   . THR B 99  ? 0.7408 0.8339 0.6652 0.0909  -0.0955 -0.0637 103 THR B O   
10456 C CB  . THR B 99  ? 0.7187 0.8201 0.6913 0.0873  -0.1006 -0.0371 103 THR B CB  
10457 O OG1 . THR B 99  ? 0.7641 0.8700 0.7583 0.0815  -0.1071 -0.0342 103 THR B OG1 
10458 C CG2 . THR B 99  ? 0.6411 0.7459 0.6175 0.0945  -0.0913 -0.0233 103 THR B CG2 
10466 N N   . LEU B 100 ? 0.7131 0.7926 0.6557 0.0985  -0.0766 -0.0557 104 LEU B N   
10467 C CA  . LEU B 100 ? 0.7638 0.8491 0.6864 0.1024  -0.0690 -0.0599 104 LEU B CA  
10468 C C   . LEU B 100 ? 0.7961 0.8915 0.7154 0.1037  -0.0641 -0.0423 104 LEU B C   
10469 O O   . LEU B 100 ? 0.7861 0.8778 0.7221 0.1054  -0.0611 -0.0299 104 LEU B O   
10470 C CB  . LEU B 100 ? 0.7852 0.8592 0.7104 0.1074  -0.0593 -0.0702 104 LEU B CB  
10471 C CG  . LEU B 100 ? 0.8211 0.8784 0.7535 0.1071  -0.0649 -0.0856 104 LEU B CG  
10472 C CD1 . LEU B 100 ? 0.8069 0.8529 0.7467 0.1131  -0.0557 -0.0907 104 LEU B CD1 
10473 C CD2 . LEU B 100 ? 0.8909 0.9501 0.8060 0.1065  -0.0728 -0.1034 104 LEU B CD2 
10485 N N   . GLN B 101 ? 0.8312 0.9390 0.7281 0.1024  -0.0637 -0.0414 105 GLN B N   
10486 C CA  . GLN B 101 ? 0.8679 0.9830 0.7576 0.1022  -0.0601 -0.0243 105 GLN B CA  
10487 C C   . GLN B 101 ? 0.9028 1.0192 0.7838 0.1039  -0.0465 -0.0268 105 GLN B C   
10488 O O   . GLN B 101 ? 0.9289 1.0533 0.7942 0.1036  -0.0426 -0.0409 105 GLN B O   
10489 C CB  . GLN B 101 ? 0.9437 1.0728 0.8127 0.0975  -0.0695 -0.0186 105 GLN B CB  
10490 C CG  . GLN B 101 ? 1.0221 1.1530 0.9016 0.0960  -0.0838 -0.0132 105 GLN B CG  
10491 C CD  . GLN B 101 ? 1.0923 1.2178 0.9949 0.0997  -0.0850 0.0028  105 GLN B CD  
10492 O OE1 . GLN B 101 ? 1.1110 1.2332 1.0358 0.1009  -0.0885 0.0008  105 GLN B OE1 
10493 N NE2 . GLN B 101 ? 1.1079 1.2332 1.0054 0.1012  -0.0824 0.0182  105 GLN B NE2 
10502 N N   . VAL B 102 ? 0.8904 1.0005 0.7823 0.1057  -0.0396 -0.0142 106 VAL B N   
10503 C CA  . VAL B 102 ? 0.8518 0.9633 0.7395 0.1065  -0.0268 -0.0151 106 VAL B CA  
10504 C C   . VAL B 102 ? 0.8523 0.9668 0.7317 0.1028  -0.0251 0.0044  106 VAL B C   
10505 O O   . VAL B 102 ? 0.8755 0.9810 0.7664 0.1040  -0.0305 0.0185  106 VAL B O   
10506 C CB  . VAL B 102 ? 0.8299 0.9275 0.7393 0.1114  -0.0201 -0.0198 106 VAL B CB  
10507 C CG1 . VAL B 102 ? 0.8527 0.9544 0.7583 0.1122  -0.0077 -0.0222 106 VAL B CG1 
10508 C CG2 . VAL B 102 ? 0.8338 0.9242 0.7516 0.1139  -0.0248 -0.0364 106 VAL B CG2 
10518 N N   . HIS B 103 ? 0.8583 0.9857 0.7181 0.0981  -0.0182 0.0050  107 HIS B N   
10519 C CA  . HIS B 103 ? 0.8552 0.9855 0.7025 0.0918  -0.0177 0.0243  107 HIS B CA  
10520 C C   . HIS B 103 ? 0.8464 0.9784 0.6950 0.0899  -0.0045 0.0255  107 HIS B C   
10521 O O   . HIS B 103 ? 0.8614 1.0069 0.7044 0.0900  0.0046  0.0109  107 HIS B O   
10522 C CB  . HIS B 103 ? 0.8742 1.0221 0.6928 0.0841  -0.0224 0.0270  107 HIS B CB  
10523 C CG  . HIS B 103 ? 0.9301 1.0796 0.7458 0.0854  -0.0354 0.0225  107 HIS B CG  
10524 N ND1 . HIS B 103 ? 0.9275 1.0688 0.7485 0.0857  -0.0483 0.0375  107 HIS B ND1 
10525 C CD2 . HIS B 103 ? 0.9386 1.0968 0.7476 0.0865  -0.0381 0.0039  107 HIS B CD2 
10526 C CE1 . HIS B 103 ? 0.9447 1.0917 0.7626 0.0862  -0.0582 0.0292  107 HIS B CE1 
10527 N NE2 . HIS B 103 ? 0.9463 1.1024 0.7562 0.0862  -0.0524 0.0089  107 HIS B NE2 
10535 N N   . VAL B 104 ? 0.8218 0.9407 0.6786 0.0887  -0.0042 0.0420  108 VAL B N   
10536 C CA  . VAL B 104 ? 0.8000 0.9190 0.6597 0.0857  0.0070  0.0452  108 VAL B CA  
10537 C C   . VAL B 104 ? 0.8772 0.9956 0.7209 0.0756  0.0048  0.0664  108 VAL B C   
10538 O O   . VAL B 104 ? 0.8732 0.9793 0.7152 0.0751  -0.0067 0.0812  108 VAL B O   
10539 C CB  . VAL B 104 ? 0.7042 0.8044 0.5900 0.0929  0.0097  0.0439  108 VAL B CB  
10540 C CG1 . VAL B 104 ? 0.7061 0.8076 0.5943 0.0891  0.0206  0.0467  108 VAL B CG1 
10541 C CG2 . VAL B 104 ? 0.6749 0.7734 0.5750 0.1011  0.0100  0.0255  108 VAL B CG2 
10551 N N   . ARG B 105 ? 0.9185 1.0506 0.7511 0.0673  0.0149  0.0679  109 ARG B N   
10552 C CA  . ARG B 105 ? 0.9055 1.0370 0.7218 0.0549  0.0136  0.0888  109 ARG B CA  
10553 C C   . ARG B 105 ? 0.8396 0.9798 0.6588 0.0490  0.0268  0.0874  109 ARG B C   
10554 O O   . ARG B 105 ? 0.8232 0.9867 0.6407 0.0494  0.0376  0.0711  109 ARG B O   
10555 C CB  . ARG B 105 ? 0.9471 1.0983 0.7337 0.0448  0.0098  0.0942  109 ARG B CB  
10556 C CG  . ARG B 105 ? 1.0155 1.1649 0.7822 0.0296  0.0064  0.1186  109 ARG B CG  
10557 C CD  . ARG B 105 ? 1.1069 1.2811 0.8419 0.0181  0.0047  0.1221  109 ARG B CD  
10558 N NE  . ARG B 105 ? 1.2371 1.4120 0.9502 0.0006  0.0023  0.1461  109 ARG B NE  
10559 C CZ  . ARG B 105 ? 1.3339 1.5231 1.0409 -0.0115 0.0141  0.1500  109 ARG B CZ  
10560 N NH1 . ARG B 105 ? 1.3530 1.5577 1.0755 -0.0062 0.0291  0.1306  109 ARG B NH1 
10561 N NH2 . ARG B 105 ? 1.4020 1.5899 1.0877 -0.0294 0.0100  0.1740  109 ARG B NH2 
10575 N N   . GLN B 106 ? 0.7932 0.9153 0.6180 0.0443  0.0254  0.1035  110 GLN B N   
10576 C CA  . GLN B 106 ? 0.7440 0.8735 0.5726 0.0372  0.0367  0.1040  110 GLN B CA  
10577 C C   . GLN B 106 ? 0.7907 0.9409 0.5933 0.0193  0.0402  0.1165  110 GLN B C   
10578 O O   . GLN B 106 ? 0.8309 0.9710 0.6165 0.0101  0.0302  0.1364  110 GLN B O   
10579 C CB  . GLN B 106 ? 0.6915 0.7914 0.5371 0.0392  0.0332  0.1145  110 GLN B CB  
10580 C CG  . GLN B 106 ? 0.6701 0.7547 0.5415 0.0550  0.0326  0.1011  110 GLN B CG  
10581 C CD  . GLN B 106 ? 0.7463 0.8103 0.6342 0.0561  0.0341  0.1059  110 GLN B CD  
10582 O OE1 . GLN B 106 ? 0.8124 0.8519 0.7113 0.0626  0.0258  0.1116  110 GLN B OE1 
10583 N NE2 . GLN B 106 ? 0.8024 0.8781 0.6927 0.0499  0.0445  0.1024  110 GLN B NE2 
10592 N N   . THR B 107 ? 0.7531 0.9336 0.5527 0.0143  0.0539  0.1050  111 THR B N   
10593 C CA  . THR B 107 ? 0.8148 1.0213 0.5905 -0.0044 0.0595  0.1158  111 THR B CA  
10594 C C   . THR B 107 ? 0.8424 1.0318 0.6177 -0.0180 0.0575  0.1379  111 THR B C   
10595 O O   . THR B 107 ? 0.8399 1.0070 0.6365 -0.0120 0.0572  0.1379  111 THR B O   
10596 C CB  . THR B 107 ? 0.8534 1.1005 0.6297 -0.0046 0.0754  0.0951  111 THR B CB  
10597 O OG1 . THR B 107 ? 0.8781 1.1567 0.6281 -0.0234 0.0812  0.1042  111 THR B OG1 
10598 C CG2 . THR B 107 ? 0.8402 1.0868 0.6407 -0.0009 0.0843  0.0877  111 THR B CG2 
10606 N N   . GLU B 108 ? 0.8970 1.0965 0.6465 -0.0375 0.0555  0.1572  112 GLU B N   
10607 C CA  . GLU B 108 ? 0.9332 1.1107 0.6795 -0.0521 0.0501  0.1811  112 GLU B CA  
10608 C C   . GLU B 108 ? 0.9440 1.1351 0.7040 -0.0585 0.0629  0.1762  112 GLU B C   
10609 O O   . GLU B 108 ? 0.9511 1.1149 0.7206 -0.0630 0.0583  0.1886  112 GLU B O   
10610 C CB  . GLU B 108 ? 0.9865 1.1718 0.6997 -0.0737 0.0439  0.2045  112 GLU B CB  
10611 C CG  . GLU B 108 ? 1.0434 1.2075 0.7430 -0.0692 0.0270  0.2155  112 GLU B CG  
10612 C CD  . GLU B 108 ? 1.1088 1.3009 0.7990 -0.0610 0.0304  0.1977  112 GLU B CD  
10613 O OE1 . GLU B 108 ? 1.1128 1.3371 0.8095 -0.0561 0.0455  0.1748  112 GLU B OE1 
10614 O OE2 . GLU B 108 ? 1.1821 1.3635 0.8586 -0.0592 0.0171  0.2062  112 GLU B OE2 
10621 N N   . ASP B 109 ? 0.9407 1.1736 0.7027 -0.0586 0.0783  0.1576  113 ASP B N   
10622 C CA  . ASP B 109 ? 0.9181 1.1700 0.6947 -0.0641 0.0908  0.1513  113 ASP B CA  
10623 C C   . ASP B 109 ? 0.8531 1.1187 0.6540 -0.0432 0.0995  0.1221  113 ASP B C   
10624 O O   . ASP B 109 ? 0.8297 1.1296 0.6264 -0.0381 0.1079  0.1039  113 ASP B O   
10625 C CB  . ASP B 109 ? 0.9692 1.2644 0.7256 -0.0867 0.1013  0.1581  113 ASP B CB  
10626 C CG  . ASP B 109 ? 0.9798 1.2892 0.7497 -0.0977 0.1108  0.1596  113 ASP B CG  
10627 O OD1 . ASP B 109 ? 0.9647 1.2629 0.7616 -0.0835 0.1131  0.1464  113 ASP B OD1 
10628 O OD2 . ASP B 109 ? 1.0575 1.3903 0.8107 -0.1215 0.1154  0.1747  113 ASP B OD2 
10633 N N   . TYR B 110 ? 0.8282 1.0659 0.6535 -0.0312 0.0967  0.1175  114 TYR B N   
10634 C CA  . TYR B 110 ? 0.7319 0.9770 0.5807 -0.0125 0.1028  0.0928  114 TYR B CA  
10635 C C   . TYR B 110 ? 0.6695 0.9142 0.5378 -0.0151 0.1083  0.0920  114 TYR B C   
10636 O O   . TYR B 110 ? 0.6800 0.8949 0.5513 -0.0217 0.1018  0.1081  114 TYR B O   
10637 C CB  . TYR B 110 ? 0.6922 0.9036 0.5517 0.0060  0.0927  0.0866  114 TYR B CB  
10638 C CG  . TYR B 110 ? 0.6728 0.8955 0.5475 0.0241  0.0970  0.0608  114 TYR B CG  
10639 C CD1 . TYR B 110 ? 0.6993 0.9522 0.5641 0.0274  0.1020  0.0456  114 TYR B CD1 
10640 C CD2 . TYR B 110 ? 0.6344 0.8365 0.5325 0.0374  0.0952  0.0518  114 TYR B CD2 
10641 C CE1 . TYR B 110 ? 0.6803 0.9396 0.5590 0.0441  0.1041  0.0219  114 TYR B CE1 
10642 C CE2 . TYR B 110 ? 0.6134 0.8223 0.5245 0.0529  0.0972  0.0301  114 TYR B CE2 
10643 C CZ  . TYR B 110 ? 0.6524 0.8884 0.5541 0.0565  0.1011  0.0151  114 TYR B CZ  
10644 O OH  . TYR B 110 ? 0.6453 0.8844 0.5599 0.0721  0.1013  -0.0068 114 TYR B OH  
10654 N N   . PRO B 111 ? 0.7041 0.9804 0.5861 -0.0097 0.1193  0.0734  115 PRO B N   
10655 C CA  . PRO B 111 ? 0.6962 0.9745 0.5972 -0.0127 0.1239  0.0727  115 PRO B CA  
10656 C C   . PRO B 111 ? 0.6198 0.8571 0.5389 0.0000  0.1157  0.0720  115 PRO B C   
10657 O O   . PRO B 111 ? 0.5924 0.8068 0.5145 0.0144  0.1089  0.0662  115 PRO B O   
10658 C CB  . PRO B 111 ? 0.7252 1.0467 0.6386 -0.0045 0.1355  0.0492  115 PRO B CB  
10659 C CG  . PRO B 111 ? 0.7457 1.0747 0.6515 0.0088  0.1347  0.0341  115 PRO B CG  
10660 C CD  . PRO B 111 ? 0.7471 1.0604 0.6278 -0.0010 0.1274  0.0516  115 PRO B CD  
10668 N N   . VAL B 112 ? 0.6275 0.8574 0.5584 -0.0067 0.1166  0.0779  116 VAL B N   
10669 C CA  . VAL B 112 ? 0.6335 0.8254 0.5791 0.0018  0.1092  0.0794  116 VAL B CA  
10670 C C   . VAL B 112 ? 0.6838 0.8884 0.6488 0.0019  0.1149  0.0712  116 VAL B C   
10671 O O   . VAL B 112 ? 0.7178 0.9356 0.6817 -0.0143 0.1186  0.0804  116 VAL B O   
10672 C CB  . VAL B 112 ? 0.6132 0.7692 0.5484 -0.0089 0.0995  0.1011  116 VAL B CB  
10673 C CG1 . VAL B 112 ? 0.5500 0.6704 0.5008 0.0009  0.0929  0.0997  116 VAL B CG1 
10674 C CG2 . VAL B 112 ? 0.6238 0.7681 0.5404 -0.0086 0.0924  0.1100  116 VAL B CG2 
10684 N N   . ASP B 113 ? 0.6823 0.8829 0.6647 0.0190  0.1146  0.0549  117 ASP B N   
10685 C CA  . ASP B 113 ? 0.6616 0.8652 0.6632 0.0211  0.1166  0.0486  117 ASP B CA  
10686 C C   . ASP B 113 ? 0.6694 0.8315 0.6758 0.0230  0.1083  0.0563  117 ASP B C   
10687 O O   . ASP B 113 ? 0.7172 0.8525 0.7212 0.0329  0.1018  0.0562  117 ASP B O   
10688 C CB  . ASP B 113 ? 0.6351 0.8557 0.6524 0.0384  0.1194  0.0273  117 ASP B CB  
10689 C CG  . ASP B 113 ? 0.6610 0.9258 0.6768 0.0386  0.1282  0.0157  117 ASP B CG  
10690 O OD1 . ASP B 113 ? 0.6576 0.9477 0.6641 0.0226  0.1345  0.0240  117 ASP B OD1 
10691 O OD2 . ASP B 113 ? 0.6354 0.9097 0.6592 0.0544  0.1285  -0.0021 117 ASP B OD2 
10696 N N   . LEU B 114 ? 0.6468 0.8055 0.6602 0.0133  0.1084  0.0621  118 LEU B N   
10697 C CA  . LEU B 114 ? 0.6066 0.7290 0.6253 0.0151  0.1012  0.0668  118 LEU B CA  
10698 C C   . LEU B 114 ? 0.5642 0.6961 0.5999 0.0159  0.1033  0.0589  118 LEU B C   
10699 O O   . LEU B 114 ? 0.5616 0.7147 0.6004 0.0030  0.1075  0.0622  118 LEU B O   
10700 C CB  . LEU B 114 ? 0.6707 0.7696 0.6767 0.0000  0.0958  0.0854  118 LEU B CB  
10701 C CG  . LEU B 114 ? 0.7020 0.7610 0.7120 0.0039  0.0875  0.0886  118 LEU B CG  
10702 C CD1 . LEU B 114 ? 0.7150 0.7445 0.7107 -0.0019 0.0793  0.1037  118 LEU B CD1 
10703 C CD2 . LEU B 114 ? 0.7249 0.7829 0.7444 -0.0049 0.0878  0.0888  118 LEU B CD2 
10715 N N   . TYR B 115 ? 0.5296 0.6468 0.5760 0.0299  0.0999  0.0491  119 TYR B N   
10716 C CA  . TYR B 115 ? 0.5099 0.6314 0.5713 0.0313  0.0998  0.0425  119 TYR B CA  
10717 C C   . TYR B 115 ? 0.5280 0.6150 0.5884 0.0282  0.0934  0.0490  119 TYR B C   
10718 O O   . TYR B 115 ? 0.5136 0.5748 0.5710 0.0373  0.0888  0.0482  119 TYR B O   
10719 C CB  . TYR B 115 ? 0.4960 0.6259 0.5692 0.0480  0.0995  0.0272  119 TYR B CB  
10720 C CG  . TYR B 115 ? 0.4964 0.6387 0.5854 0.0492  0.0991  0.0203  119 TYR B CG  
10721 C CD1 . TYR B 115 ? 0.5219 0.7001 0.6201 0.0437  0.1045  0.0165  119 TYR B CD1 
10722 C CD2 . TYR B 115 ? 0.5207 0.6410 0.6156 0.0555  0.0932  0.0175  119 TYR B CD2 
10723 C CE1 . TYR B 115 ? 0.5248 0.7157 0.6389 0.0453  0.1031  0.0102  119 TYR B CE1 
10724 C CE2 . TYR B 115 ? 0.5298 0.6611 0.6382 0.0563  0.0916  0.0120  119 TYR B CE2 
10725 C CZ  . TYR B 115 ? 0.5197 0.6857 0.6384 0.0517  0.0960  0.0084  119 TYR B CZ  
10726 O OH  . TYR B 115 ? 0.5631 0.7410 0.6965 0.0531  0.0932  0.0029  119 TYR B OH  
10736 N N   . TYR B 116 ? 0.5230 0.6110 0.5861 0.0152  0.0931  0.0546  120 TYR B N   
10737 C CA  . TYR B 116 ? 0.5569 0.6130 0.6183 0.0108  0.0868  0.0597  120 TYR B CA  
10738 C C   . TYR B 116 ? 0.6080 0.6643 0.6821 0.0180  0.0853  0.0494  120 TYR B C   
10739 O O   . TYR B 116 ? 0.5897 0.6669 0.6734 0.0122  0.0871  0.0465  120 TYR B O   
10740 C CB  . TYR B 116 ? 0.5798 0.6346 0.6359 -0.0089 0.0860  0.0717  120 TYR B CB  
10741 C CG  . TYR B 116 ? 0.6428 0.6590 0.6932 -0.0142 0.0780  0.0784  120 TYR B CG  
10742 C CD1 . TYR B 116 ? 0.6743 0.6817 0.7319 -0.0174 0.0750  0.0743  120 TYR B CD1 
10743 C CD2 . TYR B 116 ? 0.6950 0.6838 0.7328 -0.0157 0.0727  0.0881  120 TYR B CD2 
10744 C CE1 . TYR B 116 ? 0.7062 0.6781 0.7584 -0.0216 0.0675  0.0781  120 TYR B CE1 
10745 C CE2 . TYR B 116 ? 0.7379 0.6904 0.7717 -0.0188 0.0645  0.0924  120 TYR B CE2 
10746 C CZ  . TYR B 116 ? 0.7323 0.6766 0.7732 -0.0217 0.0623  0.0866  120 TYR B CZ  
10747 O OH  . TYR B 116 ? 0.7697 0.6776 0.8063 -0.0239 0.0539  0.0887  120 TYR B OH  
10757 N N   . LEU B 117 ? 0.6331 0.6679 0.7070 0.0300  0.0816  0.0442  121 LEU B N   
10758 C CA  . LEU B 117 ? 0.5932 0.6261 0.6761 0.0369  0.0792  0.0355  121 LEU B CA  
10759 C C   . LEU B 117 ? 0.6421 0.6467 0.7210 0.0331  0.0744  0.0376  121 LEU B C   
10760 O O   . LEU B 117 ? 0.6616 0.6431 0.7334 0.0376  0.0721  0.0393  121 LEU B O   
10761 C CB  . LEU B 117 ? 0.5652 0.5977 0.6502 0.0520  0.0787  0.0279  121 LEU B CB  
10762 C CG  . LEU B 117 ? 0.6103 0.6393 0.7023 0.0587  0.0751  0.0205  121 LEU B CG  
10763 C CD1 . LEU B 117 ? 0.6426 0.6940 0.7458 0.0551  0.0750  0.0170  121 LEU B CD1 
10764 C CD2 . LEU B 117 ? 0.6122 0.6404 0.7050 0.0713  0.0739  0.0149  121 LEU B CD2 
10776 N N   . MET B 118 ? 0.6330 0.6406 0.7170 0.0253  0.0726  0.0364  122 MET B N   
10777 C CA  . MET B 118 ? 0.6191 0.6012 0.6981 0.0185  0.0679  0.0384  122 MET B CA  
10778 C C   . MET B 118 ? 0.5916 0.5708 0.6750 0.0214  0.0649  0.0305  122 MET B C   
10779 O O   . MET B 118 ? 0.5597 0.5602 0.6521 0.0208  0.0650  0.0269  122 MET B O   
10780 C CB  . MET B 118 ? 0.6246 0.6090 0.7021 0.0014  0.0672  0.0467  122 MET B CB  
10781 C CG  . MET B 118 ? 0.6613 0.6152 0.7326 -0.0063 0.0609  0.0486  122 MET B CG  
10782 S SD  . MET B 118 ? 0.7157 0.6684 0.7836 -0.0287 0.0584  0.0606  122 MET B SD  
10783 C CE  . MET B 118 ? 0.7572 0.6711 0.8197 -0.0334 0.0494  0.0574  122 MET B CE  
10793 N N   . ASP B 119 ? 0.5946 0.5485 0.6716 0.0248  0.0617  0.0275  123 ASP B N   
10794 C CA  . ASP B 119 ? 0.6297 0.5770 0.7068 0.0239  0.0582  0.0209  123 ASP B CA  
10795 C C   . ASP B 119 ? 0.6661 0.6141 0.7448 0.0095  0.0551  0.0231  123 ASP B C   
10796 O O   . ASP B 119 ? 0.7076 0.6403 0.7815 0.0007  0.0533  0.0285  123 ASP B O   
10797 C CB  . ASP B 119 ? 0.6462 0.5680 0.7154 0.0302  0.0565  0.0165  123 ASP B CB  
10798 C CG  . ASP B 119 ? 0.6497 0.5657 0.7164 0.0296  0.0536  0.0085  123 ASP B CG  
10799 O OD1 . ASP B 119 ? 0.6475 0.5737 0.7175 0.0220  0.0512  0.0076  123 ASP B OD1 
10800 O OD2 . ASP B 119 ? 0.6377 0.5407 0.6991 0.0366  0.0537  0.0027  123 ASP B OD2 
10805 N N   . LEU B 120 ? 0.6522 0.6174 0.7379 0.0064  0.0534  0.0195  124 LEU B N   
10806 C CA  . LEU B 120 ? 0.7265 0.6950 0.8149 -0.0080 0.0497  0.0209  124 LEU B CA  
10807 C C   . LEU B 120 ? 0.7775 0.7359 0.8625 -0.0093 0.0444  0.0135  124 LEU B C   
10808 O O   . LEU B 120 ? 0.7610 0.7297 0.8508 -0.0194 0.0406  0.0129  124 LEU B O   
10809 C CB  . LEU B 120 ? 0.7157 0.7188 0.8171 -0.0132 0.0517  0.0235  124 LEU B CB  
10810 C CG  . LEU B 120 ? 0.7320 0.7489 0.8357 -0.0208 0.0565  0.0318  124 LEU B CG  
10811 C CD1 . LEU B 120 ? 0.8040 0.8596 0.9224 -0.0267 0.0584  0.0316  124 LEU B CD1 
10812 C CD2 . LEU B 120 ? 0.7235 0.7168 0.8178 -0.0351 0.0538  0.0393  124 LEU B CD2 
10824 N N   . SER B 121 ? 0.8360 0.7769 0.9127 0.0000  0.0441  0.0077  125 SER B N   
10825 C CA  . SER B 121 ? 0.8262 0.7558 0.8964 -0.0028 0.0394  0.0002  125 SER B CA  
10826 C C   . SER B 121 ? 0.7825 0.6904 0.8472 -0.0141 0.0353  -0.0003 125 SER B C   
10827 O O   . SER B 121 ? 0.7474 0.6465 0.8125 -0.0194 0.0357  0.0064  125 SER B O   
10828 C CB  . SER B 121 ? 0.8498 0.7687 0.9119 0.0088  0.0411  -0.0062 125 SER B CB  
10829 O OG  . SER B 121 ? 0.9223 0.8225 0.9798 0.0146  0.0438  -0.0063 125 SER B OG  
10834 N N   . ALA B 122 ? 0.7747 0.6728 0.8331 -0.0185 0.0305  -0.0081 126 ALA B N   
10835 C CA  . ALA B 122 ? 0.7245 0.6040 0.7791 -0.0315 0.0247  -0.0093 126 ALA B CA  
10836 C C   . ALA B 122 ? 0.7321 0.5807 0.7802 -0.0293 0.0239  -0.0090 126 ALA B C   
10837 O O   . ALA B 122 ? 0.7477 0.5802 0.7946 -0.0411 0.0188  -0.0050 126 ALA B O   
10838 C CB  . ALA B 122 ? 0.6993 0.5733 0.7464 -0.0350 0.0194  -0.0199 126 ALA B CB  
10844 N N   . SER B 123 ? 0.6894 0.5294 0.7340 -0.0147 0.0279  -0.0127 127 SER B N   
10845 C CA  . SER B 123 ? 0.6810 0.4916 0.7209 -0.0105 0.0257  -0.0135 127 SER B CA  
10846 C C   . SER B 123 ? 0.7217 0.5308 0.7653 -0.0141 0.0263  0.0003  127 SER B C   
10847 O O   . SER B 123 ? 0.7425 0.5267 0.7825 -0.0102 0.0232  0.0019  127 SER B O   
10848 C CB  . SER B 123 ? 0.6891 0.4953 0.7258 0.0064  0.0297  -0.0224 127 SER B CB  
10849 O OG  . SER B 123 ? 0.6969 0.5247 0.7387 0.0146  0.0364  -0.0168 127 SER B OG  
10855 N N   . MET B 124 ? 0.7393 0.5750 0.7899 -0.0211 0.0297  0.0098  128 MET B N   
10856 C CA  . MET B 124 ? 0.7871 0.6270 0.8399 -0.0258 0.0314  0.0227  128 MET B CA  
10857 C C   . MET B 124 ? 0.8174 0.6623 0.8722 -0.0458 0.0279  0.0316  128 MET B C   
10858 O O   . MET B 124 ? 0.7908 0.6486 0.8477 -0.0527 0.0306  0.0430  128 MET B O   
10859 C CB  . MET B 124 ? 0.7636 0.6337 0.8228 -0.0169 0.0393  0.0255  128 MET B CB  
10860 C CG  . MET B 124 ? 0.7642 0.6322 0.8218 0.0007  0.0427  0.0179  128 MET B CG  
10861 S SD  . MET B 124 ? 0.7734 0.6148 0.8252 0.0106  0.0414  0.0200  128 MET B SD  
10862 C CE  . MET B 124 ? 0.7374 0.5955 0.7913 0.0068  0.0450  0.0339  128 MET B CE  
10872 N N   . ASP B 125 ? 0.8843 0.7211 0.9381 -0.0562 0.0221  0.0267  129 ASP B N   
10873 C CA  . ASP B 125 ? 0.9459 0.7867 1.0019 -0.0773 0.0179  0.0354  129 ASP B CA  
10874 C C   . ASP B 125 ? 0.9747 0.7866 1.0232 -0.0863 0.0125  0.0462  129 ASP B C   
10875 O O   . ASP B 125 ? 1.0042 0.8291 1.0544 -0.1011 0.0133  0.0594  129 ASP B O   
10876 C CB  . ASP B 125 ? 1.0346 0.8679 1.0897 -0.0863 0.0111  0.0267  129 ASP B CB  
10877 C CG  . ASP B 125 ? 1.1295 0.9703 1.1883 -0.1097 0.0064  0.0355  129 ASP B CG  
10878 O OD1 . ASP B 125 ? 1.1456 1.0250 1.2155 -0.1163 0.0109  0.0398  129 ASP B OD1 
10879 O OD2 . ASP B 125 ? 1.2157 1.0241 1.2670 -0.1217 -0.0024 0.0375  129 ASP B OD2 
10884 N N   . ASP B 126 ? 0.9379 0.7111 0.9780 -0.0777 0.0065  0.0409  130 ASP B N   
10885 C CA  . ASP B 126 ? 0.9158 0.6574 0.9485 -0.0838 -0.0006 0.0516  130 ASP B CA  
10886 C C   . ASP B 126 ? 0.8678 0.6258 0.9009 -0.0802 0.0057  0.0640  130 ASP B C   
10887 O O   . ASP B 126 ? 0.9012 0.6538 0.9298 -0.0946 0.0024  0.0791  130 ASP B O   
10888 C CB  . ASP B 126 ? 0.9577 0.6579 0.9840 -0.0700 -0.0080 0.0409  130 ASP B CB  
10889 C CG  . ASP B 126 ? 0.9446 0.6549 0.9735 -0.0465 -0.0005 0.0297  130 ASP B CG  
10890 O OD1 . ASP B 126 ? 0.9566 0.6980 0.9907 -0.0416 0.0076  0.0234  130 ASP B OD1 
10891 O OD2 . ASP B 126 ? 0.9722 0.6600 0.9984 -0.0333 -0.0035 0.0277  130 ASP B OD2 
10896 N N   . ASP B 127 ? 0.7927 0.5709 0.8299 -0.0621 0.0143  0.0580  131 ASP B N   
10897 C CA  . ASP B 127 ? 0.7777 0.5721 0.8147 -0.0577 0.0200  0.0678  131 ASP B CA  
10898 C C   . ASP B 127 ? 0.7762 0.6030 0.8164 -0.0746 0.0248  0.0795  131 ASP B C   
10899 O O   . ASP B 127 ? 0.7950 0.6259 0.8303 -0.0805 0.0258  0.0921  131 ASP B O   
10900 C CB  . ASP B 127 ? 0.7425 0.5560 0.7846 -0.0374 0.0282  0.0580  131 ASP B CB  
10901 C CG  . ASP B 127 ? 0.7717 0.5593 0.8114 -0.0211 0.0249  0.0463  131 ASP B CG  
10902 O OD1 . ASP B 127 ? 0.7778 0.5528 0.8171 -0.0214 0.0213  0.0359  131 ASP B OD1 
10903 O OD2 . ASP B 127 ? 0.7892 0.5710 0.8276 -0.0081 0.0259  0.0468  131 ASP B OD2 
10908 N N   . LEU B 128 ? 0.7582 0.6105 0.8066 -0.0829 0.0276  0.0752  132 LEU B N   
10909 C CA  . LEU B 128 ? 0.8052 0.6939 0.8593 -0.0985 0.0328  0.0843  132 LEU B CA  
10910 C C   . LEU B 128 ? 0.9184 0.7916 0.9651 -0.1221 0.0261  0.0990  132 LEU B C   
10911 O O   . LEU B 128 ? 0.9348 0.8297 0.9800 -0.1341 0.0302  0.1113  132 LEU B O   
10912 C CB  . LEU B 128 ? 0.7395 0.6589 0.8062 -0.1007 0.0358  0.0755  132 LEU B CB  
10913 C CG  . LEU B 128 ? 0.7389 0.6905 0.8156 -0.0834 0.0438  0.0660  132 LEU B CG  
10914 C CD1 . LEU B 128 ? 0.7319 0.7082 0.8206 -0.0875 0.0433  0.0588  132 LEU B CD1 
10915 C CD2 . LEU B 128 ? 0.7444 0.7268 0.8242 -0.0818 0.0522  0.0722  132 LEU B CD2 
10927 N N   . ASN B 129 ? 0.9823 0.8182 1.0235 -0.1297 0.0153  0.0979  133 ASN B N   
10928 C CA  . ASN B 129 ? 1.0492 0.8669 1.0831 -0.1542 0.0070  0.1125  133 ASN B CA  
10929 C C   . ASN B 129 ? 1.0311 0.8283 1.0529 -0.1564 0.0037  0.1273  133 ASN B C   
10930 O O   . ASN B 129 ? 1.0635 0.8615 1.0790 -0.1788 0.0004  0.1439  133 ASN B O   
10931 C CB  . ASN B 129 ? 1.1324 0.9086 1.1621 -0.1597 -0.0054 0.1061  133 ASN B CB  
10932 C CG  . ASN B 129 ? 1.1915 0.9898 1.2308 -0.1695 -0.0049 0.0980  133 ASN B CG  
10933 O OD1 . ASN B 129 ? 1.2169 1.0490 1.2630 -0.1877 -0.0014 0.1059  133 ASN B OD1 
10934 N ND2 . ASN B 129 ? 1.2346 1.0161 1.2746 -0.1577 -0.0084 0.0818  133 ASN B ND2 
10941 N N   . THR B 130 ? 0.9714 0.7516 0.9896 -0.1347 0.0040  0.1225  134 THR B N   
10942 C CA  . THR B 130 ? 0.9948 0.7513 1.0013 -0.1352 -0.0016 0.1361  134 THR B CA  
10943 C C   . THR B 130 ? 0.9490 0.7426 0.9544 -0.1336 0.0090  0.1442  134 THR B C   
10944 O O   . THR B 130 ? 0.9727 0.7524 0.9669 -0.1382 0.0045  0.1584  134 THR B O   
10945 C CB  . THR B 130 ? 1.0250 0.7423 1.0289 -0.1126 -0.0085 0.1266  134 THR B CB  
10946 O OG1 . THR B 130 ? 1.0396 0.7803 1.0520 -0.0902 0.0017  0.1118  134 THR B OG1 
10947 C CG2 . THR B 130 ? 1.0422 0.7193 1.0452 -0.1142 -0.0201 0.1179  134 THR B CG2 
10955 N N   . ILE B 131 ? 0.8961 0.7353 0.9123 -0.1271 0.0217  0.1355  135 ILE B N   
10956 C CA  . ILE B 131 ? 0.9022 0.7784 0.9179 -0.1248 0.0319  0.1404  135 ILE B CA  
10957 C C   . ILE B 131 ? 0.9474 0.8674 0.9676 -0.1454 0.0393  0.1472  135 ILE B C   
10958 O O   . ILE B 131 ? 0.8739 0.8351 0.8984 -0.1414 0.0501  0.1451  135 ILE B O   
10959 C CB  . ILE B 131 ? 0.8493 0.7442 0.8738 -0.0996 0.0403  0.1248  135 ILE B CB  
10960 C CG1 . ILE B 131 ? 0.7685 0.6844 0.8074 -0.0949 0.0447  0.1103  135 ILE B CG1 
10961 C CG2 . ILE B 131 ? 0.8687 0.7264 0.8886 -0.0806 0.0341  0.1198  135 ILE B CG2 
10962 C CD1 . ILE B 131 ? 0.6749 0.6144 0.7224 -0.0738 0.0528  0.0974  135 ILE B CD1 
10974 N N   . LYS B 132 ? 1.0576 0.9704 1.0772 -0.1676 0.0335  0.1546  136 LYS B N   
10975 C CA  . LYS B 132 ? 1.0452 1.0039 1.0713 -0.1883 0.0408  0.1604  136 LYS B CA  
10976 C C   . LYS B 132 ? 1.0082 0.9922 1.0244 -0.1996 0.0468  0.1748  136 LYS B C   
10977 O O   . LYS B 132 ? 0.9675 1.0029 0.9913 -0.2087 0.0575  0.1748  136 LYS B O   
10978 C CB  . LYS B 132 ? 1.1183 1.0598 1.1435 -0.2129 0.0315  0.1682  136 LYS B CB  
10979 C CG  . LYS B 132 ? 1.1669 1.1017 1.2044 -0.2066 0.0282  0.1528  136 LYS B CG  
10980 C CD  . LYS B 132 ? 1.2778 1.1807 1.3103 -0.2294 0.0156  0.1604  136 LYS B CD  
10981 C CE  . LYS B 132 ? 1.3464 1.2463 1.3900 -0.2249 0.0124  0.1448  136 LYS B CE  
10982 N NZ  . LYS B 132 ? 1.4954 1.3529 1.5319 -0.2432 -0.0021 0.1494  136 LYS B NZ  
10996 N N   . GLU B 133 ? 1.0450 0.9955 1.0444 -0.1990 0.0399  0.1866  137 GLU B N   
10997 C CA  . GLU B 133 ? 1.0975 1.0682 1.0837 -0.2108 0.0441  0.2017  137 GLU B CA  
10998 C C   . GLU B 133 ? 1.0723 1.0344 1.0515 -0.1884 0.0456  0.1984  137 GLU B C   
10999 O O   . GLU B 133 ? 1.0707 1.0301 1.0338 -0.1964 0.0438  0.2131  137 GLU B O   
11000 C CB  . GLU B 133 ? 1.2140 1.1537 1.1833 -0.2384 0.0321  0.2247  137 GLU B CB  
11001 C CG  . GLU B 133 ? 1.3195 1.2748 1.2946 -0.2657 0.0313  0.2306  137 GLU B CG  
11002 C CD  . GLU B 133 ? 1.5276 1.4433 1.4855 -0.2934 0.0166  0.2534  137 GLU B CD  
11003 O OE1 . GLU B 133 ? 1.5942 1.4671 1.5361 -0.2894 0.0058  0.2643  137 GLU B OE1 
11004 O OE2 . GLU B 133 ? 1.5978 1.5248 1.5585 -0.3194 0.0149  0.2609  137 GLU B OE2 
11011 N N   . LEU B 134 ? 1.0006 0.9589 0.9909 -0.1615 0.0484  0.1800  138 LEU B N   
11012 C CA  . LEU B 134 ? 0.9067 0.8596 0.8921 -0.1406 0.0499  0.1758  138 LEU B CA  
11013 C C   . LEU B 134 ? 0.8237 0.8252 0.8069 -0.1417 0.0621  0.1761  138 LEU B C   
11014 O O   . LEU B 134 ? 0.7926 0.7904 0.7630 -0.1379 0.0612  0.1829  138 LEU B O   
11015 C CB  . LEU B 134 ? 0.8537 0.7968 0.8522 -0.1144 0.0510  0.1561  138 LEU B CB  
11016 C CG  . LEU B 134 ? 0.7950 0.7339 0.7911 -0.0923 0.0525  0.1499  138 LEU B CG  
11017 C CD1 . LEU B 134 ? 0.8227 0.7182 0.8053 -0.0908 0.0405  0.1613  138 LEU B CD1 
11018 C CD2 . LEU B 134 ? 0.7419 0.6805 0.7519 -0.0704 0.0554  0.1308  138 LEU B CD2 
11030 N N   . GLY B 135 ? 0.8045 0.8525 0.8003 -0.1463 0.0730  0.1678  139 GLY B N   
11031 C CA  . GLY B 135 ? 0.7547 0.8517 0.7500 -0.1457 0.0851  0.1647  139 GLY B CA  
11032 C C   . GLY B 135 ? 0.7622 0.8644 0.7368 -0.1650 0.0844  0.1840  139 GLY B C   
11033 O O   . GLY B 135 ? 0.7746 0.8888 0.7395 -0.1574 0.0882  0.1839  139 GLY B O   
11037 N N   . SER B 136 ? 0.7767 0.8690 0.7429 -0.1915 0.0788  0.2014  140 SER B N   
11038 C CA  . SER B 136 ? 0.8816 0.9781 0.8259 -0.2133 0.0770  0.2225  140 SER B CA  
11039 C C   . SER B 136 ? 0.9907 1.0347 0.9177 -0.2065 0.0634  0.2341  140 SER B C   
11040 O O   . SER B 136 ? 1.0459 1.0976 0.9570 -0.2071 0.0643  0.2420  140 SER B O   
11041 C CB  . SER B 136 ? 0.8936 0.9948 0.8342 -0.2458 0.0740  0.2388  140 SER B CB  
11042 O OG  . SER B 136 ? 0.9162 0.9655 0.8591 -0.2486 0.0601  0.2429  140 SER B OG  
11048 N N   . ARG B 137 ? 1.0361 1.0273 0.9660 -0.1996 0.0503  0.2343  141 ARG B N   
11049 C CA  . ARG B 137 ? 1.0794 1.0207 0.9965 -0.1902 0.0364  0.2432  141 ARG B CA  
11050 C C   . ARG B 137 ? 1.0378 0.9908 0.9547 -0.1660 0.0416  0.2324  141 ARG B C   
11051 O O   . ARG B 137 ? 1.0284 0.9719 0.9288 -0.1671 0.0362  0.2444  141 ARG B O   
11052 C CB  . ARG B 137 ? 1.1202 1.0103 1.0460 -0.1799 0.0241  0.2373  141 ARG B CB  
11053 C CG  . ARG B 137 ? 1.2091 1.0702 1.1292 -0.2047 0.0128  0.2522  141 ARG B CG  
11054 C CD  . ARG B 137 ? 1.3058 1.1229 1.2368 -0.1930 0.0028  0.2410  141 ARG B CD  
11055 N NE  . ARG B 137 ? 1.4472 1.2168 1.3742 -0.1734 -0.0098 0.2400  141 ARG B NE  
11056 C CZ  . ARG B 137 ? 1.5852 1.3385 1.5249 -0.1475 -0.0103 0.2209  141 ARG B CZ  
11057 N NH1 . ARG B 137 ? 1.5651 1.3421 1.5207 -0.1382 0.0001  0.2021  141 ARG B NH1 
11058 N NH2 . ARG B 137 ? 1.6851 1.3989 1.6216 -0.1311 -0.0219 0.2208  141 ARG B NH2 
11072 N N   . LEU B 138 ? 0.9937 0.9671 0.9285 -0.1449 0.0511  0.2104  142 LEU B N   
11073 C CA  . LEU B 138 ? 0.9396 0.9215 0.8755 -0.1221 0.0550  0.1991  142 LEU B CA  
11074 C C   . LEU B 138 ? 0.9233 0.9475 0.8476 -0.1295 0.0643  0.2032  142 LEU B C   
11075 O O   . LEU B 138 ? 0.9317 0.9494 0.8433 -0.1233 0.0608  0.2082  142 LEU B O   
11076 C CB  . LEU B 138 ? 0.8635 0.8578 0.8204 -0.1009 0.0624  0.1760  142 LEU B CB  
11077 C CG  . LEU B 138 ? 0.8517 0.8551 0.8116 -0.0779 0.0664  0.1630  142 LEU B CG  
11078 C CD1 . LEU B 138 ? 0.8620 0.8251 0.8136 -0.0674 0.0547  0.1691  142 LEU B CD1 
11079 C CD2 . LEU B 138 ? 0.8141 0.8279 0.7937 -0.0606 0.0723  0.1426  142 LEU B CD2 
11091 N N   . SER B 139 ? 0.9200 0.9901 0.8488 -0.1426 0.0761  0.2002  143 SER B N   
11092 C CA  . SER B 139 ? 0.9754 1.0911 0.8940 -0.1485 0.0865  0.2006  143 SER B CA  
11093 C C   . SER B 139 ? 0.9961 1.1032 0.8886 -0.1703 0.0800  0.2251  143 SER B C   
11094 O O   . SER B 139 ? 0.9307 1.0608 0.8091 -0.1707 0.0842  0.2270  143 SER B O   
11095 C CB  . SER B 139 ? 1.0212 1.1904 0.9527 -0.1574 0.1006  0.1909  143 SER B CB  
11096 O OG  . SER B 139 ? 1.1396 1.3044 1.0738 -0.1793 0.0977  0.2020  143 SER B OG  
11102 N N   . LYS B 140 ? 1.0346 1.1077 0.9192 -0.1891 0.0686  0.2440  144 LYS B N   
11103 C CA  . LYS B 140 ? 1.1475 1.2051 1.0059 -0.2099 0.0593  0.2695  144 LYS B CA  
11104 C C   . LYS B 140 ? 1.2103 1.2308 1.0584 -0.1927 0.0475  0.2732  144 LYS B C   
11105 O O   . LYS B 140 ? 1.2462 1.2763 1.0740 -0.1995 0.0460  0.2848  144 LYS B O   
11106 C CB  . LYS B 140 ? 1.2246 1.2492 1.0778 -0.2338 0.0476  0.2887  144 LYS B CB  
11107 C CG  . LYS B 140 ? 1.2766 1.2781 1.1015 -0.2568 0.0349  0.3178  144 LYS B CG  
11108 C CD  . LYS B 140 ? 1.3481 1.3490 1.1651 -0.2915 0.0312  0.3376  144 LYS B CD  
11109 C CE  . LYS B 140 ? 1.4571 1.3884 1.2679 -0.2982 0.0089  0.3542  144 LYS B CE  
11110 N NZ  . LYS B 140 ? 1.5716 1.4672 1.3577 -0.3025 -0.0071 0.3760  144 LYS B NZ  
11124 N N   . GLU B 141 ? 1.2023 1.1826 1.0641 -0.1707 0.0391  0.2631  145 GLU B N   
11125 C CA  . GLU B 141 ? 1.1192 1.0682 0.9752 -0.1525 0.0284  0.2644  145 GLU B CA  
11126 C C   . GLU B 141 ? 1.0298 1.0143 0.8863 -0.1363 0.0389  0.2500  145 GLU B C   
11127 O O   . GLU B 141 ? 1.0386 1.0177 0.8801 -0.1332 0.0328  0.2580  145 GLU B O   
11128 C CB  . GLU B 141 ? 1.0709 0.9759 0.9439 -0.1324 0.0191  0.2542  145 GLU B CB  
11129 C CG  . GLU B 141 ? 1.1756 1.0328 1.0441 -0.1453 0.0033  0.2697  145 GLU B CG  
11130 C CD  . GLU B 141 ? 1.3320 1.1605 1.1781 -0.1566 -0.0125 0.2940  145 GLU B CD  
11131 O OE1 . GLU B 141 ? 1.3833 1.2191 1.2208 -0.1468 -0.0137 0.2956  145 GLU B OE1 
11132 O OE2 . GLU B 141 ? 1.4160 1.2137 1.2526 -0.1760 -0.0246 0.3120  145 GLU B OE2 
11139 N N   . MET B 142 ? 0.9750 0.9950 0.8485 -0.1258 0.0535  0.2287  146 MET B N   
11140 C CA  . MET B 142 ? 0.9611 1.0137 0.8356 -0.1106 0.0630  0.2136  146 MET B CA  
11141 C C   . MET B 142 ? 0.9570 1.0507 0.8119 -0.1276 0.0706  0.2215  146 MET B C   
11142 O O   . MET B 142 ? 0.8979 1.0127 0.7471 -0.1172 0.0751  0.2126  146 MET B O   
11143 C CB  . MET B 142 ? 0.9398 1.0162 0.8378 -0.0952 0.0746  0.1893  146 MET B CB  
11144 C CG  . MET B 142 ? 0.9075 0.9485 0.8234 -0.0762 0.0684  0.1789  146 MET B CG  
11145 S SD  . MET B 142 ? 0.8791 0.8913 0.7929 -0.0539 0.0590  0.1753  146 MET B SD  
11146 C CE  . MET B 142 ? 0.8623 0.9192 0.7757 -0.0433 0.0708  0.1590  146 MET B CE  
11156 N N   . SER B 143 ? 1.0169 1.1233 0.8608 -0.1543 0.0721  0.2377  147 SER B N   
11157 C CA  . SER B 143 ? 1.0936 1.2414 0.9167 -0.1730 0.0796  0.2467  147 SER B CA  
11158 C C   . SER B 143 ? 1.0769 1.2035 0.8742 -0.1774 0.0677  0.2646  147 SER B C   
11159 O O   . SER B 143 ? 1.0612 1.2227 0.8408 -0.1848 0.0741  0.2664  147 SER B O   
11160 C CB  . SER B 143 ? 1.2263 1.3930 1.0440 -0.2030 0.0835  0.2614  147 SER B CB  
11161 O OG  . SER B 143 ? 1.3004 1.4985 1.1415 -0.1998 0.0961  0.2437  147 SER B OG  
11167 N N   . LYS B 144 ? 1.0924 1.1636 0.8873 -0.1726 0.0501  0.2773  148 LYS B N   
11168 C CA  . LYS B 144 ? 1.1245 1.1720 0.8974 -0.1742 0.0363  0.2943  148 LYS B CA  
11169 C C   . LYS B 144 ? 1.1240 1.1765 0.9009 -0.1487 0.0370  0.2779  148 LYS B C   
11170 O O   . LYS B 144 ? 1.1803 1.2262 0.9378 -0.1500 0.0282  0.2893  148 LYS B O   
11171 C CB  . LYS B 144 ? 1.1321 1.1179 0.9043 -0.1755 0.0159  0.3117  148 LYS B CB  
11172 C CG  . LYS B 144 ? 1.1402 1.1117 0.9106 -0.1998 0.0124  0.3271  148 LYS B CG  
11173 C CD  . LYS B 144 ? 1.1731 1.0795 0.9464 -0.1958 -0.0086 0.3391  148 LYS B CD  
11174 C CE  . LYS B 144 ? 1.2133 1.1020 0.9856 -0.2199 -0.0132 0.3530  148 LYS B CE  
11175 N NZ  . LYS B 144 ? 1.2552 1.0791 1.0334 -0.2127 -0.0335 0.3599  148 LYS B NZ  
11189 N N   . LEU B 145 ? 1.0751 1.1390 0.8759 -0.1267 0.0465  0.2524  149 LEU B N   
11190 C CA  . LEU B 145 ? 0.9771 1.0408 0.7846 -0.1023 0.0459  0.2362  149 LEU B CA  
11191 C C   . LEU B 145 ? 0.9276 1.0409 0.7379 -0.0958 0.0621  0.2154  149 LEU B C   
11192 O O   . LEU B 145 ? 0.9192 1.0405 0.7235 -0.0842 0.0611  0.2077  149 LEU B O   
11193 C CB  . LEU B 145 ? 0.9348 0.9660 0.7678 -0.0805 0.0414  0.2232  149 LEU B CB  
11194 C CG  . LEU B 145 ? 0.9662 0.9477 0.8015 -0.0834 0.0262  0.2383  149 LEU B CG  
11195 C CD1 . LEU B 145 ? 0.9788 0.9396 0.8400 -0.0644 0.0264  0.2218  149 LEU B CD1 
11196 C CD2 . LEU B 145 ? 0.9977 0.9498 0.8185 -0.0810 0.0095  0.2541  149 LEU B CD2 
11208 N N   . THR B 146 ? 0.8950 1.0412 0.7151 -0.1022 0.0759  0.2053  150 THR B N   
11209 C CA  . THR B 146 ? 0.9019 1.0966 0.7258 -0.0959 0.0910  0.1845  150 THR B CA  
11210 C C   . THR B 146 ? 0.9303 1.1659 0.7510 -0.1169 0.1031  0.1875  150 THR B C   
11211 O O   . THR B 146 ? 0.9285 1.1535 0.7557 -0.1297 0.1019  0.1977  150 THR B O   
11212 C CB  . THR B 146 ? 0.8692 1.0625 0.7203 -0.0715 0.0956  0.1595  150 THR B CB  
11213 O OG1 . THR B 146 ? 0.8719 1.1098 0.7260 -0.0645 0.1082  0.1391  150 THR B OG1 
11214 C CG2 . THR B 146 ? 0.8418 1.0248 0.7129 -0.0735 0.0975  0.1582  150 THR B CG2 
11222 N N   . SER B 147 ? 0.9462 1.2303 0.7572 -0.1205 0.1148  0.1777  151 SER B N   
11223 C CA  . SER B 147 ? 1.0051 1.3372 0.8153 -0.1389 0.1283  0.1770  151 SER B CA  
11224 C C   . SER B 147 ? 0.9606 1.3195 0.8001 -0.1247 0.1399  0.1519  151 SER B C   
11225 O O   . SER B 147 ? 1.0336 1.4327 0.8784 -0.1383 0.1508  0.1499  151 SER B O   
11226 C CB  . SER B 147 ? 1.0728 1.4500 0.8585 -0.1502 0.1364  0.1770  151 SER B CB  
11227 O OG  . SER B 147 ? 1.1507 1.5408 0.9391 -0.1279 0.1397  0.1541  151 SER B OG  
11233 N N   . ASN B 148 ? 0.8316 1.1699 0.6904 -0.0984 0.1369  0.1336  152 ASN B N   
11234 C CA  . ASN B 148 ? 0.7383 1.0981 0.6244 -0.0827 0.1455  0.1098  152 ASN B CA  
11235 C C   . ASN B 148 ? 0.7115 1.0259 0.6172 -0.0693 0.1365  0.1086  152 ASN B C   
11236 O O   . ASN B 148 ? 0.7461 1.0397 0.6610 -0.0481 0.1320  0.0959  152 ASN B O   
11237 C CB  . ASN B 148 ? 0.7211 1.1072 0.6099 -0.0634 0.1516  0.0854  152 ASN B CB  
11238 C CG  . ASN B 148 ? 0.7967 1.2382 0.6708 -0.0752 0.1636  0.0805  152 ASN B CG  
11239 O OD1 . ASN B 148 ? 0.8387 1.2842 0.6864 -0.0873 0.1619  0.0928  152 ASN B OD1 
11240 N ND2 . ASN B 148 ? 0.8230 1.3094 0.7143 -0.0713 0.1757  0.0617  152 ASN B ND2 
11247 N N   . PHE B 149 ? 0.6707 0.9710 0.5823 -0.0828 0.1339  0.1215  153 PHE B N   
11248 C CA  . PHE B 149 ? 0.6473 0.9107 0.5776 -0.0722 0.1269  0.1191  153 PHE B CA  
11249 C C   . PHE B 149 ? 0.6793 0.9713 0.6319 -0.0715 0.1352  0.1063  153 PHE B C   
11250 O O   . PHE B 149 ? 0.6660 0.9904 0.6178 -0.0901 0.1422  0.1120  153 PHE B O   
11251 C CB  . PHE B 149 ? 0.6570 0.8770 0.5777 -0.0862 0.1154  0.1420  153 PHE B CB  
11252 C CG  . PHE B 149 ? 0.6743 0.8575 0.6125 -0.0758 0.1085  0.1384  153 PHE B CG  
11253 C CD1 . PHE B 149 ? 0.6635 0.8189 0.6094 -0.0539 0.1028  0.1283  153 PHE B CD1 
11254 C CD2 . PHE B 149 ? 0.6884 0.8663 0.6346 -0.0891 0.1077  0.1450  153 PHE B CD2 
11255 C CE1 . PHE B 149 ? 0.6531 0.7779 0.6136 -0.0452 0.0973  0.1246  153 PHE B CE1 
11256 C CE2 . PHE B 149 ? 0.6839 0.8291 0.6445 -0.0799 0.1014  0.1407  153 PHE B CE2 
11257 C CZ  . PHE B 149 ? 0.6599 0.7794 0.6272 -0.0578 0.0966  0.1303  153 PHE B CZ  
11267 N N   . ARG B 150 ? 0.7320 1.0134 0.7045 -0.0508 0.1339  0.0896  154 ARG B N   
11268 C CA  . ARG B 150 ? 0.7256 1.0263 0.7210 -0.0475 0.1385  0.0779  154 ARG B CA  
11269 C C   . ARG B 150 ? 0.7118 0.9692 0.7187 -0.0376 0.1294  0.0777  154 ARG B C   
11270 O O   . ARG B 150 ? 0.6751 0.8970 0.6773 -0.0259 0.1219  0.0784  154 ARG B O   
11271 C CB  . ARG B 150 ? 0.7225 1.0610 0.7319 -0.0303 0.1464  0.0542  154 ARG B CB  
11272 C CG  . ARG B 150 ? 0.7273 1.1155 0.7273 -0.0379 0.1571  0.0496  154 ARG B CG  
11273 C CD  . ARG B 150 ? 0.7439 1.1695 0.7631 -0.0197 0.1641  0.0236  154 ARG B CD  
11274 N NE  . ARG B 150 ? 0.8315 1.2281 0.8578 0.0044  0.1570  0.0102  154 ARG B NE  
11275 C CZ  . ARG B 150 ? 0.9317 1.3395 0.9789 0.0235  0.1572  -0.0103 154 ARG B CZ  
11276 N NH1 . ARG B 150 ? 1.0370 1.4862 1.1021 0.0235  0.1643  -0.0212 154 ARG B NH1 
11277 N NH2 . ARG B 150 ? 0.9601 1.3377 1.0108 0.0424  0.1496  -0.0195 154 ARG B NH2 
11291 N N   . LEU B 151 ? 0.6943 0.9571 0.7166 -0.0426 0.1300  0.0763  155 LEU B N   
11292 C CA  . LEU B 151 ? 0.6987 0.9238 0.7310 -0.0342 0.1218  0.0751  155 LEU B CA  
11293 C C   . LEU B 151 ? 0.6735 0.9204 0.7276 -0.0306 0.1247  0.0633  155 LEU B C   
11294 O O   . LEU B 151 ? 0.7027 0.9882 0.7638 -0.0419 0.1315  0.0624  155 LEU B O   
11295 C CB  . LEU B 151 ? 0.7164 0.9038 0.7375 -0.0495 0.1137  0.0939  155 LEU B CB  
11296 C CG  . LEU B 151 ? 0.7587 0.9552 0.7830 -0.0708 0.1142  0.1036  155 LEU B CG  
11297 C CD1 . LEU B 151 ? 0.7791 0.9292 0.7913 -0.0824 0.1036  0.1206  155 LEU B CD1 
11298 C CD2 . LEU B 151 ? 0.8132 1.0561 0.8324 -0.0880 0.1235  0.1085  155 LEU B CD2 
11310 N N   . GLY B 152 ? 0.6224 0.8456 0.6874 -0.0151 0.1191  0.0545  156 GLY B N   
11311 C CA  . GLY B 152 ? 0.5913 0.8282 0.6763 -0.0104 0.1190  0.0444  156 GLY B CA  
11312 C C   . GLY B 152 ? 0.5730 0.7696 0.6596 -0.0089 0.1104  0.0481  156 GLY B C   
11313 O O   . GLY B 152 ? 0.5783 0.7385 0.6521 -0.0101 0.1051  0.0569  156 GLY B O   
11317 N N   . PHE B 153 ? 0.5829 0.7882 0.6856 -0.0057 0.1087  0.0405  157 PHE B N   
11318 C CA  . PHE B 153 ? 0.5609 0.7333 0.6647 -0.0069 0.1011  0.0433  157 PHE B CA  
11319 C C   . PHE B 153 ? 0.5636 0.7397 0.6826 0.0076  0.0978  0.0306  157 PHE B C   
11320 O O   . PHE B 153 ? 0.5544 0.7643 0.6881 0.0123  0.1006  0.0215  157 PHE B O   
11321 C CB  . PHE B 153 ? 0.5516 0.7258 0.6552 -0.0279 0.1001  0.0534  157 PHE B CB  
11322 C CG  . PHE B 153 ? 0.5616 0.7018 0.6649 -0.0299 0.0921  0.0551  157 PHE B CG  
11323 C CD1 . PHE B 153 ? 0.5483 0.6957 0.6654 -0.0248 0.0891  0.0463  157 PHE B CD1 
11324 C CD2 . PHE B 153 ? 0.6213 0.7226 0.7102 -0.0364 0.0867  0.0649  157 PHE B CD2 
11325 C CE1 . PHE B 153 ? 0.5778 0.6958 0.6929 -0.0272 0.0820  0.0469  157 PHE B CE1 
11326 C CE2 . PHE B 153 ? 0.6286 0.6999 0.7169 -0.0374 0.0797  0.0641  157 PHE B CE2 
11327 C CZ  . PHE B 153 ? 0.6055 0.6859 0.7061 -0.0334 0.0778  0.0550  157 PHE B CZ  
11337 N N   . GLY B 154 ? 0.5760 0.7176 0.6911 0.0145  0.0914  0.0301  158 GLY B N   
11338 C CA  . GLY B 154 ? 0.5423 0.6817 0.6684 0.0250  0.0865  0.0212  158 GLY B CA  
11339 C C   . GLY B 154 ? 0.5683 0.6724 0.6872 0.0223  0.0804  0.0248  158 GLY B C   
11340 O O   . GLY B 154 ? 0.5649 0.6431 0.6711 0.0181  0.0796  0.0317  158 GLY B O   
11344 N N   . SER B 155 ? 0.5827 0.6866 0.7097 0.0253  0.0755  0.0195  159 SER B N   
11345 C CA  . SER B 155 ? 0.6037 0.6791 0.7241 0.0217  0.0700  0.0211  159 SER B CA  
11346 C C   . SER B 155 ? 0.5539 0.6229 0.6775 0.0336  0.0650  0.0140  159 SER B C   
11347 O O   . SER B 155 ? 0.5154 0.6040 0.6499 0.0418  0.0636  0.0084  159 SER B O   
11348 C CB  . SER B 155 ? 0.5873 0.6687 0.7116 0.0062  0.0679  0.0242  159 SER B CB  
11349 O OG  . SER B 155 ? 0.5703 0.6833 0.7104 0.0067  0.0671  0.0193  159 SER B OG  
11355 N N   . PHE B 156 ? 0.5326 0.5739 0.6462 0.0343  0.0618  0.0143  160 PHE B N   
11356 C CA  . PHE B 156 ? 0.5138 0.5473 0.6270 0.0427  0.0570  0.0094  160 PHE B CA  
11357 C C   . PHE B 156 ? 0.5106 0.5246 0.6157 0.0361  0.0533  0.0091  160 PHE B C   
11358 O O   . PHE B 156 ? 0.4981 0.4972 0.5963 0.0284  0.0544  0.0117  160 PHE B O   
11359 C CB  . PHE B 156 ? 0.4964 0.5188 0.6039 0.0538  0.0582  0.0083  160 PHE B CB  
11360 C CG  . PHE B 156 ? 0.5457 0.5447 0.6416 0.0528  0.0604  0.0108  160 PHE B CG  
11361 C CD1 . PHE B 156 ? 0.5992 0.5806 0.6877 0.0528  0.0579  0.0086  160 PHE B CD1 
11362 C CD2 . PHE B 156 ? 0.5572 0.5533 0.6495 0.0522  0.0645  0.0150  160 PHE B CD2 
11363 C CE1 . PHE B 156 ? 0.5995 0.5620 0.6797 0.0537  0.0597  0.0090  160 PHE B CE1 
11364 C CE2 . PHE B 156 ? 0.5744 0.5491 0.6579 0.0528  0.0650  0.0170  160 PHE B CE2 
11365 C CZ  . PHE B 156 ? 0.5838 0.5422 0.6623 0.0543  0.0627  0.0133  160 PHE B CZ  
11375 N N   . VAL B 157 ? 0.5198 0.5330 0.6249 0.0393  0.0480  0.0055  161 VAL B N   
11376 C CA  . VAL B 157 ? 0.5038 0.4999 0.5990 0.0344  0.0447  0.0034  161 VAL B CA  
11377 C C   . VAL B 157 ? 0.4986 0.4882 0.5879 0.0419  0.0420  0.0012  161 VAL B C   
11378 O O   . VAL B 157 ? 0.4988 0.4736 0.5789 0.0451  0.0448  0.0002  161 VAL B O   
11379 C CB  . VAL B 157 ? 0.5281 0.5331 0.6277 0.0245  0.0396  0.0025  161 VAL B CB  
11380 C CG1 . VAL B 157 ? 0.5234 0.5105 0.6107 0.0195  0.0362  -0.0012 161 VAL B CG1 
11381 C CG2 . VAL B 157 ? 0.5811 0.5939 0.6865 0.0146  0.0422  0.0059  161 VAL B CG2 
11391 N N   . GLU B 158 ? 0.4922 0.4934 0.5871 0.0444  0.0358  0.0009  162 GLU B N   
11392 C CA  . GLU B 158 ? 0.5298 0.5236 0.6169 0.0479  0.0313  0.0005  162 GLU B CA  
11393 C C   . GLU B 158 ? 0.5879 0.5947 0.6843 0.0522  0.0229  0.0016  162 GLU B C   
11394 O O   . GLU B 158 ? 0.6055 0.6283 0.7139 0.0511  0.0200  0.0010  162 GLU B O   
11395 C CB  . GLU B 158 ? 0.5919 0.5750 0.6663 0.0400  0.0297  -0.0019 162 GLU B CB  
11396 C CG  . GLU B 158 ? 0.6148 0.5917 0.6779 0.0410  0.0263  -0.0015 162 GLU B CG  
11397 C CD  . GLU B 158 ? 0.5558 0.5246 0.6140 0.0468  0.0320  -0.0012 162 GLU B CD  
11398 O OE1 . GLU B 158 ? 0.5326 0.5045 0.5965 0.0534  0.0305  0.0020  162 GLU B OE1 
11399 O OE2 . GLU B 158 ? 0.5430 0.5028 0.5925 0.0451  0.0374  -0.0049 162 GLU B OE2 
11406 N N   . LYS B 159 ? 0.5860 0.5859 0.6771 0.0571  0.0184  0.0034  163 LYS B N   
11407 C CA  . LYS B 159 ? 0.5740 0.5804 0.6714 0.0610  0.0074  0.0052  163 LYS B CA  
11408 C C   . LYS B 159 ? 0.5522 0.5637 0.6478 0.0528  0.0009  0.0054  163 LYS B C   
11409 O O   . LYS B 159 ? 0.5400 0.5415 0.6204 0.0451  0.0009  0.0059  163 LYS B O   
11410 C CB  . LYS B 159 ? 0.5996 0.5929 0.6874 0.0638  0.0023  0.0089  163 LYS B CB  
11411 C CG  . LYS B 159 ? 0.6430 0.6320 0.7343 0.0724  0.0054  0.0087  163 LYS B CG  
11412 C CD  . LYS B 159 ? 0.6558 0.6315 0.7376 0.0726  -0.0014 0.0135  163 LYS B CD  
11413 C CE  . LYS B 159 ? 0.6456 0.6158 0.7303 0.0800  0.0008  0.0129  163 LYS B CE  
11414 N NZ  . LYS B 159 ? 0.6921 0.6708 0.7929 0.0907  -0.0028 0.0087  163 LYS B NZ  
11428 N N   . PRO B 160 ? 0.5171 0.5456 0.6276 0.0542  -0.0048 0.0044  164 PRO B N   
11429 C CA  . PRO B 160 ? 0.5546 0.5897 0.6641 0.0454  -0.0114 0.0044  164 PRO B CA  
11430 C C   . PRO B 160 ? 0.6023 0.6323 0.7047 0.0454  -0.0244 0.0086  164 PRO B C   
11431 O O   . PRO B 160 ? 0.6341 0.6763 0.7478 0.0481  -0.0354 0.0096  164 PRO B O   
11432 C CB  . PRO B 160 ? 0.5145 0.5737 0.6454 0.0476  -0.0121 0.0017  164 PRO B CB  
11433 C CG  . PRO B 160 ? 0.4552 0.5206 0.5983 0.0613  -0.0129 0.0006  164 PRO B CG  
11434 C CD  . PRO B 160 ? 0.4642 0.5098 0.5941 0.0639  -0.0055 0.0019  164 PRO B CD  
11442 N N   . VAL B 161 ? 0.6116 0.6245 0.6951 0.0420  -0.0237 0.0115  165 VAL B N   
11443 C CA  . VAL B 161 ? 0.5819 0.5883 0.6541 0.0392  -0.0357 0.0173  165 VAL B CA  
11444 C C   . VAL B 161 ? 0.5509 0.5473 0.6001 0.0281  -0.0312 0.0172  165 VAL B C   
11445 O O   . VAL B 161 ? 0.5490 0.5397 0.5918 0.0264  -0.0191 0.0127  165 VAL B O   
11446 C CB  . VAL B 161 ? 0.5744 0.5715 0.6477 0.0477  -0.0418 0.0226  165 VAL B CB  
11447 C CG1 . VAL B 161 ? 0.5843 0.5921 0.6806 0.0602  -0.0482 0.0207  165 VAL B CG1 
11448 C CG2 . VAL B 161 ? 0.5078 0.4941 0.5733 0.0489  -0.0301 0.0217  165 VAL B CG2 
11458 N N   . SER B 162 ? 0.5795 0.5749 0.6162 0.0209  -0.0416 0.0215  166 SER B N   
11459 C CA  . SER B 162 ? 0.5927 0.5810 0.6058 0.0107  -0.0378 0.0212  166 SER B CA  
11460 C C   . SER B 162 ? 0.5834 0.5621 0.5881 0.0129  -0.0326 0.0249  166 SER B C   
11461 O O   . SER B 162 ? 0.5964 0.5707 0.6082 0.0194  -0.0391 0.0313  166 SER B O   
11462 C CB  . SER B 162 ? 0.6033 0.5938 0.6032 0.0019  -0.0512 0.0267  166 SER B CB  
11463 O OG  . SER B 162 ? 0.6607 0.6495 0.6380 -0.0091 -0.0458 0.0230  166 SER B OG  
11469 N N   . PRO B 163 ? 0.5468 0.5226 0.5370 0.0076  -0.0216 0.0202  167 PRO B N   
11470 C CA  . PRO B 163 ? 0.5304 0.5086 0.5097 0.0004  -0.0145 0.0111  167 PRO B CA  
11471 C C   . PRO B 163 ? 0.5506 0.5263 0.5397 0.0053  -0.0026 0.0016  167 PRO B C   
11472 O O   . PRO B 163 ? 0.5870 0.5606 0.5661 0.0011  0.0043  -0.0070 167 PRO B O   
11473 C CB  . PRO B 163 ? 0.5459 0.5234 0.5044 -0.0066 -0.0101 0.0116  167 PRO B CB  
11474 C CG  . PRO B 163 ? 0.5216 0.4948 0.4868 0.0001  -0.0068 0.0169  167 PRO B CG  
11475 C CD  . PRO B 163 ? 0.5327 0.5031 0.5149 0.0078  -0.0172 0.0241  167 PRO B CD  
11483 N N   . PHE B 164 ? 0.5444 0.5202 0.5521 0.0139  -0.0009 0.0030  168 PHE B N   
11484 C CA  . PHE B 164 ? 0.5455 0.5179 0.5613 0.0175  0.0090  -0.0036 168 PHE B CA  
11485 C C   . PHE B 164 ? 0.5357 0.5115 0.5588 0.0132  0.0068  -0.0074 168 PHE B C   
11486 O O   . PHE B 164 ? 0.5606 0.5307 0.5870 0.0131  0.0136  -0.0125 168 PHE B O   
11487 C CB  . PHE B 164 ? 0.5569 0.5292 0.5868 0.0274  0.0125  -0.0002 168 PHE B CB  
11488 C CG  . PHE B 164 ? 0.5736 0.5424 0.5981 0.0308  0.0132  0.0042  168 PHE B CG  
11489 C CD1 . PHE B 164 ? 0.6143 0.5797 0.6248 0.0273  0.0190  0.0015  168 PHE B CD1 
11490 C CD2 . PHE B 164 ? 0.5981 0.5680 0.6319 0.0373  0.0074  0.0102  168 PHE B CD2 
11491 C CE1 . PHE B 164 ? 0.6389 0.6032 0.6448 0.0284  0.0194  0.0063  168 PHE B CE1 
11492 C CE2 . PHE B 164 ? 0.6373 0.6022 0.6657 0.0388  0.0068  0.0147  168 PHE B CE2 
11493 C CZ  . PHE B 164 ? 0.6416 0.6041 0.6559 0.0335  0.0129  0.0135  168 PHE B CZ  
11503 N N   . VAL B 165 ? 0.5357 0.5204 0.5618 0.0091  -0.0034 -0.0044 169 VAL B N   
11504 C CA  . VAL B 165 ? 0.5432 0.5338 0.5761 0.0028  -0.0067 -0.0077 169 VAL B CA  
11505 C C   . VAL B 165 ? 0.5737 0.5681 0.5948 -0.0061 -0.0165 -0.0078 169 VAL B C   
11506 O O   . VAL B 165 ? 0.5821 0.5784 0.5956 -0.0058 -0.0237 -0.0022 169 VAL B O   
11507 C CB  . VAL B 165 ? 0.5028 0.5075 0.5580 0.0076  -0.0098 -0.0039 169 VAL B CB  
11508 C CG1 . VAL B 165 ? 0.4656 0.4680 0.5304 0.0156  -0.0003 -0.0035 169 VAL B CG1 
11509 C CG2 . VAL B 165 ? 0.4690 0.4836 0.5302 0.0122  -0.0213 0.0022  169 VAL B CG2 
11519 N N   . LYS B 166 ? 0.6203 0.6146 0.6389 -0.0148 -0.0178 -0.0139 170 LYS B N   
11520 C CA  . LYS B 166 ? 0.6666 0.6678 0.6770 -0.0237 -0.0288 -0.0139 170 LYS B CA  
11521 C C   . LYS B 166 ? 0.7215 0.7391 0.7494 -0.0206 -0.0398 -0.0062 170 LYS B C   
11522 O O   . LYS B 166 ? 0.7310 0.7578 0.7796 -0.0154 -0.0379 -0.0049 170 LYS B O   
11523 C CB  . LYS B 166 ? 0.6651 0.6623 0.6713 -0.0340 -0.0284 -0.0227 170 LYS B CB  
11524 C CG  . LYS B 166 ? 0.6738 0.6540 0.6627 -0.0361 -0.0196 -0.0329 170 LYS B CG  
11525 C CD  . LYS B 166 ? 0.7573 0.7371 0.7232 -0.0397 -0.0215 -0.0355 170 LYS B CD  
11526 C CE  . LYS B 166 ? 0.8632 0.8303 0.8128 -0.0427 -0.0141 -0.0494 170 LYS B CE  
11527 N NZ  . LYS B 166 ? 0.9669 0.9287 0.9144 -0.0521 -0.0191 -0.0582 170 LYS B NZ  
11541 N N   . THR B 167 ? 0.7387 0.7613 0.7583 -0.0236 -0.0518 -0.0014 171 THR B N   
11542 C CA  . THR B 167 ? 0.6666 0.7036 0.7030 -0.0184 -0.0645 0.0058  171 THR B CA  
11543 C C   . THR B 167 ? 0.6621 0.7111 0.6982 -0.0275 -0.0774 0.0057  171 THR B C   
11544 O O   . THR B 167 ? 0.6422 0.7010 0.6858 -0.0242 -0.0913 0.0123  171 THR B O   
11545 C CB  . THR B 167 ? 0.6352 0.6660 0.6653 -0.0115 -0.0708 0.0146  171 THR B CB  
11546 O OG1 . THR B 167 ? 0.6809 0.7017 0.6835 -0.0204 -0.0718 0.0158  171 THR B OG1 
11547 C CG2 . THR B 167 ? 0.6135 0.6372 0.6518 -0.0007 -0.0606 0.0151  171 THR B CG2 
11555 N N   . THR B 168 ? 0.6813 0.7288 0.7093 -0.0387 -0.0743 -0.0020 172 THR B N   
11556 C CA  . THR B 168 ? 0.6633 0.7250 0.6959 -0.0476 -0.0863 -0.0029 172 THR B CA  
11557 C C   . THR B 168 ? 0.6510 0.7315 0.7135 -0.0448 -0.0864 -0.0032 172 THR B C   
11558 O O   . THR B 168 ? 0.6215 0.6999 0.6948 -0.0407 -0.0744 -0.0055 172 THR B O   
11559 C CB  . THR B 168 ? 0.7352 0.7877 0.7480 -0.0614 -0.0840 -0.0120 172 THR B CB  
11560 O OG1 . THR B 168 ? 0.7541 0.7979 0.7726 -0.0629 -0.0715 -0.0193 172 THR B OG1 
11561 C CG2 . THR B 168 ? 0.7962 0.8346 0.7792 -0.0643 -0.0819 -0.0136 172 THR B CG2 
11569 N N   . PRO B 169 ? 0.6986 0.7998 0.7752 -0.0473 -0.0998 -0.0009 173 PRO B N   
11570 C CA  . PRO B 169 ? 0.6458 0.7709 0.7530 -0.0447 -0.0992 -0.0016 173 PRO B CA  
11571 C C   . PRO B 169 ? 0.6726 0.7948 0.7826 -0.0541 -0.0870 -0.0076 173 PRO B C   
11572 O O   . PRO B 169 ? 0.6658 0.7989 0.7947 -0.0495 -0.0787 -0.0074 173 PRO B O   
11573 C CB  . PRO B 169 ? 0.6175 0.7643 0.7342 -0.0499 -0.1165 0.0002  173 PRO B CB  
11574 C CG  . PRO B 169 ? 0.6323 0.7665 0.7271 -0.0492 -0.1277 0.0053  173 PRO B CG  
11575 C CD  . PRO B 169 ? 0.6909 0.7972 0.7564 -0.0537 -0.1160 0.0022  173 PRO B CD  
11583 N N   . GLU B 170 ? 0.7531 0.8599 0.8435 -0.0676 -0.0862 -0.0130 174 GLU B N   
11584 C CA  . GLU B 170 ? 0.8660 0.9660 0.9582 -0.0779 -0.0775 -0.0181 174 GLU B CA  
11585 C C   . GLU B 170 ? 0.8399 0.9228 0.9299 -0.0702 -0.0626 -0.0183 174 GLU B C   
11586 O O   . GLU B 170 ? 0.8437 0.9323 0.9480 -0.0723 -0.0554 -0.0174 174 GLU B O   
11587 C CB  . GLU B 170 ? 1.0026 1.0852 1.0722 -0.0921 -0.0812 -0.0256 174 GLU B CB  
11588 C CG  . GLU B 170 ? 1.1566 1.2563 1.2275 -0.1024 -0.0967 -0.0260 174 GLU B CG  
11589 C CD  . GLU B 170 ? 1.3032 1.4061 1.3619 -0.0966 -0.1070 -0.0221 174 GLU B CD  
11590 O OE1 . GLU B 170 ? 1.3581 1.4493 1.4070 -0.0855 -0.1018 -0.0189 174 GLU B OE1 
11591 O OE2 . GLU B 170 ? 1.3827 1.4996 1.4412 -0.1041 -0.1210 -0.0214 174 GLU B OE2 
11598 N N   . GLU B 171 ? 0.8175 0.8809 0.8895 -0.0622 -0.0579 -0.0188 175 GLU B N   
11599 C CA  . GLU B 171 ? 0.7531 0.8002 0.8224 -0.0548 -0.0447 -0.0193 175 GLU B CA  
11600 C C   . GLU B 171 ? 0.6566 0.7180 0.7451 -0.0420 -0.0407 -0.0131 175 GLU B C   
11601 O O   . GLU B 171 ? 0.6365 0.6915 0.7292 -0.0381 -0.0303 -0.0127 175 GLU B O   
11602 C CB  . GLU B 171 ? 0.8134 0.8391 0.8586 -0.0510 -0.0409 -0.0227 175 GLU B CB  
11603 C CG  . GLU B 171 ? 0.9108 0.9217 0.9352 -0.0621 -0.0430 -0.0319 175 GLU B CG  
11604 C CD  . GLU B 171 ? 1.0312 1.0203 1.0500 -0.0644 -0.0338 -0.0393 175 GLU B CD  
11605 O OE1 . GLU B 171 ? 1.0683 1.0554 1.1001 -0.0600 -0.0267 -0.0358 175 GLU B OE1 
11606 O OE2 . GLU B 171 ? 1.0947 1.0686 1.0957 -0.0705 -0.0343 -0.0491 175 GLU B OE2 
11613 N N   . ILE B 172 ? 0.6447 0.7245 0.7445 -0.0351 -0.0497 -0.0087 176 ILE B N   
11614 C CA  . ILE B 172 ? 0.6433 0.7386 0.7635 -0.0224 -0.0470 -0.0051 176 ILE B CA  
11615 C C   . ILE B 172 ? 0.6332 0.7498 0.7744 -0.0273 -0.0427 -0.0060 176 ILE B C   
11616 O O   . ILE B 172 ? 0.6411 0.7614 0.7912 -0.0219 -0.0330 -0.0054 176 ILE B O   
11617 C CB  . ILE B 172 ? 0.6559 0.7642 0.7844 -0.0131 -0.0599 -0.0012 176 ILE B CB  
11618 C CG1 . ILE B 172 ? 0.7159 0.8025 0.8226 -0.0090 -0.0631 0.0020  176 ILE B CG1 
11619 C CG2 . ILE B 172 ? 0.6340 0.7618 0.7872 0.0004  -0.0583 -0.0004 176 ILE B CG2 
11620 C CD1 . ILE B 172 ? 0.7553 0.8490 0.8667 -0.0015 -0.0784 0.0077  176 ILE B CD1 
11632 N N   . ALA B 173 ? 0.5825 0.7151 0.7314 -0.0389 -0.0500 -0.0073 177 ALA B N   
11633 C CA  . ALA B 173 ? 0.5727 0.7294 0.7419 -0.0464 -0.0464 -0.0074 177 ALA B CA  
11634 C C   . ALA B 173 ? 0.6174 0.7557 0.7771 -0.0564 -0.0352 -0.0077 177 ALA B C   
11635 O O   . ALA B 173 ? 0.6308 0.7839 0.8041 -0.0585 -0.0276 -0.0057 177 ALA B O   
11636 C CB  . ALA B 173 ? 0.5689 0.7464 0.7475 -0.0584 -0.0578 -0.0084 177 ALA B CB  
11642 N N   . ASN B 174 ? 0.6375 0.7442 0.7740 -0.0624 -0.0345 -0.0104 178 ASN B N   
11643 C CA  . ASN B 174 ? 0.6068 0.6912 0.7336 -0.0714 -0.0266 -0.0113 178 ASN B CA  
11644 C C   . ASN B 174 ? 0.6165 0.6670 0.7191 -0.0668 -0.0242 -0.0157 178 ASN B C   
11645 O O   . ASN B 174 ? 0.6591 0.6946 0.7468 -0.0745 -0.0296 -0.0213 178 ASN B O   
11646 C CB  . ASN B 174 ? 0.6170 0.7047 0.7465 -0.0908 -0.0318 -0.0124 178 ASN B CB  
11647 C CG  . ASN B 174 ? 0.6864 0.7456 0.8045 -0.1006 -0.0264 -0.0129 178 ASN B CG  
11648 O OD1 . ASN B 174 ? 0.7097 0.7478 0.8185 -0.0921 -0.0186 -0.0125 178 ASN B OD1 
11649 N ND2 . ASN B 174 ? 0.7510 0.8088 0.8702 -0.1188 -0.0317 -0.0134 178 ASN B ND2 
11656 N N   . PRO B 175 ? 0.5819 0.6216 0.6804 -0.0541 -0.0159 -0.0142 179 PRO B N   
11657 C CA  . PRO B 175 ? 0.5739 0.5872 0.6515 -0.0485 -0.0133 -0.0189 179 PRO B CA  
11658 C C   . PRO B 175 ? 0.6554 0.6423 0.7188 -0.0574 -0.0118 -0.0253 179 PRO B C   
11659 O O   . PRO B 175 ? 0.6814 0.6499 0.7279 -0.0534 -0.0102 -0.0317 179 PRO B O   
11660 C CB  . PRO B 175 ? 0.5047 0.5155 0.5853 -0.0349 -0.0045 -0.0152 179 PRO B CB  
11661 C CG  . PRO B 175 ? 0.4783 0.5068 0.5774 -0.0359 -0.0009 -0.0100 179 PRO B CG  
11662 C CD  . PRO B 175 ? 0.5491 0.6026 0.6618 -0.0444 -0.0088 -0.0091 179 PRO B CD  
11670 N N   . CYS B 176 ? 0.6981 0.6826 0.7678 -0.0693 -0.0127 -0.0243 180 CYS B N   
11671 C CA  . CYS B 176 ? 0.7801 0.7364 0.8371 -0.0783 -0.0141 -0.0308 180 CYS B CA  
11672 C C   . CYS B 176 ? 0.8258 0.7853 0.8816 -0.0942 -0.0240 -0.0347 180 CYS B C   
11673 O O   . CYS B 176 ? 0.8499 0.7884 0.8997 -0.1052 -0.0270 -0.0387 180 CYS B O   
11674 C CB  . CYS B 176 ? 0.7766 0.7201 0.8387 -0.0813 -0.0088 -0.0256 180 CYS B CB  
11675 S SG  . CYS B 176 ? 0.8214 0.7667 0.8877 -0.0644 0.0021  -0.0194 180 CYS B SG  
11680 N N   . SER B 177 ? 0.8109 0.7955 0.8725 -0.0956 -0.0306 -0.0336 181 SER B N   
11681 C CA  . SER B 177 ? 0.8371 0.8285 0.8992 -0.1111 -0.0409 -0.0368 181 SER B CA  
11682 C C   . SER B 177 ? 0.8847 0.8477 0.9245 -0.1168 -0.0451 -0.0487 181 SER B C   
11683 O O   . SER B 177 ? 0.9246 0.8803 0.9622 -0.1320 -0.0524 -0.0528 181 SER B O   
11684 C CB  . SER B 177 ? 0.8357 0.8583 0.9069 -0.1090 -0.0484 -0.0337 181 SER B CB  
11685 O OG  . SER B 177 ? 0.8625 0.8802 0.9193 -0.0980 -0.0489 -0.0364 181 SER B OG  
11691 N N   . SER B 178 ? 0.9137 0.8617 0.9371 -0.1053 -0.0405 -0.0550 182 SER B N   
11692 C CA  . SER B 178 ? 0.9705 0.8950 0.9725 -0.1088 -0.0434 -0.0687 182 SER B CA  
11693 C C   . SER B 178 ? 1.0187 0.9111 1.0165 -0.1122 -0.0413 -0.0750 182 SER B C   
11694 O O   . SER B 178 ? 1.0652 0.9370 1.0484 -0.1183 -0.0462 -0.0878 182 SER B O   
11695 C CB  . SER B 178 ? 0.9897 0.9123 0.9763 -0.0957 -0.0380 -0.0737 182 SER B CB  
11696 O OG  . SER B 178 ? 1.0482 0.9611 1.0381 -0.0829 -0.0275 -0.0711 182 SER B OG  
11702 N N   . ILE B 179 ? 0.9872 0.8742 0.9969 -0.1086 -0.0352 -0.0666 183 ILE B N   
11703 C CA  . ILE B 179 ? 1.0297 0.8826 1.0339 -0.1087 -0.0336 -0.0715 183 ILE B CA  
11704 C C   . ILE B 179 ? 1.0838 0.9186 1.0855 -0.1267 -0.0438 -0.0759 183 ILE B C   
11705 O O   . ILE B 179 ? 1.1882 0.9924 1.1760 -0.1267 -0.0473 -0.0892 183 ILE B O   
11706 C CB  . ILE B 179 ? 1.0422 0.8952 1.0586 -0.1017 -0.0258 -0.0596 183 ILE B CB  
11707 C CG1 . ILE B 179 ? 0.9928 0.8514 1.0060 -0.0827 -0.0165 -0.0603 183 ILE B CG1 
11708 C CG2 . ILE B 179 ? 1.0751 0.8937 1.0888 -0.1065 -0.0279 -0.0605 183 ILE B CG2 
11709 C CD1 . ILE B 179 ? 1.0016 0.8536 1.0221 -0.0736 -0.0089 -0.0522 183 ILE B CD1 
11721 N N   . PRO B 180 ? 1.0293 0.8815 1.0442 -0.1423 -0.0492 -0.0664 184 PRO B N   
11722 C CA  . PRO B 180 ? 0.9947 0.8827 1.0294 -0.1445 -0.0460 -0.0517 184 PRO B CA  
11723 C C   . PRO B 180 ? 0.9252 0.8081 0.9700 -0.1455 -0.0401 -0.0402 184 PRO B C   
11724 O O   . PRO B 180 ? 0.8984 0.7504 0.9375 -0.1530 -0.0429 -0.0408 184 PRO B O   
11725 C CB  . PRO B 180 ? 0.9917 0.8966 1.0334 -0.1638 -0.0564 -0.0508 184 PRO B CB  
11726 C CG  . PRO B 180 ? 1.0322 0.9006 1.0606 -0.1761 -0.0642 -0.0600 184 PRO B CG  
11727 C CD  . PRO B 180 ? 1.0635 0.9029 1.0729 -0.1606 -0.0608 -0.0733 184 PRO B CD  
11735 N N   . TYR B 181 ? 0.8610 0.7735 0.9201 -0.1383 -0.0328 -0.0301 185 TYR B N   
11736 C CA  . TYR B 181 ? 0.8652 0.7792 0.9333 -0.1390 -0.0263 -0.0187 185 TYR B CA  
11737 C C   . TYR B 181 ? 0.7774 0.7350 0.8637 -0.1343 -0.0210 -0.0106 185 TYR B C   
11738 O O   . TYR B 181 ? 0.7347 0.7111 0.8236 -0.1232 -0.0208 -0.0141 185 TYR B O   
11739 C CB  . TYR B 181 ? 0.9013 0.7875 0.9591 -0.1236 -0.0198 -0.0205 185 TYR B CB  
11740 C CG  . TYR B 181 ? 0.8585 0.7348 0.9201 -0.1280 -0.0163 -0.0094 185 TYR B CG  
11741 C CD1 . TYR B 181 ? 0.8030 0.7035 0.8750 -0.1208 -0.0076 0.0002  185 TYR B CD1 
11742 C CD2 . TYR B 181 ? 0.8494 0.6908 0.9032 -0.1398 -0.0226 -0.0085 185 TYR B CD2 
11743 C CE1 . TYR B 181 ? 0.7980 0.6909 0.8713 -0.1260 -0.0046 0.0109  185 TYR B CE1 
11744 C CE2 . TYR B 181 ? 0.8686 0.6997 0.9240 -0.1452 -0.0207 0.0035  185 TYR B CE2 
11745 C CZ  . TYR B 181 ? 0.8600 0.7182 0.9246 -0.1386 -0.0113 0.0134  185 TYR B CZ  
11746 O OH  . TYR B 181 ? 0.9313 0.7808 0.9955 -0.1450 -0.0096 0.0259  185 TYR B OH  
11756 N N   . PHE B 182 ? 0.7730 0.7468 0.8717 -0.1431 -0.0173 0.0000  186 PHE B N   
11757 C CA  . PHE B 182 ? 0.7118 0.7299 0.8295 -0.1385 -0.0123 0.0057  186 PHE B CA  
11758 C C   . PHE B 182 ? 0.6688 0.6876 0.7857 -0.1186 -0.0029 0.0071  186 PHE B C   
11759 O O   . PHE B 182 ? 0.7178 0.7238 0.8310 -0.1180 0.0029  0.0129  186 PHE B O   
11760 C CB  . PHE B 182 ? 0.7015 0.7435 0.8331 -0.1566 -0.0110 0.0154  186 PHE B CB  
11761 C CG  . PHE B 182 ? 0.6885 0.7795 0.8412 -0.1505 -0.0055 0.0185  186 PHE B CG  
11762 C CD1 . PHE B 182 ? 0.7301 0.8539 0.8975 -0.1507 -0.0111 0.0144  186 PHE B CD1 
11763 C CD2 . PHE B 182 ? 0.6870 0.7914 0.8449 -0.1431 0.0045  0.0243  186 PHE B CD2 
11764 C CE1 . PHE B 182 ? 0.7300 0.8987 0.9186 -0.1427 -0.0070 0.0153  186 PHE B CE1 
11765 C CE2 . PHE B 182 ? 0.6913 0.8412 0.8689 -0.1358 0.0095  0.0246  186 PHE B CE2 
11766 C CZ  . PHE B 182 ? 0.7211 0.9029 0.9149 -0.1349 0.0036  0.0196  186 PHE B CZ  
11776 N N   . CYS B 183 ? 0.6307 0.6640 0.7507 -0.1032 -0.0026 0.0026  187 CYS B N   
11777 C CA  . CYS B 183 ? 0.6847 0.7214 0.8054 -0.0848 0.0050  0.0035  187 CYS B CA  
11778 C C   . CYS B 183 ? 0.6881 0.7641 0.8272 -0.0769 0.0052  0.0042  187 CYS B C   
11779 O O   . CYS B 183 ? 0.7297 0.8256 0.8778 -0.0813 -0.0021 0.0020  187 CYS B O   
11780 C CB  . CYS B 183 ? 0.7407 0.7508 0.8450 -0.0719 0.0047  -0.0031 187 CYS B CB  
11781 S SG  . CYS B 183 ? 0.7944 0.7589 0.8793 -0.0745 0.0057  -0.0064 187 CYS B SG  
11786 N N   . LEU B 184 ? 0.6719 0.7586 0.8168 -0.0649 0.0125  0.0067  188 LEU B N   
11787 C CA  . LEU B 184 ? 0.5994 0.7192 0.7612 -0.0536 0.0120  0.0052  188 LEU B CA  
11788 C C   . LEU B 184 ? 0.5858 0.6929 0.7401 -0.0375 0.0086  0.0013  188 LEU B C   
11789 O O   . LEU B 184 ? 0.6129 0.6906 0.7503 -0.0328 0.0111  0.0004  188 LEU B O   
11790 C CB  . LEU B 184 ? 0.5777 0.7179 0.7500 -0.0487 0.0211  0.0085  188 LEU B CB  
11791 C CG  . LEU B 184 ? 0.6178 0.7772 0.7983 -0.0660 0.0251  0.0139  188 LEU B CG  
11792 C CD1 . LEU B 184 ? 0.6023 0.7831 0.7902 -0.0604 0.0349  0.0164  188 LEU B CD1 
11793 C CD2 . LEU B 184 ? 0.6267 0.8187 0.8245 -0.0761 0.0189  0.0123  188 LEU B CD2 
11805 N N   . PRO B 185 ? 0.5697 0.6989 0.7363 -0.0293 0.0022  -0.0008 189 PRO B N   
11806 C CA  . PRO B 185 ? 0.5691 0.6853 0.7275 -0.0160 -0.0024 -0.0027 189 PRO B CA  
11807 C C   . PRO B 185 ? 0.5724 0.6733 0.7236 -0.0041 0.0054  -0.0018 189 PRO B C   
11808 O O   . PRO B 185 ? 0.5952 0.7076 0.7550 -0.0004 0.0128  -0.0007 189 PRO B O   
11809 C CB  . PRO B 185 ? 0.5527 0.6989 0.7307 -0.0082 -0.0107 -0.0039 189 PRO B CB  
11810 C CG  . PRO B 185 ? 0.5356 0.7149 0.7343 -0.0148 -0.0073 -0.0040 189 PRO B CG  
11811 C CD  . PRO B 185 ? 0.5387 0.7057 0.7277 -0.0327 -0.0024 -0.0015 189 PRO B CD  
11819 N N   . THR B 186 ? 0.5832 0.6600 0.7179 0.0010  0.0038  -0.0025 190 THR B N   
11820 C CA  . THR B 186 ? 0.5785 0.6394 0.7050 0.0107  0.0106  -0.0018 190 THR B CA  
11821 C C   . THR B 186 ? 0.5803 0.6582 0.7209 0.0236  0.0113  -0.0015 190 THR B C   
11822 O O   . THR B 186 ? 0.6202 0.7150 0.7729 0.0291  0.0036  -0.0024 190 THR B O   
11823 C CB  . THR B 186 ? 0.5452 0.5845 0.6540 0.0133  0.0076  -0.0027 190 THR B CB  
11824 O OG1 . THR B 186 ? 0.5495 0.5771 0.6464 0.0021  0.0053  -0.0054 190 THR B OG1 
11825 C CG2 . THR B 186 ? 0.5473 0.5693 0.6468 0.0202  0.0155  -0.0024 190 THR B CG2 
11833 N N   . PHE B 187 ? 0.5367 0.6094 0.6757 0.0289  0.0198  -0.0007 191 PHE B N   
11834 C CA  . PHE B 187 ? 0.5037 0.5915 0.6546 0.0409  0.0214  -0.0021 191 PHE B CA  
11835 C C   . PHE B 187 ? 0.5266 0.5954 0.6666 0.0481  0.0271  -0.0012 191 PHE B C   
11836 O O   . PHE B 187 ? 0.5160 0.5662 0.6431 0.0429  0.0322  0.0007  191 PHE B O   
11837 C CB  . PHE B 187 ? 0.4556 0.5708 0.6215 0.0375  0.0270  -0.0029 191 PHE B CB  
11838 C CG  . PHE B 187 ? 0.4836 0.5903 0.6409 0.0277  0.0361  0.0009  191 PHE B CG  
11839 C CD1 . PHE B 187 ? 0.5007 0.6024 0.6538 0.0125  0.0359  0.0037  191 PHE B CD1 
11840 C CD2 . PHE B 187 ? 0.5166 0.6187 0.6696 0.0333  0.0434  0.0020  191 PHE B CD2 
11841 C CE1 . PHE B 187 ? 0.5541 0.6443 0.6989 0.0034  0.0422  0.0083  191 PHE B CE1 
11842 C CE2 . PHE B 187 ? 0.5897 0.6825 0.7343 0.0242  0.0499  0.0068  191 PHE B CE2 
11843 C CZ  . PHE B 187 ? 0.6004 0.6862 0.7409 0.0094  0.0490  0.0103  191 PHE B CZ  
11853 N N   . GLY B 188 ? 0.5295 0.6034 0.6757 0.0604  0.0252  -0.0032 192 GLY B N   
11854 C CA  . GLY B 188 ? 0.5235 0.5810 0.6606 0.0672  0.0289  -0.0026 192 GLY B CA  
11855 C C   . GLY B 188 ? 0.5429 0.6058 0.6807 0.0676  0.0385  -0.0026 192 GLY B C   
11856 O O   . GLY B 188 ? 0.5483 0.5949 0.6745 0.0640  0.0438  0.0002  192 GLY B O   
11860 N N   . PHE B 189 ? 0.5816 0.6683 0.7328 0.0724  0.0403  -0.0061 193 PHE B N   
11861 C CA  . PHE B 189 ? 0.5779 0.6738 0.7289 0.0713  0.0494  -0.0057 193 PHE B CA  
11862 C C   . PHE B 189 ? 0.5675 0.6976 0.7343 0.0701  0.0519  -0.0094 193 PHE B C   
11863 O O   . PHE B 189 ? 0.5155 0.6632 0.6963 0.0799  0.0472  -0.0161 193 PHE B O   
11864 C CB  . PHE B 189 ? 0.5729 0.6608 0.7196 0.0823  0.0508  -0.0082 193 PHE B CB  
11865 C CG  . PHE B 189 ? 0.5708 0.6739 0.7184 0.0825  0.0590  -0.0091 193 PHE B CG  
11866 C CD1 . PHE B 189 ? 0.5823 0.6821 0.7212 0.0715  0.0656  -0.0026 193 PHE B CD1 
11867 C CD2 . PHE B 189 ? 0.5318 0.6520 0.6880 0.0936  0.0592  -0.0168 193 PHE B CD2 
11868 C CE1 . PHE B 189 ? 0.5794 0.6938 0.7168 0.0701  0.0725  -0.0020 193 PHE B CE1 
11869 C CE2 . PHE B 189 ? 0.4808 0.6174 0.6358 0.0929  0.0672  -0.0182 193 PHE B CE2 
11870 C CZ  . PHE B 189 ? 0.5458 0.6801 0.6907 0.0805  0.0739  -0.0099 193 PHE B CZ  
11880 N N   . LYS B 190 ? 0.6228 0.7627 0.7879 0.0579  0.0589  -0.0051 194 LYS B N   
11881 C CA  . LYS B 190 ? 0.6112 0.7877 0.7901 0.0536  0.0634  -0.0075 194 LYS B CA  
11882 C C   . LYS B 190 ? 0.5531 0.7381 0.7259 0.0521  0.0726  -0.0059 194 LYS B C   
11883 O O   . LYS B 190 ? 0.5384 0.7074 0.6975 0.0414  0.0764  0.0026  194 LYS B O   
11884 C CB  . LYS B 190 ? 0.6323 0.8158 0.8136 0.0368  0.0630  -0.0022 194 LYS B CB  
11885 C CG  . LYS B 190 ? 0.6525 0.8414 0.8443 0.0374  0.0541  -0.0053 194 LYS B CG  
11886 C CD  . LYS B 190 ? 0.7356 0.9267 0.9268 0.0189  0.0534  0.0003  194 LYS B CD  
11887 C CE  . LYS B 190 ? 0.8572 1.0586 1.0599 0.0186  0.0440  -0.0030 194 LYS B CE  
11888 N NZ  . LYS B 190 ? 0.9426 1.1404 1.1420 -0.0001 0.0421  0.0020  194 LYS B NZ  
11902 N N   . HIS B 191 ? 0.5068 0.7161 0.6891 0.0632  0.0752  -0.0144 195 HIS B N   
11903 C CA  . HIS B 191 ? 0.5219 0.7485 0.6995 0.0607  0.0844  -0.0142 195 HIS B CA  
11904 C C   . HIS B 191 ? 0.5426 0.8073 0.7305 0.0479  0.0903  -0.0131 195 HIS B C   
11905 O O   . HIS B 191 ? 0.5616 0.8598 0.7685 0.0538  0.0900  -0.0225 195 HIS B O   
11906 C CB  . HIS B 191 ? 0.5223 0.7590 0.7048 0.0781  0.0846  -0.0256 195 HIS B CB  
11907 C CG  . HIS B 191 ? 0.5507 0.8136 0.7301 0.0758  0.0942  -0.0279 195 HIS B CG  
11908 N ND1 . HIS B 191 ? 0.5481 0.8085 0.7126 0.0603  0.1009  -0.0166 195 HIS B ND1 
11909 C CD2 . HIS B 191 ? 0.5439 0.8360 0.7319 0.0869  0.0979  -0.0405 195 HIS B CD2 
11910 C CE1 . HIS B 191 ? 0.5585 0.8466 0.7214 0.0606  0.1086  -0.0210 195 HIS B CE1 
11911 N NE2 . HIS B 191 ? 0.5514 0.8604 0.7286 0.0770  0.1075  -0.0365 195 HIS B NE2 
11919 N N   . ILE B 192 ? 0.5573 0.8178 0.7335 0.0301  0.0951  -0.0017 196 ILE B N   
11920 C CA  . ILE B 192 ? 0.5563 0.8473 0.7400 0.0129  0.0994  0.0027  196 ILE B CA  
11921 C C   . ILE B 192 ? 0.5461 0.8707 0.7275 0.0062  0.1097  0.0034  196 ILE B C   
11922 O O   . ILE B 192 ? 0.5638 0.9337 0.7608 0.0039  0.1148  -0.0030 196 ILE B O   
11923 C CB  . ILE B 192 ? 0.5849 0.8464 0.7570 -0.0051 0.0958  0.0159  196 ILE B CB  
11924 C CG1 . ILE B 192 ? 0.5765 0.8103 0.7508 0.0015  0.0862  0.0133  196 ILE B CG1 
11925 C CG2 . ILE B 192 ? 0.6101 0.9018 0.7891 -0.0257 0.0994  0.0219  196 ILE B CG2 
11926 C CD1 . ILE B 192 ? 0.6329 0.8334 0.7949 -0.0129 0.0817  0.0230  196 ILE B CD1 
11938 N N   . LEU B 193 ? 0.5469 0.8521 0.7088 0.0028  0.1128  0.0110  197 LEU B N   
11939 C CA  . LEU B 193 ? 0.5278 0.8625 0.6829 -0.0065 0.1223  0.0141  197 LEU B CA  
11940 C C   . LEU B 193 ? 0.4865 0.8155 0.6322 0.0085  0.1245  0.0076  197 LEU B C   
11941 O O   . LEU B 193 ? 0.5323 0.8225 0.6617 0.0105  0.1206  0.0147  197 LEU B O   
11942 C CB  . LEU B 193 ? 0.5519 0.8700 0.6898 -0.0299 0.1228  0.0327  197 LEU B CB  
11943 C CG  . LEU B 193 ? 0.5518 0.8931 0.6764 -0.0422 0.1312  0.0399  197 LEU B CG  
11944 C CD1 . LEU B 193 ? 0.4956 0.8978 0.6353 -0.0474 0.1407  0.0318  197 LEU B CD1 
11945 C CD2 . LEU B 193 ? 0.5823 0.8973 0.6888 -0.0649 0.1283  0.0602  197 LEU B CD2 
11957 N N   . PRO B 194 ? 0.4672 0.8337 0.6227 0.0195  0.1302  -0.0064 198 PRO B N   
11958 C CA  . PRO B 194 ? 0.4895 0.8520 0.6337 0.0309  0.1325  -0.0123 198 PRO B CA  
11959 C C   . PRO B 194 ? 0.5228 0.8842 0.6449 0.0142  0.1379  0.0017  198 PRO B C   
11960 O O   . PRO B 194 ? 0.5600 0.9348 0.6778 -0.0064 0.1416  0.0139  198 PRO B O   
11961 C CB  . PRO B 194 ? 0.4805 0.8894 0.6419 0.0442  0.1378  -0.0316 198 PRO B CB  
11962 C CG  . PRO B 194 ? 0.4500 0.8790 0.6347 0.0449  0.1353  -0.0369 198 PRO B CG  
11963 C CD  . PRO B 194 ? 0.4271 0.8427 0.6055 0.0228  0.1344  -0.0190 198 PRO B CD  
11971 N N   . LEU B 195 ? 0.5317 0.8762 0.6393 0.0225  0.1372  0.0007  199 LEU B N   
11972 C CA  . LEU B 195 ? 0.5324 0.8718 0.6174 0.0082  0.1402  0.0146  199 LEU B CA  
11973 C C   . LEU B 195 ? 0.5413 0.9302 0.6244 -0.0073 0.1508  0.0161  199 LEU B C   
11974 O O   . LEU B 195 ? 0.4990 0.9303 0.5940 0.0010  0.1577  -0.0001 199 LEU B O   
11975 C CB  . LEU B 195 ? 0.5460 0.8699 0.6190 0.0219  0.1383  0.0091  199 LEU B CB  
11976 C CG  . LEU B 195 ? 0.5789 0.8547 0.6511 0.0342  0.1283  0.0100  199 LEU B CG  
11977 C CD1 . LEU B 195 ? 0.6099 0.8802 0.6775 0.0505  0.1265  -0.0011 199 LEU B CD1 
11978 C CD2 . LEU B 195 ? 0.5604 0.8003 0.6175 0.0215  0.1232  0.0292  199 LEU B CD2 
11990 N N   . THR B 196 ? 0.5869 0.9706 0.6551 -0.0302 0.1515  0.0355  200 THR B N   
11991 C CA  . THR B 196 ? 0.6357 1.0657 0.6988 -0.0494 0.1614  0.0405  200 THR B CA  
11992 C C   . THR B 196 ? 0.7388 1.1468 0.7762 -0.0714 0.1588  0.0643  200 THR B C   
11993 O O   . THR B 196 ? 0.7607 1.1189 0.7896 -0.0734 0.1487  0.0770  200 THR B O   
11994 C CB  . THR B 196 ? 0.6471 1.1092 0.7303 -0.0597 0.1652  0.0387  200 THR B CB  
11995 O OG1 . THR B 196 ? 0.6433 1.1498 0.7193 -0.0824 0.1749  0.0466  200 THR B OG1 
11996 C CG2 . THR B 196 ? 0.6755 1.0960 0.7608 -0.0686 0.1555  0.0518  200 THR B CG2 
12004 N N   . ASN B 197 ? 0.8347 1.2817 0.8597 -0.0878 0.1675  0.0698  201 ASN B N   
12005 C CA  . ASN B 197 ? 0.8984 1.3303 0.8983 -0.1122 0.1647  0.0943  201 ASN B CA  
12006 C C   . ASN B 197 ? 0.8924 1.3248 0.8949 -0.1373 0.1632  0.1105  201 ASN B C   
12007 O O   . ASN B 197 ? 0.8988 1.3038 0.8817 -0.1573 0.1566  0.1329  201 ASN B O   
12008 C CB  . ASN B 197 ? 0.9721 1.4472 0.9548 -0.1215 0.1746  0.0944  201 ASN B CB  
12009 C CG  . ASN B 197 ? 1.0513 1.5947 1.0500 -0.1245 0.1888  0.0791  201 ASN B CG  
12010 O OD1 . ASN B 197 ? 1.0844 1.6570 1.0944 -0.1041 0.1952  0.0559  201 ASN B OD1 
12011 N ND2 . ASN B 197 ? 1.0749 1.6442 1.0758 -0.1497 0.1930  0.0913  201 ASN B ND2 
12018 N N   . ASP B 198 ? 0.8256 1.2874 0.8520 -0.1371 0.1678  0.0999  202 ASP B N   
12019 C CA  . ASP B 198 ? 0.7762 1.2428 0.8073 -0.1618 0.1663  0.1137  202 ASP B CA  
12020 C C   . ASP B 198 ? 0.7454 1.1482 0.7754 -0.1606 0.1521  0.1236  202 ASP B C   
12021 O O   . ASP B 198 ? 0.7181 1.1073 0.7668 -0.1451 0.1482  0.1116  202 ASP B O   
12022 C CB  . ASP B 198 ? 0.7414 1.2611 0.8004 -0.1591 0.1749  0.0973  202 ASP B CB  
12023 C CG  . ASP B 198 ? 0.7669 1.3000 0.8315 -0.1871 0.1744  0.1111  202 ASP B CG  
12024 O OD1 . ASP B 198 ? 0.8035 1.3005 0.8492 -0.2085 0.1666  0.1336  202 ASP B OD1 
12025 O OD2 . ASP B 198 ? 0.7529 1.3321 0.8412 -0.1876 0.1808  0.0994  202 ASP B OD2 
12030 N N   . ALA B 199 ? 0.7979 1.1612 0.8054 -0.1770 0.1436  0.1454  203 ALA B N   
12031 C CA  . ALA B 199 ? 0.8508 1.1517 0.8560 -0.1739 0.1296  0.1531  203 ALA B CA  
12032 C C   . ALA B 199 ? 0.8576 1.1541 0.8743 -0.1904 0.1255  0.1584  203 ALA B C   
12033 O O   . ALA B 199 ? 0.8130 1.0708 0.8375 -0.1808 0.1167  0.1545  203 ALA B O   
12034 C CB  . ALA B 199 ? 0.9265 1.1852 0.9052 -0.1839 0.1201  0.1736  203 ALA B CB  
12040 N N   . GLU B 200 ? 0.9106 1.2473 0.9282 -0.2160 0.1317  0.1670  204 GLU B N   
12041 C CA  . GLU B 200 ? 0.9501 1.2872 0.9806 -0.2323 0.1279  0.1707  204 GLU B CA  
12042 C C   . GLU B 200 ? 0.9271 1.2841 0.9854 -0.2121 0.1310  0.1485  204 GLU B C   
12043 O O   . GLU B 200 ? 0.9032 1.2404 0.9719 -0.2156 0.1237  0.1479  204 GLU B O   
12044 C CB  . GLU B 200 ? 0.9675 1.3511 0.9946 -0.2647 0.1350  0.1839  204 GLU B CB  
12045 C CG  . GLU B 200 ? 1.0854 1.4349 1.0864 -0.2935 0.1258  0.2116  204 GLU B CG  
12046 C CD  . GLU B 200 ? 1.1991 1.4875 1.1986 -0.3002 0.1097  0.2208  204 GLU B CD  
12047 O OE1 . GLU B 200 ? 1.2136 1.4996 1.2334 -0.2908 0.1078  0.2075  204 GLU B OE1 
12048 O OE2 . GLU B 200 ? 1.2637 1.5058 1.2414 -0.3144 0.0980  0.2408  204 GLU B OE2 
12055 N N   . ARG B 201 ? 0.9017 1.2966 0.9718 -0.1911 0.1408  0.1301  205 ARG B N   
12056 C CA  . ARG B 201 ? 0.8731 1.2820 0.9686 -0.1695 0.1416  0.1094  205 ARG B CA  
12057 C C   . ARG B 201 ? 0.7689 1.1193 0.8631 -0.1504 0.1304  0.1054  205 ARG B C   
12058 O O   . ARG B 201 ? 0.7495 1.0907 0.8586 -0.1453 0.1251  0.0985  205 ARG B O   
12059 C CB  . ARG B 201 ? 0.9424 1.3985 1.0486 -0.1501 0.1526  0.0907  205 ARG B CB  
12060 C CG  . ARG B 201 ? 0.9810 1.4526 1.1137 -0.1262 0.1522  0.0693  205 ARG B CG  
12061 C CD  . ARG B 201 ? 1.0397 1.5465 1.1944 -0.1384 0.1532  0.0669  205 ARG B CD  
12062 N NE  . ARG B 201 ? 1.1008 1.6226 1.2807 -0.1145 0.1514  0.0468  205 ARG B NE  
12063 C CZ  . ARG B 201 ? 1.2213 1.7548 1.4212 -0.1174 0.1469  0.0430  205 ARG B CZ  
12064 N NH1 . ARG B 201 ? 1.3065 1.8383 1.5046 -0.1436 0.1441  0.0571  205 ARG B NH1 
12065 N NH2 . ARG B 201 ? 1.2603 1.8056 1.4816 -0.0943 0.1440  0.0255  205 ARG B NH2 
12079 N N   . PHE B 202 ? 0.6929 1.0058 0.7694 -0.1403 0.1266  0.1095  206 PHE B N   
12080 C CA  . PHE B 202 ? 0.6781 0.9356 0.7513 -0.1255 0.1162  0.1078  206 PHE B CA  
12081 C C   . PHE B 202 ? 0.6867 0.9106 0.7576 -0.1420 0.1065  0.1187  206 PHE B C   
12082 O O   . PHE B 202 ? 0.6376 0.8397 0.7178 -0.1327 0.1005  0.1109  206 PHE B O   
12083 C CB  . PHE B 202 ? 0.6763 0.9029 0.7298 -0.1174 0.1134  0.1139  206 PHE B CB  
12084 C CG  . PHE B 202 ? 0.6623 0.8405 0.7145 -0.0987 0.1047  0.1090  206 PHE B CG  
12085 C CD1 . PHE B 202 ? 0.6848 0.8156 0.7277 -0.1058 0.0943  0.1196  206 PHE B CD1 
12086 C CD2 . PHE B 202 ? 0.6296 0.8103 0.6896 -0.0743 0.1067  0.0935  206 PHE B CD2 
12087 C CE1 . PHE B 202 ? 0.6724 0.7636 0.7147 -0.0884 0.0874  0.1137  206 PHE B CE1 
12088 C CE2 . PHE B 202 ? 0.6031 0.7434 0.6616 -0.0590 0.0996  0.0896  206 PHE B CE2 
12089 C CZ  . PHE B 202 ? 0.6198 0.7175 0.6698 -0.0657 0.0906  0.0991  206 PHE B CZ  
12099 N N   . ASN B 203 ? 0.7490 0.9674 0.8062 -0.1675 0.1043  0.1370  207 ASN B N   
12100 C CA  . ASN B 203 ? 0.8138 0.9999 0.8684 -0.1854 0.0941  0.1474  207 ASN B CA  
12101 C C   . ASN B 203 ? 0.9398 1.1513 1.0157 -0.1885 0.0952  0.1374  207 ASN B C   
12102 O O   . ASN B 203 ? 0.9958 1.1752 1.0755 -0.1863 0.0865  0.1341  207 ASN B O   
12103 C CB  . ASN B 203 ? 0.7986 0.9839 0.8366 -0.2155 0.0921  0.1692  207 ASN B CB  
12104 C CG  . ASN B 203 ? 0.7656 0.9077 0.7805 -0.2146 0.0848  0.1825  207 ASN B CG  
12105 O OD1 . ASN B 203 ? 0.7391 0.8489 0.7516 -0.1918 0.0806  0.1751  207 ASN B OD1 
12106 N ND2 . ASN B 203 ? 0.7860 0.9281 0.7841 -0.2401 0.0826  0.2029  207 ASN B ND2 
12113 N N   . GLU B 204 ? 1.0048 1.2758 1.0952 -0.1931 0.1058  0.1315  208 GLU B N   
12114 C CA  . GLU B 204 ? 1.0199 1.3199 1.1319 -0.1980 0.1061  0.1233  208 GLU B CA  
12115 C C   . GLU B 204 ? 0.9231 1.2062 1.0479 -0.1726 0.1016  0.1065  208 GLU B C   
12116 O O   . GLU B 204 ? 0.8954 1.1616 1.0268 -0.1768 0.0938  0.1047  208 GLU B O   
12117 C CB  . GLU B 204 ? 1.0920 1.4633 1.2196 -0.2031 0.1188  0.1173  208 GLU B CB  
12118 C CG  . GLU B 204 ? 1.1918 1.5986 1.3436 -0.2107 0.1187  0.1102  208 GLU B CG  
12119 C CD  . GLU B 204 ? 1.3404 1.8201 1.5128 -0.2072 0.1311  0.0985  208 GLU B CD  
12120 O OE1 . GLU B 204 ? 1.4017 1.9108 1.5985 -0.2002 0.1306  0.0861  208 GLU B OE1 
12121 O OE2 . GLU B 204 ? 1.4324 1.9410 1.5970 -0.2107 0.1411  0.1010  208 GLU B OE2 
12128 N N   . ILE B 205 ? 0.8896 1.1770 1.0171 -0.1470 0.1057  0.0943  209 ILE B N   
12129 C CA  . ILE B 205 ? 0.8467 1.1244 0.9869 -0.1245 0.1017  0.0791  209 ILE B CA  
12130 C C   . ILE B 205 ? 0.8245 1.0429 0.9525 -0.1205 0.0911  0.0821  209 ILE B C   
12131 O O   . ILE B 205 ? 0.8315 1.0386 0.9679 -0.1136 0.0852  0.0742  209 ILE B O   
12132 C CB  . ILE B 205 ? 0.7846 1.0802 0.9303 -0.0994 0.1077  0.0659  209 ILE B CB  
12133 C CG1 . ILE B 205 ? 0.8586 1.1151 0.9849 -0.0888 0.1062  0.0696  209 ILE B CG1 
12134 C CG2 . ILE B 205 ? 0.7169 1.0709 0.8722 -0.1033 0.1188  0.0620  209 ILE B CG2 
12135 C CD1 . ILE B 205 ? 0.9155 1.1363 1.0422 -0.0685 0.0994  0.0611  209 ILE B CD1 
12147 N N   . VAL B 206 ? 0.8100 0.9911 0.9182 -0.1246 0.0882  0.0929  210 VAL B N   
12148 C CA  . VAL B 206 ? 0.7783 0.9049 0.8759 -0.1214 0.0781  0.0948  210 VAL B CA  
12149 C C   . VAL B 206 ? 0.7985 0.9136 0.8984 -0.1405 0.0708  0.0993  210 VAL B C   
12150 O O   . VAL B 206 ? 0.7891 0.8798 0.8912 -0.1344 0.0639  0.0920  210 VAL B O   
12151 C CB  . VAL B 206 ? 0.7704 0.8624 0.8482 -0.1225 0.0754  0.1060  210 VAL B CB  
12152 C CG1 . VAL B 206 ? 0.7779 0.8160 0.8457 -0.1250 0.0640  0.1096  210 VAL B CG1 
12153 C CG2 . VAL B 206 ? 0.7511 0.8442 0.8265 -0.0999 0.0800  0.0987  210 VAL B CG2 
12163 N N   . LYS B 207 ? 0.8159 0.9493 0.9145 -0.1652 0.0719  0.1113  211 LYS B N   
12164 C CA  . LYS B 207 ? 0.8476 0.9701 0.9480 -0.1862 0.0641  0.1166  211 LYS B CA  
12165 C C   . LYS B 207 ? 0.8451 0.9928 0.9650 -0.1812 0.0637  0.1034  211 LYS B C   
12166 O O   . LYS B 207 ? 0.8821 1.0082 1.0024 -0.1899 0.0548  0.1024  211 LYS B O   
12167 C CB  . LYS B 207 ? 0.8705 1.0166 0.9675 -0.2152 0.0665  0.1325  211 LYS B CB  
12168 C CG  . LYS B 207 ? 0.9107 1.0227 0.9854 -0.2264 0.0625  0.1495  211 LYS B CG  
12169 C CD  . LYS B 207 ? 0.9358 1.0809 1.0068 -0.2556 0.0669  0.1658  211 LYS B CD  
12170 C CE  . LYS B 207 ? 0.9890 1.1018 1.0362 -0.2665 0.0623  0.1842  211 LYS B CE  
12171 N NZ  . LYS B 207 ? 1.0036 1.1594 1.0456 -0.2907 0.0702  0.1988  211 LYS B NZ  
12185 N N   . ASN B 208 ? 0.7577 0.9498 0.8934 -0.1670 0.0719  0.0930  212 ASN B N   
12186 C CA  . ASN B 208 ? 0.7865 1.0055 0.9420 -0.1611 0.0705  0.0810  212 ASN B CA  
12187 C C   . ASN B 208 ? 0.7806 0.9740 0.9362 -0.1370 0.0657  0.0688  212 ASN B C   
12188 O O   . ASN B 208 ? 0.7744 0.9862 0.9447 -0.1305 0.0629  0.0593  212 ASN B O   
12189 C CB  . ASN B 208 ? 0.8497 1.1312 1.0246 -0.1572 0.0804  0.0750  212 ASN B CB  
12190 C CG  . ASN B 208 ? 0.8888 1.2065 1.0666 -0.1835 0.0859  0.0860  212 ASN B CG  
12191 O OD1 . ASN B 208 ? 0.8866 1.1881 1.0576 -0.2074 0.0801  0.0972  212 ASN B OD1 
12192 N ND2 . ASN B 208 ? 0.8945 1.2621 1.0821 -0.1799 0.0969  0.0824  212 ASN B ND2 
12199 N N   . GLN B 209 ? 0.7982 0.9513 0.9381 -0.1245 0.0644  0.0691  213 GLN B N   
12200 C CA  . GLN B 209 ? 0.7314 0.8638 0.8705 -0.1029 0.0609  0.0581  213 GLN B CA  
12201 C C   . GLN B 209 ? 0.7257 0.8271 0.8602 -0.1083 0.0512  0.0555  213 GLN B C   
12202 O O   . GLN B 209 ? 0.7300 0.8062 0.8549 -0.1249 0.0460  0.0626  213 GLN B O   
12203 C CB  . GLN B 209 ? 0.7264 0.8305 0.8516 -0.0882 0.0632  0.0589  213 GLN B CB  
12204 C CG  . GLN B 209 ? 0.7282 0.8611 0.8583 -0.0759 0.0718  0.0565  213 GLN B CG  
12205 C CD  . GLN B 209 ? 0.7491 0.9122 0.8962 -0.0607 0.0731  0.0443  213 GLN B CD  
12206 O OE1 . GLN B 209 ? 0.8321 0.9783 0.9793 -0.0468 0.0686  0.0370  213 GLN B OE1 
12207 N NE2 . GLN B 209 ? 0.7085 0.9173 0.8701 -0.0635 0.0788  0.0421  213 GLN B NE2 
12216 N N   . LYS B 210 ? 0.7101 0.8125 0.8503 -0.0944 0.0481  0.0450  214 LYS B N   
12217 C CA  . LYS B 210 ? 0.8016 0.8772 0.9361 -0.0967 0.0393  0.0400  214 LYS B CA  
12218 C C   . LYS B 210 ? 0.7687 0.8227 0.8956 -0.0763 0.0386  0.0320  214 LYS B C   
12219 O O   . LYS B 210 ? 0.7506 0.8208 0.8833 -0.0607 0.0428  0.0285  214 LYS B O   
12220 C CB  . LYS B 210 ? 0.8979 1.0024 1.0472 -0.1047 0.0347  0.0361  214 LYS B CB  
12221 C CG  . LYS B 210 ? 0.9989 1.1322 1.1584 -0.1264 0.0359  0.0437  214 LYS B CG  
12222 C CD  . LYS B 210 ? 1.1396 1.2400 1.2860 -0.1473 0.0301  0.0512  214 LYS B CD  
12223 C CE  . LYS B 210 ? 1.2605 1.3910 1.4170 -0.1719 0.0305  0.0599  214 LYS B CE  
12224 N NZ  . LYS B 210 ? 1.3525 1.4503 1.4982 -0.1938 0.0213  0.0656  214 LYS B NZ  
12238 N N   . ILE B 211 ? 0.7262 0.7440 0.8401 -0.0769 0.0329  0.0287  215 ILE B N   
12239 C CA  . ILE B 211 ? 0.6476 0.6455 0.7528 -0.0597 0.0329  0.0215  215 ILE B CA  
12240 C C   . ILE B 211 ? 0.5587 0.5722 0.6699 -0.0533 0.0291  0.0140  215 ILE B C   
12241 O O   . ILE B 211 ? 0.5501 0.5810 0.6695 -0.0629 0.0243  0.0131  215 ILE B O   
12242 C CB  . ILE B 211 ? 0.6881 0.6442 0.7777 -0.0617 0.0288  0.0189  215 ILE B CB  
12243 C CG1 . ILE B 211 ? 0.7402 0.6871 0.8278 -0.0772 0.0207  0.0162  215 ILE B CG1 
12244 C CG2 . ILE B 211 ? 0.7071 0.6444 0.7904 -0.0642 0.0311  0.0269  215 ILE B CG2 
12245 C CD1 . ILE B 211 ? 0.7959 0.7053 0.8691 -0.0749 0.0157  0.0079  215 ILE B CD1 
12257 N N   . SER B 212 ? 0.5272 0.5343 0.6337 -0.0376 0.0304  0.0095  216 SER B N   
12258 C CA  . SER B 212 ? 0.5370 0.5490 0.6431 -0.0316 0.0253  0.0034  216 SER B CA  
12259 C C   . SER B 212 ? 0.5588 0.5406 0.6481 -0.0270 0.0243  -0.0022 216 SER B C   
12260 O O   . SER B 212 ? 0.5415 0.4991 0.6218 -0.0293 0.0261  -0.0027 216 SER B O   
12261 C CB  . SER B 212 ? 0.6046 0.6391 0.7209 -0.0182 0.0268  0.0035  216 SER B CB  
12262 O OG  . SER B 212 ? 0.6790 0.7162 0.7939 -0.0137 0.0201  -0.0005 216 SER B OG  
12268 N N   . ALA B 213 ? 0.5985 0.5826 0.6835 -0.0204 0.0211  -0.0066 217 ALA B N   
12269 C CA  . ALA B 213 ? 0.5982 0.5598 0.6674 -0.0163 0.0212  -0.0129 217 ALA B CA  
12270 C C   . ALA B 213 ? 0.5472 0.5172 0.6132 -0.0075 0.0196  -0.0139 217 ALA B C   
12271 O O   . ALA B 213 ? 0.5456 0.5353 0.6218 -0.0042 0.0164  -0.0102 217 ALA B O   
12272 C CB  . ALA B 213 ? 0.5766 0.5241 0.6365 -0.0275 0.0158  -0.0192 217 ALA B CB  
12278 N N   . ASN B 214 ? 0.5494 0.5041 0.6014 -0.0037 0.0213  -0.0192 218 ASN B N   
12279 C CA  . ASN B 214 ? 0.5772 0.5361 0.6217 0.0020  0.0198  -0.0198 218 ASN B CA  
12280 C C   . ASN B 214 ? 0.6321 0.5748 0.6602 0.0016  0.0226  -0.0283 218 ASN B C   
12281 O O   . ASN B 214 ? 0.6674 0.5950 0.6924 -0.0010 0.0248  -0.0339 218 ASN B O   
12282 C CB  . ASN B 214 ? 0.5992 0.5648 0.6506 0.0126  0.0233  -0.0141 218 ASN B CB  
12283 C CG  . ASN B 214 ? 0.6278 0.5804 0.6755 0.0192  0.0313  -0.0156 218 ASN B CG  
12284 O OD1 . ASN B 214 ? 0.6506 0.6024 0.6936 0.0256  0.0336  -0.0152 218 ASN B OD1 
12285 N ND2 . ASN B 214 ? 0.6566 0.5989 0.7064 0.0170  0.0346  -0.0168 218 ASN B ND2 
12292 N N   . ILE B 215 ? 0.6948 0.6408 0.7124 0.0039  0.0222  -0.0295 219 ILE B N   
12293 C CA  . ILE B 215 ? 0.8025 0.7401 0.8038 0.0014  0.0240  -0.0393 219 ILE B CA  
12294 C C   . ILE B 215 ? 0.7679 0.7014 0.7638 0.0096  0.0321  -0.0427 219 ILE B C   
12295 O O   . ILE B 215 ? 0.8323 0.7594 0.8173 0.0093  0.0354  -0.0533 219 ILE B O   
12296 C CB  . ILE B 215 ? 0.9379 0.8851 0.9273 -0.0060 0.0170  -0.0398 219 ILE B CB  
12297 C CG1 . ILE B 215 ? 1.0247 0.9834 1.0146 -0.0028 0.0141  -0.0299 219 ILE B CG1 
12298 C CG2 . ILE B 215 ? 1.0070 0.9578 1.0010 -0.0149 0.0086  -0.0393 219 ILE B CG2 
12299 C CD1 . ILE B 215 ? 1.1119 1.0783 1.0871 -0.0105 0.0066  -0.0287 219 ILE B CD1 
12311 N N   . ASP B 216 ? 0.6069 0.5452 0.6105 0.0168  0.0352  -0.0352 220 ASP B N   
12312 C CA  . ASP B 216 ? 0.6067 0.5437 0.6068 0.0238  0.0424  -0.0380 220 ASP B CA  
12313 C C   . ASP B 216 ? 0.5888 0.5172 0.6003 0.0316  0.0471  -0.0368 220 ASP B C   
12314 O O   . ASP B 216 ? 0.5570 0.4860 0.5793 0.0324  0.0453  -0.0297 220 ASP B O   
12315 C CB  . ASP B 216 ? 0.6038 0.5521 0.6012 0.0246  0.0413  -0.0303 220 ASP B CB  
12316 C CG  . ASP B 216 ? 0.6230 0.5738 0.6339 0.0300  0.0395  -0.0206 220 ASP B CG  
12317 O OD1 . ASP B 216 ? 0.6474 0.5974 0.6688 0.0303  0.0371  -0.0182 220 ASP B OD1 
12318 O OD2 . ASP B 216 ? 0.5952 0.5498 0.6060 0.0334  0.0406  -0.0159 220 ASP B OD2 
12323 N N   . THR B 217 ? 0.6315 0.5537 0.6403 0.0375  0.0529  -0.0442 221 THR B N   
12324 C CA  . THR B 217 ? 0.6375 0.5483 0.6553 0.0444  0.0557  -0.0441 221 THR B CA  
12325 C C   . THR B 217 ? 0.6201 0.5369 0.6477 0.0492  0.0569  -0.0337 221 THR B C   
12326 O O   . THR B 217 ? 0.6333 0.5448 0.6686 0.0493  0.0557  -0.0284 221 THR B O   
12327 C CB  . THR B 217 ? 0.6342 0.5397 0.6486 0.0515  0.0607  -0.0550 221 THR B CB  
12328 O OG1 . THR B 217 ? 0.6393 0.5356 0.6457 0.0480  0.0589  -0.0667 221 THR B OG1 
12329 C CG2 . THR B 217 ? 0.6842 0.5783 0.7082 0.0599  0.0622  -0.0531 221 THR B CG2 
12337 N N   . PRO B 218 ? 0.6002 0.5277 0.6273 0.0525  0.0590  -0.0304 222 PRO B N   
12338 C CA  . PRO B 218 ? 0.6599 0.5913 0.6959 0.0574  0.0594  -0.0220 222 PRO B CA  
12339 C C   . PRO B 218 ? 0.6881 0.6244 0.7299 0.0539  0.0546  -0.0152 222 PRO B C   
12340 O O   . PRO B 218 ? 0.9192 0.8607 0.9580 0.0483  0.0500  -0.0146 222 PRO B O   
12341 C CB  . PRO B 218 ? 0.6171 0.5582 0.6494 0.0589  0.0609  -0.0206 222 PRO B CB  
12342 C CG  . PRO B 218 ? 0.5783 0.5218 0.6004 0.0559  0.0635  -0.0290 222 PRO B CG  
12343 C CD  . PRO B 218 ? 0.5851 0.5223 0.6027 0.0503  0.0604  -0.0337 222 PRO B CD  
12351 N N   . GLU B 219 ? 0.6369 0.5733 0.6873 0.0574  0.0556  -0.0106 223 GLU B N   
12352 C CA  . GLU B 219 ? 0.6352 0.5800 0.6935 0.0551  0.0524  -0.0058 223 GLU B CA  
12353 C C   . GLU B 219 ? 0.5915 0.5452 0.6556 0.0612  0.0517  -0.0017 223 GLU B C   
12354 O O   . GLU B 219 ? 0.5201 0.4720 0.5820 0.0661  0.0535  -0.0014 223 GLU B O   
12355 C CB  . GLU B 219 ? 0.6864 0.6265 0.7490 0.0523  0.0541  -0.0043 223 GLU B CB  
12356 C CG  . GLU B 219 ? 0.7634 0.6885 0.8198 0.0472  0.0538  -0.0090 223 GLU B CG  
12357 C CD  . GLU B 219 ? 0.7880 0.7151 0.8412 0.0390  0.0493  -0.0123 223 GLU B CD  
12358 O OE1 . GLU B 219 ? 0.7826 0.7213 0.8358 0.0384  0.0464  -0.0116 223 GLU B OE1 
12359 O OE2 . GLU B 219 ? 0.9018 0.8177 0.9522 0.0327  0.0477  -0.0153 223 GLU B OE2 
12366 N N   . GLY B 220 ? 0.5583 0.5229 0.6309 0.0611  0.0487  0.0007  224 GLY B N   
12367 C CA  . GLY B 220 ? 0.5021 0.4749 0.5809 0.0677  0.0465  0.0026  224 GLY B CA  
12368 C C   . GLY B 220 ? 0.5066 0.4850 0.5917 0.0720  0.0506  0.0036  224 GLY B C   
12369 O O   . GLY B 220 ? 0.5125 0.5029 0.6060 0.0763  0.0488  0.0032  224 GLY B O   
12373 N N   . GLY B 221 ? 0.5117 0.5380 0.5959 -0.0009 -0.0255 0.0257  225 GLY B N   
12374 C CA  . GLY B 221 ? 0.5406 0.5817 0.6355 -0.0037 -0.0208 0.0281  225 GLY B CA  
12375 C C   . GLY B 221 ? 0.5423 0.5913 0.6399 0.0013  -0.0149 0.0260  225 GLY B C   
12376 O O   . GLY B 221 ? 0.5179 0.5807 0.6221 0.0013  -0.0119 0.0263  225 GLY B O   
12380 N N   . PHE B 222 ? 0.5112 0.5496 0.6010 0.0050  -0.0131 0.0244  226 PHE B N   
12381 C CA  . PHE B 222 ? 0.5120 0.5514 0.6006 0.0061  -0.0098 0.0226  226 PHE B CA  
12382 C C   . PHE B 222 ? 0.5256 0.5675 0.6152 0.0109  -0.0100 0.0193  226 PHE B C   
12383 O O   . PHE B 222 ? 0.5459 0.5886 0.6321 0.0122  -0.0073 0.0166  226 PHE B O   
12384 C CB  . PHE B 222 ? 0.5422 0.5709 0.6236 0.0064  -0.0087 0.0238  226 PHE B CB  
12385 C CG  . PHE B 222 ? 0.5075 0.5414 0.5903 0.0042  -0.0059 0.0283  226 PHE B CG  
12386 C CD1 . PHE B 222 ? 0.4889 0.5283 0.5748 0.0047  -0.0055 0.0305  226 PHE B CD1 
12387 C CD2 . PHE B 222 ? 0.5289 0.5635 0.6106 0.0019  -0.0036 0.0321  226 PHE B CD2 
12388 C CE1 . PHE B 222 ? 0.5268 0.5726 0.6142 0.0065  -0.0026 0.0359  226 PHE B CE1 
12389 C CE2 . PHE B 222 ? 0.4963 0.5436 0.5834 0.0018  -0.0005 0.0385  226 PHE B CE2 
12390 C CZ  . PHE B 222 ? 0.4898 0.5429 0.5796 0.0059  0.0002  0.0401  226 PHE B CZ  
12400 N N   . ASP B 223 ? 0.5593 0.6020 0.6512 0.0152  -0.0135 0.0197  227 ASP B N   
12401 C CA  . ASP B 223 ? 0.5471 0.5980 0.6429 0.0236  -0.0130 0.0186  227 ASP B CA  
12402 C C   . ASP B 223 ? 0.5407 0.6131 0.6469 0.0235  -0.0090 0.0199  227 ASP B C   
12403 O O   . ASP B 223 ? 0.5376 0.6132 0.6405 0.0322  -0.0040 0.0174  227 ASP B O   
12404 C CB  . ASP B 223 ? 0.5561 0.6119 0.6566 0.0273  -0.0194 0.0212  227 ASP B CB  
12405 C CG  . ASP B 223 ? 0.5618 0.5974 0.6491 0.0340  -0.0211 0.0203  227 ASP B CG  
12406 O OD1 . ASP B 223 ? 0.6034 0.6205 0.6789 0.0340  -0.0172 0.0181  227 ASP B OD1 
12407 O OD2 . ASP B 223 ? 0.5568 0.5948 0.6446 0.0379  -0.0274 0.0228  227 ASP B OD2 
12412 N N   . ALA B 224 ? 0.5550 0.6393 0.6703 0.0144  -0.0107 0.0242  228 ALA B N   
12413 C CA  . ALA B 224 ? 0.5324 0.6391 0.6578 0.0125  -0.0064 0.0281  228 ALA B CA  
12414 C C   . ALA B 224 ? 0.5061 0.6076 0.6210 0.0127  -0.0003 0.0254  228 ALA B C   
12415 O O   . ALA B 224 ? 0.4480 0.5627 0.5626 0.0181  0.0061  0.0255  228 ALA B O   
12416 C CB  . ALA B 224 ? 0.5158 0.6305 0.6507 -0.0001 -0.0114 0.0347  228 ALA B CB  
12422 N N   . ILE B 225 ? 0.4921 0.5767 0.5979 0.0076  -0.0022 0.0237  229 ILE B N   
12423 C CA  . ILE B 225 ? 0.4730 0.5545 0.5687 0.0061  0.0006  0.0219  229 ILE B CA  
12424 C C   . ILE B 225 ? 0.5007 0.5737 0.5835 0.0138  0.0033  0.0149  229 ILE B C   
12425 O O   . ILE B 225 ? 0.5376 0.6149 0.6114 0.0168  0.0076  0.0130  229 ILE B O   
12426 C CB  . ILE B 225 ? 0.4899 0.5604 0.5818 0.0005  -0.0028 0.0231  229 ILE B CB  
12427 C CG1 . ILE B 225 ? 0.5228 0.5961 0.6208 -0.0035 -0.0042 0.0295  229 ILE B CG1 
12428 C CG2 . ILE B 225 ? 0.4639 0.5328 0.5456 -0.0023 -0.0030 0.0212  229 ILE B CG2 
12429 C CD1 . ILE B 225 ? 0.5186 0.5849 0.6139 -0.0039 -0.0056 0.0321  229 ILE B CD1 
12441 N N   . MET B 226 ? 0.5367 0.5931 0.6139 0.0176  0.0010  0.0111  230 MET B N   
12442 C CA  . MET B 226 ? 0.5584 0.5964 0.6177 0.0254  0.0026  0.0041  230 MET B CA  
12443 C C   . MET B 226 ? 0.5674 0.6183 0.6256 0.0389  0.0097  0.0027  230 MET B C   
12444 O O   . MET B 226 ? 0.6113 0.6529 0.6506 0.0445  0.0136  -0.0029 230 MET B O   
12445 C CB  . MET B 226 ? 0.5076 0.5258 0.5623 0.0285  -0.0008 0.0029  230 MET B CB  
12446 C CG  . MET B 226 ? 0.5636 0.5550 0.5963 0.0387  0.0004  -0.0040 230 MET B CG  
12447 S SD  . MET B 226 ? 0.6645 0.6273 0.6710 0.0271  -0.0036 -0.0106 230 MET B SD  
12448 C CE  . MET B 226 ? 0.6553 0.6086 0.6676 0.0108  -0.0105 -0.0046 230 MET B CE  
12458 N N   . GLN B 227 ? 0.5005 0.5743 0.5779 0.0445  0.0114  0.0084  231 GLN B N   
12459 C CA  . GLN B 227 ? 0.5138 0.6092 0.5958 0.0590  0.0195  0.0100  231 GLN B CA  
12460 C C   . GLN B 227 ? 0.5289 0.6419 0.6095 0.0562  0.0264  0.0123  231 GLN B C   
12461 O O   . GLN B 227 ? 0.5009 0.6155 0.5672 0.0696  0.0351  0.0089  231 GLN B O   
12462 C CB  . GLN B 227 ? 0.4945 0.6189 0.6029 0.0609  0.0174  0.0185  231 GLN B CB  
12463 C CG  . GLN B 227 ? 0.5045 0.6146 0.6111 0.0694  0.0120  0.0170  231 GLN B CG  
12464 C CD  . GLN B 227 ? 0.5265 0.6194 0.6143 0.0906  0.0181  0.0112  231 GLN B CD  
12465 O OE1 . GLN B 227 ? 0.5594 0.6759 0.6536 0.1074  0.0261  0.0141  231 GLN B OE1 
12466 N NE2 . GLN B 227 ? 0.5346 0.5854 0.5978 0.0905  0.0147  0.0038  231 GLN B NE2 
12475 N N   . ALA B 228 ? 0.5357 0.6592 0.6273 0.0404  0.0230  0.0184  232 ALA B N   
12476 C CA  . ALA B 228 ? 0.5112 0.6503 0.6002 0.0369  0.0291  0.0227  232 ALA B CA  
12477 C C   . ALA B 228 ? 0.5206 0.6375 0.5801 0.0401  0.0306  0.0140  232 ALA B C   
12478 O O   . ALA B 228 ? 0.5842 0.7111 0.6321 0.0454  0.0385  0.0148  232 ALA B O   
12479 C CB  . ALA B 228 ? 0.4950 0.6405 0.5968 0.0201  0.0237  0.0310  232 ALA B CB  
12485 N N   . ALA B 229 ? 0.5266 0.6139 0.5723 0.0357  0.0228  0.0066  233 ALA B N   
12486 C CA  . ALA B 229 ? 0.6007 0.6654 0.6176 0.0340  0.0204  -0.0014 233 ALA B CA  
12487 C C   . ALA B 229 ? 0.6846 0.7278 0.6744 0.0500  0.0256  -0.0116 233 ALA B C   
12488 O O   . ALA B 229 ? 0.7305 0.7596 0.6915 0.0527  0.0270  -0.0181 233 ALA B O   
12489 C CB  . ALA B 229 ? 0.5745 0.6198 0.5893 0.0204  0.0093  -0.0031 233 ALA B CB  
12495 N N   . VAL B 230 ? 0.7133 0.7512 0.7082 0.0622  0.0281  -0.0132 234 VAL B N   
12496 C CA  . VAL B 230 ? 0.7682 0.7765 0.7336 0.0801  0.0322  -0.0232 234 VAL B CA  
12497 C C   . VAL B 230 ? 0.7758 0.8089 0.7427 0.1030  0.0468  -0.0209 234 VAL B C   
12498 O O   . VAL B 230 ? 0.8460 0.8579 0.7797 0.1198  0.0538  -0.0297 234 VAL B O   
12499 C CB  . VAL B 230 ? 0.8369 0.8207 0.8036 0.0820  0.0260  -0.0251 234 VAL B CB  
12500 C CG1 . VAL B 230 ? 0.9683 0.9228 0.9070 0.1059  0.0319  -0.0332 234 VAL B CG1 
12501 C CG2 . VAL B 230 ? 0.8168 0.7724 0.7740 0.0610  0.0136  -0.0278 234 VAL B CG2 
12511 N N   . CYS B 231 ? 0.7266 0.8048 0.7304 0.1040  0.0515  -0.0088 235 CYS B N   
12512 C CA  . CYS B 231 ? 0.7076 0.8202 0.7212 0.1252  0.0657  -0.0029 235 CYS B CA  
12513 C C   . CYS B 231 ? 0.7360 0.8697 0.7412 0.1253  0.0759  0.0004  235 CYS B C   
12514 O O   . CYS B 231 ? 0.7366 0.9143 0.7701 0.1182  0.0809  0.0137  235 CYS B O   
12515 C CB  . CYS B 231 ? 0.6477 0.8030 0.7052 0.1217  0.0640  0.0105  235 CYS B CB  
12516 S SG  . CYS B 231 ? 0.6927 0.8277 0.7588 0.1235  0.0523  0.0087  235 CYS B SG  
12521 N N   . LYS B 232 ? 0.7633 0.8618 0.7254 0.1325  0.0782  -0.0118 236 LYS B N   
12522 C CA  . LYS B 232 ? 0.7925 0.9043 0.7385 0.1320  0.0866  -0.0098 236 LYS B CA  
12523 C C   . LYS B 232 ? 0.8375 0.9974 0.7984 0.1515  0.1057  0.0011  236 LYS B C   
12524 O O   . LYS B 232 ? 0.8122 1.0105 0.7916 0.1417  0.1116  0.0141  236 LYS B O   
12525 C CB  . LYS B 232 ? 0.8073 0.8681 0.6980 0.1380  0.0843  -0.0264 236 LYS B CB  
12526 C CG  . LYS B 232 ? 0.8238 0.8942 0.6868 0.1454  0.0955  -0.0264 236 LYS B CG  
12527 C CD  . LYS B 232 ? 0.8679 0.8827 0.6740 0.1435  0.0868  -0.0435 236 LYS B CD  
12528 C CE  . LYS B 232 ? 0.9754 0.9918 0.7418 0.1585  0.1000  -0.0465 236 LYS B CE  
12529 N NZ  . LYS B 232 ? 0.9681 1.0083 0.7401 0.1387  0.0963  -0.0368 236 LYS B NZ  
12543 N N   . GLU B 233 ? 0.9289 1.0887 0.8823 0.1799  0.1162  -0.0024 237 GLU B N   
12544 C CA  . GLU B 233 ? 0.9886 1.2000 0.9565 0.2018  0.1365  0.0093  237 GLU B CA  
12545 C C   . GLU B 233 ? 0.8712 1.1453 0.8985 0.1861  0.1358  0.0301  237 GLU B C   
12546 O O   . GLU B 233 ? 0.8615 1.1820 0.9067 0.1814  0.1466  0.0448  237 GLU B O   
12547 C CB  . GLU B 233 ? 1.1548 1.3540 1.1046 0.2389  0.1474  0.0023  237 GLU B CB  
12548 C CG  . GLU B 233 ? 1.3385 1.5929 1.2984 0.2673  0.1716  0.0143  237 GLU B CG  
12549 C CD  . GLU B 233 ? 1.5370 1.7862 1.4860 0.3075  0.1827  0.0103  237 GLU B CD  
12550 O OE1 . GLU B 233 ? 1.6328 1.8529 1.5854 0.3090  0.1701  0.0047  237 GLU B OE1 
12551 O OE2 . GLU B 233 ? 1.6589 1.9333 1.5944 0.3394  0.2049  0.0137  237 GLU B OE2 
12558 N N   . LYS B 234 ? 0.7864 1.0604 0.8421 0.1762  0.1223  0.0323  238 LYS B N   
12559 C CA  . LYS B 234 ? 0.6409 0.9700 0.7489 0.1612  0.1192  0.0509  238 LYS B CA  
12560 C C   . LYS B 234 ? 0.5872 0.9209 0.7083 0.1276  0.1100  0.0583  238 LYS B C   
12561 O O   . LYS B 234 ? 0.5611 0.9421 0.7127 0.1153  0.1141  0.0756  238 LYS B O   
12562 C CB  . LYS B 234 ? 0.5680 0.8911 0.6956 0.1621  0.1066  0.0499  238 LYS B CB  
12563 C CG  . LYS B 234 ? 0.6116 0.9564 0.7447 0.1960  0.1171  0.0522  238 LYS B CG  
12564 C CD  . LYS B 234 ? 0.6953 1.0165 0.8331 0.2000  0.1035  0.0476  238 LYS B CD  
12565 C CE  . LYS B 234 ? 0.7680 1.1298 0.9272 0.2299  0.1115  0.0572  238 LYS B CE  
12566 N NZ  . LYS B 234 ? 0.7441 1.1729 0.9580 0.2143  0.1048  0.0771  238 LYS B NZ  
12580 N N   . ILE B 235 ? 0.5688 0.8544 0.6673 0.1124  0.0974  0.0469  239 ILE B N   
12581 C CA  . ILE B 235 ? 0.5400 0.8258 0.6448 0.0858  0.0904  0.0538  239 ILE B CA  
12582 C C   . ILE B 235 ? 0.5369 0.8416 0.6281 0.0882  0.1040  0.0606  239 ILE B C   
12583 O O   . ILE B 235 ? 0.5029 0.8348 0.6131 0.0711  0.1052  0.0758  239 ILE B O   
12584 C CB  . ILE B 235 ? 0.6233 0.8589 0.7069 0.0736  0.0758  0.0412  239 ILE B CB  
12585 C CG1 . ILE B 235 ? 0.6389 0.8598 0.7375 0.0689  0.0633  0.0375  239 ILE B CG1 
12586 C CG2 . ILE B 235 ? 0.6238 0.8584 0.7087 0.0521  0.0705  0.0485  239 ILE B CG2 
12587 C CD1 . ILE B 235 ? 0.6257 0.8722 0.7591 0.0518  0.0561  0.0502  239 ILE B CD1 
12599 N N   . GLY B 236 ? 0.5503 0.8369 0.6046 0.1090  0.1141  0.0498  240 GLY B N   
12600 C CA  . GLY B 236 ? 0.5473 0.8487 0.5810 0.1146  0.1281  0.0549  240 GLY B CA  
12601 C C   . GLY B 236 ? 0.6362 0.8990 0.6325 0.1047  0.1207  0.0460  240 GLY B C   
12602 O O   . GLY B 236 ? 0.7044 0.9814 0.6864 0.1036  0.1297  0.0536  240 GLY B O   
12606 N N   . TRP B 237 ? 0.6876 0.9057 0.6688 0.0966  0.1043  0.0321  241 TRP B N   
12607 C CA  . TRP B 237 ? 0.7628 0.9483 0.7093 0.0877  0.0956  0.0242  241 TRP B CA  
12608 C C   . TRP B 237 ? 0.9122 1.0874 0.8130 0.1068  0.1078  0.0164  241 TRP B C   
12609 O O   . TRP B 237 ? 0.9651 1.1215 0.8426 0.1282  0.1144  0.0043  241 TRP B O   
12610 C CB  . TRP B 237 ? 0.7215 0.8640 0.6574 0.0798  0.0781  0.0101  241 TRP B CB  
12611 C CG  . TRP B 237 ? 0.6337 0.7799 0.6063 0.0638  0.0665  0.0155  241 TRP B CG  
12612 C CD1 . TRP B 237 ? 0.6151 0.7484 0.6002 0.0663  0.0610  0.0098  241 TRP B CD1 
12613 C CD2 . TRP B 237 ? 0.5795 0.7390 0.5757 0.0446  0.0592  0.0273  241 TRP B CD2 
12614 N NE1 . TRP B 237 ? 0.5929 0.7321 0.6069 0.0500  0.0513  0.0168  241 TRP B NE1 
12615 C CE2 . TRP B 237 ? 0.5683 0.7217 0.5888 0.0373  0.0501  0.0270  241 TRP B CE2 
12616 C CE3 . TRP B 237 ? 0.5872 0.7596 0.5828 0.0345  0.0597  0.0384  241 TRP B CE3 
12617 C CZ2 . TRP B 237 ? 0.5731 0.7311 0.6149 0.0218  0.0422  0.0359  241 TRP B CZ2 
12618 C CZ3 . TRP B 237 ? 0.5871 0.7627 0.6054 0.0189  0.0513  0.0481  241 TRP B CZ3 
12619 C CH2 . TRP B 237 ? 0.5875 0.7548 0.6274 0.0134  0.0429  0.0460  241 TRP B CH2 
12630 N N   . ARG B 238 ? 0.9861 1.1699 0.8699 0.1006  0.1109  0.0233  242 ARG B N   
12631 C CA  . ARG B 238 ? 1.1294 1.2991 0.9624 0.1173  0.1210  0.0153  242 ARG B CA  
12632 C C   . ARG B 238 ? 1.1384 1.2609 0.9305 0.1067  0.1026  0.0007  242 ARG B C   
12633 O O   . ARG B 238 ? 1.0850 1.2033 0.8932 0.0847  0.0860  0.0048  242 ARG B O   
12634 C CB  . ARG B 238 ? 1.2061 1.4160 1.0410 0.1177  0.1364  0.0332  242 ARG B CB  
12635 C CG  . ARG B 238 ? 1.2367 1.4522 1.0825 0.0924  0.1248  0.0460  242 ARG B CG  
12636 C CD  . ARG B 238 ? 1.3380 1.5934 1.1882 0.0918  0.1411  0.0668  242 ARG B CD  
12637 N NE  . ARG B 238 ? 1.4586 1.7257 1.3380 0.0671  0.1315  0.0841  242 ARG B NE  
12638 C CZ  . ARG B 238 ? 1.6869 1.9836 1.5744 0.0592  0.1415  0.1053  242 ARG B CZ  
12639 N NH1 . ARG B 238 ? 1.8182 2.1427 1.6894 0.0738  0.1629  0.1132  242 ARG B NH1 
12640 N NH2 . ARG B 238 ? 1.7384 2.0352 1.6481 0.0376  0.1307  0.1195  242 ARG B NH2 
12654 N N   . ASN B 239 ? 1.1843 1.2709 0.9220 0.1231  0.1052  -0.0161 243 ASN B N   
12655 C CA  . ASN B 239 ? 1.2337 1.2759 0.9288 0.1107  0.0859  -0.0296 243 ASN B CA  
12656 C C   . ASN B 239 ? 1.1823 1.2434 0.8778 0.0933  0.0788  -0.0170 243 ASN B C   
12657 O O   . ASN B 239 ? 1.1984 1.3009 0.9207 0.0925  0.0908  0.0013  243 ASN B O   
12658 C CB  . ASN B 239 ? 1.4563 1.4553 1.0826 0.1304  0.0905  -0.0485 243 ASN B CB  
12659 C CG  . ASN B 239 ? 1.6653 1.6348 1.2777 0.1526  0.0979  -0.0626 243 ASN B CG  
12660 O OD1 . ASN B 239 ? 1.7067 1.6944 1.3627 0.1565  0.1023  -0.0571 243 ASN B OD1 
12661 N ND2 . ASN B 239 ? 1.8517 1.7705 1.3965 0.1686  0.0986  -0.0815 243 ASN B ND2 
12667 N N   . ASP B 240 ? 1.1477 1.1781 0.8117 0.0792  0.0587  -0.0258 244 ASP B N   
12668 C CA  . ASP B 240 ? 1.1344 1.1749 0.7814 0.0681  0.0513  -0.0168 244 ASP B CA  
12669 C C   . ASP B 240 ? 1.0258 1.1122 0.7204 0.0600  0.0580  0.0070  244 ASP B C   
12670 O O   . ASP B 240 ? 0.9904 1.0978 0.6738 0.0638  0.0687  0.0196  244 ASP B O   
12671 C CB  . ASP B 240 ? 1.2480 1.2740 0.8331 0.0852  0.0622  -0.0242 244 ASP B CB  
12672 C CG  . ASP B 240 ? 1.3967 1.3657 0.9222 0.0875  0.0485  -0.0486 244 ASP B CG  
12673 O OD1 . ASP B 240 ? 1.4303 1.3782 0.9528 0.0658  0.0231  -0.0541 244 ASP B OD1 
12674 O OD2 . ASP B 240 ? 1.4879 1.4329 0.9687 0.1111  0.0630  -0.0615 244 ASP B OD2 
12679 N N   . SER B 241 ? 0.9455 1.0438 0.6907 0.0486  0.0516  0.0135  245 SER B N   
12680 C CA  . SER B 241 ? 0.8753 1.0049 0.6614 0.0379  0.0528  0.0342  245 SER B CA  
12681 C C   . SER B 241 ? 0.8091 0.9338 0.6313 0.0239  0.0371  0.0344  245 SER B C   
12682 O O   . SER B 241 ? 0.8087 0.9125 0.6306 0.0227  0.0287  0.0207  245 SER B O   
12683 C CB  . SER B 241 ? 0.8569 1.0182 0.6707 0.0460  0.0739  0.0466  245 SER B CB  
12684 O OG  . SER B 241 ? 0.8286 0.9933 0.6794 0.0459  0.0744  0.0435  245 SER B OG  
12690 N N   . LEU B 242 ? 0.7793 0.9213 0.6300 0.0140  0.0338  0.0509  246 LEU B N   
12691 C CA  . LEU B 242 ? 0.7536 0.8934 0.6386 0.0043  0.0223  0.0528  246 LEU B CA  
12692 C C   . LEU B 242 ? 0.7266 0.8722 0.6431 0.0072  0.0310  0.0514  246 LEU B C   
12693 O O   . LEU B 242 ? 0.7695 0.9322 0.6951 0.0124  0.0453  0.0582  246 LEU B O   
12694 C CB  . LEU B 242 ? 0.7389 0.8897 0.6389 -0.0033 0.0170  0.0704  246 LEU B CB  
12695 C CG  . LEU B 242 ? 0.7619 0.9079 0.6575 -0.0098 -0.0010 0.0719  246 LEU B CG  
12696 C CD1 . LEU B 242 ? 0.7750 0.9297 0.6870 -0.0121 -0.0029 0.0906  246 LEU B CD1 
12697 C CD2 . LEU B 242 ? 0.7964 0.9338 0.7088 -0.0141 -0.0113 0.0613  246 LEU B CD2 
12709 N N   . HIS B 243 ? 0.6705 0.8045 0.6041 0.0032  0.0219  0.0441  247 HIS B N   
12710 C CA  . HIS B 243 ? 0.5753 0.7120 0.5363 0.0056  0.0270  0.0421  247 HIS B CA  
12711 C C   . HIS B 243 ? 0.5196 0.6566 0.5085 -0.0035 0.0187  0.0493  247 HIS B C   
12712 O O   . HIS B 243 ? 0.5079 0.6335 0.5002 -0.0072 0.0086  0.0438  247 HIS B O   
12713 C CB  . HIS B 243 ? 0.5768 0.6940 0.5259 0.0119  0.0253  0.0258  247 HIS B CB  
12714 C CG  . HIS B 243 ? 0.6552 0.7634 0.5689 0.0241  0.0333  0.0164  247 HIS B CG  
12715 N ND1 . HIS B 243 ? 0.6957 0.7729 0.5773 0.0262  0.0260  0.0010  247 HIS B ND1 
12716 C CD2 . HIS B 243 ? 0.6868 0.8110 0.5892 0.0355  0.0484  0.0205  247 HIS B CD2 
12717 C CE1 . HIS B 243 ? 0.7482 0.8179 0.5963 0.0405  0.0362  -0.0058 247 HIS B CE1 
12718 N NE2 . HIS B 243 ? 0.7277 0.8288 0.5889 0.0475  0.0511  0.0063  247 HIS B NE2 
12727 N N   . LEU B 244 ? 0.5452 0.6937 0.5520 -0.0071 0.0232  0.0622  248 LEU B N   
12728 C CA  . LEU B 244 ? 0.5686 0.7112 0.5949 -0.0131 0.0164  0.0690  248 LEU B CA  
12729 C C   . LEU B 244 ? 0.5822 0.7250 0.6301 -0.0140 0.0190  0.0670  248 LEU B C   
12730 O O   . LEU B 244 ? 0.5937 0.7493 0.6512 -0.0162 0.0261  0.0734  248 LEU B O   
12731 C CB  . LEU B 244 ? 0.5786 0.7239 0.6033 -0.0176 0.0170  0.0846  248 LEU B CB  
12732 C CG  . LEU B 244 ? 0.6014 0.7481 0.6037 -0.0162 0.0130  0.0888  248 LEU B CG  
12733 C CD1 . LEU B 244 ? 0.6160 0.7625 0.6157 -0.0197 0.0146  0.1061  248 LEU B CD1 
12734 C CD2 . LEU B 244 ? 0.5710 0.7118 0.5722 -0.0152 0.0008  0.0836  248 LEU B CD2 
12746 N N   . LEU B 245 ? 0.5619 0.6932 0.6176 -0.0133 0.0128  0.0595  249 LEU B N   
12747 C CA  . LEU B 245 ? 0.5195 0.6480 0.5924 -0.0141 0.0128  0.0574  249 LEU B CA  
12748 C C   . LEU B 245 ? 0.5551 0.6707 0.6350 -0.0183 0.0070  0.0635  249 LEU B C   
12749 O O   . LEU B 245 ? 0.5758 0.6824 0.6535 -0.0156 0.0020  0.0615  249 LEU B O   
12750 C CB  . LEU B 245 ? 0.4528 0.5738 0.5248 -0.0089 0.0109  0.0453  249 LEU B CB  
12751 C CG  . LEU B 245 ? 0.4911 0.6101 0.5779 -0.0081 0.0103  0.0431  249 LEU B CG  
12752 C CD1 . LEU B 245 ? 0.4710 0.6092 0.5682 -0.0074 0.0166  0.0476  249 LEU B CD1 
12753 C CD2 . LEU B 245 ? 0.5400 0.6476 0.6218 -0.0028 0.0083  0.0327  249 LEU B CD2 
12765 N N   . VAL B 246 ? 0.5378 0.6521 0.6248 -0.0247 0.0077  0.0716  250 VAL B N   
12766 C CA  . VAL B 246 ? 0.5175 0.6109 0.6033 -0.0277 0.0024  0.0773  250 VAL B CA  
12767 C C   . VAL B 246 ? 0.5751 0.6577 0.6685 -0.0292 -0.0014 0.0715  250 VAL B C   
12768 O O   . VAL B 246 ? 0.6424 0.7310 0.7446 -0.0372 -0.0020 0.0737  250 VAL B O   
12769 C CB  . VAL B 246 ? 0.5372 0.6267 0.6192 -0.0364 0.0033  0.0904  250 VAL B CB  
12770 C CG1 . VAL B 246 ? 0.5828 0.6409 0.6557 -0.0364 -0.0025 0.0952  250 VAL B CG1 
12771 C CG2 . VAL B 246 ? 0.5571 0.6607 0.6294 -0.0344 0.0080  0.0965  250 VAL B CG2 
12781 N N   . PHE B 247 ? 0.5970 0.6667 0.6871 -0.0219 -0.0043 0.0655  251 PHE B N   
12782 C CA  . PHE B 247 ? 0.5349 0.5917 0.6268 -0.0212 -0.0078 0.0595  251 PHE B CA  
12783 C C   . PHE B 247 ? 0.5474 0.5754 0.6279 -0.0225 -0.0122 0.0635  251 PHE B C   
12784 O O   . PHE B 247 ? 0.6086 0.6232 0.6795 -0.0135 -0.0115 0.0656  251 PHE B O   
12785 C CB  . PHE B 247 ? 0.5039 0.5625 0.5958 -0.0125 -0.0069 0.0523  251 PHE B CB  
12786 C CG  . PHE B 247 ? 0.5115 0.5563 0.6014 -0.0099 -0.0096 0.0471  251 PHE B CG  
12787 C CD1 . PHE B 247 ? 0.5497 0.5743 0.6290 -0.0037 -0.0105 0.0479  251 PHE B CD1 
12788 C CD2 . PHE B 247 ? 0.5250 0.5764 0.6208 -0.0110 -0.0105 0.0417  251 PHE B CD2 
12789 C CE1 . PHE B 247 ? 0.5687 0.5793 0.6414 -0.0002 -0.0122 0.0429  251 PHE B CE1 
12790 C CE2 . PHE B 247 ? 0.5298 0.5683 0.6210 -0.0084 -0.0135 0.0376  251 PHE B CE2 
12791 C CZ  . PHE B 247 ? 0.5513 0.5691 0.6299 -0.0036 -0.0143 0.0379  251 PHE B CZ  
12801 N N   . VAL B 248 ? 0.5732 0.5910 0.6535 -0.0333 -0.0172 0.0652  252 VAL B N   
12802 C CA  . VAL B 248 ? 0.6058 0.5877 0.6691 -0.0377 -0.0232 0.0685  252 VAL B CA  
12803 C C   . VAL B 248 ? 0.5849 0.5477 0.6401 -0.0375 -0.0295 0.0602  252 VAL B C   
12804 O O   . VAL B 248 ? 0.5816 0.5561 0.6467 -0.0480 -0.0347 0.0586  252 VAL B O   
12805 C CB  . VAL B 248 ? 0.6116 0.5923 0.6769 -0.0553 -0.0266 0.0788  252 VAL B CB  
12806 C CG1 . VAL B 248 ? 0.6212 0.5541 0.6624 -0.0609 -0.0343 0.0819  252 VAL B CG1 
12807 C CG2 . VAL B 248 ? 0.6384 0.6413 0.7099 -0.0546 -0.0192 0.0874  252 VAL B CG2 
12817 N N   . SER B 249 ? 0.5929 0.5283 0.6292 -0.0242 -0.0288 0.0558  253 SER B N   
12818 C CA  . SER B 249 ? 0.6254 0.5386 0.6471 -0.0214 -0.0338 0.0476  253 SER B CA  
12819 C C   . SER B 249 ? 0.6508 0.5229 0.6431 -0.0071 -0.0325 0.0461  253 SER B C   
12820 O O   . SER B 249 ? 0.6744 0.5440 0.6636 0.0041  -0.0262 0.0516  253 SER B O   
12821 C CB  . SER B 249 ? 0.6090 0.5472 0.6428 -0.0132 -0.0294 0.0416  253 SER B CB  
12822 O OG  . SER B 249 ? 0.6431 0.5594 0.6596 -0.0098 -0.0339 0.0347  253 SER B OG  
12828 N N   . ASP B 250 ? 0.6444 0.4839 0.6129 -0.0061 -0.0386 0.0388  254 ASP B N   
12829 C CA  . ASP B 250 ? 0.7130 0.5099 0.6475 0.0120  -0.0358 0.0352  254 ASP B CA  
12830 C C   . ASP B 250 ? 0.6916 0.4896 0.6167 0.0254  -0.0316 0.0274  254 ASP B C   
12831 O O   . ASP B 250 ? 0.7222 0.4789 0.6122 0.0344  -0.0338 0.0209  254 ASP B O   
12832 C CB  . ASP B 250 ? 0.7934 0.5346 0.6943 0.0015  -0.0476 0.0334  254 ASP B CB  
12833 C CG  . ASP B 250 ? 0.8849 0.6131 0.7761 -0.0160 -0.0615 0.0261  254 ASP B CG  
12834 O OD1 . ASP B 250 ? 0.8611 0.6257 0.7736 -0.0185 -0.0612 0.0234  254 ASP B OD1 
12835 O OD2 . ASP B 250 ? 0.9552 0.6345 0.8156 -0.0278 -0.0740 0.0235  254 ASP B OD2 
12840 N N   . ALA B 251 ? 0.6697 0.5117 0.6223 0.0270  -0.0254 0.0282  255 ALA B N   
12841 C CA  . ALA B 251 ? 0.7131 0.5573 0.6576 0.0359  -0.0222 0.0227  255 ALA B CA  
12842 C C   . ALA B 251 ? 0.7379 0.6253 0.7095 0.0422  -0.0118 0.0270  255 ALA B C   
12843 O O   . ALA B 251 ? 0.6962 0.6134 0.6940 0.0356  -0.0102 0.0319  255 ALA B O   
12844 C CB  . ALA B 251 ? 0.7166 0.5560 0.6581 0.0205  -0.0346 0.0170  255 ALA B CB  
12850 N N   . ASP B 252 ? 0.8356 0.7231 0.7968 0.0543  -0.0053 0.0252  256 ASP B N   
12851 C CA  . ASP B 252 ? 0.8681 0.7906 0.8501 0.0567  0.0026  0.0294  256 ASP B CA  
12852 C C   . ASP B 252 ? 0.7301 0.6734 0.7340 0.0405  -0.0040 0.0281  256 ASP B C   
12853 O O   . ASP B 252 ? 0.7612 0.6954 0.7642 0.0295  -0.0139 0.0243  256 ASP B O   
12854 C CB  . ASP B 252 ? 1.0463 0.9579 1.0068 0.0693  0.0088  0.0277  256 ASP B CB  
12855 C CG  . ASP B 252 ? 1.2312 1.1758 1.2083 0.0768  0.0213  0.0362  256 ASP B CG  
12856 O OD1 . ASP B 252 ? 1.3191 1.2940 1.3245 0.0691  0.0223  0.0420  256 ASP B OD1 
12857 O OD2 . ASP B 252 ? 1.3293 1.2693 1.2895 0.0895  0.0298  0.0378  256 ASP B OD2 
12862 N N   . SER B 253 ? 0.5974 0.5679 0.6201 0.0390  0.0011  0.0319  257 SER B N   
12863 C CA  . SER B 253 ? 0.6104 0.5950 0.6487 0.0278  -0.0038 0.0302  257 SER B CA  
12864 C C   . SER B 253 ? 0.6365 0.6248 0.6728 0.0295  -0.0009 0.0312  257 SER B C   
12865 O O   . SER B 253 ? 0.6419 0.6403 0.6802 0.0339  0.0071  0.0368  257 SER B O   
12866 C CB  . SER B 253 ? 0.6060 0.6125 0.6644 0.0216  -0.0025 0.0333  257 SER B CB  
12867 O OG  . SER B 253 ? 0.6365 0.6402 0.6969 0.0179  -0.0059 0.0334  257 SER B OG  
12873 N N   . HIS B 254 ? 0.6457 0.6278 0.6789 0.0258  -0.0075 0.0275  258 HIS B N   
12874 C CA  . HIS B 254 ? 0.5983 0.5816 0.6296 0.0264  -0.0059 0.0294  258 HIS B CA  
12875 C C   . HIS B 254 ? 0.5354 0.5334 0.5829 0.0204  -0.0030 0.0322  258 HIS B C   
12876 O O   . HIS B 254 ? 0.5171 0.5240 0.5764 0.0157  -0.0050 0.0303  258 HIS B O   
12877 C CB  . HIS B 254 ? 0.5613 0.5367 0.5872 0.0254  -0.0150 0.0258  258 HIS B CB  
12878 C CG  . HIS B 254 ? 0.5660 0.5231 0.5686 0.0305  -0.0188 0.0241  258 HIS B CG  
12879 N ND1 . HIS B 254 ? 0.5741 0.5219 0.5586 0.0382  -0.0112 0.0270  258 HIS B ND1 
12880 C CD2 . HIS B 254 ? 0.5650 0.5120 0.5574 0.0284  -0.0301 0.0201  258 HIS B CD2 
12881 C CE1 . HIS B 254 ? 0.6102 0.5386 0.5702 0.0423  -0.0171 0.0234  258 HIS B CE1 
12882 N NE2 . HIS B 254 ? 0.5878 0.5145 0.5520 0.0351  -0.0301 0.0190  258 HIS B NE2 
12891 N N   . PHE B 255 ? 0.5296 0.5275 0.5744 0.0193  0.0012  0.0371  259 PHE B N   
12892 C CA  . PHE B 255 ? 0.5118 0.5160 0.5662 0.0108  0.0015  0.0393  259 PHE B CA  
12893 C C   . PHE B 255 ? 0.5210 0.5126 0.5660 0.0086  0.0020  0.0432  259 PHE B C   
12894 O O   . PHE B 255 ? 0.5325 0.5186 0.5664 0.0133  0.0054  0.0475  259 PHE B O   
12895 C CB  . PHE B 255 ? 0.5245 0.5478 0.5904 0.0061  0.0063  0.0455  259 PHE B CB  
12896 C CG  . PHE B 255 ? 0.5755 0.6081 0.6393 0.0102  0.0145  0.0545  259 PHE B CG  
12897 C CD1 . PHE B 255 ? 0.6016 0.6345 0.6582 0.0228  0.0195  0.0547  259 PHE B CD1 
12898 C CD2 . PHE B 255 ? 0.6035 0.6433 0.6705 0.0018  0.0177  0.0635  259 PHE B CD2 
12899 C CE1 . PHE B 255 ? 0.6189 0.6618 0.6713 0.0306  0.0295  0.0633  259 PHE B CE1 
12900 C CE2 . PHE B 255 ? 0.6349 0.6897 0.7021 0.0064  0.0275  0.0741  259 PHE B CE2 
12901 C CZ  . PHE B 255 ? 0.6362 0.6940 0.6960 0.0227  0.0344  0.0738  259 PHE B CZ  
12911 N N   . GLY B 256 ? 0.4873 0.4705 0.5329 0.0020  -0.0015 0.0416  260 GLY B N   
12912 C CA  . GLY B 256 ? 0.5483 0.5135 0.5828 -0.0024 -0.0018 0.0463  260 GLY B CA  
12913 C C   . GLY B 256 ? 0.5970 0.5477 0.6172 0.0067  -0.0024 0.0482  260 GLY B C   
12914 O O   . GLY B 256 ? 0.5840 0.5288 0.6009 0.0159  -0.0074 0.0424  260 GLY B O   
12918 N N   . MET B 257 ? 0.5828 0.5310 0.5949 0.0040  0.0028  0.0577  261 MET B N   
12919 C CA  . MET B 257 ? 0.6024 0.5334 0.5960 0.0112  0.0021  0.0615  261 MET B CA  
12920 C C   . MET B 257 ? 0.5655 0.5023 0.5506 0.0224  0.0031  0.0596  261 MET B C   
12921 O O   . MET B 257 ? 0.5707 0.4958 0.5373 0.0280  0.0034  0.0642  261 MET B O   
12922 C CB  . MET B 257 ? 0.6590 0.5826 0.6445 0.0017  0.0078  0.0744  261 MET B CB  
12923 C CG  . MET B 257 ? 0.7006 0.6055 0.6854 -0.0114 0.0036  0.0763  261 MET B CG  
12924 S SD  . MET B 257 ? 0.7174 0.6440 0.7235 -0.0288 0.0040  0.0765  261 MET B SD  
12925 C CE  . MET B 257 ? 0.7297 0.6804 0.7429 -0.0409 0.0140  0.0952  261 MET B CE  
12935 N N   . ASP B 258 ? 0.5499 0.5005 0.5440 0.0253  0.0029  0.0530  262 ASP B N   
12936 C CA  . ASP B 258 ? 0.5745 0.5207 0.5547 0.0346  0.0001  0.0487  262 ASP B CA  
12937 C C   . ASP B 258 ? 0.6388 0.5727 0.6096 0.0392  -0.0109 0.0454  262 ASP B C   
12938 O O   . ASP B 258 ? 0.6659 0.5899 0.6166 0.0453  -0.0145 0.0454  262 ASP B O   
12939 C CB  . ASP B 258 ? 0.5728 0.5284 0.5630 0.0350  -0.0014 0.0417  262 ASP B CB  
12940 C CG  . ASP B 258 ? 0.5931 0.5612 0.5879 0.0361  0.0093  0.0461  262 ASP B CG  
12941 O OD1 . ASP B 258 ? 0.6306 0.6056 0.6241 0.0355  0.0183  0.0552  262 ASP B OD1 
12942 O OD2 . ASP B 258 ? 0.5758 0.5484 0.5763 0.0377  0.0089  0.0419  262 ASP B OD2 
12947 N N   . SER B 259 ? 0.6302 0.5652 0.6139 0.0376  -0.0163 0.0432  263 SER B N   
12948 C CA  . SER B 259 ? 0.6128 0.5434 0.5928 0.0444  -0.0265 0.0419  263 SER B CA  
12949 C C   . SER B 259 ? 0.5932 0.5059 0.5523 0.0499  -0.0274 0.0492  263 SER B C   
12950 O O   . SER B 259 ? 0.6629 0.5732 0.6163 0.0576  -0.0369 0.0499  263 SER B O   
12951 C CB  . SER B 259 ? 0.6469 0.5832 0.6438 0.0454  -0.0285 0.0390  263 SER B CB  
12952 O OG  . SER B 259 ? 0.6782 0.5990 0.6706 0.0429  -0.0231 0.0423  263 SER B OG  
12958 N N   . LYS B 260 ? 0.5998 0.5027 0.5485 0.0458  -0.0182 0.0566  264 LYS B N   
12959 C CA  . LYS B 260 ? 0.6189 0.5032 0.5453 0.0499  -0.0181 0.0657  264 LYS B CA  
12960 C C   . LYS B 260 ? 0.6101 0.4921 0.5158 0.0581  -0.0240 0.0652  264 LYS B C   
12961 O O   . LYS B 260 ? 0.5893 0.4580 0.4774 0.0650  -0.0300 0.0707  264 LYS B O   
12962 C CB  . LYS B 260 ? 0.5672 0.4477 0.4886 0.0409  -0.0059 0.0757  264 LYS B CB  
12963 C CG  . LYS B 260 ? 0.6111 0.4716 0.5083 0.0426  -0.0037 0.0879  264 LYS B CG  
12964 C CD  . LYS B 260 ? 0.6844 0.5482 0.5834 0.0296  0.0088  0.0998  264 LYS B CD  
12965 C CE  . LYS B 260 ? 0.7689 0.6182 0.6424 0.0303  0.0143  0.1146  264 LYS B CE  
12966 N NZ  . LYS B 260 ? 0.8507 0.6683 0.7124 0.0276  0.0080  0.1214  264 LYS B NZ  
12980 N N   . LEU B 261 ? 0.5663 0.4573 0.4700 0.0579  -0.0234 0.0587  265 LEU B N   
12981 C CA  . LEU B 261 ? 0.5881 0.4711 0.4668 0.0643  -0.0316 0.0559  265 LEU B CA  
12982 C C   . LEU B 261 ? 0.6049 0.4908 0.4876 0.0675  -0.0488 0.0536  265 LEU B C   
12983 O O   . LEU B 261 ? 0.6443 0.5209 0.5038 0.0732  -0.0581 0.0562  265 LEU B O   
12984 C CB  . LEU B 261 ? 0.6265 0.5120 0.5012 0.0632  -0.0300 0.0474  265 LEU B CB  
12985 C CG  . LEU B 261 ? 0.7226 0.6108 0.5942 0.0643  -0.0127 0.0502  265 LEU B CG  
12986 C CD1 . LEU B 261 ? 0.7769 0.6573 0.6332 0.0685  -0.0133 0.0413  265 LEU B CD1 
12987 C CD2 . LEU B 261 ? 0.8027 0.6840 0.6524 0.0693  -0.0017 0.0613  265 LEU B CD2 
12999 N N   . ALA B 262 ? 0.5742 0.4761 0.4860 0.0647  -0.0532 0.0498  266 ALA B N   
13000 C CA  . ALA B 262 ? 0.5893 0.5043 0.5123 0.0685  -0.0681 0.0493  266 ALA B CA  
13001 C C   . ALA B 262 ? 0.6594 0.5694 0.5835 0.0788  -0.0693 0.0571  266 ALA B C   
13002 O O   . ALA B 262 ? 0.6906 0.6163 0.6279 0.0857  -0.0798 0.0586  266 ALA B O   
13003 C CB  . ALA B 262 ? 0.5389 0.4768 0.4924 0.0624  -0.0702 0.0432  266 ALA B CB  
13009 N N   . GLY B 263 ? 0.6689 0.5575 0.5793 0.0801  -0.0588 0.0633  267 GLY B N   
13010 C CA  . GLY B 263 ? 0.7036 0.5776 0.6099 0.0897  -0.0595 0.0707  267 GLY B CA  
13011 C C   . GLY B 263 ? 0.7287 0.6035 0.6551 0.0910  -0.0547 0.0674  267 GLY B C   
13012 O O   . GLY B 263 ? 0.7727 0.6335 0.6947 0.1028  -0.0567 0.0718  267 GLY B O   
13016 N N   . ILE B 264 ? 0.6988 0.5867 0.6433 0.0810  -0.0484 0.0598  268 ILE B N   
13017 C CA  . ILE B 264 ? 0.6820 0.5697 0.6413 0.0816  -0.0437 0.0553  268 ILE B CA  
13018 C C   . ILE B 264 ? 0.6687 0.5334 0.6184 0.0700  -0.0342 0.0573  268 ILE B C   
13019 O O   . ILE B 264 ? 0.6586 0.5315 0.6117 0.0576  -0.0284 0.0568  268 ILE B O   
13020 C CB  . ILE B 264 ? 0.6638 0.5819 0.6480 0.0769  -0.0441 0.0472  268 ILE B CB  
13021 C CG1 . ILE B 264 ? 0.6363 0.5805 0.6319 0.0836  -0.0554 0.0476  268 ILE B CG1 
13022 C CG2 . ILE B 264 ? 0.6860 0.6031 0.6808 0.0791  -0.0385 0.0424  268 ILE B CG2 
13023 C CD1 . ILE B 264 ? 0.5913 0.5643 0.6094 0.0751  -0.0568 0.0420  268 ILE B CD1 
13035 N N   . VAL B 265 ? 0.6571 0.4926 0.5943 0.0740  -0.0331 0.0602  269 VAL B N   
13036 C CA  . VAL B 265 ? 0.6601 0.4702 0.5852 0.0594  -0.0269 0.0647  269 VAL B CA  
13037 C C   . VAL B 265 ? 0.7281 0.5104 0.6462 0.0606  -0.0270 0.0603  269 VAL B C   
13038 O O   . VAL B 265 ? 0.8253 0.5724 0.7245 0.0513  -0.0260 0.0658  269 VAL B O   
13039 C CB  . VAL B 265 ? 0.6619 0.4494 0.5639 0.0582  -0.0264 0.0774  269 VAL B CB  
13040 C CG1 . VAL B 265 ? 0.6455 0.4566 0.5483 0.0554  -0.0241 0.0808  269 VAL B CG1 
13041 C CG2 . VAL B 265 ? 0.6657 0.4314 0.5516 0.0775  -0.0335 0.0813  269 VAL B CG2 
13051 N N   . CYS B 266 ? 0.7043 0.4999 0.6347 0.0714  -0.0281 0.0507  270 CYS B N   
13052 C CA  . CYS B 266 ? 0.7922 0.5611 0.7121 0.0739  -0.0270 0.0439  270 CYS B CA  
13053 C C   . CYS B 266 ? 0.7754 0.5677 0.7125 0.0615  -0.0239 0.0355  270 CYS B C   
13054 O O   . CYS B 266 ? 0.7543 0.5834 0.7128 0.0672  -0.0231 0.0312  270 CYS B O   
13055 C CB  . CYS B 266 ? 0.8618 0.6260 0.7777 0.1009  -0.0288 0.0409  270 CYS B CB  
13056 S SG  . CYS B 266 ? 1.0252 0.7703 0.9242 0.1191  -0.0342 0.0528  270 CYS B SG  
13061 N N   . PRO B 267 ? 0.7705 0.5439 0.6989 0.0431  -0.0232 0.0342  271 PRO B N   
13062 C CA  . PRO B 267 ? 0.7184 0.5190 0.6642 0.0300  -0.0213 0.0287  271 PRO B CA  
13063 C C   . PRO B 267 ? 0.6765 0.4902 0.6285 0.0433  -0.0199 0.0184  271 PRO B C   
13064 O O   . PRO B 267 ? 0.7420 0.5338 0.6788 0.0604  -0.0197 0.0137  271 PRO B O   
13065 C CB  . PRO B 267 ? 0.7650 0.5371 0.6957 0.0086  -0.0238 0.0302  271 PRO B CB  
13066 C CG  . PRO B 267 ? 0.7971 0.5368 0.7092 0.0049  -0.0253 0.0403  271 PRO B CG  
13067 C CD  . PRO B 267 ? 0.8090 0.5363 0.7116 0.0308  -0.0256 0.0394  271 PRO B CD  
13075 N N   . ASN B 268 ? 0.6048 0.4550 0.5785 0.0369  -0.0178 0.0159  272 ASN B N   
13076 C CA  . ASN B 268 ? 0.6139 0.4794 0.5936 0.0454  -0.0153 0.0079  272 ASN B CA  
13077 C C   . ASN B 268 ? 0.6729 0.5017 0.6261 0.0458  -0.0159 0.0002  272 ASN B C   
13078 O O   . ASN B 268 ? 0.6694 0.4699 0.6064 0.0294  -0.0201 0.0007  272 ASN B O   
13079 C CB  . ASN B 268 ? 0.6157 0.5160 0.6166 0.0332  -0.0139 0.0081  272 ASN B CB  
13080 C CG  . ASN B 268 ? 0.6211 0.5462 0.6331 0.0427  -0.0105 0.0034  272 ASN B CG  
13081 O OD1 . ASN B 268 ? 0.6278 0.5455 0.6292 0.0434  -0.0086 -0.0028 272 ASN B OD1 
13082 N ND2 . ASN B 268 ? 0.6348 0.5889 0.6662 0.0487  -0.0100 0.0070  272 ASN B ND2 
13089 N N   . ASP B 269 ? 0.7070 0.5360 0.6540 0.0645  -0.0119 -0.0067 273 ASP B N   
13090 C CA  . ASP B 269 ? 0.7671 0.5540 0.6807 0.0707  -0.0118 -0.0159 273 ASP B CA  
13091 C C   . ASP B 269 ? 0.7625 0.5624 0.6737 0.0678  -0.0090 -0.0238 273 ASP B C   
13092 O O   . ASP B 269 ? 0.8326 0.5959 0.7110 0.0735  -0.0090 -0.0333 273 ASP B O   
13093 C CB  . ASP B 269 ? 0.8587 0.6269 0.7573 0.1006  -0.0075 -0.0177 273 ASP B CB  
13094 C CG  . ASP B 269 ? 0.9206 0.7375 0.8444 0.1207  0.0002  -0.0165 273 ASP B CG  
13095 O OD1 . ASP B 269 ? 0.9441 0.8047 0.8954 0.1096  0.0015  -0.0141 273 ASP B OD1 
13096 O OD2 . ASP B 269 ? 0.9528 0.7649 0.8691 0.1479  0.0049  -0.0166 273 ASP B OD2 
13101 N N   . GLY B 270 ? 0.7096 0.5561 0.6501 0.0598  -0.0070 -0.0202 274 GLY B N   
13102 C CA  . GLY B 270 ? 0.7015 0.5609 0.6389 0.0560  -0.0047 -0.0258 274 GLY B CA  
13103 C C   . GLY B 270 ? 0.6929 0.5538 0.6177 0.0798  0.0041  -0.0321 274 GLY B C   
13104 O O   . GLY B 270 ? 0.7676 0.6221 0.6742 0.0793  0.0060  -0.0391 274 GLY B O   
13108 N N   . LEU B 271 ? 0.6474 0.5194 0.5813 0.1018  0.0099  -0.0288 275 LEU B N   
13109 C CA  . LEU B 271 ? 0.6989 0.5806 0.6253 0.1284  0.0207  -0.0321 275 LEU B CA  
13110 C C   . LEU B 271 ? 0.6843 0.6286 0.6517 0.1332  0.0267  -0.0221 275 LEU B C   
13111 O O   . LEU B 271 ? 0.6849 0.6549 0.6815 0.1210  0.0212  -0.0137 275 LEU B O   
13112 C CB  . LEU B 271 ? 0.7248 0.5718 0.6288 0.1535  0.0229  -0.0344 275 LEU B CB  
13113 C CG  . LEU B 271 ? 0.7682 0.5442 0.6273 0.1481  0.0156  -0.0433 275 LEU B CG  
13114 C CD1 . LEU B 271 ? 0.8110 0.5518 0.6479 0.1764  0.0185  -0.0438 275 LEU B CD1 
13115 C CD2 . LEU B 271 ? 0.8051 0.5519 0.6289 0.1433  0.0161  -0.0556 275 LEU B CD2 
13127 N N   . CYS B 272 ? 0.6897 0.6569 0.6565 0.1507  0.0379  -0.0227 276 CYS B N   
13128 C CA  . CYS B 272 ? 0.6732 0.7015 0.6790 0.1545  0.0438  -0.0113 276 CYS B CA  
13129 C C   . CYS B 272 ? 0.6759 0.7225 0.7009 0.1720  0.0434  -0.0035 276 CYS B C   
13130 O O   . CYS B 272 ? 0.7038 0.7238 0.7074 0.1959  0.0468  -0.0073 276 CYS B O   
13131 C CB  . CYS B 272 ? 0.7425 0.7940 0.7424 0.1691  0.0579  -0.0118 276 CYS B CB  
13132 S SG  . CYS B 272 ? 0.7746 0.9044 0.8246 0.1651  0.0643  0.0052  276 CYS B SG  
13137 N N   . HIS B 273 ? 0.5942 0.6838 0.6571 0.1600  0.0380  0.0077  277 HIS B N   
13138 C CA  . HIS B 273 ? 0.5777 0.6918 0.6623 0.1728  0.0343  0.0168  277 HIS B CA  
13139 C C   . HIS B 273 ? 0.5820 0.7600 0.7089 0.1634  0.0335  0.0300  277 HIS B C   
13140 O O   . HIS B 273 ? 0.6066 0.8011 0.7546 0.1495  0.0219  0.0368  277 HIS B O   
13141 C CB  . HIS B 273 ? 0.6338 0.7164 0.7118 0.1622  0.0213  0.0160  277 HIS B CB  
13142 C CG  . HIS B 273 ? 0.6980 0.7200 0.7371 0.1717  0.0210  0.0069  277 HIS B CG  
13143 N ND1 . HIS B 273 ? 0.7278 0.7307 0.7488 0.2011  0.0260  0.0058  277 HIS B ND1 
13144 C CD2 . HIS B 273 ? 0.6945 0.6703 0.7092 0.1546  0.0156  -0.0003 277 HIS B CD2 
13145 C CE1 . HIS B 273 ? 0.7614 0.7025 0.7451 0.2001  0.0229  -0.0025 277 HIS B CE1 
13146 N NE2 . HIS B 273 ? 0.7355 0.6622 0.7167 0.1706  0.0164  -0.0057 277 HIS B NE2 
13154 N N   . LEU B 274 ? 0.6186 0.8319 0.7560 0.1699  0.0454  0.0341  278 LEU B N   
13155 C CA  . LEU B 274 ? 0.6485 0.9251 0.8266 0.1602  0.0456  0.0490  278 LEU B CA  
13156 C C   . LEU B 274 ? 0.6982 1.0198 0.8972 0.1881  0.0527  0.0595  278 LEU B C   
13157 O O   . LEU B 274 ? 0.7391 1.0604 0.9226 0.2163  0.0680  0.0568  278 LEU B O   
13158 C CB  . LEU B 274 ? 0.6728 0.9660 0.8521 0.1486  0.0551  0.0506  278 LEU B CB  
13159 C CG  . LEU B 274 ? 0.6907 0.9485 0.8543 0.1220  0.0478  0.0433  278 LEU B CG  
13160 C CD1 . LEU B 274 ? 0.6909 0.9666 0.8538 0.1142  0.0577  0.0467  278 LEU B CD1 
13161 C CD2 . LEU B 274 ? 0.7084 0.9689 0.8911 0.0976  0.0320  0.0483  278 LEU B CD2 
13173 N N   . ASP B 275 ? 0.6504 1.0105 0.8827 0.1813  0.0413  0.0717  279 ASP B N   
13174 C CA  . ASP B 275 ? 0.6656 1.0736 0.9220 0.2079  0.0452  0.0840  279 ASP B CA  
13175 C C   . ASP B 275 ? 0.6140 1.0955 0.9072 0.2075  0.0562  0.0999  279 ASP B C   
13176 O O   . ASP B 275 ? 0.5242 1.0098 0.8151 0.1923  0.0641  0.0994  279 ASP B O   
13177 C CB  . ASP B 275 ? 0.6583 1.0757 0.9323 0.2005  0.0258  0.0907  279 ASP B CB  
13178 C CG  . ASP B 275 ? 0.6057 1.0512 0.9073 0.1627  0.0101  0.0990  279 ASP B CG  
13179 O OD1 . ASP B 275 ? 0.5991 1.0741 0.9176 0.1453  0.0153  0.1049  279 ASP B OD1 
13180 O OD2 . ASP B 275 ? 0.5875 1.0214 0.8901 0.1505  -0.0078 0.0995  279 ASP B OD2 
13185 N N   . SER B 276 ? 0.6902 1.2340 1.0190 0.2243  0.0568  0.1163  280 SER B N   
13186 C CA  . SER B 276 ? 0.7573 1.3799 1.1253 0.2253  0.0687  0.1348  280 SER B CA  
13187 C C   . SER B 276 ? 0.7433 1.3921 1.1377 0.1802  0.0573  0.1442  280 SER B C   
13188 O O   . SER B 276 ? 0.7499 1.4368 1.1597 0.1719  0.0697  0.1541  280 SER B O   
13189 C CB  . SER B 276 ? 0.8137 1.5035 1.2194 0.2507  0.0687  0.1528  280 SER B CB  
13190 O OG  . SER B 276 ? 0.8603 1.5359 1.2704 0.2437  0.0463  0.1527  280 SER B OG  
13196 N N   . LYS B 277 ? 0.7623 1.3878 1.1586 0.1515  0.0342  0.1416  281 LYS B N   
13197 C CA  . LYS B 277 ? 0.8067 1.4404 1.2182 0.1088  0.0213  0.1478  281 LYS B CA  
13198 C C   . LYS B 277 ? 0.7574 1.3311 1.1335 0.0929  0.0254  0.1330  281 LYS B C   
13199 O O   . LYS B 277 ? 0.7824 1.3475 1.1622 0.0595  0.0144  0.1356  281 LYS B O   
13200 C CB  . LYS B 277 ? 0.8923 1.5182 1.3122 0.0871  -0.0052 0.1491  281 LYS B CB  
13201 C CG  . LYS B 277 ? 0.9479 1.6463 1.4114 0.0921  -0.0146 0.1686  281 LYS B CG  
13202 C CD  . LYS B 277 ? 1.0286 1.7068 1.4873 0.0817  -0.0401 0.1657  281 LYS B CD  
13203 C CE  . LYS B 277 ? 1.1377 1.7890 1.5898 0.0377  -0.0605 0.1632  281 LYS B CE  
13204 N NZ  . LYS B 277 ? 1.2554 1.8855 1.6973 0.0293  -0.0849 0.1597  281 LYS B NZ  
13218 N N   . ASN B 278 ? 0.6967 1.2279 1.0373 0.1160  0.0401  0.1182  282 ASN B N   
13219 C CA  . ASN B 278 ? 0.6964 1.1706 1.0027 0.1027  0.0418  0.1040  282 ASN B CA  
13220 C C   . ASN B 278 ? 0.6118 1.0398 0.9053 0.0797  0.0223  0.0955  282 ASN B C   
13221 O O   . ASN B 278 ? 0.5722 0.9766 0.8565 0.0561  0.0175  0.0927  282 ASN B O   
13222 C CB  . ASN B 278 ? 0.7316 1.2312 1.0474 0.0852  0.0507  0.1133  282 ASN B CB  
13223 C CG  . ASN B 278 ? 0.7715 1.2795 1.0713 0.1104  0.0736  0.1114  282 ASN B CG  
13224 O OD1 . ASN B 278 ? 0.8276 1.3092 1.1017 0.1395  0.0819  0.0996  282 ASN B OD1 
13225 N ND2 . ASN B 278 ? 0.7458 1.2859 1.0564 0.0988  0.0837  0.1230  282 ASN B ND2 
13232 N N   . GLU B 279 ? 0.6326 1.0475 0.9236 0.0887  0.0117  0.0920  283 GLU B N   
13233 C CA  . GLU B 279 ? 0.6751 1.0442 0.9485 0.0730  -0.0042 0.0832  283 GLU B CA  
13234 C C   . GLU B 279 ? 0.6400 0.9574 0.8797 0.0921  -0.0006 0.0689  283 GLU B C   
13235 O O   . GLU B 279 ? 0.6502 0.9706 0.8851 0.1191  0.0074  0.0680  283 GLU B O   
13236 C CB  . GLU B 279 ? 0.7599 1.1539 1.0547 0.0634  -0.0221 0.0922  283 GLU B CB  
13237 C CG  . GLU B 279 ? 0.9231 1.3611 1.2487 0.0366  -0.0308 0.1064  283 GLU B CG  
13238 C CD  . GLU B 279 ? 1.0665 1.5115 1.4019 0.0195  -0.0536 0.1115  283 GLU B CD  
13239 O OE1 . GLU B 279 ? 1.1366 1.5454 1.4501 0.0268  -0.0621 0.1023  283 GLU B OE1 
13240 O OE2 . GLU B 279 ? 1.1182 1.6043 1.4814 -0.0026 -0.0638 0.1251  283 GLU B OE2 
13247 N N   . TYR B 280 ? 0.5537 0.8236 0.7697 0.0784  -0.0062 0.0588  284 TYR B N   
13248 C CA  . TYR B 280 ? 0.5878 0.8088 0.7733 0.0902  -0.0046 0.0473  284 TYR B CA  
13249 C C   . TYR B 280 ? 0.6114 0.8299 0.7973 0.1021  -0.0135 0.0500  284 TYR B C   
13250 O O   . TYR B 280 ? 0.6049 0.8220 0.7947 0.0888  -0.0267 0.0526  284 TYR B O   
13251 C CB  . TYR B 280 ? 0.6106 0.7930 0.7774 0.0713  -0.0089 0.0397  284 TYR B CB  
13252 C CG  . TYR B 280 ? 0.6402 0.7767 0.7793 0.0778  -0.0088 0.0308  284 TYR B CG  
13253 C CD1 . TYR B 280 ? 0.6585 0.7751 0.7793 0.0948  -0.0003 0.0249  284 TYR B CD1 
13254 C CD2 . TYR B 280 ? 0.6169 0.7282 0.7455 0.0665  -0.0170 0.0287  284 TYR B CD2 
13255 C CE1 . TYR B 280 ? 0.6591 0.7316 0.7541 0.0966  -0.0017 0.0183  284 TYR B CE1 
13256 C CE2 . TYR B 280 ? 0.5987 0.6725 0.7044 0.0699  -0.0164 0.0233  284 TYR B CE2 
13257 C CZ  . TYR B 280 ? 0.6417 0.6961 0.7317 0.0831  -0.0096 0.0186  284 TYR B CZ  
13258 O OH  . TYR B 280 ? 0.6916 0.7066 0.7585 0.0825  -0.0104 0.0147  284 TYR B OH  
13268 N N   . SER B 281 ? 0.6209 0.8354 0.7988 0.1285  -0.0064 0.0492  285 SER B N   
13269 C CA  . SER B 281 ? 0.6154 0.8362 0.7973 0.1440  -0.0141 0.0550  285 SER B CA  
13270 C C   . SER B 281 ? 0.6692 0.8371 0.8218 0.1426  -0.0210 0.0484  285 SER B C   
13271 O O   . SER B 281 ? 0.7120 0.8829 0.8668 0.1460  -0.0319 0.0540  285 SER B O   
13272 C CB  . SER B 281 ? 0.6223 0.8597 0.8062 0.1770  -0.0027 0.0583  285 SER B CB  
13273 O OG  . SER B 281 ? 0.6596 0.8490 0.8091 0.1898  0.0087  0.0466  285 SER B OG  
13279 N N   . MET B 282 ? 0.6509 0.7731 0.7764 0.1369  -0.0155 0.0382  286 MET B N   
13280 C CA  . MET B 282 ? 0.6494 0.7244 0.7486 0.1334  -0.0205 0.0342  286 MET B CA  
13281 C C   . MET B 282 ? 0.5766 0.6464 0.6763 0.1093  -0.0287 0.0340  286 MET B C   
13282 O O   . MET B 282 ? 0.5413 0.5754 0.6200 0.1033  -0.0302 0.0313  286 MET B O   
13283 C CB  . MET B 282 ? 0.6741 0.7042 0.7445 0.1363  -0.0120 0.0249  286 MET B CB  
13284 C CG  . MET B 282 ? 0.7180 0.7410 0.7773 0.1626  -0.0029 0.0225  286 MET B CG  
13285 S SD  . MET B 282 ? 0.8083 0.8206 0.8593 0.1916  -0.0064 0.0294  286 MET B SD  
13286 C CE  . MET B 282 ? 0.8465 0.7856 0.8564 0.1833  -0.0104 0.0242  286 MET B CE  
13296 N N   . SER B 283 ? 0.5293 0.6325 0.6508 0.0957  -0.0336 0.0375  287 SER B N   
13297 C CA  . SER B 283 ? 0.5185 0.6114 0.6351 0.0756  -0.0407 0.0362  287 SER B CA  
13298 C C   . SER B 283 ? 0.5141 0.5838 0.6129 0.0775  -0.0487 0.0376  287 SER B C   
13299 O O   . SER B 283 ? 0.5236 0.5671 0.6053 0.0680  -0.0483 0.0344  287 SER B O   
13300 C CB  . SER B 283 ? 0.5707 0.6985 0.7098 0.0623  -0.0481 0.0411  287 SER B CB  
13301 O OG  . SER B 283 ? 0.6730 0.7837 0.8013 0.0457  -0.0556 0.0388  287 SER B OG  
13307 N N   . THR B 284 ? 0.5168 0.5982 0.6194 0.0912  -0.0553 0.0436  288 THR B N   
13308 C CA  . THR B 284 ? 0.5588 0.6206 0.6430 0.0942  -0.0639 0.0466  288 THR B CA  
13309 C C   . THR B 284 ? 0.6067 0.6339 0.6692 0.1092  -0.0579 0.0469  288 THR B C   
13310 O O   . THR B 284 ? 0.6302 0.6419 0.6769 0.1155  -0.0644 0.0518  288 THR B O   
13311 C CB  . THR B 284 ? 0.5902 0.6857 0.6899 0.0992  -0.0779 0.0548  288 THR B CB  
13312 O OG1 . THR B 284 ? 0.6178 0.7379 0.7344 0.1199  -0.0741 0.0604  288 THR B OG1 
13313 C CG2 . THR B 284 ? 0.5634 0.6880 0.6816 0.0796  -0.0865 0.0554  288 THR B CG2 
13321 N N   . VAL B 285 ? 0.6303 0.6411 0.6878 0.1141  -0.0467 0.0421  289 VAL B N   
13322 C CA  . VAL B 285 ? 0.6347 0.6085 0.6696 0.1283  -0.0423 0.0424  289 VAL B CA  
13323 C C   . VAL B 285 ? 0.6101 0.5468 0.6256 0.1148  -0.0355 0.0369  289 VAL B C   
13324 O O   . VAL B 285 ? 0.6495 0.5488 0.6415 0.1158  -0.0352 0.0394  289 VAL B O   
13325 C CB  . VAL B 285 ? 0.6998 0.6833 0.7410 0.1509  -0.0367 0.0421  289 VAL B CB  
13326 C CG1 . VAL B 285 ? 0.7370 0.6713 0.7476 0.1667  -0.0332 0.0416  289 VAL B CG1 
13327 C CG2 . VAL B 285 ? 0.7088 0.7396 0.7755 0.1641  -0.0436 0.0505  289 VAL B CG2 
13337 N N   . LEU B 286 ? 0.6115 0.5592 0.6368 0.1010  -0.0306 0.0310  290 LEU B N   
13338 C CA  . LEU B 286 ? 0.6052 0.5260 0.6167 0.0877  -0.0253 0.0267  290 LEU B CA  
13339 C C   . LEU B 286 ? 0.6247 0.5565 0.6430 0.0690  -0.0255 0.0274  290 LEU B C   
13340 O O   . LEU B 286 ? 0.6404 0.5996 0.6746 0.0653  -0.0280 0.0274  290 LEU B O   
13341 C CB  . LEU B 286 ? 0.5804 0.5017 0.5930 0.0901  -0.0192 0.0194  290 LEU B CB  
13342 C CG  . LEU B 286 ? 0.5841 0.4893 0.5841 0.1125  -0.0164 0.0171  290 LEU B CG  
13343 C CD1 . LEU B 286 ? 0.5756 0.4799 0.5713 0.1148  -0.0095 0.0088  290 LEU B CD1 
13344 C CD2 . LEU B 286 ? 0.6155 0.4712 0.5859 0.1169  -0.0185 0.0189  290 LEU B CD2 
13356 N N   . GLU B 287 ? 0.6375 0.5469 0.6428 0.0575  -0.0229 0.0290  291 GLU B N   
13357 C CA  . GLU B 287 ? 0.6918 0.6125 0.7027 0.0433  -0.0207 0.0308  291 GLU B CA  
13358 C C   . GLU B 287 ? 0.6029 0.5463 0.6303 0.0374  -0.0184 0.0256  291 GLU B C   
13359 O O   . GLU B 287 ? 0.5630 0.5086 0.5937 0.0405  -0.0172 0.0208  291 GLU B O   
13360 C CB  . GLU B 287 ? 0.7701 0.6699 0.7686 0.0315  -0.0173 0.0356  291 GLU B CB  
13361 C CG  . GLU B 287 ? 0.8725 0.7459 0.8518 0.0353  -0.0188 0.0428  291 GLU B CG  
13362 C CD  . GLU B 287 ? 0.9863 0.8411 0.9553 0.0197  -0.0156 0.0498  291 GLU B CD  
13363 O OE1 . GLU B 287 ? 0.9996 0.8559 0.9740 0.0072  -0.0147 0.0474  291 GLU B OE1 
13364 O OE2 . GLU B 287 ? 1.0328 0.8732 0.9881 0.0187  -0.0147 0.0591  291 GLU B OE2 
13371 N N   . TYR B 288 ? 0.5848 0.5426 0.6191 0.0305  -0.0174 0.0271  292 TYR B N   
13372 C CA  . TYR B 288 ? 0.5771 0.5512 0.6236 0.0239  -0.0149 0.0243  292 TYR B CA  
13373 C C   . TYR B 288 ? 0.5603 0.5261 0.6035 0.0158  -0.0121 0.0238  292 TYR B C   
13374 O O   . TYR B 288 ? 0.5692 0.5195 0.6027 0.0104  -0.0115 0.0278  292 TYR B O   
13375 C CB  . TYR B 288 ? 0.5654 0.5482 0.6141 0.0200  -0.0134 0.0268  292 TYR B CB  
13376 C CG  . TYR B 288 ? 0.5939 0.5777 0.6390 0.0248  -0.0184 0.0264  292 TYR B CG  
13377 C CD1 . TYR B 288 ? 0.6001 0.5961 0.6547 0.0237  -0.0228 0.0237  292 TYR B CD1 
13378 C CD2 . TYR B 288 ? 0.6229 0.5943 0.6528 0.0286  -0.0196 0.0294  292 TYR B CD2 
13379 C CE1 . TYR B 288 ? 0.6230 0.6175 0.6722 0.0242  -0.0303 0.0234  292 TYR B CE1 
13380 C CE2 . TYR B 288 ? 0.6317 0.6010 0.6536 0.0315  -0.0265 0.0281  292 TYR B CE2 
13381 C CZ  . TYR B 288 ? 0.6394 0.6195 0.6711 0.0283  -0.0329 0.0248  292 TYR B CZ  
13382 O OH  . TYR B 288 ? 0.6661 0.6417 0.6878 0.0276  -0.0426 0.0236  292 TYR B OH  
13392 N N   . PRO B 289 ? 0.5634 0.5387 0.6128 0.0132  -0.0114 0.0197  293 PRO B N   
13393 C CA  . PRO B 289 ? 0.5631 0.5307 0.6070 0.0030  -0.0115 0.0190  293 PRO B CA  
13394 C C   . PRO B 289 ? 0.5547 0.5339 0.6056 -0.0076 -0.0100 0.0263  293 PRO B C   
13395 O O   . PRO B 289 ? 0.5344 0.5295 0.5943 -0.0047 -0.0073 0.0296  293 PRO B O   
13396 C CB  . PRO B 289 ? 0.5484 0.5277 0.5964 0.0043  -0.0110 0.0136  293 PRO B CB  
13397 C CG  . PRO B 289 ? 0.5668 0.5655 0.6277 0.0115  -0.0096 0.0143  293 PRO B CG  
13398 C CD  . PRO B 289 ? 0.5556 0.5484 0.6153 0.0185  -0.0112 0.0163  293 PRO B CD  
13406 N N   . THR B 290 ? 0.5820 0.5526 0.6276 -0.0199 -0.0120 0.0293  294 THR B N   
13407 C CA  . THR B 290 ? 0.6044 0.5949 0.6613 -0.0308 -0.0106 0.0383  294 THR B CA  
13408 C C   . THR B 290 ? 0.6631 0.6726 0.7289 -0.0359 -0.0132 0.0369  294 THR B C   
13409 O O   . THR B 290 ? 0.6816 0.6836 0.7406 -0.0336 -0.0160 0.0287  294 THR B O   
13410 C CB  . THR B 290 ? 0.6199 0.5967 0.6695 -0.0457 -0.0133 0.0450  294 THR B CB  
13411 O OG1 . THR B 290 ? 0.6091 0.5705 0.6486 -0.0576 -0.0211 0.0398  294 THR B OG1 
13412 C CG2 . THR B 290 ? 0.6519 0.6008 0.6861 -0.0400 -0.0122 0.0455  294 THR B CG2 
13420 N N   . ILE B 291 ? 0.7038 0.7401 0.7846 -0.0411 -0.0114 0.0461  295 ILE B N   
13421 C CA  . ILE B 291 ? 0.7315 0.7876 0.8206 -0.0459 -0.0152 0.0469  295 ILE B CA  
13422 C C   . ILE B 291 ? 0.7067 0.7483 0.7838 -0.0611 -0.0246 0.0426  295 ILE B C   
13423 O O   . ILE B 291 ? 0.6751 0.7148 0.7451 -0.0611 -0.0287 0.0360  295 ILE B O   
13424 C CB  . ILE B 291 ? 0.8153 0.9057 0.9237 -0.0469 -0.0117 0.0598  295 ILE B CB  
13425 C CG1 . ILE B 291 ? 0.8895 0.9886 1.0026 -0.0288 -0.0043 0.0602  295 ILE B CG1 
13426 C CG2 . ILE B 291 ? 0.8388 0.9507 0.9557 -0.0590 -0.0196 0.0642  295 ILE B CG2 
13427 C CD1 . ILE B 291 ? 0.9931 1.0721 1.0959 -0.0180 0.0010  0.0559  295 ILE B CD1 
13439 N N   . GLY B 292 ? 0.7164 0.7441 0.7871 -0.0750 -0.0284 0.0464  296 GLY B N   
13440 C CA  . GLY B 292 ? 0.7032 0.7070 0.7555 -0.0912 -0.0393 0.0411  296 GLY B CA  
13441 C C   . GLY B 292 ? 0.7209 0.6905 0.7482 -0.0801 -0.0400 0.0259  296 GLY B C   
13442 O O   . GLY B 292 ? 0.7351 0.6928 0.7461 -0.0857 -0.0471 0.0184  296 GLY B O   
13446 N N   . GLN B 293 ? 0.7135 0.6692 0.7368 -0.0630 -0.0326 0.0217  297 GLN B N   
13447 C CA  . GLN B 293 ? 0.6904 0.6206 0.6937 -0.0491 -0.0313 0.0095  297 GLN B CA  
13448 C C   . GLN B 293 ? 0.6583 0.6107 0.6680 -0.0401 -0.0283 0.0054  297 GLN B C   
13449 O O   . GLN B 293 ? 0.6764 0.6141 0.6669 -0.0364 -0.0297 -0.0035 297 GLN B O   
13450 C CB  . GLN B 293 ? 0.6830 0.6012 0.6853 -0.0334 -0.0252 0.0090  297 GLN B CB  
13451 C CG  . GLN B 293 ? 0.7296 0.6162 0.7174 -0.0399 -0.0281 0.0125  297 GLN B CG  
13452 C CD  . GLN B 293 ? 0.7487 0.6281 0.7366 -0.0236 -0.0231 0.0142  297 GLN B CD  
13453 O OE1 . GLN B 293 ? 0.7738 0.6802 0.7801 -0.0158 -0.0186 0.0179  297 GLN B OE1 
13454 N NE2 . GLN B 293 ? 0.7978 0.6378 0.7623 -0.0182 -0.0251 0.0114  297 GLN B NE2 
13463 N N   . LEU B 294 ? 0.6587 0.6434 0.6919 -0.0358 -0.0237 0.0120  298 LEU B N   
13464 C CA  . LEU B 294 ? 0.6065 0.6103 0.6454 -0.0292 -0.0210 0.0104  298 LEU B CA  
13465 C C   . LEU B 294 ? 0.6272 0.6360 0.6580 -0.0400 -0.0276 0.0097  298 LEU B C   
13466 O O   . LEU B 294 ? 0.6368 0.6451 0.6564 -0.0350 -0.0267 0.0044  298 LEU B O   
13467 C CB  . LEU B 294 ? 0.5696 0.5985 0.6302 -0.0245 -0.0165 0.0182  298 LEU B CB  
13468 C CG  . LEU B 294 ? 0.5930 0.6182 0.6587 -0.0138 -0.0118 0.0178  298 LEU B CG  
13469 C CD1 . LEU B 294 ? 0.6227 0.6630 0.7019 -0.0115 -0.0093 0.0246  298 LEU B CD1 
13470 C CD2 . LEU B 294 ? 0.6034 0.6286 0.6663 -0.0043 -0.0090 0.0125  298 LEU B CD2 
13482 N N   . ILE B 295 ? 0.6234 0.6399 0.6598 -0.0552 -0.0346 0.0162  299 ILE B N   
13483 C CA  . ILE B 295 ? 0.6174 0.6399 0.6455 -0.0680 -0.0442 0.0163  299 ILE B CA  
13484 C C   . ILE B 295 ? 0.7011 0.6868 0.6946 -0.0701 -0.0492 0.0034  299 ILE B C   
13485 O O   . ILE B 295 ? 0.7332 0.7180 0.7110 -0.0678 -0.0513 -0.0021 299 ILE B O   
13486 C CB  . ILE B 295 ? 0.5618 0.6022 0.6044 -0.0863 -0.0521 0.0274  299 ILE B CB  
13487 C CG1 . ILE B 295 ? 0.5307 0.6100 0.6042 -0.0791 -0.0454 0.0402  299 ILE B CG1 
13488 C CG2 . ILE B 295 ? 0.5135 0.5565 0.5440 -0.1034 -0.0661 0.0269  299 ILE B CG2 
13489 C CD1 . ILE B 295 ? 0.5076 0.6146 0.6010 -0.0933 -0.0498 0.0542  299 ILE B CD1 
13501 N N   . ASP B 296 ? 0.7343 0.6857 0.7116 -0.0731 -0.0509 -0.0016 300 ASP B N   
13502 C CA  . ASP B 296 ? 0.8176 0.7248 0.7556 -0.0730 -0.0557 -0.0148 300 ASP B CA  
13503 C C   . ASP B 296 ? 0.8164 0.7216 0.7408 -0.0518 -0.0466 -0.0237 300 ASP B C   
13504 O O   . ASP B 296 ? 0.8655 0.7559 0.7618 -0.0523 -0.0506 -0.0319 300 ASP B O   
13505 C CB  . ASP B 296 ? 0.9056 0.7737 0.8291 -0.0723 -0.0554 -0.0176 300 ASP B CB  
13506 C CG  . ASP B 296 ? 1.0329 0.8458 0.9107 -0.0784 -0.0645 -0.0297 300 ASP B CG  
13507 O OD1 . ASP B 296 ? 1.0608 0.8607 0.9276 -0.1037 -0.0786 -0.0279 300 ASP B OD1 
13508 O OD2 . ASP B 296 ? 1.0888 0.8711 0.9405 -0.0577 -0.0577 -0.0407 300 ASP B OD2 
13513 N N   . LYS B 297 ? 0.8022 0.7245 0.7459 -0.0339 -0.0345 -0.0211 301 LYS B N   
13514 C CA  . LYS B 297 ? 0.7703 0.6946 0.7043 -0.0140 -0.0245 -0.0272 301 LYS B CA  
13515 C C   . LYS B 297 ? 0.7084 0.6669 0.6543 -0.0137 -0.0216 -0.0223 301 LYS B C   
13516 O O   . LYS B 297 ? 0.7393 0.6978 0.6689 -0.0023 -0.0153 -0.0272 301 LYS B O   
13517 C CB  . LYS B 297 ? 0.6868 0.6180 0.6376 0.0027  -0.0148 -0.0248 301 LYS B CB  
13518 C CG  . LYS B 297 ? 0.6931 0.5872 0.6277 0.0071  -0.0165 -0.0291 301 LYS B CG  
13519 C CD  . LYS B 297 ? 0.7592 0.6113 0.6519 0.0173  -0.0164 -0.0416 301 LYS B CD  
13520 C CE  . LYS B 297 ? 0.9102 0.7170 0.7823 0.0198  -0.0200 -0.0449 301 LYS B CE  
13521 N NZ  . LYS B 297 ? 1.0743 0.8307 0.8988 0.0324  -0.0198 -0.0582 301 LYS B NZ  
13535 N N   . LEU B 298 ? 0.6435 0.6304 0.6156 -0.0243 -0.0250 -0.0119 302 LEU B N   
13536 C CA  . LEU B 298 ? 0.6385 0.6523 0.6181 -0.0242 -0.0235 -0.0062 302 LEU B CA  
13537 C C   . LEU B 298 ? 0.7040 0.7088 0.6567 -0.0329 -0.0323 -0.0107 302 LEU B C   
13538 O O   . LEU B 298 ? 0.7123 0.7255 0.6533 -0.0270 -0.0287 -0.0111 302 LEU B O   
13539 C CB  . LEU B 298 ? 0.5670 0.6080 0.5772 -0.0301 -0.0251 0.0060  302 LEU B CB  
13540 C CG  . LEU B 298 ? 0.5558 0.6081 0.5884 -0.0209 -0.0166 0.0110  302 LEU B CG  
13541 C CD1 . LEU B 298 ? 0.5391 0.6078 0.5927 -0.0253 -0.0188 0.0209  302 LEU B CD1 
13542 C CD2 . LEU B 298 ? 0.5534 0.6180 0.5875 -0.0121 -0.0089 0.0127  302 LEU B CD2 
13554 N N   . VAL B 299 ? 0.7031 0.6909 0.6444 -0.0485 -0.0448 -0.0133 303 VAL B N   
13555 C CA  . VAL B 299 ? 0.7593 0.7346 0.6708 -0.0598 -0.0568 -0.0185 303 VAL B CA  
13556 C C   . VAL B 299 ? 0.8589 0.7952 0.7270 -0.0487 -0.0531 -0.0338 303 VAL B C   
13557 O O   . VAL B 299 ? 0.9328 0.8658 0.7743 -0.0453 -0.0539 -0.0385 303 VAL B O   
13558 C CB  . VAL B 299 ? 0.7213 0.6912 0.6349 -0.0834 -0.0729 -0.0152 303 VAL B CB  
13559 C CG1 . VAL B 299 ? 0.7312 0.6813 0.6081 -0.0980 -0.0887 -0.0225 303 VAL B CG1 
13560 C CG2 . VAL B 299 ? 0.6847 0.6999 0.6405 -0.0902 -0.0746 0.0013  303 VAL B CG2 
13570 N N   . GLN B 300 ? 0.8763 0.7813 0.7337 -0.0409 -0.0486 -0.0413 304 GLN B N   
13571 C CA  . GLN B 300 ? 0.9987 0.8628 0.8121 -0.0257 -0.0437 -0.0560 304 GLN B CA  
13572 C C   . GLN B 300 ? 0.9280 0.8139 0.7395 -0.0039 -0.0280 -0.0560 304 GLN B C   
13573 O O   . GLN B 300 ? 0.9503 0.8153 0.7215 0.0053  -0.0257 -0.0658 304 GLN B O   
13574 C CB  . GLN B 300 ? 1.1611 0.9939 0.9704 -0.0164 -0.0394 -0.0606 304 GLN B CB  
13575 C CG  . GLN B 300 ? 1.3619 1.1446 1.1218 0.0022  -0.0345 -0.0759 304 GLN B CG  
13576 C CD  . GLN B 300 ? 1.5334 1.2808 1.2876 0.0101  -0.0329 -0.0787 304 GLN B CD  
13577 O OE1 . GLN B 300 ? 1.5767 1.3218 1.3498 -0.0074 -0.0413 -0.0718 304 GLN B OE1 
13578 N NE2 . GLN B 300 ? 1.6374 1.3588 1.3650 0.0382  -0.0213 -0.0875 304 GLN B NE2 
13587 N N   . ASN B 301 ? 0.8609 0.7876 0.7132 0.0036  -0.0172 -0.0447 305 ASN B N   
13588 C CA  . ASN B 301 ? 0.8015 0.7547 0.6585 0.0208  -0.0022 -0.0411 305 ASN B CA  
13589 C C   . ASN B 301 ? 0.7934 0.7775 0.6598 0.0119  -0.0042 -0.0316 305 ASN B C   
13590 O O   . ASN B 301 ? 0.7398 0.7483 0.6120 0.0226  0.0080  -0.0256 305 ASN B O   
13591 C CB  . ASN B 301 ? 0.7536 0.7316 0.6476 0.0318  0.0088  -0.0333 305 ASN B CB  
13592 C CG  . ASN B 301 ? 0.7894 0.7412 0.6706 0.0482  0.0141  -0.0415 305 ASN B CG  
13593 O OD1 . ASN B 301 ? 0.8897 0.8458 0.7611 0.0694  0.0271  -0.0440 305 ASN B OD1 
13594 N ND2 . ASN B 301 ? 0.7505 0.6764 0.6318 0.0395  0.0048  -0.0443 305 ASN B ND2 
13601 N N   . ASN B 302 ? 0.8144 0.7997 0.6830 -0.0071 -0.0191 -0.0283 306 ASN B N   
13602 C CA  . ASN B 302 ? 0.7904 0.8013 0.6630 -0.0140 -0.0229 -0.0189 306 ASN B CA  
13603 C C   . ASN B 302 ? 0.7170 0.7628 0.6257 -0.0083 -0.0122 -0.0050 306 ASN B C   
13604 O O   . ASN B 302 ? 0.7055 0.7677 0.6097 -0.0030 -0.0050 0.0013  306 ASN B O   
13605 C CB  . ASN B 302 ? 0.8803 0.8777 0.7086 -0.0080 -0.0217 -0.0263 306 ASN B CB  
13606 C CG  . ASN B 302 ? 0.9859 1.0052 0.8123 -0.0168 -0.0292 -0.0165 306 ASN B CG  
13607 O OD1 . ASN B 302 ? 1.0462 1.0711 0.8801 -0.0329 -0.0452 -0.0122 306 ASN B OD1 
13608 N ND2 . ASN B 302 ? 1.0705 1.1048 0.8871 -0.0058 -0.0174 -0.0114 306 ASN B ND2 
13615 N N   . VAL B 303 ? 0.6714 0.7254 0.6129 -0.0105 -0.0116 0.0001  307 VAL B N   
13616 C CA  . VAL B 303 ? 0.6090 0.6873 0.5813 -0.0074 -0.0040 0.0118  307 VAL B CA  
13617 C C   . VAL B 303 ? 0.5686 0.6590 0.5606 -0.0170 -0.0127 0.0216  307 VAL B C   
13618 O O   . VAL B 303 ? 0.6067 0.6921 0.6073 -0.0236 -0.0202 0.0203  307 VAL B O   
13619 C CB  . VAL B 303 ? 0.5861 0.6629 0.5766 -0.0003 0.0031  0.0098  307 VAL B CB  
13620 C CG1 . VAL B 303 ? 0.5495 0.6463 0.5688 -0.0013 0.0070  0.0213  307 VAL B CG1 
13621 C CG2 . VAL B 303 ? 0.6164 0.6877 0.5903 0.0137  0.0134  0.0026  307 VAL B CG2 
13631 N N   . LEU B 304 ? 0.5582 0.6647 0.5568 -0.0167 -0.0108 0.0326  308 LEU B N   
13632 C CA  . LEU B 304 ? 0.5432 0.6607 0.5592 -0.0205 -0.0169 0.0433  308 LEU B CA  
13633 C C   . LEU B 304 ? 0.5680 0.6860 0.6065 -0.0169 -0.0110 0.0483  308 LEU B C   
13634 O O   . LEU B 304 ? 0.6069 0.7269 0.6483 -0.0143 -0.0036 0.0523  308 LEU B O   
13635 C CB  . LEU B 304 ? 0.5299 0.6583 0.5361 -0.0205 -0.0192 0.0532  308 LEU B CB  
13636 C CG  . LEU B 304 ? 0.5385 0.6679 0.5210 -0.0259 -0.0293 0.0501  308 LEU B CG  
13637 C CD1 . LEU B 304 ? 0.5664 0.7074 0.5394 -0.0240 -0.0307 0.0621  308 LEU B CD1 
13638 C CD2 . LEU B 304 ? 0.5011 0.6352 0.4931 -0.0344 -0.0421 0.0496  308 LEU B CD2 
13650 N N   . LEU B 305 ? 0.5557 0.6724 0.6087 -0.0177 -0.0146 0.0489  309 LEU B N   
13651 C CA  . LEU B 305 ? 0.4929 0.6045 0.5610 -0.0140 -0.0104 0.0516  309 LEU B CA  
13652 C C   . LEU B 305 ? 0.5436 0.6575 0.6172 -0.0103 -0.0115 0.0628  309 LEU B C   
13653 O O   . LEU B 305 ? 0.5791 0.7033 0.6538 -0.0090 -0.0165 0.0686  309 LEU B O   
13654 C CB  . LEU B 305 ? 0.4446 0.5504 0.5203 -0.0145 -0.0120 0.0460  309 LEU B CB  
13655 C CG  . LEU B 305 ? 0.4143 0.5113 0.4998 -0.0104 -0.0085 0.0463  309 LEU B CG  
13656 C CD1 . LEU B 305 ? 0.4002 0.4929 0.4857 -0.0101 -0.0044 0.0436  309 LEU B CD1 
13657 C CD2 . LEU B 305 ? 0.4141 0.5067 0.5033 -0.0111 -0.0097 0.0418  309 LEU B CD2 
13669 N N   . ILE B 306 ? 0.5707 0.6741 0.6467 -0.0086 -0.0076 0.0665  310 ILE B N   
13670 C CA  . ILE B 306 ? 0.5682 0.6630 0.6429 -0.0037 -0.0082 0.0766  310 ILE B CA  
13671 C C   . ILE B 306 ? 0.5830 0.6586 0.6609 -0.0013 -0.0068 0.0744  310 ILE B C   
13672 O O   . ILE B 306 ? 0.5984 0.6652 0.6764 -0.0075 -0.0055 0.0724  310 ILE B O   
13673 C CB  . ILE B 306 ? 0.5753 0.6682 0.6411 -0.0071 -0.0066 0.0851  310 ILE B CB  
13674 C CG1 . ILE B 306 ? 0.5722 0.6817 0.6292 -0.0074 -0.0091 0.0883  310 ILE B CG1 
13675 C CG2 . ILE B 306 ? 0.6155 0.6876 0.6761 -0.0027 -0.0073 0.0949  310 ILE B CG2 
13676 C CD1 . ILE B 306 ? 0.6048 0.7154 0.6501 -0.0112 -0.0058 0.0964  310 ILE B CD1 
13688 N N   . PHE B 307 ? 0.5568 0.6278 0.6365 0.0077  -0.0072 0.0753  311 PHE B N   
13689 C CA  . PHE B 307 ? 0.5672 0.6159 0.6431 0.0122  -0.0060 0.0722  311 PHE B CA  
13690 C C   . PHE B 307 ? 0.6188 0.6410 0.6810 0.0169  -0.0066 0.0793  311 PHE B C   
13691 O O   . PHE B 307 ? 0.6402 0.6591 0.6974 0.0296  -0.0057 0.0865  311 PHE B O   
13692 C CB  . PHE B 307 ? 0.5751 0.6306 0.6557 0.0219  -0.0039 0.0708  311 PHE B CB  
13693 C CG  . PHE B 307 ? 0.5804 0.6511 0.6704 0.0153  -0.0040 0.0638  311 PHE B CG  
13694 C CD1 . PHE B 307 ? 0.6285 0.6890 0.7172 0.0096  -0.0042 0.0557  311 PHE B CD1 
13695 C CD2 . PHE B 307 ? 0.5975 0.6919 0.6969 0.0144  -0.0050 0.0664  311 PHE B CD2 
13696 C CE1 . PHE B 307 ? 0.6550 0.7240 0.7489 0.0055  -0.0044 0.0501  311 PHE B CE1 
13697 C CE2 . PHE B 307 ? 0.6159 0.7167 0.7198 0.0068  -0.0060 0.0605  311 PHE B CE2 
13698 C CZ  . PHE B 307 ? 0.6181 0.7039 0.7179 0.0036  -0.0051 0.0522  311 PHE B CZ  
13708 N N   . ALA B 308 ? 0.6451 0.6482 0.7009 0.0066  -0.0087 0.0785  312 ALA B N   
13709 C CA  . ALA B 308 ? 0.6593 0.6269 0.6974 0.0071  -0.0112 0.0844  312 ALA B CA  
13710 C C   . ALA B 308 ? 0.7026 0.6404 0.7282 0.0102  -0.0135 0.0768  312 ALA B C   
13711 O O   . ALA B 308 ? 0.7494 0.6802 0.7757 -0.0031 -0.0179 0.0719  312 ALA B O   
13712 C CB  . ALA B 308 ? 0.6717 0.6376 0.7099 -0.0101 -0.0135 0.0904  312 ALA B CB  
13718 N N   . VAL B 309 ? 0.7141 0.6361 0.7275 0.0287  -0.0104 0.0763  313 VAL B N   
13719 C CA  . VAL B 309 ? 0.7142 0.6091 0.7115 0.0353  -0.0109 0.0680  313 VAL B CA  
13720 C C   . VAL B 309 ? 0.7524 0.6036 0.7202 0.0525  -0.0097 0.0709  313 VAL B C   
13721 O O   . VAL B 309 ? 0.7488 0.5988 0.7136 0.0640  -0.0069 0.0802  313 VAL B O   
13722 C CB  . VAL B 309 ? 0.7043 0.6276 0.7149 0.0443  -0.0051 0.0631  313 VAL B CB  
13723 C CG1 . VAL B 309 ? 0.7151 0.6723 0.7490 0.0289  -0.0068 0.0596  313 VAL B CG1 
13724 C CG2 . VAL B 309 ? 0.6407 0.5862 0.6590 0.0625  0.0021  0.0707  313 VAL B CG2 
13734 N N   . THR B 310 ? 0.7900 0.6023 0.7323 0.0557  -0.0123 0.0625  314 THR B N   
13735 C CA  . THR B 310 ? 0.8502 0.6088 0.7551 0.0729  -0.0118 0.0626  314 THR B CA  
13736 C C   . THR B 310 ? 0.9542 0.7264 0.8578 0.1044  0.0007  0.0658  314 THR B C   
13737 O O   . THR B 310 ? 0.8700 0.6924 0.8017 0.1089  0.0075  0.0675  314 THR B O   
13738 C CB  . THR B 310 ? 0.8044 0.5146 0.6776 0.0656  -0.0198 0.0512  314 THR B CB  
13739 O OG1 . THR B 310 ? 0.7882 0.5228 0.6708 0.0675  -0.0169 0.0431  314 THR B OG1 
13740 C CG2 . THR B 310 ? 0.7679 0.4638 0.6421 0.0339  -0.0336 0.0517  314 THR B CG2 
13748 N N   . GLN B 311 ? 1.1719 0.8975 1.0412 0.1265  0.0037  0.0675  315 GLN B N   
13749 C CA  . GLN B 311 ? 1.3168 1.0587 1.1859 0.1602  0.0169  0.0738  315 GLN B CA  
13750 C C   . GLN B 311 ? 1.1991 0.9673 1.0749 0.1706  0.0259  0.0680  315 GLN B C   
13751 O O   . GLN B 311 ? 1.0833 0.9034 0.9862 0.1844  0.0359  0.0762  315 GLN B O   
13752 C CB  . GLN B 311 ? 1.5641 1.2408 1.3870 0.1850  0.0189  0.0748  315 GLN B CB  
13753 C CG  . GLN B 311 ? 1.7395 1.4329 1.5605 0.2252  0.0340  0.0831  315 GLN B CG  
13754 C CD  . GLN B 311 ? 1.8802 1.5040 1.6526 0.2522  0.0358  0.0848  315 GLN B CD  
13755 O OE1 . GLN B 311 ? 1.8645 1.4236 1.6032 0.2373  0.0244  0.0797  315 GLN B OE1 
13756 N NE2 . GLN B 311 ? 1.8987 1.5351 1.6668 0.2922  0.0502  0.0931  315 GLN B NE2 
13765 N N   . GLU B 312 ? 1.1824 0.9166 1.0335 0.1626  0.0217  0.0551  316 GLU B N   
13766 C CA  . GLU B 312 ? 1.1088 0.8617 0.9597 0.1735  0.0306  0.0502  316 GLU B CA  
13767 C C   . GLU B 312 ? 0.9088 0.7300 0.8071 0.1587  0.0328  0.0548  316 GLU B C   
13768 O O   . GLU B 312 ? 0.8817 0.7320 0.7885 0.1704  0.0433  0.0568  316 GLU B O   
13769 C CB  . GLU B 312 ? 1.2430 0.9462 1.0573 0.1634  0.0222  0.0356  316 GLU B CB  
13770 C CG  . GLU B 312 ? 1.4659 1.0907 1.2230 0.1778  0.0188  0.0285  316 GLU B CG  
13771 C CD  . GLU B 312 ? 1.6395 1.2270 1.3877 0.1591  0.0051  0.0305  316 GLU B CD  
13772 O OE1 . GLU B 312 ? 1.6729 1.2978 1.4592 0.1338  -0.0017 0.0364  316 GLU B OE1 
13773 O OE2 . GLU B 312 ? 1.7792 1.2981 1.4798 0.1701  0.0016  0.0266  316 GLU B OE2 
13780 N N   . GLN B 313 ? 0.7870 0.6318 0.7133 0.1339  0.0238  0.0570  317 GLN B N   
13781 C CA  . GLN B 313 ? 0.6835 0.5805 0.6468 0.1178  0.0235  0.0587  317 GLN B CA  
13782 C C   . GLN B 313 ? 0.6104 0.5543 0.6058 0.1180  0.0260  0.0704  317 GLN B C   
13783 O O   . GLN B 313 ? 0.5311 0.5148 0.5536 0.1052  0.0254  0.0719  317 GLN B O   
13784 C CB  . GLN B 313 ? 0.6975 0.5879 0.6664 0.0903  0.0116  0.0514  317 GLN B CB  
13785 C CG  . GLN B 313 ? 0.7786 0.6273 0.7187 0.0850  0.0050  0.0407  317 GLN B CG  
13786 C CD  . GLN B 313 ? 0.7890 0.6445 0.7228 0.0935  0.0110  0.0363  317 GLN B CD  
13787 O OE1 . GLN B 313 ? 0.7781 0.6746 0.7367 0.0941  0.0176  0.0408  317 GLN B OE1 
13788 N NE2 . GLN B 313 ? 0.8736 0.6861 0.7709 0.0990  0.0079  0.0278  317 GLN B NE2 
13797 N N   . VAL B 314 ? 0.6542 0.5918 0.6446 0.1320  0.0276  0.0787  318 VAL B N   
13798 C CA  . VAL B 314 ? 0.7192 0.6993 0.7376 0.1287  0.0261  0.0898  318 VAL B CA  
13799 C C   . VAL B 314 ? 0.6885 0.7226 0.7348 0.1341  0.0328  0.0972  318 VAL B C   
13800 O O   . VAL B 314 ? 0.6848 0.7554 0.7564 0.1162  0.0279  0.0991  318 VAL B O   
13801 C CB  . VAL B 314 ? 0.8113 0.7724 0.8160 0.1463  0.0265  0.0990  318 VAL B CB  
13802 C CG1 . VAL B 314 ? 0.8370 0.8501 0.8699 0.1524  0.0273  0.1131  318 VAL B CG1 
13803 C CG2 . VAL B 314 ? 0.8567 0.7791 0.8451 0.1295  0.0169  0.0958  318 VAL B CG2 
13813 N N   . HIS B 315 ? 0.7047 0.7441 0.7452 0.1586  0.0440  0.1022  319 HIS B N   
13814 C CA  . HIS B 315 ? 0.7493 0.8463 0.8196 0.1632  0.0509  0.1132  319 HIS B CA  
13815 C C   . HIS B 315 ? 0.6750 0.7914 0.7614 0.1381  0.0475  0.1076  319 HIS B C   
13816 O O   . HIS B 315 ? 0.6459 0.8076 0.7614 0.1250  0.0445  0.1152  319 HIS B O   
13817 C CB  . HIS B 315 ? 0.8593 0.9569 0.9174 0.1949  0.0663  0.1189  319 HIS B CB  
13818 C CG  . HIS B 315 ? 0.9774 1.1421 1.0700 0.2020  0.0747  0.1351  319 HIS B CG  
13819 N ND1 . HIS B 315 ? 1.0220 1.2086 1.1207 0.2038  0.0852  0.1374  319 HIS B ND1 
13820 C CD2 . HIS B 315 ? 1.0083 1.2256 1.1320 0.2063  0.0734  0.1515  319 HIS B CD2 
13821 C CE1 . HIS B 315 ? 1.0272 1.2788 1.1615 0.2074  0.0904  0.1553  319 HIS B CE1 
13822 N NE2 . HIS B 315 ? 1.0015 1.2739 1.1522 0.2088  0.0825  0.1639  319 HIS B NE2 
13830 N N   . LEU B 316 ? 0.6683 0.7484 0.7341 0.1309  0.0466  0.0946  320 LEU B N   
13831 C CA  . LEU B 316 ? 0.6403 0.7320 0.7174 0.1093  0.0430  0.0892  320 LEU B CA  
13832 C C   . LEU B 316 ? 0.6087 0.7146 0.7035 0.0861  0.0316  0.0877  320 LEU B C   
13833 O O   . LEU B 316 ? 0.5601 0.6983 0.6757 0.0727  0.0292  0.0921  320 LEU B O   
13834 C CB  . LEU B 316 ? 0.6554 0.7036 0.7053 0.1069  0.0415  0.0760  320 LEU B CB  
13835 C CG  . LEU B 316 ? 0.6741 0.7256 0.7303 0.0874  0.0368  0.0698  320 LEU B CG  
13836 C CD1 . LEU B 316 ? 0.7009 0.7805 0.7674 0.0898  0.0457  0.0774  320 LEU B CD1 
13837 C CD2 . LEU B 316 ? 0.7447 0.7538 0.7747 0.0849  0.0316  0.0577  320 LEU B CD2 
13849 N N   . TYR B 317 ? 0.5983 0.6784 0.6824 0.0806  0.0244  0.0818  321 TYR B N   
13850 C CA  . TYR B 317 ? 0.5661 0.6562 0.6613 0.0612  0.0155  0.0793  321 TYR B CA  
13851 C C   . TYR B 317 ? 0.5650 0.6898 0.6779 0.0600  0.0125  0.0897  321 TYR B C   
13852 O O   . TYR B 317 ? 0.5521 0.6910 0.6737 0.0436  0.0056  0.0879  321 TYR B O   
13853 C CB  . TYR B 317 ? 0.5828 0.6405 0.6627 0.0560  0.0103  0.0728  321 TYR B CB  
13854 C CG  . TYR B 317 ? 0.5385 0.5719 0.6077 0.0483  0.0083  0.0623  321 TYR B CG  
13855 C CD1 . TYR B 317 ? 0.5061 0.5477 0.5839 0.0331  0.0041  0.0565  321 TYR B CD1 
13856 C CD2 . TYR B 317 ? 0.5471 0.5487 0.5953 0.0574  0.0101  0.0582  321 TYR B CD2 
13857 C CE1 . TYR B 317 ? 0.4926 0.5172 0.5630 0.0278  0.0015  0.0488  321 TYR B CE1 
13858 C CE2 . TYR B 317 ? 0.5668 0.5495 0.6055 0.0492  0.0058  0.0496  321 TYR B CE2 
13859 C CZ  . TYR B 317 ? 0.5390 0.5364 0.5914 0.0346  0.0015  0.0458  321 TYR B CZ  
13860 O OH  . TYR B 317 ? 0.5913 0.5747 0.6367 0.0281  -0.0034 0.0390  321 TYR B OH  
13870 N N   . GLU B 318 ? 0.6481 0.7862 0.7641 0.0781  0.0170  0.1006  322 GLU B N   
13871 C CA  . GLU B 318 ? 0.6982 0.8773 0.8342 0.0769  0.0128  0.1126  322 GLU B CA  
13872 C C   . GLU B 318 ? 0.7009 0.9184 0.8589 0.0644  0.0117  0.1170  322 GLU B C   
13873 O O   . GLU B 318 ? 0.7002 0.9417 0.8706 0.0477  0.0021  0.1198  322 GLU B O   
13874 C CB  . GLU B 318 ? 0.7798 0.9673 0.9154 0.1027  0.0185  0.1251  322 GLU B CB  
13875 C CG  . GLU B 318 ? 0.9014 1.0618 1.0204 0.1084  0.0141  0.1260  322 GLU B CG  
13876 C CD  . GLU B 318 ? 1.0734 1.2317 1.1860 0.1378  0.0204  0.1378  322 GLU B CD  
13877 O OE1 . GLU B 318 ? 1.1392 1.2996 1.2499 0.1576  0.0311  0.1404  322 GLU B OE1 
13878 O OE2 . GLU B 318 ? 1.1691 1.3239 1.2769 0.1430  0.0153  0.1452  322 GLU B OE2 
13885 N N   . ASN B 319 ? 0.7258 0.9469 0.8860 0.0708  0.0209  0.1180  323 ASN B N   
13886 C CA  . ASN B 319 ? 0.7028 0.9567 0.8825 0.0557  0.0201  0.1235  323 ASN B CA  
13887 C C   . ASN B 319 ? 0.6484 0.8843 0.8226 0.0304  0.0105  0.1118  323 ASN B C   
13888 O O   . ASN B 319 ? 0.6919 0.9503 0.8791 0.0113  0.0025  0.1156  323 ASN B O   
13889 C CB  . ASN B 319 ? 0.7176 0.9738 0.8956 0.0684  0.0335  0.1269  323 ASN B CB  
13890 C CG  . ASN B 319 ? 0.7908 1.0795 0.9801 0.0939  0.0445  0.1424  323 ASN B CG  
13891 O OD1 . ASN B 319 ? 0.8030 1.0671 0.9723 0.1189  0.0549  0.1401  323 ASN B OD1 
13892 N ND2 . ASN B 319 ? 0.8547 1.1987 1.0746 0.0882  0.0418  0.1586  323 ASN B ND2 
13899 N N   . TYR B 320 ? 0.5838 0.7784 0.7374 0.0300  0.0106  0.0979  324 TYR B N   
13900 C CA  . TYR B 320 ? 0.5715 0.7487 0.7183 0.0112  0.0028  0.0870  324 TYR B CA  
13901 C C   . TYR B 320 ? 0.4940 0.6806 0.6425 0.0007  -0.0073 0.0869  324 TYR B C   
13902 O O   . TYR B 320 ? 0.5139 0.7044 0.6631 -0.0164 -0.0151 0.0842  324 TYR B O   
13903 C CB  . TYR B 320 ? 0.6000 0.7394 0.7283 0.0152  0.0047  0.0748  324 TYR B CB  
13904 C CG  . TYR B 320 ? 0.6210 0.7454 0.7417 0.0203  0.0110  0.0719  324 TYR B CG  
13905 C CD1 . TYR B 320 ? 0.7000 0.8397 0.8285 0.0159  0.0145  0.0779  324 TYR B CD1 
13906 C CD2 . TYR B 320 ? 0.6283 0.7231 0.7327 0.0278  0.0125  0.0640  324 TYR B CD2 
13907 C CE1 . TYR B 320 ? 0.7698 0.8950 0.8880 0.0213  0.0206  0.0760  324 TYR B CE1 
13908 C CE2 . TYR B 320 ? 0.6523 0.7323 0.7460 0.0324  0.0167  0.0611  324 TYR B CE2 
13909 C CZ  . TYR B 320 ? 0.7744 0.8692 0.8740 0.0304  0.0214  0.0670  324 TYR B CZ  
13910 O OH  . TYR B 320 ? 0.8813 0.9608 0.9672 0.0357  0.0258  0.0651  324 TYR B OH  
13920 N N   . ALA B 321 ? 0.4589 0.6452 0.6042 0.0110  -0.0076 0.0899  325 ALA B N   
13921 C CA  . ALA B 321 ? 0.4924 0.6861 0.6352 0.0026  -0.0166 0.0903  325 ALA B CA  
13922 C C   . ALA B 321 ? 0.6012 0.8321 0.7595 -0.0071 -0.0249 0.1003  325 ALA B C   
13923 O O   . ALA B 321 ? 0.6806 0.9148 0.8326 -0.0202 -0.0352 0.0979  325 ALA B O   
13924 C CB  . ALA B 321 ? 0.4263 0.6115 0.5615 0.0162  -0.0148 0.0943  325 ALA B CB  
13930 N N   . LYS B 322 ? 0.6102 0.8710 0.7879 -0.0012 -0.0210 0.1123  326 LYS B N   
13931 C CA  . LYS B 322 ? 0.6757 0.9783 0.8729 -0.0145 -0.0303 0.1240  326 LYS B CA  
13932 C C   . LYS B 322 ? 0.6949 0.9867 0.8857 -0.0409 -0.0399 0.1158  326 LYS B C   
13933 O O   . LYS B 322 ? 0.7682 1.0757 0.9605 -0.0586 -0.0539 0.1184  326 LYS B O   
13934 C CB  . LYS B 322 ? 0.7233 1.0637 0.9450 -0.0031 -0.0216 0.1396  326 LYS B CB  
13935 C CG  . LYS B 322 ? 0.7379 1.0920 0.9648 0.0257  -0.0131 0.1500  326 LYS B CG  
13936 C CD  . LYS B 322 ? 0.7786 1.1758 1.0299 0.0394  -0.0027 0.1666  326 LYS B CD  
13937 C CE  . LYS B 322 ? 0.9019 1.2986 1.1494 0.0744  0.0091  0.1739  326 LYS B CE  
13938 N NZ  . LYS B 322 ? 1.0250 1.4651 1.2942 0.0927  0.0223  0.1903  326 LYS B NZ  
13952 N N   . LEU B 323 ? 0.6422 0.9037 0.8226 -0.0435 -0.0336 0.1058  327 LEU B N   
13953 C CA  . LEU B 323 ? 0.5827 0.8267 0.7534 -0.0659 -0.0416 0.0986  327 LEU B CA  
13954 C C   . LEU B 323 ? 0.6229 0.8320 0.7668 -0.0720 -0.0487 0.0831  327 LEU B C   
13955 O O   . LEU B 323 ? 0.6719 0.8679 0.8030 -0.0909 -0.0596 0.0778  327 LEU B O   
13956 C CB  . LEU B 323 ? 0.5440 0.7683 0.7120 -0.0637 -0.0318 0.0955  327 LEU B CB  
13957 C CG  . LEU B 323 ? 0.5568 0.8110 0.7456 -0.0537 -0.0208 0.1097  327 LEU B CG  
13958 C CD1 . LEU B 323 ? 0.5855 0.8132 0.7639 -0.0490 -0.0111 0.1046  327 LEU B CD1 
13959 C CD2 . LEU B 323 ? 0.5824 0.8800 0.7947 -0.0714 -0.0274 0.1259  327 LEU B CD2 
13971 N N   . ILE B 324 ? 0.6148 0.8078 0.7481 -0.0565 -0.0426 0.0765  328 ILE B N   
13972 C CA  . ILE B 324 ? 0.6322 0.7945 0.7410 -0.0581 -0.0448 0.0627  328 ILE B CA  
13973 C C   . ILE B 324 ? 0.6804 0.8548 0.7814 -0.0619 -0.0539 0.0647  328 ILE B C   
13974 O O   . ILE B 324 ? 0.7093 0.9029 0.8197 -0.0511 -0.0518 0.0737  328 ILE B O   
13975 C CB  . ILE B 324 ? 0.6413 0.7847 0.7452 -0.0421 -0.0337 0.0568  328 ILE B CB  
13976 C CG1 . ILE B 324 ? 0.6161 0.7502 0.7266 -0.0375 -0.0262 0.0562  328 ILE B CG1 
13977 C CG2 . ILE B 324 ? 0.6721 0.7910 0.7542 -0.0427 -0.0339 0.0446  328 ILE B CG2 
13978 C CD1 . ILE B 324 ? 0.6228 0.7426 0.7309 -0.0237 -0.0178 0.0527  328 ILE B CD1 
13990 N N   . PRO B 325 ? 0.7115 0.8715 0.7914 -0.0758 -0.0643 0.0567  329 PRO B N   
13991 C CA  . PRO B 325 ? 0.6892 0.8594 0.7568 -0.0792 -0.0738 0.0584  329 PRO B CA  
13992 C C   . PRO B 325 ? 0.6561 0.8190 0.7142 -0.0629 -0.0645 0.0565  329 PRO B C   
13993 O O   . PRO B 325 ? 0.6945 0.8331 0.7403 -0.0559 -0.0554 0.0468  329 PRO B O   
13994 C CB  . PRO B 325 ? 0.7136 0.8558 0.7508 -0.0956 -0.0850 0.0460  329 PRO B CB  
13995 C CG  . PRO B 325 ? 0.7234 0.8509 0.7656 -0.1055 -0.0849 0.0434  329 PRO B CG  
13996 C CD  . PRO B 325 ? 0.7378 0.8676 0.7996 -0.0888 -0.0689 0.0460  329 PRO B CD  
14004 N N   . GLY B 326 ? 0.6121 0.7985 0.6771 -0.0572 -0.0672 0.0678  330 GLY B N   
14005 C CA  . GLY B 326 ? 0.6345 0.8145 0.6891 -0.0450 -0.0601 0.0691  330 GLY B CA  
14006 C C   . GLY B 326 ? 0.6352 0.8093 0.7035 -0.0309 -0.0469 0.0727  330 GLY B C   
14007 O O   . GLY B 326 ? 0.6851 0.8536 0.7463 -0.0231 -0.0417 0.0763  330 GLY B O   
14011 N N   . ALA B 327 ? 0.5723 0.7451 0.6570 -0.0286 -0.0421 0.0722  331 ALA B N   
14012 C CA  . ALA B 327 ? 0.5766 0.7387 0.6688 -0.0163 -0.0316 0.0742  331 ALA B CA  
14013 C C   . ALA B 327 ? 0.5940 0.7691 0.6950 -0.0043 -0.0309 0.0878  331 ALA B C   
14014 O O   . ALA B 327 ? 0.6439 0.8450 0.7564 -0.0033 -0.0366 0.0972  331 ALA B O   
14015 C CB  . ALA B 327 ? 0.5731 0.7285 0.6753 -0.0163 -0.0272 0.0697  331 ALA B CB  
14021 N N   . THR B 328 ? 0.5832 0.7400 0.6785 0.0048  -0.0244 0.0898  332 THR B N   
14022 C CA  . THR B 328 ? 0.6046 0.7617 0.7019 0.0192  -0.0226 0.1017  332 THR B CA  
14023 C C   . THR B 328 ? 0.5739 0.7019 0.6668 0.0270  -0.0149 0.0988  332 THR B C   
14024 O O   . THR B 328 ? 0.5141 0.6270 0.6046 0.0199  -0.0121 0.0888  332 THR B O   
14025 C CB  . THR B 328 ? 0.6793 0.8364 0.7644 0.0203  -0.0261 0.1099  332 THR B CB  
14026 O OG1 . THR B 328 ? 0.7348 0.8699 0.8066 0.0137  -0.0220 0.1047  332 THR B OG1 
14027 C CG2 . THR B 328 ? 0.7142 0.8980 0.7988 0.0116  -0.0360 0.1118  332 THR B CG2 
14035 N N   . VAL B 329 ? 0.5796 0.6979 0.6690 0.0426  -0.0123 0.1077  333 VAL B N   
14036 C CA  . VAL B 329 ? 0.5594 0.6441 0.6384 0.0510  -0.0067 0.1047  333 VAL B CA  
14037 C C   . VAL B 329 ? 0.6168 0.6746 0.6790 0.0601  -0.0067 0.1135  333 VAL B C   
14038 O O   . VAL B 329 ? 0.6491 0.7190 0.7114 0.0710  -0.0085 0.1250  333 VAL B O   
14039 C CB  . VAL B 329 ? 0.5572 0.6486 0.6431 0.0652  -0.0014 0.1052  333 VAL B CB  
14040 C CG1 . VAL B 329 ? 0.5218 0.5717 0.5886 0.0755  0.0034  0.1009  333 VAL B CG1 
14041 C CG2 . VAL B 329 ? 0.5632 0.6767 0.6638 0.0538  -0.0016 0.0980  333 VAL B CG2 
14051 N N   . GLY B 330 ? 0.6144 0.6349 0.6614 0.0548  -0.0059 0.1090  334 GLY B N   
14052 C CA  . GLY B 330 ? 0.6286 0.6126 0.6548 0.0613  -0.0066 0.1170  334 GLY B CA  
14053 C C   . GLY B 330 ? 0.6622 0.6020 0.6697 0.0665  -0.0052 0.1107  334 GLY B C   
14054 O O   . GLY B 330 ? 0.6467 0.5816 0.6565 0.0565  -0.0055 0.0999  334 GLY B O   
14058 N N   . LEU B 331 ? 0.6671 0.5713 0.6525 0.0834  -0.0044 0.1177  335 LEU B N   
14059 C CA  . LEU B 331 ? 0.7167 0.5706 0.6756 0.0926  -0.0034 0.1113  335 LEU B CA  
14060 C C   . LEU B 331 ? 0.7830 0.5933 0.7227 0.0709  -0.0108 0.1094  335 LEU B C   
14061 O O   . LEU B 331 ? 0.8367 0.6247 0.7636 0.0666  -0.0140 0.1197  335 LEU B O   
14062 C CB  . LEU B 331 ? 0.7951 0.6259 0.7345 0.1237  0.0013  0.1194  335 LEU B CB  
14063 C CG  . LEU B 331 ? 0.8976 0.6645 0.7985 0.1374  0.0026  0.1125  335 LEU B CG  
14064 C CD1 . LEU B 331 ? 0.9395 0.7086 0.8414 0.1326  0.0044  0.0980  335 LEU B CD1 
14065 C CD2 . LEU B 331 ? 0.9585 0.7120 0.8430 0.1749  0.0104  0.1207  335 LEU B CD2 
14077 N N   . LEU B 332 ? 0.8029 0.6025 0.7410 0.0564  -0.0141 0.0979  336 LEU B N   
14078 C CA  . LEU B 332 ? 0.8129 0.5841 0.7411 0.0307  -0.0228 0.0967  336 LEU B CA  
14079 C C   . LEU B 332 ? 0.8848 0.5877 0.7730 0.0345  -0.0283 0.0918  336 LEU B C   
14080 O O   . LEU B 332 ? 0.8931 0.5799 0.7666 0.0509  -0.0257 0.0820  336 LEU B O   
14081 C CB  . LEU B 332 ? 0.7894 0.5955 0.7420 0.0117  -0.0249 0.0883  336 LEU B CB  
14082 C CG  . LEU B 332 ? 0.8677 0.6623 0.8204 -0.0167 -0.0340 0.0889  336 LEU B CG  
14083 C CD1 . LEU B 332 ? 0.9141 0.7325 0.8817 -0.0313 -0.0329 0.1017  336 LEU B CD1 
14084 C CD2 . LEU B 332 ? 0.8447 0.6670 0.8158 -0.0264 -0.0362 0.0789  336 LEU B CD2 
14096 N N   . GLN B 333 ? 0.9535 0.6140 0.8211 0.0188  -0.0362 0.0987  337 GLN B N   
14097 C CA  . GLN B 333 ? 1.0396 0.6269 0.8641 0.0164  -0.0448 0.0930  337 GLN B CA  
14098 C C   . GLN B 333 ? 1.0156 0.6031 0.8422 -0.0032 -0.0533 0.0805  337 GLN B C   
14099 O O   . GLN B 333 ? 0.9247 0.5659 0.7871 -0.0198 -0.0537 0.0796  337 GLN B O   
14100 C CB  . GLN B 333 ? 1.0967 0.6387 0.8999 -0.0019 -0.0532 0.1051  337 GLN B CB  
14101 C CG  . GLN B 333 ? 1.0925 0.6190 0.8828 0.0210  -0.0465 0.1180  337 GLN B CG  
14102 C CD  . GLN B 333 ? 1.1153 0.5924 0.8815 0.0018  -0.0548 0.1316  337 GLN B CD  
14103 O OE1 . GLN B 333 ? 1.1408 0.5834 0.8932 -0.0282 -0.0666 0.1306  337 GLN B OE1 
14104 N NE2 . GLN B 333 ? 1.1221 0.5965 0.8832 0.0176  -0.0496 0.1460  337 GLN B NE2 
14113 N N   . LYS B 334 ? 1.1000 0.6238 0.8840 0.0005  -0.0606 0.0708  338 LYS B N   
14114 C CA  . LYS B 334 ? 1.1377 0.6573 0.9178 -0.0165 -0.0707 0.0587  338 LYS B CA  
14115 C C   . LYS B 334 ? 1.0628 0.5983 0.8632 -0.0568 -0.0841 0.0649  338 LYS B C   
14116 O O   . LYS B 334 ? 0.9962 0.5549 0.8107 -0.0724 -0.0916 0.0582  338 LYS B O   
14117 C CB  . LYS B 334 ? 1.3191 0.7582 1.0407 -0.0052 -0.0775 0.0470  338 LYS B CB  
14118 C CG  . LYS B 334 ? 1.4597 0.8804 1.1575 0.0386  -0.0622 0.0430  338 LYS B CG  
14119 C CD  . LYS B 334 ? 1.5384 1.0248 1.2695 0.0565  -0.0488 0.0388  338 LYS B CD  
14120 C CE  . LYS B 334 ? 1.6343 1.1174 1.3515 0.0988  -0.0320 0.0396  338 LYS B CE  
14121 N NZ  . LYS B 334 ? 1.7376 1.1404 1.3920 0.1201  -0.0328 0.0300  338 LYS B NZ  
14135 N N   . ASP B 335 ? 1.0927 0.6204 0.8963 -0.0733 -0.0869 0.0791  339 ASP B N   
14136 C CA  . ASP B 335 ? 1.0200 0.5682 0.8453 -0.1120 -0.0979 0.0886  339 ASP B CA  
14137 C C   . ASP B 335 ? 0.9627 0.5791 0.8327 -0.1172 -0.0871 0.1025  339 ASP B C   
14138 O O   . ASP B 335 ? 0.9717 0.6056 0.8587 -0.1462 -0.0925 0.1152  339 ASP B O   
14139 C CB  . ASP B 335 ? 1.0568 0.5310 0.8422 -0.1342 -0.1126 0.0952  339 ASP B CB  
14140 C CG  . ASP B 335 ? 1.0912 0.5292 0.8550 -0.1189 -0.1052 0.1063  339 ASP B CG  
14141 O OD1 . ASP B 335 ? 1.0372 0.5146 0.8208 -0.0928 -0.0895 0.1098  339 ASP B OD1 
14142 O OD2 . ASP B 335 ? 1.1679 0.5359 0.8931 -0.1337 -0.1163 0.1121  339 ASP B OD2 
14147 N N   . SER B 336 ? 0.8956 0.5513 0.7838 -0.0904 -0.0721 0.1010  340 SER B N   
14148 C CA  . SER B 336 ? 0.7997 0.5143 0.7226 -0.0917 -0.0619 0.1120  340 SER B CA  
14149 C C   . SER B 336 ? 0.8199 0.5130 0.7312 -0.1015 -0.0620 0.1291  340 SER B C   
14150 O O   . SER B 336 ? 0.7586 0.4963 0.6943 -0.1097 -0.0555 0.1404  340 SER B O   
14151 C CB  . SER B 336 ? 0.7294 0.5030 0.6903 -0.1117 -0.0625 0.1127  340 SER B CB  
14152 O OG  . SER B 336 ? 0.6794 0.4832 0.6554 -0.0976 -0.0588 0.0993  340 SER B OG  
14158 N N   . GLY B 337 ? 0.9080 0.5300 0.7785 -0.0992 -0.0688 0.1314  341 GLY B N   
14159 C CA  . GLY B 337 ? 0.8248 0.4179 0.6798 -0.1108 -0.0705 0.1492  341 GLY B CA  
14160 C C   . GLY B 337 ? 1.0120 0.6393 0.8796 -0.0926 -0.0580 0.1600  341 GLY B C   
14161 O O   . GLY B 337 ? 1.0616 0.6844 0.9258 -0.1060 -0.0575 0.1772  341 GLY B O   
14165 N N   . ASN B 338 ? 0.9311 0.5931 0.8123 -0.0641 -0.0486 0.1513  342 ASN B N   
14166 C CA  . ASN B 338 ? 0.8920 0.5847 0.7819 -0.0456 -0.0395 0.1606  342 ASN B CA  
14167 C C   . ASN B 338 ? 0.8504 0.6179 0.7785 -0.0453 -0.0319 0.1563  342 ASN B C   
14168 O O   . ASN B 338 ? 0.8092 0.6057 0.7450 -0.0267 -0.0258 0.1584  342 ASN B O   
14169 C CB  . ASN B 338 ? 0.8968 0.5627 0.7662 -0.0105 -0.0364 0.1571  342 ASN B CB  
14170 C CG  . ASN B 338 ? 0.8954 0.5843 0.7775 0.0063  -0.0327 0.1403  342 ASN B CG  
14171 O OD1 . ASN B 338 ? 0.8842 0.5737 0.7718 -0.0070 -0.0365 0.1288  342 ASN B OD1 
14172 N ND2 . ASN B 338 ? 0.9623 0.6732 0.8501 0.0347  -0.0258 0.1405  342 ASN B ND2 
14179 N N   . ILE B 339 ? 0.8044 0.6024 0.7548 -0.0652 -0.0329 0.1505  343 ILE B N   
14180 C CA  . ILE B 339 ? 0.7058 0.5660 0.6867 -0.0617 -0.0256 0.1444  343 ILE B CA  
14181 C C   . ILE B 339 ? 0.7290 0.6216 0.7169 -0.0639 -0.0190 0.1570  343 ILE B C   
14182 O O   . ILE B 339 ? 0.6868 0.6167 0.6864 -0.0517 -0.0134 0.1528  343 ILE B O   
14183 C CB  . ILE B 339 ? 0.6382 0.5220 0.6396 -0.0794 -0.0281 0.1369  343 ILE B CB  
14184 C CG1 . ILE B 339 ? 0.5881 0.5282 0.6156 -0.0726 -0.0201 0.1298  343 ILE B CG1 
14185 C CG2 . ILE B 339 ? 0.6422 0.5246 0.6471 -0.1076 -0.0318 0.1502  343 ILE B CG2 
14186 C CD1 . ILE B 339 ? 0.5442 0.4904 0.5718 -0.0498 -0.0175 0.1182  343 ILE B CD1 
14198 N N   . LEU B 340 ? 0.7942 0.6712 0.7722 -0.0805 -0.0200 0.1730  344 LEU B N   
14199 C CA  . LEU B 340 ? 0.8175 0.7236 0.7976 -0.0821 -0.0129 0.1863  344 LEU B CA  
14200 C C   . LEU B 340 ? 0.8613 0.7639 0.8280 -0.0579 -0.0117 0.1883  344 LEU B C   
14201 O O   . LEU B 340 ? 0.8085 0.7502 0.7829 -0.0502 -0.0067 0.1877  344 LEU B O   
14202 C CB  . LEU B 340 ? 0.8463 0.7303 0.8150 -0.1048 -0.0144 0.2057  344 LEU B CB  
14203 C CG  . LEU B 340 ? 0.8781 0.7860 0.8426 -0.1070 -0.0065 0.2228  344 LEU B CG  
14204 C CD1 . LEU B 340 ? 0.9077 0.8785 0.8957 -0.1075 0.0037  0.2180  344 LEU B CD1 
14205 C CD2 . LEU B 340 ? 0.8941 0.7756 0.8468 -0.1320 -0.0084 0.2438  344 LEU B CD2 
14217 N N   . GLN B 341 ? 0.9362 0.7918 0.8812 -0.0449 -0.0170 0.1908  345 GLN B N   
14218 C CA  . GLN B 341 ? 1.0012 0.8577 0.9363 -0.0200 -0.0167 0.1951  345 GLN B CA  
14219 C C   . GLN B 341 ? 0.9070 0.8049 0.8622 -0.0046 -0.0148 0.1809  345 GLN B C   
14220 O O   . GLN B 341 ? 0.8925 0.8212 0.8515 0.0058  -0.0140 0.1845  345 GLN B O   
14221 C CB  . GLN B 341 ? 1.1754 0.9723 1.0831 -0.0050 -0.0214 0.1998  345 GLN B CB  
14222 C CG  . GLN B 341 ? 1.3773 1.1219 1.2589 -0.0214 -0.0253 0.2150  345 GLN B CG  
14223 C CD  . GLN B 341 ? 1.5609 1.2698 1.4372 -0.0430 -0.0308 0.2078  345 GLN B CD  
14224 O OE1 . GLN B 341 ? 1.5751 1.3173 1.4748 -0.0636 -0.0300 0.2016  345 GLN B OE1 
14225 N NE2 . GLN B 341 ? 1.6990 1.3384 1.5423 -0.0374 -0.0372 0.2088  345 GLN B NE2 
14234 N N   . LEU B 342 ? 0.8383 0.7363 0.8047 -0.0047 -0.0151 0.1656  346 LEU B N   
14235 C CA  . LEU B 342 ? 0.7566 0.6920 0.7420 0.0064  -0.0134 0.1534  346 LEU B CA  
14236 C C   . LEU B 342 ? 0.7133 0.6944 0.7127 -0.0023 -0.0105 0.1519  346 LEU B C   
14237 O O   . LEU B 342 ? 0.7104 0.7190 0.7146 0.0074  -0.0113 0.1511  346 LEU B O   
14238 C CB  . LEU B 342 ? 0.7528 0.6804 0.7463 0.0037  -0.0137 0.1386  346 LEU B CB  
14239 C CG  . LEU B 342 ? 0.8492 0.7311 0.8244 0.0162  -0.0160 0.1358  346 LEU B CG  
14240 C CD1 . LEU B 342 ? 0.8474 0.7242 0.8283 0.0098  -0.0171 0.1214  346 LEU B CD1 
14241 C CD2 . LEU B 342 ? 0.8645 0.7527 0.8378 0.0431  -0.0137 0.1386  346 LEU B CD2 
14253 N N   . ILE B 343 ? 0.7096 0.6993 0.7143 -0.0205 -0.0074 0.1517  347 ILE B N   
14254 C CA  . ILE B 343 ? 0.6790 0.7081 0.6924 -0.0257 -0.0027 0.1486  347 ILE B CA  
14255 C C   . ILE B 343 ? 0.6849 0.7252 0.6846 -0.0204 -0.0027 0.1597  347 ILE B C   
14256 O O   . ILE B 343 ? 0.6570 0.7227 0.6573 -0.0142 -0.0037 0.1542  347 ILE B O   
14257 C CB  . ILE B 343 ? 0.6944 0.7331 0.7163 -0.0433 0.0023  0.1501  347 ILE B CB  
14258 C CG1 . ILE B 343 ? 0.6637 0.6974 0.7001 -0.0473 0.0001  0.1379  347 ILE B CG1 
14259 C CG2 . ILE B 343 ? 0.6726 0.7486 0.6971 -0.0445 0.0097  0.1486  347 ILE B CG2 
14260 C CD1 . ILE B 343 ? 0.6494 0.6978 0.6991 -0.0642 0.0032  0.1404  347 ILE B CD1 
14272 N N   . ILE B 344 ? 0.7274 0.7460 0.7117 -0.0237 -0.0028 0.1760  348 ILE B N   
14273 C CA  . ILE B 344 ? 0.7632 0.7913 0.7314 -0.0184 -0.0033 0.1885  348 ILE B CA  
14274 C C   . ILE B 344 ? 0.7538 0.7896 0.7210 0.0000  -0.0105 0.1864  348 ILE B C   
14275 O O   . ILE B 344 ? 0.7661 0.8291 0.7292 0.0037  -0.0130 0.1861  348 ILE B O   
14276 C CB  . ILE B 344 ? 0.7951 0.7918 0.7451 -0.0248 -0.0029 0.2082  348 ILE B CB  
14277 C CG1 . ILE B 344 ? 0.7954 0.7949 0.7505 -0.0469 0.0041  0.2131  348 ILE B CG1 
14278 C CG2 . ILE B 344 ? 0.8097 0.8144 0.7403 -0.0169 -0.0042 0.2225  348 ILE B CG2 
14279 C CD1 . ILE B 344 ? 0.8227 0.8654 0.7816 -0.0525 0.0131  0.2122  348 ILE B CD1 
14291 N N   . SER B 345 ? 0.7342 0.7478 0.7045 0.0120  -0.0142 0.1854  349 SER B N   
14292 C CA  . SER B 345 ? 0.7321 0.7612 0.7071 0.0304  -0.0200 0.1858  349 SER B CA  
14293 C C   . SER B 345 ? 0.6590 0.7271 0.6507 0.0273  -0.0218 0.1719  349 SER B C   
14294 O O   . SER B 345 ? 0.6207 0.7158 0.6127 0.0325  -0.0282 0.1748  349 SER B O   
14295 C CB  . SER B 345 ? 0.7929 0.7942 0.7693 0.0457  -0.0204 0.1851  349 SER B CB  
14296 O OG  . SER B 345 ? 0.9052 0.8646 0.8597 0.0527  -0.0208 0.1992  349 SER B OG  
14302 N N   . ALA B 346 ? 0.6208 0.6902 0.6247 0.0180  -0.0177 0.1573  350 ALA B N   
14303 C CA  . ALA B 346 ? 0.5594 0.6575 0.5753 0.0142  -0.0196 0.1440  350 ALA B CA  
14304 C C   . ALA B 346 ? 0.6033 0.7208 0.6069 0.0066  -0.0208 0.1437  350 ALA B C   
14305 O O   . ALA B 346 ? 0.5889 0.7278 0.5918 0.0073  -0.0279 0.1403  350 ALA B O   
14306 C CB  . ALA B 346 ? 0.4754 0.5667 0.5029 0.0068  -0.0145 0.1302  350 ALA B CB  
14312 N N   . TYR B 347 ? 0.6677 0.7782 0.6600 -0.0014 -0.0139 0.1476  351 TYR B N   
14313 C CA  . TYR B 347 ? 0.6934 0.8201 0.6683 -0.0059 -0.0127 0.1477  351 TYR B CA  
14314 C C   . TYR B 347 ? 0.7496 0.8848 0.7093 0.0006  -0.0218 0.1588  351 TYR B C   
14315 O O   . TYR B 347 ? 0.7418 0.8938 0.6893 -0.0007 -0.0278 0.1535  351 TYR B O   
14316 C CB  . TYR B 347 ? 0.6801 0.8018 0.6473 -0.0140 -0.0018 0.1547  351 TYR B CB  
14317 C CG  . TYR B 347 ? 0.6454 0.7831 0.5904 -0.0158 0.0026  0.1559  351 TYR B CG  
14318 C CD1 . TYR B 347 ? 0.6341 0.7847 0.5737 -0.0156 0.0050  0.1401  351 TYR B CD1 
14319 C CD2 . TYR B 347 ? 0.6585 0.7945 0.5838 -0.0165 0.0049  0.1729  351 TYR B CD2 
14320 C CE1 . TYR B 347 ? 0.6478 0.8085 0.5606 -0.0146 0.0099  0.1398  351 TYR B CE1 
14321 C CE2 . TYR B 347 ? 0.6972 0.8473 0.5978 -0.0167 0.0101  0.1741  351 TYR B CE2 
14322 C CZ  . TYR B 347 ? 0.6825 0.8446 0.5759 -0.0150 0.0128  0.1567  351 TYR B CZ  
14323 O OH  . TYR B 347 ? 0.6790 0.8508 0.5417 -0.0126 0.0188  0.1565  351 TYR B OH  
14333 N N   . GLU B 348 ? 0.8293 0.9505 0.7867 0.0082  -0.0240 0.1745  352 GLU B N   
14334 C CA  . GLU B 348 ? 0.8970 1.0280 0.8406 0.0166  -0.0333 0.1877  352 GLU B CA  
14335 C C   . GLU B 348 ? 0.9153 1.0708 0.8727 0.0228  -0.0451 0.1826  352 GLU B C   
14336 O O   . GLU B 348 ? 0.8828 1.0596 0.8291 0.0220  -0.0552 0.1851  352 GLU B O   
14337 C CB  . GLU B 348 ? 0.9036 1.0089 0.8404 0.0259  -0.0325 0.2062  352 GLU B CB  
14338 C CG  . GLU B 348 ? 0.9397 1.0237 0.8599 0.0156  -0.0232 0.2159  352 GLU B CG  
14339 C CD  . GLU B 348 ? 1.0082 1.0610 0.9141 0.0234  -0.0244 0.2361  352 GLU B CD  
14340 O OE1 . GLU B 348 ? 1.0624 1.0998 0.9745 0.0382  -0.0291 0.2390  352 GLU B OE1 
14341 O OE2 . GLU B 348 ? 1.0942 1.1363 0.9804 0.0158  -0.0199 0.2500  352 GLU B OE2 
14348 N N   . GLU B 349 ? 0.9303 1.0847 0.9110 0.0278  -0.0445 0.1765  353 GLU B N   
14349 C CA  . GLU B 349 ? 0.9355 1.1190 0.9333 0.0305  -0.0543 0.1729  353 GLU B CA  
14350 C C   . GLU B 349 ? 0.8758 1.0749 0.8675 0.0152  -0.0596 0.1585  353 GLU B C   
14351 O O   . GLU B 349 ? 0.8681 1.0924 0.8594 0.0119  -0.0727 0.1599  353 GLU B O   
14352 C CB  . GLU B 349 ? 1.0370 1.2161 1.0587 0.0375  -0.0496 0.1679  353 GLU B CB  
14353 C CG  . GLU B 349 ? 1.1951 1.4091 1.2381 0.0437  -0.0584 0.1716  353 GLU B CG  
14354 C CD  . GLU B 349 ? 1.3720 1.5832 1.4359 0.0525  -0.0514 0.1679  353 GLU B CD  
14355 O OE1 . GLU B 349 ? 1.4471 1.6247 1.5057 0.0556  -0.0413 0.1628  353 GLU B OE1 
14356 O OE2 . GLU B 349 ? 1.4221 1.6661 1.5069 0.0554  -0.0563 0.1708  353 GLU B OE2 
14363 N N   . LEU B 350 ? 0.8334 1.0169 0.8188 0.0060  -0.0504 0.1450  354 LEU B N   
14364 C CA  . LEU B 350 ? 0.7514 0.9407 0.7248 -0.0054 -0.0541 0.1301  354 LEU B CA  
14365 C C   . LEU B 350 ? 0.7505 0.9468 0.6937 -0.0085 -0.0615 0.1339  354 LEU B C   
14366 O O   . LEU B 350 ? 0.7299 0.9381 0.6632 -0.0158 -0.0746 0.1280  354 LEU B O   
14367 C CB  . LEU B 350 ? 0.7429 0.9148 0.7146 -0.0097 -0.0409 0.1174  354 LEU B CB  
14368 C CG  . LEU B 350 ? 0.7169 0.8821 0.7131 -0.0098 -0.0362 0.1088  354 LEU B CG  
14369 C CD1 . LEU B 350 ? 0.7329 0.8850 0.7269 -0.0125 -0.0241 0.0998  354 LEU B CD1 
14370 C CD2 . LEU B 350 ? 0.6807 0.8565 0.6851 -0.0155 -0.0458 0.0997  354 LEU B CD2 
14382 N N   . ARG B 351 ? 0.7745 0.9620 0.7003 -0.0043 -0.0542 0.1444  355 ARG B N   
14383 C CA  . ARG B 351 ? 0.8202 1.0135 0.7130 -0.0059 -0.0604 0.1492  355 ARG B CA  
14384 C C   . ARG B 351 ? 0.8823 1.0956 0.7754 -0.0022 -0.0780 0.1619  355 ARG B C   
14385 O O   . ARG B 351 ? 0.8848 1.1051 0.7489 -0.0046 -0.0874 0.1651  355 ARG B O   
14386 C CB  . ARG B 351 ? 0.8013 0.9827 0.6763 -0.0027 -0.0474 0.1610  355 ARG B CB  
14387 C CG  . ARG B 351 ? 0.7855 0.9556 0.6631 -0.0063 -0.0295 0.1531  355 ARG B CG  
14388 C CD  . ARG B 351 ? 0.8123 0.9834 0.6682 -0.0097 -0.0256 0.1356  355 ARG B CD  
14389 N NE  . ARG B 351 ? 0.8659 1.0399 0.6812 -0.0087 -0.0283 0.1379  355 ARG B NE  
14390 C CZ  . ARG B 351 ? 0.9434 1.1184 0.7386 -0.0061 -0.0183 0.1520  355 ARG B CZ  
14391 N NH1 . ARG B 351 ? 0.9908 1.1633 0.8040 -0.0066 -0.0062 0.1662  355 ARG B NH1 
14392 N NH2 . ARG B 351 ? 0.9905 1.1673 0.7446 -0.0044 -0.0213 0.1524  355 ARG B NH2 
14406 N N   . SER B 352 ? 0.9383 1.1627 0.8619 0.0049  -0.0826 0.1698  356 SER B N   
14407 C CA  . SER B 352 ? 1.0467 1.2975 0.9772 0.0115  -0.0985 0.1845  356 SER B CA  
14408 C C   . SER B 352 ? 0.9983 1.2770 0.9463 0.0019  -0.1136 0.1772  356 SER B C   
14409 O O   . SER B 352 ? 0.9897 1.2997 0.9514 0.0064  -0.1277 0.1906  356 SER B O   
14410 C CB  . SER B 352 ? 1.1510 1.3986 1.1027 0.0295  -0.0931 0.2008  356 SER B CB  
14411 O OG  . SER B 352 ? 1.2071 1.4510 1.1874 0.0317  -0.0856 0.1926  356 SER B OG  
14417 N N   . GLU B 353 ? 1.1799 1.1031 1.2321 -0.0553 0.0391  -0.1009 357 GLU B N   
14418 C CA  . GLU B 353 ? 1.0930 1.0428 1.1545 -0.0310 0.0353  -0.1127 357 GLU B CA  
14419 C C   . GLU B 353 ? 0.9178 0.9324 0.9652 -0.0167 0.0111  -0.0926 357 GLU B C   
14420 O O   . GLU B 353 ? 0.8838 0.9287 0.9149 -0.0285 0.0028  -0.0752 357 GLU B O   
14421 C CB  . GLU B 353 ? 1.1651 1.1094 1.2018 -0.0577 0.0521  -0.1513 357 GLU B CB  
14422 C CG  . GLU B 353 ? 1.3088 1.1773 1.3516 -0.0735 0.0887  -0.1829 357 GLU B CG  
14423 C CD  . GLU B 353 ? 1.3990 1.2591 1.3906 -0.1150 0.1057  -0.2227 357 GLU B CD  
14424 O OE1 . GLU B 353 ? 1.3714 1.2885 1.3247 -0.1371 0.0810  -0.2171 357 GLU B OE1 
14425 O OE2 . GLU B 353 ? 1.4808 1.2757 1.4706 -0.1265 0.1454  -0.2578 357 GLU B OE2 
14432 N N   . VAL B 354 ? 0.8341 0.8664 0.8918 0.0081  0.0051  -0.0965 358 VAL B N   
14433 C CA  . VAL B 354 ? 0.7261 0.8083 0.7660 0.0184  -0.0091 -0.0889 358 VAL B CA  
14434 C C   . VAL B 354 ? 0.6860 0.7750 0.7301 0.0251  -0.0047 -0.1107 358 VAL B C   
14435 O O   . VAL B 354 ? 0.6921 0.7630 0.7653 0.0423  -0.0011 -0.1158 358 VAL B O   
14436 C CB  . VAL B 354 ? 0.7126 0.8022 0.7493 0.0397  -0.0237 -0.0632 358 VAL B CB  
14437 C CG1 . VAL B 354 ? 0.6680 0.7940 0.6838 0.0492  -0.0286 -0.0635 358 VAL B CG1 
14438 C CG2 . VAL B 354 ? 0.7579 0.8391 0.7816 0.0289  -0.0240 -0.0404 358 VAL B CG2 
14448 N N   . GLU B 355 ? 0.6848 0.8028 0.7055 0.0105  -0.0057 -0.1191 359 GLU B N   
14449 C CA  . GLU B 355 ? 0.6961 0.8211 0.7106 0.0123  -0.0016 -0.1360 359 GLU B CA  
14450 C C   . GLU B 355 ? 0.7186 0.8822 0.7223 0.0249  -0.0147 -0.1202 359 GLU B C   
14451 O O   . GLU B 355 ? 0.7727 0.9654 0.7704 0.0190  -0.0217 -0.1032 359 GLU B O   
14452 C CB  . GLU B 355 ? 0.7694 0.8841 0.7561 -0.0229 0.0100  -0.1582 359 GLU B CB  
14453 C CG  . GLU B 355 ? 0.8585 0.9791 0.8272 -0.0274 0.0158  -0.1731 359 GLU B CG  
14454 C CD  . GLU B 355 ? 0.9866 1.0854 0.9118 -0.0704 0.0308  -0.1984 359 GLU B CD  
14455 O OE1 . GLU B 355 ? 1.0443 1.1161 0.9566 -0.0962 0.0397  -0.2096 359 GLU B OE1 
14456 O OE2 . GLU B 355 ? 1.0396 1.1432 0.9357 -0.0832 0.0349  -0.2077 359 GLU B OE2 
14463 N N   . LEU B 356 ? 0.7182 0.8812 0.7261 0.0421  -0.0151 -0.1248 360 LEU B N   
14464 C CA  . LEU B 356 ? 0.6755 0.8607 0.6717 0.0542  -0.0212 -0.1127 360 LEU B CA  
14465 C C   . LEU B 356 ? 0.7505 0.9522 0.7319 0.0407  -0.0213 -0.1141 360 LEU B C   
14466 O O   . LEU B 356 ? 0.7996 0.9918 0.7685 0.0192  -0.0158 -0.1299 360 LEU B O   
14467 C CB  . LEU B 356 ? 0.6059 0.7797 0.6055 0.0717  -0.0236 -0.1157 360 LEU B CB  
14468 C CG  . LEU B 356 ? 0.6151 0.7829 0.6057 0.0827  -0.0302 -0.1021 360 LEU B CG  
14469 C CD1 . LEU B 356 ? 0.6250 0.7828 0.6079 0.0888  -0.0371 -0.1064 360 LEU B CD1 
14470 C CD2 . LEU B 356 ? 0.6583 0.8394 0.6327 0.0861  -0.0224 -0.0885 360 LEU B CD2 
14482 N N   . GLU B 357 ? 0.7564 0.9785 0.7373 0.0524  -0.0251 -0.0957 361 GLU B N   
14483 C CA  . GLU B 357 ? 0.7739 1.0176 0.7476 0.0429  -0.0314 -0.0825 361 GLU B CA  
14484 C C   . GLU B 357 ? 0.7753 1.0149 0.7553 0.0684  -0.0256 -0.0711 361 GLU B C   
14485 O O   . GLU B 357 ? 0.8069 1.0421 0.7974 0.0882  -0.0167 -0.0656 361 GLU B O   
14486 C CB  . GLU B 357 ? 0.8454 1.1287 0.8320 0.0276  -0.0437 -0.0591 361 GLU B CB  
14487 C CG  . GLU B 357 ? 0.9313 1.2345 0.8959 -0.0064 -0.0600 -0.0510 361 GLU B CG  
14488 C CD  . GLU B 357 ? 0.9856 1.3366 0.9690 -0.0280 -0.0788 -0.0248 361 GLU B CD  
14489 O OE1 . GLU B 357 ? 0.9621 1.3318 0.9830 -0.0116 -0.0737 -0.0128 361 GLU B OE1 
14490 O OE2 . GLU B 357 ? 1.0626 1.4340 1.0205 -0.0661 -0.0990 -0.0152 361 GLU B OE2 
14497 N N   . VAL B 358 ? 0.7598 0.9926 0.7267 0.0646  -0.0265 -0.0695 362 VAL B N   
14498 C CA  . VAL B 358 ? 0.7454 0.9614 0.7155 0.0861  -0.0171 -0.0607 362 VAL B CA  
14499 C C   . VAL B 358 ? 0.7891 1.0250 0.7665 0.0836  -0.0262 -0.0294 362 VAL B C   
14500 O O   . VAL B 358 ? 0.8356 1.0722 0.7872 0.0598  -0.0360 -0.0290 362 VAL B O   
14501 C CB  . VAL B 358 ? 0.7482 0.9292 0.6991 0.0841  -0.0092 -0.0857 362 VAL B CB  
14502 C CG1 . VAL B 358 ? 0.7633 0.9174 0.7103 0.1003  0.0027  -0.0788 362 VAL B CG1 
14503 C CG2 . VAL B 358 ? 0.7408 0.9116 0.6945 0.0859  -0.0086 -0.1061 362 VAL B CG2 
14513 N N   . LEU B 359 ? 0.7645 1.0158 0.7786 0.1074  -0.0211 -0.0007 363 LEU B N   
14514 C CA  . LEU B 359 ? 0.7486 1.0312 0.7914 0.1101  -0.0348 0.0426  363 LEU B CA  
14515 C C   . LEU B 359 ? 0.7237 0.9736 0.7889 0.1426  -0.0128 0.0576  363 LEU B C   
14516 O O   . LEU B 359 ? 0.6849 0.8913 0.7410 0.1603  0.0151  0.0321  363 LEU B O   
14517 C CB  . LEU B 359 ? 0.7695 1.1116 0.8620 0.1109  -0.0472 0.0728  363 LEU B CB  
14518 C CG  . LEU B 359 ? 0.8048 1.1771 0.8762 0.0730  -0.0691 0.0624  363 LEU B CG  
14519 C CD1 . LEU B 359 ? 0.8199 1.1604 0.8656 0.0705  -0.0529 0.0195  363 LEU B CD1 
14520 C CD2 . LEU B 359 ? 0.8252 1.2651 0.9545 0.0693  -0.0861 0.1024  363 LEU B CD2 
14532 N N   . GLY B 360 ? 0.7393 1.0062 0.8301 0.1469  -0.0261 0.1008  364 GLY B N   
14533 C CA  . GLY B 360 ? 0.8297 1.0600 0.9512 0.1800  -0.0024 0.1212  364 GLY B CA  
14534 C C   . GLY B 360 ? 0.9366 1.1241 1.0154 0.1666  -0.0066 0.1224  364 GLY B C   
14535 O O   . GLY B 360 ? 0.9624 1.1679 1.0015 0.1321  -0.0345 0.1276  364 GLY B O   
14539 N N   . ASP B 361 ? 1.0236 1.1487 1.1043 0.1895  0.0250  0.1157  365 ASP B N   
14540 C CA  . ASP B 361 ? 1.1371 1.2136 1.1779 0.1756  0.0263  0.1156  365 ASP B CA  
14541 C C   . ASP B 361 ? 1.0806 1.1316 1.0586 0.1461  0.0305  0.0596  365 ASP B C   
14542 O O   . ASP B 361 ? 1.0916 1.0908 1.0502 0.1496  0.0556  0.0263  365 ASP B O   
14543 C CB  . ASP B 361 ? 1.3089 1.3213 1.3780 0.2086  0.0618  0.1291  365 ASP B CB  
14544 C CG  . ASP B 361 ? 1.4957 1.5350 1.6442 0.2409  0.0569  0.1960  365 ASP B CG  
14545 O OD1 . ASP B 361 ? 1.5655 1.6767 1.7361 0.2284  0.0157  0.2372  365 ASP B OD1 
14546 O OD2 . ASP B 361 ? 1.6144 1.6019 1.8059 0.2772  0.0950  0.2087  365 ASP B OD2 
14551 N N   . THR B 362 ? 1.0206 1.1092 0.9690 0.1140  0.0062  0.0503  366 THR B N   
14552 C CA  . THR B 362 ? 0.9830 1.0586 0.8919 0.0888  0.0112  0.0036  366 THR B CA  
14553 C C   . THR B 362 ? 1.0034 1.0612 0.8730 0.0588  0.0102  0.0030  366 THR B C   
14554 O O   . THR B 362 ? 0.9754 1.0204 0.8261 0.0407  0.0211  -0.0331 366 THR B O   
14555 C CB  . THR B 362 ? 0.9497 1.0686 0.8571 0.0749  -0.0023 -0.0148 366 THR B CB  
14556 O OG1 . THR B 362 ? 1.0493 1.2040 0.9439 0.0525  -0.0246 0.0107  366 THR B OG1 
14557 C CG2 . THR B 362 ? 0.8629 0.9967 0.8040 0.1001  0.0016  -0.0160 366 THR B CG2 
14565 N N   . GLU B 363 ? 1.0465 1.1062 0.9068 0.0516  -0.0026 0.0455  367 GLU B N   
14566 C CA  . GLU B 363 ? 1.0621 1.1018 0.8741 0.0177  -0.0012 0.0474  367 GLU B CA  
14567 C C   . GLU B 363 ? 0.9850 0.9712 0.7910 0.0186  0.0255  0.0227  367 GLU B C   
14568 O O   . GLU B 363 ? 0.9529 0.9016 0.7831 0.0456  0.0390  0.0280  367 GLU B O   
14569 C CB  . GLU B 363 ? 1.1788 1.2239 0.9815 0.0116  -0.0235 0.1082  367 GLU B CB  
14570 C CG  . GLU B 363 ? 1.2421 1.3286 0.9974 -0.0305 -0.0503 0.1216  367 GLU B CG  
14571 C CD  . GLU B 363 ? 1.3342 1.3957 1.0170 -0.0770 -0.0361 0.0987  367 GLU B CD  
14572 O OE1 . GLU B 363 ? 1.4221 1.4568 1.0726 -0.0927 -0.0395 0.1330  367 GLU B OE1 
14573 O OE2 . GLU B 363 ? 1.3177 1.3843 0.9800 -0.0970 -0.0177 0.0481  367 GLU B OE2 
14580 N N   . GLY B 364 ? 1.0014 0.9827 0.7757 -0.0142 0.0369  -0.0063 368 GLY B N   
14581 C CA  . GLY B 364 ? 1.0128 0.9539 0.7850 -0.0224 0.0592  -0.0297 368 GLY B CA  
14582 C C   . GLY B 364 ? 1.0107 0.9541 0.8128 -0.0112 0.0667  -0.0694 368 GLY B C   
14583 O O   . GLY B 364 ? 1.0346 0.9475 0.8367 -0.0219 0.0803  -0.0877 368 GLY B O   
14587 N N   . LEU B 365 ? 0.9882 0.9667 0.8124 0.0053  0.0556  -0.0803 369 LEU B N   
14588 C CA  . LEU B 365 ? 0.9420 0.9267 0.7888 0.0120  0.0564  -0.1114 369 LEU B CA  
14589 C C   . LEU B 365 ? 0.8857 0.9111 0.7510 -0.0042 0.0553  -0.1363 369 LEU B C   
14590 O O   . LEU B 365 ? 0.8917 0.9400 0.7492 -0.0144 0.0560  -0.1342 369 LEU B O   
14591 C CB  . LEU B 365 ? 0.9772 0.9681 0.8375 0.0411  0.0488  -0.1050 369 LEU B CB  
14592 C CG  . LEU B 365 ? 1.1027 1.0453 0.9584 0.0618  0.0623  -0.0954 369 LEU B CG  
14593 C CD1 . LEU B 365 ? 1.1116 1.0686 0.9824 0.0862  0.0612  -0.0942 369 LEU B CD1 
14594 C CD2 . LEU B 365 ? 1.1737 1.0705 1.0100 0.0450  0.0748  -0.1214 369 LEU B CD2 
14606 N N   . ASN B 366 ? 0.8498 0.8819 0.7407 -0.0087 0.0546  -0.1587 370 ASN B N   
14607 C CA  . ASN B 366 ? 0.7941 0.8667 0.7253 -0.0160 0.0545  -0.1775 370 ASN B CA  
14608 C C   . ASN B 366 ? 0.7642 0.8549 0.7156 0.0038  0.0365  -0.1791 370 ASN B C   
14609 O O   . ASN B 366 ? 0.7707 0.8462 0.7133 0.0095  0.0249  -0.1786 370 ASN B O   
14610 C CB  . ASN B 366 ? 0.8133 0.8939 0.7755 -0.0370 0.0610  -0.1922 370 ASN B CB  
14611 C CG  . ASN B 366 ? 0.8588 0.9202 0.7999 -0.0609 0.0832  -0.1908 370 ASN B CG  
14612 O OD1 . ASN B 366 ? 0.8552 0.9194 0.7775 -0.0695 0.0991  -0.1884 370 ASN B OD1 
14613 N ND2 . ASN B 366 ? 0.8880 0.9249 0.8233 -0.0774 0.0849  -0.1924 370 ASN B ND2 
14620 N N   . LEU B 367 ? 0.7418 0.8578 0.7121 0.0100  0.0368  -0.1819 371 LEU B N   
14621 C CA  . LEU B 367 ? 0.7127 0.8428 0.7003 0.0270  0.0211  -0.1796 371 LEU B CA  
14622 C C   . LEU B 367 ? 0.6963 0.8545 0.7401 0.0263  0.0245  -0.1907 371 LEU B C   
14623 O O   . LEU B 367 ? 0.7346 0.8979 0.7911 0.0171  0.0469  -0.2023 371 LEU B O   
14624 C CB  . LEU B 367 ? 0.7267 0.8550 0.6881 0.0373  0.0186  -0.1670 371 LEU B CB  
14625 C CG  . LEU B 367 ? 0.7571 0.8646 0.6849 0.0462  0.0169  -0.1481 371 LEU B CG  
14626 C CD1 . LEU B 367 ? 0.7468 0.8699 0.6686 0.0541  0.0106  -0.1308 371 LEU B CD1 
14627 C CD2 . LEU B 367 ? 0.7589 0.8442 0.6795 0.0565  0.0138  -0.1492 371 LEU B CD2 
14639 N N   . SER B 368 ? 0.6721 0.8452 0.7486 0.0346  0.0044  -0.1857 372 SER B N   
14640 C CA  . SER B 368 ? 0.6210 0.8213 0.7657 0.0417  0.0035  -0.1862 372 SER B CA  
14641 C C   . SER B 368 ? 0.5614 0.7598 0.7012 0.0566  -0.0169 -0.1722 372 SER B C   
14642 O O   . SER B 368 ? 0.6228 0.8112 0.7236 0.0566  -0.0376 -0.1619 372 SER B O   
14643 C CB  . SER B 368 ? 0.6512 0.8820 0.8561 0.0334  -0.0084 -0.1826 372 SER B CB  
14644 O OG  . SER B 368 ? 0.6760 0.9382 0.9667 0.0457  -0.0096 -0.1752 372 SER B OG  
14650 N N   . PHE B 369 ? 0.5044 0.7052 0.6784 0.0663  -0.0058 -0.1737 373 PHE B N   
14651 C CA  . PHE B 369 ? 0.5389 0.7333 0.7085 0.0780  -0.0210 -0.1594 373 PHE B CA  
14652 C C   . PHE B 369 ? 0.5501 0.7612 0.7999 0.0900  -0.0278 -0.1469 373 PHE B C   
14653 O O   . PHE B 369 ? 0.5680 0.7842 0.8782 0.0943  -0.0013 -0.1584 373 PHE B O   
14654 C CB  . PHE B 369 ? 0.5468 0.7213 0.6813 0.0758  -0.0027 -0.1683 373 PHE B CB  
14655 C CG  . PHE B 369 ? 0.6372 0.8041 0.7083 0.0673  -0.0016 -0.1691 373 PHE B CG  
14656 C CD1 . PHE B 369 ? 0.7123 0.8761 0.7486 0.0734  -0.0159 -0.1542 373 PHE B CD1 
14657 C CD2 . PHE B 369 ? 0.6737 0.8365 0.7245 0.0533  0.0161  -0.1813 373 PHE B CD2 
14658 C CE1 . PHE B 369 ? 0.7340 0.8946 0.7322 0.0713  -0.0125 -0.1491 373 PHE B CE1 
14659 C CE2 . PHE B 369 ? 0.7333 0.8916 0.7364 0.0479  0.0129  -0.1726 373 PHE B CE2 
14660 C CZ  . PHE B 369 ? 0.7369 0.8960 0.7218 0.0597  -0.0014 -0.1552 373 PHE B CZ  
14670 N N   . THR B 370 ? 0.5570 0.7743 0.8079 0.0950  -0.0607 -0.1214 374 THR B N   
14671 C CA  . THR B 370 ? 0.5936 0.8247 0.9204 0.1089  -0.0746 -0.0973 374 THR B CA  
14672 C C   . THR B 370 ? 0.6380 0.8462 0.9253 0.1127  -0.0894 -0.0791 374 THR B C   
14673 O O   . THR B 370 ? 0.6697 0.8717 0.8872 0.1017  -0.1104 -0.0705 374 THR B O   
14674 C CB  . THR B 370 ? 0.6371 0.9084 1.0119 0.1036  -0.1112 -0.0723 374 THR B CB  
14675 O OG1 . THR B 370 ? 0.6374 0.9325 1.0503 0.0962  -0.0948 -0.0898 374 THR B OG1 
14676 C CG2 . THR B 370 ? 0.6707 0.9625 1.1413 0.1217  -0.1290 -0.0371 374 THR B CG2 
14684 N N   . ALA B 371 ? 0.6646 0.8546 0.9943 0.1260  -0.0728 -0.0753 375 ALA B N   
14685 C CA  . ALA B 371 ? 0.6698 0.8340 0.9668 0.1271  -0.0815 -0.0583 375 ALA B CA  
14686 C C   . ALA B 371 ? 0.7166 0.8898 1.0693 0.1380  -0.1138 -0.0151 375 ALA B C   
14687 O O   . ALA B 371 ? 0.6966 0.8852 1.1466 0.1546  -0.1116 -0.0021 375 ALA B O   
14688 C CB  . ALA B 371 ? 0.6544 0.7834 0.9531 0.1279  -0.0434 -0.0807 375 ALA B CB  
14694 N N   . ILE B 372 ? 0.8008 0.9657 1.0950 0.1280  -0.1422 0.0102  376 ILE B N   
14695 C CA  . ILE B 372 ? 0.8326 1.0047 1.1593 0.1312  -0.1816 0.0598  376 ILE B CA  
14696 C C   . ILE B 372 ? 0.8838 1.0146 1.1835 0.1323  -0.1729 0.0734  376 ILE B C   
14697 O O   . ILE B 372 ? 0.8943 1.0113 1.1062 0.1142  -0.1801 0.0772  376 ILE B O   
14698 C CB  . ILE B 372 ? 0.8237 1.0186 1.0874 0.1069  -0.2262 0.0804  376 ILE B CB  
14699 C CG1 . ILE B 372 ? 0.8140 1.0400 1.0824 0.0978  -0.2270 0.0560  376 ILE B CG1 
14700 C CG2 . ILE B 372 ? 0.8471 1.0602 1.1556 0.1059  -0.2758 0.1391  376 ILE B CG2 
14701 C CD1 . ILE B 372 ? 0.9013 1.1328 1.0802 0.0651  -0.2593 0.0608  376 ILE B CD1 
14713 N N   . CYS B 373 ? 0.9297 1.0363 1.3064 0.1521  -0.1515 0.0793  377 CYS B N   
14714 C CA  . CYS B 373 ? 1.0552 1.1153 1.4152 0.1511  -0.1392 0.0912  377 CYS B CA  
14715 C C   . CYS B 373 ? 1.1616 1.2158 1.5682 0.1608  -0.1757 0.1527  377 CYS B C   
14716 O O   . CYS B 373 ? 1.1388 1.2309 1.6019 0.1693  -0.2122 0.1875  377 CYS B O   
14717 C CB  . CYS B 373 ? 1.0683 1.0894 1.4717 0.1605  -0.0874 0.0556  377 CYS B CB  
14718 S SG  . CYS B 373 ? 0.9794 1.0164 1.3631 0.1523  -0.0499 -0.0065 377 CYS B SG  
14723 N N   . ASN B 374 ? 1.3101 1.3183 1.6942 0.1564  -0.1685 0.1702  378 ASN B N   
14724 C CA  . ASN B 374 ? 1.4743 1.4645 1.9016 0.1654  -0.1997 0.2337  378 ASN B CA  
14725 C C   . ASN B 374 ? 1.6570 1.6925 2.0525 0.1510  -0.2620 0.2810  378 ASN B C   
14726 O O   . ASN B 374 ? 1.8087 1.8729 2.2890 0.1661  -0.2991 0.3291  378 ASN B O   
14727 C CB  . ASN B 374 ? 1.4550 1.4276 2.0223 0.2022  -0.1796 0.2475  378 ASN B CB  
14728 C CG  . ASN B 374 ? 1.3982 1.3249 1.9841 0.2083  -0.1125 0.1873  378 ASN B CG  
14729 O OD1 . ASN B 374 ? 1.3676 1.2742 1.8645 0.1832  -0.0889 0.1462  378 ASN B OD1 
14730 N ND2 . ASN B 374 ? 1.3949 1.3055 2.0978 0.2390  -0.0802 0.1830  378 ASN B ND2 
14737 N N   . ASN B 375 ? 1.6915 1.7333 1.9637 0.1185  -0.2719 0.2671  379 ASN B N   
14738 C CA  . ASN B 375 ? 1.7692 1.8446 1.9776 0.0918  -0.3238 0.2972  379 ASN B CA  
14739 C C   . ASN B 375 ? 1.7678 1.8959 2.0404 0.1012  -0.3385 0.2844  379 ASN B C   
14740 O O   . ASN B 375 ? 1.7789 1.9138 2.0621 0.1105  -0.2998 0.2297  379 ASN B O   
14741 C CB  . ASN B 375 ? 1.8439 1.9068 2.0528 0.0829  -0.3711 0.3717  379 ASN B CB  
14742 C CG  . ASN B 375 ? 1.9098 1.9204 2.0294 0.0633  -0.3529 0.3789  379 ASN B CG  
14743 O OD1 . ASN B 375 ? 1.9097 1.9073 1.9432 0.0462  -0.3167 0.3326  379 ASN B OD1 
14744 N ND2 . ASN B 375 ? 1.9833 1.9656 2.1307 0.0661  -0.3771 0.4406  379 ASN B ND2 
14751 N N   . GLY B 376 ? 1.8762 2.0451 2.1934 0.0958  -0.3946 0.3354  380 GLY B N   
14752 C CA  . GLY B 376 ? 1.8894 2.1150 2.2728 0.0993  -0.4108 0.3268  380 GLY B CA  
14753 C C   . GLY B 376 ? 1.7276 1.9812 2.2843 0.1415  -0.4032 0.3472  380 GLY B C   
14754 O O   . GLY B 376 ? 1.6600 1.9703 2.2901 0.1439  -0.4199 0.3495  380 GLY B O   
14758 N N   . THR B 377 ? 1.4613 1.5579 2.1707 0.0820  -0.2855 0.2362  381 THR B N   
14759 C CA  . THR B 377 ? 1.3277 1.4229 2.2016 0.1024  -0.2880 0.2351  381 THR B CA  
14760 C C   . THR B 377 ? 1.2440 1.3555 2.1635 0.1296  -0.2224 0.1756  381 THR B C   
14761 O O   . THR B 377 ? 1.2677 1.3905 2.3071 0.1436  -0.2173 0.1680  381 THR B O   
14762 C CB  . THR B 377 ? 1.3417 1.4110 2.2816 0.1017  -0.3059 0.2536  381 THR B CB  
14763 O OG1 . THR B 377 ? 1.3233 1.3863 2.1904 0.1062  -0.2598 0.2159  381 THR B OG1 
14764 C CG2 . THR B 377 ? 1.4085 1.4595 2.3119 0.0687  -0.3769 0.3198  381 THR B CG2 
14772 N N   . LEU B 378 ? 1.1482 1.2617 1.9760 0.1342  -0.1726 0.1339  382 LEU B N   
14773 C CA  . LEU B 378 ? 1.0529 1.1765 1.9114 0.1520  -0.1104 0.0782  382 LEU B CA  
14774 C C   . LEU B 378 ? 1.0079 1.1499 1.7649 0.1504  -0.0832 0.0561  382 LEU B C   
14775 O O   . LEU B 378 ? 0.9877 1.1299 1.6235 0.1398  -0.0899 0.0637  382 LEU B O   
14776 C CB  . LEU B 378 ? 1.0197 1.1288 1.8596 0.1547  -0.0759 0.0474  382 LEU B CB  
14777 C CG  . LEU B 378 ? 1.0301 1.1441 1.9126 0.1658  -0.0123 -0.0110 382 LEU B CG  
14778 C CD1 . LEU B 378 ? 1.0518 1.1633 2.1052 0.1787  -0.0059 -0.0195 382 LEU B CD1 
14779 C CD2 . LEU B 378 ? 1.0433 1.1439 1.8694 0.1609  0.0188  -0.0409 382 LEU B CD2 
14791 N N   . PHE B 379 ? 0.9892 1.1458 1.8024 0.1599  -0.0510 0.0280  383 PHE B N   
14792 C CA  . PHE B 379 ? 0.9983 1.1693 1.7295 0.1580  -0.0220 0.0056  383 PHE B CA  
14793 C C   . PHE B 379 ? 1.0252 1.1997 1.7727 0.1629  0.0399  -0.0465 383 PHE B C   
14794 O O   . PHE B 379 ? 1.0604 1.2378 1.9246 0.1698  0.0630  -0.0675 383 PHE B O   
14795 C CB  . PHE B 379 ? 0.9809 1.1666 1.7526 0.1563  -0.0441 0.0246  383 PHE B CB  
14796 C CG  . PHE B 379 ? 0.9427 1.1252 1.6457 0.1421  -0.0967 0.0678  383 PHE B CG  
14797 C CD1 . PHE B 379 ? 0.9577 1.1307 1.7041 0.1331  -0.1502 0.1111  383 PHE B CD1 
14798 C CD2 . PHE B 379 ? 0.9341 1.1208 1.5290 0.1342  -0.0923 0.0649  383 PHE B CD2 
14799 C CE1 . PHE B 379 ? 0.9942 1.1627 1.6649 0.1119  -0.1959 0.1483  383 PHE B CE1 
14800 C CE2 . PHE B 379 ? 0.9603 1.1421 1.4893 0.1169  -0.1342 0.0976  383 PHE B CE2 
14801 C CZ  . PHE B 379 ? 1.0083 1.1815 1.5694 0.1034  -0.1848 0.1382  383 PHE B CZ  
14811 N N   . GLN B 380 ? 1.0165 1.1906 1.6500 0.1567  0.0667  -0.0676 384 GLN B N   
14812 C CA  . GLN B 380 ? 0.9873 1.1624 1.6094 0.1522  0.1225  -0.1145 384 GLN B CA  
14813 C C   . GLN B 380 ? 0.8587 1.0407 1.3693 0.1434  0.1366  -0.1214 384 GLN B C   
14814 O O   . GLN B 380 ? 0.8055 0.9866 1.2307 0.1427  0.1096  -0.0978 384 GLN B O   
14815 C CB  . GLN B 380 ? 1.0576 1.2181 1.6620 0.1484  0.1391  -0.1342 384 GLN B CB  
14816 C CG  . GLN B 380 ? 1.1394 1.2874 1.8580 0.1567  0.1257  -0.1276 384 GLN B CG  
14817 C CD  . GLN B 380 ? 1.2610 1.3923 1.9663 0.1505  0.1494  -0.1543 384 GLN B CD  
14818 O OE1 . GLN B 380 ? 1.2915 1.4164 1.9172 0.1454  0.1300  -0.1391 384 GLN B OE1 
14819 N NE2 . GLN B 380 ? 1.3328 1.4573 2.1184 0.1488  0.1944  -0.1975 384 GLN B NE2 
14828 N N   . HIS B 381 ? 0.8082 0.9959 1.3235 0.1348  0.1804  -0.1546 385 HIS B N   
14829 C CA  . HIS B 381 ? 0.7865 0.9779 1.2051 0.1236  0.1930  -0.1584 385 HIS B CA  
14830 C C   . HIS B 381 ? 0.8733 1.0561 1.1994 0.1089  0.2151  -0.1786 385 HIS B C   
14831 O O   . HIS B 381 ? 0.9310 1.1129 1.2219 0.0900  0.2529  -0.2064 385 HIS B O   
14832 C CB  . HIS B 381 ? 0.7324 0.9344 1.2004 0.1163  0.2246  -0.1778 385 HIS B CB  
14833 C CG  . HIS B 381 ? 0.6570 0.8705 1.2301 0.1291  0.2004  -0.1578 385 HIS B CG  
14834 N ND1 . HIS B 381 ? 0.6187 0.8332 1.1739 0.1371  0.1501  -0.1173 385 HIS B ND1 
14835 C CD2 . HIS B 381 ? 0.6373 0.8623 1.3388 0.1330  0.2180  -0.1725 385 HIS B CD2 
14836 C CE1 . HIS B 381 ? 0.6053 0.8312 1.2662 0.1432  0.1328  -0.1041 385 HIS B CE1 
14837 N NE2 . HIS B 381 ? 0.6244 0.8582 1.3827 0.1431  0.1723  -0.1359 385 HIS B NE2 
14845 N N   . GLN B 382 ? 0.8952 1.0720 1.1808 0.1143  0.1889  -0.1623 386 GLN B N   
14846 C CA  . GLN B 382 ? 0.8932 1.0650 1.0909 0.1017  0.1959  -0.1714 386 GLN B CA  
14847 C C   . GLN B 382 ? 0.8934 1.0683 1.0266 0.1103  0.1576  -0.1386 386 GLN B C   
14848 O O   . GLN B 382 ? 0.8820 1.0602 1.0293 0.1221  0.1314  -0.1138 386 GLN B O   
14849 C CB  . GLN B 382 ? 0.8816 1.0445 1.1071 0.0976  0.2079  -0.1910 386 GLN B CB  
14850 C CG  . GLN B 382 ? 0.9472 1.1049 1.2788 0.0982  0.2381  -0.2194 386 GLN B CG  
14851 C CD  . GLN B 382 ? 1.0143 1.1600 1.3985 0.1045  0.2290  -0.2207 386 GLN B CD  
14852 O OE1 . GLN B 382 ? 0.9549 1.0995 1.3368 0.1162  0.1885  -0.1866 386 GLN B OE1 
14853 N NE2 . GLN B 382 ? 1.1303 1.2649 1.5598 0.0935  0.2689  -0.2615 386 GLN B NE2 
14862 N N   . LYS B 383 ? 0.9098 1.0838 0.9749 0.1018  0.1554  -0.1403 387 LYS B N   
14863 C CA  . LYS B 383 ? 0.9372 1.1163 0.9558 0.1098  0.1247  -0.1152 387 LYS B CA  
14864 C C   . LYS B 383 ? 0.9217 1.1006 0.9431 0.1089  0.1167  -0.1159 387 LYS B C   
14865 O O   . LYS B 383 ? 0.9248 1.1103 0.8994 0.1068  0.1039  -0.1076 387 LYS B O   
14866 C CB  . LYS B 383 ? 0.9723 1.1541 0.9187 0.1016  0.1229  -0.1106 387 LYS B CB  
14867 C CG  . LYS B 383 ? 1.0455 1.2233 0.9521 0.0780  0.1455  -0.1320 387 LYS B CG  
14868 C CD  . LYS B 383 ? 1.1576 1.3370 0.9943 0.0679  0.1321  -0.1176 387 LYS B CD  
14869 C CE  . LYS B 383 ? 1.3058 1.4811 1.1342 0.0716  0.1295  -0.1047 387 LYS B CE  
14870 N NZ  . LYS B 383 ? 1.4514 1.6207 1.2150 0.0497  0.1274  -0.0976 387 LYS B NZ  
14884 N N   . LYS B 384 ? 0.8948 1.0660 0.9798 0.1104  0.1235  -0.1251 388 LYS B N   
14885 C CA  . LYS B 384 ? 0.8463 1.0129 0.9386 0.1063  0.1195  -0.1286 388 LYS B CA  
14886 C C   . LYS B 384 ? 0.7803 0.9370 0.9532 0.1148  0.1080  -0.1188 388 LYS B C   
14887 O O   . LYS B 384 ? 0.7706 0.9214 1.0129 0.1191  0.1200  -0.1280 388 LYS B O   
14888 C CB  . LYS B 384 ? 0.9189 1.0790 0.9938 0.0879  0.1501  -0.1624 388 LYS B CB  
14889 C CG  . LYS B 384 ? 0.9629 1.1160 1.0454 0.0806  0.1484  -0.1701 388 LYS B CG  
14890 C CD  . LYS B 384 ? 1.0443 1.1902 1.0941 0.0561  0.1790  -0.2060 388 LYS B CD  
14891 C CE  . LYS B 384 ? 1.1020 1.2444 1.1351 0.0449  0.1718  -0.2104 388 LYS B CE  
14892 N NZ  . LYS B 384 ? 1.1630 1.3011 1.1390 0.0144  0.1945  -0.2412 388 LYS B NZ  
14906 N N   . CYS B 385 ? 0.7633 0.9184 0.9309 0.1152  0.0839  -0.0987 389 CYS B N   
14907 C CA  . CYS B 385 ? 0.7723 0.9136 1.0097 0.1177  0.0674  -0.0843 389 CYS B CA  
14908 C C   . CYS B 385 ? 0.7616 0.8933 0.9984 0.1083  0.0743  -0.0966 389 CYS B C   
14909 O O   . CYS B 385 ? 0.7774 0.9185 0.9516 0.1010  0.0684  -0.0926 389 CYS B O   
14910 C CB  . CYS B 385 ? 0.8185 0.9625 1.0432 0.1187  0.0301  -0.0454 389 CYS B CB  
14911 S SG  . CYS B 385 ? 0.9074 1.0545 1.1656 0.1261  0.0132  -0.0261 389 CYS B SG  
14916 N N   . SER B 386 ? 0.7333 0.8465 1.0471 0.1082  0.0874  -0.1127 390 SER B N   
14917 C CA  . SER B 386 ? 0.8141 0.9134 1.1348 0.0973  0.0991  -0.1311 390 SER B CA  
14918 C C   . SER B 386 ? 0.8691 0.9481 1.2615 0.0995  0.0733  -0.1061 390 SER B C   
14919 O O   . SER B 386 ? 0.9281 1.0042 1.3654 0.1076  0.0450  -0.0739 390 SER B O   
14920 C CB  . SER B 386 ? 0.9011 0.9903 1.2492 0.0899  0.1436  -0.1794 390 SER B CB  
14921 O OG  . SER B 386 ? 0.9601 1.0651 1.2291 0.0804  0.1636  -0.1982 390 SER B OG  
14927 N N   . HIS B 387 ? 0.8987 0.9623 1.2997 0.0889  0.0805  -0.1191 391 HIS B N   
14928 C CA  . HIS B 387 ? 0.8498 0.8878 1.3237 0.0878  0.0581  -0.0976 391 HIS B CA  
14929 C C   . HIS B 387 ? 0.8325 0.8748 1.2861 0.0861  0.0116  -0.0439 391 HIS B C   
14930 O O   . HIS B 387 ? 0.8839 0.9105 1.4090 0.0902  -0.0169 -0.0132 391 HIS B O   
14931 C CB  . HIS B 387 ? 0.8253 0.8415 1.4241 0.0994  0.0710  -0.1125 391 HIS B CB  
14932 C CG  . HIS B 387 ? 0.8947 0.9025 1.5168 0.0950  0.1235  -0.1715 391 HIS B CG  
14933 N ND1 . HIS B 387 ? 0.9009 0.9250 1.4992 0.0957  0.1582  -0.2041 391 HIS B ND1 
14934 C CD2 . HIS B 387 ? 0.9432 0.9258 1.6058 0.0852  0.1492  -0.2055 391 HIS B CD2 
14935 C CE1 . HIS B 387 ? 0.9483 0.9585 1.5655 0.0837  0.2044  -0.2565 391 HIS B CE1 
14936 N NE2 . HIS B 387 ? 0.9645 0.9491 1.6219 0.0777  0.2007  -0.2602 391 HIS B NE2 
14944 N N   . MET B 388 ? 0.7206 0.7842 1.0772 0.0771  0.0038  -0.0326 392 MET B N   
14945 C CA  . MET B 388 ? 0.7553 0.8244 1.0747 0.0683  -0.0320 0.0110  392 MET B CA  
14946 C C   . MET B 388 ? 0.8147 0.8845 1.0860 0.0493  -0.0390 0.0209  392 MET B C   
14947 O O   . MET B 388 ? 0.8163 0.8959 1.0558 0.0454  -0.0165 -0.0063 392 MET B O   
14948 C CB  . MET B 388 ? 0.7505 0.8462 1.0044 0.0734  -0.0316 0.0142  392 MET B CB  
14949 C CG  . MET B 388 ? 0.7775 0.8966 0.9687 0.0768  -0.0027 -0.0173 392 MET B CG  
14950 S SD  . MET B 388 ? 0.7685 0.9107 0.9077 0.0865  -0.0015 -0.0148 392 MET B SD  
14951 C CE  . MET B 388 ? 0.7671 0.9109 0.8711 0.0723  -0.0335 0.0244  392 MET B CE  
14961 N N   . LYS B 389 ? 0.8648 0.9243 1.1304 0.0336  -0.0720 0.0617  393 LYS B N   
14962 C CA  . LYS B 389 ? 0.9180 0.9785 1.1381 0.0107  -0.0793 0.0754  393 LYS B CA  
14963 C C   . LYS B 389 ? 0.8605 0.9538 0.9912 0.0024  -0.0731 0.0760  393 LYS B C   
14964 O O   . LYS B 389 ? 0.8523 0.9547 0.9561 0.0040  -0.0821 0.0885  393 LYS B O   
14965 C CB  . LYS B 389 ? 1.0168 1.0473 1.2685 -0.0090 -0.1178 0.1211  393 LYS B CB  
14966 C CG  . LYS B 389 ? 1.1135 1.1440 1.3126 -0.0389 -0.1253 0.1389  393 LYS B CG  
14967 C CD  . LYS B 389 ? 1.2127 1.2106 1.4327 -0.0646 -0.1684 0.1910  393 LYS B CD  
14968 C CE  . LYS B 389 ? 1.2735 1.2713 1.4365 -0.0990 -0.1716 0.2071  393 LYS B CE  
14969 N NZ  . LYS B 389 ? 1.3724 1.3347 1.5466 -0.1309 -0.2166 0.2627  393 LYS B NZ  
14983 N N   . VAL B 390 ? 0.8272 0.9386 0.9189 -0.0072 -0.0567 0.0608  394 VAL B N   
14984 C CA  . VAL B 390 ? 0.8212 0.9656 0.8453 -0.0144 -0.0469 0.0577  394 VAL B CA  
14985 C C   . VAL B 390 ? 0.8930 1.0317 0.8824 -0.0360 -0.0677 0.0911  394 VAL B C   
14986 O O   . VAL B 390 ? 0.9623 1.0775 0.9595 -0.0588 -0.0903 0.1208  394 VAL B O   
14987 C CB  . VAL B 390 ? 0.8286 0.9921 0.8333 -0.0266 -0.0322 0.0433  394 VAL B CB  
14988 C CG1 . VAL B 390 ? 0.8289 1.0294 0.7826 -0.0318 -0.0189 0.0372  394 VAL B CG1 
14989 C CG2 . VAL B 390 ? 0.7622 0.9281 0.7926 -0.0122 -0.0156 0.0115  394 VAL B CG2 
14999 N N   . GLY B 391 ? 0.8846 1.0423 0.8327 -0.0325 -0.0611 0.0868  395 GLY B N   
15000 C CA  . GLY B 391 ? 0.9191 1.0694 0.8276 -0.0548 -0.0793 0.1134  395 GLY B CA  
15001 C C   . GLY B 391 ? 0.9368 1.0722 0.8697 -0.0419 -0.0983 0.1254  395 GLY B C   
15002 O O   . GLY B 391 ? 0.9922 1.1297 0.8823 -0.0551 -0.1063 0.1359  395 GLY B O   
15006 N N   . ASP B 392 ? 0.9069 1.0277 0.9098 -0.0187 -0.1034 0.1212  396 ASP B N   
15007 C CA  . ASP B 392 ? 0.8637 0.9759 0.9033 -0.0038 -0.1172 0.1282  396 ASP B CA  
15008 C C   . ASP B 392 ? 0.8210 0.9564 0.8247 0.0123  -0.0947 0.1029  396 ASP B C   
15009 O O   . ASP B 392 ? 0.7905 0.9468 0.7675 0.0221  -0.0669 0.0752  396 ASP B O   
15010 C CB  . ASP B 392 ? 0.8366 0.9327 0.9665 0.0183  -0.1155 0.1185  396 ASP B CB  
15011 C CG  . ASP B 392 ? 0.8689 0.9345 1.0573 0.0050  -0.1465 0.1506  396 ASP B CG  
15012 O OD1 . ASP B 392 ? 0.9131 0.9683 1.0670 -0.0238 -0.1768 0.1881  396 ASP B OD1 
15013 O OD2 . ASP B 392 ? 0.8693 0.9193 1.1388 0.0208  -0.1400 0.1381  396 ASP B OD2 
15018 N N   . THR B 393 ? 0.8245 0.9555 0.8330 0.0139  -0.1103 0.1151  397 THR B N   
15019 C CA  . THR B 393 ? 0.8041 0.9516 0.7811 0.0265  -0.0931 0.0954  397 THR B CA  
15020 C C   . THR B 393 ? 0.7323 0.8778 0.7693 0.0524  -0.0873 0.0828  397 THR B C   
15021 O O   . THR B 393 ? 0.7164 0.8471 0.8155 0.0540  -0.1083 0.1003  397 THR B O   
15022 C CB  . THR B 393 ? 0.8459 0.9903 0.7712 0.0026  -0.1117 0.1149  397 THR B CB  
15023 O OG1 . THR B 393 ? 0.8985 1.0434 0.7655 -0.0284 -0.1134 0.1250  397 THR B OG1 
15024 C CG2 . THR B 393 ? 0.8516 1.0105 0.7448 0.0151  -0.0905 0.0910  397 THR B CG2 
15032 N N   . ALA B 394 ? 0.7010 0.8616 0.7235 0.0706  -0.0591 0.0536  398 ALA B N   
15033 C CA  . ALA B 394 ? 0.7075 0.8684 0.7704 0.0897  -0.0474 0.0384  398 ALA B CA  
15034 C C   . ALA B 394 ? 0.7679 0.9367 0.7936 0.0923  -0.0453 0.0359  398 ALA B C   
15035 O O   . ALA B 394 ? 0.8050 0.9850 0.7777 0.0916  -0.0330 0.0255  398 ALA B O   
15036 C CB  . ALA B 394 ? 0.6754 0.8429 0.7448 0.1021  -0.0184 0.0086  398 ALA B CB  
15042 N N   . SER B 395 ? 0.7864 0.9494 0.8477 0.0950  -0.0575 0.0451  399 SER B N   
15043 C CA  . SER B 395 ? 0.8409 1.0081 0.8733 0.0959  -0.0567 0.0428  399 SER B CA  
15044 C C   . SER B 395 ? 0.8073 0.9788 0.8710 0.1135  -0.0350 0.0227  399 SER B C   
15045 O O   . SER B 395 ? 0.8306 0.9999 0.9539 0.1210  -0.0268 0.0153  399 SER B O   
15046 C CB  . SER B 395 ? 0.9429 1.1014 0.9848 0.0792  -0.0901 0.0707  399 SER B CB  
15047 O OG  . SER B 395 ? 1.0690 1.2205 1.0746 0.0552  -0.1115 0.0922  399 SER B OG  
15053 N N   . PHE B 396 ? 0.7524 0.9284 0.7767 0.1176  -0.0237 0.0125  400 PHE B N   
15054 C CA  . PHE B 396 ? 0.7264 0.9049 0.7656 0.1287  -0.0030 -0.0043 400 PHE B CA  
15055 C C   . PHE B 396 ? 0.7316 0.9077 0.7566 0.1268  -0.0089 0.0002  400 PHE B C   
15056 O O   . PHE B 396 ? 0.7907 0.9639 0.7718 0.1195  -0.0184 0.0061  400 PHE B O   
15057 C CB  . PHE B 396 ? 0.7088 0.8929 0.7102 0.1346  0.0186  -0.0220 400 PHE B CB  
15058 C CG  . PHE B 396 ? 0.6900 0.8764 0.7009 0.1334  0.0254  -0.0293 400 PHE B CG  
15059 C CD1 . PHE B 396 ? 0.6923 0.8759 0.7394 0.1339  0.0428  -0.0449 400 PHE B CD1 
15060 C CD2 . PHE B 396 ? 0.6762 0.8671 0.6607 0.1288  0.0177  -0.0236 400 PHE B CD2 
15061 C CE1 . PHE B 396 ? 0.7007 0.8832 0.7551 0.1301  0.0503  -0.0547 400 PHE B CE1 
15062 C CE2 . PHE B 396 ? 0.6779 0.8701 0.6717 0.1258  0.0231  -0.0302 400 PHE B CE2 
15063 C CZ  . PHE B 396 ? 0.7074 0.8940 0.7350 0.1265  0.0383  -0.0457 400 PHE B CZ  
15073 N N   . SER B 397 ? 0.6797 0.8564 0.7437 0.1308  -0.0001 -0.0055 401 SER B N   
15074 C CA  . SER B 397 ? 0.6775 0.8515 0.7326 0.1286  -0.0025 -0.0036 401 SER B CA  
15075 C C   . SER B 397 ? 0.6395 0.8133 0.6735 0.1346  0.0240  -0.0206 401 SER B C   
15076 O O   . SER B 397 ? 0.7088 0.8862 0.7756 0.1353  0.0432  -0.0325 401 SER B O   
15077 C CB  . SER B 397 ? 0.7258 0.9025 0.8483 0.1244  -0.0166 0.0071  401 SER B CB  
15078 O OG  . SER B 397 ? 0.8191 0.9955 0.9780 0.1188  -0.0423 0.0257  401 SER B OG  
15084 N N   . VAL B 398 ? 0.5796 0.7478 0.5609 0.1361  0.0256  -0.0219 402 VAL B N   
15085 C CA  . VAL B 398 ? 0.6512 0.8157 0.6068 0.1388  0.0425  -0.0303 402 VAL B CA  
15086 C C   . VAL B 398 ? 0.6610 0.8155 0.6114 0.1358  0.0404  -0.0268 402 VAL B C   
15087 O O   . VAL B 398 ? 0.7152 0.8626 0.6491 0.1346  0.0278  -0.0220 402 VAL B O   
15088 C CB  . VAL B 398 ? 0.7131 0.8779 0.6283 0.1441  0.0421  -0.0312 402 VAL B CB  
15089 C CG1 . VAL B 398 ? 0.7512 0.9108 0.6430 0.1432  0.0521  -0.0330 402 VAL B CG1 
15090 C CG2 . VAL B 398 ? 0.7172 0.8922 0.6372 0.1447  0.0413  -0.0336 402 VAL B CG2 
15100 N N   . THR B 399 ? 0.6062 0.7589 0.5677 0.1311  0.0553  -0.0315 403 THR B N   
15101 C CA  . THR B 399 ? 0.6542 0.7961 0.6104 0.1262  0.0552  -0.0279 403 THR B CA  
15102 C C   . THR B 399 ? 0.7157 0.8455 0.6312 0.1247  0.0640  -0.0269 403 THR B C   
15103 O O   . THR B 399 ? 0.7390 0.8722 0.6413 0.1189  0.0774  -0.0312 403 THR B O   
15104 C CB  . THR B 399 ? 0.6914 0.8408 0.6965 0.1179  0.0650  -0.0315 403 THR B CB  
15105 O OG1 . THR B 399 ? 0.8656 1.0210 0.8769 0.1121  0.0908  -0.0441 403 THR B OG1 
15106 C CG2 . THR B 399 ? 0.5865 0.7473 0.6428 0.1191  0.0484  -0.0262 403 THR B CG2 
15114 N N   . VAL B 400 ? 0.7679 0.8815 0.6642 0.1268  0.0551  -0.0204 404 VAL B N   
15115 C CA  . VAL B 400 ? 0.7754 0.8730 0.6419 0.1253  0.0559  -0.0128 404 VAL B CA  
15116 C C   . VAL B 400 ? 0.7470 0.8286 0.6166 0.1157  0.0585  -0.0086 404 VAL B C   
15117 O O   . VAL B 400 ? 0.7350 0.8115 0.6201 0.1162  0.0519  -0.0111 404 VAL B O   
15118 C CB  . VAL B 400 ? 0.8074 0.8974 0.6621 0.1387  0.0435  -0.0095 404 VAL B CB  
15119 C CG1 . VAL B 400 ? 0.9023 0.9779 0.7383 0.1380  0.0380  0.0041  404 VAL B CG1 
15120 C CG2 . VAL B 400 ? 0.7512 0.8600 0.6093 0.1465  0.0413  -0.0155 404 VAL B CG2 
15130 N N   . ASN B 401 ? 0.7453 0.8179 0.5956 0.1024  0.0674  -0.0018 405 ASN B N   
15131 C CA  . ASN B 401 ? 0.8349 0.8904 0.6847 0.0898  0.0710  0.0042  405 ASN B CA  
15132 C C   . ASN B 401 ? 0.9307 0.9622 0.7442 0.0824  0.0636  0.0224  405 ASN B C   
15133 O O   . ASN B 401 ? 0.9483 0.9828 0.7327 0.0736  0.0648  0.0291  405 ASN B O   
15134 C CB  . ASN B 401 ? 0.8499 0.9201 0.7202 0.0722  0.0931  -0.0051 405 ASN B CB  
15135 C CG  . ASN B 401 ? 0.8846 0.9374 0.7431 0.0524  0.1014  0.0029  405 ASN B CG  
15136 O OD1 . ASN B 401 ? 0.9350 0.9888 0.7729 0.0306  0.1211  0.0021  405 ASN B OD1 
15137 N ND2 . ASN B 401 ? 0.8754 0.9105 0.7427 0.0560  0.0879  0.0093  405 ASN B ND2 
15144 N N   . ILE B 402 ? 1.0095 1.0155 0.8257 0.0837  0.0535  0.0317  406 ILE B N   
15145 C CA  . ILE B 402 ? 1.0890 1.0665 0.8812 0.0761  0.0409  0.0546  406 ILE B CA  
15146 C C   . ILE B 402 ? 1.1359 1.0995 0.9148 0.0500  0.0522  0.0620  406 ILE B C   
15147 O O   . ILE B 402 ? 1.1439 1.0991 0.9457 0.0495  0.0554  0.0555  406 ILE B O   
15148 C CB  . ILE B 402 ? 1.1277 1.0820 0.9421 0.0963  0.0231  0.0589  406 ILE B CB  
15149 C CG1 . ILE B 402 ? 1.1873 1.1122 0.9906 0.0913  0.0036  0.0880  406 ILE B CG1 
15150 C CG2 . ILE B 402 ? 1.1650 1.1064 1.0014 0.0972  0.0280  0.0455  406 ILE B CG2 
15151 C CD1 . ILE B 402 ? 1.1982 1.1347 0.9865 0.0932  -0.0109 0.1030  406 ILE B CD1 
15163 N N   . PRO B 403 ? 1.2216 1.1832 0.9610 0.0238  0.0599  0.0740  407 PRO B N   
15164 C CA  . PRO B 403 ? 1.2919 1.2436 1.0176 -0.0061 0.0769  0.0778  407 PRO B CA  
15165 C C   . PRO B 403 ? 1.4134 1.3278 1.1420 -0.0092 0.0606  0.0977  407 PRO B C   
15166 O O   . PRO B 403 ? 1.4496 1.3605 1.1973 -0.0190 0.0726  0.0907  407 PRO B O   
15167 C CB  . PRO B 403 ? 1.2995 1.2519 0.9674 -0.0383 0.0864  0.0879  407 PRO B CB  
15168 C CG  . PRO B 403 ? 1.2844 1.2584 0.9476 -0.0241 0.0828  0.0784  407 PRO B CG  
15169 C CD  . PRO B 403 ? 1.2379 1.2128 0.9426 0.0152  0.0599  0.0775  407 PRO B CD  
15177 N N   . HIS B 404 ? 1.5261 1.4122 1.2434 -0.0018 0.0324  0.1231  408 HIS B N   
15178 C CA  . HIS B 404 ? 1.5986 1.4429 1.3239 -0.0052 0.0148  0.1449  408 HIS B CA  
15179 C C   . HIS B 404 ? 1.5841 1.4135 1.3530 0.0301  -0.0067 0.1437  408 HIS B C   
15180 O O   . HIS B 404 ? 1.5386 1.3886 1.3196 0.0515  -0.0118 0.1349  408 HIS B O   
15181 C CB  . HIS B 404 ? 1.7025 1.5195 1.3779 -0.0374 -0.0009 0.1833  408 HIS B CB  
15182 C CG  . HIS B 404 ? 1.8371 1.6686 1.4607 -0.0789 0.0265  0.1806  408 HIS B CG  
15183 N ND1 . HIS B 404 ? 1.8862 1.7246 1.4505 -0.1067 0.0261  0.1935  408 HIS B ND1 
15184 C CD2 . HIS B 404 ? 1.8604 1.7014 1.4854 -0.1003 0.0577  0.1637  408 HIS B CD2 
15185 C CE1 . HIS B 404 ? 1.9344 1.7845 1.4626 -0.1444 0.0607  0.1810  408 HIS B CE1 
15186 N NE2 . HIS B 404 ? 1.9091 1.7628 1.4792 -0.1396 0.0807  0.1632  408 HIS B NE2 
15194 N N   . CYS B 405 ? 1.5906 1.3838 1.3867 0.0346  -0.0161 0.1497  409 CYS B N   
15195 C CA  . CYS B 405 ? 1.5884 1.3648 1.4329 0.0658  -0.0300 0.1431  409 CYS B CA  
15196 C C   . CYS B 405 ? 1.5848 1.3467 1.4377 0.0728  -0.0594 0.1756  409 CYS B C   
15197 O O   . CYS B 405 ? 1.5924 1.3376 1.4117 0.0482  -0.0768 0.2118  409 CYS B O   
15198 C CB  . CYS B 405 ? 1.6502 1.3875 1.5265 0.0674  -0.0298 0.1367  409 CYS B CB  
15199 S SG  . CYS B 405 ? 1.6996 1.4184 1.6420 0.1040  -0.0351 0.1157  409 CYS B SG  
15204 N N   . GLU B 406 ? 1.5732 1.3425 1.4723 0.1034  -0.0657 0.1633  410 GLU B N   
15205 C CA  . GLU B 406 ? 1.5970 1.3601 1.5228 0.1145  -0.0959 0.1921  410 GLU B CA  
15206 C C   . GLU B 406 ? 1.6168 1.3573 1.6253 0.1456  -0.1009 0.1802  410 GLU B C   
15207 O O   . GLU B 406 ? 1.6448 1.3841 1.6769 0.1584  -0.0756 0.1413  410 GLU B O   
15208 C CB  . GLU B 406 ? 1.5373 1.3451 1.4431 0.1192  -0.0952 0.1865  410 GLU B CB  
15209 C CG  . GLU B 406 ? 1.5226 1.3530 1.3533 0.0885  -0.0837 0.1901  410 GLU B CG  
15210 C CD  . GLU B 406 ? 1.4787 1.3492 1.2931 0.0929  -0.0816 0.1810  410 GLU B CD  
15211 O OE1 . GLU B 406 ? 1.4558 1.3442 1.3140 0.1212  -0.0794 0.1616  410 GLU B OE1 
15212 O OE2 . GLU B 406 ? 1.5082 1.3913 1.2649 0.0652  -0.0798 0.1911  410 GLU B OE2 
15219 N N   . ARG B 407 ? 1.6316 1.3536 1.6869 0.1549  -0.1342 0.2138  411 ARG B N   
15220 C CA  . ARG B 407 ? 1.6023 1.3013 1.7544 0.1854  -0.1383 0.2031  411 ARG B CA  
15221 C C   . ARG B 407 ? 1.5372 1.2718 1.7420 0.2127  -0.1355 0.1851  411 ARG B C   
15222 O O   . ARG B 407 ? 1.5116 1.2334 1.8050 0.2389  -0.1294 0.1661  411 ARG B O   
15223 C CB  . ARG B 407 ? 1.6836 1.3357 1.8811 0.1817  -0.1797 0.2533  411 ARG B CB  
15224 C CG  . ARG B 407 ? 1.7912 1.3985 1.9563 0.1572  -0.1802 0.2681  411 ARG B CG  
15225 C CD  . ARG B 407 ? 1.9234 1.4794 2.1394 0.1530  -0.2250 0.3216  411 ARG B CD  
15226 N NE  . ARG B 407 ? 2.0154 1.5282 2.1929 0.1249  -0.2251 0.3380  411 ARG B NE  
15227 C CZ  . ARG B 407 ? 2.1202 1.5822 2.3201 0.1103  -0.2638 0.3897  411 ARG B CZ  
15228 N NH1 . ARG B 407 ? 2.1841 1.6096 2.3440 0.0821  -0.2589 0.4005  411 ARG B NH1 
15229 N NH2 . ARG B 407 ? 2.1544 1.6020 2.4204 0.1220  -0.3101 0.4333  411 ARG B NH2 
15243 N N   . ARG B 408 ? 1.5137 1.2919 1.6711 0.2062  -0.1368 0.1875  412 ARG B N   
15244 C CA  . ARG B 408 ? 1.4953 1.3091 1.7015 0.2288  -0.1363 0.1739  412 ARG B CA  
15245 C C   . ARG B 408 ? 1.3562 1.2129 1.5080 0.2258  -0.1044 0.1375  412 ARG B C   
15246 O O   . ARG B 408 ? 1.3164 1.1844 1.3890 0.2033  -0.0979 0.1403  412 ARG B O   
15247 C CB  . ARG B 408 ? 1.5941 1.4174 1.8123 0.2235  -0.1819 0.2230  412 ARG B CB  
15248 C CG  . ARG B 408 ? 1.7004 1.4832 1.9963 0.2307  -0.2217 0.2643  412 ARG B CG  
15249 C CD  . ARG B 408 ? 1.7564 1.5581 2.1144 0.2400  -0.2645 0.2998  412 ARG B CD  
15250 N NE  . ARG B 408 ? 1.8893 1.6685 2.2119 0.2104  -0.3190 0.3657  412 ARG B NE  
15251 C CZ  . ARG B 408 ? 2.0208 1.7942 2.4165 0.2149  -0.3726 0.4139  412 ARG B CZ  
15252 N NH1 . ARG B 408 ? 2.0962 1.8465 2.4407 0.1792  -0.4242 0.4765  412 ARG B NH1 
15253 N NH2 . ARG B 408 ? 2.0573 1.8480 2.5798 0.2521  -0.3755 0.4007  412 ARG B NH2 
15267 N N   . SER B 409 ? 1.2430 1.1223 1.4430 0.2473  -0.0836 0.1032  413 SER B N   
15268 C CA  . SER B 409 ? 1.1597 1.0782 1.3167 0.2445  -0.0578 0.0727  413 SER B CA  
15269 C C   . SER B 409 ? 1.1010 1.0536 1.2327 0.2385  -0.0778 0.0954  413 SER B C   
15270 O O   . SER B 409 ? 1.1505 1.1027 1.3160 0.2414  -0.1106 0.1288  413 SER B O   
15271 C CB  . SER B 409 ? 1.1492 1.0788 1.3610 0.2632  -0.0281 0.0296  413 SER B CB  
15272 O OG  . SER B 409 ? 1.1499 1.0422 1.4065 0.2703  -0.0140 0.0107  413 SER B OG  
15278 N N   . ARG B 410 ? 1.0128 0.9936 1.0869 0.2281  -0.0601 0.0780  414 ARG B N   
15279 C CA  . ARG B 410 ? 0.9496 0.9617 0.9933 0.2194  -0.0727 0.0917  414 ARG B CA  
15280 C C   . ARG B 410 ? 0.8640 0.9103 0.9293 0.2320  -0.0537 0.0626  414 ARG B C   
15281 O O   . ARG B 410 ? 0.8330 0.8836 0.8854 0.2330  -0.0256 0.0312  414 ARG B O   
15282 C CB  . ARG B 410 ? 0.9777 0.9926 0.9408 0.1939  -0.0664 0.0956  414 ARG B CB  
15283 C CG  . ARG B 410 ? 1.0297 1.0135 0.9602 0.1741  -0.0800 0.1226  414 ARG B CG  
15284 C CD  . ARG B 410 ? 1.0322 1.0173 0.9073 0.1553  -0.0561 0.1078  414 ARG B CD  
15285 N NE  . ARG B 410 ? 1.0696 1.0347 0.8985 0.1273  -0.0653 0.1333  414 ARG B NE  
15286 C CZ  . ARG B 410 ? 1.0761 1.0513 0.8535 0.1018  -0.0709 0.1472  414 ARG B CZ  
15287 N NH1 . ARG B 410 ? 1.0428 1.0469 0.8124 0.1035  -0.0705 0.1386  414 ARG B NH1 
15288 N NH2 . ARG B 410 ? 1.1293 1.0840 0.8590 0.0708  -0.0751 0.1682  414 ARG B NH2 
15302 N N   . HIS B 411 ? 0.8963 0.9667 0.9922 0.2377  -0.0714 0.0754  415 HIS B N   
15303 C CA  . HIS B 411 ? 0.8506 0.9564 0.9627 0.2451  -0.0553 0.0519  415 HIS B CA  
15304 C C   . HIS B 411 ? 0.7952 0.9211 0.8408 0.2264  -0.0579 0.0570  415 HIS B C   
15305 O O   . HIS B 411 ? 0.7829 0.9127 0.8086 0.2137  -0.0842 0.0844  415 HIS B O   
15306 C CB  . HIS B 411 ? 0.8695 0.9929 1.0662 0.2622  -0.0715 0.0606  415 HIS B CB  
15307 C CG  . HIS B 411 ? 0.9379 1.0425 1.2180 0.2829  -0.0630 0.0488  415 HIS B CG  
15308 N ND1 . HIS B 411 ? 0.9467 1.0669 1.2856 0.2975  -0.0314 0.0115  415 HIS B ND1 
15309 C CD2 . HIS B 411 ? 0.9871 1.0562 1.3037 0.2893  -0.0792 0.0670  415 HIS B CD2 
15310 C CE1 . HIS B 411 ? 0.9700 1.0654 1.3822 0.3131  -0.0255 0.0033  415 HIS B CE1 
15311 N NE2 . HIS B 411 ? 0.9957 1.0588 1.3986 0.3100  -0.0563 0.0382  415 HIS B NE2 
15319 N N   . ILE B 412 ? 0.7632 0.8997 0.7752 0.2217  -0.0319 0.0312  416 ILE B N   
15320 C CA  . ILE B 412 ? 0.7696 0.9206 0.7280 0.2053  -0.0293 0.0309  416 ILE B CA  
15321 C C   . ILE B 412 ? 0.7778 0.9565 0.7470 0.2092  -0.0150 0.0107  416 ILE B C   
15322 O O   . ILE B 412 ? 0.8042 0.9856 0.7970 0.2178  0.0030  -0.0099 416 ILE B O   
15323 C CB  . ILE B 412 ? 0.7660 0.8999 0.6786 0.1929  -0.0154 0.0243  416 ILE B CB  
15324 C CG1 . ILE B 412 ? 0.8030 0.9082 0.7064 0.1869  -0.0265 0.0433  416 ILE B CG1 
15325 C CG2 . ILE B 412 ? 0.7561 0.9033 0.6282 0.1768  -0.0104 0.0219  416 ILE B CG2 
15326 C CD1 . ILE B 412 ? 0.8113 0.9024 0.6800 0.1739  -0.0119 0.0368  416 ILE B CD1 
15338 N N   . ILE B 413 ? 0.7793 0.9768 0.7273 0.1988  -0.0217 0.0156  417 ILE B N   
15339 C CA  . ILE B 413 ? 0.7504 0.9726 0.7042 0.1985  -0.0104 0.0001  417 ILE B CA  
15340 C C   . ILE B 413 ? 0.7367 0.9579 0.6446 0.1834  -0.0022 -0.0055 417 ILE B C   
15341 O O   . ILE B 413 ? 0.7918 1.0072 0.6697 0.1703  -0.0099 0.0041  417 ILE B O   
15342 C CB  . ILE B 413 ? 0.7479 0.9956 0.7350 0.2006  -0.0272 0.0099  417 ILE B CB  
15343 C CG1 . ILE B 413 ? 0.7472 1.0043 0.8045 0.2193  -0.0250 0.0046  417 ILE B CG1 
15344 C CG2 . ILE B 413 ? 0.7272 0.9966 0.6987 0.1908  -0.0195 -0.0008 417 ILE B CG2 
15345 C CD1 . ILE B 413 ? 0.8032 1.0890 0.9128 0.2233  -0.0449 0.0168  417 ILE B CD1 
15357 N N   . ILE B 414 ? 0.6918 0.9170 0.5962 0.1825  0.0136  -0.0210 418 ILE B N   
15358 C CA  . ILE B 414 ? 0.7141 0.9391 0.5946 0.1709  0.0200  -0.0259 418 ILE B CA  
15359 C C   . ILE B 414 ? 0.7390 0.9839 0.6286 0.1679  0.0228  -0.0324 418 ILE B C   
15360 O O   . ILE B 414 ? 0.7604 1.0130 0.6636 0.1710  0.0301  -0.0399 418 ILE B O   
15361 C CB  . ILE B 414 ? 0.7345 0.9438 0.6071 0.1689  0.0288  -0.0314 418 ILE B CB  
15362 C CG1 . ILE B 414 ? 0.7193 0.9094 0.5869 0.1713  0.0273  -0.0258 418 ILE B CG1 
15363 C CG2 . ILE B 414 ? 0.7864 0.9954 0.6531 0.1590  0.0325  -0.0341 418 ILE B CG2 
15364 C CD1 . ILE B 414 ? 0.6974 0.8740 0.5620 0.1676  0.0327  -0.0299 418 ILE B CD1 
15376 N N   . LYS B 415 ? 0.7332 0.9850 0.6128 0.1583  0.0196  -0.0318 419 LYS B N   
15377 C CA  . LYS B 415 ? 0.7564 1.0262 0.6455 0.1533  0.0208  -0.0364 419 LYS B CA  
15378 C C   . LYS B 415 ? 0.7128 0.9774 0.5880 0.1406  0.0232  -0.0406 419 LYS B C   
15379 O O   . LYS B 415 ? 0.7396 0.9926 0.5981 0.1341  0.0244  -0.0417 419 LYS B O   
15380 C CB  . LYS B 415 ? 0.8589 1.1510 0.7695 0.1564  0.0102  -0.0316 419 LYS B CB  
15381 C CG  . LYS B 415 ? 0.9114 1.2044 0.8065 0.1470  -0.0058 -0.0217 419 LYS B CG  
15382 C CD  . LYS B 415 ? 0.9683 1.2873 0.8933 0.1475  -0.0227 -0.0131 419 LYS B CD  
15383 C CE  . LYS B 415 ? 1.1072 1.4250 1.0069 0.1311  -0.0450 0.0011  419 LYS B CE  
15384 N NZ  . LYS B 415 ? 1.1692 1.5127 1.1081 0.1322  -0.0705 0.0168  419 LYS B NZ  
15398 N N   . PRO B 416 ? 0.6804 0.9518 0.5632 0.1343  0.0262  -0.0447 420 PRO B N   
15399 C CA  . PRO B 416 ? 0.7142 0.9793 0.5933 0.1223  0.0293  -0.0512 420 PRO B CA  
15400 C C   . PRO B 416 ? 0.7561 1.0330 0.6233 0.1125  0.0224  -0.0529 420 PRO B C   
15401 O O   . PRO B 416 ? 0.8016 1.0989 0.6775 0.1151  0.0118  -0.0462 420 PRO B O   
15402 C CB  . PRO B 416 ? 0.7258 0.9935 0.6186 0.1174  0.0304  -0.0504 420 PRO B CB  
15403 C CG  . PRO B 416 ? 0.6903 0.9704 0.5852 0.1226  0.0302  -0.0456 420 PRO B CG  
15404 C CD  . PRO B 416 ? 0.6706 0.9574 0.5662 0.1344  0.0283  -0.0449 420 PRO B CD  
15412 N N   . VAL B 417 ? 0.7773 1.0419 0.6278 0.0986  0.0288  -0.0631 421 VAL B N   
15413 C CA  . VAL B 417 ? 0.8416 1.1147 0.6691 0.0813  0.0203  -0.0650 421 VAL B CA  
15414 C C   . VAL B 417 ? 0.8104 1.1018 0.6550 0.0768  0.0135  -0.0651 421 VAL B C   
15415 O O   . VAL B 417 ? 0.7788 1.0650 0.6415 0.0769  0.0225  -0.0715 421 VAL B O   
15416 C CB  . VAL B 417 ? 0.9084 1.1621 0.7088 0.0605  0.0358  -0.0833 421 VAL B CB  
15417 C CG1 . VAL B 417 ? 0.8636 1.1004 0.6549 0.0639  0.0485  -0.0857 421 VAL B CG1 
15418 C CG2 . VAL B 417 ? 0.9745 1.2179 0.7977 0.0551  0.0513  -0.1011 421 VAL B CG2 
15428 N N   . GLY B 418 ? 0.8226 1.1360 0.6665 0.0716  -0.0051 -0.0551 422 GLY B N   
15429 C CA  . GLY B 418 ? 0.8162 1.1512 0.6790 0.0639  -0.0123 -0.0555 422 GLY B CA  
15430 C C   . GLY B 418 ? 0.7675 1.1227 0.6699 0.0794  -0.0099 -0.0500 422 GLY B C   
15431 O O   . GLY B 418 ? 0.7516 1.1268 0.6733 0.0714  -0.0127 -0.0511 422 GLY B O   
15435 N N   . LEU B 419 ? 0.7233 1.0742 0.6365 0.0974  -0.0026 -0.0464 423 LEU B N   
15436 C CA  . LEU B 419 ? 0.6583 1.0249 0.5999 0.1057  0.0066  -0.0469 423 LEU B CA  
15437 C C   . LEU B 419 ? 0.7003 1.0804 0.6691 0.1223  0.0038  -0.0420 423 LEU B C   
15438 O O   . LEU B 419 ? 0.7450 1.1096 0.7033 0.1315  -0.0011 -0.0368 423 LEU B O   
15439 C CB  . LEU B 419 ? 0.6217 0.9663 0.5494 0.1053  0.0209  -0.0503 423 LEU B CB  
15440 C CG  . LEU B 419 ? 0.6091 0.9395 0.5283 0.0904  0.0230  -0.0531 423 LEU B CG  
15441 C CD1 . LEU B 419 ? 0.5919 0.9029 0.5062 0.0884  0.0289  -0.0485 423 LEU B CD1 
15442 C CD2 . LEU B 419 ? 0.6146 0.9669 0.5478 0.0769  0.0209  -0.0548 423 LEU B CD2 
15454 N N   . GLY B 420 ? 0.7570 1.1654 0.7666 0.1251  0.0093  -0.0454 424 GLY B N   
15455 C CA  . GLY B 420 ? 0.7670 1.1898 0.8210 0.1419  0.0092  -0.0445 424 GLY B CA  
15456 C C   . GLY B 420 ? 0.7895 1.1914 0.8325 0.1519  0.0270  -0.0526 424 GLY B C   
15457 O O   . GLY B 420 ? 0.7646 1.1594 0.8260 0.1665  0.0221  -0.0488 424 GLY B O   
15461 N N   . ASP B 421 ? 0.8222 1.2121 0.8344 0.1414  0.0450  -0.0616 425 ASP B N   
15462 C CA  . ASP B 421 ? 0.8607 1.2321 0.8574 0.1444  0.0606  -0.0699 425 ASP B CA  
15463 C C   . ASP B 421 ? 0.8279 1.1729 0.8061 0.1555  0.0487  -0.0612 425 ASP B C   
15464 O O   . ASP B 421 ? 0.8473 1.1785 0.7998 0.1521  0.0360  -0.0517 425 ASP B O   
15465 C CB  . ASP B 421 ? 0.9070 1.2654 0.8626 0.1247  0.0710  -0.0724 425 ASP B CB  
15466 C CG  . ASP B 421 ? 0.9808 1.3618 0.9449 0.1077  0.0816  -0.0776 425 ASP B CG  
15467 O OD1 . ASP B 421 ? 1.0019 1.3938 0.9755 0.1043  0.0699  -0.0707 425 ASP B OD1 
15468 O OD2 . ASP B 421 ? 1.0163 1.4034 0.9742 0.0941  0.1033  -0.0901 425 ASP B OD2 
15473 N N   . ALA B 422 ? 0.8248 1.1621 0.8185 0.1669  0.0559  -0.0671 426 ALA B N   
15474 C CA  . ALA B 422 ? 0.8310 1.1439 0.8112 0.1762  0.0452  -0.0582 426 ALA B CA  
15475 C C   . ALA B 422 ? 0.8126 1.1069 0.7843 0.1776  0.0606  -0.0700 426 ALA B C   
15476 O O   . ALA B 422 ? 0.8386 1.1406 0.8246 0.1740  0.0808  -0.0876 426 ALA B O   
15477 C CB  . ALA B 422 ? 0.8790 1.1987 0.8952 0.1893  0.0270  -0.0457 426 ALA B CB  
15483 N N   . LEU B 423 ? 0.8109 1.0805 0.7577 0.1793  0.0529  -0.0623 427 LEU B N   
15484 C CA  . LEU B 423 ? 0.8008 1.0490 0.7365 0.1790  0.0625  -0.0710 427 LEU B CA  
15485 C C   . LEU B 423 ? 0.7976 1.0347 0.7621 0.1951  0.0557  -0.0658 427 LEU B C   
15486 O O   . LEU B 423 ? 0.8165 1.0460 0.7737 0.1984  0.0385  -0.0484 427 LEU B O   
15487 C CB  . LEU B 423 ? 0.7968 1.0265 0.6928 0.1679  0.0563  -0.0637 427 LEU B CB  
15488 C CG  . LEU B 423 ? 0.8303 1.0390 0.7064 0.1601  0.0623  -0.0710 427 LEU B CG  
15489 C CD1 . LEU B 423 ? 0.8175 1.0157 0.6694 0.1485  0.0504  -0.0592 427 LEU B CD1 
15490 C CD2 . LEU B 423 ? 0.8793 1.0716 0.7721 0.1729  0.0625  -0.0724 427 LEU B CD2 
15502 N N   . GLU B 424 ? 0.7835 1.0176 0.7810 0.2024  0.0702  -0.0815 428 GLU B N   
15503 C CA  . GLU B 424 ? 0.7784 0.9973 0.8134 0.2182  0.0624  -0.0754 428 GLU B CA  
15504 C C   . GLU B 424 ? 0.7439 0.9310 0.7469 0.2131  0.0652  -0.0777 428 GLU B C   
15505 O O   . GLU B 424 ? 0.7876 0.9655 0.7704 0.2020  0.0839  -0.0980 428 GLU B O   
15506 C CB  . GLU B 424 ? 0.8546 1.0838 0.9574 0.2302  0.0791  -0.0943 428 GLU B CB  
15507 C CG  . GLU B 424 ? 0.8844 1.1501 1.0215 0.2306  0.0841  -0.0993 428 GLU B CG  
15508 C CD  . GLU B 424 ? 0.9398 1.2207 1.1707 0.2504  0.0805  -0.0992 428 GLU B CD  
15509 O OE1 . GLU B 424 ? 0.9731 1.2352 1.2490 0.2625  0.0891  -0.1093 428 GLU B OE1 
15510 O OE2 . GLU B 424 ? 0.9472 1.2585 1.2134 0.2535  0.0674  -0.0883 428 GLU B OE2 
15517 N N   . LEU B 425 ? 0.7634 0.9341 0.7580 0.2167  0.0463  -0.0566 429 LEU B N   
15518 C CA  . LEU B 425 ? 0.7962 0.9389 0.7645 0.2109  0.0471  -0.0560 429 LEU B CA  
15519 C C   . LEU B 425 ? 0.8773 0.9980 0.8785 0.2224  0.0367  -0.0445 429 LEU B C   
15520 O O   . LEU B 425 ? 0.9012 1.0248 0.9167 0.2275  0.0161  -0.0210 429 LEU B O   
15521 C CB  . LEU B 425 ? 0.7785 0.9205 0.7037 0.1991  0.0375  -0.0420 429 LEU B CB  
15522 C CG  . LEU B 425 ? 0.8249 0.9425 0.7305 0.1918  0.0370  -0.0391 429 LEU B CG  
15523 C CD1 . LEU B 425 ? 0.8390 0.9495 0.7294 0.1813  0.0486  -0.0571 429 LEU B CD1 
15524 C CD2 . LEU B 425 ? 0.7967 0.9174 0.6786 0.1826  0.0302  -0.0255 429 LEU B CD2 
15536 N N   . LEU B 426 ? 0.9308 1.0272 0.9415 0.2228  0.0490  -0.0597 430 LEU B N   
15537 C CA  . LEU B 426 ? 0.9743 1.0424 1.0175 0.2320  0.0396  -0.0490 430 LEU B CA  
15538 C C   . LEU B 426 ? 0.9587 1.0020 0.9595 0.2186  0.0381  -0.0443 430 LEU B C   
15539 O O   . LEU B 426 ? 0.9350 0.9723 0.9097 0.2070  0.0533  -0.0647 430 LEU B O   
15540 C CB  . LEU B 426 ? 1.0348 1.0916 1.1362 0.2436  0.0589  -0.0750 430 LEU B CB  
15541 C CG  . LEU B 426 ? 1.0691 1.1014 1.2354 0.2600  0.0441  -0.0597 430 LEU B CG  
15542 C CD1 . LEU B 426 ? 1.0520 1.1056 1.2630 0.2727  0.0174  -0.0310 430 LEU B CD1 
15543 C CD2 . LEU B 426 ? 1.0784 1.0932 1.3021 0.2684  0.0724  -0.0955 430 LEU B CD2 
15555 N N   . VAL B 427 ? 0.9872 1.0168 0.9795 0.2163  0.0188  -0.0166 431 VAL B N   
15556 C CA  . VAL B 427 ? 0.9742 0.9814 0.9354 0.2028  0.0184  -0.0110 431 VAL B CA  
15557 C C   . VAL B 427 ? 1.0271 0.9983 1.0230 0.2091  0.0146  -0.0075 431 VAL B C   
15558 O O   . VAL B 427 ? 1.0245 0.9844 1.0501 0.2169  -0.0045 0.0166  431 VAL B O   
15559 C CB  . VAL B 427 ? 0.9566 0.9702 0.8813 0.1898  0.0060  0.0137  431 VAL B CB  
15560 C CG1 . VAL B 427 ? 0.9703 0.9661 0.8704 0.1744  0.0109  0.0151  431 VAL B CG1 
15561 C CG2 . VAL B 427 ? 0.9405 0.9869 0.8433 0.1859  0.0105  0.0082  431 VAL B CG2 
15571 N N   . SER B 428 ? 1.0671 1.0185 1.0607 0.2035  0.0301  -0.0301 432 SER B N   
15572 C CA  . SER B 428 ? 1.1652 1.0777 1.1926 0.2074  0.0299  -0.0317 432 SER B CA  
15573 C C   . SER B 428 ? 1.2508 1.1425 1.2425 0.1888  0.0274  -0.0241 432 SER B C   
15574 O O   . SER B 428 ? 1.3011 1.2037 1.2564 0.1741  0.0370  -0.0387 432 SER B O   
15575 C CB  . SER B 428 ? 1.1672 1.0697 1.2259 0.2127  0.0550  -0.0712 432 SER B CB  
15576 O OG  . SER B 428 ? 1.1212 1.0422 1.2298 0.2310  0.0598  -0.0787 432 SER B OG  
15582 N N   . PRO B 429 ? 1.2762 1.1387 1.2791 0.1866  0.0125  0.0009  433 PRO B N   
15583 C CA  . PRO B 429 ? 1.2798 1.1241 1.2520 0.1665  0.0124  0.0074  433 PRO B CA  
15584 C C   . PRO B 429 ? 1.3258 1.1415 1.3103 0.1616  0.0268  -0.0209 433 PRO B C   
15585 O O   . PRO B 429 ? 1.3382 1.1348 1.3638 0.1742  0.0360  -0.0412 433 PRO B O   
15586 C CB  . PRO B 429 ? 1.2813 1.1010 1.2607 0.1630  -0.0091 0.0456  433 PRO B CB  
15587 C CG  . PRO B 429 ? 1.2960 1.1026 1.3343 0.1854  -0.0202 0.0510  433 PRO B CG  
15588 C CD  . PRO B 429 ? 1.2795 1.1236 1.3279 0.2000  -0.0080 0.0275  433 PRO B CD  
15596 N N   . GLU B 430 ? 1.3520 1.1659 1.3041 0.1407  0.0302  -0.0245 434 GLU B N   
15597 C CA  . GLU B 430 ? 1.3990 1.1844 1.3526 0.1282  0.0405  -0.0491 434 GLU B CA  
15598 C C   . GLU B 430 ? 1.4593 1.2290 1.3984 0.1087  0.0324  -0.0299 434 GLU B C   
15599 O O   . GLU B 430 ? 1.4587 1.2471 1.3728 0.0905  0.0334  -0.0331 434 GLU B O   
15600 C CB  . GLU B 430 ? 1.3748 1.1816 1.3005 0.1164  0.0523  -0.0792 434 GLU B CB  
15601 C CG  . GLU B 430 ? 1.3861 1.1960 1.3266 0.1283  0.0682  -0.1074 434 GLU B CG  
15602 C CD  . GLU B 430 ? 1.4137 1.2131 1.3277 0.1063  0.0845  -0.1449 434 GLU B CD  
15603 O OE1 . GLU B 430 ? 1.4040 1.2177 1.2770 0.0831  0.0763  -0.1436 434 GLU B OE1 
15604 O OE2 . GLU B 430 ? 1.4437 1.2199 1.3805 0.1096  0.1053  -0.1761 434 GLU B OE2 
15611 N N   . CYS B 431 ? 1.5202 1.2556 1.4808 0.1113  0.0229  -0.0078 435 CYS B N   
15612 C CA  . CYS B 431 ? 1.6231 1.3387 1.5714 0.0901  0.0169  0.0118  435 CYS B CA  
15613 C C   . CYS B 431 ? 1.6573 1.3193 1.6349 0.0869  0.0173  0.0043  435 CYS B C   
15614 O O   . CYS B 431 ? 1.6990 1.3310 1.6800 0.0751  0.0073  0.0297  435 CYS B O   
15615 C CB  . CYS B 431 ? 1.6924 1.4136 1.6266 0.0859  0.0035  0.0515  435 CYS B CB  
15616 S SG  . CYS B 431 ? 1.8043 1.4819 1.7732 0.0983  -0.0192 0.0849  435 CYS B SG  
15621 N N   . ASN B 432 ? 1.6046 1.2520 1.6019 0.0941  0.0309  -0.0325 436 ASN B N   
15622 C CA  . ASN B 432 ? 1.6301 1.2256 1.6559 0.0884  0.0377  -0.0510 436 ASN B CA  
15623 C C   . ASN B 432 ? 1.6182 1.2162 1.6137 0.0659  0.0530  -0.0897 436 ASN B C   
15624 O O   . ASN B 432 ? 1.5843 1.2218 1.5468 0.0604  0.0577  -0.1044 436 ASN B O   
15625 C CB  . ASN B 432 ? 1.6560 1.2234 1.7432 0.1145  0.0443  -0.0652 436 ASN B CB  
15626 C CG  . ASN B 432 ? 1.6542 1.2108 1.7800 0.1329  0.0203  -0.0207 436 ASN B CG  
15627 O OD1 . ASN B 432 ? 1.6851 1.2164 1.8076 0.1213  0.0016  0.0151  436 ASN B OD1 
15628 N ND2 . ASN B 432 ? 1.6269 1.2031 1.7880 0.1580  0.0188  -0.0207 436 ASN B ND2 
15635 N N   . CYS B 433 ? 1.6470 1.2002 1.6528 0.0496  0.0575  -0.1039 437 CYS B N   
15636 C CA  . CYS B 433 ? 1.6956 1.2428 1.6705 0.0218  0.0689  -0.1407 437 CYS B CA  
15637 C C   . CYS B 433 ? 1.8179 1.3271 1.8165 0.0251  0.0936  -0.1875 437 CYS B C   
15638 O O   . CYS B 433 ? 1.8764 1.3506 1.9334 0.0477  0.0999  -0.1884 437 CYS B O   
15639 C CB  . CYS B 433 ? 1.7014 1.2253 1.6677 -0.0055 0.0593  -0.1291 437 CYS B CB  
15640 S SG  . CYS B 433 ? 1.6455 1.2111 1.5946 -0.0144 0.0395  -0.0805 437 CYS B SG  
15645 N N   . ASP B 434 ? 1.8874 1.4034 1.8427 -0.0005 0.1076  -0.2267 438 ASP B N   
15646 C CA  . ASP B 434 ? 1.9665 1.4453 1.9352 -0.0064 0.1388  -0.2801 438 ASP B CA  
15647 C C   . ASP B 434 ? 2.0608 1.4756 2.0693 -0.0131 0.1460  -0.2930 438 ASP B C   
15648 O O   . ASP B 434 ? 2.1660 1.5409 2.2308 0.0017  0.1704  -0.3235 438 ASP B O   
15649 C CB  . ASP B 434 ? 1.9850 1.4804 1.8815 -0.0447 0.1493  -0.3167 438 ASP B CB  
15650 C CG  . ASP B 434 ? 1.9911 1.5202 1.8711 -0.0362 0.1663  -0.3358 438 ASP B CG  
15651 O OD1 . ASP B 434 ? 1.9684 1.5219 1.8878 0.0001  0.1628  -0.3125 438 ASP B OD1 
15652 O OD2 . ASP B 434 ? 2.0403 1.5707 1.8642 -0.0701 0.1825  -0.3739 438 ASP B OD2 
15657 N N   . CYS B 435 ? 2.0685 1.4724 2.0567 -0.0354 0.1261  -0.2710 439 CYS B N   
15658 C CA  . CYS B 435 ? 2.1327 1.4740 2.1515 -0.0482 0.1317  -0.2836 439 CYS B CA  
15659 C C   . CYS B 435 ? 2.2294 1.5356 2.3240 -0.0162 0.1223  -0.2500 439 CYS B C   
15660 O O   . CYS B 435 ? 2.3523 1.5986 2.4883 -0.0212 0.1288  -0.2617 439 CYS B O   
15661 C CB  . CYS B 435 ? 2.0707 1.4159 2.0453 -0.0853 0.1118  -0.2684 439 CYS B CB  
15662 S SG  . CYS B 435 ? 1.9737 1.3644 1.9456 -0.0763 0.0785  -0.1994 439 CYS B SG  
15667 N N   . GLN B 436 ? 2.1341 1.4732 2.2470 0.0134  0.1049  -0.2071 440 GLN B N   
15668 C CA  . GLN B 436 ? 2.1413 1.4463 2.3210 0.0385  0.0888  -0.1687 440 GLN B CA  
15669 C C   . GLN B 436 ? 2.1688 1.4281 2.4325 0.0624  0.1092  -0.2008 440 GLN B C   
15670 O O   . GLN B 436 ? 2.2186 1.4245 2.5486 0.0725  0.0991  -0.1826 440 GLN B O   
15671 C CB  . GLN B 436 ? 2.1140 1.4658 2.2866 0.0593  0.0654  -0.1189 440 GLN B CB  
15672 C CG  . GLN B 436 ? 2.1090 1.4868 2.2284 0.0381  0.0440  -0.0763 440 GLN B CG  
15673 C CD  . GLN B 436 ? 2.0665 1.4731 2.1845 0.0542  0.0221  -0.0263 440 GLN B CD  
15674 O OE1 . GLN B 436 ? 2.0687 1.4607 2.1804 0.0429  0.0029  0.0167  440 GLN B OE1 
15675 N NE2 . GLN B 436 ? 2.0281 1.4749 2.1470 0.0763  0.0254  -0.0323 440 GLN B NE2 
15684 N N   . LYS B 437 ? 2.1540 1.4322 2.4214 0.0701  0.1389  -0.2488 441 LYS B N   
15685 C CA  . LYS B 437 ? 2.1917 1.4332 2.5533 0.0951  0.1640  -0.2832 441 LYS B CA  
15686 C C   . LYS B 437 ? 2.2920 1.4651 2.6852 0.0765  0.1894  -0.3291 441 LYS B C   
15687 O O   . LYS B 437 ? 2.2921 1.4155 2.7882 0.0989  0.1974  -0.3374 441 LYS B O   
15688 C CB  . LYS B 437 ? 2.1685 1.4518 2.5222 0.1033  0.1949  -0.3260 441 LYS B CB  
15689 C CG  . LYS B 437 ? 2.1169 1.4616 2.4638 0.1282  0.1731  -0.2851 441 LYS B CG  
15690 C CD  . LYS B 437 ? 2.1015 1.4377 2.5083 0.1560  0.1327  -0.2195 441 LYS B CD  
15691 C CE  . LYS B 437 ? 2.1332 1.4163 2.6662 0.1830  0.1372  -0.2260 441 LYS B CE  
15692 N NZ  . LYS B 437 ? 2.1357 1.3845 2.7053 0.1901  0.0926  -0.1606 441 LYS B NZ  
15706 N N   . GLU B 438 ? 1.7708 1.7227 2.3856 0.1785  -0.1847 0.0221  442 GLU B N   
15707 C CA  . GLU B 438 ? 1.8428 1.7791 2.3645 0.1858  -0.1631 0.0197  442 GLU B CA  
15708 C C   . GLU B 438 ? 1.8725 1.8086 2.3458 0.1714  -0.1814 -0.0224 442 GLU B C   
15709 O O   . GLU B 438 ? 2.0133 1.9534 2.4429 0.1645  -0.1966 -0.0454 442 GLU B O   
15710 C CB  . GLU B 438 ? 1.8466 1.7775 2.3185 0.1971  -0.1546 0.0338  442 GLU B CB  
15711 C CG  . GLU B 438 ? 1.7609 1.7091 2.2297 0.1903  -0.1855 0.0129  442 GLU B CG  
15712 C CD  . GLU B 438 ? 1.7230 1.6764 2.1792 0.2066  -0.1798 0.0421  442 GLU B CD  
15713 O OE1 . GLU B 438 ? 1.7461 1.6868 2.1945 0.2232  -0.1507 0.0789  442 GLU B OE1 
15714 O OE2 . GLU B 438 ? 1.6863 1.6586 2.1413 0.2057  -0.2023 0.0318  442 GLU B OE2 
15721 N N   . VAL B 439 ? 1.7472 1.6824 2.2340 0.1680  -0.1783 -0.0278 443 VAL B N   
15722 C CA  . VAL B 439 ? 1.8112 1.7465 2.2630 0.1563  -0.1930 -0.0622 443 VAL B CA  
15723 C C   . VAL B 439 ? 1.8856 1.7956 2.2486 0.1536  -0.1755 -0.0757 443 VAL B C   
15724 O O   . VAL B 439 ? 1.9458 1.8587 2.2753 0.1405  -0.1901 -0.1044 443 VAL B O   
15725 C CB  . VAL B 439 ? 1.7935 1.7372 2.2826 0.1568  -0.1947 -0.0586 443 VAL B CB  
15726 C CG1 . VAL B 439 ? 1.7690 1.7377 2.3315 0.1492  -0.2275 -0.0652 443 VAL B CG1 
15727 C CG2 . VAL B 439 ? 1.8141 1.7489 2.3171 0.1723  -0.1606 -0.0220 443 VAL B CG2 
15737 N N   . GLU B 440 ? 1.8098 1.6922 2.1342 0.1652  -0.1424 -0.0563 444 GLU B N   
15738 C CA  . GLU B 440 ? 1.7901 1.6364 2.0241 0.1600  -0.1248 -0.0739 444 GLU B CA  
15739 C C   . GLU B 440 ? 1.6898 1.5282 1.9083 0.1472  -0.1290 -0.0995 444 GLU B C   
15740 O O   . GLU B 440 ? 1.6621 1.4991 1.8435 0.1290  -0.1431 -0.1277 444 GLU B O   
15741 C CB  . GLU B 440 ? 1.8396 1.6904 2.0257 0.1503  -0.1415 -0.0881 444 GLU B CB  
15742 C CG  . GLU B 440 ? 1.8722 1.7151 2.0368 0.1674  -0.1257 -0.0603 444 GLU B CG  
15743 C CD  . GLU B 440 ? 1.8398 1.7124 2.0002 0.1635  -0.1537 -0.0616 444 GLU B CD  
15744 O OE1 . GLU B 440 ? 1.8811 1.7432 1.9647 0.1584  -0.1571 -0.0721 444 GLU B OE1 
15745 O OE2 . GLU B 440 ? 1.7731 1.6788 2.0066 0.1660  -0.1730 -0.0522 444 GLU B OE2 
15752 N N   . VAL B 441 ? 1.5828 1.4198 1.8351 0.1579  -0.1154 -0.0847 445 VAL B N   
15753 C CA  . VAL B 441 ? 1.5351 1.3700 1.7818 0.1512  -0.1189 -0.1006 445 VAL B CA  
15754 C C   . VAL B 441 ? 1.5322 1.3170 1.7002 0.1432  -0.0931 -0.1177 445 VAL B C   
15755 O O   . VAL B 441 ? 1.5638 1.3077 1.6811 0.1490  -0.0653 -0.1130 445 VAL B O   
15756 C CB  . VAL B 441 ? 1.5284 1.3786 1.8296 0.1678  -0.1118 -0.0745 445 VAL B CB  
15757 C CG1 . VAL B 441 ? 1.5002 1.3640 1.8050 0.1625  -0.1276 -0.0890 445 VAL B CG1 
15758 C CG2 . VAL B 441 ? 1.5056 1.3953 1.8869 0.1736  -0.1306 -0.0529 445 VAL B CG2 
15768 N N   . ASN B 442 ? 1.5073 1.2909 1.6626 0.1297  -0.1006 -0.1382 446 ASN B N   
15769 C CA  . ASN B 442 ? 1.5107 1.2444 1.6013 0.1162  -0.0777 -0.1569 446 ASN B CA  
15770 C C   . ASN B 442 ? 1.5791 1.2917 1.6140 0.0975  -0.0818 -0.1779 446 ASN B C   
15771 O O   . ASN B 442 ? 1.6662 1.3212 1.6369 0.0935  -0.0549 -0.1868 446 ASN B O   
15772 C CB  . ASN B 442 ? 1.5059 1.1910 1.5759 0.1359  -0.0343 -0.1374 446 ASN B CB  
15773 C CG  . ASN B 442 ? 1.4669 1.1792 1.5889 0.1539  -0.0342 -0.1147 446 ASN B CG  
15774 O OD1 . ASN B 442 ? 1.4388 1.1955 1.5954 0.1476  -0.0652 -0.1215 446 ASN B OD1 
15775 N ND2 . ASN B 442 ? 1.4972 1.1834 1.6218 0.1785  0.0013  -0.0867 446 ASN B ND2 
15782 N N   . SER B 443 ? 1.5815 1.3399 1.6386 0.0869  -0.1165 -0.1863 447 SER B N   
15783 C CA  . SER B 443 ? 1.6589 1.4129 1.6689 0.0694  -0.1295 -0.2032 447 SER B CA  
15784 C C   . SER B 443 ? 1.7166 1.4532 1.6908 0.0377  -0.1339 -0.2339 447 SER B C   
15785 O O   . SER B 443 ? 1.6923 1.4397 1.6951 0.0292  -0.1344 -0.2403 447 SER B O   
15786 C CB  . SER B 443 ? 1.6398 1.4535 1.6945 0.0710  -0.1643 -0.1972 447 SER B CB  
15787 O OG  . SER B 443 ? 1.6260 1.4787 1.7117 0.0538  -0.1892 -0.2140 447 SER B OG  
15793 N N   . SER B 444 ? 1.7954 1.5050 1.7055 0.0193  -0.1373 -0.2525 448 SER B N   
15794 C CA  . SER B 444 ? 1.8444 1.5410 1.7276 -0.0180 -0.1469 -0.2834 448 SER B CA  
15795 C C   . SER B 444 ? 1.8054 1.5765 1.7514 -0.0338 -0.1827 -0.2873 448 SER B C   
15796 O O   . SER B 444 ? 1.8405 1.6162 1.8050 -0.0570 -0.1829 -0.3011 448 SER B O   
15797 C CB  . SER B 444 ? 1.9321 1.5917 1.7321 -0.0368 -0.1532 -0.3052 448 SER B CB  
15798 O OG  . SER B 444 ? 1.9305 1.6516 1.7405 -0.0408 -0.1932 -0.3021 448 SER B OG  
15804 N N   . LYS B 445 ? 1.7737 1.6017 1.7559 -0.0191 -0.2085 -0.2721 449 LYS B N   
15805 C CA  . LYS B 445 ? 1.7056 1.6045 1.7464 -0.0284 -0.2395 -0.2729 449 LYS B CA  
15806 C C   . LYS B 445 ? 1.6282 1.5442 1.7222 -0.0255 -0.2305 -0.2719 449 LYS B C   
15807 O O   . LYS B 445 ? 1.6019 1.5626 1.7335 -0.0406 -0.2454 -0.2783 449 LYS B O   
15808 C CB  . LYS B 445 ? 1.6701 1.6125 1.7418 -0.0036 -0.2586 -0.2510 449 LYS B CB  
15809 C CG  . LYS B 445 ? 1.7268 1.6624 1.7429 -0.0042 -0.2699 -0.2478 449 LYS B CG  
15810 C CD  . LYS B 445 ? 1.6907 1.6482 1.7323 0.0280  -0.2733 -0.2176 449 LYS B CD  
15811 C CE  . LYS B 445 ? 1.7032 1.6102 1.6818 0.0442  -0.2500 -0.2054 449 LYS B CE  
15812 N NZ  . LYS B 445 ? 1.6560 1.5897 1.6469 0.0693  -0.2577 -0.1747 449 LYS B NZ  
15826 N N   . CYS B 446 ? 1.5474 1.4336 1.6461 -0.0046 -0.2065 -0.2614 450 CYS B N   
15827 C CA  . CYS B 446 ? 1.4813 1.3824 1.6175 0.0017  -0.1988 -0.2595 450 CYS B CA  
15828 C C   . CYS B 446 ? 1.5066 1.3616 1.6136 -0.0137 -0.1708 -0.2675 450 CYS B C   
15829 O O   . CYS B 446 ? 1.5222 1.3467 1.6225 0.0028  -0.1471 -0.2567 450 CYS B O   
15830 C CB  . CYS B 446 ? 1.4185 1.3246 1.5820 0.0330  -0.1968 -0.2424 450 CYS B CB  
15831 S SG  . CYS B 446 ? 1.3543 1.2981 1.5546 0.0501  -0.2230 -0.2307 450 CYS B SG  
15836 N N   . HIS B 447 ? 1.5232 1.3757 1.6169 -0.0470 -0.1750 -0.2851 451 HIS B N   
15837 C CA  . HIS B 447 ? 1.5598 1.3670 1.6330 -0.0696 -0.1491 -0.2950 451 HIS B CA  
15838 C C   . HIS B 447 ? 1.5984 1.3292 1.6234 -0.0562 -0.1142 -0.2897 451 HIS B C   
15839 O O   . HIS B 447 ? 1.5918 1.3072 1.6262 -0.0349 -0.0901 -0.2729 451 HIS B O   
15840 C CB  . HIS B 447 ? 1.5278 1.3650 1.6454 -0.0660 -0.1391 -0.2864 451 HIS B CB  
15841 C CG  . HIS B 447 ? 1.5966 1.4090 1.7139 -0.0991 -0.1198 -0.2959 451 HIS B CG  
15842 N ND1 . HIS B 447 ? 1.6156 1.3930 1.7304 -0.0915 -0.0840 -0.2838 451 HIS B ND1 
15843 C CD2 . HIS B 447 ? 1.6351 1.4532 1.7583 -0.1414 -0.1320 -0.3147 451 HIS B CD2 
15844 C CE1 . HIS B 447 ? 1.6626 1.4203 1.7845 -0.1280 -0.0707 -0.2940 451 HIS B CE1 
15845 N NE2 . HIS B 447 ? 1.6747 1.4576 1.8039 -0.1611 -0.1014 -0.3146 451 HIS B NE2 
15853 N N   . HIS B 448 ? 1.6420 1.3251 1.6121 -0.0658 -0.1100 -0.3024 452 HIS B N   
15854 C CA  . HIS B 448 ? 1.7116 1.3118 1.6299 -0.0550 -0.0700 -0.3001 452 HIS B CA  
15855 C C   . HIS B 448 ? 1.6496 1.2534 1.5900 -0.0111 -0.0513 -0.2681 452 HIS B C   
15856 O O   . HIS B 448 ? 1.6970 1.2600 1.6321 0.0039  -0.0171 -0.2539 452 HIS B O   
15857 C CB  . HIS B 448 ? 1.7788 1.3251 1.6833 -0.0808 -0.0426 -0.3128 452 HIS B CB  
15858 C CG  . HIS B 448 ? 1.7872 1.3369 1.6843 -0.1303 -0.0648 -0.3442 452 HIS B CG  
15859 N ND1 . HIS B 448 ? 1.8452 1.3652 1.6848 -0.1540 -0.0810 -0.3716 452 HIS B ND1 
15860 C CD2 . HIS B 448 ? 1.7669 1.3489 1.7087 -0.1614 -0.0739 -0.3511 452 HIS B CD2 
15861 C CE1 . HIS B 448 ? 1.8679 1.4059 1.7205 -0.2007 -0.1050 -0.3957 452 HIS B CE1 
15862 N NE2 . HIS B 448 ? 1.8258 1.4028 1.7461 -0.2062 -0.0992 -0.3822 452 HIS B NE2 
15870 N N   . GLY B 449 ? 1.5592 1.2146 1.5293 0.0091  -0.0752 -0.2545 453 GLY B N   
15871 C CA  . GLY B 449 ? 1.4982 1.1635 1.4965 0.0455  -0.0645 -0.2251 453 GLY B CA  
15872 C C   . GLY B 449 ? 1.4691 1.1761 1.5173 0.0589  -0.0724 -0.2113 453 GLY B C   
15873 O O   . GLY B 449 ? 1.4494 1.1541 1.5144 0.0852  -0.0586 -0.1873 453 GLY B O   
15877 N N   . ASN B 450 ? 1.4675 1.2152 1.5391 0.0432  -0.0943 -0.2245 454 ASN B N   
15878 C CA  . ASN B 450 ? 1.4807 1.2633 1.5852 0.0569  -0.1003 -0.2150 454 ASN B CA  
15879 C C   . ASN B 450 ? 1.5161 1.3527 1.6616 0.0717  -0.1331 -0.2120 454 ASN B C   
15880 O O   . ASN B 450 ? 1.5627 1.4289 1.7276 0.0813  -0.1434 -0.2113 454 ASN B O   
15881 C CB  . ASN B 450 ? 1.4427 1.2342 1.5487 0.0352  -0.0969 -0.2284 454 ASN B CB  
15882 C CG  . ASN B 450 ? 1.4132 1.1572 1.4960 0.0341  -0.0596 -0.2194 454 ASN B CG  
15883 O OD1 . ASN B 450 ? 1.4019 1.1278 1.4785 0.0599  -0.0419 -0.1977 454 ASN B OD1 
15884 N ND2 . ASN B 450 ? 1.4230 1.1488 1.4986 0.0039  -0.0475 -0.2332 454 ASN B ND2 
15891 N N   . GLY B 451 ? 1.5322 1.3768 1.6875 0.0744  -0.1472 -0.2102 455 GLY B N   
15892 C CA  . GLY B 451 ? 1.4881 1.3734 1.6862 0.0870  -0.1748 -0.2064 455 GLY B CA  
15893 C C   . GLY B 451 ? 1.5086 1.3878 1.7130 0.0927  -0.1769 -0.1948 455 GLY B C   
15894 O O   . GLY B 451 ? 1.5713 1.4143 1.7400 0.0907  -0.1554 -0.1896 455 GLY B O   
15898 N N   . SER B 452 ? 1.4328 1.3426 1.6802 0.1009  -0.1998 -0.1903 456 SER B N   
15899 C CA  . SER B 452 ? 1.4591 1.3677 1.7219 0.1084  -0.2005 -0.1739 456 SER B CA  
15900 C C   . SER B 452 ? 1.4517 1.3855 1.7277 0.1028  -0.2214 -0.1813 456 SER B C   
15901 O O   . SER B 452 ? 1.4190 1.3790 1.7260 0.1030  -0.2408 -0.1921 456 SER B O   
15902 C CB  . SER B 452 ? 1.4693 1.3897 1.7847 0.1238  -0.2062 -0.1543 456 SER B CB  
15903 O OG  . SER B 452 ? 1.4501 1.3907 1.7894 0.1249  -0.2253 -0.1654 456 SER B OG  
15909 N N   . PHE B 453 ? 1.4646 1.3888 1.7128 0.1006  -0.2158 -0.1741 457 PHE B N   
15910 C CA  . PHE B 453 ? 1.4332 1.3852 1.6948 0.1000  -0.2351 -0.1727 457 PHE B CA  
15911 C C   . PHE B 453 ? 1.4231 1.3841 1.7381 0.1172  -0.2396 -0.1506 457 PHE B C   
15912 O O   . PHE B 453 ? 1.4398 1.3837 1.7522 0.1276  -0.2234 -0.1277 457 PHE B O   
15913 C CB  . PHE B 453 ? 1.4435 1.3839 1.6475 0.0922  -0.2308 -0.1719 457 PHE B CB  
15914 C CG  . PHE B 453 ? 1.4079 1.3876 1.6192 0.0874  -0.2556 -0.1735 457 PHE B CG  
15915 C CD1 . PHE B 453 ? 1.3644 1.3775 1.5973 0.0746  -0.2725 -0.1909 457 PHE B CD1 
15916 C CD2 . PHE B 453 ? 1.4134 1.4002 1.6115 0.0986  -0.2596 -0.1530 457 PHE B CD2 
15917 C CE1 . PHE B 453 ? 1.3467 1.4037 1.5954 0.0729  -0.2946 -0.1872 457 PHE B CE1 
15918 C CE2 . PHE B 453 ? 1.4024 1.4316 1.6098 0.0974  -0.2838 -0.1493 457 PHE B CE2 
15919 C CZ  . PHE B 453 ? 1.3690 1.4353 1.6048 0.0843  -0.3020 -0.1663 457 PHE B CZ  
15929 N N   . GLN B 454 ? 1.4287 1.4125 1.7928 0.1207  -0.2585 -0.1565 458 GLN B N   
15930 C CA  . GLN B 454 ? 1.4022 1.3865 1.8244 0.1326  -0.2630 -0.1394 458 GLN B CA  
15931 C C   . GLN B 454 ? 1.5299 1.5279 1.9721 0.1415  -0.2696 -0.1240 458 GLN B C   
15932 O O   . GLN B 454 ? 1.4184 1.4083 1.8713 0.1514  -0.2584 -0.0957 458 GLN B O   
15933 C CB  . GLN B 454 ? 1.3995 1.3874 1.8605 0.1315  -0.2783 -0.1578 458 GLN B CB  
15934 C CG  . GLN B 454 ? 1.3914 1.3743 1.9173 0.1371  -0.2868 -0.1458 458 GLN B CG  
15935 C CD  . GLN B 454 ? 1.4050 1.3854 1.9551 0.1321  -0.3023 -0.1634 458 GLN B CD  
15936 O OE1 . GLN B 454 ? 1.4085 1.3922 1.9237 0.1290  -0.3058 -0.1835 458 GLN B OE1 
15937 N NE2 . GLN B 454 ? 1.4295 1.4047 2.0391 0.1305  -0.3121 -0.1539 458 GLN B NE2 
15946 N N   . CYS B 455 ? 1.6975 1.7178 2.1466 0.1415  -0.2841 -0.1373 459 CYS B N   
15947 C CA  . CYS B 455 ? 1.8993 1.9365 2.3727 0.1544  -0.2900 -0.1183 459 CYS B CA  
15948 C C   . CYS B 455 ? 1.6585 1.7314 2.1103 0.1507  -0.3018 -0.1270 459 CYS B C   
15949 O O   . CYS B 455 ? 0.9983 1.0934 1.4863 0.1623  -0.3101 -0.1230 459 CYS B O   
15950 C CB  . CYS B 455 ? 2.0265 2.0543 2.5652 0.1650  -0.2953 -0.1183 459 CYS B CB  
15951 S SG  . CYS B 455 ? 1.8087 1.8038 2.3963 0.1648  -0.2879 -0.1037 459 CYS B SG  
15956 N N   . GLY B 456 ? 1.4529 1.5317 1.8504 0.1342  -0.3019 -0.1379 460 GLY B N   
15957 C CA  . GLY B 456 ? 1.3923 1.5110 1.7796 0.1241  -0.3162 -0.1477 460 GLY B CA  
15958 C C   . GLY B 456 ? 1.3608 1.4877 1.7586 0.1130  -0.3155 -0.1740 460 GLY B C   
15959 O O   . GLY B 456 ? 1.4142 1.5783 1.8137 0.1020  -0.3247 -0.1808 460 GLY B O   
15963 N N   . VAL B 457 ? 1.2911 1.3882 1.6976 0.1158  -0.3053 -0.1864 461 VAL B N   
15964 C CA  . VAL B 457 ? 1.2646 1.3637 1.6706 0.1094  -0.3005 -0.2086 461 VAL B CA  
15965 C C   . VAL B 457 ? 1.2846 1.3470 1.6574 0.1013  -0.2880 -0.2156 461 VAL B C   
15966 O O   . VAL B 457 ? 1.2950 1.3324 1.6661 0.1067  -0.2838 -0.2040 461 VAL B O   
15967 C CB  . VAL B 457 ? 1.2044 1.3054 1.6513 0.1279  -0.3025 -0.2165 461 VAL B CB  
15968 C CG1 . VAL B 457 ? 1.1847 1.2883 1.6202 0.1254  -0.2942 -0.2373 461 VAL B CG1 
15969 C CG2 . VAL B 457 ? 1.1890 1.3221 1.6744 0.1422  -0.3097 -0.2030 461 VAL B CG2 
15979 N N   . CYS B 458 ? 1.2579 1.3192 1.6092 0.0900  -0.2792 -0.2301 462 CYS B N   
15980 C CA  . CYS B 458 ? 1.2364 1.2641 1.5553 0.0847  -0.2643 -0.2323 462 CYS B CA  
15981 C C   . CYS B 458 ? 1.2526 1.2718 1.5846 0.0985  -0.2649 -0.2380 462 CYS B C   
15982 O O   . CYS B 458 ? 1.2579 1.2914 1.5979 0.1042  -0.2670 -0.2504 462 CYS B O   
15983 C CB  . CYS B 458 ? 1.2281 1.2524 1.5154 0.0648  -0.2514 -0.2417 462 CYS B CB  
15984 S SG  . CYS B 458 ? 1.2746 1.2846 1.5210 0.0422  -0.2500 -0.2410 462 CYS B SG  
15989 N N   . ALA B 459 ? 1.2777 1.2755 1.6110 0.1047  -0.2632 -0.2278 463 ALA B N   
15990 C CA  . ALA B 459 ? 1.2802 1.2723 1.6187 0.1142  -0.2679 -0.2319 463 ALA B CA  
15991 C C   . ALA B 459 ? 1.3067 1.2843 1.6072 0.1110  -0.2483 -0.2284 463 ALA B C   
15992 O O   . ALA B 459 ? 1.3193 1.2775 1.6093 0.1111  -0.2346 -0.2127 463 ALA B O   
15993 C CB  . ALA B 459 ? 1.2950 1.2812 1.6685 0.1207  -0.2785 -0.2182 463 ALA B CB  
15999 N N   . CYS B 460 ? 1.3443 1.3284 1.6250 0.1108  -0.2423 -0.2401 464 CYS B N   
16000 C CA  . CYS B 460 ? 1.4390 1.4058 1.6855 0.1070  -0.2185 -0.2339 464 CYS B CA  
16001 C C   . CYS B 460 ? 1.4583 1.4149 1.6979 0.1218  -0.2169 -0.2198 464 CYS B C   
16002 O O   . CYS B 460 ? 1.4653 1.4363 1.7227 0.1332  -0.2393 -0.2218 464 CYS B O   
16003 C CB  . CYS B 460 ? 1.5091 1.4887 1.7424 0.1048  -0.2085 -0.2445 464 CYS B CB  
16004 S SG  . CYS B 460 ? 1.5289 1.5320 1.7806 0.0848  -0.2080 -0.2542 464 CYS B SG  
16009 N N   . HIS B 461 ? 1.4482 1.3792 1.6635 0.1211  -0.1909 -0.2052 465 HIS B N   
16010 C CA  . HIS B 461 ? 1.4497 1.3754 1.6591 0.1385  -0.1847 -0.1851 465 HIS B CA  
16011 C C   . HIS B 461 ? 1.4694 1.4073 1.6550 0.1494  -0.1851 -0.1879 465 HIS B C   
16012 O O   . HIS B 461 ? 1.4787 1.4194 1.6492 0.1421  -0.1770 -0.2018 465 HIS B O   
16013 C CB  . HIS B 461 ? 1.4587 1.3452 1.6476 0.1380  -0.1497 -0.1669 465 HIS B CB  
16014 C CG  . HIS B 461 ? 1.4257 1.2973 1.6290 0.1369  -0.1450 -0.1579 465 HIS B CG  
16015 N ND1 . HIS B 461 ? 1.3857 1.2830 1.6279 0.1391  -0.1704 -0.1572 465 HIS B ND1 
16016 C CD2 . HIS B 461 ? 1.4468 1.2757 1.6271 0.1354  -0.1139 -0.1485 465 HIS B CD2 
16017 C CE1 . HIS B 461 ? 1.3940 1.2703 1.6380 0.1408  -0.1539 -0.1439 465 HIS B CE1 
16018 N NE2 . HIS B 461 ? 1.4374 1.2707 1.6396 0.1395  -0.1197 -0.1402 465 HIS B NE2 
16026 N N   . PRO B 462 ? 1.4614 1.4108 1.6436 0.1685  -0.1942 -0.1720 466 PRO B N   
16027 C CA  . PRO B 462 ? 1.4769 1.4361 1.6233 0.1830  -0.1924 -0.1712 466 PRO B CA  
16028 C C   . PRO B 462 ? 1.4925 1.4243 1.6090 0.1801  -0.1501 -0.1603 466 PRO B C   
16029 O O   . PRO B 462 ? 1.4538 1.3544 1.5703 0.1757  -0.1222 -0.1437 466 PRO B O   
16030 C CB  . PRO B 462 ? 1.4933 1.4712 1.6439 0.2034  -0.2100 -0.1486 466 PRO B CB  
16031 C CG  . PRO B 462 ? 1.4713 1.4432 1.6639 0.2001  -0.2065 -0.1303 466 PRO B CG  
16032 C CD  . PRO B 462 ? 1.4438 1.4046 1.6577 0.1789  -0.2084 -0.1517 466 PRO B CD  
16040 N N   . GLY B 463 ? 1.5166 1.4562 1.6081 0.1827  -0.1422 -0.1699 467 GLY B N   
16041 C CA  . GLY B 463 ? 1.5767 1.4937 1.6486 0.1776  -0.1011 -0.1583 467 GLY B CA  
16042 C C   . GLY B 463 ? 1.5339 1.4412 1.6269 0.1475  -0.0871 -0.1745 467 GLY B C   
16043 O O   . GLY B 463 ? 1.6096 1.4941 1.6963 0.1357  -0.0530 -0.1654 467 GLY B O   
16047 N N   . HIS B 464 ? 1.3999 1.3250 1.5205 0.1339  -0.1130 -0.1964 468 HIS B N   
16048 C CA  . HIS B 464 ? 1.3813 1.3082 1.5244 0.1057  -0.1078 -0.2102 468 HIS B CA  
16049 C C   . HIS B 464 ? 1.3798 1.3462 1.5464 0.1074  -0.1311 -0.2287 468 HIS B C   
16050 O O   . HIS B 464 ? 1.3662 1.3454 1.5372 0.1227  -0.1575 -0.2367 468 HIS B O   
16051 C CB  . HIS B 464 ? 1.3352 1.2373 1.4854 0.0881  -0.1117 -0.2126 468 HIS B CB  
16052 C CG  . HIS B 464 ? 1.3778 1.2304 1.5043 0.0835  -0.0801 -0.1978 468 HIS B CG  
16053 N ND1 . HIS B 464 ? 1.3928 1.2249 1.5057 0.1062  -0.0721 -0.1774 468 HIS B ND1 
16054 C CD2 . HIS B 464 ? 1.4132 1.2299 1.5298 0.0590  -0.0532 -0.2002 468 HIS B CD2 
16055 C CE1 . HIS B 464 ? 1.4349 1.2166 1.5278 0.0999  -0.0373 -0.1665 468 HIS B CE1 
16056 N NE2 . HIS B 464 ? 1.4481 1.2150 1.5402 0.0694  -0.0257 -0.1826 468 HIS B NE2 
16064 N N   . MET B 465 ? 1.3942 1.3796 1.5816 0.0911  -0.1202 -0.2342 469 MET B N   
16065 C CA  . MET B 465 ? 1.3848 1.4092 1.5991 0.0969  -0.1337 -0.2465 469 MET B CA  
16066 C C   . MET B 465 ? 1.3260 1.3733 1.5804 0.0691  -0.1392 -0.2510 469 MET B C   
16067 O O   . MET B 465 ? 1.3237 1.3568 1.5799 0.0420  -0.1281 -0.2476 469 MET B O   
16068 C CB  . MET B 465 ? 1.4571 1.4968 1.6595 0.1151  -0.1108 -0.2423 469 MET B CB  
16069 C CG  . MET B 465 ? 1.5230 1.5453 1.6752 0.1448  -0.1098 -0.2388 469 MET B CG  
16070 S SD  . MET B 465 ? 1.6248 1.6604 1.7470 0.1701  -0.0767 -0.2315 469 MET B SD  
16071 C CE  . MET B 465 ? 1.6978 1.7175 1.7534 0.2047  -0.0983 -0.2384 469 MET B CE  
16081 N N   . GLY B 466 ? 1.2711 1.3528 1.5569 0.0763  -0.1578 -0.2588 470 GLY B N   
16082 C CA  . GLY B 466 ? 1.2300 1.3471 1.5581 0.0549  -0.1684 -0.2592 470 GLY B CA  
16083 C C   . GLY B 466 ? 1.1795 1.3000 1.5176 0.0561  -0.1981 -0.2631 470 GLY B C   
16084 O O   . GLY B 466 ? 1.1310 1.2204 1.4458 0.0670  -0.2076 -0.2648 470 GLY B O   
16088 N N   . PRO B 467 ? 1.2012 1.3638 1.5788 0.0461  -0.2128 -0.2606 471 PRO B N   
16089 C CA  . PRO B 467 ? 1.1904 1.3565 1.5750 0.0503  -0.2385 -0.2588 471 PRO B CA  
16090 C C   . PRO B 467 ? 1.2193 1.3467 1.5650 0.0341  -0.2443 -0.2596 471 PRO B C   
16091 O O   . PRO B 467 ? 1.2333 1.3400 1.5688 0.0476  -0.2538 -0.2562 471 PRO B O   
16092 C CB  . PRO B 467 ? 1.2004 1.4266 1.6332 0.0410  -0.2516 -0.2509 471 PRO B CB  
16093 C CG  . PRO B 467 ? 1.2213 1.4792 1.6842 0.0406  -0.2308 -0.2485 471 PRO B CG  
16094 C CD  . PRO B 467 ? 1.2290 1.4433 1.6516 0.0320  -0.2068 -0.2544 471 PRO B CD  
16102 N N   . ARG B 468 ? 1.2439 1.3573 1.5687 0.0057  -0.2358 -0.2637 472 ARG B N   
16103 C CA  . ARG B 468 ? 1.2945 1.3600 1.5725 -0.0078 -0.2337 -0.2670 472 ARG B CA  
16104 C C   . ARG B 468 ? 1.3455 1.3594 1.5903 -0.0048 -0.2059 -0.2671 472 ARG B C   
16105 O O   . ARG B 468 ? 1.3616 1.3290 1.5669 -0.0162 -0.1949 -0.2696 472 ARG B O   
16106 C CB  . ARG B 468 ? 1.3189 1.3938 1.5877 -0.0432 -0.2452 -0.2754 472 ARG B CB  
16107 C CG  . ARG B 468 ? 1.3304 1.4321 1.5981 -0.0430 -0.2747 -0.2717 472 ARG B CG  
16108 C CD  . ARG B 468 ? 1.3998 1.5241 1.6607 -0.0807 -0.2946 -0.2822 472 ARG B CD  
16109 N NE  . ARG B 468 ? 1.4000 1.5802 1.6808 -0.0762 -0.3276 -0.2719 472 ARG B NE  
16110 C CZ  . ARG B 468 ? 1.4219 1.6462 1.7112 -0.1054 -0.3559 -0.2764 472 ARG B CZ  
16111 N NH1 . ARG B 468 ? 1.4652 1.6802 1.7482 -0.1462 -0.3555 -0.2949 472 ARG B NH1 
16112 N NH2 . ARG B 468 ? 1.3729 1.6521 1.6800 -0.0947 -0.3859 -0.2609 472 ARG B NH2 
16126 N N   . CYS B 469 ? 1.3891 1.4088 1.6449 0.0131  -0.1927 -0.2630 473 CYS B N   
16127 C CA  . CYS B 469 ? 1.4632 1.4420 1.6892 0.0231  -0.1684 -0.2566 473 CYS B CA  
16128 C C   . CYS B 469 ? 1.5134 1.4624 1.7224 -0.0029 -0.1432 -0.2577 473 CYS B C   
16129 O O   . CYS B 469 ? 1.5431 1.4408 1.7183 -0.0042 -0.1239 -0.2535 473 CYS B O   
16130 C CB  . CYS B 469 ? 1.4841 1.4301 1.6882 0.0386  -0.1711 -0.2496 473 CYS B CB  
16131 S SG  . CYS B 469 ? 1.4654 1.4399 1.6992 0.0597  -0.2015 -0.2484 473 CYS B SG  
16136 N N   . GLU B 470 ? 1.5094 1.4904 1.7479 -0.0231 -0.1409 -0.2615 474 GLU B N   
16137 C CA  . GLU B 470 ? 1.5538 1.5112 1.7899 -0.0576 -0.1221 -0.2654 474 GLU B CA  
16138 C C   . GLU B 470 ? 1.5136 1.4641 1.7573 -0.0526 -0.0875 -0.2518 474 GLU B C   
16139 O O   . GLU B 470 ? 1.5562 1.4798 1.8028 -0.0814 -0.0658 -0.2520 474 GLU B O   
16140 C CB  . GLU B 470 ? 1.6221 1.6271 1.8968 -0.0899 -0.1459 -0.2759 474 GLU B CB  
16141 C CG  . GLU B 470 ? 1.6497 1.6767 1.9199 -0.0860 -0.1818 -0.2828 474 GLU B CG  
16142 C CD  . GLU B 470 ? 1.7058 1.7944 2.0191 -0.1119 -0.2099 -0.2872 474 GLU B CD  
16143 O OE1 . GLU B 470 ? 1.6862 1.8367 2.0509 -0.0963 -0.2181 -0.2767 474 GLU B OE1 
16144 O OE2 . GLU B 470 ? 1.7535 1.8287 2.0479 -0.1469 -0.2242 -0.3013 474 GLU B OE2 
16151 N N   . SER B 471 ? 1.4577 1.4281 1.7013 -0.0174 -0.0813 -0.2402 475 SER B N   
16152 C CA  . SER B 471 ? 1.4487 1.4111 1.6860 -0.0041 -0.0467 -0.2230 475 SER B CA  
16153 C C   . SER B 471 ? 1.4885 1.4146 1.6790 0.0287  -0.0378 -0.2110 475 SER B C   
16154 O O   . SER B 471 ? 1.4571 1.3848 1.6343 0.0470  -0.0629 -0.2163 475 SER B O   
16155 C CB  . SER B 471 ? 1.3610 1.3794 1.6285 0.0129  -0.0444 -0.2184 475 SER B CB  
16156 O OG  . SER B 471 ? 1.3368 1.3923 1.6585 -0.0175 -0.0395 -0.2182 475 SER B OG  
16162 N N   . GLY B 472 ? 1.5560 1.4530 1.7273 0.0361  -0.0022 -0.1913 476 GLY B N   
16163 C CA  . GLY B 472 ? 1.5870 1.4532 1.7171 0.0670  0.0078  -0.1734 476 GLY B CA  
16164 C C   . GLY B 472 ? 1.6330 1.5166 1.7422 0.0984  0.0260  -0.1539 476 GLY B C   
16165 O O   . GLY B 472 ? 1.6890 1.5791 1.8103 0.0918  0.0560  -0.1429 476 GLY B O   
16169 N N   . HIS B 473 ? 1.6579 1.5502 1.7355 0.1321  0.0073  -0.1486 477 HIS B N   
16170 C CA  . HIS B 473 ? 1.7077 1.6150 1.7485 0.1660  0.0185  -0.1322 477 HIS B CA  
16171 C C   . HIS B 473 ? 1.7070 1.6079 1.7114 0.1959  0.0021  -0.1173 477 HIS B C   
16172 O O   . HIS B 473 ? 1.6718 1.5950 1.6723 0.2066  -0.0383 -0.1333 477 HIS B O   
16173 C CB  . HIS B 473 ? 1.7282 1.6773 1.7704 0.1762  -0.0003 -0.1531 477 HIS B CB  
16174 C CG  . HIS B 473 ? 1.8555 1.8159 1.8461 0.2124  0.0122  -0.1409 477 HIS B CG  
16175 N ND1 . HIS B 473 ? 1.9366 1.8888 1.9101 0.2221  0.0586  -0.1126 477 HIS B ND1 
16176 C CD2 . HIS B 473 ? 1.8965 1.8723 1.8435 0.2413  -0.0154 -0.1538 477 HIS B CD2 
16177 C CE1 . HIS B 473 ? 1.9936 1.9578 1.9088 0.2590  0.0603  -0.1067 477 HIS B CE1 
16178 N NE2 . HIS B 473 ? 1.9682 1.9455 1.8635 0.2701  0.0135  -0.1343 477 HIS B NE2 
16186 N N   . ASP C 1   ? 1.2823 0.9403 1.1904 -0.2891 0.2107  -0.1985 1   ASP C N   
16187 C CA  . ASP C 1   ? 1.2265 0.9116 1.1508 -0.2451 0.1759  -0.1814 1   ASP C CA  
16188 C C   . ASP C 1   ? 1.2163 0.9868 1.1794 -0.2599 0.1366  -0.2057 1   ASP C C   
16189 O O   . ASP C 1   ? 1.2869 1.0882 1.2543 -0.3057 0.1390  -0.2379 1   ASP C O   
16190 C CB  . ASP C 1   ? 1.2862 0.8787 1.1507 -0.2272 0.1981  -0.1666 1   ASP C CB  
16191 C CG  . ASP C 1   ? 1.3844 0.8946 1.2031 -0.2006 0.2380  -0.1381 1   ASP C CG  
16192 O OD1 . ASP C 1   ? 1.3970 0.9188 1.2297 -0.1999 0.2492  -0.1310 1   ASP C OD1 
16193 O OD2 . ASP C 1   ? 1.4467 0.8829 1.2128 -0.1768 0.2589  -0.1218 1   ASP C OD2 
16200 N N   . ILE C 2   ? 1.1368 0.9476 1.1249 -0.2209 0.1024  -0.1906 2   ILE C N   
16201 C CA  . ILE C 2   ? 1.0940 0.9744 1.1080 -0.2231 0.0669  -0.2076 2   ILE C CA  
16202 C C   . ILE C 2   ? 1.1631 0.9960 1.1372 -0.2318 0.0722  -0.2151 2   ILE C C   
16203 O O   . ILE C 2   ? 1.1278 0.8975 1.0706 -0.2054 0.0820  -0.1930 2   ILE C O   
16204 C CB  . ILE C 2   ? 1.0177 0.9452 1.0643 -0.1783 0.0336  -0.1876 2   ILE C CB  
16205 C CG1 . ILE C 2   ? 0.9903 0.9537 1.0698 -0.1675 0.0319  -0.1787 2   ILE C CG1 
16206 C CG2 . ILE C 2   ? 0.9783 0.9735 1.0447 -0.1749 0.0001  -0.2030 2   ILE C CG2 
16207 C CD1 . ILE C 2   ? 0.9977 1.0361 1.1105 -0.1933 0.0238  -0.2033 2   ILE C CD1 
16219 N N   . GLN C 3   ? 1.2582 1.1282 1.2329 -0.2686 0.0660  -0.2471 3   GLN C N   
16220 C CA  . GLN C 3   ? 1.3442 1.1814 1.2838 -0.2786 0.0669  -0.2582 3   GLN C CA  
16221 C C   . GLN C 3   ? 1.2724 1.1749 1.2371 -0.2478 0.0257  -0.2544 3   GLN C C   
16222 O O   . GLN C 3   ? 1.2384 1.2319 1.2429 -0.2447 -0.0011 -0.2650 3   GLN C O   
16223 C CB  . GLN C 3   ? 1.4842 1.3275 1.4051 -0.3398 0.0849  -0.2982 3   GLN C CB  
16224 C CG  . GLN C 3   ? 1.5858 1.4074 1.4715 -0.3552 0.0836  -0.3158 3   GLN C CG  
16225 C CD  . GLN C 3   ? 1.7117 1.4045 1.5324 -0.3517 0.1202  -0.3023 3   GLN C CD  
16226 O OE1 . GLN C 3   ? 1.8208 1.4355 1.6021 -0.3794 0.1618  -0.3072 3   GLN C OE1 
16227 N NE2 . GLN C 3   ? 1.7383 1.4060 1.5429 -0.3155 0.1071  -0.2845 3   GLN C NE2 
16236 N N   . MET C 4   ? 1.2466 1.1013 1.1841 -0.2223 0.0228  -0.2381 4   MET C N   
16237 C CA  . MET C 4   ? 1.2038 1.1029 1.1531 -0.1942 -0.0107 -0.2334 4   MET C CA  
16238 C C   . MET C 4   ? 1.2523 1.1353 1.1685 -0.2149 -0.0088 -0.2535 4   MET C C   
16239 O O   . MET C 4   ? 1.3720 1.1733 1.2445 -0.2268 0.0188  -0.2524 4   MET C O   
16240 C CB  . MET C 4   ? 1.1503 1.0148 1.0960 -0.1488 -0.0167 -0.1983 4   MET C CB  
16241 C CG  . MET C 4   ? 1.0917 0.9653 1.0638 -0.1304 -0.0151 -0.1790 4   MET C CG  
16242 S SD  . MET C 4   ? 1.0335 1.0024 1.0553 -0.1275 -0.0419 -0.1903 4   MET C SD  
16243 C CE  . MET C 4   ? 1.0216 1.0232 1.0424 -0.0954 -0.0745 -0.1849 4   MET C CE  
16253 N N   . THR C 5   ? 1.1959 1.1564 1.1287 -0.2162 -0.0367 -0.2712 5   THR C N   
16254 C CA  . THR C 5   ? 1.2445 1.2084 1.1495 -0.2399 -0.0376 -0.2956 5   THR C CA  
16255 C C   . THR C 5   ? 1.2411 1.2525 1.1524 -0.2031 -0.0709 -0.2873 5   THR C C   
16256 O O   . THR C 5   ? 1.1984 1.2914 1.1421 -0.1824 -0.0969 -0.2871 5   THR C O   
16257 C CB  . THR C 5   ? 1.2568 1.2850 1.1709 -0.2930 -0.0331 -0.3369 5   THR C CB  
16258 O OG1 . THR C 5   ? 1.2157 1.3441 1.1787 -0.2833 -0.0553 -0.3403 5   THR C OG1 
16259 C CG2 . THR C 5   ? 1.3069 1.2581 1.1921 -0.3387 0.0093  -0.3492 5   THR C CG2 
16267 N N   . GLN C 6   ? 1.3098 1.2669 1.1857 -0.1925 -0.0677 -0.2795 6   GLN C N   
16268 C CA  . GLN C 6   ? 1.3274 1.3199 1.1986 -0.1630 -0.0945 -0.2747 6   GLN C CA  
16269 C C   . GLN C 6   ? 1.3897 1.4124 1.2396 -0.1978 -0.0951 -0.3097 6   GLN C C   
16270 O O   . GLN C 6   ? 1.4721 1.4267 1.2821 -0.2166 -0.0752 -0.3164 6   GLN C O   
16271 C CB  . GLN C 6   ? 1.2835 1.2029 1.1307 -0.1287 -0.0905 -0.2426 6   GLN C CB  
16272 C CG  . GLN C 6   ? 1.1904 1.0899 1.0580 -0.1004 -0.0893 -0.2121 6   GLN C CG  
16273 C CD  . GLN C 6   ? 1.1206 0.9568 0.9647 -0.0740 -0.0814 -0.1835 6   GLN C CD  
16274 O OE1 . GLN C 6   ? 1.0670 0.8576 0.9071 -0.0705 -0.0617 -0.1672 6   GLN C OE1 
16275 N NE2 . GLN C 6   ? 1.1202 0.9598 0.9481 -0.0538 -0.0962 -0.1770 6   GLN C NE2 
16284 N N   . THR C 7   ? 1.3610 1.4906 1.2356 -0.2056 -0.1169 -0.3328 7   THR C N   
16285 C CA  . THR C 7   ? 1.4313 1.6138 1.2912 -0.2462 -0.1183 -0.3725 7   THR C CA  
16286 C C   . THR C 7   ? 1.4262 1.5544 1.2423 -0.2417 -0.1156 -0.3720 7   THR C C   
16287 O O   . THR C 7   ? 1.4604 1.5399 1.2414 -0.2847 -0.0922 -0.3956 7   THR C O   
16288 C CB  . THR C 7   ? 1.5055 1.8275 1.3975 -0.2324 -0.1503 -0.3877 7   THR C CB  
16289 O OG1 . THR C 7   ? 1.5201 1.8534 1.4200 -0.1674 -0.1741 -0.3536 7   THR C OG1 
16290 C CG2 . THR C 7   ? 1.5343 1.9243 1.4644 -0.2579 -0.1471 -0.4040 7   THR C CG2 
16298 N N   . THR C 8   ? 1.4005 1.5311 1.2134 -0.1903 -0.1369 -0.3454 8   THR C N   
16299 C CA  . THR C 8   ? 1.4443 1.5299 1.2174 -0.1803 -0.1367 -0.3418 8   THR C CA  
16300 C C   . THR C 8   ? 1.5114 1.4768 1.2591 -0.1690 -0.1121 -0.3136 8   THR C C   
16301 O O   . THR C 8   ? 1.5471 1.4862 1.3086 -0.1322 -0.1157 -0.2799 8   THR C O   
16302 C CB  . THR C 8   ? 1.3810 1.5217 1.1574 -0.1297 -0.1677 -0.3249 8   THR C CB  
16303 O OG1 . THR C 8   ? 1.3549 1.4694 1.1482 -0.0862 -0.1733 -0.2875 8   THR C OG1 
16304 C CG2 . THR C 8   ? 1.3621 1.6333 1.1599 -0.1326 -0.1917 -0.3512 8   THR C CG2 
16312 N N   . SER C 9   ? 1.5435 1.4384 1.2508 -0.2002 -0.0857 -0.3282 9   SER C N   
16313 C CA  . SER C 9   ? 1.5240 1.3118 1.2005 -0.1836 -0.0610 -0.3014 9   SER C CA  
16314 C C   . SER C 9   ? 1.4469 1.2145 1.1016 -0.1460 -0.0725 -0.2802 9   SER C C   
16315 O O   . SER C 9   ? 1.4419 1.1419 1.0797 -0.1217 -0.0580 -0.2519 9   SER C O   
16316 C CB  . SER C 9   ? 1.6689 1.3770 1.3002 -0.2263 -0.0231 -0.3232 9   SER C CB  
16317 O OG  . SER C 9   ? 1.7221 1.4334 1.3686 -0.2613 -0.0064 -0.3387 9   SER C OG  
16323 N N   . SER C 10  ? 1.3945 1.2242 1.0480 -0.1392 -0.0974 -0.2926 10  SER C N   
16324 C CA  . SER C 10  ? 1.3634 1.1751 0.9946 -0.1037 -0.1078 -0.2722 10  SER C CA  
16325 C C   . SER C 10  ? 1.3325 1.2337 0.9743 -0.0867 -0.1400 -0.2807 10  SER C C   
16326 O O   . SER C 10  ? 1.3257 1.2984 0.9753 -0.1127 -0.1500 -0.3133 10  SER C O   
16327 C CB  . SER C 10  ? 1.4392 1.1793 1.0188 -0.1189 -0.0853 -0.2818 10  SER C CB  
16328 O OG  . SER C 10  ? 1.4359 1.1663 0.9952 -0.0851 -0.0961 -0.2629 10  SER C OG  
16334 N N   . LEU C 11  ? 1.2773 1.1758 0.9157 -0.0427 -0.1542 -0.2513 11  LEU C N   
16335 C CA  . LEU C 11  ? 1.2690 1.2364 0.9050 -0.0151 -0.1810 -0.2519 11  LEU C CA  
16336 C C   . LEU C 11  ? 1.2716 1.1912 0.8751 0.0168  -0.1813 -0.2265 11  LEU C C   
16337 O O   . LEU C 11  ? 1.2811 1.1285 0.8749 0.0228  -0.1643 -0.2039 11  LEU C O   
16338 C CB  . LEU C 11  ? 1.2460 1.2698 0.9150 0.0123  -0.1986 -0.2391 11  LEU C CB  
16339 C CG  . LEU C 11  ? 1.2227 1.1914 0.8980 0.0424  -0.1932 -0.2013 11  LEU C CG  
16340 C CD1 . LEU C 11  ? 1.2376 1.1935 0.8852 0.0846  -0.2032 -0.1767 11  LEU C CD1 
16341 C CD2 . LEU C 11  ? 1.1752 1.1793 0.8871 0.0474  -0.1983 -0.1980 11  LEU C CD2 
16353 N N   . SER C 12  ? 1.2683 1.2355 0.8541 0.0390  -0.2003 -0.2297 12  SER C N   
16354 C CA  . SER C 12  ? 1.2378 1.1664 0.7893 0.0689  -0.2011 -0.2075 12  SER C CA  
16355 C C   . SER C 12  ? 1.2241 1.1852 0.7728 0.1150  -0.2188 -0.1851 12  SER C C   
16356 O O   . SER C 12  ? 1.2362 1.2741 0.7970 0.1275  -0.2365 -0.1964 12  SER C O   
16357 C CB  . SER C 12  ? 1.2431 1.1833 0.7615 0.0546  -0.2025 -0.2314 12  SER C CB  
16358 O OG  . SER C 12  ? 1.2825 1.3117 0.8107 0.0358  -0.2175 -0.2662 12  SER C OG  
16364 N N   . ALA C 13  ? 1.2402 1.1421 0.7683 0.1407  -0.2116 -0.1534 13  ALA C N   
16365 C CA  . ALA C 13  ? 1.2718 1.1776 0.7860 0.1834  -0.2202 -0.1285 13  ALA C CA  
16366 C C   . ALA C 13  ? 1.3505 1.2013 0.8238 0.2034  -0.2124 -0.1054 13  ALA C C   
16367 O O   . ALA C 13  ? 1.3685 1.1716 0.8341 0.1849  -0.1979 -0.1020 13  ALA C O   
16368 C CB  . ALA C 13  ? 1.2188 1.1007 0.7577 0.1874  -0.2133 -0.1113 13  ALA C CB  
16374 N N   . SER C 14  ? 1.3871 1.2445 0.8303 0.2436  -0.2202 -0.0887 14  SER C N   
16375 C CA  . SER C 14  ? 1.4137 1.2161 0.8136 0.2645  -0.2107 -0.0641 14  SER C CA  
16376 C C   . SER C 14  ? 1.4093 1.1517 0.8004 0.2762  -0.1958 -0.0356 14  SER C C   
16377 O O   . SER C 14  ? 1.4010 1.1503 0.8132 0.2790  -0.1965 -0.0338 14  SER C O   
16378 C CB  . SER C 14  ? 1.4449 1.2850 0.8054 0.3028  -0.2247 -0.0632 14  SER C CB  
16379 O OG  . SER C 14  ? 1.4297 1.3199 0.7912 0.2866  -0.2357 -0.0908 14  SER C OG  
16385 N N   . LEU C 15  ? 1.4469 1.1305 0.8042 0.2803  -0.1806 -0.0148 15  LEU C N   
16386 C CA  . LEU C 15  ? 1.4388 1.0615 0.7805 0.2831  -0.1625 0.0092  15  LEU C CA  
16387 C C   . LEU C 15  ? 1.4679 1.0853 0.7813 0.3223  -0.1654 0.0209  15  LEU C C   
16388 O O   . LEU C 15  ? 1.4923 1.1360 0.7748 0.3587  -0.1767 0.0220  15  LEU C O   
16389 C CB  . LEU C 15  ? 1.4798 1.0494 0.7836 0.2799  -0.1451 0.0272  15  LEU C CB  
16390 C CG  . LEU C 15  ? 1.5252 1.0978 0.8493 0.2488  -0.1388 0.0198  15  LEU C CG  
16391 C CD1 . LEU C 15  ? 1.6050 1.1363 0.8891 0.2498  -0.1226 0.0378  15  LEU C CD1 
16392 C CD2 . LEU C 15  ? 1.4878 1.0605 0.8558 0.2180  -0.1301 0.0162  15  LEU C CD2 
16404 N N   . GLY C 16  ? 1.4515 1.0354 0.7720 0.3174  -0.1540 0.0299  16  GLY C N   
16405 C CA  . GLY C 16  ? 1.4854 1.0529 0.7748 0.3560  -0.1522 0.0420  16  GLY C CA  
16406 C C   . GLY C 16  ? 1.4274 1.0696 0.7505 0.3727  -0.1728 0.0259  16  GLY C C   
16407 O O   . GLY C 16  ? 1.4522 1.0824 0.7566 0.4035  -0.1694 0.0357  16  GLY C O   
16411 N N   . ASP C 17  ? 1.3797 1.0972 0.7481 0.3524  -0.1916 0.0007  17  ASP C N   
16412 C CA  . ASP C 17  ? 1.3726 1.1728 0.7747 0.3619  -0.2105 -0.0181 17  ASP C CA  
16413 C C   . ASP C 17  ? 1.3749 1.1635 0.8118 0.3457  -0.2040 -0.0185 17  ASP C C   
16414 O O   . ASP C 17  ? 1.3663 1.0933 0.8101 0.3188  -0.1868 -0.0094 17  ASP C O   
16415 C CB  . ASP C 17  ? 1.3490 1.2210 0.7884 0.3307  -0.2262 -0.0484 17  ASP C CB  
16416 C CG  . ASP C 17  ? 1.4486 1.3498 0.8550 0.3486  -0.2361 -0.0530 17  ASP C CG  
16417 O OD1 . ASP C 17  ? 1.5175 1.3980 0.8740 0.3934  -0.2343 -0.0323 17  ASP C OD1 
16418 O OD2 . ASP C 17  ? 1.4386 1.3787 0.8641 0.3181  -0.2437 -0.0775 17  ASP C OD2 
16423 N N   . ARG C 18  ? 1.4166 1.2743 0.8756 0.3629  -0.2181 -0.0302 18  ARG C N   
16424 C CA  . ARG C 18  ? 1.4425 1.3064 0.9400 0.3477  -0.2152 -0.0348 18  ARG C CA  
16425 C C   . ARG C 18  ? 1.2955 1.2295 0.8512 0.3058  -0.2269 -0.0646 18  ARG C C   
16426 O O   . ARG C 18  ? 1.2718 1.2894 0.8385 0.3095  -0.2441 -0.0850 18  ARG C O   
16427 C CB  . ARG C 18  ? 1.6307 1.5211 1.1095 0.3977  -0.2196 -0.0261 18  ARG C CB  
16428 C CG  . ARG C 18  ? 1.7025 1.6580 1.2337 0.3848  -0.2285 -0.0434 18  ARG C CG  
16429 C CD  . ARG C 18  ? 1.8075 1.7622 1.3139 0.4350  -0.2255 -0.0286 18  ARG C CD  
16430 N NE  . ARG C 18  ? 1.8995 1.7402 1.3705 0.4382  -0.2008 -0.0052 18  ARG C NE  
16431 C CZ  . ARG C 18  ? 2.0144 1.8207 1.4553 0.4752  -0.1898 0.0096  18  ARG C CZ  
16432 N NH1 . ARG C 18  ? 2.1374 2.0211 1.5817 0.5183  -0.2027 0.0060  18  ARG C NH1 
16433 N NH2 . ARG C 18  ? 2.0884 1.7855 1.4933 0.4682  -0.1644 0.0268  18  ARG C NH2 
16447 N N   . VAL C 19  ? 1.2141 1.1151 0.8031 0.2657  -0.2156 -0.0677 19  VAL C N   
16448 C CA  . VAL C 19  ? 1.1575 1.1012 0.7926 0.2234  -0.2191 -0.0931 19  VAL C CA  
16449 C C   . VAL C 19  ? 1.1191 1.0839 0.7913 0.2155  -0.2180 -0.0974 19  VAL C C   
16450 O O   . VAL C 19  ? 1.1334 1.0470 0.8024 0.2214  -0.2064 -0.0797 19  VAL C O   
16451 C CB  . VAL C 19  ? 1.1676 1.0555 0.8052 0.1880  -0.2043 -0.0917 19  VAL C CB  
16452 C CG1 . VAL C 19  ? 1.1900 1.1056 0.8641 0.1474  -0.2022 -0.1160 19  VAL C CG1 
16453 C CG2 . VAL C 19  ? 1.1632 1.0319 0.7627 0.1976  -0.2051 -0.0873 19  VAL C CG2 
16463 N N   . ILE C 20  ? 1.0951 1.1370 0.8006 0.1991  -0.2288 -0.1227 20  ILE C N   
16464 C CA  . ILE C 20  ? 1.0753 1.1487 0.8187 0.1893  -0.2284 -0.1299 20  ILE C CA  
16465 C C   . ILE C 20  ? 1.0625 1.1553 0.8401 0.1380  -0.2231 -0.1546 20  ILE C C   
16466 O O   . ILE C 20  ? 1.0310 1.1764 0.8113 0.1190  -0.2304 -0.1791 20  ILE C O   
16467 C CB  . ILE C 20  ? 1.0912 1.2505 0.8378 0.2247  -0.2450 -0.1362 20  ILE C CB  
16468 C CG1 . ILE C 20  ? 1.1227 1.2448 0.8227 0.2815  -0.2445 -0.1083 20  ILE C CG1 
16469 C CG2 . ILE C 20  ? 1.0849 1.2827 0.8733 0.2111  -0.2441 -0.1457 20  ILE C CG2 
16470 C CD1 . ILE C 20  ? 1.1397 1.3448 0.8317 0.3298  -0.2590 -0.1097 20  ILE C CD1 
16482 N N   . ILE C 21  ? 1.0524 1.1012 0.8512 0.1153  -0.2081 -0.1489 21  ILE C N   
16483 C CA  . ILE C 21  ? 1.0388 1.0870 0.8615 0.0703  -0.1966 -0.1677 21  ILE C CA  
16484 C C   . ILE C 21  ? 1.0402 1.1342 0.9000 0.0610  -0.1975 -0.1773 21  ILE C C   
16485 O O   . ILE C 21  ? 1.0090 1.0913 0.8770 0.0825  -0.1972 -0.1604 21  ILE C O   
16486 C CB  . ILE C 21  ? 0.9783 0.9436 0.7919 0.0559  -0.1765 -0.1520 21  ILE C CB  
16487 C CG1 . ILE C 21  ? 0.9785 0.9072 0.7559 0.0634  -0.1753 -0.1449 21  ILE C CG1 
16488 C CG2 . ILE C 21  ? 0.9348 0.8892 0.7653 0.0168  -0.1600 -0.1675 21  ILE C CG2 
16489 C CD1 . ILE C 21  ? 0.9745 0.8361 0.7366 0.0711  -0.1615 -0.1192 21  ILE C CD1 
16501 N N   . SER C 22  ? 1.1050 1.2489 0.9839 0.0262  -0.1965 -0.2058 22  SER C N   
16502 C CA  . SER C 22  ? 1.0944 1.2964 1.0088 0.0134  -0.1977 -0.2193 22  SER C CA  
16503 C C   . SER C 22  ? 1.0742 1.2290 1.0031 -0.0260 -0.1747 -0.2237 22  SER C C   
16504 O O   . SER C 22  ? 1.1328 1.2382 1.0437 -0.0543 -0.1588 -0.2310 22  SER C O   
16505 C CB  . SER C 22  ? 1.1896 1.4967 1.1148 -0.0009 -0.2117 -0.2512 22  SER C CB  
16506 O OG  . SER C 22  ? 1.2220 1.5822 1.1816 -0.0289 -0.2071 -0.2698 22  SER C OG  
16512 N N   . CYS C 23  ? 1.0055 1.1729 0.9621 -0.0241 -0.1714 -0.2184 23  CYS C N   
16513 C CA  . CYS C 23  ? 1.0354 1.1631 1.0053 -0.0551 -0.1491 -0.2198 23  CYS C CA  
16514 C C   . CYS C 23  ? 1.0195 1.2161 1.0248 -0.0653 -0.1522 -0.2336 23  CYS C C   
16515 O O   . CYS C 23  ? 0.9864 1.2289 1.0063 -0.0329 -0.1680 -0.2254 23  CYS C O   
16516 C CB  . CYS C 23  ? 1.0570 1.1098 1.0200 -0.0360 -0.1381 -0.1894 23  CYS C CB  
16517 S SG  . CYS C 23  ? 1.1002 1.1114 1.0776 -0.0603 -0.1116 -0.1849 23  CYS C SG  
16522 N N   . ARG C 24  ? 1.0613 1.2613 1.0756 -0.1099 -0.1347 -0.2545 24  ARG C N   
16523 C CA  . ARG C 24  ? 1.0569 1.3259 1.1047 -0.1274 -0.1346 -0.2707 24  ARG C CA  
16524 C C   . ARG C 24  ? 1.0405 1.2503 1.0918 -0.1560 -0.1062 -0.2677 24  ARG C C   
16525 O O   . ARG C 24  ? 1.0794 1.2187 1.1035 -0.1830 -0.0829 -0.2712 24  ARG C O   
16526 C CB  . ARG C 24  ? 1.1300 1.4894 1.1845 -0.1614 -0.1412 -0.3081 24  ARG C CB  
16527 C CG  . ARG C 24  ? 1.2005 1.6467 1.2913 -0.1821 -0.1411 -0.3273 24  ARG C CG  
16528 C CD  . ARG C 24  ? 1.3126 1.8559 1.4088 -0.2254 -0.1447 -0.3686 24  ARG C CD  
16529 N NE  . ARG C 24  ? 1.3624 2.0278 1.4750 -0.1898 -0.1757 -0.3746 24  ARG C NE  
16530 C CZ  . ARG C 24  ? 1.3591 2.1202 1.5047 -0.1694 -0.1883 -0.3762 24  ARG C CZ  
16531 N NH1 . ARG C 24  ? 1.3576 2.2283 1.5100 -0.1295 -0.2147 -0.3794 24  ARG C NH1 
16532 N NH2 . ARG C 24  ? 1.3246 2.0729 1.4933 -0.1848 -0.1735 -0.3732 24  ARG C NH2 
16546 N N   . ALA C 25  ? 0.9702 1.2064 1.0505 -0.1465 -0.1065 -0.2603 25  ALA C N   
16547 C CA  . ALA C 25  ? 0.9886 1.1783 1.0736 -0.1684 -0.0805 -0.2558 25  ALA C CA  
16548 C C   . ALA C 25  ? 1.0191 1.2742 1.1264 -0.2093 -0.0723 -0.2846 25  ALA C C   
16549 O O   . ALA C 25  ? 1.0071 1.3624 1.1388 -0.2076 -0.0923 -0.3019 25  ALA C O   
16550 C CB  . ALA C 25  ? 0.9680 1.1379 1.0678 -0.1317 -0.0839 -0.2271 25  ALA C CB  
16556 N N   . SER C 26  ? 1.0599 1.2594 1.1556 -0.2448 -0.0407 -0.2891 26  SER C N   
16557 C CA  . SER C 26  ? 1.0787 1.3275 1.1903 -0.2915 -0.0260 -0.3168 26  SER C CA  
16558 C C   . SER C 26  ? 1.0586 1.3668 1.2109 -0.2741 -0.0344 -0.3091 26  SER C C   
16559 O O   . SER C 26  ? 1.1184 1.4831 1.2894 -0.3105 -0.0246 -0.3318 26  SER C O   
16560 C CB  . SER C 26  ? 1.1215 1.2729 1.1959 -0.3333 0.0165  -0.3218 26  SER C CB  
16561 O OG  . SER C 26  ? 1.1505 1.2249 1.2162 -0.3050 0.0320  -0.2891 26  SER C OG  
16567 N N   . GLN C 27  ? 1.0212 1.3173 1.1849 -0.2225 -0.0501 -0.2793 27  GLN C N   
16568 C CA  . GLN C 27  ? 1.0127 1.3586 1.2102 -0.2018 -0.0579 -0.2710 27  GLN C CA  
16569 C C   . GLN C 27  ? 0.9670 1.3180 1.1685 -0.1446 -0.0835 -0.2473 27  GLN C C   
16570 O O   . GLN C 27  ? 0.9671 1.2706 1.1447 -0.1242 -0.0907 -0.2342 27  GLN C O   
16571 C CB  . GLN C 27  ? 1.0610 1.3445 1.2562 -0.2121 -0.0303 -0.2572 27  GLN C CB  
16572 C CG  . GLN C 27  ? 1.1658 1.4074 1.3403 -0.2661 0.0044  -0.2748 27  GLN C CG  
16573 C CD  . GLN C 27  ? 1.2303 1.4086 1.3972 -0.2665 0.0324  -0.2566 27  GLN C CD  
16574 O OE1 . GLN C 27  ? 1.2003 1.3875 1.3868 -0.2315 0.0231  -0.2356 27  GLN C OE1 
16575 N NE2 . GLN C 27  ? 1.3175 1.4276 1.4506 -0.3051 0.0690  -0.2644 27  GLN C NE2 
16584 N N   . ASP C 28  ? 0.9262 1.3310 1.1540 -0.1200 -0.0945 -0.2425 28  ASP C N   
16585 C CA  . ASP C 28  ? 0.9067 1.2985 1.1299 -0.0682 -0.1115 -0.2196 28  ASP C CA  
16586 C C   . ASP C 28  ? 0.8364 1.1328 1.0413 -0.0600 -0.0982 -0.1951 28  ASP C C   
16587 O O   . ASP C 28  ? 0.8229 1.0937 1.0356 -0.0738 -0.0801 -0.1896 28  ASP C O   
16588 C CB  . ASP C 28  ? 0.9114 1.3706 1.1608 -0.0451 -0.1202 -0.2199 28  ASP C CB  
16589 C CG  . ASP C 28  ? 0.8950 1.3350 1.1299 0.0080  -0.1345 -0.1992 28  ASP C CG  
16590 O OD1 . ASP C 28  ? 0.9095 1.2914 1.1156 0.0239  -0.1388 -0.1864 28  ASP C OD1 
16591 O OD2 . ASP C 28  ? 0.8817 1.3604 1.1297 0.0329  -0.1391 -0.1963 28  ASP C OD2 
16596 N N   . ILE C 29  ? 0.7654 1.0152 0.9449 -0.0374 -0.1061 -0.1807 29  ILE C N   
16597 C CA  . ILE C 29  ? 0.7600 0.9344 0.9217 -0.0299 -0.0949 -0.1592 29  ILE C CA  
16598 C C   . ILE C 29  ? 0.7645 0.9256 0.9188 0.0054  -0.1052 -0.1429 29  ILE C C   
16599 O O   . ILE C 29  ? 0.7732 0.8822 0.9103 0.0115  -0.0988 -0.1271 29  ILE C O   
16600 C CB  . ILE C 29  ? 0.7505 0.8738 0.8841 -0.0397 -0.0894 -0.1559 29  ILE C CB  
16601 C CG1 . ILE C 29  ? 0.6977 0.8373 0.8165 -0.0227 -0.1091 -0.1598 29  ILE C CG1 
16602 C CG2 . ILE C 29  ? 0.8141 0.9273 0.9449 -0.0775 -0.0704 -0.1707 29  ILE C CG2 
16603 C CD1 . ILE C 29  ? 0.6820 0.7718 0.7719 -0.0300 -0.1043 -0.1560 29  ILE C CD1 
16615 N N   . SER C 30  ? 0.7163 0.9241 0.8792 0.0286  -0.1188 -0.1473 30  SER C N   
16616 C CA  . SER C 30  ? 0.6559 0.8434 0.8070 0.0597  -0.1222 -0.1340 30  SER C CA  
16617 C C   . SER C 30  ? 0.6620 0.7842 0.7774 0.0715  -0.1221 -0.1195 30  SER C C   
16618 O O   . SER C 30  ? 0.6973 0.7783 0.8002 0.0757  -0.1142 -0.1083 30  SER C O   
16619 C CB  . SER C 30  ? 0.6612 0.8436 0.8302 0.0515  -0.1096 -0.1295 30  SER C CB  
16620 O OG  . SER C 30  ? 0.7239 0.9646 0.9245 0.0368  -0.1072 -0.1430 30  SER C OG  
16626 N N   . ASN C 31  ? 0.6718 0.7885 0.7697 0.0740  -0.1299 -0.1215 31  ASN C N   
16627 C CA  . ASN C 31  ? 0.6970 0.7590 0.7579 0.0877  -0.1309 -0.1091 31  ASN C CA  
16628 C C   . ASN C 31  ? 0.6945 0.7072 0.7475 0.0671  -0.1177 -0.0991 31  ASN C C   
16629 O O   . ASN C 31  ? 0.7124 0.6808 0.7359 0.0739  -0.1152 -0.0887 31  ASN C O   
16630 C CB  . ASN C 31  ? 0.7460 0.7835 0.7799 0.1201  -0.1324 -0.1002 31  ASN C CB  
16631 C CG  . ASN C 31  ? 0.8160 0.8910 0.8379 0.1545  -0.1457 -0.1041 31  ASN C CG  
16632 O OD1 . ASN C 31  ? 0.8491 0.9760 0.8887 0.1697  -0.1505 -0.1106 31  ASN C OD1 
16633 N ND2 . ASN C 31  ? 0.8576 0.9123 0.8480 0.1698  -0.1516 -0.0995 31  ASN C ND2 
16640 N N   . TYR C 32  ? 0.7339 0.7543 0.8086 0.0434  -0.1071 -0.1016 32  TYR C N   
16641 C CA  . TYR C 32  ? 0.7772 0.7619 0.8421 0.0304  -0.0939 -0.0907 32  TYR C CA  
16642 C C   . TYR C 32  ? 0.7915 0.7638 0.8456 0.0194  -0.0919 -0.0936 32  TYR C C   
16643 O O   . TYR C 32  ? 0.7991 0.7663 0.8586 0.0034  -0.0789 -0.0953 32  TYR C O   
16644 C CB  . TYR C 32  ? 0.7725 0.7665 0.8578 0.0192  -0.0799 -0.0879 32  TYR C CB  
16645 C CG  . TYR C 32  ? 0.8017 0.8004 0.8918 0.0277  -0.0790 -0.0836 32  TYR C CG  
16646 C CD1 . TYR C 32  ? 0.8203 0.7940 0.8901 0.0300  -0.0752 -0.0745 32  TYR C CD1 
16647 C CD2 . TYR C 32  ? 0.8171 0.8472 0.9303 0.0302  -0.0801 -0.0906 32  TYR C CD2 
16648 C CE1 . TYR C 32  ? 0.8525 0.8273 0.9219 0.0328  -0.0720 -0.0740 32  TYR C CE1 
16649 C CE2 . TYR C 32  ? 0.8274 0.8582 0.9415 0.0380  -0.0780 -0.0878 32  TYR C CE2 
16650 C CZ  . TYR C 32  ? 0.8476 0.8481 0.9383 0.0384  -0.0736 -0.0802 32  TYR C CZ  
16651 O OH  . TYR C 32  ? 0.8836 0.8814 0.9703 0.0414  -0.0692 -0.0806 32  TYR C OH  
16661 N N   . LEU C 33  ? 0.6507 0.7136 0.7283 0.0686  -0.0697 -0.1217 33  LEU C N   
16662 C CA  . LEU C 33  ? 0.7025 0.7643 0.7723 0.0542  -0.0793 -0.1247 33  LEU C CA  
16663 C C   . LEU C 33  ? 0.6456 0.6733 0.6712 0.0642  -0.0945 -0.1076 33  LEU C C   
16664 O O   . LEU C 33  ? 0.5688 0.5901 0.5833 0.0822  -0.1107 -0.0988 33  LEU C O   
16665 C CB  . LEU C 33  ? 0.7482 0.8630 0.8562 0.0538  -0.0984 -0.1440 33  LEU C CB  
16666 C CG  . LEU C 33  ? 0.7846 0.8987 0.8837 0.0359  -0.1064 -0.1542 33  LEU C CG  
16667 C CD1 . LEU C 33  ? 0.8685 1.0065 1.0088 0.0064  -0.0897 -0.1755 33  LEU C CD1 
16668 C CD2 . LEU C 33  ? 0.8310 0.9708 0.9232 0.0520  -0.1408 -0.1595 33  LEU C CD2 
16680 N N   . SER C 34  ? 0.6906 0.6946 0.6910 0.0526  -0.0873 -0.1027 34  SER C N   
16681 C CA  . SER C 34  ? 0.7347 0.7154 0.6987 0.0582  -0.0953 -0.0868 34  SER C CA  
16682 C C   . SER C 34  ? 0.7908 0.7770 0.7396 0.0528  -0.1022 -0.0930 34  SER C C   
16683 O O   . SER C 34  ? 0.8140 0.8060 0.7736 0.0408  -0.0958 -0.1094 34  SER C O   
16684 C CB  . SER C 34  ? 0.7451 0.6981 0.6910 0.0560  -0.0793 -0.0755 34  SER C CB  
16685 O OG  . SER C 34  ? 0.7972 0.7443 0.7522 0.0603  -0.0709 -0.0751 34  SER C OG  
16691 N N   . TRP C 35  ? 0.8224 0.8028 0.7422 0.0605  -0.1138 -0.0802 35  TRP C N   
16692 C CA  . TRP C 35  ? 0.8782 0.8625 0.7720 0.0595  -0.1191 -0.0849 35  TRP C CA  
16693 C C   . TRP C 35  ? 0.8489 0.8166 0.7150 0.0585  -0.1047 -0.0709 35  TRP C C   
16694 O O   . TRP C 35  ? 0.8618 0.8205 0.7218 0.0597  -0.1016 -0.0521 35  TRP C O   
16695 C CB  . TRP C 35  ? 0.8826 0.8791 0.7584 0.0720  -0.1429 -0.0810 35  TRP C CB  
16696 C CG  . TRP C 35  ? 0.8813 0.9096 0.7886 0.0769  -0.1613 -0.1001 35  TRP C CG  
16697 C CD1 . TRP C 35  ? 0.8397 0.8812 0.7767 0.0876  -0.1695 -0.0997 35  TRP C CD1 
16698 C CD2 . TRP C 35  ? 0.8672 0.9247 0.7840 0.0716  -0.1746 -0.1260 35  TRP C CD2 
16699 N NE1 . TRP C 35  ? 0.8223 0.9086 0.7929 0.0903  -0.1863 -0.1228 35  TRP C NE1 
16700 C CE2 . TRP C 35  ? 0.8202 0.9174 0.7803 0.0780  -0.1912 -0.1399 35  TRP C CE2 
16701 C CE3 . TRP C 35  ? 0.8873 0.9427 0.7807 0.0628  -0.1750 -0.1418 35  TRP C CE3 
16702 C CZ2 . TRP C 35  ? 0.8203 0.9618 0.8073 0.0719  -0.2098 -0.1693 35  TRP C CZ2 
16703 C CZ3 . TRP C 35  ? 0.8908 0.9793 0.8033 0.0563  -0.1941 -0.1719 35  TRP C CZ3 
16704 C CH2 . TRP C 35  ? 0.8662 1.0007 0.8282 0.0590  -0.2121 -0.1855 35  TRP C CH2 
16715 N N   . TYR C 36  ? 0.8387 0.8042 0.6905 0.0561  -0.0962 -0.0828 36  TYR C N   
16716 C CA  . TYR C 36  ? 0.8182 0.7787 0.6479 0.0598  -0.0813 -0.0741 36  TYR C CA  
16717 C C   . TYR C 36  ? 0.8738 0.8408 0.6678 0.0653  -0.0840 -0.0815 36  TYR C C   
16718 O O   . TYR C 36  ? 0.9235 0.8923 0.7111 0.0642  -0.0962 -0.1017 36  TYR C O   
16719 C CB  . TYR C 36  ? 0.7783 0.7226 0.6169 0.0603  -0.0645 -0.0821 36  TYR C CB  
16720 C CG  . TYR C 36  ? 0.7561 0.6911 0.6190 0.0575  -0.0602 -0.0755 36  TYR C CG  
16721 C CD1 . TYR C 36  ? 0.7858 0.7131 0.6688 0.0493  -0.0604 -0.0863 36  TYR C CD1 
16722 C CD2 . TYR C 36  ? 0.7513 0.6895 0.6171 0.0622  -0.0553 -0.0603 36  TYR C CD2 
16723 C CE1 . TYR C 36  ? 0.7824 0.7007 0.6794 0.0489  -0.0531 -0.0800 36  TYR C CE1 
16724 C CE2 . TYR C 36  ? 0.7576 0.6858 0.6365 0.0624  -0.0531 -0.0566 36  TYR C CE2 
16725 C CZ  . TYR C 36  ? 0.7360 0.6519 0.6264 0.0572  -0.0507 -0.0654 36  TYR C CZ  
16726 O OH  . TYR C 36  ? 0.7354 0.6409 0.6310 0.0593  -0.0453 -0.0613 36  TYR C OH  
16736 N N   . GLN C 37  ? 0.8676 0.8424 0.6393 0.0702  -0.0721 -0.0670 37  GLN C N   
16737 C CA  . GLN C 37  ? 0.8836 0.8661 0.6136 0.0783  -0.0684 -0.0720 37  GLN C CA  
16738 C C   . GLN C 37  ? 0.8927 0.8776 0.6178 0.0873  -0.0468 -0.0803 37  GLN C C   
16739 O O   . GLN C 37  ? 0.8382 0.8360 0.5830 0.0882  -0.0327 -0.0666 37  GLN C O   
16740 C CB  . GLN C 37  ? 0.8881 0.8802 0.5910 0.0778  -0.0673 -0.0457 37  GLN C CB  
16741 C CG  . GLN C 37  ? 0.9322 0.9360 0.5862 0.0868  -0.0546 -0.0449 37  GLN C CG  
16742 C CD  . GLN C 37  ? 0.9708 0.9835 0.6062 0.0800  -0.0403 -0.0124 37  GLN C CD  
16743 O OE1 . GLN C 37  ? 0.9776 1.0079 0.6396 0.0712  -0.0205 0.0001  37  GLN C OE1 
16744 N NE2 . GLN C 37  ? 1.0160 1.0163 0.6051 0.0833  -0.0507 0.0018  37  GLN C NE2 
16753 N N   . GLN C 38  ? 0.9417 0.9150 0.6405 0.0959  -0.0461 -0.1050 38  GLN C N   
16754 C CA  . GLN C 38  ? 0.9300 0.9006 0.6155 0.1120  -0.0260 -0.1159 38  GLN C CA  
16755 C C   . GLN C 38  ? 0.9225 0.9065 0.5579 0.1242  -0.0197 -0.1231 38  GLN C C   
16756 O O   . GLN C 38  ? 0.9136 0.8844 0.5172 0.1238  -0.0352 -0.1425 38  GLN C O   
16757 C CB  . GLN C 38  ? 0.9596 0.8893 0.6504 0.1141  -0.0267 -0.1416 38  GLN C CB  
16758 C CG  . GLN C 38  ? 0.9914 0.9089 0.6669 0.1379  -0.0067 -0.1517 38  GLN C CG  
16759 C CD  . GLN C 38  ? 1.0345 0.8977 0.7159 0.1398  -0.0045 -0.1676 38  GLN C CD  
16760 O OE1 . GLN C 38  ? 1.0528 0.8816 0.7322 0.1224  -0.0154 -0.1860 38  GLN C OE1 
16761 N NE2 . GLN C 38  ? 1.0600 0.9157 0.7486 0.1607  0.0098  -0.1599 38  GLN C NE2 
16770 N N   . LYS C 39  ? 0.9986 1.0136 0.6277 0.1350  0.0031  -0.1093 39  LYS C N   
16771 C CA  . LYS C 39  ? 1.1001 1.1325 0.6783 0.1490  0.0168  -0.1141 39  LYS C CA  
16772 C C   . LYS C 39  ? 1.1507 1.1686 0.7088 0.1739  0.0295  -0.1445 39  LYS C C   
16773 O O   . LYS C 39  ? 1.1475 1.1462 0.7348 0.1817  0.0325  -0.1538 39  LYS C O   
16774 C CB  . LYS C 39  ? 1.1151 1.1940 0.7006 0.1447  0.0399  -0.0830 39  LYS C CB  
16775 C CG  . LYS C 39  ? 1.1321 1.2097 0.7138 0.1225  0.0284  -0.0537 39  LYS C CG  
16776 C CD  . LYS C 39  ? 1.1617 1.2756 0.7710 0.1073  0.0503  -0.0225 39  LYS C CD  
16777 C CE  . LYS C 39  ? 1.2055 1.3049 0.7872 0.0890  0.0449  0.0076  39  LYS C CE  
16778 N NZ  . LYS C 39  ? 1.2786 1.3737 0.7857 0.1005  0.0516  0.0101  39  LYS C NZ  
16792 N N   . PRO C 40  ? 1.2250 1.2455 0.7262 0.1898  0.0373  -0.1608 40  PRO C N   
16793 C CA  . PRO C 40  ? 1.2885 1.2801 0.7618 0.2155  0.0454  -0.1967 40  PRO C CA  
16794 C C   . PRO C 40  ? 1.2994 1.3041 0.8055 0.2381  0.0685  -0.1954 40  PRO C C   
16795 O O   . PRO C 40  ? 1.3272 1.2864 0.8252 0.2568  0.0687  -0.2217 40  PRO C O   
16796 C CB  . PRO C 40  ? 1.3768 1.3852 0.7808 0.2314  0.0560  -0.2072 40  PRO C CB  
16797 C CG  . PRO C 40  ? 1.3781 1.4028 0.7653 0.2102  0.0412  -0.1824 40  PRO C CG  
16798 C CD  . PRO C 40  ? 1.2859 1.3298 0.7376 0.1879  0.0404  -0.1469 40  PRO C CD  
16806 N N   . ASP C 41  ? 1.2983 1.3625 0.8414 0.2372  0.0868  -0.1663 41  ASP C N   
16807 C CA  . ASP C 41  ? 1.3218 1.4135 0.9006 0.2628  0.1055  -0.1665 41  ASP C CA  
16808 C C   . ASP C 41  ? 1.3471 1.4048 0.9683 0.2599  0.0898  -0.1636 41  ASP C C   
16809 O O   . ASP C 41  ? 1.4228 1.4956 1.0689 0.2866  0.0997  -0.1650 41  ASP C O   
16810 C CB  . ASP C 41  ? 1.3041 1.4807 0.9173 0.2574  0.1286  -0.1388 41  ASP C CB  
16811 C CG  . ASP C 41  ? 1.2914 1.4826 0.9447 0.2185  0.1154  -0.1073 41  ASP C CG  
16812 O OD1 . ASP C 41  ? 1.3037 1.4447 0.9576 0.2001  0.0892  -0.1067 41  ASP C OD1 
16813 O OD2 . ASP C 41  ? 1.2943 1.5480 0.9800 0.2055  0.1324  -0.0847 41  ASP C OD2 
16818 N N   . GLY C 42  ? 1.2749 1.2902 0.9025 0.2314  0.0663  -0.1597 42  GLY C N   
16819 C CA  . GLY C 42  ? 1.2010 1.1838 0.8621 0.2257  0.0544  -0.1539 42  GLY C CA  
16820 C C   . GLY C 42  ? 1.1103 1.1271 0.8160 0.2006  0.0458  -0.1251 42  GLY C C   
16821 O O   . GLY C 42  ? 1.1111 1.0968 0.8365 0.1901  0.0334  -0.1202 42  GLY C O   
16825 N N   . THR C 43  ? 1.0702 1.1453 0.7886 0.1898  0.0541  -0.1063 43  THR C N   
16826 C CA  . THR C 43  ? 1.0122 1.1121 0.7690 0.1640  0.0457  -0.0814 43  THR C CA  
16827 C C   . THR C 43  ? 0.9628 1.0164 0.7174 0.1421  0.0234  -0.0799 43  THR C C   
16828 O O   . THR C 43  ? 0.9968 1.0220 0.7205 0.1370  0.0146  -0.0914 43  THR C O   
16829 C CB  . THR C 43  ? 1.0388 1.1886 0.7949 0.1484  0.0589  -0.0624 43  THR C CB  
16830 O OG1 . THR C 43  ? 1.0389 1.2473 0.8104 0.1665  0.0831  -0.0634 43  THR C OG1 
16831 C CG2 . THR C 43  ? 1.0441 1.2034 0.8331 0.1182  0.0484  -0.0386 43  THR C CG2 
16839 N N   . VAL C 44  ? 0.8441 0.8959 0.6328 0.1307  0.0135  -0.0678 44  VAL C N   
16840 C CA  . VAL C 44  ? 0.8152 0.8327 0.6090 0.1126  -0.0044 -0.0659 44  VAL C CA  
16841 C C   . VAL C 44  ? 0.7620 0.8002 0.5817 0.0942  -0.0111 -0.0449 44  VAL C C   
16842 O O   . VAL C 44  ? 0.7444 0.8079 0.5909 0.0955  -0.0078 -0.0373 44  VAL C O   
16843 C CB  . VAL C 44  ? 0.8659 0.8433 0.6662 0.1197  -0.0079 -0.0765 44  VAL C CB  
16844 C CG1 . VAL C 44  ? 0.8508 0.8049 0.6622 0.1004  -0.0218 -0.0749 44  VAL C CG1 
16845 C CG2 . VAL C 44  ? 0.9340 0.8769 0.7056 0.1351  -0.0007 -0.0985 44  VAL C CG2 
16855 N N   . LYS C 45  ? 0.7745 0.8000 0.5851 0.0788  -0.0227 -0.0375 45  LYS C N   
16856 C CA  . LYS C 45  ? 0.7836 0.8120 0.6112 0.0619  -0.0304 -0.0193 45  LYS C CA  
16857 C C   . LYS C 45  ? 0.8067 0.8036 0.6383 0.0577  -0.0480 -0.0232 45  LYS C C   
16858 O O   . LYS C 45  ? 0.8421 0.8256 0.6592 0.0614  -0.0558 -0.0345 45  LYS C O   
16859 C CB  . LYS C 45  ? 0.8445 0.8840 0.6514 0.0506  -0.0250 -0.0014 45  LYS C CB  
16860 C CG  . LYS C 45  ? 0.9652 1.0475 0.7754 0.0500  -0.0025 0.0054  45  LYS C CG  
16861 C CD  . LYS C 45  ? 1.1151 1.2006 0.8931 0.0376  0.0078  0.0255  45  LYS C CD  
16862 C CE  . LYS C 45  ? 1.1707 1.2299 0.9534 0.0147  -0.0016 0.0471  45  LYS C CE  
16863 N NZ  . LYS C 45  ? 1.2508 1.3031 0.9949 0.0017  0.0120  0.0721  45  LYS C NZ  
16877 N N   . LEU C 46  ? 0.7806 0.7707 0.6338 0.0504  -0.0546 -0.0164 46  LEU C N   
16878 C CA  . LEU C 46  ? 0.7644 0.7306 0.6221 0.0485  -0.0690 -0.0184 46  LEU C CA  
16879 C C   . LEU C 46  ? 0.8113 0.7668 0.6518 0.0430  -0.0784 -0.0040 46  LEU C C   
16880 O O   . LEU C 46  ? 0.8240 0.7796 0.6600 0.0317  -0.0740 0.0124  46  LEU C O   
16881 C CB  . LEU C 46  ? 0.7715 0.7295 0.6498 0.0467  -0.0721 -0.0186 46  LEU C CB  
16882 C CG  . LEU C 46  ? 0.7525 0.6890 0.6355 0.0477  -0.0843 -0.0209 46  LEU C CG  
16883 C CD1 . LEU C 46  ? 0.7414 0.6777 0.6299 0.0545  -0.0842 -0.0357 46  LEU C CD1 
16884 C CD2 . LEU C 46  ? 0.7458 0.6720 0.6395 0.0467  -0.0870 -0.0216 46  LEU C CD2 
16896 N N   . LEU C 47  ? 0.8401 0.7861 0.6709 0.0507  -0.0916 -0.0100 47  LEU C N   
16897 C CA  . LEU C 47  ? 0.8596 0.7882 0.6672 0.0536  -0.1046 0.0043  47  LEU C CA  
16898 C C   . LEU C 47  ? 0.8692 0.7774 0.6925 0.0599  -0.1189 0.0032  47  LEU C C   
16899 O O   . LEU C 47  ? 0.8899 0.7691 0.7040 0.0563  -0.1227 0.0187  47  LEU C O   
16900 C CB  . LEU C 47  ? 0.8856 0.8239 0.6674 0.0649  -0.1148 -0.0032 47  LEU C CB  
16901 C CG  . LEU C 47  ? 0.9227 0.8783 0.6802 0.0644  -0.1024 -0.0083 47  LEU C CG  
16902 C CD1 . LEU C 47  ? 0.9031 0.8670 0.6389 0.0763  -0.1197 -0.0245 47  LEU C CD1 
16903 C CD2 . LEU C 47  ? 0.9815 0.9340 0.7091 0.0572  -0.0876 0.0165  47  LEU C CD2 
16915 N N   . ILE C 48  ? 0.8304 0.7523 0.6777 0.0685  -0.1249 -0.0161 48  ILE C N   
16916 C CA  . ILE C 48  ? 0.7485 0.6623 0.6128 0.0804  -0.1371 -0.0213 48  ILE C CA  
16917 C C   . ILE C 48  ? 0.6895 0.6131 0.5851 0.0770  -0.1255 -0.0361 48  ILE C C   
16918 O O   . ILE C 48  ? 0.6409 0.5812 0.5472 0.0698  -0.1139 -0.0471 48  ILE C O   
16919 C CB  . ILE C 48  ? 0.7595 0.6936 0.6260 0.0966  -0.1557 -0.0312 48  ILE C CB  
16920 C CG1 . ILE C 48  ? 0.8209 0.7399 0.6428 0.1046  -0.1683 -0.0138 48  ILE C CG1 
16921 C CG2 . ILE C 48  ? 0.7883 0.7246 0.6800 0.1137  -0.1663 -0.0392 48  ILE C CG2 
16922 C CD1 . ILE C 48  ? 0.8473 0.7202 0.6438 0.1125  -0.1751 0.0090  48  ILE C CD1 
16934 N N   . PHE C 49  ? 0.6904 0.5969 0.5940 0.0835  -0.1277 -0.0362 49  PHE C N   
16935 C CA  . PHE C 49  ? 0.7016 0.6167 0.6272 0.0847  -0.1162 -0.0497 49  PHE C CA  
16936 C C   . PHE C 49  ? 0.7222 0.6367 0.6614 0.1030  -0.1244 -0.0576 49  PHE C C   
16937 O O   . PHE C 49  ? 0.6900 0.5831 0.6160 0.1160  -0.1402 -0.0503 49  PHE C O   
16938 C CB  . PHE C 49  ? 0.7307 0.6280 0.6466 0.0761  -0.1066 -0.0451 49  PHE C CB  
16939 C CG  . PHE C 49  ? 0.7630 0.6283 0.6649 0.0766  -0.1167 -0.0376 49  PHE C CG  
16940 C CD1 . PHE C 49  ? 0.7894 0.6394 0.6758 0.0647  -0.1223 -0.0224 49  PHE C CD1 
16941 C CD2 . PHE C 49  ? 0.7525 0.6002 0.6547 0.0870  -0.1185 -0.0469 49  PHE C CD2 
16942 C CE1 . PHE C 49  ? 0.8164 0.6296 0.6909 0.0587  -0.1306 -0.0164 49  PHE C CE1 
16943 C CE2 . PHE C 49  ? 0.7457 0.5550 0.6322 0.0855  -0.1293 -0.0439 49  PHE C CE2 
16944 C CZ  . PHE C 49  ? 0.7912 0.5809 0.6654 0.0690  -0.1358 -0.0285 49  PHE C CZ  
16954 N N   . TYR C 50  ? 0.7579 0.6941 0.7213 0.1056  -0.1113 -0.0719 50  TYR C N   
16955 C CA  . TYR C 50  ? 0.7354 0.6867 0.7204 0.1255  -0.1137 -0.0839 50  TYR C CA  
16956 C C   . TYR C 50  ? 0.6946 0.6672 0.6918 0.1419  -0.1353 -0.0860 50  TYR C C   
16957 O O   . TYR C 50  ? 0.7187 0.6768 0.7109 0.1665  -0.1497 -0.0854 50  TYR C O   
16958 C CB  . TYR C 50  ? 0.7267 0.6383 0.6907 0.1383  -0.1156 -0.0824 50  TYR C CB  
16959 C CG  . TYR C 50  ? 0.6913 0.6218 0.6758 0.1589  -0.1068 -0.0989 50  TYR C CG  
16960 C CD1 . TYR C 50  ? 0.6856 0.6521 0.6931 0.1515  -0.0822 -0.1091 50  TYR C CD1 
16961 C CD2 . TYR C 50  ? 0.6796 0.5889 0.6578 0.1867  -0.1203 -0.1036 50  TYR C CD2 
16962 C CE1 . TYR C 50  ? 0.7079 0.6992 0.7353 0.1695  -0.0687 -0.1239 50  TYR C CE1 
16963 C CE2 . TYR C 50  ? 0.7040 0.6364 0.7019 0.2099  -0.1097 -0.1210 50  TYR C CE2 
16964 C CZ  . TYR C 50  ? 0.7104 0.6889 0.7347 0.2004  -0.0826 -0.1312 50  TYR C CZ  
16965 O OH  . TYR C 50  ? 0.7391 0.7477 0.7841 0.2228  -0.0669 -0.1481 50  TYR C OH  
16975 N N   . THR C 51  ? 0.6725 0.6762 0.6812 0.1306  -0.1394 -0.0897 51  THR C N   
16976 C CA  . THR C 51  ? 0.6969 0.7331 0.7184 0.1462  -0.1626 -0.0959 51  THR C CA  
16977 C C   . THR C 51  ? 0.7390 0.7356 0.7146 0.1603  -0.1843 -0.0759 51  THR C C   
16978 O O   . THR C 51  ? 0.7986 0.8093 0.7607 0.1620  -0.1999 -0.0743 51  THR C O   
16979 C CB  . THR C 51  ? 0.6659 0.7432 0.7294 0.1703  -0.1674 -0.1125 51  THR C CB  
16980 O OG1 . THR C 51  ? 0.6688 0.7869 0.7756 0.1529  -0.1423 -0.1295 51  THR C OG1 
16981 C CG2 . THR C 51  ? 0.6728 0.7930 0.7524 0.1910  -0.1969 -0.1208 51  THR C CG2 
16989 N N   . SER C 52  ? 0.7688 0.7116 0.7158 0.1693  -0.1850 -0.0609 52  SER C N   
16990 C CA  . SER C 52  ? 0.8408 0.7388 0.7434 0.1838  -0.2041 -0.0400 52  SER C CA  
16991 C C   . SER C 52  ? 0.8611 0.6927 0.7267 0.1690  -0.1958 -0.0199 52  SER C C   
16992 O O   . SER C 52  ? 0.8884 0.6683 0.7159 0.1803  -0.2081 -0.0011 52  SER C O   
16993 C CB  . SER C 52  ? 0.8545 0.7524 0.7629 0.2238  -0.2253 -0.0447 52  SER C CB  
16994 O OG  . SER C 52  ? 0.8517 0.7227 0.7685 0.2346  -0.2171 -0.0514 52  SER C OG  
17000 N N   . LYS C 53  ? 0.8927 0.7230 0.7675 0.1440  -0.1765 -0.0231 53  LYS C N   
17001 C CA  . LYS C 53  ? 0.9519 0.7317 0.8023 0.1264  -0.1708 -0.0093 53  LYS C CA  
17002 C C   . LYS C 53  ? 0.9682 0.7549 0.8038 0.1004  -0.1612 0.0057  53  LYS C C   
17003 O O   . LYS C 53  ? 0.8986 0.7256 0.7515 0.0892  -0.1494 -0.0026 53  LYS C O   
17004 C CB  . LYS C 53  ? 0.9117 0.6916 0.7800 0.1199  -0.1596 -0.0246 53  LYS C CB  
17005 C CG  . LYS C 53  ? 0.9158 0.7019 0.8012 0.1471  -0.1625 -0.0429 53  LYS C CG  
17006 C CD  . LYS C 53  ? 0.9693 0.7062 0.8328 0.1726  -0.1804 -0.0376 53  LYS C CD  
17007 C CE  . LYS C 53  ? 0.9942 0.7473 0.8789 0.2058  -0.1819 -0.0584 53  LYS C CE  
17008 N NZ  . LYS C 53  ? 1.0969 0.7900 0.9546 0.2362  -0.1995 -0.0547 53  LYS C NZ  
17022 N N   . LEU C 54  ? 1.0407 0.7851 0.8423 0.0917  -0.1641 0.0282  54  LEU C N   
17023 C CA  . LEU C 54  ? 1.0454 0.8011 0.8335 0.0674  -0.1507 0.0433  54  LEU C CA  
17024 C C   . LEU C 54  ? 1.0297 0.7977 0.8407 0.0420  -0.1367 0.0379  54  LEU C C   
17025 O O   . LEU C 54  ? 1.0478 0.7840 0.8628 0.0337  -0.1399 0.0354  54  LEU C O   
17026 C CB  . LEU C 54  ? 1.1250 0.8303 0.8681 0.0621  -0.1529 0.0718  54  LEU C CB  
17027 C CG  . LEU C 54  ? 1.2363 0.9402 0.9408 0.0824  -0.1628 0.0851  54  LEU C CG  
17028 C CD1 . LEU C 54  ? 1.3775 1.0275 1.0313 0.0685  -0.1554 0.1187  54  LEU C CD1 
17029 C CD2 . LEU C 54  ? 1.2459 1.0110 0.9587 0.0822  -0.1566 0.0736  54  LEU C CD2 
17041 N N   . HIS C 55  ? 0.9876 0.8012 0.8117 0.0323  -0.1234 0.0341  55  HIS C N   
17042 C CA  . HIS C 55  ? 0.9458 0.7795 0.7912 0.0126  -0.1126 0.0305  55  HIS C CA  
17043 C C   . HIS C 55  ? 0.9871 0.8078 0.8229 -0.0138 -0.1046 0.0503  55  HIS C C   
17044 O O   . HIS C 55  ? 1.0224 0.8321 0.8303 -0.0172 -0.0990 0.0692  55  HIS C O   
17045 C CB  . HIS C 55  ? 0.8610 0.7438 0.7213 0.0164  -0.1009 0.0204  55  HIS C CB  
17046 C CG  . HIS C 55  ? 0.8394 0.7494 0.7224 0.0043  -0.0932 0.0159  55  HIS C CG  
17047 N ND1 . HIS C 55  ? 0.8362 0.7859 0.7266 -0.0016 -0.0793 0.0194  55  HIS C ND1 
17048 C CD2 . HIS C 55  ? 0.8269 0.7341 0.7257 0.0002  -0.0996 0.0065  55  HIS C CD2 
17049 C CE1 . HIS C 55  ? 0.8385 0.8136 0.7539 -0.0077 -0.0789 0.0127  55  HIS C CE1 
17050 N NE2 . HIS C 55  ? 0.8456 0.7944 0.7642 -0.0076 -0.0925 0.0047  55  HIS C NE2 
17058 N N   . SER C 56  ? 0.9919 0.8152 0.8498 -0.0341 -0.1039 0.0455  56  SER C N   
17059 C CA  . SER C 56  ? 1.0324 0.8502 0.8927 -0.0674 -0.0943 0.0615  56  SER C CA  
17060 C C   . SER C 56  ? 1.0040 0.8659 0.8612 -0.0745 -0.0735 0.0756  56  SER C C   
17061 O O   . SER C 56  ? 0.9560 0.8743 0.8337 -0.0649 -0.0656 0.0643  56  SER C O   
17062 C CB  . SER C 56  ? 1.0683 0.9089 0.9655 -0.0876 -0.0985 0.0462  56  SER C CB  
17063 O OG  . SER C 56  ? 1.1449 1.0097 1.0611 -0.1235 -0.0847 0.0580  56  SER C OG  
17069 N N   . GLY C 57  ? 1.0724 0.9030 0.8974 -0.0885 -0.0635 0.1008  57  GLY C N   
17070 C CA  . GLY C 57  ? 1.0859 0.9555 0.9032 -0.1005 -0.0388 0.1165  57  GLY C CA  
17071 C C   . GLY C 57  ? 1.1018 0.9673 0.8725 -0.0745 -0.0359 0.1252  57  GLY C C   
17072 O O   . GLY C 57  ? 1.1271 1.0094 0.8742 -0.0836 -0.0142 0.1427  57  GLY C O   
17076 N N   . VAL C 58  ? 1.0967 0.9454 0.8542 -0.0435 -0.0566 0.1118  58  VAL C N   
17077 C CA  . VAL C 58  ? 1.1825 1.0337 0.8989 -0.0194 -0.0592 0.1143  58  VAL C CA  
17078 C C   . VAL C 58  ? 1.2273 1.0155 0.8902 -0.0134 -0.0691 0.1392  58  VAL C C   
17079 O O   . VAL C 58  ? 1.2531 0.9903 0.9166 -0.0160 -0.0819 0.1450  58  VAL C O   
17080 C CB  . VAL C 58  ? 1.2034 1.0757 0.9373 0.0072  -0.0759 0.0858  58  VAL C CB  
17081 C CG1 . VAL C 58  ? 1.1748 1.0963 0.9491 0.0043  -0.0642 0.0659  58  VAL C CG1 
17082 C CG2 . VAL C 58  ? 1.2054 1.0442 0.9526 0.0185  -0.0980 0.0774  58  VAL C CG2 
17092 N N   . PRO C 59  ? 1.2496 1.0346 0.8596 -0.0019 -0.0645 0.1542  59  PRO C N   
17093 C CA  . PRO C 59  ? 1.3548 1.0734 0.9027 0.0044  -0.0712 0.1849  59  PRO C CA  
17094 C C   . PRO C 59  ? 1.3296 1.0148 0.8651 0.0392  -0.1061 0.1766  59  PRO C C   
17095 O O   . PRO C 59  ? 1.2795 1.0022 0.8499 0.0587  -0.1236 0.1467  59  PRO C O   
17096 C CB  . PRO C 59  ? 1.3781 1.1143 0.8690 0.0109  -0.0558 0.1997  59  PRO C CB  
17097 C CG  . PRO C 59  ? 1.3212 1.1284 0.8441 0.0207  -0.0533 0.1669  59  PRO C CG  
17098 C CD  . PRO C 59  ? 1.2195 1.0568 0.8172 0.0033  -0.0484 0.1467  59  PRO C CD  
17106 N N   . SER C 60  ? 1.3741 0.9865 0.8581 0.0471  -0.1144 0.2051  60  SER C N   
17107 C CA  . SER C 60  ? 1.4112 0.9875 0.8811 0.0850  -0.1479 0.2006  60  SER C CA  
17108 C C   . SER C 60  ? 1.3934 1.0070 0.8380 0.1225  -0.1708 0.1891  60  SER C C   
17109 O O   . SER C 60  ? 1.3896 1.0032 0.8433 0.1564  -0.2009 0.1751  60  SER C O   
17110 C CB  . SER C 60  ? 1.5687 1.0464 0.9802 0.0866  -0.1497 0.2372  60  SER C CB  
17111 O OG  . SER C 60  ? 1.6999 1.1513 1.0490 0.0689  -0.1261 0.2729  60  SER C OG  
17117 N N   . ARG C 61  ? 1.4052 1.0540 0.8190 0.1180  -0.1581 0.1921  61  ARG C N   
17118 C CA  . ARG C 61  ? 1.3878 1.0758 0.7785 0.1505  -0.1829 0.1746  61  ARG C CA  
17119 C C   . ARG C 61  ? 1.3012 1.0469 0.7653 0.1603  -0.2023 0.1316  61  ARG C C   
17120 O O   . ARG C 61  ? 1.3417 1.1070 0.8072 0.1916  -0.2345 0.1156  61  ARG C O   
17121 C CB  . ARG C 61  ? 1.3943 1.1161 0.7483 0.1402  -0.1621 0.1756  61  ARG C CB  
17122 C CG  . ARG C 61  ? 1.4998 1.1791 0.7949 0.1189  -0.1289 0.2171  61  ARG C CG  
17123 C CD  . ARG C 61  ? 1.5494 1.2640 0.7946 0.1207  -0.1116 0.2166  61  ARG C CD  
17124 N NE  . ARG C 61  ? 1.4013 1.1845 0.7041 0.1091  -0.0995 0.1795  61  ARG C NE  
17125 C CZ  . ARG C 61  ? 1.3546 1.1655 0.6870 0.0803  -0.0623 0.1810  61  ARG C CZ  
17126 N NH1 . ARG C 61  ? 1.3967 1.1812 0.7144 0.0534  -0.0315 0.2161  61  ARG C NH1 
17127 N NH2 . ARG C 61  ? 1.2941 1.1595 0.6721 0.0786  -0.0559 0.1468  61  ARG C NH2 
17141 N N   . PHE C 62  ? 1.1936 0.9694 0.7193 0.1338  -0.1827 0.1130  62  PHE C N   
17142 C CA  . PHE C 62  ? 1.1462 0.9697 0.7374 0.1379  -0.1939 0.0762  62  PHE C CA  
17143 C C   . PHE C 62  ? 1.1657 0.9693 0.7888 0.1527  -0.2104 0.0725  62  PHE C C   
17144 O O   . PHE C 62  ? 1.2009 0.9536 0.8171 0.1459  -0.2032 0.0918  62  PHE C O   
17145 C CB  . PHE C 62  ? 1.0910 0.9428 0.7257 0.1095  -0.1671 0.0621  62  PHE C CB  
17146 C CG  . PHE C 62  ? 1.1033 0.9795 0.7117 0.1006  -0.1498 0.0601  62  PHE C CG  
17147 C CD1 . PHE C 62  ? 1.0997 1.0128 0.7108 0.1095  -0.1592 0.0318  62  PHE C CD1 
17148 C CD2 . PHE C 62  ? 1.1243 0.9878 0.7069 0.0825  -0.1230 0.0842  62  PHE C CD2 
17149 C CE1 . PHE C 62  ? 1.1214 1.0514 0.7030 0.1054  -0.1432 0.0266  62  PHE C CE1 
17150 C CE2 . PHE C 62  ? 1.1339 1.0248 0.6924 0.0788  -0.1044 0.0804  62  PHE C CE2 
17151 C CZ  . PHE C 62  ? 1.1312 1.0520 0.6857 0.0928  -0.1150 0.0511  62  PHE C CZ  
17161 N N   . SER C 63  ? 1.1243 0.9701 0.7837 0.1725  -0.2320 0.0452  63  SER C N   
17162 C CA  . SER C 63  ? 1.1379 0.9812 0.8344 0.1919  -0.2463 0.0355  63  SER C CA  
17163 C C   . SER C 63  ? 1.0746 0.9891 0.8326 0.1937  -0.2536 -0.0014 63  SER C C   
17164 O O   . SER C 63  ? 1.0459 1.0013 0.8034 0.1905  -0.2608 -0.0172 63  SER C O   
17165 C CB  . SER C 63  ? 1.2417 1.0481 0.8949 0.2300  -0.2737 0.0534  63  SER C CB  
17166 O OG  . SER C 63  ? 1.2535 1.1098 0.9042 0.2564  -0.3023 0.0377  63  SER C OG  
17172 N N   . GLY C 64  ? 1.0225 0.9492 0.8310 0.1966  -0.2496 -0.0159 64  GLY C N   
17173 C CA  . GLY C 64  ? 0.9683 0.9591 0.8393 0.1901  -0.2473 -0.0481 64  GLY C CA  
17174 C C   . GLY C 64  ? 0.9774 1.0017 0.8880 0.2205  -0.2658 -0.0632 64  GLY C C   
17175 O O   . GLY C 64  ? 1.0098 0.9960 0.9050 0.2457  -0.2733 -0.0503 64  GLY C O   
17179 N N   . SER C 65  ? 1.0109 1.1076 0.9751 0.2176  -0.2722 -0.0925 65  SER C N   
17180 C CA  . SER C 65  ? 0.9844 1.1351 0.9975 0.2473  -0.2905 -0.1111 65  SER C CA  
17181 C C   . SER C 65  ? 0.8666 1.0894 0.9552 0.2230  -0.2744 -0.1425 65  SER C C   
17182 O O   . SER C 65  ? 0.8478 1.0803 0.9437 0.1874  -0.2601 -0.1522 65  SER C O   
17183 C CB  . SER C 65  ? 1.0859 1.2643 1.0799 0.2805  -0.3312 -0.1131 65  SER C CB  
17184 O OG  . SER C 65  ? 1.1746 1.2774 1.0900 0.3022  -0.3428 -0.0796 65  SER C OG  
17190 N N   . GLY C 66  ? 0.8433 1.1140 0.9867 0.2432  -0.2748 -0.1582 66  GLY C N   
17191 C CA  . GLY C 66  ? 0.8094 1.1592 1.0307 0.2207  -0.2594 -0.1880 66  GLY C CA  
17192 C C   . GLY C 66  ? 0.7936 1.1577 1.0550 0.2253  -0.2305 -0.1937 66  GLY C C   
17193 O O   . GLY C 66  ? 0.8076 1.1167 1.0351 0.2484  -0.2247 -0.1774 66  GLY C O   
17197 N N   . SER C 67  ? 0.7738 1.2108 1.1060 0.2014  -0.2110 -0.2183 67  SER C N   
17198 C CA  . SER C 67  ? 0.7337 1.1954 1.1063 0.2007  -0.1767 -0.2258 67  SER C CA  
17199 C C   . SER C 67  ? 0.7039 1.2451 1.1513 0.1606  -0.1552 -0.2510 67  SER C C   
17200 O O   . SER C 67  ? 0.6940 1.2834 1.1723 0.1429  -0.1760 -0.2683 67  SER C O   
17201 C CB  . SER C 67  ? 0.7319 1.2255 1.1262 0.2541  -0.1905 -0.2320 67  SER C CB  
17202 O OG  . SER C 67  ? 0.7452 1.3398 1.2068 0.2711  -0.2167 -0.2569 67  SER C OG  
17208 N N   . GLY C 68  ? 0.7004 1.2525 1.1735 0.1450  -0.1129 -0.2533 68  GLY C N   
17209 C CA  . GLY C 68  ? 0.7140 1.3339 1.2566 0.1018  -0.0843 -0.2736 68  GLY C CA  
17210 C C   . GLY C 68  ? 0.7336 1.3121 1.2550 0.0518  -0.0775 -0.2714 68  GLY C C   
17211 O O   . GLY C 68  ? 0.7453 1.2449 1.2133 0.0325  -0.0506 -0.2515 68  GLY C O   
17215 N N   . THR C 69  ? 0.7338 1.3639 1.2940 0.0335  -0.1042 -0.2939 69  THR C N   
17216 C CA  . THR C 69  ? 0.7440 1.3355 1.2862 -0.0127 -0.1001 -0.2983 69  THR C CA  
17217 C C   . THR C 69  ? 0.7886 1.3520 1.2834 -0.0003 -0.1443 -0.2991 69  THR C C   
17218 O O   . THR C 69  ? 0.8837 1.3928 1.3416 -0.0296 -0.1401 -0.2984 69  THR C O   
17219 C CB  . THR C 69  ? 0.6994 1.3708 1.3291 -0.0602 -0.0861 -0.3303 69  THR C CB  
17220 O OG1 . THR C 69  ? 0.7242 1.5007 1.4197 -0.0425 -0.1267 -0.3596 69  THR C OG1 
17221 C CG2 . THR C 69  ? 0.6950 1.3916 1.3673 -0.0789 -0.0336 -0.3269 69  THR C CG2 
17229 N N   . ASP C 70  ? 0.7372 1.3311 1.2258 0.0446  -0.1848 -0.2996 70  ASP C N   
17230 C CA  . ASP C 70  ? 0.7454 1.3196 1.1854 0.0591  -0.2266 -0.3000 70  ASP C CA  
17231 C C   . ASP C 70  ? 0.7144 1.2085 1.0708 0.0968  -0.2348 -0.2646 70  ASP C C   
17232 O O   . ASP C 70  ? 0.7106 1.2025 1.0654 0.1322  -0.2353 -0.2511 70  ASP C O   
17233 C CB  . ASP C 70  ? 0.7850 1.4578 1.2779 0.0809  -0.2710 -0.3283 70  ASP C CB  
17234 C CG  . ASP C 70  ? 0.8291 1.5866 1.4086 0.0354  -0.2680 -0.3682 70  ASP C CG  
17235 O OD1 . ASP C 70  ? 0.8268 1.6535 1.4862 0.0239  -0.2444 -0.3814 70  ASP C OD1 
17236 O OD2 . ASP C 70  ? 0.8800 1.6342 1.4473 0.0091  -0.2874 -0.3876 70  ASP C OD2 
17241 N N   . TYR C 71  ? 0.7131 1.1413 1.0013 0.0882  -0.2397 -0.2513 71  TYR C N   
17242 C CA  . TYR C 71  ? 0.7501 1.1021 0.9615 0.1132  -0.2421 -0.2175 71  TYR C CA  
17243 C C   . TYR C 71  ? 0.7951 1.1228 0.9482 0.1167  -0.2673 -0.2145 71  TYR C C   
17244 O O   . TYR C 71  ? 0.8726 1.2260 1.0364 0.0947  -0.2768 -0.2389 71  TYR C O   
17245 C CB  . TYR C 71  ? 0.7438 1.0295 0.9286 0.0937  -0.2028 -0.1974 71  TYR C CB  
17246 C CG  . TYR C 71  ? 0.7533 1.0552 0.9813 0.0911  -0.1747 -0.1989 71  TYR C CG  
17247 C CD1 . TYR C 71  ? 0.7685 1.1072 1.0499 0.0586  -0.1496 -0.2181 71  TYR C CD1 
17248 C CD2 . TYR C 71  ? 0.7950 1.0706 1.0057 0.1199  -0.1713 -0.1815 71  TYR C CD2 
17249 C CE1 . TYR C 71  ? 0.8297 1.1841 1.1439 0.0571  -0.1198 -0.2177 71  TYR C CE1 
17250 C CE2 . TYR C 71  ? 0.8323 1.1223 1.0747 0.1207  -0.1448 -0.1850 71  TYR C CE2 
17251 C CZ  . TYR C 71  ? 0.8462 1.1778 1.1388 0.0902  -0.1178 -0.2020 71  TYR C CZ  
17252 O OH  . TYR C 71  ? 0.8526 1.1992 1.1703 0.0919  -0.0873 -0.2037 71  TYR C OH  
17262 N N   . SER C 72  ? 0.7429 1.0174 0.8309 0.1431  -0.2764 -0.1850 72  SER C N   
17263 C CA  . SER C 72  ? 0.8409 1.0913 0.8644 0.1505  -0.2967 -0.1777 72  SER C CA  
17264 C C   . SER C 72  ? 0.8918 1.0668 0.8469 0.1601  -0.2836 -0.1397 72  SER C C   
17265 O O   . SER C 72  ? 0.9380 1.0856 0.8868 0.1791  -0.2813 -0.1190 72  SER C O   
17266 C CB  . SER C 72  ? 0.9179 1.2158 0.9386 0.1839  -0.3414 -0.1884 72  SER C CB  
17267 O OG  . SER C 72  ? 0.9586 1.2398 0.9657 0.2231  -0.3534 -0.1657 72  SER C OG  
17273 N N   . LEU C 73  ? 0.9028 1.0460 0.8087 0.1458  -0.2745 -0.1330 73  LEU C N   
17274 C CA  . LEU C 73  ? 0.9110 0.9954 0.7526 0.1513  -0.2630 -0.0988 73  LEU C CA  
17275 C C   . LEU C 73  ? 0.9588 1.0380 0.7383 0.1757  -0.2901 -0.0886 73  LEU C C   
17276 O O   . LEU C 73  ? 1.0211 1.1327 0.7904 0.1763  -0.3086 -0.1114 73  LEU C O   
17277 C CB  . LEU C 73  ? 0.9202 0.9803 0.7470 0.1245  -0.2327 -0.0974 73  LEU C CB  
17278 C CG  . LEU C 73  ? 0.9682 0.9844 0.7354 0.1249  -0.2179 -0.0668 73  LEU C CG  
17279 C CD1 . LEU C 73  ? 0.9478 0.9301 0.7233 0.1221  -0.2022 -0.0419 73  LEU C CD1 
17280 C CD2 . LEU C 73  ? 0.9723 0.9856 0.7251 0.1073  -0.1964 -0.0761 73  LEU C CD2 
17292 N N   . THR C 74  ? 0.9875 1.0209 0.7204 0.1948  -0.2926 -0.0546 74  THR C N   
17293 C CA  . THR C 74  ? 1.0957 1.1120 0.7573 0.2217  -0.3163 -0.0371 74  THR C CA  
17294 C C   . THR C 74  ? 1.1180 1.0766 0.7125 0.2105  -0.2903 -0.0023 74  THR C C   
17295 O O   . THR C 74  ? 1.1291 1.0454 0.7267 0.1983  -0.2676 0.0211  74  THR C O   
17296 C CB  . THR C 74  ? 1.1380 1.1446 0.7955 0.2599  -0.3444 -0.0245 74  THR C CB  
17297 O OG1 . THR C 74  ? 1.1291 1.2054 0.8585 0.2709  -0.3669 -0.0595 74  THR C OG1 
17298 C CG2 . THR C 74  ? 1.2319 1.2124 0.8033 0.2918  -0.3699 -0.0024 74  THR C CG2 
17306 N N   . ILE C 75  ? 1.1092 1.0699 0.6442 0.2135  -0.2932 -0.0012 75  ILE C N   
17307 C CA  . ILE C 75  ? 1.1805 1.0951 0.6446 0.2065  -0.2684 0.0333  75  ILE C CA  
17308 C C   . ILE C 75  ? 1.3011 1.1868 0.6835 0.2401  -0.2934 0.0582  75  ILE C C   
17309 O O   . ILE C 75  ? 1.3347 1.2528 0.6901 0.2629  -0.3245 0.0386  75  ILE C O   
17310 C CB  . ILE C 75  ? 1.1777 1.1134 0.6260 0.1876  -0.2463 0.0174  75  ILE C CB  
17311 C CG1 . ILE C 75  ? 1.1106 1.0781 0.6365 0.1637  -0.2326 -0.0151 75  ILE C CG1 
17312 C CG2 . ILE C 75  ? 1.1949 1.0934 0.5934 0.1737  -0.2099 0.0535  75  ILE C CG2 
17313 C CD1 . ILE C 75  ? 1.0867 1.0696 0.5964 0.1518  -0.2146 -0.0357 75  ILE C CD1 
17325 N N   . SER C 76  ? 1.1759 0.9829 0.9799 0.2039  -0.1656 0.1183  76  SER C N   
17326 C CA  . SER C 76  ? 1.3275 1.0880 1.0791 0.2252  -0.1751 0.1403  76  SER C CA  
17327 C C   . SER C 76  ? 1.3890 1.1448 1.1119 0.2105  -0.1515 0.1832  76  SER C C   
17328 O O   . SER C 76  ? 1.4603 1.2305 1.2090 0.1768  -0.1329 0.2015  76  SER C O   
17329 C CB  . SER C 76  ? 1.3828 1.0834 1.1267 0.2262  -0.1925 0.1420  76  SER C CB  
17330 O OG  . SER C 76  ? 1.4387 1.1071 1.1854 0.1896  -0.1803 0.1706  76  SER C OG  
17336 N N   . ASN C 77  ? 1.4230 1.1644 1.0929 0.2362  -0.1524 0.1993  77  ASN C N   
17337 C CA  . ASN C 77  ? 1.4517 1.1950 1.0880 0.2272  -0.1274 0.2412  77  ASN C CA  
17338 C C   . ASN C 77  ? 1.3946 1.2026 1.0652 0.2099  -0.1008 0.2423  77  ASN C C   
17339 O O   . ASN C 77  ? 1.4267 1.2521 1.1231 0.1770  -0.0808 0.2672  77  ASN C O   
17340 C CB  . ASN C 77  ? 1.5633 1.2528 1.1846 0.1991  -0.1229 0.2798  77  ASN C CB  
17341 C CG  . ASN C 77  ? 1.6796 1.2974 1.2778 0.2141  -0.1525 0.2706  77  ASN C CG  
17342 O OD1 . ASN C 77  ? 1.6673 1.2683 1.2995 0.2013  -0.1653 0.2509  77  ASN C OD1 
17343 N ND2 . ASN C 77  ? 1.7785 1.3522 1.3143 0.2451  -0.1641 0.2843  77  ASN C ND2 
17350 N N   . LEU C 78  ? 1.3516 1.1939 1.0201 0.2341  -0.1032 0.2139  78  LEU C N   
17351 C CA  . LEU C 78  ? 1.2824 1.1780 0.9751 0.2274  -0.0819 0.2088  78  LEU C CA  
17352 C C   . LEU C 78  ? 1.3898 1.3093 1.0624 0.2215  -0.0504 0.2507  78  LEU C C   
17353 O O   . LEU C 78  ? 1.4522 1.3523 1.0726 0.2369  -0.0444 0.2762  78  LEU C O   
17354 C CB  . LEU C 78  ? 1.1613 1.0710 0.8350 0.2575  -0.0930 0.1736  78  LEU C CB  
17355 C CG  . LEU C 78  ? 1.0947 1.0448 0.7825 0.2582  -0.0768 0.1605  78  LEU C CG  
17356 C CD1 . LEU C 78  ? 1.0384 0.9882 0.7355 0.2667  -0.0986 0.1153  78  LEU C CD1 
17357 C CD2 . LEU C 78  ? 1.0458 1.0095 0.6817 0.2829  -0.0556 0.1807  78  LEU C CD2 
17369 N N   . ASP C 79  ? 1.3731 1.3394 1.0875 0.2004  -0.0296 0.2585  79  ASP C N   
17370 C CA  . ASP C 79  ? 1.3947 1.4034 1.1065 0.1912  0.0029  0.2982  79  ASP C CA  
17371 C C   . ASP C 79  ? 1.3852 1.4417 1.0859 0.2202  0.0206  0.2868  79  ASP C C   
17372 O O   . ASP C 79  ? 1.3647 1.4173 1.0671 0.2377  0.0069  0.2485  79  ASP C O   
17373 C CB  . ASP C 79  ? 1.3594 1.3923 1.1299 0.1457  0.0113  0.3177  79  ASP C CB  
17374 C CG  . ASP C 79  ? 1.4224 1.4822 1.1885 0.1232  0.0380  0.3689  79  ASP C CG  
17375 O OD1 . ASP C 79  ? 1.4502 1.4647 1.2056 0.0967  0.0312  0.3932  79  ASP C OD1 
17376 O OD2 . ASP C 79  ? 1.3883 1.5141 1.1597 0.1323  0.0661  0.3855  79  ASP C OD2 
17381 N N   . GLN C 80  ? 1.4263 1.5272 1.1126 0.2255  0.0521  0.3211  80  GLN C N   
17382 C CA  . GLN C 80  ? 1.4271 1.5729 1.0984 0.2583  0.0711  0.3116  80  GLN C CA  
17383 C C   . GLN C 80  ? 1.3659 1.5450 1.0933 0.2476  0.0701  0.2906  80  GLN C C   
17384 O O   . GLN C 80  ? 1.3696 1.5504 1.0810 0.2763  0.0679  0.2618  80  GLN C O   
17385 C CB  . GLN C 80  ? 1.4361 1.6355 1.0884 0.2661  0.1087  0.3552  80  GLN C CB  
17386 C CG  . GLN C 80  ? 1.4585 1.7101 1.0958 0.3050  0.1318  0.3474  80  GLN C CG  
17387 C CD  . GLN C 80  ? 1.5368 1.7425 1.1060 0.3520  0.1172  0.3107  80  GLN C CD  
17388 O OE1 . GLN C 80  ? 1.6324 1.8003 1.1406 0.3711  0.1117  0.3141  80  GLN C OE1 
17389 N NE2 . GLN C 80  ? 1.5205 1.7250 1.0960 0.3698  0.1090  0.2756  80  GLN C NE2 
17398 N N   . GLU C 81  ? 1.3717 1.5716 1.1596 0.2062  0.0699  0.3046  81  GLU C N   
17399 C CA  . GLU C 81  ? 1.3702 1.6025 1.2093 0.1954  0.0681  0.2877  81  GLU C CA  
17400 C C   . GLU C 81  ? 1.3075 1.4904 1.1532 0.1944  0.0385  0.2438  81  GLU C C   
17401 O O   . GLU C 81  ? 1.2745 1.4738 1.1479 0.1931  0.0360  0.2249  81  GLU C O   
17402 C CB  . GLU C 81  ? 1.4030 1.6738 1.3016 0.1494  0.0747  0.3168  81  GLU C CB  
17403 C CG  . GLU C 81  ? 1.4688 1.6864 1.3737 0.1123  0.0563  0.3265  81  GLU C CG  
17404 C CD  . GLU C 81  ? 1.4958 1.7442 1.4562 0.0632  0.0586  0.3513  81  GLU C CD  
17405 O OE1 . GLU C 81  ? 1.5616 1.7829 1.5172 0.0321  0.0567  0.3789  81  GLU C OE1 
17406 O OE2 . GLU C 81  ? 1.4859 1.7819 1.4911 0.0551  0.0604  0.3434  81  GLU C OE2 
17413 N N   . ASP C 82  ? 1.2901 1.4165 1.1103 0.1963  0.0166  0.2282  82  ASP C N   
17414 C CA  . ASP C 82  ? 1.1524 1.2425 0.9841 0.1930  -0.0099 0.1885  82  ASP C CA  
17415 C C   . ASP C 82  ? 1.1097 1.1956 0.9163 0.2211  -0.0137 0.1564  82  ASP C C   
17416 O O   . ASP C 82  ? 1.0806 1.1533 0.9078 0.2119  -0.0284 0.1271  82  ASP C O   
17417 C CB  . ASP C 82  ? 1.1543 1.1952 0.9651 0.1935  -0.0317 0.1818  82  ASP C CB  
17418 C CG  . ASP C 82  ? 1.1955 1.2169 1.0413 0.1603  -0.0420 0.1909  82  ASP C CG  
17419 O OD1 . ASP C 82  ? 1.1805 1.1917 1.0573 0.1478  -0.0574 0.1646  82  ASP C OD1 
17420 O OD2 . ASP C 82  ? 1.2689 1.2822 1.1075 0.1460  -0.0342 0.2247  82  ASP C OD2 
17425 N N   . ILE C 83  ? 1.1868 1.2782 0.9441 0.2543  -0.0013 0.1610  83  ILE C N   
17426 C CA  . ILE C 83  ? 1.2598 1.3341 0.9824 0.2808  -0.0074 0.1298  83  ILE C CA  
17427 C C   . ILE C 83  ? 1.1542 1.2444 0.9109 0.2712  -0.0034 0.1178  83  ILE C C   
17428 O O   . ILE C 83  ? 1.1320 1.2641 0.9037 0.2767  0.0182  0.1379  83  ILE C O   
17429 C CB  . ILE C 83  ? 1.4459 1.5267 1.1067 0.3211  0.0101  0.1402  83  ILE C CB  
17430 C CG1 . ILE C 83  ? 1.5235 1.6639 1.2015 0.3258  0.0436  0.1765  83  ILE C CG1 
17431 C CG2 . ILE C 83  ? 1.5615 1.6167 1.1777 0.3334  0.0015  0.1475  83  ILE C CG2 
17432 C CD1 . ILE C 83  ? 1.6796 1.8343 1.2987 0.3710  0.0648  0.1833  83  ILE C CD1 
17444 N N   . ALA C 84  ? 1.0756 1.1357 0.8444 0.2575  -0.0242 0.0859  84  ALA C N   
17445 C CA  . ALA C 84  ? 0.9987 1.0656 0.7969 0.2449  -0.0228 0.0752  84  ALA C CA  
17446 C C   . ALA C 84  ? 0.9552 0.9815 0.7500 0.2325  -0.0460 0.0388  84  ALA C C   
17447 O O   . ALA C 84  ? 0.9773 0.9812 0.7563 0.2325  -0.0632 0.0234  84  ALA C O   
17448 C CB  . ALA C 84  ? 0.9900 1.0921 0.8478 0.2146  -0.0164 0.0963  84  ALA C CB  
17454 N N   . THR C 85  ? 0.9241 0.9444 0.7335 0.2218  -0.0465 0.0263  85  THR C N   
17455 C CA  . THR C 85  ? 0.9669 0.9559 0.7809 0.2018  -0.0651 -0.0042 85  THR C CA  
17456 C C   . THR C 85  ? 0.9643 0.9709 0.8344 0.1694  -0.0694 -0.0029 85  THR C C   
17457 O O   . THR C 85  ? 0.9880 1.0204 0.8882 0.1607  -0.0585 0.0160  85  THR C O   
17458 C CB  . THR C 85  ? 1.0087 0.9680 0.7936 0.2087  -0.0639 -0.0192 85  THR C CB  
17459 O OG1 . THR C 85  ? 1.0183 0.9590 0.7454 0.2451  -0.0575 -0.0184 85  THR C OG1 
17460 C CG2 . THR C 85  ? 1.0565 0.9807 0.8376 0.1851  -0.0831 -0.0498 85  THR C CG2 
17468 N N   . TYR C 86  ? 0.9341 0.9295 0.8173 0.1529  -0.0862 -0.0237 86  TYR C N   
17469 C CA  . TYR C 86  ? 0.8868 0.8955 0.8162 0.1278  -0.0911 -0.0261 86  TYR C CA  
17470 C C   . TYR C 86  ? 0.8865 0.8842 0.8254 0.1079  -0.0989 -0.0522 86  TYR C C   
17471 O O   . TYR C 86  ? 0.8968 0.8822 0.8200 0.1067  -0.1109 -0.0733 86  TYR C O   
17472 C CB  . TYR C 86  ? 0.8524 0.8654 0.7913 0.1305  -0.1022 -0.0245 86  TYR C CB  
17473 C CG  . TYR C 86  ? 0.8779 0.8978 0.8073 0.1434  -0.0929 0.0057  86  TYR C CG  
17474 C CD1 . TYR C 86  ? 0.9030 0.9178 0.7912 0.1685  -0.0897 0.0143  86  TYR C CD1 
17475 C CD2 . TYR C 86  ? 0.8597 0.8893 0.8176 0.1284  -0.0874 0.0263  86  TYR C CD2 
17476 C CE1 . TYR C 86  ? 0.9308 0.9549 0.8085 0.1780  -0.0780 0.0450  86  TYR C CE1 
17477 C CE2 . TYR C 86  ? 0.8753 0.9112 0.8246 0.1337  -0.0780 0.0568  86  TYR C CE2 
17478 C CZ  . TYR C 86  ? 0.9215 0.9572 0.8318 0.1583  -0.0718 0.0673  86  TYR C CZ  
17479 O OH  . TYR C 86  ? 0.9579 1.0028 0.8581 0.1614  -0.0595 0.1004  86  TYR C OH  
17489 N N   . PHE C 87  ? 0.8643 0.8680 0.8276 0.0903  -0.0925 -0.0499 87  PHE C N   
17490 C CA  . PHE C 87  ? 0.8670 0.8625 0.8393 0.0686  -0.0959 -0.0702 87  PHE C CA  
17491 C C   . PHE C 87  ? 0.8757 0.8905 0.8875 0.0518  -0.0993 -0.0755 87  PHE C C   
17492 O O   . PHE C 87  ? 0.8972 0.9222 0.9269 0.0536  -0.0976 -0.0605 87  PHE C O   
17493 C CB  . PHE C 87  ? 0.8671 0.8478 0.8255 0.0652  -0.0858 -0.0644 87  PHE C CB  
17494 C CG  . PHE C 87  ? 0.8824 0.8364 0.7947 0.0865  -0.0824 -0.0620 87  PHE C CG  
17495 C CD1 . PHE C 87  ? 0.9121 0.8281 0.7898 0.0810  -0.0892 -0.0813 87  PHE C CD1 
17496 C CD2 . PHE C 87  ? 0.8933 0.8597 0.7948 0.1118  -0.0722 -0.0404 87  PHE C CD2 
17497 C CE1 . PHE C 87  ? 0.9553 0.8348 0.7811 0.1038  -0.0877 -0.0813 87  PHE C CE1 
17498 C CE2 . PHE C 87  ? 0.9427 0.8842 0.7970 0.1381  -0.0679 -0.0397 87  PHE C CE2 
17499 C CZ  . PHE C 87  ? 0.9772 0.8696 0.7899 0.1359  -0.0765 -0.0612 87  PHE C CZ  
17509 N N   . CYS C 88  ? 0.8662 0.8850 0.8892 0.0348  -0.1040 -0.0970 88  CYS C N   
17510 C CA  . CYS C 88  ? 0.8549 0.8929 0.9107 0.0220  -0.1048 -0.1057 88  CYS C CA  
17511 C C   . CYS C 88  ? 0.8920 0.9243 0.9478 0.0009  -0.0960 -0.1119 88  CYS C C   
17512 O O   . CYS C 88  ? 0.9319 0.9478 0.9665 -0.0091 -0.0937 -0.1184 88  CYS C O   
17513 C CB  . CYS C 88  ? 0.8345 0.8960 0.9078 0.0233  -0.1161 -0.1252 88  CYS C CB  
17514 S SG  . CYS C 88  ? 0.8615 0.9315 0.9305 0.0025  -0.1201 -0.1483 88  CYS C SG  
17519 N N   . GLN C 89  ? 0.8877 0.9272 0.9612 -0.0061 -0.0920 -0.1097 89  GLN C N   
17520 C CA  . GLN C 89  ? 0.8500 0.8813 0.9172 -0.0234 -0.0832 -0.1119 89  GLN C CA  
17521 C C   . GLN C 89  ? 0.7715 0.8209 0.8603 -0.0324 -0.0814 -0.1243 89  GLN C C   
17522 O O   . GLN C 89  ? 0.7593 0.8118 0.8610 -0.0236 -0.0862 -0.1212 89  GLN C O   
17523 C CB  . GLN C 89  ? 0.8742 0.8903 0.9284 -0.0187 -0.0796 -0.0918 89  GLN C CB  
17524 C CG  . GLN C 89  ? 0.8921 0.8963 0.9337 -0.0330 -0.0730 -0.0926 89  GLN C CG  
17525 C CD  . GLN C 89  ? 0.8266 0.8387 0.8826 -0.0377 -0.0748 -0.0892 89  GLN C CD  
17526 O OE1 . GLN C 89  ? 0.7548 0.7741 0.8254 -0.0306 -0.0812 -0.0787 89  GLN C OE1 
17527 N NE2 . GLN C 89  ? 0.7940 0.8011 0.8416 -0.0513 -0.0697 -0.0978 89  GLN C NE2 
17536 N N   . GLN C 90  ? 0.7521 0.8100 0.8402 -0.0502 -0.0739 -0.1378 90  GLN C N   
17537 C CA  . GLN C 90  ? 0.7462 0.8242 0.8492 -0.0568 -0.0680 -0.1501 90  GLN C CA  
17538 C C   . GLN C 90  ? 0.7452 0.8012 0.8292 -0.0643 -0.0619 -0.1415 90  GLN C C   
17539 O O   . GLN C 90  ? 0.7369 0.7691 0.7960 -0.0729 -0.0578 -0.1316 90  GLN C O   
17540 C CB  . GLN C 90  ? 0.7641 0.8719 0.8778 -0.0747 -0.0602 -0.1667 90  GLN C CB  
17541 C CG  . GLN C 90  ? 0.8040 0.8889 0.8903 -0.1000 -0.0503 -0.1627 90  GLN C CG  
17542 C CD  . GLN C 90  ? 0.8321 0.9148 0.9066 -0.1134 -0.0365 -0.1632 90  GLN C CD  
17543 O OE1 . GLN C 90  ? 0.8039 0.9098 0.8937 -0.1051 -0.0332 -0.1712 90  GLN C OE1 
17544 N NE2 . GLN C 90  ? 0.8915 0.9405 0.9319 -0.1318 -0.0290 -0.1549 90  GLN C NE2 
17553 N N   . GLY C 91  ? 0.7328 0.7926 0.8240 -0.0587 -0.0635 -0.1462 91  GLY C N   
17554 C CA  . GLY C 91  ? 0.7152 0.7559 0.7871 -0.0653 -0.0612 -0.1409 91  GLY C CA  
17555 C C   . GLY C 91  ? 0.7716 0.8255 0.8414 -0.0693 -0.0524 -0.1578 91  GLY C C   
17556 O O   . GLY C 91  ? 0.7962 0.8340 0.8493 -0.0698 -0.0541 -0.1579 91  GLY C O   
17560 N N   . ASN C 92  ? 0.7935 0.8813 0.8802 -0.0718 -0.0431 -0.1727 92  ASN C N   
17561 C CA  . ASN C 92  ? 0.7947 0.9070 0.8823 -0.0719 -0.0311 -0.1894 92  ASN C CA  
17562 C C   . ASN C 92  ? 0.8002 0.9070 0.8609 -0.0943 -0.0147 -0.1863 92  ASN C C   
17563 O O   . ASN C 92  ? 0.8066 0.9205 0.8536 -0.0934 -0.0046 -0.1954 92  ASN C O   
17564 C CB  . ASN C 92  ? 0.7727 0.9372 0.8943 -0.0655 -0.0265 -0.2054 92  ASN C CB  
17565 C CG  . ASN C 92  ? 0.8055 1.0057 0.9321 -0.0574 -0.0129 -0.2236 92  ASN C CG  
17566 O OD1 . ASN C 92  ? 0.8608 1.0383 0.9680 -0.0423 -0.0152 -0.2289 92  ASN C OD1 
17567 N ND2 . ASN C 92  ? 0.8072 1.0654 0.9588 -0.0678 0.0012  -0.2337 92  ASN C ND2 
17574 N N   . THR C 93  ? 0.7967 0.8853 0.8431 -0.1124 -0.0121 -0.1735 93  THR C N   
17575 C CA  . THR C 93  ? 0.8292 0.9046 0.8441 -0.1352 0.0034  -0.1684 93  THR C CA  
17576 C C   . THR C 93  ? 0.8263 0.8551 0.8120 -0.1429 -0.0026 -0.1503 93  THR C C   
17577 O O   . THR C 93  ? 0.7908 0.8123 0.7872 -0.1371 -0.0129 -0.1459 93  THR C O   
17578 C CB  . THR C 93  ? 0.8860 1.0055 0.9181 -0.1562 0.0208  -0.1790 93  THR C CB  
17579 O OG1 . THR C 93  ? 0.9830 1.0805 0.9781 -0.1832 0.0364  -0.1699 93  THR C OG1 
17580 C CG2 . THR C 93  ? 0.8554 0.9920 0.9156 -0.1621 0.0126  -0.1812 93  THR C CG2 
17588 N N   . PHE C 94  ? 0.8582 0.8534 0.8020 -0.1522 0.0036  -0.1402 94  PHE C N   
17589 C CA  . PHE C 94  ? 0.8887 0.8352 0.7969 -0.1550 -0.0013 -0.1236 94  PHE C CA  
17590 C C   . PHE C 94  ? 0.8908 0.8220 0.7818 -0.1821 0.0098  -0.1229 94  PHE C C   
17591 O O   . PHE C 94  ? 0.8997 0.8549 0.7941 -0.2053 0.0260  -0.1302 94  PHE C O   
17592 C CB  . PHE C 94  ? 0.9290 0.8424 0.7948 -0.1506 -0.0023 -0.1121 94  PHE C CB  
17593 C CG  . PHE C 94  ? 0.8669 0.7866 0.7447 -0.1281 -0.0188 -0.1092 94  PHE C CG  
17594 C CD1 . PHE C 94  ? 0.8320 0.7588 0.7364 -0.1116 -0.0332 -0.1035 94  PHE C CD1 
17595 C CD2 . PHE C 94  ? 0.8770 0.7951 0.7366 -0.1257 -0.0203 -0.1116 94  PHE C CD2 
17596 C CE1 . PHE C 94  ? 0.8247 0.7603 0.7424 -0.0979 -0.0482 -0.0986 94  PHE C CE1 
17597 C CE2 . PHE C 94  ? 0.8771 0.7992 0.7473 -0.1110 -0.0385 -0.1093 94  PHE C CE2 
17598 C CZ  . PHE C 94  ? 0.8435 0.7759 0.7452 -0.0994 -0.0523 -0.1020 94  PHE C CZ  
17608 N N   . PRO C 95  ? 0.9001 0.7907 0.7703 -0.1807 0.0014  -0.1143 95  PRO C N   
17609 C CA  . PRO C 95  ? 0.8973 0.7684 0.7647 -0.1513 -0.0144 -0.1048 95  PRO C CA  
17610 C C   . PRO C 95  ? 0.8521 0.7627 0.7670 -0.1362 -0.0239 -0.1129 95  PRO C C   
17611 O O   . PRO C 95  ? 0.8306 0.7689 0.7712 -0.1483 -0.0217 -0.1256 95  PRO C O   
17612 C CB  . PRO C 95  ? 0.9951 0.8063 0.8157 -0.1557 -0.0165 -0.0961 95  PRO C CB  
17613 C CG  . PRO C 95  ? 1.0172 0.8302 0.8387 -0.1909 -0.0073 -0.1062 95  PRO C CG  
17614 C CD  . PRO C 95  ? 0.9566 0.8152 0.8000 -0.2093 0.0076  -0.1132 95  PRO C CD  
17622 N N   . TYR C 96  ? 0.8527 0.7686 0.7790 -0.1109 -0.0346 -0.1046 96  TYR C N   
17623 C CA  . TYR C 96  ? 0.8111 0.7532 0.7718 -0.0959 -0.0434 -0.1075 96  TYR C CA  
17624 C C   . TYR C 96  ? 0.8609 0.7822 0.8069 -0.0950 -0.0462 -0.1083 96  TYR C C   
17625 O O   . TYR C 96  ? 0.9139 0.7924 0.8202 -0.0905 -0.0465 -0.0993 96  TYR C O   
17626 C CB  . TYR C 96  ? 0.7662 0.7147 0.7367 -0.0742 -0.0527 -0.0938 96  TYR C CB  
17627 C CG  . TYR C 96  ? 0.7815 0.7492 0.7697 -0.0756 -0.0557 -0.0962 96  TYR C CG  
17628 C CD1 . TYR C 96  ? 0.8024 0.7834 0.7978 -0.0880 -0.0490 -0.1119 96  TYR C CD1 
17629 C CD2 . TYR C 96  ? 0.7778 0.7514 0.7742 -0.0647 -0.0658 -0.0832 96  TYR C CD2 
17630 C CE1 . TYR C 96  ? 0.7766 0.7656 0.7788 -0.0861 -0.0532 -0.1166 96  TYR C CE1 
17631 C CE2 . TYR C 96  ? 0.7526 0.7346 0.7592 -0.0688 -0.0721 -0.0870 96  TYR C CE2 
17632 C CZ  . TYR C 96  ? 0.7576 0.7420 0.7632 -0.0778 -0.0663 -0.1047 96  TYR C CZ  
17633 O OH  . TYR C 96  ? 0.7623 0.7459 0.7690 -0.0788 -0.0738 -0.1111 96  TYR C OH  
17643 N N   . THR C 97  ? 0.8139 0.7619 0.7872 -0.0972 -0.0499 -0.1201 97  THR C N   
17644 C CA  . THR C 97  ? 0.8497 0.7790 0.8078 -0.0985 -0.0556 -0.1247 97  THR C CA  
17645 C C   . THR C 97  ? 0.8504 0.8035 0.8319 -0.0758 -0.0655 -0.1249 97  THR C C   
17646 O O   . THR C 97  ? 0.8219 0.8125 0.8392 -0.0695 -0.0677 -0.1284 97  THR C O   
17647 C CB  . THR C 97  ? 0.8580 0.7984 0.8222 -0.1302 -0.0523 -0.1403 97  THR C CB  
17648 O OG1 . THR C 97  ? 0.8216 0.8222 0.8345 -0.1322 -0.0516 -0.1525 97  THR C OG1 
17649 C CG2 . THR C 97  ? 0.9186 0.8300 0.8527 -0.1560 -0.0403 -0.1367 97  THR C CG2 
17657 N N   . PHE C 98  ? 0.8761 0.8012 0.8305 -0.0617 -0.0716 -0.1210 98  PHE C N   
17658 C CA  . PHE C 98  ? 0.8498 0.7911 0.8153 -0.0387 -0.0797 -0.1187 98  PHE C CA  
17659 C C   . PHE C 98  ? 0.9014 0.8416 0.8615 -0.0465 -0.0897 -0.1350 98  PHE C C   
17660 O O   . PHE C 98  ? 0.9936 0.9122 0.9354 -0.0705 -0.0909 -0.1459 98  PHE C O   
17661 C CB  . PHE C 98  ? 0.8484 0.7661 0.7849 -0.0110 -0.0784 -0.1015 98  PHE C CB  
17662 C CG  . PHE C 98  ? 0.7656 0.6947 0.7126 -0.0028 -0.0720 -0.0843 98  PHE C CG  
17663 C CD1 . PHE C 98  ? 0.7851 0.6912 0.7116 -0.0102 -0.0669 -0.0802 98  PHE C CD1 
17664 C CD2 . PHE C 98  ? 0.7247 0.6860 0.6995 0.0107  -0.0727 -0.0711 98  PHE C CD2 
17665 C CE1 . PHE C 98  ? 0.7697 0.6909 0.7066 -0.0026 -0.0647 -0.0653 98  PHE C CE1 
17666 C CE2 . PHE C 98  ? 0.7089 0.6846 0.6960 0.0133  -0.0698 -0.0557 98  PHE C CE2 
17667 C CZ  . PHE C 98  ? 0.7247 0.6834 0.6943 0.0076  -0.0668 -0.0537 98  PHE C CZ  
17677 N N   . GLY C 99  ? 0.8925 0.8548 0.8666 -0.0277 -0.0984 -0.1357 99  GLY C N   
17678 C CA  . GLY C 99  ? 0.8872 0.8454 0.8486 -0.0282 -0.1118 -0.1495 99  GLY C CA  
17679 C C   . GLY C 99  ? 0.9660 0.8759 0.8743 -0.0085 -0.1146 -0.1439 99  GLY C C   
17680 O O   . GLY C 99  ? 0.9885 0.8793 0.8769 0.0110  -0.1052 -0.1273 99  GLY C O   
17684 N N   . GLY C 100 ? 0.9620 0.8550 0.8466 -0.0123 -0.1290 -0.1590 100 GLY C N   
17685 C CA  . GLY C 100 ? 1.0253 0.8633 0.8492 0.0075  -0.1331 -0.1582 100 GLY C CA  
17686 C C   . GLY C 100 ? 1.0090 0.8547 0.8212 0.0485  -0.1279 -0.1415 100 GLY C C   
17687 O O   . GLY C 100 ? 1.0292 0.8375 0.7953 0.0732  -0.1222 -0.1335 100 GLY C O   
17691 N N   . GLY C 101 ? 0.9419 0.8348 0.7923 0.0574  -0.1291 -0.1351 101 GLY C N   
17692 C CA  . GLY C 101 ? 0.9650 0.8687 0.8063 0.0906  -0.1227 -0.1160 101 GLY C CA  
17693 C C   . GLY C 101 ? 1.0175 0.9253 0.8418 0.1063  -0.1373 -0.1233 101 GLY C C   
17694 O O   . GLY C 101 ? 1.0999 0.9850 0.8965 0.0999  -0.1534 -0.1439 101 GLY C O   
17698 N N   . THR C 102 ? 1.0704 0.8127 0.9968 -0.1303 -0.2294 0.0663  102 THR C N   
17699 C CA  . THR C 102 ? 1.0744 0.8675 1.0081 -0.1116 -0.2360 0.0534  102 THR C CA  
17700 C C   . THR C 102 ? 1.0870 0.8699 1.0027 -0.0553 -0.2278 0.0543  102 THR C C   
17701 O O   . THR C 102 ? 1.0215 0.8306 0.9636 -0.0306 -0.2053 0.0689  102 THR C O   
17702 C CB  . THR C 102 ? 0.9740 0.8661 0.9662 -0.1202 -0.2273 0.0601  102 THR C CB  
17703 O OG1 . THR C 102 ? 0.9965 0.9078 1.0090 -0.1759 -0.2356 0.0497  102 THR C OG1 
17704 C CG2 . THR C 102 ? 0.9609 0.8933 0.9450 -0.0878 -0.2354 0.0469  102 THR C CG2 
17712 N N   . LYS C 103 ? 1.1507 0.8985 1.0228 -0.0380 -0.2435 0.0353  103 LYS C N   
17713 C CA  . LYS C 103 ? 1.1778 0.9068 1.0249 0.0106  -0.2360 0.0293  103 LYS C CA  
17714 C C   . LYS C 103 ? 1.1461 0.9273 0.9985 0.0343  -0.2276 0.0269  103 LYS C C   
17715 O O   . LYS C 103 ? 1.1698 0.9617 1.0088 0.0252  -0.2468 0.0144  103 LYS C O   
17716 C CB  . LYS C 103 ? 1.3103 0.9564 1.0969 0.0169  -0.2591 0.0096  103 LYS C CB  
17717 C CG  . LYS C 103 ? 1.4207 0.9935 1.1779 -0.0132 -0.2725 0.0099  103 LYS C CG  
17718 C CD  . LYS C 103 ? 1.5290 1.0143 1.2162 -0.0188 -0.2978 -0.0105 103 LYS C CD  
17719 C CE  . LYS C 103 ? 1.6369 1.0631 1.2934 -0.0752 -0.3078 -0.0128 103 LYS C CE  
17720 N NZ  . LYS C 103 ? 1.6046 1.0162 1.2736 -0.0924 -0.2953 0.0057  103 LYS C NZ  
17734 N N   . VAL C 104 ? 1.1098 0.9192 0.9755 0.0647  -0.1981 0.0357  104 VAL C N   
17735 C CA  . VAL C 104 ? 1.0930 0.9329 0.9455 0.0902  -0.1837 0.0355  104 VAL C CA  
17736 C C   . VAL C 104 ? 1.1973 0.9961 1.0042 0.1247  -0.1749 0.0188  104 VAL C C   
17737 O O   . VAL C 104 ? 1.1854 0.9760 0.9980 0.1403  -0.1515 0.0148  104 VAL C O   
17738 C CB  . VAL C 104 ? 0.9514 0.8418 0.8385 0.0948  -0.1498 0.0556  104 VAL C CB  
17739 C CG1 . VAL C 104 ? 0.9540 0.8505 0.8033 0.1259  -0.1304 0.0547  104 VAL C CG1 
17740 C CG2 . VAL C 104 ? 0.8742 0.8103 0.8068 0.0614  -0.1604 0.0699  104 VAL C CG2 
17750 N N   . GLU C 105 ? 1.3087 1.0869 1.0726 0.1368  -0.1936 0.0049  105 GLU C N   
17751 C CA  . GLU C 105 ? 1.4322 1.1682 1.1479 0.1671  -0.1879 -0.0129 105 GLU C CA  
17752 C C   . GLU C 105 ? 1.4358 1.1761 1.1108 0.1934  -0.1717 -0.0134 105 GLU C C   
17753 O O   . GLU C 105 ? 1.4713 1.2390 1.1444 0.1918  -0.1832 -0.0064 105 GLU C O   
17754 C CB  . GLU C 105 ? 1.5868 1.2764 1.2720 0.1610  -0.2256 -0.0311 105 GLU C CB  
17755 C CG  . GLU C 105 ? 1.6642 1.3215 1.3624 0.1409  -0.2407 -0.0328 105 GLU C CG  
17756 C CD  . GLU C 105 ? 1.8389 1.4405 1.4966 0.1303  -0.2759 -0.0501 105 GLU C CD  
17757 O OE1 . GLU C 105 ? 1.9104 1.5130 1.5434 0.1336  -0.2910 -0.0609 105 GLU C OE1 
17758 O OE2 . GLU C 105 ? 1.9005 1.4521 1.5448 0.1206  -0.2886 -0.0541 105 GLU C OE2 
17765 N N   . MET C 106 ? 1.4294 1.1392 1.0663 0.2193  -0.1446 -0.0250 106 MET C N   
17766 C CA  . MET C 106 ? 1.4666 1.1575 1.0438 0.2457  -0.1247 -0.0267 106 MET C CA  
17767 C C   . MET C 106 ? 1.5203 1.1884 1.0525 0.2582  -0.1641 -0.0378 106 MET C C   
17768 O O   . MET C 106 ? 1.4887 1.1455 1.0289 0.2472  -0.1990 -0.0502 106 MET C O   
17769 C CB  . MET C 106 ? 1.4676 1.1256 1.0108 0.2636  -0.0826 -0.0425 106 MET C CB  
17770 C CG  . MET C 106 ? 1.4307 1.1096 0.9889 0.2598  -0.0286 -0.0349 106 MET C CG  
17771 S SD  . MET C 106 ? 1.4744 1.1396 0.9739 0.2735  -0.0046 -0.0146 106 MET C SD  
17772 C CE  . MET C 106 ? 1.6333 1.2186 1.0229 0.3051  0.0091  -0.0344 106 MET C CE  
17782 N N   . ARG C 107 ? 1.5868 1.2438 1.0649 0.2834  -0.1582 -0.0354 107 ARG C N   
17783 C CA  . ARG C 107 ? 1.6729 1.3090 1.0997 0.3046  -0.1936 -0.0503 107 ARG C CA  
17784 C C   . ARG C 107 ? 1.7093 1.2784 1.0583 0.3338  -0.1736 -0.0639 107 ARG C C   
17785 O O   . ARG C 107 ? 1.7123 1.2517 1.0302 0.3424  -0.1253 -0.0606 107 ARG C O   
17786 C CB  . ARG C 107 ? 1.7180 1.3790 1.1218 0.3235  -0.2068 -0.0447 107 ARG C CB  
17787 C CG  . ARG C 107 ? 1.6739 1.4014 1.1394 0.2997  -0.2514 -0.0510 107 ARG C CG  
17788 C CD  . ARG C 107 ? 1.7159 1.4621 1.1405 0.3325  -0.2826 -0.0656 107 ARG C CD  
17789 N NE  . ARG C 107 ? 1.7148 1.5396 1.2074 0.3054  -0.3204 -0.0792 107 ARG C NE  
17790 C CZ  . ARG C 107 ? 1.7188 1.6025 1.2540 0.2965  -0.3197 -0.0703 107 ARG C CZ  
17791 N NH1 . ARG C 107 ? 1.7198 1.5885 1.2335 0.3143  -0.2840 -0.0447 107 ARG C NH1 
17792 N NH2 . ARG C 107 ? 1.7056 1.6635 1.3041 0.2670  -0.3524 -0.0899 107 ARG C NH2 
17806 N N   . ARG C 108 ? 1.7211 1.2669 1.0381 0.3458  -0.2089 -0.0821 108 ARG C N   
17807 C CA  . ARG C 108 ? 1.7227 1.2041 0.9682 0.3709  -0.1946 -0.0972 108 ARG C CA  
17808 C C   . ARG C 108 ? 1.7539 1.2171 0.9490 0.3952  -0.2373 -0.1130 108 ARG C C   
17809 O O   . ARG C 108 ? 1.7401 1.2475 0.9733 0.3833  -0.2812 -0.1196 108 ARG C O   
17810 C CB  . ARG C 108 ? 1.6924 1.1623 0.9695 0.3542  -0.1892 -0.1094 108 ARG C CB  
17811 C CG  . ARG C 108 ? 1.7436 1.1630 0.9675 0.3715  -0.1463 -0.1231 108 ARG C CG  
17812 C CD  . ARG C 108 ? 1.7574 1.1682 1.0062 0.3643  -0.1562 -0.1432 108 ARG C CD  
17813 N NE  . ARG C 108 ? 1.8429 1.2039 1.0306 0.3841  -0.1278 -0.1647 108 ARG C NE  
17814 C CZ  . ARG C 108 ? 1.9212 1.2343 1.0403 0.4060  -0.1443 -0.1748 108 ARG C CZ  
17815 N NH1 . ARG C 108 ? 1.9403 1.2553 1.0465 0.4129  -0.1907 -0.1682 108 ARG C NH1 
17816 N NH2 . ARG C 108 ? 1.9924 1.2589 1.0562 0.4205  -0.1135 -0.1954 108 ARG C NH2 
17830 N N   . ALA C 109 ? 1.8000 1.1979 0.9069 0.4280  -0.2220 -0.1226 109 ALA C N   
17831 C CA  . ALA C 109 ? 1.8604 1.2347 0.9162 0.4539  -0.2625 -0.1416 109 ALA C CA  
17832 C C   . ALA C 109 ? 1.8730 1.2558 0.9728 0.4307  -0.2920 -0.1573 109 ALA C C   
17833 O O   . ALA C 109 ? 1.8555 1.2211 0.9755 0.4151  -0.2702 -0.1586 109 ALA C O   
17834 C CB  . ALA C 109 ? 1.9194 1.2088 0.8615 0.4936  -0.2347 -0.1474 109 ALA C CB  
17840 N N   . ASP C 110 ? 1.9001 1.3104 1.0129 0.4290  -0.3419 -0.1731 110 ASP C N   
17841 C CA  . ASP C 110 ? 1.9002 1.3095 1.0448 0.4042  -0.3700 -0.1887 110 ASP C CA  
17842 C C   . ASP C 110 ? 1.9357 1.2781 1.0274 0.4219  -0.3542 -0.1979 110 ASP C C   
17843 O O   . ASP C 110 ? 1.7003 0.9968 0.7159 0.4578  -0.3406 -0.2026 110 ASP C O   
17844 C CB  . ASP C 110 ? 1.9364 1.3792 1.0860 0.4032  -0.4208 -0.2121 110 ASP C CB  
17845 C CG  . ASP C 110 ? 1.8707 1.3892 1.0945 0.3681  -0.4390 -0.2123 110 ASP C CG  
17846 O OD1 . ASP C 110 ? 1.7859 1.3287 1.0462 0.3549  -0.4136 -0.1897 110 ASP C OD1 
17847 O OD2 . ASP C 110 ? 1.8496 1.4051 1.0964 0.3509  -0.4768 -0.2379 110 ASP C OD2 
17852 N N   . ALA C 111 ? 1.8568 1.1890 0.9830 0.3981  -0.3559 -0.2022 111 ALA C N   
17853 C CA  . ALA C 111 ? 1.7953 1.0735 0.8823 0.4128  -0.3435 -0.2155 111 ALA C CA  
17854 C C   . ALA C 111 ? 1.8160 1.0808 0.9184 0.3951  -0.3816 -0.2308 111 ALA C C   
17855 O O   . ALA C 111 ? 1.8032 1.0947 0.9521 0.3633  -0.4055 -0.2284 111 ALA C O   
17856 C CB  . ALA C 111 ? 1.7064 0.9800 0.8117 0.4096  -0.2971 -0.2101 111 ALA C CB  
17862 N N   . ALA C 112 ? 1.8709 1.0873 0.9268 0.4144  -0.3844 -0.2477 112 ALA C N   
17863 C CA  . ALA C 112 ? 1.8799 1.0711 0.9364 0.4012  -0.4196 -0.2633 112 ALA C CA  
17864 C C   . ALA C 112 ? 1.8813 1.0470 0.9514 0.3984  -0.4066 -0.2680 112 ALA C C   
17865 O O   . ALA C 112 ? 1.8895 1.0465 0.9472 0.4186  -0.3723 -0.2729 112 ALA C O   
17866 C CB  . ALA C 112 ? 1.9314 1.0855 0.9267 0.4262  -0.4388 -0.2823 112 ALA C CB  
17872 N N   . PRO C 113 ? 1.8798 1.0304 0.9696 0.3747  -0.4324 -0.2709 113 PRO C N   
17873 C CA  . PRO C 113 ? 1.8957 1.0178 0.9896 0.3813  -0.4261 -0.2790 113 PRO C CA  
17874 C C   . PRO C 113 ? 1.9346 1.0129 0.9815 0.4105  -0.4292 -0.3026 113 PRO C C   
17875 O O   . PRO C 113 ? 1.9622 1.0100 0.9709 0.4132  -0.4545 -0.3125 113 PRO C O   
17876 C CB  . PRO C 113 ? 1.9177 1.0142 1.0208 0.3495  -0.4569 -0.2759 113 PRO C CB  
17877 C CG  . PRO C 113 ? 1.9304 1.0316 1.0229 0.3267  -0.4826 -0.2782 113 PRO C CG  
17878 C CD  . PRO C 113 ? 1.8915 1.0455 0.9931 0.3408  -0.4670 -0.2714 113 PRO C CD  
17886 N N   . THR C 114 ? 1.3512 1.5246 0.8120 0.5035  -0.1620 -0.1461 114 THR C N   
17887 C CA  . THR C 114 ? 1.3718 1.5238 0.7976 0.5078  -0.1539 -0.1415 114 THR C CA  
17888 C C   . THR C 114 ? 1.3047 1.4908 0.8170 0.4436  -0.1619 -0.1694 114 THR C C   
17889 O O   . THR C 114 ? 1.2491 1.4184 0.8150 0.3883  -0.1406 -0.1534 114 THR C O   
17890 C CB  . THR C 114 ? 1.3958 1.4633 0.7687 0.5091  -0.1012 -0.0842 114 THR C CB  
17891 O OG1 . THR C 114 ? 1.4810 1.5070 0.7779 0.5664  -0.0832 -0.0541 114 THR C OG1 
17892 C CG2 . THR C 114 ? 1.4447 1.4884 0.7755 0.5214  -0.0914 -0.0807 114 THR C CG2 
17900 N N   . VAL C 115 ? 1.3276 1.5589 0.8509 0.4545  -0.1921 -0.2123 115 VAL C N   
17901 C CA  . VAL C 115 ? 1.2927 1.5597 0.9015 0.3994  -0.1991 -0.2450 115 VAL C CA  
17902 C C   . VAL C 115 ? 1.3074 1.5477 0.8904 0.3919  -0.1861 -0.2352 115 VAL C C   
17903 O O   . VAL C 115 ? 1.3295 1.5587 0.8393 0.4420  -0.1933 -0.2347 115 VAL C O   
17904 C CB  . VAL C 115 ? 1.3393 1.6876 1.0100 0.4096  -0.2418 -0.3131 115 VAL C CB  
17905 C CG1 . VAL C 115 ? 1.2969 1.6692 1.0673 0.3445  -0.2336 -0.3408 115 VAL C CG1 
17906 C CG2 . VAL C 115 ? 1.3443 1.7181 1.0248 0.4344  -0.2577 -0.3232 115 VAL C CG2 
17916 N N   . SER C 116 ? 1.3218 1.5491 0.9603 0.3332  -0.1666 -0.2280 116 SER C N   
17917 C CA  . SER C 116 ? 1.3397 1.5456 0.9686 0.3192  -0.1542 -0.2220 116 SER C CA  
17918 C C   . SER C 116 ? 1.2765 1.5046 0.9895 0.2626  -0.1528 -0.2456 116 SER C C   
17919 O O   . SER C 116 ? 1.2210 1.4414 0.9790 0.2256  -0.1406 -0.2366 116 SER C O   
17920 C CB  . SER C 116 ? 1.3365 1.4706 0.9212 0.3151  -0.1154 -0.1670 116 SER C CB  
17921 O OG  . SER C 116 ? 1.3375 1.4477 0.9463 0.2898  -0.0979 -0.1406 116 SER C OG  
17927 N N   . ILE C 117 ? 1.2792 1.5299 1.0083 0.2594  -0.1628 -0.2753 117 ILE C N   
17928 C CA  . ILE C 117 ? 1.2312 1.4972 1.0364 0.2103  -0.1558 -0.2981 117 ILE C CA  
17929 C C   . ILE C 117 ? 1.2248 1.4476 1.0121 0.1910  -0.1340 -0.2710 117 ILE C C   
17930 O O   . ILE C 117 ? 1.2780 1.4829 1.0079 0.2205  -0.1332 -0.2591 117 ILE C O   
17931 C CB  . ILE C 117 ? 1.2486 1.5814 1.1090 0.2174  -0.1830 -0.3637 117 ILE C CB  
17932 C CG1 . ILE C 117 ? 1.2086 1.5488 1.1574 0.1638  -0.1640 -0.3845 117 ILE C CG1 
17933 C CG2 . ILE C 117 ? 1.2828 1.6267 1.0976 0.2529  -0.2003 -0.3818 117 ILE C CG2 
17934 C CD1 . ILE C 117 ? 1.2770 1.6841 1.3088 0.1624  -0.1823 -0.4553 117 ILE C CD1 
17946 N N   . PHE C 118 ? 1.1623 1.3650 0.9954 0.1452  -0.1146 -0.2614 118 PHE C N   
17947 C CA  . PHE C 118 ? 1.1079 1.2711 0.9331 0.1257  -0.0957 -0.2377 118 PHE C CA  
17948 C C   . PHE C 118 ? 1.0535 1.2283 0.9381 0.0910  -0.0889 -0.2628 118 PHE C C   
17949 O O   . PHE C 118 ? 1.0483 1.2259 0.9767 0.0666  -0.0805 -0.2715 118 PHE C O   
17950 C CB  . PHE C 118 ? 1.0397 1.1524 0.8503 0.1117  -0.0768 -0.1932 118 PHE C CB  
17951 C CG  . PHE C 118 ? 1.0942 1.1860 0.8536 0.1429  -0.0730 -0.1661 118 PHE C CG  
17952 C CD1 . PHE C 118 ? 1.1273 1.2305 0.8780 0.1576  -0.0805 -0.1645 118 PHE C CD1 
17953 C CD2 . PHE C 118 ? 1.1429 1.1991 0.8652 0.1584  -0.0563 -0.1422 118 PHE C CD2 
17954 C CE1 . PHE C 118 ? 1.1735 1.2515 0.8763 0.1882  -0.0713 -0.1381 118 PHE C CE1 
17955 C CE2 . PHE C 118 ? 1.1926 1.2201 0.8695 0.1884  -0.0423 -0.1160 118 PHE C CE2 
17956 C CZ  . PHE C 118 ? 1.2089 1.2465 0.8743 0.2039  -0.0499 -0.1132 118 PHE C CZ  
17966 N N   . PRO C 119 ? 1.0577 1.2335 0.9436 0.0890  -0.0870 -0.2739 119 PRO C N   
17967 C CA  . PRO C 119 ? 1.0599 1.2388 1.0018 0.0561  -0.0742 -0.2945 119 PRO C CA  
17968 C C   . PRO C 119 ? 1.0710 1.1967 1.0117 0.0298  -0.0519 -0.2573 119 PRO C C   
17969 O O   . PRO C 119 ? 1.0965 1.1890 1.0002 0.0365  -0.0497 -0.2212 119 PRO C O   
17970 C CB  . PRO C 119 ? 1.0863 1.2831 1.0205 0.0692  -0.0821 -0.3173 119 PRO C CB  
17971 C CG  . PRO C 119 ? 1.1198 1.2916 0.9810 0.1006  -0.0853 -0.2857 119 PRO C CG  
17972 C CD  . PRO C 119 ? 1.1006 1.2708 0.9333 0.1200  -0.0925 -0.2684 119 PRO C CD  
17980 N N   . PRO C 120 ? 1.0268 1.1415 1.0089 0.0028  -0.0343 -0.2675 120 PRO C N   
17981 C CA  . PRO C 120 ? 1.0255 1.0875 0.9977 -0.0137 -0.0172 -0.2345 120 PRO C CA  
17982 C C   . PRO C 120 ? 0.9979 1.0363 0.9447 -0.0091 -0.0188 -0.2128 120 PRO C C   
17983 O O   . PRO C 120 ? 1.0473 1.1016 0.9972 -0.0049 -0.0206 -0.2273 120 PRO C O   
17984 C CB  . PRO C 120 ? 1.0711 1.1252 1.0887 -0.0364 0.0067  -0.2542 120 PRO C CB  
17985 C CG  . PRO C 120 ? 1.0777 1.1821 1.1361 -0.0356 0.0009  -0.2990 120 PRO C CG  
17986 C CD  . PRO C 120 ? 1.0437 1.1911 1.0853 -0.0104 -0.0271 -0.3124 120 PRO C CD  
17994 N N   . SER C 121 ? 0.9729 0.9740 0.8993 -0.0089 -0.0179 -0.1817 121 SER C N   
17995 C CA  . SER C 121 ? 1.0103 0.9885 0.9278 -0.0061 -0.0168 -0.1646 121 SER C CA  
17996 C C   . SER C 121 ? 1.0063 0.9718 0.9450 -0.0206 -0.0060 -0.1721 121 SER C C   
17997 O O   . SER C 121 ? 0.9703 0.9272 0.9248 -0.0330 0.0048  -0.1805 121 SER C O   
17998 C CB  . SER C 121 ? 1.0280 0.9743 0.9363 -0.0032 -0.0209 -0.1401 121 SER C CB  
17999 O OG  . SER C 121 ? 1.0664 0.9867 0.9775 -0.0117 -0.0193 -0.1362 121 SER C OG  
18005 N N   . SER C 122 ? 1.0553 1.0145 0.9943 -0.0179 -0.0036 -0.1679 122 SER C N   
18006 C CA  . SER C 122 ? 1.1028 1.0462 1.0619 -0.0304 0.0067  -0.1720 122 SER C CA  
18007 C C   . SER C 122 ? 1.0919 0.9969 1.0519 -0.0340 0.0070  -0.1556 122 SER C C   
18008 O O   . SER C 122 ? 1.0881 0.9747 1.0571 -0.0421 0.0188  -0.1592 122 SER C O   
18009 C CB  . SER C 122 ? 1.1571 1.0982 1.1166 -0.0252 0.0106  -0.1693 122 SER C CB  
18010 O OG  . SER C 122 ? 1.2257 1.1968 1.1710 -0.0145 0.0099  -0.1866 122 SER C OG  
18016 N N   . GLU C 123 ? 1.1116 1.0021 1.0608 -0.0244 -0.0054 -0.1395 123 GLU C N   
18017 C CA  . GLU C 123 ? 1.1519 1.0080 1.0935 -0.0192 -0.0126 -0.1291 123 GLU C CA  
18018 C C   . GLU C 123 ? 1.1584 0.9985 1.0814 -0.0216 -0.0013 -0.1304 123 GLU C C   
18019 O O   . GLU C 123 ? 1.1932 0.9973 1.1039 -0.0172 0.0062  -0.1251 123 GLU C O   
18020 C CB  . GLU C 123 ? 1.1671 1.0186 1.1054 -0.0076 -0.0300 -0.1203 123 GLU C CB  
18021 C CG  . GLU C 123 ? 1.1881 1.0420 1.1570 -0.0044 -0.0335 -0.1196 123 GLU C CG  
18022 C CD  . GLU C 123 ? 1.1858 1.0612 1.1557 -0.0057 -0.0194 -0.1190 123 GLU C CD  
18023 O OE1 . GLU C 123 ? 1.1880 1.0834 1.1373 -0.0078 -0.0135 -0.1243 123 GLU C OE1 
18024 O OE2 . GLU C 123 ? 1.1874 1.0574 1.1794 -0.0012 -0.0127 -0.1153 123 GLU C OE2 
18031 N N   . GLN C 124 ? 1.1494 1.0116 1.0698 -0.0258 0.0036  -0.1375 124 GLN C N   
18032 C CA  . GLN C 124 ? 1.1808 1.0244 1.0913 -0.0290 0.0217  -0.1398 124 GLN C CA  
18033 C C   . GLN C 124 ? 1.1858 1.0250 1.1212 -0.0427 0.0496  -0.1547 124 GLN C C   
18034 O O   . GLN C 124 ? 1.2064 1.0029 1.1296 -0.0417 0.0741  -0.1488 124 GLN C O   
18035 C CB  . GLN C 124 ? 1.1486 1.0226 1.0623 -0.0304 0.0191  -0.1481 124 GLN C CB  
18036 C CG  . GLN C 124 ? 1.1409 0.9951 1.0524 -0.0346 0.0429  -0.1520 124 GLN C CG  
18037 C CD  . GLN C 124 ? 1.1005 0.9856 1.0183 -0.0339 0.0367  -0.1602 124 GLN C CD  
18038 O OE1 . GLN C 124 ? 1.0754 1.0079 1.0113 -0.0332 0.0213  -0.1742 124 GLN C OE1 
18039 N NE2 . GLN C 124 ? 1.1143 0.9691 1.0112 -0.0297 0.0490  -0.1509 124 GLN C NE2 
18048 N N   . LEU C 125 ? 1.1807 1.0591 1.1491 -0.0529 0.0493  -0.1750 125 LEU C N   
18049 C CA  . LEU C 125 ? 1.1967 1.0776 1.2014 -0.0679 0.0762  -0.1968 125 LEU C CA  
18050 C C   . LEU C 125 ? 1.2583 1.0918 1.2538 -0.0671 0.0920  -0.1823 125 LEU C C   
18051 O O   . LEU C 125 ? 1.3292 1.1409 1.3459 -0.0770 0.1255  -0.1919 125 LEU C O   
18052 C CB  . LEU C 125 ? 1.1731 1.1088 1.2096 -0.0732 0.0657  -0.2260 125 LEU C CB  
18053 C CG  . LEU C 125 ? 1.2073 1.1919 1.2597 -0.0702 0.0539  -0.2508 125 LEU C CG  
18054 C CD1 . LEU C 125 ? 1.2239 1.2560 1.2796 -0.0603 0.0327  -0.2731 125 LEU C CD1 
18055 C CD2 . LEU C 125 ? 1.2389 1.2309 1.3421 -0.0854 0.0812  -0.2803 125 LEU C CD2 
18067 N N   . THR C 126 ? 1.2471 1.0631 1.2170 -0.0543 0.0708  -0.1617 126 THR C N   
18068 C CA  . THR C 126 ? 1.2939 1.0629 1.2504 -0.0468 0.0811  -0.1481 126 THR C CA  
18069 C C   . THR C 126 ? 1.3613 1.0734 1.2730 -0.0295 0.0938  -0.1295 126 THR C C   
18070 O O   . THR C 126 ? 1.4366 1.0995 1.3301 -0.0203 0.1160  -0.1199 126 THR C O   
18071 C CB  . THR C 126 ? 1.2964 1.0669 1.2500 -0.0361 0.0529  -0.1383 126 THR C CB  
18072 O OG1 . THR C 126 ? 1.2893 1.0502 1.2165 -0.0185 0.0272  -0.1253 126 THR C OG1 
18073 C CG2 . THR C 126 ? 1.2820 1.0989 1.2661 -0.0475 0.0449  -0.1519 126 THR C CG2 
18081 N N   . SER C 127 ? 1.3657 1.0785 1.2525 -0.0211 0.0819  -0.1230 127 SER C N   
18082 C CA  . SER C 127 ? 1.4036 1.0591 1.2389 -0.0015 0.0972  -0.1062 127 SER C CA  
18083 C C   . SER C 127 ? 1.4153 1.0472 1.2632 -0.0141 0.1484  -0.1130 127 SER C C   
18084 O O   . SER C 127 ? 1.5159 1.0854 1.3158 0.0041  0.1751  -0.0964 127 SER C O   
18085 C CB  . SER C 127 ? 1.4351 1.1010 1.2448 0.0098  0.0703  -0.1001 127 SER C CB  
18086 O OG  . SER C 127 ? 1.4772 1.1642 1.2890 0.0199  0.0286  -0.0984 127 SER C OG  
18092 N N   . GLY C 128 ? 1.3853 1.0628 1.2977 -0.0420 0.1646  -0.1396 128 GLY C N   
18093 C CA  . GLY C 128 ? 1.4398 1.1125 1.3884 -0.0580 0.2092  -0.1573 128 GLY C CA  
18094 C C   . GLY C 128 ? 1.4647 1.1683 1.4152 -0.0593 0.1948  -0.1633 128 GLY C C   
18095 O O   . GLY C 128 ? 1.4954 1.1899 1.3952 -0.0410 0.1647  -0.1425 128 GLY C O   
18099 N N   . GLY C 129 ? 1.4109 1.1537 1.4251 -0.0796 0.2141  -0.1955 129 GLY C N   
18100 C CA  . GLY C 129 ? 1.3619 1.1391 1.3840 -0.0799 0.1992  -0.2043 129 GLY C CA  
18101 C C   . GLY C 129 ? 1.2193 1.0679 1.2523 -0.0789 0.1479  -0.2167 129 GLY C C   
18102 O O   . GLY C 129 ? 1.1780 1.0352 1.1887 -0.0720 0.1197  -0.2052 129 GLY C O   
18106 N N   . ALA C 130 ? 1.1536 1.0505 1.2210 -0.0830 0.1390  -0.2409 130 ALA C N   
18107 C CA  . ALA C 130 ? 1.0612 1.0228 1.1358 -0.0762 0.0964  -0.2559 130 ALA C CA  
18108 C C   . ALA C 130 ? 1.0501 1.0365 1.1250 -0.0692 0.0842  -0.2608 130 ALA C C   
18109 O O   . ALA C 130 ? 1.0876 1.0919 1.2147 -0.0788 0.1044  -0.2898 130 ALA C O   
18110 C CB  . ALA C 130 ? 1.0062 1.0200 1.1427 -0.0857 0.0950  -0.3003 130 ALA C CB  
18116 N N   . SER C 131 ? 1.0208 1.0080 1.0457 -0.0530 0.0544  -0.2351 131 SER C N   
18117 C CA  . SER C 131 ? 1.0116 1.0208 1.0311 -0.0438 0.0410  -0.2362 131 SER C CA  
18118 C C   . SER C 131 ? 1.0366 1.1040 1.0610 -0.0287 0.0086  -0.2544 131 SER C C   
18119 O O   . SER C 131 ? 1.0509 1.1188 1.0435 -0.0177 -0.0089 -0.2400 131 SER C O   
18120 C CB  . SER C 131 ? 0.9959 0.9629 0.9577 -0.0331 0.0333  -0.1975 131 SER C CB  
18121 O OG  . SER C 131 ? 1.0346 0.9474 0.9808 -0.0376 0.0620  -0.1842 131 SER C OG  
18127 N N   . VAL C 132 ? 1.0302 1.1431 1.0932 -0.0248 0.0026  -0.2870 132 VAL C N   
18128 C CA  . VAL C 132 ? 1.0363 1.2004 1.0904 0.0002  -0.0306 -0.3041 132 VAL C CA  
18129 C C   . VAL C 132 ? 1.0578 1.2180 1.0829 0.0137  -0.0397 -0.2842 132 VAL C C   
18130 O O   . VAL C 132 ? 1.0938 1.2545 1.1494 0.0042  -0.0262 -0.2938 132 VAL C O   
18131 C CB  . VAL C 132 ? 1.0495 1.2751 1.1715 0.0021  -0.0388 -0.3632 132 VAL C CB  
18132 C CG1 . VAL C 132 ? 1.0642 1.3374 1.1578 0.0392  -0.0783 -0.3803 132 VAL C CG1 
18133 C CG2 . VAL C 132 ? 1.0312 1.2554 1.1957 -0.0178 -0.0210 -0.3859 132 VAL C CG2 
18143 N N   . VAL C 133 ? 1.0311 1.1833 1.0004 0.0355  -0.0573 -0.2567 133 VAL C N   
18144 C CA  . VAL C 133 ? 1.0329 1.1736 0.9717 0.0482  -0.0625 -0.2330 133 VAL C CA  
18145 C C   . VAL C 133 ? 1.0315 1.2128 0.9525 0.0823  -0.0865 -0.2472 133 VAL C C   
18146 O O   . VAL C 133 ? 1.0031 1.1978 0.8992 0.1036  -0.0991 -0.2532 133 VAL C O   
18147 C CB  . VAL C 133 ? 1.0325 1.1231 0.9272 0.0472  -0.0568 -0.1900 133 VAL C CB  
18148 C CG1 . VAL C 133 ? 1.0456 1.1260 0.9156 0.0603  -0.0605 -0.1696 133 VAL C CG1 
18149 C CG2 . VAL C 133 ? 1.0049 1.0550 0.9081 0.0228  -0.0393 -0.1789 133 VAL C CG2 
18159 N N   . CYS C 134 ? 1.0446 1.2415 0.9725 0.0917  -0.0919 -0.2519 134 CYS C N   
18160 C CA  . CYS C 134 ? 1.0313 1.2624 0.9356 0.1307  -0.1155 -0.2633 134 CYS C CA  
18161 C C   . CYS C 134 ? 1.0008 1.2043 0.8706 0.1403  -0.1100 -0.2289 134 CYS C C   
18162 O O   . CYS C 134 ? 0.9519 1.1414 0.8456 0.1183  -0.0970 -0.2225 134 CYS C O   
18163 C CB  . CYS C 134 ? 1.0457 1.3385 1.0111 0.1369  -0.1322 -0.3182 134 CYS C CB  
18164 S SG  . CYS C 134 ? 1.1111 1.4547 1.0416 0.1979  -0.1728 -0.3451 134 CYS C SG  
18169 N N   . PHE C 135 ? 1.0492 1.2402 0.8612 0.1748  -0.1158 -0.2067 135 PHE C N   
18170 C CA  . PHE C 135 ? 1.1030 1.2641 0.8832 0.1863  -0.1063 -0.1737 135 PHE C CA  
18171 C C   . PHE C 135 ? 1.1748 1.3661 0.9303 0.2306  -0.1249 -0.1859 135 PHE C C   
18172 O O   . PHE C 135 ? 1.2151 1.4171 0.9274 0.2705  -0.1380 -0.1927 135 PHE C O   
18173 C CB  . PHE C 135 ? 1.1157 1.2252 0.8534 0.1911  -0.0867 -0.1344 135 PHE C CB  
18174 C CG  . PHE C 135 ? 1.0814 1.1579 0.8440 0.1522  -0.0714 -0.1202 135 PHE C CG  
18175 C CD1 . PHE C 135 ? 1.0648 1.1333 0.8573 0.1244  -0.0679 -0.1204 135 PHE C CD1 
18176 C CD2 . PHE C 135 ? 1.0650 1.1158 0.8170 0.1483  -0.0607 -0.1074 135 PHE C CD2 
18177 C CE1 . PHE C 135 ? 1.0702 1.1065 0.8747 0.0985  -0.0588 -0.1095 135 PHE C CE1 
18178 C CE2 . PHE C 135 ? 1.0243 1.0481 0.8004 0.1183  -0.0519 -0.0985 135 PHE C CE2 
18179 C CZ  . PHE C 135 ? 1.0263 1.0431 0.8254 0.0959  -0.0533 -0.1000 135 PHE C CZ  
18189 N N   . LEU C 136 ? 1.1726 1.3743 0.9495 0.2278  -0.1260 -0.1887 136 LEU C N   
18190 C CA  . LEU C 136 ? 1.1930 1.4150 0.9435 0.2713  -0.1412 -0.1934 136 LEU C CA  
18191 C C   . LEU C 136 ? 1.1737 1.3457 0.8895 0.2745  -0.1177 -0.1487 136 LEU C C   
18192 O O   . LEU C 136 ? 1.1907 1.3470 0.9382 0.2410  -0.1041 -0.1392 136 LEU C O   
18193 C CB  . LEU C 136 ? 1.2091 1.4853 1.0239 0.2654  -0.1589 -0.2363 136 LEU C CB  
18194 C CG  . LEU C 136 ? 1.2614 1.5956 1.1374 0.2597  -0.1801 -0.2928 136 LEU C CG  
18195 C CD1 . LEU C 136 ? 1.2588 1.6380 1.2134 0.2481  -0.1865 -0.3335 136 LEU C CD1 
18196 C CD2 . LEU C 136 ? 1.4058 1.7681 1.2376 0.3132  -0.2103 -0.3115 136 LEU C CD2 
18208 N N   . ASN C 137 ? 1.1838 1.3267 0.8338 0.3165  -0.1095 -0.1225 137 ASN C N   
18209 C CA  . ASN C 137 ? 1.1703 1.2590 0.7959 0.3169  -0.0787 -0.0808 137 ASN C CA  
18210 C C   . ASN C 137 ? 1.2268 1.3090 0.8031 0.3689  -0.0780 -0.0686 137 ASN C C   
18211 O O   . ASN C 137 ? 1.2736 1.3748 0.8029 0.4194  -0.0970 -0.0812 137 ASN C O   
18212 C CB  . ASN C 137 ? 1.1600 1.1969 0.7597 0.3126  -0.0498 -0.0516 137 ASN C CB  
18213 C CG  . ASN C 137 ? 1.0951 1.1345 0.7400 0.2654  -0.0509 -0.0616 137 ASN C CG  
18214 O OD1 . ASN C 137 ? 1.0287 1.0824 0.7209 0.2286  -0.0581 -0.0742 137 ASN C OD1 
18215 N ND2 . ASN C 137 ? 1.1215 1.1423 0.7467 0.2698  -0.0413 -0.0551 137 ASN C ND2 
18222 N N   . ASN C 138 ? 1.2167 1.2698 0.8015 0.3592  -0.0564 -0.0451 138 ASN C N   
18223 C CA  . ASN C 138 ? 1.2784 1.3107 0.8176 0.4046  -0.0450 -0.0250 138 ASN C CA  
18224 C C   . ASN C 138 ? 1.3216 1.4082 0.8476 0.4466  -0.0831 -0.0559 138 ASN C C   
18225 O O   . ASN C 138 ? 1.4117 1.4995 0.8731 0.5042  -0.0949 -0.0580 138 ASN C O   
18226 C CB  . ASN C 138 ? 1.3240 1.2945 0.7946 0.4422  -0.0094 0.0112  138 ASN C CB  
18227 C CG  . ASN C 138 ? 1.3351 1.2583 0.8366 0.4003  0.0274  0.0329  138 ASN C CG  
18228 O OD1 . ASN C 138 ? 1.3104 1.2403 0.8311 0.3748  0.0219  0.0229  138 ASN C OD1 
18229 N ND2 . ASN C 138 ? 1.3966 1.2745 0.9106 0.3934  0.0641  0.0586  138 ASN C ND2 
18236 N N   . PHE C 139 ? 1.2882 1.4181 0.8756 0.4209  -0.1020 -0.0825 139 PHE C N   
18237 C CA  . PHE C 139 ? 1.3278 1.5155 0.9268 0.4552  -0.1380 -0.1191 139 PHE C CA  
18238 C C   . PHE C 139 ? 1.3180 1.5097 0.9560 0.4393  -0.1307 -0.1166 139 PHE C C   
18239 O O   . PHE C 139 ? 1.3275 1.4997 1.0077 0.3873  -0.1096 -0.1059 139 PHE C O   
18240 C CB  . PHE C 139 ? 1.2639 1.5163 0.9244 0.4354  -0.1711 -0.1724 139 PHE C CB  
18241 C CG  . PHE C 139 ? 1.1114 1.3680 0.8492 0.3666  -0.1572 -0.1817 139 PHE C CG  
18242 C CD1 . PHE C 139 ? 1.0513 1.2808 0.7948 0.3279  -0.1408 -0.1694 139 PHE C CD1 
18243 C CD2 . PHE C 139 ? 1.0384 1.3205 0.8378 0.3449  -0.1581 -0.2016 139 PHE C CD2 
18244 C CE1 . PHE C 139 ? 0.9620 1.1869 0.7618 0.2737  -0.1270 -0.1756 139 PHE C CE1 
18245 C CE2 . PHE C 139 ? 0.9550 1.2287 0.8105 0.2888  -0.1393 -0.2065 139 PHE C CE2 
18246 C CZ  . PHE C 139 ? 0.9351 1.1786 0.7860 0.2557  -0.1245 -0.1928 139 PHE C CZ  
18256 N N   . TYR C 140 ? 0.7719 1.2871 1.4220 0.2980  -0.3203 -0.1825 140 TYR C N   
18257 C CA  . TYR C 140 ? 0.7661 1.2484 1.4653 0.3198  -0.2825 -0.1801 140 TYR C CA  
18258 C C   . TYR C 140 ? 0.7871 1.3416 1.6029 0.3216  -0.2731 -0.1844 140 TYR C C   
18259 O O   . TYR C 140 ? 0.7572 1.3742 1.5957 0.3031  -0.3011 -0.1675 140 TYR C O   
18260 C CB  . TYR C 140 ? 0.7670 1.2333 1.4664 0.3412  -0.3025 -0.1523 140 TYR C CB  
18261 C CG  . TYR C 140 ? 0.8210 1.2330 1.5507 0.3661  -0.2590 -0.1513 140 TYR C CG  
18262 C CD1 . TYR C 140 ? 0.8033 1.2669 1.6428 0.3832  -0.2459 -0.1431 140 TYR C CD1 
18263 C CD2 . TYR C 140 ? 0.8802 1.1898 1.5272 0.3732  -0.2309 -0.1583 140 TYR C CD2 
18264 C CE1 . TYR C 140 ? 0.8744 1.2873 1.7403 0.4099  -0.2025 -0.1415 140 TYR C CE1 
18265 C CE2 . TYR C 140 ? 0.9460 1.2013 1.6134 0.3986  -0.1895 -0.1610 140 TYR C CE2 
18266 C CZ  . TYR C 140 ? 0.9546 1.2611 1.7317 0.4184  -0.1737 -0.1523 140 TYR C CZ  
18267 O OH  . TYR C 140 ? 1.0372 1.2890 1.8341 0.4476  -0.1290 -0.1541 140 TYR C OH  
18277 N N   . PRO C 141 ? 0.8695 1.3961 1.7250 0.3300  -0.2206 -0.1952 141 PRO C N   
18278 C CA  . PRO C 141 ? 0.9585 1.3940 1.7608 0.3395  -0.1647 -0.2072 141 PRO C CA  
18279 C C   . PRO C 141 ? 1.0068 1.4084 1.7500 0.3177  -0.1403 -0.2301 141 PRO C C   
18280 O O   . PRO C 141 ? 0.9931 1.4339 1.7295 0.2943  -0.1673 -0.2388 141 PRO C O   
18281 C CB  . PRO C 141 ? 0.9969 1.4526 1.8997 0.3604  -0.1245 -0.2026 141 PRO C CB  
18282 C CG  . PRO C 141 ? 0.9402 1.4878 1.9411 0.3653  -0.1640 -0.1819 141 PRO C CG  
18283 C CD  . PRO C 141 ? 0.8419 1.4440 1.8222 0.3377  -0.2173 -0.1869 141 PRO C CD  
18291 N N   . LYS C 142 ? 1.0990 1.4278 1.8004 0.3273  -0.0876 -0.2392 142 LYS C N   
18292 C CA  . LYS C 142 ? 1.1311 1.4203 1.7676 0.3094  -0.0613 -0.2558 142 LYS C CA  
18293 C C   . LYS C 142 ? 1.1277 1.4694 1.8410 0.2934  -0.0445 -0.2670 142 LYS C C   
18294 O O   . LYS C 142 ? 1.0784 1.4110 1.7527 0.2720  -0.0411 -0.2790 142 LYS C O   
18295 C CB  . LYS C 142 ? 1.2631 1.4649 1.8339 0.3260  -0.0098 -0.2606 142 LYS C CB  
18296 C CG  . LYS C 142 ? 1.2990 1.4717 1.8329 0.3131  0.0324  -0.2739 142 LYS C CG  
18297 C CD  . LYS C 142 ? 1.3639 1.4467 1.7835 0.3198  0.0598  -0.2776 142 LYS C CD  
18298 C CE  . LYS C 142 ? 1.3569 1.4221 1.7024 0.2948  0.0587  -0.2822 142 LYS C CE  
18299 N NZ  . LYS C 142 ? 1.4344 1.4189 1.6713 0.2990  0.0864  -0.2841 142 LYS C NZ  
18313 N N   . ASP C 143 ? 1.0721 1.4681 1.8968 0.3028  -0.0338 -0.2614 143 ASP C N   
18314 C CA  . ASP C 143 ? 1.0634 1.5081 1.9691 0.2857  -0.0180 -0.2701 143 ASP C CA  
18315 C C   . ASP C 143 ? 1.0184 1.5112 1.9245 0.2554  -0.0676 -0.2817 143 ASP C C   
18316 O O   . ASP C 143 ? 0.9959 1.5387 1.9192 0.2529  -0.1188 -0.2760 143 ASP C O   
18317 C CB  . ASP C 143 ? 1.1126 1.6178 2.1449 0.3002  -0.0066 -0.2564 143 ASP C CB  
18318 C CG  . ASP C 143 ? 1.1783 1.6382 2.2103 0.3363  0.0385  -0.2437 143 ASP C CG  
18319 O OD1 . ASP C 143 ? 1.2124 1.6211 2.2164 0.3459  0.0933  -0.2485 143 ASP C OD1 
18320 O OD2 . ASP C 143 ? 1.1866 1.6614 2.2446 0.3564  0.0198  -0.2286 143 ASP C OD2 
18325 N N   . ILE C 144 ? 1.0023 1.4804 1.8893 0.2339  -0.0511 -0.2976 144 ILE C N   
18326 C CA  . ILE C 144 ? 0.9726 1.4846 1.8504 0.2064  -0.0927 -0.3131 144 ILE C CA  
18327 C C   . ILE C 144 ? 0.9860 1.4917 1.8945 0.1858  -0.0612 -0.3283 144 ILE C C   
18328 O O   . ILE C 144 ? 1.0343 1.4942 1.9315 0.1929  -0.0076 -0.3247 144 ILE C O   
18329 C CB  . ILE C 144 ? 1.0128 1.4847 1.7699 0.2044  -0.1202 -0.3133 144 ILE C CB  
18330 C CG1 . ILE C 144 ? 1.0728 1.5852 1.8221 0.1813  -0.1645 -0.3289 144 ILE C CG1 
18331 C CG2 . ILE C 144 ? 1.0352 1.4266 1.7040 0.2059  -0.0762 -0.3142 144 ILE C CG2 
18332 C CD1 . ILE C 144 ? 1.1227 1.6167 1.7726 0.1837  -0.1984 -0.3222 144 ILE C CD1 
18344 N N   . ASN C 145 ? 0.9995 1.5509 1.9458 0.1604  -0.0948 -0.3453 145 ASN C N   
18345 C CA  . ASN C 145 ? 1.0393 1.5823 2.0145 0.1373  -0.0716 -0.3614 145 ASN C CA  
18346 C C   . ASN C 145 ? 1.0736 1.6236 2.0031 0.1149  -0.1135 -0.3837 145 ASN C C   
18347 O O   . ASN C 145 ? 1.0742 1.6712 2.0052 0.1114  -0.1668 -0.3896 145 ASN C O   
18348 C CB  . ASN C 145 ? 1.0328 1.6320 2.1444 0.1275  -0.0612 -0.3606 145 ASN C CB  
18349 C CG  . ASN C 145 ? 1.0967 1.6820 2.2528 0.1511  -0.0058 -0.3382 145 ASN C CG  
18350 O OD1 . ASN C 145 ? 1.1519 1.6744 2.2333 0.1696  0.0339  -0.3297 145 ASN C OD1 
18351 N ND2 . ASN C 145 ? 1.0998 1.7452 2.3768 0.1512  -0.0029 -0.3277 145 ASN C ND2 
18358 N N   . VAL C 146 ? 1.0652 1.5689 1.9532 0.1018  -0.0874 -0.3946 146 VAL C N   
18359 C CA  . VAL C 146 ? 1.0335 1.5316 1.8713 0.0835  -0.1174 -0.4162 146 VAL C CA  
18360 C C   . VAL C 146 ? 1.0290 1.5226 1.9298 0.0587  -0.0958 -0.4347 146 VAL C C   
18361 O O   . VAL C 146 ? 1.0661 1.5342 2.0038 0.0593  -0.0443 -0.4241 146 VAL C O   
18362 C CB  . VAL C 146 ? 1.0425 1.4802 1.7520 0.0938  -0.1080 -0.4075 146 VAL C CB  
18363 C CG1 . VAL C 146 ? 1.0252 1.4688 1.6760 0.1148  -0.1367 -0.3892 146 VAL C CG1 
18364 C CG2 . VAL C 146 ? 1.0652 1.4434 1.7504 0.0992  -0.0456 -0.3943 146 VAL C CG2 
18374 N N   . LYS C 147 ? 1.0129 1.5305 1.9253 0.0375  -0.1352 -0.4621 147 LYS C N   
18375 C CA  . LYS C 147 ? 1.0172 1.5266 1.9876 0.0107  -0.1226 -0.4839 147 LYS C CA  
18376 C C   . LYS C 147 ? 1.0452 1.5288 1.9382 0.0004  -0.1479 -0.5094 147 LYS C C   
18377 O O   . LYS C 147 ? 1.0081 1.5180 1.8511 0.0051  -0.1962 -0.5196 147 LYS C O   
18378 C CB  . LYS C 147 ? 1.0008 1.5763 2.0974 -0.0093 -0.1493 -0.4964 147 LYS C CB  
18379 C CG  . LYS C 147 ? 1.0156 1.5963 2.2184 -0.0143 -0.1021 -0.4795 147 LYS C CG  
18380 C CD  . LYS C 147 ? 1.0344 1.6929 2.3575 -0.0238 -0.1300 -0.4767 147 LYS C CD  
18381 C CE  . LYS C 147 ? 1.0771 1.7454 2.5116 -0.0276 -0.0811 -0.4555 147 LYS C CE  
18382 N NZ  . LYS C 147 ? 1.0998 1.8386 2.6312 -0.0193 -0.0919 -0.4345 147 LYS C NZ  
18396 N N   . TRP C 148 ? 1.0621 1.4953 1.9456 -0.0113 -0.1131 -0.5172 148 TRP C N   
18397 C CA  . TRP C 148 ? 1.0809 1.4807 1.8910 -0.0182 -0.1276 -0.5398 148 TRP C CA  
18398 C C   . TRP C 148 ? 1.1188 1.5323 2.0043 -0.0486 -0.1493 -0.5775 148 TRP C C   
18399 O O   . TRP C 148 ? 1.1727 1.5770 2.1462 -0.0663 -0.1190 -0.5785 148 TRP C O   
18400 C CB  . TRP C 148 ? 1.0515 1.3832 1.7954 -0.0097 -0.0748 -0.5215 148 TRP C CB  
18401 C CG  . TRP C 148 ? 0.9448 1.2571 1.5860 0.0169  -0.0672 -0.4915 148 TRP C CG  
18402 C CD1 . TRP C 148 ? 0.8756 1.1789 1.5092 0.0333  -0.0362 -0.4609 148 TRP C CD1 
18403 C CD2 . TRP C 148 ? 0.9071 1.2058 1.4391 0.0295  -0.0919 -0.4890 148 TRP C CD2 
18404 N NE1 . TRP C 148 ? 0.8335 1.1160 1.3614 0.0523  -0.0430 -0.4412 148 TRP C NE1 
18405 C CE2 . TRP C 148 ? 0.8570 1.1393 1.3244 0.0503  -0.0767 -0.4551 148 TRP C CE2 
18406 C CE3 . TRP C 148 ? 0.9224 1.2211 1.4048 0.0262  -0.1248 -0.5116 148 TRP C CE3 
18407 C CZ2 . TRP C 148 ? 0.8754 1.1450 1.2379 0.0652  -0.0950 -0.4396 148 TRP C CZ2 
18408 C CZ3 . TRP C 148 ? 0.9175 1.2058 1.2934 0.0448  -0.1396 -0.4948 148 TRP C CZ3 
18409 C CH2 . TRP C 148 ? 0.8979 1.1735 1.2185 0.0629  -0.1255 -0.4574 148 TRP C CH2 
18420 N N   . LYS C 149 ? 1.1637 1.5993 2.0143 -0.0544 -0.2023 -0.6077 149 LYS C N   
18421 C CA  . LYS C 149 ? 1.2254 1.6728 2.1335 -0.0838 -0.2330 -0.6502 149 LYS C CA  
18422 C C   . LYS C 149 ? 1.3063 1.7054 2.1217 -0.0824 -0.2401 -0.6764 149 LYS C C   
18423 O O   . LYS C 149 ? 1.3479 1.7525 2.0651 -0.0617 -0.2643 -0.6741 149 LYS C O   
18424 C CB  . LYS C 149 ? 1.2607 1.7792 2.2030 -0.0885 -0.2892 -0.6582 149 LYS C CB  
18425 C CG  . LYS C 149 ? 1.3298 1.8486 2.3071 -0.1130 -0.3127 -0.6811 149 LYS C CG  
18426 C CD  . LYS C 149 ? 1.3549 1.9330 2.3393 -0.1115 -0.3558 -0.6675 149 LYS C CD  
18427 C CE  . LYS C 149 ? 1.4519 2.0333 2.4660 -0.1385 -0.3840 -0.6915 149 LYS C CE  
18428 N NZ  . LYS C 149 ? 1.5050 2.1459 2.5239 -0.1402 -0.4252 -0.6763 149 LYS C NZ  
18442 N N   . ILE C 150 ? 1.2941 1.6457 2.1427 -0.1028 -0.2172 -0.6983 150 ILE C N   
18443 C CA  . ILE C 150 ? 1.3316 1.6296 2.0972 -0.0998 -0.2166 -0.7220 150 ILE C CA  
18444 C C   . ILE C 150 ? 1.4031 1.7145 2.1702 -0.1120 -0.2566 -0.7442 150 ILE C C   
18445 O O   . ILE C 150 ? 1.4219 1.7798 2.1520 -0.1016 -0.2974 -0.7378 150 ILE C O   
18446 C CB  . ILE C 150 ? 1.3148 1.5429 2.0929 -0.1044 -0.1548 -0.7105 150 ILE C CB  
18447 C CG1 . ILE C 150 ? 1.2451 1.4682 2.0090 -0.0837 -0.1067 -0.6568 150 ILE C CG1 
18448 C CG2 . ILE C 150 ? 1.3566 1.5283 2.0361 -0.0927 -0.1472 -0.7250 150 ILE C CG2 
18449 C CD1 . ILE C 150 ? 1.2486 1.4103 2.0080 -0.0815 -0.0424 -0.6331 150 ILE C CD1 
18461 N N   . ASP C 151 ? 1.4258 1.6953 2.2341 -0.1343 -0.2450 -0.7682 151 ASP C N   
18462 C CA  . ASP C 151 ? 1.4645 1.7442 2.2771 -0.1497 -0.2851 -0.7930 151 ASP C CA  
18463 C C   . ASP C 151 ? 1.4318 1.7572 2.3661 -0.1765 -0.3012 -0.7933 151 ASP C C   
18464 O O   . ASP C 151 ? 1.4701 1.7747 2.4811 -0.2041 -0.2962 -0.8096 151 ASP C O   
18465 C CB  . ASP C 151 ? 1.5311 1.7415 2.3227 -0.1604 -0.2698 -0.8194 151 ASP C CB  
18466 C CG  . ASP C 151 ? 1.5046 1.6687 2.1804 -0.1330 -0.2494 -0.8140 151 ASP C CG  
18467 O OD1 . ASP C 151 ? 1.4845 1.6737 2.0677 -0.1084 -0.2732 -0.8034 151 ASP C OD1 
18468 O OD2 . ASP C 151 ? 1.5012 1.6041 2.1812 -0.1357 -0.2073 -0.8155 151 ASP C OD2 
18473 N N   . GLY C 152 ? 1.3719 1.7608 2.3235 -0.1670 -0.3205 -0.7705 152 GLY C N   
18474 C CA  . GLY C 152 ? 1.3716 1.8099 2.4352 -0.1884 -0.3345 -0.7626 152 GLY C CA  
18475 C C   . GLY C 152 ? 1.3974 1.8310 2.5752 -0.2016 -0.2903 -0.7476 152 GLY C C   
18476 O O   . GLY C 152 ? 1.3955 1.8586 2.6782 -0.2237 -0.2948 -0.7410 152 GLY C O   
18480 N N   . SER C 153 ? 1.3523 1.7502 2.5121 -0.1889 -0.2456 -0.7381 153 SER C N   
18481 C CA  . SER C 153 ? 1.3475 1.7373 2.6107 -0.2001 -0.1947 -0.7194 153 SER C CA  
18482 C C   . SER C 153 ? 1.3276 1.7226 2.5432 -0.1684 -0.1609 -0.6810 153 SER C C   
18483 O O   . SER C 153 ? 1.3428 1.7245 2.4424 -0.1430 -0.1696 -0.6776 153 SER C O   
18484 C CB  . SER C 153 ? 1.3428 1.6589 2.6181 -0.2146 -0.1545 -0.7316 153 SER C CB  
18485 O OG  . SER C 153 ? 1.3114 1.6174 2.6353 -0.2397 -0.1752 -0.7507 153 SER C OG  
18491 N N   . GLU C 154 ? 1.2880 1.6980 2.5816 -0.1652 -0.1190 -0.6440 154 GLU C N   
18492 C CA  . GLU C 154 ? 1.2204 1.6247 2.4637 -0.1318 -0.0777 -0.6004 154 GLU C CA  
18493 C C   . GLU C 154 ? 1.2391 1.5849 2.4796 -0.1274 -0.0099 -0.5765 154 GLU C C   
18494 O O   . GLU C 154 ? 1.2405 1.5823 2.5822 -0.1480 0.0163  -0.5729 154 GLU C O   
18495 C CB  . GLU C 154 ? 1.1543 1.6217 2.4815 -0.1256 -0.0777 -0.5743 154 GLU C CB  
18496 C CG  . GLU C 154 ? 1.1523 1.6836 2.4757 -0.1226 -0.1395 -0.5862 154 GLU C CG  
18497 C CD  . GLU C 154 ? 1.1607 1.7416 2.5362 -0.1036 -0.1277 -0.5506 154 GLU C CD  
18498 O OE1 . GLU C 154 ? 1.1629 1.7163 2.5250 -0.0819 -0.0730 -0.5180 154 GLU C OE1 
18499 O OE2 . GLU C 154 ? 1.1631 1.8107 2.5923 -0.1093 -0.1725 -0.5550 154 GLU C OE2 
18506 N N   . ARG C 155 ? 1.2501 1.5544 2.3783 -0.1012 0.0174  -0.5573 155 ARG C N   
18507 C CA  . ARG C 155 ? 1.2907 1.5435 2.4048 -0.0942 0.0816  -0.5305 155 ARG C CA  
18508 C C   . ARG C 155 ? 1.2417 1.5066 2.3691 -0.0726 0.1273  -0.4879 155 ARG C C   
18509 O O   . ARG C 155 ? 1.2568 1.5185 2.4615 -0.0777 0.1738  -0.4668 155 ARG C O   
18510 C CB  . ARG C 155 ? 1.3266 1.5268 2.3119 -0.0796 0.0878  -0.5312 155 ARG C CB  
18511 C CG  . ARG C 155 ? 1.3289 1.4826 2.2877 -0.0684 0.1541  -0.4962 155 ARG C CG  
18512 C CD  . ARG C 155 ? 1.3021 1.4036 2.1597 -0.0612 0.1616  -0.4986 155 ARG C CD  
18513 N NE  . ARG C 155 ? 1.3179 1.4058 2.1870 -0.0803 0.1262  -0.5412 155 ARG C NE  
18514 C CZ  . ARG C 155 ? 1.3657 1.4141 2.2786 -0.0976 0.1480  -0.5537 155 ARG C CZ  
18515 N NH1 . ARG C 155 ? 1.4172 1.4513 2.3316 -0.1135 0.1105  -0.5979 155 ARG C NH1 
18516 N NH2 . ARG C 155 ? 1.3361 1.3582 2.2892 -0.0983 0.2069  -0.5224 155 ARG C NH2 
18530 N N   . GLN C 156 ? 1.2039 1.4810 2.2554 -0.0475 0.1153  -0.4747 156 GLN C N   
18531 C CA  . GLN C 156 ? 1.1988 1.4825 2.2496 -0.0241 0.1548  -0.4394 156 GLN C CA  
18532 C C   . GLN C 156 ? 1.2122 1.4514 2.2424 -0.0161 0.2206  -0.4112 156 GLN C C   
18533 O O   . GLN C 156 ? 1.2618 1.5106 2.3403 -0.0056 0.2646  -0.3848 156 GLN C O   
18534 C CB  . GLN C 156 ? 1.2276 1.5669 2.4017 -0.0289 0.1542  -0.4332 156 GLN C CB  
18535 C CG  . GLN C 156 ? 1.2459 1.6394 2.4733 -0.0443 0.0908  -0.4597 156 GLN C CG  
18536 C CD  . GLN C 156 ? 1.2520 1.7026 2.6144 -0.0511 0.0963  -0.4474 156 GLN C CD  
18537 O OE1 . GLN C 156 ? 1.2484 1.7486 2.6375 -0.0437 0.0647  -0.4458 156 GLN C OE1 
18538 N NE2 . GLN C 156 ? 1.2502 1.6969 2.7028 -0.0647 0.1378  -0.4344 156 GLN C NE2 
18547 N N   . ASN C 157 ? 1.2353 1.4283 2.1934 -0.0191 0.2295  -0.4144 157 ASN C N   
18548 C CA  . ASN C 157 ? 1.2770 1.4316 2.2151 -0.0122 0.2908  -0.3849 157 ASN C CA  
18549 C C   . ASN C 157 ? 1.3116 1.4281 2.1126 0.0073  0.2996  -0.3685 157 ASN C C   
18550 O O   . ASN C 157 ? 1.3716 1.4753 2.1327 0.0252  0.3403  -0.3381 157 ASN C O   
18551 C CB  . ASN C 157 ? 1.2983 1.4317 2.3020 -0.0363 0.3071  -0.3947 157 ASN C CB  
18552 C CG  . ASN C 157 ? 1.3269 1.4543 2.3987 -0.0355 0.3725  -0.3610 157 ASN C CG  
18553 O OD1 . ASN C 157 ? 1.3224 1.4633 2.3900 -0.0158 0.4063  -0.3322 157 ASN C OD1 
18554 N ND2 . ASN C 157 ? 1.3515 1.4583 2.4872 -0.0559 0.3912  -0.3643 157 ASN C ND2 
18561 N N   . GLY C 158 ? 1.2709 1.3707 1.9977 0.0048  0.2626  -0.3863 158 GLY C N   
18562 C CA  . GLY C 158 ? 1.2769 1.3459 1.8784 0.0217  0.2665  -0.3675 158 GLY C CA  
18563 C C   . GLY C 158 ? 1.2534 1.3386 1.7833 0.0378  0.2288  -0.3660 158 GLY C C   
18564 O O   . GLY C 158 ? 1.2648 1.3280 1.6912 0.0496  0.2233  -0.3506 158 GLY C O   
18568 N N   . VAL C 159 ? 1.2968 1.2803 1.9632 0.0851  0.1926  -0.1529 159 VAL C N   
18569 C CA  . VAL C 159 ? 1.1604 1.2193 1.7700 0.0845  0.1617  -0.1643 159 VAL C CA  
18570 C C   . VAL C 159 ? 1.1871 1.1856 1.6644 0.1127  0.1782  -0.1159 159 VAL C C   
18571 O O   . VAL C 159 ? 1.2641 1.1810 1.7088 0.1263  0.2282  -0.0685 159 VAL C O   
18572 C CB  . VAL C 159 ? 1.0518 1.1870 1.7507 0.0572  0.1670  -0.1801 159 VAL C CB  
18573 C CG1 . VAL C 159 ? 1.1206 1.2071 1.8604 0.0538  0.2305  -0.1371 159 VAL C CG1 
18574 C CG2 . VAL C 159 ? 0.9478 1.1479 1.5808 0.0583  0.1340  -0.1878 159 VAL C CG2 
18584 N N   . LEU C 160 ? 1.1343 1.1711 1.5336 0.1210  0.1379  -0.1294 160 LEU C N   
18585 C CA  . LEU C 160 ? 1.1121 1.1052 1.3922 0.1448  0.1427  -0.0954 160 LEU C CA  
18586 C C   . LEU C 160 ? 1.0375 1.1060 1.2964 0.1301  0.1117  -0.1142 160 LEU C C   
18587 O O   . LEU C 160 ? 1.0108 1.1531 1.3028 0.1118  0.0750  -0.1539 160 LEU C O   
18588 C CB  . LEU C 160 ? 1.1419 1.0744 1.3312 0.1781  0.1203  -0.0897 160 LEU C CB  
18589 C CG  . LEU C 160 ? 1.2830 1.0997 1.4263 0.2086  0.1566  -0.0475 160 LEU C CG  
18590 C CD1 . LEU C 160 ? 1.3371 1.1030 1.3824 0.2484  0.1184  -0.0484 160 LEU C CD1 
18591 C CD2 . LEU C 160 ? 1.3742 1.1313 1.4663 0.2178  0.2132  0.0026  160 LEU C CD2 
18603 N N   . ASN C 161 ? 1.0201 1.0638 1.2183 0.1397  0.1292  -0.0847 161 ASN C N   
18604 C CA  . ASN C 161 ? 0.9400 1.0387 1.1208 0.1261  0.1061  -0.0947 161 ASN C CA  
18605 C C   . ASN C 161 ? 0.9716 1.0219 1.0375 0.1473  0.0983  -0.0753 161 ASN C C   
18606 O O   . ASN C 161 ? 1.0479 1.0201 1.0477 0.1762  0.1225  -0.0468 161 ASN C O   
18607 C CB  . ASN C 161 ? 0.8845 1.0126 1.1331 0.1152  0.1307  -0.0867 161 ASN C CB  
18608 C CG  . ASN C 161 ? 0.8243 1.0069 1.1972 0.0928  0.1308  -0.1144 161 ASN C CG  
18609 O OD1 . ASN C 161 ? 0.7981 1.0270 1.2002 0.0787  0.0975  -0.1501 161 ASN C OD1 
18610 N ND2 . ASN C 161 ? 0.7960 0.9760 1.2484 0.0897  0.1692  -0.1022 161 ASN C ND2 
18617 N N   . SER C 162 ? 0.9311 1.0240 0.9702 0.1326  0.0645  -0.0914 162 SER C N   
18618 C CA  . SER C 162 ? 0.9322 0.9854 0.8761 0.1460  0.0505  -0.0811 162 SER C CA  
18619 C C   . SER C 162 ? 0.9413 1.0301 0.8833 0.1264  0.0373  -0.0827 162 SER C C   
18620 O O   . SER C 162 ? 0.8837 1.0387 0.8774 0.1001  0.0220  -0.1008 162 SER C O   
18621 C CB  . SER C 162 ? 0.8580 0.9142 0.7654 0.1480  0.0143  -0.1041 162 SER C CB  
18622 O OG  . SER C 162 ? 0.8702 0.8728 0.6880 0.1674  0.0010  -0.0960 162 SER C OG  
18628 N N   . TRP C 163 ? 1.0254 1.0632 0.8996 0.1428  0.0420  -0.0638 163 TRP C N   
18629 C CA  . TRP C 163 ? 1.0280 1.0776 0.8893 0.1312  0.0300  -0.0597 163 TRP C CA  
18630 C C   . TRP C 163 ? 1.0663 1.0798 0.8493 0.1294  0.0032  -0.0642 163 TRP C C   
18631 O O   . TRP C 163 ? 1.1631 1.1183 0.8847 0.1545  0.0035  -0.0614 163 TRP C O   
18632 C CB  . TRP C 163 ? 1.0546 1.0741 0.9213 0.1543  0.0614  -0.0368 163 TRP C CB  
18633 C CG  . TRP C 163 ? 1.0329 1.0961 0.9970 0.1512  0.0869  -0.0359 163 TRP C CG  
18634 C CD1 . TRP C 163 ? 1.0262 1.1420 1.0556 0.1411  0.0789  -0.0416 163 TRP C CD1 
18635 C CD2 . TRP C 163 ? 1.0096 1.0644 1.0214 0.1586  0.1224  -0.0307 163 TRP C CD2 
18636 N NE1 . TRP C 163 ? 0.9865 1.1361 1.1135 0.1397  0.1048  -0.0461 163 TRP C NE1 
18637 C CE2 . TRP C 163 ? 0.9713 1.0814 1.0911 0.1474  0.1355  -0.0375 163 TRP C CE2 
18638 C CE3 . TRP C 163 ? 1.0435 1.0443 1.0157 0.1748  0.1423  -0.0203 163 TRP C CE3 
18639 C CZ2 . TRP C 163 ? 0.9402 1.0540 1.1404 0.1454  0.1725  -0.0353 163 TRP C CZ2 
18640 C CZ3 . TRP C 163 ? 1.0528 1.0477 1.0903 0.1758  0.1809  -0.0116 163 TRP C CZ3 
18641 C CH2 . TRP C 163 ? 0.9937 1.0453 1.1496 0.1579  0.1980  -0.0195 163 TRP C CH2 
18652 N N   . THR C 164 ? 0.9990 1.0428 0.7815 0.1002  -0.0201 -0.0716 164 THR C N   
18653 C CA  . THR C 164 ? 1.0756 1.0833 0.7984 0.0912  -0.0430 -0.0760 164 THR C CA  
18654 C C   . THR C 164 ? 1.1534 1.0992 0.8294 0.1098  -0.0382 -0.0561 164 THR C C   
18655 O O   . THR C 164 ? 1.1708 1.1205 0.8707 0.1222  -0.0217 -0.0401 164 THR C O   
18656 C CB  . THR C 164 ? 1.0979 1.1570 0.8381 0.0476  -0.0622 -0.0889 164 THR C CB  
18657 O OG1 . THR C 164 ? 1.0931 1.1688 0.8430 0.0364  -0.0592 -0.0725 164 THR C OG1 
18658 C CG2 . THR C 164 ? 1.0631 1.1914 0.8560 0.0320  -0.0646 -0.1140 164 THR C CG2 
18666 N N   . ASP C 165 ? 1.1749 1.0651 0.7908 0.1135  -0.0560 -0.0622 165 ASP C N   
18667 C CA  . ASP C 165 ? 1.2578 1.0848 0.8278 0.1284  -0.0575 -0.0491 165 ASP C CA  
18668 C C   . ASP C 165 ? 1.2361 1.0792 0.8207 0.0970  -0.0694 -0.0378 165 ASP C C   
18669 O O   . ASP C 165 ? 1.2333 1.1306 0.8475 0.0598  -0.0777 -0.0428 165 ASP C O   
18670 C CB  . ASP C 165 ? 1.4002 1.1609 0.9044 0.1382  -0.0795 -0.0656 165 ASP C CB  
18671 C CG  . ASP C 165 ? 1.4739 1.1883 0.9280 0.1863  -0.0660 -0.0687 165 ASP C CG  
18672 O OD1 . ASP C 165 ? 1.4848 1.1980 0.9474 0.2143  -0.0299 -0.0498 165 ASP C OD1 
18673 O OD2 . ASP C 165 ? 1.5204 1.1990 0.9260 0.1968  -0.0911 -0.0906 165 ASP C OD2 
18678 N N   . GLN C 166 ? 1.2636 1.0551 0.8211 0.1163  -0.0689 -0.0218 166 GLN C N   
18679 C CA  . GLN C 166 ? 1.2724 1.0559 0.8240 0.0941  -0.0840 -0.0057 166 GLN C CA  
18680 C C   . GLN C 166 ? 1.3588 1.1190 0.8818 0.0515  -0.1036 -0.0126 166 GLN C C   
18681 O O   . GLN C 166 ? 1.4274 1.1305 0.9159 0.0542  -0.1150 -0.0264 166 GLN C O   
18682 C CB  . GLN C 166 ? 1.3097 1.0294 0.8352 0.1310  -0.0837 0.0091  166 GLN C CB  
18683 C CG  . GLN C 166 ? 1.3445 1.0203 0.8398 0.1153  -0.1055 0.0283  166 GLN C CG  
18684 C CD  . GLN C 166 ? 1.3330 0.9779 0.8307 0.1585  -0.1065 0.0430  166 GLN C CD  
18685 O OE1 . GLN C 166 ? 1.3840 0.9516 0.8440 0.1853  -0.1108 0.0423  166 GLN C OE1 
18686 N NE2 . GLN C 166 ? 1.2666 0.9739 0.8134 0.1676  -0.1060 0.0515  166 GLN C NE2 
18695 N N   . ASP C 167 ? 1.3888 1.1943 0.9277 0.0116  -0.1061 -0.0053 167 ASP C N   
18696 C CA  . ASP C 167 ? 1.4461 1.2403 0.9721 -0.0363 -0.1144 -0.0111 167 ASP C CA  
18697 C C   . ASP C 167 ? 1.5333 1.2296 1.0087 -0.0408 -0.1266 0.0070  167 ASP C C   
18698 O O   . ASP C 167 ? 1.5439 1.1965 0.9925 -0.0145 -0.1300 0.0316  167 ASP C O   
18699 C CB  . ASP C 167 ? 1.4388 1.3032 0.9845 -0.0754 -0.1049 -0.0046 167 ASP C CB  
18700 C CG  . ASP C 167 ? 1.5284 1.4112 1.0865 -0.1279 -0.1014 -0.0195 167 ASP C CG  
18701 O OD1 . ASP C 167 ? 1.6410 1.4591 1.1693 -0.1548 -0.1049 -0.0070 167 ASP C OD1 
18702 O OD2 . ASP C 167 ? 1.4893 1.4514 1.0946 -0.1425 -0.0941 -0.0459 167 ASP C OD2 
18707 N N   . SER C 168 ? 1.5906 1.2518 1.0606 -0.0733 -0.1361 -0.0091 168 SER C N   
18708 C CA  . SER C 168 ? 1.6717 1.2290 1.0997 -0.0811 -0.1493 0.0028  168 SER C CA  
18709 C C   . SER C 168 ? 1.7243 1.2555 1.1270 -0.1179 -0.1413 0.0416  168 SER C C   
18710 O O   . SER C 168 ? 1.7974 1.2448 1.1546 -0.0998 -0.1503 0.0693  168 SER C O   
18711 C CB  . SER C 168 ? 1.7134 1.2443 1.1560 -0.1073 -0.1651 -0.0329 168 SER C CB  
18712 O OG  . SER C 168 ? 1.6947 1.3163 1.1930 -0.1417 -0.1591 -0.0579 168 SER C OG  
18718 N N   . LYS C 169 ? 1.7233 1.3213 1.1489 -0.1660 -0.1235 0.0448  169 LYS C N   
18719 C CA  . LYS C 169 ? 1.8305 1.3946 1.2161 -0.2049 -0.1100 0.0844  169 LYS C CA  
18720 C C   . LYS C 169 ? 1.8544 1.4117 1.1936 -0.1674 -0.1148 0.1200  169 LYS C C   
18721 O O   . LYS C 169 ? 2.0132 1.4845 1.2921 -0.1650 -0.1216 0.1585  169 LYS C O   
18722 C CB  . LYS C 169 ? 1.8625 1.5112 1.2824 -0.2614 -0.0824 0.0756  169 LYS C CB  
18723 C CG  . LYS C 169 ? 1.8840 1.5847 1.3779 -0.2892 -0.0819 0.0274  169 LYS C CG  
18724 C CD  . LYS C 169 ? 1.8223 1.6422 1.3639 -0.3174 -0.0570 0.0093  169 LYS C CD  
18725 C CE  . LYS C 169 ? 1.8603 1.7187 1.4719 -0.3721 -0.0455 -0.0243 169 LYS C CE  
18726 N NZ  . LYS C 169 ? 1.8580 1.8092 1.4973 -0.4149 -0.0064 -0.0258 169 LYS C NZ  
18740 N N   . ASP C 170 ? 1.7349 1.3816 1.1053 -0.1382 -0.1139 0.1059  170 ASP C N   
18741 C CA  . ASP C 170 ? 1.7059 1.3686 1.0557 -0.0987 -0.1246 0.1263  170 ASP C CA  
18742 C C   . ASP C 170 ? 1.6635 1.3630 1.0652 -0.0476 -0.1318 0.1010  170 ASP C C   
18743 O O   . ASP C 170 ? 1.5980 1.3540 1.0490 -0.0504 -0.1214 0.0697  170 ASP C O   
18744 C CB  . ASP C 170 ? 1.6519 1.3976 0.9975 -0.1212 -0.1124 0.1297  170 ASP C CB  
18745 C CG  . ASP C 170 ? 1.5444 1.3988 0.9633 -0.1183 -0.1029 0.0889  170 ASP C CG  
18746 O OD1 . ASP C 170 ? 1.4943 1.3831 0.9510 -0.0762 -0.1136 0.0761  170 ASP C OD1 
18747 O OD2 . ASP C 170 ? 1.5358 1.4394 0.9812 -0.1579 -0.0839 0.0686  170 ASP C OD2 
18752 N N   . SER C 171 ? 1.6484 1.3140 1.0409 0.0001  -0.1476 0.1149  171 SER C N   
18753 C CA  . SER C 171 ? 1.6096 1.2917 1.0499 0.0457  -0.1446 0.0933  171 SER C CA  
18754 C C   . SER C 171 ? 1.4943 1.2811 1.0020 0.0562  -0.1334 0.0727  171 SER C C   
18755 O O   . SER C 171 ? 1.4464 1.2477 0.9963 0.0890  -0.1218 0.0575  171 SER C O   
18756 C CB  . SER C 171 ? 1.6792 1.2983 1.1028 0.0943  -0.1612 0.1101  171 SER C CB  
18757 O OG  . SER C 171 ? 1.7738 1.2840 1.1388 0.0877  -0.1717 0.1248  171 SER C OG  
18763 N N   . THR C 172 ? 1.4316 1.2867 0.9495 0.0294  -0.1333 0.0704  172 THR C N   
18764 C CA  . THR C 172 ? 1.3454 1.2933 0.9322 0.0384  -0.1259 0.0468  172 THR C CA  
18765 C C   . THR C 172 ? 1.2708 1.2432 0.8995 0.0350  -0.1048 0.0212  172 THR C C   
18766 O O   . THR C 172 ? 1.2837 1.2174 0.8861 0.0194  -0.1002 0.0165  172 THR C O   
18767 C CB  . THR C 172 ? 1.3378 1.3490 0.9170 0.0085  -0.1301 0.0425  172 THR C CB  
18768 O OG1 . THR C 172 ? 1.3058 1.3308 0.8739 -0.0343 -0.1133 0.0316  172 THR C OG1 
18769 C CG2 . THR C 172 ? 1.4179 1.3932 0.9282 0.0098  -0.1514 0.0725  172 THR C CG2 
18777 N N   . TYR C 173 ? 1.2256 1.2619 0.9215 0.0499  -0.0951 0.0031  173 TYR C N   
18778 C CA  . TYR C 173 ? 1.1968 1.2555 0.9325 0.0534  -0.0753 -0.0173 173 TYR C CA  
18779 C C   . TYR C 173 ? 1.1345 1.2723 0.9140 0.0300  -0.0743 -0.0400 173 TYR C C   
18780 O O   . TYR C 173 ? 1.1563 1.3342 0.9320 0.0130  -0.0869 -0.0420 173 TYR C O   
18781 C CB  . TYR C 173 ? 1.2090 1.2620 0.9906 0.0925  -0.0564 -0.0163 173 TYR C CB  
18782 C CG  . TYR C 173 ? 1.2933 1.2883 1.0505 0.1238  -0.0572 0.0017  173 TYR C CG  
18783 C CD1 . TYR C 173 ? 1.3370 1.3371 1.0987 0.1336  -0.0783 0.0129  173 TYR C CD1 
18784 C CD2 . TYR C 173 ? 1.3455 1.2793 1.0716 0.1493  -0.0390 0.0048  173 TYR C CD2 
18785 C CE1 . TYR C 173 ? 1.3740 1.3215 1.1197 0.1672  -0.0817 0.0262  173 TYR C CE1 
18786 C CE2 . TYR C 173 ? 1.4405 1.3227 1.1466 0.1818  -0.0382 0.0161  173 TYR C CE2 
18787 C CZ  . TYR C 173 ? 1.4795 1.3701 1.2013 0.1905  -0.0595 0.0264  173 TYR C CZ  
18788 O OH  . TYR C 173 ? 1.6159 1.4555 1.3241 0.2276  -0.0615 0.0347  173 TYR C OH  
18798 N N   . SER C 174 ? 1.0730 1.2281 0.8877 0.0336  -0.0600 -0.0579 174 SER C N   
18799 C CA  . SER C 174 ? 0.9714 1.1958 0.8338 0.0169  -0.0593 -0.0840 174 SER C CA  
18800 C C   . SER C 174 ? 0.9116 1.1404 0.8292 0.0382  -0.0414 -0.0940 174 SER C C   
18801 O O   . SER C 174 ? 0.9540 1.1290 0.8548 0.0619  -0.0262 -0.0807 174 SER C O   
18802 C CB  . SER C 174 ? 0.9591 1.2003 0.7971 -0.0135 -0.0645 -0.0992 174 SER C CB  
18803 O OG  . SER C 174 ? 0.9909 1.2290 0.7814 -0.0397 -0.0725 -0.0869 174 SER C OG  
18809 N N   . PHE C 175 ? 0.8698 1.1578 0.8473 0.0299  -0.0418 -0.1179 175 PHE C N   
18810 C CA  . PHE C 175 ? 0.9085 1.2008 0.9513 0.0456  -0.0236 -0.1264 175 PHE C CA  
18811 C C   . PHE C 175 ? 0.9073 1.2431 0.9828 0.0322  -0.0302 -0.1581 175 PHE C C   
18812 O O   . PHE C 175 ? 0.8815 1.2741 0.9649 0.0120  -0.0462 -0.1805 175 PHE C O   
18813 C CB  . PHE C 175 ? 0.9362 1.2583 1.0476 0.0527  -0.0204 -0.1276 175 PHE C CB  
18814 C CG  . PHE C 175 ? 0.9407 1.2551 1.1282 0.0657  0.0079  -0.1293 175 PHE C CG  
18815 C CD1 . PHE C 175 ? 0.9283 1.2637 1.1662 0.0579  0.0109  -0.1528 175 PHE C CD1 
18816 C CD2 . PHE C 175 ? 0.9898 1.2754 1.2040 0.0851  0.0347  -0.1077 175 PHE C CD2 
18817 C CE1 . PHE C 175 ? 0.9398 1.2565 1.2484 0.0664  0.0410  -0.1497 175 PHE C CE1 
18818 C CE2 . PHE C 175 ? 0.9926 1.2691 1.2810 0.0919  0.0699  -0.1055 175 PHE C CE2 
18819 C CZ  . PHE C 175 ? 0.9618 1.2490 1.2956 0.0809  0.0733  -0.1242 175 PHE C CZ  
18829 N N   . SER C 176 ? 0.9441 1.2496 1.0319 0.0471  -0.0177 -0.1601 176 SER C N   
18830 C CA  . SER C 176 ? 0.8697 1.2082 0.9968 0.0426  -0.0247 -0.1915 176 SER C CA  
18831 C C   . SER C 176 ? 0.8513 1.1684 1.0425 0.0578  -0.0049 -0.1910 176 SER C C   
18832 O O   . SER C 176 ? 0.9279 1.1802 1.1017 0.0786  0.0193  -0.1615 176 SER C O   
18833 C CB  . SER C 176 ? 0.8702 1.1867 0.9524 0.0494  -0.0354 -0.1973 176 SER C CB  
18834 O OG  . SER C 176 ? 0.8581 1.1856 0.9824 0.0594  -0.0396 -0.2222 176 SER C OG  
18840 N N   . SER C 177 ? 0.7753 1.1423 1.0375 0.0471  -0.0124 -0.2242 177 SER C N   
18841 C CA  . SER C 177 ? 0.7569 1.1031 1.0949 0.0549  0.0061  -0.2279 177 SER C CA  
18842 C C   . SER C 177 ? 0.7567 1.1184 1.1288 0.0567  -0.0073 -0.2635 177 SER C C   
18843 O O   . SER C 177 ? 0.7365 1.1651 1.1212 0.0429  -0.0307 -0.3023 177 SER C O   
18844 C CB  . SER C 177 ? 0.6849 1.0747 1.1010 0.0416  0.0065  -0.2406 177 SER C CB  
18845 O OG  . SER C 177 ? 0.6576 1.0146 1.1532 0.0457  0.0342  -0.2352 177 SER C OG  
18851 N N   . THR C 178 ? 0.7574 1.0531 1.1396 0.0764  0.0095  -0.2496 178 THR C N   
18852 C CA  . THR C 178 ? 0.7701 1.0639 1.1847 0.0863  -0.0043 -0.2805 178 THR C CA  
18853 C C   . THR C 178 ? 0.8567 1.0968 1.3429 0.0911  0.0203  -0.2733 178 THR C C   
18854 O O   . THR C 178 ? 0.9606 1.1225 1.4246 0.1038  0.0540  -0.2279 178 THR C O   
18855 C CB  . THR C 178 ? 0.7494 1.0009 1.0907 0.1126  -0.0167 -0.2701 178 THR C CB  
18856 O OG1 . THR C 178 ? 0.6543 0.9577 0.9451 0.1015  -0.0370 -0.2798 178 THR C OG1 
18857 C CG2 . THR C 178 ? 0.7374 0.9872 1.1189 0.1294  -0.0351 -0.3046 178 THR C CG2 
18865 N N   . LEU C 179 ? 0.8342 1.1131 1.4046 0.0803  0.0065  -0.3186 179 LEU C N   
18866 C CA  . LEU C 179 ? 0.8331 1.0582 1.4846 0.0815  0.0257  -0.3203 179 LEU C CA  
18867 C C   . LEU C 179 ? 0.8120 1.0033 1.4619 0.1053  0.0073  -0.3424 179 LEU C C   
18868 O O   . LEU C 179 ? 0.7237 0.9828 1.3847 0.1057  -0.0260 -0.3929 179 LEU C O   
18869 C CB  . LEU C 179 ? 0.7973 1.0859 1.5571 0.0539  0.0175  -0.3633 179 LEU C CB  
18870 C CG  . LEU C 179 ? 0.8377 1.0846 1.7023 0.0494  0.0264  -0.3856 179 LEU C CG  
18871 C CD1 . LEU C 179 ? 0.9135 1.0638 1.8012 0.0490  0.0787  -0.3293 179 LEU C CD1 
18872 C CD2 . LEU C 179 ? 0.7970 1.1241 1.7631 0.0248  0.0020  -0.4453 179 LEU C CD2 
18884 N N   . THR C 180 ? 0.9199 1.0048 1.5537 0.1276  0.0305  -0.3045 180 THR C N   
18885 C CA  . THR C 180 ? 1.0612 1.0961 1.6841 0.1594  0.0100  -0.3184 180 THR C CA  
18886 C C   . THR C 180 ? 1.1573 1.1247 1.8689 0.1561  0.0279  -0.3234 180 THR C C   
18887 O O   . THR C 180 ? 1.2185 1.1146 1.9501 0.1450  0.0729  -0.2790 180 THR C O   
18888 C CB  . THR C 180 ? 1.1910 1.1412 1.6986 0.1979  0.0132  -0.2684 180 THR C CB  
18889 O OG1 . THR C 180 ? 1.3641 1.2051 1.8471 0.2033  0.0621  -0.2069 180 THR C OG1 
18890 C CG2 . THR C 180 ? 1.1050 1.1125 1.5339 0.1953  -0.0002 -0.2612 180 THR C CG2 
18898 N N   . LEU C 181 ? 1.1589 1.1484 1.9283 0.1649  -0.0043 -0.3791 181 LEU C N   
18899 C CA  . LEU C 181 ? 1.2085 1.1297 2.0681 0.1630  0.0053  -0.3929 181 LEU C CA  
18900 C C   . LEU C 181 ? 1.2467 1.1237 2.0920 0.2058  -0.0279 -0.4172 181 LEU C C   
18901 O O   . LEU C 181 ? 1.1869 1.1163 1.9768 0.2312  -0.0620 -0.4387 181 LEU C O   
18902 C CB  . LEU C 181 ? 1.1408 1.1462 2.1194 0.1262  -0.0062 -0.4563 181 LEU C CB  
18903 C CG  . LEU C 181 ? 1.0418 1.1245 2.0455 0.0884  0.0076  -0.4533 181 LEU C CG  
18904 C CD1 . LEU C 181 ? 1.0256 1.2114 2.1127 0.0675  -0.0275 -0.5326 181 LEU C CD1 
18905 C CD2 . LEU C 181 ? 1.0318 1.0406 2.0844 0.0674  0.0595  -0.4020 181 LEU C CD2 
18917 N N   . THR C 182 ? 1.2371 1.2957 1.6203 0.2193  0.0784  -0.3444 182 THR C N   
18918 C CA  . THR C 182 ? 1.2637 1.2913 1.6528 0.1875  0.0870  -0.3382 182 THR C CA  
18919 C C   . THR C 182 ? 1.2277 1.2309 1.6131 0.1605  0.0462  -0.3756 182 THR C C   
18920 O O   . THR C 182 ? 1.1880 1.2097 1.6025 0.1589  0.0150  -0.4050 182 THR C O   
18921 C CB  . THR C 182 ? 1.3251 1.4016 1.8382 0.1714  0.1239  -0.3031 182 THR C CB  
18922 O OG1 . THR C 182 ? 1.3662 1.4648 1.9923 0.1400  0.0937  -0.3215 182 THR C OG1 
18923 C CG2 . THR C 182 ? 1.3879 1.5319 1.9339 0.2118  0.1678  -0.2555 182 THR C CG2 
18931 N N   . LYS C 183 ? 1.2385 1.2054 1.5818 0.1473  0.0475  -0.3713 183 LYS C N   
18932 C CA  . LYS C 183 ? 1.3062 1.2617 1.6307 0.1414  0.0156  -0.4000 183 LYS C CA  
18933 C C   . LYS C 183 ? 1.2826 1.2491 1.7005 0.1317  -0.0041 -0.4328 183 LYS C C   
18934 O O   . LYS C 183 ? 1.2562 1.2264 1.6688 0.1409  -0.0435 -0.4702 183 LYS C O   
18935 C CB  . LYS C 183 ? 1.3727 1.3018 1.6446 0.1379  0.0283  -0.3779 183 LYS C CB  
18936 C CG  . LYS C 183 ? 1.3608 1.2889 1.6203 0.1492  0.0071  -0.4038 183 LYS C CG  
18937 C CD  . LYS C 183 ? 1.2790 1.2106 1.4573 0.1613  0.0101  -0.3681 183 LYS C CD  
18938 C CE  . LYS C 183 ? 1.2353 1.1588 1.4065 0.1779  0.0204  -0.3731 183 LYS C CE  
18939 N NZ  . LYS C 183 ? 1.1434 1.0854 1.2539 0.1867  0.0354  -0.3159 183 LYS C NZ  
18953 N N   . ASP C 184 ? 1.3060 1.2739 1.8135 0.1135  0.0145  -0.4161 184 ASP C N   
18954 C CA  . ASP C 184 ? 1.3519 1.3146 1.9649 0.0979  -0.0232 -0.4407 184 ASP C CA  
18955 C C   . ASP C 184 ? 1.3379 1.3381 2.0097 0.0968  -0.0524 -0.4539 184 ASP C C   
18956 O O   . ASP C 184 ? 1.3870 1.3664 2.0792 0.0975  -0.1082 -0.4979 184 ASP C O   
18957 C CB  . ASP C 184 ? 1.3733 1.3436 2.0984 0.0722  -0.0008 -0.3995 184 ASP C CB  
18958 C CG  . ASP C 184 ? 1.3779 1.3082 2.0504 0.0726  0.0249  -0.3888 184 ASP C CG  
18959 O OD1 . ASP C 184 ? 1.3834 1.2771 1.9509 0.0934  0.0129  -0.4188 184 ASP C OD1 
18960 O OD2 . ASP C 184 ? 1.3557 1.3018 2.0960 0.0558  0.0593  -0.3428 184 ASP C OD2 
18965 N N   . GLU C 185 ? 1.2881 1.3417 1.9784 0.1032  -0.0179 -0.4169 185 GLU C N   
18966 C CA  . GLU C 185 ? 1.3131 1.4122 2.0566 0.1074  -0.0397 -0.4223 185 GLU C CA  
18967 C C   . GLU C 185 ? 1.3140 1.3896 1.9579 0.1251  -0.0762 -0.4726 185 GLU C C   
18968 O O   . GLU C 185 ? 1.3220 1.4054 2.0087 0.1214  -0.1220 -0.5032 185 GLU C O   
18969 C CB  . GLU C 185 ? 1.3237 1.4862 2.0794 0.1307  0.0105  -0.3711 185 GLU C CB  
18970 C CG  . GLU C 185 ? 1.3450 1.5784 2.1964 0.1357  -0.0014 -0.3547 185 GLU C CG  
18971 C CD  . GLU C 185 ? 1.3657 1.6810 2.2504 0.1717  0.0572  -0.2881 185 GLU C CD  
18972 O OE1 . GLU C 185 ? 1.3823 1.6780 2.1607 0.2064  0.0975  -0.2766 185 GLU C OE1 
18973 O OE2 . GLU C 185 ? 1.3695 1.7721 2.3858 0.1711  0.0601  -0.2427 185 GLU C OE2 
18980 N N   . TYR C 186 ? 1.2969 1.3470 1.8156 0.1435  -0.0618 -0.4742 186 TYR C N   
18981 C CA  . TYR C 186 ? 1.2818 1.3228 1.7174 0.1595  -0.0962 -0.5052 186 TYR C CA  
18982 C C   . TYR C 186 ? 1.3114 1.3326 1.7451 0.1635  -0.1370 -0.5476 186 TYR C C   
18983 O O   . TYR C 186 ? 1.3616 1.3938 1.7807 0.1774  -0.1759 -0.5803 186 TYR C O   
18984 C CB  . TYR C 186 ? 1.2326 1.2509 1.5586 0.1707  -0.0832 -0.4809 186 TYR C CB  
18985 C CG  . TYR C 186 ? 1.1935 1.2189 1.4508 0.1853  -0.1188 -0.4913 186 TYR C CG  
18986 C CD1 . TYR C 186 ? 1.1692 1.2130 1.4230 0.1945  -0.1421 -0.5015 186 TYR C CD1 
18987 C CD2 . TYR C 186 ? 1.1933 1.2187 1.3942 0.1950  -0.1269 -0.4817 186 TYR C CD2 
18988 C CE1 . TYR C 186 ? 1.1770 1.2357 1.3794 0.2064  -0.1758 -0.5019 186 TYR C CE1 
18989 C CE2 . TYR C 186 ? 1.2005 1.2547 1.3513 0.2125  -0.1561 -0.4737 186 TYR C CE2 
18990 C CZ  . TYR C 186 ? 1.2071 1.2761 1.3620 0.2148  -0.1820 -0.4838 186 TYR C CZ  
18991 O OH  . TYR C 186 ? 1.2338 1.3388 1.3493 0.2307  -0.2123 -0.4674 186 TYR C OH  
19001 N N   . GLU C 187 ? 1.3278 1.3156 1.7672 0.1598  -0.1319 -0.5499 187 GLU C N   
19002 C CA  . GLU C 187 ? 1.4148 1.3693 1.8247 0.1830  -0.1752 -0.5960 187 GLU C CA  
19003 C C   . GLU C 187 ? 1.5189 1.4536 2.0202 0.1736  -0.2337 -0.6368 187 GLU C C   
19004 O O   . GLU C 187 ? 1.6708 1.5703 2.1284 0.2057  -0.2874 -0.6885 187 GLU C O   
19005 C CB  . GLU C 187 ? 1.4414 1.3575 1.8291 0.1881  -0.1568 -0.5875 187 GLU C CB  
19006 C CG  . GLU C 187 ? 1.4252 1.3594 1.7164 0.2029  -0.1144 -0.5467 187 GLU C CG  
19007 C CD  . GLU C 187 ? 1.4860 1.3883 1.7592 0.2101  -0.0937 -0.5348 187 GLU C CD  
19008 O OE1 . GLU C 187 ? 1.5335 1.3955 1.8803 0.1939  -0.1050 -0.5514 187 GLU C OE1 
19009 O OE2 . GLU C 187 ? 1.4972 1.4184 1.6920 0.2308  -0.0699 -0.5015 187 GLU C OE2 
19016 N N   . ARG C 188 ? 1.4406 1.4001 2.0673 0.1361  -0.2294 -0.6093 188 ARG C N   
19017 C CA  . ARG C 188 ? 1.4835 1.4260 2.2248 0.1171  -0.2959 -0.6320 188 ARG C CA  
19018 C C   . ARG C 188 ? 1.4964 1.4616 2.2229 0.1310  -0.3367 -0.6646 188 ARG C C   
19019 O O   . ARG C 188 ? 1.5228 1.4469 2.2868 0.1331  -0.4139 -0.7082 188 ARG C O   
19020 C CB  . ARG C 188 ? 1.4688 1.4565 2.3722 0.0732  -0.2748 -0.5683 188 ARG C CB  
19021 C CG  . ARG C 188 ? 1.4923 1.4512 2.4450 0.0538  -0.2556 -0.5379 188 ARG C CG  
19022 C CD  . ARG C 188 ? 1.5177 1.5166 2.6686 0.0090  -0.2705 -0.4758 188 ARG C CD  
19023 N NE  . ARG C 188 ? 1.5696 1.5168 2.7810 -0.0123 -0.2853 -0.4604 188 ARG C NE  
19024 C CZ  . ARG C 188 ? 1.6771 1.5273 2.9207 -0.0201 -0.3755 -0.5062 188 ARG C CZ  
19025 N NH1 . ARG C 188 ? 1.7567 1.5515 2.9711 -0.0047 -0.4595 -0.5726 188 ARG C NH1 
19026 N NH2 . ARG C 188 ? 1.7144 1.5153 3.0126 -0.0380 -0.3877 -0.4881 188 ARG C NH2 
19040 N N   . HIS C 189 ? 1.4665 1.4865 2.1365 0.1424  -0.2956 -0.6462 189 HIS C N   
19041 C CA  . HIS C 189 ? 1.4965 1.5485 2.1645 0.1521  -0.3267 -0.6670 189 HIS C CA  
19042 C C   . HIS C 189 ? 1.5434 1.5915 2.0678 0.1939  -0.3335 -0.6981 189 HIS C C   
19043 O O   . HIS C 189 ? 1.5874 1.6267 2.0209 0.2123  -0.3014 -0.6853 189 HIS C O   
19044 C CB  . HIS C 189 ? 1.3873 1.5076 2.1083 0.1403  -0.2819 -0.6173 189 HIS C CB  
19045 C CG  . HIS C 189 ? 1.2804 1.4343 2.1381 0.1114  -0.2565 -0.5629 189 HIS C CG  
19046 N ND1 . HIS C 189 ? 1.2839 1.4516 2.2938 0.0807  -0.3043 -0.5504 189 HIS C ND1 
19047 C CD2 . HIS C 189 ? 1.2198 1.4024 2.0905 0.1113  -0.1920 -0.5090 189 HIS C CD2 
19048 C CE1 . HIS C 189 ? 1.2508 1.4695 2.3739 0.0612  -0.2646 -0.4805 189 HIS C CE1 
19049 N NE2 . HIS C 189 ? 1.2245 1.4540 2.2570 0.0843  -0.1925 -0.4581 189 HIS C NE2 
19057 N N   . ASN C 190 ? 1.5493 1.6149 2.0637 0.2091  -0.3765 -0.7291 190 ASN C N   
19058 C CA  . ASN C 190 ? 1.6302 1.7054 2.0234 0.2551  -0.3928 -0.7543 190 ASN C CA  
19059 C C   . ASN C 190 ? 1.6494 1.7812 2.0133 0.2578  -0.3752 -0.7289 190 ASN C C   
19060 O O   . ASN C 190 ? 1.6947 1.8491 1.9725 0.2788  -0.3542 -0.7030 190 ASN C O   
19061 C CB  . ASN C 190 ? 1.7149 1.7592 2.0972 0.2838  -0.4640 -0.8054 190 ASN C CB  
19062 C CG  . ASN C 190 ? 1.8054 1.8560 2.0516 0.3476  -0.4663 -0.8085 190 ASN C CG  
19063 O OD1 . ASN C 190 ? 1.8594 1.8798 2.0532 0.3713  -0.4547 -0.8070 190 ASN C OD1 
19064 N ND2 . ASN C 190 ? 1.8338 1.9312 2.0255 0.3814  -0.4814 -0.8114 190 ASN C ND2 
19071 N N   . SER C 191 ? 1.5696 1.7271 2.0100 0.2379  -0.3881 -0.7286 191 SER C N   
19072 C CA  . SER C 191 ? 1.5042 1.7052 1.9158 0.2455  -0.3817 -0.7113 191 SER C CA  
19073 C C   . SER C 191 ? 1.3864 1.5959 1.8171 0.2300  -0.3339 -0.6656 191 SER C C   
19074 O O   . SER C 191 ? 1.3632 1.5713 1.8676 0.2117  -0.3081 -0.6474 191 SER C O   
19075 C CB  . SER C 191 ? 1.5374 1.7636 2.0071 0.2448  -0.4273 -0.7398 191 SER C CB  
19076 O OG  . SER C 191 ? 1.5365 1.7835 2.1213 0.2162  -0.4154 -0.7172 191 SER C OG  
19082 N N   . TYR C 192 ? 1.3143 1.5318 1.6761 0.2434  -0.3286 -0.6438 192 TYR C N   
19083 C CA  . TYR C 192 ? 1.2308 1.4346 1.5767 0.2449  -0.2997 -0.6098 192 TYR C CA  
19084 C C   . TYR C 192 ? 1.2837 1.4991 1.5945 0.2614  -0.3260 -0.6057 192 TYR C C   
19085 O O   . TYR C 192 ? 1.1773 1.4007 1.4393 0.2666  -0.3552 -0.6014 192 TYR C O   
19086 C CB  . TYR C 192 ? 1.2050 1.3678 1.4855 0.2422  -0.2786 -0.5802 192 TYR C CB  
19087 C CG  . TYR C 192 ? 1.2208 1.3684 1.5379 0.2275  -0.2468 -0.5792 192 TYR C CG  
19088 C CD1 . TYR C 192 ? 1.2139 1.3560 1.5710 0.2247  -0.2096 -0.5595 192 TYR C CD1 
19089 C CD2 . TYR C 192 ? 1.2361 1.3779 1.5439 0.2249  -0.2545 -0.5949 192 TYR C CD2 
19090 C CE1 . TYR C 192 ? 1.2317 1.3649 1.6332 0.2086  -0.1823 -0.5510 192 TYR C CE1 
19091 C CE2 . TYR C 192 ? 1.2487 1.3678 1.5919 0.2117  -0.2319 -0.5946 192 TYR C CE2 
19092 C CZ  . TYR C 192 ? 1.2422 1.3581 1.6397 0.1979  -0.1964 -0.5703 192 TYR C CZ  
19093 O OH  . TYR C 192 ? 1.2428 1.3414 1.6862 0.1821  -0.1753 -0.5624 192 TYR C OH  
19103 N N   . THR C 193 ? 1.3038 1.5270 1.6410 0.2754  -0.3151 -0.6002 193 THR C N   
19104 C CA  . THR C 193 ? 1.3716 1.6072 1.6906 0.2947  -0.3441 -0.6040 193 THR C CA  
19105 C C   . THR C 193 ? 1.3259 1.5236 1.5966 0.3287  -0.3334 -0.5861 193 THR C C   
19106 O O   . THR C 193 ? 1.0456 1.2372 1.3245 0.3440  -0.2935 -0.5726 193 THR C O   
19107 C CB  . THR C 193 ? 0.9897 1.2861 1.3976 0.2916  -0.3536 -0.6249 193 THR C CB  
19108 O OG1 . THR C 193 ? 0.9847 1.2956 1.4144 0.2720  -0.3793 -0.6516 193 THR C OG1 
19109 C CG2 . THR C 193 ? 1.1899 1.5028 1.5806 0.3138  -0.3809 -0.6277 193 THR C CG2 
19117 N N   . CYS C 194 ? 1.2220 1.3926 1.4374 0.3476  -0.3743 -0.5853 194 CYS C N   
19118 C CA  . CYS C 194 ? 1.2412 1.3499 1.3835 0.3932  -0.3864 -0.5782 194 CYS C CA  
19119 C C   . CYS C 194 ? 1.2683 1.4002 1.4179 0.4219  -0.4122 -0.5906 194 CYS C C   
19120 O O   . CYS C 194 ? 1.2548 1.3778 1.3898 0.4081  -0.4623 -0.5909 194 CYS C O   
19121 C CB  . CYS C 194 ? 1.2625 1.2807 1.3186 0.3860  -0.4340 -0.5589 194 CYS C CB  
19122 S SG  . CYS C 194 ? 1.4628 1.3682 1.4102 0.4452  -0.4929 -0.5611 194 CYS C SG  
19127 N N   . GLU C 195 ? 1.2926 1.4648 1.4701 0.4650  -0.3763 -0.5918 195 GLU C N   
19128 C CA  . GLU C 195 ? 1.3173 1.5314 1.5183 0.4956  -0.3896 -0.5993 195 GLU C CA  
19129 C C   . GLU C 195 ? 1.4472 1.5909 1.5427 0.5738  -0.4072 -0.6018 195 GLU C C   
19130 O O   . GLU C 195 ? 1.3370 1.4758 1.3963 0.6296  -0.3667 -0.5911 195 GLU C O   
19131 C CB  . GLU C 195 ? 1.2597 1.5867 1.5836 0.4932  -0.3406 -0.5863 195 GLU C CB  
19132 C CG  . GLU C 195 ? 1.1736 1.5579 1.5948 0.4309  -0.3579 -0.5989 195 GLU C CG  
19133 C CD  . GLU C 195 ? 1.1486 1.6339 1.7049 0.4252  -0.3314 -0.5785 195 GLU C CD  
19134 O OE1 . GLU C 195 ? 1.1203 1.6336 1.7640 0.3780  -0.3305 -0.5778 195 GLU C OE1 
19135 O OE2 . GLU C 195 ? 1.1884 1.7236 1.7670 0.4705  -0.3173 -0.5585 195 GLU C OE2 
19142 N N   . ALA C 196 ? 1.3287 1.4184 1.3719 0.5854  -0.4711 -0.6146 196 ALA C N   
19143 C CA  . ALA C 196 ? 1.4493 1.4470 1.3790 0.6655  -0.5103 -0.6262 196 ALA C CA  
19144 C C   . ALA C 196 ? 1.8739 1.9323 1.8315 0.7111  -0.5066 -0.6324 196 ALA C C   
19145 O O   . ALA C 196 ? 1.4012 1.5201 1.4360 0.6647  -0.5225 -0.6331 196 ALA C O   
19146 C CB  . ALA C 196 ? 1.5054 1.3753 1.3564 0.6453  -0.6047 -0.6285 196 ALA C CB  
19152 N N   . THR C 197 ? 1.9910 2.0380 1.8797 0.8104  -0.4846 -0.6346 197 THR C N   
19153 C CA  . THR C 197 ? 1.9563 2.0555 1.8529 0.8736  -0.4807 -0.6357 197 THR C CA  
19154 C C   . THR C 197 ? 2.0902 2.0491 1.8192 0.9414  -0.5469 -0.6511 197 THR C C   
19155 O O   . THR C 197 ? 2.2409 2.1378 1.8523 0.9904  -0.5381 -0.6401 197 THR C O   
19156 C CB  . THR C 197 ? 1.8720 2.1135 1.8420 0.9262  -0.3871 -0.5988 197 THR C CB  
19157 O OG1 . THR C 197 ? 2.0050 2.2028 1.8613 0.9874  -0.3522 -0.5774 197 THR C OG1 
19158 C CG2 . THR C 197 ? 1.6938 2.0544 1.8288 0.8304  -0.3376 -0.5697 197 THR C CG2 
19166 N N   . HIS C 198 ? 1.1292 1.7631 1.7270 0.0915  -0.2183 -0.5199 198 HIS C N   
19167 C CA  . HIS C 198 ? 1.1476 1.7608 1.6777 0.1164  -0.1799 -0.5066 198 HIS C CA  
19168 C C   . HIS C 198 ? 1.2429 1.8752 1.8045 0.1779  -0.2352 -0.5430 198 HIS C C   
19169 O O   . HIS C 198 ? 1.3706 1.9971 1.9571 0.2077  -0.3079 -0.5739 198 HIS C O   
19170 C CB  . HIS C 198 ? 1.1480 1.6362 1.4910 0.1303  -0.1560 -0.4770 198 HIS C CB  
19171 C CG  . HIS C 198 ? 1.0337 1.4949 1.3101 0.1318  -0.1060 -0.4502 198 HIS C CG  
19172 N ND1 . HIS C 198 ? 0.9484 1.4830 1.3068 0.0953  -0.0536 -0.4382 198 HIS C ND1 
19173 C CD2 . HIS C 198 ? 1.0760 1.4375 1.2049 0.1639  -0.1039 -0.4319 198 HIS C CD2 
19174 C CE1 . HIS C 198 ? 0.9675 1.4419 1.2280 0.1077  -0.0246 -0.4178 198 HIS C CE1 
19175 N NE2 . HIS C 198 ? 1.0603 1.4298 1.1853 0.1470  -0.0561 -0.4118 198 HIS C NE2 
19183 N N   . LYS C 199 ? 1.2176 1.8678 1.7760 0.1986  -0.2038 -0.5400 199 LYS C N   
19184 C CA  . LYS C 199 ? 1.2397 1.9141 1.8386 0.2611  -0.2533 -0.5743 199 LYS C CA  
19185 C C   . LYS C 199 ? 1.3514 1.9036 1.8077 0.3188  -0.3175 -0.5863 199 LYS C C   
19186 O O   . LYS C 199 ? 1.4199 1.9855 1.9182 0.3684  -0.3848 -0.6192 199 LYS C O   
19187 C CB  . LYS C 199 ? 1.2585 1.9616 1.8646 0.2772  -0.2033 -0.5700 199 LYS C CB  
19188 C CG  . LYS C 199 ? 1.2141 2.0544 1.9715 0.2317  -0.1441 -0.5645 199 LYS C CG  
19189 C CD  . LYS C 199 ? 1.2593 2.1128 1.9997 0.2573  -0.0949 -0.5654 199 LYS C CD  
19190 C CE  . LYS C 199 ? 1.1921 2.1861 2.0743 0.2148  -0.0316 -0.5597 199 LYS C CE  
19191 N NZ  . LYS C 199 ? 1.2217 2.2204 2.0716 0.2444  0.0193  -0.5645 199 LYS C NZ  
19205 N N   . THR C 200 ? 1.4243 1.8610 1.7147 0.3124  -0.2990 -0.5573 200 THR C N   
19206 C CA  . THR C 200 ? 1.5876 1.9049 1.7246 0.3664  -0.3502 -0.5608 200 THR C CA  
19207 C C   . THR C 200 ? 1.6914 1.9911 1.8328 0.3924  -0.4297 -0.5927 200 THR C C   
19208 O O   . THR C 200 ? 1.9039 2.1392 1.9730 0.4476  -0.4936 -0.6109 200 THR C O   
19209 C CB  . THR C 200 ? 1.6095 1.8215 1.5770 0.3478  -0.3052 -0.5147 200 THR C CB  
19210 O OG1 . THR C 200 ? 1.7560 1.8551 1.5707 0.3986  -0.3522 -0.5123 200 THR C OG1 
19211 C CG2 . THR C 200 ? 1.5481 1.7637 1.5116 0.3027  -0.2793 -0.4991 200 THR C CG2 
19219 N N   . SER C 201 ? 1.5819 1.9287 1.8007 0.3540  -0.4332 -0.6003 201 SER C N   
19220 C CA  . SER C 201 ? 1.5989 1.9202 1.8193 0.3757  -0.5142 -0.6332 201 SER C CA  
19221 C C   . SER C 201 ? 1.4348 1.8748 1.8530 0.3385  -0.5363 -0.6540 201 SER C C   
19222 O O   . SER C 201 ? 1.2692 1.7806 1.7758 0.2815  -0.4778 -0.6343 201 SER C O   
19223 C CB  . SER C 201 ? 1.7039 1.9211 1.7699 0.3724  -0.5087 -0.6201 201 SER C CB  
19224 O OG  . SER C 201 ? 1.8330 1.9434 1.7164 0.4076  -0.4968 -0.5973 201 SER C OG  
19230 N N   . THR C 202 ? 1.5003 1.9590 1.9877 0.3682  -0.6254 -0.6905 202 THR C N   
19231 C CA  . THR C 202 ? 1.4356 2.0060 2.1171 0.3313  -0.6600 -0.7071 202 THR C CA  
19232 C C   . THR C 202 ? 1.4785 2.0079 2.1405 0.2938  -0.6781 -0.7097 202 THR C C   
19233 O O   . THR C 202 ? 1.4262 2.0449 2.2451 0.2450  -0.6890 -0.7111 202 THR C O   
19234 C CB  . THR C 202 ? 1.4727 2.0750 2.2408 0.3741  -0.7584 -0.7424 202 THR C CB  
19235 O OG1 . THR C 202 ? 1.4242 2.1478 2.3981 0.3311  -0.7907 -0.7509 202 THR C OG1 
19236 C CG2 . THR C 202 ? 1.5974 2.0593 2.2071 0.4203  -0.8434 -0.7667 202 THR C CG2 
19244 N N   . SER C 203 ? 1.6011 1.9978 2.0743 0.3171  -0.6825 -0.7094 203 SER C N   
19245 C CA  . SER C 203 ? 1.6719 2.0143 2.1060 0.2939  -0.7002 -0.7168 203 SER C CA  
19246 C C   . SER C 203 ? 1.5936 1.9355 1.9898 0.2506  -0.6020 -0.6781 203 SER C C   
19247 O O   . SER C 203 ? 1.6379 1.9096 1.8840 0.2712  -0.5496 -0.6544 203 SER C O   
19248 C CB  . SER C 203 ? 1.8722 2.0723 2.1176 0.3514  -0.7615 -0.7416 203 SER C CB  
19249 O OG  . SER C 203 ? 1.9851 2.1130 2.0659 0.3906  -0.7198 -0.7207 203 SER C OG  
19255 N N   . PRO C 204 ? 1.4974 1.9146 2.0251 0.1888  -0.5771 -0.6665 204 PRO C N   
19256 C CA  . PRO C 204 ? 1.4478 1.8679 1.9479 0.1457  -0.4860 -0.6267 204 PRO C CA  
19257 C C   . PRO C 204 ? 1.5471 1.8453 1.8595 0.1740  -0.4672 -0.6198 204 PRO C C   
19258 O O   . PRO C 204 ? 1.6696 1.8923 1.9148 0.2009  -0.5245 -0.6494 204 PRO C O   
19259 C CB  . PRO C 204 ? 1.3798 1.8764 2.0413 0.0811  -0.4951 -0.6249 204 PRO C CB  
19260 C CG  . PRO C 204 ? 1.3792 1.9630 2.1950 0.0794  -0.5617 -0.6494 204 PRO C CG  
19261 C CD  . PRO C 204 ? 1.4747 1.9816 2.1902 0.1510  -0.6336 -0.6841 204 PRO C CD  
19269 N N   . ILE C 205 ? 1.4908 1.7696 1.7165 0.1690  -0.3867 -0.5796 205 ILE C N   
19270 C CA  . ILE C 205 ? 1.5307 1.7170 1.5994 0.1881  -0.3538 -0.5624 205 ILE C CA  
19271 C C   . ILE C 205 ? 1.4984 1.6986 1.6258 0.1440  -0.3337 -0.5552 205 ILE C C   
19272 O O   . ILE C 205 ? 1.3930 1.6738 1.6488 0.0841  -0.2974 -0.5330 205 ILE C O   
19273 C CB  . ILE C 205 ? 1.4780 1.6454 1.4509 0.1894  -0.2789 -0.5148 205 ILE C CB  
19274 C CG1 . ILE C 205 ? 1.5684 1.6977 1.4601 0.2406  -0.3104 -0.5240 205 ILE C CG1 
19275 C CG2 . ILE C 205 ? 1.4930 1.5906 1.3339 0.1984  -0.2337 -0.4871 205 ILE C CG2 
19276 C CD1 . ILE C 205 ? 1.6091 1.6864 1.3680 0.2512  -0.2541 -0.4776 205 ILE C CD1 
19288 N N   . VAL C 206 ? 1.5551 1.6723 1.5825 0.1757  -0.3577 -0.5742 206 VAL C N   
19289 C CA  . VAL C 206 ? 1.4876 1.5998 1.5623 0.1459  -0.3561 -0.5775 206 VAL C CA  
19290 C C   . VAL C 206 ? 1.4986 1.5392 1.4274 0.1748  -0.3031 -0.5565 206 VAL C C   
19291 O O   . VAL C 206 ? 1.6087 1.5779 1.3827 0.2332  -0.3050 -0.5623 206 VAL C O   
19292 C CB  . VAL C 206 ? 1.5666 1.6457 1.6809 0.1604  -0.4550 -0.6323 206 VAL C CB  
19293 C CG1 . VAL C 206 ? 1.5256 1.6139 1.7293 0.1152  -0.4602 -0.6329 206 VAL C CG1 
19294 C CG2 . VAL C 206 ? 1.5546 1.7011 1.7909 0.1491  -0.5148 -0.6527 206 VAL C CG2 
19304 N N   . LYS C 207 ? 1.3983 1.4624 1.3793 0.1337  -0.2549 -0.5288 207 LYS C N   
19305 C CA  . LYS C 207 ? 1.4186 1.4299 1.2894 0.1589  -0.2037 -0.5078 207 LYS C CA  
19306 C C   . LYS C 207 ? 1.3750 1.3888 1.3295 0.1280  -0.2117 -0.5153 207 LYS C C   
19307 O O   . LYS C 207 ? 1.2741 1.3577 1.3701 0.0607  -0.1984 -0.4933 207 LYS C O   
19308 C CB  . LYS C 207 ? 1.3555 1.3997 1.1943 0.1374  -0.1148 -0.4434 207 LYS C CB  
19309 C CG  . LYS C 207 ? 1.4034 1.4355 1.1551 0.1651  -0.1082 -0.4307 207 LYS C CG  
19310 C CD  . LYS C 207 ? 1.5482 1.4935 1.1228 0.2401  -0.1243 -0.4478 207 LYS C CD  
19311 C CE  . LYS C 207 ? 1.5621 1.4895 1.0282 0.2522  -0.0463 -0.3925 207 LYS C CE  
19312 N NZ  . LYS C 207 ? 1.6577 1.5289 0.9665 0.3037  -0.0485 -0.3835 207 LYS C NZ  
19326 N N   . SER C 208 ? 1.4728 1.4065 1.3352 0.1785  -0.2349 -0.5468 208 SER C N   
19327 C CA  . SER C 208 ? 1.5082 1.4254 1.4426 0.1580  -0.2598 -0.5636 208 SER C CA  
19328 C C   . SER C 208 ? 1.5915 1.4353 1.3985 0.2175  -0.2301 -0.5698 208 SER C C   
19329 O O   . SER C 208 ? 1.6613 1.4674 1.3207 0.2763  -0.1961 -0.5648 208 SER C O   
19330 C CB  . SER C 208 ? 1.5903 1.4778 1.5862 0.1559  -0.3654 -0.6211 208 SER C CB  
19331 O OG  . SER C 208 ? 1.7836 1.5754 1.6349 0.2323  -0.4202 -0.6717 208 SER C OG  
19337 N N   . PHE C 209 ? 1.5757 1.4011 1.4435 0.2022  -0.2436 -0.5797 209 PHE C N   
19338 C CA  . PHE C 209 ? 1.6780 1.4348 1.4438 0.2621  -0.2214 -0.5929 209 PHE C CA  
19339 C C   . PHE C 209 ? 1.7319 1.4360 1.5660 0.2529  -0.2935 -0.6359 209 PHE C C   
19340 O O   . PHE C 209 ? 1.7033 1.4385 1.6752 0.1887  -0.3488 -0.6415 209 PHE C O   
19341 C CB  . PHE C 209 ? 1.5727 1.3846 1.3465 0.2468  -0.1193 -0.5267 209 PHE C CB  
19342 C CG  . PHE C 209 ? 1.3977 1.2756 1.3383 0.1629  -0.1031 -0.4876 209 PHE C CG  
19343 C CD1 . PHE C 209 ? 1.2442 1.2070 1.2844 0.0892  -0.0775 -0.4428 209 PHE C CD1 
19344 C CD2 . PHE C 209 ? 1.3937 1.2426 1.3838 0.1604  -0.1151 -0.4963 209 PHE C CD2 
19345 C CE1 . PHE C 209 ? 1.1231 1.1420 1.3035 0.0117  -0.0625 -0.4057 209 PHE C CE1 
19346 C CE2 . PHE C 209 ? 1.2639 1.1682 1.4015 0.0810  -0.1040 -0.4572 209 PHE C CE2 
19347 C CZ  . PHE C 209 ? 1.1309 1.1210 1.3607 0.0052  -0.0766 -0.4109 209 PHE C CZ  
19357 N N   . ASN C 210 ? 1.8355 1.4587 1.5711 0.3188  -0.2927 -0.6650 210 ASN C N   
19358 C CA  . ASN C 210 ? 1.9004 1.4536 1.6810 0.3203  -0.3616 -0.7075 210 ASN C CA  
19359 C C   . ASN C 210 ? 1.9122 1.4695 1.7031 0.3329  -0.2970 -0.6792 210 ASN C C   
19360 O O   . ASN C 210 ? 1.9934 1.5394 1.6653 0.3998  -0.2284 -0.6692 210 ASN C O   
19361 C CB  . ASN C 210 ? 2.0927 1.5182 1.7326 0.4004  -0.4442 -0.7859 210 ASN C CB  
19362 C CG  . ASN C 210 ? 2.1527 1.5670 1.8343 0.3713  -0.5404 -0.8189 210 ASN C CG  
19363 O OD1 . ASN C 210 ? 2.0681 1.5447 1.9166 0.2886  -0.5768 -0.8012 210 ASN C OD1 
19364 N ND2 . ASN C 210 ? 2.2625 1.6223 1.8103 0.4302  -0.5689 -0.8392 210 ASN C ND2 
19371 N N   . ARG C 211 ? 1.8916 1.4692 1.8291 0.2677  -0.3196 -0.6631 211 ARG C N   
19372 C CA  . ARG C 211 ? 1.8923 1.4872 1.8683 0.2669  -0.2602 -0.6271 211 ARG C CA  
19373 C C   . ARG C 211 ? 2.1330 1.6273 1.9778 0.3701  -0.2630 -0.6752 211 ARG C C   
19374 O O   . ARG C 211 ? 2.1361 1.6549 1.9262 0.4163  -0.1789 -0.6462 211 ARG C O   
19375 C CB  . ARG C 211 ? 1.7768 1.3945 1.9270 0.1776  -0.3026 -0.6074 211 ARG C CB  
19376 C CG  . ARG C 211 ? 1.7621 1.3943 1.9687 0.1692  -0.2537 -0.5687 211 ARG C CG  
19377 C CD  . ARG C 211 ? 1.6941 1.3474 2.0690 0.0727  -0.3004 -0.5444 211 ARG C CD  
19378 N NE  . ARG C 211 ? 1.7923 1.3486 2.1852 0.0752  -0.4125 -0.6043 211 ARG C NE  
19379 C CZ  . ARG C 211 ? 1.9157 1.3689 2.2758 0.1261  -0.4569 -0.6442 211 ARG C CZ  
19380 N NH1 . ARG C 211 ? 1.9651 1.4092 2.2787 0.1832  -0.3926 -0.6310 211 ARG C NH1 
19381 N NH2 . ARG C 211 ? 2.0085 1.3669 2.3848 0.1211  -0.5682 -0.6968 211 ARG C NH2 
19395 N N   . ASN C 212 ? 2.3454 1.7258 2.1388 0.4087  -0.3602 -0.7484 212 ASN C N   
19396 C CA  . ASN C 212 ? 2.5674 1.8385 2.2261 0.5129  -0.3690 -0.8025 212 ASN C CA  
19397 C C   . ASN C 212 ? 2.6934 1.9605 2.1695 0.6042  -0.2980 -0.8081 212 ASN C C   
19398 O O   . ASN C 212 ? 2.8232 2.0734 2.2142 0.6804  -0.2359 -0.8094 212 ASN C O   
19399 C CB  . ASN C 212 ? 2.6925 1.8392 2.3222 0.5288  -0.4951 -0.8733 212 ASN C CB  
19400 C CG  . ASN C 212 ? 2.8329 1.8919 2.3601 0.6103  -0.5015 -0.8991 212 ASN C CG  
19401 O OD1 . ASN C 212 ? 2.8094 1.8744 2.3448 0.6441  -0.4417 -0.8888 212 ASN C OD1 
19402 N ND2 . ASN C 212 ? 2.9599 1.9393 2.3947 0.6442  -0.5749 -0.9323 212 ASN C ND2 
19409 N N   . GLU C 213 ? 2.6549 1.9421 2.0723 0.5977  -0.3044 -0.8079 213 GLU C N   
19410 C CA  . GLU C 213 ? 2.8282 2.1097 2.0737 0.6688  -0.2516 -0.8003 213 GLU C CA  
19411 C C   . GLU C 213 ? 2.7740 2.1544 2.0067 0.6749  -0.1299 -0.7383 213 GLU C C   
19412 O O   . GLU C 213 ? 2.6022 2.0808 1.9834 0.5969  -0.0862 -0.6745 213 GLU C O   
19413 C CB  . GLU C 213 ? 2.8416 2.1090 2.0426 0.6520  -0.3115 -0.8119 213 GLU C CB  
19414 C CG  . GLU C 213 ? 2.9266 2.1191 2.1689 0.6312  -0.4338 -0.8569 213 GLU C CG  
19415 C CD  . GLU C 213 ? 3.0423 2.2071 2.2055 0.6441  -0.4877 -0.8680 213 GLU C CD  
19416 O OE1 . GLU C 213 ? 3.0531 2.2491 2.1226 0.6697  -0.4319 -0.8426 213 GLU C OE1 
19417 O OE2 . GLU C 213 ? 3.1088 2.2210 2.3086 0.6277  -0.5878 -0.8976 213 GLU C OE2 
19424 N N   . CYS C 214 ? 2.9157 2.3006 2.0065 0.7319  -0.0731 -0.7158 214 CYS C N   
19425 C CA  . CYS C 214 ? 2.9177 2.3969 1.9841 0.7356  0.0388  -0.6465 214 CYS C CA  
19426 C C   . CYS C 214 ? 3.1177 2.5891 2.0370 0.7743  0.0626  -0.6253 214 CYS C C   
19427 O O   . CYS C 214 ? 3.1735 2.6255 2.0512 0.7576  0.0177  -0.6337 214 CYS C O   
19428 C CB  . CYS C 214 ? 2.8815 2.4017 1.9882 0.7637  0.1154  -0.6169 214 CYS C CB  
19429 S SG  . CYS C 214 ? 2.8893 2.5452 2.0078 0.7502  0.2519  -0.5125 214 CYS C SG  
19435 N N   . GLN D 1   ? 1.4119 1.2659 1.2284 -0.0970 0.0477  -0.0728 1   GLN D N   
19436 C CA  . GLN D 1   ? 1.3312 1.2568 1.1690 -0.1052 0.0433  -0.0660 1   GLN D CA  
19437 C C   . GLN D 1   ? 1.1901 1.1688 1.0414 -0.0939 0.0239  -0.0775 1   GLN D C   
19438 O O   . GLN D 1   ? 1.1665 1.2029 1.0408 -0.1104 0.0173  -0.0815 1   GLN D O   
19439 C CB  . GLN D 1   ? 1.4161 1.3589 1.2690 -0.1484 0.0533  -0.0695 1   GLN D CB  
19440 C CG  . GLN D 1   ? 1.5559 1.4443 1.3934 -0.1632 0.0733  -0.0542 1   GLN D CG  
19441 C CD  . GLN D 1   ? 1.6893 1.5866 1.5376 -0.2132 0.0839  -0.0605 1   GLN D CD  
19442 O OE1 . GLN D 1   ? 1.7212 1.6466 1.5826 -0.2398 0.0769  -0.0818 1   GLN D OE1 
19443 N NE2 . GLN D 1   ? 1.7675 1.6440 1.6085 -0.2296 0.1008  -0.0413 1   GLN D NE2 
19454 N N   . VAL D 2   ? 1.1056 1.0664 0.9424 -0.0660 0.0146  -0.0804 2   VAL D N   
19455 C CA  . VAL D 2   ? 1.0047 1.0070 0.8483 -0.0543 -0.0037 -0.0879 2   VAL D CA  
19456 C C   . VAL D 2   ? 0.9731 1.0067 0.8212 -0.0314 -0.0076 -0.0725 2   VAL D C   
19457 O O   . VAL D 2   ? 0.9790 0.9896 0.8114 -0.0125 -0.0003 -0.0602 2   VAL D O   
19458 C CB  . VAL D 2   ? 0.9938 0.9664 0.8193 -0.0378 -0.0105 -0.0985 2   VAL D CB  
19459 C CG1 . VAL D 2   ? 0.9612 0.9750 0.7899 -0.0288 -0.0292 -0.1032 2   VAL D CG1 
19460 C CG2 . VAL D 2   ? 1.0182 0.9562 0.8390 -0.0584 -0.0032 -0.1180 2   VAL D CG2 
19470 N N   . GLN D 3   ? 0.9758 1.0614 0.8441 -0.0328 -0.0187 -0.0731 3   GLN D N   
19471 C CA  . GLN D 3   ? 0.9590 1.0704 0.8333 -0.0099 -0.0206 -0.0618 3   GLN D CA  
19472 C C   . GLN D 3   ? 0.8910 1.0325 0.7738 -0.0011 -0.0395 -0.0645 3   GLN D C   
19473 O O   . GLN D 3   ? 0.8877 1.0634 0.7884 -0.0188 -0.0494 -0.0691 3   GLN D O   
19474 C CB  . GLN D 3   ? 1.0457 1.1943 0.9441 -0.0182 -0.0086 -0.0530 3   GLN D CB  
19475 C CG  . GLN D 3   ? 1.1455 1.2669 1.0344 -0.0312 0.0108  -0.0466 3   GLN D CG  
19476 C CD  . GLN D 3   ? 1.2388 1.4077 1.1534 -0.0429 0.0232  -0.0385 3   GLN D CD  
19477 O OE1 . GLN D 3   ? 1.2574 1.4778 1.1966 -0.0307 0.0191  -0.0363 3   GLN D OE1 
19478 N NE2 . GLN D 3   ? 1.2994 1.4518 1.2096 -0.0664 0.0391  -0.0332 3   GLN D NE2 
19487 N N   . LEU D 4   ? 0.7977 0.9266 0.6655 0.0236  -0.0446 -0.0607 4   LEU D N   
19488 C CA  . LEU D 4   ? 0.8318 0.9806 0.7045 0.0340  -0.0611 -0.0592 4   LEU D CA  
19489 C C   . LEU D 4   ? 0.8511 1.0112 0.7330 0.0562  -0.0553 -0.0504 4   LEU D C   
19490 O O   . LEU D 4   ? 0.8635 0.9952 0.7237 0.0718  -0.0470 -0.0504 4   LEU D O   
19491 C CB  . LEU D 4   ? 0.8746 0.9944 0.7189 0.0402  -0.0716 -0.0649 4   LEU D CB  
19492 C CG  . LEU D 4   ? 0.9120 1.0168 0.7452 0.0242  -0.0734 -0.0765 4   LEU D CG  
19493 C CD1 . LEU D 4   ? 0.9257 1.0181 0.7363 0.0310  -0.0849 -0.0811 4   LEU D CD1 
19494 C CD2 . LEU D 4   ? 0.9291 1.0642 0.7813 -0.0009 -0.0787 -0.0834 4   LEU D CD2 
19506 N N   . GLN D 5   ? 0.8781 1.0820 0.7922 0.0581  -0.0591 -0.0437 5   GLN D N   
19507 C CA  . GLN D 5   ? 0.9581 1.1766 0.8875 0.0827  -0.0514 -0.0368 5   GLN D CA  
19508 C C   . GLN D 5   ? 0.9754 1.1884 0.9040 0.1002  -0.0673 -0.0318 5   GLN D C   
19509 O O   . GLN D 5   ? 1.0085 1.2526 0.9563 0.0936  -0.0837 -0.0244 5   GLN D O   
19510 C CB  . GLN D 5   ? 1.0759 1.3524 1.0469 0.0774  -0.0437 -0.0301 5   GLN D CB  
19511 C CG  . GLN D 5   ? 1.2352 1.5151 1.2061 0.0579  -0.0255 -0.0329 5   GLN D CG  
19512 C CD  . GLN D 5   ? 1.3735 1.7197 1.3868 0.0477  -0.0183 -0.0263 5   GLN D CD  
19513 O OE1 . GLN D 5   ? 1.4176 1.8136 1.4627 0.0496  -0.0312 -0.0197 5   GLN D OE1 
19514 N NE2 . GLN D 5   ? 1.4324 1.7843 1.4467 0.0358  0.0017  -0.0260 5   GLN D NE2 
19523 N N   . GLN D 6   ? 0.9432 1.1161 0.8473 0.1200  -0.0628 -0.0352 6   GLN D N   
19524 C CA  . GLN D 6   ? 0.8893 1.0428 0.7863 0.1351  -0.0758 -0.0306 6   GLN D CA  
19525 C C   . GLN D 6   ? 0.8455 1.0109 0.7684 0.1638  -0.0671 -0.0244 6   GLN D C   
19526 O O   . GLN D 6   ? 0.7973 0.9764 0.7324 0.1746  -0.0471 -0.0287 6   GLN D O   
19527 C CB  . GLN D 6   ? 0.8750 0.9744 0.7267 0.1356  -0.0763 -0.0401 6   GLN D CB  
19528 C CG  . GLN D 6   ? 0.8122 0.9032 0.6419 0.1129  -0.0881 -0.0444 6   GLN D CG  
19529 C CD  . GLN D 6   ? 0.7920 0.8418 0.5813 0.1130  -0.0912 -0.0515 6   GLN D CD  
19530 O OE1 . GLN D 6   ? 0.7465 0.7831 0.5141 0.1087  -0.0837 -0.0586 6   GLN D OE1 
19531 N NE2 . GLN D 6   ? 0.8126 0.8435 0.5914 0.1165  -0.1029 -0.0478 6   GLN D NE2 
19540 N N   . SER D 7   ? 0.8484 1.0083 0.7797 0.1772  -0.0814 -0.0134 7   SER D N   
19541 C CA  . SER D 7   ? 0.8594 1.0274 0.8191 0.2100  -0.0742 -0.0056 7   SER D CA  
19542 C C   . SER D 7   ? 0.8781 0.9918 0.8098 0.2296  -0.0546 -0.0213 7   SER D C   
19543 O O   . SER D 7   ? 0.8436 0.9181 0.7331 0.2157  -0.0500 -0.0354 7   SER D O   
19544 C CB  . SER D 7   ? 0.8648 1.0324 0.8368 0.2196  -0.0960 0.0140  7   SER D CB  
19545 O OG  . SER D 7   ? 0.8863 0.9879 0.8161 0.2174  -0.1038 0.0105  7   SER D OG  
19551 N N   . GLY D 8   ? 0.9631 1.0779 0.9191 0.2628  -0.0425 -0.0191 8   GLY D N   
19552 C CA  . GLY D 8   ? 0.9898 1.0579 0.9217 0.2820  -0.0201 -0.0378 8   GLY D CA  
19553 C C   . GLY D 8   ? 0.9950 0.9864 0.8868 0.2860  -0.0274 -0.0430 8   GLY D C   
19554 O O   . GLY D 8   ? 0.9677 0.9422 0.8520 0.2757  -0.0502 -0.0293 8   GLY D O   
19558 N N   . ALA D 9   ? 1.0429 0.9882 0.9059 0.2980  -0.0064 -0.0643 9   ALA D N   
19559 C CA  . ALA D 9   ? 1.1088 0.9756 0.9272 0.2966  -0.0097 -0.0742 9   ALA D CA  
19560 C C   . ALA D 9   ? 1.1761 1.0149 1.0150 0.3192  -0.0223 -0.0557 9   ALA D C   
19561 O O   . ALA D 9   ? 1.2212 1.0882 1.1073 0.3522  -0.0162 -0.0440 9   ALA D O   
19562 C CB  . ALA D 9   ? 1.1516 0.9788 0.9398 0.3079  0.0184  -0.1027 9   ALA D CB  
19568 N N   . GLU D 10  ? 1.2156 1.0019 1.0194 0.3011  -0.0402 -0.0508 10  GLU D N   
19569 C CA  . GLU D 10  ? 1.2729 1.0193 1.0855 0.3177  -0.0538 -0.0305 10  GLU D CA  
19570 C C   . GLU D 10  ? 1.3866 1.0371 1.1559 0.3247  -0.0407 -0.0492 10  GLU D C   
19571 O O   . GLU D 10  ? 1.4351 1.0510 1.1539 0.2972  -0.0353 -0.0724 10  GLU D O   
19572 C CB  . GLU D 10  ? 1.2736 1.0323 1.0768 0.2872  -0.0847 -0.0081 10  GLU D CB  
19573 C CG  . GLU D 10  ? 1.2118 1.0593 1.0515 0.2747  -0.0983 0.0073  10  GLU D CG  
19574 C CD  . GLU D 10  ? 1.2448 1.1379 1.1390 0.3011  -0.1082 0.0361  10  GLU D CD  
19575 O OE1 . GLU D 10  ? 1.3063 1.1608 1.2131 0.3340  -0.1050 0.0473  10  GLU D OE1 
19576 O OE2 . GLU D 10  ? 1.2077 1.1756 1.1319 0.2887  -0.1193 0.0478  10  GLU D OE2 
19583 N N   . LEU D 11  ? 1.3777 0.9862 1.1671 0.3614  -0.0354 -0.0391 11  LEU D N   
19584 C CA  . LEU D 11  ? 1.4405 0.9448 1.1896 0.3684  -0.0246 -0.0537 11  LEU D CA  
19585 C C   . LEU D 11  ? 1.4557 0.9177 1.2098 0.3743  -0.0476 -0.0199 11  LEU D C   
19586 O O   . LEU D 11  ? 1.4511 0.9606 1.2564 0.3991  -0.0606 0.0125  11  LEU D O   
19587 C CB  . LEU D 11  ? 1.5289 1.0051 1.2942 0.4128  0.0087  -0.0757 11  LEU D CB  
19588 C CG  . LEU D 11  ? 1.5289 1.0704 1.3105 0.4198  0.0330  -0.0995 11  LEU D CG  
19589 C CD1 . LEU D 11  ? 1.5901 1.1149 1.4020 0.4717  0.0639  -0.1134 11  LEU D CD1 
19590 C CD2 . LEU D 11  ? 1.5393 1.0640 1.2608 0.3800  0.0423  -0.1320 11  LEU D CD2 
19602 N N   . ALA D 12  ? 1.4490 0.8251 1.1490 0.3489  -0.0533 -0.0255 12  ALA D N   
19603 C CA  . ALA D 12  ? 1.4493 0.7796 1.1473 0.3491  -0.0755 0.0092  12  ALA D CA  
19604 C C   . ALA D 12  ? 1.5873 0.7969 1.2259 0.3338  -0.0678 -0.0067 12  ALA D C   
19605 O O   . ALA D 12  ? 1.6063 0.7862 1.1961 0.3032  -0.0553 -0.0422 12  ALA D O   
19606 C CB  . ALA D 12  ? 1.3146 0.7069 1.0106 0.3095  -0.1073 0.0349  12  ALA D CB  
19612 N N   . GLU D 13  ? 1.6773 0.8182 1.3198 0.3539  -0.0760 0.0214  13  GLU D N   
19613 C CA  . GLU D 13  ? 1.7774 0.7941 1.3627 0.3360  -0.0711 0.0119  13  GLU D CA  
19614 C C   . GLU D 13  ? 1.7515 0.7663 1.2923 0.2756  -0.0981 0.0264  13  GLU D C   
19615 O O   . GLU D 13  ? 1.6598 0.7583 1.2225 0.2597  -0.1229 0.0542  13  GLU D O   
19616 C CB  . GLU D 13  ? 1.8626 0.8012 1.4712 0.3844  -0.0687 0.0403  13  GLU D CB  
19617 C CG  . GLU D 13  ? 1.9153 0.8602 1.5743 0.4498  -0.0407 0.0277  13  GLU D CG  
19618 C CD  . GLU D 13  ? 2.0091 0.8857 1.6996 0.5041  -0.0405 0.0618  13  GLU D CD  
19619 O OE1 . GLU D 13  ? 2.0054 0.9203 1.7273 0.5116  -0.0696 0.1131  13  GLU D OE1 
19620 O OE2 . GLU D 13  ? 2.1175 0.9143 1.8067 0.5344  -0.0109 0.0373  13  GLU D OE2 
19627 N N   . PRO D 14  ? 1.8458 0.7691 1.3230 0.2388  -0.0928 0.0061  14  PRO D N   
19628 C CA  . PRO D 14  ? 1.8454 0.7723 1.2806 0.1791  -0.1172 0.0195  14  PRO D CA  
19629 C C   . PRO D 14  ? 1.8846 0.8140 1.3392 0.1826  -0.1445 0.0733  14  PRO D C   
19630 O O   . PRO D 14  ? 1.9694 0.8403 1.4459 0.2236  -0.1431 0.0993  14  PRO D O   
19631 C CB  . PRO D 14  ? 1.9343 0.7454 1.3014 0.1469  -0.1029 -0.0101 14  PRO D CB  
19632 C CG  . PRO D 14  ? 1.9575 0.7379 1.3255 0.1785  -0.0696 -0.0528 14  PRO D CG  
19633 C CD  . PRO D 14  ? 1.9414 0.7600 1.3795 0.2453  -0.0630 -0.0337 14  PRO D CD  
19641 N N   . GLY D 15  ? 1.8436 0.8445 1.2901 0.1400  -0.1690 0.0905  15  GLY D N   
19642 C CA  . GLY D 15  ? 1.8702 0.8925 1.3312 0.1354  -0.1965 0.1408  15  GLY D CA  
19643 C C   . GLY D 15  ? 1.8309 0.9543 1.3574 0.1716  -0.2080 0.1672  15  GLY D C   
19644 O O   . GLY D 15  ? 1.8517 1.0226 1.3884 0.1579  -0.2334 0.2054  15  GLY D O   
19648 N N   . ALA D 16  ? 1.7477 0.9096 1.3170 0.2139  -0.1899 0.1478  16  ALA D N   
19649 C CA  . ALA D 16  ? 1.7175 0.9787 1.3503 0.2461  -0.1994 0.1709  16  ALA D CA  
19650 C C   . ALA D 16  ? 1.5405 0.9113 1.1796 0.2119  -0.2096 0.1599  16  ALA D C   
19651 O O   . ALA D 16  ? 1.5084 0.8809 1.1048 0.1643  -0.2149 0.1448  16  ALA D O   
19652 C CB  . ALA D 16  ? 1.7836 1.0458 1.4602 0.3025  -0.1742 0.1541  16  ALA D CB  
19658 N N   . SER D 17  ? 1.7953 0.6170 1.3257 0.3000  -0.0037 -0.0354 17  SER D N   
19659 C CA  . SER D 17  ? 1.6706 0.5703 1.2035 0.2831  -0.0169 -0.0275 17  SER D CA  
19660 C C   . SER D 17  ? 1.6063 0.5981 1.1613 0.3140  -0.0268 -0.0397 17  SER D C   
19661 O O   . SER D 17  ? 1.6737 0.6562 1.2323 0.3586  -0.0253 -0.0449 17  SER D O   
19662 C CB  . SER D 17  ? 1.7149 0.6225 1.2380 0.2822  -0.0231 0.0203  17  SER D CB  
19663 O OG  . SER D 17  ? 1.7137 0.6583 1.2414 0.3317  -0.0335 0.0447  17  SER D OG  
19669 N N   . VAL D 18  ? 1.4321 0.5129 1.0032 0.2899  -0.0352 -0.0436 18  VAL D N   
19670 C CA  . VAL D 18  ? 1.3598 0.5332 0.9536 0.3121  -0.0426 -0.0502 18  VAL D CA  
19671 C C   . VAL D 18  ? 1.4408 0.6881 1.0472 0.2950  -0.0530 -0.0258 18  VAL D C   
19672 O O   . VAL D 18  ? 1.4716 0.7096 1.0704 0.2593  -0.0538 -0.0147 18  VAL D O   
19673 C CB  . VAL D 18  ? 1.4637 0.6704 1.0646 0.3005  -0.0382 -0.0912 18  VAL D CB  
19674 C CG1 . VAL D 18  ? 1.4175 0.5568 1.0068 0.3210  -0.0277 -0.1203 18  VAL D CG1 
19675 C CG2 . VAL D 18  ? 1.4293 0.6486 1.0275 0.2495  -0.0387 -0.1032 18  VAL D CG2 
19685 N N   . LYS D 19  ? 1.3522 0.6746 0.9801 0.3202  -0.0596 -0.0196 19  LYS D N   
19686 C CA  . LYS D 19  ? 1.2769 0.6739 0.9211 0.3058  -0.0685 -0.0017 19  LYS D CA  
19687 C C   . LYS D 19  ? 1.2475 0.7257 0.9181 0.3110  -0.0677 -0.0187 19  LYS D C   
19688 O O   . LYS D 19  ? 1.3228 0.8252 1.0068 0.3456  -0.0662 -0.0249 19  LYS D O   
19689 C CB  . LYS D 19  ? 1.2913 0.6972 0.9358 0.3318  -0.0779 0.0302  19  LYS D CB  
19690 C CG  . LYS D 19  ? 1.2680 0.7304 0.9209 0.3090  -0.0864 0.0485  19  LYS D CG  
19691 C CD  . LYS D 19  ? 1.3157 0.8025 0.9708 0.3396  -0.0978 0.0747  19  LYS D CD  
19692 C CE  . LYS D 19  ? 1.2958 0.8293 0.9532 0.3157  -0.1060 0.0911  19  LYS D CE  
19693 N NZ  . LYS D 19  ? 1.3390 0.9082 0.9989 0.3470  -0.1193 0.1128  19  LYS D NZ  
19707 N N   . MET D 20  ? 1.1563 0.6762 0.8346 0.2776  -0.0672 -0.0249 20  MET D N   
19708 C CA  . MET D 20  ? 1.1264 0.7176 0.8261 0.2778  -0.0637 -0.0376 20  MET D CA  
19709 C C   . MET D 20  ? 1.1070 0.7606 0.8281 0.2639  -0.0688 -0.0198 20  MET D C   
19710 O O   . MET D 20  ? 1.1409 0.7831 0.8558 0.2439  -0.0746 -0.0042 20  MET D O   
19711 C CB  . MET D 20  ? 1.1562 0.7436 0.8458 0.2534  -0.0578 -0.0610 20  MET D CB  
19712 C CG  . MET D 20  ? 1.1736 0.7501 0.8556 0.2139  -0.0612 -0.0556 20  MET D CG  
19713 S SD  . MET D 20  ? 1.1848 0.7523 0.8531 0.1879  -0.0573 -0.0858 20  MET D SD  
19714 C CE  . MET D 20  ? 1.2642 0.7450 0.9098 0.1997  -0.0530 -0.1061 20  MET D CE  
19724 N N   . SER D 21  ? 1.0725 0.7912 0.8189 0.2735  -0.0649 -0.0235 21  SER D N   
19725 C CA  . SER D 21  ? 0.9947 0.7727 0.7662 0.2617  -0.0676 -0.0104 21  SER D CA  
19726 C C   . SER D 21  ? 0.9360 0.7537 0.7184 0.2404  -0.0588 -0.0179 21  SER D C   
19727 O O   . SER D 21  ? 0.9483 0.7554 0.7179 0.2375  -0.0521 -0.0324 21  SER D O   
19728 C CB  . SER D 21  ? 0.9950 0.8195 0.7931 0.2906  -0.0696 -0.0053 21  SER D CB  
19729 O OG  . SER D 21  ? 1.0203 0.8782 0.8337 0.3071  -0.0584 -0.0195 21  SER D OG  
19735 N N   . CYS D 22  ? 0.9289 0.7929 0.7347 0.2265  -0.0587 -0.0078 22  CYS D N   
19736 C CA  . CYS D 22  ? 0.9348 0.8322 0.7522 0.2058  -0.0498 -0.0090 22  CYS D CA  
19737 C C   . CYS D 22  ? 0.9151 0.8620 0.7650 0.1984  -0.0485 0.0003  22  CYS D C   
19738 O O   . CYS D 22  ? 0.8853 0.8303 0.7369 0.1814  -0.0554 0.0080  22  CYS D O   
19739 C CB  . CYS D 22  ? 0.9653 0.8322 0.7626 0.1795  -0.0529 -0.0090 22  CYS D CB  
19740 S SG  . CYS D 22  ? 0.9858 0.8911 0.7982 0.1558  -0.0444 -0.0048 22  CYS D SG  
19745 N N   . LYS D 23  ? 0.9402 0.9327 0.8168 0.2099  -0.0384 -0.0023 23  LYS D N   
19746 C CA  . LYS D 23  ? 0.9590 1.0007 0.8717 0.2021  -0.0361 0.0022  23  LYS D CA  
19747 C C   . LYS D 23  ? 0.8670 0.9283 0.7938 0.1793  -0.0220 0.0052  23  LYS D C   
19748 O O   . LYS D 23  ? 0.8775 0.9425 0.7995 0.1821  -0.0088 0.0042  23  LYS D O   
19749 C CB  . LYS D 23  ? 1.0549 1.1395 0.9952 0.2253  -0.0314 -0.0028 23  LYS D CB  
19750 C CG  . LYS D 23  ? 1.1228 1.2634 1.1051 0.2147  -0.0298 -0.0023 23  LYS D CG  
19751 C CD  . LYS D 23  ? 1.2518 1.4432 1.2664 0.2369  -0.0253 -0.0090 23  LYS D CD  
19752 C CE  . LYS D 23  ? 1.3267 1.5791 1.3881 0.2212  -0.0226 -0.0127 23  LYS D CE  
19753 N NZ  . LYS D 23  ? 1.3777 1.6390 1.4405 0.2196  -0.0441 -0.0123 23  LYS D NZ  
19767 N N   . ALA D 24  ? 0.8090 0.8823 0.7517 0.1585  -0.0243 0.0090  24  ALA D N   
19768 C CA  . ALA D 24  ? 0.7603 0.8441 0.7168 0.1375  -0.0108 0.0130  24  ALA D CA  
19769 C C   . ALA D 24  ? 0.7344 0.8650 0.7340 0.1312  0.0021  0.0112  24  ALA D C   
19770 O O   . ALA D 24  ? 0.7322 0.8923 0.7542 0.1346  -0.0050 0.0051  24  ALA D O   
19771 C CB  . ALA D 24  ? 0.7456 0.8085 0.6924 0.1168  -0.0190 0.0156  24  ALA D CB  
19777 N N   . SER D 25  ? 0.6830 0.8214 0.6946 0.1219  0.0219  0.0169  25  SER D N   
19778 C CA  . SER D 25  ? 0.6791 0.8545 0.7335 0.1097  0.0393  0.0161  25  SER D CA  
19779 C C   . SER D 25  ? 0.6828 0.8425 0.7395 0.0935  0.0568  0.0266  25  SER D C   
19780 O O   . SER D 25  ? 0.7362 0.8675 0.7617 0.0982  0.0567  0.0353  25  SER D O   
19781 C CB  . SER D 25  ? 0.7220 0.9310 0.7938 0.1253  0.0525  0.0145  25  SER D CB  
19782 O OG  . SER D 25  ? 0.7168 0.9104 0.7622 0.1374  0.0644  0.0232  25  SER D OG  
19788 N N   . GLY D 26  ? 0.6608 0.8398 0.7559 0.0748  0.0718  0.0250  26  GLY D N   
19789 C CA  . GLY D 26  ? 0.6483 0.8088 0.7498 0.0610  0.0911  0.0364  26  GLY D CA  
19790 C C   . GLY D 26  ? 0.6151 0.7517 0.7130 0.0457  0.0827  0.0331  26  GLY D C   
19791 O O   . GLY D 26  ? 0.6206 0.7391 0.7257 0.0363  0.0988  0.0422  26  GLY D O   
19795 N N   . TYR D 27  ? 0.6072 0.7422 0.6929 0.0447  0.0594  0.0216  27  TYR D N   
19796 C CA  . TYR D 27  ? 0.5896 0.7081 0.6729 0.0294  0.0523  0.0162  27  TYR D CA  
19797 C C   . TYR D 27  ? 0.6267 0.7601 0.7061 0.0277  0.0300  0.0023  27  TYR D C   
19798 O O   . TYR D 27  ? 0.6581 0.8070 0.7311 0.0421  0.0184  0.0002  27  TYR D O   
19799 C CB  . TYR D 27  ? 0.5831 0.6683 0.6323 0.0350  0.0483  0.0270  27  TYR D CB  
19800 C CG  . TYR D 27  ? 0.6232 0.6962 0.6357 0.0476  0.0274  0.0265  27  TYR D CG  
19801 C CD1 . TYR D 27  ? 0.6579 0.7293 0.6516 0.0659  0.0259  0.0313  27  TYR D CD1 
19802 C CD2 . TYR D 27  ? 0.6613 0.7221 0.6575 0.0404  0.0113  0.0206  27  TYR D CD2 
19803 C CE1 . TYR D 27  ? 0.7159 0.7696 0.6780 0.0758  0.0089  0.0286  27  TYR D CE1 
19804 C CE2 . TYR D 27  ? 0.7273 0.7705 0.6912 0.0495  -0.0047 0.0213  27  TYR D CE2 
19805 C CZ  . TYR D 27  ? 0.7608 0.7982 0.7089 0.0668  -0.0058 0.0245  27  TYR D CZ  
19806 O OH  . TYR D 27  ? 0.8249 0.8386 0.7426 0.0743  -0.0197 0.0230  27  TYR D OH  
19816 N N   . THR D 28  ? 0.6180 0.7468 0.6996 0.0119  0.0249  -0.0065 28  THR D N   
19817 C CA  . THR D 28  ? 0.6057 0.7503 0.6792 0.0098  0.0045  -0.0178 28  THR D CA  
19818 C C   . THR D 28  ? 0.6436 0.7601 0.6727 0.0230  -0.0120 -0.0079 28  THR D C   
19819 O O   . THR D 28  ? 0.6394 0.7299 0.6483 0.0165  -0.0129 -0.0040 28  THR D O   
19820 C CB  . THR D 28  ? 0.5996 0.7504 0.6882 -0.0119 0.0068  -0.0322 28  THR D CB  
19821 O OG1 . THR D 28  ? 0.5848 0.7572 0.7178 -0.0264 0.0244  -0.0436 28  THR D OG1 
19822 C CG2 . THR D 28  ? 0.6024 0.7746 0.6774 -0.0124 -0.0147 -0.0428 28  THR D CG2 
19830 N N   . PHE D 29  ? 0.6618 0.7840 0.6782 0.0415  -0.0239 -0.0048 29  PHE D N   
19831 C CA  . PHE D 29  ? 0.6632 0.7523 0.6395 0.0545  -0.0365 0.0045  29  PHE D CA  
19832 C C   . PHE D 29  ? 0.6873 0.7603 0.6398 0.0439  -0.0476 0.0049  29  PHE D C   
19833 O O   . PHE D 29  ? 0.7018 0.7412 0.6272 0.0418  -0.0494 0.0116  29  PHE D O   
19834 C CB  . PHE D 29  ? 0.6517 0.7514 0.6239 0.0774  -0.0466 0.0057  29  PHE D CB  
19835 C CG  . PHE D 29  ? 0.6404 0.7009 0.5732 0.0912  -0.0587 0.0140  29  PHE D CG  
19836 C CD1 . PHE D 29  ? 0.6616 0.6900 0.5755 0.0979  -0.0536 0.0177  29  PHE D CD1 
19837 C CD2 . PHE D 29  ? 0.6736 0.7293 0.5877 0.0980  -0.0744 0.0177  29  PHE D CD2 
19838 C CE1 . PHE D 29  ? 0.7386 0.7270 0.6193 0.1077  -0.0629 0.0222  29  PHE D CE1 
19839 C CE2 . PHE D 29  ? 0.7282 0.7403 0.6069 0.1099  -0.0825 0.0270  29  PHE D CE2 
19840 C CZ  . PHE D 29  ? 0.7563 0.7328 0.6200 0.1132  -0.0761 0.0278  29  PHE D CZ  
19850 N N   . SER D 30  ? 0.6923 0.7927 0.6549 0.0362  -0.0545 -0.0036 30  SER D N   
19851 C CA  . SER D 30  ? 0.7802 0.8700 0.7155 0.0289  -0.0651 -0.0019 30  SER D CA  
19852 C C   . SER D 30  ? 0.7564 0.8285 0.6877 0.0095  -0.0554 -0.0039 30  SER D C   
19853 O O   . SER D 30  ? 0.7749 0.8302 0.6786 0.0035  -0.0609 0.0006  30  SER D O   
19854 C CB  . SER D 30  ? 0.8666 0.9988 0.8129 0.0263  -0.0752 -0.0130 30  SER D CB  
19855 O OG  . SER D 30  ? 0.9141 1.0748 0.8975 0.0082  -0.0638 -0.0303 30  SER D OG  
19861 N N   . SER D 31  ? 0.7182 0.7940 0.6765 0.0008  -0.0397 -0.0092 31  SER D N   
19862 C CA  . SER D 31  ? 0.6733 0.7386 0.6342 -0.0147 -0.0298 -0.0127 31  SER D CA  
19863 C C   . SER D 31  ? 0.6910 0.7272 0.6358 -0.0115 -0.0255 -0.0016 31  SER D C   
19864 O O   . SER D 31  ? 0.6749 0.7055 0.6233 -0.0211 -0.0175 -0.0035 31  SER D O   
19865 C CB  . SER D 31  ? 0.6476 0.7291 0.6475 -0.0248 -0.0136 -0.0239 31  SER D CB  
19866 O OG  . SER D 31  ? 0.6478 0.7614 0.6660 -0.0328 -0.0176 -0.0400 31  SER D OG  
19872 N N   . PHE D 32  ? 0.7142 0.7350 0.6426 0.0023  -0.0309 0.0077  32  PHE D N   
19873 C CA  . PHE D 32  ? 0.6883 0.6886 0.6033 0.0047  -0.0281 0.0143  32  PHE D CA  
19874 C C   . PHE D 32  ? 0.7237 0.6996 0.6075 0.0109  -0.0399 0.0190  32  PHE D C   
19875 O O   . PHE D 32  ? 0.7913 0.7637 0.6679 0.0237  -0.0469 0.0208  32  PHE D O   
19876 C CB  . PHE D 32  ? 0.6782 0.6838 0.6085 0.0152  -0.0172 0.0183  32  PHE D CB  
19877 C CG  . PHE D 32  ? 0.6525 0.6722 0.6134 0.0089  -0.0018 0.0165  32  PHE D CG  
19878 C CD1 . PHE D 32  ? 0.6733 0.6879 0.6392 0.0045  0.0069  0.0193  32  PHE D CD1 
19879 C CD2 . PHE D 32  ? 0.6550 0.6929 0.6418 0.0072  0.0046  0.0113  32  PHE D CD2 
19880 C CE1 . PHE D 32  ? 0.6833 0.7028 0.6774 0.0003  0.0231  0.0186  32  PHE D CE1 
19881 C CE2 . PHE D 32  ? 0.6678 0.7119 0.6845 -0.0013 0.0214  0.0084  32  PHE D CE2 
19882 C CZ  . PHE D 32  ? 0.6570 0.6878 0.6762 -0.0040 0.0313  0.0130  32  PHE D CZ  
19892 N N   . TRP D 33  ? 0.7088 0.6680 0.5765 0.0018  -0.0411 0.0200  33  TRP D N   
19893 C CA  . TRP D 33  ? 0.7363 0.6662 0.5766 0.0038  -0.0493 0.0226  33  TRP D CA  
19894 C C   . TRP D 33  ? 0.7415 0.6639 0.5786 0.0201  -0.0498 0.0216  33  TRP D C   
19895 O O   . TRP D 33  ? 0.6704 0.6108 0.5227 0.0271  -0.0426 0.0207  33  TRP D O   
19896 C CB  . TRP D 33  ? 0.7555 0.6758 0.5864 -0.0128 -0.0480 0.0207  33  TRP D CB  
19897 C CG  . TRP D 33  ? 0.7747 0.7022 0.6051 -0.0291 -0.0458 0.0211  33  TRP D CG  
19898 C CD1 . TRP D 33  ? 0.7692 0.7088 0.6016 -0.0303 -0.0466 0.0219  33  TRP D CD1 
19899 C CD2 . TRP D 33  ? 0.7746 0.7032 0.6023 -0.0466 -0.0420 0.0186  33  TRP D CD2 
19900 N NE1 . TRP D 33  ? 0.7493 0.6950 0.5771 -0.0468 -0.0428 0.0203  33  TRP D NE1 
19901 C CE2 . TRP D 33  ? 0.7579 0.6970 0.5842 -0.0571 -0.0390 0.0189  33  TRP D CE2 
19902 C CE3 . TRP D 33  ? 0.7881 0.7151 0.6158 -0.0548 -0.0409 0.0142  33  TRP D CE3 
19903 C CZ2 . TRP D 33  ? 0.7665 0.7128 0.5913 -0.0748 -0.0331 0.0163  33  TRP D CZ2 
19904 C CZ3 . TRP D 33  ? 0.8009 0.7378 0.6308 -0.0731 -0.0361 0.0112  33  TRP D CZ3 
19905 C CH2 . TRP D 33  ? 0.7904 0.7358 0.6188 -0.0828 -0.0312 0.0129  33  TRP D CH2 
19916 N N   . MET D 34  ? 0.8085 0.7017 0.6238 0.0272  -0.0569 0.0221  34  MET D N   
19917 C CA  . MET D 34  ? 0.8322 0.7136 0.6396 0.0423  -0.0575 0.0173  34  MET D CA  
19918 C C   . MET D 34  ? 0.9011 0.7505 0.6871 0.0321  -0.0608 0.0111  34  MET D C   
19919 O O   . MET D 34  ? 0.9398 0.7581 0.7094 0.0236  -0.0645 0.0146  34  MET D O   
19920 C CB  . MET D 34  ? 0.8274 0.7013 0.6317 0.0626  -0.0616 0.0198  34  MET D CB  
19921 C CG  . MET D 34  ? 0.8382 0.7054 0.6372 0.0808  -0.0597 0.0126  34  MET D CG  
19922 S SD  . MET D 34  ? 0.8153 0.7267 0.6378 0.0883  -0.0480 0.0113  34  MET D SD  
19923 C CE  . MET D 34  ? 0.8168 0.7589 0.6664 0.0973  -0.0461 0.0168  34  MET D CE  
19933 N N   . HIS D 35  ? 0.9260 0.7841 0.7118 0.0322  -0.0589 0.0019  35  HIS D N   
19934 C CA  . HIS D 35  ? 0.9120 0.7468 0.6816 0.0207  -0.0623 -0.0097 35  HIS D CA  
19935 C C   . HIS D 35  ? 0.9124 0.7235 0.6667 0.0368  -0.0643 -0.0202 35  HIS D C   
19936 O O   . HIS D 35  ? 0.8902 0.7155 0.6486 0.0578  -0.0618 -0.0193 35  HIS D O   
19937 C CB  . HIS D 35  ? 0.8631 0.7304 0.6419 0.0110  -0.0612 -0.0164 35  HIS D CB  
19938 C CG  . HIS D 35  ? 0.9001 0.7892 0.6950 -0.0035 -0.0580 -0.0087 35  HIS D CG  
19939 N ND1 . HIS D 35  ? 0.9212 0.8131 0.7174 -0.0248 -0.0590 -0.0145 35  HIS D ND1 
19940 C CD2 . HIS D 35  ? 0.8886 0.7987 0.7009 -0.0002 -0.0526 0.0018  35  HIS D CD2 
19941 C CE1 . HIS D 35  ? 0.9057 0.8199 0.7180 -0.0316 -0.0543 -0.0072 35  HIS D CE1 
19942 N NE2 . HIS D 35  ? 0.8804 0.8035 0.7020 -0.0172 -0.0504 0.0020  35  HIS D NE2 
19950 N N   . TRP D 36  ? 0.9125 0.6864 0.6502 0.0256  -0.0671 -0.0317 36  TRP D N   
19951 C CA  . TRP D 36  ? 0.9082 0.6539 0.6303 0.0382  -0.0681 -0.0471 36  TRP D CA  
19952 C C   . TRP D 36  ? 0.8957 0.6428 0.6115 0.0211  -0.0704 -0.0691 36  TRP D C   
19953 O O   . TRP D 36  ? 0.8522 0.5983 0.5718 -0.0044 -0.0714 -0.0715 36  TRP D O   
19954 C CB  . TRP D 36  ? 0.9542 0.6421 0.6615 0.0436  -0.0683 -0.0422 36  TRP D CB  
19955 C CG  . TRP D 36  ? 0.9660 0.6595 0.6789 0.0658  -0.0687 -0.0240 36  TRP D CG  
19956 C CD1 . TRP D 36  ? 0.9426 0.6461 0.6620 0.0614  -0.0700 -0.0052 36  TRP D CD1 
19957 C CD2 . TRP D 36  ? 0.9941 0.6902 0.7082 0.0960  -0.0680 -0.0255 36  TRP D CD2 
19958 N NE1 . TRP D 36  ? 0.9449 0.6596 0.6704 0.0861  -0.0719 0.0042  36  TRP D NE1 
19959 C CE2 . TRP D 36  ? 0.9708 0.6819 0.6951 0.1078  -0.0703 -0.0073 36  TRP D CE2 
19960 C CE3 . TRP D 36  ? 1.0290 0.7205 0.7371 0.1142  -0.0655 -0.0423 36  TRP D CE3 
19961 C CZ2 . TRP D 36  ? 0.9759 0.7003 0.7084 0.1368  -0.0704 -0.0049 36  TRP D CZ2 
19962 C CZ3 . TRP D 36  ? 1.0505 0.7522 0.7651 0.1439  -0.0638 -0.0391 36  TRP D CZ3 
19963 C CH2 . TRP D 36  ? 1.0320 0.7514 0.7606 0.1547  -0.0664 -0.0203 36  TRP D CH2 
19974 N N   . VAL D 37  ? 0.9104 0.6651 0.6171 0.0350  -0.0712 -0.0868 37  VAL D N   
19975 C CA  . VAL D 37  ? 0.9240 0.6924 0.6243 0.0216  -0.0754 -0.1118 37  VAL D CA  
19976 C C   . VAL D 37  ? 0.9821 0.7141 0.6635 0.0312  -0.0751 -0.1360 37  VAL D C   
19977 O O   . VAL D 37  ? 1.0134 0.7342 0.6883 0.0572  -0.0713 -0.1332 37  VAL D O   
19978 C CB  . VAL D 37  ? 0.9018 0.7358 0.6089 0.0305  -0.0771 -0.1104 37  VAL D CB  
19979 C CG1 . VAL D 37  ? 0.9267 0.7839 0.6251 0.0198  -0.0843 -0.1379 37  VAL D CG1 
19980 C CG2 . VAL D 37  ? 0.8423 0.7060 0.5697 0.0220  -0.0757 -0.0883 37  VAL D CG2 
19990 N N   . LYS D 38  ? 1.0107 0.7260 0.6855 0.0092  -0.0785 -0.1623 38  LYS D N   
19991 C CA  . LYS D 38  ? 1.0648 0.7402 0.7223 0.0130  -0.0775 -0.1917 38  LYS D CA  
19992 C C   . LYS D 38  ? 1.1034 0.8266 0.7539 0.0100  -0.0842 -0.2219 38  LYS D C   
19993 O O   . LYS D 38  ? 1.0684 0.8340 0.7289 -0.0104 -0.0909 -0.2277 38  LYS D O   
19994 C CB  . LYS D 38  ? 1.1022 0.7090 0.7574 -0.0134 -0.0740 -0.2010 38  LYS D CB  
19995 C CG  . LYS D 38  ? 1.1776 0.7301 0.8165 -0.0117 -0.0707 -0.2335 38  LYS D CG  
19996 C CD  . LYS D 38  ? 1.2529 0.7366 0.8923 -0.0436 -0.0646 -0.2406 38  LYS D CD  
19997 C CE  . LYS D 38  ? 1.3605 0.7811 0.9857 -0.0444 -0.0592 -0.2754 38  LYS D CE  
19998 N NZ  . LYS D 38  ? 1.4381 0.7931 1.0665 -0.0821 -0.0511 -0.2848 38  LYS D NZ  
20012 N N   . GLN D 39  ? 1.1749 0.8958 0.8079 0.0320  -0.0826 -0.2417 39  GLN D N   
20013 C CA  . GLN D 39  ? 1.2288 0.9962 0.8488 0.0325  -0.0893 -0.2731 39  GLN D CA  
20014 C C   . GLN D 39  ? 1.3634 1.0845 0.9643 0.0380  -0.0860 -0.3095 39  GLN D C   
20015 O O   . GLN D 39  ? 1.3435 1.0496 0.9333 0.0678  -0.0786 -0.3071 39  GLN D O   
20016 C CB  . GLN D 39  ? 1.1582 0.9923 0.7727 0.0604  -0.0891 -0.2562 39  GLN D CB  
20017 C CG  . GLN D 39  ? 1.1316 1.0233 0.7284 0.0632  -0.0974 -0.2835 39  GLN D CG  
20018 C CD  . GLN D 39  ? 1.0763 1.0318 0.6663 0.0900  -0.0950 -0.2594 39  GLN D CD  
20019 O OE1 . GLN D 39  ? 1.0349 0.9845 0.6281 0.1116  -0.0840 -0.2329 39  GLN D OE1 
20020 N NE2 . GLN D 39  ? 1.0370 1.0551 0.6184 0.0888  -0.1048 -0.2677 39  GLN D NE2 
20029 N N   . ARG D 40  ? 1.4834 1.1833 1.0827 0.0090  -0.0902 -0.3450 40  ARG D N   
20030 C CA  . ARG D 40  ? 1.6160 1.2716 1.1976 0.0119  -0.0865 -0.3859 40  ARG D CA  
20031 C C   . ARG D 40  ? 1.5411 1.2596 1.1011 0.0328  -0.0916 -0.4111 40  ARG D C   
20032 O O   . ARG D 40  ? 1.4232 1.2190 0.9827 0.0328  -0.1012 -0.4057 40  ARG D O   
20033 C CB  . ARG D 40  ? 1.7703 1.3865 1.3590 -0.0295 -0.0883 -0.4201 40  ARG D CB  
20034 C CG  . ARG D 40  ? 1.8471 1.3681 1.4441 -0.0434 -0.0766 -0.4066 40  ARG D CG  
20035 C CD  . ARG D 40  ? 1.9273 1.3900 1.5236 -0.0760 -0.0725 -0.4515 40  ARG D CD  
20036 N NE  . ARG D 40  ? 1.9855 1.3863 1.5975 -0.1079 -0.0639 -0.4345 40  ARG D NE  
20037 C CZ  . ARG D 40  ? 2.0464 1.4809 1.6787 -0.1446 -0.0682 -0.4308 40  ARG D CZ  
20038 N NH1 . ARG D 40  ? 2.0332 1.5631 1.6740 -0.1517 -0.0827 -0.4429 40  ARG D NH1 
20039 N NH2 . ARG D 40  ? 2.1591 1.5334 1.8027 -0.1724 -0.0572 -0.4138 40  ARG D NH2 
20053 N N   . PRO D 41  ? 1.6053 1.2930 1.1457 0.0529  -0.0847 -0.4380 41  PRO D N   
20054 C CA  . PRO D 41  ? 1.6439 1.3929 1.1592 0.0738  -0.0879 -0.4632 41  PRO D CA  
20055 C C   . PRO D 41  ? 1.6749 1.4870 1.1850 0.0494  -0.1035 -0.4934 41  PRO D C   
20056 O O   . PRO D 41  ? 1.7052 1.4915 1.2234 0.0154  -0.1088 -0.5275 41  PRO D O   
20057 C CB  . PRO D 41  ? 1.6997 1.3872 1.1984 0.0876  -0.0777 -0.4997 41  PRO D CB  
20058 C CG  . PRO D 41  ? 1.6843 1.2914 1.1995 0.0941  -0.0666 -0.4711 41  PRO D CG  
20059 C CD  . PRO D 41  ? 1.6447 1.2406 1.1837 0.0612  -0.0724 -0.4450 41  PRO D CD  
20067 N N   . GLY D 42  ? 1.6721 1.5694 1.1700 0.0672  -0.1103 -0.4796 42  GLY D N   
20068 C CA  . GLY D 42  ? 1.6798 1.6485 1.1763 0.0496  -0.1245 -0.4952 42  GLY D CA  
20069 C C   . GLY D 42  ? 1.6229 1.6085 1.1468 0.0175  -0.1362 -0.4884 42  GLY D C   
20070 O O   . GLY D 42  ? 1.5951 1.6377 1.1259 0.0012  -0.1477 -0.4979 42  GLY D O   
20074 N N   . GLN D 43  ? 1.5515 1.4886 1.0989 0.0074  -0.1300 -0.4592 43  GLN D N   
20075 C CA  . GLN D 43  ? 1.5143 1.4607 1.0917 -0.0254 -0.1366 -0.4494 43  GLN D CA  
20076 C C   . GLN D 43  ? 1.4255 1.4134 1.0163 -0.0099 -0.1365 -0.3971 43  GLN D C   
20077 O O   . GLN D 43  ? 1.3943 1.4073 0.9712 0.0236  -0.1318 -0.3706 43  GLN D O   
20078 C CB  . GLN D 43  ? 1.5418 1.3960 1.1366 -0.0531 -0.1264 -0.4532 43  GLN D CB  
20079 C CG  . GLN D 43  ? 1.5997 1.4148 1.1899 -0.0804 -0.1270 -0.5088 43  GLN D CG  
20080 C CD  . GLN D 43  ? 1.5918 1.4707 1.1963 -0.1112 -0.1411 -0.5345 43  GLN D CD  
20081 O OE1 . GLN D 43  ? 1.6265 1.5284 1.2203 -0.1128 -0.1463 -0.5618 43  GLN D OE1 
20082 N NE2 . GLN D 43  ? 1.5492 1.4580 1.1814 -0.1336 -0.1460 -0.5175 43  GLN D NE2 
20091 N N   . GLY D 44  ? 1.3587 1.3531 0.9777 -0.0358 -0.1399 -0.3837 44  GLY D N   
20092 C CA  . GLY D 44  ? 1.3058 1.3359 0.9410 -0.0252 -0.1393 -0.3392 44  GLY D CA  
20093 C C   . GLY D 44  ? 1.3010 1.2693 0.9478 -0.0218 -0.1254 -0.3031 44  GLY D C   
20094 O O   . GLY D 44  ? 1.3756 1.2800 1.0128 -0.0157 -0.1161 -0.3052 44  GLY D O   
20098 N N   . LEU D 45  ? 1.0524 0.7965 1.1231 -0.0209 -0.1639 -0.2342 45  LEU D N   
20099 C CA  . LEU D 45  ? 0.9628 0.7566 1.0377 -0.0201 -0.1266 -0.2175 45  LEU D CA  
20100 C C   . LEU D 45  ? 0.9197 0.7239 1.0508 -0.0407 -0.1166 -0.1929 45  LEU D C   
20101 O O   . LEU D 45  ? 0.8636 0.6794 1.0480 -0.0625 -0.1241 -0.1861 45  LEU D O   
20102 C CB  . LEU D 45  ? 0.9103 0.7489 0.9712 -0.0247 -0.1082 -0.2164 45  LEU D CB  
20103 C CG  . LEU D 45  ? 0.9867 0.8219 0.9825 -0.0145 -0.1112 -0.2337 45  LEU D CG  
20104 C CD1 . LEU D 45  ? 0.9687 0.8268 0.9447 -0.0295 -0.1047 -0.2282 45  LEU D CD1 
20105 C CD2 . LEU D 45  ? 1.0431 0.9016 1.0063 0.0067  -0.0929 -0.2395 45  LEU D CD2 
20117 N N   . GLU D 46  ? 0.9652 0.7694 1.0826 -0.0334 -0.0997 -0.1803 46  GLU D N   
20118 C CA  . GLU D 46  ? 0.9753 0.7788 1.1251 -0.0544 -0.0878 -0.1534 46  GLU D CA  
20119 C C   . GLU D 46  ? 0.9195 0.7615 1.0525 -0.0450 -0.0545 -0.1411 46  GLU D C   
20120 O O   . GLU D 46  ? 0.9487 0.7898 1.0406 -0.0197 -0.0517 -0.1510 46  GLU D O   
20121 C CB  . GLU D 46  ? 1.0783 0.8081 1.2079 -0.0550 -0.1151 -0.1492 46  GLU D CB  
20122 C CG  . GLU D 46  ? 1.1704 0.8827 1.3377 -0.0955 -0.1158 -0.1183 46  GLU D CG  
20123 C CD  . GLU D 46  ? 1.3092 0.9254 1.4466 -0.1016 -0.1582 -0.1150 46  GLU D CD  
20124 O OE1 . GLU D 46  ? 1.3777 0.9437 1.4596 -0.0625 -0.1838 -0.1401 46  GLU D OE1 
20125 O OE2 . GLU D 46  ? 1.4092 1.0009 1.5764 -0.1456 -0.1680 -0.0880 46  GLU D OE2 
20132 N N   . TRP D 47  ? 0.8532 0.7338 1.0189 -0.0628 -0.0306 -0.1218 47  TRP D N   
20133 C CA  . TRP D 47  ? 0.8193 0.7306 0.9640 -0.0523 -0.0030 -0.1112 47  TRP D CA  
20134 C C   . TRP D 47  ? 0.8601 0.7396 0.9856 -0.0575 0.0062  -0.0884 47  TRP D C   
20135 O O   . TRP D 47  ? 0.9104 0.7784 1.0600 -0.0853 0.0104  -0.0678 47  TRP D O   
20136 C CB  . TRP D 47  ? 0.7831 0.7479 0.9592 -0.0591 0.0149  -0.1076 47  TRP D CB  
20137 C CG  . TRP D 47  ? 0.8043 0.7911 0.9520 -0.0460 0.0377  -0.0982 47  TRP D CG  
20138 C CD1 . TRP D 47  ? 0.8145 0.8088 0.9256 -0.0287 0.0350  -0.1079 47  TRP D CD1 
20139 C CD2 . TRP D 47  ? 0.7988 0.7993 0.9468 -0.0513 0.0643  -0.0762 47  TRP D CD2 
20140 N NE1 . TRP D 47  ? 0.7850 0.7899 0.8741 -0.0196 0.0528  -0.0954 47  TRP D NE1 
20141 C CE2 . TRP D 47  ? 0.7751 0.7836 0.8822 -0.0303 0.0729  -0.0769 47  TRP D CE2 
20142 C CE3 . TRP D 47  ? 0.8589 0.8650 1.0331 -0.0757 0.0813  -0.0542 47  TRP D CE3 
20143 C CZ2 . TRP D 47  ? 0.8093 0.8254 0.8948 -0.0253 0.0972  -0.0596 47  TRP D CZ2 
20144 C CZ3 . TRP D 47  ? 0.9129 0.9345 1.0657 -0.0753 0.1114  -0.0342 47  TRP D CZ3 
20145 C CH2 . TRP D 47  ? 0.8748 0.8985 0.9806 -0.0465 0.1188  -0.0387 47  TRP D CH2 
20156 N N   . ILE D 48  ? 0.8241 0.6899 0.9050 -0.0334 0.0073  -0.0911 48  ILE D N   
20157 C CA  . ILE D 48  ? 0.8786 0.6961 0.9246 -0.0318 0.0066  -0.0730 48  ILE D CA  
20158 C C   . ILE D 48  ? 0.9018 0.7419 0.9361 -0.0371 0.0364  -0.0511 48  ILE D C   
20159 O O   . ILE D 48  ? 0.9752 0.7899 1.0000 -0.0592 0.0480  -0.0247 48  ILE D O   
20160 C CB  . ILE D 48  ? 0.8766 0.6683 0.8820 0.0049  -0.0148 -0.0932 48  ILE D CB  
20161 C CG1 . ILE D 48  ? 0.8944 0.6655 0.9022 0.0173  -0.0429 -0.1187 48  ILE D CG1 
20162 C CG2 . ILE D 48  ? 0.9335 0.6590 0.8930 0.0121  -0.0261 -0.0777 48  ILE D CG2 
20163 C CD1 . ILE D 48  ? 0.8852 0.6620 0.8629 0.0606  -0.0583 -0.1469 48  ILE D CD1 
20175 N N   . GLY D 49  ? 0.8640 0.7468 0.8913 -0.0189 0.0473  -0.0607 49  GLY D N   
20176 C CA  . GLY D 49  ? 0.8764 0.7719 0.8802 -0.0152 0.0697  -0.0448 49  GLY D CA  
20177 C C   . GLY D 49  ? 0.8324 0.7527 0.8162 0.0082  0.0646  -0.0592 49  GLY D C   
20178 O O   . GLY D 49  ? 0.7876 0.7264 0.7806 0.0152  0.0491  -0.0787 49  GLY D O   
20182 N N   . TYR D 50  ? 0.8225 0.7416 0.7739 0.0176  0.0771  -0.0476 50  TYR D N   
20183 C CA  . TYR D 50  ? 0.8049 0.7377 0.7320 0.0354  0.0663  -0.0572 50  TYR D CA  
20184 C C   . TYR D 50  ? 0.8806 0.7762 0.7562 0.0521  0.0649  -0.0449 50  TYR D C   
20185 O O   . TYR D 50  ? 0.9348 0.7942 0.7850 0.0485  0.0784  -0.0263 50  TYR D O   
20186 C CB  . TYR D 50  ? 0.7792 0.7416 0.7106 0.0356  0.0713  -0.0622 50  TYR D CB  
20187 C CG  . TYR D 50  ? 0.7955 0.7529 0.6971 0.0464  0.0914  -0.0494 50  TYR D CG  
20188 C CD1 . TYR D 50  ? 0.8201 0.7519 0.6666 0.0666  0.0841  -0.0454 50  TYR D CD1 
20189 C CD2 . TYR D 50  ? 0.8169 0.8012 0.7458 0.0376  0.1174  -0.0427 50  TYR D CD2 
20190 C CE1 . TYR D 50  ? 0.8500 0.7747 0.6577 0.0820  0.1033  -0.0360 50  TYR D CE1 
20191 C CE2 . TYR D 50  ? 0.8606 0.8547 0.7604 0.0506  0.1418  -0.0331 50  TYR D CE2 
20192 C CZ  . TYR D 50  ? 0.8538 0.8138 0.6871 0.0750  0.1353  -0.0303 50  TYR D CZ  
20193 O OH  . TYR D 50  ? 0.8526 0.8195 0.6457 0.0932  0.1603  -0.0228 50  TYR D OH  
20203 N N   . ILE D 51  ? 0.8760 0.7781 0.7330 0.0670  0.0459  -0.0541 51  ILE D N   
20204 C CA  . ILE D 51  ? 0.8880 0.7531 0.6947 0.0866  0.0356  -0.0465 51  ILE D CA  
20205 C C   . ILE D 51  ? 0.9016 0.7781 0.6869 0.0939  0.0227  -0.0506 51  ILE D C   
20206 O O   . ILE D 51  ? 0.8513 0.7645 0.6622 0.0833  0.0083  -0.0626 51  ILE D O   
20207 C CB  . ILE D 51  ? 0.8730 0.7282 0.6813 0.1017  0.0108  -0.0572 51  ILE D CB  
20208 C CG1 . ILE D 51  ? 0.9034 0.7140 0.6575 0.1246  -0.0069 -0.0510 51  ILE D CG1 
20209 C CG2 . ILE D 51  ? 0.8223 0.7416 0.6753 0.0982  -0.0039 -0.0783 51  ILE D CG2 
20210 C CD1 . ILE D 51  ? 0.8817 0.6745 0.6333 0.1477  -0.0356 -0.0638 51  ILE D CD1 
20222 N N   . ASN D 52  ? 0.9770 0.8140 0.7061 0.1102  0.0250  -0.0395 52  ASN D N   
20223 C CA  . ASN D 52  ? 0.9947 0.8207 0.6877 0.1227  0.0009  -0.0439 52  ASN D CA  
20224 C C   . ASN D 52  ? 0.9666 0.7819 0.6523 0.1318  -0.0317 -0.0484 52  ASN D C   
20225 O O   . ASN D 52  ? 0.9902 0.7578 0.6334 0.1508  -0.0366 -0.0410 52  ASN D O   
20226 C CB  . ASN D 52  ? 1.0900 0.8762 0.7180 0.1435  0.0151  -0.0339 52  ASN D CB  
20227 C CG  . ASN D 52  ? 1.1685 0.9288 0.7488 0.1605  -0.0176 -0.0410 52  ASN D CG  
20228 O OD1 . ASN D 52  ? 1.1367 0.8922 0.7193 0.1564  -0.0546 -0.0462 52  ASN D OD1 
20229 N ND2 . ASN D 52  ? 1.2834 1.0294 0.8207 0.1805  -0.0066 -0.0427 52  ASN D ND2 
20236 N N   . PRO D 53  ? 0.9489 0.8100 0.6740 0.1177  -0.0555 -0.0602 53  PRO D N   
20237 C CA  . PRO D 53  ? 0.9877 0.8654 0.7285 0.1265  -0.0832 -0.0686 53  PRO D CA  
20238 C C   . PRO D 53  ? 1.0914 0.9124 0.7740 0.1502  -0.1107 -0.0635 53  PRO D C   
20239 O O   . PRO D 53  ? 1.1504 0.9531 0.8256 0.1715  -0.1268 -0.0678 53  PRO D O   
20240 C CB  . PRO D 53  ? 0.9028 0.8509 0.6920 0.0979  -0.0990 -0.0777 53  PRO D CB  
20241 C CG  . PRO D 53  ? 0.8805 0.8392 0.6796 0.0758  -0.0777 -0.0755 53  PRO D CG  
20242 C CD  . PRO D 53  ? 0.8910 0.7903 0.6423 0.0922  -0.0612 -0.0659 53  PRO D CD  
20250 N N   . ASN D 54  ? 1.1113 0.8956 0.7449 0.1518  -0.1222 -0.0569 54  ASN D N   
20251 C CA  . ASN D 54  ? 1.2174 0.9417 0.7887 0.1755  -0.1560 -0.0542 54  ASN D CA  
20252 C C   . ASN D 54  ? 1.2478 0.8992 0.7495 0.2052  -0.1385 -0.0435 54  ASN D C   
20253 O O   . ASN D 54  ? 1.3125 0.9092 0.7631 0.2288  -0.1685 -0.0428 54  ASN D O   
20254 C CB  . ASN D 54  ? 1.3165 1.0103 0.8435 0.1724  -0.1794 -0.0526 54  ASN D CB  
20255 C CG  . ASN D 54  ? 1.3548 1.0129 0.8490 0.1807  -0.2347 -0.0546 54  ASN D CG  
20256 O OD1 . ASN D 54  ? 1.3189 1.0179 0.8617 0.1724  -0.2594 -0.0606 54  ASN D OD1 
20257 N ND2 . ASN D 54  ? 1.5416 1.1258 0.9539 0.2002  -0.2574 -0.0522 54  ASN D ND2 
20264 N N   . SER D 55  ? 1.1937 0.8422 0.6900 0.2011  -0.0928 -0.0338 55  SER D N   
20265 C CA  . SER D 55  ? 1.1623 0.7447 0.5855 0.2184  -0.0701 -0.0175 55  SER D CA  
20266 C C   . SER D 55  ? 1.1703 0.7459 0.6127 0.2084  -0.0513 -0.0096 55  SER D C   
20267 O O   . SER D 55  ? 1.2508 0.7586 0.6238 0.2169  -0.0411 0.0074  55  SER D O   
20268 C CB  . SER D 55  ? 1.1327 0.7153 0.5208 0.2204  -0.0315 -0.0091 55  SER D CB  
20269 O OG  . SER D 55  ? 1.1051 0.7487 0.5605 0.1951  0.0043  -0.0084 55  SER D OG  
20275 N N   . GLY D 56  ? 1.1128 0.7472 0.6364 0.1903  -0.0494 -0.0207 56  GLY D N   
20276 C CA  . GLY D 56  ? 1.1286 0.7461 0.6652 0.1828  -0.0393 -0.0157 56  GLY D CA  
20277 C C   . GLY D 56  ? 1.1684 0.7807 0.6997 0.1585  0.0052  0.0044  56  GLY D C   
20278 O O   . GLY D 56  ? 1.1796 0.7735 0.7237 0.1449  0.0096  0.0105  56  GLY D O   
20282 N N   . TYR D 57  ? 1.2099 0.8395 0.7234 0.1538  0.0348  0.0135  57  TYR D N   
20283 C CA  . TYR D 57  ? 1.2653 0.9168 0.7926 0.1288  0.0792  0.0299  57  TYR D CA  
20284 C C   . TYR D 57  ? 1.1553 0.8644 0.7719 0.1053  0.0830  0.0187  57  TYR D C   
20285 O O   . TYR D 57  ? 1.0374 0.7911 0.7023 0.1088  0.0652  -0.0025 57  TYR D O   
20286 C CB  . TYR D 57  ? 1.3200 1.0015 0.8249 0.1387  0.1063  0.0310  57  TYR D CB  
20287 C CG  . TYR D 57  ? 1.3134 1.0464 0.8519 0.1145  0.1536  0.0430  57  TYR D CG  
20288 C CD1 . TYR D 57  ? 1.3728 1.0819 0.8671 0.0962  0.1879  0.0719  57  TYR D CD1 
20289 C CD2 . TYR D 57  ? 1.2597 1.0665 0.8735 0.1072  0.1616  0.0263  57  TYR D CD2 
20290 C CE1 . TYR D 57  ? 1.3710 1.1443 0.9079 0.0682  0.2322  0.0840  57  TYR D CE1 
20291 C CE2 . TYR D 57  ? 1.2650 1.1300 0.9210 0.0866  0.2010  0.0341  57  TYR D CE2 
20292 C CZ  . TYR D 57  ? 1.3461 1.2023 0.9698 0.0657  0.2378  0.0631  57  TYR D CZ  
20293 O OH  . TYR D 57  ? 1.3938 1.3246 1.0709 0.0394  0.2782  0.0722  57  TYR D OH  
20303 N N   . THR D 58  ? 1.1762 0.8786 0.8085 0.0780  0.1037  0.0347  58  THR D N   
20304 C CA  . THR D 58  ? 1.0851 0.8291 0.7935 0.0566  0.1034  0.0247  58  THR D CA  
20305 C C   . THR D 58  ? 1.0902 0.8645 0.8261 0.0242  0.1406  0.0431  58  THR D C   
20306 O O   . THR D 58  ? 1.1564 0.9113 0.8483 0.0114  0.1676  0.0687  58  THR D O   
20307 C CB  . THR D 58  ? 1.0699 0.7665 0.7796 0.0567  0.0725  0.0198  58  THR D CB  
20308 O OG1 . THR D 58  ? 1.1796 0.8016 0.8345 0.0402  0.0758  0.0472  58  THR D OG1 
20309 C CG2 . THR D 58  ? 1.0242 0.7091 0.7174 0.0911  0.0368  -0.0009 58  THR D CG2 
20317 N N   . GLU D 59  ? 1.0158 0.8428 0.8253 0.0094  0.1414  0.0296  59  GLU D N   
20318 C CA  . GLU D 59  ? 1.0487 0.9101 0.9057 -0.0258 0.1658  0.0431  59  GLU D CA  
20319 C C   . GLU D 59  ? 1.0075 0.8591 0.9135 -0.0407 0.1392  0.0313  59  GLU D C   
20320 O O   . GLU D 59  ? 0.9483 0.8111 0.8736 -0.0212 0.1156  0.0053  59  GLU D O   
20321 C CB  . GLU D 59  ? 1.0779 1.0237 0.9786 -0.0212 0.1917  0.0326  59  GLU D CB  
20322 C CG  . GLU D 59  ? 1.1699 1.1331 1.0213 -0.0048 0.2236  0.0433  59  GLU D CG  
20323 C CD  . GLU D 59  ? 1.2046 1.2588 1.1054 0.0032  0.2489  0.0297  59  GLU D CD  
20324 O OE1 . GLU D 59  ? 1.1911 1.2995 1.1663 -0.0243 0.2592  0.0300  59  GLU D OE1 
20325 O OE2 . GLU D 59  ? 1.2251 1.2942 1.0896 0.0403  0.2532  0.0161  59  GLU D OE2 
20332 N N   . CYS D 60  ? 1.0897 0.9176 1.0095 -0.0772 0.1416  0.0515  60  CYS D N   
20333 C CA  . CYS D 60  ? 1.0690 0.8707 1.0230 -0.0897 0.1106  0.0408  60  CYS D CA  
20334 C C   . CYS D 60  ? 0.9855 0.8332 1.0074 -0.1302 0.1238  0.0505  60  CYS D C   
20335 O O   . CYS D 60  ? 0.9630 0.8473 0.9965 -0.1595 0.1575  0.0756  60  CYS D O   
20336 C CB  . CYS D 60  ? 1.2309 0.9299 1.1265 -0.0939 0.0797  0.0534  60  CYS D CB  
20337 S SG  . CYS D 60  ? 1.2917 0.9416 1.1261 -0.0394 0.0484  0.0309  60  CYS D SG  
20343 N N   . ASN D 61  ? 0.9382 0.7897 1.0057 -0.1312 0.0970  0.0294  61  ASN D N   
20344 C CA  . ASN D 61  ? 1.0030 0.8700 1.1295 -0.1733 0.0927  0.0396  61  ASN D CA  
20345 C C   . ASN D 61  ? 1.1644 0.9567 1.2536 -0.2142 0.0848  0.0754  61  ASN D C   
20346 O O   . ASN D 61  ? 0.9534 0.6537 0.9718 -0.1994 0.0585  0.0783  61  ASN D O   
20347 C CB  . ASN D 61  ? 0.9672 0.8184 1.1235 -0.1621 0.0541  0.0101  61  ASN D CB  
20348 C CG  . ASN D 61  ? 0.9632 0.8369 1.1892 -0.2025 0.0436  0.0156  61  ASN D CG  
20349 O OD1 . ASN D 61  ? 1.0300 0.9086 1.2761 -0.2486 0.0558  0.0469  61  ASN D OD1 
20350 N ND2 . ASN D 61  ? 0.9094 0.7968 1.1708 -0.1885 0.0189  -0.0137 61  ASN D ND2 
20357 N N   . GLU D 62  ? 1.2531 1.0858 1.3885 -0.2670 0.1053  0.1030  62  GLU D N   
20358 C CA  . GLU D 62  ? 1.3791 1.1348 1.4738 -0.3191 0.0957  0.1438  62  GLU D CA  
20359 C C   . GLU D 62  ? 1.4043 1.0358 1.4560 -0.3144 0.0324  0.1352  62  GLU D C   
20360 O O   . GLU D 62  ? 1.4913 1.0143 1.4630 -0.3283 0.0087  0.1583  62  GLU D O   
20361 C CB  . GLU D 62  ? 1.4502 1.2825 1.6228 -0.3851 0.1201  0.1716  62  GLU D CB  
20362 C CG  . GLU D 62  ? 1.4987 1.4528 1.7010 -0.3916 0.1864  0.1846  62  GLU D CG  
20363 C CD  . GLU D 62  ? 1.5756 1.6295 1.8691 -0.4569 0.2131  0.2093  62  GLU D CD  
20364 O OE1 . GLU D 62  ? 1.6703 1.6828 1.9965 -0.5068 0.1765  0.2237  62  GLU D OE1 
20365 O OE2 . GLU D 62  ? 1.5956 1.7731 1.9293 -0.4570 0.2686  0.2128  62  GLU D OE2 
20372 N N   . ILE D 63  ? 1.3503 0.9890 1.4444 -0.2902 0.0011  0.0998  63  ILE D N   
20373 C CA  . ILE D 63  ? 1.4048 0.9312 1.4572 -0.2769 -0.0606 0.0847  63  ILE D CA  
20374 C C   . ILE D 63  ? 1.4351 0.8771 1.3935 -0.2298 -0.0805 0.0749  63  ILE D C   
20375 O O   . ILE D 63  ? 1.5556 0.8795 1.4446 -0.2393 -0.1212 0.0893  63  ILE D O   
20376 C CB  . ILE D 63  ? 1.3474 0.9070 1.4485 -0.2458 -0.0825 0.0428  63  ILE D CB  
20377 C CG1 . ILE D 63  ? 1.3556 0.9866 1.5501 -0.2913 -0.0752 0.0502  63  ILE D CG1 
20378 C CG2 . ILE D 63  ? 1.4265 0.8732 1.4724 -0.2179 -0.1445 0.0202  63  ILE D CG2 
20379 C CD1 . ILE D 63  ? 1.3110 0.9827 1.5498 -0.2597 -0.0910 0.0098  63  ILE D CD1 
20391 N N   . PHE D 64  ? 1.3546 0.8535 1.3090 -0.1784 -0.0577 0.0493  64  PHE D N   
20392 C CA  . PHE D 64  ? 1.3803 0.8233 1.2657 -0.1252 -0.0804 0.0293  64  PHE D CA  
20393 C C   . PHE D 64  ? 1.4246 0.8385 1.2496 -0.1271 -0.0615 0.0559  64  PHE D C   
20394 O O   . PHE D 64  ? 1.4164 0.8110 1.1974 -0.0791 -0.0733 0.0370  64  PHE D O   
20395 C CB  . PHE D 64  ? 1.2611 0.7834 1.1754 -0.0745 -0.0700 -0.0112 64  PHE D CB  
20396 C CG  . PHE D 64  ? 1.1895 0.7419 1.1521 -0.0708 -0.0844 -0.0375 64  PHE D CG  
20397 C CD1 . PHE D 64  ? 1.2024 0.7000 1.1371 -0.0371 -0.1279 -0.0673 64  PHE D CD1 
20398 C CD2 . PHE D 64  ? 1.1281 0.7606 1.1573 -0.0954 -0.0575 -0.0355 64  PHE D CD2 
20399 C CE1 . PHE D 64  ? 1.1700 0.6876 1.1364 -0.0319 -0.1416 -0.0915 64  PHE D CE1 
20400 C CE2 . PHE D 64  ? 1.0930 0.7414 1.1566 -0.0909 -0.0756 -0.0599 64  PHE D CE2 
20401 C CZ  . PHE D 64  ? 1.1190 0.7077 1.1481 -0.0609 -0.1164 -0.0864 64  PHE D CZ  
20411 N N   . ARG D 65  ? 1.4828 0.8972 1.3038 -0.1813 -0.0327 0.0985  65  ARG D N   
20412 C CA  . ARG D 65  ? 1.5922 0.9819 1.3471 -0.1824 -0.0094 0.1243  65  ARG D CA  
20413 C C   . ARG D 65  ? 1.7410 0.9964 1.3971 -0.1557 -0.0604 0.1230  65  ARG D C   
20414 O O   . ARG D 65  ? 1.7645 1.0056 1.3717 -0.1150 -0.0608 0.1138  65  ARG D O   
20415 C CB  . ARG D 65  ? 1.6549 1.0660 1.4151 -0.2509 0.0305  0.1726  65  ARG D CB  
20416 C CG  . ARG D 65  ? 1.8942 1.2061 1.6229 -0.3118 -0.0021 0.2077  65  ARG D CG  
20417 C CD  . ARG D 65  ? 1.9754 1.3503 1.7343 -0.3870 0.0484  0.2550  65  ARG D CD  
20418 N NE  . ARG D 65  ? 2.1324 1.3981 1.8374 -0.4573 0.0192  0.3008  65  ARG D NE  
20419 C CZ  . ARG D 65  ? 2.1993 1.4517 1.9552 -0.5101 -0.0089 0.3126  65  ARG D CZ  
20420 N NH1 . ARG D 65  ? 2.1068 1.4486 1.9691 -0.4961 -0.0110 0.2797  65  ARG D NH1 
20421 N NH2 . ARG D 65  ? 2.3534 1.4927 2.0468 -0.5796 -0.0401 0.3589  65  ARG D NH2 
20435 N N   . ASP D 66  ? 1.8386 0.9886 1.4618 -0.1750 -0.1110 0.1297  66  ASP D N   
20436 C CA  . ASP D 66  ? 1.9591 0.9677 1.4826 -0.1431 -0.1717 0.1230  66  ASP D CA  
20437 C C   . ASP D 66  ? 1.9642 0.9666 1.4980 -0.0708 -0.2171 0.0665  66  ASP D C   
20438 O O   . ASP D 66  ? 2.1025 1.0106 1.5625 -0.0243 -0.2675 0.0480  66  ASP D O   
20439 C CB  . ASP D 66  ? 2.0944 0.9684 1.5559 -0.2034 -0.2119 0.1627  66  ASP D CB  
20440 C CG  . ASP D 66  ? 2.1601 1.0059 1.5679 -0.2680 -0.1764 0.2214  66  ASP D CG  
20441 O OD1 . ASP D 66  ? 2.1986 1.0376 1.5506 -0.2419 -0.1578 0.2258  66  ASP D OD1 
20442 O OD2 . ASP D 66  ? 2.2558 1.0891 1.6762 -0.3466 -0.1671 0.2636  66  ASP D OD2 
20447 N N   . LYS D 67  ? 1.8241 0.9259 1.4434 -0.0579 -0.2014 0.0372  67  LYS D N   
20448 C CA  . LYS D 67  ? 1.7745 0.8825 1.4010 0.0079  -0.2377 -0.0158 67  LYS D CA  
20449 C C   . LYS D 67  ? 1.6112 0.8055 1.2526 0.0642  -0.2172 -0.0463 67  LYS D C   
20450 O O   . LYS D 67  ? 1.6255 0.7855 1.2284 0.1229  -0.2555 -0.0787 67  LYS D O   
20451 C CB  . LYS D 67  ? 1.7434 0.9138 1.4423 -0.0036 -0.2311 -0.0331 67  LYS D CB  
20452 C CG  . LYS D 67  ? 1.9575 1.0353 1.6445 -0.0509 -0.2684 -0.0125 67  LYS D CG  
20453 C CD  . LYS D 67  ? 1.9462 1.0846 1.7032 -0.0568 -0.2658 -0.0332 67  LYS D CD  
20454 C CE  . LYS D 67  ? 2.0739 1.1197 1.8245 -0.1085 -0.3086 -0.0115 67  LYS D CE  
20455 N NZ  . LYS D 67  ? 2.0186 1.1152 1.8340 -0.1132 -0.3120 -0.0325 67  LYS D NZ  
20469 N N   . ALA D 68  ? 1.4399 0.8504 1.0236 -0.0051 -0.2005 -0.1141 68  ALA D N   
20470 C CA  . ALA D 68  ? 1.3853 0.8377 0.9613 0.0324  -0.1947 -0.1144 68  ALA D CA  
20471 C C   . ALA D 68  ? 1.2780 0.7582 0.8935 0.0716  -0.1745 -0.0928 68  ALA D C   
20472 O O   . ALA D 68  ? 1.2850 0.7741 0.9440 0.0667  -0.1682 -0.0704 68  ALA D O   
20473 C CB  . ALA D 68  ? 1.3994 0.9189 0.9942 0.0115  -0.2244 -0.1050 68  ALA D CB  
20479 N N   . THR D 69  ? 1.2242 0.7175 0.8220 0.1088  -0.1636 -0.1001 69  THR D N   
20480 C CA  . THR D 69  ? 1.2117 0.7367 0.8337 0.1416  -0.1520 -0.0852 69  THR D CA  
20481 C C   . THR D 69  ? 1.1857 0.7603 0.8137 0.1565  -0.1584 -0.0923 69  THR D C   
20482 O O   . THR D 69  ? 1.1813 0.7456 0.7812 0.1682  -0.1558 -0.1085 69  THR D O   
20483 C CB  . THR D 69  ? 1.2535 0.7345 0.8487 0.1739  -0.1321 -0.0832 69  THR D CB  
20484 O OG1 . THR D 69  ? 1.2989 0.7639 0.8651 0.1961  -0.1268 -0.0997 69  THR D OG1 
20485 C CG2 . THR D 69  ? 1.3386 0.7584 0.9265 0.1576  -0.1206 -0.0770 69  THR D CG2 
20493 N N   . MET D 70  ? 1.1590 0.7824 0.8270 0.1563  -0.1612 -0.0798 70  MET D N   
20494 C CA  . MET D 70  ? 1.1141 0.7830 0.7980 0.1650  -0.1653 -0.0846 70  MET D CA  
20495 C C   . MET D 70  ? 1.1058 0.7894 0.7927 0.1925  -0.1569 -0.0873 70  MET D C   
20496 O O   . MET D 70  ? 1.1485 0.8225 0.8348 0.1983  -0.1483 -0.0790 70  MET D O   
20497 C CB  . MET D 70  ? 1.0552 0.7652 0.7863 0.1437  -0.1728 -0.0682 70  MET D CB  
20498 C CG  . MET D 70  ? 1.0485 0.7564 0.7784 0.1115  -0.1915 -0.0607 70  MET D CG  
20499 S SD  . MET D 70  ? 0.9979 0.7551 0.8059 0.0893  -0.1996 -0.0254 70  MET D SD  
20500 C CE  . MET D 70  ? 1.1420 0.8955 0.9311 0.0469  -0.2347 -0.0206 70  MET D CE  
20510 N N   . THR D 71  ? 1.0576 0.7647 0.7454 0.2070  -0.1595 -0.0985 71  THR D N   
20511 C CA  . THR D 71  ? 1.0686 0.7987 0.7626 0.2267  -0.1604 -0.1030 71  THR D CA  
20512 C C   . THR D 71  ? 1.0110 0.7848 0.7393 0.2236  -0.1629 -0.1104 71  THR D C   
20513 O O   . THR D 71  ? 1.0145 0.7972 0.7541 0.2118  -0.1614 -0.1088 71  THR D O   
20514 C CB  . THR D 71  ? 1.1319 0.8452 0.8011 0.2529  -0.1617 -0.1037 71  THR D CB  
20515 O OG1 . THR D 71  ? 1.1707 0.8801 0.8404 0.2597  -0.1568 -0.1106 71  THR D OG1 
20516 C CG2 . THR D 71  ? 1.2223 0.8861 0.8597 0.2564  -0.1546 -0.0925 71  THR D CG2 
20524 N N   . ALA D 72  ? 0.9581 0.7580 0.7002 0.2319  -0.1676 -0.1176 72  ALA D N   
20525 C CA  . ALA D 72  ? 0.9482 0.7872 0.7314 0.2260  -0.1675 -0.1248 72  ALA D CA  
20526 C C   . ALA D 72  ? 1.0046 0.8719 0.7985 0.2363  -0.1805 -0.1351 72  ALA D C   
20527 O O   . ALA D 72  ? 1.0752 0.9338 0.8410 0.2396  -0.1902 -0.1381 72  ALA D O   
20528 C CB  . ALA D 72  ? 0.9357 0.7792 0.7458 0.2072  -0.1571 -0.1221 72  ALA D CB  
20534 N N   . ASP D 73  ? 0.9960 0.8991 0.8302 0.2394  -0.1815 -0.1382 73  ASP D N   
20535 C CA  . ASP D 73  ? 1.0020 0.9465 0.8667 0.2440  -0.1985 -0.1455 73  ASP D CA  
20536 C C   . ASP D 73  ? 0.9847 0.9536 0.8949 0.2217  -0.1935 -0.1573 73  ASP D C   
20537 O O   . ASP D 73  ? 0.9748 0.9617 0.9263 0.2190  -0.1786 -0.1525 73  ASP D O   
20538 C CB  . ASP D 73  ? 1.0206 0.9890 0.9128 0.2667  -0.1975 -0.1356 73  ASP D CB  
20539 C CG  . ASP D 73  ? 1.0840 1.1094 1.0266 0.2706  -0.2198 -0.1365 73  ASP D CG  
20540 O OD1 . ASP D 73  ? 1.1143 1.1564 1.0595 0.2507  -0.2397 -0.1500 73  ASP D OD1 
20541 O OD2 . ASP D 73  ? 1.1141 1.1670 1.0956 0.2925  -0.2166 -0.1235 73  ASP D OD2 
20546 N N   . THR D 74  ? 1.0106 0.9729 0.9082 0.2053  -0.2016 -0.1730 74  THR D N   
20547 C CA  . THR D 74  ? 0.9883 0.9581 0.9267 0.1820  -0.1902 -0.1869 74  THR D CA  
20548 C C   . THR D 74  ? 0.9860 1.0066 0.9877 0.1754  -0.2013 -0.1929 74  THR D C   
20549 O O   . THR D 74  ? 0.9688 0.9989 1.0223 0.1613  -0.1829 -0.1945 74  THR D O   
20550 C CB  . THR D 74  ? 1.0476 0.9867 0.9471 0.1651  -0.1912 -0.2083 74  THR D CB  
20551 O OG1 . THR D 74  ? 1.1241 1.0793 0.9892 0.1651  -0.2247 -0.2200 74  THR D OG1 
20552 C CG2 . THR D 74  ? 1.0603 0.9519 0.9143 0.1714  -0.1711 -0.1980 74  THR D CG2 
20560 N N   . SER D 75  ? 1.0355 1.0922 1.0429 0.1860  -0.2299 -0.1914 75  SER D N   
20561 C CA  . SER D 75  ? 1.0655 1.1805 1.1481 0.1773  -0.2435 -0.1943 75  SER D CA  
20562 C C   . SER D 75  ? 1.0197 1.1551 1.1612 0.1895  -0.2145 -0.1757 75  SER D C   
20563 O O   . SER D 75  ? 1.0388 1.2123 1.2540 0.1757  -0.2091 -0.1775 75  SER D O   
20564 C CB  . SER D 75  ? 1.1310 1.2887 1.2156 0.1898  -0.2832 -0.1874 75  SER D CB  
20565 O OG  . SER D 75  ? 1.2078 1.3587 1.2748 0.2258  -0.2759 -0.1623 75  SER D OG  
20571 N N   . SER D 76  ? 0.9782 1.0855 1.0848 0.2126  -0.1939 -0.1589 76  SER D N   
20572 C CA  . SER D 76  ? 0.9572 1.0724 1.0950 0.2242  -0.1628 -0.1430 76  SER D CA  
20573 C C   . SER D 76  ? 0.9333 1.0101 1.0421 0.2147  -0.1370 -0.1374 76  SER D C   
20574 O O   . SER D 76  ? 0.9382 1.0147 1.0537 0.2219  -0.1111 -0.1234 76  SER D O   
20575 C CB  . SER D 76  ? 0.9433 1.0519 1.0587 0.2562  -0.1565 -0.1295 76  SER D CB  
20576 O OG  . SER D 76  ? 0.9825 1.0389 1.0195 0.2630  -0.1608 -0.1306 76  SER D OG  
20582 N N   . SER D 77  ? 0.8822 0.9282 0.9595 0.1997  -0.1422 -0.1448 77  SER D N   
20583 C CA  . SER D 77  ? 0.8288 0.8468 0.8894 0.1921  -0.1227 -0.1316 77  SER D CA  
20584 C C   . SER D 77  ? 0.8356 0.8317 0.8439 0.2058  -0.1169 -0.1174 77  SER D C   
20585 O O   . SER D 77  ? 0.8209 0.8147 0.8251 0.2039  -0.1000 -0.1014 77  SER D O   
20586 C CB  . SER D 77  ? 0.8190 0.8558 0.9393 0.1798  -0.1002 -0.1223 77  SER D CB  
20587 O OG  . SER D 77  ? 0.8351 0.8786 0.9990 0.1608  -0.1031 -0.1402 77  SER D OG  
20593 N N   . THR D 78  ? 0.8626 0.8381 0.8251 0.2178  -0.1310 -0.1235 78  THR D N   
20594 C CA  . THR D 78  ? 0.8985 0.8429 0.8068 0.2273  -0.1255 -0.1173 78  THR D CA  
20595 C C   . THR D 78  ? 0.8946 0.8030 0.7571 0.2225  -0.1389 -0.1181 78  THR D C   
20596 O O   . THR D 78  ? 0.8978 0.8027 0.7570 0.2265  -0.1513 -0.1252 78  THR D O   
20597 C CB  . THR D 78  ? 0.9494 0.8974 0.8570 0.2511  -0.1190 -0.1210 78  THR D CB  
20598 O OG1 . THR D 78  ? 0.9705 0.9572 0.9335 0.2559  -0.1020 -0.1167 78  THR D OG1 
20599 C CG2 . THR D 78  ? 0.9887 0.8886 0.8314 0.2580  -0.1063 -0.1209 78  THR D CG2 
20607 N N   . ALA D 79  ? 0.8876 0.7706 0.7136 0.2118  -0.1371 -0.1093 79  ALA D N   
20608 C CA  . ALA D 79  ? 0.8819 0.7311 0.6710 0.2045  -0.1479 -0.1075 79  ALA D CA  
20609 C C   . ALA D 79  ? 0.8936 0.7035 0.6289 0.2110  -0.1446 -0.1150 79  ALA D C   
20610 O O   . ALA D 79  ? 0.9275 0.7311 0.6410 0.2122  -0.1326 -0.1178 79  ALA D O   
20611 C CB  . ALA D 79  ? 0.9099 0.7632 0.7082 0.1825  -0.1530 -0.0896 79  ALA D CB  
20617 N N   . TYR D 80  ? 0.9207 0.6975 0.6313 0.2150  -0.1500 -0.1186 80  TYR D N   
20618 C CA  . TYR D 80  ? 0.9714 0.6982 0.6330 0.2206  -0.1423 -0.1275 80  TYR D CA  
20619 C C   . TYR D 80  ? 1.0026 0.6935 0.6364 0.1970  -0.1531 -0.1246 80  TYR D C   
20620 O O   . TYR D 80  ? 0.9880 0.6903 0.6463 0.1895  -0.1620 -0.1135 80  TYR D O   
20621 C CB  . TYR D 80  ? 0.9658 0.6817 0.6322 0.2512  -0.1351 -0.1298 80  TYR D CB  
20622 C CG  . TYR D 80  ? 0.9404 0.6998 0.6488 0.2742  -0.1284 -0.1292 80  TYR D CG  
20623 C CD1 . TYR D 80  ? 0.9400 0.7497 0.6936 0.2761  -0.1432 -0.1249 80  TYR D CD1 
20624 C CD2 . TYR D 80  ? 0.9740 0.7220 0.6787 0.2921  -0.1048 -0.1336 80  TYR D CD2 
20625 C CE1 . TYR D 80  ? 0.9462 0.8020 0.7485 0.2915  -0.1419 -0.1236 80  TYR D CE1 
20626 C CE2 . TYR D 80  ? 0.9813 0.7770 0.7412 0.3128  -0.0971 -0.1282 80  TYR D CE2 
20627 C CZ  . TYR D 80  ? 0.9653 0.8189 0.7780 0.3106  -0.1193 -0.1224 80  TYR D CZ  
20628 O OH  . TYR D 80  ? 0.9953 0.9025 0.8728 0.3257  -0.1164 -0.1164 80  TYR D OH  
20638 N N   . MET D 81  ? 1.1007 0.7457 0.6834 0.1833  -0.1498 -0.1356 81  MET D N   
20639 C CA  . MET D 81  ? 1.2087 0.8118 0.7668 0.1593  -0.1597 -0.1364 81  MET D CA  
20640 C C   . MET D 81  ? 1.2498 0.7816 0.7569 0.1676  -0.1406 -0.1559 81  MET D C   
20641 O O   . MET D 81  ? 1.2863 0.7955 0.7587 0.1782  -0.1219 -0.1716 81  MET D O   
20642 C CB  . MET D 81  ? 1.2893 0.9033 0.8346 0.1196  -0.1821 -0.1309 81  MET D CB  
20643 C CG  . MET D 81  ? 1.3706 0.9496 0.9060 0.0895  -0.1964 -0.1301 81  MET D CG  
20644 S SD  . MET D 81  ? 1.4924 1.1056 1.0335 0.0398  -0.2348 -0.1136 81  MET D SD  
20645 C CE  . MET D 81  ? 1.5984 1.1781 1.0439 0.0275  -0.2345 -0.1397 81  MET D CE  
20655 N N   . GLN D 82  ? 1.2138 0.7054 0.7185 0.1636  -0.1395 -0.1534 82  GLN D N   
20656 C CA  . GLN D 82  ? 1.2792 0.6928 0.7429 0.1720  -0.1168 -0.1690 82  GLN D CA  
20657 C C   . GLN D 82  ? 1.3576 0.7218 0.7948 0.1289  -0.1281 -0.1773 82  GLN D C   
20658 O O   . GLN D 82  ? 1.3369 0.7196 0.8111 0.1131  -0.1430 -0.1589 82  GLN D O   
20659 C CB  . GLN D 82  ? 1.2671 0.6738 0.7581 0.2120  -0.1011 -0.1530 82  GLN D CB  
20660 C CG  . GLN D 82  ? 1.3730 0.7017 0.8341 0.2326  -0.0695 -0.1627 82  GLN D CG  
20661 C CD  . GLN D 82  ? 1.3362 0.6695 0.8285 0.2761  -0.0586 -0.1370 82  GLN D CD  
20662 O OE1 . GLN D 82  ? 1.2981 0.6507 0.8092 0.2760  -0.0716 -0.1160 82  GLN D OE1 
20663 N NE2 . GLN D 82  ? 1.3891 0.7067 0.8875 0.3147  -0.0332 -0.1352 82  GLN D NE2 
20672 N N   . LEU D 83  ? 1.4436 0.7435 0.8171 0.1078  -0.1192 -0.2058 83  LEU D N   
20673 C CA  . LEU D 83  ? 1.5684 0.8112 0.9099 0.0606  -0.1312 -0.2207 83  LEU D CA  
20674 C C   . LEU D 83  ? 1.7359 0.8857 1.0564 0.0761  -0.0952 -0.2336 83  LEU D C   
20675 O O   . LEU D 83  ? 1.8537 0.9535 1.1382 0.1055  -0.0598 -0.2510 83  LEU D O   
20676 C CB  . LEU D 83  ? 1.5963 0.8192 0.8655 0.0194  -0.1474 -0.2482 83  LEU D CB  
20677 C CG  . LEU D 83  ? 1.4908 0.8031 0.7783 0.0070  -0.1807 -0.2295 83  LEU D CG  
20678 C CD1 . LEU D 83  ? 1.5416 0.8275 0.7390 -0.0296 -0.1941 -0.2546 83  LEU D CD1 
20679 C CD2 . LEU D 83  ? 1.4002 0.7766 0.7622 -0.0174 -0.2169 -0.1971 83  LEU D CD2 
20691 N N   . SER D 84  ? 1.7099 0.8356 1.0593 0.0584  -0.0994 -0.2214 84  SER D N   
20692 C CA  . SER D 84  ? 1.7510 0.7909 1.0940 0.0764  -0.0630 -0.2236 84  SER D CA  
20693 C C   . SER D 84  ? 1.7758 0.7405 1.0933 0.0200  -0.0682 -0.2454 84  SER D C   
20694 O O   . SER D 84  ? 1.7420 0.7447 1.0775 -0.0298 -0.1069 -0.2427 84  SER D O   
20695 C CB  . SER D 84  ? 1.7307 0.8055 1.1348 0.1142  -0.0553 -0.1821 84  SER D CB  
20696 O OG  . SER D 84  ? 1.6644 0.8109 1.1155 0.0915  -0.0858 -0.1594 84  SER D OG  
20702 N N   . GLY D 85  ? 1.2582 0.7229 0.9498 0.0250  0.0559  0.0141  85  GLY D N   
20703 C CA  . GLY D 85  ? 1.3524 0.7502 1.0582 0.0036  0.0359  0.0095  85  GLY D CA  
20704 C C   . GLY D 85  ? 1.4398 0.8064 1.1334 -0.0002 -0.0033 -0.0176 85  GLY D C   
20705 O O   . GLY D 85  ? 1.4607 0.8150 1.2048 -0.0298 -0.0282 -0.0262 85  GLY D O   
20709 N N   . LEU D 86  ? 1.4728 0.8257 1.0994 0.0324  -0.0088 -0.0295 86  LEU D N   
20710 C CA  . LEU D 86  ? 1.5185 0.8508 1.1222 0.0380  -0.0409 -0.0537 86  LEU D CA  
20711 C C   . LEU D 86  ? 1.6276 0.8706 1.2162 0.0268  -0.0790 -0.0709 86  LEU D C   
20712 O O   . LEU D 86  ? 1.7153 0.8973 1.2844 0.0267  -0.0790 -0.0653 86  LEU D O   
20713 C CB  . LEU D 86  ? 1.5197 0.8530 1.0517 0.0810  -0.0309 -0.0562 86  LEU D CB  
20714 C CG  . LEU D 86  ? 1.4172 0.8392 0.9721 0.0894  -0.0067 -0.0455 86  LEU D CG  
20715 C CD1 . LEU D 86  ? 1.4160 0.8395 0.9119 0.1317  0.0096  -0.0391 86  LEU D CD1 
20716 C CD2 . LEU D 86  ? 1.3442 0.8047 0.9373 0.0722  -0.0242 -0.0586 86  LEU D CD2 
20728 N N   . THR D 87  ? 1.6183 0.8506 1.2150 0.0179  -0.1147 -0.0929 87  THR D N   
20729 C CA  . THR D 87  ? 1.6725 0.8169 1.2504 0.0099  -0.1619 -0.1151 87  THR D CA  
20730 C C   . THR D 87  ? 1.6978 0.8203 1.2150 0.0369  -0.1895 -0.1399 87  THR D C   
20731 O O   . THR D 87  ? 1.6835 0.8573 1.1759 0.0614  -0.1666 -0.1356 87  THR D O   
20732 C CB  . THR D 87  ? 1.6778 0.8324 1.3561 -0.0397 -0.1847 -0.1142 87  THR D CB  
20733 O OG1 . THR D 87  ? 1.6630 0.8790 1.3890 -0.0528 -0.1970 -0.1228 87  THR D OG1 
20734 C CG2 . THR D 87  ? 1.6360 0.8333 1.3801 -0.0625 -0.1450 -0.0828 87  THR D CG2 
20742 N N   . SER D 88  ? 1.7970 0.8397 1.2904 0.0334  -0.2405 -0.1654 88  SER D N   
20743 C CA  . SER D 88  ? 1.8246 0.8397 1.2575 0.0602  -0.2708 -0.1899 88  SER D CA  
20744 C C   . SER D 88  ? 1.8013 0.8887 1.3056 0.0359  -0.2820 -0.1944 88  SER D C   
20745 O O   . SER D 88  ? 1.7594 0.8519 1.2183 0.0618  -0.2904 -0.2066 88  SER D O   
20746 C CB  . SER D 88  ? 1.8957 0.7922 1.2704 0.0682  -0.3283 -0.2189 88  SER D CB  
20747 O OG  . SER D 88  ? 1.9097 0.7954 1.3741 0.0188  -0.3685 -0.2266 88  SER D OG  
20753 N N   . GLU D 89  ? 1.7951 0.9372 1.4081 -0.0102 -0.2799 -0.1827 89  GLU D N   
20754 C CA  . GLU D 89  ? 1.7932 1.0097 1.4780 -0.0318 -0.2856 -0.1838 89  GLU D CA  
20755 C C   . GLU D 89  ? 1.6506 0.9560 1.3405 -0.0187 -0.2367 -0.1656 89  GLU D C   
20756 O O   . GLU D 89  ? 1.6135 0.9726 1.3370 -0.0247 -0.2404 -0.1692 89  GLU D O   
20757 C CB  . GLU D 89  ? 1.8633 1.1099 1.6654 -0.0819 -0.2951 -0.1732 89  GLU D CB  
20758 C CG  . GLU D 89  ? 2.0339 1.2026 1.8574 -0.1034 -0.3550 -0.1932 89  GLU D CG  
20759 C CD  . GLU D 89  ? 2.0859 1.2828 1.9785 -0.1264 -0.3970 -0.2079 89  GLU D CD  
20760 O OE1 . GLU D 89  ? 2.1114 1.3839 2.1125 -0.1600 -0.3810 -0.1888 89  GLU D OE1 
20761 O OE2 . GLU D 89  ? 2.2205 1.3629 2.0555 -0.1075 -0.4453 -0.2378 89  GLU D OE2 
20768 N N   . ASP D 90  ? 1.5497 0.8696 1.2089 -0.0009 -0.1942 -0.1465 90  ASP D N   
20769 C CA  . ASP D 90  ? 1.3600 0.7561 1.0200 0.0137  -0.1542 -0.1309 90  ASP D CA  
20770 C C   . ASP D 90  ? 1.3203 0.7023 0.9013 0.0551  -0.1520 -0.1385 90  ASP D C   
20771 O O   . ASP D 90  ? 1.2433 0.6875 0.8314 0.0658  -0.1247 -0.1268 90  ASP D O   
20772 C CB  . ASP D 90  ? 1.2978 0.7180 0.9634 0.0161  -0.1132 -0.1067 90  ASP D CB  
20773 C CG  . ASP D 90  ? 1.2485 0.6985 0.9950 -0.0204 -0.1031 -0.0921 90  ASP D CG  
20774 O OD1 . ASP D 90  ? 1.2246 0.7171 1.0377 -0.0458 -0.1122 -0.0937 90  ASP D OD1 
20775 O OD2 . ASP D 90  ? 1.2676 0.6982 1.0101 -0.0210 -0.0837 -0.0769 90  ASP D OD2 
20780 N N   . SER D 91  ? 1.3858 0.6850 0.8915 0.0803  -0.1795 -0.1563 91  SER D N   
20781 C CA  . SER D 91  ? 1.4021 0.6832 0.8287 0.1245  -0.1749 -0.1608 91  SER D CA  
20782 C C   . SER D 91  ? 1.3821 0.7029 0.8338 0.1188  -0.1887 -0.1698 91  SER D C   
20783 O O   . SER D 91  ? 1.4120 0.7030 0.8766 0.1035  -0.2311 -0.1908 91  SER D O   
20784 C CB  . SER D 91  ? 1.4796 0.6524 0.8111 0.1563  -0.2046 -0.1799 91  SER D CB  
20785 O OG  . SER D 91  ? 1.5240 0.6528 0.8330 0.1599  -0.1952 -0.1730 91  SER D OG  
20791 N N   . ALA D 92  ? 1.3167 0.7035 0.7780 0.1311  -0.1553 -0.1536 92  ALA D N   
20792 C CA  . ALA D 92  ? 1.3296 0.7576 0.8169 0.1258  -0.1635 -0.1589 92  ALA D CA  
20793 C C   . ALA D 92  ? 1.2600 0.7522 0.7531 0.1423  -0.1230 -0.1372 92  ALA D C   
20794 O O   . ALA D 92  ? 1.2560 0.7642 0.7390 0.1566  -0.0909 -0.1182 92  ALA D O   
20795 C CB  . ALA D 92  ? 1.3346 0.8078 0.9147 0.0792  -0.1797 -0.1636 92  ALA D CB  
20801 N N   . VAL D 93  ? 1.2179 0.7460 0.7309 0.1404  -0.1261 -0.1391 93  VAL D N   
20802 C CA  . VAL D 93  ? 1.1892 0.7830 0.7272 0.1469  -0.0921 -0.1184 93  VAL D CA  
20803 C C   . VAL D 93  ? 1.1430 0.8059 0.7674 0.1075  -0.0864 -0.1136 93  VAL D C   
20804 O O   . VAL D 93  ? 1.1677 0.8376 0.8321 0.0813  -0.1098 -0.1272 93  VAL D O   
20805 C CB  . VAL D 93  ? 1.1776 0.7658 0.6828 0.1705  -0.0959 -0.1208 93  VAL D CB  
20806 C CG1 . VAL D 93  ? 1.0602 0.7187 0.6076 0.1695  -0.0640 -0.0986 93  VAL D CG1 
20807 C CG2 . VAL D 93  ? 1.3034 0.8201 0.7116 0.2182  -0.0954 -0.1219 93  VAL D CG2 
20817 N N   . TYR D 94  ? 1.0718 0.7843 0.7244 0.1060  -0.0563 -0.0939 94  TYR D N   
20818 C CA  . TYR D 94  ? 0.9869 0.7583 0.7076 0.0762  -0.0488 -0.0886 94  TYR D CA  
20819 C C   . TYR D 94  ? 0.9449 0.7676 0.6892 0.0803  -0.0337 -0.0772 94  TYR D C   
20820 O O   . TYR D 94  ? 0.9161 0.7513 0.6483 0.0999  -0.0133 -0.0606 94  TYR D O   
20821 C CB  . TYR D 94  ? 0.9863 0.7640 0.7176 0.0703  -0.0330 -0.0777 94  TYR D CB  
20822 C CG  . TYR D 94  ? 1.0497 0.7799 0.7725 0.0589  -0.0479 -0.0872 94  TYR D CG  
20823 C CD1 . TYR D 94  ? 1.0423 0.7867 0.8165 0.0284  -0.0573 -0.0918 94  TYR D CD1 
20824 C CD2 . TYR D 94  ? 1.1188 0.7879 0.7841 0.0796  -0.0520 -0.0898 94  TYR D CD2 
20825 C CE1 . TYR D 94  ? 1.0861 0.7881 0.8642 0.0150  -0.0707 -0.0970 94  TYR D CE1 
20826 C CE2 . TYR D 94  ? 1.1681 0.7879 0.8287 0.0671  -0.0689 -0.0987 94  TYR D CE2 
20827 C CZ  . TYR D 94  ? 1.1614 0.7993 0.8833 0.0327  -0.0786 -0.1014 94  TYR D CZ  
20828 O OH  . TYR D 94  ? 1.2142 0.8045 0.9430 0.0173  -0.0950 -0.1067 94  TYR D OH  
20838 N N   . TYR D 95  ? 0.9589 0.8106 0.7410 0.0622  -0.0441 -0.0847 95  TYR D N   
20839 C CA  . TYR D 95  ? 0.9066 0.8007 0.7134 0.0630  -0.0344 -0.0762 95  TYR D CA  
20840 C C   . TYR D 95  ? 0.8568 0.7973 0.7130 0.0426  -0.0276 -0.0716 95  TYR D C   
20841 O O   . TYR D 95  ? 0.8248 0.7686 0.7016 0.0252  -0.0327 -0.0780 95  TYR D O   
20842 C CB  . TYR D 95  ? 0.8728 0.7626 0.6799 0.0617  -0.0515 -0.0881 95  TYR D CB  
20843 C CG  . TYR D 95  ? 0.8915 0.7320 0.6404 0.0879  -0.0606 -0.0935 95  TYR D CG  
20844 C CD1 . TYR D 95  ? 0.8898 0.7275 0.6099 0.1148  -0.0428 -0.0785 95  TYR D CD1 
20845 C CD2 . TYR D 95  ? 0.9502 0.7446 0.6729 0.0875  -0.0879 -0.1127 95  TYR D CD2 
20846 C CE1 . TYR D 95  ? 0.9659 0.7531 0.6215 0.1455  -0.0484 -0.0820 95  TYR D CE1 
20847 C CE2 . TYR D 95  ? 0.9980 0.7387 0.6559 0.1163  -0.1007 -0.1204 95  TYR D CE2 
20848 C CZ  . TYR D 95  ? 1.0091 0.7448 0.6280 0.1477  -0.0791 -0.1049 95  TYR D CZ  
20849 O OH  . TYR D 95  ? 1.0977 0.7745 0.6410 0.1829  -0.0890 -0.1111 95  TYR D OH  
20859 N N   . CYS D 96  ? 0.8647 0.8382 0.7393 0.0466  -0.0162 -0.0593 96  CYS D N   
20860 C CA  . CYS D 96  ? 0.8504 0.8619 0.7643 0.0312  -0.0166 -0.0588 96  CYS D CA  
20861 C C   . CYS D 96  ? 0.8532 0.8805 0.7847 0.0276  -0.0235 -0.0623 96  CYS D C   
20862 O O   . CYS D 96  ? 0.8202 0.8389 0.7387 0.0403  -0.0209 -0.0566 96  CYS D O   
20863 C CB  . CYS D 96  ? 0.8366 0.8705 0.7626 0.0366  -0.0061 -0.0443 96  CYS D CB  
20864 S SG  . CYS D 96  ? 0.8637 0.9106 0.7969 0.0541  0.0049  -0.0243 96  CYS D SG  
20869 N N   . ALA D 97  ? 0.8960 0.9434 0.8531 0.0135  -0.0304 -0.0702 97  ALA D N   
20870 C CA  . ALA D 97  ? 0.8919 0.9508 0.8638 0.0104  -0.0380 -0.0748 97  ALA D CA  
20871 C C   . ALA D 97  ? 0.8427 0.9252 0.8385 0.0013  -0.0410 -0.0778 97  ALA D C   
20872 O O   . ALA D 97  ? 0.9025 0.9888 0.9015 -0.0043 -0.0396 -0.0825 97  ALA D O   
20873 C CB  . ALA D 97  ? 0.9163 0.9602 0.8818 0.0080  -0.0496 -0.0878 97  ALA D CB  
20879 N N   . SER D 98  ? 0.7739 0.8678 0.7841 0.0018  -0.0449 -0.0740 98  SER D N   
20880 C CA  . SER D 98  ? 0.7157 0.8225 0.7399 -0.0034 -0.0527 -0.0795 98  SER D CA  
20881 C C   . SER D 98  ? 0.6898 0.7971 0.7154 -0.0063 -0.0575 -0.0919 98  SER D C   
20882 O O   . SER D 98  ? 0.7002 0.8015 0.7236 -0.0063 -0.0586 -0.0959 98  SER D O   
20883 C CB  . SER D 98  ? 0.7150 0.8287 0.7589 -0.0038 -0.0599 -0.0719 98  SER D CB  
20884 O OG  . SER D 98  ? 0.7353 0.8438 0.7838 -0.0023 -0.0596 -0.0690 98  SER D OG  
20890 N N   . PHE D 99  ? 0.6321 0.7452 0.6592 -0.0059 -0.0614 -0.0978 99  PHE D N   
20891 C CA  . PHE D 99  ? 0.5975 0.7146 0.6267 -0.0045 -0.0616 -0.1067 99  PHE D CA  
20892 C C   . PHE D 99  ? 0.6415 0.7555 0.6746 -0.0024 -0.0731 -0.1119 99  PHE D C   
20893 O O   . PHE D 99  ? 0.6638 0.7720 0.6939 -0.0004 -0.0826 -0.1132 99  PHE D O   
20894 C CB  . PHE D 99  ? 0.6685 0.7880 0.6871 0.0016  -0.0545 -0.1077 99  PHE D CB  
20895 C CG  . PHE D 99  ? 0.6733 0.8019 0.6995 0.0054  -0.0455 -0.1104 99  PHE D CG  
20896 C CD1 . PHE D 99  ? 0.6758 0.8131 0.7245 -0.0009 -0.0458 -0.1118 99  PHE D CD1 
20897 C CD2 . PHE D 99  ? 0.6864 0.8146 0.6970 0.0184  -0.0368 -0.1102 99  PHE D CD2 
20898 C CE1 . PHE D 99  ? 0.6854 0.8377 0.7531 0.0025  -0.0374 -0.1112 99  PHE D CE1 
20899 C CE2 . PHE D 99  ? 0.7040 0.8446 0.7266 0.0251  -0.0233 -0.1079 99  PHE D CE2 
20900 C CZ  . PHE D 99  ? 0.7090 0.8653 0.7663 0.0155  -0.0234 -0.1074 99  PHE D CZ  
20910 N N   . LEU D 100 ? 0.6576 0.7723 0.6971 -0.0023 -0.0750 -0.1154 100 LEU D N   
20911 C CA  . LEU D 100 ? 0.6568 0.7658 0.6974 0.0016  -0.0844 -0.1201 100 LEU D CA  
20912 C C   . LEU D 100 ? 0.6709 0.7807 0.7043 0.0096  -0.0858 -0.1284 100 LEU D C   
20913 O O   . LEU D 100 ? 0.6940 0.7903 0.7199 0.0140  -0.0966 -0.1331 100 LEU D O   
20914 C CB  . LEU D 100 ? 0.6571 0.7653 0.7014 0.0038  -0.0868 -0.1222 100 LEU D CB  
20915 C CG  . LEU D 100 ? 0.6455 0.7452 0.6886 0.0099  -0.0951 -0.1261 100 LEU D CG  
20916 C CD1 . LEU D 100 ? 0.6871 0.7722 0.7312 0.0073  -0.0995 -0.1183 100 LEU D CD1 
20917 C CD2 . LEU D 100 ? 0.6856 0.7840 0.7279 0.0153  -0.0988 -0.1284 100 LEU D CD2 
20929 N N   . GLY D 101 ? 0.6481 0.7703 0.6829 0.0132  -0.0742 -0.1287 101 GLY D N   
20930 C CA  . GLY D 101 ? 0.6685 0.7966 0.7013 0.0255  -0.0690 -0.1331 101 GLY D CA  
20931 C C   . GLY D 101 ? 0.6319 0.7772 0.6908 0.0239  -0.0673 -0.1332 101 GLY D C   
20932 O O   . GLY D 101 ? 0.5927 0.7389 0.6634 0.0144  -0.0737 -0.1324 101 GLY D O   
20936 N N   . ARG D 102 ? 0.6387 0.7962 0.7047 0.0364  -0.0596 -0.1338 102 ARG D N   
20937 C CA  . ARG D 102 ? 0.6564 0.8356 0.7557 0.0365  -0.0603 -0.1332 102 ARG D CA  
20938 C C   . ARG D 102 ? 0.6382 0.8312 0.7689 0.0206  -0.0608 -0.1282 102 ARG D C   
20939 O O   . ARG D 102 ? 0.6204 0.8190 0.7715 0.0155  -0.0745 -0.1317 102 ARG D O   
20940 C CB  . ARG D 102 ? 0.6708 0.8383 0.7633 0.0394  -0.0773 -0.1410 102 ARG D CB  
20941 C CG  . ARG D 102 ? 0.6460 0.7855 0.7044 0.0471  -0.0845 -0.1465 102 ARG D CG  
20942 C CD  . ARG D 102 ? 0.6632 0.7976 0.7026 0.0656  -0.0767 -0.1492 102 ARG D CD  
20943 N NE  . ARG D 102 ? 0.6688 0.8288 0.7297 0.0792  -0.0649 -0.1460 102 ARG D NE  
20944 C CZ  . ARG D 102 ? 0.6885 0.8521 0.7570 0.0891  -0.0714 -0.1495 102 ARG D CZ  
20945 N NH1 . ARG D 102 ? 0.7136 0.9066 0.8099 0.1024  -0.0592 -0.1438 102 ARG D NH1 
20946 N NH2 . ARG D 102 ? 0.6910 0.8301 0.7429 0.0869  -0.0884 -0.1563 102 ARG D NH2 
20960 N N   . GLY D 103 ? 0.6525 0.8460 0.7835 0.0141  -0.0486 -0.1208 103 GLY D N   
20961 C CA  . GLY D 103 ? 0.5954 0.7954 0.7549 -0.0010 -0.0501 -0.1162 103 GLY D CA  
20962 C C   . GLY D 103 ? 0.5774 0.7575 0.7245 -0.0096 -0.0701 -0.1238 103 GLY D C   
20963 O O   . GLY D 103 ? 0.5807 0.7616 0.7511 -0.0186 -0.0817 -0.1254 103 GLY D O   
20967 N N   . ALA D 104 ? 0.6099 0.7699 0.7210 -0.0053 -0.0749 -0.1274 104 ALA D N   
20968 C CA  . ALA D 104 ? 0.6145 0.7532 0.7064 -0.0070 -0.0876 -0.1304 104 ALA D CA  
20969 C C   . ALA D 104 ? 0.5973 0.7215 0.6641 -0.0079 -0.0799 -0.1244 104 ALA D C   
20970 O O   . ALA D 104 ? 0.6213 0.7501 0.6836 -0.0069 -0.0709 -0.1209 104 ALA D O   
20971 C CB  . ALA D 104 ? 0.6500 0.7814 0.7310 0.0023  -0.0988 -0.1356 104 ALA D CB  
20977 N N   . MET D 105 ? 0.6184 0.7236 0.6670 -0.0067 -0.0845 -0.1228 105 MET D N   
20978 C CA  . MET D 105 ? 0.7037 0.7983 0.7339 -0.0054 -0.0759 -0.1141 105 MET D CA  
20979 C C   . MET D 105 ? 0.7279 0.8080 0.7405 0.0041  -0.0777 -0.1089 105 MET D C   
20980 O O   . MET D 105 ? 0.7563 0.8179 0.7499 0.0122  -0.0836 -0.1109 105 MET D O   
20981 C CB  . MET D 105 ? 0.7574 0.8403 0.7800 -0.0087 -0.0732 -0.1124 105 MET D CB  
20982 C CG  . MET D 105 ? 0.7654 0.8616 0.8093 -0.0180 -0.0668 -0.1123 105 MET D CG  
20983 S SD  . MET D 105 ? 0.7907 0.8680 0.8373 -0.0256 -0.0712 -0.1133 105 MET D SD  
20984 C CE  . MET D 105 ? 0.7888 0.8652 0.8569 -0.0287 -0.0942 -0.1252 105 MET D CE  
20994 N N   . ASP D 106 ? 0.7230 0.8083 0.7414 0.0045  -0.0732 -0.1012 106 ASP D N   
20995 C CA  . ASP D 106 ? 0.7420 0.8170 0.7547 0.0126  -0.0722 -0.0927 106 ASP D CA  
20996 C C   . ASP D 106 ? 0.7045 0.7686 0.7040 0.0216  -0.0600 -0.0766 106 ASP D C   
20997 O O   . ASP D 106 ? 0.7073 0.7549 0.6882 0.0351  -0.0557 -0.0693 106 ASP D O   
20998 C CB  . ASP D 106 ? 0.7466 0.8290 0.7794 0.0074  -0.0756 -0.0902 106 ASP D CB  
20999 C CG  . ASP D 106 ? 0.7318 0.8255 0.7787 -0.0007 -0.0762 -0.0886 106 ASP D CG  
21000 O OD1 . ASP D 106 ? 0.7418 0.8400 0.7834 -0.0019 -0.0703 -0.0872 106 ASP D OD1 
21001 O OD2 . ASP D 106 ? 0.7090 0.8028 0.7694 -0.0046 -0.0850 -0.0896 106 ASP D OD2 
21006 N N   . TYR D 107 ? 0.6804 0.7522 0.6859 0.0182  -0.0524 -0.0693 107 TYR D N   
21007 C CA  . TYR D 107 ? 0.7023 0.7678 0.6994 0.0299  -0.0375 -0.0507 107 TYR D CA  
21008 C C   . TYR D 107 ? 0.7679 0.8247 0.7437 0.0336  -0.0333 -0.0530 107 TYR D C   
21009 O O   . TYR D 107 ? 0.7880 0.8556 0.7742 0.0227  -0.0370 -0.0598 107 TYR D O   
21010 C CB  . TYR D 107 ? 0.6384 0.7242 0.6736 0.0240  -0.0324 -0.0337 107 TYR D CB  
21011 C CG  . TYR D 107 ? 0.6150 0.7028 0.6732 0.0197  -0.0373 -0.0293 107 TYR D CG  
21012 C CD1 . TYR D 107 ? 0.6228 0.7000 0.6779 0.0324  -0.0240 -0.0116 107 TYR D CD1 
21013 C CD2 . TYR D 107 ? 0.6127 0.7077 0.6906 0.0059  -0.0542 -0.0419 107 TYR D CD2 
21014 C CE1 . TYR D 107 ? 0.6429 0.7181 0.7200 0.0280  -0.0275 -0.0056 107 TYR D CE1 
21015 C CE2 . TYR D 107 ? 0.6508 0.7410 0.7471 0.0023  -0.0607 -0.0387 107 TYR D CE2 
21016 C CZ  . TYR D 107 ? 0.6539 0.7350 0.7529 0.0116  -0.0474 -0.0202 107 TYR D CZ  
21017 O OH  . TYR D 107 ? 0.6704 0.7432 0.7888 0.0076  -0.0528 -0.0152 107 TYR D OH  
21027 N N   . TRP D 108 ? 0.8012 0.8333 0.7419 0.0521  -0.0250 -0.0467 108 TRP D N   
21028 C CA  . TRP D 108 ? 0.7932 0.8051 0.7041 0.0592  -0.0232 -0.0503 108 TRP D CA  
21029 C C   . TRP D 108 ? 0.7568 0.7656 0.6565 0.0778  -0.0022 -0.0283 108 TRP D C   
21030 O O   . TRP D 108 ? 0.7358 0.7455 0.6355 0.0928  0.0121  -0.0100 108 TRP D O   
21031 C CB  . TRP D 108 ? 0.8502 0.8248 0.7189 0.0698  -0.0367 -0.0654 108 TRP D CB  
21032 C CG  . TRP D 108 ? 0.8238 0.8032 0.7097 0.0519  -0.0579 -0.0859 108 TRP D CG  
21033 C CD1 . TRP D 108 ? 0.7929 0.7959 0.7094 0.0401  -0.0648 -0.0914 108 TRP D CD1 
21034 C CD2 . TRP D 108 ? 0.8159 0.7761 0.6940 0.0449  -0.0745 -0.1015 108 TRP D CD2 
21035 N NE1 . TRP D 108 ? 0.7924 0.7972 0.7230 0.0280  -0.0817 -0.1074 108 TRP D NE1 
21036 C CE2 . TRP D 108 ? 0.8027 0.7829 0.7153 0.0286  -0.0886 -0.1132 108 TRP D CE2 
21037 C CE3 . TRP D 108 ? 0.8425 0.7689 0.6906 0.0510  -0.0793 -0.1056 108 TRP D CE3 
21038 C CZ2 . TRP D 108 ? 0.8082 0.7817 0.7363 0.0163  -0.1062 -0.1261 108 TRP D CZ2 
21039 C CZ3 . TRP D 108 ? 0.9308 0.8445 0.7908 0.0370  -0.1001 -0.1208 108 TRP D CZ3 
21040 C CH2 . TRP D 108 ? 0.9083 0.8484 0.8129 0.0187  -0.1129 -0.1296 108 TRP D CH2 
21051 N N   . GLY D 109 ? 0.7569 0.7621 0.6483 0.0787  0.0018  -0.0275 109 GLY D N   
21052 C CA  . GLY D 109 ? 0.7344 0.7329 0.6087 0.1009  0.0222  -0.0072 109 GLY D CA  
21053 C C   . GLY D 109 ? 0.7679 0.7173 0.5771 0.1288  0.0259  -0.0094 109 GLY D C   
21054 O O   . GLY D 109 ? 0.7988 0.7175 0.5773 0.1283  0.0072  -0.0295 109 GLY D O   
21058 N N   . GLN D 110 ? 0.8347 0.7750 0.6216 0.1562  0.0490  0.0120  110 GLN D N   
21059 C CA  . GLN D 110 ? 0.9161 0.8028 0.6293 0.1915  0.0550  0.0122  110 GLN D CA  
21060 C C   . GLN D 110 ? 0.9770 0.8164 0.6413 0.1930  0.0354  -0.0112 110 GLN D C   
21061 O O   . GLN D 110 ? 1.0834 0.8669 0.6801 0.2182  0.0268  -0.0214 110 GLN D O   
21062 C CB  . GLN D 110 ? 0.9809 0.8719 0.6838 0.2253  0.0903  0.0456  110 GLN D CB  
21063 C CG  . GLN D 110 ? 1.0754 0.9685 0.7752 0.2335  0.1016  0.0542  110 GLN D CG  
21064 C CD  . GLN D 110 ? 1.1107 1.0665 0.8913 0.2091  0.1067  0.0685  110 GLN D CD  
21065 O OE1 . GLN D 110 ? 0.9961 0.9897 0.8337 0.1816  0.0966  0.0668  110 GLN D OE1 
21066 N NE2 . GLN D 110 ? 1.2326 1.1961 1.0149 0.2213  0.1200  0.0817  110 GLN D NE2 
21075 N N   . GLY D 111 ? 0.9556 0.8115 0.6502 0.1685  0.0273  -0.0192 111 GLY D N   
21076 C CA  . GLY D 111 ? 0.9454 0.7564 0.6025 0.1675  0.0108  -0.0375 111 GLY D CA  
21077 C C   . GLY D 111 ? 0.9292 0.7228 0.5569 0.1898  0.0294  -0.0237 111 GLY D C   
21078 O O   . GLY D 111 ? 0.9510 0.7443 0.5573 0.2213  0.0543  -0.0018 111 GLY D O   
21082 N N   . THR D 112 ? 1.2711 0.7934 0.9022 0.2866  0.0673  0.0095  112 THR D N   
21083 C CA  . THR D 112 ? 1.2551 0.8054 0.9370 0.2513  0.0380  -0.0038 112 THR D CA  
21084 C C   . THR D 112 ? 1.2234 0.8290 0.8807 0.2587  0.0040  0.0062  112 THR D C   
21085 O O   . THR D 112 ? 1.2157 0.8677 0.8575 0.2538  -0.0238 0.0017  112 THR D O   
21086 C CB  . THR D 112 ? 1.2591 0.8315 0.9850 0.2169  0.0082  -0.0296 112 THR D CB  
21087 O OG1 . THR D 112 ? 1.2993 0.8325 1.0694 0.2047  0.0417  -0.0531 112 THR D OG1 
21088 C CG2 . THR D 112 ? 1.0970 0.6985 0.8519 0.1950  -0.0321 -0.0397 112 THR D CG2 
21096 N N   . SER D 113 ? 1.2435 0.8436 0.9003 0.2669  0.0117  0.0144  113 SER D N   
21097 C CA  . SER D 113 ? 1.2376 0.8938 0.8818 0.2699  -0.0161 0.0157  113 SER D CA  
21098 C C   . SER D 113 ? 1.1898 0.8705 0.8692 0.2294  -0.0514 0.0029  113 SER D C   
21099 O O   . SER D 113 ? 1.2047 0.8601 0.9235 0.2085  -0.0572 -0.0054 113 SER D O   
21100 C CB  . SER D 113 ? 1.3103 0.9522 0.9430 0.2903  0.0027  0.0259  113 SER D CB  
21101 O OG  . SER D 113 ? 1.3516 0.9625 1.0342 0.2616  0.0098  0.0195  113 SER D OG  
21107 N N   . VAL D 114 ? 1.2017 0.9287 0.8636 0.2215  -0.0718 -0.0032 114 VAL D N   
21108 C CA  . VAL D 114 ? 1.2235 0.9540 0.8932 0.1886  -0.0960 -0.0108 114 VAL D CA  
21109 C C   . VAL D 114 ? 1.2531 1.0224 0.9214 0.1847  -0.0971 -0.0169 114 VAL D C   
21110 O O   . VAL D 114 ? 1.2660 1.0868 0.9207 0.1977  -0.0903 -0.0291 114 VAL D O   
21111 C CB  . VAL D 114 ? 1.2529 0.9854 0.8971 0.1730  -0.1049 -0.0182 114 VAL D CB  
21112 C CG1 . VAL D 114 ? 1.2824 1.0012 0.9072 0.1449  -0.1186 -0.0225 114 VAL D CG1 
21113 C CG2 . VAL D 114 ? 1.2899 0.9882 0.9430 0.1739  -0.1075 -0.0186 114 VAL D CG2 
21123 N N   . THR D 115 ? 1.2788 1.0298 0.9665 0.1693  -0.1060 -0.0154 115 THR D N   
21124 C CA  . THR D 115 ? 1.2761 1.0593 0.9699 0.1610  -0.1035 -0.0248 115 THR D CA  
21125 C C   . THR D 115 ? 1.3079 1.0589 0.9900 0.1298  -0.1125 -0.0283 115 THR D C   
21126 O O   . THR D 115 ? 1.3214 1.0209 1.0031 0.1266  -0.1292 -0.0189 115 THR D O   
21127 C CB  . THR D 115 ? 1.2512 1.0322 0.9718 0.1745  -0.0982 -0.0191 115 THR D CB  
21128 O OG1 . THR D 115 ? 1.2612 1.0319 0.9746 0.2050  -0.0817 -0.0087 115 THR D OG1 
21129 C CG2 . THR D 115 ? 1.2464 1.0806 0.9722 0.1749  -0.0925 -0.0347 115 THR D CG2 
21137 N N   . VAL D 116 ? 1.3553 1.1337 1.0251 0.1101  -0.0984 -0.0465 116 VAL D N   
21138 C CA  . VAL D 116 ? 1.4343 1.1612 1.0727 0.0797  -0.0915 -0.0490 116 VAL D CA  
21139 C C   . VAL D 116 ? 1.4338 1.1796 1.0949 0.0636  -0.0757 -0.0653 116 VAL D C   
21140 O O   . VAL D 116 ? 1.3952 1.2028 1.0736 0.0495  -0.0529 -0.0975 116 VAL D O   
21141 C CB  . VAL D 116 ? 1.5437 1.2702 1.1459 0.0590  -0.0722 -0.0638 116 VAL D CB  
21142 C CG1 . VAL D 116 ? 1.6336 1.2785 1.1823 0.0290  -0.0529 -0.0622 116 VAL D CG1 
21143 C CG2 . VAL D 116 ? 1.5825 1.2975 1.1670 0.0758  -0.0878 -0.0505 116 VAL D CG2 
21153 N N   . SER D 117 ? 1.4627 1.1626 1.1305 0.0663  -0.0878 -0.0507 117 SER D N   
21154 C CA  . SER D 117 ? 1.5020 1.2088 1.1912 0.0498  -0.0719 -0.0650 117 SER D CA  
21155 C C   . SER D 117 ? 1.5773 1.1887 1.2338 0.0466  -0.0799 -0.0468 117 SER D C   
21156 O O   . SER D 117 ? 1.6097 1.1693 1.2411 0.0674  -0.1083 -0.0264 117 SER D O   
21157 C CB  . SER D 117 ? 1.4559 1.2264 1.1987 0.0693  -0.0795 -0.0703 117 SER D CB  
21158 O OG  . SER D 117 ? 1.4709 1.2495 1.2377 0.0524  -0.0652 -0.0868 117 SER D OG  
21164 N N   . SER D 118 ? 1.5955 1.1858 1.2520 0.0243  -0.0546 -0.0597 118 SER D N   
21165 C CA  . SER D 118 ? 1.6192 1.1128 1.2386 0.0294  -0.0603 -0.0428 118 SER D CA  
21166 C C   . SER D 118 ? 1.5742 1.0886 1.2498 0.0492  -0.0866 -0.0400 118 SER D C   
21167 O O   . SER D 118 ? 1.6461 1.0924 1.2998 0.0703  -0.1097 -0.0261 118 SER D O   
21168 C CB  . SER D 118 ? 1.6461 1.0867 1.2317 -0.0067 -0.0092 -0.0587 118 SER D CB  
21169 O OG  . SER D 118 ? 1.7002 1.1071 1.2296 -0.0298 0.0241  -0.0652 118 SER D OG  
21175 N N   . ALA D 119 ? 1.4625 1.0680 1.2046 0.0475  -0.0836 -0.0559 119 ALA D N   
21176 C CA  . ALA D 119 ? 1.4377 1.0626 1.2330 0.0619  -0.1003 -0.0563 119 ALA D CA  
21177 C C   . ALA D 119 ? 1.4300 1.0194 1.2300 0.0903  -0.1374 -0.0416 119 ALA D C   
21178 O O   . ALA D 119 ? 1.4622 1.0429 1.2395 0.1020  -0.1517 -0.0330 119 ALA D O   
21179 C CB  . ALA D 119 ? 1.4123 1.1306 1.2550 0.0662  -0.0917 -0.0702 119 ALA D CB  
21185 N N   . LYS D 120 ? 1.3940 0.9702 1.2312 0.1008  -0.1523 -0.0467 120 LYS D N   
21186 C CA  . LYS D 120 ? 1.3806 0.9475 1.2494 0.1265  -0.1860 -0.0509 120 LYS D CA  
21187 C C   . LYS D 120 ? 1.2866 0.9115 1.2296 0.1245  -0.1762 -0.0648 120 LYS D C   
21188 O O   . LYS D 120 ? 1.2623 0.9245 1.2223 0.1108  -0.1505 -0.0675 120 LYS D O   
21189 C CB  . LYS D 120 ? 1.4389 0.9434 1.2926 0.1474  -0.2127 -0.0543 120 LYS D CB  
21190 C CG  . LYS D 120 ? 1.5620 0.9802 1.3160 0.1572  -0.2161 -0.0358 120 LYS D CG  
21191 C CD  . LYS D 120 ? 1.6580 1.0103 1.3801 0.2022  -0.2581 -0.0389 120 LYS D CD  
21192 C CE  . LYS D 120 ? 1.8153 1.0565 1.4103 0.2184  -0.2530 -0.0145 120 LYS D CE  
21193 N NZ  . LYS D 120 ? 1.9423 1.1150 1.4843 0.2800  -0.3023 -0.0171 120 LYS D NZ  
21207 N N   . THR D 121 ? 1.2486 0.8794 1.2337 0.1389  -0.1929 -0.0786 121 THR D N   
21208 C CA  . THR D 121 ? 1.2137 0.8803 1.2620 0.1342  -0.1715 -0.0940 121 THR D CA  
21209 C C   . THR D 121 ? 1.2295 0.9097 1.3120 0.1251  -0.1589 -0.1027 121 THR D C   
21210 O O   . THR D 121 ? 1.2789 0.9393 1.3763 0.1300  -0.1802 -0.1130 121 THR D O   
21211 C CB  . THR D 121 ? 1.1770 0.8444 1.2820 0.1453  -0.1890 -0.1240 121 THR D CB  
21212 O OG1 . THR D 121 ? 1.1407 0.8288 1.3087 0.1342  -0.1557 -0.1444 121 THR D OG1 
21213 C CG2 . THR D 121 ? 1.2032 0.8526 1.3241 0.1658  -0.2339 -0.1448 121 THR D CG2 
21221 N N   . THR D 122 ? 1.1967 0.9068 1.2838 0.1170  -0.1242 -0.0987 122 THR D N   
21222 C CA  . THR D 122 ? 1.1624 0.8924 1.2758 0.1082  -0.1087 -0.1079 122 THR D CA  
21223 C C   . THR D 122 ? 1.1375 0.8811 1.2700 0.1094  -0.0725 -0.1134 122 THR D C   
21224 O O   . THR D 122 ? 1.1938 0.9373 1.2850 0.1198  -0.0505 -0.0983 122 THR D O   
21225 C CB  . THR D 122 ? 1.1543 0.9080 1.2268 0.0999  -0.1000 -0.0992 122 THR D CB  
21226 O OG1 . THR D 122 ? 1.1918 0.9123 1.2326 0.0948  -0.1188 -0.0929 122 THR D OG1 
21227 C CG2 . THR D 122 ? 1.1521 0.9304 1.2579 0.0900  -0.0862 -0.1151 122 THR D CG2 
21235 N N   . ALA D 123 ? 1.0988 0.8456 1.2865 0.1014  -0.0624 -0.1349 123 ALA D N   
21236 C CA  . ALA D 123 ? 1.1415 0.8839 1.3409 0.1000  -0.0183 -0.1422 123 ALA D CA  
21237 C C   . ALA D 123 ? 1.2069 0.9721 1.3480 0.1104  0.0056  -0.1257 123 ALA D C   
21238 O O   . ALA D 123 ? 1.2213 1.0218 1.3508 0.1085  -0.0119 -0.1252 123 ALA D O   
21239 C CB  . ALA D 123 ? 1.1286 0.8710 1.4107 0.0857  -0.0135 -0.1776 123 ALA D CB  
21245 N N   . PRO D 124 ? 1.2573 1.0002 1.3570 0.1247  0.0486  -0.1165 124 PRO D N   
21246 C CA  . PRO D 124 ? 1.2617 1.0291 1.2913 0.1495  0.0654  -0.1040 124 PRO D CA  
21247 C C   . PRO D 124 ? 1.2489 1.0401 1.3044 0.1413  0.0769  -0.1227 124 PRO D C   
21248 O O   . PRO D 124 ? 1.2297 1.0059 1.3544 0.1167  0.0846  -0.1435 124 PRO D O   
21249 C CB  . PRO D 124 ? 1.3412 1.0505 1.2997 0.1762  0.1119  -0.0843 124 PRO D CB  
21250 C CG  . PRO D 124 ? 1.3754 1.0307 1.3919 0.1505  0.1346  -0.0973 124 PRO D CG  
21251 C CD  . PRO D 124 ? 1.3235 1.0121 1.4201 0.1258  0.0832  -0.1153 124 PRO D CD  
21259 N N   . SER D 125 ? 1.0687 0.9753 0.9854 0.2923  -0.0345 -0.0316 125 SER D N   
21260 C CA  . SER D 125 ? 1.0556 0.9648 0.9904 0.3057  -0.0204 -0.0478 125 SER D CA  
21261 C C   . SER D 125 ? 1.0053 0.9585 0.9601 0.2795  -0.0215 -0.0636 125 SER D C   
21262 O O   . SER D 125 ? 1.0368 0.9679 0.9856 0.2521  -0.0181 -0.0739 125 SER D O   
21263 C CB  . SER D 125 ? 1.1364 0.9623 1.0477 0.3073  -0.0019 -0.0588 125 SER D CB  
21264 O OG  . SER D 125 ? 1.2015 0.9841 1.0974 0.3422  0.0038  -0.0433 125 SER D OG  
21270 N N   . VAL D 126 ? 0.9410 0.9607 0.9240 0.2891  -0.0250 -0.0604 126 VAL D N   
21271 C CA  . VAL D 126 ? 0.9008 0.9648 0.9006 0.2665  -0.0256 -0.0673 126 VAL D CA  
21272 C C   . VAL D 126 ? 0.8866 0.9459 0.8749 0.2804  -0.0079 -0.0864 126 VAL D C   
21273 O O   . VAL D 126 ? 0.8928 0.9690 0.8849 0.3140  0.0051  -0.0856 126 VAL D O   
21274 C CB  . VAL D 126 ? 0.8777 1.0178 0.9157 0.2614  -0.0392 -0.0473 126 VAL D CB  
21275 C CG1 . VAL D 126 ? 0.8334 1.0098 0.8859 0.2381  -0.0365 -0.0489 126 VAL D CG1 
21276 C CG2 . VAL D 126 ? 0.8688 0.9996 0.9014 0.2457  -0.0625 -0.0354 126 VAL D CG2 
21286 N N   . TYR D 127 ? 0.8912 0.9286 0.8631 0.2568  -0.0079 -0.1034 127 TYR D N   
21287 C CA  . TYR D 127 ? 0.9168 0.9353 0.8595 0.2638  0.0019  -0.1278 127 TYR D CA  
21288 C C   . TYR D 127 ? 0.9062 0.9777 0.8517 0.2482  -0.0012 -0.1258 127 TYR D C   
21289 O O   . TYR D 127 ? 0.8706 0.9521 0.8304 0.2194  -0.0141 -0.1184 127 TYR D O   
21290 C CB  . TYR D 127 ? 0.8965 0.8409 0.8156 0.2457  -0.0026 -0.1484 127 TYR D CB  
21291 C CG  . TYR D 127 ? 0.9253 0.8056 0.8362 0.2608  0.0042  -0.1465 127 TYR D CG  
21292 C CD1 . TYR D 127 ? 0.9424 0.8088 0.8429 0.3020  0.0178  -0.1452 127 TYR D CD1 
21293 C CD2 . TYR D 127 ? 0.9632 0.7990 0.8794 0.2371  0.0005  -0.1409 127 TYR D CD2 
21294 C CE1 . TYR D 127 ? 1.0214 0.8242 0.9125 0.3194  0.0238  -0.1380 127 TYR D CE1 
21295 C CE2 . TYR D 127 ? 1.0354 0.8087 0.9401 0.2508  0.0091  -0.1329 127 TYR D CE2 
21296 C CZ  . TYR D 127 ? 1.0755 0.8289 0.9654 0.2920  0.0189  -0.1313 127 TYR D CZ  
21297 O OH  . TYR D 127 ? 1.1648 0.8512 1.0414 0.3092  0.0273  -0.1182 127 TYR D OH  
21307 N N   . PRO D 128 ? 0.9697 1.0747 0.8999 0.2693  0.0135  -0.1292 128 PRO D N   
21308 C CA  . PRO D 128 ? 1.0201 1.1694 0.9424 0.2550  0.0120  -0.1235 128 PRO D CA  
21309 C C   . PRO D 128 ? 1.1137 1.2218 0.9936 0.2365  -0.0022 -0.1491 128 PRO D C   
21310 O O   . PRO D 128 ? 1.2168 1.2638 1.0599 0.2419  -0.0033 -0.1786 128 PRO D O   
21311 C CB  . PRO D 128 ? 1.0515 1.2431 0.9610 0.2892  0.0389  -0.1194 128 PRO D CB  
21312 C CG  . PRO D 128 ? 1.0848 1.2213 0.9667 0.3227  0.0528  -0.1431 128 PRO D CG  
21313 C CD  . PRO D 128 ? 1.0326 1.1293 0.9435 0.3118  0.0366  -0.1386 128 PRO D CD  
21321 N N   . LEU D 129 ? 1.0715 1.2119 0.9595 0.2129  -0.0161 -0.1359 129 LEU D N   
21322 C CA  . LEU D 129 ? 1.0908 1.2121 0.9480 0.1932  -0.0370 -0.1535 129 LEU D CA  
21323 C C   . LEU D 129 ? 1.1096 1.2750 0.9300 0.1987  -0.0354 -0.1449 129 LEU D C   
21324 O O   . LEU D 129 ? 1.0750 1.2864 0.9236 0.1892  -0.0379 -0.1131 129 LEU D O   
21325 C CB  . LEU D 129 ? 1.1079 1.2295 1.0116 0.1641  -0.0564 -0.1400 129 LEU D CB  
21326 C CG  . LEU D 129 ? 1.1518 1.2312 1.0859 0.1581  -0.0537 -0.1430 129 LEU D CG  
21327 C CD1 . LEU D 129 ? 1.1537 1.2424 1.1317 0.1349  -0.0650 -0.1270 129 LEU D CD1 
21328 C CD2 . LEU D 129 ? 1.2362 1.2537 1.1387 0.1593  -0.0549 -0.1742 129 LEU D CD2 
21340 N N   . ALA D 130 ? 1.2198 1.3632 0.9699 0.2160  -0.0290 -0.1728 130 ALA D N   
21341 C CA  . ALA D 130 ? 1.2408 1.4163 0.9332 0.2229  -0.0279 -0.1687 130 ALA D CA  
21342 C C   . ALA D 130 ? 1.2771 1.4244 0.9203 0.1996  -0.0661 -0.1944 130 ALA D C   
21343 O O   . ALA D 130 ? 1.2635 1.3547 0.9030 0.1838  -0.0854 -0.2261 130 ALA D O   
21344 C CB  . ALA D 130 ? 1.2977 1.4692 0.9303 0.2631  0.0084  -0.1832 130 ALA D CB  
21350 N N   . PRO D 131 ? 1.3098 1.4966 0.9171 0.1947  -0.0803 -0.1783 131 PRO D N   
21351 C CA  . PRO D 131 ? 1.3874 1.5593 0.9514 0.1701  -0.1258 -0.1995 131 PRO D CA  
21352 C C   . PRO D 131 ? 1.5399 1.6432 1.0046 0.1761  -0.1334 -0.2557 131 PRO D C   
21353 O O   . PRO D 131 ? 1.6475 1.7108 1.0762 0.2062  -0.0975 -0.2777 131 PRO D O   
21354 C CB  . PRO D 131 ? 1.4020 1.6353 0.9400 0.1735  -0.1333 -0.1622 131 PRO D CB  
21355 C CG  . PRO D 131 ? 1.3701 1.6340 0.9058 0.2038  -0.0836 -0.1342 131 PRO D CG  
21356 C CD  . PRO D 131 ? 1.2702 1.5205 0.8835 0.2076  -0.0591 -0.1336 131 PRO D CD  
21364 N N   . VAL D 132 ? 1.5961 1.6836 1.0167 0.1479  -0.1822 -0.2792 132 VAL D N   
21365 C CA  . VAL D 132 ? 1.7825 1.7915 1.0963 0.1455  -0.1997 -0.3389 132 VAL D CA  
21366 C C   . VAL D 132 ? 1.9104 1.9317 1.1004 0.1710  -0.1948 -0.3455 132 VAL D C   
21367 O O   . VAL D 132 ? 1.8713 1.9653 1.0629 0.1723  -0.2027 -0.3033 132 VAL D O   
21368 C CB  . VAL D 132 ? 1.8279 1.8125 1.1626 0.0933  -0.2620 -0.3628 132 VAL D CB  
21369 C CG1 . VAL D 132 ? 1.9999 1.8761 1.2359 0.0849  -0.2775 -0.4310 132 VAL D CG1 
21370 C CG2 . VAL D 132 ? 1.6943 1.6969 1.1653 0.0687  -0.2625 -0.3364 132 VAL D CG2 
21380 N N   . CYS D 133 ? 2.1055 2.0485 1.1805 0.1944  -0.1788 -0.3977 133 CYS D N   
21381 C CA  . CYS D 133 ? 2.3400 2.2823 1.2760 0.2255  -0.1652 -0.4099 133 CYS D CA  
21382 C C   . CYS D 133 ? 2.5147 2.4728 1.3810 0.1917  -0.2324 -0.4175 133 CYS D C   
21383 O O   . CYS D 133 ? 2.5772 2.5993 1.3999 0.2047  -0.2322 -0.3809 133 CYS D O   
21384 C CB  . CYS D 133 ? 2.5327 2.3708 1.3551 0.2610  -0.1323 -0.4719 133 CYS D CB  
21385 S SG  . CYS D 133 ? 2.6275 2.3514 1.4942 0.2357  -0.1494 -0.5240 133 CYS D SG  
21390 N N   . GLY D 138 ? 1.9162 2.5137 1.1175 0.2221  -0.3047 0.2101  138 GLY D N   
21391 C CA  . GLY D 138 ? 1.8578 2.4198 1.0958 0.2231  -0.2439 0.1825  138 GLY D CA  
21392 C C   . GLY D 138 ? 1.8095 2.3812 1.1014 0.2350  -0.1869 0.2434  138 GLY D C   
21393 O O   . GLY D 138 ? 1.8500 2.4205 1.0911 0.2493  -0.1351 0.2503  138 GLY D O   
21396 N N   . SER D 139 ? 1.7491 2.3289 1.1474 0.2286  -0.1951 0.2881  139 SER D N   
21397 C CA  . SER D 139 ? 1.7430 2.3203 1.1970 0.2330  -0.1497 0.3480  139 SER D CA  
21398 C C   . SER D 139 ? 1.6615 2.2095 1.2178 0.2181  -0.1162 0.3279  139 SER D C   
21399 O O   . SER D 139 ? 1.6926 2.2379 1.2688 0.2163  -0.0696 0.3536  139 SER D O   
21400 C CB  . SER D 139 ? 1.7622 2.3504 1.2619 0.2391  -0.1764 0.4110  139 SER D CB  
21401 O OG  . SER D 139 ? 1.7091 2.2876 1.3085 0.2300  -0.2052 0.3933  139 SER D OG  
21407 N N   . SER D 140 ? 1.5273 2.0565 1.1491 0.2056  -0.1399 0.2856  140 SER D N   
21408 C CA  . SER D 140 ? 1.4209 1.9197 1.1254 0.1927  -0.1142 0.2623  140 SER D CA  
21409 C C   . SER D 140 ? 1.4416 1.9263 1.1332 0.1865  -0.1231 0.1937  140 SER D C   
21410 O O   . SER D 140 ? 1.4952 1.9855 1.1394 0.1854  -0.1587 0.1628  140 SER D O   
21411 C CB  . SER D 140 ? 1.3271 1.8041 1.1271 0.1868  -0.1256 0.2834  140 SER D CB  
21412 O OG  . SER D 140 ? 1.2914 1.7779 1.1126 0.1862  -0.1665 0.2608  140 SER D OG  
21418 N N   . VAL D 141 ? 1.3495 1.8130 1.0847 0.1805  -0.0933 0.1718  141 VAL D N   
21419 C CA  . VAL D 141 ? 1.2843 1.7259 1.0100 0.1782  -0.0940 0.1129  141 VAL D CA  
21420 C C   . VAL D 141 ? 1.1930 1.6064 1.0072 0.1655  -0.0898 0.1011  141 VAL D C   
21421 O O   . VAL D 141 ? 1.1605 1.5694 1.0266 0.1607  -0.0696 0.1290  141 VAL D O   
21422 C CB  . VAL D 141 ? 1.2821 1.7300 0.9522 0.1939  -0.0564 0.0976  141 VAL D CB  
21423 C CG1 . VAL D 141 ? 1.2019 1.6681 0.9291 0.1925  -0.0167 0.1349  141 VAL D CG1 
21424 C CG2 . VAL D 141 ? 1.2341 1.6479 0.8906 0.1965  -0.0576 0.0381  141 VAL D CG2 
21434 N N   . THR D 142 ? 1.1567 1.5473 0.9829 0.1581  -0.1095 0.0599  142 THR D N   
21435 C CA  . THR D 142 ? 1.0452 1.4060 0.9393 0.1489  -0.1040 0.0458  142 THR D CA  
21436 C C   . THR D 142 ? 1.0085 1.3451 0.8838 0.1527  -0.0885 0.0055  142 THR D C   
21437 O O   . THR D 142 ? 1.0429 1.3646 0.8724 0.1536  -0.1010 -0.0296 142 THR D O   
21438 C CB  . THR D 142 ? 1.0302 1.3870 0.9647 0.1387  -0.1330 0.0399  142 THR D CB  
21439 O OG1 . THR D 142 ? 1.0556 1.4371 1.0146 0.1428  -0.1452 0.0824  142 THR D OG1 
21440 C CG2 . THR D 142 ? 0.9534 1.2767 0.9455 0.1326  -0.1208 0.0261  142 THR D CG2 
21448 N N   . LEU D 143 ? 0.9857 1.3157 0.8952 0.1548  -0.0639 0.0114  143 LEU D N   
21449 C CA  . LEU D 143 ? 0.9816 1.2893 0.8903 0.1620  -0.0503 -0.0190 143 LEU D CA  
21450 C C   . LEU D 143 ? 0.9513 1.2263 0.9114 0.1509  -0.0561 -0.0261 143 LEU D C   
21451 O O   . LEU D 143 ? 0.9100 1.1811 0.9068 0.1406  -0.0628 -0.0062 143 LEU D O   
21452 C CB  . LEU D 143 ? 0.9581 1.2950 0.8713 0.1746  -0.0208 -0.0034 143 LEU D CB  
21453 C CG  . LEU D 143 ? 1.0254 1.3999 0.8861 0.1906  -0.0025 0.0100  143 LEU D CG  
21454 C CD1 . LEU D 143 ? 1.0118 1.4270 0.9025 0.2015  0.0308  0.0313  143 LEU D CD1 
21455 C CD2 . LEU D 143 ? 1.1060 1.4569 0.8879 0.2070  -0.0067 -0.0300 143 LEU D CD2 
21467 N N   . GLY D 144 ? 0.9794 1.2256 0.9357 0.1569  -0.0504 -0.0533 144 GLY D N   
21468 C CA  . GLY D 144 ? 0.9740 1.1859 0.9643 0.1489  -0.0536 -0.0598 144 GLY D CA  
21469 C C   . GLY D 144 ? 0.9584 1.1549 0.9520 0.1608  -0.0405 -0.0689 144 GLY D C   
21470 O O   . GLY D 144 ? 0.9991 1.2117 0.9743 0.1783  -0.0278 -0.0737 144 GLY D O   
21474 N N   . CYS D 145 ? 0.9131 1.0800 0.9288 0.1548  -0.0423 -0.0688 145 CYS D N   
21475 C CA  . CYS D 145 ? 0.9137 1.0635 0.9309 0.1662  -0.0360 -0.0737 145 CYS D CA  
21476 C C   . CYS D 145 ? 0.8753 0.9767 0.8929 0.1606  -0.0377 -0.0817 145 CYS D C   
21477 O O   . CYS D 145 ? 0.8370 0.9290 0.8685 0.1483  -0.0397 -0.0736 145 CYS D O   
21478 C CB  . CYS D 145 ? 0.9527 1.1305 0.9941 0.1629  -0.0373 -0.0530 145 CYS D CB  
21479 S SG  . CYS D 145 ? 1.0316 1.2174 1.0811 0.1813  -0.0362 -0.0519 145 CYS D SG  
21484 N N   . LEU D 146 ? 0.8660 0.9347 0.8679 0.1726  -0.0325 -0.0948 146 LEU D N   
21485 C CA  . LEU D 146 ? 0.8633 0.8840 0.8631 0.1677  -0.0290 -0.0976 146 LEU D CA  
21486 C C   . LEU D 146 ? 0.9034 0.9063 0.8926 0.1838  -0.0261 -0.0895 146 LEU D C   
21487 O O   . LEU D 146 ? 0.9363 0.9416 0.9177 0.2046  -0.0239 -0.0921 146 LEU D O   
21488 C CB  . LEU D 146 ? 0.8822 0.8677 0.8703 0.1633  -0.0282 -0.1165 146 LEU D CB  
21489 C CG  . LEU D 146 ? 0.8916 0.8258 0.8833 0.1546  -0.0207 -0.1151 146 LEU D CG  
21490 C CD1 . LEU D 146 ? 0.8643 0.8120 0.8866 0.1356  -0.0178 -0.1007 146 LEU D CD1 
21491 C CD2 . LEU D 146 ? 0.9291 0.8207 0.9084 0.1463  -0.0239 -0.1365 146 LEU D CD2 
21503 N N   . VAL D 147 ? 0.8453 0.8309 0.8307 0.1776  -0.0259 -0.0789 147 VAL D N   
21504 C CA  . VAL D 147 ? 0.8720 0.8387 0.8365 0.1907  -0.0291 -0.0696 147 VAL D CA  
21505 C C   . VAL D 147 ? 0.9365 0.8485 0.8806 0.1911  -0.0147 -0.0663 147 VAL D C   
21506 O O   . VAL D 147 ? 0.9489 0.8463 0.8913 0.1792  -0.0044 -0.0627 147 VAL D O   
21507 C CB  . VAL D 147 ? 0.8630 0.8453 0.8224 0.1820  -0.0425 -0.0618 147 VAL D CB  
21508 C CG1 . VAL D 147 ? 0.9198 0.8932 0.8541 0.1945  -0.0562 -0.0526 147 VAL D CG1 
21509 C CG2 . VAL D 147 ? 0.8060 0.8413 0.7961 0.1727  -0.0524 -0.0597 147 VAL D CG2 
21519 N N   . LYS D 148 ? 0.9928 0.8732 0.9232 0.2073  -0.0099 -0.0641 148 LYS D N   
21520 C CA  . LYS D 148 ? 1.0986 0.9234 1.0161 0.2041  0.0074  -0.0574 148 LYS D CA  
21521 C C   . LYS D 148 ? 1.1666 0.9564 1.0472 0.2267  0.0085  -0.0389 148 LYS D C   
21522 O O   . LYS D 148 ? 1.1405 0.9464 1.0157 0.2495  -0.0053 -0.0348 148 LYS D O   
21523 C CB  . LYS D 148 ? 1.1398 0.9394 1.0733 0.1969  0.0127  -0.0722 148 LYS D CB  
21524 C CG  . LYS D 148 ? 1.2001 0.9541 1.1426 0.1766  0.0292  -0.0652 148 LYS D CG  
21525 C CD  . LYS D 148 ? 1.2060 0.9393 1.1667 0.1582  0.0240  -0.0867 148 LYS D CD  
21526 C CE  . LYS D 148 ? 1.2473 0.9331 1.2271 0.1320  0.0377  -0.0766 148 LYS D CE  
21527 N NZ  . LYS D 148 ? 1.2557 0.8765 1.2058 0.1495  0.0550  -0.0554 148 LYS D NZ  
21541 N N   . GLY D 149 ? 1.2225 0.9698 1.0797 0.2221  0.0265  -0.0234 149 GLY D N   
21542 C CA  . GLY D 149 ? 1.3455 1.0491 1.1592 0.2434  0.0310  -0.0002 149 GLY D CA  
21543 C C   . GLY D 149 ? 1.3531 1.0790 1.1285 0.2617  0.0073  0.0092  149 GLY D C   
21544 O O   . GLY D 149 ? 1.4181 1.1368 1.1773 0.2875  -0.0053 0.0244  149 GLY D O   
21548 N N   . TYR D 150 ? 1.2976 1.0479 1.0585 0.2488  -0.0014 0.0010  150 TYR D N   
21549 C CA  . TYR D 150 ? 1.2968 1.0629 1.0164 0.2567  -0.0309 0.0054  150 TYR D CA  
21550 C C   . TYR D 150 ? 1.3279 1.0500 0.9757 0.2548  -0.0185 0.0108  150 TYR D C   
21551 O O   . TYR D 150 ? 1.3161 1.0169 0.9646 0.2442  0.0135  0.0068  150 TYR D O   
21552 C CB  . TYR D 150 ? 1.2276 1.0509 0.9835 0.2410  -0.0565 -0.0125 150 TYR D CB  
21553 C CG  . TYR D 150 ? 1.2058 1.0231 0.9619 0.2187  -0.0448 -0.0287 150 TYR D CG  
21554 C CD1 . TYR D 150 ? 1.1293 0.9640 0.9376 0.2066  -0.0271 -0.0384 150 TYR D CD1 
21555 C CD2 . TYR D 150 ? 1.2614 1.0513 0.9604 0.2125  -0.0527 -0.0346 150 TYR D CD2 
21556 C CE1 . TYR D 150 ? 1.1000 0.9319 0.9141 0.1924  -0.0164 -0.0477 150 TYR D CE1 
21557 C CE2 . TYR D 150 ? 1.2515 1.0271 0.9501 0.1993  -0.0378 -0.0486 150 TYR D CE2 
21558 C CZ  . TYR D 150 ? 1.1731 0.9734 0.9347 0.1910  -0.0191 -0.0522 150 TYR D CZ  
21559 O OH  . TYR D 150 ? 1.1730 0.9620 0.9397 0.1837  -0.0043 -0.0608 150 TYR D OH  
21569 N N   . PHE D 151 ? 1.3837 1.0955 0.9677 0.2673  -0.0444 0.0211  151 PHE D N   
21570 C CA  . PHE D 151 ? 1.4179 1.0795 0.9106 0.2706  -0.0332 0.0246  151 PHE D CA  
21571 C C   . PHE D 151 ? 1.4632 1.1315 0.8931 0.2751  -0.0825 0.0244  151 PHE D C   
21572 O O   . PHE D 151 ? 1.4653 1.1667 0.9146 0.2885  -0.1140 0.0415  151 PHE D O   
21573 C CB  . PHE D 151 ? 1.4752 1.0864 0.9321 0.2876  0.0057  0.0538  151 PHE D CB  
21574 C CG  . PHE D 151 ? 1.5922 1.1512 0.9462 0.2963  0.0273  0.0615  151 PHE D CG  
21575 C CD1 . PHE D 151 ? 1.7065 1.2429 0.9632 0.3126  -0.0025 0.0723  151 PHE D CD1 
21576 C CD2 . PHE D 151 ? 1.6020 1.1376 0.9546 0.2909  0.0784  0.0598  151 PHE D CD2 
21577 C CE1 . PHE D 151 ? 1.8355 1.3170 0.9797 0.3237  0.0198  0.0772  151 PHE D CE1 
21578 C CE2 . PHE D 151 ? 1.7191 1.2055 0.9707 0.3051  0.1069  0.0674  151 PHE D CE2 
21579 C CZ  . PHE D 151 ? 1.8382 1.2923 0.9775 0.3218  0.0786  0.0742  151 PHE D CZ  
21589 N N   . PRO D 152 ? 1.5096 1.1466 0.8645 0.2649  -0.0926 0.0053  152 PRO D N   
21590 C CA  . PRO D 152 ? 1.5121 1.1094 0.8429 0.2561  -0.0548 -0.0153 152 PRO D CA  
21591 C C   . PRO D 152 ? 1.4411 1.0701 0.8390 0.2314  -0.0676 -0.0419 152 PRO D C   
21592 O O   . PRO D 152 ? 1.3338 1.0176 0.7935 0.2183  -0.1047 -0.0437 152 PRO D O   
21593 C CB  . PRO D 152 ? 1.6197 1.1570 0.8178 0.2633  -0.0667 -0.0243 152 PRO D CB  
21594 C CG  . PRO D 152 ? 1.6373 1.2074 0.8228 0.2540  -0.1364 -0.0257 152 PRO D CG  
21595 C CD  . PRO D 152 ? 1.5824 1.2151 0.8596 0.2646  -0.1457 0.0034  152 PRO D CD  
21603 N N   . GLU D 153 ? 1.4899 1.0864 0.8781 0.2281  -0.0337 -0.0579 153 GLU D N   
21604 C CA  . GLU D 153 ? 1.5132 1.1153 0.9292 0.2070  -0.0515 -0.0828 153 GLU D CA  
21605 C C   . GLU D 153 ? 1.5364 1.1184 0.8857 0.1915  -0.1064 -0.0998 153 GLU D C   
21606 O O   . GLU D 153 ? 1.6183 1.1615 0.8709 0.2025  -0.1199 -0.0985 153 GLU D O   
21607 C CB  . GLU D 153 ? 1.6042 1.1598 1.0005 0.2152  -0.0054 -0.0951 153 GLU D CB  
21608 C CG  . GLU D 153 ? 1.5299 1.1207 1.0119 0.2227  0.0403  -0.0778 153 GLU D CG  
21609 C CD  . GLU D 153 ? 1.4241 1.0630 1.0011 0.2056  0.0302  -0.0829 153 GLU D CD  
21610 O OE1 . GLU D 153 ? 1.3880 1.0148 0.9845 0.2102  0.0560  -0.0878 153 GLU D OE1 
21611 O OE2 . GLU D 153 ? 1.3158 1.0052 0.9457 0.1914  -0.0013 -0.0792 153 GLU D OE2 
21618 N N   . PRO D 154 ? 1.4768 1.0848 0.8744 0.1632  -0.1413 -0.1137 154 PRO D N   
21619 C CA  . PRO D 154 ? 1.3633 1.0144 0.8623 0.1500  -0.1291 -0.1127 154 PRO D CA  
21620 C C   . PRO D 154 ? 1.3218 1.0624 0.9162 0.1420  -0.1510 -0.0938 154 PRO D C   
21621 O O   . PRO D 154 ? 1.3765 1.1522 0.9704 0.1436  -0.1838 -0.0821 154 PRO D O   
21622 C CB  . PRO D 154 ? 1.3944 1.0025 0.8674 0.1235  -0.1537 -0.1374 154 PRO D CB  
21623 C CG  . PRO D 154 ? 1.4811 1.0765 0.8883 0.1077  -0.2087 -0.1459 154 PRO D CG  
21624 C CD  . PRO D 154 ? 1.5087 1.0926 0.8486 0.1385  -0.1973 -0.1329 154 PRO D CD  
21632 N N   . VAL D 155 ? 1.2704 1.0483 0.9436 0.1375  -0.1307 -0.0894 155 VAL D N   
21633 C CA  . VAL D 155 ? 1.2113 1.0682 0.9695 0.1277  -0.1473 -0.0764 155 VAL D CA  
21634 C C   . VAL D 155 ? 1.1518 1.0143 0.9470 0.1020  -0.1528 -0.0821 155 VAL D C   
21635 O O   . VAL D 155 ? 1.1680 0.9771 0.9390 0.1009  -0.1326 -0.0933 155 VAL D O   
21636 C CB  . VAL D 155 ? 1.2047 1.0967 1.0115 0.1480  -0.1172 -0.0645 155 VAL D CB  
21637 C CG1 . VAL D 155 ? 1.2328 1.1084 1.0592 0.1479  -0.0834 -0.0695 155 VAL D CG1 
21638 C CG2 . VAL D 155 ? 1.1485 1.1168 1.0239 0.1470  -0.1316 -0.0522 155 VAL D CG2 
21648 N N   . THR D 156 ? 1.0745 1.0018 0.9310 0.0837  -0.1772 -0.0703 156 THR D N   
21649 C CA  . THR D 156 ? 1.0743 1.0129 0.9741 0.0574  -0.1807 -0.0671 156 THR D CA  
21650 C C   . THR D 156 ? 0.9750 0.9929 0.9503 0.0640  -0.1646 -0.0471 156 THR D C   
21651 O O   . THR D 156 ? 0.9645 1.0442 0.9725 0.0760  -0.1703 -0.0351 156 THR D O   
21652 C CB  . THR D 156 ? 1.1558 1.0962 1.0581 0.0204  -0.2258 -0.0685 156 THR D CB  
21653 O OG1 . THR D 156 ? 1.1472 1.1773 1.1056 0.0176  -0.2504 -0.0486 156 THR D OG1 
21654 C CG2 . THR D 156 ? 1.2786 1.1332 1.0851 0.0156  -0.2466 -0.0937 156 THR D CG2 
21662 N N   . LEU D 157 ? 0.9114 0.9246 0.9085 0.0603  -0.1433 -0.0429 157 LEU D N   
21663 C CA  . LEU D 157 ? 0.8334 0.9106 0.8814 0.0693  -0.1251 -0.0268 157 LEU D CA  
21664 C C   . LEU D 157 ? 0.8203 0.9128 0.9042 0.0450  -0.1260 -0.0099 157 LEU D C   
21665 O O   . LEU D 157 ? 0.8548 0.8883 0.9194 0.0323  -0.1260 -0.0138 157 LEU D O   
21666 C CB  . LEU D 157 ? 0.8170 0.8773 0.8499 0.0937  -0.0970 -0.0343 157 LEU D CB  
21667 C CG  . LEU D 157 ? 0.7829 0.8972 0.8475 0.1041  -0.0816 -0.0246 157 LEU D CG  
21668 C CD1 . LEU D 157 ? 0.8166 0.9185 0.8634 0.1259  -0.0669 -0.0377 157 LEU D CD1 
21669 C CD2 . LEU D 157 ? 0.7420 0.8579 0.8213 0.0939  -0.0742 -0.0121 157 LEU D CD2 
21681 N N   . THR D 158 ? 0.8102 0.9789 0.9446 0.0419  -0.1226 0.0115  158 THR D N   
21682 C CA  . THR D 158 ? 0.8280 1.0203 0.9995 0.0201  -0.1176 0.0361  158 THR D CA  
21683 C C   . THR D 158 ? 0.8199 1.0862 1.0184 0.0396  -0.0931 0.0539  158 THR D C   
21684 O O   . THR D 158 ? 0.8019 1.1026 0.9979 0.0660  -0.0848 0.0458  158 THR D O   
21685 C CB  . THR D 158 ? 0.8413 1.0510 1.0512 -0.0192 -0.1451 0.0504  158 THR D CB  
21686 O OG1 . THR D 158 ? 0.8164 1.1050 1.0661 -0.0141 -0.1557 0.0591  158 THR D OG1 
21687 C CG2 . THR D 158 ? 0.8969 1.0167 1.0605 -0.0396 -0.1719 0.0263  158 THR D CG2 
21695 N N   . TRP D 159 ? 0.8579 1.1404 1.0741 0.0287  -0.0801 0.0786  159 TRP D N   
21696 C CA  . TRP D 159 ? 0.8737 1.2213 1.1008 0.0467  -0.0545 0.0974  159 TRP D CA  
21697 C C   . TRP D 159 ? 0.8535 1.2640 1.1381 0.0223  -0.0490 0.1358  159 TRP D C   
21698 O O   . TRP D 159 ? 0.8621 1.2461 1.1663 -0.0109 -0.0579 0.1557  159 TRP D O   
21699 C CB  . TRP D 159 ? 0.9318 1.2516 1.1225 0.0587  -0.0417 0.0996  159 TRP D CB  
21700 C CG  . TRP D 159 ? 0.9344 1.2142 1.0840 0.0813  -0.0442 0.0671  159 TRP D CG  
21701 C CD1 . TRP D 159 ? 0.9275 1.1438 1.0599 0.0794  -0.0540 0.0511  159 TRP D CD1 
21702 C CD2 . TRP D 159 ? 0.9218 1.2206 1.0447 0.1077  -0.0345 0.0480  159 TRP D CD2 
21703 N NE1 . TRP D 159 ? 0.8809 1.0862 0.9885 0.0995  -0.0509 0.0282  159 TRP D NE1 
21704 C CE2 . TRP D 159 ? 0.8949 1.1441 0.9943 0.1143  -0.0421 0.0239  159 TRP D CE2 
21705 C CE3 . TRP D 159 ? 0.9424 1.2903 1.0568 0.1273  -0.0179 0.0484  159 TRP D CE3 
21706 C CZ2 . TRP D 159 ? 0.8952 1.1399 0.9679 0.1320  -0.0389 0.0008  159 TRP D CZ2 
21707 C CZ3 . TRP D 159 ? 0.9908 1.3230 1.0662 0.1497  -0.0141 0.0201  159 TRP D CZ3 
21708 C CH2 . TRP D 159 ? 0.9700 1.2499 1.0273 0.1482  -0.0272 -0.0032 159 TRP D CH2 
21719 N N   . ASN D 160 ? 0.8123 1.3040 1.1266 0.0398  -0.0314 0.1481  160 ASN D N   
21720 C CA  . ASN D 160 ? 0.7888 1.3610 1.1746 0.0185  -0.0221 0.1893  160 ASN D CA  
21721 C C   . ASN D 160 ? 0.8156 1.3696 1.2488 -0.0312 -0.0585 0.1975  160 ASN D C   
21722 O O   . ASN D 160 ? 0.8416 1.4072 1.3185 -0.0699 -0.0596 0.2309  160 ASN D O   
21723 C CB  . ASN D 160 ? 0.8017 1.3979 1.1830 0.0171  0.0093  0.2245  160 ASN D CB  
21724 C CG  . ASN D 160 ? 0.8241 1.4615 1.1634 0.0643  0.0457  0.2204  160 ASN D CG  
21725 O OD1 . ASN D 160 ? 0.8416 1.5189 1.1870 0.0946  0.0563  0.2056  160 ASN D OD1 
21726 N ND2 . ASN D 160 ? 0.8631 1.4854 1.1532 0.0727  0.0637  0.2330  160 ASN D ND2 
21733 N N   . SER D 161 ? 0.8684 1.3857 1.2854 -0.0314 -0.0902 0.1658  161 SER D N   
21734 C CA  . SER D 161 ? 0.8918 1.3920 1.3402 -0.0760 -0.1327 0.1649  161 SER D CA  
21735 C C   . SER D 161 ? 0.9476 1.3468 1.3640 -0.1121 -0.1479 0.1584  161 SER D C   
21736 O O   . SER D 161 ? 1.0122 1.3968 1.4630 -0.1611 -0.1776 0.1680  161 SER D O   
21737 C CB  . SER D 161 ? 0.8746 1.4845 1.4238 -0.1036 -0.1377 0.2061  161 SER D CB  
21738 O OG  . SER D 161 ? 0.8199 1.5258 1.4009 -0.0599 -0.1103 0.2180  161 SER D OG  
21744 N N   . GLY D 162 ? 0.9338 1.2610 1.2869 -0.0884 -0.1294 0.1421  162 GLY D N   
21745 C CA  . GLY D 162 ? 0.9840 1.2121 1.3060 -0.1105 -0.1365 0.1380  162 GLY D CA  
21746 C C   . GLY D 162 ? 0.9915 1.2274 1.3436 -0.1276 -0.1157 0.1798  162 GLY D C   
21747 O O   . GLY D 162 ? 1.0283 1.1759 1.3560 -0.1408 -0.1179 0.1814  162 GLY D O   
21751 N N   . SER D 163 ? 1.3404 1.2069 1.5248 0.0208  -0.1321 0.1709  163 SER D N   
21752 C CA  . SER D 163 ? 1.3967 1.2354 1.5651 0.0124  -0.1152 0.1626  163 SER D CA  
21753 C C   . SER D 163 ? 1.4490 1.2428 1.5453 0.0226  -0.1036 0.1362  163 SER D C   
21754 O O   . SER D 163 ? 1.5042 1.2705 1.5626 0.0168  -0.1052 0.1273  163 SER D O   
21755 C CB  . SER D 163 ? 1.3865 1.2465 1.6111 0.0195  -0.0798 0.1826  163 SER D CB  
21756 O OG  . SER D 163 ? 1.4550 1.2863 1.6554 0.0174  -0.0566 0.1740  163 SER D OG  
21762 N N   . LEU D 164 ? 1.4267 1.2163 1.5038 0.0379  -0.0891 0.1251  164 LEU D N   
21763 C CA  . LEU D 164 ? 1.3822 1.1478 1.3935 0.0448  -0.0797 0.0987  164 LEU D CA  
21764 C C   . LEU D 164 ? 1.3912 1.1465 1.3602 0.0449  -0.1113 0.0855  164 LEU D C   
21765 O O   . LEU D 164 ? 1.4221 1.1852 1.4002 0.0492  -0.1176 0.0858  164 LEU D O   
21766 C CB  . LEU D 164 ? 1.3443 1.1118 1.3563 0.0533  -0.0415 0.0877  164 LEU D CB  
21767 C CG  . LEU D 164 ? 1.3704 1.1455 1.4260 0.0550  -0.0035 0.0998  164 LEU D CG  
21768 C CD1 . LEU D 164 ? 1.3903 1.1565 1.4406 0.0596  0.0383  0.0830  164 LEU D CD1 
21769 C CD2 . LEU D 164 ? 1.3980 1.1714 1.4330 0.0511  0.0050  0.0982  164 LEU D CD2 
21781 N N   . SER D 165 ? 1.4467 1.1818 1.3691 0.0428  -0.1274 0.0765  165 SER D N   
21782 C CA  . SER D 165 ? 1.4859 1.2076 1.3630 0.0447  -0.1538 0.0632  165 SER D CA  
21783 C C   . SER D 165 ? 1.4755 1.1895 1.2905 0.0579  -0.1449 0.0459  165 SER D C   
21784 O O   . SER D 165 ? 1.4310 1.1543 1.2192 0.0637  -0.1460 0.0302  165 SER D O   
21785 C CB  . SER D 165 ? 1.5790 1.2831 1.4561 0.0301  -0.1808 0.0691  165 SER D CB  
21786 O OG  . SER D 165 ? 1.6751 1.3525 1.5349 0.0283  -0.1693 0.0721  165 SER D OG  
21792 N N   . ALA D 166 ? 1.4969 1.1994 1.2888 0.0637  -0.1345 0.0507  166 ALA D N   
21793 C CA  . ALA D 166 ? 1.5221 1.2377 1.2607 0.0806  -0.1223 0.0407  166 ALA D CA  
21794 C C   . ALA D 166 ? 1.4389 1.1919 1.1803 0.0790  -0.1008 0.0250  166 ALA D C   
21795 O O   . ALA D 166 ? 1.4038 1.1624 1.1875 0.0699  -0.0826 0.0279  166 ALA D O   
21796 C CB  . ALA D 166 ? 1.6126 1.3174 1.3354 0.0910  -0.1060 0.0565  166 ALA D CB  
21802 N N   . GLY D 167 ? 1.4008 1.1802 1.0966 0.0862  -0.0998 0.0069  167 GLY D N   
21803 C CA  . GLY D 167 ? 1.3593 1.1738 1.0510 0.0768  -0.0765 -0.0156 167 GLY D CA  
21804 C C   . GLY D 167 ? 1.3152 1.1164 1.0348 0.0639  -0.0734 -0.0273 167 GLY D C   
21805 O O   . GLY D 167 ? 1.3317 1.1479 1.0532 0.0517  -0.0451 -0.0476 167 GLY D O   
21809 N N   . VAL D 168 ? 1.2917 1.0650 1.0310 0.0656  -0.0981 -0.0151 168 VAL D N   
21810 C CA  . VAL D 168 ? 1.2715 1.0343 1.0345 0.0599  -0.0957 -0.0190 168 VAL D CA  
21811 C C   . VAL D 168 ? 1.2677 1.0334 0.9895 0.0626  -0.1149 -0.0335 168 VAL D C   
21812 O O   . VAL D 168 ? 1.2560 1.0185 0.9474 0.0714  -0.1408 -0.0297 168 VAL D O   
21813 C CB  . VAL D 168 ? 1.2244 0.9703 1.0399 0.0609  -0.1103 0.0084  168 VAL D CB  
21814 C CG1 . VAL D 168 ? 1.2072 0.9475 1.0444 0.0622  -0.1066 0.0119  168 VAL D CG1 
21815 C CG2 . VAL D 168 ? 1.2251 0.9738 1.0854 0.0586  -0.0890 0.0242  168 VAL D CG2 
21825 N N   . HIS D 169 ? 1.2586 1.0259 0.9788 0.0552  -0.0974 -0.0500 169 HIS D N   
21826 C CA  . HIS D 169 ? 1.2575 1.0279 0.9442 0.0563  -0.1121 -0.0631 169 HIS D CA  
21827 C C   . HIS D 169 ? 1.2811 1.0283 0.9969 0.0540  -0.1007 -0.0574 169 HIS D C   
21828 O O   . HIS D 169 ? 1.3064 1.0484 1.0284 0.0431  -0.0637 -0.0734 169 HIS D O   
21829 C CB  . HIS D 169 ? 1.2613 1.0691 0.9043 0.0474  -0.0967 -0.0938 169 HIS D CB  
21830 C CG  . HIS D 169 ? 1.2221 1.0623 0.8305 0.0586  -0.1105 -0.0919 169 HIS D CG  
21831 N ND1 . HIS D 169 ? 1.2228 1.0544 0.8080 0.0771  -0.1409 -0.0773 169 HIS D ND1 
21832 C CD2 . HIS D 169 ? 1.2196 1.1014 0.8106 0.0563  -0.0942 -0.1006 169 HIS D CD2 
21833 C CE1 . HIS D 169 ? 1.2294 1.0914 0.7867 0.0897  -0.1401 -0.0732 169 HIS D CE1 
21834 N NE2 . HIS D 169 ? 1.2292 1.1278 0.7895 0.0780  -0.1143 -0.0858 169 HIS D NE2 
21842 N N   . THR D 170 ? 1.2902 1.0238 1.0221 0.0638  -0.1291 -0.0343 170 THR D N   
21843 C CA  . THR D 170 ? 1.2204 0.9401 0.9750 0.0684  -0.1223 -0.0216 170 THR D CA  
21844 C C   . THR D 170 ? 1.1718 0.8913 0.8836 0.0689  -0.1363 -0.0363 170 THR D C   
21845 O O   . THR D 170 ? 1.1534 0.8785 0.8353 0.0734  -0.1711 -0.0367 170 THR D O   
21846 C CB  . THR D 170 ? 1.1898 0.9127 0.9855 0.0779  -0.1465 0.0134  170 THR D CB  
21847 O OG1 . THR D 170 ? 1.1893 0.9173 1.0283 0.0773  -0.1315 0.0279  170 THR D OG1 
21848 C CG2 . THR D 170 ? 1.1943 0.9128 1.0126 0.0890  -0.1379 0.0337  170 THR D CG2 
21856 N N   . PHE D 171 ? 1.1549 0.8638 0.8632 0.0636  -0.1050 -0.0487 171 PHE D N   
21857 C CA  . PHE D 171 ? 1.1790 0.8901 0.8481 0.0611  -0.1113 -0.0652 171 PHE D CA  
21858 C C   . PHE D 171 ? 1.2116 0.9078 0.8923 0.0752  -0.1249 -0.0394 171 PHE D C   
21859 O O   . PHE D 171 ? 1.2661 0.9529 0.9893 0.0860  -0.1164 -0.0099 171 PHE D O   
21860 C CB  . PHE D 171 ? 1.2121 0.9213 0.8687 0.0414  -0.0657 -0.0969 171 PHE D CB  
21861 C CG  . PHE D 171 ? 1.1984 0.9375 0.8388 0.0248  -0.0524 -0.1245 171 PHE D CG  
21862 C CD1 . PHE D 171 ? 1.1964 0.9283 0.8656 0.0197  -0.0274 -0.1222 171 PHE D CD1 
21863 C CD2 . PHE D 171 ? 1.1705 0.9527 0.7669 0.0164  -0.0643 -0.1500 171 PHE D CD2 
21864 C CE1 . PHE D 171 ? 1.1836 0.9497 0.8341 0.0046  -0.0156 -0.1465 171 PHE D CE1 
21865 C CE2 . PHE D 171 ? 1.1470 0.9717 0.7271 0.0034  -0.0534 -0.1713 171 PHE D CE2 
21866 C CZ  . PHE D 171 ? 1.1776 0.9938 0.7829 -0.0034 -0.0295 -0.1704 171 PHE D CZ  
21876 N N   . PRO D 172 ? 1.2084 0.9088 0.8518 0.0778  -0.1458 -0.0467 172 PRO D N   
21877 C CA  . PRO D 172 ? 1.2238 0.9147 0.8728 0.0911  -0.1559 -0.0224 172 PRO D CA  
21878 C C   . PRO D 172 ? 1.2632 0.9293 0.9319 0.0921  -0.1080 -0.0169 172 PRO D C   
21879 O O   . PRO D 172 ? 1.3148 0.9683 0.9762 0.0751  -0.0683 -0.0446 172 PRO D O   
21880 C CB  . PRO D 172 ? 1.2400 0.9395 0.8376 0.0915  -0.1839 -0.0382 172 PRO D CB  
21881 C CG  . PRO D 172 ? 1.2242 0.9390 0.7933 0.0788  -0.1744 -0.0715 172 PRO D CG  
21882 C CD  . PRO D 172 ? 1.1887 0.9086 0.7834 0.0733  -0.1647 -0.0719 172 PRO D CD  
21890 N N   . ALA D 173 ? 1.2729 0.9338 0.9656 0.1114  -0.1093 0.0198  173 ALA D N   
21891 C CA  . ALA D 173 ? 1.2755 0.9045 0.9901 0.1199  -0.0578 0.0352  173 ALA D CA  
21892 C C   . ALA D 173 ? 1.2602 0.8704 0.9358 0.1105  -0.0393 0.0129  173 ALA D C   
21893 O O   . ALA D 173 ? 1.2323 0.8620 0.8674 0.1051  -0.0738 -0.0041 173 ALA D O   
21894 C CB  . ALA D 173 ? 1.2785 0.9203 1.0299 0.1499  -0.0659 0.0890  173 ALA D CB  
21900 N N   . VAL D 174 ? 1.3186 0.8868 1.0072 0.1082  0.0208  0.0132  174 VAL D N   
21901 C CA  . VAL D 174 ? 1.3747 0.9194 1.0322 0.0958  0.0494  -0.0072 174 VAL D CA  
21902 C C   . VAL D 174 ? 1.4515 0.9514 1.1337 0.1189  0.0977  0.0316  174 VAL D C   
21903 O O   . VAL D 174 ? 1.4631 0.9402 1.1873 0.1361  0.1307  0.0607  174 VAL D O   
21904 C CB  . VAL D 174 ? 1.4094 0.9442 1.0475 0.0558  0.0877  -0.0625 174 VAL D CB  
21905 C CG1 . VAL D 174 ? 1.4528 0.9841 1.0537 0.0375  0.1019  -0.0888 174 VAL D CG1 
21906 C CG2 . VAL D 174 ? 1.3546 0.9364 0.9798 0.0410  0.0495  -0.0896 174 VAL D CG2 
21916 N N   . LEU D 175 ? 1.5177 1.0055 1.1739 0.1226  0.1049  0.0354  175 LEU D N   
21917 C CA  . LEU D 175 ? 1.6088 1.0481 1.2827 0.1455  0.1594  0.0726  175 LEU D CA  
21918 C C   . LEU D 175 ? 1.7286 1.1013 1.4070 0.1177  0.2417  0.0407  175 LEU D C   
21919 O O   . LEU D 175 ? 1.7247 1.0983 1.3747 0.0748  0.2520  -0.0165 175 LEU D O   
21920 C CB  . LEU D 175 ? 1.6028 1.0496 1.2441 0.1573  0.1427  0.0866  175 LEU D CB  
21921 C CG  . LEU D 175 ? 1.5902 1.0916 1.2303 0.1912  0.0787  0.1314  175 LEU D CG  
21922 C CD1 . LEU D 175 ? 1.6345 1.1413 1.2341 0.1976  0.0658  0.1366  175 LEU D CD1 
21923 C CD2 . LEU D 175 ? 1.6084 1.1138 1.2965 0.2319  0.0945  0.1947  175 LEU D CD2 
21935 N N   . GLN D 176 ? 1.8460 1.1639 1.5596 0.1421  0.3033  0.0782  176 GLN D N   
21936 C CA  . GLN D 176 ? 1.9408 1.1830 1.6619 0.1156  0.3907  0.0484  176 GLN D CA  
21937 C C   . GLN D 176 ? 1.9991 1.1729 1.7470 0.1555  0.4602  0.1046  176 GLN D C   
21938 O O   . GLN D 176 ? 2.0011 1.1693 1.7920 0.1955  0.4748  0.1550  176 GLN D O   
21939 C CB  . GLN D 176 ? 1.9524 1.2006 1.6959 0.1009  0.3951  0.0273  176 GLN D CB  
21940 C CG  . GLN D 176 ? 2.0095 1.1820 1.7550 0.0665  0.4849  -0.0123 176 GLN D CG  
21941 C CD  . GLN D 176 ? 1.9802 1.1644 1.7467 0.0561  0.4858  -0.0289 176 GLN D CD  
21942 O OE1 . GLN D 176 ? 1.9449 1.1347 1.7531 0.0963  0.4793  0.0201  176 GLN D OE1 
21943 N NE2 . GLN D 176 ? 1.9852 1.1824 1.7229 0.0022  0.4924  -0.0967 176 GLN D NE2 
21952 N N   . SER D 177 ? 2.0420 1.1671 1.7657 0.1467  0.5051  0.0987  177 SER D N   
21953 C CA  . SER D 177 ? 2.1470 1.2044 1.8906 0.1893  0.5743  0.1575  177 SER D CA  
21954 C C   . SER D 177 ? 2.0475 1.1665 1.8150 0.2543  0.5214  0.2381  177 SER D C   
21955 O O   . SER D 177 ? 2.0857 1.1792 1.8911 0.3045  0.5645  0.3030  177 SER D O   
21956 C CB  . SER D 177 ? 2.3303 1.2985 2.1049 0.1902  0.6699  0.1597  177 SER D CB  
21957 O OG  . SER D 177 ? 2.4232 1.3350 2.1707 0.1238  0.7249  0.0812  177 SER D OG  
21963 N N   . SER D 178 ? 1.9272 1.1324 1.6714 0.2528  0.4292  0.2340  178 SER D N   
21964 C CA  . SER D 178 ? 1.9052 1.1850 1.6615 0.3020  0.3682  0.2982  178 SER D CA  
21965 C C   . SER D 178 ? 1.8749 1.2095 1.6765 0.3256  0.3337  0.3295  178 SER D C   
21966 O O   . SER D 178 ? 1.8559 1.2461 1.6831 0.3724  0.3085  0.3952  178 SER D O   
21967 C CB  . SER D 178 ? 1.9901 1.2384 1.7542 0.3510  0.4184  0.3659  178 SER D CB  
21968 O OG  . SER D 178 ? 2.0298 1.2321 1.7514 0.3291  0.4469  0.3393  178 SER D OG  
21974 N N   . LEU D 179 ? 1.1259 1.1709 1.1943 0.0231  -0.0939 0.1249  179 LEU D N   
21975 C CA  . LEU D 179 ? 1.0921 1.0630 1.1249 0.0210  -0.1037 0.0655  179 LEU D CA  
21976 C C   . LEU D 179 ? 1.1096 1.0815 1.1082 0.0353  -0.0861 0.0432  179 LEU D C   
21977 O O   . LEU D 179 ? 1.1117 1.1370 1.1359 0.0333  -0.0743 0.0642  179 LEU D O   
21978 C CB  . LEU D 179 ? 0.9965 0.9372 1.1018 -0.0217 -0.1326 0.0347  179 LEU D CB  
21979 C CG  . LEU D 179 ? 0.9526 0.8725 1.0915 -0.0379 -0.1563 0.0455  179 LEU D CG  
21980 C CD1 . LEU D 179 ? 0.9076 0.8056 1.1271 -0.0775 -0.1838 0.0140  179 LEU D CD1 
21981 C CD2 . LEU D 179 ? 0.9706 0.8319 1.0368 -0.0137 -0.1588 0.0294  179 LEU D CD2 
21993 N N   . TYR D 180 ? 1.1508 1.0627 1.0969 0.0486  -0.0876 0.0034  180 TYR D N   
21994 C CA  . TYR D 180 ? 1.2042 1.1110 1.1143 0.0643  -0.0731 -0.0154 180 TYR D CA  
21995 C C   . TYR D 180 ? 1.1644 1.0704 1.1243 0.0315  -0.0798 -0.0436 180 TYR D C   
21996 O O   . TYR D 180 ? 1.1470 1.0259 1.1476 0.0048  -0.0973 -0.0671 180 TYR D O   
21997 C CB  . TYR D 180 ? 1.2608 1.1026 1.0997 0.0933  -0.0767 -0.0414 180 TYR D CB  
21998 C CG  . TYR D 180 ? 1.3395 1.1802 1.1067 0.1387  -0.0684 -0.0207 180 TYR D CG  
21999 C CD1 . TYR D 180 ? 1.3633 1.2548 1.0995 0.1704  -0.0431 0.0067  180 TYR D CD1 
22000 C CD2 . TYR D 180 ? 1.3677 1.1567 1.0953 0.1532  -0.0864 -0.0293 180 TYR D CD2 
22001 C CE1 . TYR D 180 ? 1.4111 1.3053 1.0753 0.2190  -0.0324 0.0238  180 TYR D CE1 
22002 C CE2 . TYR D 180 ? 1.4216 1.2085 1.0718 0.2009  -0.0797 -0.0137 180 TYR D CE2 
22003 C CZ  . TYR D 180 ? 1.4431 1.2840 1.0597 0.2357  -0.0509 0.0120  180 TYR D CZ  
22004 O OH  . TYR D 180 ? 1.4939 1.3364 1.0277 0.2899  -0.0414 0.0258  180 TYR D OH  
22014 N N   . THR D 181 ? 1.0963 1.0337 1.0503 0.0367  -0.0656 -0.0410 181 THR D N   
22015 C CA  . THR D 181 ? 1.0398 0.9817 1.0259 0.0129  -0.0694 -0.0661 181 THR D CA  
22016 C C   . THR D 181 ? 1.0306 0.9643 0.9697 0.0326  -0.0544 -0.0758 181 THR D C   
22017 O O   . THR D 181 ? 1.0645 1.0226 0.9713 0.0580  -0.0400 -0.0531 181 THR D O   
22018 C CB  . THR D 181 ? 1.0413 1.0391 1.0838 -0.0075 -0.0753 -0.0475 181 THR D CB  
22019 O OG1 . THR D 181 ? 1.0545 1.0629 1.1463 -0.0238 -0.0916 -0.0291 181 THR D OG1 
22020 C CG2 . THR D 181 ? 1.0178 1.0133 1.0861 -0.0295 -0.0846 -0.0808 181 THR D CG2 
22028 N N   . LEU D 182 ? 1.0159 0.9186 0.9556 0.0219  -0.0575 -0.1063 182 LEU D N   
22029 C CA  . LEU D 182 ? 0.9949 0.8859 0.8982 0.0372  -0.0470 -0.1128 182 LEU D CA  
22030 C C   . LEU D 182 ? 0.9539 0.8608 0.8813 0.0165  -0.0450 -0.1308 182 LEU D C   
22031 O O   . LEU D 182 ? 0.9448 0.8496 0.9089 -0.0054 -0.0534 -0.1499 182 LEU D O   
22032 C CB  . LEU D 182 ? 1.0264 0.8558 0.8993 0.0524  -0.0542 -0.1256 182 LEU D CB  
22033 C CG  . LEU D 182 ? 1.0742 0.8837 0.9137 0.0711  -0.0497 -0.1272 182 LEU D CG  
22034 C CD1 . LEU D 182 ? 1.0944 0.8471 0.8926 0.0994  -0.0631 -0.1300 182 LEU D CD1 
22035 C CD2 . LEU D 182 ? 1.1183 0.9199 0.9856 0.0506  -0.0494 -0.1426 182 LEU D CD2 
22047 N N   . SER D 183 ? 0.9243 0.8479 0.8280 0.0265  -0.0339 -0.1247 183 SER D N   
22048 C CA  . SER D 183 ? 0.9690 0.9122 0.8826 0.0126  -0.0297 -0.1378 183 SER D CA  
22049 C C   . SER D 183 ? 0.9956 0.9250 0.8795 0.0265  -0.0203 -0.1325 183 SER D C   
22050 O O   . SER D 183 ? 0.8195 0.7327 0.6754 0.0485  -0.0192 -0.1180 183 SER D O   
22051 C CB  . SER D 183 ? 0.9740 0.9681 0.9003 0.0046  -0.0315 -0.1294 183 SER D CB  
22052 O OG  . SER D 183 ? 0.9596 0.9764 0.8674 0.0226  -0.0250 -0.1009 183 SER D OG  
22058 N N   . SER D 184 ? 0.9931 0.9304 0.8844 0.0157  -0.0146 -0.1433 184 SER D N   
22059 C CA  . SER D 184 ? 0.9594 0.8884 0.8339 0.0248  -0.0072 -0.1323 184 SER D CA  
22060 C C   . SER D 184 ? 0.9671 0.9351 0.8426 0.0147  0.0036  -0.1356 184 SER D C   
22061 O O   . SER D 184 ? 0.9586 0.9408 0.8511 0.0019  0.0050  -0.1557 184 SER D O   
22062 C CB  . SER D 184 ? 0.9166 0.7958 0.8042 0.0263  -0.0135 -0.1358 184 SER D CB  
22063 O OG  . SER D 184 ? 0.9057 0.7758 0.7871 0.0342  -0.0114 -0.1193 184 SER D OG  
22069 N N   . SER D 185 ? 0.9984 0.9831 0.8531 0.0232  0.0099  -0.1163 185 SER D N   
22070 C CA  . SER D 185 ? 1.0612 1.0849 0.9068 0.0176  0.0207  -0.1140 185 SER D CA  
22071 C C   . SER D 185 ? 1.0525 1.0670 0.9016 0.0214  0.0287  -0.0933 185 SER D C   
22072 O O   . SER D 185 ? 1.0514 1.0353 0.9003 0.0319  0.0209  -0.0759 185 SER D O   
22073 C CB  . SER D 185 ? 1.1492 1.2094 0.9717 0.0217  0.0181  -0.1029 185 SER D CB  
22074 O OG  . SER D 185 ? 1.2298 1.2896 1.0376 0.0333  0.0210  -0.0759 185 SER D OG  
22080 N N   . VAL D 186 ? 1.0085 1.0507 0.8628 0.0148  0.0428  -0.0942 186 VAL D N   
22081 C CA  . VAL D 186 ? 1.0120 1.0615 0.8769 0.0162  0.0530  -0.0655 186 VAL D CA  
22082 C C   . VAL D 186 ? 1.0109 1.1167 0.8459 0.0175  0.0674  -0.0562 186 VAL D C   
22083 O O   . VAL D 186 ? 1.0101 1.1452 0.8265 0.0162  0.0733  -0.0811 186 VAL D O   
22084 C CB  . VAL D 186 ? 1.0267 1.0623 0.9333 0.0095  0.0604  -0.0669 186 VAL D CB  
22085 C CG1 . VAL D 186 ? 1.0550 1.1222 0.9604 0.0055  0.0747  -0.0956 186 VAL D CG1 
22086 C CG2 . VAL D 186 ? 1.0500 1.0976 0.9806 0.0095  0.0692  -0.0273 186 VAL D CG2 
22096 N N   . THR D 187 ? 1.0187 1.1370 0.8478 0.0217  0.0694  -0.0212 187 THR D N   
22097 C CA  . THR D 187 ? 1.0853 1.2569 0.8814 0.0243  0.0812  -0.0063 187 THR D CA  
22098 C C   . THR D 187 ? 1.1298 1.3235 0.9478 0.0235  0.0975  0.0322  187 THR D C   
22099 O O   . THR D 187 ? 1.1388 1.3059 0.9895 0.0225  0.0880  0.0636  187 THR D O   
22100 C CB  . THR D 187 ? 1.1088 1.2846 0.8798 0.0294  0.0672  0.0071  187 THR D CB  
22101 O OG1 . THR D 187 ? 1.1089 1.2715 0.8703 0.0297  0.0535  -0.0214 187 THR D OG1 
22102 C CG2 . THR D 187 ? 1.1528 1.3822 0.8865 0.0316  0.0756  0.0226  187 THR D CG2 
22110 N N   . VAL D 188 ? 1.1730 1.4163 0.9747 0.0261  0.1206  0.0311  188 VAL D N   
22111 C CA  . VAL D 188 ? 1.2327 1.5124 1.0579 0.0269  0.1424  0.0735  188 VAL D CA  
22112 C C   . VAL D 188 ? 1.2761 1.6208 1.0462 0.0367  0.1597  0.0857  188 VAL D C   
22113 O O   . VAL D 188 ? 1.2967 1.6520 1.0128 0.0424  0.1514  0.0553  188 VAL D O   
22114 C CB  . VAL D 188 ? 1.2401 1.5229 1.1067 0.0255  0.1605  0.0655  188 VAL D CB  
22115 C CG1 . VAL D 188 ? 1.1862 1.4015 1.1072 0.0156  0.1389  0.0580  188 VAL D CG1 
22116 C CG2 . VAL D 188 ? 1.2751 1.5817 1.1027 0.0346  0.1726  0.0160  188 VAL D CG2 
22126 N N   . VAL D 189 ? 1.2749 1.6643 1.0617 0.0391  0.1820  0.1339  189 VAL D N   
22127 C CA  . VAL D 189 ? 1.3866 1.8435 1.1169 0.0516  0.2013  0.1518  189 VAL D CA  
22128 C C   . VAL D 189 ? 1.4863 1.9746 1.1670 0.0681  0.2195  0.1043  189 VAL D C   
22129 O O   . VAL D 189 ? 1.5089 1.9880 1.2201 0.0698  0.2313  0.0808  189 VAL D O   
22130 C CB  . VAL D 189 ? 1.4419 1.9451 1.2105 0.0508  0.2235  0.2221  189 VAL D CB  
22131 C CG1 . VAL D 189 ? 1.4628 2.0365 1.1655 0.0649  0.2413  0.2471  189 VAL D CG1 
22132 C CG2 . VAL D 189 ? 1.4834 1.9418 1.3163 0.0345  0.1976  0.2644  189 VAL D CG2 
22142 N N   . ALA D 190 ? 1.5774 2.0999 1.1813 0.0819  0.2182  0.0880  190 ALA D N   
22143 C CA  . ALA D 190 ? 1.6617 2.2084 1.2106 0.1024  0.2280  0.0365  190 ALA D CA  
22144 C C   . ALA D 190 ? 1.6540 2.2530 1.2148 0.1193  0.2706  0.0531  190 ALA D C   
22145 O O   . ALA D 190 ? 1.7264 2.3254 1.2819 0.1327  0.2801  0.0080  190 ALA D O   
22146 C CB  . ALA D 190 ? 1.7864 2.3622 1.2480 0.1170  0.2155  0.0230  190 ALA D CB  
22152 N N   . SER D 191 ? 1.5933 2.2399 1.1766 0.1197  0.2964  0.1208  191 SER D N   
22153 C CA  . SER D 191 ? 1.6458 2.3575 1.2440 0.1381  0.3418  0.1492  191 SER D CA  
22154 C C   . SER D 191 ? 1.6040 2.2909 1.2987 0.1252  0.3513  0.1574  191 SER D C   
22155 O O   . SER D 191 ? 1.6550 2.3950 1.3724 0.1415  0.3895  0.1756  191 SER D O   
22156 C CB  . SER D 191 ? 1.6826 2.4596 1.2816 0.1407  0.3645  0.2293  191 SER D CB  
22157 O OG  . SER D 191 ? 1.6399 2.3812 1.3199 0.1110  0.3450  0.2815  191 SER D OG  
22163 N N   . THR D 192 ? 1.5310 2.1415 1.2817 0.0990  0.3177  0.1458  192 THR D N   
22164 C CA  . THR D 192 ? 1.5139 2.0922 1.3557 0.0853  0.3187  0.1540  192 THR D CA  
22165 C C   . THR D 192 ? 1.4647 1.9941 1.3066 0.0856  0.3045  0.0837  192 THR D C   
22166 O O   . THR D 192 ? 1.4046 1.9002 1.3185 0.0737  0.3004  0.0840  192 THR D O   
22167 C CB  . THR D 192 ? 1.4979 2.0215 1.4059 0.0587  0.2883  0.1937  192 THR D CB  
22168 O OG1 . THR D 192 ? 1.5303 1.9944 1.4013 0.0503  0.2511  0.1564  192 THR D OG1 
22169 C CG2 . THR D 192 ? 1.4974 2.0692 1.4256 0.0562  0.2999  0.2707  192 THR D CG2 
22177 N N   . TRP D 193 ? 1.8336 1.8771 1.1911 0.2070  0.3027  0.3120  193 TRP D N   
22178 C CA  . TRP D 193 ? 1.7044 1.7955 1.1304 0.2020  0.2931  0.2477  193 TRP D CA  
22179 C C   . TRP D 193 ? 1.7385 1.8745 1.0871 0.2306  0.2841  0.2107  193 TRP D C   
22180 O O   . TRP D 193 ? 1.7991 1.9291 1.0692 0.2584  0.2515  0.2169  193 TRP D O   
22181 C CB  . TRP D 193 ? 1.5914 1.6675 1.0899 0.2011  0.2464  0.2186  193 TRP D CB  
22182 C CG  . TRP D 193 ? 1.4237 1.5353 0.9967 0.1904  0.2412  0.1630  193 TRP D CG  
22183 C CD1 . TRP D 193 ? 1.3115 1.4255 0.9685 0.1647  0.2604  0.1544  193 TRP D CD1 
22184 C CD2 . TRP D 193 ? 1.3594 1.5041 0.9292 0.2051  0.2119  0.1099  193 TRP D CD2 
22185 N NE1 . TRP D 193 ? 1.2173 1.3591 0.9175 0.1664  0.2461  0.1032  193 TRP D NE1 
22186 C CE2 . TRP D 193 ? 1.2584 1.4156 0.9079 0.1884  0.2178  0.0751  193 TRP D CE2 
22187 C CE3 . TRP D 193 ? 1.3969 1.5601 0.9063 0.2298  0.1778  0.0880  193 TRP D CE3 
22188 C CZ2 . TRP D 193 ? 1.2455 1.4228 0.9144 0.1938  0.1942  0.0228  193 TRP D CZ2 
22189 C CZ3 . TRP D 193 ? 1.3765 1.5662 0.9119 0.2312  0.1528  0.0314  193 TRP D CZ3 
22190 C CH2 . TRP D 193 ? 1.3100 1.5016 0.9235 0.2125  0.1629  0.0009  193 TRP D CH2 
22201 N N   . PRO D 194 ? 1.6909 1.8713 1.0594 0.2278  0.3082  0.1684  194 PRO D N   
22202 C CA  . PRO D 194 ? 1.6035 1.8014 1.0707 0.2017  0.3399  0.1545  194 PRO D CA  
22203 C C   . PRO D 194 ? 1.6566 1.8698 1.1270 0.1834  0.4030  0.1968  194 PRO D C   
22204 O O   . PRO D 194 ? 1.6112 1.8564 1.1633 0.1671  0.4299  0.1796  194 PRO D O   
22205 C CB  . PRO D 194 ? 1.5526 1.7900 1.0261 0.2176  0.3324  0.0869  194 PRO D CB  
22206 C CG  . PRO D 194 ? 1.5913 1.8274 0.9810 0.2449  0.2888  0.0616  194 PRO D CG  
22207 C CD  . PRO D 194 ? 1.6948 1.9102 0.9962 0.2553  0.2917  0.1185  194 PRO D CD  
22215 N N   . SER D 195 ? 1.7584 1.9509 1.1470 0.1854  0.4262  0.2534  195 SER D N   
22216 C CA  . SER D 195 ? 1.8388 2.0510 1.2328 0.1630  0.4924  0.2978  195 SER D CA  
22217 C C   . SER D 195 ? 1.8094 2.0129 1.3327 0.1210  0.5040  0.3122  195 SER D C   
22218 O O   . SER D 195 ? 1.8305 2.0821 1.4142 0.1000  0.5527  0.3172  195 SER D O   
22219 C CB  . SER D 195 ? 1.9546 2.1276 1.2398 0.1677  0.5107  0.3668  195 SER D CB  
22220 O OG  . SER D 195 ? 1.9442 2.0429 1.2466 0.1558  0.4768  0.4051  195 SER D OG  
22226 N N   . GLN D 196 ? 1.7880 1.9353 1.3561 0.1102  0.4589  0.3165  196 GLN D N   
22227 C CA  . GLN D 196 ? 1.7359 1.8686 1.4195 0.0739  0.4565  0.3199  196 GLN D CA  
22228 C C   . GLN D 196 ? 1.5988 1.7340 1.3434 0.0832  0.4085  0.2634  196 GLN D C   
22229 O O   . GLN D 196 ? 1.5352 1.6573 1.2354 0.1103  0.3697  0.2379  196 GLN D O   
22230 C CB  . GLN D 196 ? 1.8124 1.8657 1.4902 0.0529  0.4474  0.3746  196 GLN D CB  
22231 C CG  . GLN D 196 ? 1.9967 2.0327 1.6078 0.0409  0.4948  0.4407  196 GLN D CG  
22232 C CD  . GLN D 196 ? 2.1678 2.1058 1.7460 0.0330  0.4755  0.4933  196 GLN D CD  
22233 O OE1 . GLN D 196 ? 2.2767 2.1724 1.7720 0.0682  0.4416  0.5016  196 GLN D OE1 
22234 N NE2 . GLN D 196 ? 2.2090 2.1096 1.8565 -0.0123 0.4942  0.5275  196 GLN D NE2 
22243 N N   . SER D 197 ? 1.5087 1.6635 1.3568 0.0596  0.4110  0.2460  197 SER D N   
22244 C CA  . SER D 197 ? 1.4385 1.6020 1.3416 0.0686  0.3737  0.1951  197 SER D CA  
22245 C C   . SER D 197 ? 1.3904 1.4929 1.3149 0.0608  0.3308  0.1992  197 SER D C   
22246 O O   . SER D 197 ? 1.4256 1.4924 1.3838 0.0348  0.3328  0.2281  197 SER D O   
22247 C CB  . SER D 197 ? 1.4264 1.6435 1.4250 0.0544  0.3932  0.1735  197 SER D CB  
22248 O OG  . SER D 197 ? 1.3762 1.5704 1.4537 0.0249  0.3771  0.1839  197 SER D OG  
22254 N N   . ILE D 198 ? 1.2928 1.3842 1.1993 0.0825  0.2932  0.1682  198 ILE D N   
22255 C CA  . ILE D 198 ? 1.1839 1.2280 1.1070 0.0820  0.2558  0.1656  198 ILE D CA  
22256 C C   . ILE D 198 ? 1.1078 1.1687 1.0917 0.0803  0.2361  0.1264  198 ILE D C   
22257 O O   . ILE D 198 ? 1.0883 1.1810 1.0700 0.0943  0.2323  0.0951  198 ILE D O   
22258 C CB  . ILE D 198 ? 1.1564 1.1799 1.0126 0.1087  0.2308  0.1682  198 ILE D CB  
22259 C CG1 . ILE D 198 ? 1.2624 1.2554 1.0543 0.1129  0.2458  0.2150  198 ILE D CG1 
22260 C CG2 . ILE D 198 ? 1.0811 1.0716 0.9620 0.1134  0.1965  0.1568  198 ILE D CG2 
22261 C CD1 . ILE D 198 ? 1.3330 1.3086 1.0606 0.1442  0.2175  0.2219  198 ILE D CD1 
22273 N N   . THR D 199 ? 1.0915 1.1248 1.1240 0.0638  0.2215  0.1282  199 THR D N   
22274 C CA  . THR D 199 ? 1.0544 1.0980 1.1385 0.0621  0.2024  0.0984  199 THR D CA  
22275 C C   . THR D 199 ? 1.0515 1.0506 1.1298 0.0656  0.1717  0.0947  199 THR D C   
22276 O O   . THR D 199 ? 1.0702 1.0263 1.1348 0.0600  0.1662  0.1140  199 THR D O   
22277 C CB  . THR D 199 ? 1.0777 1.1447 1.2321 0.0406  0.2132  0.0988  199 THR D CB  
22278 O OG1 . THR D 199 ? 1.1188 1.2382 1.2835 0.0413  0.2480  0.1001  199 THR D OG1 
22279 C CG2 . THR D 199 ? 1.0442 1.1168 1.2431 0.0443  0.1874  0.0712  199 THR D CG2 
22287 N N   . CYS D 200 ? 1.0441 1.0507 1.1313 0.0756  0.1539  0.0700  200 CYS D N   
22288 C CA  . CYS D 200 ? 1.0586 1.0336 1.1405 0.0806  0.1305  0.0640  200 CYS D CA  
22289 C C   . CYS D 200 ? 1.0420 1.0091 1.1654 0.0687  0.1178  0.0551  200 CYS D C   
22290 O O   . CYS D 200 ? 1.0668 1.0575 1.2183 0.0698  0.1148  0.0404  200 CYS D O   
22291 C CB  . CYS D 200 ? 1.0725 1.0632 1.1390 0.0949  0.1218  0.0478  200 CYS D CB  
22292 S SG  . CYS D 200 ? 1.1431 1.1109 1.2073 0.1007  0.1029  0.0405  200 CYS D SG  
22297 N N   . ASN D 201 ? 1.0132 0.9434 1.1386 0.0594  0.1067  0.0624  201 ASN D N   
22298 C CA  . ASN D 201 ? 0.9730 0.8939 1.1316 0.0487  0.0867  0.0517  201 ASN D CA  
22299 C C   . ASN D 201 ? 0.9540 0.8447 1.0779 0.0635  0.0664  0.0404  201 ASN D C   
22300 O O   . ASN D 201 ? 0.9334 0.7868 1.0217 0.0715  0.0623  0.0429  201 ASN D O   
22301 C CB  . ASN D 201 ? 0.9902 0.8870 1.1734 0.0257  0.0834  0.0617  201 ASN D CB  
22302 C CG  . ASN D 201 ? 1.0025 0.9171 1.1981 0.0117  0.1133  0.0844  201 ASN D CG  
22303 O OD1 . ASN D 201 ? 1.0371 0.9131 1.2003 0.0099  0.1213  0.1039  201 ASN D OD1 
22304 N ND2 . ASN D 201 ? 0.9686 0.9403 1.2081 0.0048  0.1315  0.0835  201 ASN D ND2 
22311 N N   . VAL D 202 ? 0.9460 0.8511 1.0777 0.0696  0.0557  0.0293  202 VAL D N   
22312 C CA  . VAL D 202 ? 0.9915 0.8737 1.0860 0.0828  0.0425  0.0231  202 VAL D CA  
22313 C C   . VAL D 202 ? 0.9982 0.8684 1.1024 0.0796  0.0158  0.0143  202 VAL D C   
22314 O O   . VAL D 202 ? 1.0463 0.9420 1.1959 0.0729  0.0083  0.0120  202 VAL D O   
22315 C CB  . VAL D 202 ? 0.9924 0.8953 1.0780 0.0921  0.0532  0.0235  202 VAL D CB  
22316 C CG1 . VAL D 202 ? 1.0156 0.8990 1.0640 0.1023  0.0463  0.0232  202 VAL D CG1 
22317 C CG2 . VAL D 202 ? 0.9670 0.8879 1.0444 0.0958  0.0718  0.0281  202 VAL D CG2 
22327 N N   . ALA D 203 ? 1.0197 0.8542 1.0795 0.0883  0.0004  0.0077  203 ALA D N   
22328 C CA  . ALA D 203 ? 0.9894 0.8085 1.0419 0.0891  -0.0312 -0.0028 203 ALA D CA  
22329 C C   . ALA D 203 ? 1.0010 0.7957 0.9852 0.1087  -0.0342 -0.0040 203 ALA D C   
22330 O O   . ALA D 203 ? 1.0207 0.7947 0.9628 0.1195  -0.0219 -0.0072 203 ALA D O   
22331 C CB  . ALA D 203 ? 1.0636 0.8568 1.1291 0.0748  -0.0532 -0.0155 203 ALA D CB  
22337 N N   . HIS D 204 ? 0.9958 0.7939 0.9684 0.1157  -0.0485 0.0004  204 HIS D N   
22338 C CA  . HIS D 204 ? 1.0743 0.8493 0.9751 0.1330  -0.0496 0.0048  204 HIS D CA  
22339 C C   . HIS D 204 ? 1.1720 0.9253 1.0439 0.1396  -0.0911 -0.0063 204 HIS D C   
22340 O O   . HIS D 204 ? 1.1697 0.9323 1.0581 0.1424  -0.1115 0.0021  204 HIS D O   
22341 C CB  . HIS D 204 ? 1.0546 0.8433 0.9548 0.1355  -0.0298 0.0264  204 HIS D CB  
22342 C CG  . HIS D 204 ? 1.0904 0.8622 0.9199 0.1484  -0.0159 0.0385  204 HIS D CG  
22343 N ND1 . HIS D 204 ? 1.1166 0.8743 0.9155 0.1538  -0.0206 0.0590  204 HIS D ND1 
22344 C CD2 . HIS D 204 ? 1.1184 0.8867 0.9017 0.1586  0.0056  0.0351  204 HIS D CD2 
22345 C CE1 . HIS D 204 ? 1.1661 0.9147 0.9008 0.1629  0.0010  0.0703  204 HIS D CE1 
22346 N NE2 . HIS D 204 ? 1.1713 0.9309 0.8983 0.1674  0.0180  0.0538  204 HIS D NE2 
22354 N N   . PRO D 205 ? 1.2468 0.9684 1.0739 0.1451  -0.1089 -0.0273 205 PRO D N   
22355 C CA  . PRO D 205 ? 1.3063 1.0103 1.1114 0.1488  -0.1577 -0.0442 205 PRO D CA  
22356 C C   . PRO D 205 ? 1.3928 1.0883 1.1329 0.1695  -0.1704 -0.0294 205 PRO D C   
22357 O O   . PRO D 205 ? 1.4080 1.1080 1.1571 0.1729  -0.2120 -0.0317 205 PRO D O   
22358 C CB  . PRO D 205 ? 1.3400 1.0008 1.0954 0.1534  -0.1683 -0.0732 205 PRO D CB  
22359 C CG  . PRO D 205 ? 1.3364 0.9913 1.0522 0.1678  -0.1218 -0.0644 205 PRO D CG  
22360 C CD  . PRO D 205 ? 1.2602 0.9573 1.0448 0.1543  -0.0883 -0.0387 205 PRO D CD  
22368 N N   . ALA D 206 ? 1.4863 1.1721 1.1632 0.1834  -0.1351 -0.0115 206 ALA D N   
22369 C CA  . ALA D 206 ? 1.6143 1.2852 1.2194 0.2013  -0.1409 0.0104  206 ALA D CA  
22370 C C   . ALA D 206 ? 1.6101 1.2949 1.2658 0.1978  -0.1569 0.0334  206 ALA D C   
22371 O O   . ALA D 206 ? 1.7031 1.3687 1.3074 0.2144  -0.1825 0.0490  206 ALA D O   
22372 C CB  . ALA D 206 ? 1.6323 1.3028 1.1855 0.2086  -0.0891 0.0319  206 ALA D CB  
22378 N N   . SER D 207 ? 1.5020 1.2171 1.2523 0.1807  -0.1430 0.0354  207 SER D N   
22379 C CA  . SER D 207 ? 1.4631 1.1900 1.2667 0.1819  -0.1534 0.0526  207 SER D CA  
22380 C C   . SER D 207 ? 1.4213 1.1822 1.3126 0.1756  -0.1852 0.0326  207 SER D C   
22381 O O   . SER D 207 ? 1.4151 1.1944 1.3651 0.1801  -0.1907 0.0410  207 SER D O   
22382 C CB  . SER D 207 ? 1.4151 1.1519 1.2555 0.1703  -0.1089 0.0693  207 SER D CB  
22383 O OG  . SER D 207 ? 1.4840 1.1983 1.2590 0.1722  -0.0792 0.0921  207 SER D OG  
22389 N N   . SER D 208 ? 1.3873 1.1571 1.2931 0.1653  -0.2052 0.0059  208 SER D N   
22390 C CA  . SER D 208 ? 1.3669 1.1790 1.3703 0.1511  -0.2268 -0.0111 208 SER D CA  
22391 C C   . SER D 208 ? 1.2930 1.1405 1.3736 0.1402  -0.1884 -0.0030 208 SER D C   
22392 O O   . SER D 208 ? 1.2781 1.1663 1.4367 0.1414  -0.1980 -0.0049 208 SER D O   
22393 C CB  . SER D 208 ? 1.4369 1.2650 1.4614 0.1669  -0.2801 -0.0136 208 SER D CB  
22394 O OG  . SER D 208 ? 1.5430 1.3389 1.4877 0.1778  -0.3210 -0.0253 208 SER D OG  
22400 N N   . THR D 209 ? 1.2429 1.0784 1.3000 0.1328  -0.1453 0.0041  209 THR D N   
22401 C CA  . THR D 209 ? 1.1663 1.0292 1.2758 0.1248  -0.1094 0.0095  209 THR D CA  
22402 C C   . THR D 209 ? 1.1119 0.9956 1.2611 0.1039  -0.0926 -0.0010 209 THR D C   
22403 O O   . THR D 209 ? 1.1186 0.9775 1.2335 0.0965  -0.0941 -0.0076 209 THR D O   
22404 C CB  . THR D 209 ? 1.1975 1.0387 1.2602 0.1287  -0.0769 0.0246  209 THR D CB  
22405 O OG1 . THR D 209 ? 1.2713 1.0841 1.2919 0.1441  -0.0893 0.0410  209 THR D OG1 
22406 C CG2 . THR D 209 ? 1.1233 0.9905 1.2350 0.1220  -0.0474 0.0246  209 THR D CG2 
22414 N N   . LYS D 210 ? 1.0964 1.0214 1.3137 0.0966  -0.0753 -0.0016 210 LYS D N   
22415 C CA  . LYS D 210 ? 1.1276 1.0713 1.3765 0.0766  -0.0517 -0.0032 210 LYS D CA  
22416 C C   . LYS D 210 ? 1.1312 1.1122 1.4180 0.0790  -0.0200 0.0001  210 LYS D C   
22417 O O   . LYS D 210 ? 1.1252 1.1474 1.4733 0.0831  -0.0223 -0.0050 210 LYS D O   
22418 C CB  . LYS D 210 ? 1.1489 1.1122 1.4529 0.0575  -0.0738 -0.0120 210 LYS D CB  
22419 C CG  . LYS D 210 ? 1.1968 1.1157 1.4648 0.0424  -0.0838 -0.0172 210 LYS D CG  
22420 C CD  . LYS D 210 ? 1.2360 1.1746 1.5735 0.0141  -0.1023 -0.0253 210 LYS D CD  
22421 C CE  . LYS D 210 ? 1.3168 1.1954 1.6162 -0.0005 -0.1182 -0.0349 210 LYS D CE  
22422 N NZ  . LYS D 210 ? 1.4083 1.2427 1.6349 0.0195  -0.1541 -0.0524 210 LYS D NZ  
22436 N N   . VAL D 211 ? 1.0933 1.0632 1.3439 0.0794  0.0078  0.0056  211 VAL D N   
22437 C CA  . VAL D 211 ? 1.0714 1.0704 1.3408 0.0832  0.0360  0.0040  211 VAL D CA  
22438 C C   . VAL D 211 ? 1.0566 1.0676 1.3235 0.0693  0.0609  0.0112  211 VAL D C   
22439 O O   . VAL D 211 ? 1.0427 1.0237 1.2734 0.0627  0.0598  0.0191  211 VAL D O   
22440 C CB  . VAL D 211 ? 1.1170 1.0949 1.3466 0.0946  0.0425  0.0034  211 VAL D CB  
22441 C CG1 . VAL D 211 ? 1.1269 1.1300 1.3675 0.0982  0.0670  -0.0051 211 VAL D CG1 
22442 C CG2 . VAL D 211 ? 1.1427 1.0997 1.3717 0.1073  0.0205  0.0034  211 VAL D CG2 
22452 N N   . ASP D 212 ? 1.1010 1.1535 1.4027 0.0681  0.0845  0.0096  212 ASP D N   
22453 C CA  . ASP D 212 ? 1.1042 1.1692 1.3937 0.0578  0.1133  0.0215  212 ASP D CA  
22454 C C   . ASP D 212 ? 1.0673 1.1542 1.3375 0.0733  0.1350  0.0119  212 ASP D C   
22455 O O   . ASP D 212 ? 1.0435 1.1711 1.3495 0.0803  0.1514  0.0019  212 ASP D O   
22456 C CB  . ASP D 212 ? 1.1465 1.2459 1.4942 0.0379  0.1255  0.0306  212 ASP D CB  
22457 C CG  . ASP D 212 ? 1.1571 1.2293 1.5246 0.0185  0.0982  0.0348  212 ASP D CG  
22458 O OD1 . ASP D 212 ? 1.1599 1.1784 1.4758 0.0191  0.0828  0.0378  212 ASP D OD1 
22459 O OD2 . ASP D 212 ? 1.1629 1.2702 1.6000 0.0039  0.0910  0.0322  212 ASP D OD2 
22464 N N   . LYS D 213 ? 1.0791 1.1423 1.2954 0.0803  0.1336  0.0115  213 LYS D N   
22465 C CA  . LYS D 213 ? 1.0927 1.1698 1.2856 0.0936  0.1447  -0.0038 213 LYS D CA  
22466 C C   . LYS D 213 ? 1.0350 1.1286 1.1914 0.0931  0.1678  0.0071  213 LYS D C   
22467 O O   . LYS D 213 ? 1.0051 1.0789 1.1216 0.0918  0.1632  0.0215  213 LYS D O   
22468 C CB  . LYS D 213 ? 1.1595 1.2093 1.3247 0.0982  0.1263  -0.0117 213 LYS D CB  
22469 C CG  . LYS D 213 ? 1.1480 1.1878 1.3348 0.1057  0.1151  -0.0303 213 LYS D CG  
22470 C CD  . LYS D 213 ? 1.1437 1.2041 1.3354 0.1179  0.1285  -0.0540 213 LYS D CD  
22471 C CE  . LYS D 213 ? 1.1334 1.1703 1.3490 0.1278  0.1153  -0.0725 213 LYS D CE  
22472 N NZ  . LYS D 213 ? 1.1417 1.1931 1.3616 0.1450  0.1280  -0.1022 213 LYS D NZ  
22486 N N   . LYS D 214 ? 1.0193 1.1499 1.1859 0.0981  0.1934  0.0012  214 LYS D N   
22487 C CA  . LYS D 214 ? 1.0539 1.2007 1.1721 0.1011  0.2180  0.0129  214 LYS D CA  
22488 C C   . LYS D 214 ? 1.0792 1.2212 1.1425 0.1176  0.2075  -0.0076 214 LYS D C   
22489 O O   . LYS D 214 ? 1.1078 1.2425 1.1825 0.1251  0.1903  -0.0359 214 LYS D O   
22490 C CB  . LYS D 214 ? 1.0858 1.2811 1.2287 0.1031  0.2544  0.0118  214 LYS D CB  
22491 C CG  . LYS D 214 ? 1.1413 1.3484 1.2627 0.0890  0.2857  0.0482  214 LYS D CG  
22492 C CD  . LYS D 214 ? 1.1867 1.4500 1.3052 0.0982  0.3300  0.0442  214 LYS D CD  
22493 C CE  . LYS D 214 ? 1.2346 1.5354 1.4196 0.0737  0.3618  0.0712  214 LYS D CE  
22494 N NZ  . LYS D 214 ? 1.3163 1.6720 1.4800 0.0795  0.4157  0.0813  214 LYS D NZ  
22508 N N   . ILE D 215 ? 1.1070 1.2508 1.1108 0.1222  0.2154  0.0080  215 ILE D N   
22509 C CA  . ILE D 215 ? 1.1757 1.3234 1.1243 0.1377  0.2014  -0.0115 215 ILE D CA  
22510 C C   . ILE D 215 ? 1.2933 1.4713 1.1920 0.1512  0.2301  -0.0160 215 ILE D C   
22511 O O   . ILE D 215 ? 1.3419 1.5263 1.2121 0.1480  0.2556  0.0181  215 ILE D O   
22512 C CB  . ILE D 215 ? 1.2201 1.3482 1.1338 0.1391  0.1801  0.0097  215 ILE D CB  
22513 C CG1 . ILE D 215 ? 1.1847 1.2882 1.1430 0.1293  0.1575  0.0109  215 ILE D CG1 
22514 C CG2 . ILE D 215 ? 1.2769 1.4209 1.1386 0.1551  0.1613  -0.0113 215 ILE D CG2 
22515 C CD1 . ILE D 215 ? 1.2262 1.3123 1.1614 0.1347  0.1425  0.0339  215 ILE D CD1 
22527 N N   . GLU D 216 ? 1.3787 1.5711 1.2618 0.1665  0.2271  -0.0577 216 GLU D N   
22528 C CA  . GLU D 216 ? 1.4908 1.7149 1.3225 0.1839  0.2588  -0.0683 216 GLU D CA  
22529 C C   . GLU D 216 ? 1.5799 1.8068 1.3240 0.2022  0.2411  -0.0888 216 GLU D C   
22530 O O   . GLU D 216 ? 1.6757 1.9182 1.3471 0.2126  0.2615  -0.0670 216 GLU D O   
22531 C CB  . GLU D 216 ? 1.4788 1.7208 1.3565 0.1948  0.2759  -0.1050 216 GLU D CB  
22532 C CG  . GLU D 216 ? 1.4713 1.7452 1.4073 0.1866  0.3149  -0.0800 216 GLU D CG  
22533 C CD  . GLU D 216 ? 1.4677 1.7470 1.4878 0.1918  0.3112  -0.1064 216 GLU D CD  
22534 O OE1 . GLU D 216 ? 1.4595 1.7003 1.5031 0.1907  0.2742  -0.1261 216 GLU D OE1 
22535 O OE2 . GLU D 216 ? 1.4963 1.8208 1.5614 0.1976  0.3459  -0.1048 216 GLU D OE2 
22542 N N   . PRO D 217 ? 1.5538 1.7663 1.2998 0.2053  0.2022  -0.1293 217 PRO D N   
22543 C CA  . PRO D 217 ? 1.5992 1.8216 1.2621 0.2226  0.1819  -0.1539 217 PRO D CA  
22544 C C   . PRO D 217 ? 1.6133 1.8322 1.2535 0.2187  0.1462  -0.1307 217 PRO D C   
22545 O O   . PRO D 217 ? 1.6513 1.8738 1.2793 0.2210  0.1061  -0.1628 217 PRO D O   
22546 C CB  . PRO D 217 ? 1.5900 1.7982 1.2764 0.2253  0.1575  -0.2149 217 PRO D CB  
22547 C CG  . PRO D 217 ? 1.5351 1.7171 1.3167 0.2026  0.1461  -0.2072 217 PRO D CG  
22548 C CD  . PRO D 217 ? 1.4947 1.6822 1.3114 0.1932  0.1759  -0.1557 217 PRO D CD  
# 
